data_5VRB
# 
_entry.id   5VRB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.280 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5VRB         
WWPDB D_1000227889 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          NegoA.01294.a 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        . 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5VRB 
_pdbx_database_status.recvd_initial_deposition_date   2017-05-10 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_audit_author.name               'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of a transketolase from Neisseria gonorrhoeae' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Edwards, T.E.'                                                      1 
primary 'Delker, S.L.'                                                       2 
primary 'Lorimer, D.D.'                                                      3 
primary 'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.110 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5VRB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.450 
_cell.length_a_esd                 ? 
_cell.length_b                     114.210 
_cell.length_b_esd                 ? 
_cell.length_c                     125.690 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5VRB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Transketolase  72731.000 4    2.2.1.1 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL 62.068    6    ?       ? ? ? 
3 non-polymer syn 'CALCIUM ION'  40.078    12   ?       ? ? ? 
4 water       nat water          18.015    2039 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MAHHHHHHMSQLANVIRFLSADAVQKANSGHPGAPMGMAEMAETLWTKFLNHNPANPKFYNRDRFVLSNGHASMLLYSLL
HLTGYNLSIEDLKNFRQLHSKTPGHPEYGYTDGVETTTGPLGQGIANAVGMALAEKILAAEFNKDGLNIVDHYTYVFMGD
G(OCS)LMEGVSHEACSLAGTLGLGKLIVLYDDNNISIDGKVDGWFTENIPQRFESYGWHVVPNVNGHDTAAIQTAIEAA
RAETGKPSIICCKTLIGKGSANKEGSHKTHGAPLGADEIEATRKHLGWAYPAFEIPQEIYDAWNAKEKGAKLEAGWNELF
AQYQAKYPAEAAEFVRRMDKKLPENFDEYVQTALKEVCAKAETVATRKASQNSIEILAKELPELVGGSADLTPSNLTDWS
NSVSVTRDKGGNYIHYGVREFGMGAIMNGLVLHGGVKPFGATFLMFSEYERNALRMAALMKINPVFVFTHDSIGLGEDGP
THQPIEQTATLRLIPNMDVWRPCDTAESLVAWAEAAKAEDHPSCLIFSRQNLKFQARSEQQLNDIKRGAYVISEAQGNAQ
AVIIATGSEVGLAVEAQKVLAGQGIAVRVVSMPSTSVFDRQDAAYQAAVLPEGLPRIAVEAGHTNGWYKYVGLNGAVVGI
NRFGESAPADLLFKAFGFTVDNVVDTVKSVL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHMSQLANVIRFLSADAVQKANSGHPGAPMGMAEMAETLWTKFLNHNPANPKFYNRDRFVLSNGHASMLLYSLL
HLTGYNLSIEDLKNFRQLHSKTPGHPEYGYTDGVETTTGPLGQGIANAVGMALAEKILAAEFNKDGLNIVDHYTYVFMGD
GCLMEGVSHEACSLAGTLGLGKLIVLYDDNNISIDGKVDGWFTENIPQRFESYGWHVVPNVNGHDTAAIQTAIEAARAET
GKPSIICCKTLIGKGSANKEGSHKTHGAPLGADEIEATRKHLGWAYPAFEIPQEIYDAWNAKEKGAKLEAGWNELFAQYQ
AKYPAEAAEFVRRMDKKLPENFDEYVQTALKEVCAKAETVATRKASQNSIEILAKELPELVGGSADLTPSNLTDWSNSVS
VTRDKGGNYIHYGVREFGMGAIMNGLVLHGGVKPFGATFLMFSEYERNALRMAALMKINPVFVFTHDSIGLGEDGPTHQP
IEQTATLRLIPNMDVWRPCDTAESLVAWAEAAKAEDHPSCLIFSRQNLKFQARSEQQLNDIKRGAYVISEAQGNAQAVII
ATGSEVGLAVEAQKVLAGQGIAVRVVSMPSTSVFDRQDAAYQAAVLPEGLPRIAVEAGHTNGWYKYVGLNGAVVGINRFG
ESAPADLLFKAFGFTVDNVVDTVKSVL
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         NegoA.01294.a 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   MET n 
1 10  SER n 
1 11  GLN n 
1 12  LEU n 
1 13  ALA n 
1 14  ASN n 
1 15  VAL n 
1 16  ILE n 
1 17  ARG n 
1 18  PHE n 
1 19  LEU n 
1 20  SER n 
1 21  ALA n 
1 22  ASP n 
1 23  ALA n 
1 24  VAL n 
1 25  GLN n 
1 26  LYS n 
1 27  ALA n 
1 28  ASN n 
1 29  SER n 
1 30  GLY n 
1 31  HIS n 
1 32  PRO n 
1 33  GLY n 
1 34  ALA n 
1 35  PRO n 
1 36  MET n 
1 37  GLY n 
1 38  MET n 
1 39  ALA n 
1 40  GLU n 
1 41  MET n 
1 42  ALA n 
1 43  GLU n 
1 44  THR n 
1 45  LEU n 
1 46  TRP n 
1 47  THR n 
1 48  LYS n 
1 49  PHE n 
1 50  LEU n 
1 51  ASN n 
1 52  HIS n 
1 53  ASN n 
1 54  PRO n 
1 55  ALA n 
1 56  ASN n 
1 57  PRO n 
1 58  LYS n 
1 59  PHE n 
1 60  TYR n 
1 61  ASN n 
1 62  ARG n 
1 63  ASP n 
1 64  ARG n 
1 65  PHE n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  ASN n 
1 70  GLY n 
1 71  HIS n 
1 72  ALA n 
1 73  SER n 
1 74  MET n 
1 75  LEU n 
1 76  LEU n 
1 77  TYR n 
1 78  SER n 
1 79  LEU n 
1 80  LEU n 
1 81  HIS n 
1 82  LEU n 
1 83  THR n 
1 84  GLY n 
1 85  TYR n 
1 86  ASN n 
1 87  LEU n 
1 88  SER n 
1 89  ILE n 
1 90  GLU n 
1 91  ASP n 
1 92  LEU n 
1 93  LYS n 
1 94  ASN n 
1 95  PHE n 
1 96  ARG n 
1 97  GLN n 
1 98  LEU n 
1 99  HIS n 
1 100 SER n 
1 101 LYS n 
1 102 THR n 
1 103 PRO n 
1 104 GLY n 
1 105 HIS n 
1 106 PRO n 
1 107 GLU n 
1 108 TYR n 
1 109 GLY n 
1 110 TYR n 
1 111 THR n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 GLU n 
1 116 THR n 
1 117 THR n 
1 118 THR n 
1 119 GLY n 
1 120 PRO n 
1 121 LEU n 
1 122 GLY n 
1 123 GLN n 
1 124 GLY n 
1 125 ILE n 
1 126 ALA n 
1 127 ASN n 
1 128 ALA n 
1 129 VAL n 
1 130 GLY n 
1 131 MET n 
1 132 ALA n 
1 133 LEU n 
1 134 ALA n 
1 135 GLU n 
1 136 LYS n 
1 137 ILE n 
1 138 LEU n 
1 139 ALA n 
1 140 ALA n 
1 141 GLU n 
1 142 PHE n 
1 143 ASN n 
1 144 LYS n 
1 145 ASP n 
1 146 GLY n 
1 147 LEU n 
1 148 ASN n 
1 149 ILE n 
1 150 VAL n 
1 151 ASP n 
1 152 HIS n 
1 153 TYR n 
1 154 THR n 
1 155 TYR n 
1 156 VAL n 
1 157 PHE n 
1 158 MET n 
1 159 GLY n 
1 160 ASP n 
1 161 GLY n 
1 162 OCS n 
1 163 LEU n 
1 164 MET n 
1 165 GLU n 
1 166 GLY n 
1 167 VAL n 
1 168 SER n 
1 169 HIS n 
1 170 GLU n 
1 171 ALA n 
1 172 CYS n 
1 173 SER n 
1 174 LEU n 
1 175 ALA n 
1 176 GLY n 
1 177 THR n 
1 178 LEU n 
1 179 GLY n 
1 180 LEU n 
1 181 GLY n 
1 182 LYS n 
1 183 LEU n 
1 184 ILE n 
1 185 VAL n 
1 186 LEU n 
1 187 TYR n 
1 188 ASP n 
1 189 ASP n 
1 190 ASN n 
1 191 ASN n 
1 192 ILE n 
1 193 SER n 
1 194 ILE n 
1 195 ASP n 
1 196 GLY n 
1 197 LYS n 
1 198 VAL n 
1 199 ASP n 
1 200 GLY n 
1 201 TRP n 
1 202 PHE n 
1 203 THR n 
1 204 GLU n 
1 205 ASN n 
1 206 ILE n 
1 207 PRO n 
1 208 GLN n 
1 209 ARG n 
1 210 PHE n 
1 211 GLU n 
1 212 SER n 
1 213 TYR n 
1 214 GLY n 
1 215 TRP n 
1 216 HIS n 
1 217 VAL n 
1 218 VAL n 
1 219 PRO n 
1 220 ASN n 
1 221 VAL n 
1 222 ASN n 
1 223 GLY n 
1 224 HIS n 
1 225 ASP n 
1 226 THR n 
1 227 ALA n 
1 228 ALA n 
1 229 ILE n 
1 230 GLN n 
1 231 THR n 
1 232 ALA n 
1 233 ILE n 
1 234 GLU n 
1 235 ALA n 
1 236 ALA n 
1 237 ARG n 
1 238 ALA n 
1 239 GLU n 
1 240 THR n 
1 241 GLY n 
1 242 LYS n 
1 243 PRO n 
1 244 SER n 
1 245 ILE n 
1 246 ILE n 
1 247 CYS n 
1 248 CYS n 
1 249 LYS n 
1 250 THR n 
1 251 LEU n 
1 252 ILE n 
1 253 GLY n 
1 254 LYS n 
1 255 GLY n 
1 256 SER n 
1 257 ALA n 
1 258 ASN n 
1 259 LYS n 
1 260 GLU n 
1 261 GLY n 
1 262 SER n 
1 263 HIS n 
1 264 LYS n 
1 265 THR n 
1 266 HIS n 
1 267 GLY n 
1 268 ALA n 
1 269 PRO n 
1 270 LEU n 
1 271 GLY n 
1 272 ALA n 
1 273 ASP n 
1 274 GLU n 
1 275 ILE n 
1 276 GLU n 
1 277 ALA n 
1 278 THR n 
1 279 ARG n 
1 280 LYS n 
1 281 HIS n 
1 282 LEU n 
1 283 GLY n 
1 284 TRP n 
1 285 ALA n 
1 286 TYR n 
1 287 PRO n 
1 288 ALA n 
1 289 PHE n 
1 290 GLU n 
1 291 ILE n 
1 292 PRO n 
1 293 GLN n 
1 294 GLU n 
1 295 ILE n 
1 296 TYR n 
1 297 ASP n 
1 298 ALA n 
1 299 TRP n 
1 300 ASN n 
1 301 ALA n 
1 302 LYS n 
1 303 GLU n 
1 304 LYS n 
1 305 GLY n 
1 306 ALA n 
1 307 LYS n 
1 308 LEU n 
1 309 GLU n 
1 310 ALA n 
1 311 GLY n 
1 312 TRP n 
1 313 ASN n 
1 314 GLU n 
1 315 LEU n 
1 316 PHE n 
1 317 ALA n 
1 318 GLN n 
1 319 TYR n 
1 320 GLN n 
1 321 ALA n 
1 322 LYS n 
1 323 TYR n 
1 324 PRO n 
1 325 ALA n 
1 326 GLU n 
1 327 ALA n 
1 328 ALA n 
1 329 GLU n 
1 330 PHE n 
1 331 VAL n 
1 332 ARG n 
1 333 ARG n 
1 334 MET n 
1 335 ASP n 
1 336 LYS n 
1 337 LYS n 
1 338 LEU n 
1 339 PRO n 
1 340 GLU n 
1 341 ASN n 
1 342 PHE n 
1 343 ASP n 
1 344 GLU n 
1 345 TYR n 
1 346 VAL n 
1 347 GLN n 
1 348 THR n 
1 349 ALA n 
1 350 LEU n 
1 351 LYS n 
1 352 GLU n 
1 353 VAL n 
1 354 CYS n 
1 355 ALA n 
1 356 LYS n 
1 357 ALA n 
1 358 GLU n 
1 359 THR n 
1 360 VAL n 
1 361 ALA n 
1 362 THR n 
1 363 ARG n 
1 364 LYS n 
1 365 ALA n 
1 366 SER n 
1 367 GLN n 
1 368 ASN n 
1 369 SER n 
1 370 ILE n 
1 371 GLU n 
1 372 ILE n 
1 373 LEU n 
1 374 ALA n 
1 375 LYS n 
1 376 GLU n 
1 377 LEU n 
1 378 PRO n 
1 379 GLU n 
1 380 LEU n 
1 381 VAL n 
1 382 GLY n 
1 383 GLY n 
1 384 SER n 
1 385 ALA n 
1 386 ASP n 
1 387 LEU n 
1 388 THR n 
1 389 PRO n 
1 390 SER n 
1 391 ASN n 
1 392 LEU n 
1 393 THR n 
1 394 ASP n 
1 395 TRP n 
1 396 SER n 
1 397 ASN n 
1 398 SER n 
1 399 VAL n 
1 400 SER n 
1 401 VAL n 
1 402 THR n 
1 403 ARG n 
1 404 ASP n 
1 405 LYS n 
1 406 GLY n 
1 407 GLY n 
1 408 ASN n 
1 409 TYR n 
1 410 ILE n 
1 411 HIS n 
1 412 TYR n 
1 413 GLY n 
1 414 VAL n 
1 415 ARG n 
1 416 GLU n 
1 417 PHE n 
1 418 GLY n 
1 419 MET n 
1 420 GLY n 
1 421 ALA n 
1 422 ILE n 
1 423 MET n 
1 424 ASN n 
1 425 GLY n 
1 426 LEU n 
1 427 VAL n 
1 428 LEU n 
1 429 HIS n 
1 430 GLY n 
1 431 GLY n 
1 432 VAL n 
1 433 LYS n 
1 434 PRO n 
1 435 PHE n 
1 436 GLY n 
1 437 ALA n 
1 438 THR n 
1 439 PHE n 
1 440 LEU n 
1 441 MET n 
1 442 PHE n 
1 443 SER n 
1 444 GLU n 
1 445 TYR n 
1 446 GLU n 
1 447 ARG n 
1 448 ASN n 
1 449 ALA n 
1 450 LEU n 
1 451 ARG n 
1 452 MET n 
1 453 ALA n 
1 454 ALA n 
1 455 LEU n 
1 456 MET n 
1 457 LYS n 
1 458 ILE n 
1 459 ASN n 
1 460 PRO n 
1 461 VAL n 
1 462 PHE n 
1 463 VAL n 
1 464 PHE n 
1 465 THR n 
1 466 HIS n 
1 467 ASP n 
1 468 SER n 
1 469 ILE n 
1 470 GLY n 
1 471 LEU n 
1 472 GLY n 
1 473 GLU n 
1 474 ASP n 
1 475 GLY n 
1 476 PRO n 
1 477 THR n 
1 478 HIS n 
1 479 GLN n 
1 480 PRO n 
1 481 ILE n 
1 482 GLU n 
1 483 GLN n 
1 484 THR n 
1 485 ALA n 
1 486 THR n 
1 487 LEU n 
1 488 ARG n 
1 489 LEU n 
1 490 ILE n 
1 491 PRO n 
1 492 ASN n 
1 493 MET n 
1 494 ASP n 
1 495 VAL n 
1 496 TRP n 
1 497 ARG n 
1 498 PRO n 
1 499 CYS n 
1 500 ASP n 
1 501 THR n 
1 502 ALA n 
1 503 GLU n 
1 504 SER n 
1 505 LEU n 
1 506 VAL n 
1 507 ALA n 
1 508 TRP n 
1 509 ALA n 
1 510 GLU n 
1 511 ALA n 
1 512 ALA n 
1 513 LYS n 
1 514 ALA n 
1 515 GLU n 
1 516 ASP n 
1 517 HIS n 
1 518 PRO n 
1 519 SER n 
1 520 CYS n 
1 521 LEU n 
1 522 ILE n 
1 523 PHE n 
1 524 SER n 
1 525 ARG n 
1 526 GLN n 
1 527 ASN n 
1 528 LEU n 
1 529 LYS n 
1 530 PHE n 
1 531 GLN n 
1 532 ALA n 
1 533 ARG n 
1 534 SER n 
1 535 GLU n 
1 536 GLN n 
1 537 GLN n 
1 538 LEU n 
1 539 ASN n 
1 540 ASP n 
1 541 ILE n 
1 542 LYS n 
1 543 ARG n 
1 544 GLY n 
1 545 ALA n 
1 546 TYR n 
1 547 VAL n 
1 548 ILE n 
1 549 SER n 
1 550 GLU n 
1 551 ALA n 
1 552 GLN n 
1 553 GLY n 
1 554 ASN n 
1 555 ALA n 
1 556 GLN n 
1 557 ALA n 
1 558 VAL n 
1 559 ILE n 
1 560 ILE n 
1 561 ALA n 
1 562 THR n 
1 563 GLY n 
1 564 SER n 
1 565 GLU n 
1 566 VAL n 
1 567 GLY n 
1 568 LEU n 
1 569 ALA n 
1 570 VAL n 
1 571 GLU n 
1 572 ALA n 
1 573 GLN n 
1 574 LYS n 
1 575 VAL n 
1 576 LEU n 
1 577 ALA n 
1 578 GLY n 
1 579 GLN n 
1 580 GLY n 
1 581 ILE n 
1 582 ALA n 
1 583 VAL n 
1 584 ARG n 
1 585 VAL n 
1 586 VAL n 
1 587 SER n 
1 588 MET n 
1 589 PRO n 
1 590 SER n 
1 591 THR n 
1 592 SER n 
1 593 VAL n 
1 594 PHE n 
1 595 ASP n 
1 596 ARG n 
1 597 GLN n 
1 598 ASP n 
1 599 ALA n 
1 600 ALA n 
1 601 TYR n 
1 602 GLN n 
1 603 ALA n 
1 604 ALA n 
1 605 VAL n 
1 606 LEU n 
1 607 PRO n 
1 608 GLU n 
1 609 GLY n 
1 610 LEU n 
1 611 PRO n 
1 612 ARG n 
1 613 ILE n 
1 614 ALA n 
1 615 VAL n 
1 616 GLU n 
1 617 ALA n 
1 618 GLY n 
1 619 HIS n 
1 620 THR n 
1 621 ASN n 
1 622 GLY n 
1 623 TRP n 
1 624 TYR n 
1 625 LYS n 
1 626 TYR n 
1 627 VAL n 
1 628 GLY n 
1 629 LEU n 
1 630 ASN n 
1 631 GLY n 
1 632 ALA n 
1 633 VAL n 
1 634 VAL n 
1 635 GLY n 
1 636 ILE n 
1 637 ASN n 
1 638 ARG n 
1 639 PHE n 
1 640 GLY n 
1 641 GLU n 
1 642 SER n 
1 643 ALA n 
1 644 PRO n 
1 645 ALA n 
1 646 ASP n 
1 647 LEU n 
1 648 LEU n 
1 649 PHE n 
1 650 LYS n 
1 651 ALA n 
1 652 PHE n 
1 653 GLY n 
1 654 PHE n 
1 655 THR n 
1 656 VAL n 
1 657 ASP n 
1 658 ASN n 
1 659 VAL n 
1 660 VAL n 
1 661 ASP n 
1 662 THR n 
1 663 VAL n 
1 664 LYS n 
1 665 SER n 
1 666 VAL n 
1 667 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   667 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NGK_0759 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    NCCP11945 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Neisseria gonorrhoeae (strain NCCP11945)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     521006 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    B4RKU9_NEIG2 
_struct_ref.pdbx_db_accession          B4RKU9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSQLANVIRFLSADAVQKANSGHPGAPMGMAEMAETLWTKFLNHNPANPKFYNRDRFVLSNGHASMLLYSLLHLTGYNLS
IEDLKNFRQLHSKTPGHPEYGYTDGVETTTGPLGQGIANAVGMALAEKILAAEFNKDGLNIVDHYTYVFMGDGCLMEGVS
HEACSLAGTLGLGKLIVLYDDNNISIDGKVDGWFTENIPQRFESYGWHVVPNVNGHDTAAIQTAIEAARAETGKPSIICC
KTLIGKGSANKEGSHKTHGAPLGADEIEATRKHLGWAYPAFEIPQEIYDAWNAKEKGAKLEAGWNELFAQYQAKYPAEAA
EFVRRMDKKLPENFDEYVQTALKEVCAKAETVATRKASQNSIEILAKELPELVGGSADLTPSNLTDWSNSVSVTRDKGGN
YIHYGVREFGMGAIMNGLVLHGGVKPFGATFLMFSEYERNALRMAALMKINPVFVFTHDSIGLGEDGPTHQPIEQTATLR
LIPNMDVWRPCDTAESLVAWAEAAKAEDHPSCLIFSRQNLKFQARSEQQLNDIKRGAYVISEAQGNAQAVIIATGSEVGL
AVEAQKVLAGQGIAVRVVSMPSTSVFDRQDAAYQAAVLPEGLPRIAVEAGHTNGWYKYVGLNGAVVGINRFGESAPADLL
FKAFGFTVDNVVDTVKSVL
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5VRB A 9 ? 667 ? B4RKU9 1 ? 659 ? 1 659 
2 1 5VRB B 9 ? 667 ? B4RKU9 1 ? 659 ? 1 659 
3 1 5VRB C 9 ? 667 ? B4RKU9 1 ? 659 ? 1 659 
4 1 5VRB D 9 ? 667 ? B4RKU9 1 ? 659 ? 1 659 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5VRB MET A 1 ? UNP B4RKU9 ? ? 'initiating methionine' -7 1  
1 5VRB ALA A 2 ? UNP B4RKU9 ? ? 'expression tag'        -6 2  
1 5VRB HIS A 3 ? UNP B4RKU9 ? ? 'expression tag'        -5 3  
1 5VRB HIS A 4 ? UNP B4RKU9 ? ? 'expression tag'        -4 4  
1 5VRB HIS A 5 ? UNP B4RKU9 ? ? 'expression tag'        -3 5  
1 5VRB HIS A 6 ? UNP B4RKU9 ? ? 'expression tag'        -2 6  
1 5VRB HIS A 7 ? UNP B4RKU9 ? ? 'expression tag'        -1 7  
1 5VRB HIS A 8 ? UNP B4RKU9 ? ? 'expression tag'        0  8  
2 5VRB MET B 1 ? UNP B4RKU9 ? ? 'initiating methionine' -7 9  
2 5VRB ALA B 2 ? UNP B4RKU9 ? ? 'expression tag'        -6 10 
2 5VRB HIS B 3 ? UNP B4RKU9 ? ? 'expression tag'        -5 11 
2 5VRB HIS B 4 ? UNP B4RKU9 ? ? 'expression tag'        -4 12 
2 5VRB HIS B 5 ? UNP B4RKU9 ? ? 'expression tag'        -3 13 
2 5VRB HIS B 6 ? UNP B4RKU9 ? ? 'expression tag'        -2 14 
2 5VRB HIS B 7 ? UNP B4RKU9 ? ? 'expression tag'        -1 15 
2 5VRB HIS B 8 ? UNP B4RKU9 ? ? 'expression tag'        0  16 
3 5VRB MET C 1 ? UNP B4RKU9 ? ? 'initiating methionine' -7 17 
3 5VRB ALA C 2 ? UNP B4RKU9 ? ? 'expression tag'        -6 18 
3 5VRB HIS C 3 ? UNP B4RKU9 ? ? 'expression tag'        -5 19 
3 5VRB HIS C 4 ? UNP B4RKU9 ? ? 'expression tag'        -4 20 
3 5VRB HIS C 5 ? UNP B4RKU9 ? ? 'expression tag'        -3 21 
3 5VRB HIS C 6 ? UNP B4RKU9 ? ? 'expression tag'        -2 22 
3 5VRB HIS C 7 ? UNP B4RKU9 ? ? 'expression tag'        -1 23 
3 5VRB HIS C 8 ? UNP B4RKU9 ? ? 'expression tag'        0  24 
4 5VRB MET D 1 ? UNP B4RKU9 ? ? 'initiating methionine' -7 25 
4 5VRB ALA D 2 ? UNP B4RKU9 ? ? 'expression tag'        -6 26 
4 5VRB HIS D 3 ? UNP B4RKU9 ? ? 'expression tag'        -5 27 
4 5VRB HIS D 4 ? UNP B4RKU9 ? ? 'expression tag'        -4 28 
4 5VRB HIS D 5 ? UNP B4RKU9 ? ? 'expression tag'        -3 29 
4 5VRB HIS D 6 ? UNP B4RKU9 ? ? 'expression tag'        -2 30 
4 5VRB HIS D 7 ? UNP B4RKU9 ? ? 'expression tag'        -1 31 
4 5VRB HIS D 8 ? UNP B4RKU9 ? ? 'expression tag'        0  32 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ?                 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'           ?                 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE                ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE               ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                 'C5 H11 N O2 S'  149.211 
OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ?                 'C3 H7 N O5 S'   169.156 
PHE 'L-peptide linking' y PHENYLALANINE           ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5VRB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.57 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            289 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;NegoA.01294.a.B1.PS37968 at 22.9 mg/mL against MCSG1 screen condition E9 0.2 M calcium chloride, 25% PEG 3350, cryo-protected with 15% ethylene glycol, 1 mM TPP, 2 mM CaCl2, crystal tracking ID 282795e9, unique puck ID pap7-3
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-05-03 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate            18.410 
_reflns.entry_id                         5VRB 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.850 
_reflns.d_resolution_low                 37.591 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       195499 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       -3.000 
_reflns.percent_possible_obs             98.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.152 
_reflns.pdbx_Rmerge_I_obs                0.071 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            12.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 1.026 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.086 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.996 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.850 1.900  ? 2.830  ? ? ? ? 14301 98.100 ? ? ? ? 0.455 ? ? ? ? ? ? ? ? 2.935 ? ? ? ? 0.557 ? ? 1  1 0.744 ? 
1.900 1.950  ? 3.720  ? ? ? ? 13995 98.200 ? ? ? ? 0.375 ? ? ? ? ? ? ? ? 3.210 ? ? ? ? 0.451 ? ? 2  1 0.828 ? 
1.950 2.010  ? 4.770  ? ? ? ? 13660 98.400 ? ? ? ? 0.287 ? ? ? ? ? ? ? ? 3.209 ? ? ? ? 0.345 ? ? 3  1 0.891 ? 
2.010 2.070  ? 5.870  ? ? ? ? 13249 98.600 ? ? ? ? 0.230 ? ? ? ? ? ? ? ? 3.201 ? ? ? ? 0.277 ? ? 4  1 0.928 ? 
2.070 2.140  ? 7.200  ? ? ? ? 12833 98.600 ? ? ? ? 0.182 ? ? ? ? ? ? ? ? 3.197 ? ? ? ? 0.219 ? ? 5  1 0.953 ? 
2.140 2.210  ? 8.450  ? ? ? ? 12464 98.700 ? ? ? ? 0.152 ? ? ? ? ? ? ? ? 3.197 ? ? ? ? 0.183 ? ? 6  1 0.966 ? 
2.210 2.290  ? 9.660  ? ? ? ? 12042 98.800 ? ? ? ? 0.130 ? ? ? ? ? ? ? ? 3.196 ? ? ? ? 0.157 ? ? 7  1 0.972 ? 
2.290 2.390  ? 10.940 ? ? ? ? 11623 98.900 ? ? ? ? 0.111 ? ? ? ? ? ? ? ? 3.191 ? ? ? ? 0.133 ? ? 8  1 0.980 ? 
2.390 2.490  ? 12.340 ? ? ? ? 11100 99.000 ? ? ? ? 0.096 ? ? ? ? ? ? ? ? 3.193 ? ? ? ? 0.115 ? ? 9  1 0.984 ? 
2.490 2.620  ? 13.510 ? ? ? ? 10651 99.100 ? ? ? ? 0.086 ? ? ? ? ? ? ? ? 3.185 ? ? ? ? 0.103 ? ? 10 1 0.987 ? 
2.620 2.760  ? 15.230 ? ? ? ? 10154 99.100 ? ? ? ? 0.075 ? ? ? ? ? ? ? ? 3.176 ? ? ? ? 0.090 ? ? 11 1 0.989 ? 
2.760 2.930  ? 17.550 ? ? ? ? 9615  99.100 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 3.166 ? ? ? ? 0.077 ? ? 12 1 0.992 ? 
2.930 3.130  ? 19.550 ? ? ? ? 9014  99.100 ? ? ? ? 0.055 ? ? ? ? ? ? ? ? 3.139 ? ? ? ? 0.067 ? ? 13 1 0.993 ? 
3.130 3.380  ? 22.230 ? ? ? ? 8398  99.000 ? ? ? ? 0.047 ? ? ? ? ? ? ? ? 3.127 ? ? ? ? 0.057 ? ? 14 1 0.995 ? 
3.380 3.700  ? 24.820 ? ? ? ? 7771  98.900 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 3.097 ? ? ? ? 0.049 ? ? 15 1 0.996 ? 
3.700 4.140  ? 26.640 ? ? ? ? 6948  98.600 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 3.045 ? ? ? ? 0.046 ? ? 16 1 0.996 ? 
4.140 4.780  ? 28.170 ? ? ? ? 6144  98.400 ? ? ? ? 0.036 ? ? ? ? ? ? ? ? 3.097 ? ? ? ? 0.043 ? ? 17 1 0.996 ? 
4.780 5.850  ? 27.730 ? ? ? ? 5213  98.200 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 3.092 ? ? ? ? 0.043 ? ? 18 1 0.996 ? 
5.850 8.270  ? 28.140 ? ? ? ? 4095  99.000 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 3.116 ? ? ? ? 0.042 ? ? 19 1 0.996 ? 
8.270 37.591 ? 30.270 ? ? ? ? 2229  96.900 ? ? ? ? 0.031 ? ? ? ? ? ? ? ? 3.056 ? ? ? ? 0.038 ? ? 20 1 0.997 ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                77.720 
_refine.B_iso_mean                               22.4160 
_refine.B_iso_min                                6.920 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5VRB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.8500 
_refine.ls_d_res_low                             37.5910 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     195491 
_refine.ls_number_reflns_R_free                  1970 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6900 
_refine.ls_percent_reflns_R_free                 1.0100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1509 
_refine.ls_R_factor_R_free                       0.1907 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1505 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2r8o 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.2900 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1900 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8500 
_refine_hist.d_res_low                        37.5910 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             2060 
_refine_hist.number_atoms_total               21113 
_refine_hist.pdbx_number_residues_total       2528 
_refine_hist.pdbx_B_iso_mean_ligand           28.49 
_refine_hist.pdbx_B_iso_mean_solvent          29.94 
_refine_hist.pdbx_number_atoms_protein        19017 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 19673 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.769  ? 26806 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 2988  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 3513  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 11.484 ? 11631 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.8500 1.8963  13726 . 128 13598 98.0000 . . . 0.2541 0.0000 0.2189 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 1.8963 1.9475  13900 . 131 13769 98.0000 . . . 0.2398 0.0000 0.1877 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 1.9475 2.0048  13923 . 119 13804 98.0000 . . . 0.2063 0.0000 0.1729 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.0048 2.0695  13887 . 160 13727 99.0000 . . . 0.2154 0.0000 0.1643 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.0695 2.1435  13885 . 166 13719 99.0000 . . . 0.1937 0.0000 0.1564 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.1435 2.2293  13943 . 160 13783 99.0000 . . . 0.1991 0.0000 0.1529 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.2293 2.3308  13995 . 151 13844 99.0000 . . . 0.1999 0.0000 0.1420 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.3308 2.4536  13919 . 166 13753 99.0000 . . . 0.1848 0.0000 0.1417 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.4536 2.6073  14045 . 146 13899 99.0000 . . . 0.1880 0.0000 0.1460 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.6073 2.8086  13988 . 133 13855 99.0000 . . . 0.1881 0.0000 0.1450 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 2.8086 3.0911  14073 . 156 13917 99.0000 . . . 0.2065 0.0000 0.1510 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 3.0911 3.5381  14025 . 116 13909 99.0000 . . . 0.1675 0.0000 0.1461 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 3.5381 4.4565  13994 . 131 13863 99.0000 . . . 0.1678 0.0000 0.1320 . . . . . . 14 . . . 
'X-RAY DIFFRACTION' 4.4565 37.5988 14188 . 107 14081 98.0000 . . . 0.1787 0.0000 0.1517 . . . . . . 14 . . . 
# 
_struct.entry_id                     5VRB 
_struct.title                        'Crystal structure of a transketolase from Neisseria gonorrhoeae' 
_struct.pdbx_descriptor              'Transketolase (E.C.2.2.1.1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5VRB 
_struct_keywords.text            
;transketolase, TPP, thiamine, thiamine pyrophosphate, calcium-dependent, NIAID, structural genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 2 ? 
M N N 2 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 2 ? 
T N N 3 ? 
U N N 3 ? 
V N N 3 ? 
W N N 4 ? 
X N N 4 ? 
Y N N 4 ? 
Z N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 SER A 10  ? ASN A 28  ? SER A 2   ASN A 20  1 ? 19 
HELX_P HELX_P2   AA2 PRO A 32  ? MET A 38  ? PRO A 24  MET A 30  1 ? 7  
HELX_P HELX_P3   AA3 MET A 38  ? PHE A 49  ? MET A 30  PHE A 41  1 ? 12 
HELX_P HELX_P4   AA4 ASN A 69  ? HIS A 71  ? ASN A 61  HIS A 63  5 ? 3  
HELX_P HELX_P5   AA5 ALA A 72  ? GLY A 84  ? ALA A 64  GLY A 76  1 ? 13 
HELX_P HELX_P6   AA6 SER A 88  ? LYS A 93  ? SER A 80  LYS A 85  1 ? 6  
HELX_P HELX_P7   AA7 GLY A 122 ? ASN A 143 ? GLY A 114 ASN A 135 1 ? 22 
HELX_P HELX_P8   AA8 GLY A 159 ? GLU A 165 ? GLY A 151 GLU A 157 1 ? 7  
HELX_P HELX_P9   AA9 GLU A 165 ? LEU A 178 ? GLU A 157 LEU A 170 1 ? 14 
HELX_P HELX_P10  AB1 ASN A 205 ? TYR A 213 ? ASN A 197 TYR A 205 1 ? 9  
HELX_P HELX_P11  AB2 ASP A 225 ? GLU A 239 ? ASP A 217 GLU A 231 1 ? 15 
HELX_P HELX_P12  AB3 ALA A 277 ? LEU A 282 ? ALA A 269 LEU A 274 1 ? 6  
HELX_P HELX_P13  AB4 PRO A 292 ? ASN A 300 ? PRO A 284 ASN A 292 1 ? 9  
HELX_P HELX_P14  AB5 ALA A 301 ? TYR A 323 ? ALA A 293 TYR A 315 1 ? 23 
HELX_P HELX_P15  AB6 TYR A 323 ? ASP A 335 ? TYR A 315 ASP A 327 1 ? 13 
HELX_P HELX_P16  AB7 ASN A 341 ? ALA A 357 ? ASN A 333 ALA A 349 1 ? 17 
HELX_P HELX_P17  AB8 THR A 362 ? LEU A 377 ? THR A 354 LEU A 369 1 ? 16 
HELX_P HELX_P18  AB9 LEU A 387 ? LEU A 392 ? LEU A 379 LEU A 384 1 ? 6  
HELX_P HELX_P19  AC1 ARG A 415 ? GLY A 430 ? ARG A 407 GLY A 422 1 ? 16 
HELX_P HELX_P20  AC2 MET A 441 ? TYR A 445 ? MET A 433 TYR A 437 5 ? 5  
HELX_P HELX_P21  AC3 GLU A 446 ? LYS A 457 ? GLU A 438 LYS A 449 1 ? 12 
HELX_P HELX_P22  AC4 SER A 468 ? GLY A 472 ? SER A 460 GLY A 464 5 ? 5  
HELX_P HELX_P23  AC5 GLU A 482 ? ARG A 488 ? GLU A 474 ARG A 480 1 ? 7  
HELX_P HELX_P24  AC6 ASP A 500 ? ALA A 514 ? ASP A 492 ALA A 506 1 ? 15 
HELX_P HELX_P25  AC7 SER A 534 ? ILE A 541 ? SER A 526 ILE A 533 1 ? 8  
HELX_P HELX_P26  AC8 LYS A 542 ? GLY A 544 ? LYS A 534 GLY A 536 5 ? 3  
HELX_P HELX_P27  AC9 GLU A 565 ? GLN A 579 ? GLU A 557 GLN A 571 1 ? 15 
HELX_P HELX_P28  AD1 SER A 590 ? ARG A 596 ? SER A 582 ARG A 588 1 ? 7  
HELX_P HELX_P29  AD2 ASP A 598 ? LEU A 606 ? ASP A 590 LEU A 598 1 ? 9  
HELX_P HELX_P30  AD3 THR A 620 ? GLY A 622 ? THR A 612 GLY A 614 5 ? 3  
HELX_P HELX_P31  AD4 TRP A 623 ? GLY A 628 ? TRP A 615 GLY A 620 1 ? 6  
HELX_P HELX_P32  AD5 PRO A 644 ? PHE A 652 ? PRO A 636 PHE A 644 1 ? 9  
HELX_P HELX_P33  AD6 THR A 655 ? VAL A 666 ? THR A 647 VAL A 658 1 ? 12 
HELX_P HELX_P34  AD7 GLN B 11  ? ASN B 28  ? GLN B 3   ASN B 20  1 ? 18 
HELX_P HELX_P35  AD8 PRO B 32  ? MET B 38  ? PRO B 24  MET B 30  1 ? 7  
HELX_P HELX_P36  AD9 MET B 38  ? PHE B 49  ? MET B 30  PHE B 41  1 ? 12 
HELX_P HELX_P37  AE1 ASN B 69  ? HIS B 71  ? ASN B 61  HIS B 63  5 ? 3  
HELX_P HELX_P38  AE2 ALA B 72  ? GLY B 84  ? ALA B 64  GLY B 76  1 ? 13 
HELX_P HELX_P39  AE3 SER B 88  ? LYS B 93  ? SER B 80  LYS B 85  1 ? 6  
HELX_P HELX_P40  AE4 GLY B 122 ? ASN B 143 ? GLY B 114 ASN B 135 1 ? 22 
HELX_P HELX_P41  AE5 ASP B 160 ? GLU B 165 ? ASP B 152 GLU B 157 1 ? 6  
HELX_P HELX_P42  AE6 GLU B 165 ? LEU B 178 ? GLU B 157 LEU B 170 1 ? 14 
HELX_P HELX_P43  AE7 ASP B 199 ? TRP B 201 ? ASP B 191 TRP B 193 5 ? 3  
HELX_P HELX_P44  AE8 ASN B 205 ? TYR B 213 ? ASN B 197 TYR B 205 1 ? 9  
HELX_P HELX_P45  AE9 ASP B 225 ? GLU B 239 ? ASP B 217 GLU B 231 1 ? 15 
HELX_P HELX_P46  AF1 SER B 262 ? HIS B 266 ? SER B 254 HIS B 258 5 ? 5  
HELX_P HELX_P47  AF2 GLY B 271 ? GLY B 283 ? GLY B 263 GLY B 275 1 ? 13 
HELX_P HELX_P48  AF3 PRO B 292 ? ASN B 300 ? PRO B 284 ASN B 292 1 ? 9  
HELX_P HELX_P49  AF4 ALA B 301 ? TYR B 323 ? ALA B 293 TYR B 315 1 ? 23 
HELX_P HELX_P50  AF5 TYR B 323 ? ASP B 335 ? TYR B 315 ASP B 327 1 ? 13 
HELX_P HELX_P51  AF6 ASN B 341 ? LYS B 356 ? ASN B 333 LYS B 348 1 ? 16 
HELX_P HELX_P52  AF7 ASN B 368 ? LEU B 377 ? ASN B 360 LEU B 369 1 ? 10 
HELX_P HELX_P53  AF8 ARG B 415 ? GLY B 430 ? ARG B 407 GLY B 422 1 ? 16 
HELX_P HELX_P54  AF9 MET B 441 ? TYR B 445 ? MET B 433 TYR B 437 5 ? 5  
HELX_P HELX_P55  AG1 GLU B 446 ? LYS B 457 ? GLU B 438 LYS B 449 1 ? 12 
HELX_P HELX_P56  AG2 SER B 468 ? GLY B 472 ? SER B 460 GLY B 464 5 ? 5  
HELX_P HELX_P57  AG3 GLU B 482 ? ARG B 488 ? GLU B 474 ARG B 480 1 ? 7  
HELX_P HELX_P58  AG4 ASP B 500 ? ALA B 514 ? ASP B 492 ALA B 506 1 ? 15 
HELX_P HELX_P59  AG5 SER B 534 ? ILE B 541 ? SER B 526 ILE B 533 1 ? 8  
HELX_P HELX_P60  AG6 LYS B 542 ? GLY B 544 ? LYS B 534 GLY B 536 5 ? 3  
HELX_P HELX_P61  AG7 GLU B 565 ? GLN B 579 ? GLU B 557 GLN B 571 1 ? 15 
HELX_P HELX_P62  AG8 SER B 590 ? ASP B 595 ? SER B 582 ASP B 587 1 ? 6  
HELX_P HELX_P63  AG9 ASP B 598 ? LEU B 606 ? ASP B 590 LEU B 598 1 ? 9  
HELX_P HELX_P64  AH1 THR B 620 ? GLY B 622 ? THR B 612 GLY B 614 5 ? 3  
HELX_P HELX_P65  AH2 TRP B 623 ? GLY B 628 ? TRP B 615 GLY B 620 1 ? 6  
HELX_P HELX_P66  AH3 PRO B 644 ? PHE B 652 ? PRO B 636 PHE B 644 1 ? 9  
HELX_P HELX_P67  AH4 THR B 655 ? VAL B 666 ? THR B 647 VAL B 658 1 ? 12 
HELX_P HELX_P68  AH5 GLN C 11  ? ASN C 28  ? GLN C 3   ASN C 20  1 ? 18 
HELX_P HELX_P69  AH6 PRO C 32  ? MET C 38  ? PRO C 24  MET C 30  1 ? 7  
HELX_P HELX_P70  AH7 MET C 38  ? PHE C 49  ? MET C 30  PHE C 41  1 ? 12 
HELX_P HELX_P71  AH8 ASN C 69  ? HIS C 71  ? ASN C 61  HIS C 63  5 ? 3  
HELX_P HELX_P72  AH9 ALA C 72  ? GLY C 84  ? ALA C 64  GLY C 76  1 ? 13 
HELX_P HELX_P73  AI1 SER C 88  ? ASN C 94  ? SER C 80  ASN C 86  1 ? 7  
HELX_P HELX_P74  AI2 GLY C 122 ? ASN C 143 ? GLY C 114 ASN C 135 1 ? 22 
HELX_P HELX_P75  AI3 GLY C 159 ? GLU C 165 ? GLY C 151 GLU C 157 1 ? 7  
HELX_P HELX_P76  AI4 GLU C 165 ? LEU C 178 ? GLU C 157 LEU C 170 1 ? 14 
HELX_P HELX_P77  AI5 ASN C 205 ? TYR C 213 ? ASN C 197 TYR C 205 1 ? 9  
HELX_P HELX_P78  AI6 ASP C 225 ? GLU C 239 ? ASP C 217 GLU C 231 1 ? 15 
HELX_P HELX_P79  AI7 GLU C 276 ? LEU C 282 ? GLU C 268 LEU C 274 1 ? 7  
HELX_P HELX_P80  AI8 PRO C 292 ? ASN C 300 ? PRO C 284 ASN C 292 1 ? 9  
HELX_P HELX_P81  AI9 ALA C 301 ? TYR C 323 ? ALA C 293 TYR C 315 1 ? 23 
HELX_P HELX_P82  AJ1 TYR C 323 ? ASP C 335 ? TYR C 315 ASP C 327 1 ? 13 
HELX_P HELX_P83  AJ2 ASN C 341 ? LYS C 356 ? ASN C 333 LYS C 348 1 ? 16 
HELX_P HELX_P84  AJ3 SER C 369 ? LEU C 377 ? SER C 361 LEU C 369 1 ? 9  
HELX_P HELX_P85  AJ4 ARG C 415 ? GLY C 430 ? ARG C 407 GLY C 422 1 ? 16 
HELX_P HELX_P86  AJ5 MET C 441 ? TYR C 445 ? MET C 433 TYR C 437 5 ? 5  
HELX_P HELX_P87  AJ6 GLU C 446 ? LYS C 457 ? GLU C 438 LYS C 449 1 ? 12 
HELX_P HELX_P88  AJ7 SER C 468 ? GLY C 472 ? SER C 460 GLY C 464 5 ? 5  
HELX_P HELX_P89  AJ8 GLU C 482 ? ARG C 488 ? GLU C 474 ARG C 480 1 ? 7  
HELX_P HELX_P90  AJ9 ASP C 500 ? ALA C 514 ? ASP C 492 ALA C 506 1 ? 15 
HELX_P HELX_P91  AK1 SER C 534 ? ILE C 541 ? SER C 526 ILE C 533 1 ? 8  
HELX_P HELX_P92  AK2 LYS C 542 ? GLY C 544 ? LYS C 534 GLY C 536 5 ? 3  
HELX_P HELX_P93  AK3 GLU C 565 ? GLN C 579 ? GLU C 557 GLN C 571 1 ? 15 
HELX_P HELX_P94  AK4 SER C 590 ? ASP C 595 ? SER C 582 ASP C 587 1 ? 6  
HELX_P HELX_P95  AK5 ASP C 598 ? LEU C 606 ? ASP C 590 LEU C 598 1 ? 9  
HELX_P HELX_P96  AK6 THR C 620 ? GLY C 622 ? THR C 612 GLY C 614 5 ? 3  
HELX_P HELX_P97  AK7 TRP C 623 ? GLY C 628 ? TRP C 615 GLY C 620 1 ? 6  
HELX_P HELX_P98  AK8 PRO C 644 ? PHE C 652 ? PRO C 636 PHE C 644 1 ? 9  
HELX_P HELX_P99  AK9 THR C 655 ? SER C 665 ? THR C 647 SER C 657 1 ? 11 
HELX_P HELX_P100 AL1 SER D 10  ? ASN D 28  ? SER D 2   ASN D 20  1 ? 19 
HELX_P HELX_P101 AL2 PRO D 32  ? MET D 38  ? PRO D 24  MET D 30  1 ? 7  
HELX_P HELX_P102 AL3 MET D 38  ? PHE D 49  ? MET D 30  PHE D 41  1 ? 12 
HELX_P HELX_P103 AL4 ASN D 69  ? HIS D 71  ? ASN D 61  HIS D 63  5 ? 3  
HELX_P HELX_P104 AL5 ALA D 72  ? GLY D 84  ? ALA D 64  GLY D 76  1 ? 13 
HELX_P HELX_P105 AL6 SER D 88  ? LYS D 93  ? SER D 80  LYS D 85  1 ? 6  
HELX_P HELX_P106 AL7 GLY D 122 ? ASN D 143 ? GLY D 114 ASN D 135 1 ? 22 
HELX_P HELX_P107 AL8 GLY D 159 ? GLU D 165 ? GLY D 151 GLU D 157 1 ? 7  
HELX_P HELX_P108 AL9 GLU D 165 ? LEU D 178 ? GLU D 157 LEU D 170 1 ? 14 
HELX_P HELX_P109 AM1 ASN D 205 ? TYR D 213 ? ASN D 197 TYR D 205 1 ? 9  
HELX_P HELX_P110 AM2 ASP D 225 ? GLU D 239 ? ASP D 217 GLU D 231 1 ? 15 
HELX_P HELX_P111 AM3 SER D 262 ? HIS D 266 ? SER D 254 HIS D 258 5 ? 5  
HELX_P HELX_P112 AM4 GLY D 271 ? LEU D 282 ? GLY D 263 LEU D 274 1 ? 12 
HELX_P HELX_P113 AM5 PRO D 292 ? ASN D 300 ? PRO D 284 ASN D 292 1 ? 9  
HELX_P HELX_P114 AM6 ALA D 301 ? TYR D 323 ? ALA D 293 TYR D 315 1 ? 23 
HELX_P HELX_P115 AM7 TYR D 323 ? ASP D 335 ? TYR D 315 ASP D 327 1 ? 13 
HELX_P HELX_P116 AM8 ASN D 341 ? LYS D 356 ? ASN D 333 LYS D 348 1 ? 16 
HELX_P HELX_P117 AM9 SER D 369 ? LEU D 377 ? SER D 361 LEU D 369 1 ? 9  
HELX_P HELX_P118 AN1 ARG D 415 ? GLY D 430 ? ARG D 407 GLY D 422 1 ? 16 
HELX_P HELX_P119 AN2 MET D 441 ? TYR D 445 ? MET D 433 TYR D 437 5 ? 5  
HELX_P HELX_P120 AN3 GLU D 446 ? LYS D 457 ? GLU D 438 LYS D 449 1 ? 12 
HELX_P HELX_P121 AN4 SER D 468 ? GLY D 472 ? SER D 460 GLY D 464 5 ? 5  
HELX_P HELX_P122 AN5 GLU D 482 ? ARG D 488 ? GLU D 474 ARG D 480 1 ? 7  
HELX_P HELX_P123 AN6 ASP D 500 ? ALA D 514 ? ASP D 492 ALA D 506 1 ? 15 
HELX_P HELX_P124 AN7 SER D 534 ? ILE D 541 ? SER D 526 ILE D 533 1 ? 8  
HELX_P HELX_P125 AN8 LYS D 542 ? GLY D 544 ? LYS D 534 GLY D 536 5 ? 3  
HELX_P HELX_P126 AN9 GLU D 565 ? GLN D 579 ? GLU D 557 GLN D 571 1 ? 15 
HELX_P HELX_P127 AO1 SER D 590 ? ARG D 596 ? SER D 582 ARG D 588 1 ? 7  
HELX_P HELX_P128 AO2 ASP D 598 ? LEU D 606 ? ASP D 590 LEU D 598 1 ? 9  
HELX_P HELX_P129 AO3 THR D 620 ? GLY D 622 ? THR D 612 GLY D 614 5 ? 3  
HELX_P HELX_P130 AO4 TRP D 623 ? GLY D 628 ? TRP D 615 GLY D 620 1 ? 6  
HELX_P HELX_P131 AO5 PRO D 644 ? PHE D 652 ? PRO D 636 PHE D 644 1 ? 9  
HELX_P HELX_P132 AO6 THR D 655 ? VAL D 666 ? THR D 647 VAL D 658 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1  metalc ?    ? A ASP 160 OD2 ? ? ? 1_555 G CA  .   CA ? ? A ASP 152 A CA  703  1_555 ? ? ? ? ? ? ? 2.395 ? 
covale1  covale both ? A GLY 161 C   ? ? ? 1_555 A OCS 162 N  ? ? A GLY 153 A OCS 154  1_555 ? ? ? ? ? ? ? 1.327 ? 
covale2  covale both ? A OCS 162 C   ? ? ? 1_555 A LEU 163 N  ? ? A OCS 154 A LEU 155  1_555 ? ? ? ? ? ? ? 1.326 ? 
metalc2  metalc ?    ? A OCS 162 OD3 ? ? ? 1_555 H CA  .   CA ? ? A OCS 154 A CA  704  1_555 ? ? ? ? ? ? ? 2.856 ? 
metalc3  metalc ?    ? A ASN 190 OD1 ? ? ? 1_555 G CA  .   CA ? ? A ASN 182 A CA  703  1_555 ? ? ? ? ? ? ? 2.541 ? 
metalc4  metalc ?    ? A ASN 191 OD1 ? ? ? 1_555 G CA  .   CA ? ? A ASN 183 A CA  703  1_555 ? ? ? ? ? ? ? 2.416 ? 
metalc5  metalc ?    ? A GLU 641 OE1 ? ? ? 1_555 F CA  .   CA ? ? A GLU 633 A CA  702  1_555 ? ? ? ? ? ? ? 2.632 ? 
metalc6  metalc ?    ? A GLU 641 OE2 ? ? ? 1_555 F CA  .   CA ? ? A GLU 633 A CA  702  1_555 ? ? ? ? ? ? ? 2.436 ? 
metalc7  metalc ?    ? B ASP 160 OD2 ? ? ? 1_555 J CA  .   CA ? ? B ASP 152 B CA  702  1_555 ? ? ? ? ? ? ? 2.333 ? 
covale3  covale both ? B GLY 161 C   ? ? ? 1_555 B OCS 162 N  ? ? B GLY 153 B OCS 154  1_555 ? ? ? ? ? ? ? 1.327 ? 
covale4  covale both ? B OCS 162 C   ? ? ? 1_555 B LEU 163 N  ? ? B OCS 154 B LEU 155  1_555 ? ? ? ? ? ? ? 1.329 ? 
metalc8  metalc ?    ? B ASN 190 OD1 ? ? ? 1_555 J CA  .   CA ? ? B ASN 182 B CA  702  1_555 ? ? ? ? ? ? ? 2.350 ? 
metalc9  metalc ?    ? B ILE 192 O   ? ? ? 1_555 J CA  .   CA ? ? B ILE 184 B CA  702  1_555 ? ? ? ? ? ? ? 2.259 ? 
metalc10 metalc ?    ? B GLU 641 OE1 ? ? ? 1_555 I CA  .   CA ? ? B GLU 633 B CA  701  1_555 ? ? ? ? ? ? ? 2.583 ? 
metalc11 metalc ?    ? B GLU 641 OE2 ? ? ? 1_555 I CA  .   CA ? ? B GLU 633 B CA  701  1_555 ? ? ? ? ? ? ? 2.425 ? 
metalc12 metalc ?    ? C ASP 160 OD2 ? ? ? 1_555 P CA  .   CA ? ? C ASP 152 C CA  705  1_555 ? ? ? ? ? ? ? 2.351 ? 
covale5  covale both ? C GLY 161 C   ? ? ? 1_555 C OCS 162 N  ? ? C GLY 153 C OCS 154  1_555 ? ? ? ? ? ? ? 1.325 ? 
covale6  covale both ? C OCS 162 C   ? ? ? 1_555 C LEU 163 N  ? ? C OCS 154 C LEU 155  1_555 ? ? ? ? ? ? ? 1.330 ? 
metalc13 metalc ?    ? C ASN 190 OD1 ? ? ? 1_555 P CA  .   CA ? ? C ASN 182 C CA  705  1_555 ? ? ? ? ? ? ? 2.531 ? 
metalc14 metalc ?    ? C ASN 191 OD1 ? ? ? 1_555 P CA  .   CA ? ? C ASN 183 C CA  705  1_555 ? ? ? ? ? ? ? 2.488 ? 
metalc15 metalc ?    ? C SER 398 O   ? ? ? 1_555 N CA  .   CA ? ? C SER 390 C CA  703  1_555 ? ? ? ? ? ? ? 2.427 ? 
metalc16 metalc ?    ? C SER 398 OG  ? ? ? 1_555 N CA  .   CA ? ? C SER 390 C CA  703  1_555 ? ? ? ? ? ? ? 2.411 ? 
metalc17 metalc ?    ? C GLU 641 OE1 ? ? ? 1_555 O CA  .   CA ? ? C GLU 633 C CA  704  1_555 ? ? ? ? ? ? ? 2.711 ? 
metalc18 metalc ?    ? C GLU 641 OE2 ? ? ? 1_555 O CA  .   CA ? ? C GLU 633 C CA  704  1_555 ? ? ? ? ? ? ? 2.579 ? 
metalc19 metalc ?    ? D ASP 160 OD2 ? ? ? 1_555 T CA  .   CA ? ? D ASP 152 D CA  704  1_555 ? ? ? ? ? ? ? 2.350 ? 
covale7  covale both ? D GLY 161 C   ? ? ? 1_555 D OCS 162 N  ? ? D GLY 153 D OCS 154  1_555 ? ? ? ? ? ? ? 1.327 ? 
covale8  covale both ? D OCS 162 C   ? ? ? 1_555 D LEU 163 N  ? ? D OCS 154 D LEU 155  1_555 ? ? ? ? ? ? ? 1.326 ? 
metalc20 metalc ?    ? D ASN 190 OD1 ? ? ? 1_555 T CA  .   CA ? ? D ASN 182 D CA  704  1_555 ? ? ? ? ? ? ? 2.359 ? 
metalc21 metalc ?    ? D SER 398 O   ? ? ? 1_555 V CA  .   CA ? ? D SER 390 D CA  706  1_555 ? ? ? ? ? ? ? 2.452 ? 
metalc22 metalc ?    ? D SER 398 OG  ? ? ? 1_555 V CA  .   CA ? ? D SER 390 D CA  706  1_555 ? ? ? ? ? ? ? 2.537 ? 
metalc23 metalc ?    ? D GLU 641 OE1 ? ? ? 1_555 U CA  .   CA ? ? D GLU 633 D CA  705  1_555 ? ? ? ? ? ? ? 2.482 ? 
metalc24 metalc ?    ? D GLU 641 OE2 ? ? ? 1_555 U CA  .   CA ? ? D GLU 633 D CA  705  1_555 ? ? ? ? ? ? ? 2.397 ? 
metalc25 metalc ?    ? F CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? A CA  702 A HOH 1196 1_555 ? ? ? ? ? ? ? 2.524 ? 
metalc26 metalc ?    ? F CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? A CA  702 B HOH 1000 1_555 ? ? ? ? ? ? ? 2.358 ? 
metalc27 metalc ?    ? F CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? A CA  702 B HOH 1201 1_555 ? ? ? ? ? ? ? 2.746 ? 
metalc28 metalc ?    ? F CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? A CA  702 B HOH 1339 1_555 ? ? ? ? ? ? ? 2.468 ? 
metalc29 metalc ?    ? F CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? A CA  702 A HOH 1152 1_555 ? ? ? ? ? ? ? 2.355 ? 
metalc30 metalc ?    ? F CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? A CA  702 A HOH 1181 1_555 ? ? ? ? ? ? ? 2.405 ? 
metalc31 metalc ?    ? G CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? A CA  703 A HOH 842  1_555 ? ? ? ? ? ? ? 2.379 ? 
metalc32 metalc ?    ? G CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? A CA  703 A HOH 1206 1_555 ? ? ? ? ? ? ? 2.624 ? 
metalc33 metalc ?    ? I CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? B CA  701 A HOH 906  1_555 ? ? ? ? ? ? ? 2.453 ? 
metalc34 metalc ?    ? I CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? B CA  701 A HOH 1252 1_555 ? ? ? ? ? ? ? 2.517 ? 
metalc35 metalc ?    ? I CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  701 B HOH 1261 1_555 ? ? ? ? ? ? ? 2.393 ? 
metalc36 metalc ?    ? I CA  .   CA  ? ? ? 1_555 W HOH .   O  ? ? B CA  701 A HOH 1157 1_555 ? ? ? ? ? ? ? 2.348 ? 
metalc37 metalc ?    ? I CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  701 B HOH 1271 1_555 ? ? ? ? ? ? ? 2.531 ? 
metalc38 metalc ?    ? I CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  701 B HOH 1217 1_555 ? ? ? ? ? ? ? 2.490 ? 
metalc39 metalc ?    ? J CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  702 B HOH 1281 1_555 ? ? ? ? ? ? ? 2.493 ? 
metalc40 metalc ?    ? J CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  702 B HOH 1242 1_555 ? ? ? ? ? ? ? 2.732 ? 
metalc41 metalc ?    ? J CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  702 B HOH 998  1_555 ? ? ? ? ? ? ? 2.408 ? 
metalc42 metalc ?    ? K CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  703 B HOH 1281 1_555 ? ? ? ? ? ? ? 3.083 ? 
metalc43 metalc ?    ? K CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? B CA  703 B HOH 962  1_555 ? ? ? ? ? ? ? 3.110 ? 
metalc44 metalc ?    ? L EDO .   O1  ? ? ? 1_555 N CA  .   CA ? ? C EDO 701 C CA  703  1_555 ? ? ? ? ? ? ? 2.427 ? 
metalc45 metalc ?    ? L EDO .   O2  ? ? ? 1_555 N CA  .   CA ? ? C EDO 701 C CA  703  1_555 ? ? ? ? ? ? ? 2.580 ? 
metalc46 metalc ?    ? N CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  703 C HOH 1098 1_555 ? ? ? ? ? ? ? 2.452 ? 
metalc47 metalc ?    ? N CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  703 C HOH 1192 1_555 ? ? ? ? ? ? ? 2.455 ? 
metalc48 metalc ?    ? N CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  703 C HOH 1095 1_555 ? ? ? ? ? ? ? 2.457 ? 
metalc49 metalc ?    ? N CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  703 C HOH 869  1_555 ? ? ? ? ? ? ? 2.412 ? 
metalc50 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  704 C HOH 1187 1_555 ? ? ? ? ? ? ? 2.555 ? 
metalc51 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? C CA  704 D HOH 875  1_555 ? ? ? ? ? ? ? 2.301 ? 
metalc52 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? C CA  704 D HOH 1222 1_555 ? ? ? ? ? ? ? 2.485 ? 
metalc53 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  704 C HOH 1162 1_555 ? ? ? ? ? ? ? 2.316 ? 
metalc54 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  704 C HOH 1188 1_555 ? ? ? ? ? ? ? 2.407 ? 
metalc55 metalc ?    ? O CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  704 C HOH 1199 1_555 ? ? ? ? ? ? ? 2.374 ? 
metalc56 metalc ?    ? P CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  705 C HOH 893  1_555 ? ? ? ? ? ? ? 2.548 ? 
metalc57 metalc ?    ? P CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? C CA  705 C HOH 1212 1_555 ? ? ? ? ? ? ? 2.387 ? 
metalc58 metalc ?    ? Q EDO .   O1  ? ? ? 1_555 V CA  .   CA ? ? D EDO 701 D CA  706  1_555 ? ? ? ? ? ? ? 2.576 ? 
metalc59 metalc ?    ? Q EDO .   O2  ? ? ? 1_555 V CA  .   CA ? ? D EDO 701 D CA  706  1_555 ? ? ? ? ? ? ? 2.594 ? 
metalc60 metalc ?    ? T CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? D CA  704 D HOH 924  1_555 ? ? ? ? ? ? ? 2.422 ? 
metalc61 metalc ?    ? U CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? D CA  705 C HOH 1020 1_555 ? ? ? ? ? ? ? 2.585 ? 
metalc62 metalc ?    ? U CA  .   CA  ? ? ? 1_555 Y HOH .   O  ? ? D CA  705 C HOH 1086 1_555 ? ? ? ? ? ? ? 2.475 ? 
metalc63 metalc ?    ? V CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? D CA  706 D HOH 1151 1_555 ? ? ? ? ? ? ? 2.583 ? 
metalc64 metalc ?    ? V CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? D CA  706 D HOH 1031 1_555 ? ? ? ? ? ? ? 2.443 ? 
metalc65 metalc ?    ? V CA  .   CA  ? ? ? 1_555 Z HOH .   O  ? ? D CA  706 D HOH 1057 1_555 ? ? ? ? ? ? ? 2.453 ? 
metalc66 metalc ?    ? V CA  .   CA  ? ? ? 1_555 X HOH .   O  ? ? D CA  706 B HOH 1213 2_646 ? ? ? ? ? ? ? 2.513 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
AA8 ? 5 ? 
AA9 ? 5 ? 
AB1 ? 6 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
AB4 ? 6 ? 
AB5 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB4 5 6 ? parallel      
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 64  ? LEU A 67  ? ARG A 56  LEU A 59  
AA1 2 THR A 154 ? MET A 158 ? THR A 146 MET A 150 
AA1 3 LEU A 183 ? ASP A 189 ? LEU A 175 ASP A 181 
AA1 4 SER A 244 ? LYS A 249 ? SER A 236 LYS A 241 
AA1 5 HIS A 216 ? ASN A 222 ? HIS A 208 ASN A 214 
AA2 1 VAL A 360 ? ALA A 361 ? VAL A 352 ALA A 353 
AA2 2 ASN A 527 ? LEU A 528 ? ASN A 519 LEU A 520 
AA3 1 TYR A 409 ? HIS A 411 ? TYR A 401 HIS A 403 
AA3 2 LEU A 380 ? SER A 384 ? LEU A 372 SER A 376 
AA3 3 LYS A 433 ? PHE A 439 ? LYS A 425 PHE A 431 
AA3 4 VAL A 461 ? THR A 465 ? VAL A 453 THR A 457 
AA3 5 SER A 519 ? ILE A 522 ? SER A 511 ILE A 514 
AA3 6 ASP A 494 ? TRP A 496 ? ASP A 486 TRP A 488 
AA4 1 TYR A 546 ? SER A 549 ? TYR A 538 SER A 541 
AA4 2 VAL A 583 ? SER A 587 ? VAL A 575 SER A 579 
AA4 3 ALA A 557 ? ALA A 561 ? ALA A 549 ALA A 553 
AA4 4 ARG A 612 ? VAL A 615 ? ARG A 604 VAL A 607 
AA4 5 ALA A 632 ? VAL A 634 ? ALA A 624 VAL A 626 
AA5 1 ARG B 64  ? LEU B 67  ? ARG B 56  LEU B 59  
AA5 2 THR B 154 ? GLY B 159 ? THR B 146 GLY B 151 
AA5 3 LEU B 183 ? ASP B 189 ? LEU B 175 ASP B 181 
AA5 4 SER B 244 ? LYS B 249 ? SER B 236 LYS B 241 
AA5 5 HIS B 216 ? ASN B 222 ? HIS B 208 ASN B 214 
AA6 1 ILE B 192 ? SER B 193 ? ILE B 184 SER B 185 
AA6 2 GLY B 196 ? LYS B 197 ? GLY B 188 LYS B 189 
AA7 1 TYR B 409 ? HIS B 411 ? TYR B 401 HIS B 403 
AA7 2 LEU B 380 ? SER B 384 ? LEU B 372 SER B 376 
AA7 3 LYS B 433 ? PHE B 439 ? LYS B 425 PHE B 431 
AA7 4 VAL B 461 ? THR B 465 ? VAL B 453 THR B 457 
AA7 5 SER B 519 ? ILE B 522 ? SER B 511 ILE B 514 
AA7 6 ASP B 494 ? TRP B 496 ? ASP B 486 TRP B 488 
AA8 1 TYR B 546 ? SER B 549 ? TYR B 538 SER B 541 
AA8 2 ARG B 584 ? SER B 587 ? ARG B 576 SER B 579 
AA8 3 VAL B 558 ? ALA B 561 ? VAL B 550 ALA B 553 
AA8 4 ARG B 612 ? VAL B 615 ? ARG B 604 VAL B 607 
AA8 5 ALA B 632 ? VAL B 634 ? ALA B 624 VAL B 626 
AA9 1 ARG C 64  ? LEU C 67  ? ARG C 56  LEU C 59  
AA9 2 THR C 154 ? MET C 158 ? THR C 146 MET C 150 
AA9 3 LEU C 183 ? ASP C 189 ? LEU C 175 ASP C 181 
AA9 4 SER C 244 ? LYS C 249 ? SER C 236 LYS C 241 
AA9 5 HIS C 216 ? ASN C 222 ? HIS C 208 ASN C 214 
AB1 1 TYR C 409 ? HIS C 411 ? TYR C 401 HIS C 403 
AB1 2 LEU C 380 ? SER C 384 ? LEU C 372 SER C 376 
AB1 3 LYS C 433 ? PHE C 439 ? LYS C 425 PHE C 431 
AB1 4 VAL C 461 ? THR C 465 ? VAL C 453 THR C 457 
AB1 5 SER C 519 ? ILE C 522 ? SER C 511 ILE C 514 
AB1 6 ASP C 494 ? TRP C 496 ? ASP C 486 TRP C 488 
AB2 1 TYR C 546 ? SER C 549 ? TYR C 538 SER C 541 
AB2 2 VAL C 583 ? SER C 587 ? VAL C 575 SER C 579 
AB2 3 ALA C 557 ? ALA C 561 ? ALA C 549 ALA C 553 
AB2 4 ARG C 612 ? VAL C 615 ? ARG C 604 VAL C 607 
AB2 5 ALA C 632 ? VAL C 634 ? ALA C 624 VAL C 626 
AB3 1 ARG D 64  ? LEU D 67  ? ARG D 56  LEU D 59  
AB3 2 THR D 154 ? MET D 158 ? THR D 146 MET D 150 
AB3 3 LEU D 183 ? ASP D 189 ? LEU D 175 ASP D 181 
AB3 4 SER D 244 ? LYS D 249 ? SER D 236 LYS D 241 
AB3 5 HIS D 216 ? ASN D 222 ? HIS D 208 ASN D 214 
AB4 1 TYR D 409 ? HIS D 411 ? TYR D 401 HIS D 403 
AB4 2 LEU D 380 ? SER D 384 ? LEU D 372 SER D 376 
AB4 3 LYS D 433 ? PHE D 439 ? LYS D 425 PHE D 431 
AB4 4 VAL D 461 ? THR D 465 ? VAL D 453 THR D 457 
AB4 5 SER D 519 ? ILE D 522 ? SER D 511 ILE D 514 
AB4 6 ASP D 494 ? TRP D 496 ? ASP D 486 TRP D 488 
AB5 1 TYR D 546 ? SER D 549 ? TYR D 538 SER D 541 
AB5 2 VAL D 583 ? SER D 587 ? VAL D 575 SER D 579 
AB5 3 ALA D 557 ? ALA D 561 ? ALA D 549 ALA D 553 
AB5 4 ARG D 612 ? VAL D 615 ? ARG D 604 VAL D 607 
AB5 5 ALA D 632 ? VAL D 634 ? ALA D 624 VAL D 626 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 64  ? N ARG A 56  O TYR A 155 ? O TYR A 147 
AA1 2 3 N VAL A 156 ? N VAL A 148 O LEU A 186 ? O LEU A 178 
AA1 3 4 N VAL A 185 ? N VAL A 177 O SER A 244 ? O SER A 236 
AA1 4 5 O LYS A 249 ? O LYS A 241 N VAL A 221 ? N VAL A 213 
AA2 1 2 N VAL A 360 ? N VAL A 352 O LEU A 528 ? O LEU A 520 
AA3 1 2 O ILE A 410 ? O ILE A 402 N GLY A 382 ? N GLY A 374 
AA3 2 3 N VAL A 381 ? N VAL A 373 O PHE A 435 ? O PHE A 427 
AA3 3 4 N GLY A 436 ? N GLY A 428 O VAL A 463 ? O VAL A 455 
AA3 4 5 N PHE A 464 ? N PHE A 456 O LEU A 521 ? O LEU A 513 
AA3 5 6 O CYS A 520 ? O CYS A 512 N TRP A 496 ? N TRP A 488 
AA4 1 2 N SER A 549 ? N SER A 541 O VAL A 585 ? O VAL A 577 
AA4 2 3 O VAL A 586 ? O VAL A 578 N ILE A 559 ? N ILE A 551 
AA4 3 4 N ILE A 560 ? N ILE A 552 O ILE A 613 ? O ILE A 605 
AA4 4 5 N ALA A 614 ? N ALA A 606 O VAL A 634 ? O VAL A 626 
AA5 1 2 N ARG B 64  ? N ARG B 56  O TYR B 155 ? O TYR B 147 
AA5 2 3 N VAL B 156 ? N VAL B 148 O LEU B 186 ? O LEU B 178 
AA5 3 4 N VAL B 185 ? N VAL B 177 O SER B 244 ? O SER B 236 
AA5 4 5 O LYS B 249 ? O LYS B 241 N VAL B 221 ? N VAL B 213 
AA6 1 2 N SER B 193 ? N SER B 185 O GLY B 196 ? O GLY B 188 
AA7 1 2 O ILE B 410 ? O ILE B 402 N GLY B 382 ? N GLY B 374 
AA7 2 3 N VAL B 381 ? N VAL B 373 O LYS B 433 ? O LYS B 425 
AA7 3 4 N GLY B 436 ? N GLY B 428 O VAL B 463 ? O VAL B 455 
AA7 4 5 N PHE B 464 ? N PHE B 456 O LEU B 521 ? O LEU B 513 
AA7 5 6 O CYS B 520 ? O CYS B 512 N TRP B 496 ? N TRP B 488 
AA8 1 2 N SER B 549 ? N SER B 541 O VAL B 585 ? O VAL B 577 
AA8 2 3 O VAL B 586 ? O VAL B 578 N ILE B 559 ? N ILE B 551 
AA8 3 4 N ILE B 560 ? N ILE B 552 O ILE B 613 ? O ILE B 605 
AA8 4 5 N ALA B 614 ? N ALA B 606 O VAL B 634 ? O VAL B 626 
AA9 1 2 N ARG C 64  ? N ARG C 56  O TYR C 155 ? O TYR C 147 
AA9 2 3 N VAL C 156 ? N VAL C 148 O LEU C 186 ? O LEU C 178 
AA9 3 4 N VAL C 185 ? N VAL C 177 O SER C 244 ? O SER C 236 
AA9 4 5 O LYS C 249 ? O LYS C 241 N VAL C 221 ? N VAL C 213 
AB1 1 2 O ILE C 410 ? O ILE C 402 N GLY C 382 ? N GLY C 374 
AB1 2 3 N VAL C 381 ? N VAL C 373 O LYS C 433 ? O LYS C 425 
AB1 3 4 N GLY C 436 ? N GLY C 428 O VAL C 463 ? O VAL C 455 
AB1 4 5 N PHE C 464 ? N PHE C 456 O LEU C 521 ? O LEU C 513 
AB1 5 6 O CYS C 520 ? O CYS C 512 N TRP C 496 ? N TRP C 488 
AB2 1 2 N SER C 549 ? N SER C 541 O VAL C 585 ? O VAL C 577 
AB2 2 3 O VAL C 586 ? O VAL C 578 N ILE C 559 ? N ILE C 551 
AB2 3 4 N ILE C 560 ? N ILE C 552 O ILE C 613 ? O ILE C 605 
AB2 4 5 N ALA C 614 ? N ALA C 606 O VAL C 634 ? O VAL C 626 
AB3 1 2 N ARG D 64  ? N ARG D 56  O TYR D 155 ? O TYR D 147 
AB3 2 3 N VAL D 156 ? N VAL D 148 O LEU D 186 ? O LEU D 178 
AB3 3 4 N VAL D 185 ? N VAL D 177 O ILE D 246 ? O ILE D 238 
AB3 4 5 O LYS D 249 ? O LYS D 241 N VAL D 221 ? N VAL D 213 
AB4 1 2 O ILE D 410 ? O ILE D 402 N GLY D 382 ? N GLY D 374 
AB4 2 3 N VAL D 381 ? N VAL D 373 O LYS D 433 ? O LYS D 425 
AB4 3 4 N GLY D 436 ? N GLY D 428 O VAL D 463 ? O VAL D 455 
AB4 4 5 N PHE D 464 ? N PHE D 456 O LEU D 521 ? O LEU D 513 
AB4 5 6 O CYS D 520 ? O CYS D 512 N TRP D 496 ? N TRP D 488 
AB5 1 2 N SER D 549 ? N SER D 541 O VAL D 585 ? O VAL D 577 
AB5 2 3 O VAL D 586 ? O VAL D 578 N ILE D 559 ? N ILE D 551 
AB5 3 4 N ILE D 560 ? N ILE D 552 O ILE D 613 ? O ILE D 605 
AB5 4 5 N ALA D 614 ? N ALA D 606 O VAL D 634 ? O VAL D 626 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A EDO 701 ? 6  'binding site for residue EDO A 701' 
AC2 Software A CA  702 ? 7  'binding site for residue CA A 702'  
AC3 Software A CA  703 ? 5  'binding site for residue CA A 703'  
AC4 Software A CA  704 ? 4  'binding site for residue CA A 704'  
AC5 Software B CA  701 ? 7  'binding site for residue CA B 701'  
AC6 Software B CA  702 ? 6  'binding site for residue CA B 702'  
AC7 Software B CA  703 ? 3  'binding site for residue CA B 703'  
AC8 Software C EDO 701 ? 7  'binding site for residue EDO C 701' 
AC9 Software C EDO 702 ? 9  'binding site for residue EDO C 702' 
AD1 Software C CA  703 ? 6  'binding site for residue CA C 703'  
AD2 Software C CA  704 ? 7  'binding site for residue CA C 704'  
AD3 Software C CA  705 ? 5  'binding site for residue CA C 705'  
AD4 Software D EDO 701 ? 6  'binding site for residue EDO D 701' 
AD5 Software D EDO 702 ? 7  'binding site for residue EDO D 702' 
AD6 Software D EDO 703 ? 10 'binding site for residue EDO D 703' 
AD7 Software D CA  704 ? 3  'binding site for residue CA D 704'  
AD8 Software D CA  705 ? 3  'binding site for residue CA D 705'  
AD9 Software D CA  706 ? 5  'binding site for residue CA D 706'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 6  SER A 564 ? SER A 556  . ? 1_555 ? 
2   AC1 6  GLU A 565 ? GLU A 557  . ? 1_555 ? 
3   AC1 6  PHE A 649 ? PHE A 641  . ? 1_555 ? 
4   AC1 6  PHE A 654 ? PHE A 646  . ? 1_555 ? 
5   AC1 6  HOH W .   ? HOH A 997  . ? 1_555 ? 
6   AC1 6  HOH W .   ? HOH A 1018 . ? 1_555 ? 
7   AC2 7  GLU A 641 ? GLU A 633  . ? 1_555 ? 
8   AC2 7  HOH W .   ? HOH A 1152 . ? 1_555 ? 
9   AC2 7  HOH W .   ? HOH A 1181 . ? 1_555 ? 
10  AC2 7  HOH W .   ? HOH A 1196 . ? 1_555 ? 
11  AC2 7  HOH X .   ? HOH B 1000 . ? 1_555 ? 
12  AC2 7  HOH X .   ? HOH B 1201 . ? 1_555 ? 
13  AC2 7  HOH X .   ? HOH B 1339 . ? 1_555 ? 
14  AC3 5  ASP A 160 ? ASP A 152  . ? 1_555 ? 
15  AC3 5  ASN A 190 ? ASN A 182  . ? 1_555 ? 
16  AC3 5  ASN A 191 ? ASN A 183  . ? 1_555 ? 
17  AC3 5  HOH W .   ? HOH A 842  . ? 1_555 ? 
18  AC3 5  HOH W .   ? HOH A 1206 . ? 1_555 ? 
19  AC4 4  GLY A 159 ? GLY A 151  . ? 1_555 ? 
20  AC4 4  ASP A 160 ? ASP A 152  . ? 1_555 ? 
21  AC4 4  GLY A 161 ? GLY A 153  . ? 1_555 ? 
22  AC4 4  OCS A 162 ? OCS A 154  . ? 1_555 ? 
23  AC5 7  HOH W .   ? HOH A 906  . ? 1_555 ? 
24  AC5 7  HOH W .   ? HOH A 1157 . ? 1_555 ? 
25  AC5 7  HOH W .   ? HOH A 1252 . ? 1_555 ? 
26  AC5 7  GLU B 641 ? GLU B 633  . ? 1_555 ? 
27  AC5 7  HOH X .   ? HOH B 1217 . ? 1_555 ? 
28  AC5 7  HOH X .   ? HOH B 1261 . ? 1_555 ? 
29  AC5 7  HOH X .   ? HOH B 1271 . ? 1_555 ? 
30  AC6 6  ASP B 160 ? ASP B 152  . ? 1_555 ? 
31  AC6 6  ASN B 190 ? ASN B 182  . ? 1_555 ? 
32  AC6 6  ILE B 192 ? ILE B 184  . ? 1_555 ? 
33  AC6 6  HOH X .   ? HOH B 998  . ? 1_555 ? 
34  AC6 6  HOH X .   ? HOH B 1242 . ? 1_555 ? 
35  AC6 6  HOH X .   ? HOH B 1281 . ? 1_555 ? 
36  AC7 3  GLY B 161 ? GLY B 153  . ? 1_555 ? 
37  AC7 3  OCS B 162 ? OCS B 154  . ? 1_555 ? 
38  AC7 3  HOH X .   ? HOH B 1281 . ? 1_555 ? 
39  AC8 7  ASP C 394 ? ASP C 386  . ? 1_555 ? 
40  AC8 7  SER C 398 ? SER C 390  . ? 1_555 ? 
41  AC8 7  SER C 400 ? SER C 392  . ? 1_555 ? 
42  AC8 7  TYR C 409 ? TYR C 401  . ? 1_555 ? 
43  AC8 7  CA  N .   ? CA  C 703  . ? 1_555 ? 
44  AC8 7  HOH Y .   ? HOH C 869  . ? 1_555 ? 
45  AC8 7  HOH Y .   ? HOH C 1095 . ? 1_555 ? 
46  AC9 9  VAL C 414 ? VAL C 406  . ? 1_555 ? 
47  AC9 9  GLU C 416 ? GLU C 408  . ? 1_555 ? 
48  AC9 9  PHE C 442 ? PHE C 434  . ? 1_555 ? 
49  AC9 9  HOH Y .   ? HOH C 816  . ? 1_555 ? 
50  AC9 9  HOH Y .   ? HOH C 823  . ? 1_555 ? 
51  AC9 9  GLY D 119 ? GLY D 111  . ? 1_555 ? 
52  AC9 9  PRO D 120 ? PRO D 112  . ? 1_555 ? 
53  AC9 9  LEU D 121 ? LEU D 113  . ? 1_555 ? 
54  AC9 9  GLU D 165 ? GLU D 157  . ? 1_555 ? 
55  AD1 6  SER C 398 ? SER C 390  . ? 1_555 ? 
56  AD1 6  EDO L .   ? EDO C 701  . ? 1_555 ? 
57  AD1 6  HOH Y .   ? HOH C 869  . ? 1_555 ? 
58  AD1 6  HOH Y .   ? HOH C 1095 . ? 1_555 ? 
59  AD1 6  HOH Y .   ? HOH C 1098 . ? 1_555 ? 
60  AD1 6  HOH Y .   ? HOH C 1192 . ? 1_555 ? 
61  AD2 7  GLU C 641 ? GLU C 633  . ? 1_555 ? 
62  AD2 7  HOH Y .   ? HOH C 1162 . ? 1_555 ? 
63  AD2 7  HOH Y .   ? HOH C 1187 . ? 1_555 ? 
64  AD2 7  HOH Y .   ? HOH C 1188 . ? 1_555 ? 
65  AD2 7  HOH Y .   ? HOH C 1199 . ? 1_555 ? 
66  AD2 7  HOH Z .   ? HOH D 875  . ? 1_555 ? 
67  AD2 7  HOH Z .   ? HOH D 1222 . ? 1_555 ? 
68  AD3 5  ASP C 160 ? ASP C 152  . ? 1_555 ? 
69  AD3 5  ASN C 190 ? ASN C 182  . ? 1_555 ? 
70  AD3 5  ASN C 191 ? ASN C 183  . ? 1_555 ? 
71  AD3 5  HOH Y .   ? HOH C 893  . ? 1_555 ? 
72  AD3 5  HOH Y .   ? HOH C 1212 . ? 1_555 ? 
73  AD4 6  ASP D 394 ? ASP D 386  . ? 1_555 ? 
74  AD4 6  SER D 398 ? SER D 390  . ? 1_555 ? 
75  AD4 6  SER D 400 ? SER D 392  . ? 1_555 ? 
76  AD4 6  TYR D 409 ? TYR D 401  . ? 1_555 ? 
77  AD4 6  CA  V .   ? CA  D 706  . ? 1_555 ? 
78  AD4 6  HOH Z .   ? HOH D 1031 . ? 1_555 ? 
79  AD5 7  ASP D 540 ? ASP D 532  . ? 1_555 ? 
80  AD5 7  TYR D 546 ? TYR D 538  . ? 1_555 ? 
81  AD5 7  VAL D 547 ? VAL D 539  . ? 1_555 ? 
82  AD5 7  TYR D 601 ? TYR D 593  . ? 1_555 ? 
83  AD5 7  VAL D 605 ? VAL D 597  . ? 1_555 ? 
84  AD5 7  HOH Z .   ? HOH D 841  . ? 1_555 ? 
85  AD5 7  HOH Z .   ? HOH D 908  . ? 1_555 ? 
86  AD6 10 PHE D 18  ? PHE D 10   . ? 1_555 ? 
87  AD6 10 LEU D 19  ? LEU D 11   . ? 1_555 ? 
88  AD6 10 ASP D 22  ? ASP D 14   . ? 1_555 ? 
89  AD6 10 ARG D 279 ? ARG D 271  . ? 1_555 ? 
90  AD6 10 TRP D 284 ? TRP D 276  . ? 1_555 ? 
91  AD6 10 TYR D 286 ? TYR D 278  . ? 1_555 ? 
92  AD6 10 PRO D 287 ? PRO D 279  . ? 1_555 ? 
93  AD6 10 ALA D 288 ? ALA D 280  . ? 1_555 ? 
94  AD6 10 PHE D 289 ? PHE D 281  . ? 1_555 ? 
95  AD6 10 GLU D 290 ? GLU D 282  . ? 1_555 ? 
96  AD7 3  ASP D 160 ? ASP D 152  . ? 1_555 ? 
97  AD7 3  ASN D 190 ? ASN D 182  . ? 1_555 ? 
98  AD7 3  HOH Z .   ? HOH D 924  . ? 1_555 ? 
99  AD8 3  HOH Y .   ? HOH C 1020 . ? 1_555 ? 
100 AD8 3  HOH Y .   ? HOH C 1086 . ? 1_555 ? 
101 AD8 3  GLU D 641 ? GLU D 633  . ? 1_555 ? 
102 AD9 5  SER D 398 ? SER D 390  . ? 1_555 ? 
103 AD9 5  EDO Q .   ? EDO D 701  . ? 1_555 ? 
104 AD9 5  HOH Z .   ? HOH D 1031 . ? 1_555 ? 
105 AD9 5  HOH Z .   ? HOH D 1057 . ? 1_555 ? 
106 AD9 5  HOH Z .   ? HOH D 1151 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5VRB 
_atom_sites.fract_transf_matrix[1][1]   0.012129 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000022 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008756 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007956 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . SER A 1 10  ? -7.653  8.874   -7.576  1.00 69.06 ? 2    SER A N   1 
ATOM   2     C  CA  . SER A 1 10  ? -7.794  9.834   -6.488  1.00 61.92 ? 2    SER A CA  1 
ATOM   3     C  C   . SER A 1 10  ? -8.654  9.256   -5.378  1.00 48.72 ? 2    SER A C   1 
ATOM   4     O  O   . SER A 1 10  ? -8.263  9.249   -4.195  1.00 31.13 ? 2    SER A O   1 
ATOM   5     C  CB  . SER A 1 10  ? -8.403  11.143  -7.000  1.00 71.59 ? 2    SER A CB  1 
ATOM   6     O  OG  . SER A 1 10  ? -8.530  12.094  -5.956  1.00 73.15 ? 2    SER A OG  1 
ATOM   7     N  N   . GLN A 1 11  ? -9.833  8.763   -5.771  1.00 38.36 ? 3    GLN A N   1 
ATOM   8     C  CA  . GLN A 1 11  ? -10.772 8.236   -4.790  1.00 34.15 ? 3    GLN A CA  1 
ATOM   9     C  C   . GLN A 1 11  ? -10.262 6.966   -4.132  1.00 31.44 ? 3    GLN A C   1 
ATOM   10    O  O   . GLN A 1 11  ? -10.704 6.641   -3.024  1.00 26.35 ? 3    GLN A O   1 
ATOM   11    C  CB  . GLN A 1 11  ? -12.134 7.999   -5.438  1.00 39.26 ? 3    GLN A CB  1 
ATOM   12    C  CG  . GLN A 1 11  ? -12.802 9.285   -5.919  1.00 46.25 ? 3    GLN A CG  1 
ATOM   13    C  CD  . GLN A 1 11  ? -12.910 10.344  -4.823  1.00 53.22 ? 3    GLN A CD  1 
ATOM   14    O  OE1 . GLN A 1 11  ? -11.976 11.109  -4.582  1.00 53.97 ? 3    GLN A OE1 1 
ATOM   15    N  NE2 . GLN A 1 11  ? -14.058 10.393  -4.161  1.00 61.09 ? 3    GLN A NE2 1 
ATOM   16    N  N   . LEU A 1 12  ? -9.315  6.262   -4.765  1.00 24.39 ? 4    LEU A N   1 
ATOM   17    C  CA  . LEU A 1 12  ? -8.762  5.070   -4.133  1.00 22.26 ? 4    LEU A CA  1 
ATOM   18    C  C   . LEU A 1 12  ? -7.920  5.423   -2.912  1.00 20.88 ? 4    LEU A C   1 
ATOM   19    O  O   . LEU A 1 12  ? -7.894  4.657   -1.947  1.00 21.81 ? 4    LEU A O   1 
ATOM   20    C  CB  . LEU A 1 12  ? -7.940  4.265   -5.134  1.00 28.03 ? 4    LEU A CB  1 
ATOM   21    C  CG  . LEU A 1 12  ? -8.675  3.688   -6.348  1.00 36.28 ? 4    LEU A CG  1 
ATOM   22    C  CD1 . LEU A 1 12  ? -7.862  2.545   -6.939  1.00 39.89 ? 4    LEU A CD1 1 
ATOM   23    C  CD2 . LEU A 1 12  ? -10.082 3.233   -5.995  1.00 37.81 ? 4    LEU A CD2 1 
ATOM   24    N  N   . ALA A 1 13  ? -7.236  6.573   -2.925  1.00 24.87 ? 5    ALA A N   1 
ATOM   25    C  CA  . ALA A 1 13  ? -6.562  7.039   -1.711  1.00 21.39 ? 5    ALA A CA  1 
ATOM   26    C  C   . ALA A 1 13  ? -7.551  7.676   -0.736  1.00 18.51 ? 5    ALA A C   1 
ATOM   27    O  O   . ALA A 1 13  ? -7.460  7.460   0.481   1.00 22.27 ? 5    ALA A O   1 
ATOM   28    C  CB  . ALA A 1 13  ? -5.457  8.033   -2.072  1.00 22.53 ? 5    ALA A CB  1 
ATOM   29    N  N   . ASN A 1 14  ? -8.501  8.466   -1.256  1.00 20.31 ? 6    ASN A N   1 
ATOM   30    C  CA  . ASN A 1 14  ? -9.464  9.148   -0.391  1.00 24.78 ? 6    ASN A CA  1 
ATOM   31    C  C   . ASN A 1 14  ? -10.308 8.172   0.425   1.00 25.67 ? 6    ASN A C   1 
ATOM   32    O  O   . ASN A 1 14  ? -10.683 8.487   1.562   1.00 24.34 ? 6    ASN A O   1 
ATOM   33    C  CB  . ASN A 1 14  ? -10.372 10.059  -1.218  1.00 28.33 ? 6    ASN A CB  1 
ATOM   34    C  CG  . ASN A 1 14  ? -9.753  11.420  -1.477  1.00 30.59 ? 6    ASN A CG  1 
ATOM   35    O  OD1 . ASN A 1 14  ? -8.731  11.776  -0.883  1.00 32.90 ? 6    ASN A OD1 1 
ATOM   36    N  ND2 . ASN A 1 14  ? -10.376 12.193  -2.359  1.00 28.65 ? 6    ASN A ND2 1 
ATOM   37    N  N   . VAL A 1 15  ? -10.628 6.996   -0.122  1.00 21.24 ? 7    VAL A N   1 
ATOM   38    C  CA  . VAL A 1 15  ? -11.438 6.051   0.649   1.00 22.35 ? 7    VAL A CA  1 
ATOM   39    C  C   . VAL A 1 15  ? -10.682 5.594   1.891   1.00 19.03 ? 7    VAL A C   1 
ATOM   40    O  O   . VAL A 1 15  ? -11.262 5.492   2.977   1.00 20.86 ? 7    VAL A O   1 
ATOM   41    C  CB  . VAL A 1 15  ? -11.899 4.862   -0.223  1.00 25.70 ? 7    VAL A CB  1 
ATOM   42    C  CG1 . VAL A 1 15  ? -10.725 4.027   -0.695  1.00 21.80 ? 7    VAL A CG1 1 
ATOM   43    C  CG2 . VAL A 1 15  ? -12.907 3.984   0.547   1.00 24.75 ? 7    VAL A CG2 1 
ATOM   44    N  N   . ILE A 1 16  ? -9.373  5.335   1.765   1.00 20.04 ? 8    ILE A N   1 
ATOM   45    C  CA  . ILE A 1 16  ? -8.564  5.036   2.947   1.00 18.58 ? 8    ILE A CA  1 
ATOM   46    C  C   . ILE A 1 16  ? -8.573  6.218   3.902   1.00 20.84 ? 8    ILE A C   1 
ATOM   47    O  O   . ILE A 1 16  ? -8.676  6.064   5.127   1.00 19.38 ? 8    ILE A O   1 
ATOM   48    C  CB  . ILE A 1 16  ? -7.117  4.704   2.544   1.00 23.58 ? 8    ILE A CB  1 
ATOM   49    C  CG1 . ILE A 1 16  ? -7.047  3.512   1.611   1.00 27.98 ? 8    ILE A CG1 1 
ATOM   50    C  CG2 . ILE A 1 16  ? -6.296  4.433   3.783   1.00 23.45 ? 8    ILE A CG2 1 
ATOM   51    C  CD1 . ILE A 1 16  ? -5.642  3.305   1.113   1.00 34.53 ? 8    ILE A CD1 1 
ATOM   52    N  N   . ARG A 1 17  ? -8.404  7.411   3.348   1.00 23.69 ? 9    ARG A N   1 
ATOM   53    C  CA  . ARG A 1 17  ? -8.312  8.625   4.140   1.00 26.05 ? 9    ARG A CA  1 
ATOM   54    C  C   . ARG A 1 17  ? -9.550  8.803   5.009   1.00 24.72 ? 9    ARG A C   1 
ATOM   55    O  O   . ARG A 1 17  ? -9.450  9.028   6.220   1.00 21.56 ? 9    ARG A O   1 
ATOM   56    C  CB  . ARG A 1 17  ? -8.114  9.801   3.183   1.00 27.01 ? 9    ARG A CB  1 
ATOM   57    C  CG  . ARG A 1 17  ? -8.141  11.157  3.791   1.00 34.23 ? 9    ARG A CG  1 
ATOM   58    C  CD  . ARG A 1 17  ? -7.603  12.176  2.796   1.00 34.04 ? 9    ARG A CD  1 
ATOM   59    N  NE  . ARG A 1 17  ? -6.148  12.120  2.661   1.00 28.47 ? 9    ARG A NE  1 
ATOM   60    C  CZ  . ARG A 1 17  ? -5.503  11.865  1.527   1.00 28.67 ? 9    ARG A CZ  1 
ATOM   61    N  NH1 . ARG A 1 17  ? -6.178  11.640  0.400   1.00 24.93 ? 9    ARG A NH1 1 
ATOM   62    N  NH2 . ARG A 1 17  ? -4.176  11.856  1.514   1.00 28.76 ? 9    ARG A NH2 1 
ATOM   63    N  N   . PHE A 1 18  ? -10.731 8.661   4.418   1.00 21.84 ? 10   PHE A N   1 
ATOM   64    C  CA  . PHE A 1 18  ? -11.946 8.965   5.160   1.00 22.93 ? 10   PHE A CA  1 
ATOM   65    C  C   . PHE A 1 18  ? -12.524 7.771   5.910   1.00 23.45 ? 10   PHE A C   1 
ATOM   66    O  O   . PHE A 1 18  ? -13.223 7.972   6.906   1.00 24.08 ? 10   PHE A O   1 
ATOM   67    C  CB  . PHE A 1 18  ? -12.967 9.592   4.210   1.00 21.49 ? 10   PHE A CB  1 
ATOM   68    C  CG  . PHE A 1 18  ? -12.544 10.944  3.738   1.00 27.92 ? 10   PHE A CG  1 
ATOM   69    C  CD1 . PHE A 1 18  ? -12.552 12.022  4.611   1.00 37.37 ? 10   PHE A CD1 1 
ATOM   70    C  CD2 . PHE A 1 18  ? -12.072 11.133  2.454   1.00 31.49 ? 10   PHE A CD2 1 
ATOM   71    C  CE1 . PHE A 1 18  ? -12.133 13.271  4.198   1.00 39.28 ? 10   PHE A CE1 1 
ATOM   72    C  CE2 . PHE A 1 18  ? -11.649 12.384  2.032   1.00 33.58 ? 10   PHE A CE2 1 
ATOM   73    C  CZ  . PHE A 1 18  ? -11.679 13.452  2.905   1.00 37.25 ? 10   PHE A CZ  1 
ATOM   74    N  N   . LEU A 1 19  ? -12.241 6.540   5.489   1.00 22.95 ? 11   LEU A N   1 
ATOM   75    C  CA  . LEU A 1 19  ? -12.528 5.411   6.369   1.00 21.64 ? 11   LEU A CA  1 
ATOM   76    C  C   . LEU A 1 19  ? -11.808 5.580   7.700   1.00 21.49 ? 11   LEU A C   1 
ATOM   77    O  O   . LEU A 1 19  ? -12.364 5.288   8.767   1.00 21.86 ? 11   LEU A O   1 
ATOM   78    C  CB  . LEU A 1 19  ? -12.093 4.104   5.721   1.00 24.20 ? 11   LEU A CB  1 
ATOM   79    C  CG  . LEU A 1 19  ? -13.077 3.081   5.195   1.00 24.51 ? 11   LEU A CG  1 
ATOM   80    C  CD1 . LEU A 1 19  ? -12.335 1.759   5.046   1.00 19.82 ? 11   LEU A CD1 1 
ATOM   81    C  CD2 . LEU A 1 19  ? -14.322 2.934   6.094   1.00 21.89 ? 11   LEU A CD2 1 
ATOM   82    N  N   . SER A 1 20  ? -10.563 6.050   7.649   1.00 19.91 ? 12   SER A N   1 
ATOM   83    C  CA  . SER A 1 20  ? -9.776  6.235   8.861   1.00 19.79 ? 12   SER A CA  1 
ATOM   84    C  C   . SER A 1 20  ? -10.349 7.349   9.726   1.00 21.05 ? 12   SER A C   1 
ATOM   85    O  O   . SER A 1 20  ? -10.586 7.159   10.927  1.00 26.65 ? 12   SER A O   1 
ATOM   86    C  CB  . SER A 1 20  ? -8.317  6.529   8.486   1.00 23.64 ? 12   SER A CB  1 
ATOM   87    O  OG  . SER A 1 20  ? -7.782  5.469   7.704   1.00 24.11 ? 12   SER A OG  1 
ATOM   88    N  N   . ALA A 1 21  ? -10.576 8.522   9.134   1.00 21.36 ? 13   ALA A N   1 
ATOM   89    C  CA  . ALA A 1 21  ? -11.128 9.640   9.893   1.00 24.16 ? 13   ALA A CA  1 
ATOM   90    C  C   . ALA A 1 21  ? -12.491 9.294   10.476  1.00 22.27 ? 13   ALA A C   1 
ATOM   91    O  O   . ALA A 1 21  ? -12.797 9.659   11.615  1.00 22.84 ? 13   ALA A O   1 
ATOM   92    C  CB  . ALA A 1 21  ? -11.229 10.877  9.002   1.00 26.23 ? 13   ALA A CB  1 
ATOM   93    N  N   . ASP A 1 22  ? -13.323 8.587   9.710   1.00 22.18 ? 14   ASP A N   1 
ATOM   94    C  CA  . ASP A 1 22  ? -14.661 8.252   10.182  1.00 25.05 ? 14   ASP A CA  1 
ATOM   95    C  C   . ASP A 1 22  ? -14.619 7.255   11.341  1.00 23.86 ? 14   ASP A C   1 
ATOM   96    O  O   . ASP A 1 22  ? -15.414 7.359   12.282  1.00 20.53 ? 14   ASP A O   1 
ATOM   97    C  CB  . ASP A 1 22  ? -15.505 7.697   9.029   1.00 27.32 ? 14   ASP A CB  1 
ATOM   98    C  CG  . ASP A 1 22  ? -15.894 8.770   8.005   1.00 28.27 ? 14   ASP A CG  1 
ATOM   99    O  OD1 . ASP A 1 22  ? -15.898 9.974   8.343   1.00 30.93 ? 14   ASP A OD1 1 
ATOM   100   O  OD2 . ASP A 1 22  ? -16.212 8.400   6.857   1.00 27.24 ? 14   ASP A OD2 1 
ATOM   101   N  N   . ALA A 1 23  ? -13.720 6.271   11.283  1.00 21.87 ? 15   ALA A N   1 
ATOM   102   C  CA  . ALA A 1 23  ? -13.620 5.312   12.383  1.00 21.30 ? 15   ALA A CA  1 
ATOM   103   C  C   . ALA A 1 23  ? -13.034 5.956   13.633  1.00 20.82 ? 15   ALA A C   1 
ATOM   104   O  O   . ALA A 1 23  ? -13.429 5.618   14.759  1.00 22.40 ? 15   ALA A O   1 
ATOM   105   C  CB  . ALA A 1 23  ? -12.776 4.111   11.961  1.00 23.19 ? 15   ALA A CB  1 
ATOM   106   N  N   . VAL A 1 24  ? -12.060 6.853   13.457  1.00 23.81 ? 16   VAL A N   1 
ATOM   107   C  CA  . VAL A 1 24  ? -11.497 7.573   14.594  1.00 22.33 ? 16   VAL A CA  1 
ATOM   108   C  C   . VAL A 1 24  ? -12.563 8.449   15.236  1.00 23.69 ? 16   VAL A C   1 
ATOM   109   O  O   . VAL A 1 24  ? -12.726 8.464   16.461  1.00 26.68 ? 16   VAL A O   1 
ATOM   110   C  CB  . VAL A 1 24  ? -10.270 8.394   14.152  1.00 25.97 ? 16   VAL A CB  1 
ATOM   111   C  CG1 . VAL A 1 24  ? -9.848  9.375   15.239  1.00 30.12 ? 16   VAL A CG1 1 
ATOM   112   C  CG2 . VAL A 1 24  ? -9.113  7.467   13.797  1.00 24.59 ? 16   VAL A CG2 1 
ATOM   113   N  N   . GLN A 1 25  ? -13.328 9.169   14.412  1.00 22.94 ? 17   GLN A N   1 
ATOM   114   C  CA  . GLN A 1 25  ? -14.395 10.017  14.935  1.00 31.06 ? 17   GLN A CA  1 
ATOM   115   C  C   . GLN A 1 25  ? -15.409 9.202   15.729  1.00 27.74 ? 17   GLN A C   1 
ATOM   116   O  O   . GLN A 1 25  ? -15.809 9.594   16.828  1.00 27.30 ? 17   GLN A O   1 
ATOM   117   C  CB  . GLN A 1 25  ? -15.086 10.761  13.791  1.00 35.54 ? 17   GLN A CB  1 
ATOM   118   N  N   . LYS A 1 26  ? -15.838 8.062   15.186  1.00 27.13 ? 18   LYS A N   1 
ATOM   119   C  CA  . LYS A 1 26  ? -16.836 7.245   15.875  1.00 31.76 ? 18   LYS A CA  1 
ATOM   120   C  C   . LYS A 1 26  ? -16.313 6.746   17.219  1.00 26.94 ? 18   LYS A C   1 
ATOM   121   O  O   . LYS A 1 26  ? -17.035 6.752   18.222  1.00 28.88 ? 18   LYS A O   1 
ATOM   122   C  CB  . LYS A 1 26  ? -17.242 6.069   14.989  1.00 24.10 ? 18   LYS A CB  1 
ATOM   123   C  CG  . LYS A 1 26  ? -18.387 5.231   15.539  1.00 31.63 ? 18   LYS A CG  1 
ATOM   124   C  CD  . LYS A 1 26  ? -18.815 4.189   14.524  1.00 29.30 ? 18   LYS A CD  1 
ATOM   125   C  CE  . LYS A 1 26  ? -20.083 3.470   14.972  1.00 33.09 ? 18   LYS A CE  1 
ATOM   126   N  NZ  . LYS A 1 26  ? -19.835 2.494   16.073  1.00 31.23 ? 18   LYS A NZ  1 
ATOM   127   N  N   . ALA A 1 27  ? -15.054 6.311   17.253  1.00 28.01 ? 19   ALA A N   1 
ATOM   128   C  CA  . ALA A 1 27  ? -14.451 5.846   18.498  1.00 30.75 ? 19   ALA A CA  1 
ATOM   129   C  C   . ALA A 1 27  ? -14.261 6.985   19.494  1.00 31.21 ? 19   ALA A C   1 
ATOM   130   O  O   . ALA A 1 27  ? -14.235 6.748   20.710  1.00 34.03 ? 19   ALA A O   1 
ATOM   131   C  CB  . ALA A 1 27  ? -13.108 5.176   18.191  1.00 28.41 ? 19   ALA A CB  1 
ATOM   132   N  N   . ASN A 1 28  ? -14.142 8.219   18.995  1.00 32.44 ? 20   ASN A N   1 
ATOM   133   C  CA  . ASN A 1 28  ? -13.739 9.382   19.792  1.00 41.64 ? 20   ASN A CA  1 
ATOM   134   C  C   . ASN A 1 28  ? -12.404 9.123   20.494  1.00 40.92 ? 20   ASN A C   1 
ATOM   135   O  O   . ASN A 1 28  ? -12.206 9.468   21.663  1.00 41.33 ? 20   ASN A O   1 
ATOM   136   C  CB  . ASN A 1 28  ? -14.825 9.779   20.792  1.00 46.72 ? 20   ASN A CB  1 
ATOM   137   C  CG  . ASN A 1 28  ? -14.630 11.184  21.326  1.00 55.92 ? 20   ASN A CG  1 
ATOM   138   O  OD1 . ASN A 1 28  ? -14.082 12.050  20.640  1.00 55.06 ? 20   ASN A OD1 1 
ATOM   139   N  ND2 . ASN A 1 28  ? -15.070 11.416  22.559  1.00 62.40 ? 20   ASN A ND2 1 
ATOM   140   N  N   . SER A 1 29  ? -11.476 8.512   19.760  1.00 40.44 ? 21   SER A N   1 
ATOM   141   C  CA  . SER A 1 29  ? -10.177 8.113   20.287  1.00 43.57 ? 21   SER A CA  1 
ATOM   142   C  C   . SER A 1 29  ? -9.279  7.738   19.119  1.00 41.72 ? 21   SER A C   1 
ATOM   143   O  O   . SER A 1 29  ? -9.748  7.180   18.125  1.00 37.11 ? 21   SER A O   1 
ATOM   144   C  CB  . SER A 1 29  ? -10.306 6.931   21.263  1.00 44.04 ? 21   SER A CB  1 
ATOM   145   O  OG  . SER A 1 29  ? -9.039  6.548   21.782  1.00 39.10 ? 21   SER A OG  1 
ATOM   146   N  N   . GLY A 1 30  ? -7.995  8.049   19.242  1.00 52.93 ? 22   GLY A N   1 
ATOM   147   C  CA  . GLY A 1 30  ? -7.053  7.856   18.160  1.00 56.19 ? 22   GLY A CA  1 
ATOM   148   C  C   . GLY A 1 30  ? -6.764  9.151   17.417  1.00 58.27 ? 22   GLY A C   1 
ATOM   149   O  O   . GLY A 1 30  ? -7.382  10.195  17.641  1.00 58.09 ? 22   GLY A O   1 
ATOM   150   N  N   . HIS A 1 31  ? -5.791  9.072   16.511  1.00 59.19 ? 23   HIS A N   1 
ATOM   151   C  CA  . HIS A 1 31  ? -5.343  10.230  15.750  1.00 62.26 ? 23   HIS A CA  1 
ATOM   152   C  C   . HIS A 1 31  ? -5.665  10.020  14.277  1.00 54.89 ? 23   HIS A C   1 
ATOM   153   O  O   . HIS A 1 31  ? -5.246  9.003   13.695  1.00 55.69 ? 23   HIS A O   1 
ATOM   154   C  CB  . HIS A 1 31  ? -3.842  10.466  15.941  1.00 66.25 ? 23   HIS A CB  1 
ATOM   155   N  N   . PRO A 1 32  ? -6.409  10.925  13.635  1.00 43.50 ? 24   PRO A N   1 
ATOM   156   C  CA  . PRO A 1 32  ? -6.767  10.712  12.225  1.00 41.13 ? 24   PRO A CA  1 
ATOM   157   C  C   . PRO A 1 32  ? -5.768  11.314  11.250  1.00 36.00 ? 24   PRO A C   1 
ATOM   158   O  O   . PRO A 1 32  ? -5.732  10.919  10.082  1.00 29.27 ? 24   PRO A O   1 
ATOM   159   C  CB  . PRO A 1 32  ? -8.134  11.395  12.112  1.00 37.69 ? 24   PRO A CB  1 
ATOM   160   C  CG  . PRO A 1 32  ? -8.068  12.505  13.121  1.00 39.96 ? 24   PRO A CG  1 
ATOM   161   C  CD  . PRO A 1 32  ? -7.174  12.029  14.243  1.00 41.68 ? 24   PRO A CD  1 
ATOM   162   N  N   . GLY A 1 33  ? -4.951  12.261  11.718  1.00 40.46 ? 25   GLY A N   1 
ATOM   163   C  CA  . GLY A 1 33  ? -4.076  12.989  10.809  1.00 40.30 ? 25   GLY A CA  1 
ATOM   164   C  C   . GLY A 1 33  ? -3.038  12.112  10.130  1.00 34.15 ? 25   GLY A C   1 
ATOM   165   O  O   . GLY A 1 33  ? -2.784  12.250  8.930   1.00 30.59 ? 25   GLY A O   1 
ATOM   166   N  N   . ALA A 1 34  ? -2.416  11.202  10.886  1.00 33.06 ? 26   ALA A N   1 
ATOM   167   C  CA  . ALA A 1 34  ? -1.357  10.379  10.300  1.00 34.71 ? 26   ALA A CA  1 
ATOM   168   C  C   . ALA A 1 34  ? -1.885  9.428   9.231   1.00 29.89 ? 26   ALA A C   1 
ATOM   169   O  O   . ALA A 1 34  ? -1.327  9.414   8.118   1.00 25.74 ? 26   ALA A O   1 
ATOM   170   C  CB  . ALA A 1 34  ? -0.594  9.644   11.409  1.00 42.67 ? 26   ALA A CB  1 
ATOM   171   N  N   . PRO A 1 35  ? -2.931  8.625   9.469   1.00 25.98 ? 27   PRO A N   1 
ATOM   172   C  CA  . PRO A 1 35  ? -3.467  7.819   8.364   1.00 24.32 ? 27   PRO A CA  1 
ATOM   173   C  C   . PRO A 1 35  ? -3.930  8.657   7.188   1.00 26.77 ? 27   PRO A C   1 
ATOM   174   O  O   . PRO A 1 35  ? -3.798  8.226   6.037   1.00 31.81 ? 27   PRO A O   1 
ATOM   175   C  CB  . PRO A 1 35  ? -4.643  7.069   9.006   1.00 21.48 ? 27   PRO A CB  1 
ATOM   176   C  CG  . PRO A 1 35  ? -4.445  7.180   10.449  1.00 25.89 ? 27   PRO A CG  1 
ATOM   177   C  CD  . PRO A 1 35  ? -3.728  8.451   10.697  1.00 31.23 ? 27   PRO A CD  1 
ATOM   178   N  N   . MET A 1 36  ? -4.478  9.846   7.436   1.00 27.29 ? 28   MET A N   1 
ATOM   179   C  CA  . MET A 1 36  ? -4.941  10.658  6.318   1.00 31.43 ? 28   MET A CA  1 
ATOM   180   C  C   . MET A 1 36  ? -3.773  11.178  5.494   1.00 27.54 ? 28   MET A C   1 
ATOM   181   O  O   . MET A 1 36  ? -3.862  11.244  4.264   1.00 27.90 ? 28   MET A O   1 
ATOM   182   C  CB  . MET A 1 36  ? -5.811  11.805  6.820   1.00 35.51 ? 28   MET A CB  1 
ATOM   183   C  CG  . MET A 1 36  ? -7.136  11.346  7.404   1.00 34.79 ? 28   MET A CG  1 
ATOM   184   S  SD  . MET A 1 36  ? -8.065  12.740  8.060   1.00 42.24 ? 28   MET A SD  1 
ATOM   185   C  CE  . MET A 1 36  ? -8.274  13.695  6.556   1.00 43.58 ? 28   MET A CE  1 
ATOM   186   N  N   . GLY A 1 37  ? -2.661  11.529  6.148   1.00 22.75 ? 29   GLY A N   1 
ATOM   187   C  CA  . GLY A 1 37  ? -1.507  12.033  5.416   1.00 24.64 ? 29   GLY A CA  1 
ATOM   188   C  C   . GLY A 1 37  ? -0.800  10.984  4.574   1.00 22.29 ? 29   GLY A C   1 
ATOM   189   O  O   . GLY A 1 37  ? -0.143  11.320  3.581   1.00 22.69 ? 29   GLY A O   1 
ATOM   190   N  N   . MET A 1 38  ? -0.914  9.710   4.953   1.00 20.52 ? 30   MET A N   1 
ATOM   191   C  CA  . MET A 1 38  ? -0.208  8.616   4.294   1.00 18.99 ? 30   MET A CA  1 
ATOM   192   C  C   . MET A 1 38  ? -1.059  7.870   3.277   1.00 17.98 ? 30   MET A C   1 
ATOM   193   O  O   . MET A 1 38  ? -0.655  6.799   2.824   1.00 16.43 ? 30   MET A O   1 
ATOM   194   C  CB  . MET A 1 38  ? 0.317   7.624   5.335   1.00 17.61 ? 30   MET A CB  1 
ATOM   195   C  CG  . MET A 1 38  ? 1.516   8.157   6.105   1.00 19.12 ? 30   MET A CG  1 
ATOM   196   S  SD  . MET A 1 38  ? 2.237   6.936   7.231   1.00 24.73 ? 30   MET A SD  1 
ATOM   197   C  CE  . MET A 1 38  ? 0.887   6.822   8.396   1.00 27.81 ? 30   MET A CE  1 
ATOM   198   N  N   . ALA A 1 39  ? -2.213  8.415   2.892   1.00 14.61 ? 31   ALA A N   1 
ATOM   199   C  CA  . ALA A 1 39  ? -3.150  7.641   2.086   1.00 17.95 ? 31   ALA A CA  1 
ATOM   200   C  C   . ALA A 1 39  ? -2.615  7.396   0.677   1.00 15.77 ? 31   ALA A C   1 
ATOM   201   O  O   . ALA A 1 39  ? -2.787  6.301   0.131   1.00 17.70 ? 31   ALA A O   1 
ATOM   202   C  CB  . ALA A 1 39  ? -4.500  8.358   2.036   1.00 19.36 ? 31   ALA A CB  1 
ATOM   203   N  N   . GLU A 1 40  ? -1.991  8.409   0.058   1.00 16.38 ? 32   GLU A N   1 
ATOM   204   C  CA  . GLU A 1 40  ? -1.414  8.203   -1.273  1.00 15.98 ? 32   GLU A CA  1 
ATOM   205   C  C   . GLU A 1 40  ? -0.215  7.266   -1.207  1.00 18.95 ? 32   GLU A C   1 
ATOM   206   O  O   . GLU A 1 40  ? -0.005  6.456   -2.116  1.00 19.29 ? 32   GLU A O   1 
ATOM   207   C  CB  . GLU A 1 40  ? -1.007  9.533   -1.914  1.00 17.87 ? 32   GLU A CB  1 
ATOM   208   C  CG  . GLU A 1 40  ? -2.159  10.347  -2.518  1.00 21.05 ? 32   GLU A CG  1 
ATOM   209   C  CD  . GLU A 1 40  ? -2.975  11.042  -1.462  1.00 26.80 ? 32   GLU A CD  1 
ATOM   210   O  OE1 . GLU A 1 40  ? -2.404  11.357  -0.400  1.00 21.39 ? 32   GLU A OE1 1 
ATOM   211   O  OE2 . GLU A 1 40  ? -4.182  11.265  -1.686  1.00 25.30 ? 32   GLU A OE2 1 
ATOM   212   N  N   . MET A 1 41  ? 0.596   7.369   -0.149  1.00 15.05 ? 33   MET A N   1 
ATOM   213   C  CA  . MET A 1 41  ? 1.670   6.401   0.043   1.00 16.77 ? 33   MET A CA  1 
ATOM   214   C  C   . MET A 1 41  ? 1.108   4.990   0.123   1.00 15.48 ? 33   MET A C   1 
ATOM   215   O  O   . MET A 1 41  ? 1.599   4.074   -0.547  1.00 14.94 ? 33   MET A O   1 
ATOM   216   C  CB  . MET A 1 41  ? 2.473   6.741   1.303   1.00 14.10 ? 33   MET A CB  1 
ATOM   217   C  CG  . MET A 1 41  ? 3.259   8.029   1.179   1.00 15.62 ? 33   MET A CG  1 
ATOM   218   S  SD  . MET A 1 41  ? 3.587   8.766   2.800   1.00 18.67 ? 33   MET A SD  1 
ATOM   219   C  CE  . MET A 1 41  ? 4.688   7.553   3.536   1.00 17.66 ? 33   MET A CE  1 
ATOM   220   N  N   . ALA A 1 42  ? 0.062   4.809   0.933   1.00 14.16 ? 34   ALA A N   1 
ATOM   221   C  CA  . ALA A 1 42  ? -0.581  3.508   1.077   1.00 13.04 ? 34   ALA A CA  1 
ATOM   222   C  C   . ALA A 1 42  ? -1.179  3.034   -0.238  1.00 14.36 ? 34   ALA A C   1 
ATOM   223   O  O   . ALA A 1 42  ? -1.001  1.879   -0.635  1.00 14.54 ? 34   ALA A O   1 
ATOM   224   C  CB  . ALA A 1 42  ? -1.673  3.582   2.144   1.00 14.68 ? 34   ALA A CB  1 
ATOM   225   N  N   . GLU A 1 43  ? -1.946  3.899   -0.898  1.00 13.31 ? 35   GLU A N   1 
ATOM   226   C  CA  A GLU A 1 43  ? -2.557  3.514   -2.165  0.51 16.11 ? 35   GLU A CA  1 
ATOM   227   C  CA  B GLU A 1 43  ? -2.554  3.518   -2.170  0.49 16.12 ? 35   GLU A CA  1 
ATOM   228   C  C   . GLU A 1 43  ? -1.496  3.069   -3.165  1.00 18.97 ? 35   GLU A C   1 
ATOM   229   O  O   . GLU A 1 43  ? -1.645  2.033   -3.827  1.00 18.26 ? 35   GLU A O   1 
ATOM   230   C  CB  A GLU A 1 43  ? -3.381  4.681   -2.716  0.51 16.46 ? 35   GLU A CB  1 
ATOM   231   C  CB  B GLU A 1 43  ? -3.357  4.679   -2.758  0.49 16.54 ? 35   GLU A CB  1 
ATOM   232   C  CG  A GLU A 1 43  ? -4.422  4.288   -3.770  0.51 20.39 ? 35   GLU A CG  1 
ATOM   233   C  CG  B GLU A 1 43  ? -3.934  4.349   -4.145  0.49 19.91 ? 35   GLU A CG  1 
ATOM   234   C  CD  A GLU A 1 43  ? -3.906  4.420   -5.188  0.51 20.44 ? 35   GLU A CD  1 
ATOM   235   C  CD  B GLU A 1 43  ? -4.128  5.568   -5.027  0.49 22.96 ? 35   GLU A CD  1 
ATOM   236   O  OE1 A GLU A 1 43  ? -2.677  4.501   -5.368  0.51 20.75 ? 35   GLU A OE1 1 
ATOM   237   O  OE1 B GLU A 1 43  ? -4.052  6.700   -4.509  0.49 22.71 ? 35   GLU A OE1 1 
ATOM   238   O  OE2 A GLU A 1 43  ? -4.731  4.459   -6.126  0.51 25.49 ? 35   GLU A OE2 1 
ATOM   239   O  OE2 B GLU A 1 43  ? -4.351  5.396   -6.247  0.49 24.34 ? 35   GLU A OE2 1 
ATOM   240   N  N   . THR A 1 44  ? -0.414  3.845   -3.288  1.00 16.42 ? 36   THR A N   1 
ATOM   241   C  CA  . THR A 1 44  ? 0.622   3.529   -4.270  1.00 20.39 ? 36   THR A CA  1 
ATOM   242   C  C   . THR A 1 44  ? 1.268   2.182   -3.980  1.00 17.52 ? 36   THR A C   1 
ATOM   243   O  O   . THR A 1 44  ? 1.364   1.324   -4.866  1.00 16.43 ? 36   THR A O   1 
ATOM   244   C  CB  . THR A 1 44  ? 1.677   4.635   -4.303  1.00 21.91 ? 36   THR A CB  1 
ATOM   245   O  OG1 . THR A 1 44  ? 1.061   5.865   -4.702  1.00 21.82 ? 36   THR A OG1 1 
ATOM   246   C  CG2 . THR A 1 44  ? 2.778   4.288   -5.297  1.00 19.34 ? 36   THR A CG2 1 
ATOM   247   N  N   . LEU A 1 45  ? 1.716   1.975   -2.740  1.00 13.49 ? 37   LEU A N   1 
ATOM   248   C  CA  . LEU A 1 45  ? 2.371   0.719   -2.387  1.00 14.66 ? 37   LEU A CA  1 
ATOM   249   C  C   . LEU A 1 45  ? 1.435   -0.473  -2.572  1.00 15.15 ? 37   LEU A C   1 
ATOM   250   O  O   . LEU A 1 45  ? 1.805   -1.473  -3.197  1.00 18.51 ? 37   LEU A O   1 
ATOM   251   C  CB  . LEU A 1 45  ? 2.883   0.778   -0.945  1.00 15.61 ? 37   LEU A CB  1 
ATOM   252   C  CG  . LEU A 1 45  ? 3.365   -0.558  -0.360  1.00 13.81 ? 37   LEU A CG  1 
ATOM   253   C  CD1 . LEU A 1 45  ? 4.501   -1.158  -1.191  1.00 18.98 ? 37   LEU A CD1 1 
ATOM   254   C  CD2 . LEU A 1 45  ? 3.778   -0.425  1.120   1.00 12.68 ? 37   LEU A CD2 1 
ATOM   255   N  N   . TRP A 1 46  ? 0.218   -0.390  -2.029  1.00 13.84 ? 38   TRP A N   1 
ATOM   256   C  CA  . TRP A 1 46  ? -0.648  -1.565  -1.998  1.00 17.36 ? 38   TRP A CA  1 
ATOM   257   C  C   . TRP A 1 46  ? -1.273  -1.888  -3.359  1.00 17.71 ? 38   TRP A C   1 
ATOM   258   O  O   . TRP A 1 46  ? -1.473  -3.068  -3.670  1.00 18.62 ? 38   TRP A O   1 
ATOM   259   C  CB  . TRP A 1 46  ? -1.731  -1.389  -0.935  1.00 14.99 ? 38   TRP A CB  1 
ATOM   260   C  CG  . TRP A 1 46  ? -1.238  -1.723  0.444   1.00 13.84 ? 38   TRP A CG  1 
ATOM   261   C  CD1 . TRP A 1 46  ? -0.202  -1.133  1.117   1.00 13.01 ? 38   TRP A CD1 1 
ATOM   262   C  CD2 . TRP A 1 46  ? -1.749  -2.742  1.306   1.00 14.63 ? 38   TRP A CD2 1 
ATOM   263   N  NE1 . TRP A 1 46  ? -0.038  -1.731  2.354   1.00 13.35 ? 38   TRP A NE1 1 
ATOM   264   C  CE2 . TRP A 1 46  ? -0.988  -2.707  2.499   1.00 19.16 ? 38   TRP A CE2 1 
ATOM   265   C  CE3 . TRP A 1 46  ? -2.787  -3.669  1.196   1.00 16.05 ? 38   TRP A CE3 1 
ATOM   266   C  CZ2 . TRP A 1 46  ? -1.226  -3.576  3.558   1.00 20.14 ? 38   TRP A CZ2 1 
ATOM   267   C  CZ3 . TRP A 1 46  ? -3.031  -4.524  2.254   1.00 20.41 ? 38   TRP A CZ3 1 
ATOM   268   C  CH2 . TRP A 1 46  ? -2.250  -4.474  3.419   1.00 21.76 ? 38   TRP A CH2 1 
ATOM   269   N  N   . THR A 1 47  ? -1.590  -0.886  -4.186  1.00 18.04 ? 39   THR A N   1 
ATOM   270   C  CA  . THR A 1 47  ? -2.170  -1.207  -5.493  1.00 19.45 ? 39   THR A CA  1 
ATOM   271   C  C   . THR A 1 47  ? -1.127  -1.464  -6.579  1.00 20.45 ? 39   THR A C   1 
ATOM   272   O  O   . THR A 1 47  ? -1.428  -2.175  -7.548  1.00 22.86 ? 39   THR A O   1 
ATOM   273   C  CB  . THR A 1 47  ? -3.125  -0.099  -5.978  1.00 26.33 ? 39   THR A CB  1 
ATOM   274   O  OG1 . THR A 1 47  ? -2.396  1.091   -6.293  1.00 21.41 ? 39   THR A OG1 1 
ATOM   275   C  CG2 . THR A 1 47  ? -4.178  0.222   -4.929  1.00 19.56 ? 39   THR A CG2 1 
ATOM   276   N  N   . LYS A 1 48  ? 0.094   -0.937  -6.444  1.00 19.04 ? 40   LYS A N   1 
ATOM   277   C  CA  . LYS A 1 48  ? 1.070   -1.061  -7.522  1.00 20.16 ? 40   LYS A CA  1 
ATOM   278   C  C   . LYS A 1 48  ? 2.212   -2.028  -7.242  1.00 23.99 ? 40   LYS A C   1 
ATOM   279   O  O   . LYS A 1 48  ? 2.826   -2.512  -8.199  1.00 20.98 ? 40   LYS A O   1 
ATOM   280   C  CB  . LYS A 1 48  ? 1.672   0.309   -7.861  1.00 19.88 ? 40   LYS A CB  1 
ATOM   281   C  CG  . LYS A 1 48  ? 0.667   1.326   -8.386  1.00 21.29 ? 40   LYS A CG  1 
ATOM   282   C  CD  . LYS A 1 48  ? 0.081   0.849   -9.694  1.00 28.03 ? 40   LYS A CD  1 
ATOM   283   C  CE  . LYS A 1 48  ? -0.638  1.976   -10.404 1.00 41.98 ? 40   LYS A CE  1 
ATOM   284   N  NZ  . LYS A 1 48  ? -1.561  2.694   -9.491  1.00 39.35 ? 40   LYS A NZ  1 
ATOM   285   N  N   . PHE A 1 49  ? 2.512   -2.328  -5.969  1.00 17.91 ? 41   PHE A N   1 
ATOM   286   C  CA  . PHE A 1 49  ? 3.690   -3.131  -5.648  1.00 18.73 ? 41   PHE A CA  1 
ATOM   287   C  C   . PHE A 1 49  ? 3.426   -4.317  -4.731  1.00 18.08 ? 41   PHE A C   1 
ATOM   288   O  O   . PHE A 1 49  ? 3.930   -5.407  -5.002  1.00 19.84 ? 41   PHE A O   1 
ATOM   289   C  CB  . PHE A 1 49  ? 4.774   -2.223  -5.022  1.00 21.25 ? 41   PHE A CB  1 
ATOM   290   C  CG  . PHE A 1 49  ? 5.342   -1.235  -5.987  1.00 20.42 ? 41   PHE A CG  1 
ATOM   291   C  CD1 . PHE A 1 49  ? 6.240   -1.641  -6.962  1.00 23.78 ? 41   PHE A CD1 1 
ATOM   292   C  CD2 . PHE A 1 49  ? 4.966   0.091   -5.945  1.00 22.57 ? 41   PHE A CD2 1 
ATOM   293   C  CE1 . PHE A 1 49  ? 6.760   -0.735  -7.875  1.00 24.33 ? 41   PHE A CE1 1 
ATOM   294   C  CE2 . PHE A 1 49  ? 5.486   0.998   -6.850  1.00 23.87 ? 41   PHE A CE2 1 
ATOM   295   C  CZ  . PHE A 1 49  ? 6.385   0.585   -7.815  1.00 21.49 ? 41   PHE A CZ  1 
ATOM   296   N  N   . LEU A 1 50  ? 2.664   -4.138  -3.656  1.00 16.81 ? 42   LEU A N   1 
ATOM   297   C  CA  . LEU A 1 50  ? 2.578   -5.155  -2.613  1.00 17.34 ? 42   LEU A CA  1 
ATOM   298   C  C   . LEU A 1 50  ? 2.015   -6.471  -3.152  1.00 20.69 ? 42   LEU A C   1 
ATOM   299   O  O   . LEU A 1 50  ? 0.921   -6.504  -3.714  1.00 15.45 ? 42   LEU A O   1 
ATOM   300   C  CB  . LEU A 1 50  ? 1.714   -4.643  -1.457  1.00 16.61 ? 42   LEU A CB  1 
ATOM   301   C  CG  . LEU A 1 50  ? 1.857   -5.411  -0.144  1.00 15.55 ? 42   LEU A CG  1 
ATOM   302   C  CD1 . LEU A 1 50  ? 3.222   -5.184  0.506   1.00 14.87 ? 42   LEU A CD1 1 
ATOM   303   C  CD2 . LEU A 1 50  ? 0.721   -5.064  0.843   1.00 16.93 ? 42   LEU A CD2 1 
ATOM   304   N  N   . ASN A 1 51  ? 2.768   -7.558  -2.986  1.00 17.29 ? 43   ASN A N   1 
ATOM   305   C  CA  . ASN A 1 51  ? 2.345   -8.878  -3.442  1.00 18.91 ? 43   ASN A CA  1 
ATOM   306   C  C   . ASN A 1 51  ? 1.808   -9.646  -2.239  1.00 18.34 ? 43   ASN A C   1 
ATOM   307   O  O   . ASN A 1 51  ? 2.574   -10.052 -1.361  1.00 20.75 ? 43   ASN A O   1 
ATOM   308   C  CB  . ASN A 1 51  ? 3.500   -9.624  -4.112  1.00 15.01 ? 43   ASN A CB  1 
ATOM   309   C  CG  . ASN A 1 51  ? 3.860   -9.049  -5.463  1.00 19.22 ? 43   ASN A CG  1 
ATOM   310   O  OD1 . ASN A 1 51  ? 2.982   -8.711  -6.265  1.00 19.78 ? 43   ASN A OD1 1 
ATOM   311   N  ND2 . ASN A 1 51  ? 5.156   -8.931  -5.728  1.00 20.39 ? 43   ASN A ND2 1 
ATOM   312   N  N   . HIS A 1 52  ? 0.489   -9.829  -2.195  1.00 14.64 ? 44   HIS A N   1 
ATOM   313   C  CA  . HIS A 1 52  ? -0.159  -10.469 -1.059  1.00 17.13 ? 44   HIS A CA  1 
ATOM   314   C  C   . HIS A 1 52  ? -1.404  -11.185 -1.553  1.00 17.20 ? 44   HIS A C   1 
ATOM   315   O  O   . HIS A 1 52  ? -1.928  -10.885 -2.627  1.00 22.78 ? 44   HIS A O   1 
ATOM   316   C  CB  . HIS A 1 52  ? -0.545  -9.455  0.032   1.00 15.91 ? 44   HIS A CB  1 
ATOM   317   C  CG  . HIS A 1 52  ? -1.554  -8.443  -0.417  1.00 18.46 ? 44   HIS A CG  1 
ATOM   318   N  ND1 . HIS A 1 52  ? -2.777  -8.285  0.200   1.00 21.48 ? 44   HIS A ND1 1 
ATOM   319   C  CD2 . HIS A 1 52  ? -1.526  -7.550  -1.435  1.00 18.55 ? 44   HIS A CD2 1 
ATOM   320   C  CE1 . HIS A 1 52  ? -3.453  -7.327  -0.413  1.00 20.92 ? 44   HIS A CE1 1 
ATOM   321   N  NE2 . HIS A 1 52  ? -2.714  -6.866  -1.407  1.00 18.44 ? 44   HIS A NE2 1 
ATOM   322   N  N   . ASN A 1 53  ? -1.876  -12.142 -0.765  1.00 17.98 ? 45   ASN A N   1 
ATOM   323   C  CA  . ASN A 1 53  ? -3.083  -12.888 -1.120  1.00 18.93 ? 45   ASN A CA  1 
ATOM   324   C  C   . ASN A 1 53  ? -4.059  -12.804 0.043   1.00 19.67 ? 45   ASN A C   1 
ATOM   325   O  O   . ASN A 1 53  ? -3.841  -13.467 1.078   1.00 19.67 ? 45   ASN A O   1 
ATOM   326   C  CB  . ASN A 1 53  ? -2.752  -14.334 -1.471  1.00 21.31 ? 45   ASN A CB  1 
ATOM   327   C  CG  . ASN A 1 53  ? -3.965  -15.112 -1.936  1.00 23.81 ? 45   ASN A CG  1 
ATOM   328   O  OD1 . ASN A 1 53  ? -5.046  -14.547 -2.135  1.00 24.11 ? 45   ASN A OD1 1 
ATOM   329   N  ND2 . ASN A 1 53  ? -3.797  -16.414 -2.111  1.00 25.75 ? 45   ASN A ND2 1 
ATOM   330   N  N   . PRO A 1 54  ? -5.126  -12.008 -0.068  1.00 19.03 ? 46   PRO A N   1 
ATOM   331   C  CA  . PRO A 1 54  ? -6.097  -11.936 1.037   1.00 23.71 ? 46   PRO A CA  1 
ATOM   332   C  C   . PRO A 1 54  ? -6.688  -13.283 1.400   1.00 20.71 ? 46   PRO A C   1 
ATOM   333   O  O   . PRO A 1 54  ? -7.060  -13.493 2.561   1.00 20.69 ? 46   PRO A O   1 
ATOM   334   C  CB  . PRO A 1 54  ? -7.169  -10.973 0.501   1.00 26.14 ? 46   PRO A CB  1 
ATOM   335   C  CG  . PRO A 1 54  ? -6.493  -10.214 -0.599  1.00 29.33 ? 46   PRO A CG  1 
ATOM   336   C  CD  . PRO A 1 54  ? -5.520  -11.167 -1.211  1.00 25.22 ? 46   PRO A CD  1 
ATOM   337   N  N   . ALA A 1 55  ? -6.791  -14.205 0.438   1.00 20.09 ? 47   ALA A N   1 
ATOM   338   C  CA  . ALA A 1 55  ? -7.309  -15.532 0.731   1.00 22.37 ? 47   ALA A CA  1 
ATOM   339   C  C   . ALA A 1 55  ? -6.369  -16.346 1.610   1.00 22.79 ? 47   ALA A C   1 
ATOM   340   O  O   . ALA A 1 55  ? -6.831  -17.267 2.285   1.00 21.95 ? 47   ALA A O   1 
ATOM   341   C  CB  . ALA A 1 55  ? -7.593  -16.293 -0.566  1.00 23.82 ? 47   ALA A CB  1 
ATOM   342   N  N   . ASN A 1 56  ? -5.074  -16.033 1.633   1.00 18.38 ? 48   ASN A N   1 
ATOM   343   C  CA  . ASN A 1 56  ? -4.124  -16.743 2.492   1.00 18.19 ? 48   ASN A CA  1 
ATOM   344   C  C   . ASN A 1 56  ? -3.126  -15.757 3.087   1.00 20.35 ? 48   ASN A C   1 
ATOM   345   O  O   . ASN A 1 56  ? -2.028  -15.549 2.547   1.00 18.75 ? 48   ASN A O   1 
ATOM   346   C  CB  . ASN A 1 56  ? -3.395  -17.853 1.735   1.00 21.51 ? 48   ASN A CB  1 
ATOM   347   C  CG  . ASN A 1 56  ? -2.390  -18.592 2.614   1.00 23.75 ? 48   ASN A CG  1 
ATOM   348   O  OD1 . ASN A 1 56  ? -2.443  -18.510 3.843   1.00 24.80 ? 48   ASN A OD1 1 
ATOM   349   N  ND2 . ASN A 1 56  ? -1.477  -19.311 1.988   1.00 20.77 ? 48   ASN A ND2 1 
ATOM   350   N  N   . PRO A 1 57  ? -3.467  -15.148 4.225   1.00 19.49 ? 49   PRO A N   1 
ATOM   351   C  CA  . PRO A 1 57  ? -2.542  -14.198 4.867   1.00 17.25 ? 49   PRO A CA  1 
ATOM   352   C  C   . PRO A 1 57  ? -1.229  -14.819 5.314   1.00 17.91 ? 49   PRO A C   1 
ATOM   353   O  O   . PRO A 1 57  ? -0.322  -14.074 5.715   1.00 18.26 ? 49   PRO A O   1 
ATOM   354   C  CB  . PRO A 1 57  ? -3.343  -13.685 6.075   1.00 21.68 ? 49   PRO A CB  1 
ATOM   355   C  CG  . PRO A 1 57  ? -4.781  -14.029 5.765   1.00 22.29 ? 49   PRO A CG  1 
ATOM   356   C  CD  . PRO A 1 57  ? -4.715  -15.312 4.989   1.00 20.34 ? 49   PRO A CD  1 
ATOM   357   N  N   . LYS A 1 58  ? -1.099  -16.146 5.290   1.00 17.76 ? 50   LYS A N   1 
ATOM   358   C  CA  . LYS A 1 58  ? 0.145   -16.817 5.658   1.00 18.94 ? 50   LYS A CA  1 
ATOM   359   C  C   . LYS A 1 58  ? 0.899   -17.344 4.441   1.00 18.13 ? 50   LYS A C   1 
ATOM   360   O  O   . LYS A 1 58  ? 1.794   -18.175 4.591   1.00 22.45 ? 50   LYS A O   1 
ATOM   361   C  CB  . LYS A 1 58  ? -0.120  -17.959 6.638   1.00 21.07 ? 50   LYS A CB  1 
ATOM   362   C  CG  . LYS A 1 58  ? -0.727  -17.531 7.974   1.00 26.46 ? 50   LYS A CG  1 
ATOM   363   C  CD  . LYS A 1 58  ? 0.185   -16.591 8.724   1.00 27.79 ? 50   LYS A CD  1 
ATOM   364   C  CE  . LYS A 1 58  ? -0.371  -16.256 10.109  1.00 29.93 ? 50   LYS A CE  1 
ATOM   365   N  NZ  . LYS A 1 58  ? 0.449   -15.185 10.755  1.00 29.91 ? 50   LYS A NZ  1 
ATOM   366   N  N   . PHE A 1 59  ? 0.541   -16.890 3.243   1.00 16.49 ? 51   PHE A N   1 
ATOM   367   C  CA  . PHE A 1 59  ? 1.269   -17.236 2.027   1.00 20.22 ? 51   PHE A CA  1 
ATOM   368   C  C   . PHE A 1 59  ? 2.762   -17.002 2.217   1.00 19.85 ? 51   PHE A C   1 
ATOM   369   O  O   . PHE A 1 59  ? 3.182   -15.883 2.519   1.00 15.50 ? 51   PHE A O   1 
ATOM   370   C  CB  . PHE A 1 59  ? 0.734   -16.393 0.870   1.00 15.92 ? 51   PHE A CB  1 
ATOM   371   C  CG  . PHE A 1 59  ? 1.575   -16.458 -0.386  1.00 15.90 ? 51   PHE A CG  1 
ATOM   372   C  CD1 . PHE A 1 59  ? 2.096   -17.666 -0.835  1.00 20.02 ? 51   PHE A CD1 1 
ATOM   373   C  CD2 . PHE A 1 59  ? 1.835   -15.306 -1.116  1.00 16.47 ? 51   PHE A CD2 1 
ATOM   374   C  CE1 . PHE A 1 59  ? 2.864   -17.719 -1.992  1.00 17.73 ? 51   PHE A CE1 1 
ATOM   375   C  CE2 . PHE A 1 59  ? 2.601   -15.355 -2.275  1.00 17.11 ? 51   PHE A CE2 1 
ATOM   376   C  CZ  . PHE A 1 59  ? 3.110   -16.569 -2.709  1.00 17.78 ? 51   PHE A CZ  1 
ATOM   377   N  N   . TYR A 1 60  ? 3.562   -18.064 2.040   1.00 17.94 ? 52   TYR A N   1 
ATOM   378   C  CA  . TYR A 1 60  ? 4.957   -18.016 2.476   1.00 17.59 ? 52   TYR A CA  1 
ATOM   379   C  C   . TYR A 1 60  ? 5.726   -16.877 1.814   1.00 16.62 ? 52   TYR A C   1 
ATOM   380   O  O   . TYR A 1 60  ? 6.538   -16.215 2.467   1.00 18.73 ? 52   TYR A O   1 
ATOM   381   C  CB  . TYR A 1 60  ? 5.667   -19.342 2.199   1.00 18.98 ? 52   TYR A CB  1 
ATOM   382   C  CG  . TYR A 1 60  ? 5.090   -20.569 2.882   1.00 20.43 ? 52   TYR A CG  1 
ATOM   383   C  CD1 . TYR A 1 60  ? 4.444   -20.488 4.106   1.00 20.68 ? 52   TYR A CD1 1 
ATOM   384   C  CD2 . TYR A 1 60  ? 5.204   -21.816 2.285   1.00 25.76 ? 52   TYR A CD2 1 
ATOM   385   C  CE1 . TYR A 1 60  ? 3.913   -21.627 4.714   1.00 22.30 ? 52   TYR A CE1 1 
ATOM   386   C  CE2 . TYR A 1 60  ? 4.681   -22.941 2.871   1.00 28.11 ? 52   TYR A CE2 1 
ATOM   387   C  CZ  . TYR A 1 60  ? 4.040   -22.848 4.083   1.00 25.66 ? 52   TYR A CZ  1 
ATOM   388   O  OH  . TYR A 1 60  ? 3.528   -23.988 4.646   1.00 25.64 ? 52   TYR A OH  1 
ATOM   389   N  N   . ASN A 1 61  ? 5.509   -16.638 0.520   1.00 16.77 ? 53   ASN A N   1 
ATOM   390   C  CA  . ASN A 1 61  ? 6.317   -15.663 -0.204  1.00 18.44 ? 53   ASN A CA  1 
ATOM   391   C  C   . ASN A 1 61  ? 5.647   -14.291 -0.329  1.00 15.76 ? 53   ASN A C   1 
ATOM   392   O  O   . ASN A 1 61  ? 6.077   -13.477 -1.148  1.00 20.30 ? 53   ASN A O   1 
ATOM   393   C  CB  . ASN A 1 61  ? 6.690   -16.186 -1.597  1.00 18.29 ? 53   ASN A CB  1 
ATOM   394   C  CG  . ASN A 1 61  ? 7.990   -15.575 -2.109  1.00 19.24 ? 53   ASN A CG  1 
ATOM   395   O  OD1 . ASN A 1 61  ? 8.957   -15.460 -1.357  1.00 18.42 ? 53   ASN A OD1 1 
ATOM   396   N  ND2 . ASN A 1 61  ? 8.014   -15.163 -3.382  1.00 16.35 ? 53   ASN A ND2 1 
ATOM   397   N  N   . ARG A 1 62  ? 4.618   -14.005 0.468   1.00 14.83 ? 54   ARG A N   1 
ATOM   398   C  CA  . ARG A 1 62  ? 4.024   -12.673 0.431   1.00 13.56 ? 54   ARG A CA  1 
ATOM   399   C  C   . ARG A 1 62  ? 5.065   -11.614 0.793   1.00 13.38 ? 54   ARG A C   1 
ATOM   400   O  O   . ARG A 1 62  ? 5.977   -11.851 1.592   1.00 16.51 ? 54   ARG A O   1 
ATOM   401   C  CB  . ARG A 1 62  ? 2.837   -12.586 1.404   1.00 13.35 ? 54   ARG A CB  1 
ATOM   402   C  CG  . ARG A 1 62  ? 3.269   -12.601 2.888   1.00 13.63 ? 54   ARG A CG  1 
ATOM   403   C  CD  . ARG A 1 62  ? 2.080   -12.725 3.827   1.00 13.45 ? 54   ARG A CD  1 
ATOM   404   N  NE  . ARG A 1 62  ? 2.460   -12.682 5.244   1.00 13.70 ? 54   ARG A NE  1 
ATOM   405   C  CZ  . ARG A 1 62  ? 2.972   -13.712 5.914   1.00 14.78 ? 54   ARG A CZ  1 
ATOM   406   N  NH1 . ARG A 1 62  ? 3.190   -14.862 5.288   1.00 18.46 ? 54   ARG A NH1 1 
ATOM   407   N  NH2 . ARG A 1 62  ? 3.291   -13.589 7.202   1.00 16.47 ? 54   ARG A NH2 1 
ATOM   408   N  N   . ASP A 1 63  ? 4.944   -10.444 0.173   1.00 16.71 ? 55   ASP A N   1 
ATOM   409   C  CA  . ASP A 1 63  ? 5.641   -9.281  0.701   1.00 17.34 ? 55   ASP A CA  1 
ATOM   410   C  C   . ASP A 1 63  ? 5.169   -9.019  2.131   1.00 15.60 ? 55   ASP A C   1 
ATOM   411   O  O   . ASP A 1 63  ? 4.019   -9.275  2.479   1.00 15.15 ? 55   ASP A O   1 
ATOM   412   C  CB  . ASP A 1 63  ? 5.379   -8.051  -0.164  1.00 15.17 ? 55   ASP A CB  1 
ATOM   413   C  CG  . ASP A 1 63  ? 6.065   -8.117  -1.520  1.00 19.43 ? 55   ASP A CG  1 
ATOM   414   O  OD1 . ASP A 1 63  ? 7.075   -8.847  -1.664  1.00 15.95 ? 55   ASP A OD1 1 
ATOM   415   O  OD2 . ASP A 1 63  ? 5.584   -7.412  -2.432  1.00 17.81 ? 55   ASP A OD2 1 
ATOM   416   N  N   . ARG A 1 64  ? 6.075   -8.534  2.969   1.00 13.82 ? 56   ARG A N   1 
ATOM   417   C  CA  . ARG A 1 64  ? 5.758   -8.165  4.341   1.00 14.90 ? 56   ARG A CA  1 
ATOM   418   C  C   . ARG A 1 64  ? 5.606   -6.653  4.428   1.00 17.22 ? 56   ARG A C   1 
ATOM   419   O  O   . ARG A 1 64  ? 6.515   -5.913  4.041   1.00 19.81 ? 56   ARG A O   1 
ATOM   420   C  CB  . ARG A 1 64  ? 6.856   -8.621  5.302   1.00 17.05 ? 56   ARG A CB  1 
ATOM   421   C  CG  . ARG A 1 64  ? 6.671   -9.996  5.953   1.00 21.31 ? 56   ARG A CG  1 
ATOM   422   C  CD  . ARG A 1 64  ? 6.511   -11.140 4.954   1.00 18.72 ? 56   ARG A CD  1 
ATOM   423   N  NE  . ARG A 1 64  ? 6.538   -12.453 5.603   1.00 19.40 ? 56   ARG A NE  1 
ATOM   424   C  CZ  . ARG A 1 64  ? 6.551   -13.609 4.947   1.00 19.68 ? 56   ARG A CZ  1 
ATOM   425   N  NH1 . ARG A 1 64  ? 6.536   -13.621 3.624   1.00 20.53 ? 56   ARG A NH1 1 
ATOM   426   N  NH2 . ARG A 1 64  ? 6.591   -14.756 5.610   1.00 17.56 ? 56   ARG A NH2 1 
ATOM   427   N  N   . PHE A 1 65  ? 4.477   -6.197  4.958   1.00 16.23 ? 57   PHE A N   1 
ATOM   428   C  CA  . PHE A 1 65  ? 4.267   -4.786  5.240   1.00 12.67 ? 57   PHE A CA  1 
ATOM   429   C  C   . PHE A 1 65  ? 4.282   -4.545  6.743   1.00 13.18 ? 57   PHE A C   1 
ATOM   430   O  O   . PHE A 1 65  ? 3.673   -5.300  7.508   1.00 14.07 ? 57   PHE A O   1 
ATOM   431   C  CB  . PHE A 1 65  ? 2.944   -4.300  4.646   1.00 12.19 ? 57   PHE A CB  1 
ATOM   432   C  CG  . PHE A 1 65  ? 2.616   -2.868  4.976   1.00 15.90 ? 57   PHE A CG  1 
ATOM   433   C  CD1 . PHE A 1 65  ? 3.304   -1.825  4.375   1.00 15.52 ? 57   PHE A CD1 1 
ATOM   434   C  CD2 . PHE A 1 65  ? 1.604   -2.564  5.872   1.00 16.26 ? 57   PHE A CD2 1 
ATOM   435   C  CE1 . PHE A 1 65  ? 2.994   -0.504  4.668   1.00 15.65 ? 57   PHE A CE1 1 
ATOM   436   C  CE2 . PHE A 1 65  ? 1.288   -1.252  6.163   1.00 13.62 ? 57   PHE A CE2 1 
ATOM   437   C  CZ  . PHE A 1 65  ? 1.988   -0.214  5.555   1.00 13.25 ? 57   PHE A CZ  1 
ATOM   438   N  N   . VAL A 1 66  ? 4.971   -3.483  7.164   1.00 13.56 ? 58   VAL A N   1 
ATOM   439   C  CA  . VAL A 1 66  ? 5.023   -3.080  8.563   1.00 13.99 ? 58   VAL A CA  1 
ATOM   440   C  C   . VAL A 1 66  ? 4.651   -1.609  8.665   1.00 17.16 ? 58   VAL A C   1 
ATOM   441   O  O   . VAL A 1 66  ? 5.340   -0.745  8.104   1.00 14.95 ? 58   VAL A O   1 
ATOM   442   C  CB  . VAL A 1 66  ? 6.410   -3.318  9.192   1.00 15.17 ? 58   VAL A CB  1 
ATOM   443   C  CG1 . VAL A 1 66  ? 6.450   -2.749  10.618  1.00 19.22 ? 58   VAL A CG1 1 
ATOM   444   C  CG2 . VAL A 1 66  ? 6.729   -4.788  9.211   1.00 17.60 ? 58   VAL A CG2 1 
ATOM   445   N  N   . LEU A 1 67  ? 3.582   -1.327  9.402   1.00 14.26 ? 59   LEU A N   1 
ATOM   446   C  CA  . LEU A 1 67  ? 3.212   0.029   9.797   1.00 14.15 ? 59   LEU A CA  1 
ATOM   447   C  C   . LEU A 1 67  ? 3.889   0.312   11.133  1.00 15.07 ? 59   LEU A C   1 
ATOM   448   O  O   . LEU A 1 67  ? 3.350   -0.002  12.196  1.00 18.99 ? 59   LEU A O   1 
ATOM   449   C  CB  . LEU A 1 67  ? 1.697   0.158   9.902   1.00 18.39 ? 59   LEU A CB  1 
ATOM   450   C  CG  . LEU A 1 67  ? 1.168   1.512   10.365  1.00 20.82 ? 59   LEU A CG  1 
ATOM   451   C  CD1 . LEU A 1 67  ? 1.360   2.530   9.256   1.00 19.94 ? 59   LEU A CD1 1 
ATOM   452   C  CD2 . LEU A 1 67  ? -0.305  1.419   10.809  1.00 21.45 ? 59   LEU A CD2 1 
ATOM   453   N  N   . SER A 1 68  ? 5.102   0.890   11.078  1.00 18.55 ? 60   SER A N   1 
ATOM   454   C  CA  . SER A 1 68  ? 5.894   1.107   12.293  1.00 18.50 ? 60   SER A CA  1 
ATOM   455   C  C   . SER A 1 68  ? 5.237   2.115   13.224  1.00 28.76 ? 60   SER A C   1 
ATOM   456   O  O   . SER A 1 68  ? 5.314   1.975   14.452  1.00 30.98 ? 60   SER A O   1 
ATOM   457   C  CB  . SER A 1 68  ? 7.312   1.568   11.933  1.00 19.16 ? 60   SER A CB  1 
ATOM   458   O  OG  . SER A 1 68  ? 8.150   1.646   13.084  1.00 29.73 ? 60   SER A OG  1 
ATOM   459   N  N   . ASN A 1 69  ? 4.605   3.150   12.670  1.00 25.19 ? 61   ASN A N   1 
ATOM   460   C  CA  . ASN A 1 69  ? 3.901   4.136   13.494  1.00 28.04 ? 61   ASN A CA  1 
ATOM   461   C  C   . ASN A 1 69  ? 2.488   3.623   13.775  1.00 32.52 ? 61   ASN A C   1 
ATOM   462   O  O   . ASN A 1 69  ? 1.486   4.130   13.269  1.00 33.59 ? 61   ASN A O   1 
ATOM   463   C  CB  . ASN A 1 69  ? 3.904   5.506   12.823  1.00 30.86 ? 61   ASN A CB  1 
ATOM   464   C  CG  . ASN A 1 69  ? 3.807   5.437   11.299  1.00 36.71 ? 61   ASN A CG  1 
ATOM   465   O  OD1 . ASN A 1 69  ? 3.734   4.362   10.705  1.00 37.57 ? 61   ASN A OD1 1 
ATOM   466   N  ND2 . ASN A 1 69  ? 3.810   6.605   10.660  1.00 38.54 ? 61   ASN A ND2 1 
ATOM   467   N  N   . GLY A 1 70  ? 2.436   2.581   14.612  1.00 32.51 ? 62   GLY A N   1 
ATOM   468   C  CA  . GLY A 1 70  ? 1.230   1.789   14.807  1.00 32.01 ? 62   GLY A CA  1 
ATOM   469   C  C   . GLY A 1 70  ? 0.020   2.558   15.298  1.00 30.41 ? 62   GLY A C   1 
ATOM   470   O  O   . GLY A 1 70  ? -1.096  2.033   15.236  1.00 27.46 ? 62   GLY A O   1 
ATOM   471   N  N   . HIS A 1 71  ? 0.213   3.783   15.794  1.00 24.81 ? 63   HIS A N   1 
ATOM   472   C  CA  . HIS A 1 71  ? -0.921  4.631   16.156  1.00 29.43 ? 63   HIS A CA  1 
ATOM   473   C  C   . HIS A 1 71  ? -1.825  4.920   14.958  1.00 31.39 ? 63   HIS A C   1 
ATOM   474   O  O   . HIS A 1 71  ? -3.040  5.064   15.123  1.00 31.24 ? 63   HIS A O   1 
ATOM   475   C  CB  . HIS A 1 71  ? -0.422  5.937   16.767  1.00 33.90 ? 63   HIS A CB  1 
ATOM   476   C  CG  . HIS A 1 71  ? 0.644   6.607   15.962  1.00 40.43 ? 63   HIS A CG  1 
ATOM   477   N  ND1 . HIS A 1 71  ? 0.372   7.587   15.032  1.00 44.12 ? 63   HIS A ND1 1 
ATOM   478   C  CD2 . HIS A 1 71  ? 1.987   6.426   15.938  1.00 43.40 ? 63   HIS A CD2 1 
ATOM   479   C  CE1 . HIS A 1 71  ? 1.501   7.984   14.473  1.00 45.84 ? 63   HIS A CE1 1 
ATOM   480   N  NE2 . HIS A 1 71  ? 2.497   7.298   15.008  1.00 46.63 ? 63   HIS A NE2 1 
ATOM   481   N  N   . ALA A 1 72  ? -1.253  5.007   13.754  1.00 26.42 ? 64   ALA A N   1 
ATOM   482   C  CA  . ALA A 1 72  ? -1.995  5.204   12.508  1.00 20.58 ? 64   ALA A CA  1 
ATOM   483   C  C   . ALA A 1 72  ? -2.742  3.940   12.077  1.00 15.77 ? 64   ALA A C   1 
ATOM   484   O  O   . ALA A 1 72  ? -2.906  3.671   10.878  1.00 15.71 ? 64   ALA A O   1 
ATOM   485   C  CB  . ALA A 1 72  ? -1.026  5.651   11.406  1.00 23.38 ? 64   ALA A CB  1 
ATOM   486   N  N   . SER A 1 73  ? -3.203  3.156   13.050  1.00 15.16 ? 65   SER A N   1 
ATOM   487   C  CA  . SER A 1 73  ? -3.680  1.805   12.767  1.00 12.53 ? 65   SER A CA  1 
ATOM   488   C  C   . SER A 1 73  ? -4.842  1.782   11.787  1.00 12.35 ? 65   SER A C   1 
ATOM   489   O  O   . SER A 1 73  ? -5.006  0.800   11.058  1.00 15.17 ? 65   SER A O   1 
ATOM   490   C  CB  . SER A 1 73  ? -4.114  1.124   14.060  1.00 23.98 ? 65   SER A CB  1 
ATOM   491   O  OG  . SER A 1 73  ? -5.126  1.883   14.684  1.00 23.48 ? 65   SER A OG  1 
ATOM   492   N  N   . MET A 1 74  ? -5.689  2.815   11.780  1.00 16.77 ? 66   MET A N   1 
ATOM   493   C  CA  . MET A 1 74  ? -6.820  2.774   10.853  1.00 16.97 ? 66   MET A CA  1 
ATOM   494   C  C   . MET A 1 74  ? -6.359  2.730   9.404   1.00 18.79 ? 66   MET A C   1 
ATOM   495   O  O   . MET A 1 74  ? -7.101  2.245   8.541   1.00 15.40 ? 66   MET A O   1 
ATOM   496   C  CB  . MET A 1 74  ? -7.751  3.969   11.061  1.00 15.90 ? 66   MET A CB  1 
ATOM   497   C  CG  . MET A 1 74  ? -8.903  3.709   12.050  1.00 17.24 ? 66   MET A CG  1 
ATOM   498   S  SD  . MET A 1 74  ? -9.814  2.164   11.772  1.00 18.07 ? 66   MET A SD  1 
ATOM   499   C  CE  . MET A 1 74  ? -10.325 2.349   10.076  1.00 14.30 ? 66   MET A CE  1 
ATOM   500   N  N   . LEU A 1 75  ? -5.152  3.217   9.119   1.00 15.49 ? 67   LEU A N   1 
ATOM   501   C  CA  . LEU A 1 75  ? -4.617  3.099   7.769   1.00 17.51 ? 67   LEU A CA  1 
ATOM   502   C  C   . LEU A 1 75  ? -4.511  1.634   7.366   1.00 19.53 ? 67   LEU A C   1 
ATOM   503   O  O   . LEU A 1 75  ? -4.908  1.246   6.258   1.00 14.91 ? 67   LEU A O   1 
ATOM   504   C  CB  . LEU A 1 75  ? -3.252  3.786   7.688   1.00 16.81 ? 67   LEU A CB  1 
ATOM   505   C  CG  . LEU A 1 75  ? -2.600  3.884   6.305   1.00 22.17 ? 67   LEU A CG  1 
ATOM   506   C  CD1 . LEU A 1 75  ? -3.354  4.848   5.433   1.00 26.24 ? 67   LEU A CD1 1 
ATOM   507   C  CD2 . LEU A 1 75  ? -1.164  4.347   6.440   1.00 27.90 ? 67   LEU A CD2 1 
ATOM   508   N  N   . LEU A 1 76  ? -3.983  0.804   8.269   1.00 15.11 ? 68   LEU A N   1 
ATOM   509   C  CA  . LEU A 1 76  ? -3.836  -0.618  7.989   1.00 15.04 ? 68   LEU A CA  1 
ATOM   510   C  C   . LEU A 1 76  ? -5.185  -1.319  7.980   1.00 12.91 ? 68   LEU A C   1 
ATOM   511   O  O   . LEU A 1 76  ? -5.464  -2.135  7.091   1.00 15.29 ? 68   LEU A O   1 
ATOM   512   C  CB  . LEU A 1 76  ? -2.902  -1.258  9.024   1.00 12.61 ? 68   LEU A CB  1 
ATOM   513   C  CG  . LEU A 1 76  ? -2.644  -2.752  8.833   1.00 13.49 ? 68   LEU A CG  1 
ATOM   514   C  CD1 . LEU A 1 76  ? -2.184  -3.046  7.403   1.00 16.11 ? 68   LEU A CD1 1 
ATOM   515   C  CD2 . LEU A 1 76  ? -1.606  -3.222  9.829   1.00 12.25 ? 68   LEU A CD2 1 
ATOM   516   N  N   . TYR A 1 77  ? -6.043  -1.019  8.960   1.00 13.47 ? 69   TYR A N   1 
ATOM   517   C  CA  . TYR A 1 77  ? -7.375  -1.621  8.960   1.00 14.22 ? 69   TYR A CA  1 
ATOM   518   C  C   . TYR A 1 77  ? -8.131  -1.310  7.674   1.00 15.17 ? 69   TYR A C   1 
ATOM   519   O  O   . TYR A 1 77  ? -8.805  -2.184  7.123   1.00 13.34 ? 69   TYR A O   1 
ATOM   520   C  CB  . TYR A 1 77  ? -8.170  -1.151  10.175  1.00 12.15 ? 69   TYR A CB  1 
ATOM   521   C  CG  . TYR A 1 77  ? -7.601  -1.619  11.500  1.00 14.54 ? 69   TYR A CG  1 
ATOM   522   C  CD1 . TYR A 1 77  ? -6.894  -2.816  11.596  1.00 20.12 ? 69   TYR A CD1 1 
ATOM   523   C  CD2 . TYR A 1 77  ? -7.774  -0.863  12.656  1.00 14.10 ? 69   TYR A CD2 1 
ATOM   524   C  CE1 . TYR A 1 77  ? -6.369  -3.248  12.824  1.00 21.13 ? 69   TYR A CE1 1 
ATOM   525   C  CE2 . TYR A 1 77  ? -7.259  -1.291  13.891  1.00 12.75 ? 69   TYR A CE2 1 
ATOM   526   C  CZ  . TYR A 1 77  ? -6.553  -2.473  13.963  1.00 18.49 ? 69   TYR A CZ  1 
ATOM   527   O  OH  . TYR A 1 77  ? -6.049  -2.895  15.182  1.00 19.49 ? 69   TYR A OH  1 
ATOM   528   N  N   . SER A 1 78  ? -8.052  -0.065  7.198   1.00 13.21 ? 70   SER A N   1 
ATOM   529   C  CA  . SER A 1 78  ? -8.702  0.304   5.940   1.00 18.08 ? 70   SER A CA  1 
ATOM   530   C  C   . SER A 1 78  ? -8.174  -0.523  4.776   1.00 17.23 ? 70   SER A C   1 
ATOM   531   O  O   . SER A 1 78  ? -8.949  -1.007  3.941   1.00 16.93 ? 70   SER A O   1 
ATOM   532   C  CB  . SER A 1 78  ? -8.501  1.793   5.664   1.00 17.89 ? 70   SER A CB  1 
ATOM   533   O  OG  . SER A 1 78  ? -9.099  2.577   6.676   1.00 19.98 ? 70   SER A OG  1 
ATOM   534   N  N   . LEU A 1 79  ? -6.849  -0.677  4.697   1.00 14.50 ? 71   LEU A N   1 
ATOM   535   C  CA  . LEU A 1 79  ? -6.245  -1.433  3.603   1.00 15.55 ? 71   LEU A CA  1 
ATOM   536   C  C   . LEU A 1 79  ? -6.667  -2.899  3.634   1.00 15.98 ? 71   LEU A C   1 
ATOM   537   O  O   . LEU A 1 79  ? -6.991  -3.481  2.591   1.00 18.43 ? 71   LEU A O   1 
ATOM   538   C  CB  . LEU A 1 79  ? -4.724  -1.309  3.667   1.00 14.42 ? 71   LEU A CB  1 
ATOM   539   C  CG  . LEU A 1 79  ? -4.173  0.068   3.278   1.00 15.89 ? 71   LEU A CG  1 
ATOM   540   C  CD1 . LEU A 1 79  ? -2.764  0.257   3.815   1.00 16.32 ? 71   LEU A CD1 1 
ATOM   541   C  CD2 . LEU A 1 79  ? -4.168  0.211   1.755   1.00 21.61 ? 71   LEU A CD2 1 
ATOM   542   N  N   . LEU A 1 80  ? -6.680  -3.512  4.822   1.00 16.84 ? 72   LEU A N   1 
ATOM   543   C  CA  . LEU A 1 80  ? -7.107  -4.906  4.924   1.00 17.24 ? 72   LEU A CA  1 
ATOM   544   C  C   . LEU A 1 80  ? -8.565  -5.060  4.510   1.00 14.56 ? 72   LEU A C   1 
ATOM   545   O  O   . LEU A 1 80  ? -8.918  -5.975  3.751   1.00 18.81 ? 72   LEU A O   1 
ATOM   546   C  CB  . LEU A 1 80  ? -6.890  -5.416  6.352   1.00 13.29 ? 72   LEU A CB  1 
ATOM   547   C  CG  . LEU A 1 80  ? -5.439  -5.418  6.834   1.00 15.63 ? 72   LEU A CG  1 
ATOM   548   C  CD1 . LEU A 1 80  ? -5.374  -5.784  8.319   1.00 14.53 ? 72   LEU A CD1 1 
ATOM   549   C  CD2 . LEU A 1 80  ? -4.606  -6.389  6.007   1.00 15.22 ? 72   LEU A CD2 1 
ATOM   550   N  N   . HIS A 1 81  ? -9.427  -4.164  4.988   1.00 14.70 ? 73   HIS A N   1 
ATOM   551   C  CA  . HIS A 1 81  ? -10.837 -4.227  4.616   1.00 18.52 ? 73   HIS A CA  1 
ATOM   552   C  C   . HIS A 1 81  ? -11.030 -4.071  3.108   1.00 21.16 ? 73   HIS A C   1 
ATOM   553   O  O   . HIS A 1 81  ? -11.741 -4.860  2.473   1.00 18.40 ? 73   HIS A O   1 
ATOM   554   C  CB  . HIS A 1 81  ? -11.618 -3.152  5.361   1.00 19.51 ? 73   HIS A CB  1 
ATOM   555   C  CG  . HIS A 1 81  ? -13.043 -3.051  4.925   1.00 19.76 ? 73   HIS A CG  1 
ATOM   556   N  ND1 . HIS A 1 81  ? -13.948 -4.074  5.108   1.00 20.06 ? 73   HIS A ND1 1 
ATOM   557   C  CD2 . HIS A 1 81  ? -13.709 -2.070  4.270   1.00 20.52 ? 73   HIS A CD2 1 
ATOM   558   C  CE1 . HIS A 1 81  ? -15.118 -3.716  4.609   1.00 23.65 ? 73   HIS A CE1 1 
ATOM   559   N  NE2 . HIS A 1 81  ? -14.999 -2.505  4.093   1.00 23.53 ? 73   HIS A NE2 1 
ATOM   560   N  N   . LEU A 1 82  ? -10.414 -3.044  2.518   1.00 21.79 ? 74   LEU A N   1 
ATOM   561   C  CA  . LEU A 1 82  ? -10.648 -2.747  1.104   1.00 23.22 ? 74   LEU A CA  1 
ATOM   562   C  C   . LEU A 1 82  ? -10.108 -3.838  0.184   1.00 22.63 ? 74   LEU A C   1 
ATOM   563   O  O   . LEU A 1 82  ? -10.709 -4.114  -0.867  1.00 19.28 ? 74   LEU A O   1 
ATOM   564   C  CB  . LEU A 1 82  ? -10.015 -1.404  0.740   1.00 17.64 ? 74   LEU A CB  1 
ATOM   565   C  CG  . LEU A 1 82  ? -10.694 -0.151  1.294   1.00 29.29 ? 74   LEU A CG  1 
ATOM   566   C  CD1 . LEU A 1 82  ? -9.733  1.027   1.254   1.00 30.67 ? 74   LEU A CD1 1 
ATOM   567   C  CD2 . LEU A 1 82  ? -11.952 0.156   0.502   1.00 28.96 ? 74   LEU A CD2 1 
ATOM   568   N  N   . THR A 1 83  ? -8.988  -4.464  0.546   1.00 20.37 ? 75   THR A N   1 
ATOM   569   C  CA  . THR A 1 83  ? -8.395  -5.455  -0.345  1.00 21.02 ? 75   THR A CA  1 
ATOM   570   C  C   . THR A 1 83  ? -9.001  -6.842  -0.184  1.00 22.75 ? 75   THR A C   1 
ATOM   571   O  O   . THR A 1 83  ? -8.689  -7.724  -0.985  1.00 22.26 ? 75   THR A O   1 
ATOM   572   C  CB  . THR A 1 83  ? -6.874  -5.530  -0.151  1.00 18.70 ? 75   THR A CB  1 
ATOM   573   O  OG1 . THR A 1 83  ? -6.551  -5.866  1.214   1.00 17.80 ? 75   THR A OG1 1 
ATOM   574   C  CG2 . THR A 1 83  ? -6.238  -4.202  -0.532  1.00 15.17 ? 75   THR A CG2 1 
ATOM   575   N  N   . GLY A 1 84  ? -9.850  -7.057  0.820   1.00 23.64 ? 76   GLY A N   1 
ATOM   576   C  CA  . GLY A 1 84  ? -10.653 -8.259  0.896   1.00 26.45 ? 76   GLY A CA  1 
ATOM   577   C  C   . GLY A 1 84  ? -10.339 -9.209  2.027   1.00 26.07 ? 76   GLY A C   1 
ATOM   578   O  O   . GLY A 1 84  ? -10.830 -10.344 2.007   1.00 24.48 ? 76   GLY A O   1 
ATOM   579   N  N   . TYR A 1 85  ? -9.542  -8.794  3.010   1.00 19.42 ? 77   TYR A N   1 
ATOM   580   C  CA  . TYR A 1 85  ? -9.306  -9.625  4.180   1.00 21.35 ? 77   TYR A CA  1 
ATOM   581   C  C   . TYR A 1 85  ? -10.586 -9.735  5.009   1.00 24.01 ? 77   TYR A C   1 
ATOM   582   O  O   . TYR A 1 85  ? -11.575 -9.033  4.772   1.00 24.92 ? 77   TYR A O   1 
ATOM   583   C  CB  . TYR A 1 85  ? -8.152  -9.056  5.012   1.00 18.59 ? 77   TYR A CB  1 
ATOM   584   C  CG  . TYR A 1 85  ? -6.808  -9.224  4.343   1.00 17.34 ? 77   TYR A CG  1 
ATOM   585   C  CD1 . TYR A 1 85  ? -6.393  -8.351  3.346   1.00 15.22 ? 77   TYR A CD1 1 
ATOM   586   C  CD2 . TYR A 1 85  ? -5.961  -10.275 4.697   1.00 18.24 ? 77   TYR A CD2 1 
ATOM   587   C  CE1 . TYR A 1 85  ? -5.169  -8.511  2.720   1.00 16.59 ? 77   TYR A CE1 1 
ATOM   588   C  CE2 . TYR A 1 85  ? -4.731  -10.438 4.089   1.00 18.82 ? 77   TYR A CE2 1 
ATOM   589   C  CZ  . TYR A 1 85  ? -4.344  -9.560  3.092   1.00 22.15 ? 77   TYR A CZ  1 
ATOM   590   O  OH  . TYR A 1 85  ? -3.122  -9.733  2.481   1.00 26.46 ? 77   TYR A OH  1 
ATOM   591   N  N   . ASN A 1 86  ? -10.562 -10.635 6.000   1.00 23.38 ? 78   ASN A N   1 
ATOM   592   C  CA  . ASN A 1 86  ? -11.729 -10.911 6.849   1.00 25.52 ? 78   ASN A CA  1 
ATOM   593   C  C   . ASN A 1 86  ? -11.825 -9.842  7.940   1.00 26.58 ? 78   ASN A C   1 
ATOM   594   O  O   . ASN A 1 86  ? -11.662 -10.096 9.135   1.00 20.70 ? 78   ASN A O   1 
ATOM   595   C  CB  . ASN A 1 86  ? -11.640 -12.312 7.447   1.00 26.82 ? 78   ASN A CB  1 
ATOM   596   C  CG  . ASN A 1 86  ? -12.915 -12.725 8.159   1.00 40.95 ? 78   ASN A CG  1 
ATOM   597   O  OD1 . ASN A 1 86  ? -13.999 -12.231 7.849   1.00 45.17 ? 78   ASN A OD1 1 
ATOM   598   N  ND2 . ASN A 1 86  ? -12.792 -13.636 9.122   1.00 39.55 ? 78   ASN A ND2 1 
ATOM   599   N  N   . LEU A 1 87  ? -12.087 -8.616  7.492   1.00 21.31 ? 79   LEU A N   1 
ATOM   600   C  CA  . LEU A 1 87  ? -12.230 -7.452  8.362   1.00 18.20 ? 79   LEU A CA  1 
ATOM   601   C  C   . LEU A 1 87  ? -13.317 -6.592  7.733   1.00 24.79 ? 79   LEU A C   1 
ATOM   602   O  O   . LEU A 1 87  ? -13.139 -6.106  6.612   1.00 23.85 ? 79   LEU A O   1 
ATOM   603   C  CB  . LEU A 1 87  ? -10.909 -6.688  8.477   1.00 19.43 ? 79   LEU A CB  1 
ATOM   604   C  CG  . LEU A 1 87  ? -10.747 -5.687  9.619   1.00 20.01 ? 79   LEU A CG  1 
ATOM   605   C  CD1 . LEU A 1 87  ? -10.848 -6.413  10.957  1.00 18.86 ? 79   LEU A CD1 1 
ATOM   606   C  CD2 . LEU A 1 87  ? -9.392  -4.962  9.496   1.00 15.53 ? 79   LEU A CD2 1 
ATOM   607   N  N   . SER A 1 88  ? -14.438 -6.421  8.433   1.00 22.97 ? 80   SER A N   1 
ATOM   608   C  CA  . SER A 1 88  ? -15.655 -5.864  7.851   1.00 22.61 ? 80   SER A CA  1 
ATOM   609   C  C   . SER A 1 88  ? -15.857 -4.401  8.240   1.00 20.56 ? 80   SER A C   1 
ATOM   610   O  O   . SER A 1 88  ? -15.174 -3.858  9.107   1.00 19.46 ? 80   SER A O   1 
ATOM   611   C  CB  . SER A 1 88  ? -16.877 -6.665  8.301   1.00 26.01 ? 80   SER A CB  1 
ATOM   612   O  OG  . SER A 1 88  ? -17.118 -6.417  9.674   1.00 21.96 ? 80   SER A OG  1 
ATOM   613   N  N   . ILE A 1 89  ? -16.843 -3.768  7.596   1.00 27.26 ? 81   ILE A N   1 
ATOM   614   C  CA  . ILE A 1 89  ? -17.203 -2.406  7.980   1.00 26.28 ? 81   ILE A CA  1 
ATOM   615   C  C   . ILE A 1 89  ? -17.603 -2.360  9.451   1.00 23.81 ? 81   ILE A C   1 
ATOM   616   O  O   . ILE A 1 89  ? -17.224 -1.436  10.179  1.00 24.30 ? 81   ILE A O   1 
ATOM   617   C  CB  . ILE A 1 89  ? -18.317 -1.854  7.068   1.00 26.15 ? 81   ILE A CB  1 
ATOM   618   C  CG1 . ILE A 1 89  ? -17.755 -1.434  5.715   1.00 28.71 ? 81   ILE A CG1 1 
ATOM   619   C  CG2 . ILE A 1 89  ? -18.977 -0.651  7.708   1.00 32.08 ? 81   ILE A CG2 1 
ATOM   620   C  CD1 . ILE A 1 89  ? -16.769 -0.271  5.800   1.00 31.68 ? 81   ILE A CD1 1 
ATOM   621   N  N   . GLU A 1 90  ? -18.374 -3.356  9.910   1.00 23.34 ? 82   GLU A N   1 
ATOM   622   C  CA  A GLU A 1 90  ? -18.774 -3.379  11.314  0.52 23.54 ? 82   GLU A CA  1 
ATOM   623   C  CA  B GLU A 1 90  ? -18.775 -3.393  11.315  0.48 23.57 ? 82   GLU A CA  1 
ATOM   624   C  C   . GLU A 1 90  ? -17.560 -3.471  12.228  1.00 20.92 ? 82   GLU A C   1 
ATOM   625   O  O   . GLU A 1 90  ? -17.527 -2.835  13.288  1.00 22.46 ? 82   GLU A O   1 
ATOM   626   C  CB  A GLU A 1 90  ? -19.742 -4.534  11.576  0.52 26.74 ? 82   GLU A CB  1 
ATOM   627   C  CB  B GLU A 1 90  ? -19.711 -4.576  11.567  0.48 26.80 ? 82   GLU A CB  1 
ATOM   628   C  CG  A GLU A 1 90  ? -21.100 -4.349  10.921  0.52 34.03 ? 82   GLU A CG  1 
ATOM   629   C  CG  B GLU A 1 90  ? -20.186 -4.689  13.004  0.48 28.27 ? 82   GLU A CG  1 
ATOM   630   C  CD  A GLU A 1 90  ? -21.784 -3.064  11.346  0.52 41.15 ? 82   GLU A CD  1 
ATOM   631   C  CD  B GLU A 1 90  ? -21.130 -3.565  13.397  0.48 38.97 ? 82   GLU A CD  1 
ATOM   632   O  OE1 A GLU A 1 90  ? -21.917 -2.830  12.567  0.52 41.71 ? 82   GLU A OE1 1 
ATOM   633   O  OE1 B GLU A 1 90  ? -21.837 -3.044  12.508  0.48 40.65 ? 82   GLU A OE1 1 
ATOM   634   O  OE2 A GLU A 1 90  ? -22.184 -2.282  10.456  0.52 43.18 ? 82   GLU A OE2 1 
ATOM   635   O  OE2 B GLU A 1 90  ? -21.164 -3.200  14.592  0.48 40.42 ? 82   GLU A OE2 1 
ATOM   636   N  N   . ASP A 1 91  ? -16.544 -4.241  11.826  1.00 23.29 ? 83   ASP A N   1 
ATOM   637   C  CA  . ASP A 1 91  ? -15.287 -4.253  12.568  1.00 19.42 ? 83   ASP A CA  1 
ATOM   638   C  C   . ASP A 1 91  ? -14.681 -2.857  12.632  1.00 22.05 ? 83   ASP A C   1 
ATOM   639   O  O   . ASP A 1 91  ? -14.247 -2.408  13.700  1.00 18.78 ? 83   ASP A O   1 
ATOM   640   C  CB  . ASP A 1 91  ? -14.303 -5.229  11.927  1.00 19.25 ? 83   ASP A CB  1 
ATOM   641   C  CG  . ASP A 1 91  ? -14.725 -6.672  12.088  1.00 24.40 ? 83   ASP A CG  1 
ATOM   642   O  OD1 . ASP A 1 91  ? -15.448 -6.982  13.055  1.00 25.12 ? 83   ASP A OD1 1 
ATOM   643   O  OD2 . ASP A 1 91  ? -14.326 -7.502  11.249  1.00 25.94 ? 83   ASP A OD2 1 
ATOM   644   N  N   . LEU A 1 92  ? -14.659 -2.142  11.504  1.00 18.03 ? 84   LEU A N   1 
ATOM   645   C  CA  . LEU A 1 92  ? -14.108 -0.784  11.533  1.00 19.79 ? 84   LEU A CA  1 
ATOM   646   C  C   . LEU A 1 92  ? -14.958 0.139   12.385  1.00 20.01 ? 84   LEU A C   1 
ATOM   647   O  O   . LEU A 1 92  ? -14.429 1.061   13.017  1.00 20.51 ? 84   LEU A O   1 
ATOM   648   C  CB  . LEU A 1 92  ? -13.986 -0.211  10.124  1.00 18.32 ? 84   LEU A CB  1 
ATOM   649   C  CG  . LEU A 1 92  ? -13.200 -1.068  9.139   1.00 22.17 ? 84   LEU A CG  1 
ATOM   650   C  CD1 . LEU A 1 92  ? -13.046 -0.335  7.825   1.00 24.55 ? 84   LEU A CD1 1 
ATOM   651   C  CD2 . LEU A 1 92  ? -11.866 -1.417  9.708   1.00 20.93 ? 84   LEU A CD2 1 
ATOM   652   N  N   . LYS A 1 93  ? -16.272 -0.093  12.416  1.00 20.29 ? 85   LYS A N   1 
ATOM   653   C  CA  . LYS A 1 93  ? -17.149 0.676   13.290  1.00 21.35 ? 85   LYS A CA  1 
ATOM   654   C  C   . LYS A 1 93  ? -16.905 0.384   14.761  1.00 22.45 ? 85   LYS A C   1 
ATOM   655   O  O   . LYS A 1 93  ? -17.435 1.104   15.614  1.00 17.72 ? 85   LYS A O   1 
ATOM   656   C  CB  . LYS A 1 93  ? -18.617 0.394   12.953  1.00 22.97 ? 85   LYS A CB  1 
ATOM   657   C  CG  . LYS A 1 93  ? -19.087 0.977   11.645  1.00 25.45 ? 85   LYS A CG  1 
ATOM   658   C  CD  . LYS A 1 93  ? -20.590 0.745   11.476  1.00 29.56 ? 85   LYS A CD  1 
ATOM   659   C  CE  . LYS A 1 93  ? -21.109 1.353   10.184  1.00 32.65 ? 85   LYS A CE  1 
ATOM   660   N  NZ  . LYS A 1 93  ? -22.464 0.820   9.821   1.00 36.71 ? 85   LYS A NZ  1 
ATOM   661   N  N   . ASN A 1 94  ? -16.125 -0.654  15.073  1.00 19.37 ? 86   ASN A N   1 
ATOM   662   C  CA  . ASN A 1 94  ? -15.832 -1.045  16.443  1.00 18.57 ? 86   ASN A CA  1 
ATOM   663   C  C   . ASN A 1 94  ? -14.384 -0.742  16.811  1.00 17.37 ? 86   ASN A C   1 
ATOM   664   O  O   . ASN A 1 94  ? -13.847 -1.340  17.749  1.00 15.72 ? 86   ASN A O   1 
ATOM   665   C  CB  . ASN A 1 94  ? -16.147 -2.527  16.644  1.00 17.93 ? 86   ASN A CB  1 
ATOM   666   C  CG  . ASN A 1 94  ? -17.643 -2.803  16.650  1.00 35.76 ? 86   ASN A CG  1 
ATOM   667   O  OD1 . ASN A 1 94  ? -18.434 -1.936  17.016  1.00 38.77 ? 86   ASN A OD1 1 
ATOM   668   N  ND2 . ASN A 1 94  ? -18.034 -4.010  16.245  1.00 38.81 ? 86   ASN A ND2 1 
ATOM   669   N  N   . PHE A 1 95  ? -13.752 0.170   16.072  1.00 14.36 ? 87   PHE A N   1 
ATOM   670   C  CA  . PHE A 1 95  ? -12.388 0.608   16.353  1.00 13.67 ? 87   PHE A CA  1 
ATOM   671   C  C   . PHE A 1 95  ? -12.236 0.985   17.822  1.00 14.24 ? 87   PHE A C   1 
ATOM   672   O  O   . PHE A 1 95  ? -13.015 1.781   18.353  1.00 14.50 ? 87   PHE A O   1 
ATOM   673   C  CB  . PHE A 1 95  ? -12.059 1.800   15.448  1.00 16.20 ? 87   PHE A CB  1 
ATOM   674   C  CG  . PHE A 1 95  ? -10.656 2.331   15.597  1.00 15.32 ? 87   PHE A CG  1 
ATOM   675   C  CD1 . PHE A 1 95  ? -9.556  1.492   15.469  1.00 16.50 ? 87   PHE A CD1 1 
ATOM   676   C  CD2 . PHE A 1 95  ? -10.444 3.679   15.817  1.00 15.83 ? 87   PHE A CD2 1 
ATOM   677   C  CE1 . PHE A 1 95  ? -8.243  1.992   15.579  1.00 12.68 ? 87   PHE A CE1 1 
ATOM   678   C  CE2 . PHE A 1 95  ? -9.151  4.189   15.923  1.00 18.99 ? 87   PHE A CE2 1 
ATOM   679   C  CZ  . PHE A 1 95  ? -8.050  3.335   15.800  1.00 17.85 ? 87   PHE A CZ  1 
ATOM   680   N  N   . ARG A 1 96  ? -11.254 0.367   18.489  1.00 13.51 ? 88   ARG A N   1 
ATOM   681   C  CA  . ARG A 1 96  ? -10.886 0.675   19.871  1.00 15.91 ? 88   ARG A CA  1 
ATOM   682   C  C   . ARG A 1 96  ? -11.955 0.273   20.877  1.00 18.55 ? 88   ARG A C   1 
ATOM   683   O  O   . ARG A 1 96  ? -11.953 0.772   22.006  1.00 17.88 ? 88   ARG A O   1 
ATOM   684   C  CB  . ARG A 1 96  ? -10.545 2.163   20.044  1.00 16.89 ? 88   ARG A CB  1 
ATOM   685   C  CG  . ARG A 1 96  ? -9.226  2.553   19.391  1.00 16.25 ? 88   ARG A CG  1 
ATOM   686   C  CD  . ARG A 1 96  ? -8.895  4.056   19.447  1.00 16.92 ? 88   ARG A CD  1 
ATOM   687   N  NE  . ARG A 1 96  ? -7.482  4.240   19.092  1.00 21.65 ? 88   ARG A NE  1 
ATOM   688   C  CZ  . ARG A 1 96  ? -6.514  4.573   19.952  1.00 22.12 ? 88   ARG A CZ  1 
ATOM   689   N  NH1 . ARG A 1 96  ? -6.797  4.822   21.218  1.00 23.69 ? 88   ARG A NH1 1 
ATOM   690   N  NH2 . ARG A 1 96  ? -5.255  4.668   19.539  1.00 23.95 ? 88   ARG A NH2 1 
ATOM   691   N  N   . GLN A 1 97  ? -12.857 -0.636  20.516  1.00 16.79 ? 89   GLN A N   1 
ATOM   692   C  CA  . GLN A 1 97  ? -13.911 -1.069  21.424  1.00 17.32 ? 89   GLN A CA  1 
ATOM   693   C  C   . GLN A 1 97  ? -13.572 -2.438  21.992  1.00 16.89 ? 89   GLN A C   1 
ATOM   694   O  O   . GLN A 1 97  ? -12.848 -3.223  21.373  1.00 15.71 ? 89   GLN A O   1 
ATOM   695   C  CB  . GLN A 1 97  ? -15.262 -1.103  20.711  1.00 20.31 ? 89   GLN A CB  1 
ATOM   696   C  CG  . GLN A 1 97  ? -15.643 0.246   20.094  1.00 21.76 ? 89   GLN A CG  1 
ATOM   697   C  CD  . GLN A 1 97  ? -15.422 1.407   21.056  1.00 24.37 ? 89   GLN A CD  1 
ATOM   698   O  OE1 . GLN A 1 97  ? -16.013 1.460   22.135  1.00 20.66 ? 89   GLN A OE1 1 
ATOM   699   N  NE2 . GLN A 1 97  ? -14.553 2.330   20.676  1.00 23.63 ? 89   GLN A NE2 1 
ATOM   700   N  N   . LEU A 1 98  ? -14.079 -2.708  23.191  1.00 16.83 ? 90   LEU A N   1 
ATOM   701   C  CA  . LEU A 1 98  ? -13.703 -3.916  23.914  1.00 23.16 ? 90   LEU A CA  1 
ATOM   702   C  C   . LEU A 1 98  ? -13.923 -5.166  23.073  1.00 26.74 ? 90   LEU A C   1 
ATOM   703   O  O   . LEU A 1 98  ? -15.038 -5.420  22.602  1.00 19.36 ? 90   LEU A O   1 
ATOM   704   C  CB  . LEU A 1 98  ? -14.498 -4.011  25.216  1.00 18.83 ? 90   LEU A CB  1 
ATOM   705   C  CG  . LEU A 1 98  ? -14.078 -5.167  26.130  1.00 20.06 ? 90   LEU A CG  1 
ATOM   706   C  CD1 . LEU A 1 98  ? -12.590 -5.111  26.456  1.00 19.83 ? 90   LEU A CD1 1 
ATOM   707   C  CD2 . LEU A 1 98  ? -14.889 -5.136  27.393  1.00 21.30 ? 90   LEU A CD2 1 
ATOM   708   N  N   . HIS A 1 99  ? -12.838 -5.922  22.873  1.00 17.98 ? 91   HIS A N   1 
ATOM   709   C  CA  . HIS A 1 99  ? -12.804 -7.222  22.201  1.00 18.53 ? 91   HIS A CA  1 
ATOM   710   C  C   . HIS A 1 99  ? -13.100 -7.141  20.709  1.00 22.34 ? 91   HIS A C   1 
ATOM   711   O  O   . HIS A 1 99  ? -13.393 -8.166  20.086  1.00 22.23 ? 91   HIS A O   1 
ATOM   712   C  CB  . HIS A 1 99  ? -13.751 -8.230  22.864  1.00 20.24 ? 91   HIS A CB  1 
ATOM   713   C  CG  . HIS A 1 99  ? -13.408 -8.522  24.291  1.00 22.23 ? 91   HIS A CG  1 
ATOM   714   N  ND1 . HIS A 1 99  ? -14.362 -8.694  25.271  1.00 25.69 ? 91   HIS A ND1 1 
ATOM   715   C  CD2 . HIS A 1 99  ? -12.209 -8.661  24.903  1.00 23.67 ? 91   HIS A CD2 1 
ATOM   716   C  CE1 . HIS A 1 99  ? -13.766 -8.926  26.425  1.00 26.07 ? 91   HIS A CE1 1 
ATOM   717   N  NE2 . HIS A 1 99  ? -12.459 -8.910  26.229  1.00 23.88 ? 91   HIS A NE2 1 
ATOM   718   N  N   . SER A 1 100 ? -13.006 -5.960  20.106  1.00 21.15 ? 92   SER A N   1 
ATOM   719   C  CA  . SER A 1 100 ? -13.246 -5.842  18.674  1.00 20.43 ? 92   SER A CA  1 
ATOM   720   C  C   . SER A 1 100 ? -12.031 -6.332  17.887  1.00 21.55 ? 92   SER A C   1 
ATOM   721   O  O   . SER A 1 100 ? -10.939 -6.504  18.424  1.00 20.39 ? 92   SER A O   1 
ATOM   722   C  CB  . SER A 1 100 ? -13.570 -4.400  18.302  1.00 17.34 ? 92   SER A CB  1 
ATOM   723   O  OG  . SER A 1 100 ? -12.394 -3.631  18.126  1.00 19.11 ? 92   SER A OG  1 
ATOM   724   N  N   . LYS A 1 101 ? -12.226 -6.555  16.584  1.00 21.76 ? 93   LYS A N   1 
ATOM   725   C  CA  . LYS A 1 101 ? -11.123 -6.966  15.728  1.00 21.62 ? 93   LYS A CA  1 
ATOM   726   C  C   . LYS A 1 101 ? -10.236 -5.796  15.327  1.00 17.88 ? 93   LYS A C   1 
ATOM   727   O  O   . LYS A 1 101 ? -9.289  -5.977  14.556  1.00 20.30 ? 93   LYS A O   1 
ATOM   728   C  CB  . LYS A 1 101 ? -11.666 -7.680  14.485  1.00 29.50 ? 93   LYS A CB  1 
ATOM   729   C  CG  . LYS A 1 101 ? -12.328 -9.020  14.798  1.00 31.67 ? 93   LYS A CG  1 
ATOM   730   C  CD  . LYS A 1 101 ? -13.100 -9.532  13.596  1.00 41.90 ? 93   LYS A CD  1 
ATOM   731   C  CE  . LYS A 1 101 ? -13.341 -11.024 13.672  1.00 48.36 ? 93   LYS A CE  1 
ATOM   732   N  NZ  . LYS A 1 101 ? -13.766 -11.555 12.344  1.00 52.82 ? 93   LYS A NZ  1 
ATOM   733   N  N   . THR A 1 102 ? -10.485 -4.609  15.867  1.00 15.82 ? 94   THR A N   1 
ATOM   734   C  CA  . THR A 1 102 ? -9.756  -3.402  15.485  1.00 14.56 ? 94   THR A CA  1 
ATOM   735   C  C   . THR A 1 102 ? -9.266  -2.658  16.720  1.00 17.16 ? 94   THR A C   1 
ATOM   736   O  O   . THR A 1 102 ? -9.689  -1.530  16.983  1.00 17.17 ? 94   THR A O   1 
ATOM   737   C  CB  . THR A 1 102 ? -10.661 -2.509  14.643  1.00 15.76 ? 94   THR A CB  1 
ATOM   738   O  OG1 . THR A 1 102 ? -11.951 -2.465  15.272  1.00 16.88 ? 94   THR A OG1 1 
ATOM   739   C  CG2 . THR A 1 102 ? -10.797 -3.071  13.242  1.00 14.39 ? 94   THR A CG2 1 
ATOM   740   N  N   . PRO A 1 103 ? -8.377  -3.263  17.510  1.00 17.21 ? 95   PRO A N   1 
ATOM   741   C  CA  . PRO A 1 103 ? -7.816  -2.537  18.656  1.00 18.68 ? 95   PRO A CA  1 
ATOM   742   C  C   . PRO A 1 103 ? -7.007  -1.330  18.205  1.00 15.75 ? 95   PRO A C   1 
ATOM   743   O  O   . PRO A 1 103 ? -6.592  -1.215  17.050  1.00 14.03 ? 95   PRO A O   1 
ATOM   744   C  CB  . PRO A 1 103 ? -6.931  -3.587  19.351  1.00 17.73 ? 95   PRO A CB  1 
ATOM   745   C  CG  . PRO A 1 103 ? -6.568  -4.554  18.256  1.00 14.08 ? 95   PRO A CG  1 
ATOM   746   C  CD  . PRO A 1 103 ? -7.812  -4.622  17.395  1.00 14.23 ? 95   PRO A CD  1 
ATOM   747   N  N   . GLY A 1 104 ? -6.758  -0.430  19.155  1.00 15.08 ? 96   GLY A N   1 
ATOM   748   C  CA  . GLY A 1 104 ? -6.193  0.864   18.814  1.00 16.85 ? 96   GLY A CA  1 
ATOM   749   C  C   . GLY A 1 104 ? -4.824  0.789   18.176  1.00 21.11 ? 96   GLY A C   1 
ATOM   750   O  O   . GLY A 1 104 ? -4.468  1.650   17.370  1.00 19.47 ? 96   GLY A O   1 
ATOM   751   N  N   . HIS A 1 105 ? -4.039  -0.225  18.531  1.00 15.07 ? 97   HIS A N   1 
ATOM   752   C  CA  . HIS A 1 105 ? -2.838  -0.547  17.786  1.00 14.20 ? 97   HIS A CA  1 
ATOM   753   C  C   . HIS A 1 105 ? -2.980  -1.941  17.193  1.00 19.36 ? 97   HIS A C   1 
ATOM   754   O  O   . HIS A 1 105 ? -3.540  -2.828  17.846  1.00 18.86 ? 97   HIS A O   1 
ATOM   755   C  CB  . HIS A 1 105 ? -1.596  -0.481  18.693  1.00 18.88 ? 97   HIS A CB  1 
ATOM   756   C  CG  . HIS A 1 105 ? -1.384  0.864   19.306  1.00 22.87 ? 97   HIS A CG  1 
ATOM   757   N  ND1 . HIS A 1 105 ? -1.060  1.036   20.632  1.00 30.35 ? 97   HIS A ND1 1 
ATOM   758   C  CD2 . HIS A 1 105 ? -1.457  2.105   18.772  1.00 29.64 ? 97   HIS A CD2 1 
ATOM   759   C  CE1 . HIS A 1 105 ? -0.954  2.327   20.892  1.00 32.15 ? 97   HIS A CE1 1 
ATOM   760   N  NE2 . HIS A 1 105 ? -1.187  2.997   19.780  1.00 25.39 ? 97   HIS A NE2 1 
ATOM   761   N  N   . PRO A 1 106 ? -2.518  -2.164  15.961  1.00 19.83 ? 98   PRO A N   1 
ATOM   762   C  CA  . PRO A 1 106 ? -2.759  -3.459  15.318  1.00 18.12 ? 98   PRO A CA  1 
ATOM   763   C  C   . PRO A 1 106 ? -2.062  -4.572  16.085  1.00 15.81 ? 98   PRO A C   1 
ATOM   764   O  O   . PRO A 1 106 ? -0.950  -4.404  16.584  1.00 18.92 ? 98   PRO A O   1 
ATOM   765   C  CB  . PRO A 1 106 ? -2.165  -3.279  13.912  1.00 19.79 ? 98   PRO A CB  1 
ATOM   766   C  CG  . PRO A 1 106 ? -1.984  -1.800  13.741  1.00 24.60 ? 98   PRO A CG  1 
ATOM   767   C  CD  . PRO A 1 106 ? -1.696  -1.282  15.118  1.00 25.03 ? 98   PRO A CD  1 
ATOM   768   N  N   . GLU A 1 107 ? -2.734  -5.713  16.190  1.00 17.63 ? 99   GLU A N   1 
ATOM   769   C  CA  . GLU A 1 107 ? -2.261  -6.813  17.022  1.00 15.37 ? 99   GLU A CA  1 
ATOM   770   C  C   . GLU A 1 107 ? -2.022  -8.036  16.155  1.00 20.03 ? 99   GLU A C   1 
ATOM   771   O  O   . GLU A 1 107 ? -2.959  -8.571  15.548  1.00 20.55 ? 99   GLU A O   1 
ATOM   772   C  CB  . GLU A 1 107 ? -3.260  -7.124  18.140  1.00 17.13 ? 99   GLU A CB  1 
ATOM   773   C  CG  . GLU A 1 107 ? -3.224  -6.069  19.214  1.00 14.63 ? 99   GLU A CG  1 
ATOM   774   C  CD  . GLU A 1 107 ? -4.182  -6.342  20.352  1.00 17.23 ? 99   GLU A CD  1 
ATOM   775   O  OE1 . GLU A 1 107 ? -4.713  -7.464  20.437  1.00 21.48 ? 99   GLU A OE1 1 
ATOM   776   O  OE2 . GLU A 1 107 ? -4.403  -5.416  21.151  1.00 18.08 ? 99   GLU A OE2 1 
ATOM   777   N  N   . TYR A 1 108 ? -0.766  -8.459  16.095  1.00 18.79 ? 100  TYR A N   1 
ATOM   778   C  CA  . TYR A 1 108 ? -0.415  -9.692  15.416  1.00 14.64 ? 100  TYR A CA  1 
ATOM   779   C  C   . TYR A 1 108 ? -1.145  -10.870 16.042  1.00 18.37 ? 100  TYR A C   1 
ATOM   780   O  O   . TYR A 1 108 ? -1.267  -10.962 17.270  1.00 17.42 ? 100  TYR A O   1 
ATOM   781   C  CB  . TYR A 1 108 ? 1.094   -9.923  15.499  1.00 15.01 ? 100  TYR A CB  1 
ATOM   782   C  CG  . TYR A 1 108 ? 1.513   -11.281 14.998  1.00 15.75 ? 100  TYR A CG  1 
ATOM   783   C  CD1 . TYR A 1 108 ? 1.583   -11.535 13.644  1.00 15.17 ? 100  TYR A CD1 1 
ATOM   784   C  CD2 . TYR A 1 108 ? 1.816   -12.318 15.883  1.00 16.94 ? 100  TYR A CD2 1 
ATOM   785   C  CE1 . TYR A 1 108 ? 1.945   -12.771 13.167  1.00 20.17 ? 100  TYR A CE1 1 
ATOM   786   C  CE2 . TYR A 1 108 ? 2.182   -13.566 15.413  1.00 21.24 ? 100  TYR A CE2 1 
ATOM   787   C  CZ  . TYR A 1 108 ? 2.249   -13.780 14.048  1.00 26.12 ? 100  TYR A CZ  1 
ATOM   788   O  OH  . TYR A 1 108 ? 2.609   -15.007 13.538  1.00 36.84 ? 100  TYR A OH  1 
ATOM   789   N  N   . GLY A 1 109 ? -1.586  -11.801 15.184  1.00 19.25 ? 101  GLY A N   1 
ATOM   790   C  CA  . GLY A 1 109 ? -2.217  -13.027 15.611  1.00 23.71 ? 101  GLY A CA  1 
ATOM   791   C  C   . GLY A 1 109 ? -3.698  -12.898 15.863  1.00 28.37 ? 101  GLY A C   1 
ATOM   792   O  O   . GLY A 1 109 ? -4.405  -13.909 15.903  1.00 30.70 ? 101  GLY A O   1 
ATOM   793   N  N   . TYR A 1 110 ? -4.178  -11.678 16.029  1.00 28.78 ? 102  TYR A N   1 
ATOM   794   C  CA  . TYR A 1 110 ? -5.580  -11.397 16.265  1.00 31.03 ? 102  TYR A CA  1 
ATOM   795   C  C   . TYR A 1 110 ? -6.313  -11.072 14.970  1.00 30.38 ? 102  TYR A C   1 
ATOM   796   O  O   . TYR A 1 110 ? -7.414  -11.573 14.728  1.00 36.70 ? 102  TYR A O   1 
ATOM   797   C  CB  . TYR A 1 110 ? -5.684  -10.235 17.251  1.00 31.96 ? 102  TYR A CB  1 
ATOM   798   C  CG  . TYR A 1 110 ? -7.069  -10.012 17.764  1.00 34.96 ? 102  TYR A CG  1 
ATOM   799   C  CD1 . TYR A 1 110 ? -7.803  -11.059 18.303  1.00 43.03 ? 102  TYR A CD1 1 
ATOM   800   C  CD2 . TYR A 1 110 ? -7.648  -8.758  17.720  1.00 35.50 ? 102  TYR A CD2 1 
ATOM   801   C  CE1 . TYR A 1 110 ? -9.083  -10.862 18.776  1.00 45.92 ? 102  TYR A CE1 1 
ATOM   802   C  CE2 . TYR A 1 110 ? -8.917  -8.552  18.193  1.00 37.31 ? 102  TYR A CE2 1 
ATOM   803   C  CZ  . TYR A 1 110 ? -9.634  -9.604  18.720  1.00 43.26 ? 102  TYR A CZ  1 
ATOM   804   O  OH  . TYR A 1 110 ? -10.906 -9.396  19.195  1.00 47.34 ? 102  TYR A OH  1 
ATOM   805   N  N   . THR A 1 111 ? -5.687  -10.272 14.117  1.00 22.56 ? 103  THR A N   1 
ATOM   806   C  CA  . THR A 1 111 ? -6.299  -9.729  12.914  1.00 22.06 ? 103  THR A CA  1 
ATOM   807   C  C   . THR A 1 111 ? -5.528  -10.263 11.717  1.00 19.55 ? 103  THR A C   1 
ATOM   808   O  O   . THR A 1 111 ? -4.306  -10.095 11.645  1.00 19.07 ? 103  THR A O   1 
ATOM   809   C  CB  . THR A 1 111 ? -6.255  -8.199  12.965  1.00 23.15 ? 103  THR A CB  1 
ATOM   810   O  OG1 . THR A 1 111 ? -6.910  -7.750  14.161  1.00 25.57 ? 103  THR A OG1 1 
ATOM   811   C  CG2 . THR A 1 111 ? -6.903  -7.561  11.723  1.00 19.16 ? 103  THR A CG2 1 
ATOM   812   N  N   . ASP A 1 112 ? -6.236  -10.907 10.786  1.00 23.18 ? 104  ASP A N   1 
ATOM   813   C  CA  . ASP A 1 112 ? -5.593  -11.421 9.580   1.00 22.59 ? 104  ASP A CA  1 
ATOM   814   C  C   . ASP A 1 112 ? -4.873  -10.307 8.835   1.00 17.07 ? 104  ASP A C   1 
ATOM   815   O  O   . ASP A 1 112 ? -5.412  -9.214  8.651   1.00 18.57 ? 104  ASP A O   1 
ATOM   816   C  CB  . ASP A 1 112 ? -6.625  -12.054 8.641   1.00 26.01 ? 104  ASP A CB  1 
ATOM   817   C  CG  . ASP A 1 112 ? -7.078  -13.426 9.095   1.00 29.66 ? 104  ASP A CG  1 
ATOM   818   O  OD1 . ASP A 1 112 ? -6.546  -13.946 10.093  1.00 29.05 ? 104  ASP A OD1 1 
ATOM   819   O  OD2 . ASP A 1 112 ? -7.981  -13.984 8.434   1.00 33.80 ? 104  ASP A OD2 1 
ATOM   820   N  N   . GLY A 1 113 ? -3.654  -10.597 8.374   1.00 21.56 ? 105  GLY A N   1 
ATOM   821   C  CA  . GLY A 1 113 ? -2.909  -9.654  7.572   1.00 19.81 ? 105  GLY A CA  1 
ATOM   822   C  C   . GLY A 1 113 ? -2.007  -8.719  8.351   1.00 22.19 ? 105  GLY A C   1 
ATOM   823   O  O   . GLY A 1 113 ? -1.165  -8.049  7.742   1.00 20.30 ? 105  GLY A O   1 
ATOM   824   N  N   . VAL A 1 114 ? -2.163  -8.637  9.669   1.00 14.32 ? 106  VAL A N   1 
ATOM   825   C  CA  . VAL A 1 114 ? -1.253  -7.847  10.494  1.00 13.97 ? 106  VAL A CA  1 
ATOM   826   C  C   . VAL A 1 114 ? 0.006   -8.666  10.756  1.00 21.03 ? 106  VAL A C   1 
ATOM   827   O  O   . VAL A 1 114 ? -0.066  -9.763  11.318  1.00 21.55 ? 106  VAL A O   1 
ATOM   828   C  CB  . VAL A 1 114 ? -1.921  -7.437  11.813  1.00 14.46 ? 106  VAL A CB  1 
ATOM   829   C  CG1 . VAL A 1 114 ? -0.908  -6.703  12.698  1.00 12.75 ? 106  VAL A CG1 1 
ATOM   830   C  CG2 . VAL A 1 114 ? -3.165  -6.592  11.534  1.00 18.06 ? 106  VAL A CG2 1 
ATOM   831   N  N   . GLU A 1 115 ? 1.169   -8.122  10.373  1.00 13.68 ? 107  GLU A N   1 
ATOM   832   C  CA  . GLU A 1 115 ? 2.419   -8.875  10.440  1.00 13.49 ? 107  GLU A CA  1 
ATOM   833   C  C   . GLU A 1 115 ? 3.139   -8.736  11.776  1.00 14.78 ? 107  GLU A C   1 
ATOM   834   O  O   . GLU A 1 115 ? 4.012   -9.555  12.081  1.00 12.32 ? 107  GLU A O   1 
ATOM   835   C  CB  . GLU A 1 115 ? 3.372   -8.433  9.319   1.00 14.95 ? 107  GLU A CB  1 
ATOM   836   C  CG  . GLU A 1 115 ? 2.801   -8.569  7.903   1.00 12.42 ? 107  GLU A CG  1 
ATOM   837   C  CD  . GLU A 1 115 ? 2.624   -10.013 7.445   1.00 18.59 ? 107  GLU A CD  1 
ATOM   838   O  OE1 . GLU A 1 115 ? 2.022   -10.203 6.369   1.00 17.45 ? 107  GLU A OE1 1 
ATOM   839   O  OE2 . GLU A 1 115 ? 3.070   -10.959 8.144   1.00 16.12 ? 107  GLU A OE2 1 
ATOM   840   N  N   . THR A 1 116 ? 2.811   -7.716  12.563  1.00 13.73 ? 108  THR A N   1 
ATOM   841   C  CA  . THR A 1 116 ? 3.500   -7.472  13.825  1.00 12.59 ? 108  THR A CA  1 
ATOM   842   C  C   . THR A 1 116 ? 2.658   -6.492  14.621  1.00 14.94 ? 108  THR A C   1 
ATOM   843   O  O   . THR A 1 116 ? 1.849   -5.753  14.055  1.00 14.11 ? 108  THR A O   1 
ATOM   844   C  CB  . THR A 1 116 ? 4.923   -6.928  13.614  1.00 13.35 ? 108  THR A CB  1 
ATOM   845   O  OG1 . THR A 1 116 ? 5.526   -6.654  14.889  1.00 11.48 ? 108  THR A OG1 1 
ATOM   846   C  CG2 . THR A 1 116 ? 4.901   -5.668  12.788  1.00 17.71 ? 108  THR A CG2 1 
ATOM   847   N  N   . THR A 1 117 ? 2.811   -6.535  15.938  1.00 15.15 ? 109  THR A N   1 
ATOM   848   C  CA  . THR A 1 117 ? 2.107   -5.614  16.814  1.00 14.45 ? 109  THR A CA  1 
ATOM   849   C  C   . THR A 1 117 ? 2.999   -4.400  17.017  1.00 13.10 ? 109  THR A C   1 
ATOM   850   O  O   . THR A 1 117 ? 4.120   -4.529  17.519  1.00 11.50 ? 109  THR A O   1 
ATOM   851   C  CB  . THR A 1 117 ? 1.773   -6.271  18.151  1.00 14.63 ? 109  THR A CB  1 
ATOM   852   O  OG1 . THR A 1 117 ? 0.956   -7.420  17.923  1.00 14.55 ? 109  THR A OG1 1 
ATOM   853   C  CG2 . THR A 1 117 ? 1.035   -5.300  19.067  1.00 16.36 ? 109  THR A CG2 1 
ATOM   854   N  N   . THR A 1 118 ? 2.529   -3.236  16.588  1.00 13.53 ? 110  THR A N   1 
ATOM   855   C  CA  . THR A 1 118 ? 3.295   -2.017  16.769  1.00 15.69 ? 110  THR A CA  1 
ATOM   856   C  C   . THR A 1 118 ? 2.467   -1.029  17.570  1.00 19.29 ? 110  THR A C   1 
ATOM   857   O  O   . THR A 1 118 ? 1.238   -1.090  17.602  1.00 30.80 ? 110  THR A O   1 
ATOM   858   C  CB  . THR A 1 118 ? 3.727   -1.387  15.430  1.00 16.95 ? 110  THR A CB  1 
ATOM   859   O  OG1 . THR A 1 118 ? 2.572   -1.053  14.663  1.00 19.13 ? 110  THR A OG1 1 
ATOM   860   C  CG2 . THR A 1 118 ? 4.589   -2.359  14.618  1.00 22.70 ? 110  THR A CG2 1 
ATOM   861   N  N   . GLY A 1 119 ? 3.177   -0.107  18.193  1.00 22.54 ? 111  GLY A N   1 
ATOM   862   C  CA  . GLY A 1 119 ? 2.625   0.880   19.088  1.00 23.59 ? 111  GLY A CA  1 
ATOM   863   C  C   . GLY A 1 119 ? 3.796   1.634   19.682  1.00 19.64 ? 111  GLY A C   1 
ATOM   864   O  O   . GLY A 1 119 ? 4.044   2.795   19.357  1.00 22.37 ? 111  GLY A O   1 
ATOM   865   N  N   . PRO A 1 120 ? 4.568   0.959   20.536  1.00 16.55 ? 112  PRO A N   1 
ATOM   866   C  CA  . PRO A 1 120 ? 5.832   1.537   21.016  1.00 13.17 ? 112  PRO A CA  1 
ATOM   867   C  C   . PRO A 1 120 ? 6.721   1.858   19.826  1.00 17.83 ? 112  PRO A C   1 
ATOM   868   O  O   . PRO A 1 120 ? 7.063   0.979   19.033  1.00 16.11 ? 112  PRO A O   1 
ATOM   869   C  CB  . PRO A 1 120 ? 6.427   0.419   21.879  1.00 15.90 ? 112  PRO A CB  1 
ATOM   870   C  CG  . PRO A 1 120 ? 5.229   -0.414  22.291  1.00 24.07 ? 112  PRO A CG  1 
ATOM   871   C  CD  . PRO A 1 120 ? 4.321   -0.379  21.105  1.00 23.34 ? 112  PRO A CD  1 
ATOM   872   N  N   . LEU A 1 121 ? 7.085   3.130   19.703  1.00 11.75 ? 113  LEU A N   1 
ATOM   873   C  CA  . LEU A 1 121 ? 7.747   3.623   18.500  1.00 10.90 ? 113  LEU A CA  1 
ATOM   874   C  C   . LEU A 1 121 ? 9.178   3.104   18.383  1.00 14.01 ? 113  LEU A C   1 
ATOM   875   O  O   . LEU A 1 121 ? 9.832   2.784   19.377  1.00 12.28 ? 113  LEU A O   1 
ATOM   876   C  CB  . LEU A 1 121 ? 7.736   5.150   18.502  1.00 15.79 ? 113  LEU A CB  1 
ATOM   877   C  CG  . LEU A 1 121 ? 6.323   5.741   18.488  1.00 18.07 ? 113  LEU A CG  1 
ATOM   878   C  CD1 . LEU A 1 121 ? 6.368   7.254   18.552  1.00 23.28 ? 113  LEU A CD1 1 
ATOM   879   C  CD2 . LEU A 1 121 ? 5.560   5.274   17.253  1.00 20.64 ? 113  LEU A CD2 1 
ATOM   880   N  N   . GLY A 1 122 ? 9.658   3.026   17.139  1.00 11.50 ? 114  GLY A N   1 
ATOM   881   C  CA  . GLY A 1 122 ? 10.974  2.519   16.818  1.00 12.78 ? 114  GLY A CA  1 
ATOM   882   C  C   . GLY A 1 122 ? 11.046  1.019   16.609  1.00 13.25 ? 114  GLY A C   1 
ATOM   883   O  O   . GLY A 1 122 ? 11.859  0.554   15.807  1.00 12.72 ? 114  GLY A O   1 
ATOM   884   N  N   . GLN A 1 123 ? 10.220  0.236   17.310  1.00 12.97 ? 115  GLN A N   1 
ATOM   885   C  CA  . GLN A 1 123 ? 10.382  -1.206  17.184  1.00 13.89 ? 115  GLN A CA  1 
ATOM   886   C  C   . GLN A 1 123 ? 9.842   -1.749  15.869  1.00 12.48 ? 115  GLN A C   1 
ATOM   887   O  O   . GLN A 1 123 ? 10.279  -2.819  15.438  1.00 16.13 ? 115  GLN A O   1 
ATOM   888   C  CB  . GLN A 1 123 ? 9.723   -1.929  18.362  1.00 10.03 ? 115  GLN A CB  1 
ATOM   889   C  CG  . GLN A 1 123 ? 10.436  -1.631  19.683  1.00 10.20 ? 115  GLN A CG  1 
ATOM   890   C  CD  . GLN A 1 123 ? 9.838   -2.394  20.839  1.00 12.44 ? 115  GLN A CD  1 
ATOM   891   O  OE1 . GLN A 1 123 ? 9.866   -3.620  20.863  1.00 12.22 ? 115  GLN A OE1 1 
ATOM   892   N  NE2 . GLN A 1 123 ? 9.293   -1.671  21.803  1.00 11.68 ? 115  GLN A NE2 1 
ATOM   893   N  N   . GLY A 1 124 ? 8.913   -1.045  15.221  1.00 12.78 ? 116  GLY A N   1 
ATOM   894   C  CA  . GLY A 1 124 ? 8.380   -1.549  13.966  1.00 12.55 ? 116  GLY A CA  1 
ATOM   895   C  C   . GLY A 1 124 ? 9.449   -1.697  12.900  1.00 12.52 ? 116  GLY A C   1 
ATOM   896   O  O   . GLY A 1 124 ? 9.543   -2.732  12.236  1.00 11.00 ? 116  GLY A O   1 
ATOM   897   N  N   . ILE A 1 125 ? 10.282  -0.663  12.727  1.00 10.35 ? 117  ILE A N   1 
ATOM   898   C  CA  . ILE A 1 125 ? 11.343  -0.760  11.729  1.00 13.31 ? 117  ILE A CA  1 
ATOM   899   C  C   . ILE A 1 125 ? 12.330  -1.859  12.111  1.00 11.42 ? 117  ILE A C   1 
ATOM   900   O  O   . ILE A 1 125 ? 12.822  -2.598  11.249  1.00 10.49 ? 117  ILE A O   1 
ATOM   901   C  CB  . ILE A 1 125 ? 12.029  0.612   11.524  1.00 13.72 ? 117  ILE A CB  1 
ATOM   902   C  CG1 . ILE A 1 125 ? 13.187  0.497   10.539  1.00 11.87 ? 117  ILE A CG1 1 
ATOM   903   C  CG2 . ILE A 1 125 ? 12.538  1.181   12.830  1.00 14.84 ? 117  ILE A CG2 1 
ATOM   904   C  CD1 . ILE A 1 125 ? 12.787  0.017   9.145   1.00 11.66 ? 117  ILE A CD1 1 
ATOM   905   N  N   . ALA A 1 126 ? 12.584  -2.033  13.412  1.00 12.75 ? 118  ALA A N   1 
ATOM   906   C  CA  . ALA A 1 126 ? 13.450  -3.125  13.846  1.00 11.55 ? 118  ALA A CA  1 
ATOM   907   C  C   . ALA A 1 126 ? 12.826  -4.486  13.548  1.00 12.75 ? 118  ALA A C   1 
ATOM   908   O  O   . ALA A 1 126 ? 13.514  -5.390  13.064  1.00 11.41 ? 118  ALA A O   1 
ATOM   909   C  CB  . ALA A 1 126 ? 13.761  -2.981  15.335  1.00 14.61 ? 118  ALA A CB  1 
ATOM   910   N  N   . ASN A 1 127 ? 11.521  -4.646  13.808  1.00 11.89 ? 119  ASN A N   1 
ATOM   911   C  CA  . ASN A 1 127 ? 10.818  -5.860  13.388  1.00 15.11 ? 119  ASN A CA  1 
ATOM   912   C  C   . ASN A 1 127 ? 11.000  -6.101  11.890  1.00 11.30 ? 119  ASN A C   1 
ATOM   913   O  O   . ASN A 1 127 ? 11.254  -7.231  11.446  1.00 11.52 ? 119  ASN A O   1 
ATOM   914   C  CB  . ASN A 1 127 ? 9.311   -5.760  13.683  1.00 14.62 ? 119  ASN A CB  1 
ATOM   915   C  CG  . ASN A 1 127 ? 8.965   -5.619  15.168  1.00 13.02 ? 119  ASN A CG  1 
ATOM   916   O  OD1 . ASN A 1 127 ? 7.841   -5.225  15.500  1.00 15.97 ? 119  ASN A OD1 1 
ATOM   917   N  ND2 . ASN A 1 127 ? 9.891   -5.965  16.054  1.00 11.18 ? 119  ASN A ND2 1 
ATOM   918   N  N   . ALA A 1 128 ? 10.862  -5.042  11.095  1.00 10.60 ? 120  ALA A N   1 
ATOM   919   C  CA  . ALA A 1 128 ? 10.954  -5.196  9.648   1.00 11.98 ? 120  ALA A CA  1 
ATOM   920   C  C   . ALA A 1 128 ? 12.349  -5.620  9.232   1.00 14.05 ? 120  ALA A C   1 
ATOM   921   O  O   . ALA A 1 128 ? 12.497  -6.460  8.343   1.00 12.60 ? 120  ALA A O   1 
ATOM   922   C  CB  . ALA A 1 128 ? 10.550  -3.902  8.960   1.00 13.19 ? 120  ALA A CB  1 
ATOM   923   N  N   . VAL A 1 129 ? 13.383  -5.058  9.877   1.00 12.50 ? 121  VAL A N   1 
ATOM   924   C  CA  . VAL A 1 129 ? 14.760  -5.484  9.626   1.00 10.41 ? 121  VAL A CA  1 
ATOM   925   C  C   . VAL A 1 129 ? 14.906  -6.982  9.864   1.00 13.83 ? 121  VAL A C   1 
ATOM   926   O  O   . VAL A 1 129 ? 15.544  -7.694  9.078   1.00 14.38 ? 121  VAL A O   1 
ATOM   927   C  CB  . VAL A 1 129 ? 15.744  -4.669  10.497  1.00 12.27 ? 121  VAL A CB  1 
ATOM   928   C  CG1 . VAL A 1 129 ? 17.168  -5.298  10.483  1.00 12.62 ? 121  VAL A CG1 1 
ATOM   929   C  CG2 . VAL A 1 129 ? 15.797  -3.216  10.030  1.00 11.64 ? 121  VAL A CG2 1 
ATOM   930   N  N   . GLY A 1 130 ? 14.325  -7.479  10.959  1.00 11.62 ? 122  GLY A N   1 
ATOM   931   C  CA  . GLY A 1 130 ? 14.302  -8.915  11.199  1.00 11.97 ? 122  GLY A CA  1 
ATOM   932   C  C   . GLY A 1 130 ? 13.572  -9.694  10.116  1.00 11.01 ? 122  GLY A C   1 
ATOM   933   O  O   . GLY A 1 130 ? 14.022  -10.763 9.704   1.00 12.21 ? 122  GLY A O   1 
ATOM   934   N  N   . MET A 1 131 ? 12.449  -9.170  9.628   1.00 10.45 ? 123  MET A N   1 
ATOM   935   C  CA  . MET A 1 131 ? 11.745  -9.885  8.558   1.00 11.67 ? 123  MET A CA  1 
ATOM   936   C  C   . MET A 1 131 ? 12.568  -9.902  7.273   1.00 14.01 ? 123  MET A C   1 
ATOM   937   O  O   . MET A 1 131 ? 12.603  -10.916 6.557   1.00 14.14 ? 123  MET A O   1 
ATOM   938   C  CB  . MET A 1 131 ? 10.371  -9.257  8.300   1.00 15.97 ? 123  MET A CB  1 
ATOM   939   C  CG  . MET A 1 131 ? 9.361   -9.448  9.449   1.00 14.85 ? 123  MET A CG  1 
ATOM   940   S  SD  . MET A 1 131 ? 7.931   -8.408  9.159   1.00 15.36 ? 123  MET A SD  1 
ATOM   941   C  CE  . MET A 1 131 ? 7.177   -8.399  10.791  1.00 10.95 ? 123  MET A CE  1 
ATOM   942   N  N   . ALA A 1 132 ? 13.233  -8.787  6.962   1.00 13.45 ? 124  ALA A N   1 
ATOM   943   C  CA  . ALA A 1 132 ? 14.086  -8.742  5.780   1.00 16.22 ? 124  ALA A CA  1 
ATOM   944   C  C   . ALA A 1 132 ? 15.303  -9.631  5.960   1.00 14.70 ? 124  ALA A C   1 
ATOM   945   O  O   . ALA A 1 132 ? 15.762  -10.270 5.009   1.00 15.17 ? 124  ALA A O   1 
ATOM   946   C  CB  . ALA A 1 132 ? 14.513  -7.302  5.492   1.00 13.61 ? 124  ALA A CB  1 
ATOM   947   N  N   . LEU A 1 133 ? 15.833  -9.683  7.181   1.00 14.34 ? 125  LEU A N   1 
ATOM   948   C  CA  . LEU A 1 133 ? 16.952  -10.565 7.473   1.00 16.37 ? 125  LEU A CA  1 
ATOM   949   C  C   . LEU A 1 133 ? 16.556  -12.027 7.305   1.00 14.70 ? 125  LEU A C   1 
ATOM   950   O  O   . LEU A 1 133 ? 17.311  -12.816 6.729   1.00 14.60 ? 125  LEU A O   1 
ATOM   951   C  CB  . LEU A 1 133 ? 17.458  -10.292 8.890   1.00 18.44 ? 125  LEU A CB  1 
ATOM   952   C  CG  . LEU A 1 133 ? 18.835  -10.763 9.309   1.00 26.57 ? 125  LEU A CG  1 
ATOM   953   C  CD1 . LEU A 1 133 ? 19.837  -10.547 8.183   1.00 23.68 ? 125  LEU A CD1 1 
ATOM   954   C  CD2 . LEU A 1 133 ? 19.234  -9.980  10.559  1.00 28.82 ? 125  LEU A CD2 1 
ATOM   955   N  N   . ALA A 1 134 ? 15.373  -12.407 7.800   1.00 15.13 ? 126  ALA A N   1 
ATOM   956   C  CA  . ALA A 1 134 ? 14.896  -13.774 7.599   1.00 13.72 ? 126  ALA A CA  1 
ATOM   957   C  C   . ALA A 1 134 ? 14.775  -14.118 6.116   1.00 15.82 ? 126  ALA A C   1 
ATOM   958   O  O   . ALA A 1 134 ? 15.187  -15.204 5.692   1.00 15.43 ? 126  ALA A O   1 
ATOM   959   C  CB  . ALA A 1 134 ? 13.551  -13.971 8.300   1.00 17.76 ? 126  ALA A CB  1 
ATOM   960   N  N   . GLU A 1 135 ? 14.206  -13.209 5.314   1.00 12.66 ? 127  GLU A N   1 
ATOM   961   C  CA  . GLU A 1 135 ? 14.087  -13.457 3.877   1.00 14.42 ? 127  GLU A CA  1 
ATOM   962   C  C   . GLU A 1 135 ? 15.458  -13.674 3.255   1.00 14.47 ? 127  GLU A C   1 
ATOM   963   O  O   . GLU A 1 135 ? 15.643  -14.581 2.439   1.00 15.93 ? 127  GLU A O   1 
ATOM   964   C  CB  . GLU A 1 135 ? 13.356  -12.290 3.186   1.00 12.99 ? 127  GLU A CB  1 
ATOM   965   C  CG  . GLU A 1 135 ? 12.879  -12.593 1.736   1.00 13.62 ? 127  GLU A CG  1 
ATOM   966   C  CD  . GLU A 1 135 ? 13.887  -12.225 0.664   1.00 17.28 ? 127  GLU A CD  1 
ATOM   967   O  OE1 . GLU A 1 135 ? 13.631  -12.524 -0.527  1.00 17.64 ? 127  GLU A OE1 1 
ATOM   968   O  OE2 . GLU A 1 135 ? 14.929  -11.630 1.000   1.00 19.08 ? 127  GLU A OE2 1 
ATOM   969   N  N   . LYS A 1 136 ? 16.435  -12.855 3.644   1.00 14.81 ? 128  LYS A N   1 
ATOM   970   C  CA  . LYS A 1 136 ? 17.781  -12.975 3.097   1.00 17.94 ? 128  LYS A CA  1 
ATOM   971   C  C   . LYS A 1 136 ? 18.413  -14.301 3.491   1.00 21.88 ? 128  LYS A C   1 
ATOM   972   O  O   . LYS A 1 136 ? 19.015  -14.992 2.658   1.00 15.16 ? 128  LYS A O   1 
ATOM   973   C  CB  . LYS A 1 136 ? 18.633  -11.800 3.581   1.00 19.58 ? 128  LYS A CB  1 
ATOM   974   C  CG  . LYS A 1 136 ? 20.141  -11.990 3.439   1.00 23.34 ? 128  LYS A CG  1 
ATOM   975   C  CD  . LYS A 1 136 ? 20.883  -10.860 4.147   1.00 21.97 ? 128  LYS A CD  1 
ATOM   976   C  CE  . LYS A 1 136 ? 22.386  -11.129 4.242   1.00 22.62 ? 128  LYS A CE  1 
ATOM   977   N  NZ  . LYS A 1 136 ? 23.049  -11.048 2.906   1.00 21.60 ? 128  LYS A NZ  1 
ATOM   978   N  N   . ILE A 1 137 ? 18.286  -14.660 4.769   1.00 20.10 ? 129  ILE A N   1 
ATOM   979   C  CA  . ILE A 1 137 ? 18.825  -15.912 5.282   1.00 18.23 ? 129  ILE A CA  1 
ATOM   980   C  C   . ILE A 1 137 ? 18.162  -17.104 4.604   1.00 19.16 ? 129  ILE A C   1 
ATOM   981   O  O   . ILE A 1 137 ? 18.823  -18.076 4.229   1.00 17.09 ? 129  ILE A O   1 
ATOM   982   C  CB  . ILE A 1 137 ? 18.642  -15.967 6.810   1.00 19.66 ? 129  ILE A CB  1 
ATOM   983   C  CG1 . ILE A 1 137 ? 19.637  -15.029 7.494   1.00 20.21 ? 129  ILE A CG1 1 
ATOM   984   C  CG2 . ILE A 1 137 ? 18.787  -17.397 7.333   1.00 30.14 ? 129  ILE A CG2 1 
ATOM   985   C  CD1 . ILE A 1 137 ? 19.414  -14.920 9.013   1.00 26.07 ? 129  ILE A CD1 1 
ATOM   986   N  N   . LEU A 1 138 ? 16.841  -17.063 4.468   1.00 14.87 ? 130  LEU A N   1 
ATOM   987   C  CA  . LEU A 1 138 ? 16.143  -18.203 3.888   1.00 15.88 ? 130  LEU A CA  1 
ATOM   988   C  C   . LEU A 1 138 ? 16.419  -18.309 2.395   1.00 16.53 ? 130  LEU A C   1 
ATOM   989   O  O   . LEU A 1 138 ? 16.548  -19.417 1.855   1.00 18.38 ? 130  LEU A O   1 
ATOM   990   C  CB  . LEU A 1 138 ? 14.640  -18.091 4.169   1.00 15.22 ? 130  LEU A CB  1 
ATOM   991   C  CG  . LEU A 1 138 ? 14.260  -18.291 5.645   1.00 15.57 ? 130  LEU A CG  1 
ATOM   992   C  CD1 . LEU A 1 138 ? 12.822  -17.886 5.913   1.00 18.29 ? 130  LEU A CD1 1 
ATOM   993   C  CD2 . LEU A 1 138 ? 14.503  -19.746 6.079   1.00 19.18 ? 130  LEU A CD2 1 
ATOM   994   N  N   . ALA A 1 139 ? 16.519  -17.169 1.712   1.00 15.99 ? 131  ALA A N   1 
ATOM   995   C  CA  . ALA A 1 139 ? 16.858  -17.201 0.290   1.00 16.75 ? 131  ALA A CA  1 
ATOM   996   C  C   . ALA A 1 139 ? 18.240  -17.809 0.066   1.00 23.63 ? 131  ALA A C   1 
ATOM   997   O  O   . ALA A 1 139 ? 18.430  -18.619 -0.851  1.00 23.83 ? 131  ALA A O   1 
ATOM   998   C  CB  . ALA A 1 139 ? 16.774  -15.792 -0.302  1.00 16.36 ? 131  ALA A CB  1 
ATOM   999   N  N   . ALA A 1 140 ? 19.219  -17.443 0.898   1.00 17.80 ? 132  ALA A N   1 
ATOM   1000  C  CA  . ALA A 1 140 ? 20.553  -18.006 0.719   1.00 19.90 ? 132  ALA A CA  1 
ATOM   1001  C  C   . ALA A 1 140 ? 20.549  -19.503 0.991   1.00 18.57 ? 132  ALA A C   1 
ATOM   1002  O  O   . ALA A 1 140 ? 21.228  -20.272 0.303   1.00 19.59 ? 132  ALA A O   1 
ATOM   1003  C  CB  . ALA A 1 140 ? 21.558  -17.291 1.622   1.00 18.89 ? 132  ALA A CB  1 
ATOM   1004  N  N   . GLU A 1 141 ? 19.758  -19.934 1.971   1.00 20.68 ? 133  GLU A N   1 
ATOM   1005  C  CA  . GLU A 1 141 ? 19.707  -21.338 2.348   1.00 21.39 ? 133  GLU A CA  1 
ATOM   1006  C  C   . GLU A 1 141 ? 18.954  -22.189 1.324   1.00 23.36 ? 133  GLU A C   1 
ATOM   1007  O  O   . GLU A 1 141 ? 19.427  -23.262 0.946   1.00 23.12 ? 133  GLU A O   1 
ATOM   1008  C  CB  . GLU A 1 141 ? 19.065  -21.477 3.730   1.00 17.93 ? 133  GLU A CB  1 
ATOM   1009  C  CG  . GLU A 1 141 ? 18.937  -22.914 4.180   1.00 24.58 ? 133  GLU A CG  1 
ATOM   1010  C  CD  . GLU A 1 141 ? 18.510  -23.054 5.625   1.00 27.95 ? 133  GLU A CD  1 
ATOM   1011  O  OE1 . GLU A 1 141 ? 18.152  -22.029 6.254   1.00 26.90 ? 133  GLU A OE1 1 
ATOM   1012  O  OE2 . GLU A 1 141 ? 18.535  -24.203 6.128   1.00 26.89 ? 133  GLU A OE2 1 
ATOM   1013  N  N   . PHE A 1 142 ? 17.800  -21.723 0.851   1.00 19.12 ? 134  PHE A N   1 
ATOM   1014  C  CA  . PHE A 1 142 ? 16.862  -22.582 0.136   1.00 19.80 ? 134  PHE A CA  1 
ATOM   1015  C  C   . PHE A 1 142 ? 16.855  -22.404 -1.373  1.00 20.53 ? 134  PHE A C   1 
ATOM   1016  O  O   . PHE A 1 142 ? 16.605  -23.380 -2.085  1.00 22.34 ? 134  PHE A O   1 
ATOM   1017  C  CB  . PHE A 1 142 ? 15.439  -22.367 0.666   1.00 20.90 ? 134  PHE A CB  1 
ATOM   1018  C  CG  . PHE A 1 142 ? 15.169  -23.081 1.963   1.00 25.53 ? 134  PHE A CG  1 
ATOM   1019  C  CD1 . PHE A 1 142 ? 14.893  -24.444 1.971   1.00 19.67 ? 134  PHE A CD1 1 
ATOM   1020  C  CD2 . PHE A 1 142 ? 15.216  -22.400 3.175   1.00 24.07 ? 134  PHE A CD2 1 
ATOM   1021  C  CE1 . PHE A 1 142 ? 14.657  -25.115 3.160   1.00 22.40 ? 134  PHE A CE1 1 
ATOM   1022  C  CE2 . PHE A 1 142 ? 14.972  -23.068 4.372   1.00 19.91 ? 134  PHE A CE2 1 
ATOM   1023  C  CZ  . PHE A 1 142 ? 14.697  -24.419 4.364   1.00 18.54 ? 134  PHE A CZ  1 
ATOM   1024  N  N   . ASN A 1 143 ? 17.094  -21.199 -1.885  1.00 20.94 ? 135  ASN A N   1 
ATOM   1025  C  CA  . ASN A 1 143 ? 17.020  -20.979 -3.328  1.00 20.88 ? 135  ASN A CA  1 
ATOM   1026  C  C   . ASN A 1 143 ? 18.124  -21.753 -4.043  1.00 27.74 ? 135  ASN A C   1 
ATOM   1027  O  O   . ASN A 1 143 ? 19.263  -21.811 -3.572  1.00 25.06 ? 135  ASN A O   1 
ATOM   1028  C  CB  . ASN A 1 143 ? 17.135  -19.491 -3.647  1.00 20.24 ? 135  ASN A CB  1 
ATOM   1029  C  CG  . ASN A 1 143 ? 15.908  -18.710 -3.240  1.00 19.29 ? 135  ASN A CG  1 
ATOM   1030  O  OD1 . ASN A 1 143 ? 14.871  -19.283 -2.891  1.00 21.31 ? 135  ASN A OD1 1 
ATOM   1031  N  ND2 . ASN A 1 143 ? 16.017  -17.389 -3.281  1.00 18.63 ? 135  ASN A ND2 1 
ATOM   1032  N  N   . LYS A 1 144 ? 17.784  -22.346 -5.192  1.00 27.29 ? 136  LYS A N   1 
ATOM   1033  C  CA  . LYS A 1 144 ? 18.678  -23.279 -5.873  1.00 28.28 ? 136  LYS A CA  1 
ATOM   1034  C  C   . LYS A 1 144 ? 18.486  -23.193 -7.383  1.00 39.23 ? 136  LYS A C   1 
ATOM   1035  O  O   . LYS A 1 144 ? 17.351  -23.176 -7.866  1.00 44.56 ? 136  LYS A O   1 
ATOM   1036  C  CB  . LYS A 1 144 ? 18.440  -24.722 -5.404  1.00 27.45 ? 136  LYS A CB  1 
ATOM   1037  C  CG  . LYS A 1 144 ? 19.310  -25.149 -4.228  1.00 35.45 ? 136  LYS A CG  1 
ATOM   1038  C  CD  . LYS A 1 144 ? 18.720  -26.348 -3.512  1.00 38.17 ? 136  LYS A CD  1 
ATOM   1039  C  CE  . LYS A 1 144 ? 19.708  -26.936 -2.521  1.00 46.23 ? 136  LYS A CE  1 
ATOM   1040  N  NZ  . LYS A 1 144 ? 20.376  -25.878 -1.712  1.00 48.13 ? 136  LYS A NZ  1 
ATOM   1041  N  N   . ASP A 1 145 ? 19.610  -23.180 -8.110  1.00 44.88 ? 137  ASP A N   1 
ATOM   1042  C  CA  . ASP A 1 145 ? 19.698  -23.024 -9.566  1.00 53.68 ? 137  ASP A CA  1 
ATOM   1043  C  C   . ASP A 1 145 ? 18.526  -22.267 -10.186 1.00 50.82 ? 137  ASP A C   1 
ATOM   1044  O  O   . ASP A 1 145 ? 17.739  -22.837 -10.947 1.00 49.49 ? 137  ASP A O   1 
ATOM   1045  C  CB  . ASP A 1 145 ? 19.851  -24.389 -10.261 1.00 60.11 ? 137  ASP A CB  1 
ATOM   1046  C  CG  . ASP A 1 145 ? 18.907  -25.453 -9.718  1.00 62.54 ? 137  ASP A CG  1 
ATOM   1047  O  OD1 . ASP A 1 145 ? 19.392  -26.380 -9.039  1.00 62.28 ? 137  ASP A OD1 1 
ATOM   1048  O  OD2 . ASP A 1 145 ? 17.687  -25.375 -9.973  1.00 62.90 ? 137  ASP A OD2 1 
ATOM   1049  N  N   . GLY A 1 146 ? 18.404  -20.980 -9.873  1.00 52.87 ? 138  GLY A N   1 
ATOM   1050  C  CA  . GLY A 1 146 ? 17.366  -20.151 -10.453 1.00 51.53 ? 138  GLY A CA  1 
ATOM   1051  C  C   . GLY A 1 146 ? 15.969  -20.362 -9.909  1.00 45.74 ? 138  GLY A C   1 
ATOM   1052  O  O   . GLY A 1 146 ? 15.075  -19.566 -10.224 1.00 48.80 ? 138  GLY A O   1 
ATOM   1053  N  N   . LEU A 1 147 ? 15.739  -21.403 -9.110  1.00 40.61 ? 139  LEU A N   1 
ATOM   1054  C  CA  . LEU A 1 147 ? 14.425  -21.649 -8.519  1.00 31.84 ? 139  LEU A CA  1 
ATOM   1055  C  C   . LEU A 1 147 ? 14.379  -20.871 -7.214  1.00 30.18 ? 139  LEU A C   1 
ATOM   1056  O  O   . LEU A 1 147 ? 14.750  -21.372 -6.150  1.00 26.49 ? 139  LEU A O   1 
ATOM   1057  C  CB  . LEU A 1 147 ? 14.187  -23.138 -8.311  1.00 32.74 ? 139  LEU A CB  1 
ATOM   1058  C  CG  . LEU A 1 147 ? 14.211  -23.991 -9.583  1.00 34.67 ? 139  LEU A CG  1 
ATOM   1059  C  CD1 . LEU A 1 147 ? 13.906  -25.443 -9.255  1.00 33.09 ? 139  LEU A CD1 1 
ATOM   1060  C  CD2 . LEU A 1 147 ? 13.217  -23.455 -10.591 1.00 37.35 ? 139  LEU A CD2 1 
ATOM   1061  N  N   . ASN A 1 148 ? 13.931  -19.621 -7.303  1.00 25.28 ? 140  ASN A N   1 
ATOM   1062  C  CA  . ASN A 1 148 ? 14.006  -18.698 -6.173  1.00 28.12 ? 140  ASN A CA  1 
ATOM   1063  C  C   . ASN A 1 148 ? 12.683  -18.742 -5.422  1.00 25.02 ? 140  ASN A C   1 
ATOM   1064  O  O   . ASN A 1 148 ? 11.825  -17.865 -5.544  1.00 25.07 ? 140  ASN A O   1 
ATOM   1065  C  CB  . ASN A 1 148 ? 14.348  -17.293 -6.650  1.00 32.47 ? 140  ASN A CB  1 
ATOM   1066  C  CG  . ASN A 1 148 ? 15.776  -17.182 -7.137  1.00 35.33 ? 140  ASN A CG  1 
ATOM   1067  O  OD1 . ASN A 1 148 ? 16.634  -17.983 -6.763  1.00 37.59 ? 140  ASN A OD1 1 
ATOM   1068  N  ND2 . ASN A 1 148 ? 16.041  -16.191 -7.976  1.00 35.01 ? 140  ASN A ND2 1 
ATOM   1069  N  N   . ILE A 1 149 ? 12.525  -19.794 -4.618  1.00 22.79 ? 141  ILE A N   1 
ATOM   1070  C  CA  . ILE A 1 149 ? 11.293  -19.933 -3.859  1.00 25.08 ? 141  ILE A CA  1 
ATOM   1071  C  C   . ILE A 1 149 ? 11.205  -18.916 -2.725  1.00 21.65 ? 141  ILE A C   1 
ATOM   1072  O  O   . ILE A 1 149 ? 10.103  -18.642 -2.237  1.00 22.38 ? 141  ILE A O   1 
ATOM   1073  C  CB  . ILE A 1 149 ? 11.135  -21.381 -3.359  1.00 22.02 ? 141  ILE A CB  1 
ATOM   1074  C  CG1 . ILE A 1 149 ? 12.327  -21.802 -2.505  1.00 20.14 ? 141  ILE A CG1 1 
ATOM   1075  C  CG2 . ILE A 1 149 ? 10.967  -22.345 -4.559  1.00 21.67 ? 141  ILE A CG2 1 
ATOM   1076  C  CD1 . ILE A 1 149 ? 12.011  -22.962 -1.574  1.00 22.92 ? 141  ILE A CD1 1 
ATOM   1077  N  N   . VAL A 1 150 ? 12.316  -18.320 -2.302  1.00 19.80 ? 142  VAL A N   1 
ATOM   1078  C  CA  . VAL A 1 150 ? 12.277  -17.216 -1.344  1.00 18.86 ? 142  VAL A CA  1 
ATOM   1079  C  C   . VAL A 1 150 ? 12.656  -15.952 -2.100  1.00 20.39 ? 142  VAL A C   1 
ATOM   1080  O  O   . VAL A 1 150 ? 13.810  -15.784 -2.512  1.00 21.19 ? 142  VAL A O   1 
ATOM   1081  C  CB  . VAL A 1 150 ? 13.198  -17.440 -0.135  1.00 18.22 ? 142  VAL A CB  1 
ATOM   1082  C  CG1 . VAL A 1 150 ? 13.101  -16.259 0.826   1.00 16.86 ? 142  VAL A CG1 1 
ATOM   1083  C  CG2 . VAL A 1 150 ? 12.838  -18.729 0.587   1.00 19.84 ? 142  VAL A CG2 1 
ATOM   1084  N  N   . ASP A 1 151 ? 11.683  -15.058 -2.280  1.00 17.39 ? 143  ASP A N   1 
ATOM   1085  C  CA  . ASP A 1 151 ? 11.900  -13.849 -3.063  1.00 20.73 ? 143  ASP A CA  1 
ATOM   1086  C  C   . ASP A 1 151 ? 10.778  -12.851 -2.802  1.00 19.52 ? 143  ASP A C   1 
ATOM   1087  O  O   . ASP A 1 151 ? 9.798   -12.823 -3.551  1.00 16.86 ? 143  ASP A O   1 
ATOM   1088  C  CB  . ASP A 1 151 ? 11.981  -14.211 -4.556  1.00 21.70 ? 143  ASP A CB  1 
ATOM   1089  C  CG  . ASP A 1 151 ? 12.266  -13.010 -5.450  1.00 27.73 ? 143  ASP A CG  1 
ATOM   1090  O  OD1 . ASP A 1 151 ? 12.559  -11.917 -4.929  1.00 21.17 ? 143  ASP A OD1 1 
ATOM   1091  O  OD2 . ASP A 1 151 ? 12.197  -13.172 -6.692  1.00 24.74 ? 143  ASP A OD2 1 
ATOM   1092  N  N   . HIS A 1 152 ? 10.884  -12.042 -1.745  1.00 14.91 ? 144  HIS A N   1 
ATOM   1093  C  CA  . HIS A 1 152 ? 9.855   -11.045 -1.478  1.00 21.69 ? 144  HIS A CA  1 
ATOM   1094  C  C   . HIS A 1 152 ? 10.479  -9.850  -0.768  1.00 18.38 ? 144  HIS A C   1 
ATOM   1095  O  O   . HIS A 1 152 ? 11.604  -9.913  -0.270  1.00 18.07 ? 144  HIS A O   1 
ATOM   1096  C  CB  . HIS A 1 152 ? 8.686   -11.629 -0.656  1.00 15.02 ? 144  HIS A CB  1 
ATOM   1097  C  CG  . HIS A 1 152 ? 9.095   -12.240 0.649   1.00 18.69 ? 144  HIS A CG  1 
ATOM   1098  N  ND1 . HIS A 1 152 ? 9.157   -13.606 0.843   1.00 18.37 ? 144  HIS A ND1 1 
ATOM   1099  C  CD2 . HIS A 1 152 ? 9.434   -11.675 1.835   1.00 15.77 ? 144  HIS A CD2 1 
ATOM   1100  C  CE1 . HIS A 1 152 ? 9.523   -13.855 2.089   1.00 17.50 ? 144  HIS A CE1 1 
ATOM   1101  N  NE2 . HIS A 1 152 ? 9.693   -12.701 2.712   1.00 17.49 ? 144  HIS A NE2 1 
ATOM   1102  N  N   . TYR A 1 153 ? 9.729   -8.753  -0.737  1.00 17.85 ? 145  TYR A N   1 
ATOM   1103  C  CA  . TYR A 1 153 ? 10.189  -7.495  -0.177  1.00 16.42 ? 145  TYR A CA  1 
ATOM   1104  C  C   . TYR A 1 153 ? 9.589   -7.254  1.198   1.00 17.24 ? 145  TYR A C   1 
ATOM   1105  O  O   . TYR A 1 153 ? 8.584   -7.852  1.581   1.00 18.31 ? 145  TYR A O   1 
ATOM   1106  C  CB  . TYR A 1 153 ? 9.837   -6.330  -1.106  1.00 20.79 ? 145  TYR A CB  1 
ATOM   1107  C  CG  . TYR A 1 153 ? 10.713  -6.323  -2.322  1.00 21.09 ? 145  TYR A CG  1 
ATOM   1108  C  CD1 . TYR A 1 153 ? 10.463  -7.181  -3.379  1.00 30.80 ? 145  TYR A CD1 1 
ATOM   1109  C  CD2 . TYR A 1 153 ? 11.818  -5.494  -2.394  1.00 20.27 ? 145  TYR A CD2 1 
ATOM   1110  C  CE1 . TYR A 1 153 ? 11.279  -7.199  -4.487  1.00 38.51 ? 145  TYR A CE1 1 
ATOM   1111  C  CE2 . TYR A 1 153 ? 12.645  -5.509  -3.497  1.00 25.07 ? 145  TYR A CE2 1 
ATOM   1112  C  CZ  . TYR A 1 153 ? 12.369  -6.358  -4.541  1.00 38.96 ? 145  TYR A CZ  1 
ATOM   1113  O  OH  . TYR A 1 153 ? 13.184  -6.367  -5.648  1.00 47.42 ? 145  TYR A OH  1 
ATOM   1114  N  N   . THR A 1 154 ? 10.233  -6.358  1.938   1.00 12.18 ? 146  THR A N   1 
ATOM   1115  C  CA  . THR A 1 154 ? 9.764   -5.920  3.247   1.00 12.68 ? 146  THR A CA  1 
ATOM   1116  C  C   . THR A 1 154 ? 9.571   -4.414  3.174   1.00 13.13 ? 146  THR A C   1 
ATOM   1117  O  O   . THR A 1 154 ? 10.552  -3.667  3.068   1.00 15.50 ? 146  THR A O   1 
ATOM   1118  C  CB  . THR A 1 154 ? 10.770  -6.280  4.344   1.00 12.77 ? 146  THR A CB  1 
ATOM   1119  O  OG1 . THR A 1 154 ? 11.052  -7.683  4.290   1.00 15.50 ? 146  THR A OG1 1 
ATOM   1120  C  CG2 . THR A 1 154 ? 10.223  -5.929  5.721   1.00 13.91 ? 146  THR A CG2 1 
ATOM   1121  N  N   . TYR A 1 155 ? 8.318   -3.967  3.206   1.00 11.12 ? 147  TYR A N   1 
ATOM   1122  C  CA  . TYR A 1 155 ? 8.006   -2.549  3.109   1.00 11.02 ? 147  TYR A CA  1 
ATOM   1123  C  C   . TYR A 1 155 ? 7.613   -2.000  4.470   1.00 11.33 ? 147  TYR A C   1 
ATOM   1124  O  O   . TYR A 1 155 ? 6.897   -2.663  5.226   1.00 15.61 ? 147  TYR A O   1 
ATOM   1125  C  CB  . TYR A 1 155 ? 6.865   -2.309  2.125   1.00 12.24 ? 147  TYR A CB  1 
ATOM   1126  C  CG  . TYR A 1 155 ? 7.157   -2.716  0.699   1.00 13.77 ? 147  TYR A CG  1 
ATOM   1127  C  CD1 . TYR A 1 155 ? 7.870   -1.884  -0.149  1.00 14.24 ? 147  TYR A CD1 1 
ATOM   1128  C  CD2 . TYR A 1 155 ? 6.666   -3.913  0.189   1.00 14.84 ? 147  TYR A CD2 1 
ATOM   1129  C  CE1 . TYR A 1 155 ? 8.113   -2.251  -1.463  1.00 12.52 ? 147  TYR A CE1 1 
ATOM   1130  C  CE2 . TYR A 1 155 ? 6.893   -4.280  -1.121  1.00 21.06 ? 147  TYR A CE2 1 
ATOM   1131  C  CZ  . TYR A 1 155 ? 7.619   -3.443  -1.947  1.00 19.28 ? 147  TYR A CZ  1 
ATOM   1132  O  OH  . TYR A 1 155 ? 7.849   -3.813  -3.262  1.00 17.40 ? 147  TYR A OH  1 
ATOM   1133  N  N   . VAL A 1 156 ? 8.078   -0.784  4.781   1.00 10.85 ? 148  VAL A N   1 
ATOM   1134  C  CA  . VAL A 1 156 ? 7.794   -0.146  6.067   1.00 10.26 ? 148  VAL A CA  1 
ATOM   1135  C  C   . VAL A 1 156 ? 7.304   1.273   5.855   1.00 13.43 ? 148  VAL A C   1 
ATOM   1136  O  O   . VAL A 1 156 ? 7.870   2.019   5.050   1.00 16.17 ? 148  VAL A O   1 
ATOM   1137  C  CB  . VAL A 1 156 ? 9.037   -0.102  6.981   1.00 9.96  ? 148  VAL A CB  1 
ATOM   1138  C  CG1 . VAL A 1 156 ? 8.629   0.279   8.415   1.00 11.44 ? 148  VAL A CG1 1 
ATOM   1139  C  CG2 . VAL A 1 156 ? 9.763   -1.409  6.933   1.00 12.60 ? 148  VAL A CG2 1 
ATOM   1140  N  N   . PHE A 1 157 ? 6.272   1.659   6.600   1.00 12.52 ? 149  PHE A N   1 
ATOM   1141  C  CA  . PHE A 1 157 ? 5.923   3.061   6.783   1.00 13.32 ? 149  PHE A CA  1 
ATOM   1142  C  C   . PHE A 1 157 ? 6.416   3.484   8.161   1.00 14.31 ? 149  PHE A C   1 
ATOM   1143  O  O   . PHE A 1 157 ? 6.139   2.800   9.154   1.00 16.05 ? 149  PHE A O   1 
ATOM   1144  C  CB  . PHE A 1 157 ? 4.408   3.291   6.694   1.00 13.72 ? 149  PHE A CB  1 
ATOM   1145  C  CG  . PHE A 1 157 ? 3.845   3.231   5.294   1.00 14.91 ? 149  PHE A CG  1 
ATOM   1146  C  CD1 . PHE A 1 157 ? 4.647   2.913   4.212   1.00 12.51 ? 149  PHE A CD1 1 
ATOM   1147  C  CD2 . PHE A 1 157 ? 2.498   3.516   5.071   1.00 16.03 ? 149  PHE A CD2 1 
ATOM   1148  C  CE1 . PHE A 1 157 ? 4.129   2.865   2.928   1.00 13.95 ? 149  PHE A CE1 1 
ATOM   1149  C  CE2 . PHE A 1 157 ? 1.968   3.478   3.792   1.00 17.85 ? 149  PHE A CE2 1 
ATOM   1150  C  CZ  . PHE A 1 157 ? 2.785   3.146   2.716   1.00 14.15 ? 149  PHE A CZ  1 
ATOM   1151  N  N   . MET A 1 158 ? 7.137   4.601   8.232   1.00 13.48 ? 150  MET A N   1 
ATOM   1152  C  CA  . MET A 1 158 ? 7.572   5.078   9.538   1.00 12.57 ? 150  MET A CA  1 
ATOM   1153  C  C   . MET A 1 158 ? 7.490   6.599   9.580   1.00 15.22 ? 150  MET A C   1 
ATOM   1154  O  O   . MET A 1 158 ? 7.375   7.270   8.553   1.00 14.85 ? 150  MET A O   1 
ATOM   1155  C  CB  . MET A 1 158 ? 8.980   4.535   9.903   1.00 26.49 ? 150  MET A CB  1 
ATOM   1156  C  CG  . MET A 1 158 ? 10.174  4.982   9.104   1.00 25.01 ? 150  MET A CG  1 
ATOM   1157  S  SD  . MET A 1 158 ? 11.662  3.995   9.582   1.00 21.28 ? 150  MET A SD  1 
ATOM   1158  C  CE  . MET A 1 158 ? 11.745  4.373   11.324  1.00 16.90 ? 150  MET A CE  1 
ATOM   1159  N  N   . GLY A 1 159 ? 7.463   7.131   10.800  1.00 14.38 ? 151  GLY A N   1 
ATOM   1160  C  CA  . GLY A 1 159 ? 7.294   8.554   11.005  1.00 15.13 ? 151  GLY A CA  1 
ATOM   1161  C  C   . GLY A 1 159 ? 8.407   9.148   11.844  1.00 16.37 ? 151  GLY A C   1 
ATOM   1162  O  O   . GLY A 1 159 ? 9.384   8.459   12.161  1.00 15.41 ? 151  GLY A O   1 
ATOM   1163  N  N   . ASP A 1 160 ? 8.261   10.426  12.211  1.00 15.79 ? 152  ASP A N   1 
ATOM   1164  C  CA  . ASP A 1 160 ? 9.340   11.146  12.884  1.00 15.70 ? 152  ASP A CA  1 
ATOM   1165  C  C   . ASP A 1 160 ? 9.614   10.585  14.278  1.00 15.93 ? 152  ASP A C   1 
ATOM   1166  O  O   . ASP A 1 160 ? 10.767  10.579  14.734  1.00 15.98 ? 152  ASP A O   1 
ATOM   1167  C  CB  . ASP A 1 160 ? 8.992   12.631  12.988  1.00 21.62 ? 152  ASP A CB  1 
ATOM   1168  C  CG  . ASP A 1 160 ? 9.183   13.366  11.683  1.00 24.61 ? 152  ASP A CG  1 
ATOM   1169  O  OD1 . ASP A 1 160 ? 10.149  13.064  10.962  1.00 27.00 ? 152  ASP A OD1 1 
ATOM   1170  O  OD2 . ASP A 1 160 ? 8.359   14.244  11.375  1.00 32.30 ? 152  ASP A OD2 1 
ATOM   1171  N  N   . GLY A 1 161 ? 8.572   10.152  14.983  1.00 13.37 ? 153  GLY A N   1 
ATOM   1172  C  CA  . GLY A 1 161 ? 8.755   9.587   16.313  1.00 14.77 ? 153  GLY A CA  1 
ATOM   1173  C  C   . GLY A 1 161 ? 9.642   8.361   16.258  1.00 13.88 ? 153  GLY A C   1 
ATOM   1174  O  O   . GLY A 1 161 ? 10.547  8.187   17.072  1.00 14.50 ? 153  GLY A O   1 
HETATM 1175  N  N   . OCS A 1 162 ? 9.375   7.511   15.275  1.00 12.72 ? 154  OCS A N   1 
HETATM 1176  C  CA  . OCS A 1 162 ? 10.167  6.311   15.048  1.00 12.11 ? 154  OCS A CA  1 
HETATM 1177  C  CB  . OCS A 1 162 ? 9.667   5.581   13.817  1.00 13.84 ? 154  OCS A CB  1 
HETATM 1178  S  SG  . OCS A 1 162 ? 8.003   4.950   14.017  1.00 17.97 ? 154  OCS A SG  1 
HETATM 1179  C  C   . OCS A 1 162 ? 11.620  6.636   14.845  1.00 10.26 ? 154  OCS A C   1 
HETATM 1180  O  O   . OCS A 1 162 ? 12.492  5.982   15.397  1.00 11.62 ? 154  OCS A O   1 
HETATM 1181  O  OD1 . OCS A 1 162 ? 7.551   4.668   12.701  1.00 17.29 ? 154  OCS A OD1 1 
HETATM 1182  O  OD2 . OCS A 1 162 ? 8.102   3.761   14.782  1.00 16.32 ? 154  OCS A OD2 1 
HETATM 1183  O  OD3 . OCS A 1 162 ? 7.187   5.914   14.631  1.00 37.77 ? 154  OCS A OD3 1 
ATOM   1184  N  N   . LEU A 1 163 ? 11.871  7.666   14.048  1.00 10.95 ? 155  LEU A N   1 
ATOM   1185  C  CA  . LEU A 1 163 ? 13.245  8.029   13.692  1.00 12.35 ? 155  LEU A CA  1 
ATOM   1186  C  C   . LEU A 1 163 ? 14.021  8.654   14.842  1.00 14.14 ? 155  LEU A C   1 
ATOM   1187  O  O   . LEU A 1 163 ? 15.244  8.553   14.877  1.00 15.82 ? 155  LEU A O   1 
ATOM   1188  C  CB  . LEU A 1 163 ? 13.243  8.984   12.501  1.00 10.48 ? 155  LEU A CB  1 
ATOM   1189  C  CG  . LEU A 1 163 ? 12.818  8.314   11.200  1.00 17.99 ? 155  LEU A CG  1 
ATOM   1190  C  CD1 . LEU A 1 163 ? 12.537  9.378   10.160  1.00 18.75 ? 155  LEU A CD1 1 
ATOM   1191  C  CD2 . LEU A 1 163 ? 13.915  7.362   10.730  1.00 15.65 ? 155  LEU A CD2 1 
ATOM   1192  N  N   . MET A 1 164 ? 13.323  9.303   15.780  1.00 14.18 ? 156  MET A N   1 
ATOM   1193  C  CA  . MET A 1 164 ? 14.020  9.872   16.932  1.00 15.37 ? 156  MET A CA  1 
ATOM   1194  C  C   . MET A 1 164 ? 14.490  8.789   17.891  1.00 13.55 ? 156  MET A C   1 
ATOM   1195  O  O   . MET A 1 164 ? 15.526  8.949   18.539  1.00 11.70 ? 156  MET A O   1 
ATOM   1196  C  CB  . MET A 1 164 ? 13.130  10.860  17.683  1.00 14.08 ? 156  MET A CB  1 
ATOM   1197  C  CG  . MET A 1 164 ? 13.127  12.253  17.082  1.00 16.07 ? 156  MET A CG  1 
ATOM   1198  S  SD  . MET A 1 164 ? 12.034  13.398  17.955  1.00 17.45 ? 156  MET A SD  1 
ATOM   1199  C  CE  . MET A 1 164 ? 10.542  13.202  16.999  1.00 20.15 ? 156  MET A CE  1 
ATOM   1200  N  N   . GLU A 1 165 ? 13.753  7.686   17.974  1.00 11.22 ? 157  GLU A N   1 
ATOM   1201  C  CA  . GLU A 1 165 ? 14.080  6.619   18.904  1.00 10.87 ? 157  GLU A CA  1 
ATOM   1202  C  C   . GLU A 1 165 ? 15.407  5.953   18.558  1.00 10.67 ? 157  GLU A C   1 
ATOM   1203  O  O   . GLU A 1 165 ? 15.698  5.665   17.389  1.00 11.66 ? 157  GLU A O   1 
ATOM   1204  C  CB  . GLU A 1 165 ? 12.965  5.573   18.910  1.00 12.66 ? 157  GLU A CB  1 
ATOM   1205  C  CG  . GLU A 1 165 ? 11.700  6.067   19.616  1.00 11.05 ? 157  GLU A CG  1 
ATOM   1206  C  CD  . GLU A 1 165 ? 11.817  6.099   21.136  1.00 12.26 ? 157  GLU A CD  1 
ATOM   1207  O  OE1 . GLU A 1 165 ? 12.898  5.784   21.688  1.00 11.56 ? 157  GLU A OE1 1 
ATOM   1208  O  OE2 . GLU A 1 165 ? 10.802  6.421   21.792  1.00 12.76 ? 157  GLU A OE2 1 
ATOM   1209  N  N   . GLY A 1 166 ? 16.183  5.667   19.603  1.00 10.88 ? 158  GLY A N   1 
ATOM   1210  C  CA  . GLY A 1 166 ? 17.475  5.040   19.418  1.00 10.82 ? 158  GLY A CA  1 
ATOM   1211  C  C   . GLY A 1 166 ? 17.401  3.668   18.777  1.00 13.02 ? 158  GLY A C   1 
ATOM   1212  O  O   . GLY A 1 166 ? 18.322  3.265   18.064  1.00 10.38 ? 158  GLY A O   1 
ATOM   1213  N  N   . VAL A 1 167 ? 16.311  2.933   19.005  1.00 10.69 ? 159  VAL A N   1 
ATOM   1214  C  CA  . VAL A 1 167 ? 16.246  1.587   18.437  1.00 13.40 ? 159  VAL A CA  1 
ATOM   1215  C  C   . VAL A 1 167 ? 16.179  1.635   16.909  1.00 11.59 ? 159  VAL A C   1 
ATOM   1216  O  O   . VAL A 1 167 ? 16.614  0.692   16.234  1.00 13.18 ? 159  VAL A O   1 
ATOM   1217  C  CB  . VAL A 1 167 ? 15.074  0.806   19.066  1.00 18.92 ? 159  VAL A CB  1 
ATOM   1218  C  CG1 . VAL A 1 167 ? 13.734  1.467   18.737  1.00 12.12 ? 159  VAL A CG1 1 
ATOM   1219  C  CG2 . VAL A 1 167 ? 15.097  -0.670  18.636  1.00 13.04 ? 159  VAL A CG2 1 
ATOM   1220  N  N   . SER A 1 168 ? 15.687  2.737   16.333  1.00 9.82  ? 160  SER A N   1 
ATOM   1221  C  CA  . SER A 1 168 ? 15.705  2.881   14.880  1.00 13.63 ? 160  SER A CA  1 
ATOM   1222  C  C   . SER A 1 168 ? 17.123  3.080   14.376  1.00 11.95 ? 160  SER A C   1 
ATOM   1223  O  O   . SER A 1 168 ? 17.474  2.596   13.296  1.00 12.98 ? 160  SER A O   1 
ATOM   1224  C  CB  . SER A 1 168 ? 14.822  4.051   14.429  1.00 13.77 ? 160  SER A CB  1 
ATOM   1225  O  OG  . SER A 1 168 ? 15.482  5.305   14.600  1.00 12.51 ? 160  SER A OG  1 
ATOM   1226  N  N   . HIS A 1 169 ? 17.938  3.813   15.137  1.00 10.03 ? 161  HIS A N   1 
ATOM   1227  C  CA  . HIS A 1 169 ? 19.355  3.951   14.814  1.00 10.25 ? 161  HIS A CA  1 
ATOM   1228  C  C   . HIS A 1 169 ? 20.048  2.591   14.784  1.00 10.48 ? 161  HIS A C   1 
ATOM   1229  O  O   . HIS A 1 169 ? 20.723  2.249   13.805  1.00 11.73 ? 161  HIS A O   1 
ATOM   1230  C  CB  . HIS A 1 169 ? 20.019  4.873   15.836  1.00 10.58 ? 161  HIS A CB  1 
ATOM   1231  C  CG  . HIS A 1 169 ? 21.514  4.791   15.837  1.00 10.90 ? 161  HIS A CG  1 
ATOM   1232  N  ND1 . HIS A 1 169 ? 22.280  5.272   14.798  1.00 11.08 ? 161  HIS A ND1 1 
ATOM   1233  C  CD2 . HIS A 1 169 ? 22.383  4.287   16.747  1.00 11.16 ? 161  HIS A CD2 1 
ATOM   1234  C  CE1 . HIS A 1 169 ? 23.559  5.063   15.064  1.00 11.45 ? 161  HIS A CE1 1 
ATOM   1235  N  NE2 . HIS A 1 169 ? 23.650  4.469   16.241  1.00 14.04 ? 161  HIS A NE2 1 
ATOM   1236  N  N   . GLU A 1 170 ? 19.862  1.789   15.838  1.00 10.21 ? 162  GLU A N   1 
ATOM   1237  C  CA  . GLU A 1 170 ? 20.466  0.456   15.901  1.00 10.27 ? 162  GLU A CA  1 
ATOM   1238  C  C   . GLU A 1 170 ? 20.017  -0.425  14.741  1.00 10.62 ? 162  GLU A C   1 
ATOM   1239  O  O   . GLU A 1 170 ? 20.847  -1.046  14.058  1.00 11.39 ? 162  GLU A O   1 
ATOM   1240  C  CB  . GLU A 1 170 ? 20.123  -0.220  17.237  1.00 10.29 ? 162  GLU A CB  1 
ATOM   1241  C  CG  . GLU A 1 170 ? 20.588  0.576   18.458  1.00 10.59 ? 162  GLU A CG  1 
ATOM   1242  C  CD  . GLU A 1 170 ? 20.279  -0.107  19.784  1.00 11.33 ? 162  GLU A CD  1 
ATOM   1243  O  OE1 . GLU A 1 170 ? 20.314  0.592   20.815  1.00 13.74 ? 162  GLU A OE1 1 
ATOM   1244  O  OE2 . GLU A 1 170 ? 20.015  -1.333  19.810  1.00 10.88 ? 162  GLU A OE2 1 
ATOM   1245  N  N   . ALA A 1 171 ? 18.705  -0.502  14.501  1.00 9.83  ? 163  ALA A N   1 
ATOM   1246  C  CA  . ALA A 1 171 ? 18.231  -1.426  13.476  1.00 13.24 ? 163  ALA A CA  1 
ATOM   1247  C  C   . ALA A 1 171 ? 18.671  -0.993  12.081  1.00 12.56 ? 163  ALA A C   1 
ATOM   1248  O  O   . ALA A 1 171 ? 19.092  -1.831  11.275  1.00 11.93 ? 163  ALA A O   1 
ATOM   1249  C  CB  . ALA A 1 171 ? 16.707  -1.557  13.535  1.00 13.47 ? 163  ALA A CB  1 
ATOM   1250  N  N   . CYS A 1 172 ? 18.551  0.301   11.766  1.00 12.05 ? 164  CYS A N   1 
ATOM   1251  C  CA  . CYS A 1 172 ? 18.901  0.772   10.427  1.00 12.39 ? 164  CYS A CA  1 
ATOM   1252  C  C   . CYS A 1 172 ? 20.410  0.786   10.206  1.00 12.83 ? 164  CYS A C   1 
ATOM   1253  O  O   . CYS A 1 172 ? 20.876  0.545   9.086   1.00 12.81 ? 164  CYS A O   1 
ATOM   1254  C  CB  . CYS A 1 172 ? 18.311  2.160   10.190  1.00 12.27 ? 164  CYS A CB  1 
ATOM   1255  S  SG  . CYS A 1 172 ? 16.507  2.127   10.188  1.00 13.03 ? 164  CYS A SG  1 
ATOM   1256  N  N   . SER A 1 173 ? 21.187  1.064   11.249  1.00 10.82 ? 165  SER A N   1 
ATOM   1257  C  CA  . SER A 1 173 ? 22.639  0.915   11.143  1.00 14.42 ? 165  SER A CA  1 
ATOM   1258  C  C   . SER A 1 173 ? 23.013  -0.512  10.749  1.00 14.68 ? 165  SER A C   1 
ATOM   1259  O  O   . SER A 1 173 ? 23.764  -0.727  9.788   1.00 14.18 ? 165  SER A O   1 
ATOM   1260  C  CB  . SER A 1 173 ? 23.299  1.295   12.468  1.00 11.58 ? 165  SER A CB  1 
ATOM   1261  O  OG  . SER A 1 173 ? 24.703  1.189   12.381  1.00 14.21 ? 165  SER A OG  1 
ATOM   1262  N  N   . LEU A 1 174 ? 22.483  -1.506  11.475  1.00 11.67 ? 166  LEU A N   1 
ATOM   1263  C  CA  . LEU A 1 174 ? 22.787  -2.901  11.163  1.00 14.61 ? 166  LEU A CA  1 
ATOM   1264  C  C   . LEU A 1 174 ? 22.251  -3.296  9.794   1.00 13.48 ? 166  LEU A C   1 
ATOM   1265  O  O   . LEU A 1 174 ? 22.901  -4.049  9.060   1.00 15.00 ? 166  LEU A O   1 
ATOM   1266  C  CB  . LEU A 1 174 ? 22.211  -3.831  12.238  1.00 14.60 ? 166  LEU A CB  1 
ATOM   1267  C  CG  . LEU A 1 174 ? 22.543  -5.318  12.061  1.00 13.44 ? 166  LEU A CG  1 
ATOM   1268  C  CD1 . LEU A 1 174 ? 24.049  -5.539  12.004  1.00 12.20 ? 166  LEU A CD1 1 
ATOM   1269  C  CD2 . LEU A 1 174 ? 21.941  -6.156  13.186  1.00 15.34 ? 166  LEU A CD2 1 
ATOM   1270  N  N   . ALA A 1 175 ? 21.058  -2.821  9.441   1.00 11.05 ? 167  ALA A N   1 
ATOM   1271  C  CA  . ALA A 1 175 ? 20.518  -3.126  8.120   1.00 15.14 ? 167  ALA A CA  1 
ATOM   1272  C  C   . ALA A 1 175 ? 21.423  -2.585  7.022   1.00 18.06 ? 167  ALA A C   1 
ATOM   1273  O  O   . ALA A 1 175 ? 21.588  -3.220  5.974   1.00 16.54 ? 167  ALA A O   1 
ATOM   1274  C  CB  . ALA A 1 175 ? 19.099  -2.558  7.981   1.00 13.48 ? 167  ALA A CB  1 
ATOM   1275  N  N   . GLY A 1 176 ? 22.037  -1.424  7.257   1.00 13.72 ? 168  GLY A N   1 
ATOM   1276  C  CA  . GLY A 1 176 ? 22.974  -0.880  6.283   1.00 13.28 ? 168  GLY A CA  1 
ATOM   1277  C  C   . GLY A 1 176 ? 24.199  -1.754  6.099   1.00 13.54 ? 168  GLY A C   1 
ATOM   1278  O  O   . GLY A 1 176 ? 24.631  -2.017  4.972   1.00 12.94 ? 168  GLY A O   1 
ATOM   1279  N  N   . THR A 1 177 ? 24.792  -2.201  7.208   1.00 12.32 ? 169  THR A N   1 
ATOM   1280  C  CA  A THR A 1 177 ? 25.983  -3.044  7.150   0.82 15.70 ? 169  THR A CA  1 
ATOM   1281  C  CA  B THR A 1 177 ? 25.998  -3.004  7.069   0.18 16.00 ? 169  THR A CA  1 
ATOM   1282  C  C   . THR A 1 177 ? 25.701  -4.353  6.424   1.00 18.46 ? 169  THR A C   1 
ATOM   1283  O  O   . THR A 1 177 ? 26.545  -4.862  5.675   1.00 15.25 ? 169  THR A O   1 
ATOM   1284  C  CB  A THR A 1 177 ? 26.484  -3.313  8.576   0.82 15.77 ? 169  THR A CB  1 
ATOM   1285  C  CB  B THR A 1 177 ? 26.703  -3.173  8.422   0.18 16.29 ? 169  THR A CB  1 
ATOM   1286  O  OG1 A THR A 1 177 ? 26.968  -2.090  9.148   0.82 12.88 ? 169  THR A OG1 1 
ATOM   1287  O  OG1 B THR A 1 177 ? 27.983  -3.787  8.222   0.18 16.98 ? 169  THR A OG1 1 
ATOM   1288  C  CG2 A THR A 1 177 ? 27.604  -4.347  8.580   0.82 16.39 ? 169  THR A CG2 1 
ATOM   1289  C  CG2 B THR A 1 177 ? 25.895  -4.022  9.363   0.18 14.44 ? 169  THR A CG2 1 
ATOM   1290  N  N   . LEU A 1 178 ? 24.514  -4.916  6.637   1.00 12.89 ? 170  LEU A N   1 
ATOM   1291  C  CA  . LEU A 1 178 ? 24.177  -6.199  6.029   1.00 17.04 ? 170  LEU A CA  1 
ATOM   1292  C  C   . LEU A 1 178 ? 23.564  -6.062  4.636   1.00 14.15 ? 170  LEU A C   1 
ATOM   1293  O  O   . LEU A 1 178 ? 23.198  -7.077  4.036   1.00 18.65 ? 170  LEU A O   1 
ATOM   1294  C  CB  . LEU A 1 178 ? 23.246  -6.986  6.944   1.00 16.27 ? 170  LEU A CB  1 
ATOM   1295  C  CG  . LEU A 1 178 ? 23.938  -7.458  8.237   1.00 18.10 ? 170  LEU A CG  1 
ATOM   1296  C  CD1 . LEU A 1 178 ? 22.965  -8.190  9.108   1.00 18.95 ? 170  LEU A CD1 1 
ATOM   1297  C  CD2 . LEU A 1 178 ? 25.146  -8.359  7.934   1.00 17.17 ? 170  LEU A CD2 1 
ATOM   1298  N  N   . GLY A 1 179 ? 23.480  -4.852  4.103   1.00 13.42 ? 171  GLY A N   1 
ATOM   1299  C  CA  . GLY A 1 179 ? 23.043  -4.628  2.733   1.00 16.60 ? 171  GLY A CA  1 
ATOM   1300  C  C   . GLY A 1 179 ? 21.677  -5.198  2.386   1.00 19.33 ? 171  GLY A C   1 
ATOM   1301  O  O   . GLY A 1 179 ? 21.540  -5.893  1.374   1.00 15.22 ? 171  GLY A O   1 
ATOM   1302  N  N   . LEU A 1 180 ? 20.659  -4.899  3.200   1.00 14.98 ? 172  LEU A N   1 
ATOM   1303  C  CA  . LEU A 1 180 ? 19.316  -5.479  3.046   1.00 12.73 ? 172  LEU A CA  1 
ATOM   1304  C  C   . LEU A 1 180 ? 18.538  -4.726  1.968   1.00 12.23 ? 172  LEU A C   1 
ATOM   1305  O  O   . LEU A 1 180 ? 17.653  -3.914  2.240   1.00 13.10 ? 172  LEU A O   1 
ATOM   1306  C  CB  . LEU A 1 180 ? 18.561  -5.457  4.373   1.00 11.57 ? 172  LEU A CB  1 
ATOM   1307  C  CG  . LEU A 1 180 ? 19.244  -6.214  5.513   1.00 13.77 ? 172  LEU A CG  1 
ATOM   1308  C  CD1 . LEU A 1 180 ? 18.307  -6.192  6.733   1.00 11.69 ? 172  LEU A CD1 1 
ATOM   1309  C  CD2 . LEU A 1 180 ? 19.620  -7.633  5.129   1.00 14.21 ? 172  LEU A CD2 1 
ATOM   1310  N  N   . GLY A 1 181 ? 18.859  -5.040  0.711   1.00 14.92 ? 173  GLY A N   1 
ATOM   1311  C  CA  . GLY A 1 181 ? 18.298  -4.320  -0.424  1.00 16.86 ? 173  GLY A CA  1 
ATOM   1312  C  C   . GLY A 1 181 ? 16.814  -4.535  -0.659  1.00 19.56 ? 173  GLY A C   1 
ATOM   1313  O  O   . GLY A 1 181 ? 16.204  -3.769  -1.414  1.00 20.06 ? 173  GLY A O   1 
ATOM   1314  N  N   . LYS A 1 182 ? 16.217  -5.554  -0.052  1.00 14.49 ? 174  LYS A N   1 
ATOM   1315  C  CA  . LYS A 1 182 ? 14.779  -5.750  -0.218  1.00 14.04 ? 174  LYS A CA  1 
ATOM   1316  C  C   . LYS A 1 182 ? 13.967  -5.083  0.888   1.00 14.27 ? 174  LYS A C   1 
ATOM   1317  O  O   . LYS A 1 182 ? 12.735  -5.230  0.918   1.00 14.56 ? 174  LYS A O   1 
ATOM   1318  C  CB  . LYS A 1 182 ? 14.469  -7.239  -0.306  1.00 18.33 ? 174  LYS A CB  1 
ATOM   1319  C  CG  . LYS A 1 182 ? 15.204  -7.889  -1.485  1.00 23.35 ? 174  LYS A CG  1 
ATOM   1320  C  CD  . LYS A 1 182 ? 15.006  -9.380  -1.489  1.00 30.72 ? 174  LYS A CD  1 
ATOM   1321  C  CE  . LYS A 1 182 ? 14.758  -9.891  -2.876  1.00 26.91 ? 174  LYS A CE  1 
ATOM   1322  N  NZ  . LYS A 1 182 ? 14.446  -11.342 -2.831  1.00 25.60 ? 174  LYS A NZ  1 
ATOM   1323  N  N   . LEU A 1 183 ? 14.631  -4.357  1.790   1.00 14.89 ? 175  LEU A N   1 
ATOM   1324  C  CA  . LEU A 1 183 ? 13.974  -3.553  2.809   1.00 12.32 ? 175  LEU A CA  1 
ATOM   1325  C  C   . LEU A 1 183 ? 13.775  -2.149  2.259   1.00 14.36 ? 175  LEU A C   1 
ATOM   1326  O  O   . LEU A 1 183 ? 14.748  -1.470  1.914   1.00 16.83 ? 175  LEU A O   1 
ATOM   1327  C  CB  . LEU A 1 183 ? 14.816  -3.500  4.082   1.00 12.86 ? 175  LEU A CB  1 
ATOM   1328  C  CG  . LEU A 1 183 ? 14.295  -2.585  5.188   1.00 14.34 ? 175  LEU A CG  1 
ATOM   1329  C  CD1 . LEU A 1 183 ? 12.986  -3.141  5.764   1.00 11.56 ? 175  LEU A CD1 1 
ATOM   1330  C  CD2 . LEU A 1 183 ? 15.353  -2.452  6.290   1.00 14.50 ? 175  LEU A CD2 1 
ATOM   1331  N  N   . ILE A 1 184 ? 12.525  -1.708  2.185   1.00 12.19 ? 176  ILE A N   1 
ATOM   1332  C  CA  . ILE A 1 184 ? 12.193  -0.444  1.543   1.00 13.31 ? 176  ILE A CA  1 
ATOM   1333  C  C   . ILE A 1 184 ? 11.280  0.331   2.475   1.00 17.20 ? 176  ILE A C   1 
ATOM   1334  O  O   . ILE A 1 184 ? 10.173  -0.124  2.786   1.00 16.49 ? 176  ILE A O   1 
ATOM   1335  C  CB  . ILE A 1 184 ? 11.543  -0.655  0.164   1.00 11.56 ? 176  ILE A CB  1 
ATOM   1336  C  CG1 . ILE A 1 184 ? 12.571  -1.275  -0.792  1.00 18.74 ? 176  ILE A CG1 1 
ATOM   1337  C  CG2 . ILE A 1 184 ? 11.035  0.661   -0.392  1.00 15.48 ? 176  ILE A CG2 1 
ATOM   1338  C  CD1 . ILE A 1 184 ? 12.001  -1.634  -2.158  1.00 22.64 ? 176  ILE A CD1 1 
ATOM   1339  N  N   . VAL A 1 185 ? 11.744  1.493   2.922   1.00 11.24 ? 177  VAL A N   1 
ATOM   1340  C  CA  . VAL A 1 185 ? 11.061  2.303   3.925   1.00 10.67 ? 177  VAL A CA  1 
ATOM   1341  C  C   . VAL A 1 185 ? 10.493  3.550   3.256   1.00 12.51 ? 177  VAL A C   1 
ATOM   1342  O  O   . VAL A 1 185 ? 11.218  4.265   2.556   1.00 14.13 ? 177  VAL A O   1 
ATOM   1343  C  CB  . VAL A 1 185 ? 12.023  2.691   5.057   1.00 12.66 ? 177  VAL A CB  1 
ATOM   1344  C  CG1 . VAL A 1 185 ? 11.363  3.690   5.988   1.00 17.68 ? 177  VAL A CG1 1 
ATOM   1345  C  CG2 . VAL A 1 185 ? 12.521  1.430   5.818   1.00 16.21 ? 177  VAL A CG2 1 
ATOM   1346  N  N   . LEU A 1 186 ? 9.198   3.811   3.460   1.00 11.53 ? 178  LEU A N   1 
ATOM   1347  C  CA  . LEU A 1 186 ? 8.588   5.090   3.095   1.00 16.88 ? 178  LEU A CA  1 
ATOM   1348  C  C   . LEU A 1 186 ? 8.377   5.892   4.373   1.00 14.46 ? 178  LEU A C   1 
ATOM   1349  O  O   . LEU A 1 186 ? 7.604   5.485   5.247   1.00 16.39 ? 178  LEU A O   1 
ATOM   1350  C  CB  . LEU A 1 186 ? 7.264   4.928   2.345   1.00 14.95 ? 178  LEU A CB  1 
ATOM   1351  C  CG  . LEU A 1 186 ? 7.343   4.531   0.868   1.00 18.66 ? 178  LEU A CG  1 
ATOM   1352  C  CD1 . LEU A 1 186 ? 7.681   3.058   0.727   1.00 18.51 ? 178  LEU A CD1 1 
ATOM   1353  C  CD2 . LEU A 1 186 ? 6.043   4.859   0.136   1.00 17.31 ? 178  LEU A CD2 1 
ATOM   1354  N  N   . TYR A 1 187 ? 9.087   7.006   4.478   1.00 13.62 ? 179  TYR A N   1 
ATOM   1355  C  CA  . TYR A 1 187 ? 9.086   7.869   5.653   1.00 11.34 ? 179  TYR A CA  1 
ATOM   1356  C  C   . TYR A 1 187 ? 8.104   9.014   5.438   1.00 18.73 ? 179  TYR A C   1 
ATOM   1357  O  O   . TYR A 1 187 ? 8.236   9.781   4.477   1.00 15.60 ? 179  TYR A O   1 
ATOM   1358  C  CB  . TYR A 1 187 ? 10.499  8.400   5.895   1.00 12.62 ? 179  TYR A CB  1 
ATOM   1359  C  CG  . TYR A 1 187 ? 10.611  9.678   6.704   1.00 16.13 ? 179  TYR A CG  1 
ATOM   1360  C  CD1 . TYR A 1 187 ? 9.894   9.858   7.880   1.00 11.75 ? 179  TYR A CD1 1 
ATOM   1361  C  CD2 . TYR A 1 187 ? 11.484  10.687  6.309   1.00 16.15 ? 179  TYR A CD2 1 
ATOM   1362  C  CE1 . TYR A 1 187 ? 10.009  11.016  8.611   1.00 13.14 ? 179  TYR A CE1 1 
ATOM   1363  C  CE2 . TYR A 1 187 ? 11.617  11.844  7.043   1.00 17.61 ? 179  TYR A CE2 1 
ATOM   1364  C  CZ  . TYR A 1 187 ? 10.880  12.001  8.193   1.00 16.85 ? 179  TYR A CZ  1 
ATOM   1365  O  OH  . TYR A 1 187 ? 11.016  13.158  8.919   1.00 19.32 ? 179  TYR A OH  1 
ATOM   1366  N  N   . ASP A 1 188 ? 7.132   9.127   6.338   1.00 12.09 ? 180  ASP A N   1 
ATOM   1367  C  CA  . ASP A 1 188 ? 6.126   10.191  6.322   1.00 13.39 ? 180  ASP A CA  1 
ATOM   1368  C  C   . ASP A 1 188 ? 6.751   11.468  6.864   1.00 15.86 ? 180  ASP A C   1 
ATOM   1369  O  O   . ASP A 1 188 ? 6.687   11.759  8.060   1.00 18.96 ? 180  ASP A O   1 
ATOM   1370  C  CB  . ASP A 1 188 ? 4.924   9.783   7.159   1.00 17.97 ? 180  ASP A CB  1 
ATOM   1371  C  CG  . ASP A 1 188 ? 3.871   10.863  7.239   1.00 20.03 ? 180  ASP A CG  1 
ATOM   1372  O  OD1 . ASP A 1 188 ? 3.885   11.804  6.407   1.00 18.10 ? 180  ASP A OD1 1 
ATOM   1373  O  OD2 . ASP A 1 188 ? 3.014   10.753  8.138   1.00 21.53 ? 180  ASP A OD2 1 
ATOM   1374  N  N   . ASP A 1 189 ? 7.356   12.255  5.977   1.00 14.92 ? 181  ASP A N   1 
ATOM   1375  C  CA  . ASP A 1 189 ? 7.997   13.500  6.389   1.00 16.67 ? 181  ASP A CA  1 
ATOM   1376  C  C   . ASP A 1 189 ? 6.934   14.588  6.330   1.00 20.68 ? 181  ASP A C   1 
ATOM   1377  O  O   . ASP A 1 189 ? 6.711   15.217  5.296   1.00 19.46 ? 181  ASP A O   1 
ATOM   1378  C  CB  . ASP A 1 189 ? 9.194   13.810  5.501   1.00 17.99 ? 181  ASP A CB  1 
ATOM   1379  C  CG  . ASP A 1 189 ? 9.915   15.085  5.911   1.00 20.98 ? 181  ASP A CG  1 
ATOM   1380  O  OD1 . ASP A 1 189 ? 9.396   15.830  6.767   1.00 25.50 ? 181  ASP A OD1 1 
ATOM   1381  O  OD2 . ASP A 1 189 ? 11.002  15.346  5.364   1.00 24.44 ? 181  ASP A OD2 1 
ATOM   1382  N  N   . ASN A 1 190 ? 6.273   14.825  7.458   1.00 17.91 ? 182  ASN A N   1 
ATOM   1383  C  CA  . ASN A 1 190 ? 5.147   15.749  7.510   1.00 22.97 ? 182  ASN A CA  1 
ATOM   1384  C  C   . ASN A 1 190 ? 5.521   17.092  8.132   1.00 27.02 ? 182  ASN A C   1 
ATOM   1385  O  O   . ASN A 1 190 ? 4.672   17.757  8.737   1.00 33.42 ? 182  ASN A O   1 
ATOM   1386  C  CB  . ASN A 1 190 ? 3.974   15.107  8.254   1.00 22.61 ? 182  ASN A CB  1 
ATOM   1387  C  CG  . ASN A 1 190 ? 4.328   14.703  9.663   1.00 30.60 ? 182  ASN A CG  1 
ATOM   1388  O  OD1 . ASN A 1 190 ? 5.375   15.071  10.183  1.00 28.31 ? 182  ASN A OD1 1 
ATOM   1389  N  ND2 . ASN A 1 190 ? 3.456   13.935  10.289  1.00 36.48 ? 182  ASN A ND2 1 
ATOM   1390  N  N   . ASN A 1 191 ? 6.764   17.521  7.958   1.00 31.73 ? 183  ASN A N   1 
ATOM   1391  C  CA  . ASN A 1 191 ? 7.289   18.709  8.606   1.00 37.16 ? 183  ASN A CA  1 
ATOM   1392  C  C   . ASN A 1 191 ? 7.432   19.855  7.611   1.00 43.29 ? 183  ASN A C   1 
ATOM   1393  O  O   . ASN A 1 191 ? 7.517   19.650  6.397   1.00 43.46 ? 183  ASN A O   1 
ATOM   1394  C  CB  . ASN A 1 191 ? 8.633   18.386  9.259   1.00 35.36 ? 183  ASN A CB  1 
ATOM   1395  C  CG  . ASN A 1 191 ? 8.557   17.139  10.113  1.00 34.78 ? 183  ASN A CG  1 
ATOM   1396  O  OD1 . ASN A 1 191 ? 7.948   17.157  11.178  1.00 30.78 ? 183  ASN A OD1 1 
ATOM   1397  N  ND2 . ASN A 1 191 ? 9.135   16.038  9.632   1.00 28.61 ? 183  ASN A ND2 1 
ATOM   1398  N  N   . ILE A 1 192 ? 7.452   21.072  8.146   1.00 49.45 ? 184  ILE A N   1 
ATOM   1399  C  CA  . ILE A 1 192 ? 7.595   22.272  7.327   1.00 55.51 ? 184  ILE A CA  1 
ATOM   1400  C  C   . ILE A 1 192 ? 8.976   22.324  6.680   1.00 59.31 ? 184  ILE A C   1 
ATOM   1401  O  O   . ILE A 1 192 ? 9.176   23.005  5.671   1.00 61.96 ? 184  ILE A O   1 
ATOM   1402  C  CB  . ILE A 1 192 ? 7.338   23.546  8.155   1.00 55.08 ? 184  ILE A CB  1 
ATOM   1403  N  N   . GLY A 1 200 ? 12.828  22.646  16.699  1.00 53.53 ? 192  GLY A N   1 
ATOM   1404  C  CA  . GLY A 1 200 ? 12.598  22.801  18.123  1.00 53.97 ? 192  GLY A CA  1 
ATOM   1405  C  C   . GLY A 1 200 ? 13.214  21.677  18.934  1.00 50.99 ? 192  GLY A C   1 
ATOM   1406  O  O   . GLY A 1 200 ? 13.909  21.913  19.924  1.00 53.93 ? 192  GLY A O   1 
ATOM   1407  N  N   . TRP A 1 201 ? 12.946  20.440  18.509  1.00 44.03 ? 193  TRP A N   1 
ATOM   1408  C  CA  . TRP A 1 201 ? 13.563  19.261  19.106  1.00 38.07 ? 193  TRP A CA  1 
ATOM   1409  C  C   . TRP A 1 201 ? 13.936  18.195  18.091  1.00 34.92 ? 193  TRP A C   1 
ATOM   1410  O  O   . TRP A 1 201 ? 14.541  17.196  18.485  1.00 29.76 ? 193  TRP A O   1 
ATOM   1411  C  CB  . TRP A 1 201 ? 12.632  18.628  20.150  1.00 36.26 ? 193  TRP A CB  1 
ATOM   1412  C  CG  . TRP A 1 201 ? 11.344  18.162  19.536  1.00 43.24 ? 193  TRP A CG  1 
ATOM   1413  C  CD1 . TRP A 1 201 ? 11.076  16.926  19.016  1.00 41.11 ? 193  TRP A CD1 1 
ATOM   1414  C  CD2 . TRP A 1 201 ? 10.156  18.940  19.357  1.00 51.08 ? 193  TRP A CD2 1 
ATOM   1415  N  NE1 . TRP A 1 201 ? 9.790   16.885  18.533  1.00 43.65 ? 193  TRP A NE1 1 
ATOM   1416  C  CE2 . TRP A 1 201 ? 9.204   18.109  18.726  1.00 51.94 ? 193  TRP A CE2 1 
ATOM   1417  C  CE3 . TRP A 1 201 ? 9.802   20.255  19.672  1.00 54.37 ? 193  TRP A CE3 1 
ATOM   1418  C  CZ2 . TRP A 1 201 ? 7.919   18.551  18.411  1.00 57.32 ? 193  TRP A CZ2 1 
ATOM   1419  C  CZ3 . TRP A 1 201 ? 8.527   20.693  19.354  1.00 60.48 ? 193  TRP A CZ3 1 
ATOM   1420  C  CH2 . TRP A 1 201 ? 7.601   19.842  18.731  1.00 59.19 ? 193  TRP A CH2 1 
ATOM   1421  N  N   . PHE A 1 202 ? 13.594  18.352  16.812  1.00 29.88 ? 194  PHE A N   1 
ATOM   1422  C  CA  . PHE A 1 202 ? 13.938  17.367  15.784  1.00 29.90 ? 194  PHE A CA  1 
ATOM   1423  C  C   . PHE A 1 202 ? 14.381  18.143  14.549  1.00 32.95 ? 194  PHE A C   1 
ATOM   1424  O  O   . PHE A 1 202 ? 13.548  18.706  13.835  1.00 33.79 ? 194  PHE A O   1 
ATOM   1425  C  CB  . PHE A 1 202 ? 12.763  16.445  15.467  1.00 22.59 ? 194  PHE A CB  1 
ATOM   1426  C  CG  . PHE A 1 202 ? 13.108  15.331  14.522  1.00 22.44 ? 194  PHE A CG  1 
ATOM   1427  C  CD1 . PHE A 1 202 ? 14.209  14.515  14.761  1.00 18.10 ? 194  PHE A CD1 1 
ATOM   1428  C  CD2 . PHE A 1 202 ? 12.331  15.083  13.407  1.00 27.81 ? 194  PHE A CD2 1 
ATOM   1429  C  CE1 . PHE A 1 202 ? 14.526  13.483  13.897  1.00 20.44 ? 194  PHE A CE1 1 
ATOM   1430  C  CE2 . PHE A 1 202 ? 12.643  14.051  12.537  1.00 28.73 ? 194  PHE A CE2 1 
ATOM   1431  C  CZ  . PHE A 1 202 ? 13.741  13.249  12.781  1.00 23.37 ? 194  PHE A CZ  1 
ATOM   1432  N  N   . THR A 1 203 ? 15.691  18.185  14.307  1.00 32.88 ? 195  THR A N   1 
ATOM   1433  C  CA  . THR A 1 203 ? 16.225  18.886  13.144  1.00 28.43 ? 195  THR A CA  1 
ATOM   1434  C  C   . THR A 1 203 ? 17.211  18.021  12.368  1.00 26.62 ? 195  THR A C   1 
ATOM   1435  O  O   . THR A 1 203 ? 18.018  18.551  11.592  1.00 27.92 ? 195  THR A O   1 
ATOM   1436  C  CB  . THR A 1 203 ? 16.894  20.202  13.555  1.00 31.49 ? 195  THR A CB  1 
ATOM   1437  O  OG1 . THR A 1 203 ? 18.001  19.924  14.416  1.00 35.15 ? 195  THR A OG1 1 
ATOM   1438  C  CG2 . THR A 1 203 ? 15.919  21.111  14.284  1.00 31.42 ? 195  THR A CG2 1 
ATOM   1439  N  N   . GLU A 1 204 ? 17.174  16.706  12.565  1.00 24.64 ? 196  GLU A N   1 
ATOM   1440  C  CA  . GLU A 1 204 ? 18.089  15.819  11.859  1.00 24.18 ? 196  GLU A CA  1 
ATOM   1441  C  C   . GLU A 1 204 ? 17.904  15.946  10.347  1.00 25.61 ? 196  GLU A C   1 
ATOM   1442  O  O   . GLU A 1 204 ? 16.786  16.132  9.852   1.00 21.16 ? 196  GLU A O   1 
ATOM   1443  C  CB  . GLU A 1 204 ? 17.861  14.365  12.284  1.00 25.94 ? 196  GLU A CB  1 
ATOM   1444  C  CG  . GLU A 1 204 ? 18.066  14.071  13.778  1.00 24.65 ? 196  GLU A CG  1 
ATOM   1445  C  CD  . GLU A 1 204 ? 17.870  12.599  14.112  1.00 26.99 ? 196  GLU A CD  1 
ATOM   1446  O  OE1 . GLU A 1 204 ? 17.819  11.768  13.174  1.00 23.05 ? 196  GLU A OE1 1 
ATOM   1447  O  OE2 . GLU A 1 204 ? 17.749  12.268  15.311  1.00 24.38 ? 196  GLU A OE2 1 
ATOM   1448  N  N   . ASN A 1 205 ? 19.018  15.860  9.616   1.00 19.38 ? 197  ASN A N   1 
ATOM   1449  C  CA  . ASN A 1 205 ? 18.999  15.705  8.159   1.00 17.56 ? 197  ASN A CA  1 
ATOM   1450  C  C   . ASN A 1 205 ? 18.859  14.210  7.892   1.00 16.81 ? 197  ASN A C   1 
ATOM   1451  O  O   . ASN A 1 205 ? 19.844  13.461  7.901   1.00 15.83 ? 197  ASN A O   1 
ATOM   1452  C  CB  . ASN A 1 205 ? 20.266  16.299  7.541   1.00 18.08 ? 197  ASN A CB  1 
ATOM   1453  C  CG  . ASN A 1 205 ? 20.254  16.300  6.015   1.00 21.81 ? 197  ASN A CG  1 
ATOM   1454  O  OD1 . ASN A 1 205 ? 19.658  15.436  5.378   1.00 20.41 ? 197  ASN A OD1 1 
ATOM   1455  N  ND2 . ASN A 1 205 ? 20.950  17.263  5.426   1.00 22.78 ? 197  ASN A ND2 1 
ATOM   1456  N  N   . ILE A 1 206 ? 17.621  13.761  7.686   1.00 14.41 ? 198  ILE A N   1 
ATOM   1457  C  CA  . ILE A 1 206 ? 17.368  12.330  7.564   1.00 13.00 ? 198  ILE A CA  1 
ATOM   1458  C  C   . ILE A 1 206 ? 18.073  11.737  6.351   1.00 13.08 ? 198  ILE A C   1 
ATOM   1459  O  O   . ILE A 1 206 ? 18.721  10.689  6.497   1.00 17.00 ? 198  ILE A O   1 
ATOM   1460  C  CB  . ILE A 1 206 ? 15.859  12.049  7.594   1.00 13.81 ? 198  ILE A CB  1 
ATOM   1461  C  CG1 . ILE A 1 206 ? 15.296  12.325  8.991   1.00 20.94 ? 198  ILE A CG1 1 
ATOM   1462  C  CG2 . ILE A 1 206 ? 15.569  10.615  7.183   1.00 15.32 ? 198  ILE A CG2 1 
ATOM   1463  C  CD1 . ILE A 1 206 ? 15.844  11.406  10.086  1.00 20.11 ? 198  ILE A CD1 1 
ATOM   1464  N  N   . PRO A 1 207 ? 18.028  12.346  5.155   1.00 14.34 ? 199  PRO A N   1 
ATOM   1465  C  CA  . PRO A 1 207 ? 18.805  11.772  4.046   1.00 12.13 ? 199  PRO A CA  1 
ATOM   1466  C  C   . PRO A 1 207 ? 20.278  11.619  4.376   1.00 12.36 ? 199  PRO A C   1 
ATOM   1467  O  O   . PRO A 1 207 ? 20.862  10.567  4.089   1.00 14.77 ? 199  PRO A O   1 
ATOM   1468  C  CB  . PRO A 1 207 ? 18.562  12.767  2.898   1.00 18.07 ? 199  PRO A CB  1 
ATOM   1469  C  CG  . PRO A 1 207 ? 17.209  13.324  3.191   1.00 15.77 ? 199  PRO A CG  1 
ATOM   1470  C  CD  . PRO A 1 207 ? 17.173  13.463  4.692   1.00 15.08 ? 199  PRO A CD  1 
ATOM   1471  N  N   . GLN A 1 208 ? 20.889  12.624  5.010   1.00 14.28 ? 200  GLN A N   1 
ATOM   1472  C  CA  . GLN A 1 208 ? 22.306  12.527  5.336   1.00 14.70 ? 200  GLN A CA  1 
ATOM   1473  C  C   . GLN A 1 208 ? 22.569  11.441  6.381   1.00 13.10 ? 200  GLN A C   1 
ATOM   1474  O  O   . GLN A 1 208 ? 23.564  10.714  6.287   1.00 14.57 ? 200  GLN A O   1 
ATOM   1475  C  CB  . GLN A 1 208 ? 22.819  13.886  5.821   1.00 19.75 ? 200  GLN A CB  1 
ATOM   1476  C  CG  . GLN A 1 208 ? 24.330  13.971  5.926   1.00 24.94 ? 200  GLN A CG  1 
ATOM   1477  C  CD  . GLN A 1 208 ? 24.803  15.353  6.329   1.00 28.94 ? 200  GLN A CD  1 
ATOM   1478  O  OE1 . GLN A 1 208 ? 24.128  16.056  7.081   1.00 24.73 ? 200  GLN A OE1 1 
ATOM   1479  N  NE2 . GLN A 1 208 ? 25.955  15.761  5.806   1.00 33.93 ? 200  GLN A NE2 1 
ATOM   1480  N  N   . ARG A 1 209 ? 21.700  11.329  7.391   1.00 12.22 ? 201  ARG A N   1 
ATOM   1481  C  CA  . ARG A 1 209 ? 21.838  10.278  8.399   1.00 13.77 ? 201  ARG A CA  1 
ATOM   1482  C  C   . ARG A 1 209 ? 21.776  8.894   7.766   1.00 12.40 ? 201  ARG A C   1 
ATOM   1483  O  O   . ARG A 1 209 ? 22.618  8.028   8.042   1.00 12.34 ? 201  ARG A O   1 
ATOM   1484  C  CB  . ARG A 1 209 ? 20.747  10.434  9.464   1.00 11.61 ? 201  ARG A CB  1 
ATOM   1485  C  CG  . ARG A 1 209 ? 20.695  9.309   10.504  1.00 14.76 ? 201  ARG A CG  1 
ATOM   1486  C  CD  . ARG A 1 209 ? 19.522  9.503   11.484  1.00 17.34 ? 201  ARG A CD  1 
ATOM   1487  N  NE  . ARG A 1 209 ? 19.149  8.238   12.111  1.00 15.84 ? 201  ARG A NE  1 
ATOM   1488  C  CZ  . ARG A 1 209 ? 17.973  8.004   12.677  1.00 17.76 ? 201  ARG A CZ  1 
ATOM   1489  N  NH1 . ARG A 1 209 ? 17.041  8.959   12.708  1.00 16.30 ? 201  ARG A NH1 1 
ATOM   1490  N  NH2 . ARG A 1 209 ? 17.729  6.815   13.212  1.00 16.53 ? 201  ARG A NH2 1 
ATOM   1491  N  N   . PHE A 1 210 ? 20.799  8.671   6.889   1.00 13.74 ? 202  PHE A N   1 
ATOM   1492  C  CA  . PHE A 1 210 ? 20.678  7.347   6.304   1.00 15.53 ? 202  PHE A CA  1 
ATOM   1493  C  C   . PHE A 1 210 ? 21.747  7.070   5.252   1.00 12.68 ? 202  PHE A C   1 
ATOM   1494  O  O   . PHE A 1 210 ? 22.164  5.921   5.113   1.00 16.22 ? 202  PHE A O   1 
ATOM   1495  C  CB  . PHE A 1 210 ? 19.256  7.150   5.773   1.00 14.07 ? 202  PHE A CB  1 
ATOM   1496  C  CG  . PHE A 1 210 ? 18.315  6.695   6.845   1.00 14.66 ? 202  PHE A CG  1 
ATOM   1497  C  CD1 . PHE A 1 210 ? 17.944  7.565   7.858   1.00 12.83 ? 202  PHE A CD1 1 
ATOM   1498  C  CD2 . PHE A 1 210 ? 17.881  5.378   6.896   1.00 13.69 ? 202  PHE A CD2 1 
ATOM   1499  C  CE1 . PHE A 1 210 ? 17.111  7.142   8.880   1.00 16.05 ? 202  PHE A CE1 1 
ATOM   1500  C  CE2 . PHE A 1 210 ? 17.046  4.950   7.912   1.00 13.83 ? 202  PHE A CE2 1 
ATOM   1501  C  CZ  . PHE A 1 210 ? 16.666  5.833   8.906   1.00 15.60 ? 202  PHE A CZ  1 
ATOM   1502  N  N   . GLU A 1 211 ? 22.236  8.089   4.540   1.00 12.22 ? 203  GLU A N   1 
ATOM   1503  C  CA  . GLU A 1 211 ? 23.454  7.890   3.748   1.00 12.77 ? 203  GLU A CA  1 
ATOM   1504  C  C   . GLU A 1 211 ? 24.594  7.369   4.622   1.00 17.38 ? 203  GLU A C   1 
ATOM   1505  O  O   . GLU A 1 211 ? 25.368  6.496   4.202   1.00 14.85 ? 203  GLU A O   1 
ATOM   1506  C  CB  . GLU A 1 211 ? 23.887  9.193   3.072   1.00 24.01 ? 203  GLU A CB  1 
ATOM   1507  C  CG  . GLU A 1 211 ? 23.043  9.631   1.902   1.00 32.08 ? 203  GLU A CG  1 
ATOM   1508  C  CD  . GLU A 1 211 ? 23.770  10.649  1.038   1.00 38.61 ? 203  GLU A CD  1 
ATOM   1509  O  OE1 . GLU A 1 211 ? 25.012  10.558  0.931   1.00 41.11 ? 203  GLU A OE1 1 
ATOM   1510  O  OE2 . GLU A 1 211 ? 23.102  11.545  0.481   1.00 42.50 ? 203  GLU A OE2 1 
ATOM   1511  N  N   . SER A 1 212 ? 24.719  7.897   5.843   1.00 14.85 ? 204  SER A N   1 
ATOM   1512  C  CA  . SER A 1 212 ? 25.816  7.486   6.714   1.00 13.02 ? 204  SER A CA  1 
ATOM   1513  C  C   . SER A 1 212 ? 25.669  6.046   7.187   1.00 15.39 ? 204  SER A C   1 
ATOM   1514  O  O   . SER A 1 212 ? 26.666  5.439   7.583   1.00 15.46 ? 204  SER A O   1 
ATOM   1515  C  CB  . SER A 1 212 ? 25.930  8.423   7.923   1.00 18.63 ? 204  SER A CB  1 
ATOM   1516  O  OG  . SER A 1 212 ? 25.038  8.044   8.955   1.00 15.01 ? 204  SER A OG  1 
ATOM   1517  N  N   . TYR A 1 213 ? 24.447  5.496   7.186   1.00 13.13 ? 205  TYR A N   1 
ATOM   1518  C  CA  . TYR A 1 213 ? 24.248  4.079   7.447   1.00 13.61 ? 205  TYR A CA  1 
ATOM   1519  C  C   . TYR A 1 213 ? 24.546  3.215   6.226   1.00 17.87 ? 205  TYR A C   1 
ATOM   1520  O  O   . TYR A 1 213 ? 24.476  1.983   6.315   1.00 15.36 ? 205  TYR A O   1 
ATOM   1521  C  CB  . TYR A 1 213 ? 22.799  3.817   7.879   1.00 13.97 ? 205  TYR A CB  1 
ATOM   1522  C  CG  . TYR A 1 213 ? 22.338  4.467   9.164   1.00 14.11 ? 205  TYR A CG  1 
ATOM   1523  C  CD1 . TYR A 1 213 ? 23.230  4.803   10.173  1.00 16.90 ? 205  TYR A CD1 1 
ATOM   1524  C  CD2 . TYR A 1 213 ? 20.981  4.694   9.389   1.00 10.92 ? 205  TYR A CD2 1 
ATOM   1525  C  CE1 . TYR A 1 213 ? 22.775  5.381   11.367  1.00 18.71 ? 205  TYR A CE1 1 
ATOM   1526  C  CE2 . TYR A 1 213 ? 20.522  5.261   10.562  1.00 13.96 ? 205  TYR A CE2 1 
ATOM   1527  C  CZ  . TYR A 1 213 ? 21.414  5.601   11.552  1.00 14.75 ? 205  TYR A CZ  1 
ATOM   1528  O  OH  . TYR A 1 213 ? 20.939  6.171   12.719  1.00 13.66 ? 205  TYR A OH  1 
ATOM   1529  N  N   . GLY A 1 214 ? 24.842  3.828   5.089   1.00 12.97 ? 206  GLY A N   1 
ATOM   1530  C  CA  . GLY A 1 214 ? 25.013  3.086   3.859   1.00 16.81 ? 206  GLY A CA  1 
ATOM   1531  C  C   . GLY A 1 214 ? 23.723  2.785   3.130   1.00 17.20 ? 206  GLY A C   1 
ATOM   1532  O  O   . GLY A 1 214 ? 23.708  1.893   2.277   1.00 16.59 ? 206  GLY A O   1 
ATOM   1533  N  N   . TRP A 1 215 ? 22.642  3.505   3.429   1.00 13.30 ? 207  TRP A N   1 
ATOM   1534  C  CA  . TRP A 1 215 ? 21.372  3.264   2.753   1.00 12.05 ? 207  TRP A CA  1 
ATOM   1535  C  C   . TRP A 1 215 ? 21.305  4.006   1.418   1.00 14.32 ? 207  TRP A C   1 
ATOM   1536  O  O   . TRP A 1 215 ? 22.027  4.977   1.177   1.00 14.98 ? 207  TRP A O   1 
ATOM   1537  C  CB  . TRP A 1 215 ? 20.195  3.717   3.611   1.00 11.54 ? 207  TRP A CB  1 
ATOM   1538  C  CG  . TRP A 1 215 ? 19.862  2.799   4.749   1.00 16.62 ? 207  TRP A CG  1 
ATOM   1539  C  CD1 . TRP A 1 215 ? 20.730  2.237   5.637   1.00 13.64 ? 207  TRP A CD1 1 
ATOM   1540  C  CD2 . TRP A 1 215 ? 18.557  2.376   5.131   1.00 15.71 ? 207  TRP A CD2 1 
ATOM   1541  N  NE1 . TRP A 1 215 ? 20.040  1.484   6.561   1.00 13.85 ? 207  TRP A NE1 1 
ATOM   1542  C  CE2 . TRP A 1 215 ? 18.700  1.554   6.271   1.00 15.37 ? 207  TRP A CE2 1 
ATOM   1543  C  CE3 . TRP A 1 215 ? 17.272  2.619   4.624   1.00 13.11 ? 207  TRP A CE3 1 
ATOM   1544  C  CZ2 . TRP A 1 215 ? 17.607  0.960   6.909   1.00 14.53 ? 207  TRP A CZ2 1 
ATOM   1545  C  CZ3 . TRP A 1 215 ? 16.184  2.017   5.249   1.00 14.60 ? 207  TRP A CZ3 1 
ATOM   1546  C  CH2 . TRP A 1 215 ? 16.358  1.199   6.383   1.00 15.35 ? 207  TRP A CH2 1 
ATOM   1547  N  N   . HIS A 1 216 ? 20.419  3.521   0.548   1.00 14.01 ? 208  HIS A N   1 
ATOM   1548  C  CA  . HIS A 1 216 ? 19.961  4.272   -0.619  1.00 19.84 ? 208  HIS A CA  1 
ATOM   1549  C  C   . HIS A 1 216 ? 18.854  5.228   -0.179  1.00 16.00 ? 208  HIS A C   1 
ATOM   1550  O  O   . HIS A 1 216 ? 17.935  4.831   0.543   1.00 15.39 ? 208  HIS A O   1 
ATOM   1551  C  CB  . HIS A 1 216 ? 19.454  3.301   -1.690  1.00 20.54 ? 208  HIS A CB  1 
ATOM   1552  C  CG  . HIS A 1 216 ? 18.664  3.936   -2.795  1.00 19.82 ? 208  HIS A CG  1 
ATOM   1553  N  ND1 . HIS A 1 216 ? 17.356  3.591   -3.062  1.00 20.85 ? 208  HIS A ND1 1 
ATOM   1554  C  CD2 . HIS A 1 216 ? 19.007  4.857   -3.727  1.00 20.23 ? 208  HIS A CD2 1 
ATOM   1555  C  CE1 . HIS A 1 216 ? 16.920  4.284   -4.101  1.00 20.41 ? 208  HIS A CE1 1 
ATOM   1556  N  NE2 . HIS A 1 216 ? 17.902  5.061   -4.524  1.00 19.35 ? 208  HIS A NE2 1 
ATOM   1557  N  N   . VAL A 1 217 ? 18.938  6.489   -0.591  1.00 16.05 ? 209  VAL A N   1 
ATOM   1558  C  CA  . VAL A 1 217 ? 17.987  7.503   -0.139  1.00 15.03 ? 209  VAL A CA  1 
ATOM   1559  C  C   . VAL A 1 217 ? 17.336  8.151   -1.350  1.00 17.88 ? 209  VAL A C   1 
ATOM   1560  O  O   . VAL A 1 217 ? 18.036  8.582   -2.275  1.00 15.31 ? 209  VAL A O   1 
ATOM   1561  C  CB  . VAL A 1 217 ? 18.663  8.570   0.740   1.00 16.87 ? 209  VAL A CB  1 
ATOM   1562  C  CG1 . VAL A 1 217 ? 17.641  9.620   1.170   1.00 18.88 ? 209  VAL A CG1 1 
ATOM   1563  C  CG2 . VAL A 1 217 ? 19.335  7.925   1.959   1.00 12.34 ? 209  VAL A CG2 1 
ATOM   1564  N  N   . VAL A 1 218 ? 16.007  8.231   -1.336  1.00 14.40 ? 210  VAL A N   1 
ATOM   1565  C  CA  . VAL A 1 218 ? 15.278  9.048   -2.306  1.00 12.91 ? 210  VAL A CA  1 
ATOM   1566  C  C   . VAL A 1 218 ? 14.692  10.232  -1.552  1.00 12.75 ? 210  VAL A C   1 
ATOM   1567  O  O   . VAL A 1 218 ? 13.642  10.103  -0.911  1.00 14.91 ? 210  VAL A O   1 
ATOM   1568  C  CB  . VAL A 1 218 ? 14.172  8.268   -3.036  1.00 15.03 ? 210  VAL A CB  1 
ATOM   1569  C  CG1 . VAL A 1 218 ? 13.581  9.150   -4.173  1.00 13.63 ? 210  VAL A CG1 1 
ATOM   1570  C  CG2 . VAL A 1 218 ? 14.701  6.959   -3.593  1.00 13.16 ? 210  VAL A CG2 1 
ATOM   1571  N  N   . PRO A 1 219 ? 15.316  11.398  -1.607  1.00 13.72 ? 211  PRO A N   1 
ATOM   1572  C  CA  . PRO A 1 219 ? 14.803  12.546  -0.862  1.00 17.37 ? 211  PRO A CA  1 
ATOM   1573  C  C   . PRO A 1 219 ? 13.719  13.307  -1.618  1.00 15.63 ? 211  PRO A C   1 
ATOM   1574  O  O   . PRO A 1 219 ? 13.563  13.198  -2.835  1.00 22.08 ? 211  PRO A O   1 
ATOM   1575  C  CB  . PRO A 1 219 ? 16.056  13.418  -0.686  1.00 22.42 ? 211  PRO A CB  1 
ATOM   1576  C  CG  . PRO A 1 219 ? 16.859  13.144  -1.912  1.00 16.20 ? 211  PRO A CG  1 
ATOM   1577  C  CD  . PRO A 1 219 ? 16.602  11.691  -2.268  1.00 19.18 ? 211  PRO A CD  1 
ATOM   1578  N  N   . ASN A 1 220 ? 12.941  14.057  -0.839  1.00 19.33 ? 212  ASN A N   1 
ATOM   1579  C  CA  A ASN A 1 220 ? 12.032  15.097  -1.324  0.44 18.29 ? 212  ASN A CA  1 
ATOM   1580  C  CA  B ASN A 1 220 ? 12.074  15.108  -1.373  0.56 17.85 ? 212  ASN A CA  1 
ATOM   1581  C  C   . ASN A 1 220 ? 11.043  14.578  -2.365  1.00 20.80 ? 212  ASN A C   1 
ATOM   1582  O  O   . ASN A 1 220 ? 10.819  15.183  -3.417  1.00 24.48 ? 212  ASN A O   1 
ATOM   1583  C  CB  A ASN A 1 220 ? 12.809  16.295  -1.863  0.44 21.62 ? 212  ASN A CB  1 
ATOM   1584  C  CB  B ASN A 1 220 ? 12.897  16.214  -2.041  0.56 21.87 ? 212  ASN A CB  1 
ATOM   1585  C  CG  A ASN A 1 220 ? 11.933  17.511  -2.018  0.44 24.08 ? 212  ASN A CG  1 
ATOM   1586  C  CG  B ASN A 1 220 ? 13.991  16.756  -1.153  0.56 23.57 ? 212  ASN A CG  1 
ATOM   1587  O  OD1 A ASN A 1 220 ? 11.531  18.125  -1.033  0.44 20.16 ? 212  ASN A OD1 1 
ATOM   1588  O  OD1 B ASN A 1 220 ? 13.785  16.992  0.035   0.56 32.86 ? 212  ASN A OD1 1 
ATOM   1589  N  ND2 A ASN A 1 220 ? 11.599  17.844  -3.254  0.44 26.56 ? 212  ASN A ND2 1 
ATOM   1590  N  ND2 B ASN A 1 220 ? 15.168  16.968  -1.733  0.56 27.86 ? 212  ASN A ND2 1 
ATOM   1591  N  N   . VAL A 1 221 ? 10.404  13.468  -2.044  1.00 16.84 ? 213  VAL A N   1 
ATOM   1592  C  CA  . VAL A 1 221 ? 9.347   12.925  -2.887  1.00 14.61 ? 213  VAL A CA  1 
ATOM   1593  C  C   . VAL A 1 221 ? 8.032   13.583  -2.487  1.00 15.62 ? 213  VAL A C   1 
ATOM   1594  O  O   . VAL A 1 221 ? 7.727   13.694  -1.299  1.00 16.37 ? 213  VAL A O   1 
ATOM   1595  C  CB  . VAL A 1 221 ? 9.262   11.396  -2.752  1.00 16.20 ? 213  VAL A CB  1 
ATOM   1596  C  CG1 . VAL A 1 221 ? 8.083   10.859  -3.563  1.00 19.59 ? 213  VAL A CG1 1 
ATOM   1597  C  CG2 . VAL A 1 221 ? 10.564  10.746  -3.214  1.00 18.98 ? 213  VAL A CG2 1 
ATOM   1598  N  N   . ASN A 1 222 ? 7.265   14.045  -3.473  1.00 14.46 ? 214  ASN A N   1 
ATOM   1599  C  CA  . ASN A 1 222 ? 5.913   14.519  -3.193  1.00 14.73 ? 214  ASN A CA  1 
ATOM   1600  C  C   . ASN A 1 222 ? 5.061   13.349  -2.705  1.00 15.07 ? 214  ASN A C   1 
ATOM   1601  O  O   . ASN A 1 222 ? 4.686   12.477  -3.494  1.00 14.59 ? 214  ASN A O   1 
ATOM   1602  C  CB  . ASN A 1 222 ? 5.311   15.162  -4.440  1.00 18.02 ? 214  ASN A CB  1 
ATOM   1603  C  CG  . ASN A 1 222 ? 3.937   15.784  -4.194  1.00 18.47 ? 214  ASN A CG  1 
ATOM   1604  O  OD1 . ASN A 1 222 ? 3.272   15.517  -3.194  1.00 17.70 ? 214  ASN A OD1 1 
ATOM   1605  N  ND2 . ASN A 1 222 ? 3.501   16.594  -5.137  1.00 19.03 ? 214  ASN A ND2 1 
ATOM   1606  N  N   . GLY A 1 223 ? 4.757   13.323  -1.399  1.00 19.10 ? 215  GLY A N   1 
ATOM   1607  C  CA  . GLY A 1 223 ? 4.023   12.238  -0.772  1.00 15.49 ? 215  GLY A CA  1 
ATOM   1608  C  C   . GLY A 1 223 ? 2.549   12.146  -1.115  1.00 14.37 ? 215  GLY A C   1 
ATOM   1609  O  O   . GLY A 1 223 ? 1.883   11.227  -0.631  1.00 18.08 ? 215  GLY A O   1 
ATOM   1610  N  N   . HIS A 1 224 ? 2.012   13.071  -1.912  1.00 14.99 ? 216  HIS A N   1 
ATOM   1611  C  CA  . HIS A 1 224 ? 0.643   12.984  -2.397  1.00 15.58 ? 216  HIS A CA  1 
ATOM   1612  C  C   . HIS A 1 224 ? 0.591   12.803  -3.911  1.00 19.80 ? 216  HIS A C   1 
ATOM   1613  O  O   . HIS A 1 224 ? -0.482  12.914  -4.502  1.00 20.83 ? 216  HIS A O   1 
ATOM   1614  C  CB  . HIS A 1 224 ? -0.159  14.222  -1.971  1.00 16.10 ? 216  HIS A CB  1 
ATOM   1615  C  CG  . HIS A 1 224 ? -0.206  14.421  -0.487  1.00 17.78 ? 216  HIS A CG  1 
ATOM   1616  N  ND1 . HIS A 1 224 ? -0.716  13.471  0.374   1.00 21.16 ? 216  HIS A ND1 1 
ATOM   1617  C  CD2 . HIS A 1 224 ? 0.209   15.448  0.291   1.00 19.98 ? 216  HIS A CD2 1 
ATOM   1618  C  CE1 . HIS A 1 224 ? -0.621  13.908  1.617   1.00 22.95 ? 216  HIS A CE1 1 
ATOM   1619  N  NE2 . HIS A 1 224 ? -0.057  15.103  1.596   1.00 22.02 ? 216  HIS A NE2 1 
ATOM   1620  N  N   . ASP A 1 225 ? 1.729   12.532  -4.547  1.00 19.50 ? 217  ASP A N   1 
ATOM   1621  C  CA  . ASP A 1 225 ? 1.808   12.330  -5.993  1.00 20.04 ? 217  ASP A CA  1 
ATOM   1622  C  C   . ASP A 1 225 ? 2.107   10.856  -6.223  1.00 16.01 ? 217  ASP A C   1 
ATOM   1623  O  O   . ASP A 1 225 ? 3.239   10.415  -6.007  1.00 15.53 ? 217  ASP A O   1 
ATOM   1624  C  CB  . ASP A 1 225 ? 2.889   13.218  -6.609  1.00 18.90 ? 217  ASP A CB  1 
ATOM   1625  C  CG  . ASP A 1 225 ? 2.961   13.097  -8.129  1.00 23.47 ? 217  ASP A CG  1 
ATOM   1626  O  OD1 . ASP A 1 225 ? 2.676   12.012  -8.685  1.00 23.96 ? 217  ASP A OD1 1 
ATOM   1627  O  OD2 . ASP A 1 225 ? 3.304   14.101  -8.770  1.00 29.24 ? 217  ASP A OD2 1 
ATOM   1628  N  N   . THR A 1 226 ? 1.103   10.091  -6.664  1.00 19.20 ? 218  THR A N   1 
ATOM   1629  C  CA  A THR A 1 226 ? 1.316   8.655   -6.814  0.60 18.40 ? 218  THR A CA  1 
ATOM   1630  C  CA  B THR A 1 226 ? 1.297   8.653   -6.835  0.40 18.73 ? 218  THR A CA  1 
ATOM   1631  C  C   . THR A 1 226 ? 2.358   8.351   -7.886  1.00 16.37 ? 218  THR A C   1 
ATOM   1632  O  O   . THR A 1 226 ? 3.090   7.362   -7.765  1.00 16.03 ? 218  THR A O   1 
ATOM   1633  C  CB  A THR A 1 226 ? -0.004  7.938   -7.124  0.60 16.72 ? 218  THR A CB  1 
ATOM   1634  C  CB  B THR A 1 226 ? -0.028  7.975   -7.205  0.40 16.77 ? 218  THR A CB  1 
ATOM   1635  O  OG1 A THR A 1 226 ? -0.540  8.407   -8.363  0.60 17.56 ? 218  THR A OG1 1 
ATOM   1636  O  OG1 B THR A 1 226 ? 0.203   6.586   -7.466  0.40 16.70 ? 218  THR A OG1 1 
ATOM   1637  C  CG2 A THR A 1 226 ? -1.017  8.178   -6.004  0.60 18.35 ? 218  THR A CG2 1 
ATOM   1638  C  CG2 B THR A 1 226 ? -0.649  8.621   -8.434  0.40 19.39 ? 218  THR A CG2 1 
ATOM   1639  N  N   . ALA A 1 227 ? 2.464   9.195   -8.912  1.00 18.48 ? 219  ALA A N   1 
ATOM   1640  C  CA  . ALA A 1 227 ? 3.472   8.978   -9.947  1.00 18.60 ? 219  ALA A CA  1 
ATOM   1641  C  C   . ALA A 1 227 ? 4.873   9.103   -9.374  1.00 18.65 ? 219  ALA A C   1 
ATOM   1642  O  O   . ALA A 1 227 ? 5.753   8.292   -9.680  1.00 18.06 ? 219  ALA A O   1 
ATOM   1643  C  CB  . ALA A 1 227 ? 3.279   9.975   -11.092 1.00 18.02 ? 219  ALA A CB  1 
ATOM   1644  N  N   . ALA A 1 228 ? 5.095   10.128  -8.553  1.00 16.25 ? 220  ALA A N   1 
ATOM   1645  C  CA  . ALA A 1 228 ? 6.384   10.326  -7.909  1.00 17.00 ? 220  ALA A CA  1 
ATOM   1646  C  C   . ALA A 1 228 ? 6.700   9.193   -6.944  1.00 15.69 ? 220  ALA A C   1 
ATOM   1647  O  O   . ALA A 1 228 ? 7.849   8.746   -6.858  1.00 14.83 ? 220  ALA A O   1 
ATOM   1648  C  CB  . ALA A 1 228 ? 6.388   11.663  -7.164  1.00 18.47 ? 220  ALA A CB  1 
ATOM   1649  N  N   . ILE A 1 229 ? 5.702   8.736   -6.185  1.00 14.83 ? 221  ILE A N   1 
ATOM   1650  C  CA  . ILE A 1 229 ? 5.961   7.658   -5.230  1.00 14.73 ? 221  ILE A CA  1 
ATOM   1651  C  C   . ILE A 1 229 ? 6.264   6.365   -5.971  1.00 14.43 ? 221  ILE A C   1 
ATOM   1652  O  O   . ILE A 1 229 ? 7.176   5.622   -5.597  1.00 14.09 ? 221  ILE A O   1 
ATOM   1653  C  CB  . ILE A 1 229 ? 4.777   7.493   -4.260  1.00 14.06 ? 221  ILE A CB  1 
ATOM   1654  C  CG1 . ILE A 1 229 ? 4.506   8.800   -3.519  1.00 13.98 ? 221  ILE A CG1 1 
ATOM   1655  C  CG2 . ILE A 1 229 ? 5.066   6.389   -3.240  1.00 13.57 ? 221  ILE A CG2 1 
ATOM   1656  C  CD1 . ILE A 1 229 ? 3.133   8.824   -2.874  1.00 14.82 ? 221  ILE A CD1 1 
ATOM   1657  N  N   . GLN A 1 230 ? 5.525   6.081   -7.049  1.00 15.98 ? 222  GLN A N   1 
ATOM   1658  C  CA  A GLN A 1 230 ? 5.788   4.843   -7.771  0.56 16.69 ? 222  GLN A CA  1 
ATOM   1659  C  CA  B GLN A 1 230 ? 5.772   4.865   -7.824  0.44 17.03 ? 222  GLN A CA  1 
ATOM   1660  C  C   . GLN A 1 230 ? 7.199   4.840   -8.349  1.00 16.40 ? 222  GLN A C   1 
ATOM   1661  O  O   . GLN A 1 230 ? 7.897   3.823   -8.267  1.00 16.13 ? 222  GLN A O   1 
ATOM   1662  C  CB  A GLN A 1 230 ? 4.746   4.622   -8.867  0.56 19.04 ? 222  GLN A CB  1 
ATOM   1663  C  CB  B GLN A 1 230 ? 4.794   4.776   -8.998  0.44 19.01 ? 222  GLN A CB  1 
ATOM   1664  C  CG  A GLN A 1 230 ? 4.835   3.235   -9.516  0.56 19.09 ? 222  GLN A CG  1 
ATOM   1665  C  CG  B GLN A 1 230 ? 3.372   4.436   -8.633  0.44 19.90 ? 222  GLN A CG  1 
ATOM   1666  C  CD  A GLN A 1 230 ? 3.581   2.857   -10.277 0.56 23.80 ? 222  GLN A CD  1 
ATOM   1667  C  CD  B GLN A 1 230 ? 2.444   4.430   -9.834  0.44 25.91 ? 222  GLN A CD  1 
ATOM   1668  O  OE1 A GLN A 1 230 ? 2.705   3.694   -10.506 0.56 26.96 ? 222  GLN A OE1 1 
ATOM   1669  O  OE1 B GLN A 1 230 ? 2.620   3.646   -10.766 0.44 28.88 ? 222  GLN A OE1 1 
ATOM   1670  N  NE2 A GLN A 1 230 ? 3.491   1.595   -10.681 0.56 17.61 ? 222  GLN A NE2 1 
ATOM   1671  N  NE2 B GLN A 1 230 ? 1.449   5.308   -9.816  0.44 27.07 ? 222  GLN A NE2 1 
ATOM   1672  N  N   . THR A 1 231 ? 7.638   5.965   -8.918  1.00 16.45 ? 223  THR A N   1 
ATOM   1673  C  CA  A THR A 1 231 ? 8.978   6.058   -9.479  0.61 18.02 ? 223  THR A CA  1 
ATOM   1674  C  CA  B THR A 1 231 ? 8.981   6.000   -9.482  0.39 18.35 ? 223  THR A CA  1 
ATOM   1675  C  C   . THR A 1 231 ? 10.041  5.890   -8.399  1.00 17.70 ? 223  THR A C   1 
ATOM   1676  O  O   . THR A 1 231 ? 11.079  5.254   -8.627  1.00 18.90 ? 223  THR A O   1 
ATOM   1677  C  CB  A THR A 1 231 ? 9.128   7.402   -10.196 0.61 20.75 ? 223  THR A CB  1 
ATOM   1678  C  CB  B THR A 1 231 ? 9.207   7.264   -10.317 0.39 20.72 ? 223  THR A CB  1 
ATOM   1679  O  OG1 A THR A 1 231 ? 8.114   7.513   -11.210 0.61 21.29 ? 223  THR A OG1 1 
ATOM   1680  O  OG1 B THR A 1 231 ? 9.167   8.425   -9.480  0.39 19.61 ? 223  THR A OG1 1 
ATOM   1681  C  CG2 A THR A 1 231 ? 10.492  7.524   -10.830 0.61 21.21 ? 223  THR A CG2 1 
ATOM   1682  C  CG2 B THR A 1 231 ? 8.154   7.373   -11.415 0.39 21.04 ? 223  THR A CG2 1 
ATOM   1683  N  N   . ALA A 1 232 ? 9.802   6.469   -7.217  1.00 18.35 ? 224  ALA A N   1 
ATOM   1684  C  CA  . ALA A 1 232 ? 10.764  6.313   -6.127  1.00 17.89 ? 224  ALA A CA  1 
ATOM   1685  C  C   . ALA A 1 232 ? 10.859  4.859   -5.680  1.00 16.60 ? 224  ALA A C   1 
ATOM   1686  O  O   . ALA A 1 232 ? 11.954  4.359   -5.400  1.00 15.91 ? 224  ALA A O   1 
ATOM   1687  C  CB  . ALA A 1 232 ? 10.386  7.205   -4.938  1.00 16.02 ? 224  ALA A CB  1 
ATOM   1688  N  N   . ILE A 1 233 ? 9.719   4.174   -5.567  1.00 17.19 ? 225  ILE A N   1 
ATOM   1689  C  CA  . ILE A 1 233 ? 9.743   2.769   -5.173  1.00 16.19 ? 225  ILE A CA  1 
ATOM   1690  C  C   . ILE A 1 233 ? 10.456  1.931   -6.230  1.00 16.63 ? 225  ILE A C   1 
ATOM   1691  O  O   . ILE A 1 233 ? 11.237  1.026   -5.904  1.00 16.33 ? 225  ILE A O   1 
ATOM   1692  C  CB  . ILE A 1 233 ? 8.311   2.270   -4.908  1.00 19.27 ? 225  ILE A CB  1 
ATOM   1693  C  CG1 . ILE A 1 233 ? 7.692   3.033   -3.728  1.00 13.16 ? 225  ILE A CG1 1 
ATOM   1694  C  CG2 . ILE A 1 233 ? 8.320   0.770   -4.640  1.00 21.00 ? 225  ILE A CG2 1 
ATOM   1695  C  CD1 . ILE A 1 233 ? 6.209   2.729   -3.510  1.00 16.86 ? 225  ILE A CD1 1 
ATOM   1696  N  N   . GLU A 1 234 ? 10.220  2.228   -7.511  1.00 14.89 ? 226  GLU A N   1 
ATOM   1697  C  CA  . GLU A 1 234 ? 10.974  1.552   -8.567  1.00 15.55 ? 226  GLU A CA  1 
ATOM   1698  C  C   . GLU A 1 234 ? 12.474  1.743   -8.379  1.00 21.89 ? 226  GLU A C   1 
ATOM   1699  O  O   . GLU A 1 234 ? 13.255  0.792   -8.527  1.00 16.90 ? 226  GLU A O   1 
ATOM   1700  C  CB  . GLU A 1 234 ? 10.530  2.058   -9.944  1.00 16.35 ? 226  GLU A CB  1 
ATOM   1701  N  N   . ALA A 1 235 ? 12.902  2.962   -8.046  1.00 16.94 ? 227  ALA A N   1 
ATOM   1702  C  CA  . ALA A 1 235 ? 14.328  3.194   -7.850  1.00 21.26 ? 227  ALA A CA  1 
ATOM   1703  C  C   . ALA A 1 235 ? 14.846  2.416   -6.645  1.00 16.75 ? 227  ALA A C   1 
ATOM   1704  O  O   . ALA A 1 235 ? 15.968  1.897   -6.665  1.00 17.31 ? 227  ALA A O   1 
ATOM   1705  C  CB  . ALA A 1 235 ? 14.600  4.686   -7.684  1.00 18.22 ? 227  ALA A CB  1 
ATOM   1706  N  N   . ALA A 1 236 ? 14.037  2.327   -5.587  1.00 14.01 ? 228  ALA A N   1 
ATOM   1707  C  CA  . ALA A 1 236 ? 14.428  1.549   -4.414  1.00 13.50 ? 228  ALA A CA  1 
ATOM   1708  C  C   . ALA A 1 236 ? 14.590  0.076   -4.757  1.00 18.23 ? 228  ALA A C   1 
ATOM   1709  O  O   . ALA A 1 236 ? 15.551  -0.569  -4.321  1.00 17.62 ? 228  ALA A O   1 
ATOM   1710  C  CB  . ALA A 1 236 ? 13.394  1.733   -3.297  1.00 12.87 ? 228  ALA A CB  1 
ATOM   1711  N  N   . ARG A 1 237 ? 13.653  -0.482  -5.532  1.00 15.15 ? 229  ARG A N   1 
ATOM   1712  C  CA  . ARG A 1 237 ? 13.734  -1.899  -5.861  1.00 17.24 ? 229  ARG A CA  1 
ATOM   1713  C  C   . ARG A 1 237 ? 14.961  -2.212  -6.705  1.00 21.17 ? 229  ARG A C   1 
ATOM   1714  O  O   . ARG A 1 237 ? 15.531  -3.306  -6.587  1.00 18.02 ? 229  ARG A O   1 
ATOM   1715  C  CB  . ARG A 1 237 ? 12.455  -2.340  -6.567  1.00 17.17 ? 229  ARG A CB  1 
ATOM   1716  C  CG  . ARG A 1 237 ? 11.224  -2.278  -5.657  1.00 14.38 ? 229  ARG A CG  1 
ATOM   1717  C  CD  . ARG A 1 237 ? 9.923   -2.382  -6.453  1.00 18.93 ? 229  ARG A CD  1 
ATOM   1718  N  NE  . ARG A 1 237 ? 9.896   -3.564  -7.309  1.00 21.14 ? 229  ARG A NE  1 
ATOM   1719  C  CZ  . ARG A 1 237 ? 9.549   -4.784  -6.906  1.00 27.32 ? 229  ARG A CZ  1 
ATOM   1720  N  NH1 . ARG A 1 237 ? 9.186   -4.992  -5.652  1.00 25.84 ? 229  ARG A NH1 1 
ATOM   1721  N  NH2 . ARG A 1 237 ? 9.565   -5.801  -7.763  1.00 29.03 ? 229  ARG A NH2 1 
ATOM   1722  N  N   . ALA A 1 238 ? 15.398  -1.263  -7.536  1.00 21.24 ? 230  ALA A N   1 
ATOM   1723  C  CA  . ALA A 1 238 ? 16.562  -1.473  -8.393  1.00 21.30 ? 230  ALA A CA  1 
ATOM   1724  C  C   . ALA A 1 238 ? 17.875  -1.445  -7.623  1.00 23.28 ? 230  ALA A C   1 
ATOM   1725  O  O   . ALA A 1 238 ? 18.860  -2.048  -8.067  1.00 20.24 ? 230  ALA A O   1 
ATOM   1726  C  CB  . ALA A 1 238 ? 16.584  -0.422  -9.507  1.00 21.80 ? 230  ALA A CB  1 
ATOM   1727  N  N   . GLU A 1 239 ? 17.909  -0.774  -6.482  1.00 20.62 ? 231  GLU A N   1 
ATOM   1728  C  CA  . GLU A 1 239 ? 19.083  -0.740  -5.614  1.00 20.24 ? 231  GLU A CA  1 
ATOM   1729  C  C   . GLU A 1 239 ? 19.085  -2.032  -4.789  1.00 21.97 ? 231  GLU A C   1 
ATOM   1730  O  O   . GLU A 1 239 ? 18.557  -2.090  -3.678  1.00 21.55 ? 231  GLU A O   1 
ATOM   1731  C  CB  . GLU A 1 239 ? 19.036  0.514   -4.743  1.00 20.07 ? 231  GLU A CB  1 
ATOM   1732  C  CG  . GLU A 1 239 ? 20.330  0.887   -4.030  1.00 36.37 ? 231  GLU A CG  1 
ATOM   1733  C  CD  . GLU A 1 239 ? 21.430  1.391   -4.959  1.00 40.97 ? 231  GLU A CD  1 
ATOM   1734  O  OE1 . GLU A 1 239 ? 21.235  2.391   -5.689  1.00 41.94 ? 231  GLU A OE1 1 
ATOM   1735  O  OE2 . GLU A 1 239 ? 22.508  0.768   -4.952  1.00 48.13 ? 231  GLU A OE2 1 
ATOM   1736  N  N   . THR A 1 240 ? 19.680  -3.093  -5.340  1.00 18.10 ? 232  THR A N   1 
ATOM   1737  C  CA  . THR A 1 240 ? 19.575  -4.406  -4.709  1.00 22.18 ? 232  THR A CA  1 
ATOM   1738  C  C   . THR A 1 240 ? 20.572  -4.602  -3.573  1.00 25.42 ? 232  THR A C   1 
ATOM   1739  O  O   . THR A 1 240 ? 20.414  -5.536  -2.782  1.00 21.19 ? 232  THR A O   1 
ATOM   1740  C  CB  . THR A 1 240 ? 19.765  -5.520  -5.750  1.00 23.08 ? 232  THR A CB  1 
ATOM   1741  O  OG1 . THR A 1 240 ? 21.046  -5.388  -6.368  1.00 25.17 ? 232  THR A OG1 1 
ATOM   1742  C  CG2 . THR A 1 240 ? 18.688  -5.445  -6.819  1.00 22.09 ? 232  THR A CG2 1 
ATOM   1743  N  N   . GLY A 1 241 ? 21.595  -3.760  -3.474  1.00 23.58 ? 233  GLY A N   1 
ATOM   1744  C  CA  . GLY A 1 241 ? 22.609  -3.940  -2.460  1.00 21.08 ? 233  GLY A CA  1 
ATOM   1745  C  C   . GLY A 1 241 ? 22.437  -3.135  -1.189  1.00 16.09 ? 233  GLY A C   1 
ATOM   1746  O  O   . GLY A 1 241 ? 23.217  -3.324  -0.253  1.00 17.22 ? 233  GLY A O   1 
ATOM   1747  N  N   . LYS A 1 242 ? 21.444  -2.244  -1.114  1.00 18.49 ? 234  LYS A N   1 
ATOM   1748  C  CA  . LYS A 1 242 ? 21.286  -1.369  0.056   1.00 14.76 ? 234  LYS A CA  1 
ATOM   1749  C  C   . LYS A 1 242 ? 19.810  -1.245  0.404   1.00 15.39 ? 234  LYS A C   1 
ATOM   1750  O  O   . LYS A 1 242 ? 18.978  -1.151  -0.507  1.00 16.95 ? 234  LYS A O   1 
ATOM   1751  C  CB  . LYS A 1 242 ? 21.827  0.043   -0.198  1.00 13.35 ? 234  LYS A CB  1 
ATOM   1752  C  CG  . LYS A 1 242 ? 23.154  0.163   -0.944  1.00 18.38 ? 234  LYS A CG  1 
ATOM   1753  C  CD  . LYS A 1 242 ? 23.375  1.637   -1.259  1.00 19.92 ? 234  LYS A CD  1 
ATOM   1754  C  CE  . LYS A 1 242 ? 24.734  1.915   -1.868  1.00 32.33 ? 234  LYS A CE  1 
ATOM   1755  N  NZ  . LYS A 1 242 ? 24.912  3.393   -1.991  1.00 40.84 ? 234  LYS A NZ  1 
ATOM   1756  N  N   . PRO A 1 243 ? 19.453  -1.203  1.694   1.00 13.61 ? 235  PRO A N   1 
ATOM   1757  C  CA  . PRO A 1 243 ? 18.082  -0.823  2.048   1.00 12.81 ? 235  PRO A CA  1 
ATOM   1758  C  C   . PRO A 1 243 ? 17.826  0.608   1.605   1.00 16.03 ? 235  PRO A C   1 
ATOM   1759  O  O   . PRO A 1 243 ? 18.753  1.416   1.472   1.00 13.25 ? 235  PRO A O   1 
ATOM   1760  C  CB  . PRO A 1 243 ? 18.044  -0.966  3.575   1.00 12.73 ? 235  PRO A CB  1 
ATOM   1761  C  CG  . PRO A 1 243 ? 19.491  -0.799  4.010   1.00 14.20 ? 235  PRO A CG  1 
ATOM   1762  C  CD  . PRO A 1 243 ? 20.329  -1.331  2.873   1.00 11.90 ? 235  PRO A CD  1 
ATOM   1763  N  N   . SER A 1 244 ? 16.556  0.920   1.364   1.00 11.77 ? 236  SER A N   1 
ATOM   1764  C  CA  . SER A 1 244 ? 16.171  2.217   0.828   1.00 12.27 ? 236  SER A CA  1 
ATOM   1765  C  C   . SER A 1 244 ? 15.227  2.938   1.778   1.00 14.32 ? 236  SER A C   1 
ATOM   1766  O  O   . SER A 1 244 ? 14.328  2.318   2.368   1.00 15.90 ? 236  SER A O   1 
ATOM   1767  C  CB  . SER A 1 244 ? 15.473  2.076   -0.537  1.00 16.46 ? 236  SER A CB  1 
ATOM   1768  O  OG  . SER A 1 244 ? 16.352  1.650   -1.549  1.00 12.86 ? 236  SER A OG  1 
ATOM   1769  N  N   . ILE A 1 245 ? 15.404  4.256   1.904   1.00 11.11 ? 237  ILE A N   1 
ATOM   1770  C  CA  . ILE A 1 245 ? 14.410  5.097   2.565   1.00 10.89 ? 237  ILE A CA  1 
ATOM   1771  C  C   . ILE A 1 245 ? 13.935  6.139   1.565   1.00 13.83 ? 237  ILE A C   1 
ATOM   1772  O  O   . ILE A 1 245 ? 14.746  6.781   0.888   1.00 14.27 ? 237  ILE A O   1 
ATOM   1773  C  CB  . ILE A 1 245 ? 14.944  5.747   3.857   1.00 12.90 ? 237  ILE A CB  1 
ATOM   1774  C  CG1 . ILE A 1 245 ? 13.892  6.681   4.476   1.00 10.58 ? 237  ILE A CG1 1 
ATOM   1775  C  CG2 . ILE A 1 245 ? 16.255  6.483   3.623   1.00 16.98 ? 237  ILE A CG2 1 
ATOM   1776  C  CD1 . ILE A 1 245 ? 14.205  7.060   5.915   1.00 15.50 ? 237  ILE A CD1 1 
ATOM   1777  N  N   . ILE A 1 246 ? 12.622  6.278   1.449   1.00 13.41 ? 238  ILE A N   1 
ATOM   1778  C  CA  . ILE A 1 246 ? 12.001  7.219   0.526   1.00 13.56 ? 238  ILE A CA  1 
ATOM   1779  C  C   . ILE A 1 246 ? 11.340  8.293   1.373   1.00 15.28 ? 238  ILE A C   1 
ATOM   1780  O  O   . ILE A 1 246 ? 10.413  8.002   2.139   1.00 14.12 ? 238  ILE A O   1 
ATOM   1781  C  CB  . ILE A 1 246 ? 10.990  6.521   -0.395  1.00 14.23 ? 238  ILE A CB  1 
ATOM   1782  C  CG1 . ILE A 1 246 ? 11.711  5.467   -1.250  1.00 13.76 ? 238  ILE A CG1 1 
ATOM   1783  C  CG2 . ILE A 1 246 ? 10.237  7.563   -1.263  1.00 13.01 ? 238  ILE A CG2 1 
ATOM   1784  C  CD1 . ILE A 1 246 ? 10.800  4.403   -1.844  1.00 17.19 ? 238  ILE A CD1 1 
ATOM   1785  N  N   . CYS A 1 247 ? 11.830  9.522   1.251   1.00 13.92 ? 239  CYS A N   1 
ATOM   1786  C  CA  . CYS A 1 247 ? 11.392  10.626  2.100   1.00 12.85 ? 239  CYS A CA  1 
ATOM   1787  C  C   . CYS A 1 247 ? 10.176  11.282  1.454   1.00 16.93 ? 239  CYS A C   1 
ATOM   1788  O  O   . CYS A 1 247 ? 10.300  12.065  0.507   1.00 18.34 ? 239  CYS A O   1 
ATOM   1789  C  CB  . CYS A 1 247 ? 12.544  11.603  2.323   1.00 14.37 ? 239  CYS A CB  1 
ATOM   1790  S  SG  . CYS A 1 247 ? 13.977  10.814  3.120   1.00 19.15 ? 239  CYS A SG  1 
ATOM   1791  N  N   . CYS A 1 248 ? 8.986   10.988  1.997   1.00 14.94 ? 240  CYS A N   1 
ATOM   1792  C  CA  . CYS A 1 248 ? 7.724   11.411  1.400   1.00 12.38 ? 240  CYS A CA  1 
ATOM   1793  C  C   . CYS A 1 248 ? 7.222   12.658  2.125   1.00 17.93 ? 240  CYS A C   1 
ATOM   1794  O  O   . CYS A 1 248 ? 6.798   12.581  3.278   1.00 15.81 ? 240  CYS A O   1 
ATOM   1795  C  CB  . CYS A 1 248 ? 6.688   10.291  1.470   1.00 12.83 ? 240  CYS A CB  1 
ATOM   1796  S  SG  . CYS A 1 248 ? 7.136   8.773   0.572   1.00 17.30 ? 240  CYS A SG  1 
ATOM   1797  N  N   . LYS A 1 249 ? 7.271   13.799  1.447   1.00 18.04 ? 241  LYS A N   1 
ATOM   1798  C  CA  . LYS A 1 249 ? 6.790   15.059  2.006   1.00 19.81 ? 241  LYS A CA  1 
ATOM   1799  C  C   . LYS A 1 249 ? 5.270   15.080  1.909   1.00 20.04 ? 241  LYS A C   1 
ATOM   1800  O  O   . LYS A 1 249 ? 4.718   15.108  0.806   1.00 17.73 ? 241  LYS A O   1 
ATOM   1801  C  CB  . LYS A 1 249 ? 7.396   16.238  1.249   1.00 19.93 ? 241  LYS A CB  1 
ATOM   1802  C  CG  . LYS A 1 249 ? 8.919   16.187  1.108   1.00 20.08 ? 241  LYS A CG  1 
ATOM   1803  C  CD  . LYS A 1 249 ? 9.613   16.616  2.389   1.00 26.21 ? 241  LYS A CD  1 
ATOM   1804  C  CE  . LYS A 1 249 ? 11.119  16.788  2.177   1.00 29.98 ? 241  LYS A CE  1 
ATOM   1805  N  NZ  . LYS A 1 249 ? 11.785  17.179  3.450   1.00 30.43 ? 241  LYS A NZ  1 
ATOM   1806  N  N   . THR A 1 250 ? 4.590   15.071  3.052   1.00 25.32 ? 242  THR A N   1 
ATOM   1807  C  CA  . THR A 1 250 ? 3.137   15.042  3.106   1.00 25.10 ? 242  THR A CA  1 
ATOM   1808  C  C   . THR A 1 250 ? 2.624   16.328  3.741   1.00 27.40 ? 242  THR A C   1 
ATOM   1809  O  O   . THR A 1 250 ? 3.375   17.091  4.354   1.00 31.82 ? 242  THR A O   1 
ATOM   1810  C  CB  . THR A 1 250 ? 2.629   13.833  3.901   1.00 23.63 ? 242  THR A CB  1 
ATOM   1811  O  OG1 . THR A 1 250 ? 3.074   13.941  5.257   1.00 25.08 ? 242  THR A OG1 1 
ATOM   1812  C  CG2 . THR A 1 250 ? 3.136   12.517  3.286   1.00 22.59 ? 242  THR A CG2 1 
ATOM   1813  N  N   . LEU A 1 251 ? 1.327   16.566  3.585   1.00 26.70 ? 243  LEU A N   1 
ATOM   1814  C  CA  . LEU A 1 251 ? 0.700   17.763  4.142   1.00 40.29 ? 243  LEU A CA  1 
ATOM   1815  C  C   . LEU A 1 251 ? -0.636  17.417  4.795   1.00 44.80 ? 243  LEU A C   1 
ATOM   1816  O  O   . LEU A 1 251 ? -1.109  18.138  5.676   1.00 43.11 ? 243  LEU A O   1 
ATOM   1817  C  CB  . LEU A 1 251 ? 0.491   18.830  3.060   1.00 44.06 ? 243  LEU A CB  1 
ATOM   1818  C  CG  . LEU A 1 251 ? 1.705   19.317  2.265   1.00 49.36 ? 243  LEU A CG  1 
ATOM   1819  C  CD1 . LEU A 1 251 ? 1.267   20.304  1.190   1.00 54.64 ? 243  LEU A CD1 1 
ATOM   1820  C  CD2 . LEU A 1 251 ? 2.758   19.935  3.173   1.00 49.59 ? 243  LEU A CD2 1 
ATOM   1821  N  N   . GLU A 1 276 ? -16.137 16.889  7.430   1.00 50.58 ? 268  GLU A N   1 
ATOM   1822  C  CA  . GLU A 1 276 ? -17.160 16.911  6.388   1.00 53.70 ? 268  GLU A CA  1 
ATOM   1823  C  C   . GLU A 1 276 ? -16.820 17.928  5.300   1.00 56.62 ? 268  GLU A C   1 
ATOM   1824  O  O   . GLU A 1 276 ? -17.066 17.699  4.115   1.00 60.36 ? 268  GLU A O   1 
ATOM   1825  C  CB  . GLU A 1 276 ? -18.533 17.222  6.987   1.00 52.74 ? 268  GLU A CB  1 
ATOM   1826  N  N   . ALA A 1 277 ? -16.268 19.068  5.711   1.00 54.37 ? 269  ALA A N   1 
ATOM   1827  C  CA  . ALA A 1 277 ? -15.877 20.082  4.740   1.00 54.53 ? 269  ALA A CA  1 
ATOM   1828  C  C   . ALA A 1 277 ? -14.713 19.586  3.895   1.00 57.12 ? 269  ALA A C   1 
ATOM   1829  O  O   . ALA A 1 277 ? -14.794 19.549  2.660   1.00 61.56 ? 269  ALA A O   1 
ATOM   1830  C  CB  . ALA A 1 277 ? -15.518 21.380  5.460   1.00 53.40 ? 269  ALA A CB  1 
ATOM   1831  N  N   . THR A 1 278 ? -13.621 19.186  4.554   1.00 51.52 ? 270  THR A N   1 
ATOM   1832  C  CA  . THR A 1 278 ? -12.500 18.578  3.847   1.00 49.24 ? 270  THR A CA  1 
ATOM   1833  C  C   . THR A 1 278 ? -12.962 17.399  3.005   1.00 45.53 ? 270  THR A C   1 
ATOM   1834  O  O   . THR A 1 278 ? -12.439 17.160  1.911   1.00 44.50 ? 270  THR A O   1 
ATOM   1835  C  CB  . THR A 1 278 ? -11.434 18.130  4.848   1.00 46.96 ? 270  THR A CB  1 
ATOM   1836  N  N   . ARG A 1 279 ? -13.952 16.658  3.502   1.00 42.02 ? 271  ARG A N   1 
ATOM   1837  C  CA  . ARG A 1 279 ? -14.553 15.523  2.816   1.00 36.27 ? 271  ARG A CA  1 
ATOM   1838  C  C   . ARG A 1 279 ? -14.982 15.868  1.394   1.00 45.41 ? 271  ARG A C   1 
ATOM   1839  O  O   . ARG A 1 279 ? -14.399 15.371  0.425   1.00 48.85 ? 271  ARG A O   1 
ATOM   1840  C  CB  . ARG A 1 279 ? -15.757 15.036  3.616   1.00 37.08 ? 271  ARG A CB  1 
ATOM   1841  C  CG  . ARG A 1 279 ? -15.952 13.552  3.647   1.00 42.33 ? 271  ARG A CG  1 
ATOM   1842  C  CD  . ARG A 1 279 ? -17.306 13.225  4.243   1.00 41.52 ? 271  ARG A CD  1 
ATOM   1843  N  NE  . ARG A 1 279 ? -17.554 11.795  4.173   1.00 37.89 ? 271  ARG A NE  1 
ATOM   1844  C  CZ  . ARG A 1 279 ? -17.015 10.914  5.003   1.00 35.44 ? 271  ARG A CZ  1 
ATOM   1845  N  NH1 . ARG A 1 279 ? -16.208 11.328  5.972   1.00 34.90 ? 271  ARG A NH1 1 
ATOM   1846  N  NH2 . ARG A 1 279 ? -17.282 9.620   4.862   1.00 32.49 ? 271  ARG A NH2 1 
ATOM   1847  N  N   . LYS A 1 280 ? -16.013 16.704  1.255   1.00 48.44 ? 272  LYS A N   1 
ATOM   1848  C  CA  . LYS A 1 280 ? -16.478 17.077  -0.075  1.00 58.16 ? 272  LYS A CA  1 
ATOM   1849  C  C   . LYS A 1 280 ? -15.493 17.993  -0.794  1.00 66.35 ? 272  LYS A C   1 
ATOM   1850  O  O   . LYS A 1 280 ? -15.581 18.137  -2.019  1.00 66.38 ? 272  LYS A O   1 
ATOM   1851  C  CB  . LYS A 1 280 ? -17.853 17.742  0.013   1.00 60.02 ? 272  LYS A CB  1 
ATOM   1852  N  N   . HIS A 1 281 ? -14.560 18.614  -0.065  1.00 68.60 ? 273  HIS A N   1 
ATOM   1853  C  CA  . HIS A 1 281 ? -13.493 19.372  -0.713  1.00 68.54 ? 273  HIS A CA  1 
ATOM   1854  C  C   . HIS A 1 281 ? -12.501 18.442  -1.400  1.00 70.60 ? 273  HIS A C   1 
ATOM   1855  O  O   . HIS A 1 281 ? -12.200 18.608  -2.589  1.00 75.67 ? 273  HIS A O   1 
ATOM   1856  C  CB  . HIS A 1 281 ? -12.774 20.250  0.307   1.00 68.56 ? 273  HIS A CB  1 
ATOM   1857  N  N   . LEU A 1 282 ? -11.975 17.456  -0.666  1.00 62.91 ? 274  LEU A N   1 
ATOM   1858  C  CA  . LEU A 1 282 ? -11.108 16.451  -1.269  1.00 55.67 ? 274  LEU A CA  1 
ATOM   1859  C  C   . LEU A 1 282 ? -11.847 15.546  -2.245  1.00 53.56 ? 274  LEU A C   1 
ATOM   1860  O  O   . LEU A 1 282 ? -11.223 14.633  -2.797  1.00 53.67 ? 274  LEU A O   1 
ATOM   1861  C  CB  . LEU A 1 282 ? -10.439 15.599  -0.188  1.00 50.87 ? 274  LEU A CB  1 
ATOM   1862  C  CG  . LEU A 1 282 ? -9.324  16.251  0.636   1.00 49.71 ? 274  LEU A CG  1 
ATOM   1863  C  CD1 . LEU A 1 282 ? -8.798  15.282  1.678   1.00 51.13 ? 274  LEU A CD1 1 
ATOM   1864  C  CD2 . LEU A 1 282 ? -8.192  16.746  -0.255  1.00 45.65 ? 274  LEU A CD2 1 
ATOM   1865  N  N   . GLY A 1 283 ? -13.146 15.766  -2.458  1.00 49.00 ? 275  GLY A N   1 
ATOM   1866  C  CA  . GLY A 1 283 ? -13.911 15.041  -3.448  1.00 52.56 ? 275  GLY A CA  1 
ATOM   1867  C  C   . GLY A 1 283 ? -14.593 13.777  -2.967  1.00 53.89 ? 275  GLY A C   1 
ATOM   1868  O  O   . GLY A 1 283 ? -15.186 13.068  -3.792  1.00 55.95 ? 275  GLY A O   1 
ATOM   1869  N  N   . TRP A 1 284 ? -14.532 13.464  -1.670  1.00 46.09 ? 276  TRP A N   1 
ATOM   1870  C  CA  . TRP A 1 284 ? -15.184 12.279  -1.116  1.00 41.07 ? 276  TRP A CA  1 
ATOM   1871  C  C   . TRP A 1 284 ? -16.470 12.718  -0.425  1.00 38.18 ? 276  TRP A C   1 
ATOM   1872  O  O   . TRP A 1 284 ? -16.428 13.310  0.656   1.00 37.56 ? 276  TRP A O   1 
ATOM   1873  C  CB  . TRP A 1 284 ? -14.268 11.544  -0.138  1.00 33.42 ? 276  TRP A CB  1 
ATOM   1874  C  CG  . TRP A 1 284 ? -14.854 10.240  0.344   1.00 30.34 ? 276  TRP A CG  1 
ATOM   1875  C  CD1 . TRP A 1 284 ? -15.548 10.021  1.504   1.00 34.04 ? 276  TRP A CD1 1 
ATOM   1876  C  CD2 . TRP A 1 284 ? -14.809 8.986   -0.338  1.00 27.73 ? 276  TRP A CD2 1 
ATOM   1877  N  NE1 . TRP A 1 284 ? -15.929 8.701   1.586   1.00 33.29 ? 276  TRP A NE1 1 
ATOM   1878  C  CE2 . TRP A 1 284 ? -15.488 8.045   0.466   1.00 32.41 ? 276  TRP A CE2 1 
ATOM   1879  C  CE3 . TRP A 1 284 ? -14.259 8.564   -1.552  1.00 32.49 ? 276  TRP A CE3 1 
ATOM   1880  C  CZ2 . TRP A 1 284 ? -15.632 6.710   0.091   1.00 28.73 ? 276  TRP A CZ2 1 
ATOM   1881  C  CZ3 . TRP A 1 284 ? -14.396 7.243   -1.916  1.00 32.25 ? 276  TRP A CZ3 1 
ATOM   1882  C  CH2 . TRP A 1 284 ? -15.078 6.328   -1.100  1.00 23.79 ? 276  TRP A CH2 1 
ATOM   1883  N  N   . ALA A 1 285 ? -17.612 12.433  -1.045  1.00 33.43 ? 277  ALA A N   1 
ATOM   1884  C  CA  . ALA A 1 285 ? -18.890 12.887  -0.515  1.00 31.96 ? 277  ALA A CA  1 
ATOM   1885  C  C   . ALA A 1 285 ? -19.760 11.762  0.029   1.00 32.46 ? 277  ALA A C   1 
ATOM   1886  O  O   . ALA A 1 285 ? -20.873 12.029  0.494   1.00 29.32 ? 277  ALA A O   1 
ATOM   1887  C  CB  . ALA A 1 285 ? -19.652 13.670  -1.587  1.00 36.37 ? 277  ALA A CB  1 
ATOM   1888  N  N   . TYR A 1 286 ? -19.292 10.520  -0.007  1.00 29.84 ? 278  TYR A N   1 
ATOM   1889  C  CA  . TYR A 1 286 ? -20.071 9.437   0.574   1.00 30.89 ? 278  TYR A CA  1 
ATOM   1890  C  C   . TYR A 1 286 ? -20.122 9.587   2.092   1.00 29.78 ? 278  TYR A C   1 
ATOM   1891  O  O   . TYR A 1 286 ? -19.134 9.996   2.711   1.00 29.12 ? 278  TYR A O   1 
ATOM   1892  C  CB  . TYR A 1 286 ? -19.471 8.085   0.211   1.00 30.15 ? 278  TYR A CB  1 
ATOM   1893  C  CG  . TYR A 1 286 ? -19.474 7.811   -1.268  1.00 26.96 ? 278  TYR A CG  1 
ATOM   1894  C  CD1 . TYR A 1 286 ? -20.600 7.298   -1.895  1.00 30.70 ? 278  TYR A CD1 1 
ATOM   1895  C  CD2 . TYR A 1 286 ? -18.354 8.072   -2.039  1.00 26.91 ? 278  TYR A CD2 1 
ATOM   1896  C  CE1 . TYR A 1 286 ? -20.606 7.053   -3.249  1.00 33.03 ? 278  TYR A CE1 1 
ATOM   1897  C  CE2 . TYR A 1 286 ? -18.345 7.822   -3.392  1.00 29.53 ? 278  TYR A CE2 1 
ATOM   1898  C  CZ  . TYR A 1 286 ? -19.473 7.313   -3.995  1.00 33.39 ? 278  TYR A CZ  1 
ATOM   1899  O  OH  . TYR A 1 286 ? -19.465 7.077   -5.350  1.00 29.29 ? 278  TYR A OH  1 
ATOM   1900  N  N   . PRO A 1 287 ? -21.249 9.273   2.718   1.00 26.89 ? 279  PRO A N   1 
ATOM   1901  C  CA  . PRO A 1 287 ? -21.330 9.363   4.179   1.00 29.43 ? 279  PRO A CA  1 
ATOM   1902  C  C   . PRO A 1 287 ? -20.436 8.325   4.841   1.00 32.50 ? 279  PRO A C   1 
ATOM   1903  O  O   . PRO A 1 287 ? -19.938 7.394   4.207   1.00 28.56 ? 279  PRO A O   1 
ATOM   1904  C  CB  . PRO A 1 287 ? -22.807 9.099   4.474   1.00 30.40 ? 279  PRO A CB  1 
ATOM   1905  C  CG  . PRO A 1 287 ? -23.285 8.313   3.302   1.00 34.42 ? 279  PRO A CG  1 
ATOM   1906  C  CD  . PRO A 1 287 ? -22.519 8.830   2.119   1.00 27.50 ? 279  PRO A CD  1 
ATOM   1907  N  N   . ALA A 1 288 ? -20.250 8.506   6.151   1.00 28.39 ? 280  ALA A N   1 
ATOM   1908  C  CA  . ALA A 1 288 ? -19.369 7.654   6.933   1.00 24.30 ? 280  ALA A CA  1 
ATOM   1909  C  C   . ALA A 1 288 ? -19.655 6.178   6.693   1.00 22.71 ? 280  ALA A C   1 
ATOM   1910  O  O   . ALA A 1 288 ? -20.791 5.720   6.824   1.00 23.13 ? 280  ALA A O   1 
ATOM   1911  C  CB  . ALA A 1 288 ? -19.515 7.980   8.423   1.00 24.80 ? 280  ALA A CB  1 
ATOM   1912  N  N   . PHE A 1 289 ? -18.603 5.440   6.339   1.00 26.17 ? 281  PHE A N   1 
ATOM   1913  C  CA  . PHE A 1 289 ? -18.563 3.992   6.178   1.00 21.53 ? 281  PHE A CA  1 
ATOM   1914  C  C   . PHE A 1 289 ? -19.305 3.521   4.938   1.00 22.24 ? 281  PHE A C   1 
ATOM   1915  O  O   . PHE A 1 289 ? -19.319 2.314   4.673   1.00 27.69 ? 281  PHE A O   1 
ATOM   1916  C  CB  . PHE A 1 289 ? -19.103 3.243   7.409   1.00 21.25 ? 281  PHE A CB  1 
ATOM   1917  C  CG  . PHE A 1 289 ? -18.394 3.596   8.689   1.00 24.80 ? 281  PHE A CG  1 
ATOM   1918  C  CD1 . PHE A 1 289 ? -17.170 3.023   9.002   1.00 24.51 ? 281  PHE A CD1 1 
ATOM   1919  C  CD2 . PHE A 1 289 ? -18.951 4.500   9.579   1.00 22.35 ? 281  PHE A CD2 1 
ATOM   1920  C  CE1 . PHE A 1 289 ? -16.515 3.349   10.178  1.00 23.43 ? 281  PHE A CE1 1 
ATOM   1921  C  CE2 . PHE A 1 289 ? -18.296 4.826   10.755  1.00 24.73 ? 281  PHE A CE2 1 
ATOM   1922  C  CZ  . PHE A 1 289 ? -17.079 4.249   11.050  1.00 19.74 ? 281  PHE A CZ  1 
ATOM   1923  N  N   . GLU A 1 290 ? -19.902 4.423   4.159   1.00 23.34 ? 282  GLU A N   1 
ATOM   1924  C  CA  . GLU A 1 290 ? -20.491 4.055   2.877   1.00 27.20 ? 282  GLU A CA  1 
ATOM   1925  C  C   . GLU A 1 290 ? -19.399 4.036   1.814   1.00 30.55 ? 282  GLU A C   1 
ATOM   1926  O  O   . GLU A 1 290 ? -18.702 5.035   1.606   1.00 26.48 ? 282  GLU A O   1 
ATOM   1927  C  CB  . GLU A 1 290 ? -21.598 5.030   2.483   1.00 25.11 ? 282  GLU A CB  1 
ATOM   1928  N  N   . ILE A 1 291 ? -19.243 2.900   1.139   1.00 23.69 ? 283  ILE A N   1 
ATOM   1929  C  CA  . ILE A 1 291 ? -18.261 2.751   0.077   1.00 24.85 ? 283  ILE A CA  1 
ATOM   1930  C  C   . ILE A 1 291 ? -18.955 2.155   -1.144  1.00 25.57 ? 283  ILE A C   1 
ATOM   1931  O  O   . ILE A 1 291 ? -19.542 1.075   -1.047  1.00 24.69 ? 283  ILE A O   1 
ATOM   1932  C  CB  . ILE A 1 291 ? -17.075 1.870   0.499   1.00 22.52 ? 283  ILE A CB  1 
ATOM   1933  C  CG1 . ILE A 1 291 ? -16.348 2.505   1.689   1.00 25.97 ? 283  ILE A CG1 1 
ATOM   1934  C  CG2 . ILE A 1 291 ? -16.135 1.647   -0.683  1.00 24.79 ? 283  ILE A CG2 1 
ATOM   1935  C  CD1 . ILE A 1 291 ? -15.270 1.637   2.271   1.00 20.70 ? 283  ILE A CD1 1 
ATOM   1936  N  N   . PRO A 1 292 ? -18.901 2.801   -2.306  1.00 27.20 ? 284  PRO A N   1 
ATOM   1937  C  CA  . PRO A 1 292 ? -19.595 2.267   -3.482  1.00 29.59 ? 284  PRO A CA  1 
ATOM   1938  C  C   . PRO A 1 292 ? -18.914 1.022   -4.024  1.00 31.52 ? 284  PRO A C   1 
ATOM   1939  O  O   . PRO A 1 292 ? -17.705 0.828   -3.876  1.00 26.56 ? 284  PRO A O   1 
ATOM   1940  C  CB  . PRO A 1 292 ? -19.519 3.418   -4.487  1.00 29.77 ? 284  PRO A CB  1 
ATOM   1941  C  CG  . PRO A 1 292 ? -18.238 4.110   -4.125  1.00 26.49 ? 284  PRO A CG  1 
ATOM   1942  C  CD  . PRO A 1 292 ? -18.190 4.056   -2.611  1.00 25.59 ? 284  PRO A CD  1 
ATOM   1943  N  N   . GLN A 1 293 ? -19.718 0.177   -4.676  1.00 30.23 ? 285  GLN A N   1 
ATOM   1944  C  CA  . GLN A 1 293 ? -19.211 -1.088  -5.198  1.00 29.61 ? 285  GLN A CA  1 
ATOM   1945  C  C   . GLN A 1 293 ? -18.020 -0.879  -6.126  1.00 26.77 ? 285  GLN A C   1 
ATOM   1946  O  O   . GLN A 1 293 ? -17.062 -1.665  -6.100  1.00 26.09 ? 285  GLN A O   1 
ATOM   1947  C  CB  . GLN A 1 293 ? -20.324 -1.831  -5.937  1.00 35.39 ? 285  GLN A CB  1 
ATOM   1948  C  CG  . GLN A 1 293 ? -19.989 -3.275  -6.221  1.00 38.00 ? 285  GLN A CG  1 
ATOM   1949  C  CD  . GLN A 1 293 ? -19.634 -4.023  -4.953  1.00 46.38 ? 285  GLN A CD  1 
ATOM   1950  O  OE1 . GLN A 1 293 ? -20.384 -4.001  -3.979  1.00 52.33 ? 285  GLN A OE1 1 
ATOM   1951  N  NE2 . GLN A 1 293 ? -18.476 -4.672  -4.949  1.00 45.99 ? 285  GLN A NE2 1 
ATOM   1952  N  N   . GLU A 1 294 ? -18.067 0.164   -6.964  1.00 27.52 ? 286  GLU A N   1 
ATOM   1953  C  CA  . GLU A 1 294 ? -16.992 0.393   -7.925  1.00 27.59 ? 286  GLU A CA  1 
ATOM   1954  C  C   . GLU A 1 294 ? -15.650 0.547   -7.226  1.00 26.25 ? 286  GLU A C   1 
ATOM   1955  O  O   . GLU A 1 294 ? -14.617 0.096   -7.734  1.00 25.96 ? 286  GLU A O   1 
ATOM   1956  C  CB  . GLU A 1 294 ? -17.291 1.628   -8.777  1.00 28.68 ? 286  GLU A CB  1 
ATOM   1957  N  N   . ILE A 1 295 ? -15.645 1.160   -6.047  1.00 25.51 ? 287  ILE A N   1 
ATOM   1958  C  CA  . ILE A 1 295 ? -14.382 1.351   -5.346  1.00 24.35 ? 287  ILE A CA  1 
ATOM   1959  C  C   . ILE A 1 295 ? -13.922 0.058   -4.677  1.00 23.43 ? 287  ILE A C   1 
ATOM   1960  O  O   . ILE A 1 295 ? -12.733 -0.269  -4.709  1.00 22.79 ? 287  ILE A O   1 
ATOM   1961  C  CB  . ILE A 1 295 ? -14.508 2.526   -4.365  1.00 26.80 ? 287  ILE A CB  1 
ATOM   1962  C  CG1 . ILE A 1 295 ? -14.486 3.821   -5.173  1.00 30.81 ? 287  ILE A CG1 1 
ATOM   1963  C  CG2 . ILE A 1 295 ? -13.369 2.511   -3.339  1.00 22.84 ? 287  ILE A CG2 1 
ATOM   1964  C  CD1 . ILE A 1 295 ? -14.706 5.045   -4.373  1.00 38.54 ? 287  ILE A CD1 1 
ATOM   1965  N  N   . TYR A 1 296 ? -14.847 -0.719  -4.099  1.00 23.98 ? 288  TYR A N   1 
ATOM   1966  C  CA  . TYR A 1 296 ? -14.487 -2.050  -3.608  1.00 24.11 ? 288  TYR A CA  1 
ATOM   1967  C  C   . TYR A 1 296 ? -13.904 -2.912  -4.720  1.00 26.31 ? 288  TYR A C   1 
ATOM   1968  O  O   . TYR A 1 296 ? -12.940 -3.655  -4.500  1.00 23.62 ? 288  TYR A O   1 
ATOM   1969  C  CB  . TYR A 1 296 ? -15.708 -2.761  -3.015  1.00 23.23 ? 288  TYR A CB  1 
ATOM   1970  C  CG  . TYR A 1 296 ? -16.018 -2.413  -1.576  1.00 25.25 ? 288  TYR A CG  1 
ATOM   1971  C  CD1 . TYR A 1 296 ? -15.101 -2.676  -0.565  1.00 23.12 ? 288  TYR A CD1 1 
ATOM   1972  C  CD2 . TYR A 1 296 ? -17.250 -1.863  -1.224  1.00 23.12 ? 288  TYR A CD2 1 
ATOM   1973  C  CE1 . TYR A 1 296 ? -15.390 -2.367  0.758   1.00 22.73 ? 288  TYR A CE1 1 
ATOM   1974  C  CE2 . TYR A 1 296 ? -17.554 -1.564  0.091   1.00 22.62 ? 288  TYR A CE2 1 
ATOM   1975  C  CZ  . TYR A 1 296 ? -16.621 -1.814  1.079   1.00 22.93 ? 288  TYR A CZ  1 
ATOM   1976  O  OH  . TYR A 1 296 ? -16.916 -1.512  2.386   1.00 21.17 ? 288  TYR A OH  1 
ATOM   1977  N  N   . ASP A 1 297 ? -14.501 -2.849  -5.915  1.00 24.37 ? 289  ASP A N   1 
ATOM   1978  C  CA  . ASP A 1 297 ? -14.038 -3.667  -7.031  1.00 24.91 ? 289  ASP A CA  1 
ATOM   1979  C  C   . ASP A 1 297 ? -12.623 -3.289  -7.442  1.00 27.23 ? 289  ASP A C   1 
ATOM   1980  O  O   . ASP A 1 297 ? -11.802 -4.164  -7.744  1.00 28.38 ? 289  ASP A O   1 
ATOM   1981  C  CB  . ASP A 1 297 ? -14.995 -3.534  -8.227  1.00 26.36 ? 289  ASP A CB  1 
ATOM   1982  C  CG  . ASP A 1 297 ? -16.360 -4.166  -7.968  1.00 39.28 ? 289  ASP A CG  1 
ATOM   1983  O  OD1 . ASP A 1 297 ? -16.478 -5.016  -7.061  1.00 38.65 ? 289  ASP A OD1 1 
ATOM   1984  O  OD2 . ASP A 1 297 ? -17.322 -3.817  -8.681  1.00 39.88 ? 289  ASP A OD2 1 
ATOM   1985  N  N   . ALA A 1 298 ? -12.324 -1.989  -7.474  1.00 24.28 ? 290  ALA A N   1 
ATOM   1986  C  CA  . ALA A 1 298 ? -10.991 -1.544  -7.865  1.00 25.75 ? 290  ALA A CA  1 
ATOM   1987  C  C   . ALA A 1 298 ? -9.951  -1.906  -6.818  1.00 23.71 ? 290  ALA A C   1 
ATOM   1988  O  O   . ALA A 1 298 ? -8.790  -2.159  -7.157  1.00 24.12 ? 290  ALA A O   1 
ATOM   1989  C  CB  . ALA A 1 298 ? -10.977 -0.034  -8.087  1.00 27.14 ? 290  ALA A CB  1 
ATOM   1990  N  N   . TRP A 1 299 ? -10.340 -1.899  -5.545  1.00 22.00 ? 291  TRP A N   1 
ATOM   1991  C  CA  . TRP A 1 299 ? -9.405  -2.180  -4.464  1.00 20.90 ? 291  TRP A CA  1 
ATOM   1992  C  C   . TRP A 1 299 ? -9.228  -3.667  -4.207  1.00 20.64 ? 291  TRP A C   1 
ATOM   1993  O  O   . TRP A 1 299 ? -8.197  -4.069  -3.655  1.00 23.27 ? 291  TRP A O   1 
ATOM   1994  C  CB  . TRP A 1 299 ? -9.877  -1.517  -3.170  1.00 20.41 ? 291  TRP A CB  1 
ATOM   1995  C  CG  . TRP A 1 299 ? -9.146  -0.263  -2.821  1.00 20.08 ? 291  TRP A CG  1 
ATOM   1996  C  CD1 . TRP A 1 299 ? -9.641  1.005   -2.814  1.00 23.00 ? 291  TRP A CD1 1 
ATOM   1997  C  CD2 . TRP A 1 299 ? -7.778  -0.164  -2.421  1.00 19.38 ? 291  TRP A CD2 1 
ATOM   1998  N  NE1 . TRP A 1 299 ? -8.661  1.894   -2.436  1.00 23.68 ? 291  TRP A NE1 1 
ATOM   1999  C  CE2 . TRP A 1 299 ? -7.507  1.199   -2.187  1.00 20.41 ? 291  TRP A CE2 1 
ATOM   2000  C  CE3 . TRP A 1 299 ? -6.752  -1.095  -2.247  1.00 18.80 ? 291  TRP A CE3 1 
ATOM   2001  C  CZ2 . TRP A 1 299 ? -6.252  1.653   -1.782  1.00 18.98 ? 291  TRP A CZ2 1 
ATOM   2002  C  CZ3 . TRP A 1 299 ? -5.508  -0.643  -1.838  1.00 26.08 ? 291  TRP A CZ3 1 
ATOM   2003  C  CH2 . TRP A 1 299 ? -5.270  0.720   -1.611  1.00 18.38 ? 291  TRP A CH2 1 
ATOM   2004  N  N   . ASN A 1 300 ? -10.208 -4.487  -4.564  1.00 21.32 ? 292  ASN A N   1 
ATOM   2005  C  CA  . ASN A 1 300 ? -10.155 -5.889  -4.177  1.00 25.76 ? 292  ASN A CA  1 
ATOM   2006  C  C   . ASN A 1 300 ? -8.926  -6.575  -4.768  1.00 27.52 ? 292  ASN A C   1 
ATOM   2007  O  O   . ASN A 1 300 ? -8.568  -6.366  -5.933  1.00 26.38 ? 292  ASN A O   1 
ATOM   2008  C  CB  . ASN A 1 300 ? -11.426 -6.615  -4.614  1.00 26.79 ? 292  ASN A CB  1 
ATOM   2009  C  CG  . ASN A 1 300 ? -11.573 -7.958  -3.937  1.00 27.78 ? 292  ASN A CG  1 
ATOM   2010  O  OD1 . ASN A 1 300 ? -11.056 -8.958  -4.416  1.00 26.13 ? 292  ASN A OD1 1 
ATOM   2011  N  ND2 . ASN A 1 300 ? -12.247 -7.978  -2.789  1.00 31.41 ? 292  ASN A ND2 1 
ATOM   2012  N  N   . ALA A 1 301 ? -8.267  -7.393  -3.946  1.00 22.38 ? 293  ALA A N   1 
ATOM   2013  C  CA  . ALA A 1 301 ? -7.025  -8.044  -4.343  1.00 20.31 ? 293  ALA A CA  1 
ATOM   2014  C  C   . ALA A 1 301 ? -7.143  -9.562  -4.424  1.00 27.37 ? 293  ALA A C   1 
ATOM   2015  O  O   . ALA A 1 301 ? -6.116  -10.245 -4.536  1.00 27.39 ? 293  ALA A O   1 
ATOM   2016  C  CB  . ALA A 1 301 ? -5.904  -7.664  -3.372  1.00 23.46 ? 293  ALA A CB  1 
ATOM   2017  N  N   . LYS A 1 302 ? -8.357  -10.115 -4.379  1.00 24.03 ? 294  LYS A N   1 
ATOM   2018  C  CA  . LYS A 1 302 ? -8.486  -11.571 -4.330  1.00 26.13 ? 294  LYS A CA  1 
ATOM   2019  C  C   . LYS A 1 302 ? -8.106  -12.226 -5.653  1.00 22.95 ? 294  LYS A C   1 
ATOM   2020  O  O   . LYS A 1 302 ? -7.445  -13.268 -5.660  1.00 24.04 ? 294  LYS A O   1 
ATOM   2021  C  CB  . LYS A 1 302 ? -9.902  -11.964 -3.913  1.00 27.93 ? 294  LYS A CB  1 
ATOM   2022  C  CG  . LYS A 1 302 ? -10.129 -11.670 -2.441  1.00 33.32 ? 294  LYS A CG  1 
ATOM   2023  C  CD  . LYS A 1 302 ? -11.336 -12.358 -1.859  1.00 39.13 ? 294  LYS A CD  1 
ATOM   2024  C  CE  . LYS A 1 302 ? -11.196 -12.416 -0.345  1.00 37.75 ? 294  LYS A CE  1 
ATOM   2025  N  NZ  . LYS A 1 302 ? -12.435 -12.902 0.326   1.00 42.10 ? 294  LYS A NZ  1 
ATOM   2026  N  N   . GLU A 1 303 ? -8.518  -11.645 -6.779  1.00 25.67 ? 295  GLU A N   1 
ATOM   2027  C  CA  . GLU A 1 303 ? -8.176  -12.230 -8.074  1.00 28.02 ? 295  GLU A CA  1 
ATOM   2028  C  C   . GLU A 1 303 ? -6.666  -12.208 -8.299  1.00 28.71 ? 295  GLU A C   1 
ATOM   2029  O  O   . GLU A 1 303 ? -6.061  -13.224 -8.668  1.00 25.74 ? 295  GLU A O   1 
ATOM   2030  C  CB  . GLU A 1 303 ? -8.916  -11.484 -9.192  1.00 27.17 ? 295  GLU A CB  1 
ATOM   2031  C  CG  . GLU A 1 303 ? -8.710  -12.076 -10.581 1.00 47.03 ? 295  GLU A CG  1 
ATOM   2032  C  CD  . GLU A 1 303 ? -9.660  -11.496 -11.624 1.00 54.82 ? 295  GLU A CD  1 
ATOM   2033  O  OE1 . GLU A 1 303 ? -10.383 -10.528 -11.309 1.00 58.25 ? 295  GLU A OE1 1 
ATOM   2034  O  OE2 . GLU A 1 303 ? -9.687  -12.015 -12.759 1.00 57.21 ? 295  GLU A OE2 1 
ATOM   2035  N  N   . LYS A 1 304 ? -6.041  -11.052 -8.065  1.00 28.47 ? 296  LYS A N   1 
ATOM   2036  C  CA  . LYS A 1 304 ? -4.597  -10.910 -8.247  1.00 27.34 ? 296  LYS A CA  1 
ATOM   2037  C  C   . LYS A 1 304 ? -3.820  -11.709 -7.202  1.00 23.85 ? 296  LYS A C   1 
ATOM   2038  O  O   . LYS A 1 304 ? -2.801  -12.336 -7.517  1.00 21.92 ? 296  LYS A O   1 
ATOM   2039  C  CB  . LYS A 1 304 ? -4.232  -9.429  -8.186  1.00 33.36 ? 296  LYS A CB  1 
ATOM   2040  C  CG  . LYS A 1 304 ? -2.811  -9.082  -8.543  1.00 40.00 ? 296  LYS A CG  1 
ATOM   2041  C  CD  . LYS A 1 304 ? -2.686  -7.573  -8.667  1.00 43.70 ? 296  LYS A CD  1 
ATOM   2042  C  CE  . LYS A 1 304 ? -1.408  -7.170  -9.376  1.00 49.07 ? 296  LYS A CE  1 
ATOM   2043  N  NZ  . LYS A 1 304 ? -1.538  -5.818  -9.997  1.00 52.64 ? 296  LYS A NZ  1 
ATOM   2044  N  N   . GLY A 1 305 ? -4.289  -11.700 -5.955  1.00 21.89 ? 297  GLY A N   1 
ATOM   2045  C  CA  . GLY A 1 305 ? -3.655  -12.512 -4.930  1.00 24.88 ? 297  GLY A CA  1 
ATOM   2046  C  C   . GLY A 1 305 ? -3.699  -13.996 -5.244  1.00 22.03 ? 297  GLY A C   1 
ATOM   2047  O  O   . GLY A 1 305 ? -2.708  -14.707 -5.068  1.00 21.61 ? 297  GLY A O   1 
ATOM   2048  N  N   . ALA A 1 306 ? -4.846  -14.487 -5.716  1.00 22.65 ? 298  ALA A N   1 
ATOM   2049  C  CA  . ALA A 1 306 ? -4.942  -15.903 -6.056  1.00 29.18 ? 298  ALA A CA  1 
ATOM   2050  C  C   . ALA A 1 306 ? -3.961  -16.271 -7.164  1.00 30.93 ? 298  ALA A C   1 
ATOM   2051  O  O   . ALA A 1 306 ? -3.298  -17.313 -7.100  1.00 26.61 ? 298  ALA A O   1 
ATOM   2052  C  CB  . ALA A 1 306 ? -6.373  -16.252 -6.473  1.00 27.53 ? 298  ALA A CB  1 
ATOM   2053  N  N   . LYS A 1 307 ? -3.852  -15.421 -8.190  1.00 28.90 ? 299  LYS A N   1 
ATOM   2054  C  CA  . LYS A 1 307 ? -2.940  -15.711 -9.289  1.00 32.80 ? 299  LYS A CA  1 
ATOM   2055  C  C   . LYS A 1 307 ? -1.496  -15.678 -8.813  1.00 27.81 ? 299  LYS A C   1 
ATOM   2056  O  O   . LYS A 1 307 ? -0.669  -16.479 -9.267  1.00 24.38 ? 299  LYS A O   1 
ATOM   2057  C  CB  . LYS A 1 307 ? -3.161  -14.722 -10.434 1.00 32.49 ? 299  LYS A CB  1 
ATOM   2058  N  N   . LEU A 1 308 ? -1.188  -14.767 -7.885  1.00 24.17 ? 300  LEU A N   1 
ATOM   2059  C  CA  . LEU A 1 308 ? 0.139   -14.706 -7.286  1.00 23.39 ? 300  LEU A CA  1 
ATOM   2060  C  C   . LEU A 1 308 ? 0.500   -16.023 -6.605  1.00 24.88 ? 300  LEU A C   1 
ATOM   2061  O  O   . LEU A 1 308 ? 1.550   -16.614 -6.883  1.00 25.34 ? 300  LEU A O   1 
ATOM   2062  C  CB  . LEU A 1 308 ? 0.190   -13.547 -6.286  1.00 22.24 ? 300  LEU A CB  1 
ATOM   2063  C  CG  . LEU A 1 308 ? 1.456   -13.382 -5.445  1.00 20.81 ? 300  LEU A CG  1 
ATOM   2064  C  CD1 . LEU A 1 308 ? 2.580   -12.810 -6.291  1.00 23.55 ? 300  LEU A CD1 1 
ATOM   2065  C  CD2 . LEU A 1 308 ? 1.184   -12.497 -4.233  1.00 19.05 ? 300  LEU A CD2 1 
ATOM   2066  N  N   . GLU A 1 309 ? -0.355  -16.492 -5.692  1.00 22.95 ? 301  GLU A N   1 
ATOM   2067  C  CA  . GLU A 1 309 ? -0.020  -17.700 -4.941  1.00 25.64 ? 301  GLU A CA  1 
ATOM   2068  C  C   . GLU A 1 309 ? -0.015  -18.929 -5.837  1.00 28.79 ? 301  GLU A C   1 
ATOM   2069  O  O   . GLU A 1 309 ? 0.798   -19.838 -5.640  1.00 25.96 ? 301  GLU A O   1 
ATOM   2070  C  CB  . GLU A 1 309 ? -0.994  -17.886 -3.776  1.00 25.35 ? 301  GLU A CB  1 
ATOM   2071  C  CG  . GLU A 1 309 ? -0.775  -19.163 -2.973  1.00 25.72 ? 301  GLU A CG  1 
ATOM   2072  C  CD  . GLU A 1 309 ? -1.340  -19.066 -1.557  1.00 28.63 ? 301  GLU A CD  1 
ATOM   2073  O  OE1 . GLU A 1 309 ? -1.863  -17.987 -1.209  1.00 26.76 ? 301  GLU A OE1 1 
ATOM   2074  O  OE2 . GLU A 1 309 ? -1.265  -20.059 -0.803  1.00 27.94 ? 301  GLU A OE2 1 
ATOM   2075  N  N   . ALA A 1 310 ? -0.905  -18.971 -6.828  1.00 29.87 ? 302  ALA A N   1 
ATOM   2076  C  CA  . ALA A 1 310 ? -0.877  -20.064 -7.794  1.00 26.05 ? 302  ALA A CA  1 
ATOM   2077  C  C   . ALA A 1 310 ? 0.447   -20.091 -8.543  1.00 27.35 ? 302  ALA A C   1 
ATOM   2078  O  O   . ALA A 1 310 ? 1.049   -21.157 -8.721  1.00 26.83 ? 302  ALA A O   1 
ATOM   2079  C  CB  . ALA A 1 310 ? -2.049  -19.936 -8.767  1.00 27.00 ? 302  ALA A CB  1 
ATOM   2080  N  N   . GLY A 1 311 ? 0.926   -18.922 -8.974  1.00 29.36 ? 303  GLY A N   1 
ATOM   2081  C  CA  . GLY A 1 311 ? 2.212   -18.870 -9.649  1.00 29.91 ? 303  GLY A CA  1 
ATOM   2082  C  C   . GLY A 1 311 ? 3.356   -19.325 -8.763  1.00 28.72 ? 303  GLY A C   1 
ATOM   2083  O  O   . GLY A 1 311 ? 4.230   -20.078 -9.199  1.00 28.31 ? 303  GLY A O   1 
ATOM   2084  N  N   . TRP A 1 312 ? 3.361   -18.887 -7.501  1.00 23.72 ? 304  TRP A N   1 
ATOM   2085  C  CA  . TRP A 1 312 ? 4.373   -19.376 -6.570  1.00 23.35 ? 304  TRP A CA  1 
ATOM   2086  C  C   . TRP A 1 312 ? 4.238   -20.883 -6.347  1.00 34.88 ? 304  TRP A C   1 
ATOM   2087  O  O   . TRP A 1 312 ? 5.244   -21.599 -6.285  1.00 32.52 ? 304  TRP A O   1 
ATOM   2088  C  CB  . TRP A 1 312 ? 4.295   -18.619 -5.242  1.00 22.19 ? 304  TRP A CB  1 
ATOM   2089  C  CG  . TRP A 1 312 ? 5.421   -19.005 -4.315  1.00 21.84 ? 304  TRP A CG  1 
ATOM   2090  C  CD1 . TRP A 1 312 ? 6.656   -18.425 -4.234  1.00 22.16 ? 304  TRP A CD1 1 
ATOM   2091  C  CD2 . TRP A 1 312 ? 5.426   -20.093 -3.385  1.00 23.43 ? 304  TRP A CD2 1 
ATOM   2092  N  NE1 . TRP A 1 312 ? 7.427   -19.075 -3.294  1.00 21.23 ? 304  TRP A NE1 1 
ATOM   2093  C  CE2 . TRP A 1 312 ? 6.692   -20.104 -2.759  1.00 21.85 ? 304  TRP A CE2 1 
ATOM   2094  C  CE3 . TRP A 1 312 ? 4.479   -21.058 -3.013  1.00 24.37 ? 304  TRP A CE3 1 
ATOM   2095  C  CZ2 . TRP A 1 312 ? 7.031   -21.038 -1.783  1.00 22.21 ? 304  TRP A CZ2 1 
ATOM   2096  C  CZ3 . TRP A 1 312 ? 4.820   -21.985 -2.042  1.00 23.40 ? 304  TRP A CZ3 1 
ATOM   2097  C  CH2 . TRP A 1 312 ? 6.081   -21.968 -1.438  1.00 30.39 ? 304  TRP A CH2 1 
ATOM   2098  N  N   . ASN A 1 313 ? 3.003   -21.388 -6.247  1.00 25.08 ? 305  ASN A N   1 
ATOM   2099  C  CA  . ASN A 1 313 ? 2.821   -22.823 -6.031  1.00 29.78 ? 305  ASN A CA  1 
ATOM   2100  C  C   . ASN A 1 313 ? 3.396   -23.642 -7.180  1.00 31.99 ? 305  ASN A C   1 
ATOM   2101  O  O   . ASN A 1 313 ? 3.921   -24.741 -6.955  1.00 31.34 ? 305  ASN A O   1 
ATOM   2102  C  CB  . ASN A 1 313 ? 1.340   -23.160 -5.839  1.00 32.26 ? 305  ASN A CB  1 
ATOM   2103  C  CG  . ASN A 1 313 ? 0.856   -22.872 -4.430  1.00 35.86 ? 305  ASN A CG  1 
ATOM   2104  O  OD1 . ASN A 1 313 ? 1.648   -22.795 -3.499  1.00 33.12 ? 305  ASN A OD1 1 
ATOM   2105  N  ND2 . ASN A 1 313 ? -0.453  -22.715 -4.270  1.00 35.55 ? 305  ASN A ND2 1 
ATOM   2106  N  N   . GLU A 1 314 ? 3.312   -23.128 -8.411  1.00 27.69 ? 306  GLU A N   1 
ATOM   2107  C  CA  . GLU A 1 314 ? 3.911   -23.829 -9.546  1.00 28.87 ? 306  GLU A CA  1 
ATOM   2108  C  C   . GLU A 1 314 ? 5.428   -23.854 -9.428  1.00 28.41 ? 306  GLU A C   1 
ATOM   2109  O  O   . GLU A 1 314 ? 6.067   -24.870 -9.728  1.00 39.47 ? 306  GLU A O   1 
ATOM   2110  C  CB  . GLU A 1 314 ? 3.487   -23.171 -10.865 1.00 32.83 ? 306  GLU A CB  1 
ATOM   2111  C  CG  . GLU A 1 314 ? 1.993   -23.221 -11.160 1.00 42.39 ? 306  GLU A CG  1 
ATOM   2112  C  CD  . GLU A 1 314 ? 1.584   -22.291 -12.298 1.00 56.08 ? 306  GLU A CD  1 
ATOM   2113  O  OE1 . GLU A 1 314 ? 2.463   -21.890 -13.095 1.00 59.80 ? 306  GLU A OE1 1 
ATOM   2114  O  OE2 . GLU A 1 314 ? 0.382   -21.956 -12.393 1.00 61.82 ? 306  GLU A OE2 1 
ATOM   2115  N  N   . LEU A 1 315 ? 6.019   -22.746 -8.983  1.00 27.01 ? 307  LEU A N   1 
ATOM   2116  C  CA  . LEU A 1 315 ? 7.460   -22.704 -8.781  1.00 31.45 ? 307  LEU A CA  1 
ATOM   2117  C  C   . LEU A 1 315 ? 7.879   -23.672 -7.684  1.00 32.14 ? 307  LEU A C   1 
ATOM   2118  O  O   . LEU A 1 315 ? 8.859   -24.413 -7.834  1.00 27.43 ? 307  LEU A O   1 
ATOM   2119  C  CB  . LEU A 1 315 ? 7.887   -21.277 -8.438  1.00 30.08 ? 307  LEU A CB  1 
ATOM   2120  C  CG  . LEU A 1 315 ? 9.381   -21.020 -8.256  1.00 32.13 ? 307  LEU A CG  1 
ATOM   2121  C  CD1 . LEU A 1 315 ? 10.107  -21.149 -9.590  1.00 36.54 ? 307  LEU A CD1 1 
ATOM   2122  C  CD2 . LEU A 1 315 ? 9.602   -19.651 -7.639  1.00 31.27 ? 307  LEU A CD2 1 
ATOM   2123  N  N   . PHE A 1 316 ? 7.134   -23.689 -6.577  1.00 26.40 ? 308  PHE A N   1 
ATOM   2124  C  CA  . PHE A 1 316 ? 7.462   -24.592 -5.483  1.00 26.70 ? 308  PHE A CA  1 
ATOM   2125  C  C   . PHE A 1 316 ? 7.314   -26.054 -5.896  1.00 28.39 ? 308  PHE A C   1 
ATOM   2126  O  O   . PHE A 1 316 ? 8.049   -26.914 -5.400  1.00 29.86 ? 308  PHE A O   1 
ATOM   2127  C  CB  . PHE A 1 316 ? 6.585   -24.281 -4.267  1.00 26.03 ? 308  PHE A CB  1 
ATOM   2128  C  CG  . PHE A 1 316 ? 7.048   -24.961 -3.008  1.00 28.09 ? 308  PHE A CG  1 
ATOM   2129  C  CD1 . PHE A 1 316 ? 8.212   -24.557 -2.379  1.00 29.38 ? 308  PHE A CD1 1 
ATOM   2130  C  CD2 . PHE A 1 316 ? 6.338   -26.016 -2.475  1.00 30.80 ? 308  PHE A CD2 1 
ATOM   2131  C  CE1 . PHE A 1 316 ? 8.646   -25.179 -1.227  1.00 29.01 ? 308  PHE A CE1 1 
ATOM   2132  C  CE2 . PHE A 1 316 ? 6.771   -26.643 -1.329  1.00 27.42 ? 308  PHE A CE2 1 
ATOM   2133  C  CZ  . PHE A 1 316 ? 7.926   -26.222 -0.704  1.00 29.37 ? 308  PHE A CZ  1 
ATOM   2134  N  N   . ALA A 1 317 ? 6.384   -26.356 -6.806  1.00 31.15 ? 309  ALA A N   1 
ATOM   2135  C  CA  . ALA A 1 317 ? 6.259   -27.725 -7.303  1.00 31.79 ? 309  ALA A CA  1 
ATOM   2136  C  C   . ALA A 1 317 ? 7.486   -28.131 -8.116  1.00 31.71 ? 309  ALA A C   1 
ATOM   2137  O  O   . ALA A 1 317 ? 7.999   -29.247 -7.961  1.00 32.85 ? 309  ALA A O   1 
ATOM   2138  C  CB  . ALA A 1 317 ? 4.986   -27.871 -8.136  1.00 32.01 ? 309  ALA A CB  1 
ATOM   2139  N  N   . GLN A 1 318 ? 7.964   -27.245 -8.994  1.00 31.87 ? 310  GLN A N   1 
ATOM   2140  C  CA  . GLN A 1 318 ? 9.230   -27.497 -9.676  1.00 34.14 ? 310  GLN A CA  1 
ATOM   2141  C  C   . GLN A 1 318 ? 10.353  -27.702 -8.671  1.00 31.03 ? 310  GLN A C   1 
ATOM   2142  O  O   . GLN A 1 318 ? 11.198  -28.589 -8.842  1.00 32.01 ? 310  GLN A O   1 
ATOM   2143  C  CB  . GLN A 1 318 ? 9.585   -26.338 -10.602 1.00 39.14 ? 310  GLN A CB  1 
ATOM   2144  C  CG  . GLN A 1 318 ? 8.695   -26.149 -11.802 1.00 46.71 ? 310  GLN A CG  1 
ATOM   2145  C  CD  . GLN A 1 318 ? 9.104   -24.925 -12.601 1.00 52.68 ? 310  GLN A CD  1 
ATOM   2146  O  OE1 . GLN A 1 318 ? 8.440   -23.887 -12.556 1.00 55.17 ? 310  GLN A OE1 1 
ATOM   2147  N  NE2 . GLN A 1 318 ? 10.216  -25.034 -13.322 1.00 52.66 ? 310  GLN A NE2 1 
ATOM   2148  N  N   . TYR A 1 319 ? 10.382  -26.874 -7.623  1.00 29.61 ? 311  TYR A N   1 
ATOM   2149  C  CA  . TYR A 1 319 ? 11.379  -27.025 -6.571  1.00 36.95 ? 311  TYR A CA  1 
ATOM   2150  C  C   . TYR A 1 319 ? 11.210  -28.358 -5.857  1.00 33.84 ? 311  TYR A C   1 
ATOM   2151  O  O   . TYR A 1 319 ? 12.178  -29.103 -5.671  1.00 35.34 ? 311  TYR A O   1 
ATOM   2152  C  CB  . TYR A 1 319 ? 11.261  -25.862 -5.582  1.00 27.58 ? 311  TYR A CB  1 
ATOM   2153  C  CG  . TYR A 1 319 ? 12.336  -25.801 -4.525  1.00 27.07 ? 311  TYR A CG  1 
ATOM   2154  C  CD1 . TYR A 1 319 ? 12.172  -26.443 -3.301  1.00 27.31 ? 311  TYR A CD1 1 
ATOM   2155  C  CD2 . TYR A 1 319 ? 13.504  -25.075 -4.735  1.00 26.42 ? 311  TYR A CD2 1 
ATOM   2156  C  CE1 . TYR A 1 319 ? 13.148  -26.373 -2.320  1.00 32.53 ? 311  TYR A CE1 1 
ATOM   2157  C  CE2 . TYR A 1 319 ? 14.490  -25.001 -3.755  1.00 26.04 ? 311  TYR A CE2 1 
ATOM   2158  C  CZ  . TYR A 1 319 ? 14.306  -25.654 -2.555  1.00 28.03 ? 311  TYR A CZ  1 
ATOM   2159  O  OH  . TYR A 1 319 ? 15.273  -25.581 -1.574  1.00 31.22 ? 311  TYR A OH  1 
ATOM   2160  N  N   . GLN A 1 320 ? 9.975   -28.682 -5.468  1.00 30.73 ? 312  GLN A N   1 
ATOM   2161  C  CA  . GLN A 1 320 ? 9.730   -29.915 -4.729  1.00 34.70 ? 312  GLN A CA  1 
ATOM   2162  C  C   . GLN A 1 320 ? 10.096  -31.147 -5.547  1.00 36.80 ? 312  GLN A C   1 
ATOM   2163  O  O   . GLN A 1 320 ? 10.524  -32.159 -4.979  1.00 37.70 ? 312  GLN A O   1 
ATOM   2164  C  CB  . GLN A 1 320 ? 8.269   -29.982 -4.285  1.00 32.09 ? 312  GLN A CB  1 
ATOM   2165  N  N   . ALA A 1 321 ? 9.946   -31.083 -6.874  1.00 34.28 ? 313  ALA A N   1 
ATOM   2166  C  CA  . ALA A 1 321 ? 10.338  -32.210 -7.714  1.00 36.09 ? 313  ALA A CA  1 
ATOM   2167  C  C   . ALA A 1 321 ? 11.842  -32.434 -7.672  1.00 38.56 ? 313  ALA A C   1 
ATOM   2168  O  O   . ALA A 1 321 ? 12.305  -33.579 -7.630  1.00 37.66 ? 313  ALA A O   1 
ATOM   2169  C  CB  . ALA A 1 321 ? 9.872   -31.983 -9.151  1.00 36.57 ? 313  ALA A CB  1 
ATOM   2170  N  N   . LYS A 1 322 ? 12.622  -31.353 -7.669  1.00 40.13 ? 314  LYS A N   1 
ATOM   2171  C  CA  . LYS A 1 322 ? 14.073  -31.474 -7.672  1.00 37.11 ? 314  LYS A CA  1 
ATOM   2172  C  C   . LYS A 1 322 ? 14.670  -31.539 -6.274  1.00 34.29 ? 314  LYS A C   1 
ATOM   2173  O  O   . LYS A 1 322 ? 15.702  -32.192 -6.086  1.00 34.96 ? 314  LYS A O   1 
ATOM   2174  C  CB  . LYS A 1 322 ? 14.700  -30.308 -8.440  1.00 45.72 ? 314  LYS A CB  1 
ATOM   2175  N  N   . TYR A 1 323 ? 14.055  -30.895 -5.284  1.00 31.15 ? 315  TYR A N   1 
ATOM   2176  C  CA  . TYR A 1 323 ? 14.605  -30.824 -3.928  1.00 30.88 ? 315  TYR A CA  1 
ATOM   2177  C  C   . TYR A 1 323 ? 13.528  -31.161 -2.904  1.00 35.53 ? 315  TYR A C   1 
ATOM   2178  O  O   . TYR A 1 323 ? 13.106  -30.298 -2.123  1.00 30.17 ? 315  TYR A O   1 
ATOM   2179  C  CB  . TYR A 1 323 ? 15.199  -29.439 -3.671  1.00 27.11 ? 315  TYR A CB  1 
ATOM   2180  C  CG  . TYR A 1 323 ? 16.177  -29.033 -4.742  1.00 31.10 ? 315  TYR A CG  1 
ATOM   2181  C  CD1 . TYR A 1 323 ? 17.472  -29.524 -4.739  1.00 36.71 ? 315  TYR A CD1 1 
ATOM   2182  C  CD2 . TYR A 1 323 ? 15.801  -28.179 -5.770  1.00 34.35 ? 315  TYR A CD2 1 
ATOM   2183  C  CE1 . TYR A 1 323 ? 18.374  -29.169 -5.720  1.00 41.28 ? 315  TYR A CE1 1 
ATOM   2184  C  CE2 . TYR A 1 323 ? 16.704  -27.814 -6.766  1.00 37.61 ? 315  TYR A CE2 1 
ATOM   2185  C  CZ  . TYR A 1 323 ? 17.987  -28.315 -6.730  1.00 41.40 ? 315  TYR A CZ  1 
ATOM   2186  O  OH  . TYR A 1 323 ? 18.893  -27.968 -7.699  1.00 52.87 ? 315  TYR A OH  1 
ATOM   2187  N  N   . PRO A 1 324 ? 13.085  -32.425 -2.860  1.00 37.09 ? 316  PRO A N   1 
ATOM   2188  C  CA  . PRO A 1 324 ? 11.933  -32.760 -2.001  1.00 35.44 ? 316  PRO A CA  1 
ATOM   2189  C  C   . PRO A 1 324 ? 12.221  -32.671 -0.514  1.00 31.91 ? 316  PRO A C   1 
ATOM   2190  O  O   . PRO A 1 324 ? 11.344  -32.242 0.243   1.00 30.95 ? 316  PRO A O   1 
ATOM   2191  C  CB  . PRO A 1 324 ? 11.583  -34.195 -2.426  1.00 34.76 ? 316  PRO A CB  1 
ATOM   2192  C  CG  . PRO A 1 324 ? 12.835  -34.729 -3.030  1.00 33.90 ? 316  PRO A CG  1 
ATOM   2193  C  CD  . PRO A 1 324 ? 13.514  -33.569 -3.680  1.00 37.53 ? 316  PRO A CD  1 
ATOM   2194  N  N   . ALA A 1 325 ? 13.412  -33.086 -0.065  1.00 30.09 ? 317  ALA A N   1 
ATOM   2195  C  CA  . ALA A 1 325 ? 13.744  -32.970 1.352   1.00 29.54 ? 317  ALA A CA  1 
ATOM   2196  C  C   . ALA A 1 325 ? 13.834  -31.509 1.779   1.00 27.23 ? 317  ALA A C   1 
ATOM   2197  O  O   . ALA A 1 325 ? 13.318  -31.133 2.839   1.00 24.92 ? 317  ALA A O   1 
ATOM   2198  C  CB  . ALA A 1 325 ? 15.055  -33.696 1.653   1.00 31.00 ? 317  ALA A CB  1 
ATOM   2199  N  N   . GLU A 1 326 ? 14.488  -30.672 0.963   1.00 30.02 ? 318  GLU A N   1 
ATOM   2200  C  CA  . GLU A 1 326 ? 14.517  -29.236 1.224   1.00 25.84 ? 318  GLU A CA  1 
ATOM   2201  C  C   . GLU A 1 326 ? 13.117  -28.639 1.193   1.00 26.44 ? 318  GLU A C   1 
ATOM   2202  O  O   . GLU A 1 326 ? 12.780  -27.788 2.025   1.00 22.37 ? 318  GLU A O   1 
ATOM   2203  C  CB  . GLU A 1 326 ? 15.403  -28.528 0.198   1.00 31.66 ? 318  GLU A CB  1 
ATOM   2204  C  CG  . GLU A 1 326 ? 16.886  -28.832 0.309   1.00 34.54 ? 318  GLU A CG  1 
ATOM   2205  C  CD  . GLU A 1 326 ? 17.307  -30.056 -0.475  1.00 38.89 ? 318  GLU A CD  1 
ATOM   2206  O  OE1 . GLU A 1 326 ? 16.440  -30.895 -0.802  1.00 39.11 ? 318  GLU A OE1 1 
ATOM   2207  O  OE2 . GLU A 1 326 ? 18.514  -30.172 -0.768  1.00 40.49 ? 318  GLU A OE2 1 
ATOM   2208  N  N   . ALA A 1 327 ? 12.294  -29.056 0.223   1.00 29.50 ? 319  ALA A N   1 
ATOM   2209  C  CA  . ALA A 1 327 ? 10.926  -28.549 0.139   1.00 27.04 ? 319  ALA A CA  1 
ATOM   2210  C  C   . ALA A 1 327 ? 10.146  -28.874 1.406   1.00 27.76 ? 319  ALA A C   1 
ATOM   2211  O  O   . ALA A 1 327 ? 9.441   -28.017 1.952   1.00 23.90 ? 319  ALA A O   1 
ATOM   2212  C  CB  . ALA A 1 327 ? 10.217  -29.125 -1.093  1.00 24.79 ? 319  ALA A CB  1 
ATOM   2213  N  N   . ALA A 1 328 ? 10.282  -30.104 1.899   1.00 27.43 ? 320  ALA A N   1 
ATOM   2214  C  CA  . ALA A 1 328 ? 9.581   -30.492 3.118   1.00 23.64 ? 320  ALA A CA  1 
ATOM   2215  C  C   . ALA A 1 328 ? 10.105  -29.722 4.326   1.00 26.26 ? 320  ALA A C   1 
ATOM   2216  O  O   . ALA A 1 328 ? 9.333   -29.356 5.221   1.00 26.63 ? 320  ALA A O   1 
ATOM   2217  C  CB  . ALA A 1 328 ? 9.714   -32.001 3.334   1.00 24.73 ? 320  ALA A CB  1 
ATOM   2218  N  N   . GLU A 1 329 ? 11.410  -29.466 4.375   1.00 25.42 ? 321  GLU A N   1 
ATOM   2219  C  CA  . GLU A 1 329 ? 11.940  -28.672 5.478   1.00 22.74 ? 321  GLU A CA  1 
ATOM   2220  C  C   . GLU A 1 329 ? 11.460  -27.229 5.405   1.00 23.74 ? 321  GLU A C   1 
ATOM   2221  O  O   . GLU A 1 329 ? 11.233  -26.601 6.443   1.00 23.47 ? 321  GLU A O   1 
ATOM   2222  C  CB  . GLU A 1 329 ? 13.461  -28.726 5.483   1.00 25.00 ? 321  GLU A CB  1 
ATOM   2223  C  CG  . GLU A 1 329 ? 14.007  -29.959 6.179   1.00 28.46 ? 321  GLU A CG  1 
ATOM   2224  C  CD  . GLU A 1 329 ? 13.732  -29.941 7.674   1.00 28.88 ? 321  GLU A CD  1 
ATOM   2225  O  OE1 . GLU A 1 329 ? 14.418  -29.185 8.390   1.00 29.33 ? 321  GLU A OE1 1 
ATOM   2226  O  OE2 . GLU A 1 329 ? 12.817  -30.667 8.128   1.00 29.41 ? 321  GLU A OE2 1 
ATOM   2227  N  N   . PHE A 1 330 ? 11.292  -26.692 4.195   1.00 23.39 ? 322  PHE A N   1 
ATOM   2228  C  CA  . PHE A 1 330 ? 10.818  -25.321 4.056   1.00 25.22 ? 322  PHE A CA  1 
ATOM   2229  C  C   . PHE A 1 330 ? 9.407   -25.183 4.618   1.00 23.73 ? 322  PHE A C   1 
ATOM   2230  O  O   . PHE A 1 330 ? 9.116   -24.259 5.387   1.00 23.07 ? 322  PHE A O   1 
ATOM   2231  C  CB  . PHE A 1 330 ? 10.876  -24.906 2.580   1.00 24.88 ? 322  PHE A CB  1 
ATOM   2232  C  CG  . PHE A 1 330 ? 10.481  -23.484 2.339   1.00 25.11 ? 322  PHE A CG  1 
ATOM   2233  C  CD1 . PHE A 1 330 ? 11.356  -22.447 2.637   1.00 18.75 ? 322  PHE A CD1 1 
ATOM   2234  C  CD2 . PHE A 1 330 ? 9.237   -23.178 1.804   1.00 23.44 ? 322  PHE A CD2 1 
ATOM   2235  C  CE1 . PHE A 1 330 ? 10.994  -21.133 2.412   1.00 23.24 ? 322  PHE A CE1 1 
ATOM   2236  C  CE2 . PHE A 1 330 ? 8.867   -21.864 1.585   1.00 18.98 ? 322  PHE A CE2 1 
ATOM   2237  C  CZ  . PHE A 1 330 ? 9.745   -20.841 1.888   1.00 20.78 ? 322  PHE A CZ  1 
ATOM   2238  N  N   . VAL A 1 331 ? 8.524   -26.115 4.261   1.00 22.84 ? 323  VAL A N   1 
ATOM   2239  C  CA  . VAL A 1 331 ? 7.152   -26.088 4.758   1.00 24.39 ? 323  VAL A CA  1 
ATOM   2240  C  C   . VAL A 1 331 ? 7.131   -26.234 6.273   1.00 26.84 ? 323  VAL A C   1 
ATOM   2241  O  O   . VAL A 1 331 ? 6.451   -25.476 6.976   1.00 25.91 ? 323  VAL A O   1 
ATOM   2242  C  CB  . VAL A 1 331 ? 6.316   -27.184 4.075   1.00 25.52 ? 323  VAL A CB  1 
ATOM   2243  C  CG1 . VAL A 1 331 ? 4.981   -27.375 4.795   1.00 25.39 ? 323  VAL A CG1 1 
ATOM   2244  C  CG2 . VAL A 1 331 ? 6.096   -26.840 2.611   1.00 25.09 ? 323  VAL A CG2 1 
ATOM   2245  N  N   . ARG A 1 332 ? 7.874   -27.215 6.797   1.00 19.79 ? 324  ARG A N   1 
ATOM   2246  C  CA  . ARG A 1 332 ? 7.931   -27.405 8.244   1.00 24.03 ? 324  ARG A CA  1 
ATOM   2247  C  C   . ARG A 1 332 ? 8.334   -26.119 8.947   1.00 23.05 ? 324  ARG A C   1 
ATOM   2248  O  O   . ARG A 1 332 ? 7.695   -25.698 9.920   1.00 22.27 ? 324  ARG A O   1 
ATOM   2249  C  CB  . ARG A 1 332 ? 8.915   -28.517 8.609   1.00 19.98 ? 324  ARG A CB  1 
ATOM   2250  C  CG  . ARG A 1 332 ? 8.993   -28.739 10.107  1.00 19.55 ? 324  ARG A CG  1 
ATOM   2251  C  CD  . ARG A 1 332 ? 10.071  -29.718 10.511  1.00 26.09 ? 324  ARG A CD  1 
ATOM   2252  N  NE  . ARG A 1 332 ? 11.439  -29.286 10.223  1.00 23.11 ? 324  ARG A NE  1 
ATOM   2253  C  CZ  . ARG A 1 332 ? 12.181  -28.498 11.007  1.00 20.25 ? 324  ARG A CZ  1 
ATOM   2254  N  NH1 . ARG A 1 332 ? 11.692  -27.994 12.140  1.00 20.62 ? 324  ARG A NH1 1 
ATOM   2255  N  NH2 . ARG A 1 332 ? 13.427  -28.209 10.649  1.00 22.55 ? 324  ARG A NH2 1 
ATOM   2256  N  N   . ARG A 1 333 ? 9.391   -25.475 8.451   1.00 17.95 ? 325  ARG A N   1 
ATOM   2257  C  CA  . ARG A 1 333 ? 9.962   -24.329 9.142   1.00 16.99 ? 325  ARG A CA  1 
ATOM   2258  C  C   . ARG A 1 333 ? 9.119   -23.079 8.945   1.00 16.39 ? 325  ARG A C   1 
ATOM   2259  O  O   . ARG A 1 333 ? 8.958   -22.289 9.880   1.00 17.81 ? 325  ARG A O   1 
ATOM   2260  C  CB  . ARG A 1 333 ? 11.404  -24.109 8.671   1.00 17.25 ? 325  ARG A CB  1 
ATOM   2261  C  CG  . ARG A 1 333 ? 12.361  -25.187 9.198   1.00 18.09 ? 325  ARG A CG  1 
ATOM   2262  C  CD  . ARG A 1 333 ? 13.710  -25.168 8.481   1.00 21.73 ? 325  ARG A CD  1 
ATOM   2263  N  NE  . ARG A 1 333 ? 14.296  -23.835 8.472   1.00 17.16 ? 325  ARG A NE  1 
ATOM   2264  C  CZ  . ARG A 1 333 ? 15.519  -23.546 8.045   1.00 20.55 ? 325  ARG A CZ  1 
ATOM   2265  N  NH1 . ARG A 1 333 ? 16.309  -24.507 7.591   1.00 19.28 ? 325  ARG A NH1 1 
ATOM   2266  N  NH2 . ARG A 1 333 ? 15.953  -22.289 8.080   1.00 19.85 ? 325  ARG A NH2 1 
ATOM   2267  N  N   . MET A 1 334 ? 8.565   -22.883 7.744   1.00 18.90 ? 326  MET A N   1 
ATOM   2268  C  CA  . MET A 1 334 ? 7.666   -21.755 7.550   1.00 18.24 ? 326  MET A CA  1 
ATOM   2269  C  C   . MET A 1 334 ? 6.389   -21.933 8.354   1.00 19.08 ? 326  MET A C   1 
ATOM   2270  O  O   . MET A 1 334 ? 5.783   -20.945 8.772   1.00 19.86 ? 326  MET A O   1 
ATOM   2271  C  CB  . MET A 1 334 ? 7.334   -21.571 6.073   1.00 16.88 ? 326  MET A CB  1 
ATOM   2272  C  CG  . MET A 1 334 ? 8.497   -21.065 5.203   1.00 18.45 ? 326  MET A CG  1 
ATOM   2273  S  SD  . MET A 1 334 ? 9.143   -19.465 5.740   1.00 20.02 ? 326  MET A SD  1 
ATOM   2274  C  CE  . MET A 1 334 ? 7.660   -18.455 5.762   1.00 16.35 ? 326  MET A CE  1 
ATOM   2275  N  N   . ASP A 1 335 ? 5.953   -23.175 8.550   1.00 17.75 ? 327  ASP A N   1 
ATOM   2276  C  CA  . ASP A 1 335 ? 4.812   -23.477 9.407   1.00 19.47 ? 327  ASP A CA  1 
ATOM   2277  C  C   . ASP A 1 335 ? 5.147   -23.380 10.885  1.00 23.37 ? 327  ASP A C   1 
ATOM   2278  O  O   . ASP A 1 335 ? 4.257   -23.588 11.718  1.00 23.86 ? 327  ASP A O   1 
ATOM   2279  C  CB  . ASP A 1 335 ? 4.277   -24.880 9.125   1.00 18.80 ? 327  ASP A CB  1 
ATOM   2280  C  CG  . ASP A 1 335 ? 3.497   -24.962 7.836   1.00 24.66 ? 327  ASP A CG  1 
ATOM   2281  O  OD1 . ASP A 1 335 ? 3.218   -23.907 7.215   1.00 24.05 ? 327  ASP A OD1 1 
ATOM   2282  O  OD2 . ASP A 1 335 ? 3.181   -26.099 7.437   1.00 27.10 ? 327  ASP A OD2 1 
ATOM   2283  N  N   . LYS A 1 336 ? 6.406   -23.105 11.219  1.00 20.05 ? 328  LYS A N   1 
ATOM   2284  C  CA  . LYS A 1 336 ? 6.835   -22.923 12.599  1.00 20.85 ? 328  LYS A CA  1 
ATOM   2285  C  C   . LYS A 1 336 ? 6.607   -24.191 13.424  1.00 25.90 ? 328  LYS A C   1 
ATOM   2286  O  O   . LYS A 1 336 ? 6.147   -24.138 14.566  1.00 25.77 ? 328  LYS A O   1 
ATOM   2287  C  CB  . LYS A 1 336 ? 6.138   -21.708 13.224  1.00 23.58 ? 328  LYS A CB  1 
ATOM   2288  C  CG  . LYS A 1 336 ? 6.314   -20.421 12.404  1.00 24.06 ? 328  LYS A CG  1 
ATOM   2289  C  CD  . LYS A 1 336 ? 5.493   -19.248 12.952  1.00 28.73 ? 328  LYS A CD  1 
ATOM   2290  C  CE  . LYS A 1 336 ? 5.683   -17.979 12.090  1.00 29.19 ? 328  LYS A CE  1 
ATOM   2291  N  NZ  . LYS A 1 336 ? 4.876   -16.793 12.555  1.00 24.98 ? 328  LYS A NZ  1 
ATOM   2292  N  N   . LYS A 1 337 ? 6.947   -25.340 12.842  1.00 20.56 ? 329  LYS A N   1 
ATOM   2293  C  CA  . LYS A 1 337 ? 6.805   -26.638 13.486  1.00 26.07 ? 329  LYS A CA  1 
ATOM   2294  C  C   . LYS A 1 337 ? 8.178   -27.238 13.760  1.00 28.57 ? 329  LYS A C   1 
ATOM   2295  O  O   . LYS A 1 337 ? 9.131   -27.016 13.009  1.00 22.21 ? 329  LYS A O   1 
ATOM   2296  C  CB  . LYS A 1 337 ? 6.005   -27.615 12.615  1.00 28.75 ? 329  LYS A CB  1 
ATOM   2297  C  CG  . LYS A 1 337 ? 4.620   -27.151 12.217  1.00 31.48 ? 329  LYS A CG  1 
ATOM   2298  C  CD  . LYS A 1 337 ? 3.946   -28.210 11.344  1.00 35.35 ? 329  LYS A CD  1 
ATOM   2299  C  CE  . LYS A 1 337 ? 2.488   -27.872 11.085  1.00 36.74 ? 329  LYS A CE  1 
ATOM   2300  N  NZ  . LYS A 1 337 ? 1.756   -28.982 10.422  1.00 37.39 ? 329  LYS A NZ  1 
ATOM   2301  N  N   . LEU A 1 338 ? 8.264   -28.019 14.826  1.00 23.39 ? 330  LEU A N   1 
ATOM   2302  C  CA  . LEU A 1 338 ? 9.505   -28.688 15.177  1.00 23.05 ? 330  LEU A CA  1 
ATOM   2303  C  C   . LEU A 1 338 ? 9.600   -30.035 14.477  1.00 27.27 ? 330  LEU A C   1 
ATOM   2304  O  O   . LEU A 1 338 ? 8.588   -30.587 14.030  1.00 23.85 ? 330  LEU A O   1 
ATOM   2305  C  CB  . LEU A 1 338 ? 9.586   -28.876 16.694  1.00 24.97 ? 330  LEU A CB  1 
ATOM   2306  C  CG  . LEU A 1 338 ? 9.955   -27.628 17.496  1.00 25.27 ? 330  LEU A CG  1 
ATOM   2307  C  CD1 . LEU A 1 338 ? 10.056  -27.963 18.967  1.00 30.36 ? 330  LEU A CD1 1 
ATOM   2308  C  CD2 . LEU A 1 338 ? 11.255  -27.013 17.001  1.00 30.39 ? 330  LEU A CD2 1 
ATOM   2309  N  N   . PRO A 1 339 ? 10.806  -30.596 14.367  1.00 25.27 ? 331  PRO A N   1 
ATOM   2310  C  CA  . PRO A 1 339 ? 10.935  -31.944 13.811  1.00 28.93 ? 331  PRO A CA  1 
ATOM   2311  C  C   . PRO A 1 339 ? 10.149  -32.943 14.639  1.00 26.45 ? 331  PRO A C   1 
ATOM   2312  O  O   . PRO A 1 339 ? 10.033  -32.813 15.859  1.00 25.54 ? 331  PRO A O   1 
ATOM   2313  C  CB  . PRO A 1 339 ? 12.439  -32.227 13.892  1.00 29.69 ? 331  PRO A CB  1 
ATOM   2314  C  CG  . PRO A 1 339 ? 13.082  -30.898 14.036  1.00 30.71 ? 331  PRO A CG  1 
ATOM   2315  C  CD  . PRO A 1 339 ? 12.109  -30.037 14.765  1.00 29.39 ? 331  PRO A CD  1 
ATOM   2316  N  N   . GLU A 1 340 ? 9.619   -33.958 13.952  1.00 26.90 ? 332  GLU A N   1 
ATOM   2317  C  CA  . GLU A 1 340 ? 8.752   -34.938 14.599  1.00 29.76 ? 332  GLU A CA  1 
ATOM   2318  C  C   . GLU A 1 340 ? 9.444   -35.651 15.756  1.00 35.50 ? 332  GLU A C   1 
ATOM   2319  O  O   . GLU A 1 340 ? 8.783   -36.047 16.722  1.00 37.27 ? 332  GLU A O   1 
ATOM   2320  C  CB  . GLU A 1 340 ? 8.261   -35.958 13.569  1.00 35.60 ? 332  GLU A CB  1 
ATOM   2321  N  N   . ASN A 1 341 ? 10.762  -35.824 15.690  1.00 35.93 ? 333  ASN A N   1 
ATOM   2322  C  CA  . ASN A 1 341 ? 11.481  -36.584 16.704  1.00 40.35 ? 333  ASN A CA  1 
ATOM   2323  C  C   . ASN A 1 341 ? 12.105  -35.699 17.782  1.00 38.49 ? 333  ASN A C   1 
ATOM   2324  O  O   . ASN A 1 341 ? 13.027  -36.146 18.476  1.00 38.74 ? 333  ASN A O   1 
ATOM   2325  C  CB  . ASN A 1 341 ? 12.568  -37.437 16.050  1.00 43.82 ? 333  ASN A CB  1 
ATOM   2326  C  CG  . ASN A 1 341 ? 13.765  -36.615 15.612  1.00 50.47 ? 333  ASN A CG  1 
ATOM   2327  O  OD1 . ASN A 1 341 ? 13.622  -35.464 15.196  1.00 48.86 ? 333  ASN A OD1 1 
ATOM   2328  N  ND2 . ASN A 1 341 ? 14.954  -37.196 15.718  1.00 56.05 ? 333  ASN A ND2 1 
ATOM   2329  N  N   . PHE A 1 342 ? 11.622  -34.464 17.945  1.00 31.85 ? 334  PHE A N   1 
ATOM   2330  C  CA  . PHE A 1 342 ? 12.319  -33.518 18.816  1.00 30.95 ? 334  PHE A CA  1 
ATOM   2331  C  C   . PHE A 1 342 ? 12.429  -34.043 20.240  1.00 28.42 ? 334  PHE A C   1 
ATOM   2332  O  O   . PHE A 1 342 ? 13.516  -34.031 20.835  1.00 28.55 ? 334  PHE A O   1 
ATOM   2333  C  CB  . PHE A 1 342 ? 11.625  -32.156 18.810  1.00 25.07 ? 334  PHE A CB  1 
ATOM   2334  C  CG  . PHE A 1 342 ? 12.390  -31.088 19.559  1.00 24.88 ? 334  PHE A CG  1 
ATOM   2335  C  CD1 . PHE A 1 342 ? 13.560  -30.560 19.032  1.00 22.42 ? 334  PHE A CD1 1 
ATOM   2336  C  CD2 . PHE A 1 342 ? 11.954  -30.627 20.788  1.00 21.67 ? 334  PHE A CD2 1 
ATOM   2337  C  CE1 . PHE A 1 342 ? 14.282  -29.584 19.711  1.00 22.13 ? 334  PHE A CE1 1 
ATOM   2338  C  CE2 . PHE A 1 342 ? 12.673  -29.642 21.470  1.00 25.09 ? 334  PHE A CE2 1 
ATOM   2339  C  CZ  . PHE A 1 342 ? 13.839  -29.122 20.924  1.00 24.18 ? 334  PHE A CZ  1 
ATOM   2340  N  N   . ASP A 1 343 ? 11.314  -34.507 20.808  1.00 24.79 ? 335  ASP A N   1 
ATOM   2341  C  CA  . ASP A 1 343 ? 11.319  -34.904 22.214  1.00 29.96 ? 335  ASP A CA  1 
ATOM   2342  C  C   . ASP A 1 343 ? 12.209  -36.119 22.445  1.00 33.67 ? 335  ASP A C   1 
ATOM   2343  O  O   . ASP A 1 343 ? 12.949  -36.179 23.436  1.00 28.79 ? 335  ASP A O   1 
ATOM   2344  C  CB  . ASP A 1 343 ? 9.894   -35.190 22.689  1.00 36.43 ? 335  ASP A CB  1 
ATOM   2345  C  CG  . ASP A 1 343 ? 9.045   -33.934 22.795  1.00 42.99 ? 335  ASP A CG  1 
ATOM   2346  O  OD1 . ASP A 1 343 ? 9.597   -32.852 23.092  1.00 44.54 ? 335  ASP A OD1 1 
ATOM   2347  O  OD2 . ASP A 1 343 ? 7.817   -34.035 22.593  1.00 48.36 ? 335  ASP A OD2 1 
ATOM   2348  N  N   . GLU A 1 344 ? 12.140  -37.109 21.550  1.00 30.65 ? 336  GLU A N   1 
ATOM   2349  C  CA  . GLU A 1 344 ? 12.995  -38.282 21.696  1.00 31.41 ? 336  GLU A CA  1 
ATOM   2350  C  C   . GLU A 1 344 ? 14.459  -37.905 21.535  1.00 29.19 ? 336  GLU A C   1 
ATOM   2351  O  O   . GLU A 1 344 ? 15.331  -38.461 22.216  1.00 27.78 ? 336  GLU A O   1 
ATOM   2352  C  CB  . GLU A 1 344 ? 12.597  -39.357 20.682  1.00 34.71 ? 336  GLU A CB  1 
ATOM   2353  N  N   . TYR A 1 345 ? 14.744  -36.953 20.642  1.00 25.47 ? 337  TYR A N   1 
ATOM   2354  C  CA  . TYR A 1 345 ? 16.107  -36.460 20.480  1.00 28.49 ? 337  TYR A CA  1 
ATOM   2355  C  C   . TYR A 1 345 ? 16.602  -35.806 21.762  1.00 26.13 ? 337  TYR A C   1 
ATOM   2356  O  O   . TYR A 1 345 ? 17.719  -36.075 22.222  1.00 24.36 ? 337  TYR A O   1 
ATOM   2357  C  CB  . TYR A 1 345 ? 16.176  -35.465 19.323  1.00 25.48 ? 337  TYR A CB  1 
ATOM   2358  C  CG  . TYR A 1 345 ? 17.541  -34.831 19.185  1.00 26.11 ? 337  TYR A CG  1 
ATOM   2359  C  CD1 . TYR A 1 345 ? 18.564  -35.498 18.530  1.00 24.76 ? 337  TYR A CD1 1 
ATOM   2360  C  CD2 . TYR A 1 345 ? 17.812  -33.577 19.724  1.00 30.19 ? 337  TYR A CD2 1 
ATOM   2361  C  CE1 . TYR A 1 345 ? 19.812  -34.938 18.403  1.00 29.26 ? 337  TYR A CE1 1 
ATOM   2362  C  CE2 . TYR A 1 345 ? 19.067  -33.007 19.603  1.00 27.76 ? 337  TYR A CE2 1 
ATOM   2363  C  CZ  . TYR A 1 345 ? 20.061  -33.700 18.936  1.00 25.52 ? 337  TYR A CZ  1 
ATOM   2364  O  OH  . TYR A 1 345 ? 21.316  -33.160 18.804  1.00 24.89 ? 337  TYR A OH  1 
ATOM   2365  N  N   . VAL A 1 346 ? 15.779  -34.940 22.351  1.00 22.12 ? 338  VAL A N   1 
ATOM   2366  C  CA  . VAL A 1 346 ? 16.179  -34.245 23.571  1.00 21.97 ? 338  VAL A CA  1 
ATOM   2367  C  C   . VAL A 1 346 ? 16.359  -35.240 24.711  1.00 28.20 ? 338  VAL A C   1 
ATOM   2368  O  O   . VAL A 1 346 ? 17.313  -35.141 25.494  1.00 25.84 ? 338  VAL A O   1 
ATOM   2369  C  CB  . VAL A 1 346 ? 15.156  -33.147 23.924  1.00 20.24 ? 338  VAL A CB  1 
ATOM   2370  C  CG1 . VAL A 1 346 ? 15.429  -32.584 25.324  1.00 19.67 ? 338  VAL A CG1 1 
ATOM   2371  C  CG2 . VAL A 1 346 ? 15.192  -32.028 22.891  1.00 22.74 ? 338  VAL A CG2 1 
ATOM   2372  N  N   . GLN A 1 347 ? 15.458  -36.225 24.814  1.00 25.34 ? 339  GLN A N   1 
ATOM   2373  C  CA  . GLN A 1 347 ? 15.562  -37.218 25.881  1.00 30.73 ? 339  GLN A CA  1 
ATOM   2374  C  C   . GLN A 1 347 ? 16.865  -38.005 25.784  1.00 28.86 ? 339  GLN A C   1 
ATOM   2375  O  O   . GLN A 1 347 ? 17.533  -38.237 26.794  1.00 29.69 ? 339  GLN A O   1 
ATOM   2376  C  CB  . GLN A 1 347 ? 14.360  -38.161 25.845  1.00 30.93 ? 339  GLN A CB  1 
ATOM   2377  N  N   . THR A 1 348 ? 17.251  -38.411 24.577  1.00 32.31 ? 340  THR A N   1 
ATOM   2378  C  CA  . THR A 1 348 ? 18.521  -39.110 24.411  1.00 32.62 ? 340  THR A CA  1 
ATOM   2379  C  C   . THR A 1 348 ? 19.702  -38.215 24.777  1.00 32.91 ? 340  THR A C   1 
ATOM   2380  O  O   . THR A 1 348 ? 20.636  -38.651 25.462  1.00 31.01 ? 340  THR A O   1 
ATOM   2381  C  CB  . THR A 1 348 ? 18.644  -39.609 22.976  1.00 36.44 ? 340  THR A CB  1 
ATOM   2382  O  OG1 . THR A 1 348 ? 17.495  -40.401 22.660  1.00 38.37 ? 340  THR A OG1 1 
ATOM   2383  C  CG2 . THR A 1 348 ? 19.895  -40.450 22.809  1.00 40.95 ? 340  THR A CG2 1 
ATOM   2384  N  N   . ALA A 1 349 ? 19.676  -36.956 24.340  1.00 24.63 ? 341  ALA A N   1 
ATOM   2385  C  CA  . ALA A 1 349 ? 20.779  -36.050 24.637  1.00 24.01 ? 341  ALA A CA  1 
ATOM   2386  C  C   . ALA A 1 349 ? 20.889  -35.764 26.130  1.00 23.64 ? 341  ALA A C   1 
ATOM   2387  O  O   . ALA A 1 349 ? 22.001  -35.622 26.653  1.00 29.49 ? 341  ALA A O   1 
ATOM   2388  C  CB  . ALA A 1 349 ? 20.607  -34.749 23.860  1.00 23.98 ? 341  ALA A CB  1 
ATOM   2389  N  N   . LEU A 1 350 ? 19.758  -35.666 26.824  1.00 23.18 ? 342  LEU A N   1 
ATOM   2390  C  CA  . LEU A 1 350 ? 19.782  -35.426 28.263  1.00 22.90 ? 342  LEU A CA  1 
ATOM   2391  C  C   . LEU A 1 350 ? 20.489  -36.562 28.992  1.00 26.56 ? 342  LEU A C   1 
ATOM   2392  O  O   . LEU A 1 350 ? 21.326  -36.326 29.875  1.00 28.07 ? 342  LEU A O   1 
ATOM   2393  C  CB  . LEU A 1 350 ? 18.350  -35.252 28.777  1.00 32.48 ? 342  LEU A CB  1 
ATOM   2394  C  CG  . LEU A 1 350 ? 18.158  -34.754 30.211  1.00 32.42 ? 342  LEU A CG  1 
ATOM   2395  C  CD1 . LEU A 1 350 ? 18.759  -33.364 30.361  1.00 31.62 ? 342  LEU A CD1 1 
ATOM   2396  C  CD2 . LEU A 1 350 ? 16.686  -34.757 30.610  1.00 27.96 ? 342  LEU A CD2 1 
ATOM   2397  N  N   . LYS A 1 351 ? 20.170  -37.809 28.629  1.00 29.79 ? 343  LYS A N   1 
ATOM   2398  C  CA  . LYS A 1 351 ? 20.832  -38.956 29.246  1.00 31.98 ? 343  LYS A CA  1 
ATOM   2399  C  C   . LYS A 1 351 ? 22.341  -38.911 29.026  1.00 32.56 ? 343  LYS A C   1 
ATOM   2400  O  O   . LYS A 1 351 ? 23.112  -39.310 29.903  1.00 34.25 ? 343  LYS A O   1 
ATOM   2401  C  CB  . LYS A 1 351 ? 20.242  -40.259 28.702  1.00 34.03 ? 343  LYS A CB  1 
ATOM   2402  N  N   . GLU A 1 352 ? 22.786  -38.418 27.868  1.00 29.55 ? 344  GLU A N   1 
ATOM   2403  C  CA  . GLU A 1 352 ? 24.222  -38.311 27.622  1.00 31.78 ? 344  GLU A CA  1 
ATOM   2404  C  C   . GLU A 1 352 ? 24.843  -37.165 28.420  1.00 31.18 ? 344  GLU A C   1 
ATOM   2405  O  O   . GLU A 1 352 ? 25.977  -37.277 28.898  1.00 34.84 ? 344  GLU A O   1 
ATOM   2406  C  CB  . GLU A 1 352 ? 24.487  -38.138 26.124  1.00 30.65 ? 344  GLU A CB  1 
ATOM   2407  N  N   . VAL A 1 353 ? 24.122  -36.053 28.564  1.00 28.05 ? 345  VAL A N   1 
ATOM   2408  C  CA  . VAL A 1 353 ? 24.610  -34.946 29.382  1.00 28.13 ? 345  VAL A CA  1 
ATOM   2409  C  C   . VAL A 1 353 ? 24.802  -35.400 30.823  1.00 28.28 ? 345  VAL A C   1 
ATOM   2410  O  O   . VAL A 1 353 ? 25.771  -35.018 31.493  1.00 28.46 ? 345  VAL A O   1 
ATOM   2411  C  CB  . VAL A 1 353 ? 23.643  -33.752 29.284  1.00 27.48 ? 345  VAL A CB  1 
ATOM   2412  C  CG1 . VAL A 1 353 ? 23.952  -32.714 30.348  1.00 25.43 ? 345  VAL A CG1 1 
ATOM   2413  C  CG2 . VAL A 1 353 ? 23.702  -33.137 27.878  1.00 25.59 ? 345  VAL A CG2 1 
ATOM   2414  N  N   . CYS A 1 354 ? 23.890  -36.234 31.315  1.00 27.53 ? 346  CYS A N   1 
ATOM   2415  C  CA  A CYS A 1 354 ? 24.026  -36.732 32.677  0.56 32.36 ? 346  CYS A CA  1 
ATOM   2416  C  CA  B CYS A 1 354 ? 24.000  -36.757 32.674  0.44 32.36 ? 346  CYS A CA  1 
ATOM   2417  C  C   . CYS A 1 354 ? 25.215  -37.668 32.812  1.00 34.89 ? 346  CYS A C   1 
ATOM   2418  O  O   . CYS A 1 354 ? 25.907  -37.646 33.837  1.00 37.38 ? 346  CYS A O   1 
ATOM   2419  C  CB  A CYS A 1 354 ? 22.740  -37.418 33.104  0.56 33.34 ? 346  CYS A CB  1 
ATOM   2420  C  CB  B CYS A 1 354 ? 22.714  -37.506 33.039  0.44 33.27 ? 346  CYS A CB  1 
ATOM   2421  S  SG  A CYS A 1 354 ? 21.469  -36.210 33.337  0.56 31.01 ? 346  CYS A SG  1 
ATOM   2422  S  SG  B CYS A 1 354 ? 22.171  -37.364 34.768  0.44 34.78 ? 346  CYS A SG  1 
ATOM   2423  N  N   . ALA A 1 355 ? 25.483  -38.475 31.787  1.00 31.04 ? 347  ALA A N   1 
ATOM   2424  C  CA  . ALA A 1 355 ? 26.635  -39.366 31.825  1.00 34.50 ? 347  ALA A CA  1 
ATOM   2425  C  C   . ALA A 1 355 ? 27.944  -38.597 31.968  1.00 37.30 ? 347  ALA A C   1 
ATOM   2426  O  O   . ALA A 1 355 ? 28.935  -39.147 32.464  1.00 41.93 ? 347  ALA A O   1 
ATOM   2427  C  CB  . ALA A 1 355 ? 26.665  -40.233 30.567  1.00 30.90 ? 347  ALA A CB  1 
ATOM   2428  N  N   . LYS A 1 356 ? 27.973  -37.329 31.542  1.00 29.92 ? 348  LYS A N   1 
ATOM   2429  C  CA  . LYS A 1 356 ? 29.209  -36.558 31.624  1.00 32.66 ? 348  LYS A CA  1 
ATOM   2430  C  C   . LYS A 1 356 ? 29.376  -35.929 33.000  1.00 37.52 ? 348  LYS A C   1 
ATOM   2431  O  O   . LYS A 1 356 ? 30.493  -35.887 33.528  1.00 37.41 ? 348  LYS A O   1 
ATOM   2432  C  CB  . LYS A 1 356 ? 29.244  -35.484 30.536  1.00 34.45 ? 348  LYS A CB  1 
ATOM   2433  N  N   . ALA A 1 357 ? 28.280  -35.438 33.588  1.00 36.78 ? 349  ALA A N   1 
ATOM   2434  C  CA  . ALA A 1 357 ? 28.280  -34.878 34.941  1.00 35.11 ? 349  ALA A CA  1 
ATOM   2435  C  C   . ALA A 1 357 ? 29.369  -33.817 35.107  1.00 35.76 ? 349  ALA A C   1 
ATOM   2436  O  O   . ALA A 1 357 ? 30.196  -33.870 36.023  1.00 30.75 ? 349  ALA A O   1 
ATOM   2437  C  CB  . ALA A 1 357 ? 28.430  -35.985 35.987  1.00 34.02 ? 349  ALA A CB  1 
ATOM   2438  N  N   . GLU A 1 358 ? 29.366  -32.842 34.199  1.00 24.31 ? 350  GLU A N   1 
ATOM   2439  C  CA  . GLU A 1 358 ? 30.373  -31.787 34.205  1.00 30.90 ? 350  GLU A CA  1 
ATOM   2440  C  C   . GLU A 1 358 ? 29.998  -30.658 35.159  1.00 30.69 ? 350  GLU A C   1 
ATOM   2441  O  O   . GLU A 1 358 ? 28.847  -30.217 35.206  1.00 27.55 ? 350  GLU A O   1 
ATOM   2442  C  CB  . GLU A 1 358 ? 30.547  -31.206 32.804  1.00 36.66 ? 350  GLU A CB  1 
ATOM   2443  C  CG  . GLU A 1 358 ? 31.319  -32.063 31.830  1.00 38.25 ? 350  GLU A CG  1 
ATOM   2444  C  CD  . GLU A 1 358 ? 31.566  -31.321 30.531  1.00 41.88 ? 350  GLU A CD  1 
ATOM   2445  O  OE1 . GLU A 1 358 ? 30.688  -31.361 29.647  1.00 40.78 ? 350  GLU A OE1 1 
ATOM   2446  O  OE2 . GLU A 1 358 ? 32.623  -30.666 30.413  1.00 44.23 ? 350  GLU A OE2 1 
ATOM   2447  N  N   . THR A 1 359 ? 30.983  -30.175 35.910  1.00 28.20 ? 351  THR A N   1 
ATOM   2448  C  CA  . THR A 1 359 ? 30.833  -28.945 36.683  1.00 31.39 ? 351  THR A CA  1 
ATOM   2449  C  C   . THR A 1 359 ? 31.461  -27.830 35.854  1.00 32.83 ? 351  THR A C   1 
ATOM   2450  O  O   . THR A 1 359 ? 32.688  -27.696 35.790  1.00 34.05 ? 351  THR A O   1 
ATOM   2451  C  CB  . THR A 1 359 ? 31.468  -29.064 38.067  1.00 30.71 ? 351  THR A CB  1 
ATOM   2452  O  OG1 . THR A 1 359 ? 30.672  -29.933 38.880  1.00 35.64 ? 351  THR A OG1 1 
ATOM   2453  C  CG2 . THR A 1 359 ? 31.552  -27.707 38.747  1.00 29.94 ? 351  THR A CG2 1 
ATOM   2454  N  N   . VAL A 1 360 ? 30.602  -27.063 35.184  1.00 29.76 ? 352  VAL A N   1 
ATOM   2455  C  CA  . VAL A 1 360 ? 30.986  -25.921 34.369  1.00 27.62 ? 352  VAL A CA  1 
ATOM   2456  C  C   . VAL A 1 360 ? 30.041  -24.774 34.701  1.00 26.40 ? 352  VAL A C   1 
ATOM   2457  O  O   . VAL A 1 360 ? 28.997  -24.966 35.325  1.00 27.44 ? 352  VAL A O   1 
ATOM   2458  C  CB  . VAL A 1 360 ? 30.928  -26.233 32.859  1.00 27.69 ? 352  VAL A CB  1 
ATOM   2459  C  CG1 . VAL A 1 360 ? 31.987  -27.253 32.476  1.00 23.24 ? 352  VAL A CG1 1 
ATOM   2460  C  CG2 . VAL A 1 360 ? 29.541  -26.725 32.480  1.00 22.22 ? 352  VAL A CG2 1 
ATOM   2461  N  N   . ALA A 1 361 ? 30.416  -23.570 34.271  1.00 23.48 ? 353  ALA A N   1 
ATOM   2462  C  CA  . ALA A 1 361 ? 29.480  -22.451 34.314  1.00 21.86 ? 353  ALA A CA  1 
ATOM   2463  C  C   . ALA A 1 361 ? 28.304  -22.728 33.392  1.00 25.13 ? 353  ALA A C   1 
ATOM   2464  O  O   . ALA A 1 361 ? 28.456  -23.358 32.343  1.00 21.39 ? 353  ALA A O   1 
ATOM   2465  C  CB  . ALA A 1 361 ? 30.154  -21.151 33.886  1.00 24.82 ? 353  ALA A CB  1 
ATOM   2466  N  N   . THR A 1 362 ? 27.115  -22.241 33.773  1.00 17.98 ? 354  THR A N   1 
ATOM   2467  C  CA  . THR A 1 362 ? 26.000  -22.564 32.895  1.00 22.88 ? 354  THR A CA  1 
ATOM   2468  C  C   . THR A 1 362 ? 26.024  -21.771 31.598  1.00 24.98 ? 354  THR A C   1 
ATOM   2469  O  O   . THR A 1 362 ? 25.304  -22.151 30.668  1.00 24.23 ? 354  THR A O   1 
ATOM   2470  C  CB  . THR A 1 362 ? 24.641  -22.399 33.593  1.00 17.75 ? 354  THR A CB  1 
ATOM   2471  O  OG1 . THR A 1 362 ? 24.541  -21.109 34.204  1.00 20.61 ? 354  THR A OG1 1 
ATOM   2472  C  CG2 . THR A 1 362 ? 24.455  -23.497 34.637  1.00 15.00 ? 354  THR A CG2 1 
ATOM   2473  N  N   . ARG A 1 363 ? 26.847  -20.713 31.484  1.00 21.75 ? 355  ARG A N   1 
ATOM   2474  C  CA  . ARG A 1 363 ? 27.045  -20.135 30.154  1.00 20.97 ? 355  ARG A CA  1 
ATOM   2475  C  C   . ARG A 1 363 ? 27.748  -21.124 29.240  1.00 18.54 ? 355  ARG A C   1 
ATOM   2476  O  O   . ARG A 1 363 ? 27.478  -21.156 28.036  1.00 25.32 ? 355  ARG A O   1 
ATOM   2477  C  CB  . ARG A 1 363 ? 27.823  -18.815 30.225  1.00 21.88 ? 355  ARG A CB  1 
ATOM   2478  C  CG  . ARG A 1 363 ? 29.234  -18.917 30.803  1.00 25.78 ? 355  ARG A CG  1 
ATOM   2479  C  CD  . ARG A 1 363 ? 30.056  -17.639 30.555  1.00 25.23 ? 355  ARG A CD  1 
ATOM   2480  N  NE  . ARG A 1 363 ? 31.394  -17.742 31.145  1.00 28.57 ? 355  ARG A NE  1 
ATOM   2481  C  CZ  . ARG A 1 363 ? 32.416  -16.937 30.857  1.00 36.05 ? 355  ARG A CZ  1 
ATOM   2482  N  NH1 . ARG A 1 363 ? 32.269  -15.959 29.972  1.00 27.49 ? 355  ARG A NH1 1 
ATOM   2483  N  NH2 . ARG A 1 363 ? 33.594  -17.111 31.455  1.00 35.40 ? 355  ARG A NH2 1 
ATOM   2484  N  N   . LYS A 1 364 ? 28.632  -21.960 29.795  1.00 22.15 ? 356  LYS A N   1 
ATOM   2485  C  CA  . LYS A 1 364 ? 29.222  -23.033 29.000  1.00 24.16 ? 356  LYS A CA  1 
ATOM   2486  C  C   . LYS A 1 364 ? 28.216  -24.158 28.774  1.00 27.11 ? 356  LYS A C   1 
ATOM   2487  O  O   . LYS A 1 364 ? 28.161  -24.740 27.684  1.00 21.04 ? 356  LYS A O   1 
ATOM   2488  C  CB  . LYS A 1 364 ? 30.490  -23.555 29.682  1.00 28.76 ? 356  LYS A CB  1 
ATOM   2489  C  CG  . LYS A 1 364 ? 31.190  -24.685 28.924  1.00 36.17 ? 356  LYS A CG  1 
ATOM   2490  C  CD  . LYS A 1 364 ? 31.535  -24.274 27.496  1.00 40.14 ? 356  LYS A CD  1 
ATOM   2491  C  CE  . LYS A 1 364 ? 32.119  -25.448 26.706  1.00 41.28 ? 356  LYS A CE  1 
ATOM   2492  N  NZ  . LYS A 1 364 ? 32.268  -25.133 25.255  1.00 38.09 ? 356  LYS A NZ  1 
ATOM   2493  N  N   . ALA A 1 365 ? 27.403  -24.472 29.793  1.00 30.79 ? 357  ALA A N   1 
ATOM   2494  C  CA  . ALA A 1 365 ? 26.302  -25.416 29.604  1.00 23.56 ? 357  ALA A CA  1 
ATOM   2495  C  C   . ALA A 1 365 ? 25.343  -24.931 28.523  1.00 23.43 ? 357  ALA A C   1 
ATOM   2496  O  O   . ALA A 1 365 ? 24.792  -25.738 27.765  1.00 22.60 ? 357  ALA A O   1 
ATOM   2497  C  CB  . ALA A 1 365 ? 25.555  -25.626 30.920  1.00 27.98 ? 357  ALA A CB  1 
ATOM   2498  N  N   . SER A 1 366 ? 25.129  -23.615 28.445  1.00 23.17 ? 358  SER A N   1 
ATOM   2499  C  CA  . SER A 1 366 ? 24.308  -23.043 27.377  1.00 25.32 ? 358  SER A CA  1 
ATOM   2500  C  C   . SER A 1 366 ? 24.922  -23.319 26.007  1.00 26.28 ? 358  SER A C   1 
ATOM   2501  O  O   . SER A 1 366 ? 24.244  -23.818 25.101  1.00 22.53 ? 358  SER A O   1 
ATOM   2502  C  CB  . SER A 1 366 ? 24.127  -21.535 27.600  1.00 18.66 ? 358  SER A CB  1 
ATOM   2503  O  OG  . SER A 1 366 ? 23.355  -20.945 26.555  1.00 18.57 ? 358  SER A OG  1 
ATOM   2504  N  N   . GLN A 1 367 ? 26.216  -23.017 25.846  1.00 22.60 ? 359  GLN A N   1 
ATOM   2505  C  CA  . GLN A 1 367 ? 26.880  -23.259 24.572  1.00 23.16 ? 359  GLN A CA  1 
ATOM   2506  C  C   . GLN A 1 367 ? 26.842  -24.740 24.204  1.00 26.72 ? 359  GLN A C   1 
ATOM   2507  O  O   . GLN A 1 367 ? 26.689  -25.094 23.027  1.00 19.95 ? 359  GLN A O   1 
ATOM   2508  C  CB  . GLN A 1 367 ? 28.325  -22.762 24.631  1.00 24.42 ? 359  GLN A CB  1 
ATOM   2509  C  CG  . GLN A 1 367 ? 29.060  -22.841 23.304  1.00 21.30 ? 359  GLN A CG  1 
ATOM   2510  C  CD  . GLN A 1 367 ? 30.459  -22.255 23.398  1.00 32.86 ? 359  GLN A CD  1 
ATOM   2511  O  OE1 . GLN A 1 367 ? 31.133  -22.408 24.416  1.00 32.56 ? 359  GLN A OE1 1 
ATOM   2512  N  NE2 . GLN A 1 367 ? 30.889  -21.557 22.346  1.00 30.99 ? 359  GLN A NE2 1 
ATOM   2513  N  N   . ASN A 1 368 ? 26.983  -25.620 25.200  1.00 24.08 ? 360  ASN A N   1 
ATOM   2514  C  CA  . ASN A 1 368 ? 26.838  -27.053 24.947  1.00 22.59 ? 360  ASN A CA  1 
ATOM   2515  C  C   . ASN A 1 368 ? 25.419  -27.408 24.508  1.00 23.13 ? 360  ASN A C   1 
ATOM   2516  O  O   . ASN A 1 368 ? 25.227  -28.245 23.615  1.00 20.50 ? 360  ASN A O   1 
ATOM   2517  C  CB  . ASN A 1 368 ? 27.209  -27.846 26.203  1.00 27.97 ? 360  ASN A CB  1 
ATOM   2518  C  CG  . ASN A 1 368 ? 28.694  -27.765 26.544  1.00 33.13 ? 360  ASN A CG  1 
ATOM   2519  O  OD1 . ASN A 1 368 ? 29.515  -27.353 25.724  1.00 31.65 ? 360  ASN A OD1 1 
ATOM   2520  N  ND2 . ASN A 1 368 ? 29.044  -28.185 27.760  1.00 32.04 ? 360  ASN A ND2 1 
ATOM   2521  N  N   . SER A 1 369 ? 24.408  -26.814 25.157  1.00 20.52 ? 361  SER A N   1 
ATOM   2522  C  CA  . SER A 1 369 ? 23.018  -27.062 24.770  1.00 21.31 ? 361  SER A CA  1 
ATOM   2523  C  C   . SER A 1 369 ? 22.735  -26.547 23.367  1.00 19.56 ? 361  SER A C   1 
ATOM   2524  O  O   . SER A 1 369 ? 21.993  -27.179 22.604  1.00 21.30 ? 361  SER A O   1 
ATOM   2525  C  CB  . SER A 1 369 ? 22.061  -26.393 25.765  1.00 16.24 ? 361  SER A CB  1 
ATOM   2526  O  OG  . SER A 1 369 ? 22.258  -26.883 27.080  1.00 18.64 ? 361  SER A OG  1 
ATOM   2527  N  N   . ILE A 1 370 ? 23.284  -25.380 23.027  1.00 16.31 ? 362  ILE A N   1 
ATOM   2528  C  CA  . ILE A 1 370 ? 23.120  -24.845 21.679  1.00 20.29 ? 362  ILE A CA  1 
ATOM   2529  C  C   . ILE A 1 370 ? 23.674  -25.824 20.660  1.00 17.17 ? 362  ILE A C   1 
ATOM   2530  O  O   . ILE A 1 370 ? 23.040  -26.112 19.638  1.00 20.16 ? 362  ILE A O   1 
ATOM   2531  C  CB  . ILE A 1 370 ? 23.792  -23.463 21.565  1.00 19.16 ? 362  ILE A CB  1 
ATOM   2532  C  CG1 . ILE A 1 370 ? 23.082  -22.452 22.465  1.00 19.93 ? 362  ILE A CG1 1 
ATOM   2533  C  CG2 . ILE A 1 370 ? 23.761  -22.971 20.134  1.00 21.25 ? 362  ILE A CG2 1 
ATOM   2534  C  CD1 . ILE A 1 370 ? 23.883  -21.176 22.696  1.00 16.28 ? 362  ILE A CD1 1 
ATOM   2535  N  N   . GLU A 1 371 ? 24.863  -26.368 20.931  1.00 18.96 ? 363  GLU A N   1 
ATOM   2536  C  CA  . GLU A 1 371 ? 25.452  -27.351 20.028  1.00 19.10 ? 363  GLU A CA  1 
ATOM   2537  C  C   . GLU A 1 371 ? 24.503  -28.525 19.820  1.00 23.78 ? 363  GLU A C   1 
ATOM   2538  O  O   . GLU A 1 371 ? 24.230  -28.929 18.682  1.00 23.83 ? 363  GLU A O   1 
ATOM   2539  C  CB  . GLU A 1 371 ? 26.794  -27.825 20.589  1.00 22.37 ? 363  GLU A CB  1 
ATOM   2540  C  CG  . GLU A 1 371 ? 27.586  -28.726 19.649  1.00 26.83 ? 363  GLU A CG  1 
ATOM   2541  C  CD  . GLU A 1 371 ? 28.323  -27.931 18.600  1.00 30.34 ? 363  GLU A CD  1 
ATOM   2542  O  OE1 . GLU A 1 371 ? 28.962  -26.916 18.962  1.00 34.18 ? 363  GLU A OE1 1 
ATOM   2543  O  OE2 . GLU A 1 371 ? 28.254  -28.308 17.416  1.00 37.27 ? 363  GLU A OE2 1 
ATOM   2544  N  N   . ILE A 1 372 ? 23.959  -29.056 20.919  1.00 19.55 ? 364  ILE A N   1 
ATOM   2545  C  CA  . ILE A 1 372 ? 23.042  -30.190 20.846  1.00 20.10 ? 364  ILE A CA  1 
ATOM   2546  C  C   . ILE A 1 372 ? 21.806  -29.828 20.036  1.00 26.35 ? 364  ILE A C   1 
ATOM   2547  O  O   . ILE A 1 372 ? 21.376  -30.586 19.161  1.00 27.20 ? 364  ILE A O   1 
ATOM   2548  C  CB  . ILE A 1 372 ? 22.657  -30.651 22.262  1.00 20.09 ? 364  ILE A CB  1 
ATOM   2549  C  CG1 . ILE A 1 372 ? 23.877  -31.201 23.004  1.00 27.60 ? 364  ILE A CG1 1 
ATOM   2550  C  CG2 . ILE A 1 372 ? 21.548  -31.685 22.192  1.00 29.36 ? 364  ILE A CG2 1 
ATOM   2551  C  CD1 . ILE A 1 372 ? 23.625  -31.424 24.488  1.00 24.51 ? 364  ILE A CD1 1 
ATOM   2552  N  N   . LEU A 1 373 ? 21.202  -28.674 20.335  1.00 22.81 ? 365  LEU A N   1 
ATOM   2553  C  CA  . LEU A 1 373 ? 19.967  -28.289 19.654  1.00 26.00 ? 365  LEU A CA  1 
ATOM   2554  C  C   . LEU A 1 373 ? 20.205  -27.982 18.182  1.00 25.97 ? 365  LEU A C   1 
ATOM   2555  O  O   . LEU A 1 373 ? 19.355  -28.288 17.336  1.00 21.17 ? 365  LEU A O   1 
ATOM   2556  C  CB  . LEU A 1 373 ? 19.339  -27.082 20.335  1.00 26.69 ? 365  LEU A CB  1 
ATOM   2557  C  CG  . LEU A 1 373 ? 18.076  -27.370 21.140  1.00 36.39 ? 365  LEU A CG  1 
ATOM   2558  C  CD1 . LEU A 1 373 ? 18.350  -28.452 22.157  1.00 36.91 ? 365  LEU A CD1 1 
ATOM   2559  C  CD2 . LEU A 1 373 ? 17.575  -26.091 21.813  1.00 34.87 ? 365  LEU A CD2 1 
ATOM   2560  N  N   . ALA A 1 374 ? 21.350  -27.368 17.863  1.00 24.03 ? 366  ALA A N   1 
ATOM   2561  C  CA  . ALA A 1 374 ? 21.634  -26.978 16.486  1.00 22.93 ? 366  ALA A CA  1 
ATOM   2562  C  C   . ALA A 1 374 ? 21.693  -28.181 15.563  1.00 27.01 ? 366  ALA A C   1 
ATOM   2563  O  O   . ALA A 1 374 ? 21.313  -28.076 14.387  1.00 21.46 ? 366  ALA A O   1 
ATOM   2564  C  CB  . ALA A 1 374 ? 22.945  -26.199 16.417  1.00 19.51 ? 366  ALA A CB  1 
ATOM   2565  N  N   . LYS A 1 375 ? 22.167  -29.329 16.066  1.00 24.99 ? 367  LYS A N   1 
ATOM   2566  C  CA  . LYS A 1 375 ? 22.185  -30.530 15.236  1.00 25.14 ? 367  LYS A CA  1 
ATOM   2567  C  C   . LYS A 1 375 ? 20.781  -30.908 14.803  1.00 27.61 ? 367  LYS A C   1 
ATOM   2568  O  O   . LYS A 1 375 ? 20.586  -31.419 13.699  1.00 28.68 ? 367  LYS A O   1 
ATOM   2569  C  CB  . LYS A 1 375 ? 22.820  -31.702 15.983  1.00 24.12 ? 367  LYS A CB  1 
ATOM   2570  C  CG  . LYS A 1 375 ? 24.323  -31.636 16.123  1.00 35.58 ? 367  LYS A CG  1 
ATOM   2571  C  CD  . LYS A 1 375 ? 24.922  -33.036 16.116  1.00 42.36 ? 367  LYS A CD  1 
ATOM   2572  C  CE  . LYS A 1 375 ? 24.173  -33.972 17.053  1.00 46.88 ? 367  LYS A CE  1 
ATOM   2573  N  NZ  . LYS A 1 375 ? 24.657  -35.381 16.937  1.00 53.06 ? 367  LYS A NZ  1 
ATOM   2574  N  N   . GLU A 1 376 ? 19.797  -30.643 15.655  1.00 26.14 ? 368  GLU A N   1 
ATOM   2575  C  CA  . GLU A 1 376 ? 18.423  -31.060 15.439  1.00 29.78 ? 368  GLU A CA  1 
ATOM   2576  C  C   . GLU A 1 376 ? 17.573  -29.979 14.781  1.00 24.34 ? 368  GLU A C   1 
ATOM   2577  O  O   . GLU A 1 376 ? 16.604  -30.300 14.079  1.00 24.26 ? 368  GLU A O   1 
ATOM   2578  C  CB  . GLU A 1 376 ? 17.814  -31.458 16.786  1.00 34.68 ? 368  GLU A CB  1 
ATOM   2579  C  CG  . GLU A 1 376 ? 16.320  -31.675 16.790  1.00 37.59 ? 368  GLU A CG  1 
ATOM   2580  C  CD  . GLU A 1 376 ? 15.923  -33.007 16.201  1.00 38.57 ? 368  GLU A CD  1 
ATOM   2581  O  OE1 . GLU A 1 376 ? 16.787  -33.684 15.603  1.00 37.87 ? 368  GLU A OE1 1 
ATOM   2582  O  OE2 . GLU A 1 376 ? 14.741  -33.375 16.350  1.00 38.94 ? 368  GLU A OE2 1 
ATOM   2583  N  N   . LEU A 1 377 ? 17.923  -28.707 14.979  1.00 23.48 ? 369  LEU A N   1 
ATOM   2584  C  CA  . LEU A 1 377 ? 17.127  -27.575 14.507  1.00 21.88 ? 369  LEU A CA  1 
ATOM   2585  C  C   . LEU A 1 377 ? 17.914  -26.781 13.472  1.00 19.76 ? 369  LEU A C   1 
ATOM   2586  O  O   . LEU A 1 377 ? 18.555  -25.772 13.808  1.00 17.24 ? 369  LEU A O   1 
ATOM   2587  C  CB  . LEU A 1 377 ? 16.722  -26.675 15.673  1.00 19.55 ? 369  LEU A CB  1 
ATOM   2588  C  CG  . LEU A 1 377 ? 15.979  -27.354 16.821  1.00 21.58 ? 369  LEU A CG  1 
ATOM   2589  C  CD1 . LEU A 1 377 ? 15.633  -26.341 17.927  1.00 20.01 ? 369  LEU A CD1 1 
ATOM   2590  C  CD2 . LEU A 1 377 ? 14.722  -28.046 16.301  1.00 20.61 ? 369  LEU A CD2 1 
ATOM   2591  N  N   . PRO A 1 378 ? 17.863  -27.168 12.196  1.00 22.34 ? 370  PRO A N   1 
ATOM   2592  C  CA  . PRO A 1 378 ? 18.520  -26.350 11.165  1.00 20.69 ? 370  PRO A CA  1 
ATOM   2593  C  C   . PRO A 1 378 ? 17.958  -24.942 11.076  1.00 20.33 ? 370  PRO A C   1 
ATOM   2594  O  O   . PRO A 1 378 ? 18.621  -24.055 10.525  1.00 22.30 ? 370  PRO A O   1 
ATOM   2595  C  CB  . PRO A 1 378 ? 18.273  -27.147 9.874   1.00 25.27 ? 370  PRO A CB  1 
ATOM   2596  C  CG  . PRO A 1 378 ? 17.003  -27.917 10.152  1.00 20.53 ? 370  PRO A CG  1 
ATOM   2597  C  CD  . PRO A 1 378 ? 17.070  -28.269 11.620  1.00 19.33 ? 370  PRO A CD  1 
ATOM   2598  N  N   . GLU A 1 379 ? 16.757  -24.703 11.606  1.00 19.11 ? 371  GLU A N   1 
ATOM   2599  C  CA  . GLU A 1 379 ? 16.195  -23.360 11.609  1.00 19.56 ? 371  GLU A CA  1 
ATOM   2600  C  C   . GLU A 1 379 ? 16.851  -22.446 12.635  1.00 20.18 ? 371  GLU A C   1 
ATOM   2601  O  O   . GLU A 1 379 ? 16.573  -21.241 12.626  1.00 18.76 ? 371  GLU A O   1 
ATOM   2602  C  CB  . GLU A 1 379 ? 14.685  -23.410 11.875  1.00 18.59 ? 371  GLU A CB  1 
ATOM   2603  C  CG  . GLU A 1 379 ? 14.295  -24.057 13.202  1.00 21.79 ? 371  GLU A CG  1 
ATOM   2604  C  CD  . GLU A 1 379 ? 13.960  -25.532 13.069  1.00 23.47 ? 371  GLU A CD  1 
ATOM   2605  O  OE1 . GLU A 1 379 ? 14.742  -26.273 12.439  1.00 22.61 ? 371  GLU A OE1 1 
ATOM   2606  O  OE2 . GLU A 1 379 ? 12.905  -25.950 13.593  1.00 26.14 ? 371  GLU A OE2 1 
ATOM   2607  N  N   . LEU A 1 380 ? 17.720  -22.974 13.499  1.00 18.13 ? 372  LEU A N   1 
ATOM   2608  C  CA  . LEU A 1 380 ? 18.260  -22.177 14.595  1.00 14.80 ? 372  LEU A CA  1 
ATOM   2609  C  C   . LEU A 1 380 ? 19.148  -21.065 14.051  1.00 16.98 ? 372  LEU A C   1 
ATOM   2610  O  O   . LEU A 1 380 ? 19.981  -21.293 13.172  1.00 21.29 ? 372  LEU A O   1 
ATOM   2611  C  CB  . LEU A 1 380 ? 19.041  -23.071 15.553  1.00 15.90 ? 372  LEU A CB  1 
ATOM   2612  C  CG  . LEU A 1 380 ? 19.300  -22.576 16.967  1.00 17.57 ? 372  LEU A CG  1 
ATOM   2613  C  CD1 . LEU A 1 380 ? 17.997  -22.470 17.751  1.00 15.37 ? 372  LEU A CD1 1 
ATOM   2614  C  CD2 . LEU A 1 380 ? 20.266  -23.555 17.631  1.00 25.94 ? 372  LEU A CD2 1 
ATOM   2615  N  N   . VAL A 1 381 ? 18.949  -19.854 14.558  1.00 17.49 ? 373  VAL A N   1 
ATOM   2616  C  CA  . VAL A 1 381 ? 19.750  -18.693 14.198  1.00 16.08 ? 373  VAL A CA  1 
ATOM   2617  C  C   . VAL A 1 381 ? 20.167  -18.013 15.494  1.00 20.42 ? 373  VAL A C   1 
ATOM   2618  O  O   . VAL A 1 381 ? 19.317  -17.513 16.236  1.00 20.86 ? 373  VAL A O   1 
ATOM   2619  C  CB  . VAL A 1 381 ? 18.986  -17.713 13.298  1.00 15.11 ? 373  VAL A CB  1 
ATOM   2620  C  CG1 . VAL A 1 381 ? 19.808  -16.443 13.090  1.00 15.08 ? 373  VAL A CG1 1 
ATOM   2621  C  CG2 . VAL A 1 381 ? 18.639  -18.369 11.948  1.00 16.12 ? 373  VAL A CG2 1 
ATOM   2622  N  N   . GLY A 1 382 ? 21.464  -18.008 15.777  1.00 17.30 ? 374  GLY A N   1 
ATOM   2623  C  CA  . GLY A 1 382 ? 21.973  -17.425 16.997  1.00 16.47 ? 374  GLY A CA  1 
ATOM   2624  C  C   . GLY A 1 382 ? 22.464  -16.005 16.793  1.00 13.25 ? 374  GLY A C   1 
ATOM   2625  O  O   . GLY A 1 382 ? 22.427  -15.449 15.700  1.00 14.39 ? 374  GLY A O   1 
ATOM   2626  N  N   . GLY A 1 383 ? 22.917  -15.418 17.891  1.00 12.22 ? 375  GLY A N   1 
ATOM   2627  C  CA  . GLY A 1 383 ? 23.602  -14.149 17.816  1.00 15.94 ? 375  GLY A CA  1 
ATOM   2628  C  C   . GLY A 1 383 ? 23.845  -13.607 19.202  1.00 21.52 ? 375  GLY A C   1 
ATOM   2629  O  O   . GLY A 1 383 ? 23.420  -14.187 20.207  1.00 11.44 ? 375  GLY A O   1 
ATOM   2630  N  N   . SER A 1 384 ? 24.541  -12.473 19.233  1.00 13.41 ? 376  SER A N   1 
ATOM   2631  C  CA  A SER A 1 384 ? 24.888  -11.807 20.483  0.61 14.01 ? 376  SER A CA  1 
ATOM   2632  C  CA  B SER A 1 384 ? 24.801  -11.791 20.488  0.39 13.85 ? 376  SER A CA  1 
ATOM   2633  C  C   . SER A 1 384 ? 25.100  -10.330 20.200  1.00 14.02 ? 376  SER A C   1 
ATOM   2634  O  O   . SER A 1 384 ? 25.463  -9.954  19.082  1.00 14.05 ? 376  SER A O   1 
ATOM   2635  C  CB  A SER A 1 384 ? 26.153  -12.405 21.116  0.61 14.10 ? 376  SER A CB  1 
ATOM   2636  C  CB  B SER A 1 384 ? 25.959  -12.440 21.246  0.39 14.25 ? 376  SER A CB  1 
ATOM   2637  O  OG  A SER A 1 384 ? 26.633  -11.596 22.191  0.61 14.99 ? 376  SER A OG  1 
ATOM   2638  O  OG  B SER A 1 384 ? 27.165  -12.242 20.544  0.39 12.35 ? 376  SER A OG  1 
ATOM   2639  N  N   . ALA A 1 385 ? 24.912  -9.508  21.229  1.00 12.10 ? 377  ALA A N   1 
ATOM   2640  C  CA  . ALA A 1 385 ? 25.153  -8.071  21.128  1.00 11.17 ? 377  ALA A CA  1 
ATOM   2641  C  C   . ALA A 1 385 ? 26.604  -7.758  21.524  1.00 13.81 ? 377  ALA A C   1 
ATOM   2642  O  O   . ALA A 1 385 ? 26.897  -7.196  22.586  1.00 15.59 ? 377  ALA A O   1 
ATOM   2643  C  CB  . ALA A 1 385 ? 24.149  -7.311  21.989  1.00 9.87  ? 377  ALA A CB  1 
ATOM   2644  N  N   . ASP A 1 386 ? 27.523  -8.151  20.631  1.00 13.88 ? 378  ASP A N   1 
ATOM   2645  C  CA  . ASP A 1 386 ? 28.973  -7.916  20.777  1.00 14.10 ? 378  ASP A CA  1 
ATOM   2646  C  C   . ASP A 1 386 ? 29.534  -8.604  22.019  1.00 17.32 ? 378  ASP A C   1 
ATOM   2647  O  O   . ASP A 1 386 ? 30.459  -8.107  22.658  1.00 17.55 ? 378  ASP A O   1 
ATOM   2648  C  CB  . ASP A 1 386 ? 29.297  -6.415  20.797  1.00 12.32 ? 378  ASP A CB  1 
ATOM   2649  C  CG  . ASP A 1 386 ? 30.771  -6.110  20.538  1.00 17.75 ? 378  ASP A CG  1 
ATOM   2650  O  OD1 . ASP A 1 386 ? 31.321  -6.555  19.515  1.00 20.23 ? 378  ASP A OD1 1 
ATOM   2651  O  OD2 . ASP A 1 386 ? 31.388  -5.398  21.356  1.00 21.49 ? 378  ASP A OD2 1 
ATOM   2652  N  N   . LEU A 1 387 ? 28.974  -9.745  22.395  1.00 15.28 ? 379  LEU A N   1 
ATOM   2653  C  CA  . LEU A 1 387 ? 29.479  -10.463 23.560  1.00 18.00 ? 379  LEU A CA  1 
ATOM   2654  C  C   . LEU A 1 387 ? 29.652  -11.940 23.251  1.00 25.54 ? 379  LEU A C   1 
ATOM   2655  O  O   . LEU A 1 387 ? 29.438  -12.789 24.119  1.00 27.48 ? 379  LEU A O   1 
ATOM   2656  C  CB  . LEU A 1 387 ? 28.570  -10.271 24.774  1.00 21.23 ? 379  LEU A CB  1 
ATOM   2657  C  CG  . LEU A 1 387 ? 28.554  -8.878  25.402  1.00 26.78 ? 379  LEU A CG  1 
ATOM   2658  C  CD1 . LEU A 1 387 ? 27.452  -8.769  26.458  1.00 25.34 ? 379  LEU A CD1 1 
ATOM   2659  C  CD2 . LEU A 1 387 ? 29.936  -8.527  25.983  1.00 22.30 ? 379  LEU A CD2 1 
ATOM   2660  N  N   . THR A 1 388 ? 30.032  -12.260 22.012  1.00 18.31 ? 380  THR A N   1 
ATOM   2661  C  CA  . THR A 1 388 ? 30.149  -13.663 21.620  1.00 24.79 ? 380  THR A CA  1 
ATOM   2662  C  C   . THR A 1 388 ? 31.163  -14.422 22.473  1.00 27.76 ? 380  THR A C   1 
ATOM   2663  O  O   . THR A 1 388 ? 30.835  -15.526 22.941  1.00 26.40 ? 380  THR A O   1 
ATOM   2664  C  CB  . THR A 1 388 ? 30.478  -13.751 20.122  1.00 27.30 ? 380  THR A CB  1 
ATOM   2665  O  OG1 . THR A 1 388 ? 29.503  -13.013 19.372  1.00 23.94 ? 380  THR A OG1 1 
ATOM   2666  C  CG2 . THR A 1 388 ? 30.475  -15.198 19.653  1.00 25.23 ? 380  THR A CG2 1 
ATOM   2667  N  N   . PRO A 1 389 ? 32.373  -13.912 22.732  1.00 26.48 ? 381  PRO A N   1 
ATOM   2668  C  CA  . PRO A 1 389 ? 33.301  -14.659 23.595  1.00 33.60 ? 381  PRO A CA  1 
ATOM   2669  C  C   . PRO A 1 389 ? 32.878  -14.691 25.055  1.00 33.25 ? 381  PRO A C   1 
ATOM   2670  O  O   . PRO A 1 389 ? 33.434  -15.491 25.821  1.00 24.90 ? 381  PRO A O   1 
ATOM   2671  C  CB  . PRO A 1 389 ? 34.623  -13.904 23.418  1.00 35.65 ? 381  PRO A CB  1 
ATOM   2672  C  CG  . PRO A 1 389 ? 34.174  -12.494 23.167  1.00 32.14 ? 381  PRO A CG  1 
ATOM   2673  C  CD  . PRO A 1 389 ? 32.976  -12.645 22.272  1.00 26.75 ? 381  PRO A CD  1 
ATOM   2674  N  N   . SER A 1 390 ? 31.916  -13.857 25.457  1.00 30.65 ? 382  SER A N   1 
ATOM   2675  C  CA  . SER A 1 390 ? 31.424  -13.797 26.829  1.00 25.46 ? 382  SER A CA  1 
ATOM   2676  C  C   . SER A 1 390 ? 30.121  -14.561 27.026  1.00 32.12 ? 382  SER A C   1 
ATOM   2677  O  O   . SER A 1 390 ? 29.972  -15.277 28.024  1.00 29.78 ? 382  SER A O   1 
ATOM   2678  C  CB  . SER A 1 390 ? 31.214  -12.338 27.259  1.00 23.73 ? 382  SER A CB  1 
ATOM   2679  O  OG  . SER A 1 390 ? 32.450  -11.654 27.405  1.00 34.78 ? 382  SER A OG  1 
ATOM   2680  N  N   . ASN A 1 391 ? 29.163  -14.407 26.106  1.00 27.76 ? 383  ASN A N   1 
ATOM   2681  C  CA  . ASN A 1 391 ? 27.909  -15.137 26.216  1.00 28.43 ? 383  ASN A CA  1 
ATOM   2682  C  C   . ASN A 1 391 ? 28.042  -16.585 25.770  1.00 31.39 ? 383  ASN A C   1 
ATOM   2683  O  O   . ASN A 1 391 ? 27.179  -17.402 26.113  1.00 24.88 ? 383  ASN A O   1 
ATOM   2684  C  CB  . ASN A 1 391 ? 26.810  -14.477 25.384  1.00 21.16 ? 383  ASN A CB  1 
ATOM   2685  C  CG  . ASN A 1 391 ? 26.564  -13.030 25.759  1.00 21.63 ? 383  ASN A CG  1 
ATOM   2686  O  OD1 . ASN A 1 391 ? 26.260  -12.219 24.897  1.00 19.80 ? 383  ASN A OD1 1 
ATOM   2687  N  ND2 . ASN A 1 391 ? 26.689  -12.700 27.047  1.00 22.62 ? 383  ASN A ND2 1 
ATOM   2688  N  N   . LEU A 1 392 ? 29.088  -16.913 25.005  1.00 23.43 ? 384  LEU A N   1 
ATOM   2689  C  CA  . LEU A 1 392 ? 29.305  -18.272 24.511  1.00 23.08 ? 384  LEU A CA  1 
ATOM   2690  C  C   . LEU A 1 392 ? 28.109  -18.747 23.673  1.00 28.91 ? 384  LEU A C   1 
ATOM   2691  O  O   . LEU A 1 392 ? 27.460  -19.755 23.963  1.00 26.03 ? 384  LEU A O   1 
ATOM   2692  C  CB  . LEU A 1 392 ? 29.601  -19.214 25.686  1.00 17.95 ? 384  LEU A CB  1 
ATOM   2693  C  CG  . LEU A 1 392 ? 30.847  -18.816 26.481  1.00 19.96 ? 384  LEU A CG  1 
ATOM   2694  C  CD1 . LEU A 1 392 ? 31.201  -19.860 27.543  1.00 27.05 ? 384  LEU A CD1 1 
ATOM   2695  C  CD2 . LEU A 1 392 ? 32.018  -18.595 25.553  1.00 25.73 ? 384  LEU A CD2 1 
ATOM   2696  N  N   . THR A 1 393 ? 27.813  -17.973 22.623  1.00 22.49 ? 385  THR A N   1 
ATOM   2697  C  CA  . THR A 1 393 ? 26.622  -18.185 21.811  1.00 16.87 ? 385  THR A CA  1 
ATOM   2698  C  C   . THR A 1 393 ? 26.899  -18.794 20.451  1.00 29.61 ? 385  THR A C   1 
ATOM   2699  O  O   . THR A 1 393 ? 25.948  -19.174 19.762  1.00 26.96 ? 385  THR A O   1 
ATOM   2700  C  CB  . THR A 1 393 ? 25.882  -16.860 21.594  1.00 19.70 ? 385  THR A CB  1 
ATOM   2701  O  OG1 . THR A 1 393 ? 26.836  -15.795 21.448  1.00 25.74 ? 385  THR A OG1 1 
ATOM   2702  C  CG2 . THR A 1 393 ? 24.992  -16.582 22.764  1.00 20.39 ? 385  THR A CG2 1 
ATOM   2703  N  N   . ASP A 1 394 ? 28.149  -18.856 20.019  1.00 26.50 ? 386  ASP A N   1 
ATOM   2704  C  CA  . ASP A 1 394 ? 28.410  -19.556 18.773  1.00 32.04 ? 386  ASP A CA  1 
ATOM   2705  C  C   . ASP A 1 394 ? 28.611  -21.031 19.081  1.00 34.35 ? 386  ASP A C   1 
ATOM   2706  O  O   . ASP A 1 394 ? 28.815  -21.427 20.229  1.00 27.88 ? 386  ASP A O   1 
ATOM   2707  C  CB  . ASP A 1 394 ? 29.620  -18.968 18.047  1.00 30.75 ? 386  ASP A CB  1 
ATOM   2708  C  CG  . ASP A 1 394 ? 30.837  -18.847 18.935  1.00 40.28 ? 386  ASP A CG  1 
ATOM   2709  O  OD1 . ASP A 1 394 ? 30.714  -19.050 20.163  1.00 45.89 ? 386  ASP A OD1 1 
ATOM   2710  O  OD2 . ASP A 1 394 ? 31.927  -18.545 18.403  1.00 42.05 ? 386  ASP A OD2 1 
ATOM   2711  N  N   . TRP A 1 395 ? 28.498  -21.853 18.051  1.00 35.27 ? 387  TRP A N   1 
ATOM   2712  C  CA  . TRP A 1 395 ? 28.757  -23.270 18.214  1.00 30.86 ? 387  TRP A CA  1 
ATOM   2713  C  C   . TRP A 1 395 ? 29.661  -23.702 17.076  1.00 30.75 ? 387  TRP A C   1 
ATOM   2714  O  O   . TRP A 1 395 ? 30.124  -22.880 16.277  1.00 29.63 ? 387  TRP A O   1 
ATOM   2715  C  CB  . TRP A 1 395 ? 27.451  -24.083 18.297  1.00 25.57 ? 387  TRP A CB  1 
ATOM   2716  C  CG  . TRP A 1 395 ? 26.582  -23.992 17.087  1.00 24.82 ? 387  TRP A CG  1 
ATOM   2717  C  CD1 . TRP A 1 395 ? 26.471  -24.923 16.083  1.00 22.34 ? 387  TRP A CD1 1 
ATOM   2718  C  CD2 . TRP A 1 395 ? 25.696  -22.921 16.739  1.00 23.10 ? 387  TRP A CD2 1 
ATOM   2719  N  NE1 . TRP A 1 395 ? 25.585  -24.487 15.135  1.00 20.77 ? 387  TRP A NE1 1 
ATOM   2720  C  CE2 . TRP A 1 395 ? 25.092  -23.263 15.510  1.00 19.86 ? 387  TRP A CE2 1 
ATOM   2721  C  CE3 . TRP A 1 395 ? 25.361  -21.702 17.339  1.00 24.26 ? 387  TRP A CE3 1 
ATOM   2722  C  CZ2 . TRP A 1 395 ? 24.164  -22.433 14.878  1.00 17.68 ? 387  TRP A CZ2 1 
ATOM   2723  C  CZ3 . TRP A 1 395 ? 24.441  -20.878 16.706  1.00 21.48 ? 387  TRP A CZ3 1 
ATOM   2724  C  CH2 . TRP A 1 395 ? 23.853  -21.251 15.488  1.00 20.10 ? 387  TRP A CH2 1 
ATOM   2725  N  N   . SER A 1 396 ? 29.952  -25.000 17.022  1.00 25.73 ? 388  SER A N   1 
ATOM   2726  C  CA  . SER A 1 396 ? 30.968  -25.467 16.090  1.00 26.16 ? 388  SER A CA  1 
ATOM   2727  C  C   . SER A 1 396 ? 30.604  -25.127 14.651  1.00 28.84 ? 388  SER A C   1 
ATOM   2728  O  O   . SER A 1 396 ? 31.495  -24.898 13.828  1.00 32.51 ? 388  SER A O   1 
ATOM   2729  C  CB  . SER A 1 396 ? 31.182  -26.974 16.260  1.00 26.21 ? 388  SER A CB  1 
ATOM   2730  O  OG  . SER A 1 396 ? 30.040  -27.705 15.846  1.00 24.56 ? 388  SER A OG  1 
ATOM   2731  N  N   . ASN A 1 397 ? 29.307  -25.047 14.338  1.00 28.54 ? 389  ASN A N   1 
ATOM   2732  C  CA  . ASN A 1 397 ? 28.844  -24.873 12.964  1.00 28.66 ? 389  ASN A CA  1 
ATOM   2733  C  C   . ASN A 1 397 ? 28.112  -23.552 12.737  1.00 29.92 ? 389  ASN A C   1 
ATOM   2734  O  O   . ASN A 1 397 ? 27.377  -23.421 11.755  1.00 34.87 ? 389  ASN A O   1 
ATOM   2735  C  CB  . ASN A 1 397 ? 27.951  -26.045 12.556  1.00 31.51 ? 389  ASN A CB  1 
ATOM   2736  C  CG  . ASN A 1 397 ? 28.706  -27.352 12.512  1.00 37.00 ? 389  ASN A CG  1 
ATOM   2737  O  OD1 . ASN A 1 397 ? 29.916  -27.361 12.326  1.00 48.78 ? 389  ASN A OD1 1 
ATOM   2738  N  ND2 . ASN A 1 397 ? 27.999  -28.461 12.693  1.00 33.93 ? 389  ASN A ND2 1 
ATOM   2739  N  N   . SER A 1 398 ? 28.289  -22.564 13.612  1.00 23.95 ? 390  SER A N   1 
ATOM   2740  C  CA  . SER A 1 398 ? 27.686  -21.265 13.346  1.00 20.56 ? 390  SER A CA  1 
ATOM   2741  C  C   . SER A 1 398 ? 28.441  -20.581 12.208  1.00 22.38 ? 390  SER A C   1 
ATOM   2742  O  O   . SER A 1 398 ? 29.676  -20.633 12.135  1.00 20.93 ? 390  SER A O   1 
ATOM   2743  C  CB  . SER A 1 398 ? 27.659  -20.397 14.608  1.00 24.87 ? 390  SER A CB  1 
ATOM   2744  O  OG  . SER A 1 398 ? 28.894  -20.402 15.291  1.00 24.12 ? 390  SER A OG  1 
ATOM   2745  N  N   . VAL A 1 399 ? 27.685  -20.015 11.274  1.00 19.55 ? 391  VAL A N   1 
ATOM   2746  C  CA  . VAL A 1 399 ? 28.225  -19.290 10.131  1.00 21.86 ? 391  VAL A CA  1 
ATOM   2747  C  C   . VAL A 1 399 ? 27.700  -17.866 10.229  1.00 18.51 ? 391  VAL A C   1 
ATOM   2748  O  O   . VAL A 1 399 ? 26.482  -17.651 10.245  1.00 17.15 ? 391  VAL A O   1 
ATOM   2749  C  CB  . VAL A 1 399 ? 27.830  -19.942 8.794   1.00 19.52 ? 391  VAL A CB  1 
ATOM   2750  C  CG1 . VAL A 1 399 ? 28.206  -19.036 7.632   1.00 25.15 ? 391  VAL A CG1 1 
ATOM   2751  C  CG2 . VAL A 1 399 ? 28.501  -21.311 8.654   1.00 22.38 ? 391  VAL A CG2 1 
ATOM   2752  N  N   . SER A 1 400 ? 28.612  -16.903 10.334  1.00 20.71 ? 392  SER A N   1 
ATOM   2753  C  CA  . SER A 1 400 ? 28.221  -15.511 10.518  1.00 19.92 ? 392  SER A CA  1 
ATOM   2754  C  C   . SER A 1 400 ? 27.545  -14.971 9.262   1.00 19.95 ? 392  SER A C   1 
ATOM   2755  O  O   . SER A 1 400 ? 28.085  -15.092 8.158   1.00 19.99 ? 392  SER A O   1 
ATOM   2756  C  CB  . SER A 1 400 ? 29.451  -14.662 10.852  1.00 22.62 ? 392  SER A CB  1 
ATOM   2757  O  OG  . SER A 1 400 ? 30.050  -15.070 12.071  1.00 25.51 ? 392  SER A OG  1 
ATOM   2758  N  N   . VAL A 1 401 ? 26.377  -14.350 9.435   1.00 17.03 ? 393  VAL A N   1 
ATOM   2759  C  CA  . VAL A 1 401 ? 25.701  -13.693 8.320   1.00 16.20 ? 393  VAL A CA  1 
ATOM   2760  C  C   . VAL A 1 401 ? 26.495  -12.459 7.918   1.00 18.03 ? 393  VAL A C   1 
ATOM   2761  O  O   . VAL A 1 401 ? 26.966  -11.696 8.774   1.00 16.99 ? 393  VAL A O   1 
ATOM   2762  C  CB  . VAL A 1 401 ? 24.256  -13.324 8.698   1.00 19.84 ? 393  VAL A CB  1 
ATOM   2763  C  CG1 . VAL A 1 401 ? 23.606  -12.485 7.590   1.00 19.82 ? 393  VAL A CG1 1 
ATOM   2764  C  CG2 . VAL A 1 401 ? 23.427  -14.582 8.974   1.00 19.06 ? 393  VAL A CG2 1 
ATOM   2765  N  N   . THR A 1 402 ? 26.659  -12.260 6.611   1.00 18.51 ? 394  THR A N   1 
ATOM   2766  C  CA  . THR A 1 402 ? 27.384  -11.121 6.068   1.00 17.47 ? 394  THR A CA  1 
ATOM   2767  C  C   . THR A 1 402 ? 26.535  -10.430 5.010   1.00 22.19 ? 394  THR A C   1 
ATOM   2768  O  O   . THR A 1 402 ? 25.475  -10.916 4.613   1.00 20.31 ? 394  THR A O   1 
ATOM   2769  C  CB  . THR A 1 402 ? 28.731  -11.546 5.455   1.00 24.30 ? 394  THR A CB  1 
ATOM   2770  O  OG1 . THR A 1 402 ? 28.500  -12.440 4.356   1.00 23.56 ? 394  THR A OG1 1 
ATOM   2771  C  CG2 . THR A 1 402 ? 29.598  -12.238 6.505   1.00 24.58 ? 394  THR A CG2 1 
ATOM   2772  N  N   . ARG A 1 403 ? 27.035  -9.290  4.532   1.00 25.25 ? 395  ARG A N   1 
ATOM   2773  C  CA  . ARG A 1 403 ? 26.364  -8.583  3.442   1.00 26.58 ? 395  ARG A CA  1 
ATOM   2774  C  C   . ARG A 1 403 ? 26.191  -9.478  2.216   1.00 26.75 ? 395  ARG A C   1 
ATOM   2775  O  O   . ARG A 1 403 ? 25.157  -9.423  1.541   1.00 32.44 ? 395  ARG A O   1 
ATOM   2776  C  CB  . ARG A 1 403 ? 27.150  -7.316  3.082   1.00 30.17 ? 395  ARG A CB  1 
ATOM   2777  C  CG  . ARG A 1 403 ? 26.556  -6.506  1.938   1.00 33.98 ? 395  ARG A CG  1 
ATOM   2778  C  CD  . ARG A 1 403 ? 27.526  -5.431  1.456   1.00 40.01 ? 395  ARG A CD  1 
ATOM   2779  N  NE  . ARG A 1 403 ? 27.611  -4.317  2.392   1.00 51.43 ? 395  ARG A NE  1 
ATOM   2780  C  CZ  . ARG A 1 403 ? 26.866  -3.216  2.319   1.00 53.06 ? 395  ARG A CZ  1 
ATOM   2781  N  NH1 . ARG A 1 403 ? 25.979  -3.070  1.340   1.00 51.12 ? 395  ARG A NH1 1 
ATOM   2782  N  NH2 . ARG A 1 403 ? 27.017  -2.254  3.223   1.00 48.35 ? 395  ARG A NH2 1 
ATOM   2783  N  N   . ASP A 1 404 ? 27.178  -10.323 1.921   1.00 24.27 ? 396  ASP A N   1 
ATOM   2784  C  CA  . ASP A 1 404 ? 27.176  -11.077 0.675   1.00 27.24 ? 396  ASP A CA  1 
ATOM   2785  C  C   . ASP A 1 404 ? 26.702  -12.519 0.813   1.00 25.40 ? 396  ASP A C   1 
ATOM   2786  O  O   . ASP A 1 404 ? 26.537  -13.189 -0.210  1.00 26.74 ? 396  ASP A O   1 
ATOM   2787  C  CB  . ASP A 1 404 ? 28.580  -11.074 0.054   1.00 32.42 ? 396  ASP A CB  1 
ATOM   2788  C  CG  . ASP A 1 404 ? 29.033  -9.685  -0.361  1.00 42.87 ? 396  ASP A CG  1 
ATOM   2789  O  OD1 . ASP A 1 404 ? 28.178  -8.873  -0.780  1.00 46.01 ? 396  ASP A OD1 1 
ATOM   2790  O  OD2 . ASP A 1 404 ? 30.245  -9.406  -0.263  1.00 47.00 ? 396  ASP A OD2 1 
ATOM   2791  N  N   . LYS A 1 405 ? 26.484  -13.020 2.026   1.00 20.37 ? 397  LYS A N   1 
ATOM   2792  C  CA  . LYS A 1 405 ? 26.192  -14.438 2.195   1.00 24.52 ? 397  LYS A CA  1 
ATOM   2793  C  C   . LYS A 1 405 ? 25.210  -14.629 3.338   1.00 21.53 ? 397  LYS A C   1 
ATOM   2794  O  O   . LYS A 1 405 ? 25.084  -13.778 4.221   1.00 25.83 ? 397  LYS A O   1 
ATOM   2795  C  CB  . LYS A 1 405 ? 27.472  -15.241 2.463   1.00 25.87 ? 397  LYS A CB  1 
ATOM   2796  N  N   . GLY A 1 406 ? 24.521  -15.770 3.318   1.00 21.29 ? 398  GLY A N   1 
ATOM   2797  C  CA  . GLY A 1 406 ? 23.639  -16.146 4.405   1.00 19.73 ? 398  GLY A CA  1 
ATOM   2798  C  C   . GLY A 1 406 ? 24.419  -16.742 5.568   1.00 21.35 ? 398  GLY A C   1 
ATOM   2799  O  O   . GLY A 1 406 ? 25.648  -16.720 5.615   1.00 21.30 ? 398  GLY A O   1 
ATOM   2800  N  N   . GLY A 1 407 ? 23.676  -17.284 6.524   1.00 18.69 ? 399  GLY A N   1 
ATOM   2801  C  CA  . GLY A 1 407 ? 24.295  -17.909 7.674   1.00 19.82 ? 399  GLY A CA  1 
ATOM   2802  C  C   . GLY A 1 407 ? 23.248  -18.216 8.723   1.00 19.59 ? 399  GLY A C   1 
ATOM   2803  O  O   . GLY A 1 407 ? 22.045  -18.151 8.459   1.00 22.47 ? 399  GLY A O   1 
ATOM   2804  N  N   . ASN A 1 408 ? 23.729  -18.566 9.920   1.00 23.11 ? 400  ASN A N   1 
ATOM   2805  C  CA  . ASN A 1 408 ? 22.827  -18.826 11.038  1.00 16.13 ? 400  ASN A CA  1 
ATOM   2806  C  C   . ASN A 1 408 ? 23.301  -18.147 12.317  1.00 18.22 ? 400  ASN A C   1 
ATOM   2807  O  O   . ASN A 1 408 ? 22.876  -18.532 13.414  1.00 16.34 ? 400  ASN A O   1 
ATOM   2808  C  CB  . ASN A 1 408 ? 22.635  -20.332 11.255  1.00 17.70 ? 400  ASN A CB  1 
ATOM   2809  C  CG  . ASN A 1 408 ? 23.949  -21.080 11.416  1.00 19.72 ? 400  ASN A CG  1 
ATOM   2810  O  OD1 . ASN A 1 408 ? 25.011  -20.476 11.595  1.00 19.26 ? 400  ASN A OD1 1 
ATOM   2811  N  ND2 . ASN A 1 408 ? 23.880  -22.406 11.347  1.00 22.15 ? 400  ASN A ND2 1 
ATOM   2812  N  N   . TYR A 1 409 ? 24.168  -17.144 12.202  1.00 16.51 ? 401  TYR A N   1 
ATOM   2813  C  CA  . TYR A 1 409 ? 24.643  -16.416 13.372  1.00 16.63 ? 401  TYR A CA  1 
ATOM   2814  C  C   . TYR A 1 409 ? 24.734  -14.941 13.022  1.00 15.34 ? 401  TYR A C   1 
ATOM   2815  O  O   . TYR A 1 409 ? 25.311  -14.583 11.988  1.00 16.15 ? 401  TYR A O   1 
ATOM   2816  C  CB  . TYR A 1 409 ? 26.006  -16.946 13.853  1.00 15.27 ? 401  TYR A CB  1 
ATOM   2817  C  CG  . TYR A 1 409 ? 26.350  -16.442 15.246  1.00 22.09 ? 401  TYR A CG  1 
ATOM   2818  C  CD1 . TYR A 1 409 ? 26.982  -15.221 15.421  1.00 23.71 ? 401  TYR A CD1 1 
ATOM   2819  C  CD2 . TYR A 1 409 ? 26.001  -17.167 16.381  1.00 21.15 ? 401  TYR A CD2 1 
ATOM   2820  C  CE1 . TYR A 1 409 ? 27.280  -14.739 16.686  1.00 23.67 ? 401  TYR A CE1 1 
ATOM   2821  C  CE2 . TYR A 1 409 ? 26.300  -16.689 17.662  1.00 19.00 ? 401  TYR A CE2 1 
ATOM   2822  C  CZ  . TYR A 1 409 ? 26.935  -15.470 17.796  1.00 21.44 ? 401  TYR A CZ  1 
ATOM   2823  O  OH  . TYR A 1 409 ? 27.245  -14.968 19.048  1.00 23.65 ? 401  TYR A OH  1 
ATOM   2824  N  N   . ILE A 1 410 ? 24.165  -14.088 13.872  1.00 14.63 ? 402  ILE A N   1 
ATOM   2825  C  CA  . ILE A 1 410 ? 24.114  -12.654 13.612  1.00 15.04 ? 402  ILE A CA  1 
ATOM   2826  C  C   . ILE A 1 410 ? 24.947  -11.935 14.659  1.00 16.14 ? 402  ILE A C   1 
ATOM   2827  O  O   . ILE A 1 410 ? 24.697  -12.070 15.863  1.00 15.68 ? 402  ILE A O   1 
ATOM   2828  C  CB  . ILE A 1 410 ? 22.676  -12.124 13.608  1.00 14.59 ? 402  ILE A CB  1 
ATOM   2829  C  CG1 . ILE A 1 410 ? 21.875  -12.798 12.488  1.00 20.68 ? 402  ILE A CG1 1 
ATOM   2830  C  CG2 . ILE A 1 410 ? 22.692  -10.600 13.439  1.00 12.17 ? 402  ILE A CG2 1 
ATOM   2831  C  CD1 . ILE A 1 410 ? 20.368  -12.616 12.631  1.00 20.12 ? 402  ILE A CD1 1 
ATOM   2832  N  N   . HIS A 1 411 ? 25.933  -11.173 14.200  1.00 13.73 ? 403  HIS A N   1 
ATOM   2833  C  CA  . HIS A 1 411 ? 26.662  -10.256 15.072  1.00 15.44 ? 403  HIS A CA  1 
ATOM   2834  C  C   . HIS A 1 411 ? 25.850  -8.972  15.140  1.00 16.57 ? 403  HIS A C   1 
ATOM   2835  O  O   . HIS A 1 411 ? 25.868  -8.166  14.207  1.00 14.70 ? 403  HIS A O   1 
ATOM   2836  C  CB  . HIS A 1 411 ? 28.061  -9.977  14.543  1.00 14.19 ? 403  HIS A CB  1 
ATOM   2837  C  CG  . HIS A 1 411 ? 28.973  -11.165 14.546  1.00 24.84 ? 403  HIS A CG  1 
ATOM   2838  N  ND1 . HIS A 1 411 ? 29.693  -11.549 15.659  1.00 25.79 ? 403  HIS A ND1 1 
ATOM   2839  C  CD2 . HIS A 1 411 ? 29.321  -12.023 13.557  1.00 25.84 ? 403  HIS A CD2 1 
ATOM   2840  C  CE1 . HIS A 1 411 ? 30.431  -12.603 15.358  1.00 26.52 ? 403  HIS A CE1 1 
ATOM   2841  N  NE2 . HIS A 1 411 ? 30.224  -12.912 14.090  1.00 26.53 ? 403  HIS A NE2 1 
ATOM   2842  N  N   . TYR A 1 412 ? 25.112  -8.786  16.235  1.00 11.87 ? 404  TYR A N   1 
ATOM   2843  C  CA  . TYR A 1 412 ? 24.262  -7.610  16.337  1.00 11.34 ? 404  TYR A CA  1 
ATOM   2844  C  C   . TYR A 1 412 ? 25.023  -6.333  16.671  1.00 13.01 ? 404  TYR A C   1 
ATOM   2845  O  O   . TYR A 1 412 ? 24.439  -5.250  16.567  1.00 12.56 ? 404  TYR A O   1 
ATOM   2846  C  CB  . TYR A 1 412 ? 23.177  -7.839  17.388  1.00 13.84 ? 404  TYR A CB  1 
ATOM   2847  C  CG  . TYR A 1 412 ? 22.124  -8.820  16.953  1.00 14.66 ? 404  TYR A CG  1 
ATOM   2848  C  CD1 . TYR A 1 412 ? 21.027  -8.395  16.198  1.00 12.66 ? 404  TYR A CD1 1 
ATOM   2849  C  CD2 . TYR A 1 412 ? 22.220  -10.171 17.280  1.00 11.94 ? 404  TYR A CD2 1 
ATOM   2850  C  CE1 . TYR A 1 412 ? 20.055  -9.277  15.794  1.00 13.21 ? 404  TYR A CE1 1 
ATOM   2851  C  CE2 . TYR A 1 412 ? 21.230  -11.075 16.879  1.00 10.73 ? 404  TYR A CE2 1 
ATOM   2852  C  CZ  . TYR A 1 412 ? 20.152  -10.608 16.134  1.00 11.49 ? 404  TYR A CZ  1 
ATOM   2853  O  OH  . TYR A 1 412 ? 19.176  -11.475 15.710  1.00 13.27 ? 404  TYR A OH  1 
ATOM   2854  N  N   . GLY A 1 413 ? 26.292  -6.419  17.064  1.00 11.85 ? 405  GLY A N   1 
ATOM   2855  C  CA  . GLY A 1 413 ? 26.968  -5.238  17.570  1.00 13.35 ? 405  GLY A CA  1 
ATOM   2856  C  C   . GLY A 1 413 ? 26.430  -4.828  18.939  1.00 11.30 ? 405  GLY A C   1 
ATOM   2857  O  O   . GLY A 1 413 ? 25.656  -5.538  19.578  1.00 12.98 ? 405  GLY A O   1 
ATOM   2858  N  N   . VAL A 1 414 ? 26.842  -3.634  19.376  1.00 11.35 ? 406  VAL A N   1 
ATOM   2859  C  CA  . VAL A 1 414 ? 26.447  -3.135  20.692  1.00 10.85 ? 406  VAL A CA  1 
ATOM   2860  C  C   . VAL A 1 414 ? 25.073  -2.486  20.565  1.00 11.40 ? 406  VAL A C   1 
ATOM   2861  O  O   . VAL A 1 414 ? 24.928  -1.257  20.625  1.00 11.50 ? 406  VAL A O   1 
ATOM   2862  C  CB  . VAL A 1 414 ? 27.495  -2.166  21.270  1.00 11.21 ? 406  VAL A CB  1 
ATOM   2863  C  CG1 . VAL A 1 414 ? 27.236  -1.926  22.756  1.00 11.48 ? 406  VAL A CG1 1 
ATOM   2864  C  CG2 . VAL A 1 414 ? 28.899  -2.740  21.071  1.00 13.39 ? 406  VAL A CG2 1 
ATOM   2865  N  N   . ARG A 1 415 ? 24.053  -3.328  20.367  1.00 9.99  ? 407  ARG A N   1 
ATOM   2866  C  CA  . ARG A 1 415 ? 22.713  -2.911  19.964  1.00 9.85  ? 407  ARG A CA  1 
ATOM   2867  C  C   . ARG A 1 415 ? 21.695  -3.878  20.578  1.00 10.55 ? 407  ARG A C   1 
ATOM   2868  O  O   . ARG A 1 415 ? 21.041  -4.639  19.881  1.00 10.29 ? 407  ARG A O   1 
ATOM   2869  C  CB  . ARG A 1 415 ? 22.584  -2.893  18.434  1.00 11.18 ? 407  ARG A CB  1 
ATOM   2870  C  CG  . ARG A 1 415 ? 23.596  -2.023  17.647  1.00 10.57 ? 407  ARG A CG  1 
ATOM   2871  C  CD  . ARG A 1 415 ? 23.329  -2.225  16.146  1.00 10.91 ? 407  ARG A CD  1 
ATOM   2872  N  NE  . ARG A 1 415 ? 24.170  -1.435  15.245  1.00 14.07 ? 407  ARG A NE  1 
ATOM   2873  C  CZ  . ARG A 1 415 ? 25.199  -1.922  14.557  1.00 15.14 ? 407  ARG A CZ  1 
ATOM   2874  N  NH1 . ARG A 1 415 ? 25.544  -3.201  14.704  1.00 13.12 ? 407  ARG A NH1 1 
ATOM   2875  N  NH2 . ARG A 1 415 ? 25.888  -1.131  13.728  1.00 12.78 ? 407  ARG A NH2 1 
ATOM   2876  N  N   . GLU A 1 416 ? 21.504  -3.823  21.906  1.00 10.46 ? 408  GLU A N   1 
ATOM   2877  C  CA  . GLU A 1 416 ? 20.642  -4.812  22.551  1.00 10.84 ? 408  GLU A CA  1 
ATOM   2878  C  C   . GLU A 1 416 ? 19.177  -4.610  22.176  1.00 10.48 ? 408  GLU A C   1 
ATOM   2879  O  O   . GLU A 1 416 ? 18.479  -5.574  21.839  1.00 11.80 ? 408  GLU A O   1 
ATOM   2880  C  CB  . GLU A 1 416 ? 20.810  -4.770  24.076  1.00 12.11 ? 408  GLU A CB  1 
ATOM   2881  C  CG  . GLU A 1 416 ? 22.210  -5.124  24.571  1.00 12.82 ? 408  GLU A CG  1 
ATOM   2882  C  CD  . GLU A 1 416 ? 23.174  -3.948  24.506  1.00 13.64 ? 408  GLU A CD  1 
ATOM   2883  O  OE1 . GLU A 1 416 ? 22.726  -2.818  24.242  1.00 13.77 ? 408  GLU A OE1 1 
ATOM   2884  O  OE2 . GLU A 1 416 ? 24.384  -4.157  24.711  1.00 17.19 ? 408  GLU A OE2 1 
ATOM   2885  N  N   . PHE A 1 417 ? 18.686  -3.366  22.235  1.00 9.06  ? 409  PHE A N   1 
ATOM   2886  C  CA  . PHE A 1 417 ? 17.289  -3.117  21.871  1.00 12.53 ? 409  PHE A CA  1 
ATOM   2887  C  C   . PHE A 1 417 ? 17.039  -3.511  20.420  1.00 13.96 ? 409  PHE A C   1 
ATOM   2888  O  O   . PHE A 1 417 ? 16.038  -4.170  20.098  1.00 12.78 ? 409  PHE A O   1 
ATOM   2889  C  CB  . PHE A 1 417 ? 16.936  -1.642  22.092  1.00 10.57 ? 409  PHE A CB  1 
ATOM   2890  C  CG  . PHE A 1 417 ? 15.439  -1.369  22.257  1.00 8.87  ? 409  PHE A CG  1 
ATOM   2891  C  CD1 . PHE A 1 417 ? 14.492  -2.381  22.112  1.00 9.18  ? 409  PHE A CD1 1 
ATOM   2892  C  CD2 . PHE A 1 417 ? 14.997  -0.091  22.555  1.00 8.04  ? 409  PHE A CD2 1 
ATOM   2893  C  CE1 . PHE A 1 417 ? 13.123  -2.111  22.269  1.00 12.81 ? 409  PHE A CE1 1 
ATOM   2894  C  CE2 . PHE A 1 417 ? 13.644  0.192   22.717  1.00 9.83  ? 409  PHE A CE2 1 
ATOM   2895  C  CZ  . PHE A 1 417 ? 12.701  -0.822  22.578  1.00 14.54 ? 409  PHE A CZ  1 
ATOM   2896  N  N   . GLY A 1 418 ? 17.945  -3.113  19.526  1.00 11.33 ? 410  GLY A N   1 
ATOM   2897  C  CA  . GLY A 1 418 ? 17.814  -3.528  18.139  1.00 14.10 ? 410  GLY A CA  1 
ATOM   2898  C  C   . GLY A 1 418 ? 17.780  -5.038  17.998  1.00 12.31 ? 410  GLY A C   1 
ATOM   2899  O  O   . GLY A 1 418 ? 16.941  -5.589  17.281  1.00 9.54  ? 410  GLY A O   1 
ATOM   2900  N  N   . MET A 1 419 ? 18.681  -5.729  18.700  1.00 9.21  ? 411  MET A N   1 
ATOM   2901  C  CA  . MET A 1 419 ? 18.700  -7.190  18.652  1.00 11.00 ? 411  MET A CA  1 
ATOM   2902  C  C   . MET A 1 419 ? 17.354  -7.780  19.056  1.00 12.19 ? 411  MET A C   1 
ATOM   2903  O  O   . MET A 1 419 ? 16.804  -8.642  18.358  1.00 10.93 ? 411  MET A O   1 
ATOM   2904  C  CB  . MET A 1 419 ? 19.792  -7.739  19.569  1.00 14.79 ? 411  MET A CB  1 
ATOM   2905  C  CG  . MET A 1 419 ? 19.731  -9.257  19.714  1.00 9.31  ? 411  MET A CG  1 
ATOM   2906  S  SD  . MET A 1 419 ? 21.111  -9.913  20.694  1.00 12.19 ? 411  MET A SD  1 
ATOM   2907  C  CE  . MET A 1 419 ? 20.596  -9.514  22.362  1.00 13.00 ? 411  MET A CE  1 
ATOM   2908  N  N   . GLY A 1 420 ? 16.822  -7.349  20.198  1.00 10.61 ? 412  GLY A N   1 
ATOM   2909  C  CA  . GLY A 1 420 ? 15.577  -7.928  20.673  1.00 9.92  ? 412  GLY A CA  1 
ATOM   2910  C  C   . GLY A 1 420 ? 14.437  -7.712  19.699  1.00 11.91 ? 412  GLY A C   1 
ATOM   2911  O  O   . GLY A 1 420 ? 13.692  -8.639  19.373  1.00 12.06 ? 412  GLY A O   1 
ATOM   2912  N  N   . ALA A 1 421 ? 14.304  -6.488  19.192  1.00 9.84  ? 413  ALA A N   1 
ATOM   2913  C  CA  . ALA A 1 421 ? 13.197  -6.222  18.284  1.00 10.54 ? 413  ALA A CA  1 
ATOM   2914  C  C   . ALA A 1 421 ? 13.443  -6.839  16.906  1.00 11.59 ? 413  ALA A C   1 
ATOM   2915  O  O   . ALA A 1 421 ? 12.483  -7.238  16.231  1.00 12.58 ? 413  ALA A O   1 
ATOM   2916  C  CB  . ALA A 1 421 ? 12.955  -4.716  18.205  1.00 12.01 ? 413  ALA A CB  1 
ATOM   2917  N  N   . ILE A 1 422 ? 14.707  -6.954  16.475  1.00 9.11  ? 414  ILE A N   1 
ATOM   2918  C  CA  . ILE A 1 422 ? 15.001  -7.679  15.236  1.00 11.71 ? 414  ILE A CA  1 
ATOM   2919  C  C   . ILE A 1 422 ? 14.645  -9.154  15.387  1.00 10.82 ? 414  ILE A C   1 
ATOM   2920  O  O   . ILE A 1 422 ? 14.104  -9.773  14.462  1.00 11.92 ? 414  ILE A O   1 
ATOM   2921  C  CB  . ILE A 1 422 ? 16.478  -7.504  14.822  1.00 10.93 ? 414  ILE A CB  1 
ATOM   2922  C  CG1 . ILE A 1 422 ? 16.738  -6.105  14.276  1.00 9.89  ? 414  ILE A CG1 1 
ATOM   2923  C  CG2 . ILE A 1 422 ? 16.885  -8.567  13.769  1.00 12.95 ? 414  ILE A CG2 1 
ATOM   2924  C  CD1 . ILE A 1 422 ? 18.232  -5.779  14.129  1.00 10.17 ? 414  ILE A CD1 1 
ATOM   2925  N  N   . MET A 1 423 ? 14.956  -9.748  16.545  1.00 12.36 ? 415  MET A N   1 
ATOM   2926  C  CA  A MET A 1 423 ? 14.607  -11.148 16.749  0.52 11.55 ? 415  MET A CA  1 
ATOM   2927  C  CA  B MET A 1 423 ? 14.603  -11.146 16.783  0.48 11.69 ? 415  MET A CA  1 
ATOM   2928  C  C   . MET A 1 423 ? 13.103  -11.353 16.679  1.00 10.88 ? 415  MET A C   1 
ATOM   2929  O  O   . MET A 1 423 ? 12.642  -12.365 16.138  1.00 11.50 ? 415  MET A O   1 
ATOM   2930  C  CB  A MET A 1 423 ? 15.159  -11.657 18.081  0.52 9.95  ? 415  MET A CB  1 
ATOM   2931  C  CB  B MET A 1 423 ? 15.089  -11.597 18.162  0.48 9.70  ? 415  MET A CB  1 
ATOM   2932  C  CG  A MET A 1 423 ? 16.634  -11.988 18.010  0.52 11.32 ? 415  MET A CG  1 
ATOM   2933  C  CG  B MET A 1 423 ? 16.576  -11.835 18.258  0.48 11.52 ? 415  MET A CG  1 
ATOM   2934  S  SD  A MET A 1 423 ? 17.165  -13.043 19.356  0.52 15.36 ? 415  MET A SD  1 
ATOM   2935  S  SD  B MET A 1 423 ? 17.110  -11.834 19.975  0.48 11.59 ? 415  MET A SD  1 
ATOM   2936  C  CE  A MET A 1 423 ? 16.906  -11.978 20.765  0.52 10.44 ? 415  MET A CE  1 
ATOM   2937  C  CE  B MET A 1 423 ? 16.169  -13.205 20.629  0.48 9.37  ? 415  MET A CE  1 
ATOM   2938  N  N   . ASN A 1 424 ? 12.324  -10.404 17.211  1.00 10.05 ? 416  ASN A N   1 
ATOM   2939  C  CA  . ASN A 1 424 ? 10.875  -10.488 17.066  1.00 10.70 ? 416  ASN A CA  1 
ATOM   2940  C  C   . ASN A 1 424 ? 10.491  -10.574 15.591  1.00 12.38 ? 416  ASN A C   1 
ATOM   2941  O  O   . ASN A 1 424 ? 9.684   -11.425 15.196  1.00 12.76 ? 416  ASN A O   1 
ATOM   2942  C  CB  . ASN A 1 424 ? 10.215  -9.288  17.740  1.00 13.03 ? 416  ASN A CB  1 
ATOM   2943  C  CG  . ASN A 1 424 ? 10.284  -9.361  19.260  1.00 8.77  ? 416  ASN A CG  1 
ATOM   2944  O  OD1 . ASN A 1 424 ? 10.676  -10.385 19.822  1.00 10.34 ? 416  ASN A OD1 1 
ATOM   2945  N  ND2 . ASN A 1 424 ? 9.912   -8.270  19.931  1.00 10.62 ? 416  ASN A ND2 1 
ATOM   2946  N  N   . GLY A 1 425 ? 11.115  -9.745  14.757  1.00 9.83  ? 417  GLY A N   1 
ATOM   2947  C  CA  . GLY A 1 425 ? 10.857  -9.810  13.322  1.00 16.26 ? 417  GLY A CA  1 
ATOM   2948  C  C   . GLY A 1 425 ? 11.303  -11.114 12.684  1.00 17.49 ? 417  GLY A C   1 
ATOM   2949  O  O   . GLY A 1 425 ? 10.609  -11.662 11.819  1.00 12.52 ? 417  GLY A O   1 
ATOM   2950  N  N   . LEU A 1 426 ? 12.470  -11.625 13.087  1.00 13.41 ? 418  LEU A N   1 
ATOM   2951  C  CA  . LEU A 1 426 ? 12.925  -12.915 12.567  1.00 14.54 ? 418  LEU A CA  1 
ATOM   2952  C  C   . LEU A 1 426 ? 11.898  -14.004 12.841  1.00 15.41 ? 418  LEU A C   1 
ATOM   2953  O  O   . LEU A 1 426 ? 11.562  -14.794 11.947  1.00 12.35 ? 418  LEU A O   1 
ATOM   2954  C  CB  . LEU A 1 426 ? 14.270  -13.300 13.186  1.00 11.08 ? 418  LEU A CB  1 
ATOM   2955  C  CG  . LEU A 1 426 ? 15.488  -12.512 12.690  1.00 11.16 ? 418  LEU A CG  1 
ATOM   2956  C  CD1 . LEU A 1 426 ? 16.681  -12.744 13.642  1.00 12.56 ? 418  LEU A CD1 1 
ATOM   2957  C  CD2 . LEU A 1 426 ? 15.822  -12.924 11.244  1.00 11.80 ? 418  LEU A CD2 1 
ATOM   2958  N  N   . VAL A 1 427 ? 11.387  -14.052 14.078  1.00 14.11 ? 419  VAL A N   1 
ATOM   2959  C  CA  A VAL A 1 427 ? 10.480  -15.137 14.381  0.59 13.94 ? 419  VAL A CA  1 
ATOM   2960  C  CA  B VAL A 1 427 ? 10.406  -15.061 14.504  0.41 14.24 ? 419  VAL A CA  1 
ATOM   2961  C  C   . VAL A 1 427 ? 9.118   -14.907 13.726  1.00 13.92 ? 419  VAL A C   1 
ATOM   2962  O  O   . VAL A 1 427 ? 8.489   -15.880 13.297  1.00 15.03 ? 419  VAL A O   1 
ATOM   2963  C  CB  A VAL A 1 427 ? 10.411  -15.359 15.907  0.59 15.19 ? 419  VAL A CB  1 
ATOM   2964  C  CB  B VAL A 1 427 ? 10.095  -14.929 16.012  0.41 14.45 ? 419  VAL A CB  1 
ATOM   2965  C  CG1 A VAL A 1 427 ? 9.583   -14.305 16.579  0.59 12.77 ? 419  VAL A CG1 1 
ATOM   2966  C  CG1 B VAL A 1 427 ? 8.972   -15.891 16.415  0.41 14.36 ? 419  VAL A CG1 1 
ATOM   2967  C  CG2 A VAL A 1 427 ? 9.895   -16.758 16.214  0.59 16.42 ? 419  VAL A CG2 1 
ATOM   2968  C  CG2 B VAL A 1 427 ? 11.282  -15.163 16.853  0.41 14.93 ? 419  VAL A CG2 1 
ATOM   2969  N  N   . LEU A 1 428 ? 8.660   -13.657 13.597  1.00 12.68 ? 420  LEU A N   1 
ATOM   2970  C  CA  . LEU A 1 428 ? 7.377   -13.418 12.952  1.00 13.75 ? 420  LEU A CA  1 
ATOM   2971  C  C   . LEU A 1 428 ? 7.394   -13.881 11.509  1.00 14.97 ? 420  LEU A C   1 
ATOM   2972  O  O   . LEU A 1 428 ? 6.377   -14.361 10.995  1.00 15.58 ? 420  LEU A O   1 
ATOM   2973  C  CB  . LEU A 1 428 ? 7.018   -11.935 13.026  1.00 11.47 ? 420  LEU A CB  1 
ATOM   2974  C  CG  . LEU A 1 428 ? 6.586   -11.429 14.402  1.00 14.61 ? 420  LEU A CG  1 
ATOM   2975  C  CD1 . LEU A 1 428 ? 6.796   -9.937  14.453  1.00 12.74 ? 420  LEU A CD1 1 
ATOM   2976  C  CD2 . LEU A 1 428 ? 5.112   -11.790 14.636  1.00 12.67 ? 420  LEU A CD2 1 
ATOM   2977  N  N   . HIS A 1 429 ? 8.544   -13.780 10.854  1.00 15.32 ? 421  HIS A N   1 
ATOM   2978  C  CA  . HIS A 1 429 ? 8.598   -14.092 9.431   1.00 17.14 ? 421  HIS A CA  1 
ATOM   2979  C  C   . HIS A 1 429 ? 8.221   -15.542 9.148   1.00 16.07 ? 421  HIS A C   1 
ATOM   2980  O  O   . HIS A 1 429 ? 7.589   -15.831 8.127   1.00 17.63 ? 421  HIS A O   1 
ATOM   2981  C  CB  . HIS A 1 429 ? 9.989   -13.792 8.886   1.00 12.64 ? 421  HIS A CB  1 
ATOM   2982  C  CG  . HIS A 1 429 ? 10.100  -13.986 7.408   1.00 13.27 ? 421  HIS A CG  1 
ATOM   2983  N  ND1 . HIS A 1 429 ? 10.353  -15.214 6.834   1.00 15.24 ? 421  HIS A ND1 1 
ATOM   2984  C  CD2 . HIS A 1 429 ? 9.965   -13.112 6.385   1.00 16.79 ? 421  HIS A CD2 1 
ATOM   2985  C  CE1 . HIS A 1 429 ? 10.382  -15.084 5.518   1.00 18.33 ? 421  HIS A CE1 1 
ATOM   2986  N  NE2 . HIS A 1 429 ? 10.155  -13.818 5.222   1.00 16.04 ? 421  HIS A NE2 1 
ATOM   2987  N  N   . GLY A 1 430 ? 8.582   -16.458 10.039  1.00 16.01 ? 422  GLY A N   1 
ATOM   2988  C  CA  . GLY A 1 430 ? 8.550   -17.876 9.714   1.00 17.85 ? 422  GLY A CA  1 
ATOM   2989  C  C   . GLY A 1 430 ? 9.864   -18.328 9.108   1.00 17.01 ? 422  GLY A C   1 
ATOM   2990  O  O   . GLY A 1 430 ? 10.599  -17.551 8.502   1.00 15.94 ? 422  GLY A O   1 
ATOM   2991  N  N   . GLY A 1 431 ? 10.197  -19.605 9.337   1.00 15.15 ? 423  GLY A N   1 
ATOM   2992  C  CA  . GLY A 1 431 ? 11.348  -20.246 8.726   1.00 15.01 ? 423  GLY A CA  1 
ATOM   2993  C  C   . GLY A 1 431 ? 12.600  -20.325 9.587   1.00 19.36 ? 423  GLY A C   1 
ATOM   2994  O  O   . GLY A 1 431 ? 13.482  -21.143 9.291   1.00 18.03 ? 423  GLY A O   1 
ATOM   2995  N  N   . VAL A 1 432 ? 12.717  -19.492 10.621  1.00 14.01 ? 424  VAL A N   1 
ATOM   2996  C  CA  . VAL A 1 432 ? 13.886  -19.494 11.492  1.00 14.59 ? 424  VAL A CA  1 
ATOM   2997  C  C   . VAL A 1 432 ? 13.431  -19.404 12.943  1.00 17.45 ? 424  VAL A C   1 
ATOM   2998  O  O   . VAL A 1 432 ? 12.348  -18.894 13.248  1.00 13.80 ? 424  VAL A O   1 
ATOM   2999  C  CB  . VAL A 1 432 ? 14.869  -18.336 11.182  1.00 16.52 ? 424  VAL A CB  1 
ATOM   3000  C  CG1 . VAL A 1 432 ? 15.482  -18.493 9.784   1.00 21.01 ? 424  VAL A CG1 1 
ATOM   3001  C  CG2 . VAL A 1 432 ? 14.181  -16.981 11.345  1.00 15.34 ? 424  VAL A CG2 1 
ATOM   3002  N  N   . LYS A 1 433 ? 14.284  -19.897 13.839  1.00 15.55 ? 425  LYS A N   1 
ATOM   3003  C  CA  . LYS A 1 433 ? 14.063  -19.816 15.285  1.00 13.88 ? 425  LYS A CA  1 
ATOM   3004  C  C   . LYS A 1 433 ? 15.262  -19.094 15.888  1.00 15.74 ? 425  LYS A C   1 
ATOM   3005  O  O   . LYS A 1 433 ? 16.349  -19.689 16.025  1.00 14.60 ? 425  LYS A O   1 
ATOM   3006  C  CB  . LYS A 1 433 ? 13.891  -21.208 15.896  1.00 13.57 ? 425  LYS A CB  1 
ATOM   3007  C  CG  . LYS A 1 433 ? 13.784  -21.220 17.428  1.00 17.10 ? 425  LYS A CG  1 
ATOM   3008  C  CD  . LYS A 1 433 ? 13.530  -22.615 17.996  1.00 25.32 ? 425  LYS A CD  1 
ATOM   3009  C  CE  . LYS A 1 433 ? 12.177  -23.185 17.553  1.00 20.06 ? 425  LYS A CE  1 
ATOM   3010  N  NZ  . LYS A 1 433 ? 11.060  -22.307 17.996  1.00 16.52 ? 425  LYS A NZ  1 
ATOM   3011  N  N   . PRO A 1 434 ? 15.139  -17.814 16.221  1.00 16.16 ? 426  PRO A N   1 
ATOM   3012  C  CA  . PRO A 1 434 ? 16.310  -17.060 16.661  1.00 19.17 ? 426  PRO A CA  1 
ATOM   3013  C  C   . PRO A 1 434 ? 16.496  -17.071 18.165  1.00 15.63 ? 426  PRO A C   1 
ATOM   3014  O  O   . PRO A 1 434 ? 15.548  -17.151 18.953  1.00 12.61 ? 426  PRO A O   1 
ATOM   3015  C  CB  . PRO A 1 434 ? 16.003  -15.639 16.175  1.00 14.91 ? 426  PRO A CB  1 
ATOM   3016  C  CG  . PRO A 1 434 ? 14.542  -15.545 16.367  1.00 16.01 ? 426  PRO A CG  1 
ATOM   3017  C  CD  . PRO A 1 434 ? 13.993  -16.923 15.987  1.00 14.82 ? 426  PRO A CD  1 
ATOM   3018  N  N   . PHE A 1 435 ? 17.766  -16.990 18.552  1.00 13.66 ? 427  PHE A N   1 
ATOM   3019  C  CA  . PHE A 1 435 ? 18.123  -16.628 19.909  1.00 12.68 ? 427  PHE A CA  1 
ATOM   3020  C  C   . PHE A 1 435 ? 19.166  -15.527 19.834  1.00 14.12 ? 427  PHE A C   1 
ATOM   3021  O  O   . PHE A 1 435 ? 19.863  -15.377 18.828  1.00 11.07 ? 427  PHE A O   1 
ATOM   3022  C  CB  . PHE A 1 435 ? 18.632  -17.831 20.723  1.00 11.33 ? 427  PHE A CB  1 
ATOM   3023  C  CG  . PHE A 1 435 ? 19.997  -18.349 20.310  1.00 11.94 ? 427  PHE A CG  1 
ATOM   3024  C  CD1 . PHE A 1 435 ? 21.163  -17.766 20.805  1.00 11.90 ? 427  PHE A CD1 1 
ATOM   3025  C  CD2 . PHE A 1 435 ? 20.107  -19.456 19.485  1.00 12.63 ? 427  PHE A CD2 1 
ATOM   3026  C  CE1 . PHE A 1 435 ? 22.423  -18.266 20.450  1.00 13.57 ? 427  PHE A CE1 1 
ATOM   3027  C  CE2 . PHE A 1 435 ? 21.365  -19.964 19.133  1.00 15.09 ? 427  PHE A CE2 1 
ATOM   3028  C  CZ  . PHE A 1 435 ? 22.517  -19.359 19.625  1.00 14.73 ? 427  PHE A CZ  1 
ATOM   3029  N  N   . GLY A 1 436 ? 19.248  -14.739 20.897  1.00 11.41 ? 428  GLY A N   1 
ATOM   3030  C  CA  . GLY A 1 436 ? 20.215  -13.660 20.935  1.00 13.77 ? 428  GLY A CA  1 
ATOM   3031  C  C   . GLY A 1 436 ? 20.607  -13.348 22.359  1.00 14.50 ? 428  GLY A C   1 
ATOM   3032  O  O   . GLY A 1 436 ? 19.738  -13.310 23.236  1.00 10.84 ? 428  GLY A O   1 
ATOM   3033  N  N   . ALA A 1 437 ? 21.895  -13.127 22.612  1.00 12.39 ? 429  ALA A N   1 
ATOM   3034  C  CA  . ALA A 1 437 ? 22.384  -13.033 23.980  1.00 12.56 ? 429  ALA A CA  1 
ATOM   3035  C  C   . ALA A 1 437 ? 23.008  -11.680 24.284  1.00 9.87  ? 429  ALA A C   1 
ATOM   3036  O  O   . ALA A 1 437 ? 23.539  -11.001 23.400  1.00 14.38 ? 429  ALA A O   1 
ATOM   3037  C  CB  . ALA A 1 437 ? 23.407  -14.122 24.278  1.00 13.81 ? 429  ALA A CB  1 
ATOM   3038  N  N   . THR A 1 438 ? 22.916  -11.301 25.558  1.00 9.96  ? 430  THR A N   1 
ATOM   3039  C  CA  . THR A 1 438 ? 23.703  -10.219 26.122  1.00 12.67 ? 430  THR A CA  1 
ATOM   3040  C  C   . THR A 1 438 ? 23.863  -10.523 27.605  1.00 10.70 ? 430  THR A C   1 
ATOM   3041  O  O   . THR A 1 438 ? 23.412  -11.561 28.087  1.00 13.55 ? 430  THR A O   1 
ATOM   3042  C  CB  . THR A 1 438 ? 23.057  -8.852  25.867  1.00 10.21 ? 430  THR A CB  1 
ATOM   3043  O  OG1 . THR A 1 438 ? 23.868  -7.819  26.426  1.00 11.51 ? 430  THR A OG1 1 
ATOM   3044  C  CG2 . THR A 1 438 ? 21.652  -8.788  26.468  1.00 13.02 ? 430  THR A CG2 1 
ATOM   3045  N  N   . PHE A 1 439 ? 24.571  -9.648  28.321  1.00 10.96 ? 431  PHE A N   1 
ATOM   3046  C  CA  . PHE A 1 439 ? 24.610  -9.777  29.774  1.00 13.64 ? 431  PHE A CA  1 
ATOM   3047  C  C   . PHE A 1 439 ? 23.215  -9.553  30.349  1.00 11.58 ? 431  PHE A C   1 
ATOM   3048  O  O   . PHE A 1 439 ? 22.436  -8.740  29.846  1.00 8.60  ? 431  PHE A O   1 
ATOM   3049  C  CB  . PHE A 1 439 ? 25.561  -8.754  30.394  1.00 9.60  ? 431  PHE A CB  1 
ATOM   3050  C  CG  . PHE A 1 439 ? 27.011  -8.967  30.075  1.00 13.90 ? 431  PHE A CG  1 
ATOM   3051  C  CD1 . PHE A 1 439 ? 27.526  -10.231 29.870  1.00 16.79 ? 431  PHE A CD1 1 
ATOM   3052  C  CD2 . PHE A 1 439 ? 27.872  -7.879  30.018  1.00 19.09 ? 431  PHE A CD2 1 
ATOM   3053  C  CE1 . PHE A 1 439 ? 28.876  -10.410 29.602  1.00 17.17 ? 431  PHE A CE1 1 
ATOM   3054  C  CE2 . PHE A 1 439 ? 29.226  -8.049  29.754  1.00 22.24 ? 431  PHE A CE2 1 
ATOM   3055  C  CZ  . PHE A 1 439 ? 29.724  -9.316  29.548  1.00 21.07 ? 431  PHE A CZ  1 
ATOM   3056  N  N   . LEU A 1 440 ? 22.905  -10.269 31.431  1.00 8.98  ? 432  LEU A N   1 
ATOM   3057  C  CA  . LEU A 1 440 ? 21.591  -10.117 32.045  1.00 9.05  ? 432  LEU A CA  1 
ATOM   3058  C  C   . LEU A 1 440 ? 21.275  -8.656  32.374  1.00 10.14 ? 432  LEU A C   1 
ATOM   3059  O  O   . LEU A 1 440 ? 20.122  -8.230  32.261  1.00 10.21 ? 432  LEU A O   1 
ATOM   3060  C  CB  . LEU A 1 440 ? 21.496  -10.969 33.315  1.00 8.78  ? 432  LEU A CB  1 
ATOM   3061  C  CG  . LEU A 1 440 ? 20.152  -10.822 34.043  1.00 8.79  ? 432  LEU A CG  1 
ATOM   3062  C  CD1 . LEU A 1 440 ? 18.965  -11.198 33.136  1.00 9.07  ? 432  LEU A CD1 1 
ATOM   3063  C  CD2 . LEU A 1 440 ? 20.151  -11.664 35.327  1.00 10.60 ? 432  LEU A CD2 1 
ATOM   3064  N  N   . MET A 1 441 ? 22.272  -7.879  32.804  1.00 10.87 ? 433  MET A N   1 
ATOM   3065  C  CA  . MET A 1 441 ? 21.983  -6.477  33.115  1.00 8.73  ? 433  MET A CA  1 
ATOM   3066  C  C   . MET A 1 441 ? 21.354  -5.774  31.922  1.00 10.99 ? 433  MET A C   1 
ATOM   3067  O  O   . MET A 1 441 ? 20.426  -4.974  32.081  1.00 9.34  ? 433  MET A O   1 
ATOM   3068  C  CB  . MET A 1 441 ? 23.247  -5.730  33.547  1.00 8.46  ? 433  MET A CB  1 
ATOM   3069  C  CG  . MET A 1 441 ? 22.963  -4.269  33.933  1.00 9.10  ? 433  MET A CG  1 
ATOM   3070  S  SD  . MET A 1 441 ? 21.867  -4.134  35.379  1.00 11.91 ? 433  MET A SD  1 
ATOM   3071  C  CE  . MET A 1 441 ? 22.975  -4.893  36.568  1.00 8.76  ? 433  MET A CE  1 
ATOM   3072  N  N   . PHE A 1 442 ? 21.809  -6.088  30.711  1.00 10.44 ? 434  PHE A N   1 
ATOM   3073  C  CA  . PHE A 1 442 ? 21.369  -5.321  29.556  1.00 11.16 ? 434  PHE A CA  1 
ATOM   3074  C  C   . PHE A 1 442 ? 20.105  -5.870  28.933  1.00 9.54  ? 434  PHE A C   1 
ATOM   3075  O  O   . PHE A 1 442 ? 19.660  -5.350  27.902  1.00 12.14 ? 434  PHE A O   1 
ATOM   3076  C  CB  . PHE A 1 442 ? 22.528  -5.206  28.571  1.00 12.38 ? 434  PHE A CB  1 
ATOM   3077  C  CG  . PHE A 1 442 ? 23.739  -4.636  29.233  1.00 20.54 ? 434  PHE A CG  1 
ATOM   3078  C  CD1 . PHE A 1 442 ? 23.586  -3.608  30.162  1.00 19.22 ? 434  PHE A CD1 1 
ATOM   3079  C  CD2 . PHE A 1 442 ? 24.990  -5.155  29.019  1.00 22.42 ? 434  PHE A CD2 1 
ATOM   3080  C  CE1 . PHE A 1 442 ? 24.669  -3.082  30.823  1.00 23.56 ? 434  PHE A CE1 1 
ATOM   3081  C  CE2 . PHE A 1 442 ? 26.085  -4.626  29.685  1.00 25.89 ? 434  PHE A CE2 1 
ATOM   3082  C  CZ  . PHE A 1 442 ? 25.918  -3.599  30.589  1.00 25.84 ? 434  PHE A CZ  1 
ATOM   3083  N  N   . SER A 1 443 ? 19.467  -6.848  29.585  1.00 9.03  ? 435  SER A N   1 
ATOM   3084  C  CA  . SER A 1 443 ? 18.034  -7.019  29.390  1.00 9.54  ? 435  SER A CA  1 
ATOM   3085  C  C   . SER A 1 443 ? 17.315  -5.684  29.532  1.00 8.67  ? 435  SER A C   1 
ATOM   3086  O  O   . SER A 1 443 ? 16.302  -5.448  28.867  1.00 11.94 ? 435  SER A O   1 
ATOM   3087  C  CB  . SER A 1 443 ? 17.469  -8.039  30.388  1.00 8.87  ? 435  SER A CB  1 
ATOM   3088  O  OG  . SER A 1 443 ? 17.505  -7.539  31.728  1.00 12.78 ? 435  SER A OG  1 
ATOM   3089  N  N   . GLU A 1 444 ? 17.842  -4.781  30.364  1.00 11.48 ? 436  GLU A N   1 
ATOM   3090  C  CA  . GLU A 1 444 ? 17.167  -3.499  30.560  1.00 12.06 ? 436  GLU A CA  1 
ATOM   3091  C  C   . GLU A 1 444 ? 17.241  -2.614  29.324  1.00 13.00 ? 436  GLU A C   1 
ATOM   3092  O  O   . GLU A 1 444 ? 16.350  -1.786  29.116  1.00 12.89 ? 436  GLU A O   1 
ATOM   3093  C  CB  . GLU A 1 444 ? 17.750  -2.777  31.768  1.00 9.80  ? 436  GLU A CB  1 
ATOM   3094  C  CG  . GLU A 1 444 ? 17.440  -3.581  33.035  1.00 9.75  ? 436  GLU A CG  1 
ATOM   3095  C  CD  . GLU A 1 444 ? 17.662  -2.826  34.318  1.00 12.81 ? 436  GLU A CD  1 
ATOM   3096  O  OE1 . GLU A 1 444 ? 18.305  -1.747  34.314  1.00 11.41 ? 436  GLU A OE1 1 
ATOM   3097  O  OE2 . GLU A 1 444 ? 17.172  -3.343  35.341  1.00 13.24 ? 436  GLU A OE2 1 
ATOM   3098  N  N   . TYR A 1 445 ? 18.276  -2.780  28.496  1.00 11.69 ? 437  TYR A N   1 
ATOM   3099  C  CA  . TYR A 1 445 ? 18.352  -2.020  27.251  1.00 9.96  ? 437  TYR A CA  1 
ATOM   3100  C  C   . TYR A 1 445 ? 17.334  -2.496  26.217  1.00 10.12 ? 437  TYR A C   1 
ATOM   3101  O  O   . TYR A 1 445 ? 16.960  -1.725  25.325  1.00 16.25 ? 437  TYR A O   1 
ATOM   3102  C  CB  . TYR A 1 445 ? 19.755  -2.120  26.650  1.00 10.20 ? 437  TYR A CB  1 
ATOM   3103  C  CG  . TYR A 1 445 ? 20.772  -1.142  27.206  1.00 13.53 ? 437  TYR A CG  1 
ATOM   3104  C  CD1 . TYR A 1 445 ? 20.972  -0.999  28.581  1.00 13.55 ? 437  TYR A CD1 1 
ATOM   3105  C  CD2 . TYR A 1 445 ? 21.553  -0.384  26.352  1.00 9.97  ? 437  TYR A CD2 1 
ATOM   3106  C  CE1 . TYR A 1 445 ? 21.937  -0.101  29.085  1.00 8.30  ? 437  TYR A CE1 1 
ATOM   3107  C  CE2 . TYR A 1 445 ? 22.516  0.491   26.836  1.00 12.44 ? 437  TYR A CE2 1 
ATOM   3108  C  CZ  . TYR A 1 445 ? 22.702  0.634   28.196  1.00 12.94 ? 437  TYR A CZ  1 
ATOM   3109  O  OH  . TYR A 1 445 ? 23.669  1.514   28.654  1.00 11.18 ? 437  TYR A OH  1 
ATOM   3110  N  N   . GLU A 1 446 ? 16.923  -3.762  26.270  1.00 9.82  ? 438  GLU A N   1 
ATOM   3111  C  CA  . GLU A 1 446 ? 15.988  -4.309  25.289  1.00 13.99 ? 438  GLU A CA  1 
ATOM   3112  C  C   . GLU A 1 446 ? 14.654  -4.677  25.925  1.00 9.68  ? 438  GLU A C   1 
ATOM   3113  O  O   . GLU A 1 446 ? 13.892  -5.469  25.361  1.00 10.12 ? 438  GLU A O   1 
ATOM   3114  C  CB  . GLU A 1 446 ? 16.587  -5.530  24.582  1.00 16.29 ? 438  GLU A CB  1 
ATOM   3115  C  CG  . GLU A 1 446 ? 16.978  -6.654  25.533  1.00 10.22 ? 438  GLU A CG  1 
ATOM   3116  C  CD  . GLU A 1 446 ? 17.377  -7.959  24.841  1.00 15.09 ? 438  GLU A CD  1 
ATOM   3117  O  OE1 . GLU A 1 446 ? 17.062  -8.159  23.645  1.00 12.75 ? 438  GLU A OE1 1 
ATOM   3118  O  OE2 . GLU A 1 446 ? 18.022  -8.798  25.511  1.00 13.94 ? 438  GLU A OE2 1 
ATOM   3119  N  N   . ARG A 1 447 ? 14.343  -4.082  27.074  1.00 9.85  ? 439  ARG A N   1 
ATOM   3120  C  CA  . ARG A 1 447 ? 13.264  -4.602  27.906  1.00 11.01 ? 439  ARG A CA  1 
ATOM   3121  C  C   . ARG A 1 447 ? 11.923  -4.632  27.176  1.00 11.15 ? 439  ARG A C   1 
ATOM   3122  O  O   . ARG A 1 447 ? 11.182  -5.621  27.270  1.00 8.75  ? 439  ARG A O   1 
ATOM   3123  C  CB  . ARG A 1 447 ? 13.166  -3.769  29.189  1.00 7.19  ? 439  ARG A CB  1 
ATOM   3124  C  CG  . ARG A 1 447 ? 11.998  -4.162  30.093  1.00 9.60  ? 439  ARG A CG  1 
ATOM   3125  C  CD  . ARG A 1 447 ? 12.132  -5.585  30.595  1.00 12.89 ? 439  ARG A CD  1 
ATOM   3126  N  NE  . ARG A 1 447 ? 10.995  -5.916  31.440  1.00 13.91 ? 439  ARG A NE  1 
ATOM   3127  C  CZ  . ARG A 1 447 ? 11.074  -6.435  32.654  1.00 13.30 ? 439  ARG A CZ  1 
ATOM   3128  N  NH1 . ARG A 1 447 ? 12.260  -6.764  33.169  1.00 10.14 ? 439  ARG A NH1 1 
ATOM   3129  N  NH2 . ARG A 1 447 ? 9.950   -6.658  33.332  1.00 7.78  ? 439  ARG A NH2 1 
ATOM   3130  N  N   . ASN A 1 448 ? 11.569  -3.559  26.460  1.00 8.95  ? 440  ASN A N   1 
ATOM   3131  C  CA  . ASN A 1 448 ? 10.212  -3.549  25.909  1.00 8.61  ? 440  ASN A CA  1 
ATOM   3132  C  C   . ASN A 1 448 ? 10.088  -4.498  24.722  1.00 13.60 ? 440  ASN A C   1 
ATOM   3133  O  O   . ASN A 1 448 ? 8.979   -4.959  24.416  1.00 10.78 ? 440  ASN A O   1 
ATOM   3134  C  CB  . ASN A 1 448 ? 9.786   -2.125  25.535  1.00 8.72  ? 440  ASN A CB  1 
ATOM   3135  C  CG  . ASN A 1 448 ? 8.267   -2.000  25.309  1.00 9.72  ? 440  ASN A CG  1 
ATOM   3136  O  OD1 . ASN A 1 448 ? 7.804   -1.855  24.178  1.00 11.24 ? 440  ASN A OD1 1 
ATOM   3137  N  ND2 . ASN A 1 448 ? 7.492   -2.087  26.395  1.00 13.64 ? 440  ASN A ND2 1 
ATOM   3138  N  N   . ALA A 1 449 ? 11.207  -4.842  24.079  1.00 10.51 ? 441  ALA A N   1 
ATOM   3139  C  CA  . ALA A 1 449 ? 11.163  -5.857  23.028  1.00 10.28 ? 441  ALA A CA  1 
ATOM   3140  C  C   . ALA A 1 449 ? 10.823  -7.222  23.609  1.00 8.16  ? 441  ALA A C   1 
ATOM   3141  O  O   . ALA A 1 449 ? 10.098  -8.006  22.987  1.00 10.08 ? 441  ALA A O   1 
ATOM   3142  C  CB  . ALA A 1 449 ? 12.503  -5.908  22.287  1.00 10.84 ? 441  ALA A CB  1 
ATOM   3143  N  N   . LEU A 1 450 ? 11.387  -7.540  24.776  1.00 7.69  ? 442  LEU A N   1 
ATOM   3144  C  CA  . LEU A 1 450 ? 11.007  -8.750  25.501  1.00 8.25  ? 442  LEU A CA  1 
ATOM   3145  C  C   . LEU A 1 450 ? 9.512   -8.768  25.775  1.00 7.94  ? 442  LEU A C   1 
ATOM   3146  O  O   . LEU A 1 450 ? 8.833   -9.772  25.538  1.00 10.14 ? 442  LEU A O   1 
ATOM   3147  C  CB  . LEU A 1 450 ? 11.778  -8.830  26.819  1.00 10.96 ? 442  LEU A CB  1 
ATOM   3148  C  CG  . LEU A 1 450 ? 13.178  -9.443  26.905  1.00 21.60 ? 442  LEU A CG  1 
ATOM   3149  C  CD1 . LEU A 1 450 ? 14.030  -8.993  25.783  1.00 17.34 ? 442  LEU A CD1 1 
ATOM   3150  C  CD2 . LEU A 1 450 ? 13.821  -9.047  28.225  1.00 18.12 ? 442  LEU A CD2 1 
ATOM   3151  N  N   . ARG A 1 451 ? 8.983   -7.648  26.269  1.00 10.55 ? 443  ARG A N   1 
ATOM   3152  C  CA  . ARG A 1 451 ? 7.556   -7.573  26.576  1.00 8.77  ? 443  ARG A CA  1 
ATOM   3153  C  C   . ARG A 1 451 ? 6.709   -7.700  25.318  1.00 10.08 ? 443  ARG A C   1 
ATOM   3154  O  O   . ARG A 1 451 ? 5.654   -8.348  25.330  1.00 12.19 ? 443  ARG A O   1 
ATOM   3155  C  CB  . ARG A 1 451 ? 7.248   -6.257  27.287  1.00 11.66 ? 443  ARG A CB  1 
ATOM   3156  C  CG  . ARG A 1 451 ? 5.842   -6.194  27.849  1.00 10.69 ? 443  ARG A CG  1 
ATOM   3157  C  CD  . ARG A 1 451 ? 5.567   -4.842  28.488  1.00 11.04 ? 443  ARG A CD  1 
ATOM   3158  N  NE  . ARG A 1 451 ? 4.417   -4.951  29.367  1.00 13.76 ? 443  ARG A NE  1 
ATOM   3159  C  CZ  . ARG A 1 451 ? 3.163   -4.702  29.008  1.00 14.82 ? 443  ARG A CZ  1 
ATOM   3160  N  NH1 . ARG A 1 451 ? 2.874   -4.291  27.779  1.00 10.37 ? 443  ARG A NH1 1 
ATOM   3161  N  NH2 . ARG A 1 451 ? 2.193   -4.842  29.899  1.00 12.69 ? 443  ARG A NH2 1 
ATOM   3162  N  N   . MET A 1 452 ? 7.148   -7.086  24.226  1.00 8.39  ? 444  MET A N   1 
ATOM   3163  C  CA  . MET A 1 452 ? 6.372   -7.152  22.990  1.00 9.87  ? 444  MET A CA  1 
ATOM   3164  C  C   . MET A 1 452 ? 6.353   -8.565  22.419  1.00 10.00 ? 444  MET A C   1 
ATOM   3165  O  O   . MET A 1 452 ? 5.348   -8.990  21.852  1.00 13.43 ? 444  MET A O   1 
ATOM   3166  C  CB  . MET A 1 452 ? 6.932   -6.159  21.970  1.00 11.68 ? 444  MET A CB  1 
ATOM   3167  C  CG  . MET A 1 452 ? 6.664   -4.712  22.341  1.00 13.30 ? 444  MET A CG  1 
ATOM   3168  S  SD  . MET A 1 452 ? 4.900   -4.316  22.366  1.00 12.58 ? 444  MET A SD  1 
ATOM   3169  C  CE  . MET A 1 452 ? 4.503   -4.442  20.620  1.00 13.30 ? 444  MET A CE  1 
ATOM   3170  N  N   . ALA A 1 453 ? 7.452   -9.315  22.565  1.00 12.71 ? 445  ALA A N   1 
ATOM   3171  C  CA  . ALA A 1 453 ? 7.431   -10.722 22.173  1.00 13.07 ? 445  ALA A CA  1 
ATOM   3172  C  C   . ALA A 1 453 ? 6.379   -11.495 22.959  1.00 13.44 ? 445  ALA A C   1 
ATOM   3173  O  O   . ALA A 1 453 ? 5.645   -12.314 22.398  1.00 13.17 ? 445  ALA A O   1 
ATOM   3174  C  CB  . ALA A 1 453 ? 8.812   -11.354 22.379  1.00 12.42 ? 445  ALA A CB  1 
ATOM   3175  N  N   . ALA A 1 454 ? 6.308   -11.256 24.263  1.00 9.04  ? 446  ALA A N   1 
ATOM   3176  C  CA  . ALA A 1 454 ? 5.333   -11.942 25.101  1.00 10.44 ? 446  ALA A CA  1 
ATOM   3177  C  C   . ALA A 1 454 ? 3.905   -11.548 24.721  1.00 12.06 ? 446  ALA A C   1 
ATOM   3178  O  O   . ALA A 1 454 ? 2.998   -12.394 24.664  1.00 14.17 ? 446  ALA A O   1 
ATOM   3179  C  CB  . ALA A 1 454 ? 5.639   -11.612 26.567  1.00 10.82 ? 446  ALA A CB  1 
ATOM   3180  N  N   . LEU A 1 455 ? 3.698   -10.264 24.440  1.00 10.44 ? 447  LEU A N   1 
ATOM   3181  C  CA  . LEU A 1 455 ? 2.379   -9.778  24.038  1.00 16.33 ? 447  LEU A CA  1 
ATOM   3182  C  C   . LEU A 1 455 ? 1.958   -10.357 22.699  1.00 17.46 ? 447  LEU A C   1 
ATOM   3183  O  O   . LEU A 1 455 ? 0.777   -10.656 22.483  1.00 14.59 ? 447  LEU A O   1 
ATOM   3184  C  CB  . LEU A 1 455 ? 2.394   -8.252  23.967  1.00 12.92 ? 447  LEU A CB  1 
ATOM   3185  C  CG  . LEU A 1 455 ? 1.106   -7.540  23.550  1.00 16.25 ? 447  LEU A CG  1 
ATOM   3186  C  CD1 . LEU A 1 455 ? -0.066  -8.108  24.339  1.00 15.67 ? 447  LEU A CD1 1 
ATOM   3187  C  CD2 . LEU A 1 455 ? 1.258   -6.059  23.824  1.00 20.16 ? 447  LEU A CD2 1 
ATOM   3188  N  N   . MET A 1 456 ? 2.901   -10.488 21.772  1.00 12.23 ? 448  MET A N   1 
ATOM   3189  C  CA  . MET A 1 456 ? 2.602   -11.041 20.463  1.00 11.60 ? 448  MET A CA  1 
ATOM   3190  C  C   . MET A 1 456 ? 2.432   -12.551 20.488  1.00 14.11 ? 448  MET A C   1 
ATOM   3191  O  O   . MET A 1 456 ? 2.007   -13.123 19.474  1.00 12.20 ? 448  MET A O   1 
ATOM   3192  C  CB  . MET A 1 456 ? 3.712   -10.657 19.476  1.00 16.12 ? 448  MET A CB  1 
ATOM   3193  C  CG  . MET A 1 456 ? 3.618   -9.232  18.991  1.00 14.17 ? 448  MET A CG  1 
ATOM   3194  S  SD  . MET A 1 456 ? 4.684   -8.948  17.573  1.00 14.27 ? 448  MET A SD  1 
ATOM   3195  C  CE  . MET A 1 456 ? 6.097   -8.139  18.327  1.00 12.10 ? 448  MET A CE  1 
ATOM   3196  N  N   . LYS A 1 457 ? 2.757   -13.197 21.612  1.00 12.41 ? 449  LYS A N   1 
ATOM   3197  C  CA  . LYS A 1 457 ? 2.692   -14.657 21.733  1.00 11.13 ? 449  LYS A CA  1 
ATOM   3198  C  C   . LYS A 1 457 ? 3.583   -15.342 20.698  1.00 15.49 ? 449  LYS A C   1 
ATOM   3199  O  O   . LYS A 1 457 ? 3.181   -16.314 20.051  1.00 11.89 ? 449  LYS A O   1 
ATOM   3200  C  CB  . LYS A 1 457 ? 1.256   -15.170 21.611  1.00 17.89 ? 449  LYS A CB  1 
ATOM   3201  C  CG  . LYS A 1 457 ? 0.300   -14.668 22.654  1.00 24.42 ? 449  LYS A CG  1 
ATOM   3202  C  CD  . LYS A 1 457 ? -1.072  -15.280 22.376  1.00 35.19 ? 449  LYS A CD  1 
ATOM   3203  C  CE  . LYS A 1 457 ? -2.202  -14.398 22.838  1.00 42.55 ? 449  LYS A CE  1 
ATOM   3204  N  NZ  . LYS A 1 457 ? -3.498  -14.914 22.307  1.00 44.05 ? 449  LYS A NZ  1 
ATOM   3205  N  N   . ILE A 1 458 ? 4.796   -14.821 20.531  1.00 14.62 ? 450  ILE A N   1 
ATOM   3206  C  CA  . ILE A 1 458 ? 5.789   -15.420 19.650  1.00 16.01 ? 450  ILE A CA  1 
ATOM   3207  C  C   . ILE A 1 458 ? 6.911   -16.008 20.506  1.00 10.60 ? 450  ILE A C   1 
ATOM   3208  O  O   . ILE A 1 458 ? 6.972   -15.798 21.714  1.00 10.77 ? 450  ILE A O   1 
ATOM   3209  C  CB  . ILE A 1 458 ? 6.327   -14.408 18.630  1.00 14.89 ? 450  ILE A CB  1 
ATOM   3210  C  CG1 . ILE A 1 458 ? 6.818   -13.154 19.355  1.00 9.97  ? 450  ILE A CG1 1 
ATOM   3211  C  CG2 . ILE A 1 458 ? 5.241   -14.061 17.626  1.00 13.38 ? 450  ILE A CG2 1 
ATOM   3212  C  CD1 . ILE A 1 458 ? 7.497   -12.118 18.415  1.00 12.26 ? 450  ILE A CD1 1 
ATOM   3213  N  N   . ASN A 1 459 ? 7.810   -16.761 19.864  1.00 12.78 ? 451  ASN A N   1 
ATOM   3214  C  CA  . ASN A 1 459 ? 8.757   -17.514 20.684  1.00 12.00 ? 451  ASN A CA  1 
ATOM   3215  C  C   . ASN A 1 459 ? 10.241  -17.269 20.396  1.00 10.63 ? 451  ASN A C   1 
ATOM   3216  O  O   . ASN A 1 459 ? 10.991  -18.240 20.271  1.00 15.88 ? 451  ASN A O   1 
ATOM   3217  C  CB  . ASN A 1 459 ? 8.455   -19.021 20.557  1.00 11.50 ? 451  ASN A CB  1 
ATOM   3218  C  CG  . ASN A 1 459 ? 8.459   -19.524 19.097  1.00 15.65 ? 451  ASN A CG  1 
ATOM   3219  O  OD1 . ASN A 1 459 ? 8.673   -18.759 18.159  1.00 13.84 ? 451  ASN A OD1 1 
ATOM   3220  N  ND2 . ASN A 1 459 ? 8.233   -20.824 18.918  1.00 16.69 ? 451  ASN A ND2 1 
ATOM   3221  N  N   . PRO A 1 460 ? 10.725  -16.028 20.337  1.00 11.44 ? 452  PRO A N   1 
ATOM   3222  C  CA  . PRO A 1 460 ? 12.180  -15.823 20.359  1.00 10.79 ? 452  PRO A CA  1 
ATOM   3223  C  C   . PRO A 1 460 ? 12.735  -16.258 21.704  1.00 13.81 ? 452  PRO A C   1 
ATOM   3224  O  O   . PRO A 1 460 ? 12.030  -16.302 22.714  1.00 11.89 ? 452  PRO A O   1 
ATOM   3225  C  CB  . PRO A 1 460 ? 12.345  -14.317 20.168  1.00 10.58 ? 452  PRO A CB  1 
ATOM   3226  C  CG  . PRO A 1 460 ? 11.117  -13.748 20.809  1.00 9.35  ? 452  PRO A CG  1 
ATOM   3227  C  CD  . PRO A 1 460 ? 10.004  -14.750 20.459  1.00 10.04 ? 452  PRO A CD  1 
ATOM   3228  N  N   . VAL A 1 461 ? 14.019  -16.588 21.709  1.00 10.24 ? 453  VAL A N   1 
ATOM   3229  C  CA  . VAL A 1 461 ? 14.689  -17.031 22.924  1.00 10.14 ? 453  VAL A CA  1 
ATOM   3230  C  C   . VAL A 1 461 ? 15.723  -15.974 23.291  1.00 14.21 ? 453  VAL A C   1 
ATOM   3231  O  O   . VAL A 1 461 ? 16.712  -15.776 22.577  1.00 12.46 ? 453  VAL A O   1 
ATOM   3232  C  CB  . VAL A 1 461 ? 15.315  -18.421 22.753  1.00 13.87 ? 453  VAL A CB  1 
ATOM   3233  C  CG1 . VAL A 1 461 ? 15.992  -18.842 24.049  1.00 11.37 ? 453  VAL A CG1 1 
ATOM   3234  C  CG2 . VAL A 1 461 ? 14.233  -19.430 22.362  1.00 13.56 ? 453  VAL A CG2 1 
ATOM   3235  N  N   . PHE A 1 462 ? 15.486  -15.280 24.398  1.00 9.39  ? 454  PHE A N   1 
ATOM   3236  C  CA  . PHE A 1 462 ? 16.411  -14.270 24.898  1.00 13.90 ? 454  PHE A CA  1 
ATOM   3237  C  C   . PHE A 1 462 ? 17.389  -14.913 25.875  1.00 9.33  ? 454  PHE A C   1 
ATOM   3238  O  O   . PHE A 1 462 ? 16.978  -15.432 26.919  1.00 9.61  ? 454  PHE A O   1 
ATOM   3239  C  CB  . PHE A 1 462 ? 15.624  -13.138 25.556  1.00 11.62 ? 454  PHE A CB  1 
ATOM   3240  C  CG  . PHE A 1 462 ? 14.628  -12.506 24.628  1.00 10.48 ? 454  PHE A CG  1 
ATOM   3241  C  CD1 . PHE A 1 462 ? 15.050  -11.609 23.657  1.00 13.27 ? 454  PHE A CD1 1 
ATOM   3242  C  CD2 . PHE A 1 462 ? 13.273  -12.819 24.712  1.00 10.20 ? 454  PHE A CD2 1 
ATOM   3243  C  CE1 . PHE A 1 462 ? 14.148  -11.027 22.783  1.00 12.46 ? 454  PHE A CE1 1 
ATOM   3244  C  CE2 . PHE A 1 462 ? 12.361  -12.251 23.837  1.00 12.30 ? 454  PHE A CE2 1 
ATOM   3245  C  CZ  . PHE A 1 462 ? 12.806  -11.340 22.871  1.00 10.78 ? 454  PHE A CZ  1 
ATOM   3246  N  N   . VAL A 1 463 ? 18.684  -14.864 25.543  1.00 9.55  ? 455  VAL A N   1 
ATOM   3247  C  CA  . VAL A 1 463 ? 19.731  -15.497 26.339  1.00 10.69 ? 455  VAL A CA  1 
ATOM   3248  C  C   . VAL A 1 463 ? 20.461  -14.424 27.134  1.00 12.18 ? 455  VAL A C   1 
ATOM   3249  O  O   . VAL A 1 463 ? 20.779  -13.355 26.601  1.00 10.17 ? 455  VAL A O   1 
ATOM   3250  C  CB  . VAL A 1 463 ? 20.720  -16.273 25.443  1.00 10.49 ? 455  VAL A CB  1 
ATOM   3251  C  CG1 . VAL A 1 463 ? 21.841  -16.889 26.282  1.00 11.70 ? 455  VAL A CG1 1 
ATOM   3252  C  CG2 . VAL A 1 463 ? 19.987  -17.364 24.664  1.00 15.54 ? 455  VAL A CG2 1 
ATOM   3253  N  N   . PHE A 1 464 ? 20.748  -14.714 28.403  1.00 10.83 ? 456  PHE A N   1 
ATOM   3254  C  CA  . PHE A 1 464 ? 21.446  -13.784 29.274  1.00 9.54  ? 456  PHE A CA  1 
ATOM   3255  C  C   . PHE A 1 464 ? 22.524  -14.527 30.040  1.00 10.42 ? 456  PHE A C   1 
ATOM   3256  O  O   . PHE A 1 464 ? 22.265  -15.607 30.579  1.00 12.15 ? 456  PHE A O   1 
ATOM   3257  C  CB  . PHE A 1 464 ? 20.467  -13.118 30.247  1.00 10.94 ? 456  PHE A CB  1 
ATOM   3258  C  CG  . PHE A 1 464 ? 19.423  -12.304 29.552  1.00 10.59 ? 456  PHE A CG  1 
ATOM   3259  C  CD1 . PHE A 1 464 ? 19.768  -11.121 28.919  1.00 8.78  ? 456  PHE A CD1 1 
ATOM   3260  C  CD2 . PHE A 1 464 ? 18.107  -12.756 29.478  1.00 15.47 ? 456  PHE A CD2 1 
ATOM   3261  C  CE1 . PHE A 1 464 ? 18.816  -10.384 28.240  1.00 8.40  ? 456  PHE A CE1 1 
ATOM   3262  C  CE2 . PHE A 1 464 ? 17.144  -12.018 28.809  1.00 11.43 ? 456  PHE A CE2 1 
ATOM   3263  C  CZ  . PHE A 1 464 ? 17.504  -10.828 28.192  1.00 10.01 ? 456  PHE A CZ  1 
ATOM   3264  N  N   . THR A 1 465 ? 23.734  -13.966 30.080  1.00 10.66 ? 457  THR A N   1 
ATOM   3265  C  CA  . THR A 1 465 ? 24.801  -14.558 30.878  1.00 10.78 ? 457  THR A CA  1 
ATOM   3266  C  C   . THR A 1 465 ? 25.265  -13.542 31.920  1.00 12.44 ? 457  THR A C   1 
ATOM   3267  O  O   . THR A 1 465 ? 24.816  -12.395 31.940  1.00 12.40 ? 457  THR A O   1 
ATOM   3268  C  CB  . THR A 1 465 ? 25.984  -15.009 30.012  1.00 15.58 ? 457  THR A CB  1 
ATOM   3269  O  OG1 . THR A 1 465 ? 26.634  -13.853 29.468  1.00 12.71 ? 457  THR A OG1 1 
ATOM   3270  C  CG2 . THR A 1 465 ? 25.518  -15.936 28.869  1.00 12.55 ? 457  THR A CG2 1 
ATOM   3271  N  N   . HIS A 1 466 ? 26.145  -13.986 32.820  1.00 11.08 ? 458  HIS A N   1 
ATOM   3272  C  CA  . HIS A 1 466 ? 26.678  -13.126 33.885  1.00 11.75 ? 458  HIS A CA  1 
ATOM   3273  C  C   . HIS A 1 466 ? 25.533  -12.612 34.766  1.00 10.48 ? 458  HIS A C   1 
ATOM   3274  O  O   . HIS A 1 466 ? 25.192  -11.433 34.785  1.00 12.07 ? 458  HIS A O   1 
ATOM   3275  C  CB  . HIS A 1 466 ? 27.506  -11.970 33.293  1.00 11.97 ? 458  HIS A CB  1 
ATOM   3276  C  CG  . HIS A 1 466 ? 28.738  -12.420 32.559  1.00 15.04 ? 458  HIS A CG  1 
ATOM   3277  N  ND1 . HIS A 1 466 ? 28.690  -13.273 31.477  1.00 18.00 ? 458  HIS A ND1 1 
ATOM   3278  C  CD2 . HIS A 1 466 ? 30.051  -12.143 32.760  1.00 22.09 ? 458  HIS A CD2 1 
ATOM   3279  C  CE1 . HIS A 1 466 ? 29.919  -13.498 31.038  1.00 22.03 ? 458  HIS A CE1 1 
ATOM   3280  N  NE2 . HIS A 1 466 ? 30.763  -12.819 31.795  1.00 20.21 ? 458  HIS A NE2 1 
ATOM   3281  N  N   . ASP A 1 467 ? 24.936  -13.555 35.499  1.00 10.59 ? 459  ASP A N   1 
ATOM   3282  C  CA  . ASP A 1 467 ? 23.601  -13.355 36.046  1.00 10.14 ? 459  ASP A CA  1 
ATOM   3283  C  C   . ASP A 1 467 ? 23.569  -12.835 37.479  1.00 10.63 ? 459  ASP A C   1 
ATOM   3284  O  O   . ASP A 1 467 ? 22.473  -12.632 38.004  1.00 12.48 ? 459  ASP A O   1 
ATOM   3285  C  CB  . ASP A 1 467 ? 22.805  -14.668 35.990  1.00 10.51 ? 459  ASP A CB  1 
ATOM   3286  C  CG  . ASP A 1 467 ? 23.270  -15.670 37.014  1.00 14.97 ? 459  ASP A CG  1 
ATOM   3287  O  OD1 . ASP A 1 467 ? 24.496  -15.765 37.233  1.00 16.63 ? 459  ASP A OD1 1 
ATOM   3288  O  OD2 . ASP A 1 467 ? 22.410  -16.360 37.615  1.00 15.89 ? 459  ASP A OD2 1 
ATOM   3289  N  N   . SER A 1 468 ? 24.705  -12.639 38.141  1.00 11.08 ? 460  SER A N   1 
ATOM   3290  C  CA  . SER A 1 468 ? 24.655  -12.250 39.551  1.00 15.20 ? 460  SER A CA  1 
ATOM   3291  C  C   . SER A 1 468 ? 25.964  -11.568 39.933  1.00 16.31 ? 460  SER A C   1 
ATOM   3292  O  O   . SER A 1 468 ? 26.836  -11.342 39.089  1.00 10.99 ? 460  SER A O   1 
ATOM   3293  C  CB  . SER A 1 468 ? 24.377  -13.462 40.452  1.00 12.34 ? 460  SER A CB  1 
ATOM   3294  O  OG  . SER A 1 468 ? 25.551  -14.254 40.642  1.00 11.61 ? 460  SER A OG  1 
ATOM   3295  N  N   . ILE A 1 469 ? 26.108  -11.251 41.227  1.00 11.00 ? 461  ILE A N   1 
ATOM   3296  C  CA  . ILE A 1 469 ? 27.393  -10.787 41.748  1.00 11.46 ? 461  ILE A CA  1 
ATOM   3297  C  C   . ILE A 1 469 ? 28.489  -11.806 41.468  1.00 14.65 ? 461  ILE A C   1 
ATOM   3298  O  O   . ILE A 1 469 ? 29.679  -11.473 41.511  1.00 13.10 ? 461  ILE A O   1 
ATOM   3299  C  CB  . ILE A 1 469 ? 27.287  -10.491 43.260  1.00 12.92 ? 461  ILE A CB  1 
ATOM   3300  C  CG1 . ILE A 1 469 ? 26.622  -11.668 43.981  1.00 11.81 ? 461  ILE A CG1 1 
ATOM   3301  C  CG2 . ILE A 1 469 ? 26.517  -9.195  43.481  1.00 11.33 ? 461  ILE A CG2 1 
ATOM   3302  C  CD1 . ILE A 1 469 ? 26.747  -11.623 45.526  1.00 14.78 ? 461  ILE A CD1 1 
ATOM   3303  N  N   . GLY A 1 470 ? 28.111  -13.045 41.143  1.00 15.37 ? 462  GLY A N   1 
ATOM   3304  C  CA  . GLY A 1 470 ? 29.080  -14.050 40.755  1.00 18.23 ? 462  GLY A CA  1 
ATOM   3305  C  C   . GLY A 1 470 ? 29.924  -13.675 39.553  1.00 13.10 ? 462  GLY A C   1 
ATOM   3306  O  O   . GLY A 1 470 ? 30.951  -14.321 39.309  1.00 14.27 ? 462  GLY A O   1 
ATOM   3307  N  N   . LEU A 1 471 ? 29.527  -12.647 38.793  1.00 12.50 ? 463  LEU A N   1 
ATOM   3308  C  CA  . LEU A 1 471 ? 30.391  -12.206 37.704  1.00 15.40 ? 463  LEU A CA  1 
ATOM   3309  C  C   . LEU A 1 471 ? 31.645  -11.496 38.224  1.00 14.41 ? 463  LEU A C   1 
ATOM   3310  O  O   . LEU A 1 471 ? 32.644  -11.413 37.504  1.00 13.70 ? 463  LEU A O   1 
ATOM   3311  C  CB  . LEU A 1 471 ? 29.606  -11.326 36.712  1.00 11.98 ? 463  LEU A CB  1 
ATOM   3312  C  CG  . LEU A 1 471 ? 29.096  -9.915  37.061  1.00 11.43 ? 463  LEU A CG  1 
ATOM   3313  C  CD1 . LEU A 1 471 ? 30.247  -8.902  37.022  1.00 11.78 ? 463  LEU A CD1 1 
ATOM   3314  C  CD2 . LEU A 1 471 ? 27.969  -9.471  36.125  1.00 10.76 ? 463  LEU A CD2 1 
ATOM   3315  N  N   . GLY A 1 472 ? 31.621  -10.981 39.445  1.00 13.18 ? 464  GLY A N   1 
ATOM   3316  C  CA  . GLY A 1 472 ? 32.842  -10.515 40.088  1.00 13.83 ? 464  GLY A CA  1 
ATOM   3317  C  C   . GLY A 1 472 ? 33.192  -9.065  39.763  1.00 14.03 ? 464  GLY A C   1 
ATOM   3318  O  O   . GLY A 1 472 ? 32.371  -8.165  39.938  1.00 13.05 ? 464  GLY A O   1 
ATOM   3319  N  N   . GLU A 1 473 ? 34.427  -8.853  39.289  1.00 14.34 ? 465  GLU A N   1 
ATOM   3320  C  CA  . GLU A 1 473 ? 35.101  -7.562  39.390  1.00 14.56 ? 465  GLU A CA  1 
ATOM   3321  C  C   . GLU A 1 473 ? 34.453  -6.434  38.582  1.00 13.91 ? 465  GLU A C   1 
ATOM   3322  O  O   . GLU A 1 473 ? 34.686  -5.264  38.901  1.00 13.96 ? 465  GLU A O   1 
ATOM   3323  C  CB  . GLU A 1 473 ? 36.561  -7.726  38.966  1.00 15.54 ? 465  GLU A CB  1 
ATOM   3324  C  CG  . GLU A 1 473 ? 37.411  -8.420  40.018  1.00 16.37 ? 465  GLU A CG  1 
ATOM   3325  C  CD  . GLU A 1 473 ? 37.480  -9.939  39.884  1.00 16.73 ? 465  GLU A CD  1 
ATOM   3326  O  OE1 . GLU A 1 473 ? 36.593  -10.554 39.258  1.00 16.51 ? 465  GLU A OE1 1 
ATOM   3327  O  OE2 . GLU A 1 473 ? 38.430  -10.515 40.448  1.00 17.64 ? 465  GLU A OE2 1 
ATOM   3328  N  N   . ASP A 1 474 ? 33.691  -6.737  37.533  1.00 13.40 ? 466  ASP A N   1 
ATOM   3329  C  CA  . ASP A 1 474 ? 33.093  -5.663  36.741  1.00 14.13 ? 466  ASP A CA  1 
ATOM   3330  C  C   . ASP A 1 474 ? 32.181  -4.757  37.582  1.00 15.85 ? 466  ASP A C   1 
ATOM   3331  O  O   . ASP A 1 474 ? 31.944  -3.601  37.204  1.00 12.27 ? 466  ASP A O   1 
ATOM   3332  C  CB  . ASP A 1 474 ? 32.307  -6.245  35.557  1.00 12.43 ? 466  ASP A CB  1 
ATOM   3333  C  CG  . ASP A 1 474 ? 33.179  -6.496  34.319  1.00 20.08 ? 466  ASP A CG  1 
ATOM   3334  O  OD1 . ASP A 1 474 ? 34.375  -6.122  34.310  1.00 16.46 ? 466  ASP A OD1 1 
ATOM   3335  O  OD2 . ASP A 1 474 ? 32.651  -7.080  33.343  1.00 18.05 ? 466  ASP A OD2 1 
ATOM   3336  N  N   . GLY A 1 475 ? 31.664  -5.245  38.711  1.00 13.60 ? 467  GLY A N   1 
ATOM   3337  C  CA  . GLY A 1 475 ? 31.055  -4.363  39.685  1.00 11.88 ? 467  GLY A CA  1 
ATOM   3338  C  C   . GLY A 1 475 ? 29.580  -4.063  39.477  1.00 11.12 ? 467  GLY A C   1 
ATOM   3339  O  O   . GLY A 1 475 ? 28.907  -4.627  38.601  1.00 10.75 ? 467  GLY A O   1 
ATOM   3340  N  N   . PRO A 1 476 ? 29.052  -3.151  40.306  1.00 10.96 ? 468  PRO A N   1 
ATOM   3341  C  CA  . PRO A 1 476 ? 27.588  -3.014  40.429  1.00 10.36 ? 468  PRO A CA  1 
ATOM   3342  C  C   . PRO A 1 476 ? 26.879  -2.500  39.177  1.00 9.94  ? 468  PRO A C   1 
ATOM   3343  O  O   . PRO A 1 476 ? 25.671  -2.716  39.074  1.00 12.01 ? 468  PRO A O   1 
ATOM   3344  C  CB  . PRO A 1 476 ? 27.426  -2.037  41.611  1.00 10.48 ? 468  PRO A CB  1 
ATOM   3345  C  CG  . PRO A 1 476 ? 28.734  -1.235  41.623  1.00 11.03 ? 468  PRO A CG  1 
ATOM   3346  C  CD  . PRO A 1 476 ? 29.784  -2.263  41.232  1.00 11.41 ? 468  PRO A CD  1 
ATOM   3347  N  N   . THR A 1 477 ? 27.560  -1.846  38.221  1.00 10.24 ? 469  THR A N   1 
ATOM   3348  C  CA  . THR A 1 477 ? 26.843  -1.465  37.001  1.00 12.02 ? 469  THR A CA  1 
ATOM   3349  C  C   . THR A 1 477 ? 26.470  -2.678  36.160  1.00 16.18 ? 469  THR A C   1 
ATOM   3350  O  O   . THR A 1 477 ? 25.525  -2.599  35.361  1.00 12.41 ? 469  THR A O   1 
ATOM   3351  C  CB  . THR A 1 477 ? 27.652  -0.510  36.116  1.00 10.95 ? 469  THR A CB  1 
ATOM   3352  O  OG1 . THR A 1 477 ? 28.825  -1.172  35.629  1.00 13.17 ? 469  THR A OG1 1 
ATOM   3353  C  CG2 . THR A 1 477 ? 28.027  0.769   36.856  1.00 13.55 ? 469  THR A CG2 1 
ATOM   3354  N  N   . HIS A 1 478 ? 27.193  -3.788  36.322  1.00 11.67 ? 470  HIS A N   1 
ATOM   3355  C  CA  . HIS A 1 478 ? 26.971  -5.001  35.547  1.00 10.60 ? 470  HIS A CA  1 
ATOM   3356  C  C   . HIS A 1 478 ? 26.328  -6.131  36.329  1.00 11.85 ? 470  HIS A C   1 
ATOM   3357  O  O   . HIS A 1 478 ? 25.687  -6.986  35.719  1.00 12.38 ? 470  HIS A O   1 
ATOM   3358  C  CB  . HIS A 1 478 ? 28.297  -5.507  34.959  1.00 10.31 ? 470  HIS A CB  1 
ATOM   3359  C  CG  . HIS A 1 478 ? 28.739  -4.738  33.752  1.00 24.38 ? 470  HIS A CG  1 
ATOM   3360  N  ND1 . HIS A 1 478 ? 28.817  -3.362  33.735  1.00 25.86 ? 470  HIS A ND1 1 
ATOM   3361  C  CD2 . HIS A 1 478 ? 29.096  -5.150  32.510  1.00 26.38 ? 470  HIS A CD2 1 
ATOM   3362  C  CE1 . HIS A 1 478 ? 29.211  -2.959  32.539  1.00 29.43 ? 470  HIS A CE1 1 
ATOM   3363  N  NE2 . HIS A 1 478 ? 29.387  -4.024  31.777  1.00 26.69 ? 470  HIS A NE2 1 
ATOM   3364  N  N   . GLN A 1 479 ? 26.506  -6.170  37.651  1.00 10.65 ? 471  GLN A N   1 
ATOM   3365  C  CA  . GLN A 1 479 ? 26.018  -7.257  38.496  1.00 9.83  ? 471  GLN A CA  1 
ATOM   3366  C  C   . GLN A 1 479 ? 24.499  -7.210  38.660  1.00 11.47 ? 471  GLN A C   1 
ATOM   3367  O  O   . GLN A 1 479 ? 23.983  -6.294  39.325  1.00 9.83  ? 471  GLN A O   1 
ATOM   3368  C  CB  . GLN A 1 479 ? 26.693  -7.199  39.873  1.00 10.23 ? 471  GLN A CB  1 
ATOM   3369  C  CG  . GLN A 1 479 ? 28.181  -7.556  39.830  1.00 10.87 ? 471  GLN A CG  1 
ATOM   3370  C  CD  . GLN A 1 479 ? 28.913  -7.025  41.029  1.00 14.11 ? 471  GLN A CD  1 
ATOM   3371  O  OE1 . GLN A 1 479 ? 28.391  -6.175  41.749  1.00 11.06 ? 471  GLN A OE1 1 
ATOM   3372  N  NE2 . GLN A 1 479 ? 30.124  -7.524  41.261  1.00 11.94 ? 471  GLN A NE2 1 
ATOM   3373  N  N   . PRO A 1 480 ? 23.756  -8.151  38.088  1.00 12.47 ? 472  PRO A N   1 
ATOM   3374  C  CA  . PRO A 1 480 ? 22.301  -8.147  38.277  1.00 8.82  ? 472  PRO A CA  1 
ATOM   3375  C  C   . PRO A 1 480 ? 21.943  -8.325  39.741  1.00 10.24 ? 472  PRO A C   1 
ATOM   3376  O  O   . PRO A 1 480 ? 22.640  -9.014  40.491  1.00 12.05 ? 472  PRO A O   1 
ATOM   3377  C  CB  . PRO A 1 480 ? 21.830  -9.340  37.440  1.00 10.13 ? 472  PRO A CB  1 
ATOM   3378  C  CG  . PRO A 1 480 ? 22.900  -9.476  36.376  1.00 9.00  ? 472  PRO A CG  1 
ATOM   3379  C  CD  . PRO A 1 480 ? 24.179  -9.218  37.161  1.00 10.28 ? 472  PRO A CD  1 
ATOM   3380  N  N   . ILE A 1 481 ? 20.862  -7.654  40.147  1.00 8.71  ? 473  ILE A N   1 
ATOM   3381  C  CA  . ILE A 1 481 ? 20.298  -7.793  41.485  1.00 13.03 ? 473  ILE A CA  1 
ATOM   3382  C  C   . ILE A 1 481 ? 18.819  -8.089  41.308  1.00 10.83 ? 473  ILE A C   1 
ATOM   3383  O  O   . ILE A 1 481 ? 18.315  -9.138  41.726  1.00 9.90  ? 473  ILE A O   1 
ATOM   3384  C  CB  . ILE A 1 481 ? 20.509  -6.522  42.334  1.00 10.33 ? 473  ILE A CB  1 
ATOM   3385  C  CG1 . ILE A 1 481 ? 22.004  -6.228  42.511  1.00 9.19  ? 473  ILE A CG1 1 
ATOM   3386  C  CG2 . ILE A 1 481 ? 19.814  -6.654  43.732  1.00 9.97  ? 473  ILE A CG2 1 
ATOM   3387  C  CD1 . ILE A 1 481 ? 22.717  -7.255  43.359  1.00 9.64  ? 473  ILE A CD1 1 
ATOM   3388  N  N   . GLU A 1 482 ? 18.122  -7.173  40.651  1.00 11.90 ? 474  GLU A N   1 
ATOM   3389  C  CA  . GLU A 1 482 ? 16.674  -7.241  40.525  1.00 11.12 ? 474  GLU A CA  1 
ATOM   3390  C  C   . GLU A 1 482 ? 16.210  -7.734  39.161  1.00 10.81 ? 474  GLU A C   1 
ATOM   3391  O  O   . GLU A 1 482 ? 15.000  -7.913  38.964  1.00 9.64  ? 474  GLU A O   1 
ATOM   3392  C  CB  . GLU A 1 482 ? 16.063  -5.852  40.799  1.00 8.37  ? 474  GLU A CB  1 
ATOM   3393  C  CG  . GLU A 1 482 ? 16.332  -4.788  39.705  1.00 7.93  ? 474  GLU A CG  1 
ATOM   3394  C  CD  . GLU A 1 482 ? 17.698  -4.092  39.820  1.00 14.46 ? 474  GLU A CD  1 
ATOM   3395  O  OE1 . GLU A 1 482 ? 18.698  -4.742  40.215  1.00 12.48 ? 474  GLU A OE1 1 
ATOM   3396  O  OE2 . GLU A 1 482 ? 17.773  -2.885  39.480  1.00 13.43 ? 474  GLU A OE2 1 
ATOM   3397  N  N   . GLN A 1 483 ? 17.123  -7.952  38.212  1.00 9.59  ? 475  GLN A N   1 
ATOM   3398  C  CA  . GLN A 1 483 ? 16.685  -8.168  36.831  1.00 8.94  ? 475  GLN A CA  1 
ATOM   3399  C  C   . GLN A 1 483 ? 15.878  -9.453  36.692  1.00 13.77 ? 475  GLN A C   1 
ATOM   3400  O  O   . GLN A 1 483 ? 14.797  -9.448  36.091  1.00 9.31  ? 475  GLN A O   1 
ATOM   3401  C  CB  . GLN A 1 483 ? 17.874  -8.161  35.872  1.00 8.91  ? 475  GLN A CB  1 
ATOM   3402  C  CG  . GLN A 1 483 ? 18.418  -6.748  35.591  1.00 10.62 ? 475  GLN A CG  1 
ATOM   3403  C  CD  . GLN A 1 483 ? 19.041  -6.128  36.819  1.00 10.39 ? 475  GLN A CD  1 
ATOM   3404  O  OE1 . GLN A 1 483 ? 19.643  -6.823  37.623  1.00 13.75 ? 475  GLN A OE1 1 
ATOM   3405  N  NE2 . GLN A 1 483 ? 18.859  -4.820  36.991  1.00 12.73 ? 475  GLN A NE2 1 
ATOM   3406  N  N   . THR A 1 484 ? 16.373  -10.566 37.244  1.00 9.99  ? 476  THR A N   1 
ATOM   3407  C  CA  . THR A 1 484 ? 15.617  -11.815 37.138  1.00 11.24 ? 476  THR A CA  1 
ATOM   3408  C  C   . THR A 1 484 ? 14.228  -11.680 37.754  1.00 8.75  ? 476  THR A C   1 
ATOM   3409  O  O   . THR A 1 484 ? 13.242  -12.150 37.176  1.00 11.21 ? 476  THR A O   1 
ATOM   3410  C  CB  . THR A 1 484 ? 16.380  -12.966 37.797  1.00 15.75 ? 476  THR A CB  1 
ATOM   3411  O  OG1 . THR A 1 484 ? 17.632  -13.146 37.124  1.00 11.39 ? 476  THR A OG1 1 
ATOM   3412  C  CG2 . THR A 1 484 ? 15.569  -14.258 37.708  1.00 10.53 ? 476  THR A CG2 1 
ATOM   3413  N  N   . ALA A 1 485 ? 14.128  -11.038 38.919  1.00 8.77  ? 477  ALA A N   1 
ATOM   3414  C  CA  . ALA A 1 485 ? 12.817  -10.832 39.541  1.00 10.63 ? 477  ALA A CA  1 
ATOM   3415  C  C   . ALA A 1 485 ? 11.894  -9.987  38.660  1.00 9.00  ? 477  ALA A C   1 
ATOM   3416  O  O   . ALA A 1 485 ? 10.681  -10.236 38.603  1.00 10.22 ? 477  ALA A O   1 
ATOM   3417  C  CB  . ALA A 1 485 ? 12.979  -10.175 40.911  1.00 9.86  ? 477  ALA A CB  1 
ATOM   3418  N  N   . THR A 1 486 ? 12.430  -8.965  37.997  1.00 10.23 ? 478  THR A N   1 
ATOM   3419  C  CA  . THR A 1 486 ? 11.563  -8.145  37.152  1.00 10.57 ? 478  THR A CA  1 
ATOM   3420  C  C   . THR A 1 486 ? 11.148  -8.901  35.895  1.00 12.15 ? 478  THR A C   1 
ATOM   3421  O  O   . THR A 1 486 ? 10.020  -8.736  35.412  1.00 10.20 ? 478  THR A O   1 
ATOM   3422  C  CB  . THR A 1 486 ? 12.236  -6.821  36.769  1.00 9.17  ? 478  THR A CB  1 
ATOM   3423  O  OG1 . THR A 1 486 ? 13.388  -7.074  35.958  1.00 10.01 ? 478  THR A OG1 1 
ATOM   3424  C  CG2 . THR A 1 486 ? 12.634  -6.017  38.016  1.00 10.14 ? 478  THR A CG2 1 
ATOM   3425  N  N   . LEU A 1 487 ? 12.043  -9.721  35.339  1.00 8.04  ? 479  LEU A N   1 
ATOM   3426  C  CA  . LEU A 1 487 ? 11.690  -10.473 34.132  1.00 9.07  ? 479  LEU A CA  1 
ATOM   3427  C  C   . LEU A 1 487 ? 10.560  -11.457 34.401  1.00 13.21 ? 479  LEU A C   1 
ATOM   3428  O  O   . LEU A 1 487 ? 9.758   -11.753 33.498  1.00 11.61 ? 479  LEU A O   1 
ATOM   3429  C  CB  . LEU A 1 487 ? 12.903  -11.226 33.581  1.00 9.11  ? 479  LEU A CB  1 
ATOM   3430  C  CG  . LEU A 1 487 ? 14.009  -10.343 33.002  1.00 10.86 ? 479  LEU A CG  1 
ATOM   3431  C  CD1 . LEU A 1 487 ? 15.319  -11.129 32.773  1.00 15.33 ? 479  LEU A CD1 1 
ATOM   3432  C  CD2 . LEU A 1 487 ? 13.543  -9.684  31.708  1.00 11.42 ? 479  LEU A CD2 1 
ATOM   3433  N  N   . ARG A 1 488 ? 10.485  -11.982 35.625  1.00 8.93  ? 480  ARG A N   1 
ATOM   3434  C  CA  . ARG A 1 488 ? 9.419   -12.927 35.956  1.00 10.18 ? 480  ARG A CA  1 
ATOM   3435  C  C   . ARG A 1 488 ? 8.043   -12.278 35.958  1.00 12.00 ? 480  ARG A C   1 
ATOM   3436  O  O   . ARG A 1 488 ? 7.032   -12.996 35.922  1.00 12.18 ? 480  ARG A O   1 
ATOM   3437  C  CB  . ARG A 1 488 ? 9.680   -13.555 37.327  1.00 12.68 ? 480  ARG A CB  1 
ATOM   3438  C  CG  . ARG A 1 488 ? 10.816  -14.578 37.326  1.00 9.78  ? 480  ARG A CG  1 
ATOM   3439  C  CD  . ARG A 1 488 ? 11.170  -14.966 38.766  1.00 10.07 ? 480  ARG A CD  1 
ATOM   3440  N  NE  . ARG A 1 488 ? 12.206  -15.991 38.800  1.00 10.17 ? 480  ARG A NE  1 
ATOM   3441  C  CZ  . ARG A 1 488 ? 13.211  -16.013 39.664  1.00 11.55 ? 480  ARG A CZ  1 
ATOM   3442  N  NH1 . ARG A 1 488 ? 13.334  -15.042 40.565  1.00 12.27 ? 480  ARG A NH1 1 
ATOM   3443  N  NH2 . ARG A 1 488 ? 14.113  -16.988 39.603  1.00 11.63 ? 480  ARG A NH2 1 
ATOM   3444  N  N   . LEU A 1 489 ? 7.974   -10.949 36.012  1.00 8.98  ? 481  LEU A N   1 
ATOM   3445  C  CA  . LEU A 1 489 ? 6.698   -10.261 36.067  1.00 11.42 ? 481  LEU A CA  1 
ATOM   3446  C  C   . LEU A 1 489 ? 6.122   -9.970  34.688  1.00 14.41 ? 481  LEU A C   1 
ATOM   3447  O  O   . LEU A 1 489 ? 5.005   -9.461  34.607  1.00 11.83 ? 481  LEU A O   1 
ATOM   3448  C  CB  . LEU A 1 489 ? 6.829   -8.957  36.863  1.00 10.09 ? 481  LEU A CB  1 
ATOM   3449  C  CG  . LEU A 1 489 ? 7.343   -9.135  38.291  1.00 16.66 ? 481  LEU A CG  1 
ATOM   3450  C  CD1 . LEU A 1 489 ? 7.303   -7.797  39.044  1.00 18.61 ? 481  LEU A CD1 1 
ATOM   3451  C  CD2 . LEU A 1 489 ? 6.533   -10.189 39.045  1.00 14.96 ? 481  LEU A CD2 1 
ATOM   3452  N  N   . ILE A 1 490 ? 6.844   -10.283 33.615  1.00 10.32 ? 482  ILE A N   1 
ATOM   3453  C  CA  . ILE A 1 490 ? 6.330   -10.077 32.262  1.00 10.17 ? 482  ILE A CA  1 
ATOM   3454  C  C   . ILE A 1 490 ? 5.260   -11.125 31.992  1.00 9.76  ? 482  ILE A C   1 
ATOM   3455  O  O   . ILE A 1 490 ? 5.548   -12.327 32.070  1.00 11.51 ? 482  ILE A O   1 
ATOM   3456  C  CB  . ILE A 1 490 ? 7.456   -10.166 31.217  1.00 11.55 ? 482  ILE A CB  1 
ATOM   3457  C  CG1 . ILE A 1 490 ? 8.516   -9.087  31.481  1.00 8.79  ? 482  ILE A CG1 1 
ATOM   3458  C  CG2 . ILE A 1 490 ? 6.875   -10.013 29.812  1.00 14.00 ? 482  ILE A CG2 1 
ATOM   3459  C  CD1 . ILE A 1 490 ? 9.727   -9.184  30.544  1.00 10.54 ? 482  ILE A CD1 1 
ATOM   3460  N  N   . PRO A 1 491 ? 4.029   -10.733 31.666  1.00 10.90 ? 483  PRO A N   1 
ATOM   3461  C  CA  . PRO A 1 491 ? 3.001   -11.740 31.381  1.00 14.57 ? 483  PRO A CA  1 
ATOM   3462  C  C   . PRO A 1 491 ? 3.390   -12.551 30.153  1.00 16.77 ? 483  PRO A C   1 
ATOM   3463  O  O   . PRO A 1 491 ? 3.975   -12.025 29.206  1.00 15.35 ? 483  PRO A O   1 
ATOM   3464  C  CB  . PRO A 1 491 ? 1.738   -10.902 31.132  1.00 18.50 ? 483  PRO A CB  1 
ATOM   3465  C  CG  . PRO A 1 491 ? 2.013   -9.563  31.819  1.00 17.25 ? 483  PRO A CG  1 
ATOM   3466  C  CD  . PRO A 1 491 ? 3.496   -9.359  31.614  1.00 13.18 ? 483  PRO A CD  1 
ATOM   3467  N  N   . ASN A 1 492 ? 3.084   -13.846 30.193  1.00 12.52 ? 484  ASN A N   1 
ATOM   3468  C  CA  . ASN A 1 492 ? 3.342   -14.756 29.077  1.00 14.82 ? 484  ASN A CA  1 
ATOM   3469  C  C   . ASN A 1 492 ? 4.835   -14.880 28.757  1.00 17.90 ? 484  ASN A C   1 
ATOM   3470  O  O   . ASN A 1 492 ? 5.219   -15.057 27.597  1.00 12.75 ? 484  ASN A O   1 
ATOM   3471  C  CB  . ASN A 1 492 ? 2.565   -14.331 27.825  1.00 17.44 ? 484  ASN A CB  1 
ATOM   3472  C  CG  . ASN A 1 492 ? 2.481   -15.440 26.803  1.00 18.90 ? 484  ASN A CG  1 
ATOM   3473  O  OD1 . ASN A 1 492 ? 2.235   -16.590 27.159  1.00 16.27 ? 484  ASN A OD1 1 
ATOM   3474  N  ND2 . ASN A 1 492 ? 2.724   -15.109 25.530  1.00 14.96 ? 484  ASN A ND2 1 
ATOM   3475  N  N   . MET A 1 493 ? 5.688   -14.790 29.772  1.00 13.96 ? 485  MET A N   1 
ATOM   3476  C  CA  . MET A 1 493 ? 7.126   -14.962 29.624  1.00 16.47 ? 485  MET A CA  1 
ATOM   3477  C  C   . MET A 1 493 ? 7.578   -16.063 30.570  1.00 16.05 ? 485  MET A C   1 
ATOM   3478  O  O   . MET A 1 493 ? 7.203   -16.060 31.747  1.00 14.43 ? 485  MET A O   1 
ATOM   3479  C  CB  . MET A 1 493 ? 7.880   -13.657 29.926  1.00 13.97 ? 485  MET A CB  1 
ATOM   3480  C  CG  . MET A 1 493 ? 9.416   -13.802 29.972  1.00 13.13 ? 485  MET A CG  1 
ATOM   3481  S  SD  . MET A 1 493 ? 10.128  -14.099 28.346  1.00 14.10 ? 485  MET A SD  1 
ATOM   3482  C  CE  . MET A 1 493 ? 10.252  -12.430 27.735  1.00 13.96 ? 485  MET A CE  1 
ATOM   3483  N  N   . ASP A 1 494 ? 8.370   -17.003 30.057  1.00 12.46 ? 486  ASP A N   1 
ATOM   3484  C  CA  . ASP A 1 494 ? 9.024   -18.017 30.878  1.00 14.75 ? 486  ASP A CA  1 
ATOM   3485  C  C   . ASP A 1 494 ? 10.449  -17.575 31.180  1.00 17.08 ? 486  ASP A C   1 
ATOM   3486  O  O   . ASP A 1 494 ? 11.204  -17.240 30.262  1.00 14.21 ? 486  ASP A O   1 
ATOM   3487  C  CB  . ASP A 1 494 ? 9.066   -19.375 30.175  1.00 14.00 ? 486  ASP A CB  1 
ATOM   3488  C  CG  . ASP A 1 494 ? 7.756   -20.140 30.272  1.00 14.36 ? 486  ASP A CG  1 
ATOM   3489  O  OD1 . ASP A 1 494 ? 6.822   -19.703 30.977  1.00 17.46 ? 486  ASP A OD1 1 
ATOM   3490  O  OD2 . ASP A 1 494 ? 7.680   -21.204 29.637  1.00 19.45 ? 486  ASP A OD2 1 
ATOM   3491  N  N   . VAL A 1 495 ? 10.817  -17.594 32.458  1.00 11.50 ? 487  VAL A N   1 
ATOM   3492  C  CA  . VAL A 1 495 ? 12.175  -17.281 32.898  1.00 11.23 ? 487  VAL A CA  1 
ATOM   3493  C  C   . VAL A 1 495 ? 12.792  -18.551 33.469  1.00 11.08 ? 487  VAL A C   1 
ATOM   3494  O  O   . VAL A 1 495 ? 12.257  -19.138 34.421  1.00 12.18 ? 487  VAL A O   1 
ATOM   3495  C  CB  . VAL A 1 495 ? 12.190  -16.145 33.933  1.00 13.80 ? 487  VAL A CB  1 
ATOM   3496  C  CG1 . VAL A 1 495 ? 13.603  -15.917 34.432  1.00 15.94 ? 487  VAL A CG1 1 
ATOM   3497  C  CG2 . VAL A 1 495 ? 11.611  -14.853 33.322  1.00 17.02 ? 487  VAL A CG2 1 
ATOM   3498  N  N   . TRP A 1 496 ? 13.926  -18.963 32.900  1.00 11.83 ? 488  TRP A N   1 
ATOM   3499  C  CA  . TRP A 1 496 ? 14.676  -20.138 33.335  1.00 14.82 ? 488  TRP A CA  1 
ATOM   3500  C  C   . TRP A 1 496 ? 16.029  -19.727 33.914  1.00 15.53 ? 488  TRP A C   1 
ATOM   3501  O  O   . TRP A 1 496 ? 16.739  -18.897 33.341  1.00 14.31 ? 488  TRP A O   1 
ATOM   3502  C  CB  . TRP A 1 496 ? 14.922  -21.112 32.175  1.00 12.17 ? 488  TRP A CB  1 
ATOM   3503  C  CG  . TRP A 1 496 ? 13.707  -21.815 31.673  1.00 13.84 ? 488  TRP A CG  1 
ATOM   3504  C  CD1 . TRP A 1 496 ? 12.860  -21.388 30.684  1.00 12.91 ? 488  TRP A CD1 1 
ATOM   3505  C  CD2 . TRP A 1 496 ? 13.212  -23.086 32.106  1.00 15.73 ? 488  TRP A CD2 1 
ATOM   3506  N  NE1 . TRP A 1 496 ? 11.864  -22.318 30.484  1.00 13.33 ? 488  TRP A NE1 1 
ATOM   3507  C  CE2 . TRP A 1 496 ? 12.051  -23.364 31.351  1.00 16.88 ? 488  TRP A CE2 1 
ATOM   3508  C  CE3 . TRP A 1 496 ? 13.626  -24.012 33.072  1.00 19.23 ? 488  TRP A CE3 1 
ATOM   3509  C  CZ2 . TRP A 1 496 ? 11.301  -24.529 31.528  1.00 16.16 ? 488  TRP A CZ2 1 
ATOM   3510  C  CZ3 . TRP A 1 496 ? 12.878  -25.172 33.240  1.00 19.25 ? 488  TRP A CZ3 1 
ATOM   3511  C  CH2 . TRP A 1 496 ? 11.732  -25.417 32.472  1.00 19.86 ? 488  TRP A CH2 1 
ATOM   3512  N  N   . ARG A 1 497 ? 16.385  -20.317 35.048  1.00 15.39 ? 489  ARG A N   1 
ATOM   3513  C  CA  . ARG A 1 497 ? 17.663  -20.050 35.701  1.00 10.12 ? 489  ARG A CA  1 
ATOM   3514  C  C   . ARG A 1 497 ? 18.222  -21.403 36.099  1.00 13.60 ? 489  ARG A C   1 
ATOM   3515  O  O   . ARG A 1 497 ? 18.142  -21.812 37.262  1.00 12.84 ? 489  ARG A O   1 
ATOM   3516  C  CB  . ARG A 1 497 ? 17.499  -19.108 36.901  1.00 11.11 ? 489  ARG A CB  1 
ATOM   3517  C  CG  . ARG A 1 497 ? 18.852  -18.576 37.433  1.00 13.06 ? 489  ARG A CG  1 
ATOM   3518  C  CD  . ARG A 1 497 ? 18.671  -17.576 38.583  1.00 15.77 ? 489  ARG A CD  1 
ATOM   3519  N  NE  . ARG A 1 497 ? 19.940  -16.987 39.001  1.00 15.41 ? 489  ARG A NE  1 
ATOM   3520  C  CZ  . ARG A 1 497 ? 20.560  -17.275 40.144  1.00 14.72 ? 489  ARG A CZ  1 
ATOM   3521  N  NH1 . ARG A 1 497 ? 20.029  -18.144 40.995  1.00 11.31 ? 489  ARG A NH1 1 
ATOM   3522  N  NH2 . ARG A 1 497 ? 21.715  -16.691 40.440  1.00 13.66 ? 489  ARG A NH2 1 
ATOM   3523  N  N   . PRO A 1 498 ? 18.767  -22.145 35.135  1.00 11.35 ? 490  PRO A N   1 
ATOM   3524  C  CA  . PRO A 1 498 ? 19.139  -23.540 35.386  1.00 12.64 ? 490  PRO A CA  1 
ATOM   3525  C  C   . PRO A 1 498 ? 20.374  -23.646 36.258  1.00 12.22 ? 490  PRO A C   1 
ATOM   3526  O  O   . PRO A 1 498 ? 21.277  -22.805 36.207  1.00 13.69 ? 490  PRO A O   1 
ATOM   3527  C  CB  . PRO A 1 498 ? 19.407  -24.092 33.981  1.00 17.60 ? 490  PRO A CB  1 
ATOM   3528  C  CG  . PRO A 1 498 ? 19.748  -22.885 33.157  1.00 15.35 ? 490  PRO A CG  1 
ATOM   3529  C  CD  . PRO A 1 498 ? 18.880  -21.788 33.714  1.00 11.81 ? 490  PRO A CD  1 
ATOM   3530  N  N   . CYS A 1 499 ? 20.420  -24.715 37.054  1.00 11.46 ? 491  CYS A N   1 
ATOM   3531  C  CA  . CYS A 1 499 ? 21.503  -24.865 38.019  1.00 15.44 ? 491  CYS A CA  1 
ATOM   3532  C  C   . CYS A 1 499 ? 22.677  -25.689 37.507  1.00 17.45 ? 491  CYS A C   1 
ATOM   3533  O  O   . CYS A 1 499 ? 23.728  -25.683 38.157  1.00 18.46 ? 491  CYS A O   1 
ATOM   3534  C  CB  . CYS A 1 499 ? 20.988  -25.495 39.325  1.00 17.37 ? 491  CYS A CB  1 
ATOM   3535  S  SG  . CYS A 1 499 ? 20.667  -27.290 39.280  1.00 18.13 ? 491  CYS A SG  1 
ATOM   3536  N  N   . ASP A 1 500 ? 22.532  -26.420 36.403  1.00 15.52 ? 492  ASP A N   1 
ATOM   3537  C  CA  . ASP A 1 500 ? 23.638  -27.230 35.896  1.00 14.46 ? 492  ASP A CA  1 
ATOM   3538  C  C   . ASP A 1 500 ? 23.377  -27.562 34.430  1.00 14.55 ? 492  ASP A C   1 
ATOM   3539  O  O   . ASP A 1 500 ? 22.453  -27.024 33.816  1.00 14.89 ? 492  ASP A O   1 
ATOM   3540  C  CB  . ASP A 1 500 ? 23.863  -28.483 36.754  1.00 15.33 ? 492  ASP A CB  1 
ATOM   3541  C  CG  . ASP A 1 500 ? 22.670  -29.449 36.755  1.00 20.81 ? 492  ASP A CG  1 
ATOM   3542  O  OD1 . ASP A 1 500 ? 21.823  -29.410 35.833  1.00 17.98 ? 492  ASP A OD1 1 
ATOM   3543  O  OD2 . ASP A 1 500 ? 22.597  -30.270 37.694  1.00 19.13 ? 492  ASP A OD2 1 
ATOM   3544  N  N   . THR A 1 501 ? 24.215  -28.449 33.869  1.00 17.98 ? 493  THR A N   1 
ATOM   3545  C  CA  . THR A 1 501 ? 24.135  -28.792 32.450  1.00 18.28 ? 493  THR A CA  1 
ATOM   3546  C  C   . THR A 1 501 ? 22.828  -29.487 32.104  1.00 16.32 ? 493  THR A C   1 
ATOM   3547  O  O   . THR A 1 501 ? 22.328  -29.338 30.985  1.00 18.34 ? 493  THR A O   1 
ATOM   3548  C  CB  . THR A 1 501 ? 25.296  -29.704 32.051  1.00 19.33 ? 493  THR A CB  1 
ATOM   3549  O  OG1 . THR A 1 501 ? 25.387  -30.776 33.000  1.00 21.61 ? 493  THR A OG1 1 
ATOM   3550  C  CG2 . THR A 1 501 ? 26.621  -28.932 32.004  1.00 18.27 ? 493  THR A CG2 1 
ATOM   3551  N  N   . ALA A 1 502 ? 22.279  -30.277 33.026  1.00 17.02 ? 494  ALA A N   1 
ATOM   3552  C  CA  . ALA A 1 502 ? 21.016  -30.947 32.735  1.00 19.63 ? 494  ALA A CA  1 
ATOM   3553  C  C   . ALA A 1 502 ? 19.864  -29.946 32.712  1.00 16.44 ? 494  ALA A C   1 
ATOM   3554  O  O   . ALA A 1 502 ? 19.077  -29.917 31.762  1.00 16.87 ? 494  ALA A O   1 
ATOM   3555  C  CB  . ALA A 1 502 ? 20.767  -32.072 33.746  1.00 19.44 ? 494  ALA A CB  1 
ATOM   3556  N  N   . GLU A 1 503 ? 19.752  -29.100 33.739  1.00 13.65 ? 495  GLU A N   1 
ATOM   3557  C  CA  . GLU A 1 503 ? 18.689  -28.101 33.715  1.00 15.05 ? 495  GLU A CA  1 
ATOM   3558  C  C   . GLU A 1 503 ? 18.851  -27.152 32.534  1.00 13.81 ? 495  GLU A C   1 
ATOM   3559  O  O   . GLU A 1 503 ? 17.858  -26.679 31.979  1.00 16.97 ? 495  GLU A O   1 
ATOM   3560  C  CB  . GLU A 1 503 ? 18.653  -27.323 35.036  1.00 12.01 ? 495  GLU A CB  1 
ATOM   3561  C  CG  . GLU A 1 503 ? 18.095  -28.152 36.198  1.00 13.01 ? 495  GLU A CG  1 
ATOM   3562  C  CD  . GLU A 1 503 ? 17.800  -27.324 37.449  1.00 18.54 ? 495  GLU A CD  1 
ATOM   3563  O  OE1 . GLU A 1 503 ? 18.094  -26.098 37.452  1.00 13.32 ? 495  GLU A OE1 1 
ATOM   3564  O  OE2 . GLU A 1 503 ? 17.274  -27.906 38.430  1.00 18.89 ? 495  GLU A OE2 1 
ATOM   3565  N  N   . SER A 1 504 ? 20.088  -26.879 32.126  1.00 16.98 ? 496  SER A N   1 
ATOM   3566  C  CA  . SER A 1 504 ? 20.308  -25.961 31.013  1.00 15.84 ? 496  SER A CA  1 
ATOM   3567  C  C   . SER A 1 504 ? 19.761  -26.531 29.715  1.00 17.23 ? 496  SER A C   1 
ATOM   3568  O  O   . SER A 1 504 ? 19.157  -25.802 28.919  1.00 17.32 ? 496  SER A O   1 
ATOM   3569  C  CB  . SER A 1 504 ? 21.806  -25.657 30.873  1.00 16.29 ? 496  SER A CB  1 
ATOM   3570  O  OG  . SER A 1 504 ? 22.266  -24.853 31.958  1.00 15.93 ? 496  SER A OG  1 
ATOM   3571  N  N   . LEU A 1 505 ? 19.992  -27.821 29.470  1.00 14.03 ? 497  LEU A N   1 
ATOM   3572  C  CA  . LEU A 1 505 ? 19.486  -28.439 28.248  1.00 15.66 ? 497  LEU A CA  1 
ATOM   3573  C  C   . LEU A 1 505 ? 17.963  -28.482 28.251  1.00 19.55 ? 497  LEU A C   1 
ATOM   3574  O  O   . LEU A 1 505 ? 17.319  -28.182 27.234  1.00 18.58 ? 497  LEU A O   1 
ATOM   3575  C  CB  . LEU A 1 505 ? 20.060  -29.848 28.090  1.00 16.73 ? 497  LEU A CB  1 
ATOM   3576  C  CG  . LEU A 1 505 ? 19.511  -30.628 26.895  1.00 17.10 ? 497  LEU A CG  1 
ATOM   3577  C  CD1 . LEU A 1 505 ? 19.682  -29.816 25.601  1.00 17.55 ? 497  LEU A CD1 1 
ATOM   3578  C  CD2 . LEU A 1 505 ? 20.183  -32.001 26.761  1.00 18.91 ? 497  LEU A CD2 1 
ATOM   3579  N  N   . VAL A 1 506 ? 17.369  -28.830 29.391  1.00 14.82 ? 498  VAL A N   1 
ATOM   3580  C  CA  . VAL A 1 506 ? 15.912  -28.874 29.478  1.00 14.93 ? 498  VAL A CA  1 
ATOM   3581  C  C   . VAL A 1 506 ? 15.326  -27.488 29.265  1.00 14.37 ? 498  VAL A C   1 
ATOM   3582  O  O   . VAL A 1 506 ? 14.314  -27.330 28.576  1.00 16.12 ? 498  VAL A O   1 
ATOM   3583  C  CB  . VAL A 1 506 ? 15.477  -29.475 30.829  1.00 14.18 ? 498  VAL A CB  1 
ATOM   3584  C  CG1 . VAL A 1 506 ? 13.948  -29.388 30.999  1.00 15.46 ? 498  VAL A CG1 1 
ATOM   3585  C  CG2 . VAL A 1 506 ? 15.952  -30.910 30.912  1.00 18.22 ? 498  VAL A CG2 1 
ATOM   3586  N  N   . ALA A 1 507 ? 15.956  -26.462 29.846  1.00 13.40 ? 499  ALA A N   1 
ATOM   3587  C  CA  . ALA A 1 507 ? 15.470  -25.097 29.666  1.00 13.31 ? 499  ALA A CA  1 
ATOM   3588  C  C   . ALA A 1 507 ? 15.528  -24.690 28.199  1.00 15.27 ? 499  ALA A C   1 
ATOM   3589  O  O   . ALA A 1 507 ? 14.576  -24.114 27.670  1.00 12.44 ? 499  ALA A O   1 
ATOM   3590  C  CB  . ALA A 1 507 ? 16.289  -24.129 30.523  1.00 16.45 ? 499  ALA A CB  1 
ATOM   3591  N  N   . TRP A 1 508 ? 16.630  -25.006 27.526  1.00 17.09 ? 500  TRP A N   1 
ATOM   3592  C  CA  . TRP A 1 508 ? 16.754  -24.696 26.107  1.00 16.17 ? 500  TRP A CA  1 
ATOM   3593  C  C   . TRP A 1 508 ? 15.700  -25.431 25.284  1.00 17.01 ? 500  TRP A C   1 
ATOM   3594  O  O   . TRP A 1 508 ? 15.049  -24.839 24.410  1.00 16.51 ? 500  TRP A O   1 
ATOM   3595  C  CB  . TRP A 1 508 ? 18.161  -25.055 25.634  1.00 17.16 ? 500  TRP A CB  1 
ATOM   3596  C  CG  . TRP A 1 508 ? 19.106  -23.891 25.596  1.00 18.52 ? 500  TRP A CG  1 
ATOM   3597  C  CD1 . TRP A 1 508 ? 20.111  -23.608 26.478  1.00 16.59 ? 500  TRP A CD1 1 
ATOM   3598  C  CD2 . TRP A 1 508 ? 19.140  -22.862 24.603  1.00 15.78 ? 500  TRP A CD2 1 
ATOM   3599  N  NE1 . TRP A 1 508 ? 20.769  -22.457 26.093  1.00 15.01 ? 500  TRP A NE1 1 
ATOM   3600  C  CE2 . TRP A 1 508 ? 20.188  -21.981 24.946  1.00 16.97 ? 500  TRP A CE2 1 
ATOM   3601  C  CE3 . TRP A 1 508 ? 18.371  -22.587 23.468  1.00 15.14 ? 500  TRP A CE3 1 
ATOM   3602  C  CZ2 . TRP A 1 508 ? 20.492  -20.848 24.185  1.00 17.63 ? 500  TRP A CZ2 1 
ATOM   3603  C  CZ3 . TRP A 1 508 ? 18.680  -21.460 22.710  1.00 15.51 ? 500  TRP A CZ3 1 
ATOM   3604  C  CH2 . TRP A 1 508 ? 19.733  -20.613 23.070  1.00 16.57 ? 500  TRP A CH2 1 
ATOM   3605  N  N   . ALA A 1 509 ? 15.519  -26.726 25.552  1.00 16.46 ? 501  ALA A N   1 
ATOM   3606  C  CA  . ALA A 1 509 ? 14.561  -27.522 24.792  1.00 14.78 ? 501  ALA A CA  1 
ATOM   3607  C  C   . ALA A 1 509 ? 13.135  -27.038 25.017  1.00 16.27 ? 501  ALA A C   1 
ATOM   3608  O  O   . ALA A 1 509 ? 12.327  -27.007 24.079  1.00 18.74 ? 501  ALA A O   1 
ATOM   3609  C  CB  . ALA A 1 509 ? 14.685  -29.000 25.167  1.00 19.09 ? 501  ALA A CB  1 
ATOM   3610  N  N   . GLU A 1 510 ? 12.799  -26.682 26.258  1.00 16.40 ? 502  GLU A N   1 
ATOM   3611  C  CA  . GLU A 1 510 ? 11.472  -26.142 26.543  1.00 17.38 ? 502  GLU A CA  1 
ATOM   3612  C  C   . GLU A 1 510 ? 11.269  -24.782 25.881  1.00 16.42 ? 502  GLU A C   1 
ATOM   3613  O  O   . GLU A 1 510 ? 10.187  -24.496 25.346  1.00 15.81 ? 502  GLU A O   1 
ATOM   3614  C  CB  . GLU A 1 510 ? 11.265  -26.041 28.056  1.00 17.47 ? 502  GLU A CB  1 
ATOM   3615  C  CG  . GLU A 1 510 ? 11.114  -27.406 28.725  1.00 18.64 ? 502  GLU A CG  1 
ATOM   3616  C  CD  . GLU A 1 510 ? 9.905   -28.165 28.195  1.00 21.01 ? 502  GLU A CD  1 
ATOM   3617  O  OE1 . GLU A 1 510 ? 8.790   -27.597 28.249  1.00 18.15 ? 502  GLU A OE1 1 
ATOM   3618  O  OE2 . GLU A 1 510 ? 10.067  -29.309 27.724  1.00 21.58 ? 502  GLU A OE2 1 
ATOM   3619  N  N   . ALA A 1 511 ? 12.288  -23.922 25.917  1.00 14.19 ? 503  ALA A N   1 
ATOM   3620  C  CA  . ALA A 1 511 ? 12.175  -22.648 25.216  1.00 11.60 ? 503  ALA A CA  1 
ATOM   3621  C  C   . ALA A 1 511 ? 11.962  -22.865 23.723  1.00 14.06 ? 503  ALA A C   1 
ATOM   3622  O  O   . ALA A 1 511 ? 11.172  -22.154 23.091  1.00 17.97 ? 503  ALA A O   1 
ATOM   3623  C  CB  . ALA A 1 511 ? 13.414  -21.789 25.460  1.00 10.99 ? 503  ALA A CB  1 
ATOM   3624  N  N   . ALA A 1 512 ? 12.658  -23.848 23.142  1.00 13.43 ? 504  ALA A N   1 
ATOM   3625  C  CA  . ALA A 1 512 ? 12.529  -24.089 21.714  1.00 14.57 ? 504  ALA A CA  1 
ATOM   3626  C  C   . ALA A 1 512 ? 11.174  -24.692 21.376  1.00 17.45 ? 504  ALA A C   1 
ATOM   3627  O  O   . ALA A 1 512 ? 10.610  -24.380 20.320  1.00 18.79 ? 504  ALA A O   1 
ATOM   3628  C  CB  . ALA A 1 512 ? 13.659  -24.996 21.224  1.00 18.25 ? 504  ALA A CB  1 
ATOM   3629  N  N   . LYS A 1 513 ? 10.631  -25.524 22.276  1.00 17.00 ? 505  LYS A N   1 
ATOM   3630  C  CA  . LYS A 1 513 ? 9.332   -26.167 22.078  1.00 19.87 ? 505  LYS A CA  1 
ATOM   3631  C  C   . LYS A 1 513 ? 8.166   -25.196 22.203  1.00 19.39 ? 505  LYS A C   1 
ATOM   3632  O  O   . LYS A 1 513 ? 7.111   -25.429 21.604  1.00 20.71 ? 505  LYS A O   1 
ATOM   3633  C  CB  . LYS A 1 513 ? 9.117   -27.280 23.113  1.00 22.27 ? 505  LYS A CB  1 
ATOM   3634  C  CG  . LYS A 1 513 ? 9.850   -28.573 22.869  1.00 38.62 ? 505  LYS A CG  1 
ATOM   3635  C  CD  . LYS A 1 513 ? 9.396   -29.639 23.862  1.00 40.99 ? 505  LYS A CD  1 
ATOM   3636  C  CE  . LYS A 1 513 ? 7.882   -29.808 23.809  1.00 46.65 ? 505  LYS A CE  1 
ATOM   3637  N  NZ  . LYS A 1 513 ? 7.411   -31.099 24.396  1.00 50.66 ? 505  LYS A NZ  1 
ATOM   3638  N  N   . ALA A 1 514 ? 8.297   -24.158 23.028  1.00 17.26 ? 506  ALA A N   1 
ATOM   3639  C  CA  . ALA A 1 514 ? 7.151   -23.302 23.308  1.00 16.64 ? 506  ALA A CA  1 
ATOM   3640  C  C   . ALA A 1 514 ? 6.654   -22.667 22.020  1.00 19.34 ? 506  ALA A C   1 
ATOM   3641  O  O   . ALA A 1 514 ? 7.428   -22.071 21.268  1.00 20.52 ? 506  ALA A O   1 
ATOM   3642  C  CB  . ALA A 1 514 ? 7.522   -22.221 24.321  1.00 17.72 ? 506  ALA A CB  1 
ATOM   3643  N  N   . GLU A 1 515 ? 5.365   -22.814 21.759  1.00 19.86 ? 507  GLU A N   1 
ATOM   3644  C  CA  . GLU A 1 515 ? 4.800   -22.324 20.511  1.00 27.43 ? 507  GLU A CA  1 
ATOM   3645  C  C   . GLU A 1 515 ? 4.383   -20.866 20.583  1.00 26.41 ? 507  GLU A C   1 
ATOM   3646  O  O   . GLU A 1 515 ? 4.468   -20.156 19.570  1.00 24.70 ? 507  GLU A O   1 
ATOM   3647  C  CB  . GLU A 1 515 ? 3.591   -23.173 20.112  1.00 34.98 ? 507  GLU A CB  1 
ATOM   3648  C  CG  . GLU A 1 515 ? 3.959   -24.502 19.493  1.00 44.64 ? 507  GLU A CG  1 
ATOM   3649  C  CD  . GLU A 1 515 ? 2.745   -25.344 19.157  1.00 51.54 ? 507  GLU A CD  1 
ATOM   3650  O  OE1 . GLU A 1 515 ? 2.921   -26.556 18.918  1.00 55.21 ? 507  GLU A OE1 1 
ATOM   3651  O  OE2 . GLU A 1 515 ? 1.620   -24.796 19.136  1.00 53.23 ? 507  GLU A OE2 1 
ATOM   3652  N  N   . ASP A 1 516 ? 3.957   -20.386 21.753  1.00 15.65 ? 508  ASP A N   1 
ATOM   3653  C  CA  . ASP A 1 516 ? 3.240   -19.117 21.790  1.00 15.57 ? 508  ASP A CA  1 
ATOM   3654  C  C   . ASP A 1 516 ? 3.728   -18.199 22.898  1.00 15.22 ? 508  ASP A C   1 
ATOM   3655  O  O   . ASP A 1 516 ? 2.970   -17.349 23.376  1.00 14.19 ? 508  ASP A O   1 
ATOM   3656  C  CB  . ASP A 1 516 ? 1.733   -19.345 21.925  1.00 23.52 ? 508  ASP A CB  1 
ATOM   3657  C  CG  . ASP A 1 516 ? 1.344   -20.051 23.226  1.00 32.30 ? 508  ASP A CG  1 
ATOM   3658  O  OD1 . ASP A 1 516 ? 2.223   -20.511 23.989  1.00 27.37 ? 508  ASP A OD1 1 
ATOM   3659  O  OD2 . ASP A 1 516 ? 0.127   -20.153 23.479  1.00 34.95 ? 508  ASP A OD2 1 
ATOM   3660  N  N   . HIS A 1 517 ? 4.980   -18.345 23.322  1.00 13.67 ? 509  HIS A N   1 
ATOM   3661  C  CA  . HIS A 1 517 ? 5.528   -17.411 24.292  1.00 14.34 ? 509  HIS A CA  1 
ATOM   3662  C  C   . HIS A 1 517 ? 7.038   -17.432 24.214  1.00 16.65 ? 509  HIS A C   1 
ATOM   3663  O  O   . HIS A 1 517 ? 7.628   -18.457 23.844  1.00 15.25 ? 509  HIS A O   1 
ATOM   3664  C  CB  . HIS A 1 517 ? 5.082   -17.737 25.723  1.00 16.17 ? 509  HIS A CB  1 
ATOM   3665  C  CG  . HIS A 1 517 ? 5.497   -19.090 26.204  1.00 17.56 ? 509  HIS A CG  1 
ATOM   3666  N  ND1 . HIS A 1 517 ? 4.670   -20.192 26.123  1.00 18.19 ? 509  HIS A ND1 1 
ATOM   3667  C  CD2 . HIS A 1 517 ? 6.631   -19.513 26.809  1.00 15.51 ? 509  HIS A CD2 1 
ATOM   3668  C  CE1 . HIS A 1 517 ? 5.283   -21.237 26.650  1.00 19.10 ? 509  HIS A CE1 1 
ATOM   3669  N  NE2 . HIS A 1 517 ? 6.470   -20.852 27.077  1.00 16.58 ? 509  HIS A NE2 1 
ATOM   3670  N  N   . PRO A 1 518 ? 7.686   -16.337 24.583  1.00 12.34 ? 510  PRO A N   1 
ATOM   3671  C  CA  . PRO A 1 518 ? 9.148   -16.303 24.629  1.00 10.36 ? 510  PRO A CA  1 
ATOM   3672  C  C   . PRO A 1 518 ? 9.668   -16.832 25.958  1.00 11.20 ? 510  PRO A C   1 
ATOM   3673  O  O   . PRO A 1 518 ? 8.915   -17.127 26.889  1.00 12.39 ? 510  PRO A O   1 
ATOM   3674  C  CB  . PRO A 1 518 ? 9.455   -14.815 24.463  1.00 9.80  ? 510  PRO A CB  1 
ATOM   3675  C  CG  . PRO A 1 518 ? 8.304   -14.154 25.197  1.00 12.47 ? 510  PRO A CG  1 
ATOM   3676  C  CD  . PRO A 1 518 ? 7.091   -15.015 24.851  1.00 10.95 ? 510  PRO A CD  1 
ATOM   3677  N  N   . SER A 1 519 ? 10.990  -16.958 26.020  1.00 10.51 ? 511  SER A N   1 
ATOM   3678  C  CA  . SER A 1 519 ? 11.672  -17.420 27.214  1.00 12.61 ? 511  SER A CA  1 
ATOM   3679  C  C   . SER A 1 519 ? 12.927  -16.584 27.401  1.00 8.44  ? 511  SER A C   1 
ATOM   3680  O  O   . SER A 1 519 ? 13.531  -16.125 26.429  1.00 10.81 ? 511  SER A O   1 
ATOM   3681  C  CB  . SER A 1 519 ? 12.046  -18.915 27.122  1.00 13.43 ? 511  SER A CB  1 
ATOM   3682  O  OG  . SER A 1 519 ? 10.919  -19.741 26.852  1.00 15.71 ? 511  SER A OG  1 
ATOM   3683  N  N   . CYS A 1 520 ? 13.271  -16.342 28.664  1.00 8.08  ? 512  CYS A N   1 
ATOM   3684  C  CA  . CYS A 1 520 ? 14.556  -15.778 29.053  1.00 9.04  ? 512  CYS A CA  1 
ATOM   3685  C  C   . CYS A 1 520 ? 15.350  -16.900 29.704  1.00 9.34  ? 512  CYS A C   1 
ATOM   3686  O  O   . CYS A 1 520 ? 14.876  -17.513 30.671  1.00 14.35 ? 512  CYS A O   1 
ATOM   3687  C  CB  . CYS A 1 520 ? 14.391  -14.620 30.042  1.00 13.30 ? 512  CYS A CB  1 
ATOM   3688  S  SG  . CYS A 1 520 ? 13.579  -13.153 29.408  1.00 15.31 ? 512  CYS A SG  1 
ATOM   3689  N  N   . LEU A 1 521 ? 16.535  -17.180 29.171  1.00 8.54  ? 513  LEU A N   1 
ATOM   3690  C  CA  . LEU A 1 521 ? 17.416  -18.208 29.710  1.00 9.82  ? 513  LEU A CA  1 
ATOM   3691  C  C   . LEU A 1 521 ? 18.588  -17.496 30.375  1.00 13.25 ? 513  LEU A C   1 
ATOM   3692  O  O   . LEU A 1 521 ? 19.303  -16.731 29.721  1.00 14.38 ? 513  LEU A O   1 
ATOM   3693  C  CB  . LEU A 1 521 ? 17.900  -19.150 28.607  1.00 12.63 ? 513  LEU A CB  1 
ATOM   3694  C  CG  . LEU A 1 521 ? 16.820  -19.822 27.747  1.00 14.73 ? 513  LEU A CG  1 
ATOM   3695  C  CD1 . LEU A 1 521 ? 17.431  -20.806 26.726  1.00 13.28 ? 513  LEU A CD1 1 
ATOM   3696  C  CD2 . LEU A 1 521 ? 15.798  -20.534 28.621  1.00 12.73 ? 513  LEU A CD2 1 
ATOM   3697  N  N   . ILE A 1 522 ? 18.784  -17.743 31.664  1.00 14.49 ? 514  ILE A N   1 
ATOM   3698  C  CA  . ILE A 1 522 ? 19.684  -16.933 32.478  1.00 13.86 ? 514  ILE A CA  1 
ATOM   3699  C  C   . ILE A 1 522 ? 20.801  -17.829 33.000  1.00 10.99 ? 514  ILE A C   1 
ATOM   3700  O  O   . ILE A 1 522 ? 20.532  -18.818 33.693  1.00 13.14 ? 514  ILE A O   1 
ATOM   3701  C  CB  . ILE A 1 522 ? 18.921  -16.241 33.617  1.00 11.82 ? 514  ILE A CB  1 
ATOM   3702  C  CG1 . ILE A 1 522 ? 17.945  -15.216 33.015  1.00 13.81 ? 514  ILE A CG1 1 
ATOM   3703  C  CG2 . ILE A 1 522 ? 19.873  -15.542 34.547  1.00 11.77 ? 514  ILE A CG2 1 
ATOM   3704  C  CD1 . ILE A 1 522 ? 17.011  -14.613 34.002  1.00 11.38 ? 514  ILE A CD1 1 
ATOM   3705  N  N   . PHE A 1 523 ? 22.050  -17.478 32.667  1.00 10.53 ? 515  PHE A N   1 
ATOM   3706  C  CA  . PHE A 1 523 ? 23.191  -18.359 32.850  1.00 11.94 ? 515  PHE A CA  1 
ATOM   3707  C  C   . PHE A 1 523 ? 24.280  -17.672 33.657  1.00 14.06 ? 515  PHE A C   1 
ATOM   3708  O  O   . PHE A 1 523 ? 24.438  -16.451 33.599  1.00 13.35 ? 515  PHE A O   1 
ATOM   3709  C  CB  . PHE A 1 523 ? 23.757  -18.808 31.497  1.00 12.44 ? 515  PHE A CB  1 
ATOM   3710  C  CG  . PHE A 1 523 ? 22.782  -19.615 30.677  1.00 14.32 ? 515  PHE A CG  1 
ATOM   3711  C  CD1 . PHE A 1 523 ? 22.475  -20.926 31.033  1.00 12.72 ? 515  PHE A CD1 1 
ATOM   3712  C  CD2 . PHE A 1 523 ? 22.179  -19.066 29.561  1.00 15.27 ? 515  PHE A CD2 1 
ATOM   3713  C  CE1 . PHE A 1 523 ? 21.582  -21.675 30.283  1.00 16.06 ? 515  PHE A CE1 1 
ATOM   3714  C  CE2 . PHE A 1 523 ? 21.274  -19.806 28.806  1.00 17.32 ? 515  PHE A CE2 1 
ATOM   3715  C  CZ  . PHE A 1 523 ? 20.970  -21.109 29.168  1.00 17.25 ? 515  PHE A CZ  1 
ATOM   3716  N  N   . SER A 1 524 ? 25.050  -18.477 34.383  1.00 14.88 ? 516  SER A N   1 
ATOM   3717  C  CA  . SER A 1 524 ? 26.076  -17.978 35.295  1.00 14.68 ? 516  SER A CA  1 
ATOM   3718  C  C   . SER A 1 524 ? 27.430  -17.831 34.607  1.00 23.30 ? 516  SER A C   1 
ATOM   3719  O  O   . SER A 1 524 ? 27.762  -18.573 33.680  1.00 21.79 ? 516  SER A O   1 
ATOM   3720  C  CB  . SER A 1 524 ? 26.229  -18.926 36.483  1.00 17.02 ? 516  SER A CB  1 
ATOM   3721  O  OG  . SER A 1 524 ? 27.017  -20.050 36.100  1.00 21.07 ? 516  SER A OG  1 
ATOM   3722  N  N   . ARG A 1 525 ? 28.230  -16.878 35.098  1.00 24.09 ? 517  ARG A N   1 
ATOM   3723  C  CA  . ARG A 1 525 ? 29.617  -16.780 34.658  1.00 23.02 ? 517  ARG A CA  1 
ATOM   3724  C  C   . ARG A 1 525 ? 30.488  -17.838 35.325  1.00 29.87 ? 517  ARG A C   1 
ATOM   3725  O  O   . ARG A 1 525 ? 31.395  -18.389 34.689  1.00 30.42 ? 517  ARG A O   1 
ATOM   3726  C  CB  . ARG A 1 525 ? 30.178  -15.385 34.949  1.00 23.87 ? 517  ARG A CB  1 
ATOM   3727  C  CG  . ARG A 1 525 ? 31.670  -15.245 34.607  1.00 23.92 ? 517  ARG A CG  1 
ATOM   3728  C  CD  . ARG A 1 525 ? 32.279  -13.968 35.175  1.00 36.00 ? 517  ARG A CD  1 
ATOM   3729  N  NE  . ARG A 1 525 ? 33.397  -13.480 34.370  1.00 46.41 ? 517  ARG A NE  1 
ATOM   3730  C  CZ  . ARG A 1 525 ? 34.664  -13.435 34.780  1.00 55.25 ? 517  ARG A CZ  1 
ATOM   3731  N  NH1 . ARG A 1 525 ? 34.991  -13.837 36.004  1.00 52.75 ? 517  ARG A NH1 1 
ATOM   3732  N  NH2 . ARG A 1 525 ? 35.607  -12.974 33.965  1.00 54.92 ? 517  ARG A NH2 1 
ATOM   3733  N  N   . GLN A 1 526 ? 30.228  -18.135 36.598  1.00 29.26 ? 518  GLN A N   1 
ATOM   3734  C  CA  . GLN A 1 526 ? 31.086  -19.005 37.394  1.00 31.73 ? 518  GLN A CA  1 
ATOM   3735  C  C   . GLN A 1 526 ? 30.612  -20.460 37.329  1.00 31.79 ? 518  GLN A C   1 
ATOM   3736  O  O   . GLN A 1 526 ? 29.447  -20.749 37.041  1.00 25.71 ? 518  GLN A O   1 
ATOM   3737  C  CB  . GLN A 1 526 ? 31.125  -18.516 38.848  1.00 25.95 ? 518  GLN A CB  1 
ATOM   3738  C  CG  . GLN A 1 526 ? 29.867  -18.824 39.679  1.00 21.45 ? 518  GLN A CG  1 
ATOM   3739  C  CD  . GLN A 1 526 ? 28.696  -17.870 39.435  1.00 24.89 ? 518  GLN A CD  1 
ATOM   3740  O  OE1 . GLN A 1 526 ? 28.678  -17.105 38.470  1.00 24.76 ? 518  GLN A OE1 1 
ATOM   3741  N  NE2 . GLN A 1 526 ? 27.699  -17.925 40.326  1.00 23.37 ? 518  GLN A NE2 1 
ATOM   3742  N  N   . ASN A 1 527 ? 31.538  -21.381 37.612  1.00 31.20 ? 519  ASN A N   1 
ATOM   3743  C  CA  . ASN A 1 527 ? 31.242  -22.806 37.499  1.00 31.62 ? 519  ASN A CA  1 
ATOM   3744  C  C   . ASN A 1 527 ? 30.171  -23.224 38.500  1.00 31.09 ? 519  ASN A C   1 
ATOM   3745  O  O   . ASN A 1 527 ? 30.166  -22.779 39.651  1.00 27.69 ? 519  ASN A O   1 
ATOM   3746  C  CB  . ASN A 1 527 ? 32.504  -23.644 37.732  1.00 34.80 ? 519  ASN A CB  1 
ATOM   3747  C  CG  . ASN A 1 527 ? 33.510  -23.543 36.593  1.00 33.67 ? 519  ASN A CG  1 
ATOM   3748  O  OD1 . ASN A 1 527 ? 33.220  -22.997 35.528  1.00 34.62 ? 519  ASN A OD1 1 
ATOM   3749  N  ND2 . ASN A 1 527 ? 34.705  -24.087 36.818  1.00 40.30 ? 519  ASN A ND2 1 
ATOM   3750  N  N   . LEU A 1 528 ? 29.271  -24.105 38.062  1.00 31.08 ? 520  LEU A N   1 
ATOM   3751  C  CA  . LEU A 1 528 ? 28.190  -24.611 38.900  1.00 29.92 ? 520  LEU A CA  1 
ATOM   3752  C  C   . LEU A 1 528 ? 28.293  -26.128 39.012  1.00 33.63 ? 520  LEU A C   1 
ATOM   3753  O  O   . LEU A 1 528 ? 28.482  -26.822 38.009  1.00 25.58 ? 520  LEU A O   1 
ATOM   3754  C  CB  . LEU A 1 528 ? 26.820  -24.211 38.346  1.00 24.95 ? 520  LEU A CB  1 
ATOM   3755  C  CG  . LEU A 1 528 ? 26.500  -22.730 38.122  1.00 23.96 ? 520  LEU A CG  1 
ATOM   3756  C  CD1 . LEU A 1 528 ? 25.004  -22.546 38.039  1.00 18.75 ? 520  LEU A CD1 1 
ATOM   3757  C  CD2 . LEU A 1 528 ? 27.087  -21.843 39.218  1.00 27.31 ? 520  LEU A CD2 1 
ATOM   3758  N  N   . LYS A 1 529 ? 28.161  -26.639 40.231  1.00 35.40 ? 521  LYS A N   1 
ATOM   3759  C  CA  . LYS A 1 529 ? 28.351  -28.064 40.457  1.00 33.58 ? 521  LYS A CA  1 
ATOM   3760  C  C   . LYS A 1 529 ? 27.185  -28.856 39.879  1.00 24.39 ? 521  LYS A C   1 
ATOM   3761  O  O   . LYS A 1 529 ? 26.019  -28.514 40.092  1.00 24.37 ? 521  LYS A O   1 
ATOM   3762  C  CB  . LYS A 1 529 ? 28.508  -28.349 41.952  1.00 38.19 ? 521  LYS A CB  1 
ATOM   3763  N  N   . PHE A 1 530 ? 27.508  -29.913 39.141  1.00 26.30 ? 522  PHE A N   1 
ATOM   3764  C  CA  . PHE A 1 530 ? 26.487  -30.808 38.614  1.00 29.23 ? 522  PHE A CA  1 
ATOM   3765  C  C   . PHE A 1 530 ? 25.811  -31.577 39.747  1.00 29.87 ? 522  PHE A C   1 
ATOM   3766  O  O   . PHE A 1 530 ? 26.468  -32.054 40.676  1.00 30.15 ? 522  PHE A O   1 
ATOM   3767  C  CB  . PHE A 1 530 ? 27.113  -31.783 37.613  1.00 29.39 ? 522  PHE A CB  1 
ATOM   3768  C  CG  . PHE A 1 530 ? 26.123  -32.705 36.970  1.00 28.61 ? 522  PHE A CG  1 
ATOM   3769  C  CD1 . PHE A 1 530 ? 25.389  -32.292 35.869  1.00 26.66 ? 522  PHE A CD1 1 
ATOM   3770  C  CD2 . PHE A 1 530 ? 25.922  -33.983 37.467  1.00 32.51 ? 522  PHE A CD2 1 
ATOM   3771  C  CE1 . PHE A 1 530 ? 24.466  -33.129 35.279  1.00 30.91 ? 522  PHE A CE1 1 
ATOM   3772  C  CE2 . PHE A 1 530 ? 25.002  -34.831 36.877  1.00 35.56 ? 522  PHE A CE2 1 
ATOM   3773  C  CZ  . PHE A 1 530 ? 24.276  -34.403 35.778  1.00 35.83 ? 522  PHE A CZ  1 
ATOM   3774  N  N   . GLN A 1 531 ? 24.490  -31.699 39.666  1.00 22.75 ? 523  GLN A N   1 
ATOM   3775  C  CA  . GLN A 1 531 ? 23.697  -32.398 40.676  1.00 22.09 ? 523  GLN A CA  1 
ATOM   3776  C  C   . GLN A 1 531 ? 23.248  -33.746 40.133  1.00 23.19 ? 523  GLN A C   1 
ATOM   3777  O  O   . GLN A 1 531 ? 22.697  -33.819 39.030  1.00 23.22 ? 523  GLN A O   1 
ATOM   3778  C  CB  . GLN A 1 531 ? 22.466  -31.573 41.069  1.00 24.92 ? 523  GLN A CB  1 
ATOM   3779  C  CG  . GLN A 1 531 ? 22.776  -30.155 41.518  1.00 23.58 ? 523  GLN A CG  1 
ATOM   3780  C  CD  . GLN A 1 531 ? 23.575  -30.147 42.797  1.00 29.72 ? 523  GLN A CD  1 
ATOM   3781  O  OE1 . GLN A 1 531 ? 23.231  -30.837 43.751  1.00 32.36 ? 523  GLN A OE1 1 
ATOM   3782  N  NE2 . GLN A 1 531 ? 24.666  -29.392 42.815  1.00 34.08 ? 523  GLN A NE2 1 
ATOM   3783  N  N   . ALA A 1 532 ? 23.450  -34.803 40.913  1.00 22.76 ? 524  ALA A N   1 
ATOM   3784  C  CA  . ALA A 1 532 ? 22.977  -36.114 40.495  1.00 25.96 ? 524  ALA A CA  1 
ATOM   3785  C  C   . ALA A 1 532 ? 21.455  -36.175 40.578  1.00 26.70 ? 524  ALA A C   1 
ATOM   3786  O  O   . ALA A 1 532 ? 20.834  -35.531 41.426  1.00 25.94 ? 524  ALA A O   1 
ATOM   3787  C  CB  . ALA A 1 532 ? 23.602  -37.210 41.357  1.00 29.01 ? 524  ALA A CB  1 
ATOM   3788  N  N   . ARG A 1 533 ? 20.849  -36.953 39.679  1.00 20.77 ? 525  ARG A N   1 
ATOM   3789  C  CA  . ARG A 1 533 ? 19.396  -36.998 39.588  1.00 19.18 ? 525  ARG A CA  1 
ATOM   3790  C  C   . ARG A 1 533 ? 18.943  -38.397 39.214  1.00 28.05 ? 525  ARG A C   1 
ATOM   3791  O  O   . ARG A 1 533 ? 19.621  -39.098 38.461  1.00 21.29 ? 525  ARG A O   1 
ATOM   3792  C  CB  . ARG A 1 533 ? 18.852  -36.016 38.539  1.00 18.10 ? 525  ARG A CB  1 
ATOM   3793  C  CG  . ARG A 1 533 ? 18.793  -34.574 38.984  1.00 18.29 ? 525  ARG A CG  1 
ATOM   3794  C  CD  . ARG A 1 533 ? 18.241  -33.677 37.879  1.00 19.03 ? 525  ARG A CD  1 
ATOM   3795  N  NE  . ARG A 1 533 ? 18.465  -32.284 38.231  1.00 20.24 ? 525  ARG A NE  1 
ATOM   3796  C  CZ  . ARG A 1 533 ? 19.616  -31.657 38.015  1.00 18.38 ? 525  ARG A CZ  1 
ATOM   3797  N  NH1 . ARG A 1 533 ? 20.611  -32.294 37.411  1.00 17.62 ? 525  ARG A NH1 1 
ATOM   3798  N  NH2 . ARG A 1 533 ? 19.760  -30.399 38.386  1.00 17.69 ? 525  ARG A NH2 1 
ATOM   3799  N  N   . SER A 1 534 ? 17.771  -38.782 39.718  1.00 20.22 ? 526  SER A N   1 
ATOM   3800  C  CA  . SER A 1 534 ? 17.100  -39.963 39.200  1.00 22.61 ? 526  SER A CA  1 
ATOM   3801  C  C   . SER A 1 534 ? 16.462  -39.647 37.853  1.00 20.81 ? 526  SER A C   1 
ATOM   3802  O  O   . SER A 1 534 ? 16.340  -38.487 37.446  1.00 19.68 ? 526  SER A O   1 
ATOM   3803  C  CB  . SER A 1 534 ? 16.032  -40.453 40.174  1.00 24.93 ? 526  SER A CB  1 
ATOM   3804  O  OG  . SER A 1 534 ? 14.933  -39.554 40.172  1.00 21.26 ? 526  SER A OG  1 
ATOM   3805  N  N   . GLU A 1 535 ? 16.036  -40.703 37.156  1.00 26.83 ? 527  GLU A N   1 
ATOM   3806  C  CA  . GLU A 1 535 ? 15.311  -40.499 35.906  1.00 24.58 ? 527  GLU A CA  1 
ATOM   3807  C  C   . GLU A 1 535 ? 14.053  -39.667 36.131  1.00 22.55 ? 527  GLU A C   1 
ATOM   3808  O  O   . GLU A 1 535 ? 13.715  -38.808 35.310  1.00 20.01 ? 527  GLU A O   1 
ATOM   3809  C  CB  . GLU A 1 535 ? 14.970  -41.849 35.268  1.00 28.21 ? 527  GLU A CB  1 
ATOM   3810  C  CG  . GLU A 1 535 ? 14.300  -41.733 33.910  1.00 30.73 ? 527  GLU A CG  1 
ATOM   3811  C  CD  . GLU A 1 535 ? 14.345  -43.027 33.122  1.00 32.23 ? 527  GLU A CD  1 
ATOM   3812  O  OE1 . GLU A 1 535 ? 14.206  -42.979 31.882  1.00 36.73 ? 527  GLU A OE1 1 
ATOM   3813  O  OE2 . GLU A 1 535 ? 14.523  -44.092 33.735  1.00 31.53 ? 527  GLU A OE2 1 
ATOM   3814  N  N   . GLN A 1 536 ? 13.351  -39.893 37.246  1.00 20.71 ? 528  GLN A N   1 
ATOM   3815  C  CA  . GLN A 1 536 ? 12.146  -39.109 37.517  1.00 23.23 ? 528  GLN A CA  1 
ATOM   3816  C  C   . GLN A 1 536 ? 12.472  -37.632 37.745  1.00 24.54 ? 528  GLN A C   1 
ATOM   3817  O  O   . GLN A 1 536 ? 11.739  -36.747 37.286  1.00 17.70 ? 528  GLN A O   1 
ATOM   3818  C  CB  . GLN A 1 536 ? 11.400  -39.688 38.721  1.00 25.09 ? 528  GLN A CB  1 
ATOM   3819  C  CG  . GLN A 1 536 ? 10.072  -39.005 39.005  1.00 28.81 ? 528  GLN A CG  1 
ATOM   3820  C  CD  . GLN A 1 536 ? 9.107   -39.113 37.838  1.00 33.99 ? 528  GLN A CD  1 
ATOM   3821  O  OE1 . GLN A 1 536 ? 8.913   -40.189 37.280  1.00 33.19 ? 528  GLN A OE1 1 
ATOM   3822  N  NE2 . GLN A 1 536 ? 8.511   -37.992 37.454  1.00 32.38 ? 528  GLN A NE2 1 
ATOM   3823  N  N   . GLN A 1 537 ? 13.557  -37.338 38.460  1.00 18.11 ? 529  GLN A N   1 
ATOM   3824  C  CA  . GLN A 1 537 ? 13.904  -35.937 38.687  1.00 16.90 ? 529  GLN A CA  1 
ATOM   3825  C  C   . GLN A 1 537 ? 14.291  -35.249 37.385  1.00 17.10 ? 529  GLN A C   1 
ATOM   3826  O  O   . GLN A 1 537 ? 13.860  -34.119 37.117  1.00 15.48 ? 529  GLN A O   1 
ATOM   3827  C  CB  . GLN A 1 537 ? 15.035  -35.836 39.709  1.00 17.47 ? 529  GLN A CB  1 
ATOM   3828  C  CG  . GLN A 1 537 ? 14.605  -36.152 41.124  1.00 17.25 ? 529  GLN A CG  1 
ATOM   3829  C  CD  . GLN A 1 537 ? 15.787  -36.351 42.059  1.00 23.80 ? 529  GLN A CD  1 
ATOM   3830  O  OE1 . GLN A 1 537 ? 16.794  -36.938 41.680  1.00 22.19 ? 529  GLN A OE1 1 
ATOM   3831  N  NE2 . GLN A 1 537 ? 15.665  -35.863 43.283  1.00 27.12 ? 529  GLN A NE2 1 
ATOM   3832  N  N   . LEU A 1 538 ? 15.082  -35.923 36.551  1.00 19.33 ? 530  LEU A N   1 
ATOM   3833  C  CA  . LEU A 1 538 ? 15.403  -35.386 35.235  1.00 18.58 ? 530  LEU A CA  1 
ATOM   3834  C  C   . LEU A 1 538 ? 14.143  -35.018 34.468  1.00 16.65 ? 530  LEU A C   1 
ATOM   3835  O  O   . LEU A 1 538 ? 14.061  -33.945 33.857  1.00 19.47 ? 530  LEU A O   1 
ATOM   3836  C  CB  . LEU A 1 538 ? 16.213  -36.409 34.443  1.00 19.14 ? 530  LEU A CB  1 
ATOM   3837  C  CG  . LEU A 1 538 ? 17.719  -36.378 34.679  1.00 26.17 ? 530  LEU A CG  1 
ATOM   3838  C  CD1 . LEU A 1 538 ? 18.351  -37.608 34.041  1.00 31.11 ? 530  LEU A CD1 1 
ATOM   3839  C  CD2 . LEU A 1 538 ? 18.289  -35.083 34.088  1.00 22.86 ? 530  LEU A CD2 1 
ATOM   3840  N  N   . ASN A 1 539 ? 13.149  -35.908 34.486  1.00 17.39 ? 531  ASN A N   1 
ATOM   3841  C  CA  . ASN A 1 539 ? 11.921  -35.657 33.741  1.00 17.39 ? 531  ASN A CA  1 
ATOM   3842  C  C   . ASN A 1 539 ? 11.045  -34.597 34.382  1.00 16.38 ? 531  ASN A C   1 
ATOM   3843  O  O   . ASN A 1 539 ? 10.171  -34.052 33.706  1.00 18.07 ? 531  ASN A O   1 
ATOM   3844  C  CB  . ASN A 1 539 ? 11.128  -36.950 33.590  1.00 20.38 ? 531  ASN A CB  1 
ATOM   3845  C  CG  . ASN A 1 539 ? 11.721  -37.857 32.543  1.00 30.37 ? 531  ASN A CG  1 
ATOM   3846  O  OD1 . ASN A 1 539 ? 12.329  -37.385 31.582  1.00 38.28 ? 531  ASN A OD1 1 
ATOM   3847  N  ND2 . ASN A 1 539 ? 11.548  -39.163 32.714  1.00 33.66 ? 531  ASN A ND2 1 
ATOM   3848  N  N   . ASP A 1 540 ? 11.247  -34.289 35.658  1.00 17.61 ? 532  ASP A N   1 
ATOM   3849  C  CA  . ASP A 1 540 ? 10.468  -33.236 36.290  1.00 17.37 ? 532  ASP A CA  1 
ATOM   3850  C  C   . ASP A 1 540 ? 11.095  -31.852 36.168  1.00 17.37 ? 532  ASP A C   1 
ATOM   3851  O  O   . ASP A 1 540 ? 10.469  -30.873 36.586  1.00 18.13 ? 532  ASP A O   1 
ATOM   3852  C  CB  . ASP A 1 540 ? 10.233  -33.569 37.764  1.00 17.89 ? 532  ASP A CB  1 
ATOM   3853  C  CG  . ASP A 1 540 ? 9.197   -34.650 37.951  1.00 21.26 ? 532  ASP A CG  1 
ATOM   3854  O  OD1 . ASP A 1 540 ? 8.315   -34.779 37.080  1.00 20.88 ? 532  ASP A OD1 1 
ATOM   3855  O  OD2 . ASP A 1 540 ? 9.263   -35.373 38.968  1.00 24.08 ? 532  ASP A OD2 1 
ATOM   3856  N  N   . ILE A 1 541 ? 12.302  -31.732 35.608  1.00 18.13 ? 533  ILE A N   1 
ATOM   3857  C  CA  . ILE A 1 541 ? 12.882  -30.403 35.427  1.00 13.60 ? 533  ILE A CA  1 
ATOM   3858  C  C   . ILE A 1 541 ? 11.941  -29.520 34.613  1.00 15.39 ? 533  ILE A C   1 
ATOM   3859  O  O   . ILE A 1 541 ? 11.743  -28.341 34.930  1.00 14.18 ? 533  ILE A O   1 
ATOM   3860  C  CB  . ILE A 1 541 ? 14.277  -30.501 34.777  1.00 14.02 ? 533  ILE A CB  1 
ATOM   3861  C  CG1 . ILE A 1 541 ? 15.249  -31.231 35.709  1.00 18.61 ? 533  ILE A CG1 1 
ATOM   3862  C  CG2 . ILE A 1 541 ? 14.806  -29.092 34.423  1.00 13.23 ? 533  ILE A CG2 1 
ATOM   3863  C  CD1 . ILE A 1 541 ? 16.589  -31.611 35.053  1.00 14.18 ? 533  ILE A CD1 1 
ATOM   3864  N  N   . LYS A 1 542 ? 11.295  -30.093 33.593  1.00 13.08 ? 534  LYS A N   1 
ATOM   3865  C  CA  . LYS A 1 542 ? 10.442  -29.323 32.700  1.00 16.81 ? 534  LYS A CA  1 
ATOM   3866  C  C   . LYS A 1 542 ? 9.165   -28.844 33.369  1.00 16.96 ? 534  LYS A C   1 
ATOM   3867  O  O   . LYS A 1 542 ? 8.417   -28.073 32.754  1.00 14.99 ? 534  LYS A O   1 
ATOM   3868  C  CB  . LYS A 1 542 ? 10.085  -30.146 31.464  1.00 16.03 ? 534  LYS A CB  1 
ATOM   3869  C  CG  . LYS A 1 542 ? 9.303   -31.408 31.747  1.00 16.29 ? 534  LYS A CG  1 
ATOM   3870  C  CD  . LYS A 1 542 ? 8.810   -32.075 30.462  1.00 27.67 ? 534  LYS A CD  1 
ATOM   3871  C  CE  . LYS A 1 542 ? 9.893   -32.894 29.773  1.00 32.92 ? 534  LYS A CE  1 
ATOM   3872  N  NZ  . LYS A 1 542 ? 10.177  -34.198 30.463  1.00 31.12 ? 534  LYS A NZ  1 
ATOM   3873  N  N   . ARG A 1 543 ? 8.878   -29.310 34.583  1.00 18.16 ? 535  ARG A N   1 
ATOM   3874  C  CA  . ARG A 1 543 ? 7.748   -28.810 35.350  1.00 17.24 ? 535  ARG A CA  1 
ATOM   3875  C  C   . ARG A 1 543 ? 8.111   -27.584 36.183  1.00 13.34 ? 535  ARG A C   1 
ATOM   3876  O  O   . ARG A 1 543 ? 7.273   -27.105 36.952  1.00 17.31 ? 535  ARG A O   1 
ATOM   3877  C  CB  . ARG A 1 543 ? 7.180   -29.929 36.239  1.00 14.16 ? 535  ARG A CB  1 
ATOM   3878  C  CG  . ARG A 1 543 ? 6.856   -31.213 35.459  1.00 16.23 ? 535  ARG A CG  1 
ATOM   3879  C  CD  . ARG A 1 543 ? 5.984   -32.183 36.249  1.00 17.98 ? 535  ARG A CD  1 
ATOM   3880  N  NE  . ARG A 1 543 ? 4.633   -31.655 36.393  1.00 21.14 ? 535  ARG A NE  1 
ATOM   3881  C  CZ  . ARG A 1 543 ? 3.569   -32.361 36.771  1.00 21.79 ? 535  ARG A CZ  1 
ATOM   3882  N  NH1 . ARG A 1 543 ? 3.672   -33.655 37.044  1.00 22.60 ? 535  ARG A NH1 1 
ATOM   3883  N  NH2 . ARG A 1 543 ? 2.391   -31.761 36.859  1.00 22.46 ? 535  ARG A NH2 1 
ATOM   3884  N  N   . GLY A 1 544 ? 9.332   -27.064 36.043  1.00 13.09 ? 536  GLY A N   1 
ATOM   3885  C  CA  . GLY A 1 544 ? 9.700   -25.771 36.604  1.00 12.04 ? 536  GLY A CA  1 
ATOM   3886  C  C   . GLY A 1 544 ? 10.264  -25.816 38.017  1.00 14.88 ? 536  GLY A C   1 
ATOM   3887  O  O   . GLY A 1 544 ? 11.112  -24.992 38.361  1.00 14.53 ? 536  GLY A O   1 
ATOM   3888  N  N   . ALA A 1 545 ? 9.797   -26.746 38.846  1.00 16.44 ? 537  ALA A N   1 
ATOM   3889  C  CA  . ALA A 1 545 ? 10.384  -26.996 40.156  1.00 14.90 ? 537  ALA A CA  1 
ATOM   3890  C  C   . ALA A 1 545 ? 10.131  -28.453 40.521  1.00 17.64 ? 537  ALA A C   1 
ATOM   3891  O  O   . ALA A 1 545 ? 9.138   -29.054 40.102  1.00 17.63 ? 537  ALA A O   1 
ATOM   3892  C  CB  . ALA A 1 545 ? 9.811   -26.067 41.245  1.00 11.42 ? 537  ALA A CB  1 
ATOM   3893  N  N   . TYR A 1 546 ? 11.043  -29.017 41.304  1.00 13.61 ? 538  TYR A N   1 
ATOM   3894  C  CA  . TYR A 1 546 ? 10.964  -30.423 41.680  1.00 15.80 ? 538  TYR A CA  1 
ATOM   3895  C  C   . TYR A 1 546 ? 11.832  -30.606 42.906  1.00 17.06 ? 538  TYR A C   1 
ATOM   3896  O  O   . TYR A 1 546 ? 12.651  -29.749 43.243  1.00 16.44 ? 538  TYR A O   1 
ATOM   3897  C  CB  . TYR A 1 546 ? 11.432  -31.354 40.546  1.00 14.43 ? 538  TYR A CB  1 
ATOM   3898  C  CG  . TYR A 1 546 ? 12.874  -31.094 40.125  1.00 15.03 ? 538  TYR A CG  1 
ATOM   3899  C  CD1 . TYR A 1 546 ? 13.194  -30.024 39.292  1.00 12.85 ? 538  TYR A CD1 1 
ATOM   3900  C  CD2 . TYR A 1 546 ? 13.909  -31.908 40.570  1.00 16.62 ? 538  TYR A CD2 1 
ATOM   3901  C  CE1 . TYR A 1 546 ? 14.504  -29.773 38.912  1.00 12.54 ? 538  TYR A CE1 1 
ATOM   3902  C  CE2 . TYR A 1 546 ? 15.224  -31.661 40.204  1.00 17.02 ? 538  TYR A CE2 1 
ATOM   3903  C  CZ  . TYR A 1 546 ? 15.511  -30.592 39.373  1.00 16.98 ? 538  TYR A CZ  1 
ATOM   3904  O  OH  . TYR A 1 546 ? 16.809  -30.342 39.005  1.00 17.72 ? 538  TYR A OH  1 
ATOM   3905  N  N   . VAL A 1 547 ? 11.641  -31.738 43.575  1.00 17.62 ? 539  VAL A N   1 
ATOM   3906  C  CA  . VAL A 1 547 ? 12.465  -32.071 44.730  1.00 19.26 ? 539  VAL A CA  1 
ATOM   3907  C  C   . VAL A 1 547 ? 13.782  -32.650 44.219  1.00 19.93 ? 539  VAL A C   1 
ATOM   3908  O  O   . VAL A 1 547 ? 13.828  -33.771 43.706  1.00 20.55 ? 539  VAL A O   1 
ATOM   3909  C  CB  . VAL A 1 547 ? 11.749  -33.046 45.665  1.00 16.53 ? 539  VAL A CB  1 
ATOM   3910  C  CG1 . VAL A 1 547 ? 12.643  -33.399 46.837  1.00 18.17 ? 539  VAL A CG1 1 
ATOM   3911  C  CG2 . VAL A 1 547 ? 10.430  -32.442 46.150  1.00 16.98 ? 539  VAL A CG2 1 
ATOM   3912  N  N   . ILE A 1 548 ? 14.859  -31.881 44.354  1.00 16.36 ? 540  ILE A N   1 
ATOM   3913  C  CA  . ILE A 1 548 ? 16.170  -32.361 43.933  1.00 17.52 ? 540  ILE A CA  1 
ATOM   3914  C  C   . ILE A 1 548 ? 16.894  -33.121 45.043  1.00 21.33 ? 540  ILE A C   1 
ATOM   3915  O  O   . ILE A 1 548 ? 17.781  -33.935 44.752  1.00 23.75 ? 540  ILE A O   1 
ATOM   3916  C  CB  . ILE A 1 548 ? 17.016  -31.184 43.408  1.00 18.17 ? 540  ILE A CB  1 
ATOM   3917  C  CG1 . ILE A 1 548 ? 18.264  -31.701 42.667  1.00 20.49 ? 540  ILE A CG1 1 
ATOM   3918  C  CG2 . ILE A 1 548 ? 17.379  -30.226 44.539  1.00 14.68 ? 540  ILE A CG2 1 
ATOM   3919  C  CD1 . ILE A 1 548 ? 18.966  -30.652 41.861  1.00 25.09 ? 540  ILE A CD1 1 
ATOM   3920  N  N   . SER A 1 549 ? 16.507  -32.930 46.304  1.00 20.76 ? 541  SER A N   1 
ATOM   3921  C  CA  . SER A 1 549 ? 17.116  -33.680 47.402  1.00 23.87 ? 541  SER A CA  1 
ATOM   3922  C  C   . SER A 1 549 ? 16.080  -33.798 48.516  1.00 22.63 ? 541  SER A C   1 
ATOM   3923  O  O   . SER A 1 549 ? 15.825  -32.823 49.229  1.00 21.95 ? 541  SER A O   1 
ATOM   3924  C  CB  . SER A 1 549 ? 18.383  -32.991 47.886  1.00 25.01 ? 541  SER A CB  1 
ATOM   3925  O  OG  . SER A 1 549 ? 19.053  -33.797 48.840  1.00 30.98 ? 541  SER A OG  1 
ATOM   3926  N  N   . GLU A 1 550 ? 15.477  -34.974 48.656  1.00 20.60 ? 542  GLU A N   1 
ATOM   3927  C  CA  . GLU A 1 550 ? 14.471  -35.118 49.697  1.00 26.08 ? 542  GLU A CA  1 
ATOM   3928  C  C   . GLU A 1 550 ? 15.130  -35.149 51.073  1.00 24.62 ? 542  GLU A C   1 
ATOM   3929  O  O   . GLU A 1 550 ? 16.321  -35.432 51.219  1.00 21.52 ? 542  GLU A O   1 
ATOM   3930  C  CB  . GLU A 1 550 ? 13.615  -36.374 49.478  1.00 31.17 ? 542  GLU A CB  1 
ATOM   3931  C  CG  . GLU A 1 550 ? 12.326  -36.452 50.350  1.00 34.61 ? 542  GLU A CG  1 
ATOM   3932  C  CD  . GLU A 1 550 ? 11.638  -35.090 50.587  1.00 29.87 ? 542  GLU A CD  1 
ATOM   3933  O  OE1 . GLU A 1 550 ? 11.563  -34.275 49.648  1.00 42.23 ? 542  GLU A OE1 1 
ATOM   3934  O  OE2 . GLU A 1 550 ? 11.177  -34.824 51.716  1.00 24.91 ? 542  GLU A OE2 1 
ATOM   3935  N  N   . ALA A 1 551 ? 14.342  -34.804 52.085  1.00 22.76 ? 543  ALA A N   1 
ATOM   3936  C  CA  . ALA A 1 551 ? 14.801  -34.902 53.459  1.00 27.89 ? 543  ALA A CA  1 
ATOM   3937  C  C   . ALA A 1 551 ? 15.044  -36.358 53.833  1.00 29.19 ? 543  ALA A C   1 
ATOM   3938  O  O   . ALA A 1 551 ? 14.373  -37.269 53.347  1.00 27.47 ? 543  ALA A O   1 
ATOM   3939  C  CB  . ALA A 1 551 ? 13.778  -34.282 54.410  1.00 29.08 ? 543  ALA A CB  1 
ATOM   3940  N  N   . GLN A 1 552 ? 16.044  -36.575 54.680  1.00 32.21 ? 544  GLN A N   1 
ATOM   3941  C  CA  . GLN A 1 552 ? 16.263  -37.880 55.299  1.00 35.48 ? 544  GLN A CA  1 
ATOM   3942  C  C   . GLN A 1 552 ? 15.479  -37.862 56.606  1.00 34.00 ? 544  GLN A C   1 
ATOM   3943  O  O   . GLN A 1 552 ? 15.958  -37.356 57.624  1.00 37.29 ? 544  GLN A O   1 
ATOM   3944  C  CB  . GLN A 1 552 ? 17.752  -38.139 55.512  1.00 39.51 ? 544  GLN A CB  1 
ATOM   3945  N  N   . GLY A 1 553 ? 14.263  -38.389 56.567  1.00 31.47 ? 545  GLY A N   1 
ATOM   3946  C  CA  . GLY A 1 553 ? 13.296  -38.261 57.641  1.00 32.25 ? 545  GLY A CA  1 
ATOM   3947  C  C   . GLY A 1 553 ? 12.163  -37.340 57.224  1.00 34.45 ? 545  GLY A C   1 
ATOM   3948  O  O   . GLY A 1 553 ? 12.079  -36.890 56.078  1.00 38.03 ? 545  GLY A O   1 
ATOM   3949  N  N   . ASN A 1 554 ? 11.278  -37.055 58.180  1.00 33.02 ? 546  ASN A N   1 
ATOM   3950  C  CA  . ASN A 1 554 ? 10.174  -36.135 57.917  1.00 34.23 ? 546  ASN A CA  1 
ATOM   3951  C  C   . ASN A 1 554 ? 10.707  -34.714 57.776  1.00 31.29 ? 546  ASN A C   1 
ATOM   3952  O  O   . ASN A 1 554 ? 11.361  -34.196 58.687  1.00 30.32 ? 546  ASN A O   1 
ATOM   3953  C  CB  . ASN A 1 554 ? 9.133   -36.202 59.028  1.00 39.57 ? 546  ASN A CB  1 
ATOM   3954  C  CG  . ASN A 1 554 ? 8.238   -37.421 58.913  1.00 50.02 ? 546  ASN A CG  1 
ATOM   3955  O  OD1 . ASN A 1 554 ? 8.409   -38.253 58.018  1.00 48.63 ? 546  ASN A OD1 1 
ATOM   3956  N  ND2 . ASN A 1 554 ? 7.279   -37.538 59.826  1.00 56.78 ? 546  ASN A ND2 1 
ATOM   3957  N  N   . ALA A 1 555 ? 10.421  -34.086 56.640  1.00 33.79 ? 547  ALA A N   1 
ATOM   3958  C  CA  . ALA A 1 555 ? 10.904  -32.735 56.391  1.00 28.11 ? 547  ALA A CA  1 
ATOM   3959  C  C   . ALA A 1 555 ? 10.346  -31.758 57.420  1.00 29.53 ? 547  ALA A C   1 
ATOM   3960  O  O   . ALA A 1 555 ? 9.143   -31.743 57.698  1.00 32.63 ? 547  ALA A O   1 
ATOM   3961  C  CB  . ALA A 1 555 ? 10.521  -32.293 54.978  1.00 25.49 ? 547  ALA A CB  1 
ATOM   3962  N  N   . GLN A 1 556 ? 11.232  -30.954 58.003  1.00 25.46 ? 548  GLN A N   1 
ATOM   3963  C  CA  . GLN A 1 556 ? 10.838  -29.862 58.879  1.00 26.48 ? 548  GLN A CA  1 
ATOM   3964  C  C   . GLN A 1 556 ? 10.756  -28.527 58.153  1.00 28.32 ? 548  GLN A C   1 
ATOM   3965  O  O   . GLN A 1 556 ? 10.175  -27.580 58.691  1.00 26.51 ? 548  GLN A O   1 
ATOM   3966  C  CB  . GLN A 1 556 ? 11.813  -29.754 60.058  1.00 26.04 ? 548  GLN A CB  1 
ATOM   3967  C  CG  . GLN A 1 556 ? 11.903  -31.052 60.867  1.00 39.70 ? 548  GLN A CG  1 
ATOM   3968  C  CD  . GLN A 1 556 ? 13.030  -31.050 61.874  1.00 46.58 ? 548  GLN A CD  1 
ATOM   3969  O  OE1 . GLN A 1 556 ? 13.825  -31.991 61.932  1.00 51.24 ? 548  GLN A OE1 1 
ATOM   3970  N  NE2 . GLN A 1 556 ? 13.097  -30.001 62.690  1.00 45.33 ? 548  GLN A NE2 1 
ATOM   3971  N  N   . ALA A 1 557 ? 11.312  -28.434 56.951  1.00 22.73 ? 549  ALA A N   1 
ATOM   3972  C  CA  . ALA A 1 557 ? 11.213  -27.234 56.132  1.00 21.15 ? 549  ALA A CA  1 
ATOM   3973  C  C   . ALA A 1 557 ? 11.656  -27.606 54.729  1.00 20.35 ? 549  ALA A C   1 
ATOM   3974  O  O   . ALA A 1 557 ? 12.160  -28.706 54.488  1.00 21.22 ? 549  ALA A O   1 
ATOM   3975  C  CB  . ALA A 1 557 ? 12.062  -26.079 56.680  1.00 25.28 ? 549  ALA A CB  1 
ATOM   3976  N  N   . VAL A 1 558 ? 11.467  -26.671 53.802  1.00 19.61 ? 550  VAL A N   1 
ATOM   3977  C  CA  . VAL A 1 558 ? 11.915  -26.845 52.429  1.00 18.76 ? 550  VAL A CA  1 
ATOM   3978  C  C   . VAL A 1 558 ? 12.737  -25.627 52.033  1.00 21.83 ? 550  VAL A C   1 
ATOM   3979  O  O   . VAL A 1 558 ? 12.326  -24.481 52.258  1.00 18.30 ? 550  VAL A O   1 
ATOM   3980  C  CB  . VAL A 1 558 ? 10.740  -27.068 51.452  1.00 22.64 ? 550  VAL A CB  1 
ATOM   3981  C  CG1 . VAL A 1 558 ? 9.657   -26.046 51.662  1.00 22.90 ? 550  VAL A CG1 1 
ATOM   3982  C  CG2 . VAL A 1 558 ? 11.227  -27.036 49.985  1.00 18.35 ? 550  VAL A CG2 1 
ATOM   3983  N  N   . ILE A 1 559 ? 13.911  -25.879 51.473  1.00 17.56 ? 551  ILE A N   1 
ATOM   3984  C  CA  . ILE A 1 559 ? 14.747  -24.841 50.893  1.00 15.95 ? 551  ILE A CA  1 
ATOM   3985  C  C   . ILE A 1 559 ? 14.453  -24.806 49.398  1.00 15.62 ? 551  ILE A C   1 
ATOM   3986  O  O   . ILE A 1 559 ? 14.612  -25.822 48.707  1.00 19.14 ? 551  ILE A O   1 
ATOM   3987  C  CB  . ILE A 1 559 ? 16.241  -25.104 51.160  1.00 16.81 ? 551  ILE A CB  1 
ATOM   3988  C  CG1 . ILE A 1 559 ? 16.518  -25.307 52.659  1.00 22.47 ? 551  ILE A CG1 1 
ATOM   3989  C  CG2 . ILE A 1 559 ? 17.075  -23.946 50.620  1.00 17.13 ? 551  ILE A CG2 1 
ATOM   3990  C  CD1 . ILE A 1 559 ? 18.017  -25.466 53.005  1.00 18.62 ? 551  ILE A CD1 1 
ATOM   3991  N  N   . ILE A 1 560 ? 13.989  -23.660 48.900  1.00 14.16 ? 552  ILE A N   1 
ATOM   3992  C  CA  . ILE A 1 560 ? 13.788  -23.443 47.469  1.00 16.38 ? 552  ILE A CA  1 
ATOM   3993  C  C   . ILE A 1 560 ? 15.004  -22.695 46.950  1.00 17.78 ? 552  ILE A C   1 
ATOM   3994  O  O   . ILE A 1 560 ? 15.338  -21.625 47.469  1.00 17.52 ? 552  ILE A O   1 
ATOM   3995  C  CB  . ILE A 1 560 ? 12.514  -22.633 47.188  1.00 15.98 ? 552  ILE A CB  1 
ATOM   3996  C  CG1 . ILE A 1 560 ? 11.293  -23.273 47.843  1.00 19.01 ? 552  ILE A CG1 1 
ATOM   3997  C  CG2 . ILE A 1 560 ? 12.296  -22.473 45.667  1.00 12.03 ? 552  ILE A CG2 1 
ATOM   3998  C  CD1 . ILE A 1 560 ? 10.103  -22.354 47.802  1.00 14.56 ? 552  ILE A CD1 1 
ATOM   3999  N  N   . ALA A 1 561 ? 15.668  -23.237 45.932  1.00 12.38 ? 553  ALA A N   1 
ATOM   4000  C  CA  . ALA A 1 561 ? 16.821  -22.559 45.364  1.00 12.16 ? 553  ALA A CA  1 
ATOM   4001  C  C   . ALA A 1 561 ? 16.763  -22.644 43.851  1.00 13.45 ? 553  ALA A C   1 
ATOM   4002  O  O   . ALA A 1 561 ? 16.112  -23.522 43.278  1.00 13.02 ? 553  ALA A O   1 
ATOM   4003  C  CB  . ALA A 1 561 ? 18.146  -23.150 45.873  1.00 12.94 ? 553  ALA A CB  1 
ATOM   4004  N  N   . THR A 1 562 ? 17.454  -21.708 43.211  1.00 14.06 ? 554  THR A N   1 
ATOM   4005  C  CA  . THR A 1 562 ? 17.557  -21.657 41.761  1.00 10.51 ? 554  THR A CA  1 
ATOM   4006  C  C   . THR A 1 562 ? 19.016  -21.503 41.350  1.00 14.01 ? 554  THR A C   1 
ATOM   4007  O  O   . THR A 1 562 ? 19.850  -21.009 42.116  1.00 11.32 ? 554  THR A O   1 
ATOM   4008  C  CB  . THR A 1 562 ? 16.785  -20.474 41.179  1.00 16.00 ? 554  THR A CB  1 
ATOM   4009  O  OG1 . THR A 1 562 ? 17.544  -19.285 41.433  1.00 15.56 ? 554  THR A OG1 1 
ATOM   4010  C  CG2 . THR A 1 562 ? 15.398  -20.339 41.838  1.00 11.57 ? 554  THR A CG2 1 
ATOM   4011  N  N   . GLY A 1 563 ? 19.295  -21.902 40.108  1.00 12.65 ? 555  GLY A N   1 
ATOM   4012  C  CA  . GLY A 1 563 ? 20.554  -21.555 39.458  1.00 15.04 ? 555  GLY A CA  1 
ATOM   4013  C  C   . GLY A 1 563 ? 21.782  -21.825 40.307  1.00 13.69 ? 555  GLY A C   1 
ATOM   4014  O  O   . GLY A 1 563 ? 21.951  -22.905 40.861  1.00 12.98 ? 555  GLY A O   1 
ATOM   4015  N  N   . SER A 1 564 ? 22.650  -20.812 40.420  1.00 13.03 ? 556  SER A N   1 
ATOM   4016  C  CA  . SER A 1 564 ? 23.916  -20.967 41.127  1.00 16.46 ? 556  SER A CA  1 
ATOM   4017  C  C   . SER A 1 564 ? 23.757  -21.251 42.620  1.00 17.13 ? 556  SER A C   1 
ATOM   4018  O  O   . SER A 1 564 ? 24.752  -21.594 43.269  1.00 14.80 ? 556  SER A O   1 
ATOM   4019  C  CB  . SER A 1 564 ? 24.776  -19.703 40.925  1.00 12.69 ? 556  SER A CB  1 
ATOM   4020  O  OG  . SER A 1 564 ? 24.060  -18.517 41.258  1.00 15.37 ? 556  SER A OG  1 
ATOM   4021  N  N   . GLU A 1 565 ? 22.554  -21.139 43.189  1.00 10.44 ? 557  GLU A N   1 
ATOM   4022  C  CA  . GLU A 1 565 ? 22.399  -21.311 44.632  1.00 10.89 ? 557  GLU A CA  1 
ATOM   4023  C  C   . GLU A 1 565 ? 21.932  -22.700 45.028  1.00 13.68 ? 557  GLU A C   1 
ATOM   4024  O  O   . GLU A 1 565 ? 21.824  -22.980 46.224  1.00 14.40 ? 557  GLU A O   1 
ATOM   4025  C  CB  . GLU A 1 565 ? 21.444  -20.251 45.212  1.00 12.57 ? 557  GLU A CB  1 
ATOM   4026  C  CG  . GLU A 1 565 ? 22.122  -18.904 45.439  1.00 10.35 ? 557  GLU A CG  1 
ATOM   4027  C  CD  . GLU A 1 565 ? 22.616  -18.288 44.129  1.00 15.92 ? 557  GLU A CD  1 
ATOM   4028  O  OE1 . GLU A 1 565 ? 21.748  -17.810 43.373  1.00 13.56 ? 557  GLU A OE1 1 
ATOM   4029  O  OE2 . GLU A 1 565 ? 23.851  -18.306 43.852  1.00 12.55 ? 557  GLU A OE2 1 
ATOM   4030  N  N   . VAL A 1 566 ? 21.675  -23.589 44.069  1.00 14.07 ? 558  VAL A N   1 
ATOM   4031  C  CA  . VAL A 1 566 ? 21.242  -24.930 44.443  1.00 15.32 ? 558  VAL A CA  1 
ATOM   4032  C  C   . VAL A 1 566 ? 22.329  -25.645 45.242  1.00 14.08 ? 558  VAL A C   1 
ATOM   4033  O  O   . VAL A 1 566 ? 22.041  -26.294 46.257  1.00 16.73 ? 558  VAL A O   1 
ATOM   4034  C  CB  . VAL A 1 566 ? 20.830  -25.729 43.197  1.00 15.46 ? 558  VAL A CB  1 
ATOM   4035  C  CG1 . VAL A 1 566 ? 20.575  -27.180 43.573  1.00 17.18 ? 558  VAL A CG1 1 
ATOM   4036  C  CG2 . VAL A 1 566 ? 19.581  -25.100 42.586  1.00 13.52 ? 558  VAL A CG2 1 
ATOM   4037  N  N   . GLY A 1 567 ? 23.587  -25.548 44.799  1.00 17.31 ? 559  GLY A N   1 
ATOM   4038  C  CA  . GLY A 1 567 ? 24.670  -26.196 45.536  1.00 19.06 ? 559  GLY A CA  1 
ATOM   4039  C  C   . GLY A 1 567 ? 24.737  -25.741 46.984  1.00 20.13 ? 559  GLY A C   1 
ATOM   4040  O  O   . GLY A 1 567 ? 24.869  -26.555 47.910  1.00 16.06 ? 559  GLY A O   1 
ATOM   4041  N  N   . LEU A 1 568 ? 24.630  -24.431 47.196  1.00 20.40 ? 560  LEU A N   1 
ATOM   4042  C  CA  . LEU A 1 568 ? 24.601  -23.879 48.547  1.00 18.12 ? 560  LEU A CA  1 
ATOM   4043  C  C   . LEU A 1 568 ? 23.463  -24.479 49.364  1.00 16.26 ? 560  LEU A C   1 
ATOM   4044  O  O   . LEU A 1 568 ? 23.643  -24.866 50.526  1.00 15.07 ? 560  LEU A O   1 
ATOM   4045  C  CB  . LEU A 1 568 ? 24.464  -22.359 48.455  1.00 13.57 ? 560  LEU A CB  1 
ATOM   4046  C  CG  . LEU A 1 568 ? 24.222  -21.589 49.753  1.00 21.31 ? 560  LEU A CG  1 
ATOM   4047  C  CD1 . LEU A 1 568 ? 25.365  -21.814 50.735  1.00 20.51 ? 560  LEU A CD1 1 
ATOM   4048  C  CD2 . LEU A 1 568 ? 24.074  -20.108 49.432  1.00 22.01 ? 560  LEU A CD2 1 
ATOM   4049  N  N   . ALA A 1 569 ? 22.277  -24.573 48.767  1.00 14.93 ? 561  ALA A N   1 
ATOM   4050  C  CA  . ALA A 1 569 ? 21.144  -25.161 49.480  1.00 15.75 ? 561  ALA A CA  1 
ATOM   4051  C  C   . ALA A 1 569 ? 21.407  -26.618 49.847  1.00 22.27 ? 561  ALA A C   1 
ATOM   4052  O  O   . ALA A 1 569 ? 21.087  -27.051 50.963  1.00 19.02 ? 561  ALA A O   1 
ATOM   4053  C  CB  . ALA A 1 569 ? 19.879  -25.040 48.634  1.00 13.64 ? 561  ALA A CB  1 
ATOM   4054  N  N   . VAL A 1 570 ? 21.980  -27.393 48.920  1.00 18.09 ? 562  VAL A N   1 
ATOM   4055  C  CA  . VAL A 1 570 ? 22.269  -28.798 49.209  1.00 17.86 ? 562  VAL A CA  1 
ATOM   4056  C  C   . VAL A 1 570 ? 23.281  -28.912 50.344  1.00 18.54 ? 562  VAL A C   1 
ATOM   4057  O  O   . VAL A 1 570 ? 23.156  -29.773 51.229  1.00 21.02 ? 562  VAL A O   1 
ATOM   4058  C  CB  . VAL A 1 570 ? 22.749  -29.520 47.933  1.00 18.74 ? 562  VAL A CB  1 
ATOM   4059  C  CG1 . VAL A 1 570 ? 23.213  -30.946 48.255  1.00 22.77 ? 562  VAL A CG1 1 
ATOM   4060  C  CG2 . VAL A 1 570 ? 21.613  -29.570 46.913  1.00 20.28 ? 562  VAL A CG2 1 
ATOM   4061  N  N   . GLU A 1 571 ? 24.292  -28.039 50.347  1.00 17.70 ? 563  GLU A N   1 
ATOM   4062  C  CA  . GLU A 1 571 ? 25.286  -28.081 51.416  1.00 19.46 ? 563  GLU A CA  1 
ATOM   4063  C  C   . GLU A 1 571 ? 24.657  -27.721 52.757  1.00 20.76 ? 563  GLU A C   1 
ATOM   4064  O  O   . GLU A 1 571 ? 24.962  -28.347 53.777  1.00 20.34 ? 563  GLU A O   1 
ATOM   4065  C  CB  . GLU A 1 571 ? 26.451  -27.147 51.085  1.00 22.47 ? 563  GLU A CB  1 
ATOM   4066  N  N   . ALA A 1 572 ? 23.743  -26.747 52.766  1.00 17.28 ? 564  ALA A N   1 
ATOM   4067  C  CA  . ALA A 1 572 ? 23.032  -26.405 53.999  1.00 20.18 ? 564  ALA A CA  1 
ATOM   4068  C  C   . ALA A 1 572 ? 22.165  -27.563 54.482  1.00 19.99 ? 564  ALA A C   1 
ATOM   4069  O  O   . ALA A 1 572 ? 22.069  -27.820 55.692  1.00 20.27 ? 564  ALA A O   1 
ATOM   4070  C  CB  . ALA A 1 572 ? 22.189  -25.146 53.785  1.00 18.95 ? 564  ALA A CB  1 
ATOM   4071  N  N   . GLN A 1 573 ? 21.535  -28.289 53.554  1.00 20.87 ? 565  GLN A N   1 
ATOM   4072  C  CA  . GLN A 1 573 ? 20.745  -29.452 53.954  1.00 20.10 ? 565  GLN A CA  1 
ATOM   4073  C  C   . GLN A 1 573 ? 21.601  -30.478 54.684  1.00 23.38 ? 565  GLN A C   1 
ATOM   4074  O  O   . GLN A 1 573 ? 21.169  -31.062 55.690  1.00 21.09 ? 565  GLN A O   1 
ATOM   4075  C  CB  . GLN A 1 573 ? 20.088  -30.089 52.728  1.00 21.51 ? 565  GLN A CB  1 
ATOM   4076  C  CG  . GLN A 1 573 ? 19.386  -31.402 53.023  1.00 21.91 ? 565  GLN A CG  1 
ATOM   4077  C  CD  . GLN A 1 573 ? 19.038  -32.162 51.755  1.00 24.88 ? 565  GLN A CD  1 
ATOM   4078  O  OE1 . GLN A 1 573 ? 19.853  -32.258 50.833  1.00 20.65 ? 565  GLN A OE1 1 
ATOM   4079  N  NE2 . GLN A 1 573 ? 17.819  -32.693 51.697  1.00 20.31 ? 565  GLN A NE2 1 
ATOM   4080  N  N   . LYS A 1 574 ? 22.817  -30.719 54.186  1.00 24.91 ? 566  LYS A N   1 
ATOM   4081  C  CA  . LYS A 1 574 ? 23.697  -31.688 54.834  1.00 25.48 ? 566  LYS A CA  1 
ATOM   4082  C  C   . LYS A 1 574 ? 24.100  -31.218 56.226  1.00 25.92 ? 566  LYS A C   1 
ATOM   4083  O  O   . LYS A 1 574 ? 24.110  -32.012 57.178  1.00 23.48 ? 566  LYS A O   1 
ATOM   4084  C  CB  . LYS A 1 574 ? 24.938  -31.944 53.971  1.00 23.99 ? 566  LYS A CB  1 
ATOM   4085  N  N   . VAL A 1 575 ? 24.430  -29.929 56.367  1.00 21.66 ? 567  VAL A N   1 
ATOM   4086  C  CA  . VAL A 1 575 ? 24.799  -29.408 57.682  1.00 26.61 ? 567  VAL A CA  1 
ATOM   4087  C  C   . VAL A 1 575 ? 23.620  -29.507 58.639  1.00 24.85 ? 567  VAL A C   1 
ATOM   4088  O  O   . VAL A 1 575 ? 23.776  -29.892 59.802  1.00 24.21 ? 567  VAL A O   1 
ATOM   4089  C  CB  . VAL A 1 575 ? 25.314  -27.963 57.565  1.00 24.54 ? 567  VAL A CB  1 
ATOM   4090  C  CG1 . VAL A 1 575 ? 25.448  -27.333 58.949  1.00 23.82 ? 567  VAL A CG1 1 
ATOM   4091  C  CG2 . VAL A 1 575 ? 26.655  -27.940 56.835  1.00 22.31 ? 567  VAL A CG2 1 
ATOM   4092  N  N   . LEU A 1 576 ? 22.419  -29.180 58.156  1.00 24.01 ? 568  LEU A N   1 
ATOM   4093  C  CA  . LEU A 1 576 ? 21.224  -29.282 58.987  1.00 26.55 ? 568  LEU A CA  1 
ATOM   4094  C  C   . LEU A 1 576 ? 20.954  -30.724 59.394  1.00 28.85 ? 568  LEU A C   1 
ATOM   4095  O  O   . LEU A 1 576 ? 20.593  -30.992 60.548  1.00 33.12 ? 568  LEU A O   1 
ATOM   4096  C  CB  . LEU A 1 576 ? 20.023  -28.689 58.246  1.00 23.89 ? 568  LEU A CB  1 
ATOM   4097  C  CG  . LEU A 1 576 ? 19.983  -27.161 58.183  1.00 21.79 ? 568  LEU A CG  1 
ATOM   4098  C  CD1 . LEU A 1 576 ? 19.098  -26.688 57.035  1.00 25.03 ? 568  LEU A CD1 1 
ATOM   4099  C  CD2 . LEU A 1 576 ? 19.512  -26.589 59.512  1.00 23.66 ? 568  LEU A CD2 1 
ATOM   4100  N  N   . ALA A 1 577 ? 21.129  -31.669 58.465  1.00 23.58 ? 569  ALA A N   1 
ATOM   4101  C  CA  . ALA A 1 577 ? 20.906  -33.077 58.792  1.00 25.93 ? 569  ALA A CA  1 
ATOM   4102  C  C   . ALA A 1 577 ? 21.844  -33.539 59.903  1.00 34.09 ? 569  ALA A C   1 
ATOM   4103  O  O   . ALA A 1 577 ? 21.421  -34.240 60.832  1.00 32.13 ? 569  ALA A O   1 
ATOM   4104  C  CB  . ALA A 1 577 ? 21.081  -33.949 57.546  1.00 24.31 ? 569  ALA A CB  1 
ATOM   4105  N  N   . GLY A 1 578 ? 23.118  -33.147 59.830  1.00 28.55 ? 570  GLY A N   1 
ATOM   4106  C  CA  . GLY A 1 578 ? 24.092  -33.452 60.869  1.00 27.53 ? 570  GLY A CA  1 
ATOM   4107  C  C   . GLY A 1 578 ? 23.763  -32.854 62.223  1.00 30.69 ? 570  GLY A C   1 
ATOM   4108  O  O   . GLY A 1 578 ? 24.359  -33.262 63.226  1.00 35.91 ? 570  GLY A O   1 
ATOM   4109  N  N   . GLN A 1 579 ? 22.839  -31.898 62.271  1.00 28.82 ? 571  GLN A N   1 
ATOM   4110  C  CA  . GLN A 1 579 ? 22.323  -31.340 63.510  1.00 32.24 ? 571  GLN A CA  1 
ATOM   4111  C  C   . GLN A 1 579 ? 20.973  -31.931 63.884  1.00 34.70 ? 571  GLN A C   1 
ATOM   4112  O  O   . GLN A 1 579 ? 20.329  -31.438 64.814  1.00 38.56 ? 571  GLN A O   1 
ATOM   4113  C  CB  . GLN A 1 579 ? 22.212  -29.820 63.400  1.00 31.42 ? 571  GLN A CB  1 
ATOM   4114  C  CG  . GLN A 1 579 ? 23.537  -29.122 63.182  1.00 37.25 ? 571  GLN A CG  1 
ATOM   4115  C  CD  . GLN A 1 579 ? 23.396  -27.617 63.188  1.00 45.61 ? 571  GLN A CD  1 
ATOM   4116  O  OE1 . GLN A 1 579 ? 22.380  -27.082 63.628  1.00 45.37 ? 571  GLN A OE1 1 
ATOM   4117  N  NE2 . GLN A 1 579 ? 24.416  -26.923 62.701  1.00 46.93 ? 571  GLN A NE2 1 
ATOM   4118  N  N   . GLY A 1 580 ? 20.533  -32.971 63.179  1.00 34.88 ? 572  GLY A N   1 
ATOM   4119  C  CA  . GLY A 1 580 ? 19.244  -33.579 63.447  1.00 32.49 ? 572  GLY A CA  1 
ATOM   4120  C  C   . GLY A 1 580 ? 18.054  -32.786 62.960  1.00 30.78 ? 572  GLY A C   1 
ATOM   4121  O  O   . GLY A 1 580 ? 16.966  -32.916 63.523  1.00 31.47 ? 572  GLY A O   1 
ATOM   4122  N  N   . ILE A 1 581 ? 18.229  -31.963 61.926  1.00 28.34 ? 573  ILE A N   1 
ATOM   4123  C  CA  . ILE A 1 581 ? 17.165  -31.132 61.372  1.00 29.85 ? 573  ILE A CA  1 
ATOM   4124  C  C   . ILE A 1 581 ? 16.999  -31.520 59.910  1.00 28.80 ? 573  ILE A C   1 
ATOM   4125  O  O   . ILE A 1 581 ? 17.862  -31.211 59.079  1.00 25.34 ? 573  ILE A O   1 
ATOM   4126  C  CB  . ILE A 1 581 ? 17.470  -29.635 61.504  1.00 33.78 ? 573  ILE A CB  1 
ATOM   4127  C  CG1 . ILE A 1 581 ? 17.625  -29.247 62.978  1.00 36.60 ? 573  ILE A CG1 1 
ATOM   4128  C  CG2 . ILE A 1 581 ? 16.381  -28.813 60.819  1.00 35.30 ? 573  ILE A CG2 1 
ATOM   4129  C  CD1 . ILE A 1 581 ? 18.156  -27.841 63.184  1.00 37.43 ? 573  ILE A CD1 1 
ATOM   4130  N  N   . ALA A 1 582 ? 15.890  -32.182 59.594  1.00 26.16 ? 574  ALA A N   1 
ATOM   4131  C  CA  . ALA A 1 582 ? 15.651  -32.714 58.259  1.00 23.63 ? 574  ALA A CA  1 
ATOM   4132  C  C   . ALA A 1 582 ? 14.918  -31.681 57.411  1.00 22.38 ? 574  ALA A C   1 
ATOM   4133  O  O   . ALA A 1 582 ? 13.823  -31.237 57.775  1.00 24.12 ? 574  ALA A O   1 
ATOM   4134  C  CB  . ALA A 1 582 ? 14.836  -34.005 58.351  1.00 26.00 ? 574  ALA A CB  1 
ATOM   4135  N  N   . VAL A 1 583 ? 15.513  -31.304 56.274  1.00 24.01 ? 575  VAL A N   1 
ATOM   4136  C  CA  . VAL A 1 583 ? 14.861  -30.420 55.319  1.00 23.27 ? 575  VAL A CA  1 
ATOM   4137  C  C   . VAL A 1 583 ? 14.986  -31.022 53.928  1.00 21.04 ? 575  VAL A C   1 
ATOM   4138  O  O   . VAL A 1 583 ? 15.918  -31.778 53.635  1.00 20.32 ? 575  VAL A O   1 
ATOM   4139  C  CB  . VAL A 1 583 ? 15.437  -28.979 55.330  1.00 22.56 ? 575  VAL A CB  1 
ATOM   4140  C  CG1 . VAL A 1 583 ? 15.410  -28.386 56.743  1.00 20.39 ? 575  VAL A CG1 1 
ATOM   4141  C  CG2 . VAL A 1 583 ? 16.842  -28.936 54.726  1.00 21.07 ? 575  VAL A CG2 1 
ATOM   4142  N  N   . ARG A 1 584 ? 14.028  -30.682 53.076  1.00 18.84 ? 576  ARG A N   1 
ATOM   4143  C  CA  . ARG A 1 584 ? 14.040  -30.999 51.654  1.00 18.15 ? 576  ARG A CA  1 
ATOM   4144  C  C   . ARG A 1 584 ? 14.601  -29.822 50.864  1.00 20.84 ? 576  ARG A C   1 
ATOM   4145  O  O   . ARG A 1 584 ? 14.447  -28.666 51.263  1.00 20.19 ? 576  ARG A O   1 
ATOM   4146  C  CB  . ARG A 1 584 ? 12.616  -31.331 51.196  1.00 20.35 ? 576  ARG A CB  1 
ATOM   4147  C  CG  . ARG A 1 584 ? 12.193  -30.825 49.856  1.00 28.58 ? 576  ARG A CG  1 
ATOM   4148  C  CD  . ARG A 1 584 ? 10.665  -30.884 49.729  1.00 21.02 ? 576  ARG A CD  1 
ATOM   4149  N  NE  . ARG A 1 584 ? 10.130  -32.226 49.940  1.00 23.14 ? 576  ARG A NE  1 
ATOM   4150  C  CZ  . ARG A 1 584 ? 8.919   -32.600 49.539  1.00 26.58 ? 576  ARG A CZ  1 
ATOM   4151  N  NH1 . ARG A 1 584 ? 8.142   -31.728 48.911  1.00 19.95 ? 576  ARG A NH1 1 
ATOM   4152  N  NH2 . ARG A 1 584 ? 8.487   -33.835 49.751  1.00 25.86 ? 576  ARG A NH2 1 
ATOM   4153  N  N   . VAL A 1 585 ? 15.259  -30.115 49.741  1.00 16.55 ? 577  VAL A N   1 
ATOM   4154  C  CA  . VAL A 1 585 ? 15.719  -29.085 48.809  1.00 16.83 ? 577  VAL A CA  1 
ATOM   4155  C  C   . VAL A 1 585 ? 14.930  -29.210 47.513  1.00 16.40 ? 577  VAL A C   1 
ATOM   4156  O  O   . VAL A 1 585 ? 14.866  -30.296 46.919  1.00 18.26 ? 577  VAL A O   1 
ATOM   4157  C  CB  . VAL A 1 585 ? 17.228  -29.178 48.525  1.00 19.64 ? 577  VAL A CB  1 
ATOM   4158  C  CG1 . VAL A 1 585 ? 17.641  -28.055 47.559  1.00 15.54 ? 577  VAL A CG1 1 
ATOM   4159  C  CG2 . VAL A 1 585 ? 18.019  -29.074 49.807  1.00 19.74 ? 577  VAL A CG2 1 
ATOM   4160  N  N   . VAL A 1 586 ? 14.329  -28.100 47.089  1.00 14.41 ? 578  VAL A N   1 
ATOM   4161  C  CA  . VAL A 1 586 ? 13.601  -27.989 45.829  1.00 13.95 ? 578  VAL A CA  1 
ATOM   4162  C  C   . VAL A 1 586 ? 14.415  -27.103 44.899  1.00 15.13 ? 578  VAL A C   1 
ATOM   4163  O  O   . VAL A 1 586 ? 14.822  -26.002 45.284  1.00 16.31 ? 578  VAL A O   1 
ATOM   4164  C  CB  . VAL A 1 586 ? 12.190  -27.407 46.044  1.00 17.40 ? 578  VAL A CB  1 
ATOM   4165  C  CG1 . VAL A 1 586 ? 11.565  -26.933 44.725  1.00 13.68 ? 578  VAL A CG1 1 
ATOM   4166  C  CG2 . VAL A 1 586 ? 11.279  -28.441 46.704  1.00 14.90 ? 578  VAL A CG2 1 
ATOM   4167  N  N   . SER A 1 587 ? 14.676  -27.587 43.693  1.00 13.24 ? 579  SER A N   1 
ATOM   4168  C  CA  . SER A 1 587 ? 15.247  -26.755 42.646  1.00 15.23 ? 579  SER A CA  1 
ATOM   4169  C  C   . SER A 1 587 ? 14.093  -26.168 41.854  1.00 16.65 ? 579  SER A C   1 
ATOM   4170  O  O   . SER A 1 587 ? 13.180  -26.899 41.468  1.00 16.42 ? 579  SER A O   1 
ATOM   4171  C  CB  . SER A 1 587 ? 16.165  -27.571 41.733  1.00 12.34 ? 579  SER A CB  1 
ATOM   4172  O  OG  . SER A 1 587 ? 16.724  -26.735 40.729  1.00 13.24 ? 579  SER A OG  1 
ATOM   4173  N  N   . MET A 1 588 ? 14.114  -24.854 41.628  1.00 14.24 ? 580  MET A N   1 
ATOM   4174  C  CA  . MET A 1 588 ? 13.032  -24.172 40.916  1.00 13.14 ? 580  MET A CA  1 
ATOM   4175  C  C   . MET A 1 588 ? 13.608  -23.439 39.708  1.00 14.86 ? 580  MET A C   1 
ATOM   4176  O  O   . MET A 1 588 ? 13.671  -22.205 39.695  1.00 11.12 ? 580  MET A O   1 
ATOM   4177  C  CB  . MET A 1 588 ? 12.270  -23.217 41.840  1.00 11.15 ? 580  MET A CB  1 
ATOM   4178  C  CG  . MET A 1 588 ? 11.034  -22.569 41.202  1.00 12.90 ? 580  MET A CG  1 
ATOM   4179  S  SD  . MET A 1 588 ? 9.947   -21.726 42.375  1.00 15.56 ? 580  MET A SD  1 
ATOM   4180  C  CE  . MET A 1 588 ? 9.253   -23.108 43.289  1.00 12.32 ? 580  MET A CE  1 
ATOM   4181  N  N   . PRO A 1 589 ? 14.046  -24.173 38.677  1.00 12.42 ? 581  PRO A N   1 
ATOM   4182  C  CA  . PRO A 1 589 ? 14.617  -23.494 37.499  1.00 15.94 ? 581  PRO A CA  1 
ATOM   4183  C  C   . PRO A 1 589 ? 13.666  -22.519 36.825  1.00 13.92 ? 581  PRO A C   1 
ATOM   4184  O  O   . PRO A 1 589 ? 14.141  -21.543 36.224  1.00 12.13 ? 581  PRO A O   1 
ATOM   4185  C  CB  . PRO A 1 589 ? 14.997  -24.655 36.561  1.00 15.43 ? 581  PRO A CB  1 
ATOM   4186  C  CG  . PRO A 1 589 ? 14.247  -25.863 37.101  1.00 15.51 ? 581  PRO A CG  1 
ATOM   4187  C  CD  . PRO A 1 589 ? 14.188  -25.635 38.582  1.00 16.33 ? 581  PRO A CD  1 
ATOM   4188  N  N   . SER A 1 590 ? 12.343  -22.721 36.900  1.00 10.54 ? 582  SER A N   1 
ATOM   4189  C  CA  . SER A 1 590 ? 11.430  -21.720 36.348  1.00 13.39 ? 582  SER A CA  1 
ATOM   4190  C  C   . SER A 1 590 ? 10.204  -21.565 37.238  1.00 14.03 ? 582  SER A C   1 
ATOM   4191  O  O   . SER A 1 590 ? 9.356   -22.466 37.288  1.00 12.64 ? 582  SER A O   1 
ATOM   4192  C  CB  . SER A 1 590 ? 11.007  -22.074 34.921  1.00 11.60 ? 582  SER A CB  1 
ATOM   4193  O  OG  . SER A 1 590 ? 10.167  -21.034 34.413  1.00 12.96 ? 582  SER A OG  1 
ATOM   4194  N  N   . THR A 1 591 ? 10.103  -20.418 37.926  1.00 12.55 ? 583  THR A N   1 
ATOM   4195  C  CA  . THR A 1 591 ? 8.867   -20.082 38.636  1.00 12.79 ? 583  THR A CA  1 
ATOM   4196  C  C   . THR A 1 591 ? 7.685   -20.062 37.688  1.00 11.17 ? 583  THR A C   1 
ATOM   4197  O  O   . THR A 1 591 ? 6.601   -20.557 38.023  1.00 13.92 ? 583  THR A O   1 
ATOM   4198  C  CB  . THR A 1 591 ? 8.987   -18.714 39.325  1.00 15.44 ? 583  THR A CB  1 
ATOM   4199  O  OG1 . THR A 1 591 ? 9.206   -17.687 38.344  1.00 11.80 ? 583  THR A OG1 1 
ATOM   4200  C  CG2 . THR A 1 591 ? 10.160  -18.707 40.307  1.00 11.48 ? 583  THR A CG2 1 
ATOM   4201  N  N   . SER A 1 592 ? 7.877   -19.453 36.513  1.00 13.42 ? 584  SER A N   1 
ATOM   4202  C  CA  . SER A 1 592 ? 6.822   -19.331 35.510  1.00 16.80 ? 584  SER A CA  1 
ATOM   4203  C  C   . SER A 1 592 ? 6.159   -20.680 35.249  1.00 17.96 ? 584  SER A C   1 
ATOM   4204  O  O   . SER A 1 592 ? 4.932   -20.821 35.342  1.00 17.37 ? 584  SER A O   1 
ATOM   4205  C  CB  . SER A 1 592 ? 7.424   -18.765 34.210  1.00 16.54 ? 584  SER A CB  1 
ATOM   4206  O  OG  . SER A 1 592 ? 8.605   -17.971 34.462  1.00 16.32 ? 584  SER A OG  1 
ATOM   4207  N  N   . VAL A 1 593 ? 6.979   -21.691 34.950  1.00 13.51 ? 585  VAL A N   1 
ATOM   4208  C  CA  . VAL A 1 593 ? 6.481   -23.016 34.596  1.00 12.31 ? 585  VAL A CA  1 
ATOM   4209  C  C   . VAL A 1 593 ? 5.889   -23.716 35.814  1.00 14.04 ? 585  VAL A C   1 
ATOM   4210  O  O   . VAL A 1 593 ? 4.847   -24.378 35.724  1.00 17.07 ? 585  VAL A O   1 
ATOM   4211  C  CB  . VAL A 1 593 ? 7.627   -23.832 33.974  1.00 14.79 ? 585  VAL A CB  1 
ATOM   4212  C  CG1 . VAL A 1 593 ? 7.196   -25.259 33.677  1.00 14.03 ? 585  VAL A CG1 1 
ATOM   4213  C  CG2 . VAL A 1 593 ? 8.148   -23.124 32.706  1.00 14.56 ? 585  VAL A CG2 1 
ATOM   4214  N  N   . PHE A 1 594 ? 6.545   -23.597 36.968  1.00 14.61 ? 586  PHE A N   1 
ATOM   4215  C  CA  . PHE A 1 594 ? 6.003   -24.225 38.170  1.00 12.97 ? 586  PHE A CA  1 
ATOM   4216  C  C   . PHE A 1 594 ? 4.594   -23.718 38.474  1.00 15.30 ? 586  PHE A C   1 
ATOM   4217  O  O   . PHE A 1 594 ? 3.714   -24.499 38.856  1.00 16.26 ? 586  PHE A O   1 
ATOM   4218  C  CB  . PHE A 1 594 ? 6.920   -23.977 39.362  1.00 14.92 ? 586  PHE A CB  1 
ATOM   4219  C  CG  . PHE A 1 594 ? 6.416   -24.606 40.648  1.00 13.63 ? 586  PHE A CG  1 
ATOM   4220  C  CD1 . PHE A 1 594 ? 6.354   -25.979 40.776  1.00 14.79 ? 586  PHE A CD1 1 
ATOM   4221  C  CD2 . PHE A 1 594 ? 6.013   -23.817 41.717  1.00 17.27 ? 586  PHE A CD2 1 
ATOM   4222  C  CE1 . PHE A 1 594 ? 5.894   -26.568 41.949  1.00 20.42 ? 586  PHE A CE1 1 
ATOM   4223  C  CE2 . PHE A 1 594 ? 5.552   -24.396 42.892  1.00 19.85 ? 586  PHE A CE2 1 
ATOM   4224  C  CZ  . PHE A 1 594 ? 5.492   -25.774 43.005  1.00 22.47 ? 586  PHE A CZ  1 
ATOM   4225  N  N   . ASP A 1 595 ? 4.359   -22.419 38.283  1.00 17.17 ? 587  ASP A N   1 
ATOM   4226  C  CA  . ASP A 1 595 ? 3.083   -21.811 38.660  1.00 18.79 ? 587  ASP A CA  1 
ATOM   4227  C  C   . ASP A 1 595 ? 1.917   -22.305 37.813  1.00 22.66 ? 587  ASP A C   1 
ATOM   4228  O  O   . ASP A 1 595 ? 0.762   -22.167 38.232  1.00 23.35 ? 587  ASP A O   1 
ATOM   4229  C  CB  . ASP A 1 595 ? 3.176   -20.285 38.562  1.00 19.14 ? 587  ASP A CB  1 
ATOM   4230  C  CG  . ASP A 1 595 ? 4.045   -19.664 39.658  1.00 22.33 ? 587  ASP A CG  1 
ATOM   4231  O  OD1 . ASP A 1 595 ? 4.371   -20.343 40.653  1.00 25.82 ? 587  ASP A OD1 1 
ATOM   4232  O  OD2 . ASP A 1 595 ? 4.400   -18.482 39.522  1.00 23.14 ? 587  ASP A OD2 1 
ATOM   4233  N  N   . ARG A 1 596 ? 2.170   -22.870 36.635  1.00 18.35 ? 588  ARG A N   1 
ATOM   4234  C  CA  . ARG A 1 596 ? 1.084   -23.406 35.829  1.00 20.64 ? 588  ARG A CA  1 
ATOM   4235  C  C   . ARG A 1 596 ? 0.954   -24.921 35.933  1.00 19.89 ? 588  ARG A C   1 
ATOM   4236  O  O   . ARG A 1 596 ? 0.131   -25.513 35.224  1.00 18.85 ? 588  ARG A O   1 
ATOM   4237  C  CB  . ARG A 1 596 ? 1.234   -22.968 34.367  1.00 25.57 ? 588  ARG A CB  1 
ATOM   4238  C  CG  . ARG A 1 596 ? 2.491   -23.388 33.648  1.00 22.61 ? 588  ARG A CG  1 
ATOM   4239  C  CD  . ARG A 1 596 ? 2.387   -22.942 32.183  1.00 29.90 ? 588  ARG A CD  1 
ATOM   4240  N  NE  . ARG A 1 596 ? 3.539   -23.304 31.361  1.00 29.11 ? 588  ARG A NE  1 
ATOM   4241  C  CZ  . ARG A 1 596 ? 4.540   -22.472 31.089  1.00 25.73 ? 588  ARG A CZ  1 
ATOM   4242  N  NH1 . ARG A 1 596 ? 4.528   -21.241 31.592  1.00 17.77 ? 588  ARG A NH1 1 
ATOM   4243  N  NH2 . ARG A 1 596 ? 5.552   -22.868 30.324  1.00 28.21 ? 588  ARG A NH2 1 
ATOM   4244  N  N   . GLN A 1 597 ? 1.732   -25.561 36.808  1.00 17.76 ? 589  GLN A N   1 
ATOM   4245  C  CA  . GLN A 1 597 ? 1.517   -26.970 37.107  1.00 19.74 ? 589  GLN A CA  1 
ATOM   4246  C  C   . GLN A 1 597 ? 0.237   -27.139 37.922  1.00 19.98 ? 589  GLN A C   1 
ATOM   4247  O  O   . GLN A 1 597 ? -0.218  -26.212 38.600  1.00 24.67 ? 589  GLN A O   1 
ATOM   4248  C  CB  . GLN A 1 597 ? 2.717   -27.540 37.872  1.00 19.32 ? 589  GLN A CB  1 
ATOM   4249  C  CG  . GLN A 1 597 ? 4.030   -27.246 37.189  1.00 15.96 ? 589  GLN A CG  1 
ATOM   4250  C  CD  . GLN A 1 597 ? 4.014   -27.749 35.768  1.00 23.52 ? 589  GLN A CD  1 
ATOM   4251  O  OE1 . GLN A 1 597 ? 3.759   -28.930 35.531  1.00 20.09 ? 589  GLN A OE1 1 
ATOM   4252  N  NE2 . GLN A 1 597 ? 4.232   -26.851 34.809  1.00 21.02 ? 589  GLN A NE2 1 
ATOM   4253  N  N   . ASP A 1 598 ? -0.356  -28.332 37.842  1.00 19.72 ? 590  ASP A N   1 
ATOM   4254  C  CA  . ASP A 1 598 ? -1.607  -28.580 38.550  1.00 25.86 ? 590  ASP A CA  1 
ATOM   4255  C  C   . ASP A 1 598 ? -1.383  -28.506 40.058  1.00 24.15 ? 590  ASP A C   1 
ATOM   4256  O  O   . ASP A 1 598 ? -0.257  -28.618 40.551  1.00 20.94 ? 590  ASP A O   1 
ATOM   4257  C  CB  . ASP A 1 598 ? -2.218  -29.931 38.150  1.00 28.70 ? 590  ASP A CB  1 
ATOM   4258  C  CG  . ASP A 1 598 ? -1.289  -31.114 38.409  1.00 36.18 ? 590  ASP A CG  1 
ATOM   4259  O  OD1 . ASP A 1 598 ? -1.245  -31.606 39.556  1.00 36.82 ? 590  ASP A OD1 1 
ATOM   4260  O  OD2 . ASP A 1 598 ? -0.611  -31.567 37.459  1.00 38.73 ? 590  ASP A OD2 1 
ATOM   4261  N  N   . ALA A 1 599 ? -2.479  -28.290 40.792  1.00 25.14 ? 591  ALA A N   1 
ATOM   4262  C  CA  . ALA A 1 599 ? -2.363  -28.012 42.223  1.00 23.88 ? 591  ALA A CA  1 
ATOM   4263  C  C   . ALA A 1 599 ? -1.753  -29.190 42.971  1.00 22.30 ? 591  ALA A C   1 
ATOM   4264  O  O   . ALA A 1 599 ? -0.969  -29.001 43.909  1.00 22.75 ? 591  ALA A O   1 
ATOM   4265  C  CB  . ALA A 1 599 ? -3.731  -27.658 42.810  1.00 22.42 ? 591  ALA A CB  1 
ATOM   4266  N  N   . ALA A 1 600 ? -2.100  -30.415 42.569  1.00 22.58 ? 592  ALA A N   1 
ATOM   4267  C  CA  . ALA A 1 600 ? -1.552  -31.588 43.243  1.00 27.89 ? 592  ALA A CA  1 
ATOM   4268  C  C   . ALA A 1 600 ? -0.034  -31.642 43.106  1.00 23.56 ? 592  ALA A C   1 
ATOM   4269  O  O   . ALA A 1 600 ? 0.669   -31.954 44.075  1.00 19.92 ? 592  ALA A O   1 
ATOM   4270  C  CB  . ALA A 1 600 ? -2.191  -32.866 42.695  1.00 27.34 ? 592  ALA A CB  1 
ATOM   4271  N  N   . TYR A 1 601 ? 0.492   -31.349 41.911  1.00 19.79 ? 593  TYR A N   1 
ATOM   4272  C  CA  . TYR A 1 601 ? 1.945   -31.349 41.747  1.00 21.01 ? 593  TYR A CA  1 
ATOM   4273  C  C   . TYR A 1 601 ? 2.598   -30.257 42.585  1.00 20.21 ? 593  TYR A C   1 
ATOM   4274  O  O   . TYR A 1 601 ? 3.618   -30.501 43.236  1.00 20.73 ? 593  TYR A O   1 
ATOM   4275  C  CB  . TYR A 1 601 ? 2.344   -31.186 40.274  1.00 18.60 ? 593  TYR A CB  1 
ATOM   4276  C  CG  . TYR A 1 601 ? 3.851   -31.258 40.091  1.00 18.07 ? 593  TYR A CG  1 
ATOM   4277  C  CD1 . TYR A 1 601 ? 4.518   -32.475 40.163  1.00 17.18 ? 593  TYR A CD1 1 
ATOM   4278  C  CD2 . TYR A 1 601 ? 4.608   -30.105 39.882  1.00 15.98 ? 593  TYR A CD2 1 
ATOM   4279  C  CE1 . TYR A 1 601 ? 5.894   -32.551 40.015  1.00 19.97 ? 593  TYR A CE1 1 
ATOM   4280  C  CE2 . TYR A 1 601 ? 5.985   -30.164 39.733  1.00 17.56 ? 593  TYR A CE2 1 
ATOM   4281  C  CZ  . TYR A 1 601 ? 6.622   -31.393 39.803  1.00 20.58 ? 593  TYR A CZ  1 
ATOM   4282  O  OH  . TYR A 1 601 ? 7.982   -31.470 39.662  1.00 16.05 ? 593  TYR A OH  1 
ATOM   4283  N  N   . GLN A 1 602 ? 2.031   -29.047 42.587  1.00 20.45 ? 594  GLN A N   1 
ATOM   4284  C  CA  . GLN A 1 602 ? 2.633   -27.961 43.355  1.00 21.93 ? 594  GLN A CA  1 
ATOM   4285  C  C   . GLN A 1 602 ? 2.640   -28.279 44.849  1.00 18.96 ? 594  GLN A C   1 
ATOM   4286  O  O   . GLN A 1 602 ? 3.595   -27.940 45.560  1.00 21.62 ? 594  GLN A O   1 
ATOM   4287  C  CB  . GLN A 1 602 ? 1.891   -26.652 43.094  1.00 24.04 ? 594  GLN A CB  1 
ATOM   4288  C  CG  . GLN A 1 602 ? 1.886   -26.202 41.634  1.00 26.08 ? 594  GLN A CG  1 
ATOM   4289  C  CD  . GLN A 1 602 ? 1.467   -24.754 41.477  1.00 32.87 ? 594  GLN A CD  1 
ATOM   4290  O  OE1 . GLN A 1 602 ? 1.773   -23.904 42.318  1.00 32.54 ? 594  GLN A OE1 1 
ATOM   4291  N  NE2 . GLN A 1 602 ? 0.762   -24.465 40.399  1.00 33.78 ? 594  GLN A NE2 1 
ATOM   4292  N  N   . ALA A 1 603 ? 1.584   -28.931 45.337  1.00 21.90 ? 595  ALA A N   1 
ATOM   4293  C  CA  . ALA A 1 603 ? 1.529   -29.324 46.743  1.00 22.72 ? 595  ALA A CA  1 
ATOM   4294  C  C   . ALA A 1 603 ? 2.519   -30.439 47.048  1.00 20.40 ? 595  ALA A C   1 
ATOM   4295  O  O   . ALA A 1 603 ? 3.066   -30.499 48.154  1.00 20.70 ? 595  ALA A O   1 
ATOM   4296  C  CB  . ALA A 1 603 ? 0.105   -29.755 47.119  1.00 28.62 ? 595  ALA A CB  1 
ATOM   4297  N  N   . ALA A 1 604 ? 2.758   -31.330 46.086  1.00 21.17 ? 596  ALA A N   1 
ATOM   4298  C  CA  . ALA A 1 604 ? 3.741   -32.383 46.292  1.00 20.74 ? 596  ALA A CA  1 
ATOM   4299  C  C   . ALA A 1 604 ? 5.143   -31.807 46.419  1.00 19.02 ? 596  ALA A C   1 
ATOM   4300  O  O   . ALA A 1 604 ? 5.974   -32.358 47.149  1.00 23.82 ? 596  ALA A O   1 
ATOM   4301  C  CB  . ALA A 1 604 ? 3.677   -33.394 45.145  1.00 21.64 ? 596  ALA A CB  1 
ATOM   4302  N  N   . VAL A 1 605 ? 5.420   -30.712 45.712  1.00 18.12 ? 597  VAL A N   1 
ATOM   4303  C  CA  . VAL A 1 605 ? 6.733   -30.074 45.778  1.00 16.64 ? 597  VAL A CA  1 
ATOM   4304  C  C   . VAL A 1 605 ? 6.854   -29.191 47.016  1.00 23.74 ? 597  VAL A C   1 
ATOM   4305  O  O   . VAL A 1 605 ? 7.906   -29.149 47.666  1.00 20.82 ? 597  VAL A O   1 
ATOM   4306  C  CB  . VAL A 1 605 ? 6.979   -29.261 44.497  1.00 15.74 ? 597  VAL A CB  1 
ATOM   4307  C  CG1 . VAL A 1 605 ? 8.300   -28.480 44.622  1.00 14.98 ? 597  VAL A CG1 1 
ATOM   4308  C  CG2 . VAL A 1 605 ? 6.963   -30.162 43.271  1.00 19.12 ? 597  VAL A CG2 1 
ATOM   4309  N  N   . LEU A 1 606 ? 5.791   -28.453 47.344  1.00 16.94 ? 598  LEU A N   1 
ATOM   4310  C  CA  . LEU A 1 606 ? 5.790   -27.484 48.442  1.00 18.42 ? 598  LEU A CA  1 
ATOM   4311  C  C   . LEU A 1 606 ? 4.587   -27.775 49.321  1.00 19.23 ? 598  LEU A C   1 
ATOM   4312  O  O   . LEU A 1 606 ? 3.548   -27.114 49.200  1.00 21.47 ? 598  LEU A O   1 
ATOM   4313  C  CB  . LEU A 1 606 ? 5.739   -26.047 47.922  1.00 17.36 ? 598  LEU A CB  1 
ATOM   4314  C  CG  . LEU A 1 606 ? 6.848   -25.610 46.967  1.00 17.73 ? 598  LEU A CG  1 
ATOM   4315  C  CD1 . LEU A 1 606 ? 6.567   -24.200 46.429  1.00 19.12 ? 598  LEU A CD1 1 
ATOM   4316  C  CD2 . LEU A 1 606 ? 8.205   -25.688 47.656  1.00 16.05 ? 598  LEU A CD2 1 
ATOM   4317  N  N   . PRO A 1 607 ? 4.693   -28.756 50.216  1.00 20.32 ? 599  PRO A N   1 
ATOM   4318  C  CA  . PRO A 1 607 ? 3.524   -29.163 51.008  1.00 24.77 ? 599  PRO A CA  1 
ATOM   4319  C  C   . PRO A 1 607 ? 3.024   -28.038 51.903  1.00 26.55 ? 599  PRO A C   1 
ATOM   4320  O  O   . PRO A 1 607 ? 3.799   -27.225 52.413  1.00 21.50 ? 599  PRO A O   1 
ATOM   4321  C  CB  . PRO A 1 607 ? 4.046   -30.352 51.826  1.00 24.82 ? 599  PRO A CB  1 
ATOM   4322  C  CG  . PRO A 1 607 ? 5.226   -30.871 51.033  1.00 20.06 ? 599  PRO A CG  1 
ATOM   4323  C  CD  . PRO A 1 607 ? 5.849   -29.644 50.431  1.00 19.57 ? 599  PRO A CD  1 
ATOM   4324  N  N   . GLU A 1 608 ? 1.706   -27.991 52.079  1.00 27.09 ? 600  GLU A N   1 
ATOM   4325  C  CA  . GLU A 1 608 ? 1.109   -26.974 52.930  1.00 26.66 ? 600  GLU A CA  1 
ATOM   4326  C  C   . GLU A 1 608 ? 1.597   -27.140 54.363  1.00 29.76 ? 600  GLU A C   1 
ATOM   4327  O  O   . GLU A 1 608 ? 1.717   -28.258 54.872  1.00 34.33 ? 600  GLU A O   1 
ATOM   4328  C  CB  . GLU A 1 608 ? -0.417  -27.062 52.874  1.00 34.88 ? 600  GLU A CB  1 
ATOM   4329  N  N   . GLY A 1 609 ? 1.899   -26.017 55.011  1.00 31.61 ? 601  GLY A N   1 
ATOM   4330  C  CA  . GLY A 1 609 ? 2.352   -26.037 56.382  1.00 32.58 ? 601  GLY A CA  1 
ATOM   4331  C  C   . GLY A 1 609 ? 3.829   -26.303 56.578  1.00 32.93 ? 601  GLY A C   1 
ATOM   4332  O  O   . GLY A 1 609 ? 4.309   -26.218 57.713  1.00 33.78 ? 601  GLY A O   1 
ATOM   4333  N  N   . LEU A 1 610 ? 4.566   -26.637 55.529  1.00 28.73 ? 602  LEU A N   1 
ATOM   4334  C  CA  . LEU A 1 610 ? 6.002   -26.816 55.655  1.00 33.90 ? 602  LEU A CA  1 
ATOM   4335  C  C   . LEU A 1 610 ? 6.689   -25.477 55.423  1.00 28.15 ? 602  LEU A C   1 
ATOM   4336  O  O   . LEU A 1 610 ? 6.538   -24.898 54.338  1.00 24.00 ? 602  LEU A O   1 
ATOM   4337  C  CB  . LEU A 1 610 ? 6.502   -27.853 54.665  1.00 36.11 ? 602  LEU A CB  1 
ATOM   4338  C  CG  . LEU A 1 610 ? 7.931   -28.364 54.854  1.00 33.05 ? 602  LEU A CG  1 
ATOM   4339  C  CD1 . LEU A 1 610 ? 8.048   -29.174 56.132  1.00 35.45 ? 602  LEU A CD1 1 
ATOM   4340  C  CD2 . LEU A 1 610 ? 8.364   -29.180 53.640  1.00 31.19 ? 602  LEU A CD2 1 
ATOM   4341  N  N   . PRO A 1 611 ? 7.411   -24.937 56.405  1.00 28.79 ? 603  PRO A N   1 
ATOM   4342  C  CA  . PRO A 1 611 ? 8.070   -23.636 56.216  1.00 26.67 ? 603  PRO A CA  1 
ATOM   4343  C  C   . PRO A 1 611 ? 9.002   -23.642 55.012  1.00 18.30 ? 603  PRO A C   1 
ATOM   4344  O  O   . PRO A 1 611 ? 9.742   -24.597 54.782  1.00 19.63 ? 603  PRO A O   1 
ATOM   4345  C  CB  . PRO A 1 611 ? 8.854   -23.443 57.519  1.00 23.75 ? 603  PRO A CB  1 
ATOM   4346  C  CG  . PRO A 1 611 ? 8.116   -24.249 58.519  1.00 29.09 ? 603  PRO A CG  1 
ATOM   4347  C  CD  . PRO A 1 611 ? 7.544   -25.435 57.785  1.00 29.46 ? 603  PRO A CD  1 
ATOM   4348  N  N   . ARG A 1 612 ? 8.973   -22.552 54.256  1.00 17.47 ? 604  ARG A N   1 
ATOM   4349  C  CA  . ARG A 1 612 ? 9.755   -22.427 53.033  1.00 16.37 ? 604  ARG A CA  1 
ATOM   4350  C  C   . ARG A 1 612 ? 10.828  -21.358 53.195  1.00 20.99 ? 604  ARG A C   1 
ATOM   4351  O  O   . ARG A 1 612 ? 10.567  -20.274 53.724  1.00 19.84 ? 604  ARG A O   1 
ATOM   4352  C  CB  . ARG A 1 612 ? 8.851   -22.082 51.852  1.00 17.90 ? 604  ARG A CB  1 
ATOM   4353  C  CG  . ARG A 1 612 ? 7.693   -23.061 51.694  1.00 17.05 ? 604  ARG A CG  1 
ATOM   4354  C  CD  . ARG A 1 612 ? 6.604   -22.514 50.795  1.00 17.64 ? 604  ARG A CD  1 
ATOM   4355  N  NE  . ARG A 1 612 ? 5.490   -23.456 50.689  1.00 18.95 ? 604  ARG A NE  1 
ATOM   4356  C  CZ  . ARG A 1 612 ? 4.290   -23.151 50.206  1.00 27.84 ? 604  ARG A CZ  1 
ATOM   4357  N  NH1 . ARG A 1 612 ? 4.042   -21.920 49.792  1.00 24.48 ? 604  ARG A NH1 1 
ATOM   4358  N  NH2 . ARG A 1 612 ? 3.335   -24.076 50.144  1.00 25.07 ? 604  ARG A NH2 1 
ATOM   4359  N  N   . ILE A 1 613 ? 12.039  -21.669 52.743  1.00 16.38 ? 605  ILE A N   1 
ATOM   4360  C  CA  . ILE A 1 613 ? 13.137  -20.707 52.697  1.00 17.19 ? 605  ILE A CA  1 
ATOM   4361  C  C   . ILE A 1 613 ? 13.651  -20.666 51.264  1.00 16.28 ? 605  ILE A C   1 
ATOM   4362  O  O   . ILE A 1 613 ? 14.062  -21.698 50.718  1.00 18.55 ? 605  ILE A O   1 
ATOM   4363  C  CB  . ILE A 1 613 ? 14.280  -21.068 53.662  1.00 15.26 ? 605  ILE A CB  1 
ATOM   4364  C  CG1 . ILE A 1 613 ? 13.776  -21.168 55.106  1.00 16.35 ? 605  ILE A CG1 1 
ATOM   4365  C  CG2 . ILE A 1 613 ? 15.359  -20.006 53.612  1.00 24.12 ? 605  ILE A CG2 1 
ATOM   4366  C  CD1 . ILE A 1 613 ? 13.281  -22.557 55.480  1.00 20.89 ? 605  ILE A CD1 1 
ATOM   4367  N  N   . ALA A 1 614 ? 13.649  -19.484 50.660  1.00 13.18 ? 606  ALA A N   1 
ATOM   4368  C  CA  . ALA A 1 614 ? 14.161  -19.323 49.307  1.00 12.35 ? 606  ALA A CA  1 
ATOM   4369  C  C   . ALA A 1 614 ? 15.581  -18.779 49.341  1.00 14.98 ? 606  ALA A C   1 
ATOM   4370  O  O   . ALA A 1 614 ? 15.891  -17.884 50.136  1.00 15.76 ? 606  ALA A O   1 
ATOM   4371  C  CB  . ALA A 1 614 ? 13.269  -18.389 48.484  1.00 12.98 ? 606  ALA A CB  1 
ATOM   4372  N  N   . VAL A 1 615 ? 16.427  -19.299 48.450  1.00 14.52 ? 607  VAL A N   1 
ATOM   4373  C  CA  . VAL A 1 615 ? 17.834  -18.903 48.351  1.00 11.37 ? 607  VAL A CA  1 
ATOM   4374  C  C   . VAL A 1 615 ? 18.136  -18.599 46.887  1.00 12.27 ? 607  VAL A C   1 
ATOM   4375  O  O   . VAL A 1 615 ? 18.131  -19.504 46.045  1.00 11.88 ? 607  VAL A O   1 
ATOM   4376  C  CB  . VAL A 1 615 ? 18.786  -19.978 48.885  1.00 11.88 ? 607  VAL A CB  1 
ATOM   4377  C  CG1 . VAL A 1 615 ? 20.190  -19.419 48.934  1.00 12.66 ? 607  VAL A CG1 1 
ATOM   4378  C  CG2 . VAL A 1 615 ? 18.344  -20.447 50.295  1.00 14.78 ? 607  VAL A CG2 1 
ATOM   4379  N  N   . GLU A 1 616 ? 18.423  -17.337 46.594  1.00 13.76 ? 608  GLU A N   1 
ATOM   4380  C  CA  . GLU A 1 616 ? 18.731  -16.899 45.241  1.00 10.09 ? 608  GLU A CA  1 
ATOM   4381  C  C   . GLU A 1 616 ? 19.555  -15.619 45.321  1.00 9.39  ? 608  GLU A C   1 
ATOM   4382  O  O   . GLU A 1 616 ? 19.240  -14.732 46.111  1.00 11.69 ? 608  GLU A O   1 
ATOM   4383  C  CB  . GLU A 1 616 ? 17.438  -16.668 44.446  1.00 10.33 ? 608  GLU A CB  1 
ATOM   4384  C  CG  . GLU A 1 616 ? 17.661  -16.141 43.053  1.00 12.45 ? 608  GLU A CG  1 
ATOM   4385  C  CD  . GLU A 1 616 ? 16.369  -16.119 42.263  1.00 9.76  ? 608  GLU A CD  1 
ATOM   4386  O  OE1 . GLU A 1 616 ? 15.547  -15.195 42.474  1.00 12.25 ? 608  GLU A OE1 1 
ATOM   4387  O  OE2 . GLU A 1 616 ? 16.175  -17.051 41.448  1.00 13.45 ? 608  GLU A OE2 1 
ATOM   4388  N  N   . ALA A 1 617 ? 20.617  -15.536 44.518  1.00 10.50 ? 609  ALA A N   1 
ATOM   4389  C  CA  . ALA A 1 617 ? 21.499  -14.364 44.518  1.00 11.56 ? 609  ALA A CA  1 
ATOM   4390  C  C   . ALA A 1 617 ? 20.878  -13.203 43.731  1.00 16.47 ? 609  ALA A C   1 
ATOM   4391  O  O   . ALA A 1 617 ? 21.420  -12.703 42.739  1.00 14.74 ? 609  ALA A O   1 
ATOM   4392  C  CB  . ALA A 1 617 ? 22.877  -14.734 43.973  1.00 12.43 ? 609  ALA A CB  1 
ATOM   4393  N  N   . GLY A 1 618 ? 19.718  -12.769 44.216  1.00 15.25 ? 610  GLY A N   1 
ATOM   4394  C  CA  . GLY A 1 618 ? 19.002  -11.652 43.640  1.00 12.92 ? 610  GLY A CA  1 
ATOM   4395  C  C   . GLY A 1 618 ? 18.042  -11.080 44.665  1.00 11.86 ? 610  GLY A C   1 
ATOM   4396  O  O   . GLY A 1 618 ? 17.997  -11.520 45.816  1.00 11.65 ? 610  GLY A O   1 
ATOM   4397  N  N   . HIS A 1 619 ? 17.264  -10.094 44.224  1.00 11.00 ? 611  HIS A N   1 
ATOM   4398  C  CA  . HIS A 1 619 ? 16.277  -9.444  45.083  1.00 12.53 ? 611  HIS A CA  1 
ATOM   4399  C  C   . HIS A 1 619 ? 15.338  -10.476 45.703  1.00 11.17 ? 611  HIS A C   1 
ATOM   4400  O  O   . HIS A 1 619 ? 14.989  -11.465 45.062  1.00 11.84 ? 611  HIS A O   1 
ATOM   4401  C  CB  . HIS A 1 619 ? 15.478  -8.432  44.251  1.00 12.35 ? 611  HIS A CB  1 
ATOM   4402  C  CG  . HIS A 1 619 ? 14.923  -7.287  45.043  1.00 11.87 ? 611  HIS A CG  1 
ATOM   4403  N  ND1 . HIS A 1 619 ? 13.891  -7.427  45.943  1.00 12.46 ? 611  HIS A ND1 1 
ATOM   4404  C  CD2 . HIS A 1 619 ? 15.257  -5.975  45.061  1.00 11.28 ? 611  HIS A CD2 1 
ATOM   4405  C  CE1 . HIS A 1 619 ? 13.619  -6.259  46.493  1.00 14.02 ? 611  HIS A CE1 1 
ATOM   4406  N  NE2 . HIS A 1 619 ? 14.432  -5.357  45.970  1.00 14.46 ? 611  HIS A NE2 1 
ATOM   4407  N  N   . THR A 1 620 ? 14.936  -10.239 46.965  1.00 10.72 ? 612  THR A N   1 
ATOM   4408  C  CA  . THR A 1 620 ? 14.093  -11.182 47.704  1.00 15.51 ? 612  THR A CA  1 
ATOM   4409  C  C   . THR A 1 620 ? 12.597  -11.008 47.458  1.00 18.67 ? 612  THR A C   1 
ATOM   4410  O  O   . THR A 1 620 ? 11.832  -11.944 47.718  1.00 12.27 ? 612  THR A O   1 
ATOM   4411  C  CB  . THR A 1 620 ? 14.290  -11.042 49.229  1.00 13.42 ? 612  THR A CB  1 
ATOM   4412  O  OG1 . THR A 1 620 ? 13.883  -9.736  49.645  1.00 11.93 ? 612  THR A OG1 1 
ATOM   4413  C  CG2 . THR A 1 620 ? 15.746  -11.280 49.669  1.00 11.14 ? 612  THR A CG2 1 
ATOM   4414  N  N   . ASN A 1 621 ? 12.154  -9.837  46.989  1.00 14.15 ? 613  ASN A N   1 
ATOM   4415  C  CA  A ASN A 1 621 ? 10.752  -9.504  47.213  0.53 16.17 ? 613  ASN A CA  1 
ATOM   4416  C  CA  B ASN A 1 621 ? 10.745  -9.446  47.125  0.47 16.65 ? 613  ASN A CA  1 
ATOM   4417  C  C   . ASN A 1 621 ? 9.802   -10.433 46.457  1.00 16.56 ? 613  ASN A C   1 
ATOM   4418  O  O   . ASN A 1 621 ? 8.692   -10.680 46.945  1.00 18.77 ? 613  ASN A O   1 
ATOM   4419  C  CB  A ASN A 1 621 ? 10.511  -8.023  46.892  0.53 19.73 ? 613  ASN A CB  1 
ATOM   4420  C  CB  B ASN A 1 621 ? 10.520  -8.055  46.532  0.47 19.66 ? 613  ASN A CB  1 
ATOM   4421  C  CG  A ASN A 1 621 ? 10.918  -7.101  48.056  0.53 22.22 ? 613  ASN A CG  1 
ATOM   4422  C  CG  B ASN A 1 621 ? 9.040   -7.724  46.377  0.47 22.76 ? 613  ASN A CG  1 
ATOM   4423  O  OD1 A ASN A 1 621 ? 10.373  -6.005  48.237  0.53 19.73 ? 613  ASN A OD1 1 
ATOM   4424  O  OD1 B ASN A 1 621 ? 8.403   -7.253  47.316  0.47 27.61 ? 613  ASN A OD1 1 
ATOM   4425  N  ND2 A ASN A 1 621 ? 11.865  -7.564  48.862  0.53 25.78 ? 613  ASN A ND2 1 
ATOM   4426  N  ND2 B ASN A 1 621 ? 8.486   -7.983  45.191  0.47 24.11 ? 613  ASN A ND2 1 
ATOM   4427  N  N   . GLY A 1 622 ? 10.211  -10.988 45.310  1.00 18.32 ? 614  GLY A N   1 
ATOM   4428  C  CA  . GLY A 1 622 ? 9.341   -11.901 44.581  1.00 21.19 ? 614  GLY A CA  1 
ATOM   4429  C  C   . GLY A 1 622 ? 9.112   -13.232 45.270  1.00 21.39 ? 614  GLY A C   1 
ATOM   4430  O  O   . GLY A 1 622 ? 8.138   -13.926 44.963  1.00 19.10 ? 614  GLY A O   1 
ATOM   4431  N  N   . TRP A 1 623 ? 9.977   -13.601 46.207  1.00 14.62 ? 615  TRP A N   1 
ATOM   4432  C  CA  . TRP A 1 623 ? 9.865   -14.911 46.823  1.00 15.16 ? 615  TRP A CA  1 
ATOM   4433  C  C   . TRP A 1 623 ? 8.804   -14.972 47.918  1.00 12.65 ? 615  TRP A C   1 
ATOM   4434  O  O   . TRP A 1 623 ? 8.474   -16.071 48.360  1.00 16.68 ? 615  TRP A O   1 
ATOM   4435  C  CB  . TRP A 1 623 ? 11.236  -15.335 47.360  1.00 16.74 ? 615  TRP A CB  1 
ATOM   4436  C  CG  . TRP A 1 623 ? 12.167  -15.672 46.230  1.00 14.44 ? 615  TRP A CG  1 
ATOM   4437  C  CD1 . TRP A 1 623 ? 13.221  -14.928 45.773  1.00 15.92 ? 615  TRP A CD1 1 
ATOM   4438  C  CD2 . TRP A 1 623 ? 12.087  -16.823 45.380  1.00 14.84 ? 615  TRP A CD2 1 
ATOM   4439  N  NE1 . TRP A 1 623 ? 13.806  -15.553 44.690  1.00 14.87 ? 615  TRP A NE1 1 
ATOM   4440  C  CE2 . TRP A 1 623 ? 13.138  -16.725 44.440  1.00 12.99 ? 615  TRP A CE2 1 
ATOM   4441  C  CE3 . TRP A 1 623 ? 11.234  -17.936 45.331  1.00 17.14 ? 615  TRP A CE3 1 
ATOM   4442  C  CZ2 . TRP A 1 623 ? 13.358  -17.693 43.453  1.00 14.53 ? 615  TRP A CZ2 1 
ATOM   4443  C  CZ3 . TRP A 1 623 ? 11.451  -18.899 44.345  1.00 16.00 ? 615  TRP A CZ3 1 
ATOM   4444  C  CH2 . TRP A 1 623 ? 12.505  -18.766 43.421  1.00 13.81 ? 615  TRP A CH2 1 
ATOM   4445  N  N   . TYR A 1 624 ? 8.244   -13.833 48.345  1.00 13.02 ? 616  TYR A N   1 
ATOM   4446  C  CA  . TYR A 1 624 ? 7.212   -13.878 49.380  1.00 14.01 ? 616  TYR A CA  1 
ATOM   4447  C  C   . TYR A 1 624 ? 5.932   -14.489 48.855  1.00 14.44 ? 616  TYR A C   1 
ATOM   4448  O  O   . TYR A 1 624 ? 5.147   -15.027 49.641  1.00 16.71 ? 616  TYR A O   1 
ATOM   4449  C  CB  . TYR A 1 624 ? 6.967   -12.481 49.951  1.00 15.53 ? 616  TYR A CB  1 
ATOM   4450  C  CG  . TYR A 1 624 ? 8.151   -12.048 50.787  1.00 16.50 ? 616  TYR A CG  1 
ATOM   4451  C  CD1 . TYR A 1 624 ? 8.349   -12.582 52.057  1.00 18.96 ? 616  TYR A CD1 1 
ATOM   4452  C  CD2 . TYR A 1 624 ? 9.094   -11.160 50.288  1.00 22.48 ? 616  TYR A CD2 1 
ATOM   4453  C  CE1 . TYR A 1 624 ? 9.437   -12.224 52.821  1.00 24.18 ? 616  TYR A CE1 1 
ATOM   4454  C  CE2 . TYR A 1 624 ? 10.202  -10.793 51.047  1.00 21.59 ? 616  TYR A CE2 1 
ATOM   4455  C  CZ  . TYR A 1 624 ? 10.359  -11.327 52.314  1.00 28.12 ? 616  TYR A CZ  1 
ATOM   4456  O  OH  . TYR A 1 624 ? 11.442  -10.973 53.081  1.00 27.49 ? 616  TYR A OH  1 
ATOM   4457  N  N   . LYS A 1 625 ? 5.729   -14.442 47.537  1.00 13.94 ? 617  LYS A N   1 
ATOM   4458  C  CA  . LYS A 1 625 ? 4.627   -15.178 46.923  1.00 17.02 ? 617  LYS A CA  1 
ATOM   4459  C  C   . LYS A 1 625 ? 4.632   -16.648 47.333  1.00 16.62 ? 617  LYS A C   1 
ATOM   4460  O  O   . LYS A 1 625 ? 3.564   -17.257 47.494  1.00 18.83 ? 617  LYS A O   1 
ATOM   4461  C  CB  . LYS A 1 625 ? 4.708   -15.047 45.400  1.00 18.27 ? 617  LYS A CB  1 
ATOM   4462  C  CG  . LYS A 1 625 ? 3.732   -15.934 44.645  1.00 26.67 ? 617  LYS A CG  1 
ATOM   4463  C  CD  . LYS A 1 625 ? 4.183   -16.143 43.210  1.00 36.66 ? 617  LYS A CD  1 
ATOM   4464  C  CE  . LYS A 1 625 ? 3.226   -17.057 42.468  1.00 40.41 ? 617  LYS A CE  1 
ATOM   4465  N  NZ  . LYS A 1 625 ? 3.353   -16.876 40.999  1.00 40.25 ? 617  LYS A NZ  1 
ATOM   4466  N  N   . TYR A 1 626 ? 5.816   -17.225 47.530  1.00 14.10 ? 618  TYR A N   1 
ATOM   4467  C  CA  . TYR A 1 626 ? 5.992   -18.612 47.942  1.00 18.89 ? 618  TYR A CA  1 
ATOM   4468  C  C   . TYR A 1 626 ? 6.186   -18.780 49.447  1.00 16.27 ? 618  TYR A C   1 
ATOM   4469  O  O   . TYR A 1 626 ? 5.523   -19.611 50.072  1.00 18.44 ? 618  TYR A O   1 
ATOM   4470  C  CB  . TYR A 1 626 ? 7.194   -19.224 47.205  1.00 17.64 ? 618  TYR A CB  1 
ATOM   4471  C  CG  . TYR A 1 626 ? 7.015   -19.306 45.708  1.00 17.05 ? 618  TYR A CG  1 
ATOM   4472  C  CD1 . TYR A 1 626 ? 6.239   -20.304 45.139  1.00 24.13 ? 618  TYR A CD1 1 
ATOM   4473  C  CD2 . TYR A 1 626 ? 7.611   -18.371 44.862  1.00 17.46 ? 618  TYR A CD2 1 
ATOM   4474  C  CE1 . TYR A 1 626 ? 6.068   -20.381 43.773  1.00 27.73 ? 618  TYR A CE1 1 
ATOM   4475  C  CE2 . TYR A 1 626 ? 7.437   -18.435 43.507  1.00 21.02 ? 618  TYR A CE2 1 
ATOM   4476  C  CZ  . TYR A 1 626 ? 6.667   -19.444 42.962  1.00 25.94 ? 618  TYR A CZ  1 
ATOM   4477  O  OH  . TYR A 1 626 ? 6.495   -19.510 41.598  1.00 25.94 ? 618  TYR A OH  1 
ATOM   4478  N  N   . VAL A 1 627 ? 7.105   -18.035 50.053  1.00 16.07 ? 619  VAL A N   1 
ATOM   4479  C  CA  . VAL A 1 627 ? 7.437   -18.310 51.448  1.00 19.11 ? 619  VAL A CA  1 
ATOM   4480  C  C   . VAL A 1 627 ? 6.523   -17.584 52.427  1.00 21.96 ? 619  VAL A C   1 
ATOM   4481  O  O   . VAL A 1 627 ? 6.462   -17.980 53.600  1.00 18.88 ? 619  VAL A O   1 
ATOM   4482  C  CB  . VAL A 1 627 ? 8.912   -17.983 51.770  1.00 19.71 ? 619  VAL A CB  1 
ATOM   4483  C  CG1 . VAL A 1 627 ? 9.856   -18.591 50.722  1.00 14.09 ? 619  VAL A CG1 1 
ATOM   4484  C  CG2 . VAL A 1 627 ? 9.148   -16.465 51.917  1.00 14.72 ? 619  VAL A CG2 1 
ATOM   4485  N  N   . GLY A 1 628 ? 5.815   -16.540 51.988  1.00 16.31 ? 620  GLY A N   1 
ATOM   4486  C  CA  . GLY A 1 628 ? 4.852   -15.882 52.862  1.00 20.54 ? 620  GLY A CA  1 
ATOM   4487  C  C   . GLY A 1 628 ? 5.476   -15.163 54.050  1.00 20.34 ? 620  GLY A C   1 
ATOM   4488  O  O   . GLY A 1 628 ? 6.678   -14.931 54.129  1.00 19.55 ? 620  GLY A O   1 
ATOM   4489  N  N   . LEU A 1 629 ? 4.609   -14.800 54.992  1.00 18.81 ? 621  LEU A N   1 
ATOM   4490  C  CA  . LEU A 1 629 ? 5.051   -13.991 56.124  1.00 28.95 ? 621  LEU A CA  1 
ATOM   4491  C  C   . LEU A 1 629 ? 5.884   -14.780 57.130  1.00 31.87 ? 621  LEU A C   1 
ATOM   4492  O  O   . LEU A 1 629 ? 6.660   -14.176 57.878  1.00 32.73 ? 621  LEU A O   1 
ATOM   4493  C  CB  . LEU A 1 629 ? 3.840   -13.364 56.825  1.00 24.76 ? 621  LEU A CB  1 
ATOM   4494  C  CG  . LEU A 1 629 ? 3.051   -12.368 55.969  1.00 24.19 ? 621  LEU A CG  1 
ATOM   4495  C  CD1 . LEU A 1 629 ? 1.874   -11.768 56.752  1.00 27.49 ? 621  LEU A CD1 1 
ATOM   4496  C  CD2 . LEU A 1 629 ? 3.977   -11.277 55.451  1.00 27.78 ? 621  LEU A CD2 1 
ATOM   4497  N  N   . ASN A 1 630 ? 5.760   -16.105 57.163  1.00 29.95 ? 622  ASN A N   1 
ATOM   4498  C  CA  . ASN A 1 630 ? 6.469   -16.905 58.154  1.00 31.27 ? 622  ASN A CA  1 
ATOM   4499  C  C   . ASN A 1 630 ? 7.644   -17.690 57.588  1.00 28.71 ? 622  ASN A C   1 
ATOM   4500  O  O   . ASN A 1 630 ? 8.359   -18.342 58.361  1.00 24.83 ? 622  ASN A O   1 
ATOM   4501  C  CB  . ASN A 1 630 ? 5.486   -17.845 58.856  1.00 32.77 ? 622  ASN A CB  1 
ATOM   4502  C  CG  . ASN A 1 630 ? 4.441   -17.083 59.644  1.00 39.99 ? 622  ASN A CG  1 
ATOM   4503  O  OD1 . ASN A 1 630 ? 4.759   -16.113 60.340  1.00 41.90 ? 622  ASN A OD1 1 
ATOM   4504  N  ND2 . ASN A 1 630 ? 3.186   -17.495 59.519  1.00 46.26 ? 622  ASN A ND2 1 
ATOM   4505  N  N   . GLY A 1 631 ? 7.870   -17.636 56.273  1.00 19.30 ? 623  GLY A N   1 
ATOM   4506  C  CA  . GLY A 1 631 ? 9.067   -18.176 55.655  1.00 17.44 ? 623  GLY A CA  1 
ATOM   4507  C  C   . GLY A 1 631 ? 10.199  -17.168 55.681  1.00 17.67 ? 623  GLY A C   1 
ATOM   4508  O  O   . GLY A 1 631 ? 10.187  -16.202 56.449  1.00 19.05 ? 623  GLY A O   1 
ATOM   4509  N  N   . ALA A 1 632 ? 11.200  -17.397 54.833  1.00 16.29 ? 624  ALA A N   1 
ATOM   4510  C  CA  . ALA A 1 632 ? 12.339  -16.483 54.799  1.00 19.19 ? 624  ALA A CA  1 
ATOM   4511  C  C   . ALA A 1 632 ? 13.035  -16.577 53.451  1.00 15.33 ? 624  ALA A C   1 
ATOM   4512  O  O   . ALA A 1 632 ? 12.746  -17.453 52.629  1.00 16.21 ? 624  ALA A O   1 
ATOM   4513  C  CB  . ALA A 1 632 ? 13.323  -16.762 55.946  1.00 16.07 ? 624  ALA A CB  1 
ATOM   4514  N  N   . VAL A 1 633 ? 13.938  -15.628 53.218  1.00 13.90 ? 625  VAL A N   1 
ATOM   4515  C  CA  . VAL A 1 633 ? 14.642  -15.520 51.951  1.00 14.14 ? 625  VAL A CA  1 
ATOM   4516  C  C   . VAL A 1 633 ? 16.090  -15.160 52.220  1.00 18.79 ? 625  VAL A C   1 
ATOM   4517  O  O   . VAL A 1 633 ? 16.389  -14.292 53.048  1.00 17.74 ? 625  VAL A O   1 
ATOM   4518  C  CB  . VAL A 1 633 ? 14.017  -14.464 51.012  1.00 12.44 ? 625  VAL A CB  1 
ATOM   4519  C  CG1 . VAL A 1 633 ? 14.610  -14.591 49.622  1.00 14.03 ? 625  VAL A CG1 1 
ATOM   4520  C  CG2 . VAL A 1 633 ? 12.479  -14.566 50.984  1.00 13.79 ? 625  VAL A CG2 1 
ATOM   4521  N  N   . VAL A 1 634 ? 16.983  -15.810 51.499  1.00 12.39 ? 626  VAL A N   1 
ATOM   4522  C  CA  . VAL A 1 634 ? 18.393  -15.461 51.485  1.00 13.74 ? 626  VAL A CA  1 
ATOM   4523  C  C   . VAL A 1 634 ? 18.658  -14.877 50.103  1.00 12.08 ? 626  VAL A C   1 
ATOM   4524  O  O   . VAL A 1 634 ? 18.715  -15.610 49.108  1.00 15.14 ? 626  VAL A O   1 
ATOM   4525  C  CB  . VAL A 1 634 ? 19.289  -16.669 51.772  1.00 12.57 ? 626  VAL A CB  1 
ATOM   4526  C  CG1 . VAL A 1 634 ? 20.742  -16.262 51.686  1.00 15.30 ? 626  VAL A CG1 1 
ATOM   4527  C  CG2 . VAL A 1 634 ? 18.961  -17.247 53.162  1.00 16.97 ? 626  VAL A CG2 1 
ATOM   4528  N  N   . GLY A 1 635 ? 18.794  -13.557 50.040  1.00 11.13 ? 627  GLY A N   1 
ATOM   4529  C  CA  . GLY A 1 635 ? 18.991  -12.870 48.776  1.00 12.95 ? 627  GLY A CA  1 
ATOM   4530  C  C   . GLY A 1 635 ? 19.799  -11.603 48.951  1.00 15.36 ? 627  GLY A C   1 
ATOM   4531  O  O   . GLY A 1 635 ? 20.524  -11.447 49.938  1.00 13.08 ? 627  GLY A O   1 
ATOM   4532  N  N   . ILE A 1 636 ? 19.688  -10.688 47.997  1.00 9.86  ? 628  ILE A N   1 
ATOM   4533  C  CA  . ILE A 1 636 ? 20.424  -9.430  48.064  1.00 9.91  ? 628  ILE A CA  1 
ATOM   4534  C  C   . ILE A 1 636 ? 19.543  -8.352  47.458  1.00 10.59 ? 628  ILE A C   1 
ATOM   4535  O  O   . ILE A 1 636 ? 19.045  -8.501  46.335  1.00 13.87 ? 628  ILE A O   1 
ATOM   4536  C  CB  . ILE A 1 636 ? 21.794  -9.520  47.348  1.00 11.19 ? 628  ILE A CB  1 
ATOM   4537  C  CG1 . ILE A 1 636 ? 22.461  -8.138  47.291  1.00 10.59 ? 628  ILE A CG1 1 
ATOM   4538  C  CG2 . ILE A 1 636 ? 21.647  -10.104 45.934  1.00 12.15 ? 628  ILE A CG2 1 
ATOM   4539  C  CD1 . ILE A 1 636 ? 23.894  -8.168  46.730  1.00 13.49 ? 628  ILE A CD1 1 
ATOM   4540  N  N   . ASN A 1 637 ? 19.321  -7.279  48.216  1.00 9.95  ? 629  ASN A N   1 
ATOM   4541  C  CA  . ASN A 1 637 ? 18.425  -6.217  47.786  1.00 11.98 ? 629  ASN A CA  1 
ATOM   4542  C  C   . ASN A 1 637 ? 19.142  -4.896  47.548  1.00 15.35 ? 629  ASN A C   1 
ATOM   4543  O  O   . ASN A 1 637 ? 18.481  -3.882  47.289  1.00 18.60 ? 629  ASN A O   1 
ATOM   4544  C  CB  . ASN A 1 637 ? 17.309  -6.018  48.817  1.00 14.90 ? 629  ASN A CB  1 
ATOM   4545  C  CG  . ASN A 1 637 ? 16.346  -7.175  48.851  1.00 13.63 ? 629  ASN A CG  1 
ATOM   4546  O  OD1 . ASN A 1 637 ? 16.421  -8.077  48.026  1.00 13.35 ? 629  ASN A OD1 1 
ATOM   4547  N  ND2 . ASN A 1 637 ? 15.422  -7.150  49.804  1.00 18.29 ? 629  ASN A ND2 1 
ATOM   4548  N  N   . ARG A 1 638 ? 20.463  -4.873  47.654  1.00 12.54 ? 630  ARG A N   1 
ATOM   4549  C  CA  . ARG A 1 638 ? 21.248  -3.674  47.417  1.00 10.20 ? 630  ARG A CA  1 
ATOM   4550  C  C   . ARG A 1 638 ? 22.142  -3.877  46.202  1.00 11.74 ? 630  ARG A C   1 
ATOM   4551  O  O   . ARG A 1 638 ? 22.251  -4.977  45.659  1.00 12.34 ? 630  ARG A O   1 
ATOM   4552  C  CB  . ARG A 1 638 ? 22.089  -3.336  48.648  1.00 17.13 ? 630  ARG A CB  1 
ATOM   4553  C  CG  . ARG A 1 638 ? 22.944  -4.473  49.117  1.00 14.65 ? 630  ARG A CG  1 
ATOM   4554  C  CD  . ARG A 1 638 ? 24.191  -3.936  49.845  1.00 18.02 ? 630  ARG A CD  1 
ATOM   4555  N  NE  . ARG A 1 638 ? 25.153  -3.443  48.862  1.00 24.10 ? 630  ARG A NE  1 
ATOM   4556  C  CZ  . ARG A 1 638 ? 26.324  -2.887  49.152  1.00 24.56 ? 630  ARG A CZ  1 
ATOM   4557  N  NH1 . ARG A 1 638 ? 26.709  -2.726  50.423  1.00 20.20 ? 630  ARG A NH1 1 
ATOM   4558  N  NH2 . ARG A 1 638 ? 27.109  -2.496  48.160  1.00 15.39 ? 630  ARG A NH2 1 
ATOM   4559  N  N   . PHE A 1 639 ? 22.776  -2.787  45.763  1.00 9.41  ? 631  PHE A N   1 
ATOM   4560  C  CA  . PHE A 1 639 ? 23.695  -2.886  44.639  1.00 8.85  ? 631  PHE A CA  1 
ATOM   4561  C  C   . PHE A 1 639 ? 24.911  -3.718  45.029  1.00 12.06 ? 631  PHE A C   1 
ATOM   4562  O  O   . PHE A 1 639 ? 25.257  -3.829  46.206  1.00 12.76 ? 631  PHE A O   1 
ATOM   4563  C  CB  . PHE A 1 639 ? 24.129  -1.489  44.187  1.00 8.92  ? 631  PHE A CB  1 
ATOM   4564  C  CG  . PHE A 1 639 ? 23.024  -0.699  43.523  1.00 10.77 ? 631  PHE A CG  1 
ATOM   4565  C  CD1 . PHE A 1 639 ? 22.496  -1.114  42.312  1.00 12.78 ? 631  PHE A CD1 1 
ATOM   4566  C  CD2 . PHE A 1 639 ? 22.525  0.448   44.118  1.00 11.18 ? 631  PHE A CD2 1 
ATOM   4567  C  CE1 . PHE A 1 639 ? 21.480  -0.387  41.686  1.00 11.68 ? 631  PHE A CE1 1 
ATOM   4568  C  CE2 . PHE A 1 639 ? 21.507  1.185   43.512  1.00 12.40 ? 631  PHE A CE2 1 
ATOM   4569  C  CZ  . PHE A 1 639 ? 20.992  0.767   42.287  1.00 12.73 ? 631  PHE A CZ  1 
ATOM   4570  N  N   . GLY A 1 640 ? 25.551  -4.322  44.024  1.00 9.72  ? 632  GLY A N   1 
ATOM   4571  C  CA  . GLY A 1 640 ? 26.725  -5.157  44.242  1.00 8.89  ? 632  GLY A CA  1 
ATOM   4572  C  C   . GLY A 1 640 ? 27.987  -4.365  44.546  1.00 14.96 ? 632  GLY A C   1 
ATOM   4573  O  O   . GLY A 1 640 ? 27.910  -3.179  44.889  1.00 9.82  ? 632  GLY A O   1 
ATOM   4574  N  N   . GLU A 1 641 ? 29.158  -5.003  44.429  1.00 9.77  ? 633  GLU A N   1 
ATOM   4575  C  CA  . GLU A 1 641 ? 30.444  -4.336  44.635  1.00 11.35 ? 633  GLU A CA  1 
ATOM   4576  C  C   . GLU A 1 641 ? 31.463  -4.917  43.667  1.00 10.01 ? 633  GLU A C   1 
ATOM   4577  O  O   . GLU A 1 641 ? 31.383  -6.092  43.307  1.00 10.25 ? 633  GLU A O   1 
ATOM   4578  C  CB  . GLU A 1 641 ? 30.994  -4.528  46.060  1.00 11.17 ? 633  GLU A CB  1 
ATOM   4579  C  CG  . GLU A 1 641 ? 30.235  -3.820  47.181  1.00 13.62 ? 633  GLU A CG  1 
ATOM   4580  C  CD  . GLU A 1 641 ? 30.449  -2.323  47.202  1.00 16.67 ? 633  GLU A CD  1 
ATOM   4581  O  OE1 . GLU A 1 641 ? 31.389  -1.825  46.530  1.00 17.88 ? 633  GLU A OE1 1 
ATOM   4582  O  OE2 . GLU A 1 641 ? 29.663  -1.635  47.897  1.00 18.59 ? 633  GLU A OE2 1 
ATOM   4583  N  N   . SER A 1 642 ? 32.429  -4.091  43.263  1.00 10.27 ? 634  SER A N   1 
ATOM   4584  C  CA  . SER A 1 642 ? 33.521  -4.548  42.405  1.00 10.51 ? 634  SER A CA  1 
ATOM   4585  C  C   . SER A 1 642 ? 34.541  -5.293  43.261  1.00 12.33 ? 634  SER A C   1 
ATOM   4586  O  O   . SER A 1 642 ? 35.284  -4.672  44.024  1.00 12.94 ? 634  SER A O   1 
ATOM   4587  C  CB  . SER A 1 642 ? 34.163  -3.366  41.686  1.00 12.03 ? 634  SER A CB  1 
ATOM   4588  O  OG  . SER A 1 642 ? 35.287  -3.775  40.918  1.00 12.52 ? 634  SER A OG  1 
ATOM   4589  N  N   . ALA A 1 643 ? 34.574  -6.625  43.137  1.00 12.03 ? 635  ALA A N   1 
ATOM   4590  C  CA  . ALA A 1 643 ? 35.518  -7.481  43.857  1.00 14.69 ? 635  ALA A CA  1 
ATOM   4591  C  C   . ALA A 1 643 ? 35.456  -8.890  43.278  1.00 13.08 ? 635  ALA A C   1 
ATOM   4592  O  O   . ALA A 1 643 ? 34.521  -9.196  42.530  1.00 12.56 ? 635  ALA A O   1 
ATOM   4593  C  CB  . ALA A 1 643 ? 35.187  -7.512  45.353  1.00 12.28 ? 635  ALA A CB  1 
ATOM   4594  N  N   . PRO A 1 644 ? 36.418  -9.767  43.588  1.00 13.61 ? 636  PRO A N   1 
ATOM   4595  C  CA  . PRO A 1 644 ? 36.303  -11.174 43.160  1.00 13.25 ? 636  PRO A CA  1 
ATOM   4596  C  C   . PRO A 1 644 ? 35.019  -11.818 43.655  1.00 14.66 ? 636  PRO A C   1 
ATOM   4597  O  O   . PRO A 1 644 ? 34.540  -11.525 44.756  1.00 14.54 ? 636  PRO A O   1 
ATOM   4598  C  CB  . PRO A 1 644 ? 37.528  -11.840 43.793  1.00 15.20 ? 636  PRO A CB  1 
ATOM   4599  C  CG  . PRO A 1 644 ? 38.534  -10.739 43.937  1.00 14.35 ? 636  PRO A CG  1 
ATOM   4600  C  CD  . PRO A 1 644 ? 37.719  -9.488  44.227  1.00 14.49 ? 636  PRO A CD  1 
ATOM   4601  N  N   . ALA A 1 645 ? 34.488  -12.745 42.841  1.00 12.92 ? 637  ALA A N   1 
ATOM   4602  C  CA  . ALA A 1 645 ? 33.168  -13.318 43.110  1.00 14.49 ? 637  ALA A CA  1 
ATOM   4603  C  C   . ALA A 1 645 ? 33.126  -14.066 44.439  1.00 16.96 ? 637  ALA A C   1 
ATOM   4604  O  O   . ALA A 1 645 ? 32.151  -13.955 45.185  1.00 17.64 ? 637  ALA A O   1 
ATOM   4605  C  CB  . ALA A 1 645 ? 32.755  -14.263 41.978  1.00 14.16 ? 637  ALA A CB  1 
ATOM   4606  N  N   . ASP A 1 646 ? 34.152  -14.861 44.741  1.00 14.71 ? 638  ASP A N   1 
ATOM   4607  C  CA  A ASP A 1 646 ? 34.119  -15.644 45.977  0.50 19.09 ? 638  ASP A CA  1 
ATOM   4608  C  CA  C ASP A 1 646 ? 34.162  -15.644 45.976  0.50 19.26 ? 638  ASP A CA  1 
ATOM   4609  C  C   . ASP A 1 646 ? 33.954  -14.739 47.188  1.00 21.13 ? 638  ASP A C   1 
ATOM   4610  O  O   . ASP A 1 646 ? 33.186  -15.046 48.112  1.00 16.27 ? 638  ASP A O   1 
ATOM   4611  C  CB  A ASP A 1 646 ? 35.393  -16.477 46.112  0.50 23.72 ? 638  ASP A CB  1 
ATOM   4612  C  CB  C ASP A 1 646 ? 35.477  -16.417 46.108  0.50 23.96 ? 638  ASP A CB  1 
ATOM   4613  C  CG  A ASP A 1 646 ? 35.374  -17.721 45.254  0.50 26.16 ? 638  ASP A CG  1 
ATOM   4614  C  CG  C ASP A 1 646 ? 36.693  -15.500 46.167  0.50 30.89 ? 638  ASP A CG  1 
ATOM   4615  O  OD1 A ASP A 1 646 ? 34.291  -18.094 44.768  0.50 29.95 ? 638  ASP A OD1 1 
ATOM   4616  O  OD1 C ASP A 1 646 ? 37.004  -14.980 47.259  0.50 39.55 ? 638  ASP A OD1 1 
ATOM   4617  O  OD2 A ASP A 1 646 ? 36.451  -18.327 45.071  0.50 31.44 ? 638  ASP A OD2 1 
ATOM   4618  O  OD2 C ASP A 1 646 ? 37.338  -15.295 45.120  0.50 38.30 ? 638  ASP A OD2 1 
ATOM   4619  N  N   A LEU A 1 647 ? 34.659  -13.601 47.188  0.75 15.80 ? 639  LEU A N   1 
ATOM   4620  N  N   B LEU A 1 647 ? 34.618  -13.594 47.143  0.25 16.13 ? 639  LEU A N   1 
ATOM   4621  C  CA  A LEU A 1 647 ? 34.557  -12.628 48.276  0.75 14.21 ? 639  LEU A CA  1 
ATOM   4622  C  CA  B LEU A 1 647 ? 34.550  -12.681 48.270  0.25 14.86 ? 639  LEU A CA  1 
ATOM   4623  C  C   A LEU A 1 647 ? 33.176  -11.991 48.343  0.75 14.42 ? 639  LEU A C   1 
ATOM   4624  C  C   B LEU A 1 647 ? 33.202  -11.966 48.336  0.25 14.26 ? 639  LEU A C   1 
ATOM   4625  O  O   A LEU A 1 647 ? 32.667  -11.706 49.438  0.75 15.25 ? 639  LEU A O   1 
ATOM   4626  O  O   B LEU A 1 647 ? 32.733  -11.629 49.431  0.25 14.75 ? 639  LEU A O   1 
ATOM   4627  C  CB  A LEU A 1 647 ? 35.637  -11.555 48.111  0.75 14.81 ? 639  LEU A CB  1 
ATOM   4628  C  CB  B LEU A 1 647 ? 35.722  -11.710 48.175  0.25 15.86 ? 639  LEU A CB  1 
ATOM   4629  C  CG  A LEU A 1 647 ? 37.029  -12.157 48.290  0.75 16.48 ? 639  LEU A CG  1 
ATOM   4630  C  CG  B LEU A 1 647 ? 35.743  -10.502 49.078  0.25 17.70 ? 639  LEU A CG  1 
ATOM   4631  C  CD1 A LEU A 1 647 ? 38.143  -11.125 48.089  0.75 20.50 ? 639  LEU A CD1 1 
ATOM   4632  C  CD1 B LEU A 1 647 ? 37.168  -10.199 49.480  0.25 23.63 ? 639  LEU A CD1 1 
ATOM   4633  C  CD2 A LEU A 1 647 ? 37.100  -12.751 49.672  0.75 16.90 ? 639  LEU A CD2 1 
ATOM   4634  C  CD2 B LEU A 1 647 ? 35.182  -9.406  48.252  0.25 25.34 ? 639  LEU A CD2 1 
ATOM   4635  N  N   . LEU A 1 648 ? 32.559  -11.736 47.185  1.00 13.23 ? 640  LEU A N   1 
ATOM   4636  C  CA  . LEU A 1 648 ? 31.252  -11.095 47.185  1.00 13.38 ? 640  LEU A CA  1 
ATOM   4637  C  C   . LEU A 1 648 ? 30.184  -12.017 47.761  1.00 14.34 ? 640  LEU A C   1 
ATOM   4638  O  O   . LEU A 1 648 ? 29.341  -11.577 48.554  1.00 13.44 ? 640  LEU A O   1 
ATOM   4639  C  CB  . LEU A 1 648 ? 30.870  -10.665 45.765  1.00 12.96 ? 640  LEU A CB  1 
ATOM   4640  C  CG  . LEU A 1 648 ? 31.733  -9.568  45.140  1.00 14.61 ? 640  LEU A CG  1 
ATOM   4641  C  CD1 . LEU A 1 648 ? 31.342  -9.338  43.675  1.00 13.95 ? 640  LEU A CD1 1 
ATOM   4642  C  CD2 . LEU A 1 648 ? 31.598  -8.288  45.956  1.00 12.00 ? 640  LEU A CD2 1 
ATOM   4643  N  N   . PHE A 1 649 ? 30.201  -13.296 47.369  1.00 11.68 ? 641  PHE A N   1 
ATOM   4644  C  CA  . PHE A 1 649 ? 29.227  -14.245 47.906  1.00 16.07 ? 641  PHE A CA  1 
ATOM   4645  C  C   . PHE A 1 649 ? 29.343  -14.348 49.426  1.00 13.61 ? 641  PHE A C   1 
ATOM   4646  O  O   . PHE A 1 649 ? 28.331  -14.391 50.132  1.00 17.69 ? 641  PHE A O   1 
ATOM   4647  C  CB  . PHE A 1 649 ? 29.409  -15.623 47.255  1.00 12.78 ? 641  PHE A CB  1 
ATOM   4648  C  CG  . PHE A 1 649 ? 28.777  -15.751 45.882  1.00 15.02 ? 641  PHE A CG  1 
ATOM   4649  C  CD1 . PHE A 1 649 ? 27.447  -15.409 45.676  1.00 12.66 ? 641  PHE A CD1 1 
ATOM   4650  C  CD2 . PHE A 1 649 ? 29.513  -16.229 44.809  1.00 14.94 ? 641  PHE A CD2 1 
ATOM   4651  C  CE1 . PHE A 1 649 ? 26.853  -15.544 44.418  1.00 13.93 ? 641  PHE A CE1 1 
ATOM   4652  C  CE2 . PHE A 1 649 ? 28.939  -16.360 43.545  1.00 17.18 ? 641  PHE A CE2 1 
ATOM   4653  C  CZ  . PHE A 1 649 ? 27.617  -16.015 43.340  1.00 15.36 ? 641  PHE A CZ  1 
ATOM   4654  N  N   . LYS A 1 650 ? 30.572  -14.369 49.949  1.00 15.30 ? 642  LYS A N   1 
ATOM   4655  C  CA  . LYS A 1 650 ? 30.755  -14.399 51.399  1.00 14.09 ? 642  LYS A CA  1 
ATOM   4656  C  C   . LYS A 1 650 ? 30.284  -13.096 52.033  1.00 17.42 ? 642  LYS A C   1 
ATOM   4657  O  O   . LYS A 1 650 ? 29.544  -13.109 53.023  1.00 20.25 ? 642  LYS A O   1 
ATOM   4658  C  CB  . LYS A 1 650 ? 32.226  -14.669 51.738  1.00 17.81 ? 642  LYS A CB  1 
ATOM   4659  N  N   . ALA A 1 651 ? 30.693  -11.955 51.460  1.00 16.79 ? 643  ALA A N   1 
ATOM   4660  C  CA  . ALA A 1 651 ? 30.333  -10.657 52.021  1.00 19.55 ? 643  ALA A CA  1 
ATOM   4661  C  C   . ALA A 1 651 ? 28.828  -10.438 52.045  1.00 19.32 ? 643  ALA A C   1 
ATOM   4662  O  O   . ALA A 1 651 ? 28.323  -9.776  52.955  1.00 17.76 ? 643  ALA A O   1 
ATOM   4663  C  CB  . ALA A 1 651 ? 31.002  -9.529  51.234  1.00 20.53 ? 643  ALA A CB  1 
ATOM   4664  N  N   . PHE A 1 652 ? 28.093  -10.976 51.067  1.00 17.50 ? 644  PHE A N   1 
ATOM   4665  C  CA  . PHE A 1 652 ? 26.656  -10.745 50.986  1.00 18.34 ? 644  PHE A CA  1 
ATOM   4666  C  C   . PHE A 1 652 ? 25.833  -11.885 51.573  1.00 19.57 ? 644  PHE A C   1 
ATOM   4667  O  O   . PHE A 1 652 ? 24.617  -11.935 51.356  1.00 18.11 ? 644  PHE A O   1 
ATOM   4668  C  CB  . PHE A 1 652 ? 26.242  -10.465 49.538  1.00 11.70 ? 644  PHE A CB  1 
ATOM   4669  C  CG  . PHE A 1 652 ? 26.609  -9.073  49.071  1.00 11.44 ? 644  PHE A CG  1 
ATOM   4670  C  CD1 . PHE A 1 652 ? 25.946  -7.961  49.573  1.00 18.67 ? 644  PHE A CD1 1 
ATOM   4671  C  CD2 . PHE A 1 652 ? 27.631  -8.875  48.165  1.00 17.42 ? 644  PHE A CD2 1 
ATOM   4672  C  CE1 . PHE A 1 652 ? 26.286  -6.687  49.158  1.00 19.40 ? 644  PHE A CE1 1 
ATOM   4673  C  CE2 . PHE A 1 652 ? 27.972  -7.604  47.735  1.00 13.33 ? 644  PHE A CE2 1 
ATOM   4674  C  CZ  . PHE A 1 652 ? 27.316  -6.510  48.239  1.00 15.74 ? 644  PHE A CZ  1 
ATOM   4675  N  N   . GLY A 1 653 ? 26.458  -12.788 52.323  1.00 18.39 ? 645  GLY A N   1 
ATOM   4676  C  CA  . GLY A 1 653 ? 25.721  -13.770 53.094  1.00 17.51 ? 645  GLY A CA  1 
ATOM   4677  C  C   . GLY A 1 653 ? 25.297  -15.014 52.348  1.00 17.29 ? 645  GLY A C   1 
ATOM   4678  O  O   . GLY A 1 653 ? 24.452  -15.763 52.858  1.00 17.36 ? 645  GLY A O   1 
ATOM   4679  N  N   . PHE A 1 654 ? 25.837  -15.264 51.156  1.00 12.77 ? 646  PHE A N   1 
ATOM   4680  C  CA  . PHE A 1 654 ? 25.558  -16.517 50.455  1.00 14.89 ? 646  PHE A CA  1 
ATOM   4681  C  C   . PHE A 1 654 ? 26.559  -17.566 50.934  1.00 20.00 ? 646  PHE A C   1 
ATOM   4682  O  O   . PHE A 1 654 ? 27.516  -17.948 50.252  1.00 18.47 ? 646  PHE A O   1 
ATOM   4683  C  CB  . PHE A 1 654 ? 25.575  -16.299 48.950  1.00 15.92 ? 646  PHE A CB  1 
ATOM   4684  C  CG  . PHE A 1 654 ? 24.516  -15.344 48.507  1.00 12.69 ? 646  PHE A CG  1 
ATOM   4685  C  CD1 . PHE A 1 654 ? 23.201  -15.772 48.381  1.00 13.12 ? 646  PHE A CD1 1 
ATOM   4686  C  CD2 . PHE A 1 654 ? 24.808  -14.009 48.306  1.00 13.41 ? 646  PHE A CD2 1 
ATOM   4687  C  CE1 . PHE A 1 654 ? 22.207  -14.896 48.019  1.00 11.07 ? 646  PHE A CE1 1 
ATOM   4688  C  CE2 . PHE A 1 654 ? 23.820  -13.123 47.940  1.00 11.88 ? 646  PHE A CE2 1 
ATOM   4689  C  CZ  . PHE A 1 654 ? 22.506  -13.570 47.800  1.00 13.40 ? 646  PHE A CZ  1 
ATOM   4690  N  N   . THR A 1 655 ? 26.327  -17.989 52.180  1.00 17.29 ? 647  THR A N   1 
ATOM   4691  C  CA  . THR A 1 655 ? 27.183  -18.916 52.900  1.00 15.00 ? 647  THR A CA  1 
ATOM   4692  C  C   . THR A 1 655 ? 26.326  -20.012 53.523  1.00 21.01 ? 647  THR A C   1 
ATOM   4693  O  O   . THR A 1 655 ? 25.125  -19.840 53.763  1.00 19.83 ? 647  THR A O   1 
ATOM   4694  C  CB  . THR A 1 655 ? 27.973  -18.218 54.008  1.00 24.45 ? 647  THR A CB  1 
ATOM   4695  O  OG1 . THR A 1 655 ? 27.064  -17.791 55.029  1.00 24.53 ? 647  THR A OG1 1 
ATOM   4696  C  CG2 . THR A 1 655 ? 28.708  -17.002 53.463  1.00 26.57 ? 647  THR A CG2 1 
ATOM   4697  N  N   . VAL A 1 656 ? 26.961  -21.147 53.794  1.00 20.04 ? 648  VAL A N   1 
ATOM   4698  C  CA  . VAL A 1 656 ? 26.241  -22.238 54.445  1.00 23.00 ? 648  VAL A CA  1 
ATOM   4699  C  C   . VAL A 1 656 ? 25.717  -21.797 55.806  1.00 22.69 ? 648  VAL A C   1 
ATOM   4700  O  O   . VAL A 1 656 ? 24.561  -22.070 56.155  1.00 21.14 ? 648  VAL A O   1 
ATOM   4701  C  CB  . VAL A 1 656 ? 27.142  -23.477 54.548  1.00 25.76 ? 648  VAL A CB  1 
ATOM   4702  C  CG1 . VAL A 1 656 ? 26.451  -24.566 55.364  1.00 21.09 ? 648  VAL A CG1 1 
ATOM   4703  C  CG2 . VAL A 1 656 ? 27.482  -23.970 53.150  1.00 30.47 ? 648  VAL A CG2 1 
ATOM   4704  N  N   . ASP A 1 657 ? 26.545  -21.087 56.586  1.00 25.08 ? 649  ASP A N   1 
ATOM   4705  C  CA  . ASP A 1 657 ? 26.135  -20.675 57.929  1.00 26.56 ? 649  ASP A CA  1 
ATOM   4706  C  C   . ASP A 1 657 ? 24.888  -19.801 57.881  1.00 20.76 ? 649  ASP A C   1 
ATOM   4707  O  O   . ASP A 1 657 ? 23.985  -19.943 58.713  1.00 23.34 ? 649  ASP A O   1 
ATOM   4708  C  CB  . ASP A 1 657 ? 27.269  -19.923 58.632  1.00 29.04 ? 649  ASP A CB  1 
ATOM   4709  C  CG  . ASP A 1 657 ? 28.371  -20.839 59.142  1.00 36.71 ? 649  ASP A CG  1 
ATOM   4710  O  OD1 . ASP A 1 657 ? 28.228  -22.080 59.082  1.00 36.26 ? 649  ASP A OD1 1 
ATOM   4711  O  OD2 . ASP A 1 657 ? 29.398  -20.300 59.608  1.00 38.79 ? 649  ASP A OD2 1 
ATOM   4712  N  N   . ASN A 1 658 ? 24.817  -18.892 56.913  1.00 18.17 ? 650  ASN A N   1 
ATOM   4713  C  CA  . ASN A 1 658 ? 23.669  -17.995 56.852  1.00 25.56 ? 650  ASN A CA  1 
ATOM   4714  C  C   . ASN A 1 658 ? 22.403  -18.738 56.437  1.00 20.95 ? 650  ASN A C   1 
ATOM   4715  O  O   . ASN A 1 658 ? 21.328  -18.509 57.006  1.00 19.15 ? 650  ASN A O   1 
ATOM   4716  C  CB  . ASN A 1 658 ? 23.943  -16.838 55.894  1.00 22.24 ? 650  ASN A CB  1 
ATOM   4717  C  CG  . ASN A 1 658 ? 22.887  -15.766 55.988  1.00 26.43 ? 650  ASN A CG  1 
ATOM   4718  O  OD1 . ASN A 1 658 ? 22.374  -15.488 57.078  1.00 24.44 ? 650  ASN A OD1 1 
ATOM   4719  N  ND2 . ASN A 1 658 ? 22.535  -15.170 54.852  1.00 17.22 ? 650  ASN A ND2 1 
ATOM   4720  N  N   . VAL A 1 659 ? 22.500  -19.612 55.435  1.00 15.87 ? 651  VAL A N   1 
ATOM   4721  C  CA  . VAL A 1 659 ? 21.339  -20.402 55.047  1.00 17.01 ? 651  VAL A CA  1 
ATOM   4722  C  C   . VAL A 1 659 ? 20.877  -21.271 56.211  1.00 16.80 ? 651  VAL A C   1 
ATOM   4723  O  O   . VAL A 1 659 ? 19.677  -21.369 56.492  1.00 20.85 ? 651  VAL A O   1 
ATOM   4724  C  CB  . VAL A 1 659 ? 21.652  -21.248 53.800  1.00 20.16 ? 651  VAL A CB  1 
ATOM   4725  C  CG1 . VAL A 1 659 ? 20.443  -22.114 53.440  1.00 18.17 ? 651  VAL A CG1 1 
ATOM   4726  C  CG2 . VAL A 1 659 ? 22.048  -20.343 52.642  1.00 16.88 ? 651  VAL A CG2 1 
ATOM   4727  N  N   . VAL A 1 660 ? 21.824  -21.894 56.922  1.00 18.55 ? 652  VAL A N   1 
ATOM   4728  C  CA  . VAL A 1 660 ? 21.467  -22.769 58.040  1.00 22.45 ? 652  VAL A CA  1 
ATOM   4729  C  C   . VAL A 1 660 ? 20.766  -21.974 59.139  1.00 21.96 ? 652  VAL A C   1 
ATOM   4730  O  O   . VAL A 1 660 ? 19.755  -22.410 59.705  1.00 20.54 ? 652  VAL A O   1 
ATOM   4731  C  CB  . VAL A 1 660 ? 22.720  -23.489 58.578  1.00 23.51 ? 652  VAL A CB  1 
ATOM   4732  C  CG1 . VAL A 1 660 ? 22.425  -24.127 59.931  1.00 23.67 ? 652  VAL A CG1 1 
ATOM   4733  C  CG2 . VAL A 1 660 ? 23.199  -24.544 57.588  1.00 21.92 ? 652  VAL A CG2 1 
ATOM   4734  N  N   . ASP A 1 661 ? 21.312  -20.805 59.480  1.00 21.53 ? 653  ASP A N   1 
ATOM   4735  C  CA  . ASP A 1 661 ? 20.694  -19.979 60.511  1.00 25.97 ? 653  ASP A CA  1 
ATOM   4736  C  C   . ASP A 1 661 ? 19.326  -19.492 60.068  1.00 20.34 ? 653  ASP A C   1 
ATOM   4737  O  O   . ASP A 1 661 ? 18.392  -19.432 60.875  1.00 22.21 ? 653  ASP A O   1 
ATOM   4738  C  CB  . ASP A 1 661 ? 21.579  -18.777 60.848  1.00 29.05 ? 653  ASP A CB  1 
ATOM   4739  C  CG  . ASP A 1 661 ? 22.928  -19.175 61.411  1.00 37.85 ? 653  ASP A CG  1 
ATOM   4740  O  OD1 . ASP A 1 661 ? 23.071  -20.314 61.899  1.00 36.50 ? 653  ASP A OD1 1 
ATOM   4741  O  OD2 . ASP A 1 661 ? 23.849  -18.334 61.356  1.00 38.67 ? 653  ASP A OD2 1 
ATOM   4742  N  N   . THR A 1 662 ? 19.198  -19.113 58.792  1.00 20.05 ? 654  THR A N   1 
ATOM   4743  C  CA  . THR A 1 662 ? 17.916  -18.636 58.293  1.00 20.20 ? 654  THR A CA  1 
ATOM   4744  C  C   . THR A 1 662 ? 16.863  -19.734 58.356  1.00 21.19 ? 654  THR A C   1 
ATOM   4745  O  O   . THR A 1 662 ? 15.714  -19.481 58.746  1.00 23.34 ? 654  THR A O   1 
ATOM   4746  C  CB  . THR A 1 662 ? 18.071  -18.118 56.861  1.00 16.91 ? 654  THR A CB  1 
ATOM   4747  O  OG1 . THR A 1 662 ? 19.021  -17.042 56.838  1.00 21.79 ? 654  THR A OG1 1 
ATOM   4748  C  CG2 . THR A 1 662 ? 16.745  -17.622 56.328  1.00 18.02 ? 654  THR A CG2 1 
ATOM   4749  N  N   . VAL A 1 663 ? 17.229  -20.959 57.962  1.00 19.40 ? 655  VAL A N   1 
ATOM   4750  C  CA  . VAL A 1 663 ? 16.313  -22.092 58.103  1.00 19.39 ? 655  VAL A CA  1 
ATOM   4751  C  C   . VAL A 1 663 ? 15.900  -22.257 59.560  1.00 22.31 ? 655  VAL A C   1 
ATOM   4752  O  O   . VAL A 1 663 ? 14.711  -22.393 59.879  1.00 20.86 ? 655  VAL A O   1 
ATOM   4753  C  CB  . VAL A 1 663 ? 16.955  -23.379 57.551  1.00 22.42 ? 655  VAL A CB  1 
ATOM   4754  C  CG1 . VAL A 1 663 ? 16.160  -24.602 57.976  1.00 19.35 ? 655  VAL A CG1 1 
ATOM   4755  C  CG2 . VAL A 1 663 ? 17.041  -23.311 56.024  1.00 19.97 ? 655  VAL A CG2 1 
ATOM   4756  N  N   . LYS A 1 664 ? 16.879  -22.243 60.470  1.00 24.14 ? 656  LYS A N   1 
ATOM   4757  C  CA  . LYS A 1 664 ? 16.560  -22.403 61.882  1.00 25.96 ? 656  LYS A CA  1 
ATOM   4758  C  C   . LYS A 1 664 ? 15.611  -21.321 62.371  1.00 27.61 ? 656  LYS A C   1 
ATOM   4759  O  O   . LYS A 1 664 ? 14.807  -21.569 63.276  1.00 24.58 ? 656  LYS A O   1 
ATOM   4760  C  CB  . LYS A 1 664 ? 17.831  -22.376 62.728  1.00 24.74 ? 656  LYS A CB  1 
ATOM   4761  C  CG  . LYS A 1 664 ? 18.710  -23.592 62.607  1.00 32.94 ? 656  LYS A CG  1 
ATOM   4762  C  CD  . LYS A 1 664 ? 19.831  -23.493 63.623  1.00 38.57 ? 656  LYS A CD  1 
ATOM   4763  C  CE  . LYS A 1 664 ? 21.012  -24.353 63.243  1.00 44.10 ? 656  LYS A CE  1 
ATOM   4764  N  NZ  . LYS A 1 664 ? 22.120  -24.238 64.245  1.00 41.71 ? 656  LYS A NZ  1 
ATOM   4765  N  N   . SER A 1 665 ? 15.694  -20.118 61.796  1.00 26.86 ? 657  SER A N   1 
ATOM   4766  C  CA  . SER A 1 665 ? 14.907  -18.996 62.295  1.00 31.82 ? 657  SER A CA  1 
ATOM   4767  C  C   . SER A 1 665 ? 13.416  -19.140 62.006  1.00 30.23 ? 657  SER A C   1 
ATOM   4768  O  O   . SER A 1 665 ? 12.611  -18.475 62.661  1.00 26.79 ? 657  SER A O   1 
ATOM   4769  C  CB  . SER A 1 665 ? 15.419  -17.683 61.700  1.00 29.96 ? 657  SER A CB  1 
ATOM   4770  O  OG  . SER A 1 665 ? 15.025  -17.556 60.345  1.00 23.04 ? 657  SER A OG  1 
ATOM   4771  N  N   . VAL A 1 666 ? 13.020  -19.972 61.042  1.00 27.10 ? 658  VAL A N   1 
ATOM   4772  C  CA  . VAL A 1 666 ? 11.603  -20.176 60.762  1.00 23.34 ? 658  VAL A CA  1 
ATOM   4773  C  C   . VAL A 1 666 ? 11.094  -21.498 61.329  1.00 31.74 ? 658  VAL A C   1 
ATOM   4774  O  O   . VAL A 1 666 ? 9.985   -21.933 60.985  1.00 29.87 ? 658  VAL A O   1 
ATOM   4775  C  CB  . VAL A 1 666 ? 11.313  -20.069 59.261  1.00 23.11 ? 658  VAL A CB  1 
ATOM   4776  C  CG1 . VAL A 1 666 ? 11.847  -18.761 58.743  1.00 23.26 ? 658  VAL A CG1 1 
ATOM   4777  C  CG2 . VAL A 1 666 ? 11.941  -21.238 58.502  1.00 24.45 ? 658  VAL A CG2 1 
ATOM   4778  N  N   . LEU A 1 667 ? 11.875  -22.142 62.193  1.00 33.15 ? 659  LEU A N   1 
ATOM   4779  C  CA  . LEU A 1 667 ? 11.470  -23.375 62.848  1.00 42.30 ? 659  LEU A CA  1 
ATOM   4780  C  C   . LEU A 1 667 ? 11.047  -23.069 64.279  1.00 50.73 ? 659  LEU A C   1 
ATOM   4781  O  O   . LEU A 1 667 ? 11.478  -22.065 64.856  1.00 50.45 ? 659  LEU A O   1 
ATOM   4782  C  CB  . LEU A 1 667 ? 12.605  -24.403 62.843  1.00 37.09 ? 659  LEU A CB  1 
ATOM   4783  C  CG  . LEU A 1 667 ? 13.118  -24.911 61.498  1.00 34.50 ? 659  LEU A CG  1 
ATOM   4784  C  CD1 . LEU A 1 667 ? 14.221  -25.929 61.711  1.00 38.68 ? 659  LEU A CD1 1 
ATOM   4785  C  CD2 . LEU A 1 667 ? 11.990  -25.513 60.698  1.00 38.49 ? 659  LEU A CD2 1 
ATOM   4786  O  OXT . LEU A 1 667 ? 10.276  -23.817 64.886  1.00 54.27 ? 659  LEU A OXT 1 
ATOM   4787  N  N   . SER B 1 10  ? 56.212  8.873   23.787  1.00 42.80 ? 2    SER B N   1 
ATOM   4788  C  CA  . SER B 1 10  ? 56.334  9.887   24.831  1.00 45.04 ? 2    SER B CA  1 
ATOM   4789  C  C   . SER B 1 10  ? 56.154  9.294   26.226  1.00 41.45 ? 2    SER B C   1 
ATOM   4790  O  O   . SER B 1 10  ? 55.280  8.452   26.448  1.00 28.26 ? 2    SER B O   1 
ATOM   4791  C  CB  . SER B 1 10  ? 55.317  11.002  24.612  1.00 49.27 ? 2    SER B CB  1 
ATOM   4792  O  OG  . SER B 1 10  ? 55.298  11.890  25.714  1.00 53.16 ? 2    SER B OG  1 
ATOM   4793  N  N   . GLN B 1 11  ? 56.980  9.741   27.175  1.00 37.72 ? 3    GLN B N   1 
ATOM   4794  C  CA  . GLN B 1 11  ? 56.904  9.179   28.521  1.00 34.25 ? 3    GLN B CA  1 
ATOM   4795  C  C   . GLN B 1 11  ? 55.620  9.580   29.233  1.00 26.05 ? 3    GLN B C   1 
ATOM   4796  O  O   . GLN B 1 11  ? 55.105  8.808   30.049  1.00 20.32 ? 3    GLN B O   1 
ATOM   4797  C  CB  . GLN B 1 11  ? 58.123  9.605   29.336  1.00 40.81 ? 3    GLN B CB  1 
ATOM   4798  C  CG  . GLN B 1 11  ? 59.427  9.040   28.802  1.00 44.67 ? 3    GLN B CG  1 
ATOM   4799  C  CD  . GLN B 1 11  ? 59.508  7.531   28.943  1.00 49.83 ? 3    GLN B CD  1 
ATOM   4800  O  OE1 . GLN B 1 11  ? 58.871  6.782   28.194  1.00 49.09 ? 3    GLN B OE1 1 
ATOM   4801  N  NE2 . GLN B 1 11  ? 60.294  7.074   29.914  1.00 55.17 ? 3    GLN B NE2 1 
ATOM   4802  N  N   . LEU B 1 12  ? 55.083  10.767  28.925  1.00 25.11 ? 4    LEU B N   1 
ATOM   4803  C  CA  . LEU B 1 12  ? 53.857  11.228  29.573  1.00 27.51 ? 4    LEU B CA  1 
ATOM   4804  C  C   . LEU B 1 12  ? 52.654  10.372  29.193  1.00 24.41 ? 4    LEU B C   1 
ATOM   4805  O  O   . LEU B 1 12  ? 51.737  10.193  30.008  1.00 24.05 ? 4    LEU B O   1 
ATOM   4806  C  CB  . LEU B 1 12  ? 53.610  12.697  29.220  1.00 28.73 ? 4    LEU B CB  1 
ATOM   4807  C  CG  . LEU B 1 12  ? 54.883  13.536  29.370  1.00 38.96 ? 4    LEU B CG  1 
ATOM   4808  C  CD1 . LEU B 1 12  ? 54.646  14.967  28.932  1.00 41.26 ? 4    LEU B CD1 1 
ATOM   4809  C  CD2 . LEU B 1 12  ? 55.381  13.484  30.807  1.00 41.36 ? 4    LEU B CD2 1 
ATOM   4810  N  N   . ALA B 1 13  ? 52.633  9.835   27.972  1.00 21.75 ? 5    ALA B N   1 
ATOM   4811  C  CA  . ALA B 1 13  ? 51.571  8.909   27.592  1.00 22.16 ? 5    ALA B CA  1 
ATOM   4812  C  C   . ALA B 1 13  ? 51.896  7.477   27.996  1.00 24.01 ? 5    ALA B C   1 
ATOM   4813  O  O   . ALA B 1 13  ? 50.999  6.728   28.390  1.00 17.20 ? 5    ALA B O   1 
ATOM   4814  C  CB  . ALA B 1 13  ? 51.316  8.973   26.085  1.00 20.15 ? 5    ALA B CB  1 
ATOM   4815  N  N   . ASN B 1 14  ? 53.166  7.074   27.905  1.00 20.36 ? 6    ASN B N   1 
ATOM   4816  C  CA  . ASN B 1 14  ? 53.510  5.691   28.221  1.00 19.17 ? 6    ASN B CA  1 
ATOM   4817  C  C   . ASN B 1 14  ? 53.277  5.359   29.690  1.00 20.44 ? 6    ASN B C   1 
ATOM   4818  O  O   . ASN B 1 14  ? 53.019  4.197   30.021  1.00 20.24 ? 6    ASN B O   1 
ATOM   4819  C  CB  . ASN B 1 14  ? 54.962  5.400   27.829  1.00 19.55 ? 6    ASN B CB  1 
ATOM   4820  C  CG  . ASN B 1 14  ? 55.123  5.215   26.341  1.00 21.82 ? 6    ASN B CG  1 
ATOM   4821  O  OD1 . ASN B 1 14  ? 54.132  5.132   25.617  1.00 22.82 ? 6    ASN B OD1 1 
ATOM   4822  N  ND2 . ASN B 1 14  ? 56.368  5.153   25.867  1.00 22.07 ? 6    ASN B ND2 1 
ATOM   4823  N  N   . VAL B 1 15  ? 53.360  6.347   30.585  1.00 17.63 ? 7    VAL B N   1 
ATOM   4824  C  CA  . VAL B 1 15  ? 53.082  6.063   31.991  1.00 17.02 ? 7    VAL B CA  1 
ATOM   4825  C  C   . VAL B 1 15  ? 51.636  5.621   32.163  1.00 20.97 ? 7    VAL B C   1 
ATOM   4826  O  O   . VAL B 1 15  ? 51.332  4.777   33.015  1.00 16.41 ? 7    VAL B O   1 
ATOM   4827  C  CB  . VAL B 1 15  ? 53.409  7.285   32.873  1.00 18.76 ? 7    VAL B CB  1 
ATOM   4828  C  CG1 . VAL B 1 15  ? 52.465  8.470   32.556  1.00 19.13 ? 7    VAL B CG1 1 
ATOM   4829  C  CG2 . VAL B 1 15  ? 53.338  6.905   34.343  1.00 20.46 ? 7    VAL B CG2 1 
ATOM   4830  N  N   . ILE B 1 16  ? 50.725  6.168   31.354  1.00 18.96 ? 8    ILE B N   1 
ATOM   4831  C  CA  . ILE B 1 16  ? 49.342  5.699   31.385  1.00 14.90 ? 8    ILE B CA  1 
ATOM   4832  C  C   . ILE B 1 16  ? 49.268  4.248   30.933  1.00 14.83 ? 8    ILE B C   1 
ATOM   4833  O  O   . ILE B 1 16  ? 48.544  3.438   31.519  1.00 14.24 ? 8    ILE B O   1 
ATOM   4834  C  CB  . ILE B 1 16  ? 48.452  6.602   30.512  1.00 15.56 ? 8    ILE B CB  1 
ATOM   4835  C  CG1 . ILE B 1 16  ? 48.350  8.007   31.104  1.00 17.80 ? 8    ILE B CG1 1 
ATOM   4836  C  CG2 . ILE B 1 16  ? 47.049  5.991   30.366  1.00 14.17 ? 8    ILE B CG2 1 
ATOM   4837  C  CD1 . ILE B 1 16  ? 47.717  9.047   30.153  1.00 19.63 ? 8    ILE B CD1 1 
ATOM   4838  N  N   . ARG B 1 17  ? 50.013  3.896   29.877  1.00 16.63 ? 9    ARG B N   1 
ATOM   4839  C  CA  . ARG B 1 17  ? 49.995  2.519   29.390  1.00 21.67 ? 9    ARG B CA  1 
ATOM   4840  C  C   . ARG B 1 17  ? 50.427  1.549   30.476  1.00 15.44 ? 9    ARG B C   1 
ATOM   4841  O  O   . ARG B 1 17  ? 49.769  0.529   30.706  1.00 17.21 ? 9    ARG B O   1 
ATOM   4842  C  CB  . ARG B 1 17  ? 50.888  2.371   28.161  1.00 16.50 ? 9    ARG B CB  1 
ATOM   4843  C  CG  . ARG B 1 17  ? 50.469  3.255   27.011  1.00 16.75 ? 9    ARG B CG  1 
ATOM   4844  C  CD  . ARG B 1 17  ? 51.265  2.964   25.738  1.00 24.62 ? 9    ARG B CD  1 
ATOM   4845  N  NE  . ARG B 1 17  ? 50.483  3.389   24.589  1.00 20.79 ? 9    ARG B NE  1 
ATOM   4846  C  CZ  . ARG B 1 17  ? 50.543  4.594   24.039  1.00 23.07 ? 9    ARG B CZ  1 
ATOM   4847  N  NH1 . ARG B 1 17  ? 51.389  5.506   24.513  1.00 21.19 ? 9    ARG B NH1 1 
ATOM   4848  N  NH2 . ARG B 1 17  ? 49.740  4.894   23.020  1.00 25.05 ? 9    ARG B NH2 1 
ATOM   4849  N  N   . PHE B 1 18  ? 51.519  1.864   31.178  1.00 15.87 ? 10   PHE B N   1 
ATOM   4850  C  CA  . PHE B 1 18  ? 52.034  0.904   32.150  1.00 18.78 ? 10   PHE B CA  1 
ATOM   4851  C  C   . PHE B 1 18  ? 51.231  0.894   33.452  1.00 15.64 ? 10   PHE B C   1 
ATOM   4852  O  O   . PHE B 1 18  ? 50.993  -0.177  34.021  1.00 14.83 ? 10   PHE B O   1 
ATOM   4853  C  CB  . PHE B 1 18  ? 53.513  1.170   32.385  1.00 16.75 ? 10   PHE B CB  1 
ATOM   4854  C  CG  . PHE B 1 18  ? 54.358  0.754   31.218  1.00 20.29 ? 10   PHE B CG  1 
ATOM   4855  C  CD1 . PHE B 1 18  ? 54.565  -0.593  30.950  1.00 17.81 ? 10   PHE B CD1 1 
ATOM   4856  C  CD2 . PHE B 1 18  ? 54.863  1.697   30.331  1.00 20.82 ? 10   PHE B CD2 1 
ATOM   4857  C  CE1 . PHE B 1 18  ? 55.320  -0.995  29.851  1.00 19.21 ? 10   PHE B CE1 1 
ATOM   4858  C  CE2 . PHE B 1 18  ? 55.611  1.301   29.228  1.00 21.00 ? 10   PHE B CE2 1 
ATOM   4859  C  CZ  . PHE B 1 18  ? 55.842  -0.047  28.991  1.00 20.22 ? 10   PHE B CZ  1 
ATOM   4860  N  N   . LEU B 1 19  ? 50.804  2.059   33.943  1.00 14.81 ? 11   LEU B N   1 
ATOM   4861  C  CA  . LEU B 1 19  ? 49.864  2.067   35.064  1.00 16.56 ? 11   LEU B CA  1 
ATOM   4862  C  C   . LEU B 1 19  ? 48.636  1.223   34.755  1.00 14.71 ? 11   LEU B C   1 
ATOM   4863  O  O   . LEU B 1 19  ? 48.173  0.449   35.601  1.00 14.81 ? 11   LEU B O   1 
ATOM   4864  C  CB  . LEU B 1 19  ? 49.429  3.497   35.396  1.00 17.28 ? 11   LEU B CB  1 
ATOM   4865  C  CG  . LEU B 1 19  ? 50.325  4.346   36.301  1.00 21.34 ? 11   LEU B CG  1 
ATOM   4866  C  CD1 . LEU B 1 19  ? 49.681  5.719   36.498  1.00 21.89 ? 11   LEU B CD1 1 
ATOM   4867  C  CD2 . LEU B 1 19  ? 50.561  3.651   37.655  1.00 21.00 ? 11   LEU B CD2 1 
ATOM   4868  N  N   . SER B 1 20  ? 48.088  1.365   33.545  1.00 14.97 ? 12   SER B N   1 
ATOM   4869  C  CA  . SER B 1 20  ? 46.871  0.635   33.208  1.00 12.94 ? 12   SER B CA  1 
ATOM   4870  C  C   . SER B 1 20  ? 47.152  -0.856  33.064  1.00 14.13 ? 12   SER B C   1 
ATOM   4871  O  O   . SER B 1 20  ? 46.461  -1.689  33.664  1.00 16.30 ? 12   SER B O   1 
ATOM   4872  C  CB  . SER B 1 20  ? 46.254  1.202   31.930  1.00 13.40 ? 12   SER B CB  1 
ATOM   4873  O  OG  . SER B 1 20  ? 45.916  2.571   32.100  1.00 13.81 ? 12   SER B OG  1 
ATOM   4874  N  N   . ALA B 1 21  ? 48.167  -1.215  32.270  1.00 13.77 ? 13   ALA B N   1 
ATOM   4875  C  CA  . ALA B 1 21  ? 48.497  -2.625  32.108  1.00 16.95 ? 13   ALA B CA  1 
ATOM   4876  C  C   . ALA B 1 21  ? 48.895  -3.262  33.439  1.00 13.95 ? 13   ALA B C   1 
ATOM   4877  O  O   . ALA B 1 21  ? 48.450  -4.372  33.754  1.00 13.91 ? 13   ALA B O   1 
ATOM   4878  C  CB  . ALA B 1 21  ? 49.607  -2.791  31.066  1.00 14.87 ? 13   ALA B CB  1 
ATOM   4879  N  N   . ASP B 1 22  ? 49.726  -2.577  34.241  1.00 15.29 ? 14   ASP B N   1 
ATOM   4880  C  CA  . ASP B 1 22  ? 50.172  -3.157  35.510  1.00 16.65 ? 14   ASP B CA  1 
ATOM   4881  C  C   . ASP B 1 22  ? 49.019  -3.338  36.490  1.00 13.49 ? 14   ASP B C   1 
ATOM   4882  O  O   . ASP B 1 22  ? 48.968  -4.339  37.208  1.00 14.28 ? 14   ASP B O   1 
ATOM   4883  C  CB  . ASP B 1 22  ? 51.271  -2.306  36.162  1.00 14.64 ? 14   ASP B CB  1 
ATOM   4884  C  CG  . ASP B 1 22  ? 52.576  -2.305  35.368  1.00 16.07 ? 14   ASP B CG  1 
ATOM   4885  O  OD1 . ASP B 1 22  ? 52.861  -3.286  34.652  1.00 18.68 ? 14   ASP B OD1 1 
ATOM   4886  O  OD2 . ASP B 1 22  ? 53.326  -1.307  35.473  1.00 19.91 ? 14   ASP B OD2 1 
ATOM   4887  N  N   . ALA B 1 23  ? 48.102  -2.375  36.567  1.00 13.23 ? 15   ALA B N   1 
ATOM   4888  C  CA  . ALA B 1 23  ? 47.013  -2.497  37.532  1.00 14.13 ? 15   ALA B CA  1 
ATOM   4889  C  C   . ALA B 1 23  ? 46.035  -3.592  37.128  1.00 14.84 ? 15   ALA B C   1 
ATOM   4890  O  O   . ALA B 1 23  ? 45.568  -4.356  37.978  1.00 12.93 ? 15   ALA B O   1 
ATOM   4891  C  CB  . ALA B 1 23  ? 46.292  -1.163  37.686  1.00 12.30 ? 15   ALA B CB  1 
ATOM   4892  N  N   . VAL B 1 24  ? 45.710  -3.674  35.834  1.00 13.83 ? 16   VAL B N   1 
ATOM   4893  C  CA  . VAL B 1 24  ? 44.903  -4.782  35.334  1.00 13.28 ? 16   VAL B CA  1 
ATOM   4894  C  C   . VAL B 1 24  ? 45.581  -6.109  35.641  1.00 18.05 ? 16   VAL B C   1 
ATOM   4895  O  O   . VAL B 1 24  ? 44.932  -7.072  36.074  1.00 16.94 ? 16   VAL B O   1 
ATOM   4896  C  CB  . VAL B 1 24  ? 44.645  -4.612  33.822  1.00 14.24 ? 16   VAL B CB  1 
ATOM   4897  C  CG1 . VAL B 1 24  ? 44.063  -5.887  33.222  1.00 14.95 ? 16   VAL B CG1 1 
ATOM   4898  C  CG2 . VAL B 1 24  ? 43.698  -3.449  33.586  1.00 14.02 ? 16   VAL B CG2 1 
ATOM   4899  N  N   . GLN B 1 25  ? 46.898  -6.188  35.421  1.00 12.97 ? 17   GLN B N   1 
ATOM   4900  C  CA  . GLN B 1 25  ? 47.580  -7.452  35.655  1.00 13.40 ? 17   GLN B CA  1 
ATOM   4901  C  C   . GLN B 1 25  ? 47.528  -7.848  37.124  1.00 14.30 ? 17   GLN B C   1 
ATOM   4902  O  O   . GLN B 1 25  ? 47.270  -9.010  37.448  1.00 13.30 ? 17   GLN B O   1 
ATOM   4903  C  CB  . GLN B 1 25  ? 49.027  -7.382  35.180  1.00 14.12 ? 17   GLN B CB  1 
ATOM   4904  C  CG  . GLN B 1 25  ? 49.615  -8.754  34.928  1.00 14.67 ? 17   GLN B CG  1 
ATOM   4905  C  CD  . GLN B 1 25  ? 48.889  -9.521  33.830  1.00 20.33 ? 17   GLN B CD  1 
ATOM   4906  O  OE1 . GLN B 1 25  ? 48.543  -8.968  32.787  1.00 18.55 ? 17   GLN B OE1 1 
ATOM   4907  N  NE2 . GLN B 1 25  ? 48.675  -10.812 34.056  1.00 21.44 ? 17   GLN B NE2 1 
ATOM   4908  N  N   . LYS B 1 26  ? 47.773  -6.896  38.030  1.00 14.64 ? 18   LYS B N   1 
ATOM   4909  C  CA  . LYS B 1 26  ? 47.739  -7.219  39.450  1.00 15.91 ? 18   LYS B CA  1 
ATOM   4910  C  C   . LYS B 1 26  ? 46.353  -7.705  39.868  1.00 16.87 ? 18   LYS B C   1 
ATOM   4911  O  O   . LYS B 1 26  ? 46.231  -8.637  40.672  1.00 14.28 ? 18   LYS B O   1 
ATOM   4912  C  CB  . LYS B 1 26  ? 48.165  -6.000  40.267  1.00 14.85 ? 18   LYS B CB  1 
ATOM   4913  C  CG  . LYS B 1 26  ? 48.233  -6.243  41.773  1.00 16.93 ? 18   LYS B CG  1 
ATOM   4914  C  CD  . LYS B 1 26  ? 48.999  -5.121  42.480  1.00 16.32 ? 18   LYS B CD  1 
ATOM   4915  C  CE  . LYS B 1 26  ? 49.208  -5.439  43.965  1.00 18.14 ? 18   LYS B CE  1 
ATOM   4916  N  NZ  . LYS B 1 26  ? 47.909  -5.598  44.678  1.00 16.50 ? 18   LYS B NZ  1 
ATOM   4917  N  N   . ALA B 1 27  ? 45.295  -7.095  39.321  1.00 14.20 ? 19   ALA B N   1 
ATOM   4918  C  CA  . ALA B 1 27  ? 43.929  -7.552  39.592  1.00 14.04 ? 19   ALA B CA  1 
ATOM   4919  C  C   . ALA B 1 27  ? 43.600  -8.860  38.890  1.00 14.07 ? 19   ALA B C   1 
ATOM   4920  O  O   . ALA B 1 27  ? 42.599  -9.499  39.236  1.00 13.59 ? 19   ALA B O   1 
ATOM   4921  C  CB  . ALA B 1 27  ? 42.908  -6.492  39.149  1.00 11.28 ? 19   ALA B CB  1 
ATOM   4922  N  N   . ASN B 1 28  ? 44.409  -9.255  37.904  1.00 13.34 ? 20   ASN B N   1 
ATOM   4923  C  CA  . ASN B 1 28  ? 44.065  -10.326 36.967  1.00 15.86 ? 20   ASN B CA  1 
ATOM   4924  C  C   . ASN B 1 28  ? 42.653  -10.141 36.417  1.00 18.08 ? 20   ASN B C   1 
ATOM   4925  O  O   . ASN B 1 28  ? 41.882  -11.090 36.296  1.00 14.26 ? 20   ASN B O   1 
ATOM   4926  C  CB  . ASN B 1 28  ? 44.216  -11.700 37.614  1.00 26.19 ? 20   ASN B CB  1 
ATOM   4927  C  CG  . ASN B 1 28  ? 44.159  -12.823 36.597  1.00 29.89 ? 20   ASN B CG  1 
ATOM   4928  O  OD1 . ASN B 1 28  ? 44.545  -12.641 35.436  1.00 26.93 ? 20   ASN B OD1 1 
ATOM   4929  N  ND2 . ASN B 1 28  ? 43.658  -13.983 37.017  1.00 28.05 ? 20   ASN B ND2 1 
ATOM   4930  N  N   . SER B 1 29  ? 42.310  -8.898  36.085  1.00 13.58 ? 21   SER B N   1 
ATOM   4931  C  CA  . SER B 1 29  ? 40.946  -8.555  35.707  1.00 11.73 ? 21   SER B CA  1 
ATOM   4932  C  C   . SER B 1 29  ? 40.945  -7.136  35.178  1.00 13.69 ? 21   SER B C   1 
ATOM   4933  O  O   . SER B 1 29  ? 41.587  -6.263  35.762  1.00 15.03 ? 21   SER B O   1 
ATOM   4934  C  CB  . SER B 1 29  ? 39.991  -8.659  36.912  1.00 13.94 ? 21   SER B CB  1 
ATOM   4935  O  OG  . SER B 1 29  ? 38.673  -8.277  36.561  1.00 13.16 ? 21   SER B OG  1 
ATOM   4936  N  N   . GLY B 1 30  ? 40.238  -6.910  34.069  1.00 12.87 ? 22   GLY B N   1 
ATOM   4937  C  CA  . GLY B 1 30  ? 40.079  -5.562  33.578  1.00 13.00 ? 22   GLY B CA  1 
ATOM   4938  C  C   . GLY B 1 30  ? 40.454  -5.430  32.124  1.00 12.66 ? 22   GLY B C   1 
ATOM   4939  O  O   . GLY B 1 30  ? 40.751  -6.412  31.432  1.00 15.63 ? 22   GLY B O   1 
ATOM   4940  N  N   . HIS B 1 31  ? 40.470  -4.179  31.672  1.00 12.95 ? 23   HIS B N   1 
ATOM   4941  C  CA  . HIS B 1 31  ? 40.514  -3.809  30.255  1.00 13.42 ? 23   HIS B CA  1 
ATOM   4942  C  C   . HIS B 1 31  ? 41.714  -2.916  29.974  1.00 12.52 ? 23   HIS B C   1 
ATOM   4943  O  O   . HIS B 1 31  ? 41.633  -1.694  30.185  1.00 16.58 ? 23   HIS B O   1 
ATOM   4944  C  CB  . HIS B 1 31  ? 39.233  -3.070  29.871  1.00 15.17 ? 23   HIS B CB  1 
ATOM   4945  C  CG  . HIS B 1 31  ? 37.976  -3.836  30.151  1.00 19.32 ? 23   HIS B CG  1 
ATOM   4946  N  ND1 . HIS B 1 31  ? 37.482  -4.018  31.425  1.00 21.76 ? 23   HIS B ND1 1 
ATOM   4947  C  CD2 . HIS B 1 31  ? 37.100  -4.450  29.317  1.00 27.38 ? 23   HIS B CD2 1 
ATOM   4948  C  CE1 . HIS B 1 31  ? 36.365  -4.724  31.367  1.00 26.78 ? 23   HIS B CE1 1 
ATOM   4949  N  NE2 . HIS B 1 31  ? 36.102  -4.986  30.098  1.00 21.38 ? 23   HIS B NE2 1 
ATOM   4950  N  N   . PRO B 1 32  ? 42.830  -3.461  29.469  1.00 15.00 ? 24   PRO B N   1 
ATOM   4951  C  CA  . PRO B 1 32  ? 44.041  -2.647  29.305  1.00 13.47 ? 24   PRO B CA  1 
ATOM   4952  C  C   . PRO B 1 32  ? 44.153  -1.994  27.933  1.00 15.79 ? 24   PRO B C   1 
ATOM   4953  O  O   . PRO B 1 32  ? 44.867  -0.999  27.775  1.00 14.34 ? 24   PRO B O   1 
ATOM   4954  C  CB  . PRO B 1 32  ? 45.167  -3.668  29.523  1.00 16.21 ? 24   PRO B CB  1 
ATOM   4955  C  CG  . PRO B 1 32  ? 44.597  -4.949  28.953  1.00 15.47 ? 24   PRO B CG  1 
ATOM   4956  C  CD  . PRO B 1 32  ? 43.101  -4.904  29.303  1.00 16.16 ? 24   PRO B CD  1 
ATOM   4957  N  N   . GLY B 1 33  ? 43.475  -2.553  26.931  1.00 13.55 ? 25   GLY B N   1 
ATOM   4958  C  CA  . GLY B 1 33  ? 43.767  -2.170  25.554  1.00 14.31 ? 25   GLY B CA  1 
ATOM   4959  C  C   . GLY B 1 33  ? 43.263  -0.783  25.192  1.00 16.25 ? 25   GLY B C   1 
ATOM   4960  O  O   . GLY B 1 33  ? 43.956  -0.022  24.510  1.00 15.33 ? 25   GLY B O   1 
ATOM   4961  N  N   . ALA B 1 34  ? 42.044  -0.436  25.624  1.00 15.11 ? 26   ALA B N   1 
ATOM   4962  C  CA  . ALA B 1 34  ? 41.517  0.894   25.306  1.00 13.89 ? 26   ALA B CA  1 
ATOM   4963  C  C   . ALA B 1 34  ? 42.268  1.996   26.052  1.00 13.91 ? 26   ALA B C   1 
ATOM   4964  O  O   . ALA B 1 34  ? 42.568  3.035   25.453  1.00 16.25 ? 26   ALA B O   1 
ATOM   4965  C  CB  . ALA B 1 34  ? 40.013  0.986   25.603  1.00 12.79 ? 26   ALA B CB  1 
ATOM   4966  N  N   . PRO B 1 35  ? 42.581  1.843   27.346  1.00 14.71 ? 27   PRO B N   1 
ATOM   4967  C  CA  . PRO B 1 35  ? 43.488  2.823   27.974  1.00 15.70 ? 27   PRO B CA  1 
ATOM   4968  C  C   . PRO B 1 35  ? 44.769  3.047   27.191  1.00 16.72 ? 27   PRO B C   1 
ATOM   4969  O  O   . PRO B 1 35  ? 45.180  4.202   27.012  1.00 16.94 ? 27   PRO B O   1 
ATOM   4970  C  CB  . PRO B 1 35  ? 43.752  2.208   29.353  1.00 14.49 ? 27   PRO B CB  1 
ATOM   4971  C  CG  . PRO B 1 35  ? 42.439  1.534   29.665  1.00 13.29 ? 27   PRO B CG  1 
ATOM   4972  C  CD  . PRO B 1 35  ? 42.036  0.907   28.348  1.00 14.93 ? 27   PRO B CD  1 
ATOM   4973  N  N   . MET B 1 36  ? 45.394  1.977   26.683  1.00 14.57 ? 28   MET B N   1 
ATOM   4974  C  CA  . MET B 1 36  ? 46.629  2.148   25.925  1.00 15.11 ? 28   MET B CA  1 
ATOM   4975  C  C   . MET B 1 36  ? 46.371  2.852   24.602  1.00 15.59 ? 28   MET B C   1 
ATOM   4976  O  O   . MET B 1 36  ? 47.192  3.662   24.151  1.00 16.23 ? 28   MET B O   1 
ATOM   4977  C  CB  . MET B 1 36  ? 47.296  0.791   25.694  1.00 16.52 ? 28   MET B CB  1 
ATOM   4978  C  CG  . MET B 1 36  ? 47.705  0.125   26.999  1.00 16.47 ? 28   MET B CG  1 
ATOM   4979  S  SD  . MET B 1 36  ? 48.271  -1.556  26.785  1.00 17.49 ? 28   MET B SD  1 
ATOM   4980  C  CE  . MET B 1 36  ? 49.889  -1.297  26.049  1.00 17.50 ? 28   MET B CE  1 
ATOM   4981  N  N   . GLY B 1 37  ? 45.243  2.549   23.958  1.00 17.09 ? 29   GLY B N   1 
ATOM   4982  C  CA  . GLY B 1 37  ? 44.936  3.198   22.698  1.00 15.85 ? 29   GLY B CA  1 
ATOM   4983  C  C   . GLY B 1 37  ? 44.637  4.676   22.842  1.00 18.24 ? 29   GLY B C   1 
ATOM   4984  O  O   . GLY B 1 37  ? 44.889  5.456   21.916  1.00 19.85 ? 29   GLY B O   1 
ATOM   4985  N  N   . MET B 1 38  ? 44.111  5.087   23.999  1.00 14.98 ? 30   MET B N   1 
ATOM   4986  C  CA  . MET B 1 38  ? 43.673  6.460   24.210  1.00 14.83 ? 30   MET B CA  1 
ATOM   4987  C  C   . MET B 1 38  ? 44.716  7.327   24.908  1.00 21.75 ? 30   MET B C   1 
ATOM   4988  O  O   . MET B 1 38  ? 44.411  8.466   25.269  1.00 14.94 ? 30   MET B O   1 
ATOM   4989  C  CB  . MET B 1 38  ? 42.370  6.478   25.010  1.00 13.99 ? 30   MET B CB  1 
ATOM   4990  C  CG  . MET B 1 38  ? 41.167  6.072   24.184  1.00 13.89 ? 30   MET B CG  1 
ATOM   4991  S  SD  . MET B 1 38  ? 39.626  6.284   25.099  1.00 16.63 ? 30   MET B SD  1 
ATOM   4992  C  CE  . MET B 1 38  ? 39.615  4.823   26.124  1.00 17.90 ? 30   MET B CE  1 
ATOM   4993  N  N   . ALA B 1 39  ? 45.940  6.826   25.089  1.00 15.48 ? 31   ALA B N   1 
ATOM   4994  C  CA  . ALA B 1 39  ? 46.888  7.511   25.963  1.00 21.16 ? 31   ALA B CA  1 
ATOM   4995  C  C   . ALA B 1 39  ? 47.267  8.891   25.430  1.00 16.28 ? 31   ALA B C   1 
ATOM   4996  O  O   . ALA B 1 39  ? 47.398  9.840   26.210  1.00 21.13 ? 31   ALA B O   1 
ATOM   4997  C  CB  . ALA B 1 39  ? 48.139  6.653   26.164  1.00 16.11 ? 31   ALA B CB  1 
ATOM   4998  N  N   . GLU B 1 40  ? 47.490  9.020   24.113  1.00 16.99 ? 32   GLU B N   1 
ATOM   4999  C  CA  . GLU B 1 40  ? 47.849  10.330  23.566  1.00 17.68 ? 32   GLU B CA  1 
ATOM   5000  C  C   . GLU B 1 40  ? 46.660  11.276  23.579  1.00 17.24 ? 32   GLU B C   1 
ATOM   5001  O  O   . GLU B 1 40  ? 46.825  12.484  23.787  1.00 17.50 ? 32   GLU B O   1 
ATOM   5002  C  CB  . GLU B 1 40  ? 48.396  10.218  22.139  1.00 19.84 ? 32   GLU B CB  1 
ATOM   5003  C  CG  . GLU B 1 40  ? 49.874  9.873   22.046  1.00 19.51 ? 32   GLU B CG  1 
ATOM   5004  C  CD  . GLU B 1 40  ? 50.131  8.429   22.377  1.00 23.76 ? 32   GLU B CD  1 
ATOM   5005  O  OE1 . GLU B 1 40  ? 49.279  7.592   22.042  1.00 18.78 ? 32   GLU B OE1 1 
ATOM   5006  O  OE2 . GLU B 1 40  ? 51.174  8.120   22.985  1.00 19.53 ? 32   GLU B OE2 1 
ATOM   5007  N  N   . MET B 1 41  ? 45.461  10.751  23.318  1.00 16.66 ? 33   MET B N   1 
ATOM   5008  C  CA  . MET B 1 41  ? 44.266  11.576  23.444  1.00 16.98 ? 33   MET B CA  1 
ATOM   5009  C  C   . MET B 1 41  ? 44.154  12.127  24.854  1.00 16.77 ? 33   MET B C   1 
ATOM   5010  O  O   . MET B 1 41  ? 43.876  13.316  25.042  1.00 15.89 ? 33   MET B O   1 
ATOM   5011  C  CB  . MET B 1 41  ? 43.023  10.764  23.084  1.00 15.71 ? 33   MET B CB  1 
ATOM   5012  C  CG  . MET B 1 41  ? 42.966  10.340  21.614  1.00 17.73 ? 33   MET B CG  1 
ATOM   5013  S  SD  . MET B 1 41  ? 41.910  8.884   21.446  1.00 19.53 ? 33   MET B SD  1 
ATOM   5014  C  CE  . MET B 1 41  ? 40.344  9.525   22.036  1.00 16.70 ? 33   MET B CE  1 
ATOM   5015  N  N   . ALA B 1 42  ? 44.382  11.272  25.857  1.00 17.78 ? 34   ALA B N   1 
ATOM   5016  C  CA  . ALA B 1 42  ? 44.317  11.714  27.246  1.00 17.78 ? 34   ALA B CA  1 
ATOM   5017  C  C   . ALA B 1 42  ? 45.414  12.727  27.547  1.00 17.10 ? 34   ALA B C   1 
ATOM   5018  O  O   . ALA B 1 42  ? 45.147  13.781  28.130  1.00 15.91 ? 34   ALA B O   1 
ATOM   5019  C  CB  . ALA B 1 42  ? 44.422  10.520  28.187  1.00 15.18 ? 34   ALA B CB  1 
ATOM   5020  N  N   . GLU B 1 43  ? 46.652  12.438  27.134  1.00 16.76 ? 35   GLU B N   1 
ATOM   5021  C  CA  . GLU B 1 43  ? 47.750  13.358  27.415  1.00 20.36 ? 35   GLU B CA  1 
ATOM   5022  C  C   . GLU B 1 43  ? 47.465  14.740  26.845  1.00 21.95 ? 35   GLU B C   1 
ATOM   5023  O  O   . GLU B 1 43  ? 47.635  15.754  27.530  1.00 19.65 ? 35   GLU B O   1 
ATOM   5024  C  CB  . GLU B 1 43  ? 49.069  12.814  26.859  1.00 20.48 ? 35   GLU B CB  1 
ATOM   5025  C  CG  . GLU B 1 43  ? 50.246  13.735  27.158  1.00 25.31 ? 35   GLU B CG  1 
ATOM   5026  C  CD  . GLU B 1 43  ? 51.419  13.514  26.236  1.00 31.25 ? 35   GLU B CD  1 
ATOM   5027  O  OE1 . GLU B 1 43  ? 52.219  14.452  26.069  1.00 34.99 ? 35   GLU B OE1 1 
ATOM   5028  O  OE2 . GLU B 1 43  ? 51.540  12.408  25.676  1.00 30.30 ? 35   GLU B OE2 1 
ATOM   5029  N  N   . THR B 1 44  ? 47.017  14.800  25.588  1.00 17.45 ? 36   THR B N   1 
ATOM   5030  C  CA  . THR B 1 44  ? 46.781  16.094  24.960  1.00 20.11 ? 36   THR B CA  1 
ATOM   5031  C  C   . THR B 1 44  ? 45.663  16.847  25.667  1.00 17.37 ? 36   THR B C   1 
ATOM   5032  O  O   . THR B 1 44  ? 45.826  18.010  26.048  1.00 20.09 ? 36   THR B O   1 
ATOM   5033  C  CB  . THR B 1 44  ? 46.447  15.914  23.480  1.00 25.17 ? 36   THR B CB  1 
ATOM   5034  O  OG1 . THR B 1 44  ? 47.470  15.130  22.855  1.00 22.71 ? 36   THR B OG1 1 
ATOM   5035  C  CG2 . THR B 1 44  ? 46.355  17.283  22.782  1.00 26.58 ? 36   THR B CG2 1 
ATOM   5036  N  N   . LEU B 1 45  ? 44.516  16.193  25.865  1.00 16.54 ? 37   LEU B N   1 
ATOM   5037  C  CA  . LEU B 1 45  ? 43.392  16.882  26.483  1.00 16.05 ? 37   LEU B CA  1 
ATOM   5038  C  C   . LEU B 1 45  ? 43.740  17.346  27.888  1.00 15.88 ? 37   LEU B C   1 
ATOM   5039  O  O   . LEU B 1 45  ? 43.492  18.497  28.258  1.00 16.07 ? 37   LEU B O   1 
ATOM   5040  C  CB  . LEU B 1 45  ? 42.168  15.970  26.523  1.00 19.65 ? 37   LEU B CB  1 
ATOM   5041  C  CG  . LEU B 1 45  ? 40.995  16.561  27.302  1.00 16.10 ? 37   LEU B CG  1 
ATOM   5042  C  CD1 . LEU B 1 45  ? 40.565  17.890  26.701  1.00 15.52 ? 37   LEU B CD1 1 
ATOM   5043  C  CD2 . LEU B 1 45  ? 39.823  15.588  27.338  1.00 14.66 ? 37   LEU B CD2 1 
ATOM   5044  N  N   . TRP B 1 46  ? 44.308  16.455  28.694  1.00 16.58 ? 38   TRP B N   1 
ATOM   5045  C  CA  . TRP B 1 46  ? 44.447  16.773  30.104  1.00 19.43 ? 38   TRP B CA  1 
ATOM   5046  C  C   . TRP B 1 46  ? 45.612  17.724  30.365  1.00 21.78 ? 38   TRP B C   1 
ATOM   5047  O  O   . TRP B 1 46  ? 45.505  18.574  31.252  1.00 22.44 ? 38   TRP B O   1 
ATOM   5048  C  CB  . TRP B 1 46  ? 44.573  15.482  30.920  1.00 14.81 ? 38   TRP B CB  1 
ATOM   5049  C  CG  . TRP B 1 46  ? 43.207  14.867  31.240  1.00 16.23 ? 38   TRP B CG  1 
ATOM   5050  C  CD1 . TRP B 1 46  ? 42.256  14.443  30.348  1.00 13.72 ? 38   TRP B CD1 1 
ATOM   5051  C  CD2 . TRP B 1 46  ? 42.662  14.635  32.547  1.00 14.64 ? 38   TRP B CD2 1 
ATOM   5052  N  NE1 . TRP B 1 46  ? 41.138  13.968  31.029  1.00 13.05 ? 38   TRP B NE1 1 
ATOM   5053  C  CE2 . TRP B 1 46  ? 41.374  14.071  32.377  1.00 12.88 ? 38   TRP B CE2 1 
ATOM   5054  C  CE3 . TRP B 1 46  ? 43.140  14.853  33.845  1.00 15.16 ? 38   TRP B CE3 1 
ATOM   5055  C  CZ2 . TRP B 1 46  ? 40.572  13.724  33.450  1.00 15.16 ? 38   TRP B CZ2 1 
ATOM   5056  C  CZ3 . TRP B 1 46  ? 42.345  14.494  34.909  1.00 16.32 ? 38   TRP B CZ3 1 
ATOM   5057  C  CH2 . TRP B 1 46  ? 41.075  13.934  34.707  1.00 17.25 ? 38   TRP B CH2 1 
ATOM   5058  N  N   . THR B 1 47  ? 46.709  17.637  29.604  1.00 19.61 ? 39   THR B N   1 
ATOM   5059  C  CA  . THR B 1 47  ? 47.836  18.537  29.868  1.00 19.31 ? 39   THR B CA  1 
ATOM   5060  C  C   . THR B 1 47  ? 47.730  19.869  29.133  1.00 24.75 ? 39   THR B C   1 
ATOM   5061  O  O   . THR B 1 47  ? 48.321  20.856  29.583  1.00 26.10 ? 39   THR B O   1 
ATOM   5062  C  CB  . THR B 1 47  ? 49.187  17.879  29.521  1.00 21.50 ? 39   THR B CB  1 
ATOM   5063  O  OG1 . THR B 1 47  ? 49.313  17.684  28.104  1.00 20.39 ? 39   THR B OG1 1 
ATOM   5064  C  CG2 . THR B 1 47  ? 49.341  16.551  30.227  1.00 19.63 ? 39   THR B CG2 1 
ATOM   5065  N  N   . LYS B 1 48  ? 46.983  19.939  28.033  1.00 20.34 ? 40   LYS B N   1 
ATOM   5066  C  CA  . LYS B 1 48  ? 46.964  21.155  27.231  1.00 26.01 ? 40   LYS B CA  1 
ATOM   5067  C  C   . LYS B 1 48  ? 45.670  21.951  27.323  1.00 25.02 ? 40   LYS B C   1 
ATOM   5068  O  O   . LYS B 1 48  ? 45.687  23.143  27.004  1.00 25.35 ? 40   LYS B O   1 
ATOM   5069  C  CB  . LYS B 1 48  ? 47.230  20.830  25.753  1.00 23.44 ? 40   LYS B CB  1 
ATOM   5070  C  CG  . LYS B 1 48  ? 48.564  20.144  25.496  1.00 28.97 ? 40   LYS B CG  1 
ATOM   5071  C  CD  . LYS B 1 48  ? 49.711  21.135  25.527  1.00 32.69 ? 40   LYS B CD  1 
ATOM   5072  C  CE  . LYS B 1 48  ? 50.992  20.537  24.933  1.00 34.70 ? 40   LYS B CE  1 
ATOM   5073  N  NZ  . LYS B 1 48  ? 51.548  19.422  25.760  1.00 33.13 ? 40   LYS B NZ  1 
ATOM   5074  N  N   . PHE B 1 49  ? 44.563  21.343  27.759  1.00 17.83 ? 41   PHE B N   1 
ATOM   5075  C  CA  . PHE B 1 49  ? 43.280  22.030  27.652  1.00 19.96 ? 41   PHE B CA  1 
ATOM   5076  C  C   . PHE B 1 49  ? 42.435  21.972  28.916  1.00 18.09 ? 41   PHE B C   1 
ATOM   5077  O  O   . PHE B 1 49  ? 41.818  22.977  29.266  1.00 23.57 ? 41   PHE B O   1 
ATOM   5078  C  CB  . PHE B 1 49  ? 42.462  21.448  26.480  1.00 18.09 ? 41   PHE B CB  1 
ATOM   5079  C  CG  . PHE B 1 49  ? 43.053  21.740  25.138  1.00 20.40 ? 41   PHE B CG  1 
ATOM   5080  C  CD1 . PHE B 1 49  ? 42.758  22.926  24.479  1.00 20.19 ? 41   PHE B CD1 1 
ATOM   5081  C  CD2 . PHE B 1 49  ? 43.926  20.845  24.548  1.00 22.08 ? 41   PHE B CD2 1 
ATOM   5082  C  CE1 . PHE B 1 49  ? 43.311  23.206  23.249  1.00 23.79 ? 41   PHE B CE1 1 
ATOM   5083  C  CE2 . PHE B 1 49  ? 44.494  21.125  23.317  1.00 25.97 ? 41   PHE B CE2 1 
ATOM   5084  C  CZ  . PHE B 1 49  ? 44.182  22.304  22.667  1.00 26.51 ? 41   PHE B CZ  1 
ATOM   5085  N  N   . LEU B 1 50  ? 42.376  20.828  29.595  1.00 17.90 ? 42   LEU B N   1 
ATOM   5086  C  CA  . LEU B 1 50  ? 41.391  20.641  30.658  1.00 17.21 ? 42   LEU B CA  1 
ATOM   5087  C  C   . LEU B 1 50  ? 41.661  21.598  31.811  1.00 20.31 ? 42   LEU B C   1 
ATOM   5088  O  O   . LEU B 1 50  ? 42.774  21.649  32.341  1.00 16.97 ? 42   LEU B O   1 
ATOM   5089  C  CB  . LEU B 1 50  ? 41.420  19.196  31.164  1.00 14.81 ? 42   LEU B CB  1 
ATOM   5090  C  CG  . LEU B 1 50  ? 40.287  18.768  32.099  1.00 18.57 ? 42   LEU B CG  1 
ATOM   5091  C  CD1 . LEU B 1 50  ? 38.995  18.622  31.316  1.00 16.33 ? 42   LEU B CD1 1 
ATOM   5092  C  CD2 . LEU B 1 50  ? 40.629  17.460  32.824  1.00 17.83 ? 42   LEU B CD2 1 
ATOM   5093  N  N   . ASN B 1 51  ? 40.634  22.348  32.210  1.00 17.74 ? 43   ASN B N   1 
ATOM   5094  C  CA  . ASN B 1 51  ? 40.738  23.297  33.317  1.00 18.86 ? 43   ASN B CA  1 
ATOM   5095  C  C   . ASN B 1 51  ? 40.110  22.671  34.558  1.00 17.97 ? 43   ASN B C   1 
ATOM   5096  O  O   . ASN B 1 51  ? 38.888  22.559  34.652  1.00 18.82 ? 43   ASN B O   1 
ATOM   5097  C  CB  . ASN B 1 51  ? 40.074  24.623  32.952  1.00 21.40 ? 43   ASN B CB  1 
ATOM   5098  C  CG  . ASN B 1 51  ? 40.885  25.409  31.960  1.00 19.14 ? 43   ASN B CG  1 
ATOM   5099  O  OD1 . ASN B 1 51  ? 42.101  25.502  32.093  1.00 17.74 ? 43   ASN B OD1 1 
ATOM   5100  N  ND2 . ASN B 1 51  ? 40.225  25.972  30.946  1.00 20.15 ? 43   ASN B ND2 1 
ATOM   5101  N  N   . HIS B 1 52  ? 40.948  22.265  35.511  1.00 16.44 ? 44   HIS B N   1 
ATOM   5102  C  CA  . HIS B 1 52  ? 40.456  21.547  36.676  1.00 17.12 ? 44   HIS B CA  1 
ATOM   5103  C  C   . HIS B 1 52  ? 41.396  21.813  37.850  1.00 21.37 ? 44   HIS B C   1 
ATOM   5104  O  O   . HIS B 1 52  ? 42.566  22.158  37.663  1.00 19.25 ? 44   HIS B O   1 
ATOM   5105  C  CB  . HIS B 1 52  ? 40.348  20.042  36.386  1.00 16.99 ? 44   HIS B CB  1 
ATOM   5106  C  CG  . HIS B 1 52  ? 41.674  19.393  36.091  1.00 14.32 ? 44   HIS B CG  1 
ATOM   5107  N  ND1 . HIS B 1 52  ? 42.144  18.304  36.797  1.00 14.02 ? 44   HIS B ND1 1 
ATOM   5108  C  CD2 . HIS B 1 52  ? 42.625  19.686  35.172  1.00 16.12 ? 44   HIS B CD2 1 
ATOM   5109  C  CE1 . HIS B 1 52  ? 43.330  17.957  36.325  1.00 19.14 ? 44   HIS B CE1 1 
ATOM   5110  N  NE2 . HIS B 1 52  ? 43.640  18.773  35.332  1.00 18.76 ? 44   HIS B NE2 1 
ATOM   5111  N  N   . ASN B 1 53  ? 40.879  21.631  39.065  1.00 16.99 ? 45   ASN B N   1 
ATOM   5112  C  CA  . ASN B 1 53  ? 41.676  21.814  40.281  1.00 17.59 ? 45   ASN B CA  1 
ATOM   5113  C  C   . ASN B 1 53  ? 41.661  20.543  41.126  1.00 17.21 ? 45   ASN B C   1 
ATOM   5114  O  O   . ASN B 1 53  ? 40.681  20.279  41.843  1.00 14.63 ? 45   ASN B O   1 
ATOM   5115  C  CB  . ASN B 1 53  ? 41.175  23.006  41.095  1.00 19.31 ? 45   ASN B CB  1 
ATOM   5116  C  CG  . ASN B 1 53  ? 42.059  23.299  42.292  1.00 19.69 ? 45   ASN B CG  1 
ATOM   5117  O  OD1 . ASN B 1 53  ? 43.151  22.742  42.413  1.00 21.14 ? 45   ASN B OD1 1 
ATOM   5118  N  ND2 . ASN B 1 53  ? 41.597  24.183  43.181  1.00 16.81 ? 45   ASN B ND2 1 
ATOM   5119  N  N   . PRO B 1 54  ? 42.727  19.741  41.096  1.00 15.94 ? 46   PRO B N   1 
ATOM   5120  C  CA  . PRO B 1 54  ? 42.762  18.517  41.917  1.00 20.18 ? 46   PRO B CA  1 
ATOM   5121  C  C   . PRO B 1 54  ? 42.510  18.753  43.396  1.00 23.54 ? 46   PRO B C   1 
ATOM   5122  O  O   . PRO B 1 54  ? 41.979  17.866  44.078  1.00 21.80 ? 46   PRO B O   1 
ATOM   5123  C  CB  . PRO B 1 54  ? 44.184  17.980  41.686  1.00 23.88 ? 46   PRO B CB  1 
ATOM   5124  C  CG  . PRO B 1 54  ? 44.614  18.568  40.398  1.00 25.65 ? 46   PRO B CG  1 
ATOM   5125  C  CD  . PRO B 1 54  ? 43.946  19.914  40.294  1.00 20.27 ? 46   PRO B CD  1 
ATOM   5126  N  N   . ALA B 1 55  ? 42.885  19.918  43.918  1.00 20.63 ? 47   ALA B N   1 
ATOM   5127  C  CA  . ALA B 1 55  ? 42.649  20.204  45.328  1.00 22.64 ? 47   ALA B CA  1 
ATOM   5128  C  C   . ALA B 1 55  ? 41.173  20.430  45.644  1.00 23.50 ? 47   ALA B C   1 
ATOM   5129  O  O   . ALA B 1 55  ? 40.792  20.369  46.819  1.00 18.93 ? 47   ALA B O   1 
ATOM   5130  C  CB  . ALA B 1 55  ? 43.465  21.424  45.761  1.00 22.19 ? 47   ALA B CB  1 
ATOM   5131  N  N   . ASN B 1 56  ? 40.338  20.705  44.638  1.00 19.75 ? 48   ASN B N   1 
ATOM   5132  C  CA  . ASN B 1 56  ? 38.902  20.892  44.850  1.00 15.69 ? 48   ASN B CA  1 
ATOM   5133  C  C   . ASN B 1 56  ? 38.158  20.256  43.691  1.00 17.56 ? 48   ASN B C   1 
ATOM   5134  O  O   . ASN B 1 56  ? 37.816  20.931  42.709  1.00 18.70 ? 48   ASN B O   1 
ATOM   5135  C  CB  . ASN B 1 56  ? 38.536  22.373  44.980  1.00 15.76 ? 48   ASN B CB  1 
ATOM   5136  C  CG  . ASN B 1 56  ? 37.043  22.589  45.233  1.00 15.58 ? 48   ASN B CG  1 
ATOM   5137  O  OD1 . ASN B 1 56  ? 36.287  21.634  45.411  1.00 19.90 ? 48   ASN B OD1 1 
ATOM   5138  N  ND2 . ASN B 1 56  ? 36.618  23.845  45.244  1.00 18.31 ? 48   ASN B ND2 1 
ATOM   5139  N  N   . PRO B 1 57  ? 37.874  18.953  43.778  1.00 20.99 ? 49   PRO B N   1 
ATOM   5140  C  CA  . PRO B 1 57  ? 37.132  18.278  42.698  1.00 18.52 ? 49   PRO B CA  1 
ATOM   5141  C  C   . PRO B 1 57  ? 35.746  18.848  42.447  1.00 17.95 ? 49   PRO B C   1 
ATOM   5142  O  O   . PRO B 1 57  ? 35.148  18.536  41.406  1.00 15.26 ? 49   PRO B O   1 
ATOM   5143  C  CB  . PRO B 1 57  ? 37.050  16.825  43.188  1.00 19.44 ? 49   PRO B CB  1 
ATOM   5144  C  CG  . PRO B 1 57  ? 38.248  16.676  44.106  1.00 22.59 ? 49   PRO B CG  1 
ATOM   5145  C  CD  . PRO B 1 57  ? 38.352  18.005  44.802  1.00 18.38 ? 49   PRO B CD  1 
ATOM   5146  N  N   . LYS B 1 58  ? 35.210  19.652  43.367  1.00 18.10 ? 50   LYS B N   1 
ATOM   5147  C  CA  . LYS B 1 58  ? 33.886  20.252  43.226  1.00 19.23 ? 50   LYS B CA  1 
ATOM   5148  C  C   . LYS B 1 58  ? 33.928  21.712  42.787  1.00 15.37 ? 50   LYS B C   1 
ATOM   5149  O  O   . LYS B 1 58  ? 32.887  22.376  42.826  1.00 17.52 ? 50   LYS B O   1 
ATOM   5150  C  CB  . LYS B 1 58  ? 33.099  20.146  44.541  1.00 17.53 ? 50   LYS B CB  1 
ATOM   5151  C  CG  . LYS B 1 58  ? 32.759  18.717  44.966  1.00 20.11 ? 50   LYS B CG  1 
ATOM   5152  C  CD  . LYS B 1 58  ? 32.144  17.951  43.826  1.00 30.52 ? 50   LYS B CD  1 
ATOM   5153  C  CE  . LYS B 1 58  ? 31.828  16.513  44.217  1.00 41.44 ? 50   LYS B CE  1 
ATOM   5154  N  NZ  . LYS B 1 58  ? 31.740  15.663  42.995  1.00 43.50 ? 50   LYS B NZ  1 
ATOM   5155  N  N   . PHE B 1 59  ? 35.100  22.230  42.396  1.00 17.81 ? 51   PHE B N   1 
ATOM   5156  C  CA  . PHE B 1 59  ? 35.216  23.590  41.866  1.00 17.63 ? 51   PHE B CA  1 
ATOM   5157  C  C   . PHE B 1 59  ? 34.107  23.862  40.858  1.00 14.72 ? 51   PHE B C   1 
ATOM   5158  O  O   . PHE B 1 59  ? 33.970  23.135  39.873  1.00 16.00 ? 51   PHE B O   1 
ATOM   5159  C  CB  . PHE B 1 59  ? 36.602  23.777  41.226  1.00 16.01 ? 51   PHE B CB  1 
ATOM   5160  C  CG  . PHE B 1 59  ? 36.744  25.022  40.382  1.00 17.76 ? 51   PHE B CG  1 
ATOM   5161  C  CD1 . PHE B 1 59  ? 36.344  26.266  40.857  1.00 17.90 ? 51   PHE B CD1 1 
ATOM   5162  C  CD2 . PHE B 1 59  ? 37.314  24.950  39.115  1.00 19.85 ? 51   PHE B CD2 1 
ATOM   5163  C  CE1 . PHE B 1 59  ? 36.496  27.416  40.069  1.00 16.83 ? 51   PHE B CE1 1 
ATOM   5164  C  CE2 . PHE B 1 59  ? 37.471  26.092  38.329  1.00 19.97 ? 51   PHE B CE2 1 
ATOM   5165  C  CZ  . PHE B 1 59  ? 37.052  27.322  38.811  1.00 17.48 ? 51   PHE B CZ  1 
ATOM   5166  N  N   . TYR B 1 60  ? 33.301  24.900  41.129  1.00 15.18 ? 52   TYR B N   1 
ATOM   5167  C  CA  . TYR B 1 60  ? 32.037  25.078  40.410  1.00 22.09 ? 52   TYR B CA  1 
ATOM   5168  C  C   . TYR B 1 60  ? 32.240  25.199  38.906  1.00 19.64 ? 52   TYR B C   1 
ATOM   5169  O  O   . TYR B 1 60  ? 31.415  24.709  38.124  1.00 19.69 ? 52   TYR B O   1 
ATOM   5170  C  CB  . TYR B 1 60  ? 31.293  26.323  40.895  1.00 21.66 ? 52   TYR B CB  1 
ATOM   5171  C  CG  . TYR B 1 60  ? 30.859  26.327  42.333  1.00 22.43 ? 52   TYR B CG  1 
ATOM   5172  C  CD1 . TYR B 1 60  ? 30.602  25.144  43.019  1.00 20.71 ? 52   TYR B CD1 1 
ATOM   5173  C  CD2 . TYR B 1 60  ? 30.691  27.532  43.005  1.00 22.64 ? 52   TYR B CD2 1 
ATOM   5174  C  CE1 . TYR B 1 60  ? 30.207  25.166  44.349  1.00 18.79 ? 52   TYR B CE1 1 
ATOM   5175  C  CE2 . TYR B 1 60  ? 30.291  27.566  44.323  1.00 26.83 ? 52   TYR B CE2 1 
ATOM   5176  C  CZ  . TYR B 1 60  ? 30.047  26.386  44.991  1.00 23.03 ? 52   TYR B CZ  1 
ATOM   5177  O  OH  . TYR B 1 60  ? 29.643  26.441  46.305  1.00 24.73 ? 52   TYR B OH  1 
ATOM   5178  N  N   . ASN B 1 61  ? 33.295  25.897  38.480  1.00 17.52 ? 53   ASN B N   1 
ATOM   5179  C  CA  . ASN B 1 61  ? 33.486  26.204  37.066  1.00 22.39 ? 53   ASN B CA  1 
ATOM   5180  C  C   . ASN B 1 61  ? 34.526  25.305  36.400  1.00 19.90 ? 53   ASN B C   1 
ATOM   5181  O  O   . ASN B 1 61  ? 35.047  25.655  35.338  1.00 15.51 ? 53   ASN B O   1 
ATOM   5182  C  CB  . ASN B 1 61  ? 33.871  27.672  36.875  1.00 20.87 ? 53   ASN B CB  1 
ATOM   5183  C  CG  . ASN B 1 61  ? 33.616  28.156  35.450  1.00 20.22 ? 53   ASN B CG  1 
ATOM   5184  O  OD1 . ASN B 1 61  ? 32.562  27.872  34.868  1.00 20.57 ? 53   ASN B OD1 1 
ATOM   5185  N  ND2 . ASN B 1 61  ? 34.593  28.852  34.870  1.00 18.11 ? 53   ASN B ND2 1 
ATOM   5186  N  N   . ARG B 1 62  ? 34.849  24.165  37.004  1.00 14.72 ? 54   ARG B N   1 
ATOM   5187  C  CA  . ARG B 1 62  ? 35.763  23.228  36.367  1.00 14.44 ? 54   ARG B CA  1 
ATOM   5188  C  C   . ARG B 1 62  ? 35.172  22.718  35.055  1.00 18.25 ? 54   ARG B C   1 
ATOM   5189  O  O   . ARG B 1 62  ? 33.950  22.589  34.907  1.00 16.82 ? 54   ARG B O   1 
ATOM   5190  C  CB  . ARG B 1 62  ? 36.033  22.048  37.301  1.00 16.49 ? 54   ARG B CB  1 
ATOM   5191  C  CG  . ARG B 1 62  ? 34.817  21.109  37.432  1.00 13.74 ? 54   ARG B CG  1 
ATOM   5192  C  CD  . ARG B 1 62  ? 35.032  20.058  38.516  1.00 13.96 ? 54   ARG B CD  1 
ATOM   5193  N  NE  . ARG B 1 62  ? 33.900  19.134  38.597  1.00 13.45 ? 54   ARG B NE  1 
ATOM   5194  C  CZ  . ARG B 1 62  ? 32.786  19.375  39.283  1.00 18.45 ? 54   ARG B CZ  1 
ATOM   5195  N  NH1 . ARG B 1 62  ? 32.639  20.515  39.952  1.00 14.54 ? 54   ARG B NH1 1 
ATOM   5196  N  NH2 . ARG B 1 62  ? 31.813  18.473  39.300  1.00 19.27 ? 54   ARG B NH2 1 
ATOM   5197  N  N   . ASP B 1 63  ? 36.044  22.441  34.084  1.00 14.87 ? 55   ASP B N   1 
ATOM   5198  C  CA  . ASP B 1 63  ? 35.607  21.626  32.959  1.00 14.38 ? 55   ASP B CA  1 
ATOM   5199  C  C   . ASP B 1 63  ? 35.167  20.261  33.474  1.00 13.27 ? 55   ASP B C   1 
ATOM   5200  O  O   . ASP B 1 63  ? 35.687  19.756  34.473  1.00 15.22 ? 55   ASP B O   1 
ATOM   5201  C  CB  . ASP B 1 63  ? 36.723  21.443  31.931  1.00 16.99 ? 55   ASP B CB  1 
ATOM   5202  C  CG  . ASP B 1 63  ? 37.082  22.724  31.200  1.00 17.60 ? 55   ASP B CG  1 
ATOM   5203  O  OD1 . ASP B 1 63  ? 36.235  23.645  31.104  1.00 19.09 ? 55   ASP B OD1 1 
ATOM   5204  O  OD2 . ASP B 1 63  ? 38.230  22.790  30.706  1.00 16.97 ? 55   ASP B OD2 1 
ATOM   5205  N  N   . ARG B 1 64  ? 34.188  19.664  32.801  1.00 12.98 ? 56   ARG B N   1 
ATOM   5206  C  CA  . ARG B 1 64  ? 33.727  18.319  33.125  1.00 13.66 ? 56   ARG B CA  1 
ATOM   5207  C  C   . ARG B 1 64  ? 34.303  17.334  32.111  1.00 14.60 ? 56   ARG B C   1 
ATOM   5208  O  O   . ARG B 1 64  ? 34.187  17.549  30.898  1.00 19.74 ? 56   ARG B O   1 
ATOM   5209  C  CB  . ARG B 1 64  ? 32.198  18.242  33.114  1.00 13.57 ? 56   ARG B CB  1 
ATOM   5210  C  CG  . ARG B 1 64  ? 31.518  18.532  34.459  1.00 18.45 ? 56   ARG B CG  1 
ATOM   5211  C  CD  . ARG B 1 64  ? 31.756  19.951  34.977  1.00 16.29 ? 56   ARG B CD  1 
ATOM   5212  N  NE  . ARG B 1 64  ? 30.887  20.254  36.118  1.00 18.56 ? 56   ARG B NE  1 
ATOM   5213  C  CZ  . ARG B 1 64  ? 30.882  21.404  36.791  1.00 14.83 ? 56   ARG B CZ  1 
ATOM   5214  N  NH1 . ARG B 1 64  ? 31.708  22.380  36.465  1.00 13.60 ? 56   ARG B NH1 1 
ATOM   5215  N  NH2 . ARG B 1 64  ? 30.043  21.579  37.795  1.00 17.04 ? 56   ARG B NH2 1 
ATOM   5216  N  N   . PHE B 1 65  ? 34.928  16.270  32.607  1.00 15.12 ? 57   PHE B N   1 
ATOM   5217  C  CA  . PHE B 1 65  ? 35.400  15.168  31.772  1.00 12.66 ? 57   PHE B CA  1 
ATOM   5218  C  C   . PHE B 1 65  ? 34.550  13.933  32.037  1.00 14.58 ? 57   PHE B C   1 
ATOM   5219  O  O   . PHE B 1 65  ? 34.301  13.588  33.198  1.00 12.49 ? 57   PHE B O   1 
ATOM   5220  C  CB  . PHE B 1 65  ? 36.868  14.829  32.046  1.00 13.55 ? 57   PHE B CB  1 
ATOM   5221  C  CG  . PHE B 1 65  ? 37.373  13.662  31.230  1.00 19.58 ? 57   PHE B CG  1 
ATOM   5222  C  CD1 . PHE B 1 65  ? 37.614  13.805  29.866  1.00 12.30 ? 57   PHE B CD1 1 
ATOM   5223  C  CD2 . PHE B 1 65  ? 37.584  12.420  31.817  1.00 11.55 ? 57   PHE B CD2 1 
ATOM   5224  C  CE1 . PHE B 1 65  ? 38.062  12.727  29.103  1.00 16.08 ? 57   PHE B CE1 1 
ATOM   5225  C  CE2 . PHE B 1 65  ? 38.027  11.337  31.061  1.00 15.87 ? 57   PHE B CE2 1 
ATOM   5226  C  CZ  . PHE B 1 65  ? 38.275  11.492  29.701  1.00 12.76 ? 57   PHE B CZ  1 
ATOM   5227  N  N   . VAL B 1 66  ? 34.140  13.253  30.964  1.00 14.06 ? 58   VAL B N   1 
ATOM   5228  C  CA  . VAL B 1 66  ? 33.334  12.036  31.046  1.00 12.70 ? 58   VAL B CA  1 
ATOM   5229  C  C   . VAL B 1 66  ? 33.991  10.954  30.201  1.00 15.34 ? 58   VAL B C   1 
ATOM   5230  O  O   . VAL B 1 66  ? 34.196  11.143  28.996  1.00 12.38 ? 58   VAL B O   1 
ATOM   5231  C  CB  . VAL B 1 66  ? 31.893  12.266  30.568  1.00 11.02 ? 58   VAL B CB  1 
ATOM   5232  C  CG1 . VAL B 1 66  ? 31.176  10.918  30.401  1.00 11.62 ? 58   VAL B CG1 1 
ATOM   5233  C  CG2 . VAL B 1 66  ? 31.124  13.181  31.551  1.00 11.27 ? 58   VAL B CG2 1 
ATOM   5234  N  N   . LEU B 1 67  ? 34.295  9.816   30.819  1.00 16.18 ? 59   LEU B N   1 
ATOM   5235  C  CA  . LEU B 1 67  ? 34.831  8.652   30.106  1.00 12.06 ? 59   LEU B CA  1 
ATOM   5236  C  C   . LEU B 1 67  ? 33.642  7.754   29.794  1.00 14.56 ? 59   LEU B C   1 
ATOM   5237  O  O   . LEU B 1 67  ? 33.225  6.949   30.625  1.00 15.35 ? 59   LEU B O   1 
ATOM   5238  C  CB  . LEU B 1 67  ? 35.871  7.914   30.946  1.00 13.73 ? 59   LEU B CB  1 
ATOM   5239  C  CG  . LEU B 1 67  ? 36.422  6.625   30.329  1.00 15.47 ? 59   LEU B CG  1 
ATOM   5240  C  CD1 . LEU B 1 67  ? 37.375  6.940   29.184  1.00 12.25 ? 59   LEU B CD1 1 
ATOM   5241  C  CD2 . LEU B 1 67  ? 37.119  5.769   31.386  1.00 17.48 ? 59   LEU B CD2 1 
ATOM   5242  N  N   . SER B 1 68  ? 33.075  7.908   28.591  1.00 13.24 ? 60   SER B N   1 
ATOM   5243  C  CA  . SER B 1 68  ? 31.854  7.171   28.275  1.00 14.18 ? 60   SER B CA  1 
ATOM   5244  C  C   . SER B 1 68  ? 32.132  5.681   28.101  1.00 14.60 ? 60   SER B C   1 
ATOM   5245  O  O   . SER B 1 68  ? 31.324  4.845   28.513  1.00 17.07 ? 60   SER B O   1 
ATOM   5246  C  CB  . SER B 1 68  ? 31.189  7.752   27.027  1.00 13.14 ? 60   SER B CB  1 
ATOM   5247  O  OG  . SER B 1 68  ? 29.870  7.229   26.871  1.00 15.74 ? 60   SER B OG  1 
ATOM   5248  N  N   . ASN B 1 69  ? 33.268  5.321   27.506  1.00 18.20 ? 61   ASN B N   1 
ATOM   5249  C  CA  . ASN B 1 69  ? 33.653  3.909   27.428  1.00 20.57 ? 61   ASN B CA  1 
ATOM   5250  C  C   . ASN B 1 69  ? 34.265  3.509   28.773  1.00 15.40 ? 61   ASN B C   1 
ATOM   5251  O  O   . ASN B 1 69  ? 35.482  3.422   28.943  1.00 19.09 ? 61   ASN B O   1 
ATOM   5252  C  CB  . ASN B 1 69  ? 34.597  3.662   26.253  1.00 21.28 ? 61   ASN B CB  1 
ATOM   5253  C  CG  . ASN B 1 69  ? 35.560  4.831   25.987  1.00 18.72 ? 61   ASN B CG  1 
ATOM   5254  O  OD1 . ASN B 1 69  ? 35.611  5.800   26.733  1.00 26.69 ? 61   ASN B OD1 1 
ATOM   5255  N  ND2 . ASN B 1 69  ? 36.331  4.728   24.900  1.00 22.14 ? 61   ASN B ND2 1 
ATOM   5256  N  N   . GLY B 1 70  ? 33.382  3.218   29.740  1.00 20.58 ? 62   GLY B N   1 
ATOM   5257  C  CA  . GLY B 1 70  ? 33.751  3.134   31.151  1.00 17.81 ? 62   GLY B CA  1 
ATOM   5258  C  C   . GLY B 1 70  ? 34.617  1.950   31.528  1.00 23.57 ? 62   GLY B C   1 
ATOM   5259  O  O   . GLY B 1 70  ? 35.292  2.002   32.560  1.00 21.02 ? 62   GLY B O   1 
ATOM   5260  N  N   . HIS B 1 71  ? 34.605  0.883   30.724  1.00 18.57 ? 63   HIS B N   1 
ATOM   5261  C  CA  . HIS B 1 71  ? 35.502  -0.246  30.965  1.00 23.34 ? 63   HIS B CA  1 
ATOM   5262  C  C   . HIS B 1 71  ? 36.961  0.188   30.980  1.00 21.80 ? 63   HIS B C   1 
ATOM   5263  O  O   . HIS B 1 71  ? 37.781  -0.419  31.676  1.00 23.97 ? 63   HIS B O   1 
ATOM   5264  C  CB  . HIS B 1 71  ? 35.292  -1.307  29.893  1.00 26.05 ? 63   HIS B CB  1 
ATOM   5265  C  CG  . HIS B 1 71  ? 35.343  -0.761  28.503  1.00 24.97 ? 63   HIS B CG  1 
ATOM   5266  N  ND1 . HIS B 1 71  ? 34.217  -0.346  27.826  1.00 25.83 ? 63   HIS B ND1 1 
ATOM   5267  C  CD2 . HIS B 1 71  ? 36.386  -0.547  27.667  1.00 29.79 ? 63   HIS B CD2 1 
ATOM   5268  C  CE1 . HIS B 1 71  ? 34.562  0.093   26.630  1.00 31.75 ? 63   HIS B CE1 1 
ATOM   5269  N  NE2 . HIS B 1 71  ? 35.874  -0.015  26.509  1.00 27.10 ? 63   HIS B NE2 1 
ATOM   5270  N  N   . ALA B 1 72  ? 37.299  1.233   30.220  1.00 14.75 ? 64   ALA B N   1 
ATOM   5271  C  CA  . ALA B 1 72  ? 38.642  1.804   30.175  1.00 10.94 ? 64   ALA B CA  1 
ATOM   5272  C  C   . ALA B 1 72  ? 38.988  2.545   31.462  1.00 11.90 ? 64   ALA B C   1 
ATOM   5273  O  O   . ALA B 1 72  ? 39.710  3.548   31.435  1.00 12.76 ? 64   ALA B O   1 
ATOM   5274  C  CB  . ALA B 1 72  ? 38.759  2.748   28.978  1.00 11.31 ? 64   ALA B CB  1 
ATOM   5275  N  N   . SER B 1 73  ? 38.493  2.031   32.595  1.00 12.50 ? 65   SER B N   1 
ATOM   5276  C  CA  . SER B 1 73  ? 38.544  2.758   33.858  1.00 17.07 ? 65   SER B CA  1 
ATOM   5277  C  C   . SER B 1 73  ? 39.964  3.122   34.270  1.00 10.46 ? 65   SER B C   1 
ATOM   5278  O  O   . SER B 1 73  ? 40.180  4.177   34.873  1.00 13.00 ? 65   SER B O   1 
ATOM   5279  C  CB  . SER B 1 73  ? 37.877  1.928   34.956  1.00 17.30 ? 65   SER B CB  1 
ATOM   5280  O  OG  . SER B 1 73  ? 38.475  0.649   35.021  1.00 16.95 ? 65   SER B OG  1 
ATOM   5281  N  N   . MET B 1 74  ? 40.949  2.254   33.996  1.00 10.72 ? 66   MET B N   1 
ATOM   5282  C  CA  . MET B 1 74  ? 42.305  2.588   34.423  1.00 12.90 ? 66   MET B CA  1 
ATOM   5283  C  C   . MET B 1 74  ? 42.840  3.819   33.701  1.00 12.97 ? 66   MET B C   1 
ATOM   5284  O  O   . MET B 1 74  ? 43.758  4.468   34.211  1.00 12.14 ? 66   MET B O   1 
ATOM   5285  C  CB  . MET B 1 74  ? 43.269  1.401   34.227  1.00 12.20 ? 66   MET B CB  1 
ATOM   5286  C  CG  . MET B 1 74  ? 43.291  0.402   35.398  1.00 11.20 ? 66   MET B CG  1 
ATOM   5287  S  SD  . MET B 1 74  ? 43.674  1.200   36.970  1.00 15.20 ? 66   MET B SD  1 
ATOM   5288  C  CE  . MET B 1 74  ? 45.202  2.067   36.564  1.00 12.76 ? 66   MET B CE  1 
ATOM   5289  N  N   . LEU B 1 75  ? 42.283  4.171   32.537  1.00 14.08 ? 67   LEU B N   1 
ATOM   5290  C  CA  . LEU B 1 75  ? 42.676  5.430   31.911  1.00 12.75 ? 67   LEU B CA  1 
ATOM   5291  C  C   . LEU B 1 75  ? 42.323  6.597   32.823  1.00 12.74 ? 67   LEU B C   1 
ATOM   5292  O  O   . LEU B 1 75  ? 43.158  7.467   33.098  1.00 14.91 ? 67   LEU B O   1 
ATOM   5293  C  CB  . LEU B 1 75  ? 42.002  5.586   30.543  1.00 11.93 ? 67   LEU B CB  1 
ATOM   5294  C  CG  . LEU B 1 75  ? 42.332  6.915   29.861  1.00 15.68 ? 67   LEU B CG  1 
ATOM   5295  C  CD1 . LEU B 1 75  ? 43.808  6.919   29.406  1.00 14.58 ? 67   LEU B CD1 1 
ATOM   5296  C  CD2 . LEU B 1 75  ? 41.410  7.238   28.682  1.00 17.41 ? 67   LEU B CD2 1 
ATOM   5297  N  N   . LEU B 1 76  ? 41.091  6.609   33.336  1.00 13.96 ? 68   LEU B N   1 
ATOM   5298  C  CA  . LEU B 1 76  ? 40.687  7.692   34.229  1.00 14.49 ? 68   LEU B CA  1 
ATOM   5299  C  C   . LEU B 1 76  ? 41.462  7.640   35.547  1.00 14.17 ? 68   LEU B C   1 
ATOM   5300  O  O   . LEU B 1 76  ? 41.953  8.670   36.027  1.00 15.31 ? 68   LEU B O   1 
ATOM   5301  C  CB  . LEU B 1 76  ? 39.173  7.636   34.468  1.00 10.64 ? 68   LEU B CB  1 
ATOM   5302  C  CG  . LEU B 1 76  ? 38.585  8.743   35.357  1.00 10.58 ? 68   LEU B CG  1 
ATOM   5303  C  CD1 . LEU B 1 76  ? 38.996  10.126  34.846  1.00 15.31 ? 68   LEU B CD1 1 
ATOM   5304  C  CD2 . LEU B 1 76  ? 37.066  8.627   35.478  1.00 10.26 ? 68   LEU B CD2 1 
ATOM   5305  N  N   . TYR B 1 77  ? 41.602  6.453   36.142  1.00 12.19 ? 69   TYR B N   1 
ATOM   5306  C  CA  . TYR B 1 77  ? 42.332  6.368   37.406  1.00 12.59 ? 69   TYR B CA  1 
ATOM   5307  C  C   . TYR B 1 77  ? 43.781  6.818   37.242  1.00 11.62 ? 69   TYR B C   1 
ATOM   5308  O  O   . TYR B 1 77  ? 44.338  7.465   38.139  1.00 14.42 ? 69   TYR B O   1 
ATOM   5309  C  CB  . TYR B 1 77  ? 42.272  4.946   37.962  1.00 11.90 ? 69   TYR B CB  1 
ATOM   5310  C  CG  . TYR B 1 77  ? 40.875  4.475   38.305  1.00 11.27 ? 69   TYR B CG  1 
ATOM   5311  C  CD1 . TYR B 1 77  ? 39.891  5.373   38.709  1.00 13.51 ? 69   TYR B CD1 1 
ATOM   5312  C  CD2 . TYR B 1 77  ? 40.542  3.127   38.229  1.00 13.34 ? 69   TYR B CD2 1 
ATOM   5313  C  CE1 . TYR B 1 77  ? 38.600  4.928   39.034  1.00 11.97 ? 69   TYR B CE1 1 
ATOM   5314  C  CE2 . TYR B 1 77  ? 39.261  2.677   38.550  1.00 11.28 ? 69   TYR B CE2 1 
ATOM   5315  C  CZ  . TYR B 1 77  ? 38.297  3.583   38.940  1.00 11.50 ? 69   TYR B CZ  1 
ATOM   5316  O  OH  . TYR B 1 77  ? 37.040  3.126   39.268  1.00 10.64 ? 69   TYR B OH  1 
ATOM   5317  N  N   . SER B 1 78  ? 44.401  6.500   36.100  1.00 12.69 ? 70   SER B N   1 
ATOM   5318  C  CA  . SER B 1 78  ? 45.748  7.003   35.820  1.00 17.01 ? 70   SER B CA  1 
ATOM   5319  C  C   . SER B 1 78  ? 45.769  8.527   35.814  1.00 18.33 ? 70   SER B C   1 
ATOM   5320  O  O   . SER B 1 78  ? 46.606  9.150   36.472  1.00 15.14 ? 70   SER B O   1 
ATOM   5321  C  CB  . SER B 1 78  ? 46.265  6.471   34.477  1.00 14.89 ? 70   SER B CB  1 
ATOM   5322  O  OG  . SER B 1 78  ? 46.486  5.071   34.500  1.00 16.33 ? 70   SER B OG  1 
ATOM   5323  N  N   . LEU B 1 79  ? 44.847  9.144   35.067  1.00 18.17 ? 71   LEU B N   1 
ATOM   5324  C  CA  . LEU B 1 79  ? 44.804  10.601  34.972  1.00 13.80 ? 71   LEU B CA  1 
ATOM   5325  C  C   . LEU B 1 79  ? 44.605  11.249  36.338  1.00 12.82 ? 71   LEU B C   1 
ATOM   5326  O  O   . LEU B 1 79  ? 45.251  12.253  36.656  1.00 15.96 ? 71   LEU B O   1 
ATOM   5327  C  CB  . LEU B 1 79  ? 43.688  11.018  34.011  1.00 12.68 ? 71   LEU B CB  1 
ATOM   5328  C  CG  . LEU B 1 79  ? 43.969  10.608  32.560  1.00 16.32 ? 71   LEU B CG  1 
ATOM   5329  C  CD1 . LEU B 1 79  ? 42.713  10.754  31.700  1.00 12.68 ? 71   LEU B CD1 1 
ATOM   5330  C  CD2 . LEU B 1 79  ? 45.118  11.430  31.979  1.00 18.48 ? 71   LEU B CD2 1 
ATOM   5331  N  N   . LEU B 1 80  ? 43.694  10.702  37.149  1.00 12.29 ? 72   LEU B N   1 
ATOM   5332  C  CA  . LEU B 1 80  ? 43.427  11.288  38.459  1.00 12.38 ? 72   LEU B CA  1 
ATOM   5333  C  C   . LEU B 1 80  ? 44.647  11.178  39.362  1.00 12.70 ? 72   LEU B C   1 
ATOM   5334  O  O   . LEU B 1 80  ? 45.026  12.146  40.033  1.00 16.43 ? 72   LEU B O   1 
ATOM   5335  C  CB  . LEU B 1 80  ? 42.207  10.609  39.090  1.00 11.83 ? 72   LEU B CB  1 
ATOM   5336  C  CG  . LEU B 1 80  ? 40.913  10.873  38.301  1.00 14.82 ? 72   LEU B CG  1 
ATOM   5337  C  CD1 . LEU B 1 80  ? 39.753  9.975   38.791  1.00 16.53 ? 72   LEU B CD1 1 
ATOM   5338  C  CD2 . LEU B 1 80  ? 40.535  12.358  38.384  1.00 13.24 ? 72   LEU B CD2 1 
ATOM   5339  N  N   . HIS B 1 81  ? 45.291  10.015  39.371  1.00 12.69 ? 73   HIS B N   1 
ATOM   5340  C  CA  . HIS B 1 81  ? 46.501  9.861   40.175  1.00 13.37 ? 73   HIS B CA  1 
ATOM   5341  C  C   . HIS B 1 81  ? 47.604  10.802  39.704  1.00 15.79 ? 73   HIS B C   1 
ATOM   5342  O  O   . HIS B 1 81  ? 48.252  11.476  40.517  1.00 17.61 ? 73   HIS B O   1 
ATOM   5343  C  CB  . HIS B 1 81  ? 47.000  8.418   40.127  1.00 13.10 ? 73   HIS B CB  1 
ATOM   5344  C  CG  . HIS B 1 81  ? 48.316  8.236   40.816  1.00 13.68 ? 73   HIS B CG  1 
ATOM   5345  N  ND1 . HIS B 1 81  ? 48.476  8.446   42.170  1.00 17.72 ? 73   HIS B ND1 1 
ATOM   5346  C  CD2 . HIS B 1 81  ? 49.542  7.919   40.335  1.00 19.69 ? 73   HIS B CD2 1 
ATOM   5347  C  CE1 . HIS B 1 81  ? 49.744  8.246   42.496  1.00 19.26 ? 73   HIS B CE1 1 
ATOM   5348  N  NE2 . HIS B 1 81  ? 50.412  7.929   41.401  1.00 18.47 ? 73   HIS B NE2 1 
ATOM   5349  N  N   . LEU B 1 82  ? 47.847  10.844  38.392  1.00 15.84 ? 74   LEU B N   1 
ATOM   5350  C  CA  . LEU B 1 82  ? 48.996  11.587  37.868  1.00 16.55 ? 74   LEU B CA  1 
ATOM   5351  C  C   . LEU B 1 82  ? 48.846  13.097  38.071  1.00 18.67 ? 74   LEU B C   1 
ATOM   5352  O  O   . LEU B 1 82  ? 49.843  13.798  38.303  1.00 21.30 ? 74   LEU B O   1 
ATOM   5353  C  CB  . LEU B 1 82  ? 49.182  11.262  36.385  1.00 16.16 ? 74   LEU B CB  1 
ATOM   5354  C  CG  . LEU B 1 82  ? 49.712  9.863   36.074  1.00 16.87 ? 74   LEU B CG  1 
ATOM   5355  C  CD1 . LEU B 1 82  ? 49.326  9.460   34.661  1.00 14.83 ? 74   LEU B CD1 1 
ATOM   5356  C  CD2 . LEU B 1 82  ? 51.237  9.824   36.255  1.00 18.90 ? 74   LEU B CD2 1 
ATOM   5357  N  N   . THR B 1 83  ? 47.625  13.626  37.972  1.00 16.69 ? 75   THR B N   1 
ATOM   5358  C  CA  . THR B 1 83  ? 47.452  15.070  38.062  1.00 19.68 ? 75   THR B CA  1 
ATOM   5359  C  C   . THR B 1 83  ? 47.319  15.562  39.494  1.00 20.55 ? 75   THR B C   1 
ATOM   5360  O  O   . THR B 1 83  ? 47.314  16.779  39.716  1.00 20.27 ? 75   THR B O   1 
ATOM   5361  C  CB  . THR B 1 83  ? 46.250  15.536  37.233  1.00 19.06 ? 75   THR B CB  1 
ATOM   5362  O  OG1 . THR B 1 83  ? 45.076  14.820  37.632  1.00 16.62 ? 75   THR B OG1 1 
ATOM   5363  C  CG2 . THR B 1 83  ? 46.526  15.303  35.745  1.00 14.83 ? 75   THR B CG2 1 
ATOM   5364  N  N   . GLY B 1 84  ? 47.260  14.661  40.460  1.00 14.82 ? 76   GLY B N   1 
ATOM   5365  C  CA  . GLY B 1 84  ? 47.366  15.018  41.851  1.00 22.31 ? 76   GLY B CA  1 
ATOM   5366  C  C   . GLY B 1 84  ? 46.096  14.951  42.658  1.00 21.64 ? 76   GLY B C   1 
ATOM   5367  O  O   . GLY B 1 84  ? 46.034  15.579  43.719  1.00 19.58 ? 76   GLY B O   1 
ATOM   5368  N  N   . TYR B 1 85  ? 45.074  14.239  42.183  1.00 18.63 ? 77   TYR B N   1 
ATOM   5369  C  CA  . TYR B 1 85  ? 43.895  13.992  42.987  1.00 16.23 ? 77   TYR B CA  1 
ATOM   5370  C  C   . TYR B 1 85  ? 44.236  13.037  44.125  1.00 15.53 ? 77   TYR B C   1 
ATOM   5371  O  O   . TYR B 1 85  ? 45.296  12.402  44.146  1.00 14.05 ? 77   TYR B O   1 
ATOM   5372  C  CB  . TYR B 1 85  ? 42.765  13.412  42.129  1.00 15.91 ? 77   TYR B CB  1 
ATOM   5373  C  CG  . TYR B 1 85  ? 42.137  14.429  41.189  1.00 12.78 ? 77   TYR B CG  1 
ATOM   5374  C  CD1 . TYR B 1 85  ? 42.778  14.803  40.018  1.00 13.04 ? 77   TYR B CD1 1 
ATOM   5375  C  CD2 . TYR B 1 85  ? 40.910  15.021  41.490  1.00 17.36 ? 77   TYR B CD2 1 
ATOM   5376  C  CE1 . TYR B 1 85  ? 42.219  15.748  39.164  1.00 17.09 ? 77   TYR B CE1 1 
ATOM   5377  C  CE2 . TYR B 1 85  ? 40.332  15.964  40.639  1.00 17.28 ? 77   TYR B CE2 1 
ATOM   5378  C  CZ  . TYR B 1 85  ? 40.991  16.317  39.477  1.00 19.94 ? 77   TYR B CZ  1 
ATOM   5379  O  OH  . TYR B 1 85  ? 40.436  17.253  38.628  1.00 19.48 ? 77   TYR B OH  1 
ATOM   5380  N  N   . ASN B 1 86  ? 43.306  12.928  45.073  1.00 14.17 ? 78   ASN B N   1 
ATOM   5381  C  CA  . ASN B 1 86  ? 43.445  12.016  46.210  1.00 18.64 ? 78   ASN B CA  1 
ATOM   5382  C  C   . ASN B 1 86  ? 43.101  10.588  45.777  1.00 23.39 ? 78   ASN B C   1 
ATOM   5383  O  O   . ASN B 1 86  ? 42.128  9.971   46.214  1.00 24.65 ? 78   ASN B O   1 
ATOM   5384  C  CB  . ASN B 1 86  ? 42.569  12.475  47.367  1.00 25.48 ? 78   ASN B CB  1 
ATOM   5385  C  CG  . ASN B 1 86  ? 42.807  11.680  48.627  1.00 37.06 ? 78   ASN B CG  1 
ATOM   5386  O  OD1 . ASN B 1 86  ? 43.878  11.107  48.821  1.00 42.37 ? 78   ASN B OD1 1 
ATOM   5387  N  ND2 . ASN B 1 86  ? 41.803  11.638  49.497  1.00 43.42 ? 78   ASN B ND2 1 
ATOM   5388  N  N   . LEU B 1 87  ? 43.907  10.092  44.849  1.00 17.54 ? 79   LEU B N   1 
ATOM   5389  C  CA  . LEU B 1 87  ? 43.868  8.706   44.402  1.00 16.71 ? 79   LEU B CA  1 
ATOM   5390  C  C   . LEU B 1 87  ? 45.317  8.257   44.352  1.00 19.07 ? 79   LEU B C   1 
ATOM   5391  O  O   . LEU B 1 87  ? 46.108  8.812   43.586  1.00 16.27 ? 79   LEU B O   1 
ATOM   5392  C  CB  . LEU B 1 87  ? 43.187  8.585   43.034  1.00 12.56 ? 79   LEU B CB  1 
ATOM   5393  C  CG  . LEU B 1 87  ? 42.752  7.194   42.589  1.00 12.87 ? 79   LEU B CG  1 
ATOM   5394  C  CD1 . LEU B 1 87  ? 41.638  6.700   43.510  1.00 13.76 ? 79   LEU B CD1 1 
ATOM   5395  C  CD2 . LEU B 1 87  ? 42.288  7.209   41.137  1.00 16.87 ? 79   LEU B CD2 1 
ATOM   5396  N  N   . SER B 1 88  ? 45.674  7.291   45.191  1.00 17.03 ? 80   SER B N   1 
ATOM   5397  C  CA  . SER B 1 88  ? 47.067  6.985   45.469  1.00 16.09 ? 80   SER B CA  1 
ATOM   5398  C  C   . SER B 1 88  ? 47.531  5.774   44.670  1.00 14.35 ? 80   SER B C   1 
ATOM   5399  O  O   . SER B 1 88  ? 46.734  5.041   44.081  1.00 13.16 ? 80   SER B O   1 
ATOM   5400  C  CB  . SER B 1 88  ? 47.253  6.721   46.961  1.00 16.82 ? 80   SER B CB  1 
ATOM   5401  O  OG  . SER B 1 88  ? 46.578  5.524   47.312  1.00 16.39 ? 80   SER B OG  1 
ATOM   5402  N  N   . ILE B 1 89  ? 48.847  5.544   44.699  1.00 15.92 ? 81   ILE B N   1 
ATOM   5403  C  CA  . ILE B 1 89  ? 49.392  4.306   44.147  1.00 15.48 ? 81   ILE B CA  1 
ATOM   5404  C  C   . ILE B 1 89  ? 48.767  3.093   44.826  1.00 19.89 ? 81   ILE B C   1 
ATOM   5405  O  O   . ILE B 1 89  ? 48.398  2.117   44.162  1.00 14.58 ? 81   ILE B O   1 
ATOM   5406  C  CB  . ILE B 1 89  ? 50.931  4.295   44.260  1.00 19.92 ? 81   ILE B CB  1 
ATOM   5407  C  CG1 . ILE B 1 89  ? 51.543  5.128   43.131  1.00 18.09 ? 81   ILE B CG1 1 
ATOM   5408  C  CG2 . ILE B 1 89  ? 51.463  2.874   44.207  1.00 25.44 ? 81   ILE B CG2 1 
ATOM   5409  C  CD1 . ILE B 1 89  ? 51.261  4.568   41.762  1.00 18.41 ? 81   ILE B CD1 1 
ATOM   5410  N  N   . GLU B 1 90  ? 48.607  3.139   46.150  1.00 18.58 ? 82   GLU B N   1 
ATOM   5411  C  CA  . GLU B 1 90  ? 47.947  2.027   46.832  1.00 18.16 ? 82   GLU B CA  1 
ATOM   5412  C  C   . GLU B 1 90  ? 46.502  1.861   46.370  1.00 12.68 ? 82   GLU B C   1 
ATOM   5413  O  O   . GLU B 1 90  ? 46.009  0.730   46.279  1.00 15.65 ? 82   GLU B O   1 
ATOM   5414  C  CB  . GLU B 1 90  ? 48.009  2.216   48.347  1.00 24.86 ? 82   GLU B CB  1 
ATOM   5415  C  CG  . GLU B 1 90  ? 49.425  2.098   48.904  1.00 39.69 ? 82   GLU B CG  1 
ATOM   5416  C  CD  . GLU B 1 90  ? 50.116  0.795   48.509  1.00 42.82 ? 82   GLU B CD  1 
ATOM   5417  O  OE1 . GLU B 1 90  ? 49.531  -0.284  48.746  1.00 38.86 ? 82   GLU B OE1 1 
ATOM   5418  O  OE2 . GLU B 1 90  ? 51.241  0.854   47.954  1.00 47.09 ? 82   GLU B OE2 1 
ATOM   5419  N  N   . ASP B 1 91  ? 45.815  2.959   46.049  1.00 12.44 ? 83   ASP B N   1 
ATOM   5420  C  CA  . ASP B 1 91  ? 44.485  2.816   45.460  1.00 14.23 ? 83   ASP B CA  1 
ATOM   5421  C  C   . ASP B 1 91  ? 44.564  2.066   44.131  1.00 14.85 ? 83   ASP B C   1 
ATOM   5422  O  O   . ASP B 1 91  ? 43.767  1.155   43.871  1.00 15.87 ? 83   ASP B O   1 
ATOM   5423  C  CB  . ASP B 1 91  ? 43.821  4.187   45.273  1.00 14.49 ? 83   ASP B CB  1 
ATOM   5424  C  CG  . ASP B 1 91  ? 43.478  4.876   46.603  1.00 16.01 ? 83   ASP B CG  1 
ATOM   5425  O  OD1 . ASP B 1 91  ? 43.143  4.186   47.590  1.00 18.54 ? 83   ASP B OD1 1 
ATOM   5426  O  OD2 . ASP B 1 91  ? 43.536  6.122   46.659  1.00 15.15 ? 83   ASP B OD2 1 
ATOM   5427  N  N   . LEU B 1 92  ? 45.533  2.418   43.280  1.00 13.99 ? 84   LEU B N   1 
ATOM   5428  C  CA  . LEU B 1 92  ? 45.668  1.729   41.997  1.00 13.58 ? 84   LEU B CA  1 
ATOM   5429  C  C   . LEU B 1 92  ? 46.053  0.262   42.181  1.00 15.60 ? 84   LEU B C   1 
ATOM   5430  O  O   . LEU B 1 92  ? 45.635  -0.591  41.385  1.00 12.13 ? 84   LEU B O   1 
ATOM   5431  C  CB  . LEU B 1 92  ? 46.702  2.438   41.117  1.00 14.33 ? 84   LEU B CB  1 
ATOM   5432  C  CG  . LEU B 1 92  ? 46.457  3.923   40.858  1.00 18.37 ? 84   LEU B CG  1 
ATOM   5433  C  CD1 . LEU B 1 92  ? 47.496  4.500   39.861  1.00 20.23 ? 84   LEU B CD1 1 
ATOM   5434  C  CD2 . LEU B 1 92  ? 45.036  4.146   40.377  1.00 15.29 ? 84   LEU B CD2 1 
ATOM   5435  N  N   . LYS B 1 93  ? 46.847  -0.051  43.215  1.00 14.04 ? 85   LYS B N   1 
ATOM   5436  C  CA  . LYS B 1 93  ? 47.192  -1.439  43.508  1.00 15.26 ? 85   LYS B CA  1 
ATOM   5437  C  C   . LYS B 1 93  ? 46.003  -2.231  44.027  1.00 13.34 ? 85   LYS B C   1 
ATOM   5438  O  O   . LYS B 1 93  ? 46.101  -3.456  44.183  1.00 13.14 ? 85   LYS B O   1 
ATOM   5439  C  CB  . LYS B 1 93  ? 48.335  -1.508  44.530  1.00 17.18 ? 85   LYS B CB  1 
ATOM   5440  C  CG  . LYS B 1 93  ? 49.699  -1.059  44.011  1.00 18.29 ? 85   LYS B CG  1 
ATOM   5441  C  CD  . LYS B 1 93  ? 50.752  -1.201  45.126  1.00 19.92 ? 85   LYS B CD  1 
ATOM   5442  C  CE  . LYS B 1 93  ? 52.133  -0.766  44.675  1.00 24.96 ? 85   LYS B CE  1 
ATOM   5443  N  NZ  . LYS B 1 93  ? 53.088  -0.853  45.828  1.00 31.64 ? 85   LYS B NZ  1 
ATOM   5444  N  N   . ASN B 1 94  ? 44.883  -1.570  44.300  1.00 11.71 ? 86   ASN B N   1 
ATOM   5445  C  CA  . ASN B 1 94  ? 43.691  -2.268  44.750  1.00 11.42 ? 86   ASN B CA  1 
ATOM   5446  C  C   . ASN B 1 94  ? 42.563  -2.143  43.739  1.00 12.03 ? 86   ASN B C   1 
ATOM   5447  O  O   . ASN B 1 94  ? 41.389  -2.244  44.090  1.00 11.35 ? 86   ASN B O   1 
ATOM   5448  C  CB  . ASN B 1 94  ? 43.281  -1.766  46.129  1.00 14.38 ? 86   ASN B CB  1 
ATOM   5449  C  CG  . ASN B 1 94  ? 44.193  -2.315  47.213  1.00 20.26 ? 86   ASN B CG  1 
ATOM   5450  O  OD1 . ASN B 1 94  ? 44.080  -3.474  47.579  1.00 24.20 ? 86   ASN B OD1 1 
ATOM   5451  N  ND2 . ASN B 1 94  ? 45.120  -1.506  47.685  1.00 23.89 ? 86   ASN B ND2 1 
ATOM   5452  N  N   . PHE B 1 95  ? 42.927  -1.916  42.481  1.00 13.19 ? 87   PHE B N   1 
ATOM   5453  C  CA  . PHE B 1 95  ? 41.974  -1.950  41.379  1.00 10.63 ? 87   PHE B CA  1 
ATOM   5454  C  C   . PHE B 1 95  ? 41.117  -3.207  41.449  1.00 10.50 ? 87   PHE B C   1 
ATOM   5455  O  O   . PHE B 1 95  ? 41.638  -4.318  41.608  1.00 11.69 ? 87   PHE B O   1 
ATOM   5456  C  CB  . PHE B 1 95  ? 42.755  -1.907  40.068  1.00 10.80 ? 87   PHE B CB  1 
ATOM   5457  C  CG  . PHE B 1 95  ? 41.906  -1.883  38.829  1.00 12.60 ? 87   PHE B CG  1 
ATOM   5458  C  CD1 . PHE B 1 95  ? 40.945  -0.904  38.636  1.00 10.30 ? 87   PHE B CD1 1 
ATOM   5459  C  CD2 . PHE B 1 95  ? 42.133  -2.806  37.818  1.00 12.92 ? 87   PHE B CD2 1 
ATOM   5460  C  CE1 . PHE B 1 95  ? 40.207  -0.875  37.464  1.00 12.23 ? 87   PHE B CE1 1 
ATOM   5461  C  CE2 . PHE B 1 95  ? 41.394  -2.777  36.648  1.00 12.69 ? 87   PHE B CE2 1 
ATOM   5462  C  CZ  . PHE B 1 95  ? 40.444  -1.806  36.473  1.00 10.35 ? 87   PHE B CZ  1 
ATOM   5463  N  N   . ARG B 1 96  ? 39.794  -3.018  41.363  1.00 10.21 ? 88   ARG B N   1 
ATOM   5464  C  CA  . ARG B 1 96  ? 38.817  -4.106  41.315  1.00 10.55 ? 88   ARG B CA  1 
ATOM   5465  C  C   . ARG B 1 96  ? 38.787  -4.936  42.598  1.00 13.20 ? 88   ARG B C   1 
ATOM   5466  O  O   . ARG B 1 96  ? 38.289  -6.065  42.586  1.00 11.07 ? 88   ARG B O   1 
ATOM   5467  C  CB  . ARG B 1 96  ? 39.059  -5.026  40.104  1.00 11.19 ? 88   ARG B CB  1 
ATOM   5468  C  CG  . ARG B 1 96  ? 38.581  -4.401  38.786  1.00 11.76 ? 88   ARG B CG  1 
ATOM   5469  C  CD  . ARG B 1 96  ? 38.995  -5.138  37.476  1.00 10.53 ? 88   ARG B CD  1 
ATOM   5470  N  NE  . ARG B 1 96  ? 38.255  -4.489  36.395  1.00 11.14 ? 88   ARG B NE  1 
ATOM   5471  C  CZ  . ARG B 1 96  ? 37.162  -4.993  35.812  1.00 15.44 ? 88   ARG B CZ  1 
ATOM   5472  N  NH1 . ARG B 1 96  ? 36.731  -6.205  36.128  1.00 10.73 ? 88   ARG B NH1 1 
ATOM   5473  N  NH2 . ARG B 1 96  ? 36.500  -4.279  34.902  1.00 16.18 ? 88   ARG B NH2 1 
ATOM   5474  N  N   . GLN B 1 97  ? 39.281  -4.396  43.716  1.00 10.44 ? 89   GLN B N   1 
ATOM   5475  C  CA  . GLN B 1 97  ? 39.256  -5.096  44.994  1.00 12.39 ? 89   GLN B CA  1 
ATOM   5476  C  C   . GLN B 1 97  ? 38.177  -4.513  45.897  1.00 13.72 ? 89   GLN B C   1 
ATOM   5477  O  O   . GLN B 1 97  ? 37.864  -3.320  45.833  1.00 13.00 ? 89   GLN B O   1 
ATOM   5478  C  CB  . GLN B 1 97  ? 40.616  -5.018  45.701  1.00 15.32 ? 89   GLN B CB  1 
ATOM   5479  C  CG  . GLN B 1 97  ? 41.758  -5.589  44.875  1.00 13.51 ? 89   GLN B CG  1 
ATOM   5480  C  CD  . GLN B 1 97  ? 41.417  -6.953  44.296  1.00 16.57 ? 89   GLN B CD  1 
ATOM   5481  O  OE1 . GLN B 1 97  ? 41.233  -7.924  45.036  1.00 15.83 ? 89   GLN B OE1 1 
ATOM   5482  N  NE2 . GLN B 1 97  ? 41.334  -7.038  42.963  1.00 11.84 ? 89   GLN B NE2 1 
ATOM   5483  N  N   . LEU B 1 98  ? 37.628  -5.373  46.759  1.00 12.36 ? 90   LEU B N   1 
ATOM   5484  C  CA  . LEU B 1 98  ? 36.506  -4.988  47.608  1.00 16.04 ? 90   LEU B CA  1 
ATOM   5485  C  C   . LEU B 1 98  ? 36.841  -3.738  48.408  1.00 13.92 ? 90   LEU B C   1 
ATOM   5486  O  O   . LEU B 1 98  ? 37.904  -3.652  49.026  1.00 11.27 ? 90   LEU B O   1 
ATOM   5487  C  CB  . LEU B 1 98  ? 36.144  -6.137  48.554  1.00 11.29 ? 90   LEU B CB  1 
ATOM   5488  C  CG  . LEU B 1 98  ? 34.895  -5.887  49.396  1.00 12.25 ? 90   LEU B CG  1 
ATOM   5489  C  CD1 . LEU B 1 98  ? 33.661  -5.722  48.480  1.00 13.36 ? 90   LEU B CD1 1 
ATOM   5490  C  CD2 . LEU B 1 98  ? 34.677  -6.971  50.440  1.00 15.95 ? 90   LEU B CD2 1 
ATOM   5491  N  N   . HIS B 1 99  ? 35.934  -2.760  48.367  1.00 11.98 ? 91   HIS B N   1 
ATOM   5492  C  CA  . HIS B 1 99  ? 35.985  -1.490  49.097  1.00 16.71 ? 91   HIS B CA  1 
ATOM   5493  C  C   . HIS B 1 99  ? 36.994  -0.484  48.539  1.00 12.16 ? 91   HIS B C   1 
ATOM   5494  O  O   . HIS B 1 99  ? 37.150  0.571   49.130  1.00 13.46 ? 91   HIS B O   1 
ATOM   5495  C  CB  . HIS B 1 99  ? 36.308  -1.664  50.592  1.00 17.49 ? 91   HIS B CB  1 
ATOM   5496  C  CG  . HIS B 1 99  ? 35.436  -2.652  51.302  1.00 20.02 ? 91   HIS B CG  1 
ATOM   5497  N  ND1 . HIS B 1 99  ? 34.065  -2.542  51.340  1.00 24.67 ? 91   HIS B ND1 1 
ATOM   5498  C  CD2 . HIS B 1 99  ? 35.747  -3.755  52.022  1.00 20.05 ? 91   HIS B CD2 1 
ATOM   5499  C  CE1 . HIS B 1 99  ? 33.565  -3.540  52.046  1.00 21.66 ? 91   HIS B CE1 1 
ATOM   5500  N  NE2 . HIS B 1 99  ? 34.566  -4.286  52.479  1.00 23.07 ? 91   HIS B NE2 1 
ATOM   5501  N  N   . SER B 1 100 ? 37.682  -0.770  47.434  1.00 12.06 ? 92   SER B N   1 
ATOM   5502  C  CA  . SER B 1 100 ? 38.702  0.168   46.971  1.00 11.73 ? 92   SER B CA  1 
ATOM   5503  C  C   . SER B 1 100 ? 38.059  1.409   46.347  1.00 13.49 ? 92   SER B C   1 
ATOM   5504  O  O   . SER B 1 100 ? 36.865  1.447   46.031  1.00 12.41 ? 92   SER B O   1 
ATOM   5505  C  CB  . SER B 1 100 ? 39.634  -0.498  45.956  1.00 10.64 ? 92   SER B CB  1 
ATOM   5506  O  OG  . SER B 1 100 ? 39.033  -0.600  44.669  1.00 11.98 ? 92   SER B OG  1 
ATOM   5507  N  N   . LYS B 1 101 ? 38.873  2.445   46.175  1.00 13.15 ? 93   LYS B N   1 
ATOM   5508  C  CA  . LYS B 1 101 ? 38.450  3.624   45.429  1.00 13.55 ? 93   LYS B CA  1 
ATOM   5509  C  C   . LYS B 1 101 ? 38.633  3.460   43.930  1.00 10.23 ? 93   LYS B C   1 
ATOM   5510  O  O   . LYS B 1 101 ? 38.422  4.420   43.175  1.00 12.83 ? 93   LYS B O   1 
ATOM   5511  C  CB  . LYS B 1 101 ? 39.214  4.854   45.922  1.00 18.03 ? 93   LYS B CB  1 
ATOM   5512  C  CG  . LYS B 1 101 ? 38.707  5.359   47.273  1.00 21.84 ? 93   LYS B CG  1 
ATOM   5513  C  CD  . LYS B 1 101 ? 39.491  6.567   47.724  1.00 31.37 ? 93   LYS B CD  1 
ATOM   5514  C  CE  . LYS B 1 101 ? 38.932  7.120   49.015  1.00 43.38 ? 93   LYS B CE  1 
ATOM   5515  N  NZ  . LYS B 1 101 ? 39.666  8.349   49.431  1.00 47.75 ? 93   LYS B NZ  1 
ATOM   5516  N  N   . THR B 1 102 ? 38.998  2.262   43.484  1.00 10.17 ? 94   THR B N   1 
ATOM   5517  C  CA  . THR B 1 102 ? 39.228  1.972   42.070  1.00 10.05 ? 94   THR B CA  1 
ATOM   5518  C  C   . THR B 1 102 ? 38.394  0.773   41.625  1.00 12.36 ? 94   THR B C   1 
ATOM   5519  O  O   . THR B 1 102 ? 38.941  -0.264  41.238  1.00 12.00 ? 94   THR B O   1 
ATOM   5520  C  CB  . THR B 1 102 ? 40.713  1.702   41.845  1.00 10.33 ? 94   THR B CB  1 
ATOM   5521  O  OG1 . THR B 1 102 ? 41.159  0.796   42.862  1.00 10.50 ? 94   THR B OG1 1 
ATOM   5522  C  CG2 . THR B 1 102 ? 41.525  3.013   41.949  1.00 13.22 ? 94   THR B CG2 1 
ATOM   5523  N  N   . PRO B 1 103 ? 37.060  0.876   41.661  1.00 16.14 ? 95   PRO B N   1 
ATOM   5524  C  CA  . PRO B 1 103 ? 36.233  -0.229  41.161  1.00 10.65 ? 95   PRO B CA  1 
ATOM   5525  C  C   . PRO B 1 103 ? 36.399  -0.393  39.659  1.00 10.33 ? 95   PRO B C   1 
ATOM   5526  O  O   . PRO B 1 103 ? 36.903  0.488   38.960  1.00 12.23 ? 95   PRO B O   1 
ATOM   5527  C  CB  . PRO B 1 103 ? 34.800  0.197   41.517  1.00 9.79  ? 95   PRO B CB  1 
ATOM   5528  C  CG  . PRO B 1 103 ? 34.875  1.709   41.570  1.00 9.47  ? 95   PRO B CG  1 
ATOM   5529  C  CD  . PRO B 1 103 ? 36.229  1.964   42.207  1.00 14.00 ? 95   PRO B CD  1 
ATOM   5530  N  N   . GLY B 1 104 ? 35.959  -1.557  39.172  1.00 15.07 ? 96   GLY B N   1 
ATOM   5531  C  CA  . GLY B 1 104 ? 36.243  -1.957  37.803  1.00 12.49 ? 96   GLY B CA  1 
ATOM   5532  C  C   . GLY B 1 104 ? 35.664  -1.028  36.758  1.00 13.38 ? 96   GLY B C   1 
ATOM   5533  O  O   . GLY B 1 104 ? 36.210  -0.908  35.663  1.00 10.49 ? 96   GLY B O   1 
ATOM   5534  N  N   . HIS B 1 105 ? 34.546  -0.380  37.068  1.00 11.17 ? 97   HIS B N   1 
ATOM   5535  C  CA  . HIS B 1 105 ? 34.046  0.744   36.297  1.00 10.69 ? 97   HIS B CA  1 
ATOM   5536  C  C   . HIS B 1 105 ? 33.965  1.958   37.217  1.00 10.66 ? 97   HIS B C   1 
ATOM   5537  O  O   . HIS B 1 105 ? 33.657  1.796   38.402  1.00 12.14 ? 97   HIS B O   1 
ATOM   5538  C  CB  . HIS B 1 105 ? 32.673  0.416   35.693  1.00 12.55 ? 97   HIS B CB  1 
ATOM   5539  C  CG  . HIS B 1 105 ? 32.730  -0.677  34.676  1.00 14.97 ? 97   HIS B CG  1 
ATOM   5540  N  ND1 . HIS B 1 105 ? 32.525  -2.003  34.991  1.00 21.81 ? 97   HIS B ND1 1 
ATOM   5541  C  CD2 . HIS B 1 105 ? 33.025  -0.647  33.354  1.00 18.71 ? 97   HIS B CD2 1 
ATOM   5542  C  CE1 . HIS B 1 105 ? 32.674  -2.740  33.904  1.00 16.29 ? 97   HIS B CE1 1 
ATOM   5543  N  NE2 . HIS B 1 105 ? 32.970  -1.942  32.897  1.00 18.22 ? 97   HIS B NE2 1 
ATOM   5544  N  N   . PRO B 1 106 ? 34.301  3.157   36.735  1.00 11.87 ? 98   PRO B N   1 
ATOM   5545  C  CA  . PRO B 1 106 ? 34.435  4.306   37.646  1.00 12.59 ? 98   PRO B CA  1 
ATOM   5546  C  C   . PRO B 1 106 ? 33.091  4.651   38.254  1.00 13.19 ? 98   PRO B C   1 
ATOM   5547  O  O   . PRO B 1 106 ? 32.075  4.639   37.563  1.00 12.62 ? 98   PRO B O   1 
ATOM   5548  C  CB  . PRO B 1 106 ? 34.927  5.442   36.737  1.00 13.69 ? 98   PRO B CB  1 
ATOM   5549  C  CG  . PRO B 1 106 ? 35.428  4.759   35.486  1.00 16.95 ? 98   PRO B CG  1 
ATOM   5550  C  CD  . PRO B 1 106 ? 34.541  3.545   35.335  1.00 15.91 ? 98   PRO B CD  1 
ATOM   5551  N  N   . GLU B 1 107 ? 33.088  4.953   39.557  1.00 10.12 ? 99   GLU B N   1 
ATOM   5552  C  CA  . GLU B 1 107 ? 31.852  5.246   40.280  1.00 9.95  ? 99   GLU B CA  1 
ATOM   5553  C  C   . GLU B 1 107 ? 31.906  6.648   40.865  1.00 10.50 ? 99   GLU B C   1 
ATOM   5554  O  O   . GLU B 1 107 ? 32.825  6.982   41.626  1.00 14.10 ? 99   GLU B O   1 
ATOM   5555  C  CB  . GLU B 1 107 ? 31.596  4.227   41.397  1.00 11.64 ? 99   GLU B CB  1 
ATOM   5556  C  CG  . GLU B 1 107 ? 31.282  2.835   40.907  1.00 13.47 ? 99   GLU B CG  1 
ATOM   5557  C  CD  . GLU B 1 107 ? 31.209  1.831   42.046  1.00 16.49 ? 99   GLU B CD  1 
ATOM   5558  O  OE1 . GLU B 1 107 ? 30.889  2.238   43.190  1.00 17.91 ? 99   GLU B OE1 1 
ATOM   5559  O  OE2 . GLU B 1 107 ? 31.483  0.642   41.796  1.00 14.42 ? 99   GLU B OE2 1 
ATOM   5560  N  N   . TYR B 1 108 ? 30.914  7.455   40.503  1.00 10.77 ? 100  TYR B N   1 
ATOM   5561  C  CA  . TYR B 1 108 ? 30.703  8.755   41.112  1.00 11.34 ? 100  TYR B CA  1 
ATOM   5562  C  C   . TYR B 1 108 ? 30.426  8.612   42.602  1.00 10.07 ? 100  TYR B C   1 
ATOM   5563  O  O   . TYR B 1 108 ? 29.643  7.756   43.029  1.00 10.83 ? 100  TYR B O   1 
ATOM   5564  C  CB  . TYR B 1 108 ? 29.515  9.454   40.439  1.00 11.55 ? 100  TYR B CB  1 
ATOM   5565  C  CG  . TYR B 1 108 ? 29.079  10.693  41.193  1.00 12.81 ? 100  TYR B CG  1 
ATOM   5566  C  CD1 . TYR B 1 108 ? 29.775  11.887  41.057  1.00 14.93 ? 100  TYR B CD1 1 
ATOM   5567  C  CD2 . TYR B 1 108 ? 27.989  10.658  42.060  1.00 12.63 ? 100  TYR B CD2 1 
ATOM   5568  C  CE1 . TYR B 1 108 ? 29.385  13.026  41.752  1.00 20.70 ? 100  TYR B CE1 1 
ATOM   5569  C  CE2 . TYR B 1 108 ? 27.599  11.783  42.759  1.00 21.09 ? 100  TYR B CE2 1 
ATOM   5570  C  CZ  . TYR B 1 108 ? 28.300  12.957  42.604  1.00 23.25 ? 100  TYR B CZ  1 
ATOM   5571  O  OH  . TYR B 1 108 ? 27.915  14.069  43.297  1.00 23.01 ? 100  TYR B OH  1 
ATOM   5572  N  N   . GLY B 1 109 ? 31.064  9.463   43.394  1.00 10.40 ? 101  GLY B N   1 
ATOM   5573  C  CA  . GLY B 1 109 ? 30.639  9.632   44.772  1.00 15.66 ? 101  GLY B CA  1 
ATOM   5574  C  C   . GLY B 1 109 ? 31.762  9.596   45.788  1.00 16.29 ? 101  GLY B C   1 
ATOM   5575  O  O   . GLY B 1 109 ? 31.785  10.393  46.735  1.00 15.79 ? 101  GLY B O   1 
ATOM   5576  N  N   . TYR B 1 110 ? 32.694  8.665   45.605  1.00 11.24 ? 102  TYR B N   1 
ATOM   5577  C  CA  . TYR B 1 110 ? 33.711  8.408   46.610  1.00 12.01 ? 102  TYR B CA  1 
ATOM   5578  C  C   . TYR B 1 110 ? 35.098  8.238   46.024  1.00 18.10 ? 102  TYR B C   1 
ATOM   5579  O  O   . TYR B 1 110 ? 36.046  7.958   46.775  1.00 18.33 ? 102  TYR B O   1 
ATOM   5580  C  CB  . TYR B 1 110 ? 33.335  7.172   47.430  1.00 15.06 ? 102  TYR B CB  1 
ATOM   5581  C  CG  . TYR B 1 110 ? 32.083  7.423   48.222  1.00 17.69 ? 102  TYR B CG  1 
ATOM   5582  C  CD1 . TYR B 1 110 ? 32.126  8.185   49.385  1.00 16.56 ? 102  TYR B CD1 1 
ATOM   5583  C  CD2 . TYR B 1 110 ? 30.857  6.935   47.798  1.00 17.31 ? 102  TYR B CD2 1 
ATOM   5584  C  CE1 . TYR B 1 110 ? 30.985  8.451   50.111  1.00 17.37 ? 102  TYR B CE1 1 
ATOM   5585  C  CE2 . TYR B 1 110 ? 29.695  7.189   48.533  1.00 20.92 ? 102  TYR B CE2 1 
ATOM   5586  C  CZ  . TYR B 1 110 ? 29.778  7.946   49.693  1.00 20.29 ? 102  TYR B CZ  1 
ATOM   5587  O  OH  . TYR B 1 110 ? 28.652  8.215   50.448  1.00 20.35 ? 102  TYR B OH  1 
ATOM   5588  N  N   . THR B 1 111 ? 35.244  8.381   44.717  1.00 15.07 ? 103  THR B N   1 
ATOM   5589  C  CA  . THR B 1 111 ? 36.540  8.571   44.083  1.00 15.16 ? 103  THR B CA  1 
ATOM   5590  C  C   . THR B 1 111 ? 36.591  10.010  43.579  1.00 11.84 ? 103  THR B C   1 
ATOM   5591  O  O   . THR B 1 111 ? 35.780  10.392  42.729  1.00 14.68 ? 103  THR B O   1 
ATOM   5592  C  CB  . THR B 1 111 ? 36.738  7.583   42.932  1.00 13.16 ? 103  THR B CB  1 
ATOM   5593  O  OG1 . THR B 1 111 ? 36.545  6.231   43.395  1.00 14.87 ? 103  THR B OG1 1 
ATOM   5594  C  CG2 . THR B 1 111 ? 38.139  7.732   42.376  1.00 13.55 ? 103  THR B CG2 1 
ATOM   5595  N  N   . ASP B 1 112 ? 37.512  10.815  44.126  1.00 16.75 ? 104  ASP B N   1 
ATOM   5596  C  CA  . ASP B 1 112 ? 37.599  12.225  43.731  1.00 17.95 ? 104  ASP B CA  1 
ATOM   5597  C  C   . ASP B 1 112 ? 37.898  12.349  42.241  1.00 16.28 ? 104  ASP B C   1 
ATOM   5598  O  O   . ASP B 1 112 ? 38.816  11.700  41.729  1.00 14.68 ? 104  ASP B O   1 
ATOM   5599  C  CB  . ASP B 1 112 ? 38.706  12.950  44.511  1.00 17.77 ? 104  ASP B CB  1 
ATOM   5600  C  CG  . ASP B 1 112 ? 38.318  13.285  45.938  1.00 18.42 ? 104  ASP B CG  1 
ATOM   5601  O  OD1 . ASP B 1 112 ? 37.198  12.957  46.355  1.00 20.46 ? 104  ASP B OD1 1 
ATOM   5602  O  OD2 . ASP B 1 112 ? 39.152  13.891  46.640  1.00 23.15 ? 104  ASP B OD2 1 
ATOM   5603  N  N   . GLY B 1 113 ? 37.151  13.220  41.552  1.00 12.92 ? 105  GLY B N   1 
ATOM   5604  C  CA  . GLY B 1 113 ? 37.389  13.496  40.152  1.00 17.09 ? 105  GLY B CA  1 
ATOM   5605  C  C   . GLY B 1 113 ? 36.588  12.654  39.179  1.00 17.66 ? 105  GLY B C   1 
ATOM   5606  O  O   . GLY B 1 113 ? 36.674  12.892  37.966  1.00 18.15 ? 105  GLY B O   1 
ATOM   5607  N  N   . VAL B 1 114 ? 35.831  11.669  39.664  1.00 11.04 ? 106  VAL B N   1 
ATOM   5608  C  CA  . VAL B 1 114 ? 34.953  10.858  38.822  1.00 11.05 ? 106  VAL B CA  1 
ATOM   5609  C  C   . VAL B 1 114 ? 33.612  11.576  38.742  1.00 12.82 ? 106  VAL B C   1 
ATOM   5610  O  O   . VAL B 1 114 ? 32.900  11.662  39.745  1.00 16.64 ? 106  VAL B O   1 
ATOM   5611  C  CB  . VAL B 1 114 ? 34.776  9.447   39.392  1.00 11.69 ? 106  VAL B CB  1 
ATOM   5612  C  CG1 . VAL B 1 114 ? 33.675  8.712   38.608  1.00 11.32 ? 106  VAL B CG1 1 
ATOM   5613  C  CG2 . VAL B 1 114 ? 36.083  8.687   39.379  1.00 12.44 ? 106  VAL B CG2 1 
ATOM   5614  N  N   . GLU B 1 115 ? 33.248  12.072  37.546  1.00 10.11 ? 107  GLU B N   1 
ATOM   5615  C  CA  . GLU B 1 115 ? 32.076  12.938  37.413  1.00 11.83 ? 107  GLU B CA  1 
ATOM   5616  C  C   . GLU B 1 115 ? 30.777  12.168  37.267  1.00 16.67 ? 107  GLU B C   1 
ATOM   5617  O  O   . GLU B 1 115 ? 29.705  12.744  37.501  1.00 13.49 ? 107  GLU B O   1 
ATOM   5618  C  CB  . GLU B 1 115 ? 32.209  13.870  36.200  1.00 10.06 ? 107  GLU B CB  1 
ATOM   5619  C  CG  . GLU B 1 115 ? 33.440  14.787  36.213  1.00 10.56 ? 107  GLU B CG  1 
ATOM   5620  C  CD  . GLU B 1 115 ? 33.316  15.953  37.194  1.00 15.56 ? 107  GLU B CD  1 
ATOM   5621  O  OE1 . GLU B 1 115 ? 32.225  16.148  37.780  1.00 15.87 ? 107  GLU B OE1 1 
ATOM   5622  O  OE2 . GLU B 1 115 ? 34.309  16.683  37.370  1.00 13.90 ? 107  GLU B OE2 1 
ATOM   5623  N  N   . THR B 1 116 ? 30.854  10.902  36.856  1.00 11.73 ? 108  THR B N   1 
ATOM   5624  C  CA  . THR B 1 116 ? 29.681  10.070  36.623  1.00 9.38  ? 108  THR B CA  1 
ATOM   5625  C  C   . THR B 1 116 ? 30.113  8.610   36.662  1.00 14.42 ? 108  THR B C   1 
ATOM   5626  O  O   . THR B 1 116 ? 31.283  8.290   36.431  1.00 12.63 ? 108  THR B O   1 
ATOM   5627  C  CB  . THR B 1 116 ? 28.998  10.404  35.283  1.00 8.94  ? 108  THR B CB  1 
ATOM   5628  O  OG1 . THR B 1 116 ? 27.850  9.562   35.106  1.00 12.84 ? 108  THR B OG1 1 
ATOM   5629  C  CG2 . THR B 1 116 ? 29.949  10.192  34.094  1.00 12.97 ? 108  THR B CG2 1 
ATOM   5630  N  N   . THR B 1 117 ? 29.164  7.732   36.987  1.00 12.28 ? 109  THR B N   1 
ATOM   5631  C  CA  . THR B 1 117 ? 29.394  6.293   36.962  1.00 13.20 ? 109  THR B CA  1 
ATOM   5632  C  C   . THR B 1 117 ? 29.109  5.803   35.552  1.00 13.00 ? 109  THR B C   1 
ATOM   5633  O  O   . THR B 1 117 ? 27.999  5.988   35.057  1.00 11.64 ? 109  THR B O   1 
ATOM   5634  C  CB  . THR B 1 117 ? 28.483  5.580   37.960  1.00 10.35 ? 109  THR B CB  1 
ATOM   5635  O  OG1 . THR B 1 117 ? 28.738  6.078   39.279  1.00 12.07 ? 109  THR B OG1 1 
ATOM   5636  C  CG2 . THR B 1 117 ? 28.717  4.054   37.924  1.00 10.22 ? 109  THR B CG2 1 
ATOM   5637  N  N   . THR B 1 118 ? 30.107  5.211   34.890  1.00 13.08 ? 110  THR B N   1 
ATOM   5638  C  CA  . THR B 1 118 ? 29.886  4.698   33.546  1.00 13.53 ? 110  THR B CA  1 
ATOM   5639  C  C   . THR B 1 118 ? 30.317  3.241   33.477  1.00 16.77 ? 110  THR B C   1 
ATOM   5640  O  O   . THR B 1 118 ? 30.964  2.712   34.378  1.00 24.56 ? 110  THR B O   1 
ATOM   5641  C  CB  . THR B 1 118 ? 30.621  5.518   32.468  1.00 13.30 ? 110  THR B CB  1 
ATOM   5642  O  OG1 . THR B 1 118 ? 32.028  5.565   32.751  1.00 15.45 ? 110  THR B OG1 1 
ATOM   5643  C  CG2 . THR B 1 118 ? 30.045  6.931   32.387  1.00 13.61 ? 110  THR B CG2 1 
ATOM   5644  N  N   . GLY B 1 119 ? 29.942  2.603   32.379  1.00 19.78 ? 111  GLY B N   1 
ATOM   5645  C  CA  . GLY B 1 119 ? 30.089  1.179   32.216  1.00 14.56 ? 111  GLY B CA  1 
ATOM   5646  C  C   . GLY B 1 119 ? 29.086  0.687   31.191  1.00 17.56 ? 111  GLY B C   1 
ATOM   5647  O  O   . GLY B 1 119 ? 29.451  0.254   30.096  1.00 18.60 ? 111  GLY B O   1 
ATOM   5648  N  N   . PRO B 1 120 ? 27.796  0.762   31.524  1.00 15.57 ? 112  PRO B N   1 
ATOM   5649  C  CA  . PRO B 1 120 ? 26.752  0.556   30.502  1.00 11.86 ? 112  PRO B CA  1 
ATOM   5650  C  C   . PRO B 1 120 ? 26.920  1.566   29.379  1.00 10.28 ? 112  PRO B C   1 
ATOM   5651  O  O   . PRO B 1 120 ? 26.846  2.781   29.591  1.00 16.82 ? 112  PRO B O   1 
ATOM   5652  C  CB  . PRO B 1 120 ? 25.450  0.785   31.276  1.00 14.27 ? 112  PRO B CB  1 
ATOM   5653  C  CG  . PRO B 1 120 ? 25.835  0.555   32.735  1.00 14.69 ? 112  PRO B CG  1 
ATOM   5654  C  CD  . PRO B 1 120 ? 27.221  1.102   32.836  1.00 17.50 ? 112  PRO B CD  1 
ATOM   5655  N  N   . LEU B 1 121 ? 27.134  1.053   28.172  1.00 14.23 ? 113  LEU B N   1 
ATOM   5656  C  CA  . LEU B 1 121 ? 27.618  1.888   27.085  1.00 9.53  ? 113  LEU B CA  1 
ATOM   5657  C  C   . LEU B 1 121 ? 26.523  2.833   26.593  1.00 12.49 ? 113  LEU B C   1 
ATOM   5658  O  O   . LEU B 1 121 ? 25.331  2.554   26.715  1.00 11.82 ? 113  LEU B O   1 
ATOM   5659  C  CB  . LEU B 1 121 ? 28.137  1.009   25.946  1.00 11.93 ? 113  LEU B CB  1 
ATOM   5660  C  CG  . LEU B 1 121 ? 29.379  0.200   26.364  1.00 15.76 ? 113  LEU B CG  1 
ATOM   5661  C  CD1 . LEU B 1 121 ? 29.889  -0.682  25.229  1.00 19.69 ? 113  LEU B CD1 1 
ATOM   5662  C  CD2 . LEU B 1 121 ? 30.484  1.140   26.842  1.00 18.20 ? 113  LEU B CD2 1 
ATOM   5663  N  N   . GLY B 1 122 ? 26.950  3.961   26.024  1.00 10.25 ? 114  GLY B N   1 
ATOM   5664  C  CA  . GLY B 1 122 ? 26.053  4.962   25.483  1.00 14.97 ? 114  GLY B CA  1 
ATOM   5665  C  C   . GLY B 1 122 ? 25.593  6.002   26.492  1.00 10.31 ? 114  GLY B C   1 
ATOM   5666  O  O   . GLY B 1 122 ? 25.349  7.156   26.117  1.00 12.16 ? 114  GLY B O   1 
ATOM   5667  N  N   . GLN B 1 123 ? 25.486  5.639   27.769  1.00 10.49 ? 115  GLN B N   1 
ATOM   5668  C  CA  . GLN B 1 123 ? 24.946  6.614   28.720  1.00 10.92 ? 115  GLN B CA  1 
ATOM   5669  C  C   . GLN B 1 123 ? 25.953  7.696   29.087  1.00 8.92  ? 115  GLN B C   1 
ATOM   5670  O  O   . GLN B 1 123 ? 25.548  8.791   29.495  1.00 10.12 ? 115  GLN B O   1 
ATOM   5671  C  CB  . GLN B 1 123 ? 24.448  5.907   29.978  1.00 8.56  ? 115  GLN B CB  1 
ATOM   5672  C  CG  . GLN B 1 123 ? 23.205  5.055   29.703  1.00 12.15 ? 115  GLN B CG  1 
ATOM   5673  C  CD  . GLN B 1 123 ? 22.684  4.401   30.951  1.00 10.97 ? 115  GLN B CD  1 
ATOM   5674  O  OE1 . GLN B 1 123 ? 22.265  5.081   31.880  1.00 12.68 ? 115  GLN B OE1 1 
ATOM   5675  N  NE2 . GLN B 1 123 ? 22.720  3.070   30.990  1.00 8.90  ? 115  GLN B NE2 1 
ATOM   5676  N  N   . GLY B 1 124 ? 27.252  7.413   28.985  1.00 10.46 ? 116  GLY B N   1 
ATOM   5677  C  CA  . GLY B 1 124 ? 28.243  8.424   29.321  1.00 11.43 ? 116  GLY B CA  1 
ATOM   5678  C  C   . GLY B 1 124 ? 28.093  9.675   28.476  1.00 13.99 ? 116  GLY B C   1 
ATOM   5679  O  O   . GLY B 1 124 ? 28.032  10.794  28.999  1.00 10.35 ? 116  GLY B O   1 
ATOM   5680  N  N   . ILE B 1 125 ? 27.999  9.503   27.155  1.00 10.60 ? 117  ILE B N   1 
ATOM   5681  C  CA  . ILE B 1 125 ? 27.839  10.664  26.280  1.00 9.61  ? 117  ILE B CA  1 
ATOM   5682  C  C   . ILE B 1 125 ? 26.540  11.389  26.607  1.00 11.64 ? 117  ILE B C   1 
ATOM   5683  O  O   . ILE B 1 125 ? 26.484  12.622  26.598  1.00 12.86 ? 117  ILE B O   1 
ATOM   5684  C  CB  . ILE B 1 125 ? 27.926  10.254  24.789  1.00 11.68 ? 117  ILE B CB  1 
ATOM   5685  C  CG1 . ILE B 1 125 ? 27.705  11.463  23.864  1.00 17.32 ? 117  ILE B CG1 1 
ATOM   5686  C  CG2 . ILE B 1 125 ? 26.927  9.157   24.433  1.00 17.10 ? 117  ILE B CG2 1 
ATOM   5687  C  CD1 . ILE B 1 125 ? 28.733  12.580  24.037  1.00 16.09 ? 117  ILE B CD1 1 
ATOM   5688  N  N   . ALA B 1 126 ? 25.485  10.639  26.943  1.00 10.67 ? 118  ALA B N   1 
ATOM   5689  C  CA  . ALA B 1 126 ? 24.227  11.287  27.289  1.00 11.27 ? 118  ALA B CA  1 
ATOM   5690  C  C   . ALA B 1 126 ? 24.342  12.044  28.609  1.00 12.18 ? 118  ALA B C   1 
ATOM   5691  O  O   . ALA B 1 126 ? 23.854  13.174  28.714  1.00 10.96 ? 118  ALA B O   1 
ATOM   5692  C  CB  . ALA B 1 126 ? 23.096  10.259  27.324  1.00 10.98 ? 118  ALA B CB  1 
ATOM   5693  N  N   . ASN B 1 127 ? 25.012  11.461  29.614  1.00 12.74 ? 119  ASN B N   1 
ATOM   5694  C  CA  . ASN B 1 127 ? 25.321  12.227  30.822  1.00 10.26 ? 119  ASN B CA  1 
ATOM   5695  C  C   . ASN B 1 127 ? 26.035  13.524  30.475  1.00 9.31  ? 119  ASN B C   1 
ATOM   5696  O  O   . ASN B 1 127 ? 25.757  14.575  31.059  1.00 10.24 ? 119  ASN B O   1 
ATOM   5697  C  CB  . ASN B 1 127 ? 26.227  11.462  31.789  1.00 8.71  ? 119  ASN B CB  1 
ATOM   5698  C  CG  . ASN B 1 127 ? 25.656  10.123  32.269  1.00 11.48 ? 119  ASN B CG  1 
ATOM   5699  O  OD1 . ASN B 1 127 ? 26.425  9.261   32.700  1.00 12.79 ? 119  ASN B OD1 1 
ATOM   5700  N  ND2 . ASN B 1 127 ? 24.346  9.950   32.216  1.00 10.35 ? 119  ASN B ND2 1 
ATOM   5701  N  N   . ALA B 1 128 ? 27.012  13.456  29.569  1.00 11.29 ? 120  ALA B N   1 
ATOM   5702  C  CA  . ALA B 1 128 ? 27.778  14.657  29.248  1.00 10.37 ? 120  ALA B CA  1 
ATOM   5703  C  C   . ALA B 1 128 ? 26.915  15.689  28.541  1.00 10.95 ? 120  ALA B C   1 
ATOM   5704  O  O   . ALA B 1 128 ? 27.109  16.896  28.724  1.00 10.89 ? 120  ALA B O   1 
ATOM   5705  C  CB  . ALA B 1 128 ? 28.978  14.310  28.374  1.00 9.70  ? 120  ALA B CB  1 
ATOM   5706  N  N   . VAL B 1 129 ? 25.994  15.239  27.690  1.00 10.92 ? 121  VAL B N   1 
ATOM   5707  C  CA  . VAL B 1 129 ? 25.046  16.177  27.097  1.00 12.59 ? 121  VAL B CA  1 
ATOM   5708  C  C   . VAL B 1 129 ? 24.285  16.914  28.196  1.00 14.38 ? 121  VAL B C   1 
ATOM   5709  O  O   . VAL B 1 129 ? 24.074  18.131  28.120  1.00 11.28 ? 121  VAL B O   1 
ATOM   5710  C  CB  . VAL B 1 129 ? 24.093  15.448  26.128  1.00 11.72 ? 121  VAL B CB  1 
ATOM   5711  C  CG1 . VAL B 1 129 ? 22.929  16.351  25.740  1.00 11.00 ? 121  VAL B CG1 1 
ATOM   5712  C  CG2 . VAL B 1 129 ? 24.855  15.002  24.874  1.00 9.84  ? 121  VAL B CG2 1 
ATOM   5713  N  N   . GLY B 1 130 ? 23.888  16.193  29.246  1.00 10.76 ? 122  GLY B N   1 
ATOM   5714  C  CA  . GLY B 1 130 ? 23.225  16.841  30.369  1.00 11.80 ? 122  GLY B CA  1 
ATOM   5715  C  C   . GLY B 1 130 ? 24.117  17.829  31.103  1.00 12.87 ? 122  GLY B C   1 
ATOM   5716  O  O   . GLY B 1 130 ? 23.666  18.902  31.508  1.00 10.48 ? 122  GLY B O   1 
ATOM   5717  N  N   . MET B 1 131 ? 25.390  17.480  31.295  1.00 11.75 ? 123  MET B N   1 
ATOM   5718  C  CA  . MET B 1 131 ? 26.319  18.424  31.916  1.00 10.36 ? 123  MET B CA  1 
ATOM   5719  C  C   . MET B 1 131 ? 26.513  19.668  31.055  1.00 12.28 ? 123  MET B C   1 
ATOM   5720  O  O   . MET B 1 131 ? 26.559  20.785  31.579  1.00 13.59 ? 123  MET B O   1 
ATOM   5721  C  CB  . MET B 1 131 ? 27.669  17.751  32.177  1.00 10.40 ? 123  MET B CB  1 
ATOM   5722  C  CG  . MET B 1 131 ? 27.566  16.626  33.217  1.00 10.74 ? 123  MET B CG  1 
ATOM   5723  S  SD  . MET B 1 131 ? 29.094  15.698  33.324  1.00 14.12 ? 123  MET B SD  1 
ATOM   5724  C  CE  . MET B 1 131 ? 28.566  14.333  34.376  1.00 12.95 ? 123  MET B CE  1 
ATOM   5725  N  N   . ALA B 1 132 ? 26.666  19.495  29.735  1.00 10.97 ? 124  ALA B N   1 
ATOM   5726  C  CA  . ALA B 1 132 ? 26.810  20.662  28.861  1.00 11.83 ? 124  ALA B CA  1 
ATOM   5727  C  C   . ALA B 1 132 ? 25.545  21.503  28.857  1.00 15.42 ? 124  ALA B C   1 
ATOM   5728  O  O   . ALA B 1 132 ? 25.610  22.737  28.778  1.00 14.50 ? 124  ALA B O   1 
ATOM   5729  C  CB  . ALA B 1 132 ? 27.149  20.233  27.431  1.00 13.05 ? 124  ALA B CB  1 
ATOM   5730  N  N   . LEU B 1 133 ? 24.381  20.847  28.903  1.00 12.69 ? 125  LEU B N   1 
ATOM   5731  C  CA  . LEU B 1 133 ? 23.118  21.575  28.942  1.00 14.80 ? 125  LEU B CA  1 
ATOM   5732  C  C   . LEU B 1 133 ? 22.983  22.358  30.240  1.00 13.66 ? 125  LEU B C   1 
ATOM   5733  O  O   . LEU B 1 133 ? 22.549  23.517  30.231  1.00 13.03 ? 125  LEU B O   1 
ATOM   5734  C  CB  . LEU B 1 133 ? 21.959  20.588  28.762  1.00 12.84 ? 125  LEU B CB  1 
ATOM   5735  C  CG  . LEU B 1 133 ? 20.535  21.054  28.535  1.00 19.42 ? 125  LEU B CG  1 
ATOM   5736  C  CD1 . LEU B 1 133 ? 20.469  22.095  27.430  1.00 18.53 ? 125  LEU B CD1 1 
ATOM   5737  C  CD2 . LEU B 1 133 ? 19.707  19.832  28.166  1.00 19.19 ? 125  LEU B CD2 1 
ATOM   5738  N  N   . ALA B 1 134 ? 23.387  21.755  31.363  1.00 11.67 ? 126  ALA B N   1 
ATOM   5739  C  CA  . ALA B 1 134 ? 23.364  22.467  32.638  1.00 16.43 ? 126  ALA B CA  1 
ATOM   5740  C  C   . ALA B 1 134 ? 24.225  23.724  32.586  1.00 13.21 ? 126  ALA B C   1 
ATOM   5741  O  O   . ALA B 1 134 ? 23.799  24.797  33.027  1.00 18.35 ? 126  ALA B O   1 
ATOM   5742  C  CB  . ALA B 1 134 ? 23.822  21.548  33.769  1.00 16.08 ? 126  ALA B CB  1 
ATOM   5743  N  N   . GLU B 1 135 ? 25.431  23.623  32.026  1.00 13.13 ? 127  GLU B N   1 
ATOM   5744  C  CA  . GLU B 1 135 ? 26.288  24.801  31.914  1.00 15.42 ? 127  GLU B CA  1 
ATOM   5745  C  C   . GLU B 1 135 ? 25.617  25.875  31.069  1.00 15.49 ? 127  GLU B C   1 
ATOM   5746  O  O   . GLU B 1 135 ? 25.629  27.058  31.422  1.00 14.63 ? 127  GLU B O   1 
ATOM   5747  C  CB  . GLU B 1 135 ? 27.640  24.425  31.314  1.00 13.20 ? 127  GLU B CB  1 
ATOM   5748  C  CG  . GLU B 1 135 ? 28.717  25.516  31.397  1.00 15.73 ? 127  GLU B CG  1 
ATOM   5749  C  CD  . GLU B 1 135 ? 28.756  26.441  30.186  1.00 23.21 ? 127  GLU B CD  1 
ATOM   5750  O  OE1 . GLU B 1 135 ? 27.963  26.251  29.230  1.00 18.43 ? 127  GLU B OE1 1 
ATOM   5751  O  OE2 . GLU B 1 135 ? 29.608  27.354  30.184  1.00 16.85 ? 127  GLU B OE2 1 
ATOM   5752  N  N   . LYS B 1 136 ? 25.030  25.474  29.940  1.00 15.97 ? 128  LYS B N   1 
ATOM   5753  C  CA  . LYS B 1 136 ? 24.384  26.433  29.049  1.00 14.27 ? 128  LYS B CA  1 
ATOM   5754  C  C   . LYS B 1 136 ? 23.217  27.120  29.747  1.00 14.68 ? 128  LYS B C   1 
ATOM   5755  O  O   . LYS B 1 136 ? 23.054  28.340  29.656  1.00 16.16 ? 128  LYS B O   1 
ATOM   5756  C  CB  . LYS B 1 136 ? 23.926  25.705  27.775  1.00 14.94 ? 128  LYS B CB  1 
ATOM   5757  C  CG  . LYS B 1 136 ? 23.103  26.552  26.787  1.00 25.65 ? 128  LYS B CG  1 
ATOM   5758  C  CD  . LYS B 1 136 ? 21.659  26.037  26.715  1.00 34.20 ? 128  LYS B CD  1 
ATOM   5759  C  CE  . LYS B 1 136 ? 21.061  26.089  25.297  1.00 32.95 ? 128  LYS B CE  1 
ATOM   5760  N  NZ  . LYS B 1 136 ? 21.062  27.461  24.716  1.00 31.64 ? 128  LYS B NZ  1 
ATOM   5761  N  N   . ILE B 1 137 ? 22.395  26.338  30.451  1.00 17.07 ? 129  ILE B N   1 
ATOM   5762  C  CA  . ILE B 1 137 ? 21.233  26.866  31.171  1.00 20.17 ? 129  ILE B CA  1 
ATOM   5763  C  C   . ILE B 1 137 ? 21.674  27.829  32.270  1.00 19.32 ? 129  ILE B C   1 
ATOM   5764  O  O   . ILE B 1 137 ? 21.096  28.909  32.454  1.00 20.85 ? 129  ILE B O   1 
ATOM   5765  C  CB  . ILE B 1 137 ? 20.412  25.697  31.761  1.00 24.15 ? 129  ILE B CB  1 
ATOM   5766  C  CG1 . ILE B 1 137 ? 19.631  24.957  30.676  1.00 27.09 ? 129  ILE B CG1 1 
ATOM   5767  C  CG2 . ILE B 1 137 ? 19.472  26.174  32.874  1.00 27.09 ? 129  ILE B CG2 1 
ATOM   5768  C  CD1 . ILE B 1 137 ? 18.892  23.735  31.229  1.00 26.70 ? 129  ILE B CD1 1 
ATOM   5769  N  N   . LEU B 1 138 ? 22.678  27.424  33.046  1.00 17.18 ? 130  LEU B N   1 
ATOM   5770  C  CA  . LEU B 1 138 ? 23.140  28.243  34.158  1.00 17.45 ? 130  LEU B CA  1 
ATOM   5771  C  C   . LEU B 1 138 ? 23.854  29.496  33.666  1.00 17.24 ? 130  LEU B C   1 
ATOM   5772  O  O   . LEU B 1 138 ? 23.763  30.556  34.298  1.00 17.16 ? 130  LEU B O   1 
ATOM   5773  C  CB  . LEU B 1 138 ? 24.057  27.412  35.058  1.00 17.41 ? 130  LEU B CB  1 
ATOM   5774  C  CG  . LEU B 1 138 ? 23.360  26.269  35.812  1.00 15.61 ? 130  LEU B CG  1 
ATOM   5775  C  CD1 . LEU B 1 138 ? 24.379  25.287  36.388  1.00 14.65 ? 130  LEU B CD1 1 
ATOM   5776  C  CD2 . LEU B 1 138 ? 22.493  26.843  36.920  1.00 17.11 ? 130  LEU B CD2 1 
ATOM   5777  N  N   . ALA B 1 139 ? 24.594  29.393  32.560  1.00 16.21 ? 131  ALA B N   1 
ATOM   5778  C  CA  . ALA B 1 139 ? 25.248  30.580  32.011  1.00 17.10 ? 131  ALA B CA  1 
ATOM   5779  C  C   . ALA B 1 139 ? 24.220  31.623  31.604  1.00 17.89 ? 131  ALA B C   1 
ATOM   5780  O  O   . ALA B 1 139 ? 24.406  32.823  31.848  1.00 18.87 ? 131  ALA B O   1 
ATOM   5781  C  CB  . ALA B 1 139 ? 26.122  30.207  30.815  1.00 19.77 ? 131  ALA B CB  1 
ATOM   5782  N  N   . ALA B 1 140 ? 23.128  31.179  30.981  1.00 17.55 ? 132  ALA B N   1 
ATOM   5783  C  CA  . ALA B 1 140 ? 22.091  32.107  30.542  1.00 18.33 ? 132  ALA B CA  1 
ATOM   5784  C  C   . ALA B 1 140 ? 21.392  32.744  31.732  1.00 18.90 ? 132  ALA B C   1 
ATOM   5785  O  O   . ALA B 1 140 ? 21.009  33.918  31.685  1.00 19.93 ? 132  ALA B O   1 
ATOM   5786  C  CB  . ALA B 1 140 ? 21.084  31.377  29.652  1.00 21.64 ? 132  ALA B CB  1 
ATOM   5787  N  N   . GLU B 1 141 ? 21.227  31.984  32.812  1.00 19.59 ? 133  GLU B N   1 
ATOM   5788  C  CA  . GLU B 1 141 ? 20.516  32.509  33.967  1.00 21.46 ? 133  GLU B CA  1 
ATOM   5789  C  C   . GLU B 1 141 ? 21.399  33.430  34.804  1.00 19.64 ? 133  GLU B C   1 
ATOM   5790  O  O   . GLU B 1 141 ? 20.934  34.467  35.281  1.00 20.64 ? 133  GLU B O   1 
ATOM   5791  C  CB  . GLU B 1 141 ? 19.980  31.356  34.820  1.00 18.90 ? 133  GLU B CB  1 
ATOM   5792  C  CG  . GLU B 1 141 ? 19.199  31.812  36.045  1.00 28.50 ? 133  GLU B CG  1 
ATOM   5793  C  CD  . GLU B 1 141 ? 18.704  30.664  36.913  1.00 30.87 ? 133  GLU B CD  1 
ATOM   5794  O  OE1 . GLU B 1 141 ? 18.985  29.487  36.593  1.00 29.19 ? 133  GLU B OE1 1 
ATOM   5795  O  OE2 . GLU B 1 141 ? 18.025  30.947  37.921  1.00 30.32 ? 133  GLU B OE2 1 
ATOM   5796  N  N   . PHE B 1 142 ? 22.674  33.090  34.977  1.00 20.17 ? 134  PHE B N   1 
ATOM   5797  C  CA  . PHE B 1 142 ? 23.497  33.763  35.977  1.00 19.93 ? 134  PHE B CA  1 
ATOM   5798  C  C   . PHE B 1 142 ? 24.527  34.739  35.425  1.00 20.74 ? 134  PHE B C   1 
ATOM   5799  O  O   . PHE B 1 142 ? 24.871  35.695  36.126  1.00 22.90 ? 134  PHE B O   1 
ATOM   5800  C  CB  . PHE B 1 142 ? 24.221  32.726  36.847  1.00 20.59 ? 134  PHE B CB  1 
ATOM   5801  C  CG  . PHE B 1 142 ? 23.343  32.104  37.894  1.00 18.78 ? 134  PHE B CG  1 
ATOM   5802  C  CD1 . PHE B 1 142 ? 23.078  32.777  39.080  1.00 25.46 ? 134  PHE B CD1 1 
ATOM   5803  C  CD2 . PHE B 1 142 ? 22.760  30.862  37.683  1.00 19.16 ? 134  PHE B CD2 1 
ATOM   5804  C  CE1 . PHE B 1 142 ? 22.258  32.223  40.043  1.00 19.31 ? 134  PHE B CE1 1 
ATOM   5805  C  CE2 . PHE B 1 142 ? 21.938  30.295  38.646  1.00 18.30 ? 134  PHE B CE2 1 
ATOM   5806  C  CZ  . PHE B 1 142 ? 21.691  30.981  39.829  1.00 18.40 ? 134  PHE B CZ  1 
ATOM   5807  N  N   . ASN B 1 143 ? 25.051  34.535  34.218  1.00 25.33 ? 135  ASN B N   1 
ATOM   5808  C  CA  . ASN B 1 143 ? 26.101  35.424  33.732  1.00 23.84 ? 135  ASN B CA  1 
ATOM   5809  C  C   . ASN B 1 143 ? 25.555  36.828  33.519  1.00 26.21 ? 135  ASN B C   1 
ATOM   5810  O  O   . ASN B 1 143 ? 24.429  37.005  33.054  1.00 22.71 ? 135  ASN B O   1 
ATOM   5811  C  CB  . ASN B 1 143 ? 26.706  34.905  32.430  1.00 20.80 ? 135  ASN B CB  1 
ATOM   5812  C  CG  . ASN B 1 143 ? 27.561  33.665  32.635  1.00 21.82 ? 135  ASN B CG  1 
ATOM   5813  O  OD1 . ASN B 1 143 ? 27.917  33.308  33.765  1.00 19.68 ? 135  ASN B OD1 1 
ATOM   5814  N  ND2 . ASN B 1 143 ? 27.905  33.006  31.534  1.00 22.72 ? 135  ASN B ND2 1 
ATOM   5815  N  N   . LYS B 1 144 ? 26.366  37.826  33.878  1.00 27.16 ? 136  LYS B N   1 
ATOM   5816  C  CA  . LYS B 1 144 ? 26.031  39.239  33.756  1.00 33.24 ? 136  LYS B CA  1 
ATOM   5817  C  C   . LYS B 1 144 ? 27.133  39.946  32.978  1.00 37.77 ? 136  LYS B C   1 
ATOM   5818  O  O   . LYS B 1 144 ? 28.226  39.406  32.781  1.00 41.16 ? 136  LYS B O   1 
ATOM   5819  C  CB  . LYS B 1 144 ? 25.850  39.900  35.129  1.00 34.11 ? 136  LYS B CB  1 
ATOM   5820  C  CG  . LYS B 1 144 ? 24.734  39.303  35.974  1.00 30.76 ? 136  LYS B CG  1 
ATOM   5821  C  CD  . LYS B 1 144 ? 23.405  39.400  35.264  1.00 35.49 ? 136  LYS B CD  1 
ATOM   5822  C  CE  . LYS B 1 144 ? 22.283  39.728  36.239  1.00 44.57 ? 136  LYS B CE  1 
ATOM   5823  N  NZ  . LYS B 1 144 ? 22.155  38.708  37.309  1.00 49.35 ? 136  LYS B NZ  1 
ATOM   5824  N  N   . ASP B 1 145 ? 26.831  41.171  32.544  1.00 38.25 ? 137  ASP B N   1 
ATOM   5825  C  CA  . ASP B 1 145 ? 27.743  41.968  31.727  1.00 37.05 ? 137  ASP B CA  1 
ATOM   5826  C  C   . ASP B 1 145 ? 29.152  42.005  32.308  1.00 35.49 ? 137  ASP B C   1 
ATOM   5827  O  O   . ASP B 1 145 ? 29.374  42.558  33.391  1.00 37.16 ? 137  ASP B O   1 
ATOM   5828  C  CB  . ASP B 1 145 ? 27.207  43.392  31.568  1.00 41.53 ? 137  ASP B CB  1 
ATOM   5829  N  N   . GLY B 1 146 ? 30.105  41.412  31.594  1.00 36.30 ? 138  GLY B N   1 
ATOM   5830  C  CA  . GLY B 1 146 ? 31.491  41.384  32.020  1.00 42.52 ? 138  GLY B CA  1 
ATOM   5831  C  C   . GLY B 1 146 ? 31.833  40.350  33.073  1.00 40.70 ? 138  GLY B C   1 
ATOM   5832  O  O   . GLY B 1 146 ? 33.000  40.269  33.482  1.00 45.49 ? 138  GLY B O   1 
ATOM   5833  N  N   . LEU B 1 147 ? 30.864  39.552  33.522  1.00 30.59 ? 139  LEU B N   1 
ATOM   5834  C  CA  . LEU B 1 147 ? 31.040  38.632  34.648  1.00 27.41 ? 139  LEU B CA  1 
ATOM   5835  C  C   . LEU B 1 147 ? 30.469  37.272  34.253  1.00 25.57 ? 139  LEU B C   1 
ATOM   5836  O  O   . LEU B 1 147 ? 29.343  36.925  34.617  1.00 23.10 ? 139  LEU B O   1 
ATOM   5837  C  CB  . LEU B 1 147 ? 30.368  39.196  35.900  1.00 29.73 ? 139  LEU B CB  1 
ATOM   5838  C  CG  . LEU B 1 147 ? 30.904  40.531  36.409  1.00 32.32 ? 139  LEU B CG  1 
ATOM   5839  C  CD1 . LEU B 1 147 ? 30.038  41.069  37.533  1.00 32.32 ? 139  LEU B CD1 1 
ATOM   5840  C  CD2 . LEU B 1 147 ? 32.346  40.380  36.867  1.00 33.67 ? 139  LEU B CD2 1 
ATOM   5841  N  N   . ASN B 1 148 ? 31.250  36.494  33.498  1.00 22.96 ? 140  ASN B N   1 
ATOM   5842  C  CA  . ASN B 1 148 ? 30.800  35.181  33.041  1.00 31.09 ? 140  ASN B CA  1 
ATOM   5843  C  C   . ASN B 1 148 ? 31.243  34.135  34.059  1.00 26.28 ? 140  ASN B C   1 
ATOM   5844  O  O   . ASN B 1 148 ? 32.218  33.410  33.863  1.00 27.85 ? 140  ASN B O   1 
ATOM   5845  C  CB  . ASN B 1 148 ? 31.346  34.873  31.651  1.00 31.79 ? 140  ASN B CB  1 
ATOM   5846  C  CG  . ASN B 1 148 ? 30.759  35.770  30.581  1.00 38.98 ? 140  ASN B CG  1 
ATOM   5847  O  OD1 . ASN B 1 148 ? 29.695  36.356  30.761  1.00 35.85 ? 140  ASN B OD1 1 
ATOM   5848  N  ND2 . ASN B 1 148 ? 31.452  35.879  29.458  1.00 47.90 ? 140  ASN B ND2 1 
ATOM   5849  N  N   . ILE B 1 149 ? 30.492  34.045  35.163  1.00 21.97 ? 141  ILE B N   1 
ATOM   5850  C  CA  . ILE B 1 149 ? 30.879  33.129  36.234  1.00 20.01 ? 141  ILE B CA  1 
ATOM   5851  C  C   . ILE B 1 149 ? 30.587  31.675  35.890  1.00 21.00 ? 141  ILE B C   1 
ATOM   5852  O  O   . ILE B 1 149 ? 31.126  30.776  36.543  1.00 20.63 ? 141  ILE B O   1 
ATOM   5853  C  CB  . ILE B 1 149 ? 30.208  33.491  37.574  1.00 20.36 ? 141  ILE B CB  1 
ATOM   5854  C  CG1 . ILE B 1 149 ? 28.680  33.494  37.434  1.00 28.45 ? 141  ILE B CG1 1 
ATOM   5855  C  CG2 . ILE B 1 149 ? 30.729  34.823  38.087  1.00 23.69 ? 141  ILE B CG2 1 
ATOM   5856  C  CD1 . ILE B 1 149 ? 27.942  33.550  38.767  1.00 20.29 ? 141  ILE B CD1 1 
ATOM   5857  N  N   . VAL B 1 150 ? 29.744  31.407  34.895  1.00 20.43 ? 142  VAL B N   1 
ATOM   5858  C  CA  . VAL B 1 150 ? 29.550  30.059  34.369  1.00 17.18 ? 142  VAL B CA  1 
ATOM   5859  C  C   . VAL B 1 150 ? 30.148  30.034  32.971  1.00 19.39 ? 142  VAL B C   1 
ATOM   5860  O  O   . VAL B 1 150 ? 29.615  30.654  32.044  1.00 21.77 ? 142  VAL B O   1 
ATOM   5861  C  CB  . VAL B 1 150 ? 28.072  29.652  34.353  1.00 18.94 ? 142  VAL B CB  1 
ATOM   5862  C  CG1 . VAL B 1 150 ? 27.890  28.210  33.815  1.00 15.62 ? 142  VAL B CG1 1 
ATOM   5863  C  CG2 . VAL B 1 150 ? 27.476  29.792  35.745  1.00 16.84 ? 142  VAL B CG2 1 
ATOM   5864  N  N   . ASP B 1 151 ? 31.254  29.313  32.814  1.00 17.65 ? 143  ASP B N   1 
ATOM   5865  C  CA  . ASP B 1 151 ? 31.954  29.271  31.540  1.00 19.50 ? 143  ASP B CA  1 
ATOM   5866  C  C   . ASP B 1 151 ? 32.967  28.138  31.574  1.00 18.97 ? 143  ASP B C   1 
ATOM   5867  O  O   . ASP B 1 151 ? 34.105  28.336  32.012  1.00 16.88 ? 143  ASP B O   1 
ATOM   5868  C  CB  . ASP B 1 151 ? 32.653  30.604  31.260  1.00 18.15 ? 143  ASP B CB  1 
ATOM   5869  C  CG  . ASP B 1 151 ? 33.285  30.655  29.886  1.00 27.24 ? 143  ASP B CG  1 
ATOM   5870  O  OD1 . ASP B 1 151 ? 33.174  29.669  29.129  1.00 28.56 ? 143  ASP B OD1 1 
ATOM   5871  O  OD2 . ASP B 1 151 ? 33.884  31.694  29.558  1.00 30.56 ? 143  ASP B OD2 1 
ATOM   5872  N  N   . HIS B 1 152 ? 32.558  26.950  31.139  1.00 18.19 ? 144  HIS B N   1 
ATOM   5873  C  CA  . HIS B 1 152 ? 33.463  25.810  31.112  1.00 19.52 ? 144  HIS B CA  1 
ATOM   5874  C  C   . HIS B 1 152 ? 32.954  24.818  30.082  1.00 16.21 ? 144  HIS B C   1 
ATOM   5875  O  O   . HIS B 1 152 ? 31.802  24.874  29.634  1.00 17.03 ? 144  HIS B O   1 
ATOM   5876  C  CB  . HIS B 1 152 ? 33.599  25.151  32.494  1.00 15.33 ? 144  HIS B CB  1 
ATOM   5877  C  CG  . HIS B 1 152 ? 32.295  24.688  33.070  1.00 15.61 ? 144  HIS B CG  1 
ATOM   5878  N  ND1 . HIS B 1 152 ? 31.582  25.431  33.986  1.00 20.28 ? 144  HIS B ND1 1 
ATOM   5879  C  CD2 . HIS B 1 152 ? 31.565  23.569  32.843  1.00 19.72 ? 144  HIS B CD2 1 
ATOM   5880  C  CE1 . HIS B 1 152 ? 30.477  24.783  34.312  1.00 18.35 ? 144  HIS B CE1 1 
ATOM   5881  N  NE2 . HIS B 1 152 ? 30.439  23.655  33.627  1.00 15.65 ? 144  HIS B NE2 1 
ATOM   5882  N  N   . TYR B 1 153 ? 33.829  23.895  29.728  1.00 16.09 ? 145  TYR B N   1 
ATOM   5883  C  CA  . TYR B 1 153 ? 33.582  22.923  28.679  1.00 16.62 ? 145  TYR B CA  1 
ATOM   5884  C  C   . TYR B 1 153 ? 33.225  21.564  29.261  1.00 17.28 ? 145  TYR B C   1 
ATOM   5885  O  O   . TYR B 1 153 ? 33.462  21.272  30.441  1.00 18.68 ? 145  TYR B O   1 
ATOM   5886  C  CB  . TYR B 1 153 ? 34.811  22.799  27.773  1.00 21.14 ? 145  TYR B CB  1 
ATOM   5887  C  CG  . TYR B 1 153 ? 34.938  23.975  26.832  1.00 22.08 ? 145  TYR B CG  1 
ATOM   5888  C  CD1 . TYR B 1 153 ? 35.389  25.208  27.290  1.00 32.44 ? 145  TYR B CD1 1 
ATOM   5889  C  CD2 . TYR B 1 153 ? 34.558  23.871  25.501  1.00 25.76 ? 145  TYR B CD2 1 
ATOM   5890  C  CE1 . TYR B 1 153 ? 35.483  26.297  26.448  1.00 35.68 ? 145  TYR B CE1 1 
ATOM   5891  C  CE2 . TYR B 1 153 ? 34.658  24.960  24.644  1.00 30.17 ? 145  TYR B CE2 1 
ATOM   5892  C  CZ  . TYR B 1 153 ? 35.118  26.168  25.125  1.00 39.18 ? 145  TYR B CZ  1 
ATOM   5893  O  OH  . TYR B 1 153 ? 35.218  27.257  24.286  1.00 47.46 ? 145  TYR B OH  1 
ATOM   5894  N  N   . THR B 1 154 ? 32.670  20.724  28.393  1.00 13.89 ? 146  THR B N   1 
ATOM   5895  C  CA  . THR B 1 154 ? 32.335  19.337  28.696  1.00 11.73 ? 146  THR B CA  1 
ATOM   5896  C  C   . THR B 1 154 ? 33.052  18.473  27.663  1.00 14.95 ? 146  THR B C   1 
ATOM   5897  O  O   . THR B 1 154 ? 32.737  18.540  26.470  1.00 15.60 ? 146  THR B O   1 
ATOM   5898  C  CB  . THR B 1 154 ? 30.821  19.122  28.659  1.00 14.16 ? 146  THR B CB  1 
ATOM   5899  O  OG1 . THR B 1 154 ? 30.182  20.069  29.527  1.00 16.50 ? 146  THR B OG1 1 
ATOM   5900  C  CG2 . THR B 1 154 ? 30.466  17.697  29.098  1.00 11.42 ? 146  THR B CG2 1 
ATOM   5901  N  N   . TYR B 1 155 ? 34.035  17.694  28.106  1.00 12.03 ? 147  TYR B N   1 
ATOM   5902  C  CA  . TYR B 1 155 ? 34.809  16.828  27.224  1.00 14.05 ? 147  TYR B CA  1 
ATOM   5903  C  C   . TYR B 1 155 ? 34.438  15.372  27.459  1.00 15.55 ? 147  TYR B C   1 
ATOM   5904  O  O   . TYR B 1 155 ? 34.225  14.950  28.601  1.00 14.07 ? 147  TYR B O   1 
ATOM   5905  C  CB  . TYR B 1 155 ? 36.314  17.000  27.435  1.00 13.29 ? 147  TYR B CB  1 
ATOM   5906  C  CG  . TYR B 1 155 ? 36.861  18.388  27.154  1.00 14.94 ? 147  TYR B CG  1 
ATOM   5907  C  CD1 . TYR B 1 155 ? 37.149  18.796  25.854  1.00 14.25 ? 147  TYR B CD1 1 
ATOM   5908  C  CD2 . TYR B 1 155 ? 37.129  19.273  28.191  1.00 17.75 ? 147  TYR B CD2 1 
ATOM   5909  C  CE1 . TYR B 1 155 ? 37.680  20.059  25.594  1.00 14.60 ? 147  TYR B CE1 1 
ATOM   5910  C  CE2 . TYR B 1 155 ? 37.669  20.551  27.939  1.00 17.95 ? 147  TYR B CE2 1 
ATOM   5911  C  CZ  . TYR B 1 155 ? 37.930  20.930  26.636  1.00 18.00 ? 147  TYR B CZ  1 
ATOM   5912  O  OH  . TYR B 1 155 ? 38.445  22.176  26.362  1.00 24.46 ? 147  TYR B OH  1 
ATOM   5913  N  N   . VAL B 1 156 ? 34.374  14.604  26.376  1.00 12.56 ? 148  VAL B N   1 
ATOM   5914  C  CA  . VAL B 1 156 ? 33.950  13.211  26.426  1.00 11.71 ? 148  VAL B CA  1 
ATOM   5915  C  C   . VAL B 1 156 ? 34.926  12.369  25.619  1.00 11.97 ? 148  VAL B C   1 
ATOM   5916  O  O   . VAL B 1 156 ? 35.294  12.737  24.498  1.00 14.39 ? 148  VAL B O   1 
ATOM   5917  C  CB  . VAL B 1 156 ? 32.520  13.019  25.873  1.00 11.48 ? 148  VAL B CB  1 
ATOM   5918  C  CG1 . VAL B 1 156 ? 31.994  11.626  26.205  1.00 11.48 ? 148  VAL B CG1 1 
ATOM   5919  C  CG2 . VAL B 1 156 ? 31.606  14.086  26.401  1.00 11.56 ? 148  VAL B CG2 1 
ATOM   5920  N  N   . PHE B 1 157 ? 35.327  11.236  26.177  1.00 10.86 ? 149  PHE B N   1 
ATOM   5921  C  CA  . PHE B 1 157 ? 35.885  10.158  25.373  1.00 12.70 ? 149  PHE B CA  1 
ATOM   5922  C  C   . PHE B 1 157 ? 34.798  9.114   25.155  1.00 15.29 ? 149  PHE B C   1 
ATOM   5923  O  O   . PHE B 1 157 ? 34.066  8.766   26.083  1.00 14.71 ? 149  PHE B O   1 
ATOM   5924  C  CB  . PHE B 1 157 ? 37.100  9.508   26.038  1.00 11.35 ? 149  PHE B CB  1 
ATOM   5925  C  CG  . PHE B 1 157 ? 38.355  10.358  26.014  1.00 14.03 ? 149  PHE B CG  1 
ATOM   5926  C  CD1 . PHE B 1 157 ? 38.341  11.654  25.503  1.00 12.81 ? 149  PHE B CD1 1 
ATOM   5927  C  CD2 . PHE B 1 157 ? 39.552  9.843   26.488  1.00 17.69 ? 149  PHE B CD2 1 
ATOM   5928  C  CE1 . PHE B 1 157 ? 39.500  12.424  25.477  1.00 12.74 ? 149  PHE B CE1 1 
ATOM   5929  C  CE2 . PHE B 1 157 ? 40.726  10.606  26.470  1.00 21.58 ? 149  PHE B CE2 1 
ATOM   5930  C  CZ  . PHE B 1 157 ? 40.696  11.907  25.971  1.00 14.95 ? 149  PHE B CZ  1 
ATOM   5931  N  N   . MET B 1 158 ? 34.686  8.615   23.928  1.00 13.87 ? 150  MET B N   1 
ATOM   5932  C  CA  . MET B 1 158 ? 33.712  7.559   23.680  1.00 14.54 ? 150  MET B CA  1 
ATOM   5933  C  C   . MET B 1 158 ? 34.257  6.640   22.605  1.00 12.52 ? 150  MET B C   1 
ATOM   5934  O  O   . MET B 1 158 ? 35.188  6.995   21.878  1.00 14.82 ? 150  MET B O   1 
ATOM   5935  C  CB  . MET B 1 158 ? 32.333  8.123   23.301  1.00 18.93 ? 150  MET B CB  1 
ATOM   5936  C  CG  . MET B 1 158 ? 32.202  8.847   21.977  1.00 19.09 ? 150  MET B CG  1 
ATOM   5937  S  SD  . MET B 1 158 ? 30.560  9.667   21.862  1.00 19.35 ? 150  MET B SD  1 
ATOM   5938  C  CE  . MET B 1 158 ? 29.424  8.293   21.918  1.00 18.94 ? 150  MET B CE  1 
ATOM   5939  N  N   . GLY B 1 159 ? 33.671  5.445   22.518  1.00 12.06 ? 151  GLY B N   1 
ATOM   5940  C  CA  . GLY B 1 159 ? 34.134  4.418   21.614  1.00 15.62 ? 151  GLY B CA  1 
ATOM   5941  C  C   . GLY B 1 159 ? 33.044  3.919   20.676  1.00 19.58 ? 151  GLY B C   1 
ATOM   5942  O  O   . GLY B 1 159 ? 31.914  4.418   20.660  1.00 15.21 ? 151  GLY B O   1 
ATOM   5943  N  N   . ASP B 1 160 ? 33.425  2.916   19.872  1.00 17.05 ? 152  ASP B N   1 
ATOM   5944  C  CA  . ASP B 1 160 ? 32.520  2.344   18.878  1.00 12.68 ? 152  ASP B CA  1 
ATOM   5945  C  C   . ASP B 1 160 ? 31.242  1.823   19.519  1.00 12.12 ? 152  ASP B C   1 
ATOM   5946  O  O   . ASP B 1 160 ? 30.150  1.976   18.953  1.00 15.10 ? 152  ASP B O   1 
ATOM   5947  C  CB  . ASP B 1 160 ? 33.217  1.211   18.120  1.00 14.80 ? 152  ASP B CB  1 
ATOM   5948  C  CG  . ASP B 1 160 ? 34.448  1.680   17.370  1.00 20.58 ? 152  ASP B CG  1 
ATOM   5949  O  OD1 . ASP B 1 160 ? 34.298  2.503   16.449  1.00 22.86 ? 152  ASP B OD1 1 
ATOM   5950  O  OD2 . ASP B 1 160 ? 35.564  1.225   17.708  1.00 25.53 ? 152  ASP B OD2 1 
ATOM   5951  N  N   . GLY B 1 161 ? 31.357  1.193   20.688  1.00 11.55 ? 153  GLY B N   1 
ATOM   5952  C  CA  . GLY B 1 161 ? 30.189  0.614   21.341  1.00 11.28 ? 153  GLY B CA  1 
ATOM   5953  C  C   . GLY B 1 161 ? 29.183  1.687   21.726  1.00 12.10 ? 153  GLY B C   1 
ATOM   5954  O  O   . GLY B 1 161 ? 27.982  1.530   21.539  1.00 11.25 ? 153  GLY B O   1 
HETATM 5955  N  N   . OCS B 1 162 ? 29.683  2.791   22.266  1.00 10.49 ? 154  OCS B N   1 
HETATM 5956  C  CA  . OCS B 1 162 ? 28.826  3.927   22.598  1.00 15.82 ? 154  OCS B CA  1 
HETATM 5957  C  CB  . OCS B 1 162 ? 29.667  5.061   23.153  1.00 13.71 ? 154  OCS B CB  1 
HETATM 5958  S  SG  . OCS B 1 162 ? 30.526  4.580   24.642  1.00 18.64 ? 154  OCS B SG  1 
HETATM 5959  C  C   . OCS B 1 162 ? 28.054  4.421   21.381  1.00 10.22 ? 154  OCS B C   1 
HETATM 5960  O  O   . OCS B 1 162 ? 26.854  4.699   21.468  1.00 14.54 ? 154  OCS B O   1 
HETATM 5961  O  OD1 . OCS B 1 162 ? 31.677  5.396   24.808  1.00 24.47 ? 154  OCS B OD1 1 
HETATM 5962  O  OD2 . OCS B 1 162 ? 29.613  4.786   25.700  1.00 13.09 ? 154  OCS B OD2 1 
HETATM 5963  O  OD3 . OCS B 1 162 ? 30.932  3.241   24.540  1.00 39.18 ? 154  OCS B OD3 1 
ATOM   5964  N  N   . LEU B 1 163 ? 28.751  4.512   20.253  1.00 10.60 ? 155  LEU B N   1 
ATOM   5965  C  CA  . LEU B 1 163 ? 28.151  5.034   19.021  1.00 10.92 ? 155  LEU B CA  1 
ATOM   5966  C  C   . LEU B 1 163 ? 27.132  4.086   18.408  1.00 15.15 ? 155  LEU B C   1 
ATOM   5967  O  O   . LEU B 1 163 ? 26.175  4.531   17.756  1.00 12.08 ? 155  LEU B O   1 
ATOM   5968  C  CB  . LEU B 1 163 ? 29.221  5.337   17.994  1.00 11.27 ? 155  LEU B CB  1 
ATOM   5969  C  CG  . LEU B 1 163 ? 30.053  6.562   18.319  1.00 15.20 ? 155  LEU B CG  1 
ATOM   5970  C  CD1 . LEU B 1 163 ? 31.163  6.727   17.280  1.00 15.44 ? 155  LEU B CD1 1 
ATOM   5971  C  CD2 . LEU B 1 163 ? 29.137  7.790   18.357  1.00 11.89 ? 155  LEU B CD2 1 
ATOM   5972  N  N   . MET B 1 164 ? 27.336  2.782   18.602  1.00 11.17 ? 156  MET B N   1 
ATOM   5973  C  CA  . MET B 1 164 ? 26.346  1.824   18.118  1.00 11.42 ? 156  MET B CA  1 
ATOM   5974  C  C   . MET B 1 164 ? 25.046  1.926   18.903  1.00 12.46 ? 156  MET B C   1 
ATOM   5975  O  O   . MET B 1 164 ? 23.958  1.772   18.336  1.00 12.40 ? 156  MET B O   1 
ATOM   5976  C  CB  . MET B 1 164 ? 26.907  0.406   18.185  1.00 11.78 ? 156  MET B CB  1 
ATOM   5977  C  CG  . MET B 1 164 ? 27.792  0.085   16.974  1.00 16.43 ? 156  MET B CG  1 
ATOM   5978  S  SD  . MET B 1 164 ? 28.414  -1.600  17.003  1.00 13.10 ? 156  MET B SD  1 
ATOM   5979  C  CE  . MET B 1 164 ? 30.037  -1.313  17.722  1.00 15.17 ? 156  MET B CE  1 
ATOM   5980  N  N   . GLU B 1 165 ? 25.144  2.199   20.203  1.00 12.00 ? 157  GLU B N   1 
ATOM   5981  C  CA  . GLU B 1 165 ? 23.975  2.251   21.079  1.00 10.38 ? 157  GLU B CA  1 
ATOM   5982  C  C   . GLU B 1 165 ? 22.995  3.345   20.659  1.00 10.29 ? 157  GLU B C   1 
ATOM   5983  O  O   . GLU B 1 165 ? 23.384  4.479   20.363  1.00 12.96 ? 157  GLU B O   1 
ATOM   5984  C  CB  . GLU B 1 165 ? 24.411  2.502   22.527  1.00 10.78 ? 157  GLU B CB  1 
ATOM   5985  C  CG  . GLU B 1 165 ? 25.005  1.291   23.244  1.00 10.11 ? 157  GLU B CG  1 
ATOM   5986  C  CD  . GLU B 1 165 ? 23.989  0.200   23.558  1.00 10.70 ? 157  GLU B CD  1 
ATOM   5987  O  OE1 . GLU B 1 165 ? 22.786  0.371   23.254  1.00 11.27 ? 157  GLU B OE1 1 
ATOM   5988  O  OE2 . GLU B 1 165 ? 24.400  -0.845  24.114  1.00 11.40 ? 157  GLU B OE2 1 
ATOM   5989  N  N   . GLY B 1 166 ? 21.707  3.004   20.676  1.00 10.64 ? 158  GLY B N   1 
ATOM   5990  C  CA  . GLY B 1 166 ? 20.680  3.978   20.325  1.00 11.10 ? 158  GLY B CA  1 
ATOM   5991  C  C   . GLY B 1 166 ? 20.663  5.215   21.209  1.00 10.03 ? 158  GLY B C   1 
ATOM   5992  O  O   . GLY B 1 166 ? 20.358  6.311   20.735  1.00 11.43 ? 158  GLY B O   1 
ATOM   5993  N  N   . VAL B 1 167 ? 21.018  5.078   22.492  1.00 9.73  ? 159  VAL B N   1 
ATOM   5994  C  CA  . VAL B 1 167 ? 20.964  6.263   23.351  1.00 10.18 ? 159  VAL B CA  1 
ATOM   5995  C  C   . VAL B 1 167 ? 21.960  7.329   22.892  1.00 12.24 ? 159  VAL B C   1 
ATOM   5996  O  O   . VAL B 1 167 ? 21.741  8.522   23.127  1.00 10.79 ? 159  VAL B O   1 
ATOM   5997  C  CB  . VAL B 1 167 ? 21.165  5.875   24.835  1.00 11.05 ? 159  VAL B CB  1 
ATOM   5998  C  CG1 . VAL B 1 167 ? 22.589  5.408   25.099  1.00 11.75 ? 159  VAL B CG1 1 
ATOM   5999  C  CG2 . VAL B 1 167 ? 20.787  7.032   25.761  1.00 10.64 ? 159  VAL B CG2 1 
ATOM   6000  N  N   . SER B 1 168 ? 23.038  6.938   22.197  1.00 9.56  ? 160  SER B N   1 
ATOM   6001  C  CA  . SER B 1 168 ? 23.947  7.946   21.646  1.00 13.20 ? 160  SER B CA  1 
ATOM   6002  C  C   . SER B 1 168 ? 23.282  8.720   20.517  1.00 14.93 ? 160  SER B C   1 
ATOM   6003  O  O   . SER B 1 168 ? 23.478  9.934   20.388  1.00 11.33 ? 160  SER B O   1 
ATOM   6004  C  CB  . SER B 1 168 ? 25.256  7.311   21.151  1.00 13.90 ? 160  SER B CB  1 
ATOM   6005  O  OG  . SER B 1 168 ? 25.124  6.680   19.888  1.00 14.17 ? 160  SER B OG  1 
ATOM   6006  N  N   . HIS B 1 169 ? 22.497  8.031   19.688  1.00 11.33 ? 161  HIS B N   1 
ATOM   6007  C  CA  . HIS B 1 169 ? 21.729  8.716   18.658  1.00 12.87 ? 161  HIS B CA  1 
ATOM   6008  C  C   . HIS B 1 169 ? 20.794  9.746   19.280  1.00 13.89 ? 161  HIS B C   1 
ATOM   6009  O  O   . HIS B 1 169 ? 20.718  10.893  18.818  1.00 12.73 ? 161  HIS B O   1 
ATOM   6010  C  CB  . HIS B 1 169 ? 20.947  7.687   17.837  1.00 10.79 ? 161  HIS B CB  1 
ATOM   6011  C  CG  . HIS B 1 169 ? 19.856  8.279   17.005  1.00 11.14 ? 161  HIS B CG  1 
ATOM   6012  N  ND1 . HIS B 1 169 ? 20.106  9.134   15.954  1.00 13.49 ? 161  HIS B ND1 1 
ATOM   6013  C  CD2 . HIS B 1 169 ? 18.507  8.151   17.080  1.00 11.27 ? 161  HIS B CD2 1 
ATOM   6014  C  CE1 . HIS B 1 169 ? 18.959  9.500   15.407  1.00 16.77 ? 161  HIS B CE1 1 
ATOM   6015  N  NE2 . HIS B 1 169 ? 17.973  8.914   16.068  1.00 11.69 ? 161  HIS B NE2 1 
ATOM   6016  N  N   . GLU B 1 170 ? 20.105  9.369   20.355  1.00 10.16 ? 162  GLU B N   1 
ATOM   6017  C  CA  . GLU B 1 170 ? 19.129  10.275  20.958  1.00 13.55 ? 162  GLU B CA  1 
ATOM   6018  C  C   . GLU B 1 170 ? 19.809  11.507  21.550  1.00 10.38 ? 162  GLU B C   1 
ATOM   6019  O  O   . GLU B 1 170 ? 19.401  12.645  21.290  1.00 11.14 ? 162  GLU B O   1 
ATOM   6020  C  CB  . GLU B 1 170 ? 18.323  9.520   22.019  1.00 10.01 ? 162  GLU B CB  1 
ATOM   6021  C  CG  . GLU B 1 170 ? 17.517  8.339   21.444  1.00 10.24 ? 162  GLU B CG  1 
ATOM   6022  C  CD  . GLU B 1 170 ? 16.694  7.639   22.517  1.00 11.65 ? 162  GLU B CD  1 
ATOM   6023  O  OE1 . GLU B 1 170 ? 16.536  8.227   23.607  1.00 11.26 ? 162  GLU B OE1 1 
ATOM   6024  O  OE2 . GLU B 1 170 ? 16.218  6.516   22.281  1.00 14.34 ? 162  GLU B OE2 1 
ATOM   6025  N  N   . ALA B 1 171 ? 20.876  11.303  22.315  1.00 9.78  ? 163  ALA B N   1 
ATOM   6026  C  CA  . ALA B 1 171 ? 21.475  12.417  23.040  1.00 11.20 ? 163  ALA B CA  1 
ATOM   6027  C  C   . ALA B 1 171 ? 22.255  13.333  22.107  1.00 12.86 ? 163  ALA B C   1 
ATOM   6028  O  O   . ALA B 1 171 ? 22.238  14.558  22.276  1.00 10.27 ? 163  ALA B O   1 
ATOM   6029  C  CB  . ALA B 1 171 ? 22.371  11.888  24.164  1.00 13.87 ? 163  ALA B CB  1 
ATOM   6030  N  N   . CYS B 1 172 ? 22.944  12.764  21.118  1.00 12.93 ? 164  CYS B N   1 
ATOM   6031  C  CA  . CYS B 1 172 ? 23.709  13.595  20.200  1.00 10.51 ? 164  CYS B CA  1 
ATOM   6032  C  C   . CYS B 1 172 ? 22.799  14.333  19.231  1.00 11.48 ? 164  CYS B C   1 
ATOM   6033  O  O   . CYS B 1 172 ? 23.129  15.446  18.806  1.00 13.87 ? 164  CYS B O   1 
ATOM   6034  C  CB  . CYS B 1 172 ? 24.741  12.746  19.449  1.00 11.26 ? 164  CYS B CB  1 
ATOM   6035  S  SG  . CYS B 1 172 ? 26.034  12.134  20.582  1.00 14.04 ? 164  CYS B SG  1 
ATOM   6036  N  N   . SER B 1 173 ? 21.671  13.723  18.854  1.00 10.94 ? 165  SER B N   1 
ATOM   6037  C  CA  . SER B 1 173 ? 20.690  14.431  18.036  1.00 14.17 ? 165  SER B CA  1 
ATOM   6038  C  C   . SER B 1 173 ? 20.197  15.680  18.758  1.00 15.37 ? 165  SER B C   1 
ATOM   6039  O  O   . SER B 1 173 ? 20.164  16.775  18.185  1.00 15.18 ? 165  SER B O   1 
ATOM   6040  C  CB  . SER B 1 173 ? 19.524  13.501  17.684  1.00 15.14 ? 165  SER B CB  1 
ATOM   6041  O  OG  . SER B 1 173 ? 18.454  14.210  17.059  1.00 19.02 ? 165  SER B OG  1 
ATOM   6042  N  N   . LEU B 1 174 ? 19.848  15.533  20.038  1.00 13.25 ? 166  LEU B N   1 
ATOM   6043  C  CA  . LEU B 1 174 ? 19.366  16.668  20.818  1.00 14.37 ? 166  LEU B CA  1 
ATOM   6044  C  C   . LEU B 1 174 ? 20.479  17.683  21.056  1.00 13.26 ? 166  LEU B C   1 
ATOM   6045  O  O   . LEU B 1 174 ? 20.237  18.893  21.043  1.00 14.50 ? 166  LEU B O   1 
ATOM   6046  C  CB  . LEU B 1 174 ? 18.780  16.160  22.139  1.00 13.90 ? 166  LEU B CB  1 
ATOM   6047  C  CG  . LEU B 1 174 ? 17.878  17.048  22.976  1.00 28.86 ? 166  LEU B CG  1 
ATOM   6048  C  CD1 . LEU B 1 174 ? 16.827  17.693  22.114  1.00 21.58 ? 166  LEU B CD1 1 
ATOM   6049  C  CD2 . LEU B 1 174 ? 17.244  16.189  24.069  1.00 31.39 ? 166  LEU B CD2 1 
ATOM   6050  N  N   . ALA B 1 175 ? 21.705  17.214  21.266  1.00 13.92 ? 167  ALA B N   1 
ATOM   6051  C  CA  . ALA B 1 175 ? 22.800  18.145  21.482  1.00 14.28 ? 167  ALA B CA  1 
ATOM   6052  C  C   . ALA B 1 175 ? 23.016  19.017  20.257  1.00 12.83 ? 167  ALA B C   1 
ATOM   6053  O  O   . ALA B 1 175 ? 23.336  20.202  20.391  1.00 17.21 ? 167  ALA B O   1 
ATOM   6054  C  CB  . ALA B 1 175 ? 24.079  17.386  21.838  1.00 11.29 ? 167  ALA B CB  1 
ATOM   6055  N  N   . GLY B 1 176 ? 22.812  18.452  19.063  1.00 12.09 ? 168  GLY B N   1 
ATOM   6056  C  CA  . GLY B 1 176 ? 22.954  19.238  17.845  1.00 12.73 ? 168  GLY B CA  1 
ATOM   6057  C  C   . GLY B 1 176 ? 21.841  20.256  17.680  1.00 16.24 ? 168  GLY B C   1 
ATOM   6058  O  O   . GLY B 1 176 ? 22.077  21.380  17.222  1.00 16.13 ? 168  GLY B O   1 
ATOM   6059  N  N   . THR B 1 177 ? 20.610  19.873  18.034  1.00 13.76 ? 169  THR B N   1 
ATOM   6060  C  CA  A THR B 1 177 ? 19.486  20.804  17.974  0.68 15.48 ? 169  THR B CA  1 
ATOM   6061  C  CA  B THR B 1 177 ? 19.501  20.820  17.956  0.32 15.60 ? 169  THR B CA  1 
ATOM   6062  C  C   . THR B 1 177 ? 19.704  21.990  18.910  1.00 13.74 ? 169  THR B C   1 
ATOM   6063  O  O   . THR B 1 177 ? 19.379  23.135  18.572  1.00 19.30 ? 169  THR B O   1 
ATOM   6064  C  CB  A THR B 1 177 ? 18.189  20.063  18.323  0.68 15.43 ? 169  THR B CB  1 
ATOM   6065  C  CB  B THR B 1 177 ? 18.170  20.127  18.253  0.32 16.16 ? 169  THR B CB  1 
ATOM   6066  O  OG1 A THR B 1 177 ? 17.869  19.137  17.274  0.68 17.39 ? 169  THR B OG1 1 
ATOM   6067  O  OG1 B THR B 1 177 ? 18.178  19.609  19.584  0.32 12.75 ? 169  THR B OG1 1 
ATOM   6068  C  CG2 A THR B 1 177 ? 17.025  21.036  18.513  0.68 18.49 ? 169  THR B CG2 1 
ATOM   6069  C  CG2 B THR B 1 177 ? 17.946  18.993  17.309  0.32 16.62 ? 169  THR B CG2 1 
ATOM   6070  N  N   . LEU B 1 178 ? 20.245  21.731  20.092  1.00 13.26 ? 170  LEU B N   1 
ATOM   6071  C  CA  . LEU B 1 178 ? 20.426  22.758  21.108  1.00 13.49 ? 170  LEU B CA  1 
ATOM   6072  C  C   . LEU B 1 178 ? 21.752  23.504  20.991  1.00 21.19 ? 170  LEU B C   1 
ATOM   6073  O  O   . LEU B 1 178 ? 22.017  24.389  21.811  1.00 18.44 ? 170  LEU B O   1 
ATOM   6074  C  CB  . LEU B 1 178 ? 20.288  22.130  22.504  1.00 15.84 ? 170  LEU B CB  1 
ATOM   6075  C  CG  . LEU B 1 178 ? 18.878  21.586  22.768  1.00 19.60 ? 170  LEU B CG  1 
ATOM   6076  C  CD1 . LEU B 1 178 ? 18.838  20.744  24.026  1.00 24.85 ? 170  LEU B CD1 1 
ATOM   6077  C  CD2 . LEU B 1 178 ? 17.851  22.721  22.836  1.00 24.77 ? 170  LEU B CD2 1 
ATOM   6078  N  N   . GLY B 1 179 ? 22.575  23.192  19.989  1.00 15.89 ? 171  GLY B N   1 
ATOM   6079  C  CA  . GLY B 1 179 ? 23.762  23.986  19.734  1.00 15.15 ? 171  GLY B CA  1 
ATOM   6080  C  C   . GLY B 1 179 ? 24.729  24.073  20.899  1.00 18.31 ? 171  GLY B C   1 
ATOM   6081  O  O   . GLY B 1 179 ? 25.193  25.167  21.247  1.00 17.44 ? 171  GLY B O   1 
ATOM   6082  N  N   . LEU B 1 180 ? 25.049  22.925  21.502  1.00 15.97 ? 172  LEU B N   1 
ATOM   6083  C  CA  . LEU B 1 180 ? 25.933  22.868  22.670  1.00 13.16 ? 172  LEU B CA  1 
ATOM   6084  C  C   . LEU B 1 180 ? 27.383  22.927  22.200  1.00 13.42 ? 172  LEU B C   1 
ATOM   6085  O  O   . LEU B 1 180 ? 28.083  21.916  22.127  1.00 13.04 ? 172  LEU B O   1 
ATOM   6086  C  CB  . LEU B 1 180 ? 25.676  21.605  23.480  1.00 14.86 ? 172  LEU B CB  1 
ATOM   6087  C  CG  . LEU B 1 180 ? 24.227  21.367  23.916  1.00 17.73 ? 172  LEU B CG  1 
ATOM   6088  C  CD1 . LEU B 1 180 ? 24.112  20.061  24.715  1.00 12.69 ? 172  LEU B CD1 1 
ATOM   6089  C  CD2 . LEU B 1 180 ? 23.737  22.557  24.739  1.00 22.36 ? 172  LEU B CD2 1 
ATOM   6090  N  N   . GLY B 1 181 ? 27.834  24.141  21.889  1.00 15.06 ? 173  GLY B N   1 
ATOM   6091  C  CA  . GLY B 1 181 ? 29.185  24.382  21.382  1.00 21.22 ? 173  GLY B CA  1 
ATOM   6092  C  C   . GLY B 1 181 ? 30.307  24.122  22.371  1.00 19.87 ? 173  GLY B C   1 
ATOM   6093  O  O   . GLY B 1 181 ? 31.471  24.072  21.956  1.00 17.40 ? 173  GLY B O   1 
ATOM   6094  N  N   . LYS B 1 182 ? 30.001  23.955  23.653  1.00 16.89 ? 174  LYS B N   1 
ATOM   6095  C  CA  . LYS B 1 182 ? 31.034  23.654  24.635  1.00 18.85 ? 174  LYS B CA  1 
ATOM   6096  C  C   . LYS B 1 182 ? 31.170  22.162  24.896  1.00 17.59 ? 174  LYS B C   1 
ATOM   6097  O  O   . LYS B 1 182 ? 31.957  21.759  25.759  1.00 18.93 ? 174  LYS B O   1 
ATOM   6098  C  CB  . LYS B 1 182 ? 30.747  24.404  25.933  1.00 15.15 ? 174  LYS B CB  1 
ATOM   6099  C  CG  . LYS B 1 182 ? 30.954  25.905  25.800  1.00 23.78 ? 174  LYS B CG  1 
ATOM   6100  C  CD  . LYS B 1 182 ? 30.501  26.612  27.060  1.00 31.35 ? 174  LYS B CD  1 
ATOM   6101  C  CE  . LYS B 1 182 ? 31.143  27.969  27.191  1.00 31.17 ? 174  LYS B CE  1 
ATOM   6102  N  NZ  . LYS B 1 182 ? 30.694  28.664  28.425  1.00 34.12 ? 174  LYS B NZ  1 
ATOM   6103  N  N   . LEU B 1 183 ? 30.428  21.343  24.167  1.00 15.23 ? 175  LEU B N   1 
ATOM   6104  C  CA  . LEU B 1 183 ? 30.531  19.897  24.243  1.00 12.14 ? 175  LEU B CA  1 
ATOM   6105  C  C   . LEU B 1 183 ? 31.492  19.444  23.156  1.00 17.87 ? 175  LEU B C   1 
ATOM   6106  O  O   . LEU B 1 183 ? 31.293  19.766  21.982  1.00 17.51 ? 175  LEU B O   1 
ATOM   6107  C  CB  . LEU B 1 183 ? 29.157  19.255  24.057  1.00 15.40 ? 175  LEU B CB  1 
ATOM   6108  C  CG  . LEU B 1 183 ? 29.067  17.736  24.059  1.00 16.69 ? 175  LEU B CG  1 
ATOM   6109  C  CD1 . LEU B 1 183 ? 29.429  17.171  25.451  1.00 17.06 ? 175  LEU B CD1 1 
ATOM   6110  C  CD2 . LEU B 1 183 ? 27.647  17.308  23.615  1.00 14.36 ? 175  LEU B CD2 1 
ATOM   6111  N  N   . ILE B 1 184 ? 32.543  18.729  23.547  1.00 15.62 ? 176  ILE B N   1 
ATOM   6112  C  CA  . ILE B 1 184 ? 33.598  18.343  22.617  1.00 12.63 ? 176  ILE B CA  1 
ATOM   6113  C  C   . ILE B 1 184 ? 33.937  16.887  22.885  1.00 20.73 ? 176  ILE B C   1 
ATOM   6114  O  O   . ILE B 1 184 ? 34.375  16.537  23.990  1.00 15.99 ? 176  ILE B O   1 
ATOM   6115  C  CB  . ILE B 1 184 ? 34.846  19.233  22.739  1.00 15.61 ? 176  ILE B CB  1 
ATOM   6116  C  CG1 . ILE B 1 184 ? 34.517  20.672  22.314  1.00 16.35 ? 176  ILE B CG1 1 
ATOM   6117  C  CG2 . ILE B 1 184 ? 35.978  18.691  21.861  1.00 17.47 ? 176  ILE B CG2 1 
ATOM   6118  C  CD1 . ILE B 1 184 ? 35.654  21.653  22.554  1.00 19.13 ? 176  ILE B CD1 1 
ATOM   6119  N  N   . VAL B 1 185 ? 33.723  16.042  21.883  1.00 13.74 ? 177  VAL B N   1 
ATOM   6120  C  CA  . VAL B 1 185 ? 33.875  14.599  22.004  1.00 14.49 ? 177  VAL B CA  1 
ATOM   6121  C  C   . VAL B 1 185 ? 35.117  14.173  21.236  1.00 14.53 ? 177  VAL B C   1 
ATOM   6122  O  O   . VAL B 1 185 ? 35.304  14.572  20.079  1.00 13.36 ? 177  VAL B O   1 
ATOM   6123  C  CB  . VAL B 1 185 ? 32.620  13.878  21.483  1.00 15.17 ? 177  VAL B CB  1 
ATOM   6124  C  CG1 . VAL B 1 185 ? 32.814  12.375  21.492  1.00 15.74 ? 177  VAL B CG1 1 
ATOM   6125  C  CG2 . VAL B 1 185 ? 31.402  14.303  22.292  1.00 13.94 ? 177  VAL B CG2 1 
ATOM   6126  N  N   . LEU B 1 186 ? 35.986  13.391  21.889  1.00 15.48 ? 178  LEU B N   1 
ATOM   6127  C  CA  . LEU B 1 186 ? 37.051  12.671  21.196  1.00 14.68 ? 178  LEU B CA  1 
ATOM   6128  C  C   . LEU B 1 186 ? 36.623  11.214  21.089  1.00 17.07 ? 178  LEU B C   1 
ATOM   6129  O  O   . LEU B 1 186 ? 36.424  10.543  22.107  1.00 18.50 ? 178  LEU B O   1 
ATOM   6130  C  CB  . LEU B 1 186 ? 38.404  12.790  21.908  1.00 13.82 ? 178  LEU B CB  1 
ATOM   6131  C  CG  . LEU B 1 186 ? 39.146  14.129  21.775  1.00 14.10 ? 178  LEU B CG  1 
ATOM   6132  C  CD1 . LEU B 1 186 ? 38.497  15.222  22.614  1.00 20.30 ? 178  LEU B CD1 1 
ATOM   6133  C  CD2 . LEU B 1 186 ? 40.639  13.976  22.126  1.00 17.96 ? 178  LEU B CD2 1 
ATOM   6134  N  N   . TYR B 1 187 ? 36.465  10.746  19.858  1.00 14.76 ? 179  TYR B N   1 
ATOM   6135  C  CA  . TYR B 1 187 ? 36.007  9.397   19.552  1.00 15.32 ? 179  TYR B CA  1 
ATOM   6136  C  C   . TYR B 1 187 ? 37.215  8.497   19.301  1.00 13.55 ? 179  TYR B C   1 
ATOM   6137  O  O   . TYR B 1 187 ? 38.012  8.760   18.393  1.00 15.21 ? 179  TYR B O   1 
ATOM   6138  C  CB  . TYR B 1 187 ? 35.079  9.447   18.335  1.00 17.22 ? 179  TYR B CB  1 
ATOM   6139  C  CG  . TYR B 1 187 ? 34.861  8.164   17.558  1.00 12.68 ? 179  TYR B CG  1 
ATOM   6140  C  CD1 . TYR B 1 187 ? 34.739  6.930   18.195  1.00 16.03 ? 179  TYR B CD1 1 
ATOM   6141  C  CD2 . TYR B 1 187 ? 34.721  8.204   16.173  1.00 13.14 ? 179  TYR B CD2 1 
ATOM   6142  C  CE1 . TYR B 1 187 ? 34.513  5.767   17.458  1.00 16.32 ? 179  TYR B CE1 1 
ATOM   6143  C  CE2 . TYR B 1 187 ? 34.490  7.059   15.438  1.00 14.25 ? 179  TYR B CE2 1 
ATOM   6144  C  CZ  . TYR B 1 187 ? 34.381  5.848   16.077  1.00 17.34 ? 179  TYR B CZ  1 
ATOM   6145  O  OH  . TYR B 1 187 ? 34.156  4.712   15.330  1.00 16.87 ? 179  TYR B OH  1 
ATOM   6146  N  N   . ASP B 1 188 ? 37.338  7.448   20.111  1.00 15.04 ? 180  ASP B N   1 
ATOM   6147  C  CA  . ASP B 1 188 ? 38.374  6.419   19.997  1.00 13.26 ? 180  ASP B CA  1 
ATOM   6148  C  C   . ASP B 1 188 ? 38.013  5.492   18.840  1.00 14.50 ? 180  ASP B C   1 
ATOM   6149  O  O   . ASP B 1 188 ? 37.373  4.456   19.016  1.00 17.82 ? 180  ASP B O   1 
ATOM   6150  C  CB  . ASP B 1 188 ? 38.493  5.641   21.307  1.00 12.98 ? 180  ASP B CB  1 
ATOM   6151  C  CG  . ASP B 1 188 ? 39.700  4.724   21.320  1.00 22.37 ? 180  ASP B CG  1 
ATOM   6152  O  OD1 . ASP B 1 188 ? 40.665  5.058   20.612  1.00 26.26 ? 180  ASP B OD1 1 
ATOM   6153  O  OD2 . ASP B 1 188 ? 39.682  3.684   22.014  1.00 20.24 ? 180  ASP B OD2 1 
ATOM   6154  N  N   . ASP B 1 189 ? 38.433  5.868   17.635  1.00 16.14 ? 181  ASP B N   1 
ATOM   6155  C  CA  . ASP B 1 189 ? 38.056  5.166   16.408  1.00 15.45 ? 181  ASP B CA  1 
ATOM   6156  C  C   . ASP B 1 189 ? 39.121  4.108   16.108  1.00 15.15 ? 181  ASP B C   1 
ATOM   6157  O  O   . ASP B 1 189 ? 40.076  4.349   15.368  1.00 18.48 ? 181  ASP B O   1 
ATOM   6158  C  CB  . ASP B 1 189 ? 37.915  6.189   15.285  1.00 19.22 ? 181  ASP B CB  1 
ATOM   6159  C  CG  . ASP B 1 189 ? 37.478  5.582   13.965  1.00 22.41 ? 181  ASP B CG  1 
ATOM   6160  O  OD1 . ASP B 1 189 ? 37.396  4.343   13.854  1.00 20.63 ? 181  ASP B OD1 1 
ATOM   6161  O  OD2 . ASP B 1 189 ? 37.229  6.372   13.026  1.00 24.91 ? 181  ASP B OD2 1 
ATOM   6162  N  N   . ASN B 1 190 ? 38.969  2.909   16.686  1.00 15.05 ? 182  ASN B N   1 
ATOM   6163  C  CA  . ASN B 1 190 ? 40.051  1.929   16.632  1.00 15.75 ? 182  ASN B CA  1 
ATOM   6164  C  C   . ASN B 1 190 ? 39.699  0.638   15.901  1.00 21.41 ? 182  ASN B C   1 
ATOM   6165  O  O   . ASN B 1 190 ? 40.491  -0.314  15.949  1.00 23.49 ? 182  ASN B O   1 
ATOM   6166  C  CB  . ASN B 1 190 ? 40.560  1.607   18.045  1.00 15.54 ? 182  ASN B CB  1 
ATOM   6167  C  CG  . ASN B 1 190 ? 39.527  0.921   18.912  1.00 20.99 ? 182  ASN B CG  1 
ATOM   6168  O  OD1 . ASN B 1 190 ? 38.481  0.498   18.431  1.00 19.09 ? 182  ASN B OD1 1 
ATOM   6169  N  ND2 . ASN B 1 190 ? 39.821  0.803   20.208  1.00 17.81 ? 182  ASN B ND2 1 
ATOM   6170  N  N   . ASN B 1 191 ? 38.536  0.565   15.246  1.00 19.18 ? 183  ASN B N   1 
ATOM   6171  C  CA  . ASN B 1 191 ? 38.177  -0.520  14.334  1.00 19.48 ? 183  ASN B CA  1 
ATOM   6172  C  C   . ASN B 1 191 ? 37.958  -1.857  15.039  1.00 20.54 ? 183  ASN B C   1 
ATOM   6173  O  O   . ASN B 1 191 ? 37.902  -2.902  14.379  1.00 23.39 ? 183  ASN B O   1 
ATOM   6174  C  CB  . ASN B 1 191 ? 39.241  -0.682  13.238  1.00 24.96 ? 183  ASN B CB  1 
ATOM   6175  C  CG  . ASN B 1 191 ? 38.754  -1.503  12.062  1.00 34.84 ? 183  ASN B CG  1 
ATOM   6176  O  OD1 . ASN B 1 191 ? 37.644  -1.300  11.570  1.00 31.65 ? 183  ASN B OD1 1 
ATOM   6177  N  ND2 . ASN B 1 191 ? 39.583  -2.444  11.609  1.00 38.12 ? 183  ASN B ND2 1 
ATOM   6178  N  N   . ILE B 1 192 ? 37.807  -1.860  16.364  1.00 23.08 ? 184  ILE B N   1 
ATOM   6179  C  CA  . ILE B 1 192 ? 37.752  -3.088  17.147  1.00 27.53 ? 184  ILE B CA  1 
ATOM   6180  C  C   . ILE B 1 192 ? 36.582  -3.017  18.119  1.00 23.85 ? 184  ILE B C   1 
ATOM   6181  O  O   . ILE B 1 192 ? 36.357  -1.981  18.751  1.00 21.51 ? 184  ILE B O   1 
ATOM   6182  C  CB  . ILE B 1 192 ? 39.074  -3.315  17.914  1.00 27.17 ? 184  ILE B CB  1 
ATOM   6183  C  CG1 . ILE B 1 192 ? 40.179  -3.792  16.963  1.00 27.15 ? 184  ILE B CG1 1 
ATOM   6184  C  CG2 . ILE B 1 192 ? 38.873  -4.291  19.055  1.00 31.37 ? 184  ILE B CG2 1 
ATOM   6185  C  CD1 . ILE B 1 192 ? 39.897  -5.147  16.324  1.00 32.29 ? 184  ILE B CD1 1 
ATOM   6186  N  N   . SER B 1 193 ? 35.830  -4.115  18.234  1.00 21.02 ? 185  SER B N   1 
ATOM   6187  C  CA  . SER B 1 193 ? 34.952  -4.275  19.390  1.00 24.83 ? 185  SER B CA  1 
ATOM   6188  C  C   . SER B 1 193 ? 35.144  -5.674  19.975  1.00 28.39 ? 185  SER B C   1 
ATOM   6189  O  O   . SER B 1 193 ? 36.079  -6.386  19.586  1.00 25.54 ? 185  SER B O   1 
ATOM   6190  C  CB  . SER B 1 193 ? 33.484  -3.975  19.031  1.00 25.12 ? 185  SER B CB  1 
ATOM   6191  O  OG  . SER B 1 193 ? 32.877  -4.992  18.259  1.00 24.87 ? 185  SER B OG  1 
ATOM   6192  N  N   . ILE B 1 194 ? 34.298  -6.070  20.932  1.00 26.09 ? 186  ILE B N   1 
ATOM   6193  C  CA  . ILE B 1 194 ? 34.545  -7.317  21.658  1.00 23.89 ? 186  ILE B CA  1 
ATOM   6194  C  C   . ILE B 1 194 ? 34.535  -8.510  20.712  1.00 20.91 ? 186  ILE B C   1 
ATOM   6195  O  O   . ILE B 1 194 ? 35.319  -9.451  20.870  1.00 23.83 ? 186  ILE B O   1 
ATOM   6196  C  CB  . ILE B 1 194 ? 33.522  -7.493  22.796  1.00 25.91 ? 186  ILE B CB  1 
ATOM   6197  C  CG1 . ILE B 1 194 ? 33.702  -6.401  23.855  1.00 28.55 ? 186  ILE B CG1 1 
ATOM   6198  C  CG2 . ILE B 1 194 ? 33.629  -8.879  23.412  1.00 23.97 ? 186  ILE B CG2 1 
ATOM   6199  C  CD1 . ILE B 1 194 ? 32.826  -6.599  25.084  1.00 29.76 ? 186  ILE B CD1 1 
ATOM   6200  N  N   . ASP B 1 195 ? 33.664  -8.485  19.705  1.00 20.45 ? 187  ASP B N   1 
ATOM   6201  C  CA  . ASP B 1 195 ? 33.541  -9.615  18.796  1.00 23.65 ? 187  ASP B CA  1 
ATOM   6202  C  C   . ASP B 1 195 ? 34.653  -9.672  17.754  1.00 21.20 ? 187  ASP B C   1 
ATOM   6203  O  O   . ASP B 1 195 ? 34.798  -10.707 17.099  1.00 23.79 ? 187  ASP B O   1 
ATOM   6204  C  CB  . ASP B 1 195 ? 32.173  -9.576  18.097  1.00 25.26 ? 187  ASP B CB  1 
ATOM   6205  C  CG  . ASP B 1 195 ? 31.067  -10.252 18.918  1.00 27.95 ? 187  ASP B CG  1 
ATOM   6206  O  OD1 . ASP B 1 195 ? 31.247  -10.428 20.143  1.00 25.17 ? 187  ASP B OD1 1 
ATOM   6207  O  OD2 . ASP B 1 195 ? 30.030  -10.633 18.326  1.00 27.90 ? 187  ASP B OD2 1 
ATOM   6208  N  N   . GLY B 1 196 ? 35.420  -8.594  17.580  1.00 23.78 ? 188  GLY B N   1 
ATOM   6209  C  CA  . GLY B 1 196 ? 36.512  -8.560  16.617  1.00 24.76 ? 188  GLY B CA  1 
ATOM   6210  C  C   . GLY B 1 196 ? 36.593  -7.264  15.832  1.00 27.05 ? 188  GLY B C   1 
ATOM   6211  O  O   . GLY B 1 196 ? 36.224  -6.199  16.340  1.00 24.62 ? 188  GLY B O   1 
ATOM   6212  N  N   . LYS B 1 197 ? 37.082  -7.333  14.590  1.00 27.71 ? 189  LYS B N   1 
ATOM   6213  C  CA  . LYS B 1 197 ? 37.095  -6.152  13.736  1.00 23.36 ? 189  LYS B CA  1 
ATOM   6214  C  C   . LYS B 1 197 ? 35.661  -5.749  13.412  1.00 24.06 ? 189  LYS B C   1 
ATOM   6215  O  O   . LYS B 1 197 ? 34.845  -6.588  13.013  1.00 24.43 ? 189  LYS B O   1 
ATOM   6216  C  CB  . LYS B 1 197 ? 37.889  -6.423  12.456  1.00 27.71 ? 189  LYS B CB  1 
ATOM   6217  N  N   . VAL B 1 198 ? 35.355  -4.459  13.579  1.00 21.46 ? 190  VAL B N   1 
ATOM   6218  C  CA  . VAL B 1 198 ? 33.960  -4.017  13.620  1.00 21.73 ? 190  VAL B CA  1 
ATOM   6219  C  C   . VAL B 1 198 ? 33.257  -4.081  12.273  1.00 18.98 ? 190  VAL B C   1 
ATOM   6220  O  O   . VAL B 1 198 ? 32.028  -4.011  12.235  1.00 19.12 ? 190  VAL B O   1 
ATOM   6221  C  CB  . VAL B 1 198 ? 33.841  -2.574  14.154  1.00 22.50 ? 190  VAL B CB  1 
ATOM   6222  C  CG1 . VAL B 1 198 ? 34.262  -2.495  15.610  1.00 23.86 ? 190  VAL B CG1 1 
ATOM   6223  C  CG2 . VAL B 1 198 ? 34.662  -1.612  13.290  1.00 24.10 ? 190  VAL B CG2 1 
ATOM   6224  N  N   . ASP B 1 199 ? 33.996  -4.227  11.169  1.00 19.68 ? 191  ASP B N   1 
ATOM   6225  C  CA  . ASP B 1 199 ? 33.391  -4.093  9.848   1.00 23.38 ? 191  ASP B CA  1 
ATOM   6226  C  C   . ASP B 1 199 ? 32.326  -5.146  9.571   1.00 23.80 ? 191  ASP B C   1 
ATOM   6227  O  O   . ASP B 1 199 ? 31.518  -4.962  8.655   1.00 27.16 ? 191  ASP B O   1 
ATOM   6228  C  CB  . ASP B 1 199 ? 34.486  -4.144  8.790   1.00 39.69 ? 191  ASP B CB  1 
ATOM   6229  C  CG  . ASP B 1 199 ? 35.608  -3.180  9.097   1.00 51.93 ? 191  ASP B CG  1 
ATOM   6230  O  OD1 . ASP B 1 199 ? 35.433  -1.968  8.845   1.00 54.07 ? 191  ASP B OD1 1 
ATOM   6231  O  OD2 . ASP B 1 199 ? 36.640  -3.625  9.643   1.00 54.71 ? 191  ASP B OD2 1 
ATOM   6232  N  N   . GLY B 1 200 ? 32.296  -6.240  10.331  1.00 20.70 ? 192  GLY B N   1 
ATOM   6233  C  CA  . GLY B 1 200 ? 31.216  -7.201  10.160  1.00 24.18 ? 192  GLY B CA  1 
ATOM   6234  C  C   . GLY B 1 200 ? 29.875  -6.776  10.752  1.00 20.64 ? 192  GLY B C   1 
ATOM   6235  O  O   . GLY B 1 200 ? 28.881  -7.475  10.542  1.00 19.40 ? 192  GLY B O   1 
ATOM   6236  N  N   . TRP B 1 201 ? 29.827  -5.675  11.490  1.00 17.12 ? 193  TRP B N   1 
ATOM   6237  C  CA  . TRP B 1 201 ? 28.578  -5.258  12.122  1.00 16.41 ? 193  TRP B CA  1 
ATOM   6238  C  C   . TRP B 1 201 ? 28.477  -3.755  12.326  1.00 18.78 ? 193  TRP B C   1 
ATOM   6239  O  O   . TRP B 1 201 ? 27.432  -3.292  12.782  1.00 19.11 ? 193  TRP B O   1 
ATOM   6240  C  CB  . TRP B 1 201 ? 28.406  -5.970  13.481  1.00 16.11 ? 193  TRP B CB  1 
ATOM   6241  C  CG  . TRP B 1 201 ? 29.627  -5.870  14.356  1.00 17.06 ? 193  TRP B CG  1 
ATOM   6242  C  CD1 . TRP B 1 201 ? 29.943  -4.860  15.232  1.00 15.36 ? 193  TRP B CD1 1 
ATOM   6243  C  CD2 . TRP B 1 201 ? 30.700  -6.811  14.423  1.00 16.53 ? 193  TRP B CD2 1 
ATOM   6244  N  NE1 . TRP B 1 201 ? 31.150  -5.129  15.845  1.00 17.29 ? 193  TRP B NE1 1 
ATOM   6245  C  CE2 . TRP B 1 201 ? 31.631  -6.322  15.368  1.00 17.94 ? 193  TRP B CE2 1 
ATOM   6246  C  CE3 . TRP B 1 201 ? 30.963  -8.028  13.780  1.00 17.50 ? 193  TRP B CE3 1 
ATOM   6247  C  CZ2 . TRP B 1 201 ? 32.800  -7.008  15.684  1.00 19.19 ? 193  TRP B CZ2 1 
ATOM   6248  C  CZ3 . TRP B 1 201 ? 32.130  -8.706  14.091  1.00 26.50 ? 193  TRP B CZ3 1 
ATOM   6249  C  CH2 . TRP B 1 201 ? 33.033  -8.193  15.034  1.00 21.36 ? 193  TRP B CH2 1 
ATOM   6250  N  N   . PHE B 1 202 ? 29.508  -2.973  12.003  1.00 15.67 ? 194  PHE B N   1 
ATOM   6251  C  CA  . PHE B 1 202 ? 29.492  -1.535  12.276  1.00 16.33 ? 194  PHE B CA  1 
ATOM   6252  C  C   . PHE B 1 202 ? 30.280  -0.854  11.167  1.00 21.85 ? 194  PHE B C   1 
ATOM   6253  O  O   . PHE B 1 202 ? 31.502  -1.002  11.109  1.00 15.84 ? 194  PHE B O   1 
ATOM   6254  C  CB  . PHE B 1 202 ? 30.088  -1.235  13.651  1.00 14.44 ? 194  PHE B CB  1 
ATOM   6255  C  CG  . PHE B 1 202 ? 30.082  0.222   14.029  1.00 16.40 ? 194  PHE B CG  1 
ATOM   6256  C  CD1 . PHE B 1 202 ? 28.913  0.971   13.972  1.00 15.25 ? 194  PHE B CD1 1 
ATOM   6257  C  CD2 . PHE B 1 202 ? 31.249  0.838   14.472  1.00 21.64 ? 194  PHE B CD2 1 
ATOM   6258  C  CE1 . PHE B 1 202 ? 28.902  2.312   14.347  1.00 18.25 ? 194  PHE B CE1 1 
ATOM   6259  C  CE2 . PHE B 1 202 ? 31.251  2.182   14.845  1.00 22.93 ? 194  PHE B CE2 1 
ATOM   6260  C  CZ  . PHE B 1 202 ? 30.075  2.920   14.778  1.00 20.86 ? 194  PHE B CZ  1 
ATOM   6261  N  N   . THR B 1 203 ? 29.572  -0.142  10.273  1.00 15.59 ? 195  THR B N   1 
ATOM   6262  C  CA  . THR B 1 203 ? 30.190  0.507   9.117   1.00 18.67 ? 195  THR B CA  1 
ATOM   6263  C  C   . THR B 1 203 ? 29.677  1.933   8.929   1.00 15.78 ? 195  THR B C   1 
ATOM   6264  O  O   . THR B 1 203 ? 29.744  2.472   7.821   1.00 16.29 ? 195  THR B O   1 
ATOM   6265  C  CB  . THR B 1 203 ? 29.955  -0.309  7.830   1.00 21.48 ? 195  THR B CB  1 
ATOM   6266  O  OG1 . THR B 1 203 ? 28.554  -0.549  7.653   1.00 16.92 ? 195  THR B OG1 1 
ATOM   6267  C  CG2 . THR B 1 203 ? 30.692  -1.657  7.909   1.00 17.55 ? 195  THR B CG2 1 
ATOM   6268  N  N   . GLU B 1 204 ? 29.169  2.554   9.984   1.00 15.01 ? 196  GLU B N   1 
ATOM   6269  C  CA  . GLU B 1 204 ? 28.648  3.906   9.873   1.00 14.75 ? 196  GLU B CA  1 
ATOM   6270  C  C   . GLU B 1 204 ? 29.741  4.878   9.458   1.00 19.25 ? 196  GLU B C   1 
ATOM   6271  O  O   . GLU B 1 204 ? 30.900  4.748   9.862   1.00 16.09 ? 196  GLU B O   1 
ATOM   6272  C  CB  . GLU B 1 204 ? 28.046  4.342   11.209  1.00 13.93 ? 196  GLU B CB  1 
ATOM   6273  C  CG  . GLU B 1 204 ? 26.846  3.518   11.616  1.00 16.82 ? 196  GLU B CG  1 
ATOM   6274  C  CD  . GLU B 1 204 ? 26.264  3.962   12.935  1.00 18.38 ? 196  GLU B CD  1 
ATOM   6275  O  OE1 . GLU B 1 204 ? 26.564  5.102   13.367  1.00 17.71 ? 196  GLU B OE1 1 
ATOM   6276  O  OE2 . GLU B 1 204 ? 25.521  3.164   13.545  1.00 17.62 ? 196  GLU B OE2 1 
ATOM   6277  N  N   . ASN B 1 205 ? 29.361  5.848   8.640   1.00 15.29 ? 197  ASN B N   1 
ATOM   6278  C  CA  . ASN B 1 205 ? 30.204  7.005   8.341   1.00 15.55 ? 197  ASN B CA  1 
ATOM   6279  C  C   . ASN B 1 205 ? 29.952  8.010   9.455   1.00 15.38 ? 197  ASN B C   1 
ATOM   6280  O  O   . ASN B 1 205 ? 29.022  8.818   9.403   1.00 17.38 ? 197  ASN B O   1 
ATOM   6281  C  CB  . ASN B 1 205 ? 29.871  7.570   6.968   1.00 16.22 ? 197  ASN B CB  1 
ATOM   6282  C  CG  . ASN B 1 205 ? 30.801  8.703   6.547   1.00 19.08 ? 197  ASN B CG  1 
ATOM   6283  O  OD1 . ASN B 1 205 ? 31.320  9.446   7.376   1.00 17.17 ? 197  ASN B OD1 1 
ATOM   6284  N  ND2 . ASN B 1 205 ? 31.003  8.838   5.242   1.00 18.38 ? 197  ASN B ND2 1 
ATOM   6285  N  N   . ILE B 1 206 ? 30.767  7.932   10.506  1.00 14.52 ? 198  ILE B N   1 
ATOM   6286  C  CA  . ILE B 1 206 ? 30.503  8.745   11.696  1.00 17.20 ? 198  ILE B CA  1 
ATOM   6287  C  C   . ILE B 1 206 ? 30.543  10.233  11.382  1.00 16.60 ? 198  ILE B C   1 
ATOM   6288  O  O   . ILE B 1 206 ? 29.633  10.957  11.820  1.00 15.71 ? 198  ILE B O   1 
ATOM   6289  C  CB  . ILE B 1 206 ? 31.442  8.327   12.840  1.00 13.57 ? 198  ILE B CB  1 
ATOM   6290  C  CG1 . ILE B 1 206 ? 31.073  6.913   13.303  1.00 13.31 ? 198  ILE B CG1 1 
ATOM   6291  C  CG2 . ILE B 1 206 ? 31.369  9.316   14.010  1.00 13.07 ? 198  ILE B CG2 1 
ATOM   6292  C  CD1 . ILE B 1 206 ? 29.596  6.771   13.756  1.00 12.82 ? 198  ILE B CD1 1 
ATOM   6293  N  N   . PRO B 1 207 ? 31.522  10.763  10.632  1.00 14.73 ? 199  PRO B N   1 
ATOM   6294  C  CA  . PRO B 1 207 ? 31.454  12.191  10.265  1.00 15.05 ? 199  PRO B CA  1 
ATOM   6295  C  C   . PRO B 1 207 ? 30.146  12.592  9.590   1.00 17.34 ? 199  PRO B C   1 
ATOM   6296  O  O   . PRO B 1 207 ? 29.549  13.618  9.956   1.00 16.56 ? 199  PRO B O   1 
ATOM   6297  C  CB  . PRO B 1 207 ? 32.667  12.358  9.339   1.00 16.61 ? 199  PRO B CB  1 
ATOM   6298  C  CG  . PRO B 1 207 ? 33.652  11.340  9.853   1.00 18.09 ? 199  PRO B CG  1 
ATOM   6299  C  CD  . PRO B 1 207 ? 32.808  10.155  10.212  1.00 15.24 ? 199  PRO B CD  1 
ATOM   6300  N  N   . GLN B 1 208 ? 29.664  11.793  8.635   1.00 15.44 ? 200  GLN B N   1 
ATOM   6301  C  CA  . GLN B 1 208 ? 28.414  12.130  7.957   1.00 16.73 ? 200  GLN B CA  1 
ATOM   6302  C  C   . GLN B 1 208 ? 27.223  12.043  8.907   1.00 14.92 ? 200  GLN B C   1 
ATOM   6303  O  O   . GLN B 1 208 ? 26.322  12.893  8.863   1.00 14.96 ? 200  GLN B O   1 
ATOM   6304  C  CB  . GLN B 1 208 ? 28.212  11.214  6.750   1.00 17.64 ? 200  GLN B CB  1 
ATOM   6305  C  CG  . GLN B 1 208 ? 27.087  11.654  5.821   1.00 23.37 ? 200  GLN B CG  1 
ATOM   6306  C  CD  . GLN B 1 208 ? 26.987  10.773  4.595   1.00 25.63 ? 200  GLN B CD  1 
ATOM   6307  O  OE1 . GLN B 1 208 ? 27.245  9.574   4.665   1.00 20.21 ? 200  GLN B OE1 1 
ATOM   6308  N  NE2 . GLN B 1 208 ? 26.631  11.365  3.460   1.00 25.68 ? 200  GLN B NE2 1 
ATOM   6309  N  N   . ARG B 1 209 ? 27.195  11.013  9.758   1.00 14.37 ? 201  ARG B N   1 
ATOM   6310  C  CA  . ARG B 1 209 ? 26.129  10.888  10.742  1.00 14.77 ? 201  ARG B CA  1 
ATOM   6311  C  C   . ARG B 1 209 ? 26.104  12.098  11.664  1.00 17.34 ? 201  ARG B C   1 
ATOM   6312  O  O   . ARG B 1 209 ? 25.038  12.668  11.936  1.00 13.45 ? 201  ARG B O   1 
ATOM   6313  C  CB  . ARG B 1 209 ? 26.312  9.594   11.544  1.00 14.15 ? 201  ARG B CB  1 
ATOM   6314  C  CG  . ARG B 1 209 ? 25.400  9.479   12.763  1.00 12.69 ? 201  ARG B CG  1 
ATOM   6315  C  CD  . ARG B 1 209 ? 25.638  8.180   13.541  1.00 13.65 ? 201  ARG B CD  1 
ATOM   6316  N  NE  . ARG B 1 209 ? 25.010  8.275   14.852  1.00 13.19 ? 201  ARG B NE  1 
ATOM   6317  C  CZ  . ARG B 1 209 ? 25.364  7.558   15.907  1.00 14.58 ? 201  ARG B CZ  1 
ATOM   6318  N  NH1 . ARG B 1 209 ? 26.343  6.660   15.808  1.00 12.85 ? 201  ARG B NH1 1 
ATOM   6319  N  NH2 . ARG B 1 209 ? 24.731  7.744   17.057  1.00 14.78 ? 201  ARG B NH2 1 
ATOM   6320  N  N   . PHE B 1 210 ? 27.271  12.537  12.123  1.00 13.43 ? 202  PHE B N   1 
ATOM   6321  C  CA  . PHE B 1 210 ? 27.255  13.646  13.066  1.00 13.20 ? 202  PHE B CA  1 
ATOM   6322  C  C   . PHE B 1 210 ? 27.027  14.979  12.376  1.00 13.74 ? 202  PHE B C   1 
ATOM   6323  O  O   . PHE B 1 210 ? 26.387  15.863  12.958  1.00 15.52 ? 202  PHE B O   1 
ATOM   6324  C  CB  . PHE B 1 210 ? 28.517  13.612  13.927  1.00 13.01 ? 202  PHE B CB  1 
ATOM   6325  C  CG  . PHE B 1 210 ? 28.350  12.717  15.119  1.00 15.56 ? 202  PHE B CG  1 
ATOM   6326  C  CD1 . PHE B 1 210 ? 28.236  11.343  14.947  1.00 12.24 ? 202  PHE B CD1 1 
ATOM   6327  C  CD2 . PHE B 1 210 ? 28.213  13.241  16.389  1.00 11.96 ? 202  PHE B CD2 1 
ATOM   6328  C  CE1 . PHE B 1 210 ? 28.036  10.508  16.029  1.00 13.77 ? 202  PHE B CE1 1 
ATOM   6329  C  CE2 . PHE B 1 210 ? 28.003  12.417  17.473  1.00 11.43 ? 202  PHE B CE2 1 
ATOM   6330  C  CZ  . PHE B 1 210 ? 27.914  11.052  17.300  1.00 16.79 ? 202  PHE B CZ  1 
ATOM   6331  N  N   . GLU B 1 211 ? 27.467  15.128  11.125  1.00 15.10 ? 203  GLU B N   1 
ATOM   6332  C  CA  . GLU B 1 211 ? 27.012  16.284  10.359  1.00 14.99 ? 203  GLU B CA  1 
ATOM   6333  C  C   . GLU B 1 211 ? 25.496  16.305  10.250  1.00 18.24 ? 203  GLU B C   1 
ATOM   6334  O  O   . GLU B 1 211 ? 24.888  17.383  10.293  1.00 15.24 ? 203  GLU B O   1 
ATOM   6335  C  CB  . GLU B 1 211 ? 27.652  16.301  8.973   1.00 25.44 ? 203  GLU B CB  1 
ATOM   6336  C  CG  . GLU B 1 211 ? 29.155  16.538  9.021   1.00 36.07 ? 203  GLU B CG  1 
ATOM   6337  C  CD  . GLU B 1 211 ? 29.687  17.195  7.765   1.00 46.32 ? 203  GLU B CD  1 
ATOM   6338  O  OE1 . GLU B 1 211 ? 28.941  17.270  6.765   1.00 48.83 ? 203  GLU B OE1 1 
ATOM   6339  O  OE2 . GLU B 1 211 ? 30.851  17.644  7.789   1.00 51.17 ? 203  GLU B OE2 1 
ATOM   6340  N  N   . SER B 1 212 ? 24.859  15.132  10.158  1.00 14.60 ? 204  SER B N   1 
ATOM   6341  C  CA  . SER B 1 212 ? 23.402  15.131  10.038  1.00 14.60 ? 204  SER B CA  1 
ATOM   6342  C  C   . SER B 1 212 ? 22.730  15.582  11.319  1.00 15.99 ? 204  SER B C   1 
ATOM   6343  O  O   . SER B 1 212 ? 21.564  15.977  11.277  1.00 14.24 ? 204  SER B O   1 
ATOM   6344  C  CB  . SER B 1 212 ? 22.862  13.751  9.645   1.00 14.51 ? 204  SER B CB  1 
ATOM   6345  O  OG  . SER B 1 212 ? 22.682  12.892  10.770  1.00 14.69 ? 204  SER B OG  1 
ATOM   6346  N  N   . TYR B 1 213 ? 23.436  15.539  12.447  1.00 13.59 ? 205  TYR B N   1 
ATOM   6347  C  CA  . TYR B 1 213 ? 22.913  16.058  13.700  1.00 15.12 ? 205  TYR B CA  1 
ATOM   6348  C  C   . TYR B 1 213 ? 23.167  17.548  13.865  1.00 15.39 ? 205  TYR B C   1 
ATOM   6349  O  O   . TYR B 1 213 ? 22.739  18.125  14.870  1.00 17.51 ? 205  TYR B O   1 
ATOM   6350  C  CB  . TYR B 1 213 ? 23.548  15.344  14.896  1.00 14.42 ? 205  TYR B CB  1 
ATOM   6351  C  CG  . TYR B 1 213 ? 23.320  13.857  15.036  1.00 13.77 ? 205  TYR B CG  1 
ATOM   6352  C  CD1 . TYR B 1 213 ? 22.140  13.254  14.598  1.00 16.27 ? 205  TYR B CD1 1 
ATOM   6353  C  CD2 . TYR B 1 213 ? 24.287  13.056  15.638  1.00 11.89 ? 205  TYR B CD2 1 
ATOM   6354  C  CE1 . TYR B 1 213 ? 21.933  11.903  14.749  1.00 13.47 ? 205  TYR B CE1 1 
ATOM   6355  C  CE2 . TYR B 1 213 ? 24.095  11.696  15.796  1.00 12.00 ? 205  TYR B CE2 1 
ATOM   6356  C  CZ  . TYR B 1 213 ? 22.913  11.126  15.362  1.00 15.21 ? 205  TYR B CZ  1 
ATOM   6357  O  OH  . TYR B 1 213 ? 22.710  9.781   15.516  1.00 12.86 ? 205  TYR B OH  1 
ATOM   6358  N  N   . GLY B 1 214 ? 23.876  18.176  12.930  1.00 16.53 ? 206  GLY B N   1 
ATOM   6359  C  CA  . GLY B 1 214 ? 24.310  19.544  13.125  1.00 16.49 ? 206  GLY B CA  1 
ATOM   6360  C  C   . GLY B 1 214 ? 25.569  19.710  13.947  1.00 18.74 ? 206  GLY B C   1 
ATOM   6361  O  O   . GLY B 1 214 ? 25.821  20.807  14.448  1.00 16.60 ? 206  GLY B O   1 
ATOM   6362  N  N   . TRP B 1 215 ? 26.384  18.662  14.089  1.00 16.09 ? 207  TRP B N   1 
ATOM   6363  C  CA  . TRP B 1 215 ? 27.648  18.784  14.801  1.00 15.82 ? 207  TRP B CA  1 
ATOM   6364  C  C   . TRP B 1 215 ? 28.756  19.306  13.891  1.00 18.12 ? 207  TRP B C   1 
ATOM   6365  O  O   . TRP B 1 215 ? 28.707  19.187  12.664  1.00 16.51 ? 207  TRP B O   1 
ATOM   6366  C  CB  . TRP B 1 215 ? 28.093  17.437  15.385  1.00 13.31 ? 207  TRP B CB  1 
ATOM   6367  C  CG  . TRP B 1 215 ? 27.326  16.991  16.597  1.00 13.14 ? 207  TRP B CG  1 
ATOM   6368  C  CD1 . TRP B 1 215 ? 25.963  16.970  16.749  1.00 13.18 ? 207  TRP B CD1 1 
ATOM   6369  C  CD2 . TRP B 1 215 ? 27.874  16.441  17.807  1.00 12.14 ? 207  TRP B CD2 1 
ATOM   6370  N  NE1 . TRP B 1 215 ? 25.636  16.462  17.983  1.00 11.87 ? 207  TRP B NE1 1 
ATOM   6371  C  CE2 . TRP B 1 215 ? 26.788  16.145  18.659  1.00 13.04 ? 207  TRP B CE2 1 
ATOM   6372  C  CE3 . TRP B 1 215 ? 29.177  16.214  18.265  1.00 12.13 ? 207  TRP B CE3 1 
ATOM   6373  C  CZ2 . TRP B 1 215 ? 26.963  15.610  19.941  1.00 15.38 ? 207  TRP B CZ2 1 
ATOM   6374  C  CZ3 . TRP B 1 215 ? 29.362  15.681  19.541  1.00 11.87 ? 207  TRP B CZ3 1 
ATOM   6375  C  CH2 . TRP B 1 215 ? 28.256  15.380  20.364  1.00 13.91 ? 207  TRP B CH2 1 
ATOM   6376  N  N   . HIS B 1 216 ? 29.771  19.887  14.526  1.00 14.78 ? 208  HIS B N   1 
ATOM   6377  C  CA  . HIS B 1 216 ? 31.057  20.143  13.889  1.00 21.71 ? 208  HIS B CA  1 
ATOM   6378  C  C   . HIS B 1 216 ? 31.889  18.870  13.982  1.00 17.56 ? 208  HIS B C   1 
ATOM   6379  O  O   . HIS B 1 216 ? 31.898  18.224  15.027  1.00 16.51 ? 208  HIS B O   1 
ATOM   6380  C  CB  . HIS B 1 216 ? 31.741  21.309  14.602  1.00 17.04 ? 208  HIS B CB  1 
ATOM   6381  C  CG  . HIS B 1 216 ? 33.201  21.445  14.321  1.00 19.50 ? 208  HIS B CG  1 
ATOM   6382  N  ND1 . HIS B 1 216 ? 34.163  21.322  15.304  1.00 21.44 ? 208  HIS B ND1 1 
ATOM   6383  C  CD2 . HIS B 1 216 ? 33.863  21.747  13.180  1.00 21.22 ? 208  HIS B CD2 1 
ATOM   6384  C  CE1 . HIS B 1 216 ? 35.356  21.527  14.775  1.00 20.01 ? 208  HIS B CE1 1 
ATOM   6385  N  NE2 . HIS B 1 216 ? 35.203  21.778  13.487  1.00 25.37 ? 208  HIS B NE2 1 
ATOM   6386  N  N   . VAL B 1 217 ? 32.543  18.472  12.888  1.00 19.85 ? 209  VAL B N   1 
ATOM   6387  C  CA  . VAL B 1 217 ? 33.300  17.219  12.849  1.00 19.59 ? 209  VAL B CA  1 
ATOM   6388  C  C   . VAL B 1 217 ? 34.734  17.502  12.427  1.00 19.93 ? 209  VAL B C   1 
ATOM   6389  O  O   . VAL B 1 217 ? 34.973  18.228  11.452  1.00 18.57 ? 209  VAL B O   1 
ATOM   6390  C  CB  . VAL B 1 217 ? 32.674  16.177  11.898  1.00 22.41 ? 209  VAL B CB  1 
ATOM   6391  C  CG1 . VAL B 1 217 ? 33.517  14.879  11.887  1.00 17.83 ? 209  VAL B CG1 1 
ATOM   6392  C  CG2 . VAL B 1 217 ? 31.246  15.868  12.298  1.00 20.84 ? 209  VAL B CG2 1 
ATOM   6393  N  N   . VAL B 1 218 ? 35.682  16.915  13.150  1.00 19.19 ? 210  VAL B N   1 
ATOM   6394  C  CA  . VAL B 1 218 ? 37.071  16.860  12.705  1.00 20.90 ? 210  VAL B CA  1 
ATOM   6395  C  C   . VAL B 1 218 ? 37.384  15.398  12.408  1.00 22.79 ? 210  VAL B C   1 
ATOM   6396  O  O   . VAL B 1 218 ? 37.638  14.612  13.336  1.00 20.75 ? 210  VAL B O   1 
ATOM   6397  C  CB  . VAL B 1 218 ? 38.033  17.457  13.746  1.00 17.96 ? 210  VAL B CB  1 
ATOM   6398  C  CG1 . VAL B 1 218 ? 39.460  17.548  13.168  1.00 17.76 ? 210  VAL B CG1 1 
ATOM   6399  C  CG2 . VAL B 1 218 ? 37.546  18.831  14.178  1.00 22.15 ? 210  VAL B CG2 1 
ATOM   6400  N  N   . PRO B 1 219 ? 37.363  14.992  11.145  1.00 22.34 ? 211  PRO B N   1 
ATOM   6401  C  CA  . PRO B 1 219 ? 37.565  13.583  10.811  1.00 22.47 ? 211  PRO B CA  1 
ATOM   6402  C  C   . PRO B 1 219 ? 39.041  13.225  10.703  1.00 18.62 ? 211  PRO B C   1 
ATOM   6403  O  O   . PRO B 1 219 ? 39.916  14.085  10.580  1.00 20.70 ? 211  PRO B O   1 
ATOM   6404  C  CB  . PRO B 1 219 ? 36.889  13.467  9.441   1.00 21.58 ? 211  PRO B CB  1 
ATOM   6405  C  CG  . PRO B 1 219 ? 37.227  14.793  8.805   1.00 22.15 ? 211  PRO B CG  1 
ATOM   6406  C  CD  . PRO B 1 219 ? 37.199  15.817  9.930   1.00 24.70 ? 211  PRO B CD  1 
ATOM   6407  N  N   . ASN B 1 220 ? 39.302  11.921  10.813  1.00 20.39 ? 212  ASN B N   1 
ATOM   6408  C  CA  A ASN B 1 220 ? 40.578  11.320  10.417  0.68 18.33 ? 212  ASN B CA  1 
ATOM   6409  C  CA  B ASN B 1 220 ? 40.579  11.332  10.401  0.32 23.58 ? 212  ASN B CA  1 
ATOM   6410  C  C   . ASN B 1 220 ? 41.776  11.985  11.095  1.00 20.34 ? 212  ASN B C   1 
ATOM   6411  O  O   . ASN B 1 220 ? 42.778  12.339  10.458  1.00 22.66 ? 212  ASN B O   1 
ATOM   6412  C  CB  A ASN B 1 220 ? 40.726  11.353  8.896   0.68 27.62 ? 212  ASN B CB  1 
ATOM   6413  C  CB  B ASN B 1 220 ? 40.735  11.406  8.878   0.32 27.31 ? 212  ASN B CB  1 
ATOM   6414  C  CG  A ASN B 1 220 ? 41.727  10.341  8.393   0.68 29.51 ? 212  ASN B CG  1 
ATOM   6415  C  CG  B ASN B 1 220 ? 39.645  10.655  8.139   0.32 28.07 ? 212  ASN B CG  1 
ATOM   6416  O  OD1 A ASN B 1 220 ? 41.907  9.282   8.995   0.68 25.79 ? 212  ASN B OD1 1 
ATOM   6417  O  OD1 B ASN B 1 220 ? 39.300  9.530   8.497   0.32 33.28 ? 212  ASN B OD1 1 
ATOM   6418  N  ND2 A ASN B 1 220 ? 42.389  10.661  7.288   0.68 20.97 ? 212  ASN B ND2 1 
ATOM   6419  N  ND2 B ASN B 1 220 ? 39.097  11.276  7.101   0.32 29.02 ? 212  ASN B ND2 1 
ATOM   6420  N  N   . VAL B 1 221 ? 41.690  12.130  12.407  1.00 20.83 ? 213  VAL B N   1 
ATOM   6421  C  CA  . VAL B 1 221 ? 42.813  12.638  13.192  1.00 18.35 ? 213  VAL B CA  1 
ATOM   6422  C  C   . VAL B 1 221 ? 43.685  11.461  13.605  1.00 20.75 ? 213  VAL B C   1 
ATOM   6423  O  O   . VAL B 1 221 ? 43.174  10.433  14.064  1.00 22.13 ? 213  VAL B O   1 
ATOM   6424  C  CB  . VAL B 1 221 ? 42.322  13.411  14.428  1.00 25.52 ? 213  VAL B CB  1 
ATOM   6425  C  CG1 . VAL B 1 221 ? 43.516  13.819  15.308  1.00 22.29 ? 213  VAL B CG1 1 
ATOM   6426  C  CG2 . VAL B 1 221 ? 41.528  14.627  14.006  1.00 22.80 ? 213  VAL B CG2 1 
ATOM   6427  N  N   . ASN B 1 222 ? 45.004  11.599  13.439  1.00 21.54 ? 214  ASN B N   1 
ATOM   6428  C  CA  . ASN B 1 222 ? 45.924  10.601  13.975  1.00 19.65 ? 214  ASN B CA  1 
ATOM   6429  C  C   . ASN B 1 222 ? 45.872  10.654  15.500  1.00 22.18 ? 214  ASN B C   1 
ATOM   6430  O  O   . ASN B 1 222 ? 46.448  11.555  16.116  1.00 19.93 ? 214  ASN B O   1 
ATOM   6431  C  CB  . ASN B 1 222 ? 47.342  10.841  13.464  1.00 22.30 ? 214  ASN B CB  1 
ATOM   6432  C  CG  . ASN B 1 222 ? 48.307  9.724   13.862  1.00 28.06 ? 214  ASN B CG  1 
ATOM   6433  O  OD1 . ASN B 1 222 ? 48.032  8.946   14.780  1.00 21.39 ? 214  ASN B OD1 1 
ATOM   6434  N  ND2 . ASN B 1 222 ? 49.448  9.643   13.165  1.00 27.40 ? 214  ASN B ND2 1 
ATOM   6435  N  N   . GLY B 1 223 ? 45.192  9.682   16.112  1.00 21.70 ? 215  GLY B N   1 
ATOM   6436  C  CA  . GLY B 1 223 ? 45.015  9.647   17.550  1.00 17.54 ? 215  GLY B CA  1 
ATOM   6437  C  C   . GLY B 1 223 ? 46.263  9.367   18.350  1.00 21.64 ? 215  GLY B C   1 
ATOM   6438  O  O   . GLY B 1 223 ? 46.194  9.343   19.583  1.00 18.93 ? 215  GLY B O   1 
ATOM   6439  N  N   . HIS B 1 224 ? 47.403  9.147   17.697  1.00 24.27 ? 216  HIS B N   1 
ATOM   6440  C  CA  . HIS B 1 224 ? 48.667  8.998   18.398  1.00 26.40 ? 216  HIS B CA  1 
ATOM   6441  C  C   . HIS B 1 224 ? 49.614  10.146  18.101  1.00 25.12 ? 216  HIS B C   1 
ATOM   6442  O  O   . HIS B 1 224 ? 50.790  10.071  18.462  1.00 22.00 ? 216  HIS B O   1 
ATOM   6443  C  CB  . HIS B 1 224 ? 49.296  7.641   18.064  1.00 20.22 ? 216  HIS B CB  1 
ATOM   6444  C  CG  . HIS B 1 224 ? 48.420  6.489   18.454  1.00 22.86 ? 216  HIS B CG  1 
ATOM   6445  N  ND1 . HIS B 1 224 ? 47.977  6.305   19.746  1.00 19.98 ? 216  HIS B ND1 1 
ATOM   6446  C  CD2 . HIS B 1 224 ? 47.866  5.496   17.721  1.00 22.14 ? 216  HIS B CD2 1 
ATOM   6447  C  CE1 . HIS B 1 224 ? 47.206  5.233   19.797  1.00 22.65 ? 216  HIS B CE1 1 
ATOM   6448  N  NE2 . HIS B 1 224 ? 47.124  4.722   18.581  1.00 21.23 ? 216  HIS B NE2 1 
ATOM   6449  N  N   . ASP B 1 225 ? 49.111  11.209  17.465  1.00 27.33 ? 217  ASP B N   1 
ATOM   6450  C  CA  . ASP B 1 225 ? 49.872  12.407  17.105  1.00 26.80 ? 217  ASP B CA  1 
ATOM   6451  C  C   . ASP B 1 225 ? 49.337  13.531  17.986  1.00 23.08 ? 217  ASP B C   1 
ATOM   6452  O  O   . ASP B 1 225 ? 48.274  14.091  17.704  1.00 22.51 ? 217  ASP B O   1 
ATOM   6453  C  CB  . ASP B 1 225 ? 49.707  12.715  15.613  1.00 23.12 ? 217  ASP B CB  1 
ATOM   6454  C  CG  . ASP B 1 225 ? 50.460  13.971  15.160  1.00 26.77 ? 217  ASP B CG  1 
ATOM   6455  O  OD1 . ASP B 1 225 ? 51.010  14.699  16.003  1.00 28.98 ? 217  ASP B OD1 1 
ATOM   6456  O  OD2 . ASP B 1 225 ? 50.504  14.229  13.940  1.00 27.03 ? 217  ASP B OD2 1 
ATOM   6457  N  N   . THR B 1 226 ? 50.063  13.856  19.064  1.00 23.21 ? 218  THR B N   1 
ATOM   6458  C  CA  . THR B 1 226 ? 49.544  14.856  19.999  1.00 25.64 ? 218  THR B CA  1 
ATOM   6459  C  C   . THR B 1 226 ? 49.439  16.236  19.353  1.00 30.41 ? 218  THR B C   1 
ATOM   6460  O  O   . THR B 1 226 ? 48.549  17.018  19.713  1.00 29.94 ? 218  THR B O   1 
ATOM   6461  C  CB  . THR B 1 226 ? 50.407  14.922  21.257  1.00 26.84 ? 218  THR B CB  1 
ATOM   6462  O  OG1 . THR B 1 226 ? 51.763  15.215  20.898  1.00 27.88 ? 218  THR B OG1 1 
ATOM   6463  C  CG2 . THR B 1 226 ? 50.353  13.598  22.016  1.00 27.11 ? 218  THR B CG2 1 
ATOM   6464  N  N   . ALA B 1 227 ? 50.323  16.555  18.401  1.00 26.90 ? 219  ALA B N   1 
ATOM   6465  C  CA  . ALA B 1 227 ? 50.192  17.812  17.665  1.00 22.69 ? 219  ALA B CA  1 
ATOM   6466  C  C   . ALA B 1 227 ? 48.889  17.845  16.873  1.00 24.52 ? 219  ALA B C   1 
ATOM   6467  O  O   . ALA B 1 227 ? 48.150  18.839  16.897  1.00 26.89 ? 219  ALA B O   1 
ATOM   6468  C  CB  . ALA B 1 227 ? 51.389  18.002  16.733  1.00 24.05 ? 219  ALA B CB  1 
ATOM   6469  N  N   . ALA B 1 228 ? 48.596  16.762  16.155  1.00 28.71 ? 220  ALA B N   1 
ATOM   6470  C  CA  . ALA B 1 228 ? 47.347  16.679  15.410  1.00 22.10 ? 220  ALA B CA  1 
ATOM   6471  C  C   . ALA B 1 228 ? 46.142  16.754  16.336  1.00 24.29 ? 220  ALA B C   1 
ATOM   6472  O  O   . ALA B 1 228 ? 45.122  17.367  15.994  1.00 23.92 ? 220  ALA B O   1 
ATOM   6473  C  CB  . ALA B 1 228 ? 47.317  15.387  14.597  1.00 25.40 ? 220  ALA B CB  1 
ATOM   6474  N  N   . ILE B 1 229 ? 46.228  16.118  17.508  1.00 20.96 ? 221  ILE B N   1 
ATOM   6475  C  CA  . ILE B 1 229 ? 45.089  16.123  18.425  1.00 18.47 ? 221  ILE B CA  1 
ATOM   6476  C  C   . ILE B 1 229 ? 44.873  17.521  18.989  1.00 18.44 ? 221  ILE B C   1 
ATOM   6477  O  O   . ILE B 1 229 ? 43.737  17.994  19.089  1.00 18.78 ? 221  ILE B O   1 
ATOM   6478  C  CB  . ILE B 1 229 ? 45.297  15.080  19.539  1.00 17.84 ? 221  ILE B CB  1 
ATOM   6479  C  CG1 . ILE B 1 229 ? 45.336  13.669  18.943  1.00 24.16 ? 221  ILE B CG1 1 
ATOM   6480  C  CG2 . ILE B 1 229 ? 44.211  15.197  20.612  1.00 17.34 ? 221  ILE B CG2 1 
ATOM   6481  C  CD1 . ILE B 1 229 ? 45.910  12.621  19.896  1.00 22.49 ? 221  ILE B CD1 1 
ATOM   6482  N  N   . GLN B 1 230 ? 45.961  18.212  19.347  1.00 19.97 ? 222  GLN B N   1 
ATOM   6483  C  CA  . GLN B 1 230 ? 45.843  19.580  19.841  1.00 22.62 ? 222  GLN B CA  1 
ATOM   6484  C  C   . GLN B 1 230 ? 45.209  20.490  18.793  1.00 20.80 ? 222  GLN B C   1 
ATOM   6485  O  O   . GLN B 1 230 ? 44.325  21.295  19.110  1.00 22.85 ? 222  GLN B O   1 
ATOM   6486  C  CB  . GLN B 1 230 ? 47.221  20.102  20.262  1.00 21.76 ? 222  GLN B CB  1 
ATOM   6487  C  CG  . GLN B 1 230 ? 47.198  21.492  20.866  1.00 28.79 ? 222  GLN B CG  1 
ATOM   6488  C  CD  . GLN B 1 230 ? 48.518  21.882  21.513  1.00 38.02 ? 222  GLN B CD  1 
ATOM   6489  O  OE1 . GLN B 1 230 ? 49.467  21.101  21.541  1.00 40.27 ? 222  GLN B OE1 1 
ATOM   6490  N  NE2 . GLN B 1 230 ? 48.576  23.096  22.048  1.00 42.55 ? 222  GLN B NE2 1 
ATOM   6491  N  N   . THR B 1 231 ? 45.631  20.361  17.534  1.00 25.46 ? 223  THR B N   1 
ATOM   6492  C  CA  . THR B 1 231 ? 45.051  21.188  16.479  1.00 23.78 ? 223  THR B CA  1 
ATOM   6493  C  C   . THR B 1 231 ? 43.561  20.914  16.329  1.00 21.24 ? 223  THR B C   1 
ATOM   6494  O  O   . THR B 1 231 ? 42.762  21.845  16.151  1.00 20.81 ? 223  THR B O   1 
ATOM   6495  C  CB  . THR B 1 231 ? 45.801  20.947  15.166  1.00 24.86 ? 223  THR B CB  1 
ATOM   6496  O  OG1 . THR B 1 231 ? 47.186  21.277  15.350  1.00 24.44 ? 223  THR B OG1 1 
ATOM   6497  C  CG2 . THR B 1 231 ? 45.232  21.804  14.046  1.00 24.69 ? 223  THR B CG2 1 
ATOM   6498  N  N   . ALA B 1 232 ? 43.164  19.644  16.448  1.00 19.46 ? 224  ALA B N   1 
ATOM   6499  C  CA  . ALA B 1 232 ? 41.753  19.285  16.348  1.00 18.20 ? 224  ALA B CA  1 
ATOM   6500  C  C   . ALA B 1 232 ? 40.944  19.881  17.497  1.00 21.79 ? 224  ALA B C   1 
ATOM   6501  O  O   . ALA B 1 232 ? 39.858  20.430  17.286  1.00 18.76 ? 224  ALA B O   1 
ATOM   6502  C  CB  . ALA B 1 232 ? 41.616  17.759  16.309  1.00 21.33 ? 224  ALA B CB  1 
ATOM   6503  N  N   . ILE B 1 233 ? 41.450  19.769  18.730  1.00 19.87 ? 225  ILE B N   1 
ATOM   6504  C  CA  . ILE B 1 233 ? 40.744  20.347  19.875  1.00 18.12 ? 225  ILE B CA  1 
ATOM   6505  C  C   . ILE B 1 233 ? 40.637  21.864  19.732  1.00 19.39 ? 225  ILE B C   1 
ATOM   6506  O  O   . ILE B 1 233 ? 39.592  22.460  20.035  1.00 19.00 ? 225  ILE B O   1 
ATOM   6507  C  CB  . ILE B 1 233 ? 41.441  19.938  21.190  1.00 21.56 ? 225  ILE B CB  1 
ATOM   6508  C  CG1 . ILE B 1 233 ? 41.359  18.424  21.376  1.00 19.46 ? 225  ILE B CG1 1 
ATOM   6509  C  CG2 . ILE B 1 233 ? 40.803  20.625  22.401  1.00 20.29 ? 225  ILE B CG2 1 
ATOM   6510  C  CD1 . ILE B 1 233 ? 42.019  17.943  22.657  1.00 15.91 ? 225  ILE B CD1 1 
ATOM   6511  N  N   . GLU B 1 234 ? 41.706  22.515  19.255  1.00 20.44 ? 226  GLU B N   1 
ATOM   6512  C  CA  . GLU B 1 234 ? 41.639  23.957  19.021  1.00 23.60 ? 226  GLU B CA  1 
ATOM   6513  C  C   . GLU B 1 234 ? 40.538  24.309  18.019  1.00 24.70 ? 226  GLU B C   1 
ATOM   6514  O  O   . GLU B 1 234 ? 39.773  25.258  18.233  1.00 23.08 ? 226  GLU B O   1 
ATOM   6515  C  CB  . GLU B 1 234 ? 43.006  24.482  18.556  1.00 20.53 ? 226  GLU B CB  1 
ATOM   6516  C  CG  . GLU B 1 234 ? 44.000  24.588  19.709  1.00 21.26 ? 226  GLU B CG  1 
ATOM   6517  C  CD  . GLU B 1 234 ? 45.464  24.691  19.275  1.00 30.59 ? 226  GLU B CD  1 
ATOM   6518  O  OE1 . GLU B 1 234 ? 45.754  24.636  18.064  1.00 30.99 ? 226  GLU B OE1 1 
ATOM   6519  O  OE2 . GLU B 1 234 ? 46.327  24.808  20.168  1.00 34.64 ? 226  GLU B OE2 1 
ATOM   6520  N  N   . ALA B 1 235 ? 40.425  23.544  16.932  1.00 23.39 ? 227  ALA B N   1 
ATOM   6521  C  CA  . ALA B 1 235 ? 39.355  23.797  15.969  1.00 20.17 ? 227  ALA B CA  1 
ATOM   6522  C  C   . ALA B 1 235 ? 37.983  23.603  16.602  1.00 22.70 ? 227  ALA B C   1 
ATOM   6523  O  O   . ALA B 1 235 ? 37.041  24.358  16.321  1.00 22.21 ? 227  ALA B O   1 
ATOM   6524  C  CB  . ALA B 1 235 ? 39.515  22.882  14.756  1.00 20.44 ? 227  ALA B CB  1 
ATOM   6525  N  N   . ALA B 1 236 ? 37.849  22.585  17.450  1.00 22.20 ? 228  ALA B N   1 
ATOM   6526  C  CA  . ALA B 1 236 ? 36.578  22.320  18.116  1.00 18.83 ? 228  ALA B CA  1 
ATOM   6527  C  C   . ALA B 1 236 ? 36.212  23.444  19.076  1.00 19.52 ? 228  ALA B C   1 
ATOM   6528  O  O   . ALA B 1 236 ? 35.048  23.847  19.156  1.00 22.73 ? 228  ALA B O   1 
ATOM   6529  C  CB  . ALA B 1 236 ? 36.659  20.983  18.853  1.00 18.34 ? 228  ALA B CB  1 
ATOM   6530  N  N   . ARG B 1 237 ? 37.197  23.975  19.805  1.00 19.04 ? 229  ARG B N   1 
ATOM   6531  C  CA  . ARG B 1 237 ? 36.913  25.065  20.731  1.00 20.64 ? 229  ARG B CA  1 
ATOM   6532  C  C   . ARG B 1 237 ? 36.573  26.357  19.996  1.00 24.83 ? 229  ARG B C   1 
ATOM   6533  O  O   . ARG B 1 237 ? 35.735  27.135  20.469  1.00 30.13 ? 229  ARG B O   1 
ATOM   6534  C  CB  . ARG B 1 237 ? 38.101  25.278  21.670  1.00 25.54 ? 229  ARG B CB  1 
ATOM   6535  C  CG  . ARG B 1 237 ? 38.387  24.096  22.591  1.00 25.93 ? 229  ARG B CG  1 
ATOM   6536  C  CD  . ARG B 1 237 ? 39.701  24.286  23.328  1.00 31.85 ? 229  ARG B CD  1 
ATOM   6537  N  NE  . ARG B 1 237 ? 39.771  25.589  23.983  1.00 34.96 ? 229  ARG B NE  1 
ATOM   6538  C  CZ  . ARG B 1 237 ? 39.171  25.872  25.135  1.00 35.72 ? 229  ARG B CZ  1 
ATOM   6539  N  NH1 . ARG B 1 237 ? 38.454  24.946  25.750  1.00 34.11 ? 229  ARG B NH1 1 
ATOM   6540  N  NH2 . ARG B 1 237 ? 39.269  27.083  25.663  1.00 38.17 ? 229  ARG B NH2 1 
ATOM   6541  N  N   . ALA B 1 238 ? 37.193  26.596  18.840  1.00 25.18 ? 230  ALA B N   1 
ATOM   6542  C  CA  . ALA B 1 238 ? 36.880  27.788  18.062  1.00 25.15 ? 230  ALA B CA  1 
ATOM   6543  C  C   . ALA B 1 238 ? 35.475  27.752  17.487  1.00 30.24 ? 230  ALA B C   1 
ATOM   6544  O  O   . ALA B 1 238 ? 34.933  28.809  17.148  1.00 29.14 ? 230  ALA B O   1 
ATOM   6545  C  CB  . ALA B 1 238 ? 37.893  27.969  16.935  1.00 22.64 ? 230  ALA B CB  1 
ATOM   6546  N  N   . GLU B 1 239 ? 34.875  26.572  17.369  1.00 27.88 ? 231  GLU B N   1 
ATOM   6547  C  CA  . GLU B 1 239 ? 33.507  26.438  16.871  1.00 28.06 ? 231  GLU B CA  1 
ATOM   6548  C  C   . GLU B 1 239 ? 32.570  26.554  18.067  1.00 31.70 ? 231  GLU B C   1 
ATOM   6549  O  O   . GLU B 1 239 ? 32.414  25.610  18.845  1.00 35.42 ? 231  GLU B O   1 
ATOM   6550  C  CB  . GLU B 1 239 ? 33.338  25.116  16.132  1.00 29.63 ? 231  GLU B CB  1 
ATOM   6551  C  CG  . GLU B 1 239 ? 31.916  24.801  15.748  1.00 35.28 ? 231  GLU B CG  1 
ATOM   6552  C  CD  . GLU B 1 239 ? 31.258  25.931  14.991  1.00 37.90 ? 231  GLU B CD  1 
ATOM   6553  O  OE1 . GLU B 1 239 ? 31.702  26.233  13.859  1.00 34.26 ? 231  GLU B OE1 1 
ATOM   6554  O  OE2 . GLU B 1 239 ? 30.303  26.520  15.542  1.00 37.45 ? 231  GLU B OE2 1 
ATOM   6555  N  N   . THR B 1 240 ? 31.951  27.721  18.229  1.00 32.51 ? 232  THR B N   1 
ATOM   6556  C  CA  . THR B 1 240 ? 31.181  28.007  19.431  1.00 27.30 ? 232  THR B CA  1 
ATOM   6557  C  C   . THR B 1 240 ? 29.692  27.722  19.284  1.00 29.03 ? 232  THR B C   1 
ATOM   6558  O  O   . THR B 1 240 ? 28.967  27.780  20.284  1.00 28.33 ? 232  THR B O   1 
ATOM   6559  C  CB  . THR B 1 240 ? 31.384  29.468  19.853  1.00 29.00 ? 232  THR B CB  1 
ATOM   6560  O  OG1 . THR B 1 240 ? 30.968  30.338  18.793  1.00 29.18 ? 232  THR B OG1 1 
ATOM   6561  C  CG2 . THR B 1 240 ? 32.839  29.724  20.156  1.00 31.89 ? 232  THR B CG2 1 
ATOM   6562  N  N   . GLY B 1 241 ? 29.218  27.396  18.084  1.00 25.91 ? 233  GLY B N   1 
ATOM   6563  C  CA  . GLY B 1 241 ? 27.793  27.194  17.898  1.00 28.24 ? 233  GLY B CA  1 
ATOM   6564  C  C   . GLY B 1 241 ? 27.312  25.760  17.767  1.00 25.92 ? 233  GLY B C   1 
ATOM   6565  O  O   . GLY B 1 241 ? 26.104  25.514  17.797  1.00 24.50 ? 233  GLY B O   1 
ATOM   6566  N  N   . LYS B 1 242 ? 28.228  24.804  17.613  1.00 19.68 ? 234  LYS B N   1 
ATOM   6567  C  CA  . LYS B 1 242 ? 27.860  23.414  17.400  1.00 17.32 ? 234  LYS B CA  1 
ATOM   6568  C  C   . LYS B 1 242 ? 28.707  22.517  18.293  1.00 15.75 ? 234  LYS B C   1 
ATOM   6569  O  O   . LYS B 1 242 ? 29.899  22.786  18.469  1.00 18.09 ? 234  LYS B O   1 
ATOM   6570  C  CB  . LYS B 1 242 ? 28.085  23.000  15.936  1.00 19.72 ? 234  LYS B CB  1 
ATOM   6571  C  CG  . LYS B 1 242 ? 27.424  23.861  14.865  1.00 26.50 ? 234  LYS B CG  1 
ATOM   6572  C  CD  . LYS B 1 242 ? 27.986  23.438  13.501  1.00 28.70 ? 234  LYS B CD  1 
ATOM   6573  C  CE  . LYS B 1 242 ? 27.270  24.087  12.343  1.00 35.03 ? 234  LYS B CE  1 
ATOM   6574  N  NZ  . LYS B 1 242 ? 27.885  23.645  11.055  1.00 39.90 ? 234  LYS B NZ  1 
ATOM   6575  N  N   . PRO B 1 243 ? 28.147  21.434  18.841  1.00 15.79 ? 235  PRO B N   1 
ATOM   6576  C  CA  . PRO B 1 243 ? 29.002  20.436  19.501  1.00 14.56 ? 235  PRO B CA  1 
ATOM   6577  C  C   . PRO B 1 243 ? 29.974  19.827  18.498  1.00 16.79 ? 235  PRO B C   1 
ATOM   6578  O  O   . PRO B 1 243 ? 29.704  19.780  17.297  1.00 18.39 ? 235  PRO B O   1 
ATOM   6579  C  CB  . PRO B 1 243 ? 28.008  19.396  20.032  1.00 12.80 ? 235  PRO B CB  1 
ATOM   6580  C  CG  . PRO B 1 243 ? 26.760  19.569  19.117  1.00 12.65 ? 235  PRO B CG  1 
ATOM   6581  C  CD  . PRO B 1 243 ? 26.728  21.025  18.785  1.00 14.97 ? 235  PRO B CD  1 
ATOM   6582  N  N   . SER B 1 244 ? 31.114  19.351  19.001  1.00 14.49 ? 236  SER B N   1 
ATOM   6583  C  CA  . SER B 1 244 ? 32.190  18.864  18.149  1.00 20.69 ? 236  SER B CA  1 
ATOM   6584  C  C   . SER B 1 244 ? 32.492  17.403  18.440  1.00 15.95 ? 236  SER B C   1 
ATOM   6585  O  O   . SER B 1 244 ? 32.540  16.992  19.601  1.00 13.60 ? 236  SER B O   1 
ATOM   6586  C  CB  . SER B 1 244 ? 33.476  19.682  18.344  1.00 19.52 ? 236  SER B CB  1 
ATOM   6587  O  OG  . SER B 1 244 ? 33.327  21.025  17.919  1.00 19.96 ? 236  SER B OG  1 
ATOM   6588  N  N   . ILE B 1 245 ? 32.735  16.627  17.384  1.00 16.52 ? 237  ILE B N   1 
ATOM   6589  C  CA  . ILE B 1 245 ? 33.270  15.278  17.525  1.00 16.37 ? 237  ILE B CA  1 
ATOM   6590  C  C   . ILE B 1 245 ? 34.564  15.196  16.733  1.00 15.10 ? 237  ILE B C   1 
ATOM   6591  O  O   . ILE B 1 245 ? 34.614  15.597  15.563  1.00 18.21 ? 237  ILE B O   1 
ATOM   6592  C  CB  . ILE B 1 245 ? 32.282  14.180  17.078  1.00 13.84 ? 237  ILE B CB  1 
ATOM   6593  C  CG1 . ILE B 1 245 ? 32.961  12.801  17.187  1.00 12.60 ? 237  ILE B CG1 1 
ATOM   6594  C  CG2 . ILE B 1 245 ? 31.769  14.422  15.647  1.00 13.15 ? 237  ILE B CG2 1 
ATOM   6595  C  CD1 . ILE B 1 245 ? 31.966  11.654  17.367  1.00 18.63 ? 237  ILE B CD1 1 
ATOM   6596  N  N   . ILE B 1 246 ? 35.609  14.704  17.387  1.00 13.73 ? 238  ILE B N   1 
ATOM   6597  C  CA  . ILE B 1 246 ? 36.937  14.566  16.809  1.00 14.40 ? 238  ILE B CA  1 
ATOM   6598  C  C   . ILE B 1 246 ? 37.184  13.073  16.663  1.00 15.05 ? 238  ILE B C   1 
ATOM   6599  O  O   . ILE B 1 246 ? 37.212  12.336  17.657  1.00 16.85 ? 238  ILE B O   1 
ATOM   6600  C  CB  . ILE B 1 246 ? 38.001  15.240  17.689  1.00 17.57 ? 238  ILE B CB  1 
ATOM   6601  C  CG1 . ILE B 1 246 ? 37.670  16.730  17.866  1.00 14.87 ? 238  ILE B CG1 1 
ATOM   6602  C  CG2 . ILE B 1 246 ? 39.408  15.036  17.118  1.00 17.57 ? 238  ILE B CG2 1 
ATOM   6603  C  CD1 . ILE B 1 246 ? 38.518  17.432  18.911  1.00 23.75 ? 238  ILE B CD1 1 
ATOM   6604  N  N   . CYS B 1 247 ? 37.306  12.607  15.428  1.00 14.71 ? 239  CYS B N   1 
ATOM   6605  C  CA  . CYS B 1 247 ? 37.475  11.181  15.158  1.00 17.27 ? 239  CYS B CA  1 
ATOM   6606  C  C   . CYS B 1 247 ? 38.959  10.841  15.219  1.00 18.87 ? 239  CYS B C   1 
ATOM   6607  O  O   . CYS B 1 247 ? 39.715  11.182  14.307  1.00 17.70 ? 239  CYS B O   1 
ATOM   6608  C  CB  . CYS B 1 247 ? 36.890  10.832  13.795  1.00 20.68 ? 239  CYS B CB  1 
ATOM   6609  S  SG  . CYS B 1 247 ? 35.145  11.299  13.661  1.00 18.25 ? 239  CYS B SG  1 
ATOM   6610  N  N   . CYS B 1 248 ? 39.374  10.166  16.285  1.00 15.00 ? 240  CYS B N   1 
ATOM   6611  C  CA  . CYS B 1 248 ? 40.787  9.885   16.530  1.00 20.21 ? 240  CYS B CA  1 
ATOM   6612  C  C   . CYS B 1 248 ? 41.085  8.443   16.132  1.00 18.96 ? 240  CYS B C   1 
ATOM   6613  O  O   . CYS B 1 248 ? 40.642  7.503   16.803  1.00 19.74 ? 240  CYS B O   1 
ATOM   6614  C  CB  . CYS B 1 248 ? 41.135  10.131  17.998  1.00 20.37 ? 240  CYS B CB  1 
ATOM   6615  S  SG  . CYS B 1 248 ? 40.856  11.836  18.571  1.00 18.97 ? 240  CYS B SG  1 
ATOM   6616  N  N   . LYS B 1 249 ? 41.834  8.271   15.042  1.00 16.65 ? 241  LYS B N   1 
ATOM   6617  C  CA  . LYS B 1 249 ? 42.260  6.944   14.625  1.00 17.08 ? 241  LYS B CA  1 
ATOM   6618  C  C   . LYS B 1 249 ? 43.334  6.436   15.576  1.00 17.30 ? 241  LYS B C   1 
ATOM   6619  O  O   . LYS B 1 249 ? 44.424  7.015   15.647  1.00 19.49 ? 241  LYS B O   1 
ATOM   6620  C  CB  . LYS B 1 249 ? 42.799  6.986   13.197  1.00 18.76 ? 241  LYS B CB  1 
ATOM   6621  C  CG  . LYS B 1 249 ? 41.866  7.670   12.201  1.00 20.08 ? 241  LYS B CG  1 
ATOM   6622  C  CD  . LYS B 1 249 ? 40.559  6.910   12.113  1.00 26.53 ? 241  LYS B CD  1 
ATOM   6623  C  CE  . LYS B 1 249 ? 39.754  7.320   10.880  1.00 30.61 ? 241  LYS B CE  1 
ATOM   6624  N  NZ  . LYS B 1 249 ? 38.529  6.476   10.731  1.00 27.44 ? 241  LYS B NZ  1 
ATOM   6625  N  N   . THR B 1 250 ? 43.038  5.356   16.299  1.00 21.32 ? 242  THR B N   1 
ATOM   6626  C  CA  . THR B 1 250 ? 44.002  4.736   17.203  1.00 17.88 ? 242  THR B CA  1 
ATOM   6627  C  C   . THR B 1 250 ? 44.093  3.238   16.934  1.00 23.94 ? 242  THR B C   1 
ATOM   6628  O  O   . THR B 1 250 ? 43.240  2.642   16.269  1.00 17.42 ? 242  THR B O   1 
ATOM   6629  C  CB  . THR B 1 250 ? 43.626  4.933   18.684  1.00 16.42 ? 242  THR B CB  1 
ATOM   6630  O  OG1 . THR B 1 250 ? 42.377  4.277   18.946  1.00 19.39 ? 242  THR B OG1 1 
ATOM   6631  C  CG2 . THR B 1 250 ? 43.510  6.399   19.048  1.00 17.62 ? 242  THR B CG2 1 
ATOM   6632  N  N   . LEU B 1 251 ? 45.123  2.623   17.512  1.00 21.61 ? 243  LEU B N   1 
ATOM   6633  C  CA  . LEU B 1 251 ? 45.232  1.176   17.617  1.00 23.33 ? 243  LEU B CA  1 
ATOM   6634  C  C   . LEU B 1 251 ? 44.925  0.772   19.049  1.00 26.81 ? 243  LEU B C   1 
ATOM   6635  O  O   . LEU B 1 251 ? 45.524  1.317   19.982  1.00 20.00 ? 243  LEU B O   1 
ATOM   6636  C  CB  . LEU B 1 251 ? 46.635  0.698   17.247  1.00 27.54 ? 243  LEU B CB  1 
ATOM   6637  C  CG  . LEU B 1 251 ? 47.105  0.989   15.828  1.00 27.47 ? 243  LEU B CG  1 
ATOM   6638  C  CD1 . LEU B 1 251 ? 48.551  0.545   15.647  1.00 31.45 ? 243  LEU B CD1 1 
ATOM   6639  C  CD2 . LEU B 1 251 ? 46.188  0.276   14.868  1.00 29.67 ? 243  LEU B CD2 1 
ATOM   6640  N  N   . ILE B 1 252 ? 44.010  -0.186  19.231  1.00 17.42 ? 244  ILE B N   1 
ATOM   6641  C  CA  . ILE B 1 252 ? 43.820  -0.720  20.572  1.00 17.03 ? 244  ILE B CA  1 
ATOM   6642  C  C   . ILE B 1 252 ? 45.120  -1.380  21.003  1.00 19.33 ? 244  ILE B C   1 
ATOM   6643  O  O   . ILE B 1 252 ? 45.856  -1.946  20.183  1.00 19.16 ? 244  ILE B O   1 
ATOM   6644  C  CB  . ILE B 1 252 ? 42.628  -1.692  20.636  1.00 16.64 ? 244  ILE B CB  1 
ATOM   6645  C  CG1 . ILE B 1 252 ? 42.201  -1.902  22.088  1.00 19.90 ? 244  ILE B CG1 1 
ATOM   6646  C  CG2 . ILE B 1 252 ? 42.957  -3.042  19.982  1.00 20.17 ? 244  ILE B CG2 1 
ATOM   6647  C  CD1 . ILE B 1 252 ? 40.856  -2.603  22.235  1.00 22.10 ? 244  ILE B CD1 1 
ATOM   6648  N  N   . GLY B 1 253 ? 45.439  -1.259  22.290  1.00 18.87 ? 245  GLY B N   1 
ATOM   6649  C  CA  . GLY B 1 253 ? 46.687  -1.816  22.784  1.00 18.50 ? 245  GLY B CA  1 
ATOM   6650  C  C   . GLY B 1 253 ? 47.929  -1.177  22.202  1.00 19.29 ? 245  GLY B C   1 
ATOM   6651  O  O   . GLY B 1 253 ? 48.980  -1.827  22.143  1.00 20.25 ? 245  GLY B O   1 
ATOM   6652  N  N   . LYS B 1 254 ? 47.839  0.082   21.776  1.00 21.29 ? 246  LYS B N   1 
ATOM   6653  C  CA  . LYS B 1 254 ? 48.992  0.773   21.205  1.00 22.21 ? 246  LYS B CA  1 
ATOM   6654  C  C   . LYS B 1 254 ? 50.163  0.763   22.183  1.00 25.49 ? 246  LYS B C   1 
ATOM   6655  O  O   . LYS B 1 254 ? 50.012  1.093   23.364  1.00 19.87 ? 246  LYS B O   1 
ATOM   6656  C  CB  . LYS B 1 254 ? 48.623  2.212   20.843  1.00 19.33 ? 246  LYS B CB  1 
ATOM   6657  C  CG  . LYS B 1 254 ? 49.805  3.063   20.359  1.00 20.43 ? 246  LYS B CG  1 
ATOM   6658  C  CD  . LYS B 1 254 ? 50.141  2.831   18.900  1.00 24.59 ? 246  LYS B CD  1 
ATOM   6659  C  CE  . LYS B 1 254 ? 51.416  3.601   18.518  1.00 33.04 ? 246  LYS B CE  1 
ATOM   6660  N  NZ  . LYS B 1 254 ? 51.560  3.793   17.049  1.00 40.42 ? 246  LYS B NZ  1 
ATOM   6661  N  N   . GLY B 1 255 ? 51.334  0.402   21.679  1.00 21.51 ? 247  GLY B N   1 
ATOM   6662  C  CA  . GLY B 1 255 ? 52.527  0.278   22.479  1.00 22.27 ? 247  GLY B CA  1 
ATOM   6663  C  C   . GLY B 1 255 ? 52.849  -1.146  22.872  1.00 28.34 ? 247  GLY B C   1 
ATOM   6664  O  O   . GLY B 1 255 ? 54.005  -1.438  23.193  1.00 24.62 ? 247  GLY B O   1 
ATOM   6665  N  N   . SER B 1 256 ? 51.858  -2.041  22.835  1.00 22.31 ? 248  SER B N   1 
ATOM   6666  C  CA  . SER B 1 256 ? 52.115  -3.441  23.137  1.00 22.93 ? 248  SER B CA  1 
ATOM   6667  C  C   . SER B 1 256 ? 53.152  -4.004  22.182  1.00 24.26 ? 248  SER B C   1 
ATOM   6668  O  O   . SER B 1 256 ? 53.127  -3.732  20.979  1.00 25.16 ? 248  SER B O   1 
ATOM   6669  C  CB  . SER B 1 256 ? 50.828  -4.256  23.041  1.00 22.26 ? 248  SER B CB  1 
ATOM   6670  O  OG  . SER B 1 256 ? 51.114  -5.642  23.053  1.00 26.59 ? 248  SER B OG  1 
ATOM   6671  N  N   . ALA B 1 257 ? 54.071  -4.794  22.730  1.00 25.21 ? 249  ALA B N   1 
ATOM   6672  C  CA  . ALA B 1 257 ? 55.138  -5.350  21.907  1.00 31.35 ? 249  ALA B CA  1 
ATOM   6673  C  C   . ALA B 1 257 ? 54.588  -6.319  20.869  1.00 31.50 ? 249  ALA B C   1 
ATOM   6674  O  O   . ALA B 1 257 ? 55.058  -6.345  19.727  1.00 28.72 ? 249  ALA B O   1 
ATOM   6675  C  CB  . ALA B 1 257 ? 56.176  -6.040  22.792  1.00 27.62 ? 249  ALA B CB  1 
ATOM   6676  N  N   . ASN B 1 258 ? 53.586  -7.120  21.242  1.00 32.36 ? 250  ASN B N   1 
ATOM   6677  C  CA  . ASN B 1 258 ? 53.118  -8.195  20.379  1.00 29.76 ? 250  ASN B CA  1 
ATOM   6678  C  C   . ASN B 1 258 ? 51.611  -8.242  20.179  1.00 33.93 ? 250  ASN B C   1 
ATOM   6679  O  O   . ASN B 1 258 ? 51.156  -8.993  19.309  1.00 31.74 ? 250  ASN B O   1 
ATOM   6680  C  CB  . ASN B 1 258 ? 53.585  -9.551  20.922  1.00 34.04 ? 250  ASN B CB  1 
ATOM   6681  C  CG  . ASN B 1 258 ? 55.088  -9.634  21.035  1.00 29.82 ? 250  ASN B CG  1 
ATOM   6682  O  OD1 . ASN B 1 258 ? 55.790  -9.611  20.032  1.00 32.40 ? 250  ASN B OD1 1 
ATOM   6683  N  ND2 . ASN B 1 258 ? 55.592  -9.716  22.262  1.00 30.18 ? 250  ASN B ND2 1 
ATOM   6684  N  N   . LYS B 1 259 ? 50.825  -7.472  20.937  1.00 24.35 ? 251  LYS B N   1 
ATOM   6685  C  CA  . LYS B 1 259 ? 49.371  -7.541  20.847  1.00 27.04 ? 251  LYS B CA  1 
ATOM   6686  C  C   . LYS B 1 259 ? 48.755  -6.226  20.384  1.00 29.68 ? 251  LYS B C   1 
ATOM   6687  O  O   . LYS B 1 259 ? 47.554  -6.003  20.579  1.00 25.10 ? 251  LYS B O   1 
ATOM   6688  C  CB  . LYS B 1 259 ? 48.775  -7.965  22.190  1.00 26.67 ? 251  LYS B CB  1 
ATOM   6689  C  CG  . LYS B 1 259 ? 49.231  -9.339  22.656  1.00 32.68 ? 251  LYS B CG  1 
ATOM   6690  C  CD  . LYS B 1 259 ? 48.586  -9.707  23.986  1.00 33.28 ? 251  LYS B CD  1 
ATOM   6691  C  CE  . LYS B 1 259 ? 49.236  -10.931 24.605  1.00 38.99 ? 251  LYS B CE  1 
ATOM   6692  N  NZ  . LYS B 1 259 ? 48.658  -11.238 25.944  1.00 41.12 ? 251  LYS B NZ  1 
ATOM   6693  N  N   . GLU B 1 260 ? 49.545  -5.350  19.768  1.00 29.33 ? 252  GLU B N   1 
ATOM   6694  C  CA  . GLU B 1 260 ? 49.007  -4.092  19.264  1.00 29.04 ? 252  GLU B CA  1 
ATOM   6695  C  C   . GLU B 1 260 ? 47.945  -4.359  18.199  1.00 28.00 ? 252  GLU B C   1 
ATOM   6696  O  O   . GLU B 1 260 ? 48.162  -5.149  17.274  1.00 26.67 ? 252  GLU B O   1 
ATOM   6697  C  CB  . GLU B 1 260 ? 50.144  -3.240  18.700  1.00 29.31 ? 252  GLU B CB  1 
ATOM   6698  C  CG  . GLU B 1 260 ? 49.826  -1.777  18.470  1.00 31.59 ? 252  GLU B CG  1 
ATOM   6699  C  CD  . GLU B 1 260 ? 51.076  -0.992  18.100  1.00 35.85 ? 252  GLU B CD  1 
ATOM   6700  O  OE1 . GLU B 1 260 ? 51.708  -0.395  19.003  1.00 26.45 ? 252  GLU B OE1 1 
ATOM   6701  O  OE2 . GLU B 1 260 ? 51.439  -0.998  16.904  1.00 39.06 ? 252  GLU B OE2 1 
ATOM   6702  N  N   . GLY B 1 261 ? 46.786  -3.717  18.349  1.00 26.92 ? 253  GLY B N   1 
ATOM   6703  C  CA  . GLY B 1 261 ? 45.668  -3.896  17.439  1.00 22.95 ? 253  GLY B CA  1 
ATOM   6704  C  C   . GLY B 1 261 ? 44.847  -5.151  17.640  1.00 25.91 ? 253  GLY B C   1 
ATOM   6705  O  O   . GLY B 1 261 ? 43.899  -5.379  16.879  1.00 32.02 ? 253  GLY B O   1 
ATOM   6706  N  N   . SER B 1 262 ? 45.155  -5.969  18.637  1.00 27.54 ? 254  SER B N   1 
ATOM   6707  C  CA  . SER B 1 262 ? 44.441  -7.223  18.831  1.00 30.93 ? 254  SER B CA  1 
ATOM   6708  C  C   . SER B 1 262 ? 43.246  -7.008  19.749  1.00 32.89 ? 254  SER B C   1 
ATOM   6709  O  O   . SER B 1 262 ? 43.387  -6.442  20.839  1.00 32.72 ? 254  SER B O   1 
ATOM   6710  C  CB  . SER B 1 262 ? 45.368  -8.294  19.409  1.00 30.66 ? 254  SER B CB  1 
ATOM   6711  O  OG  . SER B 1 262 ? 44.627  -9.417  19.852  1.00 28.23 ? 254  SER B OG  1 
ATOM   6712  N  N   . HIS B 1 263 ? 42.071  -7.476  19.307  1.00 28.14 ? 255  HIS B N   1 
ATOM   6713  C  CA  . HIS B 1 263 ? 40.866  -7.364  20.122  1.00 32.64 ? 255  HIS B CA  1 
ATOM   6714  C  C   . HIS B 1 263 ? 40.984  -8.143  21.423  1.00 30.65 ? 255  HIS B C   1 
ATOM   6715  O  O   . HIS B 1 263 ? 40.212  -7.888  22.357  1.00 27.54 ? 255  HIS B O   1 
ATOM   6716  C  CB  . HIS B 1 263 ? 39.640  -7.836  19.334  1.00 37.56 ? 255  HIS B CB  1 
ATOM   6717  C  CG  . HIS B 1 263 ? 39.717  -9.262  18.888  1.00 50.34 ? 255  HIS B CG  1 
ATOM   6718  N  ND1 . HIS B 1 263 ? 40.418  -9.655  17.768  1.00 53.49 ? 255  HIS B ND1 1 
ATOM   6719  C  CD2 . HIS B 1 263 ? 39.172  -10.389 19.405  1.00 53.83 ? 255  HIS B CD2 1 
ATOM   6720  C  CE1 . HIS B 1 263 ? 40.309  -10.963 17.619  1.00 54.88 ? 255  HIS B CE1 1 
ATOM   6721  N  NE2 . HIS B 1 263 ? 39.559  -11.433 18.600  1.00 55.34 ? 255  HIS B NE2 1 
ATOM   6722  N  N   . LYS B 1 264 ? 41.948  -9.067  21.512  1.00 25.08 ? 256  LYS B N   1 
ATOM   6723  C  CA  . LYS B 1 264 ? 42.201  -9.771  22.765  1.00 28.69 ? 256  LYS B CA  1 
ATOM   6724  C  C   . LYS B 1 264 ? 42.568  -8.810  23.889  1.00 26.52 ? 256  LYS B C   1 
ATOM   6725  O  O   . LYS B 1 264 ? 42.363  -9.128  25.065  1.00 28.34 ? 256  LYS B O   1 
ATOM   6726  C  CB  . LYS B 1 264 ? 43.318  -10.802 22.570  1.00 32.28 ? 256  LYS B CB  1 
ATOM   6727  N  N   . THR B 1 265 ? 43.145  -7.655  23.559  1.00 21.89 ? 257  THR B N   1 
ATOM   6728  C  CA  . THR B 1 265 ? 43.564  -6.698  24.582  1.00 24.92 ? 257  THR B CA  1 
ATOM   6729  C  C   . THR B 1 265 ? 42.394  -5.919  25.177  1.00 21.73 ? 257  THR B C   1 
ATOM   6730  O  O   . THR B 1 265 ? 42.605  -5.124  26.099  1.00 20.44 ? 257  THR B O   1 
ATOM   6731  C  CB  . THR B 1 265 ? 44.590  -5.710  24.009  1.00 21.00 ? 257  THR B CB  1 
ATOM   6732  O  OG1 . THR B 1 265 ? 43.980  -4.911  22.987  1.00 23.32 ? 257  THR B OG1 1 
ATOM   6733  C  CG2 . THR B 1 265 ? 45.785  -6.456  23.413  1.00 17.67 ? 257  THR B CG2 1 
ATOM   6734  N  N   . HIS B 1 266 ? 41.177  -6.119  24.673  1.00 21.73 ? 258  HIS B N   1 
ATOM   6735  C  CA  . HIS B 1 266 ? 40.054  -5.317  25.139  1.00 28.93 ? 258  HIS B CA  1 
ATOM   6736  C  C   . HIS B 1 266 ? 39.678  -5.658  26.574  1.00 29.73 ? 258  HIS B C   1 
ATOM   6737  O  O   . HIS B 1 266 ? 39.540  -4.765  27.413  1.00 25.66 ? 258  HIS B O   1 
ATOM   6738  C  CB  . HIS B 1 266 ? 38.839  -5.507  24.237  1.00 38.46 ? 258  HIS B CB  1 
ATOM   6739  C  CG  . HIS B 1 266 ? 37.575  -4.993  24.849  1.00 48.09 ? 258  HIS B CG  1 
ATOM   6740  N  ND1 . HIS B 1 266 ? 37.267  -3.651  24.901  1.00 50.66 ? 258  HIS B ND1 1 
ATOM   6741  C  CD2 . HIS B 1 266 ? 36.567  -5.636  25.486  1.00 50.72 ? 258  HIS B CD2 1 
ATOM   6742  C  CE1 . HIS B 1 266 ? 36.111  -3.491  25.521  1.00 51.63 ? 258  HIS B CE1 1 
ATOM   6743  N  NE2 . HIS B 1 266 ? 35.666  -4.680  25.887  1.00 50.89 ? 258  HIS B NE2 1 
ATOM   6744  N  N   . GLY B 1 267 ? 39.491  -6.939  26.872  1.00 29.44 ? 259  GLY B N   1 
ATOM   6745  C  CA  . GLY B 1 267 ? 38.845  -7.296  28.118  1.00 28.59 ? 259  GLY B CA  1 
ATOM   6746  C  C   . GLY B 1 267 ? 39.555  -8.332  28.957  1.00 28.88 ? 259  GLY B C   1 
ATOM   6747  O  O   . GLY B 1 267 ? 38.972  -8.862  29.907  1.00 24.48 ? 259  GLY B O   1 
ATOM   6748  N  N   . ALA B 1 268 ? 40.808  -8.627  28.630  1.00 26.34 ? 260  ALA B N   1 
ATOM   6749  C  CA  . ALA B 1 268 ? 41.610  -9.543  29.423  1.00 25.03 ? 260  ALA B CA  1 
ATOM   6750  C  C   . ALA B 1 268 ? 42.961  -8.905  29.705  1.00 20.41 ? 260  ALA B C   1 
ATOM   6751  O  O   . ALA B 1 268 ? 43.434  -8.091  28.910  1.00 21.64 ? 260  ALA B O   1 
ATOM   6752  C  CB  . ALA B 1 268 ? 41.812  -10.881 28.694  1.00 25.86 ? 260  ALA B CB  1 
ATOM   6753  N  N   . PRO B 1 269 ? 43.593  -9.242  30.831  1.00 17.98 ? 261  PRO B N   1 
ATOM   6754  C  CA  . PRO B 1 269 ? 44.964  -8.772  31.080  1.00 18.55 ? 261  PRO B CA  1 
ATOM   6755  C  C   . PRO B 1 269 ? 45.895  -9.107  29.921  1.00 18.24 ? 261  PRO B C   1 
ATOM   6756  O  O   . PRO B 1 269 ? 45.696  -10.083 29.200  1.00 15.92 ? 261  PRO B O   1 
ATOM   6757  C  CB  . PRO B 1 269 ? 45.367  -9.519  32.356  1.00 21.90 ? 261  PRO B CB  1 
ATOM   6758  C  CG  . PRO B 1 269 ? 44.050  -9.740  33.072  1.00 24.14 ? 261  PRO B CG  1 
ATOM   6759  C  CD  . PRO B 1 269 ? 43.048  -9.998  31.972  1.00 20.06 ? 261  PRO B CD  1 
ATOM   6760  N  N   . LEU B 1 270 ? 46.905  -8.254  29.728  1.00 19.11 ? 262  LEU B N   1 
ATOM   6761  C  CA  . LEU B 1 270 ? 47.900  -8.505  28.689  1.00 19.50 ? 262  LEU B CA  1 
ATOM   6762  C  C   . LEU B 1 270 ? 48.686  -9.775  28.966  1.00 21.30 ? 262  LEU B C   1 
ATOM   6763  O  O   . LEU B 1 270 ? 49.139  -10.443 28.027  1.00 25.97 ? 262  LEU B O   1 
ATOM   6764  C  CB  . LEU B 1 270 ? 48.862  -7.320  28.582  1.00 17.09 ? 262  LEU B CB  1 
ATOM   6765  C  CG  . LEU B 1 270 ? 48.326  -5.990  28.072  1.00 24.26 ? 262  LEU B CG  1 
ATOM   6766  C  CD1 . LEU B 1 270 ? 49.495  -5.038  27.829  1.00 21.79 ? 262  LEU B CD1 1 
ATOM   6767  C  CD2 . LEU B 1 270 ? 47.521  -6.182  26.793  1.00 28.91 ? 262  LEU B CD2 1 
ATOM   6768  N  N   . GLY B 1 271 ? 48.860  -10.121 30.231  1.00 19.52 ? 263  GLY B N   1 
ATOM   6769  C  CA  . GLY B 1 271 ? 49.733  -11.214 30.613  1.00 21.38 ? 263  GLY B CA  1 
ATOM   6770  C  C   . GLY B 1 271 ? 51.112  -10.712 31.000  1.00 21.63 ? 263  GLY B C   1 
ATOM   6771  O  O   . GLY B 1 271 ? 51.609  -9.701  30.481  1.00 17.89 ? 263  GLY B O   1 
ATOM   6772  N  N   . ALA B 1 272 ? 51.751  -11.429 31.928  1.00 19.24 ? 264  ALA B N   1 
ATOM   6773  C  CA  . ALA B 1 272 ? 53.010  -10.943 32.484  1.00 20.49 ? 264  ALA B CA  1 
ATOM   6774  C  C   . ALA B 1 272 ? 54.114  -10.917 31.432  1.00 18.96 ? 264  ALA B C   1 
ATOM   6775  O  O   . ALA B 1 272 ? 54.877  -9.949  31.359  1.00 20.60 ? 264  ALA B O   1 
ATOM   6776  C  CB  . ALA B 1 272 ? 53.429  -11.790 33.684  1.00 26.42 ? 264  ALA B CB  1 
ATOM   6777  N  N   . ASP B 1 273 ? 54.216  -11.963 30.608  1.00 19.26 ? 265  ASP B N   1 
ATOM   6778  C  CA  . ASP B 1 273 ? 55.263  -11.981 29.584  1.00 23.28 ? 265  ASP B CA  1 
ATOM   6779  C  C   . ASP B 1 273 ? 55.109  -10.811 28.618  1.00 20.29 ? 265  ASP B C   1 
ATOM   6780  O  O   . ASP B 1 273 ? 56.099  -10.174 28.237  1.00 20.99 ? 265  ASP B O   1 
ATOM   6781  C  CB  . ASP B 1 273 ? 55.233  -13.295 28.805  1.00 20.40 ? 265  ASP B CB  1 
ATOM   6782  C  CG  . ASP B 1 273 ? 55.767  -14.466 29.595  1.00 28.16 ? 265  ASP B CG  1 
ATOM   6783  O  OD1 . ASP B 1 273 ? 56.311  -14.264 30.705  1.00 28.89 ? 265  ASP B OD1 1 
ATOM   6784  O  OD2 . ASP B 1 273 ? 55.646  -15.600 29.091  1.00 27.11 ? 265  ASP B OD2 1 
ATOM   6785  N  N   . GLU B 1 274 ? 53.875  -10.528 28.198  1.00 19.73 ? 266  GLU B N   1 
ATOM   6786  C  CA  . GLU B 1 274 ? 53.644  -9.446  27.247  1.00 22.83 ? 266  GLU B CA  1 
ATOM   6787  C  C   . GLU B 1 274 ? 53.955  -8.090  27.861  1.00 20.57 ? 266  GLU B C   1 
ATOM   6788  O  O   . GLU B 1 274 ? 54.473  -7.199  27.175  1.00 20.47 ? 266  GLU B O   1 
ATOM   6789  C  CB  . GLU B 1 274 ? 52.200  -9.478  26.737  1.00 22.89 ? 266  GLU B CB  1 
ATOM   6790  C  CG  . GLU B 1 274 ? 51.857  -8.350  25.758  1.00 23.06 ? 266  GLU B CG  1 
ATOM   6791  C  CD  . GLU B 1 274 ? 52.756  -8.346  24.523  1.00 25.10 ? 266  GLU B CD  1 
ATOM   6792  O  OE1 . GLU B 1 274 ? 53.270  -9.424  24.146  1.00 25.17 ? 266  GLU B OE1 1 
ATOM   6793  O  OE2 . GLU B 1 274 ? 52.959  -7.261  23.933  1.00 24.31 ? 266  GLU B OE2 1 
ATOM   6794  N  N   . ILE B 1 275 ? 53.627  -7.901  29.144  1.00 19.31 ? 267  ILE B N   1 
ATOM   6795  C  CA  . ILE B 1 275 ? 53.940  -6.629  29.780  1.00 19.36 ? 267  ILE B CA  1 
ATOM   6796  C  C   . ILE B 1 275 ? 55.451  -6.435  29.855  1.00 20.27 ? 267  ILE B C   1 
ATOM   6797  O  O   . ILE B 1 275 ? 55.963  -5.339  29.603  1.00 20.78 ? 267  ILE B O   1 
ATOM   6798  C  CB  . ILE B 1 275 ? 53.285  -6.542  31.169  1.00 18.63 ? 267  ILE B CB  1 
ATOM   6799  C  CG1 . ILE B 1 275 ? 51.763  -6.381  31.031  1.00 17.84 ? 267  ILE B CG1 1 
ATOM   6800  C  CG2 . ILE B 1 275 ? 53.869  -5.387  31.957  1.00 18.86 ? 267  ILE B CG2 1 
ATOM   6801  C  CD1 . ILE B 1 275 ? 51.009  -6.402  32.374  1.00 20.28 ? 267  ILE B CD1 1 
ATOM   6802  N  N   . GLU B 1 276 ? 56.191  -7.495  30.188  1.00 20.56 ? 268  GLU B N   1 
ATOM   6803  C  CA  . GLU B 1 276 ? 57.643  -7.373  30.208  1.00 21.52 ? 268  GLU B CA  1 
ATOM   6804  C  C   . GLU B 1 276 ? 58.183  -7.052  28.820  1.00 22.34 ? 268  GLU B C   1 
ATOM   6805  O  O   . GLU B 1 276 ? 59.068  -6.199  28.673  1.00 23.13 ? 268  GLU B O   1 
ATOM   6806  C  CB  . GLU B 1 276 ? 58.271  -8.654  30.755  1.00 28.16 ? 268  GLU B CB  1 
ATOM   6807  C  CG  . GLU B 1 276 ? 59.774  -8.583  30.926  1.00 30.62 ? 268  GLU B CG  1 
ATOM   6808  C  CD  . GLU B 1 276 ? 60.218  -7.604  32.014  1.00 29.79 ? 268  GLU B CD  1 
ATOM   6809  O  OE1 . GLU B 1 276 ? 59.375  -7.109  32.797  1.00 26.96 ? 268  GLU B OE1 1 
ATOM   6810  O  OE2 . GLU B 1 276 ? 61.430  -7.337  32.088  1.00 29.85 ? 268  GLU B OE2 1 
ATOM   6811  N  N   . ALA B 1 277 ? 57.656  -7.715  27.785  1.00 22.27 ? 269  ALA B N   1 
ATOM   6812  C  CA  . ALA B 1 277 ? 58.081  -7.405  26.422  1.00 23.09 ? 269  ALA B CA  1 
ATOM   6813  C  C   . ALA B 1 277 ? 57.741  -5.968  26.051  1.00 25.09 ? 269  ALA B C   1 
ATOM   6814  O  O   . ALA B 1 277 ? 58.490  -5.315  25.312  1.00 24.08 ? 269  ALA B O   1 
ATOM   6815  C  CB  . ALA B 1 277 ? 57.436  -8.378  25.430  1.00 24.33 ? 269  ALA B CB  1 
ATOM   6816  N  N   . THR B 1 278 ? 56.598  -5.466  26.534  1.00 22.22 ? 270  THR B N   1 
ATOM   6817  C  CA  . THR B 1 278 ? 56.203  -4.089  26.250  1.00 22.23 ? 270  THR B CA  1 
ATOM   6818  C  C   . THR B 1 278 ? 57.103  -3.093  26.979  1.00 24.21 ? 270  THR B C   1 
ATOM   6819  O  O   . THR B 1 278 ? 57.458  -2.048  26.417  1.00 24.00 ? 270  THR B O   1 
ATOM   6820  C  CB  . THR B 1 278 ? 54.726  -3.896  26.624  1.00 23.12 ? 270  THR B CB  1 
ATOM   6821  O  OG1 . THR B 1 278 ? 53.927  -4.797  25.846  1.00 20.81 ? 270  THR B OG1 1 
ATOM   6822  C  CG2 . THR B 1 278 ? 54.261  -2.467  26.362  1.00 21.12 ? 270  THR B CG2 1 
ATOM   6823  N  N   . ARG B 1 279 ? 57.489  -3.399  28.225  1.00 22.54 ? 271  ARG B N   1 
ATOM   6824  C  CA  . ARG B 1 279 ? 58.509  -2.609  28.912  1.00 23.23 ? 271  ARG B CA  1 
ATOM   6825  C  C   . ARG B 1 279 ? 59.778  -2.510  28.079  1.00 27.87 ? 271  ARG B C   1 
ATOM   6826  O  O   . ARG B 1 279 ? 60.346  -1.426  27.905  1.00 25.30 ? 271  ARG B O   1 
ATOM   6827  C  CB  . ARG B 1 279 ? 58.846  -3.224  30.273  1.00 22.95 ? 271  ARG B CB  1 
ATOM   6828  C  CG  . ARG B 1 279 ? 57.874  -2.855  31.373  1.00 22.00 ? 271  ARG B CG  1 
ATOM   6829  C  CD  . ARG B 1 279 ? 58.319  -3.320  32.766  1.00 21.92 ? 271  ARG B CD  1 
ATOM   6830  N  NE  . ARG B 1 279 ? 57.802  -2.380  33.753  1.00 23.32 ? 271  ARG B NE  1 
ATOM   6831  C  CZ  . ARG B 1 279 ? 56.530  -2.337  34.147  1.00 29.01 ? 271  ARG B CZ  1 
ATOM   6832  N  NH1 . ARG B 1 279 ? 55.655  -3.211  33.668  1.00 19.90 ? 271  ARG B NH1 1 
ATOM   6833  N  NH2 . ARG B 1 279 ? 56.125  -1.422  35.021  1.00 20.31 ? 271  ARG B NH2 1 
ATOM   6834  N  N   . LYS B 1 280 ? 60.244  -3.648  27.568  1.00 27.41 ? 272  LYS B N   1 
ATOM   6835  C  CA  . LYS B 1 280 ? 61.464  -3.656  26.764  1.00 27.82 ? 272  LYS B CA  1 
ATOM   6836  C  C   . LYS B 1 280 ? 61.254  -2.911  25.448  1.00 26.68 ? 272  LYS B C   1 
ATOM   6837  O  O   . LYS B 1 280 ? 62.097  -2.105  25.043  1.00 27.78 ? 272  LYS B O   1 
ATOM   6838  C  CB  . LYS B 1 280 ? 61.896  -5.104  26.528  1.00 26.77 ? 272  LYS B CB  1 
ATOM   6839  C  CG  . LYS B 1 280 ? 63.212  -5.311  25.776  1.00 35.28 ? 272  LYS B CG  1 
ATOM   6840  C  CD  . LYS B 1 280 ? 63.562  -6.800  25.741  1.00 32.87 ? 272  LYS B CD  1 
ATOM   6841  C  CE  . LYS B 1 280 ? 64.838  -7.077  24.963  1.00 38.48 ? 272  LYS B CE  1 
ATOM   6842  N  NZ  . LYS B 1 280 ? 65.180  -8.539  24.929  1.00 35.76 ? 272  LYS B NZ  1 
ATOM   6843  N  N   . HIS B 1 281 ? 60.121  -3.153  24.785  1.00 25.96 ? 273  HIS B N   1 
ATOM   6844  C  CA  . HIS B 1 281 ? 59.834  -2.519  23.499  1.00 28.28 ? 273  HIS B CA  1 
ATOM   6845  C  C   . HIS B 1 281 ? 59.740  -1.001  23.625  1.00 33.07 ? 273  HIS B C   1 
ATOM   6846  O  O   . HIS B 1 281 ? 60.189  -0.269  22.735  1.00 27.67 ? 273  HIS B O   1 
ATOM   6847  C  CB  . HIS B 1 281 ? 58.535  -3.101  22.926  1.00 32.42 ? 273  HIS B CB  1 
ATOM   6848  C  CG  . HIS B 1 281 ? 57.974  -2.336  21.767  1.00 30.24 ? 273  HIS B CG  1 
ATOM   6849  N  ND1 . HIS B 1 281 ? 58.635  -2.206  20.563  1.00 28.71 ? 273  HIS B ND1 1 
ATOM   6850  C  CD2 . HIS B 1 281 ? 56.802  -1.671  21.626  1.00 28.02 ? 273  HIS B CD2 1 
ATOM   6851  C  CE1 . HIS B 1 281 ? 57.900  -1.484  19.735  1.00 27.08 ? 273  HIS B CE1 1 
ATOM   6852  N  NE2 . HIS B 1 281 ? 56.783  -1.146  20.358  1.00 26.68 ? 273  HIS B NE2 1 
ATOM   6853  N  N   . LEU B 1 282 ? 59.161  -0.508  24.717  1.00 26.89 ? 274  LEU B N   1 
ATOM   6854  C  CA  . LEU B 1 282 ? 58.974  0.924   24.915  1.00 25.95 ? 274  LEU B CA  1 
ATOM   6855  C  C   . LEU B 1 282 ? 60.105  1.575   25.707  1.00 26.78 ? 274  LEU B C   1 
ATOM   6856  O  O   . LEU B 1 282 ? 60.055  2.786   25.943  1.00 33.64 ? 274  LEU B O   1 
ATOM   6857  C  CB  . LEU B 1 282 ? 57.634  1.190   25.619  1.00 24.64 ? 274  LEU B CB  1 
ATOM   6858  C  CG  . LEU B 1 282 ? 56.377  0.762   24.852  1.00 23.86 ? 274  LEU B CG  1 
ATOM   6859  C  CD1 . LEU B 1 282 ? 55.075  1.273   25.510  1.00 22.75 ? 274  LEU B CD1 1 
ATOM   6860  C  CD2 . LEU B 1 282 ? 56.445  1.216   23.393  1.00 24.68 ? 274  LEU B CD2 1 
ATOM   6861  N  N   . GLY B 1 283 ? 61.112  0.816   26.126  1.00 31.57 ? 275  GLY B N   1 
ATOM   6862  C  CA  . GLY B 1 283 ? 62.200  1.396   26.894  1.00 28.13 ? 275  GLY B CA  1 
ATOM   6863  C  C   . GLY B 1 283 ? 61.802  1.862   28.278  1.00 27.40 ? 275  GLY B C   1 
ATOM   6864  O  O   . GLY B 1 283 ? 62.342  2.855   28.771  1.00 28.95 ? 275  GLY B O   1 
ATOM   6865  N  N   . TRP B 1 284 ? 60.873  1.163   28.920  1.00 26.13 ? 276  TRP B N   1 
ATOM   6866  C  CA  . TRP B 1 284 ? 60.345  1.521   30.230  1.00 25.37 ? 276  TRP B CA  1 
ATOM   6867  C  C   . TRP B 1 284 ? 60.932  0.548   31.246  1.00 29.21 ? 276  TRP B C   1 
ATOM   6868  O  O   . TRP B 1 284 ? 60.569  -0.633  31.261  1.00 29.10 ? 276  TRP B O   1 
ATOM   6869  C  CB  . TRP B 1 284 ? 58.815  1.459   30.208  1.00 25.49 ? 276  TRP B CB  1 
ATOM   6870  C  CG  . TRP B 1 284 ? 58.108  1.949   31.433  1.00 26.15 ? 276  TRP B CG  1 
ATOM   6871  C  CD1 . TRP B 1 284 ? 57.731  1.208   32.523  1.00 24.52 ? 276  TRP B CD1 1 
ATOM   6872  C  CD2 . TRP B 1 284 ? 57.640  3.282   31.676  1.00 30.51 ? 276  TRP B CD2 1 
ATOM   6873  N  NE1 . TRP B 1 284 ? 57.087  2.008   33.436  1.00 22.09 ? 276  TRP B NE1 1 
ATOM   6874  C  CE2 . TRP B 1 284 ? 57.020  3.283   32.941  1.00 22.51 ? 276  TRP B CE2 1 
ATOM   6875  C  CE3 . TRP B 1 284 ? 57.706  4.479   30.955  1.00 29.38 ? 276  TRP B CE3 1 
ATOM   6876  C  CZ2 . TRP B 1 284 ? 56.469  4.434   33.500  1.00 24.59 ? 276  TRP B CZ2 1 
ATOM   6877  C  CZ3 . TRP B 1 284 ? 57.151  5.617   31.508  1.00 26.26 ? 276  TRP B CZ3 1 
ATOM   6878  C  CH2 . TRP B 1 284 ? 56.541  5.588   32.768  1.00 24.11 ? 276  TRP B CH2 1 
ATOM   6879  N  N   . ALA B 1 285 ? 61.839  1.036   32.091  1.00 26.03 ? 277  ALA B N   1 
ATOM   6880  C  CA  . ALA B 1 285 ? 62.499  0.184   33.072  1.00 26.13 ? 277  ALA B CA  1 
ATOM   6881  C  C   . ALA B 1 285 ? 61.854  0.234   34.448  1.00 25.29 ? 277  ALA B C   1 
ATOM   6882  O  O   . ALA B 1 285 ? 62.203  -0.589  35.301  1.00 28.08 ? 277  ALA B O   1 
ATOM   6883  C  CB  . ALA B 1 285 ? 63.981  0.560   33.202  1.00 30.18 ? 277  ALA B CB  1 
ATOM   6884  N  N   . TYR B 1 286 ? 60.924  1.156   34.681  1.00 24.73 ? 278  TYR B N   1 
ATOM   6885  C  CA  . TYR B 1 286 ? 60.382  1.349   36.023  1.00 24.12 ? 278  TYR B CA  1 
ATOM   6886  C  C   . TYR B 1 286 ? 59.518  0.160   36.422  1.00 23.02 ? 278  TYR B C   1 
ATOM   6887  O  O   . TYR B 1 286 ? 58.638  -0.248  35.653  1.00 22.32 ? 278  TYR B O   1 
ATOM   6888  C  CB  . TYR B 1 286 ? 59.552  2.634   36.091  1.00 27.63 ? 278  TYR B CB  1 
ATOM   6889  C  CG  . TYR B 1 286 ? 60.332  3.842   35.651  1.00 25.18 ? 278  TYR B CG  1 
ATOM   6890  C  CD1 . TYR B 1 286 ? 61.428  4.280   36.385  1.00 26.00 ? 278  TYR B CD1 1 
ATOM   6891  C  CD2 . TYR B 1 286 ? 59.995  4.531   34.488  1.00 25.10 ? 278  TYR B CD2 1 
ATOM   6892  C  CE1 . TYR B 1 286 ? 62.165  5.379   35.989  1.00 31.73 ? 278  TYR B CE1 1 
ATOM   6893  C  CE2 . TYR B 1 286 ? 60.733  5.634   34.079  1.00 26.26 ? 278  TYR B CE2 1 
ATOM   6894  C  CZ  . TYR B 1 286 ? 61.821  6.047   34.836  1.00 31.14 ? 278  TYR B CZ  1 
ATOM   6895  O  OH  . TYR B 1 286 ? 62.566  7.136   34.459  1.00 33.07 ? 278  TYR B OH  1 
ATOM   6896  N  N   . PRO B 1 287 ? 59.733  -0.417  37.602  1.00 25.39 ? 279  PRO B N   1 
ATOM   6897  C  CA  . PRO B 1 287 ? 58.856  -1.493  38.065  1.00 21.94 ? 279  PRO B CA  1 
ATOM   6898  C  C   . PRO B 1 287 ? 57.425  -0.996  38.216  1.00 20.98 ? 279  PRO B C   1 
ATOM   6899  O  O   . PRO B 1 287 ? 57.158  0.204   38.276  1.00 21.07 ? 279  PRO B O   1 
ATOM   6900  C  CB  . PRO B 1 287 ? 59.455  -1.909  39.415  1.00 23.17 ? 279  PRO B CB  1 
ATOM   6901  C  CG  . PRO B 1 287 ? 60.605  -0.945  39.691  1.00 27.35 ? 279  PRO B CG  1 
ATOM   6902  C  CD  . PRO B 1 287 ? 60.957  -0.276  38.415  1.00 30.48 ? 279  PRO B CD  1 
ATOM   6903  N  N   . ALA B 1 288 ? 56.501  -1.953  38.236  1.00 20.14 ? 280  ALA B N   1 
ATOM   6904  C  CA  . ALA B 1 288 ? 55.081  -1.641  38.335  1.00 20.46 ? 280  ALA B CA  1 
ATOM   6905  C  C   . ALA B 1 288 ? 54.820  -0.688  39.491  1.00 22.27 ? 280  ALA B C   1 
ATOM   6906  O  O   . ALA B 1 288 ? 55.354  -0.866  40.590  1.00 20.33 ? 280  ALA B O   1 
ATOM   6907  C  CB  . ALA B 1 288 ? 54.269  -2.926  38.519  1.00 18.53 ? 280  ALA B CB  1 
ATOM   6908  N  N   . PHE B 1 289 ? 54.021  0.344   39.209  1.00 18.92 ? 281  PHE B N   1 
ATOM   6909  C  CA  . PHE B 1 289 ? 53.536  1.360   40.137  1.00 19.77 ? 281  PHE B CA  1 
ATOM   6910  C  C   . PHE B 1 289 ? 54.624  2.309   40.605  1.00 20.87 ? 281  PHE B C   1 
ATOM   6911  O  O   . PHE B 1 289 ? 54.378  3.124   41.504  1.00 23.85 ? 281  PHE B O   1 
ATOM   6912  C  CB  . PHE B 1 289 ? 52.827  0.724   41.338  1.00 18.49 ? 281  PHE B CB  1 
ATOM   6913  C  CG  . PHE B 1 289 ? 51.704  -0.185  40.940  1.00 17.45 ? 281  PHE B CG  1 
ATOM   6914  C  CD1 . PHE B 1 289 ? 50.458  0.328   40.629  1.00 19.56 ? 281  PHE B CD1 1 
ATOM   6915  C  CD2 . PHE B 1 289 ? 51.906  -1.553  40.845  1.00 18.98 ? 281  PHE B CD2 1 
ATOM   6916  C  CE1 . PHE B 1 289 ? 49.418  -0.520  40.247  1.00 21.00 ? 281  PHE B CE1 1 
ATOM   6917  C  CE2 . PHE B 1 289 ? 50.881  -2.401  40.461  1.00 17.07 ? 281  PHE B CE2 1 
ATOM   6918  C  CZ  . PHE B 1 289 ? 49.635  -1.881  40.156  1.00 18.10 ? 281  PHE B CZ  1 
ATOM   6919  N  N   . GLU B 1 290 ? 55.821  2.236   40.026  1.00 20.58 ? 282  GLU B N   1 
ATOM   6920  C  CA  . GLU B 1 290 ? 56.879  3.193   40.321  1.00 22.54 ? 282  GLU B CA  1 
ATOM   6921  C  C   . GLU B 1 290 ? 56.975  4.201   39.181  1.00 27.74 ? 282  GLU B C   1 
ATOM   6922  O  O   . GLU B 1 290 ? 57.152  3.819   38.016  1.00 30.32 ? 282  GLU B O   1 
ATOM   6923  C  CB  . GLU B 1 290 ? 58.206  2.475   40.555  1.00 27.16 ? 282  GLU B CB  1 
ATOM   6924  C  CG  . GLU B 1 290 ? 58.144  1.607   41.799  1.00 30.33 ? 282  GLU B CG  1 
ATOM   6925  C  CD  . GLU B 1 290 ? 59.482  1.031   42.202  1.00 36.44 ? 282  GLU B CD  1 
ATOM   6926  O  OE1 . GLU B 1 290 ? 60.517  1.523   41.703  1.00 40.98 ? 282  GLU B OE1 1 
ATOM   6927  O  OE2 . GLU B 1 290 ? 59.490  0.084   43.018  1.00 35.46 ? 282  GLU B OE2 1 
ATOM   6928  N  N   . ILE B 1 291 ? 56.827  5.475   39.517  1.00 23.55 ? 283  ILE B N   1 
ATOM   6929  C  CA  . ILE B 1 291 ? 56.823  6.566   38.549  1.00 27.56 ? 283  ILE B CA  1 
ATOM   6930  C  C   . ILE B 1 291 ? 57.882  7.569   38.982  1.00 29.44 ? 283  ILE B C   1 
ATOM   6931  O  O   . ILE B 1 291 ? 57.853  8.023   40.127  1.00 28.09 ? 283  ILE B O   1 
ATOM   6932  C  CB  . ILE B 1 291 ? 55.453  7.258   38.448  1.00 21.96 ? 283  ILE B CB  1 
ATOM   6933  C  CG1 . ILE B 1 291 ? 54.367  6.246   38.069  1.00 20.93 ? 283  ILE B CG1 1 
ATOM   6934  C  CG2 . ILE B 1 291 ? 55.526  8.426   37.463  1.00 26.77 ? 283  ILE B CG2 1 
ATOM   6935  C  CD1 . ILE B 1 291 ? 52.957  6.788   38.260  1.00 19.99 ? 283  ILE B CD1 1 
ATOM   6936  N  N   . PRO B 1 292 ? 58.821  7.941   38.114  1.00 29.34 ? 284  PRO B N   1 
ATOM   6937  C  CA  . PRO B 1 292 ? 59.862  8.893   38.517  1.00 30.76 ? 284  PRO B CA  1 
ATOM   6938  C  C   . PRO B 1 292 ? 59.288  10.278  38.778  1.00 33.45 ? 284  PRO B C   1 
ATOM   6939  O  O   . PRO B 1 292 ? 58.266  10.675  38.211  1.00 30.51 ? 284  PRO B O   1 
ATOM   6940  C  CB  . PRO B 1 292 ? 60.818  8.904   37.317  1.00 31.92 ? 284  PRO B CB  1 
ATOM   6941  C  CG  . PRO B 1 292 ? 59.942  8.530   36.156  1.00 35.44 ? 284  PRO B CG  1 
ATOM   6942  C  CD  . PRO B 1 292 ? 58.937  7.552   36.698  1.00 27.14 ? 284  PRO B CD  1 
ATOM   6943  N  N   . GLN B 1 293 ? 59.976  11.022  39.647  1.00 31.11 ? 285  GLN B N   1 
ATOM   6944  C  CA  . GLN B 1 293 ? 59.460  12.313  40.091  1.00 35.31 ? 285  GLN B CA  1 
ATOM   6945  C  C   . GLN B 1 293 ? 59.226  13.256  38.920  1.00 38.72 ? 285  GLN B C   1 
ATOM   6946  O  O   . GLN B 1 293 ? 58.270  14.039  38.934  1.00 35.27 ? 285  GLN B O   1 
ATOM   6947  C  CB  . GLN B 1 293 ? 60.423  12.948  41.101  1.00 34.52 ? 285  GLN B CB  1 
ATOM   6948  C  CG  . GLN B 1 293 ? 59.833  14.131  41.864  1.00 38.26 ? 285  GLN B CG  1 
ATOM   6949  C  CD  . GLN B 1 293 ? 58.616  13.739  42.698  1.00 43.02 ? 285  GLN B CD  1 
ATOM   6950  O  OE1 . GLN B 1 293 ? 58.638  12.734  43.411  1.00 47.99 ? 285  GLN B OE1 1 
ATOM   6951  N  NE2 . GLN B 1 293 ? 57.547  14.531  42.606  1.00 38.09 ? 285  GLN B NE2 1 
ATOM   6952  N  N   . GLU B 1 294 ? 60.077  13.180  37.895  1.00 37.87 ? 286  GLU B N   1 
ATOM   6953  C  CA  . GLU B 1 294 ? 59.979  14.086  36.756  1.00 39.11 ? 286  GLU B CA  1 
ATOM   6954  C  C   . GLU B 1 294 ? 58.698  13.866  35.955  1.00 29.34 ? 286  GLU B C   1 
ATOM   6955  O  O   . GLU B 1 294 ? 58.132  14.825  35.420  1.00 30.03 ? 286  GLU B O   1 
ATOM   6956  C  CB  . GLU B 1 294 ? 61.230  13.923  35.885  1.00 49.41 ? 286  GLU B CB  1 
ATOM   6957  C  CG  . GLU B 1 294 ? 61.024  13.902  34.379  1.00 57.40 ? 286  GLU B CG  1 
ATOM   6958  C  CD  . GLU B 1 294 ? 62.318  13.586  33.629  1.00 64.97 ? 286  GLU B CD  1 
ATOM   6959  O  OE1 . GLU B 1 294 ? 62.246  13.169  32.455  1.00 66.06 ? 286  GLU B OE1 1 
ATOM   6960  O  OE2 . GLU B 1 294 ? 63.411  13.752  34.218  1.00 68.55 ? 286  GLU B OE2 1 
ATOM   6961  N  N   . ILE B 1 295 ? 58.220  12.625  35.853  1.00 28.89 ? 287  ILE B N   1 
ATOM   6962  C  CA  . ILE B 1 295 ? 56.949  12.400  35.171  1.00 28.73 ? 287  ILE B CA  1 
ATOM   6963  C  C   . ILE B 1 295 ? 55.798  12.920  36.025  1.00 28.35 ? 287  ILE B C   1 
ATOM   6964  O  O   . ILE B 1 295 ? 54.845  13.522  35.512  1.00 24.45 ? 287  ILE B O   1 
ATOM   6965  C  CB  . ILE B 1 295 ? 56.785  10.911  34.811  1.00 31.22 ? 287  ILE B CB  1 
ATOM   6966  C  CG1 . ILE B 1 295 ? 57.807  10.519  33.742  1.00 31.55 ? 287  ILE B CG1 1 
ATOM   6967  C  CG2 . ILE B 1 295 ? 55.365  10.619  34.309  1.00 28.29 ? 287  ILE B CG2 1 
ATOM   6968  C  CD1 . ILE B 1 295 ? 57.673  9.096   33.259  1.00 31.46 ? 287  ILE B CD1 1 
ATOM   6969  N  N   . TYR B 1 296 ? 55.880  12.716  37.342  1.00 25.64 ? 288  TYR B N   1 
ATOM   6970  C  CA  . TYR B 1 296 ? 54.897  13.307  38.245  1.00 24.14 ? 288  TYR B CA  1 
ATOM   6971  C  C   . TYR B 1 296 ? 54.878  14.825  38.106  1.00 24.91 ? 288  TYR B C   1 
ATOM   6972  O  O   . TYR B 1 296 ? 53.810  15.438  38.010  1.00 26.04 ? 288  TYR B O   1 
ATOM   6973  C  CB  . TYR B 1 296 ? 55.199  12.906  39.690  1.00 28.37 ? 288  TYR B CB  1 
ATOM   6974  C  CG  . TYR B 1 296 ? 54.610  11.591  40.135  1.00 26.61 ? 288  TYR B CG  1 
ATOM   6975  C  CD1 . TYR B 1 296 ? 53.274  11.286  39.903  1.00 24.96 ? 288  TYR B CD1 1 
ATOM   6976  C  CD2 . TYR B 1 296 ? 55.391  10.653  40.802  1.00 26.92 ? 288  TYR B CD2 1 
ATOM   6977  C  CE1 . TYR B 1 296 ? 52.736  10.081  40.321  1.00 21.00 ? 288  TYR B CE1 1 
ATOM   6978  C  CE2 . TYR B 1 296 ? 54.861  9.446   41.219  1.00 26.74 ? 288  TYR B CE2 1 
ATOM   6979  C  CZ  . TYR B 1 296 ? 53.533  9.168   40.976  1.00 23.03 ? 288  TYR B CZ  1 
ATOM   6980  O  OH  . TYR B 1 296 ? 53.004  7.975   41.396  1.00 20.68 ? 288  TYR B OH  1 
ATOM   6981  N  N   . ASP B 1 297 ? 56.060  15.452  38.075  1.00 26.27 ? 289  ASP B N   1 
ATOM   6982  C  CA  . ASP B 1 297 ? 56.112  16.910  37.975  1.00 31.40 ? 289  ASP B CA  1 
ATOM   6983  C  C   . ASP B 1 297 ? 55.536  17.409  36.652  1.00 30.89 ? 289  ASP B C   1 
ATOM   6984  O  O   . ASP B 1 297 ? 54.902  18.471  36.614  1.00 32.86 ? 289  ASP B O   1 
ATOM   6985  C  CB  . ASP B 1 297 ? 57.551  17.409  38.152  1.00 35.70 ? 289  ASP B CB  1 
ATOM   6986  C  CG  . ASP B 1 297 ? 58.117  17.116  39.537  1.00 38.17 ? 289  ASP B CG  1 
ATOM   6987  O  OD1 . ASP B 1 297 ? 57.345  16.902  40.495  1.00 39.12 ? 289  ASP B OD1 1 
ATOM   6988  O  OD2 . ASP B 1 297 ? 59.356  17.114  39.670  1.00 45.60 ? 289  ASP B OD2 1 
ATOM   6989  N  N   . ALA B 1 298 ? 55.724  16.658  35.563  1.00 30.80 ? 290  ALA B N   1 
ATOM   6990  C  CA  . ALA B 1 298 ? 55.136  17.062  34.286  1.00 26.77 ? 290  ALA B CA  1 
ATOM   6991  C  C   . ALA B 1 298 ? 53.617  16.938  34.280  1.00 28.12 ? 290  ALA B C   1 
ATOM   6992  O  O   . ALA B 1 298 ? 52.940  17.728  33.615  1.00 27.68 ? 290  ALA B O   1 
ATOM   6993  C  CB  . ALA B 1 298 ? 55.718  16.236  33.144  1.00 33.22 ? 290  ALA B CB  1 
ATOM   6994  N  N   . TRP B 1 299 ? 53.063  15.955  34.991  1.00 25.22 ? 291  TRP B N   1 
ATOM   6995  C  CA  . TRP B 1 299 ? 51.619  15.729  34.979  1.00 23.02 ? 291  TRP B CA  1 
ATOM   6996  C  C   . TRP B 1 299 ? 50.871  16.518  36.037  1.00 22.73 ? 291  TRP B C   1 
ATOM   6997  O  O   . TRP B 1 299 ? 49.669  16.746  35.875  1.00 21.97 ? 291  TRP B O   1 
ATOM   6998  C  CB  . TRP B 1 299 ? 51.285  14.250  35.201  1.00 22.02 ? 291  TRP B CB  1 
ATOM   6999  C  CG  . TRP B 1 299 ? 51.144  13.441  33.956  1.00 21.72 ? 291  TRP B CG  1 
ATOM   7000  C  CD1 . TRP B 1 299 ? 52.051  12.561  33.447  1.00 26.19 ? 291  TRP B CD1 1 
ATOM   7001  C  CD2 . TRP B 1 299 ? 50.022  13.418  33.071  1.00 22.31 ? 291  TRP B CD2 1 
ATOM   7002  N  NE1 . TRP B 1 299 ? 51.566  11.995  32.293  1.00 27.18 ? 291  TRP B NE1 1 
ATOM   7003  C  CE2 . TRP B 1 299 ? 50.322  12.504  32.041  1.00 22.11 ? 291  TRP B CE2 1 
ATOM   7004  C  CE3 . TRP B 1 299 ? 48.790  14.080  33.049  1.00 20.48 ? 291  TRP B CE3 1 
ATOM   7005  C  CZ2 . TRP B 1 299 ? 49.436  12.233  31.005  1.00 25.97 ? 291  TRP B CZ2 1 
ATOM   7006  C  CZ3 . TRP B 1 299 ? 47.918  13.814  32.018  1.00 22.16 ? 291  TRP B CZ3 1 
ATOM   7007  C  CH2 . TRP B 1 299 ? 48.243  12.904  31.007  1.00 21.89 ? 291  TRP B CH2 1 
ATOM   7008  N  N   . ASN B 1 300 ? 51.532  16.913  37.117  1.00 23.36 ? 292  ASN B N   1 
ATOM   7009  C  CA  . ASN B 1 300 ? 50.816  17.422  38.279  1.00 26.99 ? 292  ASN B CA  1 
ATOM   7010  C  C   . ASN B 1 300 ? 50.097  18.729  37.953  1.00 27.99 ? 292  ASN B C   1 
ATOM   7011  O  O   . ASN B 1 300 ? 50.684  19.648  37.372  1.00 25.46 ? 292  ASN B O   1 
ATOM   7012  C  CB  . ASN B 1 300 ? 51.783  17.620  39.443  1.00 26.15 ? 292  ASN B CB  1 
ATOM   7013  C  CG  . ASN B 1 300 ? 51.066  17.993  40.710  1.00 30.20 ? 292  ASN B CG  1 
ATOM   7014  O  OD1 . ASN B 1 300 ? 50.726  19.146  40.904  1.00 28.12 ? 292  ASN B OD1 1 
ATOM   7015  N  ND2 . ASN B 1 300 ? 50.787  17.009  41.559  1.00 29.45 ? 292  ASN B ND2 1 
ATOM   7016  N  N   . ALA B 1 301 ? 48.815  18.811  38.314  1.00 26.44 ? 293  ALA B N   1 
ATOM   7017  C  CA  . ALA B 1 301 ? 47.995  19.974  37.999  1.00 22.33 ? 293  ALA B CA  1 
ATOM   7018  C  C   . ALA B 1 301 ? 47.675  20.825  39.220  1.00 23.62 ? 293  ALA B C   1 
ATOM   7019  O  O   . ALA B 1 301 ? 46.771  21.669  39.156  1.00 23.20 ? 293  ALA B O   1 
ATOM   7020  C  CB  . ALA B 1 301 ? 46.698  19.531  37.316  1.00 21.22 ? 293  ALA B CB  1 
ATOM   7021  N  N   . LYS B 1 302 ? 48.401  20.640  40.323  1.00 22.99 ? 294  LYS B N   1 
ATOM   7022  C  CA  A LYS B 1 302 ? 48.113  21.401  41.534  0.52 23.28 ? 294  LYS B CA  1 
ATOM   7023  C  CA  B LYS B 1 302 ? 48.107  21.402  41.533  0.48 23.28 ? 294  LYS B CA  1 
ATOM   7024  C  C   . LYS B 1 302 ? 48.334  22.892  41.313  1.00 24.32 ? 294  LYS B C   1 
ATOM   7025  O  O   . LYS B 1 302 ? 47.492  23.718  41.685  1.00 24.58 ? 294  LYS B O   1 
ATOM   7026  C  CB  A LYS B 1 302 ? 48.977  20.893  42.687  0.52 27.46 ? 294  LYS B CB  1 
ATOM   7027  C  CB  B LYS B 1 302 ? 48.955  20.896  42.700  0.48 27.46 ? 294  LYS B CB  1 
ATOM   7028  C  CG  A LYS B 1 302 ? 48.904  21.722  43.951  0.52 27.79 ? 294  LYS B CG  1 
ATOM   7029  C  CG  B LYS B 1 302 ? 48.537  19.535  43.230  0.48 28.14 ? 294  LYS B CG  1 
ATOM   7030  C  CD  A LYS B 1 302 ? 50.010  21.318  44.919  0.52 29.02 ? 294  LYS B CD  1 
ATOM   7031  C  CD  B LYS B 1 302 ? 47.589  19.674  44.402  0.48 29.91 ? 294  LYS B CD  1 
ATOM   7032  C  CE  A LYS B 1 302 ? 49.925  22.103  46.210  0.52 26.10 ? 294  LYS B CE  1 
ATOM   7033  C  CE  B LYS B 1 302 ? 46.903  18.357  44.723  0.48 24.56 ? 294  LYS B CE  1 
ATOM   7034  N  NZ  A LYS B 1 302 ? 50.957  21.656  47.185  0.52 26.94 ? 294  LYS B NZ  1 
ATOM   7035  N  NZ  B LYS B 1 302 ? 47.356  17.776  46.016  0.48 26.65 ? 294  LYS B NZ  1 
ATOM   7036  N  N   . GLU B 1 303 ? 49.468  23.255  40.700  1.00 25.43 ? 295  GLU B N   1 
ATOM   7037  C  CA  . GLU B 1 303 ? 49.800  24.668  40.549  1.00 26.57 ? 295  GLU B CA  1 
ATOM   7038  C  C   . GLU B 1 303 ? 48.850  25.368  39.585  1.00 29.07 ? 295  GLU B C   1 
ATOM   7039  O  O   . GLU B 1 303 ? 48.286  26.416  39.916  1.00 26.53 ? 295  GLU B O   1 
ATOM   7040  C  CB  . GLU B 1 303 ? 51.250  24.836  40.092  1.00 28.10 ? 295  GLU B CB  1 
ATOM   7041  C  CG  . GLU B 1 303 ? 51.607  26.289  39.824  1.00 34.59 ? 295  GLU B CG  1 
ATOM   7042  C  CD  . GLU B 1 303 ? 53.073  26.503  39.454  1.00 44.69 ? 295  GLU B CD  1 
ATOM   7043  O  OE1 . GLU B 1 303 ? 53.882  25.554  39.578  1.00 43.12 ? 295  GLU B OE1 1 
ATOM   7044  O  OE2 . GLU B 1 303 ? 53.409  27.637  39.039  1.00 46.85 ? 295  GLU B OE2 1 
ATOM   7045  N  N   . LYS B 1 304 ? 48.669  24.818  38.378  1.00 26.67 ? 296  LYS B N   1 
ATOM   7046  C  CA  . LYS B 1 304 ? 47.720  25.433  37.453  1.00 28.70 ? 296  LYS B CA  1 
ATOM   7047  C  C   . LYS B 1 304 ? 46.305  25.387  38.011  1.00 26.94 ? 296  LYS B C   1 
ATOM   7048  O  O   . LYS B 1 304 ? 45.520  26.312  37.785  1.00 25.03 ? 296  LYS B O   1 
ATOM   7049  C  CB  . LYS B 1 304 ? 47.776  24.754  36.081  1.00 25.14 ? 296  LYS B CB  1 
ATOM   7050  N  N   . GLY B 1 305 ? 45.974  24.337  38.769  1.00 24.94 ? 297  GLY B N   1 
ATOM   7051  C  CA  . GLY B 1 305 ? 44.625  24.211  39.296  1.00 22.44 ? 297  GLY B CA  1 
ATOM   7052  C  C   . GLY B 1 305 ? 44.313  25.238  40.370  1.00 22.89 ? 297  GLY B C   1 
ATOM   7053  O  O   . GLY B 1 305 ? 43.229  25.823  40.388  1.00 27.56 ? 297  GLY B O   1 
ATOM   7054  N  N   . ALA B 1 306 ? 45.249  25.456  41.293  1.00 23.71 ? 298  ALA B N   1 
ATOM   7055  C  CA  . ALA B 1 306 ? 45.036  26.471  42.320  1.00 24.30 ? 298  ALA B CA  1 
ATOM   7056  C  C   . ALA B 1 306 ? 44.888  27.855  41.703  1.00 25.06 ? 298  ALA B C   1 
ATOM   7057  O  O   . ALA B 1 306 ? 44.066  28.658  42.155  1.00 25.85 ? 298  ALA B O   1 
ATOM   7058  C  CB  . ALA B 1 306 ? 46.193  26.459  43.322  1.00 29.57 ? 298  ALA B CB  1 
ATOM   7059  N  N   . LYS B 1 307 ? 45.687  28.153  40.676  1.00 25.81 ? 299  LYS B N   1 
ATOM   7060  C  CA  . LYS B 1 307 ? 45.590  29.438  39.989  1.00 26.58 ? 299  LYS B CA  1 
ATOM   7061  C  C   . LYS B 1 307 ? 44.253  29.579  39.274  1.00 27.09 ? 299  LYS B C   1 
ATOM   7062  O  O   . LYS B 1 307 ? 43.621  30.641  39.317  1.00 29.07 ? 299  LYS B O   1 
ATOM   7063  C  CB  . LYS B 1 307 ? 46.730  29.577  38.982  1.00 27.84 ? 299  LYS B CB  1 
ATOM   7064  C  CG  . LYS B 1 307 ? 48.129  29.719  39.578  1.00 33.04 ? 299  LYS B CG  1 
ATOM   7065  C  CD  . LYS B 1 307 ? 49.185  29.389  38.522  1.00 33.95 ? 299  LYS B CD  1 
ATOM   7066  C  CE  . LYS B 1 307 ? 50.572  29.915  38.912  1.00 39.19 ? 299  LYS B CE  1 
ATOM   7067  N  NZ  . LYS B 1 307 ? 51.611  29.712  37.851  1.00 35.31 ? 299  LYS B NZ  1 
ATOM   7068  N  N   . LEU B 1 308 ? 43.824  28.519  38.595  1.00 24.64 ? 300  LEU B N   1 
ATOM   7069  C  CA  . LEU B 1 308 ? 42.555  28.538  37.874  1.00 29.34 ? 300  LEU B CA  1 
ATOM   7070  C  C   . LEU B 1 308 ? 41.394  28.890  38.798  1.00 23.27 ? 300  LEU B C   1 
ATOM   7071  O  O   . LEU B 1 308 ? 40.558  29.742  38.473  1.00 23.31 ? 300  LEU B O   1 
ATOM   7072  C  CB  . LEU B 1 308 ? 42.327  27.175  37.228  1.00 22.77 ? 300  LEU B CB  1 
ATOM   7073  C  CG  . LEU B 1 308 ? 40.952  27.017  36.598  1.00 21.84 ? 300  LEU B CG  1 
ATOM   7074  C  CD1 . LEU B 1 308 ? 40.906  27.803  35.271  1.00 22.38 ? 300  LEU B CD1 1 
ATOM   7075  C  CD2 . LEU B 1 308 ? 40.660  25.550  36.414  1.00 22.07 ? 300  LEU B CD2 1 
ATOM   7076  N  N   . GLU B 1 309 ? 41.329  28.240  39.962  1.00 25.66 ? 301  GLU B N   1 
ATOM   7077  C  CA  . GLU B 1 309 ? 40.250  28.514  40.905  1.00 22.56 ? 301  GLU B CA  1 
ATOM   7078  C  C   . GLU B 1 309 ? 40.424  29.878  41.569  1.00 23.48 ? 301  GLU B C   1 
ATOM   7079  O  O   . GLU B 1 309 ? 39.436  30.585  41.809  1.00 23.39 ? 301  GLU B O   1 
ATOM   7080  C  CB  . GLU B 1 309 ? 40.171  27.392  41.945  1.00 21.78 ? 301  GLU B CB  1 
ATOM   7081  C  CG  . GLU B 1 309 ? 39.059  27.558  42.967  1.00 21.39 ? 301  GLU B CG  1 
ATOM   7082  C  CD  . GLU B 1 309 ? 38.658  26.246  43.635  1.00 24.30 ? 301  GLU B CD  1 
ATOM   7083  O  OE1 . GLU B 1 309 ? 39.197  25.183  43.260  1.00 27.99 ? 301  GLU B OE1 1 
ATOM   7084  O  OE2 . GLU B 1 309 ? 37.797  26.272  44.533  1.00 26.87 ? 301  GLU B OE2 1 
ATOM   7085  N  N   . ALA B 1 310 ? 41.669  30.276  41.858  1.00 25.36 ? 302  ALA B N   1 
ATOM   7086  C  CA  . ALA B 1 310 ? 41.906  31.618  42.382  1.00 28.03 ? 302  ALA B CA  1 
ATOM   7087  C  C   . ALA B 1 310 ? 41.379  32.680  41.425  1.00 26.04 ? 302  ALA B C   1 
ATOM   7088  O  O   . ALA B 1 310 ? 40.732  33.645  41.850  1.00 30.10 ? 302  ALA B O   1 
ATOM   7089  C  CB  . ALA B 1 310 ? 43.398  31.833  42.650  1.00 29.68 ? 302  ALA B CB  1 
ATOM   7090  N  N   . GLY B 1 311 ? 41.635  32.513  40.126  1.00 28.34 ? 303  GLY B N   1 
ATOM   7091  C  CA  . GLY B 1 311 ? 41.102  33.451  39.148  1.00 26.30 ? 303  GLY B CA  1 
ATOM   7092  C  C   . GLY B 1 311 ? 39.584  33.486  39.130  1.00 27.91 ? 303  GLY B C   1 
ATOM   7093  O  O   . GLY B 1 311 ? 38.976  34.559  39.082  1.00 25.73 ? 303  GLY B O   1 
ATOM   7094  N  N   . TRP B 1 312 ? 38.948  32.310  39.166  1.00 25.47 ? 304  TRP B N   1 
ATOM   7095  C  CA  . TRP B 1 312 ? 37.488  32.274  39.185  1.00 23.22 ? 304  TRP B CA  1 
ATOM   7096  C  C   . TRP B 1 312 ? 36.936  32.914  40.454  1.00 28.67 ? 304  TRP B C   1 
ATOM   7097  O  O   . TRP B 1 312 ? 35.957  33.669  40.398  1.00 23.41 ? 304  TRP B O   1 
ATOM   7098  C  CB  . TRP B 1 312 ? 36.979  30.841  39.045  1.00 21.98 ? 304  TRP B CB  1 
ATOM   7099  C  CG  . TRP B 1 312 ? 35.487  30.805  38.898  1.00 21.19 ? 304  TRP B CG  1 
ATOM   7100  C  CD1 . TRP B 1 312 ? 34.774  30.889  37.738  1.00 20.87 ? 304  TRP B CD1 1 
ATOM   7101  C  CD2 . TRP B 1 312 ? 34.527  30.726  39.954  1.00 22.25 ? 304  TRP B CD2 1 
ATOM   7102  N  NE1 . TRP B 1 312 ? 33.430  30.851  38.005  1.00 23.81 ? 304  TRP B NE1 1 
ATOM   7103  C  CE2 . TRP B 1 312 ? 33.250  30.752  39.359  1.00 21.91 ? 304  TRP B CE2 1 
ATOM   7104  C  CE3 . TRP B 1 312 ? 34.623  30.625  41.348  1.00 23.57 ? 304  TRP B CE3 1 
ATOM   7105  C  CZ2 . TRP B 1 312 ? 32.077  30.679  40.107  1.00 21.54 ? 304  TRP B CZ2 1 
ATOM   7106  C  CZ3 . TRP B 1 312 ? 33.459  30.556  42.087  1.00 20.40 ? 304  TRP B CZ3 1 
ATOM   7107  C  CH2 . TRP B 1 312 ? 32.202  30.582  41.464  1.00 19.83 ? 304  TRP B CH2 1 
ATOM   7108  N  N   . ASN B 1 313 ? 37.560  32.632  41.606  1.00 27.00 ? 305  ASN B N   1 
ATOM   7109  C  CA  . ASN B 1 313 ? 37.131  33.238  42.867  1.00 28.32 ? 305  ASN B CA  1 
ATOM   7110  C  C   . ASN B 1 313 ? 37.190  34.758  42.802  1.00 26.47 ? 305  ASN B C   1 
ATOM   7111  O  O   . ASN B 1 313 ? 36.327  35.445  43.361  1.00 26.68 ? 305  ASN B O   1 
ATOM   7112  C  CB  . ASN B 1 313 ? 37.994  32.734  44.027  1.00 31.06 ? 305  ASN B CB  1 
ATOM   7113  C  CG  . ASN B 1 313 ? 37.571  31.361  44.526  1.00 33.35 ? 305  ASN B CG  1 
ATOM   7114  O  OD1 . ASN B 1 313 ? 36.424  30.956  44.369  1.00 26.41 ? 305  ASN B OD1 1 
ATOM   7115  N  ND2 . ASN B 1 313 ? 38.499  30.648  45.149  1.00 32.42 ? 305  ASN B ND2 1 
ATOM   7116  N  N   . GLU B 1 314 ? 38.214  35.305  42.143  1.00 28.55 ? 306  GLU B N   1 
ATOM   7117  C  CA  . GLU B 1 314 ? 38.305  36.754  42.015  1.00 30.14 ? 306  GLU B CA  1 
ATOM   7118  C  C   . GLU B 1 314 ? 37.160  37.297  41.169  1.00 31.65 ? 306  GLU B C   1 
ATOM   7119  O  O   . GLU B 1 314 ? 36.559  38.326  41.505  1.00 31.14 ? 306  GLU B O   1 
ATOM   7120  C  CB  . GLU B 1 314 ? 39.664  37.136  41.426  1.00 35.40 ? 306  GLU B CB  1 
ATOM   7121  C  CG  . GLU B 1 314 ? 40.822  36.894  42.380  1.00 35.52 ? 306  GLU B CG  1 
ATOM   7122  C  CD  . GLU B 1 314 ? 42.168  36.851  41.681  1.00 45.09 ? 306  GLU B CD  1 
ATOM   7123  O  OE1 . GLU B 1 314 ? 43.167  36.455  42.327  1.00 43.96 ? 306  GLU B OE1 1 
ATOM   7124  O  OE2 . GLU B 1 314 ? 42.227  37.203  40.485  1.00 45.84 ? 306  GLU B OE2 1 
ATOM   7125  N  N   . LEU B 1 315 ? 36.834  36.602  40.079  1.00 29.09 ? 307  LEU B N   1 
ATOM   7126  C  CA  . LEU B 1 315 ? 35.705  36.991  39.242  1.00 27.27 ? 307  LEU B CA  1 
ATOM   7127  C  C   . LEU B 1 315 ? 34.388  36.889  40.004  1.00 30.75 ? 307  LEU B C   1 
ATOM   7128  O  O   . LEU B 1 315 ? 33.523  37.763  39.880  1.00 25.05 ? 307  LEU B O   1 
ATOM   7129  C  CB  . LEU B 1 315 ? 35.665  36.106  37.994  1.00 24.88 ? 307  LEU B CB  1 
ATOM   7130  C  CG  . LEU B 1 315 ? 34.518  36.344  37.004  1.00 28.58 ? 307  LEU B CG  1 
ATOM   7131  C  CD1 . LEU B 1 315 ? 34.742  37.628  36.230  1.00 33.78 ? 307  LEU B CD1 1 
ATOM   7132  C  CD2 . LEU B 1 315 ? 34.343  35.157  36.066  1.00 23.50 ? 307  LEU B CD2 1 
ATOM   7133  N  N   . PHE B 1 316 ? 34.212  35.818  40.785  1.00 30.35 ? 308  PHE B N   1 
ATOM   7134  C  CA  . PHE B 1 316 ? 32.975  35.638  41.542  1.00 23.40 ? 308  PHE B CA  1 
ATOM   7135  C  C   . PHE B 1 316 ? 32.852  36.669  42.654  1.00 27.89 ? 308  PHE B C   1 
ATOM   7136  O  O   . PHE B 1 316 ? 31.736  37.056  43.014  1.00 26.16 ? 308  PHE B O   1 
ATOM   7137  C  CB  . PHE B 1 316 ? 32.909  34.217  42.117  1.00 25.10 ? 308  PHE B CB  1 
ATOM   7138  C  CG  . PHE B 1 316 ? 31.566  33.852  42.700  1.00 32.41 ? 308  PHE B CG  1 
ATOM   7139  C  CD1 . PHE B 1 316 ? 30.458  33.681  41.880  1.00 31.29 ? 308  PHE B CD1 1 
ATOM   7140  C  CD2 . PHE B 1 316 ? 31.411  33.672  44.066  1.00 32.52 ? 308  PHE B CD2 1 
ATOM   7141  C  CE1 . PHE B 1 316 ? 29.225  33.346  42.417  1.00 25.41 ? 308  PHE B CE1 1 
ATOM   7142  C  CE2 . PHE B 1 316 ? 30.181  33.340  44.604  1.00 25.52 ? 308  PHE B CE2 1 
ATOM   7143  C  CZ  . PHE B 1 316 ? 29.088  33.180  43.780  1.00 23.35 ? 308  PHE B CZ  1 
ATOM   7144  N  N   . ALA B 1 317 ? 33.983  37.119  43.208  1.00 29.52 ? 309  ALA B N   1 
ATOM   7145  C  CA  . ALA B 1 317 ? 33.953  38.211  44.174  1.00 32.19 ? 309  ALA B CA  1 
ATOM   7146  C  C   . ALA B 1 317 ? 33.440  39.493  43.528  1.00 31.82 ? 309  ALA B C   1 
ATOM   7147  O  O   . ALA B 1 317 ? 32.637  40.220  44.125  1.00 30.87 ? 309  ALA B O   1 
ATOM   7148  C  CB  . ALA B 1 317 ? 35.345  38.425  44.776  1.00 28.83 ? 309  ALA B CB  1 
ATOM   7149  N  N   . GLN B 1 318 ? 33.888  39.786  42.305  1.00 32.55 ? 310  GLN B N   1 
ATOM   7150  C  CA  . GLN B 1 318 ? 33.331  40.922  41.580  1.00 27.58 ? 310  GLN B CA  1 
ATOM   7151  C  C   . GLN B 1 318 ? 31.836  40.733  41.354  1.00 28.04 ? 310  GLN B C   1 
ATOM   7152  O  O   . GLN B 1 318 ? 31.049  41.672  41.528  1.00 30.22 ? 310  GLN B O   1 
ATOM   7153  C  CB  . GLN B 1 318 ? 34.068  41.117  40.251  1.00 37.99 ? 310  GLN B CB  1 
ATOM   7154  C  CG  . GLN B 1 318 ? 35.550  41.476  40.410  1.00 47.40 ? 310  GLN B CG  1 
ATOM   7155  C  CD  . GLN B 1 318 ? 36.251  41.755  39.085  1.00 53.44 ? 310  GLN B CD  1 
ATOM   7156  O  OE1 . GLN B 1 318 ? 36.418  40.860  38.256  1.00 53.99 ? 310  GLN B OE1 1 
ATOM   7157  N  NE2 . GLN B 1 318 ? 36.667  43.003  38.885  1.00 55.25 ? 310  GLN B NE2 1 
ATOM   7158  N  N   . TYR B 1 319 ? 31.432  39.510  40.994  1.00 28.48 ? 311  TYR B N   1 
ATOM   7159  C  CA  . TYR B 1 319 ? 30.024  39.193  40.772  1.00 26.75 ? 311  TYR B CA  1 
ATOM   7160  C  C   . TYR B 1 319 ? 29.211  39.358  42.048  1.00 26.02 ? 311  TYR B C   1 
ATOM   7161  O  O   . TYR B 1 319 ? 28.128  39.957  42.035  1.00 27.30 ? 311  TYR B O   1 
ATOM   7162  C  CB  . TYR B 1 319 ? 29.903  37.761  40.250  1.00 24.29 ? 311  TYR B CB  1 
ATOM   7163  C  CG  . TYR B 1 319 ? 28.508  37.320  39.863  1.00 26.56 ? 311  TYR B CG  1 
ATOM   7164  C  CD1 . TYR B 1 319 ? 27.626  36.812  40.811  1.00 23.17 ? 311  TYR B CD1 1 
ATOM   7165  C  CD2 . TYR B 1 319 ? 28.082  37.388  38.541  1.00 26.31 ? 311  TYR B CD2 1 
ATOM   7166  C  CE1 . TYR B 1 319 ? 26.359  36.384  40.453  1.00 26.35 ? 311  TYR B CE1 1 
ATOM   7167  C  CE2 . TYR B 1 319 ? 26.815  36.965  38.174  1.00 26.61 ? 311  TYR B CE2 1 
ATOM   7168  C  CZ  . TYR B 1 319 ? 25.959  36.462  39.132  1.00 25.46 ? 311  TYR B CZ  1 
ATOM   7169  O  OH  . TYR B 1 319 ? 24.700  36.043  38.768  1.00 20.93 ? 311  TYR B OH  1 
ATOM   7170  N  N   . GLN B 1 320 ? 29.712  38.813  43.160  1.00 30.87 ? 312  GLN B N   1 
ATOM   7171  C  CA  . GLN B 1 320 ? 28.982  38.884  44.423  1.00 31.85 ? 312  GLN B CA  1 
ATOM   7172  C  C   . GLN B 1 320 ? 28.818  40.322  44.889  1.00 30.49 ? 312  GLN B C   1 
ATOM   7173  O  O   . GLN B 1 320 ? 27.785  40.666  45.476  1.00 26.50 ? 312  GLN B O   1 
ATOM   7174  C  CB  . GLN B 1 320 ? 29.700  38.054  45.494  1.00 35.54 ? 312  GLN B CB  1 
ATOM   7175  C  CG  . GLN B 1 320 ? 28.867  37.751  46.750  1.00 41.88 ? 312  GLN B CG  1 
ATOM   7176  C  CD  . GLN B 1 320 ? 28.858  38.889  47.762  1.00 53.29 ? 312  GLN B CD  1 
ATOM   7177  O  OE1 . GLN B 1 320 ? 29.676  39.807  47.687  1.00 60.96 ? 312  GLN B OE1 1 
ATOM   7178  N  NE2 . GLN B 1 320 ? 27.930  38.833  48.714  1.00 50.23 ? 312  GLN B NE2 1 
ATOM   7179  N  N   . ALA B 1 321 ? 29.818  41.172  44.628  1.00 28.92 ? 313  ALA B N   1 
ATOM   7180  C  CA  . ALA B 1 321 ? 29.749  42.567  45.060  1.00 32.47 ? 313  ALA B CA  1 
ATOM   7181  C  C   . ALA B 1 321 ? 28.595  43.305  44.391  1.00 35.51 ? 313  ALA B C   1 
ATOM   7182  O  O   . ALA B 1 321 ? 27.932  44.137  45.022  1.00 41.12 ? 313  ALA B O   1 
ATOM   7183  C  CB  . ALA B 1 321 ? 31.073  43.274  44.769  1.00 31.80 ? 313  ALA B CB  1 
ATOM   7184  N  N   . LYS B 1 322 ? 28.336  43.019  43.117  1.00 29.68 ? 314  LYS B N   1 
ATOM   7185  C  CA  . LYS B 1 322 ? 27.285  43.726  42.399  1.00 27.10 ? 314  LYS B CA  1 
ATOM   7186  C  C   . LYS B 1 322 ? 25.963  42.975  42.373  1.00 33.29 ? 314  LYS B C   1 
ATOM   7187  O  O   . LYS B 1 322 ? 24.919  43.600  42.151  1.00 37.71 ? 314  LYS B O   1 
ATOM   7188  C  CB  . LYS B 1 322 ? 27.724  44.012  40.957  1.00 35.38 ? 314  LYS B CB  1 
ATOM   7189  N  N   . TYR B 1 323 ? 25.981  41.660  42.587  1.00 25.06 ? 315  TYR B N   1 
ATOM   7190  C  CA  . TYR B 1 323 ? 24.795  40.810  42.478  1.00 28.11 ? 315  TYR B CA  1 
ATOM   7191  C  C   . TYR B 1 323 ? 24.732  39.866  43.678  1.00 25.75 ? 315  TYR B C   1 
ATOM   7192  O  O   . TYR B 1 323 ? 24.814  38.643  43.525  1.00 22.78 ? 315  TYR B O   1 
ATOM   7193  C  CB  . TYR B 1 323 ? 24.812  40.029  41.161  1.00 28.33 ? 315  TYR B CB  1 
ATOM   7194  C  CG  . TYR B 1 323 ? 24.913  40.911  39.928  1.00 29.01 ? 315  TYR B CG  1 
ATOM   7195  C  CD1 . TYR B 1 323 ? 23.792  41.552  39.418  1.00 31.19 ? 315  TYR B CD1 1 
ATOM   7196  C  CD2 . TYR B 1 323 ? 26.130  41.113  39.288  1.00 32.17 ? 315  TYR B CD2 1 
ATOM   7197  C  CE1 . TYR B 1 323 ? 23.877  42.366  38.300  1.00 31.41 ? 315  TYR B CE1 1 
ATOM   7198  C  CE2 . TYR B 1 323 ? 26.225  41.924  38.170  1.00 33.53 ? 315  TYR B CE2 1 
ATOM   7199  C  CZ  . TYR B 1 323 ? 25.094  42.549  37.680  1.00 35.60 ? 315  TYR B CZ  1 
ATOM   7200  O  OH  . TYR B 1 323 ? 25.180  43.360  36.567  1.00 38.63 ? 315  TYR B OH  1 
ATOM   7201  N  N   . PRO B 1 324 ? 24.556  40.406  44.890  1.00 26.09 ? 316  PRO B N   1 
ATOM   7202  C  CA  . PRO B 1 324 ? 24.661  39.545  46.084  1.00 27.70 ? 316  PRO B CA  1 
ATOM   7203  C  C   . PRO B 1 324 ? 23.581  38.479  46.188  1.00 26.84 ? 316  PRO B C   1 
ATOM   7204  O  O   . PRO B 1 324 ? 23.878  37.348  46.596  1.00 26.30 ? 316  PRO B O   1 
ATOM   7205  C  CB  . PRO B 1 324 ? 24.582  40.554  47.238  1.00 29.09 ? 316  PRO B CB  1 
ATOM   7206  C  CG  . PRO B 1 324 ? 23.849  41.724  46.669  1.00 26.09 ? 316  PRO B CG  1 
ATOM   7207  C  CD  . PRO B 1 324 ? 24.320  41.817  45.251  1.00 29.33 ? 316  PRO B CD  1 
ATOM   7208  N  N   . ALA B 1 325 ? 22.331  38.803  45.855  1.00 27.33 ? 317  ALA B N   1 
ATOM   7209  C  CA  . ALA B 1 325 ? 21.274  37.801  45.942  1.00 25.10 ? 317  ALA B CA  1 
ATOM   7210  C  C   . ALA B 1 325 ? 21.499  36.679  44.933  1.00 26.69 ? 317  ALA B C   1 
ATOM   7211  O  O   . ALA B 1 325 ? 21.358  35.496  45.267  1.00 26.71 ? 317  ALA B O   1 
ATOM   7212  C  CB  . ALA B 1 325 ? 19.906  38.449  45.726  1.00 30.76 ? 317  ALA B CB  1 
ATOM   7213  N  N   . GLU B 1 326 ? 21.840  37.035  43.689  1.00 22.60 ? 318  GLU B N   1 
ATOM   7214  C  CA  . GLU B 1 326 ? 22.115  36.021  42.673  1.00 20.97 ? 318  GLU B CA  1 
ATOM   7215  C  C   . GLU B 1 326 ? 23.312  35.165  43.065  1.00 20.20 ? 318  GLU B C   1 
ATOM   7216  O  O   . GLU B 1 326 ? 23.326  33.950  42.830  1.00 19.48 ? 318  GLU B O   1 
ATOM   7217  C  CB  . GLU B 1 326 ? 22.362  36.687  41.317  1.00 22.32 ? 318  GLU B CB  1 
ATOM   7218  C  CG  . GLU B 1 326 ? 21.134  37.371  40.695  1.00 25.00 ? 318  GLU B CG  1 
ATOM   7219  C  CD  . GLU B 1 326 ? 20.912  38.783  41.211  1.00 36.47 ? 318  GLU B CD  1 
ATOM   7220  O  OE1 . GLU B 1 326 ? 21.676  39.243  42.094  1.00 37.42 ? 318  GLU B OE1 1 
ATOM   7221  O  OE2 . GLU B 1 326 ? 19.961  39.435  40.735  1.00 38.78 ? 318  GLU B OE2 1 
ATOM   7222  N  N   . ALA B 1 327 ? 24.336  35.785  43.655  1.00 24.97 ? 319  ALA B N   1 
ATOM   7223  C  CA  . ALA B 1 327 ? 25.530  35.038  44.035  1.00 23.47 ? 319  ALA B CA  1 
ATOM   7224  C  C   . ALA B 1 327 ? 25.218  34.007  45.112  1.00 22.71 ? 319  ALA B C   1 
ATOM   7225  O  O   . ALA B 1 327 ? 25.710  32.873  45.056  1.00 23.36 ? 319  ALA B O   1 
ATOM   7226  C  CB  . ALA B 1 327 ? 26.616  35.999  44.516  1.00 26.52 ? 319  ALA B CB  1 
ATOM   7227  N  N   . ALA B 1 328 ? 24.411  34.386  46.105  1.00 24.32 ? 320  ALA B N   1 
ATOM   7228  C  CA  . ALA B 1 328 ? 24.039  33.441  47.151  1.00 26.27 ? 320  ALA B CA  1 
ATOM   7229  C  C   . ALA B 1 328 ? 23.189  32.306  46.590  1.00 19.52 ? 320  ALA B C   1 
ATOM   7230  O  O   . ALA B 1 328 ? 23.306  31.159  47.032  1.00 19.23 ? 320  ALA B O   1 
ATOM   7231  C  CB  . ALA B 1 328 ? 23.302  34.174  48.274  1.00 21.06 ? 320  ALA B CB  1 
ATOM   7232  N  N   . GLU B 1 329 ? 22.334  32.605  45.610  1.00 19.29 ? 321  GLU B N   1 
ATOM   7233  C  CA  . GLU B 1 329 ? 21.530  31.559  44.983  1.00 21.50 ? 321  GLU B CA  1 
ATOM   7234  C  C   . GLU B 1 329 ? 22.398  30.588  44.195  1.00 21.44 ? 321  GLU B C   1 
ATOM   7235  O  O   . GLU B 1 329 ? 22.126  29.380  44.163  1.00 18.02 ? 321  GLU B O   1 
ATOM   7236  C  CB  . GLU B 1 329 ? 20.475  32.190  44.076  1.00 22.09 ? 321  GLU B CB  1 
ATOM   7237  C  CG  . GLU B 1 329 ? 19.202  32.557  44.811  1.00 26.12 ? 321  GLU B CG  1 
ATOM   7238  C  CD  . GLU B 1 329 ? 18.490  31.325  45.328  1.00 26.58 ? 321  GLU B CD  1 
ATOM   7239  O  OE1 . GLU B 1 329 ? 17.950  30.572  44.494  1.00 25.57 ? 321  GLU B OE1 1 
ATOM   7240  O  OE2 . GLU B 1 329 ? 18.502  31.094  46.557  1.00 23.17 ? 321  GLU B OE2 1 
ATOM   7241  N  N   . PHE B 1 330 ? 23.436  31.101  43.536  1.00 24.62 ? 322  PHE B N   1 
ATOM   7242  C  CA  . PHE B 1 330 ? 24.322  30.241  42.761  1.00 20.32 ? 322  PHE B CA  1 
ATOM   7243  C  C   . PHE B 1 330 ? 25.058  29.259  43.665  1.00 18.57 ? 322  PHE B C   1 
ATOM   7244  O  O   . PHE B 1 330 ? 25.172  28.070  43.343  1.00 17.81 ? 322  PHE B O   1 
ATOM   7245  C  CB  . PHE B 1 330 ? 25.309  31.106  41.974  1.00 18.63 ? 322  PHE B CB  1 
ATOM   7246  C  CG  . PHE B 1 330 ? 26.220  30.323  41.073  1.00 21.13 ? 322  PHE B CG  1 
ATOM   7247  C  CD1 . PHE B 1 330 ? 25.745  29.790  39.883  1.00 18.32 ? 322  PHE B CD1 1 
ATOM   7248  C  CD2 . PHE B 1 330 ? 27.551  30.129  41.408  1.00 23.60 ? 322  PHE B CD2 1 
ATOM   7249  C  CE1 . PHE B 1 330 ? 26.575  29.074  39.045  1.00 21.06 ? 322  PHE B CE1 1 
ATOM   7250  C  CE2 . PHE B 1 330 ? 28.390  29.416  40.567  1.00 23.52 ? 322  PHE B CE2 1 
ATOM   7251  C  CZ  . PHE B 1 330 ? 27.903  28.890  39.390  1.00 19.34 ? 322  PHE B CZ  1 
ATOM   7252  N  N   . VAL B 1 331 ? 25.543  29.737  44.814  1.00 18.13 ? 323  VAL B N   1 
ATOM   7253  C  CA  . VAL B 1 331 ? 26.240  28.865  45.758  1.00 18.08 ? 323  VAL B CA  1 
ATOM   7254  C  C   . VAL B 1 331 ? 25.282  27.818  46.318  1.00 17.60 ? 323  VAL B C   1 
ATOM   7255  O  O   . VAL B 1 331 ? 25.588  26.620  46.332  1.00 17.13 ? 323  VAL B O   1 
ATOM   7256  C  CB  . VAL B 1 331 ? 26.895  29.702  46.874  1.00 19.87 ? 323  VAL B CB  1 
ATOM   7257  C  CG1 . VAL B 1 331 ? 27.463  28.806  47.970  1.00 20.75 ? 323  VAL B CG1 1 
ATOM   7258  C  CG2 . VAL B 1 331 ? 27.983  30.602  46.297  1.00 21.29 ? 323  VAL B CG2 1 
ATOM   7259  N  N   . ARG B 1 332 ? 24.102  28.252  46.773  1.00 17.78 ? 324  ARG B N   1 
ATOM   7260  C  CA  . ARG B 1 332 ? 23.095  27.311  47.261  1.00 18.33 ? 324  ARG B CA  1 
ATOM   7261  C  C   . ARG B 1 332 ? 22.826  26.202  46.249  1.00 19.83 ? 324  ARG B C   1 
ATOM   7262  O  O   . ARG B 1 332 ? 22.855  25.013  46.581  1.00 16.37 ? 324  ARG B O   1 
ATOM   7263  C  CB  . ARG B 1 332 ? 21.787  28.050  47.583  1.00 22.26 ? 324  ARG B CB  1 
ATOM   7264  C  CG  . ARG B 1 332 ? 20.681  27.102  48.053  1.00 21.92 ? 324  ARG B CG  1 
ATOM   7265  C  CD  . ARG B 1 332 ? 19.368  27.813  48.318  1.00 20.38 ? 324  ARG B CD  1 
ATOM   7266  N  NE  . ARG B 1 332 ? 18.695  28.227  47.087  1.00 24.52 ? 324  ARG B NE  1 
ATOM   7267  C  CZ  . ARG B 1 332 ? 17.981  27.412  46.316  1.00 19.36 ? 324  ARG B CZ  1 
ATOM   7268  N  NH1 . ARG B 1 332 ? 17.880  26.122  46.623  1.00 18.04 ? 324  ARG B NH1 1 
ATOM   7269  N  NH2 . ARG B 1 332 ? 17.393  27.879  45.221  1.00 20.28 ? 324  ARG B NH2 1 
ATOM   7270  N  N   . ARG B 1 333 ? 22.559  26.577  44.998  1.00 17.95 ? 325  ARG B N   1 
ATOM   7271  C  CA  . ARG B 1 333 ? 22.153  25.589  44.013  1.00 15.87 ? 325  ARG B CA  1 
ATOM   7272  C  C   . ARG B 1 333 ? 23.329  24.753  43.518  1.00 19.72 ? 325  ARG B C   1 
ATOM   7273  O  O   . ARG B 1 333 ? 23.146  23.572  43.198  1.00 18.03 ? 325  ARG B O   1 
ATOM   7274  C  CB  . ARG B 1 333 ? 21.454  26.288  42.849  1.00 15.84 ? 325  ARG B CB  1 
ATOM   7275  C  CG  . ARG B 1 333 ? 20.074  26.866  43.232  1.00 16.12 ? 325  ARG B CG  1 
ATOM   7276  C  CD  . ARG B 1 333 ? 19.590  27.897  42.204  1.00 16.29 ? 325  ARG B CD  1 
ATOM   7277  N  NE  . ARG B 1 333 ? 19.656  27.379  40.847  1.00 15.87 ? 325  ARG B NE  1 
ATOM   7278  C  CZ  . ARG B 1 333 ? 19.208  28.021  39.769  1.00 17.14 ? 325  ARG B CZ  1 
ATOM   7279  N  NH1 . ARG B 1 333 ? 18.641  29.220  39.887  1.00 18.06 ? 325  ARG B NH1 1 
ATOM   7280  N  NH2 . ARG B 1 333 ? 19.331  27.461  38.571  1.00 15.62 ? 325  ARG B NH2 1 
ATOM   7281  N  N   . MET B 1 334 ? 24.534  25.335  43.452  1.00 17.20 ? 326  MET B N   1 
ATOM   7282  C  CA  . MET B 1 334 ? 25.710  24.543  43.079  1.00 15.56 ? 326  MET B CA  1 
ATOM   7283  C  C   . MET B 1 334 ? 26.077  23.555  44.174  1.00 19.03 ? 326  MET B C   1 
ATOM   7284  O  O   . MET B 1 334 ? 26.565  22.456  43.876  1.00 18.98 ? 326  MET B O   1 
ATOM   7285  C  CB  . MET B 1 334 ? 26.917  25.439  42.779  1.00 16.03 ? 326  MET B CB  1 
ATOM   7286  C  CG  . MET B 1 334 ? 26.928  26.140  41.414  1.00 19.16 ? 326  MET B CG  1 
ATOM   7287  S  SD  . MET B 1 334 ? 26.526  25.108  39.984  1.00 17.89 ? 326  MET B SD  1 
ATOM   7288  C  CE  . MET B 1 334 ? 27.873  23.917  39.984  1.00 16.67 ? 326  MET B CE  1 
ATOM   7289  N  N   . ASP B 1 335 ? 25.863  23.925  45.438  1.00 18.22 ? 327  ASP B N   1 
ATOM   7290  C  CA  . ASP B 1 335 ? 26.077  23.013  46.556  1.00 20.46 ? 327  ASP B CA  1 
ATOM   7291  C  C   . ASP B 1 335 ? 24.923  22.027  46.734  1.00 24.86 ? 327  ASP B C   1 
ATOM   7292  O  O   . ASP B 1 335 ? 24.944  21.237  47.684  1.00 25.72 ? 327  ASP B O   1 
ATOM   7293  C  CB  . ASP B 1 335 ? 26.292  23.793  47.861  1.00 22.77 ? 327  ASP B CB  1 
ATOM   7294  C  CG  . ASP B 1 335 ? 27.616  24.550  47.891  1.00 21.67 ? 327  ASP B CG  1 
ATOM   7295  O  OD1 . ASP B 1 335 ? 28.498  24.262  47.061  1.00 21.38 ? 327  ASP B OD1 1 
ATOM   7296  O  OD2 . ASP B 1 335 ? 27.781  25.432  48.757  1.00 24.13 ? 327  ASP B OD2 1 
ATOM   7297  N  N   . LYS B 1 336 ? 23.918  22.073  45.857  1.00 21.31 ? 328  LYS B N   1 
ATOM   7298  C  CA  . LYS B 1 336 ? 22.803  21.125  45.863  1.00 26.16 ? 328  LYS B CA  1 
ATOM   7299  C  C   . LYS B 1 336 ? 22.052  21.147  47.200  1.00 28.71 ? 328  LYS B C   1 
ATOM   7300  O  O   . LYS B 1 336 ? 21.779  20.110  47.804  1.00 31.89 ? 328  LYS B O   1 
ATOM   7301  C  CB  . LYS B 1 336 ? 23.295  19.713  45.512  1.00 26.17 ? 328  LYS B CB  1 
ATOM   7302  C  CG  . LYS B 1 336 ? 24.049  19.641  44.170  1.00 26.93 ? 328  LYS B CG  1 
ATOM   7303  C  CD  . LYS B 1 336 ? 24.799  18.305  43.978  1.00 21.73 ? 328  LYS B CD  1 
ATOM   7304  C  CE  . LYS B 1 336 ? 25.526  18.251  42.639  1.00 24.56 ? 328  LYS B CE  1 
ATOM   7305  N  NZ  . LYS B 1 336 ? 26.227  16.932  42.378  1.00 29.77 ? 328  LYS B NZ  1 
ATOM   7306  N  N   . LYS B 1 337 ? 21.706  22.351  47.658  1.00 24.05 ? 329  LYS B N   1 
ATOM   7307  C  CA  . LYS B 1 337 ? 20.948  22.545  48.888  1.00 18.98 ? 329  LYS B CA  1 
ATOM   7308  C  C   . LYS B 1 337 ? 19.609  23.210  48.579  1.00 22.60 ? 329  LYS B C   1 
ATOM   7309  O  O   . LYS B 1 337 ? 19.505  24.038  47.671  1.00 22.16 ? 329  LYS B O   1 
ATOM   7310  C  CB  . LYS B 1 337 ? 21.746  23.399  49.893  1.00 23.22 ? 329  LYS B CB  1 
ATOM   7311  C  CG  . LYS B 1 337 ? 23.202  22.934  50.057  1.00 22.30 ? 329  LYS B CG  1 
ATOM   7312  C  CD  . LYS B 1 337 ? 24.082  24.038  50.665  1.00 32.72 ? 329  LYS B CD  1 
ATOM   7313  C  CE  . LYS B 1 337 ? 24.323  23.848  52.157  1.00 33.10 ? 329  LYS B CE  1 
ATOM   7314  N  NZ  . LYS B 1 337 ? 25.289  24.864  52.694  1.00 32.05 ? 329  LYS B NZ  1 
ATOM   7315  N  N   . LEU B 1 338 ? 18.584  22.854  49.346  1.00 20.69 ? 330  LEU B N   1 
ATOM   7316  C  CA  . LEU B 1 338 ? 17.266  23.458  49.179  1.00 26.36 ? 330  LEU B CA  1 
ATOM   7317  C  C   . LEU B 1 338 ? 17.178  24.800  49.910  1.00 26.66 ? 330  LEU B C   1 
ATOM   7318  O  O   . LEU B 1 338 ? 18.023  25.116  50.751  1.00 25.20 ? 330  LEU B O   1 
ATOM   7319  C  CB  . LEU B 1 338 ? 16.188  22.508  49.699  1.00 26.46 ? 330  LEU B CB  1 
ATOM   7320  C  CG  . LEU B 1 338 ? 15.961  21.217  48.912  1.00 27.21 ? 330  LEU B CG  1 
ATOM   7321  C  CD1 . LEU B 1 338 ? 14.861  20.390  49.541  1.00 34.31 ? 330  LEU B CD1 1 
ATOM   7322  C  CD2 . LEU B 1 338 ? 15.635  21.525  47.463  1.00 29.31 ? 330  LEU B CD2 1 
ATOM   7323  N  N   . PRO B 1 339 ? 16.167  25.618  49.604  1.00 28.81 ? 331  PRO B N   1 
ATOM   7324  C  CA  . PRO B 1 339 ? 15.968  26.847  50.380  1.00 27.63 ? 331  PRO B CA  1 
ATOM   7325  C  C   . PRO B 1 339 ? 15.697  26.522  51.838  1.00 31.65 ? 331  PRO B C   1 
ATOM   7326  O  O   . PRO B 1 339 ? 15.147  25.467  52.169  1.00 26.93 ? 331  PRO B O   1 
ATOM   7327  C  CB  . PRO B 1 339 ? 14.751  27.500  49.717  1.00 28.32 ? 331  PRO B CB  1 
ATOM   7328  C  CG  . PRO B 1 339 ? 14.710  26.923  48.361  1.00 26.35 ? 331  PRO B CG  1 
ATOM   7329  C  CD  . PRO B 1 339 ? 15.206  25.523  48.495  1.00 25.65 ? 331  PRO B CD  1 
ATOM   7330  N  N   . GLU B 1 340 ? 16.114  27.443  52.711  1.00 29.80 ? 332  GLU B N   1 
ATOM   7331  C  CA  . GLU B 1 340 ? 16.008  27.212  54.148  1.00 30.31 ? 332  GLU B CA  1 
ATOM   7332  C  C   . GLU B 1 340 ? 14.561  27.007  54.575  1.00 26.96 ? 332  GLU B C   1 
ATOM   7333  O  O   . GLU B 1 340 ? 14.280  26.205  55.473  1.00 33.43 ? 332  GLU B O   1 
ATOM   7334  C  CB  . GLU B 1 340 ? 16.631  28.382  54.913  1.00 31.36 ? 332  GLU B CB  1 
ATOM   7335  N  N   . ASN B 1 341 ? 13.626  27.714  53.947  1.00 28.09 ? 333  ASN B N   1 
ATOM   7336  C  CA  . ASN B 1 341 ? 12.233  27.649  54.361  1.00 32.49 ? 333  ASN B CA  1 
ATOM   7337  C  C   . ASN B 1 341 ? 11.454  26.530  53.669  1.00 28.43 ? 333  ASN B C   1 
ATOM   7338  O  O   . ASN B 1 341 ? 10.221  26.565  53.668  1.00 30.38 ? 333  ASN B O   1 
ATOM   7339  C  CB  . ASN B 1 341 ? 11.547  28.993  54.107  1.00 38.43 ? 333  ASN B CB  1 
ATOM   7340  C  CG  . ASN B 1 341 ? 11.368  29.284  52.631  1.00 45.86 ? 333  ASN B CG  1 
ATOM   7341  O  OD1 . ASN B 1 341 ? 12.196  28.895  51.810  1.00 43.24 ? 333  ASN B OD1 1 
ATOM   7342  N  ND2 . ASN B 1 341 ? 10.276  29.965  52.283  1.00 45.15 ? 333  ASN B ND2 1 
ATOM   7343  N  N   . PHE B 1 342 ? 12.135  25.534  53.094  1.00 23.51 ? 334  PHE B N   1 
ATOM   7344  C  CA  . PHE B 1 342 ? 11.437  24.608  52.201  1.00 18.99 ? 334  PHE B CA  1 
ATOM   7345  C  C   . PHE B 1 342 ? 10.359  23.815  52.930  1.00 21.40 ? 334  PHE B C   1 
ATOM   7346  O  O   . PHE B 1 342 ? 9.235   23.680  52.431  1.00 26.22 ? 334  PHE B O   1 
ATOM   7347  C  CB  . PHE B 1 342 ? 12.418  23.653  51.528  1.00 20.12 ? 334  PHE B CB  1 
ATOM   7348  C  CG  . PHE B 1 342 ? 11.768  22.764  50.508  1.00 19.83 ? 334  PHE B CG  1 
ATOM   7349  C  CD1 . PHE B 1 342 ? 11.480  23.243  49.244  1.00 20.90 ? 334  PHE B CD1 1 
ATOM   7350  C  CD2 . PHE B 1 342 ? 11.421  21.458  50.819  1.00 21.78 ? 334  PHE B CD2 1 
ATOM   7351  C  CE1 . PHE B 1 342 ? 10.870  22.434  48.296  1.00 20.25 ? 334  PHE B CE1 1 
ATOM   7352  C  CE2 . PHE B 1 342 ? 10.818  20.641  49.869  1.00 23.53 ? 334  PHE B CE2 1 
ATOM   7353  C  CZ  . PHE B 1 342 ? 10.540  21.134  48.612  1.00 17.81 ? 334  PHE B CZ  1 
ATOM   7354  N  N   . ASP B 1 343 ? 10.690  23.252  54.096  1.00 24.05 ? 335  ASP B N   1 
ATOM   7355  C  CA  . ASP B 1 343 ? 9.730   22.416  54.815  1.00 28.06 ? 335  ASP B CA  1 
ATOM   7356  C  C   . ASP B 1 343 ? 8.514   23.221  55.255  1.00 28.65 ? 335  ASP B C   1 
ATOM   7357  O  O   . ASP B 1 343 ? 7.375   22.737  55.178  1.00 24.69 ? 335  ASP B O   1 
ATOM   7358  C  CB  . ASP B 1 343 ? 10.398  21.770  56.028  1.00 37.52 ? 335  ASP B CB  1 
ATOM   7359  C  CG  . ASP B 1 343 ? 11.434  20.735  55.643  1.00 46.13 ? 335  ASP B CG  1 
ATOM   7360  O  OD1 . ASP B 1 343 ? 11.200  19.993  54.667  1.00 42.44 ? 335  ASP B OD1 1 
ATOM   7361  O  OD2 . ASP B 1 343 ? 12.483  20.665  56.318  1.00 50.21 ? 335  ASP B OD2 1 
ATOM   7362  N  N   . GLU B 1 344 ? 8.737   24.448  55.728  1.00 26.57 ? 336  GLU B N   1 
ATOM   7363  C  CA  . GLU B 1 344 ? 7.624   25.289  56.155  1.00 28.89 ? 336  GLU B CA  1 
ATOM   7364  C  C   . GLU B 1 344 ? 6.767   25.706  54.968  1.00 28.10 ? 336  GLU B C   1 
ATOM   7365  O  O   . GLU B 1 344 ? 5.535   25.743  55.069  1.00 30.97 ? 336  GLU B O   1 
ATOM   7366  C  CB  . GLU B 1 344 ? 8.151   26.515  56.902  1.00 29.82 ? 336  GLU B CB  1 
ATOM   7367  N  N   . TYR B 1 345 ? 7.403   26.016  53.834  1.00 25.96 ? 337  TYR B N   1 
ATOM   7368  C  CA  . TYR B 1 345 ? 6.659   26.337  52.619  1.00 27.60 ? 337  TYR B CA  1 
ATOM   7369  C  C   . TYR B 1 345 ? 5.762   25.175  52.202  1.00 20.80 ? 337  TYR B C   1 
ATOM   7370  O  O   . TYR B 1 345 ? 4.579   25.368  51.894  1.00 24.80 ? 337  TYR B O   1 
ATOM   7371  C  CB  . TYR B 1 345 ? 7.622   26.695  51.484  1.00 26.45 ? 337  TYR B CB  1 
ATOM   7372  C  CG  . TYR B 1 345 ? 6.939   26.886  50.142  1.00 22.14 ? 337  TYR B CG  1 
ATOM   7373  C  CD1 . TYR B 1 345 ? 6.360   28.107  49.802  1.00 25.79 ? 337  TYR B CD1 1 
ATOM   7374  C  CD2 . TYR B 1 345 ? 6.864   25.848  49.223  1.00 18.74 ? 337  TYR B CD2 1 
ATOM   7375  C  CE1 . TYR B 1 345 ? 5.725   28.290  48.576  1.00 22.72 ? 337  TYR B CE1 1 
ATOM   7376  C  CE2 . TYR B 1 345 ? 6.233   26.021  47.991  1.00 22.72 ? 337  TYR B CE2 1 
ATOM   7377  C  CZ  . TYR B 1 345 ? 5.665   27.249  47.678  1.00 23.25 ? 337  TYR B CZ  1 
ATOM   7378  O  OH  . TYR B 1 345 ? 5.038   27.429  46.463  1.00 20.01 ? 337  TYR B OH  1 
ATOM   7379  N  N   . VAL B 1 346 ? 6.314   23.960  52.177  1.00 20.69 ? 338  VAL B N   1 
ATOM   7380  C  CA  . VAL B 1 346 ? 5.527   22.794  51.782  1.00 21.06 ? 338  VAL B CA  1 
ATOM   7381  C  C   . VAL B 1 346 ? 4.384   22.575  52.763  1.00 26.26 ? 338  VAL B C   1 
ATOM   7382  O  O   . VAL B 1 346 ? 3.231   22.354  52.368  1.00 21.19 ? 338  VAL B O   1 
ATOM   7383  C  CB  . VAL B 1 346 ? 6.427   21.549  51.672  1.00 19.23 ? 338  VAL B CB  1 
ATOM   7384  C  CG1 . VAL B 1 346 ? 5.573   20.283  51.516  1.00 18.74 ? 338  VAL B CG1 1 
ATOM   7385  C  CG2 . VAL B 1 346 ? 7.397   21.703  50.492  1.00 22.09 ? 338  VAL B CG2 1 
ATOM   7386  N  N   . GLN B 1 347 ? 4.686   22.662  54.061  1.00 24.58 ? 339  GLN B N   1 
ATOM   7387  C  CA  . GLN B 1 347 ? 3.668   22.436  55.079  1.00 25.06 ? 339  GLN B CA  1 
ATOM   7388  C  C   . GLN B 1 347 ? 2.508   23.407  54.913  1.00 27.02 ? 339  GLN B C   1 
ATOM   7389  O  O   . GLN B 1 347 ? 1.339   23.003  54.923  1.00 25.83 ? 339  GLN B O   1 
ATOM   7390  C  CB  . GLN B 1 347 ? 4.282   22.559  56.473  1.00 24.81 ? 339  GLN B CB  1 
ATOM   7391  N  N   . THR B 1 348 ? 2.815   24.692  54.729  1.00 26.41 ? 340  THR B N   1 
ATOM   7392  C  CA  . THR B 1 348 ? 1.764   25.684  54.535  1.00 30.63 ? 340  THR B CA  1 
ATOM   7393  C  C   . THR B 1 348 ? 0.968   25.400  53.265  1.00 24.39 ? 340  THR B C   1 
ATOM   7394  O  O   . THR B 1 348 ? -0.267  25.374  53.286  1.00 30.37 ? 340  THR B O   1 
ATOM   7395  C  CB  . THR B 1 348 ? 2.379   27.080  54.496  1.00 29.64 ? 340  THR B CB  1 
ATOM   7396  O  OG1 . THR B 1 348 ? 3.001   27.353  55.757  1.00 32.05 ? 340  THR B OG1 1 
ATOM   7397  C  CG2 . THR B 1 348 ? 1.312   28.126  54.232  1.00 32.67 ? 340  THR B CG2 1 
ATOM   7398  N  N   . ALA B 1 349 ? 1.665   25.169  52.151  1.00 23.06 ? 341  ALA B N   1 
ATOM   7399  C  CA  . ALA B 1 349 ? 0.987   24.883  50.890  1.00 25.55 ? 341  ALA B CA  1 
ATOM   7400  C  C   . ALA B 1 349 ? 0.114   23.640  51.007  1.00 30.84 ? 341  ALA B C   1 
ATOM   7401  O  O   . ALA B 1 349 ? -0.976  23.579  50.423  1.00 30.39 ? 341  ALA B O   1 
ATOM   7402  C  CB  . ALA B 1 349 ? 2.017   24.715  49.770  1.00 27.00 ? 341  ALA B CB  1 
ATOM   7403  N  N   . LEU B 1 350 ? 0.577   22.642  51.767  1.00 26.88 ? 342  LEU B N   1 
ATOM   7404  C  CA  . LEU B 1 350 ? -0.188  21.413  51.940  1.00 27.68 ? 342  LEU B CA  1 
ATOM   7405  C  C   . LEU B 1 350 ? -1.485  21.681  52.688  1.00 30.82 ? 342  LEU B C   1 
ATOM   7406  O  O   . LEU B 1 350 ? -2.554  21.208  52.283  1.00 28.74 ? 342  LEU B O   1 
ATOM   7407  C  CB  . LEU B 1 350 ? 0.655   20.373  52.677  1.00 27.68 ? 342  LEU B CB  1 
ATOM   7408  C  CG  . LEU B 1 350 ? 0.023   18.997  52.864  1.00 27.87 ? 342  LEU B CG  1 
ATOM   7409  C  CD1 . LEU B 1 350 ? -0.293  18.383  51.518  1.00 22.58 ? 342  LEU B CD1 1 
ATOM   7410  C  CD2 . LEU B 1 350 ? 0.947   18.096  53.675  1.00 28.97 ? 342  LEU B CD2 1 
ATOM   7411  N  N   . LYS B 1 351 ? -1.408  22.434  53.790  1.00 25.38 ? 343  LYS B N   1 
ATOM   7412  C  CA  . LYS B 1 351 ? -2.616  22.810  54.512  1.00 27.02 ? 343  LYS B CA  1 
ATOM   7413  C  C   . LYS B 1 351 ? -3.595  23.525  53.594  1.00 31.84 ? 343  LYS B C   1 
ATOM   7414  O  O   . LYS B 1 351 ? -4.804  23.267  53.644  1.00 31.65 ? 343  LYS B O   1 
ATOM   7415  C  CB  . LYS B 1 351 ? -2.263  23.692  55.713  1.00 28.00 ? 343  LYS B CB  1 
ATOM   7416  N  N   . GLU B 1 352 ? -3.083  24.401  52.721  1.00 32.64 ? 344  GLU B N   1 
ATOM   7417  C  CA  . GLU B 1 352 ? -3.942  25.145  51.803  1.00 33.94 ? 344  GLU B CA  1 
ATOM   7418  C  C   . GLU B 1 352 ? -4.570  24.230  50.757  1.00 34.81 ? 344  GLU B C   1 
ATOM   7419  O  O   . GLU B 1 352 ? -5.756  24.375  50.436  1.00 39.19 ? 344  GLU B O   1 
ATOM   7420  C  CB  . GLU B 1 352 ? -3.147  26.265  51.128  1.00 40.50 ? 344  GLU B CB  1 
ATOM   7421  C  CG  . GLU B 1 352 ? -2.709  27.389  52.070  1.00 48.10 ? 344  GLU B CG  1 
ATOM   7422  C  CD  . GLU B 1 352 ? -1.740  28.365  51.413  1.00 51.82 ? 344  GLU B CD  1 
ATOM   7423  O  OE1 . GLU B 1 352 ? -1.354  28.135  50.246  1.00 49.83 ? 344  GLU B OE1 1 
ATOM   7424  O  OE2 . GLU B 1 352 ? -1.361  29.361  52.068  1.00 53.09 ? 344  GLU B OE2 1 
ATOM   7425  N  N   . VAL B 1 353 ? -3.789  23.299  50.200  1.00 34.49 ? 345  VAL B N   1 
ATOM   7426  C  CA  . VAL B 1 353 ? -4.340  22.327  49.254  1.00 33.38 ? 345  VAL B CA  1 
ATOM   7427  C  C   . VAL B 1 353 ? -5.506  21.577  49.888  1.00 37.61 ? 345  VAL B C   1 
ATOM   7428  O  O   . VAL B 1 353 ? -6.575  21.418  49.286  1.00 40.07 ? 345  VAL B O   1 
ATOM   7429  C  CB  . VAL B 1 353 ? -3.241  21.358  48.780  1.00 34.08 ? 345  VAL B CB  1 
ATOM   7430  C  CG1 . VAL B 1 353 ? -3.854  20.112  48.151  1.00 34.55 ? 345  VAL B CG1 1 
ATOM   7431  C  CG2 . VAL B 1 353 ? -2.316  22.043  47.791  1.00 39.85 ? 345  VAL B CG2 1 
ATOM   7432  N  N   . CYS B 1 354 ? -5.314  21.106  51.118  1.00 42.37 ? 346  CYS B N   1 
ATOM   7433  C  CA  A CYS B 1 354 ? -6.359  20.362  51.815  0.77 49.09 ? 346  CYS B CA  1 
ATOM   7434  C  CA  B CYS B 1 354 ? -6.378  20.358  51.772  0.23 48.93 ? 346  CYS B CA  1 
ATOM   7435  C  C   . CYS B 1 354 ? -7.582  21.234  52.074  1.00 54.21 ? 346  CYS B C   1 
ATOM   7436  O  O   . CYS B 1 354 ? -8.708  20.726  52.136  1.00 63.03 ? 346  CYS B O   1 
ATOM   7437  C  CB  A CYS B 1 354 ? -5.802  19.799  53.128  0.77 49.88 ? 346  CYS B CB  1 
ATOM   7438  C  CB  B CYS B 1 354 ? -5.840  19.709  53.035  0.23 49.79 ? 346  CYS B CB  1 
ATOM   7439  S  SG  A CYS B 1 354 ? -6.906  18.688  54.058  0.77 54.42 ? 346  CYS B SG  1 
ATOM   7440  S  SG  B CYS B 1 354 ? -4.427  18.718  52.625  0.23 45.99 ? 346  CYS B SG  1 
ATOM   7441  N  N   . ALA B 1 355 ? -7.376  22.543  52.240  1.00 54.67 ? 347  ALA B N   1 
ATOM   7442  C  CA  . ALA B 1 355 ? -8.503  23.456  52.394  1.00 58.01 ? 347  ALA B CA  1 
ATOM   7443  C  C   . ALA B 1 355 ? -9.348  23.487  51.125  1.00 60.35 ? 347  ALA B C   1 
ATOM   7444  O  O   . ALA B 1 355 ? -10.571 23.307  51.172  1.00 64.49 ? 347  ALA B O   1 
ATOM   7445  C  CB  . ALA B 1 355 ? -7.997  24.855  52.748  1.00 58.79 ? 347  ALA B CB  1 
ATOM   7446  N  N   . LYS B 1 356 ? -8.707  23.701  49.979  1.00 54.77 ? 348  LYS B N   1 
ATOM   7447  C  CA  . LYS B 1 356 ? -9.390  23.684  48.691  1.00 55.71 ? 348  LYS B CA  1 
ATOM   7448  C  C   . LYS B 1 356 ? -9.460  22.264  48.128  1.00 59.23 ? 348  LYS B C   1 
ATOM   7449  O  O   . LYS B 1 356 ? -10.508 21.617  48.166  1.00 66.29 ? 348  LYS B O   1 
ATOM   7450  C  CB  . LYS B 1 356 ? -8.684  24.609  47.697  1.00 54.35 ? 348  LYS B CB  1 
ATOM   7451  N  N   . GLN B 1 367 ? -3.752  18.100  40.741  1.00 69.78 ? 359  GLN B N   1 
ATOM   7452  C  CA  . GLN B 1 367 ? -3.578  19.546  40.828  1.00 69.07 ? 359  GLN B CA  1 
ATOM   7453  C  C   . GLN B 1 367 ? -2.341  19.962  40.076  1.00 60.35 ? 359  GLN B C   1 
ATOM   7454  O  O   . GLN B 1 367 ? -1.998  19.372  39.053  1.00 66.91 ? 359  GLN B O   1 
ATOM   7455  C  CB  . GLN B 1 367 ? -3.464  20.007  42.281  1.00 74.56 ? 359  GLN B CB  1 
ATOM   7456  N  N   . ASN B 1 368 ? -1.660  20.986  40.589  1.00 47.63 ? 360  ASN B N   1 
ATOM   7457  C  CA  . ASN B 1 368 ? -0.348  21.365  40.075  1.00 37.86 ? 360  ASN B CA  1 
ATOM   7458  C  C   . ASN B 1 368 ? 0.607   21.473  41.262  1.00 26.81 ? 360  ASN B C   1 
ATOM   7459  O  O   . ASN B 1 368 ? 0.952   22.564  41.716  1.00 21.78 ? 360  ASN B O   1 
ATOM   7460  C  CB  . ASN B 1 368 ? -0.402  22.645  39.251  1.00 40.82 ? 360  ASN B CB  1 
ATOM   7461  C  CG  . ASN B 1 368 ? 0.538   22.593  38.054  1.00 43.26 ? 360  ASN B CG  1 
ATOM   7462  O  OD1 . ASN B 1 368 ? 1.536   21.873  38.074  1.00 29.32 ? 360  ASN B OD1 1 
ATOM   7463  N  ND2 . ASN B 1 368 ? 0.214   23.340  37.003  1.00 49.51 ? 360  ASN B ND2 1 
ATOM   7464  N  N   . SER B 1 369 ? 1.041   20.310  41.751  1.00 24.59 ? 361  SER B N   1 
ATOM   7465  C  CA  . SER B 1 369 ? 2.172   20.261  42.666  1.00 20.01 ? 361  SER B CA  1 
ATOM   7466  C  C   . SER B 1 369 ? 3.404   20.894  42.039  1.00 15.27 ? 361  SER B C   1 
ATOM   7467  O  O   . SER B 1 369 ? 4.201   21.532  42.731  1.00 15.91 ? 361  SER B O   1 
ATOM   7468  C  CB  . SER B 1 369 ? 2.473   18.811  43.050  1.00 21.69 ? 361  SER B CB  1 
ATOM   7469  O  OG  . SER B 1 369 ? 1.299   18.123  43.431  1.00 25.04 ? 361  SER B OG  1 
ATOM   7470  N  N   . ILE B 1 370 ? 3.601   20.685  40.732  1.00 15.93 ? 362  ILE B N   1 
ATOM   7471  C  CA  . ILE B 1 370 ? 4.777   21.232  40.061  1.00 15.42 ? 362  ILE B CA  1 
ATOM   7472  C  C   . ILE B 1 370 ? 4.784   22.747  40.175  1.00 14.69 ? 362  ILE B C   1 
ATOM   7473  O  O   . ILE B 1 370 ? 5.810   23.355  40.479  1.00 16.81 ? 362  ILE B O   1 
ATOM   7474  C  CB  . ILE B 1 370 ? 4.821   20.788  38.586  1.00 14.54 ? 362  ILE B CB  1 
ATOM   7475  C  CG1 . ILE B 1 370 ? 4.852   19.272  38.482  1.00 15.12 ? 362  ILE B CG1 1 
ATOM   7476  C  CG2 . ILE B 1 370 ? 6.044   21.391  37.884  1.00 17.64 ? 362  ILE B CG2 1 
ATOM   7477  C  CD1 . ILE B 1 370 ? 4.801   18.761  37.041  1.00 14.89 ? 362  ILE B CD1 1 
ATOM   7478  N  N   . GLU B 1 371 ? 3.632   23.376  39.927  1.00 18.11 ? 363  GLU B N   1 
ATOM   7479  C  CA  . GLU B 1 371 ? 3.545   24.830  40.036  1.00 23.83 ? 363  GLU B CA  1 
ATOM   7480  C  C   . GLU B 1 371 ? 3.873   25.302  41.448  1.00 21.77 ? 363  GLU B C   1 
ATOM   7481  O  O   . GLU B 1 371 ? 4.595   26.292  41.626  1.00 21.05 ? 363  GLU B O   1 
ATOM   7482  C  CB  . GLU B 1 371 ? 2.153   25.307  39.623  1.00 26.68 ? 363  GLU B CB  1 
ATOM   7483  C  CG  . GLU B 1 371 ? 2.065   26.808  39.394  1.00 32.12 ? 363  GLU B CG  1 
ATOM   7484  C  CD  . GLU B 1 371 ? 2.123   27.175  37.918  1.00 39.41 ? 363  GLU B CD  1 
ATOM   7485  O  OE1 . GLU B 1 371 ? 1.422   26.512  37.116  1.00 39.65 ? 363  GLU B OE1 1 
ATOM   7486  O  OE2 . GLU B 1 371 ? 2.877   28.114  37.559  1.00 40.32 ? 363  GLU B OE2 1 
ATOM   7487  N  N   . ILE B 1 372 ? 3.355   24.602  42.465  1.00 18.43 ? 364  ILE B N   1 
ATOM   7488  C  CA  . ILE B 1 372 ? 3.667   24.948  43.854  1.00 19.28 ? 364  ILE B CA  1 
ATOM   7489  C  C   . ILE B 1 372 ? 5.165   24.833  44.103  1.00 20.78 ? 364  ILE B C   1 
ATOM   7490  O  O   . ILE B 1 372 ? 5.781   25.704  44.730  1.00 23.24 ? 364  ILE B O   1 
ATOM   7491  C  CB  . ILE B 1 372 ? 2.875   24.047  44.822  1.00 23.06 ? 364  ILE B CB  1 
ATOM   7492  C  CG1 . ILE B 1 372 ? 1.373   24.313  44.715  1.00 25.44 ? 364  ILE B CG1 1 
ATOM   7493  C  CG2 . ILE B 1 372 ? 3.357   24.248  46.258  1.00 25.80 ? 364  ILE B CG2 1 
ATOM   7494  C  CD1 . ILE B 1 372 ? 0.514   23.292  45.454  1.00 24.50 ? 364  ILE B CD1 1 
ATOM   7495  N  N   . LEU B 1 373 ? 5.767   23.743  43.628  1.00 17.67 ? 365  LEU B N   1 
ATOM   7496  C  CA  . LEU B 1 373 ? 7.196   23.516  43.839  1.00 19.59 ? 365  LEU B CA  1 
ATOM   7497  C  C   . LEU B 1 373 ? 8.044   24.556  43.113  1.00 18.54 ? 365  LEU B C   1 
ATOM   7498  O  O   . LEU B 1 373 ? 9.022   25.067  43.670  1.00 21.13 ? 365  LEU B O   1 
ATOM   7499  C  CB  . LEU B 1 373 ? 7.564   22.112  43.362  1.00 23.82 ? 365  LEU B CB  1 
ATOM   7500  C  CG  . LEU B 1 373 ? 8.520   21.265  44.198  1.00 30.83 ? 365  LEU B CG  1 
ATOM   7501  C  CD1 . LEU B 1 373 ? 7.889   20.944  45.533  1.00 37.73 ? 365  LEU B CD1 1 
ATOM   7502  C  CD2 . LEU B 1 373 ? 8.853   19.992  43.441  1.00 33.34 ? 365  LEU B CD2 1 
ATOM   7503  N  N   . ALA B 1 374 ? 7.689   24.870  41.865  1.00 16.19 ? 366  ALA B N   1 
ATOM   7504  C  CA  . ALA B 1 374 ? 8.492   25.781  41.055  1.00 14.69 ? 366  ALA B CA  1 
ATOM   7505  C  C   . ALA B 1 374 ? 8.587   27.172  41.676  1.00 19.53 ? 366  ALA B C   1 
ATOM   7506  O  O   . ALA B 1 374 ? 9.620   27.835  41.552  1.00 21.88 ? 366  ALA B O   1 
ATOM   7507  C  CB  . ALA B 1 374 ? 7.912   25.863  39.639  1.00 15.94 ? 366  ALA B CB  1 
ATOM   7508  N  N   . LYS B 1 375 ? 7.514   27.645  42.327  1.00 20.52 ? 367  LYS B N   1 
ATOM   7509  C  CA  . LYS B 1 375 ? 7.565   28.938  43.008  1.00 22.64 ? 367  LYS B CA  1 
ATOM   7510  C  C   . LYS B 1 375 ? 8.701   28.991  44.026  1.00 24.01 ? 367  LYS B C   1 
ATOM   7511  O  O   . LYS B 1 375 ? 9.345   30.033  44.202  1.00 22.64 ? 367  LYS B O   1 
ATOM   7512  C  CB  . LYS B 1 375 ? 6.236   29.222  43.708  1.00 28.03 ? 367  LYS B CB  1 
ATOM   7513  C  CG  . LYS B 1 375 ? 5.055   29.412  42.788  1.00 31.41 ? 367  LYS B CG  1 
ATOM   7514  C  CD  . LYS B 1 375 ? 3.775   29.646  43.599  1.00 36.96 ? 367  LYS B CD  1 
ATOM   7515  C  CE  . LYS B 1 375 ? 3.915   30.851  44.527  1.00 41.97 ? 367  LYS B CE  1 
ATOM   7516  N  NZ  . LYS B 1 375 ? 2.826   30.925  45.554  1.00 43.46 ? 367  LYS B NZ  1 
ATOM   7517  N  N   . GLU B 1 376 ? 8.948   27.878  44.709  1.00 22.12 ? 368  GLU B N   1 
ATOM   7518  C  CA  . GLU B 1 376 ? 9.925   27.778  45.790  1.00 24.69 ? 368  GLU B CA  1 
ATOM   7519  C  C   . GLU B 1 376 ? 11.310  27.371  45.305  1.00 25.01 ? 368  GLU B C   1 
ATOM   7520  O  O   . GLU B 1 376 ? 12.310  27.693  45.957  1.00 21.13 ? 368  GLU B O   1 
ATOM   7521  C  CB  . GLU B 1 376 ? 9.433   26.749  46.816  1.00 30.19 ? 368  GLU B CB  1 
ATOM   7522  C  CG  . GLU B 1 376 ? 10.439  26.326  47.876  1.00 33.09 ? 368  GLU B CG  1 
ATOM   7523  C  CD  . GLU B 1 376 ? 10.636  27.381  48.945  1.00 34.73 ? 368  GLU B CD  1 
ATOM   7524  O  OE1 . GLU B 1 376 ? 9.972   28.441  48.875  1.00 29.47 ? 368  GLU B OE1 1 
ATOM   7525  O  OE2 . GLU B 1 376 ? 11.450  27.142  49.866  1.00 38.84 ? 368  GLU B OE2 1 
ATOM   7526  N  N   . LEU B 1 377 ? 11.386  26.668  44.176  1.00 19.87 ? 369  LEU B N   1 
ATOM   7527  C  CA  . LEU B 1 377 ? 12.627  26.078  43.676  1.00 17.47 ? 369  LEU B CA  1 
ATOM   7528  C  C   . LEU B 1 377 ? 12.970  26.689  42.325  1.00 21.24 ? 369  LEU B C   1 
ATOM   7529  O  O   . LEU B 1 377 ? 12.610  26.134  41.272  1.00 16.26 ? 369  LEU B O   1 
ATOM   7530  C  CB  . LEU B 1 377 ? 12.495  24.559  43.574  1.00 20.65 ? 369  LEU B CB  1 
ATOM   7531  C  CG  . LEU B 1 377 ? 12.238  23.832  44.899  1.00 22.18 ? 369  LEU B CG  1 
ATOM   7532  C  CD1 . LEU B 1 377 ? 12.300  22.332  44.715  1.00 20.63 ? 369  LEU B CD1 1 
ATOM   7533  C  CD2 . LEU B 1 377 ? 13.254  24.266  45.940  1.00 21.67 ? 369  LEU B CD2 1 
ATOM   7534  N  N   . PRO B 1 378 ? 13.664  27.831  42.304  1.00 21.33 ? 370  PRO B N   1 
ATOM   7535  C  CA  . PRO B 1 378 ? 14.120  28.396  41.019  1.00 22.03 ? 370  PRO B CA  1 
ATOM   7536  C  C   . PRO B 1 378 ? 15.084  27.491  40.262  1.00 23.06 ? 370  PRO B C   1 
ATOM   7537  O  O   . PRO B 1 378 ? 15.297  27.699  39.056  1.00 22.79 ? 370  PRO B O   1 
ATOM   7538  C  CB  . PRO B 1 378 ? 14.796  29.712  41.440  1.00 21.65 ? 370  PRO B CB  1 
ATOM   7539  C  CG  . PRO B 1 378 ? 15.247  29.454  42.868  1.00 19.84 ? 370  PRO B CG  1 
ATOM   7540  C  CD  . PRO B 1 378 ? 14.133  28.621  43.458  1.00 21.04 ? 370  PRO B CD  1 
ATOM   7541  N  N   . GLU B 1 379 ? 15.676  26.495  40.928  1.00 13.46 ? 371  GLU B N   1 
ATOM   7542  C  CA  . GLU B 1 379 ? 16.548  25.534  40.265  1.00 12.75 ? 371  GLU B CA  1 
ATOM   7543  C  C   . GLU B 1 379 ? 15.792  24.459  39.487  1.00 15.11 ? 371  GLU B C   1 
ATOM   7544  O  O   . GLU B 1 379 ? 16.434  23.648  38.804  1.00 16.41 ? 371  GLU B O   1 
ATOM   7545  C  CB  . GLU B 1 379 ? 17.455  24.853  41.290  1.00 13.71 ? 371  GLU B CB  1 
ATOM   7546  C  CG  . GLU B 1 379 ? 16.706  24.057  42.363  1.00 13.53 ? 371  GLU B CG  1 
ATOM   7547  C  CD  . GLU B 1 379 ? 16.495  24.859  43.633  1.00 16.18 ? 371  GLU B CD  1 
ATOM   7548  O  OE1 . GLU B 1 379 ? 16.011  26.008  43.539  1.00 17.92 ? 371  GLU B OE1 1 
ATOM   7549  O  OE2 . GLU B 1 379 ? 16.818  24.348  44.729  1.00 19.26 ? 371  GLU B OE2 1 
ATOM   7550  N  N   . LEU B 1 380 ? 14.461  24.422  39.572  1.00 14.50 ? 372  LEU B N   1 
ATOM   7551  C  CA  . LEU B 1 380 ? 13.709  23.313  38.997  1.00 12.47 ? 372  LEU B CA  1 
ATOM   7552  C  C   . LEU B 1 380 ? 13.758  23.380  37.478  1.00 15.69 ? 372  LEU B C   1 
ATOM   7553  O  O   . LEU B 1 380 ? 13.489  24.432  36.892  1.00 21.01 ? 372  LEU B O   1 
ATOM   7554  C  CB  . LEU B 1 380 ? 12.249  23.354  39.461  1.00 15.80 ? 372  LEU B CB  1 
ATOM   7555  C  CG  . LEU B 1 380 ? 11.388  22.131  39.099  1.00 16.88 ? 372  LEU B CG  1 
ATOM   7556  C  CD1 . LEU B 1 380 ? 11.791  20.904  39.900  1.00 17.53 ? 372  LEU B CD1 1 
ATOM   7557  C  CD2 . LEU B 1 380 ? 9.897   22.436  39.289  1.00 18.73 ? 372  LEU B CD2 1 
ATOM   7558  N  N   . VAL B 1 381 ? 14.087  22.259  36.839  1.00 15.91 ? 373  VAL B N   1 
ATOM   7559  C  CA  . VAL B 1 381 ? 14.103  22.162  35.380  1.00 15.25 ? 373  VAL B CA  1 
ATOM   7560  C  C   . VAL B 1 381 ? 13.199  21.000  34.988  1.00 13.10 ? 373  VAL B C   1 
ATOM   7561  O  O   . VAL B 1 381 ? 13.420  19.861  35.408  1.00 17.99 ? 373  VAL B O   1 
ATOM   7562  C  CB  . VAL B 1 381 ? 15.528  21.977  34.830  1.00 14.20 ? 373  VAL B CB  1 
ATOM   7563  C  CG1 . VAL B 1 381 ? 15.504  21.719  33.332  1.00 11.28 ? 373  VAL B CG1 1 
ATOM   7564  C  CG2 . VAL B 1 381 ? 16.382  23.213  35.130  1.00 15.67 ? 373  VAL B CG2 1 
ATOM   7565  N  N   . GLY B 1 382 ? 12.153  21.296  34.230  1.00 12.38 ? 374  GLY B N   1 
ATOM   7566  C  CA  . GLY B 1 382 ? 11.220  20.278  33.800  1.00 16.74 ? 374  GLY B CA  1 
ATOM   7567  C  C   . GLY B 1 382 ? 11.574  19.730  32.438  1.00 12.40 ? 374  GLY B C   1 
ATOM   7568  O  O   . GLY B 1 382 ? 12.551  20.119  31.806  1.00 12.99 ? 374  GLY B O   1 
ATOM   7569  N  N   . GLY B 1 383 ? 10.742  18.809  31.972  1.00 11.51 ? 375  GLY B N   1 
ATOM   7570  C  CA  . GLY B 1 383 ? 10.944  18.300  30.637  1.00 16.05 ? 375  GLY B CA  1 
ATOM   7571  C  C   . GLY B 1 383 ? 10.070  17.102  30.378  1.00 14.28 ? 375  GLY B C   1 
ATOM   7572  O  O   . GLY B 1 383 ? 9.560   16.503  31.326  1.00 11.00 ? 375  GLY B O   1 
ATOM   7573  N  N   . SER B 1 384 ? 9.895   16.736  29.112  1.00 9.93  ? 376  SER B N   1 
ATOM   7574  C  CA  . SER B 1 384 ? 9.125   15.541  28.810  1.00 11.11 ? 376  SER B CA  1 
ATOM   7575  C  C   . SER B 1 384 ? 9.559   15.011  27.452  1.00 12.24 ? 376  SER B C   1 
ATOM   7576  O  O   . SER B 1 384 ? 10.093  15.747  26.614  1.00 13.62 ? 376  SER B O   1 
ATOM   7577  C  CB  . SER B 1 384 ? 7.618   15.815  28.831  1.00 11.80 ? 376  SER B CB  1 
ATOM   7578  O  OG  . SER B 1 384 ? 7.196   16.441  27.639  1.00 15.78 ? 376  SER B OG  1 
ATOM   7579  N  N   . ALA B 1 385 ? 9.318   13.718  27.250  1.00 13.12 ? 377  ALA B N   1 
ATOM   7580  C  CA  . ALA B 1 385 ? 9.624   13.072  25.979  1.00 9.79  ? 377  ALA B CA  1 
ATOM   7581  C  C   . ALA B 1 385 ? 8.383   13.134  25.096  1.00 12.00 ? 377  ALA B C   1 
ATOM   7582  O  O   . ALA B 1 385 ? 7.635   12.166  24.937  1.00 13.85 ? 377  ALA B O   1 
ATOM   7583  C  CB  . ALA B 1 385 ? 10.109  11.640  26.207  1.00 14.75 ? 377  ALA B CB  1 
ATOM   7584  N  N   . ASP B 1 386 ? 8.166   14.319  24.518  1.00 12.92 ? 378  ASP B N   1 
ATOM   7585  C  CA  . ASP B 1 386 ? 7.091   14.563  23.547  1.00 14.93 ? 378  ASP B CA  1 
ATOM   7586  C  C   . ASP B 1 386 ? 5.701   14.318  24.141  1.00 18.63 ? 378  ASP B C   1 
ATOM   7587  O  O   . ASP B 1 386 ? 4.794   13.862  23.440  1.00 15.21 ? 378  ASP B O   1 
ATOM   7588  C  CB  . ASP B 1 386 ? 7.286   13.723  22.271  1.00 14.81 ? 378  ASP B CB  1 
ATOM   7589  C  CG  . ASP B 1 386 ? 6.385   14.179  21.107  1.00 22.48 ? 378  ASP B CG  1 
ATOM   7590  O  OD1 . ASP B 1 386 ? 6.254   15.393  20.891  1.00 27.24 ? 378  ASP B OD1 1 
ATOM   7591  O  OD2 . ASP B 1 386 ? 5.810   13.323  20.411  1.00 22.60 ? 378  ASP B OD2 1 
ATOM   7592  N  N   . LEU B 1 387 ? 5.504   14.622  25.428  1.00 15.59 ? 379  LEU B N   1 
ATOM   7593  C  CA  . LEU B 1 387 ? 4.165   14.564  26.001  1.00 15.26 ? 379  LEU B CA  1 
ATOM   7594  C  C   . LEU B 1 387 ? 3.414   15.868  25.740  1.00 18.38 ? 379  LEU B C   1 
ATOM   7595  O  O   . LEU B 1 387 ? 4.001   16.949  25.673  1.00 22.48 ? 379  LEU B O   1 
ATOM   7596  C  CB  . LEU B 1 387 ? 4.213   14.312  27.515  1.00 17.34 ? 379  LEU B CB  1 
ATOM   7597  C  CG  . LEU B 1 387 ? 4.856   13.022  28.042  1.00 22.14 ? 379  LEU B CG  1 
ATOM   7598  C  CD1 . LEU B 1 387 ? 4.520   12.749  29.522  1.00 14.87 ? 379  LEU B CD1 1 
ATOM   7599  C  CD2 . LEU B 1 387 ? 4.496   11.835  27.186  1.00 24.85 ? 379  LEU B CD2 1 
ATOM   7600  N  N   . THR B 1 388 ? 2.102   15.760  25.619  1.00 18.18 ? 380  THR B N   1 
ATOM   7601  C  CA  . THR B 1 388 ? 1.266   16.953  25.631  1.00 21.92 ? 380  THR B CA  1 
ATOM   7602  C  C   . THR B 1 388 ? 1.387   17.635  26.991  1.00 23.75 ? 380  THR B C   1 
ATOM   7603  O  O   . THR B 1 388 ? 1.262   16.965  28.021  1.00 20.80 ? 380  THR B O   1 
ATOM   7604  C  CB  . THR B 1 388 ? -0.188  16.581  25.344  1.00 26.70 ? 380  THR B CB  1 
ATOM   7605  O  OG1 . THR B 1 388 ? -0.298  16.123  23.993  1.00 27.96 ? 380  THR B OG1 1 
ATOM   7606  C  CG2 . THR B 1 388 ? -1.111  17.775  25.546  1.00 31.52 ? 380  THR B CG2 1 
ATOM   7607  N  N   . PRO B 1 389 ? 1.653   18.940  27.043  1.00 30.72 ? 381  PRO B N   1 
ATOM   7608  C  CA  . PRO B 1 389 ? 1.828   19.595  28.347  1.00 33.73 ? 381  PRO B CA  1 
ATOM   7609  C  C   . PRO B 1 389 ? 0.533   19.567  29.145  1.00 27.57 ? 381  PRO B C   1 
ATOM   7610  O  O   . PRO B 1 389 ? -0.556  19.755  28.603  1.00 22.51 ? 381  PRO B O   1 
ATOM   7611  C  CB  . PRO B 1 389 ? 2.233   21.030  27.979  1.00 39.64 ? 381  PRO B CB  1 
ATOM   7612  C  CG  . PRO B 1 389 ? 2.615   20.981  26.523  1.00 35.04 ? 381  PRO B CG  1 
ATOM   7613  C  CD  . PRO B 1 389 ? 1.792   19.889  25.925  1.00 34.29 ? 381  PRO B CD  1 
ATOM   7614  N  N   . SER B 1 390 ? 0.659   19.318  30.444  1.00 23.73 ? 382  SER B N   1 
ATOM   7615  C  CA  . SER B 1 390 ? -0.499  19.300  31.328  1.00 21.94 ? 382  SER B CA  1 
ATOM   7616  C  C   . SER B 1 390 ? -0.026  19.621  32.736  1.00 18.03 ? 382  SER B C   1 
ATOM   7617  O  O   . SER B 1 390 ? 1.176   19.696  33.003  1.00 14.89 ? 382  SER B O   1 
ATOM   7618  C  CB  . SER B 1 390 ? -1.208  17.948  31.293  1.00 18.45 ? 382  SER B CB  1 
ATOM   7619  O  OG  . SER B 1 390 ? -0.487  16.987  32.059  1.00 20.08 ? 382  SER B OG  1 
ATOM   7620  N  N   . ASN B 1 391 ? -0.991  19.765  33.647  1.00 18.97 ? 383  ASN B N   1 
ATOM   7621  C  CA  . ASN B 1 391 ? -0.675  20.009  35.052  1.00 19.70 ? 383  ASN B CA  1 
ATOM   7622  C  C   . ASN B 1 391 ? 0.196   18.913  35.658  1.00 17.18 ? 383  ASN B C   1 
ATOM   7623  O  O   . ASN B 1 391 ? 0.879   19.163  36.658  1.00 23.71 ? 383  ASN B O   1 
ATOM   7624  C  CB  . ASN B 1 391 ? -1.965  20.144  35.872  1.00 24.78 ? 383  ASN B CB  1 
ATOM   7625  C  CG  . ASN B 1 391 ? -2.750  18.823  35.968  1.00 31.29 ? 383  ASN B CG  1 
ATOM   7626  O  OD1 . ASN B 1 391 ? -3.025  18.165  34.960  1.00 35.66 ? 383  ASN B OD1 1 
ATOM   7627  N  ND2 . ASN B 1 391 ? -3.106  18.438  37.189  1.00 36.07 ? 383  ASN B ND2 1 
ATOM   7628  N  N   . LEU B 1 392 ? 0.196   17.715  35.076  1.00 15.99 ? 384  LEU B N   1 
ATOM   7629  C  CA  . LEU B 1 392 ? 0.994   16.609  35.606  1.00 15.95 ? 384  LEU B CA  1 
ATOM   7630  C  C   . LEU B 1 392 ? 2.466   16.681  35.241  1.00 18.29 ? 384  LEU B C   1 
ATOM   7631  O  O   . LEU B 1 392 ? 3.276   16.017  35.893  1.00 20.97 ? 384  LEU B O   1 
ATOM   7632  C  CB  . LEU B 1 392 ? 0.451   15.271  35.106  1.00 15.49 ? 384  LEU B CB  1 
ATOM   7633  C  CG  . LEU B 1 392 ? -0.950  14.915  35.591  1.00 19.46 ? 384  LEU B CG  1 
ATOM   7634  C  CD1 . LEU B 1 392 ? -1.319  13.526  35.096  1.00 23.08 ? 384  LEU B CD1 1 
ATOM   7635  C  CD2 . LEU B 1 392 ? -1.016  15.004  37.110  1.00 24.43 ? 384  LEU B CD2 1 
ATOM   7636  N  N   . THR B 1 393 ? 2.832   17.428  34.195  1.00 16.18 ? 385  THR B N   1 
ATOM   7637  C  CA  . THR B 1 393 ? 4.184   17.386  33.658  1.00 17.14 ? 385  THR B CA  1 
ATOM   7638  C  C   . THR B 1 393 ? 4.773   18.759  33.358  1.00 16.03 ? 385  THR B C   1 
ATOM   7639  O  O   . THR B 1 393 ? 5.890   18.831  32.831  1.00 14.33 ? 385  THR B O   1 
ATOM   7640  C  CB  . THR B 1 393 ? 4.214   16.558  32.366  1.00 23.57 ? 385  THR B CB  1 
ATOM   7641  O  OG1 . THR B 1 393 ? 3.386   17.199  31.395  1.00 18.29 ? 385  THR B OG1 1 
ATOM   7642  C  CG2 . THR B 1 393 ? 3.706   15.133  32.612  1.00 19.36 ? 385  THR B CG2 1 
ATOM   7643  N  N   . ASP B 1 394 ? 4.053   19.841  33.653  1.00 15.08 ? 386  ASP B N   1 
ATOM   7644  C  CA  . ASP B 1 394 ? 4.503   21.182  33.308  1.00 20.69 ? 386  ASP B CA  1 
ATOM   7645  C  C   . ASP B 1 394 ? 3.857   22.162  34.278  1.00 22.84 ? 386  ASP B C   1 
ATOM   7646  O  O   . ASP B 1 394 ? 2.973   21.798  35.059  1.00 21.60 ? 386  ASP B O   1 
ATOM   7647  C  CB  . ASP B 1 394 ? 4.152   21.512  31.851  1.00 22.44 ? 386  ASP B CB  1 
ATOM   7648  C  CG  . ASP B 1 394 ? 4.885   22.744  31.329  1.00 23.99 ? 386  ASP B CG  1 
ATOM   7649  O  OD1 . ASP B 1 394 ? 5.754   23.298  32.037  1.00 21.72 ? 386  ASP B OD1 1 
ATOM   7650  O  OD2 . ASP B 1 394 ? 4.585   23.151  30.195  1.00 28.20 ? 386  ASP B OD2 1 
ATOM   7651  N  N   . TRP B 1 395 ? 4.322   23.411  34.233  1.00 16.84 ? 387  TRP B N   1 
ATOM   7652  C  CA  . TRP B 1 395 ? 3.698   24.494  34.986  1.00 18.76 ? 387  TRP B CA  1 
ATOM   7653  C  C   . TRP B 1 395 ? 3.677   25.743  34.115  1.00 19.74 ? 387  TRP B C   1 
ATOM   7654  O  O   . TRP B 1 395 ? 4.430   25.857  33.145  1.00 18.64 ? 387  TRP B O   1 
ATOM   7655  C  CB  . TRP B 1 395 ? 4.416   24.746  36.333  1.00 21.01 ? 387  TRP B CB  1 
ATOM   7656  C  CG  . TRP B 1 395 ? 5.787   25.392  36.269  1.00 17.15 ? 387  TRP B CG  1 
ATOM   7657  C  CD1 . TRP B 1 395 ? 6.081   26.684  36.579  1.00 15.80 ? 387  TRP B CD1 1 
ATOM   7658  C  CD2 . TRP B 1 395 ? 7.042   24.765  35.939  1.00 17.87 ? 387  TRP B CD2 1 
ATOM   7659  N  NE1 . TRP B 1 395 ? 7.423   26.914  36.438  1.00 15.33 ? 387  TRP B NE1 1 
ATOM   7660  C  CE2 . TRP B 1 395 ? 8.040   25.754  36.051  1.00 16.69 ? 387  TRP B CE2 1 
ATOM   7661  C  CE3 . TRP B 1 395 ? 7.413   23.477  35.541  1.00 18.24 ? 387  TRP B CE3 1 
ATOM   7662  C  CZ2 . TRP B 1 395 ? 9.385   25.499  35.784  1.00 19.24 ? 387  TRP B CZ2 1 
ATOM   7663  C  CZ3 . TRP B 1 395 ? 8.756   23.218  35.287  1.00 21.94 ? 387  TRP B CZ3 1 
ATOM   7664  C  CH2 . TRP B 1 395 ? 9.723   24.228  35.403  1.00 19.82 ? 387  TRP B CH2 1 
ATOM   7665  N  N   . SER B 1 396 ? 2.797   26.684  34.466  1.00 19.68 ? 388  SER B N   1 
ATOM   7666  C  CA  . SER B 1 396 ? 2.475   27.759  33.533  1.00 24.07 ? 388  SER B CA  1 
ATOM   7667  C  C   . SER B 1 396 ? 3.685   28.641  33.240  1.00 21.15 ? 388  SER B C   1 
ATOM   7668  O  O   . SER B 1 396 ? 3.813   29.158  32.126  1.00 24.52 ? 388  SER B O   1 
ATOM   7669  C  CB  . SER B 1 396 ? 1.303   28.592  34.062  1.00 27.11 ? 388  SER B CB  1 
ATOM   7670  O  OG  . SER B 1 396 ? 1.621   29.223  35.290  1.00 36.10 ? 388  SER B OG  1 
ATOM   7671  N  N   . ASN B 1 397 ? 4.604   28.777  34.194  1.00 19.38 ? 389  ASN B N   1 
ATOM   7672  C  CA  . ASN B 1 397 ? 5.738   29.686  34.061  1.00 26.83 ? 389  ASN B CA  1 
ATOM   7673  C  C   . ASN B 1 397 ? 6.963   29.074  33.390  1.00 19.81 ? 389  ASN B C   1 
ATOM   7674  O  O   . ASN B 1 397 ? 7.948   29.794  33.196  1.00 22.81 ? 389  ASN B O   1 
ATOM   7675  C  CB  . ASN B 1 397 ? 6.144   30.226  35.437  1.00 26.34 ? 389  ASN B CB  1 
ATOM   7676  C  CG  . ASN B 1 397 ? 5.141   31.207  35.983  1.00 29.51 ? 389  ASN B CG  1 
ATOM   7677  O  OD1 . ASN B 1 397 ? 4.440   31.870  35.221  1.00 32.74 ? 389  ASN B OD1 1 
ATOM   7678  N  ND2 . ASN B 1 397 ? 5.053   31.298  37.304  1.00 30.13 ? 389  ASN B ND2 1 
ATOM   7679  N  N   . SER B 1 398 ? 6.945   27.789  33.025  1.00 15.63 ? 390  SER B N   1 
ATOM   7680  C  CA  . SER B 1 398 ? 8.158   27.181  32.480  1.00 17.78 ? 390  SER B CA  1 
ATOM   7681  C  C   . SER B 1 398 ? 8.543   27.835  31.153  1.00 18.81 ? 390  SER B C   1 
ATOM   7682  O  O   . SER B 1 398 ? 7.693   28.298  30.384  1.00 18.83 ? 390  SER B O   1 
ATOM   7683  C  CB  . SER B 1 398 ? 7.994   25.666  32.299  1.00 18.08 ? 390  SER B CB  1 
ATOM   7684  O  OG  . SER B 1 398 ? 7.142   25.344  31.219  1.00 19.95 ? 390  SER B OG  1 
ATOM   7685  N  N   . VAL B 1 399 ? 9.848   27.891  30.907  1.00 14.84 ? 391  VAL B N   1 
ATOM   7686  C  CA  . VAL B 1 399 ? 10.438  28.556  29.750  1.00 16.46 ? 391  VAL B CA  1 
ATOM   7687  C  C   . VAL B 1 399 ? 11.209  27.502  28.972  1.00 20.31 ? 391  VAL B C   1 
ATOM   7688  O  O   . VAL B 1 399 ? 12.208  26.972  29.471  1.00 17.32 ? 391  VAL B O   1 
ATOM   7689  C  CB  . VAL B 1 399 ? 11.373  29.710  30.167  1.00 19.20 ? 391  VAL B CB  1 
ATOM   7690  C  CG1 . VAL B 1 399 ? 12.130  30.249  28.958  1.00 17.62 ? 391  VAL B CG1 1 
ATOM   7691  C  CG2 . VAL B 1 399 ? 10.592  30.830  30.877  1.00 25.80 ? 391  VAL B CG2 1 
ATOM   7692  N  N   . SER B 1 400 ? 10.761  27.212  27.750  1.00 19.54 ? 392  SER B N   1 
ATOM   7693  C  CA  . SER B 1 400 ? 11.399  26.188  26.931  1.00 14.15 ? 392  SER B CA  1 
ATOM   7694  C  C   . SER B 1 400 ? 12.838  26.565  26.596  1.00 19.01 ? 392  SER B C   1 
ATOM   7695  O  O   . SER B 1 400 ? 13.102  27.657  26.092  1.00 14.99 ? 392  SER B O   1 
ATOM   7696  C  CB  . SER B 1 400 ? 10.609  25.990  25.634  1.00 24.99 ? 392  SER B CB  1 
ATOM   7697  O  OG  . SER B 1 400 ? 9.311   25.523  25.904  1.00 28.76 ? 392  SER B OG  1 
ATOM   7698  N  N   . VAL B 1 401 ? 13.768  25.648  26.869  1.00 16.72 ? 393  VAL B N   1 
ATOM   7699  C  CA  . VAL B 1 401 ? 15.153  25.826  26.437  1.00 14.26 ? 393  VAL B CA  1 
ATOM   7700  C  C   . VAL B 1 401 ? 15.239  25.712  24.921  1.00 18.78 ? 393  VAL B C   1 
ATOM   7701  O  O   . VAL B 1 401 ? 14.616  24.835  24.305  1.00 15.28 ? 393  VAL B O   1 
ATOM   7702  C  CB  . VAL B 1 401 ? 16.058  24.785  27.122  1.00 14.49 ? 393  VAL B CB  1 
ATOM   7703  C  CG1 . VAL B 1 401 ? 17.482  24.800  26.536  1.00 12.72 ? 393  VAL B CG1 1 
ATOM   7704  C  CG2 . VAL B 1 401 ? 16.058  25.001  28.627  1.00 14.62 ? 393  VAL B CG2 1 
ATOM   7705  N  N   . THR B 1 402 ? 16.007  26.605  24.302  1.00 18.45 ? 394  THR B N   1 
ATOM   7706  C  CA  . THR B 1 402 ? 16.173  26.586  22.852  1.00 21.33 ? 394  THR B CA  1 
ATOM   7707  C  C   . THR B 1 402 ? 17.657  26.704  22.513  1.00 19.36 ? 394  THR B C   1 
ATOM   7708  O  O   . THR B 1 402 ? 18.508  26.869  23.391  1.00 15.76 ? 394  THR B O   1 
ATOM   7709  C  CB  . THR B 1 402 ? 15.395  27.721  22.174  1.00 20.29 ? 394  THR B CB  1 
ATOM   7710  O  OG1 . THR B 1 402 ? 15.935  28.979  22.586  1.00 22.69 ? 394  THR B OG1 1 
ATOM   7711  C  CG2 . THR B 1 402 ? 13.907  27.682  22.525  1.00 24.26 ? 394  THR B CG2 1 
ATOM   7712  N  N   . ARG B 1 403 ? 17.956  26.642  21.212  1.00 20.08 ? 395  ARG B N   1 
ATOM   7713  C  CA  . ARG B 1 403 ? 19.337  26.784  20.764  1.00 25.01 ? 395  ARG B CA  1 
ATOM   7714  C  C   . ARG B 1 403 ? 19.931  28.108  21.229  1.00 24.13 ? 395  ARG B C   1 
ATOM   7715  O  O   . ARG B 1 403 ? 21.088  28.165  21.657  1.00 24.37 ? 395  ARG B O   1 
ATOM   7716  C  CB  . ARG B 1 403 ? 19.409  26.674  19.236  1.00 25.04 ? 395  ARG B CB  1 
ATOM   7717  C  CG  . ARG B 1 403 ? 20.829  26.603  18.690  1.00 27.07 ? 395  ARG B CG  1 
ATOM   7718  C  CD  . ARG B 1 403 ? 20.879  26.741  17.168  1.00 32.71 ? 395  ARG B CD  1 
ATOM   7719  N  NE  . ARG B 1 403 ? 22.206  26.378  16.677  1.00 37.55 ? 395  ARG B NE  1 
ATOM   7720  C  CZ  . ARG B 1 403 ? 22.576  25.135  16.374  1.00 37.98 ? 395  ARG B CZ  1 
ATOM   7721  N  NH1 . ARG B 1 403 ? 21.707  24.137  16.494  1.00 37.75 ? 395  ARG B NH1 1 
ATOM   7722  N  NH2 . ARG B 1 403 ? 23.811  24.887  15.946  1.00 28.89 ? 395  ARG B NH2 1 
ATOM   7723  N  N   . ASP B 1 404 ? 19.145  29.178  21.185  1.00 21.20 ? 396  ASP B N   1 
ATOM   7724  C  CA  . ASP B 1 404 ? 19.683  30.514  21.382  1.00 27.94 ? 396  ASP B CA  1 
ATOM   7725  C  C   . ASP B 1 404 ? 19.439  31.097  22.768  1.00 28.42 ? 396  ASP B C   1 
ATOM   7726  O  O   . ASP B 1 404 ? 20.015  32.148  23.076  1.00 25.00 ? 396  ASP B O   1 
ATOM   7727  C  CB  . ASP B 1 404 ? 19.107  31.458  20.327  1.00 38.94 ? 396  ASP B CB  1 
ATOM   7728  C  CG  . ASP B 1 404 ? 19.490  31.052  18.922  1.00 44.41 ? 396  ASP B CG  1 
ATOM   7729  O  OD1 . ASP B 1 404 ? 20.578  30.463  18.750  1.00 41.56 ? 396  ASP B OD1 1 
ATOM   7730  O  OD2 . ASP B 1 404 ? 18.706  31.321  17.989  1.00 50.21 ? 396  ASP B OD2 1 
ATOM   7731  N  N   . LYS B 1 405 ? 18.626  30.462  23.615  1.00 22.10 ? 397  LYS B N   1 
ATOM   7732  C  CA  . LYS B 1 405 ? 18.324  31.063  24.907  1.00 26.54 ? 397  LYS B CA  1 
ATOM   7733  C  C   . LYS B 1 405 ? 18.151  29.985  25.965  1.00 23.38 ? 397  LYS B C   1 
ATOM   7734  O  O   . LYS B 1 405 ? 17.855  28.825  25.663  1.00 25.13 ? 397  LYS B O   1 
ATOM   7735  C  CB  . LYS B 1 405 ? 17.069  31.943  24.837  1.00 34.30 ? 397  LYS B CB  1 
ATOM   7736  N  N   . GLY B 1 406 ? 18.346  30.385  27.219  1.00 23.45 ? 398  GLY B N   1 
ATOM   7737  C  CA  . GLY B 1 406 ? 18.168  29.479  28.335  1.00 17.09 ? 398  GLY B CA  1 
ATOM   7738  C  C   . GLY B 1 406 ? 16.696  29.233  28.636  1.00 18.04 ? 398  GLY B C   1 
ATOM   7739  O  O   . GLY B 1 406 ? 15.796  29.573  27.871  1.00 22.53 ? 398  GLY B O   1 
ATOM   7740  N  N   . GLY B 1 407 ? 16.461  28.635  29.792  1.00 19.39 ? 399  GLY B N   1 
ATOM   7741  C  CA  . GLY B 1 407 ? 15.123  28.251  30.188  1.00 20.80 ? 399  GLY B CA  1 
ATOM   7742  C  C   . GLY B 1 407 ? 15.191  27.174  31.249  1.00 16.63 ? 399  GLY B C   1 
ATOM   7743  O  O   . GLY B 1 407 ? 16.269  26.791  31.710  1.00 18.53 ? 399  GLY B O   1 
ATOM   7744  N  N   . ASN B 1 408 ? 14.008  26.687  31.635  1.00 13.73 ? 400  ASN B N   1 
ATOM   7745  C  CA  . ASN B 1 408 ? 13.924  25.655  32.669  1.00 16.00 ? 400  ASN B CA  1 
ATOM   7746  C  C   . ASN B 1 408 ? 12.965  24.534  32.272  1.00 17.57 ? 400  ASN B C   1 
ATOM   7747  O  O   . ASN B 1 408 ? 12.377  23.874  33.134  1.00 14.82 ? 400  ASN B O   1 
ATOM   7748  C  CB  . ASN B 1 408 ? 13.524  26.260  34.022  1.00 16.40 ? 400  ASN B CB  1 
ATOM   7749  C  CG  . ASN B 1 408 ? 12.287  27.133  33.931  1.00 20.03 ? 400  ASN B CG  1 
ATOM   7750  O  OD1 . ASN B 1 408 ? 11.611  27.162  32.901  1.00 20.00 ? 400  ASN B OD1 1 
ATOM   7751  N  ND2 . ASN B 1 408 ? 11.982  27.857  35.017  1.00 18.60 ? 400  ASN B ND2 1 
ATOM   7752  N  N   . TYR B 1 409 ? 12.809  24.293  30.973  1.00 12.00 ? 401  TYR B N   1 
ATOM   7753  C  CA  . TYR B 1 409 ? 11.977  23.192  30.506  1.00 14.04 ? 401  TYR B CA  1 
ATOM   7754  C  C   . TYR B 1 409 ? 12.571  22.656  29.216  1.00 11.47 ? 401  TYR B C   1 
ATOM   7755  O  O   . TYR B 1 409 ? 12.824  23.425  28.288  1.00 14.52 ? 401  TYR B O   1 
ATOM   7756  C  CB  . TYR B 1 409 ? 10.523  23.640  30.280  1.00 14.54 ? 401  TYR B CB  1 
ATOM   7757  C  CG  . TYR B 1 409 ? 9.596   22.469  30.313  1.00 16.15 ? 401  TYR B CG  1 
ATOM   7758  C  CD1 . TYR B 1 409 ? 9.356   21.718  29.171  1.00 17.38 ? 401  TYR B CD1 1 
ATOM   7759  C  CD2 . TYR B 1 409 ? 9.004   22.071  31.502  1.00 11.88 ? 401  TYR B CD2 1 
ATOM   7760  C  CE1 . TYR B 1 409 ? 8.519   20.612  29.207  1.00 17.97 ? 401  TYR B CE1 1 
ATOM   7761  C  CE2 . TYR B 1 409 ? 8.167   20.965  31.548  1.00 17.00 ? 401  TYR B CE2 1 
ATOM   7762  C  CZ  . TYR B 1 409 ? 7.932   20.241  30.397  1.00 19.37 ? 401  TYR B CZ  1 
ATOM   7763  O  OH  . TYR B 1 409 ? 7.113   19.135  30.433  1.00 19.11 ? 401  TYR B OH  1 
ATOM   7764  N  N   . ILE B 1 410 ? 12.790  21.347  29.159  1.00 11.07 ? 402  ILE B N   1 
ATOM   7765  C  CA  . ILE B 1 410 ? 13.508  20.722  28.056  1.00 10.66 ? 402  ILE B CA  1 
ATOM   7766  C  C   . ILE B 1 410 ? 12.539  19.830  27.304  1.00 14.79 ? 402  ILE B C   1 
ATOM   7767  O  O   . ILE B 1 410 ? 11.961  18.908  27.885  1.00 12.19 ? 402  ILE B O   1 
ATOM   7768  C  CB  . ILE B 1 410 ? 14.712  19.910  28.556  1.00 14.31 ? 402  ILE B CB  1 
ATOM   7769  C  CG1 . ILE B 1 410 ? 15.693  20.831  29.287  1.00 18.52 ? 402  ILE B CG1 1 
ATOM   7770  C  CG2 . ILE B 1 410 ? 15.391  19.178  27.387  1.00 10.54 ? 402  ILE B CG2 1 
ATOM   7771  C  CD1 . ILE B 1 410 ? 16.690  20.076  30.153  1.00 21.79 ? 402  ILE B CD1 1 
ATOM   7772  N  N   . HIS B 1 411 ? 12.389  20.082  26.009  1.00 17.50 ? 403  HIS B N   1 
ATOM   7773  C  CA  . HIS B 1 411 ? 11.620  19.208  25.126  1.00 11.16 ? 403  HIS B CA  1 
ATOM   7774  C  C   . HIS B 1 411 ? 12.567  18.145  24.576  1.00 11.84 ? 403  HIS B C   1 
ATOM   7775  O  O   . HIS B 1 411 ? 13.377  18.414  23.683  1.00 13.44 ? 403  HIS B O   1 
ATOM   7776  C  CB  . HIS B 1 411 ? 10.968  20.023  24.018  1.00 12.00 ? 403  HIS B CB  1 
ATOM   7777  C  CG  . HIS B 1 411 ? 10.097  21.127  24.534  1.00 23.22 ? 403  HIS B CG  1 
ATOM   7778  N  ND1 . HIS B 1 411 ? 8.916   20.892  25.209  1.00 24.87 ? 403  HIS B ND1 1 
ATOM   7779  C  CD2 . HIS B 1 411 ? 10.241  22.472  24.488  1.00 22.83 ? 403  HIS B CD2 1 
ATOM   7780  C  CE1 . HIS B 1 411 ? 8.364   22.045  25.544  1.00 22.41 ? 403  HIS B CE1 1 
ATOM   7781  N  NE2 . HIS B 1 411 ? 9.143   23.020  25.112  1.00 22.52 ? 403  HIS B NE2 1 
ATOM   7782  N  N   . TYR B 1 412 ? 12.494  16.942  25.146  1.00 11.33 ? 404  TYR B N   1 
ATOM   7783  C  CA  . TYR B 1 412 ? 13.379  15.857  24.756  1.00 10.13 ? 404  TYR B CA  1 
ATOM   7784  C  C   . TYR B 1 412 ? 12.988  15.200  23.441  1.00 13.51 ? 404  TYR B C   1 
ATOM   7785  O  O   . TYR B 1 412 ? 13.813  14.467  22.884  1.00 15.36 ? 404  TYR B O   1 
ATOM   7786  C  CB  . TYR B 1 412 ? 13.426  14.807  25.871  1.00 9.26  ? 404  TYR B CB  1 
ATOM   7787  C  CG  . TYR B 1 412 ? 14.119  15.311  27.117  1.00 12.51 ? 404  TYR B CG  1 
ATOM   7788  C  CD1 . TYR B 1 412 ? 15.506  15.244  27.232  1.00 14.39 ? 404  TYR B CD1 1 
ATOM   7789  C  CD2 . TYR B 1 412 ? 13.392  15.848  28.181  1.00 11.74 ? 404  TYR B CD2 1 
ATOM   7790  C  CE1 . TYR B 1 412 ? 16.156  15.698  28.363  1.00 12.12 ? 404  TYR B CE1 1 
ATOM   7791  C  CE2 . TYR B 1 412 ? 14.038  16.311  29.329  1.00 10.95 ? 404  TYR B CE2 1 
ATOM   7792  C  CZ  . TYR B 1 412 ? 15.423  16.227  29.412  1.00 14.36 ? 404  TYR B CZ  1 
ATOM   7793  O  OH  . TYR B 1 412 ? 16.093  16.682  30.537  1.00 14.90 ? 404  TYR B OH  1 
ATOM   7794  N  N   . GLY B 1 413 ? 11.769  15.443  22.922  1.00 12.34 ? 405  GLY B N   1 
ATOM   7795  C  CA  . GLY B 1 413 ? 11.344  14.679  21.752  1.00 10.98 ? 405  GLY B CA  1 
ATOM   7796  C  C   . GLY B 1 413 ? 11.093  13.225  22.132  1.00 11.57 ? 405  GLY B C   1 
ATOM   7797  O  O   . GLY B 1 413 ? 10.998  12.873  23.305  1.00 11.67 ? 405  GLY B O   1 
ATOM   7798  N  N   . VAL B 1 414 ? 10.991  12.367  21.114  1.00 12.60 ? 406  VAL B N   1 
ATOM   7799  C  CA  . VAL B 1 414 ? 10.645  10.965  21.348  1.00 13.03 ? 406  VAL B CA  1 
ATOM   7800  C  C   . VAL B 1 414 ? 11.931  10.204  21.648  1.00 12.56 ? 406  VAL B C   1 
ATOM   7801  O  O   . VAL B 1 414 ? 12.408  9.406   20.831  1.00 10.27 ? 406  VAL B O   1 
ATOM   7802  C  CB  . VAL B 1 414 ? 9.875   10.371  20.147  1.00 16.18 ? 406  VAL B CB  1 
ATOM   7803  C  CG1 . VAL B 1 414 ? 9.253   9.041   20.512  1.00 16.03 ? 406  VAL B CG1 1 
ATOM   7804  C  CG2 . VAL B 1 414 ? 8.802   11.333  19.694  1.00 14.36 ? 406  VAL B CG2 1 
ATOM   7805  N  N   . ARG B 1 415 ? 12.500  10.453  22.836  1.00 10.06 ? 407  ARG B N   1 
ATOM   7806  C  CA  . ARG B 1 415 ? 13.872  10.097  23.195  1.00 9.22  ? 407  ARG B CA  1 
ATOM   7807  C  C   . ARG B 1 415 ? 13.919  9.821   24.699  1.00 8.76  ? 407  ARG B C   1 
ATOM   7808  O  O   . ARG B 1 415 ? 14.527  10.548  25.472  1.00 10.83 ? 407  ARG B O   1 
ATOM   7809  C  CB  . ARG B 1 415 ? 14.860  11.207  22.836  1.00 9.34  ? 407  ARG B CB  1 
ATOM   7810  C  CG  . ARG B 1 415 ? 14.915  11.616  21.361  1.00 12.04 ? 407  ARG B CG  1 
ATOM   7811  C  CD  . ARG B 1 415 ? 15.992  12.709  21.180  1.00 16.37 ? 407  ARG B CD  1 
ATOM   7812  N  NE  . ARG B 1 415 ? 16.067  13.200  19.802  1.00 10.80 ? 407  ARG B NE  1 
ATOM   7813  C  CZ  . ARG B 1 415 ? 15.486  14.316  19.364  1.00 13.27 ? 407  ARG B CZ  1 
ATOM   7814  N  NH1 . ARG B 1 415 ? 14.778  15.084  20.182  1.00 13.20 ? 407  ARG B NH1 1 
ATOM   7815  N  NH2 . ARG B 1 415 ? 15.616  14.665  18.097  1.00 16.01 ? 407  ARG B NH2 1 
ATOM   7816  N  N   . GLU B 1 416 ? 13.293  8.727   25.124  1.00 9.30  ? 408  GLU B N   1 
ATOM   7817  C  CA  . GLU B 1 416 ? 13.142  8.482   26.560  1.00 9.06  ? 408  GLU B CA  1 
ATOM   7818  C  C   . GLU B 1 416 ? 14.464  8.103   27.214  1.00 8.12  ? 408  GLU B C   1 
ATOM   7819  O  O   . GLU B 1 416 ? 14.791  8.593   28.303  1.00 11.61 ? 408  GLU B O   1 
ATOM   7820  C  CB  . GLU B 1 416 ? 12.097  7.389   26.792  1.00 9.89  ? 408  GLU B CB  1 
ATOM   7821  C  CG  . GLU B 1 416 ? 10.677  7.792   26.376  1.00 9.00  ? 408  GLU B CG  1 
ATOM   7822  C  CD  . GLU B 1 416 ? 10.407  7.522   24.901  1.00 14.28 ? 408  GLU B CD  1 
ATOM   7823  O  OE1 . GLU B 1 416 ? 11.245  6.865   24.251  1.00 13.18 ? 408  GLU B OE1 1 
ATOM   7824  O  OE2 . GLU B 1 416 ? 9.364   7.976   24.386  1.00 13.13 ? 408  GLU B OE2 1 
ATOM   7825  N  N   . PHE B 1 417 ? 15.218  7.183   26.600  1.00 8.17  ? 409  PHE B N   1 
ATOM   7826  C  CA  . PHE B 1 417 ? 16.509  6.800   27.178  1.00 15.36 ? 409  PHE B CA  1 
ATOM   7827  C  C   . PHE B 1 417 ? 17.432  8.004   27.216  1.00 13.09 ? 409  PHE B C   1 
ATOM   7828  O  O   . PHE B 1 417 ? 18.066  8.286   28.241  1.00 10.43 ? 409  PHE B O   1 
ATOM   7829  C  CB  . PHE B 1 417 ? 17.136  5.656   26.371  1.00 14.13 ? 409  PHE B CB  1 
ATOM   7830  C  CG  . PHE B 1 417 ? 18.182  4.838   27.115  1.00 12.68 ? 409  PHE B CG  1 
ATOM   7831  C  CD1 . PHE B 1 417 ? 18.622  5.173   28.394  1.00 9.18  ? 409  PHE B CD1 1 
ATOM   7832  C  CD2 . PHE B 1 417 ? 18.709  3.709   26.514  1.00 10.67 ? 409  PHE B CD2 1 
ATOM   7833  C  CE1 . PHE B 1 417 ? 19.590  4.401   29.045  1.00 10.96 ? 409  PHE B CE1 1 
ATOM   7834  C  CE2 . PHE B 1 417 ? 19.671  2.921   27.160  1.00 14.37 ? 409  PHE B CE2 1 
ATOM   7835  C  CZ  . PHE B 1 417 ? 20.104  3.275   28.432  1.00 12.59 ? 409  PHE B CZ  1 
ATOM   7836  N  N   . GLY B 1 418 ? 17.493  8.749   26.108  1.00 11.89 ? 410  GLY B N   1 
ATOM   7837  C  CA  . GLY B 1 418 ? 18.264  9.979   26.109  1.00 11.55 ? 410  GLY B CA  1 
ATOM   7838  C  C   . GLY B 1 418 ? 17.823  10.927  27.206  1.00 12.11 ? 410  GLY B C   1 
ATOM   7839  O  O   . GLY B 1 418 ? 18.654  11.526  27.891  1.00 10.80 ? 410  GLY B O   1 
ATOM   7840  N  N   . MET B 1 419 ? 16.507  11.066  27.400  1.00 9.86  ? 411  MET B N   1 
ATOM   7841  C  CA  . MET B 1 419 ? 16.022  11.948  28.457  1.00 11.95 ? 411  MET B CA  1 
ATOM   7842  C  C   . MET B 1 419 ? 16.551  11.507  29.819  1.00 11.31 ? 411  MET B C   1 
ATOM   7843  O  O   . MET B 1 419 ? 17.123  12.314  30.561  1.00 10.47 ? 411  MET B O   1 
ATOM   7844  C  CB  . MET B 1 419 ? 14.489  11.988  28.458  1.00 8.14  ? 411  MET B CB  1 
ATOM   7845  C  CG  . MET B 1 419 ? 13.918  12.719  29.666  1.00 10.23 ? 411  MET B CG  1 
ATOM   7846  S  SD  . MET B 1 419 ? 12.119  12.835  29.606  1.00 11.49 ? 411  MET B SD  1 
ATOM   7847  C  CE  . MET B 1 419 ? 11.620  11.183  30.070  1.00 11.38 ? 411  MET B CE  1 
ATOM   7848  N  N   . GLY B 1 420 ? 16.383  10.224  30.157  1.00 10.27 ? 412  GLY B N   1 
ATOM   7849  C  CA  . GLY B 1 420 ? 16.800  9.753   31.474  1.00 13.77 ? 412  GLY B CA  1 
ATOM   7850  C  C   . GLY B 1 420 ? 18.291  9.944   31.719  1.00 12.17 ? 412  GLY B C   1 
ATOM   7851  O  O   . GLY B 1 420 ? 18.708  10.453  32.762  1.00 8.44  ? 412  GLY B O   1 
ATOM   7852  N  N   . ALA B 1 421 ? 19.112  9.572   30.744  1.00 7.70  ? 413  ALA B N   1 
ATOM   7853  C  CA  . ALA B 1 421 ? 20.554  9.685   30.940  1.00 10.51 ? 413  ALA B CA  1 
ATOM   7854  C  C   . ALA B 1 421 ? 21.022  11.137  30.894  1.00 11.60 ? 413  ALA B C   1 
ATOM   7855  O  O   . ALA B 1 421 ? 22.001  11.490  31.565  1.00 11.20 ? 413  ALA B O   1 
ATOM   7856  C  CB  . ALA B 1 421 ? 21.281  8.843   29.899  1.00 11.91 ? 413  ALA B CB  1 
ATOM   7857  N  N   . ILE B 1 422 ? 20.341  11.994  30.129  1.00 9.50  ? 414  ILE B N   1 
ATOM   7858  C  CA  . ILE B 1 422 ? 20.674  13.420  30.149  1.00 10.55 ? 414  ILE B CA  1 
ATOM   7859  C  C   . ILE B 1 422 ? 20.334  14.024  31.508  1.00 13.43 ? 414  ILE B C   1 
ATOM   7860  O  O   . ILE B 1 422 ? 21.105  14.828  32.058  1.00 11.47 ? 414  ILE B O   1 
ATOM   7861  C  CB  . ILE B 1 422 ? 19.964  14.158  28.997  1.00 11.47 ? 414  ILE B CB  1 
ATOM   7862  C  CG1 . ILE B 1 422 ? 20.676  13.867  27.663  1.00 8.59  ? 414  ILE B CG1 1 
ATOM   7863  C  CG2 . ILE B 1 422 ? 19.867  15.680  29.284  1.00 9.76  ? 414  ILE B CG2 1 
ATOM   7864  C  CD1 . ILE B 1 422 ? 19.900  14.330  26.405  1.00 9.78  ? 414  ILE B CD1 1 
ATOM   7865  N  N   . MET B 1 423 ? 19.179  13.647  32.075  1.00 12.24 ? 415  MET B N   1 
ATOM   7866  C  CA  A MET B 1 423 ? 18.808  14.115  33.413  0.59 12.90 ? 415  MET B CA  1 
ATOM   7867  C  CA  B MET B 1 423 ? 18.829  14.145  33.402  0.41 12.09 ? 415  MET B CA  1 
ATOM   7868  C  C   . MET B 1 423 ? 19.868  13.739  34.442  1.00 8.63  ? 415  MET B C   1 
ATOM   7869  O  O   . MET B 1 423 ? 20.186  14.526  35.340  1.00 11.21 ? 415  MET B O   1 
ATOM   7870  C  CB  A MET B 1 423 ? 17.454  13.530  33.825  0.59 9.01  ? 415  MET B CB  1 
ATOM   7871  C  CB  B MET B 1 423 ? 17.441  13.658  33.807  0.41 10.09 ? 415  MET B CB  1 
ATOM   7872  C  CG  A MET B 1 423 ? 16.266  14.067  33.033  0.59 8.03  ? 415  MET B CG  1 
ATOM   7873  C  CG  B MET B 1 423 ? 16.333  14.443  33.135  0.41 10.64 ? 415  MET B CG  1 
ATOM   7874  S  SD  A MET B 1 423 ? 14.802  13.028  33.264  0.59 12.93 ? 415  MET B SD  1 
ATOM   7875  S  SD  B MET B 1 423 ? 14.757  14.214  33.957  0.41 13.06 ? 415  MET B SD  1 
ATOM   7876  C  CE  A MET B 1 423 ? 14.646  13.068  35.051  0.59 10.42 ? 415  MET B CE  1 
ATOM   7877  C  CE  B MET B 1 423 ? 14.519  12.453  33.732  0.41 9.77  ? 415  MET B CE  1 
ATOM   7878  N  N   . ASN B 1 424 ? 20.410  12.525  34.340  1.00 8.60  ? 416  ASN B N   1 
ATOM   7879  C  CA  . ASN B 1 424 ? 21.475  12.145  35.262  1.00 12.28 ? 416  ASN B CA  1 
ATOM   7880  C  C   . ASN B 1 424 ? 22.636  13.134  35.195  1.00 12.92 ? 416  ASN B C   1 
ATOM   7881  O  O   . ASN B 1 424 ? 23.177  13.533  36.233  1.00 11.46 ? 416  ASN B O   1 
ATOM   7882  C  CB  . ASN B 1 424 ? 21.953  10.715  34.980  1.00 10.82 ? 416  ASN B CB  1 
ATOM   7883  C  CG  . ASN B 1 424 ? 20.911  9.661   35.390  1.00 14.25 ? 416  ASN B CG  1 
ATOM   7884  O  OD1 . ASN B 1 424 ? 19.942  9.972   36.082  1.00 12.96 ? 416  ASN B OD1 1 
ATOM   7885  N  ND2 . ASN B 1 424 ? 21.121  8.424   34.983  1.00 11.24 ? 416  ASN B ND2 1 
ATOM   7886  N  N   . GLY B 1 425 ? 23.020  13.557  33.986  1.00 9.28  ? 417  GLY B N   1 
ATOM   7887  C  CA  . GLY B 1 425 ? 24.086  14.546  33.851  1.00 9.01  ? 417  GLY B CA  1 
ATOM   7888  C  C   . GLY B 1 425 ? 23.684  15.941  34.296  1.00 12.13 ? 417  GLY B C   1 
ATOM   7889  O  O   . GLY B 1 425 ? 24.507  16.683  34.843  1.00 10.96 ? 417  GLY B O   1 
ATOM   7890  N  N   . LEU B 1 426 ? 22.425  16.323  34.068  1.00 8.98  ? 418  LEU B N   1 
ATOM   7891  C  CA  . LEU B 1 426 ? 21.936  17.597  34.592  1.00 14.45 ? 418  LEU B CA  1 
ATOM   7892  C  C   . LEU B 1 426 ? 22.107  17.676  36.109  1.00 11.04 ? 418  LEU B C   1 
ATOM   7893  O  O   . LEU B 1 426 ? 22.601  18.683  36.631  1.00 13.39 ? 418  LEU B O   1 
ATOM   7894  C  CB  . LEU B 1 426 ? 20.474  17.808  34.196  1.00 9.05  ? 418  LEU B CB  1 
ATOM   7895  C  CG  . LEU B 1 426 ? 20.171  18.192  32.733  1.00 10.52 ? 418  LEU B CG  1 
ATOM   7896  C  CD1 . LEU B 1 426 ? 18.698  17.930  32.445  1.00 15.10 ? 418  LEU B CD1 1 
ATOM   7897  C  CD2 . LEU B 1 426 ? 20.544  19.636  32.386  1.00 12.10 ? 418  LEU B CD2 1 
ATOM   7898  N  N   . VAL B 1 427 ? 21.707  16.622  36.833  1.00 11.91 ? 419  VAL B N   1 
ATOM   7899  C  CA  A VAL B 1 427 ? 21.822  16.573  38.299  0.39 15.08 ? 419  VAL B CA  1 
ATOM   7900  C  CA  B VAL B 1 427 ? 21.819  16.702  38.281  0.61 13.95 ? 419  VAL B CA  1 
ATOM   7901  C  C   . VAL B 1 427 ? 23.277  16.592  38.727  1.00 15.96 ? 419  VAL B C   1 
ATOM   7902  O  O   . VAL B 1 427 ? 23.671  17.264  39.684  1.00 12.96 ? 419  VAL B O   1 
ATOM   7903  C  CB  A VAL B 1 427 ? 21.161  15.298  38.856  0.39 17.99 ? 419  VAL B CB  1 
ATOM   7904  C  CB  B VAL B 1 427 ? 20.916  15.655  38.961  0.61 19.05 ? 419  VAL B CB  1 
ATOM   7905  C  CG1 A VAL B 1 427 ? 21.360  15.218  40.372  0.39 20.99 ? 419  VAL B CG1 1 
ATOM   7906  C  CG1 B VAL B 1 427 ? 21.205  14.266  38.452  0.61 15.44 ? 419  VAL B CG1 1 
ATOM   7907  C  CG2 A VAL B 1 427 ? 19.728  15.211  38.510  0.39 15.39 ? 419  VAL B CG2 1 
ATOM   7908  C  CG2 B VAL B 1 427 ? 21.098  15.718  40.472  0.61 23.48 ? 419  VAL B CG2 1 
ATOM   7909  N  N   . LEU B 1 428 ? 24.094  15.767  38.057  1.00 11.44 ? 420  LEU B N   1 
ATOM   7910  C  CA  . LEU B 1 428 ? 25.490  15.621  38.461  1.00 14.45 ? 420  LEU B CA  1 
ATOM   7911  C  C   . LEU B 1 428 ? 26.235  16.949  38.383  1.00 16.98 ? 420  LEU B C   1 
ATOM   7912  O  O   . LEU B 1 428 ? 27.102  17.225  39.218  1.00 16.75 ? 420  LEU B O   1 
ATOM   7913  C  CB  . LEU B 1 428 ? 26.175  14.556  37.587  1.00 13.77 ? 420  LEU B CB  1 
ATOM   7914  C  CG  . LEU B 1 428 ? 25.849  13.088  37.914  1.00 16.00 ? 420  LEU B CG  1 
ATOM   7915  C  CD1 . LEU B 1 428 ? 26.150  12.177  36.723  1.00 13.52 ? 420  LEU B CD1 1 
ATOM   7916  C  CD2 . LEU B 1 428 ? 26.612  12.607  39.171  1.00 10.87 ? 420  LEU B CD2 1 
ATOM   7917  N  N   . HIS B 1 429 ? 25.882  17.796  37.410  1.00 13.84 ? 421  HIS B N   1 
ATOM   7918  C  CA  . HIS B 1 429 ? 26.581  19.062  37.215  1.00 11.20 ? 421  HIS B CA  1 
ATOM   7919  C  C   . HIS B 1 429 ? 26.521  19.939  38.459  1.00 15.89 ? 421  HIS B C   1 
ATOM   7920  O  O   . HIS B 1 429 ? 27.508  20.594  38.806  1.00 14.38 ? 421  HIS B O   1 
ATOM   7921  C  CB  . HIS B 1 429 ? 25.987  19.821  36.020  1.00 11.08 ? 421  HIS B CB  1 
ATOM   7922  C  CG  . HIS B 1 429 ? 26.734  21.073  35.678  1.00 11.76 ? 421  HIS B CG  1 
ATOM   7923  N  ND1 . HIS B 1 429 ? 26.460  22.291  36.265  1.00 14.82 ? 421  HIS B ND1 1 
ATOM   7924  C  CD2 . HIS B 1 429 ? 27.764  21.290  34.825  1.00 12.20 ? 421  HIS B CD2 1 
ATOM   7925  C  CE1 . HIS B 1 429 ? 27.281  23.206  35.782  1.00 16.40 ? 421  HIS B CE1 1 
ATOM   7926  N  NE2 . HIS B 1 429 ? 28.083  22.625  34.905  1.00 16.75 ? 421  HIS B NE2 1 
ATOM   7927  N  N   . GLY B 1 430 ? 25.378  19.970  39.129  1.00 14.09 ? 422  GLY B N   1 
ATOM   7928  C  CA  . GLY B 1 430 ? 25.031  20.949  40.155  1.00 13.50 ? 422  GLY B CA  1 
ATOM   7929  C  C   . GLY B 1 430 ? 24.308  22.151  39.575  1.00 14.50 ? 422  GLY B C   1 
ATOM   7930  O  O   . GLY B 1 430 ? 24.454  22.501  38.404  1.00 15.49 ? 422  GLY B O   1 
ATOM   7931  N  N   . GLY B 1 431 ? 23.479  22.786  40.412  1.00 12.66 ? 423  GLY B N   1 
ATOM   7932  C  CA  . GLY B 1 431 ? 22.834  24.031  40.066  1.00 13.00 ? 423  GLY B CA  1 
ATOM   7933  C  C   . GLY B 1 431 ? 21.415  23.898  39.543  1.00 10.72 ? 423  GLY B C   1 
ATOM   7934  O  O   . GLY B 1 431 ? 20.676  24.887  39.538  1.00 13.19 ? 423  GLY B O   1 
ATOM   7935  N  N   . VAL B 1 432 ? 21.008  22.703  39.124  1.00 17.11 ? 424  VAL B N   1 
ATOM   7936  C  CA  . VAL B 1 432 ? 19.655  22.489  38.631  1.00 12.73 ? 424  VAL B CA  1 
ATOM   7937  C  C   . VAL B 1 432 ? 19.097  21.212  39.236  1.00 14.78 ? 424  VAL B C   1 
ATOM   7938  O  O   . VAL B 1 432 ? 19.837  20.288  39.587  1.00 13.26 ? 424  VAL B O   1 
ATOM   7939  C  CB  . VAL B 1 432 ? 19.586  22.430  37.084  1.00 14.90 ? 424  VAL B CB  1 
ATOM   7940  C  CG1 . VAL B 1 432 ? 19.946  23.785  36.478  1.00 16.93 ? 424  VAL B CG1 1 
ATOM   7941  C  CG2 . VAL B 1 432 ? 20.494  21.358  36.550  1.00 21.32 ? 424  VAL B CG2 1 
ATOM   7942  N  N   . LYS B 1 433 ? 17.774  21.180  39.382  1.00 12.16 ? 425  LYS B N   1 
ATOM   7943  C  CA  A LYS B 1 433 ? 17.055  19.994  39.849  0.44 11.56 ? 425  LYS B CA  1 
ATOM   7944  C  CA  B LYS B 1 433 ? 17.058  19.993  39.849  0.56 11.42 ? 425  LYS B CA  1 
ATOM   7945  C  C   . LYS B 1 433 ? 16.084  19.569  38.759  1.00 10.92 ? 425  LYS B C   1 
ATOM   7946  O  O   . LYS B 1 433 ? 15.006  20.174  38.615  1.00 11.36 ? 425  LYS B O   1 
ATOM   7947  C  CB  A LYS B 1 433 ? 16.309  20.277  41.154  0.44 13.63 ? 425  LYS B CB  1 
ATOM   7948  C  CB  B LYS B 1 433 ? 16.317  20.270  41.160  0.56 13.85 ? 425  LYS B CB  1 
ATOM   7949  C  CG  A LYS B 1 433 ? 17.215  20.545  42.342  0.44 9.93  ? 425  LYS B CG  1 
ATOM   7950  C  CG  B LYS B 1 433 ? 15.544  19.068  41.699  0.56 12.81 ? 425  LYS B CG  1 
ATOM   7951  C  CD  A LYS B 1 433 ? 16.428  20.664  43.647  0.44 10.70 ? 425  LYS B CD  1 
ATOM   7952  C  CD  B LYS B 1 433 ? 14.864  19.352  43.037  0.56 11.72 ? 425  LYS B CD  1 
ATOM   7953  C  CE  A LYS B 1 433 ? 15.696  19.373  43.997  0.44 12.36 ? 425  LYS B CE  1 
ATOM   7954  C  CE  B LYS B 1 433 ? 15.855  19.409  44.197  0.56 12.66 ? 425  LYS B CE  1 
ATOM   7955  N  NZ  A LYS B 1 433 ? 16.627  18.206  44.107  0.44 12.76 ? 425  LYS B NZ  1 
ATOM   7956  N  NZ  B LYS B 1 433 ? 16.604  18.120  44.370  0.56 12.35 ? 425  LYS B NZ  1 
ATOM   7957  N  N   . PRO B 1 434 ? 16.410  18.549  37.967  1.00 11.69 ? 426  PRO B N   1 
ATOM   7958  C  CA  . PRO B 1 434 ? 15.557  18.199  36.832  1.00 13.10 ? 426  PRO B CA  1 
ATOM   7959  C  C   . PRO B 1 434 ? 14.519  17.137  37.141  1.00 11.28 ? 426  PRO B C   1 
ATOM   7960  O  O   . PRO B 1 434 ? 14.713  16.243  37.969  1.00 10.47 ? 426  PRO B O   1 
ATOM   7961  C  CB  . PRO B 1 434 ? 16.565  17.656  35.811  1.00 15.19 ? 426  PRO B CB  1 
ATOM   7962  C  CG  . PRO B 1 434 ? 17.553  16.937  36.676  1.00 14.76 ? 426  PRO B CG  1 
ATOM   7963  C  CD  . PRO B 1 434 ? 17.659  17.775  37.960  1.00 14.57 ? 426  PRO B CD  1 
ATOM   7964  N  N   . PHE B 1 435 ? 13.407  17.249  36.420  1.00 9.72  ? 427  PHE B N   1 
ATOM   7965  C  CA  . PHE B 1 435 ? 12.472  16.148  36.260  1.00 11.80 ? 427  PHE B CA  1 
ATOM   7966  C  C   . PHE B 1 435 ? 12.196  15.940  34.778  1.00 13.71 ? 427  PHE B C   1 
ATOM   7967  O  O   . PHE B 1 435 ? 12.362  16.848  33.957  1.00 11.45 ? 427  PHE B O   1 
ATOM   7968  C  CB  . PHE B 1 435 ? 11.165  16.362  37.023  1.00 12.34 ? 427  PHE B CB  1 
ATOM   7969  C  CG  . PHE B 1 435 ? 10.231  17.414  36.441  1.00 15.35 ? 427  PHE B CG  1 
ATOM   7970  C  CD1 . PHE B 1 435 ? 9.337   17.091  35.420  1.00 15.18 ? 427  PHE B CD1 1 
ATOM   7971  C  CD2 . PHE B 1 435 ? 10.174  18.686  36.988  1.00 11.06 ? 427  PHE B CD2 1 
ATOM   7972  C  CE1 . PHE B 1 435 ? 8.451   18.044  34.921  1.00 16.71 ? 427  PHE B CE1 1 
ATOM   7973  C  CE2 . PHE B 1 435 ? 9.296   19.639  36.499  1.00 18.80 ? 427  PHE B CE2 1 
ATOM   7974  C  CZ  . PHE B 1 435 ? 8.430   19.324  35.465  1.00 16.72 ? 427  PHE B CZ  1 
ATOM   7975  N  N   . GLY B 1 436 ? 11.799  14.716  34.436  1.00 10.61 ? 428  GLY B N   1 
ATOM   7976  C  CA  . GLY B 1 436 ? 11.457  14.425  33.053  1.00 10.76 ? 428  GLY B CA  1 
ATOM   7977  C  C   . GLY B 1 436 ? 10.361  13.386  32.957  1.00 9.42  ? 428  GLY B C   1 
ATOM   7978  O  O   . GLY B 1 436 ? 10.404  12.374  33.662  1.00 13.41 ? 428  GLY B O   1 
ATOM   7979  N  N   . ALA B 1 437 ? 9.390   13.603  32.073  1.00 9.75  ? 429  ALA B N   1 
ATOM   7980  C  CA  . ALA B 1 437 ? 8.167   12.817  32.074  1.00 10.36 ? 429  ALA B CA  1 
ATOM   7981  C  C   . ALA B 1 437 ? 8.007   12.019  30.788  1.00 10.96 ? 429  ALA B C   1 
ATOM   7982  O  O   . ALA B 1 437 ? 8.324   12.507  29.695  1.00 11.55 ? 429  ALA B O   1 
ATOM   7983  C  CB  . ALA B 1 437 ? 6.943   13.720  32.258  1.00 12.17 ? 429  ALA B CB  1 
ATOM   7984  N  N   . THR B 1 438 ? 7.477   10.803  30.931  1.00 9.71  ? 430  THR B N   1 
ATOM   7985  C  CA  . THR B 1 438 ? 6.990   10.017  29.800  1.00 9.83  ? 430  THR B CA  1 
ATOM   7986  C  C   . THR B 1 438 ? 5.838   9.146   30.301  1.00 12.96 ? 430  THR B C   1 
ATOM   7987  O  O   . THR B 1 438 ? 5.423   9.251   31.459  1.00 11.98 ? 430  THR B O   1 
ATOM   7988  C  CB  . THR B 1 438 ? 8.146   9.225   29.151  1.00 10.65 ? 430  THR B CB  1 
ATOM   7989  O  OG1 . THR B 1 438 ? 7.667   8.480   28.026  1.00 12.09 ? 430  THR B OG1 1 
ATOM   7990  C  CG2 . THR B 1 438 ? 8.803   8.297   30.140  1.00 9.19  ? 430  THR B CG2 1 
ATOM   7991  N  N   . PHE B 1 439 ? 5.266   8.335   29.408  1.00 12.77 ? 431  PHE B N   1 
ATOM   7992  C  CA  . PHE B 1 439 ? 4.304   7.323   29.841  1.00 12.96 ? 431  PHE B CA  1 
ATOM   7993  C  C   . PHE B 1 439 ? 5.003   6.273   30.706  1.00 9.58  ? 431  PHE B C   1 
ATOM   7994  O  O   . PHE B 1 439 ? 6.156   5.920   30.469  1.00 9.34  ? 431  PHE B O   1 
ATOM   7995  C  CB  . PHE B 1 439 ? 3.651   6.610   28.641  1.00 12.23 ? 431  PHE B CB  1 
ATOM   7996  C  CG  . PHE B 1 439 ? 2.647   7.443   27.861  1.00 16.88 ? 431  PHE B CG  1 
ATOM   7997  C  CD1 . PHE B 1 439 ? 2.500   8.802   28.078  1.00 16.57 ? 431  PHE B CD1 1 
ATOM   7998  C  CD2 . PHE B 1 439 ? 1.839   6.835   26.912  1.00 26.13 ? 431  PHE B CD2 1 
ATOM   7999  C  CE1 . PHE B 1 439 ? 1.583   9.543   27.348  1.00 22.88 ? 431  PHE B CE1 1 
ATOM   8000  C  CE2 . PHE B 1 439 ? 0.914   7.572   26.175  1.00 28.23 ? 431  PHE B CE2 1 
ATOM   8001  C  CZ  . PHE B 1 439 ? 0.792   8.924   26.393  1.00 26.44 ? 431  PHE B CZ  1 
ATOM   8002  N  N   . LEU B 1 440 ? 4.280   5.744   31.703  1.00 10.66 ? 432  LEU B N   1 
ATOM   8003  C  CA  . LEU B 1 440 ? 4.878   4.722   32.569  1.00 11.19 ? 432  LEU B CA  1 
ATOM   8004  C  C   . LEU B 1 440 ? 5.406   3.533   31.767  1.00 9.61  ? 432  LEU B C   1 
ATOM   8005  O  O   . LEU B 1 440 ? 6.459   2.970   32.095  1.00 8.99  ? 432  LEU B O   1 
ATOM   8006  C  CB  . LEU B 1 440 ? 3.864   4.249   33.623  1.00 11.63 ? 432  LEU B CB  1 
ATOM   8007  C  CG  . LEU B 1 440 ? 4.358   3.139   34.566  1.00 10.10 ? 432  LEU B CG  1 
ATOM   8008  C  CD1 . LEU B 1 440 ? 5.656   3.530   35.299  1.00 11.88 ? 432  LEU B CD1 1 
ATOM   8009  C  CD2 . LEU B 1 440 ? 3.252   2.719   35.565  1.00 9.68  ? 432  LEU B CD2 1 
ATOM   8010  N  N   . MET B 1 441 ? 4.705   3.135   30.703  1.00 10.08 ? 433  MET B N   1 
ATOM   8011  C  CA  . MET B 1 441 ? 5.201   2.007   29.919  1.00 9.67  ? 433  MET B CA  1 
ATOM   8012  C  C   . MET B 1 441 ? 6.626   2.261   29.435  1.00 13.98 ? 433  MET B C   1 
ATOM   8013  O  O   . MET B 1 441 ? 7.461   1.348   29.414  1.00 10.75 ? 433  MET B O   1 
ATOM   8014  C  CB  . MET B 1 441 ? 4.291   1.743   28.721  1.00 9.85  ? 433  MET B CB  1 
ATOM   8015  C  CG  . MET B 1 441 ? 4.800   0.587   27.856  1.00 10.21 ? 433  MET B CG  1 
ATOM   8016  S  SD  . MET B 1 441 ? 4.798   -0.970  28.776  1.00 11.61 ? 433  MET B SD  1 
ATOM   8017  C  CE  . MET B 1 441 ? 3.041   -1.248  29.006  1.00 10.81 ? 433  MET B CE  1 
ATOM   8018  N  N   . PHE B 1 442 ? 6.927   3.495   29.059  1.00 9.22  ? 434  PHE B N   1 
ATOM   8019  C  CA  . PHE B 1 442 ? 8.212   3.794   28.445  1.00 13.74 ? 434  PHE B CA  1 
ATOM   8020  C  C   . PHE B 1 442 ? 9.293   4.091   29.467  1.00 8.89  ? 434  PHE B C   1 
ATOM   8021  O  O   . PHE B 1 442 ? 10.419  4.424   29.080  1.00 10.29 ? 434  PHE B O   1 
ATOM   8022  C  CB  . PHE B 1 442 ? 8.027   4.913   27.434  1.00 14.90 ? 434  PHE B CB  1 
ATOM   8023  C  CG  . PHE B 1 442 ? 6.940   4.589   26.463  1.00 22.03 ? 434  PHE B CG  1 
ATOM   8024  C  CD1 . PHE B 1 442 ? 6.829   3.295   25.972  1.00 22.14 ? 434  PHE B CD1 1 
ATOM   8025  C  CD2 . PHE B 1 442 ? 5.984   5.516   26.118  1.00 20.09 ? 434  PHE B CD2 1 
ATOM   8026  C  CE1 . PHE B 1 442 ? 5.810   2.949   25.107  1.00 28.03 ? 434  PHE B CE1 1 
ATOM   8027  C  CE2 . PHE B 1 442 ? 4.964   5.174   25.249  1.00 26.17 ? 434  PHE B CE2 1 
ATOM   8028  C  CZ  . PHE B 1 442 ? 4.877   3.891   24.753  1.00 22.76 ? 434  PHE B CZ  1 
ATOM   8029  N  N   . SER B 1 443 ? 8.994   3.905   30.758  1.00 10.51 ? 435  SER B N   1 
ATOM   8030  C  CA  . SER B 1 443 ? 10.057  3.628   31.714  1.00 12.99 ? 435  SER B CA  1 
ATOM   8031  C  C   . SER B 1 443 ? 10.945  2.495   31.215  1.00 11.74 ? 435  SER B C   1 
ATOM   8032  O  O   . SER B 1 443 ? 12.139  2.462   31.530  1.00 10.33 ? 435  SER B O   1 
ATOM   8033  C  CB  . SER B 1 443 ? 9.476   3.272   33.088  1.00 9.50  ? 435  SER B CB  1 
ATOM   8034  O  OG  . SER B 1 443 ? 8.754   2.044   33.041  1.00 11.14 ? 435  SER B OG  1 
ATOM   8035  N  N   . GLU B 1 444 ? 10.393  1.571   30.412  1.00 12.64 ? 436  GLU B N   1 
ATOM   8036  C  CA  . GLU B 1 444 ? 11.199  0.454   29.914  1.00 9.61  ? 436  GLU B CA  1 
ATOM   8037  C  C   . GLU B 1 444 ? 12.198  0.895   28.854  1.00 14.05 ? 436  GLU B C   1 
ATOM   8038  O  O   . GLU B 1 444 ? 13.249  0.255   28.703  1.00 18.80 ? 436  GLU B O   1 
ATOM   8039  C  CB  . GLU B 1 444 ? 10.293  -0.659  29.372  1.00 11.53 ? 436  GLU B CB  1 
ATOM   8040  C  CG  . GLU B 1 444 ? 9.432   -1.231  30.499  1.00 10.07 ? 436  GLU B CG  1 
ATOM   8041  C  CD  . GLU B 1 444 ? 8.747   -2.523  30.162  1.00 16.10 ? 436  GLU B CD  1 
ATOM   8042  O  OE1 . GLU B 1 444 ? 8.636   -2.869  28.964  1.00 14.59 ? 436  GLU B OE1 1 
ATOM   8043  O  OE2 . GLU B 1 444 ? 8.312   -3.196  31.117  1.00 15.57 ? 436  GLU B OE2 1 
ATOM   8044  N  N   . TYR B 1 445 ? 11.900  1.968   28.120  1.00 8.96  ? 437  TYR B N   1 
ATOM   8045  C  CA  . TYR B 1 445 ? 12.865  2.523   27.168  1.00 10.81 ? 437  TYR B CA  1 
ATOM   8046  C  C   . TYR B 1 445 ? 14.045  3.215   27.859  1.00 14.64 ? 437  TYR B C   1 
ATOM   8047  O  O   . TYR B 1 445 ? 15.114  3.347   27.253  1.00 16.28 ? 437  TYR B O   1 
ATOM   8048  C  CB  . TYR B 1 445 ? 12.174  3.522   26.230  1.00 10.44 ? 437  TYR B CB  1 
ATOM   8049  C  CG  . TYR B 1 445 ? 11.452  2.928   25.025  1.00 9.68  ? 437  TYR B CG  1 
ATOM   8050  C  CD1 . TYR B 1 445 ? 10.619  1.825   25.146  1.00 9.67  ? 437  TYR B CD1 1 
ATOM   8051  C  CD2 . TYR B 1 445 ? 11.609  3.493   23.766  1.00 10.60 ? 437  TYR B CD2 1 
ATOM   8052  C  CE1 . TYR B 1 445 ? 9.931   1.300   24.028  1.00 13.46 ? 437  TYR B CE1 1 
ATOM   8053  C  CE2 . TYR B 1 445 ? 10.946  2.980   22.649  1.00 11.50 ? 437  TYR B CE2 1 
ATOM   8054  C  CZ  . TYR B 1 445 ? 10.116  1.890   22.779  1.00 11.42 ? 437  TYR B CZ  1 
ATOM   8055  O  OH  . TYR B 1 445 ? 9.478   1.398   21.651  1.00 12.46 ? 437  TYR B OH  1 
ATOM   8056  N  N   . GLU B 1 446 ? 13.877  3.686   29.096  1.00 11.63 ? 438  GLU B N   1 
ATOM   8057  C  CA  . GLU B 1 446 ? 14.945  4.399   29.794  1.00 8.76  ? 438  GLU B CA  1 
ATOM   8058  C  C   . GLU B 1 446 ? 15.366  3.668   31.064  1.00 8.43  ? 438  GLU B C   1 
ATOM   8059  O  O   . GLU B 1 446 ? 15.977  4.276   31.942  1.00 11.94 ? 438  GLU B O   1 
ATOM   8060  C  CB  . GLU B 1 446 ? 14.512  5.829   30.143  1.00 10.32 ? 438  GLU B CB  1 
ATOM   8061  C  CG  . GLU B 1 446 ? 13.231  5.879   30.968  1.00 10.55 ? 438  GLU B CG  1 
ATOM   8062  C  CD  . GLU B 1 446 ? 12.924  7.267   31.538  1.00 15.26 ? 438  GLU B CD  1 
ATOM   8063  O  OE1 . GLU B 1 446 ? 13.819  8.138   31.590  1.00 11.67 ? 438  GLU B OE1 1 
ATOM   8064  O  OE2 . GLU B 1 446 ? 11.770  7.484   31.942  1.00 12.80 ? 438  GLU B OE2 1 
ATOM   8065  N  N   . ARG B 1 447 ? 15.073  2.366   31.150  1.00 9.26  ? 439  ARG B N   1 
ATOM   8066  C  CA  . ARG B 1 447 ? 15.126  1.655   32.428  1.00 11.29 ? 439  ARG B CA  1 
ATOM   8067  C  C   . ARG B 1 447 ? 16.517  1.719   33.065  1.00 12.34 ? 439  ARG B C   1 
ATOM   8068  O  O   . ARG B 1 447 ? 16.645  2.020   34.255  1.00 10.24 ? 439  ARG B O   1 
ATOM   8069  C  CB  . ARG B 1 447 ? 14.674  0.202   32.231  1.00 10.70 ? 439  ARG B CB  1 
ATOM   8070  C  CG  . ARG B 1 447 ? 14.782  -0.680  33.485  1.00 8.70  ? 439  ARG B CG  1 
ATOM   8071  C  CD  . ARG B 1 447 ? 14.005  -0.098  34.681  1.00 8.60  ? 439  ARG B CD  1 
ATOM   8072  N  NE  . ARG B 1 447 ? 14.125  -0.998  35.833  1.00 13.67 ? 439  ARG B NE  1 
ATOM   8073  C  CZ  . ARG B 1 447 ? 13.101  -1.582  36.451  1.00 12.49 ? 439  ARG B CZ  1 
ATOM   8074  N  NH1 . ARG B 1 447 ? 11.847  -1.335  36.069  1.00 13.10 ? 439  ARG B NH1 1 
ATOM   8075  N  NH2 . ARG B 1 447 ? 13.329  -2.405  37.469  1.00 10.92 ? 439  ARG B NH2 1 
ATOM   8076  N  N   . ASN B 1 448 ? 17.577  1.457   32.297  1.00 8.61  ? 440  ASN B N   1 
ATOM   8077  C  CA  . ASN B 1 448 ? 18.884  1.428   32.968  1.00 10.29 ? 440  ASN B CA  1 
ATOM   8078  C  C   . ASN B 1 448 ? 19.360  2.817   33.394  1.00 12.82 ? 440  ASN B C   1 
ATOM   8079  O  O   . ASN B 1 448 ? 20.207  2.917   34.290  1.00 9.12  ? 440  ASN B O   1 
ATOM   8080  C  CB  . ASN B 1 448 ? 19.938  0.748   32.091  1.00 8.98  ? 440  ASN B CB  1 
ATOM   8081  C  CG  . ASN B 1 448 ? 21.165  0.318   32.891  1.00 9.17  ? 440  ASN B CG  1 
ATOM   8082  O  OD1 . ASN B 1 448 ? 22.251  0.868   32.723  1.00 11.20 ? 440  ASN B OD1 1 
ATOM   8083  N  ND2 . ASN B 1 448 ? 20.974  -0.640  33.802  1.00 11.30 ? 440  ASN B ND2 1 
ATOM   8084  N  N   . ALA B 1 449 ? 18.840  3.891   32.794  1.00 9.62  ? 441  ALA B N   1 
ATOM   8085  C  CA  . ALA B 1 449 ? 19.175  5.226   33.291  1.00 8.60  ? 441  ALA B CA  1 
ATOM   8086  C  C   . ALA B 1 449 ? 18.568  5.470   34.671  1.00 8.51  ? 441  ALA B C   1 
ATOM   8087  O  O   . ALA B 1 449 ? 19.178  6.139   35.514  1.00 8.14  ? 441  ALA B O   1 
ATOM   8088  C  CB  . ALA B 1 449 ? 18.703  6.305   32.311  1.00 10.49 ? 441  ALA B CB  1 
ATOM   8089  N  N   . LEU B 1 450 ? 17.352  4.966   34.900  1.00 9.01  ? 442  LEU B N   1 
ATOM   8090  C  CA  . LEU B 1 450 ? 16.766  4.983   36.237  1.00 8.15  ? 442  LEU B CA  1 
ATOM   8091  C  C   . LEU B 1 450 ? 17.657  4.243   37.210  1.00 10.93 ? 442  LEU B C   1 
ATOM   8092  O  O   . LEU B 1 450 ? 17.942  4.725   38.320  1.00 11.42 ? 442  LEU B O   1 
ATOM   8093  C  CB  . LEU B 1 450 ? 15.382  4.321   36.213  1.00 8.54  ? 442  LEU B CB  1 
ATOM   8094  C  CG  . LEU B 1 450 ? 14.138  5.102   35.766  1.00 19.17 ? 442  LEU B CG  1 
ATOM   8095  C  CD1 . LEU B 1 450 ? 14.365  5.984   34.583  1.00 15.97 ? 442  LEU B CD1 1 
ATOM   8096  C  CD2 . LEU B 1 450 ? 13.032  4.112   35.451  1.00 16.63 ? 442  LEU B CD2 1 
ATOM   8097  N  N   . ARG B 1 451 ? 18.098  3.052   36.809  1.00 10.45 ? 443  ARG B N   1 
ATOM   8098  C  CA  . ARG B 1 451 ? 18.938  2.263   37.691  1.00 8.62  ? 443  ARG B CA  1 
ATOM   8099  C  C   . ARG B 1 451 ? 20.255  2.979   37.954  1.00 10.31 ? 443  ARG B C   1 
ATOM   8100  O  O   . ARG B 1 451 ? 20.765  2.972   39.087  1.00 8.80  ? 443  ARG B O   1 
ATOM   8101  C  CB  . ARG B 1 451 ? 19.175  0.880   37.088  1.00 11.01 ? 443  ARG B CB  1 
ATOM   8102  C  CG  . ARG B 1 451 ? 19.779  -0.099  38.106  1.00 13.15 ? 443  ARG B CG  1 
ATOM   8103  C  CD  . ARG B 1 451 ? 20.111  -1.446  37.491  1.00 16.62 ? 443  ARG B CD  1 
ATOM   8104  N  NE  . ARG B 1 451 ? 20.312  -2.432  38.547  1.00 11.91 ? 443  ARG B NE  1 
ATOM   8105  C  CZ  . ARG B 1 451 ? 21.491  -2.766  39.055  1.00 12.97 ? 443  ARG B CZ  1 
ATOM   8106  N  NH1 . ARG B 1 451 ? 22.606  -2.199  38.600  1.00 10.20 ? 443  ARG B NH1 1 
ATOM   8107  N  NH2 . ARG B 1 451 ? 21.551  -3.673  40.018  1.00 10.68 ? 443  ARG B NH2 1 
ATOM   8108  N  N   . MET B 1 452 ? 20.817  3.611   36.924  1.00 8.54  ? 444  MET B N   1 
ATOM   8109  C  CA  . MET B 1 452 ? 22.104  4.290   37.106  1.00 11.69 ? 444  MET B CA  1 
ATOM   8110  C  C   . MET B 1 452 ? 21.968  5.487   38.037  1.00 14.61 ? 444  MET B C   1 
ATOM   8111  O  O   . MET B 1 452 ? 22.894  5.773   38.816  1.00 11.43 ? 444  MET B O   1 
ATOM   8112  C  CB  . MET B 1 452 ? 22.685  4.709   35.751  1.00 10.27 ? 444  MET B CB  1 
ATOM   8113  C  CG  . MET B 1 452 ? 23.175  3.511   34.924  1.00 9.67  ? 444  MET B CG  1 
ATOM   8114  S  SD  . MET B 1 452 ? 24.509  2.570   35.743  1.00 11.53 ? 444  MET B SD  1 
ATOM   8115  C  CE  . MET B 1 452 ? 25.862  3.769   35.646  1.00 11.79 ? 444  MET B CE  1 
ATOM   8116  N  N   . ALA B 1 453 ? 20.818  6.173   38.006  1.00 8.30  ? 445  ALA B N   1 
ATOM   8117  C  CA  . ALA B 1 453 ? 20.611  7.266   38.950  1.00 8.63  ? 445  ALA B CA  1 
ATOM   8118  C  C   . ALA B 1 453 ? 20.598  6.744   40.379  1.00 9.75  ? 445  ALA B C   1 
ATOM   8119  O  O   . ALA B 1 453 ? 21.192  7.352   41.276  1.00 10.90 ? 445  ALA B O   1 
ATOM   8120  C  CB  . ALA B 1 453 ? 19.310  8.013   38.631  1.00 9.97  ? 445  ALA B CB  1 
ATOM   8121  N  N   . ALA B 1 454 ? 19.933  5.609   40.603  1.00 11.26 ? 446  ALA B N   1 
ATOM   8122  C  CA  . ALA B 1 454 ? 19.895  5.010   41.936  1.00 11.03 ? 446  ALA B CA  1 
ATOM   8123  C  C   . ALA B 1 454 ? 21.286  4.579   42.386  1.00 9.18  ? 446  ALA B C   1 
ATOM   8124  O  O   . ALA B 1 454 ? 21.682  4.811   43.536  1.00 12.18 ? 446  ALA B O   1 
ATOM   8125  C  CB  . ALA B 1 454 ? 18.932  3.817   41.929  1.00 9.25  ? 446  ALA B CB  1 
ATOM   8126  N  N   . LEU B 1 455 ? 22.039  3.957   41.486  1.00 9.11  ? 447  LEU B N   1 
ATOM   8127  C  CA  . LEU B 1 455 ? 23.386  3.502   41.811  1.00 9.41  ? 447  LEU B CA  1 
ATOM   8128  C  C   . LEU B 1 455 ? 24.312  4.678   42.110  1.00 14.22 ? 447  LEU B C   1 
ATOM   8129  O  O   . LEU B 1 455 ? 25.162  4.601   43.010  1.00 11.84 ? 447  LEU B O   1 
ATOM   8130  C  CB  . LEU B 1 455 ? 23.919  2.659   40.651  1.00 9.46  ? 447  LEU B CB  1 
ATOM   8131  C  CG  . LEU B 1 455 ? 25.353  2.124   40.779  1.00 9.85  ? 447  LEU B CG  1 
ATOM   8132  C  CD1 . LEU B 1 455 ? 25.535  1.282   42.043  1.00 14.48 ? 447  LEU B CD1 1 
ATOM   8133  C  CD2 . LEU B 1 455 ? 25.708  1.298   39.542  1.00 16.18 ? 447  LEU B CD2 1 
ATOM   8134  N  N   . MET B 1 456 ? 24.178  5.772   41.352  1.00 9.04  ? 448  MET B N   1 
ATOM   8135  C  CA  . MET B 1 456 ? 25.002  6.958   41.589  1.00 10.37 ? 448  MET B CA  1 
ATOM   8136  C  C   . MET B 1 456 ? 24.605  7.729   42.843  1.00 11.85 ? 448  MET B C   1 
ATOM   8137  O  O   . MET B 1 456 ? 25.353  8.624   43.260  1.00 11.28 ? 448  MET B O   1 
ATOM   8138  C  CB  . MET B 1 456 ? 24.933  7.891   40.379  1.00 10.84 ? 448  MET B CB  1 
ATOM   8139  C  CG  . MET B 1 456 ? 25.701  7.338   39.172  1.00 8.79  ? 448  MET B CG  1 
ATOM   8140  S  SD  . MET B 1 456 ? 25.991  8.620   37.949  1.00 11.51 ? 448  MET B SD  1 
ATOM   8141  C  CE  . MET B 1 456 ? 24.914  8.082   36.635  1.00 10.54 ? 448  MET B CE  1 
ATOM   8142  N  N   . LYS B 1 457 ? 23.454  7.417   43.432  1.00 12.76 ? 449  LYS B N   1 
ATOM   8143  C  CA  . LYS B 1 457 ? 22.951  8.106   44.623  1.00 12.23 ? 449  LYS B CA  1 
ATOM   8144  C  C   . LYS B 1 457 ? 22.725  9.591   44.335  1.00 14.63 ? 449  LYS B C   1 
ATOM   8145  O  O   . LYS B 1 457 ? 23.066  10.459  45.141  1.00 12.52 ? 449  LYS B O   1 
ATOM   8146  C  CB  . LYS B 1 457 ? 23.879  7.910   45.831  1.00 12.63 ? 449  LYS B CB  1 
ATOM   8147  C  CG  . LYS B 1 457 ? 24.122  6.447   46.190  1.00 16.25 ? 449  LYS B CG  1 
ATOM   8148  C  CD  . LYS B 1 457 ? 24.692  6.308   47.596  1.00 29.10 ? 449  LYS B CD  1 
ATOM   8149  C  CE  . LYS B 1 457 ? 23.598  6.514   48.646  1.00 38.93 ? 449  LYS B CE  1 
ATOM   8150  N  NZ  . LYS B 1 457 ? 24.126  6.941   49.974  1.00 38.39 ? 449  LYS B NZ  1 
ATOM   8151  N  N   . ILE B 1 458 ? 22.153  9.875   43.166  1.00 12.32 ? 450  ILE B N   1 
ATOM   8152  C  CA  . ILE B 1 458 ? 21.766  11.222  42.768  1.00 12.63 ? 450  ILE B CA  1 
ATOM   8153  C  C   . ILE B 1 458 ? 20.238  11.285  42.737  1.00 13.64 ? 450  ILE B C   1 
ATOM   8154  O  O   . ILE B 1 458 ? 19.552  10.267  42.838  1.00 11.22 ? 450  ILE B O   1 
ATOM   8155  C  CB  . ILE B 1 458 ? 22.375  11.615  41.411  1.00 13.78 ? 450  ILE B CB  1 
ATOM   8156  C  CG1 . ILE B 1 458 ? 21.979  10.584  40.347  1.00 10.92 ? 450  ILE B CG1 1 
ATOM   8157  C  CG2 . ILE B 1 458 ? 23.888  11.659  41.521  1.00 12.29 ? 450  ILE B CG2 1 
ATOM   8158  C  CD1 . ILE B 1 458 ? 22.520  10.925  38.936  1.00 15.96 ? 450  ILE B CD1 1 
ATOM   8159  N  N   . ASN B 1 459 ? 19.696  12.499  42.585  1.00 10.30 ? 451  ASN B N   1 
ATOM   8160  C  CA  . ASN B 1 459 ? 18.270  12.728  42.848  1.00 9.46  ? 451  ASN B CA  1 
ATOM   8161  C  C   . ASN B 1 459 ? 17.498  13.370  41.690  1.00 9.30  ? 451  ASN B C   1 
ATOM   8162  O  O   . ASN B 1 459 ? 16.690  14.276  41.904  1.00 12.95 ? 451  ASN B O   1 
ATOM   8163  C  CB  . ASN B 1 459 ? 18.114  13.566  44.117  1.00 14.09 ? 451  ASN B CB  1 
ATOM   8164  C  CG  . ASN B 1 459 ? 18.801  14.929  44.031  1.00 15.01 ? 451  ASN B CG  1 
ATOM   8165  O  OD1 . ASN B 1 459 ? 19.429  15.276  43.030  1.00 11.99 ? 451  ASN B OD1 1 
ATOM   8166  N  ND2 . ASN B 1 459 ? 18.678  15.707  45.102  1.00 15.75 ? 451  ASN B ND2 1 
ATOM   8167  N  N   . PRO B 1 460 ? 17.642  12.872  40.463  1.00 11.95 ? 452  PRO B N   1 
ATOM   8168  C  CA  . PRO B 1 460 ? 16.699  13.287  39.427  1.00 10.49 ? 452  PRO B CA  1 
ATOM   8169  C  C   . PRO B 1 460 ? 15.327  12.713  39.746  1.00 12.33 ? 452  PRO B C   1 
ATOM   8170  O  O   . PRO B 1 460 ? 15.191  11.745  40.497  1.00 12.10 ? 452  PRO B O   1 
ATOM   8171  C  CB  . PRO B 1 460 ? 17.272  12.674  38.150  1.00 13.88 ? 452  PRO B CB  1 
ATOM   8172  C  CG  . PRO B 1 460 ? 17.884  11.417  38.624  1.00 9.48  ? 452  PRO B CG  1 
ATOM   8173  C  CD  . PRO B 1 460 ? 18.506  11.782  39.970  1.00 8.75  ? 452  PRO B CD  1 
ATOM   8174  N  N   . VAL B 1 461 ? 14.301  13.322  39.167  1.00 12.27 ? 453  VAL B N   1 
ATOM   8175  C  CA  . VAL B 1 461 ? 12.920  12.932  39.421  1.00 11.38 ? 453  VAL B CA  1 
ATOM   8176  C  C   . VAL B 1 461 ? 12.309  12.460  38.106  1.00 11.94 ? 453  VAL B C   1 
ATOM   8177  O  O   . VAL B 1 461 ? 12.188  13.240  37.155  1.00 12.15 ? 453  VAL B O   1 
ATOM   8178  C  CB  . VAL B 1 461 ? 12.107  14.087  40.022  1.00 11.67 ? 453  VAL B CB  1 
ATOM   8179  C  CG1 . VAL B 1 461 ? 10.649  13.650  40.209  1.00 10.84 ? 453  VAL B CG1 1 
ATOM   8180  C  CG2 . VAL B 1 461 ? 12.721  14.541  41.365  1.00 13.83 ? 453  VAL B CG2 1 
ATOM   8181  N  N   . PHE B 1 462 ? 11.934  11.192  38.052  1.00 8.97  ? 454  PHE B N   1 
ATOM   8182  C  CA  . PHE B 1 462 ? 11.380  10.591  36.844  1.00 9.24  ? 454  PHE B CA  1 
ATOM   8183  C  C   . PHE B 1 462 ? 9.865   10.573  36.983  1.00 10.87 ? 454  PHE B C   1 
ATOM   8184  O  O   . PHE B 1 462 ? 9.338   9.977   37.926  1.00 12.16 ? 454  PHE B O   1 
ATOM   8185  C  CB  . PHE B 1 462 ? 11.933  9.181   36.647  1.00 11.85 ? 454  PHE B CB  1 
ATOM   8186  C  CG  . PHE B 1 462 ? 13.429  9.142   36.532  1.00 11.95 ? 454  PHE B CG  1 
ATOM   8187  C  CD1 . PHE B 1 462 ? 14.037  9.417   35.321  1.00 11.90 ? 454  PHE B CD1 1 
ATOM   8188  C  CD2 . PHE B 1 462 ? 14.226  8.825   37.634  1.00 10.77 ? 454  PHE B CD2 1 
ATOM   8189  C  CE1 . PHE B 1 462 ? 15.426  9.393   35.202  1.00 12.81 ? 454  PHE B CE1 1 
ATOM   8190  C  CE2 . PHE B 1 462 ? 15.604  8.805   37.530  1.00 8.16  ? 454  PHE B CE2 1 
ATOM   8191  C  CZ  . PHE B 1 462 ? 16.207  9.079   36.301  1.00 9.29  ? 454  PHE B CZ  1 
ATOM   8192  N  N   . VAL B 1 463 ? 9.181   11.245  36.063  1.00 13.17 ? 455  VAL B N   1 
ATOM   8193  C  CA  . VAL B 1 463 ? 7.730   11.418  36.107  1.00 12.78 ? 455  VAL B CA  1 
ATOM   8194  C  C   . VAL B 1 463 ? 7.104   10.499  35.073  1.00 11.31 ? 455  VAL B C   1 
ATOM   8195  O  O   . VAL B 1 463 ? 7.601   10.394  33.944  1.00 10.40 ? 455  VAL B O   1 
ATOM   8196  C  CB  . VAL B 1 463 ? 7.353   12.893  35.858  1.00 11.32 ? 455  VAL B CB  1 
ATOM   8197  C  CG1 . VAL B 1 463 ? 5.830   13.080  35.800  1.00 11.70 ? 455  VAL B CG1 1 
ATOM   8198  C  CG2 . VAL B 1 463 ? 7.945   13.780  36.959  1.00 11.65 ? 455  VAL B CG2 1 
ATOM   8199  N  N   . PHE B 1 464 ? 6.022   9.814   35.458  1.00 11.25 ? 456  PHE B N   1 
ATOM   8200  C  CA  . PHE B 1 464 ? 5.324   8.904   34.559  1.00 10.86 ? 456  PHE B CA  1 
ATOM   8201  C  C   . PHE B 1 464 ? 3.828   9.176   34.627  1.00 10.11 ? 456  PHE B C   1 
ATOM   8202  O  O   . PHE B 1 464 ? 3.264   9.307   35.716  1.00 14.53 ? 456  PHE B O   1 
ATOM   8203  C  CB  . PHE B 1 464 ? 5.635   7.435   34.910  1.00 9.41  ? 456  PHE B CB  1 
ATOM   8204  C  CG  . PHE B 1 464 ? 7.103   7.099   34.821  1.00 14.44 ? 456  PHE B CG  1 
ATOM   8205  C  CD1 . PHE B 1 464 ? 7.715   6.961   33.586  1.00 12.21 ? 456  PHE B CD1 1 
ATOM   8206  C  CD2 . PHE B 1 464 ? 7.874   6.963   35.968  1.00 13.65 ? 456  PHE B CD2 1 
ATOM   8207  C  CE1 . PHE B 1 464 ? 9.074   6.684   33.486  1.00 8.70  ? 456  PHE B CE1 1 
ATOM   8208  C  CE2 . PHE B 1 464 ? 9.244   6.688   35.880  1.00 11.00 ? 456  PHE B CE2 1 
ATOM   8209  C  CZ  . PHE B 1 464 ? 9.840   6.546   34.634  1.00 8.56  ? 456  PHE B CZ  1 
ATOM   8210  N  N   . THR B 1 465 ? 3.184   9.256   33.466  1.00 12.00 ? 457  THR B N   1 
ATOM   8211  C  CA  . THR B 1 465 ? 1.734   9.363   33.408  1.00 13.54 ? 457  THR B CA  1 
ATOM   8212  C  C   . THR B 1 465 ? 1.182   8.104   32.752  1.00 12.32 ? 457  THR B C   1 
ATOM   8213  O  O   . THR B 1 465 ? 1.925   7.176   32.436  1.00 11.38 ? 457  THR B O   1 
ATOM   8214  C  CB  . THR B 1 465 ? 1.319   10.623  32.656  1.00 12.76 ? 457  THR B CB  1 
ATOM   8215  O  OG1 . THR B 1 465 ? 1.738   10.511  31.293  1.00 13.96 ? 457  THR B OG1 1 
ATOM   8216  C  CG2 . THR B 1 465 ? 1.992   11.860  33.288  1.00 14.54 ? 457  THR B CG2 1 
ATOM   8217  N  N   . HIS B 1 466 ? -0.137  8.058   32.568  1.00 11.16 ? 458  HIS B N   1 
ATOM   8218  C  CA  . HIS B 1 466 ? -0.766  6.934   31.874  1.00 13.43 ? 458  HIS B CA  1 
ATOM   8219  C  C   . HIS B 1 466 ? -0.376  5.613   32.541  1.00 12.47 ? 458  HIS B C   1 
ATOM   8220  O  O   . HIS B 1 466 ? 0.175   4.701   31.926  1.00 11.05 ? 458  HIS B O   1 
ATOM   8221  C  CB  . HIS B 1 466 ? -0.387  6.933   30.382  1.00 14.85 ? 458  HIS B CB  1 
ATOM   8222  C  CG  . HIS B 1 466 ? -0.975  8.068   29.604  1.00 20.76 ? 458  HIS B CG  1 
ATOM   8223  N  ND1 . HIS B 1 466 ? -0.630  9.385   29.822  1.00 21.86 ? 458  HIS B ND1 1 
ATOM   8224  C  CD2 . HIS B 1 466 ? -1.895  8.081   28.610  1.00 24.03 ? 458  HIS B CD2 1 
ATOM   8225  C  CE1 . HIS B 1 466 ? -1.311  10.159  28.996  1.00 26.64 ? 458  HIS B CE1 1 
ATOM   8226  N  NE2 . HIS B 1 466 ? -2.085  9.392   28.250  1.00 20.54 ? 458  HIS B NE2 1 
ATOM   8227  N  N   . ASP B 1 467 ? -0.688  5.520   33.826  1.00 10.92 ? 459  ASP B N   1 
ATOM   8228  C  CA  . ASP B 1 467 ? -0.065  4.523   34.676  1.00 10.64 ? 459  ASP B CA  1 
ATOM   8229  C  C   . ASP B 1 467 ? -0.774  3.168   34.704  1.00 13.00 ? 459  ASP B C   1 
ATOM   8230  O  O   . ASP B 1 467 ? -0.304  2.270   35.409  1.00 15.45 ? 459  ASP B O   1 
ATOM   8231  C  CB  . ASP B 1 467 ? 0.037   5.079   36.100  1.00 10.77 ? 459  ASP B CB  1 
ATOM   8232  C  CG  . ASP B 1 467 ? -1.295  5.092   36.822  1.00 16.64 ? 459  ASP B CG  1 
ATOM   8233  O  OD1 . ASP B 1 467 ? -2.332  5.328   36.170  1.00 15.58 ? 459  ASP B OD1 1 
ATOM   8234  O  OD2 . ASP B 1 467 ? -1.299  4.878   38.052  1.00 16.66 ? 459  ASP B OD2 1 
ATOM   8235  N  N   . SER B 1 468 ? -1.884  2.976   33.990  1.00 11.86 ? 460  SER B N   1 
ATOM   8236  C  CA  . SER B 1 468 ? -2.592  1.706   34.126  1.00 11.17 ? 460  SER B CA  1 
ATOM   8237  C  C   . SER B 1 468 ? -3.518  1.491   32.930  1.00 13.08 ? 460  SER B C   1 
ATOM   8238  O  O   . SER B 1 468 ? -3.518  2.263   31.968  1.00 13.09 ? 460  SER B O   1 
ATOM   8239  C  CB  . SER B 1 468 ? -3.383  1.669   35.440  1.00 11.56 ? 460  SER B CB  1 
ATOM   8240  O  OG  . SER B 1 468 ? -4.600  2.392   35.295  1.00 12.05 ? 460  SER B OG  1 
ATOM   8241  N  N   . ILE B 1 469 ? -4.333  0.437   33.008  1.00 11.61 ? 461  ILE B N   1 
ATOM   8242  C  CA  . ILE B 1 469 ? -5.412  0.260   32.046  1.00 13.14 ? 461  ILE B CA  1 
ATOM   8243  C  C   . ILE B 1 469 ? -6.343  1.467   32.009  1.00 21.35 ? 461  ILE B C   1 
ATOM   8244  O  O   . ILE B 1 469 ? -7.083  1.644   31.032  1.00 16.40 ? 461  ILE B O   1 
ATOM   8245  C  CB  . ILE B 1 469 ? -6.187  -1.032  32.363  1.00 13.46 ? 461  ILE B CB  1 
ATOM   8246  C  CG1 . ILE B 1 469 ? -6.650  -1.038  33.828  1.00 12.67 ? 461  ILE B CG1 1 
ATOM   8247  C  CG2 . ILE B 1 469 ? -5.301  -2.249  32.073  1.00 11.78 ? 461  ILE B CG2 1 
ATOM   8248  C  CD1 . ILE B 1 469 ? -7.683  -2.131  34.139  1.00 13.15 ? 461  ILE B CD1 1 
ATOM   8249  N  N   . GLY B 1 470 ? -6.315  2.318   33.044  1.00 12.55 ? 462  GLY B N   1 
ATOM   8250  C  CA  . GLY B 1 470 ? -7.088  3.555   33.016  1.00 13.81 ? 462  GLY B CA  1 
ATOM   8251  C  C   . GLY B 1 470 ? -6.788  4.476   31.844  1.00 13.06 ? 462  GLY B C   1 
ATOM   8252  O  O   . GLY B 1 470 ? -7.561  5.402   31.583  1.00 13.81 ? 462  GLY B O   1 
ATOM   8253  N  N   . LEU B 1 471 ? -5.671  4.267   31.143  1.00 12.56 ? 463  LEU B N   1 
ATOM   8254  C  CA  . LEU B 1 471 ? -5.407  5.089   29.962  1.00 13.12 ? 463  LEU B CA  1 
ATOM   8255  C  C   . LEU B 1 471 ? -6.348  4.749   28.805  1.00 16.26 ? 463  LEU B C   1 
ATOM   8256  O  O   . LEU B 1 471 ? -6.529  5.580   27.901  1.00 14.43 ? 463  LEU B O   1 
ATOM   8257  C  CB  . LEU B 1 471 ? -3.937  4.961   29.536  1.00 12.11 ? 463  LEU B CB  1 
ATOM   8258  C  CG  . LEU B 1 471 ? -3.361  3.674   28.944  1.00 14.80 ? 463  LEU B CG  1 
ATOM   8259  C  CD1 . LEU B 1 471 ? -3.705  3.500   27.456  1.00 12.02 ? 463  LEU B CD1 1 
ATOM   8260  C  CD2 . LEU B 1 471 ? -1.842  3.664   29.139  1.00 16.05 ? 463  LEU B CD2 1 
ATOM   8261  N  N   . GLY B 1 472 ? -6.928  3.551   28.798  1.00 17.44 ? 464  GLY B N   1 
ATOM   8262  C  CA  . GLY B 1 472 ? -8.044  3.240   27.899  1.00 15.80 ? 464  GLY B CA  1 
ATOM   8263  C  C   . GLY B 1 472 ? -7.604  2.708   26.531  1.00 15.47 ? 464  GLY B C   1 
ATOM   8264  O  O   . GLY B 1 472 ? -6.900  1.709   26.447  1.00 13.21 ? 464  GLY B O   1 
ATOM   8265  N  N   . GLU B 1 473 ? -8.053  3.380   25.467  1.00 13.99 ? 465  GLU B N   1 
ATOM   8266  C  CA  . GLU B 1 473 ? -8.156  2.745   24.160  1.00 15.80 ? 465  GLU B CA  1 
ATOM   8267  C  C   . GLU B 1 473 ? -6.813  2.416   23.515  1.00 15.91 ? 465  GLU B C   1 
ATOM   8268  O  O   . GLU B 1 473 ? -6.783  1.559   22.625  1.00 16.95 ? 465  GLU B O   1 
ATOM   8269  C  CB  . GLU B 1 473 ? -8.965  3.626   23.214  1.00 14.94 ? 465  GLU B CB  1 
ATOM   8270  C  CG  . GLU B 1 473 ? -10.468 3.677   23.519  1.00 16.49 ? 465  GLU B CG  1 
ATOM   8271  C  CD  . GLU B 1 473 ? -10.864 4.747   24.538  1.00 17.58 ? 465  GLU B CD  1 
ATOM   8272  O  OE1 . GLU B 1 473 ? -10.014 5.201   25.341  1.00 16.70 ? 465  GLU B OE1 1 
ATOM   8273  O  OE2 . GLU B 1 473 ? -12.052 5.130   24.528  1.00 17.73 ? 465  GLU B OE2 1 
ATOM   8274  N  N   . ASP B 1 474 ? -5.716  3.069   23.920  1.00 17.20 ? 466  ASP B N   1 
ATOM   8275  C  CA  . ASP B 1 474 ? -4.421  2.767   23.303  1.00 16.37 ? 466  ASP B CA  1 
ATOM   8276  C  C   . ASP B 1 474 ? -4.049  1.297   23.452  1.00 17.82 ? 466  ASP B C   1 
ATOM   8277  O  O   . ASP B 1 474 ? -3.308  0.761   22.624  1.00 18.71 ? 466  ASP B O   1 
ATOM   8278  C  CB  . ASP B 1 474 ? -3.317  3.644   23.895  1.00 12.64 ? 466  ASP B CB  1 
ATOM   8279  C  CG  . ASP B 1 474 ? -3.272  5.031   23.281  1.00 24.62 ? 466  ASP B CG  1 
ATOM   8280  O  OD1 . ASP B 1 474 ? -3.972  5.268   22.271  1.00 28.45 ? 466  ASP B OD1 1 
ATOM   8281  O  OD2 . ASP B 1 474 ? -2.533  5.889   23.816  1.00 23.96 ? 466  ASP B OD2 1 
ATOM   8282  N  N   . GLY B 1 475 ? -4.536  0.630   24.496  1.00 17.29 ? 467  GLY B N   1 
ATOM   8283  C  CA  . GLY B 1 475 ? -4.480  -0.814  24.541  1.00 12.24 ? 467  GLY B CA  1 
ATOM   8284  C  C   . GLY B 1 475 ? -3.209  -1.403  25.127  1.00 11.71 ? 467  GLY B C   1 
ATOM   8285  O  O   . GLY B 1 475 ? -2.393  -0.704  25.726  1.00 11.42 ? 467  GLY B O   1 
ATOM   8286  N  N   . PRO B 1 476 ? -3.027  -2.716  24.953  1.00 11.63 ? 468  PRO B N   1 
ATOM   8287  C  CA  . PRO B 1 476 ? -2.032  -3.447  25.769  1.00 13.83 ? 468  PRO B CA  1 
ATOM   8288  C  C   . PRO B 1 476 ? -0.582  -3.081  25.507  1.00 14.54 ? 468  PRO B C   1 
ATOM   8289  O  O   . PRO B 1 476 ? 0.252   -3.321  26.393  1.00 11.83 ? 468  PRO B O   1 
ATOM   8290  C  CB  . PRO B 1 476 ? -2.301  -4.921  25.422  1.00 12.19 ? 468  PRO B CB  1 
ATOM   8291  C  CG  . PRO B 1 476 ? -3.020  -4.878  24.060  1.00 14.85 ? 468  PRO B CG  1 
ATOM   8292  C  CD  . PRO B 1 476 ? -3.876  -3.627  24.166  1.00 11.98 ? 468  PRO B CD  1 
ATOM   8293  N  N   . THR B 1 477 ? -0.229  -2.530  24.341  1.00 11.12 ? 469  THR B N   1 
ATOM   8294  C  CA  . THR B 1 477 ? 1.169   -2.137  24.168  1.00 12.58 ? 469  THR B CA  1 
ATOM   8295  C  C   . THR B 1 477 ? 1.530   -0.956  25.047  1.00 15.20 ? 469  THR B C   1 
ATOM   8296  O  O   . THR B 1 477 ? 2.716   -0.746  25.324  1.00 14.05 ? 469  THR B O   1 
ATOM   8297  C  CB  . THR B 1 477 ? 1.500   -1.755  22.722  1.00 12.71 ? 469  THR B CB  1 
ATOM   8298  O  OG1 . THR B 1 477 ? 0.863   -0.523  22.394  1.00 11.53 ? 469  THR B OG1 1 
ATOM   8299  C  CG2 . THR B 1 477 ? 1.073   -2.821  21.739  1.00 11.58 ? 469  THR B CG2 1 
ATOM   8300  N  N   . HIS B 1 478 ? 0.532   -0.170  25.471  1.00 10.80 ? 470  HIS B N   1 
ATOM   8301  C  CA  . HIS B 1 478 ? 0.770   1.030   26.258  1.00 10.66 ? 470  HIS B CA  1 
ATOM   8302  C  C   . HIS B 1 478 ? 0.317   0.922   27.706  1.00 12.72 ? 470  HIS B C   1 
ATOM   8303  O  O   . HIS B 1 478 ? 0.783   1.710   28.530  1.00 12.70 ? 470  HIS B O   1 
ATOM   8304  C  CB  . HIS B 1 478 ? 0.056   2.236   25.626  1.00 14.04 ? 470  HIS B CB  1 
ATOM   8305  C  CG  . HIS B 1 478 ? 0.776   2.810   24.450  1.00 19.72 ? 470  HIS B CG  1 
ATOM   8306  N  ND1 . HIS B 1 478 ? 1.301   2.024   23.446  1.00 22.86 ? 470  HIS B ND1 1 
ATOM   8307  C  CD2 . HIS B 1 478 ? 1.070   4.089   24.121  1.00 22.07 ? 470  HIS B CD2 1 
ATOM   8308  C  CE1 . HIS B 1 478 ? 1.884   2.796   22.547  1.00 25.17 ? 470  HIS B CE1 1 
ATOM   8309  N  NE2 . HIS B 1 478 ? 1.754   4.053   22.928  1.00 22.70 ? 470  HIS B NE2 1 
ATOM   8310  N  N   . GLN B 1 479 ? -0.615  0.011   28.023  1.00 12.07 ? 471  GLN B N   1 
ATOM   8311  C  CA  . GLN B 1 479 ? -1.169  -0.075  29.384  1.00 10.66 ? 471  GLN B CA  1 
ATOM   8312  C  C   . GLN B 1 479 ? -0.191  -0.750  30.340  1.00 10.33 ? 471  GLN B C   1 
ATOM   8313  O  O   . GLN B 1 479 ? 0.107   -1.938  30.168  1.00 11.82 ? 471  GLN B O   1 
ATOM   8314  C  CB  . GLN B 1 479 ? -2.486  -0.838  29.370  1.00 10.99 ? 471  GLN B CB  1 
ATOM   8315  C  CG  . GLN B 1 479 ? -3.595  -0.099  28.628  1.00 11.42 ? 471  GLN B CG  1 
ATOM   8316  C  CD  . GLN B 1 479 ? -4.711  -1.035  28.176  1.00 11.75 ? 471  GLN B CD  1 
ATOM   8317  O  OE1 . GLN B 1 479 ? -4.535  -2.241  28.124  1.00 15.12 ? 471  GLN B OE1 1 
ATOM   8318  N  NE2 . GLN B 1 479 ? -5.866  -0.467  27.834  1.00 13.37 ? 471  GLN B NE2 1 
ATOM   8319  N  N   . PRO B 1 480 ? 0.316   -0.049  31.354  1.00 11.99 ? 472  PRO B N   1 
ATOM   8320  C  CA  . PRO B 1 480 ? 1.246   -0.692  32.286  1.00 11.10 ? 472  PRO B CA  1 
ATOM   8321  C  C   . PRO B 1 480 ? 0.548   -1.776  33.077  1.00 10.16 ? 472  PRO B C   1 
ATOM   8322  O  O   . PRO B 1 480 ? -0.620  -1.644  33.441  1.00 12.26 ? 472  PRO B O   1 
ATOM   8323  C  CB  . PRO B 1 480 ? 1.692   0.453   33.206  1.00 11.78 ? 472  PRO B CB  1 
ATOM   8324  C  CG  . PRO B 1 480 ? 1.399   1.712   32.422  1.00 13.12 ? 472  PRO B CG  1 
ATOM   8325  C  CD  . PRO B 1 480 ? 0.135   1.381   31.655  1.00 12.50 ? 472  PRO B CD  1 
ATOM   8326  N  N   . ILE B 1 481 ? 1.292   -2.841  33.366  1.00 14.27 ? 473  ILE B N   1 
ATOM   8327  C  CA  . ILE B 1 481 ? 0.790   -3.949  34.165  1.00 10.30 ? 473  ILE B CA  1 
ATOM   8328  C  C   . ILE B 1 481 ? 1.809   -4.218  35.258  1.00 10.24 ? 473  ILE B C   1 
ATOM   8329  O  O   . ILE B 1 481 ? 1.511   -4.103  36.452  1.00 11.66 ? 473  ILE B O   1 
ATOM   8330  C  CB  . ILE B 1 481 ? 0.556   -5.221  33.325  1.00 10.41 ? 473  ILE B CB  1 
ATOM   8331  C  CG1 . ILE B 1 481 ? -0.492  -4.979  32.230  1.00 10.54 ? 473  ILE B CG1 1 
ATOM   8332  C  CG2 . ILE B 1 481 ? 0.116   -6.379  34.230  1.00 12.45 ? 473  ILE B CG2 1 
ATOM   8333  C  CD1 . ILE B 1 481 ? -1.861  -4.661  32.758  1.00 13.23 ? 473  ILE B CD1 1 
ATOM   8334  N  N   . GLU B 1 482 ? 3.021   -4.549  34.837  1.00 10.72 ? 474  GLU B N   1 
ATOM   8335  C  CA  . GLU B 1 482 ? 4.104   -4.933  35.728  1.00 13.57 ? 474  GLU B CA  1 
ATOM   8336  C  C   . GLU B 1 482 ? 5.089   -3.800  36.016  1.00 14.11 ? 474  GLU B C   1 
ATOM   8337  O  O   . GLU B 1 482 ? 5.956   -3.971  36.877  1.00 10.54 ? 474  GLU B O   1 
ATOM   8338  C  CB  . GLU B 1 482 ? 4.853   -6.144  35.136  1.00 10.05 ? 474  GLU B CB  1 
ATOM   8339  C  CG  . GLU B 1 482 ? 5.709   -5.877  33.867  1.00 9.80  ? 474  GLU B CG  1 
ATOM   8340  C  CD  . GLU B 1 482 ? 4.914   -5.893  32.565  1.00 13.49 ? 474  GLU B CD  1 
ATOM   8341  O  OE1 . GLU B 1 482 ? 3.724   -5.471  32.568  1.00 12.18 ? 474  GLU B OE1 1 
ATOM   8342  O  OE2 . GLU B 1 482 ? 5.480   -6.319  31.529  1.00 12.65 ? 474  GLU B OE2 1 
ATOM   8343  N  N   . GLN B 1 483 ? 4.953   -2.638  35.365  1.00 12.54 ? 475  GLN B N   1 
ATOM   8344  C  CA  . GLN B 1 483 ? 6.022   -1.633  35.405  1.00 12.55 ? 475  GLN B CA  1 
ATOM   8345  C  C   . GLN B 1 483 ? 6.243   -1.088  36.812  1.00 12.52 ? 475  GLN B C   1 
ATOM   8346  O  O   . GLN B 1 483 ? 7.385   -0.967  37.267  1.00 10.45 ? 475  GLN B O   1 
ATOM   8347  C  CB  . GLN B 1 483 ? 5.715   -0.475  34.446  1.00 10.82 ? 475  GLN B CB  1 
ATOM   8348  C  CG  . GLN B 1 483 ? 6.034   -0.804  33.001  1.00 9.97  ? 475  GLN B CG  1 
ATOM   8349  C  CD  . GLN B 1 483 ? 5.135   -1.905  32.484  1.00 14.56 ? 475  GLN B CD  1 
ATOM   8350  O  OE1 . GLN B 1 483 ? 3.961   -1.935  32.808  1.00 10.93 ? 475  GLN B OE1 1 
ATOM   8351  N  NE2 . GLN B 1 483 ? 5.686   -2.831  31.712  1.00 12.69 ? 475  GLN B NE2 1 
ATOM   8352  N  N   . THR B 1 484 ? 5.164   -0.705  37.502  1.00 9.18  ? 476  THR B N   1 
ATOM   8353  C  CA  . THR B 1 484 ? 5.328   -0.142  38.844  1.00 11.03 ? 476  THR B CA  1 
ATOM   8354  C  C   . THR B 1 484 ? 5.969   -1.154  39.780  1.00 10.38 ? 476  THR B C   1 
ATOM   8355  O  O   . THR B 1 484 ? 6.880   -0.813  40.549  1.00 10.24 ? 476  THR B O   1 
ATOM   8356  C  CB  . THR B 1 484 ? 3.980   0.334   39.403  1.00 11.46 ? 476  THR B CB  1 
ATOM   8357  O  OG1 . THR B 1 484 ? 3.457   1.351   38.541  1.00 12.77 ? 476  THR B OG1 1 
ATOM   8358  C  CG2 . THR B 1 484 ? 4.149   0.922   40.849  1.00 10.85 ? 476  THR B CG2 1 
ATOM   8359  N  N   . ALA B 1 485 ? 5.535   -2.415  39.696  1.00 9.52  ? 477  ALA B N   1 
ATOM   8360  C  CA  . ALA B 1 485 ? 6.112   -3.461  40.535  1.00 13.50 ? 477  ALA B CA  1 
ATOM   8361  C  C   . ALA B 1 485 ? 7.605   -3.636  40.258  1.00 11.19 ? 477  ALA B C   1 
ATOM   8362  O  O   . ALA B 1 485 ? 8.397   -3.806  41.193  1.00 10.36 ? 477  ALA B O   1 
ATOM   8363  C  CB  . ALA B 1 485 ? 5.361   -4.774  40.318  1.00 9.68  ? 477  ALA B CB  1 
ATOM   8364  N  N   . THR B 1 486 ? 8.013   -3.573  38.981  1.00 11.72 ? 478  THR B N   1 
ATOM   8365  C  CA  . THR B 1 486 ? 9.435   -3.712  38.655  1.00 9.51  ? 478  THR B CA  1 
ATOM   8366  C  C   . THR B 1 486 ? 10.239  -2.495  39.106  1.00 9.28  ? 478  THR B C   1 
ATOM   8367  O  O   . THR B 1 486 ? 11.415  -2.628  39.469  1.00 10.28 ? 478  THR B O   1 
ATOM   8368  C  CB  . THR B 1 486 ? 9.663   -3.925  37.146  1.00 10.65 ? 478  THR B CB  1 
ATOM   8369  O  OG1 . THR B 1 486 ? 9.278   -2.753  36.410  1.00 13.24 ? 478  THR B OG1 1 
ATOM   8370  C  CG2 . THR B 1 486 ? 8.926   -5.155  36.617  1.00 10.33 ? 478  THR B CG2 1 
ATOM   8371  N  N   . LEU B 1 487 ? 9.653   -1.300  39.034  1.00 7.23  ? 479  LEU B N   1 
ATOM   8372  C  CA  . LEU B 1 487 ? 10.371  -0.108  39.484  1.00 8.83  ? 479  LEU B CA  1 
ATOM   8373  C  C   . LEU B 1 487 ? 10.676  -0.168  40.976  1.00 11.78 ? 479  LEU B C   1 
ATOM   8374  O  O   . LEU B 1 487 ? 11.728  0.318   41.416  1.00 8.33  ? 479  LEU B O   1 
ATOM   8375  C  CB  . LEU B 1 487 ? 9.565   1.153   39.150  1.00 10.06 ? 479  LEU B CB  1 
ATOM   8376  C  CG  . LEU B 1 487 ? 9.526   1.511   37.665  1.00 12.14 ? 479  LEU B CG  1 
ATOM   8377  C  CD1 . LEU B 1 487 ? 8.537   2.663   37.419  1.00 13.64 ? 479  LEU B CD1 1 
ATOM   8378  C  CD2 . LEU B 1 487 ? 10.913  1.906   37.158  1.00 10.93 ? 479  LEU B CD2 1 
ATOM   8379  N  N   . ARG B 1 488 ? 9.784   -0.780  41.760  1.00 10.79 ? 480  ARG B N   1 
ATOM   8380  C  CA  . ARG B 1 488 ? 9.967   -0.887  43.206  1.00 11.10 ? 480  ARG B CA  1 
ATOM   8381  C  C   . ARG B 1 488 ? 11.143  -1.786  43.582  1.00 11.01 ? 480  ARG B C   1 
ATOM   8382  O  O   . ARG B 1 488 ? 11.569  -1.778  44.741  1.00 11.77 ? 480  ARG B O   1 
ATOM   8383  C  CB  . ARG B 1 488 ? 8.693   -1.433  43.860  1.00 11.58 ? 480  ARG B CB  1 
ATOM   8384  C  CG  . ARG B 1 488 ? 7.515   -0.441  43.918  1.00 11.76 ? 480  ARG B CG  1 
ATOM   8385  C  CD  . ARG B 1 488 ? 6.216   -1.135  44.323  1.00 10.58 ? 480  ARG B CD  1 
ATOM   8386  N  NE  . ARG B 1 488 ? 5.107   -0.188  44.451  1.00 11.34 ? 480  ARG B NE  1 
ATOM   8387  C  CZ  . ARG B 1 488 ? 3.842   -0.453  44.134  1.00 11.16 ? 480  ARG B CZ  1 
ATOM   8388  N  NH1 . ARG B 1 488 ? 3.495   -1.642  43.646  1.00 10.17 ? 480  ARG B NH1 1 
ATOM   8389  N  NH2 . ARG B 1 488 ? 2.913   0.488   44.293  1.00 10.81 ? 480  ARG B NH2 1 
ATOM   8390  N  N   . LEU B 1 489 ? 11.653  -2.578  42.646  1.00 8.29  ? 481  LEU B N   1 
ATOM   8391  C  CA  . LEU B 1 489 ? 12.767  -3.479  42.929  1.00 10.59 ? 481  LEU B CA  1 
ATOM   8392  C  C   . LEU B 1 489 ? 14.134  -2.866  42.650  1.00 9.55  ? 481  LEU B C   1 
ATOM   8393  O  O   . LEU B 1 489 ? 15.152  -3.530  42.893  1.00 9.60  ? 481  LEU B O   1 
ATOM   8394  C  CB  . LEU B 1 489 ? 12.618  -4.771  42.115  1.00 9.73  ? 481  LEU B CB  1 
ATOM   8395  C  CG  . LEU B 1 489 ? 11.301  -5.510  42.352  1.00 13.44 ? 481  LEU B CG  1 
ATOM   8396  C  CD1 . LEU B 1 489 ? 11.271  -6.822  41.596  1.00 13.00 ? 481  LEU B CD1 1 
ATOM   8397  C  CD2 . LEU B 1 489 ? 11.064  -5.745  43.858  1.00 13.33 ? 481  LEU B CD2 1 
ATOM   8398  N  N   . ILE B 1 490 ? 14.186  -1.642  42.134  1.00 8.31  ? 482  ILE B N   1 
ATOM   8399  C  CA  . ILE B 1 490 ? 15.450  -0.937  41.922  1.00 11.65 ? 482  ILE B CA  1 
ATOM   8400  C  C   . ILE B 1 490 ? 15.992  -0.549  43.289  1.00 14.47 ? 482  ILE B C   1 
ATOM   8401  O  O   . ILE B 1 490 ? 15.318  0.178   44.032  1.00 11.45 ? 482  ILE B O   1 
ATOM   8402  C  CB  . ILE B 1 490 ? 15.269  0.308   41.042  1.00 11.22 ? 482  ILE B CB  1 
ATOM   8403  C  CG1 . ILE B 1 490 ? 14.715  -0.079  39.668  1.00 11.80 ? 482  ILE B CG1 1 
ATOM   8404  C  CG2 . ILE B 1 490 ? 16.591  1.080   40.907  1.00 12.40 ? 482  ILE B CG2 1 
ATOM   8405  C  CD1 . ILE B 1 490 ? 14.363  1.120   38.802  1.00 11.87 ? 482  ILE B CD1 1 
ATOM   8406  N  N   . PRO B 1 491 ? 17.167  -1.024  43.675  1.00 11.63 ? 483  PRO B N   1 
ATOM   8407  C  CA  . PRO B 1 491 ? 17.749  -0.575  44.943  1.00 11.10 ? 483  PRO B CA  1 
ATOM   8408  C  C   . PRO B 1 491 ? 17.894  0.938   44.941  1.00 13.56 ? 483  PRO B C   1 
ATOM   8409  O  O   . PRO B 1 491 ? 18.229  1.539   43.921  1.00 12.36 ? 483  PRO B O   1 
ATOM   8410  C  CB  . PRO B 1 491 ? 19.112  -1.273  44.976  1.00 10.73 ? 483  PRO B CB  1 
ATOM   8411  C  CG  . PRO B 1 491 ? 18.973  -2.446  44.051  1.00 12.01 ? 483  PRO B CG  1 
ATOM   8412  C  CD  . PRO B 1 491 ? 18.047  -1.958  42.954  1.00 11.04 ? 483  PRO B CD  1 
ATOM   8413  N  N   . ASN B 1 492 ? 17.621  1.553   46.095  1.00 14.11 ? 484  ASN B N   1 
ATOM   8414  C  CA  . ASN B 1 492 ? 17.833  2.992   46.298  1.00 15.27 ? 484  ASN B CA  1 
ATOM   8415  C  C   . ASN B 1 492 ? 16.966  3.842   45.374  1.00 14.67 ? 484  ASN B C   1 
ATOM   8416  O  O   . ASN B 1 492 ? 17.371  4.931   44.963  1.00 14.09 ? 484  ASN B O   1 
ATOM   8417  C  CB  . ASN B 1 492 ? 19.309  3.389   46.128  1.00 10.65 ? 484  ASN B CB  1 
ATOM   8418  C  CG  . ASN B 1 492 ? 19.619  4.718   46.781  1.00 11.40 ? 484  ASN B CG  1 
ATOM   8419  O  OD1 . ASN B 1 492 ? 19.154  4.993   47.890  1.00 14.46 ? 484  ASN B OD1 1 
ATOM   8420  N  ND2 . ASN B 1 492 ? 20.375  5.567   46.091  1.00 12.24 ? 484  ASN B ND2 1 
ATOM   8421  N  N   . MET B 1 493 ? 15.777  3.355   45.030  1.00 14.07 ? 485  MET B N   1 
ATOM   8422  C  CA  . MET B 1 493 ? 14.800  4.122   44.269  1.00 14.97 ? 485  MET B CA  1 
ATOM   8423  C  C   . MET B 1 493 ? 13.539  4.257   45.113  1.00 14.85 ? 485  MET B C   1 
ATOM   8424  O  O   . MET B 1 493 ? 13.079  3.265   45.689  1.00 14.32 ? 485  MET B O   1 
ATOM   8425  C  CB  . MET B 1 493 ? 14.482  3.423   42.942  1.00 11.84 ? 485  MET B CB  1 
ATOM   8426  C  CG  . MET B 1 493 ? 13.338  4.080   42.139  1.00 13.98 ? 485  MET B CG  1 
ATOM   8427  S  SD  . MET B 1 493 ? 13.753  5.710   41.496  1.00 13.69 ? 485  MET B SD  1 
ATOM   8428  C  CE  . MET B 1 493 ? 14.700  5.259   40.022  1.00 12.08 ? 485  MET B CE  1 
ATOM   8429  N  N   . ASP B 1 494 ? 12.991  5.476   45.208  1.00 10.89 ? 486  ASP B N   1 
ATOM   8430  C  CA  . ASP B 1 494 ? 11.659  5.674   45.783  1.00 12.06 ? 486  ASP B CA  1 
ATOM   8431  C  C   . ASP B 1 494 ? 10.613  5.702   44.675  1.00 13.37 ? 486  ASP B C   1 
ATOM   8432  O  O   . ASP B 1 494 ? 10.743  6.471   43.718  1.00 13.80 ? 486  ASP B O   1 
ATOM   8433  C  CB  . ASP B 1 494 ? 11.582  6.983   46.567  1.00 14.78 ? 486  ASP B CB  1 
ATOM   8434  C  CG  . ASP B 1 494 ? 12.220  6.883   47.943  1.00 14.65 ? 486  ASP B CG  1 
ATOM   8435  O  OD1 . ASP B 1 494 ? 12.628  5.766   48.331  1.00 16.52 ? 486  ASP B OD1 1 
ATOM   8436  O  OD2 . ASP B 1 494 ? 12.303  7.929   48.622  1.00 15.28 ? 486  ASP B OD2 1 
ATOM   8437  N  N   . VAL B 1 495 ? 9.562   4.899   44.819  1.00 8.54  ? 487  VAL B N   1 
ATOM   8438  C  CA  . VAL B 1 495 ? 8.458   4.878   43.863  1.00 8.91  ? 487  VAL B CA  1 
ATOM   8439  C  C   . VAL B 1 495 ? 7.225   5.429   44.567  1.00 12.04 ? 487  VAL B C   1 
ATOM   8440  O  O   . VAL B 1 495 ? 6.831   4.925   45.626  1.00 12.58 ? 487  VAL B O   1 
ATOM   8441  C  CB  . VAL B 1 495 ? 8.206   3.469   43.314  1.00 12.83 ? 487  VAL B CB  1 
ATOM   8442  C  CG1 . VAL B 1 495 ? 7.011   3.482   42.340  1.00 11.92 ? 487  VAL B CG1 1 
ATOM   8443  C  CG2 . VAL B 1 495 ? 9.457   2.968   42.619  1.00 13.24 ? 487  VAL B CG2 1 
ATOM   8444  N  N   . TRP B 1 496 ? 6.633   6.473   43.988  1.00 8.26  ? 488  TRP B N   1 
ATOM   8445  C  CA  . TRP B 1 496 ? 5.459   7.131   44.547  1.00 10.44 ? 488  TRP B CA  1 
ATOM   8446  C  C   . TRP B 1 496 ? 4.295   6.987   43.572  1.00 14.13 ? 488  TRP B C   1 
ATOM   8447  O  O   . TRP B 1 496 ? 4.464   7.205   42.369  1.00 14.97 ? 488  TRP B O   1 
ATOM   8448  C  CB  . TRP B 1 496 ? 5.735   8.612   44.806  1.00 10.07 ? 488  TRP B CB  1 
ATOM   8449  C  CG  . TRP B 1 496 ? 6.623   8.922   45.983  1.00 14.30 ? 488  TRP B CG  1 
ATOM   8450  C  CD1 . TRP B 1 496 ? 7.993   9.056   45.985  1.00 10.67 ? 488  TRP B CD1 1 
ATOM   8451  C  CD2 . TRP B 1 496 ? 6.193   9.173   47.322  1.00 13.39 ? 488  TRP B CD2 1 
ATOM   8452  N  NE1 . TRP B 1 496 ? 8.433   9.371   47.255  1.00 11.68 ? 488  TRP B NE1 1 
ATOM   8453  C  CE2 . TRP B 1 496 ? 7.348   9.446   48.091  1.00 15.36 ? 488  TRP B CE2 1 
ATOM   8454  C  CE3 . TRP B 1 496 ? 4.933   9.203   47.948  1.00 13.21 ? 488  TRP B CE3 1 
ATOM   8455  C  CZ2 . TRP B 1 496 ? 7.284   9.730   49.457  1.00 18.60 ? 488  TRP B CZ2 1 
ATOM   8456  C  CZ3 . TRP B 1 496 ? 4.873   9.474   49.292  1.00 17.49 ? 488  TRP B CZ3 1 
ATOM   8457  C  CH2 . TRP B 1 496 ? 6.042   9.737   50.037  1.00 19.58 ? 488  TRP B CH2 1 
ATOM   8458  N  N   . ARG B 1 497 ? 3.115   6.621   44.084  1.00 10.68 ? 489  ARG B N   1 
ATOM   8459  C  CA  . ARG B 1 497 ? 1.900   6.519   43.266  1.00 10.23 ? 489  ARG B CA  1 
ATOM   8460  C  C   . ARG B 1 497 ? 0.773   7.218   44.012  1.00 13.22 ? 489  ARG B C   1 
ATOM   8461  O  O   . ARG B 1 497 ? -0.100  6.563   44.603  1.00 13.86 ? 489  ARG B O   1 
ATOM   8462  C  CB  . ARG B 1 497 ? 1.562   5.058   42.947  1.00 9.39  ? 489  ARG B CB  1 
ATOM   8463  C  CG  . ARG B 1 497 ? 0.428   4.870   41.916  1.00 9.75  ? 489  ARG B CG  1 
ATOM   8464  C  CD  . ARG B 1 497 ? 0.254   3.399   41.554  1.00 12.20 ? 489  ARG B CD  1 
ATOM   8465  N  NE  . ARG B 1 497 ? -0.695  3.200   40.455  1.00 13.61 ? 489  ARG B NE  1 
ATOM   8466  C  CZ  . ARG B 1 497 ? -1.931  2.726   40.610  1.00 17.56 ? 489  ARG B CZ  1 
ATOM   8467  N  NH1 . ARG B 1 497 ? -2.366  2.407   41.822  1.00 15.12 ? 489  ARG B NH1 1 
ATOM   8468  N  NH2 . ARG B 1 497 ? -2.737  2.567   39.555  1.00 14.21 ? 489  ARG B NH2 1 
ATOM   8469  N  N   . PRO B 1 498 ? 0.753   8.548   43.996  1.00 13.56 ? 490  PRO B N   1 
ATOM   8470  C  CA  . PRO B 1 498 ? -0.158  9.288   44.883  1.00 14.13 ? 490  PRO B CA  1 
ATOM   8471  C  C   . PRO B 1 498 ? -1.612  9.197   44.442  1.00 17.40 ? 490  PRO B C   1 
ATOM   8472  O  O   . PRO B 1 498 ? -1.929  9.096   43.253  1.00 15.25 ? 490  PRO B O   1 
ATOM   8473  C  CB  . PRO B 1 498 ? 0.356   10.730  44.798  1.00 11.81 ? 490  PRO B CB  1 
ATOM   8474  C  CG  . PRO B 1 498 ? 1.119   10.802  43.524  1.00 15.98 ? 490  PRO B CG  1 
ATOM   8475  C  CD  . PRO B 1 498 ? 1.690   9.435   43.282  1.00 13.98 ? 490  PRO B CD  1 
ATOM   8476  N  N   . CYS B 1 499 ? -2.515  9.247   45.423  1.00 17.06 ? 491  CYS B N   1 
ATOM   8477  C  CA  . CYS B 1 499 ? -3.928  9.107   45.103  1.00 13.44 ? 491  CYS B CA  1 
ATOM   8478  C  C   . CYS B 1 499 ? -4.661  10.428  44.936  1.00 19.11 ? 491  CYS B C   1 
ATOM   8479  O  O   . CYS B 1 499 ? -5.771  10.423  44.400  1.00 20.29 ? 491  CYS B O   1 
ATOM   8480  C  CB  . CYS B 1 499 ? -4.649  8.260   46.164  1.00 17.50 ? 491  CYS B CB  1 
ATOM   8481  S  SG  . CYS B 1 499 ? -4.947  9.080   47.762  1.00 20.88 ? 491  CYS B SG  1 
ATOM   8482  N  N   . ASP B 1 500 ? -4.096  11.551  45.363  1.00 14.73 ? 492  ASP B N   1 
ATOM   8483  C  CA  . ASP B 1 500 ? -4.794  12.821  45.195  1.00 15.88 ? 492  ASP B CA  1 
ATOM   8484  C  C   . ASP B 1 500 ? -3.769  13.946  45.245  1.00 15.89 ? 492  ASP B C   1 
ATOM   8485  O  O   . ASP B 1 500 ? -2.558  13.702  45.295  1.00 16.95 ? 492  ASP B O   1 
ATOM   8486  C  CB  . ASP B 1 500 ? -5.911  12.990  46.240  1.00 20.22 ? 492  ASP B CB  1 
ATOM   8487  C  CG  . ASP B 1 500 ? -5.401  12.968  47.687  1.00 25.73 ? 492  ASP B CG  1 
ATOM   8488  O  OD1 . ASP B 1 500 ? -4.219  13.269  47.941  1.00 20.89 ? 492  ASP B OD1 1 
ATOM   8489  O  OD2 . ASP B 1 500 ? -6.209  12.653  48.585  1.00 26.13 ? 492  ASP B OD2 1 
ATOM   8490  N  N   . THR B 1 501 ? -4.266  15.184  45.241  1.00 17.04 ? 493  THR B N   1 
ATOM   8491  C  CA  . THR B 1 501 ? -3.373  16.334  45.171  1.00 30.06 ? 493  THR B CA  1 
ATOM   8492  C  C   . THR B 1 501 ? -2.530  16.473  46.431  1.00 21.32 ? 493  THR B C   1 
ATOM   8493  O  O   . THR B 1 501 ? -1.389  16.940  46.355  1.00 20.98 ? 493  THR B O   1 
ATOM   8494  C  CB  . THR B 1 501 ? -4.179  17.605  44.912  1.00 32.15 ? 493  THR B CB  1 
ATOM   8495  O  OG1 . THR B 1 501 ? -4.991  17.900  46.052  1.00 39.11 ? 493  THR B OG1 1 
ATOM   8496  C  CG2 . THR B 1 501 ? -5.089  17.385  43.730  1.00 32.67 ? 493  THR B CG2 1 
ATOM   8497  N  N   . ALA B 1 502 ? -3.064  16.067  47.585  1.00 17.28 ? 494  ALA B N   1 
ATOM   8498  C  CA  . ALA B 1 502 ? -2.287  16.112  48.821  1.00 19.84 ? 494  ALA B CA  1 
ATOM   8499  C  C   . ALA B 1 502 ? -1.125  15.129  48.772  1.00 19.08 ? 494  ALA B C   1 
ATOM   8500  O  O   . ALA B 1 502 ? 0.020   15.488  49.079  1.00 16.43 ? 494  ALA B O   1 
ATOM   8501  C  CB  . ALA B 1 502 ? -3.189  15.818  50.023  1.00 18.99 ? 494  ALA B CB  1 
ATOM   8502  N  N   . GLU B 1 503 ? -1.398  13.879  48.387  1.00 16.85 ? 495  GLU B N   1 
ATOM   8503  C  CA  . GLU B 1 503 ? -0.314  12.914  48.272  1.00 17.52 ? 495  GLU B CA  1 
ATOM   8504  C  C   . GLU B 1 503 ? 0.651   13.296  47.158  1.00 17.03 ? 495  GLU B C   1 
ATOM   8505  O  O   . GLU B 1 503 ? 1.844   12.995  47.255  1.00 13.78 ? 495  GLU B O   1 
ATOM   8506  C  CB  . GLU B 1 503 ? -0.866  11.503  48.043  1.00 13.38 ? 495  GLU B CB  1 
ATOM   8507  C  CG  . GLU B 1 503 ? -1.500  10.902  49.303  1.00 19.37 ? 495  GLU B CG  1 
ATOM   8508  C  CD  . GLU B 1 503 ? -1.809  9.416   49.174  1.00 18.99 ? 495  GLU B CD  1 
ATOM   8509  O  OE1 . GLU B 1 503 ? -1.584  8.843   48.084  1.00 14.27 ? 495  GLU B OE1 1 
ATOM   8510  O  OE2 . GLU B 1 503 ? -2.280  8.821   50.170  1.00 17.78 ? 495  GLU B OE2 1 
ATOM   8511  N  N   . SER B 1 504 ? 0.158   13.960  46.106  1.00 17.20 ? 496  SER B N   1 
ATOM   8512  C  CA  A SER B 1 504 ? 1.030   14.359  45.001  0.55 16.74 ? 496  SER B CA  1 
ATOM   8513  C  CA  B SER B 1 504 ? 1.038   14.350  45.005  0.45 16.61 ? 496  SER B CA  1 
ATOM   8514  C  C   . SER B 1 504 ? 2.027   15.425  45.438  1.00 14.42 ? 496  SER B C   1 
ATOM   8515  O  O   . SER B 1 504 ? 3.209   15.372  45.068  1.00 14.07 ? 496  SER B O   1 
ATOM   8516  C  CB  A SER B 1 504 ? 0.191   14.883  43.830  0.55 18.21 ? 496  SER B CB  1 
ATOM   8517  C  CB  B SER B 1 504 ? 0.216   14.848  43.814  0.45 18.33 ? 496  SER B CB  1 
ATOM   8518  O  OG  A SER B 1 504 ? -0.620  13.865  43.272  0.55 13.82 ? 496  SER B OG  1 
ATOM   8519  O  OG  B SER B 1 504 ? 1.063   15.420  42.826  0.45 17.37 ? 496  SER B OG  1 
ATOM   8520  N  N   . LEU B 1 505 ? 1.561   16.422  46.196  1.00 14.88 ? 497  LEU B N   1 
ATOM   8521  C  CA  . LEU B 1 505 ? 2.470   17.466  46.656  1.00 18.32 ? 497  LEU B CA  1 
ATOM   8522  C  C   . LEU B 1 505 ? 3.530   16.880  47.570  1.00 17.63 ? 497  LEU B C   1 
ATOM   8523  O  O   . LEU B 1 505 ? 4.714   17.213  47.456  1.00 18.03 ? 497  LEU B O   1 
ATOM   8524  C  CB  . LEU B 1 505 ? 1.696   18.566  47.380  1.00 19.01 ? 497  LEU B CB  1 
ATOM   8525  C  CG  . LEU B 1 505 ? 2.532   19.679  48.021  1.00 18.22 ? 497  LEU B CG  1 
ATOM   8526  C  CD1 . LEU B 1 505 ? 3.419   20.340  46.976  1.00 21.34 ? 497  LEU B CD1 1 
ATOM   8527  C  CD2 . LEU B 1 505 ? 1.617   20.710  48.677  1.00 19.03 ? 497  LEU B CD2 1 
ATOM   8528  N  N   . VAL B 1 506 ? 3.121   16.004  48.486  1.00 15.06 ? 498  VAL B N   1 
ATOM   8529  C  CA  . VAL B 1 506 ? 4.084   15.411  49.406  1.00 15.86 ? 498  VAL B CA  1 
ATOM   8530  C  C   . VAL B 1 506 ? 5.088   14.559  48.647  1.00 14.65 ? 498  VAL B C   1 
ATOM   8531  O  O   . VAL B 1 506 ? 6.296   14.615  48.915  1.00 15.00 ? 498  VAL B O   1 
ATOM   8532  C  CB  . VAL B 1 506 ? 3.366   14.600  50.497  1.00 15.47 ? 498  VAL B CB  1 
ATOM   8533  C  CG1 . VAL B 1 506 ? 4.390   13.866  51.362  1.00 18.85 ? 498  VAL B CG1 1 
ATOM   8534  C  CG2 . VAL B 1 506 ? 2.506   15.512  51.352  1.00 15.59 ? 498  VAL B CG2 1 
ATOM   8535  N  N   . ALA B 1 507 ? 4.609   13.774  47.673  1.00 12.53 ? 499  ALA B N   1 
ATOM   8536  C  CA  . ALA B 1 507 ? 5.512   12.962  46.863  1.00 13.12 ? 499  ALA B CA  1 
ATOM   8537  C  C   . ALA B 1 507 ? 6.524   13.831  46.135  1.00 12.33 ? 499  ALA B C   1 
ATOM   8538  O  O   . ALA B 1 507 ? 7.717   13.513  46.109  1.00 12.73 ? 499  ALA B O   1 
ATOM   8539  C  CB  . ALA B 1 507 ? 4.718   12.119  45.863  1.00 14.30 ? 499  ALA B CB  1 
ATOM   8540  N  N   . TRP B 1 508 ? 6.068   14.929  45.529  1.00 14.63 ? 500  TRP B N   1 
ATOM   8541  C  CA  . TRP B 1 508 ? 6.993   15.838  44.853  1.00 12.54 ? 500  TRP B CA  1 
ATOM   8542  C  C   . TRP B 1 508 ? 7.971   16.452  45.841  1.00 17.81 ? 500  TRP B C   1 
ATOM   8543  O  O   . TRP B 1 508 ? 9.178   16.538  45.573  1.00 17.19 ? 500  TRP B O   1 
ATOM   8544  C  CB  . TRP B 1 508 ? 6.224   16.941  44.132  1.00 15.05 ? 500  TRP B CB  1 
ATOM   8545  C  CG  . TRP B 1 508 ? 5.849   16.617  42.722  1.00 15.42 ? 500  TRP B CG  1 
ATOM   8546  C  CD1 . TRP B 1 508 ? 4.627   16.211  42.270  1.00 16.05 ? 500  TRP B CD1 1 
ATOM   8547  C  CD2 . TRP B 1 508 ? 6.702   16.685  41.568  1.00 15.65 ? 500  TRP B CD2 1 
ATOM   8548  N  NE1 . TRP B 1 508 ? 4.663   16.029  40.906  1.00 19.22 ? 500  TRP B NE1 1 
ATOM   8549  C  CE2 . TRP B 1 508 ? 5.925   16.311  40.451  1.00 16.61 ? 500  TRP B CE2 1 
ATOM   8550  C  CE3 . TRP B 1 508 ? 8.046   17.021  41.374  1.00 15.72 ? 500  TRP B CE3 1 
ATOM   8551  C  CZ2 . TRP B 1 508 ? 6.444   16.266  39.157  1.00 12.38 ? 500  TRP B CZ2 1 
ATOM   8552  C  CZ3 . TRP B 1 508 ? 8.563   16.978  40.091  1.00 16.63 ? 500  TRP B CZ3 1 
ATOM   8553  C  CH2 . TRP B 1 508 ? 7.765   16.599  38.999  1.00 17.04 ? 500  TRP B CH2 1 
ATOM   8554  N  N   . ALA B 1 509 ? 7.456   16.920  46.979  1.00 13.77 ? 501  ALA B N   1 
ATOM   8555  C  CA  . ALA B 1 509 ? 8.316   17.544  47.977  1.00 15.79 ? 501  ALA B CA  1 
ATOM   8556  C  C   . ALA B 1 509 ? 9.342   16.561  48.521  1.00 18.17 ? 501  ALA B C   1 
ATOM   8557  O  O   . ALA B 1 509 ? 10.515  16.912  48.706  1.00 16.33 ? 501  ALA B O   1 
ATOM   8558  C  CB  . ALA B 1 509 ? 7.471   18.104  49.115  1.00 15.41 ? 501  ALA B CB  1 
ATOM   8559  N  N   . GLU B 1 510 ? 8.914   15.332  48.813  1.00 16.00 ? 502  GLU B N   1 
ATOM   8560  C  CA  . GLU B 1 510 ? 9.857   14.332  49.306  1.00 13.08 ? 502  GLU B CA  1 
ATOM   8561  C  C   . GLU B 1 510 ? 10.892  13.978  48.244  1.00 12.15 ? 502  GLU B C   1 
ATOM   8562  O  O   . GLU B 1 510 ? 12.077  13.814  48.558  1.00 14.06 ? 502  GLU B O   1 
ATOM   8563  C  CB  . GLU B 1 510 ? 9.106   13.088  49.781  1.00 14.31 ? 502  GLU B CB  1 
ATOM   8564  C  CG  . GLU B 1 510 ? 8.365   13.303  51.099  1.00 17.39 ? 502  GLU B CG  1 
ATOM   8565  C  CD  . GLU B 1 510 ? 9.301   13.676  52.245  1.00 25.45 ? 502  GLU B CD  1 
ATOM   8566  O  OE1 . GLU B 1 510 ? 10.285  12.944  52.476  1.00 17.53 ? 502  GLU B OE1 1 
ATOM   8567  O  OE2 . GLU B 1 510 ? 9.057   14.702  52.914  1.00 22.47 ? 502  GLU B OE2 1 
ATOM   8568  N  N   . ALA B 1 511 ? 10.471  13.879  46.981  1.00 11.61 ? 503  ALA B N   1 
ATOM   8569  C  CA  . ALA B 1 511 ? 11.419  13.617  45.904  1.00 14.86 ? 503  ALA B CA  1 
ATOM   8570  C  C   . ALA B 1 511 ? 12.424  14.754  45.768  1.00 16.89 ? 503  ALA B C   1 
ATOM   8571  O  O   . ALA B 1 511 ? 13.612  14.515  45.513  1.00 16.61 ? 503  ALA B O   1 
ATOM   8572  C  CB  . ALA B 1 511 ? 10.666  13.398  44.584  1.00 14.49 ? 503  ALA B CB  1 
ATOM   8573  N  N   . ALA B 1 512 ? 11.961  16.003  45.921  1.00 13.62 ? 504  ALA B N   1 
ATOM   8574  C  CA  . ALA B 1 512 ? 12.860  17.154  45.835  1.00 18.81 ? 504  ALA B CA  1 
ATOM   8575  C  C   . ALA B 1 512 ? 13.832  17.177  47.004  1.00 18.85 ? 504  ALA B C   1 
ATOM   8576  O  O   . ALA B 1 512 ? 15.007  17.532  46.838  1.00 19.56 ? 504  ALA B O   1 
ATOM   8577  C  CB  . ALA B 1 512 ? 12.058  18.462  45.807  1.00 16.40 ? 504  ALA B CB  1 
ATOM   8578  N  N   . LYS B 1 513 ? 13.342  16.818  48.195  1.00 16.85 ? 505  LYS B N   1 
ATOM   8579  C  CA  . LYS B 1 513 ? 14.148  16.848  49.415  1.00 17.46 ? 505  LYS B CA  1 
ATOM   8580  C  C   . LYS B 1 513 ? 15.243  15.793  49.413  1.00 18.98 ? 505  LYS B C   1 
ATOM   8581  O  O   . LYS B 1 513 ? 16.284  15.989  50.050  1.00 22.46 ? 505  LYS B O   1 
ATOM   8582  C  CB  . LYS B 1 513 ? 13.266  16.606  50.642  1.00 17.02 ? 505  LYS B CB  1 
ATOM   8583  C  CG  . LYS B 1 513 ? 12.367  17.753  51.046  1.00 32.46 ? 505  LYS B CG  1 
ATOM   8584  C  CD  . LYS B 1 513 ? 11.719  17.490  52.408  1.00 29.97 ? 505  LYS B CD  1 
ATOM   8585  C  CE  . LYS B 1 513 ? 12.781  17.342  53.499  1.00 33.34 ? 505  LYS B CE  1 
ATOM   8586  N  NZ  . LYS B 1 513 ? 12.250  17.540  54.883  1.00 40.50 ? 505  LYS B NZ  1 
ATOM   8587  N  N   . ALA B 1 514 ? 14.992  14.647  48.786  1.00 15.74 ? 506  ALA B N   1 
ATOM   8588  C  CA  . ALA B 1 514 ? 15.927  13.529  48.842  1.00 19.50 ? 506  ALA B CA  1 
ATOM   8589  C  C   . ALA B 1 514 ? 17.266  13.929  48.235  1.00 19.77 ? 506  ALA B C   1 
ATOM   8590  O  O   . ALA B 1 514 ? 17.321  14.379  47.091  1.00 27.43 ? 506  ALA B O   1 
ATOM   8591  C  CB  . ALA B 1 514 ? 15.347  12.326  48.101  1.00 13.65 ? 506  ALA B CB  1 
ATOM   8592  N  N   . GLU B 1 515 ? 18.345  13.776  49.002  1.00 20.02 ? 507  GLU B N   1 
ATOM   8593  C  CA  . GLU B 1 515 ? 19.645  14.220  48.513  1.00 27.32 ? 507  GLU B CA  1 
ATOM   8594  C  C   . GLU B 1 515 ? 20.404  13.133  47.771  1.00 22.37 ? 507  GLU B C   1 
ATOM   8595  O  O   . GLU B 1 515 ? 21.247  13.447  46.921  1.00 22.23 ? 507  GLU B O   1 
ATOM   8596  C  CB  . GLU B 1 515 ? 20.522  14.716  49.666  1.00 33.36 ? 507  GLU B CB  1 
ATOM   8597  C  CG  . GLU B 1 515 ? 19.771  15.157  50.900  1.00 49.07 ? 507  GLU B CG  1 
ATOM   8598  C  CD  . GLU B 1 515 ? 20.647  15.958  51.843  1.00 58.93 ? 507  GLU B CD  1 
ATOM   8599  O  OE1 . GLU B 1 515 ? 20.520  17.200  51.854  1.00 61.95 ? 507  GLU B OE1 1 
ATOM   8600  O  OE2 . GLU B 1 515 ? 21.473  15.350  52.559  1.00 62.97 ? 507  GLU B OE2 1 
ATOM   8601  N  N   . ASP B 1 516 ? 20.126  11.863  48.067  1.00 17.52 ? 508  ASP B N   1 
ATOM   8602  C  CA  . ASP B 1 516 ? 21.016  10.786  47.649  1.00 17.33 ? 508  ASP B CA  1 
ATOM   8603  C  C   . ASP B 1 516 ? 20.281  9.639   46.965  1.00 13.55 ? 508  ASP B C   1 
ATOM   8604  O  O   . ASP B 1 516 ? 20.799  8.521   46.931  1.00 15.29 ? 508  ASP B O   1 
ATOM   8605  C  CB  . ASP B 1 516 ? 21.807  10.261  48.853  1.00 19.36 ? 508  ASP B CB  1 
ATOM   8606  C  CG  . ASP B 1 516 ? 20.934  9.499   49.828  1.00 25.78 ? 508  ASP B CG  1 
ATOM   8607  O  OD1 . ASP B 1 516 ? 19.703  9.697   49.813  1.00 26.03 ? 508  ASP B OD1 1 
ATOM   8608  O  OD2 . ASP B 1 516 ? 21.479  8.695   50.605  1.00 32.94 ? 508  ASP B OD2 1 
ATOM   8609  N  N   . HIS B 1 517 ? 19.084  9.867   46.435  1.00 14.28 ? 509  HIS B N   1 
ATOM   8610  C  CA  . HIS B 1 517 ? 18.433  8.819   45.660  1.00 15.92 ? 509  HIS B CA  1 
ATOM   8611  C  C   . HIS B 1 517 ? 17.402  9.452   44.757  1.00 13.21 ? 509  HIS B C   1 
ATOM   8612  O  O   . HIS B 1 517 ? 16.851  10.509  45.084  1.00 10.32 ? 509  HIS B O   1 
ATOM   8613  C  CB  . HIS B 1 517 ? 17.765  7.765   46.556  1.00 10.28 ? 509  HIS B CB  1 
ATOM   8614  C  CG  . HIS B 1 517 ? 16.712  8.320   47.462  1.00 12.73 ? 509  HIS B CG  1 
ATOM   8615  N  ND1 . HIS B 1 517 ? 16.992  8.766   48.734  1.00 14.58 ? 509  HIS B ND1 1 
ATOM   8616  C  CD2 . HIS B 1 517 ? 15.376  8.483   47.288  1.00 12.45 ? 509  HIS B CD2 1 
ATOM   8617  C  CE1 . HIS B 1 517 ? 15.877  9.191   49.304  1.00 17.09 ? 509  HIS B CE1 1 
ATOM   8618  N  NE2 . HIS B 1 517 ? 14.881  9.020   48.452  1.00 14.17 ? 509  HIS B NE2 1 
ATOM   8619  N  N   . PRO B 1 518 ? 17.077  8.801   43.649  1.00 12.45 ? 510  PRO B N   1 
ATOM   8620  C  CA  . PRO B 1 518 ? 16.045  9.302   42.743  1.00 10.01 ? 510  PRO B CA  1 
ATOM   8621  C  C   . PRO B 1 518 ? 14.659  8.828   43.170  1.00 12.27 ? 510  PRO B C   1 
ATOM   8622  O  O   . PRO B 1 518 ? 14.496  7.993   44.061  1.00 13.96 ? 510  PRO B O   1 
ATOM   8623  C  CB  . PRO B 1 518 ? 16.441  8.662   41.403  1.00 8.67  ? 510  PRO B CB  1 
ATOM   8624  C  CG  . PRO B 1 518 ? 16.991  7.325   41.821  1.00 8.55  ? 510  PRO B CG  1 
ATOM   8625  C  CD  . PRO B 1 518 ? 17.810  7.659   43.072  1.00 9.13  ? 510  PRO B CD  1 
ATOM   8626  N  N   . SER B 1 519 ? 13.651  9.359   42.485  1.00 9.99  ? 511  SER B N   1 
ATOM   8627  C  CA  . SER B 1 519 ? 12.285  8.937   42.736  1.00 11.26 ? 511  SER B CA  1 
ATOM   8628  C  C   . SER B 1 519 ? 11.574  8.756   41.405  1.00 10.11 ? 511  SER B C   1 
ATOM   8629  O  O   . SER B 1 519 ? 11.894  9.427   40.415  1.00 9.72  ? 511  SER B O   1 
ATOM   8630  C  CB  . SER B 1 519 ? 11.523  9.956   43.607  1.00 16.77 ? 511  SER B CB  1 
ATOM   8631  O  OG  . SER B 1 519 ? 12.235  10.260  44.798  1.00 18.32 ? 511  SER B OG  1 
ATOM   8632  N  N   . CYS B 1 520 ? 10.600  7.850   41.396  1.00 7.88  ? 512  CYS B N   1 
ATOM   8633  C  CA  . CYS B 1 520 ? 9.649   7.724   40.301  1.00 11.86 ? 512  CYS B CA  1 
ATOM   8634  C  C   . CYS B 1 520 ? 8.291   8.187   40.812  1.00 15.08 ? 512  CYS B C   1 
ATOM   8635  O  O   . CYS B 1 520 ? 7.780   7.638   41.792  1.00 12.68 ? 512  CYS B O   1 
ATOM   8636  C  CB  . CYS B 1 520 ? 9.549   6.283   39.802  1.00 12.87 ? 512  CYS B CB  1 
ATOM   8637  S  SG  . CYS B 1 520 ? 10.998  5.586   39.001  1.00 14.86 ? 512  CYS B SG  1 
ATOM   8638  N  N   . LEU B 1 521 ? 7.710   9.183   40.150  1.00 8.51  ? 513  LEU B N   1 
ATOM   8639  C  CA  . LEU B 1 521 ? 6.401   9.721   40.509  1.00 8.98  ? 513  LEU B CA  1 
ATOM   8640  C  C   . LEU B 1 521 ? 5.416   9.302   39.427  1.00 9.39  ? 513  LEU B C   1 
ATOM   8641  O  O   . LEU B 1 521 ? 5.566   9.696   38.266  1.00 12.87 ? 513  LEU B O   1 
ATOM   8642  C  CB  . LEU B 1 521 ? 6.448   11.242  40.645  1.00 13.46 ? 513  LEU B CB  1 
ATOM   8643  C  CG  . LEU B 1 521 ? 7.558   11.812  41.540  1.00 13.00 ? 513  LEU B CG  1 
ATOM   8644  C  CD1 . LEU B 1 521 ? 7.449   13.341  41.639  1.00 13.52 ? 513  LEU B CD1 1 
ATOM   8645  C  CD2 . LEU B 1 521 ? 7.515   11.201  42.940  1.00 12.95 ? 513  LEU B CD2 1 
ATOM   8646  N  N   . ILE B 1 522 ? 4.421   8.508   39.812  1.00 11.58 ? 514  ILE B N   1 
ATOM   8647  C  CA  . ILE B 1 522 ? 3.549   7.794   38.886  1.00 11.82 ? 514  ILE B CA  1 
ATOM   8648  C  C   . ILE B 1 522 ? 2.153   8.366   39.040  1.00 10.64 ? 514  ILE B C   1 
ATOM   8649  O  O   . ILE B 1 522 ? 1.591   8.332   40.144  1.00 14.02 ? 514  ILE B O   1 
ATOM   8650  C  CB  . ILE B 1 522 ? 3.564   6.285   39.168  1.00 13.49 ? 514  ILE B CB  1 
ATOM   8651  C  CG1 . ILE B 1 522 ? 4.953   5.712   38.883  1.00 11.74 ? 514  ILE B CG1 1 
ATOM   8652  C  CG2 . ILE B 1 522 ? 2.556   5.561   38.299  1.00 9.61  ? 514  ILE B CG2 1 
ATOM   8653  C  CD1 . ILE B 1 522 ? 5.091   4.256   39.283  1.00 12.33 ? 514  ILE B CD1 1 
ATOM   8654  N  N   . PHE B 1 523 ? 1.592   8.889   37.946  1.00 10.51 ? 515  PHE B N   1 
ATOM   8655  C  CA  . PHE B 1 523 ? 0.311   9.591   38.004  1.00 15.28 ? 515  PHE B CA  1 
ATOM   8656  C  C   . PHE B 1 523 ? -0.704  8.999   37.037  1.00 17.76 ? 515  PHE B C   1 
ATOM   8657  O  O   . PHE B 1 523 ? -0.359  8.415   36.008  1.00 18.65 ? 515  PHE B O   1 
ATOM   8658  C  CB  . PHE B 1 523 ? 0.480   11.086  37.692  1.00 16.82 ? 515  PHE B CB  1 
ATOM   8659  C  CG  . PHE B 1 523 ? 1.365   11.792  38.659  1.00 17.49 ? 515  PHE B CG  1 
ATOM   8660  C  CD1 . PHE B 1 523 ? 0.864   12.242  39.874  1.00 18.05 ? 515  PHE B CD1 1 
ATOM   8661  C  CD2 . PHE B 1 523 ? 2.703   11.981  38.376  1.00 14.32 ? 515  PHE B CD2 1 
ATOM   8662  C  CE1 . PHE B 1 523 ? 1.687   12.879  40.781  1.00 19.13 ? 515  PHE B CE1 1 
ATOM   8663  C  CE2 . PHE B 1 523 ? 3.536   12.624  39.278  1.00 14.79 ? 515  PHE B CE2 1 
ATOM   8664  C  CZ  . PHE B 1 523 ? 3.031   13.065  40.483  1.00 19.81 ? 515  PHE B CZ  1 
ATOM   8665  N  N   . SER B 1 524 ? -1.975  9.190   37.373  1.00 19.57 ? 516  SER B N   1 
ATOM   8666  C  CA  . SER B 1 524 ? -3.068  9.015   36.431  1.00 25.00 ? 516  SER B CA  1 
ATOM   8667  C  C   . SER B 1 524 ? -3.784  10.356  36.275  1.00 27.93 ? 516  SER B C   1 
ATOM   8668  O  O   . SER B 1 524 ? -3.439  11.341  36.928  1.00 31.74 ? 516  SER B O   1 
ATOM   8669  C  CB  . SER B 1 524 ? -4.028  7.929   36.914  1.00 30.21 ? 516  SER B CB  1 
ATOM   8670  O  OG  . SER B 1 524 ? -4.846  8.436   37.943  1.00 36.55 ? 516  SER B OG  1 
ATOM   8671  N  N   . ARG B 1 525 ? -4.812  10.381  35.427  1.00 32.60 ? 517  ARG B N   1 
ATOM   8672  C  CA  . ARG B 1 525 ? -5.641  11.571  35.248  1.00 30.93 ? 517  ARG B CA  1 
ATOM   8673  C  C   . ARG B 1 525 ? -6.669  11.773  36.360  1.00 36.21 ? 517  ARG B C   1 
ATOM   8674  O  O   . ARG B 1 525 ? -7.383  12.781  36.339  1.00 35.63 ? 517  ARG B O   1 
ATOM   8675  C  CB  . ARG B 1 525 ? -6.366  11.508  33.898  1.00 29.17 ? 517  ARG B CB  1 
ATOM   8676  N  N   . GLN B 1 526 ? -6.769  10.859  37.319  1.00 38.11 ? 518  GLN B N   1 
ATOM   8677  C  CA  . GLN B 1 526 ? -7.806  10.926  38.337  1.00 50.04 ? 518  GLN B CA  1 
ATOM   8678  C  C   . GLN B 1 526 ? -7.302  11.642  39.589  1.00 58.09 ? 518  GLN B C   1 
ATOM   8679  O  O   . GLN B 1 526 ? -6.098  11.750  39.834  1.00 65.69 ? 518  GLN B O   1 
ATOM   8680  C  CB  . GLN B 1 526 ? -8.293  9.520   38.696  1.00 50.14 ? 518  GLN B CB  1 
ATOM   8681  N  N   . ASN B 1 527 ? -8.249  12.135  40.386  1.00 54.98 ? 519  ASN B N   1 
ATOM   8682  C  CA  . ASN B 1 527 ? -7.930  12.781  41.658  1.00 54.65 ? 519  ASN B CA  1 
ATOM   8683  C  C   . ASN B 1 527 ? -9.142  12.806  42.584  1.00 48.17 ? 519  ASN B C   1 
ATOM   8684  O  O   . ASN B 1 527 ? -10.052 11.988  42.458  1.00 45.80 ? 519  ASN B O   1 
ATOM   8685  C  CB  . ASN B 1 527 ? -7.416  14.207  41.432  1.00 59.03 ? 519  ASN B CB  1 
ATOM   8686  N  N   . PHE B 1 530 ? -10.320 12.792  46.253  1.00 60.10 ? 522  PHE B N   1 
ATOM   8687  C  CA  . PHE B 1 530 ? -10.157 13.725  47.368  1.00 64.50 ? 522  PHE B CA  1 
ATOM   8688  C  C   . PHE B 1 530 ? -10.904 13.275  48.626  1.00 65.25 ? 522  PHE B C   1 
ATOM   8689  O  O   . PHE B 1 530 ? -12.090 13.552  48.787  1.00 65.06 ? 522  PHE B O   1 
ATOM   8690  C  CB  . PHE B 1 530 ? -10.629 15.124  46.962  1.00 67.42 ? 522  PHE B CB  1 
ATOM   8691  N  N   . GLN B 1 531 ? -10.197 12.587  49.518  1.00 67.70 ? 523  GLN B N   1 
ATOM   8692  C  CA  . GLN B 1 531 ? -10.734 12.175  50.806  1.00 66.77 ? 523  GLN B CA  1 
ATOM   8693  C  C   . GLN B 1 531 ? -10.183 13.071  51.911  1.00 62.08 ? 523  GLN B C   1 
ATOM   8694  O  O   . GLN B 1 531 ? -9.056  13.569  51.828  1.00 62.96 ? 523  GLN B O   1 
ATOM   8695  C  CB  . GLN B 1 531 ? -10.393 10.710  51.096  1.00 66.22 ? 523  GLN B CB  1 
ATOM   8696  N  N   . ALA B 1 532 ? -10.988 13.271  52.952  1.00 55.38 ? 524  ALA B N   1 
ATOM   8697  C  CA  . ALA B 1 532 ? -10.601 14.169  54.031  1.00 48.37 ? 524  ALA B CA  1 
ATOM   8698  C  C   . ALA B 1 532 ? -9.466  13.576  54.862  1.00 46.53 ? 524  ALA B C   1 
ATOM   8699  O  O   . ALA B 1 532 ? -9.305  12.354  54.962  1.00 40.62 ? 524  ALA B O   1 
ATOM   8700  C  CB  . ALA B 1 532 ? -11.797 14.476  54.925  1.00 49.80 ? 524  ALA B CB  1 
ATOM   8701  N  N   . ARG B 1 533 ? -8.669  14.463  55.461  1.00 43.52 ? 525  ARG B N   1 
ATOM   8702  C  CA  . ARG B 1 533 ? -7.524  14.057  56.263  1.00 35.89 ? 525  ARG B CA  1 
ATOM   8703  C  C   . ARG B 1 533 ? -7.373  14.964  57.473  1.00 32.15 ? 525  ARG B C   1 
ATOM   8704  O  O   . ARG B 1 533 ? -7.549  16.182  57.375  1.00 29.75 ? 525  ARG B O   1 
ATOM   8705  C  CB  . ARG B 1 533 ? -6.220  14.093  55.460  1.00 32.17 ? 525  ARG B CB  1 
ATOM   8706  C  CG  . ARG B 1 533 ? -6.017  12.918  54.524  1.00 29.86 ? 525  ARG B CG  1 
ATOM   8707  C  CD  . ARG B 1 533 ? -4.662  13.033  53.836  1.00 21.34 ? 525  ARG B CD  1 
ATOM   8708  N  NE  . ARG B 1 533 ? -4.554  12.139  52.693  1.00 24.55 ? 525  ARG B NE  1 
ATOM   8709  C  CZ  . ARG B 1 533 ? -5.038  12.405  51.483  1.00 23.33 ? 525  ARG B CZ  1 
ATOM   8710  N  NH1 . ARG B 1 533 ? -5.673  13.547  51.248  1.00 26.09 ? 525  ARG B NH1 1 
ATOM   8711  N  NH2 . ARG B 1 533 ? -4.876  11.529  50.502  1.00 26.77 ? 525  ARG B NH2 1 
ATOM   8712  N  N   . SER B 1 534 ? -7.035  14.359  58.608  1.00 30.21 ? 526  SER B N   1 
ATOM   8713  C  CA  . SER B 1 534 ? -6.618  15.119  59.772  1.00 30.68 ? 526  SER B CA  1 
ATOM   8714  C  C   . SER B 1 534 ? -5.220  15.689  59.550  1.00 28.76 ? 526  SER B C   1 
ATOM   8715  O  O   . SER B 1 534 ? -4.508  15.315  58.614  1.00 26.83 ? 526  SER B O   1 
ATOM   8716  C  CB  . SER B 1 534 ? -6.620  14.234  61.012  1.00 35.32 ? 526  SER B CB  1 
ATOM   8717  O  OG  . SER B 1 534 ? -5.655  13.206  60.867  1.00 26.71 ? 526  SER B OG  1 
ATOM   8718  N  N   . GLU B 1 535 ? -4.816  16.601  60.436  1.00 25.90 ? 527  GLU B N   1 
ATOM   8719  C  CA  . GLU B 1 535 ? -3.451  17.105  60.368  1.00 27.76 ? 527  GLU B CA  1 
ATOM   8720  C  C   . GLU B 1 535 ? -2.446  15.968  60.488  1.00 24.10 ? 527  GLU B C   1 
ATOM   8721  O  O   . GLU B 1 535 ? -1.403  15.983  59.829  1.00 22.33 ? 527  GLU B O   1 
ATOM   8722  C  CB  . GLU B 1 535 ? -3.201  18.145  61.462  1.00 31.40 ? 527  GLU B CB  1 
ATOM   8723  C  CG  . GLU B 1 535 ? -1.770  18.672  61.458  1.00 43.67 ? 527  GLU B CG  1 
ATOM   8724  C  CD  . GLU B 1 535 ? -1.451  19.551  62.652  1.00 57.26 ? 527  GLU B CD  1 
ATOM   8725  O  OE1 . GLU B 1 535 ? -0.946  20.674  62.441  1.00 60.72 ? 527  GLU B OE1 1 
ATOM   8726  O  OE2 . GLU B 1 535 ? -1.699  19.117  63.799  1.00 60.53 ? 527  GLU B OE2 1 
ATOM   8727  N  N   . GLN B 1 536 ? -2.748  14.973  61.326  1.00 26.64 ? 528  GLN B N   1 
ATOM   8728  C  CA  . GLN B 1 536 ? -1.814  13.875  61.542  1.00 25.55 ? 528  GLN B CA  1 
ATOM   8729  C  C   . GLN B 1 536 ? -1.696  13.000  60.303  1.00 24.32 ? 528  GLN B C   1 
ATOM   8730  O  O   . GLN B 1 536 ? -0.590  12.591  59.928  1.00 19.86 ? 528  GLN B O   1 
ATOM   8731  C  CB  . GLN B 1 536 ? -2.250  13.037  62.744  1.00 28.73 ? 528  GLN B CB  1 
ATOM   8732  C  CG  . GLN B 1 536 ? -1.307  11.888  63.046  1.00 24.53 ? 528  GLN B CG  1 
ATOM   8733  C  CD  . GLN B 1 536 ? 0.049   12.384  63.504  1.00 27.78 ? 528  GLN B CD  1 
ATOM   8734  O  OE1 . GLN B 1 536 ? 0.137   13.233  64.397  1.00 26.33 ? 528  GLN B OE1 1 
ATOM   8735  N  NE2 . GLN B 1 536 ? 1.112   11.877  62.885  1.00 29.04 ? 528  GLN B NE2 1 
ATOM   8736  N  N   . GLN B 1 537 ? -2.825  12.689  59.658  1.00 20.58 ? 529  GLN B N   1 
ATOM   8737  C  CA  . GLN B 1 537 ? -2.758  11.925  58.420  1.00 19.25 ? 529  GLN B CA  1 
ATOM   8738  C  C   . GLN B 1 537 ? -1.961  12.678  57.367  1.00 20.77 ? 529  GLN B C   1 
ATOM   8739  O  O   . GLN B 1 537 ? -1.112  12.089  56.688  1.00 21.82 ? 529  GLN B O   1 
ATOM   8740  C  CB  . GLN B 1 537 ? -4.164  11.604  57.910  1.00 19.73 ? 529  GLN B CB  1 
ATOM   8741  C  CG  . GLN B 1 537 ? -4.859  10.496  58.677  1.00 19.66 ? 529  GLN B CG  1 
ATOM   8742  C  CD  . GLN B 1 537 ? -6.346  10.429  58.372  1.00 32.09 ? 529  GLN B CD  1 
ATOM   8743  O  OE1 . GLN B 1 537 ? -7.034  11.448  58.354  1.00 33.70 ? 529  GLN B OE1 1 
ATOM   8744  N  NE2 . GLN B 1 537 ? -6.844  9.227   58.123  1.00 32.44 ? 529  GLN B NE2 1 
ATOM   8745  N  N   . LEU B 1 538 ? -2.208  13.988  57.231  1.00 22.56 ? 530  LEU B N   1 
ATOM   8746  C  CA  . LEU B 1 538 ? -1.413  14.797  56.309  1.00 25.37 ? 530  LEU B CA  1 
ATOM   8747  C  C   . LEU B 1 538 ? 0.077   14.637  56.572  1.00 22.27 ? 530  LEU B C   1 
ATOM   8748  O  O   . LEU B 1 538 ? 0.870   14.473  55.638  1.00 23.14 ? 530  LEU B O   1 
ATOM   8749  C  CB  . LEU B 1 538 ? -1.797  16.267  56.439  1.00 29.34 ? 530  LEU B CB  1 
ATOM   8750  C  CG  . LEU B 1 538 ? -3.025  16.710  55.666  1.00 28.22 ? 530  LEU B CG  1 
ATOM   8751  C  CD1 . LEU B 1 538 ? -3.272  18.191  55.896  1.00 30.36 ? 530  LEU B CD1 1 
ATOM   8752  C  CD2 . LEU B 1 538 ? -2.782  16.393  54.202  1.00 21.93 ? 530  LEU B CD2 1 
ATOM   8753  N  N   . ASN B 1 539 ? 0.469   14.677  57.846  1.00 24.86 ? 531  ASN B N   1 
ATOM   8754  C  CA  . ASN B 1 539 ? 1.877   14.632  58.219  1.00 22.85 ? 531  ASN B CA  1 
ATOM   8755  C  C   . ASN B 1 539 ? 2.494   13.255  58.027  1.00 22.69 ? 531  ASN B C   1 
ATOM   8756  O  O   . ASN B 1 539 ? 3.721   13.159  57.886  1.00 22.15 ? 531  ASN B O   1 
ATOM   8757  C  CB  . ASN B 1 539 ? 2.036   15.087  59.674  1.00 28.53 ? 531  ASN B CB  1 
ATOM   8758  C  CG  . ASN B 1 539 ? 1.707   16.563  59.865  1.00 35.93 ? 531  ASN B CG  1 
ATOM   8759  O  OD1 . ASN B 1 539 ? 1.974   17.389  58.991  1.00 34.76 ? 531  ASN B OD1 1 
ATOM   8760  N  ND2 . ASN B 1 539 ? 1.131   16.900  61.014  1.00 39.16 ? 531  ASN B ND2 1 
ATOM   8761  N  N   . ASP B 1 540 ? 1.682   12.194  58.004  1.00 20.92 ? 532  ASP B N   1 
ATOM   8762  C  CA  . ASP B 1 540 ? 2.184   10.838  57.815  1.00 19.01 ? 532  ASP B CA  1 
ATOM   8763  C  C   . ASP B 1 540 ? 2.262   10.395  56.357  1.00 16.92 ? 532  ASP B C   1 
ATOM   8764  O  O   . ASP B 1 540 ? 2.775   9.303   56.103  1.00 18.58 ? 532  ASP B O   1 
ATOM   8765  C  CB  . ASP B 1 540 ? 1.321   9.828   58.574  1.00 16.89 ? 532  ASP B CB  1 
ATOM   8766  C  CG  . ASP B 1 540 ? 1.531   9.902   60.073  1.00 25.25 ? 532  ASP B CG  1 
ATOM   8767  O  OD1 . ASP B 1 540 ? 2.634   10.320  60.476  1.00 20.99 ? 532  ASP B OD1 1 
ATOM   8768  O  OD2 . ASP B 1 540 ? 0.599   9.558   60.839  1.00 21.66 ? 532  ASP B OD2 1 
ATOM   8769  N  N   . ILE B 1 541 ? 1.756   11.182  55.400  1.00 15.35 ? 533  ILE B N   1 
ATOM   8770  C  CA  . ILE B 1 541 ? 1.896   10.792  53.993  1.00 14.33 ? 533  ILE B CA  1 
ATOM   8771  C  C   . ILE B 1 541 ? 3.366   10.564  53.657  1.00 13.67 ? 533  ILE B C   1 
ATOM   8772  O  O   . ILE B 1 541 ? 3.716   9.636   52.914  1.00 13.26 ? 533  ILE B O   1 
ATOM   8773  C  CB  . ILE B 1 541 ? 1.278   11.847  53.054  1.00 14.56 ? 533  ILE B CB  1 
ATOM   8774  C  CG1 . ILE B 1 541 ? -0.218  12.024  53.329  1.00 15.33 ? 533  ILE B CG1 1 
ATOM   8775  C  CG2 . ILE B 1 541 ? 1.524   11.451  51.582  1.00 16.64 ? 533  ILE B CG2 1 
ATOM   8776  C  CD1 . ILE B 1 541 ? -0.844  13.226  52.610  1.00 16.53 ? 533  ILE B CD1 1 
ATOM   8777  N  N   . LYS B 1 542 ? 4.248   11.406  54.203  1.00 15.49 ? 534  LYS B N   1 
ATOM   8778  C  CA  A LYS B 1 542 ? 5.673   11.295  53.909  0.44 18.57 ? 534  LYS B CA  1 
ATOM   8779  C  CA  B LYS B 1 542 ? 5.670   11.291  53.901  0.56 18.90 ? 534  LYS B CA  1 
ATOM   8780  C  C   . LYS B 1 542 ? 6.288   10.009  54.444  1.00 19.25 ? 534  LYS B C   1 
ATOM   8781  O  O   . LYS B 1 542 ? 7.445   9.711   54.111  1.00 16.11 ? 534  LYS B O   1 
ATOM   8782  C  CB  A LYS B 1 542 ? 6.427   12.500  54.479  0.44 16.36 ? 534  LYS B CB  1 
ATOM   8783  C  CB  B LYS B 1 542 ? 6.429   12.507  54.446  0.56 15.81 ? 534  LYS B CB  1 
ATOM   8784  C  CG  A LYS B 1 542 ? 6.412   12.576  55.998  0.44 19.69 ? 534  LYS B CG  1 
ATOM   8785  C  CG  B LYS B 1 542 ? 6.517   12.576  55.967  0.56 20.07 ? 534  LYS B CG  1 
ATOM   8786  C  CD  A LYS B 1 542 ? 7.289   13.706  56.503  0.44 20.15 ? 534  LYS B CD  1 
ATOM   8787  C  CD  B LYS B 1 542 ? 7.375   13.752  56.407  0.56 20.08 ? 534  LYS B CD  1 
ATOM   8788  C  CE  A LYS B 1 542 ? 7.207   13.810  58.012  0.44 19.80 ? 534  LYS B CE  1 
ATOM   8789  C  CE  B LYS B 1 542 ? 6.692   15.084  56.112  0.56 20.11 ? 534  LYS B CE  1 
ATOM   8790  N  NZ  A LYS B 1 542 ? 7.935   14.993  58.542  0.44 30.94 ? 534  LYS B NZ  1 
ATOM   8791  N  NZ  B LYS B 1 542 ? 5.575   15.369  57.073  0.56 19.53 ? 534  LYS B NZ  1 
ATOM   8792  N  N   . ARG B 1 543 ? 5.561   9.250   55.263  1.00 15.13 ? 535  ARG B N   1 
ATOM   8793  C  CA  . ARG B 1 543 ? 6.051   7.974   55.774  1.00 15.33 ? 535  ARG B CA  1 
ATOM   8794  C  C   . ARG B 1 543 ? 5.669   6.796   54.875  1.00 16.31 ? 535  ARG B C   1 
ATOM   8795  O  O   . ARG B 1 543 ? 5.927   5.638   55.232  1.00 13.08 ? 535  ARG B O   1 
ATOM   8796  C  CB  . ARG B 1 543 ? 5.548   7.764   57.208  1.00 14.46 ? 535  ARG B CB  1 
ATOM   8797  C  CG  . ARG B 1 543 ? 5.951   8.908   58.155  1.00 15.53 ? 535  ARG B CG  1 
ATOM   8798  C  CD  . ARG B 1 543 ? 5.738   8.533   59.629  1.00 23.61 ? 535  ARG B CD  1 
ATOM   8799  N  NE  . ARG B 1 543 ? 6.792   7.633   60.092  1.00 22.30 ? 535  ARG B NE  1 
ATOM   8800  C  CZ  . ARG B 1 543 ? 6.992   7.279   61.358  1.00 23.10 ? 535  ARG B CZ  1 
ATOM   8801  N  NH1 . ARG B 1 543 ? 6.204   7.741   62.323  1.00 20.26 ? 535  ARG B NH1 1 
ATOM   8802  N  NH2 . ARG B 1 543 ? 7.992   6.461   61.661  1.00 21.97 ? 535  ARG B NH2 1 
ATOM   8803  N  N   . GLY B 1 544 ? 5.076   7.069   53.709  1.00 12.58 ? 536  GLY B N   1 
ATOM   8804  C  CA  . GLY B 1 544 ? 4.920   6.084   52.674  1.00 11.31 ? 536  GLY B CA  1 
ATOM   8805  C  C   . GLY B 1 544 ? 3.639   5.287   52.768  1.00 16.18 ? 536  GLY B C   1 
ATOM   8806  O  O   . GLY B 1 544 ? 3.108   4.860   51.743  1.00 11.70 ? 536  GLY B O   1 
ATOM   8807  N  N   . ALA B 1 545 ? 3.136   5.065   53.976  1.00 13.99 ? 537  ALA B N   1 
ATOM   8808  C  CA  . ALA B 1 545 ? 1.809   4.489   54.112  1.00 14.26 ? 537  ALA B CA  1 
ATOM   8809  C  C   . ALA B 1 545 ? 1.230   4.971   55.430  1.00 15.78 ? 537  ALA B C   1 
ATOM   8810  O  O   . ALA B 1 545 ? 1.971   5.267   56.371  1.00 17.25 ? 537  ALA B O   1 
ATOM   8811  C  CB  . ALA B 1 545 ? 1.847   2.956   54.039  1.00 13.68 ? 537  ALA B CB  1 
ATOM   8812  N  N   . TYR B 1 546 ? -0.095  5.084   55.477  1.00 16.87 ? 538  TYR B N   1 
ATOM   8813  C  CA  . TYR B 1 546 ? -0.779  5.594   56.658  1.00 17.36 ? 538  TYR B CA  1 
ATOM   8814  C  C   . TYR B 1 546 ? -2.240  5.180   56.570  1.00 20.51 ? 538  TYR B C   1 
ATOM   8815  O  O   . TYR B 1 546 ? -2.730  4.765   55.516  1.00 18.00 ? 538  TYR B O   1 
ATOM   8816  C  CB  . TYR B 1 546 ? -0.653  7.122   56.770  1.00 16.16 ? 538  TYR B CB  1 
ATOM   8817  C  CG  . TYR B 1 546 ? -1.313  7.835   55.617  1.00 15.04 ? 538  TYR B CG  1 
ATOM   8818  C  CD1 . TYR B 1 546 ? -0.708  7.874   54.365  1.00 14.56 ? 538  TYR B CD1 1 
ATOM   8819  C  CD2 . TYR B 1 546 ? -2.560  8.433   55.768  1.00 15.87 ? 538  TYR B CD2 1 
ATOM   8820  C  CE1 . TYR B 1 546 ? -1.318  8.510   53.299  1.00 19.74 ? 538  TYR B CE1 1 
ATOM   8821  C  CE2 . TYR B 1 546 ? -3.178  9.079   54.715  1.00 15.87 ? 538  TYR B CE2 1 
ATOM   8822  C  CZ  . TYR B 1 546 ? -2.560  9.114   53.484  1.00 17.63 ? 538  TYR B CZ  1 
ATOM   8823  O  OH  . TYR B 1 546 ? -3.182  9.753   52.438  1.00 15.81 ? 538  TYR B OH  1 
ATOM   8824  N  N   . VAL B 1 547 ? -2.941  5.319   57.689  1.00 16.12 ? 539  VAL B N   1 
ATOM   8825  C  CA  . VAL B 1 547 ? -4.359  4.991   57.728  1.00 16.70 ? 539  VAL B CA  1 
ATOM   8826  C  C   . VAL B 1 547 ? -5.131  6.180   57.168  1.00 17.09 ? 539  VAL B C   1 
ATOM   8827  O  O   . VAL B 1 547 ? -5.257  7.217   57.823  1.00 17.90 ? 539  VAL B O   1 
ATOM   8828  C  CB  . VAL B 1 547 ? -4.805  4.647   59.152  1.00 19.02 ? 539  VAL B CB  1 
ATOM   8829  C  CG1 . VAL B 1 547 ? -6.297  4.301   59.192  1.00 25.61 ? 539  VAL B CG1 1 
ATOM   8830  C  CG2 . VAL B 1 547 ? -3.946  3.509   59.679  1.00 17.43 ? 539  VAL B CG2 1 
ATOM   8831  N  N   . ILE B 1 548 ? -5.654  6.032   55.956  1.00 16.67 ? 540  ILE B N   1 
ATOM   8832  C  CA  . ILE B 1 548 ? -6.393  7.133   55.357  1.00 17.17 ? 540  ILE B CA  1 
ATOM   8833  C  C   . ILE B 1 548 ? -7.858  7.110   55.780  1.00 18.30 ? 540  ILE B C   1 
ATOM   8834  O  O   . ILE B 1 548 ? -8.499  8.166   55.830  1.00 19.18 ? 540  ILE B O   1 
ATOM   8835  C  CB  . ILE B 1 548 ? -6.248  7.110   53.824  1.00 17.68 ? 540  ILE B CB  1 
ATOM   8836  C  CG1 . ILE B 1 548 ? -6.843  8.380   53.203  1.00 18.24 ? 540  ILE B CG1 1 
ATOM   8837  C  CG2 . ILE B 1 548 ? -6.886  5.868   53.236  1.00 18.16 ? 540  ILE B CG2 1 
ATOM   8838  C  CD1 . ILE B 1 548 ? -6.410  8.587   51.759  1.00 19.40 ? 540  ILE B CD1 1 
ATOM   8839  N  N   . SER B 1 549 ? -8.400  5.934   56.112  1.00 21.90 ? 541  SER B N   1 
ATOM   8840  C  CA  . SER B 1 549 ? -9.774  5.824   56.610  1.00 22.10 ? 541  SER B CA  1 
ATOM   8841  C  C   . SER B 1 549 ? -9.822  4.723   57.666  1.00 21.51 ? 541  SER B C   1 
ATOM   8842  O  O   . SER B 1 549 ? -9.815  3.535   57.331  1.00 21.83 ? 541  SER B O   1 
ATOM   8843  C  CB  . SER B 1 549 ? -10.750 5.541   55.473  1.00 22.06 ? 541  SER B CB  1 
ATOM   8844  O  OG  . SER B 1 549 ? -12.073 5.516   55.967  1.00 22.56 ? 541  SER B OG  1 
ATOM   8845  N  N   . GLU B 1 550 ? -9.876  5.114   58.938  1.00 20.72 ? 542  GLU B N   1 
ATOM   8846  C  CA  . GLU B 1 550 ? -9.900  4.128   60.010  1.00 21.12 ? 542  GLU B CA  1 
ATOM   8847  C  C   . GLU B 1 550 ? -11.180 3.295   59.969  1.00 27.06 ? 542  GLU B C   1 
ATOM   8848  O  O   . GLU B 1 550 ? -12.237 3.743   59.508  1.00 22.45 ? 542  GLU B O   1 
ATOM   8849  C  CB  . GLU B 1 550 ? -9.776  4.809   61.373  1.00 22.98 ? 542  GLU B CB  1 
ATOM   8850  C  CG  . GLU B 1 550 ? -9.669  3.833   62.545  1.00 30.37 ? 542  GLU B CG  1 
ATOM   8851  C  CD  . GLU B 1 550 ? -8.454  2.920   62.415  1.00 36.57 ? 542  GLU B CD  1 
ATOM   8852  O  OE1 . GLU B 1 550 ? -7.327  3.405   62.663  1.00 36.40 ? 542  GLU B OE1 1 
ATOM   8853  O  OE2 . GLU B 1 550 ? -8.620  1.733   62.053  1.00 21.21 ? 542  GLU B OE2 1 
ATOM   8854  N  N   . ALA B 1 551 ? -11.063 2.059   60.442  1.00 21.78 ? 543  ALA B N   1 
ATOM   8855  C  CA  . ALA B 1 551 ? -12.228 1.220   60.657  1.00 22.65 ? 543  ALA B CA  1 
ATOM   8856  C  C   . ALA B 1 551 ? -13.169 1.880   61.656  1.00 29.96 ? 543  ALA B C   1 
ATOM   8857  O  O   . ALA B 1 551 ? -12.734 2.399   62.686  1.00 25.21 ? 543  ALA B O   1 
ATOM   8858  C  CB  . ALA B 1 551 ? -11.787 -0.152  61.162  1.00 22.49 ? 543  ALA B CB  1 
ATOM   8859  N  N   . GLN B 1 552 ? -14.462 1.878   61.341  1.00 26.94 ? 544  GLN B N   1 
ATOM   8860  C  CA  . GLN B 1 552 ? -15.481 2.441   62.226  1.00 28.51 ? 544  GLN B CA  1 
ATOM   8861  C  C   . GLN B 1 552 ? -16.059 1.276   63.029  1.00 31.91 ? 544  GLN B C   1 
ATOM   8862  O  O   . GLN B 1 552 ? -17.082 0.694   62.671  1.00 36.57 ? 544  GLN B O   1 
ATOM   8863  C  CB  . GLN B 1 552 ? -16.537 3.196   61.424  1.00 31.05 ? 544  GLN B CB  1 
ATOM   8864  N  N   . GLY B 1 553 ? -15.399 0.952   64.136  1.00 29.39 ? 545  GLY B N   1 
ATOM   8865  C  CA  . GLY B 1 553 ? -15.564 -0.313  64.826  1.00 29.64 ? 545  GLY B CA  1 
ATOM   8866  C  C   . GLY B 1 553 ? -14.249 -1.070  64.875  1.00 30.20 ? 545  GLY B C   1 
ATOM   8867  O  O   . GLY B 1 553 ? -13.221 -0.608  64.386  1.00 25.82 ? 545  GLY B O   1 
ATOM   8868  N  N   . ASN B 1 554 ? -14.293 -2.255  65.484  1.00 27.45 ? 546  ASN B N   1 
ATOM   8869  C  CA  . ASN B 1 554 ? -13.090 -3.079  65.575  1.00 26.63 ? 546  ASN B CA  1 
ATOM   8870  C  C   . ASN B 1 554 ? -12.758 -3.664  64.205  1.00 25.34 ? 546  ASN B C   1 
ATOM   8871  O  O   . ASN B 1 554 ? -13.536 -4.449  63.655  1.00 31.40 ? 546  ASN B O   1 
ATOM   8872  C  CB  . ASN B 1 554 ? -13.270 -4.197  66.594  1.00 34.71 ? 546  ASN B CB  1 
ATOM   8873  N  N   . ALA B 1 555 ? -11.591 -3.301  63.670  1.00 31.54 ? 547  ALA B N   1 
ATOM   8874  C  CA  . ALA B 1 555 ? -11.202 -3.712  62.322  1.00 27.13 ? 547  ALA B CA  1 
ATOM   8875  C  C   . ALA B 1 555 ? -11.101 -5.228  62.206  1.00 31.95 ? 547  ALA B C   1 
ATOM   8876  O  O   . ALA B 1 555 ? -10.503 -5.893  63.057  1.00 34.30 ? 547  ALA B O   1 
ATOM   8877  C  CB  . ALA B 1 555 ? -9.865  -3.077  61.942  1.00 25.89 ? 547  ALA B CB  1 
ATOM   8878  N  N   . GLN B 1 556 ? -11.706 -5.773  61.151  1.00 29.17 ? 548  GLN B N   1 
ATOM   8879  C  CA  . GLN B 1 556 ? -11.585 -7.187  60.826  1.00 22.71 ? 548  GLN B CA  1 
ATOM   8880  C  C   . GLN B 1 556 ? -10.572 -7.438  59.720  1.00 24.10 ? 548  GLN B C   1 
ATOM   8881  O  O   . GLN B 1 556 ? -10.148 -8.580  59.529  1.00 29.25 ? 548  GLN B O   1 
ATOM   8882  C  CB  . GLN B 1 556 ? -12.942 -7.762  60.403  1.00 23.58 ? 548  GLN B CB  1 
ATOM   8883  C  CG  . GLN B 1 556 ? -13.984 -7.866  61.536  1.00 28.30 ? 548  GLN B CG  1 
ATOM   8884  C  CD  . GLN B 1 556 ? -15.271 -8.545  61.086  1.00 33.23 ? 548  GLN B CD  1 
ATOM   8885  O  OE1 . GLN B 1 556 ? -16.345 -7.942  61.107  1.00 38.12 ? 548  GLN B OE1 1 
ATOM   8886  N  NE2 . GLN B 1 556 ? -15.165 -9.808  60.680  1.00 33.89 ? 548  GLN B NE2 1 
ATOM   8887  N  N   . ALA B 1 557 ? -10.183 -6.397  58.997  1.00 20.50 ? 549  ALA B N   1 
ATOM   8888  C  CA  . ALA B 1 557 ? -9.173  -6.510  57.958  1.00 19.31 ? 549  ALA B CA  1 
ATOM   8889  C  C   . ALA B 1 557 ? -8.656  -5.112  57.663  1.00 21.06 ? 549  ALA B C   1 
ATOM   8890  O  O   . ALA B 1 557 ? -9.199  -4.111  58.140  1.00 20.45 ? 549  ALA B O   1 
ATOM   8891  C  CB  . ALA B 1 557 ? -9.736  -7.173  56.695  1.00 20.15 ? 549  ALA B CB  1 
ATOM   8892  N  N   . VAL B 1 558 ? -7.609  -5.051  56.852  1.00 17.50 ? 550  VAL B N   1 
ATOM   8893  C  CA  . VAL B 1 558 ? -7.118  -3.788  56.327  1.00 18.80 ? 550  VAL B CA  1 
ATOM   8894  C  C   . VAL B 1 558 ? -7.019  -3.919  54.815  1.00 18.15 ? 550  VAL B C   1 
ATOM   8895  O  O   . VAL B 1 558 ? -6.466  -4.904  54.310  1.00 18.56 ? 550  VAL B O   1 
ATOM   8896  C  CB  . VAL B 1 558 ? -5.757  -3.404  56.937  1.00 22.51 ? 550  VAL B CB  1 
ATOM   8897  C  CG1 . VAL B 1 558 ? -4.837  -4.606  56.986  1.00 27.66 ? 550  VAL B CG1 1 
ATOM   8898  C  CG2 . VAL B 1 558 ? -5.115  -2.284  56.146  1.00 20.84 ? 550  VAL B CG2 1 
ATOM   8899  N  N   . ILE B 1 559 ? -7.572  -2.945  54.097  1.00 15.94 ? 551  ILE B N   1 
ATOM   8900  C  CA  . ILE B 1 559 ? -7.336  -2.833  52.662  1.00 16.38 ? 551  ILE B CA  1 
ATOM   8901  C  C   . ILE B 1 559 ? -6.167  -1.878  52.459  1.00 14.81 ? 551  ILE B C   1 
ATOM   8902  O  O   . ILE B 1 559 ? -6.204  -0.728  52.915  1.00 14.79 ? 551  ILE B O   1 
ATOM   8903  C  CB  . ILE B 1 559 ? -8.588  -2.342  51.916  1.00 16.60 ? 551  ILE B CB  1 
ATOM   8904  C  CG1 . ILE B 1 559 ? -9.794  -3.214  52.243  1.00 17.42 ? 551  ILE B CG1 1 
ATOM   8905  C  CG2 . ILE B 1 559 ? -8.349  -2.367  50.391  1.00 15.22 ? 551  ILE B CG2 1 
ATOM   8906  C  CD1 . ILE B 1 559 ? -11.119 -2.628  51.735  1.00 17.64 ? 551  ILE B CD1 1 
ATOM   8907  N  N   . ILE B 1 560 ? -5.129  -2.349  51.778  1.00 13.63 ? 552  ILE B N   1 
ATOM   8908  C  CA  . ILE B 1 560 ? -4.035  -1.501  51.330  1.00 12.86 ? 552  ILE B CA  1 
ATOM   8909  C  C   . ILE B 1 560 ? -4.321  -1.125  49.886  1.00 20.13 ? 552  ILE B C   1 
ATOM   8910  O  O   . ILE B 1 560 ? -4.597  -2.005  49.063  1.00 16.23 ? 552  ILE B O   1 
ATOM   8911  C  CB  . ILE B 1 560 ? -2.681  -2.222  51.441  1.00 12.31 ? 552  ILE B CB  1 
ATOM   8912  C  CG1 . ILE B 1 560 ? -2.442  -2.720  52.863  1.00 12.80 ? 552  ILE B CG1 1 
ATOM   8913  C  CG2 . ILE B 1 560 ? -1.550  -1.285  51.008  1.00 11.63 ? 552  ILE B CG2 1 
ATOM   8914  C  CD1 . ILE B 1 560 ? -1.466  -3.896  52.937  1.00 16.98 ? 552  ILE B CD1 1 
ATOM   8915  N  N   . ALA B 1 561 ? -4.260  0.170   49.575  1.00 12.44 ? 553  ALA B N   1 
ATOM   8916  C  CA  . ALA B 1 561 ? -4.471  0.633   48.205  1.00 12.26 ? 553  ALA B CA  1 
ATOM   8917  C  C   . ALA B 1 561 ? -3.456  1.716   47.868  1.00 13.63 ? 553  ALA B C   1 
ATOM   8918  O  O   . ALA B 1 561 ? -2.875  2.346   48.755  1.00 11.67 ? 553  ALA B O   1 
ATOM   8919  C  CB  . ALA B 1 561 ? -5.907  1.161   48.006  1.00 13.12 ? 553  ALA B CB  1 
ATOM   8920  N  N   . THR B 1 562 ? -3.272  1.945   46.566  1.00 11.41 ? 554  THR B N   1 
ATOM   8921  C  CA  . THR B 1 562 ? -2.377  2.977   46.062  1.00 10.98 ? 554  THR B CA  1 
ATOM   8922  C  C   . THR B 1 562 ? -3.062  3.733   44.932  1.00 11.34 ? 554  THR B C   1 
ATOM   8923  O  O   . THR B 1 562 ? -3.959  3.202   44.267  1.00 13.26 ? 554  THR B O   1 
ATOM   8924  C  CB  . THR B 1 562 ? -1.053  2.391   45.525  1.00 11.90 ? 554  THR B CB  1 
ATOM   8925  O  OG1 . THR B 1 562 ? -1.290  1.776   44.253  1.00 12.72 ? 554  THR B OG1 1 
ATOM   8926  C  CG2 . THR B 1 562 ? -0.475  1.325   46.486  1.00 12.83 ? 554  THR B CG2 1 
ATOM   8927  N  N   . GLY B 1 563 ? -2.630  4.980   44.725  1.00 12.69 ? 555  GLY B N   1 
ATOM   8928  C  CA  . GLY B 1 563 ? -2.993  5.710   43.511  1.00 13.56 ? 555  GLY B CA  1 
ATOM   8929  C  C   . GLY B 1 563 ? -4.489  5.726   43.249  1.00 15.06 ? 555  GLY B C   1 
ATOM   8930  O  O   . GLY B 1 563 ? -5.302  5.957   44.153  1.00 13.62 ? 555  GLY B O   1 
ATOM   8931  N  N   . SER B 1 564 ? -4.857  5.464   41.990  1.00 16.36 ? 556  SER B N   1 
ATOM   8932  C  CA  . SER B 1 564 ? -6.245  5.517   41.542  1.00 17.66 ? 556  SER B CA  1 
ATOM   8933  C  C   . SER B 1 564 ? -7.139  4.491   42.220  1.00 17.59 ? 556  SER B C   1 
ATOM   8934  O  O   . SER B 1 564 ? -8.361  4.575   42.066  1.00 16.87 ? 556  SER B O   1 
ATOM   8935  C  CB  . SER B 1 564 ? -6.309  5.314   40.019  1.00 16.48 ? 556  SER B CB  1 
ATOM   8936  O  OG  . SER B 1 564 ? -5.600  4.144   39.641  1.00 16.18 ? 556  SER B OG  1 
ATOM   8937  N  N   . GLU B 1 565 ? -6.591  3.523   42.945  1.00 14.00 ? 557  GLU B N   1 
ATOM   8938  C  CA  . GLU B 1 565 ? -7.441  2.512   43.568  1.00 15.01 ? 557  GLU B CA  1 
ATOM   8939  C  C   . GLU B 1 565 ? -7.814  2.839   45.009  1.00 13.65 ? 557  GLU B C   1 
ATOM   8940  O  O   . GLU B 1 565 ? -8.609  2.106   45.605  1.00 15.23 ? 557  GLU B O   1 
ATOM   8941  C  CB  . GLU B 1 565 ? -6.771  1.133   43.509  1.00 15.85 ? 557  GLU B CB  1 
ATOM   8942  C  CG  . GLU B 1 565 ? -6.904  0.436   42.147  1.00 13.27 ? 557  GLU B CG  1 
ATOM   8943  C  CD  . GLU B 1 565 ? -6.226  1.203   41.035  1.00 17.94 ? 557  GLU B CD  1 
ATOM   8944  O  OE1 . GLU B 1 565 ? -4.971  1.159   40.978  1.00 15.66 ? 557  GLU B OE1 1 
ATOM   8945  O  OE2 . GLU B 1 565 ? -6.934  1.864   40.233  1.00 15.87 ? 557  GLU B OE2 1 
ATOM   8946  N  N   . VAL B 1 566 ? -7.284  3.920   45.587  1.00 13.12 ? 558  VAL B N   1 
ATOM   8947  C  CA  . VAL B 1 566 ? -7.651  4.242   46.969  1.00 13.50 ? 558  VAL B CA  1 
ATOM   8948  C  C   . VAL B 1 566 ? -9.148  4.539   47.076  1.00 19.33 ? 558  VAL B C   1 
ATOM   8949  O  O   . VAL B 1 566 ? -9.819  4.097   48.021  1.00 15.22 ? 558  VAL B O   1 
ATOM   8950  C  CB  . VAL B 1 566 ? -6.797  5.409   47.505  1.00 14.96 ? 558  VAL B CB  1 
ATOM   8951  C  CG1 . VAL B 1 566 ? -7.325  5.861   48.889  1.00 17.05 ? 558  VAL B CG1 1 
ATOM   8952  C  CG2 . VAL B 1 566 ? -5.341  4.997   47.605  1.00 15.94 ? 558  VAL B CG2 1 
ATOM   8953  N  N   . GLY B 1 567 ? -9.699  5.272   46.104  1.00 19.57 ? 559  GLY B N   1 
ATOM   8954  C  CA  . GLY B 1 567 ? -11.131 5.547   46.122  1.00 21.65 ? 559  GLY B CA  1 
ATOM   8955  C  C   . GLY B 1 567 ? -11.964 4.278   46.134  1.00 21.28 ? 559  GLY B C   1 
ATOM   8956  O  O   . GLY B 1 567 ? -12.918 4.148   46.904  1.00 20.42 ? 559  GLY B O   1 
ATOM   8957  N  N   . LEU B 1 568 ? -11.606 3.324   45.278  1.00 15.61 ? 560  LEU B N   1 
ATOM   8958  C  CA  . LEU B 1 568 ? -12.281 2.030   45.255  1.00 20.45 ? 560  LEU B CA  1 
ATOM   8959  C  C   . LEU B 1 568 ? -12.210 1.341   46.616  1.00 18.06 ? 560  LEU B C   1 
ATOM   8960  O  O   . LEU B 1 568 ? -13.204 0.768   47.087  1.00 16.15 ? 560  LEU B O   1 
ATOM   8961  C  CB  . LEU B 1 568 ? -11.648 1.162   44.164  1.00 16.44 ? 560  LEU B CB  1 
ATOM   8962  C  CG  . LEU B 1 568 ? -11.976 -0.326  44.117  1.00 16.19 ? 560  LEU B CG  1 
ATOM   8963  C  CD1 . LEU B 1 568 ? -13.482 -0.554  43.954  1.00 19.50 ? 560  LEU B CD1 1 
ATOM   8964  C  CD2 . LEU B 1 568 ? -11.178 -0.982  42.987  1.00 18.97 ? 560  LEU B CD2 1 
ATOM   8965  N  N   . ALA B 1 569 ? -11.052 1.401   47.272  1.00 14.89 ? 561  ALA B N   1 
ATOM   8966  C  CA  . ALA B 1 569 ? -10.931 0.767   48.583  1.00 17.89 ? 561  ALA B CA  1 
ATOM   8967  C  C   . ALA B 1 569 ? -11.849 1.424   49.607  1.00 21.74 ? 561  ALA B C   1 
ATOM   8968  O  O   . ALA B 1 569 ? -12.476 0.737   50.422  1.00 16.34 ? 561  ALA B O   1 
ATOM   8969  C  CB  . ALA B 1 569 ? -9.478  0.808   49.061  1.00 16.38 ? 561  ALA B CB  1 
ATOM   8970  N  N   . VAL B 1 570 ? -11.935 2.757   49.590  1.00 16.65 ? 562  VAL B N   1 
ATOM   8971  C  CA  . VAL B 1 570 ? -12.779 3.447   50.561  1.00 17.82 ? 562  VAL B CA  1 
ATOM   8972  C  C   . VAL B 1 570 ? -14.260 3.167   50.290  1.00 18.56 ? 562  VAL B C   1 
ATOM   8973  O  O   . VAL B 1 570 ? -15.060 3.051   51.222  1.00 20.39 ? 562  VAL B O   1 
ATOM   8974  C  CB  . VAL B 1 570 ? -12.463 4.955   50.563  1.00 18.02 ? 562  VAL B CB  1 
ATOM   8975  C  CG1 . VAL B 1 570 ? -13.488 5.728   51.410  1.00 24.54 ? 562  VAL B CG1 1 
ATOM   8976  C  CG2 . VAL B 1 570 ? -11.054 5.192   51.091  1.00 15.86 ? 562  VAL B CG2 1 
ATOM   8977  N  N   . GLU B 1 571 ? -14.646 3.048   49.015  1.00 18.00 ? 563  GLU B N   1 
ATOM   8978  C  CA  . GLU B 1 571 ? -16.026 2.680   48.697  1.00 20.71 ? 563  GLU B CA  1 
ATOM   8979  C  C   . GLU B 1 571 ? -16.355 1.281   49.202  1.00 18.04 ? 563  GLU B C   1 
ATOM   8980  O  O   . GLU B 1 571 ? -17.441 1.047   49.749  1.00 20.81 ? 563  GLU B O   1 
ATOM   8981  C  CB  . GLU B 1 571 ? -16.261 2.768   47.187  1.00 20.07 ? 563  GLU B CB  1 
ATOM   8982  C  CG  . GLU B 1 571 ? -16.463 4.182   46.667  1.00 33.59 ? 563  GLU B CG  1 
ATOM   8983  C  CD  . GLU B 1 571 ? -16.564 4.244   45.154  1.00 45.07 ? 563  GLU B CD  1 
ATOM   8984  O  OE1 . GLU B 1 571 ? -15.542 4.534   44.495  1.00 50.98 ? 563  GLU B OE1 1 
ATOM   8985  O  OE2 . GLU B 1 571 ? -17.665 3.989   44.625  1.00 53.88 ? 563  GLU B OE2 1 
ATOM   8986  N  N   . ALA B 1 572 ? -15.430 0.337   49.020  1.00 17.51 ? 564  ALA B N   1 
ATOM   8987  C  CA  . ALA B 1 572 ? -15.617 -1.017  49.530  1.00 17.85 ? 564  ALA B CA  1 
ATOM   8988  C  C   . ALA B 1 572 ? -15.725 -1.015  51.044  1.00 18.34 ? 564  ALA B C   1 
ATOM   8989  O  O   . ALA B 1 572 ? -16.524 -1.762  51.622  1.00 22.99 ? 564  ALA B O   1 
ATOM   8990  C  CB  . ALA B 1 572 ? -14.456 -1.906  49.087  1.00 17.19 ? 564  ALA B CB  1 
ATOM   8991  N  N   . GLN B 1 573 ? -14.937 -0.165  51.699  1.00 18.03 ? 565  GLN B N   1 
ATOM   8992  C  CA  . GLN B 1 573 ? -15.033 -0.031  53.147  1.00 18.55 ? 565  GLN B CA  1 
ATOM   8993  C  C   . GLN B 1 573 ? -16.434 0.368   53.572  1.00 22.14 ? 565  GLN B C   1 
ATOM   8994  O  O   . GLN B 1 573 ? -16.951 -0.134  54.574  1.00 21.31 ? 565  GLN B O   1 
ATOM   8995  C  CB  . GLN B 1 573 ? -14.024 0.997   53.650  1.00 18.12 ? 565  GLN B CB  1 
ATOM   8996  C  CG  . GLN B 1 573 ? -14.131 1.307   55.154  1.00 18.71 ? 565  GLN B CG  1 
ATOM   8997  C  CD  . GLN B 1 573 ? -13.289 2.515   55.537  1.00 19.00 ? 565  GLN B CD  1 
ATOM   8998  O  OE1 . GLN B 1 573 ? -13.362 3.559   54.890  1.00 21.72 ? 565  GLN B OE1 1 
ATOM   8999  N  NE2 . GLN B 1 573 ? -12.467 2.372   56.573  1.00 19.36 ? 565  GLN B NE2 1 
ATOM   9000  N  N   . LYS B 1 574 ? -17.052 1.292   52.837  1.00 19.46 ? 566  LYS B N   1 
ATOM   9001  C  CA  . LYS B 1 574 ? -18.375 1.762   53.218  1.00 24.03 ? 566  LYS B CA  1 
ATOM   9002  C  C   . LYS B 1 574 ? -19.449 0.713   52.959  1.00 24.63 ? 566  LYS B C   1 
ATOM   9003  O  O   . LYS B 1 574 ? -20.422 0.630   53.722  1.00 21.89 ? 566  LYS B O   1 
ATOM   9004  C  CB  . LYS B 1 574 ? -18.689 3.070   52.490  1.00 29.44 ? 566  LYS B CB  1 
ATOM   9005  C  CG  . LYS B 1 574 ? -18.130 4.270   53.228  1.00 38.28 ? 566  LYS B CG  1 
ATOM   9006  C  CD  . LYS B 1 574 ? -17.482 5.283   52.309  1.00 43.61 ? 566  LYS B CD  1 
ATOM   9007  C  CE  . LYS B 1 574 ? -16.626 6.230   53.137  1.00 44.61 ? 566  LYS B CE  1 
ATOM   9008  N  NZ  . LYS B 1 574 ? -15.672 5.464   54.008  1.00 37.97 ? 566  LYS B NZ  1 
ATOM   9009  N  N   . VAL B 1 575 ? -19.297 -0.092  51.903  1.00 24.82 ? 567  VAL B N   1 
ATOM   9010  C  CA  . VAL B 1 575 ? -20.214 -1.210  51.678  1.00 26.84 ? 567  VAL B CA  1 
ATOM   9011  C  C   . VAL B 1 575 ? -20.051 -2.257  52.775  1.00 24.07 ? 567  VAL B C   1 
ATOM   9012  O  O   . VAL B 1 575 ? -21.034 -2.769  53.324  1.00 25.64 ? 567  VAL B O   1 
ATOM   9013  C  CB  . VAL B 1 575 ? -19.989 -1.821  50.281  1.00 24.34 ? 567  VAL B CB  1 
ATOM   9014  C  CG1 . VAL B 1 575 ? -20.749 -3.136  50.141  1.00 26.18 ? 567  VAL B CG1 1 
ATOM   9015  C  CG2 . VAL B 1 575 ? -20.408 -0.840  49.192  1.00 24.43 ? 567  VAL B CG2 1 
ATOM   9016  N  N   . LEU B 1 576 ? -18.803 -2.602  53.099  1.00 22.31 ? 568  LEU B N   1 
ATOM   9017  C  CA  . LEU B 1 576 ? -18.548 -3.532  54.197  1.00 21.45 ? 568  LEU B CA  1 
ATOM   9018  C  C   . LEU B 1 576 ? -19.144 -3.029  55.512  1.00 26.20 ? 568  LEU B C   1 
ATOM   9019  O  O   . LEU B 1 576 ? -19.735 -3.808  56.268  1.00 29.87 ? 568  LEU B O   1 
ATOM   9020  C  CB  . LEU B 1 576 ? -17.042 -3.761  54.337  1.00 20.65 ? 568  LEU B CB  1 
ATOM   9021  C  CG  . LEU B 1 576 ? -16.449 -4.634  53.226  1.00 26.64 ? 568  LEU B CG  1 
ATOM   9022  C  CD1 . LEU B 1 576 ? -14.951 -4.394  53.062  1.00 19.93 ? 568  LEU B CD1 1 
ATOM   9023  C  CD2 . LEU B 1 576 ? -16.744 -6.118  53.493  1.00 20.65 ? 568  LEU B CD2 1 
ATOM   9024  N  N   . ALA B 1 577 ? -18.998 -1.730  55.803  1.00 26.92 ? 569  ALA B N   1 
ATOM   9025  C  CA  . ALA B 1 577 ? -19.561 -1.174  57.035  1.00 26.14 ? 569  ALA B CA  1 
ATOM   9026  C  C   . ALA B 1 577 ? -21.079 -1.312  57.066  1.00 29.96 ? 569  ALA B C   1 
ATOM   9027  O  O   . ALA B 1 577 ? -21.673 -1.532  58.132  1.00 29.24 ? 569  ALA B O   1 
ATOM   9028  C  CB  . ALA B 1 577 ? -19.160 0.296   57.185  1.00 23.96 ? 569  ALA B CB  1 
ATOM   9029  N  N   . GLY B 1 578 ? -21.728 -1.165  55.911  1.00 26.16 ? 570  GLY B N   1 
ATOM   9030  C  CA  . GLY B 1 578 ? -23.154 -1.421  55.830  1.00 30.00 ? 570  GLY B CA  1 
ATOM   9031  C  C   . GLY B 1 578 ? -23.538 -2.853  56.137  1.00 30.48 ? 570  GLY B C   1 
ATOM   9032  O  O   . GLY B 1 578 ? -24.691 -3.114  56.492  1.00 34.44 ? 570  GLY B O   1 
ATOM   9033  N  N   . GLN B 1 579 ? -22.607 -3.791  55.996  1.00 29.05 ? 571  GLN B N   1 
ATOM   9034  C  CA  . GLN B 1 579 ? -22.833 -5.182  56.360  1.00 30.10 ? 571  GLN B CA  1 
ATOM   9035  C  C   . GLN B 1 579 ? -22.275 -5.529  57.735  1.00 35.40 ? 571  GLN B C   1 
ATOM   9036  O  O   . GLN B 1 579 ? -22.168 -6.714  58.065  1.00 38.59 ? 571  GLN B O   1 
ATOM   9037  C  CB  . GLN B 1 579 ? -22.224 -6.106  55.312  1.00 34.38 ? 571  GLN B CB  1 
ATOM   9038  C  CG  . GLN B 1 579 ? -22.695 -5.826  53.898  1.00 40.05 ? 571  GLN B CG  1 
ATOM   9039  C  CD  . GLN B 1 579 ? -22.003 -6.710  52.884  1.00 44.60 ? 571  GLN B CD  1 
ATOM   9040  O  OE1 . GLN B 1 579 ? -21.556 -7.809  53.209  1.00 43.45 ? 571  GLN B OE1 1 
ATOM   9041  N  NE2 . GLN B 1 579 ? -21.911 -6.237  51.650  1.00 48.36 ? 571  GLN B NE2 1 
ATOM   9042  N  N   . GLY B 1 580 ? -21.907 -4.528  58.536  1.00 32.73 ? 572  GLY B N   1 
ATOM   9043  C  CA  . GLY B 1 580 ? -21.377 -4.777  59.861  1.00 34.33 ? 572  GLY B CA  1 
ATOM   9044  C  C   . GLY B 1 580 ? -19.937 -5.226  59.896  1.00 33.14 ? 572  GLY B C   1 
ATOM   9045  O  O   . GLY B 1 580 ? -19.478 -5.702  60.942  1.00 30.69 ? 572  GLY B O   1 
ATOM   9046  N  N   . ILE B 1 581 ? -19.208 -5.078  58.794  1.00 27.02 ? 573  ILE B N   1 
ATOM   9047  C  CA  . ILE B 1 581 ? -17.815 -5.485  58.701  1.00 30.40 ? 573  ILE B CA  1 
ATOM   9048  C  C   . ILE B 1 581 ? -16.980 -4.210  58.681  1.00 28.03 ? 573  ILE B C   1 
ATOM   9049  O  O   . ILE B 1 581 ? -16.876 -3.539  57.648  1.00 25.47 ? 573  ILE B O   1 
ATOM   9050  C  CB  . ILE B 1 581 ? -17.553 -6.343  57.460  1.00 30.19 ? 573  ILE B CB  1 
ATOM   9051  C  CG1 . ILE B 1 581 ? -18.593 -7.452  57.347  1.00 30.25 ? 573  ILE B CG1 1 
ATOM   9052  C  CG2 . ILE B 1 581 ? -16.142 -6.927  57.503  1.00 26.31 ? 573  ILE B CG2 1 
ATOM   9053  C  CD1 . ILE B 1 581 ? -18.305 -8.419  56.227  1.00 32.72 ? 573  ILE B CD1 1 
ATOM   9054  N  N   . ALA B 1 582 ? -16.371 -3.874  59.814  1.00 25.61 ? 574  ALA B N   1 
ATOM   9055  C  CA  . ALA B 1 582 ? -15.476 -2.727  59.870  1.00 22.16 ? 574  ALA B CA  1 
ATOM   9056  C  C   . ALA B 1 582 ? -14.090 -3.118  59.364  1.00 24.17 ? 574  ALA B C   1 
ATOM   9057  O  O   . ALA B 1 582 ? -13.509 -4.110  59.815  1.00 25.05 ? 574  ALA B O   1 
ATOM   9058  C  CB  . ALA B 1 582 ? -15.384 -2.183  61.296  1.00 22.79 ? 574  ALA B CB  1 
ATOM   9059  N  N   . VAL B 1 583 ? -13.571 -2.352  58.411  1.00 20.37 ? 575  VAL B N   1 
ATOM   9060  C  CA  . VAL B 1 583 ? -12.210 -2.535  57.928  1.00 20.54 ? 575  VAL B CA  1 
ATOM   9061  C  C   . VAL B 1 583 ? -11.521 -1.181  57.891  1.00 18.97 ? 575  VAL B C   1 
ATOM   9062  O  O   . VAL B 1 583 ? -12.159 -0.130  57.769  1.00 21.64 ? 575  VAL B O   1 
ATOM   9063  C  CB  . VAL B 1 583 ? -12.141 -3.217  56.537  1.00 24.84 ? 575  VAL B CB  1 
ATOM   9064  C  CG1 . VAL B 1 583 ? -12.920 -4.536  56.543  1.00 24.65 ? 575  VAL B CG1 1 
ATOM   9065  C  CG2 . VAL B 1 583 ? -12.638 -2.282  55.438  1.00 18.52 ? 575  VAL B CG2 1 
ATOM   9066  N  N   . ARG B 1 584 ? -10.205 -1.217  58.024  1.00 18.48 ? 576  ARG B N   1 
ATOM   9067  C  CA  . ARG B 1 584 ? -9.370  -0.039  57.889  1.00 19.00 ? 576  ARG B CA  1 
ATOM   9068  C  C   . ARG B 1 584 ? -8.873  0.038   56.451  1.00 19.28 ? 576  ARG B C   1 
ATOM   9069  O  O   . ARG B 1 584 ? -8.633  -0.993  55.823  1.00 16.81 ? 576  ARG B O   1 
ATOM   9070  C  CB  . ARG B 1 584 ? -8.204  -0.142  58.876  1.00 19.51 ? 576  ARG B CB  1 
ATOM   9071  C  CG  . ARG B 1 584 ? -6.899  0.413   58.427  1.00 25.37 ? 576  ARG B CG  1 
ATOM   9072  C  CD  . ARG B 1 584 ? -5.813  -0.055  59.387  1.00 22.58 ? 576  ARG B CD  1 
ATOM   9073  N  NE  . ARG B 1 584 ? -5.999  0.489   60.740  1.00 21.35 ? 576  ARG B NE  1 
ATOM   9074  C  CZ  . ARG B 1 584 ? -5.026  0.562   61.645  1.00 19.66 ? 576  ARG B CZ  1 
ATOM   9075  N  NH1 . ARG B 1 584 ? -3.811  0.115   61.346  1.00 18.66 ? 576  ARG B NH1 1 
ATOM   9076  N  NH2 . ARG B 1 584 ? -5.258  1.095   62.842  1.00 22.06 ? 576  ARG B NH2 1 
ATOM   9077  N  N   . VAL B 1 585 ? -8.747  1.253   55.917  1.00 19.63 ? 577  VAL B N   1 
ATOM   9078  C  CA  . VAL B 1 585 ? -8.116  1.457   54.612  1.00 19.29 ? 577  VAL B CA  1 
ATOM   9079  C  C   . VAL B 1 585 ? -6.786  2.165   54.819  1.00 15.47 ? 577  VAL B C   1 
ATOM   9080  O  O   . VAL B 1 585 ? -6.734  3.266   55.386  1.00 15.64 ? 577  VAL B O   1 
ATOM   9081  C  CB  . VAL B 1 585 ? -9.000  2.251   53.635  1.00 18.16 ? 577  VAL B CB  1 
ATOM   9082  C  CG1 . VAL B 1 585 ? -8.256  2.436   52.306  1.00 16.63 ? 577  VAL B CG1 1 
ATOM   9083  C  CG2 . VAL B 1 585 ? -10.329 1.539   53.394  1.00 16.28 ? 577  VAL B CG2 1 
ATOM   9084  N  N   . VAL B 1 586 ? -5.718  1.554   54.317  1.00 14.96 ? 578  VAL B N   1 
ATOM   9085  C  CA  . VAL B 1 586 ? -4.382  2.140   54.332  1.00 14.55 ? 578  VAL B CA  1 
ATOM   9086  C  C   . VAL B 1 586 ? -4.050  2.609   52.921  1.00 14.72 ? 578  VAL B C   1 
ATOM   9087  O  O   . VAL B 1 586 ? -4.191  1.845   51.958  1.00 15.85 ? 578  VAL B O   1 
ATOM   9088  C  CB  . VAL B 1 586 ? -3.352  1.131   54.858  1.00 14.55 ? 578  VAL B CB  1 
ATOM   9089  C  CG1 . VAL B 1 586 ? -1.911  1.528   54.483  1.00 14.03 ? 578  VAL B CG1 1 
ATOM   9090  C  CG2 . VAL B 1 586 ? -3.523  0.977   56.386  1.00 15.26 ? 578  VAL B CG2 1 
ATOM   9091  N  N   . SER B 1 587 ? -3.641  3.871   52.797  1.00 14.30 ? 579  SER B N   1 
ATOM   9092  C  CA  . SER B 1 587 ? -3.062  4.376   51.554  1.00 16.36 ? 579  SER B CA  1 
ATOM   9093  C  C   . SER B 1 587 ? -1.562  4.166   51.634  1.00 12.90 ? 579  SER B C   1 
ATOM   9094  O  O   . SER B 1 587 ? -0.938  4.550   52.623  1.00 14.37 ? 579  SER B O   1 
ATOM   9095  C  CB  . SER B 1 587 ? -3.368  5.861   51.350  1.00 14.21 ? 579  SER B CB  1 
ATOM   9096  O  OG  . SER B 1 587 ? -2.859  6.332   50.103  1.00 14.48 ? 579  SER B OG  1 
ATOM   9097  N  N   . MET B 1 588 ? -0.979  3.543   50.606  1.00 13.45 ? 580  MET B N   1 
ATOM   9098  C  CA  . MET B 1 588 ? 0.461   3.291   50.568  1.00 12.17 ? 580  MET B CA  1 
ATOM   9099  C  C   . MET B 1 588 ? 1.028   3.972   49.325  1.00 11.74 ? 580  MET B C   1 
ATOM   9100  O  O   . MET B 1 588 ? 1.386   3.306   48.345  1.00 13.10 ? 580  MET B O   1 
ATOM   9101  C  CB  . MET B 1 588 ? 0.767   1.792   50.580  1.00 14.61 ? 580  MET B CB  1 
ATOM   9102  C  CG  . MET B 1 588 ? 2.268   1.432   50.661  1.00 13.71 ? 580  MET B CG  1 
ATOM   9103  S  SD  . MET B 1 588 ? 2.544   -0.320  51.040  1.00 13.77 ? 580  MET B SD  1 
ATOM   9104  C  CE  . MET B 1 588 ? 1.871   -0.462  52.705  1.00 14.10 ? 580  MET B CE  1 
ATOM   9105  N  N   . PRO B 1 589 ? 1.109   5.306   49.332  1.00 12.93 ? 581  PRO B N   1 
ATOM   9106  C  CA  . PRO B 1 589 ? 1.638   6.013   48.156  1.00 12.76 ? 581  PRO B CA  1 
ATOM   9107  C  C   . PRO B 1 589 ? 3.071   5.648   47.824  1.00 15.20 ? 581  PRO B C   1 
ATOM   9108  O  O   . PRO B 1 589 ? 3.471   5.807   46.668  1.00 13.86 ? 581  PRO B O   1 
ATOM   9109  C  CB  . PRO B 1 589 ? 1.518   7.492   48.544  1.00 17.35 ? 581  PRO B CB  1 
ATOM   9110  C  CG  . PRO B 1 589 ? 1.470   7.477   50.046  1.00 17.90 ? 581  PRO B CG  1 
ATOM   9111  C  CD  . PRO B 1 589 ? 0.691   6.246   50.384  1.00 12.24 ? 581  PRO B CD  1 
ATOM   9112  N  N   . SER B 1 590 ? 3.862   5.164   48.784  1.00 11.33 ? 582  SER B N   1 
ATOM   9113  C  CA  . SER B 1 590 ? 5.203   4.679   48.457  1.00 13.27 ? 582  SER B CA  1 
ATOM   9114  C  C   . SER B 1 590 ? 5.542   3.459   49.301  1.00 16.70 ? 582  SER B C   1 
ATOM   9115  O  O   . SER B 1 590 ? 5.819   3.592   50.502  1.00 13.79 ? 582  SER B O   1 
ATOM   9116  C  CB  . SER B 1 590 ? 6.258   5.772   48.654  1.00 12.81 ? 582  SER B CB  1 
ATOM   9117  O  OG  . SER B 1 590 ? 7.531   5.248   48.371  1.00 11.67 ? 582  SER B OG  1 
ATOM   9118  N  N   . THR B 1 591 ? 5.574   2.277   48.666  1.00 13.29 ? 583  THR B N   1 
ATOM   9119  C  CA  . THR B 1 591 ? 6.109   1.093   49.341  1.00 12.95 ? 583  THR B CA  1 
ATOM   9120  C  C   . THR B 1 591 ? 7.553   1.318   49.771  1.00 13.89 ? 583  THR B C   1 
ATOM   9121  O  O   . THR B 1 591 ? 7.976   0.862   50.844  1.00 12.40 ? 583  THR B O   1 
ATOM   9122  C  CB  . THR B 1 591 ? 6.037   -0.131  48.422  1.00 13.52 ? 583  THR B CB  1 
ATOM   9123  O  OG1 . THR B 1 591 ? 6.851   0.099   47.269  1.00 12.58 ? 583  THR B OG1 1 
ATOM   9124  C  CG2 . THR B 1 591 ? 4.589   -0.391  47.952  1.00 12.11 ? 583  THR B CG2 1 
ATOM   9125  N  N   . SER B 1 592 ? 8.334   1.993   48.923  1.00 11.62 ? 584  SER B N   1 
ATOM   9126  C  CA  . SER B 1 592 ? 9.762   2.170   49.172  1.00 15.18 ? 584  SER B CA  1 
ATOM   9127  C  C   . SER B 1 592 ? 9.991   2.893   50.490  1.00 15.79 ? 584  SER B C   1 
ATOM   9128  O  O   . SER B 1 592 ? 10.795  2.463   51.327  1.00 12.84 ? 584  SER B O   1 
ATOM   9129  C  CB  . SER B 1 592 ? 10.391  2.955   48.013  1.00 10.90 ? 584  SER B CB  1 
ATOM   9130  O  OG  . SER B 1 592 ? 9.695   2.695   46.787  1.00 13.70 ? 584  SER B OG  1 
ATOM   9131  N  N   . VAL B 1 593 ? 9.260   3.982   50.697  1.00 11.68 ? 585  VAL B N   1 
ATOM   9132  C  CA  . VAL B 1 593 ? 9.397   4.764   51.917  1.00 12.52 ? 585  VAL B CA  1 
ATOM   9133  C  C   . VAL B 1 593 ? 8.815   4.007   53.097  1.00 15.48 ? 585  VAL B C   1 
ATOM   9134  O  O   . VAL B 1 593 ? 9.372   4.036   54.199  1.00 14.65 ? 585  VAL B O   1 
ATOM   9135  C  CB  . VAL B 1 593 ? 8.715   6.134   51.745  1.00 12.15 ? 585  VAL B CB  1 
ATOM   9136  C  CG1 . VAL B 1 593 ? 8.745   6.927   53.070  1.00 13.15 ? 585  VAL B CG1 1 
ATOM   9137  C  CG2 . VAL B 1 593 ? 9.364   6.915   50.606  1.00 12.46 ? 585  VAL B CG2 1 
ATOM   9138  N  N   . PHE B 1 594 ? 7.664   3.347   52.899  1.00 12.39 ? 586  PHE B N   1 
ATOM   9139  C  CA  . PHE B 1 594 ? 7.038   2.653   54.019  1.00 12.83 ? 586  PHE B CA  1 
ATOM   9140  C  C   . PHE B 1 594 ? 7.968   1.591   54.568  1.00 14.08 ? 586  PHE B C   1 
ATOM   9141  O  O   . PHE B 1 594 ? 8.074   1.416   55.784  1.00 13.80 ? 586  PHE B O   1 
ATOM   9142  C  CB  . PHE B 1 594 ? 5.704   2.015   53.606  1.00 12.98 ? 586  PHE B CB  1 
ATOM   9143  C  CG  . PHE B 1 594 ? 5.036   1.252   54.724  1.00 14.05 ? 586  PHE B CG  1 
ATOM   9144  C  CD1 . PHE B 1 594 ? 4.643   1.910   55.876  1.00 13.73 ? 586  PHE B CD1 1 
ATOM   9145  C  CD2 . PHE B 1 594 ? 4.840   -0.120  54.636  1.00 13.29 ? 586  PHE B CD2 1 
ATOM   9146  C  CE1 . PHE B 1 594 ? 4.024   1.230   56.916  1.00 14.74 ? 586  PHE B CE1 1 
ATOM   9147  C  CE2 . PHE B 1 594 ? 4.239   -0.816  55.668  1.00 13.87 ? 586  PHE B CE2 1 
ATOM   9148  C  CZ  . PHE B 1 594 ? 3.825   -0.137  56.823  1.00 18.38 ? 586  PHE B CZ  1 
ATOM   9149  N  N   . ASP B 1 595 ? 8.664   0.884   53.679  1.00 12.93 ? 587  ASP B N   1 
ATOM   9150  C  CA  . ASP B 1 595 ? 9.544   -0.203  54.096  1.00 17.12 ? 587  ASP B CA  1 
ATOM   9151  C  C   . ASP B 1 595 ? 10.713  0.272   54.946  1.00 18.54 ? 587  ASP B C   1 
ATOM   9152  O  O   . ASP B 1 595 ? 11.325  -0.552  55.634  1.00 17.28 ? 587  ASP B O   1 
ATOM   9153  C  CB  . ASP B 1 595 ? 10.088  -0.945  52.872  1.00 22.18 ? 587  ASP B CB  1 
ATOM   9154  C  CG  . ASP B 1 595 ? 9.029   -1.741  52.146  1.00 29.56 ? 587  ASP B CG  1 
ATOM   9155  O  OD1 . ASP B 1 595 ? 8.019   -2.114  52.778  1.00 29.12 ? 587  ASP B OD1 1 
ATOM   9156  O  OD2 . ASP B 1 595 ? 9.215   -2.007  50.936  1.00 28.42 ? 587  ASP B OD2 1 
ATOM   9157  N  N   . ARG B 1 596 ? 11.058  1.565   54.889  1.00 14.94 ? 588  ARG B N   1 
ATOM   9158  C  CA  . ARG B 1 596 ? 12.135  2.139   55.692  1.00 20.50 ? 588  ARG B CA  1 
ATOM   9159  C  C   . ARG B 1 596 ? 11.682  2.608   57.066  1.00 18.78 ? 588  ARG B C   1 
ATOM   9160  O  O   . ARG B 1 596 ? 12.532  2.934   57.898  1.00 21.85 ? 588  ARG B O   1 
ATOM   9161  C  CB  . ARG B 1 596 ? 12.771  3.351   54.991  1.00 20.60 ? 588  ARG B CB  1 
ATOM   9162  C  CG  . ARG B 1 596 ? 13.538  3.065   53.728  1.00 26.62 ? 588  ARG B CG  1 
ATOM   9163  C  CD  . ARG B 1 596 ? 14.496  4.216   53.407  1.00 28.30 ? 588  ARG B CD  1 
ATOM   9164  N  NE  . ARG B 1 596 ? 13.836  5.465   53.024  1.00 28.22 ? 588  ARG B NE  1 
ATOM   9165  C  CZ  . ARG B 1 596 ? 13.384  5.718   51.796  1.00 26.49 ? 588  ARG B CZ  1 
ATOM   9166  N  NH1 . ARG B 1 596 ? 13.493  4.794   50.859  1.00 22.67 ? 588  ARG B NH1 1 
ATOM   9167  N  NH2 . ARG B 1 596 ? 12.818  6.881   51.508  1.00 31.09 ? 588  ARG B NH2 1 
ATOM   9168  N  N   . GLN B 1 597 ? 10.381  2.697   57.311  1.00 15.72 ? 589  GLN B N   1 
ATOM   9169  C  CA  . GLN B 1 597 ? 9.920   3.170   58.605  1.00 15.09 ? 589  GLN B CA  1 
ATOM   9170  C  C   . GLN B 1 597 ? 10.233  2.137   59.684  1.00 15.75 ? 589  GLN B C   1 
ATOM   9171  O  O   . GLN B 1 597 ? 10.374  0.944   59.413  1.00 19.08 ? 589  GLN B O   1 
ATOM   9172  C  CB  . GLN B 1 597 ? 8.412   3.448   58.584  1.00 18.54 ? 589  GLN B CB  1 
ATOM   9173  C  CG  . GLN B 1 597 ? 7.965   4.396   57.465  1.00 18.90 ? 589  GLN B CG  1 
ATOM   9174  C  CD  . GLN B 1 597 ? 8.782   5.674   57.444  1.00 19.80 ? 589  GLN B CD  1 
ATOM   9175  O  OE1 . GLN B 1 597 ? 8.719   6.480   58.369  1.00 18.40 ? 589  GLN B OE1 1 
ATOM   9176  N  NE2 . GLN B 1 597 ? 9.561   5.859   56.388  1.00 15.44 ? 589  GLN B NE2 1 
ATOM   9177  N  N   . ASP B 1 598 ? 10.313  2.612   60.926  1.00 16.45 ? 590  ASP B N   1 
ATOM   9178  C  CA  . ASP B 1 598 ? 10.619  1.730   62.044  1.00 29.62 ? 590  ASP B CA  1 
ATOM   9179  C  C   . ASP B 1 598 ? 9.503   0.699   62.237  1.00 23.81 ? 590  ASP B C   1 
ATOM   9180  O  O   . ASP B 1 598 ? 8.362   0.882   61.803  1.00 18.56 ? 590  ASP B O   1 
ATOM   9181  C  CB  . ASP B 1 598 ? 10.838  2.543   63.324  1.00 28.36 ? 590  ASP B CB  1 
ATOM   9182  C  CG  . ASP B 1 598 ? 9.649   3.430   63.673  1.00 34.77 ? 590  ASP B CG  1 
ATOM   9183  O  OD1 . ASP B 1 598 ? 8.648   2.919   64.208  1.00 31.07 ? 590  ASP B OD1 1 
ATOM   9184  O  OD2 . ASP B 1 598 ? 9.718   4.651   63.416  1.00 41.48 ? 590  ASP B OD2 1 
ATOM   9185  N  N   . ALA B 1 599 ? 9.860   -0.411  62.888  1.00 22.95 ? 591  ALA B N   1 
ATOM   9186  C  CA  . ALA B 1 599 ? 8.929   -1.525  63.035  1.00 21.79 ? 591  ALA B CA  1 
ATOM   9187  C  C   . ALA B 1 599 ? 7.646   -1.096  63.741  1.00 25.28 ? 591  ALA B C   1 
ATOM   9188  O  O   . ALA B 1 599 ? 6.552   -1.549  63.380  1.00 20.07 ? 591  ALA B O   1 
ATOM   9189  C  CB  . ALA B 1 599 ? 9.602   -2.666  63.802  1.00 21.76 ? 591  ALA B CB  1 
ATOM   9190  N  N   . ALA B 1 600 ? 7.762   -0.227  64.753  1.00 19.07 ? 592  ALA B N   1 
ATOM   9191  C  CA  . ALA B 1 600 ? 6.580   0.206   65.496  1.00 25.80 ? 592  ALA B CA  1 
ATOM   9192  C  C   . ALA B 1 600 ? 5.583   0.915   64.590  1.00 20.93 ? 592  ALA B C   1 
ATOM   9193  O  O   . ALA B 1 600 ? 4.369   0.686   64.689  1.00 18.89 ? 592  ALA B O   1 
ATOM   9194  C  CB  . ALA B 1 600 ? 6.984   1.120   66.655  1.00 22.47 ? 592  ALA B CB  1 
ATOM   9195  N  N   . TYR B 1 601 ? 6.075   1.783   63.705  1.00 19.28 ? 593  TYR B N   1 
ATOM   9196  C  CA  . TYR B 1 601 ? 5.176   2.469   62.781  1.00 19.53 ? 593  TYR B CA  1 
ATOM   9197  C  C   . TYR B 1 601 ? 4.559   1.499   61.783  1.00 21.38 ? 593  TYR B C   1 
ATOM   9198  O  O   . TYR B 1 601 ? 3.363   1.597   61.472  1.00 16.78 ? 593  TYR B O   1 
ATOM   9199  C  CB  . TYR B 1 601 ? 5.912   3.573   62.024  1.00 19.18 ? 593  TYR B CB  1 
ATOM   9200  C  CG  . TYR B 1 601 ? 4.965   4.326   61.126  1.00 16.33 ? 593  TYR B CG  1 
ATOM   9201  C  CD1 . TYR B 1 601 ? 4.083   5.249   61.660  1.00 23.08 ? 593  TYR B CD1 1 
ATOM   9202  C  CD2 . TYR B 1 601 ? 4.925   4.086   59.754  1.00 15.57 ? 593  TYR B CD2 1 
ATOM   9203  C  CE1 . TYR B 1 601 ? 3.200   5.930   60.861  1.00 22.17 ? 593  TYR B CE1 1 
ATOM   9204  C  CE2 . TYR B 1 601 ? 4.052   4.771   58.939  1.00 15.18 ? 593  TYR B CE2 1 
ATOM   9205  C  CZ  . TYR B 1 601 ? 3.183   5.689   59.507  1.00 18.69 ? 593  TYR B CZ  1 
ATOM   9206  O  OH  . TYR B 1 601 ? 2.291   6.389   58.741  1.00 15.46 ? 593  TYR B OH  1 
ATOM   9207  N  N   . GLN B 1 602 ? 5.356   0.569   61.252  1.00 16.66 ? 594  GLN B N   1 
ATOM   9208  C  CA  . GLN B 1 602 ? 4.805   -0.370  60.277  1.00 18.71 ? 594  GLN B CA  1 
ATOM   9209  C  C   . GLN B 1 602 ? 3.695   -1.211  60.897  1.00 17.35 ? 594  GLN B C   1 
ATOM   9210  O  O   . GLN B 1 602 ? 2.653   -1.436  60.270  1.00 18.26 ? 594  GLN B O   1 
ATOM   9211  C  CB  . GLN B 1 602 ? 5.913   -1.259  59.708  1.00 17.79 ? 594  GLN B CB  1 
ATOM   9212  C  CG  . GLN B 1 602 ? 6.960   -0.493  58.885  1.00 17.78 ? 594  GLN B CG  1 
ATOM   9213  C  CD  . GLN B 1 602 ? 7.791   -1.415  58.027  1.00 23.40 ? 594  GLN B CD  1 
ATOM   9214  O  OE1 . GLN B 1 602 ? 7.273   -2.369  57.443  1.00 28.81 ? 594  GLN B OE1 1 
ATOM   9215  N  NE2 . GLN B 1 602 ? 9.087   -1.143  57.947  1.00 18.46 ? 594  GLN B NE2 1 
ATOM   9216  N  N   . ALA B 1 603 ? 3.894   -1.667  62.136  1.00 19.90 ? 595  ALA B N   1 
ATOM   9217  C  CA  . ALA B 1 603 ? 2.868   -2.451  62.819  1.00 21.53 ? 595  ALA B CA  1 
ATOM   9218  C  C   . ALA B 1 603 ? 1.653   -1.601  63.183  1.00 23.10 ? 595  ALA B C   1 
ATOM   9219  O  O   . ALA B 1 603 ? 0.527   -2.113  63.202  1.00 20.82 ? 595  ALA B O   1 
ATOM   9220  C  CB  . ALA B 1 603 ? 3.456   -3.115  64.066  1.00 22.72 ? 595  ALA B CB  1 
ATOM   9221  N  N   . ALA B 1 604 ? 1.848   -0.312  63.472  1.00 18.40 ? 596  ALA B N   1 
ATOM   9222  C  CA  . ALA B 1 604 ? 0.693   0.532   63.743  1.00 19.04 ? 596  ALA B CA  1 
ATOM   9223  C  C   . ALA B 1 604 ? -0.170  0.692   62.497  1.00 17.90 ? 596  ALA B C   1 
ATOM   9224  O  O   . ALA B 1 604 ? -1.399  0.745   62.603  1.00 20.28 ? 596  ALA B O   1 
ATOM   9225  C  CB  . ALA B 1 604 ? 1.120   1.902   64.272  1.00 18.71 ? 596  ALA B CB  1 
ATOM   9226  N  N   . VAL B 1 605 ? 0.450   0.730   61.317  1.00 17.09 ? 597  VAL B N   1 
ATOM   9227  C  CA  . VAL B 1 605 ? -0.304  0.838   60.069  1.00 17.83 ? 597  VAL B CA  1 
ATOM   9228  C  C   . VAL B 1 605 ? -0.894  -0.510  59.666  1.00 26.03 ? 597  VAL B C   1 
ATOM   9229  O  O   . VAL B 1 605 ? -2.053  -0.585  59.225  1.00 16.51 ? 597  VAL B O   1 
ATOM   9230  C  CB  . VAL B 1 605 ? 0.605   1.419   58.972  1.00 15.68 ? 597  VAL B CB  1 
ATOM   9231  C  CG1 . VAL B 1 605 ? -0.096  1.411   57.598  1.00 15.09 ? 597  VAL B CG1 1 
ATOM   9232  C  CG2 . VAL B 1 605 ? 1.021   2.813   59.346  1.00 15.73 ? 597  VAL B CG2 1 
ATOM   9233  N  N   . LEU B 1 606 ? -0.115  -1.588  59.817  1.00 16.63 ? 598  LEU B N   1 
ATOM   9234  C  CA  . LEU B 1 606 ? -0.515  -2.940  59.410  1.00 20.06 ? 598  LEU B CA  1 
ATOM   9235  C  C   . LEU B 1 606 ? -0.396  -3.874  60.609  1.00 17.58 ? 598  LEU B C   1 
ATOM   9236  O  O   . LEU B 1 606 ? 0.599   -4.598  60.757  1.00 17.68 ? 598  LEU B O   1 
ATOM   9237  C  CB  . LEU B 1 606 ? 0.337   -3.439  58.246  1.00 21.80 ? 598  LEU B CB  1 
ATOM   9238  C  CG  . LEU B 1 606 ? 0.329   -2.623  56.948  1.00 18.24 ? 598  LEU B CG  1 
ATOM   9239  C  CD1 . LEU B 1 606 ? 1.275   -3.256  55.926  1.00 16.60 ? 598  LEU B CD1 1 
ATOM   9240  C  CD2 . LEU B 1 606 ? -1.087  -2.494  56.380  1.00 17.29 ? 598  LEU B CD2 1 
ATOM   9241  N  N   . PRO B 1 607 ? -1.398  -3.890  61.482  1.00 18.29 ? 599  PRO B N   1 
ATOM   9242  C  CA  . PRO B 1 607 ? -1.281  -4.662  62.731  1.00 19.26 ? 599  PRO B CA  1 
ATOM   9243  C  C   . PRO B 1 607 ? -1.083  -6.152  62.483  1.00 21.37 ? 599  PRO B C   1 
ATOM   9244  O  O   . PRO B 1 607 ? -1.684  -6.738  61.581  1.00 19.16 ? 599  PRO B O   1 
ATOM   9245  C  CB  . PRO B 1 607 ? -2.613  -4.387  63.438  1.00 19.93 ? 599  PRO B CB  1 
ATOM   9246  C  CG  . PRO B 1 607 ? -3.064  -3.061  62.900  1.00 22.74 ? 599  PRO B CG  1 
ATOM   9247  C  CD  . PRO B 1 607 ? -2.624  -3.075  61.443  1.00 18.34 ? 599  PRO B CD  1 
ATOM   9248  N  N   . GLU B 1 608 ? -0.245  -6.771  63.315  1.00 22.25 ? 600  GLU B N   1 
ATOM   9249  C  CA  . GLU B 1 608 ? -0.052  -8.210  63.223  1.00 26.18 ? 600  GLU B CA  1 
ATOM   9250  C  C   . GLU B 1 608 ? -1.374  -8.933  63.458  1.00 29.92 ? 600  GLU B C   1 
ATOM   9251  O  O   . GLU B 1 608 ? -2.154  -8.570  64.347  1.00 27.31 ? 600  GLU B O   1 
ATOM   9252  C  CB  . GLU B 1 608 ? 0.996   -8.678  64.237  1.00 26.90 ? 600  GLU B CB  1 
ATOM   9253  N  N   . GLY B 1 609 ? -1.640  -9.947  62.639  1.00 33.85 ? 601  GLY B N   1 
ATOM   9254  C  CA  . GLY B 1 609 ? -2.829  -10.753 62.820  1.00 34.61 ? 601  GLY B CA  1 
ATOM   9255  C  C   . GLY B 1 609 ? -4.093  -10.204 62.197  1.00 33.99 ? 601  GLY B C   1 
ATOM   9256  O  O   . GLY B 1 609 ? -5.137  -10.866 62.270  1.00 31.39 ? 601  GLY B O   1 
ATOM   9257  N  N   . LEU B 1 610 ? -4.046  -9.018  61.597  1.00 25.56 ? 602  LEU B N   1 
ATOM   9258  C  CA  . LEU B 1 610 ? -5.195  -8.491  60.871  1.00 23.78 ? 602  LEU B CA  1 
ATOM   9259  C  C   . LEU B 1 610 ? -5.030  -8.830  59.398  1.00 19.28 ? 602  LEU B C   1 
ATOM   9260  O  O   . LEU B 1 610 ? -4.035  -8.397  58.794  1.00 20.33 ? 602  LEU B O   1 
ATOM   9261  C  CB  . LEU B 1 610 ? -5.301  -6.980  61.063  1.00 23.30 ? 602  LEU B CB  1 
ATOM   9262  C  CG  . LEU B 1 610 ? -6.594  -6.285  60.645  1.00 29.99 ? 602  LEU B CG  1 
ATOM   9263  C  CD1 . LEU B 1 610 ? -7.743  -6.687  61.566  1.00 33.50 ? 602  LEU B CD1 1 
ATOM   9264  C  CD2 . LEU B 1 610 ? -6.409  -4.772  60.634  1.00 27.32 ? 602  LEU B CD2 1 
ATOM   9265  N  N   . PRO B 1 611 ? -5.927  -9.616  58.792  1.00 24.20 ? 603  PRO B N   1 
ATOM   9266  C  CA  . PRO B 1 611 ? -5.760  -9.976  57.375  1.00 22.17 ? 603  PRO B CA  1 
ATOM   9267  C  C   . PRO B 1 611 ? -5.678  -8.744  56.490  1.00 21.05 ? 603  PRO B C   1 
ATOM   9268  O  O   . PRO B 1 611 ? -6.356  -7.741  56.724  1.00 20.91 ? 603  PRO B O   1 
ATOM   9269  C  CB  . PRO B 1 611 ? -7.019  -10.801 57.064  1.00 19.26 ? 603  PRO B CB  1 
ATOM   9270  C  CG  . PRO B 1 611 ? -7.484  -11.308 58.378  1.00 29.51 ? 603  PRO B CG  1 
ATOM   9271  C  CD  . PRO B 1 611 ? -7.115  -10.255 59.388  1.00 27.77 ? 603  PRO B CD  1 
ATOM   9272  N  N   . ARG B 1 612 ? -4.854  -8.836  55.448  1.00 17.07 ? 604  ARG B N   1 
ATOM   9273  C  CA  . ARG B 1 612 ? -4.553  -7.709  54.584  1.00 16.34 ? 604  ARG B CA  1 
ATOM   9274  C  C   . ARG B 1 612 ? -4.961  -8.033  53.155  1.00 23.00 ? 604  ARG B C   1 
ATOM   9275  O  O   . ARG B 1 612 ? -4.722  -9.145  52.668  1.00 15.83 ? 604  ARG B O   1 
ATOM   9276  C  CB  . ARG B 1 612 ? -3.057  -7.361  54.617  1.00 15.76 ? 604  ARG B CB  1 
ATOM   9277  C  CG  . ARG B 1 612 ? -2.507  -7.101  56.022  1.00 18.46 ? 604  ARG B CG  1 
ATOM   9278  C  CD  . ARG B 1 612 ? -0.984  -7.236  56.079  1.00 17.04 ? 604  ARG B CD  1 
ATOM   9279  N  NE  . ARG B 1 612 ? -0.482  -6.998  57.437  1.00 18.32 ? 604  ARG B NE  1 
ATOM   9280  C  CZ  . ARG B 1 612 ? 0.740   -7.319  57.857  1.00 25.08 ? 604  ARG B CZ  1 
ATOM   9281  N  NH1 . ARG B 1 612 ? 1.604   -7.904  57.033  1.00 18.58 ? 604  ARG B NH1 1 
ATOM   9282  N  NH2 . ARG B 1 612 ? 1.099   -7.060  59.107  1.00 23.95 ? 604  ARG B NH2 1 
ATOM   9283  N  N   . ILE B 1 613 ? -5.562  -7.051  52.491  1.00 20.12 ? 605  ILE B N   1 
ATOM   9284  C  CA  . ILE B 1 613 ? -5.952  -7.143  51.089  1.00 19.04 ? 605  ILE B CA  1 
ATOM   9285  C  C   . ILE B 1 613 ? -5.353  -5.949  50.359  1.00 18.38 ? 605  ILE B C   1 
ATOM   9286  O  O   . ILE B 1 613 ? -5.552  -4.804  50.773  1.00 20.54 ? 605  ILE B O   1 
ATOM   9287  C  CB  . ILE B 1 613 ? -7.484  -7.152  50.918  1.00 15.53 ? 605  ILE B CB  1 
ATOM   9288  C  CG1 . ILE B 1 613 ? -8.113  -8.319  51.693  1.00 22.04 ? 605  ILE B CG1 1 
ATOM   9289  C  CG2 . ILE B 1 613 ? -7.857  -7.194  49.450  1.00 20.25 ? 605  ILE B CG2 1 
ATOM   9290  C  CD1 . ILE B 1 613 ? -8.494  -7.964  53.144  1.00 23.02 ? 605  ILE B CD1 1 
ATOM   9291  N  N   . ALA B 1 614 ? -4.634  -6.205  49.275  1.00 14.13 ? 606  ALA B N   1 
ATOM   9292  C  CA  . ALA B 1 614 ? -4.024  -5.136  48.500  1.00 13.18 ? 606  ALA B CA  1 
ATOM   9293  C  C   . ALA B 1 614 ? -4.836  -4.922  47.230  1.00 14.60 ? 606  ALA B C   1 
ATOM   9294  O  O   . ALA B 1 614 ? -5.304  -5.888  46.620  1.00 17.38 ? 606  ALA B O   1 
ATOM   9295  C  CB  . ALA B 1 614 ? -2.568  -5.471  48.155  1.00 15.74 ? 606  ALA B CB  1 
ATOM   9296  N  N   . VAL B 1 615 ? -5.040  -3.656  46.858  1.00 12.83 ? 607  VAL B N   1 
ATOM   9297  C  CA  . VAL B 1 615 ? -5.802  -3.296  45.663  1.00 16.07 ? 607  VAL B CA  1 
ATOM   9298  C  C   . VAL B 1 615 ? -4.987  -2.298  44.846  1.00 15.07 ? 607  VAL B C   1 
ATOM   9299  O  O   . VAL B 1 615 ? -4.739  -1.173  45.298  1.00 12.18 ? 607  VAL B O   1 
ATOM   9300  C  CB  . VAL B 1 615 ? -7.187  -2.703  46.000  1.00 13.27 ? 607  VAL B CB  1 
ATOM   9301  C  CG1 . VAL B 1 615 ? -7.963  -2.473  44.728  1.00 15.15 ? 607  VAL B CG1 1 
ATOM   9302  C  CG2 . VAL B 1 615 ? -7.982  -3.625  46.922  1.00 13.87 ? 607  VAL B CG2 1 
ATOM   9303  N  N   . GLU B 1 616 ? -4.583  -2.704  43.642  1.00 13.82 ? 608  GLU B N   1 
ATOM   9304  C  CA  . GLU B 1 616 ? -3.748  -1.880  42.781  1.00 12.62 ? 608  GLU B CA  1 
ATOM   9305  C  C   . GLU B 1 616 ? -3.904  -2.401  41.365  1.00 11.42 ? 608  GLU B C   1 
ATOM   9306  O  O   . GLU B 1 616 ? -3.825  -3.611  41.150  1.00 12.84 ? 608  GLU B O   1 
ATOM   9307  C  CB  . GLU B 1 616 ? -2.277  -1.946  43.219  1.00 13.45 ? 608  GLU B CB  1 
ATOM   9308  C  CG  . GLU B 1 616 ? -1.320  -1.166  42.321  1.00 11.79 ? 608  GLU B CG  1 
ATOM   9309  C  CD  . GLU B 1 616 ? 0.063   -1.092  42.931  1.00 12.25 ? 608  GLU B CD  1 
ATOM   9310  O  OE1 . GLU B 1 616 ? 0.812   -2.088  42.844  1.00 12.65 ? 608  GLU B OE1 1 
ATOM   9311  O  OE2 . GLU B 1 616 ? 0.383   -0.042  43.516  1.00 12.49 ? 608  GLU B OE2 1 
ATOM   9312  N  N   . ALA B 1 617 ? -4.097  -1.498  40.402  1.00 11.37 ? 609  ALA B N   1 
ATOM   9313  C  CA  . ALA B 1 617 ? -4.324  -1.923  39.021  1.00 12.46 ? 609  ALA B CA  1 
ATOM   9314  C  C   . ALA B 1 617 ? -2.988  -2.273  38.357  1.00 16.97 ? 609  ALA B C   1 
ATOM   9315  O  O   . ALA B 1 617 ? -2.512  -1.621  37.425  1.00 14.76 ? 609  ALA B O   1 
ATOM   9316  C  CB  . ALA B 1 617 ? -5.096  -0.858  38.254  1.00 11.60 ? 609  ALA B CB  1 
ATOM   9317  N  N   . GLY B 1 618 ? -2.386  -3.341  38.861  1.00 15.60 ? 610  GLY B N   1 
ATOM   9318  C  CA  . GLY B 1 618 ? -1.132  -3.824  38.322  1.00 13.95 ? 610  GLY B CA  1 
ATOM   9319  C  C   . GLY B 1 618 ? -0.805  -5.189  38.885  1.00 12.77 ? 610  GLY B C   1 
ATOM   9320  O  O   . GLY B 1 618 ? -1.599  -5.782  39.629  1.00 12.19 ? 610  GLY B O   1 
ATOM   9321  N  N   . HIS B 1 619 ? 0.404   -5.657  38.560  1.00 13.14 ? 611  HIS B N   1 
ATOM   9322  C  CA  . HIS B 1 619 ? 0.813   -7.005  38.927  1.00 11.59 ? 611  HIS B CA  1 
ATOM   9323  C  C   . HIS B 1 619 ? 0.664   -7.221  40.427  1.00 12.08 ? 611  HIS B C   1 
ATOM   9324  O  O   . HIS B 1 619 ? 0.916   -6.317  41.231  1.00 16.31 ? 611  HIS B O   1 
ATOM   9325  C  CB  . HIS B 1 619 ? 2.266   -7.268  38.502  1.00 10.17 ? 611  HIS B CB  1 
ATOM   9326  C  CG  . HIS B 1 619 ? 2.540   -8.701  38.160  1.00 12.21 ? 611  HIS B CG  1 
ATOM   9327  N  ND1 . HIS B 1 619 ? 2.692   -9.681  39.117  1.00 11.20 ? 611  HIS B ND1 1 
ATOM   9328  C  CD2 . HIS B 1 619 ? 2.658   -9.323  36.963  1.00 11.51 ? 611  HIS B CD2 1 
ATOM   9329  C  CE1 . HIS B 1 619 ? 2.903   -10.845 38.525  1.00 16.09 ? 611  HIS B CE1 1 
ATOM   9330  N  NE2 . HIS B 1 619 ? 2.895   -10.652 37.216  1.00 13.24 ? 611  HIS B NE2 1 
ATOM   9331  N  N   . THR B 1 620 ? 0.263   -8.434  40.800  1.00 10.99 ? 612  THR B N   1 
ATOM   9332  C  CA  . THR B 1 620 ? 0.020   -8.752  42.208  1.00 12.62 ? 612  THR B CA  1 
ATOM   9333  C  C   . THR B 1 620 ? 1.248   -9.241  42.965  1.00 14.24 ? 612  THR B C   1 
ATOM   9334  O  O   . THR B 1 620 ? 1.245   -9.194  44.199  1.00 14.49 ? 612  THR B O   1 
ATOM   9335  C  CB  . THR B 1 620 ? -1.039  -9.855  42.352  1.00 13.82 ? 612  THR B CB  1 
ATOM   9336  O  OG1 . THR B 1 620 ? -0.511  -11.078 41.828  1.00 13.12 ? 612  THR B OG1 1 
ATOM   9337  C  CG2 . THR B 1 620 ? -2.357  -9.488  41.629  1.00 14.71 ? 612  THR B CG2 1 
ATOM   9338  N  N   . ASN B 1 621 ? 2.292   -9.712  42.275  1.00 12.51 ? 613  ASN B N   1 
ATOM   9339  C  CA  A ASN B 1 621 ? 3.216   -10.582 42.980  0.41 16.96 ? 613  ASN B CA  1 
ATOM   9340  C  CA  B ASN B 1 621 ? 3.319   -10.551 42.914  0.59 17.63 ? 613  ASN B CA  1 
ATOM   9341  C  C   . ASN B 1 621 ? 3.989   -9.846  44.079  1.00 18.28 ? 613  ASN B C   1 
ATOM   9342  O  O   . ASN B 1 621 ? 4.319   -10.466 45.099  1.00 16.39 ? 613  ASN B O   1 
ATOM   9343  C  CB  A ASN B 1 621 ? 4.126   -11.295 41.969  0.41 18.78 ? 613  ASN B CB  1 
ATOM   9344  C  CB  B ASN B 1 621 ? 4.391   -10.959 41.904  0.59 16.98 ? 613  ASN B CB  1 
ATOM   9345  C  CG  A ASN B 1 621 ? 3.434   -12.515 41.325  0.41 19.96 ? 613  ASN B CG  1 
ATOM   9346  C  CG  B ASN B 1 621 ? 5.618   -11.564 42.583  0.59 16.71 ? 613  ASN B CG  1 
ATOM   9347  O  OD1 A ASN B 1 621 ? 2.222   -12.714 41.478  0.41 22.85 ? 613  ASN B OD1 1 
ATOM   9348  O  OD1 B ASN B 1 621 ? 6.564   -10.859 42.950  0.59 20.55 ? 613  ASN B OD1 1 
ATOM   9349  N  ND2 A ASN B 1 621 ? 4.203   -13.334 40.616  0.41 16.29 ? 613  ASN B ND2 1 
ATOM   9350  N  ND2 B ASN B 1 621 ? 5.599   -12.871 42.762  0.59 19.66 ? 613  ASN B ND2 1 
ATOM   9351  N  N   . GLY B 1 622 ? 4.252   -8.546  43.926  1.00 18.84 ? 614  GLY B N   1 
ATOM   9352  C  CA  . GLY B 1 622 ? 4.945   -7.810  44.970  1.00 19.88 ? 614  GLY B CA  1 
ATOM   9353  C  C   . GLY B 1 622 ? 4.155   -7.660  46.255  1.00 21.18 ? 614  GLY B C   1 
ATOM   9354  O  O   . GLY B 1 622 ? 4.748   -7.459  47.321  1.00 19.90 ? 614  GLY B O   1 
ATOM   9355  N  N   . TRP B 1 623 ? 2.831   -7.752  46.185  1.00 11.54 ? 615  TRP B N   1 
ATOM   9356  C  CA  . TRP B 1 623 ? 2.039   -7.468  47.367  1.00 14.26 ? 615  TRP B CA  1 
ATOM   9357  C  C   . TRP B 1 623 ? 2.048   -8.609  48.370  1.00 20.42 ? 615  TRP B C   1 
ATOM   9358  O  O   . TRP B 1 623 ? 1.640   -8.404  49.517  1.00 20.21 ? 615  TRP B O   1 
ATOM   9359  C  CB  . TRP B 1 623 ? 0.600   -7.119  46.956  1.00 12.78 ? 615  TRP B CB  1 
ATOM   9360  C  CG  . TRP B 1 623 ? 0.564   -5.776  46.351  1.00 14.36 ? 615  TRP B CG  1 
ATOM   9361  C  CD1 . TRP B 1 623 ? 0.396   -5.469  45.033  1.00 11.26 ? 615  TRP B CD1 1 
ATOM   9362  C  CD2 . TRP B 1 623 ? 0.778   -4.538  47.033  1.00 13.63 ? 615  TRP B CD2 1 
ATOM   9363  N  NE1 . TRP B 1 623 ? 0.468   -4.106  44.860  1.00 17.18 ? 615  TRP B NE1 1 
ATOM   9364  C  CE2 . TRP B 1 623 ? 0.694   -3.515  46.078  1.00 15.63 ? 615  TRP B CE2 1 
ATOM   9365  C  CE3 . TRP B 1 623 ? 1.011   -4.197  48.371  1.00 14.19 ? 615  TRP B CE3 1 
ATOM   9366  C  CZ2 . TRP B 1 623 ? 0.842   -2.171  46.409  1.00 12.82 ? 615  TRP B CZ2 1 
ATOM   9367  C  CZ3 . TRP B 1 623 ? 1.154   -2.859  48.703  1.00 14.73 ? 615  TRP B CZ3 1 
ATOM   9368  C  CH2 . TRP B 1 623 ? 1.072   -1.862  47.728  1.00 11.40 ? 615  TRP B CH2 1 
ATOM   9369  N  N   . TYR B 1 624 ? 2.502   -9.798  47.973  1.00 12.62 ? 616  TYR B N   1 
ATOM   9370  C  CA  . TYR B 1 624 ? 2.548   -10.904 48.921  1.00 16.90 ? 616  TYR B CA  1 
ATOM   9371  C  C   . TYR B 1 624 ? 3.537   -10.636 50.043  1.00 14.22 ? 616  TYR B C   1 
ATOM   9372  O  O   . TYR B 1 624 ? 3.422   -11.235 51.117  1.00 15.05 ? 616  TYR B O   1 
ATOM   9373  C  CB  . TYR B 1 624 ? 2.888   -12.206 48.197  1.00 14.89 ? 616  TYR B CB  1 
ATOM   9374  C  CG  . TYR B 1 624 ? 1.718   -12.675 47.367  1.00 18.32 ? 616  TYR B CG  1 
ATOM   9375  C  CD1 . TYR B 1 624 ? 0.631   -13.306 47.965  1.00 20.37 ? 616  TYR B CD1 1 
ATOM   9376  C  CD2 . TYR B 1 624 ? 1.671   -12.432 46.003  1.00 17.44 ? 616  TYR B CD2 1 
ATOM   9377  C  CE1 . TYR B 1 624 ? -0.459  -13.709 47.214  1.00 22.93 ? 616  TYR B CE1 1 
ATOM   9378  C  CE2 . TYR B 1 624 ? 0.590   -12.830 45.245  1.00 19.22 ? 616  TYR B CE2 1 
ATOM   9379  C  CZ  . TYR B 1 624 ? -0.470  -13.470 45.850  1.00 25.04 ? 616  TYR B CZ  1 
ATOM   9380  O  OH  . TYR B 1 624 ? -1.555  -13.866 45.088  1.00 25.74 ? 616  TYR B OH  1 
ATOM   9381  N  N   . LYS B 1 625 ? 4.489   -9.735  49.825  1.00 14.68 ? 617  LYS B N   1 
ATOM   9382  C  CA  . LYS B 1 625 ? 5.393   -9.364  50.908  1.00 14.48 ? 617  LYS B CA  1 
ATOM   9383  C  C   . LYS B 1 625 ? 4.621   -8.797  52.089  1.00 15.68 ? 617  LYS B C   1 
ATOM   9384  O  O   . LYS B 1 625 ? 5.028   -8.972  53.246  1.00 17.71 ? 617  LYS B O   1 
ATOM   9385  C  CB  . LYS B 1 625 ? 6.429   -8.363  50.405  1.00 14.59 ? 617  LYS B CB  1 
ATOM   9386  C  CG  . LYS B 1 625 ? 7.414   -7.889  51.473  1.00 23.20 ? 617  LYS B CG  1 
ATOM   9387  C  CD  . LYS B 1 625 ? 8.404   -6.924  50.855  1.00 26.68 ? 617  LYS B CD  1 
ATOM   9388  C  CE  . LYS B 1 625 ? 8.660   -5.714  51.731  1.00 37.46 ? 617  LYS B CE  1 
ATOM   9389  N  NZ  . LYS B 1 625 ? 9.723   -4.857  51.114  1.00 37.68 ? 617  LYS B NZ  1 
ATOM   9390  N  N   . TYR B 1 626 ? 3.493   -8.144  51.819  1.00 14.38 ? 618  TYR B N   1 
ATOM   9391  C  CA  . TYR B 1 626 ? 2.629   -7.594  52.851  1.00 17.57 ? 618  TYR B CA  1 
ATOM   9392  C  C   . TYR B 1 626 ? 1.459   -8.506  53.197  1.00 18.24 ? 618  TYR B C   1 
ATOM   9393  O  O   . TYR B 1 626 ? 1.163   -8.691  54.377  1.00 18.30 ? 618  TYR B O   1 
ATOM   9394  C  CB  . TYR B 1 626 ? 2.110   -6.213  52.419  1.00 17.09 ? 618  TYR B CB  1 
ATOM   9395  C  CG  . TYR B 1 626 ? 3.211   -5.253  52.006  1.00 22.00 ? 618  TYR B CG  1 
ATOM   9396  C  CD1 . TYR B 1 626 ? 3.947   -4.552  52.957  1.00 27.01 ? 618  TYR B CD1 1 
ATOM   9397  C  CD2 . TYR B 1 626 ? 3.527   -5.063  50.663  1.00 23.96 ? 618  TYR B CD2 1 
ATOM   9398  C  CE1 . TYR B 1 626 ? 4.966   -3.680  52.580  1.00 23.86 ? 618  TYR B CE1 1 
ATOM   9399  C  CE2 . TYR B 1 626 ? 4.540   -4.196  50.277  1.00 27.70 ? 618  TYR B CE2 1 
ATOM   9400  C  CZ  . TYR B 1 626 ? 5.257   -3.507  51.238  1.00 26.95 ? 618  TYR B CZ  1 
ATOM   9401  O  OH  . TYR B 1 626 ? 6.266   -2.638  50.852  1.00 29.86 ? 618  TYR B OH  1 
ATOM   9402  N  N   . VAL B 1 627 ? 0.794   -9.111  52.208  1.00 18.96 ? 619  VAL B N   1 
ATOM   9403  C  CA  . VAL B 1 627 ? -0.437  -9.845  52.503  1.00 20.87 ? 619  VAL B CA  1 
ATOM   9404  C  C   . VAL B 1 627 ? -0.204  -11.322 52.807  1.00 19.61 ? 619  VAL B C   1 
ATOM   9405  O  O   . VAL B 1 627 ? -1.074  -11.960 53.427  1.00 17.04 ? 619  VAL B O   1 
ATOM   9406  C  CB  . VAL B 1 627 ? -1.465  -9.716  51.360  1.00 19.95 ? 619  VAL B CB  1 
ATOM   9407  C  CG1 . VAL B 1 627 ? -1.641  -8.255  50.961  1.00 18.74 ? 619  VAL B CG1 1 
ATOM   9408  C  CG2 . VAL B 1 627 ? -1.072  -10.580 50.172  1.00 14.29 ? 619  VAL B CG2 1 
ATOM   9409  N  N   . GLY B 1 628 ? 0.940   -11.885 52.397  1.00 19.90 ? 620  GLY B N   1 
ATOM   9410  C  CA  . GLY B 1 628 ? 1.255   -13.252 52.773  1.00 19.54 ? 620  GLY B CA  1 
ATOM   9411  C  C   . GLY B 1 628 ? 0.354   -14.262 52.080  1.00 19.89 ? 620  GLY B C   1 
ATOM   9412  O  O   . GLY B 1 628 ? -0.420  -13.945 51.180  1.00 25.27 ? 620  GLY B O   1 
ATOM   9413  N  N   . LEU B 1 629 ? 0.468   -15.509 52.531  1.00 18.29 ? 621  LEU B N   1 
ATOM   9414  C  CA  . LEU B 1 629 ? -0.244  -16.598 51.880  1.00 22.99 ? 621  LEU B CA  1 
ATOM   9415  C  C   . LEU B 1 629 ? -1.724  -16.630 52.226  1.00 25.37 ? 621  LEU B C   1 
ATOM   9416  O  O   . LEU B 1 629 ? -2.493  -17.298 51.531  1.00 29.35 ? 621  LEU B O   1 
ATOM   9417  C  CB  . LEU B 1 629 ? 0.395   -17.934 52.257  1.00 21.70 ? 621  LEU B CB  1 
ATOM   9418  C  CG  . LEU B 1 629 ? 1.894   -17.980 51.960  1.00 23.07 ? 621  LEU B CG  1 
ATOM   9419  C  CD1 . LEU B 1 629 ? 2.545   -19.178 52.634  1.00 27.46 ? 621  LEU B CD1 1 
ATOM   9420  C  CD2 . LEU B 1 629 ? 2.140   -17.997 50.460  1.00 24.87 ? 621  LEU B CD2 1 
ATOM   9421  N  N   . ASN B 1 630 ? -2.140  -15.931 53.279  1.00 21.14 ? 622  ASN B N   1 
ATOM   9422  C  CA  . ASN B 1 630 ? -3.533  -15.942 53.699  1.00 28.49 ? 622  ASN B CA  1 
ATOM   9423  C  C   . ASN B 1 630 ? -4.264  -14.642 53.409  1.00 24.89 ? 622  ASN B C   1 
ATOM   9424  O  O   . ASN B 1 630 ? -5.464  -14.562 53.667  1.00 22.05 ? 622  ASN B O   1 
ATOM   9425  C  CB  . ASN B 1 630 ? -3.630  -16.258 55.197  1.00 32.55 ? 622  ASN B CB  1 
ATOM   9426  C  CG  . ASN B 1 630 ? -3.142  -17.654 55.523  1.00 38.60 ? 622  ASN B CG  1 
ATOM   9427  O  OD1 . ASN B 1 630 ? -3.497  -18.620 54.847  1.00 36.12 ? 622  ASN B OD1 1 
ATOM   9428  N  ND2 . ASN B 1 630 ? -2.317  -17.768 56.556  1.00 44.05 ? 622  ASN B ND2 1 
ATOM   9429  N  N   . GLY B 1 631 ? -3.577  -13.625 52.910  1.00 25.96 ? 623  GLY B N   1 
ATOM   9430  C  CA  . GLY B 1 631 ? -4.214  -12.411 52.453  1.00 22.26 ? 623  GLY B CA  1 
ATOM   9431  C  C   . GLY B 1 631 ? -4.653  -12.564 51.014  1.00 20.81 ? 623  GLY B C   1 
ATOM   9432  O  O   . GLY B 1 631 ? -4.809  -13.672 50.496  1.00 21.87 ? 623  GLY B O   1 
ATOM   9433  N  N   . ALA B 1 632 ? -4.858  -11.429 50.360  1.00 16.40 ? 624  ALA B N   1 
ATOM   9434  C  CA  . ALA B 1 632 ? -5.353  -11.461 48.993  1.00 15.99 ? 624  ALA B CA  1 
ATOM   9435  C  C   . ALA B 1 632 ? -4.948  -10.181 48.282  1.00 15.62 ? 624  ALA B C   1 
ATOM   9436  O  O   . ALA B 1 632 ? -4.591  -9.176  48.909  1.00 15.80 ? 624  ALA B O   1 
ATOM   9437  C  CB  . ALA B 1 632 ? -6.875  -11.657 48.957  1.00 15.87 ? 624  ALA B CB  1 
ATOM   9438  N  N   . VAL B 1 633 ? -4.988  -10.236 46.954  1.00 16.37 ? 625  VAL B N   1 
ATOM   9439  C  CA  . VAL B 1 633 ? -4.643  -9.090  46.121  1.00 14.85 ? 625  VAL B CA  1 
ATOM   9440  C  C   . VAL B 1 633 ? -5.703  -8.941  45.040  1.00 17.82 ? 625  VAL B C   1 
ATOM   9441  O  O   . VAL B 1 633 ? -6.088  -9.926  44.401  1.00 18.24 ? 625  VAL B O   1 
ATOM   9442  C  CB  . VAL B 1 633 ? -3.250  -9.228  45.466  1.00 14.56 ? 625  VAL B CB  1 
ATOM   9443  C  CG1 . VAL B 1 633 ? -2.864  -7.918  44.801  1.00 17.07 ? 625  VAL B CG1 1 
ATOM   9444  C  CG2 . VAL B 1 633 ? -2.176  -9.644  46.476  1.00 15.67 ? 625  VAL B CG2 1 
ATOM   9445  N  N   . VAL B 1 634 ? -6.158  -7.712  44.814  1.00 14.43 ? 626  VAL B N   1 
ATOM   9446  C  CA  . VAL B 1 634 ? -6.953  -7.389  43.638  1.00 15.90 ? 626  VAL B CA  1 
ATOM   9447  C  C   . VAL B 1 634 ? -6.019  -6.655  42.678  1.00 16.05 ? 626  VAL B C   1 
ATOM   9448  O  O   . VAL B 1 634 ? -5.688  -5.486  42.880  1.00 14.82 ? 626  VAL B O   1 
ATOM   9449  C  CB  . VAL B 1 634 ? -8.190  -6.562  43.986  1.00 13.77 ? 626  VAL B CB  1 
ATOM   9450  C  CG1 . VAL B 1 634 ? -8.997  -6.298  42.733  1.00 14.93 ? 626  VAL B CG1 1 
ATOM   9451  C  CG2 . VAL B 1 634 ? -9.029  -7.289  45.047  1.00 14.46 ? 626  VAL B CG2 1 
ATOM   9452  N  N   . GLY B 1 635 ? -5.586  -7.351  41.633  1.00 14.90 ? 627  GLY B N   1 
ATOM   9453  C  CA  . GLY B 1 635 ? -4.650  -6.782  40.689  1.00 13.11 ? 627  GLY B CA  1 
ATOM   9454  C  C   . GLY B 1 635 ? -4.869  -7.323  39.294  1.00 12.95 ? 627  GLY B C   1 
ATOM   9455  O  O   . GLY B 1 635 ? -5.945  -7.848  38.970  1.00 13.04 ? 627  GLY B O   1 
ATOM   9456  N  N   . ILE B 1 636 ? -3.840  -7.209  38.460  1.00 13.79 ? 628  ILE B N   1 
ATOM   9457  C  CA  . ILE B 1 636 ? -3.925  -7.685  37.092  1.00 13.59 ? 628  ILE B CA  1 
ATOM   9458  C  C   . ILE B 1 636 ? -2.559  -8.213  36.657  1.00 11.75 ? 628  ILE B C   1 
ATOM   9459  O  O   . ILE B 1 636 ? -1.537  -7.523  36.782  1.00 11.49 ? 628  ILE B O   1 
ATOM   9460  C  CB  . ILE B 1 636 ? -4.464  -6.572  36.175  1.00 18.64 ? 628  ILE B CB  1 
ATOM   9461  C  CG1 . ILE B 1 636 ? -4.374  -6.982  34.707  1.00 14.80 ? 628  ILE B CG1 1 
ATOM   9462  C  CG2 . ILE B 1 636 ? -3.785  -5.237  36.457  1.00 25.31 ? 628  ILE B CG2 1 
ATOM   9463  C  CD1 . ILE B 1 636 ? -4.951  -5.911  33.796  1.00 23.56 ? 628  ILE B CD1 1 
ATOM   9464  N  N   . ASN B 1 637 ? -2.530  -9.470  36.201  1.00 12.49 ? 629  ASN B N   1 
ATOM   9465  C  CA  . ASN B 1 637 ? -1.285  -10.168 35.873  1.00 11.95 ? 629  ASN B CA  1 
ATOM   9466  C  C   . ASN B 1 637 ? -1.206  -10.542 34.400  1.00 16.40 ? 629  ASN B C   1 
ATOM   9467  O  O   . ASN B 1 637 ? -0.329  -11.322 34.007  1.00 18.29 ? 629  ASN B O   1 
ATOM   9468  C  CB  . ASN B 1 637 ? -1.123  -11.436 36.720  1.00 13.21 ? 629  ASN B CB  1 
ATOM   9469  C  CG  . ASN B 1 637 ? -0.866  -11.131 38.175  1.00 18.95 ? 629  ASN B CG  1 
ATOM   9470  O  OD1 . ASN B 1 637 ? -0.650  -9.979  38.533  1.00 17.44 ? 629  ASN B OD1 1 
ATOM   9471  N  ND2 . ASN B 1 637 ? -0.859  -12.162 39.020  1.00 19.83 ? 629  ASN B ND2 1 
ATOM   9472  N  N   . ARG B 1 638 ? -2.108  -10.024 33.584  1.00 14.08 ? 630  ARG B N   1 
ATOM   9473  C  CA  . ARG B 1 638 ? -2.110  -10.294 32.161  1.00 14.41 ? 630  ARG B CA  1 
ATOM   9474  C  C   . ARG B 1 638 ? -2.104  -8.971  31.414  1.00 13.63 ? 630  ARG B C   1 
ATOM   9475  O  O   . ARG B 1 638 ? -2.279  -7.896  32.000  1.00 13.46 ? 630  ARG B O   1 
ATOM   9476  C  CB  . ARG B 1 638 ? -3.321  -11.145 31.757  1.00 22.50 ? 630  ARG B CB  1 
ATOM   9477  C  CG  . ARG B 1 638 ? -4.662  -10.529 32.090  1.00 26.28 ? 630  ARG B CG  1 
ATOM   9478  C  CD  . ARG B 1 638 ? -5.771  -11.457 31.603  1.00 41.08 ? 630  ARG B CD  1 
ATOM   9479  N  NE  . ARG B 1 638 ? -7.073  -10.799 31.538  1.00 54.65 ? 630  ARG B NE  1 
ATOM   9480  C  CZ  . ARG B 1 638 ? -8.057  -10.993 32.411  1.00 64.15 ? 630  ARG B CZ  1 
ATOM   9481  N  NH1 . ARG B 1 638 ? -7.895  -11.832 33.426  1.00 66.12 ? 630  ARG B NH1 1 
ATOM   9482  N  NH2 . ARG B 1 638 ? -9.208  -10.350 32.267  1.00 68.17 ? 630  ARG B NH2 1 
ATOM   9483  N  N   . PHE B 1 639 ? -1.872  -9.054  30.109  1.00 10.40 ? 631  PHE B N   1 
ATOM   9484  C  CA  . PHE B 1 639 ? -1.847  -7.838  29.309  1.00 10.67 ? 631  PHE B CA  1 
ATOM   9485  C  C   . PHE B 1 639 ? -3.236  -7.216  29.246  1.00 16.13 ? 631  PHE B C   1 
ATOM   9486  O  O   . PHE B 1 639 ? -4.254  -7.887  29.436  1.00 14.20 ? 631  PHE B O   1 
ATOM   9487  C  CB  . PHE B 1 639 ? -1.351  -8.124  27.892  1.00 12.01 ? 631  PHE B CB  1 
ATOM   9488  C  CG  . PHE B 1 639 ? 0.092   -8.551  27.831  1.00 11.68 ? 631  PHE B CG  1 
ATOM   9489  C  CD1 . PHE B 1 639 ? 1.099   -7.643  28.106  1.00 13.12 ? 631  PHE B CD1 1 
ATOM   9490  C  CD2 . PHE B 1 639 ? 0.429   -9.841  27.480  1.00 13.92 ? 631  PHE B CD2 1 
ATOM   9491  C  CE1 . PHE B 1 639 ? 2.428   -8.032  28.044  1.00 15.57 ? 631  PHE B CE1 1 
ATOM   9492  C  CE2 . PHE B 1 639 ? 1.753   -10.236 27.422  1.00 15.69 ? 631  PHE B CE2 1 
ATOM   9493  C  CZ  . PHE B 1 639 ? 2.746   -9.324  27.691  1.00 9.90  ? 631  PHE B CZ  1 
ATOM   9494  N  N   . GLY B 1 640 ? -3.268  -5.916  28.966  1.00 11.34 ? 632  GLY B N   1 
ATOM   9495  C  CA  . GLY B 1 640 ? -4.515  -5.179  28.910  1.00 15.33 ? 632  GLY B CA  1 
ATOM   9496  C  C   . GLY B 1 640 ? -5.307  -5.417  27.634  1.00 14.06 ? 632  GLY B C   1 
ATOM   9497  O  O   . GLY B 1 640 ? -5.146  -6.417  26.934  1.00 14.56 ? 632  GLY B O   1 
ATOM   9498  N  N   . GLU B 1 641 ? -6.176  -4.459  27.329  1.00 14.29 ? 633  GLU B N   1 
ATOM   9499  C  CA  . GLU B 1 641 ? -7.113  -4.551  26.218  1.00 17.51 ? 633  GLU B CA  1 
ATOM   9500  C  C   . GLU B 1 641 ? -7.398  -3.152  25.704  1.00 13.79 ? 633  GLU B C   1 
ATOM   9501  O  O   . GLU B 1 641 ? -7.509  -2.213  26.495  1.00 14.67 ? 633  GLU B O   1 
ATOM   9502  C  CB  . GLU B 1 641 ? -8.450  -5.192  26.634  1.00 19.89 ? 633  GLU B CB  1 
ATOM   9503  C  CG  . GLU B 1 641 ? -8.412  -6.688  26.862  1.00 21.42 ? 633  GLU B CG  1 
ATOM   9504  C  CD  . GLU B 1 641 ? -8.135  -7.495  25.603  1.00 21.98 ? 633  GLU B CD  1 
ATOM   9505  O  OE1 . GLU B 1 641 ? -8.299  -6.975  24.471  1.00 18.17 ? 633  GLU B OE1 1 
ATOM   9506  O  OE2 . GLU B 1 641 ? -7.748  -8.669  25.760  1.00 23.23 ? 633  GLU B OE2 1 
ATOM   9507  N  N   . SER B 1 642 ? -7.546  -3.018  24.385  1.00 11.13 ? 634  SER B N   1 
ATOM   9508  C  CA  . SER B 1 642 ? -7.979  -1.753  23.807  1.00 11.35 ? 634  SER B CA  1 
ATOM   9509  C  C   . SER B 1 642 ? -9.483  -1.605  24.013  1.00 14.52 ? 634  SER B C   1 
ATOM   9510  O  O   . SER B 1 642 ? -10.274 -2.299  23.367  1.00 16.91 ? 634  SER B O   1 
ATOM   9511  C  CB  . SER B 1 642 ? -7.623  -1.693  22.329  1.00 15.13 ? 634  SER B CB  1 
ATOM   9512  O  OG  . SER B 1 642 ? -8.035  -0.466  21.768  1.00 14.96 ? 634  SER B OG  1 
ATOM   9513  N  N   . ALA B 1 643 ? -9.873  -0.683  24.896  1.00 15.02 ? 635  ALA B N   1 
ATOM   9514  C  CA  . ALA B 1 643 ? -11.263 -0.348  25.184  1.00 13.40 ? 635  ALA B CA  1 
ATOM   9515  C  C   . ALA B 1 643 ? -11.321 0.914   26.041  1.00 15.32 ? 635  ALA B C   1 
ATOM   9516  O  O   . ALA B 1 643 ? -10.284 1.334   26.574  1.00 14.98 ? 635  ALA B O   1 
ATOM   9517  C  CB  . ALA B 1 643 ? -11.951 -1.506  25.911  1.00 15.57 ? 635  ALA B CB  1 
ATOM   9518  N  N   . PRO B 1 644 ? -12.496 1.537   26.205  1.00 14.30 ? 636  PRO B N   1 
ATOM   9519  C  CA  . PRO B 1 644 ? -12.621 2.638   27.172  1.00 14.49 ? 636  PRO B CA  1 
ATOM   9520  C  C   . PRO B 1 644 ? -12.244 2.199   28.579  1.00 17.07 ? 636  PRO B C   1 
ATOM   9521  O  O   . PRO B 1 644 ? -12.480 1.058   28.984  1.00 15.86 ? 636  PRO B O   1 
ATOM   9522  C  CB  . PRO B 1 644 ? -14.101 3.019   27.086  1.00 20.59 ? 636  PRO B CB  1 
ATOM   9523  C  CG  . PRO B 1 644 ? -14.506 2.626   25.677  1.00 20.95 ? 636  PRO B CG  1 
ATOM   9524  C  CD  . PRO B 1 644 ? -13.715 1.377   25.386  1.00 15.29 ? 636  PRO B CD  1 
ATOM   9525  N  N   . ALA B 1 645 ? -11.665 3.138   29.334  1.00 17.58 ? 637  ALA B N   1 
ATOM   9526  C  CA  . ALA B 1 645 ? -11.127 2.819   30.657  1.00 13.55 ? 637  ALA B CA  1 
ATOM   9527  C  C   . ALA B 1 645 ? -12.193 2.284   31.605  1.00 16.87 ? 637  ALA B C   1 
ATOM   9528  O  O   . ALA B 1 645 ? -11.922 1.382   32.400  1.00 15.59 ? 637  ALA B O   1 
ATOM   9529  C  CB  . ALA B 1 645 ? -10.467 4.051   31.272  1.00 16.80 ? 637  ALA B CB  1 
ATOM   9530  N  N   . ASP B 1 646 ? -13.402 2.844   31.573  1.00 20.21 ? 638  ASP B N   1 
ATOM   9531  C  CA  . ASP B 1 646 ? -14.396 2.382   32.540  1.00 18.96 ? 638  ASP B CA  1 
ATOM   9532  C  C   . ASP B 1 646 ? -14.754 0.917   32.302  1.00 18.22 ? 638  ASP B C   1 
ATOM   9533  O  O   . ASP B 1 646 ? -14.913 0.146   33.258  1.00 15.84 ? 638  ASP B O   1 
ATOM   9534  C  CB  . ASP B 1 646 ? -15.639 3.278   32.524  1.00 22.95 ? 638  ASP B CB  1 
ATOM   9535  C  CG  . ASP B 1 646 ? -16.278 3.422   31.145  1.00 30.66 ? 638  ASP B CG  1 
ATOM   9536  O  OD1 . ASP B 1 646 ? -15.715 2.961   30.131  1.00 29.28 ? 638  ASP B OD1 1 
ATOM   9537  O  OD2 . ASP B 1 646 ? -17.381 4.011   31.089  1.00 30.44 ? 638  ASP B OD2 1 
ATOM   9538  N  N   . LEU B 1 647 ? -14.838 0.501   31.037  1.00 15.75 ? 639  LEU B N   1 
ATOM   9539  C  CA  . LEU B 1 647 ? -15.146 -0.897  30.754  1.00 17.79 ? 639  LEU B CA  1 
ATOM   9540  C  C   . LEU B 1 647 ? -13.980 -1.801  31.113  1.00 17.71 ? 639  LEU B C   1 
ATOM   9541  O  O   . LEU B 1 647 ? -14.189 -2.963  31.487  1.00 15.19 ? 639  LEU B O   1 
ATOM   9542  C  CB  . LEU B 1 647 ? -15.525 -1.065  29.281  1.00 17.62 ? 639  LEU B CB  1 
ATOM   9543  C  CG  . LEU B 1 647 ? -16.843 -0.389  28.863  1.00 19.30 ? 639  LEU B CG  1 
ATOM   9544  C  CD1 . LEU B 1 647 ? -17.014 -0.468  27.345  1.00 23.99 ? 639  LEU B CD1 1 
ATOM   9545  C  CD2 . LEU B 1 647 ? -18.042 -1.003  29.562  1.00 21.58 ? 639  LEU B CD2 1 
ATOM   9546  N  N   . LEU B 1 648 ? -12.750 -1.279  31.011  1.00 14.16 ? 640  LEU B N   1 
ATOM   9547  C  CA  . LEU B 1 648 ? -11.566 -2.043  31.392  1.00 13.41 ? 640  LEU B CA  1 
ATOM   9548  C  C   . LEU B 1 648 ? -11.509 -2.282  32.897  1.00 16.93 ? 640  LEU B C   1 
ATOM   9549  O  O   . LEU B 1 648 ? -11.265 -3.407  33.343  1.00 13.43 ? 640  LEU B O   1 
ATOM   9550  C  CB  . LEU B 1 648 ? -10.306 -1.315  30.933  1.00 12.65 ? 640  LEU B CB  1 
ATOM   9551  C  CG  . LEU B 1 648 ? -10.145 -1.279  29.416  1.00 15.79 ? 640  LEU B CG  1 
ATOM   9552  C  CD1 . LEU B 1 648 ? -8.878  -0.508  29.041  1.00 11.78 ? 640  LEU B CD1 1 
ATOM   9553  C  CD2 . LEU B 1 648 ? -10.127 -2.694  28.856  1.00 17.73 ? 640  LEU B CD2 1 
ATOM   9554  N  N   . PHE B 1 649 ? -11.691 -1.230  33.701  1.00 14.43 ? 641  PHE B N   1 
ATOM   9555  C  CA  . PHE B 1 649 ? -11.661 -1.440  35.148  1.00 13.84 ? 641  PHE B CA  1 
ATOM   9556  C  C   . PHE B 1 649 ? -12.706 -2.470  35.558  1.00 17.27 ? 641  PHE B C   1 
ATOM   9557  O  O   . PHE B 1 649 ? -12.443 -3.328  36.408  1.00 16.37 ? 641  PHE B O   1 
ATOM   9558  C  CB  . PHE B 1 649 ? -11.863 -0.119  35.894  1.00 14.14 ? 641  PHE B CB  1 
ATOM   9559  C  CG  . PHE B 1 649 ? -10.620 0.738   35.951  1.00 13.58 ? 641  PHE B CG  1 
ATOM   9560  C  CD1 . PHE B 1 649 ? -9.465  0.260   36.557  1.00 14.70 ? 641  PHE B CD1 1 
ATOM   9561  C  CD2 . PHE B 1 649 ? -10.609 2.018   35.409  1.00 20.19 ? 641  PHE B CD2 1 
ATOM   9562  C  CE1 . PHE B 1 649 ? -8.307  1.039   36.607  1.00 15.67 ? 641  PHE B CE1 1 
ATOM   9563  C  CE2 . PHE B 1 649 ? -9.460  2.812   35.466  1.00 18.49 ? 641  PHE B CE2 1 
ATOM   9564  C  CZ  . PHE B 1 649 ? -8.308  2.316   36.071  1.00 19.26 ? 641  PHE B CZ  1 
ATOM   9565  N  N   . LYS B 1 650 ? -13.888 -2.425  34.930  1.00 16.09 ? 642  LYS B N   1 
ATOM   9566  C  CA  . LYS B 1 650 ? -14.897 -3.436  35.206  1.00 15.90 ? 642  LYS B CA  1 
ATOM   9567  C  C   . LYS B 1 650 ? -14.431 -4.815  34.758  1.00 17.61 ? 642  LYS B C   1 
ATOM   9568  O  O   . LYS B 1 650 ? -14.526 -5.787  35.514  1.00 18.18 ? 642  LYS B O   1 
ATOM   9569  C  CB  . LYS B 1 650 ? -16.217 -3.077  34.526  1.00 17.05 ? 642  LYS B CB  1 
ATOM   9570  C  CG  . LYS B 1 650 ? -17.226 -4.206  34.555  1.00 19.86 ? 642  LYS B CG  1 
ATOM   9571  C  CD  . LYS B 1 650 ? -18.542 -3.793  33.911  1.00 23.34 ? 642  LYS B CD  1 
ATOM   9572  C  CE  . LYS B 1 650 ? -19.521 -4.953  33.879  1.00 29.41 ? 642  LYS B CE  1 
ATOM   9573  N  NZ  . LYS B 1 650 ? -20.801 -4.564  33.219  1.00 36.14 ? 642  LYS B NZ  1 
ATOM   9574  N  N   . ALA B 1 651 ? -13.928 -4.920  33.526  1.00 15.25 ? 643  ALA B N   1 
ATOM   9575  C  CA  . ALA B 1 651 ? -13.576 -6.229  32.986  1.00 20.21 ? 643  ALA B CA  1 
ATOM   9576  C  C   . ALA B 1 651 ? -12.479 -6.901  33.797  1.00 17.00 ? 643  ALA B C   1 
ATOM   9577  O  O   . ALA B 1 651 ? -12.439 -8.133  33.887  1.00 22.23 ? 643  ALA B O   1 
ATOM   9578  C  CB  . ALA B 1 651 ? -13.138 -6.103  31.523  1.00 15.83 ? 643  ALA B CB  1 
ATOM   9579  N  N   . PHE B 1 652 ? -11.572 -6.122  34.372  1.00 17.36 ? 644  PHE B N   1 
ATOM   9580  C  CA  . PHE B 1 652 ? -10.444 -6.677  35.102  1.00 14.04 ? 644  PHE B CA  1 
ATOM   9581  C  C   . PHE B 1 652 ? -10.692 -6.739  36.604  1.00 14.00 ? 644  PHE B C   1 
ATOM   9582  O  O   . PHE B 1 652 ? -9.751  -6.990  37.368  1.00 15.51 ? 644  PHE B O   1 
ATOM   9583  C  CB  . PHE B 1 652 ? -9.183  -5.875  34.788  1.00 12.83 ? 644  PHE B CB  1 
ATOM   9584  C  CG  . PHE B 1 652 ? -8.607  -6.187  33.422  1.00 17.48 ? 644  PHE B CG  1 
ATOM   9585  C  CD1 . PHE B 1 652 ? -7.848  -7.335  33.221  1.00 23.86 ? 644  PHE B CD1 1 
ATOM   9586  C  CD2 . PHE B 1 652 ? -8.842  -5.348  32.347  1.00 15.89 ? 644  PHE B CD2 1 
ATOM   9587  C  CE1 . PHE B 1 652 ? -7.311  -7.626  31.973  1.00 27.98 ? 644  PHE B CE1 1 
ATOM   9588  C  CE2 . PHE B 1 652 ? -8.323  -5.637  31.092  1.00 19.92 ? 644  PHE B CE2 1 
ATOM   9589  C  CZ  . PHE B 1 652 ? -7.553  -6.771  30.903  1.00 26.27 ? 644  PHE B CZ  1 
ATOM   9590  N  N   . GLY B 1 653 ? -11.927 -6.504  37.034  1.00 14.67 ? 645  GLY B N   1 
ATOM   9591  C  CA  . GLY B 1 653 ? -12.332 -6.762  38.405  1.00 15.19 ? 645  GLY B CA  1 
ATOM   9592  C  C   . GLY B 1 653 ? -12.102 -5.638  39.386  1.00 15.45 ? 645  GLY B C   1 
ATOM   9593  O  O   . GLY B 1 653 ? -12.140 -5.877  40.601  1.00 16.26 ? 645  GLY B O   1 
ATOM   9594  N  N   . PHE B 1 654 ? -11.857 -4.421  38.917  1.00 17.48 ? 646  PHE B N   1 
ATOM   9595  C  CA  . PHE B 1 654 ? -11.706 -3.291  39.833  1.00 15.81 ? 646  PHE B CA  1 
ATOM   9596  C  C   . PHE B 1 654 ? -13.080 -2.659  40.055  1.00 19.92 ? 646  PHE B C   1 
ATOM   9597  O  O   . PHE B 1 654 ? -13.385 -1.542  39.635  1.00 18.33 ? 646  PHE B O   1 
ATOM   9598  C  CB  . PHE B 1 654 ? -10.655 -2.334  39.296  1.00 14.15 ? 646  PHE B CB  1 
ATOM   9599  C  CG  . PHE B 1 654 ? -9.314  -2.980  39.216  1.00 14.39 ? 646  PHE B CG  1 
ATOM   9600  C  CD1 . PHE B 1 654 ? -8.515  -3.066  40.345  1.00 20.43 ? 646  PHE B CD1 1 
ATOM   9601  C  CD2 . PHE B 1 654 ? -8.885  -3.585  38.045  1.00 14.85 ? 646  PHE B CD2 1 
ATOM   9602  C  CE1 . PHE B 1 654 ? -7.281  -3.707  40.298  1.00 13.61 ? 646  PHE B CE1 1 
ATOM   9603  C  CE2 . PHE B 1 654 ? -7.650  -4.228  37.988  1.00 18.41 ? 646  PHE B CE2 1 
ATOM   9604  C  CZ  . PHE B 1 654 ? -6.860  -4.297  39.118  1.00 15.97 ? 646  PHE B CZ  1 
ATOM   9605  N  N   . THR B 1 655 ? -13.924 -3.457  40.706  1.00 16.18 ? 647  THR B N   1 
ATOM   9606  C  CA  . THR B 1 655 ? -15.274 -3.102  41.099  1.00 17.06 ? 647  THR B CA  1 
ATOM   9607  C  C   . THR B 1 655 ? -15.394 -3.207  42.616  1.00 17.50 ? 647  THR B C   1 
ATOM   9608  O  O   . THR B 1 655 ? -14.649 -3.941  43.270  1.00 21.30 ? 647  THR B O   1 
ATOM   9609  C  CB  . THR B 1 655 ? -16.307 -4.028  40.450  1.00 22.27 ? 647  THR B CB  1 
ATOM   9610  O  OG1 . THR B 1 655 ? -16.173 -5.340  41.008  1.00 20.52 ? 647  THR B OG1 1 
ATOM   9611  C  CG2 . THR B 1 655 ? -16.112 -4.099  38.928  1.00 17.23 ? 647  THR B CG2 1 
ATOM   9612  N  N   . VAL B 1 656 ? -16.364 -2.480  43.170  1.00 20.01 ? 648  VAL B N   1 
ATOM   9613  C  CA  . VAL B 1 656 ? -16.617 -2.566  44.605  1.00 19.75 ? 648  VAL B CA  1 
ATOM   9614  C  C   . VAL B 1 656 ? -16.993 -3.991  45.007  1.00 21.93 ? 648  VAL B C   1 
ATOM   9615  O  O   . VAL B 1 656 ? -16.505 -4.514  46.017  1.00 22.14 ? 648  VAL B O   1 
ATOM   9616  C  CB  . VAL B 1 656 ? -17.708 -1.562  45.022  1.00 19.64 ? 648  VAL B CB  1 
ATOM   9617  C  CG1 . VAL B 1 656 ? -18.084 -1.792  46.458  1.00 21.08 ? 648  VAL B CG1 1 
ATOM   9618  C  CG2 . VAL B 1 656 ? -17.221 -0.133  44.826  1.00 26.05 ? 648  VAL B CG2 1 
ATOM   9619  N  N   . ASP B 1 657 ? -17.869 -4.638  44.230  1.00 19.55 ? 649  ASP B N   1 
ATOM   9620  C  CA  . ASP B 1 657 ? -18.292 -5.998  44.562  1.00 24.89 ? 649  ASP B CA  1 
ATOM   9621  C  C   . ASP B 1 657 ? -17.105 -6.945  44.648  1.00 21.91 ? 649  ASP B C   1 
ATOM   9622  O  O   . ASP B 1 657 ? -17.048 -7.797  45.540  1.00 23.06 ? 649  ASP B O   1 
ATOM   9623  C  CB  . ASP B 1 657 ? -19.290 -6.524  43.530  1.00 22.17 ? 649  ASP B CB  1 
ATOM   9624  C  CG  . ASP B 1 657 ? -20.705 -6.110  43.824  1.00 33.86 ? 649  ASP B CG  1 
ATOM   9625  O  OD1 . ASP B 1 657 ? -20.943 -5.454  44.868  1.00 34.42 ? 649  ASP B OD1 1 
ATOM   9626  O  OD2 . ASP B 1 657 ? -21.583 -6.453  43.002  1.00 40.94 ? 649  ASP B OD2 1 
ATOM   9627  N  N   . ASN B 1 658 ? -16.151 -6.818  43.724  1.00 19.97 ? 650  ASN B N   1 
ATOM   9628  C  CA  . ASN B 1 658 ? -15.013 -7.731  43.739  1.00 20.41 ? 650  ASN B CA  1 
ATOM   9629  C  C   . ASN B 1 658 ? -14.097 -7.444  44.917  1.00 20.50 ? 650  ASN B C   1 
ATOM   9630  O  O   . ASN B 1 658 ? -13.580 -8.373  45.547  1.00 20.14 ? 650  ASN B O   1 
ATOM   9631  C  CB  . ASN B 1 658 ? -14.228 -7.653  42.430  1.00 17.29 ? 650  ASN B CB  1 
ATOM   9632  C  CG  . ASN B 1 658 ? -13.169 -8.738  42.335  1.00 22.42 ? 650  ASN B CG  1 
ATOM   9633  O  OD1 . ASN B 1 658 ? -13.429 -9.896  42.663  1.00 23.20 ? 650  ASN B OD1 1 
ATOM   9634  N  ND2 . ASN B 1 658 ? -11.968 -8.367  41.919  1.00 16.17 ? 650  ASN B ND2 1 
ATOM   9635  N  N   . VAL B 1 659 ? -13.878 -6.167  45.235  1.00 17.68 ? 651  VAL B N   1 
ATOM   9636  C  CA  . VAL B 1 659 ? -13.059 -5.866  46.406  1.00 20.20 ? 651  VAL B CA  1 
ATOM   9637  C  C   . VAL B 1 659 ? -13.750 -6.371  47.666  1.00 20.69 ? 651  VAL B C   1 
ATOM   9638  O  O   . VAL B 1 659 ? -13.121 -7.004  48.521  1.00 22.02 ? 651  VAL B O   1 
ATOM   9639  C  CB  . VAL B 1 659 ? -12.744 -4.359  46.482  1.00 17.44 ? 651  VAL B CB  1 
ATOM   9640  C  CG1 . VAL B 1 659 ? -12.033 -4.024  47.811  1.00 18.93 ? 651  VAL B CG1 1 
ATOM   9641  C  CG2 . VAL B 1 659 ? -11.874 -3.930  45.282  1.00 16.60 ? 651  VAL B CG2 1 
ATOM   9642  N  N   . VAL B 1 660 ? -15.068 -6.158  47.767  1.00 19.18 ? 652  VAL B N   1 
ATOM   9643  C  CA  . VAL B 1 660 ? -15.816 -6.606  48.941  1.00 20.51 ? 652  VAL B CA  1 
ATOM   9644  C  C   . VAL B 1 660 ? -15.765 -8.125  49.064  1.00 20.70 ? 652  VAL B C   1 
ATOM   9645  O  O   . VAL B 1 660 ? -15.534 -8.668  50.151  1.00 21.16 ? 652  VAL B O   1 
ATOM   9646  C  CB  . VAL B 1 660 ? -17.267 -6.091  48.884  1.00 20.77 ? 652  VAL B CB  1 
ATOM   9647  C  CG1 . VAL B 1 660 ? -18.144 -6.831  49.892  1.00 21.76 ? 652  VAL B CG1 1 
ATOM   9648  C  CG2 . VAL B 1 660 ? -17.302 -4.590  49.147  1.00 22.06 ? 652  VAL B CG2 1 
ATOM   9649  N  N   . ASP B 1 661 ? -15.992 -8.834  47.956  1.00 21.12 ? 653  ASP B N   1 
ATOM   9650  C  CA  . ASP B 1 661 ? -15.961 -10.294 48.006  1.00 20.61 ? 653  ASP B CA  1 
ATOM   9651  C  C   . ASP B 1 661 ? -14.568 -10.794 48.363  1.00 20.20 ? 653  ASP B C   1 
ATOM   9652  O  O   . ASP B 1 661 ? -14.420 -11.783 49.095  1.00 22.23 ? 653  ASP B O   1 
ATOM   9653  C  CB  . ASP B 1 661 ? -16.419 -10.884 46.669  1.00 26.55 ? 653  ASP B CB  1 
ATOM   9654  C  CG  . ASP B 1 661 ? -17.923 -10.711 46.428  1.00 35.15 ? 653  ASP B CG  1 
ATOM   9655  O  OD1 . ASP B 1 661 ? -18.673 -10.523 47.402  1.00 34.31 ? 653  ASP B OD1 1 
ATOM   9656  O  OD2 . ASP B 1 661 ? -18.350 -10.763 45.254  1.00 41.29 ? 653  ASP B OD2 1 
ATOM   9657  N  N   . THR B 1 662 ? -13.534 -10.112 47.863  1.00 21.06 ? 654  THR B N   1 
ATOM   9658  C  CA  . THR B 1 662 ? -12.162 -10.512 48.149  1.00 25.78 ? 654  THR B CA  1 
ATOM   9659  C  C   . THR B 1 662 ? -11.824 -10.310 49.619  1.00 25.29 ? 654  THR B C   1 
ATOM   9660  O  O   . THR B 1 662 ? -11.163 -11.160 50.227  1.00 21.06 ? 654  THR B O   1 
ATOM   9661  C  CB  . THR B 1 662 ? -11.185 -9.737  47.258  1.00 19.84 ? 654  THR B CB  1 
ATOM   9662  O  OG1 . THR B 1 662 ? -11.449 -10.036 45.882  1.00 21.24 ? 654  THR B OG1 1 
ATOM   9663  C  CG2 . THR B 1 662 ? -9.741  -10.117 47.570  1.00 20.52 ? 654  THR B CG2 1 
ATOM   9664  N  N   . VAL B 1 663 ? -12.277 -9.196  50.208  1.00 19.60 ? 655  VAL B N   1 
ATOM   9665  C  CA  . VAL B 1 663 ? -12.082 -8.976  51.640  1.00 20.19 ? 655  VAL B CA  1 
ATOM   9666  C  C   . VAL B 1 663 ? -12.774 -10.069 52.439  1.00 23.40 ? 655  VAL B C   1 
ATOM   9667  O  O   . VAL B 1 663 ? -12.199 -10.633 53.380  1.00 26.56 ? 655  VAL B O   1 
ATOM   9668  C  CB  . VAL B 1 663 ? -12.580 -7.573  52.043  1.00 20.27 ? 655  VAL B CB  1 
ATOM   9669  C  CG1 . VAL B 1 663 ? -12.661 -7.446  53.552  1.00 21.07 ? 655  VAL B CG1 1 
ATOM   9670  C  CG2 . VAL B 1 663 ? -11.654 -6.493  51.468  1.00 22.71 ? 655  VAL B CG2 1 
ATOM   9671  N  N   . LYS B 1 664 ? -14.019 -10.392 52.077  1.00 22.81 ? 656  LYS B N   1 
ATOM   9672  C  CA  . LYS B 1 664 ? -14.748 -11.426 52.810  1.00 25.74 ? 656  LYS B CA  1 
ATOM   9673  C  C   . LYS B 1 664 ? -14.023 -12.760 52.751  1.00 23.99 ? 656  LYS B C   1 
ATOM   9674  O  O   . LYS B 1 664 ? -14.047 -13.532 53.719  1.00 24.39 ? 656  LYS B O   1 
ATOM   9675  C  CB  . LYS B 1 664 ? -16.160 -11.585 52.255  1.00 25.94 ? 656  LYS B CB  1 
ATOM   9676  C  CG  . LYS B 1 664 ? -17.074 -10.438 52.546  1.00 29.85 ? 656  LYS B CG  1 
ATOM   9677  C  CD  . LYS B 1 664 ? -18.436 -10.715 51.965  1.00 32.62 ? 656  LYS B CD  1 
ATOM   9678  C  CE  . LYS B 1 664 ? -19.331 -9.519  52.150  1.00 38.54 ? 656  LYS B CE  1 
ATOM   9679  N  NZ  . LYS B 1 664 ? -20.773 -9.878  51.993  1.00 38.91 ? 656  LYS B NZ  1 
ATOM   9680  N  N   . SER B 1 665 ? -13.377 -13.046 51.622  1.00 21.92 ? 657  SER B N   1 
ATOM   9681  C  CA  . SER B 1 665 ? -12.772 -14.352 51.397  1.00 29.54 ? 657  SER B CA  1 
ATOM   9682  C  C   . SER B 1 665 ? -11.571 -14.619 52.296  1.00 30.19 ? 657  SER B C   1 
ATOM   9683  O  O   . SER B 1 665 ? -11.144 -15.772 52.394  1.00 28.36 ? 657  SER B O   1 
ATOM   9684  C  CB  . SER B 1 665 ? -12.340 -14.492 49.934  1.00 27.57 ? 657  SER B CB  1 
ATOM   9685  O  OG  . SER B 1 665 ? -11.074 -13.876 49.711  1.00 28.25 ? 657  SER B OG  1 
ATOM   9686  N  N   . VAL B 1 666 ? -10.986 -13.598 52.925  1.00 25.91 ? 658  VAL B N   1 
ATOM   9687  C  CA  . VAL B 1 666 ? -9.866  -13.824 53.836  1.00 24.63 ? 658  VAL B CA  1 
ATOM   9688  C  C   . VAL B 1 666 ? -10.250 -13.610 55.291  1.00 35.45 ? 658  VAL B C   1 
ATOM   9689  O  O   . VAL B 1 666 ? -9.388  -13.737 56.175  1.00 33.38 ? 658  VAL B O   1 
ATOM   9690  C  CB  . VAL B 1 666 ? -8.639  -12.970 53.458  1.00 27.50 ? 658  VAL B CB  1 
ATOM   9691  C  CG1 . VAL B 1 666 ? -8.260  -13.236 52.019  1.00 24.53 ? 658  VAL B CG1 1 
ATOM   9692  C  CG2 . VAL B 1 666 ? -8.899  -11.489 53.680  1.00 28.30 ? 658  VAL B CG2 1 
ATOM   9693  N  N   . LEU B 1 667 ? -11.517 -13.329 55.574  1.00 32.70 ? 659  LEU B N   1 
ATOM   9694  C  CA  . LEU B 1 667 ? -11.982 -13.183 56.944  1.00 42.56 ? 659  LEU B CA  1 
ATOM   9695  C  C   . LEU B 1 667 ? -12.117 -14.544 57.620  1.00 53.28 ? 659  LEU B C   1 
ATOM   9696  O  O   . LEU B 1 667 ? -12.687 -15.483 57.058  1.00 53.88 ? 659  LEU B O   1 
ATOM   9697  C  CB  . LEU B 1 667 ? -13.322 -12.445 56.981  1.00 38.77 ? 659  LEU B CB  1 
ATOM   9698  C  CG  . LEU B 1 667 ? -13.288 -10.991 56.518  1.00 32.74 ? 659  LEU B CG  1 
ATOM   9699  C  CD1 . LEU B 1 667 ? -14.656 -10.349 56.696  1.00 35.04 ? 659  LEU B CD1 1 
ATOM   9700  C  CD2 . LEU B 1 667 ? -12.236 -10.241 57.296  1.00 31.55 ? 659  LEU B CD2 1 
ATOM   9701  O  OXT . LEU B 1 667 ? -11.663 -14.726 58.750  1.00 59.08 ? 659  LEU B OXT 1 
ATOM   9702  N  N   . SER C 1 10  ? 50.311  1.031   56.038  1.00 63.19 ? 2    SER C N   1 
ATOM   9703  C  CA  . SER C 1 10  ? 50.304  0.162   57.208  1.00 55.50 ? 2    SER C CA  1 
ATOM   9704  C  C   . SER C 1 10  ? 51.178  0.760   58.298  1.00 47.79 ? 2    SER C C   1 
ATOM   9705  O  O   . SER C 1 10  ? 50.894  0.610   59.491  1.00 40.15 ? 2    SER C O   1 
ATOM   9706  C  CB  . SER C 1 10  ? 50.790  -1.243  56.845  1.00 59.48 ? 2    SER C CB  1 
ATOM   9707  O  OG  . SER C 1 10  ? 50.466  -2.174  57.863  1.00 58.48 ? 2    SER C OG  1 
ATOM   9708  N  N   . GLN C 1 11  ? 52.248  1.441   57.876  1.00 40.73 ? 3    GLN C N   1 
ATOM   9709  C  CA  . GLN C 1 11  ? 53.114  2.118   58.835  1.00 36.37 ? 3    GLN C CA  1 
ATOM   9710  C  C   . GLN C 1 11  ? 52.390  3.265   59.529  1.00 31.22 ? 3    GLN C C   1 
ATOM   9711  O  O   . GLN C 1 11  ? 52.723  3.606   60.668  1.00 28.29 ? 3    GLN C O   1 
ATOM   9712  C  CB  . GLN C 1 11  ? 54.379  2.627   58.141  1.00 41.61 ? 3    GLN C CB  1 
ATOM   9713  N  N   . LEU C 1 12  ? 51.396  3.869   58.870  1.00 32.22 ? 4    LEU C N   1 
ATOM   9714  C  CA  . LEU C 1 12  ? 50.630  4.917   59.533  1.00 32.09 ? 4    LEU C CA  1 
ATOM   9715  C  C   . LEU C 1 12  ? 49.831  4.363   60.705  1.00 33.08 ? 4    LEU C C   1 
ATOM   9716  O  O   . LEU C 1 12  ? 49.622  5.065   61.699  1.00 31.68 ? 4    LEU C O   1 
ATOM   9717  C  CB  . LEU C 1 12  ? 49.703  5.613   58.535  1.00 34.77 ? 4    LEU C CB  1 
ATOM   9718  C  CG  . LEU C 1 12  ? 50.376  6.238   57.310  1.00 42.54 ? 4    LEU C CG  1 
ATOM   9719  C  CD1 . LEU C 1 12  ? 49.406  7.183   56.608  1.00 40.84 ? 4    LEU C CD1 1 
ATOM   9720  C  CD2 . LEU C 1 12  ? 51.672  6.957   57.689  1.00 37.40 ? 4    LEU C CD2 1 
ATOM   9721  N  N   . ALA C 1 13  ? 49.373  3.117   60.611  1.00 33.45 ? 5    ALA C N   1 
ATOM   9722  C  CA  . ALA C 1 13  ? 48.709  2.506   61.755  1.00 27.03 ? 5    ALA C CA  1 
ATOM   9723  C  C   . ALA C 1 13  ? 49.720  1.922   62.731  1.00 27.96 ? 5    ALA C C   1 
ATOM   9724  O  O   . ALA C 1 13  ? 49.500  1.959   63.946  1.00 26.06 ? 5    ALA C O   1 
ATOM   9725  C  CB  . ALA C 1 13  ? 47.743  1.418   61.290  1.00 26.88 ? 5    ALA C CB  1 
ATOM   9726  N  N   . ASN C 1 14  ? 50.830  1.395   62.217  1.00 26.69 ? 6    ASN C N   1 
ATOM   9727  C  CA  . ASN C 1 14  ? 51.809  0.754   63.085  1.00 30.38 ? 6    ASN C CA  1 
ATOM   9728  C  C   . ASN C 1 14  ? 52.432  1.737   64.061  1.00 27.52 ? 6    ASN C C   1 
ATOM   9729  O  O   . ASN C 1 14  ? 52.725  1.368   65.203  1.00 25.75 ? 6    ASN C O   1 
ATOM   9730  C  CB  . ASN C 1 14  ? 52.892  0.081   62.249  1.00 31.70 ? 6    ASN C CB  1 
ATOM   9731  C  CG  . ASN C 1 14  ? 52.531  -1.333  61.882  1.00 34.69 ? 6    ASN C CG  1 
ATOM   9732  O  OD1 . ASN C 1 14  ? 51.573  -1.899  62.414  1.00 29.99 ? 6    ASN C OD1 1 
ATOM   9733  N  ND2 . ASN C 1 14  ? 53.303  -1.924  60.981  1.00 32.44 ? 6    ASN C ND2 1 
ATOM   9734  N  N   . VAL C 1 15  ? 52.628  2.988   63.644  1.00 27.45 ? 7    VAL C N   1 
ATOM   9735  C  CA  . VAL C 1 15  ? 53.254  3.961   64.534  1.00 24.16 ? 7    VAL C CA  1 
ATOM   9736  C  C   . VAL C 1 15  ? 52.381  4.202   65.761  1.00 25.23 ? 7    VAL C C   1 
ATOM   9737  O  O   . VAL C 1 15  ? 52.891  4.377   66.871  1.00 26.26 ? 7    VAL C O   1 
ATOM   9738  C  CB  . VAL C 1 15  ? 53.566  5.267   63.780  1.00 26.10 ? 7    VAL C CB  1 
ATOM   9739  C  CG1 . VAL C 1 15  ? 52.296  5.902   63.218  1.00 24.81 ? 7    VAL C CG1 1 
ATOM   9740  C  CG2 . VAL C 1 15  ? 54.315  6.230   64.691  1.00 25.16 ? 7    VAL C CG2 1 
ATOM   9741  N  N   . ILE C 1 16  ? 51.056  4.197   65.592  1.00 21.78 ? 8    ILE C N   1 
ATOM   9742  C  CA  . ILE C 1 16  ? 50.172  4.313   66.751  1.00 19.06 ? 8    ILE C CA  1 
ATOM   9743  C  C   . ILE C 1 16  ? 50.328  3.096   67.647  1.00 24.14 ? 8    ILE C C   1 
ATOM   9744  O  O   . ILE C 1 16  ? 50.380  3.203   68.880  1.00 23.98 ? 8    ILE C O   1 
ATOM   9745  C  CB  . ILE C 1 16  ? 48.708  4.484   66.306  1.00 21.10 ? 8    ILE C CB  1 
ATOM   9746  C  CG1 . ILE C 1 16  ? 48.547  5.701   65.398  1.00 23.50 ? 8    ILE C CG1 1 
ATOM   9747  C  CG2 . ILE C 1 16  ? 47.802  4.609   67.526  1.00 27.64 ? 8    ILE C CG2 1 
ATOM   9748  C  CD1 . ILE C 1 16  ? 47.139  5.819   64.800  1.00 21.00 ? 8    ILE C CD1 1 
ATOM   9749  N  N   . ARG C 1 17  ? 50.427  1.923   67.026  1.00 27.82 ? 9    ARG C N   1 
ATOM   9750  C  CA  . ARG C 1 17  ? 50.526  0.657   67.737  1.00 28.93 ? 9    ARG C CA  1 
ATOM   9751  C  C   . ARG C 1 17  ? 51.769  0.602   68.625  1.00 29.45 ? 9    ARG C C   1 
ATOM   9752  O  O   . ARG C 1 17  ? 51.692  0.187   69.789  1.00 26.32 ? 9    ARG C O   1 
ATOM   9753  C  CB  . ARG C 1 17  ? 50.525  -0.464  66.692  1.00 33.31 ? 9    ARG C CB  1 
ATOM   9754  C  CG  . ARG C 1 17  ? 50.344  -1.876  67.175  1.00 34.02 ? 9    ARG C CG  1 
ATOM   9755  C  CD  . ARG C 1 17  ? 50.027  -2.795  65.984  1.00 29.99 ? 9    ARG C CD  1 
ATOM   9756  N  NE  . ARG C 1 17  ? 48.587  -2.937  65.757  1.00 28.26 ? 9    ARG C NE  1 
ATOM   9757  C  CZ  . ARG C 1 17  ? 47.948  -2.597  64.639  1.00 25.19 ? 9    ARG C CZ  1 
ATOM   9758  N  NH1 . ARG C 1 17  ? 48.616  -2.088  63.610  1.00 25.18 ? 9    ARG C NH1 1 
ATOM   9759  N  NH2 . ARG C 1 17  ? 46.632  -2.775  64.549  1.00 25.35 ? 9    ARG C NH2 1 
ATOM   9760  N  N   . PHE C 1 18  ? 52.924  1.025   68.107  1.00 23.81 ? 10   PHE C N   1 
ATOM   9761  C  CA  . PHE C 1 18  ? 54.145  0.886   68.896  1.00 22.40 ? 10   PHE C CA  1 
ATOM   9762  C  C   . PHE C 1 18  ? 54.442  2.091   69.778  1.00 21.75 ? 10   PHE C C   1 
ATOM   9763  O  O   . PHE C 1 18  ? 55.044  1.921   70.843  1.00 23.12 ? 10   PHE C O   1 
ATOM   9764  C  CB  . PHE C 1 18  ? 55.325  0.569   67.975  1.00 29.01 ? 10   PHE C CB  1 
ATOM   9765  C  CG  . PHE C 1 18  ? 55.218  -0.786  67.354  1.00 35.96 ? 10   PHE C CG  1 
ATOM   9766  C  CD1 . PHE C 1 18  ? 55.710  -1.902  68.015  1.00 44.78 ? 10   PHE C CD1 1 
ATOM   9767  C  CD2 . PHE C 1 18  ? 54.573  -0.957  66.137  1.00 33.26 ? 10   PHE C CD2 1 
ATOM   9768  C  CE1 . PHE C 1 18  ? 55.591  -3.161  67.457  1.00 48.74 ? 10   PHE C CE1 1 
ATOM   9769  C  CE2 . PHE C 1 18  ? 54.445  -2.212  65.575  1.00 36.87 ? 10   PHE C CE2 1 
ATOM   9770  C  CZ  . PHE C 1 18  ? 54.956  -3.315  66.233  1.00 47.08 ? 10   PHE C CZ  1 
ATOM   9771  N  N   . LEU C 1 19  ? 54.026  3.301   69.389  1.00 21.33 ? 11   LEU C N   1 
ATOM   9772  C  CA  . LEU C 1 19  ? 54.075  4.415   70.334  1.00 28.98 ? 11   LEU C CA  1 
ATOM   9773  C  C   . LEU C 1 19  ? 53.319  4.067   71.603  1.00 24.10 ? 11   LEU C C   1 
ATOM   9774  O  O   . LEU C 1 19  ? 53.784  4.343   72.717  1.00 24.54 ? 11   LEU C O   1 
ATOM   9775  C  CB  . LEU C 1 19  ? 53.477  5.685   69.724  1.00 24.99 ? 11   LEU C CB  1 
ATOM   9776  C  CG  . LEU C 1 19  ? 54.374  6.756   69.114  1.00 29.82 ? 11   LEU C CG  1 
ATOM   9777  C  CD1 . LEU C 1 19  ? 53.526  7.956   68.715  1.00 29.47 ? 11   LEU C CD1 1 
ATOM   9778  C  CD2 . LEU C 1 19  ? 55.507  7.170   70.072  1.00 23.15 ? 11   LEU C CD2 1 
ATOM   9779  N  N   . SER C 1 20  ? 52.147  3.448   71.448  1.00 20.26 ? 12   SER C N   1 
ATOM   9780  C  CA  . SER C 1 20  ? 51.332  3.087   72.600  1.00 20.36 ? 12   SER C CA  1 
ATOM   9781  C  C   . SER C 1 20  ? 51.992  1.989   73.426  1.00 22.92 ? 12   SER C C   1 
ATOM   9782  O  O   . SER C 1 20  ? 52.068  2.089   74.657  1.00 20.08 ? 12   SER C O   1 
ATOM   9783  C  CB  . SER C 1 20  ? 49.945  2.659   72.125  1.00 21.24 ? 12   SER C CB  1 
ATOM   9784  O  OG  . SER C 1 20  ? 49.319  3.716   71.409  1.00 20.93 ? 12   SER C OG  1 
ATOM   9785  N  N   . ALA C 1 21  ? 52.471  0.924   72.766  1.00 20.42 ? 13   ALA C N   1 
ATOM   9786  C  CA  . ALA C 1 21  ? 53.141  -0.159  73.486  1.00 22.77 ? 13   ALA C CA  1 
ATOM   9787  C  C   . ALA C 1 21  ? 54.421  0.328   74.148  1.00 23.35 ? 13   ALA C C   1 
ATOM   9788  O  O   . ALA C 1 21  ? 54.723  -0.049  75.287  1.00 25.79 ? 13   ALA C O   1 
ATOM   9789  C  CB  . ALA C 1 21  ? 53.449  -1.321  72.540  1.00 29.00 ? 13   ALA C CB  1 
ATOM   9790  N  N   . ASP C 1 22  ? 55.189  1.168   73.450  1.00 21.95 ? 14   ASP C N   1 
ATOM   9791  C  CA  . ASP C 1 22  ? 56.440  1.661   74.024  1.00 25.02 ? 14   ASP C CA  1 
ATOM   9792  C  C   . ASP C 1 22  ? 56.196  2.558   75.231  1.00 24.29 ? 14   ASP C C   1 
ATOM   9793  O  O   . ASP C 1 22  ? 56.929  2.477   76.222  1.00 23.05 ? 14   ASP C O   1 
ATOM   9794  C  CB  . ASP C 1 22  ? 57.254  2.406   72.970  1.00 23.20 ? 14   ASP C CB  1 
ATOM   9795  C  CG  . ASP C 1 22  ? 57.800  1.482   71.905  1.00 28.22 ? 14   ASP C CG  1 
ATOM   9796  O  OD1 . ASP C 1 22  ? 58.053  0.298   72.219  1.00 30.68 ? 14   ASP C OD1 1 
ATOM   9797  O  OD2 . ASP C 1 22  ? 57.974  1.941   70.756  1.00 27.31 ? 14   ASP C OD2 1 
ATOM   9798  N  N   . ALA C 1 23  ? 55.185  3.431   75.164  1.00 24.86 ? 15   ALA C N   1 
ATOM   9799  C  CA  . ALA C 1 23  ? 54.941  4.333   76.283  1.00 21.55 ? 15   ALA C CA  1 
ATOM   9800  C  C   . ALA C 1 23  ? 54.410  3.574   77.495  1.00 23.39 ? 15   ALA C C   1 
ATOM   9801  O  O   . ALA C 1 23  ? 54.760  3.893   78.640  1.00 22.56 ? 15   ALA C O   1 
ATOM   9802  C  CB  . ALA C 1 23  ? 53.970  5.436   75.873  1.00 20.82 ? 15   ALA C CB  1 
ATOM   9803  N  N   . VAL C 1 24  ? 53.560  2.571   77.263  1.00 21.91 ? 16   VAL C N   1 
ATOM   9804  C  CA  . VAL C 1 24  ? 53.074  1.742   78.360  1.00 22.60 ? 16   VAL C CA  1 
ATOM   9805  C  C   . VAL C 1 24  ? 54.234  1.014   79.023  1.00 23.15 ? 16   VAL C C   1 
ATOM   9806  O  O   . VAL C 1 24  ? 54.321  0.941   80.254  1.00 24.03 ? 16   VAL C O   1 
ATOM   9807  C  CB  . VAL C 1 24  ? 52.004  0.758   77.851  1.00 22.86 ? 16   VAL C CB  1 
ATOM   9808  C  CG1 . VAL C 1 24  ? 51.730  -0.327  78.897  1.00 26.37 ? 16   VAL C CG1 1 
ATOM   9809  C  CG2 . VAL C 1 24  ? 50.728  1.507   77.497  1.00 22.85 ? 16   VAL C CG2 1 
ATOM   9810  N  N   . GLN C 1 25  ? 55.159  0.488   78.220  1.00 25.01 ? 17   GLN C N   1 
ATOM   9811  C  CA  . GLN C 1 25  ? 56.292  -0.229  78.795  1.00 27.92 ? 17   GLN C CA  1 
ATOM   9812  C  C   . GLN C 1 25  ? 57.192  0.697   79.604  1.00 24.93 ? 17   GLN C C   1 
ATOM   9813  O  O   . GLN C 1 25  ? 57.680  0.310   80.672  1.00 25.92 ? 17   GLN C O   1 
ATOM   9814  C  CB  . GLN C 1 25  ? 57.093  -0.923  77.700  1.00 27.62 ? 17   GLN C CB  1 
ATOM   9815  C  CG  . GLN C 1 25  ? 57.925  -2.068  78.250  1.00 38.34 ? 17   GLN C CG  1 
ATOM   9816  C  CD  . GLN C 1 25  ? 57.074  -3.074  79.017  1.00 39.03 ? 17   GLN C CD  1 
ATOM   9817  O  OE1 . GLN C 1 25  ? 55.987  -3.449  78.571  1.00 45.46 ? 17   GLN C OE1 1 
ATOM   9818  N  NE2 . GLN C 1 25  ? 57.557  -3.501  80.179  1.00 37.51 ? 17   GLN C NE2 1 
ATOM   9819  N  N   . LYS C 1 26  ? 57.430  1.919   79.116  1.00 25.82 ? 18   LYS C N   1 
ATOM   9820  C  CA  . LYS C 1 26  ? 58.296  2.845   79.846  1.00 27.36 ? 18   LYS C CA  1 
ATOM   9821  C  C   . LYS C 1 26  ? 57.663  3.261   81.167  1.00 27.89 ? 18   LYS C C   1 
ATOM   9822  O  O   . LYS C 1 26  ? 58.366  3.456   82.169  1.00 29.10 ? 18   LYS C O   1 
ATOM   9823  C  CB  . LYS C 1 26  ? 58.612  4.078   78.995  1.00 25.07 ? 18   LYS C CB  1 
ATOM   9824  C  CG  . LYS C 1 26  ? 59.662  5.007   79.617  1.00 26.59 ? 18   LYS C CG  1 
ATOM   9825  C  CD  . LYS C 1 26  ? 59.998  6.191   78.709  1.00 28.81 ? 18   LYS C CD  1 
ATOM   9826  C  CE  . LYS C 1 26  ? 61.123  7.047   79.300  1.00 35.70 ? 18   LYS C CE  1 
ATOM   9827  N  NZ  . LYS C 1 26  ? 60.687  7.862   80.482  1.00 32.60 ? 18   LYS C NZ  1 
ATOM   9828  N  N   . ALA C 1 27  ? 56.336  3.412   81.184  1.00 28.21 ? 19   ALA C N   1 
ATOM   9829  C  CA  . ALA C 1 27  ? 55.630  3.683   82.427  1.00 25.85 ? 19   ALA C CA  1 
ATOM   9830  C  C   . ALA C 1 27  ? 55.535  2.445   83.302  1.00 31.86 ? 19   ALA C C   1 
ATOM   9831  O  O   . ALA C 1 27  ? 55.328  2.572   84.514  1.00 31.09 ? 19   ALA C O   1 
ATOM   9832  C  CB  . ALA C 1 27  ? 54.228  4.219   82.128  1.00 27.41 ? 19   ALA C CB  1 
ATOM   9833  N  N   . ASN C 1 28  ? 55.696  1.257   82.715  1.00 28.92 ? 20   ASN C N   1 
ATOM   9834  C  CA  . ASN C 1 28  ? 55.453  -0.006  83.408  1.00 30.04 ? 20   ASN C CA  1 
ATOM   9835  C  C   . ASN C 1 28  ? 54.063  -0.004  84.041  1.00 27.84 ? 20   ASN C C   1 
ATOM   9836  O  O   . ASN C 1 28  ? 53.850  -0.518  85.141  1.00 29.33 ? 20   ASN C O   1 
ATOM   9837  C  CB  . ASN C 1 28  ? 56.539  -0.285  84.452  1.00 39.07 ? 20   ASN C CB  1 
ATOM   9838  C  CG  . ASN C 1 28  ? 56.565  -1.730  84.884  1.00 50.76 ? 20   ASN C CG  1 
ATOM   9839  O  OD1 . ASN C 1 28  ? 56.162  -2.619  84.131  1.00 56.58 ? 20   ASN C OD1 1 
ATOM   9840  N  ND2 . ASN C 1 28  ? 57.029  -1.977  86.103  1.00 56.58 ? 20   ASN C ND2 1 
ATOM   9841  N  N   . SER C 1 29  ? 53.109  0.585   83.324  1.00 26.71 ? 21   SER C N   1 
ATOM   9842  C  CA  . SER C 1 29  ? 51.754  0.822   83.798  1.00 30.44 ? 21   SER C CA  1 
ATOM   9843  C  C   . SER C 1 29  ? 50.909  1.241   82.602  1.00 25.56 ? 21   SER C C   1 
ATOM   9844  O  O   . SER C 1 29  ? 51.382  1.988   81.739  1.00 24.42 ? 21   SER C O   1 
ATOM   9845  C  CB  . SER C 1 29  ? 51.742  1.908   84.892  1.00 31.03 ? 21   SER C CB  1 
ATOM   9846  O  OG  . SER C 1 29  ? 50.438  2.201   85.361  1.00 28.91 ? 21   SER C OG  1 
ATOM   9847  N  N   . GLY C 1 30  ? 49.684  0.735   82.532  1.00 25.72 ? 22   GLY C N   1 
ATOM   9848  C  CA  . GLY C 1 30  ? 48.758  1.102   81.479  1.00 36.49 ? 22   GLY C CA  1 
ATOM   9849  C  C   . GLY C 1 30  ? 48.315  -0.090  80.647  1.00 36.78 ? 22   GLY C C   1 
ATOM   9850  O  O   . GLY C 1 30  ? 48.704  -1.234  80.881  1.00 33.06 ? 22   GLY C O   1 
ATOM   9851  N  N   . HIS C 1 31  ? 47.499  0.217   79.640  1.00 34.88 ? 23   HIS C N   1 
ATOM   9852  C  CA  . HIS C 1 31  ? 46.805  -0.791  78.836  1.00 40.40 ? 23   HIS C CA  1 
ATOM   9853  C  C   . HIS C 1 31  ? 47.220  -0.660  77.379  1.00 34.38 ? 23   HIS C C   1 
ATOM   9854  O  O   . HIS C 1 31  ? 46.771  0.280   76.694  1.00 36.36 ? 23   HIS C O   1 
ATOM   9855  C  CB  . HIS C 1 31  ? 45.286  -0.643  78.949  1.00 47.96 ? 23   HIS C CB  1 
ATOM   9856  C  CG  . HIS C 1 31  ? 44.797  -0.329  80.330  1.00 60.20 ? 23   HIS C CG  1 
ATOM   9857  N  ND1 . HIS C 1 31  ? 44.902  0.926   80.891  1.00 61.58 ? 23   HIS C ND1 1 
ATOM   9858  C  CD2 . HIS C 1 31  ? 44.172  -1.101  81.251  1.00 64.69 ? 23   HIS C CD2 1 
ATOM   9859  C  CE1 . HIS C 1 31  ? 44.375  0.910   82.102  1.00 64.14 ? 23   HIS C CE1 1 
ATOM   9860  N  NE2 . HIS C 1 31  ? 43.925  -0.308  82.345  1.00 64.97 ? 23   HIS C NE2 1 
ATOM   9861  N  N   . PRO C 1 32  ? 48.043  -1.560  76.848  1.00 33.30 ? 24   PRO C N   1 
ATOM   9862  C  CA  . PRO C 1 32  ? 48.474  -1.425  75.449  1.00 29.92 ? 24   PRO C CA  1 
ATOM   9863  C  C   . PRO C 1 32  ? 47.567  -2.145  74.458  1.00 32.15 ? 24   PRO C C   1 
ATOM   9864  O  O   . PRO C 1 32  ? 47.599  -1.846  73.260  1.00 30.53 ? 24   PRO C O   1 
ATOM   9865  C  CB  . PRO C 1 32  ? 49.880  -2.037  75.470  1.00 27.84 ? 24   PRO C CB  1 
ATOM   9866  C  CG  . PRO C 1 32  ? 49.769  -3.115  76.509  1.00 32.81 ? 24   PRO C CG  1 
ATOM   9867  C  CD  . PRO C 1 32  ? 48.797  -2.611  77.555  1.00 33.55 ? 24   PRO C CD  1 
ATOM   9868  N  N   . GLY C 1 33  ? 46.749  -3.082  74.940  1.00 31.70 ? 25   GLY C N   1 
ATOM   9869  C  CA  . GLY C 1 33  ? 46.030  -3.963  74.029  1.00 22.91 ? 25   GLY C CA  1 
ATOM   9870  C  C   . GLY C 1 33  ? 44.986  -3.242  73.198  1.00 27.35 ? 25   GLY C C   1 
ATOM   9871  O  O   . GLY C 1 33  ? 44.885  -3.452  71.984  1.00 24.47 ? 25   GLY C O   1 
ATOM   9872  N  N   . ALA C 1 34  ? 44.186  -2.390  73.841  1.00 25.74 ? 26   ALA C N   1 
ATOM   9873  C  CA  . ALA C 1 34  ? 43.157  -1.655  73.110  1.00 23.40 ? 26   ALA C CA  1 
ATOM   9874  C  C   . ALA C 1 34  ? 43.733  -0.665  72.107  1.00 23.14 ? 26   ALA C C   1 
ATOM   9875  O  O   . ALA C 1 34  ? 43.221  -0.605  70.974  1.00 22.84 ? 26   ALA C O   1 
ATOM   9876  C  CB  . ALA C 1 34  ? 42.216  -0.965  74.102  1.00 29.30 ? 26   ALA C CB  1 
ATOM   9877  N  N   . PRO C 1 35  ? 44.745  0.155   72.436  1.00 23.23 ? 27   PRO C N   1 
ATOM   9878  C  CA  . PRO C 1 35  ? 45.312  1.024   71.392  1.00 26.26 ? 27   PRO C CA  1 
ATOM   9879  C  C   . PRO C 1 35  ? 45.892  0.241   70.235  1.00 26.19 ? 27   PRO C C   1 
ATOM   9880  O  O   . PRO C 1 35  ? 45.706  0.628   69.074  1.00 27.27 ? 27   PRO C O   1 
ATOM   9881  C  CB  . PRO C 1 35  ? 46.393  1.821   72.142  1.00 27.80 ? 27   PRO C CB  1 
ATOM   9882  C  CG  . PRO C 1 35  ? 45.969  1.791   73.549  1.00 22.39 ? 27   PRO C CG  1 
ATOM   9883  C  CD  . PRO C 1 35  ? 45.355  0.437   73.750  1.00 26.31 ? 27   PRO C CD  1 
ATOM   9884  N  N   . MET C 1 36  ? 46.579  -0.868  70.516  1.00 23.77 ? 28   MET C N   1 
ATOM   9885  C  CA  . MET C 1 36  ? 47.130  -1.677  69.432  1.00 22.90 ? 28   MET C CA  1 
ATOM   9886  C  C   . MET C 1 36  ? 46.025  -2.208  68.526  1.00 25.76 ? 28   MET C C   1 
ATOM   9887  O  O   . MET C 1 36  ? 46.133  -2.147  67.293  1.00 28.11 ? 28   MET C O   1 
ATOM   9888  C  CB  . MET C 1 36  ? 47.973  -2.820  70.006  1.00 26.46 ? 28   MET C CB  1 
ATOM   9889  C  CG  . MET C 1 36  ? 49.239  -2.333  70.697  1.00 26.56 ? 28   MET C CG  1 
ATOM   9890  S  SD  . MET C 1 36  ? 50.162  -3.637  71.529  1.00 33.31 ? 28   MET C SD  1 
ATOM   9891  C  CE  . MET C 1 36  ? 50.592  -4.671  70.133  1.00 34.10 ? 28   MET C CE  1 
ATOM   9892  N  N   . GLY C 1 37  ? 44.941  -2.715  69.118  1.00 23.32 ? 29   GLY C N   1 
ATOM   9893  C  CA  . GLY C 1 37  ? 43.864  -3.271  68.319  1.00 21.50 ? 29   GLY C CA  1 
ATOM   9894  C  C   . GLY C 1 37  ? 43.133  -2.233  67.493  1.00 24.31 ? 29   GLY C C   1 
ATOM   9895  O  O   . GLY C 1 37  ? 42.660  -2.536  66.392  1.00 26.70 ? 29   GLY C O   1 
ATOM   9896  N  N   . MET C 1 38  ? 43.049  -1.000  67.989  1.00 19.16 ? 30   MET C N   1 
ATOM   9897  C  CA  . MET C 1 38  ? 42.261  0.045   67.343  1.00 18.26 ? 30   MET C CA  1 
ATOM   9898  C  C   . MET C 1 38  ? 43.077  0.906   66.387  1.00 20.19 ? 30   MET C C   1 
ATOM   9899  O  O   . MET C 1 38  ? 42.547  1.897   65.873  1.00 18.75 ? 30   MET C O   1 
ATOM   9900  C  CB  . MET C 1 38  ? 41.587  0.932   68.396  1.00 17.47 ? 30   MET C CB  1 
ATOM   9901  C  CG  . MET C 1 38  ? 40.405  0.261   69.120  1.00 18.14 ? 30   MET C CG  1 
ATOM   9902  S  SD  . MET C 1 38  ? 39.523  1.391   70.247  1.00 22.75 ? 30   MET C SD  1 
ATOM   9903  C  CE  . MET C 1 38  ? 40.697  1.610   71.568  1.00 28.91 ? 30   MET C CE  1 
ATOM   9904  N  N   . ALA C 1 39  ? 44.332  0.526   66.106  1.00 18.50 ? 31   ALA C N   1 
ATOM   9905  C  CA  . ALA C 1 39  ? 45.220  1.390   65.333  1.00 18.46 ? 31   ALA C CA  1 
ATOM   9906  C  C   . ALA C 1 39  ? 44.670  1.667   63.937  1.00 18.76 ? 31   ALA C C   1 
ATOM   9907  O  O   . ALA C 1 39  ? 44.729  2.803   63.459  1.00 19.76 ? 31   ALA C O   1 
ATOM   9908  C  CB  . ALA C 1 39  ? 46.615  0.765   65.236  1.00 19.53 ? 31   ALA C CB  1 
ATOM   9909  N  N   . GLU C 1 40  ? 44.162  0.640   63.251  1.00 19.75 ? 32   GLU C N   1 
ATOM   9910  C  CA  . GLU C 1 40  ? 43.632  0.866   61.906  1.00 20.28 ? 32   GLU C CA  1 
ATOM   9911  C  C   . GLU C 1 40  ? 42.330  1.643   61.946  1.00 20.76 ? 32   GLU C C   1 
ATOM   9912  O  O   . GLU C 1 40  ? 42.043  2.410   61.024  1.00 19.13 ? 32   GLU C O   1 
ATOM   9913  C  CB  . GLU C 1 40  ? 43.414  -0.452  61.159  1.00 23.03 ? 32   GLU C CB  1 
ATOM   9914  C  CG  . GLU C 1 40  ? 44.672  -1.036  60.553  1.00 25.11 ? 32   GLU C CG  1 
ATOM   9915  C  CD  . GLU C 1 40  ? 45.550  -1.665  61.595  1.00 30.44 ? 32   GLU C CD  1 
ATOM   9916  O  OE1 . GLU C 1 40  ? 45.030  -1.967  62.688  1.00 27.52 ? 32   GLU C OE1 1 
ATOM   9917  O  OE2 . GLU C 1 40  ? 46.755  -1.845  61.326  1.00 30.63 ? 32   GLU C OE2 1 
ATOM   9918  N  N   . MET C 1 41  ? 41.526  1.452   62.990  1.00 18.43 ? 33   MET C N   1 
ATOM   9919  C  CA  . MET C 1 41  ? 40.350  2.297   63.154  1.00 22.54 ? 33   MET C CA  1 
ATOM   9920  C  C   . MET C 1 41  ? 40.748  3.756   63.327  1.00 16.50 ? 33   MET C C   1 
ATOM   9921  O  O   . MET C 1 41  ? 40.138  4.651   62.730  1.00 17.53 ? 33   MET C O   1 
ATOM   9922  C  CB  . MET C 1 41  ? 39.522  1.813   64.345  1.00 22.34 ? 33   MET C CB  1 
ATOM   9923  C  CG  . MET C 1 41  ? 38.983  0.405   64.154  1.00 18.98 ? 33   MET C CG  1 
ATOM   9924  S  SD  . MET C 1 41  ? 38.621  -0.408  65.720  1.00 19.45 ? 33   MET C SD  1 
ATOM   9925  C  CE  . MET C 1 41  ? 37.420  0.735   66.419  1.00 19.85 ? 33   MET C CE  1 
ATOM   9926  N  N   . ALA C 1 42  ? 41.788  4.016   64.123  1.00 16.27 ? 34   ALA C N   1 
ATOM   9927  C  CA  . ALA C 1 42  ? 42.210  5.394   64.349  1.00 15.68 ? 34   ALA C CA  1 
ATOM   9928  C  C   . ALA C 1 42  ? 42.806  6.006   63.089  1.00 16.23 ? 34   ALA C C   1 
ATOM   9929  O  O   . ALA C 1 42  ? 42.506  7.161   62.755  1.00 16.89 ? 34   ALA C O   1 
ATOM   9930  C  CB  . ALA C 1 42  ? 43.219  5.451   65.493  1.00 15.60 ? 34   ALA C CB  1 
ATOM   9931  N  N   . GLU C 1 43  ? 43.665  5.257   62.390  1.00 17.28 ? 35   GLU C N   1 
ATOM   9932  C  CA  . GLU C 1 43  ? 44.255  5.772   61.159  1.00 18.28 ? 35   GLU C CA  1 
ATOM   9933  C  C   . GLU C 1 43  ? 43.171  6.195   60.184  1.00 18.30 ? 35   GLU C C   1 
ATOM   9934  O  O   . GLU C 1 43  ? 43.207  7.299   59.632  1.00 24.24 ? 35   GLU C O   1 
ATOM   9935  C  CB  . GLU C 1 43  ? 45.160  4.728   60.504  1.00 19.81 ? 35   GLU C CB  1 
ATOM   9936  C  CG  . GLU C 1 43  ? 45.824  5.245   59.240  1.00 24.37 ? 35   GLU C CG  1 
ATOM   9937  C  CD  . GLU C 1 43  ? 46.319  4.142   58.334  1.00 30.86 ? 35   GLU C CD  1 
ATOM   9938  O  OE1 . GLU C 1 43  ? 46.420  2.983   58.786  1.00 29.92 ? 35   GLU C OE1 1 
ATOM   9939  O  OE2 . GLU C 1 43  ? 46.611  4.440   57.162  1.00 33.61 ? 35   GLU C OE2 1 
ATOM   9940  N  N   . THR C 1 44  ? 42.180  5.329   59.980  1.00 22.35 ? 36   THR C N   1 
ATOM   9941  C  CA  . THR C 1 44  ? 41.156  5.616   58.988  1.00 19.04 ? 36   THR C CA  1 
ATOM   9942  C  C   . THR C 1 44  ? 40.335  6.838   59.382  1.00 17.32 ? 36   THR C C   1 
ATOM   9943  O  O   . THR C 1 44  ? 40.156  7.757   58.578  1.00 17.60 ? 36   THR C O   1 
ATOM   9944  C  CB  . THR C 1 44  ? 40.262  4.397   58.789  1.00 21.98 ? 36   THR C CB  1 
ATOM   9945  O  OG1 . THR C 1 44  ? 41.072  3.275   58.420  1.00 22.50 ? 36   THR C OG1 1 
ATOM   9946  C  CG2 . THR C 1 44  ? 39.273  4.673   57.663  1.00 19.44 ? 36   THR C CG2 1 
ATOM   9947  N  N   . LEU C 1 45  ? 39.834  6.878   60.618  1.00 16.23 ? 37   LEU C N   1 
ATOM   9948  C  CA  . LEU C 1 45  ? 39.017  8.019   61.025  1.00 15.40 ? 37   LEU C CA  1 
ATOM   9949  C  C   . LEU C 1 45  ? 39.819  9.317   60.980  1.00 20.66 ? 37   LEU C C   1 
ATOM   9950  O  O   . LEU C 1 45  ? 39.384  10.314  60.395  1.00 16.08 ? 37   LEU C O   1 
ATOM   9951  C  CB  . LEU C 1 45  ? 38.448  7.791   62.423  1.00 14.68 ? 37   LEU C CB  1 
ATOM   9952  C  CG  . LEU C 1 45  ? 37.673  8.995   62.947  1.00 15.68 ? 37   LEU C CG  1 
ATOM   9953  C  CD1 . LEU C 1 45  ? 36.440  9.249   62.054  1.00 14.19 ? 37   LEU C CD1 1 
ATOM   9954  C  CD2 . LEU C 1 45  ? 37.273  8.764   64.382  1.00 17.80 ? 37   LEU C CD2 1 
ATOM   9955  N  N   . TRP C 1 46  ? 41.011  9.316   61.572  1.00 18.30 ? 38   TRP C N   1 
ATOM   9956  C  CA  . TRP C 1 46  ? 41.731  10.568  61.742  1.00 20.83 ? 38   TRP C CA  1 
ATOM   9957  C  C   . TRP C 1 46  ? 42.370  11.061  60.447  1.00 22.50 ? 38   TRP C C   1 
ATOM   9958  O  O   . TRP C 1 46  ? 42.406  12.275  60.221  1.00 19.71 ? 38   TRP C O   1 
ATOM   9959  C  CB  . TRP C 1 46  ? 42.768  10.434  62.871  1.00 15.77 ? 38   TRP C CB  1 
ATOM   9960  C  CG  . TRP C 1 46  ? 42.128  10.609  64.233  1.00 17.58 ? 38   TRP C CG  1 
ATOM   9961  C  CD1 . TRP C 1 46  ? 41.138  9.840   64.775  1.00 16.34 ? 38   TRP C CD1 1 
ATOM   9962  C  CD2 . TRP C 1 46  ? 42.417  11.633  65.204  1.00 15.02 ? 38   TRP C CD2 1 
ATOM   9963  N  NE1 . TRP C 1 46  ? 40.795  10.320  66.016  1.00 14.19 ? 38   TRP C NE1 1 
ATOM   9964  C  CE2 . TRP C 1 46  ? 41.569  11.415  66.304  1.00 14.54 ? 38   TRP C CE2 1 
ATOM   9965  C  CE3 . TRP C 1 46  ? 43.312  12.713  65.242  1.00 21.64 ? 38   TRP C CE3 1 
ATOM   9966  C  CZ2 . TRP C 1 46  ? 41.587  12.233  67.442  1.00 14.78 ? 38   TRP C CZ2 1 
ATOM   9967  C  CZ3 . TRP C 1 46  ? 43.337  13.526  66.377  1.00 25.54 ? 38   TRP C CZ3 1 
ATOM   9968  C  CH2 . TRP C 1 46  ? 42.471  13.281  67.459  1.00 20.84 ? 38   TRP C CH2 1 
ATOM   9969  N  N   . THR C 1 47  ? 42.857  10.171  59.573  1.00 17.95 ? 39   THR C N   1 
ATOM   9970  C  CA  . THR C 1 47  ? 43.476  10.661  58.344  1.00 19.51 ? 39   THR C CA  1 
ATOM   9971  C  C   . THR C 1 47  ? 42.483  10.887  57.215  1.00 19.93 ? 39   THR C C   1 
ATOM   9972  O  O   . THR C 1 47  ? 42.773  11.679  56.314  1.00 21.20 ? 39   THR C O   1 
ATOM   9973  C  CB  . THR C 1 47  ? 44.579  9.716   57.818  1.00 24.70 ? 39   THR C CB  1 
ATOM   9974  O  OG1 . THR C 1 47  ? 44.000  8.504   57.316  1.00 21.11 ? 39   THR C OG1 1 
ATOM   9975  C  CG2 . THR C 1 47  ? 45.608  9.396   58.897  1.00 22.79 ? 39   THR C CG2 1 
ATOM   9976  N  N   . LYS C 1 48  ? 41.334  10.206  57.220  1.00 19.12 ? 40   LYS C N   1 
ATOM   9977  C  CA  . LYS C 1 48  ? 40.418  10.280  56.088  1.00 19.71 ? 40   LYS C CA  1 
ATOM   9978  C  C   . LYS C 1 48  ? 39.158  11.094  56.355  1.00 18.63 ? 40   LYS C C   1 
ATOM   9979  O  O   . LYS C 1 48  ? 38.517  11.524  55.393  1.00 19.25 ? 40   LYS C O   1 
ATOM   9980  C  CB  . LYS C 1 48  ? 39.991  8.874   55.629  1.00 20.17 ? 40   LYS C CB  1 
ATOM   9981  C  CG  . LYS C 1 48  ? 41.131  7.907   55.249  1.00 21.61 ? 40   LYS C CG  1 
ATOM   9982  C  CD  . LYS C 1 48  ? 41.926  8.379   54.041  1.00 32.78 ? 40   LYS C CD  1 
ATOM   9983  C  CE  . LYS C 1 48  ? 43.035  7.383   53.690  1.00 36.34 ? 40   LYS C CE  1 
ATOM   9984  N  NZ  . LYS C 1 48  ? 43.984  7.938   52.691  1.00 40.24 ? 40   LYS C NZ  1 
ATOM   9985  N  N   . PHE C 1 49  ? 38.785  11.318  57.609  1.00 15.46 ? 41   PHE C N   1 
ATOM   9986  C  CA  . PHE C 1 49  ? 37.492  11.961  57.841  1.00 15.86 ? 41   PHE C CA  1 
ATOM   9987  C  C   . PHE C 1 49  ? 37.541  13.113  58.836  1.00 20.71 ? 41   PHE C C   1 
ATOM   9988  O  O   . PHE C 1 49  ? 36.882  14.134  58.621  1.00 18.03 ? 41   PHE C O   1 
ATOM   9989  C  CB  . PHE C 1 49  ? 36.468  10.908  58.336  1.00 17.06 ? 41   PHE C CB  1 
ATOM   9990  C  CG  . PHE C 1 49  ? 36.104  9.882   57.310  1.00 16.67 ? 41   PHE C CG  1 
ATOM   9991  C  CD1 . PHE C 1 49  ? 35.099  10.141  56.378  1.00 19.60 ? 41   PHE C CD1 1 
ATOM   9992  C  CD2 . PHE C 1 49  ? 36.757  8.660   57.268  1.00 16.90 ? 41   PHE C CD2 1 
ATOM   9993  C  CE1 . PHE C 1 49  ? 34.754  9.198   55.423  1.00 17.65 ? 41   PHE C CE1 1 
ATOM   9994  C  CE2 . PHE C 1 49  ? 36.423  7.707   56.304  1.00 18.36 ? 41   PHE C CE2 1 
ATOM   9995  C  CZ  . PHE C 1 49  ? 35.419  7.980   55.388  1.00 18.75 ? 41   PHE C CZ  1 
ATOM   9996  N  N   . LEU C 1 50  ? 38.287  12.976  59.929  1.00 13.79 ? 42   LEU C N   1 
ATOM   9997  C  CA  . LEU C 1 50  ? 38.131  13.903  61.044  1.00 12.99 ? 42   LEU C CA  1 
ATOM   9998  C  C   . LEU C 1 50  ? 38.547  15.318  60.652  1.00 14.66 ? 42   LEU C C   1 
ATOM   9999  O  O   . LEU C 1 50  ? 39.655  15.539  60.155  1.00 18.35 ? 42   LEU C O   1 
ATOM   10000 C  CB  . LEU C 1 50  ? 38.961  13.426  62.229  1.00 12.04 ? 42   LEU C CB  1 
ATOM   10001 C  CG  . LEU C 1 50  ? 38.704  14.129  63.560  1.00 17.24 ? 42   LEU C CG  1 
ATOM   10002 C  CD1 . LEU C 1 50  ? 37.385  13.653  64.180  1.00 15.98 ? 42   LEU C CD1 1 
ATOM   10003 C  CD2 . LEU C 1 50  ? 39.877  13.844  64.492  1.00 16.50 ? 42   LEU C CD2 1 
ATOM   10004 N  N   . ASN C 1 51  ? 37.645  16.279  60.859  1.00 14.07 ? 43   ASN C N   1 
ATOM   10005 C  CA  . ASN C 1 51  ? 37.913  17.684  60.554  1.00 13.82 ? 43   ASN C CA  1 
ATOM   10006 C  C   . ASN C 1 51  ? 38.317  18.388  61.846  1.00 15.33 ? 43   ASN C C   1 
ATOM   10007 O  O   . ASN C 1 51  ? 37.482  18.605  62.728  1.00 14.51 ? 43   ASN C O   1 
ATOM   10008 C  CB  . ASN C 1 51  ? 36.697  18.361  59.918  1.00 16.90 ? 43   ASN C CB  1 
ATOM   10009 C  CG  . ASN C 1 51  ? 36.422  17.862  58.510  1.00 17.92 ? 43   ASN C CG  1 
ATOM   10010 O  OD1 . ASN C 1 51  ? 35.320  17.406  58.195  1.00 23.10 ? 43   ASN C OD1 1 
ATOM   10011 N  ND2 . ASN C 1 51  ? 37.424  17.943  57.660  1.00 17.79 ? 43   ASN C ND2 1 
ATOM   10012 N  N   . HIS C 1 52  ? 39.595  18.753  61.954  1.00 17.59 ? 44   HIS C N   1 
ATOM   10013 C  CA  . HIS C 1 52  ? 40.094  19.393  63.165  1.00 12.63 ? 44   HIS C CA  1 
ATOM   10014 C  C   . HIS C 1 52  ? 41.290  20.252  62.803  1.00 18.41 ? 44   HIS C C   1 
ATOM   10015 O  O   . HIS C 1 52  ? 41.920  20.053  61.765  1.00 18.98 ? 44   HIS C O   1 
ATOM   10016 C  CB  . HIS C 1 52  ? 40.490  18.355  64.224  1.00 12.92 ? 44   HIS C CB  1 
ATOM   10017 C  CG  . HIS C 1 52  ? 41.636  17.474  63.804  1.00 13.89 ? 44   HIS C CG  1 
ATOM   10018 N  ND1 . HIS C 1 52  ? 42.800  17.370  64.533  1.00 17.40 ? 44   HIS C ND1 1 
ATOM   10019 C  CD2 . HIS C 1 52  ? 41.780  16.640  62.745  1.00 19.52 ? 44   HIS C CD2 1 
ATOM   10020 C  CE1 . HIS C 1 52  ? 43.618  16.518  63.938  1.00 21.76 ? 44   HIS C CE1 1 
ATOM   10021 N  NE2 . HIS C 1 52  ? 43.024  16.060  62.849  1.00 22.15 ? 44   HIS C NE2 1 
ATOM   10022 N  N   . ASN C 1 53  ? 41.615  21.200  63.681  1.00 17.34 ? 45   ASN C N   1 
ATOM   10023 C  CA  . ASN C 1 53  ? 42.789  22.056  63.502  1.00 18.41 ? 45   ASN C CA  1 
ATOM   10024 C  C   . ASN C 1 53  ? 43.707  21.947  64.711  1.00 15.01 ? 45   ASN C C   1 
ATOM   10025 O  O   . ASN C 1 53  ? 43.407  22.522  65.774  1.00 14.97 ? 45   ASN C O   1 
ATOM   10026 C  CB  . ASN C 1 53  ? 42.382  23.509  63.281  1.00 14.87 ? 45   ASN C CB  1 
ATOM   10027 C  CG  . ASN C 1 53  ? 43.566  24.393  62.934  1.00 21.15 ? 45   ASN C CG  1 
ATOM   10028 O  OD1 . ASN C 1 53  ? 44.681  23.904  62.743  1.00 18.42 ? 45   ASN C OD1 1 
ATOM   10029 N  ND2 . ASN C 1 53  ? 43.330  25.701  62.845  1.00 16.41 ? 45   ASN C ND2 1 
ATOM   10030 N  N   . PRO C 1 54  ? 44.828  21.229  64.601  1.00 17.09 ? 46   PRO C N   1 
ATOM   10031 C  CA  . PRO C 1 54  ? 45.773  21.156  65.727  1.00 19.92 ? 46   PRO C CA  1 
ATOM   10032 C  C   . PRO C 1 54  ? 46.216  22.519  66.230  1.00 24.03 ? 46   PRO C C   1 
ATOM   10033 O  O   . PRO C 1 54  ? 46.522  22.658  67.419  1.00 21.48 ? 46   PRO C O   1 
ATOM   10034 C  CB  . PRO C 1 54  ? 46.954  20.368  65.142  1.00 25.83 ? 46   PRO C CB  1 
ATOM   10035 C  CG  . PRO C 1 54  ? 46.387  19.610  64.010  1.00 27.26 ? 46   PRO C CG  1 
ATOM   10036 C  CD  . PRO C 1 54  ? 45.296  20.463  63.434  1.00 18.50 ? 46   PRO C CD  1 
ATOM   10037 N  N   . ALA C 1 55  ? 46.246  23.533  65.358  1.00 21.30 ? 47   ALA C N   1 
ATOM   10038 C  CA  . ALA C 1 55  ? 46.627  24.877  65.761  1.00 18.16 ? 47   ALA C CA  1 
ATOM   10039 C  C   . ALA C 1 55  ? 45.599  25.541  66.667  1.00 21.38 ? 47   ALA C C   1 
ATOM   10040 O  O   . ALA C 1 55  ? 45.952  26.480  67.390  1.00 19.41 ? 47   ALA C O   1 
ATOM   10041 C  CB  . ALA C 1 55  ? 46.848  25.754  64.530  1.00 24.10 ? 47   ALA C CB  1 
ATOM   10042 N  N   . ASN C 1 56  ? 44.340  25.096  66.636  1.00 20.41 ? 48   ASN C N   1 
ATOM   10043 C  CA  . ASN C 1 56  ? 43.292  25.659  67.487  1.00 20.87 ? 48   ASN C CA  1 
ATOM   10044 C  C   . ASN C 1 56  ? 42.401  24.533  67.985  1.00 18.99 ? 48   ASN C C   1 
ATOM   10045 O  O   . ASN C 1 56  ? 41.366  24.224  67.380  1.00 15.89 ? 48   ASN C O   1 
ATOM   10046 C  CB  . ASN C 1 56  ? 42.463  26.710  66.748  1.00 22.41 ? 48   ASN C CB  1 
ATOM   10047 C  CG  . ASN C 1 56  ? 41.371  27.317  67.629  1.00 24.06 ? 48   ASN C CG  1 
ATOM   10048 O  OD1 . ASN C 1 56  ? 41.359  27.121  68.845  1.00 17.39 ? 48   ASN C OD1 1 
ATOM   10049 N  ND2 . ASN C 1 56  ? 40.454  28.051  67.015  1.00 18.68 ? 48   ASN C ND2 1 
ATOM   10050 N  N   . PRO C 1 57  ? 42.773  23.895  69.099  1.00 19.93 ? 49   PRO C N   1 
ATOM   10051 C  CA  . PRO C 1 57  ? 41.937  22.817  69.648  1.00 16.59 ? 49   PRO C CA  1 
ATOM   10052 C  C   . PRO C 1 57  ? 40.545  23.270  70.060  1.00 14.95 ? 49   PRO C C   1 
ATOM   10053 O  O   . PRO C 1 57  ? 39.689  22.410  70.306  1.00 17.01 ? 49   PRO C O   1 
ATOM   10054 C  CB  . PRO C 1 57  ? 42.742  22.326  70.860  1.00 21.25 ? 49   PRO C CB  1 
ATOM   10055 C  CG  . PRO C 1 57  ? 44.149  22.790  70.622  1.00 21.86 ? 49   PRO C CG  1 
ATOM   10056 C  CD  . PRO C 1 57  ? 44.041  24.060  69.834  1.00 20.56 ? 49   PRO C CD  1 
ATOM   10057 N  N   . LYS C 1 58  ? 40.288  24.576  70.140  1.00 17.11 ? 50   LYS C N   1 
ATOM   10058 C  CA  . LYS C 1 58  ? 38.963  25.092  70.472  1.00 20.27 ? 50   LYS C CA  1 
ATOM   10059 C  C   . LYS C 1 58  ? 38.200  25.626  69.258  1.00 13.65 ? 50   LYS C C   1 
ATOM   10060 O  O   . LYS C 1 58  ? 37.186  26.310  69.432  1.00 19.26 ? 50   LYS C O   1 
ATOM   10061 C  CB  . LYS C 1 58  ? 39.071  26.180  71.536  1.00 20.45 ? 50   LYS C CB  1 
ATOM   10062 C  CG  . LYS C 1 58  ? 39.630  25.690  72.860  1.00 23.91 ? 50   LYS C CG  1 
ATOM   10063 C  CD  . LYS C 1 58  ? 38.737  24.626  73.477  1.00 23.26 ? 50   LYS C CD  1 
ATOM   10064 C  CE  . LYS C 1 58  ? 39.205  24.251  74.880  1.00 33.25 ? 50   LYS C CE  1 
ATOM   10065 N  NZ  . LYS C 1 58  ? 38.442  23.082  75.409  1.00 33.53 ? 50   LYS C NZ  1 
ATOM   10066 N  N   . PHE C 1 59  ? 38.656  25.326  68.044  1.00 13.29 ? 51   PHE C N   1 
ATOM   10067 C  CA  . PHE C 1 59  ? 37.912  25.657  66.833  1.00 14.97 ? 51   PHE C CA  1 
ATOM   10068 C  C   . PHE C 1 59  ? 36.438  25.273  66.976  1.00 14.88 ? 51   PHE C C   1 
ATOM   10069 O  O   . PHE C 1 59  ? 36.117  24.114  67.238  1.00 13.62 ? 51   PHE C O   1 
ATOM   10070 C  CB  . PHE C 1 59  ? 38.550  24.931  65.646  1.00 13.72 ? 51   PHE C CB  1 
ATOM   10071 C  CG  . PHE C 1 59  ? 37.787  25.070  64.369  1.00 18.98 ? 51   PHE C CG  1 
ATOM   10072 C  CD1 . PHE C 1 59  ? 37.213  26.287  64.014  1.00 17.71 ? 51   PHE C CD1 1 
ATOM   10073 C  CD2 . PHE C 1 59  ? 37.638  23.982  63.522  1.00 17.93 ? 51   PHE C CD2 1 
ATOM   10074 C  CE1 . PHE C 1 59  ? 36.503  26.411  62.842  1.00 15.98 ? 51   PHE C CE1 1 
ATOM   10075 C  CE2 . PHE C 1 59  ? 36.929  24.094  62.348  1.00 17.80 ? 51   PHE C CE2 1 
ATOM   10076 C  CZ  . PHE C 1 59  ? 36.357  25.312  62.003  1.00 15.94 ? 51   PHE C CZ  1 
ATOM   10077 N  N   . TYR C 1 60  ? 35.547  26.258  66.817  1.00 16.94 ? 52   TYR C N   1 
ATOM   10078 C  CA  . TYR C 1 60  ? 34.148  26.066  67.204  1.00 17.30 ? 52   TYR C CA  1 
ATOM   10079 C  C   . TYR C 1 60  ? 33.498  24.918  66.446  1.00 17.35 ? 52   TYR C C   1 
ATOM   10080 O  O   . TYR C 1 60  ? 32.676  24.191  67.013  1.00 16.17 ? 52   TYR C O   1 
ATOM   10081 C  CB  . TYR C 1 60  ? 33.332  27.338  66.962  1.00 13.58 ? 52   TYR C CB  1 
ATOM   10082 C  CG  . TYR C 1 60  ? 33.708  28.543  67.789  1.00 16.37 ? 52   TYR C CG  1 
ATOM   10083 C  CD1 . TYR C 1 60  ? 34.261  28.413  69.062  1.00 17.10 ? 52   TYR C CD1 1 
ATOM   10084 C  CD2 . TYR C 1 60  ? 33.495  29.817  67.295  1.00 19.62 ? 52   TYR C CD2 1 
ATOM   10085 C  CE1 . TYR C 1 60  ? 34.599  29.542  69.804  1.00 16.39 ? 52   TYR C CE1 1 
ATOM   10086 C  CE2 . TYR C 1 60  ? 33.824  30.929  68.014  1.00 21.83 ? 52   TYR C CE2 1 
ATOM   10087 C  CZ  . TYR C 1 60  ? 34.375  30.794  69.263  1.00 21.48 ? 52   TYR C CZ  1 
ATOM   10088 O  OH  . TYR C 1 60  ? 34.687  31.930  69.954  1.00 19.22 ? 52   TYR C OH  1 
ATOM   10089 N  N   . ASN C 1 61  ? 33.809  24.768  65.154  1.00 19.78 ? 53   ASN C N   1 
ATOM   10090 C  CA  . ASN C 1 61  ? 33.130  23.792  64.308  1.00 15.56 ? 53   ASN C CA  1 
ATOM   10091 C  C   . ASN C 1 61  ? 33.956  22.524  64.071  1.00 15.92 ? 53   ASN C C   1 
ATOM   10092 O  O   . ASN C 1 61  ? 33.689  21.793  63.116  1.00 16.50 ? 53   ASN C O   1 
ATOM   10093 C  CB  . ASN C 1 61  ? 32.739  24.413  62.964  1.00 15.15 ? 53   ASN C CB  1 
ATOM   10094 C  CG  . ASN C 1 61  ? 31.600  23.660  62.295  1.00 12.75 ? 53   ASN C CG  1 
ATOM   10095 O  OD1 . ASN C 1 61  ? 30.615  23.301  62.949  1.00 12.87 ? 53   ASN C OD1 1 
ATOM   10096 N  ND2 . ASN C 1 61  ? 31.739  23.395  60.996  1.00 14.96 ? 53   ASN C ND2 1 
ATOM   10097 N  N   . ARG C 1 62  ? 34.935  22.233  64.923  1.00 12.44 ? 54   ARG C N   1 
ATOM   10098 C  CA  . ARG C 1 62  ? 35.677  20.983  64.780  1.00 11.67 ? 54   ARG C CA  1 
ATOM   10099 C  C   . ARG C 1 62  ? 34.750  19.788  65.007  1.00 10.34 ? 54   ARG C C   1 
ATOM   10100 O  O   . ARG C 1 62  ? 33.791  19.860  65.783  1.00 14.81 ? 54   ARG C O   1 
ATOM   10101 C  CB  . ARG C 1 62  ? 36.839  20.941  65.785  1.00 15.75 ? 54   ARG C CB  1 
ATOM   10102 C  CG  . ARG C 1 62  ? 36.355  20.896  67.233  1.00 10.74 ? 54   ARG C CG  1 
ATOM   10103 C  CD  . ARG C 1 62  ? 37.496  21.006  68.247  1.00 13.78 ? 54   ARG C CD  1 
ATOM   10104 N  NE  . ARG C 1 62  ? 37.007  20.780  69.606  1.00 13.90 ? 54   ARG C NE  1 
ATOM   10105 C  CZ  . ARG C 1 62  ? 36.382  21.697  70.338  1.00 15.81 ? 54   ARG C CZ  1 
ATOM   10106 N  NH1 . ARG C 1 62  ? 36.175  22.908  69.844  1.00 14.50 ? 54   ARG C NH1 1 
ATOM   10107 N  NH2 . ARG C 1 62  ? 35.965  21.407  71.566  1.00 15.28 ? 54   ARG C NH2 1 
ATOM   10108 N  N   . ASP C 1 63  ? 35.023  18.685  64.300  1.00 11.61 ? 55   ASP C N   1 
ATOM   10109 C  CA  . ASP C 1 63  ? 34.443  17.412  64.710  1.00 10.23 ? 55   ASP C CA  1 
ATOM   10110 C  C   . ASP C 1 63  ? 34.904  17.102  66.127  1.00 13.67 ? 55   ASP C C   1 
ATOM   10111 O  O   . ASP C 1 63  ? 36.009  17.461  66.529  1.00 14.97 ? 55   ASP C O   1 
ATOM   10112 C  CB  . ASP C 1 63  ? 34.864  16.258  63.787  1.00 12.58 ? 55   ASP C CB  1 
ATOM   10113 C  CG  . ASP C 1 63  ? 34.297  16.370  62.380  1.00 15.11 ? 55   ASP C CG  1 
ATOM   10114 O  OD1 . ASP C 1 63  ? 33.195  16.936  62.198  1.00 13.89 ? 55   ASP C OD1 1 
ATOM   10115 O  OD2 . ASP C 1 63  ? 34.961  15.855  61.447  1.00 14.44 ? 55   ASP C OD2 1 
ATOM   10116 N  N   . ARG C 1 64  ? 34.038  16.444  66.889  1.00 12.93 ? 56   ARG C N   1 
ATOM   10117 C  CA  . ARG C 1 64  ? 34.346  16.030  68.250  1.00 13.59 ? 56   ARG C CA  1 
ATOM   10118 C  C   . ARG C 1 64  ? 34.680  14.546  68.234  1.00 12.47 ? 56   ARG C C   1 
ATOM   10119 O  O   . ARG C 1 64  ? 33.905  13.739  67.712  1.00 17.34 ? 56   ARG C O   1 
ATOM   10120 C  CB  . ARG C 1 64  ? 33.161  16.299  69.179  1.00 11.57 ? 56   ARG C CB  1 
ATOM   10121 C  CG  . ARG C 1 64  ? 33.183  17.642  69.913  1.00 17.99 ? 56   ARG C CG  1 
ATOM   10122 C  CD  . ARG C 1 64  ? 33.199  18.851  68.992  1.00 17.80 ? 56   ARG C CD  1 
ATOM   10123 N  NE  . ARG C 1 64  ? 32.984  20.087  69.744  1.00 14.64 ? 56   ARG C NE  1 
ATOM   10124 C  CZ  . ARG C 1 64  ? 32.847  21.287  69.194  1.00 16.31 ? 56   ARG C CZ  1 
ATOM   10125 N  NH1 . ARG C 1 64  ? 32.916  21.424  67.876  1.00 16.29 ? 56   ARG C NH1 1 
ATOM   10126 N  NH2 . ARG C 1 64  ? 32.634  22.353  69.962  1.00 17.00 ? 56   ARG C NH2 1 
ATOM   10127 N  N   . PHE C 1 65  ? 35.840  14.189  68.786  1.00 14.66 ? 57   PHE C N   1 
ATOM   10128 C  CA  . PHE C 1 65  ? 36.224  12.797  68.950  1.00 13.40 ? 57   PHE C CA  1 
ATOM   10129 C  C   . PHE C 1 65  ? 36.210  12.438  70.428  1.00 18.14 ? 57   PHE C C   1 
ATOM   10130 O  O   . PHE C 1 65  ? 36.726  13.188  71.264  1.00 14.65 ? 57   PHE C O   1 
ATOM   10131 C  CB  . PHE C 1 65  ? 37.621  12.510  68.369  1.00 15.09 ? 57   PHE C CB  1 
ATOM   10132 C  CG  . PHE C 1 65  ? 38.092  11.096  68.609  1.00 15.98 ? 57   PHE C CG  1 
ATOM   10133 C  CD1 . PHE C 1 65  ? 37.608  10.047  67.835  1.00 16.75 ? 57   PHE C CD1 1 
ATOM   10134 C  CD2 . PHE C 1 65  ? 38.999  10.813  69.617  1.00 17.94 ? 57   PHE C CD2 1 
ATOM   10135 C  CE1 . PHE C 1 65  ? 38.018  8.740   68.067  1.00 13.91 ? 57   PHE C CE1 1 
ATOM   10136 C  CE2 . PHE C 1 65  ? 39.428  9.516   69.852  1.00 15.74 ? 57   PHE C CE2 1 
ATOM   10137 C  CZ  . PHE C 1 65  ? 38.942  8.475   69.075  1.00 18.84 ? 57   PHE C CZ  1 
ATOM   10138 N  N   . VAL C 1 66  ? 35.655  11.274  70.745  1.00 11.15 ? 58   VAL C N   1 
ATOM   10139 C  CA  . VAL C 1 66  ? 35.579  10.809  72.124  1.00 11.11 ? 58   VAL C CA  1 
ATOM   10140 C  C   . VAL C 1 66  ? 36.098  9.383   72.172  1.00 11.43 ? 58   VAL C C   1 
ATOM   10141 O  O   . VAL C 1 66  ? 35.554  8.497   71.505  1.00 14.87 ? 58   VAL C O   1 
ATOM   10142 C  CB  . VAL C 1 66  ? 34.149  10.876  72.680  1.00 11.55 ? 58   VAL C CB  1 
ATOM   10143 C  CG1 . VAL C 1 66  ? 34.073  10.185  74.025  1.00 12.86 ? 58   VAL C CG1 1 
ATOM   10144 C  CG2 . VAL C 1 66  ? 33.688  12.329  72.781  1.00 13.13 ? 58   VAL C CG2 1 
ATOM   10145 N  N   . LEU C 1 67  ? 37.142  9.165   72.970  1.00 13.28 ? 59   LEU C N   1 
ATOM   10146 C  CA  . LEU C 1 67  ? 37.669  7.835   73.277  1.00 12.75 ? 59   LEU C CA  1 
ATOM   10147 C  C   . LEU C 1 67  ? 36.944  7.358   74.526  1.00 16.46 ? 59   LEU C C   1 
ATOM   10148 O  O   . LEU C 1 67  ? 37.345  7.659   75.653  1.00 16.35 ? 59   LEU C O   1 
ATOM   10149 C  CB  . LEU C 1 67  ? 39.176  7.895   73.490  1.00 12.62 ? 59   LEU C CB  1 
ATOM   10150 C  CG  . LEU C 1 67  ? 39.863  6.574   73.847  1.00 17.59 ? 59   LEU C CG  1 
ATOM   10151 C  CD1 . LEU C 1 67  ? 39.870  5.646   72.651  1.00 13.85 ? 59   LEU C CD1 1 
ATOM   10152 C  CD2 . LEU C 1 67  ? 41.280  6.832   74.351  1.00 22.16 ? 59   LEU C CD2 1 
ATOM   10153 N  N   . SER C 1 68  ? 35.835  6.638   74.330  1.00 13.51 ? 60   SER C N   1 
ATOM   10154 C  CA  . SER C 1 68  ? 35.013  6.255   75.476  1.00 15.73 ? 60   SER C CA  1 
ATOM   10155 C  C   . SER C 1 68  ? 35.751  5.260   76.355  1.00 20.03 ? 60   SER C C   1 
ATOM   10156 O  O   . SER C 1 68  ? 35.662  5.328   77.587  1.00 21.16 ? 60   SER C O   1 
ATOM   10157 C  CB  . SER C 1 68  ? 33.668  5.686   75.015  1.00 14.16 ? 60   SER C CB  1 
ATOM   10158 O  OG  . SER C 1 68  ? 32.770  5.507   76.109  1.00 18.00 ? 60   SER C OG  1 
ATOM   10159 N  N   . ASN C 1 69  ? 36.500  4.342   75.743  1.00 18.77 ? 61   ASN C N   1 
ATOM   10160 C  CA  . ASN C 1 69  ? 37.318  3.391   76.493  1.00 22.93 ? 61   ASN C CA  1 
ATOM   10161 C  C   . ASN C 1 69  ? 38.628  4.081   76.878  1.00 23.15 ? 61   ASN C C   1 
ATOM   10162 O  O   . ASN C 1 69  ? 39.698  3.836   76.314  1.00 24.34 ? 61   ASN C O   1 
ATOM   10163 C  CB  . ASN C 1 69  ? 37.537  2.106   75.692  1.00 25.83 ? 61   ASN C CB  1 
ATOM   10164 C  CG  . ASN C 1 69  ? 37.645  2.336   74.181  1.00 28.26 ? 61   ASN C CG  1 
ATOM   10165 O  OD1 . ASN C 1 69  ? 37.533  3.457   73.689  1.00 28.10 ? 61   ASN C OD1 1 
ATOM   10166 N  ND2 . ASN C 1 69  ? 37.868  1.249   73.439  1.00 33.21 ? 61   ASN C ND2 1 
ATOM   10167 N  N   . GLY C 1 70  ? 38.532  4.948   77.896  1.00 20.87 ? 62   GLY C N   1 
ATOM   10168 C  CA  . GLY C 1 70  ? 39.607  5.867   78.253  1.00 19.83 ? 62   GLY C CA  1 
ATOM   10169 C  C   . GLY C 1 70  ? 40.893  5.212   78.726  1.00 24.94 ? 62   GLY C C   1 
ATOM   10170 O  O   . GLY C 1 70  ? 41.941  5.867   78.742  1.00 23.90 ? 62   GLY C O   1 
ATOM   10171 N  N   . HIS C 1 71  ? 40.844  3.940   79.122  1.00 24.93 ? 63   HIS C N   1 
ATOM   10172 C  CA  . HIS C 1 71  ? 42.076  3.214   79.424  1.00 25.97 ? 63   HIS C CA  1 
ATOM   10173 C  C   . HIS C 1 71  ? 42.997  3.129   78.210  1.00 26.50 ? 63   HIS C C   1 
ATOM   10174 O  O   . HIS C 1 71  ? 44.217  2.984   78.365  1.00 26.86 ? 63   HIS C O   1 
ATOM   10175 C  CB  . HIS C 1 71  ? 41.743  1.808   79.913  1.00 26.73 ? 63   HIS C CB  1 
ATOM   10176 C  CG  . HIS C 1 71  ? 40.823  1.065   78.994  1.00 27.63 ? 63   HIS C CG  1 
ATOM   10177 N  ND1 . HIS C 1 71  ? 39.451  1.122   79.111  1.00 28.61 ? 63   HIS C ND1 1 
ATOM   10178 C  CD2 . HIS C 1 71  ? 41.077  0.260   77.934  1.00 30.16 ? 63   HIS C CD2 1 
ATOM   10179 C  CE1 . HIS C 1 71  ? 38.898  0.380   78.168  1.00 31.80 ? 63   HIS C CE1 1 
ATOM   10180 N  NE2 . HIS C 1 71  ? 39.862  -0.151  77.437  1.00 29.84 ? 63   HIS C NE2 1 
ATOM   10181 N  N   . ALA C 1 72  ? 42.436  3.205   77.000  1.00 20.40 ? 64   ALA C N   1 
ATOM   10182 C  CA  . ALA C 1 72  ? 43.217  3.185   75.765  1.00 16.54 ? 64   ALA C CA  1 
ATOM   10183 C  C   . ALA C 1 72  ? 43.843  4.549   75.485  1.00 17.16 ? 64   ALA C C   1 
ATOM   10184 O  O   . ALA C 1 72  ? 44.035  4.925   74.325  1.00 17.48 ? 64   ALA C O   1 
ATOM   10185 C  CB  . ALA C 1 72  ? 42.332  2.764   74.586  1.00 14.62 ? 64   ALA C CB  1 
ATOM   10186 N  N   . SER C 1 73  ? 44.170  5.288   76.548  1.00 16.25 ? 65   SER C N   1 
ATOM   10187 C  CA  . SER C 1 73  ? 44.590  6.681   76.429  1.00 14.19 ? 65   SER C CA  1 
ATOM   10188 C  C   . SER C 1 73  ? 45.762  6.877   75.462  1.00 18.25 ? 65   SER C C   1 
ATOM   10189 O  O   . SER C 1 73  ? 45.842  7.902   74.772  1.00 16.91 ? 65   SER C O   1 
ATOM   10190 C  CB  . SER C 1 73  ? 44.957  7.198   77.815  1.00 19.45 ? 65   SER C CB  1 
ATOM   10191 O  OG  . SER C 1 73  ? 45.979  6.380   78.360  1.00 19.51 ? 65   SER C OG  1 
ATOM   10192 N  N   . MET C 1 74  ? 46.700  5.925   75.412  1.00 18.56 ? 66   MET C N   1 
ATOM   10193 C  CA  . MET C 1 74  ? 47.875  6.140   74.566  1.00 15.61 ? 66   MET C CA  1 
ATOM   10194 C  C   . MET C 1 74  ? 47.503  6.224   73.089  1.00 19.76 ? 66   MET C C   1 
ATOM   10195 O  O   . MET C 1 74  ? 48.227  6.846   72.303  1.00 17.72 ? 66   MET C O   1 
ATOM   10196 C  CB  . MET C 1 74  ? 48.913  5.039   74.781  1.00 19.11 ? 66   MET C CB  1 
ATOM   10197 C  CG  . MET C 1 74  ? 49.944  5.359   75.861  1.00 18.94 ? 66   MET C CG  1 
ATOM   10198 S  SD  . MET C 1 74  ? 50.741  6.968   75.645  1.00 18.58 ? 66   MET C SD  1 
ATOM   10199 C  CE  . MET C 1 74  ? 51.366  6.878   73.953  1.00 16.61 ? 66   MET C CE  1 
ATOM   10200 N  N   . LEU C 1 75  ? 46.394  5.598   72.688  1.00 20.09 ? 67   LEU C N   1 
ATOM   10201 C  CA  . LEU C 1 75  ? 45.917  5.765   71.315  1.00 18.37 ? 67   LEU C CA  1 
ATOM   10202 C  C   . LEU C 1 75  ? 45.632  7.236   71.016  1.00 15.44 ? 67   LEU C C   1 
ATOM   10203 O  O   . LEU C 1 75  ? 46.057  7.767   69.986  1.00 18.11 ? 67   LEU C O   1 
ATOM   10204 C  CB  . LEU C 1 75  ? 44.663  4.914   71.090  1.00 20.82 ? 67   LEU C CB  1 
ATOM   10205 C  CG  . LEU C 1 75  ? 43.950  5.005   69.733  1.00 23.64 ? 67   LEU C CG  1 
ATOM   10206 C  CD1 . LEU C 1 75  ? 44.546  4.045   68.754  1.00 24.44 ? 67   LEU C CD1 1 
ATOM   10207 C  CD2 . LEU C 1 75  ? 42.445  4.740   69.879  1.00 29.73 ? 67   LEU C CD2 1 
ATOM   10208 N  N   . LEU C 1 76  ? 44.926  7.917   71.928  1.00 19.15 ? 68   LEU C N   1 
ATOM   10209 C  CA  . LEU C 1 76  ? 44.587  9.322   71.719  1.00 13.10 ? 68   LEU C CA  1 
ATOM   10210 C  C   . LEU C 1 76  ? 45.813  10.223  71.844  1.00 15.88 ? 68   LEU C C   1 
ATOM   10211 O  O   . LEU C 1 76  ? 45.964  11.184  71.082  1.00 16.37 ? 68   LEU C O   1 
ATOM   10212 C  CB  . LEU C 1 76  ? 43.508  9.745   72.712  1.00 11.81 ? 68   LEU C CB  1 
ATOM   10213 C  CG  . LEU C 1 76  ? 43.132  11.231  72.657  1.00 16.28 ? 68   LEU C CG  1 
ATOM   10214 C  CD1 . LEU C 1 76  ? 42.641  11.628  71.269  1.00 16.46 ? 68   LEU C CD1 1 
ATOM   10215 C  CD2 . LEU C 1 76  ? 42.105  11.588  73.717  1.00 18.27 ? 68   LEU C CD2 1 
ATOM   10216 N  N   . TYR C 1 77  ? 46.703  9.929   72.800  1.00 15.37 ? 69   TYR C N   1 
ATOM   10217 C  CA  . TYR C 1 77  ? 47.957  10.676  72.899  1.00 14.65 ? 69   TYR C CA  1 
ATOM   10218 C  C   . TYR C 1 77  ? 48.798  10.509  71.643  1.00 14.56 ? 69   TYR C C   1 
ATOM   10219 O  O   . TYR C 1 77  ? 49.392  11.477  71.150  1.00 17.86 ? 69   TYR C O   1 
ATOM   10220 C  CB  . TYR C 1 77  ? 48.751  10.223  74.128  1.00 15.08 ? 69   TYR C CB  1 
ATOM   10221 C  CG  . TYR C 1 77  ? 48.065  10.503  75.449  1.00 13.70 ? 69   TYR C CG  1 
ATOM   10222 C  CD1 . TYR C 1 77  ? 47.170  11.564  75.586  1.00 22.53 ? 69   TYR C CD1 1 
ATOM   10223 C  CD2 . TYR C 1 77  ? 48.316  9.708   76.566  1.00 17.53 ? 69   TYR C CD2 1 
ATOM   10224 C  CE1 . TYR C 1 77  ? 46.536  11.828  76.814  1.00 20.53 ? 69   TYR C CE1 1 
ATOM   10225 C  CE2 . TYR C 1 77  ? 47.687  9.960   77.796  1.00 18.80 ? 69   TYR C CE2 1 
ATOM   10226 C  CZ  . TYR C 1 77  ? 46.797  11.016  77.909  1.00 22.49 ? 69   TYR C CZ  1 
ATOM   10227 O  OH  . TYR C 1 77  ? 46.183  11.266  79.126  1.00 19.49 ? 69   TYR C OH  1 
ATOM   10228 N  N   . SER C 1 78  ? 48.866  9.285   71.111  1.00 19.11 ? 70   SER C N   1 
ATOM   10229 C  CA  . SER C 1 78  ? 49.600  9.068   69.869  1.00 17.59 ? 70   SER C CA  1 
ATOM   10230 C  C   . SER C 1 78  ? 49.008  9.895   68.737  1.00 21.49 ? 70   SER C C   1 
ATOM   10231 O  O   . SER C 1 78  ? 49.742  10.528  67.970  1.00 21.00 ? 70   SER C O   1 
ATOM   10232 C  CB  . SER C 1 78  ? 49.590  7.589   69.496  1.00 16.94 ? 70   SER C CB  1 
ATOM   10233 O  OG  . SER C 1 78  ? 50.356  6.817   70.412  1.00 22.30 ? 70   SER C OG  1 
ATOM   10234 N  N   . LEU C 1 79  ? 47.676  9.909   68.628  1.00 17.46 ? 71   LEU C N   1 
ATOM   10235 C  CA  . LEU C 1 79  ? 47.024  10.667  67.565  1.00 18.76 ? 71   LEU C CA  1 
ATOM   10236 C  C   . LEU C 1 79  ? 47.288  12.159  67.705  1.00 20.96 ? 71   LEU C C   1 
ATOM   10237 O  O   . LEU C 1 79  ? 47.553  12.850  66.711  1.00 19.63 ? 71   LEU C O   1 
ATOM   10238 C  CB  . LEU C 1 79  ? 45.523  10.393  67.587  1.00 19.67 ? 71   LEU C CB  1 
ATOM   10239 C  CG  . LEU C 1 79  ? 45.113  9.028   67.053  1.00 20.54 ? 71   LEU C CG  1 
ATOM   10240 C  CD1 . LEU C 1 79  ? 43.717  8.655   67.554  1.00 15.09 ? 71   LEU C CD1 1 
ATOM   10241 C  CD2 . LEU C 1 79  ? 45.160  9.065   65.546  1.00 21.79 ? 71   LEU C CD2 1 
ATOM   10242 N  N   . LEU C 1 80  ? 47.225  12.673  68.936  1.00 19.17 ? 72   LEU C N   1 
ATOM   10243 C  CA  . LEU C 1 80  ? 47.445  14.098  69.158  1.00 18.35 ? 72   LEU C CA  1 
ATOM   10244 C  C   . LEU C 1 80  ? 48.883  14.479  68.834  1.00 19.77 ? 72   LEU C C   1 
ATOM   10245 O  O   . LEU C 1 80  ? 49.142  15.495  68.177  1.00 20.55 ? 72   LEU C O   1 
ATOM   10246 C  CB  . LEU C 1 80  ? 47.094  14.460  70.610  1.00 18.41 ? 72   LEU C CB  1 
ATOM   10247 C  CG  . LEU C 1 80  ? 45.634  14.371  71.060  1.00 19.00 ? 72   LEU C CG  1 
ATOM   10248 C  CD1 . LEU C 1 80  ? 45.531  14.646  72.567  1.00 13.44 ? 72   LEU C CD1 1 
ATOM   10249 C  CD2 . LEU C 1 80  ? 44.759  15.345  70.285  1.00 19.72 ? 72   LEU C CD2 1 
ATOM   10250 N  N   . HIS C 1 81  ? 49.838  13.675  69.297  1.00 15.87 ? 73   HIS C N   1 
ATOM   10251 C  CA  . HIS C 1 81  ? 51.239  13.928  68.973  1.00 17.85 ? 73   HIS C CA  1 
ATOM   10252 C  C   . HIS C 1 81  ? 51.478  13.901  67.465  1.00 19.30 ? 73   HIS C C   1 
ATOM   10253 O  O   . HIS C 1 81  ? 52.136  14.789  66.916  1.00 23.95 ? 73   HIS C O   1 
ATOM   10254 C  CB  . HIS C 1 81  ? 52.137  12.899  69.656  1.00 20.80 ? 73   HIS C CB  1 
ATOM   10255 C  CG  . HIS C 1 81  ? 53.579  13.030  69.272  1.00 21.63 ? 73   HIS C CG  1 
ATOM   10256 N  ND1 . HIS C 1 81  ? 54.314  14.168  69.533  1.00 23.53 ? 73   HIS C ND1 1 
ATOM   10257 C  CD2 . HIS C 1 81  ? 54.412  12.187  68.617  1.00 21.14 ? 73   HIS C CD2 1 
ATOM   10258 C  CE1 . HIS C 1 81  ? 55.542  14.013  69.071  1.00 24.28 ? 73   HIS C CE1 1 
ATOM   10259 N  NE2 . HIS C 1 81  ? 55.627  12.823  68.504  1.00 24.69 ? 73   HIS C NE2 1 
ATOM   10260 N  N   . LEU C 1 82  ? 50.949  12.881  66.782  1.00 22.98 ? 74   LEU C N   1 
ATOM   10261 C  CA  . LEU C 1 82  ? 51.275  12.684  65.370  1.00 23.76 ? 74   LEU C CA  1 
ATOM   10262 C  C   . LEU C 1 82  ? 50.657  13.757  64.486  1.00 19.62 ? 74   LEU C C   1 
ATOM   10263 O  O   . LEU C 1 82  ? 51.257  14.150  63.477  1.00 23.95 ? 74   LEU C O   1 
ATOM   10264 C  CB  . LEU C 1 82  ? 50.816  11.300  64.905  1.00 23.72 ? 74   LEU C CB  1 
ATOM   10265 C  CG  . LEU C 1 82  ? 51.658  10.091  65.320  1.00 24.23 ? 74   LEU C CG  1 
ATOM   10266 C  CD1 . LEU C 1 82  ? 50.877  8.817   65.040  1.00 31.48 ? 74   LEU C CD1 1 
ATOM   10267 C  CD2 . LEU C 1 82  ? 52.997  10.079  64.591  1.00 24.35 ? 74   LEU C CD2 1 
ATOM   10268 N  N   . THR C 1 83  ? 49.454  14.224  64.822  1.00 18.16 ? 75   THR C N   1 
ATOM   10269 C  CA  . THR C 1 83  ? 48.781  15.170  63.944  1.00 21.83 ? 75   THR C CA  1 
ATOM   10270 C  C   . THR C 1 83  ? 49.219  16.609  64.173  1.00 24.25 ? 75   THR C C   1 
ATOM   10271 O  O   . THR C 1 83  ? 48.920  17.463  63.335  1.00 26.79 ? 75   THR C O   1 
ATOM   10272 C  CB  . THR C 1 83  ? 47.257  15.050  64.089  1.00 24.72 ? 75   THR C CB  1 
ATOM   10273 O  OG1 . THR C 1 83  ? 46.869  15.227  65.461  1.00 23.04 ? 75   THR C OG1 1 
ATOM   10274 C  CG2 . THR C 1 83  ? 46.784  13.689  63.575  1.00 19.68 ? 75   THR C CG2 1 
ATOM   10275 N  N   . GLY C 1 84  ? 49.928  16.899  65.263  1.00 23.72 ? 76   GLY C N   1 
ATOM   10276 C  CA  . GLY C 1 84  ? 50.573  18.192  65.389  1.00 26.72 ? 76   GLY C CA  1 
ATOM   10277 C  C   . GLY C 1 84  ? 50.146  19.027  66.577  1.00 25.02 ? 76   GLY C C   1 
ATOM   10278 O  O   . GLY C 1 84  ? 50.501  20.204  66.658  1.00 23.63 ? 76   GLY C O   1 
ATOM   10279 N  N   . TYR C 1 85  ? 49.395  18.436  67.504  1.00 21.25 ? 77   TYR C N   1 
ATOM   10280 C  CA  . TYR C 1 85  ? 49.009  19.131  68.725  1.00 20.03 ? 77   TYR C CA  1 
ATOM   10281 C  C   . TYR C 1 85  ? 50.226  19.369  69.611  1.00 24.71 ? 77   TYR C C   1 
ATOM   10282 O  O   . TYR C 1 85  ? 51.303  18.795  69.413  1.00 22.28 ? 77   TYR C O   1 
ATOM   10283 C  CB  . TYR C 1 85  ? 47.954  18.332  69.497  1.00 19.32 ? 77   TYR C CB  1 
ATOM   10284 C  CG  . TYR C 1 85  ? 46.620  18.343  68.812  1.00 19.37 ? 77   TYR C CG  1 
ATOM   10285 C  CD1 . TYR C 1 85  ? 46.402  17.570  67.680  1.00 17.58 ? 77   TYR C CD1 1 
ATOM   10286 C  CD2 . TYR C 1 85  ? 45.585  19.150  69.270  1.00 18.29 ? 77   TYR C CD2 1 
ATOM   10287 C  CE1 . TYR C 1 85  ? 45.187  17.584  67.033  1.00 16.34 ? 77   TYR C CE1 1 
ATOM   10288 C  CE2 . TYR C 1 85  ? 44.364  19.168  68.631  1.00 18.77 ? 77   TYR C CE2 1 
ATOM   10289 C  CZ  . TYR C 1 85  ? 44.175  18.388  67.506  1.00 19.63 ? 77   TYR C CZ  1 
ATOM   10290 O  OH  . TYR C 1 85  ? 42.964  18.391  66.852  1.00 24.83 ? 77   TYR C OH  1 
ATOM   10291 N  N   . ASN C 1 86  ? 50.037  20.234  70.611  1.00 26.05 ? 78   ASN C N   1 
ATOM   10292 C  CA  . ASN C 1 86  ? 51.080  20.535  71.593  1.00 29.36 ? 78   ASN C CA  1 
ATOM   10293 C  C   . ASN C 1 86  ? 51.180  19.372  72.579  1.00 32.90 ? 78   ASN C C   1 
ATOM   10294 O  O   . ASN C 1 86  ? 50.792  19.448  73.748  1.00 40.45 ? 78   ASN C O   1 
ATOM   10295 C  CB  . ASN C 1 86  ? 50.798  21.850  72.304  1.00 38.95 ? 78   ASN C CB  1 
ATOM   10296 C  CG  . ASN C 1 86  ? 51.823  22.156  73.386  1.00 50.82 ? 78   ASN C CG  1 
ATOM   10297 O  OD1 . ASN C 1 86  ? 51.500  22.178  74.574  1.00 59.32 ? 78   ASN C OD1 1 
ATOM   10298 N  ND2 . ASN C 1 86  ? 53.070  22.365  72.981  1.00 51.88 ? 78   ASN C ND2 1 
ATOM   10299 N  N   . LEU C 1 87  ? 51.698  18.263  72.067  1.00 24.20 ? 79   LEU C N   1 
ATOM   10300 C  CA  . LEU C 1 87  ? 51.965  17.077  72.876  1.00 19.68 ? 79   LEU C CA  1 
ATOM   10301 C  C   . LEU C 1 87  ? 53.186  16.433  72.242  1.00 23.66 ? 79   LEU C C   1 
ATOM   10302 O  O   . LEU C 1 87  ? 53.111  15.963  71.104  1.00 21.17 ? 79   LEU C O   1 
ATOM   10303 C  CB  . LEU C 1 87  ? 50.764  16.132  72.892  1.00 20.58 ? 79   LEU C CB  1 
ATOM   10304 C  CG  . LEU C 1 87  ? 50.710  15.018  73.946  1.00 22.44 ? 79   LEU C CG  1 
ATOM   10305 C  CD1 . LEU C 1 87  ? 50.709  15.596  75.357  1.00 16.38 ? 79   LEU C CD1 1 
ATOM   10306 C  CD2 . LEU C 1 87  ? 49.499  14.121  73.721  1.00 19.58 ? 79   LEU C CD2 1 
ATOM   10307 N  N   . SER C 1 88  ? 54.309  16.444  72.951  1.00 21.41 ? 80   SER C N   1 
ATOM   10308 C  CA  . SER C 1 88  ? 55.595  16.071  72.379  1.00 24.67 ? 80   SER C CA  1 
ATOM   10309 C  C   . SER C 1 88  ? 55.953  14.619  72.690  1.00 21.69 ? 80   SER C C   1 
ATOM   10310 O  O   . SER C 1 88  ? 55.314  13.943  73.501  1.00 22.04 ? 80   SER C O   1 
ATOM   10311 C  CB  . SER C 1 88  ? 56.689  16.995  72.912  1.00 26.64 ? 80   SER C CB  1 
ATOM   10312 O  OG  . SER C 1 88  ? 56.851  16.779  74.305  1.00 28.62 ? 80   SER C OG  1 
ATOM   10313 N  N   . ILE C 1 89  ? 57.015  14.147  72.030  1.00 23.08 ? 81   ILE C N   1 
ATOM   10314 C  CA  . ILE C 1 89  ? 57.577  12.843  72.374  1.00 23.45 ? 81   ILE C CA  1 
ATOM   10315 C  C   . ILE C 1 89  ? 57.953  12.794  73.856  1.00 23.54 ? 81   ILE C C   1 
ATOM   10316 O  O   . ILE C 1 89  ? 57.712  11.791  74.539  1.00 26.13 ? 81   ILE C O   1 
ATOM   10317 C  CB  . ILE C 1 89  ? 58.777  12.525  71.459  1.00 32.63 ? 81   ILE C CB  1 
ATOM   10318 C  CG1 . ILE C 1 89  ? 58.297  11.905  70.144  1.00 34.16 ? 81   ILE C CG1 1 
ATOM   10319 C  CG2 . ILE C 1 89  ? 59.772  11.603  72.153  1.00 37.40 ? 81   ILE C CG2 1 
ATOM   10320 C  CD1 . ILE C 1 89  ? 57.685  10.514  70.305  1.00 29.14 ? 81   ILE C CD1 1 
ATOM   10321 N  N   . GLU C 1 90  ? 58.549  13.872  74.382  1.00 24.51 ? 82   GLU C N   1 
ATOM   10322 C  CA  . GLU C 1 90  ? 58.871  13.890  75.810  1.00 27.18 ? 82   GLU C CA  1 
ATOM   10323 C  C   . GLU C 1 90  ? 57.614  13.741  76.661  1.00 25.04 ? 82   GLU C C   1 
ATOM   10324 O  O   . GLU C 1 90  ? 57.632  13.056  77.689  1.00 27.57 ? 82   GLU C O   1 
ATOM   10325 C  CB  . GLU C 1 90  ? 59.621  15.170  76.179  1.00 34.13 ? 82   GLU C CB  1 
ATOM   10326 C  CG  . GLU C 1 90  ? 61.022  15.252  75.591  1.00 43.63 ? 82   GLU C CG  1 
ATOM   10327 C  CD  . GLU C 1 90  ? 61.902  14.070  75.982  1.00 51.40 ? 82   GLU C CD  1 
ATOM   10328 O  OE1 . GLU C 1 90  ? 61.812  13.602  77.142  1.00 50.31 ? 82   GLU C OE1 1 
ATOM   10329 O  OE2 . GLU C 1 90  ? 62.685  13.606  75.122  1.00 54.59 ? 82   GLU C OE2 1 
ATOM   10330 N  N   . ASP C 1 91  ? 56.510  14.365  76.248  1.00 24.11 ? 83   ASP C N   1 
ATOM   10331 C  CA  . ASP C 1 91  ? 55.250  14.156  76.960  1.00 21.12 ? 83   ASP C CA  1 
ATOM   10332 C  C   . ASP C 1 91  ? 54.840  12.688  76.940  1.00 24.79 ? 83   ASP C C   1 
ATOM   10333 O  O   . ASP C 1 91  ? 54.417  12.143  77.966  1.00 19.83 ? 83   ASP C O   1 
ATOM   10334 C  CB  . ASP C 1 91  ? 54.146  15.020  76.361  1.00 19.98 ? 83   ASP C CB  1 
ATOM   10335 C  CG  . ASP C 1 91  ? 54.376  16.496  76.588  1.00 26.62 ? 83   ASP C CG  1 
ATOM   10336 O  OD1 . ASP C 1 91  ? 54.884  16.861  77.672  1.00 27.19 ? 83   ASP C OD1 1 
ATOM   10337 O  OD2 . ASP C 1 91  ? 54.041  17.291  75.687  1.00 26.97 ? 83   ASP C OD2 1 
ATOM   10338 N  N   . LEU C 1 92  ? 54.967  12.025  75.786  1.00 19.50 ? 84   LEU C N   1 
ATOM   10339 C  CA  . LEU C 1 92  ? 54.626  10.605  75.710  1.00 20.25 ? 84   LEU C CA  1 
ATOM   10340 C  C   . LEU C 1 92  ? 55.539  9.756   76.588  1.00 25.09 ? 84   LEU C C   1 
ATOM   10341 O  O   . LEU C 1 92  ? 55.092  8.765   77.179  1.00 23.68 ? 84   LEU C O   1 
ATOM   10342 C  CB  . LEU C 1 92  ? 54.698  10.115  74.265  1.00 21.00 ? 84   LEU C CB  1 
ATOM   10343 C  CG  . LEU C 1 92  ? 53.820  10.884  73.288  1.00 25.73 ? 84   LEU C CG  1 
ATOM   10344 C  CD1 . LEU C 1 92  ? 53.802  10.166  71.944  1.00 27.73 ? 84   LEU C CD1 1 
ATOM   10345 C  CD2 . LEU C 1 92  ? 52.404  11.090  73.847  1.00 19.24 ? 84   LEU C CD2 1 
ATOM   10346 N  N   . LYS C 1 93  ? 56.825  10.113  76.672  1.00 21.19 ? 85   LYS C N   1 
ATOM   10347 C  CA  . LYS C 1 93  ? 57.736  9.402   77.563  1.00 22.07 ? 85   LYS C CA  1 
ATOM   10348 C  C   . LYS C 1 93  ? 57.426  9.644   79.032  1.00 22.67 ? 85   LYS C C   1 
ATOM   10349 O  O   . LYS C 1 93  ? 58.022  8.980   79.891  1.00 22.81 ? 85   LYS C O   1 
ATOM   10350 C  CB  . LYS C 1 93  ? 59.197  9.804   77.294  1.00 23.97 ? 85   LYS C CB  1 
ATOM   10351 C  CG  . LYS C 1 93  ? 59.721  9.416   75.920  1.00 28.56 ? 85   LYS C CG  1 
ATOM   10352 C  CD  . LYS C 1 93  ? 61.159  9.898   75.733  1.00 32.59 ? 85   LYS C CD  1 
ATOM   10353 C  CE  . LYS C 1 93  ? 61.691  9.537   74.362  1.00 37.25 ? 85   LYS C CE  1 
ATOM   10354 N  NZ  . LYS C 1 93  ? 63.110  9.962   74.178  1.00 43.14 ? 85   LYS C NZ  1 
ATOM   10355 N  N   . ASN C 1 94  ? 56.556  10.601  79.345  1.00 22.09 ? 86   ASN C N   1 
ATOM   10356 C  CA  . ASN C 1 94  ? 56.141  10.863  80.716  1.00 25.24 ? 86   ASN C CA  1 
ATOM   10357 C  C   . ASN C 1 94  ? 54.736  10.346  80.999  1.00 25.25 ? 86   ASN C C   1 
ATOM   10358 O  O   . ASN C 1 94  ? 54.087  10.816  81.942  1.00 19.33 ? 86   ASN C O   1 
ATOM   10359 C  CB  . ASN C 1 94  ? 56.212  12.357  81.022  1.00 21.89 ? 86   ASN C CB  1 
ATOM   10360 C  CG  . ASN C 1 94  ? 57.619  12.881  81.038  1.00 29.05 ? 86   ASN C CG  1 
ATOM   10361 O  OD1 . ASN C 1 94  ? 58.547  12.189  81.448  1.00 33.12 ? 86   ASN C OD1 1 
ATOM   10362 N  ND2 . ASN C 1 94  ? 57.787  14.124  80.610  1.00 33.19 ? 86   ASN C ND2 1 
ATOM   10363 N  N   . PHE C 1 95  ? 54.258  9.405   80.190  1.00 18.42 ? 87   PHE C N   1 
ATOM   10364 C  CA  . PHE C 1 95  ? 52.973  8.753   80.425  1.00 17.31 ? 87   PHE C CA  1 
ATOM   10365 C  C   . PHE C 1 95  ? 52.863  8.292   81.875  1.00 26.83 ? 87   PHE C C   1 
ATOM   10366 O  O   . PHE C 1 95  ? 53.762  7.633   82.405  1.00 18.16 ? 87   PHE C O   1 
ATOM   10367 C  CB  . PHE C 1 95  ? 52.833  7.565   79.465  1.00 17.77 ? 87   PHE C CB  1 
ATOM   10368 C  CG  . PHE C 1 95  ? 51.511  6.838   79.552  1.00 16.21 ? 87   PHE C CG  1 
ATOM   10369 C  CD1 . PHE C 1 95  ? 50.312  7.515   79.420  1.00 19.08 ? 87   PHE C CD1 1 
ATOM   10370 C  CD2 . PHE C 1 95  ? 51.482  5.465   79.724  1.00 19.65 ? 87   PHE C CD2 1 
ATOM   10371 C  CE1 . PHE C 1 95  ? 49.094  6.826   79.469  1.00 21.08 ? 87   PHE C CE1 1 
ATOM   10372 C  CE2 . PHE C 1 95  ? 50.280  4.776   79.782  1.00 20.57 ? 87   PHE C CE2 1 
ATOM   10373 C  CZ  . PHE C 1 95  ? 49.084  5.461   79.652  1.00 19.60 ? 87   PHE C CZ  1 
ATOM   10374 N  N   . ARG C 1 96  ? 51.773  8.692   82.526  1.00 23.96 ? 88   ARG C N   1 
ATOM   10375 C  CA  . ARG C 1 96  ? 51.411  8.231   83.864  1.00 23.16 ? 88   ARG C CA  1 
ATOM   10376 C  C   . ARG C 1 96  ? 52.351  8.738   84.949  1.00 25.61 ? 88   ARG C C   1 
ATOM   10377 O  O   . ARG C 1 96  ? 52.407  8.154   86.036  1.00 23.69 ? 88   ARG C O   1 
ATOM   10378 C  CB  . ARG C 1 96  ? 51.317  6.696   83.906  1.00 17.97 ? 88   ARG C CB  1 
ATOM   10379 C  CG  . ARG C 1 96  ? 49.980  6.186   83.398  1.00 16.69 ? 88   ARG C CG  1 
ATOM   10380 C  CD  . ARG C 1 96  ? 49.895  4.672   83.223  1.00 22.94 ? 88   ARG C CD  1 
ATOM   10381 N  NE  . ARG C 1 96  ? 48.556  4.339   82.731  1.00 22.11 ? 88   ARG C NE  1 
ATOM   10382 C  CZ  . ARG C 1 96  ? 47.593  3.782   83.460  1.00 22.59 ? 88   ARG C CZ  1 
ATOM   10383 N  NH1 . ARG C 1 96  ? 47.820  3.421   84.714  1.00 22.77 ? 88   ARG C NH1 1 
ATOM   10384 N  NH2 . ARG C 1 96  ? 46.405  3.556   82.923  1.00 28.67 ? 88   ARG C NH2 1 
ATOM   10385 N  N   . GLN C 1 97  ? 53.081  9.823   84.694  1.00 18.58 ? 89   GLN C N   1 
ATOM   10386 C  CA  . GLN C 1 97  ? 54.015  10.381  85.658  1.00 20.22 ? 89   GLN C CA  1 
ATOM   10387 C  C   . GLN C 1 97  ? 53.449  11.675  86.230  1.00 20.09 ? 89   GLN C C   1 
ATOM   10388 O  O   . GLN C 1 97  ? 52.647  12.359  85.584  1.00 23.47 ? 89   GLN C O   1 
ATOM   10389 C  CB  . GLN C 1 97  ? 55.389  10.629  85.021  1.00 21.62 ? 89   GLN C CB  1 
ATOM   10390 C  CG  . GLN C 1 97  ? 56.028  9.352   84.438  1.00 22.81 ? 89   GLN C CG  1 
ATOM   10391 C  CD  . GLN C 1 97  ? 55.924  8.156   85.376  1.00 26.02 ? 89   GLN C CD  1 
ATOM   10392 O  OE1 . GLN C 1 97  ? 56.462  8.164   86.491  1.00 24.35 ? 89   GLN C OE1 1 
ATOM   10393 N  NE2 . GLN C 1 97  ? 55.215  7.126   84.934  1.00 21.79 ? 89   GLN C NE2 1 
ATOM   10394 N  N   . LEU C 1 98  ? 53.870  11.995  87.451  1.00 21.16 ? 90   LEU C N   1 
ATOM   10395 C  CA  . LEU C 1 98  ? 53.263  13.091  88.201  1.00 25.92 ? 90   LEU C CA  1 
ATOM   10396 C  C   . LEU C 1 98  ? 53.320  14.396  87.415  1.00 29.83 ? 90   LEU C C   1 
ATOM   10397 O  O   . LEU C 1 98  ? 54.398  14.835  86.995  1.00 24.39 ? 90   LEU C O   1 
ATOM   10398 C  CB  . LEU C 1 98  ? 53.957  13.254  89.555  1.00 27.49 ? 90   LEU C CB  1 
ATOM   10399 C  CG  . LEU C 1 98  ? 53.297  14.281  90.482  1.00 24.06 ? 90   LEU C CG  1 
ATOM   10400 C  CD1 . LEU C 1 98  ? 51.889  13.820  90.883  1.00 23.25 ? 90   LEU C CD1 1 
ATOM   10401 C  CD2 . LEU C 1 98  ? 54.149  14.537  91.707  1.00 25.80 ? 90   LEU C CD2 1 
ATOM   10402 N  N   . HIS C 1 99  ? 52.142  14.997  87.215  1.00 22.62 ? 91   HIS C N   1 
ATOM   10403 C  CA  . HIS C 1 99  ? 51.916  16.284  86.564  1.00 26.87 ? 91   HIS C CA  1 
ATOM   10404 C  C   . HIS C 1 99  ? 52.249  16.286  85.080  1.00 28.72 ? 91   HIS C C   1 
ATOM   10405 O  O   . HIS C 1 99  ? 52.322  17.360  84.475  1.00 32.09 ? 91   HIS C O   1 
ATOM   10406 C  CB  . HIS C 1 99  ? 52.673  17.414  87.269  1.00 28.95 ? 91   HIS C CB  1 
ATOM   10407 C  CG  . HIS C 1 99  ? 52.222  17.635  88.677  1.00 30.72 ? 91   HIS C CG  1 
ATOM   10408 N  ND1 . HIS C 1 99  ? 50.889  17.725  89.020  1.00 32.18 ? 91   HIS C ND1 1 
ATOM   10409 C  CD2 . HIS C 1 99  ? 52.919  17.761  89.831  1.00 32.51 ? 91   HIS C CD2 1 
ATOM   10410 C  CE1 . HIS C 1 99  ? 50.785  17.911  90.324  1.00 33.03 ? 91   HIS C CE1 1 
ATOM   10411 N  NE2 . HIS C 1 99  ? 52.002  17.936  90.840  1.00 34.76 ? 91   HIS C NE2 1 
ATOM   10412 N  N   . SER C 1 100 ? 52.416  15.123  84.459  1.00 26.32 ? 92   SER C N   1 
ATOM   10413 C  CA  . SER C 1 100 ? 52.643  15.114  83.023  1.00 25.10 ? 92   SER C CA  1 
ATOM   10414 C  C   . SER C 1 100 ? 51.365  15.484  82.277  1.00 25.75 ? 92   SER C C   1 
ATOM   10415 O  O   . SER C 1 100 ? 50.258  15.448  82.822  1.00 27.07 ? 92   SER C O   1 
ATOM   10416 C  CB  . SER C 1 100 ? 53.134  13.744  82.560  1.00 22.43 ? 92   SER C CB  1 
ATOM   10417 O  OG  . SER C 1 100 ? 52.061  12.830  82.423  1.00 21.13 ? 92   SER C OG  1 
ATOM   10418 N  N   . LYS C 1 101 ? 51.532  15.842  81.003  1.00 23.69 ? 93   LYS C N   1 
ATOM   10419 C  CA  . LYS C 1 101 ? 50.403  16.039  80.098  1.00 24.62 ? 93   LYS C CA  1 
ATOM   10420 C  C   . LYS C 1 101 ? 49.791  14.733  79.612  1.00 21.08 ? 93   LYS C C   1 
ATOM   10421 O  O   . LYS C 1 101 ? 48.860  14.766  78.800  1.00 21.76 ? 93   LYS C O   1 
ATOM   10422 C  CB  . LYS C 1 101 ? 50.838  16.874  78.889  1.00 27.56 ? 93   LYS C CB  1 
ATOM   10423 C  CG  . LYS C 1 101 ? 51.266  18.299  79.234  1.00 33.30 ? 93   LYS C CG  1 
ATOM   10424 C  CD  . LYS C 1 101 ? 51.518  19.094  77.962  1.00 46.23 ? 93   LYS C CD  1 
ATOM   10425 C  CE  . LYS C 1 101 ? 51.889  20.535  78.261  1.00 55.64 ? 93   LYS C CE  1 
ATOM   10426 N  NZ  . LYS C 1 101 ? 52.055  21.309  77.001  1.00 61.09 ? 93   LYS C NZ  1 
ATOM   10427 N  N   . THR C 1 102 ? 50.281  13.583  80.075  1.00 19.04 ? 94   THR C N   1 
ATOM   10428 C  CA  . THR C 1 102 ? 49.788  12.282  79.619  1.00 17.27 ? 94   THR C CA  1 
ATOM   10429 C  C   . THR C 1 102 ? 49.385  11.409  80.806  1.00 21.50 ? 94   THR C C   1 
ATOM   10430 O  O   . THR C 1 102 ? 49.982  10.356  81.052  1.00 19.57 ? 94   THR C O   1 
ATOM   10431 C  CB  . THR C 1 102 ? 50.847  11.590  78.767  1.00 16.69 ? 94   THR C CB  1 
ATOM   10432 O  OG1 . THR C 1 102 ? 52.106  11.655  79.443  1.00 18.52 ? 94   THR C OG1 1 
ATOM   10433 C  CG2 . THR C 1 102 ? 50.978  12.286  77.409  1.00 18.47 ? 94   THR C CG2 1 
ATOM   10434 N  N   . PRO C 1 103 ? 48.371  11.815  81.568  1.00 17.37 ? 95   PRO C N   1 
ATOM   10435 C  CA  . PRO C 1 103 ? 47.906  10.968  82.670  1.00 15.12 ? 95   PRO C CA  1 
ATOM   10436 C  C   . PRO C 1 103 ? 47.305  9.672   82.149  1.00 14.51 ? 95   PRO C C   1 
ATOM   10437 O  O   . PRO C 1 103 ? 46.951  9.544   80.974  1.00 17.69 ? 95   PRO C O   1 
ATOM   10438 C  CB  . PRO C 1 103 ? 46.852  11.835  83.370  1.00 22.21 ? 95   PRO C CB  1 
ATOM   10439 C  CG  . PRO C 1 103 ? 46.372  12.766  82.324  1.00 15.54 ? 95   PRO C CG  1 
ATOM   10440 C  CD  . PRO C 1 103 ? 47.570  13.048  81.454  1.00 17.18 ? 95   PRO C CD  1 
ATOM   10441 N  N   . GLY C 1 104 ? 47.184  8.697   83.056  1.00 18.40 ? 96   GLY C N   1 
ATOM   10442 C  CA  . GLY C 1 104 ? 46.775  7.354   82.658  1.00 16.17 ? 96   GLY C CA  1 
ATOM   10443 C  C   . GLY C 1 104 ? 45.438  7.303   81.942  1.00 19.52 ? 96   GLY C C   1 
ATOM   10444 O  O   . GLY C 1 104 ? 45.215  6.435   81.094  1.00 16.81 ? 96   GLY C O   1 
ATOM   10445 N  N   . HIS C 1 105 ? 44.533  8.214   82.275  1.00 19.64 ? 97   HIS C N   1 
ATOM   10446 C  CA  . HIS C 1 105 ? 43.324  8.412   81.503  1.00 16.54 ? 97   HIS C CA  1 
ATOM   10447 C  C   . HIS C 1 105 ? 43.276  9.856   81.011  1.00 17.76 ? 97   HIS C C   1 
ATOM   10448 O  O   . HIS C 1 105 ? 43.706  10.764  81.737  1.00 17.00 ? 97   HIS C O   1 
ATOM   10449 C  CB  . HIS C 1 105 ? 42.069  8.093   82.344  1.00 21.50 ? 97   HIS C CB  1 
ATOM   10450 C  CG  . HIS C 1 105 ? 42.038  6.692   82.875  1.00 33.12 ? 97   HIS C CG  1 
ATOM   10451 N  ND1 . HIS C 1 105 ? 41.920  6.408   84.217  1.00 38.42 ? 97   HIS C ND1 1 
ATOM   10452 C  CD2 . HIS C 1 105 ? 42.101  5.495   82.243  1.00 38.17 ? 97   HIS C CD2 1 
ATOM   10453 C  CE1 . HIS C 1 105 ? 41.926  5.098   84.392  1.00 38.07 ? 97   HIS C CE1 1 
ATOM   10454 N  NE2 . HIS C 1 105 ? 42.033  4.521   83.210  1.00 33.41 ? 97   HIS C NE2 1 
ATOM   10455 N  N   . PRO C 1 106 ? 42.782  10.100  79.792  1.00 19.23 ? 98   PRO C N   1 
ATOM   10456 C  CA  . PRO C 1 106 ? 42.824  11.462  79.229  1.00 19.14 ? 98   PRO C CA  1 
ATOM   10457 C  C   . PRO C 1 106 ? 42.048  12.446  80.094  1.00 18.69 ? 98   PRO C C   1 
ATOM   10458 O  O   . PRO C 1 106 ? 40.942  12.152  80.562  1.00 16.62 ? 98   PRO C O   1 
ATOM   10459 C  CB  . PRO C 1 106 ? 42.159  11.301  77.851  1.00 15.56 ? 98   PRO C CB  1 
ATOM   10460 C  CG  . PRO C 1 106 ? 42.112  9.797   77.593  1.00 22.07 ? 98   PRO C CG  1 
ATOM   10461 C  CD  . PRO C 1 106 ? 42.031  9.161   78.937  1.00 18.35 ? 98   PRO C CD  1 
ATOM   10462 N  N   . GLU C 1 107 ? 42.621  13.631  80.295  1.00 16.27 ? 99   GLU C N   1 
ATOM   10463 C  CA  . GLU C 1 107 ? 42.018  14.614  81.191  1.00 18.71 ? 99   GLU C CA  1 
ATOM   10464 C  C   . GLU C 1 107 ? 41.637  15.869  80.419  1.00 14.99 ? 99   GLU C C   1 
ATOM   10465 O  O   . GLU C 1 107 ? 42.503  16.564  79.875  1.00 20.59 ? 99   GLU C O   1 
ATOM   10466 C  CB  . GLU C 1 107 ? 42.956  14.940  82.358  1.00 22.56 ? 99   GLU C CB  1 
ATOM   10467 C  CG  . GLU C 1 107 ? 42.940  13.855  83.442  1.00 20.82 ? 99   GLU C CG  1 
ATOM   10468 C  CD  . GLU C 1 107 ? 43.862  14.168  84.605  1.00 22.73 ? 99   GLU C CD  1 
ATOM   10469 O  OE1 . GLU C 1 107 ? 44.189  15.362  84.808  1.00 23.86 ? 99   GLU C OE1 1 
ATOM   10470 O  OE2 . GLU C 1 107 ? 44.280  13.216  85.303  1.00 23.20 ? 99   GLU C OE2 1 
ATOM   10471 N  N   . TYR C 1 108 ? 40.337  16.139  80.351  1.00 14.16 ? 100  TYR C N   1 
ATOM   10472 C  CA  . TYR C 1 108 ? 39.880  17.389  79.767  1.00 13.76 ? 100  TYR C CA  1 
ATOM   10473 C  C   . TYR C 1 108 ? 40.479  18.571  80.514  1.00 16.11 ? 100  TYR C C   1 
ATOM   10474 O  O   . TYR C 1 108 ? 40.521  18.592  81.749  1.00 15.69 ? 100  TYR C O   1 
ATOM   10475 C  CB  . TYR C 1 108 ? 38.361  17.477  79.815  1.00 15.98 ? 100  TYR C CB  1 
ATOM   10476 C  CG  . TYR C 1 108 ? 37.839  18.815  79.352  1.00 15.19 ? 100  TYR C CG  1 
ATOM   10477 C  CD1 . TYR C 1 108 ? 37.807  19.131  78.000  1.00 15.21 ? 100  TYR C CD1 1 
ATOM   10478 C  CD2 . TYR C 1 108 ? 37.390  19.767  80.263  1.00 14.93 ? 100  TYR C CD2 1 
ATOM   10479 C  CE1 . TYR C 1 108 ? 37.325  20.350  77.560  1.00 19.26 ? 100  TYR C CE1 1 
ATOM   10480 C  CE2 . TYR C 1 108 ? 36.907  20.991  79.830  1.00 15.01 ? 100  TYR C CE2 1 
ATOM   10481 C  CZ  . TYR C 1 108 ? 36.873  21.271  78.476  1.00 23.60 ? 100  TYR C CZ  1 
ATOM   10482 O  OH  . TYR C 1 108 ? 36.396  22.481  78.029  1.00 30.71 ? 100  TYR C OH  1 
ATOM   10483 N  N   . GLY C 1 109 ? 40.932  19.569  79.753  1.00 16.62 ? 101  GLY C N   1 
ATOM   10484 C  CA  . GLY C 1 109 ? 41.397  20.823  80.289  1.00 22.38 ? 101  GLY C CA  1 
ATOM   10485 C  C   . GLY C 1 109 ? 42.904  20.950  80.396  1.00 28.60 ? 101  GLY C C   1 
ATOM   10486 O  O   . GLY C 1 109 ? 43.427  22.064  80.287  1.00 36.57 ? 101  GLY C O   1 
ATOM   10487 N  N   . TYR C 1 110 ? 43.614  19.843  80.609  1.00 28.91 ? 102  TYR C N   1 
ATOM   10488 C  CA  . TYR C 1 110 ? 45.059  19.897  80.791  1.00 35.80 ? 102  TYR C CA  1 
ATOM   10489 C  C   . TYR C 1 110 ? 45.841  19.493  79.551  1.00 31.77 ? 102  TYR C C   1 
ATOM   10490 O  O   . TYR C 1 110 ? 47.005  19.886  79.419  1.00 31.94 ? 102  TYR C O   1 
ATOM   10491 C  CB  . TYR C 1 110 ? 45.482  19.001  81.962  1.00 42.07 ? 102  TYR C CB  1 
ATOM   10492 N  N   . THR C 1 111 ? 45.240  18.719  78.653  1.00 22.35 ? 103  THR C N   1 
ATOM   10493 C  CA  . THR C 1 111 ? 45.894  18.253  77.435  1.00 18.55 ? 103  THR C CA  1 
ATOM   10494 C  C   . THR C 1 111 ? 45.098  18.772  76.247  1.00 17.69 ? 103  THR C C   1 
ATOM   10495 O  O   . THR C 1 111 ? 43.905  18.486  76.137  1.00 18.67 ? 103  THR C O   1 
ATOM   10496 C  CB  . THR C 1 111 ? 45.966  16.724  77.409  1.00 21.97 ? 103  THR C CB  1 
ATOM   10497 O  OG1 . THR C 1 111 ? 46.618  16.255  78.595  1.00 29.14 ? 103  THR C OG1 1 
ATOM   10498 C  CG2 . THR C 1 111 ? 46.744  16.236  76.194  1.00 25.72 ? 103  THR C CG2 1 
ATOM   10499 N  N   . ASP C 1 112 ? 45.753  19.547  75.379  1.00 18.45 ? 104  ASP C N   1 
ATOM   10500 C  CA  . ASP C 1 112 ? 45.095  20.068  74.185  1.00 18.41 ? 104  ASP C CA  1 
ATOM   10501 C  C   . ASP C 1 112 ? 44.542  18.936  73.335  1.00 19.14 ? 104  ASP C C   1 
ATOM   10502 O  O   . ASP C 1 112 ? 45.233  17.949  73.068  1.00 19.69 ? 104  ASP C O   1 
ATOM   10503 C  CB  . ASP C 1 112 ? 46.075  20.893  73.346  1.00 27.80 ? 104  ASP C CB  1 
ATOM   10504 C  CG  . ASP C 1 112 ? 46.398  22.229  73.965  1.00 31.75 ? 104  ASP C CG  1 
ATOM   10505 O  OD1 . ASP C 1 112 ? 45.767  22.589  74.980  1.00 31.99 ? 104  ASP C OD1 1 
ATOM   10506 O  OD2 . ASP C 1 112 ? 47.281  22.921  73.423  1.00 29.33 ? 104  ASP C OD2 1 
ATOM   10507 N  N   . GLY C 1 113 ? 43.295  19.085  72.895  1.00 18.02 ? 105  GLY C N   1 
ATOM   10508 C  CA  . GLY C 1 113 ? 42.681  18.143  71.995  1.00 17.26 ? 105  GLY C CA  1 
ATOM   10509 C  C   . GLY C 1 113 ? 41.817  17.090  72.662  1.00 21.23 ? 105  GLY C C   1 
ATOM   10510 O  O   . GLY C 1 113 ? 41.019  16.446  71.974  1.00 25.06 ? 105  GLY C O   1 
ATOM   10511 N  N   . VAL C 1 114 ? 41.955  16.899  73.975  1.00 20.76 ? 106  VAL C N   1 
ATOM   10512 C  CA  . VAL C 1 114 ? 41.108  15.969  74.723  1.00 14.95 ? 106  VAL C CA  1 
ATOM   10513 C  C   . VAL C 1 114 ? 39.758  16.631  74.976  1.00 17.83 ? 106  VAL C C   1 
ATOM   10514 O  O   . VAL C 1 114 ? 39.688  17.683  75.619  1.00 15.88 ? 106  VAL C O   1 
ATOM   10515 C  CB  . VAL C 1 114 ? 41.770  15.553  76.046  1.00 15.93 ? 106  VAL C CB  1 
ATOM   10516 C  CG1 . VAL C 1 114 ? 40.861  14.584  76.826  1.00 13.49 ? 106  VAL C CG1 1 
ATOM   10517 C  CG2 . VAL C 1 114 ? 43.142  14.930  75.800  1.00 15.26 ? 106  VAL C CG2 1 
ATOM   10518 N  N   . GLU C 1 115 ? 38.680  16.005  74.490  1.00 14.07 ? 107  GLU C N   1 
ATOM   10519 C  CA  . GLU C 1 115 ? 37.354  16.610  74.555  1.00 14.62 ? 107  GLU C CA  1 
ATOM   10520 C  C   . GLU C 1 115 ? 36.604  16.287  75.834  1.00 14.04 ? 107  GLU C C   1 
ATOM   10521 O  O   . GLU C 1 115 ? 35.638  16.987  76.153  1.00 13.66 ? 107  GLU C O   1 
ATOM   10522 C  CB  . GLU C 1 115 ? 36.484  16.160  73.375  1.00 13.47 ? 107  GLU C CB  1 
ATOM   10523 C  CG  . GLU C 1 115 ? 37.111  16.422  72.014  1.00 15.41 ? 107  GLU C CG  1 
ATOM   10524 C  CD  . GLU C 1 115 ? 37.123  17.884  71.628  1.00 20.49 ? 107  GLU C CD  1 
ATOM   10525 O  OE1 . GLU C 1 115 ? 36.587  18.716  72.391  1.00 19.06 ? 107  GLU C OE1 1 
ATOM   10526 O  OE2 . GLU C 1 115 ? 37.674  18.204  70.549  1.00 17.91 ? 107  GLU C OE2 1 
ATOM   10527 N  N   . THR C 1 116 ? 37.007  15.245  76.557  1.00 13.44 ? 108  THR C N   1 
ATOM   10528 C  CA  . THR C 1 116 ? 36.305  14.839  77.772  1.00 11.71 ? 108  THR C CA  1 
ATOM   10529 C  C   . THR C 1 116 ? 37.244  13.951  78.566  1.00 16.48 ? 108  THR C C   1 
ATOM   10530 O  O   . THR C 1 116 ? 38.150  13.327  78.012  1.00 15.42 ? 108  THR C O   1 
ATOM   10531 C  CB  . THR C 1 116 ? 34.993  14.096  77.460  1.00 16.44 ? 108  THR C CB  1 
ATOM   10532 O  OG1 . THR C 1 116 ? 34.319  13.754  78.679  1.00 15.39 ? 108  THR C OG1 1 
ATOM   10533 C  CG2 . THR C 1 116 ? 35.257  12.820  76.661  1.00 17.89 ? 108  THR C CG2 1 
ATOM   10534 N  N   . THR C 1 117 ? 37.022  13.899  79.869  1.00 12.82 ? 109  THR C N   1 
ATOM   10535 C  CA  . THR C 1 117 ? 37.784  13.000  80.725  1.00 14.93 ? 109  THR C CA  1 
ATOM   10536 C  C   . THR C 1 117 ? 37.050  11.669  80.790  1.00 16.84 ? 109  THR C C   1 
ATOM   10537 O  O   . THR C 1 117 ? 35.907  11.613  81.256  1.00 15.33 ? 109  THR C O   1 
ATOM   10538 C  CB  . THR C 1 117 ? 37.937  13.587  82.120  1.00 14.43 ? 109  THR C CB  1 
ATOM   10539 O  OG1 . THR C 1 117 ? 38.651  14.824  82.022  1.00 14.89 ? 109  THR C OG1 1 
ATOM   10540 C  CG2 . THR C 1 117 ? 38.700  12.606  83.034  1.00 13.57 ? 109  THR C CG2 1 
ATOM   10541 N  N   . THR C 1 118 ? 37.685  10.609  80.300  1.00 16.14 ? 110  THR C N   1 
ATOM   10542 C  CA  . THR C 1 118 ? 37.066  9.294   80.319  1.00 16.75 ? 110  THR C CA  1 
ATOM   10543 C  C   . THR C 1 118 ? 37.967  8.309   81.044  1.00 21.15 ? 110  THR C C   1 
ATOM   10544 O  O   . THR C 1 118 ? 39.191  8.425   81.034  1.00 24.87 ? 110  THR C O   1 
ATOM   10545 C  CB  . THR C 1 118 ? 36.737  8.758   78.900  1.00 15.27 ? 110  THR C CB  1 
ATOM   10546 O  OG1 . THR C 1 118 ? 37.931  8.657   78.116  1.00 19.99 ? 110  THR C OG1 1 
ATOM   10547 C  CG2 . THR C 1 118 ? 35.728  9.663   78.199  1.00 15.08 ? 110  THR C CG2 1 
ATOM   10548 N  N   . GLY C 1 119 ? 37.327  7.341   81.671  1.00 21.39 ? 111  GLY C N   1 
ATOM   10549 C  CA  . GLY C 1 119 ? 37.989  6.333   82.455  1.00 25.27 ? 111  GLY C CA  1 
ATOM   10550 C  C   . GLY C 1 119 ? 36.924  5.387   82.950  1.00 20.69 ? 111  GLY C C   1 
ATOM   10551 O  O   . GLY C 1 119 ? 36.871  4.218   82.558  1.00 21.11 ? 111  GLY C O   1 
ATOM   10552 N  N   . PRO C 1 120 ? 36.023  5.890   83.796  1.00 21.01 ? 112  PRO C N   1 
ATOM   10553 C  CA  . PRO C 1 120 ? 34.845  5.094   84.167  1.00 16.79 ? 112  PRO C CA  1 
ATOM   10554 C  C   . PRO C 1 120 ? 34.040  4.772   82.918  1.00 16.68 ? 112  PRO C C   1 
ATOM   10555 O  O   . PRO C 1 120 ? 33.624  5.662   82.174  1.00 14.45 ? 112  PRO C O   1 
ATOM   10556 C  CB  . PRO C 1 120 ? 34.089  6.009   85.136  1.00 17.10 ? 112  PRO C CB  1 
ATOM   10557 C  CG  . PRO C 1 120 ? 35.139  6.944   85.664  1.00 21.63 ? 112  PRO C CG  1 
ATOM   10558 C  CD  . PRO C 1 120 ? 36.048  7.186   84.500  1.00 21.71 ? 112  PRO C CD  1 
ATOM   10559 N  N   . LEU C 1 121 ? 33.848  3.481   82.677  1.00 14.70 ? 113  LEU C N   1 
ATOM   10560 C  CA  . LEU C 1 121 ? 33.358  3.035   81.385  1.00 11.65 ? 113  LEU C CA  1 
ATOM   10561 C  C   . LEU C 1 121 ? 31.880  3.380   81.201  1.00 16.02 ? 113  LEU C C   1 
ATOM   10562 O  O   . LEU C 1 121 ? 31.129  3.593   82.163  1.00 15.21 ? 113  LEU C O   1 
ATOM   10563 C  CB  . LEU C 1 121 ? 33.596  1.535   81.223  1.00 15.07 ? 113  LEU C CB  1 
ATOM   10564 C  CG  . LEU C 1 121 ? 35.089  1.148   81.191  1.00 18.56 ? 113  LEU C CG  1 
ATOM   10565 C  CD1 . LEU C 1 121 ? 35.268  -0.351  81.096  1.00 17.93 ? 113  LEU C CD1 1 
ATOM   10566 C  CD2 . LEU C 1 121 ? 35.807  1.845   80.047  1.00 22.37 ? 113  LEU C CD2 1 
ATOM   10567 N  N   . GLY C 1 122 ? 31.476  3.453   79.929  1.00 13.46 ? 114  GLY C N   1 
ATOM   10568 C  CA  . GLY C 1 122 ? 30.122  3.812   79.554  1.00 14.81 ? 114  GLY C CA  1 
ATOM   10569 C  C   . GLY C 1 122 ? 29.843  5.303   79.496  1.00 13.65 ? 114  GLY C C   1 
ATOM   10570 O  O   . GLY C 1 122 ? 28.976  5.731   78.730  1.00 12.87 ? 114  GLY C O   1 
ATOM   10571 N  N   . GLN C 1 123 ? 30.545  6.124   80.287  1.00 10.48 ? 115  GLN C N   1 
ATOM   10572 C  CA  . GLN C 1 123 ? 30.171  7.537   80.315  1.00 13.55 ? 115  GLN C CA  1 
ATOM   10573 C  C   . GLN C 1 123 ? 30.625  8.282   79.067  1.00 13.31 ? 115  GLN C C   1 
ATOM   10574 O  O   . GLN C 1 123 ? 30.009  9.287   78.702  1.00 13.15 ? 115  GLN C O   1 
ATOM   10575 C  CB  . GLN C 1 123 ? 30.718  8.213   81.577  1.00 14.06 ? 115  GLN C CB  1 
ATOM   10576 C  CG  . GLN C 1 123 ? 29.996  7.732   82.814  1.00 14.02 ? 115  GLN C CG  1 
ATOM   10577 C  CD  . GLN C 1 123 ? 30.417  8.456   84.069  1.00 17.39 ? 115  GLN C CD  1 
ATOM   10578 O  OE1 . GLN C 1 123 ? 30.295  9.674   84.161  1.00 12.20 ? 115  GLN C OE1 1 
ATOM   10579 N  NE2 . GLN C 1 123 ? 30.902  7.700   85.057  1.00 13.28 ? 115  GLN C NE2 1 
ATOM   10580 N  N   . GLY C 1 124 ? 31.681  7.810   78.399  1.00 11.79 ? 116  GLY C N   1 
ATOM   10581 C  CA  . GLY C 1 124 ? 32.168  8.509   77.216  1.00 12.86 ? 116  GLY C CA  1 
ATOM   10582 C  C   . GLY C 1 124 ? 31.152  8.555   76.087  1.00 14.15 ? 116  GLY C C   1 
ATOM   10583 O  O   . GLY C 1 124 ? 30.937  9.608   75.480  1.00 11.48 ? 116  GLY C O   1 
ATOM   10584 N  N   . ILE C 1 125 ? 30.507  7.421   75.787  1.00 10.33 ? 117  ILE C N   1 
ATOM   10585 C  CA  . ILE C 1 125 ? 29.466  7.452   74.758  1.00 13.38 ? 117  ILE C CA  1 
ATOM   10586 C  C   . ILE C 1 125 ? 28.340  8.400   75.166  1.00 14.58 ? 117  ILE C C   1 
ATOM   10587 O  O   . ILE C 1 125 ? 27.789  9.125   74.332  1.00 11.90 ? 117  ILE C O   1 
ATOM   10588 C  CB  . ILE C 1 125 ? 28.945  6.030   74.458  1.00 14.40 ? 117  ILE C CB  1 
ATOM   10589 C  CG1 . ILE C 1 125 ? 27.811  6.066   73.427  1.00 11.71 ? 117  ILE C CG1 1 
ATOM   10590 C  CG2 . ILE C 1 125 ? 28.450  5.333   75.711  1.00 12.64 ? 117  ILE C CG2 1 
ATOM   10591 C  CD1 . ILE C 1 125 ? 28.213  6.640   72.063  1.00 15.17 ? 117  ILE C CD1 1 
ATOM   10592 N  N   . ALA C 1 126 ? 27.978  8.411   76.452  1.00 13.18 ? 118  ALA C N   1 
ATOM   10593 C  CA  . ALA C 1 126 ? 26.965  9.357   76.909  1.00 14.63 ? 118  ALA C CA  1 
ATOM   10594 C  C   . ALA C 1 126 ? 27.429  10.799  76.726  1.00 12.63 ? 118  ALA C C   1 
ATOM   10595 O  O   . ALA C 1 126 ? 26.645  11.653  76.289  1.00 9.80  ? 118  ALA C O   1 
ATOM   10596 C  CB  . ALA C 1 126 ? 26.609  9.088   78.373  1.00 9.06  ? 118  ALA C CB  1 
ATOM   10597 N  N   . ASN C 1 127 ? 28.694  11.099  77.072  1.00 9.90  ? 119  ASN C N   1 
ATOM   10598 C  CA  . ASN C 1 127 ? 29.231  12.432  76.796  1.00 10.40 ? 119  ASN C CA  1 
ATOM   10599 C  C   . ASN C 1 127 ? 29.078  12.767  75.314  1.00 12.56 ? 119  ASN C C   1 
ATOM   10600 O  O   . ASN C 1 127 ? 28.690  13.885  74.948  1.00 13.17 ? 119  ASN C O   1 
ATOM   10601 C  CB  . ASN C 1 127 ? 30.732  12.542  77.152  1.00 11.79 ? 119  ASN C CB  1 
ATOM   10602 C  CG  . ASN C 1 127 ? 31.075  12.247  78.625  1.00 13.48 ? 119  ASN C CG  1 
ATOM   10603 O  OD1 . ASN C 1 127 ? 32.233  11.931  78.924  1.00 14.67 ? 119  ASN C OD1 1 
ATOM   10604 N  ND2 . ASN C 1 127 ? 30.122  12.400  79.537  1.00 9.69  ? 119  ASN C ND2 1 
ATOM   10605 N  N   . ALA C 1 128 ? 29.405  11.806  74.447  1.00 12.37 ? 120  ALA C N   1 
ATOM   10606 C  CA  . ALA C 1 128 ? 29.349  12.051  73.010  1.00 14.22 ? 120  ALA C CA  1 
ATOM   10607 C  C   . ALA C 1 128 ? 27.920  12.273  72.542  1.00 11.91 ? 120  ALA C C   1 
ATOM   10608 O  O   . ALA C 1 128 ? 27.672  13.084  71.647  1.00 11.46 ? 120  ALA C O   1 
ATOM   10609 C  CB  . ALA C 1 128 ? 29.984  10.887  72.266  1.00 14.90 ? 120  ALA C CB  1 
ATOM   10610 N  N   . VAL C 1 129 ? 26.960  11.553  73.121  1.00 8.98  ? 121  VAL C N   1 
ATOM   10611 C  CA  . VAL C 1 129 ? 25.560  11.846  72.804  1.00 8.96  ? 121  VAL C CA  1 
ATOM   10612 C  C   . VAL C 1 129 ? 25.245  13.301  73.123  1.00 11.56 ? 121  VAL C C   1 
ATOM   10613 O  O   . VAL C 1 129 ? 24.588  14.000  72.339  1.00 12.62 ? 121  VAL C O   1 
ATOM   10614 C  CB  . VAL C 1 129 ? 24.633  10.877  73.558  1.00 9.08  ? 121  VAL C CB  1 
ATOM   10615 C  CG1 . VAL C 1 129 ? 23.155  11.333  73.451  1.00 9.41  ? 121  VAL C CG1 1 
ATOM   10616 C  CG2 . VAL C 1 129 ? 24.810  9.474   73.011  1.00 9.83  ? 121  VAL C CG2 1 
ATOM   10617 N  N   . GLY C 1 130 ? 25.739  13.788  74.266  1.00 11.08 ? 122  GLY C N   1 
ATOM   10618 C  CA  . GLY C 1 130 ? 25.516  15.173  74.638  1.00 11.27 ? 122  GLY C CA  1 
ATOM   10619 C  C   . GLY C 1 130 ? 26.165  16.157  73.682  1.00 10.82 ? 122  GLY C C   1 
ATOM   10620 O  O   . GLY C 1 130 ? 25.586  17.204  73.381  1.00 10.78 ? 122  GLY C O   1 
ATOM   10621 N  N   . MET C 1 131 ? 27.378  15.840  73.196  1.00 9.61  ? 123  MET C N   1 
ATOM   10622 C  CA  . MET C 1 131 ? 28.043  16.714  72.227  1.00 14.53 ? 123  MET C CA  1 
ATOM   10623 C  C   . MET C 1 131 ? 27.289  16.740  70.903  1.00 12.72 ? 123  MET C C   1 
ATOM   10624 O  O   . MET C 1 131 ? 27.176  17.793  70.262  1.00 12.23 ? 123  MET C O   1 
ATOM   10625 C  CB  . MET C 1 131 ? 29.489  16.265  71.991  1.00 16.81 ? 123  MET C CB  1 
ATOM   10626 C  CG  . MET C 1 131 ? 30.361  16.277  73.244  1.00 13.32 ? 123  MET C CG  1 
ATOM   10627 S  SD  . MET C 1 131 ? 32.018  15.665  72.914  1.00 13.69 ? 123  MET C SD  1 
ATOM   10628 C  CE  . MET C 1 131 ? 32.731  15.758  74.575  1.00 12.43 ? 123  MET C CE  1 
ATOM   10629 N  N   . ALA C 1 132 ? 26.774  15.588  70.474  1.00 10.39 ? 124  ALA C N   1 
ATOM   10630 C  CA  . ALA C 1 132 ? 26.006  15.555  69.234  1.00 13.11 ? 124  ALA C CA  1 
ATOM   10631 C  C   . ALA C 1 132 ? 24.671  16.268  69.412  1.00 13.39 ? 124  ALA C C   1 
ATOM   10632 O  O   . ALA C 1 132 ? 24.178  16.925  68.490  1.00 11.52 ? 124  ALA C O   1 
ATOM   10633 C  CB  . ALA C 1 132 ? 25.796  14.111  68.782  1.00 11.89 ? 124  ALA C CB  1 
ATOM   10634 N  N   . LEU C 1 133 ? 24.069  16.134  70.594  1.00 12.82 ? 125  LEU C N   1 
ATOM   10635 C  CA  . LEU C 1 133 ? 22.847  16.867  70.909  1.00 14.47 ? 125  LEU C CA  1 
ATOM   10636 C  C   . LEU C 1 133 ? 23.096  18.374  70.916  1.00 15.35 ? 125  LEU C C   1 
ATOM   10637 O  O   . LEU C 1 133 ? 22.260  19.155  70.445  1.00 12.25 ? 125  LEU C O   1 
ATOM   10638 C  CB  . LEU C 1 133 ? 22.337  16.389  72.265  1.00 13.61 ? 125  LEU C CB  1 
ATOM   10639 C  CG  . LEU C 1 133 ? 20.906  16.587  72.716  1.00 23.76 ? 125  LEU C CG  1 
ATOM   10640 C  CD1 . LEU C 1 133 ? 19.945  16.142  71.622  1.00 24.25 ? 125  LEU C CD1 1 
ATOM   10641 C  CD2 . LEU C 1 133 ? 20.722  15.758  73.989  1.00 20.78 ? 125  LEU C CD2 1 
ATOM   10642 N  N   . ALA C 1 134 ? 24.252  18.803  71.436  1.00 13.49 ? 126  ALA C N   1 
ATOM   10643 C  CA  . ALA C 1 134 ? 24.581  20.228  71.419  1.00 16.54 ? 126  ALA C CA  1 
ATOM   10644 C  C   . ALA C 1 134 ? 24.673  20.743  69.991  1.00 11.64 ? 126  ALA C C   1 
ATOM   10645 O  O   . ALA C 1 134 ? 24.111  21.793  69.657  1.00 18.30 ? 126  ALA C O   1 
ATOM   10646 C  CB  . ALA C 1 134 ? 25.899  20.480  72.154  1.00 12.46 ? 126  ALA C CB  1 
ATOM   10647 N  N   . GLU C 1 135 ? 25.378  20.004  69.133  1.00 10.38 ? 127  GLU C N   1 
ATOM   10648 C  CA  . GLU C 1 135 ? 25.507  20.405  67.733  1.00 13.61 ? 127  GLU C CA  1 
ATOM   10649 C  C   . GLU C 1 135 ? 24.135  20.505  67.079  1.00 14.86 ? 127  GLU C C   1 
ATOM   10650 O  O   . GLU C 1 135 ? 23.828  21.490  66.401  1.00 14.79 ? 127  GLU C O   1 
ATOM   10651 C  CB  . GLU C 1 135 ? 26.402  19.405  66.991  1.00 11.54 ? 127  GLU C CB  1 
ATOM   10652 C  CG  . GLU C 1 135 ? 26.889  19.863  65.607  1.00 11.75 ? 127  GLU C CG  1 
ATOM   10653 C  CD  . GLU C 1 135 ? 25.958  19.453  64.469  1.00 13.44 ? 127  GLU C CD  1 
ATOM   10654 O  OE1 . GLU C 1 135 ? 24.948  18.753  64.718  1.00 14.15 ? 127  GLU C OE1 1 
ATOM   10655 O  OE2 . GLU C 1 135 ? 26.237  19.840  63.316  1.00 15.74 ? 127  GLU C OE2 1 
ATOM   10656 N  N   . LYS C 1 136 ? 23.290  19.493  67.292  1.00 11.67 ? 128  LYS C N   1 
ATOM   10657 C  CA  . LYS C 1 136 ? 21.952  19.483  66.702  1.00 12.00 ? 128  LYS C CA  1 
ATOM   10658 C  C   . LYS C 1 136 ? 21.142  20.701  67.144  1.00 13.50 ? 128  LYS C C   1 
ATOM   10659 O  O   . LYS C 1 136 ? 20.513  21.376  66.317  1.00 13.39 ? 128  LYS C O   1 
ATOM   10660 C  CB  . LYS C 1 136 ? 21.232  18.182  67.079  1.00 24.27 ? 128  LYS C CB  1 
ATOM   10661 C  CG  . LYS C 1 136 ? 19.735  18.156  66.750  1.00 22.23 ? 128  LYS C CG  1 
ATOM   10662 C  CD  . LYS C 1 136 ? 19.022  17.021  67.491  1.00 21.07 ? 128  LYS C CD  1 
ATOM   10663 C  CE  . LYS C 1 136 ? 17.503  17.247  67.547  1.00 16.74 ? 128  LYS C CE  1 
ATOM   10664 N  NZ  . LYS C 1 136 ? 16.845  17.222  66.197  1.00 19.58 ? 128  LYS C NZ  1 
ATOM   10665 N  N   . ILE C 1 137 ? 21.163  20.992  68.451  1.00 12.87 ? 129  ILE C N   1 
ATOM   10666 C  CA  . ILE C 1 137 ? 20.448  22.129  69.042  1.00 17.74 ? 129  ILE C CA  1 
ATOM   10667 C  C   . ILE C 1 137 ? 20.972  23.447  68.482  1.00 16.13 ? 129  ILE C C   1 
ATOM   10668 O  O   . ILE C 1 137 ? 20.200  24.321  68.062  1.00 17.07 ? 129  ILE C O   1 
ATOM   10669 C  CB  . ILE C 1 137 ? 20.590  22.082  70.579  1.00 16.75 ? 129  ILE C CB  1 
ATOM   10670 C  CG1 . ILE C 1 137 ? 19.714  20.989  71.178  1.00 24.03 ? 129  ILE C CG1 1 
ATOM   10671 C  CG2 . ILE C 1 137 ? 20.319  23.437  71.221  1.00 17.52 ? 129  ILE C CG2 1 
ATOM   10672 C  CD1 . ILE C 1 137 ? 19.928  20.822  72.682  1.00 20.90 ? 129  ILE C CD1 1 
ATOM   10673 N  N   . LEU C 1 138 ? 22.300  23.609  68.475  1.00 14.14 ? 130  LEU C N   1 
ATOM   10674 C  CA  . LEU C 1 138 ? 22.918  24.844  67.995  1.00 17.41 ? 130  LEU C CA  1 
ATOM   10675 C  C   . LEU C 1 138 ? 22.695  25.053  66.498  1.00 16.33 ? 130  LEU C C   1 
ATOM   10676 O  O   . LEU C 1 138 ? 22.449  26.185  66.057  1.00 15.63 ? 130  LEU C O   1 
ATOM   10677 C  CB  . LEU C 1 138 ? 24.414  24.834  68.319  1.00 16.65 ? 130  LEU C CB  1 
ATOM   10678 C  CG  . LEU C 1 138 ? 24.736  24.868  69.817  1.00 15.68 ? 130  LEU C CG  1 
ATOM   10679 C  CD1 . LEU C 1 138 ? 26.211  24.554  70.057  1.00 16.41 ? 130  LEU C CD1 1 
ATOM   10680 C  CD2 . LEU C 1 138 ? 24.364  26.221  70.417  1.00 16.77 ? 130  LEU C CD2 1 
ATOM   10681 N  N   . ALA C 1 139 ? 22.809  23.988  65.694  1.00 14.02 ? 131  ALA C N   1 
ATOM   10682 C  CA  . ALA C 1 139 ? 22.513  24.107  64.268  1.00 14.06 ? 131  ALA C CA  1 
ATOM   10683 C  C   . ALA C 1 139 ? 21.095  24.626  64.051  1.00 19.28 ? 131  ALA C C   1 
ATOM   10684 O  O   . ALA C 1 139 ? 20.867  25.555  63.261  1.00 17.12 ? 131  ALA C O   1 
ATOM   10685 C  CB  . ALA C 1 139 ? 22.705  22.757  63.569  1.00 14.01 ? 131  ALA C CB  1 
ATOM   10686 N  N   . ALA C 1 140 ? 20.125  24.040  64.753  1.00 16.27 ? 132  ALA C N   1 
ATOM   10687 C  CA  . ALA C 1 140 ? 18.737  24.453  64.568  1.00 15.61 ? 132  ALA C CA  1 
ATOM   10688 C  C   . ALA C 1 140 ? 18.541  25.913  64.964  1.00 25.02 ? 132  ALA C C   1 
ATOM   10689 O  O   . ALA C 1 140 ? 17.775  26.637  64.327  1.00 17.04 ? 132  ALA C O   1 
ATOM   10690 C  CB  . ALA C 1 140 ? 17.808  23.541  65.370  1.00 15.50 ? 132  ALA C CB  1 
ATOM   10691 N  N   . GLU C 1 141 ? 19.247  26.372  65.998  1.00 18.17 ? 133  GLU C N   1 
ATOM   10692 C  CA  . GLU C 1 141 ? 19.057  27.738  66.473  1.00 15.85 ? 133  GLU C CA  1 
ATOM   10693 C  C   . GLU C 1 141 ? 19.816  28.759  65.632  1.00 16.29 ? 133  GLU C C   1 
ATOM   10694 O  O   . GLU C 1 141 ? 19.292  29.843  65.352  1.00 17.20 ? 133  GLU C O   1 
ATOM   10695 C  CB  . GLU C 1 141 ? 19.497  27.858  67.933  1.00 15.20 ? 133  GLU C CB  1 
ATOM   10696 C  CG  . GLU C 1 141 ? 19.376  29.272  68.491  1.00 23.71 ? 133  GLU C CG  1 
ATOM   10697 C  CD  . GLU C 1 141 ? 19.879  29.369  69.918  1.00 20.33 ? 133  GLU C CD  1 
ATOM   10698 O  OE1 . GLU C 1 141 ? 20.427  28.365  70.420  1.00 23.87 ? 133  GLU C OE1 1 
ATOM   10699 O  OE2 . GLU C 1 141 ? 19.738  30.447  70.533  1.00 20.30 ? 133  GLU C OE2 1 
ATOM   10700 N  N   . PHE C 1 142 ? 21.048  28.445  65.224  1.00 16.12 ? 134  PHE C N   1 
ATOM   10701 C  CA  . PHE C 1 142 ? 21.897  29.465  64.616  1.00 16.24 ? 134  PHE C CA  1 
ATOM   10702 C  C   . PHE C 1 142 ? 21.992  29.404  63.097  1.00 18.54 ? 134  PHE C C   1 
ATOM   10703 O  O   . PHE C 1 142 ? 22.149  30.456  62.477  1.00 21.37 ? 134  PHE C O   1 
ATOM   10704 C  CB  . PHE C 1 142 ? 23.308  29.407  65.213  1.00 15.52 ? 134  PHE C CB  1 
ATOM   10705 C  CG  . PHE C 1 142 ? 23.401  30.047  66.573  1.00 16.37 ? 134  PHE C CG  1 
ATOM   10706 C  CD1 . PHE C 1 142 ? 23.589  31.411  66.693  1.00 19.92 ? 134  PHE C CD1 1 
ATOM   10707 C  CD2 . PHE C 1 142 ? 23.253  29.291  67.725  1.00 19.54 ? 134  PHE C CD2 1 
ATOM   10708 C  CE1 . PHE C 1 142 ? 23.659  32.019  67.944  1.00 18.91 ? 134  PHE C CE1 1 
ATOM   10709 C  CE2 . PHE C 1 142 ? 23.322  29.885  68.978  1.00 16.45 ? 134  PHE C CE2 1 
ATOM   10710 C  CZ  . PHE C 1 142 ? 23.530  31.253  69.088  1.00 17.14 ? 134  PHE C CZ  1 
ATOM   10711 N  N   . ASN C 1 143 ? 21.932  28.232  62.467  1.00 18.97 ? 135  ASN C N   1 
ATOM   10712 C  CA  . ASN C 1 143 ? 22.132  28.196  61.019  1.00 19.20 ? 135  ASN C CA  1 
ATOM   10713 C  C   . ASN C 1 143 ? 21.025  28.974  60.303  1.00 19.30 ? 135  ASN C C   1 
ATOM   10714 O  O   . ASN C 1 143 ? 19.843  28.830  60.625  1.00 19.61 ? 135  ASN C O   1 
ATOM   10715 C  CB  . ASN C 1 143 ? 22.176  26.752  60.516  1.00 17.39 ? 135  ASN C CB  1 
ATOM   10716 C  CG  . ASN C 1 143 ? 23.455  26.022  60.925  1.00 20.38 ? 135  ASN C CG  1 
ATOM   10717 O  OD1 . ASN C 1 143 ? 24.400  26.628  61.422  1.00 21.89 ? 135  ASN C OD1 1 
ATOM   10718 N  ND2 . ASN C 1 143 ? 23.484  24.717  60.705  1.00 18.66 ? 135  ASN C ND2 1 
ATOM   10719 N  N   . LYS C 1 144 ? 21.410  29.807  59.337  1.00 19.81 ? 136  LYS C N   1 
ATOM   10720 C  CA  . LYS C 1 144 ? 20.451  30.609  58.582  1.00 21.17 ? 136  LYS C CA  1 
ATOM   10721 C  C   . LYS C 1 144 ? 20.814  30.611  57.101  1.00 23.96 ? 136  LYS C C   1 
ATOM   10722 O  O   . LYS C 1 144 ? 21.990  30.565  56.733  1.00 22.23 ? 136  LYS C O   1 
ATOM   10723 C  CB  . LYS C 1 144 ? 20.394  32.067  59.081  1.00 23.94 ? 136  LYS C CB  1 
ATOM   10724 C  CG  . LYS C 1 144 ? 20.144  32.262  60.585  1.00 30.58 ? 136  LYS C CG  1 
ATOM   10725 C  CD  . LYS C 1 144 ? 18.692  32.596  60.878  1.00 38.24 ? 136  LYS C CD  1 
ATOM   10726 C  CE  . LYS C 1 144 ? 18.551  33.472  62.122  1.00 36.95 ? 136  LYS C CE  1 
ATOM   10727 N  NZ  . LYS C 1 144 ? 19.318  32.942  63.273  1.00 40.28 ? 136  LYS C NZ  1 
ATOM   10728 N  N   . ASP C 1 145 ? 19.782  30.659  56.254  1.00 25.26 ? 137  ASP C N   1 
ATOM   10729 C  CA  . ASP C 1 145 ? 19.928  30.904  54.814  1.00 25.59 ? 137  ASP C CA  1 
ATOM   10730 C  C   . ASP C 1 145 ? 20.977  30.002  54.170  1.00 25.05 ? 137  ASP C C   1 
ATOM   10731 O  O   . ASP C 1 145 ? 21.713  30.416  53.275  1.00 31.25 ? 137  ASP C O   1 
ATOM   10732 C  CB  . ASP C 1 145 ? 20.260  32.368  54.545  1.00 33.04 ? 137  ASP C CB  1 
ATOM   10733 C  CG  . ASP C 1 145 ? 19.309  33.319  55.237  1.00 37.51 ? 137  ASP C CG  1 
ATOM   10734 O  OD1 . ASP C 1 145 ? 18.135  32.948  55.443  1.00 37.48 ? 137  ASP C OD1 1 
ATOM   10735 O  OD2 . ASP C 1 145 ? 19.747  34.438  55.576  1.00 41.29 ? 137  ASP C OD2 1 
ATOM   10736 N  N   . GLY C 1 146 ? 21.049  28.756  54.621  1.00 31.94 ? 138  GLY C N   1 
ATOM   10737 C  CA  . GLY C 1 146 ? 22.062  27.850  54.121  1.00 36.45 ? 138  GLY C CA  1 
ATOM   10738 C  C   . GLY C 1 146 ? 23.481  28.159  54.553  1.00 41.09 ? 138  GLY C C   1 
ATOM   10739 O  O   . GLY C 1 146 ? 24.405  27.472  54.100  1.00 44.05 ? 138  GLY C O   1 
ATOM   10740 N  N   . LEU C 1 147 ? 23.685  29.181  55.392  1.00 30.62 ? 139  LEU C N   1 
ATOM   10741 C  CA  . LEU C 1 147 ? 24.976  29.472  56.014  1.00 21.48 ? 139  LEU C CA  1 
ATOM   10742 C  C   . LEU C 1 147 ? 25.056  28.632  57.278  1.00 20.80 ? 139  LEU C C   1 
ATOM   10743 O  O   . LEU C 1 147 ? 24.653  29.063  58.363  1.00 22.20 ? 139  LEU C O   1 
ATOM   10744 C  CB  . LEU C 1 147 ? 25.117  30.954  56.339  1.00 28.51 ? 139  LEU C CB  1 
ATOM   10745 C  CG  . LEU C 1 147 ? 24.930  31.989  55.223  1.00 30.00 ? 139  LEU C CG  1 
ATOM   10746 C  CD1 . LEU C 1 147 ? 25.457  33.337  55.686  1.00 26.36 ? 139  LEU C CD1 1 
ATOM   10747 C  CD2 . LEU C 1 147 ? 25.617  31.546  53.937  1.00 33.06 ? 139  LEU C CD2 1 
ATOM   10748 N  N   . ASN C 1 148 ? 25.569  27.410  57.134  1.00 20.17 ? 140  ASN C N   1 
ATOM   10749 C  CA  . ASN C 1 148 ? 25.524  26.430  58.220  1.00 21.34 ? 140  ASN C CA  1 
ATOM   10750 C  C   . ASN C 1 148 ? 26.802  26.543  59.043  1.00 21.00 ? 140  ASN C C   1 
ATOM   10751 O  O   . ASN C 1 148 ? 27.707  25.708  58.971  1.00 17.21 ? 140  ASN C O   1 
ATOM   10752 C  CB  . ASN C 1 148 ? 25.334  25.024  57.668  1.00 23.48 ? 140  ASN C CB  1 
ATOM   10753 C  CG  . ASN C 1 148 ? 24.077  24.898  56.854  1.00 36.20 ? 140  ASN C CG  1 
ATOM   10754 O  OD1 . ASN C 1 148 ? 23.117  25.641  57.064  1.00 37.83 ? 140  ASN C OD1 1 
ATOM   10755 N  ND2 . ASN C 1 148 ? 24.071  23.961  55.911  1.00 38.58 ? 140  ASN C ND2 1 
ATOM   10756 N  N   . ILE C 1 149 ? 26.862  27.599  59.858  1.00 19.23 ? 141  ILE C N   1 
ATOM   10757 C  CA  . ILE C 1 149 ? 28.017  27.796  60.728  1.00 16.67 ? 141  ILE C CA  1 
ATOM   10758 C  C   . ILE C 1 149 ? 28.130  26.740  61.822  1.00 20.01 ? 141  ILE C C   1 
ATOM   10759 O  O   . ILE C 1 149 ? 29.182  26.652  62.466  1.00 17.23 ? 141  ILE C O   1 
ATOM   10760 C  CB  . ILE C 1 149 ? 28.002  29.202  61.369  1.00 16.86 ? 141  ILE C CB  1 
ATOM   10761 C  CG1 . ILE C 1 149 ? 26.764  29.402  62.244  1.00 19.53 ? 141  ILE C CG1 1 
ATOM   10762 C  CG2 . ILE C 1 149 ? 28.080  30.283  60.309  1.00 18.09 ? 141  ILE C CG2 1 
ATOM   10763 C  CD1 . ILE C 1 149 ? 26.811  30.713  63.058  1.00 18.77 ? 141  ILE C CD1 1 
ATOM   10764 N  N   . VAL C 1 150 ? 27.086  25.947  62.073  1.00 18.12 ? 142  VAL C N   1 
ATOM   10765 C  CA  . VAL C 1 150 ? 27.195  24.773  62.937  1.00 15.79 ? 142  VAL C CA  1 
ATOM   10766 C  C   . VAL C 1 150 ? 26.972  23.543  62.077  1.00 17.54 ? 142  VAL C C   1 
ATOM   10767 O  O   . VAL C 1 150 ? 25.853  23.286  61.618  1.00 16.73 ? 142  VAL C O   1 
ATOM   10768 C  CB  . VAL C 1 150 ? 26.206  24.776  64.106  1.00 14.61 ? 142  VAL C CB  1 
ATOM   10769 C  CG1 . VAL C 1 150 ? 26.500  23.561  64.992  1.00 12.74 ? 142  VAL C CG1 1 
ATOM   10770 C  CG2 . VAL C 1 150 ? 26.283  26.073  64.902  1.00 17.12 ? 142  VAL C CG2 1 
ATOM   10771 N  N   . ASP C 1 151 ? 28.030  22.762  61.890  1.00 16.99 ? 143  ASP C N   1 
ATOM   10772 C  CA  . ASP C 1 151 ? 27.965  21.605  61.011  1.00 14.99 ? 143  ASP C CA  1 
ATOM   10773 C  C   . ASP C 1 151 ? 29.172  20.719  61.265  1.00 15.87 ? 143  ASP C C   1 
ATOM   10774 O  O   . ASP C 1 151 ? 30.201  20.874  60.599  1.00 16.27 ? 143  ASP C O   1 
ATOM   10775 C  CB  . ASP C 1 151 ? 27.933  22.059  59.548  1.00 17.07 ? 143  ASP C CB  1 
ATOM   10776 C  CG  . ASP C 1 151 ? 27.828  20.906  58.576  1.00 23.31 ? 143  ASP C CG  1 
ATOM   10777 O  OD1 . ASP C 1 151 ? 27.485  19.780  58.995  1.00 22.89 ? 143  ASP C OD1 1 
ATOM   10778 O  OD2 . ASP C 1 151 ? 28.103  21.135  57.384  1.00 22.05 ? 143  ASP C OD2 1 
ATOM   10779 N  N   . HIS C 1 152 ? 29.081  19.806  62.228  1.00 14.40 ? 144  HIS C N   1 
ATOM   10780 C  CA  . HIS C 1 152 ? 30.207  18.918  62.479  1.00 15.38 ? 144  HIS C CA  1 
ATOM   10781 C  C   . HIS C 1 152 ? 29.706  17.617  63.089  1.00 15.33 ? 144  HIS C C   1 
ATOM   10782 O  O   . HIS C 1 152 ? 28.560  17.507  63.532  1.00 15.80 ? 144  HIS C O   1 
ATOM   10783 C  CB  . HIS C 1 152 ? 31.266  19.590  63.367  1.00 13.77 ? 144  HIS C CB  1 
ATOM   10784 C  CG  . HIS C 1 152 ? 30.742  20.049  64.691  1.00 16.77 ? 144  HIS C CG  1 
ATOM   10785 N  ND1 . HIS C 1 152 ? 30.388  21.359  64.939  1.00 12.60 ? 144  HIS C ND1 1 
ATOM   10786 C  CD2 . HIS C 1 152 ? 30.512  19.373  65.840  1.00 16.74 ? 144  HIS C CD2 1 
ATOM   10787 C  CE1 . HIS C 1 152 ? 29.962  21.470  66.183  1.00 16.85 ? 144  HIS C CE1 1 
ATOM   10788 N  NE2 . HIS C 1 152 ? 30.024  20.280  66.751  1.00 15.74 ? 144  HIS C NE2 1 
ATOM   10789 N  N   . TYR C 1 153 ? 30.584  16.623  63.092  1.00 13.84 ? 145  TYR C N   1 
ATOM   10790 C  CA  . TYR C 1 153 ? 30.248  15.273  63.508  1.00 13.74 ? 145  TYR C CA  1 
ATOM   10791 C  C   . TYR C 1 153 ? 30.798  14.978  64.893  1.00 15.55 ? 145  TYR C C   1 
ATOM   10792 O  O   . TYR C 1 153 ? 31.680  15.673  65.400  1.00 16.51 ? 145  TYR C O   1 
ATOM   10793 C  CB  . TYR C 1 153 ? 30.789  14.253  62.505  1.00 13.16 ? 145  TYR C CB  1 
ATOM   10794 C  CG  . TYR C 1 153 ? 29.890  14.133  61.298  1.00 16.39 ? 145  TYR C CG  1 
ATOM   10795 C  CD1 . TYR C 1 153 ? 29.908  15.086  60.288  1.00 24.80 ? 145  TYR C CD1 1 
ATOM   10796 C  CD2 . TYR C 1 153 ? 29.011  13.069  61.181  1.00 16.40 ? 145  TYR C CD2 1 
ATOM   10797 C  CE1 . TYR C 1 153 ? 29.060  14.972  59.186  1.00 28.70 ? 145  TYR C CE1 1 
ATOM   10798 C  CE2 . TYR C 1 153 ? 28.176  12.948  60.100  1.00 20.09 ? 145  TYR C CE2 1 
ATOM   10799 C  CZ  . TYR C 1 153 ? 28.197  13.892  59.111  1.00 30.23 ? 145  TYR C CZ  1 
ATOM   10800 O  OH  . TYR C 1 153 ? 27.345  13.725  58.045  1.00 36.51 ? 145  TYR C OH  1 
ATOM   10801 N  N   . THR C 1 154 ? 30.258  13.922  65.498  1.00 16.08 ? 146  THR C N   1 
ATOM   10802 C  CA  . THR C 1 154 ? 30.717  13.413  66.785  1.00 14.94 ? 146  THR C CA  1 
ATOM   10803 C  C   . THR C 1 154 ? 31.077  11.949  66.582  1.00 15.25 ? 146  THR C C   1 
ATOM   10804 O  O   . THR C 1 154 ? 30.192  11.122  66.338  1.00 12.03 ? 146  THR C O   1 
ATOM   10805 C  CB  . THR C 1 154 ? 29.649  13.562  67.871  1.00 10.38 ? 146  THR C CB  1 
ATOM   10806 O  OG1 . THR C 1 154 ? 29.123  14.894  67.864  1.00 13.94 ? 146  THR C OG1 1 
ATOM   10807 C  CG2 . THR C 1 154 ? 30.256  13.268  69.235  1.00 10.40 ? 146  THR C CG2 1 
ATOM   10808 N  N   . TYR C 1 155 ? 32.371  11.638  66.648  1.00 12.51 ? 147  TYR C N   1 
ATOM   10809 C  CA  . TYR C 1 155 ? 32.883  10.283  66.466  1.00 12.94 ? 147  TYR C CA  1 
ATOM   10810 C  C   . TYR C 1 155 ? 33.310  9.693   67.802  1.00 12.80 ? 147  TYR C C   1 
ATOM   10811 O  O   . TYR C 1 155 ? 33.913  10.387  68.626  1.00 13.76 ? 147  TYR C O   1 
ATOM   10812 C  CB  . TYR C 1 155 ? 34.074  10.264  65.523  1.00 12.50 ? 147  TYR C CB  1 
ATOM   10813 C  CG  . TYR C 1 155 ? 33.789  10.748  64.120  1.00 13.73 ? 147  TYR C CG  1 
ATOM   10814 C  CD1 . TYR C 1 155 ? 33.190  9.913   63.191  1.00 13.72 ? 147  TYR C CD1 1 
ATOM   10815 C  CD2 . TYR C 1 155 ? 34.145  12.034  63.721  1.00 15.36 ? 147  TYR C CD2 1 
ATOM   10816 C  CE1 . TYR C 1 155 ? 32.940  10.346  61.887  1.00 14.50 ? 147  TYR C CE1 1 
ATOM   10817 C  CE2 . TYR C 1 155 ? 33.906  12.477  62.423  1.00 14.54 ? 147  TYR C CE2 1 
ATOM   10818 C  CZ  . TYR C 1 155 ? 33.302  11.633  61.516  1.00 14.68 ? 147  TYR C CZ  1 
ATOM   10819 O  OH  . TYR C 1 155 ? 33.069  12.072  60.239  1.00 15.56 ? 147  TYR C OH  1 
ATOM   10820 N  N   . VAL C 1 156 ? 33.001  8.409   68.013  1.00 14.36 ? 148  VAL C N   1 
ATOM   10821 C  CA  . VAL C 1 156 ? 33.255  7.729   69.283  1.00 16.43 ? 148  VAL C CA  1 
ATOM   10822 C  C   . VAL C 1 156 ? 33.933  6.394   69.021  1.00 16.07 ? 148  VAL C C   1 
ATOM   10823 O  O   . VAL C 1 156 ? 33.501  5.636   68.146  1.00 15.04 ? 148  VAL C O   1 
ATOM   10824 C  CB  . VAL C 1 156 ? 31.953  7.474   70.067  1.00 11.48 ? 148  VAL C CB  1 
ATOM   10825 C  CG1 . VAL C 1 156 ? 32.276  7.006   71.481  1.00 15.85 ? 148  VAL C CG1 1 
ATOM   10826 C  CG2 . VAL C 1 156 ? 31.106  8.711   70.081  1.00 10.98 ? 148  VAL C CG2 1 
ATOM   10827 N  N   . PHE C 1 157 ? 34.975  6.092   69.801  1.00 11.81 ? 149  PHE C N   1 
ATOM   10828 C  CA  . PHE C 1 157 ? 35.527  4.746   69.887  1.00 13.39 ? 149  PHE C CA  1 
ATOM   10829 C  C   . PHE C 1 157 ? 35.041  4.120   71.186  1.00 16.07 ? 149  PHE C C   1 
ATOM   10830 O  O   . PHE C 1 157 ? 35.140  4.746   72.249  1.00 14.13 ? 149  PHE C O   1 
ATOM   10831 C  CB  . PHE C 1 157 ? 37.059  4.754   69.862  1.00 13.12 ? 149  PHE C CB  1 
ATOM   10832 C  CG  . PHE C 1 157 ? 37.659  4.926   68.485  1.00 15.23 ? 149  PHE C CG  1 
ATOM   10833 C  CD1 . PHE C 1 157 ? 36.873  5.293   67.400  1.00 13.88 ? 149  PHE C CD1 1 
ATOM   10834 C  CD2 . PHE C 1 157 ? 39.007  4.705   68.284  1.00 17.84 ? 149  PHE C CD2 1 
ATOM   10835 C  CE1 . PHE C 1 157 ? 37.428  5.446   66.129  1.00 14.77 ? 149  PHE C CE1 1 
ATOM   10836 C  CE2 . PHE C 1 157 ? 39.579  4.852   67.020  1.00 20.27 ? 149  PHE C CE2 1 
ATOM   10837 C  CZ  . PHE C 1 157 ? 38.783  5.226   65.935  1.00 17.50 ? 149  PHE C CZ  1 
ATOM   10838 N  N   . MET C 1 158 ? 34.520  2.894   71.113  1.00 14.03 ? 150  MET C N   1 
ATOM   10839 C  CA  . MET C 1 158 ? 34.023  2.284   72.339  1.00 17.48 ? 150  MET C CA  1 
ATOM   10840 C  C   . MET C 1 158 ? 34.265  0.777   72.302  1.00 15.95 ? 150  MET C C   1 
ATOM   10841 O  O   . MET C 1 158 ? 34.439  0.188   71.234  1.00 19.85 ? 150  MET C O   1 
ATOM   10842 C  CB  . MET C 1 158 ? 32.544  2.675   72.596  1.00 18.45 ? 150  MET C CB  1 
ATOM   10843 C  CG  . MET C 1 158 ? 31.450  2.023   71.810  1.00 25.65 ? 150  MET C CG  1 
ATOM   10844 S  SD  . MET C 1 158 ? 29.835  2.823   72.211  1.00 22.80 ? 150  MET C SD  1 
ATOM   10845 C  CE  . MET C 1 158 ? 29.637  2.374   73.936  1.00 14.76 ? 150  MET C CE  1 
ATOM   10846 N  N   . GLY C 1 159 ? 34.352  0.178   73.494  1.00 12.86 ? 151  GLY C N   1 
ATOM   10847 C  CA  . GLY C 1 159 ? 34.699  -1.217  73.650  1.00 16.09 ? 151  GLY C CA  1 
ATOM   10848 C  C   . GLY C 1 159 ? 33.597  -2.007  74.343  1.00 15.33 ? 151  GLY C C   1 
ATOM   10849 O  O   . GLY C 1 159 ? 32.529  -1.482  74.665  1.00 16.88 ? 151  GLY C O   1 
ATOM   10850 N  N   . ASP C 1 160 ? 33.883  -3.295  74.558  1.00 14.13 ? 152  ASP C N   1 
ATOM   10851 C  CA  . ASP C 1 160 ? 32.893  -4.198  75.147  1.00 15.88 ? 152  ASP C CA  1 
ATOM   10852 C  C   . ASP C 1 160 ? 32.452  -3.737  76.532  1.00 19.14 ? 152  ASP C C   1 
ATOM   10853 O  O   . ASP C 1 160 ? 31.270  -3.843  76.879  1.00 13.82 ? 152  ASP C O   1 
ATOM   10854 C  CB  . ASP C 1 160 ? 33.450  -5.612  75.246  1.00 20.08 ? 152  ASP C CB  1 
ATOM   10855 C  CG  . ASP C 1 160 ? 33.530  -6.316  73.904  1.00 31.56 ? 152  ASP C CG  1 
ATOM   10856 O  OD1 . ASP C 1 160 ? 32.710  -6.031  73.011  1.00 35.10 ? 152  ASP C OD1 1 
ATOM   10857 O  OD2 . ASP C 1 160 ? 34.417  -7.172  73.752  1.00 35.74 ? 152  ASP C OD2 1 
ATOM   10858 N  N   . GLY C 1 161 ? 33.390  -3.280  77.357  1.00 14.15 ? 153  GLY C N   1 
ATOM   10859 C  CA  . GLY C 1 161 ? 33.047  -2.820  78.696  1.00 13.46 ? 153  GLY C CA  1 
ATOM   10860 C  C   . GLY C 1 161 ? 32.061  -1.667  78.658  1.00 13.51 ? 153  GLY C C   1 
ATOM   10861 O  O   . GLY C 1 161 ? 31.109  -1.604  79.428  1.00 14.90 ? 153  GLY C O   1 
HETATM 10862 N  N   . OCS C 1 162 ? 32.291  -0.738  77.742  1.00 12.74 ? 154  OCS C N   1 
HETATM 10863 C  CA  . OCS C 1 162 ? 31.363  0.371   77.553  1.00 14.21 ? 154  OCS C CA  1 
HETATM 10864 C  CB  . OCS C 1 162 ? 31.840  1.265   76.419  1.00 15.83 ? 154  OCS C CB  1 
HETATM 10865 S  SG  . OCS C 1 162 ? 33.445  2.013   76.730  1.00 17.52 ? 154  OCS C SG  1 
HETATM 10866 C  C   . OCS C 1 162 ? 29.959  -0.112  77.248  1.00 16.23 ? 154  OCS C C   1 
HETATM 10867 O  O   . OCS C 1 162 ? 28.985  0.419   77.776  1.00 12.04 ? 154  OCS C O   1 
HETATM 10868 O  OD1 . OCS C 1 162 ? 33.937  2.493   75.490  1.00 23.26 ? 154  OCS C OD1 1 
HETATM 10869 O  OD2 . OCS C 1 162 ? 33.275  3.093   77.628  1.00 16.77 ? 154  OCS C OD2 1 
HETATM 10870 O  OD3 . OCS C 1 162 ? 34.343  1.052   77.256  1.00 38.25 ? 154  OCS C OD3 1 
ATOM   10871 N  N   . LEU C 1 163 ? 29.863  -1.114  76.378  1.00 15.73 ? 155  LEU C N   1 
ATOM   10872 C  CA  . LEU C 1 163 ? 28.568  -1.613  75.930  1.00 12.15 ? 155  LEU C CA  1 
ATOM   10873 C  C   . LEU C 1 163 ? 27.857  -2.430  76.995  1.00 15.05 ? 155  LEU C C   1 
ATOM   10874 O  O   . LEU C 1 163 ? 26.632  -2.512  77.009  1.00 16.14 ? 155  LEU C O   1 
ATOM   10875 C  CB  . LEU C 1 163 ? 28.742  -2.462  74.675  1.00 12.72 ? 155  LEU C CB  1 
ATOM   10876 C  CG  . LEU C 1 163 ? 29.133  -1.687  73.417  1.00 16.91 ? 155  LEU C CG  1 
ATOM   10877 C  CD1 . LEU C 1 163 ? 29.448  -2.654  72.270  1.00 16.43 ? 155  LEU C CD1 1 
ATOM   10878 C  CD2 . LEU C 1 163 ? 28.015  -0.706  73.034  1.00 16.77 ? 155  LEU C CD2 1 
ATOM   10879 N  N   . MET C 1 164 ? 28.635  -3.081  77.860  1.00 12.86 ? 156  MET C N   1 
ATOM   10880 C  CA  . MET C 1 164 ? 28.032  -3.830  78.957  1.00 13.31 ? 156  MET C CA  1 
ATOM   10881 C  C   . MET C 1 164 ? 27.398  -2.897  79.977  1.00 13.17 ? 156  MET C C   1 
ATOM   10882 O  O   . MET C 1 164 ? 26.386  -3.249  80.596  1.00 13.29 ? 156  MET C O   1 
ATOM   10883 C  CB  . MET C 1 164 ? 29.078  -4.721  79.629  1.00 13.91 ? 156  MET C CB  1 
ATOM   10884 C  CG  . MET C 1 164 ? 29.270  -6.080  78.940  1.00 14.68 ? 156  MET C CG  1 
ATOM   10885 S  SD  . MET C 1 164 ? 30.456  -7.156  79.789  1.00 17.76 ? 156  MET C SD  1 
ATOM   10886 C  CE  . MET C 1 164 ? 31.947  -6.806  78.866  1.00 18.96 ? 156  MET C CE  1 
ATOM   10887 N  N   . GLU C 1 165 ? 27.971  -1.712  80.153  1.00 12.38 ? 157  GLU C N   1 
ATOM   10888 C  CA  . GLU C 1 165 ? 27.487  -0.776  81.163  1.00 14.23 ? 157  GLU C CA  1 
ATOM   10889 C  C   . GLU C 1 165 ? 26.091  -0.270  80.825  1.00 12.59 ? 157  GLU C C   1 
ATOM   10890 O  O   . GLU C 1 165 ? 25.804  0.082   79.678  1.00 13.20 ? 157  GLU C O   1 
ATOM   10891 C  CB  . GLU C 1 165 ? 28.445  0.411   81.283  1.00 11.70 ? 157  GLU C CB  1 
ATOM   10892 C  CG  . GLU C 1 165 ? 29.735  0.091   82.036  1.00 14.34 ? 157  GLU C CG  1 
ATOM   10893 C  CD  . GLU C 1 165 ? 29.545  -0.123  83.533  1.00 12.64 ? 157  GLU C CD  1 
ATOM   10894 O  OE1 . GLU C 1 165 ? 28.412  0.000   84.053  1.00 13.18 ? 157  GLU C OE1 1 
ATOM   10895 O  OE2 . GLU C 1 165 ? 30.558  -0.426  84.198  1.00 13.67 ? 157  GLU C OE2 1 
ATOM   10896 N  N   . GLY C 1 166 ? 25.231  -0.203  81.849  1.00 12.40 ? 158  GLY C N   1 
ATOM   10897 C  CA  . GLY C 1 166 ? 23.879  0.285   81.640  1.00 11.81 ? 158  GLY C CA  1 
ATOM   10898 C  C   . GLY C 1 166 ? 23.819  1.700   81.102  1.00 13.78 ? 158  GLY C C   1 
ATOM   10899 O  O   . GLY C 1 166 ? 22.908  2.043   80.358  1.00 12.25 ? 158  GLY C O   1 
ATOM   10900 N  N   . VAL C 1 167 ? 24.798  2.538   81.441  1.00 12.88 ? 159  VAL C N   1 
ATOM   10901 C  CA  . VAL C 1 167 ? 24.673  3.918   80.978  1.00 12.89 ? 159  VAL C CA  1 
ATOM   10902 C  C   . VAL C 1 167 ? 24.805  3.993   79.456  1.00 13.22 ? 159  VAL C C   1 
ATOM   10903 O  O   . VAL C 1 167 ? 24.221  4.881   78.822  1.00 13.86 ? 159  VAL C O   1 
ATOM   10904 C  CB  . VAL C 1 167 ? 25.673  4.828   81.717  1.00 10.95 ? 159  VAL C CB  1 
ATOM   10905 C  CG1 . VAL C 1 167 ? 27.099  4.520   81.298  1.00 11.42 ? 159  VAL C CG1 1 
ATOM   10906 C  CG2 . VAL C 1 167 ? 25.336  6.315   81.489  1.00 10.52 ? 159  VAL C CG2 1 
ATOM   10907 N  N   . SER C 1 168 ? 25.499  3.035   78.832  1.00 14.47 ? 160  SER C N   1 
ATOM   10908 C  CA  . SER C 1 168 ? 25.531  3.007   77.369  1.00 13.25 ? 160  SER C CA  1 
ATOM   10909 C  C   . SER C 1 168 ? 24.159  2.692   76.798  1.00 13.77 ? 160  SER C C   1 
ATOM   10910 O  O   . SER C 1 168 ? 23.757  3.262   75.776  1.00 12.92 ? 160  SER C O   1 
ATOM   10911 C  CB  . SER C 1 168 ? 26.555  1.984   76.870  1.00 14.97 ? 160  SER C CB  1 
ATOM   10912 O  OG  . SER C 1 168 ? 26.034  0.659   76.939  1.00 17.17 ? 160  SER C OG  1 
ATOM   10913 N  N   . HIS C 1 169 ? 23.424  1.790   77.450  1.00 10.01 ? 161  HIS C N   1 
ATOM   10914 C  CA  . HIS C 1 169 ? 22.051  1.519   77.036  1.00 11.46 ? 161  HIS C CA  1 
ATOM   10915 C  C   . HIS C 1 169 ? 21.198  2.785   77.094  1.00 10.30 ? 161  HIS C C   1 
ATOM   10916 O  O   . HIS C 1 169 ? 20.478  3.101   76.136  1.00 12.20 ? 161  HIS C O   1 
ATOM   10917 C  CB  . HIS C 1 169 ? 21.460  0.406   77.912  1.00 11.40 ? 161  HIS C CB  1 
ATOM   10918 C  CG  . HIS C 1 169 ? 19.964  0.301   77.852  1.00 10.94 ? 161  HIS C CG  1 
ATOM   10919 N  ND1 . HIS C 1 169 ? 19.291  -0.232  76.769  1.00 12.88 ? 161  HIS C ND1 1 
ATOM   10920 C  CD2 . HIS C 1 169 ? 19.014  0.631   78.761  1.00 10.51 ? 161  HIS C CD2 1 
ATOM   10921 C  CE1 . HIS C 1 169 ? 17.993  -0.203  77.007  1.00 16.17 ? 161  HIS C CE1 1 
ATOM   10922 N  NE2 . HIS C 1 169 ? 17.796  0.318   78.208  1.00 10.64 ? 161  HIS C NE2 1 
ATOM   10923 N  N   . GLU C 1 170 ? 21.262  3.518   78.214  1.00 11.08 ? 162  GLU C N   1 
ATOM   10924 C  CA  . GLU C 1 170 ? 20.444  4.724   78.366  1.00 12.48 ? 162  GLU C CA  1 
ATOM   10925 C  C   . GLU C 1 170 ? 20.786  5.759   77.304  1.00 13.04 ? 162  GLU C C   1 
ATOM   10926 O  O   . GLU C 1 170 ? 19.893  6.317   76.652  1.00 9.91  ? 162  GLU C O   1 
ATOM   10927 C  CB  . GLU C 1 170 ? 20.634  5.324   79.765  1.00 12.45 ? 162  GLU C CB  1 
ATOM   10928 C  CG  . GLU C 1 170 ? 20.109  4.433   80.896  1.00 10.96 ? 162  GLU C CG  1 
ATOM   10929 C  CD  . GLU C 1 170 ? 20.378  5.014   82.278  1.00 11.09 ? 162  GLU C CD  1 
ATOM   10930 O  OE1 . GLU C 1 170 ? 20.371  4.241   83.263  1.00 13.72 ? 162  GLU C OE1 1 
ATOM   10931 O  OE2 . GLU C 1 170 ? 20.602  6.242   82.389  1.00 14.51 ? 162  GLU C OE2 1 
ATOM   10932 N  N   . ALA C 1 171 ? 22.087  6.039   77.120  1.00 12.35 ? 163  ALA C N   1 
ATOM   10933 C  CA  . ALA C 1 171 ? 22.487  7.100   76.201  1.00 11.76 ? 163  ALA C CA  1 
ATOM   10934 C  C   . ALA C 1 171 ? 22.190  6.735   74.754  1.00 14.13 ? 163  ALA C C   1 
ATOM   10935 O  O   . ALA C 1 171 ? 21.726  7.582   73.983  1.00 12.11 ? 163  ALA C O   1 
ATOM   10936 C  CB  . ALA C 1 171 ? 23.969  7.421   76.377  1.00 12.17 ? 163  ALA C CB  1 
ATOM   10937 N  N   . CYS C 1 172 ? 22.452  5.486   74.362  1.00 13.31 ? 164  CYS C N   1 
ATOM   10938 C  CA  . CYS C 1 172 ? 22.218  5.093   72.972  1.00 12.50 ? 164  CYS C CA  1 
ATOM   10939 C  C   . CYS C 1 172 ? 20.735  4.908   72.671  1.00 11.31 ? 164  CYS C C   1 
ATOM   10940 O  O   . CYS C 1 172 ? 20.303  5.108   71.528  1.00 11.05 ? 164  CYS C O   1 
ATOM   10941 C  CB  . CYS C 1 172 ? 22.983  3.809   72.656  1.00 11.41 ? 164  CYS C CB  1 
ATOM   10942 S  SG  . CYS C 1 172 ? 24.782  4.047   72.709  1.00 13.12 ? 164  CYS C SG  1 
ATOM   10943 N  N   . SER C 1 173 ? 19.947  4.506   73.666  1.00 11.04 ? 165  SER C N   1 
ATOM   10944 C  CA  . SER C 1 173 ? 18.502  4.455   73.465  1.00 9.99  ? 165  SER C CA  1 
ATOM   10945 C  C   . SER C 1 173 ? 17.963  5.840   73.137  1.00 9.16  ? 165  SER C C   1 
ATOM   10946 O  O   . SER C 1 173 ? 17.218  6.018   72.168  1.00 11.02 ? 165  SER C O   1 
ATOM   10947 C  CB  . SER C 1 173 ? 17.815  3.877   74.714  1.00 10.96 ? 165  SER C CB  1 
ATOM   10948 O  OG  . SER C 1 173 ? 16.400  3.893   74.587  1.00 14.95 ? 165  SER C OG  1 
ATOM   10949 N  N   . LEU C 1 174 ? 18.365  6.841   73.925  1.00 16.71 ? 166  LEU C N   1 
ATOM   10950 C  CA  . LEU C 1 174 ? 17.894  8.210   73.724  1.00 13.98 ? 166  LEU C CA  1 
ATOM   10951 C  C   . LEU C 1 174 ? 18.426  8.804   72.426  1.00 10.97 ? 166  LEU C C   1 
ATOM   10952 O  O   . LEU C 1 174 ? 17.715  9.559   71.751  1.00 12.57 ? 166  LEU C O   1 
ATOM   10953 C  CB  . LEU C 1 174 ? 18.311  9.077   74.912  1.00 9.03  ? 166  LEU C CB  1 
ATOM   10954 C  CG  . LEU C 1 174 ? 17.822  10.519  74.933  1.00 16.42 ? 166  LEU C CG  1 
ATOM   10955 C  CD1 . LEU C 1 174 ? 16.301  10.558  74.921  1.00 18.10 ? 166  LEU C CD1 1 
ATOM   10956 C  CD2 . LEU C 1 174 ? 18.368  11.211  76.176  1.00 16.44 ? 166  LEU C CD2 1 
ATOM   10957 N  N   . ALA C 1 175 ? 19.677  8.488   72.069  1.00 9.55  ? 167  ALA C N   1 
ATOM   10958 C  CA  . ALA C 1 175 ? 20.234  8.959   70.804  1.00 10.21 ? 167  ALA C CA  1 
ATOM   10959 C  C   . ALA C 1 175 ? 19.441  8.422   69.618  1.00 12.24 ? 167  ALA C C   1 
ATOM   10960 O  O   . ALA C 1 175 ? 19.266  9.118   68.611  1.00 15.27 ? 167  ALA C O   1 
ATOM   10961 C  CB  . ALA C 1 175 ? 21.700  8.535   70.679  1.00 13.61 ? 167  ALA C CB  1 
ATOM   10962 N  N   . GLY C 1 176 ? 18.981  7.176   69.712  1.00 10.74 ? 168  GLY C N   1 
ATOM   10963 C  CA  . GLY C 1 176 ? 18.160  6.619   68.648  1.00 14.07 ? 168  GLY C CA  1 
ATOM   10964 C  C   . GLY C 1 176 ? 16.807  7.299   68.544  1.00 13.81 ? 168  GLY C C   1 
ATOM   10965 O  O   . GLY C 1 176 ? 16.309  7.549   67.443  1.00 15.62 ? 168  GLY C O   1 
ATOM   10966 N  N   . THR C 1 177 ? 16.195  7.606   69.684  1.00 14.39 ? 169  THR C N   1 
ATOM   10967 C  CA  . THR C 1 177 ? 14.918  8.316   69.672  1.00 14.31 ? 169  THR C CA  1 
ATOM   10968 C  C   . THR C 1 177 ? 15.058  9.698   69.048  1.00 15.66 ? 169  THR C C   1 
ATOM   10969 O  O   . THR C 1 177 ? 14.174  10.141  68.310  1.00 13.11 ? 169  THR C O   1 
ATOM   10970 C  CB  . THR C 1 177 ? 14.371  8.429   71.096  1.00 18.28 ? 169  THR C CB  1 
ATOM   10971 O  OG1 . THR C 1 177 ? 14.090  7.117   71.593  1.00 15.56 ? 169  THR C OG1 1 
ATOM   10972 C  CG2 . THR C 1 177 ? 13.089  9.269   71.127  1.00 21.44 ? 169  THR C CG2 1 
ATOM   10973 N  N   . LEU C 1 178 ? 16.164  10.390  69.324  1.00 12.00 ? 170  LEU C N   1 
ATOM   10974 C  CA  . LEU C 1 178 ? 16.361  11.743  68.824  1.00 13.61 ? 170  LEU C CA  1 
ATOM   10975 C  C   . LEU C 1 178 ? 17.023  11.781  67.451  1.00 15.97 ? 170  LEU C C   1 
ATOM   10976 O  O   . LEU C 1 178 ? 17.239  12.874  66.914  1.00 14.90 ? 170  LEU C O   1 
ATOM   10977 C  CB  . LEU C 1 178 ? 17.172  12.568  69.834  1.00 14.75 ? 170  LEU C CB  1 
ATOM   10978 C  CG  . LEU C 1 178 ? 16.401  12.796  71.148  1.00 18.53 ? 170  LEU C CG  1 
ATOM   10979 C  CD1 . LEU C 1 178 ? 17.259  13.495  72.186  1.00 19.95 ? 170  LEU C CD1 1 
ATOM   10980 C  CD2 . LEU C 1 178 ? 15.110  13.589  70.904  1.00 20.38 ? 170  LEU C CD2 1 
ATOM   10981 N  N   . GLY C 1 179 ? 17.331  10.626  66.868  1.00 16.87 ? 171  GLY C N   1 
ATOM   10982 C  CA  . GLY C 1 179 ? 17.779  10.584  65.486  1.00 15.48 ? 171  GLY C CA  1 
ATOM   10983 C  C   . GLY C 1 179 ? 19.069  11.348  65.235  1.00 16.49 ? 171  GLY C C   1 
ATOM   10984 O  O   . GLY C 1 179 ? 19.171  12.121  64.269  1.00 18.39 ? 171  GLY C O   1 
ATOM   10985 N  N   . LEU C 1 180 ? 20.073  11.126  66.082  1.00 13.99 ? 172  LEU C N   1 
ATOM   10986 C  CA  . LEU C 1 180 ? 21.293  11.924  66.036  1.00 14.01 ? 172  LEU C CA  1 
ATOM   10987 C  C   . LEU C 1 180 ? 22.188  11.375  64.929  1.00 14.93 ? 172  LEU C C   1 
ATOM   10988 O  O   . LEU C 1 180 ? 23.141  10.624  65.164  1.00 12.13 ? 172  LEU C O   1 
ATOM   10989 C  CB  . LEU C 1 180 ? 21.994  11.909  67.387  1.00 15.64 ? 172  LEU C CB  1 
ATOM   10990 C  CG  . LEU C 1 180 ? 21.206  12.449  68.583  1.00 12.33 ? 172  LEU C CG  1 
ATOM   10991 C  CD1 . LEU C 1 180 ? 22.090  12.423  69.819  1.00 12.04 ? 172  LEU C CD1 1 
ATOM   10992 C  CD2 . LEU C 1 180 ? 20.683  13.846  68.335  1.00 10.55 ? 172  LEU C CD2 1 
ATOM   10993 N  N   . GLY C 1 181 ? 21.886  11.796  63.699  1.00 12.23 ? 173  GLY C N   1 
ATOM   10994 C  CA  . GLY C 1 181 ? 22.542  11.260  62.519  1.00 15.72 ? 173  GLY C CA  1 
ATOM   10995 C  C   . GLY C 1 181 ? 24.000  11.635  62.375  1.00 15.63 ? 173  GLY C C   1 
ATOM   10996 O  O   . GLY C 1 181 ? 24.697  11.040  61.549  1.00 18.43 ? 173  GLY C O   1 
ATOM   10997 N  N   . LYS C 1 182 ? 24.487  12.581  63.166  1.00 12.40 ? 174  LYS C N   1 
ATOM   10998 C  CA  . LYS C 1 182 ? 25.883  12.964  63.094  1.00 11.32 ? 174  LYS C CA  1 
ATOM   10999 C  C   . LYS C 1 182 ? 26.726  12.280  64.163  1.00 13.26 ? 174  LYS C C   1 
ATOM   11000 O  O   . LYS C 1 182 ? 27.921  12.558  64.275  1.00 14.04 ? 174  LYS C O   1 
ATOM   11001 C  CB  . LYS C 1 182 ? 26.003  14.481  63.185  1.00 13.14 ? 174  LYS C CB  1 
ATOM   11002 C  CG  . LYS C 1 182 ? 25.398  15.187  61.982  1.00 17.08 ? 174  LYS C CG  1 
ATOM   11003 C  CD  . LYS C 1 182 ? 25.464  16.679  62.169  1.00 23.29 ? 174  LYS C CD  1 
ATOM   11004 C  CE  . LYS C 1 182 ? 25.876  17.374  60.903  1.00 22.46 ? 174  LYS C CE  1 
ATOM   11005 N  NZ  . LYS C 1 182 ? 25.533  18.813  60.984  1.00 23.55 ? 174  LYS C NZ  1 
ATOM   11006 N  N   . LEU C 1 183 ? 26.134  11.372  64.920  1.00 11.99 ? 175  LEU C N   1 
ATOM   11007 C  CA  . LEU C 1 183 ? 26.856  10.563  65.895  1.00 9.69  ? 175  LEU C CA  1 
ATOM   11008 C  C   . LEU C 1 183 ? 27.242  9.243   65.243  1.00 15.45 ? 175  LEU C C   1 
ATOM   11009 O  O   . LEU C 1 183 ? 26.371  8.500   64.777  1.00 15.00 ? 175  LEU C O   1 
ATOM   11010 C  CB  . LEU C 1 183 ? 25.981  10.323  67.129  1.00 9.32  ? 175  LEU C CB  1 
ATOM   11011 C  CG  . LEU C 1 183 ? 26.552  9.385   68.198  1.00 12.46 ? 175  LEU C CG  1 
ATOM   11012 C  CD1 . LEU C 1 183 ? 27.813  10.002  68.835  1.00 17.35 ? 175  LEU C CD1 1 
ATOM   11013 C  CD2 . LEU C 1 183 ? 25.504  9.112   69.273  1.00 11.89 ? 175  LEU C CD2 1 
ATOM   11014 N  N   . ILE C 1 184 ? 28.542  8.953   65.201  1.00 10.01 ? 176  ILE C N   1 
ATOM   11015 C  CA  . ILE C 1 184 ? 29.045  7.748   64.549  1.00 9.97  ? 176  ILE C CA  1 
ATOM   11016 C  C   . ILE C 1 184 ? 30.025  7.079   65.492  1.00 14.17 ? 176  ILE C C   1 
ATOM   11017 O  O   . ILE C 1 184 ? 31.013  7.696   65.914  1.00 14.45 ? 176  ILE C O   1 
ATOM   11018 C  CB  . ILE C 1 184 ? 29.710  8.051   63.198  1.00 11.71 ? 176  ILE C CB  1 
ATOM   11019 C  CG1 . ILE C 1 184 ? 28.662  8.629   62.231  1.00 14.55 ? 176  ILE C CG1 1 
ATOM   11020 C  CG2 . ILE C 1 184 ? 30.317  6.784   62.602  1.00 11.81 ? 176  ILE C CG2 1 
ATOM   11021 C  CD1 . ILE C 1 184 ? 29.282  9.161   60.925  1.00 14.98 ? 176  ILE C CD1 1 
ATOM   11022 N  N   . VAL C 1 185 ? 29.750  5.824   65.816  1.00 12.79 ? 177  VAL C N   1 
ATOM   11023 C  CA  . VAL C 1 185 ? 30.505  5.049   66.787  1.00 12.78 ? 177  VAL C CA  1 
ATOM   11024 C  C   . VAL C 1 185 ? 31.255  3.963   66.038  1.00 14.87 ? 177  VAL C C   1 
ATOM   11025 O  O   . VAL C 1 185 ? 30.676  3.278   65.185  1.00 15.05 ? 177  VAL C O   1 
ATOM   11026 C  CB  . VAL C 1 185 ? 29.573  4.425   67.839  1.00 17.80 ? 177  VAL C CB  1 
ATOM   11027 C  CG1 . VAL C 1 185 ? 30.352  3.465   68.753  1.00 15.14 ? 177  VAL C CG1 1 
ATOM   11028 C  CG2 . VAL C 1 185 ? 28.852  5.512   68.633  1.00 17.50 ? 177  VAL C CG2 1 
ATOM   11029 N  N   . LEU C 1 186 ? 32.537  3.807   66.351  1.00 14.05 ? 178  LEU C N   1 
ATOM   11030 C  CA  . LEU C 1 186 ? 33.304  2.641   65.929  1.00 13.89 ? 178  LEU C CA  1 
ATOM   11031 C  C   . LEU C 1 186 ? 33.528  1.768   67.156  1.00 13.95 ? 178  LEU C C   1 
ATOM   11032 O  O   . LEU C 1 186 ? 34.184  2.190   68.121  1.00 15.02 ? 178  LEU C O   1 
ATOM   11033 C  CB  . LEU C 1 186 ? 34.640  3.020   65.278  1.00 18.70 ? 178  LEU C CB  1 
ATOM   11034 C  CG  . LEU C 1 186 ? 34.556  3.462   63.805  1.00 17.40 ? 178  LEU C CG  1 
ATOM   11035 C  CD1 . LEU C 1 186 ? 34.028  4.877   63.697  1.00 15.64 ? 178  LEU C CD1 1 
ATOM   11036 C  CD2 . LEU C 1 186 ? 35.893  3.331   63.108  1.00 21.81 ? 178  LEU C CD2 1 
ATOM   11037 N  N   . TYR C 1 187 ? 32.986  0.558   67.110  1.00 13.88 ? 179  TYR C N   1 
ATOM   11038 C  CA  . TYR C 1 187 ? 33.018  -0.368  68.232  1.00 15.24 ? 179  TYR C CA  1 
ATOM   11039 C  C   . TYR C 1 187 ? 34.168  -1.349  68.015  1.00 17.16 ? 179  TYR C C   1 
ATOM   11040 O  O   . TYR C 1 187 ? 34.255  -1.993  66.964  1.00 15.70 ? 179  TYR C O   1 
ATOM   11041 C  CB  . TYR C 1 187 ? 31.655  -1.058  68.367  1.00 11.94 ? 179  TYR C CB  1 
ATOM   11042 C  CG  . TYR C 1 187 ? 31.650  -2.392  69.088  1.00 16.27 ? 179  TYR C CG  1 
ATOM   11043 C  CD1 . TYR C 1 187 ? 32.385  -2.588  70.251  1.00 16.42 ? 179  TYR C CD1 1 
ATOM   11044 C  CD2 . TYR C 1 187 ? 30.869  -3.445  68.621  1.00 20.81 ? 179  TYR C CD2 1 
ATOM   11045 C  CE1 . TYR C 1 187 ? 32.377  -3.805  70.907  1.00 23.08 ? 179  TYR C CE1 1 
ATOM   11046 C  CE2 . TYR C 1 187 ? 30.848  -4.668  69.278  1.00 20.29 ? 179  TYR C CE2 1 
ATOM   11047 C  CZ  . TYR C 1 187 ? 31.604  -4.838  70.418  1.00 21.66 ? 179  TYR C CZ  1 
ATOM   11048 O  OH  . TYR C 1 187 ? 31.595  -6.052  71.068  1.00 23.84 ? 179  TYR C OH  1 
ATOM   11049 N  N   . ASP C 1 188 ? 35.061  -1.429  68.997  1.00 16.86 ? 180  ASP C N   1 
ATOM   11050 C  CA  . ASP C 1 188 ? 36.202  -2.345  68.979  1.00 17.05 ? 180  ASP C CA  1 
ATOM   11051 C  C   . ASP C 1 188 ? 35.706  -3.702  69.456  1.00 16.53 ? 180  ASP C C   1 
ATOM   11052 O  O   . ASP C 1 188 ? 35.674  -4.005  70.652  1.00 19.46 ? 180  ASP C O   1 
ATOM   11053 C  CB  . ASP C 1 188 ? 37.336  -1.818  69.855  1.00 15.46 ? 180  ASP C CB  1 
ATOM   11054 C  CG  . ASP C 1 188 ? 38.535  -2.765  69.907  1.00 23.22 ? 180  ASP C CG  1 
ATOM   11055 O  OD1 . ASP C 1 188 ? 38.702  -3.581  68.979  1.00 23.57 ? 180  ASP C OD1 1 
ATOM   11056 O  OD2 . ASP C 1 188 ? 39.311  -2.689  70.886  1.00 22.08 ? 180  ASP C OD2 1 
ATOM   11057 N  N   . ASP C 1 189 ? 35.302  -4.526  68.495  1.00 18.65 ? 181  ASP C N   1 
ATOM   11058 C  CA  . ASP C 1 189 ? 34.756  -5.852  68.758  1.00 20.74 ? 181  ASP C CA  1 
ATOM   11059 C  C   . ASP C 1 189 ? 35.927  -6.822  68.669  1.00 20.20 ? 181  ASP C C   1 
ATOM   11060 O  O   . ASP C 1 189 ? 36.205  -7.400  67.619  1.00 20.41 ? 181  ASP C O   1 
ATOM   11061 C  CB  . ASP C 1 189 ? 33.646  -6.167  67.758  1.00 20.17 ? 181  ASP C CB  1 
ATOM   11062 C  CG  . ASP C 1 189 ? 33.004  -7.524  67.982  1.00 27.11 ? 181  ASP C CG  1 
ATOM   11063 O  OD1 . ASP C 1 189 ? 33.609  -8.392  68.647  1.00 26.19 ? 181  ASP C OD1 1 
ATOM   11064 O  OD2 . ASP C 1 189 ? 31.888  -7.724  67.460  1.00 32.77 ? 181  ASP C OD2 1 
ATOM   11065 N  N   . ASN C 1 190 ? 36.626  -7.003  69.790  1.00 20.67 ? 182  ASN C N   1 
ATOM   11066 C  CA  . ASN C 1 190 ? 37.827  -7.839  69.829  1.00 29.43 ? 182  ASN C CA  1 
ATOM   11067 C  C   . ASN C 1 190 ? 37.531  -9.250  70.325  1.00 39.82 ? 182  ASN C C   1 
ATOM   11068 O  O   . ASN C 1 190 ? 38.348  -9.866  71.022  1.00 42.14 ? 182  ASN C O   1 
ATOM   11069 C  CB  . ASN C 1 190 ? 38.909  -7.179  70.679  1.00 31.27 ? 182  ASN C CB  1 
ATOM   11070 C  CG  . ASN C 1 190 ? 38.439  -6.847  72.085  1.00 37.73 ? 182  ASN C CG  1 
ATOM   11071 O  OD1 . ASN C 1 190 ? 37.423  -7.355  72.552  1.00 35.53 ? 182  ASN C OD1 1 
ATOM   11072 N  ND2 . ASN C 1 190 ? 39.187  -5.986  72.767  1.00 40.13 ? 182  ASN C ND2 1 
ATOM   11073 N  N   . ASN C 1 191 ? 36.377  -9.789  69.952  1.00 42.85 ? 183  ASN C N   1 
ATOM   11074 C  CA  . ASN C 1 191 ? 35.960  -11.120 70.375  1.00 46.33 ? 183  ASN C CA  1 
ATOM   11075 C  C   . ASN C 1 191 ? 35.923  -12.078 69.190  1.00 51.55 ? 183  ASN C C   1 
ATOM   11076 O  O   . ASN C 1 191 ? 35.768  -11.649 68.047  1.00 53.84 ? 183  ASN C O   1 
ATOM   11077 C  CB  . ASN C 1 191 ? 34.590  -11.049 71.049  1.00 42.88 ? 183  ASN C CB  1 
ATOM   11078 C  CG  . ASN C 1 191 ? 34.536  -9.989  72.130  1.00 43.22 ? 183  ASN C CG  1 
ATOM   11079 O  OD1 . ASN C 1 191 ? 35.186  -10.122 73.167  1.00 43.44 ? 183  ASN C OD1 1 
ATOM   11080 N  ND2 . ASN C 1 191 ? 33.763  -8.923  71.890  1.00 37.04 ? 183  ASN C ND2 1 
ATOM   11081 N  N   . ASP C 1 199 ? 32.472  -14.657 76.071  1.00 57.96 ? 191  ASP C N   1 
ATOM   11082 C  CA  . ASP C 1 199 ? 31.534  -15.766 75.955  1.00 56.06 ? 191  ASP C CA  1 
ATOM   11083 C  C   . ASP C 1 199 ? 30.963  -16.150 77.320  1.00 53.90 ? 191  ASP C C   1 
ATOM   11084 O  O   . ASP C 1 199 ? 29.766  -16.407 77.452  1.00 55.83 ? 191  ASP C O   1 
ATOM   11085 C  CB  . ASP C 1 199 ? 32.213  -16.974 75.305  1.00 58.85 ? 191  ASP C CB  1 
ATOM   11086 N  N   . GLY C 1 200 ? 31.826  -16.181 78.338  1.00 48.36 ? 192  GLY C N   1 
ATOM   11087 C  CA  . GLY C 1 200 ? 31.386  -16.529 79.679  1.00 46.11 ? 192  GLY C CA  1 
ATOM   11088 C  C   . GLY C 1 200 ? 30.504  -15.488 80.346  1.00 39.04 ? 192  GLY C C   1 
ATOM   11089 O  O   . GLY C 1 200 ? 29.830  -15.808 81.331  1.00 40.16 ? 192  GLY C O   1 
ATOM   11090 N  N   . TRP C 1 201 ? 30.494  -14.250 79.837  1.00 32.09 ? 193  TRP C N   1 
ATOM   11091 C  CA  . TRP C 1 201 ? 29.679  -13.210 80.458  1.00 30.56 ? 193  TRP C CA  1 
ATOM   11092 C  C   . TRP C 1 201 ? 29.198  -12.124 79.506  1.00 27.24 ? 193  TRP C C   1 
ATOM   11093 O  O   . TRP C 1 201 ? 28.472  -11.235 79.955  1.00 25.78 ? 193  TRP C O   1 
ATOM   11094 C  CB  . TRP C 1 201 ? 30.452  -12.557 81.617  1.00 35.17 ? 193  TRP C CB  1 
ATOM   11095 C  CG  . TRP C 1 201 ? 31.756  -11.953 81.189  1.00 35.89 ? 193  TRP C CG  1 
ATOM   11096 C  CD1 . TRP C 1 201 ? 31.951  -10.718 80.628  1.00 32.42 ? 193  TRP C CD1 1 
ATOM   11097 C  CD2 . TRP C 1 201 ? 33.046  -12.562 81.277  1.00 38.88 ? 193  TRP C CD2 1 
ATOM   11098 N  NE1 . TRP C 1 201 ? 33.284  -10.523 80.369  1.00 37.57 ? 193  TRP C NE1 1 
ATOM   11099 C  CE2 . TRP C 1 201 ? 33.978  -11.642 80.757  1.00 43.30 ? 193  TRP C CE2 1 
ATOM   11100 C  CE3 . TRP C 1 201 ? 33.504  -13.800 81.740  1.00 43.26 ? 193  TRP C CE3 1 
ATOM   11101 C  CZ2 . TRP C 1 201 ? 35.342  -11.920 80.694  1.00 49.42 ? 193  TRP C CZ2 1 
ATOM   11102 C  CZ3 . TRP C 1 201 ? 34.852  -14.074 81.679  1.00 47.93 ? 193  TRP C CZ3 1 
ATOM   11103 C  CH2 . TRP C 1 201 ? 35.758  -13.139 81.160  1.00 50.23 ? 193  TRP C CH2 1 
ATOM   11104 N  N   . PHE C 1 202 ? 29.571  -12.134 78.229  1.00 26.07 ? 194  PHE C N   1 
ATOM   11105 C  CA  . PHE C 1 202 ? 29.099  -11.107 77.298  1.00 28.36 ? 194  PHE C CA  1 
ATOM   11106 C  C   . PHE C 1 202 ? 28.839  -11.755 75.946  1.00 30.83 ? 194  PHE C C   1 
ATOM   11107 O  O   . PHE C 1 202 ? 29.782  -12.128 75.242  1.00 29.23 ? 194  PHE C O   1 
ATOM   11108 C  CB  . PHE C 1 202 ? 30.105  -9.963  77.170  1.00 29.07 ? 194  PHE C CB  1 
ATOM   11109 C  CG  . PHE C 1 202 ? 29.638  -8.839  76.289  1.00 26.24 ? 194  PHE C CG  1 
ATOM   11110 C  CD1 . PHE C 1 202 ? 28.432  -8.211  76.526  1.00 22.24 ? 194  PHE C CD1 1 
ATOM   11111 C  CD2 . PHE C 1 202 ? 30.411  -8.406  75.224  1.00 31.50 ? 194  PHE C CD2 1 
ATOM   11112 C  CE1 . PHE C 1 202 ? 28.002  -7.177  75.726  1.00 21.47 ? 194  PHE C CE1 1 
ATOM   11113 C  CE2 . PHE C 1 202 ? 29.981  -7.363  74.414  1.00 30.09 ? 194  PHE C CE2 1 
ATOM   11114 C  CZ  . PHE C 1 202 ? 28.773  -6.753  74.668  1.00 27.68 ? 194  PHE C CZ  1 
ATOM   11115 N  N   . THR C 1 203 ? 27.559  -11.881 75.584  1.00 27.91 ? 195  THR C N   1 
ATOM   11116 C  CA  . THR C 1 203 ? 27.150  -12.573 74.365  1.00 25.28 ? 195  THR C CA  1 
ATOM   11117 C  C   . THR C 1 203 ? 26.093  -11.789 73.590  1.00 21.11 ? 195  THR C C   1 
ATOM   11118 O  O   . THR C 1 203 ? 25.367  -12.377 72.778  1.00 24.03 ? 195  THR C O   1 
ATOM   11119 C  CB  . THR C 1 203 ? 26.604  -13.967 74.690  1.00 28.86 ? 195  THR C CB  1 
ATOM   11120 O  OG1 . THR C 1 203 ? 25.460  -13.827 75.538  1.00 24.46 ? 195  THR C OG1 1 
ATOM   11121 C  CG2 . THR C 1 203 ? 27.651  -14.828 75.389  1.00 23.08 ? 195  THR C CG2 1 
ATOM   11122 N  N   . GLU C 1 204 ? 25.977  -10.487 73.836  1.00 20.15 ? 196  GLU C N   1 
ATOM   11123 C  CA  . GLU C 1 204 ? 24.946  -9.685  73.190  1.00 19.43 ? 196  GLU C CA  1 
ATOM   11124 C  C   . GLU C 1 204 ? 25.177  -9.632  71.686  1.00 23.24 ? 196  GLU C C   1 
ATOM   11125 O  O   . GLU C 1 204 ? 26.312  -9.496  71.218  1.00 18.52 ? 196  GLU C O   1 
ATOM   11126 C  CB  . GLU C 1 204 ? 24.935  -8.262  73.745  1.00 19.70 ? 196  GLU C CB  1 
ATOM   11127 C  CG  . GLU C 1 204 ? 24.615  -8.132  75.236  1.00 20.45 ? 196  GLU C CG  1 
ATOM   11128 C  CD  . GLU C 1 204 ? 24.664  -6.692  75.702  1.00 21.12 ? 196  GLU C CD  1 
ATOM   11129 O  OE1 . GLU C 1 204 ? 24.575  -5.790  74.840  1.00 18.19 ? 196  GLU C OE1 1 
ATOM   11130 O  OE2 . GLU C 1 204 ? 24.806  -6.459  76.927  1.00 22.25 ? 196  GLU C OE2 1 
ATOM   11131 N  N   . ASN C 1 205 ? 24.092  -9.749  70.929  1.00 16.39 ? 197  ASN C N   1 
ATOM   11132 C  CA  . ASN C 1 205 ? 24.117  -9.483  69.490  1.00 16.21 ? 197  ASN C CA  1 
ATOM   11133 C  C   . ASN C 1 205 ? 24.044  -7.967  69.319  1.00 22.26 ? 197  ASN C C   1 
ATOM   11134 O  O   . ASN C 1 205 ? 22.964  -7.368  69.322  1.00 14.45 ? 197  ASN C O   1 
ATOM   11135 C  CB  . ASN C 1 205 ? 22.967  -10.212 68.802  1.00 16.89 ? 197  ASN C CB  1 
ATOM   11136 C  CG  . ASN C 1 205 ? 22.936  -9.990  67.300  1.00 16.92 ? 197  ASN C CG  1 
ATOM   11137 O  OD1 . ASN C 1 205 ? 23.476  -9.013  66.783  1.00 16.18 ? 197  ASN C OD1 1 
ATOM   11138 N  ND2 . ASN C 1 205 ? 22.284  -10.899 66.594  1.00 21.00 ? 197  ASN C ND2 1 
ATOM   11139 N  N   . ILE C 1 206 ? 25.209  -7.331  69.185  1.00 16.71 ? 198  ILE C N   1 
ATOM   11140 C  CA  . ILE C 1 206 ? 25.294  -5.867  69.239  1.00 16.41 ? 198  ILE C CA  1 
ATOM   11141 C  C   . ILE C 1 206 ? 24.583  -5.230  68.039  1.00 15.29 ? 198  ILE C C   1 
ATOM   11142 O  O   . ILE C 1 206 ? 23.827  -4.257  68.221  1.00 14.36 ? 198  ILE C O   1 
ATOM   11143 C  CB  . ILE C 1 206 ? 26.763  -5.407  69.363  1.00 17.39 ? 198  ILE C CB  1 
ATOM   11144 C  CG1 . ILE C 1 206 ? 27.326  -5.745  70.751  1.00 18.93 ? 198  ILE C CG1 1 
ATOM   11145 C  CG2 . ILE C 1 206 ? 26.906  -3.915  69.114  1.00 13.01 ? 198  ILE C CG2 1 
ATOM   11146 C  CD1 . ILE C 1 206 ? 26.593  -5.092  71.919  1.00 22.52 ? 198  ILE C CD1 1 
ATOM   11147 N  N   . PRO C 1 207 ? 24.748  -5.729  66.809  1.00 13.69 ? 199  PRO C N   1 
ATOM   11148 C  CA  . PRO C 1 207 ? 23.949  -5.165  65.709  1.00 14.45 ? 199  PRO C CA  1 
ATOM   11149 C  C   . PRO C 1 207 ? 22.447  -5.188  65.974  1.00 17.99 ? 199  PRO C C   1 
ATOM   11150 O  O   . PRO C 1 207 ? 21.757  -4.190  65.735  1.00 15.93 ? 199  PRO C O   1 
ATOM   11151 C  CB  . PRO C 1 207 ? 24.333  -6.063  64.526  1.00 15.91 ? 199  PRO C CB  1 
ATOM   11152 C  CG  . PRO C 1 207 ? 25.750  -6.416  64.818  1.00 14.96 ? 199  PRO C CG  1 
ATOM   11153 C  CD  . PRO C 1 207 ? 25.775  -6.664  66.297  1.00 16.74 ? 199  PRO C CD  1 
ATOM   11154 N  N   . GLN C 1 208 ? 21.931  -6.303  66.495  1.00 16.77 ? 200  GLN C N   1 
ATOM   11155 C  CA  . GLN C 1 208 ? 20.502  -6.397  66.761  1.00 16.28 ? 200  GLN C CA  1 
ATOM   11156 C  C   . GLN C 1 208 ? 20.085  -5.450  67.880  1.00 18.32 ? 200  GLN C C   1 
ATOM   11157 O  O   . GLN C 1 208 ? 19.028  -4.809  67.796  1.00 16.41 ? 200  GLN C O   1 
ATOM   11158 C  CB  . GLN C 1 208 ? 20.140  -7.836  67.106  1.00 15.76 ? 200  GLN C CB  1 
ATOM   11159 C  CG  . GLN C 1 208 ? 18.656  -8.125  67.126  1.00 17.17 ? 200  GLN C CG  1 
ATOM   11160 C  CD  . GLN C 1 208 ? 18.364  -9.592  67.362  1.00 21.84 ? 200  GLN C CD  1 
ATOM   11161 O  OE1 . GLN C 1 208 ? 19.065  -10.260 68.126  1.00 25.06 ? 200  GLN C OE1 1 
ATOM   11162 N  NE2 . GLN C 1 208 ? 17.336  -10.113 66.688  1.00 20.05 ? 200  GLN C NE2 1 
ATOM   11163 N  N   . ARG C 1 209 ? 20.901  -5.346  68.935  1.00 13.18 ? 201  ARG C N   1 
ATOM   11164 C  CA  . ARG C 1 209 ? 20.581  -4.432  70.027  1.00 12.48 ? 201  ARG C CA  1 
ATOM   11165 C  C   . ARG C 1 209 ? 20.502  -2.998  69.534  1.00 17.21 ? 201  ARG C C   1 
ATOM   11166 O  O   . ARG C 1 209 ? 19.592  -2.245  69.912  1.00 13.70 ? 201  ARG C O   1 
ATOM   11167 C  CB  . ARG C 1 209 ? 21.626  -4.567  71.143  1.00 16.22 ? 201  ARG C CB  1 
ATOM   11168 C  CG  . ARG C 1 209 ? 21.646  -3.420  72.125  1.00 16.57 ? 201  ARG C CG  1 
ATOM   11169 C  CD  . ARG C 1 209 ? 22.662  -3.643  73.277  1.00 18.59 ? 201  ARG C CD  1 
ATOM   11170 N  NE  . ARG C 1 209 ? 22.828  -2.409  74.039  1.00 16.05 ? 201  ARG C NE  1 
ATOM   11171 C  CZ  . ARG C 1 209 ? 23.910  -2.087  74.734  1.00 17.62 ? 201  ARG C CZ  1 
ATOM   11172 N  NH1 . ARG C 1 209 ? 24.959  -2.920  74.769  1.00 13.44 ? 201  ARG C NH1 1 
ATOM   11173 N  NH2 . ARG C 1 209 ? 23.950  -0.920  75.380  1.00 15.84 ? 201  ARG C NH2 1 
ATOM   11174 N  N   . PHE C 1 210 ? 21.440  -2.599  68.677  1.00 15.24 ? 202  PHE C N   1 
ATOM   11175 C  CA  . PHE C 1 210 ? 21.440  -1.215  68.229  1.00 17.34 ? 202  PHE C CA  1 
ATOM   11176 C  C   . PHE C 1 210 ? 20.371  -0.963  67.172  1.00 17.32 ? 202  PHE C C   1 
ATOM   11177 O  O   . PHE C 1 210 ? 19.810  0.137   67.128  1.00 18.44 ? 202  PHE C O   1 
ATOM   11178 C  CB  . PHE C 1 210 ? 22.858  -0.821  67.791  1.00 10.83 ? 202  PHE C CB  1 
ATOM   11179 C  CG  . PHE C 1 210 ? 23.688  -0.341  68.957  1.00 10.38 ? 202  PHE C CG  1 
ATOM   11180 C  CD1 . PHE C 1 210 ? 24.117  -1.242  69.930  1.00 14.80 ? 202  PHE C CD1 1 
ATOM   11181 C  CD2 . PHE C 1 210 ? 23.950  1.005   69.141  1.00 11.72 ? 202  PHE C CD2 1 
ATOM   11182 C  CE1 . PHE C 1 210 ? 24.834  -0.813  71.054  1.00 14.87 ? 202  PHE C CE1 1 
ATOM   11183 C  CE2 . PHE C 1 210 ? 24.668  1.445   70.268  1.00 10.66 ? 202  PHE C CE2 1 
ATOM   11184 C  CZ  . PHE C 1 210 ? 25.105  0.531   71.221  1.00 13.50 ? 202  PHE C CZ  1 
ATOM   11185 N  N   . GLU C 1 211 ? 20.019  -1.972  66.369  1.00 15.79 ? 203  GLU C N   1 
ATOM   11186 C  CA  . GLU C 1 211 ? 18.810  -1.853  65.557  1.00 16.51 ? 203  GLU C CA  1 
ATOM   11187 C  C   . GLU C 1 211 ? 17.581  -1.608  66.430  1.00 18.72 ? 203  GLU C C   1 
ATOM   11188 O  O   . GLU C 1 211 ? 16.716  -0.792  66.087  1.00 14.60 ? 203  GLU C O   1 
ATOM   11189 C  CB  . GLU C 1 211 ? 18.626  -3.102  64.696  1.00 18.15 ? 203  GLU C CB  1 
ATOM   11190 C  CG  . GLU C 1 211 ? 19.670  -3.193  63.592  1.00 31.02 ? 203  GLU C CG  1 
ATOM   11191 C  CD  . GLU C 1 211 ? 19.432  -4.352  62.647  1.00 37.10 ? 203  GLU C CD  1 
ATOM   11192 O  OE1 . GLU C 1 211 ? 18.259  -4.631  62.337  1.00 32.90 ? 203  GLU C OE1 1 
ATOM   11193 O  OE2 . GLU C 1 211 ? 20.426  -4.981  62.223  1.00 42.22 ? 203  GLU C OE2 1 
ATOM   11194 N  N   . SER C 1 212 ? 17.501  -2.282  67.578  1.00 14.33 ? 204  SER C N   1 
ATOM   11195 C  CA  . SER C 1 212 ? 16.357  -2.096  68.460  1.00 12.47 ? 204  SER C CA  1 
ATOM   11196 C  C   . SER C 1 212 ? 16.291  -0.681  69.023  1.00 15.74 ? 204  SER C C   1 
ATOM   11197 O  O   . SER C 1 212 ? 15.209  -0.235  69.409  1.00 14.22 ? 204  SER C O   1 
ATOM   11198 C  CB  . SER C 1 212 ? 16.390  -3.135  69.586  1.00 16.75 ? 204  SER C CB  1 
ATOM   11199 O  OG  . SER C 1 212 ? 17.117  -2.672  70.720  1.00 13.95 ? 204  SER C OG  1 
ATOM   11200 N  N   . TYR C 1 213 ? 17.417  0.044   69.064  1.00 13.61 ? 205  TYR C N   1 
ATOM   11201 C  CA  . TYR C 1 213 ? 17.403  1.450   69.460  1.00 13.21 ? 205  TYR C CA  1 
ATOM   11202 C  C   . TYR C 1 213 ? 17.055  2.392   68.317  1.00 17.54 ? 205  TYR C C   1 
ATOM   11203 O  O   . TYR C 1 213 ? 16.956  3.602   68.550  1.00 16.34 ? 205  TYR C O   1 
ATOM   11204 C  CB  . TYR C 1 213 ? 18.768  1.902   69.984  1.00 15.90 ? 205  TYR C CB  1 
ATOM   11205 C  CG  . TYR C 1 213 ? 19.284  1.203   71.211  1.00 14.34 ? 205  TYR C CG  1 
ATOM   11206 C  CD1 . TYR C 1 213 ? 18.426  0.756   72.203  1.00 16.62 ? 205  TYR C CD1 1 
ATOM   11207 C  CD2 . TYR C 1 213 ? 20.644  1.021   71.388  1.00 16.17 ? 205  TYR C CD2 1 
ATOM   11208 C  CE1 . TYR C 1 213 ? 18.912  0.123   73.334  1.00 16.70 ? 205  TYR C CE1 1 
ATOM   11209 C  CE2 . TYR C 1 213 ? 21.140  0.403   72.515  1.00 14.62 ? 205  TYR C CE2 1 
ATOM   11210 C  CZ  . TYR C 1 213 ? 20.275  -0.046  73.486  1.00 14.27 ? 205  TYR C CZ  1 
ATOM   11211 O  OH  . TYR C 1 213 ? 20.777  -0.674  74.608  1.00 14.12 ? 205  TYR C OH  1 
ATOM   11212 N  N   . GLY C 1 214 ? 16.921  1.884   67.097  1.00 17.62 ? 206  GLY C N   1 
ATOM   11213 C  CA  . GLY C 1 214 ? 16.731  2.740   65.945  1.00 14.90 ? 206  GLY C CA  1 
ATOM   11214 C  C   . GLY C 1 214 ? 18.013  3.254   65.332  1.00 16.45 ? 206  GLY C C   1 
ATOM   11215 O  O   . GLY C 1 214 ? 17.972  4.241   64.590  1.00 16.70 ? 206  GLY C O   1 
ATOM   11216 N  N   . TRP C 1 215 ? 19.154  2.627   65.624  1.00 11.58 ? 207  TRP C N   1 
ATOM   11217 C  CA  . TRP C 1 215 ? 20.422  3.023   65.025  1.00 13.31 ? 207  TRP C CA  1 
ATOM   11218 C  C   . TRP C 1 215 ? 20.625  2.365   63.661  1.00 13.10 ? 207  TRP C C   1 
ATOM   11219 O  O   . TRP C 1 215 ? 20.020  1.335   63.336  1.00 14.36 ? 207  TRP C O   1 
ATOM   11220 C  CB  . TRP C 1 215 ? 21.599  2.633   65.922  1.00 11.68 ? 207  TRP C CB  1 
ATOM   11221 C  CG  . TRP C 1 215 ? 21.820  3.494   67.108  1.00 12.19 ? 207  TRP C CG  1 
ATOM   11222 C  CD1 . TRP C 1 215 ? 20.895  3.865   68.056  1.00 14.47 ? 207  TRP C CD1 1 
ATOM   11223 C  CD2 . TRP C 1 215 ? 23.075  4.034   67.536  1.00 12.21 ? 207  TRP C CD2 1 
ATOM   11224 N  NE1 . TRP C 1 215 ? 21.504  4.635   69.026  1.00 12.85 ? 207  TRP C NE1 1 
ATOM   11225 C  CE2 . TRP C 1 215 ? 22.837  4.753   68.731  1.00 13.26 ? 207  TRP C CE2 1 
ATOM   11226 C  CE3 . TRP C 1 215 ? 24.371  3.998   67.014  1.00 11.40 ? 207  TRP C CE3 1 
ATOM   11227 C  CZ2 . TRP C 1 215 ? 23.851  5.433   69.410  1.00 12.46 ? 207  TRP C CZ2 1 
ATOM   11228 C  CZ3 . TRP C 1 215 ? 25.381  4.675   67.683  1.00 13.19 ? 207  TRP C CZ3 1 
ATOM   11229 C  CH2 . TRP C 1 215 ? 25.114  5.384   68.873  1.00 11.49 ? 207  TRP C CH2 1 
ATOM   11230 N  N   . HIS C 1 216 ? 21.476  3.006   62.853  1.00 13.78 ? 208  HIS C N   1 
ATOM   11231 C  CA  . HIS C 1 216 ? 22.059  2.401   61.659  1.00 15.25 ? 208  HIS C CA  1 
ATOM   11232 C  C   . HIS C 1 216 ? 23.278  1.587   62.080  1.00 15.81 ? 208  HIS C C   1 
ATOM   11233 O  O   . HIS C 1 216 ? 24.055  2.017   62.939  1.00 13.64 ? 208  HIS C O   1 
ATOM   11234 C  CB  . HIS C 1 216 ? 22.453  3.498   60.665  1.00 15.35 ? 208  HIS C CB  1 
ATOM   11235 C  CG  . HIS C 1 216 ? 23.374  3.050   59.567  1.00 15.47 ? 208  HIS C CG  1 
ATOM   11236 N  ND1 . HIS C 1 216 ? 24.669  3.511   59.447  1.00 16.18 ? 208  HIS C ND1 1 
ATOM   11237 C  CD2 . HIS C 1 216 ? 23.174  2.217   58.517  1.00 20.11 ? 208  HIS C CD2 1 
ATOM   11238 C  CE1 . HIS C 1 216 ? 25.235  2.959   58.386  1.00 20.71 ? 208  HIS C CE1 1 
ATOM   11239 N  NE2 . HIS C 1 216 ? 24.350  2.172   57.803  1.00 19.34 ? 208  HIS C NE2 1 
ATOM   11240 N  N   . VAL C 1 217 ? 23.414  0.387   61.523  1.00 17.75 ? 209  VAL C N   1 
ATOM   11241 C  CA  . VAL C 1 217 ? 24.458  -0.544  61.943  1.00 14.32 ? 209  VAL C CA  1 
ATOM   11242 C  C   . VAL C 1 217 ? 25.230  -1.023  60.723  1.00 17.84 ? 209  VAL C C   1 
ATOM   11243 O  O   . VAL C 1 217 ? 24.629  -1.474  59.740  1.00 15.33 ? 209  VAL C O   1 
ATOM   11244 C  CB  . VAL C 1 217 ? 23.875  -1.753  62.704  1.00 14.52 ? 209  VAL C CB  1 
ATOM   11245 C  CG1 . VAL C 1 217 ? 25.000  -2.719  63.106  1.00 17.92 ? 209  VAL C CG1 1 
ATOM   11246 C  CG2 . VAL C 1 217 ? 23.087  -1.295  63.926  1.00 14.29 ? 209  VAL C CG2 1 
ATOM   11247 N  N   . VAL C 1 218 ? 26.558  -0.945  60.792  1.00 13.13 ? 210  VAL C N   1 
ATOM   11248 C  CA  . VAL C 1 218 ? 27.406  -1.637  59.824  1.00 15.47 ? 210  VAL C CA  1 
ATOM   11249 C  C   . VAL C 1 218 ? 28.052  -2.806  60.561  1.00 15.43 ? 210  VAL C C   1 
ATOM   11250 O  O   . VAL C 1 218 ? 28.977  -2.597  61.360  1.00 17.65 ? 210  VAL C O   1 
ATOM   11251 C  CB  . VAL C 1 218 ? 28.461  -0.701  59.211  1.00 15.26 ? 210  VAL C CB  1 
ATOM   11252 C  CG1 . VAL C 1 218 ? 29.165  -1.384  58.023  1.00 15.85 ? 210  VAL C CG1 1 
ATOM   11253 C  CG2 . VAL C 1 218 ? 27.824  0.617   58.788  1.00 14.38 ? 210  VAL C CG2 1 
ATOM   11254 N  N   . PRO C 1 219 ? 27.578  -4.030  60.364  1.00 16.31 ? 211  PRO C N   1 
ATOM   11255 C  CA  . PRO C 1 219 ? 28.105  -5.170  61.117  1.00 19.17 ? 211  PRO C CA  1 
ATOM   11256 C  C   . PRO C 1 219 ? 29.331  -5.786  60.457  1.00 18.60 ? 211  PRO C C   1 
ATOM   11257 O  O   . PRO C 1 219 ? 29.583  -5.618  59.266  1.00 21.64 ? 211  PRO C O   1 
ATOM   11258 C  CB  . PRO C 1 219 ? 26.935  -6.160  61.089  1.00 19.46 ? 211  PRO C CB  1 
ATOM   11259 C  CG  . PRO C 1 219 ? 26.306  -5.904  59.735  1.00 20.88 ? 211  PRO C CG  1 
ATOM   11260 C  CD  . PRO C 1 219 ? 26.462  -4.418  59.479  1.00 15.51 ? 211  PRO C CD  1 
ATOM   11261 N  N   . ASN C 1 220 ? 30.103  -6.505  61.273  1.00 21.39 ? 212  ASN C N   1 
ATOM   11262 C  CA  . ASN C 1 220 ? 31.115  -7.438  60.775  1.00 24.18 ? 212  ASN C CA  1 
ATOM   11263 C  C   . ASN C 1 220 ? 32.116  -6.770  59.822  1.00 23.84 ? 212  ASN C C   1 
ATOM   11264 O  O   . ASN C 1 220 ? 32.433  -7.295  58.752  1.00 22.20 ? 212  ASN C O   1 
ATOM   11265 C  CB  . ASN C 1 220 ? 30.433  -8.635  60.099  1.00 27.93 ? 212  ASN C CB  1 
ATOM   11266 C  CG  . ASN C 1 220 ? 31.368  -9.792  59.903  1.00 34.82 ? 212  ASN C CG  1 
ATOM   11267 O  OD1 . ASN C 1 220 ? 32.220  -10.062 60.752  1.00 37.93 ? 212  ASN C OD1 1 
ATOM   11268 N  ND2 . ASN C 1 220 ? 31.233  -10.482 58.773  1.00 34.64 ? 212  ASN C ND2 1 
ATOM   11269 N  N   . VAL C 1 221 ? 32.620  -5.602  60.220  1.00 17.62 ? 213  VAL C N   1 
ATOM   11270 C  CA  . VAL C 1 221 ? 33.670  -4.911  59.471  1.00 18.68 ? 213  VAL C CA  1 
ATOM   11271 C  C   . VAL C 1 221 ? 35.025  -5.468  59.894  1.00 17.45 ? 213  VAL C C   1 
ATOM   11272 O  O   . VAL C 1 221 ? 35.298  -5.619  61.088  1.00 21.73 ? 213  VAL C O   1 
ATOM   11273 C  CB  . VAL C 1 221 ? 33.610  -3.390  59.704  1.00 21.47 ? 213  VAL C CB  1 
ATOM   11274 C  CG1 . VAL C 1 221 ? 34.741  -2.674  58.951  1.00 19.40 ? 213  VAL C CG1 1 
ATOM   11275 C  CG2 . VAL C 1 221 ? 32.249  -2.838  59.302  1.00 21.05 ? 213  VAL C CG2 1 
ATOM   11276 N  N   . ASN C 1 222 ? 35.864  -5.790  58.913  1.00 22.26 ? 214  ASN C N   1 
ATOM   11277 C  CA  . ASN C 1 222 ? 37.252  -6.146  59.163  1.00 20.20 ? 214  ASN C CA  1 
ATOM   11278 C  C   . ASN C 1 222 ? 37.954  -4.967  59.826  1.00 19.72 ? 214  ASN C C   1 
ATOM   11279 O  O   . ASN C 1 222 ? 38.253  -3.967  59.170  1.00 18.04 ? 214  ASN C O   1 
ATOM   11280 C  CB  . ASN C 1 222 ? 37.935  -6.547  57.845  1.00 22.56 ? 214  ASN C CB  1 
ATOM   11281 C  CG  . ASN C 1 222 ? 39.381  -6.991  58.029  1.00 26.76 ? 214  ASN C CG  1 
ATOM   11282 O  OD1 . ASN C 1 222 ? 40.038  -6.647  59.011  1.00 30.91 ? 214  ASN C OD1 1 
ATOM   11283 N  ND2 . ASN C 1 222 ? 39.888  -7.750  57.062  1.00 28.99 ? 214  ASN C ND2 1 
ATOM   11284 N  N   . GLY C 1 223 ? 38.227  -5.073  61.126  1.00 20.53 ? 215  GLY C N   1 
ATOM   11285 C  CA  . GLY C 1 223 ? 38.766  -3.951  61.876  1.00 21.04 ? 215  GLY C CA  1 
ATOM   11286 C  C   . GLY C 1 223 ? 40.215  -3.603  61.613  1.00 19.62 ? 215  GLY C C   1 
ATOM   11287 O  O   . GLY C 1 223 ? 40.708  -2.630  62.196  1.00 23.81 ? 215  GLY C O   1 
ATOM   11288 N  N   . HIS C 1 224 ? 40.911  -4.353  60.754  1.00 19.48 ? 216  HIS C N   1 
ATOM   11289 C  CA  . HIS C 1 224 ? 42.263  -4.010  60.331  1.00 21.98 ? 216  HIS C CA  1 
ATOM   11290 C  C   . HIS C 1 224 ? 42.350  -3.747  58.832  1.00 26.26 ? 216  HIS C C   1 
ATOM   11291 O  O   . HIS C 1 224 ? 43.456  -3.701  58.277  1.00 25.59 ? 216  HIS C O   1 
ATOM   11292 C  CB  . HIS C 1 224 ? 43.249  -5.114  60.741  1.00 25.27 ? 216  HIS C CB  1 
ATOM   11293 C  CG  . HIS C 1 224 ? 43.248  -5.396  62.213  1.00 24.30 ? 216  HIS C CG  1 
ATOM   11294 N  ND1 . HIS C 1 224 ? 43.549  -4.434  63.153  1.00 27.23 ? 216  HIS C ND1 1 
ATOM   11295 C  CD2 . HIS C 1 224 ? 42.957  -6.521  62.907  1.00 27.94 ? 216  HIS C CD2 1 
ATOM   11296 C  CE1 . HIS C 1 224 ? 43.450  -4.956  64.362  1.00 28.12 ? 216  HIS C CE1 1 
ATOM   11297 N  NE2 . HIS C 1 224 ? 43.099  -6.223  64.240  1.00 28.80 ? 216  HIS C NE2 1 
ATOM   11298 N  N   . ASP C 1 225 ? 41.216  -3.574  58.163  1.00 26.85 ? 217  ASP C N   1 
ATOM   11299 C  CA  . ASP C 1 225 ? 41.158  -3.291  56.730  1.00 27.16 ? 217  ASP C CA  1 
ATOM   11300 C  C   . ASP C 1 225 ? 40.717  -1.838  56.613  1.00 28.62 ? 217  ASP C C   1 
ATOM   11301 O  O   . ASP C 1 225 ? 39.531  -1.533  56.769  1.00 18.22 ? 217  ASP C O   1 
ATOM   11302 C  CB  . ASP C 1 225 ? 40.191  -4.249  56.028  1.00 24.55 ? 217  ASP C CB  1 
ATOM   11303 C  CG  . ASP C 1 225 ? 40.099  -4.025  54.512  1.00 26.20 ? 217  ASP C CG  1 
ATOM   11304 O  OD1 . ASP C 1 225 ? 40.382  -2.918  54.012  1.00 25.52 ? 217  ASP C OD1 1 
ATOM   11305 O  OD2 . ASP C 1 225 ? 39.719  -4.981  53.807  1.00 36.56 ? 217  ASP C OD2 1 
ATOM   11306 N  N   . THR C 1 226 ? 41.670  -0.939  56.333  1.00 19.21 ? 218  THR C N   1 
ATOM   11307 C  CA  . THR C 1 226 ? 41.331  0.483   56.307  1.00 24.38 ? 218  THR C CA  1 
ATOM   11308 C  C   . THR C 1 226 ? 40.322  0.807   55.208  1.00 20.67 ? 218  THR C C   1 
ATOM   11309 O  O   . THR C 1 226 ? 39.506  1.723   55.370  1.00 18.63 ? 218  THR C O   1 
ATOM   11310 C  CB  . THR C 1 226 ? 42.590  1.333   56.136  1.00 18.83 ? 218  THR C CB  1 
ATOM   11311 O  OG1 . THR C 1 226 ? 43.256  0.956   54.929  1.00 23.25 ? 218  THR C OG1 1 
ATOM   11312 C  CG2 . THR C 1 226 ? 43.527  1.134   57.313  1.00 31.84 ? 218  THR C CG2 1 
ATOM   11313 N  N   . ALA C 1 227 ? 40.366  0.087   54.086  1.00 19.23 ? 219  ALA C N   1 
ATOM   11314 C  CA  . ALA C 1 227 ? 39.357  0.290   53.046  1.00 22.24 ? 219  ALA C CA  1 
ATOM   11315 C  C   . ALA C 1 227 ? 37.973  -0.109  53.541  1.00 21.26 ? 219  ALA C C   1 
ATOM   11316 O  O   . ALA C 1 227 ? 36.985  0.603   53.299  1.00 19.23 ? 219  ALA C O   1 
ATOM   11317 C  CB  . ALA C 1 227 ? 39.720  -0.504  51.797  1.00 20.63 ? 219  ALA C CB  1 
ATOM   11318 N  N   . ALA C 1 228 ? 37.882  -1.236  54.248  1.00 18.71 ? 220  ALA C N   1 
ATOM   11319 C  CA  . ALA C 1 228 ? 36.593  -1.662  54.787  1.00 18.44 ? 220  ALA C CA  1 
ATOM   11320 C  C   . ALA C 1 228 ? 36.081  -0.680  55.827  1.00 19.53 ? 220  ALA C C   1 
ATOM   11321 O  O   . ALA C 1 228 ? 34.886  -0.358  55.856  1.00 16.46 ? 220  ALA C O   1 
ATOM   11322 C  CB  . ALA C 1 228 ? 36.708  -3.062  55.389  1.00 19.92 ? 220  ALA C CB  1 
ATOM   11323 N  N   . ILE C 1 229 ? 36.970  -0.191  56.696  1.00 18.03 ? 221  ILE C N   1 
ATOM   11324 C  CA  . ILE C 1 229 ? 36.547  0.796   57.680  1.00 15.89 ? 221  ILE C CA  1 
ATOM   11325 C  C   . ILE C 1 229 ? 36.092  2.072   56.989  1.00 15.32 ? 221  ILE C C   1 
ATOM   11326 O  O   . ILE C 1 229 ? 35.095  2.698   57.393  1.00 14.65 ? 221  ILE C O   1 
ATOM   11327 C  CB  . ILE C 1 229 ? 37.679  1.067   58.687  1.00 15.44 ? 221  ILE C CB  1 
ATOM   11328 C  CG1 . ILE C 1 229 ? 38.049  -0.231  59.413  1.00 18.31 ? 221  ILE C CG1 1 
ATOM   11329 C  CG2 . ILE C 1 229 ? 37.252  2.160   59.679  1.00 17.09 ? 221  ILE C CG2 1 
ATOM   11330 C  CD1 . ILE C 1 229 ? 39.426  -0.190  60.124  1.00 17.61 ? 221  ILE C CD1 1 
ATOM   11331 N  N   . GLN C 1 230 ? 36.805  2.476   55.938  1.00 15.99 ? 222  GLN C N   1 
ATOM   11332 C  CA  . GLN C 1 230 ? 36.468  3.718   55.256  1.00 15.97 ? 222  GLN C CA  1 
ATOM   11333 C  C   . GLN C 1 230 ? 35.074  3.657   54.634  1.00 16.02 ? 222  GLN C C   1 
ATOM   11334 O  O   . GLN C 1 230 ? 34.302  4.614   54.740  1.00 17.01 ? 222  GLN C O   1 
ATOM   11335 C  CB  . GLN C 1 230 ? 37.519  4.048   54.197  1.00 16.87 ? 222  GLN C CB  1 
ATOM   11336 C  CG  . GLN C 1 230 ? 37.179  5.324   53.449  1.00 28.33 ? 222  GLN C CG  1 
ATOM   11337 C  CD  . GLN C 1 230 ? 38.374  5.996   52.812  1.00 30.54 ? 222  GLN C CD  1 
ATOM   11338 O  OE1 . GLN C 1 230 ? 39.489  5.482   52.855  1.00 30.93 ? 222  GLN C OE1 1 
ATOM   11339 N  NE2 . GLN C 1 230 ? 38.145  7.164   52.223  1.00 27.37 ? 222  GLN C NE2 1 
ATOM   11340 N  N   . THR C 1 231 ? 34.739  2.550   53.960  1.00 16.73 ? 223  THR C N   1 
ATOM   11341 C  CA  . THR C 1 231 ? 33.425  2.475   53.318  1.00 16.88 ? 223  THR C CA  1 
ATOM   11342 C  C   . THR C 1 231 ? 32.312  2.354   54.354  1.00 18.24 ? 223  THR C C   1 
ATOM   11343 O  O   . THR C 1 231 ? 31.193  2.827   54.121  1.00 16.00 ? 223  THR C O   1 
ATOM   11344 C  CB  . THR C 1 231 ? 33.373  1.316   52.307  1.00 22.01 ? 223  THR C CB  1 
ATOM   11345 O  OG1 . THR C 1 231 ? 33.531  0.063   52.977  1.00 27.72 ? 223  THR C OG1 1 
ATOM   11346 C  CG2 . THR C 1 231 ? 34.486  1.455   51.284  1.00 21.86 ? 223  THR C CG2 1 
ATOM   11347 N  N   . ALA C 1 232 ? 32.612  1.764   55.512  1.00 16.45 ? 224  ALA C N   1 
ATOM   11348 C  CA  . ALA C 1 232 ? 31.659  1.749   56.619  1.00 16.24 ? 224  ALA C CA  1 
ATOM   11349 C  C   . ALA C 1 232 ? 31.376  3.152   57.139  1.00 19.25 ? 224  ALA C C   1 
ATOM   11350 O  O   . ALA C 1 232 ? 30.221  3.488   57.441  1.00 14.73 ? 224  ALA C O   1 
ATOM   11351 C  CB  . ALA C 1 232 ? 32.186  0.870   57.752  1.00 14.39 ? 224  ALA C CB  1 
ATOM   11352 N  N   . ILE C 1 233 ? 32.418  3.975   57.281  1.00 13.87 ? 225  ILE C N   1 
ATOM   11353 C  CA  . ILE C 1 233 ? 32.218  5.343   57.748  1.00 17.82 ? 225  ILE C CA  1 
ATOM   11354 C  C   . ILE C 1 233 ? 31.461  6.157   56.703  1.00 15.52 ? 225  ILE C C   1 
ATOM   11355 O  O   . ILE C 1 233 ? 30.591  6.970   57.045  1.00 13.55 ? 225  ILE C O   1 
ATOM   11356 C  CB  . ILE C 1 233 ? 33.573  5.989   58.103  1.00 19.91 ? 225  ILE C CB  1 
ATOM   11357 C  CG1 . ILE C 1 233 ? 34.198  5.309   59.335  1.00 18.67 ? 225  ILE C CG1 1 
ATOM   11358 C  CG2 . ILE C 1 233 ? 33.413  7.493   58.324  1.00 18.58 ? 225  ILE C CG2 1 
ATOM   11359 C  CD1 . ILE C 1 233 ? 35.595  5.829   59.647  1.00 14.10 ? 225  ILE C CD1 1 
ATOM   11360 N  N   . GLU C 1 234 ? 31.780  5.951   55.417  1.00 18.03 ? 226  GLU C N   1 
ATOM   11361 C  CA  . GLU C 1 234 ? 31.015  6.582   54.339  1.00 16.37 ? 226  GLU C CA  1 
ATOM   11362 C  C   . GLU C 1 234 ? 29.539  6.250   54.456  1.00 15.32 ? 226  GLU C C   1 
ATOM   11363 O  O   . GLU C 1 234 ? 28.677  7.126   54.290  1.00 18.52 ? 226  GLU C O   1 
ATOM   11364 C  CB  . GLU C 1 234 ? 31.531  6.123   52.973  1.00 18.13 ? 226  GLU C CB  1 
ATOM   11365 C  CG  . GLU C 1 234 ? 32.949  6.555   52.646  1.00 17.06 ? 226  GLU C CG  1 
ATOM   11366 C  CD  . GLU C 1 234 ? 33.510  5.839   51.424  1.00 17.83 ? 226  GLU C CD  1 
ATOM   11367 O  OE1 . GLU C 1 234 ? 32.851  4.916   50.877  1.00 23.44 ? 226  GLU C OE1 1 
ATOM   11368 O  OE2 . GLU C 1 234 ? 34.609  6.210   51.010  1.00 27.13 ? 226  GLU C OE2 1 
ATOM   11369 N  N   . ALA C 1 235 ? 29.226  4.982   54.720  1.00 16.56 ? 227  ALA C N   1 
ATOM   11370 C  CA  . ALA C 1 235 ? 27.829  4.580   54.836  1.00 18.51 ? 227  ALA C CA  1 
ATOM   11371 C  C   . ALA C 1 235 ? 27.183  5.204   56.062  1.00 17.12 ? 227  ALA C C   1 
ATOM   11372 O  O   . ALA C 1 235 ? 26.017  5.625   56.012  1.00 14.52 ? 227  ALA C O   1 
ATOM   11373 C  CB  . ALA C 1 235 ? 27.721  3.057   54.879  1.00 15.45 ? 227  ALA C CB  1 
ATOM   11374 N  N   . ALA C 1 236 ? 27.925  5.278   57.172  1.00 16.58 ? 228  ALA C N   1 
ATOM   11375 C  CA  . ALA C 1 236 ? 27.394  5.915   58.371  1.00 12.80 ? 228  ALA C CA  1 
ATOM   11376 C  C   . ALA C 1 236 ? 27.115  7.390   58.127  1.00 16.00 ? 228  ALA C C   1 
ATOM   11377 O  O   . ALA C 1 236 ? 26.074  7.913   58.548  1.00 19.89 ? 228  ALA C O   1 
ATOM   11378 C  CB  . ALA C 1 236 ? 28.372  5.743   59.537  1.00 12.12 ? 228  ALA C CB  1 
ATOM   11379 N  N   . ARG C 1 237 ? 28.041  8.084   57.456  1.00 15.72 ? 229  ARG C N   1 
ATOM   11380 C  CA  . ARG C 1 237 ? 27.840  9.501   57.199  1.00 13.66 ? 229  ARG C CA  1 
ATOM   11381 C  C   . ARG C 1 237 ? 26.644  9.724   56.280  1.00 18.11 ? 229  ARG C C   1 
ATOM   11382 O  O   . ARG C 1 237 ? 25.885  10.681  56.468  1.00 18.80 ? 229  ARG C O   1 
ATOM   11383 C  CB  . ARG C 1 237 ? 29.114  10.109  56.618  1.00 16.80 ? 229  ARG C CB  1 
ATOM   11384 C  CG  . ARG C 1 237 ? 30.251  10.231  57.644  1.00 13.41 ? 229  ARG C CG  1 
ATOM   11385 C  CD  . ARG C 1 237 ? 31.589  10.549  56.986  1.00 15.95 ? 229  ARG C CD  1 
ATOM   11386 N  NE  . ARG C 1 237 ? 31.527  11.741  56.150  1.00 24.60 ? 229  ARG C NE  1 
ATOM   11387 C  CZ  . ARG C 1 237 ? 31.550  12.987  56.612  1.00 25.98 ? 229  ARG C CZ  1 
ATOM   11388 N  NH1 . ARG C 1 237 ? 31.622  13.222  57.917  1.00 24.93 ? 229  ARG C NH1 1 
ATOM   11389 N  NH2 . ARG C 1 237 ? 31.469  14.002  55.766  1.00 23.45 ? 229  ARG C NH2 1 
ATOM   11390 N  N   . ALA C 1 238 ? 26.438  8.835   55.303  1.00 17.70 ? 230  ALA C N   1 
ATOM   11391 C  CA  . ALA C 1 238 ? 25.308  8.992   54.387  1.00 18.51 ? 230  ALA C CA  1 
ATOM   11392 C  C   . ALA C 1 238 ? 23.961  8.846   55.077  1.00 21.91 ? 230  ALA C C   1 
ATOM   11393 O  O   . ALA C 1 238 ? 22.966  9.382   54.574  1.00 20.53 ? 230  ALA C O   1 
ATOM   11394 C  CB  . ALA C 1 238 ? 25.397  7.987   53.240  1.00 16.91 ? 230  ALA C CB  1 
ATOM   11395 N  N   . GLU C 1 239 ? 23.901  8.146   56.211  1.00 20.19 ? 231  GLU C N   1 
ATOM   11396 C  CA  . GLU C 1 239 ? 22.648  7.943   56.940  1.00 22.39 ? 231  GLU C CA  1 
ATOM   11397 C  C   . GLU C 1 239 ? 22.466  9.114   57.899  1.00 21.72 ? 231  GLU C C   1 
ATOM   11398 O  O   . GLU C 1 239 ? 22.977  9.101   59.019  1.00 22.22 ? 231  GLU C O   1 
ATOM   11399 C  CB  . GLU C 1 239 ? 22.654  6.607   57.675  1.00 23.36 ? 231  GLU C CB  1 
ATOM   11400 C  CG  . GLU C 1 239 ? 21.468  6.423   58.621  1.00 30.82 ? 231  GLU C CG  1 
ATOM   11401 C  CD  . GLU C 1 239 ? 20.132  6.622   57.923  1.00 34.33 ? 231  GLU C CD  1 
ATOM   11402 O  OE1 . GLU C 1 239 ? 19.828  5.832   57.005  1.00 34.46 ? 231  GLU C OE1 1 
ATOM   11403 O  OE2 . GLU C 1 239 ? 19.402  7.579   58.273  1.00 30.86 ? 231  GLU C OE2 1 
ATOM   11404 N  N   . THR C 1 240 ? 21.715  10.123  57.468  1.00 20.70 ? 232  THR C N   1 
ATOM   11405 C  CA  . THR C 1 240 ? 21.607  11.357  58.229  1.00 20.22 ? 232  THR C CA  1 
ATOM   11406 C  C   . THR C 1 240 ? 20.480  11.347  59.249  1.00 22.87 ? 232  THR C C   1 
ATOM   11407 O  O   . THR C 1 240 ? 20.370  12.300  60.029  1.00 20.05 ? 232  THR C O   1 
ATOM   11408 C  CB  . THR C 1 240 ? 21.417  12.543  57.280  1.00 26.94 ? 232  THR C CB  1 
ATOM   11409 O  OG1 . THR C 1 240 ? 20.219  12.358  56.515  1.00 24.46 ? 232  THR C OG1 1 
ATOM   11410 C  CG2 . THR C 1 240 ? 22.604  12.652  56.341  1.00 25.79 ? 232  THR C CG2 1 
ATOM   11411 N  N   . GLY C 1 241 ? 19.655  10.303  59.276  1.00 18.75 ? 233  GLY C N   1 
ATOM   11412 C  CA  . GLY C 1 241 ? 18.532  10.281  60.195  1.00 20.15 ? 233  GLY C CA  1 
ATOM   11413 C  C   . GLY C 1 241 ? 18.701  9.406   61.422  1.00 21.90 ? 233  GLY C C   1 
ATOM   11414 O  O   . GLY C 1 241 ? 17.860  9.449   62.322  1.00 18.70 ? 233  GLY C O   1 
ATOM   11415 N  N   . LYS C 1 242 ? 19.775  8.612   61.487  1.00 17.35 ? 234  LYS C N   1 
ATOM   11416 C  CA  . LYS C 1 242 ? 19.980  7.705   62.612  1.00 13.19 ? 234  LYS C CA  1 
ATOM   11417 C  C   . LYS C 1 242 ? 21.442  7.754   63.026  1.00 12.78 ? 234  LYS C C   1 
ATOM   11418 O  O   . LYS C 1 242 ? 22.318  7.889   62.163  1.00 15.53 ? 234  LYS C O   1 
ATOM   11419 C  CB  . LYS C 1 242 ? 19.631  6.252   62.271  1.00 17.74 ? 234  LYS C CB  1 
ATOM   11420 C  CG  . LYS C 1 242 ? 18.305  6.033   61.568  1.00 16.83 ? 234  LYS C CG  1 
ATOM   11421 C  CD  . LYS C 1 242 ? 18.171  4.561   61.191  1.00 13.28 ? 234  LYS C CD  1 
ATOM   11422 C  CE  . LYS C 1 242 ? 16.943  4.292   60.347  1.00 22.25 ? 234  LYS C CE  1 
ATOM   11423 N  NZ  . LYS C 1 242 ? 16.875  2.833   59.988  1.00 26.43 ? 234  LYS C NZ  1 
ATOM   11424 N  N   . PRO C 1 243 ? 21.735  7.651   64.322  1.00 13.19 ? 235  PRO C N   1 
ATOM   11425 C  CA  . PRO C 1 243 ? 23.125  7.447   64.737  1.00 11.87 ? 235  PRO C CA  1 
ATOM   11426 C  C   . PRO C 1 243 ? 23.600  6.095   64.232  1.00 13.40 ? 235  PRO C C   1 
ATOM   11427 O  O   . PRO C 1 243 ? 22.804  5.174   64.040  1.00 12.89 ? 235  PRO C O   1 
ATOM   11428 C  CB  . PRO C 1 243 ? 23.057  7.496   66.271  1.00 9.56  ? 235  PRO C CB  1 
ATOM   11429 C  CG  . PRO C 1 243 ? 21.638  7.133   66.602  1.00 14.42 ? 235  PRO C CG  1 
ATOM   11430 C  CD  . PRO C 1 243 ? 20.797  7.634   65.459  1.00 13.32 ? 235  PRO C CD  1 
ATOM   11431 N  N   . SER C 1 244 ? 24.909  5.985   63.997  1.00 11.38 ? 236  SER C N   1 
ATOM   11432 C  CA  . SER C 1 244 ? 25.490  4.793   63.394  1.00 15.07 ? 236  SER C CA  1 
ATOM   11433 C  C   . SER C 1 244 ? 26.488  4.133   64.335  1.00 12.05 ? 236  SER C C   1 
ATOM   11434 O  O   . SER C 1 244 ? 27.269  4.813   65.009  1.00 13.98 ? 236  SER C O   1 
ATOM   11435 C  CB  . SER C 1 244 ? 26.211  5.118   62.073  1.00 13.77 ? 236  SER C CB  1 
ATOM   11436 O  OG  . SER C 1 244 ? 25.321  5.603   61.092  1.00 13.58 ? 236  SER C OG  1 
ATOM   11437 N  N   . ILE C 1 245 ? 26.482  2.804   64.350  1.00 12.63 ? 237  ILE C N   1 
ATOM   11438 C  CA  . ILE C 1 245 ? 27.520  2.039   65.020  1.00 13.35 ? 237  ILE C CA  1 
ATOM   11439 C  C   . ILE C 1 245 ? 28.150  1.097   64.002  1.00 13.68 ? 237  ILE C C   1 
ATOM   11440 O  O   . ILE C 1 245 ? 27.445  0.374   63.283  1.00 15.19 ? 237  ILE C O   1 
ATOM   11441 C  CB  . ILE C 1 245 ? 26.994  1.290   66.261  1.00 11.07 ? 237  ILE C CB  1 
ATOM   11442 C  CG1 . ILE C 1 245 ? 28.148  0.561   66.958  1.00 14.86 ? 237  ILE C CG1 1 
ATOM   11443 C  CG2 . ILE C 1 245 ? 25.863  0.334   65.897  1.00 17.07 ? 237  ILE C CG2 1 
ATOM   11444 C  CD1 . ILE C 1 245 ? 27.805  0.031   68.363  1.00 16.35 ? 237  ILE C CD1 1 
ATOM   11445 N  N   . ILE C 1 246 ? 29.478  1.129   63.931  1.00 11.84 ? 238  ILE C N   1 
ATOM   11446 C  CA  . ILE C 1 246 ? 30.263  0.310   63.009  1.00 12.62 ? 238  ILE C CA  1 
ATOM   11447 C  C   . ILE C 1 246 ? 30.988  -0.731  63.848  1.00 15.23 ? 238  ILE C C   1 
ATOM   11448 O  O   . ILE C 1 246 ? 31.807  -0.377  64.704  1.00 12.53 ? 238  ILE C O   1 
ATOM   11449 C  CB  . ILE C 1 246 ? 31.247  1.172   62.205  1.00 14.56 ? 238  ILE C CB  1 
ATOM   11450 C  CG1 . ILE C 1 246 ? 30.475  2.192   61.359  1.00 14.84 ? 238  ILE C CG1 1 
ATOM   11451 C  CG2 . ILE C 1 246 ? 32.183  0.298   61.345  1.00 15.18 ? 238  ILE C CG2 1 
ATOM   11452 C  CD1 . ILE C 1 246 ? 31.306  3.408   60.928  1.00 16.82 ? 238  ILE C CD1 1 
ATOM   11453 N  N   . CYS C 1 247 ? 30.673  -2.010  63.629  1.00 12.95 ? 239  CYS C N   1 
ATOM   11454 C  CA  . CYS C 1 247 ? 31.195  -3.100  64.460  1.00 17.89 ? 239  CYS C CA  1 
ATOM   11455 C  C   . CYS C 1 247 ? 32.493  -3.598  63.841  1.00 18.20 ? 239  CYS C C   1 
ATOM   11456 O  O   . CYS C 1 247 ? 32.481  -4.333  62.851  1.00 17.57 ? 239  CYS C O   1 
ATOM   11457 C  CB  . CYS C 1 247 ? 30.177  -4.227  64.578  1.00 13.86 ? 239  CYS C CB  1 
ATOM   11458 S  SG  . CYS C 1 247 ? 28.649  -3.676  65.324  1.00 19.58 ? 239  CYS C SG  1 
ATOM   11459 N  N   . CYS C 1 248 ? 33.620  -3.204  64.428  1.00 14.24 ? 240  CYS C N   1 
ATOM   11460 C  CA  . CYS C 1 248 ? 34.936  -3.483  63.859  1.00 17.51 ? 240  CYS C CA  1 
ATOM   11461 C  C   . CYS C 1 248 ? 35.527  -4.704  64.546  1.00 23.62 ? 240  CYS C C   1 
ATOM   11462 O  O   . CYS C 1 248 ? 35.883  -4.646  65.730  1.00 18.58 ? 240  CYS C O   1 
ATOM   11463 C  CB  . CYS C 1 248 ? 35.865  -2.282  64.017  1.00 14.66 ? 240  CYS C CB  1 
ATOM   11464 S  SG  . CYS C 1 248 ? 35.270  -0.782  63.242  1.00 18.06 ? 240  CYS C SG  1 
ATOM   11465 N  N   . LYS C 1 249 ? 35.644  -5.798  63.796  1.00 17.62 ? 241  LYS C N   1 
ATOM   11466 C  CA  . LYS C 1 249 ? 36.242  -7.029  64.294  1.00 22.01 ? 241  LYS C CA  1 
ATOM   11467 C  C   . LYS C 1 249 ? 37.754  -6.871  64.270  1.00 21.75 ? 241  LYS C C   1 
ATOM   11468 O  O   . LYS C 1 249 ? 38.354  -6.824  63.194  1.00 19.34 ? 241  LYS C O   1 
ATOM   11469 C  CB  . LYS C 1 249 ? 35.806  -8.210  63.432  1.00 26.52 ? 241  LYS C CB  1 
ATOM   11470 C  CG  . LYS C 1 249 ? 34.300  -8.394  63.344  1.00 28.59 ? 241  LYS C CG  1 
ATOM   11471 C  CD  . LYS C 1 249 ? 33.763  -9.040  64.609  1.00 31.62 ? 241  LYS C CD  1 
ATOM   11472 C  CE  . LYS C 1 249 ? 32.275  -9.305  64.516  1.00 31.69 ? 241  LYS C CE  1 
ATOM   11473 N  NZ  . LYS C 1 249 ? 31.791  -10.077 65.690  1.00 30.23 ? 241  LYS C NZ  1 
ATOM   11474 N  N   . THR C 1 250 ? 38.372  -6.765  65.444  1.00 20.22 ? 242  THR C N   1 
ATOM   11475 C  CA  . THR C 1 250 ? 39.820  -6.661  65.535  1.00 24.28 ? 242  THR C CA  1 
ATOM   11476 C  C   . THR C 1 250 ? 40.403  -7.962  66.076  1.00 29.32 ? 242  THR C C   1 
ATOM   11477 O  O   . THR C 1 250 ? 39.696  -8.807  66.634  1.00 32.57 ? 242  THR C O   1 
ATOM   11478 C  CB  . THR C 1 250 ? 40.242  -5.483  66.422  1.00 21.89 ? 242  THR C CB  1 
ATOM   11479 O  OG1 . THR C 1 250 ? 39.683  -5.637  67.735  1.00 25.36 ? 242  THR C OG1 1 
ATOM   11480 C  CG2 . THR C 1 250 ? 39.782  -4.158  65.816  1.00 18.39 ? 242  THR C CG2 1 
ATOM   11481 N  N   . LEU C 1 251 ? 41.709  -8.121  65.904  1.00 29.81 ? 243  LEU C N   1 
ATOM   11482 C  CA  . LEU C 1 251 ? 42.354  -9.384  66.256  1.00 43.96 ? 243  LEU C CA  1 
ATOM   11483 C  C   . LEU C 1 251 ? 43.345  -9.203  67.398  1.00 50.01 ? 243  LEU C C   1 
ATOM   11484 O  O   . LEU C 1 251 ? 44.553  -9.317  67.205  1.00 53.80 ? 243  LEU C O   1 
ATOM   11485 C  CB  . LEU C 1 251 ? 43.059  -9.988  65.037  1.00 44.45 ? 243  LEU C CB  1 
ATOM   11486 N  N   . ALA C 1 268 ? 47.806  -4.595  81.236  1.00 56.11 ? 260  ALA C N   1 
ATOM   11487 C  CA  . ALA C 1 268 ? 49.168  -4.634  81.760  1.00 56.40 ? 260  ALA C CA  1 
ATOM   11488 C  C   . ALA C 1 268 ? 50.186  -4.426  80.641  1.00 51.63 ? 260  ALA C C   1 
ATOM   11489 O  O   . ALA C 1 268 ? 49.897  -4.727  79.484  1.00 48.84 ? 260  ALA C O   1 
ATOM   11490 C  CB  . ALA C 1 268 ? 49.423  -5.960  82.477  1.00 55.71 ? 260  ALA C CB  1 
ATOM   11491 N  N   . PRO C 1 269 ? 51.365  -3.901  80.982  1.00 53.99 ? 261  PRO C N   1 
ATOM   11492 C  CA  . PRO C 1 269 ? 52.444  -3.790  79.989  1.00 56.36 ? 261  PRO C CA  1 
ATOM   11493 C  C   . PRO C 1 269 ? 52.695  -5.114  79.272  1.00 56.45 ? 261  PRO C C   1 
ATOM   11494 O  O   . PRO C 1 269 ? 52.502  -6.194  79.837  1.00 55.63 ? 261  PRO C O   1 
ATOM   11495 C  CB  . PRO C 1 269 ? 53.656  -3.372  80.831  1.00 53.54 ? 261  PRO C CB  1 
ATOM   11496 C  CG  . PRO C 1 269 ? 53.067  -2.648  81.992  1.00 53.40 ? 261  PRO C CG  1 
ATOM   11497 C  CD  . PRO C 1 269 ? 51.736  -3.295  82.276  1.00 53.14 ? 261  PRO C CD  1 
ATOM   11498 N  N   . LEU C 1 270 ? 53.122  -5.018  78.011  1.00 52.39 ? 262  LEU C N   1 
ATOM   11499 C  CA  . LEU C 1 270 ? 53.381  -6.205  77.187  1.00 52.11 ? 262  LEU C CA  1 
ATOM   11500 C  C   . LEU C 1 270 ? 54.416  -7.128  77.824  1.00 55.19 ? 262  LEU C C   1 
ATOM   11501 O  O   . LEU C 1 270 ? 54.632  -8.247  77.358  1.00 58.89 ? 262  LEU C O   1 
ATOM   11502 C  CB  . LEU C 1 270 ? 53.852  -5.808  75.780  1.00 50.73 ? 262  LEU C CB  1 
ATOM   11503 C  CG  . LEU C 1 270 ? 52.833  -5.287  74.761  1.00 52.89 ? 262  LEU C CG  1 
ATOM   11504 C  CD1 . LEU C 1 270 ? 53.353  -5.467  73.331  1.00 54.28 ? 262  LEU C CD1 1 
ATOM   11505 C  CD2 . LEU C 1 270 ? 51.478  -5.963  74.936  1.00 53.41 ? 262  LEU C CD2 1 
ATOM   11506 N  N   . ILE C 1 275 ? 57.706  -6.989  73.374  1.00 57.28 ? 267  ILE C N   1 
ATOM   11507 C  CA  . ILE C 1 275 ? 57.589  -5.875  72.437  1.00 57.88 ? 267  ILE C CA  1 
ATOM   11508 C  C   . ILE C 1 275 ? 58.569  -6.055  71.280  1.00 59.84 ? 267  ILE C C   1 
ATOM   11509 O  O   . ILE C 1 275 ? 58.223  -5.816  70.120  1.00 58.84 ? 267  ILE C O   1 
ATOM   11510 C  CB  . ILE C 1 275 ? 57.806  -4.525  73.152  1.00 57.70 ? 267  ILE C CB  1 
ATOM   11511 C  CG1 . ILE C 1 275 ? 56.588  -4.181  74.015  1.00 56.60 ? 267  ILE C CG1 1 
ATOM   11512 C  CG2 . ILE C 1 275 ? 58.075  -3.415  72.148  1.00 54.86 ? 267  ILE C CG2 1 
ATOM   11513 C  CD1 . ILE C 1 275 ? 56.747  -2.928  74.828  1.00 56.06 ? 267  ILE C CD1 1 
ATOM   11514 N  N   . GLU C 1 276 ? 59.793  -6.485  71.603  1.00 67.25 ? 268  GLU C N   1 
ATOM   11515 C  CA  . GLU C 1 276 ? 60.770  -6.794  70.562  1.00 71.16 ? 268  GLU C CA  1 
ATOM   11516 C  C   . GLU C 1 276 ? 60.271  -7.904  69.642  1.00 72.54 ? 268  GLU C C   1 
ATOM   11517 O  O   . GLU C 1 276 ? 60.575  -7.903  68.444  1.00 73.28 ? 268  GLU C O   1 
ATOM   11518 C  CB  . GLU C 1 276 ? 62.109  -7.182  71.194  1.00 71.24 ? 268  GLU C CB  1 
ATOM   11519 N  N   . ALA C 1 277 ? 59.498  -8.850  70.182  1.00 71.86 ? 269  ALA C N   1 
ATOM   11520 C  CA  . ALA C 1 277 ? 58.901  -9.886  69.346  1.00 67.46 ? 269  ALA C CA  1 
ATOM   11521 C  C   . ALA C 1 277 ? 57.781  -9.321  68.484  1.00 62.70 ? 269  ALA C C   1 
ATOM   11522 O  O   . ALA C 1 277 ? 57.631  -9.710  67.320  1.00 63.25 ? 269  ALA C O   1 
ATOM   11523 C  CB  . ALA C 1 277 ? 58.383  -11.031 70.215  1.00 66.32 ? 269  ALA C CB  1 
ATOM   11524 N  N   . THR C 1 278 ? 56.981  -8.406  69.037  1.00 60.65 ? 270  THR C N   1 
ATOM   11525 C  CA  . THR C 1 278 ? 55.893  -7.809  68.263  1.00 59.24 ? 270  THR C CA  1 
ATOM   11526 C  C   . THR C 1 278 ? 56.423  -6.906  67.155  1.00 53.41 ? 270  THR C C   1 
ATOM   11527 O  O   . THR C 1 278 ? 55.804  -6.801  66.090  1.00 51.19 ? 270  THR C O   1 
ATOM   11528 C  CB  . THR C 1 278 ? 54.963  -7.020  69.185  1.00 57.39 ? 270  THR C CB  1 
ATOM   11529 O  OG1 . THR C 1 278 ? 54.756  -7.754  70.397  1.00 61.46 ? 270  THR C OG1 1 
ATOM   11530 C  CG2 . THR C 1 278 ? 53.619  -6.771  68.504  1.00 53.71 ? 270  THR C CG2 1 
ATOM   11531 N  N   . ARG C 1 279 ? 57.560  -6.248  67.394  1.00 49.77 ? 271  ARG C N   1 
ATOM   11532 C  CA  . ARG C 1 279 ? 58.170  -5.402  66.376  1.00 53.39 ? 271  ARG C CA  1 
ATOM   11533 C  C   . ARG C 1 279 ? 58.532  -6.203  65.129  1.00 58.67 ? 271  ARG C C   1 
ATOM   11534 O  O   . ARG C 1 279 ? 58.373  -5.720  64.002  1.00 56.90 ? 271  ARG C O   1 
ATOM   11535 C  CB  . ARG C 1 279 ? 59.409  -4.720  66.959  1.00 55.82 ? 271  ARG C CB  1 
ATOM   11536 C  CG  . ARG C 1 279 ? 59.119  -3.426  67.702  1.00 50.16 ? 271  ARG C CG  1 
ATOM   11537 C  CD  . ARG C 1 279 ? 60.394  -2.779  68.229  1.00 51.49 ? 271  ARG C CD  1 
ATOM   11538 N  NE  . ARG C 1 279 ? 60.320  -1.321  68.161  1.00 51.04 ? 271  ARG C NE  1 
ATOM   11539 C  CZ  . ARG C 1 279 ? 59.591  -0.568  68.981  1.00 50.63 ? 271  ARG C CZ  1 
ATOM   11540 N  NH1 . ARG C 1 279 ? 58.867  -1.131  69.939  1.00 55.09 ? 271  ARG C NH1 1 
ATOM   11541 N  NH2 . ARG C 1 279 ? 59.575  0.751   68.840  1.00 43.98 ? 271  ARG C NH2 1 
ATOM   11542 N  N   . LYS C 1 280 ? 59.019  -7.432  65.314  1.00 61.50 ? 272  LYS C N   1 
ATOM   11543 C  CA  . LYS C 1 280 ? 59.434  -8.253  64.181  1.00 60.50 ? 272  LYS C CA  1 
ATOM   11544 C  C   . LYS C 1 280 ? 58.242  -8.781  63.390  1.00 58.91 ? 272  LYS C C   1 
ATOM   11545 O  O   . LYS C 1 280 ? 58.322  -8.903  62.163  1.00 59.88 ? 272  LYS C O   1 
ATOM   11546 C  CB  . LYS C 1 280 ? 60.301  -9.411  64.672  1.00 62.43 ? 272  LYS C CB  1 
ATOM   11547 N  N   . HIS C 1 281 ? 57.133  -9.095  64.066  1.00 58.85 ? 273  HIS C N   1 
ATOM   11548 C  CA  . HIS C 1 281 ? 55.975  -9.656  63.375  1.00 54.83 ? 273  HIS C CA  1 
ATOM   11549 C  C   . HIS C 1 281 ? 55.287  -8.628  62.485  1.00 53.13 ? 273  HIS C C   1 
ATOM   11550 O  O   . HIS C 1 281 ? 54.724  -8.987  61.444  1.00 48.91 ? 273  HIS C O   1 
ATOM   11551 C  CB  . HIS C 1 281 ? 54.981  -10.218 64.391  1.00 53.64 ? 273  HIS C CB  1 
ATOM   11552 N  N   . LEU C 1 282 ? 55.321  -7.356  62.867  1.00 52.57 ? 274  LEU C N   1 
ATOM   11553 C  CA  . LEU C 1 282 ? 54.597  -6.316  62.153  1.00 52.93 ? 274  LEU C CA  1 
ATOM   11554 C  C   . LEU C 1 282 ? 55.488  -5.462  61.258  1.00 46.44 ? 274  LEU C C   1 
ATOM   11555 O  O   . LEU C 1 282 ? 55.001  -4.495  60.665  1.00 45.51 ? 274  LEU C O   1 
ATOM   11556 C  CB  . LEU C 1 282 ? 53.853  -5.431  63.158  1.00 52.70 ? 274  LEU C CB  1 
ATOM   11557 C  CG  . LEU C 1 282 ? 52.808  -6.213  63.956  1.00 54.74 ? 274  LEU C CG  1 
ATOM   11558 C  CD1 . LEU C 1 282 ? 52.356  -5.441  65.181  1.00 56.07 ? 274  LEU C CD1 1 
ATOM   11559 C  CD2 . LEU C 1 282 ? 51.622  -6.556  63.067  1.00 56.60 ? 274  LEU C CD2 1 
ATOM   11560 N  N   . GLY C 1 283 ? 56.769  -5.789  61.142  1.00 47.23 ? 275  GLY C N   1 
ATOM   11561 C  CA  . GLY C 1 283 ? 57.646  -5.041  60.264  1.00 46.24 ? 275  GLY C CA  1 
ATOM   11562 C  C   . GLY C 1 283 ? 57.943  -3.645  60.766  1.00 48.12 ? 275  GLY C C   1 
ATOM   11563 O  O   . GLY C 1 283 ? 57.900  -2.675  60.003  1.00 49.71 ? 275  GLY C O   1 
ATOM   11564 N  N   . TRP C 1 284 ? 58.245  -3.534  62.058  1.00 46.76 ? 276  TRP C N   1 
ATOM   11565 C  CA  . TRP C 1 284 ? 58.512  -2.255  62.715  1.00 39.61 ? 276  TRP C CA  1 
ATOM   11566 C  C   . TRP C 1 284 ? 59.811  -2.405  63.500  1.00 39.87 ? 276  TRP C C   1 
ATOM   11567 O  O   . TRP C 1 284 ? 59.804  -2.921  64.617  1.00 40.66 ? 276  TRP C O   1 
ATOM   11568 C  CB  . TRP C 1 284 ? 57.356  -1.863  63.632  1.00 33.16 ? 276  TRP C CB  1 
ATOM   11569 C  CG  . TRP C 1 284 ? 57.499  -0.510  64.256  1.00 29.71 ? 276  TRP C CG  1 
ATOM   11570 C  CD1 . TRP C 1 284 ? 58.029  -0.223  65.485  1.00 31.56 ? 276  TRP C CD1 1 
ATOM   11571 C  CD2 . TRP C 1 284 ? 57.097  0.743   63.690  1.00 29.54 ? 276  TRP C CD2 1 
ATOM   11572 N  NE1 . TRP C 1 284 ? 57.989  1.128   65.712  1.00 26.67 ? 276  TRP C NE1 1 
ATOM   11573 C  CE2 . TRP C 1 284 ? 57.421  1.746   64.630  1.00 26.36 ? 276  TRP C CE2 1 
ATOM   11574 C  CE3 . TRP C 1 284 ? 56.499  1.117   62.480  1.00 29.53 ? 276  TRP C CE3 1 
ATOM   11575 C  CZ2 . TRP C 1 284 ? 57.174  3.099   64.395  1.00 27.36 ? 276  TRP C CZ2 1 
ATOM   11576 C  CZ3 . TRP C 1 284 ? 56.248  2.461   62.252  1.00 29.10 ? 276  TRP C CZ3 1 
ATOM   11577 C  CH2 . TRP C 1 284 ? 56.586  3.435   63.205  1.00 27.71 ? 276  TRP C CH2 1 
ATOM   11578 N  N   . ALA C 1 285 ? 60.928  -1.965  62.935  1.00 39.19 ? 277  ALA C N   1 
ATOM   11579 C  CA  . ALA C 1 285 ? 62.210  -2.105  63.614  1.00 38.80 ? 277  ALA C CA  1 
ATOM   11580 C  C   . ALA C 1 285 ? 62.646  -0.838  64.337  1.00 34.27 ? 277  ALA C C   1 
ATOM   11581 O  O   . ALA C 1 285 ? 63.681  -0.854  65.007  1.00 37.48 ? 277  ALA C O   1 
ATOM   11582 C  CB  . ALA C 1 285 ? 63.296  -2.537  62.619  1.00 42.33 ? 277  ALA C CB  1 
ATOM   11583 N  N   . TYR C 1 286 ? 61.872  0.239   64.240  1.00 31.10 ? 278  TYR C N   1 
ATOM   11584 C  CA  . TYR C 1 286 ? 62.299  1.533   64.758  1.00 32.26 ? 278  TYR C CA  1 
ATOM   11585 C  C   . TYR C 1 286 ? 62.375  1.521   66.284  1.00 30.18 ? 278  TYR C C   1 
ATOM   11586 O  O   . TYR C 1 286 ? 61.487  0.974   66.946  1.00 33.23 ? 278  TYR C O   1 
ATOM   11587 C  CB  . TYR C 1 286 ? 61.340  2.627   64.302  1.00 29.57 ? 278  TYR C CB  1 
ATOM   11588 C  CG  . TYR C 1 286 ? 61.237  2.718   62.807  1.00 36.87 ? 278  TYR C CG  1 
ATOM   11589 C  CD1 . TYR C 1 286 ? 62.253  3.305   62.057  1.00 36.36 ? 278  TYR C CD1 1 
ATOM   11590 C  CD2 . TYR C 1 286 ? 60.135  2.205   62.138  1.00 34.47 ? 278  TYR C CD2 1 
ATOM   11591 C  CE1 . TYR C 1 286 ? 62.164  3.389   60.677  1.00 38.71 ? 278  TYR C CE1 1 
ATOM   11592 C  CE2 . TYR C 1 286 ? 60.038  2.282   60.759  1.00 41.43 ? 278  TYR C CE2 1 
ATOM   11593 C  CZ  . TYR C 1 286 ? 61.053  2.872   60.035  1.00 40.33 ? 278  TYR C CZ  1 
ATOM   11594 O  OH  . TYR C 1 286 ? 60.952  2.946   58.671  1.00 40.39 ? 278  TYR C OH  1 
ATOM   11595 N  N   . PRO C 1 287 ? 63.413  2.125   66.866  1.00 31.06 ? 279  PRO C N   1 
ATOM   11596 C  CA  . PRO C 1 287 ? 63.540  2.153   68.328  1.00 31.02 ? 279  PRO C CA  1 
ATOM   11597 C  C   . PRO C 1 287 ? 62.391  2.916   68.967  1.00 29.59 ? 279  PRO C C   1 
ATOM   11598 O  O   . PRO C 1 287 ? 61.735  3.744   68.335  1.00 28.72 ? 279  PRO C O   1 
ATOM   11599 C  CB  . PRO C 1 287 ? 64.876  2.874   68.556  1.00 32.93 ? 279  PRO C CB  1 
ATOM   11600 C  CG  . PRO C 1 287 ? 65.625  2.717   67.268  1.00 33.82 ? 279  PRO C CG  1 
ATOM   11601 C  CD  . PRO C 1 287 ? 64.575  2.737   66.197  1.00 32.64 ? 279  PRO C CD  1 
ATOM   11602 N  N   . ALA C 1 288 ? 62.162  2.628   70.247  1.00 32.14 ? 280  ALA C N   1 
ATOM   11603 C  CA  . ALA C 1 288 ? 61.071  3.254   70.975  1.00 28.57 ? 280  ALA C CA  1 
ATOM   11604 C  C   . ALA C 1 288 ? 61.168  4.773   70.890  1.00 37.29 ? 280  ALA C C   1 
ATOM   11605 O  O   . ALA C 1 288 ? 62.241  5.356   71.071  1.00 29.94 ? 280  ALA C O   1 
ATOM   11606 C  CB  . ALA C 1 288 ? 61.078  2.788   72.434  1.00 29.33 ? 280  ALA C CB  1 
ATOM   11607 N  N   . PHE C 1 289 ? 60.044  5.402   70.554  1.00 27.17 ? 281  PHE C N   1 
ATOM   11608 C  CA  . PHE C 1 289 ? 59.863  6.848   70.455  1.00 28.60 ? 281  PHE C CA  1 
ATOM   11609 C  C   . PHE C 1 289 ? 60.623  7.496   69.300  1.00 34.22 ? 281  PHE C C   1 
ATOM   11610 O  O   . PHE C 1 289 ? 60.709  8.730   69.248  1.00 34.89 ? 281  PHE C O   1 
ATOM   11611 C  CB  . PHE C 1 289 ? 60.228  7.541   71.769  1.00 28.20 ? 281  PHE C CB  1 
ATOM   11612 C  CG  . PHE C 1 289 ? 59.442  7.033   72.944  1.00 27.93 ? 281  PHE C CG  1 
ATOM   11613 C  CD1 . PHE C 1 289 ? 58.125  7.424   73.128  1.00 26.73 ? 281  PHE C CD1 1 
ATOM   11614 C  CD2 . PHE C 1 289 ? 60.011  6.145   73.844  1.00 29.12 ? 281  PHE C CD2 1 
ATOM   11615 C  CE1 . PHE C 1 289 ? 57.387  6.952   74.195  1.00 26.86 ? 281  PHE C CE1 1 
ATOM   11616 C  CE2 . PHE C 1 289 ? 59.284  5.673   74.919  1.00 36.81 ? 281  PHE C CE2 1 
ATOM   11617 C  CZ  . PHE C 1 289 ? 57.970  6.075   75.093  1.00 32.41 ? 281  PHE C CZ  1 
ATOM   11618 N  N   . GLU C 1 290 ? 61.144  6.717   68.353  1.00 28.10 ? 282  GLU C N   1 
ATOM   11619 C  CA  . GLU C 1 290 ? 61.897  7.248   67.217  1.00 31.02 ? 282  GLU C CA  1 
ATOM   11620 C  C   . GLU C 1 290 ? 61.101  7.007   65.933  1.00 41.02 ? 282  GLU C C   1 
ATOM   11621 O  O   . GLU C 1 290 ? 61.187  5.931   65.331  1.00 42.98 ? 282  GLU C O   1 
ATOM   11622 C  CB  . GLU C 1 290 ? 63.283  6.611   67.148  1.00 31.01 ? 282  GLU C CB  1 
ATOM   11623 N  N   . ILE C 1 291 ? 60.368  8.024   65.497  1.00 27.66 ? 283  ILE C N   1 
ATOM   11624 C  CA  . ILE C 1 291 ? 59.434  7.924   64.374  1.00 27.68 ? 283  ILE C CA  1 
ATOM   11625 C  C   . ILE C 1 291 ? 60.071  8.568   63.154  1.00 31.45 ? 283  ILE C C   1 
ATOM   11626 O  O   . ILE C 1 291 ? 60.432  9.757   63.210  1.00 33.06 ? 283  ILE C O   1 
ATOM   11627 C  CB  . ILE C 1 291 ? 58.096  8.599   64.700  1.00 25.63 ? 283  ILE C CB  1 
ATOM   11628 C  CG1 . ILE C 1 291 ? 57.437  7.938   65.908  1.00 24.11 ? 283  ILE C CG1 1 
ATOM   11629 C  CG2 . ILE C 1 291 ? 57.181  8.556   63.495  1.00 27.72 ? 283  ILE C CG2 1 
ATOM   11630 C  CD1 . ILE C 1 291 ? 56.202  8.680   66.404  1.00 22.80 ? 283  ILE C CD1 1 
ATOM   11631 N  N   . PRO C 1 292 ? 60.193  7.865   62.027  1.00 31.71 ? 284  PRO C N   1 
ATOM   11632 C  CA  . PRO C 1 292 ? 60.839  8.463   60.853  1.00 34.53 ? 284  PRO C CA  1 
ATOM   11633 C  C   . PRO C 1 292 ? 60.037  9.644   60.325  1.00 33.64 ? 284  PRO C C   1 
ATOM   11634 O  O   . PRO C 1 292 ? 58.808  9.686   60.422  1.00 32.66 ? 284  PRO C O   1 
ATOM   11635 C  CB  . PRO C 1 292 ? 60.894  7.310   59.844  1.00 36.54 ? 284  PRO C CB  1 
ATOM   11636 C  CG  . PRO C 1 292 ? 59.816  6.375   60.273  1.00 36.89 ? 284  PRO C CG  1 
ATOM   11637 C  CD  . PRO C 1 292 ? 59.725  6.490   61.771  1.00 30.56 ? 284  PRO C CD  1 
ATOM   11638 N  N   . GLN C 1 293 ? 60.760  10.618  59.768  1.00 36.38 ? 285  GLN C N   1 
ATOM   11639 C  CA  . GLN C 1 293 ? 60.151  11.899  59.419  1.00 38.04 ? 285  GLN C CA  1 
ATOM   11640 C  C   . GLN C 1 293 ? 59.050  11.747  58.375  1.00 36.70 ? 285  GLN C C   1 
ATOM   11641 O  O   . GLN C 1 293 ? 58.096  12.533  58.369  1.00 32.48 ? 285  GLN C O   1 
ATOM   11642 C  CB  . GLN C 1 293 ? 61.228  12.874  58.925  1.00 44.19 ? 285  GLN C CB  1 
ATOM   11643 C  CG  . GLN C 1 293 ? 60.752  14.313  58.761  1.00 44.18 ? 285  GLN C CG  1 
ATOM   11644 C  CD  . GLN C 1 293 ? 60.124  14.869  60.027  1.00 54.79 ? 285  GLN C CD  1 
ATOM   11645 O  OE1 . GLN C 1 293 ? 60.668  14.718  61.124  1.00 59.43 ? 285  GLN C OE1 1 
ATOM   11646 N  NE2 . GLN C 1 293 ? 58.958  15.500  59.884  1.00 56.12 ? 285  GLN C NE2 1 
ATOM   11647 N  N   . GLU C 1 294 ? 59.155  10.750  57.491  1.00 33.16 ? 286  GLU C N   1 
ATOM   11648 C  CA  . GLU C 1 294 ? 58.119  10.562  56.482  1.00 33.11 ? 286  GLU C CA  1 
ATOM   11649 C  C   . GLU C 1 294 ? 56.787  10.185  57.116  1.00 34.75 ? 286  GLU C C   1 
ATOM   11650 O  O   . GLU C 1 294 ? 55.725  10.542  56.592  1.00 37.74 ? 286  GLU C O   1 
ATOM   11651 C  CB  . GLU C 1 294 ? 58.544  9.497   55.473  1.00 35.77 ? 286  GLU C CB  1 
ATOM   11652 N  N   . ILE C 1 295 ? 56.818  9.471   58.242  1.00 31.12 ? 287  ILE C N   1 
ATOM   11653 C  CA  . ILE C 1 295 ? 55.572  9.120   58.914  1.00 29.19 ? 287  ILE C CA  1 
ATOM   11654 C  C   . ILE C 1 295 ? 54.970  10.350  59.586  1.00 31.44 ? 287  ILE C C   1 
ATOM   11655 O  O   . ILE C 1 295 ? 53.754  10.566  59.536  1.00 31.33 ? 287  ILE C O   1 
ATOM   11656 C  CB  . ILE C 1 295 ? 55.812  7.961   59.899  1.00 29.74 ? 287  ILE C CB  1 
ATOM   11657 C  CG1 . ILE C 1 295 ? 56.156  6.685   59.115  1.00 28.96 ? 287  ILE C CG1 1 
ATOM   11658 C  CG2 . ILE C 1 295 ? 54.591  7.749   60.805  1.00 26.91 ? 287  ILE C CG2 1 
ATOM   11659 C  CD1 . ILE C 1 295 ? 56.351  5.439   59.981  1.00 28.74 ? 287  ILE C CD1 1 
ATOM   11660 N  N   . TYR C 1 296 ? 55.810  11.202  60.179  1.00 27.58 ? 288  TYR C N   1 
ATOM   11661 C  CA  . TYR C 1 296 ? 55.305  12.447  60.752  1.00 28.52 ? 288  TYR C CA  1 
ATOM   11662 C  C   . TYR C 1 296 ? 54.689  13.342  59.682  1.00 27.16 ? 288  TYR C C   1 
ATOM   11663 O  O   . TYR C 1 296 ? 53.663  13.990  59.919  1.00 26.42 ? 288  TYR C O   1 
ATOM   11664 C  CB  . TYR C 1 296 ? 56.422  13.206  61.466  1.00 27.18 ? 288  TYR C CB  1 
ATOM   11665 C  CG  . TYR C 1 296 ? 56.702  12.819  62.902  1.00 25.46 ? 288  TYR C CG  1 
ATOM   11666 C  CD1 . TYR C 1 296 ? 55.718  12.879  63.876  1.00 27.33 ? 288  TYR C CD1 1 
ATOM   11667 C  CD2 . TYR C 1 296 ? 57.981  12.456  63.289  1.00 26.80 ? 288  TYR C CD2 1 
ATOM   11668 C  CE1 . TYR C 1 296 ? 56.007  12.553  65.205  1.00 30.51 ? 288  TYR C CE1 1 
ATOM   11669 C  CE2 . TYR C 1 296 ? 58.278  12.137  64.593  1.00 32.63 ? 288  TYR C CE2 1 
ATOM   11670 C  CZ  . TYR C 1 296 ? 57.300  12.181  65.551  1.00 31.03 ? 288  TYR C CZ  1 
ATOM   11671 O  OH  . TYR C 1 296 ? 57.633  11.850  66.849  1.00 28.57 ? 288  TYR C OH  1 
ATOM   11672 N  N   . ASP C 1 297 ? 55.317  13.420  58.506  1.00 30.69 ? 289  ASP C N   1 
ATOM   11673 C  CA  . ASP C 1 297 ? 54.766  14.260  57.450  1.00 35.96 ? 289  ASP C CA  1 
ATOM   11674 C  C   . ASP C 1 297 ? 53.429  13.719  56.962  1.00 38.95 ? 289  ASP C C   1 
ATOM   11675 O  O   . ASP C 1 297 ? 52.522  14.492  56.634  1.00 41.43 ? 289  ASP C O   1 
ATOM   11676 C  CB  . ASP C 1 297 ? 55.749  14.369  56.288  1.00 39.31 ? 289  ASP C CB  1 
ATOM   11677 C  CG  . ASP C 1 297 ? 57.067  14.983  56.696  1.00 41.39 ? 289  ASP C CG  1 
ATOM   11678 O  OD1 . ASP C 1 297 ? 57.097  15.739  57.687  1.00 42.96 ? 289  ASP C OD1 1 
ATOM   11679 O  OD2 . ASP C 1 297 ? 58.078  14.710  56.018  1.00 45.28 ? 289  ASP C OD2 1 
ATOM   11680 N  N   . ALA C 1 298 ? 53.292  12.395  56.896  1.00 37.80 ? 290  ALA C N   1 
ATOM   11681 C  CA  . ALA C 1 298 ? 52.038  11.817  56.436  1.00 34.87 ? 290  ALA C CA  1 
ATOM   11682 C  C   . ALA C 1 298 ? 50.916  12.056  57.436  1.00 30.77 ? 290  ALA C C   1 
ATOM   11683 O  O   . ALA C 1 298 ? 49.752  12.169  57.038  1.00 29.15 ? 290  ALA C O   1 
ATOM   11684 C  CB  . ALA C 1 298 ? 52.209  10.321  56.171  1.00 30.33 ? 290  ALA C CB  1 
ATOM   11685 N  N   . TRP C 1 299 ? 51.248  12.155  58.728  1.00 28.91 ? 291  TRP C N   1 
ATOM   11686 C  CA  . TRP C 1 299 ? 50.256  12.305  59.790  1.00 21.13 ? 291  TRP C CA  1 
ATOM   11687 C  C   . TRP C 1 299 ? 49.940  13.755  60.128  1.00 24.84 ? 291  TRP C C   1 
ATOM   11688 O  O   . TRP C 1 299 ? 48.899  14.019  60.744  1.00 24.27 ? 291  TRP C O   1 
ATOM   11689 C  CB  . TRP C 1 299 ? 50.742  11.615  61.071  1.00 20.45 ? 291  TRP C CB  1 
ATOM   11690 C  CG  . TRP C 1 299 ? 50.219  10.241  61.270  1.00 25.06 ? 291  TRP C CG  1 
ATOM   11691 C  CD1 . TRP C 1 299 ? 50.907  9.073   61.129  1.00 27.11 ? 291  TRP C CD1 1 
ATOM   11692 C  CD2 . TRP C 1 299 ? 48.884  9.879   61.647  1.00 26.56 ? 291  TRP C CD2 1 
ATOM   11693 N  NE1 . TRP C 1 299 ? 50.081  8.002   61.399  1.00 24.81 ? 291  TRP C NE1 1 
ATOM   11694 C  CE2 . TRP C 1 299 ? 48.834  8.472   61.716  1.00 26.12 ? 291  TRP C CE2 1 
ATOM   11695 C  CE3 . TRP C 1 299 ? 47.726  10.610  61.930  1.00 26.21 ? 291  TRP C CE3 1 
ATOM   11696 C  CZ2 . TRP C 1 299 ? 47.670  7.780   62.060  1.00 23.44 ? 291  TRP C CZ2 1 
ATOM   11697 C  CZ3 . TRP C 1 299 ? 46.572  9.922   62.270  1.00 24.59 ? 291  TRP C CZ3 1 
ATOM   11698 C  CH2 . TRP C 1 299 ? 46.555  8.521   62.333  1.00 21.89 ? 291  TRP C CH2 1 
ATOM   11699 N  N   . ASN C 1 300 ? 50.810  14.694  59.768  1.00 28.68 ? 292  ASN C N   1 
ATOM   11700 C  CA  . ASN C 1 300 ? 50.645  16.064  60.234  1.00 29.35 ? 292  ASN C CA  1 
ATOM   11701 C  C   . ASN C 1 300 ? 49.382  16.689  59.648  1.00 28.50 ? 292  ASN C C   1 
ATOM   11702 O  O   . ASN C 1 300 ? 49.155  16.632  58.436  1.00 25.91 ? 292  ASN C O   1 
ATOM   11703 C  CB  . ASN C 1 300 ? 51.866  16.896  59.861  1.00 33.11 ? 292  ASN C CB  1 
ATOM   11704 C  CG  . ASN C 1 300 ? 51.922  18.189  60.629  1.00 31.62 ? 292  ASN C CG  1 
ATOM   11705 O  OD1 . ASN C 1 300 ? 51.401  19.205  60.181  1.00 31.62 ? 292  ASN C OD1 1 
ATOM   11706 N  ND2 . ASN C 1 300 ? 52.531  18.153  61.810  1.00 29.52 ? 292  ASN C ND2 1 
ATOM   11707 N  N   . ALA C 1 301 ? 48.559  17.289  60.514  1.00 24.62 ? 293  ALA C N   1 
ATOM   11708 C  CA  . ALA C 1 301 ? 47.292  17.880  60.098  1.00 24.56 ? 293  ALA C CA  1 
ATOM   11709 C  C   . ALA C 1 301 ? 47.302  19.405  60.108  1.00 23.52 ? 293  ALA C C   1 
ATOM   11710 O  O   . ALA C 1 301 ? 46.232  20.016  60.014  1.00 25.94 ? 293  ALA C O   1 
ATOM   11711 C  CB  . ALA C 1 301 ? 46.155  17.377  60.991  1.00 23.78 ? 293  ALA C CB  1 
ATOM   11712 N  N   . LYS C 1 302 ? 48.472  20.037  60.215  1.00 23.65 ? 294  LYS C N   1 
ATOM   11713 C  CA  . LYS C 1 302 ? 48.517  21.492  60.334  1.00 24.71 ? 294  LYS C CA  1 
ATOM   11714 C  C   . LYS C 1 302 ? 47.967  22.171  59.084  1.00 27.86 ? 294  LYS C C   1 
ATOM   11715 O  O   . LYS C 1 302 ? 47.107  23.056  59.171  1.00 29.59 ? 294  LYS C O   1 
ATOM   11716 C  CB  . LYS C 1 302 ? 49.950  21.956  60.610  1.00 24.06 ? 294  LYS C CB  1 
ATOM   11717 N  N   . GLU C 1 303 ? 48.447  21.764  57.908  1.00 24.36 ? 295  GLU C N   1 
ATOM   11718 C  CA  . GLU C 1 303 ? 48.019  22.418  56.674  1.00 25.70 ? 295  GLU C CA  1 
ATOM   11719 C  C   . GLU C 1 303 ? 46.521  22.250  56.453  1.00 28.71 ? 295  GLU C C   1 
ATOM   11720 O  O   . GLU C 1 303 ? 45.816  23.218  56.149  1.00 24.48 ? 295  GLU C O   1 
ATOM   11721 C  CB  . GLU C 1 303 ? 48.804  21.863  55.482  1.00 34.08 ? 295  GLU C CB  1 
ATOM   11722 C  CG  . GLU C 1 303 ? 48.327  22.398  54.132  1.00 42.08 ? 295  GLU C CG  1 
ATOM   11723 C  CD  . GLU C 1 303 ? 49.216  21.984  52.970  1.00 56.25 ? 295  GLU C CD  1 
ATOM   11724 O  OE1 . GLU C 1 303 ? 50.282  21.379  53.215  1.00 60.80 ? 295  GLU C OE1 1 
ATOM   11725 O  OE2 . GLU C 1 303 ? 48.845  22.268  51.807  1.00 62.25 ? 295  GLU C OE2 1 
ATOM   11726 N  N   . LYS C 1 304 ? 46.015  21.022  56.605  1.00 28.84 ? 296  LYS C N   1 
ATOM   11727 C  CA  . LYS C 1 304 ? 44.590  20.789  56.390  1.00 26.82 ? 296  LYS C CA  1 
ATOM   11728 C  C   . LYS C 1 304 ? 43.755  21.484  57.456  1.00 20.95 ? 296  LYS C C   1 
ATOM   11729 O  O   . LYS C 1 304 ? 42.699  22.053  57.151  1.00 21.82 ? 296  LYS C O   1 
ATOM   11730 C  CB  . LYS C 1 304 ? 44.291  19.289  56.365  1.00 24.57 ? 296  LYS C CB  1 
ATOM   11731 N  N   . GLY C 1 305 ? 44.212  21.445  58.708  1.00 19.33 ? 297  GLY C N   1 
ATOM   11732 C  CA  . GLY C 1 305 ? 43.466  22.085  59.782  1.00 18.21 ? 297  GLY C CA  1 
ATOM   11733 C  C   . GLY C 1 305 ? 43.369  23.586  59.597  1.00 24.06 ? 297  GLY C C   1 
ATOM   11734 O  O   . GLY C 1 305 ? 42.308  24.183  59.816  1.00 20.35 ? 297  GLY C O   1 
ATOM   11735 N  N   . ALA C 1 306 ? 44.470  24.211  59.161  1.00 22.04 ? 298  ALA C N   1 
ATOM   11736 C  CA  . ALA C 1 306 ? 44.469  25.650  58.938  1.00 22.20 ? 298  ALA C CA  1 
ATOM   11737 C  C   . ALA C 1 306 ? 43.528  26.034  57.804  1.00 29.22 ? 298  ALA C C   1 
ATOM   11738 O  O   . ALA C 1 306 ? 42.816  27.039  57.900  1.00 26.19 ? 298  ALA C O   1 
ATOM   11739 C  CB  . ALA C 1 306 ? 45.888  26.147  58.647  1.00 27.66 ? 298  ALA C CB  1 
ATOM   11740 N  N   . LYS C 1 307 ? 43.526  25.261  56.710  1.00 23.03 ? 299  LYS C N   1 
ATOM   11741 C  CA  . LYS C 1 307 ? 42.596  25.541  55.620  1.00 23.65 ? 299  LYS C CA  1 
ATOM   11742 C  C   . LYS C 1 307 ? 41.149  25.356  56.065  1.00 23.78 ? 299  LYS C C   1 
ATOM   11743 O  O   . LYS C 1 307 ? 40.255  26.084  55.618  1.00 22.11 ? 299  LYS C O   1 
ATOM   11744 C  CB  . LYS C 1 307 ? 42.901  24.642  54.421  1.00 24.90 ? 299  LYS C CB  1 
ATOM   11745 N  N   . LEU C 1 308 ? 40.905  24.376  56.940  1.00 20.09 ? 300  LEU C N   1 
ATOM   11746 C  CA  . LEU C 1 308 ? 39.553  24.100  57.423  1.00 21.99 ? 300  LEU C CA  1 
ATOM   11747 C  C   . LEU C 1 308 ? 38.997  25.274  58.219  1.00 21.98 ? 300  LEU C C   1 
ATOM   11748 O  O   . LEU C 1 308 ? 37.870  25.727  57.979  1.00 19.14 ? 300  LEU C O   1 
ATOM   11749 C  CB  . LEU C 1 308 ? 39.570  22.834  58.279  1.00 17.39 ? 300  LEU C CB  1 
ATOM   11750 C  CG  . LEU C 1 308 ? 38.281  22.464  59.024  1.00 16.70 ? 300  LEU C CG  1 
ATOM   11751 C  CD1 . LEU C 1 308 ? 37.281  21.882  58.036  1.00 18.49 ? 300  LEU C CD1 1 
ATOM   11752 C  CD2 . LEU C 1 308 ? 38.603  21.498  60.177  1.00 16.36 ? 300  LEU C CD2 1 
ATOM   11753 N  N   . GLU C 1 309 ? 39.784  25.786  59.169  1.00 18.18 ? 301  GLU C N   1 
ATOM   11754 C  CA  . GLU C 1 309 ? 39.322  26.878  60.015  1.00 21.23 ? 301  GLU C CA  1 
ATOM   11755 C  C   . GLU C 1 309 ? 39.258  28.188  59.243  1.00 20.21 ? 301  GLU C C   1 
ATOM   11756 O  O   . GLU C 1 309 ? 38.350  28.990  59.476  1.00 19.40 ? 301  GLU C O   1 
ATOM   11757 C  CB  . GLU C 1 309 ? 40.224  27.011  61.250  1.00 18.18 ? 301  GLU C CB  1 
ATOM   11758 C  CG  . GLU C 1 309 ? 39.781  28.098  62.236  1.00 22.88 ? 301  GLU C CG  1 
ATOM   11759 C  CD  . GLU C 1 309 ? 40.359  27.910  63.637  1.00 25.67 ? 301  GLU C CD  1 
ATOM   11760 O  OE1 . GLU C 1 309 ? 41.041  26.889  63.879  1.00 25.99 ? 301  GLU C OE1 1 
ATOM   11761 O  OE2 . GLU C 1 309 ? 40.129  28.785  64.498  1.00 21.75 ? 301  GLU C OE2 1 
ATOM   11762 N  N   . ALA C 1 310 ? 40.189  28.419  58.312  1.00 22.71 ? 302  ALA C N   1 
ATOM   11763 C  CA  . ALA C 1 310 ? 40.104  29.619  57.481  1.00 22.91 ? 302  ALA C CA  1 
ATOM   11764 C  C   . ALA C 1 310 ? 38.817  29.623  56.661  1.00 22.58 ? 302  ALA C C   1 
ATOM   11765 O  O   . ALA C 1 310 ? 38.171  30.666  56.506  1.00 23.36 ? 302  ALA C O   1 
ATOM   11766 C  CB  . ALA C 1 310 ? 41.325  29.727  56.561  1.00 25.09 ? 302  ALA C CB  1 
ATOM   11767 N  N   . GLY C 1 311 ? 38.431  28.464  56.126  1.00 22.56 ? 303  GLY C N   1 
ATOM   11768 C  CA  . GLY C 1 311 ? 37.193  28.390  55.369  1.00 24.59 ? 303  GLY C CA  1 
ATOM   11769 C  C   . GLY C 1 311 ? 35.970  28.634  56.234  1.00 20.37 ? 303  GLY C C   1 
ATOM   11770 O  O   . GLY C 1 311 ? 35.041  29.334  55.825  1.00 21.25 ? 303  GLY C O   1 
ATOM   11771 N  N   . TRP C 1 312 ? 35.958  28.072  57.445  1.00 18.84 ? 304  TRP C N   1 
ATOM   11772 C  CA  . TRP C 1 312 ? 34.855  28.349  58.354  1.00 20.62 ? 304  TRP C CA  1 
ATOM   11773 C  C   . TRP C 1 312 ? 34.834  29.822  58.763  1.00 22.06 ? 304  TRP C C   1 
ATOM   11774 O  O   . TRP C 1 312 ? 33.757  30.427  58.843  1.00 20.34 ? 304  TRP C O   1 
ATOM   11775 C  CB  . TRP C 1 312 ? 34.925  27.430  59.579  1.00 16.49 ? 304  TRP C CB  1 
ATOM   11776 C  CG  . TRP C 1 312 ? 33.757  27.613  60.496  1.00 18.08 ? 304  TRP C CG  1 
ATOM   11777 C  CD1 . TRP C 1 312 ? 32.577  26.921  60.473  1.00 18.11 ? 304  TRP C CD1 1 
ATOM   11778 C  CD2 . TRP C 1 312 ? 33.634  28.581  61.548  1.00 21.37 ? 304  TRP C CD2 1 
ATOM   11779 N  NE1 . TRP C 1 312 ? 31.734  27.393  61.456  1.00 16.80 ? 304  TRP C NE1 1 
ATOM   11780 C  CE2 . TRP C 1 312 ? 32.357  28.411  62.126  1.00 16.00 ? 304  TRP C CE2 1 
ATOM   11781 C  CE3 . TRP C 1 312 ? 34.481  29.572  62.060  1.00 19.33 ? 304  TRP C CE3 1 
ATOM   11782 C  CZ2 . TRP C 1 312 ? 31.908  29.192  63.194  1.00 18.22 ? 304  TRP C CZ2 1 
ATOM   11783 C  CZ3 . TRP C 1 312 ? 34.034  30.348  63.114  1.00 24.99 ? 304  TRP C CZ3 1 
ATOM   11784 C  CH2 . TRP C 1 312 ? 32.757  30.147  63.673  1.00 20.27 ? 304  TRP C CH2 1 
ATOM   11785 N  N   . ASN C 1 313 ? 36.009  30.423  59.003  1.00 19.40 ? 305  ASN C N   1 
ATOM   11786 C  CA  . ASN C 1 313 ? 36.058  31.851  59.316  1.00 20.57 ? 305  ASN C CA  1 
ATOM   11787 C  C   . ASN C 1 313 ? 35.425  32.688  58.207  1.00 22.84 ? 305  ASN C C   1 
ATOM   11788 O  O   . ASN C 1 313 ? 34.719  33.663  58.487  1.00 22.06 ? 305  ASN C O   1 
ATOM   11789 C  CB  . ASN C 1 313 ? 37.503  32.314  59.550  1.00 22.04 ? 305  ASN C CB  1 
ATOM   11790 C  CG  . ASN C 1 313 ? 38.068  31.862  60.892  1.00 28.66 ? 305  ASN C CG  1 
ATOM   11791 O  OD1 . ASN C 1 313 ? 39.289  31.736  61.059  1.00 34.90 ? 305  ASN C OD1 1 
ATOM   11792 N  ND2 . ASN C 1 313 ? 37.195  31.627  61.851  1.00 22.29 ? 305  ASN C ND2 1 
ATOM   11793 N  N   . GLU C 1 314 ? 35.682  32.336  56.939  1.00 23.52 ? 306  GLU C N   1 
ATOM   11794 C  CA  . GLU C 1 314 ? 35.060  33.061  55.834  1.00 23.88 ? 306  GLU C CA  1 
ATOM   11795 C  C   . GLU C 1 314 ? 33.542  32.913  55.866  1.00 23.49 ? 306  GLU C C   1 
ATOM   11796 O  O   . GLU C 1 314 ? 32.808  33.883  55.637  1.00 23.48 ? 306  GLU C O   1 
ATOM   11797 C  CB  . GLU C 1 314 ? 35.621  32.575  54.495  1.00 33.43 ? 306  GLU C CB  1 
ATOM   11798 C  CG  . GLU C 1 314 ? 37.108  32.825  54.305  1.00 40.26 ? 306  GLU C CG  1 
ATOM   11799 C  CD  . GLU C 1 314 ? 37.561  32.656  52.859  1.00 53.47 ? 306  GLU C CD  1 
ATOM   11800 O  OE1 . GLU C 1 314 ? 36.705  32.394  51.983  1.00 54.97 ? 306  GLU C OE1 1 
ATOM   11801 O  OE2 . GLU C 1 314 ? 38.776  32.793  52.598  1.00 57.63 ? 306  GLU C OE2 1 
ATOM   11802 N  N   . LEU C 1 315 ? 33.056  31.700  56.135  1.00 21.60 ? 307  LEU C N   1 
ATOM   11803 C  CA  . LEU C 1 315 ? 31.619  31.487  56.248  1.00 23.80 ? 307  LEU C CA  1 
ATOM   11804 C  C   . LEU C 1 315 ? 31.050  32.245  57.440  1.00 23.47 ? 307  LEU C C   1 
ATOM   11805 O  O   . LEU C 1 315 ? 29.975  32.850  57.345  1.00 22.63 ? 307  LEU C O   1 
ATOM   11806 C  CB  . LEU C 1 315 ? 31.321  29.992  56.372  1.00 20.95 ? 307  LEU C CB  1 
ATOM   11807 C  CG  . LEU C 1 315 ? 29.851  29.620  56.580  1.00 19.81 ? 307  LEU C CG  1 
ATOM   11808 C  CD1 . LEU C 1 315 ? 29.049  29.910  55.320  1.00 23.06 ? 307  LEU C CD1 1 
ATOM   11809 C  CD2 . LEU C 1 315 ? 29.719  28.160  56.998  1.00 21.97 ? 307  LEU C CD2 1 
ATOM   11810 N  N   . PHE C 1 316 ? 31.758  32.229  58.573  1.00 19.14 ? 308  PHE C N   1 
ATOM   11811 C  CA  . PHE C 1 316 ? 31.288  32.988  59.727  1.00 23.89 ? 308  PHE C CA  1 
ATOM   11812 C  C   . PHE C 1 316 ? 31.328  34.491  59.473  1.00 24.53 ? 308  PHE C C   1 
ATOM   11813 O  O   . PHE C 1 316 ? 30.469  35.222  59.979  1.00 25.39 ? 308  PHE C O   1 
ATOM   11814 C  CB  . PHE C 1 316 ? 32.110  32.644  60.967  1.00 18.48 ? 308  PHE C CB  1 
ATOM   11815 C  CG  . PHE C 1 316 ? 31.527  33.196  62.244  1.00 23.20 ? 308  PHE C CG  1 
ATOM   11816 C  CD1 . PHE C 1 316 ? 30.368  32.660  62.774  1.00 21.91 ? 308  PHE C CD1 1 
ATOM   11817 C  CD2 . PHE C 1 316 ? 32.130  34.250  62.902  1.00 24.44 ? 308  PHE C CD2 1 
ATOM   11818 C  CE1 . PHE C 1 316 ? 29.821  33.165  63.947  1.00 18.00 ? 308  PHE C CE1 1 
ATOM   11819 C  CE2 . PHE C 1 316 ? 31.588  34.759  64.073  1.00 22.78 ? 308  PHE C CE2 1 
ATOM   11820 C  CZ  . PHE C 1 316 ? 30.427  34.209  64.589  1.00 19.22 ? 308  PHE C CZ  1 
ATOM   11821 N  N   . ALA C 1 317 ? 32.302  34.978  58.700  1.00 21.87 ? 309  ALA C N   1 
ATOM   11822 C  CA  . ALA C 1 317 ? 32.291  36.397  58.348  1.00 23.70 ? 309  ALA C CA  1 
ATOM   11823 C  C   . ALA C 1 317 ? 31.052  36.747  57.529  1.00 27.74 ? 309  ALA C C   1 
ATOM   11824 O  O   . ALA C 1 317 ? 30.431  37.800  57.738  1.00 24.68 ? 309  ALA C O   1 
ATOM   11825 C  CB  . ALA C 1 317 ? 33.564  36.776  57.589  1.00 28.87 ? 309  ALA C CB  1 
ATOM   11826 N  N   . GLN C 1 318 ? 30.679  35.876  56.588  1.00 29.20 ? 310  GLN C N   1 
ATOM   11827 C  CA  A GLN C 1 318 ? 29.472  36.100  55.799  0.52 30.18 ? 310  GLN C CA  1 
ATOM   11828 C  CA  B GLN C 1 318 ? 29.471  36.115  55.803  0.48 30.10 ? 310  GLN C CA  1 
ATOM   11829 C  C   . GLN C 1 318 ? 28.238  36.147  56.697  1.00 28.58 ? 310  GLN C C   1 
ATOM   11830 O  O   . GLN C 1 318 ? 27.381  37.030  56.554  1.00 24.85 ? 310  GLN C O   1 
ATOM   11831 C  CB  A GLN C 1 318 ? 29.349  34.993  54.749  0.52 28.43 ? 310  GLN C CB  1 
ATOM   11832 C  CB  B GLN C 1 318 ? 29.320  35.044  54.722  0.48 28.62 ? 310  GLN C CB  1 
ATOM   11833 C  CG  A GLN C 1 318 ? 28.378  35.260  53.623  0.52 31.42 ? 310  GLN C CG  1 
ATOM   11834 C  CG  B GLN C 1 318 ? 30.398  35.078  53.661  0.48 31.44 ? 310  GLN C CG  1 
ATOM   11835 C  CD  A GLN C 1 318 ? 28.461  34.197  52.541  0.52 37.76 ? 310  GLN C CD  1 
ATOM   11836 C  CD  B GLN C 1 318 ? 30.126  34.107  52.531  0.48 39.04 ? 310  GLN C CD  1 
ATOM   11837 O  OE1 A GLN C 1 318 ? 29.408  33.408  52.503  0.52 40.38 ? 310  GLN C OE1 1 
ATOM   11838 O  OE1 B GLN C 1 318 ? 29.202  33.296  52.602  0.48 38.56 ? 310  GLN C OE1 1 
ATOM   11839 N  NE2 A GLN C 1 318 ? 27.467  34.166  51.662  0.52 35.61 ? 310  GLN C NE2 1 
ATOM   11840 N  NE2 B GLN C 1 318 ? 30.929  34.186  51.478  0.48 42.85 ? 310  GLN C NE2 1 
ATOM   11841 N  N   . TYR C 1 319 ? 28.145  35.203  57.629  1.00 21.15 ? 311  TYR C N   1 
ATOM   11842 C  CA  . TYR C 1 319 ? 27.040  35.147  58.581  1.00 25.40 ? 311  TYR C CA  1 
ATOM   11843 C  C   . TYR C 1 319 ? 27.006  36.386  59.467  1.00 26.31 ? 311  TYR C C   1 
ATOM   11844 O  O   . TYR C 1 319 ? 25.944  36.984  59.678  1.00 29.46 ? 311  TYR C O   1 
ATOM   11845 C  CB  . TYR C 1 319 ? 27.185  33.871  59.416  1.00 24.66 ? 311  TYR C CB  1 
ATOM   11846 C  CG  . TYR C 1 319 ? 26.112  33.597  60.447  1.00 21.43 ? 311  TYR C CG  1 
ATOM   11847 C  CD1 . TYR C 1 319 ? 26.185  34.159  61.711  1.00 21.05 ? 311  TYR C CD1 1 
ATOM   11848 C  CD2 . TYR C 1 319 ? 25.052  32.734  60.169  1.00 18.19 ? 311  TYR C CD2 1 
ATOM   11849 C  CE1 . TYR C 1 319 ? 25.232  33.906  62.659  1.00 18.34 ? 311  TYR C CE1 1 
ATOM   11850 C  CE2 . TYR C 1 319 ? 24.077  32.465  61.128  1.00 18.05 ? 311  TYR C CE2 1 
ATOM   11851 C  CZ  . TYR C 1 319 ? 24.182  33.059  62.372  1.00 26.45 ? 311  TYR C CZ  1 
ATOM   11852 O  OH  . TYR C 1 319 ? 23.251  32.813  63.357  1.00 22.10 ? 311  TYR C OH  1 
ATOM   11853 N  N   . GLN C 1 320 ? 28.165  36.790  59.995  1.00 24.22 ? 312  GLN C N   1 
ATOM   11854 C  CA  . GLN C 1 320 ? 28.219  37.957  60.871  1.00 24.66 ? 312  GLN C CA  1 
ATOM   11855 C  C   . GLN C 1 320 ? 27.750  39.217  60.154  1.00 30.30 ? 312  GLN C C   1 
ATOM   11856 O  O   . GLN C 1 320 ? 27.057  40.057  60.744  1.00 32.55 ? 312  GLN C O   1 
ATOM   11857 C  CB  . GLN C 1 320 ? 29.641  38.149  61.407  1.00 23.24 ? 312  GLN C CB  1 
ATOM   11858 N  N   . ALA C 1 321 ? 28.120  39.366  58.878  1.00 25.13 ? 313  ALA C N   1 
ATOM   11859 C  CA  . ALA C 1 321 ? 27.726  40.548  58.120  1.00 26.68 ? 313  ALA C CA  1 
ATOM   11860 C  C   . ALA C 1 321 ? 26.209  40.680  58.050  1.00 30.44 ? 313  ALA C C   1 
ATOM   11861 O  O   . ALA C 1 321 ? 25.672  41.791  58.116  1.00 33.86 ? 313  ALA C O   1 
ATOM   11862 C  CB  . ALA C 1 321 ? 28.330  40.494  56.714  1.00 28.17 ? 313  ALA C CB  1 
ATOM   11863 N  N   . LYS C 1 322 ? 25.501  39.558  57.938  1.00 24.60 ? 314  LYS C N   1 
ATOM   11864 C  CA  . LYS C 1 322 ? 24.047  39.577  57.842  1.00 28.73 ? 314  LYS C CA  1 
ATOM   11865 C  C   . LYS C 1 322 ? 23.359  39.445  59.193  1.00 29.54 ? 314  LYS C C   1 
ATOM   11866 O  O   . LYS C 1 322 ? 22.277  40.016  59.384  1.00 28.67 ? 314  LYS C O   1 
ATOM   11867 C  CB  . LYS C 1 322 ? 23.565  38.455  56.915  1.00 30.01 ? 314  LYS C CB  1 
ATOM   11868 N  N   . TYR C 1 323 ? 23.956  38.711  60.136  1.00 25.60 ? 315  TYR C N   1 
ATOM   11869 C  CA  . TYR C 1 323 ? 23.363  38.462  61.451  1.00 21.83 ? 315  TYR C CA  1 
ATOM   11870 C  C   . TYR C 1 323 ? 24.375  38.804  62.539  1.00 25.00 ? 315  TYR C C   1 
ATOM   11871 O  O   . TYR C 1 323 ? 24.860  37.918  63.252  1.00 27.35 ? 315  TYR C O   1 
ATOM   11872 C  CB  . TYR C 1 323 ? 22.900  37.005  61.570  1.00 24.19 ? 315  TYR C CB  1 
ATOM   11873 C  CG  . TYR C 1 323 ? 21.951  36.597  60.465  1.00 23.10 ? 315  TYR C CG  1 
ATOM   11874 C  CD1 . TYR C 1 323 ? 20.615  36.983  60.500  1.00 28.95 ? 315  TYR C CD1 1 
ATOM   11875 C  CD2 . TYR C 1 323 ? 22.391  35.854  59.373  1.00 23.21 ? 315  TYR C CD2 1 
ATOM   11876 C  CE1 . TYR C 1 323 ? 19.741  36.636  59.488  1.00 29.46 ? 315  TYR C CE1 1 
ATOM   11877 C  CE2 . TYR C 1 323 ? 21.514  35.500  58.344  1.00 23.15 ? 315  TYR C CE2 1 
ATOM   11878 C  CZ  . TYR C 1 323 ? 20.191  35.897  58.412  1.00 32.23 ? 315  TYR C CZ  1 
ATOM   11879 O  OH  . TYR C 1 323 ? 19.304  35.570  57.412  1.00 32.38 ? 315  TYR C OH  1 
ATOM   11880 N  N   . PRO C 1 324 ? 24.715  40.089  62.700  1.00 26.25 ? 316  PRO C N   1 
ATOM   11881 C  CA  . PRO C 1 324 ? 25.754  40.440  63.680  1.00 23.45 ? 316  PRO C CA  1 
ATOM   11882 C  C   . PRO C 1 324 ? 25.345  40.170  65.121  1.00 25.36 ? 316  PRO C C   1 
ATOM   11883 O  O   . PRO C 1 324 ? 26.198  39.771  65.924  1.00 24.18 ? 316  PRO C O   1 
ATOM   11884 C  CB  . PRO C 1 324 ? 25.992  41.934  63.420  1.00 27.57 ? 316  PRO C CB  1 
ATOM   11885 C  CG  . PRO C 1 324 ? 24.728  42.415  62.821  1.00 28.12 ? 316  PRO C CG  1 
ATOM   11886 C  CD  . PRO C 1 324 ? 24.208  41.278  61.992  1.00 29.51 ? 316  PRO C CD  1 
ATOM   11887 N  N   . ALA C 1 325 ? 24.071  40.349  65.475  1.00 28.63 ? 317  ALA C N   1 
ATOM   11888 C  CA  . ALA C 1 325 ? 23.657  40.055  66.843  1.00 27.88 ? 317  ALA C CA  1 
ATOM   11889 C  C   . ALA C 1 325 ? 23.768  38.563  67.133  1.00 25.34 ? 317  ALA C C   1 
ATOM   11890 O  O   . ALA C 1 325 ? 24.334  38.159  68.157  1.00 23.54 ? 317  ALA C O   1 
ATOM   11891 C  CB  . ALA C 1 325 ? 22.231  40.552  67.086  1.00 25.37 ? 317  ALA C CB  1 
ATOM   11892 N  N   . GLU C 1 326 ? 23.240  37.726  66.235  1.00 17.90 ? 318  GLU C N   1 
ATOM   11893 C  CA  . GLU C 1 326 ? 23.331  36.283  66.426  1.00 25.94 ? 318  GLU C CA  1 
ATOM   11894 C  C   . GLU C 1 326 ? 24.781  35.819  66.408  1.00 20.10 ? 318  GLU C C   1 
ATOM   11895 O  O   . GLU C 1 326 ? 25.157  34.900  67.148  1.00 17.70 ? 318  GLU C O   1 
ATOM   11896 C  CB  . GLU C 1 326 ? 22.525  35.556  65.349  1.00 29.31 ? 318  GLU C CB  1 
ATOM   11897 C  CG  . GLU C 1 326 ? 21.016  35.733  65.453  1.00 29.88 ? 318  GLU C CG  1 
ATOM   11898 C  CD  . GLU C 1 326 ? 20.499  36.975  64.746  1.00 33.95 ? 318  GLU C CD  1 
ATOM   11899 O  OE1 . GLU C 1 326 ? 21.312  37.846  64.365  1.00 35.85 ? 318  GLU C OE1 1 
ATOM   11900 O  OE2 . GLU C 1 326 ? 19.264  37.074  64.565  1.00 39.56 ? 318  GLU C OE2 1 
ATOM   11901 N  N   . ALA C 1 327 ? 25.612  36.448  65.567  1.00 20.79 ? 319  ALA C N   1 
ATOM   11902 C  CA  . ALA C 1 327 ? 27.020  36.070  65.508  1.00 20.57 ? 319  ALA C CA  1 
ATOM   11903 C  C   . ALA C 1 327 ? 27.717  36.376  66.825  1.00 22.21 ? 319  ALA C C   1 
ATOM   11904 O  O   . ALA C 1 327 ? 28.504  35.566  67.326  1.00 20.60 ? 319  ALA C O   1 
ATOM   11905 C  CB  . ALA C 1 327 ? 27.705  36.786  64.344  1.00 17.95 ? 319  ALA C CB  1 
ATOM   11906 N  N   . ALA C 1 328 ? 27.421  37.531  67.417  1.00 19.84 ? 320  ALA C N   1 
ATOM   11907 C  CA  . ALA C 1 328 ? 28.049  37.870  68.690  1.00 19.54 ? 320  ALA C CA  1 
ATOM   11908 C  C   . ALA C 1 328 ? 27.585  36.931  69.798  1.00 24.27 ? 320  ALA C C   1 
ATOM   11909 O  O   . ALA C 1 328 ? 28.382  36.536  70.661  1.00 21.87 ? 320  ALA C O   1 
ATOM   11910 C  CB  . ALA C 1 328 ? 27.756  39.325  69.046  1.00 21.11 ? 320  ALA C CB  1 
ATOM   11911 N  N   . GLU C 1 329 ? 26.304  36.545  69.777  1.00 18.83 ? 321  GLU C N   1 
ATOM   11912 C  CA  . GLU C 1 329 ? 25.796  35.587  70.755  1.00 19.08 ? 321  GLU C CA  1 
ATOM   11913 C  C   . GLU C 1 329 ? 26.449  34.218  70.592  1.00 19.84 ? 321  GLU C C   1 
ATOM   11914 O  O   . GLU C 1 329 ? 26.767  33.553  71.587  1.00 15.36 ? 321  GLU C O   1 
ATOM   11915 C  CB  . GLU C 1 329 ? 24.275  35.481  70.634  1.00 18.61 ? 321  GLU C CB  1 
ATOM   11916 C  CG  . GLU C 1 329 ? 23.564  36.596  71.376  1.00 15.45 ? 321  GLU C CG  1 
ATOM   11917 C  CD  . GLU C 1 329 ? 23.760  36.491  72.880  1.00 20.66 ? 321  GLU C CD  1 
ATOM   11918 O  OE1 . GLU C 1 329 ? 23.058  35.674  73.500  1.00 22.30 ? 321  GLU C OE1 1 
ATOM   11919 O  OE2 . GLU C 1 329 ? 24.629  37.195  73.439  1.00 18.64 ? 321  GLU C OE2 1 
ATOM   11920 N  N   . PHE C 1 330 ? 26.647  33.781  69.346  1.00 16.80 ? 322  PHE C N   1 
ATOM   11921 C  CA  . PHE C 1 330 ? 27.295  32.497  69.093  1.00 16.80 ? 322  PHE C CA  1 
ATOM   11922 C  C   . PHE C 1 330 ? 28.702  32.473  69.676  1.00 17.41 ? 322  PHE C C   1 
ATOM   11923 O  O   . PHE C 1 330 ? 29.098  31.504  70.336  1.00 18.75 ? 322  PHE C O   1 
ATOM   11924 C  CB  . PHE C 1 330 ? 27.325  32.219  67.582  1.00 19.74 ? 322  PHE C CB  1 
ATOM   11925 C  CG  . PHE C 1 330 ? 27.897  30.875  67.228  1.00 19.16 ? 322  PHE C CG  1 
ATOM   11926 C  CD1 . PHE C 1 330 ? 27.175  29.723  67.462  1.00 18.74 ? 322  PHE C CD1 1 
ATOM   11927 C  CD2 . PHE C 1 330 ? 29.161  30.766  66.670  1.00 18.06 ? 322  PHE C CD2 1 
ATOM   11928 C  CE1 . PHE C 1 330 ? 27.710  28.476  67.151  1.00 20.78 ? 322  PHE C CE1 1 
ATOM   11929 C  CE2 . PHE C 1 330 ? 29.691  29.530  66.356  1.00 17.30 ? 322  PHE C CE2 1 
ATOM   11930 C  CZ  . PHE C 1 330 ? 28.966  28.389  66.596  1.00 18.16 ? 322  PHE C CZ  1 
ATOM   11931 N  N   . VAL C 1 331 ? 29.472  33.538  69.436  1.00 18.02 ? 323  VAL C N   1 
ATOM   11932 C  CA  . VAL C 1 331 ? 30.827  33.630  69.976  1.00 17.60 ? 323  VAL C CA  1 
ATOM   11933 C  C   . VAL C 1 331 ? 30.796  33.600  71.498  1.00 17.57 ? 323  VAL C C   1 
ATOM   11934 O  O   . VAL C 1 331 ? 31.540  32.847  72.140  1.00 17.73 ? 323  VAL C O   1 
ATOM   11935 C  CB  . VAL C 1 331 ? 31.518  34.902  69.458  1.00 19.50 ? 323  VAL C CB  1 
ATOM   11936 C  CG1 . VAL C 1 331 ? 32.797  35.179  70.242  1.00 16.46 ? 323  VAL C CG1 1 
ATOM   11937 C  CG2 . VAL C 1 331 ? 31.816  34.770  67.970  1.00 22.59 ? 323  VAL C CG2 1 
ATOM   11938 N  N   . ARG C 1 332 ? 29.939  34.426  72.099  1.00 15.99 ? 324  ARG C N   1 
ATOM   11939 C  CA  . ARG C 1 332 ? 29.846  34.460  73.558  1.00 16.78 ? 324  ARG C CA  1 
ATOM   11940 C  C   . ARG C 1 332 ? 29.536  33.080  74.129  1.00 19.55 ? 324  ARG C C   1 
ATOM   11941 O  O   . ARG C 1 332 ? 30.193  32.616  75.071  1.00 15.27 ? 324  ARG C O   1 
ATOM   11942 C  CB  . ARG C 1 332 ? 28.773  35.470  73.987  1.00 13.94 ? 324  ARG C CB  1 
ATOM   11943 C  CG  . ARG C 1 332 ? 28.544  35.486  75.496  1.00 13.56 ? 324  ARG C CG  1 
ATOM   11944 C  CD  . ARG C 1 332 ? 27.362  36.351  75.882  1.00 17.64 ? 324  ARG C CD  1 
ATOM   11945 N  NE  . ARG C 1 332 ? 26.053  35.797  75.511  1.00 14.74 ? 324  ARG C NE  1 
ATOM   11946 C  CZ  . ARG C 1 332 ? 25.422  34.833  76.179  1.00 16.91 ? 324  ARG C CZ  1 
ATOM   11947 N  NH1 . ARG C 1 332 ? 25.998  34.261  77.233  1.00 15.27 ? 324  ARG C NH1 1 
ATOM   11948 N  NH2 . ARG C 1 332 ? 24.216  34.424  75.785  1.00 13.50 ? 324  ARG C NH2 1 
ATOM   11949 N  N   . ARG C 1 333 ? 28.537  32.403  73.562  1.00 14.00 ? 325  ARG C N   1 
ATOM   11950 C  CA  . ARG C 1 333 ? 28.090  31.133  74.116  1.00 13.75 ? 325  ARG C CA  1 
ATOM   11951 C  C   . ARG C 1 333 ? 29.086  30.011  73.841  1.00 15.95 ? 325  ARG C C   1 
ATOM   11952 O  O   . ARG C 1 333 ? 29.314  29.154  74.705  1.00 16.43 ? 325  ARG C O   1 
ATOM   11953 C  CB  . ARG C 1 333 ? 26.707  30.796  73.563  1.00 13.82 ? 325  ARG C CB  1 
ATOM   11954 C  CG  . ARG C 1 333 ? 25.648  31.735  74.111  1.00 16.67 ? 325  ARG C CG  1 
ATOM   11955 C  CD  . ARG C 1 333 ? 24.335  31.625  73.348  1.00 18.44 ? 325  ARG C CD  1 
ATOM   11956 N  NE  . ARG C 1 333 ? 23.917  30.240  73.192  1.00 19.57 ? 325  ARG C NE  1 
ATOM   11957 C  CZ  . ARG C 1 333 ? 22.761  29.869  72.652  1.00 21.79 ? 325  ARG C CZ  1 
ATOM   11958 N  NH1 . ARG C 1 333 ? 21.899  30.790  72.223  1.00 12.83 ? 325  ARG C NH1 1 
ATOM   11959 N  NH2 . ARG C 1 333 ? 22.476  28.577  72.535  1.00 15.52 ? 325  ARG C NH2 1 
ATOM   11960 N  N   . MET C 1 334 ? 29.684  29.987  72.650  1.00 15.15 ? 326  MET C N   1 
ATOM   11961 C  CA  . MET C 1 334 ? 30.727  28.997  72.396  1.00 14.20 ? 326  MET C CA  1 
ATOM   11962 C  C   . MET C 1 334 ? 31.932  29.210  73.307  1.00 17.98 ? 326  MET C C   1 
ATOM   11963 O  O   . MET C 1 334 ? 32.585  28.237  73.703  1.00 19.21 ? 326  MET C O   1 
ATOM   11964 C  CB  . MET C 1 334 ? 31.175  29.033  70.935  1.00 14.93 ? 326  MET C CB  1 
ATOM   11965 C  CG  . MET C 1 334 ? 30.188  28.425  69.931  1.00 15.93 ? 326  MET C CG  1 
ATOM   11966 S  SD  . MET C 1 334 ? 29.609  26.757  70.355  1.00 16.45 ? 326  MET C SD  1 
ATOM   11967 C  CE  . MET C 1 334 ? 31.134  25.805  70.337  1.00 15.00 ? 326  MET C CE  1 
ATOM   11968 N  N   . ASP C 1 335 ? 32.246  30.466  73.644  1.00 16.92 ? 327  ASP C N   1 
ATOM   11969 C  CA  . ASP C 1 335 ? 33.330  30.755  74.576  1.00 16.35 ? 327  ASP C CA  1 
ATOM   11970 C  C   . ASP C 1 335 ? 32.929  30.526  76.018  1.00 20.37 ? 327  ASP C C   1 
ATOM   11971 O  O   . ASP C 1 335 ? 33.746  30.781  76.908  1.00 22.54 ? 327  ASP C O   1 
ATOM   11972 C  CB  . ASP C 1 335 ? 33.816  32.199  74.431  1.00 19.44 ? 327  ASP C CB  1 
ATOM   11973 C  CG  . ASP C 1 335 ? 34.591  32.433  73.150  1.00 25.83 ? 327  ASP C CG  1 
ATOM   11974 O  OD1 . ASP C 1 335 ? 34.909  31.447  72.450  1.00 25.38 ? 327  ASP C OD1 1 
ATOM   11975 O  OD2 . ASP C 1 335 ? 34.876  33.613  72.851  1.00 22.42 ? 327  ASP C OD2 1 
ATOM   11976 N  N   . LYS C 1 336 ? 31.691  30.095  76.261  1.00 17.29 ? 328  LYS C N   1 
ATOM   11977 C  CA  . LYS C 1 336 ? 31.237  29.690  77.590  1.00 20.58 ? 328  LYS C CA  1 
ATOM   11978 C  C   . LYS C 1 336 ? 31.247  30.870  78.560  1.00 26.05 ? 328  LYS C C   1 
ATOM   11979 O  O   . LYS C 1 336 ? 31.589  30.725  79.733  1.00 25.38 ? 328  LYS C O   1 
ATOM   11980 C  CB  . LYS C 1 336 ? 32.073  28.512  78.115  1.00 18.19 ? 328  LYS C CB  1 
ATOM   11981 C  CG  . LYS C 1 336 ? 32.095  27.309  77.137  1.00 16.66 ? 328  LYS C CG  1 
ATOM   11982 C  CD  . LYS C 1 336 ? 32.976  26.157  77.629  1.00 21.29 ? 328  LYS C CD  1 
ATOM   11983 C  CE  . LYS C 1 336 ? 32.869  24.922  76.704  1.00 19.54 ? 328  LYS C CE  1 
ATOM   11984 N  NZ  . LYS C 1 336 ? 33.813  23.792  77.086  1.00 14.13 ? 328  LYS C NZ  1 
ATOM   11985 N  N   . LYS C 1 337 ? 30.861  32.047  78.056  1.00 19.71 ? 329  LYS C N   1 
ATOM   11986 C  CA  . LYS C 1 337 ? 30.772  33.284  78.822  1.00 22.03 ? 329  LYS C CA  1 
ATOM   11987 C  C   . LYS C 1 337 ? 29.317  33.684  79.043  1.00 18.34 ? 329  LYS C C   1 
ATOM   11988 O  O   . LYS C 1 337 ? 28.460  33.467  78.182  1.00 18.29 ? 329  LYS C O   1 
ATOM   11989 C  CB  . LYS C 1 337 ? 31.487  34.434  78.100  1.00 21.78 ? 329  LYS C CB  1 
ATOM   11990 C  CG  . LYS C 1 337 ? 32.987  34.257  77.931  1.00 27.52 ? 329  LYS C CG  1 
ATOM   11991 C  CD  . LYS C 1 337 ? 33.580  35.495  77.278  1.00 24.94 ? 329  LYS C CD  1 
ATOM   11992 C  CE  . LYS C 1 337 ? 35.038  35.293  76.897  1.00 26.64 ? 329  LYS C CE  1 
ATOM   11993 N  NZ  . LYS C 1 337 ? 35.536  36.417  76.060  1.00 26.83 ? 329  LYS C NZ  1 
ATOM   11994 N  N   . LEU C 1 338 ? 29.053  34.310  80.196  1.00 23.88 ? 330  LEU C N   1 
ATOM   11995 C  CA  . LEU C 1 338 ? 27.742  34.865  80.512  1.00 15.75 ? 330  LEU C CA  1 
ATOM   11996 C  C   . LEU C 1 338 ? 27.550  36.231  79.861  1.00 18.18 ? 330  LEU C C   1 
ATOM   11997 O  O   . LEU C 1 338 ? 28.519  36.881  79.464  1.00 19.89 ? 330  LEU C O   1 
ATOM   11998 C  CB  . LEU C 1 338 ? 27.583  35.000  82.026  1.00 15.63 ? 330  LEU C CB  1 
ATOM   11999 C  CG  . LEU C 1 338 ? 27.432  33.683  82.799  1.00 22.53 ? 330  LEU C CG  1 
ATOM   12000 C  CD1 . LEU C 1 338 ? 27.251  33.981  84.269  1.00 23.23 ? 330  LEU C CD1 1 
ATOM   12001 C  CD2 . LEU C 1 338 ? 26.258  32.883  82.269  1.00 27.15 ? 330  LEU C CD2 1 
ATOM   12002 N  N   . PRO C 1 339 ? 26.302  36.702  79.761  1.00 19.04 ? 331  PRO C N   1 
ATOM   12003 C  CA  . PRO C 1 339 ? 26.072  38.072  79.293  1.00 20.46 ? 331  PRO C CA  1 
ATOM   12004 C  C   . PRO C 1 339 ? 26.747  39.069  80.219  1.00 24.99 ? 331  PRO C C   1 
ATOM   12005 O  O   . PRO C 1 339 ? 26.938  38.802  81.407  1.00 21.43 ? 331  PRO C O   1 
ATOM   12006 C  CB  . PRO C 1 339 ? 24.546  38.214  79.332  1.00 19.05 ? 331  PRO C CB  1 
ATOM   12007 C  CG  . PRO C 1 339 ? 24.031  36.818  79.280  1.00 19.64 ? 331  PRO C CG  1 
ATOM   12008 C  CD  . PRO C 1 339 ? 25.039  35.992  80.027  1.00 17.29 ? 331  PRO C CD  1 
ATOM   12009 N  N   . GLU C 1 340 ? 27.110  40.228  79.657  1.00 22.74 ? 332  GLU C N   1 
ATOM   12010 C  CA  . GLU C 1 340 ? 27.871  41.219  80.417  1.00 26.25 ? 332  GLU C CA  1 
ATOM   12011 C  C   . GLU C 1 340 ? 27.072  41.781  81.590  1.00 24.78 ? 332  GLU C C   1 
ATOM   12012 O  O   . GLU C 1 340 ? 27.650  42.114  82.631  1.00 30.53 ? 332  GLU C O   1 
ATOM   12013 C  CB  . GLU C 1 340 ? 28.326  42.356  79.492  1.00 27.94 ? 332  GLU C CB  1 
ATOM   12014 N  N   . ASN C 1 341 ? 25.753  41.884  81.453  1.00 19.43 ? 333  ASN C N   1 
ATOM   12015 C  CA  . ASN C 1 341 ? 24.909  42.450  82.499  1.00 21.93 ? 333  ASN C CA  1 
ATOM   12016 C  C   . ASN C 1 341 ? 24.358  41.405  83.479  1.00 18.45 ? 333  ASN C C   1 
ATOM   12017 O  O   . ASN C 1 341 ? 23.405  41.706  84.206  1.00 24.07 ? 333  ASN C O   1 
ATOM   12018 C  CB  . ASN C 1 341 ? 23.743  43.212  81.866  1.00 34.94 ? 333  ASN C CB  1 
ATOM   12019 C  CG  . ASN C 1 341 ? 22.689  42.277  81.273  1.00 39.06 ? 333  ASN C CG  1 
ATOM   12020 O  OD1 . ASN C 1 341 ? 23.002  41.166  80.845  1.00 33.46 ? 333  ASN C OD1 1 
ATOM   12021 N  ND2 . ASN C 1 341 ? 21.433  42.722  81.263  1.00 45.33 ? 333  ASN C ND2 1 
ATOM   12022 N  N   . PHE C 1 342 ? 24.922  40.195  83.519  1.00 15.31 ? 334  PHE C N   1 
ATOM   12023 C  CA  . PHE C 1 342 ? 24.295  39.116  84.285  1.00 16.56 ? 334  PHE C CA  1 
ATOM   12024 C  C   . PHE C 1 342 ? 24.119  39.486  85.755  1.00 17.70 ? 334  PHE C C   1 
ATOM   12025 O  O   . PHE C 1 342 ? 23.026  39.334  86.317  1.00 15.12 ? 334  PHE C O   1 
ATOM   12026 C  CB  . PHE C 1 342 ? 25.115  37.830  84.163  1.00 18.78 ? 334  PHE C CB  1 
ATOM   12027 C  CG  . PHE C 1 342 ? 24.447  36.632  84.769  1.00 20.08 ? 334  PHE C CG  1 
ATOM   12028 C  CD1 . PHE C 1 342 ? 23.370  36.033  84.138  1.00 18.16 ? 334  PHE C CD1 1 
ATOM   12029 C  CD2 . PHE C 1 342 ? 24.888  36.104  85.972  1.00 18.82 ? 334  PHE C CD2 1 
ATOM   12030 C  CE1 . PHE C 1 342 ? 22.737  34.926  84.698  1.00 20.58 ? 334  PHE C CE1 1 
ATOM   12031 C  CE2 . PHE C 1 342 ? 24.258  35.003  86.540  1.00 17.73 ? 334  PHE C CE2 1 
ATOM   12032 C  CZ  . PHE C 1 342 ? 23.188  34.412  85.899  1.00 20.68 ? 334  PHE C CZ  1 
ATOM   12033 N  N   . ASP C 1 343 ? 25.196  39.936  86.408  1.00 20.07 ? 335  ASP C N   1 
ATOM   12034 C  CA  . ASP C 1 343 ? 25.131  40.220  87.841  1.00 21.30 ? 335  ASP C CA  1 
ATOM   12035 C  C   . ASP C 1 343 ? 24.124  41.323  88.139  1.00 22.59 ? 335  ASP C C   1 
ATOM   12036 O  O   . ASP C 1 343 ? 23.343  41.227  89.094  1.00 22.97 ? 335  ASP C O   1 
ATOM   12037 C  CB  . ASP C 1 343 ? 26.518  40.612  88.361  1.00 25.23 ? 335  ASP C CB  1 
ATOM   12038 C  CG  . ASP C 1 343 ? 27.470  39.436  88.413  1.00 25.84 ? 335  ASP C CG  1 
ATOM   12039 O  OD1 . ASP C 1 343 ? 27.017  38.339  88.769  1.00 26.50 ? 335  ASP C OD1 1 
ATOM   12040 O  OD2 . ASP C 1 343 ? 28.665  39.600  88.099  1.00 30.91 ? 335  ASP C OD2 1 
ATOM   12041 N  N   . GLU C 1 344 ? 24.132  42.376  87.326  1.00 15.93 ? 336  GLU C N   1 
ATOM   12042 C  CA  . GLU C 1 344 ? 23.178  43.462  87.489  1.00 21.29 ? 336  GLU C CA  1 
ATOM   12043 C  C   . GLU C 1 344 ? 21.750  42.959  87.307  1.00 20.75 ? 336  GLU C C   1 
ATOM   12044 O  O   . GLU C 1 344 ? 20.861  43.278  88.107  1.00 20.16 ? 336  GLU C O   1 
ATOM   12045 C  CB  . GLU C 1 344 ? 23.516  44.568  86.492  1.00 26.70 ? 336  GLU C CB  1 
ATOM   12046 C  CG  . GLU C 1 344 ? 22.782  45.867  86.690  1.00 41.17 ? 336  GLU C CG  1 
ATOM   12047 C  CD  . GLU C 1 344 ? 23.261  46.927  85.720  1.00 47.84 ? 336  GLU C CD  1 
ATOM   12048 O  OE1 . GLU C 1 344 ? 23.960  46.555  84.750  1.00 49.26 ? 336  GLU C OE1 1 
ATOM   12049 O  OE2 . GLU C 1 344 ? 22.950  48.121  85.927  1.00 46.73 ? 336  GLU C OE2 1 
ATOM   12050 N  N   . TYR C 1 345 ? 21.519  42.153  86.261  1.00 18.29 ? 337  TYR C N   1 
ATOM   12051 C  CA  . TYR C 1 345 ? 20.206  41.548  86.043  1.00 16.93 ? 337  TYR C CA  1 
ATOM   12052 C  C   . TYR C 1 345 ? 19.764  40.718  87.248  1.00 17.55 ? 337  TYR C C   1 
ATOM   12053 O  O   . TYR C 1 345 ? 18.613  40.814  87.705  1.00 17.22 ? 337  TYR C O   1 
ATOM   12054 C  CB  . TYR C 1 345 ? 20.233  40.680  84.780  1.00 18.42 ? 337  TYR C CB  1 
ATOM   12055 C  CG  . TYR C 1 345 ? 18.939  39.919  84.557  1.00 20.07 ? 337  TYR C CG  1 
ATOM   12056 C  CD1 . TYR C 1 345 ? 17.858  40.522  83.912  1.00 23.94 ? 337  TYR C CD1 1 
ATOM   12057 C  CD2 . TYR C 1 345 ? 18.788  38.610  85.012  1.00 20.21 ? 337  TYR C CD2 1 
ATOM   12058 C  CE1 . TYR C 1 345 ? 16.659  39.834  83.719  1.00 24.23 ? 337  TYR C CE1 1 
ATOM   12059 C  CE2 . TYR C 1 345 ? 17.597  37.916  84.826  1.00 19.01 ? 337  TYR C CE2 1 
ATOM   12060 C  CZ  . TYR C 1 345 ? 16.538  38.532  84.180  1.00 21.07 ? 337  TYR C CZ  1 
ATOM   12061 O  OH  . TYR C 1 345 ? 15.357  37.839  84.004  1.00 22.39 ? 337  TYR C OH  1 
ATOM   12062 N  N   . VAL C 1 346 ? 20.656  39.880  87.770  1.00 15.37 ? 338  VAL C N   1 
ATOM   12063 C  CA  . VAL C 1 346 ? 20.281  39.069  88.926  1.00 16.53 ? 338  VAL C CA  1 
ATOM   12064 C  C   . VAL C 1 346 ? 19.961  39.953  90.127  1.00 16.93 ? 338  VAL C C   1 
ATOM   12065 O  O   . VAL C 1 346 ? 18.975  39.717  90.841  1.00 18.43 ? 338  VAL C O   1 
ATOM   12066 C  CB  . VAL C 1 346 ? 21.379  38.041  89.237  1.00 14.83 ? 338  VAL C CB  1 
ATOM   12067 C  CG1 . VAL C 1 346 ? 21.127  37.375  90.585  1.00 16.68 ? 338  VAL C CG1 1 
ATOM   12068 C  CG2 . VAL C 1 346 ? 21.406  36.983  88.147  1.00 13.61 ? 338  VAL C CG2 1 
ATOM   12069 N  N   . GLN C 1 347 ? 20.780  40.982  90.376  1.00 19.70 ? 339  GLN C N   1 
ATOM   12070 C  CA  . GLN C 1 347 ? 20.572  41.814  91.559  1.00 23.12 ? 339  GLN C CA  1 
ATOM   12071 C  C   . GLN C 1 347 ? 19.221  42.518  91.505  1.00 24.66 ? 339  GLN C C   1 
ATOM   12072 O  O   . GLN C 1 347 ? 18.529  42.638  92.524  1.00 23.96 ? 339  GLN C O   1 
ATOM   12073 C  CB  . GLN C 1 347 ? 21.702  42.839  91.695  1.00 25.69 ? 339  GLN C CB  1 
ATOM   12074 N  N   . THR C 1 348 ? 18.830  42.986  90.321  1.00 18.10 ? 340  THR C N   1 
ATOM   12075 C  CA  . THR C 1 348 ? 17.536  43.644  90.169  1.00 22.02 ? 340  THR C CA  1 
ATOM   12076 C  C   . THR C 1 348 ? 16.394  42.651  90.325  1.00 23.35 ? 340  THR C C   1 
ATOM   12077 O  O   . THR C 1 348 ? 15.392  42.945  90.988  1.00 22.29 ? 340  THR C O   1 
ATOM   12078 C  CB  . THR C 1 348 ? 17.473  44.332  88.808  1.00 27.54 ? 340  THR C CB  1 
ATOM   12079 O  OG1 . THR C 1 348 ? 18.494  45.335  88.751  1.00 33.11 ? 340  THR C OG1 1 
ATOM   12080 C  CG2 . THR C 1 348 ? 16.110  44.977  88.595  1.00 30.23 ? 340  THR C CG2 1 
ATOM   12081 N  N   . ALA C 1 349 ? 16.542  41.458  89.740  1.00 20.97 ? 341  ALA C N   1 
ATOM   12082 C  CA  . ALA C 1 349 ? 15.511  40.433  89.847  1.00 16.38 ? 341  ALA C CA  1 
ATOM   12083 C  C   . ALA C 1 349 ? 15.325  39.970  91.283  1.00 19.11 ? 341  ALA C C   1 
ATOM   12084 O  O   . ALA C 1 349 ? 14.202  39.652  91.698  1.00 22.64 ? 341  ALA C O   1 
ATOM   12085 C  CB  . ALA C 1 349 ? 15.866  39.241  88.957  1.00 17.13 ? 341  ALA C CB  1 
ATOM   12086 N  N   . LEU C 1 350 ? 16.414  39.914  92.047  1.00 17.94 ? 342  LEU C N   1 
ATOM   12087 C  CA  . LEU C 1 350 ? 16.337  39.473  93.431  1.00 19.14 ? 342  LEU C CA  1 
ATOM   12088 C  C   . LEU C 1 350 ? 15.574  40.476  94.283  1.00 23.90 ? 342  LEU C C   1 
ATOM   12089 O  O   . LEU C 1 350 ? 14.778  40.084  95.141  1.00 23.46 ? 342  LEU C O   1 
ATOM   12090 C  CB  . LEU C 1 350 ? 17.747  39.250  93.980  1.00 19.76 ? 342  LEU C CB  1 
ATOM   12091 C  CG  . LEU C 1 350 ? 17.889  38.749  95.418  1.00 22.66 ? 342  LEU C CG  1 
ATOM   12092 C  CD1 . LEU C 1 350 ? 17.107  37.461  95.624  1.00 22.30 ? 342  LEU C CD1 1 
ATOM   12093 C  CD2 . LEU C 1 350 ? 19.355  38.524  95.709  1.00 21.32 ? 342  LEU C CD2 1 
ATOM   12094 N  N   . LYS C 1 351 ? 15.818  41.773  94.073  1.00 21.89 ? 343  LYS C N   1 
ATOM   12095 C  CA  . LYS C 1 351 ? 15.026  42.795  94.753  1.00 24.41 ? 343  LYS C CA  1 
ATOM   12096 C  C   . LYS C 1 351 ? 13.550  42.651  94.418  1.00 26.76 ? 343  LYS C C   1 
ATOM   12097 O  O   . LYS C 1 351 ? 12.690  42.815  95.290  1.00 26.90 ? 343  LYS C O   1 
ATOM   12098 C  CB  . LYS C 1 351 ? 15.509  44.192  94.369  1.00 25.07 ? 343  LYS C CB  1 
ATOM   12099 C  CG  . LYS C 1 351 ? 16.857  44.574  94.947  1.00 30.82 ? 343  LYS C CG  1 
ATOM   12100 C  CD  . LYS C 1 351 ? 17.231  45.977  94.506  1.00 37.13 ? 343  LYS C CD  1 
ATOM   12101 C  CE  . LYS C 1 351 ? 18.655  46.315  94.903  1.00 45.03 ? 343  LYS C CE  1 
ATOM   12102 N  NZ  . LYS C 1 351 ? 19.103  47.598  94.291  1.00 45.96 ? 343  LYS C NZ  1 
ATOM   12103 N  N   . GLU C 1 352 ? 13.237  42.354  93.155  1.00 29.41 ? 344  GLU C N   1 
ATOM   12104 C  CA  . GLU C 1 352 ? 11.846  42.137  92.770  1.00 33.17 ? 344  GLU C CA  1 
ATOM   12105 C  C   . GLU C 1 352 ? 11.276  40.894  93.448  1.00 33.26 ? 344  GLU C C   1 
ATOM   12106 O  O   . GLU C 1 352 ? 10.148  40.918  93.957  1.00 36.73 ? 344  GLU C O   1 
ATOM   12107 C  CB  . GLU C 1 352 ? 11.738  42.027  91.247  1.00 30.36 ? 344  GLU C CB  1 
ATOM   12108 N  N   . VAL C 1 353 ? 12.047  39.805  93.473  1.00 28.16 ? 345  VAL C N   1 
ATOM   12109 C  CA  . VAL C 1 353 ? 11.606  38.588  94.156  1.00 29.18 ? 345  VAL C CA  1 
ATOM   12110 C  C   . VAL C 1 353 ? 11.309  38.882  95.621  1.00 32.78 ? 345  VAL C C   1 
ATOM   12111 O  O   . VAL C 1 353 ? 10.272  38.475  96.159  1.00 35.16 ? 345  VAL C O   1 
ATOM   12112 C  CB  . VAL C 1 353 ? 12.661  37.474  94.017  1.00 22.73 ? 345  VAL C CB  1 
ATOM   12113 C  CG1 . VAL C 1 353 ? 12.426  36.398  95.063  1.00 27.85 ? 345  VAL C CG1 1 
ATOM   12114 C  CG2 . VAL C 1 353 ? 12.618  36.873  92.626  1.00 22.15 ? 345  VAL C CG2 1 
ATOM   12115 N  N   . CYS C 1 354 ? 12.216  39.598  96.286  1.00 27.30 ? 346  CYS C N   1 
ATOM   12116 C  CA  . CYS C 1 354 ? 12.013  39.896  97.698  1.00 32.99 ? 346  CYS C CA  1 
ATOM   12117 C  C   . CYS C 1 354 ? 10.766  40.750  97.905  1.00 36.06 ? 346  CYS C C   1 
ATOM   12118 O  O   . CYS C 1 354 ? 9.997   40.516  98.845  1.00 37.88 ? 346  CYS C O   1 
ATOM   12119 C  CB  . CYS C 1 354 ? 13.252  40.583  98.278  1.00 38.67 ? 346  CYS C CB  1 
ATOM   12120 S  SG  . CYS C 1 354 ? 13.121  40.969  100.056 1.00 46.41 ? 346  CYS C SG  1 
ATOM   12121 N  N   . ALA C 1 355 ? 10.537  41.735  97.028  1.00 35.43 ? 347  ALA C N   1 
ATOM   12122 C  CA  . ALA C 1 355 ? 9.336   42.556  97.146  1.00 42.43 ? 347  ALA C CA  1 
ATOM   12123 C  C   . ALA C 1 355 ? 8.077   41.714  96.976  1.00 46.74 ? 347  ALA C C   1 
ATOM   12124 O  O   . ALA C 1 355 ? 7.112   41.868  97.734  1.00 53.91 ? 347  ALA C O   1 
ATOM   12125 C  CB  . ALA C 1 355 ? 9.368   43.693  96.124  1.00 38.49 ? 347  ALA C CB  1 
ATOM   12126 N  N   . LYS C 1 356 ? 8.075   40.811  96.001  1.00 43.47 ? 348  LYS C N   1 
ATOM   12127 C  CA  . LYS C 1 356 ? 6.942   39.926  95.747  1.00 45.53 ? 348  LYS C CA  1 
ATOM   12128 C  C   . LYS C 1 356 ? 6.615   39.037  96.946  1.00 44.10 ? 348  LYS C C   1 
ATOM   12129 O  O   . LYS C 1 356 ? 7.489   38.367  97.499  1.00 42.98 ? 348  LYS C O   1 
ATOM   12130 C  CB  . LYS C 1 356 ? 7.221   39.056  94.516  1.00 46.43 ? 348  LYS C CB  1 
ATOM   12131 N  N   . ASN C 1 368 ? 9.276   30.994  90.282  1.00 28.30 ? 360  ASN C N   1 
ATOM   12132 C  CA  . ASN C 1 368 ? 10.080  30.271  89.308  1.00 21.61 ? 360  ASN C CA  1 
ATOM   12133 C  C   . ASN C 1 368 ? 11.417  30.997  89.035  1.00 22.87 ? 360  ASN C C   1 
ATOM   12134 O  O   . ASN C 1 368 ? 11.484  31.950  88.254  1.00 22.33 ? 360  ASN C O   1 
ATOM   12135 C  CB  . ASN C 1 368 ? 9.272   30.079  88.015  1.00 27.74 ? 360  ASN C CB  1 
ATOM   12136 C  CG  . ASN C 1 368 ? 9.845   28.984  87.121  1.00 24.19 ? 360  ASN C CG  1 
ATOM   12137 O  OD1 . ASN C 1 368 ? 11.053  28.845  87.002  1.00 27.50 ? 360  ASN C OD1 1 
ATOM   12138 N  ND2 . ASN C 1 368 ? 8.974   28.196  86.507  1.00 24.84 ? 360  ASN C ND2 1 
ATOM   12139 N  N   . SER C 1 369 ? 12.479  30.523  89.696  1.00 16.83 ? 361  SER C N   1 
ATOM   12140 C  CA  . SER C 1 369 ? 13.823  31.036  89.447  1.00 18.13 ? 361  SER C CA  1 
ATOM   12141 C  C   . SER C 1 369 ? 14.274  30.746  88.024  1.00 19.13 ? 361  SER C C   1 
ATOM   12142 O  O   . SER C 1 369 ? 14.961  31.566  87.403  1.00 18.45 ? 361  SER C O   1 
ATOM   12143 C  CB  . SER C 1 369 ? 14.813  30.402  90.424  1.00 22.21 ? 361  SER C CB  1 
ATOM   12144 O  OG  . SER C 1 369 ? 14.379  30.546  91.752  1.00 24.75 ? 361  SER C OG  1 
ATOM   12145 N  N   . ILE C 1 370 ? 13.925  29.564  87.508  1.00 13.87 ? 362  ILE C N   1 
ATOM   12146 C  CA  . ILE C 1 370 ? 14.329  29.182  86.159  1.00 14.08 ? 362  ILE C CA  1 
ATOM   12147 C  C   . ILE C 1 370 ? 13.771  30.161  85.144  1.00 14.03 ? 362  ILE C C   1 
ATOM   12148 O  O   . ILE C 1 370 ? 14.448  30.535  84.176  1.00 15.38 ? 362  ILE C O   1 
ATOM   12149 C  CB  . ILE C 1 370 ? 13.870  27.742  85.854  1.00 19.06 ? 362  ILE C CB  1 
ATOM   12150 C  CG1 . ILE C 1 370 ? 14.513  26.754  86.827  1.00 18.23 ? 362  ILE C CG1 1 
ATOM   12151 C  CG2 . ILE C 1 370 ? 14.175  27.379  84.387  1.00 16.59 ? 362  ILE C CG2 1 
ATOM   12152 C  CD1 . ILE C 1 370 ? 13.811  25.405  86.856  1.00 16.92 ? 362  ILE C CD1 1 
ATOM   12153 N  N   . GLU C 1 371 ? 12.518  30.581  85.343  1.00 18.51 ? 363  GLU C N   1 
ATOM   12154 C  CA  . GLU C 1 371 ? 11.901  31.554  84.449  1.00 15.78 ? 363  GLU C CA  1 
ATOM   12155 C  C   . GLU C 1 371 ? 12.698  32.853  84.426  1.00 19.18 ? 363  GLU C C   1 
ATOM   12156 O  O   . GLU C 1 371 ? 12.919  33.438  83.358  1.00 18.49 ? 363  GLU C O   1 
ATOM   12157 C  CB  . GLU C 1 371 ? 10.455  31.807  84.886  1.00 16.82 ? 363  GLU C CB  1 
ATOM   12158 C  CG  . GLU C 1 371 ? 9.614   32.595  83.893  1.00 20.30 ? 363  GLU C CG  1 
ATOM   12159 C  CD  . GLU C 1 371 ? 9.003   31.708  82.825  1.00 22.15 ? 363  GLU C CD  1 
ATOM   12160 O  OE1 . GLU C 1 371 ? 8.358   30.700  83.191  1.00 20.57 ? 363  GLU C OE1 1 
ATOM   12161 O  OE2 . GLU C 1 371 ? 9.180   32.007  81.622  1.00 23.27 ? 363  GLU C OE2 1 
ATOM   12162 N  N   . ILE C 1 372 ? 13.139  33.312  85.601  1.00 15.22 ? 364  ILE C N   1 
ATOM   12163 C  CA  . ILE C 1 372 ? 13.970  34.509  85.689  1.00 15.28 ? 364  ILE C CA  1 
ATOM   12164 C  C   . ILE C 1 372 ? 15.294  34.291  84.966  1.00 19.32 ? 364  ILE C C   1 
ATOM   12165 O  O   . ILE C 1 372 ? 15.748  35.144  84.196  1.00 20.33 ? 364  ILE C O   1 
ATOM   12166 C  CB  . ILE C 1 372 ? 14.193  34.883  87.165  1.00 15.04 ? 364  ILE C CB  1 
ATOM   12167 C  CG1 . ILE C 1 372 ? 12.855  35.204  87.841  1.00 23.38 ? 364  ILE C CG1 1 
ATOM   12168 C  CG2 . ILE C 1 372 ? 15.162  36.049  87.290  1.00 15.61 ? 364  ILE C CG2 1 
ATOM   12169 C  CD1 . ILE C 1 372 ? 12.953  35.336  89.359  1.00 23.38 ? 364  ILE C CD1 1 
ATOM   12170 N  N   . LEU C 1 373 ? 15.932  33.141  85.200  1.00 17.37 ? 365  LEU C N   1 
ATOM   12171 C  CA  . LEU C 1 373 ? 17.218  32.873  84.552  1.00 21.14 ? 365  LEU C CA  1 
ATOM   12172 C  C   . LEU C 1 373 ? 17.070  32.724  83.041  1.00 19.72 ? 365  LEU C C   1 
ATOM   12173 O  O   . LEU C 1 373 ? 17.894  33.241  82.279  1.00 18.08 ? 365  LEU C O   1 
ATOM   12174 C  CB  . LEU C 1 373 ? 17.861  31.616  85.133  1.00 22.93 ? 365  LEU C CB  1 
ATOM   12175 C  CG  . LEU C 1 373 ? 19.216  31.871  85.782  1.00 32.04 ? 365  LEU C CG  1 
ATOM   12176 C  CD1 . LEU C 1 373 ? 18.991  32.533  87.132  1.00 37.13 ? 365  LEU C CD1 1 
ATOM   12177 C  CD2 . LEU C 1 373 ? 20.004  30.575  85.920  1.00 32.38 ? 365  LEU C CD2 1 
ATOM   12178 N  N   . ALA C 1 374 ? 16.035  32.008  82.590  1.00 15.23 ? 366  ALA C N   1 
ATOM   12179 C  CA  . ALA C 1 374 ? 15.893  31.723  81.164  1.00 16.86 ? 366  ALA C CA  1 
ATOM   12180 C  C   . ALA C 1 374 ? 15.769  33.007  80.352  1.00 23.85 ? 366  ALA C C   1 
ATOM   12181 O  O   . ALA C 1 374 ? 16.242  33.082  79.207  1.00 20.11 ? 366  ALA C O   1 
ATOM   12182 C  CB  . ALA C 1 374 ? 14.688  30.823  80.923  1.00 17.92 ? 366  ALA C CB  1 
ATOM   12183 N  N   . LYS C 1 375 ? 15.130  34.027  80.926  1.00 21.74 ? 367  LYS C N   1 
ATOM   12184 C  CA  . LYS C 1 375 ? 14.960  35.291  80.219  1.00 18.79 ? 367  LYS C CA  1 
ATOM   12185 C  C   . LYS C 1 375 ? 16.307  35.929  79.903  1.00 18.75 ? 367  LYS C C   1 
ATOM   12186 O  O   . LYS C 1 375 ? 16.473  36.563  78.854  1.00 20.31 ? 367  LYS C O   1 
ATOM   12187 C  CB  . LYS C 1 375 ? 14.087  36.207  81.081  1.00 24.39 ? 367  LYS C CB  1 
ATOM   12188 C  CG  . LYS C 1 375 ? 13.452  37.387  80.395  1.00 30.41 ? 367  LYS C CG  1 
ATOM   12189 C  CD  . LYS C 1 375 ? 12.583  38.139  81.410  1.00 32.71 ? 367  LYS C CD  1 
ATOM   12190 C  CE  . LYS C 1 375 ? 12.497  39.622  81.093  1.00 44.63 ? 367  LYS C CE  1 
ATOM   12191 N  NZ  . LYS C 1 375 ? 12.006  40.402  82.266  1.00 48.65 ? 367  LYS C NZ  1 
ATOM   12192 N  N   . GLU C 1 376 ? 17.288  35.738  80.783  1.00 16.09 ? 368  GLU C N   1 
ATOM   12193 C  CA  . GLU C 1 376 ? 18.615  36.322  80.638  1.00 17.39 ? 368  GLU C CA  1 
ATOM   12194 C  C   . GLU C 1 376 ? 19.593  35.402  79.911  1.00 16.99 ? 368  GLU C C   1 
ATOM   12195 O  O   . GLU C 1 376 ? 20.595  35.880  79.358  1.00 19.44 ? 368  GLU C O   1 
ATOM   12196 C  CB  . GLU C 1 376 ? 19.146  36.673  82.039  1.00 23.88 ? 368  GLU C CB  1 
ATOM   12197 C  CG  . GLU C 1 376 ? 20.612  37.061  82.143  1.00 21.67 ? 368  GLU C CG  1 
ATOM   12198 C  CD  . GLU C 1 376 ? 20.908  38.426  81.567  1.00 24.12 ? 368  GLU C CD  1 
ATOM   12199 O  OE1 . GLU C 1 376 ? 19.974  39.121  81.105  1.00 26.40 ? 368  GLU C OE1 1 
ATOM   12200 O  OE2 . GLU C 1 376 ? 22.095  38.809  81.576  1.00 24.75 ? 368  GLU C OE2 1 
ATOM   12201 N  N   . LEU C 1 377 ? 19.321  34.098  79.874  1.00 14.95 ? 369  LEU C N   1 
ATOM   12202 C  CA  . LEU C 1 377 ? 20.278  33.110  79.371  1.00 16.66 ? 369  LEU C CA  1 
ATOM   12203 C  C   . LEU C 1 377 ? 19.661  32.304  78.238  1.00 19.13 ? 369  LEU C C   1 
ATOM   12204 O  O   . LEU C 1 377 ? 19.107  31.215  78.468  1.00 15.03 ? 369  LEU C O   1 
ATOM   12205 C  CB  . LEU C 1 377 ? 20.726  32.181  80.497  1.00 15.35 ? 369  LEU C CB  1 
ATOM   12206 C  CG  . LEU C 1 377 ? 21.492  32.812  81.657  1.00 20.40 ? 369  LEU C CG  1 
ATOM   12207 C  CD1 . LEU C 1 377 ? 21.851  31.742  82.680  1.00 21.61 ? 369  LEU C CD1 1 
ATOM   12208 C  CD2 . LEU C 1 377 ? 22.749  33.520  81.153  1.00 16.01 ? 369  LEU C CD2 1 
ATOM   12209 N  N   . PRO C 1 378 ? 19.748  32.781  76.995  1.00 17.62 ? 370  PRO C N   1 
ATOM   12210 C  CA  . PRO C 1 378 ? 19.212  31.991  75.875  1.00 14.36 ? 370  PRO C CA  1 
ATOM   12211 C  C   . PRO C 1 378 ? 19.972  30.695  75.634  1.00 17.51 ? 370  PRO C C   1 
ATOM   12212 O  O   . PRO C 1 378 ? 19.460  29.820  74.926  1.00 20.39 ? 370  PRO C O   1 
ATOM   12213 C  CB  . PRO C 1 378 ? 19.328  32.949  74.675  1.00 17.02 ? 370  PRO C CB  1 
ATOM   12214 C  CG  . PRO C 1 378 ? 20.392  33.934  75.063  1.00 20.19 ? 370  PRO C CG  1 
ATOM   12215 C  CD  . PRO C 1 378 ? 20.320  34.071  76.562  1.00 14.67 ? 370  PRO C CD  1 
ATOM   12216 N  N   . GLU C 1 379 ? 21.161  30.534  76.213  1.00 15.82 ? 371  GLU C N   1 
ATOM   12217 C  CA  . GLU C 1 379 ? 21.903  29.284  76.150  1.00 16.43 ? 371  GLU C CA  1 
ATOM   12218 C  C   . GLU C 1 379 ? 21.349  28.222  77.094  1.00 16.76 ? 371  GLU C C   1 
ATOM   12219 O  O   . GLU C 1 379 ? 21.852  27.095  77.091  1.00 14.25 ? 371  GLU C O   1 
ATOM   12220 C  CB  . GLU C 1 379 ? 23.381  29.532  76.481  1.00 15.66 ? 371  GLU C CB  1 
ATOM   12221 C  CG  . GLU C 1 379 ? 23.624  30.074  77.883  1.00 11.90 ? 371  GLU C CG  1 
ATOM   12222 C  CD  . GLU C 1 379 ? 23.802  31.584  77.924  1.00 14.13 ? 371  GLU C CD  1 
ATOM   12223 O  OE1 . GLU C 1 379 ? 22.965  32.314  77.349  1.00 15.39 ? 371  GLU C OE1 1 
ATOM   12224 O  OE2 . GLU C 1 379 ? 24.791  32.049  78.530  1.00 15.46 ? 371  GLU C OE2 1 
ATOM   12225 N  N   . LEU C 1 380 ? 20.358  28.557  77.916  1.00 18.36 ? 372  LEU C N   1 
ATOM   12226 C  CA  . LEU C 1 380 ? 19.854  27.608  78.901  1.00 17.09 ? 372  LEU C CA  1 
ATOM   12227 C  C   . LEU C 1 380 ? 19.162  26.437  78.208  1.00 16.36 ? 372  LEU C C   1 
ATOM   12228 O  O   . LEU C 1 380 ? 18.283  26.633  77.364  1.00 16.38 ? 372  LEU C O   1 
ATOM   12229 C  CB  . LEU C 1 380 ? 18.880  28.296  79.862  1.00 13.63 ? 372  LEU C CB  1 
ATOM   12230 C  CG  . LEU C 1 380 ? 18.615  27.543  81.175  1.00 16.93 ? 372  LEU C CG  1 
ATOM   12231 C  CD1 . LEU C 1 380 ? 19.899  27.441  81.985  1.00 17.51 ? 372  LEU C CD1 1 
ATOM   12232 C  CD2 . LEU C 1 380 ? 17.494  28.217  81.981  1.00 17.57 ? 372  LEU C CD2 1 
ATOM   12233 N  N   . VAL C 1 381 ? 19.560  25.222  78.571  1.00 12.15 ? 373  VAL C N   1 
ATOM   12234 C  CA  . VAL C 1 381 ? 18.912  23.996  78.114  1.00 15.98 ? 373  VAL C CA  1 
ATOM   12235 C  C   . VAL C 1 381 ? 18.484  23.208  79.342  1.00 14.99 ? 373  VAL C C   1 
ATOM   12236 O  O   . VAL C 1 381 ? 19.329  22.774  80.131  1.00 17.70 ? 373  VAL C O   1 
ATOM   12237 C  CB  . VAL C 1 381 ? 19.838  23.147  77.233  1.00 16.42 ? 373  VAL C CB  1 
ATOM   12238 C  CG1 . VAL C 1 381 ? 19.151  21.820  76.889  1.00 17.27 ? 373  VAL C CG1 1 
ATOM   12239 C  CG2 . VAL C 1 381 ? 20.230  23.918  75.972  1.00 13.42 ? 373  VAL C CG2 1 
ATOM   12240 N  N   . GLY C 1 382 ? 17.176  23.000  79.495  1.00 14.08 ? 374  GLY C N   1 
ATOM   12241 C  CA  . GLY C 1 382 ? 16.655  22.255  80.614  1.00 12.92 ? 374  GLY C CA  1 
ATOM   12242 C  C   . GLY C 1 382 ? 16.419  20.787  80.289  1.00 14.83 ? 374  GLY C C   1 
ATOM   12243 O  O   . GLY C 1 382 ? 16.628  20.308  79.181  1.00 13.88 ? 374  GLY C O   1 
ATOM   12244 N  N   . GLY C 1 383 ? 15.953  20.073  81.301  1.00 14.05 ? 375  GLY C N   1 
ATOM   12245 C  CA  . GLY C 1 383 ? 15.560  18.696  81.099  1.00 11.95 ? 375  GLY C CA  1 
ATOM   12246 C  C   . GLY C 1 383 ? 15.248  18.040  82.420  1.00 14.98 ? 375  GLY C C   1 
ATOM   12247 O  O   . GLY C 1 383 ? 15.542  18.566  83.499  1.00 12.52 ? 375  GLY C O   1 
ATOM   12248 N  N   . SER C 1 384 ? 14.618  16.876  82.317  1.00 11.14 ? 376  SER C N   1 
ATOM   12249 C  CA  . SER C 1 384 ? 14.350  16.074  83.498  1.00 11.45 ? 376  SER C CA  1 
ATOM   12250 C  C   . SER C 1 384 ? 14.282  14.623  83.071  1.00 14.49 ? 376  SER C C   1 
ATOM   12251 O  O   . SER C 1 384 ? 14.037  14.306  81.898  1.00 15.16 ? 376  SER C O   1 
ATOM   12252 C  CB  . SER C 1 384 ? 13.044  16.490  84.191  1.00 10.89 ? 376  SER C CB  1 
ATOM   12253 O  OG  . SER C 1 384 ? 11.937  16.038  83.438  1.00 14.83 ? 376  SER C OG  1 
ATOM   12254 N  N   . ALA C 1 385 ? 14.509  13.740  84.041  1.00 13.15 ? 377  ALA C N   1 
ATOM   12255 C  CA  . ALA C 1 385 ? 14.411  12.305  83.808  1.00 12.04 ? 377  ALA C CA  1 
ATOM   12256 C  C   . ALA C 1 385 ? 12.992  11.861  84.172  1.00 15.13 ? 377  ALA C C   1 
ATOM   12257 O  O   . ALA C 1 385 ? 12.739  11.272  85.221  1.00 13.40 ? 377  ALA C O   1 
ATOM   12258 C  CB  . ALA C 1 385 ? 15.479  11.562  84.604  1.00 12.75 ? 377  ALA C CB  1 
ATOM   12259 N  N   . ASP C 1 386 ? 12.046  12.193  83.284  1.00 10.49 ? 378  ASP C N   1 
ATOM   12260 C  CA  . ASP C 1 386 ? 10.647  11.760  83.409  1.00 14.31 ? 378  ASP C CA  1 
ATOM   12261 C  C   . ASP C 1 386 ? 9.998   12.299  84.687  1.00 16.72 ? 378  ASP C C   1 
ATOM   12262 O  O   . ASP C 1 386 ? 9.182   11.629  85.317  1.00 17.46 ? 378  ASP C O   1 
ATOM   12263 C  CB  . ASP C 1 386 ? 10.532  10.228  83.334  1.00 14.55 ? 378  ASP C CB  1 
ATOM   12264 C  CG  . ASP C 1 386 ? 9.100   9.751   83.159  1.00 22.77 ? 378  ASP C CG  1 
ATOM   12265 O  OD1 . ASP C 1 386 ? 8.404   10.334  82.316  1.00 20.35 ? 378  ASP C OD1 1 
ATOM   12266 O  OD2 . ASP C 1 386 ? 8.683   8.801   83.865  1.00 20.23 ? 378  ASP C OD2 1 
ATOM   12267 N  N   . LEU C 1 387 ? 10.340  13.527  85.069  1.00 14.36 ? 379  LEU C N   1 
ATOM   12268 C  CA  . LEU C 1 387 ? 9.632   14.197  86.159  1.00 13.10 ? 379  LEU C CA  1 
ATOM   12269 C  C   . LEU C 1 387 ? 8.389   14.893  85.627  1.00 17.47 ? 379  LEU C C   1 
ATOM   12270 O  O   . LEU C 1 387 ? 8.364   15.378  84.495  1.00 19.59 ? 379  LEU C O   1 
ATOM   12271 C  CB  . LEU C 1 387 ? 10.498  15.249  86.857  1.00 15.41 ? 379  LEU C CB  1 
ATOM   12272 C  CG  . LEU C 1 387 ? 11.757  14.808  87.596  1.00 16.04 ? 379  LEU C CG  1 
ATOM   12273 C  CD1 . LEU C 1 387 ? 12.177  15.873  88.589  1.00 17.07 ? 379  LEU C CD1 1 
ATOM   12274 C  CD2 . LEU C 1 387 ? 11.529  13.477  88.283  1.00 17.88 ? 379  LEU C CD2 1 
ATOM   12275 N  N   . THR C 1 388 ? 7.369   14.963  86.461  1.00 16.61 ? 380  THR C N   1 
ATOM   12276 C  CA  . THR C 1 388 ? 6.217   15.790  86.133  1.00 19.59 ? 380  THR C CA  1 
ATOM   12277 C  C   . THR C 1 388 ? 6.651   17.251  86.091  1.00 21.13 ? 380  THR C C   1 
ATOM   12278 O  O   . THR C 1 388 ? 7.346   17.708  87.005  1.00 20.05 ? 380  THR C O   1 
ATOM   12279 C  CB  . THR C 1 388 ? 5.115   15.576  87.160  1.00 25.77 ? 380  THR C CB  1 
ATOM   12280 O  OG1 . THR C 1 388 ? 4.618   14.238  87.027  1.00 26.71 ? 380  THR C OG1 1 
ATOM   12281 C  CG2 . THR C 1 388 ? 3.988   16.571  86.961  1.00 28.75 ? 380  THR C CG2 1 
ATOM   12282 N  N   . PRO C 1 389 ? 6.296   18.003  85.048  1.00 25.46 ? 381  PRO C N   1 
ATOM   12283 C  CA  . PRO C 1 389 ? 6.747   19.397  84.964  1.00 29.80 ? 381  PRO C CA  1 
ATOM   12284 C  C   . PRO C 1 389 ? 6.196   20.229  86.116  1.00 19.56 ? 381  PRO C C   1 
ATOM   12285 O  O   . PRO C 1 389 ? 5.072   20.020  86.581  1.00 24.69 ? 381  PRO C O   1 
ATOM   12286 C  CB  . PRO C 1 389 ? 6.195   19.870  83.614  1.00 36.54 ? 381  PRO C CB  1 
ATOM   12287 C  CG  . PRO C 1 389 ? 5.879   18.611  82.854  1.00 37.42 ? 381  PRO C CG  1 
ATOM   12288 C  CD  . PRO C 1 389 ? 5.467   17.624  83.891  1.00 33.93 ? 381  PRO C CD  1 
ATOM   12289 N  N   . SER C 1 390 ? 7.015   21.167  86.586  1.00 15.75 ? 382  SER C N   1 
ATOM   12290 C  CA  . SER C 1 390 ? 6.630   22.094  87.643  1.00 18.44 ? 382  SER C CA  1 
ATOM   12291 C  C   . SER C 1 390 ? 7.581   23.279  87.595  1.00 19.51 ? 382  SER C C   1 
ATOM   12292 O  O   . SER C 1 390 ? 8.581   23.266  86.872  1.00 18.90 ? 382  SER C O   1 
ATOM   12293 C  CB  . SER C 1 390 ? 6.679   21.438  89.024  1.00 19.89 ? 382  SER C CB  1 
ATOM   12294 O  OG  . SER C 1 390 ? 8.027   21.271  89.444  1.00 16.22 ? 382  SER C OG  1 
ATOM   12295 N  N   . ASN C 1 391 ? 7.266   24.304  88.392  1.00 19.72 ? 383  ASN C N   1 
ATOM   12296 C  CA  . ASN C 1 391 ? 8.119   25.488  88.437  1.00 22.44 ? 383  ASN C CA  1 
ATOM   12297 C  C   . ASN C 1 391 ? 9.510   25.194  88.986  1.00 20.57 ? 383  ASN C C   1 
ATOM   12298 O  O   . ASN C 1 391 ? 10.408  26.025  88.816  1.00 21.14 ? 383  ASN C O   1 
ATOM   12299 C  CB  . ASN C 1 391 ? 7.452   26.605  89.256  1.00 29.29 ? 383  ASN C CB  1 
ATOM   12300 C  CG  . ASN C 1 391 ? 6.920   26.126  90.594  1.00 38.80 ? 383  ASN C CG  1 
ATOM   12301 O  OD1 . ASN C 1 391 ? 7.245   25.037  91.059  1.00 37.02 ? 383  ASN C OD1 1 
ATOM   12302 N  ND2 . ASN C 1 391 ? 6.093   26.955  91.227  1.00 50.04 ? 383  ASN C ND2 1 
ATOM   12303 N  N   . LEU C 1 392 ? 9.724   24.027  89.603  1.00 17.28 ? 384  LEU C N   1 
ATOM   12304 C  CA  . LEU C 1 392 ? 11.062  23.660  90.057  1.00 11.53 ? 384  LEU C CA  1 
ATOM   12305 C  C   . LEU C 1 392 ? 11.952  23.120  88.945  1.00 16.82 ? 384  LEU C C   1 
ATOM   12306 O  O   . LEU C 1 392 ? 13.173  23.063  89.125  1.00 18.69 ? 384  LEU C O   1 
ATOM   12307 C  CB  . LEU C 1 392 ? 10.981  22.608  91.170  1.00 16.63 ? 384  LEU C CB  1 
ATOM   12308 C  CG  . LEU C 1 392 ? 10.280  23.066  92.449  1.00 18.17 ? 384  LEU C CG  1 
ATOM   12309 C  CD1 . LEU C 1 392 ? 10.119  21.907  93.421  1.00 16.11 ? 384  LEU C CD1 1 
ATOM   12310 C  CD2 . LEU C 1 392 ? 11.082  24.202  93.079  1.00 18.22 ? 384  LEU C CD2 1 
ATOM   12311 N  N   . THR C 1 393 ? 11.379  22.683  87.819  1.00 16.37 ? 385  THR C N   1 
ATOM   12312 C  CA  . THR C 1 393 ? 12.165  21.967  86.820  1.00 13.78 ? 385  THR C CA  1 
ATOM   12313 C  C   . THR C 1 393 ? 11.875  22.413  85.391  1.00 15.71 ? 385  THR C C   1 
ATOM   12314 O  O   . THR C 1 393 ? 12.382  21.788  84.455  1.00 16.80 ? 385  THR C O   1 
ATOM   12315 C  CB  . THR C 1 393 ? 11.909  20.461  86.911  1.00 17.45 ? 385  THR C CB  1 
ATOM   12316 O  OG1 . THR C 1 393 ? 10.528  20.213  86.636  1.00 17.37 ? 385  THR C OG1 1 
ATOM   12317 C  CG2 . THR C 1 393 ? 12.248  19.923  88.304  1.00 18.99 ? 385  THR C CG2 1 
ATOM   12318 N  N   . ASP C 1 394 ? 11.082  23.460  85.195  1.00 14.76 ? 386  ASP C N   1 
ATOM   12319 C  CA  . ASP C 1 394 ? 10.590  23.826  83.872  1.00 16.43 ? 386  ASP C CA  1 
ATOM   12320 C  C   . ASP C 1 394 ? 10.194  25.294  83.917  1.00 19.35 ? 386  ASP C C   1 
ATOM   12321 O  O   . ASP C 1 394 ? 10.078  25.888  84.994  1.00 17.43 ? 386  ASP C O   1 
ATOM   12322 C  CB  . ASP C 1 394 ? 9.410   22.935  83.476  1.00 19.79 ? 386  ASP C CB  1 
ATOM   12323 C  CG  . ASP C 1 394 ? 9.126   22.948  81.983  1.00 20.16 ? 386  ASP C CG  1 
ATOM   12324 O  OD1 . ASP C 1 394 ? 9.861   23.604  81.205  1.00 15.99 ? 386  ASP C OD1 1 
ATOM   12325 O  OD2 . ASP C 1 394 ? 8.156   22.273  81.593  1.00 21.41 ? 386  ASP C OD2 1 
ATOM   12326 N  N   . TRP C 1 395 ? 9.991   25.879  82.735  1.00 16.68 ? 387  TRP C N   1 
ATOM   12327 C  CA  . TRP C 1 395 ? 9.529   27.257  82.657  1.00 17.27 ? 387  TRP C CA  1 
ATOM   12328 C  C   . TRP C 1 395 ? 8.612   27.419  81.448  1.00 18.28 ? 387  TRP C C   1 
ATOM   12329 O  O   . TRP C 1 395 ? 8.467   26.517  80.618  1.00 19.02 ? 387  TRP C O   1 
ATOM   12330 C  CB  . TRP C 1 395 ? 10.705  28.244  82.613  1.00 18.79 ? 387  TRP C CB  1 
ATOM   12331 C  CG  . TRP C 1 395 ? 11.474  28.296  81.313  1.00 18.68 ? 387  TRP C CG  1 
ATOM   12332 C  CD1 . TRP C 1 395 ? 11.393  29.264  80.355  1.00 19.95 ? 387  TRP C CD1 1 
ATOM   12333 C  CD2 . TRP C 1 395 ? 12.450  27.351  80.845  1.00 14.72 ? 387  TRP C CD2 1 
ATOM   12334 N  NE1 . TRP C 1 395 ? 12.251  28.975  79.319  1.00 16.98 ? 387  TRP C NE1 1 
ATOM   12335 C  CE2 . TRP C 1 395 ? 12.912  27.811  79.598  1.00 15.36 ? 387  TRP C CE2 1 
ATOM   12336 C  CE3 . TRP C 1 395 ? 12.977  26.159  81.360  1.00 11.30 ? 387  TRP C CE3 1 
ATOM   12337 C  CZ2 . TRP C 1 395 ? 13.872  27.127  78.862  1.00 18.41 ? 387  TRP C CZ2 1 
ATOM   12338 C  CZ3 . TRP C 1 395 ? 13.939  25.488  80.631  1.00 20.30 ? 387  TRP C CZ3 1 
ATOM   12339 C  CH2 . TRP C 1 395 ? 14.373  25.968  79.394  1.00 18.92 ? 387  TRP C CH2 1 
ATOM   12340 N  N   . SER C 1 396 ? 8.004   28.605  81.353  1.00 16.67 ? 388  SER C N   1 
ATOM   12341 C  CA  . SER C 1 396 ? 6.907   28.813  80.405  1.00 19.67 ? 388  SER C CA  1 
ATOM   12342 C  C   . SER C 1 396 ? 7.347   28.707  78.947  1.00 19.63 ? 388  SER C C   1 
ATOM   12343 O  O   . SER C 1 396 ? 6.525   28.382  78.080  1.00 19.22 ? 388  SER C O   1 
ATOM   12344 C  CB  . SER C 1 396 ? 6.269   30.180  80.645  1.00 21.30 ? 388  SER C CB  1 
ATOM   12345 O  OG  . SER C 1 396 ? 7.150   31.218  80.247  1.00 19.63 ? 388  SER C OG  1 
ATOM   12346 N  N   . ASN C 1 397 ? 8.609   29.006  78.643  1.00 21.17 ? 389  ASN C N   1 
ATOM   12347 C  CA  . ASN C 1 397 ? 9.085   29.069  77.264  1.00 21.36 ? 389  ASN C CA  1 
ATOM   12348 C  C   . ASN C 1 397 ? 9.988   27.898  76.891  1.00 20.02 ? 389  ASN C C   1 
ATOM   12349 O  O   . ASN C 1 397 ? 10.789  28.011  75.958  1.00 24.85 ? 389  ASN C O   1 
ATOM   12350 C  CB  . ASN C 1 397 ? 9.811   30.390  77.016  1.00 24.90 ? 389  ASN C CB  1 
ATOM   12351 C  CG  . ASN C 1 397 ? 8.879   31.575  77.059  1.00 26.74 ? 389  ASN C CG  1 
ATOM   12352 O  OD1 . ASN C 1 397 ? 9.241   32.657  77.516  1.00 30.50 ? 389  ASN C OD1 1 
ATOM   12353 N  ND2 . ASN C 1 397 ? 7.660   31.369  76.594  1.00 18.54 ? 389  ASN C ND2 1 
ATOM   12354 N  N   . SER C 1 398 ? 9.890   26.780  77.602  1.00 14.06 ? 390  SER C N   1 
ATOM   12355 C  CA  . SER C 1 398 ? 10.655  25.595  77.222  1.00 14.89 ? 390  SER C CA  1 
ATOM   12356 C  C   . SER C 1 398 ? 10.083  24.965  75.954  1.00 16.47 ? 390  SER C C   1 
ATOM   12357 O  O   . SER C 1 398 ? 8.869   24.743  75.851  1.00 18.31 ? 390  SER C O   1 
ATOM   12358 C  CB  . SER C 1 398 ? 10.650  24.577  78.356  1.00 15.89 ? 390  SER C CB  1 
ATOM   12359 O  OG  . SER C 1 398 ? 9.321   24.288  78.751  1.00 19.58 ? 390  SER C OG  1 
ATOM   12360 N  N   . VAL C 1 399 ? 10.966  24.648  75.005  1.00 16.90 ? 391  VAL C N   1 
ATOM   12361 C  CA  . VAL C 1 399 ? 10.603  24.008  73.739  1.00 17.58 ? 391  VAL C CA  1 
ATOM   12362 C  C   . VAL C 1 399 ? 11.269  22.636  73.687  1.00 15.74 ? 391  VAL C C   1 
ATOM   12363 O  O   . VAL C 1 399 ? 12.500  22.540  73.738  1.00 16.55 ? 391  VAL C O   1 
ATOM   12364 C  CB  . VAL C 1 399 ? 11.018  24.862  72.528  1.00 19.33 ? 391  VAL C CB  1 
ATOM   12365 C  CG1 . VAL C 1 399 ? 10.724  24.121  71.208  1.00 22.45 ? 391  VAL C CG1 1 
ATOM   12366 C  CG2 . VAL C 1 399 ? 10.313  26.217  72.561  1.00 15.95 ? 391  VAL C CG2 1 
ATOM   12367 N  N   . SER C 1 400 ? 10.459  21.580  73.561  1.00 16.34 ? 392  SER C N   1 
ATOM   12368 C  CA  . SER C 1 400 ? 10.976  20.216  73.633  1.00 17.35 ? 392  SER C CA  1 
ATOM   12369 C  C   . SER C 1 400 ? 11.807  19.858  72.403  1.00 15.51 ? 392  SER C C   1 
ATOM   12370 O  O   . SER C 1 400 ? 11.344  20.011  71.269  1.00 16.78 ? 392  SER C O   1 
ATOM   12371 C  CB  . SER C 1 400 ? 9.819   19.230  73.780  1.00 21.74 ? 392  SER C CB  1 
ATOM   12372 O  OG  . SER C 1 400 ? 9.164   19.427  75.021  1.00 20.94 ? 392  SER C OG  1 
ATOM   12373 N  N   . VAL C 1 401 ? 13.025  19.354  72.638  1.00 11.67 ? 393  VAL C N   1 
ATOM   12374 C  CA  . VAL C 1 401 ? 13.855  18.821  71.554  1.00 13.50 ? 393  VAL C CA  1 
ATOM   12375 C  C   . VAL C 1 401 ? 13.254  17.517  71.051  1.00 16.25 ? 393  VAL C C   1 
ATOM   12376 O  O   . VAL C 1 401 ? 12.868  16.645  71.843  1.00 16.74 ? 393  VAL C O   1 
ATOM   12377 C  CB  . VAL C 1 401 ? 15.302  18.617  72.030  1.00 17.93 ? 393  VAL C CB  1 
ATOM   12378 C  CG1 . VAL C 1 401 ? 16.145  17.896  70.965  1.00 17.01 ? 393  VAL C CG1 1 
ATOM   12379 C  CG2 . VAL C 1 401 ? 15.922  19.945  72.402  1.00 14.42 ? 393  VAL C CG2 1 
ATOM   12380 N  N   . THR C 1 402 ? 13.156  17.380  69.729  1.00 17.56 ? 394  THR C N   1 
ATOM   12381 C  CA  . THR C 1 402 ? 12.586  16.193  69.114  1.00 19.20 ? 394  THR C CA  1 
ATOM   12382 C  C   . THR C 1 402 ? 13.517  15.688  68.021  1.00 20.88 ? 394  THR C C   1 
ATOM   12383 O  O   . THR C 1 402 ? 14.526  16.310  67.684  1.00 17.32 ? 394  THR C O   1 
ATOM   12384 C  CB  . THR C 1 402 ? 11.199  16.462  68.509  1.00 21.76 ? 394  THR C CB  1 
ATOM   12385 O  OG1 . THR C 1 402 ? 11.324  17.377  67.414  1.00 23.10 ? 394  THR C OG1 1 
ATOM   12386 C  CG2 . THR C 1 402 ? 10.253  17.053  69.549  1.00 18.97 ? 394  THR C CG2 1 
ATOM   12387 N  N   . ARG C 1 403 ? 13.138  14.549  67.453  1.00 20.27 ? 395  ARG C N   1 
ATOM   12388 C  CA  A ARG C 1 403 ? 13.871  14.013  66.315  0.53 23.71 ? 395  ARG C CA  1 
ATOM   12389 C  CA  B ARG C 1 403 ? 13.860  14.009  66.310  0.47 23.79 ? 395  ARG C CA  1 
ATOM   12390 C  C   . ARG C 1 403 ? 13.943  15.021  65.173  1.00 23.50 ? 395  ARG C C   1 
ATOM   12391 O  O   . ARG C 1 403 ? 14.970  15.127  64.493  1.00 23.35 ? 395  ARG C O   1 
ATOM   12392 C  CB  A ARG C 1 403 ? 13.212  12.716  65.849  0.53 26.49 ? 395  ARG C CB  1 
ATOM   12393 C  CB  B ARG C 1 403 ? 13.171  12.730  65.835  0.47 26.51 ? 395  ARG C CB  1 
ATOM   12394 C  CG  A ARG C 1 403 ? 13.814  12.132  64.603  0.53 29.85 ? 395  ARG C CG  1 
ATOM   12395 C  CG  B ARG C 1 403 ? 13.855  12.062  64.679  0.47 29.45 ? 395  ARG C CG  1 
ATOM   12396 C  CD  A ARG C 1 403 ? 13.008  10.937  64.142  0.53 31.37 ? 395  ARG C CD  1 
ATOM   12397 C  CD  B ARG C 1 403 ? 13.074  10.849  64.220  0.47 31.32 ? 395  ARG C CD  1 
ATOM   12398 N  NE  A ARG C 1 403 ? 13.013  9.867   65.131  0.53 31.85 ? 395  ARG C NE  1 
ATOM   12399 N  NE  B ARG C 1 403 ? 13.949  9.911   63.532  0.47 33.19 ? 395  ARG C NE  1 
ATOM   12400 C  CZ  A ARG C 1 403 ? 13.910  8.889   65.165  0.53 32.31 ? 395  ARG C CZ  1 
ATOM   12401 C  CZ  B ARG C 1 403 ? 14.644  8.962   64.149  0.47 32.53 ? 395  ARG C CZ  1 
ATOM   12402 N  NH1 A ARG C 1 403 ? 14.882  8.848   64.260  0.53 33.16 ? 395  ARG C NH1 1 
ATOM   12403 N  NH1 B ARG C 1 403 ? 14.552  8.829   65.468  0.47 32.24 ? 395  ARG C NH1 1 
ATOM   12404 N  NH2 A ARG C 1 403 ? 13.834  7.950   66.098  0.53 34.10 ? 395  ARG C NH2 1 
ATOM   12405 N  NH2 B ARG C 1 403 ? 15.428  8.149   63.451  0.47 24.60 ? 395  ARG C NH2 1 
ATOM   12406 N  N   . ASP C 1 404 ? 12.875  15.786  64.957  1.00 19.08 ? 396  ASP C N   1 
ATOM   12407 C  CA  . ASP C 1 404 ? 12.798  16.651  63.788  1.00 27.27 ? 396  ASP C CA  1 
ATOM   12408 C  C   . ASP C 1 404 ? 13.114  18.118  64.057  1.00 27.82 ? 396  ASP C C   1 
ATOM   12409 O  O   . ASP C 1 404 ? 13.312  18.869  63.095  1.00 27.68 ? 396  ASP C O   1 
ATOM   12410 C  CB  . ASP C 1 404 ? 11.402  16.549  63.162  1.00 31.95 ? 396  ASP C CB  1 
ATOM   12411 C  CG  . ASP C 1 404 ? 11.087  15.151  62.682  1.00 36.96 ? 396  ASP C CG  1 
ATOM   12412 O  OD1 . ASP C 1 404 ? 12.009  14.479  62.177  1.00 38.36 ? 396  ASP C OD1 1 
ATOM   12413 O  OD2 . ASP C 1 404 ? 9.923   14.720  62.823  1.00 42.67 ? 396  ASP C OD2 1 
ATOM   12414 N  N   . LYS C 1 405 ? 13.150  18.555  65.313  1.00 23.66 ? 397  LYS C N   1 
ATOM   12415 C  CA  . LYS C 1 405 ? 13.257  19.980  65.608  1.00 24.71 ? 397  LYS C CA  1 
ATOM   12416 C  C   . LYS C 1 405 ? 14.210  20.221  66.771  1.00 22.69 ? 397  LYS C C   1 
ATOM   12417 O  O   . LYS C 1 405 ? 14.366  19.375  67.653  1.00 19.60 ? 397  LYS C O   1 
ATOM   12418 C  CB  . LYS C 1 405 ? 11.881  20.586  65.927  1.00 26.93 ? 397  LYS C CB  1 
ATOM   12419 C  CG  . LYS C 1 405 ? 10.934  20.625  64.733  1.00 36.41 ? 397  LYS C CG  1 
ATOM   12420 C  CD  . LYS C 1 405 ? 10.528  22.051  64.390  1.00 41.09 ? 397  LYS C CD  1 
ATOM   12421 C  CE  . LYS C 1 405 ? 9.706   22.096  63.115  1.00 44.79 ? 397  LYS C CE  1 
ATOM   12422 N  NZ  . LYS C 1 405 ? 10.443  21.471  61.985  1.00 45.96 ? 397  LYS C NZ  1 
ATOM   12423 N  N   . GLY C 1 406 ? 14.848  21.389  66.762  1.00 18.05 ? 398  GLY C N   1 
ATOM   12424 C  CA  . GLY C 1 406 ? 15.668  21.795  67.883  1.00 19.17 ? 398  GLY C CA  1 
ATOM   12425 C  C   . GLY C 1 406 ? 14.811  22.208  69.072  1.00 19.25 ? 398  GLY C C   1 
ATOM   12426 O  O   . GLY C 1 406 ? 13.600  21.994  69.120  1.00 20.23 ? 398  GLY C O   1 
ATOM   12427 N  N   . GLY C 1 407 ? 15.462  22.822  70.048  1.00 18.47 ? 399  GLY C N   1 
ATOM   12428 C  CA  . GLY C 1 407 ? 14.754  23.255  71.235  1.00 17.21 ? 399  GLY C CA  1 
ATOM   12429 C  C   . GLY C 1 407 ? 15.719  23.514  72.376  1.00 20.83 ? 399  GLY C C   1 
ATOM   12430 O  O   . GLY C 1 407 ? 16.932  23.565  72.186  1.00 16.39 ? 399  GLY C O   1 
ATOM   12431 N  N   . ASN C 1 408 ? 15.140  23.688  73.575  1.00 15.71 ? 400  ASN C N   1 
ATOM   12432 C  CA  . ASN C 1 408 ? 15.931  23.996  74.762  1.00 12.80 ? 400  ASN C CA  1 
ATOM   12433 C  C   . ASN C 1 408 ? 15.499  23.175  75.974  1.00 15.32 ? 400  ASN C C   1 
ATOM   12434 O  O   . ASN C 1 408 ? 15.781  23.568  77.112  1.00 15.18 ? 400  ASN C O   1 
ATOM   12435 C  CB  . ASN C 1 408 ? 15.865  25.495  75.088  1.00 17.78 ? 400  ASN C CB  1 
ATOM   12436 C  CG  . ASN C 1 408 ? 14.432  25.999  75.311  1.00 20.05 ? 400  ASN C CG  1 
ATOM   12437 O  OD1 . ASN C 1 408 ? 13.497  25.219  75.488  1.00 17.93 ? 400  ASN C OD1 1 
ATOM   12438 N  ND2 . ASN C 1 408 ? 14.267  27.314  75.307  1.00 19.68 ? 400  ASN C ND2 1 
ATOM   12439 N  N   . TYR C 1 409 ? 14.818  22.050  75.757  1.00 12.45 ? 401  TYR C N   1 
ATOM   12440 C  CA  . TYR C 1 409 ? 14.408  21.180  76.856  1.00 12.49 ? 401  TYR C CA  1 
ATOM   12441 C  C   . TYR C 1 409 ? 14.463  19.728  76.405  1.00 15.10 ? 401  TYR C C   1 
ATOM   12442 O  O   . TYR C 1 409 ? 13.866  19.366  75.389  1.00 14.12 ? 401  TYR C O   1 
ATOM   12443 C  CB  . TYR C 1 409 ? 12.993  21.522  77.339  1.00 10.87 ? 401  TYR C CB  1 
ATOM   12444 C  CG  . TYR C 1 409 ? 12.734  21.059  78.760  1.00 10.56 ? 401  TYR C CG  1 
ATOM   12445 C  CD1 . TYR C 1 409 ? 12.353  19.744  79.037  1.00 22.91 ? 401  TYR C CD1 1 
ATOM   12446 C  CD2 . TYR C 1 409 ? 12.884  21.929  79.819  1.00 13.66 ? 401  TYR C CD2 1 
ATOM   12447 C  CE1 . TYR C 1 409 ? 12.125  19.325  80.348  1.00 20.88 ? 401  TYR C CE1 1 
ATOM   12448 C  CE2 . TYR C 1 409 ? 12.674  21.520  81.125  1.00 14.10 ? 401  TYR C CE2 1 
ATOM   12449 C  CZ  . TYR C 1 409 ? 12.298  20.229  81.386  1.00 15.58 ? 401  TYR C CZ  1 
ATOM   12450 O  OH  . TYR C 1 409 ? 12.086  19.860  82.697  1.00 18.33 ? 401  TYR C OH  1 
ATOM   12451 N  N   . ILE C 1 410 ? 15.149  18.894  77.177  1.00 14.64 ? 402  ILE C N   1 
ATOM   12452 C  CA  . ILE C 1 410 ? 15.408  17.510  76.807  1.00 12.30 ? 402  ILE C CA  1 
ATOM   12453 C  C   . ILE C 1 410 ? 14.630  16.590  77.732  1.00 14.88 ? 402  ILE C C   1 
ATOM   12454 O  O   . ILE C 1 410 ? 14.760  16.675  78.962  1.00 13.34 ? 402  ILE C O   1 
ATOM   12455 C  CB  . ILE C 1 410 ? 16.907  17.193  76.865  1.00 13.12 ? 402  ILE C CB  1 
ATOM   12456 C  CG1 . ILE C 1 410 ? 17.649  18.039  75.814  1.00 17.87 ? 402  ILE C CG1 1 
ATOM   12457 C  CG2 . ILE C 1 410 ? 17.129  15.689  76.670  1.00 12.98 ? 402  ILE C CG2 1 
ATOM   12458 C  CD1 . ILE C 1 410 ? 19.138  18.188  76.080  1.00 20.63 ? 402  ILE C CD1 1 
ATOM   12459 N  N   . HIS C 1 411 ? 13.843  15.696  77.143  1.00 11.33 ? 403  HIS C N   1 
ATOM   12460 C  CA  . HIS C 1 411 ? 13.120  14.684  77.916  1.00 10.75 ? 403  HIS C CA  1 
ATOM   12461 C  C   . HIS C 1 411 ? 13.999  13.440  77.967  1.00 9.82  ? 403  HIS C C   1 
ATOM   12462 O  O   . HIS C 1 411 ? 14.066  12.669  77.004  1.00 11.07 ? 403  HIS C O   1 
ATOM   12463 C  CB  . HIS C 1 411 ? 11.762  14.392  77.293  1.00 11.56 ? 403  HIS C CB  1 
ATOM   12464 C  CG  . HIS C 1 411 ? 10.866  15.590  77.228  1.00 20.02 ? 403  HIS C CG  1 
ATOM   12465 N  ND1 . HIS C 1 411 ? 10.256  16.125  78.343  1.00 22.40 ? 403  HIS C ND1 1 
ATOM   12466 C  CD2 . HIS C 1 411 ? 10.489  16.366  76.184  1.00 26.41 ? 403  HIS C CD2 1 
ATOM   12467 C  CE1 . HIS C 1 411 ? 9.533   17.173  77.988  1.00 25.19 ? 403  HIS C CE1 1 
ATOM   12468 N  NE2 . HIS C 1 411 ? 9.662   17.346  76.684  1.00 23.59 ? 403  HIS C NE2 1 
ATOM   12469 N  N   . TYR C 1 412 ? 14.688  13.249  79.086  1.00 9.09  ? 404  TYR C N   1 
ATOM   12470 C  CA  . TYR C 1 412 ? 15.643  12.155  79.176  1.00 10.68 ? 404  TYR C CA  1 
ATOM   12471 C  C   . TYR C 1 412 ? 14.976  10.806  79.412  1.00 13.77 ? 404  TYR C C   1 
ATOM   12472 O  O   . TYR C 1 412 ? 15.621  9.774   79.209  1.00 11.02 ? 404  TYR C O   1 
ATOM   12473 C  CB  . TYR C 1 412 ? 16.655  12.433  80.290  1.00 11.99 ? 404  TYR C CB  1 
ATOM   12474 C  CG  . TYR C 1 412 ? 17.592  13.580  79.988  1.00 12.31 ? 404  TYR C CG  1 
ATOM   12475 C  CD1 . TYR C 1 412 ? 18.736  13.373  79.218  1.00 12.64 ? 404  TYR C CD1 1 
ATOM   12476 C  CD2 . TYR C 1 412 ? 17.333  14.867  80.460  1.00 10.52 ? 404  TYR C CD2 1 
ATOM   12477 C  CE1 . TYR C 1 412 ? 19.604  14.408  78.926  1.00 12.56 ? 404  TYR C CE1 1 
ATOM   12478 C  CE2 . TYR C 1 412 ? 18.211  15.914  80.185  1.00 12.47 ? 404  TYR C CE2 1 
ATOM   12479 C  CZ  . TYR C 1 412 ? 19.342  15.669  79.413  1.00 14.53 ? 404  TYR C CZ  1 
ATOM   12480 O  OH  . TYR C 1 412 ? 20.221  16.671  79.111  1.00 12.16 ? 404  TYR C OH  1 
ATOM   12481 N  N   . GLY C 1 413 ? 13.711  10.785  79.821  1.00 12.16 ? 405  GLY C N   1 
ATOM   12482 C  CA  . GLY C 1 413 ? 13.097  9.511   80.155  1.00 11.76 ? 405  GLY C CA  1 
ATOM   12483 C  C   . GLY C 1 413 ? 13.639  9.003   81.484  1.00 12.67 ? 405  GLY C C   1 
ATOM   12484 O  O   . GLY C 1 413 ? 14.276  9.732   82.253  1.00 11.50 ? 405  GLY C O   1 
ATOM   12485 N  N   . VAL C 1 414 ? 13.404  7.720   81.748  1.00 12.02 ? 406  VAL C N   1 
ATOM   12486 C  CA  . VAL C 1 414 ? 13.828  7.163   83.033  1.00 10.59 ? 406  VAL C CA  1 
ATOM   12487 C  C   . VAL C 1 414 ? 15.276  6.706   82.927  1.00 14.85 ? 406  VAL C C   1 
ATOM   12488 O  O   . VAL C 1 414 ? 15.568  5.504   82.922  1.00 10.63 ? 406  VAL C O   1 
ATOM   12489 C  CB  . VAL C 1 414 ? 12.902  6.016   83.481  1.00 13.59 ? 406  VAL C CB  1 
ATOM   12490 C  CG1 . VAL C 1 414 ? 13.129  5.683   84.960  1.00 12.26 ? 406  VAL C CG1 1 
ATOM   12491 C  CG2 . VAL C 1 414 ? 11.458  6.416   83.265  1.00 18.35 ? 406  VAL C CG2 1 
ATOM   12492 N  N   . ARG C 1 415 ? 16.196  7.674   82.864  1.00 9.95  ? 407  ARG C N   1 
ATOM   12493 C  CA  . ARG C 1 415 ? 17.579  7.456   82.474  1.00 8.14  ? 407  ARG C CA  1 
ATOM   12494 C  C   . ARG C 1 415 ? 18.455  8.480   83.202  1.00 10.29 ? 407  ARG C C   1 
ATOM   12495 O  O   . ARG C 1 415 ? 18.992  9.406   82.595  1.00 11.72 ? 407  ARG C O   1 
ATOM   12496 C  CB  . ARG C 1 415 ? 17.745  7.608   80.963  1.00 8.31  ? 407  ARG C CB  1 
ATOM   12497 C  CG  . ARG C 1 415 ? 16.865  6.732   80.079  1.00 10.53 ? 407  ARG C CG  1 
ATOM   12498 C  CD  . ARG C 1 415 ? 17.247  7.008   78.619  1.00 10.79 ? 407  ARG C CD  1 
ATOM   12499 N  NE  . ARG C 1 415 ? 16.497  6.217   77.642  1.00 11.90 ? 407  ARG C NE  1 
ATOM   12500 C  CZ  . ARG C 1 415 ? 15.414  6.652   77.000  1.00 13.44 ? 407  ARG C CZ  1 
ATOM   12501 N  NH1 . ARG C 1 415 ? 14.918  7.867   77.252  1.00 9.60  ? 407  ARG C NH1 1 
ATOM   12502 N  NH2 . ARG C 1 415 ? 14.819  5.871   76.107  1.00 14.76 ? 407  ARG C NH2 1 
ATOM   12503 N  N   . GLU C 1 416 ? 18.591  8.329   84.523  1.00 12.06 ? 408  GLU C N   1 
ATOM   12504 C  CA  . GLU C 1 416 ? 19.259  9.368   85.301  1.00 8.63  ? 408  GLU C CA  1 
ATOM   12505 C  C   . GLU C 1 416 ? 20.755  9.411   85.017  1.00 8.08  ? 408  GLU C C   1 
ATOM   12506 O  O   . GLU C 1 416 ? 21.320  10.494  84.853  1.00 12.54 ? 408  GLU C O   1 
ATOM   12507 C  CB  . GLU C 1 416 ? 19.005  9.173   86.797  1.00 12.05 ? 408  GLU C CB  1 
ATOM   12508 C  CG  . GLU C 1 416 ? 17.548  9.367   87.200  1.00 10.77 ? 408  GLU C CG  1 
ATOM   12509 C  CD  . GLU C 1 416 ? 16.725  8.092   87.023  1.00 13.73 ? 408  GLU C CD  1 
ATOM   12510 O  OE1 . GLU C 1 416 ? 17.318  7.031   86.735  1.00 14.39 ? 408  GLU C OE1 1 
ATOM   12511 O  OE2 . GLU C 1 416 ? 15.494  8.153   87.161  1.00 15.58 ? 408  GLU C OE2 1 
ATOM   12512 N  N   . PHE C 1 417 ? 21.421  8.247   84.983  1.00 9.12  ? 409  PHE C N   1 
ATOM   12513 C  CA  . PHE C 1 417 ? 22.859  8.220   84.710  1.00 7.16  ? 409  PHE C CA  1 
ATOM   12514 C  C   . PHE C 1 417 ? 23.125  8.734   83.302  1.00 10.62 ? 409  PHE C C   1 
ATOM   12515 O  O   . PHE C 1 417 ? 24.023  9.557   83.081  1.00 11.33 ? 409  PHE C O   1 
ATOM   12516 C  CB  . PHE C 1 417 ? 23.385  6.791   84.881  1.00 7.61  ? 409  PHE C CB  1 
ATOM   12517 C  CG  . PHE C 1 417 ? 24.888  6.673   85.094  1.00 8.80  ? 409  PHE C CG  1 
ATOM   12518 C  CD1 . PHE C 1 417 ? 25.715  7.789   85.125  1.00 10.23 ? 409  PHE C CD1 1 
ATOM   12519 C  CD2 . PHE C 1 417 ? 25.461  5.417   85.255  1.00 11.27 ? 409  PHE C CD2 1 
ATOM   12520 C  CE1 . PHE C 1 417 ? 27.085  7.656   85.311  1.00 13.86 ? 409  PHE C CE1 1 
ATOM   12521 C  CE2 . PHE C 1 417 ? 26.834  5.270   85.441  1.00 9.63  ? 409  PHE C CE2 1 
ATOM   12522 C  CZ  . PHE C 1 417 ? 27.649  6.394   85.479  1.00 11.90 ? 409  PHE C CZ  1 
ATOM   12523 N  N   . GLY C 1 418 ? 22.342  8.249   82.336  1.00 11.38 ? 410  GLY C N   1 
ATOM   12524 C  CA  . GLY C 1 418 ? 22.394  8.810   80.993  1.00 12.22 ? 410  GLY C CA  1 
ATOM   12525 C  C   . GLY C 1 418 ? 22.252  10.318  80.986  1.00 10.81 ? 410  GLY C C   1 
ATOM   12526 O  O   . GLY C 1 418 ? 23.029  11.024  80.342  1.00 10.28 ? 410  GLY C O   1 
ATOM   12527 N  N   . MET C 1 419 ? 21.271  10.838  81.726  1.00 11.46 ? 411  MET C N   1 
ATOM   12528 C  CA  . MET C 1 419 ? 21.068  12.284  81.774  1.00 9.97  ? 411  MET C CA  1 
ATOM   12529 C  C   . MET C 1 419 ? 22.321  13.014  82.257  1.00 11.31 ? 411  MET C C   1 
ATOM   12530 O  O   . MET C 1 419 ? 22.755  13.994  81.645  1.00 8.43  ? 411  MET C O   1 
ATOM   12531 C  CB  . MET C 1 419 ? 19.881  12.619  82.681  1.00 11.10 ? 411  MET C CB  1 
ATOM   12532 C  CG  . MET C 1 419 ? 19.662  14.123  82.859  1.00 12.43 ? 411  MET C CG  1 
ATOM   12533 S  SD  . MET C 1 419 ? 18.234  14.510  83.900  1.00 11.89 ? 411  MET C SD  1 
ATOM   12534 C  CE  . MET C 1 419 ? 18.866  14.039  85.508  1.00 10.87 ? 411  MET C CE  1 
ATOM   12535 N  N   . GLY C 1 420 ? 22.890  12.581  83.385  1.00 9.60  ? 412  GLY C N   1 
ATOM   12536 C  CA  . GLY C 1 420 ? 24.006  13.314  83.948  1.00 6.94  ? 412  GLY C CA  1 
ATOM   12537 C  C   . GLY C 1 420 ? 25.221  13.312  83.038  1.00 9.44  ? 412  GLY C C   1 
ATOM   12538 O  O   . GLY C 1 420 ? 25.883  14.341  82.864  1.00 11.80 ? 412  GLY C O   1 
ATOM   12539 N  N   . ALA C 1 421 ? 25.516  12.165  82.428  1.00 9.24  ? 413  ALA C N   1 
ATOM   12540 C  CA  . ALA C 1 421 ? 26.671  12.080  81.542  1.00 8.84  ? 413  ALA C CA  1 
ATOM   12541 C  C   . ALA C 1 421 ? 26.414  12.747  80.192  1.00 9.48  ? 413  ALA C C   1 
ATOM   12542 O  O   . ALA C 1 421 ? 27.352  13.281  79.585  1.00 10.85 ? 413  ALA C O   1 
ATOM   12543 C  CB  . ALA C 1 421 ? 27.077  10.615  81.367  1.00 8.30  ? 413  ALA C CB  1 
ATOM   12544 N  N   . ILE C 1 422 ? 25.162  12.751  79.715  1.00 10.16 ? 414  ILE C N   1 
ATOM   12545 C  CA  . ILE C 1 422 ? 24.812  13.553  78.536  1.00 7.69  ? 414  ILE C CA  1 
ATOM   12546 C  C   . ILE C 1 422 ? 24.977  15.040  78.827  1.00 11.24 ? 414  ILE C C   1 
ATOM   12547 O  O   . ILE C 1 422 ? 25.515  15.792  78.006  1.00 12.30 ? 414  ILE C O   1 
ATOM   12548 C  CB  . ILE C 1 422 ? 23.384  13.220  78.061  1.00 8.84  ? 414  ILE C CB  1 
ATOM   12549 C  CG1 . ILE C 1 422 ? 23.375  11.816  77.441  1.00 12.32 ? 414  ILE C CG1 1 
ATOM   12550 C  CG2 . ILE C 1 422 ? 22.896  14.274  77.063  1.00 10.89 ? 414  ILE C CG2 1 
ATOM   12551 C  CD1 . ILE C 1 422 ? 21.988  11.229  77.145  1.00 8.18  ? 414  ILE C CD1 1 
ATOM   12552 N  N   . MET C 1 423 ? 24.514  15.488  79.998  1.00 8.13  ? 415  MET C N   1 
ATOM   12553 C  CA  . MET C 1 423 ? 24.709  16.878  80.389  1.00 13.36 ? 415  MET C CA  1 
ATOM   12554 C  C   . MET C 1 423 ? 26.183  17.258  80.365  1.00 11.67 ? 415  MET C C   1 
ATOM   12555 O  O   . MET C 1 423 ? 26.541  18.351  79.903  1.00 11.33 ? 415  MET C O   1 
ATOM   12556 C  CB  . MET C 1 423 ? 24.112  17.124  81.781  1.00 8.59  ? 415  MET C CB  1 
ATOM   12557 C  CG  . MET C 1 423 ? 22.601  17.293  81.776  1.00 13.09 ? 415  MET C CG  1 
ATOM   12558 S  SD  . MET C 1 423 ? 21.952  17.244  83.470  1.00 21.94 ? 415  MET C SD  1 
ATOM   12559 C  CE  . MET C 1 423 ? 23.009  18.447  84.297  1.00 17.44 ? 415  MET C CE  1 
ATOM   12560 N  N   . ASN C 1 424 ? 27.058  16.373  80.856  1.00 9.28  ? 416  ASN C N   1 
ATOM   12561 C  CA  . ASN C 1 424 ? 28.482  16.689  80.809  1.00 12.91 ? 416  ASN C CA  1 
ATOM   12562 C  C   . ASN C 1 424 ? 28.937  16.961  79.378  1.00 12.63 ? 416  ASN C C   1 
ATOM   12563 O  O   . ASN C 1 424 ? 29.707  17.893  79.131  1.00 12.99 ? 416  ASN C O   1 
ATOM   12564 C  CB  . ASN C 1 424 ? 29.304  15.564  81.438  1.00 10.21 ? 416  ASN C CB  1 
ATOM   12565 C  CG  . ASN C 1 424 ? 29.143  15.510  82.952  1.00 9.32  ? 416  ASN C CG  1 
ATOM   12566 O  OD1 . ASN C 1 424 ? 28.604  16.436  83.556  1.00 11.54 ? 416  ASN C OD1 1 
ATOM   12567 N  ND2 . ASN C 1 424 ? 29.607  14.428  83.565  1.00 12.49 ? 416  ASN C ND2 1 
ATOM   12568 N  N   . GLY C 1 425 ? 28.470  16.160  78.420  1.00 10.98 ? 417  GLY C N   1 
ATOM   12569 C  CA  . GLY C 1 425 ? 28.858  16.386  77.033  1.00 9.58  ? 417  GLY C CA  1 
ATOM   12570 C  C   . GLY C 1 425 ? 28.238  17.648  76.458  1.00 8.93  ? 417  GLY C C   1 
ATOM   12571 O  O   . GLY C 1 425 ? 28.877  18.360  75.682  1.00 11.58 ? 417  GLY C O   1 
ATOM   12572 N  N   . LEU C 1 426 ? 26.987  17.946  76.831  1.00 9.06  ? 418  LEU C N   1 
ATOM   12573 C  CA  . LEU C 1 426 ? 26.371  19.197  76.391  1.00 13.21 ? 418  LEU C CA  1 
ATOM   12574 C  C   . LEU C 1 426 ? 27.209  20.392  76.830  1.00 11.35 ? 418  LEU C C   1 
ATOM   12575 O  O   . LEU C 1 426 ? 27.473  21.301  76.038  1.00 12.34 ? 418  LEU C O   1 
ATOM   12576 C  CB  . LEU C 1 426 ? 24.947  19.312  76.944  1.00 12.11 ? 418  LEU C CB  1 
ATOM   12577 C  CG  . LEU C 1 426 ? 23.848  18.450  76.327  1.00 8.50  ? 418  LEU C CG  1 
ATOM   12578 C  CD1 . LEU C 1 426 ? 22.659  18.371  77.277  1.00 13.82 ? 418  LEU C CD1 1 
ATOM   12579 C  CD2 . LEU C 1 426 ? 23.438  19.073  75.001  1.00 9.16  ? 418  LEU C CD2 1 
ATOM   12580 N  N   . VAL C 1 427 ? 27.643  20.388  78.097  1.00 11.95 ? 419  VAL C N   1 
ATOM   12581 C  CA  . VAL C 1 427 ? 28.499  21.450  78.638  1.00 15.11 ? 419  VAL C CA  1 
ATOM   12582 C  C   . VAL C 1 427 ? 29.835  21.487  77.917  1.00 11.65 ? 419  VAL C C   1 
ATOM   12583 O  O   . VAL C 1 427 ? 30.349  22.560  77.574  1.00 12.90 ? 419  VAL C O   1 
ATOM   12584 C  CB  . VAL C 1 427 ? 28.734  21.247  80.151  1.00 19.64 ? 419  VAL C CB  1 
ATOM   12585 C  CG1 . VAL C 1 427 ? 29.834  22.179  80.650  1.00 24.60 ? 419  VAL C CG1 1 
ATOM   12586 C  CG2 . VAL C 1 427 ? 27.513  21.494  80.919  1.00 26.09 ? 419  VAL C CG2 1 
ATOM   12587 N  N   . LEU C 1 428 ? 30.467  20.319  77.768  1.00 10.77 ? 420  LEU C N   1 
ATOM   12588 C  CA  . LEU C 1 428 ? 31.793  20.285  77.161  1.00 11.67 ? 420  LEU C CA  1 
ATOM   12589 C  C   . LEU C 1 428 ? 31.778  20.879  75.763  1.00 14.77 ? 420  LEU C C   1 
ATOM   12590 O  O   . LEU C 1 428 ? 32.745  21.528  75.358  1.00 16.43 ? 420  LEU C O   1 
ATOM   12591 C  CB  . LEU C 1 428 ? 32.311  18.855  77.107  1.00 8.69  ? 420  LEU C CB  1 
ATOM   12592 C  CG  . LEU C 1 428 ? 32.770  18.315  78.466  1.00 13.19 ? 420  LEU C CG  1 
ATOM   12593 C  CD1 . LEU C 1 428 ? 32.810  16.802  78.454  1.00 17.55 ? 420  LEU C CD1 1 
ATOM   12594 C  CD2 . LEU C 1 428 ? 34.141  18.881  78.795  1.00 13.59 ? 420  LEU C CD2 1 
ATOM   12595 N  N   . HIS C 1 429 ? 30.684  20.684  75.020  1.00 15.88 ? 421  HIS C N   1 
ATOM   12596 C  CA  . HIS C 1 429 ? 30.656  21.117  73.624  1.00 13.99 ? 421  HIS C CA  1 
ATOM   12597 C  C   . HIS C 1 429 ? 30.834  22.622  73.499  1.00 13.90 ? 421  HIS C C   1 
ATOM   12598 O  O   . HIS C 1 429 ? 31.489  23.103  72.566  1.00 14.10 ? 421  HIS C O   1 
ATOM   12599 C  CB  . HIS C 1 429 ? 29.337  20.704  72.964  1.00 12.15 ? 421  HIS C CB  1 
ATOM   12600 C  CG  . HIS C 1 429 ? 29.261  21.052  71.511  1.00 11.73 ? 421  HIS C CG  1 
ATOM   12601 N  ND1 . HIS C 1 429 ? 28.914  22.309  71.059  1.00 12.56 ? 421  HIS C ND1 1 
ATOM   12602 C  CD2 . HIS C 1 429 ? 29.485  20.303  70.405  1.00 11.11 ? 421  HIS C CD2 1 
ATOM   12603 C  CE1 . HIS C 1 429 ? 28.934  22.319  69.736  1.00 14.00 ? 421  HIS C CE1 1 
ATOM   12604 N  NE2 . HIS C 1 429 ? 29.284  21.116  69.315  1.00 14.43 ? 421  HIS C NE2 1 
ATOM   12605 N  N   . GLY C 1 430 ? 30.236  23.376  74.395  1.00 12.89 ? 422  GLY C N   1 
ATOM   12606 C  CA  . GLY C 1 430 ? 30.173  24.811  74.194  1.00 16.00 ? 422  GLY C CA  1 
ATOM   12607 C  C   . GLY C 1 430 ? 28.854  25.218  73.560  1.00 17.25 ? 422  GLY C C   1 
ATOM   12608 O  O   . GLY C 1 430 ? 28.254  24.478  72.769  1.00 14.45 ? 422  GLY C O   1 
ATOM   12609 N  N   . GLY C 1 431 ? 28.364  26.399  73.944  1.00 14.66 ? 423  GLY C N   1 
ATOM   12610 C  CA  . GLY C 1 431 ? 27.207  27.000  73.316  1.00 10.90 ? 423  GLY C CA  1 
ATOM   12611 C  C   . GLY C 1 431 ? 25.904  26.870  74.081  1.00 13.21 ? 423  GLY C C   1 
ATOM   12612 O  O   . GLY C 1 431 ? 24.974  27.639  73.819  1.00 14.11 ? 423  GLY C O   1 
ATOM   12613 N  N   . VAL C 1 432 ? 25.806  25.923  75.014  1.00 12.94 ? 424  VAL C N   1 
ATOM   12614 C  CA  . VAL C 1 432 ? 24.595  25.735  75.801  1.00 16.17 ? 424  VAL C CA  1 
ATOM   12615 C  C   . VAL C 1 432 ? 24.981  25.565  77.263  1.00 16.70 ? 424  VAL C C   1 
ATOM   12616 O  O   . VAL C 1 432 ? 26.097  25.170  77.599  1.00 15.80 ? 424  VAL C O   1 
ATOM   12617 C  CB  . VAL C 1 432 ? 23.770  24.519  75.328  1.00 18.54 ? 424  VAL C CB  1 
ATOM   12618 C  CG1 . VAL C 1 432 ? 23.320  24.702  73.883  1.00 14.64 ? 424  VAL C CG1 1 
ATOM   12619 C  CG2 . VAL C 1 432 ? 24.599  23.252  75.459  1.00 14.18 ? 424  VAL C CG2 1 
ATOM   12620 N  N   . LYS C 1 433 ? 24.032  25.867  78.137  1.00 13.70 ? 425  LYS C N   1 
ATOM   12621 C  CA  A LYS C 1 433 ? 24.208  25.677  79.578  0.48 14.18 ? 425  LYS C CA  1 
ATOM   12622 C  CA  B LYS C 1 433 ? 24.200  25.689  79.582  0.52 14.27 ? 425  LYS C CA  1 
ATOM   12623 C  C   . LYS C 1 433 ? 23.087  24.780  80.079  1.00 12.75 ? 425  LYS C C   1 
ATOM   12624 O  O   . LYS C 1 433 ? 21.938  25.227  80.218  1.00 14.00 ? 425  LYS C O   1 
ATOM   12625 C  CB  A LYS C 1 433 ? 24.220  27.015  80.316  0.48 13.49 ? 425  LYS C CB  1 
ATOM   12626 C  CB  B LYS C 1 433 ? 24.162  27.035  80.308  0.52 13.44 ? 425  LYS C CB  1 
ATOM   12627 C  CG  A LYS C 1 433 ? 25.484  27.841  80.056  0.48 10.81 ? 425  LYS C CG  1 
ATOM   12628 C  CG  B LYS C 1 433 ? 24.263  26.942  81.834  0.52 10.73 ? 425  LYS C CG  1 
ATOM   12629 C  CD  A LYS C 1 433 ? 25.535  29.107  80.898  0.48 12.96 ? 425  LYS C CD  1 
ATOM   12630 C  CD  B LYS C 1 433 ? 24.274  28.332  82.485  0.52 11.79 ? 425  LYS C CD  1 
ATOM   12631 C  CE  A LYS C 1 433 ? 25.743  28.819  82.379  0.48 15.10 ? 425  LYS C CE  1 
ATOM   12632 C  CE  B LYS C 1 433 ? 25.515  29.144  82.107  0.52 12.93 ? 425  LYS C CE  1 
ATOM   12633 N  NZ  A LYS C 1 433 ? 27.062  28.168  82.662  0.48 12.41 ? 425  LYS C NZ  1 
ATOM   12634 N  NZ  B LYS C 1 433 ? 26.797  28.509  82.566  0.52 15.05 ? 425  LYS C NZ  1 
ATOM   12635 N  N   . PRO C 1 434 ? 23.364  23.524  80.357  1.00 15.94 ? 426  PRO C N   1 
ATOM   12636 C  CA  . PRO C 1 434 ? 22.289  22.590  80.680  1.00 15.85 ? 426  PRO C CA  1 
ATOM   12637 C  C   . PRO C 1 434 ? 22.044  22.422  82.165  1.00 12.85 ? 426  PRO C C   1 
ATOM   12638 O  O   . PRO C 1 434 ? 22.968  22.529  82.984  1.00 10.41 ? 426  PRO C O   1 
ATOM   12639 C  CB  . PRO C 1 434 ? 22.790  21.277  80.071  1.00 14.07 ? 426  PRO C CB  1 
ATOM   12640 C  CG  . PRO C 1 434 ? 24.229  21.341  80.346  1.00 15.27 ? 426  PRO C CG  1 
ATOM   12641 C  CD  . PRO C 1 434 ? 24.612  22.805  80.078  1.00 13.69 ? 426  PRO C CD  1 
ATOM   12642 N  N   . PHE C 1 435 ? 20.780  22.176  82.500  1.00 13.72 ? 427  PHE C N   1 
ATOM   12643 C  CA  . PHE C 1 435 ? 20.404  21.609  83.780  1.00 13.05 ? 427  PHE C CA  1 
ATOM   12644 C  C   . PHE C 1 435 ? 19.580  20.359  83.510  1.00 12.29 ? 427  PHE C C   1 
ATOM   12645 O  O   . PHE C 1 435 ? 19.006  20.191  82.429  1.00 12.01 ? 427  PHE C O   1 
ATOM   12646 C  CB  . PHE C 1 435 ? 19.650  22.627  84.675  1.00 11.09 ? 427  PHE C CB  1 
ATOM   12647 C  CG  . PHE C 1 435 ? 18.220  22.942  84.257  1.00 11.42 ? 427  PHE C CG  1 
ATOM   12648 C  CD1 . PHE C 1 435 ? 17.155  22.131  84.666  1.00 14.51 ? 427  PHE C CD1 1 
ATOM   12649 C  CD2 . PHE C 1 435 ? 17.927  24.101  83.549  1.00 10.52 ? 427  PHE C CD2 1 
ATOM   12650 C  CE1 . PHE C 1 435 ? 15.830  22.443  84.327  1.00 14.18 ? 427  PHE C CE1 1 
ATOM   12651 C  CE2 . PHE C 1 435 ? 16.590  24.427  83.206  1.00 15.86 ? 427  PHE C CE2 1 
ATOM   12652 C  CZ  . PHE C 1 435 ? 15.544  23.589  83.596  1.00 13.61 ? 427  PHE C CZ  1 
ATOM   12653 N  N   . GLY C 1 436 ? 19.573  19.449  84.481  1.00 8.87  ? 428  GLY C N   1 
ATOM   12654 C  CA  . GLY C 1 436 ? 18.738  18.263  84.369  1.00 9.48  ? 428  GLY C CA  1 
ATOM   12655 C  C   . GLY C 1 436 ? 18.261  17.808  85.732  1.00 11.20 ? 428  GLY C C   1 
ATOM   12656 O  O   . GLY C 1 436 ? 19.061  17.773  86.671  1.00 12.02 ? 428  GLY C O   1 
ATOM   12657 N  N   . ALA C 1 437 ? 16.979  17.472  85.867  1.00 9.18  ? 429  ALA C N   1 
ATOM   12658 C  CA  . ALA C 1 437 ? 16.377  17.246  87.176  1.00 9.91  ? 429  ALA C CA  1 
ATOM   12659 C  C   . ALA C 1 437 ? 15.929  15.804  87.364  1.00 8.77  ? 429  ALA C C   1 
ATOM   12660 O  O   . ALA C 1 437 ? 15.458  15.149  86.428  1.00 10.77 ? 429  ALA C O   1 
ATOM   12661 C  CB  . ALA C 1 437 ? 15.162  18.165  87.386  1.00 9.39  ? 429  ALA C CB  1 
ATOM   12662 N  N   . THR C 1 438 ? 16.034  15.335  88.605  1.00 9.57  ? 430  THR C N   1 
ATOM   12663 C  CA  . THR C 1 438 ? 15.465  14.062  89.025  1.00 10.67 ? 430  THR C CA  1 
ATOM   12664 C  C   . THR C 1 438 ? 15.192  14.181  90.523  1.00 12.38 ? 430  THR C C   1 
ATOM   12665 O  O   . THR C 1 438 ? 15.454  15.222  91.126  1.00 10.01 ? 430  THR C O   1 
ATOM   12666 C  CB  . THR C 1 438 ? 16.393  12.876  88.684  1.00 12.02 ? 430  THR C CB  1 
ATOM   12667 O  OG1 . THR C 1 438 ? 15.749  11.644  89.034  1.00 11.77 ? 430  THR C OG1 1 
ATOM   12668 C  CG2 . THR C 1 438 ? 17.710  12.966  89.427  1.00 7.42  ? 430  THR C CG2 1 
ATOM   12669 N  N   . PHE C 1 439 ? 14.631  13.131  91.123  1.00 10.53 ? 431  PHE C N   1 
ATOM   12670 C  CA  . PHE C 1 439 ? 14.532  13.110  92.581  1.00 13.51 ? 431  PHE C CA  1 
ATOM   12671 C  C   . PHE C 1 439 ? 15.923  13.023  93.207  1.00 7.92  ? 431  PHE C C   1 
ATOM   12672 O  O   . PHE C 1 439 ? 16.814  12.333  92.706  1.00 10.70 ? 431  PHE C O   1 
ATOM   12673 C  CB  . PHE C 1 439 ? 13.707  11.923  93.087  1.00 13.02 ? 431  PHE C CB  1 
ATOM   12674 C  CG  . PHE C 1 439 ? 12.241  11.980  92.746  1.00 16.41 ? 431  PHE C CG  1 
ATOM   12675 C  CD1 . PHE C 1 439 ? 11.706  13.022  92.011  1.00 14.35 ? 431  PHE C CD1 1 
ATOM   12676 C  CD2 . PHE C 1 439 ? 11.392  10.974  93.179  1.00 27.58 ? 431  PHE C CD2 1 
ATOM   12677 C  CE1 . PHE C 1 439 ? 10.353  13.060  91.704  1.00 20.97 ? 431  PHE C CE1 1 
ATOM   12678 C  CE2 . PHE C 1 439 ? 10.038  11.003  92.871  1.00 28.85 ? 431  PHE C CE2 1 
ATOM   12679 C  CZ  . PHE C 1 439 ? 9.522   12.052  92.128  1.00 26.71 ? 431  PHE C CZ  1 
ATOM   12680 N  N   . LEU C 1 440 ? 16.084  13.687  94.353  1.00 7.99  ? 432  LEU C N   1 
ATOM   12681 C  CA  . LEU C 1 440 ? 17.372  13.664  95.045  1.00 7.77  ? 432  LEU C CA  1 
ATOM   12682 C  C   . LEU C 1 440 ? 17.870  12.239  95.284  1.00 11.39 ? 432  LEU C C   1 
ATOM   12683 O  O   . LEU C 1 440 ? 19.074  11.972  95.162  1.00 9.29  ? 432  LEU C O   1 
ATOM   12684 C  CB  . LEU C 1 440 ? 17.268  14.443  96.364  1.00 10.69 ? 432  LEU C CB  1 
ATOM   12685 C  CG  . LEU C 1 440 ? 18.517  14.423  97.262  1.00 11.27 ? 432  LEU C CG  1 
ATOM   12686 C  CD1 . LEU C 1 440 ? 19.766  14.934  96.527  1.00 12.68 ? 432  LEU C CD1 1 
ATOM   12687 C  CD2 . LEU C 1 440 ? 18.270  15.240  98.547  1.00 12.39 ? 432  LEU C CD2 1 
ATOM   12688 N  N   . MET C 1 441 ? 16.961  11.295  95.582  1.00 10.97 ? 433  MET C N   1 
ATOM   12689 C  CA  . MET C 1 441 ? 17.400  9.909   95.795  1.00 8.76  ? 433  MET C CA  1 
ATOM   12690 C  C   . MET C 1 441 ? 18.135  9.365   94.573  1.00 11.23 ? 433  MET C C   1 
ATOM   12691 O  O   . MET C 1 441 ? 19.119  8.632   94.704  1.00 10.76 ? 433  MET C O   1 
ATOM   12692 C  CB  . MET C 1 441 ? 16.206  9.008   96.147  1.00 11.98 ? 433  MET C CB  1 
ATOM   12693 C  CG  . MET C 1 441 ? 16.590  7.540   96.402  1.00 12.29 ? 433  MET C CG  1 
ATOM   12694 S  SD  . MET C 1 441 ? 17.682  7.409   97.855  1.00 12.26 ? 433  MET C SD  1 
ATOM   12695 C  CE  . MET C 1 441 ? 16.519  7.930   99.114  1.00 8.66  ? 433  MET C CE  1 
ATOM   12696 N  N   . PHE C 1 442 ? 17.698  9.724   93.374  1.00 12.00 ? 434  PHE C N   1 
ATOM   12697 C  CA  . PHE C 1 442 ? 18.311  9.134   92.193  1.00 13.47 ? 434  PHE C CA  1 
ATOM   12698 C  C   . PHE C 1 442 ? 19.517  9.919   91.712  1.00 11.98 ? 434  PHE C C   1 
ATOM   12699 O  O   . PHE C 1 442 ? 20.086  9.586   90.666  1.00 13.52 ? 434  PHE C O   1 
ATOM   12700 C  CB  . PHE C 1 442 ? 17.233  8.933   91.130  1.00 14.70 ? 434  PHE C CB  1 
ATOM   12701 C  CG  . PHE C 1 442 ? 16.080  8.175   91.688  1.00 18.93 ? 434  PHE C CG  1 
ATOM   12702 C  CD1 . PHE C 1 442 ? 16.329  7.070   92.503  1.00 18.64 ? 434  PHE C CD1 1 
ATOM   12703 C  CD2 . PHE C 1 442 ? 14.782  8.614   91.540  1.00 21.01 ? 434  PHE C CD2 1 
ATOM   12704 C  CE1 . PHE C 1 442 ? 15.293  6.382   93.108  1.00 20.89 ? 434  PHE C CE1 1 
ATOM   12705 C  CE2 . PHE C 1 442 ? 13.742  7.922   92.139  1.00 24.90 ? 434  PHE C CE2 1 
ATOM   12706 C  CZ  . PHE C 1 442 ? 14.000  6.816   92.930  1.00 24.88 ? 434  PHE C CZ  1 
ATOM   12707 N  N   . SER C 1 443 ? 19.974  10.896  92.507  1.00 8.89  ? 435  SER C N   1 
ATOM   12708 C  CA  . SER C 1 443 ? 21.380  11.284  92.435  1.00 10.50 ? 435  SER C CA  1 
ATOM   12709 C  C   . SER C 1 443 ? 22.272  10.052  92.510  1.00 14.35 ? 435  SER C C   1 
ATOM   12710 O  O   . SER C 1 443 ? 23.352  10.019  91.908  1.00 11.73 ? 435  SER C O   1 
ATOM   12711 C  CB  . SER C 1 443 ? 21.729  12.270  93.558  1.00 11.17 ? 435  SER C CB  1 
ATOM   12712 O  OG  . SER C 1 443 ? 21.620  11.681  94.854  1.00 11.84 ? 435  SER C OG  1 
ATOM   12713 N  N   . GLU C 1 444 ? 21.816  9.010   93.213  1.00 8.66  ? 436  GLU C N   1 
ATOM   12714 C  CA  . GLU C 1 444 ? 22.641  7.818   93.369  1.00 8.31  ? 436  GLU C CA  1 
ATOM   12715 C  C   . GLU C 1 444 ? 22.726  7.026   92.073  1.00 9.00  ? 436  GLU C C   1 
ATOM   12716 O  O   . GLU C 1 444 ? 23.708  6.312   91.850  1.00 17.44 ? 436  GLU C O   1 
ATOM   12717 C  CB  . GLU C 1 444 ? 22.090  6.951   94.504  1.00 11.62 ? 436  GLU C CB  1 
ATOM   12718 C  CG  . GLU C 1 444 ? 22.124  7.676   95.842  1.00 13.10 ? 436  GLU C CG  1 
ATOM   12719 C  CD  . GLU C 1 444 ? 22.056  6.746   97.033  1.00 14.43 ? 436  GLU C CD  1 
ATOM   12720 O  OE1 . GLU C 1 444 ? 21.592  5.588   96.885  1.00 14.14 ? 436  GLU C OE1 1 
ATOM   12721 O  OE2 . GLU C 1 444 ? 22.454  7.191   98.129  1.00 15.61 ? 436  GLU C OE2 1 
ATOM   12722 N  N   . TYR C 1 445 ? 21.716  7.140   91.207  1.00 8.60  ? 437  TYR C N   1 
ATOM   12723 C  CA  . TYR C 1 445 ? 21.800  6.479   89.916  1.00 8.54  ? 437  TYR C CA  1 
ATOM   12724 C  C   . TYR C 1 445 ? 22.785  7.177   88.991  1.00 17.15 ? 437  TYR C C   1 
ATOM   12725 O  O   . TYR C 1 445 ? 23.343  6.531   88.099  1.00 19.28 ? 437  TYR C O   1 
ATOM   12726 C  CB  . TYR C 1 445 ? 20.425  6.420   89.238  1.00 9.16  ? 437  TYR C CB  1 
ATOM   12727 C  CG  . TYR C 1 445 ? 19.512  5.271   89.651  1.00 12.61 ? 437  TYR C CG  1 
ATOM   12728 C  CD1 . TYR C 1 445 ? 19.273  4.975   90.994  1.00 12.97 ? 437  TYR C CD1 1 
ATOM   12729 C  CD2 . TYR C 1 445 ? 18.841  4.529   88.692  1.00 13.22 ? 437  TYR C CD2 1 
ATOM   12730 C  CE1 . TYR C 1 445 ? 18.419  3.939   91.359  1.00 10.81 ? 437  TYR C CE1 1 
ATOM   12731 C  CE2 . TYR C 1 445 ? 17.977  3.499   89.042  1.00 14.04 ? 437  TYR C CE2 1 
ATOM   12732 C  CZ  . TYR C 1 445 ? 17.764  3.211   90.378  1.00 13.79 ? 437  TYR C CZ  1 
ATOM   12733 O  OH  . TYR C 1 445 ? 16.908  2.188   90.718  1.00 13.41 ? 437  TYR C OH  1 
ATOM   12734 N  N   . GLU C 1 446 ? 22.994  8.490   89.159  1.00 10.30 ? 438  GLU C N   1 
ATOM   12735 C  CA  . GLU C 1 446 ? 23.877  9.241   88.271  1.00 7.88  ? 438  GLU C CA  1 
ATOM   12736 C  C   . GLU C 1 446 ? 25.148  9.704   88.978  1.00 10.12 ? 438  GLU C C   1 
ATOM   12737 O  O   . GLU C 1 446 ? 25.848  10.586  88.473  1.00 10.59 ? 438  GLU C O   1 
ATOM   12738 C  CB  . GLU C 1 446 ? 23.143  10.442  87.667  1.00 11.68 ? 438  GLU C CB  1 
ATOM   12739 C  CG  . GLU C 1 446 ? 22.587  11.398  88.710  1.00 12.70 ? 438  GLU C CG  1 
ATOM   12740 C  CD  . GLU C 1 446 ? 22.036  12.681  88.111  1.00 15.92 ? 438  GLU C CD  1 
ATOM   12741 O  OE1 . GLU C 1 446 ? 22.381  13.034  86.958  1.00 12.78 ? 438  GLU C OE1 1 
ATOM   12742 O  OE2 . GLU C 1 446 ? 21.269  13.357  88.816  1.00 13.08 ? 438  GLU C OE2 1 
ATOM   12743 N  N   . ARG C 1 447 ? 25.497  9.063   90.099  1.00 9.52  ? 439  ARG C N   1 
ATOM   12744 C  CA  . ARG C 1 447 ? 26.444  9.652   91.040  1.00 10.90 ? 439  ARG C CA  1 
ATOM   12745 C  C   . ARG C 1 447 ? 27.793  9.954   90.398  1.00 13.23 ? 439  ARG C C   1 
ATOM   12746 O  O   . ARG C 1 447 ? 28.355  11.030  90.602  1.00 11.07 ? 439  ARG C O   1 
ATOM   12747 C  CB  . ARG C 1 447 ? 26.632  8.720   92.229  1.00 9.55  ? 439  ARG C CB  1 
ATOM   12748 C  CG  . ARG C 1 447 ? 27.675  9.216   93.207  1.00 9.60  ? 439  ARG C CG  1 
ATOM   12749 C  CD  . ARG C 1 447 ? 27.292  10.544  93.846  1.00 11.38 ? 439  ARG C CD  1 
ATOM   12750 N  NE  . ARG C 1 447 ? 28.324  10.924  94.805  1.00 12.12 ? 439  ARG C NE  1 
ATOM   12751 C  CZ  . ARG C 1 447 ? 28.086  11.371  96.031  1.00 13.97 ? 439  ARG C CZ  1 
ATOM   12752 N  NH1 . ARG C 1 447 ? 26.830  11.495  96.462  1.00 10.01 ? 439  ARG C NH1 1 
ATOM   12753 N  NH2 . ARG C 1 447 ? 29.108  11.686  96.823  1.00 12.20 ? 439  ARG C NH2 1 
ATOM   12754 N  N   . ASN C 1 448 ? 28.360  8.995   89.665  1.00 10.61 ? 440  ASN C N   1 
ATOM   12755 C  CA  . ASN C 1 448 ? 29.703  9.225   89.151  1.00 12.71 ? 440  ASN C CA  1 
ATOM   12756 C  C   . ASN C 1 448 ? 29.721  10.273  88.047  1.00 11.73 ? 440  ASN C C   1 
ATOM   12757 O  O   . ASN C 1 448 ? 30.762  10.903  87.833  1.00 11.12 ? 440  ASN C O   1 
ATOM   12758 C  CB  . ASN C 1 448 ? 30.341  7.915   88.654  1.00 11.68 ? 440  ASN C CB  1 
ATOM   12759 C  CG  . ASN C 1 448 ? 31.869  8.033   88.512  1.00 13.29 ? 440  ASN C CG  1 
ATOM   12760 O  OD1 . ASN C 1 448 ? 32.411  7.984   87.408  1.00 14.16 ? 440  ASN C OD1 1 
ATOM   12761 N  ND2 . ASN C 1 448 ? 32.555  8.232   89.639  1.00 12.29 ? 440  ASN C ND2 1 
ATOM   12762 N  N   . ALA C 1 449 ? 28.597  10.491  87.347  1.00 12.41 ? 441  ALA C N   1 
ATOM   12763 C  CA  . ALA C 1 449 ? 28.552  11.595  86.390  1.00 15.18 ? 441  ALA C CA  1 
ATOM   12764 C  C   . ALA C 1 449 ? 28.665  12.944  87.098  1.00 14.04 ? 441  ALA C C   1 
ATOM   12765 O  O   . ALA C 1 449 ? 29.306  13.875  86.582  1.00 10.88 ? 441  ALA C O   1 
ATOM   12766 C  CB  . ALA C 1 449 ? 27.275  11.522  85.555  1.00 13.85 ? 441  ALA C CB  1 
ATOM   12767 N  N   . LEU C 1 450 ? 28.046  13.070  88.280  1.00 8.92  ? 442  LEU C N   1 
ATOM   12768 C  CA  . LEU C 1 450 ? 28.247  14.265  89.098  1.00 12.20 ? 442  LEU C CA  1 
ATOM   12769 C  C   . LEU C 1 450 ? 29.716  14.437  89.443  1.00 12.25 ? 442  LEU C C   1 
ATOM   12770 O  O   . LEU C 1 450 ? 30.267  15.544  89.349  1.00 11.58 ? 442  LEU C O   1 
ATOM   12771 C  CB  . LEU C 1 450 ? 27.425  14.174  90.389  1.00 10.53 ? 442  LEU C CB  1 
ATOM   12772 C  CG  . LEU C 1 450 ? 25.933  14.538  90.426  1.00 22.42 ? 442  LEU C CG  1 
ATOM   12773 C  CD1 . LEU C 1 450 ? 25.171  13.963  89.289  1.00 14.56 ? 442  LEU C CD1 1 
ATOM   12774 C  CD2 . LEU C 1 450 ? 25.301  14.082  91.730  1.00 22.26 ? 442  LEU C CD2 1 
ATOM   12775 N  N   . ARG C 1 451 ? 30.370  13.339  89.834  1.00 12.11 ? 443  ARG C N   1 
ATOM   12776 C  CA  . ARG C 1 451 ? 31.769  13.416  90.229  1.00 9.47  ? 443  ARG C CA  1 
ATOM   12777 C  C   . ARG C 1 451 ? 32.656  13.784  89.046  1.00 10.78 ? 443  ARG C C   1 
ATOM   12778 O  O   . ARG C 1 451 ? 33.577  14.591  89.186  1.00 8.51  ? 443  ARG C O   1 
ATOM   12779 C  CB  . ARG C 1 451 ? 32.207  12.087  90.838  1.00 9.22  ? 443  ARG C CB  1 
ATOM   12780 C  CG  . ARG C 1 451 ? 33.640  12.108  91.369  1.00 8.78  ? 443  ARG C CG  1 
ATOM   12781 C  CD  . ARG C 1 451 ? 34.032  10.779  91.989  1.00 11.83 ? 443  ARG C CD  1 
ATOM   12782 N  NE  . ARG C 1 451 ? 35.090  10.982  92.980  1.00 12.01 ? 443  ARG C NE  1 
ATOM   12783 C  CZ  . ARG C 1 451 ? 36.389  10.950  92.714  1.00 12.23 ? 443  ARG C CZ  1 
ATOM   12784 N  NH1 . ARG C 1 451 ? 36.818  10.700  91.478  1.00 13.62 ? 443  ARG C NH1 1 
ATOM   12785 N  NH2 . ARG C 1 451 ? 37.265  11.158  93.691  1.00 12.93 ? 443  ARG C NH2 1 
ATOM   12786 N  N   . MET C 1 452 ? 32.390  13.193  87.874  1.00 8.03  ? 444  MET C N   1 
ATOM   12787 C  CA  . MET C 1 452 ? 33.180  13.482  86.678  1.00 10.73 ? 444  MET C CA  1 
ATOM   12788 C  C   . MET C 1 452 ? 33.033  14.940  86.240  1.00 11.17 ? 444  MET C C   1 
ATOM   12789 O  O   . MET C 1 452 ? 33.995  15.549  85.757  1.00 11.92 ? 444  MET C O   1 
ATOM   12790 C  CB  . MET C 1 452 ? 32.769  12.532  85.542  1.00 8.88  ? 444  MET C CB  1 
ATOM   12791 C  CG  . MET C 1 452 ? 33.190  11.079  85.767  1.00 9.51  ? 444  MET C CG  1 
ATOM   12792 S  SD  . MET C 1 452 ? 34.993  10.879  85.951  1.00 13.45 ? 444  MET C SD  1 
ATOM   12793 C  CE  . MET C 1 452 ? 35.554  11.257  84.295  1.00 16.85 ? 444  MET C CE  1 
ATOM   12794 N  N   . ALA C 1 453 ? 31.834  15.514  86.387  1.00 11.00 ? 445  ALA C N   1 
ATOM   12795 C  CA  . ALA C 1 453 ? 31.665  16.947  86.150  1.00 10.35 ? 445  ALA C CA  1 
ATOM   12796 C  C   . ALA C 1 453 ? 32.602  17.761  87.039  1.00 11.46 ? 445  ALA C C   1 
ATOM   12797 O  O   . ALA C 1 453 ? 33.297  18.665  86.571  1.00 12.32 ? 445  ALA C O   1 
ATOM   12798 C  CB  . ALA C 1 453 ? 30.209  17.354  86.392  1.00 9.97  ? 445  ALA C CB  1 
ATOM   12799 N  N   . ALA C 1 454 ? 32.632  17.451  88.330  1.00 7.33  ? 446  ALA C N   1 
ATOM   12800 C  CA  . ALA C 1 454 ? 33.499  18.193  89.240  1.00 7.57  ? 446  ALA C CA  1 
ATOM   12801 C  C   . ALA C 1 454 ? 34.971  17.984  88.898  1.00 9.70  ? 446  ALA C C   1 
ATOM   12802 O  O   . ALA C 1 454 ? 35.770  18.938  88.903  1.00 11.79 ? 446  ALA C O   1 
ATOM   12803 C  CB  . ALA C 1 454 ? 33.189  17.763  90.674  1.00 11.63 ? 446  ALA C CB  1 
ATOM   12804 N  N   . LEU C 1 455 ? 35.344  16.739  88.591  1.00 12.09 ? 447  LEU C N   1 
ATOM   12805 C  CA  . LEU C 1 455 ? 36.718  16.423  88.210  1.00 12.96 ? 447  LEU C CA  1 
ATOM   12806 C  C   . LEU C 1 455 ? 37.143  17.167  86.947  1.00 14.00 ? 447  LEU C C   1 
ATOM   12807 O  O   . LEU C 1 455 ? 38.276  17.656  86.855  1.00 12.81 ? 447  LEU C O   1 
ATOM   12808 C  CB  . LEU C 1 455 ? 36.855  14.916  88.008  1.00 10.71 ? 447  LEU C CB  1 
ATOM   12809 C  CG  . LEU C 1 455 ? 38.201  14.406  87.473  1.00 18.25 ? 447  LEU C CG  1 
ATOM   12810 C  CD1 . LEU C 1 455 ? 39.363  14.892  88.320  1.00 22.62 ? 447  LEU C CD1 1 
ATOM   12811 C  CD2 . LEU C 1 455 ? 38.168  12.898  87.479  1.00 22.06 ? 447  LEU C CD2 1 
ATOM   12812 N  N   . MET C 1 456 ? 36.259  17.240  85.953  1.00 11.09 ? 448  MET C N   1 
ATOM   12813 C  CA  . MET C 1 456 ? 36.569  17.954  84.718  1.00 10.91 ? 448  MET C CA  1 
ATOM   12814 C  C   . MET C 1 456 ? 36.530  19.469  84.871  1.00 9.84  ? 448  MET C C   1 
ATOM   12815 O  O   . MET C 1 456 ? 36.886  20.165  83.921  1.00 12.51 ? 448  MET C O   1 
ATOM   12816 C  CB  . MET C 1 456 ? 35.595  17.552  83.606  1.00 9.99  ? 448  MET C CB  1 
ATOM   12817 C  CG  . MET C 1 456 ? 35.772  16.126  83.113  1.00 14.56 ? 448  MET C CG  1 
ATOM   12818 S  SD  . MET C 1 456 ? 34.844  15.805  81.599  1.00 15.52 ? 448  MET C SD  1 
ATOM   12819 C  CE  . MET C 1 456 ? 33.515  14.796  82.236  1.00 15.27 ? 448  MET C CE  1 
ATOM   12820 N  N   . LYS C 1 457 ? 36.081  19.982  86.016  1.00 10.73 ? 449  LYS C N   1 
ATOM   12821 C  CA  A LYS C 1 457 ? 35.931  21.418  86.245  0.59 11.02 ? 449  LYS C CA  1 
ATOM   12822 C  CA  B LYS C 1 457 ? 35.945  21.422  86.230  0.41 11.41 ? 449  LYS C CA  1 
ATOM   12823 C  C   . LYS C 1 457 ? 35.012  22.057  85.199  1.00 13.18 ? 449  LYS C C   1 
ATOM   12824 O  O   . LYS C 1 457 ? 35.302  23.117  84.642  1.00 15.11 ? 449  LYS C O   1 
ATOM   12825 C  CB  A LYS C 1 457 ? 37.297  22.110  86.292  0.59 13.74 ? 449  LYS C CB  1 
ATOM   12826 C  CB  B LYS C 1 457 ? 37.310  22.118  86.225  0.41 13.79 ? 449  LYS C CB  1 
ATOM   12827 C  CG  A LYS C 1 457 ? 38.248  21.509  87.333  0.59 16.99 ? 449  LYS C CG  1 
ATOM   12828 C  CG  B LYS C 1 457 ? 38.270  21.619  87.294  0.41 17.20 ? 449  LYS C CG  1 
ATOM   12829 C  CD  A LYS C 1 457 ? 39.662  22.070  87.219  0.59 21.13 ? 449  LYS C CD  1 
ATOM   12830 C  CD  B LYS C 1 457 ? 39.596  22.358  87.217  0.41 20.74 ? 449  LYS C CD  1 
ATOM   12831 C  CE  A LYS C 1 457 ? 39.715  23.518  87.663  0.59 24.05 ? 449  LYS C CE  1 
ATOM   12832 C  CE  B LYS C 1 457 ? 40.422  22.127  88.469  0.41 22.75 ? 449  LYS C CE  1 
ATOM   12833 N  NZ  A LYS C 1 457 ? 41.070  24.115  87.474  0.59 28.84 ? 449  LYS C NZ  1 
ATOM   12834 N  NZ  B LYS C 1 457 ? 41.516  23.139  88.580  0.41 29.53 ? 449  LYS C NZ  1 
ATOM   12835 N  N   . ILE C 1 458 ? 33.884  21.407  84.940  1.00 12.28 ? 450  ILE C N   1 
ATOM   12836 C  CA  . ILE C 1 458 ? 32.856  21.945  84.056  1.00 12.84 ? 450  ILE C CA  1 
ATOM   12837 C  C   . ILE C 1 458 ? 31.630  22.272  84.905  1.00 14.93 ? 450  ILE C C   1 
ATOM   12838 O  O   . ILE C 1 458 ? 31.554  21.909  86.076  1.00 10.28 ? 450  ILE C O   1 
ATOM   12839 C  CB  . ILE C 1 458 ? 32.515  20.976  82.916  1.00 13.38 ? 450  ILE C CB  1 
ATOM   12840 C  CG1 . ILE C 1 458 ? 32.062  19.631  83.501  1.00 11.38 ? 450  ILE C CG1 1 
ATOM   12841 C  CG2 . ILE C 1 458 ? 33.738  20.826  82.008  1.00 10.59 ? 450  ILE C CG2 1 
ATOM   12842 C  CD1 . ILE C 1 458 ? 31.656  18.585  82.457  1.00 19.32 ? 450  ILE C CD1 1 
ATOM   12843 N  N   . ASN C 1 459 ? 30.647  22.970  84.311  1.00 12.08 ? 451  ASN C N   1 
ATOM   12844 C  CA  . ASN C 1 459 ? 29.578  23.578  85.114  1.00 14.80 ? 451  ASN C CA  1 
ATOM   12845 C  C   . ASN C 1 459 ? 28.150  23.204  84.703  1.00 10.00 ? 451  ASN C C   1 
ATOM   12846 O  O   . ASN C 1 459 ? 27.286  24.074  84.624  1.00 13.10 ? 451  ASN C O   1 
ATOM   12847 C  CB  . ASN C 1 459 ? 29.745  25.099  85.121  1.00 12.10 ? 451  ASN C CB  1 
ATOM   12848 C  CG  . ASN C 1 459 ? 29.651  25.724  83.726  1.00 15.61 ? 451  ASN C CG  1 
ATOM   12849 O  OD1 . ASN C 1 459 ? 29.500  25.031  82.722  1.00 14.10 ? 451  ASN C OD1 1 
ATOM   12850 N  ND2 . ASN C 1 459 ? 29.737  27.051  83.669  1.00 12.72 ? 451  ASN C ND2 1 
ATOM   12851 N  N   . PRO C 1 460 ? 27.840  21.911  84.526  1.00 9.19  ? 452  PRO C N   1 
ATOM   12852 C  CA  . PRO C 1 460 ? 26.425  21.515  84.419  1.00 9.47  ? 452  PRO C CA  1 
ATOM   12853 C  C   . PRO C 1 460 ? 25.724  21.723  85.753  1.00 9.12  ? 452  PRO C C   1 
ATOM   12854 O  O   . PRO C 1 460 ? 26.361  21.761  86.809  1.00 11.41 ? 452  PRO C O   1 
ATOM   12855 C  CB  . PRO C 1 460 ? 26.490  20.026  84.060  1.00 13.58 ? 452  PRO C CB  1 
ATOM   12856 C  CG  . PRO C 1 460 ? 27.758  19.555  84.773  1.00 13.96 ? 452  PRO C CG  1 
ATOM   12857 C  CD  . PRO C 1 460 ? 28.722  20.729  84.670  1.00 11.02 ? 452  PRO C CD  1 
ATOM   12858 N  N   . VAL C 1 461 ? 24.403  21.895  85.698  1.00 8.90  ? 453  VAL C N   1 
ATOM   12859 C  CA  . VAL C 1 461 ? 23.599  22.177  86.895  1.00 9.10  ? 453  VAL C CA  1 
ATOM   12860 C  C   . VAL C 1 461 ? 22.696  20.974  87.144  1.00 11.28 ? 453  VAL C C   1 
ATOM   12861 O  O   . VAL C 1 461 ? 21.800  20.679  86.348  1.00 11.06 ? 453  VAL C O   1 
ATOM   12862 C  CB  . VAL C 1 461 ? 22.786  23.477  86.766  1.00 8.02  ? 453  VAL C CB  1 
ATOM   12863 C  CG1 . VAL C 1 461 ? 22.061  23.768  88.074  1.00 10.76 ? 453  VAL C CG1 1 
ATOM   12864 C  CG2 . VAL C 1 461 ? 23.716  24.657  86.435  1.00 13.56 ? 453  VAL C CG2 1 
ATOM   12865 N  N   . PHE C 1 462 ? 22.941  20.262  88.237  1.00 10.62 ? 454  PHE C N   1 
ATOM   12866 C  CA  . PHE C 1 462 ? 22.160  19.083  88.583  1.00 10.59 ? 454  PHE C CA  1 
ATOM   12867 C  C   . PHE C 1 462 ? 21.060  19.497  89.544  1.00 12.46 ? 454  PHE C C   1 
ATOM   12868 O  O   . PHE C 1 462 ? 21.346  20.018  90.627  1.00 11.87 ? 454  PHE C O   1 
ATOM   12869 C  CB  . PHE C 1 462 ? 23.051  18.012  89.204  1.00 8.37  ? 454  PHE C CB  1 
ATOM   12870 C  CG  . PHE C 1 462 ? 24.148  17.554  88.288  1.00 11.12 ? 454  PHE C CG  1 
ATOM   12871 C  CD1 . PHE C 1 462 ? 23.880  16.650  87.274  1.00 15.87 ? 454  PHE C CD1 1 
ATOM   12872 C  CD2 . PHE C 1 462 ? 25.447  18.037  88.437  1.00 11.38 ? 454  PHE C CD2 1 
ATOM   12873 C  CE1 . PHE C 1 462 ? 24.886  16.225  86.425  1.00 15.00 ? 454  PHE C CE1 1 
ATOM   12874 C  CE2 . PHE C 1 462 ? 26.460  17.620  87.592  1.00 10.12 ? 454  PHE C CE2 1 
ATOM   12875 C  CZ  . PHE C 1 462 ? 26.181  16.717  86.580  1.00 11.87 ? 454  PHE C CZ  1 
ATOM   12876 N  N   . VAL C 1 463 ? 19.814  19.274  89.148  1.00 12.05 ? 455  VAL C N   1 
ATOM   12877 C  CA  . VAL C 1 463 ? 18.664  19.717  89.922  1.00 13.50 ? 455  VAL C CA  1 
ATOM   12878 C  C   . VAL C 1 463 ? 18.037  18.505  90.590  1.00 9.73  ? 455  VAL C C   1 
ATOM   12879 O  O   . VAL C 1 463 ? 17.891  17.443  89.972  1.00 10.11 ? 455  VAL C O   1 
ATOM   12880 C  CB  . VAL C 1 463 ? 17.656  20.463  89.021  1.00 12.37 ? 455  VAL C CB  1 
ATOM   12881 C  CG1 . VAL C 1 463 ? 16.373  20.773  89.756  1.00 11.07 ? 455  VAL C CG1 1 
ATOM   12882 C  CG2 . VAL C 1 463 ? 18.298  21.748  88.500  1.00 12.13 ? 455  VAL C CG2 1 
ATOM   12883 N  N   . PHE C 1 464 ? 17.665  18.661  91.857  1.00 10.00 ? 456  PHE C N   1 
ATOM   12884 C  CA  . PHE C 1 464 ? 17.031  17.596  92.618  1.00 8.61  ? 456  PHE C CA  1 
ATOM   12885 C  C   . PHE C 1 464 ? 15.806  18.124  93.357  1.00 8.83  ? 456  PHE C C   1 
ATOM   12886 O  O   . PHE C 1 464 ? 15.872  19.171  94.008  1.00 14.22 ? 456  PHE C O   1 
ATOM   12887 C  CB  . PHE C 1 464 ? 18.034  16.986  93.586  1.00 10.11 ? 456  PHE C CB  1 
ATOM   12888 C  CG  . PHE C 1 464 ? 19.228  16.386  92.890  1.00 9.88  ? 456  PHE C CG  1 
ATOM   12889 C  CD1 . PHE C 1 464 ? 19.096  15.223  92.148  1.00 9.37  ? 456  PHE C CD1 1 
ATOM   12890 C  CD2 . PHE C 1 464 ? 20.460  17.004  92.944  1.00 12.01 ? 456  PHE C CD2 1 
ATOM   12891 C  CE1 . PHE C 1 464 ? 20.172  14.672  91.495  1.00 11.62 ? 456  PHE C CE1 1 
ATOM   12892 C  CE2 . PHE C 1 464 ? 21.549  16.467  92.278  1.00 11.18 ? 456  PHE C CE2 1 
ATOM   12893 C  CZ  . PHE C 1 464 ? 21.409  15.297  91.555  1.00 10.31 ? 456  PHE C CZ  1 
ATOM   12894 N  N   . THR C 1 465 ? 14.701  17.392  93.260  1.00 8.75  ? 457  THR C N   1 
ATOM   12895 C  CA  . THR C 1 465 ? 13.464  17.661  93.982  1.00 12.52 ? 457  THR C CA  1 
ATOM   12896 C  C   . THR C 1 465 ? 13.188  16.492  94.927  1.00 12.61 ? 457  THR C C   1 
ATOM   12897 O  O   . THR C 1 465 ? 13.939  15.522  94.967  1.00 13.58 ? 457  THR C O   1 
ATOM   12898 C  CB  . THR C 1 465 ? 12.296  17.884  93.015  1.00 14.05 ? 457  THR C CB  1 
ATOM   12899 O  OG1 . THR C 1 465 ? 12.027  16.674  92.303  1.00 14.27 ? 457  THR C OG1 1 
ATOM   12900 C  CG2 . THR C 1 465 ? 12.644  18.992  92.017  1.00 16.36 ? 457  THR C CG2 1 
ATOM   12901 N  N   . HIS C 1 466 ? 12.122  16.605  95.721  1.00 9.42  ? 458  HIS C N   1 
ATOM   12902 C  CA  . HIS C 1 466 ? 11.756  15.543  96.671  1.00 10.87 ? 458  HIS C CA  1 
ATOM   12903 C  C   . HIS C 1 466 ? 12.923  15.241  97.625  1.00 14.40 ? 458  HIS C C   1 
ATOM   12904 O  O   . HIS C 1 466 ? 13.456  14.132  97.673  1.00 12.97 ? 458  HIS C O   1 
ATOM   12905 C  CB  . HIS C 1 466 ? 11.317  14.276  95.914  1.00 12.58 ? 458  HIS C CB  1 
ATOM   12906 C  CG  . HIS C 1 466 ? 10.056  14.447  95.123  1.00 21.30 ? 458  HIS C CG  1 
ATOM   12907 N  ND1 . HIS C 1 466 ? 9.969   15.279  94.028  1.00 22.81 ? 458  HIS C ND1 1 
ATOM   12908 C  CD2 . HIS C 1 466 ? 8.831   13.883  95.264  1.00 25.88 ? 458  HIS C CD2 1 
ATOM   12909 C  CE1 . HIS C 1 466 ? 8.738   15.238  93.542  1.00 25.07 ? 458  HIS C CE1 1 
ATOM   12910 N  NE2 . HIS C 1 466 ? 8.031   14.393  94.269  1.00 19.31 ? 458  HIS C NE2 1 
ATOM   12911 N  N   . ASP C 1 467 ? 13.325  16.258  98.387  1.00 12.98 ? 459  ASP C N   1 
ATOM   12912 C  CA  . ASP C 1 467 ? 14.633  16.230  99.034  1.00 10.10 ? 459  ASP C CA  1 
ATOM   12913 C  C   . ASP C 1 467 ? 14.638  15.611  100.435 1.00 12.86 ? 459  ASP C C   1 
ATOM   12914 O  O   . ASP C 1 467 ? 15.710  15.508  101.040 1.00 12.04 ? 459  ASP C O   1 
ATOM   12915 C  CB  . ASP C 1 467 ? 15.189  17.654  99.111  1.00 12.19 ? 459  ASP C CB  1 
ATOM   12916 C  CG  . ASP C 1 467 ? 14.507  18.484  100.189 1.00 17.24 ? 459  ASP C CG  1 
ATOM   12917 O  OD1 . ASP C 1 467 ? 13.274  18.346  100.370 1.00 18.06 ? 459  ASP C OD1 1 
ATOM   12918 O  OD2 . ASP C 1 467 ? 15.215  19.261  100.854 1.00 16.78 ? 459  ASP C OD2 1 
ATOM   12919 N  N   . SER C 1 468 ? 13.496  15.194  100.979 1.00 11.07 ? 460  SER C N   1 
ATOM   12920 C  CA  . SER C 1 468 ? 13.511  14.712  102.357 1.00 11.69 ? 460  SER C CA  1 
ATOM   12921 C  C   . SER C 1 468 ? 12.283  13.853  102.609 1.00 13.12 ? 460  SER C C   1 
ATOM   12922 O  O   . SER C 1 468 ? 11.492  13.581  101.701 1.00 13.84 ? 460  SER C O   1 
ATOM   12923 C  CB  . SER C 1 468 ? 13.530  15.874  103.356 1.00 11.14 ? 460  SER C CB  1 
ATOM   12924 O  OG  . SER C 1 468 ? 12.219  16.394  103.500 1.00 12.88 ? 460  SER C OG  1 
ATOM   12925 N  N   . ILE C 1 469 ? 12.113  13.449  103.870 1.00 12.57 ? 461  ILE C N   1 
ATOM   12926 C  CA  . ILE C 1 469 ? 10.923  12.732  104.321 1.00 14.75 ? 461  ILE C CA  1 
ATOM   12927 C  C   . ILE C 1 469 ? 9.674   13.543  103.987 1.00 15.52 ? 461  ILE C C   1 
ATOM   12928 O  O   . ILE C 1 469 ? 8.571   12.996  103.909 1.00 18.57 ? 461  ILE C O   1 
ATOM   12929 C  CB  . ILE C 1 469 ? 11.008  12.427  105.829 1.00 16.44 ? 461  ILE C CB  1 
ATOM   12930 C  CG1 . ILE C 1 469 ? 11.378  13.699  106.611 1.00 13.59 ? 461  ILE C CG1 1 
ATOM   12931 C  CG2 . ILE C 1 469 ? 12.037  11.311  106.084 1.00 11.28 ? 461  ILE C CG2 1 
ATOM   12932 C  CD1 . ILE C 1 469 ? 11.129  13.611  108.145 1.00 14.08 ? 461  ILE C CD1 1 
ATOM   12933 N  N   . GLY C 1 470 ? 9.830   14.853  103.776 1.00 17.01 ? 462  GLY C N   1 
ATOM   12934 C  CA  . GLY C 1 470 ? 8.694   15.687  103.388 1.00 20.89 ? 462  GLY C CA  1 
ATOM   12935 C  C   . GLY C 1 470 ? 8.034   15.302  102.063 1.00 18.62 ? 462  GLY C C   1 
ATOM   12936 O  O   . GLY C 1 470 ? 6.961   15.832  101.752 1.00 20.35 ? 462  GLY C O   1 
ATOM   12937 N  N   . LEU C 1 471 ? 8.642   14.422  101.267 1.00 14.57 ? 463  LEU C N   1 
ATOM   12938 C  CA  . LEU C 1 471 ? 7.950   13.966  100.064 1.00 15.55 ? 463  LEU C CA  1 
ATOM   12939 C  C   . LEU C 1 471 ? 6.784   13.050  100.404 1.00 22.21 ? 463  LEU C C   1 
ATOM   12940 O  O   . LEU C 1 471 ? 5.893   12.864  99.567  1.00 20.68 ? 463  LEU C O   1 
ATOM   12941 C  CB  . LEU C 1 471 ? 8.909   13.259  99.094  1.00 19.05 ? 463  LEU C CB  1 
ATOM   12942 C  CG  . LEU C 1 471 ? 9.587   11.927  99.443  1.00 17.04 ? 463  LEU C CG  1 
ATOM   12943 C  CD1 . LEU C 1 471 ? 8.676   10.686  99.281  1.00 15.66 ? 463  LEU C CD1 1 
ATOM   12944 C  CD2 . LEU C 1 471 ? 10.855  11.773  98.596  1.00 14.05 ? 463  LEU C CD2 1 
ATOM   12945 N  N   . GLY C 1 472 ? 6.785   12.448  101.589 1.00 18.39 ? 464  GLY C N   1 
ATOM   12946 C  CA  . GLY C 1 472 ? 5.576   11.815  102.121 1.00 15.72 ? 464  GLY C CA  1 
ATOM   12947 C  C   . GLY C 1 472 ? 5.455   10.336  101.742 1.00 17.21 ? 464  GLY C C   1 
ATOM   12948 O  O   . GLY C 1 472 ? 6.359   9.550   102.006 1.00 18.32 ? 464  GLY C O   1 
ATOM   12949 N  N   . GLU C 1 473 ? 4.325   9.977   101.119 1.00 15.13 ? 465  GLU C N   1 
ATOM   12950 C  CA  . GLU C 1 473 ? 3.842   8.597   101.089 1.00 17.40 ? 465  GLU C CA  1 
ATOM   12951 C  C   . GLU C 1 473 ? 4.718   7.627   100.297 1.00 20.29 ? 465  GLU C C   1 
ATOM   12952 O  O   . GLU C 1 473 ? 4.652   6.417   100.554 1.00 23.38 ? 465  GLU C O   1 
ATOM   12953 C  CB  . GLU C 1 473 ? 2.419   8.565   100.522 1.00 15.75 ? 465  GLU C CB  1 
ATOM   12954 C  CG  . GLU C 1 473 ? 1.356   8.980   101.516 1.00 16.63 ? 465  GLU C CG  1 
ATOM   12955 C  CD  . GLU C 1 473 ? 1.057   10.486  101.514 1.00 20.36 ? 465  GLU C CD  1 
ATOM   12956 O  OE1 . GLU C 1 473 ? 1.848   11.280  100.955 1.00 20.49 ? 465  GLU C OE1 1 
ATOM   12957 O  OE2 . GLU C 1 473 ? 0.010   10.862  102.071 1.00 18.06 ? 465  GLU C OE2 1 
ATOM   12958 N  N   . ASP C 1 474 ? 5.510   8.105   99.335  1.00 14.75 ? 466  ASP C N   1 
ATOM   12959 C  CA  . ASP C 1 474 ? 6.313   7.178   98.537  1.00 17.07 ? 466  ASP C CA  1 
ATOM   12960 C  C   . ASP C 1 474 ? 7.306   6.386   99.394  1.00 19.42 ? 466  ASP C C   1 
ATOM   12961 O  O   . ASP C 1 474 ? 7.660   5.255   99.034  1.00 21.92 ? 466  ASP C O   1 
ATOM   12962 C  CB  . ASP C 1 474 ? 7.046   7.931   97.425  1.00 16.73 ? 466  ASP C CB  1 
ATOM   12963 C  CG  . ASP C 1 474 ? 6.189   8.126   96.177  1.00 25.24 ? 466  ASP C CG  1 
ATOM   12964 O  OD1 . ASP C 1 474 ? 5.065   7.566   96.090  1.00 20.91 ? 466  ASP C OD1 1 
ATOM   12965 O  OD2 . ASP C 1 474 ? 6.661   8.842   95.275  1.00 23.88 ? 466  ASP C OD2 1 
ATOM   12966 N  N   . GLY C 1 475 ? 7.761   6.945   100.521 1.00 17.35 ? 467  GLY C N   1 
ATOM   12967 C  CA  . GLY C 1 475 ? 8.386   6.142   101.555 1.00 11.75 ? 467  GLY C CA  1 
ATOM   12968 C  C   . GLY C 1 475 ? 9.901   6.021   101.497 1.00 14.12 ? 467  GLY C C   1 
ATOM   12969 O  O   . GLY C 1 475 ? 10.581  6.732   100.758 1.00 12.23 ? 467  GLY C O   1 
ATOM   12970 N  N   . PRO C 1 476 ? 10.450  5.074   102.270 1.00 11.28 ? 468  PRO C N   1 
ATOM   12971 C  CA  . PRO C 1 476 ? 11.905  5.064   102.528 1.00 10.86 ? 468  PRO C CA  1 
ATOM   12972 C  C   . PRO C 1 476 ? 12.785  4.781   101.314 1.00 10.37 ? 468  PRO C C   1 
ATOM   12973 O  O   . PRO C 1 476 ? 13.977  5.103   101.361 1.00 10.51 ? 468  PRO C O   1 
ATOM   12974 C  CB  . PRO C 1 476 ? 12.060  3.955   103.583 1.00 11.95 ? 468  PRO C CB  1 
ATOM   12975 C  CG  . PRO C 1 476 ? 10.829  3.114   103.428 1.00 15.07 ? 468  PRO C CG  1 
ATOM   12976 C  CD  . PRO C 1 476 ? 9.740   4.087   103.100 1.00 11.86 ? 468  PRO C CD  1 
ATOM   12977 N  N   . THR C 1 477 ? 12.274  4.147   100.261 1.00 10.42 ? 469  THR C N   1 
ATOM   12978 C  CA  . THR C 1 477 ? 13.105  3.932   99.080  1.00 14.77 ? 469  THR C CA  1 
ATOM   12979 C  C   . THR C 1 477 ? 13.339  5.223   98.305  1.00 15.66 ? 469  THR C C   1 
ATOM   12980 O  O   . THR C 1 477 ? 14.324  5.316   97.566  1.00 13.89 ? 469  THR C O   1 
ATOM   12981 C  CB  . THR C 1 477 ? 12.479  2.902   98.131  1.00 13.03 ? 469  THR C CB  1 
ATOM   12982 O  OG1 . THR C 1 477 ? 11.275  3.440   97.565  1.00 15.40 ? 469  THR C OG1 1 
ATOM   12983 C  CG2 . THR C 1 477 ? 12.166  1.598   98.857  1.00 16.60 ? 469  THR C CG2 1 
ATOM   12984 N  N   . HIS C 1 478 ? 12.442  6.204   98.440  1.00 11.00 ? 470  HIS C N   1 
ATOM   12985 C  CA  . HIS C 1 478 ? 12.550  7.489   97.762  1.00 9.50  ? 470  HIS C CA  1 
ATOM   12986 C  C   . HIS C 1 478 ? 12.948  8.655   98.664  1.00 11.07 ? 470  HIS C C   1 
ATOM   12987 O  O   . HIS C 1 478 ? 13.426  9.669   98.147  1.00 13.23 ? 470  HIS C O   1 
ATOM   12988 C  CB  . HIS C 1 478 ? 11.208  7.837   97.090  1.00 14.45 ? 470  HIS C CB  1 
ATOM   12989 C  CG  . HIS C 1 478 ? 10.954  7.069   95.833  1.00 21.37 ? 470  HIS C CG  1 
ATOM   12990 N  ND1 . HIS C 1 478 ? 11.052  5.698   95.772  1.00 24.77 ? 470  HIS C ND1 1 
ATOM   12991 C  CD2 . HIS C 1 478 ? 10.606  7.479   94.589  1.00 22.29 ? 470  HIS C CD2 1 
ATOM   12992 C  CE1 . HIS C 1 478 ? 10.780  5.294   94.543  1.00 25.78 ? 470  HIS C CE1 1 
ATOM   12993 N  NE2 . HIS C 1 478 ? 10.508  6.355   93.806  1.00 23.49 ? 470  HIS C NE2 1 
ATOM   12994 N  N   . GLN C 1 479 ? 12.730  8.559   99.977  1.00 9.72  ? 471  GLN C N   1 
ATOM   12995 C  CA  . GLN C 1 479 ? 12.975  9.684   100.870 1.00 9.75  ? 471  GLN C CA  1 
ATOM   12996 C  C   . GLN C 1 479 ? 14.463  9.806   101.171 1.00 12.80 ? 471  GLN C C   1 
ATOM   12997 O  O   . GLN C 1 479 ? 15.037  8.900   101.798 1.00 13.01 ? 471  GLN C O   1 
ATOM   12998 C  CB  . GLN C 1 479 ? 12.203  9.527   102.175 1.00 10.27 ? 471  GLN C CB  1 
ATOM   12999 C  CG  . GLN C 1 479 ? 10.685  9.693   102.055 1.00 12.12 ? 471  GLN C CG  1 
ATOM   13000 C  CD  . GLN C 1 479 ? 9.958   9.077   103.231 1.00 12.49 ? 471  GLN C CD  1 
ATOM   13001 O  OE1 . GLN C 1 479 ? 10.548  8.335   103.995 1.00 12.57 ? 471  GLN C OE1 1 
ATOM   13002 N  NE2 . GLN C 1 479 ? 8.670   9.355   103.358 1.00 12.53 ? 471  GLN C NE2 1 
ATOM   13003 N  N   . PRO C 1 480 ? 15.117  10.891  100.757 1.00 9.11  ? 472  PRO C N   1 
ATOM   13004 C  CA  . PRO C 1 480 ? 16.541  11.049  101.051 1.00 8.84  ? 472  PRO C CA  1 
ATOM   13005 C  C   . PRO C 1 480 ? 16.788  11.179  102.542 1.00 10.15 ? 472  PRO C C   1 
ATOM   13006 O  O   . PRO C 1 480 ? 15.985  11.754  103.277 1.00 11.39 ? 472  PRO C O   1 
ATOM   13007 C  CB  . PRO C 1 480 ? 16.919  12.343  100.315 1.00 9.56  ? 472  PRO C CB  1 
ATOM   13008 C  CG  . PRO C 1 480 ? 15.861  12.499  99.243  1.00 11.02 ? 472  PRO C CG  1 
ATOM   13009 C  CD  . PRO C 1 480 ? 14.601  11.981  99.908  1.00 10.27 ? 472  PRO C CD  1 
ATOM   13010 N  N   . ILE C 1 481 ? 17.920  10.629  102.974 1.00 10.14 ? 473  ILE C N   1 
ATOM   13011 C  CA  . ILE C 1 481 ? 18.410  10.754  104.344 1.00 10.24 ? 473  ILE C CA  1 
ATOM   13012 C  C   . ILE C 1 481 ? 19.848  11.255  104.270 1.00 9.02  ? 473  ILE C C   1 
ATOM   13013 O  O   . ILE C 1 481 ? 20.178  12.343  104.755 1.00 12.38 ? 473  ILE C O   1 
ATOM   13014 C  CB  . ILE C 1 481 ? 18.337  9.416   105.102 1.00 12.49 ? 473  ILE C CB  1 
ATOM   13015 C  CG1 . ILE C 1 481 ? 16.889  8.896   105.179 1.00 12.27 ? 473  ILE C CG1 1 
ATOM   13016 C  CG2 . ILE C 1 481 ? 18.983  9.555   106.493 1.00 18.27 ? 473  ILE C CG2 1 
ATOM   13017 C  CD1 . ILE C 1 481 ? 15.954  9.748   106.063 1.00 10.75 ? 473  ILE C CD1 1 
ATOM   13018 N  N   . GLU C 1 482 ? 20.705  10.472  103.627 1.00 10.34 ? 474  GLU C N   1 
ATOM   13019 C  CA  . GLU C 1 482 ? 22.133  10.741  103.617 1.00 8.62  ? 474  GLU C CA  1 
ATOM   13020 C  C   . GLU C 1 482 ? 22.611  11.429  102.346 1.00 11.45 ? 474  GLU C C   1 
ATOM   13021 O  O   . GLU C 1 482 ? 23.763  11.877  102.298 1.00 11.70 ? 474  GLU C O   1 
ATOM   13022 C  CB  . GLU C 1 482 ? 22.901  9.424   103.829 1.00 15.16 ? 474  GLU C CB  1 
ATOM   13023 C  CG  . GLU C 1 482 ? 22.844  8.402   102.669 1.00 8.49  ? 474  GLU C CG  1 
ATOM   13024 C  CD  . GLU C 1 482 ? 21.623  7.460   102.668 1.00 12.43 ? 474  GLU C CD  1 
ATOM   13025 O  OE1 . GLU C 1 482 ? 20.503  7.868   103.055 1.00 9.20  ? 474  GLU C OE1 1 
ATOM   13026 O  OE2 . GLU C 1 482 ? 21.788  6.290   102.250 1.00 12.48 ? 474  GLU C OE2 1 
ATOM   13027 N  N   . GLN C 1 483 ? 21.755  11.561  101.333 1.00 11.55 ? 475  GLN C N   1 
ATOM   13028 C  CA  . GLN C 1 483 ? 22.230  11.964  100.014 1.00 10.22 ? 475  GLN C CA  1 
ATOM   13029 C  C   . GLN C 1 483 ? 22.846  13.360  100.028 1.00 8.03  ? 475  GLN C C   1 
ATOM   13030 O  O   . GLN C 1 483 ? 23.915  13.571  99.454  1.00 11.39 ? 475  GLN C O   1 
ATOM   13031 C  CB  . GLN C 1 483 ? 21.091  11.885  98.995  1.00 12.63 ? 475  GLN C CB  1 
ATOM   13032 C  CG  . GLN C 1 483 ? 20.775  10.454  98.539  1.00 12.00 ? 475  GLN C CG  1 
ATOM   13033 C  CD  . GLN C 1 483 ? 20.209  9.595   99.669  1.00 14.74 ? 475  GLN C CD  1 
ATOM   13034 O  OE1 . GLN C 1 483 ? 19.458  10.080  100.518 1.00 11.57 ? 475  GLN C OE1 1 
ATOM   13035 N  NE2 . GLN C 1 483 ? 20.593  8.334   99.700  1.00 11.77 ? 475  GLN C NE2 1 
ATOM   13036 N  N   . THR C 1 484 ? 22.169  14.338  100.639 1.00 8.03  ? 476  THR C N   1 
ATOM   13037 C  CA  . THR C 1 484 ? 22.738  15.684  100.659 1.00 12.27 ? 476  THR C CA  1 
ATOM   13038 C  C   . THR C 1 484 ? 24.105  15.691  101.328 1.00 13.16 ? 476  THR C C   1 
ATOM   13039 O  O   . THR C 1 484 ? 25.054  16.303  100.820 1.00 11.48 ? 476  THR C O   1 
ATOM   13040 C  CB  . THR C 1 484 ? 21.784  16.652  101.359 1.00 11.08 ? 476  THR C CB  1 
ATOM   13041 O  OG1 . THR C 1 484 ? 20.549  16.709  100.622 1.00 13.76 ? 476  THR C OG1 1 
ATOM   13042 C  CG2 . THR C 1 484 ? 22.389  18.034  101.436 1.00 14.94 ? 476  THR C CG2 1 
ATOM   13043 N  N   . ALA C 1 485 ? 24.236  14.986  102.452 1.00 11.51 ? 477  ALA C N   1 
ATOM   13044 C  CA  . ALA C 1 485 ? 25.529  14.914  103.123 1.00 12.14 ? 477  ALA C CA  1 
ATOM   13045 C  C   . ALA C 1 485 ? 26.596  14.284  102.225 1.00 13.38 ? 477  ALA C C   1 
ATOM   13046 O  O   . ALA C 1 485 ? 27.755  14.722  102.233 1.00 10.58 ? 477  ALA C O   1 
ATOM   13047 C  CB  . ALA C 1 485 ? 25.398  14.144  104.440 1.00 9.97  ? 477  ALA C CB  1 
ATOM   13048 N  N   . THR C 1 486 ? 26.235  13.247  101.457 1.00 10.41 ? 478  THR C N   1 
ATOM   13049 C  CA  . THR C 1 486 ? 27.224  12.612  100.578 1.00 12.59 ? 478  THR C CA  1 
ATOM   13050 C  C   . THR C 1 486 ? 27.595  13.518  99.407  1.00 10.24 ? 478  THR C C   1 
ATOM   13051 O  O   . THR C 1 486 ? 28.761  13.539  98.973  1.00 8.18  ? 478  THR C O   1 
ATOM   13052 C  CB  . THR C 1 486 ? 26.724  11.251  100.065 1.00 9.29  ? 478  THR C CB  1 
ATOM   13053 O  OG1 . THR C 1 486 ? 25.581  11.423  99.214  1.00 9.88  ? 478  THR C OG1 1 
ATOM   13054 C  CG2 . THR C 1 486 ? 26.372  10.323  101.229 1.00 12.68 ? 478  THR C CG2 1 
ATOM   13055 N  N   . LEU C 1 487 ? 26.621  14.259  98.867  1.00 11.32 ? 479  LEU C N   1 
ATOM   13056 C  CA  . LEU C 1 487 ? 26.916  15.170  97.759  1.00 7.86  ? 479  LEU C CA  1 
ATOM   13057 C  C   . LEU C 1 487 ? 27.887  16.260  98.179  1.00 10.87 ? 479  LEU C C   1 
ATOM   13058 O  O   . LEU C 1 487 ? 28.717  16.703  97.368  1.00 10.18 ? 479  LEU C O   1 
ATOM   13059 C  CB  . LEU C 1 487 ? 25.630  15.800  97.231  1.00 10.21 ? 479  LEU C CB  1 
ATOM   13060 C  CG  . LEU C 1 487 ? 24.661  14.863  96.510  1.00 10.46 ? 479  LEU C CG  1 
ATOM   13061 C  CD1 . LEU C 1 487 ? 23.323  15.579  96.249  1.00 8.99  ? 479  LEU C CD1 1 
ATOM   13062 C  CD2 . LEU C 1 487 ? 25.270  14.394  95.210  1.00 13.91 ? 479  LEU C CD2 1 
ATOM   13063 N  N   . ARG C 1 488 ? 27.816  16.689  99.447  1.00 8.68  ? 480  ARG C N   1 
ATOM   13064 C  CA  . ARG C 1 488 ? 28.733  17.711  99.937  1.00 11.12 ? 480  ARG C CA  1 
ATOM   13065 C  C   . ARG C 1 488 ? 30.175  17.231  99.961  1.00 14.38 ? 480  ARG C C   1 
ATOM   13066 O  O   . ARG C 1 488 ? 31.087  18.057  100.075 1.00 10.34 ? 480  ARG C O   1 
ATOM   13067 C  CB  . ARG C 1 488 ? 28.319  18.165  101.349 1.00 10.49 ? 480  ARG C CB  1 
ATOM   13068 C  CG  . ARG C 1 488 ? 27.042  19.004  101.387 1.00 14.30 ? 480  ARG C CG  1 
ATOM   13069 C  CD  . ARG C 1 488 ? 26.536  19.212  102.819 1.00 10.13 ? 480  ARG C CD  1 
ATOM   13070 N  NE  . ARG C 1 488 ? 25.392  20.128  102.847 1.00 14.03 ? 480  ARG C NE  1 
ATOM   13071 C  CZ  . ARG C 1 488 ? 24.339  19.984  103.644 1.00 11.59 ? 480  ARG C CZ  1 
ATOM   13072 N  NH1 . ARG C 1 488 ? 24.258  18.954  104.479 1.00 13.33 ? 480  ARG C NH1 1 
ATOM   13073 N  NH2 . ARG C 1 488 ? 23.359  20.869  103.601 1.00 12.08 ? 480  ARG C NH2 1 
ATOM   13074 N  N   . LEU C 1 489 ? 30.407  15.920  99.889  1.00 13.35 ? 481  LEU C N   1 
ATOM   13075 C  CA  . LEU C 1 489 ? 31.768  15.404  99.973  1.00 10.58 ? 481  LEU C CA  1 
ATOM   13076 C  C   . LEU C 1 489 ? 32.444  15.287  98.615  1.00 10.62 ? 481  LEU C C   1 
ATOM   13077 O  O   . LEU C 1 489 ? 33.634  14.951  98.566  1.00 13.69 ? 481  LEU C O   1 
ATOM   13078 C  CB  . LEU C 1 489 ? 31.788  14.041  100.679 1.00 8.22  ? 481  LEU C CB  1 
ATOM   13079 C  CG  . LEU C 1 489 ? 31.262  14.075  102.127 1.00 11.89 ? 481  LEU C CG  1 
ATOM   13080 C  CD1 . LEU C 1 489 ? 31.357  12.712  102.785 1.00 16.51 ? 481  LEU C CD1 1 
ATOM   13081 C  CD2 . LEU C 1 489 ? 31.978  15.142  102.963 1.00 12.81 ? 481  LEU C CD2 1 
ATOM   13082 N  N   . ILE C 1 490 ? 31.733  15.565  97.523  1.00 8.12  ? 482  ILE C N   1 
ATOM   13083 C  CA  . ILE C 1 490 ? 32.350  15.547  96.197  1.00 11.86 ? 482  ILE C CA  1 
ATOM   13084 C  C   . ILE C 1 490 ? 33.292  16.737  96.104  1.00 10.89 ? 482  ILE C C   1 
ATOM   13085 O  O   . ILE C 1 490 ? 32.864  17.882  96.303  1.00 8.88  ? 482  ILE C O   1 
ATOM   13086 C  CB  . ILE C 1 490 ? 31.314  15.596  95.063  1.00 10.48 ? 482  ILE C CB  1 
ATOM   13087 C  CG1 . ILE C 1 490 ? 30.330  14.434  95.191  1.00 7.79  ? 482  ILE C CG1 1 
ATOM   13088 C  CG2 . ILE C 1 490 ? 32.048  15.560  93.683  1.00 11.37 ? 482  ILE C CG2 1 
ATOM   13089 C  CD1 . ILE C 1 490 ? 29.183  14.505  94.198  1.00 14.49 ? 482  ILE C CD1 1 
ATOM   13090 N  N   . PRO C 1 491 ? 34.571  16.523  95.826  1.00 12.56 ? 483  PRO C N   1 
ATOM   13091 C  CA  . PRO C 1 491 ? 35.475  17.665  95.665  1.00 16.59 ? 483  PRO C CA  1 
ATOM   13092 C  C   . PRO C 1 491 ? 35.034  18.514  94.478  1.00 13.59 ? 483  PRO C C   1 
ATOM   13093 O  O   . PRO C 1 491 ? 34.509  17.999  93.491  1.00 14.53 ? 483  PRO C O   1 
ATOM   13094 C  CB  . PRO C 1 491 ? 36.843  17.007  95.437  1.00 11.82 ? 483  PRO C CB  1 
ATOM   13095 C  CG  . PRO C 1 491 ? 36.703  15.624  96.048  1.00 11.61 ? 483  PRO C CG  1 
ATOM   13096 C  CD  . PRO C 1 491 ? 35.275  15.233  95.719  1.00 11.63 ? 483  PRO C CD  1 
ATOM   13097 N  N   . ASN C 1 492 ? 35.202  19.834  94.611  1.00 12.65 ? 484  ASN C N   1 
ATOM   13098 C  CA  . ASN C 1 492 ? 34.894  20.802  93.543  1.00 13.91 ? 484  ASN C CA  1 
ATOM   13099 C  C   . ASN C 1 492 ? 33.412  20.796  93.150  1.00 14.58 ? 484  ASN C C   1 
ATOM   13100 O  O   . ASN C 1 492 ? 33.065  20.948  91.978  1.00 11.85 ? 484  ASN C O   1 
ATOM   13101 C  CB  . ASN C 1 492 ? 35.760  20.571  92.303  1.00 11.91 ? 484  ASN C CB  1 
ATOM   13102 C  CG  . ASN C 1 492 ? 35.776  21.782  91.386  1.00 16.12 ? 484  ASN C CG  1 
ATOM   13103 O  OD1 . ASN C 1 492 ? 35.850  22.914  91.860  1.00 15.07 ? 484  ASN C OD1 1 
ATOM   13104 N  ND2 . ASN C 1 492 ? 35.674  21.555  90.080  1.00 10.95 ? 484  ASN C ND2 1 
ATOM   13105 N  N   . MET C 1 493 ? 32.528  20.624  94.126  1.00 14.56 ? 485  MET C N   1 
ATOM   13106 C  CA  . MET C 1 493 ? 31.085  20.628  93.874  1.00 14.37 ? 485  MET C CA  1 
ATOM   13107 C  C   . MET C 1 493 ? 30.407  21.572  94.857  1.00 17.41 ? 485  MET C C   1 
ATOM   13108 O  O   . MET C 1 493 ? 30.696  21.524  96.055  1.00 17.63 ? 485  MET C O   1 
ATOM   13109 C  CB  . MET C 1 493 ? 30.491  19.212  94.012  1.00 15.13 ? 485  MET C CB  1 
ATOM   13110 C  CG  . MET C 1 493 ? 28.953  19.160  94.005  1.00 15.98 ? 485  MET C CG  1 
ATOM   13111 S  SD  . MET C 1 493 ? 28.270  19.476  92.363  1.00 14.14 ? 485  MET C SD  1 
ATOM   13112 C  CE  . MET C 1 493 ? 28.549  17.882  91.569  1.00 10.81 ? 485  MET C CE  1 
ATOM   13113 N  N   . ASP C 1 494 ? 29.508  22.423  94.357  1.00 13.95 ? 486  ASP C N   1 
ATOM   13114 C  CA  . ASP C 1 494 ? 28.678  23.270  95.209  1.00 14.91 ? 486  ASP C CA  1 
ATOM   13115 C  C   . ASP C 1 494 ? 27.332  22.591  95.425  1.00 18.80 ? 486  ASP C C   1 
ATOM   13116 O  O   . ASP C 1 494 ? 26.663  22.231  94.457  1.00 16.00 ? 486  ASP C O   1 
ATOM   13117 C  CB  . ASP C 1 494 ? 28.457  24.645  94.578  1.00 17.07 ? 486  ASP C CB  1 
ATOM   13118 C  CG  . ASP C 1 494 ? 29.645  25.564  94.743  1.00 18.07 ? 486  ASP C CG  1 
ATOM   13119 O  OD1 . ASP C 1 494 ? 30.603  25.192  95.446  1.00 14.17 ? 486  ASP C OD1 1 
ATOM   13120 O  OD2 . ASP C 1 494 ? 29.604  26.668  94.175  1.00 18.19 ? 486  ASP C OD2 1 
ATOM   13121 N  N   . VAL C 1 495 ? 26.935  22.426  96.684  1.00 11.10 ? 487  VAL C N   1 
ATOM   13122 C  CA  . VAL C 1 495 ? 25.633  21.862  97.035  1.00 10.31 ? 487  VAL C CA  1 
ATOM   13123 C  C   . VAL C 1 495 ? 24.804  22.983  97.648  1.00 13.56 ? 487  VAL C C   1 
ATOM   13124 O  O   . VAL C 1 495 ? 25.216  23.592  98.638  1.00 12.87 ? 487  VAL C O   1 
ATOM   13125 C  CB  . VAL C 1 495 ? 25.762  20.676  98.003  1.00 9.88  ? 487  VAL C CB  1 
ATOM   13126 C  CG1 . VAL C 1 495 ? 24.391  20.196  98.418  1.00 11.70 ? 487  VAL C CG1 1 
ATOM   13127 C  CG2 . VAL C 1 495 ? 26.553  19.524  97.354  1.00 13.55 ? 487  VAL C CG2 1 
ATOM   13128 N  N   . TRP C 1 496 ? 23.659  23.279  97.038  1.00 9.26  ? 488  TRP C N   1 
ATOM   13129 C  CA  . TRP C 1 496 ? 22.751  24.321  97.490  1.00 12.25 ? 488  TRP C CA  1 
ATOM   13130 C  C   . TRP C 1 496 ? 21.435  23.687  97.928  1.00 12.97 ? 488  TRP C C   1 
ATOM   13131 O  O   . TRP C 1 496 ? 20.888  22.831  97.224  1.00 11.36 ? 488  TRP C O   1 
ATOM   13132 C  CB  . TRP C 1 496 ? 22.461  25.344  96.374  1.00 13.65 ? 488  TRP C CB  1 
ATOM   13133 C  CG  . TRP C 1 496 ? 23.603  26.257  96.001  1.00 11.69 ? 488  TRP C CG  1 
ATOM   13134 C  CD1 . TRP C 1 496 ? 24.559  26.037  95.036  1.00 15.05 ? 488  TRP C CD1 1 
ATOM   13135 C  CD2 . TRP C 1 496 ? 23.883  27.548  96.549  1.00 10.87 ? 488  TRP C CD2 1 
ATOM   13136 N  NE1 . TRP C 1 496 ? 25.421  27.113  94.967  1.00 14.94 ? 488  TRP C NE1 1 
ATOM   13137 C  CE2 . TRP C 1 496 ? 25.040  28.042  95.899  1.00 15.50 ? 488  TRP C CE2 1 
ATOM   13138 C  CE3 . TRP C 1 496 ? 23.298  28.321  97.559  1.00 13.21 ? 488  TRP C CE3 1 
ATOM   13139 C  CZ2 . TRP C 1 496 ? 25.596  29.295  96.201  1.00 15.50 ? 488  TRP C CZ2 1 
ATOM   13140 C  CZ3 . TRP C 1 496 ? 23.859  29.558  97.862  1.00 14.68 ? 488  TRP C CZ3 1 
ATOM   13141 C  CH2 . TRP C 1 496 ? 24.987  30.034  97.179  1.00 17.66 ? 488  TRP C CH2 1 
ATOM   13142 N  N   . ARG C 1 497 ? 20.918  24.125  99.081  1.00 10.42 ? 489  ARG C N   1 
ATOM   13143 C  CA  . ARG C 1 497 ? 19.615  23.682  99.591  1.00 10.60 ? 489  ARG C CA  1 
ATOM   13144 C  C   . ARG C 1 497 ? 18.847  24.921  100.040 1.00 13.13 ? 489  ARG C C   1 
ATOM   13145 O  O   . ARG C 1 497 ? 18.757  25.220  101.241 1.00 13.26 ? 489  ARG C O   1 
ATOM   13146 C  CB  . ARG C 1 497 ? 19.772  22.672  100.726 1.00 11.22 ? 489  ARG C CB  1 
ATOM   13147 C  CG  . ARG C 1 497 ? 18.463  21.944  101.093 1.00 9.47  ? 489  ARG C CG  1 
ATOM   13148 C  CD  . ARG C 1 497 ? 18.742  20.851  102.135 1.00 13.62 ? 489  ARG C CD  1 
ATOM   13149 N  NE  . ARG C 1 497 ? 17.548  20.079  102.455 1.00 14.73 ? 489  ARG C NE  1 
ATOM   13150 C  CZ  . ARG C 1 497 ? 16.822  20.231  103.561 1.00 15.41 ? 489  ARG C CZ  1 
ATOM   13151 N  NH1 . ARG C 1 497 ? 17.172  21.115  104.484 1.00 13.88 ? 489  ARG C NH1 1 
ATOM   13152 N  NH2 . ARG C 1 497 ? 15.750  19.476  103.754 1.00 16.54 ? 489  ARG C NH2 1 
ATOM   13153 N  N   . PRO C 1 498 ? 18.291  25.672  99.093  1.00 11.21 ? 490  PRO C N   1 
ATOM   13154 C  CA  . PRO C 1 498 ? 17.699  26.982  99.419  1.00 13.15 ? 490  PRO C CA  1 
ATOM   13155 C  C   . PRO C 1 498 ? 16.413  26.871  100.225 1.00 12.65 ? 490  PRO C C   1 
ATOM   13156 O  O   . PRO C 1 498 ? 15.625  25.936  100.058 1.00 13.25 ? 490  PRO C O   1 
ATOM   13157 C  CB  . PRO C 1 498 ? 17.416  27.588  98.039  1.00 16.14 ? 490  PRO C CB  1 
ATOM   13158 C  CG  . PRO C 1 498 ? 17.223  26.380  97.142  1.00 18.78 ? 490  PRO C CG  1 
ATOM   13159 C  CD  . PRO C 1 498 ? 18.254  25.385  97.647  1.00 9.73  ? 490  PRO C CD  1 
ATOM   13160 N  N   . CYS C 1 499 ? 16.164  27.885  101.065 1.00 13.43 ? 491  CYS C N   1 
ATOM   13161 C  CA  . CYS C 1 499 ? 14.996  27.841  101.936 1.00 16.04 ? 491  CYS C CA  1 
ATOM   13162 C  C   . CYS C 1 499 ? 13.787  28.587  101.386 1.00 21.19 ? 491  CYS C C   1 
ATOM   13163 O  O   . CYS C 1 499 ? 12.690  28.435  101.937 1.00 18.91 ? 491  CYS C O   1 
ATOM   13164 C  CB  . CYS C 1 499 ? 15.337  28.393  103.329 1.00 21.08 ? 491  CYS C CB  1 
ATOM   13165 S  SG  . CYS C 1 499 ? 15.539  30.206  103.446 1.00 20.13 ? 491  CYS C SG  1 
ATOM   13166 N  N   . ASP C 1 500 ? 13.943  29.392  100.341 1.00 15.48 ? 492  ASP C N   1 
ATOM   13167 C  CA  . ASP C 1 500 ? 12.808  30.135  99.795  1.00 17.81 ? 492  ASP C CA  1 
ATOM   13168 C  C   . ASP C 1 500 ? 13.175  30.624  98.402  1.00 16.02 ? 492  ASP C C   1 
ATOM   13169 O  O   . ASP C 1 500 ? 14.223  30.260  97.857  1.00 15.68 ? 492  ASP C O   1 
ATOM   13170 C  CB  . ASP C 1 500 ? 12.385  31.284  100.718 1.00 20.73 ? 492  ASP C CB  1 
ATOM   13171 C  CG  . ASP C 1 500 ? 13.483  32.311  100.946 1.00 22.31 ? 492  ASP C CG  1 
ATOM   13172 O  OD1 . ASP C 1 500 ? 14.376  32.491  100.088 1.00 23.01 ? 492  ASP C OD1 1 
ATOM   13173 O  OD2 . ASP C 1 500 ? 13.443  32.960  102.006 1.00 27.36 ? 492  ASP C OD2 1 
ATOM   13174 N  N   . THR C 1 501 ? 12.301  31.453  97.829  1.00 15.78 ? 493  THR C N   1 
ATOM   13175 C  CA  . THR C 1 501 ? 12.475  31.892  96.452  1.00 21.11 ? 493  THR C CA  1 
ATOM   13176 C  C   . THR C 1 501 ? 13.684  32.810  96.299  1.00 18.23 ? 493  THR C C   1 
ATOM   13177 O  O   . THR C 1 501 ? 14.317  32.818  95.240  1.00 16.26 ? 493  THR C O   1 
ATOM   13178 C  CB  . THR C 1 501 ? 11.202  32.595  95.961  1.00 27.93 ? 493  THR C CB  1 
ATOM   13179 O  OG1 . THR C 1 501 ? 10.952  33.754  96.765  1.00 34.43 ? 493  THR C OG1 1 
ATOM   13180 C  CG2 . THR C 1 501 ? 10.002  31.670  96.062  1.00 22.38 ? 493  THR C CG2 1 
ATOM   13181 N  N   . ALA C 1 502 ? 14.025  33.586  97.331  1.00 16.55 ? 494  ALA C N   1 
ATOM   13182 C  CA  . ALA C 1 502 ? 15.216  34.430  97.233  1.00 17.52 ? 494  ALA C CA  1 
ATOM   13183 C  C   . ALA C 1 502 ? 16.478  33.583  97.183  1.00 14.61 ? 494  ALA C C   1 
ATOM   13184 O  O   . ALA C 1 502 ? 17.314  33.753  96.286  1.00 14.73 ? 494  ALA C O   1 
ATOM   13185 C  CB  . ALA C 1 502 ? 15.278  35.421  98.400  1.00 19.87 ? 494  ALA C CB  1 
ATOM   13186 N  N   . GLU C 1 503 ? 16.628  32.649  98.136  1.00 13.49 ? 495  GLU C N   1 
ATOM   13187 C  CA  . GLU C 1 503 ? 17.786  31.759  98.118  1.00 13.85 ? 495  GLU C CA  1 
ATOM   13188 C  C   . GLU C 1 503 ? 17.797  30.888  96.867  1.00 13.63 ? 495  GLU C C   1 
ATOM   13189 O  O   . GLU C 1 503 ? 18.868  30.524  96.377  1.00 13.38 ? 495  GLU C O   1 
ATOM   13190 C  CB  . GLU C 1 503 ? 17.813  30.871  99.370  1.00 11.95 ? 495  GLU C CB  1 
ATOM   13191 C  CG  . GLU C 1 503 ? 18.007  31.626  100.690 1.00 12.47 ? 495  GLU C CG  1 
ATOM   13192 C  CD  . GLU C 1 503 ? 18.436  30.716  101.839 1.00 19.07 ? 495  GLU C CD  1 
ATOM   13193 O  OE1 . GLU C 1 503 ? 18.340  29.478  101.690 1.00 15.34 ? 495  GLU C OE1 1 
ATOM   13194 O  OE2 . GLU C 1 503 ? 18.867  31.244  102.892 1.00 18.83 ? 495  GLU C OE2 1 
ATOM   13195 N  N   . SER C 1 504 ? 16.621  30.547  96.335  1.00 12.97 ? 496  SER C N   1 
ATOM   13196 C  CA  A SER C 1 504 ? 16.572  29.748  95.112  0.46 15.30 ? 496  SER C CA  1 
ATOM   13197 C  CA  B SER C 1 504 ? 16.570  29.748  95.114  0.54 15.35 ? 496  SER C CA  1 
ATOM   13198 C  C   . SER C 1 504 ? 17.179  30.505  93.938  1.00 11.23 ? 496  SER C C   1 
ATOM   13199 O  O   . SER C 1 504 ? 17.982  29.951  93.172  1.00 12.45 ? 496  SER C O   1 
ATOM   13200 C  CB  A SER C 1 504 ? 15.133  29.343  94.793  0.46 16.17 ? 496  SER C CB  1 
ATOM   13201 C  CB  B SER C 1 504 ? 15.126  29.349  94.813  0.54 16.22 ? 496  SER C CB  1 
ATOM   13202 O  OG  A SER C 1 504 ? 14.651  28.393  95.722  0.46 16.64 ? 496  SER C OG  1 
ATOM   13203 O  OG  B SER C 1 504 ? 15.040  28.653  93.588  0.54 18.36 ? 496  SER C OG  1 
ATOM   13204 N  N   . LEU C 1 505 ? 16.804  31.775  93.778  1.00 13.22 ? 497  LEU C N   1 
ATOM   13205 C  CA  . LEU C 1 505 ? 17.339  32.567  92.673  1.00 12.33 ? 497  LEU C CA  1 
ATOM   13206 C  C   . LEU C 1 505 ? 18.850  32.713  92.786  1.00 14.83 ? 497  LEU C C   1 
ATOM   13207 O  O   . LEU C 1 505 ? 19.577  32.510  91.805  1.00 12.32 ? 497  LEU C O   1 
ATOM   13208 C  CB  . LEU C 1 505 ? 16.669  33.942  92.630  1.00 12.72 ? 497  LEU C CB  1 
ATOM   13209 C  CG  . LEU C 1 505 ? 17.202  34.855  91.526  1.00 12.96 ? 497  LEU C CG  1 
ATOM   13210 C  CD1 . LEU C 1 505 ? 17.199  34.121  90.180  1.00 20.79 ? 497  LEU C CD1 1 
ATOM   13211 C  CD2 . LEU C 1 505 ? 16.385  36.131  91.423  1.00 13.79 ? 497  LEU C CD2 1 
ATOM   13212 N  N   . VAL C 1 506 ? 19.345  33.043  93.981  1.00 16.71 ? 498  VAL C N   1 
ATOM   13213 C  CA  . VAL C 1 506 ? 20.787  33.170  94.173  1.00 15.86 ? 498  VAL C CA  1 
ATOM   13214 C  C   . VAL C 1 506 ? 21.495  31.854  93.861  1.00 14.81 ? 498  VAL C C   1 
ATOM   13215 O  O   . VAL C 1 506 ? 22.539  31.841  93.196  1.00 13.44 ? 498  VAL C O   1 
ATOM   13216 C  CB  . VAL C 1 506 ? 21.105  33.653  95.599  1.00 14.14 ? 498  VAL C CB  1 
ATOM   13217 C  CG1 . VAL C 1 506 ? 22.612  33.633  95.829  1.00 13.87 ? 498  VAL C CG1 1 
ATOM   13218 C  CG2 . VAL C 1 506 ? 20.540  35.073  95.828  1.00 14.09 ? 498  VAL C CG2 1 
ATOM   13219 N  N   . ALA C 1 507 ? 20.950  30.728  94.343  1.00 14.39 ? 499  ALA C N   1 
ATOM   13220 C  CA  . ALA C 1 507 ? 21.572  29.433  94.073  1.00 10.05 ? 499  ALA C CA  1 
ATOM   13221 C  C   . ALA C 1 507 ? 21.681  29.181  92.575  1.00 11.41 ? 499  ALA C C   1 
ATOM   13222 O  O   . ALA C 1 507 ? 22.741  28.795  92.074  1.00 13.91 ? 499  ALA C O   1 
ATOM   13223 C  CB  . ALA C 1 507 ? 20.784  28.311  94.748  1.00 11.97 ? 499  ALA C CB  1 
ATOM   13224 N  N   . TRP C 1 508 ? 20.584  29.395  91.843  1.00 16.92 ? 500  TRP C N   1 
ATOM   13225 C  CA  . TRP C 1 508 ? 20.598  29.251  90.390  1.00 15.51 ? 500  TRP C CA  1 
ATOM   13226 C  C   . TRP C 1 508 ? 21.630  30.178  89.744  1.00 15.59 ? 500  TRP C C   1 
ATOM   13227 O  O   . TRP C 1 508 ? 22.429  29.752  88.898  1.00 14.38 ? 500  TRP C O   1 
ATOM   13228 C  CB  . TRP C 1 508 ? 19.195  29.533  89.839  1.00 13.69 ? 500  TRP C CB  1 
ATOM   13229 C  CG  . TRP C 1 508 ? 18.323  28.323  89.740  1.00 15.85 ? 500  TRP C CG  1 
ATOM   13230 C  CD1 . TRP C 1 508 ? 17.267  27.990  90.550  1.00 16.96 ? 500  TRP C CD1 1 
ATOM   13231 C  CD2 . TRP C 1 508 ? 18.420  27.282  88.762  1.00 16.31 ? 500  TRP C CD2 1 
ATOM   13232 N  NE1 . TRP C 1 508 ? 16.722  26.796  90.146  1.00 15.58 ? 500  TRP C NE1 1 
ATOM   13233 C  CE2 . TRP C 1 508 ? 17.398  26.348  89.042  1.00 14.29 ? 500  TRP C CE2 1 
ATOM   13234 C  CE3 . TRP C 1 508 ? 19.272  27.048  87.675  1.00 11.73 ? 500  TRP C CE3 1 
ATOM   13235 C  CZ2 . TRP C 1 508 ? 17.207  25.196  88.271  1.00 17.22 ? 500  TRP C CZ2 1 
ATOM   13236 C  CZ3 . TRP C 1 508 ? 19.080  25.909  86.907  1.00 14.70 ? 500  TRP C CZ3 1 
ATOM   13237 C  CH2 . TRP C 1 508 ? 18.058  25.000  87.205  1.00 16.71 ? 500  TRP C CH2 1 
ATOM   13238 N  N   . ALA C 1 509 ? 21.625  31.450  90.135  1.00 10.60 ? 501  ALA C N   1 
ATOM   13239 C  CA  . ALA C 1 509 ? 22.535  32.431  89.548  1.00 13.37 ? 501  ALA C CA  1 
ATOM   13240 C  C   . ALA C 1 509 ? 23.997  32.076  89.807  1.00 16.25 ? 501  ALA C C   1 
ATOM   13241 O  O   . ALA C 1 509 ? 24.840  32.206  88.911  1.00 14.52 ? 501  ALA C O   1 
ATOM   13242 C  CB  . ALA C 1 509 ? 22.226  33.817  90.103  1.00 13.51 ? 501  ALA C CB  1 
ATOM   13243 N  N   . GLU C 1 510 ? 24.323  31.670  91.040  1.00 13.45 ? 502  GLU C N   1 
ATOM   13244 C  CA  . GLU C 1 510 ? 25.700  31.294  91.352  1.00 11.54 ? 502  GLU C CA  1 
ATOM   13245 C  C   . GLU C 1 510 ? 26.099  30.026  90.617  1.00 15.30 ? 502  GLU C C   1 
ATOM   13246 O  O   . GLU C 1 510 ? 27.248  29.899  90.181  1.00 15.06 ? 502  GLU C O   1 
ATOM   13247 C  CB  . GLU C 1 510 ? 25.879  31.099  92.858  1.00 16.51 ? 502  GLU C CB  1 
ATOM   13248 C  CG  . GLU C 1 510 ? 25.757  32.366  93.680  1.00 16.79 ? 502  GLU C CG  1 
ATOM   13249 C  CD  . GLU C 1 510 ? 26.815  33.409  93.329  1.00 20.78 ? 502  GLU C CD  1 
ATOM   13250 O  OE1 . GLU C 1 510 ? 28.016  33.076  93.315  1.00 19.01 ? 502  GLU C OE1 1 
ATOM   13251 O  OE2 . GLU C 1 510 ? 26.445  34.565  93.069  1.00 17.17 ? 502  GLU C OE2 1 
ATOM   13252 N  N   . ALA C 1 511 ? 25.169  29.064  90.495  1.00 11.99 ? 503  ALA C N   1 
ATOM   13253 C  CA  . ALA C 1 511 ? 25.450  27.853  89.732  1.00 14.08 ? 503  ALA C CA  1 
ATOM   13254 C  C   . ALA C 1 511 ? 25.752  28.177  88.276  1.00 14.85 ? 503  ALA C C   1 
ATOM   13255 O  O   . ALA C 1 511 ? 26.681  27.609  87.679  1.00 11.28 ? 503  ALA C O   1 
ATOM   13256 C  CB  . ALA C 1 511 ? 24.269  26.888  89.816  1.00 10.12 ? 503  ALA C CB  1 
ATOM   13257 N  N   . ALA C 1 512 ? 24.963  29.083  87.686  1.00 13.34 ? 504  ALA C N   1 
ATOM   13258 C  CA  . ALA C 1 512 ? 25.173  29.488  86.298  1.00 14.34 ? 504  ALA C CA  1 
ATOM   13259 C  C   . ALA C 1 512 ? 26.444  30.309  86.139  1.00 15.09 ? 504  ALA C C   1 
ATOM   13260 O  O   . ALA C 1 512 ? 27.088  30.266  85.084  1.00 16.29 ? 504  ALA C O   1 
ATOM   13261 C  CB  . ALA C 1 512 ? 23.978  30.295  85.802  1.00 18.01 ? 504  ALA C CB  1 
ATOM   13262 N  N   . LYS C 1 513 ? 26.805  31.070  87.167  1.00 13.96 ? 505  LYS C N   1 
ATOM   13263 C  CA  . LYS C 1 513 ? 27.977  31.925  87.091  1.00 20.71 ? 505  LYS C CA  1 
ATOM   13264 C  C   . LYS C 1 513 ? 29.262  31.122  87.243  1.00 19.49 ? 505  LYS C C   1 
ATOM   13265 O  O   . LYS C 1 513 ? 30.303  31.538  86.742  1.00 19.08 ? 505  LYS C O   1 
ATOM   13266 C  CB  . LYS C 1 513 ? 27.876  32.997  88.174  1.00 26.89 ? 505  LYS C CB  1 
ATOM   13267 C  CG  . LYS C 1 513 ? 28.805  34.171  88.019  1.00 42.02 ? 505  LYS C CG  1 
ATOM   13268 C  CD  . LYS C 1 513 ? 28.544  35.175  89.140  1.00 40.90 ? 505  LYS C CD  1 
ATOM   13269 C  CE  . LYS C 1 513 ? 29.576  36.285  89.128  1.00 41.61 ? 505  LYS C CE  1 
ATOM   13270 N  NZ  . LYS C 1 513 ? 29.462  37.138  90.332  1.00 38.18 ? 505  LYS C NZ  1 
ATOM   13271 N  N   . ALA C 1 514 ? 29.201  29.989  87.942  1.00 14.94 ? 506  ALA C N   1 
ATOM   13272 C  CA  . ALA C 1 514 ? 30.371  29.159  88.201  1.00 19.22 ? 506  ALA C CA  1 
ATOM   13273 C  C   . ALA C 1 514 ? 31.003  28.697  86.897  1.00 22.31 ? 506  ALA C C   1 
ATOM   13274 O  O   . ALA C 1 514 ? 30.360  28.017  86.094  1.00 26.82 ? 506  ALA C O   1 
ATOM   13275 C  CB  . ALA C 1 514 ? 29.957  27.955  89.045  1.00 16.36 ? 506  ALA C CB  1 
ATOM   13276 N  N   . GLU C 1 515 ? 32.256  29.073  86.675  1.00 20.98 ? 507  GLU C N   1 
ATOM   13277 C  CA  . GLU C 1 515 ? 32.899  28.711  85.418  1.00 22.92 ? 507  GLU C CA  1 
ATOM   13278 C  C   . GLU C 1 515 ? 33.572  27.347  85.471  1.00 24.18 ? 507  GLU C C   1 
ATOM   13279 O  O   . GLU C 1 515 ? 33.666  26.666  84.439  1.00 24.43 ? 507  GLU C O   1 
ATOM   13280 C  CB  . GLU C 1 515 ? 33.925  29.777  85.022  1.00 27.67 ? 507  GLU C CB  1 
ATOM   13281 C  CG  . GLU C 1 515 ? 33.354  31.175  84.924  1.00 42.46 ? 507  GLU C CG  1 
ATOM   13282 C  CD  . GLU C 1 515 ? 34.196  32.088  84.058  1.00 56.36 ? 507  GLU C CD  1 
ATOM   13283 O  OE1 . GLU C 1 515 ? 33.874  32.237  82.860  1.00 61.68 ? 507  GLU C OE1 1 
ATOM   13284 O  OE2 . GLU C 1 515 ? 35.188  32.647  84.571  1.00 63.29 ? 507  GLU C OE2 1 
ATOM   13285 N  N   . ASP C 1 516 ? 34.020  26.913  86.649  1.00 17.84 ? 508  ASP C N   1 
ATOM   13286 C  CA  . ASP C 1 516 ? 34.926  25.773  86.726  1.00 14.15 ? 508  ASP C CA  1 
ATOM   13287 C  C   . ASP C 1 516 ? 34.443  24.689  87.689  1.00 14.05 ? 508  ASP C C   1 
ATOM   13288 O  O   . ASP C 1 516 ? 35.254  23.877  88.142  1.00 13.33 ? 508  ASP C O   1 
ATOM   13289 C  CB  . ASP C 1 516 ? 36.327  26.238  87.129  1.00 16.35 ? 508  ASP C CB  1 
ATOM   13290 C  CG  . ASP C 1 516 ? 36.376  26.782  88.545  1.00 27.42 ? 508  ASP C CG  1 
ATOM   13291 O  OD1 . ASP C 1 516 ? 35.313  27.152  89.094  1.00 24.36 ? 508  ASP C OD1 1 
ATOM   13292 O  OD2 . ASP C 1 516 ? 37.485  26.843  89.109  1.00 26.18 ? 508  ASP C OD2 1 
ATOM   13293 N  N   . HIS C 1 517 ? 33.156  24.654  88.021  1.00 11.83 ? 509  HIS C N   1 
ATOM   13294 C  CA  . HIS C 1 517 ? 32.664  23.590  88.883  1.00 10.96 ? 509  HIS C CA  1 
ATOM   13295 C  C   . HIS C 1 517 ? 31.155  23.446  88.716  1.00 10.26 ? 509  HIS C C   1 
ATOM   13296 O  O   . HIS C 1 517 ? 30.470  24.417  88.374  1.00 13.47 ? 509  HIS C O   1 
ATOM   13297 C  CB  . HIS C 1 517 ? 33.033  23.842  90.362  1.00 12.22 ? 509  HIS C CB  1 
ATOM   13298 C  CG  . HIS C 1 517 ? 32.436  25.088  90.952  1.00 18.41 ? 509  HIS C CG  1 
ATOM   13299 N  ND1 . HIS C 1 517 ? 33.110  26.293  90.990  1.00 19.20 ? 509  HIS C ND1 1 
ATOM   13300 C  CD2 . HIS C 1 517 ? 31.247  25.303  91.568  1.00 19.37 ? 509  HIS C CD2 1 
ATOM   13301 C  CE1 . HIS C 1 517 ? 32.356  27.198  91.590  1.00 19.32 ? 509  HIS C CE1 1 
ATOM   13302 N  NE2 . HIS C 1 517 ? 31.224  26.623  91.956  1.00 20.29 ? 509  HIS C NE2 1 
ATOM   13303 N  N   . PRO C 1 518 ? 30.620  22.253  88.938  1.00 11.94 ? 510  PRO C N   1 
ATOM   13304 C  CA  . PRO C 1 518 ? 29.178  22.036  88.854  1.00 11.03 ? 510  PRO C CA  1 
ATOM   13305 C  C   . PRO C 1 518 ? 28.491  22.367  90.174  1.00 12.05 ? 510  PRO C C   1 
ATOM   13306 O  O   . PRO C 1 518 ? 29.131  22.629  91.191  1.00 12.49 ? 510  PRO C O   1 
ATOM   13307 C  CB  . PRO C 1 518 ? 29.081  20.536  88.551  1.00 8.09  ? 510  PRO C CB  1 
ATOM   13308 C  CG  . PRO C 1 518 ? 30.268  19.964  89.315  1.00 9.54  ? 510  PRO C CG  1 
ATOM   13309 C  CD  . PRO C 1 518 ? 31.364  20.991  89.124  1.00 11.41 ? 510  PRO C CD  1 
ATOM   13310 N  N   . SER C 1 519 ? 27.163  22.318  90.135  1.00 9.02  ? 511  SER C N   1 
ATOM   13311 C  CA  . SER C 1 519 ? 26.347  22.574  91.309  1.00 10.10 ? 511  SER C CA  1 
ATOM   13312 C  C   . SER C 1 519 ? 25.221  21.554  91.379  1.00 12.00 ? 511  SER C C   1 
ATOM   13313 O  O   . SER C 1 519 ? 24.689  21.116  90.349  1.00 10.83 ? 511  SER C O   1 
ATOM   13314 C  CB  . SER C 1 519 ? 25.749  23.993  91.296  1.00 13.73 ? 511  SER C CB  1 
ATOM   13315 O  OG  . SER C 1 519 ? 26.764  24.991  91.235  1.00 13.51 ? 511  SER C OG  1 
ATOM   13316 N  N   . CYS C 1 520 ? 24.869  21.186  92.614  1.00 8.40  ? 512  CYS C N   1 
ATOM   13317 C  CA  . CYS C 1 520 ? 23.650  20.443  92.932  1.00 11.12 ? 512  CYS C CA  1 
ATOM   13318 C  C   . CYS C 1 520 ? 22.685  21.405  93.611  1.00 14.01 ? 512  CYS C C   1 
ATOM   13319 O  O   . CYS C 1 520 ? 23.019  21.983  94.649  1.00 14.82 ? 512  CYS C O   1 
ATOM   13320 C  CB  . CYS C 1 520 ? 23.940  19.254  93.856  1.00 7.87  ? 512  CYS C CB  1 
ATOM   13321 S  SG  . CYS C 1 520 ? 24.940  17.946  93.125  1.00 15.24 ? 512  CYS C SG  1 
ATOM   13322 N  N   . LEU C 1 521 ? 21.511  21.587  93.021  1.00 8.80  ? 513  LEU C N   1 
ATOM   13323 C  CA  . LEU C 1 521 ? 20.461  22.449  93.549  1.00 9.40  ? 513  LEU C CA  1 
ATOM   13324 C  C   . LEU C 1 521 ? 19.332  21.562  94.047  1.00 12.78 ? 513  LEU C C   1 
ATOM   13325 O  O   . LEU C 1 521 ? 18.729  20.821  93.262  1.00 12.28 ? 513  LEU C O   1 
ATOM   13326 C  CB  . LEU C 1 521 ? 19.930  23.403  92.483  1.00 9.74  ? 513  LEU C CB  1 
ATOM   13327 C  CG  . LEU C 1 521 ? 20.952  24.233  91.730  1.00 14.38 ? 513  LEU C CG  1 
ATOM   13328 C  CD1 . LEU C 1 521 ? 20.216  25.182  90.800  1.00 12.99 ? 513  LEU C CD1 1 
ATOM   13329 C  CD2 . LEU C 1 521 ? 21.861  24.981  92.706  1.00 13.10 ? 513  LEU C CD2 1 
ATOM   13330 N  N   . ILE C 1 522 ? 19.048  21.642  95.342  1.00 9.72  ? 514  ILE C N   1 
ATOM   13331 C  CA  . ILE C 1 522 ? 18.207  20.672  96.033  1.00 11.40 ? 514  ILE C CA  1 
ATOM   13332 C  C   . ILE C 1 522 ? 16.967  21.392  96.549  1.00 17.55 ? 514  ILE C C   1 
ATOM   13333 O  O   . ILE C 1 522 ? 17.087  22.337  97.340  1.00 14.10 ? 514  ILE C O   1 
ATOM   13334 C  CB  . ILE C 1 522 ? 18.969  20.008  97.190  1.00 12.92 ? 514  ILE C CB  1 
ATOM   13335 C  CG1 . ILE C 1 522 ? 20.156  19.191  96.650  1.00 13.28 ? 514  ILE C CG1 1 
ATOM   13336 C  CG2 . ILE C 1 522 ? 18.042  19.117  98.010  1.00 10.56 ? 514  ILE C CG2 1 
ATOM   13337 C  CD1 . ILE C 1 522 ? 21.096  18.685  97.761  1.00 11.12 ? 514  ILE C CD1 1 
ATOM   13338 N  N   . PHE C 1 523 ? 15.779  20.917  96.144  1.00 10.61 ? 515  PHE C N   1 
ATOM   13339 C  CA  . PHE C 1 523 ? 14.528  21.630  96.380  1.00 11.38 ? 515  PHE C CA  1 
ATOM   13340 C  C   . PHE C 1 523 ? 13.481  20.753  97.054  1.00 16.83 ? 515  PHE C C   1 
ATOM   13341 O  O   . PHE C 1 523 ? 13.384  19.550  96.785  1.00 17.11 ? 515  PHE C O   1 
ATOM   13342 C  CB  . PHE C 1 523 ? 13.937  22.162  95.065  1.00 12.30 ? 515  PHE C CB  1 
ATOM   13343 C  CG  . PHE C 1 523 ? 14.804  23.173  94.381  1.00 16.63 ? 515  PHE C CG  1 
ATOM   13344 C  CD1 . PHE C 1 523 ? 14.755  24.509  94.752  1.00 19.35 ? 515  PHE C CD1 1 
ATOM   13345 C  CD2 . PHE C 1 523 ? 15.681  22.789  93.379  1.00 12.47 ? 515  PHE C CD2 1 
ATOM   13346 C  CE1 . PHE C 1 523 ? 15.553  25.446  94.120  1.00 16.78 ? 515  PHE C CE1 1 
ATOM   13347 C  CE2 . PHE C 1 523 ? 16.484  23.727  92.746  1.00 13.92 ? 515  PHE C CE2 1 
ATOM   13348 C  CZ  . PHE C 1 523 ? 16.421  25.053  93.125  1.00 14.66 ? 515  PHE C CZ  1 
ATOM   13349 N  N   . SER C 1 524 ? 12.697  21.365  97.935  1.00 18.09 ? 516  SER C N   1 
ATOM   13350 C  CA  . SER C 1 524 ? 11.454  20.767  98.395  1.00 22.43 ? 516  SER C CA  1 
ATOM   13351 C  C   . SER C 1 524 ? 10.287  21.444  97.685  1.00 32.64 ? 516  SER C C   1 
ATOM   13352 O  O   . SER C 1 524 ? 10.459  22.400  96.925  1.00 33.54 ? 516  SER C O   1 
ATOM   13353 C  CB  . SER C 1 524 ? 11.311  20.901  99.909  1.00 26.08 ? 516  SER C CB  1 
ATOM   13354 O  OG  . SER C 1 524 ? 11.444  22.264  100.283 1.00 29.46 ? 516  SER C OG  1 
ATOM   13355 N  N   . ARG C 1 525 ? 9.081   20.960  97.965  1.00 38.00 ? 517  ARG C N   1 
ATOM   13356 C  CA  . ARG C 1 525 ? 7.859   21.572  97.452  1.00 43.51 ? 517  ARG C CA  1 
ATOM   13357 C  C   . ARG C 1 525 ? 7.632   22.962  98.056  1.00 50.54 ? 517  ARG C C   1 
ATOM   13358 O  O   . ARG C 1 525 ? 7.977   23.219  99.213  1.00 50.34 ? 517  ARG C O   1 
ATOM   13359 C  CB  . ARG C 1 525 ? 6.654   20.670  97.736  1.00 40.16 ? 517  ARG C CB  1 
ATOM   13360 N  N   . GLN C 1 531 ? 10.543  34.621  104.657 1.00 52.45 ? 523  GLN C N   1 
ATOM   13361 C  CA  . GLN C 1 531 ? 11.640  35.148  105.463 1.00 54.78 ? 523  GLN C CA  1 
ATOM   13362 C  C   . GLN C 1 531 ? 12.012  36.566  105.042 1.00 49.10 ? 523  GLN C C   1 
ATOM   13363 O  O   . GLN C 1 531 ? 12.505  36.780  103.934 1.00 49.52 ? 523  GLN C O   1 
ATOM   13364 C  CB  . GLN C 1 531 ? 12.874  34.244  105.357 1.00 58.29 ? 523  GLN C CB  1 
ATOM   13365 C  CG  . GLN C 1 531 ? 12.630  32.781  105.710 1.00 61.13 ? 523  GLN C CG  1 
ATOM   13366 C  CD  . GLN C 1 531 ? 12.137  32.587  107.134 1.00 60.85 ? 523  GLN C CD  1 
ATOM   13367 O  OE1 . GLN C 1 531 ? 12.337  33.440  108.000 1.00 59.33 ? 523  GLN C OE1 1 
ATOM   13368 N  NE2 . GLN C 1 531 ? 11.486  31.457  107.380 1.00 62.19 ? 523  GLN C NE2 1 
ATOM   13369 N  N   . ALA C 1 532 ? 11.782  37.529  105.929 1.00 42.53 ? 524  ALA C N   1 
ATOM   13370 C  CA  . ALA C 1 532 ? 12.173  38.903  105.648 1.00 40.86 ? 524  ALA C CA  1 
ATOM   13371 C  C   . ALA C 1 532 ? 13.692  39.034  105.665 1.00 34.00 ? 524  ALA C C   1 
ATOM   13372 O  O   . ALA C 1 532 ? 14.379  38.393  106.466 1.00 34.07 ? 524  ALA C O   1 
ATOM   13373 C  CB  . ALA C 1 532 ? 11.549  39.856  106.664 1.00 40.36 ? 524  ALA C CB  1 
ATOM   13374 N  N   . ARG C 1 533 ? 14.219  39.866  104.768 1.00 30.06 ? 525  ARG C N   1 
ATOM   13375 C  CA  . ARG C 1 533 ? 15.655  40.056  104.656 1.00 27.95 ? 525  ARG C CA  1 
ATOM   13376 C  C   . ARG C 1 533 ? 15.972  41.513  104.359 1.00 29.15 ? 525  ARG C C   1 
ATOM   13377 O  O   . ARG C 1 533 ? 15.285  42.162  103.566 1.00 35.85 ? 525  ARG C O   1 
ATOM   13378 C  CB  . ARG C 1 533 ? 16.265  39.169  103.558 1.00 26.57 ? 525  ARG C CB  1 
ATOM   13379 C  CG  . ARG C 1 533 ? 16.448  37.710  103.944 1.00 22.91 ? 525  ARG C CG  1 
ATOM   13380 C  CD  . ARG C 1 533 ? 17.119  36.948  102.792 1.00 28.00 ? 525  ARG C CD  1 
ATOM   13381 N  NE  . ARG C 1 533 ? 17.051  35.494  102.960 1.00 24.91 ? 525  ARG C NE  1 
ATOM   13382 C  CZ  . ARG C 1 533 ? 16.007  34.754  102.606 1.00 23.64 ? 525  ARG C CZ  1 
ATOM   13383 N  NH1 . ARG C 1 533 ? 14.939  35.325  102.074 1.00 26.02 ? 525  ARG C NH1 1 
ATOM   13384 N  NH2 . ARG C 1 533 ? 16.025  33.442  102.791 1.00 25.24 ? 525  ARG C NH2 1 
ATOM   13385 N  N   . SER C 1 534 ? 17.013  42.016  105.012 1.00 25.27 ? 526  SER C N   1 
ATOM   13386 C  CA  . SER C 1 534 ? 17.612  43.282  104.635 1.00 28.40 ? 526  SER C CA  1 
ATOM   13387 C  C   . SER C 1 534 ? 18.364  43.133  103.314 1.00 30.35 ? 526  SER C C   1 
ATOM   13388 O  O   . SER C 1 534 ? 18.575  42.030  102.800 1.00 27.01 ? 526  SER C O   1 
ATOM   13389 C  CB  . SER C 1 534 ? 18.571  43.765  105.719 1.00 29.37 ? 526  SER C CB  1 
ATOM   13390 O  OG  . SER C 1 534 ? 19.636  42.843  105.892 1.00 30.92 ? 526  SER C OG  1 
ATOM   13391 N  N   . GLU C 1 535 ? 18.779  44.273  102.767 1.00 32.73 ? 527  GLU C N   1 
ATOM   13392 C  CA  . GLU C 1 535 ? 19.648  44.253  101.596 1.00 33.78 ? 527  GLU C CA  1 
ATOM   13393 C  C   . GLU C 1 535 ? 20.947  43.505  101.883 1.00 24.98 ? 527  GLU C C   1 
ATOM   13394 O  O   . GLU C 1 535 ? 21.398  42.697  101.064 1.00 26.91 ? 527  GLU C O   1 
ATOM   13395 C  CB  . GLU C 1 535 ? 19.931  45.684  101.152 1.00 34.71 ? 527  GLU C CB  1 
ATOM   13396 C  CG  . GLU C 1 535 ? 21.094  45.843  100.206 1.00 38.42 ? 527  GLU C CG  1 
ATOM   13397 C  CD  . GLU C 1 535 ? 21.486  47.294  100.072 1.00 39.92 ? 527  GLU C CD  1 
ATOM   13398 O  OE1 . GLU C 1 535 ? 21.447  48.012  101.103 1.00 37.38 ? 527  GLU C OE1 1 
ATOM   13399 O  OE2 . GLU C 1 535 ? 21.804  47.713  98.938  1.00 37.50 ? 527  GLU C OE2 1 
ATOM   13400 N  N   . GLN C 1 536 ? 21.557  43.754  103.045 1.00 30.03 ? 528  GLN C N   1 
ATOM   13401 C  CA  . GLN C 1 536 ? 22.781  43.042  103.401 1.00 30.41 ? 528  GLN C CA  1 
ATOM   13402 C  C   . GLN C 1 536 ? 22.555  41.537  103.443 1.00 27.78 ? 528  GLN C C   1 
ATOM   13403 O  O   . GLN C 1 536 ? 23.381  40.762  102.950 1.00 26.30 ? 528  GLN C O   1 
ATOM   13404 C  CB  . GLN C 1 536 ? 23.307  43.534  104.746 1.00 34.14 ? 528  GLN C CB  1 
ATOM   13405 C  CG  . GLN C 1 536 ? 24.647  42.923  105.134 1.00 40.61 ? 528  GLN C CG  1 
ATOM   13406 C  CD  . GLN C 1 536 ? 25.732  43.193  104.109 1.00 45.70 ? 528  GLN C CD  1 
ATOM   13407 O  OE1 . GLN C 1 536 ? 26.375  44.242  104.136 1.00 51.41 ? 528  GLN C OE1 1 
ATOM   13408 N  NE2 . GLN C 1 536 ? 25.941  42.246  103.196 1.00 46.72 ? 528  GLN C NE2 1 
ATOM   13409 N  N   . GLN C 1 537 ? 21.444  41.101  104.034 1.00 23.93 ? 529  GLN C N   1 
ATOM   13410 C  CA  . GLN C 1 537 ? 21.181  39.669  104.130 1.00 22.35 ? 529  GLN C CA  1 
ATOM   13411 C  C   . GLN C 1 537 ? 20.971  39.049  102.751 1.00 21.46 ? 529  GLN C C   1 
ATOM   13412 O  O   . GLN C 1 537 ? 21.536  37.993  102.448 1.00 20.58 ? 529  GLN C O   1 
ATOM   13413 C  CB  . GLN C 1 537 ? 19.975  39.421  105.034 1.00 22.46 ? 529  GLN C CB  1 
ATOM   13414 C  CG  . GLN C 1 537 ? 20.285  39.604  106.497 1.00 29.83 ? 529  GLN C CG  1 
ATOM   13415 C  CD  . GLN C 1 537 ? 19.037  39.659  107.337 1.00 34.63 ? 529  GLN C CD  1 
ATOM   13416 O  OE1 . GLN C 1 537 ? 18.017  40.199  106.910 1.00 33.03 ? 529  GLN C OE1 1 
ATOM   13417 N  NE2 . GLN C 1 537 ? 19.101  39.087  108.535 1.00 37.36 ? 529  GLN C NE2 1 
ATOM   13418 N  N   . LEU C 1 538 ? 20.160  39.692  101.901 1.00 22.93 ? 530  LEU C N   1 
ATOM   13419 C  CA  . LEU C 1 538 ? 20.006  39.226  100.524 1.00 22.98 ? 530  LEU C CA  1 
ATOM   13420 C  C   . LEU C 1 538 ? 21.354  39.096  99.833  1.00 20.83 ? 530  LEU C C   1 
ATOM   13421 O  O   . LEU C 1 538 ? 21.623  38.096  99.167  1.00 19.91 ? 530  LEU C O   1 
ATOM   13422 C  CB  . LEU C 1 538 ? 19.109  40.178  99.727  1.00 25.64 ? 530  LEU C CB  1 
ATOM   13423 C  CG  . LEU C 1 538 ? 17.597  40.095  99.933  1.00 32.44 ? 530  LEU C CG  1 
ATOM   13424 C  CD1 . LEU C 1 538 ? 16.923  41.293  99.284  1.00 31.40 ? 530  LEU C CD1 1 
ATOM   13425 C  CD2 . LEU C 1 538 ? 17.024  38.786  99.367  1.00 25.36 ? 530  LEU C CD2 1 
ATOM   13426 N  N   . ASN C 1 539 ? 22.221  40.093  100.003 1.00 22.35 ? 531  ASN C N   1 
ATOM   13427 C  CA  . ASN C 1 539 ? 23.515  40.109  99.330  1.00 23.57 ? 531  ASN C CA  1 
ATOM   13428 C  C   . ASN C 1 539 ? 24.467  39.042  99.845  1.00 21.07 ? 531  ASN C C   1 
ATOM   13429 O  O   . ASN C 1 539 ? 25.436  38.709  99.151  1.00 21.53 ? 531  ASN C O   1 
ATOM   13430 C  CB  . ASN C 1 539 ? 24.186  41.472  99.500  1.00 25.14 ? 531  ASN C CB  1 
ATOM   13431 C  CG  . ASN C 1 539 ? 23.588  42.532  98.611  1.00 28.29 ? 531  ASN C CG  1 
ATOM   13432 O  OD1 . ASN C 1 539 ? 22.944  42.227  97.606  1.00 33.30 ? 531  ASN C OD1 1 
ATOM   13433 N  ND2 . ASN C 1 539 ? 23.817  43.790  98.965  1.00 28.31 ? 531  ASN C ND2 1 
ATOM   13434 N  N   . ASP C 1 540 ? 24.244  38.535  101.048 1.00 20.87 ? 532  ASP C N   1 
ATOM   13435 C  CA  . ASP C 1 540 ? 25.129  37.538  101.632 1.00 25.74 ? 532  ASP C CA  1 
ATOM   13436 C  C   . ASP C 1 540 ? 24.683  36.105  101.378 1.00 20.70 ? 532  ASP C C   1 
ATOM   13437 O  O   . ASP C 1 540 ? 25.417  35.179  101.739 1.00 19.32 ? 532  ASP C O   1 
ATOM   13438 C  CB  . ASP C 1 540 ? 25.273  37.766  103.139 1.00 20.98 ? 532  ASP C CB  1 
ATOM   13439 C  CG  . ASP C 1 540 ? 26.186  38.924  103.460 1.00 25.96 ? 532  ASP C CG  1 
ATOM   13440 O  OD1 . ASP C 1 540 ? 26.991  39.290  102.581 1.00 23.97 ? 532  ASP C OD1 1 
ATOM   13441 O  OD2 . ASP C 1 540 ? 26.097  39.471  104.587 1.00 29.19 ? 532  ASP C OD2 1 
ATOM   13442 N  N   . ILE C 1 541 ? 23.516  35.892  100.763 1.00 18.72 ? 533  ILE C N   1 
ATOM   13443 C  CA  . ILE C 1 541 ? 23.123  34.533  100.398 1.00 17.83 ? 533  ILE C CA  1 
ATOM   13444 C  C   . ILE C 1 541 ? 24.206  33.876  99.555  1.00 17.38 ? 533  ILE C C   1 
ATOM   13445 O  O   . ILE C 1 541 ? 24.551  32.704  99.763  1.00 17.13 ? 533  ILE C O   1 
ATOM   13446 C  CB  . ILE C 1 541 ? 21.769  34.534  99.665  1.00 17.37 ? 533  ILE C CB  1 
ATOM   13447 C  CG1 . ILE C 1 541 ? 20.652  35.029  100.581 1.00 17.95 ? 533  ILE C CG1 1 
ATOM   13448 C  CG2 . ILE C 1 541 ? 21.440  33.132  99.156  1.00 19.30 ? 533  ILE C CG2 1 
ATOM   13449 C  CD1 . ILE C 1 541 ? 19.348  35.362  99.839  1.00 18.08 ? 533  ILE C CD1 1 
ATOM   13450 N  N   . LYS C 1 542 ? 24.785  34.624  98.609  1.00 17.41 ? 534  LYS C N   1 
ATOM   13451 C  CA  . LYS C 1 542 ? 25.799  34.033  97.741  1.00 16.96 ? 534  LYS C CA  1 
ATOM   13452 C  C   . LYS C 1 542 ? 27.091  33.697  98.476  1.00 17.92 ? 534  LYS C C   1 
ATOM   13453 O  O   . LYS C 1 542 ? 27.990  33.114  97.868  1.00 16.89 ? 534  LYS C O   1 
ATOM   13454 C  CB  . LYS C 1 542 ? 26.102  34.964  96.568  1.00 17.54 ? 534  LYS C CB  1 
ATOM   13455 C  CG  . LYS C 1 542 ? 26.715  36.297  96.969  1.00 18.77 ? 534  LYS C CG  1 
ATOM   13456 C  CD  . LYS C 1 542 ? 27.070  37.112  95.722  1.00 19.41 ? 534  LYS C CD  1 
ATOM   13457 C  CE  . LYS C 1 542 ? 27.218  38.562  96.060  1.00 31.44 ? 534  LYS C CE  1 
ATOM   13458 N  NZ  . LYS C 1 542 ? 25.900  39.186  96.389  1.00 32.40 ? 534  LYS C NZ  1 
ATOM   13459 N  N   . ARG C 1 543 ? 27.214  34.059  99.750  1.00 19.51 ? 535  ARG C N   1 
ATOM   13460 C  CA  . ARG C 1 543 ? 28.344  33.639  100.561 1.00 17.85 ? 535  ARG C CA  1 
ATOM   13461 C  C   . ARG C 1 543 ? 28.099  32.316  101.273 1.00 17.07 ? 535  ARG C C   1 
ATOM   13462 O  O   . ARG C 1 543 ? 28.946  31.890  102.063 1.00 17.26 ? 535  ARG C O   1 
ATOM   13463 C  CB  . ARG C 1 543 ? 28.694  34.740  101.578 1.00 19.03 ? 535  ARG C CB  1 
ATOM   13464 C  CG  . ARG C 1 543 ? 28.961  36.085  100.912 1.00 22.03 ? 535  ARG C CG  1 
ATOM   13465 C  CD  . ARG C 1 543 ? 29.719  37.064  101.809 1.00 25.67 ? 535  ARG C CD  1 
ATOM   13466 N  NE  . ARG C 1 543 ? 31.119  36.681  101.995 1.00 25.17 ? 535  ARG C NE  1 
ATOM   13467 C  CZ  . ARG C 1 543 ? 32.045  37.480  102.512 1.00 25.45 ? 535  ARG C CZ  1 
ATOM   13468 N  NH1 . ARG C 1 543 ? 31.726  38.716  102.879 1.00 25.54 ? 535  ARG C NH1 1 
ATOM   13469 N  NH2 . ARG C 1 543 ? 33.295  37.053  102.650 1.00 25.77 ? 535  ARG C NH2 1 
ATOM   13470 N  N   . GLY C 1 544 ? 26.972  31.649  101.010 1.00 16.31 ? 536  GLY C N   1 
ATOM   13471 C  CA  . GLY C 1 544 ? 26.747  30.281  101.439 1.00 15.56 ? 536  GLY C CA  1 
ATOM   13472 C  C   . GLY C 1 544 ? 26.140  30.130  102.818 1.00 18.32 ? 536  GLY C C   1 
ATOM   13473 O  O   . GLY C 1 544 ? 25.390  29.182  103.053 1.00 15.97 ? 536  GLY C O   1 
ATOM   13474 N  N   . ALA C 1 545 ? 26.464  31.028  103.741 1.00 16.80 ? 537  ALA C N   1 
ATOM   13475 C  CA  . ALA C 1 545 ? 25.791  31.081  105.028 1.00 17.27 ? 537  ALA C CA  1 
ATOM   13476 C  C   . ALA C 1 545 ? 25.817  32.520  105.504 1.00 21.47 ? 537  ALA C C   1 
ATOM   13477 O  O   . ALA C 1 545 ? 26.751  33.269  105.208 1.00 19.36 ? 537  ALA C O   1 
ATOM   13478 C  CB  . ALA C 1 545 ? 26.433  30.163  106.075 1.00 17.72 ? 537  ALA C CB  1 
ATOM   13479 N  N   . TYR C 1 546 ? 24.774  32.898  106.231 1.00 19.34 ? 538  TYR C N   1 
ATOM   13480 C  CA  . TYR C 1 546 ? 24.620  34.267  106.693 1.00 22.50 ? 538  TYR C CA  1 
ATOM   13481 C  C   . TYR C 1 546 ? 23.612  34.265  107.829 1.00 23.63 ? 538  TYR C C   1 
ATOM   13482 O  O   . TYR C 1 546 ? 22.816  33.334  107.969 1.00 19.70 ? 538  TYR C O   1 
ATOM   13483 C  CB  . TYR C 1 546 ? 24.154  35.187  105.563 1.00 20.49 ? 538  TYR C CB  1 
ATOM   13484 C  CG  . TYR C 1 546 ? 22.778  34.818  105.064 1.00 19.29 ? 538  TYR C CG  1 
ATOM   13485 C  CD1 . TYR C 1 546 ? 22.599  33.762  104.173 1.00 22.94 ? 538  TYR C CD1 1 
ATOM   13486 C  CD2 . TYR C 1 546 ? 21.650  35.519  105.498 1.00 19.89 ? 538  TYR C CD2 1 
ATOM   13487 C  CE1 . TYR C 1 546 ? 21.329  33.409  103.721 1.00 21.50 ? 538  TYR C CE1 1 
ATOM   13488 C  CE2 . TYR C 1 546 ? 20.383  35.175  105.055 1.00 20.32 ? 538  TYR C CE2 1 
ATOM   13489 C  CZ  . TYR C 1 546 ? 20.232  34.130  104.166 1.00 21.07 ? 538  TYR C CZ  1 
ATOM   13490 O  OH  . TYR C 1 546 ? 18.979  33.802  103.727 1.00 21.29 ? 538  TYR C OH  1 
ATOM   13491 N  N   . VAL C 1 547 ? 23.650  35.323  108.636 1.00 21.28 ? 539  VAL C N   1 
ATOM   13492 C  CA  . VAL C 1 547 ? 22.703  35.471  109.735 1.00 22.83 ? 539  VAL C CA  1 
ATOM   13493 C  C   . VAL C 1 547 ? 21.360  35.884  109.138 1.00 23.87 ? 539  VAL C C   1 
ATOM   13494 O  O   . VAL C 1 547 ? 21.201  37.006  108.648 1.00 25.97 ? 539  VAL C O   1 
ATOM   13495 C  CB  . VAL C 1 547 ? 23.193  36.490  110.773 1.00 27.96 ? 539  VAL C CB  1 
ATOM   13496 C  CG1 . VAL C 1 547 ? 22.215  36.567  111.933 1.00 25.19 ? 539  VAL C CG1 1 
ATOM   13497 C  CG2 . VAL C 1 547 ? 24.562  36.105  111.274 1.00 25.46 ? 539  VAL C CG2 1 
ATOM   13498 N  N   . ILE C 1 548 ? 20.394  34.968  109.155 1.00 24.75 ? 540  ILE C N   1 
ATOM   13499 C  CA  . ILE C 1 548 ? 19.066  35.286  108.644 1.00 23.70 ? 540  ILE C CA  1 
ATOM   13500 C  C   . ILE C 1 548 ? 18.167  35.906  109.709 1.00 25.85 ? 540  ILE C C   1 
ATOM   13501 O  O   . ILE C 1 548 ? 17.206  36.607  109.364 1.00 22.70 ? 540  ILE C O   1 
ATOM   13502 C  CB  . ILE C 1 548 ? 18.400  34.030  108.051 1.00 23.12 ? 540  ILE C CB  1 
ATOM   13503 C  CG1 . ILE C 1 548 ? 17.177  34.407  107.210 1.00 27.60 ? 540  ILE C CG1 1 
ATOM   13504 C  CG2 . ILE C 1 548 ? 18.002  33.065  109.150 1.00 21.13 ? 540  ILE C CG2 1 
ATOM   13505 C  CD1 . ILE C 1 548 ? 16.579  33.227  106.453 1.00 29.23 ? 540  ILE C CD1 1 
ATOM   13506 N  N   . SER C 1 549 ? 18.456  35.685  110.993 1.00 22.87 ? 541  SER C N   1 
ATOM   13507 C  CA  . SER C 1 549 ? 17.677  36.312  112.059 1.00 30.24 ? 541  SER C CA  1 
ATOM   13508 C  C   . SER C 1 549 ? 18.590  36.488  113.271 1.00 27.06 ? 541  SER C C   1 
ATOM   13509 O  O   . SER C 1 549 ? 18.887  35.518  113.974 1.00 26.33 ? 541  SER C O   1 
ATOM   13510 C  CB  . SER C 1 549 ? 16.449  35.480  112.399 1.00 28.54 ? 541  SER C CB  1 
ATOM   13511 O  OG  . SER C 1 549 ? 15.702  36.124  113.407 1.00 26.64 ? 541  SER C OG  1 
ATOM   13512 N  N   . GLU C 1 550 ? 19.032  37.718  113.503 1.00 25.50 ? 542  GLU C N   1 
ATOM   13513 C  CA  . GLU C 1 550 ? 19.933  37.980  114.617 1.00 32.10 ? 542  GLU C CA  1 
ATOM   13514 C  C   . GLU C 1 550 ? 19.200  37.837  115.948 1.00 30.62 ? 542  GLU C C   1 
ATOM   13515 O  O   . GLU C 1 550 ? 17.983  38.025  116.041 1.00 30.30 ? 542  GLU C O   1 
ATOM   13516 C  CB  . GLU C 1 550 ? 20.545  39.381  114.498 1.00 40.46 ? 542  GLU C CB  1 
ATOM   13517 C  CG  . GLU C 1 550 ? 21.578  39.725  115.582 1.00 48.20 ? 542  GLU C CG  1 
ATOM   13518 C  CD  . GLU C 1 550 ? 22.790  38.798  115.581 1.00 53.71 ? 542  GLU C CD  1 
ATOM   13519 O  OE1 . GLU C 1 550 ? 23.595  38.895  114.632 1.00 55.88 ? 542  GLU C OE1 1 
ATOM   13520 O  OE2 . GLU C 1 550 ? 22.940  37.979  116.525 1.00 27.69 ? 542  GLU C OE2 1 
ATOM   13521 N  N   . ALA C 1 551 ? 19.957  37.485  116.983 1.00 30.76 ? 543  ALA C N   1 
ATOM   13522 C  CA  . ALA C 1 551 ? 19.404  37.436  118.328 1.00 30.89 ? 543  ALA C CA  1 
ATOM   13523 C  C   . ALA C 1 551 ? 18.981  38.828  118.783 1.00 32.44 ? 543  ALA C C   1 
ATOM   13524 O  O   . ALA C 1 551 ? 19.542  39.840  118.360 1.00 32.76 ? 543  ALA C O   1 
ATOM   13525 C  CB  . ALA C 1 551 ? 20.430  36.863  119.305 1.00 29.16 ? 543  ALA C CB  1 
ATOM   13526 N  N   . GLN C 1 552 ? 17.962  38.869  119.640 1.00 34.32 ? 544  GLN C N   1 
ATOM   13527 C  CA  . GLN C 1 552 ? 17.575  40.080  120.354 1.00 38.60 ? 544  GLN C CA  1 
ATOM   13528 C  C   . GLN C 1 552 ? 18.398  40.128  121.634 1.00 39.75 ? 544  GLN C C   1 
ATOM   13529 O  O   . GLN C 1 552 ? 18.146  39.365  122.570 1.00 37.92 ? 544  GLN C O   1 
ATOM   13530 C  CB  . GLN C 1 552 ? 16.078  40.085  120.650 1.00 37.85 ? 544  GLN C CB  1 
ATOM   13531 N  N   . GLY C 1 553 ? 19.393  41.008  121.668 1.00 37.90 ? 545  GLY C N   1 
ATOM   13532 C  CA  . GLY C 1 553 ? 20.398  40.950  122.706 1.00 37.78 ? 545  GLY C CA  1 
ATOM   13533 C  C   . GLY C 1 553 ? 21.509  39.998  122.316 1.00 39.59 ? 545  GLY C C   1 
ATOM   13534 O  O   . GLY C 1 553 ? 21.540  39.438  121.218 1.00 38.63 ? 545  GLY C O   1 
ATOM   13535 N  N   . ASN C 1 554 ? 22.438  39.797  123.247 1.00 38.10 ? 546  ASN C N   1 
ATOM   13536 C  CA  . ASN C 1 554 ? 23.609  38.977  122.964 1.00 36.08 ? 546  ASN C CA  1 
ATOM   13537 C  C   . ASN C 1 554 ? 23.216  37.512  122.814 1.00 36.16 ? 546  ASN C C   1 
ATOM   13538 O  O   . ASN C 1 554 ? 22.524  36.945  123.667 1.00 33.08 ? 546  ASN C O   1 
ATOM   13539 C  CB  . ASN C 1 554 ? 24.649  39.134  124.073 1.00 38.05 ? 546  ASN C CB  1 
ATOM   13540 N  N   . ALA C 1 555 ? 23.668  36.895  121.730 1.00 39.86 ? 547  ALA C N   1 
ATOM   13541 C  CA  . ALA C 1 555 ? 23.306  35.512  121.464 1.00 38.59 ? 547  ALA C CA  1 
ATOM   13542 C  C   . ALA C 1 555 ? 23.968  34.582  122.473 1.00 36.15 ? 547  ALA C C   1 
ATOM   13543 O  O   . ALA C 1 555 ? 25.142  34.742  122.817 1.00 31.47 ? 547  ALA C O   1 
ATOM   13544 C  CB  . ALA C 1 555 ? 23.708  35.122  120.038 1.00 28.97 ? 547  ALA C CB  1 
ATOM   13545 N  N   . GLN C 1 556 ? 23.195  33.611  122.959 1.00 32.02 ? 548  GLN C N   1 
ATOM   13546 C  CA  . GLN C 1 556 ? 23.714  32.531  123.787 1.00 37.32 ? 548  GLN C CA  1 
ATOM   13547 C  C   . GLN C 1 556 ? 24.010  31.263  122.996 1.00 36.74 ? 548  GLN C C   1 
ATOM   13548 O  O   . GLN C 1 556 ? 24.678  30.366  123.519 1.00 30.39 ? 548  GLN C O   1 
ATOM   13549 C  CB  . GLN C 1 556 ? 22.727  32.206  124.905 1.00 38.74 ? 548  GLN C CB  1 
ATOM   13550 C  CG  . GLN C 1 556 ? 22.329  33.421  125.722 1.00 46.94 ? 548  GLN C CG  1 
ATOM   13551 C  CD  . GLN C 1 556 ? 21.366  33.071  126.829 1.00 50.02 ? 548  GLN C CD  1 
ATOM   13552 O  OE1 . GLN C 1 556 ? 21.609  32.150  127.607 1.00 49.13 ? 548  GLN C OE1 1 
ATOM   13553 N  NE2 . GLN C 1 556 ? 20.259  33.794  126.898 1.00 60.60 ? 548  GLN C NE2 1 
ATOM   13554 N  N   . ALA C 1 557 ? 23.526  31.167  121.762 1.00 31.14 ? 549  ALA C N   1 
ATOM   13555 C  CA  . ALA C 1 557 ? 23.839  30.059  120.873 1.00 27.62 ? 549  ALA C CA  1 
ATOM   13556 C  C   . ALA C 1 557 ? 23.430  30.479  119.470 1.00 27.91 ? 549  ALA C C   1 
ATOM   13557 O  O   . ALA C 1 557 ? 22.778  31.507  119.277 1.00 26.67 ? 549  ALA C O   1 
ATOM   13558 C  CB  . ALA C 1 557 ? 23.126  28.765  121.281 1.00 27.58 ? 549  ALA C CB  1 
ATOM   13559 N  N   . VAL C 1 558 ? 23.807  29.661  118.492 1.00 25.31 ? 550  VAL C N   1 
ATOM   13560 C  CA  . VAL C 1 558 ? 23.437  29.893  117.102 1.00 24.19 ? 550  VAL C CA  1 
ATOM   13561 C  C   . VAL C 1 558 ? 22.786  28.624  116.565 1.00 23.28 ? 550  VAL C C   1 
ATOM   13562 O  O   . VAL C 1 558 ? 23.301  27.517  116.767 1.00 23.44 ? 550  VAL C O   1 
ATOM   13563 C  CB  . VAL C 1 558 ? 24.651  30.316  116.246 1.00 26.91 ? 550  VAL C CB  1 
ATOM   13564 C  CG1 . VAL C 1 558 ? 25.820  29.379  116.463 1.00 31.11 ? 550  VAL C CG1 1 
ATOM   13565 C  CG2 . VAL C 1 558 ? 24.286  30.368  114.769 1.00 22.58 ? 550  VAL C CG2 1 
ATOM   13566 N  N   . ILE C 1 559 ? 21.632  28.779  115.929 1.00 22.85 ? 551  ILE C N   1 
ATOM   13567 C  CA  . ILE C 1 559 ? 20.957  27.683  115.242 1.00 21.98 ? 551  ILE C CA  1 
ATOM   13568 C  C   . ILE C 1 559 ? 21.295  27.784  113.764 1.00 20.84 ? 551  ILE C C   1 
ATOM   13569 O  O   . ILE C 1 559 ? 20.966  28.787  113.119 1.00 20.76 ? 551  ILE C O   1 
ATOM   13570 C  CB  . ILE C 1 559 ? 19.435  27.733  115.441 1.00 22.34 ? 551  ILE C CB  1 
ATOM   13571 C  CG1 . ILE C 1 559 ? 19.068  27.715  116.921 1.00 23.63 ? 551  ILE C CG1 1 
ATOM   13572 C  CG2 . ILE C 1 559 ? 18.777  26.556  114.707 1.00 21.52 ? 551  ILE C CG2 1 
ATOM   13573 C  CD1 . ILE C 1 559 ? 17.597  27.874  117.136 1.00 24.15 ? 551  ILE C CD1 1 
ATOM   13574 N  N   . ILE C 1 560 ? 21.942  26.749  113.228 1.00 20.04 ? 552  ILE C N   1 
ATOM   13575 C  CA  . ILE C 1 560 ? 22.248  26.644  111.807 1.00 23.11 ? 552  ILE C CA  1 
ATOM   13576 C  C   . ILE C 1 560 ? 21.178  25.778  111.157 1.00 19.90 ? 552  ILE C C   1 
ATOM   13577 O  O   . ILE C 1 560 ? 20.942  24.649  111.595 1.00 20.08 ? 552  ILE C O   1 
ATOM   13578 C  CB  . ILE C 1 560 ? 23.643  26.034  111.580 1.00 18.56 ? 552  ILE C CB  1 
ATOM   13579 C  CG1 . ILE C 1 560 ? 24.719  26.826  112.331 1.00 19.40 ? 552  ILE C CG1 1 
ATOM   13580 C  CG2 . ILE C 1 560 ? 23.955  25.949  110.077 1.00 18.20 ? 552  ILE C CG2 1 
ATOM   13581 C  CD1 . ILE C 1 560 ? 26.071  26.197  112.272 1.00 19.24 ? 552  ILE C CD1 1 
ATOM   13582 N  N   . ALA C 1 561 ? 20.546  26.282  110.100 1.00 17.81 ? 553  ALA C N   1 
ATOM   13583 C  CA  . ALA C 1 561 ? 19.514  25.505  109.426 1.00 17.27 ? 553  ALA C CA  1 
ATOM   13584 C  C   . ALA C 1 561 ? 19.615  25.698  107.920 1.00 16.38 ? 553  ALA C C   1 
ATOM   13585 O  O   . ALA C 1 561 ? 20.158  26.688  107.434 1.00 19.06 ? 553  ALA C O   1 
ATOM   13586 C  CB  . ALA C 1 561 ? 18.113  25.886  109.921 1.00 17.98 ? 553  ALA C CB  1 
ATOM   13587 N  N   . THR C 1 562 ? 19.088  24.728  107.177 1.00 15.71 ? 554  THR C N   1 
ATOM   13588 C  CA  . THR C 1 562 ? 19.100  24.781  105.725 1.00 14.91 ? 554  THR C CA  1 
ATOM   13589 C  C   . THR C 1 562 ? 17.708  24.476  105.201 1.00 14.84 ? 554  THR C C   1 
ATOM   13590 O  O   . THR C 1 562 ? 16.898  23.839  105.874 1.00 15.22 ? 554  THR C O   1 
ATOM   13591 C  CB  . THR C 1 562 ? 20.072  23.765  105.105 1.00 19.44 ? 554  THR C CB  1 
ATOM   13592 O  OG1 . THR C 1 562 ? 19.524  22.450  105.258 1.00 15.08 ? 554  THR C OG1 1 
ATOM   13593 C  CG2 . THR C 1 562 ? 21.476  23.844  105.768 1.00 16.94 ? 554  THR C CG2 1 
ATOM   13594 N  N   . GLY C 1 563 ? 17.458  24.921  103.972 1.00 15.68 ? 555  GLY C N   1 
ATOM   13595 C  CA  . GLY C 1 563 ? 16.294  24.456  103.232 1.00 12.06 ? 555  GLY C CA  1 
ATOM   13596 C  C   . GLY C 1 563 ? 15.001  24.579  104.011 1.00 12.35 ? 555  GLY C C   1 
ATOM   13597 O  O   . GLY C 1 563 ? 14.721  25.596  104.655 1.00 13.04 ? 555  GLY C O   1 
ATOM   13598 N  N   . SER C 1 564 ? 14.201  23.513  103.963 1.00 15.45 ? 556  SER C N   1 
ATOM   13599 C  CA  . SER C 1 564 ? 12.879  23.517  104.578 1.00 17.29 ? 556  SER C CA  1 
ATOM   13600 C  C   . SER C 1 564 ? 12.922  23.627  106.098 1.00 21.04 ? 556  SER C C   1 
ATOM   13601 O  O   . SER C 1 564 ? 11.862  23.770  106.711 1.00 20.55 ? 556  SER C O   1 
ATOM   13602 C  CB  . SER C 1 564 ? 12.112  22.248  104.165 1.00 14.47 ? 556  SER C CB  1 
ATOM   13603 O  OG  . SER C 1 564 ? 12.882  21.076  104.408 1.00 18.97 ? 556  SER C OG  1 
ATOM   13604 N  N   . GLU C 1 565 ? 14.096  23.575  106.728 1.00 15.85 ? 557  GLU C N   1 
ATOM   13605 C  CA  . GLU C 1 565 ? 14.172  23.635  108.185 1.00 14.18 ? 557  GLU C CA  1 
ATOM   13606 C  C   . GLU C 1 565 ? 14.497  25.025  108.722 1.00 16.32 ? 557  GLU C C   1 
ATOM   13607 O  O   . GLU C 1 565 ? 14.494  25.210  109.947 1.00 15.64 ? 557  GLU C O   1 
ATOM   13608 C  CB  . GLU C 1 565 ? 15.209  22.637  108.712 1.00 20.66 ? 557  GLU C CB  1 
ATOM   13609 C  CG  . GLU C 1 565 ? 14.713  21.206  108.773 1.00 19.15 ? 557  GLU C CG  1 
ATOM   13610 C  CD  . GLU C 1 565 ? 14.377  20.656  107.404 1.00 12.86 ? 557  GLU C CD  1 
ATOM   13611 O  OE1 . GLU C 1 565 ? 15.313  20.342  106.646 1.00 13.37 ? 557  GLU C OE1 1 
ATOM   13612 O  OE2 . GLU C 1 565 ? 13.171  20.562  107.085 1.00 14.78 ? 557  GLU C OE2 1 
ATOM   13613 N  N   . VAL C 1 566 ? 14.787  26.002  107.850 1.00 16.14 ? 558  VAL C N   1 
ATOM   13614 C  CA  . VAL C 1 566 ? 15.061  27.360  108.332 1.00 16.85 ? 558  VAL C CA  1 
ATOM   13615 C  C   . VAL C 1 566 ? 13.848  27.924  109.078 1.00 16.35 ? 558  VAL C C   1 
ATOM   13616 O  O   . VAL C 1 566 ? 13.989  28.540  110.142 1.00 17.19 ? 558  VAL C O   1 
ATOM   13617 C  CB  . VAL C 1 566 ? 15.505  28.272  107.168 1.00 16.18 ? 558  VAL C CB  1 
ATOM   13618 C  CG1 . VAL C 1 566 ? 15.645  29.717  107.643 1.00 18.77 ? 558  VAL C CG1 1 
ATOM   13619 C  CG2 . VAL C 1 566 ? 16.845  27.782  106.577 1.00 14.49 ? 558  VAL C CG2 1 
ATOM   13620 N  N   . GLY C 1 567 ? 12.640  27.697  108.551 1.00 19.12 ? 559  GLY C N   1 
ATOM   13621 C  CA  . GLY C 1 567 ? 11.448  28.227  109.208 1.00 19.72 ? 559  GLY C CA  1 
ATOM   13622 C  C   . GLY C 1 567 ? 11.235  27.649  110.595 1.00 21.93 ? 559  GLY C C   1 
ATOM   13623 O  O   . GLY C 1 567 ? 10.852  28.362  111.528 1.00 21.22 ? 559  GLY C O   1 
ATOM   13624 N  N   . LEU C 1 568 ? 11.484  26.350  110.744 1.00 19.63 ? 560  LEU C N   1 
ATOM   13625 C  CA  . LEU C 1 568 ? 11.474  25.716  112.056 1.00 20.35 ? 560  LEU C CA  1 
ATOM   13626 C  C   . LEU C 1 568 ? 12.458  26.395  113.002 1.00 21.14 ? 560  LEU C C   1 
ATOM   13627 O  O   . LEU C 1 568 ? 12.137  26.654  114.170 1.00 22.37 ? 560  LEU C O   1 
ATOM   13628 C  CB  . LEU C 1 568 ? 11.810  24.233  111.888 1.00 21.09 ? 560  LEU C CB  1 
ATOM   13629 C  CG  . LEU C 1 568 ? 11.860  23.305  113.089 1.00 22.50 ? 560  LEU C CG  1 
ATOM   13630 C  CD1 . LEU C 1 568 ? 10.523  23.337  113.799 1.00 27.54 ? 560  LEU C CD1 1 
ATOM   13631 C  CD2 . LEU C 1 568 ? 12.193  21.894  112.638 1.00 20.82 ? 560  LEU C CD2 1 
ATOM   13632 N  N   . ALA C 1 569 ? 13.660  26.705  112.504 1.00 21.29 ? 561  ALA C N   1 
ATOM   13633 C  CA  . ALA C 1 569 ? 14.683  27.335  113.336 1.00 18.55 ? 561  ALA C CA  1 
ATOM   13634 C  C   . ALA C 1 569 ? 14.253  28.724  113.799 1.00 21.37 ? 561  ALA C C   1 
ATOM   13635 O  O   . ALA C 1 569 ? 14.460  29.092  114.963 1.00 25.22 ? 561  ALA C O   1 
ATOM   13636 C  CB  . ALA C 1 569 ? 16.007  27.407  112.567 1.00 17.85 ? 561  ALA C CB  1 
ATOM   13637 N  N   . VAL C 1 570 ? 13.645  29.509  112.908 1.00 21.23 ? 562  VAL C N   1 
ATOM   13638 C  CA  . VAL C 1 570 ? 13.200  30.848  113.289 1.00 22.96 ? 562  VAL C CA  1 
ATOM   13639 C  C   . VAL C 1 570 ? 12.055  30.770  114.296 1.00 29.87 ? 562  VAL C C   1 
ATOM   13640 O  O   . VAL C 1 570 ? 11.994  31.558  115.252 1.00 30.09 ? 562  VAL C O   1 
ATOM   13641 C  CB  . VAL C 1 570 ? 12.819  31.655  112.035 1.00 24.89 ? 562  VAL C CB  1 
ATOM   13642 C  CG1 . VAL C 1 570 ? 12.169  32.977  112.414 1.00 26.92 ? 562  VAL C CG1 1 
ATOM   13643 C  CG2 . VAL C 1 570 ? 14.062  31.908  111.189 1.00 21.75 ? 562  VAL C CG2 1 
ATOM   13644 N  N   . GLU C 1 571 ? 11.134  29.820  114.110 1.00 23.29 ? 563  GLU C N   1 
ATOM   13645 C  CA  . GLU C 1 571 ? 10.055  29.653  115.081 1.00 24.00 ? 563  GLU C CA  1 
ATOM   13646 C  C   . GLU C 1 571 ? 10.607  29.266  116.448 1.00 26.25 ? 563  GLU C C   1 
ATOM   13647 O  O   . GLU C 1 571 ? 10.137  29.759  117.481 1.00 29.02 ? 563  GLU C O   1 
ATOM   13648 C  CB  . GLU C 1 571 ? 9.053   28.611  114.579 1.00 24.24 ? 563  GLU C CB  1 
ATOM   13649 N  N   . ALA C 1 572 ? 11.618  28.392  116.471 1.00 25.90 ? 564  ALA C N   1 
ATOM   13650 C  CA  . ALA C 1 572 ? 12.265  28.029  117.730 1.00 26.98 ? 564  ALA C CA  1 
ATOM   13651 C  C   . ALA C 1 572 ? 12.941  29.233  118.376 1.00 25.49 ? 564  ALA C C   1 
ATOM   13652 O  O   . ALA C 1 572 ? 12.876  29.405  119.600 1.00 30.18 ? 564  ALA C O   1 
ATOM   13653 C  CB  . ALA C 1 572 ? 13.272  26.901  117.493 1.00 25.88 ? 564  ALA C CB  1 
ATOM   13654 N  N   . GLN C 1 573 ? 13.601  30.077  117.570 1.00 23.10 ? 565  GLN C N   1 
ATOM   13655 C  CA  . GLN C 1 573 ? 14.218  31.294  118.097 1.00 23.97 ? 565  GLN C CA  1 
ATOM   13656 C  C   . GLN C 1 573 ? 13.209  32.161  118.842 1.00 25.28 ? 565  GLN C C   1 
ATOM   13657 O  O   . GLN C 1 573 ? 13.523  32.720  119.899 1.00 29.88 ? 565  GLN C O   1 
ATOM   13658 C  CB  . GLN C 1 573 ? 14.859  32.094  116.958 1.00 23.35 ? 565  GLN C CB  1 
ATOM   13659 C  CG  . GLN C 1 573 ? 15.397  33.469  117.375 1.00 26.56 ? 565  GLN C CG  1 
ATOM   13660 C  CD  . GLN C 1 573 ? 15.831  34.294  116.169 1.00 26.83 ? 565  GLN C CD  1 
ATOM   13661 O  OE1 . GLN C 1 573 ? 15.096  34.406  115.193 1.00 27.61 ? 565  GLN C OE1 1 
ATOM   13662 N  NE2 . GLN C 1 573 ? 17.030  34.855  116.228 1.00 23.96 ? 565  GLN C NE2 1 
ATOM   13663 N  N   . LYS C 1 574 ? 11.991  32.286  118.308 1.00 25.91 ? 566  LYS C N   1 
ATOM   13664 C  CA  . LYS C 1 574 ? 10.964  33.076  118.984 1.00 26.61 ? 566  LYS C CA  1 
ATOM   13665 C  C   . LYS C 1 574 ? 10.575  32.453  120.322 1.00 27.55 ? 566  LYS C C   1 
ATOM   13666 O  O   . LYS C 1 574 ? 10.460  33.153  121.337 1.00 29.22 ? 566  LYS C O   1 
ATOM   13667 C  CB  . LYS C 1 574 ? 9.740   33.227  118.079 1.00 32.07 ? 566  LYS C CB  1 
ATOM   13668 N  N   . VAL C 1 575 ? 10.364  31.135  120.347 1.00 29.69 ? 567  VAL C N   1 
ATOM   13669 C  CA  . VAL C 1 575 ? 10.014  30.468  121.600 1.00 34.51 ? 567  VAL C CA  1 
ATOM   13670 C  C   . VAL C 1 575 ? 11.118  30.670  122.629 1.00 36.42 ? 567  VAL C C   1 
ATOM   13671 O  O   . VAL C 1 575 ? 10.855  30.993  123.795 1.00 31.80 ? 567  VAL C O   1 
ATOM   13672 C  CB  . VAL C 1 575 ? 9.732   28.971  121.366 1.00 32.53 ? 567  VAL C CB  1 
ATOM   13673 C  CG1 . VAL C 1 575 ? 9.540   28.246  122.699 1.00 32.90 ? 567  VAL C CG1 1 
ATOM   13674 C  CG2 . VAL C 1 575 ? 8.505   28.790  120.492 1.00 30.86 ? 567  VAL C CG2 1 
ATOM   13675 N  N   . LEU C 1 576 ? 12.373  30.487  122.210 1.00 32.58 ? 568  LEU C N   1 
ATOM   13676 C  CA  . LEU C 1 576 ? 13.491  30.682  123.129 1.00 28.49 ? 568  LEU C CA  1 
ATOM   13677 C  C   . LEU C 1 576 ? 13.520  32.109  123.654 1.00 33.36 ? 568  LEU C C   1 
ATOM   13678 O  O   . LEU C 1 576 ? 13.651  32.333  124.862 1.00 37.16 ? 568  LEU C O   1 
ATOM   13679 C  CB  . LEU C 1 576 ? 14.814  30.329  122.437 1.00 27.10 ? 568  LEU C CB  1 
ATOM   13680 C  CG  . LEU C 1 576 ? 15.103  28.828  122.309 1.00 31.01 ? 568  LEU C CG  1 
ATOM   13681 C  CD1 . LEU C 1 576 ? 16.184  28.550  121.269 1.00 24.98 ? 568  LEU C CD1 1 
ATOM   13682 C  CD2 . LEU C 1 576 ? 15.493  28.219  123.645 1.00 33.90 ? 568  LEU C CD2 1 
ATOM   13683 N  N   . ALA C 1 577 ? 13.397  33.092  122.754 1.00 30.52 ? 569  ALA C N   1 
ATOM   13684 C  CA  . ALA C 1 577 ? 13.395  34.488  123.178 1.00 33.80 ? 569  ALA C CA  1 
ATOM   13685 C  C   . ALA C 1 577 ? 12.278  34.752  124.178 1.00 35.71 ? 569  ALA C C   1 
ATOM   13686 O  O   . ALA C 1 577 ? 12.473  35.485  125.155 1.00 35.40 ? 569  ALA C O   1 
ATOM   13687 C  CB  . ALA C 1 577 ? 13.262  35.411  121.968 1.00 35.15 ? 569  ALA C CB  1 
ATOM   13688 N  N   . GLY C 1 578 ? 11.109  34.148  123.966 1.00 35.97 ? 570  GLY C N   1 
ATOM   13689 C  CA  . GLY C 1 578 ? 10.019  34.302  124.915 1.00 38.21 ? 570  GLY C CA  1 
ATOM   13690 C  C   . GLY C 1 578 ? 10.322  33.742  126.287 1.00 43.83 ? 570  GLY C C   1 
ATOM   13691 O  O   . GLY C 1 578 ? 9.606   34.051  127.247 1.00 46.95 ? 570  GLY C O   1 
ATOM   13692 N  N   . GLN C 1 579 ? 11.371  32.924  126.404 1.00 45.46 ? 571  GLN C N   1 
ATOM   13693 C  CA  . GLN C 1 579 ? 11.777  32.310  127.662 1.00 45.51 ? 571  GLN C CA  1 
ATOM   13694 C  C   . GLN C 1 579 ? 13.070  32.911  128.205 1.00 43.66 ? 571  GLN C C   1 
ATOM   13695 O  O   . GLN C 1 579 ? 13.701  32.322  129.087 1.00 46.36 ? 571  GLN C O   1 
ATOM   13696 C  CB  . GLN C 1 579 ? 11.925  30.797  127.486 1.00 47.74 ? 571  GLN C CB  1 
ATOM   13697 C  CG  . GLN C 1 579 ? 10.691  30.122  126.905 1.00 50.97 ? 571  GLN C CG  1 
ATOM   13698 C  CD  . GLN C 1 579 ? 10.876  28.630  126.697 1.00 52.28 ? 571  GLN C CD  1 
ATOM   13699 O  OE1 . GLN C 1 579 ? 11.935  28.076  126.985 1.00 47.95 ? 571  GLN C OE1 1 
ATOM   13700 N  NE2 . GLN C 1 579 ? 9.837   27.971  126.199 1.00 56.38 ? 571  GLN C NE2 1 
ATOM   13701 N  N   . GLY C 1 580 ? 13.478  34.070  127.691 1.00 43.17 ? 572  GLY C N   1 
ATOM   13702 C  CA  . GLY C 1 580 ? 14.697  34.711  128.142 1.00 43.81 ? 572  GLY C CA  1 
ATOM   13703 C  C   . GLY C 1 580 ? 15.975  34.158  127.556 1.00 45.27 ? 572  GLY C C   1 
ATOM   13704 O  O   . GLY C 1 580 ? 17.051  34.390  128.120 1.00 39.55 ? 572  GLY C O   1 
ATOM   13705 N  N   . ILE C 1 581 ? 15.899  33.451  126.427 1.00 42.78 ? 573  ILE C N   1 
ATOM   13706 C  CA  . ILE C 1 581 ? 17.051  32.804  125.810 1.00 39.18 ? 573  ILE C CA  1 
ATOM   13707 C  C   . ILE C 1 581 ? 17.248  33.421  124.431 1.00 36.32 ? 573  ILE C C   1 
ATOM   13708 O  O   . ILE C 1 581 ? 16.436  33.202  123.523 1.00 33.95 ? 573  ILE C O   1 
ATOM   13709 C  CB  . ILE C 1 581 ? 16.870  31.284  125.714 1.00 36.83 ? 573  ILE C CB  1 
ATOM   13710 C  CG1 . ILE C 1 581 ? 16.622  30.691  127.104 1.00 36.93 ? 573  ILE C CG1 1 
ATOM   13711 C  CG2 . ILE C 1 581 ? 18.089  30.647  125.077 1.00 37.03 ? 573  ILE C CG2 1 
ATOM   13712 C  CD1 . ILE C 1 581 ? 16.361  29.194  127.097 1.00 34.90 ? 573  ILE C CD1 1 
ATOM   13713 N  N   . ALA C 1 582 ? 18.323  34.189  124.271 1.00 33.28 ? 574  ALA C N   1 
ATOM   13714 C  CA  . ALA C 1 582 ? 18.608  34.877  123.019 1.00 31.54 ? 574  ALA C CA  1 
ATOM   13715 C  C   . ALA C 1 582 ? 19.512  34.003  122.160 1.00 30.11 ? 574  ALA C C   1 
ATOM   13716 O  O   . ALA C 1 582 ? 20.632  33.677  122.566 1.00 32.79 ? 574  ALA C O   1 
ATOM   13717 C  CB  . ALA C 1 582 ? 19.263  36.233  123.284 1.00 38.64 ? 574  ALA C CB  1 
ATOM   13718 N  N   . VAL C 1 583 ? 19.023  33.620  120.978 1.00 28.19 ? 575  VAL C N   1 
ATOM   13719 C  CA  . VAL C 1 583 ? 19.815  32.866  120.018 1.00 25.71 ? 575  VAL C CA  1 
ATOM   13720 C  C   . VAL C 1 583 ? 19.738  33.554  118.661 1.00 24.96 ? 575  VAL C C   1 
ATOM   13721 O  O   . VAL C 1 583 ? 18.815  34.314  118.365 1.00 26.00 ? 575  VAL C O   1 
ATOM   13722 C  CB  . VAL C 1 583 ? 19.367  31.388  119.902 1.00 30.45 ? 575  VAL C CB  1 
ATOM   13723 C  CG1 . VAL C 1 583 ? 19.330  30.732  121.277 1.00 25.73 ? 575  VAL C CG1 1 
ATOM   13724 C  CG2 . VAL C 1 583 ? 18.017  31.281  119.210 1.00 28.55 ? 575  VAL C CG2 1 
ATOM   13725 N  N   . ARG C 1 584 ? 20.745  33.286  117.847 1.00 24.17 ? 576  ARG C N   1 
ATOM   13726 C  CA  . ARG C 1 584 ? 20.836  33.742  116.471 1.00 23.36 ? 576  ARG C CA  1 
ATOM   13727 C  C   . ARG C 1 584 ? 20.500  32.568  115.556 1.00 22.05 ? 576  ARG C C   1 
ATOM   13728 O  O   . ARG C 1 584 ? 20.704  31.413  115.925 1.00 22.67 ? 576  ARG C O   1 
ATOM   13729 C  CB  . ARG C 1 584 ? 22.251  34.287  116.214 1.00 23.56 ? 576  ARG C CB  1 
ATOM   13730 C  CG  . ARG C 1 584 ? 22.801  34.169  114.826 1.00 33.85 ? 576  ARG C CG  1 
ATOM   13731 C  CD  . ARG C 1 584 ? 24.314  34.365  114.844 1.00 26.10 ? 576  ARG C CD  1 
ATOM   13732 N  NE  . ARG C 1 584 ? 24.708  35.734  115.173 1.00 26.51 ? 576  ARG C NE  1 
ATOM   13733 C  CZ  . ARG C 1 584 ? 25.885  36.256  114.846 1.00 28.59 ? 576  ARG C CZ  1 
ATOM   13734 N  NH1 . ARG C 1 584 ? 26.758  35.520  114.177 1.00 25.08 ? 576  ARG C NH1 1 
ATOM   13735 N  NH2 . ARG C 1 584 ? 26.188  37.511  115.175 1.00 27.46 ? 576  ARG C NH2 1 
ATOM   13736 N  N   . VAL C 1 585 ? 19.948  32.859  114.378 1.00 22.53 ? 577  VAL C N   1 
ATOM   13737 C  CA  . VAL C 1 585 ? 19.638  31.829  113.386 1.00 20.14 ? 577  VAL C CA  1 
ATOM   13738 C  C   . VAL C 1 585 ? 20.450  32.114  112.132 1.00 19.48 ? 577  VAL C C   1 
ATOM   13739 O  O   . VAL C 1 585 ? 20.357  33.205  111.553 1.00 24.71 ? 577  VAL C O   1 
ATOM   13740 C  CB  . VAL C 1 585 ? 18.139  31.755  113.055 1.00 20.21 ? 577  VAL C CB  1 
ATOM   13741 C  CG1 . VAL C 1 585 ? 17.905  30.707  111.966 1.00 19.63 ? 577  VAL C CG1 1 
ATOM   13742 C  CG2 . VAL C 1 585 ? 17.323  31.423  114.308 1.00 22.54 ? 577  VAL C CG2 1 
ATOM   13743 N  N   . VAL C 1 586 ? 21.237  31.136  111.712 1.00 18.77 ? 578  VAL C N   1 
ATOM   13744 C  CA  . VAL C 1 586 ? 22.054  31.226  110.511 1.00 18.15 ? 578  VAL C CA  1 
ATOM   13745 C  C   . VAL C 1 586 ? 21.431  30.318  109.465 1.00 17.06 ? 578  VAL C C   1 
ATOM   13746 O  O   . VAL C 1 586 ? 21.148  29.148  109.740 1.00 16.67 ? 578  VAL C O   1 
ATOM   13747 C  CB  . VAL C 1 586 ? 23.514  30.835  110.802 1.00 18.33 ? 578  VAL C CB  1 
ATOM   13748 C  CG1 . VAL C 1 586 ? 24.284  30.517  109.517 1.00 17.57 ? 578  VAL C CG1 1 
ATOM   13749 C  CG2 . VAL C 1 586 ? 24.199  31.957  111.589 1.00 19.47 ? 578  VAL C CG2 1 
ATOM   13750 N  N   . SER C 1 587 ? 21.189  30.863  108.281 1.00 16.65 ? 579  SER C N   1 
ATOM   13751 C  CA  . SER C 1 587 ? 20.797  30.044  107.149 1.00 15.66 ? 579  SER C CA  1 
ATOM   13752 C  C   . SER C 1 587 ? 22.060  29.660  106.399 1.00 16.56 ? 579  SER C C   1 
ATOM   13753 O  O   . SER C 1 587 ? 22.898  30.520  106.108 1.00 19.98 ? 579  SER C O   1 
ATOM   13754 C  CB  . SER C 1 587 ? 19.824  30.789  106.233 1.00 18.99 ? 579  SER C CB  1 
ATOM   13755 O  OG  . SER C 1 587 ? 19.495  29.988  105.105 1.00 15.50 ? 579  SER C OG  1 
ATOM   13756 N  N   . MET C 1 588 ? 22.212  28.374  106.095 1.00 18.02 ? 580  MET C N   1 
ATOM   13757 C  CA  . MET C 1 588 ? 23.406  27.888  105.414 1.00 17.51 ? 580  MET C CA  1 
ATOM   13758 C  C   . MET C 1 588 ? 22.986  27.206  104.117 1.00 17.55 ? 580  MET C C   1 
ATOM   13759 O  O   . MET C 1 588 ? 23.078  25.979  103.992 1.00 13.53 ? 580  MET C O   1 
ATOM   13760 C  CB  . MET C 1 588 ? 24.223  26.953  106.306 1.00 14.41 ? 580  MET C CB  1 
ATOM   13761 C  CG  . MET C 1 588 ? 25.587  26.580  105.706 1.00 14.30 ? 580  MET C CG  1 
ATOM   13762 S  SD  . MET C 1 588 ? 26.716  25.754  106.848 1.00 16.28 ? 580  MET C SD  1 
ATOM   13763 C  CE  . MET C 1 588 ? 27.130  27.096  107.969 1.00 16.04 ? 580  MET C CE  1 
ATOM   13764 N  N   . PRO C 1 589 ? 22.530  27.978  103.122 1.00 16.69 ? 581  PRO C N   1 
ATOM   13765 C  CA  . PRO C 1 589 ? 22.074  27.350  101.872 1.00 12.37 ? 581  PRO C CA  1 
ATOM   13766 C  C   . PRO C 1 589 ? 23.165  26.557  101.145 1.00 11.98 ? 581  PRO C C   1 
ATOM   13767 O  O   . PRO C 1 589 ? 22.837  25.628  100.403 1.00 12.07 ? 581  PRO C O   1 
ATOM   13768 C  CB  . PRO C 1 589 ? 21.570  28.543  101.045 1.00 16.03 ? 581  PRO C CB  1 
ATOM   13769 C  CG  . PRO C 1 589 ? 22.240  29.759  101.636 1.00 17.74 ? 581  PRO C CG  1 
ATOM   13770 C  CD  . PRO C 1 589 ? 22.332  29.440  103.106 1.00 16.40 ? 581  PRO C CD  1 
ATOM   13771 N  N   . SER C 1 590 ? 24.446  26.869  101.336 1.00 12.83 ? 582  SER C N   1 
ATOM   13772 C  CA  . SER C 1 590 ? 25.499  26.043  100.748 1.00 14.16 ? 582  SER C CA  1 
ATOM   13773 C  C   . SER C 1 590 ? 26.666  25.951  101.719 1.00 14.29 ? 582  SER C C   1 
ATOM   13774 O  O   . SER C 1 590 ? 27.412  26.922  101.883 1.00 13.44 ? 582  SER C O   1 
ATOM   13775 C  CB  . SER C 1 590 ? 25.972  26.600  99.404  1.00 12.08 ? 582  SER C CB  1 
ATOM   13776 O  OG  . SER C 1 590 ? 26.999  25.777  98.874  1.00 11.96 ? 582  SER C OG  1 
ATOM   13777 N  N   . THR C 1 591 ? 26.833  24.786  102.347 1.00 13.95 ? 583  THR C N   1 
ATOM   13778 C  CA  . THR C 1 591 ? 28.052  24.541  103.115 1.00 15.38 ? 583  THR C CA  1 
ATOM   13779 C  C   . THR C 1 591 ? 29.287  24.701  102.237 1.00 14.35 ? 583  THR C C   1 
ATOM   13780 O  O   . THR C 1 591 ? 30.300  25.243  102.681 1.00 14.95 ? 583  THR C O   1 
ATOM   13781 C  CB  . THR C 1 591 ? 28.040  23.136  103.727 1.00 16.72 ? 583  THR C CB  1 
ATOM   13782 O  OG1 . THR C 1 591 ? 28.049  22.168  102.667 1.00 16.86 ? 583  THR C OG1 1 
ATOM   13783 C  CG2 . THR C 1 591 ? 26.809  22.917  104.625 1.00 14.70 ? 583  THR C CG2 1 
ATOM   13784 N  N   . SER C 1 592 ? 29.215  24.214  100.988 1.00 13.33 ? 584  SER C N   1 
ATOM   13785 C  CA  . SER C 1 592 ? 30.354  24.264  100.074 1.00 18.04 ? 584  SER C CA  1 
ATOM   13786 C  C   . SER C 1 592 ? 30.869  25.685  99.917  1.00 17.88 ? 584  SER C C   1 
ATOM   13787 O  O   . SER C 1 592 ? 32.079  25.935  99.976  1.00 19.04 ? 584  SER C O   1 
ATOM   13788 C  CB  . SER C 1 592 ? 29.942  23.703  98.708  1.00 13.36 ? 584  SER C CB  1 
ATOM   13789 O  OG  . SER C 1 592 ? 28.926  22.705  98.847  1.00 12.94 ? 584  SER C OG  1 
ATOM   13790 N  N   . VAL C 1 593 ? 29.955  26.631  99.694  1.00 13.63 ? 585  VAL C N   1 
ATOM   13791 C  CA  . VAL C 1 593 ? 30.356  28.010  99.462  1.00 16.87 ? 585  VAL C CA  1 
ATOM   13792 C  C   . VAL C 1 593 ? 30.811  28.661  100.757 1.00 15.11 ? 585  VAL C C   1 
ATOM   13793 O  O   . VAL C 1 593 ? 31.805  29.388  100.782 1.00 17.10 ? 585  VAL C O   1 
ATOM   13794 C  CB  . VAL C 1 593 ? 29.205  28.794  98.812  1.00 17.05 ? 585  VAL C CB  1 
ATOM   13795 C  CG1 . VAL C 1 593 ? 29.561  30.263  98.730  1.00 18.49 ? 585  VAL C CG1 1 
ATOM   13796 C  CG2 . VAL C 1 593 ? 28.919  28.227  97.429  1.00 16.68 ? 585  VAL C CG2 1 
ATOM   13797 N  N   . PHE C 1 594 ? 30.091  28.416  101.850 1.00 15.05 ? 586  PHE C N   1 
ATOM   13798 C  CA  . PHE C 1 594 ? 30.485  29.009  103.125 1.00 18.10 ? 586  PHE C CA  1 
ATOM   13799 C  C   . PHE C 1 594 ? 31.917  28.635  103.488 1.00 17.72 ? 586  PHE C C   1 
ATOM   13800 O  O   . PHE C 1 594 ? 32.696  29.488  103.934 1.00 18.98 ? 586  PHE C O   1 
ATOM   13801 C  CB  . PHE C 1 594 ? 29.524  28.569  104.230 1.00 15.77 ? 586  PHE C CB  1 
ATOM   13802 C  CG  . PHE C 1 594 ? 29.878  29.129  105.573 1.00 22.04 ? 586  PHE C CG  1 
ATOM   13803 C  CD1 . PHE C 1 594 ? 29.865  30.498  105.788 1.00 18.41 ? 586  PHE C CD1 1 
ATOM   13804 C  CD2 . PHE C 1 594 ? 30.242  28.291  106.611 1.00 20.61 ? 586  PHE C CD2 1 
ATOM   13805 C  CE1 . PHE C 1 594 ? 30.194  31.020  107.028 1.00 21.38 ? 586  PHE C CE1 1 
ATOM   13806 C  CE2 . PHE C 1 594 ? 30.575  28.810  107.852 1.00 21.17 ? 586  PHE C CE2 1 
ATOM   13807 C  CZ  . PHE C 1 594 ? 30.549  30.170  108.060 1.00 22.24 ? 586  PHE C CZ  1 
ATOM   13808 N  N   . ASP C 1 595 ? 32.278  27.363  103.288 1.00 19.62 ? 587  ASP C N   1 
ATOM   13809 C  CA  . ASP C 1 595 ? 33.606  26.855  103.614 1.00 16.93 ? 587  ASP C CA  1 
ATOM   13810 C  C   . ASP C 1 595 ? 34.720  27.597  102.885 1.00 21.15 ? 587  ASP C C   1 
ATOM   13811 O  O   . ASP C 1 595 ? 35.865  27.581  103.357 1.00 22.84 ? 587  ASP C O   1 
ATOM   13812 C  CB  . ASP C 1 595 ? 33.688  25.361  103.275 1.00 16.80 ? 587  ASP C CB  1 
ATOM   13813 C  CG  . ASP C 1 595 ? 32.907  24.495  104.240 1.00 23.47 ? 587  ASP C CG  1 
ATOM   13814 O  OD1 . ASP C 1 595 ? 32.576  24.972  105.345 1.00 29.14 ? 587  ASP C OD1 1 
ATOM   13815 O  OD2 . ASP C 1 595 ? 32.627  23.327  103.887 1.00 26.86 ? 587  ASP C OD2 1 
ATOM   13816 N  N   . ARG C 1 596 ? 34.415  28.236  101.749 1.00 22.39 ? 588  ARG C N   1 
ATOM   13817 C  CA  . ARG C 1 596 ? 35.391  28.994  100.967 1.00 23.87 ? 588  ARG C CA  1 
ATOM   13818 C  C   . ARG C 1 596 ? 35.519  30.447  101.388 1.00 27.36 ? 588  ARG C C   1 
ATOM   13819 O  O   . ARG C 1 596 ? 36.399  31.142  100.873 1.00 23.17 ? 588  ARG C O   1 
ATOM   13820 C  CB  . ARG C 1 596 ? 35.026  28.993  99.478  1.00 31.22 ? 588  ARG C CB  1 
ATOM   13821 C  CG  . ARG C 1 596 ? 34.960  27.649  98.834  1.00 34.74 ? 588  ARG C CG  1 
ATOM   13822 C  CD  . ARG C 1 596 ? 35.169  27.785  97.336  1.00 35.43 ? 588  ARG C CD  1 
ATOM   13823 N  NE  . ARG C 1 596 ? 34.052  28.435  96.649  1.00 32.00 ? 588  ARG C NE  1 
ATOM   13824 C  CZ  . ARG C 1 596 ? 32.963  27.788  96.246  1.00 23.57 ? 588  ARG C CZ  1 
ATOM   13825 N  NH1 . ARG C 1 596 ? 32.844  26.495  96.488  1.00 21.40 ? 588  ARG C NH1 1 
ATOM   13826 N  NH2 . ARG C 1 596 ? 31.995  28.427  95.611  1.00 27.83 ? 588  ARG C NH2 1 
ATOM   13827 N  N   . GLN C 1 597 ? 34.655  30.937  102.273 1.00 20.50 ? 589  GLN C N   1 
ATOM   13828 C  CA  . GLN C 1 597 ? 34.735  32.332  102.687 1.00 19.54 ? 589  GLN C CA  1 
ATOM   13829 C  C   . GLN C 1 597 ? 35.926  32.550  103.614 1.00 24.04 ? 589  GLN C C   1 
ATOM   13830 O  O   . GLN C 1 597 ? 36.368  31.636  104.314 1.00 25.88 ? 589  GLN C O   1 
ATOM   13831 C  CB  . GLN C 1 597 ? 33.441  32.754  103.388 1.00 19.24 ? 589  GLN C CB  1 
ATOM   13832 C  CG  . GLN C 1 597 ? 32.188  32.473  102.579 1.00 18.11 ? 589  GLN C CG  1 
ATOM   13833 C  CD  . GLN C 1 597 ? 32.226  33.127  101.212 1.00 20.83 ? 589  GLN C CD  1 
ATOM   13834 O  OE1 . GLN C 1 597 ? 32.390  34.337  101.102 1.00 21.62 ? 589  GLN C OE1 1 
ATOM   13835 N  NE2 . GLN C 1 597 ? 32.088  32.320  100.157 1.00 20.73 ? 589  GLN C NE2 1 
ATOM   13836 N  N   . ASP C 1 598 ? 36.444  33.778  103.620 1.00 25.58 ? 590  ASP C N   1 
ATOM   13837 C  CA  . ASP C 1 598 ? 37.591  34.075  104.465 1.00 30.24 ? 590  ASP C CA  1 
ATOM   13838 C  C   . ASP C 1 598 ? 37.237  33.848  105.935 1.00 29.14 ? 590  ASP C C   1 
ATOM   13839 O  O   . ASP C 1 598 ? 36.063  33.808  106.325 1.00 23.89 ? 590  ASP C O   1 
ATOM   13840 C  CB  . ASP C 1 598 ? 38.096  35.505  104.224 1.00 40.94 ? 590  ASP C CB  1 
ATOM   13841 C  CG  . ASP C 1 598 ? 37.042  36.566  104.502 1.00 50.10 ? 590  ASP C CG  1 
ATOM   13842 O  OD1 . ASP C 1 598 ? 36.618  36.707  105.668 1.00 45.98 ? 590  ASP C OD1 1 
ATOM   13843 O  OD2 . ASP C 1 598 ? 36.654  37.281  103.552 1.00 54.58 ? 590  ASP C OD2 1 
ATOM   13844 N  N   . ALA C 1 599 ? 38.280  33.670  106.751 1.00 30.44 ? 591  ALA C N   1 
ATOM   13845 C  CA  . ALA C 1 599 ? 38.080  33.257  108.138 1.00 32.89 ? 591  ALA C CA  1 
ATOM   13846 C  C   . ALA C 1 599 ? 37.337  34.313  108.939 1.00 29.75 ? 591  ALA C C   1 
ATOM   13847 O  O   . ALA C 1 599 ? 36.558  33.973  109.836 1.00 29.18 ? 591  ALA C O   1 
ATOM   13848 C  CB  . ALA C 1 599 ? 39.427  32.944  108.789 1.00 39.14 ? 591  ALA C CB  1 
ATOM   13849 N  N   . ALA C 1 600 ? 37.566  35.592  108.630 1.00 30.01 ? 592  ALA C N   1 
ATOM   13850 C  CA  . ALA C 1 600 ? 36.841  36.672  109.291 1.00 31.78 ? 592  ALA C CA  1 
ATOM   13851 C  C   . ALA C 1 600 ? 35.340  36.540  109.074 1.00 28.82 ? 592  ALA C C   1 
ATOM   13852 O  O   . ALA C 1 600 ? 34.550  36.669  110.019 1.00 30.19 ? 592  ALA C O   1 
ATOM   13853 C  CB  . ALA C 1 600 ? 37.334  38.023  108.778 1.00 31.69 ? 592  ALA C CB  1 
ATOM   13854 N  N   . TYR C 1 601 ? 34.923  36.295  107.829 1.00 27.12 ? 593  TYR C N   1 
ATOM   13855 C  CA  . TYR C 1 601 ? 33.495  36.162  107.564 1.00 24.05 ? 593  TYR C CA  1 
ATOM   13856 C  C   . TYR C 1 601 ? 32.914  34.947  108.273 1.00 24.34 ? 593  TYR C C   1 
ATOM   13857 O  O   . TYR C 1 601 ? 31.815  35.017  108.835 1.00 28.01 ? 593  TYR C O   1 
ATOM   13858 C  CB  . TYR C 1 601 ? 33.216  36.072  106.061 1.00 23.37 ? 593  TYR C CB  1 
ATOM   13859 C  CG  . TYR C 1 601 ? 31.731  35.992  105.778 1.00 23.76 ? 593  TYR C CG  1 
ATOM   13860 C  CD1 . TYR C 1 601 ? 30.942  37.137  105.801 1.00 26.67 ? 593  TYR C CD1 1 
ATOM   13861 C  CD2 . TYR C 1 601 ? 31.108  34.773  105.543 1.00 22.74 ? 593  TYR C CD2 1 
ATOM   13862 C  CE1 . TYR C 1 601 ? 29.584  37.075  105.576 1.00 24.33 ? 593  TYR C CE1 1 
ATOM   13863 C  CE2 . TYR C 1 601 ? 29.751  34.701  105.304 1.00 21.44 ? 593  TYR C CE2 1 
ATOM   13864 C  CZ  . TYR C 1 601 ? 28.989  35.852  105.325 1.00 21.07 ? 593  TYR C CZ  1 
ATOM   13865 O  OH  . TYR C 1 601 ? 27.628  35.775  105.104 1.00 19.42 ? 593  TYR C OH  1 
ATOM   13866 N  N   . GLN C 1 602 ? 33.629  33.823  108.254 1.00 22.65 ? 594  GLN C N   1 
ATOM   13867 C  CA  . GLN C 1 602 ? 33.108  32.628  108.907 1.00 23.11 ? 594  GLN C CA  1 
ATOM   13868 C  C   . GLN C 1 602 ? 32.936  32.845  110.403 1.00 25.55 ? 594  GLN C C   1 
ATOM   13869 O  O   . GLN C 1 602 ? 31.994  32.319  111.007 1.00 23.06 ? 594  GLN C O   1 
ATOM   13870 C  CB  . GLN C 1 602 ? 34.028  31.440  108.648 1.00 24.78 ? 594  GLN C CB  1 
ATOM   13871 C  CG  . GLN C 1 602 ? 34.127  31.045  107.184 1.00 25.66 ? 594  GLN C CG  1 
ATOM   13872 C  CD  . GLN C 1 602 ? 34.672  29.650  107.020 1.00 29.26 ? 594  GLN C CD  1 
ATOM   13873 O  OE1 . GLN C 1 602 ? 34.477  28.792  107.882 1.00 34.28 ? 594  GLN C OE1 1 
ATOM   13874 N  NE2 . GLN C 1 602 ? 35.359  29.411  105.916 1.00 27.72 ? 594  GLN C NE2 1 
ATOM   13875 N  N   . ALA C 1 603 ? 33.834  33.622  111.016 1.00 26.93 ? 595  ALA C N   1 
ATOM   13876 C  CA  . ALA C 1 603 ? 33.722  33.899  112.441 1.00 28.61 ? 595  ALA C CA  1 
ATOM   13877 C  C   . ALA C 1 603 ? 32.603  34.889  112.736 1.00 27.77 ? 595  ALA C C   1 
ATOM   13878 O  O   . ALA C 1 603 ? 31.992  34.831  113.810 1.00 25.55 ? 595  ALA C O   1 
ATOM   13879 C  CB  . ALA C 1 603 ? 35.059  34.417  112.981 1.00 32.40 ? 595  ALA C CB  1 
ATOM   13880 N  N   . ALA C 1 604 ? 32.327  35.812  111.812 1.00 25.88 ? 596  ALA C N   1 
ATOM   13881 C  CA  . ALA C 1 604 ? 31.197  36.716  112.005 1.00 29.75 ? 596  ALA C CA  1 
ATOM   13882 C  C   . ALA C 1 604 ? 29.875  35.961  111.977 1.00 27.35 ? 596  ALA C C   1 
ATOM   13883 O  O   . ALA C 1 604 ? 28.938  36.312  112.705 1.00 24.42 ? 596  ALA C O   1 
ATOM   13884 C  CB  . ALA C 1 604 ? 31.205  37.807  110.935 1.00 29.63 ? 596  ALA C CB  1 
ATOM   13885 N  N   . VAL C 1 605 ? 29.782  34.926  111.147 1.00 27.66 ? 597  VAL C N   1 
ATOM   13886 C  CA  . VAL C 1 605 ? 28.564  34.129  111.083 1.00 23.65 ? 597  VAL C CA  1 
ATOM   13887 C  C   . VAL C 1 605 ? 28.494  33.149  112.246 1.00 21.64 ? 597  VAL C C   1 
ATOM   13888 O  O   . VAL C 1 605 ? 27.430  32.967  112.858 1.00 22.26 ? 597  VAL C O   1 
ATOM   13889 C  CB  . VAL C 1 605 ? 28.493  33.405  109.726 1.00 20.70 ? 597  VAL C CB  1 
ATOM   13890 C  CG1 . VAL C 1 605 ? 27.251  32.548  109.646 1.00 21.29 ? 597  VAL C CG1 1 
ATOM   13891 C  CG2 . VAL C 1 605 ? 28.526  34.423  108.585 1.00 21.52 ? 597  VAL C CG2 1 
ATOM   13892 N  N   . LEU C 1 606 ? 29.623  32.501  112.567 1.00 24.74 ? 598  LEU C N   1 
ATOM   13893 C  CA  . LEU C 1 606 ? 29.710  31.470  113.603 1.00 23.57 ? 598  LEU C CA  1 
ATOM   13894 C  C   . LEU C 1 606 ? 30.778  31.889  114.611 1.00 27.74 ? 598  LEU C C   1 
ATOM   13895 O  O   . LEU C 1 606 ? 31.922  31.416  114.548 1.00 27.97 ? 598  LEU C O   1 
ATOM   13896 C  CB  . LEU C 1 606 ? 30.032  30.101  112.999 1.00 21.27 ? 598  LEU C CB  1 
ATOM   13897 C  CG  . LEU C 1 606 ? 29.088  29.525  111.933 1.00 19.96 ? 598  LEU C CG  1 
ATOM   13898 C  CD1 . LEU C 1 606 ? 29.551  28.150  111.492 1.00 19.34 ? 598  LEU C CD1 1 
ATOM   13899 C  CD2 . LEU C 1 606 ? 27.648  29.459  112.447 1.00 19.73 ? 598  LEU C CD2 1 
ATOM   13900 N  N   . PRO C 1 607 ? 30.438  32.758  115.561 1.00 28.49 ? 599  PRO C N   1 
ATOM   13901 C  CA  . PRO C 1 607 ? 31.450  33.269  116.502 1.00 30.64 ? 599  PRO C CA  1 
ATOM   13902 C  C   . PRO C 1 607 ? 32.062  32.170  117.359 1.00 33.84 ? 599  PRO C C   1 
ATOM   13903 O  O   . PRO C 1 607 ? 31.383  31.231  117.776 1.00 26.69 ? 599  PRO C O   1 
ATOM   13904 C  CB  . PRO C 1 607 ? 30.664  34.265  117.357 1.00 30.29 ? 599  PRO C CB  1 
ATOM   13905 C  CG  . PRO C 1 607 ? 29.513  34.672  116.492 1.00 31.18 ? 599  PRO C CG  1 
ATOM   13906 C  CD  . PRO C 1 607 ? 29.140  33.428  115.733 1.00 27.58 ? 599  PRO C CD  1 
ATOM   13907 N  N   . GLU C 1 608 ? 33.360  32.305  117.629 1.00 33.47 ? 600  GLU C N   1 
ATOM   13908 C  CA  . GLU C 1 608 ? 34.059  31.341  118.470 1.00 37.97 ? 600  GLU C CA  1 
ATOM   13909 C  C   . GLU C 1 608 ? 33.431  31.269  119.857 1.00 39.65 ? 600  GLU C C   1 
ATOM   13910 O  O   . GLU C 1 608 ? 33.052  32.286  120.443 1.00 37.05 ? 600  GLU C O   1 
ATOM   13911 C  CB  . GLU C 1 608 ? 35.538  31.715  118.586 1.00 34.49 ? 600  GLU C CB  1 
ATOM   13912 N  N   . GLY C 1 609 ? 33.312  30.050  120.382 1.00 40.50 ? 601  GLY C N   1 
ATOM   13913 C  CA  . GLY C 1 609 ? 32.773  29.841  121.708 1.00 42.16 ? 601  GLY C CA  1 
ATOM   13914 C  C   . GLY C 1 609 ? 31.267  29.937  121.829 1.00 42.64 ? 601  GLY C C   1 
ATOM   13915 O  O   . GLY C 1 609 ? 30.736  29.692  122.919 1.00 41.53 ? 601  GLY C O   1 
ATOM   13916 N  N   . LEU C 1 610 ? 30.558  30.290  120.761 1.00 34.82 ? 602  LEU C N   1 
ATOM   13917 C  CA  . LEU C 1 610 ? 29.104  30.321  120.792 1.00 35.38 ? 602  LEU C CA  1 
ATOM   13918 C  C   . LEU C 1 610 ? 28.571  28.946  120.414 1.00 31.95 ? 602  LEU C C   1 
ATOM   13919 O  O   . LEU C 1 610 ? 28.822  28.490  119.291 1.00 26.03 ? 602  LEU C O   1 
ATOM   13920 C  CB  . LEU C 1 610 ? 28.573  31.368  119.832 1.00 35.74 ? 602  LEU C CB  1 
ATOM   13921 C  CG  . LEU C 1 610 ? 27.095  31.741  119.921 1.00 36.50 ? 602  LEU C CG  1 
ATOM   13922 C  CD1 . LEU C 1 610 ? 26.811  32.446  121.239 1.00 40.54 ? 602  LEU C CD1 1 
ATOM   13923 C  CD2 . LEU C 1 610 ? 26.688  32.613  118.734 1.00 30.39 ? 602  LEU C CD2 1 
ATOM   13924 N  N   . PRO C 1 611 ? 27.860  28.253  121.309 1.00 34.80 ? 603  PRO C N   1 
ATOM   13925 C  CA  . PRO C 1 611 ? 27.395  26.894  121.005 1.00 30.77 ? 603  PRO C CA  1 
ATOM   13926 C  C   . PRO C 1 611 ? 26.506  26.858  119.772 1.00 25.20 ? 603  PRO C C   1 
ATOM   13927 O  O   . PRO C 1 611 ? 25.702  27.760  119.534 1.00 25.13 ? 603  PRO C O   1 
ATOM   13928 C  CB  . PRO C 1 611 ? 26.615  26.500  122.261 1.00 28.34 ? 603  PRO C CB  1 
ATOM   13929 C  CG  . PRO C 1 611 ? 27.177  27.350  123.333 1.00 27.20 ? 603  PRO C CG  1 
ATOM   13930 C  CD  . PRO C 1 611 ? 27.546  28.646  122.692 1.00 34.39 ? 603  PRO C CD  1 
ATOM   13931 N  N   . ARG C 1 612 ? 26.650  25.792  118.992 1.00 22.99 ? 604  ARG C N   1 
ATOM   13932 C  CA  . ARG C 1 612 ? 25.993  25.687  117.700 1.00 23.01 ? 604  ARG C CA  1 
ATOM   13933 C  C   . ARG C 1 612 ? 25.084  24.469  117.670 1.00 22.88 ? 604  ARG C C   1 
ATOM   13934 O  O   . ARG C 1 612 ? 25.451  23.396  118.158 1.00 24.60 ? 604  ARG C O   1 
ATOM   13935 C  CB  . ARG C 1 612 ? 27.024  25.603  116.566 1.00 28.36 ? 604  ARG C CB  1 
ATOM   13936 C  CG  . ARG C 1 612 ? 28.101  26.688  116.647 1.00 21.67 ? 604  ARG C CG  1 
ATOM   13937 C  CD  . ARG C 1 612 ? 29.279  26.370  115.740 1.00 22.33 ? 604  ARG C CD  1 
ATOM   13938 N  NE  . ARG C 1 612 ? 30.249  27.459  115.743 1.00 25.40 ? 604  ARG C NE  1 
ATOM   13939 C  CZ  . ARG C 1 612 ? 31.496  27.368  115.300 1.00 26.69 ? 604  ARG C CZ  1 
ATOM   13940 N  NH1 . ARG C 1 612 ? 31.953  26.224  114.808 1.00 24.73 ? 604  ARG C NH1 1 
ATOM   13941 N  NH2 . ARG C 1 612 ? 32.292  28.426  115.363 1.00 31.36 ? 604  ARG C NH2 1 
ATOM   13942 N  N   . ILE C 1 613 ? 23.896  24.655  117.097 1.00 21.67 ? 605  ILE C N   1 
ATOM   13943 C  CA  . ILE C 1 613 ? 22.912  23.600  116.884 1.00 21.29 ? 605  ILE C CA  1 
ATOM   13944 C  C   . ILE C 1 613 ? 22.520  23.624  115.417 1.00 20.73 ? 605  ILE C C   1 
ATOM   13945 O  O   . ILE C 1 613 ? 22.038  24.648  114.922 1.00 24.68 ? 605  ILE C O   1 
ATOM   13946 C  CB  . ILE C 1 613 ? 21.660  23.787  117.756 1.00 22.53 ? 605  ILE C CB  1 
ATOM   13947 C  CG1 . ILE C 1 613 ? 22.027  23.829  119.242 1.00 25.65 ? 605  ILE C CG1 1 
ATOM   13948 C  CG2 . ILE C 1 613 ? 20.647  22.712  117.443 1.00 19.94 ? 605  ILE C CG2 1 
ATOM   13949 C  CD1 . ILE C 1 613 ? 22.226  25.253  119.759 1.00 28.12 ? 605  ILE C CD1 1 
ATOM   13950 N  N   . ALA C 1 614 ? 22.703  22.503  114.727 1.00 17.59 ? 606  ALA C N   1 
ATOM   13951 C  CA  . ALA C 1 614 ? 22.307  22.395  113.333 1.00 16.56 ? 606  ALA C CA  1 
ATOM   13952 C  C   . ALA C 1 614 ? 20.962  21.679  113.235 1.00 20.44 ? 606  ALA C C   1 
ATOM   13953 O  O   . ALA C 1 614 ? 20.681  20.751  114.000 1.00 16.41 ? 606  ALA C O   1 
ATOM   13954 C  CB  . ALA C 1 614 ? 23.367  21.657  112.522 1.00 17.46 ? 606  ALA C CB  1 
ATOM   13955 N  N   . VAL C 1 615 ? 20.120  22.137  112.310 1.00 16.29 ? 607  VAL C N   1 
ATOM   13956 C  CA  . VAL C 1 615 ? 18.794  21.566  112.091 1.00 16.11 ? 607  VAL C CA  1 
ATOM   13957 C  C   . VAL C 1 615 ? 18.650  21.317  110.603 1.00 17.99 ? 607  VAL C C   1 
ATOM   13958 O  O   . VAL C 1 615 ? 18.678  22.266  109.808 1.00 14.16 ? 607  VAL C O   1 
ATOM   13959 C  CB  . VAL C 1 615 ? 17.663  22.483  112.586 1.00 17.20 ? 607  VAL C CB  1 
ATOM   13960 C  CG1 . VAL C 1 615 ? 16.311  21.778  112.436 1.00 19.66 ? 607  VAL C CG1 1 
ATOM   13961 C  CG2 . VAL C 1 615 ? 17.906  22.921  114.027 1.00 19.03 ? 607  VAL C CG2 1 
ATOM   13962 N  N   . GLU C 1 616 ? 18.505  20.048  110.225 1.00 15.15 ? 608  GLU C N   1 
ATOM   13963 C  CA  . GLU C 1 616 ? 18.384  19.686  108.819 1.00 12.95 ? 608  GLU C CA  1 
ATOM   13964 C  C   . GLU C 1 616 ? 17.748  18.310  108.742 1.00 16.48 ? 608  GLU C C   1 
ATOM   13965 O  O   . GLU C 1 616 ? 18.136  17.405  109.489 1.00 13.17 ? 608  GLU C O   1 
ATOM   13966 C  CB  . GLU C 1 616 ? 19.747  19.671  108.121 1.00 12.58 ? 608  GLU C CB  1 
ATOM   13967 C  CG  . GLU C 1 616 ? 19.687  19.252  106.662 1.00 12.50 ? 608  GLU C CG  1 
ATOM   13968 C  CD  . GLU C 1 616 ? 21.005  19.490  105.964 1.00 13.15 ? 608  GLU C CD  1 
ATOM   13969 O  OE1 . GLU C 1 616 ? 21.922  18.672  106.163 1.00 14.83 ? 608  GLU C OE1 1 
ATOM   13970 O  OE2 . GLU C 1 616 ? 21.127  20.508  105.248 1.00 15.29 ? 608  GLU C OE2 1 
ATOM   13971 N  N   . ALA C 1 617 ? 16.790  18.146  107.826 1.00 13.44 ? 609  ALA C N   1 
ATOM   13972 C  CA  . ALA C 1 617 ? 16.041  16.890  107.746 1.00 16.36 ? 609  ALA C CA  1 
ATOM   13973 C  C   . ALA C 1 617 ? 16.839  15.851  106.955 1.00 17.30 ? 609  ALA C C   1 
ATOM   13974 O  O   . ALA C 1 617 ? 16.472  15.420  105.863 1.00 16.01 ? 609  ALA C O   1 
ATOM   13975 C  CB  . ALA C 1 617 ? 14.660  17.123  107.144 1.00 12.72 ? 609  ALA C CB  1 
ATOM   13976 N  N   . GLY C 1 618 ? 17.954  15.440  107.542 1.00 12.96 ? 610  GLY C N   1 
ATOM   13977 C  CA  . GLY C 1 618 ? 18.771  14.396  106.954 1.00 13.92 ? 610  GLY C CA  1 
ATOM   13978 C  C   . GLY C 1 618 ? 19.864  14.002  107.922 1.00 11.56 ? 610  GLY C C   1 
ATOM   13979 O  O   . GLY C 1 618 ? 19.867  14.424  109.079 1.00 12.22 ? 610  GLY C O   1 
ATOM   13980 N  N   . HIS C 1 619 ? 20.812  13.206  107.421 1.00 12.79 ? 611  HIS C N   1 
ATOM   13981 C  CA  . HIS C 1 619 ? 21.863  12.640  108.263 1.00 11.81 ? 611  HIS C CA  1 
ATOM   13982 C  C   . HIS C 1 619 ? 22.616  13.740  109.016 1.00 14.65 ? 611  HIS C C   1 
ATOM   13983 O  O   . HIS C 1 619 ? 22.812  14.849  108.506 1.00 18.31 ? 611  HIS C O   1 
ATOM   13984 C  CB  . HIS C 1 619 ? 22.836  11.824  107.397 1.00 11.48 ? 611  HIS C CB  1 
ATOM   13985 C  CG  . HIS C 1 619 ? 23.539  10.733  108.147 1.00 16.23 ? 611  HIS C CG  1 
ATOM   13986 N  ND1 . HIS C 1 619 ? 24.476  10.990  109.128 1.00 16.48 ? 611  HIS C ND1 1 
ATOM   13987 C  CD2 . HIS C 1 619 ? 23.407  9.387   108.096 1.00 16.89 ? 611  HIS C CD2 1 
ATOM   13988 C  CE1 . HIS C 1 619 ? 24.898  9.847   109.638 1.00 19.03 ? 611  HIS C CE1 1 
ATOM   13989 N  NE2 . HIS C 1 619 ? 24.268  8.860   109.028 1.00 16.43 ? 611  HIS C NE2 1 
ATOM   13990 N  N   . THR C 1 620 ? 23.051  13.426  110.244 1.00 14.58 ? 612  THR C N   1 
ATOM   13991 C  CA  . THR C 1 620 ? 23.682  14.419  111.109 1.00 16.76 ? 612  THR C CA  1 
ATOM   13992 C  C   . THR C 1 620 ? 25.199  14.455  111.018 1.00 18.70 ? 612  THR C C   1 
ATOM   13993 O  O   . THR C 1 620 ? 25.793  15.452  111.440 1.00 18.03 ? 612  THR C O   1 
ATOM   13994 C  CB  . THR C 1 620 ? 23.357  14.173  112.597 1.00 18.60 ? 612  THR C CB  1 
ATOM   13995 O  OG1 . THR C 1 620 ? 23.967  12.952  113.027 1.00 14.97 ? 612  THR C OG1 1 
ATOM   13996 C  CG2 . THR C 1 620 ? 21.860  14.102  112.857 1.00 18.44 ? 612  THR C CG2 1 
ATOM   13997 N  N   . ASN C 1 621 ? 25.850  13.407  110.501 1.00 17.15 ? 613  ASN C N   1 
ATOM   13998 C  CA  A ASN C 1 621 ? 27.263  13.290  110.823 0.51 18.21 ? 613  ASN C CA  1 
ATOM   13999 C  CA  B ASN C 1 621 ? 27.297  13.225  110.698 0.49 18.26 ? 613  ASN C CA  1 
ATOM   14000 C  C   . ASN C 1 621 ? 28.097  14.415  110.198 1.00 20.20 ? 613  ASN C C   1 
ATOM   14001 O  O   . ASN C 1 621 ? 29.081  14.841  110.823 1.00 19.38 ? 613  ASN C O   1 
ATOM   14002 C  CB  A ASN C 1 621 ? 27.758  11.884  110.468 0.51 20.76 ? 613  ASN C CB  1 
ATOM   14003 C  CB  B ASN C 1 621 ? 27.783  11.965  109.978 0.49 19.07 ? 613  ASN C CB  1 
ATOM   14004 C  CG  A ASN C 1 621 ? 27.379  10.839  111.552 0.51 23.13 ? 613  ASN C CG  1 
ATOM   14005 C  CG  B ASN C 1 621 ? 29.296  11.990  109.700 0.49 20.60 ? 613  ASN C CG  1 
ATOM   14006 O  OD1 A ASN C 1 621 ? 26.549  11.104  112.437 0.51 19.47 ? 613  ASN C OD1 1 
ATOM   14007 O  OD1 B ASN C 1 621 ? 29.750  12.495  108.668 0.49 25.01 ? 613  ASN C OD1 1 
ATOM   14008 N  ND2 A ASN C 1 621 ? 27.988  9.656   111.480 0.51 16.89 ? 613  ASN C ND2 1 
ATOM   14009 N  ND2 B ASN C 1 621 ? 30.072  11.436  110.618 0.49 18.12 ? 613  ASN C ND2 1 
ATOM   14010 N  N   . GLY C 1 622 ? 27.710  14.952  109.040 1.00 19.33 ? 614  GLY C N   1 
ATOM   14011 C  CA  . GLY C 1 622 ? 28.471  16.048  108.459 1.00 20.64 ? 614  GLY C CA  1 
ATOM   14012 C  C   . GLY C 1 622 ? 28.484  17.313  109.298 1.00 21.51 ? 614  GLY C C   1 
ATOM   14013 O  O   . GLY C 1 622 ? 29.429  18.103  109.201 1.00 25.23 ? 614  GLY C O   1 
ATOM   14014 N  N   . TRP C 1 623 ? 27.473  17.513  110.141 1.00 17.67 ? 615  TRP C N   1 
ATOM   14015 C  CA  . TRP C 1 623 ? 27.355  18.759  110.883 1.00 18.07 ? 615  TRP C CA  1 
ATOM   14016 C  C   . TRP C 1 623 ? 28.330  18.865  112.045 1.00 17.34 ? 615  TRP C C   1 
ATOM   14017 O  O   . TRP C 1 623 ? 28.492  19.958  112.598 1.00 17.84 ? 615  TRP C O   1 
ATOM   14018 C  CB  . TRP C 1 623 ? 25.905  18.932  111.382 1.00 17.97 ? 615  TRP C CB  1 
ATOM   14019 C  CG  . TRP C 1 623 ? 25.002  19.260  110.242 1.00 14.38 ? 615  TRP C CG  1 
ATOM   14020 C  CD1 . TRP C 1 623 ? 24.068  18.441  109.654 1.00 16.55 ? 615  TRP C CD1 1 
ATOM   14021 C  CD2 . TRP C 1 623 ? 24.993  20.480  109.499 1.00 14.44 ? 615  TRP C CD2 1 
ATOM   14022 N  NE1 . TRP C 1 623 ? 23.474  19.093  108.596 1.00 18.95 ? 615  TRP C NE1 1 
ATOM   14023 C  CE2 . TRP C 1 623 ? 24.014  20.351  108.491 1.00 18.63 ? 615  TRP C CE2 1 
ATOM   14024 C  CE3 . TRP C 1 623 ? 25.705  21.682  109.600 1.00 15.05 ? 615  TRP C CE3 1 
ATOM   14025 C  CZ2 . TRP C 1 623 ? 23.744  21.368  107.588 1.00 16.38 ? 615  TRP C CZ2 1 
ATOM   14026 C  CZ3 . TRP C 1 623 ? 25.430  22.692  108.703 1.00 20.68 ? 615  TRP C CZ3 1 
ATOM   14027 C  CH2 . TRP C 1 623 ? 24.455  22.535  107.720 1.00 16.29 ? 615  TRP C CH2 1 
ATOM   14028 N  N   . TYR C 1 624 ? 28.996  17.776  112.428 1.00 20.36 ? 616  TYR C N   1 
ATOM   14029 C  CA  . TYR C 1 624 ? 29.942  17.891  113.530 1.00 20.25 ? 616  TYR C CA  1 
ATOM   14030 C  C   . TYR C 1 624 ? 31.155  18.733  113.160 1.00 22.41 ? 616  TYR C C   1 
ATOM   14031 O  O   . TYR C 1 624 ? 31.818  19.272  114.057 1.00 21.82 ? 616  TYR C O   1 
ATOM   14032 C  CB  . TYR C 1 624 ? 30.344  16.498  114.010 1.00 21.46 ? 616  TYR C CB  1 
ATOM   14033 C  CG  . TYR C 1 624 ? 29.189  15.851  114.713 1.00 20.17 ? 616  TYR C CG  1 
ATOM   14034 C  CD1 . TYR C 1 624 ? 28.892  16.180  116.028 1.00 24.88 ? 616  TYR C CD1 1 
ATOM   14035 C  CD2 . TYR C 1 624 ? 28.354  14.963  114.052 1.00 25.62 ? 616  TYR C CD2 1 
ATOM   14036 C  CE1 . TYR C 1 624 ? 27.817  15.618  116.679 1.00 26.94 ? 616  TYR C CE1 1 
ATOM   14037 C  CE2 . TYR C 1 624 ? 27.266  14.394  114.697 1.00 29.83 ? 616  TYR C CE2 1 
ATOM   14038 C  CZ  . TYR C 1 624 ? 27.006  14.726  116.010 1.00 27.39 ? 616  TYR C CZ  1 
ATOM   14039 O  OH  . TYR C 1 624 ? 25.929  14.171  116.662 1.00 25.24 ? 616  TYR C OH  1 
ATOM   14040 N  N   . LYS C 1 625 ? 31.432  18.887  111.864 1.00 19.07 ? 617  LYS C N   1 
ATOM   14041 C  CA  . LYS C 1 625 ? 32.490  19.799  111.440 1.00 19.70 ? 617  LYS C CA  1 
ATOM   14042 C  C   . LYS C 1 625 ? 32.227  21.218  111.917 1.00 20.62 ? 617  LYS C C   1 
ATOM   14043 O  O   . LYS C 1 625 ? 33.171  21.982  112.146 1.00 22.13 ? 617  LYS C O   1 
ATOM   14044 C  CB  . LYS C 1 625 ? 32.625  19.779  109.917 1.00 22.34 ? 617  LYS C CB  1 
ATOM   14045 C  CG  . LYS C 1 625 ? 33.775  20.635  109.410 1.00 27.53 ? 617  LYS C CG  1 
ATOM   14046 C  CD  . LYS C 1 625 ? 33.974  20.491  107.918 1.00 31.93 ? 617  LYS C CD  1 
ATOM   14047 C  CE  . LYS C 1 625 ? 32.986  21.331  107.145 1.00 32.59 ? 617  LYS C CE  1 
ATOM   14048 N  NZ  . LYS C 1 625 ? 33.337  21.361  105.695 1.00 36.10 ? 617  LYS C NZ  1 
ATOM   14049 N  N   . TYR C 1 626 ? 30.960  21.598  112.062 1.00 18.16 ? 618  TYR C N   1 
ATOM   14050 C  CA  . TYR C 1 626 ? 30.611  22.911  112.588 1.00 18.67 ? 618  TYR C CA  1 
ATOM   14051 C  C   . TYR C 1 626 ? 30.304  22.878  114.084 1.00 25.16 ? 618  TYR C C   1 
ATOM   14052 O  O   . TYR C 1 626 ? 30.823  23.709  114.832 1.00 27.95 ? 618  TYR C O   1 
ATOM   14053 C  CB  . TYR C 1 626 ? 29.418  23.492  111.813 1.00 17.96 ? 618  TYR C CB  1 
ATOM   14054 C  CG  . TYR C 1 626 ? 29.654  23.587  110.315 1.00 22.88 ? 618  TYR C CG  1 
ATOM   14055 C  CD1 . TYR C 1 626 ? 30.424  24.610  109.771 1.00 25.84 ? 618  TYR C CD1 1 
ATOM   14056 C  CD2 . TYR C 1 626 ? 29.114  22.648  109.448 1.00 30.38 ? 618  TYR C CD2 1 
ATOM   14057 C  CE1 . TYR C 1 626 ? 30.642  24.695  108.396 1.00 22.97 ? 618  TYR C CE1 1 
ATOM   14058 C  CE2 . TYR C 1 626 ? 29.325  22.723  108.079 1.00 32.93 ? 618  TYR C CE2 1 
ATOM   14059 C  CZ  . TYR C 1 626 ? 30.084  23.745  107.561 1.00 29.96 ? 618  TYR C CZ  1 
ATOM   14060 O  OH  . TYR C 1 626 ? 30.291  23.806  106.198 1.00 35.91 ? 618  TYR C OH  1 
ATOM   14061 N  N   . VAL C 1 627 ? 29.487  21.923  114.545 1.00 21.19 ? 619  VAL C N   1 
ATOM   14062 C  CA  . VAL C 1 627 ? 29.003  21.977  115.921 1.00 19.98 ? 619  VAL C CA  1 
ATOM   14063 C  C   . VAL C 1 627 ? 29.972  21.346  116.916 1.00 24.72 ? 619  VAL C C   1 
ATOM   14064 O  O   . VAL C 1 627 ? 29.907  21.663  118.112 1.00 21.91 ? 619  VAL C O   1 
ATOM   14065 C  CB  . VAL C 1 627 ? 27.609  21.329  116.067 1.00 19.40 ? 619  VAL C CB  1 
ATOM   14066 C  CG1 . VAL C 1 627 ? 26.622  21.928  115.037 1.00 18.51 ? 619  VAL C CG1 1 
ATOM   14067 C  CG2 . VAL C 1 627 ? 27.679  19.800  115.923 1.00 18.96 ? 619  VAL C CG2 1 
ATOM   14068 N  N   . GLY C 1 628 ? 30.869  20.479  116.465 1.00 25.41 ? 620  GLY C N   1 
ATOM   14069 C  CA  . GLY C 1 628 ? 31.802  19.874  117.397 1.00 23.52 ? 620  GLY C CA  1 
ATOM   14070 C  C   . GLY C 1 628 ? 31.150  18.878  118.350 1.00 26.91 ? 620  GLY C C   1 
ATOM   14071 O  O   . GLY C 1 628 ? 29.996  18.462  118.199 1.00 25.37 ? 620  GLY C O   1 
ATOM   14072 N  N   . LEU C 1 629 ? 31.929  18.504  119.366 1.00 24.99 ? 621  LEU C N   1 
ATOM   14073 C  CA  . LEU C 1 629 ? 31.480  17.477  120.295 1.00 29.02 ? 621  LEU C CA  1 
ATOM   14074 C  C   . LEU C 1 629 ? 30.478  18.008  121.307 1.00 30.43 ? 621  LEU C C   1 
ATOM   14075 O  O   . LEU C 1 629 ? 29.687  17.227  121.845 1.00 32.70 ? 621  LEU C O   1 
ATOM   14076 C  CB  . LEU C 1 629 ? 32.680  16.864  121.019 1.00 33.52 ? 621  LEU C CB  1 
ATOM   14077 C  CG  . LEU C 1 629 ? 33.767  16.220  120.150 1.00 31.46 ? 621  LEU C CG  1 
ATOM   14078 C  CD1 . LEU C 1 629 ? 34.891  15.702  121.028 1.00 36.18 ? 621  LEU C CD1 1 
ATOM   14079 C  CD2 . LEU C 1 629 ? 33.193  15.103  119.279 1.00 30.07 ? 621  LEU C CD2 1 
ATOM   14080 N  N   . ASN C 1 630 ? 30.476  19.314  121.552 1.00 31.12 ? 622  ASN C N   1 
ATOM   14081 C  CA  . ASN C 1 630 ? 29.590  19.932  122.527 1.00 34.22 ? 622  ASN C CA  1 
ATOM   14082 C  C   . ASN C 1 630 ? 28.433  20.688  121.886 1.00 37.59 ? 622  ASN C C   1 
ATOM   14083 O  O   . ASN C 1 630 ? 27.657  21.326  122.604 1.00 34.68 ? 622  ASN C O   1 
ATOM   14084 C  CB  . ASN C 1 630 ? 30.394  20.866  123.433 1.00 35.61 ? 622  ASN C CB  1 
ATOM   14085 C  CG  . ASN C 1 630 ? 31.486  20.132  124.187 1.00 42.91 ? 622  ASN C CG  1 
ATOM   14086 O  OD1 . ASN C 1 630 ? 31.251  19.052  124.730 1.00 39.92 ? 622  ASN C OD1 1 
ATOM   14087 N  ND2 . ASN C 1 630 ? 32.690  20.700  124.204 1.00 43.64 ? 622  ASN C ND2 1 
ATOM   14088 N  N   . GLY C 1 631 ? 28.298  20.636  120.564 1.00 31.82 ? 623  GLY C N   1 
ATOM   14089 C  CA  . GLY C 1 631 ? 27.117  21.125  119.885 1.00 27.36 ? 623  GLY C CA  1 
ATOM   14090 C  C   . GLY C 1 631 ? 26.052  20.048  119.829 1.00 29.43 ? 623  GLY C C   1 
ATOM   14091 O  O   . GLY C 1 631 ? 26.100  19.051  120.552 1.00 29.40 ? 623  GLY C O   1 
ATOM   14092 N  N   . ALA C 1 632 ? 25.079  20.251  118.947 1.00 24.11 ? 624  ALA C N   1 
ATOM   14093 C  CA  . ALA C 1 632 ? 24.030  19.260  118.765 1.00 24.49 ? 624  ALA C CA  1 
ATOM   14094 C  C   . ALA C 1 632 ? 23.442  19.405  117.368 1.00 20.92 ? 624  ALA C C   1 
ATOM   14095 O  O   . ALA C 1 632 ? 23.629  20.422  116.693 1.00 24.35 ? 624  ALA C O   1 
ATOM   14096 C  CB  . ALA C 1 632 ? 22.938  19.389  119.830 1.00 25.09 ? 624  ALA C CB  1 
ATOM   14097 N  N   . VAL C 1 633 ? 22.759  18.351  116.930 1.00 18.19 ? 625  VAL C N   1 
ATOM   14098 C  CA  . VAL C 1 633 ? 22.143  18.311  115.609 1.00 17.13 ? 625  VAL C CA  1 
ATOM   14099 C  C   . VAL C 1 633 ? 20.741  17.741  115.750 1.00 21.28 ? 625  VAL C C   1 
ATOM   14100 O  O   . VAL C 1 633 ? 20.542  16.729  116.432 1.00 20.97 ? 625  VAL C O   1 
ATOM   14101 C  CB  . VAL C 1 633 ? 22.957  17.463  114.606 1.00 19.53 ? 625  VAL C CB  1 
ATOM   14102 C  CG1 . VAL C 1 633 ? 22.392  17.624  113.206 1.00 15.38 ? 625  VAL C CG1 1 
ATOM   14103 C  CG2 . VAL C 1 633 ? 24.463  17.835  114.644 1.00 22.96 ? 625  VAL C CG2 1 
ATOM   14104 N  N   . VAL C 1 634 ? 19.776  18.389  115.115 1.00 20.14 ? 626  VAL C N   1 
ATOM   14105 C  CA  . VAL C 1 634 ? 18.437  17.851  114.936 1.00 17.72 ? 626  VAL C CA  1 
ATOM   14106 C  C   . VAL C 1 634 ? 18.392  17.311  113.514 1.00 17.87 ? 626  VAL C C   1 
ATOM   14107 O  O   . VAL C 1 634 ? 18.356  18.080  112.550 1.00 16.45 ? 626  VAL C O   1 
ATOM   14108 C  CB  . VAL C 1 634 ? 17.354  18.915  115.173 1.00 16.81 ? 626  VAL C CB  1 
ATOM   14109 C  CG1 . VAL C 1 634 ? 15.964  18.333  114.936 1.00 16.66 ? 626  VAL C CG1 1 
ATOM   14110 C  CG2 . VAL C 1 634 ? 17.461  19.500  116.590 1.00 20.16 ? 626  VAL C CG2 1 
ATOM   14111 N  N   . GLY C 1 635 ? 18.428  15.992  113.378 1.00 14.99 ? 627  GLY C N   1 
ATOM   14112 C  CA  . GLY C 1 635 ? 18.443  15.376  112.063 1.00 14.06 ? 627  GLY C CA  1 
ATOM   14113 C  C   . GLY C 1 635 ? 17.769  14.025  112.070 1.00 14.61 ? 627  GLY C C   1 
ATOM   14114 O  O   . GLY C 1 635 ? 16.954  13.731  112.953 1.00 14.50 ? 627  GLY C O   1 
ATOM   14115 N  N   . ILE C 1 636 ? 18.098  13.187  111.090 1.00 13.81 ? 628  ILE C N   1 
ATOM   14116 C  CA  . ILE C 1 636 ? 17.560  11.833  111.031 1.00 13.68 ? 628  ILE C CA  1 
ATOM   14117 C  C   . ILE C 1 636 ? 18.617  10.940  110.401 1.00 15.17 ? 628  ILE C C   1 
ATOM   14118 O  O   . ILE C 1 636 ? 19.125  11.237  109.316 1.00 14.24 ? 628  ILE C O   1 
ATOM   14119 C  CB  . ILE C 1 636 ? 16.218  11.778  110.263 1.00 13.96 ? 628  ILE C CB  1 
ATOM   14120 C  CG1 . ILE C 1 636 ? 15.741  10.328  110.098 1.00 14.72 ? 628  ILE C CG1 1 
ATOM   14121 C  CG2 . ILE C 1 636 ? 16.314  12.484  108.912 1.00 17.06 ? 628  ILE C CG2 1 
ATOM   14122 C  CD1 . ILE C 1 636 ? 14.304  10.216  109.548 1.00 17.66 ? 628  ILE C CD1 1 
ATOM   14123 N  N   . ASN C 1 637 ? 18.971  9.861   111.098 1.00 14.21 ? 629  ASN C N   1 
ATOM   14124 C  CA  . ASN C 1 637 ? 20.020  8.960   110.641 1.00 12.85 ? 629  ASN C CA  1 
ATOM   14125 C  C   . ASN C 1 637 ? 19.500  7.578   110.277 1.00 16.28 ? 629  ASN C C   1 
ATOM   14126 O  O   . ASN C 1 637 ? 20.306  6.686   109.994 1.00 18.79 ? 629  ASN C O   1 
ATOM   14127 C  CB  . ASN C 1 637 ? 21.120  8.837   111.695 1.00 13.57 ? 629  ASN C CB  1 
ATOM   14128 C  CG  . ASN C 1 637 ? 21.881  10.122  111.884 1.00 21.07 ? 629  ASN C CG  1 
ATOM   14129 O  OD1 . ASN C 1 637 ? 21.721  11.057  111.106 1.00 14.07 ? 629  ASN C OD1 1 
ATOM   14130 N  ND2 . ASN C 1 637 ? 22.724  10.178  112.925 1.00 22.43 ? 629  ASN C ND2 1 
ATOM   14131 N  N   . ARG C 1 638 ? 18.188  7.377   110.261 1.00 12.92 ? 630  ARG C N   1 
ATOM   14132 C  CA  . ARG C 1 638 ? 17.596  6.100   109.893 1.00 12.99 ? 630  ARG C CA  1 
ATOM   14133 C  C   . ARG C 1 638 ? 16.804  6.260   108.599 1.00 14.70 ? 630  ARG C C   1 
ATOM   14134 O  O   . ARG C 1 638 ? 16.610  7.373   108.098 1.00 13.78 ? 630  ARG C O   1 
ATOM   14135 C  CB  . ARG C 1 638 ? 16.701  5.566   111.021 1.00 13.77 ? 630  ARG C CB  1 
ATOM   14136 C  CG  . ARG C 1 638 ? 15.722  6.596   111.568 1.00 14.79 ? 630  ARG C CG  1 
ATOM   14137 C  CD  . ARG C 1 638 ? 14.462  5.927   112.091 1.00 20.43 ? 630  ARG C CD  1 
ATOM   14138 N  NE  . ARG C 1 638 ? 13.672  5.419   110.971 1.00 18.22 ? 630  ARG C NE  1 
ATOM   14139 C  CZ  . ARG C 1 638 ? 12.524  4.757   111.093 1.00 22.28 ? 630  ARG C CZ  1 
ATOM   14140 N  NH1 . ARG C 1 638 ? 12.016  4.503   112.301 1.00 18.29 ? 630  ARG C NH1 1 
ATOM   14141 N  NH2 . ARG C 1 638 ? 11.894  4.337   110.004 1.00 14.76 ? 630  ARG C NH2 1 
ATOM   14142 N  N   . PHE C 1 639 ? 16.370  5.137   108.032 1.00 11.65 ? 631  PHE C N   1 
ATOM   14143 C  CA  . PHE C 1 639 ? 15.544  5.222   106.833 1.00 11.42 ? 631  PHE C CA  1 
ATOM   14144 C  C   . PHE C 1 639 ? 14.186  5.849   107.164 1.00 12.87 ? 631  PHE C C   1 
ATOM   14145 O  O   . PHE C 1 639 ? 13.747  5.870   108.315 1.00 12.08 ? 631  PHE C O   1 
ATOM   14146 C  CB  . PHE C 1 639 ? 15.361  3.838   106.201 1.00 16.53 ? 631  PHE C CB  1 
ATOM   14147 C  CG  . PHE C 1 639 ? 16.637  3.263   105.647 1.00 15.89 ? 631  PHE C CG  1 
ATOM   14148 C  CD1 . PHE C 1 639 ? 17.216  3.810   104.508 1.00 17.58 ? 631  PHE C CD1 1 
ATOM   14149 C  CD2 . PHE C 1 639 ? 17.262  2.199   106.270 1.00 13.00 ? 631  PHE C CD2 1 
ATOM   14150 C  CE1 . PHE C 1 639 ? 18.407  3.289   103.998 1.00 12.87 ? 631  PHE C CE1 1 
ATOM   14151 C  CE2 . PHE C 1 639 ? 18.449  1.678   105.770 1.00 11.68 ? 631  PHE C CE2 1 
ATOM   14152 C  CZ  . PHE C 1 639 ? 19.012  2.228   104.629 1.00 10.97 ? 631  PHE C CZ  1 
ATOM   14153 N  N   . GLY C 1 640 ? 13.529  6.378   106.134 1.00 11.02 ? 632  GLY C N   1 
ATOM   14154 C  CA  . GLY C 1 640 ? 12.228  7.007   106.298 1.00 12.12 ? 632  GLY C CA  1 
ATOM   14155 C  C   . GLY C 1 640 ? 11.058  6.047   106.504 1.00 13.14 ? 632  GLY C C   1 
ATOM   14156 O  O   . GLY C 1 640 ? 11.244  4.889   106.895 1.00 12.02 ? 632  GLY C O   1 
ATOM   14157 N  N   . GLU C 1 641 ? 9.844   6.531   106.250 1.00 13.60 ? 633  GLU C N   1 
ATOM   14158 C  CA  . GLU C 1 641 ? 8.616   5.762   106.423 1.00 13.41 ? 633  GLU C CA  1 
ATOM   14159 C  C   . GLU C 1 641 ? 7.589   6.233   105.409 1.00 12.53 ? 633  GLU C C   1 
ATOM   14160 O  O   . GLU C 1 641 ? 7.499   7.427   105.129 1.00 12.75 ? 633  GLU C O   1 
ATOM   14161 C  CB  . GLU C 1 641 ? 8.008   5.945   107.819 1.00 14.82 ? 633  GLU C CB  1 
ATOM   14162 C  CG  . GLU C 1 641 ? 8.765   5.296   108.956 1.00 20.13 ? 633  GLU C CG  1 
ATOM   14163 C  CD  . GLU C 1 641 ? 8.661   3.792   108.943 1.00 20.57 ? 633  GLU C CD  1 
ATOM   14164 O  OE1 . GLU C 1 641 ? 7.839   3.246   108.166 1.00 22.50 ? 633  GLU C OE1 1 
ATOM   14165 O  OE2 . GLU C 1 641 ? 9.403   3.161   109.721 1.00 20.94 ? 633  GLU C OE2 1 
ATOM   14166 N  N   . SER C 1 642 ? 6.788   5.299   104.905 1.00 12.72 ? 634  SER C N   1 
ATOM   14167 C  CA  . SER C 1 642 ? 5.656   5.640   104.047 1.00 17.41 ? 634  SER C CA  1 
ATOM   14168 C  C   . SER C 1 642 ? 4.530   6.209   104.910 1.00 16.40 ? 634  SER C C   1 
ATOM   14169 O  O   . SER C 1 642 ? 3.940   5.488   105.720 1.00 20.12 ? 634  SER C O   1 
ATOM   14170 C  CB  . SER C 1 642 ? 5.191   4.403   103.281 1.00 14.06 ? 634  SER C CB  1 
ATOM   14171 O  OG  . SER C 1 642 ? 4.102   4.739   102.440 1.00 15.52 ? 634  SER C OG  1 
ATOM   14172 N  N   . ALA C 1 643 ? 4.227   7.513   104.736 1.00 14.90 ? 635  ALA C N   1 
ATOM   14173 C  CA  . ALA C 1 643 ? 3.262   8.257   105.550 1.00 17.29 ? 635  ALA C CA  1 
ATOM   14174 C  C   . ALA C 1 643 ? 3.092   9.679   105.021 1.00 16.26 ? 635  ALA C C   1 
ATOM   14175 O  O   . ALA C 1 643 ? 3.947   10.153  104.267 1.00 19.04 ? 635  ALA C O   1 
ATOM   14176 C  CB  . ALA C 1 643 ? 3.710   8.300   107.017 1.00 15.50 ? 635  ALA C CB  1 
ATOM   14177 N  N   . PRO C 1 644 ? 2.017   10.394  105.378 1.00 19.60 ? 636  PRO C N   1 
ATOM   14178 C  CA  . PRO C 1 644 ? 1.919   11.807  104.977 1.00 18.21 ? 636  PRO C CA  1 
ATOM   14179 C  C   . PRO C 1 644 ? 3.046   12.654  105.570 1.00 19.88 ? 636  PRO C C   1 
ATOM   14180 O  O   . PRO C 1 644 ? 3.520   12.416  106.683 1.00 18.31 ? 636  PRO C O   1 
ATOM   14181 C  CB  . PRO C 1 644 ? 0.547   12.238  105.513 1.00 26.05 ? 636  PRO C CB  1 
ATOM   14182 C  CG  . PRO C 1 644 ? -0.247  10.951  105.621 1.00 24.77 ? 636  PRO C CG  1 
ATOM   14183 C  CD  . PRO C 1 644 ? 0.780   9.913   106.023 1.00 23.41 ? 636  PRO C CD  1 
ATOM   14184 N  N   . ALA C 1 645 ? 3.458   13.669  104.801 1.00 15.11 ? 637  ALA C N   1 
ATOM   14185 C  CA  . ALA C 1 645 ? 4.639   14.471  105.129 1.00 20.38 ? 637  ALA C CA  1 
ATOM   14186 C  C   . ALA C 1 645 ? 4.498   15.191  106.470 1.00 25.14 ? 637  ALA C C   1 
ATOM   14187 O  O   . ALA C 1 645 ? 5.435   15.211  107.275 1.00 22.85 ? 637  ALA C O   1 
ATOM   14188 C  CB  . ALA C 1 645 ? 4.897   15.487  104.013 1.00 25.33 ? 637  ALA C CB  1 
ATOM   14189 N  N   . ASP C 1 646 ? 3.353   15.827  106.714 1.00 25.24 ? 638  ASP C N   1 
ATOM   14190 C  CA  . ASP C 1 646 ? 3.172   16.523  107.988 1.00 32.14 ? 638  ASP C CA  1 
ATOM   14191 C  C   . ASP C 1 646 ? 3.420   15.588  109.165 1.00 32.76 ? 638  ASP C C   1 
ATOM   14192 O  O   . ASP C 1 646 ? 4.083   15.959  110.144 1.00 27.78 ? 638  ASP C O   1 
ATOM   14193 C  CB  . ASP C 1 646 ? 1.763   17.112  108.078 1.00 36.18 ? 638  ASP C CB  1 
ATOM   14194 C  CG  . ASP C 1 646 ? 1.600   18.362  107.244 1.00 48.93 ? 638  ASP C CG  1 
ATOM   14195 O  OD1 . ASP C 1 646 ? 2.564   18.737  106.539 1.00 47.20 ? 638  ASP C OD1 1 
ATOM   14196 O  OD2 . ASP C 1 646 ? 0.506   18.970  107.298 1.00 57.15 ? 638  ASP C OD2 1 
ATOM   14197 N  N   . LEU C 1 647 ? 2.907   14.361  109.071 1.00 18.10 ? 639  LEU C N   1 
ATOM   14198 C  CA  . LEU C 1 647 ? 3.070   13.391  110.143 1.00 21.88 ? 639  LEU C CA  1 
ATOM   14199 C  C   . LEU C 1 647 ? 4.525   12.954  110.297 1.00 21.62 ? 639  LEU C C   1 
ATOM   14200 O  O   . LEU C 1 647 ? 4.971   12.688  111.417 1.00 20.15 ? 639  LEU C O   1 
ATOM   14201 C  CB  . LEU C 1 647 ? 2.154   12.196  109.871 1.00 20.69 ? 639  LEU C CB  1 
ATOM   14202 C  CG  . LEU C 1 647 ? 1.901   11.192  110.988 1.00 30.33 ? 639  LEU C CG  1 
ATOM   14203 C  CD1 . LEU C 1 647 ? 0.564   10.510  110.767 1.00 35.76 ? 639  LEU C CD1 1 
ATOM   14204 C  CD2 . LEU C 1 647 ? 3.005   10.166  110.997 1.00 37.69 ? 639  LEU C CD2 1 
ATOM   14205 N  N   . LEU C 1 648 ? 5.280   12.889  109.198 1.00 18.97 ? 640  LEU C N   1 
ATOM   14206 C  CA  . LEU C 1 648 ? 6.664   12.420  109.274 1.00 16.65 ? 640  LEU C CA  1 
ATOM   14207 C  C   . LEU C 1 648 ? 7.569   13.427  109.970 1.00 21.94 ? 640  LEU C C   1 
ATOM   14208 O  O   . LEU C 1 648 ? 8.431   13.045  110.775 1.00 19.53 ? 640  LEU C O   1 
ATOM   14209 C  CB  . LEU C 1 648 ? 7.197   12.107  107.878 1.00 18.61 ? 640  LEU C CB  1 
ATOM   14210 C  CG  . LEU C 1 648 ? 6.518   10.905  107.217 1.00 21.10 ? 640  LEU C CG  1 
ATOM   14211 C  CD1 . LEU C 1 648 ? 6.862   10.804  105.734 1.00 17.90 ? 640  LEU C CD1 1 
ATOM   14212 C  CD2 . LEU C 1 648 ? 6.889   9.620   107.955 1.00 21.80 ? 640  LEU C CD2 1 
ATOM   14213 N  N   . PHE C 1 649 ? 7.404   14.714  109.667 1.00 17.13 ? 641  PHE C N   1 
ATOM   14214 C  CA  . PHE C 1 649 ? 8.181   15.728  110.366 1.00 20.17 ? 641  PHE C CA  1 
ATOM   14215 C  C   . PHE C 1 649 ? 7.908   15.684  111.863 1.00 20.00 ? 641  PHE C C   1 
ATOM   14216 O  O   . PHE C 1 649 ? 8.832   15.795  112.675 1.00 18.26 ? 641  PHE C O   1 
ATOM   14217 C  CB  . PHE C 1 649 ? 7.875   17.109  109.792 1.00 16.74 ? 641  PHE C CB  1 
ATOM   14218 C  CG  . PHE C 1 649 ? 8.568   17.377  108.484 1.00 17.45 ? 641  PHE C CG  1 
ATOM   14219 C  CD1 . PHE C 1 649 ? 9.946   17.222  108.370 1.00 16.44 ? 641  PHE C CD1 1 
ATOM   14220 C  CD2 . PHE C 1 649 ? 7.844   17.763  107.363 1.00 20.39 ? 641  PHE C CD2 1 
ATOM   14221 C  CE1 . PHE C 1 649 ? 10.592  17.452  107.165 1.00 21.60 ? 641  PHE C CE1 1 
ATOM   14222 C  CE2 . PHE C 1 649 ? 8.490   17.997  106.148 1.00 19.68 ? 641  PHE C CE2 1 
ATOM   14223 C  CZ  . PHE C 1 649 ? 9.862   17.847  106.055 1.00 20.09 ? 641  PHE C CZ  1 
ATOM   14224 N  N   . LYS C 1 650 ? 6.650   15.486  112.245 1.00 18.45 ? 642  LYS C N   1 
ATOM   14225 C  CA  . LYS C 1 650 ? 6.330   15.382  113.666 1.00 28.72 ? 642  LYS C CA  1 
ATOM   14226 C  C   . LYS C 1 650 ? 6.929   14.115  114.267 1.00 22.85 ? 642  LYS C C   1 
ATOM   14227 O  O   . LYS C 1 650 ? 7.573   14.160  115.322 1.00 24.42 ? 642  LYS C O   1 
ATOM   14228 C  CB  . LYS C 1 650 ? 4.812   15.418  113.865 1.00 31.94 ? 642  LYS C CB  1 
ATOM   14229 N  N   . ALA C 1 651 ? 6.745   12.979  113.591 1.00 19.13 ? 643  ALA C N   1 
ATOM   14230 C  CA  . ALA C 1 651 ? 7.144   11.695  114.157 1.00 20.21 ? 643  ALA C CA  1 
ATOM   14231 C  C   . ALA C 1 651 ? 8.650   11.600  114.362 1.00 20.27 ? 643  ALA C C   1 
ATOM   14232 O  O   . ALA C 1 651 ? 9.104   10.893  115.269 1.00 17.88 ? 643  ALA C O   1 
ATOM   14233 C  CB  . ALA C 1 651 ? 6.655   10.555  113.265 1.00 25.36 ? 643  ALA C CB  1 
ATOM   14234 N  N   . PHE C 1 652 ? 9.438   12.301  113.547 1.00 16.47 ? 644  PHE C N   1 
ATOM   14235 C  CA  . PHE C 1 652 ? 10.891  12.240  113.628 1.00 18.22 ? 644  PHE C CA  1 
ATOM   14236 C  C   . PHE C 1 652 ? 11.499  13.447  114.339 1.00 20.87 ? 644  PHE C C   1 
ATOM   14237 O  O   . PHE C 1 652 ? 12.715  13.656  114.266 1.00 20.58 ? 644  PHE C O   1 
ATOM   14238 C  CB  . PHE C 1 652 ? 11.483  12.075  112.226 1.00 16.09 ? 644  PHE C CB  1 
ATOM   14239 C  CG  . PHE C 1 652 ? 11.247  10.711  111.629 1.00 18.55 ? 644  PHE C CG  1 
ATOM   14240 C  CD1 . PHE C 1 652 ? 11.768  9.578   112.232 1.00 23.54 ? 644  PHE C CD1 1 
ATOM   14241 C  CD2 . PHE C 1 652 ? 10.510  10.562  110.470 1.00 19.35 ? 644  PHE C CD2 1 
ATOM   14242 C  CE1 . PHE C 1 652 ? 11.560  8.321   111.682 1.00 26.79 ? 644  PHE C CE1 1 
ATOM   14243 C  CE2 . PHE C 1 652 ? 10.306  9.308   109.918 1.00 24.23 ? 644  PHE C CE2 1 
ATOM   14244 C  CZ  . PHE C 1 652 ? 10.832  8.190   110.523 1.00 21.69 ? 644  PHE C CZ  1 
ATOM   14245 N  N   . GLY C 1 653 ? 10.686  14.238  115.033 1.00 22.10 ? 645  GLY C N   1 
ATOM   14246 C  CA  . GLY C 1 653 ? 11.221  15.264  115.900 1.00 23.45 ? 645  GLY C CA  1 
ATOM   14247 C  C   . GLY C 1 653 ? 11.605  16.567  115.242 1.00 21.79 ? 645  GLY C C   1 
ATOM   14248 O  O   . GLY C 1 653 ? 12.374  17.332  115.832 1.00 23.74 ? 645  GLY C O   1 
ATOM   14249 N  N   . PHE C 1 654 ? 11.100  16.856  114.041 1.00 22.06 ? 646  PHE C N   1 
ATOM   14250 C  CA  . PHE C 1 654 ? 11.305  18.171  113.430 1.00 16.62 ? 646  PHE C CA  1 
ATOM   14251 C  C   . PHE C 1 654 ? 10.150  19.081  113.843 1.00 17.69 ? 646  PHE C C   1 
ATOM   14252 O  O   . PHE C 1 654 ? 9.274   19.456  113.060 1.00 20.87 ? 646  PHE C O   1 
ATOM   14253 C  CB  . PHE C 1 654 ? 11.458  18.040  111.919 1.00 15.55 ? 646  PHE C CB  1 
ATOM   14254 C  CG  . PHE C 1 654 ? 12.665  17.235  111.524 1.00 18.26 ? 646  PHE C CG  1 
ATOM   14255 C  CD1 . PHE C 1 654 ? 13.923  17.808  111.536 1.00 18.17 ? 646  PHE C CD1 1 
ATOM   14256 C  CD2 . PHE C 1 654 ? 12.544  15.887  111.203 1.00 14.41 ? 646  PHE C CD2 1 
ATOM   14257 C  CE1 . PHE C 1 654 ? 15.041  17.068  111.203 1.00 15.07 ? 646  PHE C CE1 1 
ATOM   14258 C  CE2 . PHE C 1 654 ? 13.657  15.138  110.875 1.00 13.84 ? 646  PHE C CE2 1 
ATOM   14259 C  CZ  . PHE C 1 654 ? 14.911  15.729  110.879 1.00 14.92 ? 646  PHE C CZ  1 
ATOM   14260 N  N   . THR C 1 655 ? 10.167  19.410  115.135 1.00 21.07 ? 647  THR C N   1 
ATOM   14261 C  CA  . THR C 1 655 ? 9.151   20.223  115.783 1.00 22.04 ? 647  THR C CA  1 
ATOM   14262 C  C   . THR C 1 655 ? 9.825   21.373  116.520 1.00 23.60 ? 647  THR C C   1 
ATOM   14263 O  O   . THR C 1 655 ? 11.005  21.308  116.875 1.00 22.78 ? 647  THR C O   1 
ATOM   14264 C  CB  . THR C 1 655 ? 8.334   19.416  116.795 1.00 25.95 ? 647  THR C CB  1 
ATOM   14265 O  OG1 . THR C 1 655 ? 9.189   19.044  117.878 1.00 25.20 ? 647  THR C OG1 1 
ATOM   14266 C  CG2 . THR C 1 655 ? 7.769   18.159  116.159 1.00 22.13 ? 647  THR C CG2 1 
ATOM   14267 N  N   . VAL C 1 656 ? 9.046   22.427  116.763 1.00 24.92 ? 648  VAL C N   1 
ATOM   14268 C  CA  . VAL C 1 656 ? 9.565   23.573  117.503 1.00 29.15 ? 648  VAL C CA  1 
ATOM   14269 C  C   . VAL C 1 656 ? 10.038  23.135  118.883 1.00 30.49 ? 648  VAL C C   1 
ATOM   14270 O  O   . VAL C 1 656 ? 11.143  23.476  119.318 1.00 23.09 ? 648  VAL C O   1 
ATOM   14271 C  CB  . VAL C 1 656 ? 8.495   24.677  117.595 1.00 34.10 ? 648  VAL C CB  1 
ATOM   14272 C  CG1 . VAL C 1 656 ? 8.948   25.772  118.543 1.00 37.76 ? 648  VAL C CG1 1 
ATOM   14273 C  CG2 . VAL C 1 656 ? 8.191   25.240  116.212 1.00 31.24 ? 648  VAL C CG2 1 
ATOM   14274 N  N   . ASP C 1 657 ? 9.212   22.341  119.576 1.00 27.31 ? 649  ASP C N   1 
ATOM   14275 C  CA  . ASP C 1 657 ? 9.545   21.899  120.927 1.00 30.72 ? 649  ASP C CA  1 
ATOM   14276 C  C   . ASP C 1 657 ? 10.879  21.165  120.971 1.00 30.58 ? 649  ASP C C   1 
ATOM   14277 O  O   . ASP C 1 657 ? 11.658  21.329  121.919 1.00 23.98 ? 649  ASP C O   1 
ATOM   14278 C  CB  . ASP C 1 657 ? 8.436   20.998  121.473 1.00 36.16 ? 649  ASP C CB  1 
ATOM   14279 C  CG  . ASP C 1 657 ? 7.233   21.781  121.957 1.00 51.28 ? 649  ASP C CG  1 
ATOM   14280 O  OD1 . ASP C 1 657 ? 7.343   23.018  122.091 1.00 55.72 ? 649  ASP C OD1 1 
ATOM   14281 O  OD2 . ASP C 1 657 ? 6.177   21.158  122.203 1.00 58.25 ? 649  ASP C OD2 1 
ATOM   14282 N  N   . ASN C 1 658 ? 11.155  20.335  119.965 1.00 22.30 ? 650  ASN C N   1 
ATOM   14283 C  CA  . ASN C 1 658 ? 12.394  19.568  119.993 1.00 26.30 ? 650  ASN C CA  1 
ATOM   14284 C  C   . ASN C 1 658 ? 13.614  20.437  119.683 1.00 21.25 ? 650  ASN C C   1 
ATOM   14285 O  O   . ASN C 1 658 ? 14.683  20.237  120.271 1.00 27.56 ? 650  ASN C O   1 
ATOM   14286 C  CB  . ASN C 1 658 ? 12.313  18.388  119.027 1.00 26.28 ? 650  ASN C CB  1 
ATOM   14287 C  CG  . ASN C 1 658 ? 13.465  17.437  119.206 1.00 26.50 ? 650  ASN C CG  1 
ATOM   14288 O  OD1 . ASN C 1 658 ? 13.875  17.167  120.332 1.00 26.85 ? 650  ASN C OD1 1 
ATOM   14289 N  ND2 . ASN C 1 658 ? 14.018  16.949  118.104 1.00 22.95 ? 650  ASN C ND2 1 
ATOM   14290 N  N   . VAL C 1 659 ? 13.489  21.397  118.763 1.00 24.55 ? 651  VAL C N   1 
ATOM   14291 C  CA  . VAL C 1 659 ? 14.617  22.297  118.512 1.00 26.00 ? 651  VAL C CA  1 
ATOM   14292 C  C   . VAL C 1 659 ? 14.916  23.132  119.754 1.00 25.82 ? 651  VAL C C   1 
ATOM   14293 O  O   . VAL C 1 659 ? 16.081  23.315  120.131 1.00 25.13 ? 651  VAL C O   1 
ATOM   14294 C  CB  . VAL C 1 659 ? 14.351  23.183  117.280 1.00 23.30 ? 651  VAL C CB  1 
ATOM   14295 C  CG1 . VAL C 1 659 ? 15.491  24.190  117.077 1.00 21.32 ? 651  VAL C CG1 1 
ATOM   14296 C  CG2 . VAL C 1 659 ? 14.188  22.322  116.036 1.00 21.46 ? 651  VAL C CG2 1 
ATOM   14297 N  N   . VAL C 1 660 ? 13.870  23.643  120.413 1.00 23.86 ? 652  VAL C N   1 
ATOM   14298 C  CA  . VAL C 1 660 ? 14.059  24.440  121.624 1.00 25.43 ? 652  VAL C CA  1 
ATOM   14299 C  C   . VAL C 1 660 ? 14.795  23.627  122.683 1.00 26.80 ? 652  VAL C C   1 
ATOM   14300 O  O   . VAL C 1 660 ? 15.787  24.083  123.267 1.00 25.22 ? 652  VAL C O   1 
ATOM   14301 C  CB  . VAL C 1 660 ? 12.700  24.955  122.140 1.00 29.46 ? 652  VAL C CB  1 
ATOM   14302 C  CG1 . VAL C 1 660 ? 12.818  25.498  123.562 1.00 31.36 ? 652  VAL C CG1 1 
ATOM   14303 C  CG2 . VAL C 1 660 ? 12.136  26.024  121.196 1.00 26.08 ? 652  VAL C CG2 1 
ATOM   14304 N  N   . ASP C 1 661 ? 14.326  22.403  122.940 1.00 25.62 ? 653  ASP C N   1 
ATOM   14305 C  CA  . ASP C 1 661 ? 14.951  21.581  123.970 1.00 28.19 ? 653  ASP C CA  1 
ATOM   14306 C  C   . ASP C 1 661 ? 16.392  21.251  123.610 1.00 29.79 ? 653  ASP C C   1 
ATOM   14307 O  O   . ASP C 1 661 ? 17.263  21.203  124.483 1.00 28.29 ? 653  ASP C O   1 
ATOM   14308 C  CB  . ASP C 1 661 ? 14.145  20.298  124.183 1.00 30.59 ? 653  ASP C CB  1 
ATOM   14309 N  N   . THR C 1 662 ? 16.662  21.016  122.326 1.00 27.22 ? 654  THR C N   1 
ATOM   14310 C  CA  . THR C 1 662 ? 18.022  20.706  121.901 1.00 22.60 ? 654  THR C CA  1 
ATOM   14311 C  C   . THR C 1 662 ? 18.960  21.887  122.123 1.00 28.61 ? 654  THR C C   1 
ATOM   14312 O  O   . THR C 1 662 ? 20.098  21.707  122.572 1.00 31.52 ? 654  THR C O   1 
ATOM   14313 C  CB  . THR C 1 662 ? 18.019  20.287  120.433 1.00 26.02 ? 654  THR C CB  1 
ATOM   14314 O  OG1 . THR C 1 662 ? 17.208  19.119  120.290 1.00 25.17 ? 654  THR C OG1 1 
ATOM   14315 C  CG2 . THR C 1 662 ? 19.424  19.980  119.966 1.00 30.73 ? 654  THR C CG2 1 
ATOM   14316 N  N   . VAL C 1 663 ? 18.502  23.103  121.814 1.00 27.60 ? 655  VAL C N   1 
ATOM   14317 C  CA  . VAL C 1 663 ? 19.303  24.291  122.102 1.00 26.02 ? 655  VAL C CA  1 
ATOM   14318 C  C   . VAL C 1 663 ? 19.593  24.389  123.596 1.00 32.88 ? 655  VAL C C   1 
ATOM   14319 O  O   . VAL C 1 663 ? 20.726  24.673  124.007 1.00 25.73 ? 655  VAL C O   1 
ATOM   14320 C  CB  . VAL C 1 663 ? 18.599  25.558  121.590 1.00 23.82 ? 655  VAL C CB  1 
ATOM   14321 C  CG1 . VAL C 1 663 ? 19.364  26.810  122.063 1.00 28.22 ? 655  VAL C CG1 1 
ATOM   14322 C  CG2 . VAL C 1 663 ? 18.497  25.530  120.077 1.00 25.51 ? 655  VAL C CG2 1 
ATOM   14323 N  N   . LYS C 1 664 ? 18.579  24.160  124.434 1.00 29.98 ? 656  LYS C N   1 
ATOM   14324 C  CA  . LYS C 1 664 ? 18.806  24.246  125.873 1.00 35.42 ? 656  LYS C CA  1 
ATOM   14325 C  C   . LYS C 1 664 ? 19.859  23.246  126.340 1.00 38.31 ? 656  LYS C C   1 
ATOM   14326 O  O   . LYS C 1 664 ? 20.620  23.541  127.267 1.00 35.48 ? 656  LYS C O   1 
ATOM   14327 C  CB  . LYS C 1 664 ? 17.492  24.035  126.630 1.00 32.39 ? 656  LYS C CB  1 
ATOM   14328 C  CG  . LYS C 1 664 ? 16.536  25.212  126.537 1.00 33.91 ? 656  LYS C CG  1 
ATOM   14329 C  CD  . LYS C 1 664 ? 15.277  24.957  127.337 1.00 40.28 ? 656  LYS C CD  1 
ATOM   14330 C  CE  . LYS C 1 664 ? 14.190  25.951  126.987 1.00 44.37 ? 656  LYS C CE  1 
ATOM   14331 N  NZ  . LYS C 1 664 ? 12.944  25.717  127.783 1.00 44.49 ? 656  LYS C NZ  1 
ATOM   14332 N  N   . SER C 1 665 ? 19.934  22.074  125.703 1.00 38.86 ? 657  SER C N   1 
ATOM   14333 C  CA  . SER C 1 665 ? 20.855  21.031  126.142 1.00 37.39 ? 657  SER C CA  1 
ATOM   14334 C  C   . SER C 1 665 ? 22.322  21.395  125.942 1.00 39.33 ? 657  SER C C   1 
ATOM   14335 O  O   . SER C 1 665 ? 23.185  20.721  126.513 1.00 44.98 ? 657  SER C O   1 
ATOM   14336 C  CB  . SER C 1 665 ? 20.546  19.716  125.418 1.00 32.85 ? 657  SER C CB  1 
ATOM   14337 O  OG  . SER C 1 665 ? 20.944  19.761  124.055 1.00 33.05 ? 657  SER C OG  1 
ATOM   14338 N  N   . VAL C 1 666 ? 22.633  22.426  125.158 1.00 32.78 ? 658  VAL C N   1 
ATOM   14339 C  CA  . VAL C 1 666 ? 24.016  22.826  124.927 1.00 33.10 ? 658  VAL C CA  1 
ATOM   14340 C  C   . VAL C 1 666 ? 24.339  24.159  125.586 1.00 36.47 ? 658  VAL C C   1 
ATOM   14341 O  O   . VAL C 1 666 ? 25.436  24.697  125.385 1.00 36.59 ? 658  VAL C O   1 
ATOM   14342 C  CB  . VAL C 1 666 ? 24.355  22.865  123.426 1.00 38.98 ? 658  VAL C CB  1 
ATOM   14343 C  CG1 . VAL C 1 666 ? 24.100  21.515  122.792 1.00 33.21 ? 658  VAL C CG1 1 
ATOM   14344 C  CG2 . VAL C 1 666 ? 23.566  23.952  122.722 1.00 41.16 ? 658  VAL C CG2 1 
ATOM   14345 N  N   . LEU C 1 667 ? 23.415  24.708  126.369 1.00 39.76 ? 659  LEU C N   1 
ATOM   14346 C  CA  . LEU C 1 667 ? 23.683  25.932  127.114 1.00 42.22 ? 659  LEU C CA  1 
ATOM   14347 C  C   . LEU C 1 667 ? 24.271  25.615  128.485 1.00 50.25 ? 659  LEU C C   1 
ATOM   14348 O  O   . LEU C 1 667 ? 24.246  24.465  128.937 1.00 51.06 ? 659  LEU C O   1 
ATOM   14349 C  CB  . LEU C 1 667 ? 22.407  26.753  127.265 1.00 42.60 ? 659  LEU C CB  1 
ATOM   14350 C  CG  . LEU C 1 667 ? 21.722  27.192  125.972 1.00 37.97 ? 659  LEU C CG  1 
ATOM   14351 C  CD1 . LEU C 1 667 ? 20.394  27.860  126.298 1.00 39.47 ? 659  LEU C CD1 1 
ATOM   14352 C  CD2 . LEU C 1 667 ? 22.617  28.124  125.165 1.00 37.87 ? 659  LEU C CD2 1 
ATOM   14353 N  N   . MET D 1 9   ? -13.825 -8.548  81.072  1.00 47.97 ? 1    MET D N   1 
ATOM   14354 C  CA  . MET D 1 9   ? -13.112 -8.613  82.341  1.00 42.11 ? 1    MET D CA  1 
ATOM   14355 C  C   . MET D 1 9   ? -13.867 -9.468  83.356  1.00 40.19 ? 1    MET D C   1 
ATOM   14356 O  O   . MET D 1 9   ? -15.081 -9.335  83.520  1.00 41.13 ? 1    MET D O   1 
ATOM   14357 C  CB  . MET D 1 9   ? -12.877 -7.203  82.891  1.00 42.98 ? 1    MET D CB  1 
ATOM   14358 C  CG  . MET D 1 9   ? -11.758 -6.453  82.177  1.00 44.32 ? 1    MET D CG  1 
ATOM   14359 S  SD  . MET D 1 9   ? -11.996 -4.667  82.126  1.00 48.55 ? 1    MET D SD  1 
ATOM   14360 C  CE  . MET D 1 9   ? -13.287 -4.553  80.892  1.00 51.03 ? 1    MET D CE  1 
ATOM   14361 N  N   . SER D 1 10  ? -13.142 -10.358 84.027  1.00 35.76 ? 2    SER D N   1 
ATOM   14362 C  CA  . SER D 1 10  ? -13.747 -11.246 85.005  1.00 31.76 ? 2    SER D CA  1 
ATOM   14363 C  C   . SER D 1 10  ? -13.810 -10.571 86.371  1.00 29.03 ? 2    SER D C   1 
ATOM   14364 O  O   . SER D 1 10  ? -13.093 -9.608  86.652  1.00 27.85 ? 2    SER D O   1 
ATOM   14365 C  CB  . SER D 1 10  ? -12.968 -12.559 85.110  1.00 27.50 ? 2    SER D CB  1 
ATOM   14366 O  OG  . SER D 1 10  ? -11.688 -12.351 85.689  1.00 33.93 ? 2    SER D OG  1 
ATOM   14367 N  N   . GLN D 1 11  ? -14.702 -11.094 87.220  1.00 32.21 ? 3    GLN D N   1 
ATOM   14368 C  CA  . GLN D 1 11  ? -14.753 -10.649 88.609  1.00 31.93 ? 3    GLN D CA  1 
ATOM   14369 C  C   . GLN D 1 11  ? -13.418 -10.842 89.307  1.00 26.49 ? 3    GLN D C   1 
ATOM   14370 O  O   . GLN D 1 11  ? -13.054 -10.038 90.172  1.00 29.49 ? 3    GLN D O   1 
ATOM   14371 C  CB  . GLN D 1 11  ? -15.845 -11.403 89.367  1.00 32.65 ? 3    GLN D CB  1 
ATOM   14372 C  CG  . GLN D 1 11  ? -17.241 -11.100 88.873  1.00 38.30 ? 3    GLN D CG  1 
ATOM   14373 C  CD  . GLN D 1 11  ? -17.611 -9.648  89.070  1.00 41.60 ? 3    GLN D CD  1 
ATOM   14374 O  OE1 . GLN D 1 11  ? -17.452 -8.827  88.167  1.00 45.36 ? 3    GLN D OE1 1 
ATOM   14375 N  NE2 . GLN D 1 11  ? -18.107 -9.320  90.258  1.00 42.05 ? 3    GLN D NE2 1 
ATOM   14376 N  N   . LEU D 1 12  ? -12.680 -11.901 88.949  1.00 22.26 ? 4    LEU D N   1 
ATOM   14377 C  CA  . LEU D 1 12  ? -11.405 -12.181 89.607  1.00 24.48 ? 4    LEU D CA  1 
ATOM   14378 C  C   . LEU D 1 12  ? -10.375 -11.093 89.329  1.00 24.79 ? 4    LEU D C   1 
ATOM   14379 O  O   . LEU D 1 12  ? -9.577  -10.747 90.211  1.00 22.97 ? 4    LEU D O   1 
ATOM   14380 C  CB  . LEU D 1 12  ? -10.865 -13.539 89.163  1.00 29.36 ? 4    LEU D CB  1 
ATOM   14381 C  CG  . LEU D 1 12  ? -11.772 -14.737 89.438  1.00 33.98 ? 4    LEU D CG  1 
ATOM   14382 C  CD1 . LEU D 1 12  ? -10.977 -16.026 89.332  1.00 35.18 ? 4    LEU D CD1 1 
ATOM   14383 C  CD2 . LEU D 1 12  ? -12.431 -14.599 90.805  1.00 32.22 ? 4    LEU D CD2 1 
ATOM   14384 N  N   . ALA D 1 13  ? -10.368 -10.550 88.108  1.00 23.61 ? 5    ALA D N   1 
ATOM   14385 C  CA  . ALA D 1 13  ? -9.484  -9.429  87.801  1.00 23.34 ? 5    ALA D CA  1 
ATOM   14386 C  C   . ALA D 1 13  ? -10.061 -8.118  88.309  1.00 18.56 ? 5    ALA D C   1 
ATOM   14387 O  O   . ALA D 1 13  ? -9.317  -7.240  88.762  1.00 20.37 ? 5    ALA D O   1 
ATOM   14388 C  CB  . ALA D 1 13  ? -9.235  -9.339  86.294  1.00 22.62 ? 5    ALA D CB  1 
ATOM   14389 N  N   . ASN D 1 14  ? -11.387 -7.969  88.245  1.00 19.78 ? 6    ASN D N   1 
ATOM   14390 C  CA  . ASN D 1 14  ? -11.993 -6.700  88.634  1.00 17.55 ? 6    ASN D CA  1 
ATOM   14391 C  C   . ASN D 1 14  ? -11.880 -6.454  90.137  1.00 20.09 ? 6    ASN D C   1 
ATOM   14392 O  O   . ASN D 1 14  ? -11.792 -5.295  90.558  1.00 16.45 ? 6    ASN D O   1 
ATOM   14393 C  CB  . ASN D 1 14  ? -13.454 -6.644  88.161  1.00 19.19 ? 6    ASN D CB  1 
ATOM   14394 C  CG  . ASN D 1 14  ? -13.565 -6.349  86.672  1.00 23.22 ? 6    ASN D CG  1 
ATOM   14395 O  OD1 . ASN D 1 14  ? -12.576 -5.970  86.034  1.00 25.44 ? 6    ASN D OD1 1 
ATOM   14396 N  ND2 . ASN D 1 14  ? -14.765 -6.504  86.113  1.00 21.00 ? 6    ASN D ND2 1 
ATOM   14397 N  N   . VAL D 1 15  ? -11.852 -7.512  90.961  1.00 20.86 ? 7    VAL D N   1 
ATOM   14398 C  CA  . VAL D 1 15  ? -11.650 -7.292  92.393  1.00 21.82 ? 7    VAL D CA  1 
ATOM   14399 C  C   . VAL D 1 15  ? -10.300 -6.626  92.644  1.00 23.40 ? 7    VAL D C   1 
ATOM   14400 O  O   . VAL D 1 15  ? -10.175 -5.773  93.529  1.00 20.22 ? 7    VAL D O   1 
ATOM   14401 C  CB  . VAL D 1 15  ? -11.806 -8.601  93.197  1.00 24.71 ? 7    VAL D CB  1 
ATOM   14402 C  CG1 . VAL D 1 15  ? -10.704 -9.598  92.882  1.00 25.09 ? 7    VAL D CG1 1 
ATOM   14403 C  CG2 . VAL D 1 15  ? -11.803 -8.290  94.699  1.00 22.72 ? 7    VAL D CG2 1 
ATOM   14404 N  N   . ILE D 1 16  ? -9.282  -6.965  91.843  1.00 14.74 ? 8    ILE D N   1 
ATOM   14405 C  CA  . ILE D 1 16  ? -7.996  -6.271  91.944  1.00 17.16 ? 8    ILE D CA  1 
ATOM   14406 C  C   . ILE D 1 16  ? -8.157  -4.797  91.586  1.00 18.47 ? 8    ILE D C   1 
ATOM   14407 O  O   . ILE D 1 16  ? -7.624  -3.911  92.271  1.00 18.12 ? 8    ILE D O   1 
ATOM   14408 C  CB  . ILE D 1 16  ? -6.943  -6.948  91.044  1.00 16.52 ? 8    ILE D CB  1 
ATOM   14409 C  CG1 . ILE D 1 16  ? -6.643  -8.377  91.524  1.00 18.83 ? 8    ILE D CG1 1 
ATOM   14410 C  CG2 . ILE D 1 16  ? -5.682  -6.109  90.991  1.00 16.53 ? 8    ILE D CG2 1 
ATOM   14411 C  CD1 . ILE D 1 16  ? -5.705  -9.162  90.583  1.00 15.55 ? 8    ILE D CD1 1 
ATOM   14412 N  N   . ARG D 1 17  ? -8.859  -4.518  90.481  1.00 19.90 ? 9    ARG D N   1 
ATOM   14413 C  CA  . ARG D 1 17  ? -9.089  -3.136  90.060  1.00 19.36 ? 9    ARG D CA  1 
ATOM   14414 C  C   . ARG D 1 17  ? -9.697  -2.312  91.184  1.00 17.05 ? 9    ARG D C   1 
ATOM   14415 O  O   . ARG D 1 17  ? -9.257  -1.193  91.455  1.00 15.43 ? 9    ARG D O   1 
ATOM   14416 C  CB  . ARG D 1 17  ? -10.007 -3.081  88.830  1.00 15.54 ? 9    ARG D CB  1 
ATOM   14417 C  CG  . ARG D 1 17  ? -9.454  -3.774  87.588  1.00 15.79 ? 9    ARG D CG  1 
ATOM   14418 C  CD  . ARG D 1 17  ? -10.212 -3.463  86.282  1.00 17.99 ? 9    ARG D CD  1 
ATOM   14419 N  NE  . ARG D 1 17  ? -9.281  -3.705  85.180  1.00 24.34 ? 9    ARG D NE  1 
ATOM   14420 C  CZ  . ARG D 1 17  ? -9.123  -4.869  84.559  1.00 23.39 ? 9    ARG D CZ  1 
ATOM   14421 N  NH1 . ARG D 1 17  ? -9.885  -5.914  84.876  1.00 18.41 ? 9    ARG D NH1 1 
ATOM   14422 N  NH2 . ARG D 1 17  ? -8.216  -4.979  83.598  1.00 22.35 ? 9    ARG D NH2 1 
ATOM   14423 N  N   . PHE D 1 18  ? -10.725 -2.846  91.845  1.00 18.56 ? 10   PHE D N   1 
ATOM   14424 C  CA  . PHE D 1 18  ? -11.434 -2.029  92.823  1.00 19.94 ? 10   PHE D CA  1 
ATOM   14425 C  C   . PHE D 1 18  ? -10.712 -1.969  94.163  1.00 19.17 ? 10   PHE D C   1 
ATOM   14426 O  O   . PHE D 1 18  ? -10.712 -0.917  94.813  1.00 15.61 ? 10   PHE D O   1 
ATOM   14427 C  CB  . PHE D 1 18  ? -12.869 -2.522  92.968  1.00 20.42 ? 10   PHE D CB  1 
ATOM   14428 C  CG  . PHE D 1 18  ? -13.711 -2.133  91.803  1.00 23.48 ? 10   PHE D CG  1 
ATOM   14429 C  CD1 . PHE D 1 18  ? -14.119 -0.822  91.649  1.00 17.43 ? 10   PHE D CD1 1 
ATOM   14430 C  CD2 . PHE D 1 18  ? -14.013 -3.045  90.812  1.00 24.35 ? 10   PHE D CD2 1 
ATOM   14431 C  CE1 . PHE D 1 18  ? -14.857 -0.431  90.538  1.00 18.34 ? 10   PHE D CE1 1 
ATOM   14432 C  CE2 . PHE D 1 18  ? -14.740 -2.661  89.706  1.00 24.68 ? 10   PHE D CE2 1 
ATOM   14433 C  CZ  . PHE D 1 18  ? -15.171 -1.354  89.575  1.00 25.78 ? 10   PHE D CZ  1 
ATOM   14434 N  N   . LEU D 1 19  ? -10.082 -3.060  94.593  1.00 20.02 ? 11   LEU D N   1 
ATOM   14435 C  CA  . LEU D 1 19  ? -9.222  -2.959  95.770  1.00 19.50 ? 11   LEU D CA  1 
ATOM   14436 C  C   . LEU D 1 19  ? -8.136  -1.908  95.566  1.00 18.90 ? 11   LEU D C   1 
ATOM   14437 O  O   . LEU D 1 19  ? -7.867  -1.090  96.459  1.00 18.78 ? 11   LEU D O   1 
ATOM   14438 C  CB  . LEU D 1 19  ? -8.587  -4.308  96.087  1.00 19.11 ? 11   LEU D CB  1 
ATOM   14439 C  CG  . LEU D 1 19  ? -9.393  -5.341  96.872  1.00 15.91 ? 11   LEU D CG  1 
ATOM   14440 C  CD1 . LEU D 1 19  ? -8.554  -6.595  97.007  1.00 19.34 ? 11   LEU D CD1 1 
ATOM   14441 C  CD2 . LEU D 1 19  ? -9.744  -4.765  98.243  1.00 17.46 ? 11   LEU D CD2 1 
ATOM   14442 N  N   . SER D 1 20  ? -7.499  -1.915  94.398  1.00 13.41 ? 12   SER D N   1 
ATOM   14443 C  CA  . SER D 1 20  ? -6.425  -0.960  94.135  1.00 14.25 ? 12   SER D CA  1 
ATOM   14444 C  C   . SER D 1 20  ? -6.956  0.467   94.064  1.00 16.18 ? 12   SER D C   1 
ATOM   14445 O  O   . SER D 1 20  ? -6.385  1.380   94.673  1.00 15.28 ? 12   SER D O   1 
ATOM   14446 C  CB  . SER D 1 20  ? -5.711  -1.328  92.844  1.00 17.81 ? 12   SER D CB  1 
ATOM   14447 O  OG  . SER D 1 20  ? -5.183  -2.631  92.945  1.00 17.12 ? 12   SER D OG  1 
ATOM   14448 N  N   . ALA D 1 21  ? -8.046  0.673   93.315  1.00 16.11 ? 13   ALA D N   1 
ATOM   14449 C  CA  . ALA D 1 21  ? -8.632  2.001   93.171  1.00 18.52 ? 13   ALA D CA  1 
ATOM   14450 C  C   . ALA D 1 21  ? -9.136  2.530   94.508  1.00 17.00 ? 13   ALA D C   1 
ATOM   14451 O  O   . ALA D 1 21  ? -8.882  3.683   94.868  1.00 15.61 ? 13   ALA D O   1 
ATOM   14452 C  CB  . ALA D 1 21  ? -9.777  1.965   92.155  1.00 17.04 ? 13   ALA D CB  1 
ATOM   14453 N  N   . ASP D 1 22  ? -9.857  1.693   95.255  1.00 18.36 ? 14   ASP D N   1 
ATOM   14454 C  CA  . ASP D 1 22  ? -10.438 2.125   96.522  1.00 16.78 ? 14   ASP D CA  1 
ATOM   14455 C  C   . ASP D 1 22  ? -9.362  2.445   97.548  1.00 17.97 ? 14   ASP D C   1 
ATOM   14456 O  O   . ASP D 1 22  ? -9.518  3.373   98.354  1.00 15.28 ? 14   ASP D O   1 
ATOM   14457 C  CB  . ASP D 1 22  ? -11.366 1.040   97.076  1.00 14.86 ? 14   ASP D CB  1 
ATOM   14458 C  CG  . ASP D 1 22  ? -12.650 0.873   96.263  1.00 21.98 ? 14   ASP D CG  1 
ATOM   14459 O  OD1 . ASP D 1 22  ? -13.047 1.826   95.561  1.00 24.21 ? 14   ASP D OD1 1 
ATOM   14460 O  OD2 . ASP D 1 22  ? -13.266 -0.219  96.336  1.00 19.70 ? 14   ASP D OD2 1 
ATOM   14461 N  N   . ALA D 1 23  ? -8.292  1.646   97.575  1.00 13.16 ? 15   ALA D N   1 
ATOM   14462 C  CA  . ALA D 1 23  ? -7.261  1.842   98.587  1.00 17.33 ? 15   ALA D CA  1 
ATOM   14463 C  C   . ALA D 1 23  ? -6.443  3.090   98.291  1.00 16.26 ? 15   ALA D C   1 
ATOM   14464 O  O   . ALA D 1 23  ? -6.063  3.832   99.206  1.00 15.87 ? 15   ALA D O   1 
ATOM   14465 C  CB  . ALA D 1 23  ? -6.350  0.616   98.663  1.00 16.05 ? 15   ALA D CB  1 
ATOM   14466 N  N   . VAL D 1 24  ? -6.166  3.332   97.014  1.00 16.50 ? 16   VAL D N   1 
ATOM   14467 C  CA  . VAL D 1 24  ? -5.500  4.563   96.618  1.00 13.31 ? 16   VAL D CA  1 
ATOM   14468 C  C   . VAL D 1 24  ? -6.370  5.766   96.956  1.00 16.52 ? 16   VAL D C   1 
ATOM   14469 O  O   . VAL D 1 24  ? -5.869  6.800   97.416  1.00 17.35 ? 16   VAL D O   1 
ATOM   14470 C  CB  . VAL D 1 24  ? -5.154  4.518   95.120  1.00 14.67 ? 16   VAL D CB  1 
ATOM   14471 C  CG1 . VAL D 1 24  ? -4.769  5.912   94.622  1.00 17.46 ? 16   VAL D CG1 1 
ATOM   14472 C  CG2 . VAL D 1 24  ? -4.017  3.515   94.866  1.00 15.82 ? 16   VAL D CG2 1 
ATOM   14473 N  N   . GLN D 1 25  ? -7.686  5.656   96.719  1.00 14.03 ? 17   GLN D N   1 
ATOM   14474 C  CA  . GLN D 1 25  ? -8.564  6.795   96.975  1.00 14.41 ? 17   GLN D CA  1 
ATOM   14475 C  C   . GLN D 1 25  ? -8.615  7.117   98.459  1.00 16.09 ? 17   GLN D C   1 
ATOM   14476 O  O   . GLN D 1 25  ? -8.598  8.293   98.847  1.00 21.06 ? 17   GLN D O   1 
ATOM   14477 C  CB  . GLN D 1 25  ? -9.969  6.524   96.445  1.00 17.95 ? 17   GLN D CB  1 
ATOM   14478 C  CG  . GLN D 1 25  ? -10.812 7.788   96.290  1.00 20.80 ? 17   GLN D CG  1 
ATOM   14479 C  CD  . GLN D 1 25  ? -10.221 8.743   95.266  1.00 17.93 ? 17   GLN D CD  1 
ATOM   14480 O  OE1 . GLN D 1 25  ? -9.762  8.315   94.214  1.00 17.08 ? 17   GLN D OE1 1 
ATOM   14481 N  NE2 . GLN D 1 25  ? -10.222 10.040  95.578  1.00 18.51 ? 17   GLN D NE2 1 
ATOM   14482 N  N   . LYS D 1 26  ? -8.668  6.084   99.304  1.00 14.18 ? 18   LYS D N   1 
ATOM   14483 C  CA  . LYS D 1 26  ? -8.739  6.308   100.748 1.00 22.69 ? 18   LYS D CA  1 
ATOM   14484 C  C   . LYS D 1 26  ? -7.465  6.964   101.263 1.00 22.15 ? 18   LYS D C   1 
ATOM   14485 O  O   . LYS D 1 26  ? -7.516  7.846   102.128 1.00 18.33 ? 18   LYS D O   1 
ATOM   14486 C  CB  . LYS D 1 26  ? -8.989  4.991   101.478 1.00 20.42 ? 18   LYS D CB  1 
ATOM   14487 C  CG  . LYS D 1 26  ? -9.287  5.153   102.976 1.00 20.08 ? 18   LYS D CG  1 
ATOM   14488 C  CD  . LYS D 1 26  ? -9.665  3.820   103.590 1.00 16.17 ? 18   LYS D CD  1 
ATOM   14489 C  CE  . LYS D 1 26  ? -9.961  3.942   105.091 1.00 20.56 ? 18   LYS D CE  1 
ATOM   14490 N  NZ  . LYS D 1 26  ? -8.708  4.208   105.890 1.00 18.52 ? 18   LYS D NZ  1 
ATOM   14491 N  N   . ALA D 1 27  ? -6.311  6.542   100.743 1.00 20.37 ? 19   ALA D N   1 
ATOM   14492 C  CA  . ALA D 1 27  ? -5.048  7.182   101.077 1.00 17.13 ? 19   ALA D CA  1 
ATOM   14493 C  C   . ALA D 1 27  ? -4.910  8.561   100.447 1.00 20.12 ? 19   ALA D C   1 
ATOM   14494 O  O   . ALA D 1 27  ? -4.044  9.328   100.875 1.00 16.55 ? 19   ALA D O   1 
ATOM   14495 C  CB  . ALA D 1 27  ? -3.880  6.293   100.634 1.00 14.09 ? 19   ALA D CB  1 
ATOM   14496 N  N   . ASN D 1 28  ? -5.748  8.893   99.460  1.00 16.96 ? 20   ASN D N   1 
ATOM   14497 C  CA  . ASN D 1 28  ? -5.549  10.074  98.612  1.00 20.95 ? 20   ASN D CA  1 
ATOM   14498 C  C   . ASN D 1 28  ? -4.102  10.157  98.124  1.00 21.02 ? 20   ASN D C   1 
ATOM   14499 O  O   . ASN D 1 28  ? -3.506  11.235  98.044  1.00 18.82 ? 20   ASN D O   1 
ATOM   14500 C  CB  . ASN D 1 28  ? -5.958  11.357  99.339  1.00 29.41 ? 20   ASN D CB  1 
ATOM   14501 C  CG  . ASN D 1 28  ? -6.147  12.529  98.391  1.00 37.65 ? 20   ASN D CG  1 
ATOM   14502 O  OD1 . ASN D 1 28  ? -6.485  12.352  97.217  1.00 33.88 ? 20   ASN D OD1 1 
ATOM   14503 N  ND2 . ASN D 1 28  ? -5.932  13.735  98.897  1.00 45.88 ? 20   ASN D ND2 1 
ATOM   14504 N  N   . SER D 1 29  ? -3.533  9.001   97.788  1.00 16.37 ? 21   SER D N   1 
ATOM   14505 C  CA  . SER D 1 29  ? -2.129  8.920   97.411  1.00 17.96 ? 21   SER D CA  1 
ATOM   14506 C  C   . SER D 1 29  ? -1.880  7.566   96.761  1.00 16.91 ? 21   SER D C   1 
ATOM   14507 O  O   . SER D 1 29  ? -2.407  6.551   97.231  1.00 18.30 ? 21   SER D O   1 
ATOM   14508 C  CB  . SER D 1 29  ? -1.227  9.098   98.649  1.00 15.17 ? 21   SER D CB  1 
ATOM   14509 O  OG  . SER D 1 29  ? 0.147   8.964   98.328  1.00 15.66 ? 21   SER D OG  1 
ATOM   14510 N  N   . GLY D 1 30  ? -1.094  7.545   95.678  1.00 15.65 ? 22   GLY D N   1 
ATOM   14511 C  CA  . GLY D 1 30  ? -0.718  6.259   95.117  1.00 15.43 ? 22   GLY D CA  1 
ATOM   14512 C  C   . GLY D 1 30  ? -1.020  6.134   93.633  1.00 15.61 ? 22   GLY D C   1 
ATOM   14513 O  O   . GLY D 1 30  ? -1.377  7.104   92.952  1.00 20.87 ? 22   GLY D O   1 
ATOM   14514 N  N   . HIS D 1 31  ? -0.864  4.906   93.131  1.00 14.79 ? 23   HIS D N   1 
ATOM   14515 C  CA  . HIS D 1 31  ? -0.761  4.630   91.698  1.00 14.64 ? 23   HIS D CA  1 
ATOM   14516 C  C   . HIS D 1 31  ? -1.800  3.586   91.309  1.00 16.64 ? 23   HIS D C   1 
ATOM   14517 O  O   . HIS D 1 31  ? -1.547  2.379   91.416  1.00 16.21 ? 23   HIS D O   1 
ATOM   14518 C  CB  . HIS D 1 31  ? 0.645   4.150   91.336  1.00 17.14 ? 23   HIS D CB  1 
ATOM   14519 C  CG  . HIS D 1 31  ? 1.727   5.124   91.688  1.00 23.05 ? 23   HIS D CG  1 
ATOM   14520 N  ND1 . HIS D 1 31  ? 2.082   5.403   92.991  1.00 22.11 ? 23   HIS D ND1 1 
ATOM   14521 C  CD2 . HIS D 1 31  ? 2.528   5.888   90.908  1.00 22.95 ? 23   HIS D CD2 1 
ATOM   14522 C  CE1 . HIS D 1 31  ? 3.052   6.300   92.998  1.00 23.97 ? 23   HIS D CE1 1 
ATOM   14523 N  NE2 . HIS D 1 31  ? 3.340   6.613   91.748  1.00 23.28 ? 23   HIS D NE2 1 
ATOM   14524 N  N   . PRO D 1 32  ? -2.988  4.012   90.855  1.00 15.81 ? 24   PRO D N   1 
ATOM   14525 C  CA  . PRO D 1 32  ? -4.053  3.042   90.554  1.00 15.95 ? 24   PRO D CA  1 
ATOM   14526 C  C   . PRO D 1 32  ? -4.026  2.499   89.129  1.00 15.10 ? 24   PRO D C   1 
ATOM   14527 O  O   . PRO D 1 32  ? -4.578  1.426   88.866  1.00 14.68 ? 24   PRO D O   1 
ATOM   14528 C  CB  . PRO D 1 32  ? -5.336  3.847   90.808  1.00 20.71 ? 24   PRO D CB  1 
ATOM   14529 C  CG  . PRO D 1 32  ? -4.949  5.260   90.520  1.00 21.37 ? 24   PRO D CG  1 
ATOM   14530 C  CD  . PRO D 1 32  ? -3.481  5.399   90.862  1.00 19.70 ? 24   PRO D CD  1 
ATOM   14531 N  N   . GLY D 1 33  ? -3.377  3.213   88.207  1.00 18.69 ? 25   GLY D N   1 
ATOM   14532 C  CA  . GLY D 1 33  ? -3.527  2.894   86.792  1.00 20.39 ? 25   GLY D CA  1 
ATOM   14533 C  C   . GLY D 1 33  ? -2.801  1.630   86.360  1.00 19.14 ? 25   GLY D C   1 
ATOM   14534 O  O   . GLY D 1 33  ? -3.339  0.829   85.587  1.00 14.07 ? 25   GLY D O   1 
ATOM   14535 N  N   . ALA D 1 34  ? -1.573  1.436   86.830  1.00 15.20 ? 26   ALA D N   1 
ATOM   14536 C  CA  . ALA D 1 34  ? -0.848  0.233   86.434  1.00 16.31 ? 26   ALA D CA  1 
ATOM   14537 C  C   . ALA D 1 34  ? -1.431  -1.032  87.078  1.00 16.27 ? 26   ALA D C   1 
ATOM   14538 O  O   . ALA D 1 34  ? -1.505  -2.076  86.413  1.00 15.89 ? 26   ALA D O   1 
ATOM   14539 C  CB  . ALA D 1 34  ? 0.643   0.382   86.759  1.00 16.41 ? 26   ALA D CB  1 
ATOM   14540 N  N   . PRO D 1 35  ? -1.847  -1.009  88.355  1.00 16.46 ? 27   PRO D N   1 
ATOM   14541 C  CA  . PRO D 1 35  ? -2.581  -2.177  88.882  1.00 15.04 ? 27   PRO D CA  1 
ATOM   14542 C  C   . PRO D 1 35  ? -3.812  -2.549  88.061  1.00 16.30 ? 27   PRO D C   1 
ATOM   14543 O  O   . PRO D 1 35  ? -4.042  -3.738  87.792  1.00 18.69 ? 27   PRO D O   1 
ATOM   14544 C  CB  . PRO D 1 35  ? -2.955  -1.731  90.301  1.00 15.22 ? 27   PRO D CB  1 
ATOM   14545 C  CG  . PRO D 1 35  ? -1.800  -0.837  90.697  1.00 14.67 ? 27   PRO D CG  1 
ATOM   14546 C  CD  . PRO D 1 35  ? -1.449  -0.082  89.437  1.00 13.81 ? 27   PRO D CD  1 
ATOM   14547 N  N   . MET D 1 36  ? -4.609  -1.564  87.649  1.00 13.57 ? 28   MET D N   1 
ATOM   14548 C  CA  . MET D 1 36  ? -5.767  -1.852  86.808  1.00 14.14 ? 28   MET D CA  1 
ATOM   14549 C  C   . MET D 1 36  ? -5.350  -2.423  85.461  1.00 17.64 ? 28   MET D C   1 
ATOM   14550 O  O   . MET D 1 36  ? -5.979  -3.363  84.953  1.00 19.50 ? 28   MET D O   1 
ATOM   14551 C  CB  . MET D 1 36  ? -6.601  -0.589  86.620  1.00 16.09 ? 28   MET D CB  1 
ATOM   14552 C  CG  . MET D 1 36  ? -7.185  -0.088  87.929  1.00 18.63 ? 28   MET D CG  1 
ATOM   14553 S  SD  . MET D 1 36  ? -7.956  1.520   87.742  1.00 20.44 ? 28   MET D SD  1 
ATOM   14554 C  CE  . MET D 1 36  ? -9.382  1.102   86.732  1.00 19.91 ? 28   MET D CE  1 
ATOM   14555 N  N   . GLY D 1 37  ? -4.297  -1.865  84.864  1.00 17.52 ? 29   GLY D N   1 
ATOM   14556 C  CA  . GLY D 1 37  ? -3.822  -2.368  83.588  1.00 15.30 ? 29   GLY D CA  1 
ATOM   14557 C  C   . GLY D 1 37  ? -3.257  -3.775  83.656  1.00 15.08 ? 29   GLY D C   1 
ATOM   14558 O  O   . GLY D 1 37  ? -3.325  -4.519  82.674  1.00 18.01 ? 29   GLY D O   1 
ATOM   14559 N  N   . MET D 1 38  ? -2.688  -4.160  84.799  1.00 14.18 ? 30   MET D N   1 
ATOM   14560 C  CA  . MET D 1 38  ? -2.056  -5.464  84.944  1.00 14.00 ? 30   MET D CA  1 
ATOM   14561 C  C   . MET D 1 38  ? -2.973  -6.508  85.585  1.00 15.96 ? 30   MET D C   1 
ATOM   14562 O  O   . MET D 1 38  ? -2.506  -7.602  85.922  1.00 16.40 ? 30   MET D O   1 
ATOM   14563 C  CB  . MET D 1 38  ? -0.756  -5.335  85.761  1.00 13.23 ? 30   MET D CB  1 
ATOM   14564 C  CG  . MET D 1 38  ? 0.380   -4.593  85.052  1.00 18.68 ? 30   MET D CG  1 
ATOM   14565 S  SD  . MET D 1 38  ? 1.946   -4.732  85.961  1.00 18.64 ? 30   MET D SD  1 
ATOM   14566 C  CE  . MET D 1 38  ? 1.707   -3.490  87.219  1.00 21.15 ? 30   MET D CE  1 
ATOM   14567 N  N   . ALA D 1 39  ? -4.269  -6.213  85.736  1.00 14.67 ? 31   ALA D N   1 
ATOM   14568 C  CA  . ALA D 1 39  ? -5.146  -7.106  86.490  1.00 17.06 ? 31   ALA D CA  1 
ATOM   14569 C  C   . ALA D 1 39  ? -5.291  -8.476  85.824  1.00 16.72 ? 31   ALA D C   1 
ATOM   14570 O  O   . ALA D 1 39  ? -5.276  -9.503  86.512  1.00 18.86 ? 31   ALA D O   1 
ATOM   14571 C  CB  . ALA D 1 39  ? -6.515  -6.453  86.693  1.00 15.65 ? 31   ALA D CB  1 
ATOM   14572 N  N   . GLU D 1 40  ? -5.439  -8.521  84.493  1.00 16.03 ? 32   GLU D N   1 
ATOM   14573 C  CA  . GLU D 1 40  ? -5.542  -9.816  83.817  1.00 16.82 ? 32   GLU D CA  1 
ATOM   14574 C  C   . GLU D 1 40  ? -4.215  -10.563 83.840  1.00 22.13 ? 32   GLU D C   1 
ATOM   14575 O  O   . GLU D 1 40  ? -4.198  -11.789 83.970  1.00 19.49 ? 32   GLU D O   1 
ATOM   14576 C  CB  . GLU D 1 40  ? -6.022  -9.649  82.378  1.00 18.02 ? 32   GLU D CB  1 
ATOM   14577 C  CG  . GLU D 1 40  ? -7.518  -9.499  82.254  1.00 21.67 ? 32   GLU D CG  1 
ATOM   14578 C  CD  . GLU D 1 40  ? -8.007  -8.120  82.673  1.00 26.21 ? 32   GLU D CD  1 
ATOM   14579 O  OE1 . GLU D 1 40  ? -7.306  -7.127  82.399  1.00 23.87 ? 32   GLU D OE1 1 
ATOM   14580 O  OE2 . GLU D 1 40  ? -9.093  -8.028  83.275  1.00 20.83 ? 32   GLU D OE2 1 
ATOM   14581 N  N   . MET D 1 41  ? -3.096  -9.846  83.701  1.00 17.67 ? 33   MET D N   1 
ATOM   14582 C  CA  . MET D 1 41  ? -1.790  -10.481 83.851  1.00 15.46 ? 33   MET D CA  1 
ATOM   14583 C  C   . MET D 1 41  ? -1.660  -11.137 85.220  1.00 15.70 ? 33   MET D C   1 
ATOM   14584 O  O   . MET D 1 41  ? -1.193  -12.277 85.338  1.00 18.49 ? 33   MET D O   1 
ATOM   14585 C  CB  . MET D 1 41  ? -0.685  -9.446  83.644  1.00 15.03 ? 33   MET D CB  1 
ATOM   14586 C  CG  . MET D 1 41  ? -0.681  -8.801  82.260  1.00 16.72 ? 33   MET D CG  1 
ATOM   14587 S  SD  . MET D 1 41  ? 0.252   -7.246  82.221  1.00 19.39 ? 33   MET D SD  1 
ATOM   14588 C  CE  . MET D 1 41  ? 1.904   -7.806  82.624  1.00 16.56 ? 33   MET D CE  1 
ATOM   14589 N  N   . ALA D 1 42  ? -2.058  -10.416 86.270  1.00 14.14 ? 34   ALA D N   1 
ATOM   14590 C  CA  . ALA D 1 42  ? -1.992  -10.952 87.625  1.00 15.89 ? 34   ALA D CA  1 
ATOM   14591 C  C   . ALA D 1 42  ? -2.936  -12.136 87.795  1.00 20.40 ? 34   ALA D C   1 
ATOM   14592 O  O   . ALA D 1 42  ? -2.567  -13.161 88.385  1.00 19.70 ? 34   ALA D O   1 
ATOM   14593 C  CB  . ALA D 1 42  ? -2.329  -9.853  88.633  1.00 15.56 ? 34   ALA D CB  1 
ATOM   14594 N  N   . GLU D 1 43  ? -4.172  -11.998 87.312  1.00 19.01 ? 35   GLU D N   1 
ATOM   14595 C  CA  . GLU D 1 43  ? -5.131  -13.096 87.421  1.00 21.02 ? 35   GLU D CA  1 
ATOM   14596 C  C   . GLU D 1 43  ? -4.568  -14.370 86.804  1.00 18.54 ? 35   GLU D C   1 
ATOM   14597 O  O   . GLU D 1 43  ? -4.527  -15.420 87.450  1.00 17.65 ? 35   GLU D O   1 
ATOM   14598 C  CB  . GLU D 1 43  ? -6.458  -12.733 86.750  1.00 19.11 ? 35   GLU D CB  1 
ATOM   14599 C  CG  . GLU D 1 43  ? -7.447  -13.915 86.724  1.00 27.27 ? 35   GLU D CG  1 
ATOM   14600 C  CD  . GLU D 1 43  ? -8.743  -13.629 85.964  1.00 32.04 ? 35   GLU D CD  1 
ATOM   14601 O  OE1 . GLU D 1 43  ? -9.615  -14.525 85.925  1.00 34.14 ? 35   GLU D OE1 1 
ATOM   14602 O  OE2 . GLU D 1 43  ? -8.901  -12.526 85.401  1.00 29.73 ? 35   GLU D OE2 1 
ATOM   14603 N  N   . THR D 1 44  ? -4.099  -14.276 85.557  1.00 18.74 ? 36   THR D N   1 
ATOM   14604 C  CA  . THR D 1 44  ? -3.590  -15.449 84.853  1.00 17.81 ? 36   THR D CA  1 
ATOM   14605 C  C   . THR D 1 44  ? -2.398  -16.063 85.578  1.00 16.64 ? 36   THR D C   1 
ATOM   14606 O  O   . THR D 1 44  ? -2.398  -17.262 85.884  1.00 21.29 ? 36   THR D O   1 
ATOM   14607 C  CB  . THR D 1 44  ? -3.206  -15.077 83.421  1.00 19.73 ? 36   THR D CB  1 
ATOM   14608 O  OG1 . THR D 1 44  ? -4.305  -14.426 82.781  1.00 24.06 ? 36   THR D OG1 1 
ATOM   14609 C  CG2 . THR D 1 44  ? -2.837  -16.328 82.622  1.00 18.75 ? 36   THR D CG2 1 
ATOM   14610 N  N   . LEU D 1 45  ? -1.366  -15.259 85.859  1.00 17.50 ? 37   LEU D N   1 
ATOM   14611 C  CA  . LEU D 1 45  ? -0.167  -15.796 86.497  1.00 17.12 ? 37   LEU D CA  1 
ATOM   14612 C  C   . LEU D 1 45  ? -0.486  -16.417 87.851  1.00 20.87 ? 37   LEU D C   1 
ATOM   14613 O  O   . LEU D 1 45  ? -0.137  -17.573 88.112  1.00 18.20 ? 37   LEU D O   1 
ATOM   14614 C  CB  . LEU D 1 45  ? 0.895   -14.705 86.660  1.00 14.53 ? 37   LEU D CB  1 
ATOM   14615 C  CG  . LEU D 1 45  ? 2.138   -15.251 87.375  1.00 15.87 ? 37   LEU D CG  1 
ATOM   14616 C  CD1 . LEU D 1 45  ? 2.788   -16.387 86.573  1.00 15.60 ? 37   LEU D CD1 1 
ATOM   14617 C  CD2 . LEU D 1 45  ? 3.161   -14.155 87.690  1.00 15.40 ? 37   LEU D CD2 1 
ATOM   14618 N  N   . TRP D 1 46  ? -1.162  -15.667 88.723  1.00 14.64 ? 38   TRP D N   1 
ATOM   14619 C  CA  . TRP D 1 46  ? -1.347  -16.118 90.103  1.00 18.21 ? 38   TRP D CA  1 
ATOM   14620 C  C   . TRP D 1 46  ? -2.369  -17.249 90.222  1.00 20.80 ? 38   TRP D C   1 
ATOM   14621 O  O   . TRP D 1 46  ? -2.213  -18.125 91.080  1.00 20.58 ? 38   TRP D O   1 
ATOM   14622 C  CB  . TRP D 1 46  ? -1.747  -14.935 90.988  1.00 17.92 ? 38   TRP D CB  1 
ATOM   14623 C  CG  . TRP D 1 46  ? -0.541  -14.131 91.431  1.00 14.14 ? 38   TRP D CG  1 
ATOM   14624 C  CD1 . TRP D 1 46  ? 0.342   -13.476 90.628  1.00 16.01 ? 38   TRP D CD1 1 
ATOM   14625 C  CD2 . TRP D 1 46  ? -0.075  -13.949 92.777  1.00 16.21 ? 38   TRP D CD2 1 
ATOM   14626 N  NE1 . TRP D 1 46  ? 1.333   -12.889 91.394  1.00 17.60 ? 38   TRP D NE1 1 
ATOM   14627 C  CE2 . TRP D 1 46  ? 1.092   -13.164 92.714  1.00 15.05 ? 38   TRP D CE2 1 
ATOM   14628 C  CE3 . TRP D 1 46  ? -0.538  -14.376 94.031  1.00 20.13 ? 38   TRP D CE3 1 
ATOM   14629 C  CZ2 . TRP D 1 46  ? 1.801   -12.781 93.857  1.00 15.26 ? 38   TRP D CZ2 1 
ATOM   14630 C  CZ3 . TRP D 1 46  ? 0.162   -13.999 95.161  1.00 21.54 ? 38   TRP D CZ3 1 
ATOM   14631 C  CH2 . TRP D 1 46  ? 1.324   -13.209 95.066  1.00 15.09 ? 38   TRP D CH2 1 
ATOM   14632 N  N   . THR D 1 47  ? -3.418  -17.260 89.398  1.00 17.45 ? 39   THR D N   1 
ATOM   14633 C  CA  . THR D 1 47  ? -4.395  -18.340 89.528  1.00 22.47 ? 39   THR D CA  1 
ATOM   14634 C  C   . THR D 1 47  ? -4.023  -19.588 88.736  1.00 24.80 ? 39   THR D C   1 
ATOM   14635 O  O   . THR D 1 47  ? -4.423  -20.688 89.125  1.00 27.91 ? 39   THR D O   1 
ATOM   14636 C  CB  . THR D 1 47  ? -5.804  -17.892 89.108  1.00 22.69 ? 39   THR D CB  1 
ATOM   14637 O  OG1 . THR D 1 47  ? -5.867  -17.671 87.691  1.00 23.17 ? 39   THR D OG1 1 
ATOM   14638 C  CG2 . THR D 1 47  ? -6.226  -16.638 89.849  1.00 21.58 ? 39   THR D CG2 1 
ATOM   14639 N  N   . LYS D 1 48  ? -3.267  -19.461 87.643  1.00 25.17 ? 40   LYS D N   1 
ATOM   14640 C  CA  . LYS D 1 48  ? -3.001  -20.613 86.784  1.00 23.67 ? 40   LYS D CA  1 
ATOM   14641 C  C   . LYS D 1 48  ? -1.604  -21.204 86.938  1.00 23.06 ? 40   LYS D C   1 
ATOM   14642 O  O   . LYS D 1 48  ? -1.416  -22.379 86.607  1.00 21.56 ? 40   LYS D O   1 
ATOM   14643 C  CB  . LYS D 1 48  ? -3.196  -20.246 85.307  1.00 22.51 ? 40   LYS D CB  1 
ATOM   14644 C  CG  . LYS D 1 48  ? -4.599  -19.784 84.924  1.00 28.72 ? 40   LYS D CG  1 
ATOM   14645 C  CD  . LYS D 1 48  ? -5.658  -20.768 85.356  1.00 32.20 ? 40   LYS D CD  1 
ATOM   14646 C  CE  . LYS D 1 48  ? -6.953  -20.552 84.583  1.00 40.77 ? 40   LYS D CE  1 
ATOM   14647 N  NZ  . LYS D 1 48  ? -6.832  -21.007 83.168  1.00 46.93 ? 40   LYS D NZ  1 
ATOM   14648 N  N   . PHE D 1 49  ? -0.616  -20.431 87.399  1.00 17.78 ? 41   PHE D N   1 
ATOM   14649 C  CA  . PHE D 1 49  ? 0.738   -20.986 87.370  1.00 22.42 ? 41   PHE D CA  1 
ATOM   14650 C  C   . PHE D 1 49  ? 1.480   -20.887 88.694  1.00 20.92 ? 41   PHE D C   1 
ATOM   14651 O  O   . PHE D 1 49  ? 2.203   -21.819 89.049  1.00 21.86 ? 41   PHE D O   1 
ATOM   14652 C  CB  . PHE D 1 49  ? 1.578   -20.287 86.291  1.00 21.27 ? 41   PHE D CB  1 
ATOM   14653 C  CG  . PHE D 1 49  ? 1.027   -20.421 84.911  1.00 18.11 ? 41   PHE D CG  1 
ATOM   14654 C  CD1 . PHE D 1 49  ? 1.408   -21.472 84.101  1.00 19.09 ? 41   PHE D CD1 1 
ATOM   14655 C  CD2 . PHE D 1 49  ? 0.130   -19.484 84.417  1.00 18.78 ? 41   PHE D CD2 1 
ATOM   14656 C  CE1 . PHE D 1 49  ? 0.904   -21.599 82.823  1.00 27.69 ? 41   PHE D CE1 1 
ATOM   14657 C  CE2 . PHE D 1 49  ? -0.377  -19.601 83.142  1.00 19.13 ? 41   PHE D CE2 1 
ATOM   14658 C  CZ  . PHE D 1 49  ? 0.007   -20.662 82.341  1.00 23.02 ? 41   PHE D CZ  1 
ATOM   14659 N  N   . LEU D 1 50  ? 1.340   -19.777 89.417  1.00 21.16 ? 42   LEU D N   1 
ATOM   14660 C  CA  . LEU D 1 50  ? 2.205   -19.504 90.563  1.00 19.51 ? 42   LEU D CA  1 
ATOM   14661 C  C   . LEU D 1 50  ? 2.046   -20.565 91.648  1.00 21.26 ? 42   LEU D C   1 
ATOM   14662 O  O   . LEU D 1 50  ? 0.937   -20.846 92.104  1.00 22.00 ? 42   LEU D O   1 
ATOM   14663 C  CB  . LEU D 1 50  ? 1.899   -18.114 91.131  1.00 14.34 ? 42   LEU D CB  1 
ATOM   14664 C  CG  . LEU D 1 50  ? 2.923   -17.602 92.148  1.00 13.75 ? 42   LEU D CG  1 
ATOM   14665 C  CD1 . LEU D 1 50  ? 4.280   -17.392 91.489  1.00 14.85 ? 42   LEU D CD1 1 
ATOM   14666 C  CD2 . LEU D 1 50  ? 2.471   -16.322 92.869  1.00 14.97 ? 42   LEU D CD2 1 
ATOM   14667 N  N   . ASN D 1 51  ? 3.169   -21.158 92.061  1.00 20.40 ? 43   ASN D N   1 
ATOM   14668 C  CA  . ASN D 1 51  ? 3.196   -22.200 93.086  1.00 19.30 ? 43   ASN D CA  1 
ATOM   14669 C  C   . ASN D 1 51  ? 3.736   -21.600 94.377  1.00 19.54 ? 43   ASN D C   1 
ATOM   14670 O  O   . ASN D 1 51  ? 4.937   -21.348 94.494  1.00 22.64 ? 43   ASN D O   1 
ATOM   14671 C  CB  . ASN D 1 51  ? 4.044   -23.381 92.628  1.00 21.27 ? 43   ASN D CB  1 
ATOM   14672 C  CG  . ASN D 1 51  ? 3.351   -24.202 91.563  1.00 21.71 ? 43   ASN D CG  1 
ATOM   14673 O  OD1 . ASN D 1 51  ? 2.148   -24.430 91.645  1.00 20.48 ? 43   ASN D OD1 1 
ATOM   14674 N  ND2 . ASN D 1 51  ? 4.096   -24.627 90.551  1.00 19.85 ? 43   ASN D ND2 1 
ATOM   14675 N  N   . HIS D 1 52  ? 2.851   -21.383 95.345  1.00 17.32 ? 44   HIS D N   1 
ATOM   14676 C  CA  . HIS D 1 52  ? 3.228   -20.723 96.586  1.00 15.32 ? 44   HIS D CA  1 
ATOM   14677 C  C   . HIS D 1 52  ? 2.327   -21.224 97.706  1.00 21.63 ? 44   HIS D C   1 
ATOM   14678 O  O   . HIS D 1 52  ? 1.230   -21.741 97.461  1.00 20.84 ? 44   HIS D O   1 
ATOM   14679 C  CB  . HIS D 1 52  ? 3.129   -19.192 96.462  1.00 17.14 ? 44   HIS D CB  1 
ATOM   14680 C  CG  . HIS D 1 52  ? 1.746   -18.692 96.171  1.00 19.82 ? 44   HIS D CG  1 
ATOM   14681 N  ND1 . HIS D 1 52  ? 1.085   -17.807 96.996  1.00 19.73 ? 44   HIS D ND1 1 
ATOM   14682 C  CD2 . HIS D 1 52  ? 0.895   -18.959 95.149  1.00 21.80 ? 44   HIS D CD2 1 
ATOM   14683 C  CE1 . HIS D 1 52  ? -0.111  -17.547 96.495  1.00 20.79 ? 44   HIS D CE1 1 
ATOM   14684 N  NE2 . HIS D 1 52  ? -0.252  -18.234 95.375  1.00 23.47 ? 44   HIS D NE2 1 
ATOM   14685 N  N   . ASN D 1 53  ? 2.794   -21.064 98.944  1.00 16.47 ? 45   ASN D N   1 
ATOM   14686 C  CA  . ASN D 1 53  ? 2.003   -21.451 100.115 1.00 16.73 ? 45   ASN D CA  1 
ATOM   14687 C  C   . ASN D 1 53  ? 1.786   -20.253 101.027 1.00 16.34 ? 45   ASN D C   1 
ATOM   14688 O  O   . ASN D 1 53  ? 2.688   -19.892 101.801 1.00 18.07 ? 45   ASN D O   1 
ATOM   14689 C  CB  . ASN D 1 53  ? 2.674   -22.586 100.885 1.00 20.09 ? 45   ASN D CB  1 
ATOM   14690 C  CG  . ASN D 1 53  ? 1.813   -23.101 102.023 1.00 19.70 ? 45   ASN D CG  1 
ATOM   14691 O  OD1 . ASN D 1 53  ? 0.665   -22.690 102.176 1.00 21.08 ? 45   ASN D OD1 1 
ATOM   14692 N  ND2 . ASN D 1 53  ? 2.355   -24.024 102.816 1.00 21.54 ? 45   ASN D ND2 1 
ATOM   14693 N  N   . PRO D 1 54  ? 0.597   -19.641 101.014 1.00 23.44 ? 46   PRO D N   1 
ATOM   14694 C  CA  . PRO D 1 54  ? 0.342   -18.507 101.921 1.00 21.21 ? 46   PRO D CA  1 
ATOM   14695 C  C   . PRO D 1 54  ? 0.571   -18.828 103.390 1.00 21.49 ? 46   PRO D C   1 
ATOM   14696 O  O   . PRO D 1 54  ? 0.914   -17.921 104.156 1.00 21.95 ? 46   PRO D O   1 
ATOM   14697 C  CB  . PRO D 1 54  ? -1.134  -18.164 101.656 1.00 25.18 ? 46   PRO D CB  1 
ATOM   14698 C  CG  . PRO D 1 54  ? -1.465  -18.814 100.357 1.00 26.92 ? 46   PRO D CG  1 
ATOM   14699 C  CD  . PRO D 1 54  ? -0.610  -20.038 100.270 1.00 23.42 ? 46   PRO D CD  1 
ATOM   14700 N  N   . ALA D 1 55  ? 0.385   -20.081 103.817 1.00 20.56 ? 47   ALA D N   1 
ATOM   14701 C  CA  . ALA D 1 55  ? 0.642   -20.421 105.211 1.00 24.85 ? 47   ALA D CA  1 
ATOM   14702 C  C   . ALA D 1 55  ? 2.127   -20.513 105.546 1.00 25.24 ? 47   ALA D C   1 
ATOM   14703 O  O   . ALA D 1 55  ? 2.470   -20.588 106.729 1.00 23.99 ? 47   ALA D O   1 
ATOM   14704 C  CB  . ALA D 1 55  ? -0.034  -21.744 105.581 1.00 28.06 ? 47   ALA D CB  1 
ATOM   14705 N  N   . ASN D 1 56  ? 3.012   -20.541 104.549 1.00 20.00 ? 48   ASN D N   1 
ATOM   14706 C  CA  . ASN D 1 56  ? 4.452   -20.519 104.794 1.00 17.93 ? 48   ASN D CA  1 
ATOM   14707 C  C   . ASN D 1 56  ? 5.106   -19.710 103.682 1.00 17.58 ? 48   ASN D C   1 
ATOM   14708 O  O   . ASN D 1 56  ? 5.560   -20.256 102.665 1.00 19.83 ? 48   ASN D O   1 
ATOM   14709 C  CB  . ASN D 1 56  ? 5.047   -21.926 104.888 1.00 18.83 ? 48   ASN D CB  1 
ATOM   14710 C  CG  . ASN D 1 56  ? 6.557   -21.900 105.106 1.00 19.95 ? 48   ASN D CG  1 
ATOM   14711 O  OD1 . ASN D 1 56  ? 7.111   -20.869 105.462 1.00 21.33 ? 48   ASN D OD1 1 
ATOM   14712 N  ND2 . ASN D 1 56  ? 7.219   -23.028 104.894 1.00 19.86 ? 48   ASN D ND2 1 
ATOM   14713 N  N   . PRO D 1 57  ? 5.171   -18.391 103.848 1.00 20.00 ? 49   PRO D N   1 
ATOM   14714 C  CA  . PRO D 1 57  ? 5.823   -17.546 102.834 1.00 21.24 ? 49   PRO D CA  1 
ATOM   14715 C  C   . PRO D 1 57  ? 7.315   -17.821 102.675 1.00 17.47 ? 49   PRO D C   1 
ATOM   14716 O  O   . PRO D 1 57  ? 7.923   -17.313 101.720 1.00 18.72 ? 49   PRO D O   1 
ATOM   14717 C  CB  . PRO D 1 57  ? 5.567   -16.121 103.349 1.00 24.77 ? 49   PRO D CB  1 
ATOM   14718 C  CG  . PRO D 1 57  ? 4.416   -16.259 104.323 1.00 24.26 ? 49   PRO D CG  1 
ATOM   14719 C  CD  . PRO D 1 57  ? 4.593   -17.604 104.949 1.00 22.21 ? 49   PRO D CD  1 
ATOM   14720 N  N   . LYS D 1 58  ? 7.919   -18.596 103.568 1.00 18.01 ? 50   LYS D N   1 
ATOM   14721 C  CA  . LYS D 1 58  ? 9.317   -18.988 103.462 1.00 17.42 ? 50   LYS D CA  1 
ATOM   14722 C  C   . LYS D 1 58  ? 9.497   -20.398 102.920 1.00 17.14 ? 50   LYS D C   1 
ATOM   14723 O  O   . LYS D 1 58  ? 10.595  -20.950 103.025 1.00 19.69 ? 50   LYS D O   1 
ATOM   14724 C  CB  . LYS D 1 58  ? 10.002  -18.873 104.824 1.00 23.56 ? 50   LYS D CB  1 
ATOM   14725 C  CG  . LYS D 1 58  ? 9.920   -17.483 105.443 1.00 31.07 ? 50   LYS D CG  1 
ATOM   14726 C  CD  . LYS D 1 58  ? 10.719  -16.477 104.635 1.00 37.79 ? 50   LYS D CD  1 
ATOM   14727 C  CE  . LYS D 1 58  ? 10.894  -15.171 105.399 1.00 41.86 ? 50   LYS D CE  1 
ATOM   14728 N  NZ  . LYS D 1 58  ? 11.560  -14.137 104.566 1.00 42.90 ? 50   LYS D NZ  1 
ATOM   14729 N  N   . PHE D 1 59  ? 8.449   -20.998 102.357 1.00 17.06 ? 51   PHE D N   1 
ATOM   14730 C  CA  . PHE D 1 59  ? 8.568   -22.332 101.787 1.00 17.63 ? 51   PHE D CA  1 
ATOM   14731 C  C   . PHE D 1 59  ? 9.712   -22.375 100.779 1.00 17.41 ? 51   PHE D C   1 
ATOM   14732 O  O   . PHE D 1 59  ? 9.729   -21.605 99.815  1.00 18.93 ? 51   PHE D O   1 
ATOM   14733 C  CB  . PHE D 1 59  ? 7.241   -22.724 101.129 1.00 17.51 ? 51   PHE D CB  1 
ATOM   14734 C  CG  . PHE D 1 59  ? 7.329   -23.945 100.273 1.00 19.81 ? 51   PHE D CG  1 
ATOM   14735 C  CD1 . PHE D 1 59  ? 7.930   -25.100 100.753 1.00 20.16 ? 51   PHE D CD1 1 
ATOM   14736 C  CD2 . PHE D 1 59  ? 6.811   -23.943 98.987  1.00 26.23 ? 51   PHE D CD2 1 
ATOM   14737 C  CE1 . PHE D 1 59  ? 8.024   -26.227 99.966  1.00 22.95 ? 51   PHE D CE1 1 
ATOM   14738 C  CE2 . PHE D 1 59  ? 6.896   -25.074 98.188  1.00 23.10 ? 51   PHE D CE2 1 
ATOM   14739 C  CZ  . PHE D 1 59  ? 7.502   -26.219 98.683  1.00 21.18 ? 51   PHE D CZ  1 
ATOM   14740 N  N   . TYR D 1 60  ? 10.657  -23.297 101.004 1.00 19.62 ? 52   TYR D N   1 
ATOM   14741 C  CA  . TYR D 1 60  ? 11.924  -23.287 100.275 1.00 21.88 ? 52   TYR D CA  1 
ATOM   14742 C  C   . TYR D 1 60  ? 11.727  -23.320 98.762  1.00 24.39 ? 52   TYR D C   1 
ATOM   14743 O  O   . TYR D 1 60  ? 12.464  -22.656 98.028  1.00 17.38 ? 52   TYR D O   1 
ATOM   14744 C  CB  . TYR D 1 60  ? 12.797  -24.474 100.692 1.00 19.41 ? 52   TYR D CB  1 
ATOM   14745 C  CG  . TYR D 1 60  ? 13.188  -24.535 102.149 1.00 20.18 ? 52   TYR D CG  1 
ATOM   14746 C  CD1 . TYR D 1 60  ? 13.314  -23.383 102.914 1.00 26.93 ? 52   TYR D CD1 1 
ATOM   14747 C  CD2 . TYR D 1 60  ? 13.454  -25.758 102.758 1.00 25.64 ? 52   TYR D CD2 1 
ATOM   14748 C  CE1 . TYR D 1 60  ? 13.685  -23.449 104.250 1.00 25.88 ? 52   TYR D CE1 1 
ATOM   14749 C  CE2 . TYR D 1 60  ? 13.823  -25.832 104.091 1.00 28.11 ? 52   TYR D CE2 1 
ATOM   14750 C  CZ  . TYR D 1 60  ? 13.931  -24.675 104.832 1.00 29.82 ? 52   TYR D CZ  1 
ATOM   14751 O  OH  . TYR D 1 60  ? 14.295  -24.740 106.161 1.00 31.64 ? 52   TYR D OH  1 
ATOM   14752 N  N   . ASN D 1 61  ? 10.773  -24.113 98.266  1.00 19.33 ? 53   ASN D N   1 
ATOM   14753 C  CA  . ASN D 1 61  ? 10.669  -24.345 96.828  1.00 22.32 ? 53   ASN D CA  1 
ATOM   14754 C  C   . ASN D 1 61  ? 9.531   -23.568 96.175  1.00 21.94 ? 53   ASN D C   1 
ATOM   14755 O  O   . ASN D 1 61  ? 9.112   -23.916 95.067  1.00 17.10 ? 53   ASN D O   1 
ATOM   14756 C  CB  . ASN D 1 61  ? 10.520  -25.835 96.520  1.00 20.08 ? 53   ASN D CB  1 
ATOM   14757 C  CG  . ASN D 1 61  ? 10.956  -26.170 95.100  1.00 20.86 ? 53   ASN D CG  1 
ATOM   14758 O  OD1 . ASN D 1 61  ? 11.977  -25.678 94.632  1.00 23.76 ? 53   ASN D OD1 1 
ATOM   14759 N  ND2 . ASN D 1 61  ? 10.177  -26.986 94.408  1.00 20.06 ? 53   ASN D ND2 1 
ATOM   14760 N  N   . ARG D 1 62  ? 9.037   -22.519 96.826  1.00 18.79 ? 54   ARG D N   1 
ATOM   14761 C  CA  . ARG D 1 62  ? 8.028   -21.666 96.216  1.00 19.51 ? 54   ARG D CA  1 
ATOM   14762 C  C   . ARG D 1 62  ? 8.584   -20.967 94.981  1.00 17.66 ? 54   ARG D C   1 
ATOM   14763 O  O   . ARG D 1 62  ? 9.768   -20.624 94.906  1.00 16.68 ? 54   ARG D O   1 
ATOM   14764 C  CB  . ARG D 1 62  ? 7.550   -20.615 97.219  1.00 16.12 ? 54   ARG D CB  1 
ATOM   14765 C  CG  . ARG D 1 62  ? 8.635   -19.570 97.560  1.00 14.87 ? 54   ARG D CG  1 
ATOM   14766 C  CD  . ARG D 1 62  ? 8.213   -18.630 98.690  1.00 14.50 ? 54   ARG D CD  1 
ATOM   14767 N  NE  . ARG D 1 62  ? 9.180   -17.556 98.886  1.00 16.79 ? 54   ARG D NE  1 
ATOM   14768 C  CZ  . ARG D 1 62  ? 10.328  -17.697 99.544  1.00 19.34 ? 54   ARG D CZ  1 
ATOM   14769 N  NH1 . ARG D 1 62  ? 10.656  -18.873 100.067 1.00 16.66 ? 54   ARG D NH1 1 
ATOM   14770 N  NH2 . ARG D 1 62  ? 11.153  -16.662 99.678  1.00 15.75 ? 54   ARG D NH2 1 
ATOM   14771 N  N   . ASP D 1 63  ? 7.720   -20.761 93.994  1.00 19.81 ? 55   ASP D N   1 
ATOM   14772 C  CA  . ASP D 1 63  ? 8.044   -19.797 92.957  1.00 21.18 ? 55   ASP D CA  1 
ATOM   14773 C  C   . ASP D 1 63  ? 8.270   -18.432 93.594  1.00 20.71 ? 55   ASP D C   1 
ATOM   14774 O  O   . ASP D 1 63  ? 7.633   -18.080 94.587  1.00 15.13 ? 55   ASP D O   1 
ATOM   14775 C  CB  . ASP D 1 63  ? 6.917   -19.702 91.926  1.00 18.13 ? 55   ASP D CB  1 
ATOM   14776 C  CG  . ASP D 1 63  ? 6.773   -20.958 91.095  1.00 18.19 ? 55   ASP D CG  1 
ATOM   14777 O  OD1 . ASP D 1 63  ? 7.774   -21.682 90.905  1.00 18.34 ? 55   ASP D OD1 1 
ATOM   14778 O  OD2 . ASP D 1 63  ? 5.654   -21.214 90.617  1.00 19.46 ? 55   ASP D OD2 1 
ATOM   14779 N  N   . ARG D 1 64  ? 9.198   -17.667 93.025  1.00 13.75 ? 56   ARG D N   1 
ATOM   14780 C  CA  . ARG D 1 64  ? 9.450   -16.298 93.449  1.00 15.57 ? 56   ARG D CA  1 
ATOM   14781 C  C   . ARG D 1 64  ? 8.749   -15.340 92.486  1.00 18.41 ? 56   ARG D C   1 
ATOM   14782 O  O   . ARG D 1 64  ? 8.892   -15.467 91.268  1.00 22.13 ? 56   ARG D O   1 
ATOM   14783 C  CB  . ARG D 1 64  ? 10.956  -16.015 93.498  1.00 16.74 ? 56   ARG D CB  1 
ATOM   14784 C  CG  . ARG D 1 64  ? 11.638  -16.247 94.859  1.00 19.26 ? 56   ARG D CG  1 
ATOM   14785 C  CD  . ARG D 1 64  ? 11.598  -17.703 95.322  1.00 18.84 ? 56   ARG D CD  1 
ATOM   14786 N  NE  . ARG D 1 64  ? 12.464  -17.969 96.480  1.00 18.20 ? 56   ARG D NE  1 
ATOM   14787 C  CZ  . ARG D 1 64  ? 12.644  -19.180 97.007  1.00 21.56 ? 56   ARG D CZ  1 
ATOM   14788 N  NH1 . ARG D 1 64  ? 12.017  -20.233 96.487  1.00 19.99 ? 56   ARG D NH1 1 
ATOM   14789 N  NH2 . ARG D 1 64  ? 13.453  -19.351 98.049  1.00 17.79 ? 56   ARG D NH2 1 
ATOM   14790 N  N   . PHE D 1 65  ? 7.971   -14.406 93.026  1.00 15.39 ? 57   PHE D N   1 
ATOM   14791 C  CA  . PHE D 1 65  ? 7.353   -13.345 92.234  1.00 15.42 ? 57   PHE D CA  1 
ATOM   14792 C  C   . PHE D 1 65  ? 7.941   -11.998 92.635  1.00 15.71 ? 57   PHE D C   1 
ATOM   14793 O  O   . PHE D 1 65  ? 8.066   -11.704 93.828  1.00 13.85 ? 57   PHE D O   1 
ATOM   14794 C  CB  . PHE D 1 65  ? 5.833   -13.315 92.430  1.00 13.61 ? 57   PHE D CB  1 
ATOM   14795 C  CG  . PHE D 1 65  ? 5.162   -12.142 91.770  1.00 15.46 ? 57   PHE D CG  1 
ATOM   14796 C  CD1 . PHE D 1 65  ? 4.929   -12.144 90.402  1.00 17.88 ? 57   PHE D CD1 1 
ATOM   14797 C  CD2 . PHE D 1 65  ? 4.770   -11.035 92.514  1.00 14.24 ? 57   PHE D CD2 1 
ATOM   14798 C  CE1 . PHE D 1 65  ? 4.316   -11.058 89.781  1.00 18.61 ? 57   PHE D CE1 1 
ATOM   14799 C  CE2 . PHE D 1 65  ? 4.164   -9.952  91.905  1.00 11.05 ? 57   PHE D CE2 1 
ATOM   14800 C  CZ  . PHE D 1 65  ? 3.932   -9.965  90.527  1.00 14.98 ? 57   PHE D CZ  1 
ATOM   14801 N  N   . VAL D 1 66  ? 8.265   -11.165 91.641  1.00 12.97 ? 58   VAL D N   1 
ATOM   14802 C  CA  . VAL D 1 66  ? 8.819   -9.834  91.869  1.00 14.10 ? 58   VAL D CA  1 
ATOM   14803 C  C   . VAL D 1 66  ? 8.017   -8.819  91.067  1.00 14.18 ? 58   VAL D C   1 
ATOM   14804 O  O   . VAL D 1 66  ? 7.885   -8.948  89.842  1.00 12.03 ? 58   VAL D O   1 
ATOM   14805 C  CB  . VAL D 1 66  ? 10.309  -9.751  91.498  1.00 14.49 ? 58   VAL D CB  1 
ATOM   14806 C  CG1 . VAL D 1 66  ? 10.817  -8.312  91.629  1.00 12.05 ? 58   VAL D CG1 1 
ATOM   14807 C  CG2 . VAL D 1 66  ? 11.094  -10.679 92.393  1.00 15.11 ? 58   VAL D CG2 1 
ATOM   14808 N  N   . LEU D 1 67  ? 7.481   -7.818  91.756  1.00 10.97 ? 59   LEU D N   1 
ATOM   14809 C  CA  . LEU D 1 67  ? 6.818   -6.687  91.110  1.00 12.23 ? 59   LEU D CA  1 
ATOM   14810 C  C   . LEU D 1 67  ? 7.884   -5.619  90.923  1.00 11.06 ? 59   LEU D C   1 
ATOM   14811 O  O   . LEU D 1 67  ? 8.156   -4.821  91.821  1.00 14.56 ? 59   LEU D O   1 
ATOM   14812 C  CB  . LEU D 1 67  ? 5.662   -6.185  91.964  1.00 14.98 ? 59   LEU D CB  1 
ATOM   14813 C  CG  . LEU D 1 67  ? 4.955   -4.930  91.442  1.00 17.03 ? 59   LEU D CG  1 
ATOM   14814 C  CD1 . LEU D 1 67  ? 4.204   -5.299  90.173  1.00 17.16 ? 59   LEU D CD1 1 
ATOM   14815 C  CD2 . LEU D 1 67  ? 4.007   -4.357  92.485  1.00 16.86 ? 59   LEU D CD2 1 
ATOM   14816 N  N   . SER D 1 68  ? 8.531   -5.611  89.757  1.00 15.59 ? 60   SER D N   1 
ATOM   14817 C  CA  . SER D 1 68  ? 9.641   -4.672  89.592  1.00 13.79 ? 60   SER D CA  1 
ATOM   14818 C  C   . SER D 1 68  ? 9.134   -3.239  89.560  1.00 17.10 ? 60   SER D C   1 
ATOM   14819 O  O   . SER D 1 68  ? 9.797   -2.333  90.080  1.00 19.75 ? 60   SER D O   1 
ATOM   14820 C  CB  . SER D 1 68  ? 10.454  -4.987  88.336  1.00 12.50 ? 60   SER D CB  1 
ATOM   14821 O  OG  . SER D 1 68  ? 11.684  -4.254  88.367  1.00 18.28 ? 60   SER D OG  1 
ATOM   14822 N  N   . ASN D 1 69  ? 7.961   -3.009  88.963  1.00 16.09 ? 61   ASN D N   1 
ATOM   14823 C  CA  . ASN D 1 69  ? 7.389   -1.658  88.917  1.00 21.41 ? 61   ASN D CA  1 
ATOM   14824 C  C   . ASN D 1 69  ? 6.677   -1.390  90.245  1.00 24.31 ? 61   ASN D C   1 
ATOM   14825 O  O   . ASN D 1 69  ? 5.449   -1.372  90.344  1.00 25.85 ? 61   ASN D O   1 
ATOM   14826 C  CB  . ASN D 1 69  ? 6.468   -1.479  87.708  1.00 18.18 ? 61   ASN D CB  1 
ATOM   14827 C  CG  . ASN D 1 69  ? 5.736   -2.761  87.298  1.00 18.43 ? 61   ASN D CG  1 
ATOM   14828 O  OD1 . ASN D 1 69  ? 5.835   -3.797  87.951  1.00 23.13 ? 61   ASN D OD1 1 
ATOM   14829 N  ND2 . ASN D 1 69  ? 4.994   -2.683  86.202  1.00 20.77 ? 61   ASN D ND2 1 
ATOM   14830 N  N   . GLY D 1 70  ? 7.492   -1.134  91.280  1.00 23.41 ? 62   GLY D N   1 
ATOM   14831 C  CA  . GLY D 1 70  ? 7.055   -1.127  92.672  1.00 27.56 ? 62   GLY D CA  1 
ATOM   14832 C  C   . GLY D 1 70  ? 6.000   -0.097  93.032  1.00 23.40 ? 62   GLY D C   1 
ATOM   14833 O  O   . GLY D 1 70  ? 5.322   -0.256  94.052  1.00 20.28 ? 62   GLY D O   1 
ATOM   14834 N  N   . HIS D 1 71  ? 5.856   0.967   92.241  1.00 15.98 ? 63   HIS D N   1 
ATOM   14835 C  CA  . HIS D 1 71  ? 4.773   1.923   92.480  1.00 22.54 ? 63   HIS D CA  1 
ATOM   14836 C  C   . HIS D 1 71  ? 3.398   1.276   92.358  1.00 22.53 ? 63   HIS D C   1 
ATOM   14837 O  O   . HIS D 1 71  ? 2.434   1.746   92.976  1.00 20.51 ? 63   HIS D O   1 
ATOM   14838 C  CB  . HIS D 1 71  ? 4.889   3.090   91.498  1.00 21.90 ? 63   HIS D CB  1 
ATOM   14839 C  CG  . HIS D 1 71  ? 5.073   2.652   90.080  1.00 25.38 ? 63   HIS D CG  1 
ATOM   14840 N  ND1 . HIS D 1 71  ? 6.313   2.366   89.547  1.00 28.57 ? 63   HIS D ND1 1 
ATOM   14841 C  CD2 . HIS D 1 71  ? 4.177   2.434   89.089  1.00 27.61 ? 63   HIS D CD2 1 
ATOM   14842 C  CE1 . HIS D 1 71  ? 6.172   1.995   88.286  1.00 27.49 ? 63   HIS D CE1 1 
ATOM   14843 N  NE2 . HIS D 1 71  ? 4.886   2.025   87.985  1.00 25.08 ? 63   HIS D NE2 1 
ATOM   14844 N  N   . ALA D 1 72  ? 3.280   0.209   91.567  1.00 18.69 ? 64   ALA D N   1 
ATOM   14845 C  CA  . ALA D 1 72  ? 2.030   -0.535  91.442  1.00 16.87 ? 64   ALA D CA  1 
ATOM   14846 C  C   . ALA D 1 72  ? 1.770   -1.418  92.661  1.00 16.95 ? 64   ALA D C   1 
ATOM   14847 O  O   . ALA D 1 72  ? 1.184   -2.500  92.542  1.00 16.69 ? 64   ALA D O   1 
ATOM   14848 C  CB  . ALA D 1 72  ? 2.061   -1.382  90.164  1.00 13.28 ? 64   ALA D CB  1 
ATOM   14849 N  N   . SER D 1 73  ? 2.161   -0.936  93.842  1.00 10.78 ? 65   SER D N   1 
ATOM   14850 C  CA  . SER D 1 73  ? 2.145   -1.754  95.055  1.00 10.37 ? 65   SER D CA  1 
ATOM   14851 C  C   . SER D 1 73  ? 0.786   -2.382  95.347  1.00 14.96 ? 65   SER D C   1 
ATOM   14852 O  O   . SER D 1 73  ? 0.718   -3.497  95.882  1.00 13.86 ? 65   SER D O   1 
ATOM   14853 C  CB  . SER D 1 73  ? 2.586   -0.904  96.239  1.00 14.52 ? 65   SER D CB  1 
ATOM   14854 O  OG  . SER D 1 73  ? 1.829   0.289   96.314  1.00 16.33 ? 65   SER D OG  1 
ATOM   14855 N  N   . MET D 1 74  ? -0.312  -1.674  95.043  1.00 15.45 ? 66   MET D N   1 
ATOM   14856 C  CA  . MET D 1 74  ? -1.623  -2.209  95.394  1.00 15.36 ? 66   MET D CA  1 
ATOM   14857 C  C   . MET D 1 74  ? -1.965  -3.452  94.594  1.00 16.24 ? 66   MET D C   1 
ATOM   14858 O  O   . MET D 1 74  ? -2.800  -4.240  95.038  1.00 16.57 ? 66   MET D O   1 
ATOM   14859 C  CB  . MET D 1 74  ? -2.718  -1.156  95.219  1.00 14.02 ? 66   MET D CB  1 
ATOM   14860 C  CG  . MET D 1 74  ? -2.974  -0.310  96.484  1.00 15.91 ? 66   MET D CG  1 
ATOM   14861 S  SD  . MET D 1 74  ? -3.283  -1.222  98.035  1.00 16.01 ? 66   MET D SD  1 
ATOM   14862 C  CE  . MET D 1 74  ? -4.606  -2.337  97.546  1.00 13.00 ? 66   MET D CE  1 
ATOM   14863 N  N   . LEU D 1 75  ? -1.324  -3.662  93.446  1.00 12.09 ? 67   LEU D N   1 
ATOM   14864 C  CA  . LEU D 1 75  ? -1.493  -4.930  92.749  1.00 13.49 ? 67   LEU D CA  1 
ATOM   14865 C  C   . LEU D 1 75  ? -1.024  -6.076  93.632  1.00 14.55 ? 67   LEU D C   1 
ATOM   14866 O  O   . LEU D 1 75  ? -1.749  -7.052  93.852  1.00 14.02 ? 67   LEU D O   1 
ATOM   14867 C  CB  . LEU D 1 75  ? -0.720  -4.906  91.428  1.00 12.13 ? 67   LEU D CB  1 
ATOM   14868 C  CG  . LEU D 1 75  ? -0.749  -6.204  90.618  1.00 19.08 ? 67   LEU D CG  1 
ATOM   14869 C  CD1 . LEU D 1 75  ? -2.163  -6.501  90.187  1.00 22.43 ? 67   LEU D CD1 1 
ATOM   14870 C  CD2 . LEU D 1 75  ? 0.179   -6.124  89.395  1.00 17.52 ? 67   LEU D CD2 1 
ATOM   14871 N  N   . LEU D 1 76  ? 0.170   -5.938  94.204  1.00 11.78 ? 68   LEU D N   1 
ATOM   14872 C  CA  . LEU D 1 76  ? 0.712   -6.998  95.040  1.00 14.50 ? 68   LEU D CA  1 
ATOM   14873 C  C   . LEU D 1 76  ? -0.084  -7.142  96.331  1.00 15.33 ? 68   LEU D C   1 
ATOM   14874 O  O   . LEU D 1 76  ? -0.405  -8.264  96.746  1.00 12.48 ? 68   LEU D O   1 
ATOM   14875 C  CB  . LEU D 1 76  ? 2.191   -6.711  95.325  1.00 12.45 ? 68   LEU D CB  1 
ATOM   14876 C  CG  . LEU D 1 76  ? 2.929   -7.756  96.154  1.00 14.64 ? 68   LEU D CG  1 
ATOM   14877 C  CD1 . LEU D 1 76  ? 2.793   -9.137  95.503  1.00 19.00 ? 68   LEU D CD1 1 
ATOM   14878 C  CD2 . LEU D 1 76  ? 4.405   -7.349  96.328  1.00 12.91 ? 68   LEU D CD2 1 
ATOM   14879 N  N   . TYR D 1 77  ? -0.421  -6.026  96.984  1.00 12.35 ? 69   TYR D N   1 
ATOM   14880 C  CA  . TYR D 1 77  ? -1.203  -6.130  98.216  1.00 11.72 ? 69   TYR D CA  1 
ATOM   14881 C  C   . TYR D 1 77  ? -2.544  -6.811  97.956  1.00 14.13 ? 69   TYR D C   1 
ATOM   14882 O  O   . TYR D 1 77  ? -3.003  -7.623  98.768  1.00 15.83 ? 69   TYR D O   1 
ATOM   14883 C  CB  . TYR D 1 77  ? -1.402  -4.750  98.837  1.00 11.31 ? 69   TYR D CB  1 
ATOM   14884 C  CG  . TYR D 1 77  ? -0.106  -4.085  99.292  1.00 10.75 ? 69   TYR D CG  1 
ATOM   14885 C  CD1 . TYR D 1 77  ? 0.975   -4.846  99.746  1.00 14.79 ? 69   TYR D CD1 1 
ATOM   14886 C  CD2 . TYR D 1 77  ? 0.033   -2.707  99.252  1.00 14.36 ? 69   TYR D CD2 1 
ATOM   14887 C  CE1 . TYR D 1 77  ? 2.161   -4.233  100.166 1.00 15.55 ? 69   TYR D CE1 1 
ATOM   14888 C  CE2 . TYR D 1 77  ? 1.209   -2.082  99.656  1.00 13.91 ? 69   TYR D CE2 1 
ATOM   14889 C  CZ  . TYR D 1 77  ? 2.267   -2.850  100.126 1.00 13.98 ? 69   TYR D CZ  1 
ATOM   14890 O  OH  . TYR D 1 77  ? 3.417   -2.219  100.532 1.00 15.10 ? 69   TYR D OH  1 
ATOM   14891 N  N   . SER D 1 78  ? -3.178  -6.507  96.821  1.00 14.91 ? 70   SER D N   1 
ATOM   14892 C  CA  . SER D 1 78  ? -4.420  -7.195  96.462  1.00 16.86 ? 70   SER D CA  1 
ATOM   14893 C  C   . SER D 1 78  ? -4.199  -8.697  96.338  1.00 16.57 ? 70   SER D C   1 
ATOM   14894 O  O   . SER D 1 78  ? -4.969  -9.493  96.882  1.00 16.42 ? 70   SER D O   1 
ATOM   14895 C  CB  . SER D 1 78  ? -4.985  -6.639  95.152  1.00 18.82 ? 70   SER D CB  1 
ATOM   14896 O  OG  . SER D 1 78  ? -5.393  -5.294  95.295  1.00 17.58 ? 70   SER D OG  1 
ATOM   14897 N  N   . LEU D 1 79  ? -3.145  -9.103  95.620  1.00 16.07 ? 71   LEU D N   1 
ATOM   14898 C  CA  . LEU D 1 79  ? -2.904  -10.529 95.401  1.00 15.31 ? 71   LEU D CA  1 
ATOM   14899 C  C   . LEU D 1 79  ? -2.626  -11.254 96.715  1.00 18.39 ? 71   LEU D C   1 
ATOM   14900 O  O   . LEU D 1 79  ? -3.097  -12.376 96.924  1.00 19.25 ? 71   LEU D O   1 
ATOM   14901 C  CB  . LEU D 1 79  ? -1.746  -10.717 94.418  1.00 15.52 ? 71   LEU D CB  1 
ATOM   14902 C  CG  . LEU D 1 79  ? -2.034  -10.272 92.973  1.00 15.44 ? 71   LEU D CG  1 
ATOM   14903 C  CD1 . LEU D 1 79  ? -0.752  -10.104 92.167  1.00 17.32 ? 71   LEU D CD1 1 
ATOM   14904 C  CD2 . LEU D 1 79  ? -2.990  -11.248 92.289  1.00 18.76 ? 71   LEU D CD2 1 
ATOM   14905 N  N   . LEU D 1 80  ? -1.871  -10.621 97.619  1.00 15.95 ? 72   LEU D N   1 
ATOM   14906 C  CA  . LEU D 1 80  ? -1.541  -11.265 98.892  1.00 17.89 ? 72   LEU D CA  1 
ATOM   14907 C  C   . LEU D 1 80  ? -2.773  -11.423 99.772  1.00 16.86 ? 72   LEU D C   1 
ATOM   14908 O  O   . LEU D 1 80  ? -2.974  -12.475 100.393 1.00 17.70 ? 72   LEU D O   1 
ATOM   14909 C  CB  . LEU D 1 80  ? -0.472  -10.454 99.621  1.00 17.17 ? 72   LEU D CB  1 
ATOM   14910 C  CG  . LEU D 1 80  ? 0.892   -10.443 98.926  1.00 16.71 ? 72   LEU D CG  1 
ATOM   14911 C  CD1 . LEU D 1 80  ? 1.797   -9.430  99.565  1.00 15.46 ? 72   LEU D CD1 1 
ATOM   14912 C  CD2 . LEU D 1 80  ? 1.522   -11.829 98.967  1.00 15.63 ? 72   LEU D CD2 1 
ATOM   14913 N  N   . HIS D 1 81  ? -3.604  -10.382 99.844  1.00 15.66 ? 73   HIS D N   1 
ATOM   14914 C  CA  . HIS D 1 81  ? -4.830  -10.478 100.618 1.00 16.70 ? 73   HIS D CA  1 
ATOM   14915 C  C   . HIS D 1 81  ? -5.757  -11.537 100.034 1.00 18.10 ? 73   HIS D C   1 
ATOM   14916 O  O   . HIS D 1 81  ? -6.301  -12.379 100.760 1.00 17.25 ? 73   HIS D O   1 
ATOM   14917 C  CB  . HIS D 1 81  ? -5.535  -9.118  100.660 1.00 17.18 ? 73   HIS D CB  1 
ATOM   14918 C  CG  . HIS D 1 81  ? -6.905  -9.190  101.251 1.00 20.11 ? 73   HIS D CG  1 
ATOM   14919 N  ND1 . HIS D 1 81  ? -7.119  -9.407  102.595 1.00 19.31 ? 73   HIS D ND1 1 
ATOM   14920 C  CD2 . HIS D 1 81  ? -8.130  -9.123  100.678 1.00 17.23 ? 73   HIS D CD2 1 
ATOM   14921 C  CE1 . HIS D 1 81  ? -8.421  -9.452  102.828 1.00 20.89 ? 73   HIS D CE1 1 
ATOM   14922 N  NE2 . HIS D 1 81  ? -9.056  -9.283  101.682 1.00 17.65 ? 73   HIS D NE2 1 
ATOM   14923 N  N   . LEU D 1 82  ? -5.944  -11.514 98.711  1.00 19.11 ? 74   LEU D N   1 
ATOM   14924 C  CA  . LEU D 1 82  ? -6.936  -12.398 98.099  1.00 20.06 ? 74   LEU D CA  1 
ATOM   14925 C  C   . LEU D 1 82  ? -6.515  -13.860 98.184  1.00 19.28 ? 74   LEU D C   1 
ATOM   14926 O  O   . LEU D 1 82  ? -7.371  -14.737 98.342  1.00 21.85 ? 74   LEU D O   1 
ATOM   14927 C  CB  . LEU D 1 82  ? -7.180  -11.999 96.640  1.00 16.04 ? 74   LEU D CB  1 
ATOM   14928 C  CG  . LEU D 1 82  ? -7.912  -10.682 96.349  1.00 20.78 ? 74   LEU D CG  1 
ATOM   14929 C  CD1 . LEU D 1 82  ? -7.537  -10.141 94.963  1.00 20.47 ? 74   LEU D CD1 1 
ATOM   14930 C  CD2 . LEU D 1 82  ? -9.425  -10.876 96.455  1.00 26.78 ? 74   LEU D CD2 1 
ATOM   14931 N  N   . THR D 1 83  ? -5.214  -14.148 98.094  1.00 18.88 ? 75   THR D N   1 
ATOM   14932 C  CA  . THR D 1 83  ? -4.793  -15.540 98.084  1.00 20.40 ? 75   THR D CA  1 
ATOM   14933 C  C   . THR D 1 83  ? -4.656  -16.118 99.481  1.00 20.89 ? 75   THR D C   1 
ATOM   14934 O  O   . THR D 1 83  ? -4.454  -17.327 99.613  1.00 21.62 ? 75   THR D O   1 
ATOM   14935 C  CB  . THR D 1 83  ? -3.483  -15.708 97.303  1.00 18.62 ? 75   THR D CB  1 
ATOM   14936 O  OG1 . THR D 1 83  ? -2.462  -14.873 97.864  1.00 14.99 ? 75   THR D OG1 1 
ATOM   14937 C  CG2 . THR D 1 83  ? -3.704  -15.342 95.832  1.00 20.15 ? 75   THR D CG2 1 
ATOM   14938 N  N   . GLY D 1 84  ? -4.773  -15.298 100.520 1.00 16.81 ? 76   GLY D N   1 
ATOM   14939 C  CA  . GLY D 1 84  ? -4.850  -15.800 101.875 1.00 17.28 ? 76   GLY D CA  1 
ATOM   14940 C  C   . GLY D 1 84  ? -3.643  -15.525 102.747 1.00 16.06 ? 76   GLY D C   1 
ATOM   14941 O  O   . GLY D 1 84  ? -3.520  -16.148 103.803 1.00 19.01 ? 76   GLY D O   1 
ATOM   14942 N  N   . TYR D 1 85  ? -2.744  -14.635 102.338 1.00 15.20 ? 77   TYR D N   1 
ATOM   14943 C  CA  . TYR D 1 85  ? -1.645  -14.249 103.211 1.00 18.20 ? 77   TYR D CA  1 
ATOM   14944 C  C   . TYR D 1 85  ? -2.165  -13.427 104.390 1.00 24.93 ? 77   TYR D C   1 
ATOM   14945 O  O   . TYR D 1 85  ? -3.319  -12.975 104.417 1.00 17.40 ? 77   TYR D O   1 
ATOM   14946 C  CB  . TYR D 1 85  ? -0.592  -13.456 102.438 1.00 20.61 ? 77   TYR D CB  1 
ATOM   14947 C  CG  . TYR D 1 85  ? 0.213   -14.296 101.470 1.00 17.89 ? 77   TYR D CG  1 
ATOM   14948 C  CD1 . TYR D 1 85  ? -0.306  -14.646 100.231 1.00 16.04 ? 77   TYR D CD1 1 
ATOM   14949 C  CD2 . TYR D 1 85  ? 1.496   -14.728 101.794 1.00 19.86 ? 77   TYR D CD2 1 
ATOM   14950 C  CE1 . TYR D 1 85  ? 0.419   -15.428 99.347  1.00 17.12 ? 77   TYR D CE1 1 
ATOM   14951 C  CE2 . TYR D 1 85  ? 2.232   -15.502 100.916 1.00 23.69 ? 77   TYR D CE2 1 
ATOM   14952 C  CZ  . TYR D 1 85  ? 1.689   -15.845 99.692  1.00 24.08 ? 77   TYR D CZ  1 
ATOM   14953 O  OH  . TYR D 1 85  ? 2.414   -16.608 98.805  1.00 27.93 ? 77   TYR D OH  1 
ATOM   14954 N  N   . ASN D 1 86  ? -1.279  -13.216 105.368 1.00 19.06 ? 78   ASN D N   1 
ATOM   14955 C  CA  . ASN D 1 86  ? -1.608  -12.460 106.572 1.00 21.11 ? 78   ASN D CA  1 
ATOM   14956 C  C   . ASN D 1 86  ? -1.596  -10.960 106.288 1.00 29.06 ? 78   ASN D C   1 
ATOM   14957 O  O   . ASN D 1 86  ? -0.895  -10.189 106.951 1.00 25.18 ? 78   ASN D O   1 
ATOM   14958 C  CB  . ASN D 1 86  ? -0.626  -12.807 107.704 1.00 24.79 ? 78   ASN D CB  1 
ATOM   14959 C  CG  . ASN D 1 86  ? -1.075  -12.277 109.051 1.00 36.57 ? 78   ASN D CG  1 
ATOM   14960 O  OD1 . ASN D 1 86  ? -2.159  -11.704 109.180 1.00 44.63 ? 78   ASN D OD1 1 
ATOM   14961 N  ND2 . ASN D 1 86  ? -0.245  -12.474 110.069 1.00 40.35 ? 78   ASN D ND2 1 
ATOM   14962 N  N   . LEU D 1 87  ? -2.362  -10.543 105.290 1.00 23.32 ? 79   LEU D N   1 
ATOM   14963 C  CA  . LEU D 1 87  ? -2.539  -9.138  104.953 1.00 16.84 ? 79   LEU D CA  1 
ATOM   14964 C  C   . LEU D 1 87  ? -4.041  -8.921  104.867 1.00 17.73 ? 79   LEU D C   1 
ATOM   14965 O  O   . LEU D 1 87  ? -4.706  -9.515  104.009 1.00 19.53 ? 79   LEU D O   1 
ATOM   14966 C  CB  . LEU D 1 87  ? -1.846  -8.787  103.638 1.00 14.91 ? 79   LEU D CB  1 
ATOM   14967 C  CG  . LEU D 1 87  ? -1.686  -7.304  103.317 1.00 19.31 ? 79   LEU D CG  1 
ATOM   14968 C  CD1 . LEU D 1 87  ? -0.778  -6.629  104.341 1.00 15.63 ? 79   LEU D CD1 1 
ATOM   14969 C  CD2 . LEU D 1 87  ? -1.143  -7.121  101.890 1.00 14.55 ? 79   LEU D CD2 1 
ATOM   14970 N  N   . SER D 1 88  ? -4.581  -8.104  105.761 1.00 16.87 ? 80   SER D N   1 
ATOM   14971 C  CA  . SER D 1 88  ? -6.022  -8.051  105.965 1.00 16.47 ? 80   SER D CA  1 
ATOM   14972 C  C   . SER D 1 88  ? -6.638  -6.868  105.238 1.00 16.00 ? 80   SER D C   1 
ATOM   14973 O  O   . SER D 1 88  ? -5.942  -6.002  104.700 1.00 14.69 ? 80   SER D O   1 
ATOM   14974 C  CB  . SER D 1 88  ? -6.353  -7.954  107.457 1.00 17.58 ? 80   SER D CB  1 
ATOM   14975 O  OG  . SER D 1 88  ? -5.985  -6.675  107.956 1.00 21.47 ? 80   SER D OG  1 
ATOM   14976 N  N   . ILE D 1 89  ? -7.975  -6.829  105.265 1.00 16.44 ? 81   ILE D N   1 
ATOM   14977 C  CA  . ILE D 1 89  ? -8.692  -5.669  104.746 1.00 19.16 ? 81   ILE D CA  1 
ATOM   14978 C  C   . ILE D 1 89  ? -8.292  -4.415  105.511 1.00 20.95 ? 81   ILE D C   1 
ATOM   14979 O  O   . ILE D 1 89  ? -8.087  -3.349  104.918 1.00 18.84 ? 81   ILE D O   1 
ATOM   14980 C  CB  . ILE D 1 89  ? -10.212 -5.908  104.798 1.00 22.39 ? 81   ILE D CB  1 
ATOM   14981 C  CG1 . ILE D 1 89  ? -10.654 -6.769  103.611 1.00 22.86 ? 81   ILE D CG1 1 
ATOM   14982 C  CG2 . ILE D 1 89  ? -10.966 -4.583  104.832 1.00 21.06 ? 81   ILE D CG2 1 
ATOM   14983 C  CD1 . ILE D 1 89  ? -10.311 -6.163  102.262 1.00 16.01 ? 81   ILE D CD1 1 
ATOM   14984 N  N   . GLU D 1 90  ? -8.168  -4.520  106.838 1.00 19.60 ? 82   GLU D N   1 
ATOM   14985 C  CA  . GLU D 1 90  ? -7.736  -3.361  107.614 1.00 22.12 ? 82   GLU D CA  1 
ATOM   14986 C  C   . GLU D 1 90  ? -6.341  -2.901  107.189 1.00 16.44 ? 82   GLU D C   1 
ATOM   14987 O  O   . GLU D 1 90  ? -6.069  -1.694  107.122 1.00 20.60 ? 82   GLU D O   1 
ATOM   14988 C  CB  . GLU D 1 90  ? -7.776  -3.686  109.109 1.00 25.02 ? 82   GLU D CB  1 
ATOM   14989 C  CG  . GLU D 1 90  ? -7.433  -2.507  110.018 1.00 39.23 ? 82   GLU D CG  1 
ATOM   14990 C  CD  . GLU D 1 90  ? -8.455  -1.376  109.948 1.00 49.16 ? 82   GLU D CD  1 
ATOM   14991 O  OE1 . GLU D 1 90  ? -9.657  -1.653  109.726 1.00 50.63 ? 82   GLU D OE1 1 
ATOM   14992 O  OE2 . GLU D 1 90  ? -8.048  -0.205  110.114 1.00 51.86 ? 82   GLU D OE2 1 
ATOM   14993 N  N   . ASP D 1 91  ? -5.441  -3.847  106.893 1.00 16.91 ? 83   ASP D N   1 
ATOM   14994 C  CA  . ASP D 1 91  ? -4.142  -3.481  106.342 1.00 16.22 ? 83   ASP D CA  1 
ATOM   14995 C  C   . ASP D 1 91  ? -4.305  -2.691  105.046 1.00 17.14 ? 83   ASP D C   1 
ATOM   14996 O  O   . ASP D 1 91  ? -3.658  -1.654  104.853 1.00 16.38 ? 83   ASP D O   1 
ATOM   14997 C  CB  . ASP D 1 91  ? -3.285  -4.731  106.107 1.00 16.18 ? 83   ASP D CB  1 
ATOM   14998 C  CG  . ASP D 1 91  ? -2.844  -5.390  107.391 1.00 20.16 ? 83   ASP D CG  1 
ATOM   14999 O  OD1 . ASP D 1 91  ? -2.603  -4.672  108.379 1.00 23.10 ? 83   ASP D OD1 1 
ATOM   15000 O  OD2 . ASP D 1 91  ? -2.723  -6.631  107.410 1.00 18.90 ? 83   ASP D OD2 1 
ATOM   15001 N  N   . LEU D 1 92  ? -5.184  -3.157  104.144 1.00 15.41 ? 84   LEU D N   1 
ATOM   15002 C  CA  . LEU D 1 92  ? -5.369  -2.438  102.884 1.00 14.88 ? 84   LEU D CA  1 
ATOM   15003 C  C   . LEU D 1 92  ? -5.954  -1.053  103.123 1.00 19.27 ? 84   LEU D C   1 
ATOM   15004 O  O   . LEU D 1 92  ? -5.603  -0.093  102.422 1.00 17.19 ? 84   LEU D O   1 
ATOM   15005 C  CB  . LEU D 1 92  ? -6.258  -3.233  101.932 1.00 19.05 ? 84   LEU D CB  1 
ATOM   15006 C  CG  . LEU D 1 92  ? -5.773  -4.637  101.559 1.00 21.34 ? 84   LEU D CG  1 
ATOM   15007 C  CD1 . LEU D 1 92  ? -6.715  -5.256  100.538 1.00 21.87 ? 84   LEU D CD1 1 
ATOM   15008 C  CD2 . LEU D 1 92  ? -4.350  -4.633  101.035 1.00 16.26 ? 84   LEU D CD2 1 
ATOM   15009 N  N   . LYS D 1 93  ? -6.844  -0.931  104.111 1.00 17.22 ? 85   LYS D N   1 
ATOM   15010 C  CA  . LYS D 1 93  ? -7.405  0.368   104.460 1.00 14.64 ? 85   LYS D CA  1 
ATOM   15011 C  C   . LYS D 1 93  ? -6.368  1.312   105.060 1.00 21.37 ? 85   LYS D C   1 
ATOM   15012 O  O   . LYS D 1 93  ? -6.661  2.498   105.227 1.00 19.45 ? 85   LYS D O   1 
ATOM   15013 C  CB  . LYS D 1 93  ? -8.558  0.196   105.441 1.00 15.69 ? 85   LYS D CB  1 
ATOM   15014 C  CG  . LYS D 1 93  ? -9.806  -0.447  104.850 1.00 17.97 ? 85   LYS D CG  1 
ATOM   15015 C  CD  . LYS D 1 93  ? -10.862 -0.617  105.932 1.00 23.05 ? 85   LYS D CD  1 
ATOM   15016 C  CE  . LYS D 1 93  ? -12.190 -1.050  105.358 1.00 27.92 ? 85   LYS D CE  1 
ATOM   15017 N  NZ  . LYS D 1 93  ? -13.215 -1.221  106.441 1.00 29.65 ? 85   LYS D NZ  1 
ATOM   15018 N  N   . ASN D 1 94  ? -5.171  0.827   105.391 1.00 19.09 ? 86   ASN D N   1 
ATOM   15019 C  CA  . ASN D 1 94  ? -4.112  1.694   105.891 1.00 15.69 ? 86   ASN D CA  1 
ATOM   15020 C  C   . ASN D 1 94  ? -2.937  1.772   104.921 1.00 16.01 ? 86   ASN D C   1 
ATOM   15021 O  O   . ASN D 1 94  ? -1.804  2.038   105.322 1.00 15.54 ? 86   ASN D O   1 
ATOM   15022 C  CB  . ASN D 1 94  ? -3.688  1.252   107.285 1.00 22.06 ? 86   ASN D CB  1 
ATOM   15023 C  CG  . ASN D 1 94  ? -4.719  1.648   108.328 1.00 23.96 ? 86   ASN D CG  1 
ATOM   15024 O  OD1 . ASN D 1 94  ? -4.711  2.778   108.823 1.00 30.26 ? 86   ASN D OD1 1 
ATOM   15025 N  ND2 . ASN D 1 94  ? -5.643  0.750   108.617 1.00 24.15 ? 86   ASN D ND2 1 
ATOM   15026 N  N   . PHE D 1 95  ? -3.228  1.568   103.637 1.00 16.59 ? 87   PHE D N   1 
ATOM   15027 C  CA  . PHE D 1 95  ? -2.285  1.829   102.563 1.00 12.24 ? 87   PHE D CA  1 
ATOM   15028 C  C   . PHE D 1 95  ? -1.631  3.194   102.750 1.00 15.14 ? 87   PHE D C   1 
ATOM   15029 O  O   . PHE D 1 95  ? -2.314  4.203   102.939 1.00 14.54 ? 87   PHE D O   1 
ATOM   15030 C  CB  . PHE D 1 95  ? -3.026  1.760   101.224 1.00 11.94 ? 87   PHE D CB  1 
ATOM   15031 C  CG  . PHE D 1 95  ? -2.147  1.983   100.020 1.00 13.71 ? 87   PHE D CG  1 
ATOM   15032 C  CD1 . PHE D 1 95  ? -1.025  1.198   99.812  1.00 11.47 ? 87   PHE D CD1 1 
ATOM   15033 C  CD2 . PHE D 1 95  ? -2.475  2.940   99.075  1.00 16.47 ? 87   PHE D CD2 1 
ATOM   15034 C  CE1 . PHE D 1 95  ? -0.224  1.379   98.691  1.00 13.94 ? 87   PHE D CE1 1 
ATOM   15035 C  CE2 . PHE D 1 95  ? -1.689  3.122   97.943  1.00 14.12 ? 87   PHE D CE2 1 
ATOM   15036 C  CZ  . PHE D 1 95  ? -0.547  2.351   97.760  1.00 14.15 ? 87   PHE D CZ  1 
ATOM   15037 N  N   . ARG D 1 96  ? -0.296  3.208   102.746 1.00 16.20 ? 88   ARG D N   1 
ATOM   15038 C  CA  . ARG D 1 96  ? 0.506   4.433   102.774 1.00 14.95 ? 88   ARG D CA  1 
ATOM   15039 C  C   . ARG D 1 96  ? 0.383   5.202   104.082 1.00 14.53 ? 88   ARG D C   1 
ATOM   15040 O  O   . ARG D 1 96  ? 0.720   6.390   104.133 1.00 17.06 ? 88   ARG D O   1 
ATOM   15041 C  CB  . ARG D 1 96  ? 0.164   5.349   101.584 1.00 12.21 ? 88   ARG D CB  1 
ATOM   15042 C  CG  . ARG D 1 96  ? 0.772   4.828   100.285 1.00 12.54 ? 88   ARG D CG  1 
ATOM   15043 C  CD  . ARG D 1 96  ? 0.381   5.597   99.004  1.00 18.43 ? 88   ARG D CD  1 
ATOM   15044 N  NE  . ARG D 1 96  ? 1.278   5.142   97.948  1.00 16.04 ? 88   ARG D NE  1 
ATOM   15045 C  CZ  . ARG D 1 96  ? 2.230   5.883   97.393  1.00 20.18 ? 88   ARG D CZ  1 
ATOM   15046 N  NH1 . ARG D 1 96  ? 2.360   7.157   97.731  1.00 21.59 ? 88   ARG D NH1 1 
ATOM   15047 N  NH2 . ARG D 1 96  ? 3.039   5.352   96.483  1.00 20.70 ? 88   ARG D NH2 1 
ATOM   15048 N  N   . GLN D 1 97  ? -0.060  4.551   105.155 1.00 13.54 ? 89   GLN D N   1 
ATOM   15049 C  CA  . GLN D 1 97  ? -0.161  5.194   106.453 1.00 16.02 ? 89   GLN D CA  1 
ATOM   15050 C  C   . GLN D 1 97  ? 0.984   4.746   107.353 1.00 15.99 ? 89   GLN D C   1 
ATOM   15051 O  O   . GLN D 1 97  ? 1.553   3.663   107.176 1.00 16.53 ? 89   GLN D O   1 
ATOM   15052 C  CB  . GLN D 1 97  ? -1.510  4.891   107.113 1.00 17.77 ? 89   GLN D CB  1 
ATOM   15053 C  CG  . GLN D 1 97  ? -2.703  5.283   106.236 1.00 16.66 ? 89   GLN D CG  1 
ATOM   15054 C  CD  . GLN D 1 97  ? -2.608  6.704   105.718 1.00 22.59 ? 89   GLN D CD  1 
ATOM   15055 O  OE1 . GLN D 1 97  ? -2.589  7.667   106.493 1.00 23.99 ? 89   GLN D OE1 1 
ATOM   15056 N  NE2 . GLN D 1 97  ? -2.541  6.845   104.399 1.00 17.52 ? 89   GLN D NE2 1 
ATOM   15057 N  N   . LEU D 1 98  ? 1.322   5.606   108.316 1.00 16.65 ? 90   LEU D N   1 
ATOM   15058 C  CA  . LEU D 1 98  ? 2.493   5.391   109.155 1.00 20.20 ? 90   LEU D CA  1 
ATOM   15059 C  C   . LEU D 1 98  ? 2.495   4.002   109.777 1.00 19.54 ? 90   LEU D C   1 
ATOM   15060 O  O   . LEU D 1 98  ? 1.530   3.598   110.433 1.00 17.20 ? 90   LEU D O   1 
ATOM   15061 C  CB  . LEU D 1 98  ? 2.549   6.444   110.264 1.00 21.96 ? 90   LEU D CB  1 
ATOM   15062 C  CG  . LEU D 1 98  ? 3.840   6.319   111.079 1.00 18.21 ? 90   LEU D CG  1 
ATOM   15063 C  CD1 . LEU D 1 98  ? 5.036   6.742   110.236 1.00 22.10 ? 90   LEU D CD1 1 
ATOM   15064 C  CD2 . LEU D 1 98  ? 3.774   7.106   112.383 1.00 19.77 ? 90   LEU D CD2 1 
ATOM   15065 N  N   . HIS D 1 99  ? 3.589   3.273   109.558 1.00 17.80 ? 91   HIS D N   1 
ATOM   15066 C  CA  . HIS D 1 99  ? 3.849   1.973   110.174 1.00 23.52 ? 91   HIS D CA  1 
ATOM   15067 C  C   . HIS D 1 99  ? 2.806   0.907   109.819 1.00 19.92 ? 91   HIS D C   1 
ATOM   15068 O  O   . HIS D 1 99  ? 2.689   -0.104  110.519 1.00 20.90 ? 91   HIS D O   1 
ATOM   15069 C  CB  . HIS D 1 99  ? 3.986   2.119   111.696 1.00 27.47 ? 91   HIS D CB  1 
ATOM   15070 C  CG  . HIS D 1 99  ? 5.170   2.937   112.106 1.00 27.28 ? 91   HIS D CG  1 
ATOM   15071 N  ND1 . HIS D 1 99  ? 5.077   4.020   112.957 1.00 28.41 ? 91   HIS D ND1 1 
ATOM   15072 C  CD2 . HIS D 1 99  ? 6.478   2.837   111.766 1.00 24.89 ? 91   HIS D CD2 1 
ATOM   15073 C  CE1 . HIS D 1 99  ? 6.278   4.547   113.127 1.00 26.00 ? 91   HIS D CE1 1 
ATOM   15074 N  NE2 . HIS D 1 99  ? 7.146   3.844   112.419 1.00 27.12 ? 91   HIS D NE2 1 
ATOM   15075 N  N   . SER D 1 100 ? 2.074   1.072   108.721 1.00 15.17 ? 92   SER D N   1 
ATOM   15076 C  CA  . SER D 1 100 ? 1.167   0.025   108.275 1.00 17.19 ? 92   SER D CA  1 
ATOM   15077 C  C   . SER D 1 100 ? 1.940   -1.088  107.574 1.00 18.36 ? 92   SER D C   1 
ATOM   15078 O  O   . SER D 1 100 ? 3.122   -0.954  107.249 1.00 15.94 ? 92   SER D O   1 
ATOM   15079 C  CB  . SER D 1 100 ? 0.098   0.584   107.331 1.00 18.30 ? 92   SER D CB  1 
ATOM   15080 O  OG  . SER D 1 100 ? 0.583   0.720   105.998 1.00 16.27 ? 92   SER D OG  1 
ATOM   15081 N  N   . LYS D 1 101 ? 1.249   -2.206  107.341 1.00 15.57 ? 93   LYS D N   1 
ATOM   15082 C  CA  . LYS D 1 101 ? 1.813   -3.314  106.584 1.00 19.08 ? 93   LYS D CA  1 
ATOM   15083 C  C   . LYS D 1 101 ? 1.761   -3.083  105.083 1.00 17.10 ? 93   LYS D C   1 
ATOM   15084 O  O   . LYS D 1 101 ? 2.202   -3.949  104.315 1.00 14.97 ? 93   LYS D O   1 
ATOM   15085 C  CB  . LYS D 1 101 ? 1.087   -4.616  106.940 1.00 20.61 ? 93   LYS D CB  1 
ATOM   15086 C  CG  . LYS D 1 101 ? 1.508   -5.178  108.296 1.00 26.36 ? 93   LYS D CG  1 
ATOM   15087 C  CD  . LYS D 1 101 ? 0.762   -6.457  108.647 1.00 33.90 ? 93   LYS D CD  1 
ATOM   15088 C  CE  . LYS D 1 101 ? 1.253   -7.010  109.983 1.00 46.20 ? 93   LYS D CE  1 
ATOM   15089 N  NZ  . LYS D 1 101 ? 0.357   -8.073  110.535 1.00 51.61 ? 93   LYS D NZ  1 
ATOM   15090 N  N   . THR D 1 102 ? 1.262   -1.930  104.649 1.00 17.96 ? 94   THR D N   1 
ATOM   15091 C  CA  . THR D 1 102 ? 1.064   -1.632  103.231 1.00 15.04 ? 94   THR D CA  1 
ATOM   15092 C  C   . THR D 1 102 ? 1.694   -0.282  102.872 1.00 14.31 ? 94   THR D C   1 
ATOM   15093 O  O   . THR D 1 102 ? 0.994   0.664   102.492 1.00 13.68 ? 94   THR D O   1 
ATOM   15094 C  CB  . THR D 1 102 ? -0.432  -1.642  102.917 1.00 15.85 ? 94   THR D CB  1 
ATOM   15095 O  OG1 . THR D 1 102 ? -1.121  -0.895  103.929 1.00 13.64 ? 94   THR D OG1 1 
ATOM   15096 C  CG2 . THR D 1 102 ? -0.977  -3.077  102.901 1.00 14.58 ? 94   THR D CG2 1 
ATOM   15097 N  N   . PRO D 1 103 ? 3.023   -0.156  102.982 1.00 13.42 ? 95   PRO D N   1 
ATOM   15098 C  CA  . PRO D 1 103 ? 3.680   1.086   102.540 1.00 12.20 ? 95   PRO D CA  1 
ATOM   15099 C  C   . PRO D 1 103 ? 3.537   1.313   101.036 1.00 14.40 ? 95   PRO D C   1 
ATOM   15100 O  O   . PRO D 1 103 ? 3.184   0.415   100.264 1.00 12.72 ? 95   PRO D O   1 
ATOM   15101 C  CB  . PRO D 1 103 ? 5.152   0.885   102.949 1.00 12.94 ? 95   PRO D CB  1 
ATOM   15102 C  CG  . PRO D 1 103 ? 5.328   -0.595  103.011 1.00 11.93 ? 95   PRO D CG  1 
ATOM   15103 C  CD  . PRO D 1 103 ? 3.992   -1.135  103.510 1.00 12.19 ? 95   PRO D CD  1 
ATOM   15104 N  N   . GLY D 1 104 ? 3.805   2.558   100.623 1.00 15.90 ? 96   GLY D N   1 
ATOM   15105 C  CA  . GLY D 1 104 ? 3.530   2.955   99.250  1.00 13.37 ? 96   GLY D CA  1 
ATOM   15106 C  C   . GLY D 1 104 ? 4.301   2.159   98.214  1.00 18.79 ? 96   GLY D C   1 
ATOM   15107 O  O   . GLY D 1 104 ? 3.841   2.001   97.079  1.00 18.46 ? 96   GLY D O   1 
ATOM   15108 N  N   . HIS D 1 105 ? 5.489   1.671   98.576  1.00 11.05 ? 97   HIS D N   1 
ATOM   15109 C  CA  . HIS D 1 105 ? 6.222   0.689   97.800  1.00 13.42 ? 97   HIS D CA  1 
ATOM   15110 C  C   . HIS D 1 105 ? 6.411   -0.564  98.645  1.00 11.87 ? 97   HIS D C   1 
ATOM   15111 O  O   . HIS D 1 105 ? 6.578   -0.457  99.862  1.00 18.84 ? 97   HIS D O   1 
ATOM   15112 C  CB  . HIS D 1 105 ? 7.588   1.242   97.344  1.00 16.48 ? 97   HIS D CB  1 
ATOM   15113 C  CG  . HIS D 1 105 ? 7.465   2.373   96.372  1.00 24.73 ? 97   HIS D CG  1 
ATOM   15114 N  ND1 . HIS D 1 105 ? 7.517   3.693   96.757  1.00 31.83 ? 97   HIS D ND1 1 
ATOM   15115 C  CD2 . HIS D 1 105 ? 7.236   2.378   95.038  1.00 29.33 ? 97   HIS D CD2 1 
ATOM   15116 C  CE1 . HIS D 1 105 ? 7.348   4.465   95.699  1.00 30.13 ? 97   HIS D CE1 1 
ATOM   15117 N  NE2 . HIS D 1 105 ? 7.182   3.692   94.642  1.00 31.75 ? 97   HIS D NE2 1 
ATOM   15118 N  N   . PRO D 1 106 ? 6.323   -1.755  98.053  1.00 13.91 ? 98   PRO D N   1 
ATOM   15119 C  CA  . PRO D 1 106 ? 6.356   -2.975  98.869  1.00 17.66 ? 98   PRO D CA  1 
ATOM   15120 C  C   . PRO D 1 106 ? 7.715   -3.141  99.534  1.00 16.34 ? 98   PRO D C   1 
ATOM   15121 O  O   . PRO D 1 106 ? 8.753   -2.884  98.923  1.00 16.85 ? 98   PRO D O   1 
ATOM   15122 C  CB  . PRO D 1 106 ? 6.086   -4.097  97.857  1.00 14.99 ? 98   PRO D CB  1 
ATOM   15123 C  CG  . PRO D 1 106 ? 5.468   -3.377  96.626  1.00 13.60 ? 98   PRO D CG  1 
ATOM   15124 C  CD  . PRO D 1 106 ? 6.167   -2.049  96.615  1.00 12.63 ? 98   PRO D CD  1 
ATOM   15125 N  N   . GLU D 1 107 ? 7.695   -3.568  100.798 1.00 15.31 ? 99   GLU D N   1 
ATOM   15126 C  CA  . GLU D 1 107 ? 8.900   -3.679  101.619 1.00 14.40 ? 99   GLU D CA  1 
ATOM   15127 C  C   . GLU D 1 107 ? 9.092   -5.113  102.087 1.00 16.49 ? 99   GLU D C   1 
ATOM   15128 O  O   . GLU D 1 107 ? 8.223   -5.680  102.759 1.00 19.23 ? 99   GLU D O   1 
ATOM   15129 C  CB  . GLU D 1 107 ? 8.830   -2.742  102.826 1.00 13.95 ? 99   GLU D CB  1 
ATOM   15130 C  CG  . GLU D 1 107 ? 8.940   -1.280  102.426 1.00 15.97 ? 99   GLU D CG  1 
ATOM   15131 C  CD  . GLU D 1 107 ? 8.866   -0.338  103.613 1.00 19.36 ? 99   GLU D CD  1 
ATOM   15132 O  OE1 . GLU D 1 107 ? 9.076   -0.803  104.748 1.00 21.34 ? 99   GLU D OE1 1 
ATOM   15133 O  OE2 . GLU D 1 107 ? 8.580   0.860   103.407 1.00 16.06 ? 99   GLU D OE2 1 
ATOM   15134 N  N   . TYR D 1 108 ? 10.237  -5.684  101.739 1.00 11.16 ? 100  TYR D N   1 
ATOM   15135 C  CA  . TYR D 1 108 ? 10.626  -6.983  102.256 1.00 11.48 ? 100  TYR D CA  1 
ATOM   15136 C  C   . TYR D 1 108 ? 10.800  -6.927  103.767 1.00 11.86 ? 100  TYR D C   1 
ATOM   15137 O  O   . TYR D 1 108 ? 11.402  -5.993  104.301 1.00 14.60 ? 100  TYR D O   1 
ATOM   15138 C  CB  . TYR D 1 108 ? 11.942  -7.418  101.606 1.00 15.76 ? 100  TYR D CB  1 
ATOM   15139 C  CG  . TYR D 1 108 ? 12.506  -8.684  102.188 1.00 14.51 ? 100  TYR D CG  1 
ATOM   15140 C  CD1 . TYR D 1 108 ? 11.987  -9.920  101.827 1.00 15.98 ? 100  TYR D CD1 1 
ATOM   15141 C  CD2 . TYR D 1 108 ? 13.555  -8.649  103.103 1.00 16.57 ? 100  TYR D CD2 1 
ATOM   15142 C  CE1 . TYR D 1 108 ? 12.500  -11.090 102.361 1.00 20.25 ? 100  TYR D CE1 1 
ATOM   15143 C  CE2 . TYR D 1 108 ? 14.064  -9.816  103.650 1.00 21.21 ? 100  TYR D CE2 1 
ATOM   15144 C  CZ  . TYR D 1 108 ? 13.535  -11.030 103.273 1.00 22.56 ? 100  TYR D CZ  1 
ATOM   15145 O  OH  . TYR D 1 108 ? 14.034  -12.194 103.797 1.00 32.94 ? 100  TYR D OH  1 
ATOM   15146 N  N   . GLY D 1 109 ? 10.303  -7.946  104.456 1.00 12.31 ? 101  GLY D N   1 
ATOM   15147 C  CA  . GLY D 1 109 ? 10.640  -8.072  105.862 1.00 16.32 ? 101  GLY D CA  1 
ATOM   15148 C  C   . GLY D 1 109 ? 9.469   -8.173  106.813 1.00 28.94 ? 101  GLY D C   1 
ATOM   15149 O  O   . GLY D 1 109 ? 9.446   -9.052  107.679 1.00 38.58 ? 101  GLY D O   1 
ATOM   15150 N  N   . TYR D 1 110 ? 8.494   -7.283  106.674 1.00 27.81 ? 102  TYR D N   1 
ATOM   15151 C  CA  . TYR D 1 110 ? 7.389   -7.216  107.617 1.00 27.80 ? 102  TYR D CA  1 
ATOM   15152 C  C   . TYR D 1 110 ? 6.035   -7.521  106.996 1.00 28.10 ? 102  TYR D C   1 
ATOM   15153 O  O   . TYR D 1 110 ? 5.078   -7.764  107.737 1.00 29.06 ? 102  TYR D O   1 
ATOM   15154 C  CB  . TYR D 1 110 ? 7.336   -5.829  108.280 1.00 30.53 ? 102  TYR D CB  1 
ATOM   15155 N  N   . THR D 1 111 ? 5.923   -7.507  105.674 1.00 21.59 ? 103  THR D N   1 
ATOM   15156 C  CA  . THR D 1 111 ? 4.707   -7.888  104.970 1.00 17.49 ? 103  THR D CA  1 
ATOM   15157 C  C   . THR D 1 111 ? 4.939   -9.275  104.387 1.00 17.24 ? 103  THR D C   1 
ATOM   15158 O  O   . THR D 1 111 ? 5.826   -9.449  103.548 1.00 15.27 ? 103  THR D O   1 
ATOM   15159 C  CB  . THR D 1 111 ? 4.390   -6.864  103.882 1.00 21.19 ? 103  THR D CB  1 
ATOM   15160 O  OG1 . THR D 1 111 ? 4.290   -5.567  104.481 1.00 23.70 ? 103  THR D OG1 1 
ATOM   15161 C  CG2 . THR D 1 111 ? 3.072   -7.198  103.164 1.00 17.18 ? 103  THR D CG2 1 
ATOM   15162 N  N   . ASP D 1 112 ? 4.178   -10.263 104.863 1.00 19.24 ? 104  ASP D N   1 
ATOM   15163 C  CA  . ASP D 1 112 ? 4.343   -11.629 104.379 1.00 17.12 ? 104  ASP D CA  1 
ATOM   15164 C  C   . ASP D 1 112 ? 4.171   -11.687 102.870 1.00 16.38 ? 104  ASP D C   1 
ATOM   15165 O  O   . ASP D 1 112 ? 3.262   -11.073 102.312 1.00 15.07 ? 104  ASP D O   1 
ATOM   15166 C  CB  . ASP D 1 112 ? 3.318   -12.556 105.029 1.00 24.79 ? 104  ASP D CB  1 
ATOM   15167 C  CG  . ASP D 1 112 ? 3.695   -12.953 106.429 1.00 30.60 ? 104  ASP D CG  1 
ATOM   15168 O  OD1 . ASP D 1 112 ? 4.788   -12.561 106.875 1.00 28.78 ? 104  ASP D OD1 1 
ATOM   15169 O  OD2 . ASP D 1 112 ? 2.890   -13.659 107.076 1.00 33.70 ? 104  ASP D OD2 1 
ATOM   15170 N  N   . GLY D 1 113 ? 5.038   -12.449 102.209 1.00 16.79 ? 105  GLY D N   1 
ATOM   15171 C  CA  . GLY D 1 113 ? 4.894   -12.693 100.796 1.00 18.11 ? 105  GLY D CA  1 
ATOM   15172 C  C   . GLY D 1 113 ? 5.556   -11.676 99.899  1.00 18.84 ? 105  GLY D C   1 
ATOM   15173 O  O   . GLY D 1 113 ? 5.578   -11.880 98.680  1.00 19.39 ? 105  GLY D O   1 
ATOM   15174 N  N   . VAL D 1 114 ? 6.094   -10.591 100.454 1.00 14.47 ? 106  VAL D N   1 
ATOM   15175 C  CA  . VAL D 1 114 ? 6.876   -9.644  99.666  1.00 13.73 ? 106  VAL D CA  1 
ATOM   15176 C  C   . VAL D 1 114 ? 8.299   -10.177 99.571  1.00 20.20 ? 106  VAL D C   1 
ATOM   15177 O  O   . VAL D 1 114 ? 8.971   -10.355 100.591 1.00 16.72 ? 106  VAL D O   1 
ATOM   15178 C  CB  . VAL D 1 114 ? 6.849   -8.241  100.291 1.00 12.27 ? 106  VAL D CB  1 
ATOM   15179 C  CG1 . VAL D 1 114 ? 7.736   -7.296  99.490  1.00 15.12 ? 106  VAL D CG1 1 
ATOM   15180 C  CG2 . VAL D 1 114 ? 5.409   -7.723  100.355 1.00 13.66 ? 106  VAL D CG2 1 
ATOM   15181 N  N   . GLU D 1 115 ? 8.762   -10.427 98.347  1.00 17.09 ? 107  GLU D N   1 
ATOM   15182 C  CA  . GLU D 1 115 ? 10.042  -11.093 98.160  1.00 11.80 ? 107  GLU D CA  1 
ATOM   15183 C  C   . GLU D 1 115 ? 11.214  -10.124 98.143  1.00 12.09 ? 107  GLU D C   1 
ATOM   15184 O  O   . GLU D 1 115 ? 12.347  -10.539 98.416  1.00 17.61 ? 107  GLU D O   1 
ATOM   15185 C  CB  . GLU D 1 115 ? 10.040  -11.901 96.853  1.00 13.39 ? 107  GLU D CB  1 
ATOM   15186 C  CG  . GLU D 1 115 ? 9.000   -13.023 96.777  1.00 17.94 ? 107  GLU D CG  1 
ATOM   15187 C  CD  . GLU D 1 115 ? 9.288   -14.191 97.708  1.00 18.13 ? 107  GLU D CD  1 
ATOM   15188 O  OE1 . GLU D 1 115 ? 10.367  -14.228 98.343  1.00 19.77 ? 107  GLU D OE1 1 
ATOM   15189 O  OE2 . GLU D 1 115 ? 8.427   -15.092 97.806  1.00 19.97 ? 107  GLU D OE2 1 
ATOM   15190 N  N   . THR D 1 116 ? 10.970  -8.862  97.811  1.00 13.50 ? 108  THR D N   1 
ATOM   15191 C  CA  . THR D 1 116 ? 12.016  -7.854  97.718  1.00 14.67 ? 108  THR D CA  1 
ATOM   15192 C  C   . THR D 1 116 ? 11.355  -6.494  97.858  1.00 10.99 ? 108  THR D C   1 
ATOM   15193 O  O   . THR D 1 116 ? 10.146  -6.356  97.663  1.00 14.95 ? 108  THR D O   1 
ATOM   15194 C  CB  . THR D 1 116 ? 12.787  -7.970  96.398  1.00 16.56 ? 108  THR D CB  1 
ATOM   15195 O  OG1 . THR D 1 116 ? 13.847  -7.007  96.371  1.00 16.00 ? 108  THR D OG1 1 
ATOM   15196 C  CG2 . THR D 1 116 ? 11.857  -7.754  95.204  1.00 16.91 ? 108  THR D CG2 1 
ATOM   15197 N  N   . THR D 1 117 ? 12.153  -5.493  98.215  1.00 10.36 ? 109  THR D N   1 
ATOM   15198 C  CA  . THR D 1 117 ? 11.671  -4.122  98.302  1.00 12.08 ? 109  THR D CA  1 
ATOM   15199 C  C   . THR D 1 117 ? 11.952  -3.455  96.967  1.00 11.60 ? 109  THR D C   1 
ATOM   15200 O  O   . THR D 1 117 ? 13.108  -3.390  96.538  1.00 15.71 ? 109  THR D O   1 
ATOM   15201 C  CB  . THR D 1 117 ? 12.358  -3.364  99.442  1.00 15.87 ? 109  THR D CB  1 
ATOM   15202 O  OG1 . THR D 1 117 ? 12.102  -4.035  100.684 1.00 15.60 ? 109  THR D OG1 1 
ATOM   15203 C  CG2 . THR D 1 117 ? 11.840  -1.934  99.534  1.00 15.35 ? 109  THR D CG2 1 
ATOM   15204 N  N   . THR D 1 118 ? 10.906  -2.994  96.291  1.00 12.09 ? 110  THR D N   1 
ATOM   15205 C  CA  . THR D 1 118 ? 11.087  -2.316  95.019  1.00 16.88 ? 110  THR D CA  1 
ATOM   15206 C  C   . THR D 1 118 ? 10.449  -0.934  95.071  1.00 20.35 ? 110  THR D C   1 
ATOM   15207 O  O   . THR D 1 118 ? 9.612   -0.634  95.917  1.00 24.82 ? 110  THR D O   1 
ATOM   15208 C  CB  . THR D 1 118 ? 10.495  -3.117  93.850  1.00 12.23 ? 110  THR D CB  1 
ATOM   15209 O  OG1 . THR D 1 118 ? 9.089   -3.307  94.056  1.00 16.89 ? 110  THR D OG1 1 
ATOM   15210 C  CG2 . THR D 1 118 ? 11.190  -4.481  93.721  1.00 16.62 ? 110  THR D CG2 1 
ATOM   15211 N  N   . GLY D 1 119 ? 10.839  -0.107  94.130  1.00 18.34 ? 111  GLY D N   1 
ATOM   15212 C  CA  . GLY D 1 119 ? 10.506  1.291   94.158  1.00 20.52 ? 111  GLY D CA  1 
ATOM   15213 C  C   . GLY D 1 119 ? 11.403  2.012   93.183  1.00 20.31 ? 111  GLY D C   1 
ATOM   15214 O  O   . GLY D 1 119 ? 10.958  2.514   92.148  1.00 21.29 ? 111  GLY D O   1 
ATOM   15215 N  N   . PRO D 1 120 ? 12.697  2.067   93.490  1.00 18.96 ? 112  PRO D N   1 
ATOM   15216 C  CA  . PRO D 1 120 ? 13.662  2.542   92.491  1.00 13.11 ? 112  PRO D CA  1 
ATOM   15217 C  C   . PRO D 1 120 ? 13.681  1.583   91.313  1.00 14.98 ? 112  PRO D C   1 
ATOM   15218 O  O   . PRO D 1 120 ? 13.907  0.381   91.465  1.00 17.02 ? 112  PRO D O   1 
ATOM   15219 C  CB  . PRO D 1 120 ? 14.989  2.560   93.258  1.00 16.05 ? 112  PRO D CB  1 
ATOM   15220 C  CG  . PRO D 1 120 ? 14.581  2.580   94.717  1.00 18.43 ? 112  PRO D CG  1 
ATOM   15221 C  CD  . PRO D 1 120 ? 13.352  1.737   94.767  1.00 20.09 ? 112  PRO D CD  1 
ATOM   15222 N  N   . LEU D 1 121 ? 13.401  2.118   90.132  1.00 12.75 ? 113  LEU D N   1 
ATOM   15223 C  CA  . LEU D 1 121 ? 13.112  1.265   88.990  1.00 10.72 ? 113  LEU D CA  1 
ATOM   15224 C  C   . LEU D 1 121 ? 14.357  0.547   88.480  1.00 14.01 ? 113  LEU D C   1 
ATOM   15225 O  O   . LEU D 1 121 ? 15.493  1.005   88.649  1.00 15.05 ? 113  LEU D O   1 
ATOM   15226 C  CB  . LEU D 1 121 ? 12.494  2.096   87.870  1.00 12.77 ? 113  LEU D CB  1 
ATOM   15227 C  CG  . LEU D 1 121 ? 11.186  2.755   88.331  1.00 17.65 ? 113  LEU D CG  1 
ATOM   15228 C  CD1 . LEU D 1 121 ? 10.604  3.675   87.240  1.00 19.30 ? 113  LEU D CD1 1 
ATOM   15229 C  CD2 . LEU D 1 121 ? 10.180  1.698   88.744  1.00 21.85 ? 113  LEU D CD2 1 
ATOM   15230 N  N   . GLY D 1 122 ? 14.122  -0.597  87.845  1.00 12.41 ? 114  GLY D N   1 
ATOM   15231 C  CA  . GLY D 1 122 ? 15.161  -1.399  87.264  1.00 12.92 ? 114  GLY D CA  1 
ATOM   15232 C  C   . GLY D 1 122 ? 15.737  -2.431  88.199  1.00 13.15 ? 114  GLY D C   1 
ATOM   15233 O  O   . GLY D 1 122 ? 16.186  -3.480  87.741  1.00 13.26 ? 114  GLY D O   1 
ATOM   15234 N  N   . GLN D 1 123 ? 15.738  -2.163  89.507  1.00 11.55 ? 115  GLN D N   1 
ATOM   15235 C  CA  . GLN D 1 123 ? 16.405  -3.086  90.415  1.00 11.46 ? 115  GLN D CA  1 
ATOM   15236 C  C   . GLN D 1 123 ? 15.603  -4.356  90.662  1.00 14.31 ? 115  GLN D C   1 
ATOM   15237 O  O   . GLN D 1 123 ? 16.198  -5.403  90.932  1.00 14.19 ? 115  GLN D O   1 
ATOM   15238 C  CB  . GLN D 1 123 ? 16.713  -2.391  91.734  1.00 13.87 ? 115  GLN D CB  1 
ATOM   15239 C  CG  . GLN D 1 123 ? 17.877  -1.408  91.594  1.00 12.60 ? 115  GLN D CG  1 
ATOM   15240 C  CD  . GLN D 1 123 ? 18.253  -0.795  92.918  1.00 15.10 ? 115  GLN D CD  1 
ATOM   15241 O  OE1 . GLN D 1 123 ? 18.750  -1.485  93.809  1.00 12.32 ? 115  GLN D OE1 1 
ATOM   15242 N  NE2 . GLN D 1 123 ? 18.015  0.502   93.062  1.00 13.04 ? 115  GLN D NE2 1 
ATOM   15243 N  N   . GLY D 1 124 ? 14.274  -4.298  90.550  1.00 12.51 ? 116  GLY D N   1 
ATOM   15244 C  CA  . GLY D 1 124 ? 13.479  -5.501  90.772  1.00 11.67 ? 116  GLY D CA  1 
ATOM   15245 C  C   . GLY D 1 124 ? 13.826  -6.624  89.809  1.00 11.16 ? 116  GLY D C   1 
ATOM   15246 O  O   . GLY D 1 124 ? 14.007  -7.776  90.214  1.00 11.18 ? 116  GLY D O   1 
ATOM   15247 N  N   . ILE D 1 125 ? 13.932  -6.307  88.516  1.00 13.59 ? 117  ILE D N   1 
ATOM   15248 C  CA  . ILE D 1 125 ? 14.293  -7.347  87.553  1.00 15.77 ? 117  ILE D CA  1 
ATOM   15249 C  C   . ILE D 1 125 ? 15.690  -7.885  87.853  1.00 14.38 ? 117  ILE D C   1 
ATOM   15250 O  O   . ILE D 1 125 ? 15.941  -9.093  87.752  1.00 14.40 ? 117  ILE D O   1 
ATOM   15251 C  CB  . ILE D 1 125 ? 14.168  -6.824  86.108  1.00 16.37 ? 117  ILE D CB  1 
ATOM   15252 C  CG1 . ILE D 1 125 ? 14.645  -7.880  85.111  1.00 11.94 ? 117  ILE D CG1 1 
ATOM   15253 C  CG2 . ILE D 1 125 ? 14.961  -5.547  85.917  1.00 18.52 ? 117  ILE D CG2 1 
ATOM   15254 C  CD1 . ILE D 1 125 ? 13.897  -9.200  85.199  1.00 14.29 ? 117  ILE D CD1 1 
ATOM   15255 N  N   . ALA D 1 126 ? 16.609  -7.008  88.265  1.00 11.56 ? 118  ALA D N   1 
ATOM   15256 C  CA  . ALA D 1 126 ? 17.941  -7.472  88.650  1.00 14.51 ? 118  ALA D CA  1 
ATOM   15257 C  C   . ALA D 1 126 ? 17.891  -8.359  89.888  1.00 17.07 ? 118  ALA D C   1 
ATOM   15258 O  O   . ALA D 1 126 ? 18.574  -9.393  89.940  1.00 12.26 ? 118  ALA D O   1 
ATOM   15259 C  CB  . ALA D 1 126 ? 18.862  -6.284  88.881  1.00 12.62 ? 118  ALA D CB  1 
ATOM   15260 N  N   . ASN D 1 127 ? 17.108  -7.965  90.907  1.00 10.94 ? 119  ASN D N   1 
ATOM   15261 C  CA  . ASN D 1 127 ? 16.888  -8.859  92.044  1.00 14.96 ? 119  ASN D CA  1 
ATOM   15262 C  C   . ASN D 1 127 ? 16.401  -10.220 91.571  1.00 12.77 ? 119  ASN D C   1 
ATOM   15263 O  O   . ASN D 1 127 ? 16.849  -11.263 92.063  1.00 13.01 ? 119  ASN D O   1 
ATOM   15264 C  CB  . ASN D 1 127 ? 15.843  -8.296  93.019  1.00 13.54 ? 119  ASN D CB  1 
ATOM   15265 C  CG  . ASN D 1 127 ? 16.209  -6.939  93.617  1.00 13.40 ? 119  ASN D CG  1 
ATOM   15266 O  OD1 . ASN D 1 127 ? 15.323  -6.213  94.048  1.00 13.59 ? 119  ASN D OD1 1 
ATOM   15267 N  ND2 . ASN D 1 127 ? 17.494  -6.598  93.653  1.00 10.18 ? 119  ASN D ND2 1 
ATOM   15268 N  N   . ALA D 1 128 ? 15.446  -10.221 90.636  1.00 14.24 ? 120  ALA D N   1 
ATOM   15269 C  CA  . ALA D 1 128 ? 14.853  -11.471 90.187  1.00 15.11 ? 120  ALA D CA  1 
ATOM   15270 C  C   . ALA D 1 128 ? 15.870  -12.315 89.432  1.00 11.71 ? 120  ALA D C   1 
ATOM   15271 O  O   . ALA D 1 128 ? 15.853  -13.543 89.528  1.00 15.75 ? 120  ALA D O   1 
ATOM   15272 C  CB  . ALA D 1 128 ? 13.630  -11.190 89.318  1.00 11.31 ? 120  ALA D CB  1 
ATOM   15273 N  N   . VAL D 1 129 ? 16.739  -11.670 88.651  1.00 11.71 ? 121  VAL D N   1 
ATOM   15274 C  CA  . VAL D 1 129 ? 17.822  -12.398 87.998  1.00 14.52 ? 121  VAL D CA  1 
ATOM   15275 C  C   . VAL D 1 129 ? 18.651  -13.124 89.043  1.00 15.33 ? 121  VAL D C   1 
ATOM   15276 O  O   . VAL D 1 129 ? 19.000  -14.296 88.873  1.00 14.10 ? 121  VAL D O   1 
ATOM   15277 C  CB  . VAL D 1 129 ? 18.668  -11.437 87.138  1.00 14.69 ? 121  VAL D CB  1 
ATOM   15278 C  CG1 . VAL D 1 129 ? 19.963  -12.099 86.685  1.00 14.59 ? 121  VAL D CG1 1 
ATOM   15279 C  CG2 . VAL D 1 129 ? 17.852  -10.971 85.922  1.00 15.21 ? 121  VAL D CG2 1 
ATOM   15280 N  N   . GLY D 1 130 ? 18.902  -12.465 90.177  1.00 14.30 ? 122  GLY D N   1 
ATOM   15281 C  CA  . GLY D 1 130 ? 19.648  -13.106 91.247  1.00 15.13 ? 122  GLY D CA  1 
ATOM   15282 C  C   . GLY D 1 130 ? 18.885  -14.247 91.890  1.00 13.94 ? 122  GLY D C   1 
ATOM   15283 O  O   . GLY D 1 130 ? 19.470  -15.273 92.243  1.00 15.29 ? 122  GLY D O   1 
ATOM   15284 N  N   . MET D 1 131 ? 17.570  -14.094 92.041  1.00 12.89 ? 123  MET D N   1 
ATOM   15285 C  CA  . MET D 1 131 ? 16.766  -15.196 92.568  1.00 13.63 ? 123  MET D CA  1 
ATOM   15286 C  C   . MET D 1 131 ? 16.768  -16.392 91.626  1.00 14.65 ? 123  MET D C   1 
ATOM   15287 O  O   . MET D 1 131 ? 16.868  -17.543 92.073  1.00 14.83 ? 123  MET D O   1 
ATOM   15288 C  CB  . MET D 1 131 ? 15.337  -14.731 92.824  1.00 15.39 ? 123  MET D CB  1 
ATOM   15289 C  CG  . MET D 1 131 ? 15.239  -13.740 93.957  1.00 17.57 ? 123  MET D CG  1 
ATOM   15290 S  SD  . MET D 1 131 ? 13.561  -13.113 94.059  1.00 15.39 ? 123  MET D SD  1 
ATOM   15291 C  CE  . MET D 1 131 ? 13.770  -11.748 95.223  1.00 16.06 ? 123  MET D CE  1 
ATOM   15292 N  N   . ALA D 1 132 ? 16.641  -16.148 90.319  1.00 17.57 ? 124  ALA D N   1 
ATOM   15293 C  CA  . ALA D 1 132 ? 16.682  -17.258 89.369  1.00 17.86 ? 124  ALA D CA  1 
ATOM   15294 C  C   . ALA D 1 132 ? 18.069  -17.880 89.309  1.00 19.76 ? 124  ALA D C   1 
ATOM   15295 O  O   . ALA D 1 132 ? 18.201  -19.090 89.084  1.00 19.18 ? 124  ALA D O   1 
ATOM   15296 C  CB  . ALA D 1 132 ? 16.253  -16.782 87.977  1.00 19.20 ? 124  ALA D CB  1 
ATOM   15297 N  N   . LEU D 1 133 ? 19.110  -17.064 89.483  1.00 19.02 ? 125  LEU D N   1 
ATOM   15298 C  CA  . LEU D 1 133 ? 20.466  -17.592 89.491  1.00 19.63 ? 125  LEU D CA  1 
ATOM   15299 C  C   . LEU D 1 133 ? 20.687  -18.486 90.701  1.00 21.33 ? 125  LEU D C   1 
ATOM   15300 O  O   . LEU D 1 133 ? 21.288  -19.558 90.584  1.00 20.13 ? 125  LEU D O   1 
ATOM   15301 C  CB  . LEU D 1 133 ? 21.463  -16.439 89.466  1.00 17.47 ? 125  LEU D CB  1 
ATOM   15302 C  CG  . LEU D 1 133 ? 22.926  -16.768 89.164  1.00 24.57 ? 125  LEU D CG  1 
ATOM   15303 C  CD1 . LEU D 1 133 ? 23.061  -17.593 87.884  1.00 23.98 ? 125  LEU D CD1 1 
ATOM   15304 C  CD2 . LEU D 1 133 ? 23.728  -15.476 89.065  1.00 24.32 ? 125  LEU D CD2 1 
ATOM   15305 N  N   . ALA D 1 134 ? 20.197  -18.068 91.871  1.00 19.56 ? 126  ALA D N   1 
ATOM   15306 C  CA  . ALA D 1 134 ? 20.313  -18.909 93.058  1.00 16.81 ? 126  ALA D CA  1 
ATOM   15307 C  C   . ALA D 1 134 ? 19.612  -20.244 92.856  1.00 18.60 ? 126  ALA D C   1 
ATOM   15308 O  O   . ALA D 1 134 ? 20.130  -21.292 93.265  1.00 21.40 ? 126  ALA D O   1 
ATOM   15309 C  CB  . ALA D 1 134 ? 19.733  -18.196 94.277  1.00 14.92 ? 126  ALA D CB  1 
ATOM   15310 N  N   . GLU D 1 135 ? 18.419  -20.230 92.249  1.00 15.83 ? 127  GLU D N   1 
ATOM   15311 C  CA  . GLU D 1 135 ? 17.729  -21.494 92.000  1.00 17.03 ? 127  GLU D CA  1 
ATOM   15312 C  C   . GLU D 1 135 ? 18.562  -22.386 91.092  1.00 18.69 ? 127  GLU D C   1 
ATOM   15313 O  O   . GLU D 1 135 ? 18.667  -23.594 91.323  1.00 18.43 ? 127  GLU D O   1 
ATOM   15314 C  CB  . GLU D 1 135 ? 16.341  -21.243 91.394  1.00 16.24 ? 127  GLU D CB  1 
ATOM   15315 C  CG  . GLU D 1 135 ? 15.427  -22.481 91.384  1.00 18.93 ? 127  GLU D CG  1 
ATOM   15316 C  CD  . GLU D 1 135 ? 15.541  -23.326 90.108  1.00 22.47 ? 127  GLU D CD  1 
ATOM   15317 O  OE1 . GLU D 1 135 ? 16.274  -22.924 89.171  1.00 21.42 ? 127  GLU D OE1 1 
ATOM   15318 O  OE2 . GLU D 1 135 ? 14.880  -24.395 90.044  1.00 19.16 ? 127  GLU D OE2 1 
ATOM   15319 N  N   . LYS D 1 136 ? 19.169  -21.800 90.060  1.00 24.04 ? 128  LYS D N   1 
ATOM   15320 C  CA  A LYS D 1 136 ? 19.985  -22.579 89.133  0.52 27.00 ? 128  LYS D CA  1 
ATOM   15321 C  CA  B LYS D 1 136 ? 19.983  -22.580 89.134  0.48 26.98 ? 128  LYS D CA  1 
ATOM   15322 C  C   . LYS D 1 136 ? 21.199  -23.168 89.839  1.00 18.23 ? 128  LYS D C   1 
ATOM   15323 O  O   . LYS D 1 136 ? 21.510  -24.354 89.678  1.00 20.04 ? 128  LYS D O   1 
ATOM   15324 C  CB  A LYS D 1 136 ? 20.419  -21.703 87.956  0.52 27.76 ? 128  LYS D CB  1 
ATOM   15325 C  CB  B LYS D 1 136 ? 20.401  -21.700 87.954  0.48 27.71 ? 128  LYS D CB  1 
ATOM   15326 C  CG  A LYS D 1 136 ? 21.515  -22.328 87.099  0.52 29.38 ? 128  LYS D CG  1 
ATOM   15327 C  CG  B LYS D 1 136 ? 21.207  -22.419 86.884  0.48 29.48 ? 128  LYS D CG  1 
ATOM   15328 C  CD  A LYS D 1 136 ? 22.299  -21.271 86.343  0.52 25.96 ? 128  LYS D CD  1 
ATOM   15329 C  CD  B LYS D 1 136 ? 20.880  -21.858 85.514  0.48 28.52 ? 128  LYS D CD  1 
ATOM   15330 C  CE  A LYS D 1 136 ? 23.616  -21.831 85.800  0.52 24.96 ? 128  LYS D CE  1 
ATOM   15331 C  CE  B LYS D 1 136 ? 21.685  -22.530 84.419  0.48 25.82 ? 128  LYS D CE  1 
ATOM   15332 N  NZ  A LYS D 1 136 ? 23.430  -22.794 84.681  0.52 19.77 ? 128  LYS D NZ  1 
ATOM   15333 N  NZ  B LYS D 1 136 ? 21.146  -22.173 83.090  0.48 18.16 ? 128  LYS D NZ  1 
ATOM   15334 N  N   . ILE D 1 137 ? 21.889  -22.347 90.630  1.00 20.96 ? 129  ILE D N   1 
ATOM   15335 C  CA  . ILE D 1 137 ? 23.074  -22.787 91.369  1.00 27.02 ? 129  ILE D CA  1 
ATOM   15336 C  C   . ILE D 1 137 ? 22.721  -23.920 92.327  1.00 26.21 ? 129  ILE D C   1 
ATOM   15337 O  O   . ILE D 1 137 ? 23.411  -24.947 92.392  1.00 22.60 ? 129  ILE D O   1 
ATOM   15338 C  CB  . ILE D 1 137 ? 23.694  -21.591 92.118  1.00 25.97 ? 129  ILE D CB  1 
ATOM   15339 C  CG1 . ILE D 1 137 ? 24.290  -20.591 91.130  1.00 30.02 ? 129  ILE D CG1 1 
ATOM   15340 C  CG2 . ILE D 1 137 ? 24.742  -22.038 93.118  1.00 30.38 ? 129  ILE D CG2 1 
ATOM   15341 C  CD1 . ILE D 1 137 ? 24.813  -19.341 91.795  1.00 22.04 ? 129  ILE D CD1 1 
ATOM   15342 N  N   . LEU D 1 138 ? 21.642  -23.741 93.089  1.00 20.72 ? 130  LEU D N   1 
ATOM   15343 C  CA  . LEU D 1 138 ? 21.260  -24.711 94.108  1.00 21.10 ? 130  LEU D CA  1 
ATOM   15344 C  C   . LEU D 1 138 ? 20.744  -26.009 93.501  1.00 20.47 ? 130  LEU D C   1 
ATOM   15345 O  O   . LEU D 1 138 ? 20.961  -27.084 94.072  1.00 22.78 ? 130  LEU D O   1 
ATOM   15346 C  CB  . LEU D 1 138 ? 20.210  -24.096 95.037  1.00 21.96 ? 130  LEU D CB  1 
ATOM   15347 C  CG  . LEU D 1 138 ? 20.718  -22.947 95.919  1.00 22.88 ? 130  LEU D CG  1 
ATOM   15348 C  CD1 . LEU D 1 138 ? 19.573  -22.219 96.605  1.00 22.24 ? 130  LEU D CD1 1 
ATOM   15349 C  CD2 . LEU D 1 138 ? 21.709  -23.491 96.946  1.00 22.45 ? 130  LEU D CD2 1 
ATOM   15350 N  N   . ALA D 1 139 ? 20.063  -25.936 92.354  1.00 20.20 ? 131  ALA D N   1 
ATOM   15351 C  CA  . ALA D 1 139 ? 19.619  -27.159 91.696  1.00 21.10 ? 131  ALA D CA  1 
ATOM   15352 C  C   . ALA D 1 139 ? 20.805  -27.966 91.186  1.00 27.25 ? 131  ALA D C   1 
ATOM   15353 O  O   . ALA D 1 139 ? 20.844  -29.193 91.354  1.00 23.35 ? 131  ALA D O   1 
ATOM   15354 C  CB  . ALA D 1 139 ? 18.651  -26.832 90.557  1.00 20.65 ? 131  ALA D CB  1 
ATOM   15355 N  N   . ALA D 1 140 ? 21.789  -27.296 90.577  1.00 26.46 ? 132  ALA D N   1 
ATOM   15356 C  CA  . ALA D 1 140 ? 22.996  -27.994 90.129  1.00 26.09 ? 132  ALA D CA  1 
ATOM   15357 C  C   . ALA D 1 140 ? 23.714  -28.650 91.297  1.00 25.30 ? 132  ALA D C   1 
ATOM   15358 O  O   . ALA D 1 140 ? 24.254  -29.755 91.168  1.00 28.01 ? 132  ALA D O   1 
ATOM   15359 C  CB  . ALA D 1 140 ? 23.940  -27.026 89.409  1.00 21.90 ? 132  ALA D CB  1 
ATOM   15360 N  N   . GLU D 1 141 ? 23.718  -27.992 92.451  1.00 22.78 ? 133  GLU D N   1 
ATOM   15361 C  CA  . GLU D 1 141 ? 24.459  -28.515 93.589  1.00 30.88 ? 133  GLU D CA  1 
ATOM   15362 C  C   . GLU D 1 141 ? 23.708  -29.636 94.303  1.00 32.42 ? 133  GLU D C   1 
ATOM   15363 O  O   . GLU D 1 141 ? 24.311  -30.649 94.676  1.00 27.26 ? 133  GLU D O   1 
ATOM   15364 C  CB  . GLU D 1 141 ? 24.770  -27.380 94.555  1.00 29.25 ? 133  GLU D CB  1 
ATOM   15365 C  CG  . GLU D 1 141 ? 25.417  -27.836 95.833  1.00 25.01 ? 133  GLU D CG  1 
ATOM   15366 C  CD  . GLU D 1 141 ? 25.876  -26.673 96.673  1.00 24.38 ? 133  GLU D CD  1 
ATOM   15367 O  OE1 . GLU D 1 141 ? 26.668  -26.905 97.610  1.00 30.25 ? 133  GLU D OE1 1 
ATOM   15368 O  OE2 . GLU D 1 141 ? 25.438  -25.528 96.399  1.00 27.17 ? 133  GLU D OE2 1 
ATOM   15369 N  N   . PHE D 1 142 ? 22.398  -29.489 94.491  1.00 28.56 ? 134  PHE D N   1 
ATOM   15370 C  CA  . PHE D 1 142 ? 21.672  -30.371 95.402  1.00 26.50 ? 134  PHE D CA  1 
ATOM   15371 C  C   . PHE D 1 142 ? 20.827  -31.439 94.720  1.00 27.60 ? 134  PHE D C   1 
ATOM   15372 O  O   . PHE D 1 142 ? 20.627  -32.505 95.311  1.00 30.54 ? 134  PHE D O   1 
ATOM   15373 C  CB  . PHE D 1 142 ? 20.776  -29.547 96.333  1.00 29.40 ? 134  PHE D CB  1 
ATOM   15374 C  CG  . PHE D 1 142 ? 21.530  -28.880 97.444  1.00 30.51 ? 134  PHE D CG  1 
ATOM   15375 C  CD1 . PHE D 1 142 ? 21.846  -29.580 98.599  1.00 29.33 ? 134  PHE D CD1 1 
ATOM   15376 C  CD2 . PHE D 1 142 ? 21.950  -27.564 97.321  1.00 24.65 ? 134  PHE D CD2 1 
ATOM   15377 C  CE1 . PHE D 1 142 ? 22.550  -28.972 99.623  1.00 27.18 ? 134  PHE D CE1 1 
ATOM   15378 C  CE2 . PHE D 1 142 ? 22.658  -26.954 98.341  1.00 25.98 ? 134  PHE D CE2 1 
ATOM   15379 C  CZ  . PHE D 1 142 ? 22.956  -27.661 99.491  1.00 27.74 ? 134  PHE D CZ  1 
ATOM   15380 N  N   . ASN D 1 143 ? 20.305  -31.199 93.520  1.00 27.09 ? 135  ASN D N   1 
ATOM   15381 C  CA  . ASN D 1 143 ? 19.398  -32.177 92.925  1.00 25.79 ? 135  ASN D CA  1 
ATOM   15382 C  C   . ASN D 1 143 ? 20.130  -33.464 92.573  1.00 30.29 ? 135  ASN D C   1 
ATOM   15383 O  O   . ASN D 1 143 ? 21.239  -33.446 92.034  1.00 27.94 ? 135  ASN D O   1 
ATOM   15384 C  CB  . ASN D 1 143 ? 18.720  -31.621 91.673  1.00 25.04 ? 135  ASN D CB  1 
ATOM   15385 C  CG  . ASN D 1 143 ? 17.654  -30.600 91.994  1.00 23.90 ? 135  ASN D CG  1 
ATOM   15386 O  OD1 . ASN D 1 143 ? 17.307  -30.395 93.154  1.00 28.60 ? 135  ASN D OD1 1 
ATOM   15387 N  ND2 . ASN D 1 143 ? 17.114  -29.964 90.961  1.00 23.20 ? 135  ASN D ND2 1 
ATOM   15388 N  N   . LYS D 1 144 ? 19.487  -34.583 92.883  1.00 28.32 ? 136  LYS D N   1 
ATOM   15389 C  CA  . LYS D 1 144 ? 19.969  -35.917 92.581  1.00 30.28 ? 136  LYS D CA  1 
ATOM   15390 C  C   . LYS D 1 144 ? 18.943  -36.626 91.706  1.00 40.61 ? 136  LYS D C   1 
ATOM   15391 O  O   . LYS D 1 144 ? 17.780  -36.217 91.629  1.00 41.12 ? 136  LYS D O   1 
ATOM   15392 C  CB  . LYS D 1 144 ? 20.208  -36.715 93.860  1.00 32.35 ? 136  LYS D CB  1 
ATOM   15393 C  CG  . LYS D 1 144 ? 21.055  -36.012 94.897  1.00 35.12 ? 136  LYS D CG  1 
ATOM   15394 C  CD  . LYS D 1 144 ? 22.487  -35.843 94.434  1.00 38.77 ? 136  LYS D CD  1 
ATOM   15395 C  CE  . LYS D 1 144 ? 23.397  -35.528 95.615  1.00 41.50 ? 136  LYS D CE  1 
ATOM   15396 N  NZ  . LYS D 1 144 ? 24.795  -35.258 95.192  1.00 43.85 ? 136  LYS D NZ  1 
ATOM   15397 N  N   . ASP D 1 145 ? 19.390  -37.694 91.044  1.00 40.37 ? 137  ASP D N   1 
ATOM   15398 C  CA  . ASP D 1 145 ? 18.555  -38.416 90.091  1.00 41.56 ? 137  ASP D CA  1 
ATOM   15399 C  C   . ASP D 1 145 ? 17.199  -38.744 90.698  1.00 43.96 ? 137  ASP D C   1 
ATOM   15400 O  O   . ASP D 1 145 ? 17.114  -39.363 91.763  1.00 43.03 ? 137  ASP D O   1 
ATOM   15401 C  CB  . ASP D 1 145 ? 19.264  -39.695 89.640  1.00 43.43 ? 137  ASP D CB  1 
ATOM   15402 N  N   . GLY D 1 146 ? 16.139  -38.287 90.033  1.00 50.58 ? 138  GLY D N   1 
ATOM   15403 C  CA  . GLY D 1 146 ? 14.785  -38.489 90.499  1.00 52.22 ? 138  GLY D CA  1 
ATOM   15404 C  C   . GLY D 1 146 ? 14.337  -37.586 91.629  1.00 48.19 ? 138  GLY D C   1 
ATOM   15405 O  O   . GLY D 1 146 ? 13.134  -37.540 91.915  1.00 54.15 ? 138  GLY D O   1 
ATOM   15406 N  N   . LEU D 1 147 ? 15.249  -36.862 92.277  1.00 38.51 ? 139  LEU D N   1 
ATOM   15407 C  CA  . LEU D 1 147 ? 14.953  -36.104 93.496  1.00 38.22 ? 139  LEU D CA  1 
ATOM   15408 C  C   . LEU D 1 147 ? 15.315  -34.635 93.278  1.00 32.83 ? 139  LEU D C   1 
ATOM   15409 O  O   . LEU D 1 147 ? 16.356  -34.164 93.742  1.00 29.14 ? 139  LEU D O   1 
ATOM   15410 C  CB  . LEU D 1 147 ? 15.715  -36.713 94.704  1.00 37.14 ? 139  LEU D CB  1 
ATOM   15411 C  CG  . LEU D 1 147 ? 15.346  -38.149 95.105  1.00 38.83 ? 139  LEU D CG  1 
ATOM   15412 C  CD1 . LEU D 1 147 ? 16.249  -38.645 96.224  1.00 38.42 ? 139  LEU D CD1 1 
ATOM   15413 C  CD2 . LEU D 1 147 ? 13.882  -38.253 95.518  1.00 36.92 ? 139  LEU D CD2 1 
ATOM   15414 N  N   . ASN D 1 148 ? 14.436  -33.907 92.584  1.00 31.11 ? 140  ASN D N   1 
ATOM   15415 C  CA  . ASN D 1 148 ? 14.682  -32.506 92.239  1.00 30.56 ? 140  ASN D CA  1 
ATOM   15416 C  C   . ASN D 1 148 ? 14.067  -31.613 93.310  1.00 34.11 ? 140  ASN D C   1 
ATOM   15417 O  O   . ASN D 1 148 ? 12.996  -31.023 93.144  1.00 33.18 ? 140  ASN D O   1 
ATOM   15418 C  CB  . ASN D 1 148 ? 14.130  -32.191 90.857  1.00 35.31 ? 140  ASN D CB  1 
ATOM   15419 C  CG  . ASN D 1 148 ? 14.826  -32.975 89.764  1.00 41.24 ? 140  ASN D CG  1 
ATOM   15420 O  OD1 . ASN D 1 148 ? 16.044  -33.169 89.800  1.00 35.71 ? 140  ASN D OD1 1 
ATOM   15421 N  ND2 . ASN D 1 148 ? 14.055  -33.441 88.788  1.00 51.20 ? 140  ASN D ND2 1 
ATOM   15422 N  N   . ILE D 1 149 ? 14.779  -31.506 94.432  1.00 33.13 ? 141  ILE D N   1 
ATOM   15423 C  CA  . ILE D 1 149 ? 14.283  -30.723 95.558  1.00 29.96 ? 141  ILE D CA  1 
ATOM   15424 C  C   . ILE D 1 149 ? 14.395  -29.221 95.330  1.00 30.28 ? 141  ILE D C   1 
ATOM   15425 O  O   . ILE D 1 149 ? 13.747  -28.447 96.048  1.00 26.16 ? 141  ILE D O   1 
ATOM   15426 C  CB  . ILE D 1 149 ? 15.018  -31.136 96.838  1.00 28.19 ? 141  ILE D CB  1 
ATOM   15427 C  CG1 . ILE D 1 149 ? 16.526  -30.930 96.675  1.00 26.80 ? 141  ILE D CG1 1 
ATOM   15428 C  CG2 . ILE D 1 149 ? 14.710  -32.593 97.157  1.00 26.05 ? 141  ILE D CG2 1 
ATOM   15429 C  CD1 . ILE D 1 149 ? 17.262  -30.846 97.997  1.00 26.30 ? 141  ILE D CD1 1 
ATOM   15430 N  N   . VAL D 1 150 ? 15.192  -28.778 94.359  1.00 26.82 ? 142  VAL D N   1 
ATOM   15431 C  CA  . VAL D 1 150 ? 15.194  -27.385 93.922  1.00 25.15 ? 142  VAL D CA  1 
ATOM   15432 C  C   . VAL D 1 150 ? 14.629  -27.348 92.511  1.00 25.28 ? 142  VAL D C   1 
ATOM   15433 O  O   . VAL D 1 150 ? 15.272  -27.807 91.561  1.00 24.85 ? 142  VAL D O   1 
ATOM   15434 C  CB  . VAL D 1 150 ? 16.590  -26.754 93.957  1.00 24.25 ? 142  VAL D CB  1 
ATOM   15435 C  CG1 . VAL D 1 150 ? 16.486  -25.272 93.581  1.00 19.23 ? 142  VAL D CG1 1 
ATOM   15436 C  CG2 . VAL D 1 150 ? 17.233  -26.939 95.322  1.00 27.74 ? 142  VAL D CG2 1 
ATOM   15437 N  N   . ASP D 1 151 ? 13.430  -26.789 92.371  1.00 22.73 ? 143  ASP D N   1 
ATOM   15438 C  CA  . ASP D 1 151 ? 12.772  -26.728 91.069  1.00 23.36 ? 143  ASP D CA  1 
ATOM   15439 C  C   . ASP D 1 151 ? 11.636  -25.709 91.196  1.00 19.25 ? 143  ASP D C   1 
ATOM   15440 O  O   . ASP D 1 151 ? 10.526  -26.069 91.584  1.00 19.66 ? 143  ASP D O   1 
ATOM   15441 C  CB  . ASP D 1 151 ? 12.249  -28.087 90.651  1.00 25.12 ? 143  ASP D CB  1 
ATOM   15442 C  CG  . ASP D 1 151 ? 11.520  -28.057 89.322  1.00 26.61 ? 143  ASP D CG  1 
ATOM   15443 O  OD1 . ASP D 1 151 ? 11.730  -27.112 88.545  1.00 26.99 ? 143  ASP D OD1 1 
ATOM   15444 O  OD2 . ASP D 1 151 ? 10.725  -28.982 89.061  1.00 33.33 ? 143  ASP D OD2 1 
ATOM   15445 N  N   . HIS D 1 152 ? 11.924  -24.452 90.868  1.00 18.30 ? 144  HIS D N   1 
ATOM   15446 C  CA  . HIS D 1 152 ? 10.861  -23.451 90.890  1.00 22.77 ? 144  HIS D CA  1 
ATOM   15447 C  C   . HIS D 1 152 ? 11.218  -22.292 89.973  1.00 24.91 ? 144  HIS D C   1 
ATOM   15448 O  O   . HIS D 1 152 ? 12.361  -22.134 89.546  1.00 19.01 ? 144  HIS D O   1 
ATOM   15449 C  CB  . HIS D 1 152 ? 10.580  -22.947 92.308  1.00 20.02 ? 144  HIS D CB  1 
ATOM   15450 C  CG  . HIS D 1 152 ? 11.777  -22.379 93.000  1.00 20.12 ? 144  HIS D CG  1 
ATOM   15451 N  ND1 . HIS D 1 152 ? 12.551  -23.119 93.870  1.00 19.33 ? 144  HIS D ND1 1 
ATOM   15452 C  CD2 . HIS D 1 152 ? 12.321  -21.137 92.968  1.00 20.81 ? 144  HIS D CD2 1 
ATOM   15453 C  CE1 . HIS D 1 152 ? 13.526  -22.356 94.339  1.00 21.23 ? 144  HIS D CE1 1 
ATOM   15454 N  NE2 . HIS D 1 152 ? 13.407  -21.150 93.809  1.00 20.03 ? 144  HIS D NE2 1 
ATOM   15455 N  N   . TYR D 1 153 ? 10.208  -21.484 89.672  1.00 16.35 ? 145  TYR D N   1 
ATOM   15456 C  CA  . TYR D 1 153 ? 10.324  -20.416 88.695  1.00 21.44 ? 145  TYR D CA  1 
ATOM   15457 C  C   . TYR D 1 153 ? 10.441  -19.066 89.374  1.00 19.31 ? 145  TYR D C   1 
ATOM   15458 O  O   . TYR D 1 153 ? 10.132  -18.899 90.557  1.00 18.07 ? 145  TYR D O   1 
ATOM   15459 C  CB  . TYR D 1 153 ? 9.125   -20.415 87.743  1.00 25.43 ? 145  TYR D CB  1 
ATOM   15460 C  CG  . TYR D 1 153 ? 9.237   -21.494 86.699  1.00 24.82 ? 145  TYR D CG  1 
ATOM   15461 C  CD1 . TYR D 1 153 ? 9.040   -22.828 87.033  1.00 32.78 ? 145  TYR D CD1 1 
ATOM   15462 C  CD2 . TYR D 1 153 ? 9.567   -21.183 85.387  1.00 21.73 ? 145  TYR D CD2 1 
ATOM   15463 C  CE1 . TYR D 1 153 ? 9.161   -23.825 86.088  1.00 39.54 ? 145  TYR D CE1 1 
ATOM   15464 C  CE2 . TYR D 1 153 ? 9.687   -22.174 84.435  1.00 27.63 ? 145  TYR D CE2 1 
ATOM   15465 C  CZ  . TYR D 1 153 ? 9.485   -23.493 84.792  1.00 40.56 ? 145  TYR D CZ  1 
ATOM   15466 O  OH  . TYR D 1 153 ? 9.608   -24.489 83.849  1.00 51.40 ? 145  TYR D OH  1 
ATOM   15467 N  N   . THR D 1 154 ? 10.901  -18.096 88.594  1.00 16.01 ? 146  THR D N   1 
ATOM   15468 C  CA  . THR D 1 154 ? 11.008  -16.712 89.028  1.00 16.01 ? 146  THR D CA  1 
ATOM   15469 C  C   . THR D 1 154 ? 10.233  -15.887 88.016  1.00 15.82 ? 146  THR D C   1 
ATOM   15470 O  O   . THR D 1 154 ? 10.628  -15.798 86.851  1.00 15.31 ? 146  THR D O   1 
ATOM   15471 C  CB  . THR D 1 154 ? 12.471  -16.263 89.122  1.00 16.51 ? 146  THR D CB  1 
ATOM   15472 O  OG1 . THR D 1 154 ? 13.207  -17.181 89.951  1.00 17.49 ? 146  THR D OG1 1 
ATOM   15473 C  CG2 . THR D 1 154 ? 12.568  -14.861 89.742  1.00 12.70 ? 146  THR D CG2 1 
ATOM   15474 N  N   . TYR D 1 155 ? 9.117   -15.314 88.450  1.00 13.22 ? 147  TYR D N   1 
ATOM   15475 C  CA  . TYR D 1 155 ? 8.247   -14.512 87.603  1.00 13.90 ? 147  TYR D CA  1 
ATOM   15476 C  C   . TYR D 1 155 ? 8.367   -13.039 87.978  1.00 17.21 ? 147  TYR D C   1 
ATOM   15477 O  O   . TYR D 1 155 ? 8.435   -12.703 89.163  1.00 16.38 ? 147  TYR D O   1 
ATOM   15478 C  CB  . TYR D 1 155 ? 6.789   -14.949 87.760  1.00 16.49 ? 147  TYR D CB  1 
ATOM   15479 C  CG  . TYR D 1 155 ? 6.469   -16.364 87.354  1.00 17.39 ? 147  TYR D CG  1 
ATOM   15480 C  CD1 . TYR D 1 155 ? 6.322   -16.709 86.015  1.00 17.31 ? 147  TYR D CD1 1 
ATOM   15481 C  CD2 . TYR D 1 155 ? 6.268   -17.353 88.316  1.00 18.14 ? 147  TYR D CD2 1 
ATOM   15482 C  CE1 . TYR D 1 155 ? 5.997   -18.017 85.645  1.00 18.24 ? 147  TYR D CE1 1 
ATOM   15483 C  CE2 . TYR D 1 155 ? 5.947   -18.643 87.962  1.00 19.99 ? 147  TYR D CE2 1 
ATOM   15484 C  CZ  . TYR D 1 155 ? 5.816   -18.973 86.626  1.00 19.43 ? 147  TYR D CZ  1 
ATOM   15485 O  OH  . TYR D 1 155 ? 5.490   -20.266 86.283  1.00 17.25 ? 147  TYR D OH  1 
ATOM   15486 N  N   . VAL D 1 156 ? 8.357   -12.157 86.967  1.00 13.34 ? 148  VAL D N   1 
ATOM   15487 C  CA  . VAL D 1 156 ? 8.535   -10.718 87.154  1.00 12.81 ? 148  VAL D CA  1 
ATOM   15488 C  C   . VAL D 1 156 ? 7.481   -9.955  86.357  1.00 14.03 ? 148  VAL D C   1 
ATOM   15489 O  O   . VAL D 1 156 ? 7.211   -10.280 85.194  1.00 15.13 ? 148  VAL D O   1 
ATOM   15490 C  CB  . VAL D 1 156 ? 9.943   -10.253 86.714  1.00 17.04 ? 148  VAL D CB  1 
ATOM   15491 C  CG1 . VAL D 1 156 ? 10.212  -8.801  87.160  1.00 15.11 ? 148  VAL D CG1 1 
ATOM   15492 C  CG2 . VAL D 1 156 ? 11.002  -11.191 87.243  1.00 14.84 ? 148  VAL D CG2 1 
ATOM   15493 N  N   . PHE D 1 157 ? 6.885   -8.943  86.986  1.00 11.60 ? 149  PHE D N   1 
ATOM   15494 C  CA  . PHE D 1 157 ? 6.150   -7.901  86.272  1.00 13.08 ? 149  PHE D CA  1 
ATOM   15495 C  C   . PHE D 1 157 ? 7.062   -6.683  86.187  1.00 14.73 ? 149  PHE D C   1 
ATOM   15496 O  O   . PHE D 1 157 ? 7.664   -6.282  87.187  1.00 16.74 ? 149  PHE D O   1 
ATOM   15497 C  CB  . PHE D 1 157 ? 4.832   -7.527  86.965  1.00 11.74 ? 149  PHE D CB  1 
ATOM   15498 C  CG  . PHE D 1 157 ? 3.727   -8.564  86.830  1.00 13.28 ? 149  PHE D CG  1 
ATOM   15499 C  CD1 . PHE D 1 157 ? 3.958   -9.782  86.218  1.00 19.76 ? 149  PHE D CD1 1 
ATOM   15500 C  CD2 . PHE D 1 157 ? 2.450   -8.298  87.311  1.00 15.38 ? 149  PHE D CD2 1 
ATOM   15501 C  CE1 . PHE D 1 157 ? 2.950   -10.726 86.100  1.00 20.55 ? 149  PHE D CE1 1 
ATOM   15502 C  CE2 . PHE D 1 157 ? 1.428   -9.244  87.193  1.00 14.76 ? 149  PHE D CE2 1 
ATOM   15503 C  CZ  . PHE D 1 157 ? 1.687   -10.458 86.586  1.00 18.14 ? 149  PHE D CZ  1 
ATOM   15504 N  N   . MET D 1 158 ? 7.204   -6.114  84.996  1.00 14.94 ? 150  MET D N   1 
ATOM   15505 C  CA  . MET D 1 158 ? 8.018   -4.915  84.885  1.00 15.36 ? 150  MET D CA  1 
ATOM   15506 C  C   . MET D 1 158 ? 7.402   -3.979  83.859  1.00 14.30 ? 150  MET D C   1 
ATOM   15507 O  O   . MET D 1 158 ? 6.583   -4.386  83.033  1.00 14.62 ? 150  MET D O   1 
ATOM   15508 C  CB  . MET D 1 158 ? 9.494   -5.248  84.565  1.00 22.24 ? 150  MET D CB  1 
ATOM   15509 C  CG  . MET D 1 158 ? 9.800   -5.789  83.193  1.00 26.55 ? 150  MET D CG  1 
ATOM   15510 S  SD  . MET D 1 158 ? 11.541  -6.344  83.069  1.00 20.86 ? 150  MET D SD  1 
ATOM   15511 C  CE  . MET D 1 158 ? 12.432  -4.818  83.323  1.00 19.64 ? 150  MET D CE  1 
ATOM   15512 N  N   . GLY D 1 159 ? 7.792   -2.704  83.949  1.00 14.63 ? 151  GLY D N   1 
ATOM   15513 C  CA  . GLY D 1 159 ? 7.225   -1.645  83.142  1.00 16.32 ? 151  GLY D CA  1 
ATOM   15514 C  C   . GLY D 1 159 ? 8.273   -0.921  82.311  1.00 13.64 ? 151  GLY D C   1 
ATOM   15515 O  O   . GLY D 1 159 ? 9.460   -1.258  82.325  1.00 14.58 ? 151  GLY D O   1 
ATOM   15516 N  N   . ASP D 1 160 ? 7.790   0.079   81.560  1.00 11.88 ? 152  ASP D N   1 
ATOM   15517 C  CA  . ASP D 1 160 ? 8.643   0.848   80.651  1.00 15.60 ? 152  ASP D CA  1 
ATOM   15518 C  C   . ASP D 1 160 ? 9.786   1.536   81.386  1.00 16.66 ? 152  ASP D C   1 
ATOM   15519 O  O   . ASP D 1 160 ? 10.913  1.609   80.871  1.00 15.07 ? 152  ASP D O   1 
ATOM   15520 C  CB  . ASP D 1 160 ? 7.804   1.899   79.919  1.00 22.31 ? 152  ASP D CB  1 
ATOM   15521 C  CG  . ASP D 1 160 ? 6.711   1.280   79.057  1.00 30.72 ? 152  ASP D CG  1 
ATOM   15522 O  OD1 . ASP D 1 160 ? 7.029   0.380   78.251  1.00 30.19 ? 152  ASP D OD1 1 
ATOM   15523 O  OD2 . ASP D 1 160 ? 5.534   1.682   79.195  1.00 33.82 ? 152  ASP D OD2 1 
ATOM   15524 N  N   . GLY D 1 161 ? 9.510   2.079   82.568  1.00 11.46 ? 153  GLY D N   1 
ATOM   15525 C  CA  . GLY D 1 161 ? 10.539  2.779   83.328  1.00 11.48 ? 153  GLY D CA  1 
ATOM   15526 C  C   . GLY D 1 161 ? 11.685  1.855   83.704  1.00 13.57 ? 153  GLY D C   1 
ATOM   15527 O  O   . GLY D 1 161 ? 12.863  2.214   83.595  1.00 13.57 ? 153  GLY D O   1 
HETATM 15528 N  N   . OCS D 1 162 ? 11.335  0.664   84.174  1.00 10.67 ? 154  OCS D N   1 
HETATM 15529 C  CA  . OCS D 1 162 ? 12.327  -0.393  84.428  1.00 10.46 ? 154  OCS D CA  1 
HETATM 15530 C  CB  . OCS D 1 162 ? 11.625  -1.680  84.781  1.00 10.45 ? 154  OCS D CB  1 
HETATM 15531 S  SG  . OCS D 1 162 ? 10.638  -1.569  86.272  1.00 19.05 ? 154  OCS D SG  1 
HETATM 15532 C  C   . OCS D 1 162 ? 13.233  -0.665  83.236  1.00 12.51 ? 154  OCS D C   1 
HETATM 15533 O  O   . OCS D 1 162 ? 14.444  -0.792  83.367  1.00 14.28 ? 154  OCS D O   1 
HETATM 15534 O  OD1 . OCS D 1 162 ? 9.747   -2.662  86.265  1.00 20.04 ? 154  OCS D OD1 1 
HETATM 15535 O  OD2 . OCS D 1 162 ? 11.536  -1.642  87.382  1.00 17.08 ? 154  OCS D OD2 1 
HETATM 15536 O  OD3 . OCS D 1 162 ? 9.887   -0.375  86.311  1.00 42.89 ? 154  OCS D OD3 1 
ATOM   15537 N  N   . LEU D 1 163 ? 12.616  -0.776  82.068  1.00 12.28 ? 155  LEU D N   1 
ATOM   15538 C  CA  . LEU D 1 163 ? 13.327  -1.135  80.848  1.00 11.25 ? 155  LEU D CA  1 
ATOM   15539 C  C   . LEU D 1 163 ? 14.217  -0.005  80.323  1.00 11.75 ? 155  LEU D C   1 
ATOM   15540 O  O   . LEU D 1 163 ? 15.235  -0.270  79.672  1.00 11.51 ? 155  LEU D O   1 
ATOM   15541 C  CB  . LEU D 1 163 ? 12.318  -1.550  79.777  1.00 11.67 ? 155  LEU D CB  1 
ATOM   15542 C  CG  . LEU D 1 163 ? 11.657  -2.911  79.993  1.00 12.68 ? 155  LEU D CG  1 
ATOM   15543 C  CD1 . LEU D 1 163 ? 10.543  -3.117  78.973  1.00 16.70 ? 155  LEU D CD1 1 
ATOM   15544 C  CD2 . LEU D 1 163 ? 12.704  -4.034  79.920  1.00 14.02 ? 155  LEU D CD2 1 
ATOM   15545 N  N   . MET D 1 164 ? 13.834  1.247   80.606  1.00 11.66 ? 156  MET D N   1 
ATOM   15546 C  CA  . MET D 1 164 ? 14.673  2.381   80.224  1.00 12.12 ? 156  MET D CA  1 
ATOM   15547 C  C   . MET D 1 164 ? 15.945  2.450   81.060  1.00 12.89 ? 156  MET D C   1 
ATOM   15548 O  O   . MET D 1 164 ? 16.981  2.903   80.560  1.00 11.74 ? 156  MET D O   1 
ATOM   15549 C  CB  . MET D 1 164 ? 13.903  3.696   80.358  1.00 11.76 ? 156  MET D CB  1 
ATOM   15550 C  CG  . MET D 1 164 ? 13.167  4.099   79.085  1.00 18.10 ? 156  MET D CG  1 
ATOM   15551 S  SD  . MET D 1 164 ? 12.257  5.644   79.228  1.00 15.94 ? 156  MET D SD  1 
ATOM   15552 C  CE  . MET D 1 164 ? 10.661  5.072   79.838  1.00 16.21 ? 156  MET D CE  1 
ATOM   15553 N  N   . GLU D 1 165 ? 15.880  2.015   82.320  1.00 10.88 ? 157  GLU D N   1 
ATOM   15554 C  CA  . GLU D 1 165 ? 17.026  2.067   83.225  1.00 13.63 ? 157  GLU D CA  1 
ATOM   15555 C  C   . GLU D 1 165 ? 18.157  1.138   82.782  1.00 12.91 ? 157  GLU D C   1 
ATOM   15556 O  O   . GLU D 1 165 ? 17.928  -0.018  82.425  1.00 12.82 ? 157  GLU D O   1 
ATOM   15557 C  CB  . GLU D 1 165 ? 16.603  1.673   84.637  1.00 12.40 ? 157  GLU D CB  1 
ATOM   15558 C  CG  . GLU D 1 165 ? 15.817  2.728   85.383  1.00 10.30 ? 157  GLU D CG  1 
ATOM   15559 C  CD  . GLU D 1 165 ? 16.643  3.935   85.769  1.00 12.71 ? 157  GLU D CD  1 
ATOM   15560 O  OE1 . GLU D 1 165 ? 17.875  3.963   85.545  1.00 12.36 ? 157  GLU D OE1 1 
ATOM   15561 O  OE2 . GLU D 1 165 ? 16.044  4.880   86.305  1.00 12.41 ? 157  GLU D OE2 1 
ATOM   15562 N  N   . GLY D 1 166 ? 19.392  1.631   82.890  1.00 10.75 ? 158  GLY D N   1 
ATOM   15563 C  CA  . GLY D 1 166 ? 20.545  0.835   82.493  1.00 10.87 ? 158  GLY D CA  1 
ATOM   15564 C  C   . GLY D 1 166 ? 20.721  -0.454  83.279  1.00 11.80 ? 158  GLY D C   1 
ATOM   15565 O  O   . GLY D 1 166 ? 21.228  -1.443  82.749  1.00 12.15 ? 158  GLY D O   1 
ATOM   15566 N  N   . VAL D 1 167 ? 20.296  -0.477  84.545  1.00 10.63 ? 159  VAL D N   1 
ATOM   15567 C  CA  . VAL D 1 167 ? 20.472  -1.699  85.321  1.00 10.89 ? 159  VAL D CA  1 
ATOM   15568 C  C   . VAL D 1 167 ? 19.625  -2.845  84.765  1.00 16.87 ? 159  VAL D C   1 
ATOM   15569 O  O   . VAL D 1 167 ? 19.993  -4.019  84.921  1.00 13.17 ? 159  VAL D O   1 
ATOM   15570 C  CB  . VAL D 1 167 ? 20.197  -1.411  86.812  1.00 10.37 ? 159  VAL D CB  1 
ATOM   15571 C  CG1 . VAL D 1 167 ? 18.726  -1.075  87.061  1.00 11.28 ? 159  VAL D CG1 1 
ATOM   15572 C  CG2 . VAL D 1 167 ? 20.679  -2.588  87.690  1.00 14.56 ? 159  VAL D CG2 1 
ATOM   15573 N  N   . SER D 1 168 ? 18.531  -2.546  84.058  1.00 10.43 ? 160  SER D N   1 
ATOM   15574 C  CA  . SER D 1 168 ? 17.785  -3.623  83.411  1.00 14.92 ? 160  SER D CA  1 
ATOM   15575 C  C   . SER D 1 168 ? 18.567  -4.194  82.238  1.00 12.34 ? 160  SER D C   1 
ATOM   15576 O  O   . SER D 1 168 ? 18.516  -5.402  81.978  1.00 14.22 ? 160  SER D O   1 
ATOM   15577 C  CB  . SER D 1 168 ? 16.403  -3.136  82.955  1.00 15.99 ? 160  SER D CB  1 
ATOM   15578 O  OG  . SER D 1 168 ? 16.472  -2.342  81.772  1.00 18.88 ? 160  SER D OG  1 
ATOM   15579 N  N   . HIS D 1 169 ? 19.291  -3.337  81.518  1.00 12.22 ? 161  HIS D N   1 
ATOM   15580 C  CA  . HIS D 1 169 ? 20.196  -3.809  80.476  1.00 15.23 ? 161  HIS D CA  1 
ATOM   15581 C  C   . HIS D 1 169 ? 21.243  -4.760  81.042  1.00 15.51 ? 161  HIS D C   1 
ATOM   15582 O  O   . HIS D 1 169 ? 21.488  -5.829  80.487  1.00 11.86 ? 161  HIS D O   1 
ATOM   15583 C  CB  . HIS D 1 169 ? 20.886  -2.618  79.806  1.00 11.63 ? 161  HIS D CB  1 
ATOM   15584 C  CG  . HIS D 1 169 ? 22.055  -2.995  78.955  1.00 12.03 ? 161  HIS D CG  1 
ATOM   15585 N  ND1 . HIS D 1 169 ? 21.935  -3.791  77.835  1.00 12.45 ? 161  HIS D ND1 1 
ATOM   15586 C  CD2 . HIS D 1 169 ? 23.363  -2.667  79.045  1.00 12.15 ? 161  HIS D CD2 1 
ATOM   15587 C  CE1 . HIS D 1 169 ? 23.123  -3.945  77.277  1.00 18.14 ? 161  HIS D CE1 1 
ATOM   15588 N  NE2 . HIS D 1 169 ? 24.008  -3.268  77.988  1.00 14.52 ? 161  HIS D NE2 1 
ATOM   15589 N  N   . GLU D 1 170 ? 21.892  -4.372  82.142  1.00 11.29 ? 162  GLU D N   1 
ATOM   15590 C  CA  . GLU D 1 170 ? 22.965  -5.198  82.686  1.00 16.10 ? 162  GLU D CA  1 
ATOM   15591 C  C   . GLU D 1 170 ? 22.438  -6.552  83.140  1.00 17.08 ? 162  GLU D C   1 
ATOM   15592 O  O   . GLU D 1 170 ? 22.987  -7.602  82.776  1.00 11.88 ? 162  GLU D O   1 
ATOM   15593 C  CB  . GLU D 1 170 ? 23.655  -4.459  83.834  1.00 12.48 ? 162  GLU D CB  1 
ATOM   15594 C  CG  . GLU D 1 170 ? 24.268  -3.127  83.406  1.00 14.08 ? 162  GLU D CG  1 
ATOM   15595 C  CD  . GLU D 1 170 ? 24.975  -2.407  84.547  1.00 15.18 ? 162  GLU D CD  1 
ATOM   15596 O  OE1 . GLU D 1 170 ? 25.188  -3.030  85.608  1.00 15.05 ? 162  GLU D OE1 1 
ATOM   15597 O  OE2 . GLU D 1 170 ? 25.313  -1.215  84.381  1.00 13.26 ? 162  GLU D OE2 1 
ATOM   15598 N  N   . ALA D 1 171 ? 21.351  -6.549  83.914  1.00 11.20 ? 163  ALA D N   1 
ATOM   15599 C  CA  . ALA D 1 171 ? 20.835  -7.799  84.474  1.00 15.78 ? 163  ALA D CA  1 
ATOM   15600 C  C   . ALA D 1 171 ? 20.266  -8.717  83.394  1.00 14.39 ? 163  ALA D C   1 
ATOM   15601 O  O   . ALA D 1 171 ? 20.495  -9.928  83.425  1.00 12.26 ? 163  ALA D O   1 
ATOM   15602 C  CB  . ALA D 1 171 ? 19.767  -7.506  85.526  1.00 12.61 ? 163  ALA D CB  1 
ATOM   15603 N  N   . CYS D 1 172 ? 19.511  -8.180  82.442  1.00 13.49 ? 164  CYS D N   1 
ATOM   15604 C  CA  . CYS D 1 172 ? 18.941  -9.068  81.429  1.00 12.26 ? 164  CYS D CA  1 
ATOM   15605 C  C   . CYS D 1 172 ? 19.997  -9.566  80.443  1.00 14.67 ? 164  CYS D C   1 
ATOM   15606 O  O   . CYS D 1 172 ? 19.886  -10.687 79.932  1.00 13.87 ? 164  CYS D O   1 
ATOM   15607 C  CB  . CYS D 1 172 ? 17.795  -8.366  80.705  1.00 17.91 ? 164  CYS D CB  1 
ATOM   15608 S  SG  . CYS D 1 172 ? 16.429  -8.011  81.832  1.00 15.68 ? 164  CYS D SG  1 
ATOM   15609 N  N   . SER D 1 173 ? 21.021  -8.761  80.167  1.00 13.19 ? 165  SER D N   1 
ATOM   15610 C  CA  . SER D 1 173 ? 22.135  -9.247  79.366  1.00 14.48 ? 165  SER D CA  1 
ATOM   15611 C  C   . SER D 1 173 ? 22.765  -10.460 80.031  1.00 15.09 ? 165  SER D C   1 
ATOM   15612 O  O   . SER D 1 173 ? 22.948  -11.503 79.401  1.00 13.82 ? 165  SER D O   1 
ATOM   15613 C  CB  . SER D 1 173 ? 23.166  -8.126  79.165  1.00 12.93 ? 165  SER D CB  1 
ATOM   15614 O  OG  . SER D 1 173 ? 24.287  -8.562  78.398  1.00 17.06 ? 165  SER D OG  1 
ATOM   15615 N  N   . LEU D 1 174 ? 23.031  -10.361 81.333  1.00 14.66 ? 166  LEU D N   1 
ATOM   15616 C  CA  . LEU D 1 174 ? 23.674  -11.462 82.038  1.00 16.00 ? 166  LEU D CA  1 
ATOM   15617 C  C   . LEU D 1 174 ? 22.743  -12.661 82.144  1.00 14.68 ? 166  LEU D C   1 
ATOM   15618 O  O   . LEU D 1 174 ? 23.188  -13.809 82.013  1.00 16.00 ? 166  LEU D O   1 
ATOM   15619 C  CB  . LEU D 1 174 ? 24.127  -10.995 83.425  1.00 15.36 ? 166  LEU D CB  1 
ATOM   15620 C  CG  . LEU D 1 174 ? 24.988  -11.981 84.217  1.00 21.20 ? 166  LEU D CG  1 
ATOM   15621 C  CD1 . LEU D 1 174 ? 26.248  -12.384 83.438  1.00 20.40 ? 166  LEU D CD1 1 
ATOM   15622 C  CD2 . LEU D 1 174 ? 25.368  -11.381 85.558  1.00 20.74 ? 166  LEU D CD2 1 
ATOM   15623 N  N   . ALA D 1 175 ? 21.442  -12.410 82.368  1.00 14.34 ? 167  ALA D N   1 
ATOM   15624 C  CA  . ALA D 1 175 ? 20.459  -13.491 82.392  1.00 14.28 ? 167  ALA D CA  1 
ATOM   15625 C  C   . ALA D 1 175 ? 20.435  -14.250 81.071  1.00 15.23 ? 167  ALA D C   1 
ATOM   15626 O  O   . ALA D 1 175 ? 20.278  -15.476 81.055  1.00 14.62 ? 167  ALA D O   1 
ATOM   15627 C  CB  . ALA D 1 175 ? 19.070  -12.930 82.702  1.00 15.89 ? 167  ALA D CB  1 
ATOM   15628 N  N   . GLY D 1 176 ? 20.585  -13.536 79.954  1.00 16.04 ? 168  GLY D N   1 
ATOM   15629 C  CA  . GLY D 1 176 ? 20.662  -14.199 78.662  1.00 14.75 ? 168  GLY D CA  1 
ATOM   15630 C  C   . GLY D 1 176 ? 21.892  -15.081 78.528  1.00 19.45 ? 168  GLY D C   1 
ATOM   15631 O  O   . GLY D 1 176 ? 21.799  -16.228 78.085  1.00 18.18 ? 168  GLY D O   1 
ATOM   15632 N  N   . THR D 1 177 ? 23.062  -14.562 78.913  1.00 16.61 ? 169  THR D N   1 
ATOM   15633 C  CA  A THR D 1 177 ? 24.288  -15.342 78.780  0.72 19.01 ? 169  THR D CA  1 
ATOM   15634 C  CA  B THR D 1 177 ? 24.295  -15.343 78.791  0.28 19.35 ? 169  THR D CA  1 
ATOM   15635 C  C   . THR D 1 177 ? 24.234  -16.607 79.628  1.00 24.73 ? 169  THR D C   1 
ATOM   15636 O  O   . THR D 1 177 ? 24.744  -17.662 79.222  1.00 20.58 ? 169  THR D O   1 
ATOM   15637 C  CB  A THR D 1 177 ? 25.493  -14.480 79.166  0.72 18.47 ? 169  THR D CB  1 
ATOM   15638 C  CB  B THR D 1 177 ? 25.505  -14.525 79.231  0.28 18.22 ? 169  THR D CB  1 
ATOM   15639 O  OG1 A THR D 1 177 ? 25.558  -13.345 78.292  0.72 18.46 ? 169  THR D OG1 1 
ATOM   15640 O  OG1 B THR D 1 177 ? 25.478  -14.364 80.653  0.28 15.69 ? 169  THR D OG1 1 
ATOM   15641 C  CG2 A THR D 1 177 ? 26.779  -15.274 79.052  0.72 18.00 ? 169  THR D CG2 1 
ATOM   15642 C  CG2 B THR D 1 177 ? 25.474  -13.188 78.604  0.28 18.54 ? 169  THR D CG2 1 
ATOM   15643 N  N   . LEU D 1 178 ? 23.622  -16.520 80.798  1.00 18.27 ? 170  LEU D N   1 
ATOM   15644 C  CA  . LEU D 1 178 ? 23.585  -17.628 81.730  1.00 20.77 ? 170  LEU D CA  1 
ATOM   15645 C  C   . LEU D 1 178 ? 22.416  -18.571 81.475  1.00 22.26 ? 170  LEU D C   1 
ATOM   15646 O  O   . LEU D 1 178 ? 22.304  -19.591 82.162  1.00 26.04 ? 170  LEU D O   1 
ATOM   15647 C  CB  . LEU D 1 178 ? 23.554  -17.081 83.164  1.00 16.92 ? 170  LEU D CB  1 
ATOM   15648 C  CG  . LEU D 1 178 ? 24.864  -16.381 83.579  1.00 20.76 ? 170  LEU D CG  1 
ATOM   15649 C  CD1 . LEU D 1 178 ? 24.814  -15.889 85.020  1.00 18.54 ? 170  LEU D CD1 1 
ATOM   15650 C  CD2 . LEU D 1 178 ? 26.059  -17.304 83.377  1.00 24.77 ? 170  LEU D CD2 1 
ATOM   15651 N  N   . GLY D 1 179 ? 21.559  -18.264 80.500  1.00 20.84 ? 171  GLY D N   1 
ATOM   15652 C  CA  . GLY D 1 179 ? 20.507  -19.176 80.082  1.00 18.81 ? 171  GLY D CA  1 
ATOM   15653 C  C   . GLY D 1 179 ? 19.498  -19.490 81.170  1.00 18.62 ? 171  GLY D C   1 
ATOM   15654 O  O   . GLY D 1 179 ? 19.155  -20.655 81.398  1.00 18.22 ? 171  GLY D O   1 
ATOM   15655 N  N   . LEU D 1 180 ? 19.008  -18.450 81.847  1.00 19.20 ? 172  LEU D N   1 
ATOM   15656 C  CA  . LEU D 1 180 ? 18.100  -18.621 82.983  1.00 16.55 ? 172  LEU D CA  1 
ATOM   15657 C  C   . LEU D 1 180 ? 16.677  -18.882 82.480  1.00 22.08 ? 172  LEU D C   1 
ATOM   15658 O  O   . LEU D 1 180 ? 15.793  -18.019 82.520  1.00 16.21 ? 172  LEU D O   1 
ATOM   15659 C  CB  . LEU D 1 180 ? 18.165  -17.402 83.887  1.00 17.11 ? 172  LEU D CB  1 
ATOM   15660 C  CG  . LEU D 1 180 ? 19.552  -17.056 84.437  1.00 20.74 ? 172  LEU D CG  1 
ATOM   15661 C  CD1 . LEU D 1 180 ? 19.461  -15.826 85.319  1.00 15.87 ? 172  LEU D CD1 1 
ATOM   15662 C  CD2 . LEU D 1 180 ? 20.136  -18.236 85.215  1.00 20.08 ? 172  LEU D CD2 1 
ATOM   15663 N  N   . GLY D 1 181 ? 16.449  -20.125 82.043  1.00 20.18 ? 173  GLY D N   1 
ATOM   15664 C  CA  . GLY D 1 181 ? 15.181  -20.507 81.436  1.00 21.07 ? 173  GLY D CA  1 
ATOM   15665 C  C   . GLY D 1 181 ? 14.001  -20.521 82.388  1.00 22.50 ? 173  GLY D C   1 
ATOM   15666 O  O   . GLY D 1 181 ? 12.855  -20.561 81.934  1.00 24.98 ? 173  GLY D O   1 
ATOM   15667 N  N   . LYS D 1 182 ? 14.247  -20.496 83.693  1.00 18.73 ? 174  LYS D N   1 
ATOM   15668 C  CA  . LYS D 1 182 ? 13.164  -20.442 84.662  1.00 16.14 ? 174  LYS D CA  1 
ATOM   15669 C  C   . LYS D 1 182 ? 12.785  -19.017 85.051  1.00 22.29 ? 174  LYS D C   1 
ATOM   15670 O  O   . LYS D 1 182 ? 11.888  -18.837 85.881  1.00 19.51 ? 174  LYS D O   1 
ATOM   15671 C  CB  . LYS D 1 182 ? 13.537  -21.249 85.908  1.00 16.48 ? 174  LYS D CB  1 
ATOM   15672 C  CG  . LYS D 1 182 ? 13.803  -22.717 85.629  1.00 28.14 ? 174  LYS D CG  1 
ATOM   15673 C  CD  . LYS D 1 182 ? 13.526  -23.536 86.868  1.00 30.23 ? 174  LYS D CD  1 
ATOM   15674 C  CE  . LYS D 1 182 ? 14.073  -24.925 86.738  1.00 30.59 ? 174  LYS D CE  1 
ATOM   15675 N  NZ  . LYS D 1 182 ? 13.685  -25.751 87.898  1.00 29.13 ? 174  LYS D NZ  1 
ATOM   15676 N  N   . LEU D 1 183 ? 13.437  -18.008 84.467  1.00 19.38 ? 175  LEU D N   1 
ATOM   15677 C  CA  . LEU D 1 183 ? 13.076  -16.610 84.665  1.00 18.31 ? 175  LEU D CA  1 
ATOM   15678 C  C   . LEU D 1 183 ? 12.073  -16.203 83.585  1.00 23.22 ? 175  LEU D C   1 
ATOM   15679 O  O   . LEU D 1 183 ? 12.363  -16.317 82.390  1.00 18.03 ? 175  LEU D O   1 
ATOM   15680 C  CB  . LEU D 1 183 ? 14.320  -15.716 84.618  1.00 14.90 ? 175  LEU D CB  1 
ATOM   15681 C  CG  . LEU D 1 183 ? 14.060  -14.198 84.616  1.00 15.93 ? 175  LEU D CG  1 
ATOM   15682 C  CD1 . LEU D 1 183 ? 13.410  -13.734 85.917  1.00 18.83 ? 175  LEU D CD1 1 
ATOM   15683 C  CD2 . LEU D 1 183 ? 15.341  -13.382 84.328  1.00 12.69 ? 175  LEU D CD2 1 
ATOM   15684 N  N   . ILE D 1 184 ? 10.898  -15.734 83.997  1.00 13.88 ? 176  ILE D N   1 
ATOM   15685 C  CA  . ILE D 1 184 ? 9.825   -15.412 83.059  1.00 16.67 ? 176  ILE D CA  1 
ATOM   15686 C  C   . ILE D 1 184 ? 9.267   -14.038 83.411  1.00 21.90 ? 176  ILE D C   1 
ATOM   15687 O  O   . ILE D 1 184 ? 8.760   -13.835 84.520  1.00 17.73 ? 176  ILE D O   1 
ATOM   15688 C  CB  . ILE D 1 184 ? 8.725   -16.486 83.067  1.00 17.70 ? 176  ILE D CB  1 
ATOM   15689 C  CG1 . ILE D 1 184 ? 9.285   -17.797 82.509  1.00 15.34 ? 176  ILE D CG1 1 
ATOM   15690 C  CG2 . ILE D 1 184 ? 7.518   -16.047 82.236  1.00 18.84 ? 176  ILE D CG2 1 
ATOM   15691 C  CD1 . ILE D 1 184 ? 8.309   -18.971 82.572  1.00 16.57 ? 176  ILE D CD1 1 
ATOM   15692 N  N   . VAL D 1 185 ? 9.375   -13.096 82.475  1.00 14.88 ? 177  VAL D N   1 
ATOM   15693 C  CA  . VAL D 1 185 ? 8.998   -11.707 82.692  1.00 16.97 ? 177  VAL D CA  1 
ATOM   15694 C  C   . VAL D 1 185 ? 7.731   -11.407 81.903  1.00 16.44 ? 177  VAL D C   1 
ATOM   15695 O  O   . VAL D 1 185 ? 7.640   -11.730 80.711  1.00 15.30 ? 177  VAL D O   1 
ATOM   15696 C  CB  . VAL D 1 185 ? 10.132  -10.760 82.268  1.00 15.95 ? 177  VAL D CB  1 
ATOM   15697 C  CG1 . VAL D 1 185 ? 9.689   -9.304  82.391  1.00 14.82 ? 177  VAL D CG1 1 
ATOM   15698 C  CG2 . VAL D 1 185 ? 11.380  -11.050 83.092  1.00 15.99 ? 177  VAL D CG2 1 
ATOM   15699 N  N   . LEU D 1 186 ? 6.763   -10.780 82.561  1.00 15.92 ? 178  LEU D N   1 
ATOM   15700 C  CA  . LEU D 1 186 ? 5.608   -10.198 81.883  1.00 14.33 ? 178  LEU D CA  1 
ATOM   15701 C  C   . LEU D 1 186 ? 5.783   -8.691  81.900  1.00 12.84 ? 178  LEU D C   1 
ATOM   15702 O  O   . LEU D 1 186 ? 5.847   -8.072  82.969  1.00 13.66 ? 178  LEU D O   1 
ATOM   15703 C  CB  . LEU D 1 186 ? 4.281   -10.610 82.521  1.00 15.69 ? 178  LEU D CB  1 
ATOM   15704 C  CG  . LEU D 1 186 ? 3.804   -12.028 82.166  1.00 17.52 ? 178  LEU D CG  1 
ATOM   15705 C  CD1 . LEU D 1 186 ? 4.586   -13.071 82.954  1.00 17.38 ? 178  LEU D CD1 1 
ATOM   15706 C  CD2 . LEU D 1 186 ? 2.290   -12.191 82.386  1.00 16.08 ? 178  LEU D CD2 1 
ATOM   15707 N  N   . TYR D 1 187 ? 5.891   -8.117  80.717  1.00 16.63 ? 179  TYR D N   1 
ATOM   15708 C  CA  . TYR D 1 187 ? 6.146   -6.697  80.540  1.00 16.44 ? 179  TYR D CA  1 
ATOM   15709 C  C   . TYR D 1 187 ? 4.809   -5.985  80.331  1.00 18.61 ? 179  TYR D C   1 
ATOM   15710 O  O   . TYR D 1 187 ? 4.016   -6.374  79.467  1.00 19.18 ? 179  TYR D O   1 
ATOM   15711 C  CB  . TYR D 1 187 ? 7.117   -6.515  79.370  1.00 19.39 ? 179  TYR D CB  1 
ATOM   15712 C  CG  . TYR D 1 187 ? 7.173   -5.162  78.721  1.00 14.84 ? 179  TYR D CG  1 
ATOM   15713 C  CD1 . TYR D 1 187 ? 7.141   -3.996  79.475  1.00 17.17 ? 179  TYR D CD1 1 
ATOM   15714 C  CD2 . TYR D 1 187 ? 7.313   -5.056  77.335  1.00 15.99 ? 179  TYR D CD2 1 
ATOM   15715 C  CE1 . TYR D 1 187 ? 7.198   -2.756  78.875  1.00 17.28 ? 179  TYR D CE1 1 
ATOM   15716 C  CE2 . TYR D 1 187 ? 7.380   -3.829  76.725  1.00 17.58 ? 179  TYR D CE2 1 
ATOM   15717 C  CZ  . TYR D 1 187 ? 7.332   -2.679  77.491  1.00 20.95 ? 179  TYR D CZ  1 
ATOM   15718 O  OH  . TYR D 1 187 ? 7.387   -1.448  76.867  1.00 17.30 ? 179  TYR D OH  1 
ATOM   15719 N  N   . ASP D 1 188 ? 4.545   -4.981  81.162  1.00 13.37 ? 180  ASP D N   1 
ATOM   15720 C  CA  . ASP D 1 188 ? 3.338   -4.161  81.075  1.00 13.11 ? 180  ASP D CA  1 
ATOM   15721 C  C   . ASP D 1 188 ? 3.587   -3.101  80.011  1.00 16.49 ? 180  ASP D C   1 
ATOM   15722 O  O   . ASP D 1 188 ? 4.105   -2.017  80.283  1.00 20.70 ? 180  ASP D O   1 
ATOM   15723 C  CB  . ASP D 1 188 ? 3.018   -3.546  82.434  1.00 15.51 ? 180  ASP D CB  1 
ATOM   15724 C  CG  . ASP D 1 188 ? 1.743   -2.700  82.415  1.00 20.30 ? 180  ASP D CG  1 
ATOM   15725 O  OD1 . ASP D 1 188 ? 0.909   -2.907  81.514  1.00 24.74 ? 180  ASP D OD1 1 
ATOM   15726 O  OD2 . ASP D 1 188 ? 1.586   -1.828  83.302  1.00 20.21 ? 180  ASP D OD2 1 
ATOM   15727 N  N   . ASP D 1 189 ? 3.228   -3.433  78.771  1.00 16.43 ? 181  ASP D N   1 
ATOM   15728 C  CA  . ASP D 1 189 ? 3.511   -2.593  77.610  1.00 18.31 ? 181  ASP D CA  1 
ATOM   15729 C  C   . ASP D 1 189 ? 2.286   -1.720  77.389  1.00 17.63 ? 181  ASP D C   1 
ATOM   15730 O  O   . ASP D 1 189 ? 1.397   -2.051  76.609  1.00 19.27 ? 181  ASP D O   1 
ATOM   15731 C  CB  . ASP D 1 189 ? 3.829   -3.458  76.394  1.00 18.57 ? 181  ASP D CB  1 
ATOM   15732 C  CG  . ASP D 1 189 ? 4.255   -2.644  75.170  1.00 25.49 ? 181  ASP D CG  1 
ATOM   15733 O  OD1 . ASP D 1 189 ? 4.170   -1.401  75.190  1.00 25.29 ? 181  ASP D OD1 1 
ATOM   15734 O  OD2 . ASP D 1 189 ? 4.673   -3.265  74.172  1.00 26.88 ? 181  ASP D OD2 1 
ATOM   15735 N  N   . ASN D 1 190 ? 2.224   -0.599  78.095  1.00 18.41 ? 182  ASN D N   1 
ATOM   15736 C  CA  . ASN D 1 190 ? 1.016   0.217   78.031  1.00 17.86 ? 182  ASN D CA  1 
ATOM   15737 C  C   . ASN D 1 190 ? 1.247   1.516   77.264  1.00 28.91 ? 182  ASN D C   1 
ATOM   15738 O  O   . ASN D 1 190 ? 0.604   2.525   77.547  1.00 37.37 ? 182  ASN D O   1 
ATOM   15739 C  CB  . ASN D 1 190 ? 0.477   0.503   79.440  1.00 21.88 ? 182  ASN D CB  1 
ATOM   15740 C  CG  . ASN D 1 190 ? 1.473   1.233   80.331  1.00 33.18 ? 182  ASN D CG  1 
ATOM   15741 O  OD1 . ASN D 1 190 ? 2.463   1.792   79.864  1.00 30.70 ? 182  ASN D OD1 1 
ATOM   15742 N  ND2 . ASN D 1 190 ? 1.196   1.238   81.632  1.00 32.88 ? 182  ASN D ND2 1 
ATOM   15743 N  N   . ASP D 1 199 ? 6.675   8.199   73.294  1.00 54.11 ? 191  ASP D N   1 
ATOM   15744 C  CA  . ASP D 1 199 ? 7.272   8.200   71.961  1.00 51.23 ? 191  ASP D CA  1 
ATOM   15745 C  C   . ASP D 1 199 ? 8.234   9.372   71.801  1.00 41.08 ? 191  ASP D C   1 
ATOM   15746 O  O   . ASP D 1 199 ? 9.056   9.395   70.881  1.00 40.47 ? 191  ASP D O   1 
ATOM   15747 C  CB  . ASP D 1 199 ? 6.189   8.253   70.879  1.00 58.90 ? 191  ASP D CB  1 
ATOM   15748 N  N   . GLY D 1 200 ? 8.121   10.351  72.703  1.00 33.27 ? 192  GLY D N   1 
ATOM   15749 C  CA  . GLY D 1 200 ? 9.056   11.460  72.714  1.00 28.22 ? 192  GLY D CA  1 
ATOM   15750 C  C   . GLY D 1 200 ? 10.368  11.156  73.402  1.00 26.22 ? 192  GLY D C   1 
ATOM   15751 O  O   . GLY D 1 200 ? 11.334  11.904  73.222  1.00 29.85 ? 192  GLY D O   1 
ATOM   15752 N  N   . TRP D 1 201 ? 10.428  10.075  74.188  1.00 22.80 ? 193  TRP D N   1 
ATOM   15753 C  CA  . TRP D 1 201 ? 11.660  9.706   74.877  1.00 24.97 ? 193  TRP D CA  1 
ATOM   15754 C  C   . TRP D 1 201 ? 11.923  8.207   74.926  1.00 19.92 ? 193  TRP D C   1 
ATOM   15755 O  O   . TRP D 1 201 ? 12.975  7.812   75.436  1.00 26.28 ? 193  TRP D O   1 
ATOM   15756 C  CB  . TRP D 1 201 ? 11.660  10.256  76.318  1.00 21.28 ? 193  TRP D CB  1 
ATOM   15757 C  CG  . TRP D 1 201 ? 10.459  9.825   77.093  1.00 25.84 ? 193  TRP D CG  1 
ATOM   15758 C  CD1 . TRP D 1 201 ? 10.320  8.689   77.844  1.00 22.32 ? 193  TRP D CD1 1 
ATOM   15759 C  CD2 . TRP D 1 201 ? 9.210   10.517  77.172  1.00 27.09 ? 193  TRP D CD2 1 
ATOM   15760 N  NE1 . TRP D 1 201 ? 9.056   8.640   78.393  1.00 29.70 ? 193  TRP D NE1 1 
ATOM   15761 C  CE2 . TRP D 1 201 ? 8.357   9.751   77.992  1.00 29.82 ? 193  TRP D CE2 1 
ATOM   15762 C  CE3 . TRP D 1 201 ? 8.734   11.719  76.638  1.00 30.59 ? 193  TRP D CE3 1 
ATOM   15763 C  CZ2 . TRP D 1 201 ? 7.051   10.152  78.290  1.00 32.57 ? 193  TRP D CZ2 1 
ATOM   15764 C  CZ3 . TRP D 1 201 ? 7.439   12.112  76.930  1.00 31.09 ? 193  TRP D CZ3 1 
ATOM   15765 C  CH2 . TRP D 1 201 ? 6.614   11.331  77.748  1.00 31.73 ? 193  TRP D CH2 1 
ATOM   15766 N  N   . PHE D 1 202 ? 11.018  7.362   74.422  1.00 17.37 ? 194  PHE D N   1 
ATOM   15767 C  CA  . PHE D 1 202 ? 11.185  5.911   74.527  1.00 18.87 ? 194  PHE D CA  1 
ATOM   15768 C  C   . PHE D 1 202 ? 10.589  5.275   73.283  1.00 19.95 ? 194  PHE D C   1 
ATOM   15769 O  O   . PHE D 1 202 ? 9.371   5.318   73.087  1.00 16.26 ? 194  PHE D O   1 
ATOM   15770 C  CB  . PHE D 1 202 ? 10.523  5.372   75.795  1.00 18.65 ? 194  PHE D CB  1 
ATOM   15771 C  CG  . PHE D 1 202 ? 10.725  3.902   76.023  1.00 14.61 ? 194  PHE D CG  1 
ATOM   15772 C  CD1 . PHE D 1 202 ? 12.000  3.356   76.086  1.00 16.28 ? 194  PHE D CD1 1 
ATOM   15773 C  CD2 . PHE D 1 202 ? 9.636   3.064   76.213  1.00 23.64 ? 194  PHE D CD2 1 
ATOM   15774 C  CE1 . PHE D 1 202 ? 12.182  1.996   76.322  1.00 23.15 ? 194  PHE D CE1 1 
ATOM   15775 C  CE2 . PHE D 1 202 ? 9.808   1.710   76.443  1.00 23.93 ? 194  PHE D CE2 1 
ATOM   15776 C  CZ  . PHE D 1 202 ? 11.079  1.171   76.496  1.00 25.90 ? 194  PHE D CZ  1 
ATOM   15777 N  N   . THR D 1 203 ? 11.453  4.688   72.448  1.00 17.95 ? 195  THR D N   1 
ATOM   15778 C  CA  . THR D 1 203 ? 11.037  4.073   71.195  1.00 16.12 ? 195  THR D CA  1 
ATOM   15779 C  C   . THR D 1 203 ? 11.748  2.743   70.959  1.00 17.01 ? 195  THR D C   1 
ATOM   15780 O  O   . THR D 1 203 ? 11.868  2.313   69.809  1.00 16.47 ? 195  THR D O   1 
ATOM   15781 C  CB  . THR D 1 203 ? 11.311  5.019   70.017  1.00 20.90 ? 195  THR D CB  1 
ATOM   15782 O  OG1 . THR D 1 203 ? 12.667  5.471   70.086  1.00 20.71 ? 195  THR D OG1 1 
ATOM   15783 C  CG2 . THR D 1 203 ? 10.376  6.234   70.063  1.00 21.17 ? 195  THR D CG2 1 
ATOM   15784 N  N   . GLU D 1 204 ? 12.242  2.095   72.012  1.00 15.17 ? 196  GLU D N   1 
ATOM   15785 C  CA  . GLU D 1 204 ? 12.948  0.834   71.842  1.00 16.90 ? 196  GLU D CA  1 
ATOM   15786 C  C   . GLU D 1 204 ? 12.011  -0.244  71.304  1.00 19.49 ? 196  GLU D C   1 
ATOM   15787 O  O   . GLU D 1 204 ? 10.841  -0.322  71.692  1.00 18.25 ? 196  GLU D O   1 
ATOM   15788 C  CB  . GLU D 1 204 ? 13.551  0.378   73.172  1.00 18.32 ? 196  GLU D CB  1 
ATOM   15789 C  CG  . GLU D 1 204 ? 14.603  1.330   73.718  1.00 20.48 ? 196  GLU D CG  1 
ATOM   15790 C  CD  . GLU D 1 204 ? 15.216  0.854   75.025  1.00 19.66 ? 196  GLU D CD  1 
ATOM   15791 O  OE1 . GLU D 1 204 ? 15.064  -0.340  75.363  1.00 15.25 ? 196  GLU D OE1 1 
ATOM   15792 O  OE2 . GLU D 1 204 ? 15.855  1.685   75.712  1.00 18.16 ? 196  GLU D OE2 1 
ATOM   15793 N  N   . ASN D 1 205 ? 12.532  -1.066  70.392  1.00 15.76 ? 197  ASN D N   1 
ATOM   15794 C  CA  . ASN D 1 205 ? 11.852  -2.286  69.941  1.00 16.08 ? 197  ASN D CA  1 
ATOM   15795 C  C   . ASN D 1 205 ? 12.236  -3.353  70.959  1.00 15.50 ? 197  ASN D C   1 
ATOM   15796 O  O   . ASN D 1 205 ? 13.295  -3.982  70.872  1.00 17.56 ? 197  ASN D O   1 
ATOM   15797 C  CB  . ASN D 1 205 ? 12.272  -2.640  68.515  1.00 16.86 ? 197  ASN D CB  1 
ATOM   15798 C  CG  . ASN D 1 205 ? 11.615  -3.922  67.981  1.00 19.80 ? 197  ASN D CG  1 
ATOM   15799 O  OD1 . ASN D 1 205 ? 11.149  -4.776  68.732  1.00 17.32 ? 197  ASN D OD1 1 
ATOM   15800 N  ND2 . ASN D 1 205 ? 11.615  -4.063  66.661  1.00 19.56 ? 197  ASN D ND2 1 
ATOM   15801 N  N   . ILE D 1 206 ? 11.384  -3.519  71.975  1.00 15.08 ? 198  ILE D N   1 
ATOM   15802 C  CA  . ILE D 1 206 ? 11.753  -4.375  73.108  1.00 14.52 ? 198  ILE D CA  1 
ATOM   15803 C  C   . ILE D 1 206 ? 11.914  -5.831  72.705  1.00 14.84 ? 198  ILE D C   1 
ATOM   15804 O  O   . ILE D 1 206 ? 12.885  -6.468  73.148  1.00 14.61 ? 198  ILE D O   1 
ATOM   15805 C  CB  . ILE D 1 206 ? 10.766  -4.164  74.268  1.00 14.10 ? 198  ILE D CB  1 
ATOM   15806 C  CG1 . ILE D 1 206 ? 10.952  -2.765  74.883  1.00 13.73 ? 198  ILE D CG1 1 
ATOM   15807 C  CG2 . ILE D 1 206 ? 10.919  -5.271  75.326  1.00 15.98 ? 198  ILE D CG2 1 
ATOM   15808 C  CD1 . ILE D 1 206 ? 12.351  -2.475  75.436  1.00 13.96 ? 198  ILE D CD1 1 
ATOM   15809 N  N   . PRO D 1 207 ? 11.036  -6.432  71.889  1.00 17.59 ? 199  PRO D N   1 
ATOM   15810 C  CA  . PRO D 1 207 ? 11.325  -7.793  71.394  1.00 17.37 ? 199  PRO D CA  1 
ATOM   15811 C  C   . PRO D 1 207 ? 12.692  -7.920  70.743  1.00 21.43 ? 199  PRO D C   1 
ATOM   15812 O  O   . PRO D 1 207 ? 13.442  -8.861  71.038  1.00 19.00 ? 199  PRO D O   1 
ATOM   15813 C  CB  . PRO D 1 207 ? 10.186  -8.035  70.392  1.00 16.62 ? 199  PRO D CB  1 
ATOM   15814 C  CG  . PRO D 1 207 ? 9.061   -7.263  70.935  1.00 16.85 ? 199  PRO D CG  1 
ATOM   15815 C  CD  . PRO D 1 207 ? 9.673   -6.002  71.521  1.00 15.79 ? 199  PRO D CD  1 
ATOM   15816 N  N   . GLN D 1 208 ? 13.042  -6.979  69.866  1.00 18.82 ? 200  GLN D N   1 
ATOM   15817 C  CA  . GLN D 1 208 ? 14.335  -7.049  69.198  1.00 20.02 ? 200  GLN D CA  1 
ATOM   15818 C  C   . GLN D 1 208 ? 15.474  -6.905  70.195  1.00 18.21 ? 200  GLN D C   1 
ATOM   15819 O  O   . GLN D 1 208 ? 16.482  -7.620  70.112  1.00 16.14 ? 200  GLN D O   1 
ATOM   15820 C  CB  . GLN D 1 208 ? 14.430  -5.970  68.126  1.00 19.21 ? 200  GLN D CB  1 
ATOM   15821 C  CG  . GLN D 1 208 ? 15.636  -6.148  67.220  1.00 21.15 ? 200  GLN D CG  1 
ATOM   15822 C  CD  . GLN D 1 208 ? 15.633  -5.178  66.065  1.00 24.40 ? 200  GLN D CD  1 
ATOM   15823 O  OE1 . GLN D 1 208 ? 15.303  -4.004  66.226  1.00 25.46 ? 200  GLN D OE1 1 
ATOM   15824 N  NE2 . GLN D 1 208 ? 16.004  -5.663  64.886  1.00 26.42 ? 200  GLN D NE2 1 
ATOM   15825 N  N   . ARG D 1 209 ? 15.328  -5.990  71.150  1.00 15.36 ? 201  ARG D N   1 
ATOM   15826 C  CA  . ARG D 1 209 ? 16.361  -5.814  72.158  1.00 15.35 ? 201  ARG D CA  1 
ATOM   15827 C  C   . ARG D 1 209 ? 16.562  -7.087  72.964  1.00 14.96 ? 201  ARG D C   1 
ATOM   15828 O  O   . ARG D 1 209 ? 17.702  -7.496  73.214  1.00 14.61 ? 201  ARG D O   1 
ATOM   15829 C  CB  . ARG D 1 209 ? 16.003  -4.646  73.077  1.00 14.22 ? 201  ARG D CB  1 
ATOM   15830 C  CG  . ARG D 1 209 ? 16.881  -4.535  74.319  1.00 13.63 ? 201  ARG D CG  1 
ATOM   15831 C  CD  . ARG D 1 209 ? 16.370  -3.425  75.242  1.00 17.22 ? 201  ARG D CD  1 
ATOM   15832 N  NE  . ARG D 1 209 ? 16.997  -3.483  76.560  1.00 17.16 ? 201  ARG D NE  1 
ATOM   15833 C  CZ  . ARG D 1 209 ? 16.511  -2.883  77.635  1.00 15.97 ? 201  ARG D CZ  1 
ATOM   15834 N  NH1 . ARG D 1 209 ? 15.393  -2.157  77.540  1.00 14.39 ? 201  ARG D NH1 1 
ATOM   15835 N  NH2 . ARG D 1 209 ? 17.144  -3.001  78.797  1.00 19.63 ? 201  ARG D NH2 1 
ATOM   15836 N  N   . PHE D 1 210 ? 15.476  -7.746  73.362  1.00 14.56 ? 202  PHE D N   1 
ATOM   15837 C  CA  . PHE D 1 210 ? 15.655  -8.929  74.200  1.00 16.56 ? 202  PHE D CA  1 
ATOM   15838 C  C   . PHE D 1 210 ? 16.090  -10.152 73.402  1.00 15.62 ? 202  PHE D C   1 
ATOM   15839 O  O   . PHE D 1 210 ? 16.780  -11.023 73.947  1.00 19.11 ? 202  PHE D O   1 
ATOM   15840 C  CB  . PHE D 1 210 ? 14.389  -9.181  75.026  1.00 15.31 ? 202  PHE D CB  1 
ATOM   15841 C  CG  . PHE D 1 210 ? 14.375  -8.395  76.313  1.00 15.18 ? 202  PHE D CG  1 
ATOM   15842 C  CD1 . PHE D 1 210 ? 14.190  -7.019  76.295  1.00 18.43 ? 202  PHE D CD1 1 
ATOM   15843 C  CD2 . PHE D 1 210 ? 14.608  -9.018  77.535  1.00 14.82 ? 202  PHE D CD2 1 
ATOM   15844 C  CE1 . PHE D 1 210 ? 14.222  -6.268  77.478  1.00 15.58 ? 202  PHE D CE1 1 
ATOM   15845 C  CE2 . PHE D 1 210 ? 14.637  -8.279  78.730  1.00 16.70 ? 202  PHE D CE2 1 
ATOM   15846 C  CZ  . PHE D 1 210 ? 14.442  -6.902  78.699  1.00 16.09 ? 202  PHE D CZ  1 
ATOM   15847 N  N   . GLU D 1 211 ? 15.743  -10.235 72.116  1.00 15.73 ? 203  GLU D N   1 
ATOM   15848 C  CA  . GLU D 1 211 ? 16.367  -11.257 71.286  1.00 16.42 ? 203  GLU D CA  1 
ATOM   15849 C  C   . GLU D 1 211 ? 17.878  -11.062 71.244  1.00 16.40 ? 203  GLU D C   1 
ATOM   15850 O  O   . GLU D 1 211 ? 18.637  -12.036 71.298  1.00 18.36 ? 203  GLU D O   1 
ATOM   15851 C  CB  . GLU D 1 211 ? 15.784  -11.225 69.876  1.00 22.60 ? 203  GLU D CB  1 
ATOM   15852 C  CG  . GLU D 1 211 ? 14.332  -11.622 69.805  1.00 25.78 ? 203  GLU D CG  1 
ATOM   15853 C  CD  . GLU D 1 211 ? 13.896  -11.914 68.380  1.00 36.23 ? 203  GLU D CD  1 
ATOM   15854 O  OE1 . GLU D 1 211 ? 14.759  -12.274 67.550  1.00 37.92 ? 203  GLU D OE1 1 
ATOM   15855 O  OE2 . GLU D 1 211 ? 12.691  -11.766 68.094  1.00 42.50 ? 203  GLU D OE2 1 
ATOM   15856 N  N   . SER D 1 212 ? 18.332  -9.804  71.177  1.00 16.09 ? 204  SER D N   1 
ATOM   15857 C  CA  . SER D 1 212 ? 19.765  -9.521  71.138  1.00 16.10 ? 204  SER D CA  1 
ATOM   15858 C  C   . SER D 1 212 ? 20.472  -10.010 72.389  1.00 18.86 ? 204  SER D C   1 
ATOM   15859 O  O   . SER D 1 212 ? 21.689  -10.245 72.352  1.00 18.98 ? 204  SER D O   1 
ATOM   15860 C  CB  . SER D 1 212 ? 20.017  -8.017  70.952  1.00 17.89 ? 204  SER D CB  1 
ATOM   15861 O  OG  . SER D 1 212 ? 19.989  -7.299  72.187  1.00 16.34 ? 204  SER D OG  1 
ATOM   15862 N  N   . TYR D 1 213 ? 19.740  -10.148 73.493  1.00 18.08 ? 205  TYR D N   1 
ATOM   15863 C  CA  . TYR D 1 213 ? 20.267  -10.702 74.731  1.00 20.09 ? 205  TYR D CA  1 
ATOM   15864 C  C   . TYR D 1 213 ? 20.253  -12.222 74.758  1.00 17.39 ? 205  TYR D C   1 
ATOM   15865 O  O   . TYR D 1 213 ? 20.791  -12.810 75.702  1.00 19.28 ? 205  TYR D O   1 
ATOM   15866 C  CB  . TYR D 1 213 ? 19.441  -10.218 75.921  1.00 15.50 ? 205  TYR D CB  1 
ATOM   15867 C  CG  . TYR D 1 213 ? 19.492  -8.738  76.226  1.00 16.70 ? 205  TYR D CG  1 
ATOM   15868 C  CD1 . TYR D 1 213 ? 20.593  -7.949  75.877  1.00 14.41 ? 205  TYR D CD1 1 
ATOM   15869 C  CD2 . TYR D 1 213 ? 18.435  -8.139  76.877  1.00 13.21 ? 205  TYR D CD2 1 
ATOM   15870 C  CE1 . TYR D 1 213 ? 20.623  -6.599  76.187  1.00 16.39 ? 205  TYR D CE1 1 
ATOM   15871 C  CE2 . TYR D 1 213 ? 18.452  -6.798  77.197  1.00 13.51 ? 205  TYR D CE2 1 
ATOM   15872 C  CZ  . TYR D 1 213 ? 19.537  -6.033  76.852  1.00 13.58 ? 205  TYR D CZ  1 
ATOM   15873 O  OH  . TYR D 1 213 ? 19.512  -4.698  77.163  1.00 12.58 ? 205  TYR D OH  1 
ATOM   15874 N  N   . GLY D 1 214 ? 19.623  -12.867 73.785  1.00 18.05 ? 206  GLY D N   1 
ATOM   15875 C  CA  . GLY D 1 214 ? 19.434  -14.303 73.837  1.00 22.38 ? 206  GLY D CA  1 
ATOM   15876 C  C   . GLY D 1 214 ? 18.207  -14.743 74.599  1.00 18.99 ? 206  GLY D C   1 
ATOM   15877 O  O   . GLY D 1 214 ? 18.136  -15.902 75.020  1.00 19.41 ? 206  GLY D O   1 
ATOM   15878 N  N   . TRP D 1 215 ? 17.233  -13.861 74.782  1.00 17.18 ? 207  TRP D N   1 
ATOM   15879 C  CA  . TRP D 1 215 ? 15.996  -14.218 75.456  1.00 16.74 ? 207  TRP D CA  1 
ATOM   15880 C  C   . TRP D 1 215 ? 14.998  -14.814 74.480  1.00 22.78 ? 207  TRP D C   1 
ATOM   15881 O  O   . TRP D 1 215 ? 15.023  -14.521 73.282  1.00 18.50 ? 207  TRP D O   1 
ATOM   15882 C  CB  . TRP D 1 215 ? 15.367  -12.998 76.110  1.00 16.37 ? 207  TRP D CB  1 
ATOM   15883 C  CG  . TRP D 1 215 ? 16.020  -12.565 77.387  1.00 19.00 ? 207  TRP D CG  1 
ATOM   15884 C  CD1 . TRP D 1 215 ? 17.362  -12.366 77.626  1.00 14.12 ? 207  TRP D CD1 1 
ATOM   15885 C  CD2 . TRP D 1 215 ? 15.341  -12.239 78.596  1.00 14.34 ? 207  TRP D CD2 1 
ATOM   15886 N  NE1 . TRP D 1 215 ? 17.545  -11.947 78.931  1.00 13.55 ? 207  TRP D NE1 1 
ATOM   15887 C  CE2 . TRP D 1 215 ? 16.317  -11.848 79.537  1.00 13.30 ? 207  TRP D CE2 1 
ATOM   15888 C  CE3 . TRP D 1 215 ? 13.990  -12.242 78.977  1.00 14.27 ? 207  TRP D CE3 1 
ATOM   15889 C  CZ2 . TRP D 1 215 ? 15.991  -11.485 80.835  1.00 12.81 ? 207  TRP D CZ2 1 
ATOM   15890 C  CZ3 . TRP D 1 215 ? 13.670  -11.879 80.261  1.00 14.60 ? 207  TRP D CZ3 1 
ATOM   15891 C  CH2 . TRP D 1 215 ? 14.663  -11.500 81.178  1.00 12.72 ? 207  TRP D CH2 1 
ATOM   15892 N  N   . HIS D 1 216 ? 14.117  -15.653 75.011  1.00 16.40 ? 208  HIS D N   1 
ATOM   15893 C  CA  . HIS D 1 216 ? 12.907  -16.037 74.302  1.00 19.90 ? 208  HIS D CA  1 
ATOM   15894 C  C   . HIS D 1 216 ? 11.902  -14.903 74.450  1.00 16.45 ? 208  HIS D C   1 
ATOM   15895 O  O   . HIS D 1 216 ? 11.774  -14.315 75.527  1.00 19.51 ? 208  HIS D O   1 
ATOM   15896 C  CB  . HIS D 1 216 ? 12.358  -17.345 74.876  1.00 17.34 ? 208  HIS D CB  1 
ATOM   15897 C  CG  . HIS D 1 216 ? 10.954  -17.653 74.473  1.00 19.27 ? 208  HIS D CG  1 
ATOM   15898 N  ND1 . HIS D 1 216 ? 9.922   -17.736 75.382  1.00 21.61 ? 208  HIS D ND1 1 
ATOM   15899 C  CD2 . HIS D 1 216 ? 10.414  -17.930 73.263  1.00 21.26 ? 208  HIS D CD2 1 
ATOM   15900 C  CE1 . HIS D 1 216 ? 8.805   -18.042 74.747  1.00 22.95 ? 208  HIS D CE1 1 
ATOM   15901 N  NE2 . HIS D 1 216 ? 9.075   -18.157 73.460  1.00 22.11 ? 208  HIS D NE2 1 
ATOM   15902 N  N   . VAL D 1 217 ? 11.236  -14.547 73.358  1.00 16.86 ? 209  VAL D N   1 
ATOM   15903 C  CA  . VAL D 1 217 ? 10.342  -13.392 73.354  1.00 22.99 ? 209  VAL D CA  1 
ATOM   15904 C  C   . VAL D 1 217 ? 8.971   -13.807 72.845  1.00 19.92 ? 209  VAL D C   1 
ATOM   15905 O  O   . VAL D 1 217 ? 8.856   -14.389 71.759  1.00 18.49 ? 209  VAL D O   1 
ATOM   15906 C  CB  . VAL D 1 217 ? 10.890  -12.239 72.492  1.00 27.05 ? 209  VAL D CB  1 
ATOM   15907 C  CG1 . VAL D 1 217 ? 9.867   -11.103 72.414  1.00 19.02 ? 209  VAL D CG1 1 
ATOM   15908 C  CG2 . VAL D 1 217 ? 12.222  -11.741 73.045  1.00 22.55 ? 209  VAL D CG2 1 
ATOM   15909 N  N   . VAL D 1 218 ? 7.933   -13.484 73.612  1.00 17.49 ? 210  VAL D N   1 
ATOM   15910 C  CA  . VAL D 1 218 ? 6.561   -13.615 73.116  1.00 17.91 ? 210  VAL D CA  1 
ATOM   15911 C  C   . VAL D 1 218 ? 6.024   -12.211 72.873  1.00 17.70 ? 210  VAL D C   1 
ATOM   15912 O  O   . VAL D 1 218 ? 5.591   -11.544 73.821  1.00 17.56 ? 210  VAL D O   1 
ATOM   15913 C  CB  . VAL D 1 218 ? 5.656   -14.387 74.089  1.00 18.91 ? 210  VAL D CB  1 
ATOM   15914 C  CG1 . VAL D 1 218 ? 4.305   -14.713 73.405  1.00 20.91 ? 210  VAL D CG1 1 
ATOM   15915 C  CG2 . VAL D 1 218 ? 6.347   -15.653 74.582  1.00 17.52 ? 210  VAL D CG2 1 
ATOM   15916 N  N   . PRO D 1 219 ? 6.021   -11.727 71.637  1.00 20.40 ? 211  PRO D N   1 
ATOM   15917 C  CA  . PRO D 1 219 ? 5.635   -10.338 71.389  1.00 18.74 ? 211  PRO D CA  1 
ATOM   15918 C  C   . PRO D 1 219 ? 4.126   -10.179 71.275  1.00 20.78 ? 211  PRO D C   1 
ATOM   15919 O  O   . PRO D 1 219 ? 3.385   -11.142 71.080  1.00 19.15 ? 211  PRO D O   1 
ATOM   15920 C  CB  . PRO D 1 219 ? 6.322   -10.035 70.056  1.00 20.10 ? 211  PRO D CB  1 
ATOM   15921 C  CG  . PRO D 1 219 ? 6.246   -11.347 69.331  1.00 26.83 ? 211  PRO D CG  1 
ATOM   15922 C  CD  . PRO D 1 219 ? 6.380   -12.425 70.387  1.00 21.17 ? 211  PRO D CD  1 
ATOM   15923 N  N   . ASN D 1 220 ? 3.683   -8.930  71.422  1.00 20.98 ? 212  ASN D N   1 
ATOM   15924 C  CA  . ASN D 1 220 ? 2.331   -8.500  71.026  1.00 18.26 ? 212  ASN D CA  1 
ATOM   15925 C  C   . ASN D 1 220 ? 1.228   -9.403  71.588  1.00 19.30 ? 212  ASN D C   1 
ATOM   15926 O  O   . ASN D 1 220 ? 0.328   -9.853  70.874  1.00 23.95 ? 212  ASN D O   1 
ATOM   15927 C  CB  . ASN D 1 220 ? 2.225   -8.401  69.504  1.00 26.61 ? 212  ASN D CB  1 
ATOM   15928 C  CG  . ASN D 1 220 ? 0.993   -7.641  69.064  1.00 30.21 ? 212  ASN D CG  1 
ATOM   15929 O  OD1 . ASN D 1 220 ? 0.625   -6.641  69.673  1.00 30.76 ? 212  ASN D OD1 1 
ATOM   15930 N  ND2 . ASN D 1 220 ? 0.338   -8.123  68.020  1.00 33.23 ? 212  ASN D ND2 1 
ATOM   15931 N  N   . VAL D 1 221 ? 1.284   -9.655  72.889  1.00 17.84 ? 213  VAL D N   1 
ATOM   15932 C  CA  . VAL D 1 221 ? 0.240   -10.410 73.570  1.00 21.15 ? 213  VAL D CA  1 
ATOM   15933 C  C   . VAL D 1 221 ? -0.840  -9.444  74.040  1.00 18.61 ? 213  VAL D C   1 
ATOM   15934 O  O   . VAL D 1 221 ? -0.540  -8.407  74.640  1.00 21.66 ? 213  VAL D O   1 
ATOM   15935 C  CB  . VAL D 1 221 ? 0.812   -11.203 74.756  1.00 18.60 ? 213  VAL D CB  1 
ATOM   15936 C  CG1 . VAL D 1 221 ? -0.314  -11.952 75.487  1.00 18.08 ? 213  VAL D CG1 1 
ATOM   15937 C  CG2 . VAL D 1 221 ? 1.857   -12.164 74.268  1.00 17.60 ? 213  VAL D CG2 1 
ATOM   15938 N  N   . ASN D 1 222 ? -2.098  -9.792  73.782  1.00 21.53 ? 214  ASN D N   1 
ATOM   15939 C  CA  . ASN D 1 222 ? -3.229  -9.019  74.292  1.00 18.79 ? 214  ASN D CA  1 
ATOM   15940 C  C   . ASN D 1 222 ? -3.248  -9.140  75.810  1.00 20.72 ? 214  ASN D C   1 
ATOM   15941 O  O   . ASN D 1 222 ? -3.656  -10.168 76.361  1.00 22.32 ? 214  ASN D O   1 
ATOM   15942 C  CB  . ASN D 1 222 ? -4.538  -9.515  73.680  1.00 22.83 ? 214  ASN D CB  1 
ATOM   15943 C  CG  . ASN D 1 222 ? -5.739  -8.680  74.103  1.00 26.22 ? 214  ASN D CG  1 
ATOM   15944 O  OD1 . ASN D 1 222 ? -5.745  -8.058  75.168  1.00 21.69 ? 214  ASN D OD1 1 
ATOM   15945 N  ND2 . ASN D 1 222 ? -6.764  -8.664  73.263  1.00 32.48 ? 214  ASN D ND2 1 
ATOM   15946 N  N   . GLY D 1 223 ? -2.819  -8.077  76.494  1.00 18.63 ? 215  GLY D N   1 
ATOM   15947 C  CA  . GLY D 1 223 ? -2.682  -8.091  77.937  1.00 16.78 ? 215  GLY D CA  1 
ATOM   15948 C  C   . GLY D 1 223 ? -3.977  -8.138  78.718  1.00 18.45 ? 215  GLY D C   1 
ATOM   15949 O  O   . GLY D 1 223 ? -3.929  -8.187  79.951  1.00 18.62 ? 215  GLY D O   1 
ATOM   15950 N  N   . HIS D 1 224 ? -5.130  -8.106  78.049  1.00 22.18 ? 216  HIS D N   1 
ATOM   15951 C  CA  . HIS D 1 224 ? -6.418  -8.246  78.722  1.00 18.97 ? 216  HIS D CA  1 
ATOM   15952 C  C   . HIS D 1 224 ? -7.167  -9.483  78.237  1.00 21.61 ? 216  HIS D C   1 
ATOM   15953 O  O   . HIS D 1 224 ? -8.382  -9.593  78.420  1.00 23.66 ? 216  HIS D O   1 
ATOM   15954 C  CB  . HIS D 1 224 ? -7.254  -6.977  78.536  1.00 23.67 ? 216  HIS D CB  1 
ATOM   15955 C  CG  . HIS D 1 224 ? -6.575  -5.746  79.061  1.00 24.04 ? 216  HIS D CG  1 
ATOM   15956 N  ND1 . HIS D 1 224 ? -6.166  -5.634  80.372  1.00 19.40 ? 216  HIS D ND1 1 
ATOM   15957 C  CD2 . HIS D 1 224 ? -6.208  -4.592  78.452  1.00 24.23 ? 216  HIS D CD2 1 
ATOM   15958 C  CE1 . HIS D 1 224 ? -5.576  -4.465  80.551  1.00 22.16 ? 216  HIS D CE1 1 
ATOM   15959 N  NE2 . HIS D 1 224 ? -5.590  -3.811  79.404  1.00 23.54 ? 216  HIS D NE2 1 
ATOM   15960 N  N   . ASP D 1 225 ? -6.452  -10.416 77.622  1.00 21.97 ? 217  ASP D N   1 
ATOM   15961 C  CA  . ASP D 1 225 ? -6.986  -11.694 77.156  1.00 20.09 ? 217  ASP D CA  1 
ATOM   15962 C  C   . ASP D 1 225 ? -6.292  -12.780 77.974  1.00 19.45 ? 217  ASP D C   1 
ATOM   15963 O  O   . ASP D 1 225 ? -5.141  -13.132 77.697  1.00 21.63 ? 217  ASP D O   1 
ATOM   15964 C  CB  . ASP D 1 225 ? -6.736  -11.855 75.657  1.00 21.67 ? 217  ASP D CB  1 
ATOM   15965 C  CG  . ASP D 1 225 ? -7.238  -13.179 75.109  1.00 28.94 ? 217  ASP D CG  1 
ATOM   15966 O  OD1 . ASP D 1 225 ? -7.626  -14.060 75.899  1.00 27.24 ? 217  ASP D OD1 1 
ATOM   15967 O  OD2 . ASP D 1 225 ? -7.236  -13.333 73.869  1.00 30.16 ? 217  ASP D OD2 1 
ATOM   15968 N  N   . THR D 1 226 ? -6.978  -13.305 78.993  1.00 24.23 ? 218  THR D N   1 
ATOM   15969 C  CA  . THR D 1 226 ? -6.328  -14.272 79.875  1.00 25.41 ? 218  THR D CA  1 
ATOM   15970 C  C   . THR D 1 226 ? -5.945  -15.544 79.134  1.00 25.80 ? 218  THR D C   1 
ATOM   15971 O  O   . THR D 1 226 ? -4.983  -16.219 79.521  1.00 26.65 ? 218  THR D O   1 
ATOM   15972 C  CB  . THR D 1 226 ? -7.223  -14.616 81.068  1.00 26.13 ? 218  THR D CB  1 
ATOM   15973 O  OG1 . THR D 1 226 ? -8.486  -15.107 80.602  1.00 23.60 ? 218  THR D OG1 1 
ATOM   15974 C  CG2 . THR D 1 226 ? -7.435  -13.391 81.945  1.00 29.42 ? 218  THR D CG2 1 
ATOM   15975 N  N   . ALA D 1 227 ? -6.681  -15.892 78.075  1.00 27.19 ? 219  ALA D N   1 
ATOM   15976 C  CA  . ALA D 1 227 ? -6.317  -17.061 77.281  1.00 26.40 ? 219  ALA D CA  1 
ATOM   15977 C  C   . ALA D 1 227 ? -5.011  -16.829 76.533  1.00 26.67 ? 219  ALA D C   1 
ATOM   15978 O  O   . ALA D 1 227 ? -4.155  -17.722 76.477  1.00 25.59 ? 219  ALA D O   1 
ATOM   15979 C  CB  . ALA D 1 227 ? -7.441  -17.414 76.306  1.00 26.65 ? 219  ALA D CB  1 
ATOM   15980 N  N   . ALA D 1 228 ? -4.833  -15.636 75.955  1.00 25.12 ? 220  ALA D N   1 
ATOM   15981 C  CA  . ALA D 1 228 ? -3.580  -15.341 75.265  1.00 24.46 ? 220  ALA D CA  1 
ATOM   15982 C  C   . ALA D 1 228 ? -2.419  -15.284 76.248  1.00 19.56 ? 220  ALA D C   1 
ATOM   15983 O  O   . ALA D 1 228 ? -1.318  -15.760 75.947  1.00 19.18 ? 220  ALA D O   1 
ATOM   15984 C  CB  . ALA D 1 228 ? -3.696  -14.028 74.492  1.00 22.92 ? 220  ALA D CB  1 
ATOM   15985 N  N   . ILE D 1 229 ? -2.649  -14.716 77.432  1.00 18.68 ? 221  ILE D N   1 
ATOM   15986 C  CA  . ILE D 1 229 ? -1.600  -14.657 78.448  1.00 18.61 ? 221  ILE D CA  1 
ATOM   15987 C  C   . ILE D 1 229 ? -1.209  -16.063 78.897  1.00 20.25 ? 221  ILE D C   1 
ATOM   15988 O  O   . ILE D 1 229 ? -0.019  -16.381 79.041  1.00 17.77 ? 221  ILE D O   1 
ATOM   15989 C  CB  . ILE D 1 229 ? -2.059  -13.789 79.634  1.00 20.28 ? 221  ILE D CB  1 
ATOM   15990 C  CG1 . ILE D 1 229 ? -2.310  -12.345 79.183  1.00 21.45 ? 221  ILE D CG1 1 
ATOM   15991 C  CG2 . ILE D 1 229 ? -1.001  -13.790 80.729  1.00 19.20 ? 221  ILE D CG2 1 
ATOM   15992 C  CD1 . ILE D 1 229 ? -3.155  -11.530 80.160  1.00 24.40 ? 221  ILE D CD1 1 
ATOM   15993 N  N   . GLN D 1 230 ? -2.201  -16.928 79.126  1.00 22.59 ? 222  GLN D N   1 
ATOM   15994 C  CA  . GLN D 1 230 ? -1.895  -18.294 79.536  1.00 21.01 ? 222  GLN D CA  1 
ATOM   15995 C  C   . GLN D 1 230 ? -1.079  -19.022 78.474  1.00 20.53 ? 222  GLN D C   1 
ATOM   15996 O  O   . GLN D 1 230 ? -0.109  -19.718 78.796  1.00 20.83 ? 222  GLN D O   1 
ATOM   15997 C  CB  . GLN D 1 230 ? -3.186  -19.059 79.842  1.00 25.10 ? 222  GLN D CB  1 
ATOM   15998 C  CG  . GLN D 1 230 ? -2.960  -20.531 80.161  1.00 30.31 ? 222  GLN D CG  1 
ATOM   15999 C  CD  . GLN D 1 230 ? -4.251  -21.272 80.450  1.00 35.64 ? 222  GLN D CD  1 
ATOM   16000 O  OE1 . GLN D 1 230 ? -5.203  -20.700 80.983  1.00 38.00 ? 222  GLN D OE1 1 
ATOM   16001 N  NE2 . GLN D 1 230 ? -4.292  -22.552 80.095  1.00 38.75 ? 222  GLN D NE2 1 
ATOM   16002 N  N   . THR D 1 231 ? -1.455  -18.874 77.201  1.00 20.96 ? 223  THR D N   1 
ATOM   16003 C  CA  . THR D 1 231 ? -0.697  -19.519 76.134  1.00 20.60 ? 223  THR D CA  1 
ATOM   16004 C  C   . THR D 1 231 ? 0.730   -18.993 76.090  1.00 22.75 ? 223  THR D C   1 
ATOM   16005 O  O   . THR D 1 231 ? 1.683   -19.761 75.899  1.00 25.51 ? 223  THR D O   1 
ATOM   16006 C  CB  . THR D 1 231 ? -1.396  -19.307 74.787  1.00 23.76 ? 223  THR D CB  1 
ATOM   16007 O  OG1 . THR D 1 231 ? -2.724  -19.829 74.854  1.00 25.08 ? 223  THR D OG1 1 
ATOM   16008 C  CG2 . THR D 1 231 ? -0.647  -20.007 73.669  1.00 23.74 ? 223  THR D CG2 1 
ATOM   16009 N  N   . ALA D 1 232 ? 0.896   -17.684 76.291  1.00 22.07 ? 224  ALA D N   1 
ATOM   16010 C  CA  . ALA D 1 232 ? 2.223   -17.087 76.270  1.00 19.34 ? 224  ALA D CA  1 
ATOM   16011 C  C   . ALA D 1 232 ? 3.076   -17.612 77.417  1.00 21.64 ? 224  ALA D C   1 
ATOM   16012 O  O   . ALA D 1 232 ? 4.264   -17.902 77.235  1.00 21.05 ? 224  ALA D O   1 
ATOM   16013 C  CB  . ALA D 1 232 ? 2.096   -15.565 76.336  1.00 19.13 ? 224  ALA D CB  1 
ATOM   16014 N  N   . ILE D 1 233 ? 2.483   -17.749 78.604  1.00 18.98 ? 225  ILE D N   1 
ATOM   16015 C  CA  . ILE D 1 233 ? 3.237   -18.246 79.748  1.00 17.44 ? 225  ILE D CA  1 
ATOM   16016 C  C   . ILE D 1 233 ? 3.600   -19.709 79.543  1.00 20.22 ? 225  ILE D C   1 
ATOM   16017 O  O   . ILE D 1 233 ? 4.718   -20.141 79.860  1.00 19.39 ? 225  ILE D O   1 
ATOM   16018 C  CB  . ILE D 1 233 ? 2.440   -18.025 81.047  1.00 23.85 ? 225  ILE D CB  1 
ATOM   16019 C  CG1 . ILE D 1 233 ? 2.232   -16.526 81.295  1.00 20.19 ? 225  ILE D CG1 1 
ATOM   16020 C  CG2 . ILE D 1 233 ? 3.157   -18.677 82.233  1.00 25.28 ? 225  ILE D CG2 1 
ATOM   16021 C  CD1 . ILE D 1 233 ? 1.371   -16.199 82.526  1.00 19.66 ? 225  ILE D CD1 1 
ATOM   16022 N  N   . GLU D 1 234 ? 2.671   -20.489 78.991  1.00 19.12 ? 226  GLU D N   1 
ATOM   16023 C  CA  . GLU D 1 234 ? 2.959   -21.883 78.672  1.00 19.87 ? 226  GLU D CA  1 
ATOM   16024 C  C   . GLU D 1 234 ? 4.126   -22.002 77.700  1.00 23.62 ? 226  GLU D C   1 
ATOM   16025 O  O   . GLU D 1 234 ? 5.014   -22.844 77.886  1.00 22.27 ? 226  GLU D O   1 
ATOM   16026 C  CB  . GLU D 1 234 ? 1.704   -22.556 78.111  1.00 27.13 ? 226  GLU D CB  1 
ATOM   16027 C  CG  . GLU D 1 234 ? 0.646   -22.791 79.179  1.00 24.64 ? 226  GLU D CG  1 
ATOM   16028 C  CD  . GLU D 1 234 ? -0.672  -23.284 78.631  1.00 31.75 ? 226  GLU D CD  1 
ATOM   16029 O  OE1 . GLU D 1 234 ? -0.806  -23.410 77.397  1.00 32.25 ? 226  GLU D OE1 1 
ATOM   16030 O  OE2 . GLU D 1 234 ? -1.574  -23.540 79.451  1.00 28.15 ? 226  GLU D OE2 1 
ATOM   16031 N  N   . ALA D 1 235 ? 4.153   -21.158 76.663  1.00 24.53 ? 227  ALA D N   1 
ATOM   16032 C  CA  . ALA D 1 235 ? 5.283   -21.173 75.739  1.00 25.00 ? 227  ALA D CA  1 
ATOM   16033 C  C   . ALA D 1 235 ? 6.577   -20.790 76.449  1.00 21.36 ? 227  ALA D C   1 
ATOM   16034 O  O   . ALA D 1 235 ? 7.634   -21.377 76.194  1.00 21.89 ? 227  ALA D O   1 
ATOM   16035 C  CB  . ALA D 1 235 ? 5.018   -20.232 74.565  1.00 29.32 ? 227  ALA D CB  1 
ATOM   16036 N  N   . ALA D 1 236 ? 6.503   -19.820 77.356  1.00 18.38 ? 228  ALA D N   1 
ATOM   16037 C  CA  . ALA D 1 236 ? 7.674   -19.410 78.127  1.00 24.26 ? 228  ALA D CA  1 
ATOM   16038 C  C   . ALA D 1 236 ? 8.225   -20.565 78.959  1.00 21.48 ? 228  ALA D C   1 
ATOM   16039 O  O   . ALA D 1 236 ? 9.435   -20.822 78.975  1.00 21.24 ? 228  ALA D O   1 
ATOM   16040 C  CB  . ALA D 1 236 ? 7.304   -18.232 79.030  1.00 21.19 ? 228  ALA D CB  1 
ATOM   16041 N  N   . ARG D 1 237 ? 7.348   -21.265 79.671  1.00 18.29 ? 229  ARG D N   1 
ATOM   16042 C  CA  . ARG D 1 237 ? 7.793   -22.379 80.496  1.00 22.12 ? 229  ARG D CA  1 
ATOM   16043 C  C   . ARG D 1 237 ? 8.331   -23.530 79.650  1.00 28.70 ? 229  ARG D C   1 
ATOM   16044 O  O   . ARG D 1 237 ? 9.217   -24.267 80.101  1.00 26.39 ? 229  ARG D O   1 
ATOM   16045 C  CB  . ARG D 1 237 ? 6.638   -22.838 81.385  1.00 20.95 ? 229  ARG D CB  1 
ATOM   16046 C  CG  . ARG D 1 237 ? 6.172   -21.761 82.360  1.00 22.02 ? 229  ARG D CG  1 
ATOM   16047 C  CD  . ARG D 1 237 ? 4.823   -22.097 82.976  1.00 24.16 ? 229  ARG D CD  1 
ATOM   16048 N  NE  . ARG D 1 237 ? 4.767   -23.487 83.417  1.00 28.77 ? 229  ARG D NE  1 
ATOM   16049 C  CZ  . ARG D 1 237 ? 5.260   -23.920 84.571  1.00 33.56 ? 229  ARG D CZ  1 
ATOM   16050 N  NH1 . ARG D 1 237 ? 5.849   -23.069 85.399  1.00 25.39 ? 229  ARG D NH1 1 
ATOM   16051 N  NH2 . ARG D 1 237 ? 5.171   -25.205 84.892  1.00 34.99 ? 229  ARG D NH2 1 
ATOM   16052 N  N   . ALA D 1 238 ? 7.831   -23.685 78.420  1.00 24.78 ? 230  ALA D N   1 
ATOM   16053 C  CA  . ALA D 1 238 ? 8.317   -24.747 77.545  1.00 27.85 ? 230  ALA D CA  1 
ATOM   16054 C  C   . ALA D 1 238 ? 9.712   -24.453 77.018  1.00 27.56 ? 230  ALA D C   1 
ATOM   16055 O  O   . ALA D 1 238 ? 10.443  -25.380 76.659  1.00 25.89 ? 230  ALA D O   1 
ATOM   16056 C  CB  . ALA D 1 238 ? 7.355   -24.952 76.372  1.00 29.90 ? 230  ALA D CB  1 
ATOM   16057 N  N   . GLU D 1 239 ? 10.093  -23.180 76.951  1.00 25.90 ? 231  GLU D N   1 
ATOM   16058 C  CA  . GLU D 1 239 ? 11.440  -22.792 76.544  1.00 26.07 ? 231  GLU D CA  1 
ATOM   16059 C  C   . GLU D 1 239 ? 12.345  -22.892 77.764  1.00 28.08 ? 231  GLU D C   1 
ATOM   16060 O  O   . GLU D 1 239 ? 12.342  -22.017 78.631  1.00 34.64 ? 231  GLU D O   1 
ATOM   16061 C  CB  . GLU D 1 239 ? 11.444  -21.386 75.956  1.00 31.20 ? 231  GLU D CB  1 
ATOM   16062 C  CG  . GLU D 1 239 ? 12.840  -20.851 75.714  1.00 34.88 ? 231  GLU D CG  1 
ATOM   16063 C  CD  . GLU D 1 239 ? 13.662  -21.781 74.854  1.00 36.49 ? 231  GLU D CD  1 
ATOM   16064 O  OE1 . GLU D 1 239 ? 13.244  -22.052 73.710  1.00 36.54 ? 231  GLU D OE1 1 
ATOM   16065 O  OE2 . GLU D 1 239 ? 14.714  -22.259 75.332  1.00 39.32 ? 231  GLU D OE2 1 
ATOM   16066 N  N   . THR D 1 240 ? 13.120  -23.969 77.848  1.00 27.80 ? 232  THR D N   1 
ATOM   16067 C  CA  . THR D 1 240 ? 13.887  -24.223 79.057  1.00 26.21 ? 232  THR D CA  1 
ATOM   16068 C  C   . THR D 1 240 ? 15.291  -23.642 79.011  1.00 25.81 ? 232  THR D C   1 
ATOM   16069 O  O   . THR D 1 240 ? 15.959  -23.605 80.049  1.00 28.25 ? 232  THR D O   1 
ATOM   16070 C  CB  . THR D 1 240 ? 13.988  -25.729 79.330  1.00 33.41 ? 232  THR D CB  1 
ATOM   16071 O  OG1 . THR D 1 240 ? 14.658  -26.367 78.240  1.00 37.30 ? 232  THR D OG1 1 
ATOM   16072 C  CG2 . THR D 1 240 ? 12.600  -26.341 79.500  1.00 34.60 ? 232  THR D CG2 1 
ATOM   16073 N  N   . GLY D 1 241 ? 15.757  -23.199 77.851  1.00 23.05 ? 233  GLY D N   1 
ATOM   16074 C  CA  . GLY D 1 241 ? 17.145  -22.804 77.722  1.00 26.72 ? 233  GLY D CA  1 
ATOM   16075 C  C   . GLY D 1 241 ? 17.388  -21.314 77.840  1.00 24.38 ? 233  GLY D C   1 
ATOM   16076 O  O   . GLY D 1 241 ? 18.523  -20.886 78.062  1.00 28.11 ? 233  GLY D O   1 
ATOM   16077 N  N   . LYS D 1 242 ? 16.340  -20.515 77.687  1.00 19.03 ? 234  LYS D N   1 
ATOM   16078 C  CA  . LYS D 1 242 ? 16.449  -19.068 77.633  1.00 20.20 ? 234  LYS D CA  1 
ATOM   16079 C  C   . LYS D 1 242 ? 15.465  -18.438 78.605  1.00 21.13 ? 234  LYS D C   1 
ATOM   16080 O  O   . LYS D 1 242 ? 14.346  -18.934 78.759  1.00 21.74 ? 234  LYS D O   1 
ATOM   16081 C  CB  . LYS D 1 242 ? 16.138  -18.532 76.224  1.00 19.40 ? 234  LYS D CB  1 
ATOM   16082 C  CG  . LYS D 1 242 ? 16.898  -19.176 75.080  1.00 29.97 ? 234  LYS D CG  1 
ATOM   16083 C  CD  . LYS D 1 242 ? 16.352  -18.656 73.755  1.00 30.43 ? 234  LYS D CD  1 
ATOM   16084 C  CE  . LYS D 1 242 ? 17.122  -19.197 72.573  1.00 36.10 ? 234  LYS D CE  1 
ATOM   16085 N  NZ  . LYS D 1 242 ? 16.688  -18.543 71.304  1.00 38.81 ? 234  LYS D NZ  1 
ATOM   16086 N  N   . PRO D 1 243 ? 15.830  -17.321 79.234  1.00 19.97 ? 235  PRO D N   1 
ATOM   16087 C  CA  . PRO D 1 243 ? 14.816  -16.517 79.927  1.00 16.39 ? 235  PRO D CA  1 
ATOM   16088 C  C   . PRO D 1 243 ? 13.830  -15.956 78.920  1.00 20.36 ? 235  PRO D C   1 
ATOM   16089 O  O   . PRO D 1 243 ? 14.177  -15.713 77.762  1.00 18.38 ? 235  PRO D O   1 
ATOM   16090 C  CB  . PRO D 1 243 ? 15.630  -15.403 80.597  1.00 15.81 ? 235  PRO D CB  1 
ATOM   16091 C  CG  . PRO D 1 243 ? 16.861  -15.283 79.748  1.00 14.60 ? 235  PRO D CG  1 
ATOM   16092 C  CD  . PRO D 1 243 ? 17.152  -16.673 79.232  1.00 15.41 ? 235  PRO D CD  1 
ATOM   16093 N  N   . SER D 1 244 ? 12.582  -15.763 79.373  1.00 19.69 ? 236  SER D N   1 
ATOM   16094 C  CA  . SER D 1 244 ? 11.479  -15.352 78.514  1.00 20.78 ? 236  SER D CA  1 
ATOM   16095 C  C   . SER D 1 244 ? 10.943  -13.990 78.929  1.00 17.19 ? 236  SER D C   1 
ATOM   16096 O  O   . SER D 1 244 ? 10.802  -13.701 80.122  1.00 16.20 ? 236  SER D O   1 
ATOM   16097 C  CB  . SER D 1 244 ? 10.312  -16.367 78.556  1.00 18.82 ? 236  SER D CB  1 
ATOM   16098 O  OG  . SER D 1 244 ? 10.702  -17.646 78.118  1.00 22.41 ? 236  SER D OG  1 
ATOM   16099 N  N   . ILE D 1 245 ? 10.607  -13.161 77.943  1.00 15.57 ? 237  ILE D N   1 
ATOM   16100 C  CA  . ILE D 1 245 ? 9.856   -11.936 78.189  1.00 16.19 ? 237  ILE D CA  1 
ATOM   16101 C  C   . ILE D 1 245 ? 8.590   -11.981 77.343  1.00 16.75 ? 237  ILE D C   1 
ATOM   16102 O  O   . ILE D 1 245 ? 8.642   -12.295 76.146  1.00 15.19 ? 237  ILE D O   1 
ATOM   16103 C  CB  . ILE D 1 245 ? 10.690  -10.666 77.911  1.00 15.15 ? 237  ILE D CB  1 
ATOM   16104 C  CG1 . ILE D 1 245 ? 9.854   -9.404  78.195  1.00 16.29 ? 237  ILE D CG1 1 
ATOM   16105 C  CG2 . ILE D 1 245 ? 11.248  -10.665 76.477  1.00 16.45 ? 237  ILE D CG2 1 
ATOM   16106 C  CD1 . ILE D 1 245 ? 10.675  -8.090  78.276  1.00 13.73 ? 237  ILE D CD1 1 
ATOM   16107 N  N   . ILE D 1 246 ? 7.455   -11.712 77.983  1.00 14.51 ? 238  ILE D N   1 
ATOM   16108 C  CA  . ILE D 1 246 ? 6.140   -11.712 77.347  1.00 15.81 ? 238  ILE D CA  1 
ATOM   16109 C  C   . ILE D 1 246 ? 5.660   -10.270 77.307  1.00 16.32 ? 238  ILE D C   1 
ATOM   16110 O  O   . ILE D 1 246 ? 5.449   -9.654  78.359  1.00 14.25 ? 238  ILE D O   1 
ATOM   16111 C  CB  . ILE D 1 246 ? 5.143   -12.598 78.110  1.00 16.98 ? 238  ILE D CB  1 
ATOM   16112 C  CG1 . ILE D 1 246 ? 5.647   -14.039 78.181  1.00 21.96 ? 238  ILE D CG1 1 
ATOM   16113 C  CG2 . ILE D 1 246 ? 3.755   -12.548 77.460  1.00 16.36 ? 238  ILE D CG2 1 
ATOM   16114 C  CD1 . ILE D 1 246 ? 4.877   -14.905 79.174  1.00 20.45 ? 238  ILE D CD1 1 
ATOM   16115 N  N   . CYS D 1 247 ? 5.500   -9.721  76.103  1.00 16.17 ? 239  CYS D N   1 
ATOM   16116 C  CA  . CYS D 1 247 ? 5.156   -8.305  75.951  1.00 18.43 ? 239  CYS D CA  1 
ATOM   16117 C  C   . CYS D 1 247 ? 3.639   -8.171  75.972  1.00 17.03 ? 239  CYS D C   1 
ATOM   16118 O  O   . CYS D 1 247 ? 2.964   -8.477  74.989  1.00 16.59 ? 239  CYS D O   1 
ATOM   16119 C  CB  . CYS D 1 247 ? 5.748   -7.741  74.667  1.00 15.85 ? 239  CYS D CB  1 
ATOM   16120 S  SG  . CYS D 1 247 ? 7.527   -7.933  74.625  1.00 20.27 ? 239  CYS D SG  1 
ATOM   16121 N  N   . CYS D 1 248 ? 3.110   -7.694  77.093  1.00 14.98 ? 240  CYS D N   1 
ATOM   16122 C  CA  . CYS D 1 248 ? 1.672   -7.622  77.318  1.00 19.48 ? 240  CYS D CA  1 
ATOM   16123 C  C   . CYS D 1 248 ? 1.176   -6.224  76.987  1.00 17.74 ? 240  CYS D C   1 
ATOM   16124 O  O   . CYS D 1 248 ? 1.420   -5.277  77.743  1.00 16.65 ? 240  CYS D O   1 
ATOM   16125 C  CB  . CYS D 1 248 ? 1.339   -7.987  78.762  1.00 19.53 ? 240  CYS D CB  1 
ATOM   16126 S  SG  . CYS D 1 248 ? 1.742   -9.691  79.131  1.00 21.89 ? 240  CYS D SG  1 
ATOM   16127 N  N   . LYS D 1 249 ? 0.476   -6.101  75.864  1.00 17.75 ? 241  LYS D N   1 
ATOM   16128 C  CA  A LYS D 1 249 ? -0.124  -4.832  75.467  0.33 19.93 ? 241  LYS D CA  1 
ATOM   16129 C  CA  B LYS D 1 249 ? -0.127  -4.834  75.463  0.67 19.80 ? 241  LYS D CA  1 
ATOM   16130 C  C   . LYS D 1 249 ? -1.343  -4.561  76.340  1.00 17.44 ? 241  LYS D C   1 
ATOM   16131 O  O   . LYS D 1 249 ? -2.350  -5.271  76.246  1.00 17.30 ? 241  LYS D O   1 
ATOM   16132 C  CB  A LYS D 1 249 ? -0.513  -4.871  73.992  0.33 23.67 ? 241  LYS D CB  1 
ATOM   16133 C  CB  B LYS D 1 249 ? -0.526  -4.890  73.991  0.67 23.70 ? 241  LYS D CB  1 
ATOM   16134 C  CG  A LYS D 1 249 ? 0.636   -5.154  73.032  0.33 26.53 ? 241  LYS D CG  1 
ATOM   16135 C  CG  B LYS D 1 249 ? 0.601   -5.268  73.036  0.67 26.27 ? 241  LYS D CG  1 
ATOM   16136 C  CD  A LYS D 1 249 ? 1.632   -4.004  72.998  0.33 28.92 ? 241  LYS D CD  1 
ATOM   16137 C  CD  B LYS D 1 249 ? 1.642   -4.163  72.958  0.67 29.94 ? 241  LYS D CD  1 
ATOM   16138 C  CE  A LYS D 1 249 ? 2.617   -4.156  71.846  0.33 28.40 ? 241  LYS D CE  1 
ATOM   16139 C  CE  B LYS D 1 249 ? 2.727   -4.475  71.936  0.67 28.69 ? 241  LYS D CE  1 
ATOM   16140 N  NZ  A LYS D 1 249 ? 3.392   -5.424  71.936  0.33 27.16 ? 241  LYS D NZ  1 
ATOM   16141 N  NZ  B LYS D 1 249 ? 3.733   -3.380  71.886  0.67 24.70 ? 241  LYS D NZ  1 
ATOM   16142 N  N   . THR D 1 250 ? -1.264  -3.535  77.193  1.00 16.41 ? 242  THR D N   1 
ATOM   16143 C  CA  . THR D 1 250 ? -2.359  -3.200  78.099  1.00 17.41 ? 242  THR D CA  1 
ATOM   16144 C  C   . THR D 1 250 ? -2.761  -1.740  77.952  1.00 22.79 ? 242  THR D C   1 
ATOM   16145 O  O   . THR D 1 250 ? -2.049  -0.928  77.362  1.00 22.04 ? 242  THR D O   1 
ATOM   16146 C  CB  . THR D 1 250 ? -1.988  -3.433  79.568  1.00 18.22 ? 242  THR D CB  1 
ATOM   16147 O  OG1 . THR D 1 250 ? -0.879  -2.585  79.909  1.00 21.27 ? 242  THR D OG1 1 
ATOM   16148 C  CG2 . THR D 1 250 ? -1.643  -4.904  79.834  1.00 17.13 ? 242  THR D CG2 1 
ATOM   16149 N  N   . LEU D 1 251 ? -3.915  -1.409  78.530  1.00 17.57 ? 243  LEU D N   1 
ATOM   16150 C  CA  . LEU D 1 251 ? -4.333  -0.028  78.730  1.00 21.00 ? 243  LEU D CA  1 
ATOM   16151 C  C   . LEU D 1 251 ? -4.140  0.334   80.198  1.00 22.55 ? 243  LEU D C   1 
ATOM   16152 O  O   . LEU D 1 251 ? -4.677  -0.345  81.079  1.00 21.30 ? 243  LEU D O   1 
ATOM   16153 C  CB  . LEU D 1 251 ? -5.795  0.164   78.329  1.00 26.02 ? 243  LEU D CB  1 
ATOM   16154 C  CG  . LEU D 1 251 ? -6.143  -0.119  76.865  1.00 25.15 ? 243  LEU D CG  1 
ATOM   16155 C  CD1 . LEU D 1 251 ? -7.633  -0.012  76.665  1.00 27.32 ? 243  LEU D CD1 1 
ATOM   16156 C  CD2 . LEU D 1 251 ? -5.416  0.859   75.982  1.00 26.65 ? 243  LEU D CD2 1 
ATOM   16157 N  N   . ILE D 1 252 ? -3.374  1.397   80.463  1.00 19.30 ? 244  ILE D N   1 
ATOM   16158 C  CA  . ILE D 1 252 ? -3.286  1.895   81.831  1.00 17.82 ? 244  ILE D CA  1 
ATOM   16159 C  C   . ILE D 1 252 ? -4.672  2.339   82.288  1.00 16.25 ? 244  ILE D C   1 
ATOM   16160 O  O   . ILE D 1 252 ? -5.450  2.922   81.523  1.00 19.61 ? 244  ILE D O   1 
ATOM   16161 C  CB  . ILE D 1 252 ? -2.255  3.033   81.940  1.00 21.42 ? 244  ILE D CB  1 
ATOM   16162 C  CG1 . ILE D 1 252 ? -1.942  3.336   83.407  1.00 25.19 ? 244  ILE D CG1 1 
ATOM   16163 C  CG2 . ILE D 1 252 ? -2.727  4.293   81.215  1.00 23.46 ? 244  ILE D CG2 1 
ATOM   16164 C  CD1 . ILE D 1 252 ? -0.770  4.284   83.595  1.00 23.93 ? 244  ILE D CD1 1 
ATOM   16165 N  N   . GLY D 1 253 ? -5.005  2.023   83.537  1.00 18.64 ? 245  GLY D N   1 
ATOM   16166 C  CA  . GLY D 1 253 ? -6.335  2.325   84.020  1.00 16.57 ? 245  GLY D CA  1 
ATOM   16167 C  C   . GLY D 1 253 ? -7.434  1.549   83.333  1.00 21.25 ? 245  GLY D C   1 
ATOM   16168 O  O   . GLY D 1 253 ? -8.574  2.014   83.306  1.00 21.68 ? 245  GLY D O   1 
ATOM   16169 N  N   . LYS D 1 254 ? -7.111  0.386   82.760  1.00 17.81 ? 246  LYS D N   1 
ATOM   16170 C  CA  . LYS D 1 254 ? -8.098  -0.451  82.082  1.00 18.25 ? 246  LYS D CA  1 
ATOM   16171 C  C   . LYS D 1 254 ? -9.316  -0.675  82.967  1.00 22.69 ? 246  LYS D C   1 
ATOM   16172 O  O   . LYS D 1 254 ? -9.190  -1.003  84.149  1.00 22.88 ? 246  LYS D O   1 
ATOM   16173 C  CB  . LYS D 1 254 ? -7.465  -1.795  81.709  1.00 22.16 ? 246  LYS D CB  1 
ATOM   16174 C  CG  . LYS D 1 254 ? -8.439  -2.834  81.128  1.00 25.70 ? 246  LYS D CG  1 
ATOM   16175 C  CD  . LYS D 1 254 ? -8.839  -2.501  79.695  1.00 30.39 ? 246  LYS D CD  1 
ATOM   16176 C  CE  . LYS D 1 254 ? -9.815  -3.542  79.141  1.00 29.05 ? 246  LYS D CE  1 
ATOM   16177 N  NZ  . LYS D 1 254 ? -10.451 -3.086  77.881  1.00 37.48 ? 246  LYS D NZ  1 
ATOM   16178 N  N   . GLY D 1 255 ? -10.501 -0.488  82.385  1.00 24.32 ? 247  GLY D N   1 
ATOM   16179 C  CA  . GLY D 1 255 ? -11.740 -0.600  83.119  1.00 27.29 ? 247  GLY D CA  1 
ATOM   16180 C  C   . GLY D 1 255 ? -12.283 0.705   83.665  1.00 24.07 ? 247  GLY D C   1 
ATOM   16181 O  O   . GLY D 1 255 ? -13.456 0.750   84.068  1.00 22.07 ? 247  GLY D O   1 
ATOM   16182 N  N   . SER D 1 256 ? -11.474 1.762   83.708  1.00 21.98 ? 248  SER D N   1 
ATOM   16183 C  CA  . SER D 1 256 ? -11.984 3.055   84.143  1.00 20.54 ? 248  SER D CA  1 
ATOM   16184 C  C   . SER D 1 256 ? -13.041 3.543   83.166  1.00 21.08 ? 248  SER D C   1 
ATOM   16185 O  O   . SER D 1 256 ? -12.901 3.401   81.948  1.00 27.42 ? 248  SER D O   1 
ATOM   16186 C  CB  . SER D 1 256 ? -10.844 4.071   84.252  1.00 25.69 ? 248  SER D CB  1 
ATOM   16187 O  OG  . SER D 1 256 ? -11.339 5.371   84.504  1.00 28.38 ? 248  SER D OG  1 
ATOM   16188 N  N   . ALA D 1 257 ? -14.119 4.111   83.708  1.00 23.82 ? 249  ALA D N   1 
ATOM   16189 C  CA  . ALA D 1 257 ? -15.232 4.523   82.862  1.00 29.26 ? 249  ALA D CA  1 
ATOM   16190 C  C   . ALA D 1 257 ? -14.871 5.703   81.966  1.00 32.55 ? 249  ALA D C   1 
ATOM   16191 O  O   . ALA D 1 257 ? -15.403 5.815   80.854  1.00 35.20 ? 249  ALA D O   1 
ATOM   16192 C  CB  . ALA D 1 257 ? -16.439 4.875   83.725  1.00 23.69 ? 249  ALA D CB  1 
ATOM   16193 N  N   . ASN D 1 258 ? -13.974 6.585   82.424  1.00 27.76 ? 250  ASN D N   1 
ATOM   16194 C  CA  . ASN D 1 258 ? -13.650 7.817   81.709  1.00 23.89 ? 250  ASN D CA  1 
ATOM   16195 C  C   . ASN D 1 258 ? -12.163 8.120   81.608  1.00 26.31 ? 250  ASN D C   1 
ATOM   16196 O  O   . ASN D 1 258 ? -11.790 8.997   80.824  1.00 28.71 ? 250  ASN D O   1 
ATOM   16197 C  CB  . ASN D 1 258 ? -14.330 9.020   82.378  1.00 25.16 ? 250  ASN D CB  1 
ATOM   16198 C  CG  . ASN D 1 258 ? -15.836 8.901   82.387  1.00 27.83 ? 250  ASN D CG  1 
ATOM   16199 O  OD1 . ASN D 1 258 ? -16.490 9.142   81.375  1.00 28.29 ? 250  ASN D OD1 1 
ATOM   16200 N  ND2 . ASN D 1 258 ? -16.398 8.536   83.534  1.00 27.13 ? 250  ASN D ND2 1 
ATOM   16201 N  N   . LYS D 1 259 ? -11.310 7.456   82.385  1.00 22.18 ? 251  LYS D N   1 
ATOM   16202 C  CA  . LYS D 1 259 ? -9.884  7.738   82.379  1.00 21.32 ? 251  LYS D CA  1 
ATOM   16203 C  C   . LYS D 1 259 ? -9.076  6.563   81.849  1.00 21.07 ? 251  LYS D C   1 
ATOM   16204 O  O   . LYS D 1 259 ? -7.860  6.519   82.029  1.00 24.49 ? 251  LYS D O   1 
ATOM   16205 C  CB  . LYS D 1 259 ? -9.423  8.127   83.783  1.00 23.88 ? 251  LYS D CB  1 
ATOM   16206 C  CG  . LYS D 1 259 ? -10.219 9.280   84.354  1.00 23.25 ? 251  LYS D CG  1 
ATOM   16207 C  CD  . LYS D 1 259 ? -9.639  9.766   85.677  1.00 20.22 ? 251  LYS D CD  1 
ATOM   16208 C  CE  . LYS D 1 259 ? -10.286 11.101  86.090  1.00 21.35 ? 251  LYS D CE  1 
ATOM   16209 N  NZ  . LYS D 1 259 ? -9.727  11.595  87.384  1.00 24.66 ? 251  LYS D NZ  1 
ATOM   16210 N  N   . GLU D 1 260 ? -9.734  5.609   81.200  1.00 26.24 ? 252  GLU D N   1 
ATOM   16211 C  CA  . GLU D 1 260 ? -9.027  4.464   80.647  1.00 23.87 ? 252  GLU D CA  1 
ATOM   16212 C  C   . GLU D 1 260 ? -8.020  4.928   79.604  1.00 26.85 ? 252  GLU D C   1 
ATOM   16213 O  O   . GLU D 1 260 ? -8.347  5.737   78.730  1.00 27.06 ? 252  GLU D O   1 
ATOM   16214 C  CB  . GLU D 1 260 ? -10.024 3.495   80.022  1.00 25.84 ? 252  GLU D CB  1 
ATOM   16215 C  CG  . GLU D 1 260 ? -9.397  2.244   79.468  1.00 25.75 ? 252  GLU D CG  1 
ATOM   16216 C  CD  . GLU D 1 260 ? -10.450 1.244   79.081  1.00 28.79 ? 252  GLU D CD  1 
ATOM   16217 O  OE1 . GLU D 1 260 ? -10.938 1.315   77.931  1.00 35.18 ? 252  GLU D OE1 1 
ATOM   16218 O  OE2 . GLU D 1 260 ? -10.817 0.410   79.934  1.00 25.21 ? 252  GLU D OE2 1 
ATOM   16219 N  N   . GLY D 1 261 ? -6.794  4.417   79.705  1.00 27.18 ? 253  GLY D N   1 
ATOM   16220 C  CA  . GLY D 1 261 ? -5.717  4.800   78.822  1.00 31.14 ? 253  GLY D CA  1 
ATOM   16221 C  C   . GLY D 1 261 ? -5.064  6.123   79.144  1.00 29.29 ? 253  GLY D C   1 
ATOM   16222 O  O   . GLY D 1 261 ? -4.112  6.510   78.456  1.00 30.79 ? 253  GLY D O   1 
ATOM   16223 N  N   . SER D 1 262 ? -5.523  6.823   80.174  1.00 28.02 ? 254  SER D N   1 
ATOM   16224 C  CA  . SER D 1 262 ? -5.040  8.163   80.463  1.00 30.59 ? 254  SER D CA  1 
ATOM   16225 C  C   . SER D 1 262 ? -3.839  8.105   81.395  1.00 29.40 ? 254  SER D C   1 
ATOM   16226 O  O   . SER D 1 262 ? -3.901  7.486   82.465  1.00 27.90 ? 254  SER D O   1 
ATOM   16227 C  CB  . SER D 1 262 ? -6.143  9.015   81.086  1.00 33.86 ? 254  SER D CB  1 
ATOM   16228 O  OG  . SER D 1 262 ? -5.606  10.242  81.533  1.00 33.58 ? 254  SER D OG  1 
ATOM   16229 N  N   . HIS D 1 263 ? -2.756  8.778   80.997  1.00 40.82 ? 255  HIS D N   1 
ATOM   16230 C  CA  . HIS D 1 263 ? -1.559  8.822   81.827  1.00 42.13 ? 255  HIS D CA  1 
ATOM   16231 C  C   . HIS D 1 263 ? -1.822  9.450   83.192  1.00 38.57 ? 255  HIS D C   1 
ATOM   16232 O  O   . HIS D 1 263 ? -1.024  9.252   84.114  1.00 32.76 ? 255  HIS D O   1 
ATOM   16233 C  CB  . HIS D 1 263 ? -0.447  9.585   81.099  1.00 52.20 ? 255  HIS D CB  1 
ATOM   16234 C  CG  . HIS D 1 263 ? -0.429  11.056  81.381  1.00 60.31 ? 255  HIS D CG  1 
ATOM   16235 N  ND1 . HIS D 1 263 ? -1.423  11.911  80.955  1.00 62.54 ? 255  HIS D ND1 1 
ATOM   16236 C  CD2 . HIS D 1 263 ? 0.469   11.824  82.043  1.00 62.17 ? 255  HIS D CD2 1 
ATOM   16237 C  CE1 . HIS D 1 263 ? -1.140  13.141  81.346  1.00 64.66 ? 255  HIS D CE1 1 
ATOM   16238 N  NE2 . HIS D 1 263 ? 0.003   13.116  82.008  1.00 63.70 ? 255  HIS D NE2 1 
ATOM   16239 N  N   . LYS D 1 264 ? -2.928  10.188  83.352  1.00 39.13 ? 256  LYS D N   1 
ATOM   16240 C  CA  . LYS D 1 264 ? -3.236  10.772  84.652  1.00 38.74 ? 256  LYS D CA  1 
ATOM   16241 C  C   . LYS D 1 264 ? -3.596  9.718   85.695  1.00 35.26 ? 256  LYS D C   1 
ATOM   16242 O  O   . LYS D 1 264 ? -3.610  10.042  86.887  1.00 29.45 ? 256  LYS D O   1 
ATOM   16243 C  CB  . LYS D 1 264 ? -4.369  11.801  84.529  1.00 44.68 ? 256  LYS D CB  1 
ATOM   16244 C  CG  . LYS D 1 264 ? -5.764  11.209  84.353  1.00 51.44 ? 256  LYS D CG  1 
ATOM   16245 C  CD  . LYS D 1 264 ? -6.758  12.260  83.845  1.00 56.94 ? 256  LYS D CD  1 
ATOM   16246 C  CE  . LYS D 1 264 ? -7.936  11.622  83.114  1.00 56.19 ? 256  LYS D CE  1 
ATOM   16247 N  NZ  . LYS D 1 264 ? -8.968  12.611  82.676  1.00 57.56 ? 256  LYS D NZ  1 
ATOM   16248 N  N   . THR D 1 265 ? -3.891  8.474   85.283  1.00 23.99 ? 257  THR D N   1 
ATOM   16249 C  CA  . THR D 1 265 ? -4.140  7.399   86.240  1.00 24.02 ? 257  THR D CA  1 
ATOM   16250 C  C   . THR D 1 265 ? -2.853  6.752   86.737  1.00 25.13 ? 257  THR D C   1 
ATOM   16251 O  O   . THR D 1 265 ? -2.913  5.870   87.604  1.00 22.68 ? 257  THR D O   1 
ATOM   16252 C  CB  . THR D 1 265 ? -5.046  6.310   85.641  1.00 27.88 ? 257  THR D CB  1 
ATOM   16253 O  OG1 . THR D 1 265 ? -4.363  5.630   84.577  1.00 25.58 ? 257  THR D OG1 1 
ATOM   16254 C  CG2 . THR D 1 265 ? -6.346  6.906   85.110  1.00 31.00 ? 257  THR D CG2 1 
ATOM   16255 N  N   . HIS D 1 266 ? -1.695  7.168   86.222  1.00 26.00 ? 258  HIS D N   1 
ATOM   16256 C  CA  . HIS D 1 266 ? -0.447  6.552   86.651  1.00 27.23 ? 258  HIS D CA  1 
ATOM   16257 C  C   . HIS D 1 266 ? -0.162  6.835   88.124  1.00 23.21 ? 258  HIS D C   1 
ATOM   16258 O  O   . HIS D 1 266 ? 0.064   5.908   88.908  1.00 24.92 ? 258  HIS D O   1 
ATOM   16259 C  CB  . HIS D 1 266 ? 0.710   7.035   85.777  1.00 31.40 ? 258  HIS D CB  1 
ATOM   16260 C  CG  . HIS D 1 266 ? 2.035   6.461   86.171  1.00 40.95 ? 258  HIS D CG  1 
ATOM   16261 N  ND1 . HIS D 1 266 ? 2.942   7.149   86.948  1.00 41.17 ? 258  HIS D ND1 1 
ATOM   16262 C  CD2 . HIS D 1 266 ? 2.597   5.255   85.914  1.00 41.76 ? 258  HIS D CD2 1 
ATOM   16263 C  CE1 . HIS D 1 266 ? 4.011   6.398   87.141  1.00 41.96 ? 258  HIS D CE1 1 
ATOM   16264 N  NE2 . HIS D 1 266 ? 3.828   5.244   86.524  1.00 42.70 ? 258  HIS D NE2 1 
ATOM   16265 N  N   . GLY D 1 267 ? -0.179  8.104   88.522  1.00 23.21 ? 259  GLY D N   1 
ATOM   16266 C  CA  . GLY D 1 267 ? 0.330   8.467   89.837  1.00 24.76 ? 259  GLY D CA  1 
ATOM   16267 C  C   . GLY D 1 267 ? -0.600  9.298   90.700  1.00 28.40 ? 259  GLY D C   1 
ATOM   16268 O  O   . GLY D 1 267 ? -0.155  9.947   91.654  1.00 24.61 ? 259  GLY D O   1 
ATOM   16269 N  N   . ALA D 1 268 ? -1.893  9.285   90.396  1.00 24.64 ? 260  ALA D N   1 
ATOM   16270 C  CA  . ALA D 1 268 ? -2.861  10.041  91.175  1.00 25.41 ? 260  ALA D CA  1 
ATOM   16271 C  C   . ALA D 1 268 ? -4.122  9.215   91.371  1.00 22.66 ? 260  ALA D C   1 
ATOM   16272 O  O   . ALA D 1 268 ? -4.447  8.362   90.536  1.00 22.11 ? 260  ALA D O   1 
ATOM   16273 C  CB  . ALA D 1 268 ? -3.222  11.376  90.501  1.00 29.34 ? 260  ALA D CB  1 
ATOM   16274 N  N   . PRO D 1 269 ? -4.849  9.442   92.466  1.00 22.38 ? 261  PRO D N   1 
ATOM   16275 C  CA  . PRO D 1 269 ? -6.135  8.761   92.649  1.00 20.09 ? 261  PRO D CA  1 
ATOM   16276 C  C   . PRO D 1 269 ? -7.064  9.027   91.477  1.00 22.50 ? 261  PRO D C   1 
ATOM   16277 O  O   . PRO D 1 269 ? -6.989  10.071  90.822  1.00 21.94 ? 261  PRO D O   1 
ATOM   16278 C  CB  . PRO D 1 269 ? -6.683  9.376   93.943  1.00 24.81 ? 261  PRO D CB  1 
ATOM   16279 C  CG  . PRO D 1 269 ? -5.463  9.816   94.690  1.00 26.22 ? 261  PRO D CG  1 
ATOM   16280 C  CD  . PRO D 1 269 ? -4.479  10.263  93.633  1.00 24.85 ? 261  PRO D CD  1 
ATOM   16281 N  N   . LEU D 1 270 ? -7.941  8.056   91.209  1.00 19.84 ? 262  LEU D N   1 
ATOM   16282 C  CA  . LEU D 1 270 ? -8.903  8.200   90.115  1.00 23.52 ? 262  LEU D CA  1 
ATOM   16283 C  C   . LEU D 1 270 ? -9.912  9.308   90.375  1.00 25.95 ? 262  LEU D C   1 
ATOM   16284 O  O   . LEU D 1 270 ? -10.405 9.934   89.425  1.00 27.62 ? 262  LEU D O   1 
ATOM   16285 C  CB  . LEU D 1 270 ? -9.649  6.887   89.890  1.00 21.57 ? 262  LEU D CB  1 
ATOM   16286 C  CG  . LEU D 1 270 ? -8.898  5.686   89.317  1.00 22.27 ? 262  LEU D CG  1 
ATOM   16287 C  CD1 . LEU D 1 270 ? -9.868  4.544   89.056  1.00 26.59 ? 262  LEU D CD1 1 
ATOM   16288 C  CD2 . LEU D 1 270 ? -8.195  6.076   88.036  1.00 20.68 ? 262  LEU D CD2 1 
ATOM   16289 N  N   . GLY D 1 271 ? -10.250 9.555   91.637  1.00 24.21 ? 263  GLY D N   1 
ATOM   16290 C  CA  . GLY D 1 271 ? -11.320 10.477  91.971  1.00 22.37 ? 263  GLY D CA  1 
ATOM   16291 C  C   . GLY D 1 271 ? -12.565 9.722   92.391  1.00 22.20 ? 263  GLY D C   1 
ATOM   16292 O  O   . GLY D 1 271 ? -12.857 8.671   91.818  1.00 21.61 ? 263  GLY D O   1 
ATOM   16293 N  N   . ALA D 1 272 ? -13.301 10.232  93.387  1.00 22.92 ? 264  ALA D N   1 
ATOM   16294 C  CA  . ALA D 1 272 ? -14.427 9.476   93.930  1.00 22.97 ? 264  ALA D CA  1 
ATOM   16295 C  C   . ALA D 1 272 ? -15.514 9.280   92.885  1.00 24.73 ? 264  ALA D C   1 
ATOM   16296 O  O   . ALA D 1 272 ? -16.079 8.188   92.765  1.00 23.95 ? 264  ALA D O   1 
ATOM   16297 C  CB  . ALA D 1 272 ? -15.003 10.178  95.159  1.00 24.46 ? 264  ALA D CB  1 
ATOM   16298 N  N   . ASP D 1 273 ? -15.838 10.332  92.132  1.00 24.80 ? 265  ASP D N   1 
ATOM   16299 C  CA  . ASP D 1 273 ? -16.896 10.204  91.137  1.00 25.75 ? 265  ASP D CA  1 
ATOM   16300 C  C   . ASP D 1 273 ? -16.511 9.198   90.062  1.00 24.94 ? 265  ASP D C   1 
ATOM   16301 O  O   . ASP D 1 273 ? -17.350 8.412   89.611  1.00 25.27 ? 265  ASP D O   1 
ATOM   16302 C  CB  . ASP D 1 273 ? -17.212 11.565  90.520  1.00 35.55 ? 265  ASP D CB  1 
ATOM   16303 C  CG  . ASP D 1 273 ? -18.005 12.460  91.461  1.00 37.11 ? 265  ASP D CG  1 
ATOM   16304 O  OD1 . ASP D 1 273 ? -18.233 12.063  92.627  1.00 36.23 ? 265  ASP D OD1 1 
ATOM   16305 O  OD2 . ASP D 1 273 ? -18.401 13.558  91.034  1.00 35.98 ? 265  ASP D OD2 1 
ATOM   16306 N  N   . GLU D 1 274 ? -15.244 9.204   89.649  1.00 24.11 ? 266  GLU D N   1 
ATOM   16307 C  CA  . GLU D 1 274 ? -14.793 8.279   88.614  1.00 23.57 ? 266  GLU D CA  1 
ATOM   16308 C  C   . GLU D 1 274 ? -14.827 6.833   89.095  1.00 23.70 ? 266  GLU D C   1 
ATOM   16309 O  O   . GLU D 1 274 ? -15.146 5.926   88.314  1.00 22.51 ? 266  GLU D O   1 
ATOM   16310 C  CB  . GLU D 1 274 ? -13.384 8.656   88.148  1.00 25.54 ? 266  GLU D CB  1 
ATOM   16311 C  CG  . GLU D 1 274 ? -12.785 7.685   87.142  1.00 22.97 ? 266  GLU D CG  1 
ATOM   16312 C  CD  . GLU D 1 274 ? -13.590 7.595   85.859  1.00 24.05 ? 266  GLU D CD  1 
ATOM   16313 O  OE1 . GLU D 1 274 ? -14.380 8.522   85.576  1.00 26.65 ? 266  GLU D OE1 1 
ATOM   16314 O  OE2 . GLU D 1 274 ? -13.432 6.596   85.125  1.00 23.91 ? 266  GLU D OE2 1 
ATOM   16315 N  N   . ILE D 1 275 ? -14.487 6.587   90.366  1.00 23.21 ? 267  ILE D N   1 
ATOM   16316 C  CA  . ILE D 1 275 ? -14.612 5.233   90.902  1.00 21.06 ? 267  ILE D CA  1 
ATOM   16317 C  C   . ILE D 1 275 ? -16.070 4.795   90.890  1.00 27.49 ? 267  ILE D C   1 
ATOM   16318 O  O   . ILE D 1 275 ? -16.392 3.657   90.515  1.00 21.52 ? 267  ILE D O   1 
ATOM   16319 C  CB  . ILE D 1 275 ? -14.007 5.149   92.315  1.00 19.96 ? 267  ILE D CB  1 
ATOM   16320 C  CG1 . ILE D 1 275 ? -12.485 5.278   92.243  1.00 22.60 ? 267  ILE D CG1 1 
ATOM   16321 C  CG2 . ILE D 1 275 ? -14.379 3.825   92.975  1.00 19.49 ? 267  ILE D CG2 1 
ATOM   16322 C  CD1 . ILE D 1 275 ? -11.812 5.443   93.604  1.00 21.21 ? 267  ILE D CD1 1 
ATOM   16323 N  N   . GLU D 1 276 ? -16.972 5.699   91.290  1.00 24.80 ? 268  GLU D N   1 
ATOM   16324 C  CA  . GLU D 1 276 ? -18.401 5.414   91.253  1.00 27.02 ? 268  GLU D CA  1 
ATOM   16325 C  C   . GLU D 1 276 ? -18.847 5.069   89.838  1.00 25.18 ? 268  GLU D C   1 
ATOM   16326 O  O   . GLU D 1 276 ? -19.538 4.067   89.619  1.00 26.66 ? 268  GLU D O   1 
ATOM   16327 C  CB  . GLU D 1 276 ? -19.174 6.616   91.799  1.00 25.38 ? 268  GLU D CB  1 
ATOM   16328 C  CG  . GLU D 1 276 ? -20.689 6.479   91.796  1.00 46.51 ? 268  GLU D CG  1 
ATOM   16329 C  CD  . GLU D 1 276 ? -21.383 7.780   92.195  1.00 55.36 ? 268  GLU D CD  1 
ATOM   16330 O  OE1 . GLU D 1 276 ? -21.277 8.780   91.448  1.00 56.91 ? 268  GLU D OE1 1 
ATOM   16331 O  OE2 . GLU D 1 276 ? -22.022 7.807   93.268  1.00 60.27 ? 268  GLU D OE2 1 
ATOM   16332 N  N   . ALA D 1 277 ? -18.435 5.877   88.856  1.00 25.10 ? 269  ALA D N   1 
ATOM   16333 C  CA  . ALA D 1 277 ? -18.760 5.577   87.464  1.00 26.00 ? 269  ALA D CA  1 
ATOM   16334 C  C   . ALA D 1 277 ? -18.129 4.270   87.015  1.00 25.04 ? 269  ALA D C   1 
ATOM   16335 O  O   . ALA D 1 277 ? -18.698 3.558   86.177  1.00 28.41 ? 269  ALA D O   1 
ATOM   16336 C  CB  . ALA D 1 277 ? -18.303 6.720   86.553  1.00 26.70 ? 269  ALA D CB  1 
ATOM   16337 N  N   . THR D 1 278 ? -16.957 3.939   87.560  1.00 23.46 ? 270  THR D N   1 
ATOM   16338 C  CA  . THR D 1 278 ? -16.262 2.724   87.149  1.00 22.67 ? 270  THR D CA  1 
ATOM   16339 C  C   . THR D 1 278 ? -16.951 1.482   87.704  1.00 24.16 ? 270  THR D C   1 
ATOM   16340 O  O   . THR D 1 278 ? -17.029 0.455   87.019  1.00 23.02 ? 270  THR D O   1 
ATOM   16341 C  CB  . THR D 1 278 ? -14.794 2.807   87.587  1.00 21.28 ? 270  THR D CB  1 
ATOM   16342 O  OG1 . THR D 1 278 ? -14.161 3.884   86.880  1.00 27.62 ? 270  THR D OG1 1 
ATOM   16343 C  CG2 . THR D 1 278 ? -14.043 1.504   87.309  1.00 22.68 ? 270  THR D CG2 1 
ATOM   16344 N  N   . ARG D 1 279 ? -17.485 1.564   88.928  1.00 22.70 ? 271  ARG D N   1 
ATOM   16345 C  CA  . ARG D 1 279 ? -18.313 0.476   89.451  1.00 22.84 ? 271  ARG D CA  1 
ATOM   16346 C  C   . ARG D 1 279 ? -19.503 0.194   88.538  1.00 26.52 ? 271  ARG D C   1 
ATOM   16347 O  O   . ARG D 1 279 ? -19.828 -0.968  88.267  1.00 27.31 ? 271  ARG D O   1 
ATOM   16348 C  CB  . ARG D 1 279 ? -18.802 0.811   90.862  1.00 27.77 ? 271  ARG D CB  1 
ATOM   16349 C  CG  . ARG D 1 279 ? -17.802 0.513   91.954  1.00 21.54 ? 271  ARG D CG  1 
ATOM   16350 C  CD  . ARG D 1 279 ? -18.374 0.677   93.374  1.00 25.64 ? 271  ARG D CD  1 
ATOM   16351 N  NE  . ARG D 1 279 ? -17.596 -0.123  94.320  1.00 25.71 ? 271  ARG D NE  1 
ATOM   16352 C  CZ  . ARG D 1 279 ? -16.388 0.218   94.768  1.00 26.25 ? 271  ARG D CZ  1 
ATOM   16353 N  NH1 . ARG D 1 279 ? -15.829 1.359   94.383  1.00 19.67 ? 271  ARG D NH1 1 
ATOM   16354 N  NH2 . ARG D 1 279 ? -15.737 -0.579  95.600  1.00 22.29 ? 271  ARG D NH2 1 
ATOM   16355 N  N   . LYS D 1 280 ? -20.174 1.248   88.065  1.00 25.77 ? 272  LYS D N   1 
ATOM   16356 C  CA  . LYS D 1 280 ? -21.307 1.059   87.163  1.00 27.68 ? 272  LYS D CA  1 
ATOM   16357 C  C   . LYS D 1 280 ? -20.859 0.504   85.814  1.00 32.67 ? 272  LYS D C   1 
ATOM   16358 O  O   . LYS D 1 280 ? -21.511 -0.386  85.250  1.00 30.90 ? 272  LYS D O   1 
ATOM   16359 C  CB  . LYS D 1 280 ? -22.049 2.381   86.972  1.00 29.84 ? 272  LYS D CB  1 
ATOM   16360 C  CG  . LYS D 1 280 ? -23.255 2.293   86.048  1.00 35.24 ? 272  LYS D CG  1 
ATOM   16361 C  CD  . LYS D 1 280 ? -23.892 3.665   85.833  1.00 38.51 ? 272  LYS D CD  1 
ATOM   16362 C  CE  . LYS D 1 280 ? -24.258 4.325   87.152  1.00 41.40 ? 272  LYS D CE  1 
ATOM   16363 N  NZ  . LYS D 1 280 ? -24.906 5.658   86.950  1.00 46.51 ? 272  LYS D NZ  1 
ATOM   16364 N  N   . HIS D 1 281 ? -19.758 1.032   85.278  1.00 29.88 ? 273  HIS D N   1 
ATOM   16365 C  CA  . HIS D 1 281 ? -19.282 0.598   83.971  1.00 29.41 ? 273  HIS D CA  1 
ATOM   16366 C  C   . HIS D 1 281 ? -18.938 -0.885  83.981  1.00 30.67 ? 273  HIS D C   1 
ATOM   16367 O  O   . HIS D 1 281 ? -19.293 -1.622  83.052  1.00 28.30 ? 273  HIS D O   1 
ATOM   16368 C  CB  . HIS D 1 281 ? -18.077 1.451   83.566  1.00 28.61 ? 273  HIS D CB  1 
ATOM   16369 C  CG  . HIS D 1 281 ? -17.427 1.030   82.284  1.00 37.40 ? 273  HIS D CG  1 
ATOM   16370 N  ND1 . HIS D 1 281 ? -18.100 0.999   81.082  1.00 40.21 ? 273  HIS D ND1 1 
ATOM   16371 C  CD2 . HIS D 1 281 ? -16.158 0.640   82.016  1.00 39.10 ? 273  HIS D CD2 1 
ATOM   16372 C  CE1 . HIS D 1 281 ? -17.277 0.596   80.130  1.00 44.03 ? 273  HIS D CE1 1 
ATOM   16373 N  NE2 . HIS D 1 281 ? -16.093 0.371   80.671  1.00 40.93 ? 273  HIS D NE2 1 
ATOM   16374 N  N   . LEU D 1 282 ? -18.272 -1.348  85.034  1.00 28.15 ? 274  LEU D N   1 
ATOM   16375 C  CA  . LEU D 1 282 ? -17.878 -2.744  85.142  1.00 29.05 ? 274  LEU D CA  1 
ATOM   16376 C  C   . LEU D 1 282 ? -18.906 -3.599  85.867  1.00 30.39 ? 274  LEU D C   1 
ATOM   16377 O  O   . LEU D 1 282 ? -18.657 -4.791  86.070  1.00 29.13 ? 274  LEU D O   1 
ATOM   16378 C  CB  . LEU D 1 282 ? -16.533 -2.852  85.860  1.00 25.75 ? 274  LEU D CB  1 
ATOM   16379 C  CG  . LEU D 1 282 ? -15.385 -2.046  85.238  1.00 25.94 ? 274  LEU D CG  1 
ATOM   16380 C  CD1 . LEU D 1 282 ? -14.086 -2.279  86.001  1.00 20.95 ? 274  LEU D CD1 1 
ATOM   16381 C  CD2 . LEU D 1 282 ? -15.233 -2.440  83.776  1.00 26.29 ? 274  LEU D CD2 1 
ATOM   16382 N  N   . GLY D 1 283 ? -20.032 -3.021  86.275  1.00 28.62 ? 275  GLY D N   1 
ATOM   16383 C  CA  . GLY D 1 283 ? -21.058 -3.772  86.986  1.00 31.49 ? 275  GLY D CA  1 
ATOM   16384 C  C   . GLY D 1 283 ? -20.569 -4.375  88.284  1.00 34.91 ? 275  GLY D C   1 
ATOM   16385 O  O   . GLY D 1 283 ? -20.890 -5.530  88.591  1.00 33.12 ? 275  GLY D O   1 
ATOM   16386 N  N   . TRP D 1 284 ? -19.777 -3.624  89.046  1.00 26.85 ? 276  TRP D N   1 
ATOM   16387 C  CA  . TRP D 1 284 ? -19.219 -4.092  90.310  1.00 30.18 ? 276  TRP D CA  1 
ATOM   16388 C  C   . TRP D 1 284 ? -20.124 -3.618  91.441  1.00 35.34 ? 276  TRP D C   1 
ATOM   16389 O  O   . TRP D 1 284 ? -20.135 -2.431  91.782  1.00 34.11 ? 276  TRP D O   1 
ATOM   16390 C  CB  . TRP D 1 284 ? -17.794 -3.577  90.496  1.00 27.49 ? 276  TRP D CB  1 
ATOM   16391 C  CG  . TRP D 1 284 ? -17.159 -4.018  91.778  1.00 27.77 ? 276  TRP D CG  1 
ATOM   16392 C  CD1 . TRP D 1 284 ? -17.044 -3.294  92.927  1.00 28.99 ? 276  TRP D CD1 1 
ATOM   16393 C  CD2 . TRP D 1 284 ? -16.545 -5.286  92.037  1.00 25.83 ? 276  TRP D CD2 1 
ATOM   16394 N  NE1 . TRP D 1 284 ? -16.402 -4.036  93.890  1.00 28.40 ? 276  TRP D NE1 1 
ATOM   16395 C  CE2 . TRP D 1 284 ? -16.086 -5.263  93.368  1.00 28.32 ? 276  TRP D CE2 1 
ATOM   16396 C  CE3 . TRP D 1 284 ? -16.349 -6.438  91.275  1.00 24.64 ? 276  TRP D CE3 1 
ATOM   16397 C  CZ2 . TRP D 1 284 ? -15.447 -6.353  93.958  1.00 22.30 ? 276  TRP D CZ2 1 
ATOM   16398 C  CZ3 . TRP D 1 284 ? -15.715 -7.515  91.856  1.00 25.34 ? 276  TRP D CZ3 1 
ATOM   16399 C  CH2 . TRP D 1 284 ? -15.269 -7.465  93.185  1.00 24.45 ? 276  TRP D CH2 1 
ATOM   16400 N  N   . ALA D 1 285 ? -20.869 -4.547  92.029  1.00 33.26 ? 277  ALA D N   1 
ATOM   16401 C  CA  . ALA D 1 285 ? -21.941 -4.206  92.952  1.00 31.76 ? 277  ALA D CA  1 
ATOM   16402 C  C   . ALA D 1 285 ? -21.477 -4.026  94.391  1.00 31.12 ? 277  ALA D C   1 
ATOM   16403 O  O   . ALA D 1 285 ? -22.317 -3.801  95.266  1.00 37.88 ? 277  ALA D O   1 
ATOM   16404 C  CB  . ALA D 1 285 ? -23.033 -5.285  92.900  1.00 32.69 ? 277  ALA D CB  1 
ATOM   16405 N  N   . TYR D 1 286 ? -20.169 -4.098  94.663  1.00 31.11 ? 278  TYR D N   1 
ATOM   16406 C  CA  . TYR D 1 286 ? -19.804 -4.179  96.067  1.00 24.18 ? 278  TYR D CA  1 
ATOM   16407 C  C   . TYR D 1 286 ? -19.100 -2.910  96.547  1.00 25.25 ? 278  TYR D C   1 
ATOM   16408 O  O   . TYR D 1 286 ? -18.275 -2.337  95.822  1.00 23.90 ? 278  TYR D O   1 
ATOM   16409 C  CB  . TYR D 1 286 ? -18.904 -5.395  96.305  1.00 28.24 ? 278  TYR D CB  1 
ATOM   16410 C  CG  . TYR D 1 286 ? -19.485 -6.658  95.704  1.00 32.92 ? 278  TYR D CG  1 
ATOM   16411 C  CD1 . TYR D 1 286 ? -20.598 -7.267  96.271  1.00 34.82 ? 278  TYR D CD1 1 
ATOM   16412 C  CD2 . TYR D 1 286 ? -18.934 -7.229  94.558  1.00 30.86 ? 278  TYR D CD2 1 
ATOM   16413 C  CE1 . TYR D 1 286 ? -21.146 -8.411  95.722  1.00 37.50 ? 278  TYR D CE1 1 
ATOM   16414 C  CE2 . TYR D 1 286 ? -19.476 -8.377  94.001  1.00 34.17 ? 278  TYR D CE2 1 
ATOM   16415 C  CZ  . TYR D 1 286 ? -20.580 -8.963  94.591  1.00 38.63 ? 278  TYR D CZ  1 
ATOM   16416 O  OH  . TYR D 1 286 ? -21.126 -10.106 94.047  1.00 44.03 ? 278  TYR D OH  1 
ATOM   16417 N  N   . PRO D 1 287 ? -19.409 -2.458  97.760  1.00 23.41 ? 279  PRO D N   1 
ATOM   16418 C  CA  . PRO D 1 287 ? -18.782 -1.243  98.292  1.00 23.89 ? 279  PRO D CA  1 
ATOM   16419 C  C   . PRO D 1 287 ? -17.304 -1.466  98.545  1.00 25.51 ? 279  PRO D C   1 
ATOM   16420 O  O   . PRO D 1 287 ? -16.804 -2.593  98.530  1.00 27.60 ? 279  PRO D O   1 
ATOM   16421 C  CB  . PRO D 1 287 ? -19.527 -0.993  99.610  1.00 26.05 ? 279  PRO D CB  1 
ATOM   16422 C  CG  . PRO D 1 287 ? -20.689 -1.909  99.602  1.00 32.03 ? 279  PRO D CG  1 
ATOM   16423 C  CD  . PRO D 1 287 ? -20.338 -3.064  98.725  1.00 32.03 ? 279  PRO D CD  1 
ATOM   16424 N  N   . ALA D 1 288 ? -16.607 -0.356  98.797  1.00 23.74 ? 280  ALA D N   1 
ATOM   16425 C  CA  . ALA D 1 288 ? -15.168 -0.394  99.011  1.00 23.51 ? 280  ALA D CA  1 
ATOM   16426 C  C   . ALA D 1 288 ? -14.804 -1.398  100.095 1.00 21.60 ? 280  ALA D C   1 
ATOM   16427 O  O   . ALA D 1 288 ? -15.412 -1.420  101.165 1.00 22.48 ? 280  ALA D O   1 
ATOM   16428 C  CB  . ALA D 1 288 ? -14.654 1.000   99.391  1.00 22.49 ? 280  ALA D CB  1 
ATOM   16429 N  N   . PHE D 1 289 ? -13.813 -2.239  99.797  1.00 18.78 ? 281  PHE D N   1 
ATOM   16430 C  CA  . PHE D 1 289 ? -13.217 -3.204  100.717 1.00 23.60 ? 281  PHE D CA  1 
ATOM   16431 C  C   . PHE D 1 289 ? -14.171 -4.328  101.107 1.00 25.37 ? 281  PHE D C   1 
ATOM   16432 O  O   . PHE D 1 289 ? -13.877 -5.092  102.039 1.00 28.40 ? 281  PHE D O   1 
ATOM   16433 C  CB  . PHE D 1 289 ? -12.666 -2.513  101.973 1.00 22.03 ? 281  PHE D CB  1 
ATOM   16434 C  CG  . PHE D 1 289 ? -11.652 -1.435  101.671 1.00 23.10 ? 281  PHE D CG  1 
ATOM   16435 C  CD1 . PHE D 1 289 ? -10.346 -1.762  101.344 1.00 24.04 ? 281  PHE D CD1 1 
ATOM   16436 C  CD2 . PHE D 1 289 ? -12.014 -0.094  101.697 1.00 21.13 ? 281  PHE D CD2 1 
ATOM   16437 C  CE1 . PHE D 1 289 ? -9.413  -0.766  101.052 1.00 22.68 ? 281  PHE D CE1 1 
ATOM   16438 C  CE2 . PHE D 1 289 ? -11.091 0.900   101.406 1.00 19.57 ? 281  PHE D CE2 1 
ATOM   16439 C  CZ  . PHE D 1 289 ? -9.788  0.554   101.083 1.00 23.67 ? 281  PHE D CZ  1 
ATOM   16440 N  N   . GLU D 1 290 ? -15.298 -4.464  100.420 1.00 21.48 ? 282  GLU D N   1 
ATOM   16441 C  CA  . GLU D 1 290 ? -16.219 -5.576  100.625 1.00 21.35 ? 282  GLU D CA  1 
ATOM   16442 C  C   . GLU D 1 290 ? -16.130 -6.498  99.417  1.00 30.21 ? 282  GLU D C   1 
ATOM   16443 O  O   . GLU D 1 290 ? -16.320 -6.060  98.278  1.00 27.91 ? 282  GLU D O   1 
ATOM   16444 C  CB  . GLU D 1 290 ? -17.647 -5.076  100.843 1.00 25.45 ? 282  GLU D CB  1 
ATOM   16445 C  CG  . GLU D 1 290 ? -17.815 -4.446  102.213 1.00 39.11 ? 282  GLU D CG  1 
ATOM   16446 C  CD  . GLU D 1 290 ? -19.191 -3.868  102.457 1.00 49.84 ? 282  GLU D CD  1 
ATOM   16447 O  OE1 . GLU D 1 290 ? -20.163 -4.333  101.821 1.00 52.78 ? 282  GLU D OE1 1 
ATOM   16448 O  OE2 . GLU D 1 290 ? -19.292 -2.943  103.293 1.00 49.61 ? 282  GLU D OE2 1 
ATOM   16449 N  N   . ILE D 1 291 ? -15.820 -7.767  99.668  1.00 29.76 ? 283  ILE D N   1 
ATOM   16450 C  CA  . ILE D 1 291 ? -15.601 -8.749  98.620  1.00 23.20 ? 283  ILE D CA  1 
ATOM   16451 C  C   . ILE D 1 291 ? -16.461 -9.969  98.930  1.00 26.00 ? 283  ILE D C   1 
ATOM   16452 O  O   . ILE D 1 291 ? -16.349 -10.535 100.020 1.00 26.93 ? 283  ILE D O   1 
ATOM   16453 C  CB  . ILE D 1 291 ? -14.123 -9.156  98.517  1.00 22.35 ? 283  ILE D CB  1 
ATOM   16454 C  CG1 . ILE D 1 291 ? -13.254 -7.929  98.222  1.00 19.47 ? 283  ILE D CG1 1 
ATOM   16455 C  CG2 . ILE D 1 291 ? -13.955 -10.235 97.468  1.00 25.74 ? 283  ILE D CG2 1 
ATOM   16456 C  CD1 . ILE D 1 291 ? -11.787 -8.173  98.446  1.00 17.46 ? 283  ILE D CD1 1 
ATOM   16457 N  N   . PRO D 1 292 ? -17.319 -10.419 98.014  1.00 27.20 ? 284  PRO D N   1 
ATOM   16458 C  CA  . PRO D 1 292 ? -18.176 -11.570 98.319  1.00 27.39 ? 284  PRO D CA  1 
ATOM   16459 C  C   . PRO D 1 292 ? -17.352 -12.831 98.533  1.00 28.66 ? 284  PRO D C   1 
ATOM   16460 O  O   . PRO D 1 292 ? -16.238 -12.968 98.020  1.00 27.97 ? 284  PRO D O   1 
ATOM   16461 C  CB  . PRO D 1 292 ? -19.068 -11.687 97.079  1.00 26.35 ? 284  PRO D CB  1 
ATOM   16462 C  CG  . PRO D 1 292 ? -18.237 -11.107 95.981  1.00 25.65 ? 284  PRO D CG  1 
ATOM   16463 C  CD  . PRO D 1 292 ? -17.482 -9.966  96.622  1.00 24.96 ? 284  PRO D CD  1 
ATOM   16464 N  N   . GLN D 1 293 ? -17.926 -13.767 99.296  1.00 29.39 ? 285  GLN D N   1 
ATOM   16465 C  CA  . GLN D 1 293 ? -17.182 -14.967 99.668  1.00 31.76 ? 285  GLN D CA  1 
ATOM   16466 C  C   . GLN D 1 293 ? -16.818 -15.822 98.459  1.00 25.81 ? 285  GLN D C   1 
ATOM   16467 O  O   . GLN D 1 293 ? -15.780 -16.493 98.467  1.00 27.33 ? 285  GLN D O   1 
ATOM   16468 C  CB  . GLN D 1 293 ? -17.983 -15.795 100.670 1.00 36.49 ? 285  GLN D CB  1 
ATOM   16469 C  CG  . GLN D 1 293 ? -17.194 -16.952 101.260 1.00 36.39 ? 285  GLN D CG  1 
ATOM   16470 C  CD  . GLN D 1 293 ? -16.012 -16.479 102.063 1.00 41.06 ? 285  GLN D CD  1 
ATOM   16471 O  OE1 . GLN D 1 293 ? -16.162 -15.678 102.978 1.00 46.12 ? 285  GLN D OE1 1 
ATOM   16472 N  NE2 . GLN D 1 293 ? -14.821 -16.960 101.718 1.00 40.72 ? 285  GLN D NE2 1 
ATOM   16473 N  N   . GLU D 1 294 ? -17.646 -15.817 97.412  1.00 26.46 ? 286  GLU D N   1 
ATOM   16474 C  CA  . GLU D 1 294 ? -17.329 -16.617 96.233  1.00 30.70 ? 286  GLU D CA  1 
ATOM   16475 C  C   . GLU D 1 294 ? -16.029 -16.166 95.577  1.00 28.82 ? 286  GLU D C   1 
ATOM   16476 O  O   . GLU D 1 294 ? -15.288 -16.998 95.035  1.00 27.56 ? 286  GLU D O   1 
ATOM   16477 C  CB  . GLU D 1 294 ? -18.474 -16.561 95.223  1.00 38.09 ? 286  GLU D CB  1 
ATOM   16478 C  CG  . GLU D 1 294 ? -19.101 -15.184 95.046  1.00 46.72 ? 286  GLU D CG  1 
ATOM   16479 C  CD  . GLU D 1 294 ? -20.291 -14.959 95.969  1.00 56.23 ? 286  GLU D CD  1 
ATOM   16480 O  OE1 . GLU D 1 294 ? -20.404 -15.680 96.984  1.00 58.27 ? 286  GLU D OE1 1 
ATOM   16481 O  OE2 . GLU D 1 294 ? -21.117 -14.068 95.669  1.00 59.49 ? 286  GLU D OE2 1 
ATOM   16482 N  N   . ILE D 1 295 ? -15.733 -14.864 95.608  1.00 30.82 ? 287  ILE D N   1 
ATOM   16483 C  CA  . ILE D 1 295 ? -14.497 -14.379 94.995  1.00 26.90 ? 287  ILE D CA  1 
ATOM   16484 C  C   . ILE D 1 295 ? -13.294 -14.745 95.859  1.00 21.23 ? 287  ILE D C   1 
ATOM   16485 O  O   . ILE D 1 295 ? -12.243 -15.152 95.345  1.00 20.77 ? 287  ILE D O   1 
ATOM   16486 C  CB  . ILE D 1 295 ? -14.591 -12.863 94.730  1.00 26.81 ? 287  ILE D CB  1 
ATOM   16487 C  CG1 . ILE D 1 295 ? -15.532 -12.593 93.547  1.00 30.74 ? 287  ILE D CG1 1 
ATOM   16488 C  CG2 . ILE D 1 295 ? -13.231 -12.266 94.444  1.00 24.56 ? 287  ILE D CG2 1 
ATOM   16489 C  CD1 . ILE D 1 295 ? -15.610 -11.120 93.158  1.00 32.89 ? 287  ILE D CD1 1 
ATOM   16490 N  N   . TYR D 1 296 ? -13.432 -14.631 97.183  1.00 21.42 ? 288  TYR D N   1 
ATOM   16491 C  CA  . TYR D 1 296 ? -12.390 -15.132 98.078  1.00 21.22 ? 288  TYR D CA  1 
ATOM   16492 C  C   . TYR D 1 296 ? -12.117 -16.613 97.840  1.00 24.21 ? 288  TYR D C   1 
ATOM   16493 O  O   . TYR D 1 296 ? -10.955 -17.041 97.796  1.00 26.03 ? 288  TYR D O   1 
ATOM   16494 C  CB  . TYR D 1 296 ? -12.795 -14.901 99.533  1.00 25.14 ? 288  TYR D CB  1 
ATOM   16495 C  CG  . TYR D 1 296 ? -12.451 -13.536 100.088 1.00 22.58 ? 288  TYR D CG  1 
ATOM   16496 C  CD1 . TYR D 1 296 ? -11.183 -12.989 99.920  1.00 19.83 ? 288  TYR D CD1 1 
ATOM   16497 C  CD2 . TYR D 1 296 ? -13.399 -12.796 100.791 1.00 25.63 ? 288  TYR D CD2 1 
ATOM   16498 C  CE1 . TYR D 1 296 ? -10.867 -11.740 100.436 1.00 19.63 ? 288  TYR D CE1 1 
ATOM   16499 C  CE2 . TYR D 1 296 ? -13.096 -11.554 101.307 1.00 23.45 ? 288  TYR D CE2 1 
ATOM   16500 C  CZ  . TYR D 1 296 ? -11.830 -11.030 101.130 1.00 21.58 ? 288  TYR D CZ  1 
ATOM   16501 O  OH  . TYR D 1 296 ? -11.529 -9.802  101.658 1.00 21.16 ? 288  TYR D OH  1 
ATOM   16502 N  N   . ASP D 1 297 ? -13.179 -17.413 97.696  1.00 29.02 ? 289  ASP D N   1 
ATOM   16503 C  CA  . ASP D 1 297 ? -13.004 -18.847 97.482  1.00 27.75 ? 289  ASP D CA  1 
ATOM   16504 C  C   . ASP D 1 297 ? -12.296 -19.121 96.166  1.00 25.89 ? 289  ASP D C   1 
ATOM   16505 O  O   . ASP D 1 297 ? -11.448 -20.017 96.082  1.00 28.52 ? 289  ASP D O   1 
ATOM   16506 C  CB  . ASP D 1 297 ? -14.358 -19.553 97.509  1.00 26.51 ? 289  ASP D CB  1 
ATOM   16507 C  CG  . ASP D 1 297 ? -14.960 -19.605 98.898  1.00 34.52 ? 289  ASP D CG  1 
ATOM   16508 O  OD1 . ASP D 1 297 ? -14.240 -19.290 99.868  1.00 34.33 ? 289  ASP D OD1 1 
ATOM   16509 O  OD2 . ASP D 1 297 ? -16.152 -19.954 99.018  1.00 34.45 ? 289  ASP D OD2 1 
ATOM   16510 N  N   . ALA D 1 298 ? -12.638 -18.364 95.122  1.00 27.15 ? 290  ALA D N   1 
ATOM   16511 C  CA  . ALA D 1 298 ? -11.983 -18.547 93.834  1.00 25.29 ? 290  ALA D CA  1 
ATOM   16512 C  C   . ALA D 1 298 ? -10.509 -18.175 93.895  1.00 23.87 ? 290  ALA D C   1 
ATOM   16513 O  O   . ALA D 1 298 ? -9.695  -18.764 93.178  1.00 27.87 ? 290  ALA D O   1 
ATOM   16514 C  CB  . ALA D 1 298 ? -12.690 -17.723 92.765  1.00 29.95 ? 290  ALA D CB  1 
ATOM   16515 N  N   . TRP D 1 299 ? -10.146 -17.215 94.744  1.00 23.62 ? 291  TRP D N   1 
ATOM   16516 C  CA  . TRP D 1 299 ? -8.780  -16.705 94.793  1.00 25.28 ? 291  TRP D CA  1 
ATOM   16517 C  C   . TRP D 1 299 ? -7.911  -17.403 95.830  1.00 27.88 ? 291  TRP D C   1 
ATOM   16518 O  O   . TRP D 1 299 ? -6.678  -17.367 95.710  1.00 23.13 ? 291  TRP D O   1 
ATOM   16519 C  CB  . TRP D 1 299 ? -8.790  -15.203 95.097  1.00 19.97 ? 291  TRP D CB  1 
ATOM   16520 C  CG  . TRP D 1 299 ? -8.669  -14.306 93.908  1.00 18.50 ? 291  TRP D CG  1 
ATOM   16521 C  CD1 . TRP D 1 299 ? -9.638  -13.511 93.375  1.00 24.36 ? 291  TRP D CD1 1 
ATOM   16522 C  CD2 . TRP D 1 299 ? -7.496  -14.093 93.119  1.00 20.87 ? 291  TRP D CD2 1 
ATOM   16523 N  NE1 . TRP D 1 299 ? -9.140  -12.818 92.294  1.00 21.73 ? 291  TRP D NE1 1 
ATOM   16524 C  CE2 . TRP D 1 299 ? -7.827  -13.161 92.117  1.00 22.54 ? 291  TRP D CE2 1 
ATOM   16525 C  CE3 . TRP D 1 299 ? -6.198  -14.610 93.157  1.00 21.48 ? 291  TRP D CE3 1 
ATOM   16526 C  CZ2 . TRP D 1 299 ? -6.902  -12.726 91.163  1.00 20.28 ? 291  TRP D CZ2 1 
ATOM   16527 C  CZ3 . TRP D 1 299 ? -5.280  -14.171 92.209  1.00 22.67 ? 291  TRP D CZ3 1 
ATOM   16528 C  CH2 . TRP D 1 299 ? -5.639  -13.243 91.228  1.00 21.55 ? 291  TRP D CH2 1 
ATOM   16529 N  N   . ASN D 1 300 ? -8.519  -18.045 96.829  1.00 23.45 ? 292  ASN D N   1 
ATOM   16530 C  CA  . ASN D 1 300 ? -7.769  -18.517 97.987  1.00 21.67 ? 292  ASN D CA  1 
ATOM   16531 C  C   . ASN D 1 300 ? -6.801  -19.626 97.593  1.00 22.38 ? 292  ASN D C   1 
ATOM   16532 O  O   . ASN D 1 300 ? -7.180  -20.588 96.918  1.00 23.35 ? 292  ASN D O   1 
ATOM   16533 C  CB  . ASN D 1 300 ? -8.721  -19.025 99.073  1.00 23.84 ? 292  ASN D CB  1 
ATOM   16534 C  CG  . ASN D 1 300 ? -8.012  -19.243 100.389 1.00 30.64 ? 292  ASN D CG  1 
ATOM   16535 O  OD1 . ASN D 1 300 ? -7.366  -20.264 100.585 1.00 30.30 ? 292  ASN D OD1 1 
ATOM   16536 N  ND2 . ASN D 1 300 ? -8.090  -18.262 101.284 1.00 33.35 ? 292  ASN D ND2 1 
ATOM   16537 N  N   . ALA D 1 301 ? -5.551  -19.502 98.039  1.00 22.14 ? 293  ALA D N   1 
ATOM   16538 C  CA  . ALA D 1 301 ? -4.507  -20.459 97.703  1.00 22.96 ? 293  ALA D CA  1 
ATOM   16539 C  C   . ALA D 1 301 ? -4.080  -21.321 98.888  1.00 25.81 ? 293  ALA D C   1 
ATOM   16540 O  O   . ALA D 1 301 ? -3.047  -21.997 98.805  1.00 24.84 ? 293  ALA D O   1 
ATOM   16541 C  CB  . ALA D 1 301 ? -3.288  -19.726 97.125  1.00 22.22 ? 293  ALA D CB  1 
ATOM   16542 N  N   . LYS D 1 302 ? -4.843  -21.332 99.984  1.00 23.58 ? 294  LYS D N   1 
ATOM   16543 C  CA  . LYS D 1 302 ? -4.404  -22.082 101.161 1.00 27.82 ? 294  LYS D CA  1 
ATOM   16544 C  C   . LYS D 1 302 ? -4.357  -23.585 100.890 1.00 24.22 ? 294  LYS D C   1 
ATOM   16545 O  O   . LYS D 1 302 ? -3.381  -24.256 101.248 1.00 24.63 ? 294  LYS D O   1 
ATOM   16546 C  CB  . LYS D 1 302 ? -5.306  -21.779 102.361 1.00 32.59 ? 294  LYS D CB  1 
ATOM   16547 C  CG  . LYS D 1 302 ? -5.144  -20.361 102.894 1.00 42.26 ? 294  LYS D CG  1 
ATOM   16548 C  CD  . LYS D 1 302 ? -4.747  -20.329 104.362 1.00 49.95 ? 294  LYS D CD  1 
ATOM   16549 C  CE  . LYS D 1 302 ? -4.596  -18.891 104.858 1.00 48.69 ? 294  LYS D CE  1 
ATOM   16550 N  NZ  . LYS D 1 302 ? -5.795  -18.052 104.545 1.00 50.84 ? 294  LYS D NZ  1 
ATOM   16551 N  N   . GLU D 1 303 ? -5.398  -24.137 100.263 1.00 23.43 ? 295  GLU D N   1 
ATOM   16552 C  CA  . GLU D 1 303 ? -5.436  -25.583 100.065 1.00 24.40 ? 295  GLU D CA  1 
ATOM   16553 C  C   . GLU D 1 303 ? -4.408  -26.023 99.034  1.00 24.17 ? 295  GLU D C   1 
ATOM   16554 O  O   . GLU D 1 303 ? -3.702  -27.016 99.236  1.00 24.71 ? 295  GLU D O   1 
ATOM   16555 C  CB  . GLU D 1 303 ? -6.837  -26.037 99.647  1.00 25.15 ? 295  GLU D CB  1 
ATOM   16556 C  CG  . GLU D 1 303 ? -6.889  -27.515 99.289  1.00 26.18 ? 295  GLU D CG  1 
ATOM   16557 C  CD  . GLU D 1 303 ? -8.311  -28.055 99.109  1.00 27.09 ? 295  GLU D CD  1 
ATOM   16558 O  OE1 . GLU D 1 303 ? -9.269  -27.266 99.033  1.00 29.16 ? 295  GLU D OE1 1 
ATOM   16559 O  OE2 . GLU D 1 303 ? -8.447  -29.282 99.053  1.00 28.08 ? 295  GLU D OE2 1 
ATOM   16560 N  N   . LYS D 1 304 ? -4.300  -25.285 97.929  1.00 24.57 ? 296  LYS D N   1 
ATOM   16561 C  CA  . LYS D 1 304 ? -3.323  -25.626 96.904  1.00 23.24 ? 296  LYS D CA  1 
ATOM   16562 C  C   . LYS D 1 304 ? -1.905  -25.454 97.434  1.00 22.75 ? 296  LYS D C   1 
ATOM   16563 O  O   . LYS D 1 304 ? -1.027  -26.277 97.152  1.00 23.06 ? 296  LYS D O   1 
ATOM   16564 C  CB  . LYS D 1 304 ? -3.565  -24.764 95.663  1.00 33.78 ? 296  LYS D CB  1 
ATOM   16565 C  CG  . LYS D 1 304 ? -2.647  -25.055 94.484  1.00 39.21 ? 296  LYS D CG  1 
ATOM   16566 C  CD  . LYS D 1 304 ? -3.011  -24.191 93.282  1.00 39.52 ? 296  LYS D CD  1 
ATOM   16567 C  CE  . LYS D 1 304 ? -2.021  -24.373 92.138  1.00 41.70 ? 296  LYS D CE  1 
ATOM   16568 N  NZ  . LYS D 1 304 ? -2.363  -23.523 90.961  1.00 44.51 ? 296  LYS D NZ  1 
ATOM   16569 N  N   . GLY D 1 305 ? -1.676  -24.400 98.222  1.00 22.30 ? 297  GLY D N   1 
ATOM   16570 C  CA  . GLY D 1 305 ? -0.356  -24.176 98.787  1.00 23.91 ? 297  GLY D CA  1 
ATOM   16571 C  C   . GLY D 1 305 ? 0.021   -25.204 99.837  1.00 22.85 ? 297  GLY D C   1 
ATOM   16572 O  O   . GLY D 1 305 ? 1.185   -25.601 99.938  1.00 24.99 ? 297  GLY D O   1 
ATOM   16573 N  N   . ALA D 1 306 ? -0.952  -25.643 100.643 1.00 23.17 ? 298  ALA D N   1 
ATOM   16574 C  CA  . ALA D 1 306 ? -0.674  -26.704 101.608 1.00 24.10 ? 298  ALA D CA  1 
ATOM   16575 C  C   . ALA D 1 306 ? -0.325  -28.007 100.903 1.00 28.08 ? 298  ALA D C   1 
ATOM   16576 O  O   . ALA D 1 306 ? 0.591   -28.724 101.322 1.00 25.30 ? 298  ALA D O   1 
ATOM   16577 C  CB  . ALA D 1 306 ? -1.869  -26.905 102.540 1.00 27.33 ? 298  ALA D CB  1 
ATOM   16578 N  N   . LYS D 1 307 ? -1.050  -28.336 99.831  1.00 28.16 ? 299  LYS D N   1 
ATOM   16579 C  CA  . LYS D 1 307 ? -0.749  -29.556 99.090  1.00 28.69 ? 299  LYS D CA  1 
ATOM   16580 C  C   . LYS D 1 307 ? 0.622   -29.477 98.432  1.00 25.33 ? 299  LYS D C   1 
ATOM   16581 O  O   . LYS D 1 307 ? 1.345   -30.478 98.371  1.00 26.03 ? 299  LYS D O   1 
ATOM   16582 C  CB  . LYS D 1 307 ? -1.829  -29.808 98.043  1.00 33.13 ? 299  LYS D CB  1 
ATOM   16583 C  CG  . LYS D 1 307 ? -3.164  -30.228 98.620  1.00 42.42 ? 299  LYS D CG  1 
ATOM   16584 C  CD  . LYS D 1 307 ? -4.247  -30.233 97.552  1.00 45.31 ? 299  LYS D CD  1 
ATOM   16585 C  CE  . LYS D 1 307 ? -3.784  -30.945 96.300  1.00 39.75 ? 299  LYS D CE  1 
ATOM   16586 N  NZ  . LYS D 1 307 ? -4.880  -30.997 95.305  1.00 39.30 ? 299  LYS D NZ  1 
ATOM   16587 N  N   . LEU D 1 308 ? 0.979   -28.299 97.913  1.00 24.21 ? 300  LEU D N   1 
ATOM   16588 C  CA  . LEU D 1 308 ? 2.293   -28.101 97.311  1.00 26.05 ? 300  LEU D CA  1 
ATOM   16589 C  C   . LEU D 1 308 ? 3.401   -28.359 98.321  1.00 23.82 ? 300  LEU D C   1 
ATOM   16590 O  O   . LEU D 1 308 ? 4.358   -29.094 98.043  1.00 24.21 ? 300  LEU D O   1 
ATOM   16591 C  CB  . LEU D 1 308 ? 2.403   -26.677 96.753  1.00 22.49 ? 300  LEU D CB  1 
ATOM   16592 C  CG  . LEU D 1 308 ? 3.733   -26.281 96.101  1.00 25.91 ? 300  LEU D CG  1 
ATOM   16593 C  CD1 . LEU D 1 308 ? 3.867   -26.888 94.700  1.00 25.27 ? 300  LEU D CD1 1 
ATOM   16594 C  CD2 . LEU D 1 308 ? 3.887   -24.769 96.054  1.00 25.55 ? 300  LEU D CD2 1 
ATOM   16595 N  N   . GLU D 1 309 ? 3.293   -27.760 99.506  1.00 23.57 ? 301  GLU D N   1 
ATOM   16596 C  CA  . GLU D 1 309 ? 4.367   -27.922 100.475 1.00 23.71 ? 301  GLU D CA  1 
ATOM   16597 C  C   . GLU D 1 309 ? 4.382   -29.330 101.055 1.00 25.00 ? 301  GLU D C   1 
ATOM   16598 O  O   . GLU D 1 309 ? 5.451   -29.846 101.398 1.00 25.36 ? 301  GLU D O   1 
ATOM   16599 C  CB  . GLU D 1 309 ? 4.258   -26.866 101.580 1.00 27.84 ? 301  GLU D CB  1 
ATOM   16600 C  CG  . GLU D 1 309 ? 5.390   -26.966 102.601 1.00 27.66 ? 301  GLU D CG  1 
ATOM   16601 C  CD  . GLU D 1 309 ? 5.573   -25.705 103.417 1.00 30.52 ? 301  GLU D CD  1 
ATOM   16602 O  OE1 . GLU D 1 309 ? 4.935   -24.685 103.089 1.00 26.83 ? 301  GLU D OE1 1 
ATOM   16603 O  OE2 . GLU D 1 309 ? 6.359   -25.734 104.389 1.00 29.18 ? 301  GLU D OE2 1 
ATOM   16604 N  N   . ALA D 1 310 ? 3.218   -29.981 101.149 1.00 25.77 ? 302  ALA D N   1 
ATOM   16605 C  CA  . ALA D 1 310 ? 3.206   -31.366 101.601 1.00 29.86 ? 302  ALA D CA  1 
ATOM   16606 C  C   . ALA D 1 310 ? 3.909   -32.274 100.600 1.00 34.68 ? 302  ALA D C   1 
ATOM   16607 O  O   . ALA D 1 310 ? 4.708   -33.134 100.987 1.00 28.32 ? 302  ALA D O   1 
ATOM   16608 C  CB  . ALA D 1 310 ? 1.772   -31.830 101.840 1.00 27.83 ? 302  ALA D CB  1 
ATOM   16609 N  N   . GLY D 1 311 ? 3.635   -32.091 99.309  1.00 27.15 ? 303  GLY D N   1 
ATOM   16610 C  CA  . GLY D 1 311 ? 4.296   -32.913 98.311  1.00 32.17 ? 303  GLY D CA  1 
ATOM   16611 C  C   . GLY D 1 311 ? 5.796   -32.715 98.318  1.00 30.66 ? 303  GLY D C   1 
ATOM   16612 O  O   . GLY D 1 311 ? 6.562   -33.670 98.162  1.00 28.01 ? 303  GLY D O   1 
ATOM   16613 N  N   . TRP D 1 312 ? 6.237   -31.471 98.518  1.00 32.37 ? 304  TRP D N   1 
ATOM   16614 C  CA  . TRP D 1 312 ? 7.667   -31.202 98.577  1.00 29.97 ? 304  TRP D CA  1 
ATOM   16615 C  C   . TRP D 1 312 ? 8.284   -31.811 99.827  1.00 26.42 ? 304  TRP D C   1 
ATOM   16616 O  O   . TRP D 1 312 ? 9.382   -32.374 99.770  1.00 29.73 ? 304  TRP D O   1 
ATOM   16617 C  CB  . TRP D 1 312 ? 7.933   -29.695 98.524  1.00 24.32 ? 304  TRP D CB  1 
ATOM   16618 C  CG  . TRP D 1 312 ? 9.392   -29.402 98.420  1.00 23.92 ? 304  TRP D CG  1 
ATOM   16619 C  CD1 . TRP D 1 312 ? 10.117  -29.243 97.275  1.00 23.56 ? 304  TRP D CD1 1 
ATOM   16620 C  CD2 . TRP D 1 312 ? 10.317  -29.281 99.504  1.00 23.96 ? 304  TRP D CD2 1 
ATOM   16621 N  NE1 . TRP D 1 312 ? 11.440  -29.014 97.582  1.00 23.34 ? 304  TRP D NE1 1 
ATOM   16622 C  CE2 . TRP D 1 312 ? 11.586  -29.032 98.944  1.00 23.57 ? 304  TRP D CE2 1 
ATOM   16623 C  CE3 . TRP D 1 312 ? 10.195  -29.352 100.892 1.00 24.33 ? 304  TRP D CE3 1 
ATOM   16624 C  CZ2 . TRP D 1 312 ? 12.720  -28.853 99.726  1.00 31.96 ? 304  TRP D CZ2 1 
ATOM   16625 C  CZ3 . TRP D 1 312 ? 11.318  -29.172 101.667 1.00 27.66 ? 304  TRP D CZ3 1 
ATOM   16626 C  CH2 . TRP D 1 312 ? 12.567  -28.928 101.084 1.00 32.59 ? 304  TRP D CH2 1 
ATOM   16627 N  N   . ASN D 1 313 ? 7.590   -31.716 100.964 1.00 26.65 ? 305  ASN D N   1 
ATOM   16628 C  CA  . ASN D 1 313 ? 8.105   -32.327 102.185 1.00 27.49 ? 305  ASN D CA  1 
ATOM   16629 C  C   . ASN D 1 313 ? 8.295   -33.826 102.005 1.00 31.68 ? 305  ASN D C   1 
ATOM   16630 O  O   . ASN D 1 313 ? 9.273   -34.397 102.499 1.00 29.50 ? 305  ASN D O   1 
ATOM   16631 C  CB  . ASN D 1 313 ? 7.172   -32.032 103.363 1.00 29.84 ? 305  ASN D CB  1 
ATOM   16632 C  CG  . ASN D 1 313 ? 7.353   -30.632 103.916 1.00 31.69 ? 305  ASN D CG  1 
ATOM   16633 O  OD1 . ASN D 1 313 ? 8.378   -30.001 103.698 1.00 35.77 ? 305  ASN D OD1 1 
ATOM   16634 N  ND2 . ASN D 1 313 ? 6.363   -30.147 104.646 1.00 31.03 ? 305  ASN D ND2 1 
ATOM   16635 N  N   . GLU D 1 314 ? 7.387   -34.478 101.273 1.00 29.37 ? 306  GLU D N   1 
ATOM   16636 C  CA  . GLU D 1 314 ? 7.536   -35.909 101.032 1.00 34.37 ? 306  GLU D CA  1 
ATOM   16637 C  C   . GLU D 1 314 ? 8.738   -36.193 100.142 1.00 34.68 ? 306  GLU D C   1 
ATOM   16638 O  O   . GLU D 1 314 ? 9.498   -37.133 100.400 1.00 35.96 ? 306  GLU D O   1 
ATOM   16639 C  CB  . GLU D 1 314 ? 6.264   -36.482 100.410 1.00 34.23 ? 306  GLU D CB  1 
ATOM   16640 C  CG  . GLU D 1 314 ? 6.307   -37.990 100.226 1.00 44.34 ? 306  GLU D CG  1 
ATOM   16641 C  CD  . GLU D 1 314 ? 5.033   -38.541 99.615  1.00 53.09 ? 306  GLU D CD  1 
ATOM   16642 O  OE1 . GLU D 1 314 ? 4.217   -37.736 99.122  1.00 54.67 ? 306  GLU D OE1 1 
ATOM   16643 O  OE2 . GLU D 1 314 ? 4.849   -39.778 99.627  1.00 55.41 ? 306  GLU D OE2 1 
ATOM   16644 N  N   . LEU D 1 315 ? 8.917   -35.400 99.084  1.00 35.58 ? 307  LEU D N   1 
ATOM   16645 C  CA  . LEU D 1 315 ? 10.101  -35.542 98.243  1.00 34.48 ? 307  LEU D CA  1 
ATOM   16646 C  C   . LEU D 1 315 ? 11.369  -35.303 99.048  1.00 33.25 ? 307  LEU D C   1 
ATOM   16647 O  O   . LEU D 1 315 ? 12.345  -36.057 98.931  1.00 36.76 ? 307  LEU D O   1 
ATOM   16648 C  CB  . LEU D 1 315 ? 10.022  -34.571 97.064  1.00 32.87 ? 307  LEU D CB  1 
ATOM   16649 C  CG  . LEU D 1 315 ? 11.111  -34.672 95.993  1.00 28.37 ? 307  LEU D CG  1 
ATOM   16650 C  CD1 . LEU D 1 315 ? 10.853  -35.868 95.090  1.00 29.49 ? 307  LEU D CD1 1 
ATOM   16651 C  CD2 . LEU D 1 315 ? 11.183  -33.379 95.185  1.00 27.59 ? 307  LEU D CD2 1 
ATOM   16652 N  N   . PHE D 1 316 ? 11.371  -34.260 99.882  1.00 28.61 ? 308  PHE D N   1 
ATOM   16653 C  CA  . PHE D 1 316 ? 12.548  -33.969 100.692 1.00 28.50 ? 308  PHE D CA  1 
ATOM   16654 C  C   . PHE D 1 316 ? 12.791  -35.051 101.736 1.00 29.86 ? 308  PHE D C   1 
ATOM   16655 O  O   . PHE D 1 316 ? 13.934  -35.258 102.162 1.00 36.28 ? 308  PHE D O   1 
ATOM   16656 C  CB  . PHE D 1 316 ? 12.399  -32.594 101.351 1.00 29.91 ? 308  PHE D CB  1 
ATOM   16657 C  CG  . PHE D 1 316 ? 13.647  -32.110 102.020 1.00 30.47 ? 308  PHE D CG  1 
ATOM   16658 C  CD1 . PHE D 1 316 ? 14.754  -31.766 101.270 1.00 31.18 ? 308  PHE D CD1 1 
ATOM   16659 C  CD2 . PHE D 1 316 ? 13.721  -32.008 103.400 1.00 37.70 ? 308  PHE D CD2 1 
ATOM   16660 C  CE1 . PHE D 1 316 ? 15.912  -31.332 101.881 1.00 29.94 ? 308  PHE D CE1 1 
ATOM   16661 C  CE2 . PHE D 1 316 ? 14.877  -31.565 104.016 1.00 33.06 ? 308  PHE D CE2 1 
ATOM   16662 C  CZ  . PHE D 1 316 ? 15.970  -31.227 103.256 1.00 29.71 ? 308  PHE D CZ  1 
ATOM   16663 N  N   . ALA D 1 317 ? 11.737  -35.752 102.157 1.00 32.65 ? 309  ALA D N   1 
ATOM   16664 C  CA  . ALA D 1 317 ? 11.917  -36.879 103.066 1.00 34.78 ? 309  ALA D CA  1 
ATOM   16665 C  C   . ALA D 1 317 ? 12.665  -38.023 102.388 1.00 35.38 ? 309  ALA D C   1 
ATOM   16666 O  O   . ALA D 1 317 ? 13.560  -38.630 102.987 1.00 38.11 ? 309  ALA D O   1 
ATOM   16667 C  CB  . ALA D 1 317 ? 10.559  -37.355 103.585 1.00 37.19 ? 309  ALA D CB  1 
ATOM   16668 N  N   . GLN D 1 318 ? 12.299  -38.346 101.145 1.00 33.19 ? 310  GLN D N   1 
ATOM   16669 C  CA  . GLN D 1 318 ? 13.058  -39.339 100.392 1.00 34.12 ? 310  GLN D CA  1 
ATOM   16670 C  C   . GLN D 1 318 ? 14.497  -38.884 100.195 1.00 33.62 ? 310  GLN D C   1 
ATOM   16671 O  O   . GLN D 1 318 ? 15.435  -39.686 100.292 1.00 34.61 ? 310  GLN D O   1 
ATOM   16672 C  CB  . GLN D 1 318 ? 12.399  -39.587 99.038  1.00 37.92 ? 310  GLN D CB  1 
ATOM   16673 C  CG  . GLN D 1 318 ? 10.955  -40.025 99.113  1.00 43.45 ? 310  GLN D CG  1 
ATOM   16674 C  CD  . GLN D 1 318 ? 10.307  -40.051 97.747  1.00 53.12 ? 310  GLN D CD  1 
ATOM   16675 O  OE1 . GLN D 1 318 ? 9.444   -39.228 97.439  1.00 58.10 ? 310  GLN D OE1 1 
ATOM   16676 N  NE2 . GLN D 1 318 ? 10.727  -40.994 96.913  1.00 54.88 ? 310  GLN D NE2 1 
ATOM   16677 N  N   . TYR D 1 319 ? 14.683  -37.595 99.912  1.00 32.13 ? 311  TYR D N   1 
ATOM   16678 C  CA  . TYR D 1 319 ? 16.022  -37.042 99.761  1.00 33.53 ? 311  TYR D CA  1 
ATOM   16679 C  C   . TYR D 1 319 ? 16.827  -37.183 101.045 1.00 32.12 ? 311  TYR D C   1 
ATOM   16680 O  O   . TYR D 1 319 ? 18.003  -37.569 101.007 1.00 42.70 ? 311  TYR D O   1 
ATOM   16681 C  CB  . TYR D 1 319 ? 15.918  -35.576 99.339  1.00 29.93 ? 311  TYR D CB  1 
ATOM   16682 C  CG  . TYR D 1 319 ? 17.225  -34.940 98.929  1.00 29.28 ? 311  TYR D CG  1 
ATOM   16683 C  CD1 . TYR D 1 319 ? 18.065  -34.373 99.871  1.00 30.67 ? 311  TYR D CD1 1 
ATOM   16684 C  CD2 . TYR D 1 319 ? 17.604  -34.881 97.594  1.00 30.51 ? 311  TYR D CD2 1 
ATOM   16685 C  CE1 . TYR D 1 319 ? 19.267  -33.774 99.500  1.00 28.41 ? 311  TYR D CE1 1 
ATOM   16686 C  CE2 . TYR D 1 319 ? 18.802  -34.283 97.214  1.00 31.25 ? 311  TYR D CE2 1 
ATOM   16687 C  CZ  . TYR D 1 319 ? 19.628  -33.737 98.173  1.00 28.16 ? 311  TYR D CZ  1 
ATOM   16688 O  OH  . TYR D 1 319 ? 20.819  -33.134 97.811  1.00 28.78 ? 311  TYR D OH  1 
ATOM   16689 N  N   . GLN D 1 320 ? 16.215  -36.880 102.196 1.00 32.06 ? 312  GLN D N   1 
ATOM   16690 C  CA  . GLN D 1 320 ? 16.944  -36.962 103.461 1.00 38.23 ? 312  GLN D CA  1 
ATOM   16691 C  C   . GLN D 1 320 ? 17.343  -38.399 103.772 1.00 39.19 ? 312  GLN D C   1 
ATOM   16692 O  O   . GLN D 1 320 ? 18.464  -38.656 104.231 1.00 36.55 ? 312  GLN D O   1 
ATOM   16693 C  CB  . GLN D 1 320 ? 16.100  -36.382 104.599 1.00 38.47 ? 312  GLN D CB  1 
ATOM   16694 C  CG  . GLN D 1 320 ? 16.895  -35.741 105.745 1.00 41.91 ? 312  GLN D CG  1 
ATOM   16695 C  CD  . GLN D 1 320 ? 17.290  -36.706 106.860 1.00 52.46 ? 312  GLN D CD  1 
ATOM   16696 O  OE1 . GLN D 1 320 ? 17.942  -37.724 106.630 1.00 48.42 ? 312  GLN D OE1 1 
ATOM   16697 N  NE2 . GLN D 1 320 ? 16.902  -36.371 108.087 1.00 60.46 ? 312  GLN D NE2 1 
ATOM   16698 N  N   . ALA D 1 321 ? 16.441  -39.349 103.523 1.00 41.50 ? 313  ALA D N   1 
ATOM   16699 C  CA  . ALA D 1 321 ? 16.750  -40.749 103.784 1.00 41.47 ? 313  ALA D CA  1 
ATOM   16700 C  C   . ALA D 1 321 ? 17.988  -41.191 103.016 1.00 42.59 ? 313  ALA D C   1 
ATOM   16701 O  O   . ALA D 1 321 ? 18.831  -41.926 103.545 1.00 44.31 ? 313  ALA D O   1 
ATOM   16702 C  CB  . ALA D 1 321 ? 15.549  -41.620 103.420 1.00 38.22 ? 313  ALA D CB  1 
ATOM   16703 N  N   . LYS D 1 322 ? 18.126  -40.735 101.776 1.00 38.27 ? 314  LYS D N   1 
ATOM   16704 C  CA  . LYS D 1 322 ? 19.221  -41.160 100.917 1.00 39.65 ? 314  LYS D CA  1 
ATOM   16705 C  C   . LYS D 1 322 ? 20.459  -40.288 101.084 1.00 37.45 ? 314  LYS D C   1 
ATOM   16706 O  O   . LYS D 1 322 ? 21.586  -40.794 101.040 1.00 39.78 ? 314  LYS D O   1 
ATOM   16707 C  CB  . LYS D 1 322 ? 18.759  -41.146 99.459  1.00 41.43 ? 314  LYS D CB  1 
ATOM   16708 C  CG  . LYS D 1 322 ? 19.516  -42.085 98.549  1.00 48.55 ? 314  LYS D CG  1 
ATOM   16709 C  CD  . LYS D 1 322 ? 18.854  -42.164 97.184  1.00 52.50 ? 314  LYS D CD  1 
ATOM   16710 C  CE  . LYS D 1 322 ? 19.510  -43.238 96.346  1.00 57.22 ? 314  LYS D CE  1 
ATOM   16711 N  NZ  . LYS D 1 322 ? 20.986  -43.233 96.545  1.00 59.97 ? 314  LYS D NZ  1 
ATOM   16712 N  N   . TYR D 1 323 ? 20.267  -38.988 101.290 1.00 34.62 ? 315  TYR D N   1 
ATOM   16713 C  CA  . TYR D 1 323 ? 21.350  -38.006 101.336 1.00 35.98 ? 315  TYR D CA  1 
ATOM   16714 C  C   . TYR D 1 323 ? 21.219  -37.167 102.602 1.00 38.85 ? 315  TYR D C   1 
ATOM   16715 O  O   . TYR D 1 323 ? 20.889  -35.976 102.541 1.00 42.19 ? 315  TYR D O   1 
ATOM   16716 C  CB  . TYR D 1 323 ? 21.321  -37.120 100.090 1.00 32.38 ? 315  TYR D CB  1 
ATOM   16717 C  CG  . TYR D 1 323 ? 21.318  -37.889 98.791  1.00 35.02 ? 315  TYR D CG  1 
ATOM   16718 C  CD1 . TYR D 1 323 ? 22.486  -38.465 98.300  1.00 34.87 ? 315  TYR D CD1 1 
ATOM   16719 C  CD2 . TYR D 1 323 ? 20.155  -38.041 98.053  1.00 38.53 ? 315  TYR D CD2 1 
ATOM   16720 C  CE1 . TYR D 1 323 ? 22.492  -39.168 97.109  1.00 39.20 ? 315  TYR D CE1 1 
ATOM   16721 C  CE2 . TYR D 1 323 ? 20.150  -38.747 96.858  1.00 38.68 ? 315  TYR D CE2 1 
ATOM   16722 C  CZ  . TYR D 1 323 ? 21.323  -39.308 96.393  1.00 40.03 ? 315  TYR D CZ  1 
ATOM   16723 O  OH  . TYR D 1 323 ? 21.326  -40.009 95.208  1.00 42.12 ? 315  TYR D OH  1 
ATOM   16724 N  N   . PRO D 1 324 ? 21.476  -37.761 103.773 1.00 35.05 ? 316  PRO D N   1 
ATOM   16725 C  CA  . PRO D 1 324 ? 21.204  -37.036 105.028 1.00 34.83 ? 316  PRO D CA  1 
ATOM   16726 C  C   . PRO D 1 324 ? 22.096  -35.828 105.256 1.00 38.07 ? 316  PRO D C   1 
ATOM   16727 O  O   . PRO D 1 324 ? 21.628  -34.816 105.792 1.00 39.17 ? 316  PRO D O   1 
ATOM   16728 C  CB  . PRO D 1 324 ? 21.421  -38.112 106.102 1.00 35.47 ? 316  PRO D CB  1 
ATOM   16729 C  CG  . PRO D 1 324 ? 22.316  -39.116 105.456 1.00 36.53 ? 316  PRO D CG  1 
ATOM   16730 C  CD  . PRO D 1 324 ? 21.911  -39.146 104.019 1.00 37.56 ? 316  PRO D CD  1 
ATOM   16731 N  N   . ALA D 1 325 ? 23.375  -35.901 104.884 1.00 38.13 ? 317  ALA D N   1 
ATOM   16732 C  CA  . ALA D 1 325 ? 24.273  -34.776 105.126 1.00 35.31 ? 317  ALA D CA  1 
ATOM   16733 C  C   . ALA D 1 325 ? 23.942  -33.604 104.212 1.00 30.32 ? 317  ALA D C   1 
ATOM   16734 O  O   . ALA D 1 325 ? 23.901  -32.449 104.654 1.00 29.29 ? 317  ALA D O   1 
ATOM   16735 C  CB  . ALA D 1 325 ? 25.726  -35.214 104.942 1.00 36.48 ? 317  ALA D CB  1 
ATOM   16736 N  N   . GLU D 1 326 ? 23.703  -33.880 102.927 1.00 32.07 ? 318  GLU D N   1 
ATOM   16737 C  CA  . GLU D 1 326 ? 23.329  -32.811 102.005 1.00 30.39 ? 318  GLU D CA  1 
ATOM   16738 C  C   . GLU D 1 326 ? 21.974  -32.224 102.359 1.00 27.97 ? 318  GLU D C   1 
ATOM   16739 O  O   . GLU D 1 326 ? 21.733  -31.035 102.128 1.00 26.71 ? 318  GLU D O   1 
ATOM   16740 C  CB  . GLU D 1 326 ? 23.303  -33.317 100.565 1.00 31.77 ? 318  GLU D CB  1 
ATOM   16741 C  CG  . GLU D 1 326 ? 24.542  -34.054 100.121 1.00 41.20 ? 318  GLU D CG  1 
ATOM   16742 C  CD  . GLU D 1 326 ? 24.432  -35.545 100.356 1.00 46.86 ? 318  GLU D CD  1 
ATOM   16743 O  OE1 . GLU D 1 326 ? 24.149  -35.957 101.503 1.00 45.31 ? 318  GLU D OE1 1 
ATOM   16744 O  OE2 . GLU D 1 326 ? 24.609  -36.305 99.383  1.00 52.94 ? 318  GLU D OE2 1 
ATOM   16745 N  N   . ALA D 1 327 ? 21.072  -33.045 102.902 1.00 28.81 ? 319  ALA D N   1 
ATOM   16746 C  CA  . ALA D 1 327 ? 19.763  -32.542 103.295 1.00 30.35 ? 319  ALA D CA  1 
ATOM   16747 C  C   . ALA D 1 327 ? 19.884  -31.558 104.449 1.00 31.22 ? 319  ALA D C   1 
ATOM   16748 O  O   . ALA D 1 327 ? 19.299  -30.470 104.415 1.00 31.95 ? 319  ALA D O   1 
ATOM   16749 C  CB  . ALA D 1 327 ? 18.850  -33.707 103.666 1.00 29.44 ? 319  ALA D CB  1 
ATOM   16750 N  N   . ALA D 1 328 ? 20.650  -31.924 105.480 1.00 28.53 ? 320  ALA D N   1 
ATOM   16751 C  CA  . ALA D 1 328 ? 20.853  -31.018 106.604 1.00 32.11 ? 320  ALA D CA  1 
ATOM   16752 C  C   . ALA D 1 328 ? 21.553  -29.740 106.161 1.00 26.83 ? 320  ALA D C   1 
ATOM   16753 O  O   . ALA D 1 328 ? 21.255  -28.654 106.667 1.00 28.52 ? 320  ALA D O   1 
ATOM   16754 C  CB  . ALA D 1 328 ? 21.662  -31.713 107.698 1.00 33.02 ? 320  ALA D CB  1 
ATOM   16755 N  N   . GLU D 1 329 ? 22.511  -29.857 105.240 1.00 31.88 ? 321  GLU D N   1 
ATOM   16756 C  CA  . GLU D 1 329 ? 23.159  -28.672 104.686 1.00 27.40 ? 321  GLU D CA  1 
ATOM   16757 C  C   . GLU D 1 329 ? 22.164  -27.802 103.928 1.00 24.36 ? 321  GLU D C   1 
ATOM   16758 O  O   . GLU D 1 329 ? 22.209  -26.568 104.016 1.00 23.33 ? 321  GLU D O   1 
ATOM   16759 C  CB  . GLU D 1 329 ? 24.310  -29.092 103.772 1.00 31.04 ? 321  GLU D CB  1 
ATOM   16760 C  CG  . GLU D 1 329 ? 25.609  -29.308 104.509 1.00 29.09 ? 321  GLU D CG  1 
ATOM   16761 C  CD  . GLU D 1 329 ? 26.097  -28.023 105.140 1.00 32.63 ? 321  GLU D CD  1 
ATOM   16762 O  OE1 . GLU D 1 329 ? 26.670  -27.189 104.409 1.00 35.61 ? 321  GLU D OE1 1 
ATOM   16763 O  OE2 . GLU D 1 329 ? 25.871  -27.830 106.356 1.00 27.96 ? 321  GLU D OE2 1 
ATOM   16764 N  N   . PHE D 1 330 ? 21.272  -28.428 103.156 1.00 27.03 ? 322  PHE D N   1 
ATOM   16765 C  CA  . PHE D 1 330 ? 20.278  -27.657 102.416 1.00 27.12 ? 322  PHE D CA  1 
ATOM   16766 C  C   . PHE D 1 330 ? 19.371  -26.889 103.366 1.00 23.06 ? 322  PHE D C   1 
ATOM   16767 O  O   . PHE D 1 330 ? 19.049  -25.723 103.122 1.00 22.89 ? 322  PHE D O   1 
ATOM   16768 C  CB  . PHE D 1 330 ? 19.457  -28.581 101.513 1.00 27.47 ? 322  PHE D CB  1 
ATOM   16769 C  CG  . PHE D 1 330 ? 18.425  -27.862 100.684 1.00 29.12 ? 322  PHE D CG  1 
ATOM   16770 C  CD1 . PHE D 1 330 ? 18.774  -27.274 99.484  1.00 25.95 ? 322  PHE D CD1 1 
ATOM   16771 C  CD2 . PHE D 1 330 ? 17.107  -27.780 101.108 1.00 23.02 ? 322  PHE D CD2 1 
ATOM   16772 C  CE1 . PHE D 1 330 ? 17.832  -26.605 98.721  1.00 32.63 ? 322  PHE D CE1 1 
ATOM   16773 C  CE2 . PHE D 1 330 ? 16.166  -27.132 100.353 1.00 22.87 ? 322  PHE D CE2 1 
ATOM   16774 C  CZ  . PHE D 1 330 ? 16.522  -26.536 99.153  1.00 25.54 ? 322  PHE D CZ  1 
ATOM   16775 N  N   . VAL D 1 331 ? 18.956  -27.526 104.462 1.00 26.89 ? 323  VAL D N   1 
ATOM   16776 C  CA  . VAL D 1 331 ? 18.106  -26.854 105.445 1.00 30.34 ? 323  VAL D CA  1 
ATOM   16777 C  C   . VAL D 1 331 ? 18.855  -25.695 106.095 1.00 26.44 ? 323  VAL D C   1 
ATOM   16778 O  O   . VAL D 1 331 ? 18.344  -24.571 106.178 1.00 22.61 ? 323  VAL D O   1 
ATOM   16779 C  CB  . VAL D 1 331 ? 17.596  -27.867 106.489 1.00 32.12 ? 323  VAL D CB  1 
ATOM   16780 C  CG1 . VAL D 1 331 ? 16.921  -27.156 107.651 1.00 27.46 ? 323  VAL D CG1 1 
ATOM   16781 C  CG2 . VAL D 1 331 ? 16.638  -28.844 105.834 1.00 29.26 ? 323  VAL D CG2 1 
ATOM   16782 N  N   . ARG D 1 332 ? 20.087  -25.943 106.552 1.00 29.38 ? 324  ARG D N   1 
ATOM   16783 C  CA  . ARG D 1 332 ? 20.865  -24.879 107.185 1.00 25.68 ? 324  ARG D CA  1 
ATOM   16784 C  C   . ARG D 1 332 ? 21.044  -23.688 106.248 1.00 23.34 ? 324  ARG D C   1 
ATOM   16785 O  O   . ARG D 1 332 ? 20.886  -22.528 106.658 1.00 24.44 ? 324  ARG D O   1 
ATOM   16786 C  CB  . ARG D 1 332 ? 22.224  -25.420 107.630 1.00 26.55 ? 324  ARG D CB  1 
ATOM   16787 C  CG  . ARG D 1 332 ? 23.180  -24.335 108.138 1.00 25.11 ? 324  ARG D CG  1 
ATOM   16788 C  CD  . ARG D 1 332 ? 24.567  -24.898 108.407 1.00 27.08 ? 324  ARG D CD  1 
ATOM   16789 N  NE  . ARG D 1 332 ? 25.331  -25.141 107.182 1.00 29.95 ? 324  ARG D NE  1 
ATOM   16790 C  CZ  . ARG D 1 332 ? 25.915  -24.187 106.456 1.00 26.47 ? 324  ARG D CZ  1 
ATOM   16791 N  NH1 . ARG D 1 332 ? 25.807  -22.910 106.802 1.00 23.93 ? 324  ARG D NH1 1 
ATOM   16792 N  NH2 . ARG D 1 332 ? 26.593  -24.507 105.361 1.00 26.39 ? 324  ARG D NH2 1 
ATOM   16793 N  N   . ARG D 1 333 ? 21.341  -23.952 104.975 1.00 24.78 ? 325  ARG D N   1 
ATOM   16794 C  CA  . ARG D 1 333 ? 21.642  -22.860 104.056 1.00 20.29 ? 325  ARG D CA  1 
ATOM   16795 C  C   . ARG D 1 333 ? 20.380  -22.109 103.631 1.00 19.47 ? 325  ARG D C   1 
ATOM   16796 O  O   . ARG D 1 333 ? 20.397  -20.876 103.527 1.00 21.72 ? 325  ARG D O   1 
ATOM   16797 C  CB  . ARG D 1 333 ? 22.419  -23.403 102.850 1.00 20.46 ? 325  ARG D CB  1 
ATOM   16798 C  CG  . ARG D 1 333 ? 23.849  -23.871 103.214 1.00 21.11 ? 325  ARG D CG  1 
ATOM   16799 C  CD  . ARG D 1 333 ? 24.523  -24.645 102.084 1.00 26.01 ? 325  ARG D CD  1 
ATOM   16800 N  NE  . ARG D 1 333 ? 24.446  -23.941 100.808 1.00 22.66 ? 325  ARG D NE  1 
ATOM   16801 C  CZ  . ARG D 1 333 ? 25.031  -24.354 99.688  1.00 22.90 ? 325  ARG D CZ  1 
ATOM   16802 N  NH1 . ARG D 1 333 ? 25.741  -25.474 99.687  1.00 22.82 ? 325  ARG D NH1 1 
ATOM   16803 N  NH2 . ARG D 1 333 ? 24.899  -23.650 98.569  1.00 20.01 ? 325  ARG D NH2 1 
ATOM   16804 N  N   . MET D 1 334 ? 19.276  -22.822 103.400 1.00 19.83 ? 326  MET D N   1 
ATOM   16805 C  CA  . MET D 1 334 ? 18.032  -22.134 103.052 1.00 19.15 ? 326  MET D CA  1 
ATOM   16806 C  C   . MET D 1 334 ? 17.497  -21.324 104.226 1.00 22.12 ? 326  MET D C   1 
ATOM   16807 O  O   . MET D 1 334 ? 16.868  -20.279 104.023 1.00 20.19 ? 326  MET D O   1 
ATOM   16808 C  CB  . MET D 1 334 ? 16.980  -23.143 102.575 1.00 19.70 ? 326  MET D CB  1 
ATOM   16809 C  CG  . MET D 1 334 ? 17.265  -23.758 101.212 1.00 19.82 ? 326  MET D CG  1 
ATOM   16810 S  SD  . MET D 1 334 ? 17.359  -22.534 99.904  1.00 21.99 ? 326  MET D SD  1 
ATOM   16811 C  CE  . MET D 1 334 ? 15.812  -21.629 100.101 1.00 22.60 ? 326  MET D CE  1 
ATOM   16812 N  N   . ASP D 1 335 ? 17.755  -21.772 105.452 1.00 21.30 ? 327  ASP D N   1 
ATOM   16813 C  CA  . ASP D 1 335 ? 17.417  -21.016 106.655 1.00 26.37 ? 327  ASP D CA  1 
ATOM   16814 C  C   . ASP D 1 335 ? 18.379  -19.869 106.934 1.00 27.42 ? 327  ASP D C   1 
ATOM   16815 O  O   . ASP D 1 335 ? 18.187  -19.157 107.927 1.00 31.59 ? 327  ASP D O   1 
ATOM   16816 C  CB  . ASP D 1 335 ? 17.379  -21.941 107.869 1.00 23.84 ? 327  ASP D CB  1 
ATOM   16817 C  CG  . ASP D 1 335 ? 16.153  -22.807 107.885 1.00 30.57 ? 327  ASP D CG  1 
ATOM   16818 O  OD1 . ASP D 1 335 ? 15.221  -22.519 107.103 1.00 25.51 ? 327  ASP D OD1 1 
ATOM   16819 O  OD2 . ASP D 1 335 ? 16.129  -23.780 108.664 1.00 31.87 ? 327  ASP D OD2 1 
ATOM   16820 N  N   . LYS D 1 336 ? 19.403  -19.682 106.098 1.00 25.52 ? 328  LYS D N   1 
ATOM   16821 C  CA  . LYS D 1 336 ? 20.348  -18.571 106.229 1.00 26.46 ? 328  LYS D CA  1 
ATOM   16822 C  C   . LYS D 1 336 ? 21.097  -18.627 107.565 1.00 27.91 ? 328  LYS D C   1 
ATOM   16823 O  O   . LYS D 1 336 ? 21.344  -17.604 108.205 1.00 33.90 ? 328  LYS D O   1 
ATOM   16824 C  CB  . LYS D 1 336 ? 19.633  -17.227 106.034 1.00 26.80 ? 328  LYS D CB  1 
ATOM   16825 C  CG  . LYS D 1 336 ? 18.821  -17.164 104.732 1.00 34.29 ? 328  LYS D CG  1 
ATOM   16826 C  CD  . LYS D 1 336 ? 17.934  -15.912 104.616 1.00 33.27 ? 328  LYS D CD  1 
ATOM   16827 C  CE  . LYS D 1 336 ? 17.137  -15.908 103.300 1.00 35.74 ? 328  LYS D CE  1 
ATOM   16828 N  NZ  . LYS D 1 336 ? 16.187  -14.740 103.140 1.00 30.23 ? 328  LYS D NZ  1 
ATOM   16829 N  N   . LYS D 1 337 ? 21.477  -19.837 107.978 1.00 26.15 ? 329  LYS D N   1 
ATOM   16830 C  CA  . LYS D 1 337 ? 22.239  -20.068 109.197 1.00 26.45 ? 329  LYS D CA  1 
ATOM   16831 C  C   . LYS D 1 337 ? 23.682  -20.432 108.867 1.00 30.94 ? 329  LYS D C   1 
ATOM   16832 O  O   . LYS D 1 337 ? 23.960  -21.094 107.861 1.00 28.83 ? 329  LYS D O   1 
ATOM   16833 C  CB  . LYS D 1 337 ? 21.621  -21.195 110.032 1.00 29.88 ? 329  LYS D CB  1 
ATOM   16834 C  CG  . LYS D 1 337 ? 20.209  -20.921 110.513 1.00 33.83 ? 329  LYS D CG  1 
ATOM   16835 C  CD  . LYS D 1 337 ? 19.592  -22.191 111.104 1.00 39.23 ? 329  LYS D CD  1 
ATOM   16836 C  CE  . LYS D 1 337 ? 18.159  -21.957 111.564 1.00 39.90 ? 329  LYS D CE  1 
ATOM   16837 N  NZ  . LYS D 1 337 ? 17.481  -23.245 111.890 1.00 40.08 ? 329  LYS D NZ  1 
ATOM   16838 N  N   . LEU D 1 338 ? 24.596  -20.005 109.740 1.00 34.99 ? 330  LEU D N   1 
ATOM   16839 C  CA  . LEU D 1 338 ? 25.999  -20.372 109.643 1.00 34.34 ? 330  LEU D CA  1 
ATOM   16840 C  C   . LEU D 1 338 ? 26.241  -21.726 110.301 1.00 33.81 ? 330  LEU D C   1 
ATOM   16841 O  O   . LEU D 1 338 ? 25.444  -22.173 111.135 1.00 30.72 ? 330  LEU D O   1 
ATOM   16842 C  CB  . LEU D 1 338 ? 26.868  -19.312 110.314 1.00 34.68 ? 330  LEU D CB  1 
ATOM   16843 C  CG  . LEU D 1 338 ? 26.881  -17.926 109.683 1.00 34.30 ? 330  LEU D CG  1 
ATOM   16844 C  CD1 . LEU D 1 338 ? 27.791  -17.017 110.471 1.00 36.33 ? 330  LEU D CD1 1 
ATOM   16845 C  CD2 . LEU D 1 338 ? 27.317  -17.997 108.235 1.00 38.72 ? 330  LEU D CD2 1 
ATOM   16846 N  N   . PRO D 1 339 ? 27.336  -22.407 109.941 1.00 29.32 ? 331  PRO D N   1 
ATOM   16847 C  CA  . PRO D 1 339 ? 27.683  -23.652 110.637 1.00 33.58 ? 331  PRO D CA  1 
ATOM   16848 C  C   . PRO D 1 339 ? 27.844  -23.408 112.127 1.00 34.06 ? 331  PRO D C   1 
ATOM   16849 O  O   . PRO D 1 339 ? 28.265  -22.334 112.558 1.00 32.38 ? 331  PRO D O   1 
ATOM   16850 C  CB  . PRO D 1 339 ? 29.010  -24.069 109.990 1.00 31.61 ? 331  PRO D CB  1 
ATOM   16851 C  CG  . PRO D 1 339 ? 28.996  -23.412 108.650 1.00 30.60 ? 331  PRO D CG  1 
ATOM   16852 C  CD  . PRO D 1 339 ? 28.274  -22.109 108.846 1.00 29.38 ? 331  PRO D CD  1 
ATOM   16853 N  N   . GLU D 1 340 ? 27.493  -24.429 112.914 1.00 38.80 ? 332  GLU D N   1 
ATOM   16854 C  CA  . GLU D 1 340 ? 27.504  -24.297 114.367 1.00 40.55 ? 332  GLU D CA  1 
ATOM   16855 C  C   . GLU D 1 340 ? 28.899  -24.037 114.925 1.00 39.51 ? 332  GLU D C   1 
ATOM   16856 O  O   . GLU D 1 340 ? 29.020  -23.456 116.010 1.00 46.49 ? 332  GLU D O   1 
ATOM   16857 C  CB  . GLU D 1 340 ? 26.913  -25.554 115.008 1.00 41.81 ? 332  GLU D CB  1 
ATOM   16858 N  N   . ASN D 1 341 ? 29.950  -24.439 114.213 1.00 33.98 ? 333  ASN D N   1 
ATOM   16859 C  CA  . ASN D 1 341 ? 31.317  -24.295 114.696 1.00 38.99 ? 333  ASN D CA  1 
ATOM   16860 C  C   . ASN D 1 341 ? 32.022  -23.069 114.120 1.00 36.35 ? 333  ASN D C   1 
ATOM   16861 O  O   . ASN D 1 341 ? 33.259  -23.017 114.128 1.00 27.73 ? 333  ASN D O   1 
ATOM   16862 C  CB  . ASN D 1 341 ? 32.116  -25.557 114.373 1.00 44.53 ? 333  ASN D CB  1 
ATOM   16863 C  CG  . ASN D 1 341 ? 32.319  -25.747 112.882 1.00 50.56 ? 333  ASN D CG  1 
ATOM   16864 O  OD1 . ASN D 1 341 ? 31.505  -25.298 112.076 1.00 50.04 ? 333  ASN D OD1 1 
ATOM   16865 N  ND2 . ASN D 1 341 ? 33.414  -26.404 112.508 1.00 51.79 ? 333  ASN D ND2 1 
ATOM   16866 N  N   . PHE D 1 342 ? 31.266  -22.075 113.645 1.00 33.70 ? 334  PHE D N   1 
ATOM   16867 C  CA  . PHE D 1 342 ? 31.858  -21.000 112.852 1.00 30.25 ? 334  PHE D CA  1 
ATOM   16868 C  C   . PHE D 1 342 ? 32.803  -20.142 113.682 1.00 33.72 ? 334  PHE D C   1 
ATOM   16869 O  O   . PHE D 1 342 ? 33.943  -19.888 113.275 1.00 30.33 ? 334  PHE D O   1 
ATOM   16870 C  CB  . PHE D 1 342 ? 30.762  -20.131 112.235 1.00 30.51 ? 334  PHE D CB  1 
ATOM   16871 C  CG  . PHE D 1 342 ? 31.283  -19.041 111.338 1.00 27.31 ? 334  PHE D CG  1 
ATOM   16872 C  CD1 . PHE D 1 342 ? 31.666  -19.320 110.037 1.00 28.28 ? 334  PHE D CD1 1 
ATOM   16873 C  CD2 . PHE D 1 342 ? 31.365  -17.734 111.786 1.00 26.55 ? 334  PHE D CD2 1 
ATOM   16874 C  CE1 . PHE D 1 342 ? 32.140  -18.313 109.201 1.00 28.44 ? 334  PHE D CE1 1 
ATOM   16875 C  CE2 . PHE D 1 342 ? 31.833  -16.725 110.955 1.00 21.20 ? 334  PHE D CE2 1 
ATOM   16876 C  CZ  . PHE D 1 342 ? 32.217  -17.015 109.661 1.00 24.48 ? 334  PHE D CZ  1 
ATOM   16877 N  N   . ASP D 1 343 ? 32.341  -19.659 114.837 1.00 34.37 ? 335  ASP D N   1 
ATOM   16878 C  CA  . ASP D 1 343 ? 33.196  -18.806 115.654 1.00 35.10 ? 335  ASP D CA  1 
ATOM   16879 C  C   . ASP D 1 343 ? 34.465  -19.542 116.071 1.00 34.09 ? 335  ASP D C   1 
ATOM   16880 O  O   . ASP D 1 343 ? 35.557  -18.962 116.060 1.00 29.65 ? 335  ASP D O   1 
ATOM   16881 C  CB  . ASP D 1 343 ? 32.420  -18.297 116.871 1.00 38.48 ? 335  ASP D CB  1 
ATOM   16882 C  CG  . ASP D 1 343 ? 31.344  -17.282 116.495 1.00 38.91 ? 335  ASP D CG  1 
ATOM   16883 O  OD1 . ASP D 1 343 ? 31.541  -16.540 115.514 1.00 38.79 ? 335  ASP D OD1 1 
ATOM   16884 O  OD2 . ASP D 1 343 ? 30.301  -17.223 117.179 1.00 43.03 ? 335  ASP D OD2 1 
ATOM   16885 N  N   . GLU D 1 344 ? 34.346  -20.832 116.406 1.00 35.72 ? 336  GLU D N   1 
ATOM   16886 C  CA  . GLU D 1 344 ? 35.523  -21.615 116.785 1.00 29.10 ? 336  GLU D CA  1 
ATOM   16887 C  C   . GLU D 1 344 ? 36.474  -21.796 115.607 1.00 33.20 ? 336  GLU D C   1 
ATOM   16888 O  O   . GLU D 1 344 ? 37.697  -21.700 115.767 1.00 33.75 ? 336  GLU D O   1 
ATOM   16889 C  CB  . GLU D 1 344 ? 35.096  -22.974 117.342 1.00 32.64 ? 336  GLU D CB  1 
ATOM   16890 N  N   . TYR D 1 345 ? 35.930  -22.065 114.418 1.00 33.03 ? 337  TYR D N   1 
ATOM   16891 C  CA  . TYR D 1 345 ? 36.756  -22.144 113.217 1.00 37.41 ? 337  TYR D CA  1 
ATOM   16892 C  C   . TYR D 1 345 ? 37.500  -20.833 112.977 1.00 34.79 ? 337  TYR D C   1 
ATOM   16893 O  O   . TYR D 1 345 ? 38.706  -20.834 112.697 1.00 29.93 ? 337  TYR D O   1 
ATOM   16894 C  CB  . TYR D 1 345 ? 35.886  -22.503 112.004 1.00 26.99 ? 337  TYR D CB  1 
ATOM   16895 C  CG  . TYR D 1 345 ? 36.640  -22.488 110.695 1.00 28.53 ? 337  TYR D CG  1 
ATOM   16896 C  CD1 . TYR D 1 345 ? 37.340  -23.608 110.263 1.00 27.55 ? 337  TYR D CD1 1 
ATOM   16897 C  CD2 . TYR D 1 345 ? 36.658  -21.350 109.890 1.00 28.71 ? 337  TYR D CD2 1 
ATOM   16898 C  CE1 . TYR D 1 345 ? 38.038  -23.600 109.070 1.00 35.89 ? 337  TYR D CE1 1 
ATOM   16899 C  CE2 . TYR D 1 345 ? 37.359  -21.331 108.695 1.00 30.79 ? 337  TYR D CE2 1 
ATOM   16900 C  CZ  . TYR D 1 345 ? 38.046  -22.460 108.289 1.00 32.76 ? 337  TYR D CZ  1 
ATOM   16901 O  OH  . TYR D 1 345 ? 38.738  -22.451 107.098 1.00 30.75 ? 337  TYR D OH  1 
ATOM   16902 N  N   . VAL D 1 346 ? 36.789  -19.702 113.077 1.00 30.20 ? 338  VAL D N   1 
ATOM   16903 C  CA  . VAL D 1 346 ? 37.408  -18.399 112.838 1.00 31.09 ? 338  VAL D CA  1 
ATOM   16904 C  C   . VAL D 1 346 ? 38.482  -18.110 113.881 1.00 30.56 ? 338  VAL D C   1 
ATOM   16905 O  O   . VAL D 1 346 ? 39.564  -17.611 113.552 1.00 30.62 ? 338  VAL D O   1 
ATOM   16906 C  CB  . VAL D 1 346 ? 36.333  -17.296 112.809 1.00 28.66 ? 338  VAL D CB  1 
ATOM   16907 C  CG1 . VAL D 1 346 ? 36.980  -15.907 112.720 1.00 25.57 ? 338  VAL D CG1 1 
ATOM   16908 C  CG2 . VAL D 1 346 ? 35.386  -17.527 111.647 1.00 22.87 ? 338  VAL D CG2 1 
ATOM   16909 N  N   . GLN D 1 347 ? 38.208  -18.424 115.150 1.00 29.59 ? 339  GLN D N   1 
ATOM   16910 C  CA  . GLN D 1 347 ? 39.181  -18.140 116.202 1.00 35.93 ? 339  GLN D CA  1 
ATOM   16911 C  C   . GLN D 1 347 ? 40.458  -18.953 116.008 1.00 40.25 ? 339  GLN D C   1 
ATOM   16912 O  O   . GLN D 1 347 ? 41.569  -18.436 116.181 1.00 39.81 ? 339  GLN D O   1 
ATOM   16913 C  CB  . GLN D 1 347 ? 38.562  -18.414 117.572 1.00 36.48 ? 339  GLN D CB  1 
ATOM   16914 N  N   . THR D 1 348 ? 40.316  -20.227 115.639 1.00 39.08 ? 340  THR D N   1 
ATOM   16915 C  CA  . THR D 1 348 ? 41.482  -21.051 115.343 1.00 34.56 ? 340  THR D CA  1 
ATOM   16916 C  C   . THR D 1 348 ? 42.231  -20.513 114.131 1.00 36.26 ? 340  THR D C   1 
ATOM   16917 O  O   . THR D 1 348 ? 43.459  -20.384 114.154 1.00 32.47 ? 340  THR D O   1 
ATOM   16918 C  CB  . THR D 1 348 ? 41.047  -22.499 115.115 1.00 34.68 ? 340  THR D CB  1 
ATOM   16919 O  OG1 . THR D 1 348 ? 40.477  -23.020 116.321 1.00 32.37 ? 340  THR D OG1 1 
ATOM   16920 C  CG2 . THR D 1 348 ? 42.227  -23.362 114.700 1.00 35.82 ? 340  THR D CG2 1 
ATOM   16921 N  N   . ALA D 1 349 ? 41.496  -20.181 113.063 1.00 29.80 ? 341  ALA D N   1 
ATOM   16922 C  CA  . ALA D 1 349 ? 42.116  -19.624 111.863 1.00 34.11 ? 341  ALA D CA  1 
ATOM   16923 C  C   . ALA D 1 349 ? 42.829  -18.310 112.159 1.00 32.33 ? 341  ALA D C   1 
ATOM   16924 O  O   . ALA D 1 349 ? 43.882  -18.024 111.579 1.00 31.83 ? 341  ALA D O   1 
ATOM   16925 C  CB  . ALA D 1 349 ? 41.058  -19.415 110.779 1.00 28.93 ? 341  ALA D CB  1 
ATOM   16926 N  N   . LEU D 1 350 ? 42.258  -17.488 113.044 1.00 29.79 ? 342  LEU D N   1 
ATOM   16927 C  CA  . LEU D 1 350 ? 42.859  -16.196 113.359 1.00 28.35 ? 342  LEU D CA  1 
ATOM   16928 C  C   . LEU D 1 350 ? 44.206  -16.369 114.059 1.00 32.78 ? 342  LEU D C   1 
ATOM   16929 O  O   . LEU D 1 350 ? 45.187  -15.701 113.709 1.00 32.47 ? 342  LEU D O   1 
ATOM   16930 C  CB  . LEU D 1 350 ? 41.888  -15.372 114.212 1.00 28.94 ? 342  LEU D CB  1 
ATOM   16931 C  CG  . LEU D 1 350 ? 42.277  -13.933 114.559 1.00 28.83 ? 342  LEU D CG  1 
ATOM   16932 C  CD1 . LEU D 1 350 ? 42.767  -13.183 113.324 1.00 31.47 ? 342  LEU D CD1 1 
ATOM   16933 C  CD2 . LEU D 1 350 ? 41.097  -13.204 115.187 1.00 27.02 ? 342  LEU D CD2 1 
ATOM   16934 N  N   . LYS D 1 351 ? 44.278  -17.275 115.038 1.00 33.62 ? 343  LYS D N   1 
ATOM   16935 C  CA  . LYS D 1 351 ? 45.539  -17.508 115.737 1.00 38.36 ? 343  LYS D CA  1 
ATOM   16936 C  C   . LYS D 1 351 ? 46.623  -17.990 114.777 1.00 41.54 ? 343  LYS D C   1 
ATOM   16937 O  O   . LYS D 1 351 ? 47.789  -17.600 114.900 1.00 41.91 ? 343  LYS D O   1 
ATOM   16938 C  CB  . LYS D 1 351 ? 45.335  -18.512 116.872 1.00 42.43 ? 343  LYS D CB  1 
ATOM   16939 N  N   . GLU D 1 352 ? 46.255  -18.824 113.800 1.00 39.92 ? 344  GLU D N   1 
ATOM   16940 C  CA  . GLU D 1 352 ? 47.227  -19.249 112.797 1.00 36.86 ? 344  GLU D CA  1 
ATOM   16941 C  C   . GLU D 1 352 ? 47.663  -18.081 111.913 1.00 41.20 ? 344  GLU D C   1 
ATOM   16942 O  O   . GLU D 1 352 ? 48.847  -17.968 111.570 1.00 43.72 ? 344  GLU D O   1 
ATOM   16943 C  CB  . GLU D 1 352 ? 46.650  -20.385 111.950 1.00 34.23 ? 344  GLU D CB  1 
ATOM   16944 N  N   . VAL D 1 353 ? 46.729  -17.200 111.534 1.00 36.21 ? 345  VAL D N   1 
ATOM   16945 C  CA  . VAL D 1 353 ? 47.104  -16.024 110.747 1.00 38.22 ? 345  VAL D CA  1 
ATOM   16946 C  C   . VAL D 1 353 ? 48.023  -15.113 111.554 1.00 43.45 ? 345  VAL D C   1 
ATOM   16947 O  O   . VAL D 1 353 ? 49.020  -14.594 111.035 1.00 48.36 ? 345  VAL D O   1 
ATOM   16948 C  CB  . VAL D 1 353 ? 45.847  -15.279 110.250 1.00 36.35 ? 345  VAL D CB  1 
ATOM   16949 C  CG1 . VAL D 1 353 ? 46.191  -13.863 109.810 1.00 31.20 ? 345  VAL D CG1 1 
ATOM   16950 C  CG2 . VAL D 1 353 ? 45.209  -16.029 109.093 1.00 38.07 ? 345  VAL D CG2 1 
ATOM   16951 N  N   . CYS D 1 354 ? 47.721  -14.924 112.843 1.00 45.11 ? 346  CYS D N   1 
ATOM   16952 C  CA  . CYS D 1 354 ? 48.584  -14.105 113.690 1.00 45.97 ? 346  CYS D CA  1 
ATOM   16953 C  C   . CYS D 1 354 ? 49.963  -14.737 113.861 1.00 48.56 ? 346  CYS D C   1 
ATOM   16954 O  O   . CYS D 1 354 ? 50.962  -14.019 113.995 1.00 52.70 ? 346  CYS D O   1 
ATOM   16955 C  CB  . CYS D 1 354 ? 47.919  -13.872 115.051 1.00 48.25 ? 346  CYS D CB  1 
ATOM   16956 S  SG  . CYS D 1 354 ? 48.689  -12.577 116.087 1.00 51.97 ? 346  CYS D SG  1 
ATOM   16957 N  N   . ALA D 1 355 ? 50.045  -16.070 113.851 1.00 46.70 ? 347  ALA D N   1 
ATOM   16958 C  CA  . ALA D 1 355 ? 51.346  -16.728 113.920 1.00 46.03 ? 347  ALA D CA  1 
ATOM   16959 C  C   . ALA D 1 355 ? 52.161  -16.469 112.656 1.00 49.97 ? 347  ALA D C   1 
ATOM   16960 O  O   . ALA D 1 355 ? 53.341  -16.108 112.730 1.00 55.03 ? 347  ALA D O   1 
ATOM   16961 C  CB  . ALA D 1 355 ? 51.167  -18.228 114.152 1.00 42.56 ? 347  ALA D CB  1 
ATOM   16962 N  N   . LYS D 1 356 ? 51.545  -16.633 111.487 1.00 47.27 ? 348  LYS D N   1 
ATOM   16963 C  CA  . LYS D 1 356 ? 52.248  -16.449 110.220 1.00 46.08 ? 348  LYS D CA  1 
ATOM   16964 C  C   . LYS D 1 356 ? 52.699  -15.002 110.025 1.00 44.12 ? 348  LYS D C   1 
ATOM   16965 O  O   . LYS D 1 356 ? 51.942  -14.066 110.276 1.00 46.22 ? 348  LYS D O   1 
ATOM   16966 C  CB  . LYS D 1 356 ? 51.364  -16.886 109.049 1.00 43.77 ? 348  LYS D CB  1 
ATOM   16967 N  N   . ASN D 1 368 ? 44.843  -14.789 102.502 1.00 39.83 ? 360  ASN D N   1 
ATOM   16968 C  CA  . ASN D 1 368 ? 43.562  -14.859 101.818 1.00 36.00 ? 360  ASN D CA  1 
ATOM   16969 C  C   . ASN D 1 368 ? 42.448  -15.246 102.780 1.00 30.44 ? 360  ASN D C   1 
ATOM   16970 O  O   . ASN D 1 368 ? 42.210  -16.429 103.036 1.00 27.32 ? 360  ASN D O   1 
ATOM   16971 C  CB  . ASN D 1 368 ? 43.615  -15.852 100.655 1.00 43.46 ? 360  ASN D CB  1 
ATOM   16972 C  CG  . ASN D 1 368 ? 42.371  -15.784 99.765  1.00 43.69 ? 360  ASN D CG  1 
ATOM   16973 O  OD1 . ASN D 1 368 ? 41.274  -15.504 100.232 1.00 45.29 ? 360  ASN D OD1 1 
ATOM   16974 N  ND2 . ASN D 1 368 ? 42.549  -16.041 98.479  1.00 47.90 ? 360  ASN D ND2 1 
ATOM   16975 N  N   . SER D 1 369 ? 41.754  -14.226 103.287 1.00 25.61 ? 361  SER D N   1 
ATOM   16976 C  CA  . SER D 1 369 ? 40.597  -14.459 104.146 1.00 26.35 ? 361  SER D CA  1 
ATOM   16977 C  C   . SER D 1 369 ? 39.521  -15.260 103.424 1.00 26.42 ? 361  SER D C   1 
ATOM   16978 O  O   . SER D 1 369 ? 38.855  -16.103 104.033 1.00 24.59 ? 361  SER D O   1 
ATOM   16979 C  CB  . SER D 1 369 ? 40.018  -13.123 104.623 1.00 26.26 ? 361  SER D CB  1 
ATOM   16980 O  OG  . SER D 1 369 ? 40.964  -12.376 105.366 1.00 28.50 ? 361  SER D OG  1 
ATOM   16981 N  N   . ILE D 1 370 ? 39.322  -14.989 102.131 1.00 26.65 ? 362  ILE D N   1 
ATOM   16982 C  CA  . ILE D 1 370 ? 38.290  -15.688 101.367 1.00 24.24 ? 362  ILE D CA  1 
ATOM   16983 C  C   . ILE D 1 370 ? 38.591  -17.180 101.321 1.00 22.71 ? 362  ILE D C   1 
ATOM   16984 O  O   . ILE D 1 370 ? 37.711  -18.017 101.558 1.00 26.65 ? 362  ILE D O   1 
ATOM   16985 C  CB  . ILE D 1 370 ? 38.171  -15.089 99.953  1.00 23.53 ? 362  ILE D CB  1 
ATOM   16986 C  CG1 . ILE D 1 370 ? 37.843  -13.593 100.029 1.00 23.79 ? 362  ILE D CG1 1 
ATOM   16987 C  CG2 . ILE D 1 370 ? 37.118  -15.851 99.134  1.00 20.34 ? 362  ILE D CG2 1 
ATOM   16988 C  CD1 . ILE D 1 370 ? 37.833  -12.887 98.676  1.00 20.30 ? 362  ILE D CD1 1 
ATOM   16989 N  N   . GLU D 1 371 ? 39.843  -17.536 101.015 1.00 23.55 ? 363  GLU D N   1 
ATOM   16990 C  CA  . GLU D 1 371 ? 40.221  -18.943 101.024 1.00 24.80 ? 363  GLU D CA  1 
ATOM   16991 C  C   . GLU D 1 371 ? 39.857  -19.591 102.355 1.00 28.86 ? 363  GLU D C   1 
ATOM   16992 O  O   . GLU D 1 371 ? 39.282  -20.689 102.388 1.00 30.32 ? 363  GLU D O   1 
ATOM   16993 C  CB  . GLU D 1 371 ? 41.718  -19.084 100.738 1.00 30.65 ? 363  GLU D CB  1 
ATOM   16994 C  CG  . GLU D 1 371 ? 42.167  -20.516 100.441 1.00 31.49 ? 363  GLU D CG  1 
ATOM   16995 C  CD  . GLU D 1 371 ? 42.148  -20.847 98.946  1.00 38.44 ? 363  GLU D CD  1 
ATOM   16996 O  OE1 . GLU D 1 371 ? 42.644  -20.024 98.138  1.00 34.31 ? 363  GLU D OE1 1 
ATOM   16997 O  OE2 . GLU D 1 371 ? 41.643  -21.935 98.579  1.00 42.65 ? 363  GLU D OE2 1 
ATOM   16998 N  N   . ILE D 1 372 ? 40.146  -18.901 103.463 1.00 29.46 ? 364  ILE D N   1 
ATOM   16999 C  CA  . ILE D 1 372 ? 39.823  -19.426 104.789 1.00 27.96 ? 364  ILE D CA  1 
ATOM   17000 C  C   . ILE D 1 372 ? 38.318  -19.579 104.956 1.00 28.20 ? 364  ILE D C   1 
ATOM   17001 O  O   . ILE D 1 372 ? 37.839  -20.584 105.498 1.00 32.20 ? 364  ILE D O   1 
ATOM   17002 C  CB  . ILE D 1 372 ? 40.418  -18.519 105.881 1.00 24.05 ? 364  ILE D CB  1 
ATOM   17003 C  CG1 . ILE D 1 372 ? 41.950  -18.535 105.806 1.00 26.67 ? 364  ILE D CG1 1 
ATOM   17004 C  CG2 . ILE D 1 372 ? 39.923  -18.939 107.258 1.00 23.53 ? 364  ILE D CG2 1 
ATOM   17005 C  CD1 . ILE D 1 372 ? 42.620  -17.534 106.711 1.00 29.37 ? 364  ILE D CD1 1 
ATOM   17006 N  N   . LEU D 1 373 ? 37.551  -18.589 104.496 1.00 27.49 ? 365  LEU D N   1 
ATOM   17007 C  CA  . LEU D 1 373 ? 36.103  -18.624 104.672 1.00 31.96 ? 365  LEU D CA  1 
ATOM   17008 C  C   . LEU D 1 373 ? 35.462  -19.689 103.792 1.00 21.07 ? 365  LEU D C   1 
ATOM   17009 O  O   . LEU D 1 373 ? 34.515  -20.361 104.216 1.00 25.77 ? 365  LEU D O   1 
ATOM   17010 C  CB  . LEU D 1 373 ? 35.502  -17.251 104.359 1.00 32.97 ? 365  LEU D CB  1 
ATOM   17011 C  CG  . LEU D 1 373 ? 34.584  -16.617 105.407 1.00 40.49 ? 365  LEU D CG  1 
ATOM   17012 C  CD1 . LEU D 1 373 ? 35.378  -16.234 106.648 1.00 46.34 ? 365  LEU D CD1 1 
ATOM   17013 C  CD2 . LEU D 1 373 ? 33.852  -15.405 104.838 1.00 36.20 ? 365  LEU D CD2 1 
ATOM   17014 N  N   . ALA D 1 374 ? 35.960  -19.851 102.562 1.00 26.35 ? 366  ALA D N   1 
ATOM   17015 C  CA  . ALA D 1 374 ? 35.336  -20.785 101.626 1.00 27.36 ? 366  ALA D CA  1 
ATOM   17016 C  C   . ALA D 1 374 ? 35.379  -22.217 102.146 1.00 27.96 ? 366  ALA D C   1 
ATOM   17017 O  O   . ALA D 1 374 ? 34.418  -22.974 101.969 1.00 32.34 ? 366  ALA D O   1 
ATOM   17018 C  CB  . ALA D 1 374 ? 36.009  -20.693 100.254 1.00 28.65 ? 366  ALA D CB  1 
ATOM   17019 N  N   . LYS D 1 375 ? 36.484  -22.611 102.790 1.00 30.23 ? 367  LYS D N   1 
ATOM   17020 C  CA  . LYS D 1 375 ? 36.578  -23.966 103.322 1.00 31.16 ? 367  LYS D CA  1 
ATOM   17021 C  C   . LYS D 1 375 ? 35.481  -24.240 104.342 1.00 32.31 ? 367  LYS D C   1 
ATOM   17022 O  O   . LYS D 1 375 ? 34.982  -25.367 104.430 1.00 31.96 ? 367  LYS D O   1 
ATOM   17023 C  CB  . LYS D 1 375 ? 37.961  -24.199 103.944 1.00 29.40 ? 367  LYS D CB  1 
ATOM   17024 N  N   . GLU D 1 376 ? 35.070  -23.219 105.091 1.00 28.91 ? 368  GLU D N   1 
ATOM   17025 C  CA  . GLU D 1 376 ? 34.057  -23.363 106.128 1.00 32.01 ? 368  GLU D CA  1 
ATOM   17026 C  C   . GLU D 1 376 ? 32.637  -23.143 105.614 1.00 31.67 ? 368  GLU D C   1 
ATOM   17027 O  O   . GLU D 1 376 ? 31.694  -23.752 106.137 1.00 28.82 ? 368  GLU D O   1 
ATOM   17028 C  CB  . GLU D 1 376 ? 34.350  -22.378 107.269 1.00 34.15 ? 368  GLU D CB  1 
ATOM   17029 C  CG  . GLU D 1 376 ? 33.266  -22.249 108.336 1.00 32.23 ? 368  GLU D CG  1 
ATOM   17030 C  CD  . GLU D 1 376 ? 33.228  -23.421 109.303 1.00 42.56 ? 368  GLU D CD  1 
ATOM   17031 O  OE1 . GLU D 1 376 ? 33.927  -24.433 109.067 1.00 43.18 ? 368  GLU D OE1 1 
ATOM   17032 O  OE2 . GLU D 1 376 ? 32.497  -23.326 110.311 1.00 43.90 ? 368  GLU D OE2 1 
ATOM   17033 N  N   . LEU D 1 377 ? 32.460  -22.303 104.592 1.00 27.05 ? 369  LEU D N   1 
ATOM   17034 C  CA  . LEU D 1 377 ? 31.132  -21.927 104.115 1.00 22.78 ? 369  LEU D CA  1 
ATOM   17035 C  C   . LEU D 1 377 ? 30.908  -22.446 102.702 1.00 25.26 ? 369  LEU D C   1 
ATOM   17036 O  O   . LEU D 1 377 ? 31.181  -21.731 101.723 1.00 23.94 ? 369  LEU D O   1 
ATOM   17037 C  CB  . LEU D 1 377 ? 30.964  -20.407 104.165 1.00 23.76 ? 369  LEU D CB  1 
ATOM   17038 C  CG  . LEU D 1 377 ? 31.162  -19.697 105.506 1.00 29.63 ? 369  LEU D CG  1 
ATOM   17039 C  CD1 . LEU D 1 377 ? 31.082  -18.178 105.326 1.00 29.91 ? 369  LEU D CD1 1 
ATOM   17040 C  CD2 . LEU D 1 377 ? 30.145  -20.165 106.526 1.00 26.28 ? 369  LEU D CD2 1 
ATOM   17041 N  N   . PRO D 1 378 ? 30.406  -23.675 102.536 1.00 29.24 ? 370  PRO D N   1 
ATOM   17042 C  CA  . PRO D 1 378 ? 30.080  -24.156 101.184 1.00 27.34 ? 370  PRO D CA  1 
ATOM   17043 C  C   . PRO D 1 378 ? 29.026  -23.317 100.482 1.00 21.35 ? 370  PRO D C   1 
ATOM   17044 O  O   . PRO D 1 378 ? 28.921  -23.379 99.251  1.00 25.56 ? 370  PRO D O   1 
ATOM   17045 C  CB  . PRO D 1 378 ? 29.592  -25.592 101.429 1.00 28.79 ? 370  PRO D CB  1 
ATOM   17046 C  CG  . PRO D 1 378 ? 29.166  -25.612 102.861 1.00 32.36 ? 370  PRO D CG  1 
ATOM   17047 C  CD  . PRO D 1 378 ? 30.134  -24.701 103.559 1.00 29.68 ? 370  PRO D CD  1 
ATOM   17048 N  N   . GLU D 1 379 ? 28.246  -22.528 101.217 1.00 22.99 ? 371  GLU D N   1 
ATOM   17049 C  CA  . GLU D 1 379 ? 27.284  -21.628 100.595 1.00 21.98 ? 371  GLU D CA  1 
ATOM   17050 C  C   . GLU D 1 379 ? 27.923  -20.390 99.982  1.00 21.38 ? 371  GLU D C   1 
ATOM   17051 O  O   . GLU D 1 379 ? 27.221  -19.613 99.333  1.00 21.03 ? 371  GLU D O   1 
ATOM   17052 C  CB  . GLU D 1 379 ? 26.222  -21.189 101.614 1.00 24.44 ? 371  GLU D CB  1 
ATOM   17053 C  CG  . GLU D 1 379 ? 26.748  -20.365 102.785 1.00 26.84 ? 371  GLU D CG  1 
ATOM   17054 C  CD  . GLU D 1 379 ? 27.138  -21.227 103.983 1.00 28.64 ? 371  GLU D CD  1 
ATOM   17055 O  OE1 . GLU D 1 379 ? 27.753  -22.294 103.780 1.00 23.24 ? 371  GLU D OE1 1 
ATOM   17056 O  OE2 . GLU D 1 379 ? 26.815  -20.837 105.128 1.00 20.90 ? 371  GLU D OE2 1 
ATOM   17057 N  N   . LEU D 1 380 ? 29.222  -20.176 100.176 1.00 26.88 ? 372  LEU D N   1 
ATOM   17058 C  CA  . LEU D 1 380 ? 29.857  -18.971 99.662  1.00 21.80 ? 372  LEU D CA  1 
ATOM   17059 C  C   . LEU D 1 380 ? 29.811  -18.952 98.138  1.00 20.23 ? 372  LEU D C   1 
ATOM   17060 O  O   . LEU D 1 380 ? 30.101  -19.955 97.480  1.00 21.80 ? 372  LEU D O   1 
ATOM   17061 C  CB  . LEU D 1 380 ? 31.301  -18.893 100.157 1.00 23.68 ? 372  LEU D CB  1 
ATOM   17062 C  CG  . LEU D 1 380 ? 31.983  -17.530 100.043 1.00 19.96 ? 372  LEU D CG  1 
ATOM   17063 C  CD1 . LEU D 1 380 ? 31.294  -16.515 100.937 1.00 19.18 ? 372  LEU D CD1 1 
ATOM   17064 C  CD2 . LEU D 1 380 ? 33.460  -17.678 100.407 1.00 22.88 ? 372  LEU D CD2 1 
ATOM   17065 N  N   . VAL D 1 381 ? 29.409  -17.814 97.581  1.00 18.68 ? 373  VAL D N   1 
ATOM   17066 C  CA  . VAL D 1 381 ? 29.383  -17.596 96.140  1.00 17.25 ? 373  VAL D CA  1 
ATOM   17067 C  C   . VAL D 1 381 ? 30.123  -16.288 95.888  1.00 19.16 ? 373  VAL D C   1 
ATOM   17068 O  O   . VAL D 1 381 ? 29.685  -15.225 96.342  1.00 22.47 ? 373  VAL D O   1 
ATOM   17069 C  CB  . VAL D 1 381 ? 27.955  -17.539 95.580  1.00 18.00 ? 373  VAL D CB  1 
ATOM   17070 C  CG1 . VAL D 1 381 ? 27.969  -17.187 94.092  1.00 20.62 ? 373  VAL D CG1 1 
ATOM   17071 C  CG2 . VAL D 1 381 ? 27.235  -18.862 95.821  1.00 19.34 ? 373  VAL D CG2 1 
ATOM   17072 N  N   . GLY D 1 382 ? 31.262  -16.364 95.205  1.00 16.02 ? 374  GLY D N   1 
ATOM   17073 C  CA  . GLY D 1 382 ? 32.022  -15.173 94.888  1.00 15.37 ? 374  GLY D CA  1 
ATOM   17074 C  C   . GLY D 1 382 ? 31.569  -14.522 93.591  1.00 14.83 ? 374  GLY D C   1 
ATOM   17075 O  O   . GLY D 1 382 ? 30.674  -14.992 92.896  1.00 18.55 ? 374  GLY D O   1 
ATOM   17076 N  N   . GLY D 1 383 ? 32.217  -13.413 93.264  1.00 14.38 ? 375  GLY D N   1 
ATOM   17077 C  CA  . GLY D 1 383 ? 31.953  -12.761 91.996  1.00 15.40 ? 375  GLY D CA  1 
ATOM   17078 C  C   . GLY D 1 383 ? 32.733  -11.470 91.903  1.00 19.40 ? 375  GLY D C   1 
ATOM   17079 O  O   . GLY D 1 383 ? 33.170  -10.906 92.908  1.00 16.43 ? 375  GLY D O   1 
ATOM   17080 N  N   . SER D 1 384 ? 32.894  -11.003 90.669  1.00 13.40 ? 376  SER D N   1 
ATOM   17081 C  CA  . SER D 1 384 ? 33.473  -9.685  90.483  1.00 16.87 ? 376  SER D CA  1 
ATOM   17082 C  C   . SER D 1 384 ? 32.965  -9.114  89.172  1.00 15.57 ? 376  SER D C   1 
ATOM   17083 O  O   . SER D 1 384 ? 32.513  -9.842  88.280  1.00 16.36 ? 376  SER D O   1 
ATOM   17084 C  CB  . SER D 1 384 ? 35.013  -9.703  90.516  1.00 14.26 ? 376  SER D CB  1 
ATOM   17085 O  OG  . SER D 1 384 ? 35.569  -10.201 89.312  1.00 18.04 ? 376  SER D OG  1 
ATOM   17086 N  N   . ALA D 1 385 ? 33.031  -7.787  89.089  1.00 14.27 ? 377  ALA D N   1 
ATOM   17087 C  CA  . ALA D 1 385 ? 32.656  -7.052  87.883  1.00 14.60 ? 377  ALA D CA  1 
ATOM   17088 C  C   . ALA D 1 385 ? 33.903  -6.849  87.021  1.00 12.85 ? 377  ALA D C   1 
ATOM   17089 O  O   . ALA D 1 385 ? 34.483  -5.761  86.933  1.00 17.45 ? 377  ALA D O   1 
ATOM   17090 C  CB  . ALA D 1 385 ? 31.982  -5.732  88.256  1.00 12.66 ? 377  ALA D CB  1 
ATOM   17091 N  N   . ASP D 1 386 ? 34.334  -7.954  86.409  1.00 18.77 ? 378  ASP D N   1 
ATOM   17092 C  CA  . ASP D 1 386 ? 35.474  -7.986  85.478  1.00 19.60 ? 378  ASP D CA  1 
ATOM   17093 C  C   . ASP D 1 386 ? 36.780  -7.540  86.140  1.00 22.55 ? 378  ASP D C   1 
ATOM   17094 O  O   . ASP D 1 386 ? 37.588  -6.841  85.528  1.00 18.27 ? 378  ASP D O   1 
ATOM   17095 C  CB  . ASP D 1 386 ? 35.189  -7.147  84.221  1.00 23.95 ? 378  ASP D CB  1 
ATOM   17096 C  CG  . ASP D 1 386 ? 36.205  -7.391  83.096  1.00 26.21 ? 378  ASP D CG  1 
ATOM   17097 O  OD1 . ASP D 1 386 ? 36.590  -8.555  82.877  1.00 29.87 ? 378  ASP D OD1 1 
ATOM   17098 O  OD2 . ASP D 1 386 ? 36.620  -6.416  82.434  1.00 25.87 ? 378  ASP D OD2 1 
ATOM   17099 N  N   . LEU D 1 387 ? 37.004  -7.956  87.392  1.00 15.43 ? 379  LEU D N   1 
ATOM   17100 C  CA  . LEU D 1 387 ? 38.294  -7.715  88.036  1.00 18.91 ? 379  LEU D CA  1 
ATOM   17101 C  C   . LEU D 1 387 ? 39.298  -8.810  87.681  1.00 22.83 ? 379  LEU D C   1 
ATOM   17102 O  O   . LEU D 1 387 ? 38.929  -9.939  87.347  1.00 26.92 ? 379  LEU D O   1 
ATOM   17103 C  CB  . LEU D 1 387 ? 38.154  -7.648  89.558  1.00 14.63 ? 379  LEU D CB  1 
ATOM   17104 C  CG  . LEU D 1 387 ? 37.387  -6.446  90.092  1.00 22.25 ? 379  LEU D CG  1 
ATOM   17105 C  CD1 . LEU D 1 387 ? 37.656  -6.238  91.588  1.00 23.38 ? 379  LEU D CD1 1 
ATOM   17106 C  CD2 . LEU D 1 387 ? 37.736  -5.211  89.300  1.00 21.36 ? 379  LEU D CD2 1 
ATOM   17107 N  N   . THR D 1 388 ? 40.578  -8.464  87.741  1.00 16.84 ? 380  THR D N   1 
ATOM   17108 C  CA  . THR D 1 388 ? 41.615  -9.479  87.595  1.00 23.91 ? 380  THR D CA  1 
ATOM   17109 C  C   . THR D 1 388 ? 41.627  -10.346 88.849  1.00 24.50 ? 380  THR D C   1 
ATOM   17110 O  O   . THR D 1 388 ? 41.653  -9.807  89.959  1.00 25.17 ? 380  THR D O   1 
ATOM   17111 C  CB  . THR D 1 388 ? 42.986  -8.833  87.381  1.00 28.75 ? 380  THR D CB  1 
ATOM   17112 O  OG1 . THR D 1 388 ? 42.983  -8.118  86.142  1.00 35.49 ? 380  THR D OG1 1 
ATOM   17113 C  CG2 . THR D 1 388 ? 44.084  -9.888  87.343  1.00 32.68 ? 380  THR D CG2 1 
ATOM   17114 N  N   . PRO D 1 389 ? 41.603  -11.674 88.720  1.00 31.80 ? 381  PRO D N   1 
ATOM   17115 C  CA  . PRO D 1 389 ? 41.524  -12.525 89.915  1.00 31.79 ? 381  PRO D CA  1 
ATOM   17116 C  C   . PRO D 1 389 ? 42.741  -12.322 90.803  1.00 29.37 ? 381  PRO D C   1 
ATOM   17117 O  O   . PRO D 1 389 ? 43.878  -12.272 90.327  1.00 32.00 ? 381  PRO D O   1 
ATOM   17118 C  CB  . PRO D 1 389 ? 41.475  -13.950 89.344  1.00 36.03 ? 381  PRO D CB  1 
ATOM   17119 C  CG  . PRO D 1 389 ? 41.164  -13.792 87.882  1.00 39.85 ? 381  PRO D CG  1 
ATOM   17120 C  CD  . PRO D 1 389 ? 41.731  -12.466 87.483  1.00 34.01 ? 381  PRO D CD  1 
ATOM   17121 N  N   . SER D 1 390 ? 42.492  -12.184 92.102  1.00 26.80 ? 382  SER D N   1 
ATOM   17122 C  CA  . SER D 1 390 ? 43.571  -12.096 93.074  1.00 26.03 ? 382  SER D CA  1 
ATOM   17123 C  C   . SER D 1 390 ? 43.067  -12.637 94.403  1.00 28.25 ? 382  SER D C   1 
ATOM   17124 O  O   . SER D 1 390 ? 41.885  -12.959 94.561  1.00 23.58 ? 382  SER D O   1 
ATOM   17125 C  CB  . SER D 1 390 ? 44.087  -10.658 93.228  1.00 22.70 ? 382  SER D CB  1 
ATOM   17126 O  OG  . SER D 1 390 ? 43.187  -9.865  93.983  1.00 23.86 ? 382  SER D OG  1 
ATOM   17127 N  N   . ASN D 1 391 ? 43.987  -12.727 95.366  1.00 22.88 ? 383  ASN D N   1 
ATOM   17128 C  CA  . ASN D 1 391 ? 43.634  -13.212 96.697  1.00 27.10 ? 383  ASN D CA  1 
ATOM   17129 C  C   . ASN D 1 391 ? 42.611  -12.319 97.385  1.00 22.77 ? 383  ASN D C   1 
ATOM   17130 O  O   . ASN D 1 391 ? 41.956  -12.767 98.332  1.00 24.82 ? 383  ASN D O   1 
ATOM   17131 C  CB  . ASN D 1 391 ? 44.889  -13.306 97.563  1.00 32.08 ? 383  ASN D CB  1 
ATOM   17132 C  CG  . ASN D 1 391 ? 45.542  -11.953 97.768  1.00 42.32 ? 383  ASN D CG  1 
ATOM   17133 O  OD1 . ASN D 1 391 ? 46.090  -11.371 96.832  1.00 47.36 ? 383  ASN D OD1 1 
ATOM   17134 N  ND2 . ASN D 1 391 ? 45.465  -11.432 98.990  1.00 44.27 ? 383  ASN D ND2 1 
ATOM   17135 N  N   . LEU D 1 392 ? 42.468  -11.066 96.940  1.00 19.38 ? 384  LEU D N   1 
ATOM   17136 C  CA  . LEU D 1 392 ? 41.505  -10.150 97.543  1.00 17.24 ? 384  LEU D CA  1 
ATOM   17137 C  C   . LEU D 1 392 ? 40.069  -10.422 97.116  1.00 24.90 ? 384  LEU D C   1 
ATOM   17138 O  O   . LEU D 1 392 ? 39.140  -9.999  97.816  1.00 22.48 ? 384  LEU D O   1 
ATOM   17139 C  CB  . LEU D 1 392 ? 41.853  -8.702  97.185  1.00 19.94 ? 384  LEU D CB  1 
ATOM   17140 C  CG  . LEU D 1 392 ? 43.161  -8.148  97.754  1.00 27.64 ? 384  LEU D CG  1 
ATOM   17141 C  CD1 . LEU D 1 392 ? 43.413  -6.735  97.244  1.00 22.80 ? 384  LEU D CD1 1 
ATOM   17142 C  CD2 . LEU D 1 392 ? 43.133  -8.188  99.276  1.00 27.19 ? 384  LEU D CD2 1 
ATOM   17143 N  N   . THR D 1 393 ? 39.863  -11.085 95.974  1.00 22.18 ? 385  THR D N   1 
ATOM   17144 C  CA  . THR D 1 393 ? 38.521  -11.235 95.425  1.00 25.35 ? 385  THR D CA  1 
ATOM   17145 C  C   . THR D 1 393 ? 38.223  -12.646 94.933  1.00 24.21 ? 385  THR D C   1 
ATOM   17146 O  O   . THR D 1 393 ? 37.203  -12.843 94.267  1.00 20.42 ? 385  THR D O   1 
ATOM   17147 C  CB  . THR D 1 393 ? 38.294  -10.260 94.260  1.00 27.06 ? 385  THR D CB  1 
ATOM   17148 O  OG1 . THR D 1 393 ? 39.203  -10.571 93.200  1.00 28.50 ? 385  THR D OG1 1 
ATOM   17149 C  CG2 . THR D 1 393 ? 38.511  -8.826  94.692  1.00 29.75 ? 385  THR D CG2 1 
ATOM   17150 N  N   . ASP D 1 394 ? 39.070  -13.631 95.228  1.00 25.20 ? 386  ASP D N   1 
ATOM   17151 C  CA  . ASP D 1 394 ? 38.941  -14.959 94.639  1.00 23.55 ? 386  ASP D CA  1 
ATOM   17152 C  C   . ASP D 1 394 ? 39.689  -15.935 95.535  1.00 23.88 ? 386  ASP D C   1 
ATOM   17153 O  O   . ASP D 1 394 ? 40.409  -15.530 96.450  1.00 23.11 ? 386  ASP D O   1 
ATOM   17154 C  CB  . ASP D 1 394 ? 39.494  -14.964 93.211  1.00 26.46 ? 386  ASP D CB  1 
ATOM   17155 C  CG  . ASP D 1 394 ? 39.086  -16.188 92.415  1.00 29.73 ? 386  ASP D CG  1 
ATOM   17156 O  OD1 . ASP D 1 394 ? 38.317  -17.031 92.923  1.00 26.45 ? 386  ASP D OD1 1 
ATOM   17157 O  OD2 . ASP D 1 394 ? 39.550  -16.300 91.262  1.00 32.23 ? 386  ASP D OD2 1 
ATOM   17158 N  N   . TRP D 1 395 ? 39.502  -17.228 95.278  1.00 27.73 ? 387  TRP D N   1 
ATOM   17159 C  CA  . TRP D 1 395 ? 40.252  -18.253 95.992  1.00 27.93 ? 387  TRP D CA  1 
ATOM   17160 C  C   . TRP D 1 395 ? 40.525  -19.423 95.051  1.00 29.06 ? 387  TRP D C   1 
ATOM   17161 O  O   . TRP D 1 395 ? 40.044  -19.464 93.915  1.00 27.51 ? 387  TRP D O   1 
ATOM   17162 C  CB  . TRP D 1 395 ? 39.525  -18.699 97.262  1.00 27.80 ? 387  TRP D CB  1 
ATOM   17163 C  CG  . TRP D 1 395 ? 38.307  -19.529 97.025  1.00 29.03 ? 387  TRP D CG  1 
ATOM   17164 C  CD1 . TRP D 1 395 ? 38.206  -20.881 97.147  1.00 30.12 ? 387  TRP D CD1 1 
ATOM   17165 C  CD2 . TRP D 1 395 ? 37.005  -19.060 96.646  1.00 25.25 ? 387  TRP D CD2 1 
ATOM   17166 N  NE1 . TRP D 1 395 ? 36.926  -21.288 96.866  1.00 28.49 ? 387  TRP D NE1 1 
ATOM   17167 C  CE2 . TRP D 1 395 ? 36.169  -20.188 96.551  1.00 26.91 ? 387  TRP D CE2 1 
ATOM   17168 C  CE3 . TRP D 1 395 ? 36.471  -17.797 96.370  1.00 22.02 ? 387  TRP D CE3 1 
ATOM   17169 C  CZ2 . TRP D 1 395 ? 34.820  -20.093 96.197  1.00 23.12 ? 387  TRP D CZ2 1 
ATOM   17170 C  CZ3 . TRP D 1 395 ? 35.131  -17.701 96.018  1.00 22.32 ? 387  TRP D CZ3 1 
ATOM   17171 C  CH2 . TRP D 1 395 ? 34.322  -18.843 95.928  1.00 19.40 ? 387  TRP D CH2 1 
ATOM   17172 N  N   . SER D 1 396 ? 41.279  -20.402 95.565  1.00 30.79 ? 388  SER D N   1 
ATOM   17173 C  CA  . SER D 1 396 ? 41.999  -21.349 94.714  1.00 33.41 ? 388  SER D CA  1 
ATOM   17174 C  C   . SER D 1 396 ? 41.065  -22.209 93.871  1.00 33.16 ? 388  SER D C   1 
ATOM   17175 O  O   . SER D 1 396 ? 41.326  -22.440 92.685  1.00 33.53 ? 388  SER D O   1 
ATOM   17176 C  CB  . SER D 1 396 ? 42.889  -22.244 95.579  1.00 32.86 ? 388  SER D CB  1 
ATOM   17177 O  OG  . SER D 1 396 ? 42.084  -23.031 96.452  1.00 29.72 ? 388  SER D OG  1 
ATOM   17178 N  N   . ASN D 1 397 ? 39.995  -22.726 94.465  1.00 33.12 ? 389  ASN D N   1 
ATOM   17179 C  CA  . ASN D 1 397 ? 39.132  -23.680 93.782  1.00 36.98 ? 389  ASN D CA  1 
ATOM   17180 C  C   . ASN D 1 397 ? 37.732  -23.124 93.534  1.00 33.82 ? 389  ASN D C   1 
ATOM   17181 O  O   . ASN D 1 397 ? 36.760  -23.880 93.484  1.00 39.67 ? 389  ASN D O   1 
ATOM   17182 C  CB  . ASN D 1 397 ? 39.063  -24.985 94.569  1.00 46.03 ? 389  ASN D CB  1 
ATOM   17183 C  CG  . ASN D 1 397 ? 38.883  -24.754 96.048  1.00 47.26 ? 389  ASN D CG  1 
ATOM   17184 O  OD1 . ASN D 1 397 ? 38.176  -23.835 96.456  1.00 41.21 ? 389  ASN D OD1 1 
ATOM   17185 N  ND2 . ASN D 1 397 ? 39.538  -25.576 96.863  1.00 47.85 ? 389  ASN D ND2 1 
ATOM   17186 N  N   . SER D 1 398 ? 37.619  -21.805 93.383  1.00 27.71 ? 390  SER D N   1 
ATOM   17187 C  CA  . SER D 1 398 ? 36.376  -21.209 92.909  1.00 22.72 ? 390  SER D CA  1 
ATOM   17188 C  C   . SER D 1 398 ? 36.013  -21.777 91.542  1.00 24.83 ? 390  SER D C   1 
ATOM   17189 O  O   . SER D 1 398 ? 36.869  -21.914 90.664  1.00 23.82 ? 390  SER D O   1 
ATOM   17190 C  CB  . SER D 1 398 ? 36.517  -19.689 92.823  1.00 21.98 ? 390  SER D CB  1 
ATOM   17191 O  OG  . SER D 1 398 ? 37.612  -19.333 91.994  1.00 21.67 ? 390  SER D OG  1 
ATOM   17192 N  N   . VAL D 1 399 ? 34.734  -22.101 91.365  1.00 20.76 ? 391  VAL D N   1 
ATOM   17193 C  CA  . VAL D 1 399 ? 34.215  -22.683 90.130  1.00 27.42 ? 391  VAL D CA  1 
ATOM   17194 C  C   . VAL D 1 399 ? 33.303  -21.660 89.466  1.00 27.15 ? 391  VAL D C   1 
ATOM   17195 O  O   . VAL D 1 399 ? 32.301  -21.240 90.055  1.00 19.42 ? 391  VAL D O   1 
ATOM   17196 C  CB  . VAL D 1 399 ? 33.459  -23.996 90.395  1.00 28.62 ? 391  VAL D CB  1 
ATOM   17197 C  CG1 . VAL D 1 399 ? 32.787  -24.506 89.111  1.00 22.14 ? 391  VAL D CG1 1 
ATOM   17198 C  CG2 . VAL D 1 399 ? 34.405  -25.045 90.982  1.00 23.01 ? 391  VAL D CG2 1 
ATOM   17199 N  N   . SER D 1 400 ? 33.634  -21.286 88.231  1.00 24.99 ? 392  SER D N   1 
ATOM   17200 C  CA  . SER D 1 400 ? 32.848  -20.304 87.496  1.00 20.59 ? 392  SER D CA  1 
ATOM   17201 C  C   . SER D 1 400 ? 31.475  -20.867 87.154  1.00 22.57 ? 392  SER D C   1 
ATOM   17202 O  O   . SER D 1 400 ? 31.357  -21.958 86.594  1.00 20.32 ? 392  SER D O   1 
ATOM   17203 C  CB  . SER D 1 400 ? 33.574  -19.897 86.214  1.00 25.11 ? 392  SER D CB  1 
ATOM   17204 O  OG  . SER D 1 400 ? 34.832  -19.297 86.491  1.00 26.68 ? 392  SER D OG  1 
ATOM   17205 N  N   . VAL D 1 401 ? 30.430  -20.113 87.484  1.00 19.90 ? 393  VAL D N   1 
ATOM   17206 C  CA  . VAL D 1 401 ? 29.097  -20.432 86.991  1.00 20.95 ? 393  VAL D CA  1 
ATOM   17207 C  C   . VAL D 1 401 ? 29.048  -20.186 85.487  1.00 24.85 ? 393  VAL D C   1 
ATOM   17208 O  O   . VAL D 1 401 ? 29.585  -19.191 84.984  1.00 21.03 ? 393  VAL D O   1 
ATOM   17209 C  CB  . VAL D 1 401 ? 28.052  -19.588 87.741  1.00 20.99 ? 393  VAL D CB  1 
ATOM   17210 C  CG1 . VAL D 1 401 ? 26.647  -19.810 87.180  1.00 23.29 ? 393  VAL D CG1 1 
ATOM   17211 C  CG2 . VAL D 1 401 ? 28.105  -19.907 89.228  1.00 22.22 ? 393  VAL D CG2 1 
ATOM   17212 N  N   . THR D 1 402 ? 28.415  -21.097 84.758  1.00 24.32 ? 394  THR D N   1 
ATOM   17213 C  CA  . THR D 1 402 ? 28.307  -21.001 83.309  1.00 27.58 ? 394  THR D CA  1 
ATOM   17214 C  C   . THR D 1 402 ? 26.863  -21.256 82.900  1.00 25.09 ? 394  THR D C   1 
ATOM   17215 O  O   . THR D 1 402 ? 26.003  -21.575 83.729  1.00 22.74 ? 394  THR D O   1 
ATOM   17216 C  CB  . THR D 1 402 ? 29.236  -21.997 82.599  1.00 28.38 ? 394  THR D CB  1 
ATOM   17217 O  OG1 . THR D 1 402 ? 28.839  -23.338 82.915  1.00 25.72 ? 394  THR D OG1 1 
ATOM   17218 C  CG2 . THR D 1 402 ? 30.686  -21.775 83.019  1.00 22.35 ? 394  THR D CG2 1 
ATOM   17219 N  N   . ARG D 1 403 ? 26.607  -21.126 81.597  1.00 28.58 ? 395  ARG D N   1 
ATOM   17220 C  CA  . ARG D 1 403 ? 25.269  -21.369 81.072  1.00 26.74 ? 395  ARG D CA  1 
ATOM   17221 C  C   . ARG D 1 403 ? 24.776  -22.775 81.405  1.00 26.83 ? 395  ARG D C   1 
ATOM   17222 O  O   . ARG D 1 403 ? 23.605  -22.964 81.753  1.00 28.16 ? 395  ARG D O   1 
ATOM   17223 C  CB  . ARG D 1 403 ? 25.265  -21.151 79.559  1.00 31.16 ? 395  ARG D CB  1 
ATOM   17224 C  CG  . ARG D 1 403 ? 23.912  -21.358 78.906  1.00 33.22 ? 395  ARG D CG  1 
ATOM   17225 C  CD  . ARG D 1 403 ? 23.990  -21.253 77.390  1.00 33.16 ? 395  ARG D CD  1 
ATOM   17226 N  NE  . ARG D 1 403 ? 22.653  -21.094 76.835  1.00 39.36 ? 395  ARG D NE  1 
ATOM   17227 C  CZ  . ARG D 1 403 ? 22.058  -19.917 76.661  1.00 41.90 ? 395  ARG D CZ  1 
ATOM   17228 N  NH1 . ARG D 1 403 ? 22.701  -18.801 76.984  1.00 43.65 ? 395  ARG D NH1 1 
ATOM   17229 N  NH2 . ARG D 1 403 ? 20.824  -19.852 76.166  1.00 32.02 ? 395  ARG D NH2 1 
ATOM   17230 N  N   . ASP D 1 404 ? 25.649  -23.777 81.306  1.00 25.24 ? 396  ASP D N   1 
ATOM   17231 C  CA  . ASP D 1 404 ? 25.208  -25.165 81.357  1.00 31.29 ? 396  ASP D CA  1 
ATOM   17232 C  C   . ASP D 1 404 ? 25.581  -25.892 82.640  1.00 28.48 ? 396  ASP D C   1 
ATOM   17233 O  O   . ASP D 1 404 ? 25.237  -27.069 82.785  1.00 34.82 ? 396  ASP D O   1 
ATOM   17234 C  CB  . ASP D 1 404 ? 25.767  -25.927 80.153  1.00 38.73 ? 396  ASP D CB  1 
ATOM   17235 C  CG  . ASP D 1 404 ? 25.337  -25.314 78.838  1.00 50.52 ? 396  ASP D CG  1 
ATOM   17236 O  OD1 . ASP D 1 404 ? 24.133  -24.991 78.696  1.00 43.94 ? 396  ASP D OD1 1 
ATOM   17237 O  OD2 . ASP D 1 404 ? 26.206  -25.137 77.958  1.00 58.42 ? 396  ASP D OD2 1 
ATOM   17238 N  N   . LYS D 1 405 ? 26.249  -25.232 83.583  1.00 26.46 ? 397  LYS D N   1 
ATOM   17239 C  CA  . LYS D 1 405 ? 26.715  -25.923 84.775  1.00 23.59 ? 397  LYS D CA  1 
ATOM   17240 C  C   . LYS D 1 405 ? 26.736  -24.958 85.953  1.00 25.85 ? 397  LYS D C   1 
ATOM   17241 O  O   . LYS D 1 405 ? 26.999  -23.762 85.791  1.00 25.19 ? 397  LYS D O   1 
ATOM   17242 C  CB  . LYS D 1 405 ? 28.107  -26.534 84.546  1.00 28.58 ? 397  LYS D CB  1 
ATOM   17243 N  N   . GLY D 1 406 ? 26.468  -25.496 87.142  1.00 25.18 ? 398  GLY D N   1 
ATOM   17244 C  CA  . GLY D 1 406 ? 26.503  -24.718 88.361  1.00 20.79 ? 398  GLY D CA  1 
ATOM   17245 C  C   . GLY D 1 406 ? 27.914  -24.282 88.726  1.00 26.88 ? 398  GLY D C   1 
ATOM   17246 O  O   . GLY D 1 406 ? 28.896  -24.558 88.036  1.00 27.97 ? 398  GLY D O   1 
ATOM   17247 N  N   . GLY D 1 407 ? 28.006  -23.581 89.847  1.00 22.99 ? 399  GLY D N   1 
ATOM   17248 C  CA  . GLY D 1 407 ? 29.303  -23.172 90.350  1.00 23.10 ? 399  GLY D CA  1 
ATOM   17249 C  C   . GLY D 1 407 ? 29.138  -22.316 91.582  1.00 24.98 ? 399  GLY D C   1 
ATOM   17250 O  O   . GLY D 1 407 ? 28.053  -22.242 92.162  1.00 23.81 ? 399  GLY D O   1 
ATOM   17251 N  N   . ASN D 1 408 ? 30.239  -21.650 91.971  1.00 22.21 ? 400  ASN D N   1 
ATOM   17252 C  CA  . ASN D 1 408 ? 30.194  -20.762 93.128  1.00 21.82 ? 400  ASN D CA  1 
ATOM   17253 C  C   . ASN D 1 408 ? 30.925  -19.440 92.886  1.00 22.46 ? 400  ASN D C   1 
ATOM   17254 O  O   . ASN D 1 408 ? 31.366  -18.802 93.847  1.00 22.55 ? 400  ASN D O   1 
ATOM   17255 C  CB  . ASN D 1 408 ? 30.755  -21.473 94.378  1.00 19.16 ? 400  ASN D CB  1 
ATOM   17256 C  CG  . ASN D 1 408 ? 32.169  -21.993 94.179  1.00 25.59 ? 400  ASN D CG  1 
ATOM   17257 O  OD1 . ASN D 1 408 ? 32.835  -21.680 93.193  1.00 24.32 ? 400  ASN D OD1 1 
ATOM   17258 N  ND2 . ASN D 1 408 ? 32.637  -22.791 95.131  1.00 25.58 ? 400  ASN D ND2 1 
ATOM   17259 N  N   . TYR D 1 409 ? 31.051  -18.999 91.635  1.00 17.45 ? 401  TYR D N   1 
ATOM   17260 C  CA  . TYR D 1 409 ? 31.711  -17.735 91.332  1.00 16.80 ? 401  TYR D CA  1 
ATOM   17261 C  C   . TYR D 1 409 ? 31.103  -17.167 90.063  1.00 17.11 ? 401  TYR D C   1 
ATOM   17262 O  O   . TYR D 1 409 ? 31.105  -17.828 89.016  1.00 18.04 ? 401  TYR D O   1 
ATOM   17263 C  CB  . TYR D 1 409 ? 33.227  -17.908 91.165  1.00 18.50 ? 401  TYR D CB  1 
ATOM   17264 C  CG  . TYR D 1 409 ? 33.975  -16.599 91.314  1.00 16.73 ? 401  TYR D CG  1 
ATOM   17265 C  CD1 . TYR D 1 409 ? 34.036  -15.677 90.269  1.00 16.24 ? 401  TYR D CD1 1 
ATOM   17266 C  CD2 . TYR D 1 409 ? 34.610  -16.279 92.510  1.00 20.03 ? 401  TYR D CD2 1 
ATOM   17267 C  CE1 . TYR D 1 409 ? 34.713  -14.472 90.418  1.00 22.35 ? 401  TYR D CE1 1 
ATOM   17268 C  CE2 . TYR D 1 409 ? 35.293  -15.085 92.664  1.00 18.25 ? 401  TYR D CE2 1 
ATOM   17269 C  CZ  . TYR D 1 409 ? 35.339  -14.183 91.622  1.00 23.04 ? 401  TYR D CZ  1 
ATOM   17270 O  OH  . TYR D 1 409 ? 36.023  -12.994 91.800  1.00 21.50 ? 401  TYR D OH  1 
ATOM   17271 N  N   . ILE D 1 410 ? 30.607  -15.939 90.150  1.00 16.98 ? 402  ILE D N   1 
ATOM   17272 C  CA  . ILE D 1 410 ? 29.847  -15.321 89.070  1.00 18.83 ? 402  ILE D CA  1 
ATOM   17273 C  C   . ILE D 1 410 ? 30.702  -14.245 88.415  1.00 16.54 ? 402  ILE D C   1 
ATOM   17274 O  O   . ILE D 1 410 ? 31.154  -13.310 89.085  1.00 18.60 ? 402  ILE D O   1 
ATOM   17275 C  CB  . ILE D 1 410 ? 28.534  -14.727 89.591  1.00 14.40 ? 402  ILE D CB  1 
ATOM   17276 C  CG1 . ILE D 1 410 ? 27.658  -15.828 90.197  1.00 22.53 ? 402  ILE D CG1 1 
ATOM   17277 C  CG2 . ILE D 1 410 ? 27.850  -13.941 88.488  1.00 13.97 ? 402  ILE D CG2 1 
ATOM   17278 C  CD1 . ILE D 1 410 ? 26.637  -15.305 91.203  1.00 19.50 ? 402  ILE D CD1 1 
ATOM   17279 N  N   . HIS D 1 411 ? 30.910  -14.364 87.106  1.00 15.02 ? 403  HIS D N   1 
ATOM   17280 C  CA  . HIS D 1 411 ? 31.546  -13.306 86.322  1.00 14.74 ? 403  HIS D CA  1 
ATOM   17281 C  C   . HIS D 1 411 ? 30.458  -12.336 85.886  1.00 17.91 ? 403  HIS D C   1 
ATOM   17282 O  O   . HIS D 1 411 ? 29.736  -12.591 84.914  1.00 16.93 ? 403  HIS D O   1 
ATOM   17283 C  CB  . HIS D 1 411 ? 32.282  -13.883 85.119  1.00 15.47 ? 403  HIS D CB  1 
ATOM   17284 C  CG  . HIS D 1 411 ? 33.348  -14.862 85.484  1.00 21.90 ? 403  HIS D CG  1 
ATOM   17285 N  ND1 . HIS D 1 411 ? 34.543  -14.479 86.058  1.00 24.13 ? 403  HIS D ND1 1 
ATOM   17286 C  CD2 . HIS D 1 411 ? 33.401  -16.209 85.367  1.00 25.19 ? 403  HIS D CD2 1 
ATOM   17287 C  CE1 . HIS D 1 411 ? 35.288  -15.549 86.271  1.00 24.84 ? 403  HIS D CE1 1 
ATOM   17288 N  NE2 . HIS D 1 411 ? 34.619  -16.610 85.862  1.00 25.02 ? 403  HIS D NE2 1 
ATOM   17289 N  N   . TYR D 1 412 ? 30.325  -11.225 86.615  1.00 15.45 ? 404  TYR D N   1 
ATOM   17290 C  CA  . TYR D 1 412 ? 29.301  -10.249 86.269  1.00 12.83 ? 404  TYR D CA  1 
ATOM   17291 C  C   . TYR D 1 412 ? 29.652  -9.420  85.039  1.00 15.80 ? 404  TYR D C   1 
ATOM   17292 O  O   . TYR D 1 412 ? 28.763  -8.755  84.498  1.00 17.44 ? 404  TYR D O   1 
ATOM   17293 C  CB  . TYR D 1 412 ? 29.021  -9.320  87.452  1.00 12.23 ? 404  TYR D CB  1 
ATOM   17294 C  CG  . TYR D 1 412 ? 28.395  -10.020 88.633  1.00 16.54 ? 404  TYR D CG  1 
ATOM   17295 C  CD1 . TYR D 1 412 ? 27.020  -10.206 88.709  1.00 12.04 ? 404  TYR D CD1 1 
ATOM   17296 C  CD2 . TYR D 1 412 ? 29.182  -10.505 89.667  1.00 13.89 ? 404  TYR D CD2 1 
ATOM   17297 C  CE1 . TYR D 1 412 ? 26.446  -10.842 89.788  1.00 17.62 ? 404  TYR D CE1 1 
ATOM   17298 C  CE2 . TYR D 1 412 ? 28.622  -11.135 90.749  1.00 14.91 ? 404  TYR D CE2 1 
ATOM   17299 C  CZ  . TYR D 1 412 ? 27.250  -11.304 90.804  1.00 17.75 ? 404  TYR D CZ  1 
ATOM   17300 O  OH  . TYR D 1 412 ? 26.688  -11.934 91.888  1.00 19.10 ? 404  TYR D OH  1 
ATOM   17301 N  N   . GLY D 1 413 ? 30.901  -9.452  84.579  1.00 15.92 ? 405  GLY D N   1 
ATOM   17302 C  CA  . GLY D 1 413 ? 31.303  -8.576  83.501  1.00 17.52 ? 405  GLY D CA  1 
ATOM   17303 C  C   . GLY D 1 413 ? 31.296  -7.134  83.984  1.00 15.24 ? 405  GLY D C   1 
ATOM   17304 O  O   . GLY D 1 413 ? 31.323  -6.851  85.184  1.00 15.07 ? 405  GLY D O   1 
ATOM   17305 N  N   . VAL D 1 414 ? 31.253  -6.207  83.027  1.00 14.93 ? 406  VAL D N   1 
ATOM   17306 C  CA  . VAL D 1 414 ? 31.403  -4.794  83.369  1.00 16.60 ? 406  VAL D CA  1 
ATOM   17307 C  C   . VAL D 1 414 ? 30.034  -4.221  83.719  1.00 16.32 ? 406  VAL D C   1 
ATOM   17308 O  O   . VAL D 1 414 ? 29.472  -3.414  82.971  1.00 12.91 ? 406  VAL D O   1 
ATOM   17309 C  CB  . VAL D 1 414 ? 32.073  -4.012  82.221  1.00 12.20 ? 406  VAL D CB  1 
ATOM   17310 C  CG1 . VAL D 1 414 ? 32.459  -2.627  82.682  1.00 15.32 ? 406  VAL D CG1 1 
ATOM   17311 C  CG2 . VAL D 1 414 ? 33.301  -4.759  81.726  1.00 19.06 ? 406  VAL D CG2 1 
ATOM   17312 N  N   . ARG D 1 415 ? 29.491  -4.628  84.873  1.00 12.96 ? 407  ARG D N   1 
ATOM   17313 C  CA  . ARG D 1 415 ? 28.073  -4.444  85.202  1.00 12.07 ? 407  ARG D CA  1 
ATOM   17314 C  C   . ARG D 1 415 ? 27.926  -4.293  86.715  1.00 11.24 ? 407  ARG D C   1 
ATOM   17315 O  O   . ARG D 1 415 ? 27.352  -5.143  87.390  1.00 14.26 ? 407  ARG D O   1 
ATOM   17316 C  CB  . ARG D 1 415 ? 27.221  -5.621  84.723  1.00 11.14 ? 407  ARG D CB  1 
ATOM   17317 C  CG  . ARG D 1 415 ? 27.281  -5.949  83.234  1.00 11.97 ? 407  ARG D CG  1 
ATOM   17318 C  CD  . ARG D 1 415 ? 26.326  -7.132  82.942  1.00 13.13 ? 407  ARG D CD  1 
ATOM   17319 N  NE  . ARG D 1 415 ? 26.267  -7.548  81.536  1.00 14.45 ? 407  ARG D NE  1 
ATOM   17320 C  CZ  . ARG D 1 415 ? 26.973  -8.550  81.008  1.00 17.06 ? 407  ARG D CZ  1 
ATOM   17321 N  NH1 . ARG D 1 415 ? 27.819  -9.248  81.751  1.00 16.94 ? 407  ARG D NH1 1 
ATOM   17322 N  NH2 . ARG D 1 415 ? 26.825  -8.870  79.731  1.00 18.03 ? 407  ARG D NH2 1 
ATOM   17323 N  N   . GLU D 1 416 ? 28.426  -3.180  87.261  1.00 10.10 ? 408  GLU D N   1 
ATOM   17324 C  CA  . GLU D 1 416 ? 28.488  -3.062  88.714  1.00 9.85  ? 408  GLU D CA  1 
ATOM   17325 C  C   . GLU D 1 416 ? 27.103  -2.921  89.333  1.00 9.82  ? 408  GLU D C   1 
ATOM   17326 O  O   . GLU D 1 416 ? 26.810  -3.546  90.360  1.00 9.64  ? 408  GLU D O   1 
ATOM   17327 C  CB  . GLU D 1 416 ? 29.378  -1.880  89.112  1.00 10.68 ? 408  GLU D CB  1 
ATOM   17328 C  CG  . GLU D 1 416 ? 30.839  -2.061  88.748  1.00 13.42 ? 408  GLU D CG  1 
ATOM   17329 C  CD  . GLU D 1 416 ? 31.144  -1.640  87.324  1.00 15.43 ? 408  GLU D CD  1 
ATOM   17330 O  OE1 . GLU D 1 416 ? 30.253  -1.041  86.680  1.00 16.51 ? 408  GLU D OE1 1 
ATOM   17331 O  OE2 . GLU D 1 416 ? 32.270  -1.907  86.849  1.00 22.54 ? 408  GLU D OE2 1 
ATOM   17332 N  N   . PHE D 1 417 ? 26.248  -2.069  88.757  1.00 12.69 ? 409  PHE D N   1 
ATOM   17333 C  CA  . PHE D 1 417 ? 24.895  -1.923  89.287  1.00 15.01 ? 409  PHE D CA  1 
ATOM   17334 C  C   . PHE D 1 417 ? 24.138  -3.239  89.173  1.00 14.01 ? 409  PHE D C   1 
ATOM   17335 O  O   . PHE D 1 417 ? 23.481  -3.681  90.124  1.00 11.53 ? 409  PHE D O   1 
ATOM   17336 C  CB  . PHE D 1 417 ? 24.150  -0.807  88.546  1.00 13.42 ? 409  PHE D CB  1 
ATOM   17337 C  CG  . PHE D 1 417 ? 22.959  -0.231  89.303  1.00 15.25 ? 409  PHE D CG  1 
ATOM   17338 C  CD1 . PHE D 1 417 ? 22.550  -0.755  90.520  1.00 9.84  ? 409  PHE D CD1 1 
ATOM   17339 C  CD2 . PHE D 1 417 ? 22.259  0.854   88.775  1.00 12.30 ? 409  PHE D CD2 1 
ATOM   17340 C  CE1 . PHE D 1 417 ? 21.456  -0.208  91.203  1.00 14.22 ? 409  PHE D CE1 1 
ATOM   17341 C  CE2 . PHE D 1 417 ? 21.171  1.412   89.443  1.00 12.23 ? 409  PHE D CE2 1 
ATOM   17342 C  CZ  . PHE D 1 417 ? 20.771  0.886   90.659  1.00 12.79 ? 409  PHE D CZ  1 
ATOM   17343 N  N   . GLY D 1 418 ? 24.224  -3.884  88.008  1.00 10.83 ? 410  GLY D N   1 
ATOM   17344 C  CA  . GLY D 1 418 ? 23.622  -5.196  87.872  1.00 13.08 ? 410  GLY D CA  1 
ATOM   17345 C  C   . GLY D 1 418 ? 24.131  -6.152  88.931  1.00 10.78 ? 410  GLY D C   1 
ATOM   17346 O  O   . GLY D 1 418 ? 23.348  -6.863  89.568  1.00 11.94 ? 410  GLY D O   1 
ATOM   17347 N  N   . MET D 1 419 ? 25.447  -6.147  89.159  1.00 10.28 ? 411  MET D N   1 
ATOM   17348 C  CA  . MET D 1 419 ? 26.036  -7.027  90.165  1.00 10.53 ? 411  MET D CA  1 
ATOM   17349 C  C   . MET D 1 419 ? 25.421  -6.786  91.539  1.00 10.28 ? 411  MET D C   1 
ATOM   17350 O  O   . MET D 1 419 ? 24.954  -7.725  92.195  1.00 13.94 ? 411  MET D O   1 
ATOM   17351 C  CB  . MET D 1 419 ? 27.552  -6.834  90.224  1.00 10.66 ? 411  MET D CB  1 
ATOM   17352 C  CG  . MET D 1 419 ? 28.200  -7.576  91.406  1.00 13.33 ? 411  MET D CG  1 
ATOM   17353 S  SD  . MET D 1 419 ? 30.010  -7.484  91.417  1.00 16.25 ? 411  MET D SD  1 
ATOM   17354 C  CE  . MET D 1 419 ? 30.273  -5.839  92.069  1.00 12.57 ? 411  MET D CE  1 
ATOM   17355 N  N   . GLY D 1 420 ? 25.423  -5.538  92.001  1.00 11.17 ? 412  GLY D N   1 
ATOM   17356 C  CA  . GLY D 1 420 ? 24.892  -5.272  93.330  1.00 9.68  ? 412  GLY D CA  1 
ATOM   17357 C  C   . GLY D 1 420 ? 23.438  -5.686  93.471  1.00 14.15 ? 412  GLY D C   1 
ATOM   17358 O  O   . GLY D 1 420 ? 23.052  -6.312  94.460  1.00 12.36 ? 412  GLY D O   1 
ATOM   17359 N  N   . ALA D 1 421 ? 22.614  -5.361  92.473  1.00 12.45 ? 413  ALA D N   1 
ATOM   17360 C  CA  . ALA D 1 421 ? 21.197  -5.690  92.579  1.00 14.64 ? 413  ALA D CA  1 
ATOM   17361 C  C   . ALA D 1 421 ? 20.943  -7.184  92.401  1.00 12.35 ? 413  ALA D C   1 
ATOM   17362 O  O   . ALA D 1 421 ? 19.982  -7.713  92.967  1.00 12.39 ? 413  ALA D O   1 
ATOM   17363 C  CB  . ALA D 1 421 ? 20.387  -4.890  91.560  1.00 13.23 ? 413  ALA D CB  1 
ATOM   17364 N  N   . ILE D 1 422 ? 21.776  -7.875  91.613  1.00 13.31 ? 414  ILE D N   1 
ATOM   17365 C  CA  . ILE D 1 422 ? 21.642  -9.324  91.494  1.00 11.51 ? 414  ILE D CA  1 
ATOM   17366 C  C   . ILE D 1 422 ? 22.023  -9.992  92.806  1.00 13.80 ? 414  ILE D C   1 
ATOM   17367 O  O   . ILE D 1 422 ? 21.380  -10.957 93.234  1.00 14.78 ? 414  ILE D O   1 
ATOM   17368 C  CB  . ILE D 1 422 ? 22.482  -9.856  90.317  1.00 12.08 ? 414  ILE D CB  1 
ATOM   17369 C  CG1 . ILE D 1 422 ? 21.863  -9.436  88.988  1.00 15.40 ? 414  ILE D CG1 1 
ATOM   17370 C  CG2 . ILE D 1 422 ? 22.615  -11.382 90.375  1.00 15.40 ? 414  ILE D CG2 1 
ATOM   17371 C  CD1 . ILE D 1 422 ? 22.722  -9.807  87.782  1.00 16.21 ? 414  ILE D CD1 1 
ATOM   17372 N  N   . MET D 1 423 ? 23.066  -9.478  93.466  1.00 11.98 ? 415  MET D N   1 
ATOM   17373 C  CA  . MET D 1 423 ? 23.493  -10.016 94.758  1.00 13.70 ? 415  MET D CA  1 
ATOM   17374 C  C   . MET D 1 423 ? 22.393  -9.889  95.799  1.00 11.19 ? 415  MET D C   1 
ATOM   17375 O  O   . MET D 1 423 ? 22.216  -10.782 96.641  1.00 11.62 ? 415  MET D O   1 
ATOM   17376 C  CB  . MET D 1 423 ? 24.746  -9.289  95.251  1.00 11.76 ? 415  MET D CB  1 
ATOM   17377 C  CG  . MET D 1 423 ? 26.043  -9.700  94.576  1.00 17.36 ? 415  MET D CG  1 
ATOM   17378 S  SD  . MET D 1 423 ? 27.420  -8.636  95.128  1.00 25.96 ? 415  MET D SD  1 
ATOM   17379 C  CE  . MET D 1 423 ? 27.395  -8.865  96.907  1.00 27.49 ? 415  MET D CE  1 
ATOM   17380 N  N   . ASN D 1 424 ? 21.661  -8.773  95.778  1.00 14.35 ? 416  ASN D N   1 
ATOM   17381 C  CA  . ASN D 1 424 ? 20.522  -8.642  96.682  1.00 14.35 ? 416  ASN D CA  1 
ATOM   17382 C  C   . ASN D 1 424 ? 19.529  -9.781  96.463  1.00 14.64 ? 416  ASN D C   1 
ATOM   17383 O  O   . ASN D 1 424 ? 19.004  -10.351 97.423  1.00 13.51 ? 416  ASN D O   1 
ATOM   17384 C  CB  . ASN D 1 424 ? 19.846  -7.277  96.496  1.00 10.15 ? 416  ASN D CB  1 
ATOM   17385 C  CG  . ASN D 1 424 ? 20.705  -6.114  96.988  1.00 16.18 ? 416  ASN D CG  1 
ATOM   17386 O  OD1 . ASN D 1 424 ? 21.724  -6.314  97.646  1.00 14.57 ? 416  ASN D OD1 1 
ATOM   17387 N  ND2 . ASN D 1 424 ? 20.285  -4.888  96.672  1.00 13.21 ? 416  ASN D ND2 1 
ATOM   17388 N  N   . GLY D 1 425 ? 19.292  -10.149 95.204  1.00 15.23 ? 417  GLY D N   1 
ATOM   17389 C  CA  . GLY D 1 425 ? 18.368  -11.234 94.920  1.00 15.50 ? 417  GLY D CA  1 
ATOM   17390 C  C   . GLY D 1 425 ? 18.926  -12.598 95.282  1.00 13.46 ? 417  GLY D C   1 
ATOM   17391 O  O   . GLY D 1 425 ? 18.184  -13.476 95.733  1.00 13.63 ? 417  GLY D O   1 
ATOM   17392 N  N   . LEU D 1 426 ? 20.236  -12.802 95.080  1.00 12.32 ? 418  LEU D N   1 
ATOM   17393 C  CA  . LEU D 1 426 ? 20.857  -14.048 95.531  1.00 12.99 ? 418  LEU D CA  1 
ATOM   17394 C  C   . LEU D 1 426 ? 20.660  -14.241 97.027  1.00 13.21 ? 418  LEU D C   1 
ATOM   17395 O  O   . LEU D 1 426 ? 20.352  -15.351 97.485  1.00 15.39 ? 418  LEU D O   1 
ATOM   17396 C  CB  . LEU D 1 426 ? 22.353  -14.059 95.206  1.00 13.09 ? 418  LEU D CB  1 
ATOM   17397 C  CG  . LEU D 1 426 ? 22.803  -14.205 93.753  1.00 15.36 ? 418  LEU D CG  1 
ATOM   17398 C  CD1 . LEU D 1 426 ? 24.294  -13.868 93.638  1.00 16.31 ? 418  LEU D CD1 1 
ATOM   17399 C  CD2 . LEU D 1 426 ? 22.515  -15.641 93.266  1.00 15.15 ? 418  LEU D CD2 1 
ATOM   17400 N  N   . VAL D 1 427 ? 20.866  -13.172 97.801  1.00 14.38 ? 419  VAL D N   1 
ATOM   17401 C  CA  . VAL D 1 427 ? 20.712  -13.235 99.255  1.00 19.34 ? 419  VAL D CA  1 
ATOM   17402 C  C   . VAL D 1 427 ? 19.266  -13.504 99.628  1.00 15.70 ? 419  VAL D C   1 
ATOM   17403 O  O   . VAL D 1 427 ? 18.979  -14.314 100.513 1.00 15.97 ? 419  VAL D O   1 
ATOM   17404 C  CB  . VAL D 1 427 ? 21.189  -11.924 99.910  1.00 21.76 ? 419  VAL D CB  1 
ATOM   17405 C  CG1 . VAL D 1 427 ? 20.811  -11.909 101.391 1.00 23.49 ? 419  VAL D CG1 1 
ATOM   17406 C  CG2 . VAL D 1 427 ? 22.654  -11.751 99.745  1.00 30.42 ? 419  VAL D CG2 1 
ATOM   17407 N  N   . LEU D 1 428 ? 18.340  -12.773 99.008  1.00 15.05 ? 420  LEU D N   1 
ATOM   17408 C  CA  . LEU D 1 428 ? 16.935  -12.889 99.379  1.00 12.77 ? 420  LEU D CA  1 
ATOM   17409 C  C   . LEU D 1 428 ? 16.418  -14.292 99.123  1.00 17.53 ? 420  LEU D C   1 
ATOM   17410 O  O   . LEU D 1 428 ? 15.520  -14.762 99.826  1.00 22.56 ? 420  LEU D O   1 
ATOM   17411 C  CB  . LEU D 1 428 ? 16.093  -11.870 98.596  1.00 12.76 ? 420  LEU D CB  1 
ATOM   17412 C  CG  . LEU D 1 428 ? 16.165  -10.409 99.054  1.00 16.26 ? 420  LEU D CG  1 
ATOM   17413 C  CD1 . LEU D 1 428 ? 15.634  -9.451  97.991  1.00 17.19 ? 420  LEU D CD1 1 
ATOM   17414 C  CD2 . LEU D 1 428 ? 15.401  -10.220 100.346 1.00 12.91 ? 420  LEU D CD2 1 
ATOM   17415 N  N   . HIS D 1 429 ? 16.981  -14.977 98.129  1.00 16.60 ? 421  HIS D N   1 
ATOM   17416 C  CA  . HIS D 1 429 ? 16.479  -16.296 97.778  1.00 14.28 ? 421  HIS D CA  1 
ATOM   17417 C  C   . HIS D 1 429 ? 16.683  -17.289 98.915  1.00 15.02 ? 421  HIS D C   1 
ATOM   17418 O  O   . HIS D 1 429 ? 15.813  -18.128 99.174  1.00 16.01 ? 421  HIS D O   1 
ATOM   17419 C  CB  . HIS D 1 429 ? 17.164  -16.808 96.513  1.00 20.99 ? 421  HIS D CB  1 
ATOM   17420 C  CG  . HIS D 1 429 ? 16.656  -18.143 96.066  1.00 15.16 ? 421  HIS D CG  1 
ATOM   17421 N  ND1 . HIS D 1 429 ? 17.120  -19.333 96.586  1.00 15.95 ? 421  HIS D ND1 1 
ATOM   17422 C  CD2 . HIS D 1 429 ? 15.706  -18.472 95.159  1.00 16.12 ? 421  HIS D CD2 1 
ATOM   17423 C  CE1 . HIS D 1 429 ? 16.476  -20.338 96.015  1.00 22.02 ? 421  HIS D CE1 1 
ATOM   17424 N  NE2 . HIS D 1 429 ? 15.615  -19.841 95.143  1.00 17.01 ? 421  HIS D NE2 1 
ATOM   17425 N  N   . GLY D 1 430 ? 17.808  -17.192 99.613  1.00 17.41 ? 422  GLY D N   1 
ATOM   17426 C  CA  . GLY D 1 430 ? 18.244  -18.201 100.570 1.00 15.91 ? 422  GLY D CA  1 
ATOM   17427 C  C   . GLY D 1 430 ? 19.112  -19.260 99.921  1.00 22.23 ? 422  GLY D C   1 
ATOM   17428 O  O   . GLY D 1 430 ? 19.022  -19.537 98.724  1.00 21.41 ? 422  GLY D O   1 
ATOM   17429 N  N   . GLY D 1 431 ? 19.988  -19.857 100.731 1.00 18.71 ? 423  GLY D N   1 
ATOM   17430 C  CA  . GLY D 1 431 ? 20.800  -20.983 100.316 1.00 17.84 ? 423  GLY D CA  1 
ATOM   17431 C  C   . GLY D 1 431 ? 22.215  -20.648 99.878  1.00 17.66 ? 423  GLY D C   1 
ATOM   17432 O  O   . GLY D 1 431 ? 23.051  -21.561 99.788  1.00 21.19 ? 423  GLY D O   1 
ATOM   17433 N  N   . VAL D 1 432 ? 22.504  -19.386 99.571  1.00 20.87 ? 424  VAL D N   1 
ATOM   17434 C  CA  . VAL D 1 432 ? 23.847  -18.965 99.192  1.00 21.59 ? 424  VAL D CA  1 
ATOM   17435 C  C   . VAL D 1 432 ? 24.198  -17.695 99.946  1.00 20.89 ? 424  VAL D C   1 
ATOM   17436 O  O   . VAL D 1 432 ? 23.326  -16.938 100.383 1.00 18.71 ? 424  VAL D O   1 
ATOM   17437 C  CB  . VAL D 1 432 ? 24.012  -18.730 97.670  1.00 18.18 ? 424  VAL D CB  1 
ATOM   17438 C  CG1 . VAL D 1 432 ? 23.791  -20.034 96.889  1.00 18.44 ? 424  VAL D CG1 1 
ATOM   17439 C  CG2 . VAL D 1 432 ? 23.087  -17.623 97.178  1.00 20.93 ? 424  VAL D CG2 1 
ATOM   17440 N  N   . LYS D 1 433 ? 25.502  -17.480 100.105 1.00 17.68 ? 425  LYS D N   1 
ATOM   17441 C  CA  A LYS D 1 433 ? 26.041  -16.263 100.714 0.63 19.33 ? 425  LYS D CA  1 
ATOM   17442 C  CA  B LYS D 1 433 ? 26.035  -16.258 100.710 0.37 18.79 ? 425  LYS D CA  1 
ATOM   17443 C  C   . LYS D 1 433 ? 26.970  -15.600 99.708  1.00 18.50 ? 425  LYS D C   1 
ATOM   17444 O  O   . LYS D 1 433 ? 28.123  -16.041 99.542  1.00 18.61 ? 425  LYS D O   1 
ATOM   17445 C  CB  A LYS D 1 433 ? 26.786  -16.578 102.012 0.63 17.08 ? 425  LYS D CB  1 
ATOM   17446 C  CB  B LYS D 1 433 ? 26.763  -16.551 102.022 0.37 17.77 ? 425  LYS D CB  1 
ATOM   17447 C  CG  A LYS D 1 433 ? 27.319  -15.346 102.727 0.63 15.73 ? 425  LYS D CG  1 
ATOM   17448 C  CG  B LYS D 1 433 ? 25.825  -16.895 103.172 0.37 17.86 ? 425  LYS D CG  1 
ATOM   17449 C  CD  A LYS D 1 433 ? 27.817  -15.651 104.138 0.63 16.76 ? 425  LYS D CD  1 
ATOM   17450 C  CD  B LYS D 1 433 ? 26.548  -16.941 104.516 0.37 17.61 ? 425  LYS D CD  1 
ATOM   17451 C  CE  A LYS D 1 433 ? 26.663  -15.939 105.092 0.63 19.16 ? 425  LYS D CE  1 
ATOM   17452 C  CE  B LYS D 1 433 ? 26.932  -15.545 104.994 0.37 18.82 ? 425  LYS D CE  1 
ATOM   17453 N  NZ  A LYS D 1 433 ? 25.643  -14.849 105.045 0.63 19.21 ? 425  LYS D NZ  1 
ATOM   17454 N  NZ  B LYS D 1 433 ? 25.750  -14.632 105.059 0.37 18.64 ? 425  LYS D NZ  1 
ATOM   17455 N  N   . PRO D 1 434 ? 26.529  -14.564 99.016  1.00 17.50 ? 426  PRO D N   1 
ATOM   17456 C  CA  . PRO D 1 434 ? 27.352  -14.005 97.943  1.00 17.29 ? 426  PRO D CA  1 
ATOM   17457 C  C   . PRO D 1 434 ? 28.196  -12.822 98.375  1.00 17.49 ? 426  PRO D C   1 
ATOM   17458 O  O   . PRO D 1 434 ? 27.817  -12.042 99.256  1.00 18.71 ? 426  PRO D O   1 
ATOM   17459 C  CB  . PRO D 1 434 ? 26.304  -13.577 96.904  1.00 18.02 ? 426  PRO D CB  1 
ATOM   17460 C  CG  . PRO D 1 434 ? 25.187  -13.065 97.763  1.00 19.82 ? 426  PRO D CG  1 
ATOM   17461 C  CD  . PRO D 1 434 ? 25.187  -13.963 99.028  1.00 19.23 ? 426  PRO D CD  1 
ATOM   17462 N  N   . PHE D 1 435 ? 29.347  -12.683 97.737  1.00 17.77 ? 427  PHE D N   1 
ATOM   17463 C  CA  . PHE D 1 435 ? 30.078  -11.431 97.720  1.00 13.18 ? 427  PHE D CA  1 
ATOM   17464 C  C   . PHE D 1 435 ? 30.295  -11.038 96.265  1.00 19.79 ? 427  PHE D C   1 
ATOM   17465 O  O   . PHE D 1 435 ? 30.239  -11.874 95.358  1.00 16.48 ? 427  PHE D O   1 
ATOM   17466 C  CB  . PHE D 1 435 ? 31.417  -11.517 98.505  1.00 14.60 ? 427  PHE D CB  1 
ATOM   17467 C  CG  . PHE D 1 435 ? 32.498  -12.393 97.868  1.00 17.60 ? 427  PHE D CG  1 
ATOM   17468 C  CD1 . PHE D 1 435 ? 33.338  -11.890 96.880  1.00 17.22 ? 427  PHE D CD1 1 
ATOM   17469 C  CD2 . PHE D 1 435 ? 32.724  -13.687 98.327  1.00 19.16 ? 427  PHE D CD2 1 
ATOM   17470 C  CE1 . PHE D 1 435 ? 34.353  -12.686 96.328  1.00 16.88 ? 427  PHE D CE1 1 
ATOM   17471 C  CE2 . PHE D 1 435 ? 33.741  -14.483 97.784  1.00 19.05 ? 427  PHE D CE2 1 
ATOM   17472 C  CZ  . PHE D 1 435 ? 34.549  -13.980 96.786  1.00 17.85 ? 427  PHE D CZ  1 
ATOM   17473 N  N   . GLY D 1 436 ? 30.507  -9.747  96.048  1.00 15.16 ? 428  GLY D N   1 
ATOM   17474 C  CA  . GLY D 1 436 ? 30.785  -9.245  94.717  1.00 14.30 ? 428  GLY D CA  1 
ATOM   17475 C  C   . GLY D 1 436 ? 31.746  -8.075  94.768  1.00 14.28 ? 428  GLY D C   1 
ATOM   17476 O  O   . GLY D 1 436 ? 31.530  -7.120  95.516  1.00 13.92 ? 428  GLY D O   1 
ATOM   17477 N  N   . ALA D 1 437 ? 32.808  -8.124  93.980  1.00 13.64 ? 429  ALA D N   1 
ATOM   17478 C  CA  . ALA D 1 437 ? 33.876  -7.144  94.091  1.00 15.24 ? 429  ALA D CA  1 
ATOM   17479 C  C   . ALA D 1 437 ? 33.943  -6.236  92.868  1.00 14.86 ? 429  ALA D C   1 
ATOM   17480 O  O   . ALA D 1 437 ? 33.699  -6.671  91.735  1.00 14.24 ? 429  ALA D O   1 
ATOM   17481 C  CB  . ALA D 1 437 ? 35.224  -7.833  94.284  1.00 12.58 ? 429  ALA D CB  1 
ATOM   17482 N  N   . THR D 1 438 ? 34.286  -4.973  93.114  1.00 15.63 ? 430  THR D N   1 
ATOM   17483 C  CA  . THR D 1 438 ? 34.694  -4.034  92.077  1.00 14.74 ? 430  THR D CA  1 
ATOM   17484 C  C   . THR D 1 438 ? 35.691  -3.064  92.709  1.00 15.10 ? 430  THR D C   1 
ATOM   17485 O  O   . THR D 1 438 ? 36.036  -3.197  93.886  1.00 14.38 ? 430  THR D O   1 
ATOM   17486 C  CB  . THR D 1 438 ? 33.476  -3.340  91.454  1.00 17.46 ? 430  THR D CB  1 
ATOM   17487 O  OG1 . THR D 1 438 ? 33.902  -2.458  90.409  1.00 14.70 ? 430  THR D OG1 1 
ATOM   17488 C  CG2 . THR D 1 438 ? 32.689  -2.563  92.499  1.00 10.17 ? 430  THR D CG2 1 
ATOM   17489 N  N   . PHE D 1 439 ? 36.198  -2.118  91.916  1.00 12.88 ? 431  PHE D N   1 
ATOM   17490 C  CA  . PHE D 1 439 ? 36.999  -1.036  92.479  1.00 13.54 ? 431  PHE D CA  1 
ATOM   17491 C  C   . PHE D 1 439 ? 36.130  -0.168  93.380  1.00 12.35 ? 431  PHE D C   1 
ATOM   17492 O  O   . PHE D 1 439 ? 34.937  0.013   93.130  1.00 14.54 ? 431  PHE D O   1 
ATOM   17493 C  CB  . PHE D 1 439 ? 37.596  -0.133  91.391  1.00 10.91 ? 431  PHE D CB  1 
ATOM   17494 C  CG  . PHE D 1 439 ? 38.739  -0.740  90.610  1.00 22.12 ? 431  PHE D CG  1 
ATOM   17495 C  CD1 . PHE D 1 439 ? 39.045  -2.084  90.683  1.00 23.71 ? 431  PHE D CD1 1 
ATOM   17496 C  CD2 . PHE D 1 439 ? 39.532  0.075   89.812  1.00 32.27 ? 431  PHE D CD2 1 
ATOM   17497 C  CE1 . PHE D 1 439 ? 40.107  -2.609  89.952  1.00 25.51 ? 431  PHE D CE1 1 
ATOM   17498 C  CE2 . PHE D 1 439 ? 40.594  -0.441  89.090  1.00 31.00 ? 431  PHE D CE2 1 
ATOM   17499 C  CZ  . PHE D 1 439 ? 40.880  -1.784  89.160  1.00 24.09 ? 431  PHE D CZ  1 
ATOM   17500 N  N   . LEU D 1 440 ? 36.746  0.405   94.425  1.00 12.42 ? 432  LEU D N   1 
ATOM   17501 C  CA  . LEU D 1 440 ? 35.978  1.237   95.354  1.00 10.14 ? 432  LEU D CA  1 
ATOM   17502 C  C   . LEU D 1 440 ? 35.262  2.374   94.635  1.00 13.60 ? 432  LEU D C   1 
ATOM   17503 O  O   . LEU D 1 440 ? 34.125  2.724   94.985  1.00 10.17 ? 432  LEU D O   1 
ATOM   17504 C  CB  . LEU D 1 440 ? 36.893  1.795   96.454  1.00 10.35 ? 432  LEU D CB  1 
ATOM   17505 C  CG  . LEU D 1 440 ? 36.184  2.682   97.491  1.00 10.99 ? 432  LEU D CG  1 
ATOM   17506 C  CD1 . LEU D 1 440 ? 35.010  1.967   98.151  1.00 17.70 ? 432  LEU D CD1 1 
ATOM   17507 C  CD2 . LEU D 1 440 ? 37.178  3.171   98.567  1.00 12.39 ? 432  LEU D CD2 1 
ATOM   17508 N  N   . MET D 1 441 ? 35.902  2.959   93.620  1.00 12.40 ? 433  MET D N   1 
ATOM   17509 C  CA  . MET D 1 441 ? 35.269  4.064   92.905  1.00 14.39 ? 433  MET D CA  1 
ATOM   17510 C  C   . MET D 1 441 ? 33.905  3.660   92.365  1.00 14.94 ? 433  MET D C   1 
ATOM   17511 O  O   . MET D 1 441 ? 32.961  4.454   92.382  1.00 14.11 ? 433  MET D O   1 
ATOM   17512 C  CB  . MET D 1 441 ? 36.148  4.543   91.753  1.00 12.33 ? 433  MET D CB  1 
ATOM   17513 C  CG  . MET D 1 441 ? 35.518  5.754   91.024  1.00 12.96 ? 433  MET D CG  1 
ATOM   17514 S  SD  . MET D 1 441 ? 35.341  7.176   92.124  1.00 15.02 ? 433  MET D SD  1 
ATOM   17515 C  CE  . MET D 1 441 ? 37.062  7.590   92.454  1.00 12.02 ? 433  MET D CE  1 
ATOM   17516 N  N   . PHE D 1 442 ? 33.774  2.423   91.905  1.00 12.75 ? 434  PHE D N   1 
ATOM   17517 C  CA  . PHE D 1 442 ? 32.565  2.003   91.222  1.00 12.24 ? 434  PHE D CA  1 
ATOM   17518 C  C   . PHE D 1 442 ? 31.519  1.465   92.178  1.00 14.52 ? 434  PHE D C   1 
ATOM   17519 O  O   . PHE D 1 442 ? 30.479  0.965   91.732  1.00 13.84 ? 434  PHE D O   1 
ATOM   17520 C  CB  . PHE D 1 442 ? 32.939  1.014   90.112  1.00 14.00 ? 434  PHE D CB  1 
ATOM   17521 C  CG  . PHE D 1 442 ? 34.025  1.549   89.222  1.00 20.81 ? 434  PHE D CG  1 
ATOM   17522 C  CD1 . PHE D 1 442 ? 33.997  2.878   88.817  1.00 24.21 ? 434  PHE D CD1 1 
ATOM   17523 C  CD2 . PHE D 1 442 ? 35.106  0.770   88.855  1.00 21.81 ? 434  PHE D CD2 1 
ATOM   17524 C  CE1 . PHE D 1 442 ? 35.013  3.405   88.029  1.00 28.04 ? 434  PHE D CE1 1 
ATOM   17525 C  CE2 . PHE D 1 442 ? 36.117  1.290   88.067  1.00 23.84 ? 434  PHE D CE2 1 
ATOM   17526 C  CZ  . PHE D 1 442 ? 36.075  2.606   87.658  1.00 21.96 ? 434  PHE D CZ  1 
ATOM   17527 N  N   . SER D 1 443 ? 31.745  1.607   93.490  1.00 14.57 ? 435  SER D N   1 
ATOM   17528 C  CA  . SER D 1 443 ? 30.617  1.646   94.408  1.00 12.53 ? 435  SER D CA  1 
ATOM   17529 C  C   . SER D 1 443 ? 29.597  2.670   93.935  1.00 13.86 ? 435  SER D C   1 
ATOM   17530 O  O   . SER D 1 443 ? 28.399  2.509   94.173  1.00 14.33 ? 435  SER D O   1 
ATOM   17531 C  CB  . SER D 1 443 ? 31.077  1.992   95.837  1.00 11.51 ? 435  SER D CB  1 
ATOM   17532 O  OG  . SER D 1 443 ? 31.682  3.281   95.888  1.00 11.33 ? 435  SER D OG  1 
ATOM   17533 N  N   . GLU D 1 444 ? 30.054  3.719   93.246  1.00 9.60  ? 436  GLU D N   1 
ATOM   17534 C  CA  . GLU D 1 444 ? 29.142  4.764   92.796  1.00 11.59 ? 436  GLU D CA  1 
ATOM   17535 C  C   . GLU D 1 444 ? 28.268  4.296   91.639  1.00 12.77 ? 436  GLU D C   1 
ATOM   17536 O  O   . GLU D 1 444 ? 27.184  4.846   91.436  1.00 15.91 ? 436  GLU D O   1 
ATOM   17537 C  CB  . GLU D 1 444 ? 29.934  6.013   92.407  1.00 13.57 ? 436  GLU D CB  1 
ATOM   17538 C  CG  . GLU D 1 444 ? 30.650  6.634   93.617  1.00 8.69  ? 436  GLU D CG  1 
ATOM   17539 C  CD  . GLU D 1 444 ? 31.124  8.049   93.379  1.00 13.60 ? 436  GLU D CD  1 
ATOM   17540 O  OE1 . GLU D 1 444 ? 31.172  8.497   92.208  1.00 15.84 ? 436  GLU D OE1 1 
ATOM   17541 O  OE2 . GLU D 1 444 ? 31.444  8.728   94.379  1.00 16.01 ? 436  GLU D OE2 1 
ATOM   17542 N  N   . TYR D 1 445 ? 28.718  3.305   90.862  1.00 12.12 ? 437  TYR D N   1 
ATOM   17543 C  CA  . TYR D 1 445 ? 27.850  2.739   89.826  1.00 12.86 ? 437  TYR D CA  1 
ATOM   17544 C  C   . TYR D 1 445 ? 26.751  1.866   90.425  1.00 15.15 ? 437  TYR D C   1 
ATOM   17545 O  O   . TYR D 1 445 ? 25.668  1.751   89.845  1.00 19.74 ? 437  TYR D O   1 
ATOM   17546 C  CB  . TYR D 1 445 ? 28.666  1.919   88.820  1.00 8.92  ? 437  TYR D CB  1 
ATOM   17547 C  CG  . TYR D 1 445 ? 29.332  2.715   87.704  1.00 11.53 ? 437  TYR D CG  1 
ATOM   17548 C  CD1 . TYR D 1 445 ? 30.040  3.884   87.971  1.00 15.87 ? 437  TYR D CD1 1 
ATOM   17549 C  CD2 . TYR D 1 445 ? 29.269  2.274   86.378  1.00 11.49 ? 437  TYR D CD2 1 
ATOM   17550 C  CE1 . TYR D 1 445 ? 30.662  4.600   86.935  1.00 16.73 ? 437  TYR D CE1 1 
ATOM   17551 C  CE2 . TYR D 1 445 ? 29.870  2.971   85.353  1.00 11.04 ? 437  TYR D CE2 1 
ATOM   17552 C  CZ  . TYR D 1 445 ? 30.580  4.130   85.636  1.00 13.30 ? 437  TYR D CZ  1 
ATOM   17553 O  OH  . TYR D 1 445 ? 31.203  4.826   84.617  1.00 13.44 ? 437  TYR D OH  1 
ATOM   17554 N  N   . GLU D 1 446 ? 27.001  1.239   91.571  1.00 11.78 ? 438  GLU D N   1 
ATOM   17555 C  CA  . GLU D 1 446 ? 26.024  0.346   92.180  1.00 10.74 ? 438  GLU D CA  1 
ATOM   17556 C  C   . GLU D 1 446 ? 25.436  0.936   93.455  1.00 11.77 ? 438  GLU D C   1 
ATOM   17557 O  O   . GLU D 1 446 ? 24.897  0.199   94.280  1.00 13.82 ? 438  GLU D O   1 
ATOM   17558 C  CB  . GLU D 1 446 ? 26.661  -1.016  92.475  1.00 17.57 ? 438  GLU D CB  1 
ATOM   17559 C  CG  . GLU D 1 446 ? 27.925  -0.947  93.348  1.00 16.85 ? 438  GLU D CG  1 
ATOM   17560 C  CD  . GLU D 1 446 ? 28.417  -2.321  93.814  1.00 18.51 ? 438  GLU D CD  1 
ATOM   17561 O  OE1 . GLU D 1 446 ? 27.686  -3.316  93.671  1.00 15.53 ? 438  GLU D OE1 1 
ATOM   17562 O  OE2 . GLU D 1 446 ? 29.540  -2.403  94.354  1.00 14.83 ? 438  GLU D OE2 1 
ATOM   17563 N  N   . ARG D 1 447 ? 25.524  2.255   93.620  1.00 11.62 ? 439  ARG D N   1 
ATOM   17564 C  CA  . ARG D 1 447 ? 25.329  2.858   94.941  1.00 17.18 ? 439  ARG D CA  1 
ATOM   17565 C  C   . ARG D 1 447 ? 23.957  2.533   95.525  1.00 11.37 ? 439  ARG D C   1 
ATOM   17566 O  O   . ARG D 1 447 ? 23.849  2.165   96.703  1.00 12.30 ? 439  ARG D O   1 
ATOM   17567 C  CB  . ARG D 1 447 ? 25.532  4.373   94.864  1.00 12.60 ? 439  ARG D CB  1 
ATOM   17568 C  CG  . ARG D 1 447 ? 25.218  5.103   96.182  1.00 13.15 ? 439  ARG D CG  1 
ATOM   17569 C  CD  . ARG D 1 447 ? 26.067  4.604   97.334  1.00 11.76 ? 439  ARG D CD  1 
ATOM   17570 N  NE  . ARG D 1 447 ? 25.743  5.323   98.566  1.00 11.64 ? 439  ARG D NE  1 
ATOM   17571 C  CZ  . ARG D 1 447 ? 26.632  5.955   99.337  1.00 14.21 ? 439  ARG D CZ  1 
ATOM   17572 N  NH1 . ARG D 1 447 ? 27.931  5.937   99.032  1.00 13.19 ? 439  ARG D NH1 1 
ATOM   17573 N  NH2 . ARG D 1 447 ? 26.222  6.594   100.420 1.00 10.92 ? 439  ARG D NH2 1 
ATOM   17574 N  N   . ASN D 1 448 ? 22.888  2.679   94.730  1.00 10.17 ? 440  ASN D N   1 
ATOM   17575 C  CA  . ASN D 1 448 ? 21.567  2.489   95.322  1.00 9.29  ? 440  ASN D CA  1 
ATOM   17576 C  C   . ASN D 1 448 ? 21.274  1.028   95.617  1.00 8.76  ? 440  ASN D C   1 
ATOM   17577 O  O   . ASN D 1 448 ? 20.424  0.751   96.465  1.00 8.83  ? 440  ASN D O   1 
ATOM   17578 C  CB  . ASN D 1 448 ? 20.467  3.065   94.425  1.00 12.91 ? 440  ASN D CB  1 
ATOM   17579 C  CG  . ASN D 1 448 ? 19.166  3.295   95.185  1.00 10.57 ? 440  ASN D CG  1 
ATOM   17580 O  OD1 . ASN D 1 448 ? 18.166  2.636   94.931  1.00 12.51 ? 440  ASN D OD1 1 
ATOM   17581 N  ND2 . ASN D 1 448 ? 19.187  4.222   96.129  1.00 14.38 ? 440  ASN D ND2 1 
ATOM   17582 N  N   . ALA D 1 449 ? 21.959  0.088   94.946  1.00 9.45  ? 441  ALA D N   1 
ATOM   17583 C  CA  . ALA D 1 449 ? 21.826  -1.322  95.317  1.00 12.92 ? 441  ALA D CA  1 
ATOM   17584 C  C   . ALA D 1 449 ? 22.411  -1.582  96.700  1.00 11.59 ? 441  ALA D C   1 
ATOM   17585 O  O   . ALA D 1 449 ? 21.894  -2.415  97.454  1.00 10.41 ? 441  ALA D O   1 
ATOM   17586 C  CB  . ALA D 1 449 ? 22.502  -2.222  94.282  1.00 13.20 ? 441  ALA D CB  1 
ATOM   17587 N  N   . LEU D 1 450 ? 23.512  -0.906  97.037  1.00 12.13 ? 442  LEU D N   1 
ATOM   17588 C  CA  . LEU D 1 450 ? 24.037  -1.009  98.396  1.00 11.72 ? 442  LEU D CA  1 
ATOM   17589 C  C   . LEU D 1 450 ? 23.041  -0.451  99.395  1.00 12.02 ? 442  LEU D C   1 
ATOM   17590 O  O   . LEU D 1 450 ? 22.818  -1.037  100.459 1.00 13.34 ? 442  LEU D O   1 
ATOM   17591 C  CB  . LEU D 1 450 ? 25.362  -0.251  98.516  1.00 9.51  ? 442  LEU D CB  1 
ATOM   17592 C  CG  . LEU D 1 450 ? 26.734  -0.812  98.124  1.00 22.58 ? 442  LEU D CG  1 
ATOM   17593 C  CD1 . LEU D 1 450 ? 26.741  -1.563  96.833  1.00 11.76 ? 442  LEU D CD1 1 
ATOM   17594 C  CD2 . LEU D 1 450 ? 27.701  0.368   98.008  1.00 21.80 ? 442  LEU D CD2 1 
ATOM   17595 N  N   . ARG D 1 451 ? 22.457  0.708   99.081  1.00 11.24 ? 443  ARG D N   1 
ATOM   17596 C  CA  . ARG D 1 451 ? 21.460  1.295   99.970  1.00 8.57  ? 443  ARG D CA  1 
ATOM   17597 C  C   . ARG D 1 451 ? 20.254  0.376   100.122 1.00 8.72  ? 443  ARG D C   1 
ATOM   17598 O  O   . ARG D 1 451 ? 19.709  0.228   101.220 1.00 9.61  ? 443  ARG D O   1 
ATOM   17599 C  CB  . ARG D 1 451 ? 21.008  2.658   99.447  1.00 10.50 ? 443  ARG D CB  1 
ATOM   17600 C  CG  . ARG D 1 451 ? 20.195  3.428   100.465 1.00 11.18 ? 443  ARG D CG  1 
ATOM   17601 C  CD  . ARG D 1 451 ? 19.676  4.752   99.914  1.00 11.42 ? 443  ARG D CD  1 
ATOM   17602 N  NE  . ARG D 1 451 ? 19.260  5.653   100.992 1.00 9.83  ? 443  ARG D NE  1 
ATOM   17603 C  CZ  . ARG D 1 451 ? 18.021  5.792   101.451 1.00 13.47 ? 443  ARG D CZ  1 
ATOM   17604 N  NH1 . ARG D 1 451 ? 17.019  5.090   100.940 1.00 12.31 ? 443  ARG D NH1 1 
ATOM   17605 N  NH2 . ARG D 1 451 ? 17.787  6.650   102.431 1.00 12.10 ? 443  ARG D NH2 1 
ATOM   17606 N  N   . MET D 1 452 ? 19.831  -0.265  99.031  1.00 11.47 ? 444  MET D N   1 
ATOM   17607 C  CA  . MET D 1 452 ? 18.652  -1.125  99.112  1.00 8.84  ? 444  MET D CA  1 
ATOM   17608 C  C   . MET D 1 452 ? 18.903  -2.374  99.956  1.00 9.60  ? 444  MET D C   1 
ATOM   17609 O  O   . MET D 1 452 ? 17.986  -2.845  100.644 1.00 14.77 ? 444  MET D O   1 
ATOM   17610 C  CB  . MET D 1 452 ? 18.194  -1.502  97.705  1.00 8.75  ? 444  MET D CB  1 
ATOM   17611 C  CG  . MET D 1 452 ? 17.547  -0.352  96.948  1.00 12.86 ? 444  MET D CG  1 
ATOM   17612 S  SD  . MET D 1 452 ? 16.046  0.340   97.729  1.00 14.51 ? 444  MET D SD  1 
ATOM   17613 C  CE  . MET D 1 452 ? 14.887  -0.996  97.494  1.00 17.41 ? 444  MET D CE  1 
ATOM   17614 N  N   . ALA D 1 453 ? 20.118  -2.935  99.911  1.00 13.93 ? 445  ALA D N   1 
ATOM   17615 C  CA  . ALA D 1 453 ? 20.451  -4.051  100.795 1.00 12.27 ? 445  ALA D CA  1 
ATOM   17616 C  C   . ALA D 1 453 ? 20.347  -3.638  102.256 1.00 11.22 ? 445  ALA D C   1 
ATOM   17617 O  O   . ALA D 1 453 ? 19.830  -4.392  103.094 1.00 13.52 ? 445  ALA D O   1 
ATOM   17618 C  CB  . ALA D 1 453 ? 21.868  -4.564  100.502 1.00 11.95 ? 445  ALA D CB  1 
ATOM   17619 N  N   . ALA D 1 454 ? 20.855  -2.447  102.576 1.00 9.76  ? 446  ALA D N   1 
ATOM   17620 C  CA  . ALA D 1 454 ? 20.776  -1.926  103.935 1.00 12.79 ? 446  ALA D CA  1 
ATOM   17621 C  C   . ALA D 1 454 ? 19.333  -1.681  104.338 1.00 13.06 ? 446  ALA D C   1 
ATOM   17622 O  O   . ALA D 1 454 ? 18.942  -1.986  105.469 1.00 13.78 ? 446  ALA D O   1 
ATOM   17623 C  CB  . ALA D 1 454 ? 21.582  -0.632  104.050 1.00 12.66 ? 446  ALA D CB  1 
ATOM   17624 N  N   . LEU D 1 455 ? 18.529  -1.140  103.416 1.00 13.16 ? 447  LEU D N   1 
ATOM   17625 C  CA  . LEU D 1 455 ? 17.113  -0.898  103.705 1.00 9.78  ? 447  LEU D CA  1 
ATOM   17626 C  C   . LEU D 1 455 ? 16.354  -2.198  103.912 1.00 12.20 ? 447  LEU D C   1 
ATOM   17627 O  O   . LEU D 1 455 ? 15.532  -2.296  104.827 1.00 13.46 ? 447  LEU D O   1 
ATOM   17628 C  CB  . LEU D 1 455 ? 16.480  -0.067  102.587 1.00 9.84  ? 447  LEU D CB  1 
ATOM   17629 C  CG  . LEU D 1 455 ? 14.967  0.219   102.663 1.00 18.30 ? 447  LEU D CG  1 
ATOM   17630 C  CD1 . LEU D 1 455 ? 14.557  0.751   104.030 1.00 22.85 ? 447  LEU D CD1 1 
ATOM   17631 C  CD2 . LEU D 1 455 ? 14.546  1.207   101.570 1.00 22.08 ? 447  LEU D CD2 1 
ATOM   17632 N  N   . MET D 1 456 ? 16.623  -3.213  103.088 1.00 10.63 ? 448  MET D N   1 
ATOM   17633 C  CA  . MET D 1 456 ? 15.943  -4.491  103.222 1.00 12.84 ? 448  MET D CA  1 
ATOM   17634 C  C   . MET D 1 456 ? 16.465  -5.317  104.391 1.00 14.75 ? 448  MET D C   1 
ATOM   17635 O  O   . MET D 1 456 ? 15.893  -6.372  104.684 1.00 15.76 ? 448  MET D O   1 
ATOM   17636 C  CB  . MET D 1 456 ? 16.080  -5.306  101.934 1.00 13.86 ? 448  MET D CB  1 
ATOM   17637 C  CG  . MET D 1 456 ? 15.290  -4.777  100.753 1.00 14.06 ? 448  MET D CG  1 
ATOM   17638 S  SD  . MET D 1 456 ? 15.315  -5.994  99.435  1.00 15.32 ? 448  MET D SD  1 
ATOM   17639 C  CE  . MET D 1 456 ? 16.371  -5.174  98.242  1.00 17.22 ? 448  MET D CE  1 
ATOM   17640 N  N   . LYS D 1 457 ? 17.527  -4.861  105.050 1.00 13.90 ? 449  LYS D N   1 
ATOM   17641 C  CA  . LYS D 1 457 ? 18.121  -5.554  106.192 1.00 15.82 ? 449  LYS D CA  1 
ATOM   17642 C  C   . LYS D 1 457 ? 18.603  -6.957  105.812 1.00 16.62 ? 449  LYS D C   1 
ATOM   17643 O  O   . LYS D 1 457 ? 18.403  -7.924  106.553 1.00 15.47 ? 449  LYS D O   1 
ATOM   17644 C  CB  . LYS D 1 457 ? 17.143  -5.599  107.370 1.00 20.58 ? 449  LYS D CB  1 
ATOM   17645 C  CG  . LYS D 1 457 ? 16.603  -4.207  107.756 1.00 19.07 ? 449  LYS D CG  1 
ATOM   17646 C  CD  . LYS D 1 457 ? 15.601  -4.290  108.902 1.00 28.52 ? 449  LYS D CD  1 
ATOM   17647 C  CE  . LYS D 1 457 ? 16.286  -4.489  110.236 1.00 36.88 ? 449  LYS D CE  1 
ATOM   17648 N  NZ  . LYS D 1 457 ? 15.294  -4.679  111.322 1.00 45.61 ? 449  LYS D NZ  1 
ATOM   17649 N  N   . ILE D 1 458 ? 19.227  -7.069  104.641 1.00 15.66 ? 450  ILE D N   1 
ATOM   17650 C  CA  . ILE D 1 458 ? 19.815  -8.318  104.175 1.00 14.62 ? 450  ILE D CA  1 
ATOM   17651 C  C   . ILE D 1 458 ? 21.340  -8.179  104.209 1.00 15.75 ? 450  ILE D C   1 
ATOM   17652 O  O   . ILE D 1 458 ? 21.882  -7.094  104.436 1.00 13.31 ? 450  ILE D O   1 
ATOM   17653 C  CB  . ILE D 1 458 ? 19.309  -8.695  102.774 1.00 12.89 ? 450  ILE D CB  1 
ATOM   17654 C  CG1 . ILE D 1 458 ? 19.585  -7.554  101.793 1.00 11.05 ? 450  ILE D CG1 1 
ATOM   17655 C  CG2 . ILE D 1 458 ? 17.808  -9.035  102.824 1.00 15.91 ? 450  ILE D CG2 1 
ATOM   17656 C  CD1 . ILE D 1 458 ? 19.316  -7.897  100.329 1.00 17.01 ? 450  ILE D CD1 1 
ATOM   17657 N  N   . ASN D 1 459 ? 22.045  -9.300  103.982 1.00 12.40 ? 451  ASN D N   1 
ATOM   17658 C  CA  . ASN D 1 459 ? 23.487  -9.362  104.273 1.00 12.63 ? 451  ASN D CA  1 
ATOM   17659 C  C   . ASN D 1 459 ? 24.378  -9.808  103.105 1.00 18.77 ? 451  ASN D C   1 
ATOM   17660 O  O   . ASN D 1 459 ? 25.293  -10.614 103.297 1.00 15.72 ? 451  ASN D O   1 
ATOM   17661 C  CB  . ASN D 1 459 ? 23.729  -10.258 105.493 1.00 15.12 ? 451  ASN D CB  1 
ATOM   17662 C  CG  . ASN D 1 459 ? 23.272  -11.705 105.285 1.00 17.14 ? 451  ASN D CG  1 
ATOM   17663 O  OD1 . ASN D 1 459 ? 22.769  -12.064 104.227 1.00 16.76 ? 451  ASN D OD1 1 
ATOM   17664 N  ND2 . ASN D 1 459 ? 23.467  -12.545 106.310 1.00 15.38 ? 451  ASN D ND2 1 
ATOM   17665 N  N   . PRO D 1 460 ? 24.212  -9.241  101.902 1.00 13.69 ? 452  PRO D N   1 
ATOM   17666 C  CA  . PRO D 1 460 ? 25.256  -9.414  100.886 1.00 17.03 ? 452  PRO D CA  1 
ATOM   17667 C  C   . PRO D 1 460 ? 26.520  -8.689  101.320 1.00 16.41 ? 452  PRO D C   1 
ATOM   17668 O  O   . PRO D 1 460 ? 26.484  -7.753  102.122 1.00 18.34 ? 452  PRO D O   1 
ATOM   17669 C  CB  . PRO D 1 460 ? 24.654  -8.775  99.633  1.00 17.09 ? 452  PRO D CB  1 
ATOM   17670 C  CG  . PRO D 1 460 ? 23.781  -7.697  100.185 1.00 14.83 ? 452  PRO D CG  1 
ATOM   17671 C  CD  . PRO D 1 460 ? 23.191  -8.281  101.441 1.00 11.43 ? 452  PRO D CD  1 
ATOM   17672 N  N   . VAL D 1 461 ? 27.651  -9.134  100.776 1.00 15.58 ? 453  VAL D N   1 
ATOM   17673 C  CA  . VAL D 1 461 ? 28.964  -8.594  101.130 1.00 17.13 ? 453  VAL D CA  1 
ATOM   17674 C  C   . VAL D 1 461 ? 29.532  -7.897  99.898  1.00 16.65 ? 453  VAL D C   1 
ATOM   17675 O  O   . VAL D 1 461 ? 29.863  -8.544  98.896  1.00 15.04 ? 453  VAL D O   1 
ATOM   17676 C  CB  . VAL D 1 461 ? 29.917  -9.683  101.642 1.00 14.47 ? 453  VAL D CB  1 
ATOM   17677 C  CG1 . VAL D 1 461 ? 31.292  -9.097  101.948 1.00 16.95 ? 453  VAL D CG1 1 
ATOM   17678 C  CG2 . VAL D 1 461 ? 29.339  -10.374 102.892 1.00 14.76 ? 453  VAL D CG2 1 
ATOM   17679 N  N   . PHE D 1 462 ? 29.654  -6.578  99.969  1.00 13.27 ? 454  PHE D N   1 
ATOM   17680 C  CA  . PHE D 1 462 ? 30.185  -5.788  98.869  1.00 12.20 ? 454  PHE D CA  1 
ATOM   17681 C  C   . PHE D 1 462 ? 31.680  -5.584  99.083  1.00 12.42 ? 454  PHE D C   1 
ATOM   17682 O  O   . PHE D 1 462 ? 32.091  -5.024  100.104 1.00 17.75 ? 454  PHE D O   1 
ATOM   17683 C  CB  . PHE D 1 462 ? 29.439  -4.458  98.782  1.00 11.71 ? 454  PHE D CB  1 
ATOM   17684 C  CG  . PHE D 1 462 ? 27.938  -4.621  98.591  1.00 15.24 ? 454  PHE D CG  1 
ATOM   17685 C  CD1 . PHE D 1 462 ? 27.416  -4.945  97.349  1.00 16.18 ? 454  PHE D CD1 1 
ATOM   17686 C  CD2 . PHE D 1 462 ? 27.066  -4.486  99.661  1.00 12.69 ? 454  PHE D CD2 1 
ATOM   17687 C  CE1 . PHE D 1 462 ? 26.050  -5.112  97.161  1.00 18.22 ? 454  PHE D CE1 1 
ATOM   17688 C  CE2 . PHE D 1 462 ? 25.695  -4.650  99.489  1.00 16.64 ? 454  PHE D CE2 1 
ATOM   17689 C  CZ  . PHE D 1 462 ? 25.181  -4.971  98.232  1.00 16.08 ? 454  PHE D CZ  1 
ATOM   17690 N  N   . VAL D 1 463 ? 32.489  -6.052  98.136  1.00 14.06 ? 455  VAL D N   1 
ATOM   17691 C  CA  . VAL D 1 463 ? 33.950  -6.038  98.248  1.00 12.20 ? 455  VAL D CA  1 
ATOM   17692 C  C   . VAL D 1 463 ? 34.493  -4.954  97.329  1.00 13.06 ? 455  VAL D C   1 
ATOM   17693 O  O   . VAL D 1 463 ? 34.098  -4.875  96.160  1.00 13.27 ? 455  VAL D O   1 
ATOM   17694 C  CB  . VAL D 1 463 ? 34.537  -7.409  97.885  1.00 14.06 ? 455  VAL D CB  1 
ATOM   17695 C  CG1 . VAL D 1 463 ? 36.076  -7.375  97.839  1.00 17.54 ? 455  VAL D CG1 1 
ATOM   17696 C  CG2 . VAL D 1 463 ? 34.020  -8.474  98.852  1.00 14.33 ? 455  VAL D CG2 1 
ATOM   17697 N  N   . PHE D 1 464 ? 35.423  -4.142  97.842  1.00 14.22 ? 456  PHE D N   1 
ATOM   17698 C  CA  . PHE D 1 464 ? 36.020  -3.064  97.065  1.00 12.36 ? 456  PHE D CA  1 
ATOM   17699 C  C   . PHE D 1 464 ? 37.535  -3.115  97.189  1.00 16.40 ? 456  PHE D C   1 
ATOM   17700 O  O   . PHE D 1 464 ? 38.068  -3.230  98.298  1.00 17.04 ? 456  PHE D O   1 
ATOM   17701 C  CB  . PHE D 1 464 ? 35.482  -1.699  97.513  1.00 11.06 ? 456  PHE D CB  1 
ATOM   17702 C  CG  . PHE D 1 464 ? 33.988  -1.573  97.352  1.00 13.05 ? 456  PHE D CG  1 
ATOM   17703 C  CD1 . PHE D 1 464 ? 33.429  -1.470  96.088  1.00 12.26 ? 456  PHE D CD1 1 
ATOM   17704 C  CD2 . PHE D 1 464 ? 33.146  -1.606  98.459  1.00 15.21 ? 456  PHE D CD2 1 
ATOM   17705 C  CE1 . PHE D 1 464 ? 32.050  -1.375  95.922  1.00 13.63 ? 456  PHE D CE1 1 
ATOM   17706 C  CE2 . PHE D 1 464 ? 31.762  -1.528  98.305  1.00 11.59 ? 456  PHE D CE2 1 
ATOM   17707 C  CZ  . PHE D 1 464 ? 31.217  -1.402  97.030  1.00 9.71  ? 456  PHE D CZ  1 
ATOM   17708 N  N   . THR D 1 465 ? 38.216  -3.049  96.052  1.00 17.54 ? 457  THR D N   1 
ATOM   17709 C  CA  . THR D 1 465 ? 39.668  -2.979  96.002  1.00 16.46 ? 457  THR D CA  1 
ATOM   17710 C  C   . THR D 1 465 ? 40.064  -1.606  95.469  1.00 14.87 ? 457  THR D C   1 
ATOM   17711 O  O   . THR D 1 465 ? 39.207  -0.789  95.112  1.00 12.51 ? 457  THR D O   1 
ATOM   17712 C  CB  . THR D 1 465 ? 40.241  -4.116  95.149  1.00 16.13 ? 457  THR D CB  1 
ATOM   17713 O  OG1 . THR D 1 465 ? 39.913  -3.908  93.769  1.00 17.75 ? 457  THR D OG1 1 
ATOM   17714 C  CG2 . THR D 1 465 ? 39.673  -5.461  95.597  1.00 22.04 ? 457  THR D CG2 1 
ATOM   17715 N  N   . HIS D 1 466 ? 41.371  -1.347  95.425  1.00 13.83 ? 458  HIS D N   1 
ATOM   17716 C  CA  . HIS D 1 466 ? 41.887  -0.090  94.873  1.00 14.23 ? 458  HIS D CA  1 
ATOM   17717 C  C   . HIS D 1 466 ? 41.280  1.097   95.618  1.00 17.76 ? 458  HIS D C   1 
ATOM   17718 O  O   . HIS D 1 466 ? 40.573  1.938   95.058  1.00 16.36 ? 458  HIS D O   1 
ATOM   17719 C  CB  . HIS D 1 466 ? 41.612  -0.005  93.364  1.00 17.64 ? 458  HIS D CB  1 
ATOM   17720 C  CG  . HIS D 1 466 ? 42.328  -1.050  92.566  1.00 23.81 ? 458  HIS D CG  1 
ATOM   17721 N  ND1 . HIS D 1 466 ? 42.053  -2.396  92.684  1.00 28.93 ? 458  HIS D ND1 1 
ATOM   17722 C  CD2 . HIS D 1 466 ? 43.327  -0.950  91.658  1.00 30.38 ? 458  HIS D CD2 1 
ATOM   17723 C  CE1 . HIS D 1 466 ? 42.846  -3.079  91.877  1.00 26.98 ? 458  HIS D CE1 1 
ATOM   17724 N  NE2 . HIS D 1 466 ? 43.631  -2.225  91.245  1.00 26.81 ? 458  HIS D NE2 1 
ATOM   17725 N  N   . ASP D 1 467 ? 41.570  1.148   96.912  1.00 15.49 ? 459  ASP D N   1 
ATOM   17726 C  CA  . ASP D 1 467 ? 40.753  1.932   97.817  1.00 15.76 ? 459  ASP D CA  1 
ATOM   17727 C  C   . ASP D 1 467 ? 41.214  3.375   98.005  1.00 17.80 ? 459  ASP D C   1 
ATOM   17728 O  O   . ASP D 1 467 ? 40.558  4.110   98.745  1.00 16.82 ? 459  ASP D O   1 
ATOM   17729 C  CB  . ASP D 1 467 ? 40.697  1.245   99.181  1.00 17.51 ? 459  ASP D CB  1 
ATOM   17730 C  CG  . ASP D 1 467 ? 41.945  1.458   99.983  1.00 19.27 ? 459  ASP D CG  1 
ATOM   17731 O  OD1 . ASP D 1 467 ? 43.036  1.453   99.385  1.00 21.93 ? 459  ASP D OD1 1 
ATOM   17732 O  OD2 . ASP D 1 467 ? 41.833  1.643   101.215 1.00 20.49 ? 459  ASP D OD2 1 
ATOM   17733 N  N   . SER D 1 468 ? 42.294  3.816   97.365  1.00 16.73 ? 460  SER D N   1 
ATOM   17734 C  CA  . SER D 1 468 ? 42.754  5.181   97.610  1.00 14.06 ? 460  SER D CA  1 
ATOM   17735 C  C   . SER D 1 468 ? 43.725  5.592   96.508  1.00 14.57 ? 460  SER D C   1 
ATOM   17736 O  O   . SER D 1 468 ? 43.923  4.869   95.524  1.00 17.19 ? 460  SER D O   1 
ATOM   17737 C  CB  . SER D 1 468 ? 43.410  5.288   98.994  1.00 15.61 ? 460  SER D CB  1 
ATOM   17738 O  OG  . SER D 1 468 ? 44.712  4.708   98.965  1.00 16.89 ? 460  SER D OG  1 
ATOM   17739 N  N   . ILE D 1 469 ? 44.374  6.747   96.700  1.00 14.80 ? 461  ILE D N   1 
ATOM   17740 C  CA  . ILE D 1 469 ? 45.432  7.217   95.806  1.00 17.69 ? 461  ILE D CA  1 
ATOM   17741 C  C   . ILE D 1 469 ? 46.542  6.175   95.727  1.00 23.06 ? 461  ILE D C   1 
ATOM   17742 O  O   . ILE D 1 469 ? 47.378  6.211   94.814  1.00 21.79 ? 461  ILE D O   1 
ATOM   17743 C  CB  . ILE D 1 469 ? 45.998  8.574   96.265  1.00 19.61 ? 461  ILE D CB  1 
ATOM   17744 C  CG1 . ILE D 1 469 ? 46.405  8.511   97.742  1.00 19.86 ? 461  ILE D CG1 1 
ATOM   17745 C  CG2 . ILE D 1 469 ? 44.981  9.693   96.031  1.00 23.44 ? 461  ILE D CG2 1 
ATOM   17746 C  CD1 . ILE D 1 469 ? 47.124  9.775   98.250  1.00 20.40 ? 461  ILE D CD1 1 
ATOM   17747 N  N   . GLY D 1 470 ? 46.561  5.245   96.687  1.00 18.52 ? 462  GLY D N   1 
ATOM   17748 C  CA  . GLY D 1 470 ? 47.477  4.114   96.670  1.00 15.41 ? 462  GLY D CA  1 
ATOM   17749 C  C   . GLY D 1 470 ? 47.395  3.235   95.429  1.00 16.63 ? 462  GLY D C   1 
ATOM   17750 O  O   . GLY D 1 470 ? 48.313  2.436   95.203  1.00 17.38 ? 462  GLY D O   1 
ATOM   17751 N  N   . LEU D 1 471 ? 46.324  3.331   94.638  1.00 16.73 ? 463  LEU D N   1 
ATOM   17752 C  CA  . LEU D 1 471 ? 46.277  2.545   93.404  1.00 17.23 ? 463  LEU D CA  1 
ATOM   17753 C  C   . LEU D 1 471 ? 47.213  3.103   92.338  1.00 23.79 ? 463  LEU D C   1 
ATOM   17754 O  O   . LEU D 1 471 ? 47.531  2.390   91.381  1.00 22.24 ? 463  LEU D O   1 
ATOM   17755 C  CB  . LEU D 1 471 ? 44.840  2.455   92.862  1.00 16.71 ? 463  LEU D CB  1 
ATOM   17756 C  CG  . LEU D 1 471 ? 44.083  3.683   92.357  1.00 14.89 ? 463  LEU D CG  1 
ATOM   17757 C  CD1 . LEU D 1 471 ? 44.510  4.060   90.934  1.00 19.06 ? 463  LEU D CD1 1 
ATOM   17758 C  CD2 . LEU D 1 471 ? 42.578  3.435   92.413  1.00 14.70 ? 463  LEU D CD2 1 
ATOM   17759 N  N   . GLY D 1 472 ? 47.643  4.357   92.466  1.00 17.83 ? 464  GLY D N   1 
ATOM   17760 C  CA  . GLY D 1 472 ? 48.710  4.874   91.621  1.00 16.76 ? 464  GLY D CA  1 
ATOM   17761 C  C   . GLY D 1 472 ? 48.209  5.400   90.285  1.00 18.19 ? 464  GLY D C   1 
ATOM   17762 O  O   . GLY D 1 472 ? 47.284  6.212   90.237  1.00 22.47 ? 464  GLY D O   1 
ATOM   17763 N  N   . GLU D 1 473 ? 48.803  4.898   89.200  1.00 16.08 ? 465  GLU D N   1 
ATOM   17764 C  CA  . GLU D 1 473 ? 48.858  5.620   87.929  1.00 19.64 ? 465  GLU D CA  1 
ATOM   17765 C  C   . GLU D 1 473 ? 47.509  5.777   87.228  1.00 20.33 ? 465  GLU D C   1 
ATOM   17766 O  O   . GLU D 1 473 ? 47.390  6.647   86.359  1.00 18.69 ? 465  GLU D O   1 
ATOM   17767 C  CB  . GLU D 1 473 ? 49.832  4.915   86.984  1.00 18.21 ? 465  GLU D CB  1 
ATOM   17768 C  CG  . GLU D 1 473 ? 51.309  5.081   87.356  1.00 19.24 ? 465  GLU D CG  1 
ATOM   17769 C  CD  . GLU D 1 473 ? 51.831  3.993   88.288  1.00 24.68 ? 465  GLU D CD  1 
ATOM   17770 O  OE1 . GLU D 1 473 ? 51.037  3.424   89.078  1.00 23.80 ? 465  GLU D OE1 1 
ATOM   17771 O  OE2 . GLU D 1 473 ? 53.048  3.713   88.226  1.00 25.41 ? 465  GLU D OE2 1 
ATOM   17772 N  N   . ASP D 1 474 ? 46.507  4.954   87.550  1.00 18.31 ? 466  ASP D N   1 
ATOM   17773 C  CA  . ASP D 1 474 ? 45.207  5.104   86.886  1.00 20.71 ? 466  ASP D CA  1 
ATOM   17774 C  C   . ASP D 1 474 ? 44.601  6.491   87.112  1.00 23.82 ? 466  ASP D C   1 
ATOM   17775 O  O   . ASP D 1 474 ? 43.780  6.944   86.303  1.00 24.96 ? 466  ASP D O   1 
ATOM   17776 C  CB  . ASP D 1 474 ? 44.226  4.027   87.355  1.00 15.79 ? 466  ASP D CB  1 
ATOM   17777 C  CG  . ASP D 1 474 ? 44.400  2.703   86.623  1.00 25.65 ? 466  ASP D CG  1 
ATOM   17778 O  OD1 . ASP D 1 474 ? 45.283  2.594   85.739  1.00 24.09 ? 466  ASP D OD1 1 
ATOM   17779 O  OD2 . ASP D 1 474 ? 43.634  1.766   86.929  1.00 24.10 ? 466  ASP D OD2 1 
ATOM   17780 N  N   . GLY D 1 475 ? 44.953  7.159   88.217  1.00 19.36 ? 467  GLY D N   1 
ATOM   17781 C  CA  . GLY D 1 475 ? 44.706  8.579   88.368  1.00 15.78 ? 467  GLY D CA  1 
ATOM   17782 C  C   . GLY D 1 475 ? 43.340  8.960   88.916  1.00 15.62 ? 467  GLY D C   1 
ATOM   17783 O  O   . GLY D 1 475 ? 42.587  8.122   89.422  1.00 13.52 ? 467  GLY D O   1 
ATOM   17784 N  N   . PRO D 1 476 ? 42.989  10.249  88.799  1.00 16.40 ? 468  PRO D N   1 
ATOM   17785 C  CA  . PRO D 1 476 ? 41.875  10.791  89.602  1.00 16.76 ? 468  PRO D CA  1 
ATOM   17786 C  C   . PRO D 1 476 ? 40.501  10.248  89.246  1.00 16.88 ? 468  PRO D C   1 
ATOM   17787 O  O   . PRO D 1 476 ? 39.594  10.346  90.081  1.00 16.29 ? 468  PRO D O   1 
ATOM   17788 C  CB  . PRO D 1 476 ? 41.953  12.307  89.351  1.00 14.79 ? 468  PRO D CB  1 
ATOM   17789 C  CG  . PRO D 1 476 ? 42.748  12.453  88.086  1.00 16.22 ? 468  PRO D CG  1 
ATOM   17790 C  CD  . PRO D 1 476 ? 43.709  11.302  88.062  1.00 17.07 ? 468  PRO D CD  1 
ATOM   17791 N  N   . THR D 1 477 ? 40.293  9.682   88.057  1.00 14.12 ? 469  THR D N   1 
ATOM   17792 C  CA  . THR D 1 477 ? 38.963  9.138   87.792  1.00 10.81 ? 469  THR D CA  1 
ATOM   17793 C  C   . THR D 1 477 ? 38.721  7.854   88.561  1.00 17.01 ? 469  THR D C   1 
ATOM   17794 O  O   . THR D 1 477 ? 37.564  7.486   88.775  1.00 17.76 ? 469  THR D O   1 
ATOM   17795 C  CB  . THR D 1 477 ? 38.755  8.846   86.312  1.00 14.06 ? 469  THR D CB  1 
ATOM   17796 O  OG1 . THR D 1 477 ? 39.662  7.811   85.921  1.00 18.14 ? 469  THR D OG1 1 
ATOM   17797 C  CG2 . THR D 1 477 ? 39.010  10.080  85.481  1.00 13.37 ? 469  THR D CG2 1 
ATOM   17798 N  N   . HIS D 1 478 ? 39.792  7.162   88.968  1.00 10.89 ? 470  HIS D N   1 
ATOM   17799 C  CA  . HIS D 1 478 ? 39.673  5.886   89.651  1.00 16.04 ? 470  HIS D CA  1 
ATOM   17800 C  C   . HIS D 1 478 ? 40.037  5.953   91.128  1.00 11.92 ? 470  HIS D C   1 
ATOM   17801 O  O   . HIS D 1 478 ? 39.616  5.072   91.886  1.00 15.36 ? 470  HIS D O   1 
ATOM   17802 C  CB  . HIS D 1 478 ? 40.569  4.826   88.971  1.00 16.57 ? 470  HIS D CB  1 
ATOM   17803 C  CG  . HIS D 1 478 ? 40.006  4.251   87.704  1.00 19.19 ? 470  HIS D CG  1 
ATOM   17804 N  ND1 . HIS D 1 478 ? 39.504  5.029   86.682  1.00 27.34 ? 470  HIS D ND1 1 
ATOM   17805 C  CD2 . HIS D 1 478 ? 39.900  2.965   87.281  1.00 24.51 ? 470  HIS D CD2 1 
ATOM   17806 C  CE1 . HIS D 1 478 ? 39.093  4.248   85.695  1.00 26.28 ? 470  HIS D CE1 1 
ATOM   17807 N  NE2 . HIS D 1 478 ? 39.323  2.991   86.033  1.00 22.89 ? 470  HIS D NE2 1 
ATOM   17808 N  N   . GLN D 1 479 ? 40.795  6.965   91.553  1.00 14.52 ? 471  GLN D N   1 
ATOM   17809 C  CA  . GLN D 1 479 ? 41.320  7.002   92.921  1.00 15.07 ? 471  GLN D CA  1 
ATOM   17810 C  C   . GLN D 1 479 ? 40.255  7.497   93.895  1.00 14.65 ? 471  GLN D C   1 
ATOM   17811 O  O   . GLN D 1 479 ? 39.844  8.666   93.815  1.00 13.51 ? 471  GLN D O   1 
ATOM   17812 C  CB  . GLN D 1 479 ? 42.549  7.909   93.015  1.00 12.59 ? 471  GLN D CB  1 
ATOM   17813 C  CG  . GLN D 1 479 ? 43.783  7.413   92.279  1.00 14.33 ? 471  GLN D CG  1 
ATOM   17814 C  CD  . GLN D 1 479 ? 44.779  8.524   91.993  1.00 17.21 ? 471  GLN D CD  1 
ATOM   17815 O  OE1 . GLN D 1 479 ? 44.429  9.704   92.009  1.00 17.36 ? 471  GLN D OE1 1 
ATOM   17816 N  NE2 . GLN D 1 479 ? 46.027  8.150   91.710  1.00 18.07 ? 471  GLN D NE2 1 
ATOM   17817 N  N   . PRO D 1 480 ? 39.810  6.669   94.834  1.00 14.94 ? 472  PRO D N   1 
ATOM   17818 C  CA  . PRO D 1 480 ? 38.787  7.117   95.781  1.00 19.63 ? 472  PRO D CA  1 
ATOM   17819 C  C   . PRO D 1 480 ? 39.297  8.228   96.682  1.00 14.15 ? 472  PRO D C   1 
ATOM   17820 O  O   . PRO D 1 480 ? 40.473  8.276   97.050  1.00 14.69 ? 472  PRO D O   1 
ATOM   17821 C  CB  . PRO D 1 480 ? 38.464  5.848   96.579  1.00 17.26 ? 472  PRO D CB  1 
ATOM   17822 C  CG  . PRO D 1 480 ? 38.848  4.739   95.679  1.00 15.90 ? 472  PRO D CG  1 
ATOM   17823 C  CD  . PRO D 1 480 ? 40.076  5.230   94.970  1.00 12.03 ? 472  PRO D CD  1 
ATOM   17824 N  N   . ILE D 1 481 ? 38.400  9.159   96.983  1.00 16.64 ? 473  ILE D N   1 
ATOM   17825 C  CA  . ILE D 1 481 ? 38.671  10.260  97.895  1.00 16.36 ? 473  ILE D CA  1 
ATOM   17826 C  C   . ILE D 1 481 ? 37.549  10.235  98.915  1.00 13.51 ? 473  ILE D C   1 
ATOM   17827 O  O   . ILE D 1 481 ? 37.785  10.038  100.111 1.00 14.71 ? 473  ILE D O   1 
ATOM   17828 C  CB  . ILE D 1 481 ? 38.731  11.632  97.186  1.00 11.26 ? 473  ILE D CB  1 
ATOM   17829 C  CG1 . ILE D 1 481 ? 39.813  11.669  96.102  1.00 13.58 ? 473  ILE D CG1 1 
ATOM   17830 C  CG2 . ILE D 1 481 ? 38.930  12.746  98.202  1.00 13.22 ? 473  ILE D CG2 1 
ATOM   17831 C  CD1 . ILE D 1 481 ? 41.209  11.439  96.610  1.00 13.56 ? 473  ILE D CD1 1 
ATOM   17832 N  N   . GLU D 1 482 ? 36.314  10.413  98.440  1.00 9.79  ? 474  GLU D N   1 
ATOM   17833 C  CA  . GLU D 1 482 ? 35.167  10.565  99.322  1.00 14.36 ? 474  GLU D CA  1 
ATOM   17834 C  C   . GLU D 1 482 ? 34.326  9.296   99.468  1.00 11.29 ? 474  GLU D C   1 
ATOM   17835 O  O   . GLU D 1 482 ? 33.385  9.291   100.262 1.00 11.84 ? 474  GLU D O   1 
ATOM   17836 C  CB  . GLU D 1 482 ? 34.280  11.723  98.834  1.00 13.01 ? 474  GLU D CB  1 
ATOM   17837 C  CG  . GLU D 1 482 ? 33.507  11.475  97.522  1.00 13.46 ? 474  GLU D CG  1 
ATOM   17838 C  CD  . GLU D 1 482 ? 34.323  11.664  96.244  1.00 14.54 ? 474  GLU D CD  1 
ATOM   17839 O  OE1 . GLU D 1 482 ? 35.548  11.419  96.249  1.00 11.83 ? 474  GLU D OE1 1 
ATOM   17840 O  OE2 . GLU D 1 482 ? 33.717  12.012  95.201  1.00 12.76 ? 474  GLU D OE2 1 
ATOM   17841 N  N   . GLN D 1 483 ? 34.650  8.216   98.749  1.00 10.82 ? 475  GLN D N   1 
ATOM   17842 C  CA  . GLN D 1 483 ? 33.725  7.081   98.672  1.00 12.11 ? 475  GLN D CA  1 
ATOM   17843 C  C   . GLN D 1 483 ? 33.535  6.409   100.024 1.00 12.35 ? 475  GLN D C   1 
ATOM   17844 O  O   . GLN D 1 483 ? 32.399  6.135   100.428 1.00 12.09 ? 475  GLN D O   1 
ATOM   17845 C  CB  . GLN D 1 483 ? 34.204  6.058   97.641  1.00 16.49 ? 475  GLN D CB  1 
ATOM   17846 C  CG  . GLN D 1 483 ? 33.915  6.487   96.218  1.00 13.53 ? 475  GLN D CG  1 
ATOM   17847 C  CD  . GLN D 1 483 ? 34.724  7.714   95.815  1.00 14.43 ? 475  GLN D CD  1 
ATOM   17848 O  OE1 . GLN D 1 483 ? 35.881  7.830   96.172  1.00 13.51 ? 475  GLN D OE1 1 
ATOM   17849 N  NE2 . GLN D 1 483 ? 34.111  8.632   95.075  1.00 14.74 ? 475  GLN D NE2 1 
ATOM   17850 N  N   . THR D 1 484 ? 34.636  6.101   100.720 1.00 12.12 ? 476  THR D N   1 
ATOM   17851 C  CA  . THR D 1 484 ? 34.517  5.438   102.020 1.00 13.61 ? 476  THR D CA  1 
ATOM   17852 C  C   . THR D 1 484 ? 33.700  6.283   103.000 1.00 14.56 ? 476  THR D C   1 
ATOM   17853 O  O   . THR D 1 484 ? 32.793  5.768   103.672 1.00 13.59 ? 476  THR D O   1 
ATOM   17854 C  CB  . THR D 1 484 ? 35.913  5.121   102.570 1.00 13.35 ? 476  THR D CB  1 
ATOM   17855 O  OG1 . THR D 1 484 ? 36.588  4.220   101.669 1.00 13.98 ? 476  THR D OG1 1 
ATOM   17856 C  CG2 . THR D 1 484 ? 35.832  4.453   103.944 1.00 12.20 ? 476  THR D CG2 1 
ATOM   17857 N  N   . ALA D 1 485 ? 33.970  7.591   103.062 1.00 12.19 ? 477  ALA D N   1 
ATOM   17858 C  CA  . ALA D 1 485 ? 33.173  8.466   103.923 1.00 15.29 ? 477  ALA D CA  1 
ATOM   17859 C  C   . ALA D 1 485 ? 31.697  8.438   103.544 1.00 15.04 ? 477  ALA D C   1 
ATOM   17860 O  O   . ALA D 1 485 ? 30.824  8.448   104.425 1.00 13.23 ? 477  ALA D O   1 
ATOM   17861 C  CB  . ALA D 1 485 ? 33.706  9.902   103.876 1.00 12.10 ? 477  ALA D CB  1 
ATOM   17862 N  N   . THR D 1 486 ? 31.384  8.405   102.243 1.00 11.54 ? 478  THR D N   1 
ATOM   17863 C  CA  . THR D 1 486 ? 29.967  8.406   101.875 1.00 10.37 ? 478  THR D CA  1 
ATOM   17864 C  C   . THR D 1 486 ? 29.312  7.064   102.184 1.00 9.89  ? 478  THR D C   1 
ATOM   17865 O  O   . THR D 1 486 ? 28.130  7.024   102.529 1.00 11.57 ? 478  THR D O   1 
ATOM   17866 C  CB  . THR D 1 486 ? 29.753  8.739   100.393 1.00 11.54 ? 478  THR D CB  1 
ATOM   17867 O  OG1 . THR D 1 486 ? 30.301  7.699   99.571  1.00 10.93 ? 478  THR D OG1 1 
ATOM   17868 C  CG2 . THR D 1 486 ? 30.363  10.101  100.031 1.00 14.11 ? 478  THR D CG2 1 
ATOM   17869 N  N   . LEU D 1 487 ? 30.049  5.960   102.048 1.00 11.31 ? 479  LEU D N   1 
ATOM   17870 C  CA  . LEU D 1 487 ? 29.473  4.653   102.366 1.00 13.72 ? 479  LEU D CA  1 
ATOM   17871 C  C   . LEU D 1 487 ? 29.113  4.542   103.844 1.00 12.56 ? 479  LEU D C   1 
ATOM   17872 O  O   . LEU D 1 487 ? 28.139  3.869   104.196 1.00 11.51 ? 479  LEU D O   1 
ATOM   17873 C  CB  . LEU D 1 487 ? 30.450  3.541   101.976 1.00 13.78 ? 479  LEU D CB  1 
ATOM   17874 C  CG  . LEU D 1 487 ? 30.614  3.325   100.465 1.00 12.00 ? 479  LEU D CG  1 
ATOM   17875 C  CD1 . LEU D 1 487 ? 31.837  2.462   100.193 1.00 10.74 ? 479  LEU D CD1 1 
ATOM   17876 C  CD2 . LEU D 1 487 ? 29.348  2.696   99.869  1.00 9.00  ? 479  LEU D CD2 1 
ATOM   17877 N  N   . ARG D 1 488 ? 29.876  5.198   104.718 1.00 10.37 ? 480  ARG D N   1 
ATOM   17878 C  CA  . ARG D 1 488 ? 29.597  5.135   106.152 1.00 13.60 ? 480  ARG D CA  1 
ATOM   17879 C  C   . ARG D 1 488 ? 28.284  5.819   106.535 1.00 16.41 ? 480  ARG D C   1 
ATOM   17880 O  O   . ARG D 1 488 ? 27.775  5.579   107.634 1.00 15.31 ? 480  ARG D O   1 
ATOM   17881 C  CB  . ARG D 1 488 ? 30.757  5.766   106.944 1.00 11.91 ? 480  ARG D CB  1 
ATOM   17882 C  CG  . ARG D 1 488 ? 32.114  5.056   106.808 1.00 12.08 ? 480  ARG D CG  1 
ATOM   17883 C  CD  . ARG D 1 488 ? 33.212  5.780   107.642 1.00 14.41 ? 480  ARG D CD  1 
ATOM   17884 N  NE  . ARG D 1 488 ? 34.447  4.989   107.724 1.00 14.09 ? 480  ARG D NE  1 
ATOM   17885 C  CZ  . ARG D 1 488 ? 35.660  5.419   107.385 1.00 14.01 ? 480  ARG D CZ  1 
ATOM   17886 N  NH1 . ARG D 1 488 ? 35.841  6.663   106.967 1.00 15.17 ? 480  ARG D NH1 1 
ATOM   17887 N  NH2 . ARG D 1 488 ? 36.709  4.605   107.494 1.00 13.15 ? 480  ARG D NH2 1 
ATOM   17888 N  N   . LEU D 1 489 ? 27.731  6.671   105.673 1.00 13.64 ? 481  LEU D N   1 
ATOM   17889 C  CA  . LEU D 1 489 ? 26.485  7.369   105.970 1.00 9.79  ? 481  LEU D CA  1 
ATOM   17890 C  C   . LEU D 1 489 ? 25.248  6.596   105.543 1.00 17.72 ? 481  LEU D C   1 
ATOM   17891 O  O   . LEU D 1 489 ? 24.130  7.057   105.799 1.00 13.95 ? 481  LEU D O   1 
ATOM   17892 C  CB  . LEU D 1 489 ? 26.464  8.747   105.304 1.00 10.15 ? 481  LEU D CB  1 
ATOM   17893 C  CG  . LEU D 1 489 ? 27.642  9.630   105.676 1.00 16.55 ? 481  LEU D CG  1 
ATOM   17894 C  CD1 . LEU D 1 489 ? 27.523  10.972  104.967 1.00 18.59 ? 481  LEU D CD1 1 
ATOM   17895 C  CD2 . LEU D 1 489 ? 27.679  9.798   107.184 1.00 18.79 ? 481  LEU D CD2 1 
ATOM   17896 N  N   . ILE D 1 490 ? 25.407  5.449   104.893 1.00 12.36 ? 482  ILE D N   1 
ATOM   17897 C  CA  . ILE D 1 490 ? 24.257  4.599   104.606 1.00 10.36 ? 482  ILE D CA  1 
ATOM   17898 C  C   . ILE D 1 490 ? 23.731  4.031   105.918 1.00 13.59 ? 482  ILE D C   1 
ATOM   17899 O  O   . ILE D 1 490 ? 24.473  3.324   106.613 1.00 12.21 ? 482  ILE D O   1 
ATOM   17900 C  CB  . ILE D 1 490 ? 24.616  3.463   103.638 1.00 9.21  ? 482  ILE D CB  1 
ATOM   17901 C  CG1 . ILE D 1 490 ? 25.164  4.029   102.324 1.00 8.87  ? 482  ILE D CG1 1 
ATOM   17902 C  CG2 . ILE D 1 490 ? 23.365  2.589   103.389 1.00 11.24 ? 482  ILE D CG2 1 
ATOM   17903 C  CD1 . ILE D 1 490 ? 25.734  2.974   101.375 1.00 10.35 ? 482  ILE D CD1 1 
ATOM   17904 N  N   . PRO D 1 491 ? 22.476  4.295   106.294 1.00 12.39 ? 483  PRO D N   1 
ATOM   17905 C  CA  . PRO D 1 491 ? 21.929  3.659   107.498 1.00 14.24 ? 483  PRO D CA  1 
ATOM   17906 C  C   . PRO D 1 491 ? 21.974  2.140   107.371 1.00 13.24 ? 483  PRO D C   1 
ATOM   17907 O  O   . PRO D 1 491 ? 21.739  1.584   106.298 1.00 13.18 ? 483  PRO D O   1 
ATOM   17908 C  CB  . PRO D 1 491 ? 20.491  4.189   107.560 1.00 15.35 ? 483  PRO D CB  1 
ATOM   17909 C  CG  . PRO D 1 491 ? 20.531  5.489   106.768 1.00 11.81 ? 483  PRO D CG  1 
ATOM   17910 C  CD  . PRO D 1 491 ? 21.500  5.197   105.656 1.00 16.52 ? 483  PRO D CD  1 
ATOM   17911 N  N   . ASN D 1 492 ? 22.349  1.479   108.468 1.00 13.31 ? 484  ASN D N   1 
ATOM   17912 C  CA  . ASN D 1 492 ? 22.370  0.016   108.550 1.00 18.26 ? 484  ASN D CA  1 
ATOM   17913 C  C   . ASN D 1 492 ? 23.398  -0.619  107.609 1.00 17.02 ? 484  ASN D C   1 
ATOM   17914 O  O   . ASN D 1 492 ? 23.213  -1.743  107.142 1.00 18.73 ? 484  ASN D O   1 
ATOM   17915 C  CB  . ASN D 1 492 ? 20.978  -0.579  108.284 1.00 19.32 ? 484  ASN D CB  1 
ATOM   17916 C  CG  . ASN D 1 492 ? 20.852  -2.002  108.809 1.00 19.69 ? 484  ASN D CG  1 
ATOM   17917 O  OD1 . ASN D 1 492 ? 21.359  -2.315  109.882 1.00 17.53 ? 484  ASN D OD1 1 
ATOM   17918 N  ND2 . ASN D 1 492 ? 20.231  -2.878  108.029 1.00 11.58 ? 484  ASN D ND2 1 
ATOM   17919 N  N   . MET D 1 493 ? 24.491  0.081   107.312 1.00 14.48 ? 485  MET D N   1 
ATOM   17920 C  CA  . MET D 1 493 ? 25.597  -0.479  106.546 1.00 16.15 ? 485  MET D CA  1 
ATOM   17921 C  C   . MET D 1 493 ? 26.835  -0.529  107.429 1.00 16.08 ? 485  MET D C   1 
ATOM   17922 O  O   . MET D 1 493 ? 27.150  0.450   108.109 1.00 18.17 ? 485  MET D O   1 
ATOM   17923 C  CB  . MET D 1 493 ? 25.880  0.359   105.296 1.00 13.47 ? 485  MET D CB  1 
ATOM   17924 C  CG  . MET D 1 493 ? 27.141  -0.073  104.563 1.00 16.98 ? 485  MET D CG  1 
ATOM   17925 S  SD  . MET D 1 493 ? 26.958  -1.684  103.741 1.00 15.10 ? 485  MET D SD  1 
ATOM   17926 C  CE  . MET D 1 493 ? 25.937  -1.196  102.338 1.00 11.64 ? 485  MET D CE  1 
ATOM   17927 N  N   . ASP D 1 494 ? 27.536  -1.661  107.430 1.00 14.48 ? 486  ASP D N   1 
ATOM   17928 C  CA  . ASP D 1 494 ? 28.849  -1.743  108.061 1.00 15.90 ? 486  ASP D CA  1 
ATOM   17929 C  C   . ASP D 1 494 ? 29.925  -1.521  107.005 1.00 16.92 ? 486  ASP D C   1 
ATOM   17930 O  O   . ASP D 1 494 ? 29.900  -2.157  105.952 1.00 18.41 ? 486  ASP D O   1 
ATOM   17931 C  CB  . ASP D 1 494 ? 29.064  -3.095  108.738 1.00 16.19 ? 486  ASP D CB  1 
ATOM   17932 C  CG  . ASP D 1 494 ? 28.367  -3.202  110.092 1.00 20.28 ? 486  ASP D CG  1 
ATOM   17933 O  OD1 . ASP D 1 494 ? 27.761  -2.209  110.556 1.00 21.81 ? 486  ASP D OD1 1 
ATOM   17934 O  OD2 . ASP D 1 494 ? 28.438  -4.297  110.691 1.00 17.96 ? 486  ASP D OD2 1 
ATOM   17935 N  N   . VAL D 1 495 ? 30.866  -0.628  107.295 1.00 11.86 ? 487  VAL D N   1 
ATOM   17936 C  CA  . VAL D 1 495 ? 32.008  -0.359  106.429 1.00 13.76 ? 487  VAL D CA  1 
ATOM   17937 C  C   . VAL D 1 495 ? 33.260  -0.829  107.156 1.00 15.65 ? 487  VAL D C   1 
ATOM   17938 O  O   . VAL D 1 495 ? 33.552  -0.362  108.263 1.00 15.66 ? 487  VAL D O   1 
ATOM   17939 C  CB  . VAL D 1 495 ? 32.103  1.133   106.066 1.00 14.35 ? 487  VAL D CB  1 
ATOM   17940 C  CG1 . VAL D 1 495 ? 33.299  1.392   105.154 1.00 15.94 ? 487  VAL D CG1 1 
ATOM   17941 C  CG2 . VAL D 1 495 ? 30.821  1.584   105.394 1.00 12.76 ? 487  VAL D CG2 1 
ATOM   17942 N  N   . TRP D 1 496 ? 33.998  -1.755  106.539 1.00 12.92 ? 488  TRP D N   1 
ATOM   17943 C  CA  . TRP D 1 496 ? 35.265  -2.236  107.078 1.00 16.56 ? 488  TRP D CA  1 
ATOM   17944 C  C   . TRP D 1 496 ? 36.414  -1.821  106.164 1.00 14.95 ? 488  TRP D C   1 
ATOM   17945 O  O   . TRP D 1 496 ? 36.322  -1.937  104.938 1.00 16.87 ? 488  TRP D O   1 
ATOM   17946 C  CB  . TRP D 1 496 ? 35.266  -3.765  107.240 1.00 13.77 ? 488  TRP D CB  1 
ATOM   17947 C  CG  . TRP D 1 496 ? 34.361  -4.311  108.322 1.00 14.44 ? 488  TRP D CG  1 
ATOM   17948 C  CD1 . TRP D 1 496 ? 33.038  -4.626  108.206 1.00 20.72 ? 488  TRP D CD1 1 
ATOM   17949 C  CD2 . TRP D 1 496 ? 34.735  -4.651  109.663 1.00 18.49 ? 488  TRP D CD2 1 
ATOM   17950 N  NE1 . TRP D 1 496 ? 32.562  -5.128  109.394 1.00 17.33 ? 488  TRP D NE1 1 
ATOM   17951 C  CE2 . TRP D 1 496 ? 33.582  -5.148  110.307 1.00 18.42 ? 488  TRP D CE2 1 
ATOM   17952 C  CE3 . TRP D 1 496 ? 35.930  -4.577  110.384 1.00 17.84 ? 488  TRP D CE3 1 
ATOM   17953 C  CZ2 . TRP D 1 496 ? 33.586  -5.567  111.630 1.00 16.25 ? 488  TRP D CZ2 1 
ATOM   17954 C  CZ3 . TRP D 1 496 ? 35.932  -4.992  111.698 1.00 17.76 ? 488  TRP D CZ3 1 
ATOM   17955 C  CH2 . TRP D 1 496 ? 34.768  -5.484  112.310 1.00 21.61 ? 488  TRP D CH2 1 
ATOM   17956 N  N   . ARG D 1 497 ? 37.500  -1.334  106.766 1.00 16.36 ? 489  ARG D N   1 
ATOM   17957 C  CA  . ARG D 1 497 ? 38.717  -0.970  106.040 1.00 16.23 ? 489  ARG D CA  1 
ATOM   17958 C  C   . ARG D 1 497 ? 39.890  -1.582  106.804 1.00 17.31 ? 489  ARG D C   1 
ATOM   17959 O  O   . ARG D 1 497 ? 40.621  -0.881  107.516 1.00 17.50 ? 489  ARG D O   1 
ATOM   17960 C  CB  . ARG D 1 497 ? 38.829  0.552   105.896 1.00 16.83 ? 489  ARG D CB  1 
ATOM   17961 C  CG  . ARG D 1 497 ? 39.954  1.047   104.980 1.00 13.11 ? 489  ARG D CG  1 
ATOM   17962 C  CD  . ARG D 1 497 ? 39.884  2.558   104.763 1.00 17.75 ? 489  ARG D CD  1 
ATOM   17963 N  NE  . ARG D 1 497 ? 40.821  2.992   103.726 1.00 22.05 ? 489  ARG D NE  1 
ATOM   17964 C  CZ  . ARG D 1 497 ? 42.008  3.540   103.954 1.00 19.97 ? 489  ARG D CZ  1 
ATOM   17965 N  NH1 . ARG D 1 497 ? 42.428  3.732   105.200 1.00 15.54 ? 489  ARG D NH1 1 
ATOM   17966 N  NH2 . ARG D 1 497 ? 42.783  3.891   102.927 1.00 17.71 ? 489  ARG D NH2 1 
ATOM   17967 N  N   . PRO D 1 498 ? 40.089  -2.897  106.690 1.00 18.19 ? 490  PRO D N   1 
ATOM   17968 C  CA  . PRO D 1 498 ? 41.072  -3.575  107.552 1.00 16.93 ? 490  PRO D CA  1 
ATOM   17969 C  C   . PRO D 1 498 ? 42.515  -3.224  107.215 1.00 20.09 ? 490  PRO D C   1 
ATOM   17970 O  O   . PRO D 1 498 ? 42.862  -2.943  106.071 1.00 18.14 ? 490  PRO D O   1 
ATOM   17971 C  CB  . PRO D 1 498 ? 40.797  -5.063  107.304 1.00 17.46 ? 490  PRO D CB  1 
ATOM   17972 C  CG  . PRO D 1 498 ? 40.151  -5.110  105.942 1.00 19.34 ? 490  PRO D CG  1 
ATOM   17973 C  CD  . PRO D 1 498 ? 39.354  -3.831  105.816 1.00 16.43 ? 490  PRO D CD  1 
ATOM   17974 N  N   . CYS D 1 499 ? 43.376  -3.276  108.233 1.00 21.78 ? 491  CYS D N   1 
ATOM   17975 C  CA  . CYS D 1 499 ? 44.757  -2.832  108.058 1.00 20.14 ? 491  CYS D CA  1 
ATOM   17976 C  C   . CYS D 1 499 ? 45.744  -3.961  107.787 1.00 20.91 ? 491  CYS D C   1 
ATOM   17977 O  O   . CYS D 1 499 ? 46.882  -3.673  107.403 1.00 22.60 ? 491  CYS D O   1 
ATOM   17978 C  CB  . CYS D 1 499 ? 45.233  -2.037  109.286 1.00 20.19 ? 491  CYS D CB  1 
ATOM   17979 S  SG  . CYS D 1 499 ? 45.634  -3.010  110.735 1.00 22.58 ? 491  CYS D SG  1 
ATOM   17980 N  N   . ASP D 1 500 ? 45.357  -5.221  107.979 1.00 21.25 ? 492  ASP D N   1 
ATOM   17981 C  CA  . ASP D 1 500 ? 46.266  -6.344  107.767 1.00 22.35 ? 492  ASP D CA  1 
ATOM   17982 C  C   . ASP D 1 500 ? 45.440  -7.621  107.629 1.00 19.76 ? 492  ASP D C   1 
ATOM   17983 O  O   . ASP D 1 500 ? 44.207  -7.590  107.655 1.00 18.77 ? 492  ASP D O   1 
ATOM   17984 C  CB  . ASP D 1 500 ? 47.300  -6.439  108.896 1.00 24.28 ? 492  ASP D CB  1 
ATOM   17985 C  CG  . ASP D 1 500 ? 46.672  -6.649  110.271 1.00 27.19 ? 492  ASP D CG  1 
ATOM   17986 O  OD1 . ASP D 1 500 ? 45.548  -7.179  110.375 1.00 23.85 ? 492  ASP D OD1 1 
ATOM   17987 O  OD2 . ASP D 1 500 ? 47.323  -6.276  111.268 1.00 26.89 ? 492  ASP D OD2 1 
ATOM   17988 N  N   . THR D 1 501 ? 46.136  -8.757  107.506 1.00 22.27 ? 493  THR D N   1 
ATOM   17989 C  CA  . THR D 1 501 ? 45.437  -10.027 107.296 1.00 23.17 ? 493  THR D CA  1 
ATOM   17990 C  C   . THR D 1 501 ? 44.568  -10.416 108.490 1.00 20.71 ? 493  THR D C   1 
ATOM   17991 O  O   . THR D 1 501 ? 43.549  -11.096 108.316 1.00 26.31 ? 493  THR D O   1 
ATOM   17992 C  CB  . THR D 1 501 ? 46.441  -11.150 107.016 1.00 27.03 ? 493  THR D CB  1 
ATOM   17993 O  OG1 . THR D 1 501 ? 47.293  -11.304 108.152 1.00 31.78 ? 493  THR D OG1 1 
ATOM   17994 C  CG2 . THR D 1 501 ? 47.298  -10.829 105.794 1.00 30.26 ? 493  THR D CG2 1 
ATOM   17995 N  N   . ALA D 1 502 ? 44.963  -10.036 109.708 1.00 21.25 ? 494  ALA D N   1 
ATOM   17996 C  CA  . ALA D 1 502 ? 44.159  -10.391 110.875 1.00 21.63 ? 494  ALA D CA  1 
ATOM   17997 C  C   . ALA D 1 502 ? 42.859  -9.596  110.900 1.00 22.27 ? 494  ALA D C   1 
ATOM   17998 O  O   . ALA D 1 502 ? 41.775  -10.161 111.105 1.00 20.56 ? 494  ALA D O   1 
ATOM   17999 C  CB  . ALA D 1 502 ? 44.962  -10.172 112.161 1.00 22.57 ? 494  ALA D CB  1 
ATOM   18000 N  N   . GLU D 1 503 ? 42.939  -8.281  110.677 1.00 19.89 ? 495  GLU D N   1 
ATOM   18001 C  CA  . GLU D 1 503 ? 41.707  -7.502  110.582 1.00 18.96 ? 495  GLU D CA  1 
ATOM   18002 C  C   . GLU D 1 503 ? 40.867  -7.940  109.388 1.00 18.25 ? 495  GLU D C   1 
ATOM   18003 O  O   . GLU D 1 503 ? 39.637  -7.947  109.470 1.00 17.81 ? 495  GLU D O   1 
ATOM   18004 C  CB  . GLU D 1 503 ? 42.019  -6.001  110.505 1.00 18.38 ? 495  GLU D CB  1 
ATOM   18005 C  CG  . GLU D 1 503 ? 42.678  -5.437  111.785 1.00 19.07 ? 495  GLU D CG  1 
ATOM   18006 C  CD  . GLU D 1 503 ? 42.648  -3.909  111.848 1.00 20.96 ? 495  GLU D CD  1 
ATOM   18007 O  OE1 . GLU D 1 503 ? 42.275  -3.271  110.843 1.00 20.66 ? 495  GLU D OE1 1 
ATOM   18008 O  OE2 . GLU D 1 503 ? 42.995  -3.343  112.910 1.00 20.20 ? 495  GLU D OE2 1 
ATOM   18009 N  N   . SER D 1 504 ? 41.510  -8.339  108.284 1.00 18.21 ? 496  SER D N   1 
ATOM   18010 C  CA  A SER D 1 504 ? 40.752  -8.756  107.107 0.65 18.59 ? 496  SER D CA  1 
ATOM   18011 C  CA  B SER D 1 504 ? 40.760  -8.761  107.105 0.35 18.70 ? 496  SER D CA  1 
ATOM   18012 C  C   . SER D 1 504 ? 39.939  -10.014 107.391 1.00 18.04 ? 496  SER D C   1 
ATOM   18013 O  O   . SER D 1 504 ? 38.776  -10.112 106.987 1.00 17.48 ? 496  SER D O   1 
ATOM   18014 C  CB  A SER D 1 504 ? 41.688  -8.984  105.918 0.65 19.83 ? 496  SER D CB  1 
ATOM   18015 C  CB  B SER D 1 504 ? 41.720  -8.992  105.937 0.35 19.60 ? 496  SER D CB  1 
ATOM   18016 O  OG  A SER D 1 504 ? 42.243  -7.768  105.448 0.65 18.33 ? 496  SER D OG  1 
ATOM   18017 O  OG  B SER D 1 504 ? 41.049  -9.505  104.802 0.35 17.27 ? 496  SER D OG  1 
ATOM   18018 N  N   . LEU D 1 505 ? 40.527  -10.988 108.082 1.00 19.07 ? 497  LEU D N   1 
ATOM   18019 C  CA  . LEU D 1 505 ? 39.780  -12.201 108.390 1.00 22.02 ? 497  LEU D CA  1 
ATOM   18020 C  C   . LEU D 1 505 ? 38.607  -11.895 109.312 1.00 20.86 ? 497  LEU D C   1 
ATOM   18021 O  O   . LEU D 1 505 ? 37.502  -12.412 109.114 1.00 19.15 ? 497  LEU D O   1 
ATOM   18022 C  CB  . LEU D 1 505 ? 40.703  -13.256 109.008 1.00 23.80 ? 497  LEU D CB  1 
ATOM   18023 C  CG  . LEU D 1 505 ? 40.009  -14.550 109.456 1.00 25.09 ? 497  LEU D CG  1 
ATOM   18024 C  CD1 . LEU D 1 505 ? 39.375  -15.255 108.271 1.00 22.41 ? 497  LEU D CD1 1 
ATOM   18025 C  CD2 . LEU D 1 505 ? 40.964  -15.487 110.185 1.00 28.11 ? 497  LEU D CD2 1 
ATOM   18026 N  N   . VAL D 1 506 ? 38.818  -11.031 110.308 1.00 22.86 ? 498  VAL D N   1 
ATOM   18027 C  CA  . VAL D 1 506 ? 37.739  -10.681 111.227 1.00 19.31 ? 498  VAL D CA  1 
ATOM   18028 C  C   . VAL D 1 506 ? 36.650  -9.895  110.504 1.00 18.17 ? 498  VAL D C   1 
ATOM   18029 O  O   . VAL D 1 506 ? 35.454  -10.133 110.710 1.00 18.18 ? 498  VAL D O   1 
ATOM   18030 C  CB  . VAL D 1 506 ? 38.297  -9.892  112.426 1.00 23.69 ? 498  VAL D CB  1 
ATOM   18031 C  CG1 . VAL D 1 506 ? 37.161  -9.429  113.322 1.00 19.60 ? 498  VAL D CG1 1 
ATOM   18032 C  CG2 . VAL D 1 506 ? 39.294  -10.736 113.200 1.00 22.90 ? 498  VAL D CG2 1 
ATOM   18033 N  N   . ALA D 1 507 ? 37.045  -8.940  109.660 1.00 17.44 ? 499  ALA D N   1 
ATOM   18034 C  CA  . ALA D 1 507 ? 36.067  -8.176  108.890 1.00 16.42 ? 499  ALA D CA  1 
ATOM   18035 C  C   . ALA D 1 507 ? 35.199  -9.096  108.037 1.00 19.86 ? 499  ALA D C   1 
ATOM   18036 O  O   . ALA D 1 507 ? 33.970  -8.955  108.010 1.00 16.48 ? 499  ALA D O   1 
ATOM   18037 C  CB  . ALA D 1 507 ? 36.784  -7.145  108.014 1.00 17.33 ? 499  ALA D CB  1 
ATOM   18038 N  N   . TRP D 1 508 ? 35.824  -10.059 107.355 1.00 19.27 ? 500  TRP D N   1 
ATOM   18039 C  CA  . TRP D 1 508 ? 35.081  -11.035 106.560 1.00 20.19 ? 500  TRP D CA  1 
ATOM   18040 C  C   . TRP D 1 508 ? 34.166  -11.879 107.435 1.00 17.05 ? 500  TRP D C   1 
ATOM   18041 O  O   . TRP D 1 508 ? 32.997  -12.103 107.098 1.00 17.94 ? 500  TRP D O   1 
ATOM   18042 C  CB  . TRP D 1 508 ? 36.055  -11.940 105.802 1.00 24.05 ? 500  TRP D CB  1 
ATOM   18043 C  CG  . TRP D 1 508 ? 36.397  -11.450 104.434 1.00 16.43 ? 500  TRP D CG  1 
ATOM   18044 C  CD1 . TRP D 1 508 ? 37.547  -10.836 104.041 1.00 16.38 ? 500  TRP D CD1 1 
ATOM   18045 C  CD2 . TRP D 1 508 ? 35.580  -11.564 103.270 1.00 15.87 ? 500  TRP D CD2 1 
ATOM   18046 N  NE1 . TRP D 1 508 ? 37.483  -10.532 102.694 1.00 18.12 ? 500  TRP D NE1 1 
ATOM   18047 C  CE2 . TRP D 1 508 ? 36.288  -10.985 102.201 1.00 17.46 ? 500  TRP D CE2 1 
ATOM   18048 C  CE3 . TRP D 1 508 ? 34.317  -12.106 103.026 1.00 17.68 ? 500  TRP D CE3 1 
ATOM   18049 C  CZ2 . TRP D 1 508 ? 35.766  -10.927 100.904 1.00 18.66 ? 500  TRP D CZ2 1 
ATOM   18050 C  CZ3 . TRP D 1 508 ? 33.804  -12.047 101.740 1.00 19.75 ? 500  TRP D CZ3 1 
ATOM   18051 C  CH2 . TRP D 1 508 ? 34.531  -11.471 100.697 1.00 17.52 ? 500  TRP D CH2 1 
ATOM   18052 N  N   . ALA D 1 509 ? 34.689  -12.372 108.557 1.00 20.98 ? 501  ALA D N   1 
ATOM   18053 C  CA  . ALA D 1 509 ? 33.886  -13.224 109.428 1.00 19.69 ? 501  ALA D CA  1 
ATOM   18054 C  C   . ALA D 1 509 ? 32.705  -12.460 110.015 1.00 21.44 ? 501  ALA D C   1 
ATOM   18055 O  O   . ALA D 1 509 ? 31.592  -12.993 110.100 1.00 18.69 ? 501  ALA D O   1 
ATOM   18056 C  CB  . ALA D 1 509 ? 34.762  -13.804 110.540 1.00 19.71 ? 501  ALA D CB  1 
ATOM   18057 N  N   . GLU D 1 510 ? 32.927  -11.213 110.437 1.00 17.68 ? 502  GLU D N   1 
ATOM   18058 C  CA  . GLU D 1 510 ? 31.824  -10.414 110.970 1.00 18.30 ? 502  GLU D CA  1 
ATOM   18059 C  C   . GLU D 1 510 ? 30.795  -10.092 109.895 1.00 19.53 ? 502  GLU D C   1 
ATOM   18060 O  O   . GLU D 1 510 ? 29.583  -10.080 110.164 1.00 18.66 ? 502  GLU D O   1 
ATOM   18061 C  CB  . GLU D 1 510 ? 32.363  -9.130  111.600 1.00 21.76 ? 502  GLU D CB  1 
ATOM   18062 C  CG  . GLU D 1 510 ? 33.116  -9.384  112.894 1.00 18.90 ? 502  GLU D CG  1 
ATOM   18063 C  CD  . GLU D 1 510 ? 32.251  -10.054 113.938 1.00 21.02 ? 502  GLU D CD  1 
ATOM   18064 O  OE1 . GLU D 1 510 ? 31.152  -9.535  114.227 1.00 22.21 ? 502  GLU D OE1 1 
ATOM   18065 O  OE2 . GLU D 1 510 ? 32.670  -11.112 114.463 1.00 25.11 ? 502  GLU D OE2 1 
ATOM   18066 N  N   . ALA D 1 511 ? 31.256  -9.813  108.675 1.00 18.29 ? 503  ALA D N   1 
ATOM   18067 C  CA  . ALA D 1 511 ? 30.330  -9.586  107.573 1.00 14.97 ? 503  ALA D CA  1 
ATOM   18068 C  C   . ALA D 1 511 ? 29.516  -10.840 107.278 1.00 19.50 ? 503  ALA D C   1 
ATOM   18069 O  O   . ALA D 1 511 ? 28.319  -10.753 106.981 1.00 22.29 ? 503  ALA D O   1 
ATOM   18070 C  CB  . ALA D 1 511 ? 31.094  -9.128  106.333 1.00 14.46 ? 503  ALA D CB  1 
ATOM   18071 N  N   . ALA D 1 512 ? 30.145  -12.021 107.369 1.00 19.11 ? 504  ALA D N   1 
ATOM   18072 C  CA  . ALA D 1 512 ? 29.414  -13.270 107.161 1.00 19.77 ? 504  ALA D CA  1 
ATOM   18073 C  C   . ALA D 1 512 ? 28.408  -13.524 108.273 1.00 22.03 ? 504  ALA D C   1 
ATOM   18074 O  O   . ALA D 1 512 ? 27.345  -14.107 108.029 1.00 22.55 ? 504  ALA D O   1 
ATOM   18075 C  CB  . ALA D 1 512 ? 30.387  -14.454 107.075 1.00 18.07 ? 504  ALA D CB  1 
ATOM   18076 N  N   . LYS D 1 513 ? 28.731  -13.104 109.497 1.00 20.70 ? 505  LYS D N   1 
ATOM   18077 C  CA  . LYS D 1 513 ? 27.882  -13.378 110.652 1.00 23.33 ? 505  LYS D CA  1 
ATOM   18078 C  C   . LYS D 1 513 ? 26.688  -12.430 110.748 1.00 22.62 ? 505  LYS D C   1 
ATOM   18079 O  O   . LYS D 1 513 ? 25.671  -12.785 111.357 1.00 24.57 ? 505  LYS D O   1 
ATOM   18080 C  CB  . LYS D 1 513 ? 28.697  -13.266 111.937 1.00 26.37 ? 505  LYS D CB  1 
ATOM   18081 C  CG  . LYS D 1 513 ? 29.564  -14.456 112.265 1.00 34.99 ? 505  LYS D CG  1 
ATOM   18082 C  CD  . LYS D 1 513 ? 30.468  -14.132 113.445 1.00 39.71 ? 505  LYS D CD  1 
ATOM   18083 C  CE  . LYS D 1 513 ? 29.676  -13.708 114.675 1.00 45.14 ? 505  LYS D CE  1 
ATOM   18084 N  NZ  . LYS D 1 513 ? 30.582  -13.344 115.814 1.00 46.23 ? 505  LYS D NZ  1 
ATOM   18085 N  N   . ALA D 1 514 ? 26.810  -11.220 110.211 1.00 18.74 ? 506  ALA D N   1 
ATOM   18086 C  CA  . ALA D 1 514 ? 25.722  -10.252 110.287 1.00 27.09 ? 506  ALA D CA  1 
ATOM   18087 C  C   . ALA D 1 514 ? 24.462  -10.847 109.685 1.00 26.85 ? 506  ALA D C   1 
ATOM   18088 O  O   . ALA D 1 514 ? 24.477  -11.356 108.562 1.00 29.47 ? 506  ALA D O   1 
ATOM   18089 C  CB  . ALA D 1 514 ? 26.095  -8.961  109.556 1.00 16.75 ? 506  ALA D CB  1 
ATOM   18090 N  N   . GLU D 1 515 ? 23.377  -10.815 110.449 1.00 21.79 ? 507  GLU D N   1 
ATOM   18091 C  CA  . GLU D 1 515 ? 22.136  -11.406 109.977 1.00 25.21 ? 507  GLU D CA  1 
ATOM   18092 C  C   . GLU D 1 515 ? 21.229  -10.396 109.283 1.00 29.92 ? 507  GLU D C   1 
ATOM   18093 O  O   . GLU D 1 515 ? 20.537  -10.762 108.329 1.00 30.57 ? 507  GLU D O   1 
ATOM   18094 C  CB  . GLU D 1 515 ? 21.400  -12.071 111.146 1.00 35.10 ? 507  GLU D CB  1 
ATOM   18095 C  CG  . GLU D 1 515 ? 22.192  -13.227 111.758 1.00 41.54 ? 507  GLU D CG  1 
ATOM   18096 C  CD  . GLU D 1 515 ? 21.418  -14.005 112.809 1.00 52.91 ? 507  GLU D CD  1 
ATOM   18097 O  OE1 . GLU D 1 515 ? 21.980  -14.978 113.357 1.00 56.46 ? 507  GLU D OE1 1 
ATOM   18098 O  OE2 . GLU D 1 515 ? 20.253  -13.651 113.088 1.00 57.29 ? 507  GLU D OE2 1 
ATOM   18099 N  N   . ASP D 1 516 ? 21.245  -9.126  109.706 1.00 22.67 ? 508  ASP D N   1 
ATOM   18100 C  CA  . ASP D 1 516 ? 20.257  -8.155  109.245 1.00 21.59 ? 508  ASP D CA  1 
ATOM   18101 C  C   . ASP D 1 516 ? 20.876  -6.915  108.598 1.00 18.51 ? 508  ASP D C   1 
ATOM   18102 O  O   . ASP D 1 516 ? 20.204  -5.885  108.522 1.00 18.62 ? 508  ASP D O   1 
ATOM   18103 C  CB  . ASP D 1 516 ? 19.351  -7.725  110.404 1.00 24.03 ? 508  ASP D CB  1 
ATOM   18104 C  CG  . ASP D 1 516 ? 20.101  -6.912  111.460 1.00 25.78 ? 508  ASP D CG  1 
ATOM   18105 O  OD1 . ASP D 1 516 ? 21.346  -6.961  111.473 1.00 24.09 ? 508  ASP D OD1 1 
ATOM   18106 O  OD2 . ASP D 1 516 ? 19.454  -6.224  112.273 1.00 28.60 ? 508  ASP D OD2 1 
ATOM   18107 N  N   . HIS D 1 517 ? 22.129  -6.970  108.139 1.00 17.11 ? 509  HIS D N   1 
ATOM   18108 C  CA  . HIS D 1 517 ? 22.694  -5.797  107.478 1.00 18.38 ? 509  HIS D CA  1 
ATOM   18109 C  C   . HIS D 1 517 ? 23.825  -6.208  106.558 1.00 16.68 ? 509  HIS D C   1 
ATOM   18110 O  O   . HIS D 1 517 ? 24.489  -7.225  106.801 1.00 14.76 ? 509  HIS D O   1 
ATOM   18111 C  CB  . HIS D 1 517 ? 23.190  -4.733  108.476 1.00 15.64 ? 509  HIS D CB  1 
ATOM   18112 C  CG  . HIS D 1 517 ? 24.211  -5.223  109.454 1.00 19.00 ? 509  HIS D CG  1 
ATOM   18113 N  ND1 . HIS D 1 517 ? 23.862  -5.825  110.642 1.00 20.93 ? 509  HIS D ND1 1 
ATOM   18114 C  CD2 . HIS D 1 517 ? 25.565  -5.154  109.449 1.00 19.06 ? 509  HIS D CD2 1 
ATOM   18115 C  CE1 . HIS D 1 517 ? 24.958  -6.134  111.315 1.00 25.07 ? 509  HIS D CE1 1 
ATOM   18116 N  NE2 . HIS D 1 517 ? 26.004  -5.738  110.613 1.00 21.26 ? 509  HIS D NE2 1 
ATOM   18117 N  N   . PRO D 1 518 ? 24.052  -5.448  105.491 1.00 15.83 ? 510  PRO D N   1 
ATOM   18118 C  CA  . PRO D 1 518 ? 25.165  -5.718  104.580 1.00 17.66 ? 510  PRO D CA  1 
ATOM   18119 C  C   . PRO D 1 518 ? 26.455  -5.095  105.089 1.00 15.18 ? 510  PRO D C   1 
ATOM   18120 O  O   . PRO D 1 518 ? 26.477  -4.315  106.041 1.00 14.53 ? 510  PRO D O   1 
ATOM   18121 C  CB  . PRO D 1 518 ? 24.715  -5.045  103.274 1.00 12.14 ? 510  PRO D CB  1 
ATOM   18122 C  CG  . PRO D 1 518 ? 23.908  -3.828  103.776 1.00 12.39 ? 510  PRO D CG  1 
ATOM   18123 C  CD  . PRO D 1 518 ? 23.216  -4.313  105.045 1.00 13.93 ? 510  PRO D CD  1 
ATOM   18124 N  N   . SER D 1 519 ? 27.536  -5.440  104.405 1.00 17.66 ? 511  SER D N   1 
ATOM   18125 C  CA  . SER D 1 519 ? 28.856  -4.915  104.712 1.00 17.33 ? 511  SER D CA  1 
ATOM   18126 C  C   . SER D 1 519 ? 29.562  -4.523  103.426 1.00 15.56 ? 511  SER D C   1 
ATOM   18127 O  O   . SER D 1 519 ? 29.403  -5.173  102.389 1.00 14.83 ? 511  SER D O   1 
ATOM   18128 C  CB  . SER D 1 519 ? 29.710  -5.944  105.474 1.00 13.50 ? 511  SER D CB  1 
ATOM   18129 O  OG  . SER D 1 519 ? 29.090  -6.294  106.697 1.00 15.84 ? 511  SER D OG  1 
ATOM   18130 N  N   . CYS D 1 520 ? 30.357  -3.458  103.511 1.00 11.46 ? 512  CYS D N   1 
ATOM   18131 C  CA  . CYS D 1 520 ? 31.334  -3.109  102.494 1.00 13.80 ? 512  CYS D CA  1 
ATOM   18132 C  C   . CYS D 1 520 ? 32.710  -3.426  103.053 1.00 15.25 ? 512  CYS D C   1 
ATOM   18133 O  O   . CYS D 1 520 ? 33.076  -2.919  104.116 1.00 14.34 ? 512  CYS D O   1 
ATOM   18134 C  CB  . CYS D 1 520 ? 31.245  -1.630  102.121 1.00 14.28 ? 512  CYS D CB  1 
ATOM   18135 S  SG  . CYS D 1 520 ? 29.653  -1.115  101.407 1.00 15.47 ? 512  CYS D SG  1 
ATOM   18136 N  N   . LEU D 1 521 ? 33.463  -4.261  102.352 1.00 15.90 ? 513  LEU D N   1 
ATOM   18137 C  CA  . LEU D 1 521 ? 34.818  -4.608  102.761 1.00 15.97 ? 513  LEU D CA  1 
ATOM   18138 C  C   . LEU D 1 521 ? 35.785  -3.948  101.786 1.00 17.19 ? 513  LEU D C   1 
ATOM   18139 O  O   . LEU D 1 521 ? 35.748  -4.239  100.586 1.00 14.11 ? 513  LEU D O   1 
ATOM   18140 C  CB  . LEU D 1 521 ? 35.009  -6.123  102.795 1.00 13.95 ? 513  LEU D CB  1 
ATOM   18141 C  CG  . LEU D 1 521 ? 33.951  -6.927  103.555 1.00 16.96 ? 513  LEU D CG  1 
ATOM   18142 C  CD1 . LEU D 1 521 ? 34.368  -8.383  103.611 1.00 13.43 ? 513  LEU D CD1 1 
ATOM   18143 C  CD2 . LEU D 1 521 ? 33.746  -6.380  104.977 1.00 15.98 ? 513  LEU D CD2 1 
ATOM   18144 N  N   . ILE D 1 522 ? 36.630  -3.054  102.302 1.00 12.46 ? 514  ILE D N   1 
ATOM   18145 C  CA  . ILE D 1 522 ? 37.440  -2.146  101.494 1.00 12.66 ? 514  ILE D CA  1 
ATOM   18146 C  C   . ILE D 1 522 ? 38.916  -2.490  101.687 1.00 14.30 ? 514  ILE D C   1 
ATOM   18147 O  O   . ILE D 1 522 ? 39.426  -2.408  102.812 1.00 15.61 ? 514  ILE D O   1 
ATOM   18148 C  CB  . ILE D 1 522 ? 37.163  -0.685  101.878 1.00 12.34 ? 514  ILE D CB  1 
ATOM   18149 C  CG1 . ILE D 1 522 ? 35.715  -0.306  101.530 1.00 14.67 ? 514  ILE D CG1 1 
ATOM   18150 C  CG2 . ILE D 1 522 ? 38.118  0.240   101.155 1.00 13.19 ? 514  ILE D CG2 1 
ATOM   18151 C  CD1 . ILE D 1 522 ? 35.315  1.088   102.020 1.00 18.07 ? 514  ILE D CD1 1 
ATOM   18152 N  N   . PHE D 1 523 ? 39.612  -2.846  100.595 1.00 14.63 ? 515  PHE D N   1 
ATOM   18153 C  CA  . PHE D 1 523 ? 40.985  -3.357  100.658 1.00 16.65 ? 515  PHE D CA  1 
ATOM   18154 C  C   . PHE D 1 523 ? 41.954  -2.534  99.814  1.00 21.65 ? 515  PHE D C   1 
ATOM   18155 O  O   . PHE D 1 523 ? 41.617  -2.058  98.722  1.00 18.58 ? 515  PHE D O   1 
ATOM   18156 C  CB  . PHE D 1 523 ? 41.048  -4.826  100.205 1.00 16.63 ? 515  PHE D CB  1 
ATOM   18157 C  CG  . PHE D 1 523 ? 40.191  -5.740  101.032 1.00 17.60 ? 515  PHE D CG  1 
ATOM   18158 C  CD1 . PHE D 1 523 ? 40.648  -6.228  102.249 1.00 24.91 ? 515  PHE D CD1 1 
ATOM   18159 C  CD2 . PHE D 1 523 ? 38.917  -6.088  100.613 1.00 18.06 ? 515  PHE D CD2 1 
ATOM   18160 C  CE1 . PHE D 1 523 ? 39.858  -7.057  103.017 1.00 20.94 ? 515  PHE D CE1 1 
ATOM   18161 C  CE2 . PHE D 1 523 ? 38.116  -6.911  101.390 1.00 16.69 ? 515  PHE D CE2 1 
ATOM   18162 C  CZ  . PHE D 1 523 ? 38.591  -7.395  102.589 1.00 20.10 ? 515  PHE D CZ  1 
ATOM   18163 N  N   . SER D 1 524 ? 43.174  -2.391  100.309 1.00 24.30 ? 516  SER D N   1 
ATOM   18164 C  CA  . SER D 1 524 ? 44.177  -1.634  99.583  1.00 30.04 ? 516  SER D CA  1 
ATOM   18165 C  C   . SER D 1 524 ? 44.929  -2.546  98.634  1.00 42.20 ? 516  SER D C   1 
ATOM   18166 O  O   . SER D 1 524 ? 45.046  -3.754  98.861  1.00 39.57 ? 516  SER D O   1 
ATOM   18167 C  CB  . SER D 1 524 ? 45.163  -0.958  100.535 1.00 31.67 ? 516  SER D CB  1 
ATOM   18168 O  OG  . SER D 1 524 ? 45.886  -1.922  101.273 1.00 32.52 ? 516  SER D OG  1 
ATOM   18169 N  N   . ARG D 1 525 ? 45.432  -1.947  97.553  1.00 60.65 ? 517  ARG D N   1 
ATOM   18170 C  CA  . ARG D 1 525 ? 46.312  -2.667  96.641  1.00 72.15 ? 517  ARG D CA  1 
ATOM   18171 C  C   . ARG D 1 525 ? 47.552  -3.162  97.371  1.00 74.79 ? 517  ARG D C   1 
ATOM   18172 O  O   . ARG D 1 525 ? 47.913  -4.341  97.282  1.00 74.80 ? 517  ARG D O   1 
ATOM   18173 C  CB  . ARG D 1 525 ? 46.691  -1.765  95.464  1.00 75.34 ? 517  ARG D CB  1 
ATOM   18174 N  N   . GLN D 1 526 ? 48.200  -2.274  98.120  1.00 77.10 ? 518  GLN D N   1 
ATOM   18175 C  CA  . GLN D 1 526 ? 49.421  -2.632  98.827  1.00 77.43 ? 518  GLN D CA  1 
ATOM   18176 C  C   . GLN D 1 526 ? 49.108  -3.543  100.005 1.00 72.53 ? 518  GLN D C   1 
ATOM   18177 O  O   . GLN D 1 526 ? 48.263  -3.222  100.845 1.00 65.27 ? 518  GLN D O   1 
ATOM   18178 C  CB  . GLN D 1 526 ? 50.140  -1.372  99.311  1.00 77.72 ? 518  GLN D CB  1 
ATOM   18179 N  N   . ASN D 1 527 ? 49.785  -4.688  100.058 1.00 76.58 ? 519  ASN D N   1 
ATOM   18180 C  CA  . ASN D 1 527 ? 49.740  -5.534  101.242 1.00 72.57 ? 519  ASN D CA  1 
ATOM   18181 C  C   . ASN D 1 527 ? 50.424  -4.806  102.394 1.00 67.68 ? 519  ASN D C   1 
ATOM   18182 O  O   . ASN D 1 527 ? 51.590  -4.409  102.285 1.00 71.40 ? 519  ASN D O   1 
ATOM   18183 C  CB  . ASN D 1 527 ? 50.415  -6.876  100.964 1.00 73.05 ? 519  ASN D CB  1 
ATOM   18184 N  N   . LEU D 1 528 ? 49.700  -4.622  103.491 1.00 56.87 ? 520  LEU D N   1 
ATOM   18185 C  CA  . LEU D 1 528 ? 50.143  -3.770  104.584 1.00 55.34 ? 520  LEU D CA  1 
ATOM   18186 C  C   . LEU D 1 528 ? 50.850  -4.589  105.654 1.00 54.64 ? 520  LEU D C   1 
ATOM   18187 O  O   . LEU D 1 528 ? 50.469  -5.731  105.927 1.00 55.42 ? 520  LEU D O   1 
ATOM   18188 C  CB  . LEU D 1 528 ? 48.952  -3.029  105.186 1.00 51.82 ? 520  LEU D CB  1 
ATOM   18189 C  CG  . LEU D 1 528 ? 48.015  -2.490  104.106 1.00 44.62 ? 520  LEU D CG  1 
ATOM   18190 C  CD1 . LEU D 1 528 ? 46.671  -2.078  104.691 1.00 36.02 ? 520  LEU D CD1 1 
ATOM   18191 C  CD2 . LEU D 1 528 ? 48.678  -1.339  103.369 1.00 48.40 ? 520  LEU D CD2 1 
ATOM   18192 N  N   . LYS D 1 529 ? 51.878  -3.994  106.258 1.00 57.67 ? 521  LYS D N   1 
ATOM   18193 C  CA  . LYS D 1 529 ? 52.694  -4.698  107.240 1.00 60.39 ? 521  LYS D CA  1 
ATOM   18194 C  C   . LYS D 1 529 ? 51.846  -5.136  108.428 1.00 58.06 ? 521  LYS D C   1 
ATOM   18195 O  O   . LYS D 1 529 ? 50.869  -4.481  108.801 1.00 57.00 ? 521  LYS D O   1 
ATOM   18196 C  CB  . LYS D 1 529 ? 53.850  -3.814  107.716 1.00 60.09 ? 521  LYS D CB  1 
ATOM   18197 N  N   . PHE D 1 530 ? 52.234  -6.259  109.023 1.00 62.53 ? 522  PHE D N   1 
ATOM   18198 C  CA  . PHE D 1 530 ? 51.472  -6.872  110.102 1.00 62.61 ? 522  PHE D CA  1 
ATOM   18199 C  C   . PHE D 1 530 ? 51.933  -6.314  111.446 1.00 65.11 ? 522  PHE D C   1 
ATOM   18200 O  O   . PHE D 1 530 ? 53.117  -6.403  111.791 1.00 69.50 ? 522  PHE D O   1 
ATOM   18201 C  CB  . PHE D 1 530 ? 51.626  -8.391  110.068 1.00 59.44 ? 522  PHE D CB  1 
ATOM   18202 C  CG  . PHE D 1 530 ? 50.661  -9.116  110.959 1.00 55.14 ? 522  PHE D CG  1 
ATOM   18203 C  CD1 . PHE D 1 530 ? 49.429  -9.525  110.477 1.00 51.88 ? 522  PHE D CD1 1 
ATOM   18204 C  CD2 . PHE D 1 530 ? 50.979  -9.380  112.280 1.00 53.63 ? 522  PHE D CD2 1 
ATOM   18205 C  CE1 . PHE D 1 530 ? 48.536  -10.191 111.294 1.00 50.95 ? 522  PHE D CE1 1 
ATOM   18206 C  CE2 . PHE D 1 530 ? 50.089  -10.047 113.104 1.00 52.82 ? 522  PHE D CE2 1 
ATOM   18207 C  CZ  . PHE D 1 530 ? 48.868  -10.453 112.611 1.00 50.53 ? 522  PHE D CZ  1 
ATOM   18208 N  N   . GLN D 1 531 ? 50.995  -5.748  112.201 1.00 60.24 ? 523  GLN D N   1 
ATOM   18209 C  CA  . GLN D 1 531 ? 51.275  -5.257  113.543 1.00 55.78 ? 523  GLN D CA  1 
ATOM   18210 C  C   . GLN D 1 531 ? 51.142  -6.390  114.552 1.00 50.79 ? 523  GLN D C   1 
ATOM   18211 O  O   . GLN D 1 531 ? 50.265  -7.249  114.427 1.00 50.69 ? 523  GLN D O   1 
ATOM   18212 C  CB  . GLN D 1 531 ? 50.319  -4.121  113.909 1.00 54.62 ? 523  GLN D CB  1 
ATOM   18213 N  N   . ALA D 1 532 ? 52.014  -6.387  115.554 1.00 48.88 ? 524  ALA D N   1 
ATOM   18214 C  CA  . ALA D 1 532 ? 51.926  -7.388  116.606 1.00 43.35 ? 524  ALA D CA  1 
ATOM   18215 C  C   . ALA D 1 532 ? 50.666  -7.168  117.435 1.00 42.87 ? 524  ALA D C   1 
ATOM   18216 O  O   . ALA D 1 532 ? 50.236  -6.029  117.650 1.00 41.01 ? 524  ALA D O   1 
ATOM   18217 C  CB  . ALA D 1 532 ? 53.163  -7.333  117.496 1.00 47.20 ? 524  ALA D CB  1 
ATOM   18218 N  N   . ARG D 1 533 ? 50.059  -8.266  117.892 1.00 42.40 ? 525  ARG D N   1 
ATOM   18219 C  CA  . ARG D 1 533 ? 48.813  -8.179  118.637 1.00 27.02 ? 525  ARG D CA  1 
ATOM   18220 C  C   . ARG D 1 533 ? 48.773  -9.195  119.767 1.00 32.80 ? 525  ARG D C   1 
ATOM   18221 O  O   . ARG D 1 533 ? 49.209  -10.340 119.609 1.00 37.89 ? 525  ARG D O   1 
ATOM   18222 C  CB  . ARG D 1 533 ? 47.599  -8.386  117.726 1.00 27.41 ? 525  ARG D CB  1 
ATOM   18223 C  CG  . ARG D 1 533 ? 47.194  -7.144  116.977 1.00 28.80 ? 525  ARG D CG  1 
ATOM   18224 C  CD  . ARG D 1 533 ? 45.842  -7.330  116.330 1.00 32.02 ? 525  ARG D CD  1 
ATOM   18225 N  NE  . ARG D 1 533 ? 45.642  -6.382  115.243 1.00 31.22 ? 525  ARG D NE  1 
ATOM   18226 C  CZ  . ARG D 1 533 ? 46.173  -6.526  114.035 1.00 28.53 ? 525  ARG D CZ  1 
ATOM   18227 N  NH1 . ARG D 1 533 ? 46.942  -7.574  113.767 1.00 29.50 ? 525  ARG D NH1 1 
ATOM   18228 N  NH2 . ARG D 1 533 ? 45.940  -5.621  113.099 1.00 32.10 ? 525  ARG D NH2 1 
ATOM   18229 N  N   . SER D 1 534 ? 48.244  -8.760  120.907 1.00 28.37 ? 526  SER D N   1 
ATOM   18230 C  CA  . SER D 1 534 ? 47.939  -9.658  122.007 1.00 29.77 ? 526  SER D CA  1 
ATOM   18231 C  C   . SER D 1 534 ? 46.666  -10.436 121.695 1.00 29.35 ? 526  SER D C   1 
ATOM   18232 O  O   . SER D 1 534 ? 45.936  -10.126 120.755 1.00 27.77 ? 526  SER D O   1 
ATOM   18233 C  CB  . SER D 1 534 ? 47.770  -8.875  123.308 1.00 29.95 ? 526  SER D CB  1 
ATOM   18234 O  OG  . SER D 1 534 ? 46.625  -8.035  123.236 1.00 30.47 ? 526  SER D OG  1 
ATOM   18235 N  N   . GLU D 1 535 ? 46.397  -11.463 122.505 1.00 33.43 ? 527  GLU D N   1 
ATOM   18236 C  CA  . GLU D 1 535 ? 45.140  -12.189 122.355 1.00 33.85 ? 527  GLU D CA  1 
ATOM   18237 C  C   . GLU D 1 535 ? 43.946  -11.254 122.530 1.00 31.75 ? 527  GLU D C   1 
ATOM   18238 O  O   . GLU D 1 535 ? 42.995  -11.301 121.745 1.00 29.92 ? 527  GLU D O   1 
ATOM   18239 C  CB  . GLU D 1 535 ? 45.075  -13.344 123.355 1.00 37.34 ? 527  GLU D CB  1 
ATOM   18240 N  N   . GLN D 1 536 ? 43.986  -10.389 123.549 1.00 34.48 ? 528  GLN D N   1 
ATOM   18241 C  CA  . GLN D 1 536 ? 42.889  -9.452  123.784 1.00 32.40 ? 528  GLN D CA  1 
ATOM   18242 C  C   . GLN D 1 536 ? 42.695  -8.510  122.598 1.00 32.00 ? 528  GLN D C   1 
ATOM   18243 O  O   . GLN D 1 536 ? 41.560  -8.239  122.182 1.00 26.00 ? 528  GLN D O   1 
ATOM   18244 C  CB  . GLN D 1 536 ? 43.152  -8.657  125.067 1.00 32.16 ? 528  GLN D CB  1 
ATOM   18245 C  CG  . GLN D 1 536 ? 42.111  -7.594  125.361 1.00 31.63 ? 528  GLN D CG  1 
ATOM   18246 C  CD  . GLN D 1 536 ? 40.764  -8.190  125.705 1.00 35.47 ? 528  GLN D CD  1 
ATOM   18247 O  OE1 . GLN D 1 536 ? 40.680  -9.183  126.432 1.00 40.90 ? 528  GLN D OE1 1 
ATOM   18248 N  NE2 . GLN D 1 536 ? 39.701  -7.589  125.190 1.00 30.97 ? 528  GLN D NE2 1 
ATOM   18249 N  N   . GLN D 1 537 ? 43.793  -7.999  122.042 1.00 30.77 ? 529  GLN D N   1 
ATOM   18250 C  CA  . GLN D 1 537 ? 43.694  -7.136  120.871 1.00 30.65 ? 529  GLN D CA  1 
ATOM   18251 C  C   . GLN D 1 537 ? 43.047  -7.864  119.701 1.00 25.87 ? 529  GLN D C   1 
ATOM   18252 O  O   . GLN D 1 537 ? 42.196  -7.298  119.010 1.00 28.54 ? 529  GLN D O   1 
ATOM   18253 C  CB  . GLN D 1 537 ? 45.079  -6.618  120.486 1.00 27.61 ? 529  GLN D CB  1 
ATOM   18254 C  CG  . GLN D 1 537 ? 45.579  -5.473  121.352 1.00 29.15 ? 529  GLN D CG  1 
ATOM   18255 C  CD  . GLN D 1 537 ? 47.027  -5.121  121.067 1.00 33.77 ? 529  GLN D CD  1 
ATOM   18256 O  OE1 . GLN D 1 537 ? 47.879  -6.000  120.984 1.00 34.39 ? 529  GLN D OE1 1 
ATOM   18257 N  NE2 . GLN D 1 537 ? 47.307  -3.834  120.904 1.00 31.87 ? 529  GLN D NE2 1 
ATOM   18258 N  N   . LEU D 1 538 ? 43.436  -9.122  119.463 1.00 32.03 ? 530  LEU D N   1 
ATOM   18259 C  CA  . LEU D 1 538 ? 42.831  -9.894  118.376 1.00 27.48 ? 530  LEU D CA  1 
ATOM   18260 C  C   . LEU D 1 538 ? 41.335  -10.062 118.588 1.00 30.00 ? 530  LEU D C   1 
ATOM   18261 O  O   . LEU D 1 538 ? 40.550  -10.009 117.631 1.00 29.17 ? 530  LEU D O   1 
ATOM   18262 C  CB  . LEU D 1 538 ? 43.497  -11.268 118.263 1.00 30.88 ? 530  LEU D CB  1 
ATOM   18263 C  CG  . LEU D 1 538 ? 44.823  -11.404 117.524 1.00 33.75 ? 530  LEU D CG  1 
ATOM   18264 C  CD1 . LEU D 1 538 ? 45.422  -12.769 117.812 1.00 39.86 ? 530  LEU D CD1 1 
ATOM   18265 C  CD2 . LEU D 1 538 ? 44.628  -11.219 116.031 1.00 31.55 ? 530  LEU D CD2 1 
ATOM   18266 N  N   . ASN D 1 539 ? 40.917  -10.269 119.836 1.00 24.62 ? 531  ASN D N   1 
ATOM   18267 C  CA  . ASN D 1 539 ? 39.497  -10.439 120.100 1.00 27.89 ? 531  ASN D CA  1 
ATOM   18268 C  C   . ASN D 1 539 ? 38.726  -9.132  120.014 1.00 23.22 ? 531  ASN D C   1 
ATOM   18269 O  O   . ASN D 1 539 ? 37.504  -9.168  119.864 1.00 29.64 ? 531  ASN D O   1 
ATOM   18270 C  CB  . ASN D 1 539 ? 39.294  -11.078 121.471 1.00 34.04 ? 531  ASN D CB  1 
ATOM   18271 C  CG  . ASN D 1 539 ? 39.744  -12.519 121.501 1.00 32.52 ? 531  ASN D CG  1 
ATOM   18272 O  OD1 . ASN D 1 539 ? 39.723  -13.208 120.481 1.00 34.79 ? 531  ASN D OD1 1 
ATOM   18273 N  ND2 . ASN D 1 539 ? 40.156  -12.983 122.665 1.00 32.44 ? 531  ASN D ND2 1 
ATOM   18274 N  N   . ASP D 1 540 ? 39.402  -7.984  120.102 1.00 22.47 ? 532  ASP D N   1 
ATOM   18275 C  CA  . ASP D 1 540 ? 38.715  -6.699  120.064 1.00 24.63 ? 532  ASP D CA  1 
ATOM   18276 C  C   . ASP D 1 540 ? 38.581  -6.128  118.659 1.00 20.80 ? 532  ASP D C   1 
ATOM   18277 O  O   . ASP D 1 540 ? 37.859  -5.139  118.478 1.00 20.42 ? 532  ASP D O   1 
ATOM   18278 C  CB  . ASP D 1 540 ? 39.426  -5.678  120.962 1.00 21.75 ? 532  ASP D CB  1 
ATOM   18279 C  CG  . ASP D 1 540 ? 39.093  -5.863  122.429 1.00 25.48 ? 532  ASP D CG  1 
ATOM   18280 O  OD1 . ASP D 1 540 ? 38.059  -6.495  122.735 1.00 30.98 ? 532  ASP D OD1 1 
ATOM   18281 O  OD2 . ASP D 1 540 ? 39.859  -5.376  123.276 1.00 27.17 ? 532  ASP D OD2 1 
ATOM   18282 N  N   . ILE D 1 541 ? 39.239  -6.730  117.663 1.00 19.46 ? 533  ILE D N   1 
ATOM   18283 C  CA  . ILE D 1 541 ? 39.068  -6.272  116.285 1.00 18.13 ? 533  ILE D CA  1 
ATOM   18284 C  C   . ILE D 1 541 ? 37.593  -6.248  115.909 1.00 17.96 ? 533  ILE D C   1 
ATOM   18285 O  O   . ILE D 1 541 ? 37.116  -5.307  115.267 1.00 17.46 ? 533  ILE D O   1 
ATOM   18286 C  CB  . ILE D 1 541 ? 39.871  -7.161  115.313 1.00 20.61 ? 533  ILE D CB  1 
ATOM   18287 C  CG1 . ILE D 1 541 ? 41.365  -7.092  115.601 1.00 19.09 ? 533  ILE D CG1 1 
ATOM   18288 C  CG2 . ILE D 1 541 ? 39.591  -6.744  113.865 1.00 19.84 ? 533  ILE D CG2 1 
ATOM   18289 C  CD1 . ILE D 1 541 ? 42.175  -8.137  114.818 1.00 20.00 ? 533  ILE D CD1 1 
ATOM   18290 N  N   . LYS D 1 542 ? 36.837  -7.270  116.323 1.00 20.28 ? 534  LYS D N   1 
ATOM   18291 C  CA  . LYS D 1 542 ? 35.423  -7.314  115.950 1.00 21.33 ? 534  LYS D CA  1 
ATOM   18292 C  C   . LYS D 1 542 ? 34.592  -6.224  116.615 1.00 21.43 ? 534  LYS D C   1 
ATOM   18293 O  O   . LYS D 1 542 ? 33.419  -6.076  116.264 1.00 21.69 ? 534  LYS D O   1 
ATOM   18294 C  CB  . LYS D 1 542 ? 34.822  -8.675  116.284 1.00 19.31 ? 534  LYS D CB  1 
ATOM   18295 C  CG  . LYS D 1 542 ? 34.847  -8.994  117.778 1.00 20.90 ? 534  LYS D CG  1 
ATOM   18296 C  CD  . LYS D 1 542 ? 34.085  -10.272 118.067 1.00 29.72 ? 534  LYS D CD  1 
ATOM   18297 C  CE  . LYS D 1 542 ? 34.848  -11.152 119.017 1.00 36.97 ? 534  LYS D CE  1 
ATOM   18298 N  NZ  . LYS D 1 542 ? 36.093  -11.644 118.378 1.00 34.83 ? 534  LYS D NZ  1 
ATOM   18299 N  N   . ARG D 1 543 ? 35.156  -5.462  117.555 1.00 19.82 ? 535  ARG D N   1 
ATOM   18300 C  CA  . ARG D 1 543 ? 34.447  -4.346  118.169 1.00 18.50 ? 535  ARG D CA  1 
ATOM   18301 C  C   . ARG D 1 543 ? 34.596  -3.041  117.383 1.00 17.31 ? 535  ARG D C   1 
ATOM   18302 O  O   . ARG D 1 543 ? 34.135  -1.994  117.850 1.00 17.58 ? 535  ARG D O   1 
ATOM   18303 C  CB  . ARG D 1 543 ? 34.907  -4.148  119.617 1.00 23.14 ? 535  ARG D CB  1 
ATOM   18304 C  CG  . ARG D 1 543 ? 34.761  -5.403  120.472 1.00 23.30 ? 535  ARG D CG  1 
ATOM   18305 C  CD  . ARG D 1 543 ? 34.758  -5.119  121.986 1.00 24.25 ? 535  ARG D CD  1 
ATOM   18306 N  NE  . ARG D 1 543 ? 33.500  -4.513  122.407 1.00 26.01 ? 535  ARG D NE  1 
ATOM   18307 C  CZ  . ARG D 1 543 ? 33.124  -4.344  123.673 1.00 25.30 ? 535  ARG D CZ  1 
ATOM   18308 N  NH1 . ARG D 1 543 ? 33.911  -4.734  124.672 1.00 26.49 ? 535  ARG D NH1 1 
ATOM   18309 N  NH2 . ARG D 1 543 ? 31.950  -3.787  123.940 1.00 28.70 ? 535  ARG D NH2 1 
ATOM   18310 N  N   . GLY D 1 544 ? 35.208  -3.078  116.205 1.00 17.99 ? 536  GLY D N   1 
ATOM   18311 C  CA  . GLY D 1 544 ? 35.238  -1.924  115.316 1.00 18.36 ? 536  GLY D CA  1 
ATOM   18312 C  C   . GLY D 1 544 ? 36.416  -0.980  115.506 1.00 16.98 ? 536  GLY D C   1 
ATOM   18313 O  O   . GLY D 1 544 ? 36.925  -0.418  114.534 1.00 15.88 ? 536  GLY D O   1 
ATOM   18314 N  N   . ALA D 1 545 ? 36.860  -0.805  116.749 1.00 21.60 ? 537  ALA D N   1 
ATOM   18315 C  CA  . ALA D 1 545 ? 38.053  -0.033  117.059 1.00 20.98 ? 537  ALA D CA  1 
ATOM   18316 C  C   . ALA D 1 545 ? 38.636  -0.543  118.370 1.00 21.09 ? 537  ALA D C   1 
ATOM   18317 O  O   . ALA D 1 545 ? 37.905  -1.011  119.247 1.00 20.97 ? 537  ALA D O   1 
ATOM   18318 C  CB  . ALA D 1 545 ? 37.761  1.467   117.180 1.00 16.73 ? 537  ALA D CB  1 
ATOM   18319 N  N   . TYR D 1 546 ? 39.956  -0.434  118.493 1.00 18.03 ? 538  TYR D N   1 
ATOM   18320 C  CA  . TYR D 1 546 ? 40.683  -0.930  119.654 1.00 20.40 ? 538  TYR D CA  1 
ATOM   18321 C  C   . TYR D 1 546 ? 42.056  -0.270  119.666 1.00 21.94 ? 538  TYR D C   1 
ATOM   18322 O  O   . TYR D 1 546 ? 42.496  0.322   118.677 1.00 23.25 ? 538  TYR D O   1 
ATOM   18323 C  CB  . TYR D 1 546 ? 40.805  -2.460  119.625 1.00 19.49 ? 538  TYR D CB  1 
ATOM   18324 C  CG  . TYR D 1 546 ? 41.609  -2.937  118.449 1.00 21.60 ? 538  TYR D CG  1 
ATOM   18325 C  CD1 . TYR D 1 546 ? 41.029  -3.042  117.187 1.00 17.92 ? 538  TYR D CD1 1 
ATOM   18326 C  CD2 . TYR D 1 546 ? 42.956  -3.257  118.585 1.00 24.80 ? 538  TYR D CD2 1 
ATOM   18327 C  CE1 . TYR D 1 546 ? 41.764  -3.464  116.096 1.00 17.71 ? 538  TYR D CE1 1 
ATOM   18328 C  CE2 . TYR D 1 546 ? 43.701  -3.677  117.499 1.00 22.66 ? 538  TYR D CE2 1 
ATOM   18329 C  CZ  . TYR D 1 546 ? 43.093  -3.775  116.253 1.00 19.21 ? 538  TYR D CZ  1 
ATOM   18330 O  OH  . TYR D 1 546 ? 43.823  -4.180  115.161 1.00 22.02 ? 538  TYR D OH  1 
ATOM   18331 N  N   . VAL D 1 547 ? 42.732  -0.376  120.803 1.00 24.74 ? 539  VAL D N   1 
ATOM   18332 C  CA  . VAL D 1 547 ? 44.062  0.206   120.944 1.00 21.32 ? 539  VAL D CA  1 
ATOM   18333 C  C   . VAL D 1 547 ? 45.069  -0.792  120.385 1.00 23.66 ? 539  VAL D C   1 
ATOM   18334 O  O   . VAL D 1 547 ? 45.320  -1.838  120.992 1.00 22.63 ? 539  VAL D O   1 
ATOM   18335 C  CB  . VAL D 1 547 ? 44.373  0.556   122.403 1.00 28.83 ? 539  VAL D CB  1 
ATOM   18336 C  CG1 . VAL D 1 547 ? 45.701  1.309   122.488 1.00 29.98 ? 539  VAL D CG1 1 
ATOM   18337 C  CG2 . VAL D 1 547 ? 43.233  1.381   123.007 1.00 27.64 ? 539  VAL D CG2 1 
ATOM   18338 N  N   . ILE D 1 548 ? 45.646  -0.473  119.227 1.00 21.08 ? 540  ILE D N   1 
ATOM   18339 C  CA  . ILE D 1 548 ? 46.608  -1.378  118.603 1.00 21.54 ? 540  ILE D CA  1 
ATOM   18340 C  C   . ILE D 1 548 ? 48.024  -1.155  119.133 1.00 28.04 ? 540  ILE D C   1 
ATOM   18341 O  O   . ILE D 1 548 ? 48.840  -2.085  119.132 1.00 25.81 ? 540  ILE D O   1 
ATOM   18342 C  CB  . ILE D 1 548 ? 46.555  -1.248  117.067 1.00 20.70 ? 540  ILE D CB  1 
ATOM   18343 C  CG1 . ILE D 1 548 ? 47.415  -2.330  116.404 1.00 23.74 ? 540  ILE D CG1 1 
ATOM   18344 C  CG2 . ILE D 1 548 ? 46.996  0.148   116.612 1.00 24.31 ? 540  ILE D CG2 1 
ATOM   18345 C  CD1 . ILE D 1 548 ? 47.247  -2.407  114.904 1.00 25.28 ? 540  ILE D CD1 1 
ATOM   18346 N  N   . SER D 1 549 ? 48.335  0.051   119.614 1.00 30.04 ? 541  SER D N   1 
ATOM   18347 C  CA  . SER D 1 549 ? 49.659  0.328   120.173 1.00 27.35 ? 541  SER D CA  1 
ATOM   18348 C  C   . SER D 1 549 ? 49.491  1.360   121.282 1.00 28.31 ? 541  SER D C   1 
ATOM   18349 O  O   . SER D 1 549 ? 49.297  2.543   120.998 1.00 25.64 ? 541  SER D O   1 
ATOM   18350 C  CB  . SER D 1 549 ? 50.614  0.826   119.101 1.00 25.18 ? 541  SER D CB  1 
ATOM   18351 O  OG  . SER D 1 549 ? 51.867  1.149   119.672 1.00 26.79 ? 541  SER D OG  1 
ATOM   18352 N  N   . GLU D 1 550 ? 49.575  0.916   122.532 1.00 30.26 ? 542  GLU D N   1 
ATOM   18353 C  CA  . GLU D 1 550 ? 49.376  1.835   123.643 1.00 31.92 ? 542  GLU D CA  1 
ATOM   18354 C  C   . GLU D 1 550 ? 50.540  2.823   123.739 1.00 34.80 ? 542  GLU D C   1 
ATOM   18355 O  O   . GLU D 1 550 ? 51.652  2.564   123.271 1.00 32.75 ? 542  GLU D O   1 
ATOM   18356 C  CB  . GLU D 1 550 ? 49.209  1.062   124.960 1.00 34.73 ? 542  GLU D CB  1 
ATOM   18357 C  CG  . GLU D 1 550 ? 48.851  1.935   126.172 1.00 40.48 ? 542  GLU D CG  1 
ATOM   18358 C  CD  . GLU D 1 550 ? 47.562  2.734   125.973 1.00 42.40 ? 542  GLU D CD  1 
ATOM   18359 O  OE1 . GLU D 1 550 ? 46.487  2.103   125.948 1.00 45.02 ? 542  GLU D OE1 1 
ATOM   18360 O  OE2 . GLU D 1 550 ? 47.620  3.985   125.849 1.00 31.02 ? 542  GLU D OE2 1 
ATOM   18361 N  N   . ALA D 1 551 ? 50.258  3.985   124.319 1.00 28.30 ? 543  ALA D N   1 
ATOM   18362 C  CA  . ALA D 1 551 ? 51.306  4.952   124.597 1.00 32.47 ? 543  ALA D CA  1 
ATOM   18363 C  C   . ALA D 1 551 ? 52.260  4.404   125.648 1.00 38.32 ? 543  ALA D C   1 
ATOM   18364 O  O   . ALA D 1 551 ? 51.850  3.704   126.577 1.00 32.63 ? 543  ALA D O   1 
ATOM   18365 C  CB  . ALA D 1 551 ? 50.704  6.268   125.084 1.00 35.25 ? 543  ALA D CB  1 
ATOM   18366 N  N   . GLN D 1 552 ? 53.540  4.715   125.487 1.00 41.64 ? 544  GLN D N   1 
ATOM   18367 C  CA  . GLN D 1 552 ? 54.530  4.466   126.534 1.00 40.68 ? 544  GLN D CA  1 
ATOM   18368 C  C   . GLN D 1 552 ? 54.486  5.665   127.475 1.00 44.10 ? 544  GLN D C   1 
ATOM   18369 O  O   . GLN D 1 552 ? 55.142  6.686   127.254 1.00 44.57 ? 544  GLN D O   1 
ATOM   18370 C  CB  . GLN D 1 552 ? 55.915  4.256   125.934 1.00 38.23 ? 544  GLN D CB  1 
ATOM   18371 N  N   . GLY D 1 553 ? 53.696  5.539   128.534 1.00 46.58 ? 545  GLY D N   1 
ATOM   18372 C  CA  . GLY D 1 553 ? 53.428  6.626   129.457 1.00 44.61 ? 545  GLY D CA  1 
ATOM   18373 C  C   . GLY D 1 553 ? 52.007  7.135   129.293 1.00 43.91 ? 545  GLY D C   1 
ATOM   18374 O  O   . GLY D 1 553 ? 51.229  6.635   128.480 1.00 39.83 ? 545  GLY D O   1 
ATOM   18375 N  N   . ASN D 1 554 ? 51.672  8.147   130.097 1.00 36.37 ? 546  ASN D N   1 
ATOM   18376 C  CA  . ASN D 1 554 ? 50.341  8.742   130.023 1.00 37.87 ? 546  ASN D CA  1 
ATOM   18377 C  C   . ASN D 1 554 ? 50.149  9.408   128.666 1.00 34.66 ? 546  ASN D C   1 
ATOM   18378 O  O   . ASN D 1 554 ? 50.915  10.298  128.290 1.00 38.73 ? 546  ASN D O   1 
ATOM   18379 C  CB  . ASN D 1 554 ? 50.146  9.753   131.151 1.00 41.72 ? 546  ASN D CB  1 
ATOM   18380 N  N   . ALA D 1 555 ? 49.140  8.962   127.925 1.00 32.98 ? 547  ALA D N   1 
ATOM   18381 C  CA  . ALA D 1 555 ? 48.931  9.465   126.573 1.00 31.90 ? 547  ALA D CA  1 
ATOM   18382 C  C   . ALA D 1 555 ? 48.594  10.956  126.580 1.00 42.41 ? 547  ALA D C   1 
ATOM   18383 O  O   . ALA D 1 555 ? 47.779  11.423  127.382 1.00 36.34 ? 547  ALA D O   1 
ATOM   18384 C  CB  . ALA D 1 555 ? 47.815  8.670   125.890 1.00 30.07 ? 547  ALA D CB  1 
ATOM   18385 N  N   . GLN D 1 556 ? 49.242  11.710  125.679 1.00 33.19 ? 548  GLN D N   1 
ATOM   18386 C  CA  . GLN D 1 556 ? 48.884  13.104  125.430 1.00 34.16 ? 548  GLN D CA  1 
ATOM   18387 C  C   . GLN D 1 556 ? 47.873  13.261  124.297 1.00 32.81 ? 548  GLN D C   1 
ATOM   18388 O  O   . GLN D 1 556 ? 47.242  14.317  124.189 1.00 33.59 ? 548  GLN D O   1 
ATOM   18389 C  CB  . GLN D 1 556 ? 50.128  13.938  125.089 1.00 35.65 ? 548  GLN D CB  1 
ATOM   18390 C  CG  . GLN D 1 556 ? 51.157  14.085  126.218 1.00 37.48 ? 548  GLN D CG  1 
ATOM   18391 C  CD  . GLN D 1 556 ? 52.221  15.132  125.901 1.00 48.39 ? 548  GLN D CD  1 
ATOM   18392 O  OE1 . GLN D 1 556 ? 51.921  16.210  125.377 1.00 46.81 ? 548  GLN D OE1 1 
ATOM   18393 N  NE2 . GLN D 1 556 ? 53.471  14.814  126.212 1.00 49.61 ? 548  GLN D NE2 1 
ATOM   18394 N  N   . ALA D 1 557 ? 47.712  12.245  123.453 1.00 30.99 ? 549  ALA D N   1 
ATOM   18395 C  CA  . ALA D 1 557 ? 46.778  12.302  122.335 1.00 29.69 ? 549  ALA D CA  1 
ATOM   18396 C  C   . ALA D 1 557 ? 46.555  10.883  121.837 1.00 33.54 ? 549  ALA D C   1 
ATOM   18397 O  O   . ALA D 1 557 ? 47.297  9.959   122.186 1.00 27.73 ? 549  ALA D O   1 
ATOM   18398 C  CB  . ALA D 1 557 ? 47.299  13.210  121.216 1.00 30.24 ? 549  ALA D CB  1 
ATOM   18399 N  N   . VAL D 1 558 ? 45.520  10.713  121.016 1.00 32.02 ? 550  VAL D N   1 
ATOM   18400 C  CA  . VAL D 1 558 ? 45.247  9.430   120.385 1.00 29.57 ? 550  VAL D CA  1 
ATOM   18401 C  C   . VAL D 1 558 ? 45.164  9.635   118.881 1.00 28.78 ? 550  VAL D C   1 
ATOM   18402 O  O   . VAL D 1 558 ? 44.437  10.516  118.403 1.00 24.23 ? 550  VAL D O   1 
ATOM   18403 C  CB  . VAL D 1 558 ? 43.965  8.763   120.923 1.00 30.63 ? 550  VAL D CB  1 
ATOM   18404 C  CG1 . VAL D 1 558 ? 42.758  9.684   120.798 1.00 32.38 ? 550  VAL D CG1 1 
ATOM   18405 C  CG2 . VAL D 1 558 ? 43.713  7.450   120.187 1.00 24.38 ? 550  VAL D CG2 1 
ATOM   18406 N  N   . ILE D 1 559 ? 45.932  8.843   118.142 1.00 26.43 ? 551  ILE D N   1 
ATOM   18407 C  CA  . ILE D 1 559 ? 45.831  8.796   116.689 1.00 26.29 ? 551  ILE D CA  1 
ATOM   18408 C  C   . ILE D 1 559 ? 44.880  7.666   116.315 1.00 22.54 ? 551  ILE D C   1 
ATOM   18409 O  O   . ILE D 1 559 ? 45.122  6.500   116.648 1.00 21.88 ? 551  ILE D O   1 
ATOM   18410 C  CB  . ILE D 1 559 ? 47.208  8.596   116.042 1.00 23.55 ? 551  ILE D CB  1 
ATOM   18411 C  CG1 . ILE D 1 559 ? 48.192  9.647   116.557 1.00 25.37 ? 551  ILE D CG1 1 
ATOM   18412 C  CG2 . ILE D 1 559 ? 47.092  8.674   114.530 1.00 24.96 ? 551  ILE D CG2 1 
ATOM   18413 C  CD1 . ILE D 1 559 ? 49.596  9.465   116.044 1.00 28.62 ? 551  ILE D CD1 1 
ATOM   18414 N  N   . ILE D 1 560 ? 43.787  8.016   115.645 1.00 20.57 ? 552  ILE D N   1 
ATOM   18415 C  CA  . ILE D 1 560 ? 42.857  7.054   115.073 1.00 19.19 ? 552  ILE D CA  1 
ATOM   18416 C  C   . ILE D 1 560 ? 43.252  6.839   113.620 1.00 20.86 ? 552  ILE D C   1 
ATOM   18417 O  O   . ILE D 1 560 ? 43.319  7.799   112.845 1.00 23.81 ? 552  ILE D O   1 
ATOM   18418 C  CB  . ILE D 1 560 ? 41.407  7.565   115.160 1.00 18.87 ? 552  ILE D CB  1 
ATOM   18419 C  CG1 . ILE D 1 560 ? 41.069  8.043   116.578 1.00 23.84 ? 552  ILE D CG1 1 
ATOM   18420 C  CG2 . ILE D 1 560 ? 40.433  6.505   114.662 1.00 17.60 ? 552  ILE D CG2 1 
ATOM   18421 C  CD1 . ILE D 1 560 ? 39.692  8.731   116.647 1.00 22.14 ? 552  ILE D CD1 1 
ATOM   18422 N  N   . ALA D 1 561 ? 43.478  5.589   113.233 1.00 18.57 ? 553  ALA D N   1 
ATOM   18423 C  CA  . ALA D 1 561 ? 43.863  5.296   111.861 1.00 19.61 ? 553  ALA D CA  1 
ATOM   18424 C  C   . ALA D 1 561 ? 43.101  4.076   111.376 1.00 16.82 ? 553  ALA D C   1 
ATOM   18425 O  O   . ALA D 1 561 ? 42.656  3.238   112.170 1.00 17.22 ? 553  ALA D O   1 
ATOM   18426 C  CB  . ALA D 1 561 ? 45.381  5.067   111.738 1.00 20.71 ? 553  ALA D CB  1 
ATOM   18427 N  N   . THR D 1 562 ? 42.964  3.980   110.054 1.00 16.52 ? 554  THR D N   1 
ATOM   18428 C  CA  . THR D 1 562 ? 42.313  2.850   109.414 1.00 18.56 ? 554  THR D CA  1 
ATOM   18429 C  C   . THR D 1 562 ? 43.178  2.318   108.278 1.00 16.87 ? 554  THR D C   1 
ATOM   18430 O  O   . THR D 1 562 ? 44.014  3.036   107.719 1.00 17.08 ? 554  THR D O   1 
ATOM   18431 C  CB  . THR D 1 562 ? 40.949  3.245   108.830 1.00 15.60 ? 554  THR D CB  1 
ATOM   18432 O  OG1 . THR D 1 562 ? 41.165  4.071   107.682 1.00 16.58 ? 554  THR D OG1 1 
ATOM   18433 C  CG2 . THR D 1 562 ? 40.132  4.023   109.835 1.00 14.74 ? 554  THR D CG2 1 
ATOM   18434 N  N   . GLY D 1 563 ? 42.934  1.050   107.931 1.00 15.04 ? 555  GLY D N   1 
ATOM   18435 C  CA  . GLY D 1 563 ? 43.449  0.474   106.693 1.00 14.35 ? 555  GLY D CA  1 
ATOM   18436 C  C   . GLY D 1 563 ? 44.934  0.708   106.486 1.00 16.82 ? 555  GLY D C   1 
ATOM   18437 O  O   . GLY D 1 563 ? 45.749  0.491   107.387 1.00 17.06 ? 555  GLY D O   1 
ATOM   18438 N  N   . SER D 1 564 ? 45.292  1.187   105.288 1.00 16.29 ? 556  SER D N   1 
ATOM   18439 C  CA  . SER D 1 564 ? 46.694  1.359   104.919 1.00 20.43 ? 556  SER D CA  1 
ATOM   18440 C  C   . SER D 1 564 ? 47.413  2.438   105.724 1.00 22.03 ? 556  SER D C   1 
ATOM   18441 O  O   . SER D 1 564 ? 48.642  2.526   105.627 1.00 23.73 ? 556  SER D O   1 
ATOM   18442 C  CB  . SER D 1 564 ? 46.814  1.663   103.419 1.00 19.79 ? 556  SER D CB  1 
ATOM   18443 O  OG  . SER D 1 564 ? 45.919  2.684   103.016 1.00 19.58 ? 556  SER D OG  1 
ATOM   18444 N  N   . GLU D 1 565 ? 46.703  3.233   106.530 1.00 15.80 ? 557  GLU D N   1 
ATOM   18445 C  CA  . GLU D 1 565 ? 47.320  4.321   107.285 1.00 16.37 ? 557  GLU D CA  1 
ATOM   18446 C  C   . GLU D 1 565 ? 47.670  3.955   108.727 1.00 17.33 ? 557  GLU D C   1 
ATOM   18447 O  O   . GLU D 1 565 ? 48.267  4.781   109.426 1.00 20.00 ? 557  GLU D O   1 
ATOM   18448 C  CB  . GLU D 1 565 ? 46.411  5.563   107.287 1.00 19.55 ? 557  GLU D CB  1 
ATOM   18449 C  CG  . GLU D 1 565 ? 46.457  6.368   105.988 1.00 19.58 ? 557  GLU D CG  1 
ATOM   18450 C  CD  . GLU D 1 565 ? 45.965  5.565   104.799 1.00 18.39 ? 557  GLU D CD  1 
ATOM   18451 O  OE1 . GLU D 1 565 ? 44.742  5.389   104.669 1.00 16.10 ? 557  GLU D OE1 1 
ATOM   18452 O  OE2 . GLU D 1 565 ? 46.802  5.087   104.008 1.00 18.15 ? 557  GLU D OE2 1 
ATOM   18453 N  N   . VAL D 1 566 ? 47.319  2.753   109.196 1.00 19.39 ? 558  VAL D N   1 
ATOM   18454 C  CA  . VAL D 1 566 ? 47.674  2.374   110.564 1.00 17.39 ? 558  VAL D CA  1 
ATOM   18455 C  C   . VAL D 1 566 ? 49.188  2.303   110.709 1.00 23.67 ? 558  VAL D C   1 
ATOM   18456 O  O   . VAL D 1 566 ? 49.754  2.776   111.701 1.00 21.86 ? 558  VAL D O   1 
ATOM   18457 C  CB  . VAL D 1 566 ? 46.999  1.048   110.961 1.00 18.20 ? 558  VAL D CB  1 
ATOM   18458 C  CG1 . VAL D 1 566 ? 47.512  0.580   112.335 1.00 17.88 ? 558  VAL D CG1 1 
ATOM   18459 C  CG2 . VAL D 1 566 ? 45.490  1.215   111.000 1.00 17.43 ? 558  VAL D CG2 1 
ATOM   18460 N  N   . GLY D 1 567 ? 49.874  1.755   109.704 1.00 20.32 ? 559  GLY D N   1 
ATOM   18461 C  CA  . GLY D 1 567 ? 51.327  1.679   109.782 1.00 24.92 ? 559  GLY D CA  1 
ATOM   18462 C  C   . GLY D 1 567 ? 51.983  3.044   109.862 1.00 21.86 ? 559  GLY D C   1 
ATOM   18463 O  O   . GLY D 1 567 ? 52.954  3.236   110.596 1.00 22.57 ? 559  GLY D O   1 
ATOM   18464 N  N   . LEU D 1 568 ? 51.454  4.016   109.117 1.00 24.03 ? 560  LEU D N   1 
ATOM   18465 C  CA  . LEU D 1 568 ? 51.961  5.381   109.203 1.00 20.75 ? 560  LEU D CA  1 
ATOM   18466 C  C   . LEU D 1 568 ? 51.737  5.972   110.590 1.00 25.24 ? 560  LEU D C   1 
ATOM   18467 O  O   . LEU D 1 568 ? 52.606  6.673   111.126 1.00 20.96 ? 560  LEU D O   1 
ATOM   18468 C  CB  . LEU D 1 568 ? 51.281  6.249   108.145 1.00 19.15 ? 560  LEU D CB  1 
ATOM   18469 C  CG  . LEU D 1 568 ? 51.412  7.763   108.300 1.00 25.61 ? 560  LEU D CG  1 
ATOM   18470 C  CD1 . LEU D 1 568 ? 52.844  8.183   108.072 1.00 22.31 ? 560  LEU D CD1 1 
ATOM   18471 C  CD2 . LEU D 1 568 ? 50.477  8.483   107.321 1.00 28.11 ? 560  LEU D CD2 1 
ATOM   18472 N  N   . ALA D 1 569 ? 50.563  5.723   111.174 1.00 23.20 ? 561  ALA D N   1 
ATOM   18473 C  CA  . ALA D 1 569 ? 50.266  6.245   112.504 1.00 20.28 ? 561  ALA D CA  1 
ATOM   18474 C  C   . ALA D 1 569 ? 51.201  5.659   113.555 1.00 20.79 ? 561  ALA D C   1 
ATOM   18475 O  O   . ALA D 1 569 ? 51.631  6.359   114.483 1.00 21.53 ? 561  ALA D O   1 
ATOM   18476 C  CB  . ALA D 1 569 ? 48.808  5.950   112.860 1.00 24.04 ? 561  ALA D CB  1 
ATOM   18477 N  N   . VAL D 1 570 ? 51.521  4.373   113.437 1.00 20.80 ? 562  VAL D N   1 
ATOM   18478 C  CA  . VAL D 1 570 ? 52.414  3.760   114.416 1.00 21.71 ? 562  VAL D CA  1 
ATOM   18479 C  C   . VAL D 1 570 ? 53.828  4.310   114.260 1.00 22.67 ? 562  VAL D C   1 
ATOM   18480 O  O   . VAL D 1 570 ? 54.527  4.554   115.252 1.00 26.28 ? 562  VAL D O   1 
ATOM   18481 C  CB  . VAL D 1 570 ? 52.365  2.226   114.294 1.00 25.74 ? 562  VAL D CB  1 
ATOM   18482 C  CG1 . VAL D 1 570 ? 53.415  1.589   115.183 1.00 35.40 ? 562  VAL D CG1 1 
ATOM   18483 C  CG2 . VAL D 1 570 ? 50.983  1.721   114.675 1.00 30.08 ? 562  VAL D CG2 1 
ATOM   18484 N  N   . GLU D 1 571 ? 54.265  4.547   113.020 1.00 27.42 ? 563  GLU D N   1 
ATOM   18485 C  CA  . GLU D 1 571 ? 55.590  5.132   112.819 1.00 30.70 ? 563  GLU D CA  1 
ATOM   18486 C  C   . GLU D 1 571 ? 55.663  6.538   113.402 1.00 29.96 ? 563  GLU D C   1 
ATOM   18487 O  O   . GLU D 1 571 ? 56.693  6.931   113.964 1.00 32.48 ? 563  GLU D O   1 
ATOM   18488 C  CB  . GLU D 1 571 ? 55.950  5.146   111.331 1.00 26.42 ? 563  GLU D CB  1 
ATOM   18489 N  N   . ALA D 1 572 ? 54.579  7.314   113.276 1.00 23.21 ? 564  ALA D N   1 
ATOM   18490 C  CA  . ALA D 1 572 ? 54.546  8.639   113.890 1.00 23.65 ? 564  ALA D CA  1 
ATOM   18491 C  C   . ALA D 1 572 ? 54.537  8.536   115.408 1.00 24.26 ? 564  ALA D C   1 
ATOM   18492 O  O   . ALA D 1 572 ? 55.143  9.366   116.096 1.00 26.55 ? 564  ALA D O   1 
ATOM   18493 C  CB  . ALA D 1 572 ? 53.330  9.422   113.404 1.00 22.75 ? 564  ALA D CB  1 
ATOM   18494 N  N   . GLN D 1 573 ? 53.846  7.532   115.946 1.00 25.77 ? 565  GLN D N   1 
ATOM   18495 C  CA  . GLN D 1 573 ? 53.886  7.303   117.386 1.00 26.93 ? 565  GLN D CA  1 
ATOM   18496 C  C   . GLN D 1 573 ? 55.319  7.146   117.870 1.00 25.70 ? 565  GLN D C   1 
ATOM   18497 O  O   . GLN D 1 573 ? 55.694  7.695   118.912 1.00 26.60 ? 565  GLN D O   1 
ATOM   18498 C  CB  . GLN D 1 573 ? 53.067  6.067   117.750 1.00 27.24 ? 565  GLN D CB  1 
ATOM   18499 C  CG  . GLN D 1 573 ? 53.140  5.715   119.229 1.00 28.30 ? 565  GLN D CG  1 
ATOM   18500 C  CD  . GLN D 1 573 ? 52.485  4.385   119.546 1.00 31.16 ? 565  GLN D CD  1 
ATOM   18501 O  OE1 . GLN D 1 573 ? 52.688  3.401   118.840 1.00 29.40 ? 565  GLN D OE1 1 
ATOM   18502 N  NE2 . GLN D 1 573 ? 51.687  4.353   120.606 1.00 31.41 ? 565  GLN D NE2 1 
ATOM   18503 N  N   . LYS D 1 574 ? 56.139  6.414   117.113 1.00 26.73 ? 566  LYS D N   1 
ATOM   18504 C  CA  . LYS D 1 574 ? 57.532  6.215   117.508 1.00 30.07 ? 566  LYS D CA  1 
ATOM   18505 C  C   . LYS D 1 574 ? 58.327  7.513   117.432 1.00 33.86 ? 566  LYS D C   1 
ATOM   18506 O  O   . LYS D 1 574 ? 59.189  7.767   118.282 1.00 29.06 ? 566  LYS D O   1 
ATOM   18507 C  CB  . LYS D 1 574 ? 58.180  5.143   116.633 1.00 32.64 ? 566  LYS D CB  1 
ATOM   18508 C  CG  . LYS D 1 574 ? 57.610  3.755   116.832 1.00 31.31 ? 566  LYS D CG  1 
ATOM   18509 C  CD  . LYS D 1 574 ? 58.358  2.734   116.000 1.00 39.19 ? 566  LYS D CD  1 
ATOM   18510 C  CE  . LYS D 1 574 ? 57.987  1.323   116.416 1.00 45.45 ? 566  LYS D CE  1 
ATOM   18511 N  NZ  . LYS D 1 574 ? 56.516  1.114   116.358 1.00 50.40 ? 566  LYS D NZ  1 
ATOM   18512 N  N   . VAL D 1 575 ? 58.067  8.338   116.414 1.00 31.41 ? 567  VAL D N   1 
ATOM   18513 C  CA  . VAL D 1 575 ? 58.780  9.607   116.298 1.00 32.31 ? 567  VAL D CA  1 
ATOM   18514 C  C   . VAL D 1 575 ? 58.375  10.546  117.425 1.00 30.67 ? 567  VAL D C   1 
ATOM   18515 O  O   . VAL D 1 575 ? 59.224  11.198  118.045 1.00 33.73 ? 567  VAL D O   1 
ATOM   18516 C  CB  . VAL D 1 575 ? 58.530  10.237  114.916 1.00 32.90 ? 567  VAL D CB  1 
ATOM   18517 C  CG1 . VAL D 1 575 ? 59.250  11.568  114.799 1.00 35.75 ? 567  VAL D CG1 1 
ATOM   18518 C  CG2 . VAL D 1 575 ? 58.984  9.291   113.820 1.00 31.19 ? 567  VAL D CG2 1 
ATOM   18519 N  N   . LEU D 1 576 ? 57.073  10.621  117.712 1.00 28.27 ? 568  LEU D N   1 
ATOM   18520 C  CA  . LEU D 1 576 ? 56.584  11.436  118.822 1.00 28.09 ? 568  LEU D CA  1 
ATOM   18521 C  C   . LEU D 1 576 ? 57.155  10.967  120.153 1.00 29.12 ? 568  LEU D C   1 
ATOM   18522 O  O   . LEU D 1 576 ? 57.493  11.788  121.018 1.00 30.10 ? 568  LEU D O   1 
ATOM   18523 C  CB  . LEU D 1 576 ? 55.054  11.397  118.851 1.00 30.17 ? 568  LEU D CB  1 
ATOM   18524 C  CG  . LEU D 1 576 ? 54.380  12.157  117.710 1.00 27.60 ? 568  LEU D CG  1 
ATOM   18525 C  CD1 . LEU D 1 576 ? 52.981  11.591  117.390 1.00 25.31 ? 568  LEU D CD1 1 
ATOM   18526 C  CD2 . LEU D 1 576 ? 54.316  13.634  118.048 1.00 26.70 ? 568  LEU D CD2 1 
ATOM   18527 N  N   . ALA D 1 577 ? 57.253  9.653   120.347 1.00 28.96 ? 569  ALA D N   1 
ATOM   18528 C  CA  . ALA D 1 577 ? 57.841  9.147   121.583 1.00 30.00 ? 569  ALA D CA  1 
ATOM   18529 C  C   . ALA D 1 577 ? 59.264  9.660   121.749 1.00 32.41 ? 569  ALA D C   1 
ATOM   18530 O  O   . ALA D 1 577 ? 59.663  10.060  122.847 1.00 32.45 ? 569  ALA D O   1 
ATOM   18531 C  CB  . ALA D 1 577 ? 57.810  7.618   121.599 1.00 29.66 ? 569  ALA D CB  1 
ATOM   18532 N  N   . GLY D 1 578 ? 60.032  9.692   120.657 1.00 31.41 ? 570  GLY D N   1 
ATOM   18533 C  CA  . GLY D 1 578 ? 61.381  10.230  120.679 1.00 32.74 ? 570  GLY D CA  1 
ATOM   18534 C  C   . GLY D 1 578 ? 61.463  11.723  120.917 1.00 39.00 ? 570  GLY D C   1 
ATOM   18535 O  O   . GLY D 1 578 ? 62.554  12.226  121.206 1.00 41.68 ? 570  GLY D O   1 
ATOM   18536 N  N   . GLN D 1 579 ? 60.349  12.442  120.797 1.00 37.21 ? 571  GLN D N   1 
ATOM   18537 C  CA  . GLN D 1 579 ? 60.308  13.865  121.105 1.00 38.45 ? 571  GLN D CA  1 
ATOM   18538 C  C   . GLN D 1 579 ? 59.619  14.150  122.434 1.00 39.47 ? 571  GLN D C   1 
ATOM   18539 O  O   . GLN D 1 579 ? 59.291  15.307  122.720 1.00 37.00 ? 571  GLN D O   1 
ATOM   18540 C  CB  . GLN D 1 579 ? 59.630  14.629  119.964 1.00 35.29 ? 571  GLN D CB  1 
ATOM   18541 C  CG  . GLN D 1 579 ? 60.462  14.644  118.686 1.00 35.31 ? 571  GLN D CG  1 
ATOM   18542 C  CD  . GLN D 1 579 ? 59.745  15.275  117.516 1.00 39.78 ? 571  GLN D CD  1 
ATOM   18543 O  OE1 . GLN D 1 579 ? 58.755  15.984  117.689 1.00 39.13 ? 571  GLN D OE1 1 
ATOM   18544 N  NE2 . GLN D 1 579 ? 60.238  15.014  116.311 1.00 42.34 ? 571  GLN D NE2 1 
ATOM   18545 N  N   . GLY D 1 580 ? 59.403  13.125  123.256 1.00 33.39 ? 572  GLY D N   1 
ATOM   18546 C  CA  . GLY D 1 580 ? 58.792  13.320  124.555 1.00 34.60 ? 572  GLY D CA  1 
ATOM   18547 C  C   . GLY D 1 580 ? 57.291  13.475  124.530 1.00 33.89 ? 572  GLY D C   1 
ATOM   18548 O  O   . GLY D 1 580 ? 56.724  14.075  125.449 1.00 33.14 ? 572  GLY D O   1 
ATOM   18549 N  N   . ILE D 1 581 ? 56.624  12.935  123.510 1.00 33.14 ? 573  ILE D N   1 
ATOM   18550 C  CA  . ILE D 1 581 ? 55.178  13.060  123.343 1.00 30.25 ? 573  ILE D CA  1 
ATOM   18551 C  C   . ILE D 1 581 ? 54.605  11.649  123.228 1.00 29.34 ? 573  ILE D C   1 
ATOM   18552 O  O   . ILE D 1 581 ? 54.686  11.020  122.168 1.00 28.54 ? 573  ILE D O   1 
ATOM   18553 C  CB  . ILE D 1 581 ? 54.808  13.913  122.126 1.00 29.51 ? 573  ILE D CB  1 
ATOM   18554 C  CG1 . ILE D 1 581 ? 55.492  15.276  122.205 1.00 34.43 ? 573  ILE D CG1 1 
ATOM   18555 C  CG2 . ILE D 1 581 ? 53.302  14.091  122.033 1.00 34.29 ? 573  ILE D CG2 1 
ATOM   18556 C  CD1 . ILE D 1 581 ? 55.272  16.124  120.975 1.00 35.33 ? 573  ILE D CD1 1 
ATOM   18557 N  N   . ALA D 1 582 ? 54.029  11.148  124.317 1.00 29.54 ? 574  ALA D N   1 
ATOM   18558 C  CA  . ALA D 1 582 ? 53.437  9.818   124.333 1.00 28.80 ? 574  ALA D CA  1 
ATOM   18559 C  C   . ALA D 1 582 ? 52.035  9.877   123.737 1.00 27.57 ? 574  ALA D C   1 
ATOM   18560 O  O   . ALA D 1 582 ? 51.167  10.593  124.250 1.00 31.06 ? 574  ALA D O   1 
ATOM   18561 C  CB  . ALA D 1 582 ? 53.386  9.276   125.758 1.00 29.62 ? 574  ALA D CB  1 
ATOM   18562 N  N   . VAL D 1 583 ? 51.806  9.134   122.655 1.00 28.09 ? 575  VAL D N   1 
ATOM   18563 C  CA  . VAL D 1 583 ? 50.466  9.026   122.090 1.00 26.67 ? 575  VAL D CA  1 
ATOM   18564 C  C   . VAL D 1 583 ? 50.091  7.559   121.954 1.00 30.20 ? 575  VAL D C   1 
ATOM   18565 O  O   . VAL D 1 583 ? 50.945  6.673   121.857 1.00 29.13 ? 575  VAL D O   1 
ATOM   18566 C  CB  . VAL D 1 583 ? 50.311  9.740   120.725 1.00 24.69 ? 575  VAL D CB  1 
ATOM   18567 C  CG1 . VAL D 1 583 ? 50.830  11.164  120.812 1.00 29.24 ? 575  VAL D CG1 1 
ATOM   18568 C  CG2 . VAL D 1 583 ? 50.987  8.947   119.610 1.00 25.96 ? 575  VAL D CG2 1 
ATOM   18569 N  N   . ARG D 1 584 ? 48.786  7.317   121.967 1.00 26.55 ? 576  ARG D N   1 
ATOM   18570 C  CA  . ARG D 1 584 ? 48.210  6.003   121.741 1.00 24.80 ? 576  ARG D CA  1 
ATOM   18571 C  C   . ARG D 1 584 ? 47.698  5.934   120.305 1.00 24.74 ? 576  ARG D C   1 
ATOM   18572 O  O   . ARG D 1 584 ? 47.231  6.936   119.760 1.00 27.20 ? 576  ARG D O   1 
ATOM   18573 C  CB  . ARG D 1 584 ? 47.080  5.752   122.748 1.00 27.96 ? 576  ARG D CB  1 
ATOM   18574 C  CG  . ARG D 1 584 ? 45.885  4.981   122.230 1.00 33.93 ? 576  ARG D CG  1 
ATOM   18575 C  CD  . ARG D 1 584 ? 44.657  5.193   123.108 1.00 31.23 ? 576  ARG D CD  1 
ATOM   18576 N  NE  . ARG D 1 584 ? 44.837  4.665   124.457 1.00 29.56 ? 576  ARG D NE  1 
ATOM   18577 C  CZ  . ARG D 1 584 ? 43.840  4.334   125.272 1.00 27.66 ? 576  ARG D CZ  1 
ATOM   18578 N  NH1 . ARG D 1 584 ? 42.580  4.459   124.875 1.00 25.66 ? 576  ARG D NH1 1 
ATOM   18579 N  NH2 . ARG D 1 584 ? 44.104  3.850   126.477 1.00 27.33 ? 576  ARG D NH2 1 
ATOM   18580 N  N   . VAL D 1 585 ? 47.811  4.763   119.680 1.00 21.75 ? 577  VAL D N   1 
ATOM   18581 C  CA  . VAL D 1 585 ? 47.269  4.544   118.343 1.00 20.72 ? 577  VAL D CA  1 
ATOM   18582 C  C   . VAL D 1 585 ? 46.079  3.602   118.445 1.00 21.79 ? 577  VAL D C   1 
ATOM   18583 O  O   . VAL D 1 585 ? 46.187  2.500   119.003 1.00 21.67 ? 577  VAL D O   1 
ATOM   18584 C  CB  . VAL D 1 585 ? 48.321  3.990   117.372 1.00 23.64 ? 577  VAL D CB  1 
ATOM   18585 C  CG1 . VAL D 1 585 ? 47.674  3.779   115.997 1.00 21.76 ? 577  VAL D CG1 1 
ATOM   18586 C  CG2 . VAL D 1 585 ? 49.506  4.948   117.270 1.00 24.18 ? 577  VAL D CG2 1 
ATOM   18587 N  N   . VAL D 1 586 ? 44.945  4.049   117.921 1.00 19.42 ? 578  VAL D N   1 
ATOM   18588 C  CA  . VAL D 1 586 ? 43.737  3.246   117.810 1.00 18.81 ? 578  VAL D CA  1 
ATOM   18589 C  C   . VAL D 1 586 ? 43.574  2.839   116.351 1.00 19.24 ? 578  VAL D C   1 
ATOM   18590 O  O   . VAL D 1 586 ? 43.614  3.689   115.451 1.00 21.72 ? 578  VAL D O   1 
ATOM   18591 C  CB  . VAL D 1 586 ? 42.511  4.034   118.313 1.00 18.75 ? 578  VAL D CB  1 
ATOM   18592 C  CG1 . VAL D 1 586 ? 41.219  3.435   117.784 1.00 19.23 ? 578  VAL D CG1 1 
ATOM   18593 C  CG2 . VAL D 1 586 ? 42.510  4.079   119.842 1.00 19.65 ? 578  VAL D CG2 1 
ATOM   18594 N  N   . SER D 1 587 ? 43.420  1.545   116.110 1.00 20.15 ? 579  SER D N   1 
ATOM   18595 C  CA  . SER D 1 587 ? 42.976  1.088   114.803 1.00 17.04 ? 579  SER D CA  1 
ATOM   18596 C  C   . SER D 1 587 ? 41.454  1.041   114.816 1.00 18.95 ? 579  SER D C   1 
ATOM   18597 O  O   . SER D 1 587 ? 40.854  0.498   115.751 1.00 17.10 ? 579  SER D O   1 
ATOM   18598 C  CB  . SER D 1 587 ? 43.555  -0.283  114.465 1.00 16.93 ? 579  SER D CB  1 
ATOM   18599 O  OG  . SER D 1 587 ? 43.109  -0.691  113.169 1.00 18.14 ? 579  SER D OG  1 
ATOM   18600 N  N   . MET D 1 588 ? 40.829  1.623   113.794 1.00 16.27 ? 580  MET D N   1 
ATOM   18601 C  CA  . MET D 1 588 ? 39.371  1.662   113.686 1.00 19.09 ? 580  MET D CA  1 
ATOM   18602 C  C   . MET D 1 588 ? 38.929  1.007   112.376 1.00 17.53 ? 580  MET D C   1 
ATOM   18603 O  O   . MET D 1 588 ? 38.461  1.691   111.452 1.00 14.12 ? 580  MET D O   1 
ATOM   18604 C  CB  . MET D 1 588 ? 38.850  3.095   113.786 1.00 19.31 ? 580  MET D CB  1 
ATOM   18605 C  CG  . MET D 1 588 ? 37.332  3.171   113.935 1.00 19.14 ? 580  MET D CG  1 
ATOM   18606 S  SD  . MET D 1 588 ? 36.707  4.800   114.364 1.00 17.85 ? 580  MET D SD  1 
ATOM   18607 C  CE  . MET D 1 588 ? 37.091  4.913   116.121 1.00 18.45 ? 580  MET D CE  1 
ATOM   18608 N  N   . PRO D 1 589 ? 39.058  -0.320  112.262 1.00 18.39 ? 581  PRO D N   1 
ATOM   18609 C  CA  . PRO D 1 589 ? 38.676  -0.976  111.001 1.00 18.72 ? 581  PRO D CA  1 
ATOM   18610 C  C   . PRO D 1 589 ? 37.214  -0.775  110.614 1.00 20.69 ? 581  PRO D C   1 
ATOM   18611 O  O   . PRO D 1 589 ? 36.897  -0.874  109.422 1.00 14.60 ? 581  PRO D O   1 
ATOM   18612 C  CB  . PRO D 1 589 ? 39.003  -2.456  111.249 1.00 18.06 ? 581  PRO D CB  1 
ATOM   18613 C  CG  . PRO D 1 589 ? 39.121  -2.600  112.770 1.00 19.61 ? 581  PRO D CG  1 
ATOM   18614 C  CD  . PRO D 1 589 ? 39.656  -1.274  113.222 1.00 21.84 ? 581  PRO D CD  1 
ATOM   18615 N  N   . SER D 1 590 ? 36.318  -0.476  111.560 1.00 15.53 ? 582  SER D N   1 
ATOM   18616 C  CA  . SER D 1 590 ? 34.931  -0.175  111.199 1.00 14.18 ? 582  SER D CA  1 
ATOM   18617 C  C   . SER D 1 590 ? 34.382  0.871   112.159 1.00 17.48 ? 582  SER D C   1 
ATOM   18618 O  O   . SER D 1 590 ? 34.164  0.576   113.341 1.00 19.17 ? 582  SER D O   1 
ATOM   18619 C  CB  . SER D 1 590 ? 34.051  -1.423  111.213 1.00 13.86 ? 582  SER D CB  1 
ATOM   18620 O  OG  . SER D 1 590 ? 32.706  -1.081  110.874 1.00 16.39 ? 582  SER D OG  1 
ATOM   18621 N  N   . THR D 1 591 ? 34.156  2.082   111.641 1.00 17.42 ? 583  THR D N   1 
ATOM   18622 C  CA  . THR D 1 591 ? 33.453  3.108   112.409 1.00 16.93 ? 583  THR D CA  1 
ATOM   18623 C  C   . THR D 1 591 ? 32.042  2.655   112.750 1.00 18.47 ? 583  THR D C   1 
ATOM   18624 O  O   . THR D 1 591 ? 31.544  2.910   113.852 1.00 18.06 ? 583  THR D O   1 
ATOM   18625 C  CB  . THR D 1 591 ? 33.406  4.421   111.622 1.00 17.52 ? 583  THR D CB  1 
ATOM   18626 O  OG1 . THR D 1 591 ? 32.649  4.235   110.418 1.00 17.80 ? 583  THR D OG1 1 
ATOM   18627 C  CG2 . THR D 1 591 ? 34.815  4.896   111.246 1.00 13.62 ? 583  THR D CG2 1 
ATOM   18628 N  N   . SER D 1 592 ? 31.387  1.983   111.801 1.00 16.97 ? 584  SER D N   1 
ATOM   18629 C  CA  . SER D 1 592 ? 30.019  1.513   111.977 1.00 23.00 ? 584  SER D CA  1 
ATOM   18630 C  C   . SER D 1 592 ? 29.905  0.652   113.226 1.00 19.78 ? 584  SER D C   1 
ATOM   18631 O  O   . SER D 1 592 ? 29.077  0.903   114.108 1.00 20.95 ? 584  SER D O   1 
ATOM   18632 C  CB  . SER D 1 592 ? 29.599  0.720   110.729 1.00 18.28 ? 584  SER D CB  1 
ATOM   18633 O  OG  . SER D 1 592 ? 30.225  1.246   109.537 1.00 18.27 ? 584  SER D OG  1 
ATOM   18634 N  N   . VAL D 1 593 ? 30.771  -0.352  113.323 1.00 16.24 ? 585  VAL D N   1 
ATOM   18635 C  CA  . VAL D 1 593 ? 30.719  -1.305  114.424 1.00 16.22 ? 585  VAL D CA  1 
ATOM   18636 C  C   . VAL D 1 593 ? 31.121  -0.636  115.730 1.00 18.91 ? 585  VAL D C   1 
ATOM   18637 O  O   . VAL D 1 593 ? 30.486  -0.844  116.771 1.00 15.86 ? 585  VAL D O   1 
ATOM   18638 C  CB  . VAL D 1 593 ? 31.614  -2.509  114.089 1.00 14.43 ? 585  VAL D CB  1 
ATOM   18639 C  CG1 . VAL D 1 593 ? 31.727  -3.457  115.297 1.00 15.09 ? 585  VAL D CG1 1 
ATOM   18640 C  CG2 . VAL D 1 593 ? 31.058  -3.237  112.870 1.00 14.10 ? 585  VAL D CG2 1 
ATOM   18641 N  N   . PHE D 1 594 ? 32.175  0.184   115.698 1.00 16.83 ? 586  PHE D N   1 
ATOM   18642 C  CA  . PHE D 1 594 ? 32.587  0.887   116.907 1.00 16.63 ? 586  PHE D CA  1 
ATOM   18643 C  C   . PHE D 1 594 ? 31.451  1.733   117.468 1.00 18.53 ? 586  PHE D C   1 
ATOM   18644 O  O   . PHE D 1 594 ? 31.270  1.815   118.689 1.00 20.41 ? 586  PHE D O   1 
ATOM   18645 C  CB  . PHE D 1 594 ? 33.808  1.762   116.633 1.00 17.06 ? 586  PHE D CB  1 
ATOM   18646 C  CG  . PHE D 1 594 ? 34.285  2.507   117.852 1.00 23.55 ? 586  PHE D CG  1 
ATOM   18647 C  CD1 . PHE D 1 594 ? 34.851  1.820   118.907 1.00 19.51 ? 586  PHE D CD1 1 
ATOM   18648 C  CD2 . PHE D 1 594 ? 34.146  3.881   117.950 1.00 28.96 ? 586  PHE D CD2 1 
ATOM   18649 C  CE1 . PHE D 1 594 ? 35.292  2.485   120.033 1.00 18.15 ? 586  PHE D CE1 1 
ATOM   18650 C  CE2 . PHE D 1 594 ? 34.580  4.553   119.073 1.00 28.96 ? 586  PHE D CE2 1 
ATOM   18651 C  CZ  . PHE D 1 594 ? 35.158  3.849   120.120 1.00 18.35 ? 586  PHE D CZ  1 
ATOM   18652 N  N   . ASP D 1 595 ? 30.664  2.349   116.590 1.00 18.33 ? 587  ASP D N   1 
ATOM   18653 C  CA  . ASP D 1 595 ? 29.614  3.260   117.044 1.00 19.86 ? 587  ASP D CA  1 
ATOM   18654 C  C   . ASP D 1 595 ? 28.540  2.555   117.869 1.00 24.01 ? 587  ASP D C   1 
ATOM   18655 O  O   . ASP D 1 595 ? 27.918  3.185   118.731 1.00 28.63 ? 587  ASP D O   1 
ATOM   18656 C  CB  . ASP D 1 595 ? 28.996  3.972   115.837 1.00 22.45 ? 587  ASP D CB  1 
ATOM   18657 C  CG  . ASP D 1 595 ? 29.882  5.079   115.298 1.00 25.97 ? 587  ASP D CG  1 
ATOM   18658 O  OD1 . ASP D 1 595 ? 30.842  5.463   115.997 1.00 29.36 ? 587  ASP D OD1 1 
ATOM   18659 O  OD2 . ASP D 1 595 ? 29.618  5.573   114.181 1.00 26.84 ? 587  ASP D OD2 1 
ATOM   18660 N  N   . ARG D 1 596 ? 28.311  1.258   117.657 1.00 20.89 ? 588  ARG D N   1 
ATOM   18661 C  CA  . ARG D 1 596 ? 27.285  0.570   118.439 1.00 22.70 ? 588  ARG D CA  1 
ATOM   18662 C  C   . ARG D 1 596 ? 27.843  -0.215  119.626 1.00 24.22 ? 588  ARG D C   1 
ATOM   18663 O  O   . ARG D 1 596 ? 27.102  -0.997  120.237 1.00 25.97 ? 588  ARG D O   1 
ATOM   18664 C  CB  . ARG D 1 596 ? 26.436  -0.342  117.543 1.00 31.21 ? 588  ARG D CB  1 
ATOM   18665 C  CG  . ARG D 1 596 ? 27.163  -1.449  116.790 1.00 33.00 ? 588  ARG D CG  1 
ATOM   18666 C  CD  . ARG D 1 596 ? 26.160  -2.256  115.938 1.00 31.69 ? 588  ARG D CD  1 
ATOM   18667 N  NE  . ARG D 1 596 ? 26.801  -3.329  115.179 1.00 28.95 ? 588  ARG D NE  1 
ATOM   18668 C  CZ  . ARG D 1 596 ? 27.116  -3.243  113.888 1.00 22.99 ? 588  ARG D CZ  1 
ATOM   18669 N  NH1 . ARG D 1 596 ? 26.847  -2.138  113.211 1.00 21.40 ? 588  ARG D NH1 1 
ATOM   18670 N  NH2 . ARG D 1 596 ? 27.702  -4.259  113.275 1.00 29.08 ? 588  ARG D NH2 1 
ATOM   18671 N  N   . GLN D 1 597 ? 29.110  -0.013  119.990 1.00 18.44 ? 589  GLN D N   1 
ATOM   18672 C  CA  . GLN D 1 597 ? 29.633  -0.654  121.186 1.00 21.75 ? 589  GLN D CA  1 
ATOM   18673 C  C   . GLN D 1 597 ? 29.153  0.088   122.427 1.00 24.75 ? 589  GLN D C   1 
ATOM   18674 O  O   . GLN D 1 597 ? 28.828  1.276   122.374 1.00 26.33 ? 589  GLN D O   1 
ATOM   18675 C  CB  . GLN D 1 597 ? 31.160  -0.687  121.164 1.00 21.09 ? 589  GLN D CB  1 
ATOM   18676 C  CG  . GLN D 1 597 ? 31.746  -1.398  119.952 1.00 17.76 ? 589  GLN D CG  1 
ATOM   18677 C  CD  . GLN D 1 597 ? 31.261  -2.833  119.825 1.00 21.44 ? 589  GLN D CD  1 
ATOM   18678 O  OE1 . GLN D 1 597 ? 31.422  -3.642  120.739 1.00 23.57 ? 589  GLN D OE1 1 
ATOM   18679 N  NE2 . GLN D 1 597 ? 30.647  -3.148  118.690 1.00 17.01 ? 589  GLN D NE2 1 
ATOM   18680 N  N   . ASP D 1 598 ? 29.116  -0.626  123.553 1.00 23.15 ? 590  ASP D N   1 
ATOM   18681 C  CA  . ASP D 1 598 ? 28.671  -0.019  124.801 1.00 28.16 ? 590  ASP D CA  1 
ATOM   18682 C  C   . ASP D 1 598 ? 29.525  1.205   125.141 1.00 29.22 ? 590  ASP D C   1 
ATOM   18683 O  O   . ASP D 1 598 ? 30.672  1.349   124.700 1.00 22.15 ? 590  ASP D O   1 
ATOM   18684 C  CB  . ASP D 1 598 ? 28.702  -1.038  125.943 1.00 32.71 ? 590  ASP D CB  1 
ATOM   18685 C  CG  . ASP D 1 598 ? 30.099  -1.570  126.225 1.00 36.38 ? 590  ASP D CG  1 
ATOM   18686 O  OD1 . ASP D 1 598 ? 30.862  -0.900  126.958 1.00 34.38 ? 590  ASP D OD1 1 
ATOM   18687 O  OD2 . ASP D 1 598 ? 30.429  -2.663  125.717 1.00 33.00 ? 590  ASP D OD2 1 
ATOM   18688 N  N   . ALA D 1 599 ? 28.932  2.109   125.924 1.00 28.81 ? 591  ALA D N   1 
ATOM   18689 C  CA  . ALA D 1 599 ? 29.555  3.406   126.167 1.00 32.40 ? 591  ALA D CA  1 
ATOM   18690 C  C   . ALA D 1 599 ? 30.877  3.259   126.906 1.00 28.99 ? 591  ALA D C   1 
ATOM   18691 O  O   . ALA D 1 599 ? 31.826  4.014   126.656 1.00 30.32 ? 591  ALA D O   1 
ATOM   18692 C  CB  . ALA D 1 599 ? 28.599  4.307   126.957 1.00 30.35 ? 591  ALA D CB  1 
ATOM   18693 N  N   . ALA D 1 600 ? 30.957  2.298   127.826 1.00 29.73 ? 592  ALA D N   1 
ATOM   18694 C  CA  . ALA D 1 600 ? 32.187  2.116   128.586 1.00 30.30 ? 592  ALA D CA  1 
ATOM   18695 C  C   . ALA D 1 600 ? 33.339  1.714   127.672 1.00 29.11 ? 592  ALA D C   1 
ATOM   18696 O  O   . ALA D 1 600 ? 34.461  2.217   127.817 1.00 27.31 ? 592  ALA D O   1 
ATOM   18697 C  CB  . ALA D 1 600 ? 31.971  1.083   129.695 1.00 34.00 ? 592  ALA D CB  1 
ATOM   18698 N  N   . TYR D 1 601 ? 33.076  0.834   126.701 1.00 23.45 ? 593  TYR D N   1 
ATOM   18699 C  CA  . TYR D 1 601 ? 34.133  0.428   125.782 1.00 22.04 ? 593  TYR D CA  1 
ATOM   18700 C  C   . TYR D 1 601 ? 34.582  1.581   124.891 1.00 24.81 ? 593  TYR D C   1 
ATOM   18701 O  O   . TYR D 1 601 ? 35.788  1.776   124.677 1.00 23.71 ? 593  TYR D O   1 
ATOM   18702 C  CB  . TYR D 1 601 ? 33.679  -0.744  124.919 1.00 27.48 ? 593  TYR D CB  1 
ATOM   18703 C  CG  . TYR D 1 601 ? 34.770  -1.170  123.973 1.00 27.94 ? 593  TYR D CG  1 
ATOM   18704 C  CD1 . TYR D 1 601 ? 35.856  -1.892  124.437 1.00 26.24 ? 593  TYR D CD1 1 
ATOM   18705 C  CD2 . TYR D 1 601 ? 34.733  -0.826  122.623 1.00 26.35 ? 593  TYR D CD2 1 
ATOM   18706 C  CE1 . TYR D 1 601 ? 36.864  -2.286  123.586 1.00 24.35 ? 593  TYR D CE1 1 
ATOM   18707 C  CE2 . TYR D 1 601 ? 35.741  -1.213  121.765 1.00 19.10 ? 593  TYR D CE2 1 
ATOM   18708 C  CZ  . TYR D 1 601 ? 36.809  -1.943  122.259 1.00 21.47 ? 593  TYR D CZ  1 
ATOM   18709 O  OH  . TYR D 1 601 ? 37.831  -2.344  121.426 1.00 19.78 ? 593  TYR D OH  1 
ATOM   18710 N  N   . GLN D 1 602 ? 33.632  2.337   124.335 1.00 21.09 ? 594  GLN D N   1 
ATOM   18711 C  CA  . GLN D 1 602 ? 33.998  3.480   123.506 1.00 21.10 ? 594  GLN D CA  1 
ATOM   18712 C  C   . GLN D 1 602 ? 34.918  4.419   124.270 1.00 25.12 ? 594  GLN D C   1 
ATOM   18713 O  O   . GLN D 1 602 ? 35.944  4.872   123.748 1.00 23.73 ? 594  GLN D O   1 
ATOM   18714 C  CB  . GLN D 1 602 ? 32.740  4.216   123.039 1.00 27.35 ? 594  GLN D CB  1 
ATOM   18715 C  CG  . GLN D 1 602 ? 31.774  3.345   122.246 1.00 29.54 ? 594  GLN D CG  1 
ATOM   18716 C  CD  . GLN D 1 602 ? 30.893  4.158   121.318 1.00 33.70 ? 594  GLN D CD  1 
ATOM   18717 O  OE1 . GLN D 1 602 ? 31.314  5.189   120.795 1.00 40.22 ? 594  GLN D OE1 1 
ATOM   18718 N  NE2 . GLN D 1 602 ? 29.669  3.695   121.104 1.00 31.36 ? 594  GLN D NE2 1 
ATOM   18719 N  N   . ALA D 1 603 ? 34.572  4.695   125.529 1.00 26.35 ? 595  ALA D N   1 
ATOM   18720 C  CA  . ALA D 1 603 ? 35.410  5.533   126.380 1.00 32.22 ? 595  ALA D CA  1 
ATOM   18721 C  C   . ALA D 1 603 ? 36.777  4.906   126.643 1.00 30.84 ? 595  ALA D C   1 
ATOM   18722 O  O   . ALA D 1 603 ? 37.778  5.626   126.751 1.00 29.78 ? 595  ALA D O   1 
ATOM   18723 C  CB  . ALA D 1 603 ? 34.690  5.810   127.702 1.00 34.29 ? 595  ALA D CB  1 
ATOM   18724 N  N   . ALA D 1 604 ? 36.846  3.578   126.774 1.00 27.61 ? 596  ALA D N   1 
ATOM   18725 C  CA  . ALA D 1 604 ? 38.146  2.941   126.972 1.00 25.09 ? 596  ALA D CA  1 
ATOM   18726 C  C   . ALA D 1 604 ? 39.059  3.148   125.772 1.00 24.98 ? 596  ALA D C   1 
ATOM   18727 O  O   . ALA D 1 604 ? 40.280  3.278   125.931 1.00 23.95 ? 596  ALA D O   1 
ATOM   18728 C  CB  . ALA D 1 604 ? 37.973  1.448   127.247 1.00 30.08 ? 596  ALA D CB  1 
ATOM   18729 N  N   . VAL D 1 605 ? 38.488  3.189   124.569 1.00 27.17 ? 597  VAL D N   1 
ATOM   18730 C  CA  . VAL D 1 605 ? 39.289  3.330   123.360 1.00 25.27 ? 597  VAL D CA  1 
ATOM   18731 C  C   . VAL D 1 605 ? 39.631  4.794   123.105 1.00 21.16 ? 597  VAL D C   1 
ATOM   18732 O  O   . VAL D 1 605 ? 40.773  5.125   122.768 1.00 21.23 ? 597  VAL D O   1 
ATOM   18733 C  CB  . VAL D 1 605 ? 38.540  2.689   122.179 1.00 25.92 ? 597  VAL D CB  1 
ATOM   18734 C  CG1 . VAL D 1 605 ? 39.259  2.946   120.858 1.00 19.31 ? 597  VAL D CG1 1 
ATOM   18735 C  CG2 . VAL D 1 605 ? 38.385  1.193   122.422 1.00 21.41 ? 597  VAL D CG2 1 
ATOM   18736 N  N   . LEU D 1 606 ? 38.655  5.692   123.285 1.00 24.44 ? 598  LEU D N   1 
ATOM   18737 C  CA  . LEU D 1 606 ? 38.802  7.124   123.032 1.00 21.39 ? 598  LEU D CA  1 
ATOM   18738 C  C   . LEU D 1 606 ? 38.451  7.861   124.318 1.00 23.62 ? 598  LEU D C   1 
ATOM   18739 O  O   . LEU D 1 606 ? 37.329  8.365   124.461 1.00 23.73 ? 598  LEU D O   1 
ATOM   18740 C  CB  . LEU D 1 606 ? 37.899  7.589   121.887 1.00 20.53 ? 598  LEU D CB  1 
ATOM   18741 C  CG  . LEU D 1 606 ? 38.062  6.910   120.533 1.00 24.73 ? 598  LEU D CG  1 
ATOM   18742 C  CD1 . LEU D 1 606 ? 37.105  7.507   119.512 1.00 18.79 ? 598  LEU D CD1 1 
ATOM   18743 C  CD2 . LEU D 1 606 ? 39.499  7.030   120.057 1.00 29.11 ? 598  LEU D CD2 1 
ATOM   18744 N  N   . PRO D 1 607 ? 39.384  7.949   125.273 1.00 26.36 ? 599  PRO D N   1 
ATOM   18745 C  CA  . PRO D 1 607 ? 39.066  8.578   126.563 1.00 25.69 ? 599  PRO D CA  1 
ATOM   18746 C  C   . PRO D 1 607 ? 38.616  10.021  126.407 1.00 30.67 ? 599  PRO D C   1 
ATOM   18747 O  O   . PRO D 1 607 ? 39.119  10.762  125.560 1.00 24.75 ? 599  PRO D O   1 
ATOM   18748 C  CB  . PRO D 1 607 ? 40.387  8.496   127.335 1.00 31.06 ? 599  PRO D CB  1 
ATOM   18749 C  CG  . PRO D 1 607 ? 41.150  7.399   126.680 1.00 32.74 ? 599  PRO D CG  1 
ATOM   18750 C  CD  . PRO D 1 607 ? 40.767  7.450   125.228 1.00 31.07 ? 599  PRO D CD  1 
ATOM   18751 N  N   . GLU D 1 608 ? 37.667  10.421  127.249 1.00 29.55 ? 600  GLU D N   1 
ATOM   18752 C  CA  . GLU D 1 608 ? 37.215  11.804  127.250 1.00 32.00 ? 600  GLU D CA  1 
ATOM   18753 C  C   . GLU D 1 608 ? 38.349  12.727  127.680 1.00 37.66 ? 600  GLU D C   1 
ATOM   18754 O  O   . GLU D 1 608 ? 39.093  12.431  128.621 1.00 42.33 ? 600  GLU D O   1 
ATOM   18755 C  CB  . GLU D 1 608 ? 36.008  11.969  128.176 1.00 32.40 ? 600  GLU D CB  1 
ATOM   18756 N  N   . GLY D 1 609 ? 38.491  13.846  126.973 1.00 38.20 ? 601  GLY D N   1 
ATOM   18757 C  CA  . GLY D 1 609 ? 39.523  14.811  127.280 1.00 44.08 ? 601  GLY D CA  1 
ATOM   18758 C  C   . GLY D 1 609 ? 40.864  14.551  126.631 1.00 41.13 ? 601  GLY D C   1 
ATOM   18759 O  O   . GLY D 1 609 ? 41.796  15.336  126.841 1.00 43.56 ? 601  GLY D O   1 
ATOM   18760 N  N   . LEU D 1 610 ? 40.997  13.480  125.854 1.00 31.38 ? 602  LEU D N   1 
ATOM   18761 C  CA  . LEU D 1 610 ? 42.244  13.186  125.167 1.00 32.46 ? 602  LEU D CA  1 
ATOM   18762 C  C   . LEU D 1 610 ? 42.131  13.631  123.720 1.00 29.22 ? 602  LEU D C   1 
ATOM   18763 O  O   . LEU D 1 610 ? 41.279  13.100  122.988 1.00 33.78 ? 602  LEU D O   1 
ATOM   18764 C  CB  . LEU D 1 610 ? 42.556  11.696  125.238 1.00 34.18 ? 602  LEU D CB  1 
ATOM   18765 C  CG  . LEU D 1 610 ? 43.925  11.232  124.742 1.00 35.49 ? 602  LEU D CG  1 
ATOM   18766 C  CD1 . LEU D 1 610 ? 45.034  11.790  125.618 1.00 37.72 ? 602  LEU D CD1 1 
ATOM   18767 C  CD2 . LEU D 1 610 ? 43.984  9.707   124.699 1.00 33.20 ? 602  LEU D CD2 1 
ATOM   18768 N  N   . PRO D 1 611 ? 42.946  14.586  123.270 1.00 26.91 ? 603  PRO D N   1 
ATOM   18769 C  CA  . PRO D 1 611 ? 42.829  15.078  121.892 1.00 27.94 ? 603  PRO D CA  1 
ATOM   18770 C  C   . PRO D 1 611 ? 43.002  13.949  120.888 1.00 25.06 ? 603  PRO D C   1 
ATOM   18771 O  O   . PRO D 1 611 ? 43.831  13.052  121.073 1.00 24.46 ? 603  PRO D O   1 
ATOM   18772 C  CB  . PRO D 1 611 ? 43.962  16.105  121.786 1.00 33.39 ? 603  PRO D CB  1 
ATOM   18773 C  CG  . PRO D 1 611 ? 44.234  16.513  123.201 1.00 35.52 ? 603  PRO D CG  1 
ATOM   18774 C  CD  . PRO D 1 611 ? 44.005  15.282  124.019 1.00 27.96 ? 603  PRO D CD  1 
ATOM   18775 N  N   . ARG D 1 612 ? 42.201  14.001  119.825 1.00 24.35 ? 604  ARG D N   1 
ATOM   18776 C  CA  . ARG D 1 612 ? 42.126  12.946  118.818 1.00 20.92 ? 604  ARG D CA  1 
ATOM   18777 C  C   . ARG D 1 612 ? 42.592  13.466  117.464 1.00 26.70 ? 604  ARG D C   1 
ATOM   18778 O  O   . ARG D 1 612 ? 42.229  14.571  117.052 1.00 25.77 ? 604  ARG D O   1 
ATOM   18779 C  CB  . ARG D 1 612 ? 40.690  12.406  118.694 1.00 20.27 ? 604  ARG D CB  1 
ATOM   18780 C  CG  . ARG D 1 612 ? 40.109  11.896  120.014 1.00 20.82 ? 604  ARG D CG  1 
ATOM   18781 C  CD  . ARG D 1 612 ? 38.595  11.744  119.942 1.00 24.23 ? 604  ARG D CD  1 
ATOM   18782 N  NE  . ARG D 1 612 ? 38.044  11.242  121.205 1.00 26.11 ? 604  ARG D NE  1 
ATOM   18783 C  CZ  . ARG D 1 612 ? 36.750  11.255  121.522 1.00 31.28 ? 604  ARG D CZ  1 
ATOM   18784 N  NH1 . ARG D 1 612 ? 35.859  11.752  120.674 1.00 28.92 ? 604  ARG D NH1 1 
ATOM   18785 N  NH2 . ARG D 1 612 ? 36.343  10.770  122.691 1.00 31.54 ? 604  ARG D NH2 1 
ATOM   18786 N  N   . ILE D 1 613 ? 43.393  12.662  116.771 1.00 24.31 ? 605  ILE D N   1 
ATOM   18787 C  CA  . ILE D 1 613 ? 43.819  12.957  115.406 1.00 21.46 ? 605  ILE D CA  1 
ATOM   18788 C  C   . ILE D 1 613 ? 43.493  11.739  114.555 1.00 23.51 ? 605  ILE D C   1 
ATOM   18789 O  O   . ILE D 1 613 ? 43.951  10.627  114.848 1.00 21.92 ? 605  ILE D O   1 
ATOM   18790 C  CB  . ILE D 1 613 ? 45.320  13.301  115.313 1.00 22.57 ? 605  ILE D CB  1 
ATOM   18791 C  CG1 . ILE D 1 613 ? 45.677  14.489  116.214 1.00 21.21 ? 605  ILE D CG1 1 
ATOM   18792 C  CG2 . ILE D 1 613 ? 45.729  13.590  113.864 1.00 19.82 ? 605  ILE D CG2 1 
ATOM   18793 C  CD1 . ILE D 1 613 ? 46.168  14.078  117.613 1.00 24.74 ? 605  ILE D CD1 1 
ATOM   18794 N  N   . ALA D 1 614 ? 42.707  11.939  113.508 1.00 20.94 ? 606  ALA D N   1 
ATOM   18795 C  CA  . ALA D 1 614 ? 42.362  10.866  112.592 1.00 17.07 ? 606  ALA D CA  1 
ATOM   18796 C  C   . ALA D 1 614 ? 43.280  10.921  111.380 1.00 16.90 ? 606  ALA D C   1 
ATOM   18797 O  O   . ALA D 1 614 ? 43.614  12.008  110.898 1.00 19.80 ? 606  ALA D O   1 
ATOM   18798 C  CB  . ALA D 1 614 ? 40.901  10.978  112.163 1.00 18.08 ? 606  ALA D CB  1 
ATOM   18799 N  N   . VAL D 1 615 ? 43.705  9.748   110.906 1.00 18.86 ? 607  VAL D N   1 
ATOM   18800 C  CA  . VAL D 1 615 ? 44.595  9.629   109.754 1.00 18.20 ? 607  VAL D CA  1 
ATOM   18801 C  C   . VAL D 1 615 ? 44.010  8.590   108.808 1.00 18.77 ? 607  VAL D C   1 
ATOM   18802 O  O   . VAL D 1 615 ? 43.888  7.413   109.164 1.00 16.67 ? 607  VAL D O   1 
ATOM   18803 C  CB  . VAL D 1 615 ? 46.027  9.244   110.158 1.00 20.31 ? 607  VAL D CB  1 
ATOM   18804 C  CG1 . VAL D 1 615 ? 46.932  9.184   108.930 1.00 17.68 ? 607  VAL D CG1 1 
ATOM   18805 C  CG2 . VAL D 1 615 ? 46.563  10.220  111.173 1.00 20.42 ? 607  VAL D CG2 1 
ATOM   18806 N  N   . GLU D 1 616 ? 43.639  9.028   107.608 1.00 15.29 ? 608  GLU D N   1 
ATOM   18807 C  CA  . GLU D 1 616 ? 43.041  8.149   106.618 1.00 14.61 ? 608  GLU D CA  1 
ATOM   18808 C  C   . GLU D 1 616 ? 43.187  8.813   105.255 1.00 15.28 ? 608  GLU D C   1 
ATOM   18809 O  O   . GLU D 1 616 ? 42.935  10.011  105.125 1.00 16.59 ? 608  GLU D O   1 
ATOM   18810 C  CB  . GLU D 1 616 ? 41.570  7.896   106.959 1.00 16.77 ? 608  GLU D CB  1 
ATOM   18811 C  CG  . GLU D 1 616 ? 40.767  7.138   105.915 1.00 16.90 ? 608  GLU D CG  1 
ATOM   18812 C  CD  . GLU D 1 616 ? 39.383  6.770   106.436 1.00 17.65 ? 608  GLU D CD  1 
ATOM   18813 O  OE1 . GLU D 1 616 ? 38.486  7.646   106.418 1.00 16.19 ? 608  GLU D OE1 1 
ATOM   18814 O  OE2 . GLU D 1 616 ? 39.209  5.606   106.881 1.00 18.99 ? 608  GLU D OE2 1 
ATOM   18815 N  N   . ALA D 1 617 ? 43.592  8.035   104.246 1.00 14.25 ? 609  ALA D N   1 
ATOM   18816 C  CA  . ALA D 1 617 ? 43.793  8.562   102.896 1.00 14.16 ? 609  ALA D CA  1 
ATOM   18817 C  C   . ALA D 1 617 ? 42.454  8.755   102.179 1.00 17.37 ? 609  ALA D C   1 
ATOM   18818 O  O   . ALA D 1 617 ? 42.161  8.137   101.156 1.00 17.74 ? 609  ALA D O   1 
ATOM   18819 C  CB  . ALA D 1 617 ? 44.727  7.653   102.100 1.00 14.35 ? 609  ALA D CB  1 
ATOM   18820 N  N   . GLY D 1 618 ? 41.648  9.649   102.741 1.00 17.57 ? 610  GLY D N   1 
ATOM   18821 C  CA  . GLY D 1 618 ? 40.368  9.999   102.155 1.00 14.37 ? 610  GLY D CA  1 
ATOM   18822 C  C   . GLY D 1 618 ? 39.837  11.281  102.765 1.00 13.11 ? 610  GLY D C   1 
ATOM   18823 O  O   . GLY D 1 618 ? 40.509  11.936  103.569 1.00 14.41 ? 610  GLY D O   1 
ATOM   18824 N  N   . HIS D 1 619 ? 38.610  11.631  102.372 1.00 12.73 ? 611  HIS D N   1 
ATOM   18825 C  CA  . HIS D 1 619 ? 37.987  12.873  102.816 1.00 16.22 ? 611  HIS D CA  1 
ATOM   18826 C  C   . HIS D 1 619 ? 38.004  12.958  104.337 1.00 15.57 ? 611  HIS D C   1 
ATOM   18827 O  O   . HIS D 1 619 ? 37.832  11.951  105.025 1.00 16.77 ? 611  HIS D O   1 
ATOM   18828 C  CB  . HIS D 1 619 ? 36.543  12.965  102.286 1.00 13.42 ? 611  HIS D CB  1 
ATOM   18829 C  CG  . HIS D 1 619 ? 36.051  14.372  102.111 1.00 12.76 ? 611  HIS D CG  1 
ATOM   18830 N  ND1 . HIS D 1 619 ? 35.781  15.206  103.173 1.00 13.71 ? 611  HIS D ND1 1 
ATOM   18831 C  CD2 . HIS D 1 619 ? 35.804  15.096  100.993 1.00 14.81 ? 611  HIS D CD2 1 
ATOM   18832 C  CE1 . HIS D 1 619 ? 35.391  16.384  102.719 1.00 17.50 ? 611  HIS D CE1 1 
ATOM   18833 N  NE2 . HIS D 1 619 ? 35.393  16.342  101.399 1.00 15.48 ? 611  HIS D NE2 1 
ATOM   18834 N  N   . THR D 1 620 ? 38.233  14.169  104.858 1.00 14.79 ? 612  THR D N   1 
ATOM   18835 C  CA  . THR D 1 620 ? 38.324  14.391  106.302 1.00 15.66 ? 612  THR D CA  1 
ATOM   18836 C  C   . THR D 1 620 ? 36.984  14.615  106.988 1.00 17.74 ? 612  THR D C   1 
ATOM   18837 O  O   . THR D 1 620 ? 36.915  14.505  108.216 1.00 14.83 ? 612  THR D O   1 
ATOM   18838 C  CB  . THR D 1 620 ? 39.181  15.626  106.620 1.00 19.54 ? 612  THR D CB  1 
ATOM   18839 O  OG1 . THR D 1 620 ? 38.530  16.801  106.114 1.00 15.24 ? 612  THR D OG1 1 
ATOM   18840 C  CG2 . THR D 1 620 ? 40.579  15.503  106.021 1.00 15.35 ? 612  THR D CG2 1 
ATOM   18841 N  N   . ASN D 1 621 ? 35.927  14.958  106.250 1.00 16.34 ? 613  ASN D N   1 
ATOM   18842 C  CA  . ASN D 1 621 ? 34.841  15.680  106.907 1.00 20.60 ? 613  ASN D CA  1 
ATOM   18843 C  C   . ASN D 1 621 ? 34.014  14.770  107.815 1.00 24.62 ? 613  ASN D C   1 
ATOM   18844 O  O   . ASN D 1 621 ? 33.451  15.245  108.808 1.00 23.83 ? 613  ASN D O   1 
ATOM   18845 C  CB  . ASN D 1 621 ? 33.980  16.412  105.863 1.00 24.20 ? 613  ASN D CB  1 
ATOM   18846 C  CG  . ASN D 1 621 ? 34.530  17.824  105.519 1.00 31.46 ? 613  ASN D CG  1 
ATOM   18847 O  OD1 . ASN D 1 621 ? 33.808  18.692  105.011 1.00 28.04 ? 613  ASN D OD1 1 
ATOM   18848 N  ND2 . ASN D 1 621 ? 35.804  18.051  105.820 1.00 22.41 ? 613  ASN D ND2 1 
ATOM   18849 N  N   . GLY D 1 622 ? 33.988  13.459  107.553 1.00 21.55 ? 614  GLY D N   1 
ATOM   18850 C  CA  . GLY D 1 622 ? 33.279  12.563  108.457 1.00 17.03 ? 614  GLY D CA  1 
ATOM   18851 C  C   . GLY D 1 622 ? 33.981  12.333  109.784 1.00 22.70 ? 614  GLY D C   1 
ATOM   18852 O  O   . GLY D 1 622 ? 33.344  11.879  110.742 1.00 27.80 ? 614  GLY D O   1 
ATOM   18853 N  N   . TRP D 1 623 ? 35.276  12.637  109.871 1.00 18.17 ? 615  TRP D N   1 
ATOM   18854 C  CA  . TRP D 1 623 ? 36.018  12.361  111.096 1.00 21.49 ? 615  TRP D CA  1 
ATOM   18855 C  C   . TRP D 1 623 ? 35.745  13.360  112.213 1.00 20.81 ? 615  TRP D C   1 
ATOM   18856 O  O   . TRP D 1 623 ? 36.123  13.088  113.357 1.00 22.47 ? 615  TRP D O   1 
ATOM   18857 C  CB  . TRP D 1 623 ? 37.518  12.301  110.805 1.00 19.03 ? 615  TRP D CB  1 
ATOM   18858 C  CG  . TRP D 1 623 ? 37.861  11.022  110.121 1.00 15.74 ? 615  TRP D CG  1 
ATOM   18859 C  CD1 . TRP D 1 623 ? 38.146  10.847  108.804 1.00 14.29 ? 615  TRP D CD1 1 
ATOM   18860 C  CD2 . TRP D 1 623 ? 37.896  9.725   110.718 1.00 17.27 ? 615  TRP D CD2 1 
ATOM   18861 N  NE1 . TRP D 1 623 ? 38.379  9.522   108.544 1.00 18.82 ? 615  TRP D NE1 1 
ATOM   18862 C  CE2 . TRP D 1 623 ? 38.237  8.810   109.704 1.00 16.37 ? 615  TRP D CE2 1 
ATOM   18863 C  CE3 . TRP D 1 623 ? 37.671  9.248   112.009 1.00 18.73 ? 615  TRP D CE3 1 
ATOM   18864 C  CZ2 . TRP D 1 623 ? 38.344  7.445   109.933 1.00 15.99 ? 615  TRP D CZ2 1 
ATOM   18865 C  CZ3 . TRP D 1 623 ? 37.794  7.884   112.242 1.00 19.49 ? 615  TRP D CZ3 1 
ATOM   18866 C  CH2 . TRP D 1 623 ? 38.132  7.001   111.209 1.00 20.36 ? 615  TRP D CH2 1 
ATOM   18867 N  N   . TYR D 1 624 ? 35.075  14.482  111.930 1.00 17.60 ? 616  TYR D N   1 
ATOM   18868 C  CA  . TYR D 1 624 ? 34.826  15.468  112.979 1.00 17.02 ? 616  TYR D CA  1 
ATOM   18869 C  C   . TYR D 1 624 ? 33.839  14.964  114.014 1.00 22.36 ? 616  TYR D C   1 
ATOM   18870 O  O   . TYR D 1 624 ? 33.840  15.466  115.143 1.00 20.27 ? 616  TYR D O   1 
ATOM   18871 C  CB  . TYR D 1 624 ? 34.345  16.787  112.366 1.00 21.08 ? 616  TYR D CB  1 
ATOM   18872 C  CG  . TYR D 1 624 ? 35.488  17.500  111.688 1.00 23.05 ? 616  TYR D CG  1 
ATOM   18873 C  CD1 . TYR D 1 624 ? 36.509  18.063  112.438 1.00 22.38 ? 616  TYR D CD1 1 
ATOM   18874 C  CD2 . TYR D 1 624 ? 35.573  17.567  110.306 1.00 23.49 ? 616  TYR D CD2 1 
ATOM   18875 C  CE1 . TYR D 1 624 ? 37.580  18.694  111.832 1.00 24.41 ? 616  TYR D CE1 1 
ATOM   18876 C  CE2 . TYR D 1 624 ? 36.639  18.187  109.690 1.00 30.86 ? 616  TYR D CE2 1 
ATOM   18877 C  CZ  . TYR D 1 624 ? 37.638  18.757  110.460 1.00 29.07 ? 616  TYR D CZ  1 
ATOM   18878 O  OH  . TYR D 1 624 ? 38.702  19.382  109.854 1.00 31.26 ? 616  TYR D OH  1 
ATOM   18879 N  N   . LYS D 1 625 ? 33.010  13.982  113.652 1.00 20.48 ? 617  LYS D N   1 
ATOM   18880 C  CA  . LYS D 1 625 ? 32.163  13.311  114.631 1.00 25.37 ? 617  LYS D CA  1 
ATOM   18881 C  C   . LYS D 1 625 ? 32.984  12.788  115.801 1.00 22.61 ? 617  LYS D C   1 
ATOM   18882 O  O   . LYS D 1 625 ? 32.528  12.812  116.948 1.00 21.79 ? 617  LYS D O   1 
ATOM   18883 C  CB  . LYS D 1 625 ? 31.405  12.164  113.957 1.00 26.24 ? 617  LYS D CB  1 
ATOM   18884 C  CG  . LYS D 1 625 ? 30.546  11.337  114.891 1.00 35.11 ? 617  LYS D CG  1 
ATOM   18885 C  CD  . LYS D 1 625 ? 30.042  10.088  114.185 1.00 40.29 ? 617  LYS D CD  1 
ATOM   18886 C  CE  . LYS D 1 625 ? 29.367  9.137   115.158 1.00 43.69 ? 617  LYS D CE  1 
ATOM   18887 N  NZ  . LYS D 1 625 ? 28.886  7.912   114.468 1.00 41.99 ? 617  LYS D NZ  1 
ATOM   18888 N  N   . TYR D 1 626 ? 34.196  12.308  115.527 1.00 19.26 ? 618  TYR D N   1 
ATOM   18889 C  CA  . TYR D 1 626 ? 35.100  11.831  116.570 1.00 19.57 ? 618  TYR D CA  1 
ATOM   18890 C  C   . TYR D 1 626 ? 36.059  12.903  117.075 1.00 22.79 ? 618  TYR D C   1 
ATOM   18891 O  O   . TYR D 1 626 ? 36.258  13.014  118.287 1.00 23.89 ? 618  TYR D O   1 
ATOM   18892 C  CB  . TYR D 1 626 ? 35.907  10.627  116.075 1.00 19.79 ? 618  TYR D CB  1 
ATOM   18893 C  CG  . TYR D 1 626 ? 35.039  9.492   115.611 1.00 19.96 ? 618  TYR D CG  1 
ATOM   18894 C  CD1 . TYR D 1 626 ? 34.379  8.676   116.525 1.00 28.85 ? 618  TYR D CD1 1 
ATOM   18895 C  CD2 . TYR D 1 626 ? 34.837  9.258   114.257 1.00 29.57 ? 618  TYR D CD2 1 
ATOM   18896 C  CE1 . TYR D 1 626 ? 33.562  7.649   116.100 1.00 24.10 ? 618  TYR D CE1 1 
ATOM   18897 C  CE2 . TYR D 1 626 ? 34.025  8.225   113.824 1.00 33.73 ? 618  TYR D CE2 1 
ATOM   18898 C  CZ  . TYR D 1 626 ? 33.394  7.424   114.754 1.00 31.79 ? 618  TYR D CZ  1 
ATOM   18899 O  OH  . TYR D 1 626 ? 32.585  6.399   114.334 1.00 37.17 ? 618  TYR D OH  1 
ATOM   18900 N  N   . VAL D 1 627 ? 36.674  13.697  116.190 1.00 20.09 ? 619  VAL D N   1 
ATOM   18901 C  CA  . VAL D 1 627 ? 37.761  14.561  116.645 1.00 22.02 ? 619  VAL D CA  1 
ATOM   18902 C  C   . VAL D 1 627 ? 37.285  15.946  117.070 1.00 23.83 ? 619  VAL D C   1 
ATOM   18903 O  O   . VAL D 1 627 ? 38.017  16.646  117.786 1.00 25.33 ? 619  VAL D O   1 
ATOM   18904 C  CB  . VAL D 1 627 ? 38.880  14.697  115.592 1.00 26.67 ? 619  VAL D CB  1 
ATOM   18905 C  CG1 . VAL D 1 627 ? 39.299  13.315  115.062 1.00 20.03 ? 619  VAL D CG1 1 
ATOM   18906 C  CG2 . VAL D 1 627 ? 38.477  15.640  114.464 1.00 23.23 ? 619  VAL D CG2 1 
ATOM   18907 N  N   . GLY D 1 628 ? 36.081  16.354  116.675 1.00 23.99 ? 620  GLY D N   1 
ATOM   18908 C  CA  . GLY D 1 628 ? 35.555  17.623  117.143 1.00 24.43 ? 620  GLY D CA  1 
ATOM   18909 C  C   . GLY D 1 628 ? 36.346  18.819  116.629 1.00 27.03 ? 620  GLY D C   1 
ATOM   18910 O  O   . GLY D 1 628 ? 37.165  18.730  115.716 1.00 26.82 ? 620  GLY D O   1 
ATOM   18911 N  N   . LEU D 1 629 ? 36.089  19.964  117.264 1.00 23.51 ? 621  LEU D N   1 
ATOM   18912 C  CA  . LEU D 1 629 ? 36.671  21.223  116.822 1.00 27.18 ? 621  LEU D CA  1 
ATOM   18913 C  C   . LEU D 1 629 ? 38.115  21.399  117.266 1.00 30.07 ? 621  LEU D C   1 
ATOM   18914 O  O   . LEU D 1 629 ? 38.828  22.224  116.688 1.00 33.29 ? 621  LEU D O   1 
ATOM   18915 C  CB  . LEU D 1 629 ? 35.842  22.397  117.348 1.00 32.24 ? 621  LEU D CB  1 
ATOM   18916 C  CG  . LEU D 1 629 ? 34.425  22.521  116.793 1.00 26.70 ? 621  LEU D CG  1 
ATOM   18917 C  CD1 . LEU D 1 629 ? 33.735  23.753  117.379 1.00 25.05 ? 621  LEU D CD1 1 
ATOM   18918 C  CD2 . LEU D 1 629 ? 34.467  22.591  115.293 1.00 27.81 ? 621  LEU D CD2 1 
ATOM   18919 N  N   . ASN D 1 630 ? 38.551  20.669  118.285 1.00 30.00 ? 622  ASN D N   1 
ATOM   18920 C  CA  . ASN D 1 630 ? 39.892  20.830  118.825 1.00 35.55 ? 622  ASN D CA  1 
ATOM   18921 C  C   . ASN D 1 630 ? 40.840  19.716  118.399 1.00 35.41 ? 622  ASN D C   1 
ATOM   18922 O  O   . ASN D 1 630 ? 42.043  19.809  118.668 1.00 25.48 ? 622  ASN D O   1 
ATOM   18923 C  CB  . ASN D 1 630 ? 39.829  20.914  120.352 1.00 39.77 ? 622  ASN D CB  1 
ATOM   18924 C  CG  . ASN D 1 630 ? 38.876  21.994  120.826 1.00 45.84 ? 622  ASN D CG  1 
ATOM   18925 O  OD1 . ASN D 1 630 ? 38.817  23.077  120.246 1.00 41.55 ? 622  ASN D OD1 1 
ATOM   18926 N  ND2 . ASN D 1 630 ? 38.114  21.700  121.875 1.00 54.59 ? 622  ASN D ND2 1 
ATOM   18927 N  N   . GLY D 1 631 ? 40.334  18.679  117.739 1.00 31.67 ? 623  GLY D N   1 
ATOM   18928 C  CA  . GLY D 1 631 ? 41.164  17.661  117.134 1.00 28.28 ? 623  GLY D CA  1 
ATOM   18929 C  C   . GLY D 1 631 ? 41.605  18.073  115.745 1.00 24.17 ? 623  GLY D C   1 
ATOM   18930 O  O   . GLY D 1 631 ? 41.516  19.239  115.354 1.00 25.86 ? 623  GLY D O   1 
ATOM   18931 N  N   . ALA D 1 632 ? 42.094  17.095  114.991 1.00 20.66 ? 624  ALA D N   1 
ATOM   18932 C  CA  . ALA D 1 632 ? 42.548  17.352  113.632 1.00 27.57 ? 624  ALA D CA  1 
ATOM   18933 C  C   . ALA D 1 632 ? 42.468  16.058  112.831 1.00 24.67 ? 624  ALA D C   1 
ATOM   18934 O  O   . ALA D 1 632 ? 42.306  14.969  113.384 1.00 18.66 ? 624  ALA D O   1 
ATOM   18935 C  CB  . ALA D 1 632 ? 43.969  17.929  113.625 1.00 30.46 ? 624  ALA D CB  1 
ATOM   18936 N  N   . VAL D 1 633 ? 42.579  16.196  111.513 1.00 21.63 ? 625  VAL D N   1 
ATOM   18937 C  CA  . VAL D 1 633 ? 42.524  15.068  110.589 1.00 19.54 ? 625  VAL D CA  1 
ATOM   18938 C  C   . VAL D 1 633 ? 43.656  15.201  109.586 1.00 21.67 ? 625  VAL D C   1 
ATOM   18939 O  O   . VAL D 1 633 ? 43.939  16.301  109.099 1.00 23.27 ? 625  VAL D O   1 
ATOM   18940 C  CB  . VAL D 1 633 ? 41.180  14.991  109.831 1.00 18.68 ? 625  VAL D CB  1 
ATOM   18941 C  CG1 . VAL D 1 633 ? 41.081  13.659  109.061 1.00 15.97 ? 625  VAL D CG1 1 
ATOM   18942 C  CG2 . VAL D 1 633 ? 39.997  15.183  110.764 1.00 18.75 ? 625  VAL D CG2 1 
ATOM   18943 N  N   . VAL D 1 634 ? 44.287  14.077  109.262 1.00 18.86 ? 626  VAL D N   1 
ATOM   18944 C  CA  . VAL D 1 634 ? 45.196  13.972  108.128 1.00 17.64 ? 626  VAL D CA  1 
ATOM   18945 C  C   . VAL D 1 634 ? 44.448  13.203  107.047 1.00 19.13 ? 626  VAL D C   1 
ATOM   18946 O  O   . VAL D 1 634 ? 44.187  12.003  107.191 1.00 17.41 ? 626  VAL D O   1 
ATOM   18947 C  CB  . VAL D 1 634 ? 46.509  13.275  108.503 1.00 17.88 ? 626  VAL D CB  1 
ATOM   18948 C  CG1 . VAL D 1 634 ? 47.421  13.133  107.268 1.00 19.30 ? 626  VAL D CG1 1 
ATOM   18949 C  CG2 . VAL D 1 634 ? 47.200  14.038  109.616 1.00 21.49 ? 626  VAL D CG2 1 
ATOM   18950 N  N   . GLY D 1 635 ? 44.081  13.892  105.976 1.00 17.38 ? 627  GLY D N   1 
ATOM   18951 C  CA  . GLY D 1 635 ? 43.258  13.283  104.949 1.00 18.98 ? 627  GLY D CA  1 
ATOM   18952 C  C   . GLY D 1 635 ? 43.461  13.959  103.612 1.00 21.99 ? 627  GLY D C   1 
ATOM   18953 O  O   . GLY D 1 635 ? 44.451  14.673  103.421 1.00 18.14 ? 627  GLY D O   1 
ATOM   18954 N  N   . ILE D 1 636 ? 42.529  13.759  102.685 1.00 14.69 ? 628  ILE D N   1 
ATOM   18955 C  CA  . ILE D 1 636 ? 42.628  14.359  101.362 1.00 14.65 ? 628  ILE D CA  1 
ATOM   18956 C  C   . ILE D 1 636 ? 41.220  14.714  100.901 1.00 14.12 ? 628  ILE D C   1 
ATOM   18957 O  O   . ILE D 1 636 ? 40.330  13.859  100.880 1.00 13.55 ? 628  ILE D O   1 
ATOM   18958 C  CB  . ILE D 1 636 ? 43.352  13.419  100.377 1.00 18.96 ? 628  ILE D CB  1 
ATOM   18959 C  CG1 . ILE D 1 636 ? 43.364  13.999  98.961  1.00 14.55 ? 628  ILE D CG1 1 
ATOM   18960 C  CG2 . ILE D 1 636 ? 42.741  12.025  100.379 1.00 21.49 ? 628  ILE D CG2 1 
ATOM   18961 C  CD1 . ILE D 1 636 ? 44.074  13.109  97.985  1.00 21.19 ? 628  ILE D CD1 1 
ATOM   18962 N  N   . ASN D 1 637 ? 40.991  15.993  100.600 1.00 15.25 ? 629  ASN D N   1 
ATOM   18963 C  CA  . ASN D 1 637 ? 39.673  16.478  100.204 1.00 16.77 ? 629  ASN D CA  1 
ATOM   18964 C  C   . ASN D 1 637 ? 39.644  16.972  98.764  1.00 19.36 ? 629  ASN D C   1 
ATOM   18965 O  O   . ASN D 1 637 ? 38.717  17.686  98.384  1.00 21.03 ? 629  ASN D O   1 
ATOM   18966 C  CB  . ASN D 1 637 ? 39.194  17.592  101.131 1.00 14.40 ? 629  ASN D CB  1 
ATOM   18967 C  CG  . ASN D 1 637 ? 38.974  17.105  102.547 1.00 15.73 ? 629  ASN D CG  1 
ATOM   18968 O  OD1 . ASN D 1 637 ? 38.970  15.911  102.791 1.00 16.59 ? 629  ASN D OD1 1 
ATOM   18969 N  ND2 . ASN D 1 637 ? 38.793  18.030  103.483 1.00 19.81 ? 629  ASN D ND2 1 
ATOM   18970 N  N   . ARG D 1 638 ? 40.650  16.624  97.969  1.00 18.08 ? 630  ARG D N   1 
ATOM   18971 C  CA  . ARG D 1 638 ? 40.721  17.022  96.573  1.00 16.57 ? 630  ARG D CA  1 
ATOM   18972 C  C   . ARG D 1 638 ? 40.919  15.778  95.718  1.00 20.57 ? 630  ARG D C   1 
ATOM   18973 O  O   . ARG D 1 638 ? 41.210  14.690  96.224  1.00 17.34 ? 630  ARG D O   1 
ATOM   18974 C  CB  . ARG D 1 638 ? 41.852  18.021  96.331  1.00 16.81 ? 630  ARG D CB  1 
ATOM   18975 C  CG  . ARG D 1 638 ? 43.199  17.517  96.763  1.00 21.33 ? 630  ARG D CG  1 
ATOM   18976 C  CD  . ARG D 1 638 ? 44.307  18.088  95.873  1.00 29.65 ? 630  ARG D CD  1 
ATOM   18977 N  NE  . ARG D 1 638 ? 44.334  17.403  94.584  1.00 29.47 ? 630  ARG D NE  1 
ATOM   18978 C  CZ  . ARG D 1 638 ? 45.183  17.672  93.599  1.00 30.43 ? 630  ARG D CZ  1 
ATOM   18979 N  NH1 . ARG D 1 638 ? 46.094  18.629  93.738  1.00 32.03 ? 630  ARG D NH1 1 
ATOM   18980 N  NH2 . ARG D 1 638 ? 45.116  16.982  92.472  1.00 28.08 ? 630  ARG D NH2 1 
ATOM   18981 N  N   . PHE D 1 639 ? 40.737  15.943  94.410  1.00 13.73 ? 631  PHE D N   1 
ATOM   18982 C  CA  . PHE D 1 639 ? 40.912  14.825  93.502  1.00 13.50 ? 631  PHE D CA  1 
ATOM   18983 C  C   . PHE D 1 639 ? 42.385  14.427  93.452  1.00 14.28 ? 631  PHE D C   1 
ATOM   18984 O  O   . PHE D 1 639 ? 43.271  15.210  93.796  1.00 15.26 ? 631  PHE D O   1 
ATOM   18985 C  CB  . PHE D 1 639 ? 40.407  15.182  92.108  1.00 18.16 ? 631  PHE D CB  1 
ATOM   18986 C  CG  . PHE D 1 639 ? 38.915  15.342  92.028  1.00 13.84 ? 631  PHE D CG  1 
ATOM   18987 C  CD1 . PHE D 1 639 ? 38.081  14.259  92.235  1.00 18.27 ? 631  PHE D CD1 1 
ATOM   18988 C  CD2 . PHE D 1 639 ? 38.350  16.581  91.752  1.00 13.10 ? 631  PHE D CD2 1 
ATOM   18989 C  CE1 . PHE D 1 639 ? 36.702  14.412  92.158  1.00 20.07 ? 631  PHE D CE1 1 
ATOM   18990 C  CE2 . PHE D 1 639 ? 36.980  16.739  91.684  1.00 12.71 ? 631  PHE D CE2 1 
ATOM   18991 C  CZ  . PHE D 1 639 ? 36.160  15.657  91.873  1.00 12.17 ? 631  PHE D CZ  1 
ATOM   18992 N  N   . GLY D 1 640 ? 42.636  13.191  93.026  1.00 14.55 ? 632  GLY D N   1 
ATOM   18993 C  CA  . GLY D 1 640 ? 43.978  12.640  92.996  1.00 17.41 ? 632  GLY D CA  1 
ATOM   18994 C  C   . GLY D 1 640 ? 44.777  13.092  91.787  1.00 17.63 ? 632  GLY D C   1 
ATOM   18995 O  O   . GLY D 1 640 ? 44.472  14.095  91.143  1.00 18.28 ? 632  GLY D O   1 
ATOM   18996 N  N   . GLU D 1 641 ? 45.835  12.334  91.495  1.00 16.40 ? 633  GLU D N   1 
ATOM   18997 C  CA  . GLU D 1 641 ? 46.750  12.589  90.392  1.00 18.00 ? 633  GLU D CA  1 
ATOM   18998 C  C   . GLU D 1 641 ? 47.225  11.254  89.839  1.00 19.69 ? 633  GLU D C   1 
ATOM   18999 O  O   . GLU D 1 641 ? 47.403  10.287  90.586  1.00 16.28 ? 633  GLU D O   1 
ATOM   19000 C  CB  . GLU D 1 641 ? 47.996  13.402  90.824  1.00 21.51 ? 633  GLU D CB  1 
ATOM   19001 C  CG  . GLU D 1 641 ? 47.743  14.845  91.204  1.00 19.04 ? 633  GLU D CG  1 
ATOM   19002 C  CD  . GLU D 1 641 ? 47.371  15.728  90.027  1.00 24.86 ? 633  GLU D CD  1 
ATOM   19003 O  OE1 . GLU D 1 641 ? 47.602  15.330  88.863  1.00 23.49 ? 633  GLU D OE1 1 
ATOM   19004 O  OE2 . GLU D 1 641 ? 46.828  16.824  90.278  1.00 23.30 ? 633  GLU D OE2 1 
ATOM   19005 N  N   . SER D 1 642 ? 47.438  11.207  88.526  1.00 16.82 ? 634  SER D N   1 
ATOM   19006 C  CA  . SER D 1 642 ? 48.027  10.031  87.889  1.00 17.20 ? 634  SER D CA  1 
ATOM   19007 C  C   . SER D 1 642 ? 49.532  10.070  88.125  1.00 19.90 ? 634  SER D C   1 
ATOM   19008 O  O   . SER D 1 642 ? 50.221  10.946  87.594  1.00 18.94 ? 634  SER D O   1 
ATOM   19009 C  CB  . SER D 1 642 ? 47.689  10.005  86.398  1.00 19.27 ? 634  SER D CB  1 
ATOM   19010 O  OG  . SER D 1 642 ? 48.324  8.919   85.730  1.00 21.12 ? 634  SER D OG  1 
ATOM   19011 N  N   . ALA D 1 643 ? 50.032  9.135   88.929  1.00 18.27 ? 635  ALA D N   1 
ATOM   19012 C  CA  . ALA D 1 643 ? 51.442  9.030   89.287  1.00 19.25 ? 635  ALA D CA  1 
ATOM   19013 C  C   . ALA D 1 643 ? 51.633  7.752   90.110  1.00 20.38 ? 635  ALA D C   1 
ATOM   19014 O  O   . ALA D 1 643 ? 50.653  7.193   90.618  1.00 20.35 ? 635  ALA D O   1 
ATOM   19015 C  CB  . ALA D 1 643 ? 51.913  10.253  90.092  1.00 20.47 ? 635  ALA D CB  1 
ATOM   19016 N  N   . PRO D 1 644 ? 52.874  7.276   90.251  1.00 20.05 ? 636  PRO D N   1 
ATOM   19017 C  CA  . PRO D 1 644 ? 53.122  6.127   91.139  1.00 21.74 ? 636  PRO D CA  1 
ATOM   19018 C  C   . PRO D 1 644 ? 52.679  6.402   92.574  1.00 21.55 ? 636  PRO D C   1 
ATOM   19019 O  O   . PRO D 1 644 ? 52.770  7.524   93.076  1.00 23.57 ? 636  PRO D O   1 
ATOM   19020 C  CB  . PRO D 1 644 ? 54.637  5.929   91.049  1.00 23.38 ? 636  PRO D CB  1 
ATOM   19021 C  CG  . PRO D 1 644 ? 54.979  6.425   89.663  1.00 25.53 ? 636  PRO D CG  1 
ATOM   19022 C  CD  . PRO D 1 644 ? 54.054  7.600   89.426  1.00 23.84 ? 636  PRO D CD  1 
ATOM   19023 N  N   . ALA D 1 645 ? 52.201  5.343   93.234  1.00 19.83 ? 637  ALA D N   1 
ATOM   19024 C  CA  . ALA D 1 645 ? 51.525  5.497   94.520  1.00 22.83 ? 637  ALA D CA  1 
ATOM   19025 C  C   . ALA D 1 645 ? 52.461  6.041   95.599  1.00 18.86 ? 637  ALA D C   1 
ATOM   19026 O  O   . ALA D 1 645 ? 52.031  6.803   96.472  1.00 20.88 ? 637  ALA D O   1 
ATOM   19027 C  CB  . ALA D 1 645 ? 50.927  4.162   94.963  1.00 27.78 ? 637  ALA D CB  1 
ATOM   19028 N  N   . ASP D 1 646 ? 53.737  5.645   95.574  1.00 19.86 ? 638  ASP D N   1 
ATOM   19029 C  CA  . ASP D 1 646 ? 54.674  6.144   96.576  1.00 33.92 ? 638  ASP D CA  1 
ATOM   19030 C  C   . ASP D 1 646 ? 54.744  7.669   96.545  1.00 34.22 ? 638  ASP D C   1 
ATOM   19031 O  O   . ASP D 1 646 ? 54.629  8.331   97.585  1.00 29.58 ? 638  ASP D O   1 
ATOM   19032 C  CB  . ASP D 1 646 ? 56.059  5.528   96.355  1.00 37.47 ? 638  ASP D CB  1 
ATOM   19033 N  N   . LEU D 1 647 ? 54.923  8.244   95.350  1.00 27.75 ? 639  LEU D N   1 
ATOM   19034 C  CA  . LEU D 1 647 ? 54.995  9.694   95.226  1.00 24.48 ? 639  LEU D CA  1 
ATOM   19035 C  C   . LEU D 1 647 ? 53.685  10.349  95.640  1.00 23.89 ? 639  LEU D C   1 
ATOM   19036 O  O   . LEU D 1 647 ? 53.685  11.443  96.215  1.00 22.75 ? 639  LEU D O   1 
ATOM   19037 C  CB  . LEU D 1 647 ? 55.353  10.083  93.790  1.00 28.30 ? 639  LEU D CB  1 
ATOM   19038 C  CG  . LEU D 1 647 ? 56.710  9.620   93.258  1.00 42.26 ? 639  LEU D CG  1 
ATOM   19039 C  CD1 . LEU D 1 647 ? 56.939  10.158  91.845  1.00 46.41 ? 639  LEU D CD1 1 
ATOM   19040 C  CD2 . LEU D 1 647 ? 57.847  10.030  94.190  1.00 43.34 ? 639  LEU D CD2 1 
ATOM   19041 N  N   . LEU D 1 648 ? 52.553  9.706   95.340  1.00 19.29 ? 640  LEU D N   1 
ATOM   19042 C  CA  . LEU D 1 648 ? 51.262  10.305  95.668  1.00 18.39 ? 640  LEU D CA  1 
ATOM   19043 C  C   . LEU D 1 648 ? 51.083  10.460  97.174  1.00 25.71 ? 640  LEU D C   1 
ATOM   19044 O  O   . LEU D 1 648 ? 50.699  11.533  97.652  1.00 21.06 ? 640  LEU D O   1 
ATOM   19045 C  CB  . LEU D 1 648 ? 50.127  9.470   95.089  1.00 17.49 ? 640  LEU D CB  1 
ATOM   19046 C  CG  . LEU D 1 648 ? 50.063  9.480   93.566  1.00 18.58 ? 640  LEU D CG  1 
ATOM   19047 C  CD1 . LEU D 1 648 ? 48.902  8.574   93.134  1.00 19.84 ? 640  LEU D CD1 1 
ATOM   19048 C  CD2 . LEU D 1 648 ? 49.876  10.901  93.058  1.00 21.33 ? 640  LEU D CD2 1 
ATOM   19049 N  N   . PHE D 1 649 ? 51.333  9.387   97.936  1.00 20.78 ? 641  PHE D N   1 
ATOM   19050 C  CA  . PHE D 1 649 ? 51.189  9.477   99.388  1.00 24.93 ? 641  PHE D CA  1 
ATOM   19051 C  C   . PHE D 1 649 ? 52.043  10.606  99.950  1.00 23.31 ? 641  PHE D C   1 
ATOM   19052 O  O   . PHE D 1 649 ? 51.594  11.359  100.820 1.00 23.25 ? 641  PHE D O   1 
ATOM   19053 C  CB  . PHE D 1 649 ? 51.554  8.146   100.051 1.00 18.31 ? 641  PHE D CB  1 
ATOM   19054 C  CG  . PHE D 1 649 ? 50.449  7.118   100.011 1.00 20.52 ? 641  PHE D CG  1 
ATOM   19055 C  CD1 . PHE D 1 649 ? 49.176  7.421   100.480 1.00 16.86 ? 641  PHE D CD1 1 
ATOM   19056 C  CD2 . PHE D 1 649 ? 50.683  5.849   99.501  1.00 20.70 ? 641  PHE D CD2 1 
ATOM   19057 C  CE1 . PHE D 1 649 ? 48.160  6.469   100.444 1.00 17.08 ? 641  PHE D CE1 1 
ATOM   19058 C  CE2 . PHE D 1 649 ? 49.666  4.897   99.466  1.00 18.73 ? 641  PHE D CE2 1 
ATOM   19059 C  CZ  . PHE D 1 649 ? 48.411  5.212   99.941  1.00 20.89 ? 641  PHE D CZ  1 
ATOM   19060 N  N   . LYS D 1 650 ? 53.269  10.756  99.439  1.00 24.40 ? 642  LYS D N   1 
ATOM   19061 C  CA  . LYS D 1 650 ? 54.143  11.827  99.907  1.00 24.69 ? 642  LYS D CA  1 
ATOM   19062 C  C   . LYS D 1 650 ? 53.602  13.193  99.499  1.00 25.13 ? 642  LYS D C   1 
ATOM   19063 O  O   . LYS D 1 650 ? 53.518  14.109  100.324 1.00 29.47 ? 642  LYS D O   1 
ATOM   19064 C  CB  . LYS D 1 650 ? 55.563  11.621  99.370  1.00 27.89 ? 642  LYS D CB  1 
ATOM   19065 N  N   . ALA D 1 651 ? 53.215  13.344  98.231  1.00 25.23 ? 643  ALA D N   1 
ATOM   19066 C  CA  . ALA D 1 651 ? 52.736  14.638  97.757  1.00 20.34 ? 643  ALA D CA  1 
ATOM   19067 C  C   . ALA D 1 651 ? 51.483  15.087  98.500  1.00 24.46 ? 643  ALA D C   1 
ATOM   19068 O  O   . ALA D 1 651 ? 51.281  16.289  98.706  1.00 28.70 ? 643  ALA D O   1 
ATOM   19069 C  CB  . ALA D 1 651 ? 52.470  14.575  96.256  1.00 23.61 ? 643  ALA D CB  1 
ATOM   19070 N  N   . PHE D 1 652 ? 50.637  14.149  98.919  1.00 21.25 ? 644  PHE D N   1 
ATOM   19071 C  CA  . PHE D 1 652 ? 49.397  14.503  99.596  1.00 22.98 ? 644  PHE D CA  1 
ATOM   19072 C  C   . PHE D 1 652 ? 49.518  14.479  101.110 1.00 24.70 ? 644  PHE D C   1 
ATOM   19073 O  O   . PHE D 1 652 ? 48.496  14.531  101.803 1.00 21.83 ? 644  PHE D O   1 
ATOM   19074 C  CB  . PHE D 1 652 ? 48.271  13.586  99.123  1.00 17.08 ? 644  PHE D CB  1 
ATOM   19075 C  CG  . PHE D 1 652 ? 47.784  13.919  97.743  1.00 19.03 ? 644  PHE D CG  1 
ATOM   19076 C  CD1 . PHE D 1 652 ? 47.013  15.052  97.532  1.00 23.74 ? 644  PHE D CD1 1 
ATOM   19077 C  CD2 . PHE D 1 652 ? 48.105  13.116  96.659  1.00 17.46 ? 644  PHE D CD2 1 
ATOM   19078 C  CE1 . PHE D 1 652 ? 46.563  15.381  96.274  1.00 22.92 ? 644  PHE D CE1 1 
ATOM   19079 C  CE2 . PHE D 1 652 ? 47.649  13.437  95.386  1.00 21.66 ? 644  PHE D CE2 1 
ATOM   19080 C  CZ  . PHE D 1 652 ? 46.880  14.574  95.195  1.00 24.66 ? 644  PHE D CZ  1 
ATOM   19081 N  N   . GLY D 1 653 ? 50.738  14.413  101.636 1.00 27.30 ? 645  GLY D N   1 
ATOM   19082 C  CA  . GLY D 1 653 ? 50.961  14.626  103.053 1.00 20.75 ? 645  GLY D CA  1 
ATOM   19083 C  C   . GLY D 1 653 ? 50.760  13.421  103.938 1.00 21.74 ? 645  GLY D C   1 
ATOM   19084 O  O   . GLY D 1 653 ? 50.631  13.577  105.157 1.00 19.43 ? 645  GLY D O   1 
ATOM   19085 N  N   . PHE D 1 654 ? 50.725  12.216  103.375 1.00 19.89 ? 646  PHE D N   1 
ATOM   19086 C  CA  . PHE D 1 654 ? 50.668  11.006  104.196 1.00 19.73 ? 646  PHE D CA  1 
ATOM   19087 C  C   . PHE D 1 654 ? 52.094  10.572  104.508 1.00 22.84 ? 646  PHE D C   1 
ATOM   19088 O  O   . PHE D 1 654 ? 52.600  9.537   104.070 1.00 26.77 ? 646  PHE D O   1 
ATOM   19089 C  CB  . PHE D 1 654 ? 49.834  9.936   103.507 1.00 20.82 ? 646  PHE D CB  1 
ATOM   19090 C  CG  . PHE D 1 654 ? 48.415  10.363  103.322 1.00 19.64 ? 646  PHE D CG  1 
ATOM   19091 C  CD1 . PHE D 1 654 ? 47.517  10.302  104.383 1.00 18.91 ? 646  PHE D CD1 1 
ATOM   19092 C  CD2 . PHE D 1 654 ? 48.000  10.911  102.128 1.00 19.49 ? 646  PHE D CD2 1 
ATOM   19093 C  CE1 . PHE D 1 654 ? 46.214  10.749  104.236 1.00 15.98 ? 646  PHE D CE1 1 
ATOM   19094 C  CE2 . PHE D 1 654 ? 46.700  11.352  101.974 1.00 19.96 ? 646  PHE D CE2 1 
ATOM   19095 C  CZ  . PHE D 1 654 ? 45.810  11.274  103.034 1.00 22.99 ? 646  PHE D CZ  1 
ATOM   19096 N  N   . THR D 1 655 ? 52.743  11.429  105.288 1.00 22.04 ? 647  THR D N   1 
ATOM   19097 C  CA  . THR D 1 655 ? 54.132  11.286  105.678 1.00 23.16 ? 647  THR D CA  1 
ATOM   19098 C  C   . THR D 1 655 ? 54.214  11.339  107.197 1.00 26.93 ? 647  THR D C   1 
ATOM   19099 O  O   . THR D 1 655 ? 53.346  11.915  107.862 1.00 22.78 ? 647  THR D O   1 
ATOM   19100 C  CB  . THR D 1 655 ? 55.009  12.396  105.070 1.00 28.49 ? 647  THR D CB  1 
ATOM   19101 O  OG1 . THR D 1 655 ? 54.654  13.661  105.646 1.00 27.34 ? 647  THR D OG1 1 
ATOM   19102 C  CG2 . THR D 1 655 ? 54.819  12.469  103.559 1.00 24.62 ? 647  THR D CG2 1 
ATOM   19103 N  N   . VAL D 1 656 ? 55.265  10.724  107.741 1.00 26.37 ? 648  VAL D N   1 
ATOM   19104 C  CA  . VAL D 1 656 ? 55.441  10.721  109.190 1.00 26.02 ? 648  VAL D CA  1 
ATOM   19105 C  C   . VAL D 1 656 ? 55.513  12.144  109.717 1.00 27.68 ? 648  VAL D C   1 
ATOM   19106 O  O   . VAL D 1 656 ? 54.883  12.482  110.731 1.00 26.56 ? 648  VAL D O   1 
ATOM   19107 C  CB  . VAL D 1 656 ? 56.690  9.908   109.567 1.00 33.06 ? 648  VAL D CB  1 
ATOM   19108 C  CG1 . VAL D 1 656 ? 57.135  10.241  110.978 1.00 36.29 ? 648  VAL D CG1 1 
ATOM   19109 C  CG2 . VAL D 1 656 ? 56.403  8.415   109.420 1.00 32.46 ? 648  VAL D CG2 1 
ATOM   19110 N  N   . ASP D 1 657 ? 56.283  12.998  109.035 1.00 29.78 ? 649  ASP D N   1 
ATOM   19111 C  CA  . ASP D 1 657 ? 56.440  14.389  109.451 1.00 32.44 ? 649  ASP D CA  1 
ATOM   19112 C  C   . ASP D 1 657 ? 55.102  15.108  109.541 1.00 30.89 ? 649  ASP D C   1 
ATOM   19113 O  O   . ASP D 1 657 ? 54.859  15.859  110.492 1.00 31.79 ? 649  ASP D O   1 
ATOM   19114 C  CB  . ASP D 1 657 ? 57.363  15.119  108.478 1.00 35.99 ? 649  ASP D CB  1 
ATOM   19115 C  CG  . ASP D 1 657 ? 58.827  14.792  108.707 1.00 47.82 ? 649  ASP D CG  1 
ATOM   19116 O  OD1 . ASP D 1 657 ? 59.117  13.928  109.567 1.00 52.14 ? 649  ASP D OD1 1 
ATOM   19117 O  OD2 . ASP D 1 657 ? 59.684  15.402  108.030 1.00 46.69 ? 649  ASP D OD2 1 
ATOM   19118 N  N   . ASN D 1 658 ? 54.228  14.914  108.551 1.00 23.17 ? 650  ASN D N   1 
ATOM   19119 C  CA  . ASN D 1 658 ? 52.955  15.629  108.562 1.00 26.70 ? 650  ASN D CA  1 
ATOM   19120 C  C   . ASN D 1 658 ? 52.060  15.172  109.710 1.00 27.12 ? 650  ASN D C   1 
ATOM   19121 O  O   . ASN D 1 658 ? 51.394  15.999  110.350 1.00 27.92 ? 650  ASN D O   1 
ATOM   19122 C  CB  . ASN D 1 658 ? 52.230  15.446  107.232 1.00 30.49 ? 650  ASN D CB  1 
ATOM   19123 C  CG  . ASN D 1 658 ? 50.966  16.273  107.156 1.00 29.64 ? 650  ASN D CG  1 
ATOM   19124 O  OD1 . ASN D 1 658 ? 50.892  17.352  107.741 1.00 30.57 ? 650  ASN D OD1 1 
ATOM   19125 N  ND2 . ASN D 1 658 ? 49.963  15.773  106.444 1.00 25.59 ? 650  ASN D ND2 1 
ATOM   19126 N  N   . VAL D 1 659 ? 52.019  13.862  109.978 1.00 26.07 ? 651  VAL D N   1 
ATOM   19127 C  CA  . VAL D 1 659 ? 51.223  13.351  111.095 1.00 26.80 ? 651  VAL D CA  1 
ATOM   19128 C  C   . VAL D 1 659 ? 51.765  13.865  112.428 1.00 27.41 ? 651  VAL D C   1 
ATOM   19129 O  O   . VAL D 1 659 ? 50.999  14.278  113.306 1.00 26.49 ? 651  VAL D O   1 
ATOM   19130 C  CB  . VAL D 1 659 ? 51.181  11.811  111.064 1.00 21.01 ? 651  VAL D CB  1 
ATOM   19131 C  CG1 . VAL D 1 659 ? 50.425  11.268  112.289 1.00 22.53 ? 651  VAL D CG1 1 
ATOM   19132 C  CG2 . VAL D 1 659 ? 50.550  11.301  109.764 1.00 20.04 ? 651  VAL D CG2 1 
ATOM   19133 N  N   . VAL D 1 660 ? 53.088  13.841  112.604 1.00 26.88 ? 652  VAL D N   1 
ATOM   19134 C  CA  . VAL D 1 660 ? 53.697  14.347  113.836 1.00 26.35 ? 652  VAL D CA  1 
ATOM   19135 C  C   . VAL D 1 660 ? 53.336  15.814  114.047 1.00 28.60 ? 652  VAL D C   1 
ATOM   19136 O  O   . VAL D 1 660 ? 52.949  16.226  115.151 1.00 26.15 ? 652  VAL D O   1 
ATOM   19137 C  CB  . VAL D 1 660 ? 55.225  14.148  113.801 1.00 26.89 ? 652  VAL D CB  1 
ATOM   19138 C  CG1 . VAL D 1 660 ? 55.885  14.884  114.959 1.00 26.76 ? 652  VAL D CG1 1 
ATOM   19139 C  CG2 . VAL D 1 660 ? 55.588  12.673  113.824 1.00 28.30 ? 652  VAL D CG2 1 
ATOM   19140 N  N   . ASP D 1 661 ? 53.483  16.627  112.994 1.00 26.42 ? 653  ASP D N   1 
ATOM   19141 C  CA  . ASP D 1 661 ? 53.165  18.050  113.090 1.00 30.44 ? 653  ASP D CA  1 
ATOM   19142 C  C   . ASP D 1 661 ? 51.695  18.266  113.409 1.00 29.38 ? 653  ASP D C   1 
ATOM   19143 O  O   . ASP D 1 661 ? 51.343  19.166  114.182 1.00 27.22 ? 653  ASP D O   1 
ATOM   19144 C  CB  . ASP D 1 661 ? 53.517  18.766  111.782 1.00 36.67 ? 653  ASP D CB  1 
ATOM   19145 C  CG  . ASP D 1 661 ? 55.009  18.801  111.510 1.00 48.73 ? 653  ASP D CG  1 
ATOM   19146 O  OD1 . ASP D 1 661 ? 55.797  18.734  112.475 1.00 49.78 ? 653  ASP D OD1 1 
ATOM   19147 O  OD2 . ASP D 1 661 ? 55.389  18.899  110.322 1.00 53.24 ? 653  ASP D OD2 1 
ATOM   19148 N  N   . THR D 1 662 ? 50.820  17.466  112.799 1.00 27.48 ? 654  THR D N   1 
ATOM   19149 C  CA  . THR D 1 662 ? 49.392  17.599  113.059 1.00 28.96 ? 654  THR D CA  1 
ATOM   19150 C  C   . THR D 1 662 ? 49.072  17.267  114.505 1.00 24.23 ? 654  THR D C   1 
ATOM   19151 O  O   . THR D 1 662 ? 48.278  17.962  115.146 1.00 24.53 ? 654  THR D O   1 
ATOM   19152 C  CB  . THR D 1 662 ? 48.600  16.691  112.120 1.00 27.52 ? 654  THR D CB  1 
ATOM   19153 O  OG1 . THR D 1 662 ? 48.832  17.086  110.762 1.00 29.42 ? 654  THR D OG1 1 
ATOM   19154 C  CG2 . THR D 1 662 ? 47.103  16.775  112.420 1.00 21.53 ? 654  THR D CG2 1 
ATOM   19155 N  N   . VAL D 1 663 ? 49.679  16.202  115.035 1.00 23.19 ? 655  VAL D N   1 
ATOM   19156 C  CA  . VAL D 1 663 ? 49.467  15.850  116.437 1.00 28.14 ? 655  VAL D CA  1 
ATOM   19157 C  C   . VAL D 1 663 ? 49.912  16.992  117.337 1.00 29.94 ? 655  VAL D C   1 
ATOM   19158 O  O   . VAL D 1 663 ? 49.195  17.408  118.257 1.00 28.27 ? 655  VAL D O   1 
ATOM   19159 C  CB  . VAL D 1 663 ? 50.210  14.548  116.784 1.00 27.19 ? 655  VAL D CB  1 
ATOM   19160 C  CG1 . VAL D 1 663 ? 50.351  14.417  118.288 1.00 24.63 ? 655  VAL D CG1 1 
ATOM   19161 C  CG2 . VAL D 1 663 ? 49.483  13.343  116.195 1.00 28.90 ? 655  VAL D CG2 1 
ATOM   19162 N  N   . LYS D 1 664 ? 51.107  17.516  117.081 1.00 29.95 ? 656  LYS D N   1 
ATOM   19163 C  CA  . LYS D 1 664 ? 51.611  18.609  117.899 1.00 34.78 ? 656  LYS D CA  1 
ATOM   19164 C  C   . LYS D 1 664 ? 50.704  19.828  117.807 1.00 32.80 ? 656  LYS D C   1 
ATOM   19165 O  O   . LYS D 1 664 ? 50.584  20.585  118.776 1.00 33.24 ? 656  LYS D O   1 
ATOM   19166 C  CB  . LYS D 1 664 ? 53.045  18.940  117.483 1.00 35.99 ? 656  LYS D CB  1 
ATOM   19167 C  CG  . LYS D 1 664 ? 54.040  17.821  117.791 1.00 40.25 ? 656  LYS D CG  1 
ATOM   19168 C  CD  . LYS D 1 664 ? 55.268  17.902  116.906 1.00 45.11 ? 656  LYS D CD  1 
ATOM   19169 C  CE  . LYS D 1 664 ? 56.464  18.481  117.633 1.00 50.37 ? 656  LYS D CE  1 
ATOM   19170 N  NZ  . LYS D 1 664 ? 57.654  18.573  116.731 1.00 51.67 ? 656  LYS D NZ  1 
ATOM   19171 N  N   . SER D 1 665 ? 50.022  20.009  116.673 1.00 33.65 ? 657  SER D N   1 
ATOM   19172 C  CA  . SER D 1 665 ? 49.184  21.190  116.491 1.00 32.08 ? 657  SER D CA  1 
ATOM   19173 C  C   . SER D 1 665 ? 47.990  21.204  117.438 1.00 31.72 ? 657  SER D C   1 
ATOM   19174 O  O   . SER D 1 665 ? 47.462  22.279  117.734 1.00 30.73 ? 657  SER D O   1 
ATOM   19175 C  CB  . SER D 1 665 ? 48.702  21.280  115.044 1.00 26.79 ? 657  SER D CB  1 
ATOM   19176 O  OG  . SER D 1 665 ? 47.656  20.370  114.802 1.00 27.62 ? 657  SER D OG  1 
ATOM   19177 N  N   . VAL D 1 666 ? 47.546  20.042  117.926 1.00 28.58 ? 658  VAL D N   1 
ATOM   19178 C  CA  . VAL D 1 666 ? 46.391  19.992  118.820 1.00 30.34 ? 658  VAL D CA  1 
ATOM   19179 C  C   . VAL D 1 666 ? 46.808  19.901  120.285 1.00 39.18 ? 658  VAL D C   1 
ATOM   19180 O  O   . VAL D 1 666 ? 45.949  19.748  121.161 1.00 37.92 ? 658  VAL D O   1 
ATOM   19181 C  CB  . VAL D 1 666 ? 45.436  18.840  118.458 1.00 28.37 ? 658  VAL D CB  1 
ATOM   19182 C  CG1 . VAL D 1 666 ? 45.039  18.913  116.994 1.00 30.21 ? 658  VAL D CG1 1 
ATOM   19183 C  CG2 . VAL D 1 666 ? 46.058  17.494  118.795 1.00 27.96 ? 658  VAL D CG2 1 
ATOM   19184 N  N   . LEU D 1 667 ? 48.105  19.987  120.570 1.00 36.53 ? 659  LEU D N   1 
ATOM   19185 C  CA  . LEU D 1 667 ? 48.617  19.916  121.936 1.00 42.57 ? 659  LEU D CA  1 
ATOM   19186 C  C   . LEU D 1 667 ? 48.933  21.310  122.462 1.00 41.93 ? 659  LEU D C   1 
ATOM   19187 O  O   . LEU D 1 667 ? 48.996  22.265  121.686 1.00 40.63 ? 659  LEU D O   1 
ATOM   19188 C  CB  . LEU D 1 667 ? 49.865  19.035  121.993 1.00 40.57 ? 659  LEU D CB  1 
ATOM   19189 C  CG  . LEU D 1 667 ? 49.622  17.589  121.569 1.00 41.02 ? 659  LEU D CG  1 
ATOM   19190 C  CD1 . LEU D 1 667 ? 50.928  16.832  121.486 1.00 43.12 ? 659  LEU D CD1 1 
ATOM   19191 C  CD2 . LEU D 1 667 ? 48.657  16.904  122.537 1.00 39.25 ? 659  LEU D CD2 1 
HETATM 19192 C  C1  . EDO E 2 .   ? 27.562  -19.090 46.792  1.00 22.33 ? 701  EDO A C1  1 
HETATM 19193 O  O1  . EDO E 2 .   ? 27.686  -20.511 46.722  1.00 22.21 ? 701  EDO A O1  1 
HETATM 19194 C  C2  . EDO E 2 .   ? 26.245  -18.721 46.124  1.00 23.44 ? 701  EDO A C2  1 
HETATM 19195 O  O2  . EDO E 2 .   ? 26.213  -19.365 44.847  1.00 19.33 ? 701  EDO A O2  1 
HETATM 19196 CA CA  . CA  F 3 .   ? 30.472  0.552   47.192  1.00 22.19 ? 702  CA  A CA  1 
HETATM 19197 CA CA  . CA  G 3 .   ? 6.600   15.537  12.360  1.00 50.61 ? 703  CA  A CA  1 
HETATM 19198 CA CA  . CA  H 3 .   ? 5.984   8.485   14.313  1.00 31.69 ? 704  CA  A CA  1 
HETATM 19199 CA CA  . CA  I 3 .   ? -7.439  -9.166  23.407  1.00 25.41 ? 701  CA  B CA  1 
HETATM 19200 CA CA  . CA  J 3 .   ? 36.455  0.125   19.562  1.00 22.78 ? 702  CA  B CA  1 
HETATM 19201 CA CA  . CA  K 3 .   ? 33.253  1.243   23.330  1.00 30.31 ? 703  CA  B CA  1 
HETATM 19202 C  C1  . EDO L 2 .   ? 8.260   20.746  78.889  1.00 26.95 ? 701  EDO C C1  1 
HETATM 19203 O  O1  . EDO L 2 .   ? 7.545   21.965  79.132  1.00 21.90 ? 701  EDO C O1  1 
HETATM 19204 C  C2  . EDO L 2 .   ? 9.418   21.037  77.946  1.00 24.26 ? 701  EDO C C2  1 
HETATM 19205 O  O2  . EDO L 2 .   ? 8.921   21.757  76.811  1.00 23.65 ? 701  EDO C O2  1 
HETATM 19206 C  C1  . EDO M 2 .   ? 14.178  5.248   90.108  1.00 29.15 ? 702  EDO C C1  1 
HETATM 19207 O  O1  . EDO M 2 .   ? 12.803  4.879   90.205  1.00 23.18 ? 702  EDO C O1  1 
HETATM 19208 C  C2  . EDO M 2 .   ? 14.542  5.505   88.666  1.00 31.37 ? 702  EDO C C2  1 
HETATM 19209 O  O2  . EDO M 2 .   ? 13.790  6.585   88.115  1.00 20.83 ? 702  EDO C O2  1 
HETATM 19210 CA CA  . CA  N 3 .   ? 7.369   23.714  77.458  1.00 19.30 ? 703  CA  C CA  1 
HETATM 19211 CA CA  . CA  O 3 .   ? 8.927   0.828   108.729 1.00 32.77 ? 704  CA  C CA  1 
HETATM 19212 CA CA  . CA  P 3 .   ? 36.269  -8.371  74.563  1.00 47.78 ? 705  CA  C CA  1 
HETATM 19213 C  C1  . EDO Q 2 .   ? 36.266  -17.919 89.048  1.00 28.36 ? 701  EDO D C1  1 
HETATM 19214 O  O1  . EDO Q 2 .   ? 36.304  -19.352 89.103  1.00 27.23 ? 701  EDO D O1  1 
HETATM 19215 C  C2  . EDO Q 2 .   ? 37.611  -17.377 88.587  1.00 33.26 ? 701  EDO D C2  1 
HETATM 19216 O  O2  . EDO Q 2 .   ? 38.622  -17.761 89.520  1.00 27.50 ? 701  EDO D O2  1 
HETATM 19217 C  C1  . EDO R 2 .   ? 40.234  -0.829  124.806 1.00 35.56 ? 702  EDO D C1  1 
HETATM 19218 O  O1  . EDO R 2 .   ? 41.305  -1.084  125.724 1.00 44.31 ? 702  EDO D O1  1 
HETATM 19219 C  C2  . EDO R 2 .   ? 40.349  -1.790  123.632 1.00 30.85 ? 702  EDO D C2  1 
HETATM 19220 O  O2  . EDO R 2 .   ? 41.658  -1.680  123.068 1.00 30.58 ? 702  EDO D O2  1 
HETATM 19221 C  C1  . EDO S 2 .   ? -14.145 -4.436  96.810  1.00 28.23 ? 703  EDO D C1  1 
HETATM 19222 O  O1  . EDO S 2 .   ? -15.307 -3.629  96.561  1.00 20.61 ? 703  EDO D O1  1 
HETATM 19223 C  C2  . EDO S 2 .   ? -12.887 -3.614  96.549  1.00 25.73 ? 703  EDO D C2  1 
HETATM 19224 O  O2  . EDO S 2 .   ? -12.840 -2.551  97.504  1.00 22.08 ? 703  EDO D O2  1 
HETATM 19225 CA CA  . CA  T 3 .   ? 4.373   2.409   81.104  1.00 39.48 ? 704  CA  D CA  1 
HETATM 19226 CA CA  . CA  U 3 .   ? 46.449  17.337  87.967  1.00 34.93 ? 705  CA  D CA  1 
HETATM 19227 CA CA  . CA  V 3 .   ? 38.562  -20.331 89.864  1.00 25.37 ? 706  CA  D CA  1 
HETATM 19228 O  O   . HOH W 4 .   ? 31.832  -28.391 12.002  1.00 39.72 ? 801  HOH A O   1 
HETATM 19229 O  O   . HOH W 4 .   ? 22.265  -1.409  -4.510  1.00 26.88 ? 802  HOH A O   1 
HETATM 19230 O  O   . HOH W 4 .   ? 36.542  -15.508 43.029  1.00 24.28 ? 803  HOH A O   1 
HETATM 19231 O  O   . HOH W 4 .   ? 15.429  16.988  1.648   1.00 39.37 ? 804  HOH A O   1 
HETATM 19232 O  O   . HOH W 4 .   ? 22.975  -41.046 31.453  1.00 37.28 ? 805  HOH A O   1 
HETATM 19233 O  O   . HOH W 4 .   ? 12.183  -35.194 60.653  1.00 35.14 ? 806  HOH A O   1 
HETATM 19234 O  O   . HOH W 4 .   ? 9.904   19.796  -0.702  1.00 33.64 ? 807  HOH A O   1 
HETATM 19235 O  O   . HOH W 4 .   ? -22.678 -4.188  -4.488  1.00 49.13 ? 808  HOH A O   1 
HETATM 19236 O  O   . HOH W 4 .   ? 30.965  -19.955 14.172  1.00 28.67 ? 809  HOH A O   1 
HETATM 19237 O  O   . HOH W 4 .   ? 20.601  -23.486 -1.754  1.00 58.43 ? 810  HOH A O   1 
HETATM 19238 O  O   . HOH W 4 .   ? 20.378  19.744  14.008  1.00 37.03 ? 811  HOH A O   1 
HETATM 19239 O  O   . HOH W 4 .   ? -4.735  4.714   16.819  1.00 28.68 ? 812  HOH A O   1 
HETATM 19240 O  O   . HOH W 4 .   ? -10.594 -9.243  -6.791  1.00 22.76 ? 813  HOH A O   1 
HETATM 19241 O  O   . HOH W 4 .   ? 13.326  -39.992 41.956  1.00 30.34 ? 814  HOH A O   1 
HETATM 19242 O  O   . HOH W 4 .   ? 14.416  -12.952 -7.714  1.00 42.58 ? 815  HOH A O   1 
HETATM 19243 O  O   . HOH W 4 .   ? 23.393  18.397  7.199   1.00 33.54 ? 816  HOH A O   1 
HETATM 19244 O  O   . HOH W 4 .   ? 12.829  -18.719 -9.695  1.00 34.62 ? 817  HOH A O   1 
HETATM 19245 O  O   . HOH W 4 .   ? -1.419  4.736   -7.587  1.00 42.61 ? 818  HOH A O   1 
HETATM 19246 O  O   . HOH W 4 .   ? 7.256   -32.901 56.603  1.00 38.07 ? 819  HOH A O   1 
HETATM 19247 O  O   . HOH W 4 .   ? 3.195   -28.555 7.782   1.00 38.99 ? 820  HOH A O   1 
HETATM 19248 O  O   . HOH W 4 .   ? 4.850   -13.743 34.009  1.00 39.05 ? 821  HOH A O   1 
HETATM 19249 O  O   . HOH W 4 .   ? 6.867   -29.201 28.285  1.00 31.60 ? 822  HOH A O   1 
HETATM 19250 O  O   . HOH W 4 .   ? 20.802  -34.739 43.804  1.00 38.98 ? 823  HOH A O   1 
HETATM 19251 O  O   . HOH W 4 .   ? 3.590   10.108  10.496  1.00 33.12 ? 824  HOH A O   1 
HETATM 19252 O  O   . HOH W 4 .   ? 5.350   -16.669 15.019  1.00 33.31 ? 825  HOH A O   1 
HETATM 19253 O  O   . HOH W 4 .   ? 0.740   -21.578 -0.988  1.00 29.93 ? 826  HOH A O   1 
HETATM 19254 O  O   . HOH W 4 .   ? 25.711  -2.925  52.736  1.00 31.31 ? 827  HOH A O   1 
HETATM 19255 O  O   . HOH W 4 .   ? -9.328  -5.218  -8.059  1.00 28.68 ? 828  HOH A O   1 
HETATM 19256 O  O   . HOH W 4 .   ? 11.191  -32.167 6.885   1.00 29.78 ? 829  HOH A O   1 
HETATM 19257 O  O   . HOH W 4 .   ? 10.149  -3.747  47.095  1.00 42.96 ? 830  HOH A O   1 
HETATM 19258 O  O   . HOH W 4 .   ? -15.971 6.180   5.640   1.00 28.67 ? 831  HOH A O   1 
HETATM 19259 O  O   . HOH W 4 .   ? 19.476  -35.742 45.335  1.00 31.69 ? 832  HOH A O   1 
HETATM 19260 O  O   . HOH W 4 .   ? 13.469  -9.658  52.252  1.00 28.17 ? 833  HOH A O   1 
HETATM 19261 O  O   . HOH W 4 .   ? 10.652  -24.817 13.176  1.00 20.98 ? 834  HOH A O   1 
HETATM 19262 O  O   . HOH W 4 .   ? -0.556  -4.830  -5.281  1.00 30.64 ? 835  HOH A O   1 
HETATM 19263 O  O   . HOH W 4 .   ? 25.173  -16.609 39.718  1.00 12.16 ? 836  HOH A O   1 
HETATM 19264 O  O   . HOH W 4 .   ? 14.480  12.771  -5.189  1.00 31.38 ? 837  HOH A O   1 
HETATM 19265 O  O   . HOH W 4 .   ? -8.733  -14.544 4.193   1.00 34.72 ? 838  HOH A O   1 
HETATM 19266 O  O   . HOH W 4 .   ? 17.924  2.775   -8.072  1.00 25.58 ? 839  HOH A O   1 
HETATM 19267 O  O   . HOH W 4 .   ? 13.428  -45.196 35.775  1.00 19.13 ? 840  HOH A O   1 
HETATM 19268 O  O   . HOH W 4 .   ? 10.706  -17.488 11.862  1.00 21.96 ? 841  HOH A O   1 
HETATM 19269 O  O   . HOH W 4 .   ? 5.389   13.495  12.213  1.00 36.26 ? 842  HOH A O   1 
HETATM 19270 O  O   . HOH W 4 .   ? 27.771  -15.817 56.517  1.00 39.05 ? 843  HOH A O   1 
HETATM 19271 O  O   . HOH W 4 .   ? 2.171   -32.274 49.785  1.00 31.57 ? 844  HOH A O   1 
HETATM 19272 O  O   . HOH W 4 .   ? 5.917   -34.466 48.625  1.00 30.71 ? 845  HOH A O   1 
HETATM 19273 O  O   . HOH W 4 .   ? 16.826  -0.969  -1.912  1.00 19.76 ? 846  HOH A O   1 
HETATM 19274 O  O   . HOH W 4 .   ? 15.228  -23.108 65.301  1.00 40.01 ? 847  HOH A O   1 
HETATM 19275 O  O   . HOH W 4 .   ? 24.186  13.053  -1.313  1.00 35.85 ? 848  HOH A O   1 
HETATM 19276 O  O   . HOH W 4 .   ? -5.502  -5.879  15.250  1.00 20.49 ? 849  HOH A O   1 
HETATM 19277 O  O   . HOH W 4 .   ? -0.578  -33.358 35.598  1.00 46.41 ? 850  HOH A O   1 
HETATM 19278 O  O   . HOH W 4 .   ? 5.994   -26.040 51.729  1.00 21.41 ? 851  HOH A O   1 
HETATM 19279 O  O   . HOH W 4 .   ? 6.928   -6.043  -4.195  1.00 18.46 ? 852  HOH A O   1 
HETATM 19280 O  O   . HOH W 4 .   ? -17.474 -8.582  13.246  1.00 46.56 ? 853  HOH A O   1 
HETATM 19281 O  O   . HOH W 4 .   ? 13.554  -40.782 30.675  1.00 38.26 ? 854  HOH A O   1 
HETATM 19282 O  O   . HOH W 4 .   ? 17.637  -35.453 58.143  1.00 30.65 ? 855  HOH A O   1 
HETATM 19283 O  O   . HOH W 4 .   ? 11.132  -35.263 40.766  1.00 17.93 ? 856  HOH A O   1 
HETATM 19284 O  O   . HOH W 4 .   ? 33.318  -6.426  30.920  1.00 31.99 ? 857  HOH A O   1 
HETATM 19285 O  O   . HOH W 4 .   ? 1.940   17.262  -1.805  1.00 37.31 ? 858  HOH A O   1 
HETATM 19286 O  O   . HOH W 4 .   ? 4.272   -11.665 10.344  1.00 20.54 ? 859  HOH A O   1 
HETATM 19287 O  O   . HOH W 4 .   ? -7.475  -14.637 -3.444  1.00 22.90 ? 860  HOH A O   1 
HETATM 19288 O  O   . HOH W 4 .   ? 10.219  -19.702 24.343  1.00 14.93 ? 861  HOH A O   1 
HETATM 19289 O  O   . HOH W 4 .   ? 26.421  -28.626 47.610  1.00 30.81 ? 862  HOH A O   1 
HETATM 19290 O  O   . HOH W 4 .   ? 16.097  -33.355 -1.591  1.00 27.82 ? 863  HOH A O   1 
HETATM 19291 O  O   . HOH W 4 .   ? 2.661   -21.318 42.361  1.00 26.81 ? 864  HOH A O   1 
HETATM 19292 O  O   . HOH W 4 .   ? 27.923  -15.051 5.554   1.00 30.35 ? 865  HOH A O   1 
HETATM 19293 O  O   . HOH W 4 .   ? 12.327  -35.450 29.674  1.00 41.42 ? 866  HOH A O   1 
HETATM 19294 O  O   . HOH W 4 .   ? 21.084  -23.296 11.909  1.00 21.06 ? 867  HOH A O   1 
HETATM 19295 O  O   . HOH W 4 .   ? 25.650  -6.431  24.942  1.00 11.86 ? 868  HOH A O   1 
HETATM 19296 O  O   . HOH W 4 .   ? -0.405  -11.622 6.615   1.00 28.44 ? 869  HOH A O   1 
HETATM 19297 O  O   . HOH W 4 .   ? 12.607  -32.572 32.172  1.00 19.90 ? 870  HOH A O   1 
HETATM 19298 O  O   . HOH W 4 .   ? 16.256  -2.005  37.397  1.00 14.07 ? 871  HOH A O   1 
HETATM 19299 O  O   . HOH W 4 .   ? 15.205  -9.488  2.482   1.00 15.51 ? 872  HOH A O   1 
HETATM 19300 O  O   . HOH W 4 .   ? -21.572 5.848   -6.307  1.00 25.68 ? 873  HOH A O   1 
HETATM 19301 O  O   . HOH W 4 .   ? 23.876  -1.035  2.662   1.00 15.52 ? 874  HOH A O   1 
HETATM 19302 O  O   . HOH W 4 .   ? 8.218   -26.336 30.478  1.00 25.28 ? 875  HOH A O   1 
HETATM 19303 O  O   . HOH W 4 .   ? -1.089  -11.175 3.304   1.00 19.42 ? 876  HOH A O   1 
HETATM 19304 O  O   . HOH W 4 .   ? 8.850   -36.420 30.917  1.00 39.30 ? 877  HOH A O   1 
HETATM 19305 O  O   . HOH W 4 .   ? 6.061   -1.382  18.458  1.00 20.38 ? 878  HOH A O   1 
HETATM 19306 O  O   . HOH W 4 .   ? 25.276  -19.330 25.367  1.00 17.20 ? 879  HOH A O   1 
HETATM 19307 O  O   . HOH W 4 .   ? 20.942  -28.778 11.878  1.00 31.96 ? 880  HOH A O   1 
HETATM 19308 O  O   . HOH W 4 .   ? -12.967 -7.050  3.266   1.00 22.89 ? 881  HOH A O   1 
HETATM 19309 O  O   . HOH W 4 .   ? 7.819   -35.057 34.329  1.00 33.45 ? 882  HOH A O   1 
HETATM 19310 O  O   . HOH W 4 .   ? -5.680  -4.106  -4.430  1.00 23.76 ? 883  HOH A O   1 
HETATM 19311 O  O   . HOH W 4 .   ? -0.595  -13.008 18.789  1.00 24.79 ? 884  HOH A O   1 
HETATM 19312 O  O   . HOH W 4 .   ? 9.038   17.523  -3.805  1.00 38.08 ? 885  HOH A O   1 
HETATM 19313 O  O   . HOH W 4 .   ? 8.437   -31.182 26.828  1.00 42.02 ? 886  HOH A O   1 
HETATM 19314 O  O   . HOH W 4 .   ? 8.776   -27.279 60.910  1.00 26.87 ? 887  HOH A O   1 
HETATM 19315 O  O   . HOH W 4 .   ? 0.966   14.754  6.624   1.00 34.33 ? 888  HOH A O   1 
HETATM 19316 O  O   . HOH W 4 .   ? 4.898   15.988  -7.834  1.00 29.37 ? 889  HOH A O   1 
HETATM 19317 O  O   . HOH W 4 .   ? 11.977  -18.423 36.951  1.00 20.59 ? 890  HOH A O   1 
HETATM 19318 O  O   . HOH W 4 .   ? -12.855 -5.174  -1.993  1.00 30.95 ? 891  HOH A O   1 
HETATM 19319 O  O   . HOH W 4 .   ? -3.532  -4.493  -2.812  1.00 19.11 ? 892  HOH A O   1 
HETATM 19320 O  O   . HOH W 4 .   ? 33.796  -14.687 38.209  1.00 45.20 ? 893  HOH A O   1 
HETATM 19321 O  O   . HOH W 4 .   ? 6.777   -4.251  17.722  1.00 16.08 ? 894  HOH A O   1 
HETATM 19322 O  O   . HOH W 4 .   ? 12.304  -44.572 30.953  1.00 21.59 ? 895  HOH A O   1 
HETATM 19323 O  O   . HOH W 4 .   ? 18.165  9.019   -4.885  1.00 33.07 ? 896  HOH A O   1 
HETATM 19324 O  O   . HOH W 4 .   ? -5.136  11.188  -4.157  1.00 31.40 ? 897  HOH A O   1 
HETATM 19325 O  O   . HOH W 4 .   ? 26.349  -2.812  25.874  1.00 20.10 ? 898  HOH A O   1 
HETATM 19326 O  O   . HOH W 4 .   ? 7.313   -9.661  -4.175  1.00 23.34 ? 899  HOH A O   1 
HETATM 19327 O  O   . HOH W 4 .   ? 7.396   -15.636 34.838  1.00 24.03 ? 900  HOH A O   1 
HETATM 19328 O  O   . HOH W 4 .   ? 22.051  -20.367 35.491  1.00 13.59 ? 901  HOH A O   1 
HETATM 19329 O  O   . HOH W 4 .   ? 22.189  -8.711  1.970   1.00 25.55 ? 902  HOH A O   1 
HETATM 19330 O  O   . HOH W 4 .   ? 21.160  -20.083 -2.352  1.00 43.01 ? 903  HOH A O   1 
HETATM 19331 O  O   . HOH W 4 .   ? 21.207  -18.671 5.256   1.00 22.14 ? 904  HOH A O   1 
HETATM 19332 O  O   . HOH W 4 .   ? 30.399  -1.519  37.817  1.00 11.60 ? 905  HOH A O   1 
HETATM 19333 O  O   . HOH W 4 .   ? -7.189  -7.834  21.362  1.00 33.24 ? 906  HOH A O   1 
HETATM 19334 O  O   . HOH W 4 .   ? 20.239  -0.963  22.984  1.00 8.89  ? 907  HOH A O   1 
HETATM 19335 O  O   . HOH W 4 .   ? 1.292   -3.308  13.132  1.00 18.17 ? 908  HOH A O   1 
HETATM 19336 O  O   . HOH W 4 .   ? -0.161  -33.624 45.990  1.00 26.21 ? 909  HOH A O   1 
HETATM 19337 O  O   . HOH W 4 .   ? -3.621  -2.881  20.518  1.00 19.17 ? 910  HOH A O   1 
HETATM 19338 O  O   . HOH W 4 .   ? 2.471   -0.340  -12.222 1.00 36.21 ? 911  HOH A O   1 
HETATM 19339 O  O   . HOH W 4 .   ? 13.684  -15.378 59.558  1.00 38.14 ? 912  HOH A O   1 
HETATM 19340 O  O   . HOH W 4 .   ? 3.971   -17.794 6.100   1.00 24.41 ? 913  HOH A O   1 
HETATM 19341 O  O   . HOH W 4 .   ? 7.150   0.985   16.133  1.00 17.34 ? 914  HOH A O   1 
HETATM 19342 O  O   . HOH W 4 .   ? -17.878 8.406   12.155  1.00 26.90 ? 915  HOH A O   1 
HETATM 19343 O  O   . HOH W 4 .   ? -0.055  -5.907  6.574   1.00 21.85 ? 916  HOH A O   1 
HETATM 19344 O  O   . HOH W 4 .   ? 18.859  -11.309 25.080  1.00 12.07 ? 917  HOH A O   1 
HETATM 19345 O  O   . HOH W 4 .   ? -0.317  -9.196  19.483  1.00 20.45 ? 918  HOH A O   1 
HETATM 19346 O  O   . HOH W 4 .   ? -1.880  -11.421 12.400  1.00 23.02 ? 919  HOH A O   1 
HETATM 19347 O  O   . HOH W 4 .   ? 7.980   -25.808 26.135  1.00 20.26 ? 920  HOH A O   1 
HETATM 19348 O  O   . HOH W 4 .   ? 0.327   9.976   1.299   1.00 15.72 ? 921  HOH A O   1 
HETATM 19349 O  O   . HOH W 4 .   ? 11.756  -37.891 53.393  1.00 37.40 ? 922  HOH A O   1 
HETATM 19350 O  O   A HOH W 4 .   ? 19.938  -13.533 38.455  0.51 10.81 ? 923  HOH A O   1 
HETATM 19351 O  O   B HOH W 4 .   ? 20.190  -12.603 39.952  0.49 16.87 ? 923  HOH A O   1 
HETATM 19352 O  O   . HOH W 4 .   ? 16.839  -12.026 -0.856  1.00 30.76 ? 924  HOH A O   1 
HETATM 19353 O  O   . HOH W 4 .   ? 18.758  -7.623  -2.377  1.00 34.45 ? 925  HOH A O   1 
HETATM 19354 O  O   . HOH W 4 .   ? 14.285  16.964  10.419  1.00 44.17 ? 926  HOH A O   1 
HETATM 19355 O  O   . HOH W 4 .   ? 26.424  -24.043 9.310   1.00 36.09 ? 927  HOH A O   1 
HETATM 19356 O  O   . HOH W 4 .   ? 17.459  6.770   -6.567  1.00 21.65 ? 928  HOH A O   1 
HETATM 19357 O  O   . HOH W 4 .   ? 19.553  -14.057 16.405  1.00 12.53 ? 929  HOH A O   1 
HETATM 19358 O  O   . HOH W 4 .   ? 27.005  -28.308 35.711  1.00 23.79 ? 930  HOH A O   1 
HETATM 19359 O  O   . HOH W 4 .   ? 12.511  -11.686 43.998  1.00 14.60 ? 931  HOH A O   1 
HETATM 19360 O  O   . HOH W 4 .   ? 26.217  -10.973 11.273  1.00 21.77 ? 932  HOH A O   1 
HETATM 19361 O  O   . HOH W 4 .   ? 8.630   -13.819 55.640  1.00 40.55 ? 933  HOH A O   1 
HETATM 19362 O  O   . HOH W 4 .   ? 20.637  19.230  11.462  1.00 40.25 ? 934  HOH A O   1 
HETATM 19363 O  O   . HOH W 4 .   ? -1.369  -9.233  -4.701  1.00 20.88 ? 935  HOH A O   1 
HETATM 19364 O  O   . HOH W 4 .   ? -10.294 -3.076  20.479  1.00 23.28 ? 936  HOH A O   1 
HETATM 19365 O  O   . HOH W 4 .   ? 15.588  -13.937 -3.392  1.00 26.52 ? 937  HOH A O   1 
HETATM 19366 O  O   . HOH W 4 .   ? -3.477  -3.868  -8.081  1.00 37.96 ? 938  HOH A O   1 
HETATM 19367 O  O   . HOH W 4 .   ? 6.802   -16.437 38.248  1.00 23.08 ? 939  HOH A O   1 
HETATM 19368 O  O   . HOH W 4 .   ? 10.135  -21.988 28.151  1.00 16.74 ? 940  HOH A O   1 
HETATM 19369 O  O   . HOH W 4 .   ? 12.804  15.133  8.414   1.00 27.36 ? 941  HOH A O   1 
HETATM 19370 O  O   . HOH W 4 .   ? 26.706  0.019   10.834  1.00 12.56 ? 942  HOH A O   1 
HETATM 19371 O  O   . HOH W 4 .   ? 18.106  1.916   21.673  1.00 13.16 ? 943  HOH A O   1 
HETATM 19372 O  O   . HOH W 4 .   ? 24.807  -34.636 57.283  1.00 41.92 ? 944  HOH A O   1 
HETATM 19373 O  O   . HOH W 4 .   ? 25.743  -28.879 16.425  1.00 23.96 ? 945  HOH A O   1 
HETATM 19374 O  O   . HOH W 4 .   ? -17.422 -4.119  22.708  1.00 27.58 ? 946  HOH A O   1 
HETATM 19375 O  O   . HOH W 4 .   ? 23.507  -10.781 42.367  1.00 12.22 ? 947  HOH A O   1 
HETATM 19376 O  O   . HOH W 4 .   ? 29.593  -13.080 55.743  1.00 39.98 ? 948  HOH A O   1 
HETATM 19377 O  O   . HOH W 4 .   ? 15.980  -4.580  -4.224  1.00 18.54 ? 949  HOH A O   1 
HETATM 19378 O  O   . HOH W 4 .   ? -6.642  -5.186  22.682  1.00 15.50 ? 950  HOH A O   1 
HETATM 19379 O  O   . HOH W 4 .   ? 5.723   -35.519 37.465  1.00 19.45 ? 951  HOH A O   1 
HETATM 19380 O  O   . HOH W 4 .   ? 6.097   11.664  10.717  1.00 19.13 ? 952  HOH A O   1 
HETATM 19381 O  O   . HOH W 4 .   ? 15.934  -12.499 42.725  1.00 12.28 ? 953  HOH A O   1 
HETATM 19382 O  O   . HOH W 4 .   ? 32.185  -26.297 11.255  1.00 39.97 ? 954  HOH A O   1 
HETATM 19383 O  O   . HOH W 4 .   ? 14.207  -19.809 38.508  1.00 16.15 ? 955  HOH A O   1 
HETATM 19384 O  O   . HOH W 4 .   ? 16.241  -11.968 -4.789  1.00 42.06 ? 956  HOH A O   1 
HETATM 19385 O  O   . HOH W 4 .   ? 32.084  -17.517 48.492  1.00 20.73 ? 957  HOH A O   1 
HETATM 19386 O  O   . HOH W 4 .   ? 2.179   -7.880  4.937   1.00 20.21 ? 958  HOH A O   1 
HETATM 19387 O  O   . HOH W 4 .   ? 26.702  -26.076 34.329  1.00 23.88 ? 959  HOH A O   1 
HETATM 19388 O  O   . HOH W 4 .   ? -7.257  -15.461 -9.696  1.00 31.20 ? 960  HOH A O   1 
HETATM 19389 O  O   . HOH W 4 .   ? 21.386  -25.631 13.157  1.00 34.83 ? 961  HOH A O   1 
HETATM 19390 O  O   . HOH W 4 .   ? 12.930  -1.366  -10.183 1.00 19.03 ? 962  HOH A O   1 
HETATM 19391 O  O   . HOH W 4 .   ? 26.367  -29.856 44.912  1.00 37.50 ? 963  HOH A O   1 
HETATM 19392 O  O   . HOH W 4 .   ? 39.494  -13.041 40.381  1.00 26.68 ? 964  HOH A O   1 
HETATM 19393 O  O   . HOH W 4 .   ? 27.217  -32.655 32.201  1.00 26.76 ? 965  HOH A O   1 
HETATM 19394 O  O   . HOH W 4 .   ? 10.071  10.208  -7.525  1.00 36.61 ? 966  HOH A O   1 
HETATM 19395 O  O   . HOH W 4 .   ? 20.233  -14.042 0.392   1.00 24.41 ? 967  HOH A O   1 
HETATM 19396 O  O   . HOH W 4 .   ? -15.417 2.714   17.409  1.00 19.23 ? 968  HOH A O   1 
HETATM 19397 O  O   . HOH W 4 .   ? 5.251   -20.676 16.991  1.00 20.99 ? 969  HOH A O   1 
HETATM 19398 O  O   . HOH W 4 .   ? 22.088  -12.914 51.807  1.00 16.41 ? 970  HOH A O   1 
HETATM 19399 O  O   . HOH W 4 .   ? 25.258  -21.887 61.350  1.00 34.47 ? 971  HOH A O   1 
HETATM 19400 O  O   . HOH W 4 .   ? 1.318   -8.775  2.604   1.00 29.27 ? 972  HOH A O   1 
HETATM 19401 O  O   . HOH W 4 .   ? 22.558  -32.667 51.127  1.00 32.38 ? 973  HOH A O   1 
HETATM 19402 O  O   . HOH W 4 .   ? 0.774   12.351  8.058   1.00 32.26 ? 974  HOH A O   1 
HETATM 19403 O  O   . HOH W 4 .   ? 7.669   -36.701 40.779  1.00 35.77 ? 975  HOH A O   1 
HETATM 19404 O  O   . HOH W 4 .   ? 31.717  -21.381 41.447  1.00 33.81 ? 976  HOH A O   1 
HETATM 19405 O  O   . HOH W 4 .   ? 21.429  -34.890 36.832  1.00 28.16 ? 977  HOH A O   1 
HETATM 19406 O  O   . HOH W 4 .   ? 16.320  -10.766 40.746  1.00 12.40 ? 978  HOH A O   1 
HETATM 19407 O  O   . HOH W 4 .   ? 30.266  -18.081 50.362  1.00 31.30 ? 979  HOH A O   1 
HETATM 19408 O  O   . HOH W 4 .   ? -18.638 -8.355  10.910  1.00 36.70 ? 980  HOH A O   1 
HETATM 19409 O  O   . HOH W 4 .   ? 6.376   17.807  4.416   1.00 31.16 ? 981  HOH A O   1 
HETATM 19410 O  O   . HOH W 4 .   ? -14.929 -6.091  15.611  1.00 26.19 ? 982  HOH A O   1 
HETATM 19411 O  O   . HOH W 4 .   ? 24.156  -26.599 40.773  1.00 26.00 ? 983  HOH A O   1 
HETATM 19412 O  O   . HOH W 4 .   ? 1.583   -19.149 26.362  1.00 30.49 ? 984  HOH A O   1 
HETATM 19413 O  O   . HOH W 4 .   ? 22.835  -9.931  50.707  1.00 16.79 ? 985  HOH A O   1 
HETATM 19414 O  O   . HOH W 4 .   ? 7.968   -32.769 17.690  1.00 30.62 ? 986  HOH A O   1 
HETATM 19415 O  O   . HOH W 4 .   ? 0.410   -9.636  -6.668  1.00 25.35 ? 987  HOH A O   1 
HETATM 19416 O  O   . HOH W 4 .   ? 32.170  -9.792  33.560  1.00 27.27 ? 988  HOH A O   1 
HETATM 19417 O  O   . HOH W 4 .   ? 5.154   -12.489 -3.558  1.00 20.72 ? 989  HOH A O   1 
HETATM 19418 O  O   . HOH W 4 .   ? 23.205  -15.873 59.687  1.00 47.08 ? 990  HOH A O   1 
HETATM 19419 O  O   . HOH W 4 .   ? 17.391  -24.285 39.419  1.00 14.56 ? 991  HOH A O   1 
HETATM 19420 O  O   . HOH W 4 .   ? 13.968  -32.041 10.235  1.00 37.79 ? 992  HOH A O   1 
HETATM 19421 O  O   . HOH W 4 .   ? 24.906  -8.792  33.770  1.00 7.42  ? 993  HOH A O   1 
HETATM 19422 O  O   . HOH W 4 .   ? -2.177  8.037   14.043  1.00 40.45 ? 994  HOH A O   1 
HETATM 19423 O  O   . HOH W 4 .   ? 1.315   -5.499  8.950   1.00 17.97 ? 995  HOH A O   1 
HETATM 19424 O  O   . HOH W 4 .   ? -16.740 -6.108  17.512  1.00 37.63 ? 996  HOH A O   1 
HETATM 19425 O  O   . HOH W 4 .   ? 26.014  -22.616 45.515  1.00 21.66 ? 997  HOH A O   1 
HETATM 19426 O  O   . HOH W 4 .   ? 1.534   -21.756 7.686   1.00 33.97 ? 998  HOH A O   1 
HETATM 19427 O  O   . HOH W 4 .   ? 35.807  -7.960  32.805  1.00 32.30 ? 999  HOH A O   1 
HETATM 19428 O  O   . HOH W 4 .   ? -9.528  -6.316  20.805  1.00 34.85 ? 1000 HOH A O   1 
HETATM 19429 O  O   . HOH W 4 .   ? 14.869  -4.800  34.814  1.00 19.40 ? 1001 HOH A O   1 
HETATM 19430 O  O   . HOH W 4 .   ? 12.556  -8.893  2.295   1.00 15.78 ? 1002 HOH A O   1 
HETATM 19431 O  O   . HOH W 4 .   ? 24.488  -4.224  41.105  1.00 6.92  ? 1003 HOH A O   1 
HETATM 19432 O  O   . HOH W 4 .   ? -1.380  11.324  -6.816  1.00 32.37 ? 1004 HOH A O   1 
HETATM 19433 O  O   . HOH W 4 .   ? -8.470  -12.725 6.007   1.00 26.82 ? 1005 HOH A O   1 
HETATM 19434 O  O   . HOH W 4 .   ? 13.022  -1.261  25.888  1.00 16.69 ? 1006 HOH A O   1 
HETATM 19435 O  O   . HOH W 4 .   ? -15.096 3.410   14.490  1.00 21.78 ? 1007 HOH A O   1 
HETATM 19436 O  O   . HOH W 4 .   ? 29.083  -4.017  4.731   1.00 40.94 ? 1008 HOH A O   1 
HETATM 19437 O  O   . HOH W 4 .   ? 10.746  -22.323 12.009  1.00 24.97 ? 1009 HOH A O   1 
HETATM 19438 O  O   . HOH W 4 .   ? 5.951   -28.536 16.281  1.00 39.01 ? 1010 HOH A O   1 
HETATM 19439 O  O   . HOH W 4 .   ? 31.643  -28.632 28.788  1.00 30.21 ? 1011 HOH A O   1 
HETATM 19440 O  O   . HOH W 4 .   ? 27.181  -15.033 37.238  1.00 13.68 ? 1012 HOH A O   1 
HETATM 19441 O  O   . HOH W 4 .   ? 5.610   -27.532 20.569  1.00 41.89 ? 1013 HOH A O   1 
HETATM 19442 O  O   . HOH W 4 .   ? 33.982  -2.797  46.232  1.00 16.11 ? 1014 HOH A O   1 
HETATM 19443 O  O   . HOH W 4 .   ? 33.784  -9.246  36.175  1.00 13.73 ? 1015 HOH A O   1 
HETATM 19444 O  O   . HOH W 4 .   ? 0.899   -17.893 40.142  1.00 39.81 ? 1016 HOH A O   1 
HETATM 19445 O  O   . HOH W 4 .   ? 10.263  -37.653 19.556  1.00 35.42 ? 1017 HOH A O   1 
HETATM 19446 O  O   . HOH W 4 .   ? 27.996  -19.751 42.732  1.00 19.60 ? 1018 HOH A O   1 
HETATM 19447 O  O   . HOH W 4 .   ? 17.148  11.188  18.125  1.00 10.75 ? 1019 HOH A O   1 
HETATM 19448 O  O   . HOH W 4 .   ? 23.724  -6.903  -0.051  1.00 30.95 ? 1020 HOH A O   1 
HETATM 19449 O  O   . HOH W 4 .   ? -6.695  9.225   21.425  1.00 40.29 ? 1021 HOH A O   1 
HETATM 19450 O  O   . HOH W 4 .   ? 18.499  -31.733 56.403  1.00 20.51 ? 1022 HOH A O   1 
HETATM 19451 O  O   . HOH W 4 .   ? 22.699  -19.228 38.111  1.00 12.90 ? 1023 HOH A O   1 
HETATM 19452 O  O   . HOH W 4 .   ? -10.161 -5.171  23.215  1.00 14.72 ? 1024 HOH A O   1 
HETATM 19453 O  O   . HOH W 4 .   ? 0.082   -12.695 9.525   1.00 28.29 ? 1025 HOH A O   1 
HETATM 19454 O  O   . HOH W 4 .   ? 23.351  -0.842  35.555  1.00 22.16 ? 1026 HOH A O   1 
HETATM 19455 O  O   . HOH W 4 .   ? 6.754   -20.632 54.458  1.00 22.23 ? 1027 HOH A O   1 
HETATM 19456 O  O   . HOH W 4 .   ? 8.253   14.272  -6.087  1.00 22.48 ? 1028 HOH A O   1 
HETATM 19457 O  O   . HOH W 4 .   ? -14.012 -0.813  -10.317 1.00 35.13 ? 1029 HOH A O   1 
HETATM 19458 O  O   . HOH W 4 .   ? 15.982  -31.919 11.875  1.00 34.62 ? 1030 HOH A O   1 
HETATM 19459 O  O   . HOH W 4 .   ? 31.915  -21.864 13.292  1.00 38.62 ? 1031 HOH A O   1 
HETATM 19460 O  O   . HOH W 4 .   ? 23.004  -13.255 1.174   1.00 24.64 ? 1032 HOH A O   1 
HETATM 19461 O  O   . HOH W 4 .   ? -9.487  -10.609 10.832  1.00 28.25 ? 1033 HOH A O   1 
HETATM 19462 O  O   . HOH W 4 .   ? 9.586   -11.679 40.746  1.00 14.22 ? 1034 HOH A O   1 
HETATM 19463 O  O   . HOH W 4 .   ? 13.879  -9.941  -6.423  1.00 40.21 ? 1035 HOH A O   1 
HETATM 19464 O  O   . HOH W 4 .   ? 27.283  -30.156 23.568  1.00 35.15 ? 1036 HOH A O   1 
HETATM 19465 O  O   . HOH W 4 .   ? 20.639  -13.147 54.403  1.00 32.79 ? 1037 HOH A O   1 
HETATM 19466 O  O   . HOH W 4 .   ? 2.463   -17.664 11.411  1.00 28.30 ? 1038 HOH A O   1 
HETATM 19467 O  O   . HOH W 4 .   ? 26.327  -8.276  11.436  1.00 16.15 ? 1039 HOH A O   1 
HETATM 19468 O  O   . HOH W 4 .   ? 3.819   -27.396 60.218  1.00 47.19 ? 1040 HOH A O   1 
HETATM 19469 O  O   . HOH W 4 .   ? -15.927 -0.811  24.139  1.00 19.18 ? 1041 HOH A O   1 
HETATM 19470 O  O   . HOH W 4 .   ? 15.085  -6.341  32.524  1.00 15.77 ? 1042 HOH A O   1 
HETATM 19471 O  O   . HOH W 4 .   ? 23.908  -28.976 28.683  1.00 22.70 ? 1043 HOH A O   1 
HETATM 19472 O  O   . HOH W 4 .   ? 30.921  -12.358 2.921   1.00 35.24 ? 1044 HOH A O   1 
HETATM 19473 O  O   . HOH W 4 .   ? 24.429  -26.024 13.077  1.00 23.07 ? 1045 HOH A O   1 
HETATM 19474 O  O   . HOH W 4 .   ? 9.008   -17.826 0.229   1.00 22.33 ? 1046 HOH A O   1 
HETATM 19475 O  O   . HOH W 4 .   ? 35.466  -13.038 39.990  1.00 17.50 ? 1047 HOH A O   1 
HETATM 19476 O  O   . HOH W 4 .   ? 5.794   -25.653 29.918  1.00 35.15 ? 1048 HOH A O   1 
HETATM 19477 O  O   . HOH W 4 .   ? 24.838  5.170   0.961   1.00 37.23 ? 1049 HOH A O   1 
HETATM 19478 O  O   . HOH W 4 .   ? 21.954  -24.369 1.566   1.00 41.33 ? 1050 HOH A O   1 
HETATM 19479 O  O   . HOH W 4 .   ? -0.649  -13.146 1.578   1.00 18.33 ? 1051 HOH A O   1 
HETATM 19480 O  O   . HOH W 4 .   ? 11.441  14.878  -6.161  1.00 31.86 ? 1052 HOH A O   1 
HETATM 19481 O  O   . HOH W 4 .   ? -19.146 0.182   2.800   1.00 27.31 ? 1053 HOH A O   1 
HETATM 19482 O  O   . HOH W 4 .   ? -2.389  -12.871 9.490   1.00 27.64 ? 1054 HOH A O   1 
HETATM 19483 O  O   . HOH W 4 .   ? 20.087  -20.509 7.655   1.00 35.86 ? 1055 HOH A O   1 
HETATM 19484 O  O   . HOH W 4 .   ? 16.097  -27.366 7.013   1.00 24.21 ? 1056 HOH A O   1 
HETATM 19485 O  O   . HOH W 4 .   ? 20.373  -24.535 8.258   1.00 41.02 ? 1057 HOH A O   1 
HETATM 19486 O  O   . HOH W 4 .   ? 16.326  -37.003 46.868  1.00 34.49 ? 1058 HOH A O   1 
HETATM 19487 O  O   . HOH W 4 .   ? 13.342  -33.153 4.828   1.00 38.21 ? 1059 HOH A O   1 
HETATM 19488 O  O   . HOH W 4 .   ? 11.506  -21.029 20.506  1.00 13.00 ? 1060 HOH A O   1 
HETATM 19489 O  O   . HOH W 4 .   ? 11.477  -13.322 41.853  1.00 12.50 ? 1061 HOH A O   1 
HETATM 19490 O  O   . HOH W 4 .   ? 2.205   4.857   18.694  1.00 42.21 ? 1062 HOH A O   1 
HETATM 19491 O  O   . HOH W 4 .   ? 6.773   -11.561 58.985  1.00 42.63 ? 1063 HOH A O   1 
HETATM 19492 O  O   . HOH W 4 .   ? 10.927  -19.777 16.704  1.00 23.46 ? 1064 HOH A O   1 
HETATM 19493 O  O   . HOH W 4 .   ? 13.476  14.136  4.628   1.00 22.08 ? 1065 HOH A O   1 
HETATM 19494 O  O   . HOH W 4 .   ? 16.239  1.012   25.678  1.00 16.46 ? 1066 HOH A O   1 
HETATM 19495 O  O   . HOH W 4 .   ? 26.371  1.313   8.341   1.00 28.32 ? 1067 HOH A O   1 
HETATM 19496 O  O   . HOH W 4 .   ? 8.913   -8.203  -6.351  1.00 32.59 ? 1068 HOH A O   1 
HETATM 19497 O  O   . HOH W 4 .   ? 2.209   -23.432 53.819  1.00 38.52 ? 1069 HOH A O   1 
HETATM 19498 O  O   . HOH W 4 .   ? 27.874  -31.759 29.997  1.00 31.96 ? 1070 HOH A O   1 
HETATM 19499 O  O   . HOH W 4 .   ? 0.186   -30.184 51.038  1.00 27.98 ? 1071 HOH A O   1 
HETATM 19500 O  O   . HOH W 4 .   ? 5.855   -28.917 31.786  1.00 39.16 ? 1072 HOH A O   1 
HETATM 19501 O  O   . HOH W 4 .   ? 3.221   -18.522 35.208  1.00 39.78 ? 1073 HOH A O   1 
HETATM 19502 O  O   . HOH W 4 .   ? -12.660 -6.821  -8.428  1.00 40.10 ? 1074 HOH A O   1 
HETATM 19503 O  O   . HOH W 4 .   ? 14.613  3.505   21.328  1.00 9.51  ? 1075 HOH A O   1 
HETATM 19504 O  O   . HOH W 4 .   ? 0.185   -29.863 35.279  1.00 24.99 ? 1076 HOH A O   1 
HETATM 19505 O  O   . HOH W 4 .   ? 1.582   -15.184 32.253  1.00 23.97 ? 1077 HOH A O   1 
HETATM 19506 O  O   . HOH W 4 .   ? 17.245  -43.223 37.848  1.00 32.19 ? 1078 HOH A O   1 
HETATM 19507 O  O   . HOH W 4 .   ? -17.219 6.866   3.417   1.00 26.68 ? 1079 HOH A O   1 
HETATM 19508 O  O   . HOH W 4 .   ? 9.867   -33.843 42.726  1.00 18.26 ? 1080 HOH A O   1 
HETATM 19509 O  O   . HOH W 4 .   ? 9.561   -35.244 54.072  1.00 40.87 ? 1081 HOH A O   1 
HETATM 19510 O  O   . HOH W 4 .   ? -1.366  -11.528 24.211  1.00 30.82 ? 1082 HOH A O   1 
HETATM 19511 O  O   . HOH W 4 .   ? 21.300  7.382   -1.993  1.00 23.38 ? 1083 HOH A O   1 
HETATM 19512 O  O   . HOH W 4 .   ? -21.795 0.415   15.638  1.00 49.21 ? 1084 HOH A O   1 
HETATM 19513 O  O   . HOH W 4 .   ? -5.474  5.182   13.425  1.00 20.17 ? 1085 HOH A O   1 
HETATM 19514 O  O   . HOH W 4 .   ? 10.929  -15.684 -7.356  1.00 44.42 ? 1086 HOH A O   1 
HETATM 19515 O  O   A HOH W 4 .   ? -19.346 0.306   18.610  0.53 20.13 ? 1087 HOH A O   1 
HETATM 19516 O  O   B HOH W 4 .   ? -19.735 -1.314  19.019  0.47 17.75 ? 1087 HOH A O   1 
HETATM 19517 O  O   . HOH W 4 .   ? 10.201  -10.406 4.801   1.00 13.76 ? 1088 HOH A O   1 
HETATM 19518 O  O   . HOH W 4 .   ? 4.071   -18.614 8.556   1.00 30.62 ? 1089 HOH A O   1 
HETATM 19519 O  O   . HOH W 4 .   ? 31.277  -17.836 9.664   1.00 35.34 ? 1090 HOH A O   1 
HETATM 19520 O  O   . HOH W 4 .   ? 8.982   -5.616  18.949  1.00 13.65 ? 1091 HOH A O   1 
HETATM 19521 O  O   . HOH W 4 .   ? 20.239  -6.887  50.944  1.00 12.28 ? 1092 HOH A O   1 
HETATM 19522 O  O   . HOH W 4 .   ? 34.243  -20.340 37.833  1.00 39.40 ? 1093 HOH A O   1 
HETATM 19523 O  O   . HOH W 4 .   ? 17.158  -7.600  1.787   1.00 15.46 ? 1094 HOH A O   1 
HETATM 19524 O  O   . HOH W 4 .   ? 14.008  -13.369 55.048  1.00 26.51 ? 1095 HOH A O   1 
HETATM 19525 O  O   . HOH W 4 .   ? 34.262  -11.011 51.828  1.00 34.70 ? 1096 HOH A O   1 
HETATM 19526 O  O   . HOH W 4 .   ? 26.329  1.155   1.242   1.00 28.54 ? 1097 HOH A O   1 
HETATM 19527 O  O   . HOH W 4 .   ? 15.318  -5.220  -8.773  1.00 47.31 ? 1098 HOH A O   1 
HETATM 19528 O  O   . HOH W 4 .   ? 13.971  14.612  1.833   1.00 22.63 ? 1099 HOH A O   1 
HETATM 19529 O  O   . HOH W 4 .   ? 22.691  4.542   -3.493  1.00 38.31 ? 1100 HOH A O   1 
HETATM 19530 O  O   . HOH W 4 .   ? -7.391  -8.477  -7.823  1.00 22.81 ? 1101 HOH A O   1 
HETATM 19531 O  O   . HOH W 4 .   ? 29.800  -21.166 53.120  1.00 25.01 ? 1102 HOH A O   1 
HETATM 19532 O  O   . HOH W 4 .   ? -1.453  -14.274 12.772  1.00 38.67 ? 1103 HOH A O   1 
HETATM 19533 O  O   . HOH W 4 .   ? 10.049  -2.127  -9.845  1.00 36.00 ? 1104 HOH A O   1 
HETATM 19534 O  O   . HOH W 4 .   ? 2.220   -2.351  -11.050 1.00 41.50 ? 1105 HOH A O   1 
HETATM 19535 O  O   . HOH W 4 .   ? 6.218   4.928   21.839  1.00 22.34 ? 1106 HOH A O   1 
HETATM 19536 O  O   . HOH W 4 .   ? 12.518  -30.883 27.467  1.00 26.59 ? 1107 HOH A O   1 
HETATM 19537 O  O   . HOH W 4 .   ? -5.715  -18.266 -3.316  1.00 29.98 ? 1108 HOH A O   1 
HETATM 19538 O  O   . HOH W 4 .   ? 3.764   -24.402 23.627  1.00 34.88 ? 1109 HOH A O   1 
HETATM 19539 O  O   . HOH W 4 .   ? 15.515  -11.579 53.731  1.00 19.77 ? 1110 HOH A O   1 
HETATM 19540 O  O   . HOH W 4 .   ? 30.643  -4.394  24.008  1.00 40.90 ? 1111 HOH A O   1 
HETATM 19541 O  O   . HOH W 4 .   ? -5.957  -2.376  -6.426  1.00 36.63 ? 1112 HOH A O   1 
HETATM 19542 O  O   . HOH W 4 .   ? 1.261   -35.171 37.755  1.00 37.10 ? 1113 HOH A O   1 
HETATM 19543 O  O   . HOH W 4 .   ? 28.076  5.394   4.490   1.00 30.43 ? 1114 HOH A O   1 
HETATM 19544 O  O   . HOH W 4 .   ? 6.890   -30.846 5.893   1.00 30.13 ? 1115 HOH A O   1 
HETATM 19545 O  O   . HOH W 4 .   ? 20.125  10.642  -2.456  1.00 35.21 ? 1116 HOH A O   1 
HETATM 19546 O  O   . HOH W 4 .   ? 2.028   -3.470  10.685  1.00 17.43 ? 1117 HOH A O   1 
HETATM 19547 O  O   . HOH W 4 .   ? 13.217  -42.464 38.675  1.00 23.78 ? 1118 HOH A O   1 
HETATM 19548 O  O   . HOH W 4 .   ? 30.076  -8.503  33.202  1.00 35.56 ? 1119 HOH A O   1 
HETATM 19549 O  O   . HOH W 4 .   ? 3.333   -26.636 -4.776  1.00 32.76 ? 1120 HOH A O   1 
HETATM 19550 O  O   . HOH W 4 .   ? -13.415 -9.937  -0.920  1.00 33.96 ? 1121 HOH A O   1 
HETATM 19551 O  O   . HOH W 4 .   ? 8.467   -32.564 -0.326  1.00 30.99 ? 1122 HOH A O   1 
HETATM 19552 O  O   . HOH W 4 .   ? 25.368  -5.257  -0.859  1.00 34.97 ? 1123 HOH A O   1 
HETATM 19553 O  O   . HOH W 4 .   ? 4.422   -18.337 55.709  1.00 38.13 ? 1124 HOH A O   1 
HETATM 19554 O  O   . HOH W 4 .   ? 8.376   -22.006 16.212  1.00 33.69 ? 1125 HOH A O   1 
HETATM 19555 O  O   . HOH W 4 .   ? 18.306  -11.804 52.370  1.00 17.41 ? 1126 HOH A O   1 
HETATM 19556 O  O   . HOH W 4 .   ? 25.057  -18.345 1.961   1.00 30.51 ? 1127 HOH A O   1 
HETATM 19557 O  O   . HOH W 4 .   ? 0.047   -34.239 39.963  1.00 31.25 ? 1128 HOH A O   1 
HETATM 19558 O  O   . HOH W 4 .   ? 24.331  -24.524 42.121  1.00 21.08 ? 1129 HOH A O   1 
HETATM 19559 O  O   . HOH W 4 .   ? 29.619  -8.297  55.173  1.00 38.85 ? 1130 HOH A O   1 
HETATM 19560 O  O   A HOH W 4 .   ? 4.405   -16.323 32.718  0.59 22.67 ? 1131 HOH A O   1 
HETATM 19561 O  O   B HOH W 4 .   ? 4.562   -17.701 31.374  0.41 23.64 ? 1131 HOH A O   1 
HETATM 19562 O  O   . HOH W 4 .   ? 16.391  -13.878 46.660  1.00 13.17 ? 1132 HOH A O   1 
HETATM 19563 O  O   A HOH W 4 .   ? 29.480  -1.664  50.867  0.55 17.43 ? 1133 HOH A O   1 
HETATM 19564 O  O   B HOH W 4 .   ? 30.087  -3.484  51.399  0.45 21.80 ? 1133 HOH A O   1 
HETATM 19565 O  O   . HOH W 4 .   ? 18.810  -10.810 38.936  1.00 15.67 ? 1134 HOH A O   1 
HETATM 19566 O  O   . HOH W 4 .   ? 8.412   -34.515 19.715  1.00 30.69 ? 1135 HOH A O   1 
HETATM 19567 O  O   . HOH W 4 .   ? 29.480  -20.779 56.186  1.00 26.60 ? 1136 HOH A O   1 
HETATM 19568 O  O   . HOH W 4 .   ? 32.924  -23.074 32.565  1.00 29.39 ? 1137 HOH A O   1 
HETATM 19569 O  O   . HOH W 4 .   ? 3.357   17.616  -0.054  1.00 41.08 ? 1138 HOH A O   1 
HETATM 19570 O  O   . HOH W 4 .   ? 8.470   -23.877 18.307  1.00 35.17 ? 1139 HOH A O   1 
HETATM 19571 O  O   . HOH W 4 .   ? 6.350   -11.886 8.524   1.00 20.88 ? 1140 HOH A O   1 
HETATM 19572 O  O   . HOH W 4 .   ? 6.628   -7.879  -8.101  1.00 45.50 ? 1141 HOH A O   1 
HETATM 19573 O  O   . HOH W 4 .   ? 17.845  -34.354 55.571  1.00 26.95 ? 1142 HOH A O   1 
HETATM 19574 O  O   . HOH W 4 .   ? 22.742  -38.071 37.630  1.00 38.18 ? 1143 HOH A O   1 
HETATM 19575 O  O   . HOH W 4 .   ? -16.677 4.184   23.217  1.00 39.62 ? 1144 HOH A O   1 
HETATM 19576 O  O   . HOH W 4 .   ? 1.866   -16.024 55.191  1.00 11.57 ? 1145 HOH A O   1 
HETATM 19577 O  O   . HOH W 4 .   ? 25.245  -28.447 13.919  1.00 28.30 ? 1146 HOH A O   1 
HETATM 19578 O  O   . HOH W 4 .   ? 3.384   -14.488 10.603  1.00 23.22 ? 1147 HOH A O   1 
HETATM 19579 O  O   A HOH W 4 .   ? 15.798  -2.564  47.774  0.45 20.18 ? 1148 HOH A O   1 
HETATM 19580 O  O   B HOH W 4 .   ? 14.504  -2.784  46.718  0.55 23.06 ? 1148 HOH A O   1 
HETATM 19581 O  O   . HOH W 4 .   ? 18.555  -26.284 3.916   1.00 39.98 ? 1149 HOH A O   1 
HETATM 19582 O  O   . HOH W 4 .   ? 22.587  -0.284  47.478  1.00 22.80 ? 1150 HOH A O   1 
HETATM 19583 O  O   . HOH W 4 .   ? 15.214  15.454  6.923   1.00 20.69 ? 1151 HOH A O   1 
HETATM 19584 O  O   . HOH W 4 .   ? 30.073  0.927   49.482  1.00 25.77 ? 1152 HOH A O   1 
HETATM 19585 O  O   . HOH W 4 .   ? 34.465  -17.815 41.745  1.00 39.15 ? 1153 HOH A O   1 
HETATM 19586 O  O   . HOH W 4 .   ? 4.089   -27.288 31.803  1.00 27.15 ? 1154 HOH A O   1 
HETATM 19587 O  O   . HOH W 4 .   ? 7.168   -11.880 -4.753  1.00 39.32 ? 1155 HOH A O   1 
HETATM 19588 O  O   . HOH W 4 .   ? 12.400  -36.397 44.271  1.00 24.40 ? 1156 HOH A O   1 
HETATM 19589 O  O   . HOH W 4 .   ? -5.433  -7.947  23.354  1.00 38.84 ? 1157 HOH A O   1 
HETATM 19590 O  O   . HOH W 4 .   ? 20.179  12.145  -0.134  1.00 26.36 ? 1158 HOH A O   1 
HETATM 19591 O  O   . HOH W 4 .   ? 18.629  -15.955 -3.917  1.00 26.90 ? 1159 HOH A O   1 
HETATM 19592 O  O   . HOH W 4 .   ? 9.930   -20.592 14.006  1.00 30.66 ? 1160 HOH A O   1 
HETATM 19593 O  O   . HOH W 4 .   ? 4.608   -15.953 8.764   1.00 21.07 ? 1161 HOH A O   1 
HETATM 19594 O  O   . HOH W 4 .   ? 2.087   -20.588 1.160   1.00 20.93 ? 1162 HOH A O   1 
HETATM 19595 O  O   . HOH W 4 .   ? 2.152   -19.918 46.974  1.00 39.80 ? 1163 HOH A O   1 
HETATM 19596 O  O   . HOH W 4 .   ? 27.580  -0.140  44.930  1.00 27.41 ? 1164 HOH A O   1 
HETATM 19597 O  O   . HOH W 4 .   ? 4.413   -15.643 -7.349  1.00 38.26 ? 1165 HOH A O   1 
HETATM 19598 O  O   . HOH W 4 .   ? 5.376   -15.121 -4.942  1.00 18.74 ? 1166 HOH A O   1 
HETATM 19599 O  O   . HOH W 4 .   ? 0.529   -20.940 3.646   1.00 33.63 ? 1167 HOH A O   1 
HETATM 19600 O  O   . HOH W 4 .   ? 27.115  -24.679 42.351  1.00 35.25 ? 1168 HOH A O   1 
HETATM 19601 O  O   . HOH W 4 .   ? 7.347   -23.752 27.588  1.00 42.63 ? 1169 HOH A O   1 
HETATM 19602 O  O   . HOH W 4 .   ? 8.217   -4.502  45.957  1.00 22.53 ? 1170 HOH A O   1 
HETATM 19603 O  O   . HOH W 4 .   ? 32.708  -20.513 30.924  1.00 28.47 ? 1171 HOH A O   1 
HETATM 19604 O  O   . HOH W 4 .   ? 11.663  -32.274 25.299  1.00 33.03 ? 1172 HOH A O   1 
HETATM 19605 O  O   . HOH W 4 .   ? -20.730 1.593   -7.556  1.00 29.35 ? 1173 HOH A O   1 
HETATM 19606 O  O   . HOH W 4 .   ? -4.531  -30.899 40.734  1.00 30.66 ? 1174 HOH A O   1 
HETATM 19607 O  O   . HOH W 4 .   ? -1.083  -8.729  4.734   1.00 32.15 ? 1175 HOH A O   1 
HETATM 19608 O  O   . HOH W 4 .   ? 19.370  -19.401 -6.579  1.00 43.24 ? 1176 HOH A O   1 
HETATM 19609 O  O   . HOH W 4 .   ? 0.995   -22.117 49.296  1.00 44.87 ? 1177 HOH A O   1 
HETATM 19610 O  O   A HOH W 4 .   ? 0.707   -4.870  -8.064  0.47 25.21 ? 1178 HOH A O   1 
HETATM 19611 O  O   B HOH W 4 .   ? 1.941   -6.110  -7.717  0.53 23.28 ? 1178 HOH A O   1 
HETATM 19612 O  O   . HOH W 4 .   ? 30.128  -17.311 14.263  1.00 34.73 ? 1179 HOH A O   1 
HETATM 19613 O  O   . HOH W 4 .   ? 1.863   -25.602 46.739  1.00 44.48 ? 1180 HOH A O   1 
HETATM 19614 O  O   . HOH W 4 .   ? 32.638  0.503   48.237  1.00 28.69 ? 1181 HOH A O   1 
HETATM 19615 O  O   . HOH W 4 .   ? -18.311 -5.292  5.259   1.00 22.86 ? 1182 HOH A O   1 
HETATM 19616 O  O   . HOH W 4 .   ? 4.387   -22.598 54.175  1.00 42.36 ? 1183 HOH A O   1 
HETATM 19617 O  O   . HOH W 4 .   ? 32.552  -19.306 12.153  1.00 38.41 ? 1184 HOH A O   1 
HETATM 19618 O  O   . HOH W 4 .   ? 33.820  -13.032 30.974  1.00 37.54 ? 1185 HOH A O   1 
HETATM 19619 O  O   . HOH W 4 .   ? -2.215  -9.178  21.392  1.00 33.37 ? 1186 HOH A O   1 
HETATM 19620 O  O   . HOH W 4 .   ? -15.181 -7.651  4.732   1.00 32.49 ? 1187 HOH A O   1 
HETATM 19621 O  O   . HOH W 4 .   ? 28.580  -22.245 42.352  1.00 36.28 ? 1188 HOH A O   1 
HETATM 19622 O  O   . HOH W 4 .   ? 5.941   -5.631  -7.452  1.00 39.88 ? 1189 HOH A O   1 
HETATM 19623 O  O   . HOH W 4 .   ? 19.249  -21.009 9.840   1.00 33.05 ? 1190 HOH A O   1 
HETATM 19624 O  O   . HOH W 4 .   ? -17.880 2.602   18.597  1.00 22.38 ? 1191 HOH A O   1 
HETATM 19625 O  O   . HOH W 4 .   ? 29.625  -8.317  6.174   1.00 37.80 ? 1192 HOH A O   1 
HETATM 19626 O  O   . HOH W 4 .   ? -22.493 1.432   -5.716  1.00 28.74 ? 1193 HOH A O   1 
HETATM 19627 O  O   . HOH W 4 .   ? 10.262  -33.809 10.799  1.00 31.52 ? 1194 HOH A O   1 
HETATM 19628 O  O   . HOH W 4 .   ? 29.138  -21.863 49.267  1.00 46.04 ? 1195 HOH A O   1 
HETATM 19629 O  O   . HOH W 4 .   ? 27.997  1.045   47.216  1.00 29.67 ? 1196 HOH A O   1 
HETATM 19630 O  O   . HOH W 4 .   ? 31.774  -19.137 46.501  1.00 41.78 ? 1197 HOH A O   1 
HETATM 19631 O  O   . HOH W 4 .   ? 26.474  -29.994 28.502  1.00 31.02 ? 1198 HOH A O   1 
HETATM 19632 O  O   . HOH W 4 .   ? -10.957 -8.762  29.090  1.00 39.12 ? 1199 HOH A O   1 
HETATM 19633 O  O   . HOH W 4 .   ? -20.221 -5.234  8.031   1.00 37.12 ? 1200 HOH A O   1 
HETATM 19634 O  O   . HOH W 4 .   ? 31.302  -23.103 10.820  1.00 48.61 ? 1201 HOH A O   1 
HETATM 19635 O  O   . HOH W 4 .   ? 6.563   -37.807 34.871  1.00 41.14 ? 1202 HOH A O   1 
HETATM 19636 O  O   . HOH W 4 .   ? -15.694 -10.365 20.757  1.00 35.57 ? 1203 HOH A O   1 
HETATM 19637 O  O   . HOH W 4 .   ? 33.417  -16.084 20.503  1.00 46.24 ? 1204 HOH A O   1 
HETATM 19638 O  O   . HOH W 4 .   ? 19.079  -15.101 -8.619  1.00 43.50 ? 1205 HOH A O   1 
HETATM 19639 O  O   . HOH W 4 .   ? 4.605   17.228  12.569  1.00 42.36 ? 1206 HOH A O   1 
HETATM 19640 O  O   . HOH W 4 .   ? -5.422  -28.428 39.271  1.00 24.50 ? 1207 HOH A O   1 
HETATM 19641 O  O   . HOH W 4 .   ? 29.331  -4.122  28.450  1.00 47.06 ? 1208 HOH A O   1 
HETATM 19642 O  O   . HOH W 4 .   ? 32.190  -39.686 32.008  1.00 41.67 ? 1209 HOH A O   1 
HETATM 19643 O  O   . HOH W 4 .   ? -5.591  -17.817 -9.753  1.00 42.06 ? 1210 HOH A O   1 
HETATM 19644 O  O   . HOH W 4 .   ? 20.726  -15.705 -1.626  1.00 32.29 ? 1211 HOH A O   1 
HETATM 19645 O  O   . HOH W 4 .   ? 18.616  1.062   24.230  1.00 10.78 ? 1212 HOH A O   1 
HETATM 19646 O  O   . HOH W 4 .   ? 9.824   -17.107 3.029   1.00 18.33 ? 1213 HOH A O   1 
HETATM 19647 O  O   . HOH W 4 .   ? 13.061  -32.683 29.297  1.00 31.94 ? 1214 HOH A O   1 
HETATM 19648 O  O   . HOH W 4 .   ? 10.355  -15.453 42.778  1.00 20.55 ? 1215 HOH A O   1 
HETATM 19649 O  O   . HOH W 4 .   ? 3.015   -17.165 16.265  1.00 37.91 ? 1216 HOH A O   1 
HETATM 19650 O  O   . HOH W 4 .   ? -17.674 -3.864  19.839  1.00 45.21 ? 1217 HOH A O   1 
HETATM 19651 O  O   . HOH W 4 .   ? 24.857  -25.643 10.404  1.00 40.32 ? 1218 HOH A O   1 
HETATM 19652 O  O   . HOH W 4 .   ? 25.127  -30.480 12.378  1.00 39.91 ? 1219 HOH A O   1 
HETATM 19653 O  O   . HOH W 4 .   ? 14.071  -38.010 45.636  1.00 40.12 ? 1220 HOH A O   1 
HETATM 19654 O  O   . HOH W 4 .   ? -4.348  -30.847 45.369  1.00 27.53 ? 1221 HOH A O   1 
HETATM 19655 O  O   . HOH W 4 .   ? 18.144  16.403  0.363   1.00 37.19 ? 1222 HOH A O   1 
HETATM 19656 O  O   . HOH W 4 .   ? 5.346   -29.629 8.003   1.00 43.95 ? 1223 HOH A O   1 
HETATM 19657 O  O   . HOH W 4 .   ? 5.723   -20.837 57.570  1.00 39.10 ? 1224 HOH A O   1 
HETATM 19658 O  O   . HOH W 4 .   ? 19.471  -8.890  0.624   1.00 19.75 ? 1225 HOH A O   1 
HETATM 19659 O  O   . HOH W 4 .   ? -2.547  -6.965  -5.150  1.00 30.74 ? 1226 HOH A O   1 
HETATM 19660 O  O   . HOH W 4 .   ? 24.867  -21.564 7.807   1.00 33.83 ? 1227 HOH A O   1 
HETATM 19661 O  O   . HOH W 4 .   ? 5.660   -4.685  -9.427  1.00 42.63 ? 1228 HOH A O   1 
HETATM 19662 O  O   . HOH W 4 .   ? -8.226  -16.725 5.834   1.00 41.72 ? 1229 HOH A O   1 
HETATM 19663 O  O   . HOH W 4 .   ? 9.480   -36.843 47.644  1.00 46.08 ? 1230 HOH A O   1 
HETATM 19664 O  O   . HOH W 4 .   ? 1.622   -34.986 41.930  1.00 33.45 ? 1231 HOH A O   1 
HETATM 19665 O  O   . HOH W 4 .   ? 22.446  -22.428 7.813   1.00 47.10 ? 1232 HOH A O   1 
HETATM 19666 O  O   . HOH W 4 .   ? 0.836   -33.911 48.171  1.00 35.84 ? 1233 HOH A O   1 
HETATM 19667 O  O   . HOH W 4 .   ? 28.682  -5.625  51.994  1.00 48.43 ? 1234 HOH A O   1 
HETATM 19668 O  O   . HOH W 4 .   ? 15.007  -44.283 38.119  1.00 32.19 ? 1235 HOH A O   1 
HETATM 19669 O  O   . HOH W 4 .   ? 10.363  -43.160 32.175  1.00 54.03 ? 1236 HOH A O   1 
HETATM 19670 O  O   . HOH W 4 .   ? 0.502   -18.625 36.716  1.00 44.04 ? 1237 HOH A O   1 
HETATM 19671 O  O   . HOH W 4 .   ? -13.437 -10.213 29.739  1.00 35.93 ? 1238 HOH A O   1 
HETATM 19672 O  O   . HOH W 4 .   ? 8.703   -32.681 7.100   1.00 38.58 ? 1239 HOH A O   1 
HETATM 19673 O  O   . HOH W 4 .   ? 23.163  -20.314 3.784   1.00 32.15 ? 1240 HOH A O   1 
HETATM 19674 O  O   . HOH W 4 .   ? -20.183 4.424   -8.092  1.00 30.90 ? 1241 HOH A O   1 
HETATM 19675 O  O   . HOH W 4 .   ? 18.485  -8.995  52.191  1.00 41.42 ? 1242 HOH A O   1 
HETATM 19676 O  O   . HOH W 4 .   ? 6.813   -17.074 -7.766  1.00 29.21 ? 1243 HOH A O   1 
HETATM 19677 O  O   . HOH W 4 .   ? 0.374   -35.873 44.140  1.00 43.86 ? 1244 HOH A O   1 
HETATM 19678 O  O   . HOH W 4 .   ? 34.124  -27.170 29.361  1.00 42.07 ? 1245 HOH A O   1 
HETATM 19679 O  O   . HOH W 4 .   ? 28.352  -5.061  25.572  1.00 34.81 ? 1246 HOH A O   1 
HETATM 19680 O  O   . HOH W 4 .   ? -9.208  -16.284 -3.743  1.00 38.99 ? 1247 HOH A O   1 
HETATM 19681 O  O   . HOH W 4 .   ? 27.461  -31.539 26.231  1.00 34.93 ? 1248 HOH A O   1 
HETATM 19682 O  O   . HOH W 4 .   ? 21.889  -26.253 9.668   1.00 42.70 ? 1249 HOH A O   1 
HETATM 19683 O  O   . HOH W 4 .   ? -4.640  -5.705  -6.579  1.00 31.77 ? 1250 HOH A O   1 
HETATM 19684 O  O   . HOH W 4 .   ? 37.311  -14.932 40.942  1.00 33.64 ? 1251 HOH A O   1 
HETATM 19685 O  O   . HOH W 4 .   ? -6.706  -10.786 21.625  1.00 30.83 ? 1252 HOH A O   1 
HETATM 19686 O  O   . HOH W 4 .   ? 11.990  -42.184 41.139  1.00 27.19 ? 1253 HOH A O   1 
HETATM 19687 O  O   . HOH W 4 .   ? 19.393  -4.488  51.562  1.00 40.23 ? 1254 HOH A O   1 
HETATM 19688 O  O   . HOH W 4 .   ? 0.114   -6.922  4.006   1.00 39.40 ? 1255 HOH A O   1 
HETATM 19689 O  O   . HOH W 4 .   ? 14.993  -39.905 44.298  1.00 31.65 ? 1256 HOH A O   1 
HETATM 19690 O  O   . HOH W 4 .   ? 25.436  -5.234  -3.958  1.00 38.44 ? 1257 HOH A O   1 
HETATM 19691 O  O   . HOH W 4 .   ? 15.759  -33.069 5.571   1.00 37.37 ? 1258 HOH A O   1 
HETATM 19692 O  O   . HOH W 4 .   ? 33.290  -19.726 14.669  1.00 42.32 ? 1259 HOH A O   1 
HETATM 19693 O  O   . HOH W 4 .   ? -14.294 -8.200  1.046   1.00 38.00 ? 1260 HOH A O   1 
HETATM 19694 O  O   . HOH W 4 .   ? -21.460 -2.993  -0.056  1.00 44.20 ? 1261 HOH A O   1 
HETATM 19695 O  O   . HOH W 4 .   ? 5.495   -26.475 25.340  1.00 32.95 ? 1262 HOH A O   1 
HETATM 19696 O  O   . HOH W 4 .   ? 1.886   -19.911 9.990   1.00 38.12 ? 1263 HOH A O   1 
HETATM 19697 O  O   . HOH W 4 .   ? 2.110   -29.945 6.016   1.00 48.59 ? 1264 HOH A O   1 
HETATM 19698 O  O   . HOH W 4 .   ? 14.302  7.558   -10.135 1.00 24.38 ? 1265 HOH A O   1 
HETATM 19699 O  O   . HOH W 4 .   ? 30.667  -19.674 43.168  1.00 29.43 ? 1266 HOH A O   1 
HETATM 19700 O  O   . HOH W 4 .   ? 2.043   -19.879 44.461  1.00 35.12 ? 1267 HOH A O   1 
HETATM 19701 O  O   . HOH W 4 .   ? -22.893 4.470   -2.168  1.00 32.29 ? 1268 HOH A O   1 
HETATM 19702 O  O   . HOH W 4 .   ? 11.472  -37.622 42.282  1.00 23.32 ? 1269 HOH A O   1 
HETATM 19703 O  O   . HOH W 4 .   ? 5.840   -31.351 3.317   1.00 41.00 ? 1270 HOH A O   1 
HETATM 19704 O  O   . HOH W 4 .   ? -21.595 -1.305  2.106   1.00 49.38 ? 1271 HOH A O   1 
HETATM 19705 O  O   . HOH W 4 .   ? 7.579   -34.480 43.559  1.00 41.72 ? 1272 HOH A O   1 
HETATM 19706 O  O   . HOH W 4 .   ? 15.362  -13.616 57.367  1.00 41.18 ? 1273 HOH A O   1 
HETATM 19707 O  O   . HOH W 4 .   ? 8.800   -38.048 42.588  1.00 34.94 ? 1274 HOH A O   1 
HETATM 19708 O  O   . HOH W 4 .   ? 19.425  -11.675 -0.397  1.00 36.21 ? 1275 HOH A O   1 
HETATM 19709 O  O   . HOH W 4 .   ? -15.331 -5.994  -0.073  1.00 43.14 ? 1276 HOH A O   1 
HETATM 19710 O  O   . HOH W 4 .   ? 16.899  -28.042 4.316   1.00 39.73 ? 1277 HOH A O   1 
HETATM 19711 O  O   . HOH W 4 .   ? 34.419  -17.508 38.648  1.00 43.25 ? 1278 HOH A O   1 
HETATM 19712 O  O   . HOH W 4 .   ? 17.195  3.496   -10.796 1.00 31.81 ? 1279 HOH A O   1 
HETATM 19713 O  O   . HOH W 4 .   ? 26.038  -37.887 38.682  1.00 28.53 ? 1280 HOH A O   1 
HETATM 19714 O  O   . HOH W 4 .   ? 19.840  14.743  -0.113  1.00 31.96 ? 1281 HOH A O   1 
HETATM 19715 O  O   . HOH W 4 .   ? 22.932  -7.407  51.129  1.00 32.16 ? 1282 HOH A O   1 
HETATM 19716 O  O   . HOH W 4 .   ? 5.433   -31.486 31.750  1.00 29.59 ? 1283 HOH A O   1 
HETATM 19717 O  O   . HOH W 4 .   ? 31.428  -19.360 52.514  1.00 24.30 ? 1284 HOH A O   1 
HETATM 19718 O  O   . HOH W 4 .   ? 24.677  -6.305  52.779  1.00 34.12 ? 1285 HOH A O   1 
HETATM 19719 O  O   . HOH W 4 .   ? 8.431   -0.823  -10.955 1.00 41.87 ? 1286 HOH A O   1 
HETATM 19720 O  O   . HOH W 4 .   ? 13.010  -39.107 47.872  1.00 41.85 ? 1287 HOH A O   1 
HETATM 19721 O  O   . HOH W 4 .   ? 9.255   -36.140 45.448  1.00 47.68 ? 1288 HOH A O   1 
HETATM 19722 O  O   . HOH W 4 .   ? -8.236  -18.461 -3.816  1.00 31.35 ? 1289 HOH A O   1 
HETATM 19723 O  O   . HOH W 4 .   ? 34.545  -24.902 30.801  1.00 41.67 ? 1290 HOH A O   1 
HETATM 19724 O  O   . HOH W 4 .   ? 17.179  -25.567 65.800  1.00 46.18 ? 1291 HOH A O   1 
HETATM 19725 O  O   . HOH W 4 .   ? -16.398 4.238   -10.563 1.00 49.82 ? 1292 HOH A O   1 
HETATM 19726 O  O   . HOH X 4 .   ? 38.342  -1.805  24.433  1.00 40.54 ? 801  HOH B O   1 
HETATM 19727 O  O   . HOH X 4 .   ? 39.795  9.667   51.240  1.00 31.05 ? 802  HOH B O   1 
HETATM 19728 O  O   . HOH X 4 .   ? 10.055  10.714  39.932  1.00 72.47 ? 803  HOH B O   1 
HETATM 19729 O  O   . HOH X 4 .   ? 34.963  34.578  45.022  1.00 34.86 ? 804  HOH B O   1 
HETATM 19730 O  O   . HOH X 4 .   ? 43.539  35.648  44.474  1.00 35.37 ? 805  HOH B O   1 
HETATM 19731 O  O   . HOH X 4 .   ? 33.150  15.173  41.205  1.00 37.98 ? 806  HOH B O   1 
HETATM 19732 O  O   . HOH X 4 .   ? 41.976  -8.497  16.460  1.00 32.60 ? 807  HOH B O   1 
HETATM 19733 O  O   . HOH X 4 .   ? 47.684  -1.626  49.273  1.00 43.34 ? 808  HOH B O   1 
HETATM 19734 O  O   . HOH X 4 .   ? -1.146  13.712  66.302  1.00 40.70 ? 809  HOH B O   1 
HETATM 19735 O  O   . HOH X 4 .   ? 28.304  8.336   2.921   1.00 39.92 ? 810  HOH B O   1 
HETATM 19736 O  O   . HOH X 4 .   ? 38.353  10.178  48.630  1.00 33.54 ? 811  HOH B O   1 
HETATM 19737 O  O   . HOH X 4 .   ? 19.680  6.303   49.821  1.00 41.67 ? 812  HOH B O   1 
HETATM 19738 O  O   . HOH X 4 .   ? 15.599  0.681   28.393  1.00 33.15 ? 813  HOH B O   1 
HETATM 19739 O  O   . HOH X 4 .   ? -3.052  7.073   25.848  1.00 28.27 ? 814  HOH B O   1 
HETATM 19740 O  O   . HOH X 4 .   ? -2.130  -13.146 42.856  1.00 29.20 ? 815  HOH B O   1 
HETATM 19741 O  O   . HOH X 4 .   ? -9.153  -14.946 48.684  1.00 34.75 ? 816  HOH B O   1 
HETATM 19742 O  O   . HOH X 4 .   ? 42.747  7.839   48.187  1.00 33.52 ? 817  HOH B O   1 
HETATM 19743 O  O   . HOH X 4 .   ? 27.156  43.582  35.169  1.00 42.79 ? 818  HOH B O   1 
HETATM 19744 O  O   . HOH X 4 .   ? 27.277  0.868   6.144   1.00 34.80 ? 819  HOH B O   1 
HETATM 19745 O  O   . HOH X 4 .   ? 3.493   -0.394  66.688  1.00 24.39 ? 820  HOH B O   1 
HETATM 19746 O  O   . HOH X 4 .   ? 25.628  3.436   45.105  1.00 25.25 ? 821  HOH B O   1 
HETATM 19747 O  O   . HOH X 4 .   ? 10.003  15.592  54.990  1.00 37.66 ? 822  HOH B O   1 
HETATM 19748 O  O   . HOH X 4 .   ? 32.346  -1.746  49.770  1.00 37.10 ? 823  HOH B O   1 
HETATM 19749 O  O   . HOH X 4 .   ? 56.403  -5.168  18.033  1.00 26.35 ? 824  HOH B O   1 
HETATM 19750 O  O   . HOH X 4 .   ? 28.789  9.231   52.701  1.00 20.69 ? 825  HOH B O   1 
HETATM 19751 O  O   . HOH X 4 .   ? 62.753  1.019   42.640  1.00 31.63 ? 826  HOH B O   1 
HETATM 19752 O  O   . HOH X 4 .   ? -0.497  -2.528  65.427  1.00 30.86 ? 827  HOH B O   1 
HETATM 19753 O  O   . HOH X 4 .   ? 5.926   30.045  30.292  1.00 29.10 ? 828  HOH B O   1 
HETATM 19754 O  O   . HOH X 4 .   ? 34.430  -8.597  11.599  1.00 38.43 ? 829  HOH B O   1 
HETATM 19755 O  O   . HOH X 4 .   ? 7.633   -3.252  54.968  1.00 35.88 ? 830  HOH B O   1 
HETATM 19756 O  O   . HOH X 4 .   ? 0.382   -13.713 34.166  1.00 40.83 ? 831  HOH B O   1 
HETATM 19757 O  O   . HOH X 4 .   ? 18.929  23.027  44.964  1.00 18.28 ? 832  HOH B O   1 
HETATM 19758 O  O   . HOH X 4 .   ? 53.460  14.851  16.485  1.00 45.82 ? 833  HOH B O   1 
HETATM 19759 O  O   . HOH X 4 .   ? 22.463  44.068  41.929  1.00 39.45 ? 834  HOH B O   1 
HETATM 19760 O  O   . HOH X 4 .   ? 21.480  40.869  43.997  1.00 30.11 ? 835  HOH B O   1 
HETATM 19761 O  O   . HOH X 4 .   ? -18.046 -0.018  60.461  1.00 24.93 ? 836  HOH B O   1 
HETATM 19762 O  O   . HOH X 4 .   ? -10.395 9.692   55.198  1.00 32.48 ? 837  HOH B O   1 
HETATM 19763 O  O   . HOH X 4 .   ? 8.222   -5.696  31.382  1.00 16.51 ? 838  HOH B O   1 
HETATM 19764 O  O   . HOH X 4 .   ? 14.314  30.112  52.414  1.00 35.06 ? 839  HOH B O   1 
HETATM 19765 O  O   . HOH X 4 .   ? 53.071  9.771   22.888  1.00 34.28 ? 840  HOH B O   1 
HETATM 19766 O  O   . HOH X 4 .   ? 29.476  30.727  29.205  1.00 25.38 ? 841  HOH B O   1 
HETATM 19767 O  O   . HOH X 4 .   ? -13.431 6.730   25.904  1.00 32.81 ? 842  HOH B O   1 
HETATM 19768 O  O   . HOH X 4 .   ? 56.334  -2.851  41.800  1.00 31.91 ? 843  HOH B O   1 
HETATM 19769 O  O   . HOH X 4 .   ? 36.579  19.663  10.136  1.00 28.55 ? 844  HOH B O   1 
HETATM 19770 O  O   . HOH X 4 .   ? 15.122  31.028  21.352  1.00 31.76 ? 845  HOH B O   1 
HETATM 19771 O  O   . HOH X 4 .   ? 38.386  39.370  37.698  1.00 36.95 ? 846  HOH B O   1 
HETATM 19772 O  O   . HOH X 4 .   ? 24.543  15.039  42.434  1.00 26.71 ? 847  HOH B O   1 
HETATM 19773 O  O   . HOH X 4 .   ? 60.575  -2.206  43.091  1.00 35.32 ? 848  HOH B O   1 
HETATM 19774 O  O   . HOH X 4 .   ? 39.773  13.324  49.035  1.00 28.22 ? 849  HOH B O   1 
HETATM 19775 O  O   . HOH X 4 .   ? 15.458  23.393  53.602  1.00 30.72 ? 850  HOH B O   1 
HETATM 19776 O  O   . HOH X 4 .   ? 24.356  22.436  16.355  1.00 18.27 ? 851  HOH B O   1 
HETATM 19777 O  O   . HOH X 4 .   ? 63.648  5.003   29.180  1.00 14.64 ? 852  HOH B O   1 
HETATM 19778 O  O   . HOH X 4 .   ? 25.097  11.448  46.324  1.00 21.82 ? 853  HOH B O   1 
HETATM 19779 O  O   . HOH X 4 .   ? 36.270  2.198   14.662  1.00 20.59 ? 854  HOH B O   1 
HETATM 19780 O  O   . HOH X 4 .   ? 6.253   -11.510 46.400  1.00 20.37 ? 855  HOH B O   1 
HETATM 19781 O  O   . HOH X 4 .   ? 62.872  -6.917  30.022  1.00 46.54 ? 856  HOH B O   1 
HETATM 19782 O  O   . HOH X 4 .   ? 37.463  2.679   22.784  1.00 19.66 ? 857  HOH B O   1 
HETATM 19783 O  O   . HOH X 4 .   ? 13.405  24.968  57.531  1.00 47.05 ? 858  HOH B O   1 
HETATM 19784 O  O   . HOH X 4 .   ? 55.577  28.872  38.450  1.00 30.38 ? 859  HOH B O   1 
HETATM 19785 O  O   . HOH X 4 .   ? 49.313  13.511  11.783  1.00 42.88 ? 860  HOH B O   1 
HETATM 19786 O  O   . HOH X 4 .   ? 11.308  12.727  54.823  1.00 29.80 ? 861  HOH B O   1 
HETATM 19787 O  O   . HOH X 4 .   ? 1.203   15.926  30.371  1.00 23.49 ? 862  HOH B O   1 
HETATM 19788 O  O   . HOH X 4 .   ? -16.240 -7.420  36.530  1.00 27.84 ? 863  HOH B O   1 
HETATM 19789 O  O   . HOH X 4 .   ? 29.957  22.187  46.609  1.00 31.68 ? 864  HOH B O   1 
HETATM 19790 O  O   . HOH X 4 .   ? 14.298  11.787  44.555  1.00 13.71 ? 865  HOH B O   1 
HETATM 19791 O  O   . HOH X 4 .   ? -0.676  19.211  44.691  1.00 26.02 ? 866  HOH B O   1 
HETATM 19792 O  O   . HOH X 4 .   ? 10.716  5.435   61.166  1.00 24.97 ? 867  HOH B O   1 
HETATM 19793 O  O   . HOH X 4 .   ? 64.167  -1.768  23.528  1.00 27.26 ? 868  HOH B O   1 
HETATM 19794 O  O   . HOH X 4 .   ? 43.220  28.162  44.550  1.00 26.78 ? 869  HOH B O   1 
HETATM 19795 O  O   . HOH X 4 .   ? 32.015  0.008   39.313  1.00 13.67 ? 870  HOH B O   1 
HETATM 19796 O  O   . HOH X 4 .   ? 41.962  8.072   50.608  1.00 39.14 ? 871  HOH B O   1 
HETATM 19797 O  O   . HOH X 4 .   ? 11.474  -1.500  49.761  1.00 42.07 ? 872  HOH B O   1 
HETATM 19798 O  O   . HOH X 4 .   ? 27.640  24.013  27.776  1.00 14.46 ? 873  HOH B O   1 
HETATM 19799 O  O   A HOH X 4 .   ? 7.324   -7.510  46.979  0.47 15.28 ? 874  HOH B O   1 
HETATM 19800 O  O   B HOH X 4 .   ? 11.726  -7.247  49.510  0.53 14.85 ? 874  HOH B O   1 
HETATM 19801 O  O   . HOH X 4 .   ? 41.362  2.293   47.578  1.00 17.39 ? 875  HOH B O   1 
HETATM 19802 O  O   . HOH X 4 .   ? 51.612  14.269  40.149  1.00 31.48 ? 876  HOH B O   1 
HETATM 19803 O  O   . HOH X 4 .   ? -6.724  -12.355 63.696  1.00 47.03 ? 877  HOH B O   1 
HETATM 19804 O  O   . HOH X 4 .   ? 11.051  0.562   46.165  1.00 26.96 ? 878  HOH B O   1 
HETATM 19805 O  O   . HOH X 4 .   ? 23.875  29.824  27.676  1.00 20.20 ? 879  HOH B O   1 
HETATM 19806 O  O   . HOH X 4 .   ? -9.211  6.667   33.158  1.00 32.15 ? 880  HOH B O   1 
HETATM 19807 O  O   . HOH X 4 .   ? -23.512 -2.412  52.591  1.00 32.25 ? 881  HOH B O   1 
HETATM 19808 O  O   . HOH X 4 .   ? 27.668  28.337  27.691  1.00 32.74 ? 882  HOH B O   1 
HETATM 19809 O  O   . HOH X 4 .   ? 19.754  35.119  47.291  1.00 28.83 ? 883  HOH B O   1 
HETATM 19810 O  O   . HOH X 4 .   ? 8.281   16.994  21.265  1.00 38.74 ? 884  HOH B O   1 
HETATM 19811 O  O   . HOH X 4 .   ? 38.095  18.381  38.908  1.00 18.82 ? 885  HOH B O   1 
HETATM 19812 O  O   . HOH X 4 .   ? -20.599 -5.443  47.462  1.00 37.83 ? 886  HOH B O   1 
HETATM 19813 O  O   . HOH X 4 .   ? 45.291  21.461  31.646  1.00 23.01 ? 887  HOH B O   1 
HETATM 19814 O  O   . HOH X 4 .   ? -19.385 3.592   32.723  1.00 34.04 ? 888  HOH B O   1 
HETATM 19815 O  O   . HOH X 4 .   ? 9.638   10.428  52.139  1.00 21.11 ? 889  HOH B O   1 
HETATM 19816 O  O   . HOH X 4 .   ? 13.005  29.985  47.020  1.00 31.22 ? 890  HOH B O   1 
HETATM 19817 O  O   . HOH X 4 .   ? -4.673  4.507   37.024  1.00 16.45 ? 891  HOH B O   1 
HETATM 19818 O  O   . HOH X 4 .   ? 61.127  -2.878  20.081  1.00 39.29 ? 892  HOH B O   1 
HETATM 19819 O  O   . HOH X 4 .   ? 14.719  29.753  25.483  1.00 31.79 ? 893  HOH B O   1 
HETATM 19820 O  O   . HOH X 4 .   ? 28.582  20.857  43.349  1.00 47.16 ? 894  HOH B O   1 
HETATM 19821 O  O   . HOH X 4 .   ? 15.261  29.995  37.776  1.00 27.72 ? 895  HOH B O   1 
HETATM 19822 O  O   . HOH X 4 .   ? 22.384  20.088  38.964  1.00 19.62 ? 896  HOH B O   1 
HETATM 19823 O  O   . HOH X 4 .   ? 15.292  15.930  43.732  1.00 12.37 ? 897  HOH B O   1 
HETATM 19824 O  O   . HOH X 4 .   ? 26.203  6.498   33.201  1.00 12.26 ? 898  HOH B O   1 
HETATM 19825 O  O   . HOH X 4 .   ? 39.508  9.761   46.024  1.00 16.22 ? 899  HOH B O   1 
HETATM 19826 O  O   . HOH X 4 .   ? 37.134  13.391  35.419  1.00 20.91 ? 900  HOH B O   1 
HETATM 19827 O  O   . HOH X 4 .   ? 48.598  18.402  34.123  1.00 24.75 ? 901  HOH B O   1 
HETATM 19828 O  O   . HOH X 4 .   ? 36.118  0.840   11.818  1.00 35.05 ? 902  HOH B O   1 
HETATM 19829 O  O   . HOH X 4 .   ? 32.402  22.888  19.546  1.00 24.23 ? 903  HOH B O   1 
HETATM 19830 O  O   . HOH X 4 .   ? 52.759  20.182  35.827  1.00 36.57 ? 904  HOH B O   1 
HETATM 19831 O  O   . HOH X 4 .   ? 18.555  29.322  31.861  1.00 17.83 ? 905  HOH B O   1 
HETATM 19832 O  O   . HOH X 4 .   ? 14.855  4.339   48.406  1.00 36.75 ? 906  HOH B O   1 
HETATM 19833 O  O   . HOH X 4 .   ? 33.049  7.472   34.638  1.00 15.92 ? 907  HOH B O   1 
HETATM 19834 O  O   . HOH X 4 .   ? -15.933 -1.100  56.818  1.00 20.95 ? 908  HOH B O   1 
HETATM 19835 O  O   . HOH X 4 .   ? 14.475  5.753   24.122  1.00 10.99 ? 909  HOH B O   1 
HETATM 19836 O  O   . HOH X 4 .   ? -9.566  2.136   40.127  1.00 23.59 ? 910  HOH B O   1 
HETATM 19837 O  O   . HOH X 4 .   ? 26.132  8.604   49.496  1.00 28.47 ? 911  HOH B O   1 
HETATM 19838 O  O   . HOH X 4 .   ? 42.684  2.420   13.688  1.00 26.07 ? 912  HOH B O   1 
HETATM 19839 O  O   . HOH X 4 .   ? 60.194  -6.450  23.630  1.00 24.78 ? 913  HOH B O   1 
HETATM 19840 O  O   . HOH X 4 .   ? 7.548   9.564   25.611  1.00 11.87 ? 914  HOH B O   1 
HETATM 19841 O  O   . HOH X 4 .   ? 45.984  5.759   49.884  1.00 33.60 ? 915  HOH B O   1 
HETATM 19842 O  O   . HOH X 4 .   ? 28.174  5.488   41.801  1.00 12.87 ? 916  HOH B O   1 
HETATM 19843 O  O   . HOH X 4 .   ? -10.865 4.005   42.736  1.00 27.10 ? 917  HOH B O   1 
HETATM 19844 O  O   . HOH X 4 .   ? 39.248  -5.324  50.589  1.00 38.82 ? 918  HOH B O   1 
HETATM 19845 O  O   . HOH X 4 .   ? 54.418  -3.518  18.668  1.00 43.77 ? 919  HOH B O   1 
HETATM 19846 O  O   . HOH X 4 .   ? 3.880   9.223   62.553  1.00 21.95 ? 920  HOH B O   1 
HETATM 19847 O  O   . HOH X 4 .   ? -15.160 1.121   35.721  1.00 18.83 ? 921  HOH B O   1 
HETATM 19848 O  O   . HOH X 4 .   ? 37.449  26.406  34.473  1.00 22.54 ? 922  HOH B O   1 
HETATM 19849 O  O   . HOH X 4 .   ? 36.773  25.790  14.093  1.00 28.05 ? 923  HOH B O   1 
HETATM 19850 O  O   . HOH X 4 .   ? 17.350  17.415  52.030  1.00 32.89 ? 924  HOH B O   1 
HETATM 19851 O  O   . HOH X 4 .   ? 19.490  26.784  52.220  1.00 32.58 ? 925  HOH B O   1 
HETATM 19852 O  O   . HOH X 4 .   ? -16.000 -13.915 49.352  1.00 27.81 ? 926  HOH B O   1 
HETATM 19853 O  O   . HOH X 4 .   ? 39.120  23.784  28.379  1.00 18.28 ? 927  HOH B O   1 
HETATM 19854 O  O   . HOH X 4 .   ? 32.627  -3.657  30.883  1.00 36.12 ? 928  HOH B O   1 
HETATM 19855 O  O   . HOH X 4 .   ? 35.746  16.572  39.703  1.00 21.58 ? 929  HOH B O   1 
HETATM 19856 O  O   . HOH X 4 .   ? 8.942   -1.485  47.755  1.00 19.19 ? 930  HOH B O   1 
HETATM 19857 O  O   . HOH X 4 .   ? 41.707  -3.408  12.905  1.00 36.44 ? 931  HOH B O   1 
HETATM 19858 O  O   . HOH X 4 .   ? 29.860  15.266  38.647  1.00 17.96 ? 932  HOH B O   1 
HETATM 19859 O  O   . HOH X 4 .   ? 18.006  31.137  41.885  1.00 21.86 ? 933  HOH B O   1 
HETATM 19860 O  O   . HOH X 4 .   ? 44.921  -10.653 41.834  1.00 32.68 ? 934  HOH B O   1 
HETATM 19861 O  O   . HOH X 4 .   ? 0.319   8.467   63.261  1.00 28.27 ? 935  HOH B O   1 
HETATM 19862 O  O   . HOH X 4 .   ? -2.478  -6.117  59.106  1.00 17.76 ? 936  HOH B O   1 
HETATM 19863 O  O   . HOH X 4 .   ? 12.668  13.030  51.044  1.00 20.85 ? 937  HOH B O   1 
HETATM 19864 O  O   . HOH X 4 .   ? -1.067  8.187   40.891  1.00 16.46 ? 938  HOH B O   1 
HETATM 19865 O  O   . HOH X 4 .   ? 21.898  29.797  25.715  1.00 27.91 ? 939  HOH B O   1 
HETATM 19866 O  O   . HOH X 4 .   ? -13.715 4.648   22.488  1.00 22.86 ? 940  HOH B O   1 
HETATM 19867 O  O   . HOH X 4 .   ? 13.031  26.998  37.502  1.00 16.42 ? 941  HOH B O   1 
HETATM 19868 O  O   . HOH X 4 .   ? 32.517  6.236   44.180  1.00 12.96 ? 942  HOH B O   1 
HETATM 19869 O  O   . HOH X 4 .   ? 57.389  -4.480  38.250  1.00 20.98 ? 943  HOH B O   1 
HETATM 19870 O  O   . HOH X 4 .   ? 43.132  -3.680  14.955  1.00 32.13 ? 944  HOH B O   1 
HETATM 19871 O  O   . HOH X 4 .   ? 33.808  0.110   10.318  1.00 35.77 ? 945  HOH B O   1 
HETATM 19872 O  O   . HOH X 4 .   ? 45.598  8.042   21.965  1.00 15.94 ? 946  HOH B O   1 
HETATM 19873 O  O   . HOH X 4 .   ? 34.944  11.896  35.177  1.00 14.63 ? 947  HOH B O   1 
HETATM 19874 O  O   . HOH X 4 .   ? 38.340  27.112  28.179  1.00 33.08 ? 948  HOH B O   1 
HETATM 19875 O  O   . HOH X 4 .   ? 32.353  2.837   11.060  1.00 24.79 ? 949  HOH B O   1 
HETATM 19876 O  O   . HOH X 4 .   ? 42.149  -10.447 45.050  1.00 26.29 ? 950  HOH B O   1 
HETATM 19877 O  O   . HOH X 4 .   ? 39.357  36.516  37.283  1.00 23.85 ? 951  HOH B O   1 
HETATM 19878 O  O   . HOH X 4 .   ? 55.922  -15.263 33.168  1.00 38.49 ? 952  HOH B O   1 
HETATM 19879 O  O   . HOH X 4 .   ? 52.320  3.314   47.964  1.00 39.57 ? 953  HOH B O   1 
HETATM 19880 O  O   . HOH X 4 .   ? 35.468  8.192   12.129  1.00 18.37 ? 954  HOH B O   1 
HETATM 19881 O  O   . HOH X 4 .   ? 19.910  32.560  48.316  1.00 28.38 ? 955  HOH B O   1 
HETATM 19882 O  O   . HOH X 4 .   ? 30.897  -5.077  6.042   1.00 43.45 ? 956  HOH B O   1 
HETATM 19883 O  O   . HOH X 4 .   ? 44.727  -9.355  26.328  1.00 38.29 ? 957  HOH B O   1 
HETATM 19884 O  O   . HOH X 4 .   ? 33.217  26.112  21.788  1.00 28.27 ? 958  HOH B O   1 
HETATM 19885 O  O   . HOH X 4 .   ? 33.121  11.153  42.381  1.00 13.54 ? 959  HOH B O   1 
HETATM 19886 O  O   . HOH X 4 .   ? 31.691  -0.973  29.239  1.00 34.33 ? 960  HOH B O   1 
HETATM 19887 O  O   . HOH X 4 .   ? -17.965 -7.028  39.904  1.00 35.73 ? 961  HOH B O   1 
HETATM 19888 O  O   . HOH X 4 .   ? 36.252  0.679   23.929  1.00 30.40 ? 962  HOH B O   1 
HETATM 19889 O  O   . HOH X 4 .   ? 28.568  5.057   28.920  1.00 14.47 ? 963  HOH B O   1 
HETATM 19890 O  O   A HOH X 4 .   ? 0.878   1.788   37.790  0.57 12.85 ? 964  HOH B O   1 
HETATM 19891 O  O   B HOH X 4 .   ? -0.172  0.015   37.517  0.43 20.40 ? 964  HOH B O   1 
HETATM 19892 O  O   . HOH X 4 .   ? 37.658  2.848   50.493  1.00 26.16 ? 965  HOH B O   1 
HETATM 19893 O  O   . HOH X 4 .   ? 64.124  -9.735  27.110  1.00 47.13 ? 966  HOH B O   1 
HETATM 19894 O  O   . HOH X 4 .   ? 7.386   -5.022  43.385  1.00 14.33 ? 967  HOH B O   1 
HETATM 19895 O  O   . HOH X 4 .   ? 9.607   -2.741  33.446  1.00 13.79 ? 968  HOH B O   1 
HETATM 19896 O  O   . HOH X 4 .   ? -8.723  -7.778  39.741  1.00 17.30 ? 969  HOH B O   1 
HETATM 19897 O  O   . HOH X 4 .   ? 32.090  -1.276  43.604  1.00 13.35 ? 970  HOH B O   1 
HETATM 19898 O  O   . HOH X 4 .   ? 39.165  -4.461  9.148   1.00 40.43 ? 971  HOH B O   1 
HETATM 19899 O  O   . HOH X 4 .   ? 45.913  18.335  33.927  1.00 24.26 ? 972  HOH B O   1 
HETATM 19900 O  O   . HOH X 4 .   ? 45.585  22.729  43.603  1.00 19.19 ? 973  HOH B O   1 
HETATM 19901 O  O   . HOH X 4 .   ? 44.184  -5.095  42.113  1.00 13.22 ? 974  HOH B O   1 
HETATM 19902 O  O   . HOH X 4 .   ? 2.914   -3.177  38.577  1.00 14.71 ? 975  HOH B O   1 
HETATM 19903 O  O   . HOH X 4 .   ? -6.135  -9.578  28.461  1.00 36.71 ? 976  HOH B O   1 
HETATM 19904 O  O   . HOH X 4 .   ? 6.002   23.399  27.896  1.00 25.92 ? 977  HOH B O   1 
HETATM 19905 O  O   . HOH X 4 .   ? 1.367   -3.697  40.683  1.00 13.69 ? 978  HOH B O   1 
HETATM 19906 O  O   . HOH X 4 .   ? 25.993  36.979  48.290  1.00 24.73 ? 979  HOH B O   1 
HETATM 19907 O  O   . HOH X 4 .   ? -5.761  11.194  62.688  1.00 26.88 ? 980  HOH B O   1 
HETATM 19908 O  O   . HOH X 4 .   ? -10.085 -11.676 44.200  1.00 48.37 ? 981  HOH B O   1 
HETATM 19909 O  O   . HOH X 4 .   ? 48.182  -9.819  42.153  1.00 27.52 ? 982  HOH B O   1 
HETATM 19910 O  O   . HOH X 4 .   ? 37.425  -3.335  22.204  1.00 40.07 ? 983  HOH B O   1 
HETATM 19911 O  O   . HOH X 4 .   ? 47.800  11.940  43.160  1.00 20.66 ? 984  HOH B O   1 
HETATM 19912 O  O   . HOH X 4 .   ? 40.519  27.577  19.446  1.00 30.43 ? 985  HOH B O   1 
HETATM 19913 O  O   . HOH X 4 .   ? 46.053  -12.685 29.919  1.00 41.35 ? 986  HOH B O   1 
HETATM 19914 O  O   . HOH X 4 .   ? 34.742  4.778   44.829  1.00 14.11 ? 987  HOH B O   1 
HETATM 19915 O  O   . HOH X 4 .   ? -21.874 -3.083  35.238  1.00 28.74 ? 988  HOH B O   1 
HETATM 19916 O  O   . HOH X 4 .   ? 37.800  40.340  42.856  1.00 34.38 ? 989  HOH B O   1 
HETATM 19917 O  O   . HOH X 4 .   ? -0.628  7.329   22.503  1.00 36.13 ? 990  HOH B O   1 
HETATM 19918 O  O   . HOH X 4 .   ? 3.337   -6.365  42.482  1.00 15.29 ? 991  HOH B O   1 
HETATM 19919 O  O   . HOH X 4 .   ? 27.491  7.901   44.790  1.00 12.20 ? 992  HOH B O   1 
HETATM 19920 O  O   . HOH X 4 .   ? 23.279  35.748  30.923  1.00 33.57 ? 993  HOH B O   1 
HETATM 19921 O  O   . HOH X 4 .   ? 17.792  4.385   22.933  1.00 13.67 ? 994  HOH B O   1 
HETATM 19922 O  O   . HOH X 4 .   ? -10.150 -1.235  64.721  1.00 32.10 ? 995  HOH B O   1 
HETATM 19923 O  O   . HOH X 4 .   ? -1.909  -1.538  22.169  1.00 15.77 ? 996  HOH B O   1 
HETATM 19924 O  O   . HOH X 4 .   ? 14.783  20.580  22.798  1.00 25.99 ? 997  HOH B O   1 
HETATM 19925 O  O   . HOH X 4 .   ? 36.411  2.354   20.472  1.00 14.08 ? 998  HOH B O   1 
HETATM 19926 O  O   . HOH X 4 .   ? 17.395  16.449  15.905  1.00 26.92 ? 999  HOH B O   1 
HETATM 19927 O  O   . HOH X 4 .   ? 29.702  0.531   44.963  1.00 23.21 ? 1000 HOH B O   1 
HETATM 19928 O  O   . HOH X 4 .   ? 40.803  -9.335  41.290  1.00 13.36 ? 1001 HOH B O   1 
HETATM 19929 O  O   . HOH X 4 .   ? 4.585   -2.740  25.387  1.00 20.09 ? 1002 HOH B O   1 
HETATM 19930 O  O   . HOH X 4 .   ? 14.433  17.832  32.466  1.00 12.81 ? 1003 HOH B O   1 
HETATM 19931 O  O   . HOH X 4 .   ? -10.698 -10.862 60.933  1.00 32.85 ? 1004 HOH B O   1 
HETATM 19932 O  O   . HOH X 4 .   ? 36.678  -2.021  43.738  1.00 16.02 ? 1005 HOH B O   1 
HETATM 19933 O  O   . HOH X 4 .   ? 34.821  11.650  45.999  1.00 26.84 ? 1006 HOH B O   1 
HETATM 19934 O  O   . HOH X 4 .   ? 41.830  16.004  10.205  1.00 31.64 ? 1007 HOH B O   1 
HETATM 19935 O  O   . HOH X 4 .   ? 34.654  -0.131  45.692  1.00 24.05 ? 1008 HOH B O   1 
HETATM 19936 O  O   . HOH X 4 .   ? 45.248  -5.757  46.609  1.00 25.75 ? 1009 HOH B O   1 
HETATM 19937 O  O   . HOH X 4 .   ? 40.072  -2.089  26.572  1.00 15.20 ? 1010 HOH B O   1 
HETATM 19938 O  O   . HOH X 4 .   ? -2.701  5.996   40.127  1.00 13.11 ? 1011 HOH B O   1 
HETATM 19939 O  O   . HOH X 4 .   ? 27.164  20.685  10.960  1.00 39.11 ? 1012 HOH B O   1 
HETATM 19940 O  O   . HOH X 4 .   ? 24.041  1.447   15.612  1.00 11.61 ? 1013 HOH B O   1 
HETATM 19941 O  O   . HOH X 4 .   ? 1.695   18.680  39.234  1.00 22.72 ? 1014 HOH B O   1 
HETATM 19942 O  O   . HOH X 4 .   ? 15.267  3.091   57.722  1.00 27.94 ? 1015 HOH B O   1 
HETATM 19943 O  O   . HOH X 4 .   ? 12.784  0.743   50.538  1.00 30.42 ? 1016 HOH B O   1 
HETATM 19944 O  O   . HOH X 4 .   ? 26.164  26.604  50.758  1.00 27.97 ? 1017 HOH B O   1 
HETATM 19945 O  O   . HOH X 4 .   ? 39.429  3.919   10.288  1.00 32.16 ? 1018 HOH B O   1 
HETATM 19946 O  O   . HOH X 4 .   ? 33.191  -12.869 17.638  1.00 33.72 ? 1019 HOH B O   1 
HETATM 19947 O  O   . HOH X 4 .   ? 37.389  26.069  30.519  1.00 25.84 ? 1020 HOH B O   1 
HETATM 19948 O  O   . HOH X 4 .   ? 27.105  4.168   31.949  1.00 19.14 ? 1021 HOH B O   1 
HETATM 19949 O  O   . HOH X 4 .   ? 28.177  2.837   5.592   1.00 32.11 ? 1022 HOH B O   1 
HETATM 19950 O  O   . HOH X 4 .   ? -0.650  -4.291  28.803  1.00 9.62  ? 1023 HOH B O   1 
HETATM 19951 O  O   . HOH X 4 .   ? 42.996  -1.108  16.762  1.00 15.53 ? 1024 HOH B O   1 
HETATM 19952 O  O   . HOH X 4 .   ? 38.600  -2.356  33.452  1.00 9.76  ? 1025 HOH B O   1 
HETATM 19953 O  O   . HOH X 4 .   ? 23.313  7.242   33.231  1.00 11.91 ? 1026 HOH B O   1 
HETATM 19954 O  O   . HOH X 4 .   ? 53.122  -5.669  36.011  1.00 16.18 ? 1027 HOH B O   1 
HETATM 19955 O  O   . HOH X 4 .   ? 3.490   14.241  54.816  1.00 16.68 ? 1028 HOH B O   1 
HETATM 19956 O  O   . HOH X 4 .   ? -5.675  5.641   25.281  1.00 16.98 ? 1029 HOH B O   1 
HETATM 19957 O  O   . HOH X 4 .   ? 29.072  -9.860  9.173   1.00 29.21 ? 1030 HOH B O   1 
HETATM 19958 O  O   . HOH X 4 .   ? 20.616  8.567   53.221  1.00 28.47 ? 1031 HOH B O   1 
HETATM 19959 O  O   . HOH X 4 .   ? 39.790  30.792  36.041  1.00 38.49 ? 1032 HOH B O   1 
HETATM 19960 O  O   . HOH X 4 .   ? 19.557  7.165   51.864  1.00 33.89 ? 1033 HOH B O   1 
HETATM 19961 O  O   . HOH X 4 .   ? 46.498  6.147   14.041  1.00 36.26 ? 1034 HOH B O   1 
HETATM 19962 O  O   . HOH X 4 .   ? 24.209  30.613  49.589  1.00 21.85 ? 1035 HOH B O   1 
HETATM 19963 O  O   . HOH X 4 .   ? 40.528  -12.900 37.891  1.00 45.36 ? 1036 HOH B O   1 
HETATM 19964 O  O   . HOH X 4 .   ? 33.935  9.652   33.560  1.00 14.72 ? 1037 HOH B O   1 
HETATM 19965 O  O   . HOH X 4 .   ? 5.822   18.017  23.879  1.00 29.81 ? 1038 HOH B O   1 
HETATM 19966 O  O   . HOH X 4 .   ? 40.318  2.888   13.026  1.00 25.14 ? 1039 HOH B O   1 
HETATM 19967 O  O   . HOH X 4 .   ? 10.590  9.610   33.272  1.00 11.33 ? 1040 HOH B O   1 
HETATM 19968 O  O   . HOH X 4 .   ? -4.659  13.595  38.348  1.00 40.22 ? 1041 HOH B O   1 
HETATM 19969 O  O   . HOH X 4 .   ? 40.738  -0.229  32.362  1.00 14.61 ? 1042 HOH B O   1 
HETATM 19970 O  O   . HOH X 4 .   ? 29.976  22.770  28.935  1.00 12.01 ? 1043 HOH B O   1 
HETATM 19971 O  O   . HOH X 4 .   ? 15.851  25.827  19.601  1.00 32.90 ? 1044 HOH B O   1 
HETATM 19972 O  O   . HOH X 4 .   ? 36.674  9.654   7.614   1.00 40.91 ? 1045 HOH B O   1 
HETATM 19973 O  O   . HOH X 4 .   ? 14.205  22.198  25.059  1.00 23.48 ? 1046 HOH B O   1 
HETATM 19974 O  O   . HOH X 4 .   ? 7.709   6.739   22.535  1.00 20.93 ? 1047 HOH B O   1 
HETATM 19975 O  O   . HOH X 4 .   ? 42.239  5.108   50.047  1.00 42.03 ? 1048 HOH B O   1 
HETATM 19976 O  O   . HOH X 4 .   ? 33.895  10.025  6.514   1.00 22.47 ? 1049 HOH B O   1 
HETATM 19977 O  O   . HOH X 4 .   ? 52.454  -14.107 30.699  1.00 25.07 ? 1050 HOH B O   1 
HETATM 19978 O  O   . HOH X 4 .   ? 8.200   18.255  25.713  1.00 16.71 ? 1051 HOH B O   1 
HETATM 19979 O  O   . HOH X 4 .   ? 30.474  4.398   44.892  1.00 16.07 ? 1052 HOH B O   1 
HETATM 19980 O  O   . HOH X 4 .   ? 53.154  1.203   36.659  1.00 16.62 ? 1053 HOH B O   1 
HETATM 19981 O  O   . HOH X 4 .   ? 36.061  16.237  35.251  1.00 16.35 ? 1054 HOH B O   1 
HETATM 19982 O  O   . HOH X 4 .   ? 31.694  17.342  5.151   1.00 48.24 ? 1055 HOH B O   1 
HETATM 19983 O  O   . HOH X 4 .   ? 21.876  16.069  46.208  1.00 28.20 ? 1056 HOH B O   1 
HETATM 19984 O  O   . HOH X 4 .   ? -5.350  -12.760 45.823  1.00 24.31 ? 1057 HOH B O   1 
HETATM 19985 O  O   . HOH X 4 .   ? 4.923   12.068  60.155  1.00 28.54 ? 1058 HOH B O   1 
HETATM 19986 O  O   . HOH X 4 .   ? -18.981 -8.829  60.884  1.00 37.28 ? 1059 HOH B O   1 
HETATM 19987 O  O   . HOH X 4 .   ? -11.263 1.333   64.817  1.00 33.12 ? 1060 HOH B O   1 
HETATM 19988 O  O   . HOH X 4 .   ? 43.989  25.425  34.147  1.00 23.25 ? 1061 HOH B O   1 
HETATM 19989 O  O   . HOH X 4 .   ? 23.774  28.607  21.039  1.00 32.47 ? 1062 HOH B O   1 
HETATM 19990 O  O   . HOH X 4 .   ? 9.990   30.114  35.073  1.00 26.84 ? 1063 HOH B O   1 
HETATM 19991 O  O   . HOH X 4 .   ? 9.492   16.921  23.575  1.00 13.05 ? 1064 HOH B O   1 
HETATM 19992 O  O   . HOH X 4 .   ? 37.767  -9.924  13.803  1.00 36.78 ? 1065 HOH B O   1 
HETATM 19993 O  O   . HOH X 4 .   ? 35.688  28.100  44.391  1.00 24.13 ? 1066 HOH B O   1 
HETATM 19994 O  O   . HOH X 4 .   ? 43.105  24.255  14.776  1.00 27.36 ? 1067 HOH B O   1 
HETATM 19995 O  O   . HOH X 4 .   ? -6.199  9.102   41.973  1.00 32.51 ? 1068 HOH B O   1 
HETATM 19996 O  O   . HOH X 4 .   ? 39.567  -9.133  25.133  1.00 44.81 ? 1069 HOH B O   1 
HETATM 19997 O  O   . HOH X 4 .   ? 54.822  5.903   41.879  1.00 20.79 ? 1070 HOH B O   1 
HETATM 19998 O  O   . HOH X 4 .   ? 40.395  -2.387  48.847  1.00 18.38 ? 1071 HOH B O   1 
HETATM 19999 O  O   . HOH X 4 .   ? 18.301  33.032  28.130  1.00 33.05 ? 1072 HOH B O   1 
HETATM 20000 O  O   . HOH X 4 .   ? 44.048  23.011  35.444  1.00 18.90 ? 1073 HOH B O   1 
HETATM 20001 O  O   . HOH X 4 .   ? 29.466  20.845  32.123  1.00 14.86 ? 1074 HOH B O   1 
HETATM 20002 O  O   . HOH X 4 .   ? 2.574   3.220   45.808  1.00 16.35 ? 1075 HOH B O   1 
HETATM 20003 O  O   . HOH X 4 .   ? 21.005  2.477   23.754  1.00 11.16 ? 1076 HOH B O   1 
HETATM 20004 O  O   . HOH X 4 .   ? 41.265  14.939  45.122  1.00 19.66 ? 1077 HOH B O   1 
HETATM 20005 O  O   . HOH X 4 .   ? 51.946  16.949  27.474  1.00 42.26 ? 1078 HOH B O   1 
HETATM 20006 O  O   . HOH X 4 .   ? 51.783  21.494  39.790  1.00 27.27 ? 1079 HOH B O   1 
HETATM 20007 O  O   . HOH X 4 .   ? -3.180  -1.626  34.699  1.00 11.34 ? 1080 HOH B O   1 
HETATM 20008 O  O   . HOH X 4 .   ? 29.065  27.811  23.089  1.00 38.89 ? 1081 HOH B O   1 
HETATM 20009 O  O   . HOH X 4 .   ? 37.633  18.196  35.761  1.00 24.45 ? 1082 HOH B O   1 
HETATM 20010 O  O   . HOH X 4 .   ? 30.398  21.771  41.676  1.00 23.72 ? 1083 HOH B O   1 
HETATM 20011 O  O   . HOH X 4 .   ? 53.627  22.795  39.122  1.00 34.44 ? 1084 HOH B O   1 
HETATM 20012 O  O   . HOH X 4 .   ? 47.436  -6.524  31.952  1.00 14.69 ? 1085 HOH B O   1 
HETATM 20013 O  O   . HOH X 4 .   ? 38.679  -8.988  32.701  1.00 25.56 ? 1086 HOH B O   1 
HETATM 20014 O  O   . HOH X 4 .   ? 4.658   -4.195  43.853  1.00 12.44 ? 1087 HOH B O   1 
HETATM 20015 O  O   . HOH X 4 .   ? 37.468  -9.397  22.687  1.00 34.92 ? 1088 HOH B O   1 
HETATM 20016 O  O   . HOH X 4 .   ? 16.868  4.916   49.531  1.00 26.83 ? 1089 HOH B O   1 
HETATM 20017 O  O   . HOH X 4 .   ? 46.036  -3.288  40.682  1.00 11.90 ? 1090 HOH B O   1 
HETATM 20018 O  O   . HOH X 4 .   ? 55.462  -8.553  33.734  1.00 15.65 ? 1091 HOH B O   1 
HETATM 20019 O  O   . HOH X 4 .   ? 17.771  1.220   29.494  1.00 16.44 ? 1092 HOH B O   1 
HETATM 20020 O  O   . HOH X 4 .   ? -1.131  -14.225 55.286  1.00 23.04 ? 1093 HOH B O   1 
HETATM 20021 O  O   . HOH X 4 .   ? 48.088  23.176  17.448  1.00 38.44 ? 1094 HOH B O   1 
HETATM 20022 O  O   . HOH X 4 .   ? 18.469  17.699  41.948  1.00 25.03 ? 1095 HOH B O   1 
HETATM 20023 O  O   . HOH X 4 .   ? -15.332 -0.776  37.740  1.00 28.42 ? 1096 HOH B O   1 
HETATM 20024 O  O   . HOH X 4 .   ? 51.363  -5.560  38.076  1.00 17.38 ? 1097 HOH B O   1 
HETATM 20025 O  O   . HOH X 4 .   ? 63.757  -2.179  37.045  1.00 28.38 ? 1098 HOH B O   1 
HETATM 20026 O  O   . HOH X 4 .   ? 5.361   2.512   45.732  1.00 16.56 ? 1099 HOH B O   1 
HETATM 20027 O  O   . HOH X 4 .   ? 31.887  44.366  41.331  1.00 41.40 ? 1100 HOH B O   1 
HETATM 20028 O  O   . HOH X 4 .   ? 33.870  37.330  32.837  1.00 27.07 ? 1101 HOH B O   1 
HETATM 20029 O  O   . HOH X 4 .   ? 2.692   15.867  38.657  1.00 20.81 ? 1102 HOH B O   1 
HETATM 20030 O  O   . HOH X 4 .   ? 44.392  17.874  13.308  1.00 26.32 ? 1103 HOH B O   1 
HETATM 20031 O  O   . HOH X 4 .   ? 8.683   32.499  42.981  1.00 42.39 ? 1104 HOH B O   1 
HETATM 20032 O  O   . HOH X 4 .   ? -9.773  12.159  58.294  1.00 38.68 ? 1105 HOH B O   1 
HETATM 20033 O  O   . HOH X 4 .   ? 27.381  41.600  48.475  1.00 47.27 ? 1106 HOH B O   1 
HETATM 20034 O  O   . HOH X 4 .   ? 11.194  10.315  47.431  1.00 17.08 ? 1107 HOH B O   1 
HETATM 20035 O  O   . HOH X 4 .   ? 6.638   -3.887  61.784  1.00 40.42 ? 1108 HOH B O   1 
HETATM 20036 O  O   . HOH X 4 .   ? -1.789  5.959   47.507  1.00 14.94 ? 1109 HOH B O   1 
HETATM 20037 O  O   . HOH X 4 .   ? 42.051  -4.686  49.147  1.00 29.89 ? 1110 HOH B O   1 
HETATM 20038 O  O   . HOH X 4 .   ? 56.786  -6.285  33.615  1.00 19.18 ? 1111 HOH B O   1 
HETATM 20039 O  O   . HOH X 4 .   ? 64.933  3.662   27.941  1.00 31.24 ? 1112 HOH B O   1 
HETATM 20040 O  O   . HOH X 4 .   ? 52.522  12.477  19.395  1.00 37.59 ? 1113 HOH B O   1 
HETATM 20041 O  O   . HOH X 4 .   ? 35.592  5.163   40.879  1.00 15.17 ? 1114 HOH B O   1 
HETATM 20042 O  O   . HOH X 4 .   ? 26.943  33.665  28.944  1.00 35.04 ? 1115 HOH B O   1 
HETATM 20043 O  O   . HOH X 4 .   ? 7.146   16.786  52.635  1.00 24.10 ? 1116 HOH B O   1 
HETATM 20044 O  O   . HOH X 4 .   ? -7.361  -16.672 53.843  1.00 43.40 ? 1117 HOH B O   1 
HETATM 20045 O  O   . HOH X 4 .   ? 36.470  4.294   11.166  1.00 31.81 ? 1118 HOH B O   1 
HETATM 20046 O  O   . HOH X 4 .   ? 23.361  26.645  22.903  1.00 26.55 ? 1119 HOH B O   1 
HETATM 20047 O  O   . HOH X 4 .   ? 2.064   4.014   29.913  1.00 10.43 ? 1120 HOH B O   1 
HETATM 20048 O  O   . HOH X 4 .   ? -4.249  -8.513  25.230  1.00 34.44 ? 1121 HOH B O   1 
HETATM 20049 O  O   . HOH X 4 .   ? 38.241  20.865  39.818  1.00 15.96 ? 1122 HOH B O   1 
HETATM 20050 O  O   . HOH X 4 .   ? 33.196  11.724  48.822  1.00 36.52 ? 1123 HOH B O   1 
HETATM 20051 O  O   A HOH X 4 .   ? 37.032  23.175  11.806  0.57 16.69 ? 1124 HOH B O   1 
HETATM 20052 O  O   B HOH X 4 .   ? 37.568  21.619  11.587  0.43 16.97 ? 1124 HOH B O   1 
HETATM 20053 O  O   . HOH X 4 .   ? 5.035   17.972  28.708  1.00 30.41 ? 1125 HOH B O   1 
HETATM 20054 O  O   . HOH X 4 .   ? -8.630  -4.741  64.888  1.00 41.83 ? 1126 HOH B O   1 
HETATM 20055 O  O   . HOH X 4 .   ? 17.835  17.827  47.169  1.00 37.13 ? 1127 HOH B O   1 
HETATM 20056 O  O   . HOH X 4 .   ? 37.295  29.148  35.770  1.00 22.12 ? 1128 HOH B O   1 
HETATM 20057 O  O   A HOH X 4 .   ? 28.059  -8.660  17.669  0.67 9.03  ? 1129 HOH B O   1 
HETATM 20058 O  O   B HOH X 4 .   ? 29.537  -7.330  17.560  0.33 8.29  ? 1129 HOH B O   1 
HETATM 20059 O  O   . HOH X 4 .   ? 44.529  2.398   49.350  1.00 41.12 ? 1130 HOH B O   1 
HETATM 20060 O  O   . HOH X 4 .   ? 20.475  22.655  42.706  1.00 23.35 ? 1131 HOH B O   1 
HETATM 20061 O  O   . HOH X 4 .   ? -1.901  -6.740  66.541  1.00 31.00 ? 1132 HOH B O   1 
HETATM 20062 O  O   . HOH X 4 .   ? 47.386  -8.415  44.535  1.00 29.53 ? 1133 HOH B O   1 
HETATM 20063 O  O   . HOH X 4 .   ? 49.415  21.337  17.531  1.00 34.16 ? 1134 HOH B O   1 
HETATM 20064 O  O   . HOH X 4 .   ? -14.168 6.627   47.648  1.00 25.12 ? 1135 HOH B O   1 
HETATM 20065 O  O   . HOH X 4 .   ? 61.380  8.860   31.889  1.00 41.33 ? 1136 HOH B O   1 
HETATM 20066 O  O   . HOH X 4 .   ? 22.276  15.277  43.436  1.00 31.19 ? 1137 HOH B O   1 
HETATM 20067 O  O   . HOH X 4 .   ? 33.925  4.533   12.469  1.00 23.54 ? 1138 HOH B O   1 
HETATM 20068 O  O   . HOH X 4 .   ? 9.888   8.894   59.408  1.00 37.81 ? 1139 HOH B O   1 
HETATM 20069 O  O   . HOH X 4 .   ? -2.841  -11.071 55.516  1.00 18.06 ? 1140 HOH B O   1 
HETATM 20070 O  O   . HOH X 4 .   ? 10.829  30.442  41.702  1.00 37.89 ? 1141 HOH B O   1 
HETATM 20071 O  O   . HOH X 4 .   ? -16.636 -4.320  30.814  1.00 17.59 ? 1142 HOH B O   1 
HETATM 20072 O  O   . HOH X 4 .   ? -10.791 5.756   28.056  1.00 19.63 ? 1143 HOH B O   1 
HETATM 20073 O  O   . HOH X 4 .   ? 10.939  28.016  38.999  1.00 18.65 ? 1144 HOH B O   1 
HETATM 20074 O  O   . HOH X 4 .   ? 4.860   28.363  39.636  1.00 25.07 ? 1145 HOH B O   1 
HETATM 20075 O  O   . HOH X 4 .   ? 9.692   9.953   55.902  1.00 35.26 ? 1146 HOH B O   1 
HETATM 20076 O  O   . HOH X 4 .   ? -1.930  -5.523  42.484  1.00 12.94 ? 1147 HOH B O   1 
HETATM 20077 O  O   . HOH X 4 .   ? -9.695  -10.073 41.403  1.00 33.20 ? 1148 HOH B O   1 
HETATM 20078 O  O   . HOH X 4 .   ? -8.070  6.921   44.377  1.00 19.81 ? 1149 HOH B O   1 
HETATM 20079 O  O   . HOH X 4 .   ? -2.125  8.960   60.078  1.00 24.89 ? 1150 HOH B O   1 
HETATM 20080 O  O   . HOH X 4 .   ? 10.557  -0.123  33.783  1.00 15.14 ? 1151 HOH B O   1 
HETATM 20081 O  O   . HOH X 4 .   ? -7.439  -8.618  36.617  1.00 20.72 ? 1152 HOH B O   1 
HETATM 20082 O  O   . HOH X 4 .   ? 10.668  -3.234  56.719  1.00 42.08 ? 1153 HOH B O   1 
HETATM 20083 O  O   . HOH X 4 .   ? 12.637  -1.226  62.704  1.00 24.56 ? 1154 HOH B O   1 
HETATM 20084 O  O   . HOH X 4 .   ? 27.138  -1.829  27.835  1.00 18.91 ? 1155 HOH B O   1 
HETATM 20085 O  O   . HOH X 4 .   ? 49.871  18.259  21.979  1.00 38.27 ? 1156 HOH B O   1 
HETATM 20086 O  O   . HOH X 4 .   ? 38.905  -7.970  47.005  1.00 15.67 ? 1157 HOH B O   1 
HETATM 20087 O  O   . HOH X 4 .   ? 8.980   29.064  37.617  1.00 20.41 ? 1158 HOH B O   1 
HETATM 20088 O  O   . HOH X 4 .   ? 7.709   25.208  28.371  1.00 28.45 ? 1159 HOH B O   1 
HETATM 20089 O  O   . HOH X 4 .   ? 32.018  20.004  10.472  1.00 18.88 ? 1160 HOH B O   1 
HETATM 20090 O  O   . HOH X 4 .   ? 38.015  16.132  48.105  1.00 44.30 ? 1161 HOH B O   1 
HETATM 20091 O  O   . HOH X 4 .   ? 42.146  2.377   21.182  1.00 17.52 ? 1162 HOH B O   1 
HETATM 20092 O  O   . HOH X 4 .   ? 55.867  1.763   36.183  1.00 16.14 ? 1163 HOH B O   1 
HETATM 20093 O  O   . HOH X 4 .   ? 2.416   -0.903  36.560  1.00 14.28 ? 1164 HOH B O   1 
HETATM 20094 O  O   . HOH X 4 .   ? 62.794  -0.725  21.516  1.00 43.54 ? 1165 HOH B O   1 
HETATM 20095 O  O   . HOH X 4 .   ? 26.902  14.241  3.082   1.00 26.26 ? 1166 HOH B O   1 
HETATM 20096 O  O   . HOH X 4 .   ? 16.831  0.342   48.625  1.00 21.68 ? 1167 HOH B O   1 
HETATM 20097 O  O   . HOH X 4 .   ? 25.522  13.933  44.955  1.00 37.22 ? 1168 HOH B O   1 
HETATM 20098 O  O   . HOH X 4 .   ? 54.125  -15.471 26.606  1.00 37.32 ? 1169 HOH B O   1 
HETATM 20099 O  O   . HOH X 4 .   ? -1.611  6.328   60.081  1.00 23.94 ? 1170 HOH B O   1 
HETATM 20100 O  O   . HOH X 4 .   ? -5.872  8.420   27.793  1.00 41.19 ? 1171 HOH B O   1 
HETATM 20101 O  O   . HOH X 4 .   ? 50.637  -13.824 33.168  1.00 28.61 ? 1172 HOH B O   1 
HETATM 20102 O  O   . HOH X 4 .   ? 6.771   4.659   65.612  1.00 40.58 ? 1173 HOH B O   1 
HETATM 20103 O  O   . HOH X 4 .   ? 12.643  10.288  50.310  1.00 44.23 ? 1174 HOH B O   1 
HETATM 20104 O  O   . HOH X 4 .   ? 45.851  -11.675 25.262  1.00 39.91 ? 1175 HOH B O   1 
HETATM 20105 O  O   . HOH X 4 .   ? -2.174  10.080  33.118  1.00 20.88 ? 1176 HOH B O   1 
HETATM 20106 O  O   . HOH X 4 .   ? 50.276  22.688  37.164  1.00 26.98 ? 1177 HOH B O   1 
HETATM 20107 O  O   . HOH X 4 .   ? -3.814  5.492   33.646  1.00 18.49 ? 1178 HOH B O   1 
HETATM 20108 O  O   . HOH X 4 .   ? 34.677  14.313  42.690  1.00 26.38 ? 1179 HOH B O   1 
HETATM 20109 O  O   . HOH X 4 .   ? -10.011 8.002   59.440  1.00 24.02 ? 1180 HOH B O   1 
HETATM 20110 O  O   . HOH X 4 .   ? 29.300  19.113  40.674  1.00 20.26 ? 1181 HOH B O   1 
HETATM 20111 O  O   . HOH X 4 .   ? 51.757  -12.558 28.290  1.00 29.12 ? 1182 HOH B O   1 
HETATM 20112 O  O   . HOH X 4 .   ? 0.802   12.916  29.894  1.00 8.18  ? 1183 HOH B O   1 
HETATM 20113 O  O   . HOH X 4 .   ? -2.947  9.993   25.509  1.00 42.31 ? 1184 HOH B O   1 
HETATM 20114 O  O   . HOH X 4 .   ? 35.226  3.600   47.170  1.00 20.88 ? 1185 HOH B O   1 
HETATM 20115 O  O   . HOH X 4 .   ? 6.875   29.897  39.131  1.00 26.64 ? 1186 HOH B O   1 
HETATM 20116 O  O   . HOH X 4 .   ? 27.994  27.574  14.066  1.00 35.81 ? 1187 HOH B O   1 
HETATM 20117 O  O   . HOH X 4 .   ? 32.811  40.144  47.056  1.00 39.53 ? 1188 HOH B O   1 
HETATM 20118 O  O   . HOH X 4 .   ? 10.255  0.047   66.289  1.00 23.93 ? 1189 HOH B O   1 
HETATM 20119 O  O   . HOH X 4 .   ? 27.448  38.232  30.198  1.00 37.09 ? 1190 HOH B O   1 
HETATM 20120 O  O   . HOH X 4 .   ? 0.375   -5.209  65.738  1.00 21.56 ? 1191 HOH B O   1 
HETATM 20121 O  O   . HOH X 4 .   ? 46.165  13.770  11.816  1.00 23.48 ? 1192 HOH B O   1 
HETATM 20122 O  O   . HOH X 4 .   ? 58.486  -10.151 22.625  1.00 33.51 ? 1193 HOH B O   1 
HETATM 20123 O  O   . HOH X 4 .   ? 27.445  24.190  25.107  1.00 18.20 ? 1194 HOH B O   1 
HETATM 20124 O  O   . HOH X 4 .   ? 29.329  16.354  40.954  1.00 26.90 ? 1195 HOH B O   1 
HETATM 20125 O  O   . HOH X 4 .   ? -18.138 -0.936  41.376  1.00 16.93 ? 1196 HOH B O   1 
HETATM 20126 O  O   . HOH X 4 .   ? 49.675  16.546  44.264  1.00 40.25 ? 1197 HOH B O   1 
HETATM 20127 O  O   . HOH X 4 .   ? 13.394  23.379  55.389  1.00 26.65 ? 1198 HOH B O   1 
HETATM 20128 O  O   . HOH X 4 .   ? -6.443  17.731  62.643  1.00 35.56 ? 1199 HOH B O   1 
HETATM 20129 O  O   . HOH X 4 .   ? -4.866  -11.294 36.084  1.00 17.80 ? 1200 HOH B O   1 
HETATM 20130 O  O   . HOH X 4 .   ? 32.503  1.195   45.459  1.00 29.46 ? 1201 HOH B O   1 
HETATM 20131 O  O   . HOH X 4 .   ? 37.079  9.957   10.554  1.00 15.68 ? 1202 HOH B O   1 
HETATM 20132 O  O   . HOH X 4 .   ? -6.166  -10.262 41.367  1.00 22.14 ? 1203 HOH B O   1 
HETATM 20133 O  O   . HOH X 4 .   ? 4.239   17.883  56.183  1.00 44.04 ? 1204 HOH B O   1 
HETATM 20134 O  O   . HOH X 4 .   ? -3.717  20.146  32.482  1.00 29.58 ? 1205 HOH B O   1 
HETATM 20135 O  O   . HOH X 4 .   ? 43.172  25.454  45.387  1.00 21.41 ? 1206 HOH B O   1 
HETATM 20136 O  O   . HOH X 4 .   ? -14.076 5.475   30.312  1.00 28.78 ? 1207 HOH B O   1 
HETATM 20137 O  O   . HOH X 4 .   ? 30.533  27.897  37.125  1.00 23.13 ? 1208 HOH B O   1 
HETATM 20138 O  O   . HOH X 4 .   ? 0.004   -10.407 60.172  1.00 31.18 ? 1209 HOH B O   1 
HETATM 20139 O  O   . HOH X 4 .   ? 3.605   5.931   21.496  1.00 30.56 ? 1210 HOH B O   1 
HETATM 20140 O  O   . HOH X 4 .   ? 37.266  7.162   8.097   1.00 40.42 ? 1211 HOH B O   1 
HETATM 20141 O  O   . HOH X 4 .   ? 50.287  17.015  24.476  1.00 38.94 ? 1212 HOH B O   1 
HETATM 20142 O  O   . HOH X 4 .   ? 41.824  37.182  37.507  1.00 34.12 ? 1213 HOH B O   1 
HETATM 20143 O  O   . HOH X 4 .   ? -4.510  15.601  63.679  1.00 31.21 ? 1214 HOH B O   1 
HETATM 20144 O  O   . HOH X 4 .   ? -19.622 -3.458  42.089  1.00 16.53 ? 1215 HOH B O   1 
HETATM 20145 O  O   . HOH X 4 .   ? 8.570   18.805  53.805  1.00 33.04 ? 1216 HOH B O   1 
HETATM 20146 O  O   . HOH X 4 .   ? -5.700  -10.527 24.557  1.00 37.83 ? 1217 HOH B O   1 
HETATM 20147 O  O   . HOH X 4 .   ? 19.259  38.187  37.970  1.00 37.47 ? 1218 HOH B O   1 
HETATM 20148 O  O   . HOH X 4 .   ? 41.987  16.906  46.938  1.00 44.18 ? 1219 HOH B O   1 
HETATM 20149 O  O   . HOH X 4 .   ? 18.598  33.759  38.854  1.00 32.52 ? 1220 HOH B O   1 
HETATM 20150 O  O   . HOH X 4 .   ? -4.906  -12.323 42.998  1.00 23.85 ? 1221 HOH B O   1 
HETATM 20151 O  O   . HOH X 4 .   ? 33.925  31.815  45.835  1.00 41.18 ? 1222 HOH B O   1 
HETATM 20152 O  O   . HOH X 4 .   ? 12.756  23.713  22.204  1.00 38.48 ? 1223 HOH B O   1 
HETATM 20153 O  O   . HOH X 4 .   ? -15.880 0.750   58.916  1.00 31.71 ? 1224 HOH B O   1 
HETATM 20154 O  O   . HOH X 4 .   ? 49.013  -4.776  47.383  1.00 31.85 ? 1225 HOH B O   1 
HETATM 20155 O  O   . HOH X 4 .   ? 52.233  -5.744  18.405  1.00 29.66 ? 1226 HOH B O   1 
HETATM 20156 O  O   . HOH X 4 .   ? 11.394  8.261   56.052  1.00 31.45 ? 1227 HOH B O   1 
HETATM 20157 O  O   . HOH X 4 .   ? -7.844  8.349   30.880  1.00 50.74 ? 1228 HOH B O   1 
HETATM 20158 O  O   . HOH X 4 .   ? 14.227  -0.904  54.779  1.00 44.81 ? 1229 HOH B O   1 
HETATM 20159 O  O   . HOH X 4 .   ? 12.241  -4.009  34.659  1.00 25.07 ? 1230 HOH B O   1 
HETATM 20160 O  O   . HOH X 4 .   ? -1.747  -10.318 58.181  1.00 31.72 ? 1231 HOH B O   1 
HETATM 20161 O  O   . HOH X 4 .   ? 33.590  24.208  45.311  1.00 25.87 ? 1232 HOH B O   1 
HETATM 20162 O  O   . HOH X 4 .   ? 33.576  6.738   10.597  1.00 15.36 ? 1233 HOH B O   1 
HETATM 20163 O  O   . HOH X 4 .   ? 20.563  20.017  42.541  1.00 27.99 ? 1234 HOH B O   1 
HETATM 20164 O  O   . HOH X 4 .   ? 19.933  16.948  15.144  1.00 29.04 ? 1235 HOH B O   1 
HETATM 20165 O  O   . HOH X 4 .   ? 30.877  23.030  11.136  1.00 35.07 ? 1236 HOH B O   1 
HETATM 20166 O  O   . HOH X 4 .   ? 3.450   28.113  51.151  1.00 45.41 ? 1237 HOH B O   1 
HETATM 20167 O  O   . HOH X 4 .   ? 50.242  5.052   47.899  1.00 21.66 ? 1238 HOH B O   1 
HETATM 20168 O  O   . HOH X 4 .   ? 32.458  12.995  44.327  1.00 28.83 ? 1239 HOH B O   1 
HETATM 20169 O  O   . HOH X 4 .   ? 29.429  17.634  36.778  1.00 16.28 ? 1240 HOH B O   1 
HETATM 20170 O  O   . HOH X 4 .   ? 47.223  -12.789 32.209  1.00 21.72 ? 1241 HOH B O   1 
HETATM 20171 O  O   . HOH X 4 .   ? 37.723  -0.786  21.804  1.00 18.51 ? 1242 HOH B O   1 
HETATM 20172 O  O   . HOH X 4 .   ? -13.499 6.395   58.576  1.00 37.00 ? 1243 HOH B O   1 
HETATM 20173 O  O   . HOH X 4 .   ? 50.796  7.624   45.874  1.00 15.62 ? 1244 HOH B O   1 
HETATM 20174 O  O   . HOH X 4 .   ? 25.200  4.562   51.627  1.00 34.23 ? 1245 HOH B O   1 
HETATM 20175 O  O   . HOH X 4 .   ? 0.641   13.257  26.691  1.00 23.35 ? 1246 HOH B O   1 
HETATM 20176 O  O   . HOH X 4 .   ? 29.054  11.154  47.970  1.00 39.93 ? 1247 HOH B O   1 
HETATM 20177 O  O   . HOH X 4 .   ? -2.763  10.616  40.004  1.00 31.41 ? 1248 HOH B O   1 
HETATM 20178 O  O   . HOH X 4 .   ? 18.050  29.676  51.790  1.00 17.78 ? 1249 HOH B O   1 
HETATM 20179 O  O   . HOH X 4 .   ? 17.236  27.912  34.578  1.00 39.07 ? 1250 HOH B O   1 
HETATM 20180 O  O   . HOH X 4 .   ? 34.027  26.456  43.709  1.00 24.00 ? 1251 HOH B O   1 
HETATM 20181 O  O   . HOH X 4 .   ? -0.178  17.420  40.791  1.00 45.19 ? 1252 HOH B O   1 
HETATM 20182 O  O   . HOH X 4 .   ? -5.447  7.771   60.875  1.00 32.86 ? 1253 HOH B O   1 
HETATM 20183 O  O   . HOH X 4 .   ? 59.389  11.625  26.554  1.00 38.57 ? 1254 HOH B O   1 
HETATM 20184 O  O   . HOH X 4 .   ? 45.012  -6.643  44.165  1.00 17.25 ? 1255 HOH B O   1 
HETATM 20185 O  O   . HOH X 4 .   ? 42.583  28.520  31.449  1.00 41.27 ? 1256 HOH B O   1 
HETATM 20186 O  O   . HOH X 4 .   ? -6.883  16.301  52.104  1.00 46.56 ? 1257 HOH B O   1 
HETATM 20187 O  O   . HOH X 4 .   ? 35.664  -6.757  54.062  1.00 34.99 ? 1258 HOH B O   1 
HETATM 20188 O  O   . HOH X 4 .   ? -2.066  -11.933 28.869  1.00 28.22 ? 1259 HOH B O   1 
HETATM 20189 O  O   . HOH X 4 .   ? -0.090  -16.640 44.907  1.00 43.10 ? 1260 HOH B O   1 
HETATM 20190 O  O   . HOH X 4 .   ? -9.602  -8.965  22.404  1.00 33.25 ? 1261 HOH B O   1 
HETATM 20191 O  O   . HOH X 4 .   ? 14.146  1.329   47.950  1.00 40.34 ? 1262 HOH B O   1 
HETATM 20192 O  O   . HOH X 4 .   ? 33.049  -3.159  26.814  1.00 46.08 ? 1263 HOH B O   1 
HETATM 20193 O  O   . HOH X 4 .   ? 28.735  25.974  36.992  1.00 24.25 ? 1264 HOH B O   1 
HETATM 20194 O  O   . HOH X 4 .   ? 40.296  -11.495 25.522  1.00 37.89 ? 1265 HOH B O   1 
HETATM 20195 O  O   . HOH X 4 .   ? -2.355  6.011   19.636  1.00 42.86 ? 1266 HOH B O   1 
HETATM 20196 O  O   . HOH X 4 .   ? 16.649  29.173  19.120  1.00 35.20 ? 1267 HOH B O   1 
HETATM 20197 O  O   . HOH X 4 .   ? 3.199   -14.584 37.861  1.00 30.19 ? 1268 HOH B O   1 
HETATM 20198 O  O   . HOH X 4 .   ? 62.686  5.596   27.158  1.00 49.95 ? 1269 HOH B O   1 
HETATM 20199 O  O   . HOH X 4 .   ? 42.076  26.718  22.067  1.00 18.99 ? 1270 HOH B O   1 
HETATM 20200 O  O   . HOH X 4 .   ? -8.722  -11.235 24.098  1.00 37.17 ? 1271 HOH B O   1 
HETATM 20201 O  O   . HOH X 4 .   ? 32.128  -6.207  53.305  1.00 24.55 ? 1272 HOH B O   1 
HETATM 20202 O  O   . HOH X 4 .   ? 27.749  5.170   50.947  1.00 30.71 ? 1273 HOH B O   1 
HETATM 20203 O  O   . HOH X 4 .   ? 44.874  33.077  37.617  1.00 42.70 ? 1274 HOH B O   1 
HETATM 20204 O  O   A HOH X 4 .   ? 19.843  18.740  44.988  0.52 18.65 ? 1275 HOH B O   1 
HETATM 20205 O  O   B HOH X 4 .   ? 18.798  20.005  46.053  0.48 19.22 ? 1275 HOH B O   1 
HETATM 20206 O  O   . HOH X 4 .   ? 15.573  3.135   24.017  1.00 13.59 ? 1276 HOH B O   1 
HETATM 20207 O  O   . HOH X 4 .   ? 50.572  -11.766 36.558  1.00 28.39 ? 1277 HOH B O   1 
HETATM 20208 O  O   . HOH X 4 .   ? 36.061  -9.389  34.896  1.00 29.43 ? 1278 HOH B O   1 
HETATM 20209 O  O   A HOH X 4 .   ? 7.452   -13.772 40.237  0.59 14.67 ? 1279 HOH B O   1 
HETATM 20210 O  O   B HOH X 4 .   ? 6.057   -14.119 38.741  0.41 12.81 ? 1279 HOH B O   1 
HETATM 20211 O  O   . HOH X 4 .   ? 50.562  28.524  34.926  1.00 40.54 ? 1280 HOH B O   1 
HETATM 20212 O  O   . HOH X 4 .   ? 34.451  -0.340  20.971  1.00 22.64 ? 1281 HOH B O   1 
HETATM 20213 O  O   . HOH X 4 .   ? 23.076  30.846  23.534  1.00 49.13 ? 1282 HOH B O   1 
HETATM 20214 O  O   . HOH X 4 .   ? 50.796  -8.343  38.442  1.00 24.54 ? 1283 HOH B O   1 
HETATM 20215 O  O   . HOH X 4 .   ? 30.251  13.517  45.677  1.00 32.85 ? 1284 HOH B O   1 
HETATM 20216 O  O   . HOH X 4 .   ? 4.857   16.747  54.057  1.00 25.59 ? 1285 HOH B O   1 
HETATM 20217 O  O   A HOH X 4 .   ? 46.405  23.528  30.512  0.52 21.77 ? 1286 HOH B O   1 
HETATM 20218 O  O   B HOH X 4 .   ? 45.110  24.984  30.917  0.48 25.51 ? 1286 HOH B O   1 
HETATM 20219 O  O   . HOH X 4 .   ? 4.349   25.514  58.323  1.00 43.72 ? 1287 HOH B O   1 
HETATM 20220 O  O   . HOH X 4 .   ? -3.136  14.776  31.991  1.00 36.41 ? 1288 HOH B O   1 
HETATM 20221 O  O   . HOH X 4 .   ? -5.062  9.420   30.011  1.00 40.35 ? 1289 HOH B O   1 
HETATM 20222 O  O   . HOH X 4 .   ? 4.344   -4.458  60.093  1.00 37.95 ? 1290 HOH B O   1 
HETATM 20223 O  O   . HOH X 4 .   ? 34.521  -2.832  22.175  1.00 23.99 ? 1291 HOH B O   1 
HETATM 20224 O  O   . HOH X 4 .   ? 49.191  11.226  10.071  1.00 43.58 ? 1292 HOH B O   1 
HETATM 20225 O  O   . HOH X 4 .   ? 26.156  26.603  24.309  1.00 24.39 ? 1293 HOH B O   1 
HETATM 20226 O  O   . HOH X 4 .   ? 4.043   -4.080  46.496  1.00 18.80 ? 1294 HOH B O   1 
HETATM 20227 O  O   . HOH X 4 .   ? 41.117  26.517  15.087  1.00 36.81 ? 1295 HOH B O   1 
HETATM 20228 O  O   . HOH X 4 .   ? 40.480  29.451  31.809  1.00 41.56 ? 1296 HOH B O   1 
HETATM 20229 O  O   . HOH X 4 .   ? 48.765  21.269  34.791  1.00 34.64 ? 1297 HOH B O   1 
HETATM 20230 O  O   . HOH X 4 .   ? 7.375   32.002  30.365  1.00 29.62 ? 1298 HOH B O   1 
HETATM 20231 O  O   . HOH X 4 .   ? -20.144 -4.959  40.009  1.00 27.28 ? 1299 HOH B O   1 
HETATM 20232 O  O   . HOH X 4 .   ? 29.345  20.766  9.368   1.00 54.14 ? 1300 HOH B O   1 
HETATM 20233 O  O   . HOH X 4 .   ? 32.805  -4.563  55.666  1.00 26.02 ? 1301 HOH B O   1 
HETATM 20234 O  O   A HOH X 4 .   ? 46.826  19.143  12.403  0.50 21.89 ? 1302 HOH B O   1 
HETATM 20235 O  O   B HOH X 4 .   ? 48.475  19.608  13.299  0.50 21.29 ? 1302 HOH B O   1 
HETATM 20236 O  O   . HOH X 4 .   ? 37.725  32.734  35.745  1.00 35.91 ? 1303 HOH B O   1 
HETATM 20237 O  O   . HOH X 4 .   ? 37.480  1.027   8.278   1.00 48.07 ? 1304 HOH B O   1 
HETATM 20238 O  O   . HOH X 4 .   ? 7.263   -3.250  66.846  1.00 39.06 ? 1305 HOH B O   1 
HETATM 20239 O  O   . HOH X 4 .   ? 24.355  32.730  27.835  1.00 36.98 ? 1306 HOH B O   1 
HETATM 20240 O  O   . HOH X 4 .   ? 17.475  31.930  31.203  1.00 30.09 ? 1307 HOH B O   1 
HETATM 20241 O  O   . HOH X 4 .   ? 47.564  13.644  46.851  1.00 44.36 ? 1308 HOH B O   1 
HETATM 20242 O  O   . HOH X 4 .   ? 51.669  -13.439 25.624  1.00 44.01 ? 1309 HOH B O   1 
HETATM 20243 O  O   . HOH X 4 .   ? -5.392  12.970  64.601  1.00 40.12 ? 1310 HOH B O   1 
HETATM 20244 O  O   A HOH X 4 .   ? 47.128  10.605  47.008  0.47 16.58 ? 1311 HOH B O   1 
HETATM 20245 O  O   B HOH X 4 .   ? 48.441  10.171  45.518  0.53 16.65 ? 1311 HOH B O   1 
HETATM 20246 O  O   . HOH X 4 .   ? 42.101  -10.892 42.891  1.00 29.45 ? 1312 HOH B O   1 
HETATM 20247 O  O   . HOH X 4 .   ? -8.077  8.110   61.501  1.00 38.72 ? 1313 HOH B O   1 
HETATM 20248 O  O   . HOH X 4 .   ? 41.827  -0.078  48.840  1.00 15.03 ? 1314 HOH B O   1 
HETATM 20249 O  O   . HOH X 4 .   ? 37.934  4.368   7.650   1.00 43.34 ? 1315 HOH B O   1 
HETATM 20250 O  O   . HOH X 4 .   ? 35.644  16.399  46.586  1.00 54.99 ? 1316 HOH B O   1 
HETATM 20251 O  O   . HOH X 4 .   ? 45.989  21.680  34.348  1.00 26.22 ? 1317 HOH B O   1 
HETATM 20252 O  O   . HOH X 4 .   ? -2.061  12.525  31.402  1.00 24.77 ? 1318 HOH B O   1 
HETATM 20253 O  O   . HOH X 4 .   ? 55.793  -5.839  36.403  1.00 25.80 ? 1319 HOH B O   1 
HETATM 20254 O  O   . HOH X 4 .   ? -12.257 5.195   34.335  1.00 37.95 ? 1320 HOH B O   1 
HETATM 20255 O  O   . HOH X 4 .   ? 4.385   4.531   65.726  1.00 43.23 ? 1321 HOH B O   1 
HETATM 20256 O  O   . HOH X 4 .   ? 18.187  36.046  43.046  1.00 33.05 ? 1322 HOH B O   1 
HETATM 20257 O  O   . HOH X 4 .   ? 34.748  8.494   4.388   1.00 34.83 ? 1323 HOH B O   1 
HETATM 20258 O  O   . HOH X 4 .   ? 32.930  -6.593  28.588  1.00 36.49 ? 1324 HOH B O   1 
HETATM 20259 O  O   . HOH X 4 .   ? 53.451  7.528   45.216  1.00 43.31 ? 1325 HOH B O   1 
HETATM 20260 O  O   . HOH X 4 .   ? 7.548   11.574  60.342  1.00 38.98 ? 1326 HOH B O   1 
HETATM 20261 O  O   . HOH X 4 .   ? 34.130  21.368  9.328   1.00 45.69 ? 1327 HOH B O   1 
HETATM 20262 O  O   . HOH X 4 .   ? 24.693  12.770  48.618  1.00 32.81 ? 1328 HOH B O   1 
HETATM 20263 O  O   . HOH X 4 .   ? 28.030  5.236   45.582  1.00 20.55 ? 1329 HOH B O   1 
HETATM 20264 O  O   . HOH X 4 .   ? 34.115  6.022   8.028   1.00 35.74 ? 1330 HOH B O   1 
HETATM 20265 O  O   . HOH X 4 .   ? -4.287  7.893   32.437  1.00 20.96 ? 1331 HOH B O   1 
HETATM 20266 O  O   . HOH X 4 .   ? -13.819 6.618   32.573  1.00 41.73 ? 1332 HOH B O   1 
HETATM 20267 O  O   . HOH X 4 .   ? 42.462  23.085  12.428  1.00 36.71 ? 1333 HOH B O   1 
HETATM 20268 O  O   . HOH X 4 .   ? 43.748  -0.152  51.128  1.00 39.27 ? 1334 HOH B O   1 
HETATM 20269 O  O   . HOH X 4 .   ? 20.244  0.092   48.690  1.00 43.48 ? 1335 HOH B O   1 
HETATM 20270 O  O   . HOH X 4 .   ? 1.000   -1.279  67.237  1.00 35.58 ? 1336 HOH B O   1 
HETATM 20271 O  O   . HOH X 4 .   ? 63.577  1.979   38.058  1.00 28.24 ? 1337 HOH B O   1 
HETATM 20272 O  O   . HOH X 4 .   ? -4.430  -13.287 34.890  1.00 43.85 ? 1338 HOH B O   1 
HETATM 20273 O  O   . HOH X 4 .   ? 30.720  3.007   47.167  1.00 26.10 ? 1339 HOH B O   1 
HETATM 20274 O  O   . HOH X 4 .   ? -3.938  9.472   61.916  1.00 25.60 ? 1340 HOH B O   1 
HETATM 20275 O  O   . HOH X 4 .   ? -6.970  5.704   35.732  1.00 27.76 ? 1341 HOH B O   1 
HETATM 20276 O  O   . HOH X 4 .   ? -22.472 -4.766  36.973  1.00 32.93 ? 1342 HOH B O   1 
HETATM 20277 O  O   . HOH X 4 .   ? 16.118  32.947  41.641  1.00 47.57 ? 1343 HOH B O   1 
HETATM 20278 O  O   . HOH X 4 .   ? 27.118  9.729   46.843  1.00 21.13 ? 1344 HOH B O   1 
HETATM 20279 O  O   . HOH X 4 .   ? 42.430  19.477  12.350  1.00 43.96 ? 1345 HOH B O   1 
HETATM 20280 O  O   . HOH X 4 .   ? 37.214  2.512   9.935   1.00 22.04 ? 1346 HOH B O   1 
HETATM 20281 O  O   . HOH X 4 .   ? 4.936   21.273  23.915  1.00 36.57 ? 1347 HOH B O   1 
HETATM 20282 O  O   . HOH X 4 .   ? 46.487  23.408  45.773  1.00 31.64 ? 1348 HOH B O   1 
HETATM 20283 O  O   . HOH X 4 .   ? 49.837  13.791  44.155  1.00 36.69 ? 1349 HOH B O   1 
HETATM 20284 O  O   . HOH X 4 .   ? 25.018  11.117  50.886  1.00 32.76 ? 1350 HOH B O   1 
HETATM 20285 O  O   . HOH X 4 .   ? 43.146  -13.491 31.328  1.00 39.82 ? 1351 HOH B O   1 
HETATM 20286 O  O   . HOH X 4 .   ? 53.161  -8.170  34.886  1.00 17.68 ? 1352 HOH B O   1 
HETATM 20287 O  O   . HOH X 4 .   ? 52.079  23.984  35.873  1.00 31.12 ? 1353 HOH B O   1 
HETATM 20288 O  O   . HOH X 4 .   ? -11.917 2.580   40.658  1.00 31.15 ? 1354 HOH B O   1 
HETATM 20289 O  O   . HOH X 4 .   ? 38.889  14.425  51.049  1.00 47.48 ? 1355 HOH B O   1 
HETATM 20290 O  O   . HOH X 4 .   ? 39.296  -7.958  49.794  1.00 36.85 ? 1356 HOH B O   1 
HETATM 20291 O  O   . HOH X 4 .   ? 34.631  2.549   10.362  1.00 36.96 ? 1357 HOH B O   1 
HETATM 20292 O  O   . HOH X 4 .   ? 9.281   10.845  58.350  1.00 29.89 ? 1358 HOH B O   1 
HETATM 20293 O  O   . HOH X 4 .   ? -14.256 3.077   36.426  1.00 42.88 ? 1359 HOH B O   1 
HETATM 20294 O  O   . HOH X 4 .   ? 64.737  -0.546  38.866  1.00 19.97 ? 1360 HOH B O   1 
HETATM 20295 O  O   . HOH X 4 .   ? 44.709  16.017  11.829  1.00 35.66 ? 1361 HOH B O   1 
HETATM 20296 O  O   . HOH X 4 .   ? 31.411  -10.911 9.500   1.00 32.53 ? 1362 HOH B O   1 
HETATM 20297 O  O   . HOH X 4 .   ? 57.195  -9.813  35.516  1.00 36.85 ? 1363 HOH B O   1 
HETATM 20298 O  O   . HOH X 4 .   ? 62.657  -4.250  37.742  1.00 22.22 ? 1364 HOH B O   1 
HETATM 20299 O  O   . HOH X 4 .   ? -13.365 7.095   28.272  1.00 40.19 ? 1365 HOH B O   1 
HETATM 20300 O  O   . HOH X 4 .   ? 19.173  33.860  41.251  1.00 46.30 ? 1366 HOH B O   1 
HETATM 20301 O  O   . HOH X 4 .   ? 44.963  3.835   12.340  1.00 41.78 ? 1367 HOH B O   1 
HETATM 20302 O  O   . HOH X 4 .   ? 46.309  21.708  47.849  1.00 43.72 ? 1368 HOH B O   1 
HETATM 20303 O  O   . HOH X 4 .   ? 4.721   23.803  25.626  1.00 31.55 ? 1369 HOH B O   1 
HETATM 20304 O  O   . HOH X 4 .   ? 38.293  30.035  32.284  1.00 48.97 ? 1370 HOH B O   1 
HETATM 20305 O  O   . HOH X 4 .   ? 49.056  -7.652  48.553  1.00 49.68 ? 1371 HOH B O   1 
HETATM 20306 O  O   . HOH X 4 .   ? -0.719  5.348   61.983  1.00 41.10 ? 1372 HOH B O   1 
HETATM 20307 O  O   . HOH X 4 .   ? 32.459  30.305  46.509  1.00 41.44 ? 1373 HOH B O   1 
HETATM 20308 O  O   . HOH X 4 .   ? 4.706   -3.029  67.358  1.00 33.29 ? 1374 HOH B O   1 
HETATM 20309 O  O   . HOH X 4 .   ? 20.829  36.322  49.872  1.00 42.57 ? 1375 HOH B O   1 
HETATM 20310 O  O   . HOH X 4 .   ? -10.336 -12.088 39.776  1.00 44.18 ? 1376 HOH B O   1 
HETATM 20311 O  O   . HOH X 4 .   ? 45.750  7.209   11.134  1.00 42.38 ? 1377 HOH B O   1 
HETATM 20312 O  O   . HOH X 4 .   ? 34.074  -8.802  53.439  1.00 37.19 ? 1378 HOH B O   1 
HETATM 20313 O  O   . HOH X 4 .   ? 51.765  -7.659  42.734  1.00 40.65 ? 1379 HOH B O   1 
HETATM 20314 O  O   . HOH X 4 .   ? 44.431  5.419   10.326  1.00 41.79 ? 1380 HOH B O   1 
HETATM 20315 O  O   . HOH X 4 .   ? 28.017  3.990   48.158  1.00 32.94 ? 1381 HOH B O   1 
HETATM 20316 O  O   . HOH X 4 .   ? 52.579  -9.920  36.895  1.00 21.82 ? 1382 HOH B O   1 
HETATM 20317 O  O   . HOH X 4 .   ? 52.234  -5.728  40.732  1.00 26.47 ? 1383 HOH B O   1 
HETATM 20318 O  O   . HOH Y 4 .   ? 28.153  43.204  84.442  1.00 34.58 ? 801  HOH C O   1 
HETATM 20319 O  O   . HOH Y 4 .   ? 35.464  8.170   51.446  1.00 25.60 ? 802  HOH C O   1 
HETATM 20320 O  O   . HOH Y 4 .   ? 19.644  35.889  126.644 1.00 35.41 ? 803  HOH C O   1 
HETATM 20321 O  O   . HOH Y 4 .   ? 16.043  32.170  55.870  1.00 43.23 ? 804  HOH C O   1 
HETATM 20322 O  O   . HOH Y 4 .   ? 5.693   32.397  75.980  1.00 24.42 ? 805  HOH C O   1 
HETATM 20323 O  O   . HOH Y 4 .   ? 12.663  35.443  109.166 1.00 45.91 ? 806  HOH C O   1 
HETATM 20324 O  O   . HOH Y 4 .   ? 60.634  2.851   82.645  1.00 28.31 ? 807  HOH C O   1 
HETATM 20325 O  O   . HOH Y 4 .   ? 33.778  25.940  107.177 1.00 28.56 ? 808  HOH C O   1 
HETATM 20326 O  O   . HOH Y 4 .   ? 21.757  31.808  51.324  1.00 42.56 ? 809  HOH C O   1 
HETATM 20327 O  O   . HOH Y 4 .   ? 16.033  -3.737  62.227  1.00 29.55 ? 810  HOH C O   1 
HETATM 20328 O  O   . HOH Y 4 .   ? 41.081  3.965   53.852  1.00 31.69 ? 811  HOH C O   1 
HETATM 20329 O  O   . HOH Y 4 .   ? 55.621  19.180  77.590  1.00 39.98 ? 812  HOH C O   1 
HETATM 20330 O  O   . HOH Y 4 .   ? 54.714  20.657  73.582  1.00 39.12 ? 813  HOH C O   1 
HETATM 20331 O  O   . HOH Y 4 .   ? 33.474  22.131  101.928 1.00 33.02 ? 814  HOH C O   1 
HETATM 20332 O  O   . HOH Y 4 .   ? 41.597  31.039  60.594  1.00 39.26 ? 815  HOH C O   1 
HETATM 20333 O  O   . HOH Y 4 .   ? 11.413  7.253   88.002  1.00 33.56 ? 816  HOH C O   1 
HETATM 20334 O  O   . HOH Y 4 .   ? 49.853  15.572  56.309  1.00 33.94 ? 817  HOH C O   1 
HETATM 20335 O  O   . HOH Y 4 .   ? 37.105  24.365  83.486  1.00 31.19 ? 818  HOH C O   1 
HETATM 20336 O  O   . HOH Y 4 .   ? 14.924  36.988  76.952  1.00 40.40 ? 819  HOH C O   1 
HETATM 20337 O  O   . HOH Y 4 .   ? 36.123  4.889   49.539  1.00 19.47 ? 820  HOH C O   1 
HETATM 20338 O  O   . HOH Y 4 .   ? 38.307  27.152  103.604 1.00 40.12 ? 821  HOH C O   1 
HETATM 20339 O  O   . HOH Y 4 .   ? 33.237  23.289  79.459  1.00 32.60 ? 822  HOH C O   1 
HETATM 20340 O  O   . HOH Y 4 .   ? 10.654  5.762   91.110  1.00 28.07 ? 823  HOH C O   1 
HETATM 20341 O  O   . HOH Y 4 .   ? 41.334  -4.171  70.894  1.00 38.01 ? 824  HOH C O   1 
HETATM 20342 O  O   . HOH Y 4 .   ? 27.065  31.026  78.257  1.00 18.00 ? 825  HOH C O   1 
HETATM 20343 O  O   . HOH Y 4 .   ? 16.894  7.727   58.382  1.00 33.39 ? 826  HOH C O   1 
HETATM 20344 O  O   . HOH Y 4 .   ? 38.501  -2.630  73.270  1.00 27.40 ? 827  HOH C O   1 
HETATM 20345 O  O   . HOH Y 4 .   ? 24.968  14.524  58.284  1.00 42.12 ? 828  HOH C O   1 
HETATM 20346 O  O   . HOH Y 4 .   ? 8.655   9.413   86.401  1.00 45.60 ? 829  HOH C O   1 
HETATM 20347 O  O   . HOH Y 4 .   ? 9.005   18.780  88.578  1.00 22.21 ? 830  HOH C O   1 
HETATM 20348 O  O   . HOH Y 4 .   ? 16.997  19.255  64.689  1.00 25.73 ? 831  HOH C O   1 
HETATM 20349 O  O   . HOH Y 4 .   ? 29.872  34.788  93.570  1.00 28.24 ? 832  HOH C O   1 
HETATM 20350 O  O   . HOH Y 4 .   ? 46.237  3.324   80.401  1.00 25.74 ? 833  HOH C O   1 
HETATM 20351 O  O   . HOH Y 4 .   ? 6.803   11.355  95.643  1.00 27.90 ? 834  HOH C O   1 
HETATM 20352 O  O   . HOH Y 4 .   ? 30.465  20.769  99.461  1.00 28.60 ? 835  HOH C O   1 
HETATM 20353 O  O   . HOH Y 4 .   ? 39.601  32.781  56.584  1.00 28.07 ? 836  HOH C O   1 
HETATM 20354 O  O   . HOH Y 4 .   ? 33.920  14.505  59.536  1.00 21.22 ? 837  HOH C O   1 
HETATM 20355 O  O   . HOH Y 4 .   ? 37.997  16.109  69.107  1.00 22.45 ? 838  HOH C O   1 
HETATM 20356 O  O   . HOH Y 4 .   ? 53.307  15.102  62.264  1.00 32.12 ? 839  HOH C O   1 
HETATM 20357 O  O   . HOH Y 4 .   ? 28.664  40.456  65.626  1.00 23.93 ? 840  HOH C O   1 
HETATM 20358 O  O   . HOH Y 4 .   ? 14.076  10.386  87.528  1.00 11.96 ? 841  HOH C O   1 
HETATM 20359 O  O   . HOH Y 4 .   ? 29.156  31.243  91.280  1.00 19.20 ? 842  HOH C O   1 
HETATM 20360 O  O   . HOH Y 4 .   ? 24.000  12.791  115.644 1.00 24.61 ? 843  HOH C O   1 
HETATM 20361 O  O   . HOH Y 4 .   ? 27.546  36.681  92.070  1.00 36.38 ? 844  HOH C O   1 
HETATM 20362 O  O   . HOH Y 4 .   ? 24.581  8.211   60.948  1.00 17.89 ? 845  HOH C O   1 
HETATM 20363 O  O   . HOH Y 4 .   ? 33.394  10.991  81.151  1.00 16.06 ? 846  HOH C O   1 
HETATM 20364 O  O   . HOH Y 4 .   ? 43.791  10.710  84.327  1.00 17.60 ? 847  HOH C O   1 
HETATM 20365 O  O   . HOH Y 4 .   ? 23.448  5.871   100.130 1.00 16.95 ? 848  HOH C O   1 
HETATM 20366 O  O   . HOH Y 4 .   ? 49.079  1.022   87.236  1.00 44.47 ? 849  HOH C O   1 
HETATM 20367 O  O   . HOH Y 4 .   ? 32.899  17.674  59.721  1.00 16.48 ? 850  HOH C O   1 
HETATM 20368 O  O   . HOH Y 4 .   ? 24.377  4.745   54.183  1.00 22.22 ? 851  HOH C O   1 
HETATM 20369 O  O   . HOH Y 4 .   ? 15.477  23.430  99.345  1.00 14.29 ? 852  HOH C O   1 
HETATM 20370 O  O   . HOH Y 4 .   ? 15.678  11.139  62.006  1.00 37.68 ? 853  HOH C O   1 
HETATM 20371 O  O   . HOH Y 4 .   ? 40.017  18.615  88.552  1.00 31.16 ? 854  HOH C O   1 
HETATM 20372 O  O   . HOH Y 4 .   ? 36.691  29.578  72.861  1.00 30.48 ? 855  HOH C O   1 
HETATM 20373 O  O   . HOH Y 4 .   ? 44.133  14.012  61.139  1.00 21.78 ? 856  HOH C O   1 
HETATM 20374 O  O   . HOH Y 4 .   ? -1.139  13.192  101.759 1.00 39.08 ? 857  HOH C O   1 
HETATM 20375 O  O   . HOH Y 4 .   ? 8.424   31.323  124.706 1.00 39.52 ? 858  HOH C O   1 
HETATM 20376 O  O   . HOH Y 4 .   ? 23.416  46.173  97.567  1.00 22.81 ? 859  HOH C O   1 
HETATM 20377 O  O   . HOH Y 4 .   ? 36.358  -4.092  73.178  1.00 18.92 ? 860  HOH C O   1 
HETATM 20378 O  O   . HOH Y 4 .   ? 39.936  26.586  88.223  1.00 40.37 ? 861  HOH C O   1 
HETATM 20379 O  O   . HOH Y 4 .   ? 27.902  24.042  76.067  1.00 24.31 ? 862  HOH C O   1 
HETATM 20380 O  O   . HOH Y 4 .   ? 28.655  38.176  114.582 1.00 33.85 ? 863  HOH C O   1 
HETATM 20381 O  O   . HOH Y 4 .   ? 8.358   14.993  81.898  1.00 30.18 ? 864  HOH C O   1 
HETATM 20382 O  O   . HOH Y 4 .   ? 46.365  13.243  86.902  1.00 21.08 ? 865  HOH C O   1 
HETATM 20383 O  O   . HOH Y 4 .   ? 29.564  -6.910  66.541  1.00 18.07 ? 866  HOH C O   1 
HETATM 20384 O  O   . HOH Y 4 .   ? 12.271  19.060  102.833 1.00 12.57 ? 867  HOH C O   1 
HETATM 20385 O  O   . HOH Y 4 .   ? 40.047  19.816  70.555  1.00 28.72 ? 868  HOH C O   1 
HETATM 20386 O  O   . HOH Y 4 .   ? 6.776   24.834  79.510  1.00 19.36 ? 869  HOH C O   1 
HETATM 20387 O  O   . HOH Y 4 .   ? 17.221  6.849   65.077  1.00 17.40 ? 870  HOH C O   1 
HETATM 20388 O  O   . HOH Y 4 .   ? 24.806  16.406  65.986  1.00 13.96 ? 871  HOH C O   1 
HETATM 20389 O  O   . HOH Y 4 .   ? 20.429  40.840  61.071  1.00 29.44 ? 872  HOH C O   1 
HETATM 20390 O  O   . HOH Y 4 .   ? 57.574  4.197   69.454  1.00 28.90 ? 873  HOH C O   1 
HETATM 20391 O  O   . HOH Y 4 .   ? 19.724  20.517  63.953  1.00 21.27 ? 874  HOH C O   1 
HETATM 20392 O  O   . HOH Y 4 .   ? 9.994   25.344  126.357 1.00 42.55 ? 875  HOH C O   1 
HETATM 20393 O  O   . HOH Y 4 .   ? 35.116  19.228  74.519  1.00 18.79 ? 876  HOH C O   1 
HETATM 20394 O  O   . HOH Y 4 .   ? 44.221  22.252  77.091  1.00 40.65 ? 877  HOH C O   1 
HETATM 20395 O  O   . HOH Y 4 .   ? 11.470  33.162  80.993  1.00 19.99 ? 878  HOH C O   1 
HETATM 20396 O  O   . HOH Y 4 .   ? 39.837  19.004  57.487  1.00 23.69 ? 879  HOH C O   1 
HETATM 20397 O  O   . HOH Y 4 .   ? 30.676  38.237  78.755  1.00 32.76 ? 880  HOH C O   1 
HETATM 20398 O  O   . HOH Y 4 .   ? 39.571  16.501  83.850  1.00 21.05 ? 881  HOH C O   1 
HETATM 20399 O  O   . HOH Y 4 .   ? 29.854  25.110  78.077  1.00 32.68 ? 882  HOH C O   1 
HETATM 20400 O  O   . HOH Y 4 .   ? 20.269  5.651   85.501  1.00 11.61 ? 883  HOH C O   1 
HETATM 20401 O  O   . HOH Y 4 .   ? 19.540  32.275  66.372  1.00 42.54 ? 884  HOH C O   1 
HETATM 20402 O  O   . HOH Y 4 .   ? 6.819   15.060  117.698 1.00 26.35 ? 885  HOH C O   1 
HETATM 20403 O  O   . HOH Y 4 .   ? 26.740  32.436  49.788  1.00 28.85 ? 886  HOH C O   1 
HETATM 20404 O  O   . HOH Y 4 .   ? 39.011  11.083  76.889  1.00 15.91 ? 887  HOH C O   1 
HETATM 20405 O  O   . HOH Y 4 .   ? 7.950   17.671  119.781 1.00 37.22 ? 888  HOH C O   1 
HETATM 20406 O  O   . HOH Y 4 .   ? 30.525  21.218  102.562 1.00 28.57 ? 889  HOH C O   1 
HETATM 20407 O  O   . HOH Y 4 .   ? 17.957  16.768  101.689 1.00 25.79 ? 890  HOH C O   1 
HETATM 20408 O  O   . HOH Y 4 .   ? 35.673  35.238  101.532 1.00 30.40 ? 891  HOH C O   1 
HETATM 20409 O  O   . HOH Y 4 .   ? 36.892  34.551  71.385  1.00 34.66 ? 892  HOH C O   1 
HETATM 20410 O  O   . HOH Y 4 .   ? 36.968  -5.928  74.755  1.00 29.72 ? 893  HOH C O   1 
HETATM 20411 O  O   . HOH Y 4 .   ? 47.032  24.361  61.573  1.00 22.86 ? 894  HOH C O   1 
HETATM 20412 O  O   . HOH Y 4 .   ? 40.166  14.356  70.556  1.00 22.89 ? 895  HOH C O   1 
HETATM 20413 O  O   . HOH Y 4 .   ? 22.649  5.587   110.646 1.00 32.99 ? 896  HOH C O   1 
HETATM 20414 O  O   . HOH Y 4 .   ? 59.942  10.367  67.281  1.00 30.24 ? 897  HOH C O   1 
HETATM 20415 O  O   . HOH Y 4 .   ? 27.322  25.707  81.324  1.00 25.54 ? 898  HOH C O   1 
HETATM 20416 O  O   . HOH Y 4 .   ? 9.343   11.522  80.111  1.00 36.27 ? 899  HOH C O   1 
HETATM 20417 O  O   . HOH Y 4 .   ? 21.981  14.220  104.137 1.00 12.68 ? 900  HOH C O   1 
HETATM 20418 O  O   . HOH Y 4 .   ? 35.486  39.107  106.010 1.00 35.63 ? 901  HOH C O   1 
HETATM 20419 O  O   . HOH Y 4 .   ? 11.033  15.296  81.031  1.00 18.22 ? 902  HOH C O   1 
HETATM 20420 O  O   . HOH Y 4 .   ? 24.441  41.955  78.731  1.00 29.96 ? 903  HOH C O   1 
HETATM 20421 O  O   . HOH Y 4 .   ? 30.521  37.964  71.403  1.00 22.56 ? 904  HOH C O   1 
HETATM 20422 O  O   . HOH Y 4 .   ? 32.515  20.238  59.410  1.00 28.77 ? 905  HOH C O   1 
HETATM 20423 O  O   . HOH Y 4 .   ? 50.201  11.799  84.646  1.00 20.61 ? 906  HOH C O   1 
HETATM 20424 O  O   . HOH Y 4 .   ? 14.555  36.890  109.101 1.00 43.29 ? 907  HOH C O   1 
HETATM 20425 O  O   . HOH Y 4 .   ? 29.504  40.132  103.364 1.00 23.42 ? 908  HOH C O   1 
HETATM 20426 O  O   . HOH Y 4 .   ? 10.465  24.764  108.770 1.00 28.17 ? 909  HOH C O   1 
HETATM 20427 O  O   . HOH Y 4 .   ? 16.598  3.931   97.868  1.00 19.33 ? 910  HOH C O   1 
HETATM 20428 O  O   . HOH Y 4 .   ? 26.700  37.980  54.142  1.00 37.46 ? 911  HOH C O   1 
HETATM 20429 O  O   . HOH Y 4 .   ? 12.534  27.460  89.595  1.00 23.11 ? 912  HOH C O   1 
HETATM 20430 O  O   . HOH Y 4 .   ? 30.272  42.021  83.182  1.00 34.68 ? 913  HOH C O   1 
HETATM 20431 O  O   . HOH Y 4 .   ? 48.859  19.636  75.597  1.00 22.99 ? 914  HOH C O   1 
HETATM 20432 O  O   . HOH Y 4 .   ? 1.021   11.560  98.419  1.00 26.74 ? 915  HOH C O   1 
HETATM 20433 O  O   . HOH Y 4 .   ? 34.455  36.420  73.604  1.00 32.37 ? 916  HOH C O   1 
HETATM 20434 O  O   . HOH Y 4 .   ? 54.390  15.894  80.126  1.00 21.80 ? 917  HOH C O   1 
HETATM 20435 O  O   . HOH Y 4 .   ? 27.682  25.178  88.720  1.00 12.98 ? 918  HOH C O   1 
HETATM 20436 O  O   . HOH Y 4 .   ? 59.531  1.857   75.990  1.00 25.16 ? 919  HOH C O   1 
HETATM 20437 O  O   . HOH Y 4 .   ? 22.721  3.171   83.999  1.00 14.63 ? 920  HOH C O   1 
HETATM 20438 O  O   . HOH Y 4 .   ? 19.382  19.179  79.969  1.00 14.84 ? 921  HOH C O   1 
HETATM 20439 O  O   . HOH Y 4 .   ? 9.486   3.381   99.654  1.00 14.20 ? 922  HOH C O   1 
HETATM 20440 O  O   . HOH Y 4 .   ? 34.659  21.000  60.736  1.00 19.03 ? 923  HOH C O   1 
HETATM 20441 O  O   . HOH Y 4 .   ? 41.472  19.307  76.939  1.00 18.05 ? 924  HOH C O   1 
HETATM 20442 O  O   . HOH Y 4 .   ? 15.950  -0.426  63.532  1.00 32.18 ? 925  HOH C O   1 
HETATM 20443 O  O   . HOH Y 4 .   ? 20.970  37.833  77.541  1.00 25.04 ? 926  HOH C O   1 
HETATM 20444 O  O   . HOH Y 4 .   ? 40.681  19.580  67.647  1.00 20.89 ? 927  HOH C O   1 
HETATM 20445 O  O   . HOH Y 4 .   ? 34.039  24.086  99.903  1.00 31.72 ? 928  HOH C O   1 
HETATM 20446 O  O   . HOH Y 4 .   ? 28.471  31.503  95.458  1.00 22.64 ? 929  HOH C O   1 
HETATM 20447 O  O   . HOH Y 4 .   ? 43.541  28.857  59.763  1.00 31.85 ? 930  HOH C O   1 
HETATM 20448 O  O   . HOH Y 4 .   ? 33.645  6.147   79.225  1.00 17.14 ? 931  HOH C O   1 
HETATM 20449 O  O   . HOH Y 4 .   ? 35.855  -1.178  77.041  1.00 14.33 ? 932  HOH C O   1 
HETATM 20450 O  O   . HOH Y 4 .   ? 52.942  17.230  67.762  1.00 20.92 ? 933  HOH C O   1 
HETATM 20451 O  O   . HOH Y 4 .   ? 39.790  36.451  107.344 1.00 33.87 ? 934  HOH C O   1 
HETATM 20452 O  O   . HOH Y 4 .   ? 17.138  28.756  76.129  1.00 16.02 ? 935  HOH C O   1 
HETATM 20453 O  O   . HOH Y 4 .   ? 17.706  24.683  69.060  1.00 16.86 ? 936  HOH C O   1 
HETATM 20454 O  O   . HOH Y 4 .   ? 59.581  -0.205  74.401  1.00 33.98 ? 937  HOH C O   1 
HETATM 20455 O  O   . HOH Y 4 .   ? 21.782  15.891  106.225 1.00 16.68 ? 938  HOH C O   1 
HETATM 20456 O  O   . HOH Y 4 .   ? 25.084  0.548   55.760  1.00 35.22 ? 939  HOH C O   1 
HETATM 20457 O  O   . HOH Y 4 .   ? 27.331  27.246  92.814  1.00 15.30 ? 940  HOH C O   1 
HETATM 20458 O  O   . HOH Y 4 .   ? 21.826  14.537  60.511  1.00 34.21 ? 941  HOH C O   1 
HETATM 20459 O  O   . HOH Y 4 .   ? 27.701  16.072  65.877  1.00 13.35 ? 942  HOH C O   1 
HETATM 20460 O  O   . HOH Y 4 .   ? 25.905  39.342  72.370  1.00 32.29 ? 943  HOH C O   1 
HETATM 20461 O  O   . HOH Y 4 .   ? 31.347  17.461  107.384 1.00 36.74 ? 944  HOH C O   1 
HETATM 20462 O  O   . HOH Y 4 .   ? 38.946  13.544  72.793  1.00 17.02 ? 945  HOH C O   1 
HETATM 20463 O  O   . HOH Y 4 .   ? 16.066  33.481  120.843 1.00 24.60 ? 946  HOH C O   1 
HETATM 20464 O  O   . HOH Y 4 .   ? 4.757   18.549  110.634 1.00 21.68 ? 947  HOH C O   1 
HETATM 20465 O  O   . HOH Y 4 .   ? 49.632  14.007  87.567  1.00 20.54 ? 948  HOH C O   1 
HETATM 20466 O  O   . HOH Y 4 .   ? 25.227  22.671  101.199 1.00 19.72 ? 949  HOH C O   1 
HETATM 20467 O  O   . HOH Y 4 .   ? 24.875  -1.746  57.042  1.00 35.01 ? 950  HOH C O   1 
HETATM 20468 O  O   . HOH Y 4 .   ? 26.543  26.736  85.103  1.00 12.35 ? 951  HOH C O   1 
HETATM 20469 O  O   . HOH Y 4 .   ? 28.806  38.810  83.390  1.00 24.44 ? 952  HOH C O   1 
HETATM 20470 O  O   . HOH Y 4 .   ? 26.330  45.208  84.779  1.00 45.88 ? 953  HOH C O   1 
HETATM 20471 O  O   . HOH Y 4 .   ? 41.373  14.228  58.493  1.00 21.74 ? 954  HOH C O   1 
HETATM 20472 O  O   . HOH Y 4 .   ? 27.968  39.446  100.039 1.00 37.08 ? 955  HOH C O   1 
HETATM 20473 O  O   . HOH Y 4 .   ? 17.042  36.437  76.189  1.00 45.41 ? 956  HOH C O   1 
HETATM 20474 O  O   . HOH Y 4 .   ? 10.913  16.992  100.185 1.00 26.10 ? 957  HOH C O   1 
HETATM 20475 O  O   . HOH Y 4 .   ? 5.233   10.681  98.067  1.00 14.07 ? 958  HOH C O   1 
HETATM 20476 O  O   . HOH Y 4 .   ? 23.331  36.964  97.362  1.00 20.06 ? 959  HOH C O   1 
HETATM 20477 O  O   . HOH Y 4 .   ? 5.483   14.161  97.197  1.00 33.43 ? 960  HOH C O   1 
HETATM 20478 O  O   . HOH Y 4 .   ? 24.363  21.267  60.534  1.00 19.58 ? 961  HOH C O   1 
HETATM 20479 O  O   . HOH Y 4 .   ? 14.274  4.895   73.190  1.00 17.09 ? 962  HOH C O   1 
HETATM 20480 O  O   . HOH Y 4 .   ? 34.368  8.294   82.160  1.00 28.83 ? 963  HOH C O   1 
HETATM 20481 O  O   . HOH Y 4 .   ? 14.110  11.802  96.395  1.00 10.23 ? 964  HOH C O   1 
HETATM 20482 O  O   . HOH Y 4 .   ? 17.431  1.134   62.469  1.00 27.41 ? 965  HOH C O   1 
HETATM 20483 O  O   . HOH Y 4 .   ? 13.781  12.938  74.294  1.00 17.52 ? 966  HOH C O   1 
HETATM 20484 O  O   . HOH Y 4 .   ? 34.911  14.133  56.720  1.00 32.67 ? 967  HOH C O   1 
HETATM 20485 O  O   . HOH Y 4 .   ? 24.085  35.909  92.708  1.00 23.05 ? 968  HOH C O   1 
HETATM 20486 O  O   . HOH Y 4 .   ? 61.470  -0.554  60.647  1.00 40.98 ? 969  HOH C O   1 
HETATM 20487 O  O   . HOH Y 4 .   ? 14.914  6.712   103.451 1.00 11.30 ? 970  HOH C O   1 
HETATM 20488 O  O   . HOH Y 4 .   ? 45.152  14.012  79.198  1.00 27.71 ? 971  HOH C O   1 
HETATM 20489 O  O   . HOH Y 4 .   ? 11.824  2.208   107.043 1.00 26.55 ? 972  HOH C O   1 
HETATM 20490 O  O   . HOH Y 4 .   ? 43.547  17.987  84.308  1.00 35.98 ? 973  HOH C O   1 
HETATM 20491 O  O   . HOH Y 4 .   ? 47.793  21.819  70.531  1.00 28.60 ? 974  HOH C O   1 
HETATM 20492 O  O   . HOH Y 4 .   ? 25.165  11.822  58.955  1.00 17.02 ? 975  HOH C O   1 
HETATM 20493 O  O   . HOH Y 4 .   ? 44.190  -2.251  56.058  1.00 38.91 ? 976  HOH C O   1 
HETATM 20494 O  O   . HOH Y 4 .   ? 23.843  38.126  75.907  1.00 36.95 ? 977  HOH C O   1 
HETATM 20495 O  O   . HOH Y 4 .   ? 21.358  42.959  108.037 1.00 39.90 ? 978  HOH C O   1 
HETATM 20496 O  O   . HOH Y 4 .   ? 20.109  15.820  88.405  1.00 10.22 ? 979  HOH C O   1 
HETATM 20497 O  O   . HOH Y 4 .   ? 34.968  38.699  111.832 1.00 33.09 ? 980  HOH C O   1 
HETATM 20498 O  O   . HOH Y 4 .   ? 30.197  34.480  96.948  1.00 38.46 ? 981  HOH C O   1 
HETATM 20499 O  O   . HOH Y 4 .   ? 42.020  -1.110  64.123  1.00 19.26 ? 982  HOH C O   1 
HETATM 20500 O  O   . HOH Y 4 .   ? 37.291  28.131  91.537  1.00 45.91 ? 983  HOH C O   1 
HETATM 20501 O  O   . HOH Y 4 .   ? 30.109  -8.271  70.389  1.00 25.89 ? 984  HOH C O   1 
HETATM 20502 O  O   . HOH Y 4 .   ? 56.263  6.966   81.457  1.00 18.69 ? 985  HOH C O   1 
HETATM 20503 O  O   . HOH Y 4 .   ? 32.965  27.273  81.843  1.00 22.19 ? 986  HOH C O   1 
HETATM 20504 O  O   . HOH Y 4 .   ? 32.517  36.803  115.665 1.00 33.11 ? 987  HOH C O   1 
HETATM 20505 O  O   A HOH Y 4 .   ? 22.844  19.032  62.957  0.53 14.74 ? 988  HOH C O   1 
HETATM 20506 O  O   B HOH Y 4 .   ? 20.842  18.488  62.776  0.47 19.07 ? 988  HOH C O   1 
HETATM 20507 O  O   . HOH Y 4 .   ? 34.656  26.439  73.413  1.00 31.29 ? 989  HOH C O   1 
HETATM 20508 O  O   . HOH Y 4 .   ? 29.179  29.786  116.769 1.00 23.94 ? 990  HOH C O   1 
HETATM 20509 O  O   . HOH Y 4 .   ? 29.297  29.043  81.300  1.00 44.00 ? 991  HOH C O   1 
HETATM 20510 O  O   . HOH Y 4 .   ? 39.598  20.542  83.471  1.00 21.75 ? 992  HOH C O   1 
HETATM 20511 O  O   . HOH Y 4 .   ? 22.757  23.674  102.506 1.00 14.11 ? 993  HOH C O   1 
HETATM 20512 O  O   . HOH Y 4 .   ? 14.746  13.324  105.183 1.00 13.83 ? 994  HOH C O   1 
HETATM 20513 O  O   . HOH Y 4 .   ? 20.417  -12.671 68.122  1.00 33.96 ? 995  HOH C O   1 
HETATM 20514 O  O   . HOH Y 4 .   ? 38.594  -1.245  75.237  1.00 40.08 ? 996  HOH C O   1 
HETATM 20515 O  O   . HOH Y 4 .   ? 37.676  24.856  91.125  1.00 39.70 ? 997  HOH C O   1 
HETATM 20516 O  O   . HOH Y 4 .   ? 22.732  -13.148 72.428  1.00 34.78 ? 998  HOH C O   1 
HETATM 20517 O  O   . HOH Y 4 .   ? 26.778  17.657  57.363  1.00 28.71 ? 999  HOH C O   1 
HETATM 20518 O  O   . HOH Y 4 .   ? 9.405   30.621  110.839 1.00 29.49 ? 1000 HOH C O   1 
HETATM 20519 O  O   . HOH Y 4 .   ? 24.500  9.044   97.888  1.00 15.57 ? 1001 HOH C O   1 
HETATM 20520 O  O   . HOH Y 4 .   ? 34.977  25.534  70.917  1.00 20.41 ? 1002 HOH C O   1 
HETATM 20521 O  O   . HOH Y 4 .   ? 38.276  11.282  74.358  1.00 17.77 ? 1003 HOH C O   1 
HETATM 20522 O  O   . HOH Y 4 .   ? 41.538  18.517  59.487  1.00 21.43 ? 1004 HOH C O   1 
HETATM 20523 O  O   . HOH Y 4 .   ? 13.045  38.806  85.197  1.00 36.18 ? 1005 HOH C O   1 
HETATM 20524 O  O   . HOH Y 4 .   ? 17.769  30.198  72.756  1.00 22.77 ? 1006 HOH C O   1 
HETATM 20525 O  O   . HOH Y 4 .   ? 47.964  18.448  72.995  1.00 38.79 ? 1007 HOH C O   1 
HETATM 20526 O  O   . HOH Y 4 .   ? 34.216  24.491  111.569 1.00 46.25 ? 1008 HOH C O   1 
HETATM 20527 O  O   . HOH Y 4 .   ? 47.672  18.794  56.718  1.00 29.89 ? 1009 HOH C O   1 
HETATM 20528 O  O   . HOH Y 4 .   ? 21.373  40.543  63.698  1.00 25.45 ? 1010 HOH C O   1 
HETATM 20529 O  O   . HOH Y 4 .   ? 10.890  13.210  68.392  1.00 41.88 ? 1011 HOH C O   1 
HETATM 20530 O  O   . HOH Y 4 .   ? 6.494   11.116  85.809  1.00 38.09 ? 1012 HOH C O   1 
HETATM 20531 O  O   . HOH Y 4 .   ? 27.921  40.893  106.132 1.00 39.14 ? 1013 HOH C O   1 
HETATM 20532 O  O   . HOH Y 4 .   ? 36.270  21.219  96.775  1.00 23.80 ? 1014 HOH C O   1 
HETATM 20533 O  O   . HOH Y 4 .   ? 21.749  33.735  71.993  1.00 15.73 ? 1015 HOH C O   1 
HETATM 20534 O  O   . HOH Y 4 .   ? 34.150  -8.574  56.974  1.00 35.48 ? 1016 HOH C O   1 
HETATM 20535 O  O   . HOH Y 4 .   ? 24.298  10.677  95.642  1.00 16.79 ? 1017 HOH C O   1 
HETATM 20536 O  O   . HOH Y 4 .   ? 37.796  30.287  64.256  1.00 21.88 ? 1018 HOH C O   1 
HETATM 20537 O  O   . HOH Y 4 .   ? 33.399  36.127  54.095  1.00 38.55 ? 1019 HOH C O   1 
HETATM 20538 O  O   . HOH Y 4 .   ? 46.725  15.990  85.778  1.00 39.60 ? 1020 HOH C O   1 
HETATM 20539 O  O   . HOH Y 4 .   ? 17.841  34.588  64.972  1.00 31.33 ? 1021 HOH C O   1 
HETATM 20540 O  O   . HOH Y 4 .   ? 29.059  30.966  51.075  1.00 42.78 ? 1022 HOH C O   1 
HETATM 20541 O  O   . HOH Y 4 .   ? 14.695  21.919  101.522 1.00 14.39 ? 1023 HOH C O   1 
HETATM 20542 O  O   . HOH Y 4 .   ? 15.858  41.438  108.172 1.00 35.03 ? 1024 HOH C O   1 
HETATM 20543 O  O   . HOH Y 4 .   ? 25.381  15.500  107.597 1.00 16.29 ? 1025 HOH C O   1 
HETATM 20544 O  O   . HOH Y 4 .   ? 12.751  5.139   114.921 1.00 16.94 ? 1026 HOH C O   1 
HETATM 20545 O  O   . HOH Y 4 .   ? 47.625  -1.424  58.703  1.00 40.65 ? 1027 HOH C O   1 
HETATM 20546 O  O   . HOH Y 4 .   ? 41.601  -3.739  51.633  1.00 43.59 ? 1028 HOH C O   1 
HETATM 20547 O  O   . HOH Y 4 .   ? 36.735  18.861  55.108  1.00 44.00 ? 1029 HOH C O   1 
HETATM 20548 O  O   . HOH Y 4 .   ? 40.279  22.180  77.318  1.00 34.79 ? 1030 HOH C O   1 
HETATM 20549 O  O   . HOH Y 4 .   ? 15.403  3.874   70.867  1.00 34.09 ? 1031 HOH C O   1 
HETATM 20550 O  O   . HOH Y 4 .   ? 40.189  27.698  53.326  1.00 39.58 ? 1032 HOH C O   1 
HETATM 20551 O  O   . HOH Y 4 .   ? 13.192  44.758  97.249  1.00 30.58 ? 1033 HOH C O   1 
HETATM 20552 O  O   . HOH Y 4 .   ? 6.456   31.093  85.215  1.00 35.34 ? 1034 HOH C O   1 
HETATM 20553 O  O   . HOH Y 4 .   ? 24.102  40.099  91.549  1.00 36.63 ? 1035 HOH C O   1 
HETATM 20554 O  O   . HOH Y 4 .   ? 27.282  28.843  76.616  1.00 25.08 ? 1036 HOH C O   1 
HETATM 20555 O  O   . HOH Y 4 .   ? 13.870  15.752  74.311  1.00 17.22 ? 1037 HOH C O   1 
HETATM 20556 O  O   . HOH Y 4 .   ? 23.879  39.094  106.270 1.00 28.37 ? 1038 HOH C O   1 
HETATM 20557 O  O   . HOH Y 4 .   ? 14.942  11.893  113.637 1.00 20.67 ? 1039 HOH C O   1 
HETATM 20558 O  O   . HOH Y 4 .   ? 29.707  17.540  68.613  1.00 14.11 ? 1040 HOH C O   1 
HETATM 20559 O  O   . HOH Y 4 .   ? 59.088  3.576   67.397  1.00 22.52 ? 1041 HOH C O   1 
HETATM 20560 O  O   . HOH Y 4 .   ? 18.195  14.755  65.049  1.00 23.67 ? 1042 HOH C O   1 
HETATM 20561 O  O   . HOH Y 4 .   ? 28.569  15.990  104.613 1.00 14.19 ? 1043 HOH C O   1 
HETATM 20562 O  O   . HOH Y 4 .   ? 30.246  25.599  64.854  1.00 22.07 ? 1044 HOH C O   1 
HETATM 20563 O  O   . HOH Y 4 .   ? 19.421  42.616  95.199  1.00 40.53 ? 1045 HOH C O   1 
HETATM 20564 O  O   . HOH Y 4 .   ? 3.498   9.319   94.533  1.00 27.14 ? 1046 HOH C O   1 
HETATM 20565 O  O   . HOH Y 4 .   ? 19.072  27.512  103.575 1.00 14.34 ? 1047 HOH C O   1 
HETATM 20566 O  O   . HOH Y 4 .   ? 37.127  31.483  111.034 1.00 35.75 ? 1048 HOH C O   1 
HETATM 20567 O  O   . HOH Y 4 .   ? 30.904  11.844  82.462  1.00 12.45 ? 1049 HOH C O   1 
HETATM 20568 O  O   . HOH Y 4 .   ? 6.366   22.074  115.949 1.00 29.52 ? 1050 HOH C O   1 
HETATM 20569 O  O   . HOH Y 4 .   ? 7.103   20.936  92.093  1.00 35.44 ? 1051 HOH C O   1 
HETATM 20570 O  O   . HOH Y 4 .   ? 46.379  13.896  59.466  1.00 24.76 ? 1052 HOH C O   1 
HETATM 20571 O  O   . HOH Y 4 .   ? 6.636   23.114  93.047  1.00 40.13 ? 1053 HOH C O   1 
HETATM 20572 O  O   . HOH Y 4 .   ? 15.181  14.939  114.860 1.00 20.21 ? 1054 HOH C O   1 
HETATM 20573 O  O   . HOH Y 4 .   ? 48.931  14.731  85.233  1.00 28.68 ? 1055 HOH C O   1 
HETATM 20574 O  O   . HOH Y 4 .   ? 63.599  10.525  59.602  1.00 39.21 ? 1056 HOH C O   1 
HETATM 20575 O  O   . HOH Y 4 .   ? 28.907  24.102  119.403 1.00 27.54 ? 1057 HOH C O   1 
HETATM 20576 O  O   . HOH Y 4 .   ? 27.181  6.549   88.801  1.00 19.56 ? 1058 HOH C O   1 
HETATM 20577 O  O   . HOH Y 4 .   ? 26.394  43.232  85.817  1.00 31.48 ? 1059 HOH C O   1 
HETATM 20578 O  O   . HOH Y 4 .   ? 40.197  21.900  66.054  1.00 13.08 ? 1060 HOH C O   1 
HETATM 20579 O  O   . HOH Y 4 .   ? 36.022  21.940  112.089 1.00 41.99 ? 1061 HOH C O   1 
HETATM 20580 O  O   . HOH Y 4 .   ? 50.241  19.522  57.593  1.00 28.46 ? 1062 HOH C O   1 
HETATM 20581 O  O   . HOH Y 4 .   ? 56.012  6.452   78.815  1.00 22.00 ? 1063 HOH C O   1 
HETATM 20582 O  O   . HOH Y 4 .   ? 46.658  3.170   76.893  1.00 24.84 ? 1064 HOH C O   1 
HETATM 20583 O  O   . HOH Y 4 .   ? 26.430  2.117   83.748  1.00 11.02 ? 1065 HOH C O   1 
HETATM 20584 O  O   . HOH Y 4 .   ? 10.641  21.291  108.198 1.00 29.55 ? 1066 HOH C O   1 
HETATM 20585 O  O   . HOH Y 4 .   ? 63.965  0.757   71.441  1.00 38.67 ? 1067 HOH C O   1 
HETATM 20586 O  O   . HOH Y 4 .   ? 4.533   24.247  89.238  1.00 26.49 ? 1068 HOH C O   1 
HETATM 20587 O  O   . HOH Y 4 .   ? 32.624  -1.990  55.212  1.00 27.09 ? 1069 HOH C O   1 
HETATM 20588 O  O   . HOH Y 4 .   ? 39.986  12.123  53.008  1.00 42.02 ? 1070 HOH C O   1 
HETATM 20589 O  O   . HOH Y 4 .   ? 38.840  17.063  66.804  1.00 27.24 ? 1071 HOH C O   1 
HETATM 20590 O  O   . HOH Y 4 .   ? 31.496  25.469  80.703  1.00 29.34 ? 1072 HOH C O   1 
HETATM 20591 O  O   . HOH Y 4 .   ? 22.865  -3.664  59.149  1.00 37.77 ? 1073 HOH C O   1 
HETATM 20592 O  O   . HOH Y 4 .   ? 45.881  6.944   55.801  1.00 32.09 ? 1074 HOH C O   1 
HETATM 20593 O  O   . HOH Y 4 .   ? 11.596  12.656  80.371  1.00 10.71 ? 1075 HOH C O   1 
HETATM 20594 O  O   . HOH Y 4 .   ? 23.103  -5.269  61.209  1.00 25.29 ? 1076 HOH C O   1 
HETATM 20595 O  O   . HOH Y 4 .   ? 34.752  24.755  93.783  1.00 25.81 ? 1077 HOH C O   1 
HETATM 20596 O  O   . HOH Y 4 .   ? 31.787  21.585  120.294 1.00 44.12 ? 1078 HOH C O   1 
HETATM 20597 O  O   . HOH Y 4 .   ? 24.369  40.085  70.300  1.00 24.36 ? 1079 HOH C O   1 
HETATM 20598 O  O   . HOH Y 4 .   ? 15.904  14.970  117.186 1.00 35.63 ? 1080 HOH C O   1 
HETATM 20599 O  O   . HOH Y 4 .   ? 6.424   19.042  112.838 1.00 25.51 ? 1081 HOH C O   1 
HETATM 20600 O  O   . HOH Y 4 .   ? 40.741  21.032  55.289  1.00 34.41 ? 1082 HOH C O   1 
HETATM 20601 O  O   . HOH Y 4 .   ? 17.075  46.574  103.154 1.00 30.93 ? 1083 HOH C O   1 
HETATM 20602 O  O   . HOH Y 4 .   ? 24.945  37.489  90.599  1.00 26.41 ? 1084 HOH C O   1 
HETATM 20603 O  O   . HOH Y 4 .   ? 10.780  14.759  72.514  1.00 35.36 ? 1085 HOH C O   1 
HETATM 20604 O  O   . HOH Y 4 .   ? 48.692  17.997  87.156  1.00 33.66 ? 1086 HOH C O   1 
HETATM 20605 O  O   . HOH Y 4 .   ? 35.967  25.468  76.123  1.00 22.77 ? 1087 HOH C O   1 
HETATM 20606 O  O   . HOH Y 4 .   ? 17.642  15.430  103.201 1.00 34.01 ? 1088 HOH C O   1 
HETATM 20607 O  O   . HOH Y 4 .   ? 18.311  26.514  61.471  1.00 28.64 ? 1089 HOH C O   1 
HETATM 20608 O  O   . HOH Y 4 .   ? 10.211  18.790  95.699  1.00 21.05 ? 1090 HOH C O   1 
HETATM 20609 O  O   . HOH Y 4 .   ? 6.459   22.071  118.695 1.00 27.18 ? 1091 HOH C O   1 
HETATM 20610 O  O   . HOH Y 4 .   ? 36.697  28.892  66.406  1.00 20.57 ? 1092 HOH C O   1 
HETATM 20611 O  O   . HOH Y 4 .   ? 29.074  -9.850  72.047  1.00 39.56 ? 1093 HOH C O   1 
HETATM 20612 O  O   . HOH Y 4 .   ? 23.212  16.026  118.616 1.00 34.11 ? 1094 HOH C O   1 
HETATM 20613 O  O   . HOH Y 4 .   ? 5.087   22.918  77.903  1.00 23.21 ? 1095 HOH C O   1 
HETATM 20614 O  O   . HOH Y 4 .   ? 23.219  14.395  65.054  1.00 13.60 ? 1096 HOH C O   1 
HETATM 20615 O  O   . HOH Y 4 .   ? 19.033  14.136  115.535 1.00 27.44 ? 1097 HOH C O   1 
HETATM 20616 O  O   . HOH Y 4 .   ? 6.289   25.784  76.709  1.00 23.79 ? 1098 HOH C O   1 
HETATM 20617 O  O   . HOH Y 4 .   ? 24.859  -10.004 64.420  1.00 30.47 ? 1099 HOH C O   1 
HETATM 20618 O  O   . HOH Y 4 .   ? 55.810  14.282  84.508  1.00 35.05 ? 1100 HOH C O   1 
HETATM 20619 O  O   . HOH Y 4 .   ? 34.453  34.873  116.793 1.00 43.05 ? 1101 HOH C O   1 
HETATM 20620 O  O   . HOH Y 4 .   ? 21.086  23.315  59.819  1.00 27.69 ? 1102 HOH C O   1 
HETATM 20621 O  O   . HOH Y 4 .   ? 21.605  14.062  116.942 1.00 27.67 ? 1103 HOH C O   1 
HETATM 20622 O  O   . HOH Y 4 .   ? 19.657  13.869  102.046 1.00 15.20 ? 1104 HOH C O   1 
HETATM 20623 O  O   . HOH Y 4 .   ? 35.197  35.172  60.939  1.00 26.16 ? 1105 HOH C O   1 
HETATM 20624 O  O   . HOH Y 4 .   ? 5.479   23.116  82.399  1.00 35.03 ? 1106 HOH C O   1 
HETATM 20625 O  O   . HOH Y 4 .   ? 2.468   13.940  101.990 1.00 21.73 ? 1107 HOH C O   1 
HETATM 20626 O  O   . HOH Y 4 .   ? 33.316  27.478  118.995 1.00 32.64 ? 1108 HOH C O   1 
HETATM 20627 O  O   . HOH Y 4 .   ? 44.812  28.054  61.934  1.00 28.21 ? 1109 HOH C O   1 
HETATM 20628 O  O   . HOH Y 4 .   ? 57.090  14.133  87.903  1.00 38.10 ? 1110 HOH C O   1 
HETATM 20629 O  O   . HOH Y 4 .   ? 55.964  10.167  88.566  1.00 24.45 ? 1111 HOH C O   1 
HETATM 20630 O  O   . HOH Y 4 .   ? 9.610   17.150  90.720  1.00 14.41 ? 1112 HOH C O   1 
HETATM 20631 O  O   . HOH Y 4 .   ? 9.887   14.496  65.743  1.00 37.71 ? 1113 HOH C O   1 
HETATM 20632 O  O   . HOH Y 4 .   ? 32.091  -7.878  55.902  1.00 55.21 ? 1114 HOH C O   1 
HETATM 20633 O  O   . HOH Y 4 .   ? 34.391  23.312  73.143  1.00 16.67 ? 1115 HOH C O   1 
HETATM 20634 O  O   . HOH Y 4 .   ? 33.041  3.481   48.326  1.00 27.08 ? 1116 HOH C O   1 
HETATM 20635 O  O   . HOH Y 4 .   ? 19.462  2.249   58.735  1.00 25.84 ? 1117 HOH C O   1 
HETATM 20636 O  O   . HOH Y 4 .   ? 12.305  26.887  105.704 1.00 22.73 ? 1118 HOH C O   1 
HETATM 20637 O  O   . HOH Y 4 .   ? 41.350  31.568  63.142  1.00 38.63 ? 1119 HOH C O   1 
HETATM 20638 O  O   . HOH Y 4 .   ? 15.859  30.754  77.456  1.00 20.43 ? 1120 HOH C O   1 
HETATM 20639 O  O   . HOH Y 4 .   ? 21.185  -0.601  59.881  1.00 18.01 ? 1121 HOH C O   1 
HETATM 20640 O  O   . HOH Y 4 .   ? 21.054  16.908  110.117 1.00 17.60 ? 1122 HOH C O   1 
HETATM 20641 O  O   . HOH Y 4 .   ? 14.178  25.406  90.650  1.00 21.98 ? 1123 HOH C O   1 
HETATM 20642 O  O   . HOH Y 4 .   ? 34.979  -6.074  56.120  1.00 24.77 ? 1124 HOH C O   1 
HETATM 20643 O  O   . HOH Y 4 .   ? 34.238  23.677  59.466  1.00 15.55 ? 1125 HOH C O   1 
HETATM 20644 O  O   . HOH Y 4 .   ? 25.357  37.635  107.997 1.00 29.39 ? 1126 HOH C O   1 
HETATM 20645 O  O   . HOH Y 4 .   ? 1.035   16.105  104.920 1.00 27.39 ? 1127 HOH C O   1 
HETATM 20646 O  O   . HOH Y 4 .   ? 19.727  32.695  68.631  1.00 34.52 ? 1128 HOH C O   1 
HETATM 20647 O  O   . HOH Y 4 .   ? 26.343  17.304  105.757 1.00 12.84 ? 1129 HOH C O   1 
HETATM 20648 O  O   . HOH Y 4 .   ? 31.412  34.640  81.942  1.00 23.76 ? 1130 HOH C O   1 
HETATM 20649 O  O   . HOH Y 4 .   ? 22.845  11.258  52.291  1.00 28.05 ? 1131 HOH C O   1 
HETATM 20650 O  O   . HOH Y 4 .   ? 32.464  32.759  97.256  1.00 33.73 ? 1132 HOH C O   1 
HETATM 20651 O  O   . HOH Y 4 .   ? 25.004  44.918  101.600 1.00 35.43 ? 1133 HOH C O   1 
HETATM 20652 O  O   . HOH Y 4 .   ? 24.935  6.013   109.524 1.00 41.05 ? 1134 HOH C O   1 
HETATM 20653 O  O   . HOH Y 4 .   ? 37.046  26.972  106.123 1.00 40.00 ? 1135 HOH C O   1 
HETATM 20654 O  O   . HOH Y 4 .   ? 20.020  -7.650  63.477  1.00 45.68 ? 1136 HOH C O   1 
HETATM 20655 O  O   . HOH Y 4 .   ? 20.475  27.016  57.091  1.00 32.51 ? 1137 HOH C O   1 
HETATM 20656 O  O   . HOH Y 4 .   ? 17.013  13.546  62.788  1.00 36.48 ? 1138 HOH C O   1 
HETATM 20657 O  O   . HOH Y 4 .   ? 62.150  7.442   83.048  1.00 42.74 ? 1139 HOH C O   1 
HETATM 20658 O  O   . HOH Y 4 .   ? 41.537  21.170  74.110  1.00 26.18 ? 1140 HOH C O   1 
HETATM 20659 O  O   . HOH Y 4 .   ? 26.789  40.302  76.689  1.00 23.74 ? 1141 HOH C O   1 
HETATM 20660 O  O   . HOH Y 4 .   ? 33.325  28.964  53.407  1.00 39.98 ? 1142 HOH C O   1 
HETATM 20661 O  O   . HOH Y 4 .   ? 39.231  20.539  74.052  1.00 28.32 ? 1143 HOH C O   1 
HETATM 20662 O  O   . HOH Y 4 .   ? 13.515  37.788  101.157 1.00 40.88 ? 1144 HOH C O   1 
HETATM 20663 O  O   . HOH Y 4 .   ? 29.195  -7.549  63.924  1.00 19.92 ? 1145 HOH C O   1 
HETATM 20664 O  O   . HOH Y 4 .   ? 33.946  18.787  99.582  1.00 43.61 ? 1146 HOH C O   1 
HETATM 20665 O  O   . HOH Y 4 .   ? 16.340  34.214  76.437  1.00 29.34 ? 1147 HOH C O   1 
HETATM 20666 O  O   . HOH Y 4 .   ? 17.864  9.022   113.754 1.00 18.05 ? 1148 HOH C O   1 
HETATM 20667 O  O   . HOH Y 4 .   ? 35.706  21.821  74.967  1.00 19.64 ? 1149 HOH C O   1 
HETATM 20668 O  O   . HOH Y 4 .   ? 13.468  30.924  77.385  1.00 17.00 ? 1150 HOH C O   1 
HETATM 20669 O  O   . HOH Y 4 .   ? 15.807  37.483  122.698 1.00 33.40 ? 1151 HOH C O   1 
HETATM 20670 O  O   . HOH Y 4 .   ? 10.049  18.239  84.226  1.00 26.81 ? 1152 HOH C O   1 
HETATM 20671 O  O   . HOH Y 4 .   ? 27.986  40.598  85.342  1.00 25.29 ? 1153 HOH C O   1 
HETATM 20672 O  O   . HOH Y 4 .   ? 7.578   22.127  72.865  1.00 19.46 ? 1154 HOH C O   1 
HETATM 20673 O  O   . HOH Y 4 .   ? 21.667  -10.254 63.713  1.00 45.18 ? 1155 HOH C O   1 
HETATM 20674 O  O   . HOH Y 4 .   ? 61.522  9.032   56.753  1.00 38.94 ? 1156 HOH C O   1 
HETATM 20675 O  O   . HOH Y 4 .   ? 33.821  40.147  104.512 1.00 36.84 ? 1157 HOH C O   1 
HETATM 20676 O  O   . HOH Y 4 .   ? 23.595  19.122  58.686  1.00 41.94 ? 1158 HOH C O   1 
HETATM 20677 O  O   . HOH Y 4 .   ? 31.693  40.267  58.946  1.00 31.38 ? 1159 HOH C O   1 
HETATM 20678 O  O   . HOH Y 4 .   ? 35.787  33.975  63.134  1.00 41.77 ? 1160 HOH C O   1 
HETATM 20679 O  O   . HOH Y 4 .   ? 31.122  31.304  95.267  1.00 36.03 ? 1161 HOH C O   1 
HETATM 20680 O  O   . HOH Y 4 .   ? 6.728   0.737   109.451 1.00 52.91 ? 1162 HOH C O   1 
HETATM 20681 O  O   . HOH Y 4 .   ? 48.880  26.867  68.068  1.00 41.53 ? 1163 HOH C O   1 
HETATM 20682 O  O   . HOH Y 4 .   ? 20.401  43.016  119.620 1.00 41.76 ? 1164 HOH C O   1 
HETATM 20683 O  O   . HOH Y 4 .   ? 33.112  19.208  72.652  1.00 15.51 ? 1165 HOH C O   1 
HETATM 20684 O  O   A HOH Y 4 .   ? 34.824  1.373   84.644  0.46 14.11 ? 1166 HOH C O   1 
HETATM 20685 O  O   B HOH Y 4 .   ? 33.808  -0.512  85.121  0.54 12.81 ? 1166 HOH C O   1 
HETATM 20686 O  O   . HOH Y 4 .   ? 31.204  26.644  118.859 1.00 35.19 ? 1167 HOH C O   1 
HETATM 20687 O  O   . HOH Y 4 .   ? 34.498  20.062  119.879 1.00 16.70 ? 1168 HOH C O   1 
HETATM 20688 O  O   . HOH Y 4 .   ? 3.563   28.005  78.737  1.00 33.27 ? 1169 HOH C O   1 
HETATM 20689 O  O   . HOH Y 4 .   ? 12.137  32.947  78.457  1.00 24.46 ? 1170 HOH C O   1 
HETATM 20690 O  O   . HOH Y 4 .   ? 27.431  8.813   97.813  1.00 27.15 ? 1171 HOH C O   1 
HETATM 20691 O  O   . HOH Y 4 .   ? 31.654  10.473  53.361  1.00 9.97  ? 1172 HOH C O   1 
HETATM 20692 O  O   . HOH Y 4 .   ? 11.867  24.159  67.811  1.00 41.28 ? 1173 HOH C O   1 
HETATM 20693 O  O   . HOH Y 4 .   ? 34.284  16.481  55.460  1.00 29.23 ? 1174 HOH C O   1 
HETATM 20694 O  O   . HOH Y 4 .   ? 38.115  29.237  68.607  1.00 30.48 ? 1175 HOH C O   1 
HETATM 20695 O  O   . HOH Y 4 .   ? 20.498  44.581  83.523  1.00 45.52 ? 1176 HOH C O   1 
HETATM 20696 O  O   . HOH Y 4 .   ? 27.908  -8.594  68.423  1.00 21.56 ? 1177 HOH C O   1 
HETATM 20697 O  O   . HOH Y 4 .   ? 24.570  38.599  119.326 1.00 39.91 ? 1178 HOH C O   1 
HETATM 20698 O  O   . HOH Y 4 .   ? 30.304  14.393  106.304 1.00 29.86 ? 1179 HOH C O   1 
HETATM 20699 O  O   . HOH Y 4 .   ? 21.033  46.242  104.798 1.00 30.32 ? 1180 HOH C O   1 
HETATM 20700 O  O   A HOH Y 4 .   ? 7.857   14.699  89.500  0.55 14.53 ? 1181 HOH C O   1 
HETATM 20701 O  O   B HOH Y 4 .   ? 7.380   13.128  88.974  0.45 13.84 ? 1181 HOH C O   1 
HETATM 20702 O  O   . HOH Y 4 .   ? 16.195  36.399  120.233 1.00 27.28 ? 1182 HOH C O   1 
HETATM 20703 O  O   . HOH Y 4 .   ? 40.982  33.012  58.803  1.00 25.91 ? 1183 HOH C O   1 
HETATM 20704 O  O   . HOH Y 4 .   ? 58.409  16.023  69.998  1.00 20.27 ? 1184 HOH C O   1 
HETATM 20705 O  O   . HOH Y 4 .   ? 33.405  21.758  97.550  1.00 34.66 ? 1185 HOH C O   1 
HETATM 20706 O  O   . HOH Y 4 .   ? 13.841  23.884  65.203  1.00 35.91 ? 1186 HOH C O   1 
HETATM 20707 O  O   . HOH Y 4 .   ? 7.051   0.458   107.035 1.00 34.19 ? 1187 HOH C O   1 
HETATM 20708 O  O   . HOH Y 4 .   ? 8.338   0.552   111.046 1.00 38.95 ? 1188 HOH C O   1 
HETATM 20709 O  O   . HOH Y 4 .   ? 34.799  30.256  114.848 1.00 42.76 ? 1189 HOH C O   1 
HETATM 20710 O  O   A HOH Y 4 .   ? 18.463  26.254  71.787  0.66 21.89 ? 1190 HOH C O   1 
HETATM 20711 O  O   B HOH Y 4 .   ? 18.950  27.020  73.596  0.34 20.87 ? 1190 HOH C O   1 
HETATM 20712 O  O   . HOH Y 4 .   ? 16.297  2.472   109.663 1.00 30.03 ? 1191 HOH C O   1 
HETATM 20713 O  O   . HOH Y 4 .   ? 6.386   22.881  75.368  1.00 32.72 ? 1192 HOH C O   1 
HETATM 20714 O  O   . HOH Y 4 .   ? 38.745  15.690  55.939  1.00 43.17 ? 1193 HOH C O   1 
HETATM 20715 O  O   . HOH Y 4 .   ? 48.521  -1.096  84.814  1.00 38.45 ? 1194 HOH C O   1 
HETATM 20716 O  O   . HOH Y 4 .   ? 62.714  10.660  70.743  1.00 47.75 ? 1195 HOH C O   1 
HETATM 20717 O  O   . HOH Y 4 .   ? 21.908  39.941  109.709 1.00 44.06 ? 1196 HOH C O   1 
HETATM 20718 O  O   . HOH Y 4 .   ? 30.603  8.525   109.498 1.00 28.77 ? 1197 HOH C O   1 
HETATM 20719 O  O   . HOH Y 4 .   ? 17.823  39.912  111.376 1.00 35.24 ? 1198 HOH C O   1 
HETATM 20720 O  O   . HOH Y 4 .   ? 11.128  0.442   109.530 1.00 41.11 ? 1199 HOH C O   1 
HETATM 20721 O  O   . HOH Y 4 .   ? 27.625  26.549  54.775  1.00 42.83 ? 1200 HOH C O   1 
HETATM 20722 O  O   . HOH Y 4 .   ? 10.193  1.816   112.599 1.00 40.42 ? 1201 HOH C O   1 
HETATM 20723 O  O   . HOH Y 4 .   ? 27.595  43.398  60.218  1.00 45.54 ? 1202 HOH C O   1 
HETATM 20724 O  O   . HOH Y 4 .   ? 28.734  37.117  85.939  1.00 32.95 ? 1203 HOH C O   1 
HETATM 20725 O  O   . HOH Y 4 .   ? 55.260  17.796  69.380  1.00 34.01 ? 1204 HOH C O   1 
HETATM 20726 O  O   . HOH Y 4 .   ? 28.546  27.102  78.711  1.00 38.20 ? 1205 HOH C O   1 
HETATM 20727 O  O   . HOH Y 4 .   ? 6.769   26.781  74.296  1.00 35.36 ? 1206 HOH C O   1 
HETATM 20728 O  O   . HOH Y 4 .   ? 35.771  24.488  80.593  1.00 34.44 ? 1207 HOH C O   1 
HETATM 20729 O  O   . HOH Y 4 .   ? 40.921  19.099  85.418  1.00 38.64 ? 1208 HOH C O   1 
HETATM 20730 O  O   . HOH Y 4 .   ? 19.432  9.073   55.269  1.00 28.86 ? 1209 HOH C O   1 
HETATM 20731 O  O   . HOH Y 4 .   ? 9.188   21.199  110.209 1.00 47.06 ? 1210 HOH C O   1 
HETATM 20732 O  O   . HOH Y 4 .   ? 8.302   26.768  109.809 1.00 45.43 ? 1211 HOH C O   1 
HETATM 20733 O  O   . HOH Y 4 .   ? 38.024  -9.946  74.935  1.00 43.12 ? 1212 HOH C O   1 
HETATM 20734 O  O   . HOH Y 4 .   ? 15.698  41.952  86.496  1.00 38.57 ? 1213 HOH C O   1 
HETATM 20735 O  O   . HOH Y 4 .   ? 58.487  7.026   82.883  1.00 42.47 ? 1214 HOH C O   1 
HETATM 20736 O  O   . HOH Y 4 .   ? 40.466  3.148   50.622  1.00 25.64 ? 1215 HOH C O   1 
HETATM 20737 O  O   . HOH Y 4 .   ? 12.912  30.352  74.656  1.00 49.10 ? 1216 HOH C O   1 
HETATM 20738 O  O   . HOH Y 4 .   ? 14.263  1.995   111.902 1.00 37.73 ? 1217 HOH C O   1 
HETATM 20739 O  O   . HOH Y 4 .   ? 29.312  24.665  67.361  1.00 24.06 ? 1218 HOH C O   1 
HETATM 20740 O  O   . HOH Y 4 .   ? 22.020  3.689   86.744  1.00 10.96 ? 1219 HOH C O   1 
HETATM 20741 O  O   . HOH Y 4 .   ? 40.825  14.522  56.022  1.00 39.42 ? 1220 HOH C O   1 
HETATM 20742 O  O   . HOH Y 4 .   ? 8.071   17.497  80.694  1.00 40.55 ? 1221 HOH C O   1 
HETATM 20743 O  O   . HOH Y 4 .   ? 25.863  6.905   111.816 1.00 47.17 ? 1222 HOH C O   1 
HETATM 20744 O  O   . HOH Y 4 .   ? 19.163  16.615  103.977 1.00 33.60 ? 1223 HOH C O   1 
HETATM 20745 O  O   . HOH Y 4 .   ? 25.802  43.704  90.129  1.00 29.59 ? 1224 HOH C O   1 
HETATM 20746 O  O   . HOH Y 4 .   ? 24.106  28.224  50.666  1.00 29.55 ? 1225 HOH C O   1 
HETATM 20747 O  O   . HOH Y 4 .   ? 27.088  19.471  106.941 1.00 22.28 ? 1226 HOH C O   1 
HETATM 20748 O  O   . HOH Y 4 .   ? 2.065   21.330  85.250  1.00 35.35 ? 1227 HOH C O   1 
HETATM 20749 O  O   . HOH Y 4 .   ? 33.634  30.274  89.716  1.00 40.17 ? 1228 HOH C O   1 
HETATM 20750 O  O   . HOH Y 4 .   ? 19.321  25.653  54.615  1.00 40.19 ? 1229 HOH C O   1 
HETATM 20751 O  O   . HOH Y 4 .   ? 30.442  -1.411  53.932  1.00 41.39 ? 1230 HOH C O   1 
HETATM 20752 O  O   . HOH Y 4 .   ? 27.362  34.361  48.111  1.00 32.26 ? 1231 HOH C O   1 
HETATM 20753 O  O   . HOH Y 4 .   ? 14.474  3.083   114.464 1.00 22.74 ? 1232 HOH C O   1 
HETATM 20754 O  O   . HOH Y 4 .   ? 45.138  29.741  57.687  1.00 38.46 ? 1233 HOH C O   1 
HETATM 20755 O  O   . HOH Y 4 .   ? 5.779   18.961  119.418 1.00 22.39 ? 1234 HOH C O   1 
HETATM 20756 O  O   . HOH Y 4 .   ? 6.351   17.854  123.568 1.00 37.75 ? 1235 HOH C O   1 
HETATM 20757 O  O   . HOH Y 4 .   ? 14.673  46.356  91.866  1.00 40.19 ? 1236 HOH C O   1 
HETATM 20758 O  O   . HOH Y 4 .   ? 18.910  11.626  115.145 1.00 35.53 ? 1237 HOH C O   1 
HETATM 20759 O  O   . HOH Y 4 .   ? 35.658  27.228  93.384  1.00 36.47 ? 1238 HOH C O   1 
HETATM 20760 O  O   . HOH Y 4 .   ? 16.512  50.129  94.336  1.00 23.32 ? 1239 HOH C O   1 
HETATM 20761 O  O   . HOH Y 4 .   ? 23.190  37.567  94.606  1.00 31.00 ? 1240 HOH C O   1 
HETATM 20762 O  O   . HOH Y 4 .   ? 8.699   17.330  98.127  1.00 29.15 ? 1241 HOH C O   1 
HETATM 20763 O  O   . HOH Y 4 .   ? 19.165  22.075  61.806  1.00 29.42 ? 1242 HOH C O   1 
HETATM 20764 O  O   . HOH Y 4 .   ? 29.373  20.248  106.024 1.00 43.07 ? 1243 HOH C O   1 
HETATM 20765 O  O   . HOH Y 4 .   ? 20.797  37.487  69.056  1.00 39.59 ? 1244 HOH C O   1 
HETATM 20766 O  O   . HOH Y 4 .   ? 30.960  38.127  66.236  1.00 27.48 ? 1245 HOH C O   1 
HETATM 20767 O  O   . HOH Y 4 .   ? 32.882  25.995  57.009  1.00 25.40 ? 1246 HOH C O   1 
HETATM 20768 O  O   . HOH Y 4 .   ? 30.811  35.189  47.878  1.00 44.24 ? 1247 HOH C O   1 
HETATM 20769 O  O   . HOH Y 4 .   ? 38.995  20.148  91.076  1.00 38.16 ? 1248 HOH C O   1 
HETATM 20770 O  O   . HOH Y 4 .   ? 28.446  39.678  72.699  1.00 30.09 ? 1249 HOH C O   1 
HETATM 20771 O  O   . HOH Y 4 .   ? 45.565  15.954  57.598  1.00 30.14 ? 1250 HOH C O   1 
HETATM 20772 O  O   . HOH Y 4 .   ? 30.372  38.540  98.818  1.00 43.51 ? 1251 HOH C O   1 
HETATM 20773 O  O   . HOH Y 4 .   ? 8.350   18.646  93.325  1.00 38.21 ? 1252 HOH C O   1 
HETATM 20774 O  O   . HOH Y 4 .   ? 43.161  16.383  58.915  1.00 23.87 ? 1253 HOH C O   1 
HETATM 20775 O  O   . HOH Y 4 .   ? 20.829  15.512  63.663  1.00 19.82 ? 1254 HOH C O   1 
HETATM 20776 O  O   . HOH Y 4 .   ? 19.304  42.839  109.727 1.00 40.71 ? 1255 HOH C O   1 
HETATM 20777 O  O   . HOH Y 4 .   ? 15.989  5.655   56.699  1.00 37.43 ? 1256 HOH C O   1 
HETATM 20778 O  O   . HOH Y 4 .   ? 38.983  20.598  94.929  1.00 34.06 ? 1257 HOH C O   1 
HETATM 20779 O  O   . HOH Y 4 .   ? 13.217  1.037   108.472 1.00 42.45 ? 1258 HOH C O   1 
HETATM 20780 O  O   . HOH Y 4 .   ? 15.730  25.915  67.586  1.00 28.57 ? 1259 HOH C O   1 
HETATM 20781 O  O   . HOH Y 4 .   ? 27.826  28.151  52.350  1.00 32.74 ? 1260 HOH C O   1 
HETATM 20782 O  O   . HOH Y 4 .   ? 31.966  37.303  73.809  1.00 23.82 ? 1261 HOH C O   1 
HETATM 20783 O  O   . HOH Y 4 .   ? 27.547  43.815  88.605  1.00 36.44 ? 1262 HOH C O   1 
HETATM 20784 O  O   . HOH Y 4 .   ? 13.826  26.886  71.420  1.00 28.77 ? 1263 HOH C O   1 
HETATM 20785 O  O   . HOH Y 4 .   ? 39.300  22.960  82.557  1.00 39.51 ? 1264 HOH C O   1 
HETATM 20786 O  O   . HOH Y 4 .   ? 13.026  0.567   65.828  1.00 36.88 ? 1265 HOH C O   1 
HETATM 20787 O  O   . HOH Y 4 .   ? 33.275  39.883  107.785 1.00 39.69 ? 1266 HOH C O   1 
HETATM 20788 O  O   . HOH Y 4 .   ? 51.063  17.980  55.096  1.00 39.52 ? 1267 HOH C O   1 
HETATM 20789 O  O   . HOH Y 4 .   ? 24.860  51.509  85.089  1.00 47.90 ? 1268 HOH C O   1 
HETATM 20790 O  O   . HOH Y 4 .   ? 9.415   19.047  102.530 1.00 25.79 ? 1269 HOH C O   1 
HETATM 20791 O  O   . HOH Y 4 .   ? 36.634  -3.127  79.681  1.00 40.72 ? 1270 HOH C O   1 
HETATM 20792 O  O   . HOH Y 4 .   ? 6.811   17.206  96.831  1.00 42.35 ? 1271 HOH C O   1 
HETATM 20793 O  O   . HOH Y 4 .   ? 32.908  -10.583 55.116  1.00 39.86 ? 1272 HOH C O   1 
HETATM 20794 O  O   . HOH Y 4 .   ? 22.851  39.995  93.876  1.00 40.70 ? 1273 HOH C O   1 
HETATM 20795 O  O   . HOH Y 4 .   ? 38.338  35.184  63.468  1.00 45.49 ? 1274 HOH C O   1 
HETATM 20796 O  O   . HOH Y 4 .   ? 31.724  32.278  90.485  1.00 25.07 ? 1275 HOH C O   1 
HETATM 20797 O  O   . HOH Y 4 .   ? 59.755  6.810   56.653  1.00 43.47 ? 1276 HOH C O   1 
HETATM 20798 O  O   . HOH Y 4 .   ? 54.423  17.948  65.549  1.00 39.57 ? 1277 HOH C O   1 
HETATM 20799 O  O   . HOH Y 4 .   ? 21.525  39.705  70.780  1.00 38.07 ? 1278 HOH C O   1 
HETATM 20800 O  O   . HOH Y 4 .   ? 33.407  39.032  114.196 1.00 39.51 ? 1279 HOH C O   1 
HETATM 20801 O  O   . HOH Y 4 .   ? 13.226  26.278  69.315  1.00 41.56 ? 1280 HOH C O   1 
HETATM 20802 O  O   . HOH Y 4 .   ? 6.690   24.840  72.252  1.00 37.25 ? 1281 HOH C O   1 
HETATM 20803 O  O   . HOH Y 4 .   ? 32.366  26.432  54.323  1.00 33.91 ? 1282 HOH C O   1 
HETATM 20804 O  O   . HOH Y 4 .   ? 23.221  41.241  107.877 1.00 30.38 ? 1283 HOH C O   1 
HETATM 20805 O  O   . HOH Y 4 .   ? 24.701  42.413  69.185  1.00 42.13 ? 1284 HOH C O   1 
HETATM 20806 O  O   . HOH Y 4 .   ? 30.961  36.610  97.685  1.00 43.77 ? 1285 HOH C O   1 
HETATM 20807 O  O   . HOH Y 4 .   ? 7.163   32.861  87.015  1.00 30.68 ? 1286 HOH C O   1 
HETATM 20808 O  O   . HOH Y 4 .   ? 15.238  48.309  96.162  1.00 32.06 ? 1287 HOH C O   1 
HETATM 20809 O  O   . HOH Y 4 .   ? 19.111  35.199  71.685  1.00 33.87 ? 1288 HOH C O   1 
HETATM 20810 O  O   . HOH Y 4 .   ? 30.120  38.082  116.995 1.00 50.03 ? 1289 HOH C O   1 
HETATM 20811 O  O   . HOH Y 4 .   ? 21.094  34.453  69.314  1.00 41.74 ? 1290 HOH C O   1 
HETATM 20812 O  O   . HOH Y 4 .   ? 23.564  -8.003  61.475  1.00 30.94 ? 1291 HOH C O   1 
HETATM 20813 O  O   . HOH Y 4 .   ? 35.342  37.883  71.754  1.00 36.37 ? 1292 HOH C O   1 
HETATM 20814 O  O   . HOH Y 4 .   ? 15.757  32.556  74.815  1.00 39.98 ? 1293 HOH C O   1 
HETATM 20815 O  O   . HOH Y 4 .   ? 36.809  27.505  74.952  1.00 37.42 ? 1294 HOH C O   1 
HETATM 20816 O  O   . HOH Y 4 .   ? 31.751  39.014  69.073  1.00 32.50 ? 1295 HOH C O   1 
HETATM 20817 O  O   . HOH Y 4 .   ? 48.432  26.650  61.577  1.00 28.61 ? 1296 HOH C O   1 
HETATM 20818 O  O   . HOH Y 4 .   ? 0.340   15.537  102.095 1.00 38.00 ? 1297 HOH C O   1 
HETATM 20819 O  O   . HOH Y 4 .   ? 26.919  38.866  109.549 1.00 45.48 ? 1298 HOH C O   1 
HETATM 20820 O  O   . HOH Y 4 .   ? 33.903  10.722  51.443  1.00 34.23 ? 1299 HOH C O   1 
HETATM 20821 O  O   . HOH Y 4 .   ? 26.351  -3.063  55.718  1.00 35.96 ? 1300 HOH C O   1 
HETATM 20822 O  O   . HOH Y 4 .   ? 35.299  33.957  65.441  1.00 38.67 ? 1301 HOH C O   1 
HETATM 20823 O  O   . HOH Y 4 .   ? 3.383   21.365  81.200  1.00 30.84 ? 1302 HOH C O   1 
HETATM 20824 O  O   . HOH Y 4 .   ? 9.193   23.367  68.032  1.00 39.75 ? 1303 HOH C O   1 
HETATM 20825 O  O   . HOH Y 4 .   ? 4.896   20.130  114.773 1.00 28.59 ? 1304 HOH C O   1 
HETATM 20826 O  O   . HOH Y 4 .   ? 15.098  9.321   113.941 1.00 29.44 ? 1305 HOH C O   1 
HETATM 20827 O  O   . HOH Y 4 .   ? 25.845  17.653  54.685  1.00 45.50 ? 1306 HOH C O   1 
HETATM 20828 O  O   . HOH Y 4 .   ? 1.944   20.322  82.451  1.00 31.78 ? 1307 HOH C O   1 
HETATM 20829 O  O   . HOH Y 4 .   ? 62.126  3.625   76.300  1.00 32.53 ? 1308 HOH C O   1 
HETATM 20830 O  O   . HOH Y 4 .   ? 49.909  27.494  63.668  1.00 50.33 ? 1309 HOH C O   1 
HETATM 20831 O  O   . HOH Z 4 .   ? 27.187  -23.507 76.924  1.00 41.52 ? 801  HOH D O   1 
HETATM 20832 O  O   . HOH Z 4 .   ? -0.542  -23.474 75.154  1.00 35.39 ? 802  HOH D O   1 
HETATM 20833 O  O   . HOH Z 4 .   ? 50.502  17.873  126.023 1.00 42.42 ? 803  HOH D O   1 
HETATM 20834 O  O   . HOH Z 4 .   ? 55.405  15.585  104.608 1.00 40.12 ? 804  HOH D O   1 
HETATM 20835 O  O   . HOH Z 4 .   ? 27.645  -22.714 117.723 1.00 53.68 ? 805  HOH D O   1 
HETATM 20836 O  O   . HOH Z 4 .   ? 25.684  3.643   108.582 1.00 43.94 ? 806  HOH D O   1 
HETATM 20837 O  O   . HOH Z 4 .   ? 47.505  23.478  119.745 1.00 45.50 ? 807  HOH D O   1 
HETATM 20838 O  O   . HOH Z 4 .   ? 25.186  -32.038 106.607 1.00 36.78 ? 808  HOH D O   1 
HETATM 20839 O  O   . HOH Z 4 .   ? 59.008  13.430  111.911 1.00 37.95 ? 809  HOH D O   1 
HETATM 20840 O  O   . HOH Z 4 .   ? -6.285  4.358   107.920 1.00 28.99 ? 810  HOH D O   1 
HETATM 20841 O  O   . HOH Z 4 .   ? 5.432   -6.615  71.430  1.00 15.17 ? 811  HOH D O   1 
HETATM 20842 O  O   . HOH Z 4 .   ? 28.912  3.148   108.829 1.00 25.18 ? 812  HOH D O   1 
HETATM 20843 O  O   . HOH Z 4 .   ? -20.232 1.947   80.415  1.00 34.00 ? 813  HOH D O   1 
HETATM 20844 O  O   . HOH Z 4 .   ? 34.069  -27.404 103.423 1.00 42.29 ? 814  HOH D O   1 
HETATM 20845 O  O   . HOH Z 4 .   ? -1.954  -8.255  109.091 1.00 36.86 ? 815  HOH D O   1 
HETATM 20846 O  O   . HOH Z 4 .   ? 30.910  6.522   118.221 1.00 31.83 ? 816  HOH D O   1 
HETATM 20847 O  O   . HOH Z 4 .   ? 31.251  11.157  94.780  1.00 15.50 ? 817  HOH D O   1 
HETATM 20848 O  O   . HOH Z 4 .   ? -2.500  -5.555  110.684 1.00 36.78 ? 818  HOH D O   1 
HETATM 20849 O  O   . HOH Z 4 .   ? -20.823 -6.466  100.732 1.00 46.63 ? 819  HOH D O   1 
HETATM 20850 O  O   . HOH Z 4 .   ? -7.273  11.800  87.044  1.00 36.54 ? 820  HOH D O   1 
HETATM 20851 O  O   . HOH Z 4 .   ? 46.424  -6.376  125.080 1.00 27.19 ? 821  HOH D O   1 
HETATM 20852 O  O   . HOH Z 4 .   ? 17.030  -6.207  112.849 1.00 33.62 ? 822  HOH D O   1 
HETATM 20853 O  O   . HOH Z 4 .   ? 50.908  3.318   106.311 1.00 27.99 ? 823  HOH D O   1 
HETATM 20854 O  O   . HOH Z 4 .   ? 31.075  -22.223 97.881  1.00 20.41 ? 824  HOH D O   1 
HETATM 20855 O  O   . HOH Z 4 .   ? 3.525   -0.527  84.210  1.00 30.62 ? 825  HOH D O   1 
HETATM 20856 O  O   . HOH Z 4 .   ? 41.320  -8.780  92.226  1.00 34.59 ? 826  HOH D O   1 
HETATM 20857 O  O   . HOH Z 4 .   ? -9.508  8.563   103.483 1.00 33.62 ? 827  HOH D O   1 
HETATM 20858 O  O   . HOH Z 4 .   ? 16.662  -23.274 74.101  1.00 44.56 ? 828  HOH D O   1 
HETATM 20859 O  O   . HOH Z 4 .   ? 37.335  -11.137 85.807  1.00 28.44 ? 829  HOH D O   1 
HETATM 20860 O  O   . HOH Z 4 .   ? 37.498  -4.282  83.448  1.00 50.34 ? 830  HOH D O   1 
HETATM 20861 O  O   . HOH Z 4 .   ? 28.944  -9.591  112.553 1.00 25.56 ? 831  HOH D O   1 
HETATM 20862 O  O   . HOH Z 4 .   ? 11.973  -19.570 79.378  1.00 20.83 ? 832  HOH D O   1 
HETATM 20863 O  O   . HOH Z 4 .   ? 24.932  -37.888 102.948 1.00 41.03 ? 833  HOH D O   1 
HETATM 20864 O  O   . HOH Z 4 .   ? 56.915  19.823  114.481 1.00 50.24 ? 834  HOH D O   1 
HETATM 20865 O  O   . HOH Z 4 .   ? -17.049 -6.329  87.893  1.00 37.81 ? 835  HOH D O   1 
HETATM 20866 O  O   . HOH Z 4 .   ? 50.757  -3.545  117.883 1.00 38.33 ? 836  HOH D O   1 
HETATM 20867 O  O   . HOH Z 4 .   ? 5.162   -22.024 88.099  1.00 15.29 ? 837  HOH D O   1 
HETATM 20868 O  O   . HOH Z 4 .   ? 34.169  -3.290  87.865  1.00 14.13 ? 838  HOH D O   1 
HETATM 20869 O  O   . HOH Z 4 .   ? 29.919  -23.793 85.537  1.00 32.59 ? 839  HOH D O   1 
HETATM 20870 O  O   . HOH Z 4 .   ? 43.559  15.793  89.458  1.00 38.61 ? 840  HOH D O   1 
HETATM 20871 O  O   . HOH Z 4 .   ? 43.876  -1.024  125.598 1.00 42.37 ? 841  HOH D O   1 
HETATM 20872 O  O   . HOH Z 4 .   ? 14.334  -15.617 104.699 1.00 34.89 ? 842  HOH D O   1 
HETATM 20873 O  O   . HOH Z 4 .   ? 5.119   -11.948 96.146  1.00 18.42 ? 843  HOH D O   1 
HETATM 20874 O  O   . HOH Z 4 .   ? 34.837  -24.421 95.111  1.00 33.44 ? 844  HOH D O   1 
HETATM 20875 O  O   . HOH Z 4 .   ? 24.825  4.048   90.772  1.00 35.35 ? 845  HOH D O   1 
HETATM 20876 O  O   . HOH Z 4 .   ? 8.442   -5.555  95.902  1.00 15.79 ? 846  HOH D O   1 
HETATM 20877 O  O   . HOH Z 4 .   ? 5.233   -0.569  72.991  1.00 40.55 ? 847  HOH D O   1 
HETATM 20878 O  O   . HOH Z 4 .   ? -9.118  -15.839 99.889  1.00 29.00 ? 848  HOH D O   1 
HETATM 20879 O  O   . HOH Z 4 .   ? -2.949  3.805   110.406 1.00 29.00 ? 849  HOH D O   1 
HETATM 20880 O  O   . HOH Z 4 .   ? -5.485  -6.828  110.485 1.00 30.98 ? 850  HOH D O   1 
HETATM 20881 O  O   . HOH Z 4 .   ? 41.193  -12.622 100.799 1.00 28.25 ? 851  HOH D O   1 
HETATM 20882 O  O   . HOH Z 4 .   ? 24.431  -19.877 105.429 1.00 25.91 ? 852  HOH D O   1 
HETATM 20883 O  O   . HOH Z 4 .   ? -1.929  -23.277 103.158 1.00 20.42 ? 853  HOH D O   1 
HETATM 20884 O  O   . HOH Z 4 .   ? 12.553  -13.163 99.244  1.00 20.67 ? 854  HOH D O   1 
HETATM 20885 O  O   . HOH Z 4 .   ? 24.300  -14.048 102.972 1.00 26.64 ? 855  HOH D O   1 
HETATM 20886 O  O   . HOH Z 4 .   ? 20.843  -16.903 99.624  1.00 19.15 ? 856  HOH D O   1 
HETATM 20887 O  O   . HOH Z 4 .   ? 42.196  8.968   85.913  1.00 18.35 ? 857  HOH D O   1 
HETATM 20888 O  O   . HOH Z 4 .   ? 7.022   -24.962 93.925  1.00 28.91 ? 858  HOH D O   1 
HETATM 20889 O  O   . HOH Z 4 .   ? 39.508  18.867  107.356 1.00 31.75 ? 859  HOH D O   1 
HETATM 20890 O  O   . HOH Z 4 .   ? 31.676  15.091  110.707 1.00 24.05 ? 860  HOH D O   1 
HETATM 20891 O  O   . HOH Z 4 .   ? 30.135  -10.202 116.535 1.00 38.09 ? 861  HOH D O   1 
HETATM 20892 O  O   . HOH Z 4 .   ? 9.048   1.179   72.853  1.00 29.78 ? 862  HOH D O   1 
HETATM 20893 O  O   . HOH Z 4 .   ? 36.535  -6.015  124.802 1.00 23.77 ? 863  HOH D O   1 
HETATM 20894 O  O   . HOH Z 4 .   ? 23.107  -25.141 85.783  1.00 29.23 ? 864  HOH D O   1 
HETATM 20895 O  O   . HOH Z 4 .   ? 2.779   2.738   105.061 1.00 16.88 ? 865  HOH D O   1 
HETATM 20896 O  O   . HOH Z 4 .   ? 45.265  2.477   100.490 1.00 20.48 ? 866  HOH D O   1 
HETATM 20897 O  O   . HOH Z 4 .   ? -0.632  -15.699 73.421  1.00 29.21 ? 867  HOH D O   1 
HETATM 20898 O  O   . HOH Z 4 .   ? 29.839  -6.197  109.558 1.00 21.59 ? 868  HOH D O   1 
HETATM 20899 O  O   . HOH Z 4 .   ? 42.000  -2.077  103.755 1.00 16.23 ? 869  HOH D O   1 
HETATM 20900 O  O   . HOH Z 4 .   ? 30.918  -4.411  95.323  1.00 12.10 ? 870  HOH D O   1 
HETATM 20901 O  O   . HOH Z 4 .   ? 29.084  -25.909 97.830  1.00 43.51 ? 871  HOH D O   1 
HETATM 20902 O  O   . HOH Z 4 .   ? 4.433   1.295   85.507  1.00 32.63 ? 872  HOH D O   1 
HETATM 20903 O  O   . HOH Z 4 .   ? -2.633  -17.975 93.665  1.00 21.86 ? 873  HOH D O   1 
HETATM 20904 O  O   . HOH Z 4 .   ? 8.773   -5.515  67.900  1.00 26.38 ? 874  HOH D O   1 
HETATM 20905 O  O   . HOH Z 4 .   ? 9.692   0.988   106.565 1.00 30.79 ? 875  HOH D O   1 
HETATM 20906 O  O   . HOH Z 4 .   ? 6.661   -4.757  73.318  1.00 18.44 ? 876  HOH D O   1 
HETATM 20907 O  O   . HOH Z 4 .   ? 16.339  -20.548 87.927  1.00 19.08 ? 877  HOH D O   1 
HETATM 20908 O  O   . HOH Z 4 .   ? 26.364  -18.328 77.256  1.00 45.33 ? 878  HOH D O   1 
HETATM 20909 O  O   . HOH Z 4 .   ? 16.346  -9.204  107.591 1.00 30.08 ? 879  HOH D O   1 
HETATM 20910 O  O   . HOH Z 4 .   ? 17.315  -24.820 87.664  1.00 36.63 ? 880  HOH D O   1 
HETATM 20911 O  O   . HOH Z 4 .   ? 9.753   -2.699  106.454 1.00 35.93 ? 881  HOH D O   1 
HETATM 20912 O  O   . HOH Z 4 .   ? -5.988  9.699   87.985  1.00 38.55 ? 882  HOH D O   1 
HETATM 20913 O  O   . HOH Z 4 .   ? -5.933  -12.776 103.346 1.00 18.01 ? 883  HOH D O   1 
HETATM 20914 O  O   . HOH Z 4 .   ? -1.226  -2.416  108.442 1.00 23.52 ? 884  HOH D O   1 
HETATM 20915 O  O   . HOH Z 4 .   ? 6.992   -15.392 100.160 1.00 26.33 ? 885  HOH D O   1 
HETATM 20916 O  O   . HOH Z 4 .   ? 39.780  -22.729 100.281 1.00 33.61 ? 886  HOH D O   1 
HETATM 20917 O  O   . HOH Z 4 .   ? 36.446  -8.565  122.355 1.00 29.80 ? 887  HOH D O   1 
HETATM 20918 O  O   . HOH Z 4 .   ? 12.664  -3.429  103.207 1.00 13.94 ? 888  HOH D O   1 
HETATM 20919 O  O   . HOH Z 4 .   ? 15.405  -42.341 100.238 1.00 50.16 ? 889  HOH D O   1 
HETATM 20920 O  O   . HOH Z 4 .   ? 7.906   -25.682 91.789  1.00 35.01 ? 890  HOH D O   1 
HETATM 20921 O  O   . HOH Z 4 .   ? 31.226  -6.877  114.311 1.00 28.88 ? 891  HOH D O   1 
HETATM 20922 O  O   . HOH Z 4 .   ? 9.986   -33.428 104.872 1.00 43.99 ? 892  HOH D O   1 
HETATM 20923 O  O   . HOH Z 4 .   ? 54.860  4.636   86.509  1.00 24.83 ? 893  HOH D O   1 
HETATM 20924 O  O   . HOH Z 4 .   ? -1.625  -20.873 91.383  1.00 23.49 ? 894  HOH D O   1 
HETATM 20925 O  O   . HOH Z 4 .   ? 19.422  -3.674  111.509 1.00 35.82 ? 895  HOH D O   1 
HETATM 20926 O  O   . HOH Z 4 .   ? 43.347  0.472   103.066 1.00 17.16 ? 896  HOH D O   1 
HETATM 20927 O  O   . HOH Z 4 .   ? 40.620  20.305  111.470 1.00 39.79 ? 897  HOH D O   1 
HETATM 20928 O  O   . HOH Z 4 .   ? -2.205  9.393   102.816 1.00 25.24 ? 898  HOH D O   1 
HETATM 20929 O  O   . HOH Z 4 .   ? 5.249   3.647   107.491 1.00 18.70 ? 899  HOH D O   1 
HETATM 20930 O  O   . HOH Z 4 .   ? 17.641  -12.520 103.503 1.00 26.38 ? 900  HOH D O   1 
HETATM 20931 O  O   . HOH Z 4 .   ? 49.465  5.361   103.907 1.00 25.05 ? 901  HOH D O   1 
HETATM 20932 O  O   . HOH Z 4 .   ? 46.205  0.095   85.424  1.00 46.33 ? 902  HOH D O   1 
HETATM 20933 O  O   . HOH Z 4 .   ? 6.896   -24.129 90.239  1.00 26.49 ? 903  HOH D O   1 
HETATM 20934 O  O   . HOH Z 4 .   ? -3.582  -7.189  82.505  1.00 15.11 ? 904  HOH D O   1 
HETATM 20935 O  O   . HOH Z 4 .   ? 26.839  -0.326  86.407  1.00 11.70 ? 905  HOH D O   1 
HETATM 20936 O  O   . HOH Z 4 .   ? 54.264  8.507   121.312 1.00 23.47 ? 906  HOH D O   1 
HETATM 20937 O  O   . HOH Z 4 .   ? 30.272  5.379   110.939 1.00 26.92 ? 907  HOH D O   1 
HETATM 20938 O  O   . HOH Z 4 .   ? 42.374  -4.247  122.703 1.00 29.11 ? 908  HOH D O   1 
HETATM 20939 O  O   . HOH Z 4 .   ? 35.458  11.498  106.206 1.00 17.87 ? 909  HOH D O   1 
HETATM 20940 O  O   . HOH Z 4 .   ? 7.270   5.579   92.724  1.00 33.63 ? 910  HOH D O   1 
HETATM 20941 O  O   . HOH Z 4 .   ? -6.823  12.563  91.829  1.00 42.96 ? 911  HOH D O   1 
HETATM 20942 O  O   . HOH Z 4 .   ? 54.271  12.329  126.873 1.00 31.97 ? 912  HOH D O   1 
HETATM 20943 O  O   . HOH Z 4 .   ? 37.537  2.013   108.942 1.00 18.66 ? 913  HOH D O   1 
HETATM 20944 O  O   . HOH Z 4 .   ? -5.135  -18.533 93.834  1.00 24.21 ? 914  HOH D O   1 
HETATM 20945 O  O   . HOH Z 4 .   ? 55.192  7.337   100.029 1.00 30.19 ? 915  HOH D O   1 
HETATM 20946 O  O   . HOH Z 4 .   ? 54.601  1.201   111.263 1.00 30.94 ? 916  HOH D O   1 
HETATM 20947 O  O   . HOH Z 4 .   ? -5.749  -12.423 71.805  1.00 36.44 ? 917  HOH D O   1 
HETATM 20948 O  O   . HOH Z 4 .   ? 46.917  2.294   88.751  1.00 20.02 ? 918  HOH D O   1 
HETATM 20949 O  O   . HOH Z 4 .   ? 4.989   -17.376 99.099  1.00 19.05 ? 919  HOH D O   1 
HETATM 20950 O  O   . HOH Z 4 .   ? 40.109  15.713  119.799 1.00 30.99 ? 920  HOH D O   1 
HETATM 20951 O  O   . HOH Z 4 .   ? 31.019  -26.173 107.134 1.00 29.59 ? 921  HOH D O   1 
HETATM 20952 O  O   . HOH Z 4 .   ? 27.177  -8.153  106.237 1.00 14.46 ? 922  HOH D O   1 
HETATM 20953 O  O   . HOH Z 4 .   ? 13.428  -2.346  65.192  1.00 24.65 ? 923  HOH D O   1 
HETATM 20954 O  O   . HOH Z 4 .   ? 4.658   0.122   81.850  1.00 17.76 ? 924  HOH D O   1 
HETATM 20955 O  O   . HOH Z 4 .   ? 13.918  -17.991 92.436  1.00 16.54 ? 925  HOH D O   1 
HETATM 20956 O  O   . HOH Z 4 .   ? 54.636  3.485   94.207  1.00 32.41 ? 926  HOH D O   1 
HETATM 20957 O  O   . HOH Z 4 .   ? 18.008  -3.844  94.917  1.00 15.77 ? 927  HOH D O   1 
HETATM 20958 O  O   . HOH Z 4 .   ? 7.901   1.763   100.943 1.00 16.25 ? 928  HOH D O   1 
HETATM 20959 O  O   A HOH Z 4 .   ? 39.251  4.317   101.171 0.50 15.96 ? 929  HOH D O   1 
HETATM 20960 O  O   B HOH Z 4 .   ? 39.982  5.996   100.918 0.50 19.87 ? 929  HOH D O   1 
HETATM 20961 O  O   . HOH Z 4 .   ? -10.470 -10.364 83.265  1.00 27.23 ? 930  HOH D O   1 
HETATM 20962 O  O   . HOH Z 4 .   ? 37.859  -13.673 118.024 1.00 39.29 ? 931  HOH D O   1 
HETATM 20963 O  O   . HOH Z 4 .   ? 13.991  -1.147  93.707  1.00 25.20 ? 932  HOH D O   1 
HETATM 20964 O  O   . HOH Z 4 .   ? 37.918  9.217   104.277 1.00 16.27 ? 933  HOH D O   1 
HETATM 20965 O  O   . HOH Z 4 .   ? -0.217  10.080  94.366  1.00 32.51 ? 934  HOH D O   1 
HETATM 20966 O  O   . HOH Z 4 .   ? 7.571   2.597   105.236 1.00 14.26 ? 935  HOH D O   1 
HETATM 20967 O  O   . HOH Z 4 .   ? 1.436   -28.383 103.883 1.00 27.51 ? 936  HOH D O   1 
HETATM 20968 O  O   . HOH Z 4 .   ? 17.113  3.420   77.894  1.00 12.17 ? 937  HOH D O   1 
HETATM 20969 O  O   . HOH Z 4 .   ? -11.611 -3.057  108.456 1.00 40.53 ? 938  HOH D O   1 
HETATM 20970 O  O   . HOH Z 4 .   ? 8.229   -22.402 73.745  1.00 27.78 ? 939  HOH D O   1 
HETATM 20971 O  O   . HOH Z 4 .   ? 13.510  -6.004  106.023 1.00 17.39 ? 940  HOH D O   1 
HETATM 20972 O  O   . HOH Z 4 .   ? 7.064   -10.300 95.936  1.00 18.46 ? 941  HOH D O   1 
HETATM 20973 O  O   . HOH Z 4 .   ? 8.503   -9.950  103.245 1.00 15.45 ? 942  HOH D O   1 
HETATM 20974 O  O   . HOH Z 4 .   ? 35.457  9.210   88.912  1.00 18.49 ? 943  HOH D O   1 
HETATM 20975 O  O   . HOH Z 4 .   ? -16.075 -19.412 94.043  1.00 33.39 ? 944  HOH D O   1 
HETATM 20976 O  O   . HOH Z 4 .   ? 34.474  2.172   108.665 1.00 20.10 ? 945  HOH D O   1 
HETATM 20977 O  O   . HOH Z 4 .   ? 0.029   3.324   87.974  1.00 25.13 ? 946  HOH D O   1 
HETATM 20978 O  O   . HOH Z 4 .   ? -17.186 0.321   102.295 1.00 31.21 ? 947  HOH D O   1 
HETATM 20979 O  O   . HOH Z 4 .   ? 15.246  -3.596  94.823  1.00 16.25 ? 948  HOH D O   1 
HETATM 20980 O  O   . HOH Z 4 .   ? 26.485  -12.508 101.731 1.00 33.36 ? 949  HOH D O   1 
HETATM 20981 O  O   . HOH Z 4 .   ? 0.565   -25.037 93.787  1.00 31.24 ? 950  HOH D O   1 
HETATM 20982 O  O   . HOH Z 4 .   ? 51.465  2.717   91.683  1.00 27.50 ? 951  HOH D O   1 
HETATM 20983 O  O   . HOH Z 4 .   ? 5.500   -3.025  69.829  1.00 37.97 ? 952  HOH D O   1 
HETATM 20984 O  O   . HOH Z 4 .   ? 19.658  -17.465 76.817  1.00 21.68 ? 953  HOH D O   1 
HETATM 20985 O  O   . HOH Z 4 .   ? 13.777  -19.726 89.125  1.00 19.37 ? 954  HOH D O   1 
HETATM 20986 O  O   . HOH Z 4 .   ? -3.729  10.054  107.195 1.00 25.93 ? 955  HOH D O   1 
HETATM 20987 O  O   . HOH Z 4 .   ? -11.972 4.244   99.197  1.00 18.93 ? 956  HOH D O   1 
HETATM 20988 O  O   . HOH Z 4 .   ? -0.430  -27.476 94.765  1.00 30.21 ? 957  HOH D O   1 
HETATM 20989 O  O   . HOH Z 4 .   ? 40.298  11.096  92.639  1.00 12.00 ? 958  HOH D O   1 
HETATM 20990 O  O   . HOH Z 4 .   ? -20.039 9.186   89.037  1.00 28.78 ? 959  HOH D O   1 
HETATM 20991 O  O   . HOH Z 4 .   ? 28.459  -13.079 93.643  1.00 17.83 ? 960  HOH D O   1 
HETATM 20992 O  O   . HOH Z 4 .   ? -0.117  -22.505 95.196  1.00 20.38 ? 961  HOH D O   1 
HETATM 20993 O  O   . HOH Z 4 .   ? 42.791  8.564   98.490  1.00 16.48 ? 962  HOH D O   1 
HETATM 20994 O  O   . HOH Z 4 .   ? -7.908  -22.785 99.642  1.00 24.44 ? 963  HOH D O   1 
HETATM 20995 O  O   . HOH Z 4 .   ? 25.225  -5.711  79.779  1.00 11.55 ? 964  HOH D O   1 
HETATM 20996 O  O   . HOH Z 4 .   ? 7.499   -0.931  74.170  1.00 23.90 ? 965  HOH D O   1 
HETATM 20997 O  O   . HOH Z 4 .   ? 37.447  18.663  119.807 1.00 29.63 ? 966  HOH D O   1 
HETATM 20998 O  O   . HOH Z 4 .   ? 20.503  -13.600 104.484 1.00 29.63 ? 967  HOH D O   1 
HETATM 20999 O  O   . HOH Z 4 .   ? 61.914  10.985  117.507 1.00 28.39 ? 968  HOH D O   1 
HETATM 21000 O  O   . HOH Z 4 .   ? -0.142  -32.793 98.282  1.00 41.35 ? 969  HOH D O   1 
HETATM 21001 O  O   . HOH Z 4 .   ? -21.619 -0.583  93.185  1.00 38.09 ? 970  HOH D O   1 
HETATM 21002 O  O   . HOH Z 4 .   ? 20.542  -22.764 78.101  1.00 39.88 ? 971  HOH D O   1 
HETATM 21003 O  O   . HOH Z 4 .   ? 25.659  -10.652 77.233  1.00 23.95 ? 972  HOH D O   1 
HETATM 21004 O  O   . HOH Z 4 .   ? 8.735   -27.128 104.228 1.00 28.63 ? 973  HOH D O   1 
HETATM 21005 O  O   . HOH Z 4 .   ? 47.987  19.233  91.823  1.00 34.87 ? 974  HOH D O   1 
HETATM 21006 O  O   . HOH Z 4 .   ? 22.290  -31.772 90.108  1.00 44.64 ? 975  HOH D O   1 
HETATM 21007 O  O   . HOH Z 4 .   ? 23.349  0.545   85.197  1.00 15.95 ? 976  HOH D O   1 
HETATM 21008 O  O   . HOH Z 4 .   ? 46.033  15.665  101.275 1.00 24.73 ? 977  HOH D O   1 
HETATM 21009 O  O   . HOH Z 4 .   ? 40.190  10.480  123.028 1.00 23.34 ? 978  HOH D O   1 
HETATM 21010 O  O   . HOH Z 4 .   ? 26.850  -12.080 105.049 1.00 19.73 ? 979  HOH D O   1 
HETATM 21011 O  O   . HOH Z 4 .   ? 38.725  2.672   92.935  1.00 13.10 ? 980  HOH D O   1 
HETATM 21012 O  O   . HOH Z 4 .   ? 4.931   1.060   106.678 1.00 29.77 ? 981  HOH D O   1 
HETATM 21013 O  O   . HOH Z 4 .   ? -16.654 6.479   94.865  1.00 22.99 ? 982  HOH D O   1 
HETATM 21014 O  O   . HOH Z 4 .   ? 57.148  9.545   106.088 1.00 25.83 ? 983  HOH D O   1 
HETATM 21015 O  O   . HOH Z 4 .   ? 15.338  -27.810 88.746  1.00 28.70 ? 984  HOH D O   1 
HETATM 21016 O  O   . HOH Z 4 .   ? 37.926  -11.352 90.219  1.00 37.82 ? 985  HOH D O   1 
HETATM 21017 O  O   . HOH Z 4 .   ? 22.537  2.701   110.953 1.00 26.74 ? 986  HOH D O   1 
HETATM 21018 O  O   . HOH Z 4 .   ? -13.679 4.074   97.066  1.00 20.71 ? 987  HOH D O   1 
HETATM 21019 O  O   . HOH Z 4 .   ? 31.444  9.522   106.911 1.00 15.84 ? 988  HOH D O   1 
HETATM 21020 O  O   . HOH Z 4 .   ? 37.872  -10.040 116.891 1.00 22.14 ? 989  HOH D O   1 
HETATM 21021 O  O   . HOH Z 4 .   ? 55.907  12.860  95.333  1.00 44.15 ? 990  HOH D O   1 
HETATM 21022 O  O   . HOH Z 4 .   ? 27.246  4.700   113.024 1.00 42.91 ? 991  HOH D O   1 
HETATM 21023 O  O   . HOH Z 4 .   ? 36.437  8.699   102.142 1.00 14.34 ? 992  HOH D O   1 
HETATM 21024 O  O   . HOH Z 4 .   ? 20.422  -15.423 102.622 1.00 33.89 ? 993  HOH D O   1 
HETATM 21025 O  O   . HOH Z 4 .   ? -0.306  7.853   108.566 1.00 26.34 ? 994  HOH D O   1 
HETATM 21026 O  O   . HOH Z 4 .   ? 22.188  -16.970 102.926 1.00 33.20 ? 995  HOH D O   1 
HETATM 21027 O  O   . HOH Z 4 .   ? 26.147  -25.005 91.856  1.00 20.53 ? 996  HOH D O   1 
HETATM 21028 O  O   . HOH Z 4 .   ? 1.297   3.511   94.884  1.00 15.57 ? 997  HOH D O   1 
HETATM 21029 O  O   . HOH Z 4 .   ? 7.810   -7.807  94.528  1.00 17.47 ? 998  HOH D O   1 
HETATM 21030 O  O   . HOH Z 4 .   ? 13.977  -25.820 96.972  1.00 28.06 ? 999  HOH D O   1 
HETATM 21031 O  O   . HOH Z 4 .   ? 59.226  6.163   113.067 1.00 35.69 ? 1000 HOH D O   1 
HETATM 21032 O  O   . HOH Z 4 .   ? 26.608  -29.540 98.544  1.00 41.65 ? 1001 HOH D O   1 
HETATM 21033 O  O   . HOH Z 4 .   ? 14.555  -18.843 103.377 1.00 38.34 ? 1002 HOH D O   1 
HETATM 21034 O  O   . HOH Z 4 .   ? 42.074  -0.344  110.589 1.00 21.20 ? 1003 HOH D O   1 
HETATM 21035 O  O   . HOH Z 4 .   ? 12.545  -1.979  90.517  1.00 15.94 ? 1004 HOH D O   1 
HETATM 21036 O  O   . HOH Z 4 .   ? 11.897  -15.793 70.933  1.00 23.27 ? 1005 HOH D O   1 
HETATM 21037 O  O   . HOH Z 4 .   ? 13.755  -20.173 106.632 1.00 50.08 ? 1006 HOH D O   1 
HETATM 21038 O  O   . HOH Z 4 .   ? 28.679  -20.231 79.927  1.00 43.54 ? 1007 HOH D O   1 
HETATM 21039 O  O   . HOH Z 4 .   ? 48.233  -12.451 124.386 1.00 34.86 ? 1008 HOH D O   1 
HETATM 21040 O  O   . HOH Z 4 .   ? 48.506  -0.020  107.541 1.00 26.08 ? 1009 HOH D O   1 
HETATM 21041 O  O   . HOH Z 4 .   ? 26.474  -27.612 101.637 1.00 25.36 ? 1010 HOH D O   1 
HETATM 21042 O  O   . HOH Z 4 .   ? 7.397   -16.321 70.330  1.00 31.53 ? 1011 HOH D O   1 
HETATM 21043 O  O   . HOH Z 4 .   ? 19.306  -40.447 93.302  1.00 37.96 ? 1012 HOH D O   1 
HETATM 21044 O  O   . HOH Z 4 .   ? 15.200  -0.681  107.107 1.00 28.87 ? 1013 HOH D O   1 
HETATM 21045 O  O   . HOH Z 4 .   ? 30.155  7.771   96.690  1.00 17.03 ? 1014 HOH D O   1 
HETATM 21046 O  O   . HOH Z 4 .   ? 34.864  -11.880 87.088  1.00 26.47 ? 1015 HOH D O   1 
HETATM 21047 O  O   . HOH Z 4 .   ? -0.886  -0.926  74.799  1.00 30.47 ? 1016 HOH D O   1 
HETATM 21048 O  O   . HOH Z 4 .   ? -6.198  -23.398 97.054  1.00 23.07 ? 1017 HOH D O   1 
HETATM 21049 O  O   . HOH Z 4 .   ? 46.324  17.768  108.796 1.00 40.02 ? 1018 HOH D O   1 
HETATM 21050 O  O   . HOH Z 4 .   ? 12.929  -19.866 101.879 1.00 24.71 ? 1019 HOH D O   1 
HETATM 21051 O  O   . HOH Z 4 .   ? -21.979 3.226   90.748  1.00 32.94 ? 1020 HOH D O   1 
HETATM 21052 O  O   . HOH Z 4 .   ? -0.955  2.280   110.232 1.00 32.81 ? 1021 HOH D O   1 
HETATM 21053 O  O   . HOH Z 4 .   ? 44.565  1.450   97.015  1.00 29.69 ? 1022 HOH D O   1 
HETATM 21054 O  O   . HOH Z 4 .   ? 23.484  -2.039  111.717 1.00 30.08 ? 1023 HOH D O   1 
HETATM 21055 O  O   . HOH Z 4 .   ? -19.140 9.954   94.267  1.00 43.11 ? 1024 HOH D O   1 
HETATM 21056 O  O   . HOH Z 4 .   ? 29.344  -5.555  117.999 1.00 30.34 ? 1025 HOH D O   1 
HETATM 21057 O  O   . HOH Z 4 .   ? 47.545  17.183  106.074 1.00 38.96 ? 1026 HOH D O   1 
HETATM 21058 O  O   . HOH Z 4 .   ? 6.538   -14.797 95.728  1.00 24.41 ? 1027 HOH D O   1 
HETATM 21059 O  O   . HOH Z 4 .   ? 1.009   -14.895 105.364 1.00 27.99 ? 1028 HOH D O   1 
HETATM 21060 O  O   . HOH Z 4 .   ? 43.485  -3.197  95.772  1.00 27.81 ? 1029 HOH D O   1 
HETATM 21061 O  O   . HOH Z 4 .   ? 34.921  -12.756 113.970 1.00 24.39 ? 1030 HOH D O   1 
HETATM 21062 O  O   . HOH Z 4 .   ? 40.512  -19.572 91.125  1.00 28.28 ? 1031 HOH D O   1 
HETATM 21063 O  O   . HOH Z 4 .   ? 9.892   -30.863 91.007  1.00 49.06 ? 1032 HOH D O   1 
HETATM 21064 O  O   . HOH Z 4 .   ? -3.220  -22.629 76.139  1.00 38.85 ? 1033 HOH D O   1 
HETATM 21065 O  O   . HOH Z 4 .   ? 38.389  6.305   129.433 1.00 29.95 ? 1034 HOH D O   1 
HETATM 21066 O  O   . HOH Z 4 .   ? 4.551   -25.259 79.294  1.00 32.73 ? 1035 HOH D O   1 
HETATM 21067 O  O   . HOH Z 4 .   ? 33.910  -15.188 114.739 1.00 31.28 ? 1036 HOH D O   1 
HETATM 21068 O  O   . HOH Z 4 .   ? 57.855  9.845   125.021 1.00 39.64 ? 1037 HOH D O   1 
HETATM 21069 O  O   . HOH Z 4 .   ? 37.038  8.814   129.503 1.00 24.39 ? 1038 HOH D O   1 
HETATM 21070 O  O   . HOH Z 4 .   ? 11.391  -22.971 81.391  1.00 29.48 ? 1039 HOH D O   1 
HETATM 21071 O  O   . HOH Z 4 .   ? -9.813  3.102   108.262 1.00 32.68 ? 1040 HOH D O   1 
HETATM 21072 O  O   . HOH Z 4 .   ? 47.126  14.901  104.351 1.00 20.81 ? 1041 HOH D O   1 
HETATM 21073 O  O   . HOH Z 4 .   ? 19.881  2.004   86.005  1.00 11.67 ? 1042 HOH D O   1 
HETATM 21074 O  O   . HOH Z 4 .   ? -0.439  1.003   93.645  1.00 16.90 ? 1043 HOH D O   1 
HETATM 21075 O  O   . HOH Z 4 .   ? -0.863  10.641  87.319  1.00 46.55 ? 1044 HOH D O   1 
HETATM 21076 O  O   . HOH Z 4 .   ? 29.474  -16.487 85.862  1.00 21.11 ? 1045 HOH D O   1 
HETATM 21077 O  O   . HOH Z 4 .   ? 38.740  -22.083 118.387 1.00 36.60 ? 1046 HOH D O   1 
HETATM 21078 O  O   . HOH Z 4 .   ? 0.303   -20.140 108.520 1.00 46.97 ? 1047 HOH D O   1 
HETATM 21079 O  O   . HOH Z 4 .   ? 33.467  -23.090 99.287  1.00 34.79 ? 1048 HOH D O   1 
HETATM 21080 O  O   . HOH Z 4 .   ? -20.286 4.637   84.073  1.00 29.58 ? 1049 HOH D O   1 
HETATM 21081 O  O   . HOH Z 4 .   ? 39.655  -9.844  100.617 1.00 23.40 ? 1050 HOH D O   1 
HETATM 21082 O  O   . HOH Z 4 .   ? -2.303  -10.502 69.981  1.00 43.05 ? 1051 HOH D O   1 
HETATM 21083 O  O   . HOH Z 4 .   ? 24.898  -29.853 108.118 1.00 38.54 ? 1052 HOH D O   1 
HETATM 21084 O  O   . HOH Z 4 .   ? 7.889   1.234   85.060  1.00 11.95 ? 1053 HOH D O   1 
HETATM 21085 O  O   . HOH Z 4 .   ? 29.813  -20.300 116.002 1.00 33.30 ? 1054 HOH D O   1 
HETATM 21086 O  O   . HOH Z 4 .   ? 5.258   -19.931 99.841  1.00 16.75 ? 1055 HOH D O   1 
HETATM 21087 O  O   . HOH Z 4 .   ? 22.781  3.176   91.919  1.00 19.52 ? 1056 HOH D O   1 
HETATM 21088 O  O   . HOH Z 4 .   ? 39.951  -22.328 90.181  1.00 19.18 ? 1057 HOH D O   1 
HETATM 21089 O  O   . HOH Z 4 .   ? -8.183  6.089   93.271  1.00 20.79 ? 1058 HOH D O   1 
HETATM 21090 O  O   . HOH Z 4 .   ? -2.727  -11.878 71.929  1.00 21.06 ? 1059 HOH D O   1 
HETATM 21091 O  O   . HOH Z 4 .   ? 24.437  3.783   88.252  1.00 17.25 ? 1060 HOH D O   1 
HETATM 21092 O  O   . HOH Z 4 .   ? 50.105  -1.882  122.845 1.00 29.95 ? 1061 HOH D O   1 
HETATM 21093 O  O   . HOH Z 4 .   ? -18.053 2.070   98.313  1.00 27.36 ? 1062 HOH D O   1 
HETATM 21094 O  O   . HOH Z 4 .   ? -9.601  -12.172 79.217  1.00 27.35 ? 1063 HOH D O   1 
HETATM 21095 O  O   . HOH Z 4 .   ? 23.892  -18.339 111.964 1.00 33.95 ? 1064 HOH D O   1 
HETATM 21096 O  O   . HOH Z 4 .   ? 28.520  -14.914 83.755  1.00 21.35 ? 1065 HOH D O   1 
HETATM 21097 O  O   . HOH Z 4 .   ? -11.511 13.491  88.597  1.00 35.49 ? 1066 HOH D O   1 
HETATM 21098 O  O   . HOH Z 4 .   ? -5.119  4.572   103.448 1.00 18.28 ? 1067 HOH D O   1 
HETATM 21099 O  O   . HOH Z 4 .   ? 42.661  18.443  107.670 1.00 27.67 ? 1068 HOH D O   1 
HETATM 21100 O  O   . HOH Z 4 .   ? -13.785 -7.964  102.194 1.00 32.01 ? 1069 HOH D O   1 
HETATM 21101 O  O   . HOH Z 4 .   ? 33.423  -10.665 85.262  1.00 16.08 ? 1070 HOH D O   1 
HETATM 21102 O  O   . HOH Z 4 .   ? 20.951  -25.812 87.256  1.00 28.15 ? 1071 HOH D O   1 
HETATM 21103 O  O   . HOH Z 4 .   ? 6.968   -18.695 71.560  1.00 31.75 ? 1072 HOH D O   1 
HETATM 21104 O  O   . HOH Z 4 .   ? -6.339  2.726   101.866 1.00 17.40 ? 1073 HOH D O   1 
HETATM 21105 O  O   . HOH Z 4 .   ? 1.946   -9.665  106.769 1.00 23.38 ? 1074 HOH D O   1 
HETATM 21106 O  O   . HOH Z 4 .   ? 30.522  -25.103 81.354  1.00 45.46 ? 1075 HOH D O   1 
HETATM 21107 O  O   . HOH Z 4 .   ? -20.445 -7.237  90.890  1.00 40.00 ? 1076 HOH D O   1 
HETATM 21108 O  O   . HOH Z 4 .   ? 8.439   3.664   91.283  1.00 35.55 ? 1077 HOH D O   1 
HETATM 21109 O  O   . HOH Z 4 .   ? 35.855  2.411   130.354 1.00 45.42 ? 1078 HOH D O   1 
HETATM 21110 O  O   . HOH Z 4 .   ? 42.649  -9.776  128.479 1.00 34.38 ? 1079 HOH D O   1 
HETATM 21111 O  O   . HOH Z 4 .   ? 52.403  21.836  114.596 1.00 38.41 ? 1080 HOH D O   1 
HETATM 21112 O  O   . HOH Z 4 .   ? 24.419  -40.196 100.830 1.00 40.01 ? 1081 HOH D O   1 
HETATM 21113 O  O   . HOH Z 4 .   ? -1.003  -0.851  82.423  1.00 22.59 ? 1082 HOH D O   1 
HETATM 21114 O  O   . HOH Z 4 .   ? 5.151   -4.176  102.067 1.00 15.58 ? 1083 HOH D O   1 
HETATM 21115 O  O   . HOH Z 4 .   ? -2.395  2.717   78.060  1.00 24.09 ? 1084 HOH D O   1 
HETATM 21116 O  O   . HOH Z 4 .   ? 1.920   -22.293 74.481  1.00 29.24 ? 1085 HOH D O   1 
HETATM 21117 O  O   . HOH Z 4 .   ? 43.340  21.937  120.175 1.00 51.99 ? 1086 HOH D O   1 
HETATM 21118 O  O   . HOH Z 4 .   ? 45.410  -6.618  86.761  1.00 53.23 ? 1087 HOH D O   1 
HETATM 21119 O  O   . HOH Z 4 .   ? 45.719  -10.594 125.892 1.00 36.34 ? 1088 HOH D O   1 
HETATM 21120 O  O   . HOH Z 4 .   ? 49.996  1.481   93.012  1.00 41.53 ? 1089 HOH D O   1 
HETATM 21121 O  O   . HOH Z 4 .   ? 22.996  -19.621 103.053 1.00 26.84 ? 1090 HOH D O   1 
HETATM 21122 O  O   . HOH Z 4 .   ? 28.339  -7.105  111.724 1.00 26.02 ? 1091 HOH D O   1 
HETATM 21123 O  O   . HOH Z 4 .   ? 16.780  -20.437 85.157  1.00 18.61 ? 1092 HOH D O   1 
HETATM 21124 O  O   . HOH Z 4 .   ? 54.919  8.781   102.450 1.00 26.78 ? 1093 HOH D O   1 
HETATM 21125 O  O   . HOH Z 4 .   ? 29.521  5.135   96.701  1.00 15.10 ? 1094 HOH D O   1 
HETATM 21126 O  O   . HOH Z 4 .   ? 1.044   -25.726 104.824 1.00 25.34 ? 1095 HOH D O   1 
HETATM 21127 O  O   . HOH Z 4 .   ? 42.965  18.168  100.794 1.00 16.65 ? 1096 HOH D O   1 
HETATM 21128 O  O   . HOH Z 4 .   ? -16.641 3.491   79.535  1.00 46.92 ? 1097 HOH D O   1 
HETATM 21129 O  O   . HOH Z 4 .   ? 16.157  -8.528  64.219  1.00 20.68 ? 1098 HOH D O   1 
HETATM 21130 O  O   . HOH Z 4 .   ? 3.082   -24.821 81.401  1.00 21.30 ? 1099 HOH D O   1 
HETATM 21131 O  O   . HOH Z 4 .   ? 13.814  -16.903 100.963 1.00 24.52 ? 1100 HOH D O   1 
HETATM 21132 O  O   . HOH Z 4 .   ? 9.291   -13.763 68.909  1.00 36.81 ? 1101 HOH D O   1 
HETATM 21133 O  O   . HOH Z 4 .   ? 13.466  -15.297 97.230  1.00 16.67 ? 1102 HOH D O   1 
HETATM 21134 O  O   . HOH Z 4 .   ? 44.242  16.839  105.925 1.00 27.09 ? 1103 HOH D O   1 
HETATM 21135 O  O   . HOH Z 4 .   ? 23.414  -11.599 76.313  1.00 25.49 ? 1104 HOH D O   1 
HETATM 21136 O  O   . HOH Z 4 .   ? 40.656  11.476  106.494 1.00 17.75 ? 1105 HOH D O   1 
HETATM 21137 O  O   . HOH Z 4 .   ? 9.874   -11.349 68.926  1.00 34.41 ? 1106 HOH D O   1 
HETATM 21138 O  O   . HOH Z 4 .   ? 18.705  -30.199 88.465  1.00 33.83 ? 1107 HOH D O   1 
HETATM 21139 O  O   . HOH Z 4 .   ? 41.403  -5.960  92.224  1.00 15.46 ? 1108 HOH D O   1 
HETATM 21140 O  O   . HOH Z 4 .   ? 6.514   -25.343 87.538  1.00 34.79 ? 1109 HOH D O   1 
HETATM 21141 O  O   . HOH Z 4 .   ? -6.315  -30.972 100.257 1.00 35.04 ? 1110 HOH D O   1 
HETATM 21142 O  O   . HOH Z 4 .   ? -9.065  12.261  93.971  1.00 26.04 ? 1111 HOH D O   1 
HETATM 21143 O  O   . HOH Z 4 .   ? 13.056  -14.244 101.414 1.00 21.90 ? 1112 HOH D O   1 
HETATM 21144 O  O   . HOH Z 4 .   ? -8.265  7.156   106.084 1.00 35.66 ? 1113 HOH D O   1 
HETATM 21145 O  O   . HOH Z 4 .   ? 15.468  -18.169 108.674 1.00 43.71 ? 1114 HOH D O   1 
HETATM 21146 O  O   . HOH Z 4 .   ? 37.415  6.849   99.912  1.00 15.99 ? 1115 HOH D O   1 
HETATM 21147 O  O   . HOH Z 4 .   ? 7.388   -27.458 95.377  1.00 20.56 ? 1116 HOH D O   1 
HETATM 21148 O  O   . HOH Z 4 .   ? -6.657  -23.807 82.123  1.00 43.93 ? 1117 HOH D O   1 
HETATM 21149 O  O   . HOH Z 4 .   ? -4.189  -29.018 101.410 1.00 35.31 ? 1118 HOH D O   1 
HETATM 21150 O  O   . HOH Z 4 .   ? 42.361  -11.161 102.678 1.00 39.31 ? 1119 HOH D O   1 
HETATM 21151 O  O   . HOH Z 4 .   ? 10.158  -11.524 105.029 1.00 35.13 ? 1120 HOH D O   1 
HETATM 21152 O  O   . HOH Z 4 .   ? 7.339   -13.605 105.673 1.00 43.11 ? 1121 HOH D O   1 
HETATM 21153 O  O   . HOH Z 4 .   ? 7.504   7.135   80.487  1.00 35.77 ? 1122 HOH D O   1 
HETATM 21154 O  O   . HOH Z 4 .   ? 37.092  -12.577 115.692 1.00 26.47 ? 1123 HOH D O   1 
HETATM 21155 O  O   . HOH Z 4 .   ? 34.518  8.931   125.395 1.00 33.98 ? 1124 HOH D O   1 
HETATM 21156 O  O   . HOH Z 4 .   ? 37.674  1.126   84.330  1.00 35.23 ? 1125 HOH D O   1 
HETATM 21157 O  O   . HOH Z 4 .   ? 5.223   -16.767 95.839  1.00 46.14 ? 1126 HOH D O   1 
HETATM 21158 O  O   . HOH Z 4 .   ? -2.631  10.234  78.358  1.00 40.48 ? 1127 HOH D O   1 
HETATM 21159 O  O   . HOH Z 4 .   ? 42.479  19.089  110.663 1.00 29.77 ? 1128 HOH D O   1 
HETATM 21160 O  O   . HOH Z 4 .   ? -5.034  -20.627 76.627  1.00 34.27 ? 1129 HOH D O   1 
HETATM 21161 O  O   . HOH Z 4 .   ? 10.211  -23.229 105.248 1.00 31.96 ? 1130 HOH D O   1 
HETATM 21162 O  O   . HOH Z 4 .   ? -20.524 -13.315 100.770 1.00 33.67 ? 1131 HOH D O   1 
HETATM 21163 O  O   . HOH Z 4 .   ? 49.065  -8.280  106.936 1.00 33.75 ? 1132 HOH D O   1 
HETATM 21164 O  O   . HOH Z 4 .   ? 12.001  -1.573  104.724 1.00 26.71 ? 1133 HOH D O   1 
HETATM 21165 O  O   . HOH Z 4 .   ? 54.574  6.415   123.202 1.00 33.29 ? 1134 HOH D O   1 
HETATM 21166 O  O   . HOH Z 4 .   ? -16.248 -13.261 85.767  1.00 36.82 ? 1135 HOH D O   1 
HETATM 21167 O  O   . HOH Z 4 .   ? 58.304  12.199  106.905 1.00 25.68 ? 1136 HOH D O   1 
HETATM 21168 O  O   . HOH Z 4 .   ? 13.536  -25.983 75.436  1.00 43.48 ? 1137 HOH D O   1 
HETATM 21169 O  O   . HOH Z 4 .   ? -6.258  10.341  103.340 1.00 34.10 ? 1138 HOH D O   1 
HETATM 21170 O  O   . HOH Z 4 .   ? 27.957  6.217   119.091 1.00 55.73 ? 1139 HOH D O   1 
HETATM 21171 O  O   . HOH Z 4 .   ? 27.005  -23.173 95.243  1.00 49.56 ? 1140 HOH D O   1 
HETATM 21172 O  O   . HOH Z 4 .   ? 45.204  -2.775  123.899 1.00 37.03 ? 1141 HOH D O   1 
HETATM 21173 O  O   . HOH Z 4 .   ? 14.690  -27.800 85.855  1.00 44.52 ? 1142 HOH D O   1 
HETATM 21174 O  O   . HOH Z 4 .   ? 35.403  -23.755 97.855  1.00 28.60 ? 1143 HOH D O   1 
HETATM 21175 O  O   . HOH Z 4 .   ? 28.671  -3.699  123.426 1.00 36.36 ? 1144 HOH D O   1 
HETATM 21176 O  O   . HOH Z 4 .   ? 8.476   -2.526  72.038  1.00 16.14 ? 1145 HOH D O   1 
HETATM 21177 O  O   . HOH Z 4 .   ? 28.288  -23.668 79.691  1.00 37.60 ? 1146 HOH D O   1 
HETATM 21178 O  O   . HOH Z 4 .   ? 38.625  14.565  122.428 1.00 39.50 ? 1147 HOH D O   1 
HETATM 21179 O  O   . HOH Z 4 .   ? 34.218  9.272   107.280 1.00 14.58 ? 1148 HOH D O   1 
HETATM 21180 O  O   . HOH Z 4 .   ? 42.436  -17.231 90.672  1.00 40.59 ? 1149 HOH D O   1 
HETATM 21181 O  O   . HOH Z 4 .   ? -6.117  5.853   105.514 1.00 17.81 ? 1150 HOH D O   1 
HETATM 21182 O  O   . HOH Z 4 .   ? 37.963  -21.567 87.676  1.00 26.98 ? 1151 HOH D O   1 
HETATM 21183 O  O   . HOH Z 4 .   ? -9.609  -6.761  108.454 1.00 27.28 ? 1152 HOH D O   1 
HETATM 21184 O  O   . HOH Z 4 .   ? 35.509  -23.179 86.608  1.00 16.77 ? 1153 HOH D O   1 
HETATM 21185 O  O   . HOH Z 4 .   ? 31.618  -22.098 117.323 1.00 46.29 ? 1154 HOH D O   1 
HETATM 21186 O  O   . HOH Z 4 .   ? 23.912  -9.724  113.353 1.00 39.22 ? 1155 HOH D O   1 
HETATM 21187 O  O   . HOH Z 4 .   ? 2.638   -9.899  109.355 1.00 38.92 ? 1156 HOH D O   1 
HETATM 21188 O  O   . HOH Z 4 .   ? 17.270  -15.228 71.184  1.00 46.79 ? 1157 HOH D O   1 
HETATM 21189 O  O   . HOH Z 4 .   ? 2.814   2.675   83.928  1.00 38.24 ? 1158 HOH D O   1 
HETATM 21190 O  O   . HOH Z 4 .   ? 1.526   -0.174  73.980  1.00 39.30 ? 1159 HOH D O   1 
HETATM 21191 O  O   . HOH Z 4 .   ? -9.608  -9.328  106.295 1.00 15.49 ? 1160 HOH D O   1 
HETATM 21192 O  O   . HOH Z 4 .   ? 19.246  -22.131 74.644  1.00 32.82 ? 1161 HOH D O   1 
HETATM 21193 O  O   . HOH Z 4 .   ? 41.578  -5.893  89.299  1.00 35.93 ? 1162 HOH D O   1 
HETATM 21194 O  O   . HOH Z 4 .   ? 13.518  -18.718 71.391  1.00 34.45 ? 1163 HOH D O   1 
HETATM 21195 O  O   . HOH Z 4 .   ? -6.811  -11.412 105.448 1.00 32.75 ? 1164 HOH D O   1 
HETATM 21196 O  O   . HOH Z 4 .   ? -17.584 4.017   94.536  1.00 19.59 ? 1165 HOH D O   1 
HETATM 21197 O  O   . HOH Z 4 .   ? 28.917  -6.390  115.313 1.00 33.44 ? 1166 HOH D O   1 
HETATM 21198 O  O   . HOH Z 4 .   ? 39.891  18.941  93.695  1.00 24.46 ? 1167 HOH D O   1 
HETATM 21199 O  O   A HOH Z 4 .   ? 8.978   -13.280 101.889 0.51 14.53 ? 1168 HOH D O   1 
HETATM 21200 O  O   B HOH Z 4 .   ? 7.525   -13.159 103.296 0.49 12.36 ? 1168 HOH D O   1 
HETATM 21201 O  O   . HOH Z 4 .   ? 10.107  -25.095 103.605 1.00 26.91 ? 1169 HOH D O   1 
HETATM 21202 O  O   . HOH Z 4 .   ? 47.229  6.434   128.439 1.00 38.22 ? 1170 HOH D O   1 
HETATM 21203 O  O   . HOH Z 4 .   ? -12.479 5.885   79.505  1.00 33.66 ? 1171 HOH D O   1 
HETATM 21204 O  O   . HOH Z 4 .   ? 16.232  -11.394 106.044 1.00 30.93 ? 1172 HOH D O   1 
HETATM 21205 O  O   . HOH Z 4 .   ? 12.844  -8.861  66.645  1.00 40.58 ? 1173 HOH D O   1 
HETATM 21206 O  O   . HOH Z 4 .   ? -4.744  -18.023 73.024  1.00 34.01 ? 1174 HOH D O   1 
HETATM 21207 O  O   . HOH Z 4 .   ? 40.541  -23.232 111.442 1.00 30.52 ? 1175 HOH D O   1 
HETATM 21208 O  O   . HOH Z 4 .   ? 28.259  1.118   129.268 1.00 35.53 ? 1176 HOH D O   1 
HETATM 21209 O  O   . HOH Z 4 .   ? 37.513  -24.606 99.574  1.00 38.29 ? 1177 HOH D O   1 
HETATM 21210 O  O   . HOH Z 4 .   ? 6.057   -29.831 95.317  1.00 35.93 ? 1178 HOH D O   1 
HETATM 21211 O  O   . HOH Z 4 .   ? 21.357  -13.461 70.087  1.00 35.78 ? 1179 HOH D O   1 
HETATM 21212 O  O   . HOH Z 4 .   ? 46.515  21.068  95.925  1.00 33.19 ? 1180 HOH D O   1 
HETATM 21213 O  O   . HOH Z 4 .   ? 40.665  -6.773  84.201  1.00 48.25 ? 1181 HOH D O   1 
HETATM 21214 O  O   . HOH Z 4 .   ? 15.505  -23.401 96.951  1.00 23.11 ? 1182 HOH D O   1 
HETATM 21215 O  O   . HOH Z 4 .   ? -1.941  -21.027 93.760  1.00 30.89 ? 1183 HOH D O   1 
HETATM 21216 O  O   . HOH Z 4 .   ? -9.423  -24.148 97.856  1.00 34.87 ? 1184 HOH D O   1 
HETATM 21217 O  O   . HOH Z 4 .   ? 17.881  -32.563 107.233 1.00 33.45 ? 1185 HOH D O   1 
HETATM 21218 O  O   . HOH Z 4 .   ? 25.537  2.250   110.472 1.00 33.94 ? 1186 HOH D O   1 
HETATM 21219 O  O   . HOH Z 4 .   ? 38.592  -24.855 90.498  1.00 26.08 ? 1187 HOH D O   1 
HETATM 21220 O  O   . HOH Z 4 .   ? 30.420  18.375  104.617 1.00 25.84 ? 1188 HOH D O   1 
HETATM 21221 O  O   . HOH Z 4 .   ? 25.264  2.078   86.417  1.00 14.17 ? 1189 HOH D O   1 
HETATM 21222 O  O   . HOH Z 4 .   ? -21.351 -0.419  95.722  1.00 33.78 ? 1190 HOH D O   1 
HETATM 21223 O  O   . HOH Z 4 .   ? 34.670  8.762   109.911 1.00 21.83 ? 1191 HOH D O   1 
HETATM 21224 O  O   . HOH Z 4 .   ? -2.177  -30.670 102.170 1.00 28.40 ? 1192 HOH D O   1 
HETATM 21225 O  O   . HOH Z 4 .   ? -21.621 7.174   88.157  1.00 30.82 ? 1193 HOH D O   1 
HETATM 21226 O  O   . HOH Z 4 .   ? 56.806  1.595   112.888 1.00 33.25 ? 1194 HOH D O   1 
HETATM 21227 O  O   . HOH Z 4 .   ? 6.622   -26.639 80.213  1.00 41.45 ? 1195 HOH D O   1 
HETATM 21228 O  O   . HOH Z 4 .   ? 56.721  10.991  127.142 1.00 29.08 ? 1196 HOH D O   1 
HETATM 21229 O  O   . HOH Z 4 .   ? 3.795   -24.072 74.723  1.00 34.68 ? 1197 HOH D O   1 
HETATM 21230 O  O   . HOH Z 4 .   ? 8.975   -1.942  67.718  1.00 30.24 ? 1198 HOH D O   1 
HETATM 21231 O  O   . HOH Z 4 .   ? 26.987  -32.413 102.562 1.00 39.43 ? 1199 HOH D O   1 
HETATM 21232 O  O   . HOH Z 4 .   ? 17.913  -22.975 84.501  1.00 33.86 ? 1200 HOH D O   1 
HETATM 21233 O  O   . HOH Z 4 .   ? 12.610  -3.253  106.735 1.00 44.41 ? 1201 HOH D O   1 
HETATM 21234 O  O   . HOH Z 4 .   ? -4.690  -21.405 94.393  1.00 40.03 ? 1202 HOH D O   1 
HETATM 21235 O  O   . HOH Z 4 .   ? -12.138 7.029   99.880  1.00 25.21 ? 1203 HOH D O   1 
HETATM 21236 O  O   . HOH Z 4 .   ? 20.452  -28.503 87.409  1.00 32.47 ? 1204 HOH D O   1 
HETATM 21237 O  O   . HOH Z 4 .   ? 56.391  4.338   120.210 1.00 30.96 ? 1205 HOH D O   1 
HETATM 21238 O  O   . HOH Z 4 .   ? 0.462   -29.970 94.643  1.00 35.65 ? 1206 HOH D O   1 
HETATM 21239 O  O   . HOH Z 4 .   ? -14.313 -21.426 93.816  1.00 43.35 ? 1207 HOH D O   1 
HETATM 21240 O  O   . HOH Z 4 .   ? 33.732  8.123   123.507 1.00 38.17 ? 1208 HOH D O   1 
HETATM 21241 O  O   . HOH Z 4 .   ? 7.878   -31.350 95.140  1.00 37.33 ? 1209 HOH D O   1 
HETATM 21242 O  O   . HOH Z 4 .   ? -3.845  10.557  104.433 1.00 27.32 ? 1210 HOH D O   1 
HETATM 21243 O  O   . HOH Z 4 .   ? 26.582  -10.428 114.150 1.00 30.22 ? 1211 HOH D O   1 
HETATM 21244 O  O   . HOH Z 4 .   ? 43.869  -5.392  94.202  1.00 32.99 ? 1212 HOH D O   1 
HETATM 21245 O  O   . HOH Z 4 .   ? 14.087  -7.904  107.703 1.00 34.88 ? 1213 HOH D O   1 
HETATM 21246 O  O   . HOH Z 4 .   ? -5.611  -11.661 107.227 1.00 34.36 ? 1214 HOH D O   1 
HETATM 21247 O  O   . HOH Z 4 .   ? 47.164  1.398   98.777  1.00 35.93 ? 1215 HOH D O   1 
HETATM 21248 O  O   . HOH Z 4 .   ? -7.684  -14.687 104.107 1.00 33.93 ? 1216 HOH D O   1 
HETATM 21249 O  O   . HOH Z 4 .   ? -2.825  -17.232 71.916  1.00 38.29 ? 1217 HOH D O   1 
HETATM 21250 O  O   . HOH Z 4 .   ? -0.919  -30.211 104.629 1.00 40.64 ? 1218 HOH D O   1 
HETATM 21251 O  O   . HOH Z 4 .   ? 23.109  -3.292  113.737 1.00 36.27 ? 1219 HOH D O   1 
HETATM 21252 O  O   . HOH Z 4 .   ? 7.768   -1.852  69.711  1.00 36.63 ? 1220 HOH D O   1 
HETATM 21253 O  O   . HOH Z 4 .   ? -0.872  -13.565 71.729  1.00 33.08 ? 1221 HOH D O   1 
HETATM 21254 O  O   . HOH Z 4 .   ? 9.212   -1.640  108.658 1.00 37.12 ? 1222 HOH D O   1 
HETATM 21255 O  O   . HOH Z 4 .   ? -18.468 8.038   96.007  1.00 30.49 ? 1223 HOH D O   1 
HETATM 21256 O  O   . HOH Z 4 .   ? 7.216   1.124   70.511  1.00 45.53 ? 1224 HOH D O   1 
HETATM 21257 O  O   . HOH Z 4 .   ? -2.023  -0.215  110.253 1.00 30.73 ? 1225 HOH D O   1 
HETATM 21258 O  O   . HOH Z 4 .   ? -14.132 6.688   96.046  1.00 24.86 ? 1226 HOH D O   1 
HETATM 21259 O  O   . HOH Z 4 .   ? 32.912  -25.771 99.376  1.00 47.53 ? 1227 HOH D O   1 
HETATM 21260 O  O   . HOH Z 4 .   ? -13.052 12.414  83.334  1.00 29.70 ? 1228 HOH D O   1 
HETATM 21261 O  O   . HOH Z 4 .   ? 6.137   -6.243  68.924  1.00 35.23 ? 1229 HOH D O   1 
HETATM 21262 O  O   . HOH Z 4 .   ? -20.007 -8.817  101.050 1.00 45.44 ? 1230 HOH D O   1 
HETATM 21263 O  O   . HOH Z 4 .   ? 7.132   -16.007 107.121 1.00 45.55 ? 1231 HOH D O   1 
HETATM 21264 O  O   . HOH Z 4 .   ? 44.078  -4.871  124.801 1.00 32.74 ? 1232 HOH D O   1 
HETATM 21265 O  O   . HOH Z 4 .   ? -13.066 2.340   104.193 1.00 35.08 ? 1233 HOH D O   1 
HETATM 21266 O  O   . HOH Z 4 .   ? 38.070  22.909  112.594 1.00 48.23 ? 1234 HOH D O   1 
HETATM 21267 O  O   . HOH Z 4 .   ? 17.233  -0.125  109.383 1.00 41.03 ? 1235 HOH D O   1 
HETATM 21268 O  O   . HOH Z 4 .   ? -2.332  -24.239 105.437 1.00 34.47 ? 1236 HOH D O   1 
HETATM 21269 O  O   . HOH Z 4 .   ? 59.160  4.299   120.883 1.00 30.20 ? 1237 HOH D O   1 
HETATM 21270 O  O   . HOH Z 4 .   ? 6.946   1.757   73.966  1.00 43.68 ? 1238 HOH D O   1 
HETATM 21271 O  O   . HOH Z 4 .   ? -5.503  -27.469 103.268 1.00 35.87 ? 1239 HOH D O   1 
HETATM 21272 O  O   . HOH Z 4 .   ? 13.770  -17.594 106.016 1.00 36.66 ? 1240 HOH D O   1 
HETATM 21273 O  O   . HOH Z 4 .   ? -16.204 4.271   97.612  1.00 30.16 ? 1241 HOH D O   1 
HETATM 21274 O  O   . HOH Z 4 .   ? -1.438  7.815   110.889 1.00 36.70 ? 1242 HOH D O   1 
HETATM 21275 O  O   . HOH Z 4 .   ? 4.319   0.162   69.353  1.00 50.20 ? 1243 HOH D O   1 
HETATM 21276 O  O   . HOH Z 4 .   ? -20.315 1.984   97.112  1.00 34.97 ? 1244 HOH D O   1 
HETATM 21277 O  O   . HOH Z 4 .   ? -12.046 -5.351  108.885 1.00 34.86 ? 1245 HOH D O   1 
HETATM 21278 O  O   . HOH Z 4 .   ? 12.823  -1.822  108.932 1.00 32.04 ? 1246 HOH D O   1 
HETATM 21279 O  O   . HOH Z 4 .   ? 26.006  -30.256 100.860 1.00 34.57 ? 1247 HOH D O   1 
HETATM 21280 O  O   . HOH Z 4 .   ? 5.337   -15.504 69.120  1.00 45.07 ? 1248 HOH D O   1 
HETATM 21281 O  O   . HOH Z 4 .   ? -2.082  -32.822 100.705 1.00 34.64 ? 1249 HOH D O   1 
HETATM 21282 O  O   . HOH Z 4 .   ? -20.240 3.729   94.769  1.00 32.53 ? 1250 HOH D O   1 
HETATM 21283 O  O   . HOH Z 4 .   ? 32.633  -24.075 79.866  1.00 41.31 ? 1251 HOH D O   1 
HETATM 21284 O  O   . HOH Z 4 .   ? -14.005 8.142   98.122  1.00 29.34 ? 1252 HOH D O   1 
HETATM 21285 O  O   . HOH Z 4 .   ? -13.378 3.745   101.643 1.00 32.57 ? 1253 HOH D O   1 
HETATM 21286 O  O   . HOH Z 4 .   ? 39.306  -26.201 110.723 1.00 48.60 ? 1254 HOH D O   1 
HETATM 21287 O  O   . HOH Z 4 .   ? -15.874 4.558   100.979 1.00 39.84 ? 1255 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . SER A 10  ? 0.8449 1.0407 0.7385 0.1069  -0.0369 0.1428  2   SER A N   
2     C CA  . SER A 10  ? 0.7523 0.9212 0.6793 0.1075  -0.0234 0.1589  2   SER A CA  
3     C C   . SER A 10  ? 0.5789 0.7532 0.5189 0.0892  -0.0420 0.1388  2   SER A C   
4     O O   . SER A 10  ? 0.3609 0.5046 0.3173 0.0753  -0.0392 0.1350  2   SER A O   
5     C CB  . SER A 10  ? 0.8625 1.0500 0.8077 0.1350  -0.0036 0.1901  2   SER A CB  
6     O OG  . SER A 10  ? 0.8788 1.0374 0.8631 0.1345  0.0144  0.2034  2   SER A OG  
7     N N   . GLN A 11  ? 0.4347 0.6522 0.3708 0.0898  -0.0598 0.1254  3   GLN A N   
8     C CA  . GLN A 11  ? 0.3719 0.5979 0.3277 0.0739  -0.0743 0.1065  3   GLN A CA  
9     C C   . GLN A 11  ? 0.3446 0.5530 0.2968 0.0477  -0.0837 0.0778  3   GLN A C   
10    O O   . GLN A 11  ? 0.2748 0.4779 0.2485 0.0339  -0.0877 0.0675  3   GLN A O   
11    C CB  . GLN A 11  ? 0.4180 0.6962 0.3774 0.0802  -0.0889 0.0968  3   GLN A CB  
12    C CG  . GLN A 11  ? 0.4960 0.7971 0.4643 0.1076  -0.0775 0.1289  3   GLN A CG  
13    C CD  . GLN A 11  ? 0.5843 0.8539 0.5839 0.1119  -0.0600 0.1518  3   GLN A CD  
14    O OE1 . GLN A 11  ? 0.6043 0.8360 0.6102 0.1174  -0.0380 0.1709  3   GLN A OE1 
15    N NE2 . GLN A 11  ? 0.6702 0.9557 0.6952 0.1090  -0.0672 0.1478  3   GLN A NE2 
16    N N   . LEU A 12  ? 0.2663 0.4658 0.1944 0.0418  -0.0835 0.0673  4   LEU A N   
17    C CA  . LEU A 12  ? 0.2452 0.4269 0.1737 0.0184  -0.0866 0.0438  4   LEU A CA  
18    C C   . LEU A 12  ? 0.2383 0.3786 0.1767 0.0108  -0.0754 0.0549  4   LEU A C   
19    O O   . LEU A 12  ? 0.2511 0.3740 0.2034 -0.0065 -0.0734 0.0388  4   LEU A O   
20    C CB  . LEU A 12  ? 0.3267 0.5088 0.2296 0.0149  -0.0859 0.0308  4   LEU A CB  
21    C CG  . LEU A 12  ? 0.4194 0.6448 0.3144 0.0179  -0.0960 0.0104  4   LEU A CG  
22    C CD1 . LEU A 12  ? 0.4716 0.6931 0.3509 0.0053  -0.0935 -0.0131 4   LEU A CD1 
23    C CD2 . LEU A 12  ? 0.4187 0.6746 0.3431 0.0086  -0.1071 -0.0110 4   LEU A CD2 
24    N N   . ALA A 13  ? 0.2961 0.4139 0.2350 0.0238  -0.0616 0.0786  5   ALA A N   
25    C CA  . ALA A 13  ? 0.2580 0.3377 0.2171 0.0150  -0.0487 0.0781  5   ALA A CA  
26    C C   . ALA A 13  ? 0.2117 0.2944 0.1973 0.0153  -0.0472 0.0783  5   ALA A C   
27    O O   . ALA A 13  ? 0.2602 0.3288 0.2574 0.0030  -0.0450 0.0647  5   ALA A O   
28    C CB  . ALA A 13  ? 0.2792 0.3343 0.2425 0.0253  -0.0302 0.0957  5   ALA A CB  
29    N N   . ASN A 14  ? 0.2242 0.3290 0.2186 0.0323  -0.0468 0.0957  6   ASN A N   
30    C CA  . ASN A 14  ? 0.2708 0.3767 0.2940 0.0341  -0.0418 0.0979  6   ASN A CA  
31    C C   . ASN A 14  ? 0.2765 0.3940 0.3049 0.0190  -0.0544 0.0768  6   ASN A C   
32    O O   . ASN A 14  ? 0.2575 0.3625 0.3050 0.0138  -0.0470 0.0712  6   ASN A O   
33    C CB  . ASN A 14  ? 0.3029 0.4371 0.3365 0.0588  -0.0384 0.1254  6   ASN A CB  
34    C CG  . ASN A 14  ? 0.3336 0.4430 0.3858 0.0760  -0.0104 0.1519  6   ASN A CG  
35    O OD1 . ASN A 14  ? 0.3712 0.4421 0.4368 0.0650  0.0058  0.1422  6   ASN A OD1 
36    N ND2 . ASN A 14  ? 0.2992 0.4323 0.3571 0.1019  -0.0012 0.1811  6   ASN A ND2 
37    N N   . VAL A 15  ? 0.2166 0.3578 0.2327 0.0119  -0.0695 0.0634  7   VAL A N   
38    C CA  . VAL A 15  ? 0.2227 0.3710 0.2553 -0.0020 -0.0738 0.0447  7   VAL A CA  
39    C C   . VAL A 15  ? 0.1925 0.3069 0.2238 -0.0136 -0.0624 0.0371  7   VAL A C   
40    O O   . VAL A 15  ? 0.2118 0.3217 0.2590 -0.0169 -0.0561 0.0335  7   VAL A O   
41    C CB  . VAL A 15  ? 0.2544 0.4358 0.2865 -0.0099 -0.0871 0.0250  7   VAL A CB  
42    C CG1 . VAL A 15  ? 0.2178 0.3831 0.2273 -0.0186 -0.0848 0.0152  7   VAL A CG1 
43    C CG2 . VAL A 15  ? 0.2289 0.4176 0.2940 -0.0233 -0.0849 0.0068  7   VAL A CG2 
44    N N   . ILE A 16  ? 0.2181 0.3131 0.2301 -0.0170 -0.0589 0.0366  8   ILE A N   
45    C CA  . ILE A 16  ? 0.2073 0.2821 0.2167 -0.0225 -0.0495 0.0328  8   ILE A CA  
46    C C   . ILE A 16  ? 0.2346 0.3031 0.2539 -0.0177 -0.0426 0.0343  8   ILE A C   
47    O O   . ILE A 16  ? 0.2150 0.2840 0.2372 -0.0190 -0.0369 0.0285  8   ILE A O   
48    C CB  . ILE A 16  ? 0.2811 0.3421 0.2728 -0.0250 -0.0476 0.0333  8   ILE A CB  
49    C CG1 . ILE A 16  ? 0.3380 0.4031 0.3219 -0.0311 -0.0505 0.0273  8   ILE A CG1 
50    C CG2 . ILE A 16  ? 0.2824 0.3365 0.2722 -0.0266 -0.0404 0.0306  8   ILE A CG2 
51    C CD1 . ILE A 16  ? 0.4315 0.4814 0.3991 -0.0319 -0.0467 0.0302  8   ILE A CD1 
52    N N   . ARG A 17  ? 0.2701 0.3337 0.2963 -0.0108 -0.0391 0.0419  9   ARG A N   
53    C CA  . ARG A 17  ? 0.2964 0.3511 0.3421 -0.0086 -0.0268 0.0377  9   ARG A CA  
54    C C   . ARG A 17  ? 0.2720 0.3350 0.3322 -0.0074 -0.0240 0.0345  9   ARG A C   
55    O O   . ARG A 17  ? 0.2307 0.2934 0.2950 -0.0106 -0.0171 0.0204  9   ARG A O   
56    C CB  . ARG A 17  ? 0.3065 0.3519 0.3677 0.0015  -0.0161 0.0525  9   ARG A CB  
57    C CG  . ARG A 17  ? 0.3908 0.4235 0.4865 0.0036  0.0041  0.0476  9   ARG A CG  
58    C CD  . ARG A 17  ? 0.3867 0.4037 0.5030 0.0148  0.0229  0.0658  9   ARG A CD  
59    N NE  . ARG A 17  ? 0.3209 0.3244 0.4363 0.0074  0.0276  0.0557  9   ARG A NE  
60    C CZ  . ARG A 17  ? 0.3304 0.3291 0.4297 0.0148  0.0274  0.0733  9   ARG A CZ  
61    N NH1 . ARG A 17  ? 0.2854 0.2982 0.3635 0.0308  0.0208  0.1000  9   ARG A NH1 
62    N NH2 . ARG A 17  ? 0.3340 0.3195 0.4394 0.0071  0.0339  0.0627  9   ARG A NH2 
63    N N   . PHE A 18  ? 0.2284 0.3050 0.2963 -0.0020 -0.0298 0.0456  10  PHE A N   
64    C CA  . PHE A 18  ? 0.2331 0.3165 0.3216 0.0004  -0.0244 0.0451  10  PHE A CA  
65    C C   . PHE A 18  ? 0.2382 0.3294 0.3233 -0.0060 -0.0275 0.0372  10  PHE A C   
66    O O   . PHE A 18  ? 0.2422 0.3333 0.3395 -0.0046 -0.0181 0.0340  10  PHE A O   
67    C CB  . PHE A 18  ? 0.2028 0.3031 0.3106 0.0127  -0.0263 0.0633  10  PHE A CB  
68    C CG  . PHE A 18  ? 0.2837 0.3715 0.4056 0.0243  -0.0113 0.0779  10  PHE A CG  
69    C CD1 . PHE A 18  ? 0.4010 0.4690 0.5497 0.0245  0.0104  0.0723  10  PHE A CD1 
70    C CD2 . PHE A 18  ? 0.3301 0.4247 0.4418 0.0355  -0.0139 0.0958  10  PHE A CD2 
71    C CE1 . PHE A 18  ? 0.4222 0.4733 0.5969 0.0342  0.0327  0.0845  10  PHE A CE1 
72    C CE2 . PHE A 18  ? 0.3551 0.4339 0.4870 0.0492  0.0082  0.1143  10  PHE A CE2 
73    C CZ  . PHE A 18  ? 0.3975 0.4522 0.5656 0.0476  0.0333  0.1086  10  PHE A CZ  
74    N N   . LEU A 19  ? 0.2344 0.3301 0.3074 -0.0122 -0.0352 0.0344  11  LEU A N   
75    C CA  . LEU A 19  ? 0.2170 0.3124 0.2928 -0.0164 -0.0278 0.0299  11  LEU A CA  
76    C C   . LEU A 19  ? 0.2232 0.3110 0.2825 -0.0124 -0.0171 0.0277  11  LEU A C   
77    O O   . LEU A 19  ? 0.2253 0.3166 0.2888 -0.0078 -0.0054 0.0291  11  LEU A O   
78    C CB  . LEU A 19  ? 0.2507 0.3465 0.3221 -0.0239 -0.0305 0.0261  11  LEU A CB  
79    C CG  . LEU A 19  ? 0.2406 0.3504 0.3404 -0.0317 -0.0303 0.0174  11  LEU A CG  
80    C CD1 . LEU A 19  ? 0.1852 0.2842 0.2835 -0.0391 -0.0210 0.0123  11  LEU A CD1 
81    C CD2 . LEU A 19  ? 0.1956 0.3097 0.3264 -0.0301 -0.0179 0.0184  11  LEU A CD2 
82    N N   . SER A 20  ? 0.2105 0.2938 0.2522 -0.0127 -0.0204 0.0233  12  SER A N   
83    C CA  . SER A 20  ? 0.2115 0.3026 0.2379 -0.0085 -0.0145 0.0148  12  SER A CA  
84    C C   . SER A 20  ? 0.2222 0.3183 0.2593 -0.0055 -0.0066 0.0034  12  SER A C   
85    O O   . SER A 20  ? 0.2916 0.4021 0.3190 0.0015  0.0016  -0.0007 12  SER A O   
86    C CB  . SER A 20  ? 0.2642 0.3542 0.2798 -0.0118 -0.0207 0.0077  12  SER A CB  
87    O OG  . SER A 20  ? 0.2755 0.3592 0.2815 -0.0142 -0.0251 0.0180  12  SER A OG  
88    N N   . ALA A 21  ? 0.2227 0.3078 0.2809 -0.0083 -0.0052 -0.0002 13  ALA A N   
89    C CA  . ALA A 21  ? 0.2519 0.3372 0.3288 -0.0068 0.0077  -0.0130 13  ALA A CA  
90    C C   . ALA A 21  ? 0.2246 0.3138 0.3077 -0.0013 0.0143  -0.0047 13  ALA A C   
91    O O   . ALA A 21  ? 0.2294 0.3268 0.3115 0.0021  0.0258  -0.0175 13  ALA A O   
92    C CB  . ALA A 21  ? 0.2734 0.3418 0.3813 -0.0074 0.0152  -0.0095 13  ALA A CB  
93    N N   . ASP A 22  ? 0.2210 0.3085 0.3133 -0.0008 0.0081  0.0134  14  ASP A N   
94    C CA  . ASP A 22  ? 0.2502 0.3420 0.3594 0.0031  0.0162  0.0205  14  ASP A CA  
95    C C   . ASP A 22  ? 0.2391 0.3377 0.3297 0.0082  0.0260  0.0210  14  ASP A C   
96    O O   . ASP A 22  ? 0.1938 0.2955 0.2908 0.0150  0.0406  0.0215  14  ASP A O   
97    C CB  . ASP A 22  ? 0.2695 0.3678 0.4006 0.0007  0.0058  0.0326  14  ASP A CB  
98    C CG  . ASP A 22  ? 0.2735 0.3760 0.4248 0.0047  0.0001  0.0407  14  ASP A CG  
99    O OD1 . ASP A 22  ? 0.3068 0.3995 0.4691 0.0093  0.0122  0.0400  14  ASP A OD1 
100   O OD2 . ASP A 22  ? 0.2523 0.3717 0.4109 0.0049  -0.0139 0.0476  14  ASP A OD2 
101   N N   . ALA A 23  ? 0.2200 0.3217 0.2892 0.0082  0.0218  0.0247  15  ALA A N   
102   C CA  . ALA A 23  ? 0.2151 0.3265 0.2676 0.0196  0.0365  0.0335  15  ALA A CA  
103   C C   . ALA A 23  ? 0.2118 0.3441 0.2352 0.0301  0.0413  0.0212  15  ALA A C   
104   O O   . ALA A 23  ? 0.2311 0.3777 0.2424 0.0449  0.0576  0.0283  15  ALA A O   
105   C CB  . ALA A 23  ? 0.2428 0.3528 0.2856 0.0193  0.0349  0.0441  15  ALA A CB  
106   N N   . VAL A 24  ? 0.2506 0.3895 0.2645 0.0236  0.0292  0.0008  16  VAL A N   
107   C CA  . VAL A 24  ? 0.2288 0.3969 0.2227 0.0299  0.0319  -0.0231 16  VAL A CA  
108   C C   . VAL A 24  ? 0.2421 0.4075 0.2507 0.0311  0.0459  -0.0350 16  VAL A C   
109   O O   . VAL A 24  ? 0.2780 0.4702 0.2655 0.0440  0.0567  -0.0433 16  VAL A O   
110   C CB  . VAL A 24  ? 0.2719 0.4455 0.2694 0.0183  0.0193  -0.0482 16  VAL A CB  
111   C CG1 . VAL A 24  ? 0.3150 0.5218 0.3076 0.0190  0.0233  -0.0864 16  VAL A CG1 
112   C CG2 . VAL A 24  ? 0.2573 0.4416 0.2355 0.0208  0.0078  -0.0371 16  VAL A CG2 
113   N N   . GLN A 25  ? 0.2303 0.3667 0.2748 0.0207  0.0476  -0.0334 17  GLN A N   
114   C CA  . GLN A 25  ? 0.3282 0.4580 0.3941 0.0221  0.0639  -0.0415 17  GLN A CA  
115   C C   . GLN A 25  ? 0.2869 0.4222 0.3451 0.0353  0.0776  -0.0233 17  GLN A C   
116   O O   . GLN A 25  ? 0.2800 0.4283 0.3291 0.0437  0.0932  -0.0354 17  GLN A O   
117   C CB  . GLN A 25  ? 0.3798 0.4822 0.4883 0.0141  0.0643  -0.0317 17  GLN A CB  
118   N N   . LYS A 26  ? 0.2798 0.4056 0.3456 0.0370  0.0753  0.0037  18  LYS A N   
119   C CA  . LYS A 26  ? 0.3364 0.4626 0.4078 0.0491  0.0946  0.0229  18  LYS A CA  
120   C C   . LYS A 26  ? 0.2805 0.4342 0.3088 0.0690  0.1079  0.0255  18  LYS A C   
121   O O   . LYS A 26  ? 0.3043 0.4658 0.3271 0.0833  0.1291  0.0304  18  LYS A O   
122   C CB  . LYS A 26  ? 0.2349 0.3481 0.3327 0.0440  0.0924  0.0439  18  LYS A CB  
123   C CG  . LYS A 26  ? 0.3233 0.4317 0.4468 0.0532  0.1175  0.0625  18  LYS A CG  
124   C CD  . LYS A 26  ? 0.2834 0.3817 0.4482 0.0421  0.1155  0.0712  18  LYS A CD  
125   C CE  . LYS A 26  ? 0.3187 0.4106 0.5279 0.0473  0.1437  0.0847  18  LYS A CE  
126   N NZ  . LYS A 26  ? 0.3008 0.3919 0.4941 0.0679  0.1756  0.1072  18  LYS A NZ  
127   N N   . ALA A 27  ? 0.2982 0.4715 0.2948 0.0732  0.0966  0.0243  19  ALA A N   
128   C CA  . ALA A 27  ? 0.3343 0.5478 0.2861 0.0975  0.1066  0.0297  19  ALA A CA  
129   C C   . ALA A 27  ? 0.3371 0.5846 0.2641 0.1021  0.1064  -0.0051 19  ALA A C   
130   O O   . ALA A 27  ? 0.3725 0.6564 0.2641 0.1252  0.1184  -0.0016 19  ALA A O   
131   C CB  . ALA A 27  ? 0.3061 0.5375 0.2360 0.1007  0.0924  0.0364  19  ALA A CB  
132   N N   . ASN A 28  ? 0.3495 0.5842 0.2987 0.0803  0.0946  -0.0389 20  ASN A N   
133   C CA  . ASN A 28  ? 0.4593 0.7262 0.3969 0.0778  0.0947  -0.0842 20  ASN A CA  
134   C C   . ASN A 28  ? 0.4445 0.7713 0.3389 0.0897  0.0810  -0.1015 20  ASN A C   
135   O O   . ASN A 28  ? 0.4458 0.8042 0.3205 0.0968  0.0783  -0.1201 20  ASN A O   
136   C CB  . ASN A 28  ? 0.5228 0.7948 0.4573 0.0888  0.1183  -0.0903 20  ASN A CB  
137   C CG  . ASN A 28  ? 0.6304 0.9209 0.5735 0.0775  0.1225  -0.1447 20  ASN A CG  
138   O OD1 . ASN A 28  ? 0.6135 0.8893 0.5894 0.0557  0.1139  -0.1723 20  ASN A OD1 
139   N ND2 . ASN A 28  ? 0.7139 1.0229 0.6342 0.0891  0.1346  -0.1550 20  ASN A ND2 
140   N N   . SER A 29  ? 0.4393 0.7660 0.3312 0.0864  0.0646  -0.0879 21  SER A N   
141   C CA  . SER A 29  ? 0.4726 0.8407 0.3421 0.0947  0.0449  -0.0901 21  SER A CA  
142   C C   . SER A 29  ? 0.4502 0.8055 0.3296 0.0838  0.0314  -0.0826 21  SER A C   
143   O O   . SER A 29  ? 0.4016 0.7127 0.2957 0.0782  0.0366  -0.0542 21  SER A O   
144   C CB  . SER A 29  ? 0.4808 0.8689 0.3234 0.1242  0.0513  -0.0499 21  SER A CB  
145   O OG  . SER A 29  ? 0.4054 0.8420 0.2383 0.1362  0.0340  -0.0501 21  SER A OG  
146   N N   . GLY A 30  ? 0.5799 0.9667 0.4646 0.0780  0.0127  -0.1058 22  GLY A N   
147   C CA  . GLY A 30  ? 0.6214 0.9946 0.5190 0.0658  0.0007  -0.1035 22  GLY A CA  
148   C C   . GLY A 30  ? 0.6422 0.9979 0.5737 0.0387  -0.0028 -0.1463 22  GLY A C   
149   O O   . GLY A 30  ? 0.6362 0.9834 0.5874 0.0283  0.0078  -0.1767 22  GLY A O   
150   N N   . HIS A 31  ? 0.6528 0.9977 0.5984 0.0279  -0.0137 -0.1463 23  HIS A N   
151   C CA  . HIS A 31  ? 0.6848 1.0060 0.6746 0.0038  -0.0131 -0.1792 23  HIS A CA  
152   C C   . HIS A 31  ? 0.6072 0.8623 0.6160 -0.0050 -0.0106 -0.1438 23  HIS A C   
153   O O   . HIS A 31  ? 0.6258 0.8728 0.6175 0.0003  -0.0191 -0.1136 23  HIS A O   
154   C CB  . HIS A 31  ? 0.7173 1.0730 0.7268 -0.0001 -0.0220 -0.1995 23  HIS A CB  
155   N N   . PRO A 32  ? 0.4659 0.6774 0.5097 -0.0161 0.0022  -0.1453 24  PRO A N   
156   C CA  . PRO A 32  ? 0.4482 0.6106 0.5040 -0.0194 0.0026  -0.1106 24  PRO A CA  
157   C C   . PRO A 32  ? 0.3796 0.5238 0.4645 -0.0301 0.0042  -0.1177 24  PRO A C   
158   O O   . PRO A 32  ? 0.3043 0.4206 0.3870 -0.0294 0.0007  -0.0889 24  PRO A O   
159   C CB  . PRO A 32  ? 0.4060 0.5417 0.4843 -0.0195 0.0172  -0.1035 24  PRO A CB  
160   C CG  . PRO A 32  ? 0.4211 0.5756 0.5216 -0.0251 0.0310  -0.1459 24  PRO A CG  
161   C CD  . PRO A 32  ? 0.4350 0.6446 0.5040 -0.0209 0.0189  -0.1725 24  PRO A CD  
162   N N   . GLY A 33  ? 0.4199 0.5825 0.5350 -0.0399 0.0115  -0.1584 25  GLY A N   
163   C CA  . GLY A 33  ? 0.4117 0.5514 0.5682 -0.0502 0.0216  -0.1656 25  GLY A CA  
164   C C   . GLY A 33  ? 0.3397 0.4814 0.4763 -0.0485 0.0068  -0.1476 25  GLY A C   
165   O O   . GLY A 33  ? 0.3016 0.4080 0.4526 -0.0494 0.0137  -0.1255 25  GLY A O   
166   N N   . ALA A 34  ? 0.3224 0.5080 0.4257 -0.0432 -0.0113 -0.1542 26  ALA A N   
167   C CA  . ALA A 34  ? 0.3466 0.5354 0.4367 -0.0413 -0.0223 -0.1380 26  ALA A CA  
168   C C   . ALA A 34  ? 0.3075 0.4572 0.3708 -0.0346 -0.0249 -0.0920 26  ALA A C   
169   O O   . ALA A 34  ? 0.2609 0.3833 0.3338 -0.0380 -0.0218 -0.0782 26  ALA A O   
170   C CB  . ALA A 34  ? 0.4352 0.6868 0.4992 -0.0323 -0.0381 -0.1513 26  ALA A CB  
171   N N   . PRO A 35  ? 0.2687 0.4158 0.3027 -0.0257 -0.0284 -0.0700 27  PRO A N   
172   C CA  . PRO A 35  ? 0.2632 0.3775 0.2834 -0.0235 -0.0294 -0.0371 27  PRO A CA  
173   C C   . PRO A 35  ? 0.2986 0.3789 0.3398 -0.0276 -0.0219 -0.0288 27  PRO A C   
174   O O   . PRO A 35  ? 0.3712 0.4328 0.4046 -0.0268 -0.0238 -0.0099 27  PRO A O   
175   C CB  . PRO A 35  ? 0.2310 0.3522 0.2328 -0.0156 -0.0292 -0.0243 27  PRO A CB  
176   C CG  . PRO A 35  ? 0.2768 0.4375 0.2694 -0.0086 -0.0293 -0.0419 27  PRO A CG  
177   C CD  . PRO A 35  ? 0.3317 0.5060 0.3490 -0.0175 -0.0284 -0.0762 27  PRO A CD  
178   N N   . MET A 36  ? 0.2979 0.3727 0.3663 -0.0294 -0.0107 -0.0412 28  MET A N   
179   C CA  . MET A 36  ? 0.3524 0.3990 0.4427 -0.0266 0.0009  -0.0247 28  MET A CA  
180   C C   . MET A 36  ? 0.3016 0.3325 0.4121 -0.0288 0.0110  -0.0242 28  MET A C   
181   O O   . MET A 36  ? 0.3132 0.3257 0.4212 -0.0210 0.0156  0.0016  28  MET A O   
182   C CB  . MET A 36  ? 0.3951 0.4370 0.5171 -0.0259 0.0169  -0.0344 28  MET A CB  
183   C CG  . MET A 36  ? 0.3880 0.4399 0.4939 -0.0214 0.0104  -0.0279 28  MET A CG  
184   S SD  . MET A 36  ? 0.4709 0.5158 0.6180 -0.0208 0.0332  -0.0413 28  MET A SD  
185   C CE  . MET A 36  ? 0.4861 0.5029 0.6669 -0.0105 0.0513  -0.0102 28  MET A CE  
186   N N   . GLY A 37  ? 0.2298 0.2734 0.3611 -0.0379 0.0148  -0.0533 29  GLY A N   
187   C CA  . GLY A 37  ? 0.2494 0.2774 0.4096 -0.0411 0.0281  -0.0549 29  GLY A CA  
188   C C   . GLY A 37  ? 0.2318 0.2550 0.3600 -0.0377 0.0164  -0.0336 29  GLY A C   
189   O O   . GLY A 37  ? 0.2392 0.2403 0.3828 -0.0350 0.0299  -0.0206 29  GLY A O   
190   N N   . MET A 38  ? 0.2169 0.2586 0.3042 -0.0364 -0.0039 -0.0286 30  MET A N   
191   C CA  . MET A 38  ? 0.2074 0.2453 0.2688 -0.0346 -0.0117 -0.0127 30  MET A CA  
192   C C   . MET A 38  ? 0.2099 0.2320 0.2412 -0.0283 -0.0163 0.0133  30  MET A C   
193   O O   . MET A 38  ? 0.1983 0.2183 0.2076 -0.0283 -0.0215 0.0224  30  MET A O   
194   C CB  . MET A 38  ? 0.1849 0.2552 0.2290 -0.0350 -0.0246 -0.0219 30  MET A CB  
195   C CG  . MET A 38  ? 0.1849 0.2849 0.2567 -0.0401 -0.0247 -0.0501 30  MET A CG  
196   S SD  . MET A 38  ? 0.2467 0.3985 0.2943 -0.0317 -0.0398 -0.0515 30  MET A SD  
197   C CE  . MET A 38  ? 0.2860 0.4594 0.3111 -0.0241 -0.0441 -0.0541 30  MET A CE  
198   N N   . ALA A 39  ? 0.1687 0.1840 0.2025 -0.0230 -0.0133 0.0229  31  ALA A N   
199   C CA  . ALA A 39  ? 0.2190 0.2358 0.2271 -0.0180 -0.0221 0.0387  31  ALA A CA  
200   C C   . ALA A 39  ? 0.2000 0.2067 0.1925 -0.0126 -0.0195 0.0534  31  ALA A C   
201   O O   . ALA A 39  ? 0.2304 0.2428 0.1992 -0.0143 -0.0281 0.0547  31  ALA A O   
202   C CB  . ALA A 39  ? 0.2317 0.2536 0.2503 -0.0111 -0.0207 0.0457  31  ALA A CB  
203   N N   . GLU A 40  ? 0.2072 0.1992 0.2161 -0.0053 -0.0039 0.0634  32  GLU A N   
204   C CA  . GLU A 40  ? 0.2110 0.1947 0.2014 0.0035  0.0018  0.0799  32  GLU A CA  
205   C C   . GLU A 40  ? 0.2542 0.2306 0.2352 -0.0065 -0.0004 0.0708  32  GLU A C   
206   O O   . GLU A 40  ? 0.2677 0.2434 0.2217 -0.0043 -0.0029 0.0766  32  GLU A O   
207   C CB  . GLU A 40  ? 0.2320 0.1987 0.2484 0.0174  0.0267  0.0987  32  GLU A CB  
208   C CG  . GLU A 40  ? 0.2682 0.2451 0.2865 0.0373  0.0338  0.1226  32  GLU A CG  
209   C CD  . GLU A 40  ? 0.3299 0.3087 0.3796 0.0326  0.0361  0.1125  32  GLU A CD  
210   O OE1 . GLU A 40  ? 0.2551 0.2225 0.3351 0.0173  0.0421  0.0886  32  GLU A OE1 
211   O OE2 . GLU A 40  ? 0.3065 0.3034 0.3513 0.0445  0.0315  0.1263  32  GLU A OE2 
212   N N   . MET A 41  ? 0.1972 0.1731 0.2016 -0.0164 0.0011  0.0549  33  MET A N   
213   C CA  . MET A 41  ? 0.2209 0.1978 0.2187 -0.0231 -0.0019 0.0493  33  MET A CA  
214   C C   . MET A 41  ? 0.2110 0.1964 0.1807 -0.0261 -0.0131 0.0496  33  MET A C   
215   O O   . MET A 41  ? 0.2119 0.1892 0.1664 -0.0271 -0.0102 0.0542  33  MET A O   
216   C CB  . MET A 41  ? 0.1718 0.1647 0.1992 -0.0302 -0.0027 0.0300  33  MET A CB  
217   C CG  . MET A 41  ? 0.1800 0.1635 0.2500 -0.0318 0.0139  0.0218  33  MET A CG  
218   S SD  . MET A 41  ? 0.1937 0.2114 0.3044 -0.0420 0.0100  -0.0155 33  MET A SD  
219   C CE  . MET A 41  ? 0.1731 0.2267 0.2712 -0.0434 -0.0059 -0.0227 33  MET A CE  
220   N N   . ALA A 42  ? 0.1899 0.1897 0.1583 -0.0277 -0.0217 0.0438  34  ALA A N   
221   C CA  . ALA A 42  ? 0.1783 0.1840 0.1332 -0.0308 -0.0257 0.0432  34  ALA A CA  
222   C C   . ALA A 42  ? 0.2017 0.2037 0.1403 -0.0311 -0.0269 0.0443  34  ALA A C   
223   O O   . ALA A 42  ? 0.2074 0.2054 0.1396 -0.0362 -0.0225 0.0403  34  ALA A O   
224   C CB  . ALA A 42  ? 0.1919 0.2124 0.1534 -0.0305 -0.0307 0.0384  34  ALA A CB  
225   N N   . GLU A 43  ? 0.1875 0.1963 0.1219 -0.0244 -0.0314 0.0482  35  GLU A N   
226   C CA  A GLU A 43  ? 0.2248 0.2468 0.1404 -0.0213 -0.0362 0.0463  35  GLU A CA  
227   C CA  B GLU A 43  ? 0.2250 0.2470 0.1405 -0.0213 -0.0362 0.0464  35  GLU A CA  
228   C C   . GLU A 43  ? 0.2708 0.2813 0.1686 -0.0203 -0.0283 0.0483  35  GLU A C   
229   O O   . GLU A 43  ? 0.2631 0.2816 0.1491 -0.0263 -0.0290 0.0346  35  GLU A O   
230   C CB  A GLU A 43  ? 0.2245 0.2629 0.1380 -0.0068 -0.0403 0.0586  35  GLU A CB  
231   C CB  B GLU A 43  ? 0.2258 0.2642 0.1386 -0.0066 -0.0402 0.0588  35  GLU A CB  
232   C CG  A GLU A 43  ? 0.2681 0.3424 0.1643 -0.0013 -0.0523 0.0523  35  GLU A CG  
233   C CG  B GLU A 43  ? 0.2667 0.3353 0.1543 0.0020  -0.0482 0.0569  35  GLU A CG  
234   C CD  A GLU A 43  ? 0.2750 0.3600 0.1417 0.0127  -0.0491 0.0619  35  GLU A CD  
235   C CD  B GLU A 43  ? 0.3039 0.3872 0.1811 0.0263  -0.0441 0.0827  35  GLU A CD  
236   O OE1 A GLU A 43  ? 0.2901 0.3467 0.1514 0.0136  -0.0356 0.0706  35  GLU A OE1 
237   O OE1 B GLU A 43  ? 0.2992 0.3656 0.1983 0.0342  -0.0329 0.1003  35  GLU A OE1 
238   O OE2 A GLU A 43  ? 0.3315 0.4510 0.1860 0.0237  -0.0576 0.0581  35  GLU A OE2 
239   O OE2 B GLU A 43  ? 0.3209 0.4264 0.1776 0.0368  -0.0469 0.0799  35  GLU A OE2 
240   N N   . THR A 44  ? 0.2435 0.2354 0.1449 -0.0137 -0.0178 0.0621  36  THR A N   
241   C CA  . THR A 44  ? 0.3034 0.2822 0.1890 -0.0105 -0.0071 0.0672  36  THR A CA  
242   C C   . THR A 44  ? 0.2698 0.2381 0.1576 -0.0236 -0.0029 0.0552  36  THR A C   
243   O O   . THR A 44  ? 0.2615 0.2305 0.1321 -0.0263 0.0013  0.0465  36  THR A O   
244   C CB  . THR A 44  ? 0.3238 0.2825 0.2263 -0.0024 0.0078  0.0835  36  THR A CB  
245   O OG1 . THR A 44  ? 0.3194 0.2842 0.2254 0.0131  0.0123  0.0994  36  THR A OG1 
246   C CG2 . THR A 44  ? 0.3012 0.2440 0.1895 0.0019  0.0218  0.0908  36  THR A CG2 
247   N N   . LEU A 45  ? 0.2132 0.1759 0.1237 -0.0300 -0.0018 0.0547  37  LEU A N   
248   C CA  . LEU A 45  ? 0.2282 0.1828 0.1459 -0.0369 0.0071  0.0518  37  LEU A CA  
249   C C   . LEU A 45  ? 0.2332 0.1931 0.1494 -0.0450 0.0091  0.0377  37  LEU A C   
250   O O   . LEU A 45  ? 0.2795 0.2289 0.1946 -0.0506 0.0220  0.0302  37  LEU A O   
251   C CB  . LEU A 45  ? 0.2304 0.1930 0.1698 -0.0359 0.0062  0.0572  37  LEU A CB  
252   C CG  . LEU A 45  ? 0.2041 0.1661 0.1545 -0.0366 0.0181  0.0626  37  LEU A CG  
253   C CD1 . LEU A 45  ? 0.2759 0.2190 0.2263 -0.0374 0.0331  0.0675  37  LEU A CD1 
254   C CD2 . LEU A 45  ? 0.1767 0.1632 0.1419 -0.0289 0.0143  0.0704  37  LEU A CD2 
255   N N   . TRP A 46  ? 0.2092 0.1847 0.1320 -0.0470 -0.0003 0.0310  38  TRP A N   
256   C CA  . TRP A 46  ? 0.2474 0.2276 0.1845 -0.0567 0.0065  0.0150  38  TRP A CA  
257   C C   . TRP A 46  ? 0.2511 0.2456 0.1761 -0.0630 0.0025  -0.0085 38  TRP A C   
258   O O   . TRP A 46  ? 0.2576 0.2502 0.1996 -0.0747 0.0160  -0.0293 38  TRP A O   
259   C CB  . TRP A 46  ? 0.2078 0.2009 0.1609 -0.0562 0.0004  0.0157  38  TRP A CB  
260   C CG  . TRP A 46  ? 0.1900 0.1776 0.1581 -0.0504 0.0112  0.0326  38  TRP A CG  
261   C CD1 . TRP A 46  ? 0.1809 0.1703 0.1431 -0.0414 0.0085  0.0475  38  TRP A CD1 
262   C CD2 . TRP A 46  ? 0.1919 0.1787 0.1851 -0.0504 0.0284  0.0363  38  TRP A CD2 
263   N NE1 . TRP A 46  ? 0.1781 0.1760 0.1531 -0.0333 0.0192  0.0610  38  TRP A NE1 
264   C CE2 . TRP A 46  ? 0.2472 0.2403 0.2405 -0.0368 0.0339  0.0586  38  TRP A CE2 
265   C CE3 . TRP A 46  ? 0.2013 0.1865 0.2219 -0.0595 0.0421  0.0223  38  TRP A CE3 
266   C CZ2 . TRP A 46  ? 0.2518 0.2487 0.2647 -0.0272 0.0543  0.0748  38  TRP A CZ2 
267   C CZ3 . TRP A 46  ? 0.2487 0.2292 0.2977 -0.0533 0.0661  0.0368  38  TRP A CZ3 
268   C CH2 . TRP A 46  ? 0.2664 0.2524 0.3080 -0.0350 0.0728  0.0666  38  TRP A CH2 
269   N N   . THR A 47  ? 0.2575 0.2710 0.1568 -0.0539 -0.0130 -0.0069 39  THR A N   
270   C CA  . THR A 47  ? 0.2713 0.3140 0.1535 -0.0555 -0.0194 -0.0305 39  THR A CA  
271   C C   . THR A 47  ? 0.2955 0.3291 0.1524 -0.0525 -0.0091 -0.0324 39  THR A C   
272   O O   . THR A 47  ? 0.3214 0.3780 0.1689 -0.0588 -0.0085 -0.0617 39  THR A O   
273   C CB  . THR A 47  ? 0.3521 0.4323 0.2162 -0.0410 -0.0396 -0.0244 39  THR A CB  
274   O OG1 . THR A 47  ? 0.3008 0.3699 0.1429 -0.0224 -0.0378 0.0062  39  THR A OG1 
275   C CG2 . THR A 47  ? 0.2549 0.3431 0.1451 -0.0435 -0.0482 -0.0221 39  THR A CG2 
276   N N   . LYS A 48  ? 0.2903 0.2939 0.1394 -0.0439 0.0003  -0.0062 40  LYS A N   
277   C CA  . LYS A 48  ? 0.3158 0.3099 0.1403 -0.0383 0.0120  -0.0043 40  LYS A CA  
278   C C   . LYS A 48  ? 0.3699 0.3289 0.2126 -0.0486 0.0336  -0.0049 40  LYS A C   
279   O O   . LYS A 48  ? 0.3393 0.2921 0.1658 -0.0488 0.0465  -0.0138 40  LYS A O   
280   C CB  . LYS A 48  ? 0.3204 0.3078 0.1272 -0.0181 0.0127  0.0273  40  LYS A CB  
281   C CG  . LYS A 48  ? 0.3331 0.3560 0.1199 -0.0005 -0.0015 0.0365  40  LYS A CG  
282   C CD  . LYS A 48  ? 0.4159 0.4821 0.1672 0.0057  -0.0085 0.0160  40  LYS A CD  
283   C CE  . LYS A 48  ? 0.5868 0.6827 0.3256 0.0300  -0.0175 0.0350  40  LYS A CE  
284   N NZ  . LYS A 48  ? 0.5428 0.6445 0.3080 0.0309  -0.0286 0.0446  40  LYS A NZ  
285   N N   . PHE A 49  ? 0.3175 0.2324 0.1305 0.0047  0.0330  0.0337  41  PHE A N   
286   C CA  . PHE A 49  ? 0.3188 0.2423 0.1506 -0.0081 0.0326  0.0214  41  PHE A CA  
287   C C   . PHE A 49  ? 0.2961 0.2446 0.1465 -0.0137 0.0130  0.0158  41  PHE A C   
288   O O   . PHE A 49  ? 0.3163 0.2699 0.1677 -0.0164 0.0066  0.0105  41  PHE A O   
289   C CB  . PHE A 49  ? 0.3474 0.2638 0.1961 -0.0180 0.0527  0.0123  41  PHE A CB  
290   C CG  . PHE A 49  ? 0.3534 0.2386 0.1838 -0.0161 0.0784  0.0148  41  PHE A CG  
291   C CD1 . PHE A 49  ? 0.4022 0.2778 0.2237 -0.0178 0.0865  0.0109  41  PHE A CD1 
292   C CD2 . PHE A 49  ? 0.3923 0.2536 0.2117 -0.0119 0.0968  0.0217  41  PHE A CD2 
293   C CE1 . PHE A 49  ? 0.4269 0.2691 0.2284 -0.0161 0.1136  0.0138  41  PHE A CE1 
294   C CE2 . PHE A 49  ? 0.4282 0.2528 0.2258 -0.0094 0.1251  0.0252  41  PHE A CE2 
295   C CZ  . PHE A 49  ? 0.4043 0.2192 0.1929 -0.0119 0.1339  0.0212  41  PHE A CZ  
296   N N   . LEU A 50  ? 0.2717 0.2326 0.1345 -0.0146 0.0056  0.0173  42  LEU A N   
297   C CA  . LEU A 50  ? 0.2670 0.2459 0.1460 -0.0198 -0.0075 0.0121  42  LEU A CA  
298   C C   . LEU A 50  ? 0.3111 0.2938 0.1812 -0.0192 -0.0204 0.0127  42  LEU A C   
299   O O   . LEU A 50  ? 0.2471 0.2330 0.1070 -0.0153 -0.0270 0.0172  42  LEU A O   
300   C CB  . LEU A 50  ? 0.2508 0.2393 0.1409 -0.0200 -0.0113 0.0149  42  LEU A CB  
301   C CG  . LEU A 50  ? 0.2276 0.2304 0.1330 -0.0241 -0.0191 0.0095  42  LEU A CG  
302   C CD1 . LEU A 50  ? 0.2122 0.2219 0.1311 -0.0269 -0.0119 -0.0009 42  LEU A CD1 
303   C CD2 . LEU A 50  ? 0.2399 0.2511 0.1522 -0.0238 -0.0241 0.0138  42  LEU A CD2 
304   N N   . ASN A 51  ? 0.2665 0.2502 0.1404 -0.0224 -0.0229 0.0066  43  ASN A N   
305   C CA  . ASN A 51  ? 0.2902 0.2726 0.1557 -0.0239 -0.0311 0.0050  43  ASN A CA  
306   C C   . ASN A 51  ? 0.2782 0.2660 0.1527 -0.0271 -0.0370 0.0043  43  ASN A C   
307   O O   . ASN A 51  ? 0.3066 0.2944 0.1874 -0.0253 -0.0353 0.0019  43  ASN A O   
308   C CB  . ASN A 51  ? 0.2458 0.2194 0.1051 -0.0235 -0.0270 -0.0001 43  ASN A CB  
309   C CG  . ASN A 51  ? 0.3068 0.2713 0.1522 -0.0208 -0.0202 0.0009  43  ASN A CG  
310   O OD1 . ASN A 51  ? 0.3186 0.2822 0.1506 -0.0175 -0.0230 0.0053  43  ASN A OD1 
311   N ND2 . ASN A 51  ? 0.3225 0.2819 0.1702 -0.0206 -0.0105 -0.0036 43  ASN A ND2 
312   N N   . HIS A 52  ? 0.2294 0.2233 0.1036 -0.0304 -0.0431 0.0056  44  HIS A N   
313   C CA  . HIS A 52  ? 0.2578 0.2537 0.1394 -0.0346 -0.0452 0.0053  44  HIS A CA  
314   C C   . HIS A 52  ? 0.2578 0.2586 0.1371 -0.0421 -0.0494 0.0007  44  HIS A C   
315   O O   . HIS A 52  ? 0.3268 0.3377 0.2011 -0.0414 -0.0538 -0.0017 44  HIS A O   
316   C CB  . HIS A 52  ? 0.2352 0.2410 0.1285 -0.0326 -0.0453 0.0096  44  HIS A CB  
317   C CG  . HIS A 52  ? 0.2632 0.2803 0.1579 -0.0310 -0.0481 0.0128  44  HIS A CG  
318   N ND1 . HIS A 52  ? 0.2946 0.3239 0.1976 -0.0333 -0.0518 0.0137  44  HIS A ND1 
319   C CD2 . HIS A 52  ? 0.2671 0.2843 0.1535 -0.0248 -0.0467 0.0157  44  HIS A CD2 
320   C CE1 . HIS A 52  ? 0.2850 0.3244 0.1855 -0.0271 -0.0540 0.0169  44  HIS A CE1 
321   N NE2 . HIS A 52  ? 0.2607 0.2908 0.1491 -0.0209 -0.0505 0.0190  44  HIS A NE2 
322   N N   . ASN A 53  ? 0.2689 0.2633 0.1510 -0.0488 -0.0468 -0.0020 45  ASN A N   
323   C CA  . ASN A 53  ? 0.2780 0.2789 0.1623 -0.0601 -0.0476 -0.0109 45  ASN A CA  
324   C C   . ASN A 53  ? 0.2812 0.2888 0.1774 -0.0651 -0.0456 -0.0101 45  ASN A C   
325   O O   . ASN A 53  ? 0.2884 0.2770 0.1818 -0.0664 -0.0373 -0.0074 45  ASN A O   
326   C CB  . ASN A 53  ? 0.3188 0.2981 0.1928 -0.0672 -0.0402 -0.0180 45  ASN A CB  
327   C CG  . ASN A 53  ? 0.3460 0.3341 0.2248 -0.0825 -0.0386 -0.0321 45  ASN A CG  
328   O OD1 . ASN A 53  ? 0.3362 0.3531 0.2268 -0.0861 -0.0458 -0.0376 45  ASN A OD1 
329   N ND2 . ASN A 53  ? 0.3813 0.3458 0.2513 -0.0914 -0.0280 -0.0399 45  ASN A ND2 
330   N N   . PRO A 54  ? 0.2608 0.2942 0.1680 -0.0658 -0.0522 -0.0119 46  PRO A N   
331   C CA  . PRO A 54  ? 0.3133 0.3546 0.2332 -0.0714 -0.0493 -0.0122 46  PRO A CA  
332   C C   . PRO A 54  ? 0.2787 0.3080 0.2003 -0.0866 -0.0390 -0.0220 46  PRO A C   
333   O O   . PRO A 54  ? 0.2803 0.3003 0.2057 -0.0903 -0.0309 -0.0193 46  PRO A O   
334   C CB  . PRO A 54  ? 0.3292 0.4046 0.2595 -0.0680 -0.0589 -0.0154 46  PRO A CB  
335   C CG  . PRO A 54  ? 0.3729 0.4504 0.2913 -0.0554 -0.0651 -0.0104 46  PRO A CG  
336   C CD  . PRO A 54  ? 0.3319 0.3884 0.2380 -0.0592 -0.0615 -0.0135 46  PRO A CD  
337   N N   . ALA A 55  ? 0.2729 0.2998 0.1905 -0.0962 -0.0369 -0.0340 47  ALA A N   
338   C CA  . ALA A 55  ? 0.3076 0.3169 0.2256 -0.1131 -0.0222 -0.0453 47  ALA A CA  
339   C C   . ALA A 55  ? 0.3340 0.2982 0.2338 -0.1088 -0.0078 -0.0352 47  ALA A C   
340   O O   . ALA A 55  ? 0.3321 0.2731 0.2288 -0.1194 0.0089  -0.0392 47  ALA A O   
341   C CB  . ALA A 55  ? 0.3229 0.3412 0.2409 -0.1251 -0.0225 -0.0633 47  ALA A CB  
342   N N   . ASN A 56  ? 0.2867 0.2383 0.1735 -0.0923 -0.0124 -0.0228 48  ASN A N   
343   C CA  . ASN A 56  ? 0.3026 0.2181 0.1706 -0.0822 -0.0010 -0.0131 48  ASN A CA  
344   C C   . ASN A 56  ? 0.3275 0.2517 0.1942 -0.0635 -0.0103 -0.0007 48  ASN A C   
345   O O   . ASN A 56  ? 0.3085 0.2339 0.1700 -0.0536 -0.0159 0.0015  48  ASN A O   
346   C CB  . ASN A 56  ? 0.3592 0.2478 0.2104 -0.0826 0.0070  -0.0172 48  ASN A CB  
347   C CG  . ASN A 56  ? 0.4073 0.2594 0.2356 -0.0667 0.0187  -0.0062 48  ASN A CG  
348   O OD1 . ASN A 56  ? 0.4254 0.2686 0.2482 -0.0582 0.0238  0.0027  48  ASN A OD1 
349   N ND2 . ASN A 56  ? 0.3813 0.2136 0.1944 -0.0603 0.0229  -0.0067 48  ASN A ND2 
350   N N   . PRO A 57  ? 0.3122 0.2437 0.1847 -0.0593 -0.0108 0.0055  49  PRO A N   
351   C CA  . PRO A 57  ? 0.2797 0.2228 0.1531 -0.0436 -0.0184 0.0134  49  PRO A CA  
352   C C   . PRO A 57  ? 0.3000 0.2250 0.1555 -0.0272 -0.0144 0.0182  49  PRO A C   
353   O O   . PRO A 57  ? 0.2979 0.2389 0.1568 -0.0149 -0.0212 0.0202  49  PRO A O   
354   C CB  . PRO A 57  ? 0.3311 0.2813 0.2115 -0.0442 -0.0167 0.0172  49  PRO A CB  
355   C CG  . PRO A 57  ? 0.3346 0.2876 0.2247 -0.0618 -0.0119 0.0101  49  PRO A CG  
356   C CD  . PRO A 57  ? 0.3210 0.2516 0.2002 -0.0700 -0.0029 0.0034  49  PRO A CD  
357   N N   . LYS A 58  ? 0.3149 0.2085 0.1515 -0.0260 -0.0023 0.0188  50  LYS A N   
358   C CA  . LYS A 58  ? 0.3425 0.2187 0.1586 -0.0061 0.0019  0.0238  50  LYS A CA  
359   C C   . LYS A 58  ? 0.3362 0.2053 0.1474 -0.0060 0.0016  0.0191  50  LYS A C   
360   O O   . LYS A 58  ? 0.4041 0.2532 0.1958 0.0096  0.0082  0.0224  50  LYS A O   
361   C CB  . LYS A 58  ? 0.3907 0.2287 0.1812 0.0016  0.0193  0.0309  50  LYS A CB  
362   C CG  . LYS A 58  ? 0.4580 0.2994 0.2478 0.0055  0.0215  0.0370  50  LYS A CG  
363   C CD  . LYS A 58  ? 0.4634 0.3351 0.2574 0.0247  0.0080  0.0397  50  LYS A CD  
364   C CE  . LYS A 58  ? 0.4917 0.3646 0.2808 0.0307  0.0112  0.0456  50  LYS A CE  
365   N NZ  . LYS A 58  ? 0.4758 0.3860 0.2746 0.0453  -0.0033 0.0435  50  LYS A NZ  
366   N N   . PHE A 59  ? 0.3053 0.1900 0.1314 -0.0211 -0.0053 0.0116  51  PHE A N   
367   C CA  . PHE A 59  ? 0.3550 0.2363 0.1771 -0.0211 -0.0065 0.0067  51  PHE A CA  
368   C C   . PHE A 59  ? 0.3483 0.2386 0.1672 -0.0019 -0.0106 0.0092  51  PHE A C   
369   O O   . PHE A 59  ? 0.2792 0.1971 0.1125 0.0027  -0.0194 0.0090  51  PHE A O   
370   C CB  . PHE A 59  ? 0.2873 0.1924 0.1253 -0.0347 -0.0162 0.0001  51  PHE A CB  
371   C CG  . PHE A 59  ? 0.2880 0.1941 0.1222 -0.0330 -0.0187 -0.0042 51  PHE A CG  
372   C CD1 . PHE A 59  ? 0.3539 0.2346 0.1721 -0.0309 -0.0100 -0.0070 51  PHE A CD1 
373   C CD2 . PHE A 59  ? 0.2842 0.2131 0.1285 -0.0330 -0.0273 -0.0051 51  PHE A CD2 
374   C CE1 . PHE A 59  ? 0.3257 0.2077 0.1402 -0.0294 -0.0118 -0.0113 51  PHE A CE1 
375   C CE2 . PHE A 59  ? 0.2946 0.2221 0.1334 -0.0314 -0.0275 -0.0087 51  PHE A CE2 
376   C CZ  . PHE A 59  ? 0.3150 0.2209 0.1399 -0.0299 -0.0206 -0.0122 51  PHE A CZ  
377   N N   . TYR A 60  ? 0.3377 0.2054 0.1384 0.0093  -0.0029 0.0099  52  TYR A N   
378   C CA  . TYR A 60  ? 0.3308 0.2100 0.1274 0.0317  -0.0059 0.0112  52  TYR A CA  
379   C C   . TYR A 60  ? 0.3000 0.2139 0.1178 0.0295  -0.0163 0.0041  52  TYR A C   
380   O O   . TYR A 60  ? 0.3144 0.2552 0.1422 0.0412  -0.0218 0.0015  52  TYR A O   
381   C CB  . TYR A 60  ? 0.3663 0.2155 0.1392 0.0452  0.0047  0.0128  52  TYR A CB  
382   C CG  . TYR A 60  ? 0.4085 0.2136 0.1542 0.0504  0.0210  0.0204  52  TYR A CG  
383   C CD1 . TYR A 60  ? 0.4156 0.2146 0.1554 0.0544  0.0246  0.0275  52  TYR A CD1 
384   C CD2 . TYR A 60  ? 0.4962 0.2620 0.2206 0.0511  0.0357  0.0200  52  TYR A CD2 
385   C CE1 . TYR A 60  ? 0.4613 0.2132 0.1729 0.0588  0.0442  0.0348  52  TYR A CE1 
386   C CE2 . TYR A 60  ? 0.5507 0.2691 0.2481 0.0545  0.0557  0.0264  52  TYR A CE2 
387   C CZ  . TYR A 60  ? 0.5248 0.2350 0.2152 0.0585  0.0608  0.0342  52  TYR A CZ  
388   O OH  . TYR A 60  ? 0.5523 0.2091 0.2128 0.0616  0.0851  0.0408  52  TYR A OH  
389   N N   . ASN A 61  ? 0.2997 0.2138 0.1235 0.0148  -0.0175 -0.0005 53  ASN A N   
390   C CA  . ASN A 61  ? 0.3079 0.2460 0.1465 0.0134  -0.0222 -0.0065 53  ASN A CA  
391   C C   . ASN A 61  ? 0.2626 0.2188 0.1174 0.0014  -0.0272 -0.0067 53  ASN A C   
392   O O   . ASN A 61  ? 0.3141 0.2807 0.1767 -0.0028 -0.0270 -0.0106 53  ASN A O   
393   C CB  . ASN A 61  ? 0.3130 0.2385 0.1435 0.0091  -0.0185 -0.0106 53  ASN A CB  
394   C CG  . ASN A 61  ? 0.3151 0.2599 0.1558 0.0146  -0.0184 -0.0172 53  ASN A CG  
395   O OD1 . ASN A 61  ? 0.2962 0.2592 0.1445 0.0276  -0.0190 -0.0208 53  ASN A OD1 
396   N ND2 . ASN A 61  ? 0.2789 0.2224 0.1200 0.0050  -0.0168 -0.0201 53  ASN A ND2 
397   N N   . ARG A 62  ? 0.2493 0.2068 0.1075 -0.0030 -0.0295 -0.0022 54  ARG A N   
398   C CA  . ARG A 62  ? 0.2233 0.1969 0.0952 -0.0110 -0.0331 -0.0017 54  ARG A CA  
399   C C   . ARG A 62  ? 0.2092 0.2039 0.0954 -0.0061 -0.0325 -0.0067 54  ARG A C   
400   O O   . ARG A 62  ? 0.2442 0.2499 0.1334 0.0046  -0.0326 -0.0109 54  ARG A O   
401   C CB  . ARG A 62  ? 0.2197 0.1934 0.0942 -0.0146 -0.0350 0.0032  54  ARG A CB  
402   C CG  . ARG A 62  ? 0.2204 0.2009 0.0965 -0.0035 -0.0349 0.0046  54  ARG A CG  
403   C CD  . ARG A 62  ? 0.2206 0.1953 0.0952 -0.0070 -0.0342 0.0100  54  ARG A CD  
404   N NE  . ARG A 62  ? 0.2222 0.2037 0.0947 0.0055  -0.0342 0.0119  54  ARG A NE  
405   C CZ  . ARG A 62  ? 0.2462 0.2142 0.1011 0.0201  -0.0301 0.0149  54  ARG A CZ  
406   N NH1 . ARG A 62  ? 0.3061 0.2499 0.1453 0.0223  -0.0241 0.0163  54  ARG A NH1 
407   N NH2 . ARG A 62  ? 0.2658 0.2438 0.1164 0.0344  -0.0313 0.0163  54  ARG A NH2 
408   N N   . ASP A 63  ? 0.2467 0.2474 0.1407 -0.0131 -0.0304 -0.0078 55  ASP A N   
409   C CA  . ASP A 63  ? 0.2434 0.2620 0.1534 -0.0131 -0.0264 -0.0143 55  ASP A CA  
410   C C   . ASP A 63  ? 0.2152 0.2451 0.1325 -0.0105 -0.0304 -0.0132 55  ASP A C   
411   O O   . ASP A 63  ? 0.2141 0.2357 0.1257 -0.0123 -0.0343 -0.0053 55  ASP A O   
412   C CB  . ASP A 63  ? 0.2171 0.2304 0.1288 -0.0205 -0.0194 -0.0130 55  ASP A CB  
413   C CG  . ASP A 63  ? 0.2772 0.2802 0.1808 -0.0218 -0.0125 -0.0154 55  ASP A CG  
414   O OD1 . ASP A 63  ? 0.2313 0.2385 0.1361 -0.0182 -0.0117 -0.0220 55  ASP A OD1 
415   O OD2 . ASP A 63  ? 0.2639 0.2546 0.1583 -0.0243 -0.0074 -0.0101 55  ASP A OD2 
416   N N   . ARG A 64  ? 0.1808 0.2326 0.1116 -0.0064 -0.0291 -0.0231 56  ARG A N   
417   C CA  . ARG A 64  ? 0.1875 0.2535 0.1252 -0.0031 -0.0324 -0.0243 56  ARG A CA  
418   C C   . ARG A 64  ? 0.2093 0.2830 0.1620 -0.0132 -0.0256 -0.0295 56  ARG A C   
419   O O   . ARG A 64  ? 0.2348 0.3181 0.1998 -0.0185 -0.0170 -0.0412 56  ARG A O   
420   C CB  . ARG A 64  ? 0.2052 0.2959 0.1468 0.0106  -0.0361 -0.0346 56  ARG A CB  
421   C CG  . ARG A 64  ? 0.2694 0.3496 0.1908 0.0262  -0.0417 -0.0258 56  ARG A CG  
422   C CD  . ARG A 64  ? 0.2519 0.3035 0.1560 0.0267  -0.0398 -0.0174 56  ARG A CD  
423   N NE  . ARG A 64  ? 0.2725 0.3096 0.1550 0.0432  -0.0402 -0.0105 56  ARG A NE  
424   C CZ  . ARG A 64  ? 0.2907 0.3013 0.1556 0.0465  -0.0362 -0.0049 56  ARG A CZ  
425   N NH1 . ARG A 64  ? 0.3040 0.3045 0.1717 0.0344  -0.0340 -0.0064 56  ARG A NH1 
426   N NH2 . ARG A 64  ? 0.2778 0.2696 0.1198 0.0631  -0.0328 0.0021  56  ARG A NH2 
427   N N   . PHE A 65  ? 0.1989 0.2669 0.1507 -0.0161 -0.0272 -0.0219 57  PHE A N   
428   C CA  . PHE A 65  ? 0.1484 0.2208 0.1122 -0.0235 -0.0194 -0.0261 57  PHE A CA  
429   C C   . PHE A 65  ? 0.1451 0.2378 0.1179 -0.0200 -0.0228 -0.0328 57  PHE A C   
430   O O   . PHE A 65  ? 0.1595 0.2516 0.1233 -0.0128 -0.0310 -0.0253 57  PHE A O   
431   C CB  . PHE A 65  ? 0.1518 0.2042 0.1072 -0.0272 -0.0177 -0.0129 57  PHE A CB  
432   C CG  . PHE A 65  ? 0.1965 0.2474 0.1600 -0.0320 -0.0079 -0.0148 57  PHE A CG  
433   C CD1 . PHE A 65  ? 0.1929 0.2360 0.1609 -0.0379 0.0076  -0.0220 57  PHE A CD1 
434   C CD2 . PHE A 65  ? 0.1996 0.2533 0.1650 -0.0308 -0.0114 -0.0096 57  PHE A CD2 
435   C CE1 . PHE A 65  ? 0.1957 0.2306 0.1683 -0.0422 0.0206  -0.0236 57  PHE A CE1 
436   C CE2 . PHE A 65  ? 0.1658 0.2150 0.1369 -0.0342 -0.0008 -0.0111 57  PHE A CE2 
437   C CZ  . PHE A 65  ? 0.1637 0.2019 0.1377 -0.0398 0.0158  -0.0180 57  PHE A CZ  
438   N N   . VAL A 66  ? 0.1386 0.2483 0.1282 -0.0258 -0.0146 -0.0480 58  VAL A N   
439   C CA  . VAL A 66  ? 0.1332 0.2659 0.1325 -0.0235 -0.0170 -0.0577 58  VAL A CA  
440   C C   . VAL A 66  ? 0.1718 0.2983 0.1820 -0.0355 -0.0040 -0.0626 58  VAL A C   
441   O O   . VAL A 66  ? 0.1406 0.2656 0.1619 -0.0459 0.0105  -0.0745 58  VAL A O   
442   C CB  . VAL A 66  ? 0.1317 0.3016 0.1433 -0.0174 -0.0202 -0.0784 58  VAL A CB  
443   C CG1 . VAL A 66  ? 0.1703 0.3680 0.1919 -0.0152 -0.0224 -0.0914 58  VAL A CG1 
444   C CG2 . VAL A 66  ? 0.1667 0.3392 0.1628 -0.0010 -0.0319 -0.0715 58  VAL A CG2 
445   N N   . LEU A 67  ? 0.1383 0.2591 0.1444 -0.0341 -0.0066 -0.0539 59  LEU A N   
446   C CA  . LEU A 67  ? 0.1353 0.2519 0.1507 -0.0427 0.0056  -0.0594 59  LEU A CA  
447   C C   . LEU A 67  ? 0.1308 0.2810 0.1607 -0.0429 0.0041  -0.0797 59  LEU A C   
448   O O   . LEU A 67  ? 0.1787 0.3391 0.2037 -0.0352 -0.0053 -0.0760 59  LEU A O   
449   C CB  . LEU A 67  ? 0.1991 0.2961 0.2035 -0.0395 0.0029  -0.0407 59  LEU A CB  
450   C CG  . LEU A 67  ? 0.2304 0.3197 0.2411 -0.0452 0.0157  -0.0436 59  LEU A CG  
451   C CD1 . LEU A 67  ? 0.2283 0.2921 0.2373 -0.0518 0.0344  -0.0435 59  LEU A CD1 
452   C CD2 . LEU A 67  ? 0.2437 0.3252 0.2462 -0.0392 0.0090  -0.0276 59  LEU A CD2 
453   N N   . SER A 68  ? 0.1623 0.3323 0.2101 -0.0518 0.0141  -0.1031 60  SER A N   
454   C CA  . SER A 68  ? 0.1425 0.3542 0.2064 -0.0510 0.0113  -0.1274 60  SER A CA  
455   C C   . SER A 68  ? 0.2709 0.4819 0.3400 -0.0573 0.0183  -0.1325 60  SER A C   
456   O O   . SER A 68  ? 0.2918 0.5245 0.3607 -0.0465 0.0115  -0.1368 60  SER A O   
457   C CB  . SER A 68  ? 0.1390 0.3675 0.2215 -0.0581 0.0253  -0.1496 60  SER A CB  
458   O OG  . SER A 68  ? 0.2569 0.5221 0.3508 -0.0493 0.0244  -0.1669 60  SER A OG  
459   N N   . ASN A 69  ? 0.2371 0.4141 0.3059 -0.0691 0.0357  -0.1261 61  ASN A N   
460   C CA  . ASN A 69  ? 0.2743 0.4450 0.3461 -0.0742 0.0444  -0.1291 61  ASN A CA  
461   C C   . ASN A 69  ? 0.3432 0.4963 0.3960 -0.0617 0.0318  -0.1021 61  ASN A C   
462   O O   . ASN A 69  ? 0.3707 0.4914 0.4143 -0.0621 0.0396  -0.0853 61  ASN A O   
463   C CB  . ASN A 69  ? 0.3188 0.4576 0.3961 -0.0898 0.0723  -0.1346 61  ASN A CB  
464   C CG  . ASN A 69  ? 0.4096 0.5118 0.4735 -0.0893 0.0808  -0.1173 61  ASN A CG  
465   O OD1 . ASN A 69  ? 0.4238 0.5267 0.4770 -0.0792 0.0651  -0.1026 61  ASN A OD1 
466   N ND2 . ASN A 69  ? 0.4448 0.5125 0.5071 -0.0994 0.1079  -0.1192 61  ASN A ND2 
467   N N   . GLY A 70  ? 0.3376 0.5138 0.3837 -0.0490 0.0130  -0.0992 62  GLY A N   
468   C CA  . GLY A 70  ? 0.3424 0.5034 0.3706 -0.0380 0.0016  -0.0752 62  GLY A CA  
469   C C   . GLY A 70  ? 0.3279 0.4734 0.3542 -0.0400 0.0078  -0.0667 62  GLY A C   
470   O O   . GLY A 70  ? 0.2991 0.4302 0.3140 -0.0339 0.0016  -0.0474 62  GLY A O   
471   N N   . HIS A 71  ? 0.2516 0.4011 0.2901 -0.0492 0.0211  -0.0824 63  HIS A N   
472   C CA  . HIS A 71  ? 0.3169 0.4481 0.3534 -0.0506 0.0297  -0.0742 63  HIS A CA  
473   C C   . HIS A 71  ? 0.3559 0.4530 0.3838 -0.0491 0.0366  -0.0538 63  HIS A C   
474   O O   . HIS A 71  ? 0.3598 0.4458 0.3814 -0.0434 0.0356  -0.0394 63  HIS A O   
475   C CB  . HIS A 71  ? 0.3667 0.5038 0.4174 -0.0623 0.0467  -0.0971 63  HIS A CB  
476   C CG  . HIS A 71  ? 0.4475 0.5789 0.5098 -0.0754 0.0634  -0.1136 63  HIS A CG  
477   N ND1 . HIS A 71  ? 0.5082 0.6009 0.5671 -0.0818 0.0851  -0.1074 63  HIS A ND1 
478   C CD2 . HIS A 71  ? 0.4712 0.6302 0.5474 -0.0824 0.0634  -0.1366 63  HIS A CD2 
479   C CE1 . HIS A 71  ? 0.5265 0.6191 0.5963 -0.0944 0.0998  -0.1256 63  HIS A CE1 
480   N NE2 . HIS A 71  ? 0.5178 0.6533 0.6008 -0.0960 0.0865  -0.1448 63  HIS A NE2 
481   N N   . ALA A 72  ? 0.2981 0.3811 0.3248 -0.0526 0.0434  -0.0531 64  ALA A N   
482   C CA  . ALA A 72  ? 0.2380 0.2916 0.2522 -0.0474 0.0485  -0.0343 64  ALA A CA  
483   C C   . ALA A 72  ? 0.1788 0.2370 0.1834 -0.0379 0.0296  -0.0171 64  ALA A C   
484   O O   . ALA A 72  ? 0.1854 0.2305 0.1808 -0.0340 0.0284  -0.0066 64  ALA A O   
485   C CB  . ALA A 72  ? 0.2792 0.3161 0.2929 -0.0538 0.0634  -0.0407 64  ALA A CB  
486   N N   . SER A 73  ? 0.1649 0.2406 0.1704 -0.0346 0.0165  -0.0151 65  SER A N   
487   C CA  . SER A 73  ? 0.1327 0.2127 0.1305 -0.0294 0.0017  -0.0039 65  SER A CA  
488   C C   . SER A 73  ? 0.1364 0.2047 0.1280 -0.0248 0.0002  0.0109  65  SER A C   
489   O O   . SER A 73  ? 0.1739 0.2426 0.1599 -0.0234 -0.0085 0.0169  65  SER A O   
490   C CB  . SER A 73  ? 0.2738 0.3671 0.2703 -0.0263 -0.0062 -0.0035 65  SER A CB  
491   O OG  . SER A 73  ? 0.2669 0.3584 0.2668 -0.0257 -0.0011 -0.0001 65  SER A OG  
492   N N   . MET A 74  ? 0.1949 0.2552 0.1870 -0.0213 0.0083  0.0159  66  MET A N   
493   C CA  . MET A 74  ? 0.2004 0.2578 0.1866 -0.0131 0.0048  0.0283  66  MET A CA  
494   C C   . MET A 74  ? 0.2308 0.2764 0.2066 -0.0098 0.0060  0.0320  66  MET A C   
495   O O   . MET A 74  ? 0.1879 0.2390 0.1581 -0.0034 -0.0022 0.0394  66  MET A O   
496   C CB  . MET A 74  ? 0.1891 0.2400 0.1750 -0.0054 0.0142  0.0334  66  MET A CB  
497   C CG  . MET A 74  ? 0.1975 0.2655 0.1919 -0.0043 0.0082  0.0355  66  MET A CG  
498   S SD  . MET A 74  ? 0.1998 0.2891 0.1978 -0.0058 -0.0080 0.0391  66  MET A SD  
499   C CE  . MET A 74  ? 0.1543 0.2450 0.1442 0.0057  -0.0115 0.0461  66  MET A CE  
500   N N   . LEU A 75  ? 0.1943 0.2262 0.1682 -0.0145 0.0167  0.0251  67  LEU A N   
501   C CA  . LEU A 75  ? 0.2279 0.2469 0.1906 -0.0120 0.0193  0.0282  67  LEU A CA  
502   C C   . LEU A 75  ? 0.2490 0.2819 0.2112 -0.0141 0.0030  0.0288  67  LEU A C   
503   O O   . LEU A 75  ? 0.1944 0.2256 0.1464 -0.0080 -0.0023 0.0357  67  LEU A O   
504   C CB  . LEU A 75  ? 0.2232 0.2276 0.1880 -0.0204 0.0357  0.0170  67  LEU A CB  
505   C CG  . LEU A 75  ? 0.3020 0.2870 0.2535 -0.0184 0.0443  0.0198  67  LEU A CG  
506   C CD1 . LEU A 75  ? 0.3686 0.3279 0.3004 -0.0046 0.0566  0.0333  67  LEU A CD1 
507   C CD2 . LEU A 75  ? 0.3736 0.3522 0.3344 -0.0313 0.0602  0.0035  67  LEU A CD2 
508   N N   . LEU A 76  ? 0.1857 0.2318 0.1567 -0.0211 -0.0040 0.0211  68  LEU A N   
509   C CA  . LEU A 76  ? 0.1834 0.2367 0.1514 -0.0226 -0.0160 0.0216  68  LEU A CA  
510   C C   . LEU A 76  ? 0.1539 0.2155 0.1213 -0.0208 -0.0250 0.0285  68  LEU A C   
511   O O   . LEU A 76  ? 0.1853 0.2482 0.1473 -0.0208 -0.0314 0.0307  68  LEU A O   
512   C CB  . LEU A 76  ? 0.1477 0.2105 0.1208 -0.0260 -0.0189 0.0127  68  LEU A CB  
513   C CG  . LEU A 76  ? 0.1607 0.2248 0.1269 -0.0253 -0.0278 0.0139  68  LEU A CG  
514   C CD1 . LEU A 76  ? 0.1990 0.2543 0.1586 -0.0257 -0.0280 0.0150  68  LEU A CD1 
515   C CD2 . LEU A 76  ? 0.1415 0.2152 0.1085 -0.0227 -0.0295 0.0056  68  LEU A CD2 
516   N N   . TYR A 77  ? 0.1562 0.2253 0.1303 -0.0204 -0.0246 0.0298  69  TYR A N   
517   C CA  . TYR A 77  ? 0.1608 0.2413 0.1381 -0.0206 -0.0308 0.0334  69  TYR A CA  
518   C C   . TYR A 77  ? 0.1722 0.2583 0.1460 -0.0139 -0.0338 0.0374  69  TYR A C   
519   O O   . TYR A 77  ? 0.1444 0.2427 0.1196 -0.0163 -0.0411 0.0357  69  TYR A O   
520   C CB  . TYR A 77  ? 0.1295 0.2171 0.1150 -0.0205 -0.0277 0.0340  69  TYR A CB  
521   C CG  . TYR A 77  ? 0.1606 0.2461 0.1460 -0.0244 -0.0262 0.0302  69  TYR A CG  
522   C CD1 . TYR A 77  ? 0.2355 0.3158 0.2134 -0.0268 -0.0293 0.0283  69  TYR A CD1 
523   C CD2 . TYR A 77  ? 0.1525 0.2408 0.1423 -0.0231 -0.0211 0.0286  69  TYR A CD2 
524   C CE1 . TYR A 77  ? 0.2506 0.3295 0.2230 -0.0249 -0.0280 0.0259  69  TYR A CE1 
525   C CE2 . TYR A 77  ? 0.1363 0.2255 0.1225 -0.0234 -0.0205 0.0247  69  TYR A CE2 
526   C CZ  . TYR A 77  ? 0.2138 0.2987 0.1901 -0.0228 -0.0243 0.0239  69  TYR A CZ  
527   O OH  . TYR A 77  ? 0.2289 0.3152 0.1966 -0.0179 -0.0238 0.0212  69  TYR A OH  
528   N N   . SER A 78  ? 0.1522 0.2297 0.1200 -0.0045 -0.0270 0.0418  70  SER A N   
529   C CA  . SER A 78  ? 0.2156 0.2975 0.1737 0.0078  -0.0294 0.0471  70  SER A CA  
530   C C   . SER A 78  ? 0.2086 0.2888 0.1574 0.0063  -0.0352 0.0454  70  SER A C   
531   O O   . SER A 78  ? 0.1997 0.2975 0.1460 0.0109  -0.0443 0.0444  70  SER A O   
532   C CB  . SER A 78  ? 0.2238 0.2856 0.1703 0.0200  -0.0160 0.0539  70  SER A CB  
533   O OG  . SER A 78  ? 0.2471 0.3105 0.2015 0.0225  -0.0101 0.0551  70  SER A OG  
534   N N   . LEU A 79  ? 0.1814 0.2436 0.1258 -0.0000 -0.0300 0.0430  71  LEU A N   
535   C CA  . LEU A 79  ? 0.1994 0.2574 0.1341 -0.0014 -0.0339 0.0414  71  LEU A CA  
536   C C   . LEU A 79  ? 0.1977 0.2708 0.1388 -0.0103 -0.0449 0.0356  71  LEU A C   
537   O O   . LEU A 79  ? 0.2282 0.3093 0.1629 -0.0087 -0.0514 0.0335  71  LEU A O   
538   C CB  . LEU A 79  ? 0.1919 0.2315 0.1245 -0.0071 -0.0250 0.0379  71  LEU A CB  
539   C CG  . LEU A 79  ? 0.2204 0.2392 0.1440 -0.0011 -0.0092 0.0410  71  LEU A CG  
540   C CD1 . LEU A 79  ? 0.2259 0.2362 0.1578 -0.0112 0.0007  0.0317  71  LEU A CD1 
541   C CD2 . LEU A 79  ? 0.3034 0.3110 0.2066 0.0092  -0.0070 0.0472  71  LEU A CD2 
542   N N   . LEU A 80  ? 0.2043 0.2796 0.1559 -0.0193 -0.0453 0.0322  72  LEU A N   
543   C CA  . LEU A 80  ? 0.2061 0.2877 0.1612 -0.0285 -0.0503 0.0269  72  LEU A CA  
544   C C   . LEU A 80  ? 0.1619 0.2669 0.1243 -0.0289 -0.0560 0.0233  72  LEU A C   
545   O O   . LEU A 80  ? 0.2129 0.3267 0.1749 -0.0345 -0.0604 0.0162  72  LEU A O   
546   C CB  . LEU A 80  ? 0.1569 0.2317 0.1165 -0.0343 -0.0464 0.0261  72  LEU A CB  
547   C CG  . LEU A 80  ? 0.1930 0.2540 0.1469 -0.0322 -0.0429 0.0261  72  LEU A CG  
548   C CD1 . LEU A 80  ? 0.1796 0.2381 0.1344 -0.0327 -0.0399 0.0260  72  LEU A CD1 
549   C CD2 . LEU A 80  ? 0.1943 0.2454 0.1387 -0.0336 -0.0443 0.0236  72  LEU A CD2 
550   N N   . HIS A 81  ? 0.1567 0.2749 0.1270 -0.0229 -0.0555 0.0260  73  HIS A N   
551   C CA  . HIS A 81  ? 0.1917 0.3401 0.1718 -0.0212 -0.0617 0.0204  73  HIS A CA  
552   C C   . HIS A 81  ? 0.2253 0.3822 0.1964 -0.0100 -0.0671 0.0181  73  HIS A C   
553   O O   . HIS A 81  ? 0.1823 0.3568 0.1601 -0.0144 -0.0716 0.0069  73  HIS A O   
554   C CB  . HIS A 81  ? 0.1980 0.3571 0.1864 -0.0128 -0.0592 0.0249  73  HIS A CB  
555   C CG  . HIS A 81  ? 0.1860 0.3794 0.1854 -0.0067 -0.0652 0.0181  73  HIS A CG  
556   N ND1 . HIS A 81  ? 0.1772 0.3914 0.1935 -0.0203 -0.0664 0.0048  73  HIS A ND1 
557   C CD2 . HIS A 81  ? 0.1930 0.3986 0.1881 0.0124  -0.0672 0.0209  73  HIS A CD2 
558   C CE1 . HIS A 81  ? 0.2107 0.4524 0.2355 -0.0105 -0.0701 -0.0017 73  HIS A CE1 
559   N NE2 . HIS A 81  ? 0.2153 0.4524 0.2264 0.0106  -0.0714 0.0086  73  HIS A NE2 
560   N N   . LEU A 82  ? 0.2436 0.3859 0.1984 0.0045  -0.0646 0.0277  74  LEU A N   
561   C CA  . LEU A 82  ? 0.2648 0.4105 0.2068 0.0187  -0.0678 0.0275  74  LEU A CA  
562   C C   . LEU A 82  ? 0.2608 0.4017 0.1972 0.0108  -0.0714 0.0201  74  LEU A C   
563   O O   . LEU A 82  ? 0.2142 0.3703 0.1482 0.0163  -0.0770 0.0135  74  LEU A O   
564   C CB  . LEU A 82  ? 0.2085 0.3319 0.1299 0.0355  -0.0595 0.0410  74  LEU A CB  
565   C CG  . LEU A 82  ? 0.3553 0.4812 0.2763 0.0497  -0.0541 0.0491  74  LEU A CG  
566   C CD1 . LEU A 82  ? 0.3913 0.4827 0.2912 0.0600  -0.0393 0.0623  74  LEU A CD1 
567   C CD2 . LEU A 82  ? 0.3438 0.4926 0.2641 0.0659  -0.0594 0.0459  74  LEU A CD2 
568   N N   . THR A 83  ? 0.2394 0.3611 0.1734 -0.0012 -0.0680 0.0207  75  THR A N   
569   C CA  . THR A 83  ? 0.2526 0.3672 0.1791 -0.0070 -0.0701 0.0146  75  THR A CA  
570   C C   . THR A 83  ? 0.2653 0.3939 0.2053 -0.0226 -0.0733 0.0014  75  THR A C   
571   O O   . THR A 83  ? 0.2619 0.3874 0.1963 -0.0278 -0.0748 -0.0056 75  THR A O   
572   C CB  . THR A 83  ? 0.2351 0.3237 0.1518 -0.0115 -0.0639 0.0203  75  THR A CB  
573   O OG1 . THR A 83  ? 0.2223 0.3049 0.1492 -0.0224 -0.0608 0.0209  75  THR A OG1 
574   C CG2 . THR A 83  ? 0.2001 0.2748 0.1012 0.0015  -0.0576 0.0313  75  THR A CG2 
575   N N   . GLY A 84  ? 0.2664 0.4090 0.2228 -0.0311 -0.0725 -0.0027 76  GLY A N   
576   C CA  . GLY A 84  ? 0.2924 0.4504 0.2619 -0.0469 -0.0723 -0.0173 76  GLY A CA  
577   C C   . GLY A 84  ? 0.2918 0.4345 0.2641 -0.0657 -0.0651 -0.0190 76  GLY A C   
578   O O   . GLY A 84  ? 0.2681 0.4145 0.2474 -0.0821 -0.0606 -0.0324 76  GLY A O   
579   N N   . TYR A 85  ? 0.2175 0.3364 0.1842 -0.0617 -0.0600 -0.0065 77  TYR A N   
580   C CA  . TYR A 85  ? 0.2497 0.3453 0.2162 -0.0713 -0.0494 -0.0055 77  TYR A CA  
581   C C   . TYR A 85  ? 0.2728 0.3839 0.2555 -0.0803 -0.0445 -0.0115 77  TYR A C   
582   O O   . TYR A 85  ? 0.2692 0.4120 0.2655 -0.0773 -0.0509 -0.0157 77  TYR A O   
583   C CB  . TYR A 85  ? 0.2250 0.2992 0.1821 -0.0613 -0.0468 0.0069  77  TYR A CB  
584   C CG  . TYR A 85  ? 0.2193 0.2770 0.1627 -0.0558 -0.0480 0.0097  77  TYR A CG  
585   C CD1 . TYR A 85  ? 0.1914 0.2559 0.1310 -0.0475 -0.0537 0.0121  77  TYR A CD1 
586   C CD2 . TYR A 85  ? 0.2424 0.2761 0.1746 -0.0576 -0.0418 0.0101  77  TYR A CD2 
587   C CE1 . TYR A 85  ? 0.2173 0.2673 0.1458 -0.0438 -0.0530 0.0133  77  TYR A CE1 
588   C CE2 . TYR A 85  ? 0.2571 0.2794 0.1787 -0.0518 -0.0428 0.0114  77  TYR A CE2 
589   C CZ  . TYR A 85  ? 0.2962 0.3278 0.2177 -0.0465 -0.0484 0.0122  77  TYR A CZ  
590   O OH  . TYR A 85  ? 0.3574 0.3782 0.2697 -0.0421 -0.0477 0.0122  77  TYR A OH  
591   N N   . ASN A 86  ? 0.2738 0.3614 0.2533 -0.0897 -0.0317 -0.0116 78  ASN A N   
592   C CA  . ASN A 86  ? 0.2935 0.3894 0.2869 -0.1010 -0.0223 -0.0181 78  ASN A CA  
593   C C   . ASN A 86  ? 0.3048 0.4041 0.3012 -0.0907 -0.0233 -0.0073 78  ASN A C   
594   O O   . ASN A 86  ? 0.2401 0.3175 0.2289 -0.0909 -0.0130 -0.0010 78  ASN A O   
595   C CB  . ASN A 86  ? 0.3250 0.3862 0.3079 -0.1138 -0.0039 -0.0213 78  ASN A CB  
596   C CG  . ASN A 86  ? 0.4966 0.5645 0.4946 -0.1296 0.0101  -0.0313 78  ASN A CG  
597   O OD1 . ASN A 86  ? 0.5288 0.6369 0.5505 -0.1352 0.0041  -0.0425 78  ASN A OD1 
598   N ND2 . ASN A 86  ? 0.4970 0.5257 0.4801 -0.1354 0.0301  -0.0275 78  ASN A ND2 
599   N N   . LEU A 87  ? 0.2264 0.3521 0.2312 -0.0799 -0.0350 -0.0049 79  LEU A N   
600   C CA  . LEU A 87  ? 0.1840 0.3149 0.1926 -0.0699 -0.0359 0.0038  79  LEU A CA  
601   C C   . LEU A 87  ? 0.2498 0.4182 0.2739 -0.0640 -0.0442 -0.0011 79  LEU A C   
602   O O   . LEU A 87  ? 0.2356 0.4154 0.2552 -0.0541 -0.0534 -0.0005 79  LEU A O   
603   C CB  . LEU A 87  ? 0.2106 0.3229 0.2049 -0.0572 -0.0388 0.0149  79  LEU A CB  
604   C CG  . LEU A 87  ? 0.2190 0.3276 0.2139 -0.0497 -0.0359 0.0221  79  LEU A CG  
605   C CD1 . LEU A 87  ? 0.2103 0.3045 0.2016 -0.0555 -0.0263 0.0228  79  LEU A CD1 
606   C CD2 . LEU A 87  ? 0.1701 0.2656 0.1545 -0.0404 -0.0377 0.0274  79  LEU A CD2 
607   N N   . SER A 88  ? 0.2149 0.4026 0.2552 -0.0681 -0.0403 -0.0058 80  SER A N   
608   C CA  . SER A 88  ? 0.1901 0.4210 0.2479 -0.0627 -0.0478 -0.0144 80  SER A CA  
609   C C   . SER A 88  ? 0.1620 0.3996 0.2197 -0.0447 -0.0505 -0.0036 80  SER A C   
610   O O   . SER A 88  ? 0.1601 0.3710 0.2084 -0.0407 -0.0449 0.0076  80  SER A O   
611   C CB  . SER A 88  ? 0.2182 0.4719 0.2982 -0.0802 -0.0401 -0.0305 80  SER A CB  
612   O OG  . SER A 88  ? 0.1702 0.4110 0.2534 -0.0828 -0.0295 -0.0244 80  SER A OG  
613   N N   . ILE A 89  ? 0.2331 0.5030 0.2996 -0.0320 -0.0570 -0.0085 81  ILE A N   
614   C CA  . ILE A 89  ? 0.2182 0.4956 0.2848 -0.0141 -0.0573 0.0009  81  ILE A CA  
615   C C   . ILE A 89  ? 0.1834 0.4587 0.2626 -0.0235 -0.0480 0.0015  81  ILE A C   
616   O O   . ILE A 89  ? 0.1991 0.4538 0.2703 -0.0149 -0.0428 0.0127  81  ILE A O   
617   C CB  . ILE A 89  ? 0.2059 0.5118 0.2759 0.0033  -0.0630 -0.0053 81  ILE A CB  
618   C CG1 . ILE A 89  ? 0.2489 0.5445 0.2974 0.0200  -0.0688 0.0006  81  ILE A CG1 
619   C CG2 . ILE A 89  ? 0.2760 0.5928 0.3502 0.0189  -0.0605 0.0015  81  ILE A CG2 
620   C CD1 . ILE A 89  ? 0.3033 0.5692 0.3311 0.0352  -0.0651 0.0189  81  ILE A CD1 
621   N N   . GLU A 90  ? 0.1661 0.4574 0.2635 -0.0418 -0.0427 -0.0117 82  GLU A N   
622   C CA  A GLU A 90  ? 0.1688 0.4513 0.2742 -0.0505 -0.0307 -0.0109 82  GLU A CA  
623   C CA  B GLU A 90  ? 0.1693 0.4517 0.2747 -0.0507 -0.0306 -0.0110 82  GLU A CA  
624   C C   . GLU A 90  ? 0.1584 0.3935 0.2429 -0.0532 -0.0230 0.0016  82  GLU A C   
625   O O   . GLU A 90  ? 0.1827 0.4061 0.2645 -0.0489 -0.0168 0.0086  82  GLU A O   
626   C CB  A GLU A 90  ? 0.1962 0.4977 0.3221 -0.0718 -0.0220 -0.0283 82  GLU A CB  
627   C CB  B GLU A 90  ? 0.1974 0.4981 0.3229 -0.0724 -0.0219 -0.0283 82  GLU A CB  
628   C CG  A GLU A 90  ? 0.2709 0.6087 0.4132 -0.0650 -0.0269 -0.0426 82  GLU A CG  
629   C CG  B GLU A 90  ? 0.2175 0.5071 0.3494 -0.0820 -0.0065 -0.0277 82  GLU A CG  
630   C CD  A GLU A 90  ? 0.3524 0.7096 0.5014 -0.0472 -0.0294 -0.0370 82  GLU A CD  
631   C CD  B GLU A 90  ? 0.3381 0.6575 0.4852 -0.0692 -0.0086 -0.0275 82  GLU A CD  
632   O OE1 A GLU A 90  ? 0.3601 0.7100 0.5148 -0.0521 -0.0195 -0.0324 82  GLU A OE1 
633   O OE1 B GLU A 90  ? 0.3477 0.6951 0.5017 -0.0552 -0.0190 -0.0335 82  GLU A OE1 
634   O OE2 A GLU A 90  ? 0.3722 0.7499 0.5183 -0.0270 -0.0399 -0.0367 82  GLU A OE2 
635   O OE2 B GLU A 90  ? 0.3631 0.6656 0.5070 -0.0690 0.0013  -0.0202 82  GLU A OE2 
636   N N   . ASP A 91  ? 0.2016 0.4121 0.2711 -0.0588 -0.0238 0.0034  83  ASP A N   
637   C CA  . ASP A 91  ? 0.1718 0.3449 0.2211 -0.0567 -0.0193 0.0139  83  ASP A CA  
638   C C   . ASP A 91  ? 0.2093 0.3770 0.2516 -0.0412 -0.0234 0.0229  83  ASP A C   
639   O O   . ASP A 91  ? 0.1750 0.3277 0.2110 -0.0386 -0.0178 0.0277  83  ASP A O   
640   C CB  . ASP A 91  ? 0.1810 0.3339 0.2164 -0.0618 -0.0209 0.0135  83  ASP A CB  
641   C CG  . ASP A 91  ? 0.2484 0.3934 0.2854 -0.0784 -0.0111 0.0052  83  ASP A CG  
642   O OD1 . ASP A 91  ? 0.2563 0.3993 0.2990 -0.0861 0.0005  0.0028  83  ASP A OD1 
643   O OD2 . ASP A 91  ? 0.2721 0.4099 0.3036 -0.0841 -0.0125 0.0008  83  ASP A OD2 
644   N N   . LEU A 92  ? 0.1547 0.3337 0.1966 -0.0304 -0.0311 0.0245  84  LEU A N   
645   C CA  . LEU A 92  ? 0.1837 0.3511 0.2172 -0.0168 -0.0298 0.0325  84  LEU A CA  
646   C C   . LEU A 92  ? 0.1804 0.3573 0.2227 -0.0106 -0.0244 0.0342  84  LEU A C   
647   O O   . LEU A 92  ? 0.1945 0.3544 0.2305 -0.0056 -0.0180 0.0386  84  LEU A O   
648   C CB  . LEU A 92  ? 0.1660 0.3379 0.1920 -0.0041 -0.0356 0.0355  84  LEU A CB  
649   C CG  . LEU A 92  ? 0.2204 0.3847 0.2373 -0.0091 -0.0410 0.0334  84  LEU A CG  
650   C CD1 . LEU A 92  ? 0.2544 0.4191 0.2592 0.0063  -0.0444 0.0381  84  LEU A CD1 
651   C CD2 . LEU A 92  ? 0.2168 0.3537 0.2246 -0.0169 -0.0366 0.0348  84  LEU A CD2 
652   N N   . LYS A 93  ? 0.1688 0.3746 0.2273 -0.0117 -0.0259 0.0286  85  LYS A N   
653   C CA  . LYS A 93  ? 0.1753 0.3921 0.2438 -0.0062 -0.0201 0.0293  85  LYS A CA  
654   C C   . LYS A 93  ? 0.1955 0.3948 0.2627 -0.0171 -0.0109 0.0295  85  LYS A C   
655   O O   . LYS A 93  ? 0.1328 0.3354 0.2052 -0.0128 -0.0046 0.0308  85  LYS A O   
656   C CB  . LYS A 93  ? 0.1749 0.4335 0.2644 -0.0057 -0.0240 0.0201  85  LYS A CB  
657   C CG  . LYS A 93  ? 0.1977 0.4820 0.2871 0.0129  -0.0338 0.0201  85  LYS A CG  
658   C CD  . LYS A 93  ? 0.2245 0.5600 0.3387 0.0144  -0.0382 0.0072  85  LYS A CD  
659   C CE  . LYS A 93  ? 0.2606 0.6136 0.3662 0.0372  -0.0471 0.0064  85  LYS A CE  
660   N NZ  . LYS A 93  ? 0.2944 0.6835 0.4170 0.0338  -0.0506 -0.0115 85  LYS A NZ  
661   N N   . ASN A 94  ? 0.1659 0.3464 0.2238 -0.0287 -0.0094 0.0285  86  ASN A N   
662   C CA  . ASN A 94  ? 0.1641 0.3270 0.2146 -0.0351 -0.0007 0.0295  86  ASN A CA  
663   C C   . ASN A 94  ? 0.1625 0.3021 0.1953 -0.0307 -0.0013 0.0333  86  ASN A C   
664   O O   . ASN A 94  ? 0.1505 0.2756 0.1712 -0.0334 0.0030  0.0338  86  ASN A O   
665   C CB  . ASN A 94  ? 0.1576 0.3161 0.2078 -0.0488 0.0048  0.0252  86  ASN A CB  
666   C CG  . ASN A 94  ? 0.3674 0.5521 0.4392 -0.0569 0.0098  0.0170  86  ASN A CG  
667   O OD1 . ASN A 94  ? 0.3954 0.5982 0.4795 -0.0511 0.0111  0.0164  86  ASN A OD1 
668   N ND2 . ASN A 94  ? 0.4032 0.5908 0.4807 -0.0710 0.0140  0.0088  86  ASN A ND2 
669   N N   . PHE A 95  ? 0.1261 0.2631 0.1566 -0.0231 -0.0054 0.0350  87  PHE A N   
670   C CA  . PHE A 95  ? 0.1264 0.2473 0.1455 -0.0207 -0.0045 0.0342  87  PHE A CA  
671   C C   . PHE A 95  ? 0.1360 0.2534 0.1517 -0.0202 0.0019  0.0317  87  PHE A C   
672   O O   . PHE A 95  ? 0.1350 0.2580 0.1578 -0.0175 0.0073  0.0320  87  PHE A O   
673   C CB  . PHE A 95  ? 0.1597 0.2766 0.1791 -0.0135 -0.0035 0.0355  87  PHE A CB  
674   C CG  . PHE A 95  ? 0.1556 0.2587 0.1678 -0.0142 0.0001  0.0307  87  PHE A CG  
675   C CD1 . PHE A 95  ? 0.1740 0.2734 0.1796 -0.0184 -0.0047 0.0272  87  PHE A CD1 
676   C CD2 . PHE A 95  ? 0.1646 0.2592 0.1777 -0.0110 0.0100  0.0281  87  PHE A CD2 
677   C CE1 . PHE A 95  ? 0.1283 0.2223 0.1313 -0.0198 -0.0013 0.0191  87  PHE A CE1 
678   C CE2 . PHE A 95  ? 0.2086 0.2938 0.2190 -0.0149 0.0157  0.0193  87  PHE A CE2 
679   C CZ  . PHE A 95  ? 0.1943 0.2825 0.2012 -0.0195 0.0092  0.0139  87  PHE A CZ  
680   N N   . ARG A 96  ? 0.1332 0.2433 0.1367 -0.0210 0.0009  0.0289  88  ARG A N   
681   C CA  . ARG A 96  ? 0.1661 0.2761 0.1623 -0.0180 0.0051  0.0246  88  ARG A CA  
682   C C   . ARG A 96  ? 0.2001 0.3106 0.1944 -0.0186 0.0112  0.0282  88  ARG A C   
683   O O   . ARG A 96  ? 0.1925 0.3047 0.1823 -0.0153 0.0159  0.0250  88  ARG A O   
684   C CB  . ARG A 96  ? 0.1753 0.2878 0.1785 -0.0165 0.0096  0.0177  88  ARG A CB  
685   C CG  . ARG A 96  ? 0.1681 0.2784 0.1710 -0.0176 0.0078  0.0103  88  ARG A CG  
686   C CD  . ARG A 96  ? 0.1752 0.2823 0.1854 -0.0191 0.0176  0.0016  88  ARG A CD  
687   N NE  . ARG A 96  ? 0.2346 0.3428 0.2453 -0.0229 0.0179  -0.0100 88  ARG A NE  
688   C CZ  . ARG A 96  ? 0.2361 0.3564 0.2480 -0.0254 0.0199  -0.0264 88  ARG A CZ  
689   N NH1 . ARG A 96  ? 0.2534 0.3831 0.2636 -0.0236 0.0218  -0.0321 88  ARG A NH1 
690   N NH2 . ARG A 96  ? 0.2559 0.3823 0.2718 -0.0298 0.0203  -0.0390 88  ARG A NH2 
691   N N   . GLN A 97  ? 0.1770 0.2863 0.1746 -0.0239 0.0129  0.0329  89  GLN A N   
692   C CA  . GLN A 97  ? 0.1841 0.2925 0.1813 -0.0270 0.0223  0.0350  89  GLN A CA  
693   C C   . GLN A 97  ? 0.1923 0.2816 0.1679 -0.0271 0.0278  0.0385  89  GLN A C   
694   O O   . GLN A 97  ? 0.1836 0.2634 0.1500 -0.0269 0.0236  0.0397  89  GLN A O   
695   C CB  . GLN A 97  ? 0.2101 0.3332 0.2284 -0.0342 0.0241  0.0344  89  GLN A CB  
696   C CG  . GLN A 97  ? 0.2176 0.3572 0.2521 -0.0286 0.0197  0.0333  89  GLN A CG  
697   C CD  . GLN A 97  ? 0.2527 0.3892 0.2839 -0.0219 0.0243  0.0324  89  GLN A CD  
698   O OE1 . GLN A 97  ? 0.2057 0.3430 0.2363 -0.0224 0.0322  0.0320  89  GLN A OE1 
699   N NE2 . GLN A 97  ? 0.2460 0.3774 0.2745 -0.0168 0.0215  0.0309  89  GLN A NE2 
700   N N   . LEU A 98  ? 0.1980 0.2789 0.1626 -0.0256 0.0388  0.0407  90  LEU A N   
701   C CA  . LEU A 98  ? 0.2959 0.3522 0.2318 -0.0207 0.0476  0.0461  90  LEU A CA  
702   C C   . LEU A 98  ? 0.3468 0.3877 0.2814 -0.0301 0.0529  0.0481  90  LEU A C   
703   O O   . LEU A 98  ? 0.2450 0.2918 0.1990 -0.0443 0.0598  0.0448  90  LEU A O   
704   C CB  . LEU A 98  ? 0.2478 0.2947 0.1728 -0.0194 0.0626  0.0490  90  LEU A CB  
705   C CG  . LEU A 98  ? 0.2867 0.3022 0.1733 -0.0089 0.0747  0.0569  90  LEU A CG  
706   C CD1 . LEU A 98  ? 0.2914 0.3080 0.1541 0.0103  0.0627  0.0573  90  LEU A CD1 
707   C CD2 . LEU A 98  ? 0.3097 0.3152 0.1845 -0.0071 0.0908  0.0599  90  LEU A CD2 
708   N N   . HIS A 99  ? 0.2485 0.2729 0.1616 -0.0220 0.0496  0.0515  91  HIS A N   
709   C CA  . HIS A 99  ? 0.2659 0.2682 0.1699 -0.0282 0.0568  0.0538  91  HIS A CA  
710   C C   . HIS A 99  ? 0.2994 0.3188 0.2308 -0.0419 0.0481  0.0471  91  HIS A C   
711   O O   . HIS A 99  ? 0.3027 0.3083 0.2336 -0.0523 0.0560  0.0453  91  HIS A O   
712   C CB  . HIS A 99  ? 0.3010 0.2756 0.1922 -0.0359 0.0804  0.0571  91  HIS A CB  
713   C CG  . HIS A 99  ? 0.3466 0.2967 0.2015 -0.0188 0.0917  0.0661  91  HIS A CG  
714   N ND1 . HIS A 99  ? 0.3977 0.3333 0.2450 -0.0226 0.1111  0.0687  91  HIS A ND1 
715   C CD2 . HIS A 99  ? 0.3786 0.3190 0.2015 0.0041  0.0860  0.0723  91  HIS A CD2 
716   C CE1 . HIS A 99  ? 0.4224 0.3371 0.2312 -0.0016 0.1172  0.0777  91  HIS A CE1 
717   N NE2 . HIS A 99  ? 0.3979 0.3177 0.1917 0.0158  0.1012  0.0795  91  HIS A NE2 
718   N N   . SER A 100 ? 0.2679 0.3151 0.2206 -0.0412 0.0334  0.0429  92  SER A N   
719   C CA  . SER A 100 ? 0.2464 0.3100 0.2198 -0.0497 0.0246  0.0378  92  SER A CA  
720   C C   . SER A 100 ? 0.2681 0.3212 0.2293 -0.0452 0.0167  0.0389  92  SER A C   
721   O O   . SER A 100 ? 0.2644 0.3049 0.2055 -0.0337 0.0153  0.0426  92  SER A O   
722   C CB  . SER A 100 ? 0.1915 0.2819 0.1856 -0.0469 0.0149  0.0351  92  SER A CB  
723   O OG  . SER A 100 ? 0.2157 0.3065 0.2039 -0.0372 0.0057  0.0361  92  SER A OG  
724   N N   . LYS A 101 ? 0.2637 0.3256 0.2375 -0.0530 0.0112  0.0345  93  LYS A N   
725   C CA  . LYS A 101 ? 0.2680 0.3213 0.2322 -0.0494 0.0040  0.0350  93  LYS A CA  
726   C C   . LYS A 101 ? 0.2148 0.2812 0.1833 -0.0405 -0.0079 0.0350  93  LYS A C   
727   O O   . LYS A 101 ? 0.2486 0.3111 0.2117 -0.0376 -0.0138 0.0344  93  LYS A O   
728   C CB  . LYS A 101 ? 0.3630 0.4206 0.3372 -0.0615 0.0036  0.0288  93  LYS A CB  
729   C CG  . LYS A 101 ? 0.3991 0.4371 0.3673 -0.0736 0.0198  0.0258  93  LYS A CG  
730   C CD  . LYS A 101 ? 0.5177 0.5709 0.5035 -0.0888 0.0194  0.0141  93  LYS A CD  
731   C CE  . LYS A 101 ? 0.6124 0.6371 0.5878 -0.1022 0.0378  0.0092  93  LYS A CE  
732   N NZ  . LYS A 101 ? 0.6586 0.6992 0.6492 -0.1163 0.0351  -0.0048 93  LYS A NZ  
733   N N   . THR A 102 ? 0.1816 0.2608 0.1588 -0.0365 -0.0090 0.0349  94  THR A N   
734   C CA  . THR A 102 ? 0.1611 0.2488 0.1434 -0.0307 -0.0152 0.0332  94  THR A CA  
735   C C   . THR A 102 ? 0.1948 0.2841 0.1730 -0.0244 -0.0125 0.0312  94  THR A C   
736   O O   . THR A 102 ? 0.1890 0.2864 0.1771 -0.0236 -0.0103 0.0298  94  THR A O   
737   C CB  . THR A 102 ? 0.1664 0.2682 0.1642 -0.0318 -0.0172 0.0332  94  THR A CB  
738   O OG1 . THR A 102 ? 0.1742 0.2857 0.1815 -0.0348 -0.0125 0.0334  94  THR A OG1 
739   C CG2 . THR A 102 ? 0.1472 0.2524 0.1471 -0.0350 -0.0227 0.0325  94  THR A CG2 
740   N N   . PRO A 103 ? 0.2029 0.2857 0.1654 -0.0183 -0.0123 0.0302  95  PRO A N   
741   C CA  . PRO A 103 ? 0.2199 0.3111 0.1788 -0.0113 -0.0116 0.0247  95  PRO A CA  
742   C C   . PRO A 103 ? 0.1751 0.2773 0.1460 -0.0125 -0.0139 0.0156  95  PRO A C   
743   O O   . PRO A 103 ? 0.1522 0.2524 0.1287 -0.0158 -0.0164 0.0149  95  PRO A O   
744   C CB  . PRO A 103 ? 0.2172 0.3025 0.1538 -0.0005 -0.0128 0.0251  95  PRO A CB  
745   C CG  . PRO A 103 ? 0.1763 0.2502 0.1085 -0.0023 -0.0155 0.0286  95  PRO A CG  
746   C CD  . PRO A 103 ? 0.1755 0.2442 0.1210 -0.0150 -0.0125 0.0331  95  PRO A CD  
747   N N   . GLY A 104 ? 0.1623 0.2748 0.1360 -0.0103 -0.0111 0.0075  96  GLY A N   
748   C CA  . GLY A 104 ? 0.1783 0.2969 0.1651 -0.0148 -0.0075 -0.0029 96  GLY A CA  
749   C C   . GLY A 104 ? 0.2297 0.3543 0.2182 -0.0156 -0.0106 -0.0124 96  GLY A C   
750   O O   . GLY A 104 ? 0.2068 0.3274 0.2054 -0.0219 -0.0048 -0.0175 96  GLY A O   
751   N N   . HIS A 105 ? 0.1333 0.2879 0.1515 0.0165  0.0470  0.0199  97  HIS A N   
752   C CA  . HIS A 105 ? 0.1302 0.2707 0.1386 0.0135  0.0403  0.0181  97  HIS A CA  
753   C C   . HIS A 105 ? 0.1941 0.3362 0.2054 0.0061  0.0339  0.0223  97  HIS A C   
754   O O   . HIS A 105 ? 0.1837 0.3341 0.1988 0.0015  0.0353  0.0260  97  HIS A O   
755   C CB  . HIS A 105 ? 0.1982 0.3273 0.1918 0.0129  0.0425  0.0142  97  HIS A CB  
756   C CG  . HIS A 105 ? 0.2520 0.3767 0.2404 0.0194  0.0479  0.0096  97  HIS A CG  
757   N ND1 . HIS A 105 ? 0.3509 0.4727 0.3295 0.0196  0.0532  0.0071  97  HIS A ND1 
758   C CD2 . HIS A 105 ? 0.3381 0.4594 0.3286 0.0258  0.0482  0.0069  97  HIS A CD2 
759   C CE1 . HIS A 105 ? 0.3769 0.4932 0.3514 0.0260  0.0567  0.0027  97  HIS A CE1 
760   N NE2 . HIS A 105 ? 0.2889 0.4049 0.2711 0.0299  0.0537  0.0026  97  HIS A NE2 
761   N N   . PRO A 106 ? 0.2035 0.3374 0.2126 0.0048  0.0269  0.0221  98  PRO A N   
762   C CA  . PRO A 106 ? 0.1812 0.3152 0.1922 -0.0019 0.0204  0.0257  98  PRO A CA  
763   C C   . PRO A 106 ? 0.1563 0.2851 0.1594 -0.0073 0.0205  0.0261  98  PRO A C   
764   O O   . PRO A 106 ? 0.2020 0.3218 0.1952 -0.0061 0.0225  0.0228  98  PRO A O   
765   C CB  . PRO A 106 ? 0.2077 0.3306 0.2135 -0.0009 0.0143  0.0239  98  PRO A CB  
766   C CG  . PRO A 106 ? 0.2692 0.3906 0.2751 0.0062  0.0174  0.0209  98  PRO A CG  
767   C CD  . PRO A 106 ? 0.2749 0.3980 0.2780 0.0089  0.0248  0.0185  98  PRO A CD  
768   N N   . GLU A 107 ? 0.1758 0.3103 0.1839 -0.0135 0.0176  0.0306  99  GLU A N   
769   C CA  . GLU A 107 ? 0.1503 0.2813 0.1526 -0.0190 0.0176  0.0321  99  GLU A CA  
770   C C   . GLU A 107 ? 0.2132 0.3354 0.2126 -0.0246 0.0095  0.0336  99  GLU A C   
771   O O   . GLU A 107 ? 0.2156 0.3428 0.2224 -0.0284 0.0047  0.0373  99  GLU A O   
772   C CB  . GLU A 107 ? 0.1653 0.3106 0.1751 -0.0220 0.0223  0.0367  99  GLU A CB  
773   C CG  . GLU A 107 ? 0.1327 0.2827 0.1403 -0.0166 0.0312  0.0341  99  GLU A CG  
774   C CD  . GLU A 107 ? 0.1589 0.3231 0.1726 -0.0190 0.0373  0.0385  99  GLU A CD  
775   O OE1 . GLU A 107 ? 0.2093 0.3789 0.2282 -0.0259 0.0343  0.0440  99  GLU A OE1 
776   O OE2 . GLU A 107 ? 0.1682 0.3376 0.1810 -0.0138 0.0453  0.0364  99  GLU A OE2 
777   N N   . TYR A 108 ? 0.2056 0.3142 0.1942 -0.0248 0.0078  0.0308  100 TYR A N   
778   C CA  . TYR A 108 ? 0.1581 0.2561 0.1421 -0.0294 0.0011  0.0315  100 TYR A CA  
779   C C   . TYR A 108 ? 0.2022 0.3053 0.1906 -0.0368 -0.0013 0.0369  100 TYR A C   
780   O O   . TYR A 108 ? 0.1873 0.2974 0.1772 -0.0385 0.0031  0.0392  100 TYR A O   
781   C CB  . TYR A 108 ? 0.1708 0.2553 0.1443 -0.0275 0.0013  0.0281  100 TYR A CB  
782   C CG  . TYR A 108 ? 0.1857 0.2585 0.1541 -0.0316 -0.0046 0.0288  100 TYR A CG  
783   C CD1 . TYR A 108 ? 0.1828 0.2465 0.1472 -0.0310 -0.0093 0.0268  100 TYR A CD1 
784   C CD2 . TYR A 108 ? 0.2024 0.2722 0.1689 -0.0361 -0.0056 0.0314  100 TYR A CD2 
785   C CE1 . TYR A 108 ? 0.2522 0.3034 0.2106 -0.0342 -0.0145 0.0267  100 TYR A CE1 
786   C CE2 . TYR A 108 ? 0.2626 0.3203 0.2244 -0.0394 -0.0112 0.0318  100 TYR A CE2 
787   C CZ  . TYR A 108 ? 0.3289 0.3769 0.2864 -0.0381 -0.0154 0.0291  100 TYR A CZ  
788   O OH  . TYR A 108 ? 0.4715 0.5055 0.4228 -0.0407 -0.0208 0.0288  100 TYR A OH  
789   N N   . GLY A 109 ? 0.2146 0.3131 0.2039 -0.0416 -0.0086 0.0389  101 GLY A N   
790   C CA  . GLY A 109 ? 0.2690 0.3698 0.2620 -0.0495 -0.0126 0.0443  101 GLY A CA  
791   C C   . GLY A 109 ? 0.3176 0.4360 0.3244 -0.0530 -0.0121 0.0500  101 GLY A C   
792   O O   . GLY A 109 ? 0.3446 0.4654 0.3564 -0.0606 -0.0172 0.0553  101 GLY A O   
793   N N   . TYR A 110 ? 0.3163 0.4470 0.3302 -0.0476 -0.0062 0.0493  102 TYR A N   
794   C CA  . TYR A 110 ? 0.3335 0.4828 0.3627 -0.0493 -0.0044 0.0548  102 TYR A CA  
795   C C   . TYR A 110 ? 0.3221 0.4738 0.3585 -0.0489 -0.0107 0.0556  102 TYR A C   
796   O O   . TYR A 110 ? 0.3951 0.5563 0.4430 -0.0546 -0.0155 0.0616  102 TYR A O   
797   C CB  . TYR A 110 ? 0.3403 0.5011 0.3729 -0.0428 0.0062  0.0534  102 TYR A CB  
798   C CG  . TYR A 110 ? 0.3660 0.5475 0.4148 -0.0439 0.0104  0.0594  102 TYR A CG  
799   C CD1 . TYR A 110 ? 0.4628 0.6531 0.5189 -0.0521 0.0090  0.0665  102 TYR A CD1 
800   C CD2 . TYR A 110 ? 0.3662 0.5587 0.4238 -0.0366 0.0161  0.0583  102 TYR A CD2 
801   C CE1 . TYR A 110 ? 0.4871 0.6981 0.5596 -0.0530 0.0136  0.0728  102 TYR A CE1 
802   C CE2 . TYR A 110 ? 0.3771 0.5896 0.4510 -0.0368 0.0208  0.0640  102 TYR A CE2 
803   C CZ  . TYR A 110 ? 0.4464 0.6689 0.5282 -0.0450 0.0198  0.0714  102 TYR A CZ  
804   O OH  . TYR A 110 ? 0.4850 0.7292 0.5846 -0.0451 0.0253  0.0778  102 TYR A OH  
805   N N   . THR A 111 ? 0.2284 0.3709 0.2578 -0.0427 -0.0113 0.0500  103 THR A N   
806   C CA  . THR A 111 ? 0.2197 0.3640 0.2544 -0.0411 -0.0166 0.0504  103 THR A CA  
807   C C   . THR A 111 ? 0.1992 0.3240 0.2198 -0.0426 -0.0243 0.0467  103 THR A C   
808   O O   . THR A 111 ? 0.2016 0.3136 0.2095 -0.0386 -0.0216 0.0412  103 THR A O   
809   C CB  . THR A 111 ? 0.2303 0.3808 0.2685 -0.0321 -0.0099 0.0474  103 THR A CB  
810   O OG1 . THR A 111 ? 0.2518 0.4187 0.3009 -0.0301 -0.0016 0.0501  103 THR A OG1 
811   C CG2 . THR A 111 ? 0.1772 0.3297 0.2212 -0.0302 -0.0156 0.0484  103 THR A CG2 
812   N N   . ASP A 112 ? 0.2452 0.3677 0.2678 -0.0483 -0.0337 0.0498  104 ASP A N   
813   C CA  . ASP A 112 ? 0.2494 0.3523 0.2568 -0.0496 -0.0410 0.0460  104 ASP A CA  
814   C C   . ASP A 112 ? 0.1844 0.2806 0.1837 -0.0418 -0.0383 0.0406  104 ASP A C   
815   O O   . ASP A 112 ? 0.1970 0.3035 0.2050 -0.0377 -0.0366 0.0418  104 ASP A O   
816   C CB  . ASP A 112 ? 0.2918 0.3940 0.3027 -0.0568 -0.0523 0.0503  104 ASP A CB  
817   C CG  . ASP A 112 ? 0.3372 0.4388 0.3509 -0.0660 -0.0575 0.0548  104 ASP A CG  
818   O OD1 . ASP A 112 ? 0.3306 0.4311 0.3423 -0.0667 -0.0525 0.0545  104 ASP A OD1 
819   O OD2 . ASP A 112 ? 0.3883 0.4900 0.4060 -0.0729 -0.0673 0.0592  104 ASP A OD2 
820   N N   . GLY A 113 ? 0.2524 0.3312 0.2357 -0.0397 -0.0381 0.0353  105 GLY A N   
821   C CA  . GLY A 113 ? 0.2357 0.3069 0.2102 -0.0332 -0.0359 0.0308  105 GLY A CA  
822   C C   . GLY A 113 ? 0.2647 0.3390 0.2395 -0.0264 -0.0264 0.0277  105 GLY A C   
823   O O   . GLY A 113 ? 0.2462 0.3125 0.2126 -0.0215 -0.0243 0.0240  105 GLY A O   
824   N N   . VAL A 114 ? 0.1586 0.2437 0.1419 -0.0263 -0.0209 0.0294  106 VAL A N   
825   C CA  . VAL A 114 ? 0.1545 0.2403 0.1361 -0.0208 -0.0128 0.0264  106 VAL A CA  
826   C C   . VAL A 114 ? 0.2515 0.3248 0.2225 -0.0215 -0.0118 0.0238  106 VAL A C   
827   O O   . VAL A 114 ? 0.2585 0.3306 0.2295 -0.0264 -0.0135 0.0257  106 VAL A O   
828   C CB  . VAL A 114 ? 0.1518 0.2530 0.1447 -0.0204 -0.0071 0.0290  106 VAL A CB  
829   C CG1 . VAL A 114 ? 0.1323 0.2315 0.1206 -0.0155 0.0001  0.0255  106 VAL A CG1 
830   C CG2 . VAL A 114 ? 0.1889 0.3033 0.1942 -0.0185 -0.0075 0.0318  106 VAL A CG2 
831   N N   . GLU A 115 ? 0.1641 0.2286 0.1271 -0.0167 -0.0090 0.0199  107 GLU A N   
832   C CA  . GLU A 115 ? 0.1687 0.2212 0.1227 -0.0166 -0.0083 0.0176  107 GLU A CA  
833   C C   . GLU A 115 ? 0.1834 0.2391 0.1392 -0.0155 -0.0031 0.0175  107 GLU A C   
834   O O   . GLU A 115 ? 0.1562 0.2042 0.1075 -0.0165 -0.0032 0.0171  107 GLU A O   
835   C CB  . GLU A 115 ? 0.1937 0.2357 0.1388 -0.0121 -0.0077 0.0141  107 GLU A CB  
836   C CG  . GLU A 115 ? 0.1654 0.2015 0.1050 -0.0132 -0.0132 0.0138  107 GLU A CG  
837   C CD  . GLU A 115 ? 0.2492 0.2751 0.1821 -0.0179 -0.0189 0.0138  107 GLU A CD  
838   O OE1 . GLU A 115 ? 0.2383 0.2589 0.1659 -0.0199 -0.0245 0.0138  107 GLU A OE1 
839   O OE2 . GLU A 115 ? 0.2194 0.2415 0.1517 -0.0199 -0.0184 0.0140  107 GLU A OE2 
840   N N   . THR A 116 ? 0.1647 0.2305 0.1264 -0.0133 0.0012  0.0180  108 THR A N   
841   C CA  . THR A 116 ? 0.1499 0.2174 0.1111 -0.0125 0.0057  0.0176  108 THR A CA  
842   C C   . THR A 116 ? 0.1736 0.2529 0.1412 -0.0109 0.0097  0.0183  108 THR A C   
843   O O   . THR A 116 ? 0.1596 0.2445 0.1321 -0.0086 0.0097  0.0183  108 THR A O   
844   C CB  . THR A 116 ? 0.1641 0.2233 0.1197 -0.0084 0.0077  0.0147  108 THR A CB  
845   O OG1 . THR A 116 ? 0.1401 0.2009 0.0951 -0.0083 0.0109  0.0148  108 THR A OG1 
846   C CG2 . THR A 116 ? 0.2191 0.2787 0.1749 -0.0038 0.0088  0.0128  108 THR A CG2 
847   N N   . THR A 117 ? 0.1753 0.2581 0.1424 -0.0121 0.0132  0.0190  109 THR A N   
848   C CA  . THR A 117 ? 0.1619 0.2544 0.1328 -0.0099 0.0182  0.0190  109 THR A CA  
849   C C   . THR A 117 ? 0.1482 0.2355 0.1142 -0.0049 0.0212  0.0152  109 THR A C   
850   O O   . THR A 117 ? 0.1324 0.2126 0.0919 -0.0056 0.0212  0.0143  109 THR A O   
851   C CB  . THR A 117 ? 0.1623 0.2604 0.1331 -0.0141 0.0207  0.0217  109 THR A CB  
852   O OG1 . THR A 117 ? 0.1580 0.2606 0.1340 -0.0194 0.0172  0.0258  109 THR A OG1 
853   C CG2 . THR A 117 ? 0.1802 0.2879 0.1535 -0.0111 0.0272  0.0212  109 THR A CG2 
854   N N   . THR A 118 ? 0.1514 0.2418 0.1208 -0.0002 0.0230  0.0136  110 THR A N   
855   C CA  . THR A 118 ? 0.1822 0.2670 0.1470 0.0042  0.0253  0.0102  110 THR A CA  
856   C C   . THR A 118 ? 0.2247 0.3163 0.1920 0.0077  0.0304  0.0090  110 THR A C   
857   O O   . THR A 118 ? 0.3645 0.4662 0.3396 0.0082  0.0321  0.0109  110 THR A O   
858   C CB  . THR A 118 ? 0.2001 0.2790 0.1648 0.0072  0.0226  0.0090  110 THR A CB  
859   O OG1 . THR A 118 ? 0.2231 0.3085 0.1951 0.0091  0.0216  0.0101  110 THR A OG1 
860   C CG2 . THR A 118 ? 0.2766 0.3481 0.2377 0.0045  0.0187  0.0098  110 THR A CG2 
861   N N   . GLY A 119 ? 0.2701 0.3554 0.2308 0.0104  0.0327  0.0059  111 GLY A N   
862   C CA  . GLY A 119 ? 0.2830 0.3710 0.2425 0.0143  0.0380  0.0036  111 GLY A CA  
863   C C   . GLY A 119 ? 0.2401 0.3168 0.1893 0.0151  0.0379  0.0003  111 GLY A C   
864   O O   . GLY A 119 ? 0.2770 0.3480 0.2249 0.0193  0.0379  -0.0023 111 GLY A O   
865   N N   . PRO A 120 ? 0.2047 0.2775 0.1465 0.0107  0.0371  0.0009  112 PRO A N   
866   C CA  . PRO A 120 ? 0.1686 0.2303 0.1014 0.0102  0.0352  -0.0012 112 PRO A CA  
867   C C   . PRO A 120 ? 0.2286 0.2845 0.1644 0.0111  0.0309  -0.0009 112 PRO A C   
868   O O   . PRO A 120 ? 0.2050 0.2620 0.1450 0.0089  0.0281  0.0016  112 PRO A O   
869   C CB  . PRO A 120 ? 0.2053 0.2659 0.1328 0.0044  0.0335  0.0012  112 PRO A CB  
870   C CG  . PRO A 120 ? 0.3042 0.3752 0.2351 0.0027  0.0369  0.0034  112 PRO A CG  
871   C CD  . PRO A 120 ? 0.2889 0.3671 0.2308 0.0055  0.0371  0.0042  112 PRO A CD  
872   N N   . LEU A 121 ? 0.1547 0.2039 0.0878 0.0143  0.0308  -0.0035 113 LEU A N   
873   C CA  . LEU A 121 ? 0.1442 0.1892 0.0809 0.0157  0.0276  -0.0028 113 LEU A CA  
874   C C   . LEU A 121 ? 0.1857 0.2256 0.1209 0.0119  0.0240  -0.0007 113 LEU A C   
875   O O   . LEU A 121 ? 0.1666 0.2034 0.0967 0.0087  0.0229  -0.0003 113 LEU A O   
876   C CB  . LEU A 121 ? 0.2091 0.2476 0.1433 0.0198  0.0282  -0.0057 113 LEU A CB  
877   C CG  . LEU A 121 ? 0.2350 0.2788 0.1729 0.0249  0.0320  -0.0076 113 LEU A CG  
878   C CD1 . LEU A 121 ? 0.3048 0.3402 0.2394 0.0293  0.0323  -0.0107 113 LEU A CD1 
879   C CD2 . LEU A 121 ? 0.2615 0.3135 0.2091 0.0260  0.0312  -0.0049 113 LEU A CD2 
880   N N   . GLY A 122 ? 0.1527 0.1918 0.0924 0.0125  0.0222  0.0011  114 GLY A N   
881   C CA  . GLY A 122 ? 0.1697 0.2056 0.1104 0.0100  0.0197  0.0036  114 GLY A CA  
882   C C   . GLY A 122 ? 0.1738 0.2131 0.1167 0.0077  0.0192  0.0058  114 GLY A C   
883   O O   . GLY A 122 ? 0.1666 0.2044 0.1122 0.0075  0.0182  0.0077  114 GLY A O   
884   N N   . GLN A 123 ? 0.1690 0.2127 0.1110 0.0059  0.0201  0.0056  115 GLN A N   
885   C CA  . GLN A 123 ? 0.1797 0.2248 0.1233 0.0032  0.0189  0.0079  115 GLN A CA  
886   C C   . GLN A 123 ? 0.1602 0.2069 0.1071 0.0045  0.0186  0.0082  115 GLN A C   
887   O O   . GLN A 123 ? 0.2069 0.2516 0.1544 0.0032  0.0173  0.0097  115 GLN A O   
888   C CB  . GLN A 123 ? 0.1303 0.1791 0.0716 0.0001  0.0194  0.0085  115 GLN A CB  
889   C CG  . GLN A 123 ? 0.1356 0.1809 0.0713 -0.0021 0.0187  0.0086  115 GLN A CG  
890   C CD  . GLN A 123 ? 0.1640 0.2126 0.0960 -0.0056 0.0195  0.0097  115 GLN A CD  
891   O OE1 . GLN A 123 ? 0.1602 0.2099 0.0940 -0.0085 0.0178  0.0124  115 GLN A OE1 
892   N NE2 . GLN A 123 ? 0.1562 0.2055 0.0822 -0.0053 0.0222  0.0077  115 GLN A NE2 
893   N N   . GLY A 124 ? 0.1626 0.2121 0.1110 0.0071  0.0196  0.0070  116 GLY A N   
894   C CA  . GLY A 124 ? 0.1589 0.2090 0.1090 0.0076  0.0183  0.0075  116 GLY A CA  
895   C C   . GLY A 124 ? 0.1611 0.2050 0.1094 0.0087  0.0176  0.0080  116 GLY A C   
896   O O   . GLY A 124 ? 0.1431 0.1845 0.0901 0.0078  0.0164  0.0085  116 GLY A O   
897   N N   . ILE A 125 ? 0.1348 0.1758 0.0828 0.0107  0.0185  0.0079  117 ILE A N   
898   C CA  . ILE A 125 ? 0.1741 0.2104 0.1212 0.0119  0.0189  0.0089  117 ILE A CA  
899   C C   . ILE A 125 ? 0.1506 0.1849 0.0984 0.0104  0.0189  0.0102  117 ILE A C   
900   O O   . ILE A 125 ? 0.1403 0.1713 0.0870 0.0114  0.0196  0.0107  117 ILE A O   
901   C CB  . ILE A 125 ? 0.1797 0.2141 0.1275 0.0137  0.0197  0.0094  117 ILE A CB  
902   C CG1 . ILE A 125 ? 0.1574 0.1885 0.1051 0.0148  0.0211  0.0114  117 ILE A CG1 
903   C CG2 . ILE A 125 ? 0.1936 0.2278 0.1426 0.0123  0.0192  0.0094  117 ILE A CG2 
904   C CD1 . ILE A 125 ? 0.1568 0.1857 0.1004 0.0163  0.0216  0.0110  117 ILE A CD1 
905   N N   . ALA A 126 ? 0.1665 0.2023 0.1157 0.0081  0.0181  0.0108  118 ALA A N   
906   C CA  . ALA A 126 ? 0.1514 0.1854 0.1022 0.0066  0.0174  0.0126  118 ALA A CA  
907   C C   . ALA A 126 ? 0.1674 0.2003 0.1166 0.0055  0.0165  0.0124  118 ALA A C   
908   O O   . ALA A 126 ? 0.1516 0.1806 0.1013 0.0064  0.0166  0.0132  118 ALA A O   
909   C CB  . ALA A 126 ? 0.1896 0.2248 0.1408 0.0038  0.0158  0.0136  118 ALA A CB  
910   N N   . ASN A 127 ? 0.1560 0.1922 0.1037 0.0038  0.0156  0.0114  119 ASN A N   
911   C CA  . ASN A 127 ? 0.1977 0.2324 0.1440 0.0021  0.0139  0.0114  119 ASN A CA  
912   C C   . ASN A 127 ? 0.1524 0.1816 0.0955 0.0046  0.0141  0.0102  119 ASN A C   
913   O O   . ASN A 127 ? 0.1579 0.1813 0.0987 0.0044  0.0131  0.0102  119 ASN A O   
914   C CB  . ASN A 127 ? 0.1893 0.2302 0.1362 0.0000  0.0130  0.0112  119 ASN A CB  
915   C CG  . ASN A 127 ? 0.1667 0.2131 0.1150 -0.0025 0.0137  0.0122  119 ASN A CG  
916   O OD1 . ASN A 127 ? 0.2014 0.2543 0.1513 -0.0030 0.0147  0.0120  119 ASN A OD1 
917   N ND2 . ASN A 127 ? 0.1445 0.1884 0.0920 -0.0040 0.0134  0.0135  119 ASN A ND2 
918   N N   . ALA A 128 ? 0.1436 0.1735 0.0857 0.0071  0.0153  0.0093  120 ALA A N   
919   C CA  . ALA A 128 ? 0.1646 0.1890 0.1017 0.0093  0.0156  0.0083  120 ALA A CA  
920   C C   . ALA A 128 ? 0.1931 0.2118 0.1290 0.0118  0.0183  0.0086  120 ALA A C   
921   O O   . ALA A 128 ? 0.1788 0.1907 0.1093 0.0129  0.0185  0.0075  120 ALA A O   
922   C CB  . ALA A 128 ? 0.1795 0.2059 0.1157 0.0112  0.0161  0.0079  120 ALA A CB  
923   N N   . VAL A 129 ? 0.1707 0.1921 0.1120 0.0127  0.0202  0.0103  121 VAL A N   
924   C CA  . VAL A 129 ? 0.1446 0.1629 0.0880 0.0151  0.0230  0.0116  121 VAL A CA  
925   C C   . VAL A 129 ? 0.1896 0.2033 0.1325 0.0146  0.0218  0.0114  121 VAL A C   
926   O O   . VAL A 129 ? 0.1994 0.2072 0.1399 0.0177  0.0242  0.0109  121 VAL A O   
927   C CB  . VAL A 129 ? 0.1641 0.1871 0.1150 0.0148  0.0236  0.0143  121 VAL A CB  
928   C CG1 . VAL A 129 ? 0.1671 0.1888 0.1236 0.0169  0.0258  0.0168  121 VAL A CG1 
929   C CG2 . VAL A 129 ? 0.1554 0.1805 0.1063 0.0158  0.0249  0.0146  121 VAL A CG2 
930   N N   . GLY A 130 ? 0.1604 0.1762 0.1051 0.0110  0.0185  0.0120  122 GLY A N   
931   C CA  . GLY A 130 ? 0.1669 0.1774 0.1106 0.0098  0.0164  0.0122  122 GLY A CA  
932   C C   . GLY A 130 ? 0.1598 0.1629 0.0955 0.0101  0.0153  0.0095  122 GLY A C   
933   O O   . GLY A 130 ? 0.1787 0.1737 0.1117 0.0118  0.0155  0.0088  122 GLY A O   
934   N N   . MET A 131 ? 0.1533 0.1585 0.0851 0.0085  0.0139  0.0081  123 MET A N   
935   C CA  . MET A 131 ? 0.1743 0.1715 0.0975 0.0081  0.0117  0.0059  123 MET A CA  
936   C C   . MET A 131 ? 0.2090 0.1982 0.1253 0.0129  0.0154  0.0039  123 MET A C   
937   O O   . MET A 131 ? 0.2168 0.1953 0.1251 0.0139  0.0147  0.0017  123 MET A O   
938   C CB  . MET A 131 ? 0.2276 0.2298 0.1496 0.0053  0.0087  0.0056  123 MET A CB  
939   C CG  . MET A 131 ? 0.2087 0.2187 0.1367 0.0005  0.0056  0.0076  123 MET A CG  
940   S SD  . MET A 131 ? 0.2116 0.2302 0.1417 -0.0009 0.0037  0.0080  123 MET A SD  
941   C CE  . MET A 131 ? 0.1491 0.1790 0.0881 -0.0047 0.0035  0.0106  123 MET A CE  
942   N N   . ALA A 132 ? 0.1997 0.1931 0.1181 0.0160  0.0195  0.0046  124 ALA A N   
943   C CA  . ALA A 132 ? 0.2390 0.2262 0.1512 0.0206  0.0242  0.0034  124 ALA A CA  
944   C C   . ALA A 132 ? 0.2201 0.2030 0.1354 0.0241  0.0277  0.0038  124 ALA A C   
945   O O   . ALA A 132 ? 0.2317 0.2054 0.1393 0.0279  0.0309  0.0016  124 ALA A O   
946   C CB  . ALA A 132 ? 0.2027 0.1964 0.1179 0.0223  0.0276  0.0051  124 ALA A CB  
947   N N   . LEU A 133 ? 0.2098 0.1989 0.1361 0.0231  0.0271  0.0066  125 LEU A N   
948   C CA  . LEU A 133 ? 0.2347 0.2208 0.1663 0.0262  0.0294  0.0078  125 LEU A CA  
949   C C   . LEU A 133 ? 0.2196 0.1945 0.1446 0.0260  0.0267  0.0053  125 LEU A C   
950   O O   . LEU A 133 ? 0.2219 0.1885 0.1442 0.0308  0.0301  0.0041  125 LEU A O   
951   C CB  . LEU A 133 ? 0.2540 0.2488 0.1980 0.0239  0.0275  0.0118  125 LEU A CB  
952   C CG  . LEU A 133 ? 0.3533 0.3490 0.3072 0.0272  0.0298  0.0149  125 LEU A CG  
953   C CD1 . LEU A 133 ? 0.3170 0.3115 0.2713 0.0333  0.0369  0.0149  125 LEU A CD1 
954   C CD2 . LEU A 133 ? 0.3752 0.3806 0.3392 0.0238  0.0273  0.0190  125 LEU A CD2 
955   N N   . ALA A 134 ? 0.2262 0.2003 0.1484 0.0206  0.0207  0.0048  126 ALA A N   
956   C CA  . ALA A 134 ? 0.2145 0.1770 0.1297 0.0194  0.0170  0.0027  126 ALA A CA  
957   C C   . ALA A 134 ? 0.2498 0.2000 0.1511 0.0226  0.0188  -0.0016 126 ALA A C   
958   O O   . ALA A 134 ? 0.2510 0.1888 0.1464 0.0257  0.0195  -0.0039 126 ALA A O   
959   C CB  . ALA A 134 ? 0.2647 0.2303 0.1799 0.0123  0.0104  0.0037  126 ALA A CB  
960   N N   . GLU A 135 ? 0.2112 0.1637 0.1062 0.0220  0.0193  -0.0029 127 GLU A N   
961   C CA  . GLU A 135 ? 0.2427 0.1830 0.1223 0.0246  0.0207  -0.0069 127 GLU A CA  
962   C C   . GLU A 135 ? 0.2458 0.1805 0.1233 0.0321  0.0288  -0.0081 127 GLU A C   
963   O O   . GLU A 135 ? 0.2733 0.1935 0.1387 0.0354  0.0302  -0.0119 127 GLU A O   
964   C CB  . GLU A 135 ? 0.2245 0.1698 0.0992 0.0227  0.0199  -0.0069 127 GLU A CB  
965   C CG  . GLU A 135 ? 0.2432 0.1749 0.0994 0.0232  0.0186  -0.0108 127 GLU A CG  
966   C CD  . GLU A 135 ? 0.2940 0.2209 0.1418 0.0295  0.0267  -0.0124 127 GLU A CD  
967   O OE1 . GLU A 135 ? 0.3085 0.2227 0.1390 0.0304  0.0264  -0.0158 127 GLU A OE1 
968   O OE2 . GLU A 135 ? 0.3104 0.2461 0.1685 0.0333  0.0332  -0.0099 127 GLU A OE2 
969   N N   . LYS A 136 ? 0.2425 0.1884 0.1317 0.0351  0.0342  -0.0048 128 LYS A N   
970   C CA  . LYS A 136 ? 0.2826 0.2263 0.1730 0.0424  0.0426  -0.0048 128 LYS A CA  
971   C C   . LYS A 136 ? 0.3340 0.2698 0.2277 0.0458  0.0433  -0.0055 128 LYS A C   
972   O O   . LYS A 136 ? 0.2552 0.1800 0.1410 0.0519  0.0486  -0.0084 128 LYS A O   
973   C CB  . LYS A 136 ? 0.2935 0.2522 0.1982 0.0433  0.0467  0.0000  128 LYS A CB  
974   C CG  . LYS A 136 ? 0.3376 0.2984 0.2509 0.0501  0.0547  0.0022  128 LYS A CG  
975   C CD  . LYS A 136 ? 0.3096 0.2860 0.2391 0.0491  0.0562  0.0079  128 LYS A CD  
976   C CE  . LYS A 136 ? 0.3121 0.2929 0.2546 0.0550  0.0628  0.0115  128 LYS A CE  
977   N NZ  . LYS A 136 ? 0.3025 0.2800 0.2382 0.0614  0.0723  0.0104  128 LYS A NZ  
978   N N   . ILE A 137 ? 0.3060 0.2467 0.2109 0.0421  0.0380  -0.0026 129 ILE A N   
979   C CA  . ILE A 137 ? 0.2832 0.2168 0.1926 0.0446  0.0371  -0.0023 129 ILE A CA  
980   C C   . ILE A 137 ? 0.3064 0.2216 0.2001 0.0446  0.0340  -0.0075 129 ILE A C   
981   O O   . ILE A 137 ? 0.2852 0.1886 0.1756 0.0505  0.0372  -0.0097 129 ILE A O   
982   C CB  . ILE A 137 ? 0.2940 0.2365 0.2164 0.0390  0.0309  0.0022  129 ILE A CB  
983   C CG1 . ILE A 137 ? 0.2909 0.2482 0.2288 0.0403  0.0342  0.0073  129 ILE A CG1 
984   C CG2 . ILE A 137 ? 0.4297 0.3621 0.3536 0.0395  0.0273  0.0024  129 ILE A CG2 
985   C CD1 . ILE A 137 ? 0.3589 0.3248 0.3069 0.0342  0.0279  0.0116  129 ILE A CD1 
986   N N   . LEU A 138 ? 0.2561 0.1683 0.1405 0.0380  0.0273  -0.0092 130 LEU A N   
987   C CA  . LEU A 138 ? 0.2799 0.1740 0.1495 0.0366  0.0226  -0.0136 130 LEU A CA  
988   C C   . LEU A 138 ? 0.2983 0.1791 0.1507 0.0423  0.0280  -0.0190 130 LEU A C   
989   O O   . LEU A 138 ? 0.3315 0.1943 0.1724 0.0455  0.0279  -0.0232 130 LEU A O   
990   C CB  . LEU A 138 ? 0.2718 0.1683 0.1381 0.0274  0.0136  -0.0130 130 LEU A CB  
991   C CG  . LEU A 138 ? 0.2685 0.1746 0.1485 0.0215  0.0081  -0.0081 130 LEU A CG  
992   C CD1 . LEU A 138 ? 0.3008 0.2140 0.1803 0.0132  0.0014  -0.0067 130 LEU A CD1 
993   C CD2 . LEU A 138 ? 0.3185 0.2120 0.1984 0.0217  0.0047  -0.0082 130 LEU A CD2 
994   N N   . ALA A 139 ? 0.2900 0.1782 0.1395 0.0437  0.0328  -0.0189 131 ALA A N   
995   C CA  . ALA A 139 ? 0.3094 0.1855 0.1415 0.0493  0.0389  -0.0236 131 ALA A CA  
996   C C   . ALA A 139 ? 0.3976 0.2680 0.2321 0.0589  0.0482  -0.0247 131 ALA A C   
997   O O   . ALA A 139 ? 0.4116 0.2641 0.2297 0.0638  0.0513  -0.0301 131 ALA A O   
998   C CB  . ALA A 139 ? 0.3015 0.1883 0.1319 0.0487  0.0423  -0.0220 131 ALA A CB  
999   N N   . ALA A 140 ? 0.3123 0.1973 0.1669 0.0618  0.0527  -0.0197 132 ALA A N   
1000  C CA  . ALA A 140 ? 0.3381 0.2199 0.1981 0.0713  0.0617  -0.0198 132 ALA A CA  
1001  C C   . ALA A 140 ? 0.3277 0.1933 0.1845 0.0734  0.0582  -0.0228 132 ALA A C   
1002  O O   . ALA A 140 ? 0.3476 0.1999 0.1967 0.0817  0.0648  -0.0266 132 ALA A O   
1003  C CB  . ALA A 140 ? 0.3107 0.2124 0.1946 0.0729  0.0655  -0.0129 132 ALA A CB  
1004  N N   . GLU A 141 ? 0.3528 0.2185 0.2145 0.0660  0.0480  -0.0211 133 GLU A N   
1005  C CA  . GLU A 141 ? 0.3673 0.2180 0.2272 0.0668  0.0433  -0.0228 133 GLU A CA  
1006  C C   . GLU A 141 ? 0.4083 0.2354 0.2438 0.0664  0.0400  -0.0301 133 GLU A C   
1007  O O   . GLU A 141 ? 0.4137 0.2232 0.2417 0.0728  0.0424  -0.0341 133 GLU A O   
1008  C CB  . GLU A 141 ? 0.3167 0.1757 0.1890 0.0582  0.0334  -0.0179 133 GLU A CB  
1009  C CG  . GLU A 141 ? 0.4065 0.2500 0.2773 0.0577  0.0274  -0.0187 133 GLU A CG  
1010  C CD  . GLU A 141 ? 0.4414 0.2947 0.3260 0.0499  0.0190  -0.0127 133 GLU A CD  
1011  O OE1 . GLU A 141 ? 0.4192 0.2903 0.3124 0.0443  0.0175  -0.0087 133 GLU A OE1 
1012  O OE2 . GLU A 141 ? 0.4312 0.2733 0.3172 0.0494  0.0141  -0.0120 133 GLU A OE2 
1013  N N   . PHE A 142 ? 0.3593 0.1850 0.1822 0.0592  0.0344  -0.0319 134 PHE A N   
1014  C CA  . PHE A 142 ? 0.3823 0.1863 0.1838 0.0557  0.0274  -0.0376 134 PHE A CA  
1015  C C   . PHE A 142 ? 0.4038 0.1943 0.1821 0.0597  0.0324  -0.0438 134 PHE A C   
1016  O O   . PHE A 142 ? 0.4410 0.2080 0.1998 0.0610  0.0298  -0.0498 134 PHE A O   
1017  C CB  . PHE A 142 ? 0.3937 0.2037 0.1966 0.0438  0.0157  -0.0348 134 PHE A CB  
1018  C CG  . PHE A 142 ? 0.4468 0.2597 0.2635 0.0387  0.0084  -0.0306 134 PHE A CG  
1019  C CD1 . PHE A 142 ? 0.3821 0.1749 0.1902 0.0373  0.0021  -0.0332 134 PHE A CD1 
1020  C CD2 . PHE A 142 ? 0.4143 0.2488 0.2513 0.0352  0.0078  -0.0239 134 PHE A CD2 
1021  C CE1 . PHE A 142 ? 0.4119 0.2070 0.2323 0.0322  -0.0047 -0.0286 134 PHE A CE1 
1022  C CE2 . PHE A 142 ? 0.3572 0.1940 0.2053 0.0302  0.0013  -0.0197 134 PHE A CE2 
1023  C CZ  . PHE A 142 ? 0.3488 0.1665 0.1891 0.0287  -0.0049 -0.0217 134 PHE A CZ  
1024  N N   . ASN A 143 ? 0.4046 0.2078 0.1832 0.0613  0.0388  -0.0425 135 ASN A N   
1025  C CA  . ASN A 143 ? 0.4161 0.2065 0.1709 0.0642  0.0431  -0.0478 135 ASN A CA  
1026  C C   . ASN A 143 ? 0.5118 0.2861 0.2560 0.0755  0.0536  -0.0530 135 ASN A C   
1027  O O   . ASN A 143 ? 0.4695 0.2526 0.2302 0.0830  0.0620  -0.0504 135 ASN A O   
1028  C CB  . ASN A 143 ? 0.4003 0.2089 0.1597 0.0636  0.0482  -0.0442 135 ASN A CB  
1029  C CG  . ASN A 143 ? 0.3826 0.2031 0.1471 0.0532  0.0381  -0.0406 135 ASN A CG  
1030  O OD1 . ASN A 143 ? 0.4112 0.2255 0.1730 0.0460  0.0274  -0.0410 135 ASN A OD1 
1031  N ND2 . ASN A 143 ? 0.3660 0.2036 0.1383 0.0525  0.0417  -0.0366 135 ASN A ND2 
1032  N N   . LYS A 144 ? 0.5197 0.2753 0.2420 0.0753  0.0517  -0.0585 136 LYS A N   
1033  C CA  . LYS A 144 ? 0.5380 0.2815 0.2551 0.0834  0.0586  -0.0620 136 LYS A CA  
1034  C C   . LYS A 144 ? 0.6860 0.4209 0.3836 0.0826  0.0599  -0.0652 136 LYS A C   
1035  O O   . LYS A 144 ? 0.7616 0.4875 0.4438 0.0746  0.0502  -0.0670 136 LYS A O   
1036  C CB  . LYS A 144 ? 0.5359 0.2589 0.2481 0.0836  0.0519  -0.0658 136 LYS A CB  
1037  C CG  . LYS A 144 ? 0.6288 0.3568 0.3613 0.0901  0.0559  -0.0632 136 LYS A CG  
1038  C CD  . LYS A 144 ? 0.6705 0.3800 0.3997 0.0867  0.0453  -0.0654 136 LYS A CD  
1039  C CE  . LYS A 144 ? 0.7643 0.4777 0.5146 0.0937  0.0492  -0.0621 136 LYS A CE  
1040  N NZ  . LYS A 144 ? 0.7691 0.5129 0.5466 0.0944  0.0547  -0.0539 136 LYS A NZ  
1041  N N   . ASP A 145 ? 0.7563 0.4939 0.4551 0.0907  0.0715  -0.0656 137 ASP A N   
1042  C CA  . ASP A 145 ? 0.8757 0.6068 0.5572 0.0917  0.0754  -0.0682 137 ASP A CA  
1043  C C   . ASP A 145 ? 0.8440 0.5748 0.5123 0.0824  0.0670  -0.0677 137 ASP A C   
1044  O O   . ASP A 145 ? 0.8400 0.5526 0.4877 0.0783  0.0598  -0.0719 137 ASP A O   
1045  C CB  . ASP A 145 ? 0.9708 0.6780 0.6350 0.0959  0.0757  -0.0748 137 ASP A CB  
1046  C CG  . ASP A 145 ? 1.0104 0.6993 0.6666 0.0908  0.0632  -0.0781 137 ASP A CG  
1047  O OD1 . ASP A 145 ? 1.0066 0.6891 0.6706 0.0957  0.0642  -0.0794 137 ASP A OD1 
1048  O OD2 . ASP A 145 ? 1.0220 0.7031 0.6650 0.0817  0.0520  -0.0790 137 ASP A OD2 
1049  N N   . GLY A 146 ? 0.8593 0.6099 0.5396 0.0789  0.0676  -0.0624 138 GLY A N   
1050  C CA  . GLY A 146 ? 0.8447 0.5976 0.5156 0.0708  0.0602  -0.0611 138 GLY A CA  
1051  C C   . GLY A 146 ? 0.7747 0.5216 0.4414 0.0616  0.0460  -0.0614 138 GLY A C   
1052  O O   . GLY A 146 ? 0.8129 0.5652 0.4761 0.0546  0.0393  -0.0592 138 GLY A O   
1053  N N   . LEU A 147 ? 0.7130 0.4493 0.3805 0.0612  0.0407  -0.0637 139 LEU A N   
1054  C CA  . LEU A 147 ? 0.6044 0.3359 0.2695 0.0518  0.0268  -0.0635 139 LEU A CA  
1055  C C   . LEU A 147 ? 0.5703 0.3212 0.2553 0.0501  0.0267  -0.0587 139 LEU A C   
1056  O O   . LEU A 147 ? 0.5200 0.2712 0.2153 0.0527  0.0277  -0.0586 139 LEU A O   
1057  C CB  . LEU A 147 ? 0.6261 0.3360 0.2821 0.0513  0.0205  -0.0679 139 LEU A CB  
1058  C CG  . LEU A 147 ? 0.6647 0.3533 0.2993 0.0531  0.0202  -0.0731 139 LEU A CG  
1059  C CD1 . LEU A 147 ? 0.6540 0.3218 0.2813 0.0517  0.0126  -0.0768 139 LEU A CD1 
1060  C CD2 . LEU A 147 ? 0.7041 0.3904 0.3248 0.0456  0.0129  -0.0726 139 LEU A CD2 
1061  N N   . ASN A 148 ? 0.5011 0.2680 0.1914 0.0458  0.0254  -0.0545 140 ASN A N   
1062  C CA  . ASN A 148 ? 0.5240 0.3112 0.2330 0.0450  0.0270  -0.0496 140 ASN A CA  
1063  C C   . ASN A 148 ? 0.4824 0.2726 0.1956 0.0352  0.0139  -0.0475 140 ASN A C   
1064  O O   . ASN A 148 ? 0.4790 0.2793 0.1941 0.0291  0.0083  -0.0443 140 ASN A O   
1065  C CB  . ASN A 148 ? 0.5711 0.3757 0.2871 0.0461  0.0333  -0.0454 140 ASN A CB  
1066  C CG  . ASN A 148 ? 0.6046 0.4127 0.3249 0.0549  0.0465  -0.0454 140 ASN A CG  
1067  O OD1 . ASN A 148 ? 0.6335 0.4367 0.3581 0.0613  0.0523  -0.0471 140 ASN A OD1 
1068  N ND2 . ASN A 148 ? 0.5978 0.4146 0.3178 0.0553  0.0509  -0.0429 140 ASN A ND2 
1069  N N   . ILE A 149 ? 0.4537 0.2384 0.1738 0.0332  0.0087  -0.0478 141 ILE A N   
1070  C CA  . ILE A 149 ? 0.4773 0.2685 0.2072 0.0231  -0.0035 -0.0441 141 ILE A CA  
1071  C C   . ILE A 149 ? 0.4162 0.2346 0.1720 0.0207  -0.0024 -0.0371 141 ILE A C   
1072  O O   . ILE A 149 ? 0.4194 0.2475 0.1835 0.0127  -0.0110 -0.0333 141 ILE A O   
1073  C CB  . ILE A 149 ? 0.4440 0.2201 0.1724 0.0211  -0.0097 -0.0460 141 ILE A CB  
1074  C CG1 . ILE A 149 ? 0.4139 0.1941 0.1571 0.0284  -0.0016 -0.0451 141 ILE A CG1 
1075  C CG2 . ILE A 149 ? 0.4591 0.2055 0.1585 0.0218  -0.0131 -0.0534 141 ILE A CG2 
1076  C CD1 . ILE A 149 ? 0.4489 0.2226 0.1994 0.0242  -0.0092 -0.0438 141 ILE A CD1 
1077  N N   . VAL A 150 ? 0.3842 0.2152 0.1529 0.0274  0.0077  -0.0351 142 VAL A N   
1078  C CA  . VAL A 150 ? 0.3572 0.2121 0.1473 0.0253  0.0089  -0.0291 142 VAL A CA  
1079  C C   . VAL A 150 ? 0.3751 0.2377 0.1621 0.0287  0.0155  -0.0284 142 VAL A C   
1080  O O   . VAL A 150 ? 0.3863 0.2476 0.1713 0.0361  0.0254  -0.0295 142 VAL A O   
1081  C CB  . VAL A 150 ? 0.3396 0.2041 0.1487 0.0287  0.0136  -0.0261 142 VAL A CB  
1082  C CG1 . VAL A 150 ? 0.3083 0.1956 0.1366 0.0261  0.0141  -0.0205 142 VAL A CG1 
1083  C CG2 . VAL A 150 ? 0.3622 0.2180 0.1735 0.0252  0.0068  -0.0263 142 VAL A CG2 
1084  N N   . ASP A 151 ? 0.3341 0.2050 0.1215 0.0233  0.0102  -0.0261 143 ASP A N   
1085  C CA  . ASP A 151 ? 0.3761 0.2527 0.1590 0.0255  0.0149  -0.0250 143 ASP A CA  
1086  C C   . ASP A 151 ? 0.3535 0.2434 0.1447 0.0192  0.0080  -0.0210 143 ASP A C   
1087  O O   . ASP A 151 ? 0.3260 0.2093 0.1054 0.0149  0.0008  -0.0218 143 ASP A O   
1088  C CB  . ASP A 151 ? 0.4034 0.2608 0.1604 0.0278  0.0162  -0.0300 143 ASP A CB  
1089  C CG  . ASP A 151 ? 0.4805 0.3423 0.2307 0.0301  0.0215  -0.0285 143 ASP A CG  
1090  O OD1 . ASP A 151 ? 0.3863 0.2655 0.1526 0.0307  0.0249  -0.0239 143 ASP A OD1 
1091  O OD2 . ASP A 151 ? 0.4508 0.3021 0.1869 0.0301  0.0212  -0.0309 143 ASP A OD2 
1092  N N   . HIS A 152 ? 0.2825 0.1904 0.0936 0.0188  0.0097  -0.0167 144 HIS A N   
1093  C CA  . HIS A 152 ? 0.3614 0.2819 0.1810 0.0141  0.0043  -0.0131 144 HIS A CA  
1094  C C   . HIS A 152 ? 0.3090 0.2453 0.1441 0.0168  0.0101  -0.0096 144 HIS A C   
1095  O O   . HIS A 152 ? 0.3018 0.2410 0.1439 0.0209  0.0169  -0.0093 144 HIS A O   
1096  C CB  . HIS A 152 ? 0.2729 0.1972 0.1006 0.0077  -0.0045 -0.0117 144 HIS A CB  
1097  C CG  . HIS A 152 ? 0.3133 0.2428 0.1542 0.0077  -0.0028 -0.0107 144 HIS A CG  
1098  N ND1 . HIS A 152 ? 0.3144 0.2327 0.1510 0.0066  -0.0054 -0.0127 144 HIS A ND1 
1099  C CD2 . HIS A 152 ? 0.2659 0.2098 0.1234 0.0084  0.0005  -0.0076 144 HIS A CD2 
1100  C CE1 . HIS A 152 ? 0.2961 0.2223 0.1465 0.0065  -0.0037 -0.0105 144 HIS A CE1 
1101  N NE2 . HIS A 152 ? 0.2867 0.2283 0.1494 0.0075  -0.0002 -0.0075 144 HIS A NE2 
1102  N N   . TYR A 153 ? 0.2971 0.2433 0.1380 0.0144  0.0070  -0.0068 145 TYR A N   
1103  C CA  . TYR A 153 ? 0.2704 0.2296 0.1238 0.0164  0.0113  -0.0037 145 TYR A CA  
1104  C C   . TYR A 153 ? 0.2711 0.2428 0.1409 0.0135  0.0084  -0.0014 145 TYR A C   
1105  O O   . TYR A 153 ? 0.2837 0.2562 0.1557 0.0093  0.0025  -0.0014 145 TYR A O   
1106  C CB  . TYR A 153 ? 0.3272 0.2876 0.1751 0.0165  0.0105  -0.0021 145 TYR A CB  
1107  C CG  . TYR A 153 ? 0.3394 0.2898 0.1723 0.0201  0.0159  -0.0035 145 TYR A CG  
1108  C CD1 . TYR A 153 ? 0.4734 0.4091 0.2877 0.0196  0.0137  -0.0068 145 TYR A CD1 
1109  C CD2 . TYR A 153 ? 0.3260 0.2812 0.1629 0.0239  0.0235  -0.0015 145 TYR A CD2 
1110  C CE1 . TYR A 153 ? 0.5795 0.5055 0.3784 0.0233  0.0197  -0.0083 145 TYR A CE1 
1111  C CE2 . TYR A 153 ? 0.3940 0.3410 0.2175 0.0274  0.0297  -0.0023 145 TYR A CE2 
1112  C CZ  . TYR A 153 ? 0.5813 0.5138 0.3854 0.0274  0.0282  -0.0059 145 TYR A CZ  
1113  O OH  . TYR A 153 ? 0.6933 0.6199 0.4887 0.0301  0.0342  -0.0068 145 TYR A OH  
1114  N N   . THR A 154 ? 0.2002 0.1814 0.0810 0.0155  0.0128  0.0006  146 THR A N   
1115  C CA  . THR A 154 ? 0.1982 0.1908 0.0928 0.0135  0.0112  0.0025  146 THR A CA  
1116  C C   . THR A 154 ? 0.2000 0.1998 0.0992 0.0146  0.0118  0.0045  146 THR A C   
1117  O O   . THR A 154 ? 0.2292 0.2299 0.1297 0.0174  0.0164  0.0055  146 THR A O   
1118  C CB  . THR A 154 ? 0.1957 0.1912 0.0983 0.0147  0.0150  0.0030  146 THR A CB  
1119  O OG1 . THR A 154 ? 0.2347 0.2218 0.1325 0.0145  0.0146  0.0013  146 THR A OG1 
1120  C CG2 . THR A 154 ? 0.2030 0.2087 0.1169 0.0122  0.0132  0.0046  146 THR A CG2 
1121  N N   . TYR A 155 ? 0.1717 0.1765 0.0741 0.0124  0.0070  0.0055  147 TYR A N   
1122  C CA  . TYR A 155 ? 0.1671 0.1776 0.0739 0.0137  0.0069  0.0073  147 TYR A CA  
1123  C C   . TYR A 155 ? 0.1635 0.1841 0.0829 0.0134  0.0073  0.0081  147 TYR A C   
1124  O O   . TYR A 155 ? 0.2147 0.2396 0.1389 0.0110  0.0053  0.0080  147 TYR A O   
1125  C CB  . TYR A 155 ? 0.1846 0.1938 0.0868 0.0122  0.0013  0.0083  147 TYR A CB  
1126  C CG  . TYR A 155 ? 0.2129 0.2107 0.0998 0.0123  0.0004  0.0074  147 TYR A CG  
1127  C CD1 . TYR A 155 ? 0.2223 0.2163 0.1025 0.0149  0.0036  0.0083  147 TYR A CD1 
1128  C CD2 . TYR A 155 ? 0.2318 0.2222 0.1099 0.0094  -0.0038 0.0057  147 TYR A CD2 
1129  C CE1 . TYR A 155 ? 0.2093 0.1926 0.0737 0.0150  0.0034  0.0074  147 TYR A CE1 
1130  C CE2 . TYR A 155 ? 0.3201 0.2984 0.1817 0.0095  -0.0047 0.0043  147 TYR A CE2 
1131  C CZ  . TYR A 155 ? 0.3011 0.2760 0.1553 0.0125  -0.0007 0.0051  147 TYR A CZ  
1132  O OH  . TYR A 155 ? 0.2876 0.2500 0.1234 0.0127  -0.0009 0.0037  147 TYR A OH  
1133  N N   . VAL A 156 ? 0.1549 0.1785 0.0787 0.0158  0.0100  0.0090  148 VAL A N   
1134  C CA  . VAL A 156 ? 0.1419 0.1729 0.0751 0.0161  0.0109  0.0091  148 VAL A CA  
1135  C C   . VAL A 156 ? 0.1801 0.2136 0.1165 0.0183  0.0101  0.0102  148 VAL A C   
1136  O O   . VAL A 156 ? 0.2175 0.2467 0.1501 0.0199  0.0107  0.0113  148 VAL A O   
1137  C CB  . VAL A 156 ? 0.1374 0.1680 0.0729 0.0166  0.0147  0.0088  148 VAL A CB  
1138  C CG1 . VAL A 156 ? 0.1519 0.1887 0.0942 0.0161  0.0152  0.0083  148 VAL A CG1 
1139  C CG2 . VAL A 156 ? 0.1734 0.1999 0.1054 0.0154  0.0158  0.0083  148 VAL A CG2 
1140  N N   . PHE A 157 ? 0.1637 0.2042 0.1076 0.0187  0.0090  0.0102  149 PHE A N   
1141  C CA  . PHE A 157 ? 0.1716 0.2142 0.1201 0.0217  0.0092  0.0106  149 PHE A CA  
1142  C C   . PHE A 157 ? 0.1826 0.2266 0.1344 0.0225  0.0126  0.0090  149 PHE A C   
1143  O O   . PHE A 157 ? 0.2024 0.2508 0.1567 0.0210  0.0138  0.0080  149 PHE A O   
1144  C CB  . PHE A 157 ? 0.1722 0.2217 0.1275 0.0226  0.0062  0.0117  149 PHE A CB  
1145  C CG  . PHE A 157 ? 0.1890 0.2364 0.1411 0.0219  0.0014  0.0139  149 PHE A CG  
1146  C CD1 . PHE A 157 ? 0.1650 0.2039 0.1066 0.0207  0.0007  0.0142  149 PHE A CD1 
1147  C CD2 . PHE A 157 ? 0.1985 0.2524 0.1580 0.0226  -0.0023 0.0159  149 PHE A CD2 
1148  C CE1 . PHE A 157 ? 0.1861 0.2217 0.1223 0.0197  -0.0041 0.0161  149 PHE A CE1 
1149  C CE2 . PHE A 157 ? 0.2236 0.2751 0.1796 0.0215  -0.0079 0.0184  149 PHE A CE2 
1150  C CZ  . PHE A 157 ? 0.1843 0.2259 0.1275 0.0198  -0.0090 0.0183  149 PHE A CZ  
1151  N N   . MET A 158 ? 0.1738 0.2135 0.1248 0.0244  0.0137  0.0090  150 MET A N   
1152  C CA  . MET A 158 ? 0.1619 0.2013 0.1144 0.0248  0.0160  0.0072  150 MET A CA  
1153  C C   . MET A 158 ? 0.1963 0.2322 0.1500 0.0280  0.0157  0.0069  150 MET A C   
1154  O O   . MET A 158 ? 0.1925 0.2257 0.1460 0.0295  0.0138  0.0087  150 MET A O   
1155  C CB  . MET A 158 ? 0.3404 0.3762 0.2898 0.0223  0.0173  0.0075  150 MET A CB  
1156  C CG  . MET A 158 ? 0.3242 0.3546 0.2712 0.0221  0.0175  0.0095  150 MET A CG  
1157  S SD  . MET A 158 ? 0.2775 0.3068 0.2241 0.0194  0.0192  0.0104  150 MET A SD  
1158  C CE  . MET A 158 ? 0.2214 0.2511 0.1695 0.0181  0.0188  0.0087  150 MET A CE  
1159  N N   . GLY A 159 ? 0.1856 0.2209 0.1400 0.0291  0.0173  0.0046  151 GLY A N   
1160  C CA  . GLY A 159 ? 0.1965 0.2269 0.1514 0.0325  0.0170  0.0035  151 GLY A CA  
1161  C C   . GLY A 159 ? 0.2162 0.2391 0.1667 0.0311  0.0172  0.0023  151 GLY A C   
1162  O O   . GLY A 159 ? 0.2049 0.2272 0.1532 0.0274  0.0173  0.0030  151 GLY A O   
1163  N N   . ASP A 160 ? 0.2112 0.2277 0.1608 0.0340  0.0167  0.0006  152 ASP A N   
1164  C CA  . ASP A 160 ? 0.2148 0.2221 0.1596 0.0321  0.0154  -0.0003 152 ASP A CA  
1165  C C   . ASP A 160 ? 0.2192 0.2266 0.1596 0.0298  0.0169  -0.0030 152 ASP A C   
1166  O O   . ASP A 160 ? 0.2225 0.2250 0.1596 0.0260  0.0150  -0.0022 152 ASP A O   
1167  C CB  . ASP A 160 ? 0.2931 0.2918 0.2367 0.0360  0.0141  -0.0021 152 ASP A CB  
1168  C CG  . ASP A 160 ? 0.3312 0.3264 0.2775 0.0367  0.0112  0.0017  152 ASP A CG  
1169  O OD1 . ASP A 160 ? 0.3615 0.3568 0.3077 0.0329  0.0099  0.0055  152 ASP A OD1 
1170  O OD2 . ASP A 160 ? 0.4288 0.4213 0.3772 0.0412  0.0105  0.0011  152 ASP A OD2 
1171  N N   . GLY A 161 ? 0.1848 0.1978 0.1253 0.0319  0.0201  -0.0057 153 GLY A N   
1172  C CA  . GLY A 161 ? 0.2044 0.2175 0.1394 0.0295  0.0217  -0.0079 153 GLY A CA  
1173  C C   . GLY A 161 ? 0.1917 0.2085 0.1273 0.0243  0.0204  -0.0049 153 GLY A C   
1174  O O   . GLY A 161 ? 0.2025 0.2151 0.1334 0.0207  0.0189  -0.0049 153 GLY A O   
1175  N N   . OCS A 162 ? 0.1727 0.1966 0.1139 0.0240  0.0207  -0.0024 154 OCS A N   
1176  C CA  . OCS A 162 ? 0.1637 0.1905 0.1060 0.0201  0.0198  0.0003  154 OCS A CA  
1177  C CB  . OCS A 162 ? 0.1823 0.2146 0.1290 0.0208  0.0200  0.0022  154 OCS A CB  
1178  S SG  . OCS A 162 ? 0.2306 0.2718 0.1804 0.0222  0.0219  0.0011  154 OCS A SG  
1179  C C   . OCS A 162 ? 0.1424 0.1634 0.0841 0.0177  0.0174  0.0026  154 OCS A C   
1180  O O   . OCS A 162 ? 0.1598 0.1806 0.1010 0.0143  0.0164  0.0039  154 OCS A O   
1181  O OD1 . OCS A 162 ? 0.2201 0.2638 0.1730 0.0230  0.0204  0.0030  154 OCS A OD1 
1182  O OD2 . OCS A 162 ? 0.2090 0.2535 0.1576 0.0188  0.0225  0.0015  154 OCS A OD2 
1183  O OD3 . OCS A 162 ? 0.4812 0.5227 0.4313 0.0257  0.0237  -0.0013 154 OCS A OD3 
1184  N N   . LEU A 163 ? 0.1522 0.1689 0.0951 0.0192  0.0162  0.0036  155 LEU A N   
1185  C CA  . LEU A 163 ? 0.1708 0.1833 0.1149 0.0167  0.0141  0.0068  155 LEU A CA  
1186  C C   . LEU A 163 ? 0.1969 0.2027 0.1376 0.0140  0.0114  0.0062  155 LEU A C   
1187  O O   . LEU A 163 ? 0.2177 0.2225 0.1609 0.0106  0.0093  0.0095  155 LEU A O   
1188  C CB  . LEU A 163 ? 0.1476 0.1572 0.0933 0.0187  0.0134  0.0087  155 LEU A CB  
1189  C CG  . LEU A 163 ? 0.2403 0.2552 0.1880 0.0202  0.0152  0.0104  155 LEU A CG  
1190  C CD1 . LEU A 163 ? 0.2511 0.2625 0.1989 0.0223  0.0141  0.0120  155 LEU A CD1 
1191  C CD2 . LEU A 163 ? 0.2091 0.2267 0.1587 0.0178  0.0163  0.0135  155 LEU A CD2 
1192  N N   . MET A 164 ? 0.2009 0.2020 0.1358 0.0155  0.0113  0.0021  156 MET A N   
1193  C CA  . MET A 164 ? 0.2207 0.2135 0.1497 0.0125  0.0081  0.0009  156 MET A CA  
1194  C C   . MET A 164 ? 0.1973 0.1931 0.1243 0.0086  0.0075  0.0015  156 MET A C   
1195  O O   . MET A 164 ? 0.1762 0.1671 0.1013 0.0044  0.0035  0.0031  156 MET A O   
1196  C CB  . MET A 164 ? 0.2095 0.1948 0.1308 0.0157  0.0088  -0.0043 156 MET A CB  
1197  C CG  . MET A 164 ? 0.2374 0.2143 0.1588 0.0181  0.0068  -0.0046 156 MET A CG  
1198  S SD  . MET A 164 ? 0.2612 0.2282 0.1736 0.0234  0.0084  -0.0113 156 MET A SD  
1199  C CE  . MET A 164 ? 0.2892 0.2667 0.2097 0.0300  0.0133  -0.0117 156 MET A CE  
1200  N N   . GLU A 165 ? 0.1648 0.1686 0.0929 0.0096  0.0108  0.0008  157 GLU A N   
1201  C CA  . GLU A 165 ? 0.1603 0.1666 0.0862 0.0060  0.0102  0.0016  157 GLU A CA  
1202  C C   . GLU A 165 ? 0.1549 0.1633 0.0873 0.0026  0.0074  0.0066  157 GLU A C   
1203  O O   . GLU A 165 ? 0.1636 0.1762 0.1034 0.0039  0.0086  0.0093  157 GLU A O   
1204  C CB  . GLU A 165 ? 0.1799 0.1944 0.1067 0.0077  0.0141  0.0005  157 GLU A CB  
1205  C CG  . GLU A 165 ? 0.1617 0.1758 0.0824 0.0106  0.0174  -0.0039 157 GLU A CG  
1206  C CD  . GLU A 165 ? 0.1821 0.1912 0.0924 0.0080  0.0169  -0.0059 157 GLU A CD  
1207  O OE1 . GLU A 165 ? 0.1754 0.1808 0.0832 0.0034  0.0129  -0.0037 157 GLU A OE1 
1208  O OE2 . GLU A 165 ? 0.1904 0.1995 0.0950 0.0107  0.0208  -0.0096 157 GLU A OE2 
1209  N N   . GLY A 166 ? 0.1595 0.1651 0.0889 -0.0017 0.0038  0.0080  158 GLY A N   
1210  C CA  . GLY A 166 ? 0.1552 0.1635 0.0924 -0.0048 0.0010  0.0132  158 GLY A CA  
1211  C C   . GLY A 166 ? 0.1783 0.1944 0.1222 -0.0035 0.0039  0.0153  158 GLY A C   
1212  O O   . GLY A 166 ? 0.1409 0.1602 0.0934 -0.0035 0.0038  0.0192  158 GLY A O   
1213  N N   . VAL A 167 ? 0.1490 0.1682 0.0891 -0.0022 0.0067  0.0127  159 VAL A N   
1214  C CA  . VAL A 167 ? 0.1797 0.2045 0.1251 -0.0015 0.0085  0.0145  159 VAL A CA  
1215  C C   . VAL A 167 ? 0.1542 0.1813 0.1049 0.0021  0.0114  0.0149  159 VAL A C   
1216  O O   . VAL A 167 ? 0.1719 0.2014 0.1274 0.0029  0.0125  0.0170  159 VAL A O   
1217  C CB  . VAL A 167 ? 0.2504 0.2777 0.1907 -0.0019 0.0102  0.0123  159 VAL A CB  
1218  C CG1 . VAL A 167 ? 0.1649 0.1937 0.1022 0.0013  0.0135  0.0085  159 VAL A CG1 
1219  C CG2 . VAL A 167 ? 0.1732 0.2042 0.1181 -0.0022 0.0107  0.0144  159 VAL A CG2 
1220  N N   . SER A 168 ? 0.1328 0.1582 0.0819 0.0044  0.0126  0.0129  160 SER A N   
1221  C CA  . SER A 168 ? 0.1796 0.2063 0.1321 0.0073  0.0148  0.0139  160 SER A CA  
1222  C C   . SER A 168 ? 0.1564 0.1826 0.1149 0.0066  0.0143  0.0180  160 SER A C   
1223  O O   . SER A 168 ? 0.1677 0.1961 0.1295 0.0084  0.0168  0.0198  160 SER A O   
1224  C CB  . SER A 168 ? 0.1829 0.2076 0.1326 0.0098  0.0155  0.0114  160 SER A CB  
1225  O OG  . SER A 168 ? 0.1687 0.1884 0.1182 0.0090  0.0134  0.0123  160 SER A OG  
1226  N N   . HIS A 169 ? 0.1327 0.1561 0.0923 0.0038  0.0110  0.0197  161 HIS A N   
1227  C CA  . HIS A 169 ? 0.1324 0.1570 0.0999 0.0023  0.0100  0.0247  161 HIS A CA  
1228  C C   . HIS A 169 ? 0.1317 0.1610 0.1055 0.0024  0.0111  0.0276  161 HIS A C   
1229  O O   . HIS A 169 ? 0.1444 0.1769 0.1244 0.0044  0.0143  0.0305  161 HIS A O   
1230  C CB  . HIS A 169 ? 0.1383 0.1585 0.1054 -0.0018 0.0048  0.0261  161 HIS A CB  
1231  C CG  . HIS A 169 ? 0.1380 0.1611 0.1152 -0.0045 0.0025  0.0323  161 HIS A CG  
1232  N ND1 . HIS A 169 ? 0.1368 0.1626 0.1217 -0.0038 0.0044  0.0365  161 HIS A ND1 
1233  C CD2 . HIS A 169 ? 0.1393 0.1636 0.1210 -0.0080 -0.0016 0.0356  161 HIS A CD2 
1234  C CE1 . HIS A 169 ? 0.1367 0.1664 0.1319 -0.0066 0.0020  0.0423  161 HIS A CE1 
1235  N NE2 . HIS A 169 ? 0.1703 0.1990 0.1640 -0.0092 -0.0021 0.0419  161 HIS A NE2 
1236  N N   . GLU A 170 ? 0.1291 0.1583 0.1007 0.0004  0.0089  0.0267  162 GLU A N   
1237  C CA  . GLU A 170 ? 0.1268 0.1592 0.1043 0.0007  0.0093  0.0294  162 GLU A CA  
1238  C C   . GLU A 170 ? 0.1308 0.1647 0.1082 0.0048  0.0142  0.0279  162 GLU A C   
1239  O O   . GLU A 170 ? 0.1375 0.1736 0.1217 0.0070  0.0167  0.0307  162 GLU A O   
1240  C CB  . GLU A 170 ? 0.1291 0.1601 0.1020 -0.0024 0.0057  0.0286  162 GLU A CB  
1241  C CG  . GLU A 170 ? 0.1347 0.1625 0.1051 -0.0070 0.0002  0.0298  162 GLU A CG  
1242  C CD  . GLU A 170 ? 0.1467 0.1727 0.1109 -0.0104 -0.0031 0.0293  162 GLU A CD  
1243  O OE1 . GLU A 170 ? 0.1812 0.2026 0.1384 -0.0139 -0.0071 0.0286  162 GLU A OE1 
1244  O OE2 . GLU A 170 ? 0.1400 0.1681 0.1053 -0.0097 -0.0020 0.0298  162 GLU A OE2 
1245  N N   . ALA A 171 ? 0.1238 0.1562 0.0934 0.0059  0.0156  0.0237  163 ALA A N   
1246  C CA  . ALA A 171 ? 0.1675 0.1999 0.1355 0.0089  0.0189  0.0222  163 ALA A CA  
1247  C C   . ALA A 171 ? 0.1585 0.1909 0.1280 0.0121  0.0226  0.0231  163 ALA A C   
1248  O O   . ALA A 171 ? 0.1502 0.1821 0.1210 0.0148  0.0257  0.0238  163 ALA A O   
1249  C CB  . ALA A 171 ? 0.1731 0.2049 0.1339 0.0087  0.0186  0.0182  163 ALA A CB  
1250  N N   . CYS A 172 ? 0.1525 0.1846 0.1208 0.0120  0.0226  0.0231  164 CYS A N   
1251  C CA  . CYS A 172 ? 0.1568 0.1887 0.1251 0.0146  0.0261  0.0245  164 CYS A CA  
1252  C C   . CYS A 172 ? 0.1585 0.1933 0.1358 0.0149  0.0282  0.0295  164 CYS A C   
1253  O O   . CYS A 172 ? 0.1578 0.1933 0.1357 0.0179  0.0329  0.0309  164 CYS A O   
1254  C CB  . CYS A 172 ? 0.1570 0.1872 0.1218 0.0142  0.0249  0.0236  164 CYS A CB  
1255  S SG  . CYS A 172 ? 0.1700 0.1985 0.1267 0.0149  0.0235  0.0187  164 CYS A SG  
1256  N N   . SER A 173 ? 0.1300 0.1668 0.1143 0.0119  0.0248  0.0324  165 SER A N   
1257  C CA  . SER A 173 ? 0.1704 0.2117 0.1658 0.0121  0.0263  0.0380  165 SER A CA  
1258  C C   . SER A 173 ? 0.1721 0.2149 0.1706 0.0157  0.0302  0.0383  165 SER A C   
1259  O O   . SER A 173 ? 0.1634 0.2088 0.1665 0.0190  0.0356  0.0409  165 SER A O   
1260  C CB  . SER A 173 ? 0.1320 0.1745 0.1337 0.0075  0.0203  0.0410  165 SER A CB  
1261  O OG  . SER A 173 ? 0.1589 0.2072 0.1738 0.0073  0.0210  0.0474  165 SER A OG  
1262  N N   . LEU A 174 ? 0.1358 0.1763 0.1313 0.0152  0.0277  0.0357  166 LEU A N   
1263  C CA  . LEU A 174 ? 0.1725 0.2124 0.1702 0.0187  0.0306  0.0357  166 LEU A CA  
1264  C C   . LEU A 174 ? 0.1624 0.1984 0.1516 0.0229  0.0361  0.0322  166 LEU A C   
1265  O O   . LEU A 174 ? 0.1809 0.2164 0.1726 0.0272  0.0410  0.0331  166 LEU A O   
1266  C CB  . LEU A 174 ? 0.1741 0.2114 0.1691 0.0164  0.0261  0.0338  166 LEU A CB  
1267  C CG  . LEU A 174 ? 0.1593 0.1944 0.1569 0.0197  0.0280  0.0340  166 LEU A CG  
1268  C CD1 . LEU A 174 ? 0.1374 0.1773 0.1489 0.0222  0.0301  0.0396  166 LEU A CD1 
1269  C CD2 . LEU A 174 ? 0.1853 0.2177 0.1800 0.0165  0.0228  0.0330  166 LEU A CD2 
1270  N N   . ALA A 175 ? 0.1361 0.1687 0.1149 0.0219  0.0351  0.0283  167 ALA A N   
1271  C CA  . ALA A 175 ? 0.1926 0.2207 0.1620 0.0251  0.0391  0.0253  167 ALA A CA  
1272  C C   . ALA A 175 ? 0.2282 0.2582 0.1996 0.0281  0.0449  0.0282  167 ALA A C   
1273  O O   . ALA A 175 ? 0.2121 0.2384 0.1781 0.0321  0.0500  0.0270  167 ALA A O   
1274  C CB  . ALA A 175 ? 0.1756 0.2012 0.1356 0.0231  0.0360  0.0217  167 ALA A CB  
1275  N N   . GLY A 176 ? 0.1692 0.2043 0.1479 0.0261  0.0443  0.0322  168 GLY A N   
1276  C CA  . GLY A 176 ? 0.1614 0.1996 0.1436 0.0282  0.0500  0.0362  168 GLY A CA  
1277  C C   . GLY A 176 ? 0.1603 0.2022 0.1518 0.0320  0.0554  0.0394  168 GLY A C   
1278  O O   . GLY A 176 ? 0.1538 0.1952 0.1426 0.0363  0.0626  0.0400  168 GLY A O   
1279  N N   . THR A 177 ? 0.1399 0.1856 0.1427 0.0307  0.0521  0.0418  169 THR A N   
1280  C CA  A THR A 177 ? 0.1774 0.2275 0.1918 0.0346  0.0565  0.0455  169 THR A CA  
1281  C CA  B THR A 177 ? 0.1811 0.2313 0.1953 0.0348  0.0570  0.0456  169 THR A CA  
1282  C C   . THR A 177 ? 0.2175 0.2606 0.2234 0.0402  0.0614  0.0411  169 THR A C   
1283  O O   . THR A 177 ? 0.1749 0.2196 0.1850 0.0457  0.0690  0.0428  169 THR A O   
1284  C CB  A THR A 177 ? 0.1729 0.2270 0.1994 0.0314  0.0501  0.0488  169 THR A CB  
1285  C CB  B THR A 177 ? 0.1783 0.2339 0.2068 0.0318  0.0512  0.0499  169 THR A CB  
1286  O OG1 A THR A 177 ? 0.1316 0.1914 0.1662 0.0264  0.0459  0.0535  169 THR A OG1 
1287  O OG1 B THR A 177 ? 0.1802 0.2420 0.2229 0.0360  0.0562  0.0549  169 THR A OG1 
1288  C CG2 A THR A 177 ? 0.1750 0.2332 0.2144 0.0360  0.0539  0.0525  169 THR A CG2 
1289  C CG2 B THR A 177 ? 0.1587 0.2086 0.1815 0.0300  0.0454  0.0458  169 THR A CG2 
1290  N N   . LEU A 178 ? 0.1535 0.1887 0.1476 0.0389  0.0574  0.0353  170 LEU A N   
1291  C CA  . LEU A 178 ? 0.2120 0.2384 0.1969 0.0433  0.0604  0.0308  170 LEU A CA  
1292  C C   . LEU A 178 ? 0.1830 0.2026 0.1520 0.0457  0.0649  0.0268  170 LEU A C   
1293  O O   . LEU A 178 ? 0.2466 0.2568 0.2051 0.0489  0.0668  0.0224  170 LEU A O   
1294  C CB  . LEU A 178 ? 0.2054 0.2266 0.1861 0.0402  0.0533  0.0274  170 LEU A CB  
1295  C CG  . LEU A 178 ? 0.2224 0.2482 0.2169 0.0388  0.0494  0.0313  170 LEU A CG  
1296  C CD1 . LEU A 178 ? 0.2368 0.2574 0.2257 0.0352  0.0428  0.0284  170 LEU A CD1 
1297  C CD2 . LEU A 178 ? 0.2073 0.2337 0.2114 0.0450  0.0548  0.0340  170 LEU A CD2 
1298  N N   . GLY A 179 ? 0.1735 0.1964 0.1400 0.0440  0.0661  0.0285  171 GLY A N   
1299  C CA  . GLY A 179 ? 0.2207 0.2376 0.1724 0.0460  0.0704  0.0259  171 GLY A CA  
1300  C C   . GLY A 179 ? 0.2643 0.2707 0.1997 0.0448  0.0662  0.0197  171 GLY A C   
1301  O O   . GLY A 179 ? 0.2194 0.2169 0.1420 0.0483  0.0701  0.0162  171 GLY A O   
1302  N N   . LEU A 180 ? 0.2089 0.2160 0.1443 0.0399  0.0584  0.0183  172 LEU A N   
1303  C CA  . LEU A 180 ? 0.1871 0.1863 0.1104 0.0380  0.0534  0.0134  172 LEU A CA  
1304  C C   . LEU A 180 ? 0.1861 0.1817 0.0970 0.0371  0.0529  0.0121  172 LEU A C   
1305  O O   . LEU A 180 ? 0.1961 0.1946 0.1071 0.0335  0.0479  0.0123  172 LEU A O   
1306  C CB  . LEU A 180 ? 0.1690 0.1720 0.0987 0.0333  0.0462  0.0132  172 LEU A CB  
1307  C CG  . LEU A 180 ? 0.1922 0.1981 0.1330 0.0333  0.0453  0.0148  172 LEU A CG  
1308  C CD1 . LEU A 180 ? 0.1641 0.1726 0.1074 0.0284  0.0384  0.0142  172 LEU A CD1 
1309  C CD2 . LEU A 180 ? 0.2016 0.1996 0.1388 0.0372  0.0479  0.0128  172 LEU A CD2 
1310  N N   . GLY A 181 ? 0.2262 0.2149 0.1258 0.0407  0.0584  0.0108  173 GLY A N   
1311  C CA  . GLY A 181 ? 0.2564 0.2412 0.1431 0.0400  0.0584  0.0105  173 GLY A CA  
1312  C C   . GLY A 181 ? 0.2964 0.2747 0.1721 0.0366  0.0509  0.0069  173 GLY A C   
1313  O O   . GLY A 181 ? 0.3060 0.2827 0.1736 0.0350  0.0489  0.0075  173 GLY A O   
1314  N N   . LYS A 182 ? 0.2333 0.2081 0.1093 0.0351  0.0464  0.0040  174 LYS A N   
1315  C CA  . LYS A 182 ? 0.2317 0.2021 0.0997 0.0312  0.0387  0.0016  174 LYS A CA  
1316  C C   . LYS A 182 ? 0.2274 0.2076 0.1074 0.0272  0.0329  0.0033  174 LYS A C   
1317  O O   . LYS A 182 ? 0.2323 0.2115 0.1094 0.0239  0.0266  0.0022  174 LYS A O   
1318  C CB  . LYS A 182 ? 0.2922 0.2521 0.1521 0.0312  0.0365  -0.0024 174 LYS A CB  
1319  C CG  . LYS A 182 ? 0.3646 0.3126 0.2098 0.0358  0.0427  -0.0051 174 LYS A CG  
1320  C CD  . LYS A 182 ? 0.4646 0.4005 0.3022 0.0362  0.0405  -0.0092 174 LYS A CD  
1321  C CE  . LYS A 182 ? 0.4291 0.3492 0.2443 0.0375  0.0409  -0.0133 174 LYS A CE  
1322  N NZ  . LYS A 182 ? 0.4197 0.3263 0.2268 0.0372  0.0372  -0.0176 174 LYS A NZ  
1323  N N   . LEU A 183 ? 0.2277 0.2172 0.1210 0.0276  0.0351  0.0062  175 LEU A N   
1324  C CA  . LEU A 183 ? 0.1891 0.1870 0.0921 0.0246  0.0309  0.0076  175 LEU A CA  
1325  C C   . LEU A 183 ? 0.2143 0.2148 0.1164 0.0246  0.0307  0.0097  175 LEU A C   
1326  O O   . LEU A 183 ? 0.2447 0.2464 0.1484 0.0264  0.0351  0.0122  175 LEU A O   
1327  C CB  . LEU A 183 ? 0.1895 0.1939 0.1051 0.0246  0.0324  0.0095  175 LEU A CB  
1328  C CG  . LEU A 183 ? 0.2030 0.2148 0.1270 0.0220  0.0291  0.0106  175 LEU A CG  
1329  C CD1 . LEU A 183 ? 0.1677 0.1804 0.0912 0.0192  0.0243  0.0086  175 LEU A CD1 
1330  C CD2 . LEU A 183 ? 0.2002 0.2166 0.1343 0.0218  0.0306  0.0127  175 LEU A CD2 
1331  N N   . ILE A 184 ? 0.1869 0.1886 0.0876 0.0226  0.0255  0.0093  176 ILE A N   
1332  C CA  . ILE A 184 ? 0.2014 0.2040 0.1002 0.0227  0.0243  0.0113  176 ILE A CA  
1333  C C   . ILE A 184 ? 0.2454 0.2548 0.1535 0.0213  0.0203  0.0118  176 ILE A C   
1334  O O   . ILE A 184 ? 0.2353 0.2465 0.1446 0.0196  0.0161  0.0104  176 ILE A O   
1335  C CB  . ILE A 184 ? 0.1863 0.1815 0.0715 0.0224  0.0219  0.0107  176 ILE A CB  
1336  C CG1 . ILE A 184 ? 0.2833 0.2709 0.1577 0.0247  0.0276  0.0100  176 ILE A CG1 
1337  C CG2 . ILE A 184 ? 0.2356 0.2322 0.1202 0.0222  0.0193  0.0133  176 ILE A CG2 
1338  C CD1 . ILE A 184 ? 0.3417 0.3195 0.1991 0.0241  0.0253  0.0087  176 ILE A CD1 
1339  N N   . VAL A 185 ? 0.1665 0.1794 0.0812 0.0221  0.0216  0.0137  177 VAL A N   
1340  C CA  . VAL A 185 ? 0.1547 0.1729 0.0777 0.0216  0.0190  0.0137  177 VAL A CA  
1341  C C   . VAL A 185 ? 0.1786 0.1961 0.1006 0.0226  0.0166  0.0155  177 VAL A C   
1342  O O   . VAL A 185 ? 0.2011 0.2155 0.1202 0.0233  0.0183  0.0179  177 VAL A O   
1343  C CB  . VAL A 185 ? 0.1766 0.1975 0.1069 0.0215  0.0213  0.0142  177 VAL A CB  
1344  C CG1 . VAL A 185 ? 0.2372 0.2611 0.1733 0.0217  0.0191  0.0136  177 VAL A CG1 
1345  C CG2 . VAL A 185 ? 0.2206 0.2425 0.1529 0.0205  0.0228  0.0129  177 VAL A CG2 
1346  N N   . LEU A 186 ? 0.1641 0.1848 0.0894 0.0227  0.0126  0.0149  178 LEU A N   
1347  C CA  . LEU A 186 ? 0.2311 0.2518 0.1584 0.0242  0.0099  0.0167  178 LEU A CA  
1348  C C   . LEU A 186 ? 0.1962 0.2207 0.1325 0.0255  0.0104  0.0156  178 LEU A C   
1349  O O   . LEU A 186 ? 0.2172 0.2469 0.1585 0.0255  0.0099  0.0137  178 LEU A O   
1350  C CB  . LEU A 186 ? 0.2069 0.2286 0.1325 0.0239  0.0050  0.0174  178 LEU A CB  
1351  C CG  . LEU A 186 ? 0.2599 0.2752 0.1738 0.0227  0.0032  0.0188  178 LEU A CG  
1352  C CD1 . LEU A 186 ? 0.2612 0.2737 0.1683 0.0208  0.0047  0.0166  178 LEU A CD1 
1353  C CD2 . LEU A 186 ? 0.2427 0.2587 0.1563 0.0224  -0.0032 0.0208  178 LEU A CD2 
1354  N N   . TYR A 187 ? 0.1863 0.2075 0.1236 0.0265  0.0113  0.0169  179 TYR A N   
1355  C CA  . TYR A 187 ? 0.1554 0.1771 0.0985 0.0278  0.0117  0.0155  179 TYR A CA  
1356  C C   . TYR A 187 ? 0.2481 0.2691 0.1944 0.0307  0.0087  0.0162  179 TYR A C   
1357  O O   . TYR A 187 ? 0.2108 0.2274 0.1546 0.0312  0.0068  0.0191  179 TYR A O   
1358  C CB  . TYR A 187 ? 0.1732 0.1907 0.1157 0.0265  0.0135  0.0169  179 TYR A CB  
1359  C CG  . TYR A 187 ? 0.2179 0.2316 0.1634 0.0276  0.0124  0.0163  179 TYR A CG  
1360  C CD1 . TYR A 187 ? 0.1609 0.1761 0.1093 0.0292  0.0123  0.0128  179 TYR A CD1 
1361  C CD2 . TYR A 187 ? 0.2203 0.2283 0.1651 0.0267  0.0116  0.0194  179 TYR A CD2 
1362  C CE1 . TYR A 187 ? 0.1802 0.1899 0.1293 0.0304  0.0113  0.0116  179 TYR A CE1 
1363  C CE2 . TYR A 187 ? 0.2401 0.2427 0.1865 0.0273  0.0098  0.0186  179 TYR A CE2 
1364  C CZ  . TYR A 187 ? 0.2299 0.2326 0.1778 0.0294  0.0096  0.0144  179 TYR A CZ  
1365  O OH  . TYR A 187 ? 0.2638 0.2590 0.2114 0.0302  0.0079  0.0130  179 TYR A OH  
1366  N N   . ASP A 188 ? 0.1608 0.1861 0.1126 0.0329  0.0087  0.0138  180 ASP A N   
1367  C CA  . ASP A 188 ? 0.1754 0.2009 0.1324 0.0368  0.0066  0.0140  180 ASP A CA  
1368  C C   . ASP A 188 ? 0.2094 0.2273 0.1660 0.0384  0.0070  0.0133  180 ASP A C   
1369  O O   . ASP A 188 ? 0.2483 0.2657 0.2065 0.0399  0.0090  0.0100  180 ASP A O   
1370  C CB  . ASP A 188 ? 0.2285 0.2622 0.1922 0.0388  0.0077  0.0118  180 ASP A CB  
1371  C CG  . ASP A 188 ? 0.2518 0.2866 0.2226 0.0439  0.0065  0.0119  180 ASP A CG  
1372  O OD1 . ASP A 188 ? 0.2293 0.2587 0.1997 0.0456  0.0033  0.0144  180 ASP A OD1 
1373  O OD2 . ASP A 188 ? 0.2666 0.3080 0.2435 0.0464  0.0089  0.0098  180 ASP A OD2 
1374  N N   . ASP A 189 ? 0.2007 0.2120 0.1543 0.0379  0.0048  0.0165  181 ASP A N   
1375  C CA  . ASP A 189 ? 0.2259 0.2286 0.1789 0.0386  0.0041  0.0165  181 ASP A CA  
1376  C C   . ASP A 189 ? 0.2761 0.2762 0.2335 0.0436  0.0017  0.0163  181 ASP A C   
1377  O O   . ASP A 189 ? 0.2616 0.2586 0.2191 0.0445  -0.0017 0.0201  181 ASP A O   
1378  C CB  . ASP A 189 ? 0.2458 0.2432 0.1944 0.0352  0.0033  0.0208  181 ASP A CB  
1379  C CG  . ASP A 189 ? 0.2869 0.2749 0.2353 0.0348  0.0016  0.0216  181 ASP A CG  
1380  O OD1 . ASP A 189 ? 0.3449 0.3287 0.2952 0.0380  0.0007  0.0183  181 ASP A OD1 
1381  O OD2 . ASP A 189 ? 0.3326 0.3172 0.2787 0.0314  0.0013  0.0255  181 ASP A OD2 
1382  N N   . ASN A 190 ? 0.2395 0.2406 0.2005 0.0473  0.0035  0.0121  182 ASN A N   
1383  C CA  . ASN A 190 ? 0.3020 0.3020 0.2688 0.0533  0.0022  0.0115  182 ASN A CA  
1384  C C   . ASN A 190 ? 0.3581 0.3458 0.3227 0.0559  0.0015  0.0094  182 ASN A C   
1385  O O   . ASN A 190 ? 0.4385 0.4244 0.4069 0.0618  0.0025  0.0064  182 ASN A O   
1386  C CB  . ASN A 190 ? 0.2919 0.3024 0.2650 0.0566  0.0055  0.0085  182 ASN A CB  
1387  C CG  . ASN A 190 ? 0.3942 0.4048 0.3637 0.0558  0.0101  0.0037  182 ASN A CG  
1388  O OD1 . ASN A 190 ? 0.3703 0.3721 0.3331 0.0535  0.0102  0.0021  182 ASN A OD1 
1389  N ND2 . ASN A 190 ? 0.4638 0.4846 0.4378 0.0572  0.0135  0.0019  182 ASN A ND2 
1390  N N   . ASN A 191 ? 0.4226 0.4015 0.3813 0.0517  -0.0004 0.0111  183 ASN A N   
1391  C CA  . ASN A 191 ? 0.4971 0.4627 0.4523 0.0526  -0.0020 0.0092  183 ASN A CA  
1392  C C   . ASN A 191 ? 0.5775 0.5341 0.5332 0.0531  -0.0069 0.0138  183 ASN A C   
1393  O O   . ASN A 191 ? 0.5782 0.5384 0.5347 0.0509  -0.0088 0.0192  183 ASN A O   
1394  C CB  . ASN A 191 ? 0.4774 0.4395 0.4266 0.0466  -0.0014 0.0085  183 ASN A CB  
1395  C CG  . ASN A 191 ? 0.4672 0.4385 0.4157 0.0453  0.0029  0.0051  183 ASN A CG  
1396  O OD1 . ASN A 191 ? 0.4170 0.3881 0.3645 0.0486  0.0054  0.0001  183 ASN A OD1 
1397  N ND2 . ASN A 191 ? 0.3863 0.3656 0.3351 0.0408  0.0039  0.0078  183 ASN A ND2 
1398  N N   . ILE A 192 ? 0.6604 0.6041 0.6144 0.0560  -0.0090 0.0117  184 ILE A N   
1399  C CA  . ILE A 192 ? 0.7406 0.6736 0.6949 0.0564  -0.0142 0.0161  184 ILE A CA  
1400  C C   . ILE A 192 ? 0.7912 0.7208 0.7414 0.0486  -0.0167 0.0217  184 ILE A C   
1401  O O   . ILE A 192 ? 0.8264 0.7510 0.7768 0.0472  -0.0206 0.0275  184 ILE A O   
1402  C CB  . ILE A 192 ? 0.7408 0.6588 0.6933 0.0614  -0.0160 0.0119  184 ILE A CB  
1403  N N   . GLY A 200 ? 0.7569 0.6277 0.6492 0.0324  -0.0184 -0.0160 192 GLY A N   
1404  C CA  . GLY A 200 ? 0.7707 0.6306 0.6494 0.0340  -0.0175 -0.0238 192 GLY A CA  
1405  C C   . GLY A 200 ? 0.7315 0.5992 0.6065 0.0282  -0.0167 -0.0238 192 GLY A C   
1406  O O   . GLY A 200 ? 0.7765 0.6321 0.6403 0.0234  -0.0212 -0.0261 192 GLY A O   
1407  N N   . TRP A 201 ? 0.6339 0.5210 0.5180 0.0284  -0.0117 -0.0209 193 TRP A N   
1408  C CA  . TRP A 201 ? 0.5558 0.4519 0.4389 0.0228  -0.0112 -0.0196 193 TRP A CA  
1409  C C   . TRP A 201 ? 0.5055 0.4193 0.4019 0.0201  -0.0097 -0.0128 193 TRP A C   
1410  O O   . TRP A 201 ? 0.4374 0.3586 0.3346 0.0155  -0.0098 -0.0108 193 TRP A O   
1411  C CB  . TRP A 201 ? 0.5342 0.4338 0.4096 0.0268  -0.0050 -0.0257 193 TRP A CB  
1412  C CG  . TRP A 201 ? 0.6152 0.5284 0.4994 0.0339  0.0022  -0.0263 193 TRP A CG  
1413  C CD1 . TRP A 201 ? 0.5792 0.5101 0.4728 0.0334  0.0058  -0.0229 193 TRP A CD1 
1414  C CD2 . TRP A 201 ? 0.7154 0.6252 0.6002 0.0425  0.0059  -0.0301 193 TRP A CD2 
1415  N NE1 . TRP A 201 ? 0.6065 0.5455 0.5066 0.0404  0.0110  -0.0241 193 TRP A NE1 
1416  C CE2 . TRP A 201 ? 0.7168 0.6440 0.6126 0.0463  0.0113  -0.0283 193 TRP A CE2 
1417  C CE3 . TRP A 201 ? 0.7650 0.6583 0.6425 0.0475  0.0049  -0.0349 193 TRP A CE3 
1418  C CZ2 . TRP A 201 ? 0.7821 0.7123 0.6834 0.0547  0.0156  -0.0303 193 TRP A CZ2 
1419  C CZ3 . TRP A 201 ? 0.8398 0.7356 0.7225 0.0567  0.0098  -0.0373 193 TRP A CZ3 
1420  C CH2 . TRP A 201 ? 0.8130 0.7279 0.7082 0.0601  0.0150  -0.0348 193 TRP A CH2 
1421  N N   . PHE A 202 ? 0.4365 0.3564 0.3424 0.0229  -0.0084 -0.0092 194 PHE A N   
1422  C CA  . PHE A 202 ? 0.4283 0.3631 0.3446 0.0207  -0.0066 -0.0033 194 PHE A CA  
1423  C C   . PHE A 202 ? 0.4658 0.3980 0.3881 0.0197  -0.0096 0.0022  194 PHE A C   
1424  O O   . PHE A 202 ? 0.4761 0.4071 0.4005 0.0246  -0.0086 0.0020  194 PHE A O   
1425  C CB  . PHE A 202 ? 0.3301 0.2779 0.2505 0.0257  -0.0005 -0.0049 194 PHE A CB  
1426  C CG  . PHE A 202 ? 0.3211 0.2822 0.2495 0.0234  0.0013  0.0001  194 PHE A CG  
1427  C CD1 . PHE A 202 ? 0.2642 0.2295 0.1941 0.0178  0.0003  0.0031  194 PHE A CD1 
1428  C CD2 . PHE A 202 ? 0.3846 0.3534 0.3187 0.0269  0.0037  0.0018  194 PHE A CD2 
1429  C CE1 . PHE A 202 ? 0.2880 0.2642 0.2244 0.0165  0.0025  0.0072  194 PHE A CE1 
1430  C CE2 . PHE A 202 ? 0.3913 0.3702 0.3304 0.0249  0.0053  0.0058  194 PHE A CE2 
1431  C CZ  . PHE A 202 ? 0.3219 0.3042 0.2620 0.0201  0.0051  0.0082  194 PHE A CZ  
1432  N N   . THR A 203 ? 0.4639 0.3956 0.3895 0.0132  -0.0134 0.0078  195 THR A N   
1433  C CA  . THR A 203 ? 0.4063 0.3363 0.3375 0.0113  -0.0158 0.0140  195 THR A CA  
1434  C C   . THR A 203 ? 0.3765 0.3188 0.3161 0.0069  -0.0142 0.0209  195 THR A C   
1435  O O   . THR A 203 ? 0.3918 0.3331 0.3361 0.0034  -0.0164 0.0272  195 THR A O   
1436  C CB  . THR A 203 ? 0.4517 0.3657 0.3790 0.0075  -0.0227 0.0149  195 THR A CB  
1437  O OG1 . THR A 203 ? 0.4989 0.4115 0.4251 0.0009  -0.0264 0.0163  195 THR A OG1 
1438  C CG2 . THR A 203 ? 0.4587 0.3586 0.3766 0.0128  -0.0239 0.0076  195 THR A CG2 
1439  N N   . GLU A 204 ? 0.3470 0.3006 0.2886 0.0073  -0.0101 0.0200  196 GLU A N   
1440  C CA  . GLU A 204 ? 0.3349 0.2996 0.2841 0.0042  -0.0078 0.0258  196 GLU A CA  
1441  C C   . GLU A 204 ? 0.3505 0.3195 0.3031 0.0062  -0.0051 0.0300  196 GLU A C   
1442  O O   . GLU A 204 ? 0.2954 0.2635 0.2451 0.0109  -0.0036 0.0274  196 GLU A O   
1443  C CB  . GLU A 204 ? 0.3539 0.3283 0.3036 0.0054  -0.0038 0.0233  196 GLU A CB  
1444  C CG  . GLU A 204 ? 0.3400 0.3112 0.2855 0.0030  -0.0063 0.0199  196 GLU A CG  
1445  C CD  . GLU A 204 ? 0.3660 0.3470 0.3126 0.0037  -0.0026 0.0184  196 GLU A CD  
1446  O OE1 . GLU A 204 ? 0.3115 0.3014 0.2630 0.0054  0.0014  0.0206  196 GLU A OE1 
1447  O OE2 . GLU A 204 ? 0.3353 0.3142 0.2769 0.0026  -0.0039 0.0151  196 GLU A OE2 
1448  N N   . ASN A 205 ? 0.2680 0.2417 0.2267 0.0026  -0.0044 0.0368  197 ASN A N   
1449  C CA  . ASN A 205 ? 0.2425 0.2218 0.2031 0.0040  -0.0005 0.0411  197 ASN A CA  
1450  C C   . ASN A 205 ? 0.2292 0.2190 0.1905 0.0062  0.0050  0.0397  197 ASN A C   
1451  O O   . ASN A 205 ? 0.2127 0.2094 0.1795 0.0040  0.0074  0.0429  197 ASN A O   
1452  C CB  . ASN A 205 ? 0.2469 0.2267 0.2135 -0.0008 -0.0014 0.0493  197 ASN A CB  
1453  C CG  . ASN A 205 ? 0.2928 0.2767 0.2591 0.0004  0.0027  0.0541  197 ASN A CG  
1454  O OD1 . ASN A 205 ? 0.2745 0.2638 0.2374 0.0041  0.0072  0.0521  197 ASN A OD1 
1455  N ND2 . ASN A 205 ? 0.3052 0.2861 0.2744 -0.0032 0.0008  0.0609  197 ASN A ND2 
1456  N N   . ILE A 206 ? 0.2000 0.1910 0.1565 0.0106  0.0068  0.0351  198 ILE A N   
1457  C CA  . ILE A 206 ? 0.1797 0.1786 0.1358 0.0124  0.0110  0.0330  198 ILE A CA  
1458  C C   . ILE A 206 ? 0.1783 0.1829 0.1359 0.0120  0.0154  0.0377  198 ILE A C   
1459  O O   . ILE A 206 ? 0.2249 0.2353 0.1856 0.0115  0.0184  0.0382  198 ILE A O   
1460  C CB  . ILE A 206 ? 0.1913 0.1904 0.1429 0.0165  0.0111  0.0277  198 ILE A CB  
1461  C CG1 . ILE A 206 ? 0.2832 0.2787 0.2337 0.0171  0.0087  0.0227  198 ILE A CG1 
1462  C CG2 . ILE A 206 ? 0.2085 0.2145 0.1589 0.0177  0.0148  0.0265  198 ILE A CG2 
1463  C CD1 . ILE A 206 ? 0.2711 0.2700 0.2228 0.0148  0.0094  0.0212  198 ILE A CD1 
1464  N N   . PRO A 207 ? 0.1957 0.1983 0.1507 0.0125  0.0161  0.0413  199 PRO A N   
1465  C CA  . PRO A 207 ? 0.1661 0.1738 0.1211 0.0122  0.0213  0.0458  199 PRO A CA  
1466  C C   . PRO A 207 ? 0.1644 0.1769 0.1281 0.0091  0.0233  0.0504  199 PRO A C   
1467  O O   . PRO A 207 ? 0.1923 0.2109 0.1581 0.0101  0.0284  0.0513  199 PRO A O   
1468  C CB  . PRO A 207 ? 0.2443 0.2475 0.1947 0.0121  0.0205  0.0496  199 PRO A CB  
1469  C CG  . PRO A 207 ? 0.2184 0.2160 0.1650 0.0144  0.0157  0.0453  199 PRO A CG  
1470  C CD  . PRO A 207 ? 0.2087 0.2047 0.1597 0.0138  0.0127  0.0413  199 PRO A CD  
1471  N N   . GLN A 208 ? 0.1879 0.1974 0.1573 0.0054  0.0191  0.0534  200 GLN A N   
1472  C CA  . GLN A 208 ? 0.1880 0.2029 0.1676 0.0018  0.0200  0.0589  200 GLN A CA  
1473  C C   . GLN A 208 ? 0.1648 0.1842 0.1486 0.0021  0.0201  0.0558  200 GLN A C   
1474  O O   . GLN A 208 ? 0.1784 0.2055 0.1700 0.0017  0.0238  0.0595  200 GLN A O   
1475  C CB  . GLN A 208 ? 0.2525 0.2615 0.2362 -0.0030 0.0138  0.0627  200 GLN A CB  
1476  C CG  . GLN A 208 ? 0.3120 0.3275 0.3079 -0.0077 0.0141  0.0704  200 GLN A CG  
1477  C CD  . GLN A 208 ? 0.3639 0.3723 0.3633 -0.0133 0.0070  0.0746  200 GLN A CD  
1478  O OE1 . GLN A 208 ? 0.3163 0.3140 0.3095 -0.0138 0.0007  0.0699  200 GLN A OE1 
1479  N NE2 . GLN A 208 ? 0.4221 0.4359 0.4311 -0.0175 0.0081  0.0836  200 GLN A NE2 
1480  N N   . ARG A 209 ? 0.1568 0.1716 0.1358 0.0028  0.0162  0.0494  201 ARG A N   
1481  C CA  . ARG A 209 ? 0.1745 0.1928 0.1560 0.0028  0.0160  0.0466  201 ARG A CA  
1482  C C   . ARG A 209 ? 0.1551 0.1799 0.1363 0.0064  0.0221  0.0457  201 ARG A C   
1483  O O   . ARG A 209 ? 0.1500 0.1805 0.1381 0.0061  0.0240  0.0478  201 ARG A O   
1484  C CB  . ARG A 209 ? 0.1515 0.1636 0.1259 0.0035  0.0119  0.0399  201 ARG A CB  
1485  C CG  . ARG A 209 ? 0.1903 0.2054 0.1651 0.0034  0.0116  0.0368  201 ARG A CG  
1486  C CD  . ARG A 209 ? 0.2275 0.2370 0.1943 0.0044  0.0089  0.0303  201 ARG A CD  
1487  N NE  . ARG A 209 ? 0.2076 0.2212 0.1731 0.0052  0.0103  0.0273  201 ARG A NE  
1488  C CZ  . ARG A 209 ? 0.2346 0.2467 0.1937 0.0071  0.0103  0.0221  201 ARG A CZ  
1489  N NH1 . ARG A 209 ? 0.2195 0.2264 0.1736 0.0090  0.0094  0.0189  201 ARG A NH1 
1490  N NH2 . ARG A 209 ? 0.2178 0.2338 0.1764 0.0071  0.0115  0.0204  201 ARG A NH2 
1491  N N   . PHE A 210 ? 0.1753 0.1984 0.1483 0.0099  0.0247  0.0426  202 PHE A N   
1492  C CA  . PHE A 210 ? 0.1976 0.2244 0.1681 0.0130  0.0297  0.0410  202 PHE A CA  
1493  C C   . PHE A 210 ? 0.1587 0.1901 0.1329 0.0140  0.0358  0.0462  202 PHE A C   
1494  O O   . PHE A 210 ? 0.2017 0.2367 0.1777 0.0161  0.0400  0.0459  202 PHE A O   
1495  C CB  . PHE A 210 ? 0.1836 0.2068 0.1440 0.0157  0.0295  0.0362  202 PHE A CB  
1496  C CG  . PHE A 210 ? 0.1920 0.2143 0.1507 0.0158  0.0263  0.0309  202 PHE A CG  
1497  C CD1 . PHE A 210 ? 0.1696 0.1889 0.1291 0.0143  0.0218  0.0293  202 PHE A CD1 
1498  C CD2 . PHE A 210 ? 0.1799 0.2040 0.1361 0.0174  0.0279  0.0278  202 PHE A CD2 
1499  C CE1 . PHE A 210 ? 0.2110 0.2302 0.1685 0.0145  0.0199  0.0247  202 PHE A CE1 
1500  C CE2 . PHE A 210 ? 0.1820 0.2062 0.1371 0.0170  0.0253  0.0239  202 PHE A CE2 
1501  C CZ  . PHE A 210 ? 0.2049 0.2272 0.1607 0.0156  0.0217  0.0224  202 PHE A CZ  
1502  N N   . GLU A 211 ? 0.1525 0.1836 0.1280 0.0125  0.0366  0.0513  203 GLU A N   
1503  C CA  . GLU A 211 ? 0.1554 0.1928 0.1371 0.0128  0.0430  0.0574  203 GLU A CA  
1504  C C   . GLU A 211 ? 0.2070 0.2512 0.2022 0.0115  0.0432  0.0605  203 GLU A C   
1505  O O   . GLU A 211 ? 0.1713 0.2215 0.1715 0.0142  0.0495  0.0628  203 GLU A O   
1506  C CB  . GLU A 211 ? 0.2975 0.3341 0.2805 0.0101  0.0428  0.0636  203 GLU A CB  
1507  C CG  . GLU A 211 ? 0.4057 0.4369 0.3762 0.0116  0.0440  0.0627  203 GLU A CG  
1508  C CD  . GLU A 211 ? 0.4873 0.5197 0.4600 0.0091  0.0462  0.0705  203 GLU A CD  
1509  O OE1 . GLU A 211 ? 0.5130 0.5530 0.4959 0.0078  0.0506  0.0766  203 GLU A OE1 
1510  O OE2 . GLU A 211 ? 0.5412 0.5674 0.5063 0.0082  0.0432  0.0710  203 GLU A OE2 
1511  N N   . SER A 212 ? 0.1735 0.2164 0.1744 0.0076  0.0362  0.0607  204 SER A N   
1512  C CA  . SER A 212 ? 0.1438 0.1930 0.1578 0.0054  0.0348  0.0645  204 SER A CA  
1513  C C   . SER A 212 ? 0.1731 0.2243 0.1872 0.0086  0.0365  0.0605  204 SER A C   
1514  O O   . SER A 212 ? 0.1680 0.2258 0.1937 0.0084  0.0374  0.0644  204 SER A O   
1515  C CB  . SER A 212 ? 0.2152 0.2603 0.2324 -0.0001 0.0259  0.0652  204 SER A CB  
1516  O OG  . SER A 212 ? 0.1735 0.2132 0.1835 0.0001  0.0215  0.0584  204 SER A OG  
1517  N N   . TYR A 213 ? 0.1502 0.1960 0.1526 0.0112  0.0363  0.0534  205 TYR A N   
1518  C CA  . TYR A 213 ? 0.1564 0.2030 0.1576 0.0142  0.0382  0.0499  205 TYR A CA  
1519  C C   . TYR A 213 ? 0.2102 0.2589 0.2097 0.0192  0.0465  0.0504  205 TYR A C   
1520  O O   . TYR A 213 ? 0.1790 0.2274 0.1774 0.0221  0.0485  0.0477  205 TYR A O   
1521  C CB  . TYR A 213 ? 0.1669 0.2073 0.1567 0.0146  0.0348  0.0428  205 TYR A CB  
1522  C CG  . TYR A 213 ? 0.1700 0.2073 0.1589 0.0108  0.0279  0.0409  205 TYR A CG  
1523  C CD1 . TYR A 213 ? 0.2019 0.2410 0.1992 0.0070  0.0236  0.0444  205 TYR A CD1 
1524  C CD2 . TYR A 213 ? 0.1345 0.1668 0.1137 0.0112  0.0255  0.0354  205 TYR A CD2 
1525  C CE1 . TYR A 213 ? 0.2277 0.2620 0.2212 0.0037  0.0174  0.0418  205 TYR A CE1 
1526  C CE2 . TYR A 213 ? 0.1748 0.2038 0.1518 0.0086  0.0204  0.0331  205 TYR A CE2 
1527  C CZ  . TYR A 213 ? 0.1828 0.2119 0.1657 0.0049  0.0164  0.0359  205 TYR A CZ  
1528  O OH  . TYR A 213 ? 0.1724 0.1964 0.1503 0.0024  0.0114  0.0329  205 TYR A OH  
1529  N N   . GLY A 214 ? 0.1485 0.1981 0.1461 0.0201  0.0511  0.0535  206 GLY A N   
1530  C CA  . GLY A 214 ? 0.1990 0.2487 0.1911 0.0250  0.0594  0.0532  206 GLY A CA  
1531  C C   . GLY A 214 ? 0.2124 0.2538 0.1874 0.0270  0.0595  0.0469  206 GLY A C   
1532  O O   . GLY A 214 ? 0.2079 0.2468 0.1756 0.0311  0.0652  0.0448  206 GLY A O   
1533  N N   . TRP A 215 ? 0.1665 0.2034 0.1352 0.0244  0.0533  0.0441  207 TRP A N   
1534  C CA  . TRP A 215 ? 0.1578 0.1879 0.1121 0.0258  0.0524  0.0390  207 TRP A CA  
1535  C C   . TRP A 215 ? 0.1902 0.2178 0.1361 0.0263  0.0554  0.0414  207 TRP A C   
1536  O O   . TRP A 215 ? 0.1958 0.2265 0.1471 0.0246  0.0567  0.0469  207 TRP A O   
1537  C CB  . TRP A 215 ? 0.1529 0.1803 0.1053 0.0234  0.0450  0.0354  207 TRP A CB  
1538  C CG  . TRP A 215 ? 0.2160 0.2440 0.1714 0.0230  0.0421  0.0318  207 TRP A CG  
1539  C CD1 . TRP A 215 ? 0.1738 0.2057 0.1386 0.0225  0.0423  0.0334  207 TRP A CD1 
1540  C CD2 . TRP A 215 ? 0.2075 0.2325 0.1568 0.0227  0.0382  0.0269  207 TRP A CD2 
1541  N NE1 . TRP A 215 ? 0.1772 0.2080 0.1410 0.0217  0.0387  0.0296  207 TRP A NE1 
1542  C CE2 . TRP A 215 ? 0.2008 0.2278 0.1554 0.0218  0.0365  0.0256  207 TRP A CE2 
1543  C CE3 . TRP A 215 ? 0.1785 0.2001 0.1193 0.0229  0.0357  0.0240  207 TRP A CE3 
1544  C CZ2 . TRP A 215 ? 0.1917 0.2174 0.1429 0.0210  0.0331  0.0216  207 TRP A CZ2 
1545  C CZ3 . TRP A 215 ? 0.1983 0.2194 0.1371 0.0222  0.0323  0.0202  207 TRP A CZ3 
1546  C CH2 . TRP A 215 ? 0.2054 0.2287 0.1493 0.0212  0.0313  0.0191  207 TRP A CH2 
1547  N N   . HIS A 216 ? 0.1929 0.2143 0.1250 0.0282  0.0560  0.0376  208 HIS A N   
1548  C CA  . HIS A 216 ? 0.2718 0.2890 0.1931 0.0279  0.0562  0.0391  208 HIS A CA  
1549  C C   . HIS A 216 ? 0.2240 0.2390 0.1450 0.0253  0.0483  0.0379  208 HIS A C   
1550  O O   . HIS A 216 ? 0.2165 0.2306 0.1378 0.0251  0.0436  0.0335  208 HIS A O   
1551  C CB  . HIS A 216 ? 0.2882 0.2985 0.1938 0.0306  0.0590  0.0353  208 HIS A CB  
1552  C CG  . HIS A 216 ? 0.2855 0.2898 0.1776 0.0297  0.0569  0.0359  208 HIS A CG  
1553  N ND1 . HIS A 216 ? 0.3040 0.3023 0.1859 0.0292  0.0513  0.0317  208 HIS A ND1 
1554  C CD2 . HIS A 216 ? 0.2926 0.2961 0.1798 0.0289  0.0593  0.0407  208 HIS A CD2 
1555  C CE1 . HIS A 216 ? 0.3035 0.2972 0.1747 0.0283  0.0498  0.0338  208 HIS A CE1 
1556  N NE2 . HIS A 216 ? 0.2884 0.2848 0.1619 0.0281  0.0547  0.0392  208 HIS A NE2 
1557  N N   . VAL A 217 ? 0.2247 0.2391 0.1459 0.0236  0.0470  0.0422  209 VAL A N   
1558  C CA  . VAL A 217 ? 0.2121 0.2242 0.1346 0.0219  0.0399  0.0414  209 VAL A CA  
1559  C C   . VAL A 217 ? 0.2535 0.2604 0.1653 0.0218  0.0383  0.0433  209 VAL A C   
1560  O O   . VAL A 217 ? 0.2225 0.2287 0.1305 0.0213  0.0422  0.0481  209 VAL A O   
1561  C CB  . VAL A 217 ? 0.2308 0.2452 0.1648 0.0193  0.0376  0.0449  209 VAL A CB  
1562  C CG1 . VAL A 217 ? 0.2578 0.2680 0.1918 0.0186  0.0308  0.0434  209 VAL A CG1 
1563  C CG2 . VAL A 217 ? 0.1686 0.1878 0.1126 0.0188  0.0382  0.0436  209 VAL A CG2 
1564  N N   . VAL A 218 ? 0.2119 0.2157 0.1194 0.0223  0.0327  0.0400  210 VAL A N   
1565  C CA  . VAL A 218 ? 0.1973 0.1962 0.0970 0.0219  0.0291  0.0424  210 VAL A CA  
1566  C C   . VAL A 218 ? 0.1928 0.1911 0.1006 0.0214  0.0232  0.0428  210 VAL A C   
1567  O O   . VAL A 218 ? 0.2190 0.2180 0.1297 0.0226  0.0190  0.0389  210 VAL A O   
1568  C CB  . VAL A 218 ? 0.2291 0.2244 0.1176 0.0228  0.0265  0.0393  210 VAL A CB  
1569  C CG1 . VAL A 218 ? 0.2161 0.2061 0.0957 0.0220  0.0227  0.0431  210 VAL A CG1 
1570  C CG2 . VAL A 218 ? 0.2089 0.2028 0.0884 0.0238  0.0322  0.0372  210 VAL A CG2 
1571  N N   . PRO A 219 ? 0.2044 0.2011 0.1160 0.0199  0.0227  0.0476  211 PRO A N   
1572  C CA  . PRO A 219 ? 0.2491 0.2432 0.1676 0.0198  0.0171  0.0475  211 PRO A CA  
1573  C C   . PRO A 219 ? 0.2303 0.2195 0.1439 0.0209  0.0118  0.0490  211 PRO A C   
1574  O O   . PRO A 219 ? 0.3160 0.3030 0.2201 0.0205  0.0121  0.0518  211 PRO A O   
1575  C CB  . PRO A 219 ? 0.3114 0.3049 0.2356 0.0170  0.0185  0.0526  211 PRO A CB  
1576  C CG  . PRO A 219 ? 0.2344 0.2291 0.1521 0.0158  0.0238  0.0575  211 PRO A CG  
1577  C CD  . PRO A 219 ? 0.2735 0.2709 0.1842 0.0180  0.0277  0.0534  211 PRO A CD  
1578  N N   . ASN A 220 ? 0.2757 0.2629 0.1956 0.0225  0.0070  0.0469  212 ASN A N   
1579  C CA  A ASN A 220 ? 0.2646 0.2466 0.1837 0.0239  0.0013  0.0492  212 ASN A CA  
1580  C CA  B ASN A 220 ? 0.2591 0.2411 0.1779 0.0238  0.0014  0.0494  212 ASN A CA  
1581  C C   . ASN A 220 ? 0.2987 0.2812 0.2103 0.0249  -0.0010 0.0496  212 ASN A C   
1582  O O   . ASN A 220 ? 0.3488 0.3268 0.2545 0.0242  -0.0041 0.0543  212 ASN A O   
1583  C CB  A ASN A 220 ? 0.3091 0.2851 0.2272 0.0215  0.0002  0.0556  212 ASN A CB  
1584  C CB  B ASN A 220 ? 0.3126 0.2889 0.2295 0.0212  0.0008  0.0561  212 ASN A CB  
1585  C CG  A ASN A 220 ? 0.3417 0.3112 0.2618 0.0234  -0.0063 0.0574  212 ASN A CG  
1586  C CG  B ASN A 220 ? 0.3321 0.3074 0.2561 0.0190  0.0022  0.0570  212 ASN A CG  
1587  O OD1 A ASN A 220 ? 0.2907 0.2575 0.2179 0.0257  -0.0090 0.0543  212 ASN A OD1 
1588  O OD1 B ASN A 220 ? 0.4479 0.4222 0.3783 0.0203  0.0004  0.0529  212 ASN A OD1 
1589  N ND2 A ASN A 220 ? 0.3767 0.3428 0.2897 0.0228  -0.0090 0.0623  212 ASN A ND2 
1590  N ND2 B ASN A 220 ? 0.3869 0.3623 0.3093 0.0154  0.0053  0.0628  212 ASN A ND2 
1591  N N   . VAL A 221 ? 0.2469 0.2344 0.1587 0.0260  -0.0004 0.0449  213 VAL A N   
1592  C CA  . VAL A 221 ? 0.2205 0.2084 0.1262 0.0265  -0.0040 0.0449  213 VAL A CA  
1593  C C   . VAL A 221 ? 0.2301 0.2191 0.1443 0.0295  -0.0100 0.0443  213 VAL A C   
1594  O O   . VAL A 221 ? 0.2351 0.2276 0.1591 0.0317  -0.0093 0.0406  213 VAL A O   
1595  C CB  . VAL A 221 ? 0.2404 0.2325 0.1425 0.0258  -0.0012 0.0407  213 VAL A CB  
1596  C CG1 . VAL A 221 ? 0.2855 0.2772 0.1817 0.0256  -0.0064 0.0407  213 VAL A CG1 
1597  C CG2 . VAL A 221 ? 0.2789 0.2695 0.1728 0.0239  0.0052  0.0413  213 VAL A CG2 
1598  N N   . ASN A 222 ? 0.2176 0.2036 0.1282 0.0297  -0.0156 0.0481  214 ASN A N   
1599  C CA  . ASN A 222 ? 0.2169 0.2056 0.1371 0.0330  -0.0213 0.0480  214 ASN A CA  
1600  C C   . ASN A 222 ? 0.2171 0.2139 0.1415 0.0335  -0.0214 0.0438  214 ASN A C   
1601  O O   . ASN A 222 ? 0.2133 0.2108 0.1302 0.0311  -0.0237 0.0445  214 ASN A O   
1602  C CB  . ASN A 222 ? 0.2618 0.2458 0.1770 0.0326  -0.0281 0.0539  214 ASN A CB  
1603  C CG  . ASN A 222 ? 0.2625 0.2495 0.1898 0.0367  -0.0343 0.0548  214 ASN A CG  
1604  O OD1 . ASN A 222 ? 0.2466 0.2408 0.1852 0.0398  -0.0332 0.0508  214 ASN A OD1 
1605  N ND2 . ASN A 222 ? 0.2719 0.2540 0.1970 0.0369  -0.0408 0.0605  214 ASN A ND2 
1606  N N   . GLY A 223 ? 0.2627 0.2650 0.1981 0.0362  -0.0189 0.0397  215 GLY A N   
1607  C CA  . GLY A 223 ? 0.2125 0.2232 0.1530 0.0363  -0.0182 0.0361  215 GLY A CA  
1608  C C   . GLY A 223 ? 0.1940 0.2104 0.1414 0.0377  -0.0242 0.0380  215 GLY A C   
1609  O O   . GLY A 223 ? 0.2368 0.2609 0.1894 0.0372  -0.0240 0.0359  215 GLY A O   
1610  N N   . HIS A 224 ? 0.2025 0.2158 0.1511 0.0392  -0.0299 0.0426  216 HIS A N   
1611  C CA  . HIS A 224 ? 0.2058 0.2248 0.1614 0.0400  -0.0369 0.0457  216 HIS A CA  
1612  C C   . HIS A 224 ? 0.2655 0.2785 0.2084 0.0359  -0.0433 0.0504  216 HIS A C   
1613  O O   . HIS A 224 ? 0.2761 0.2920 0.2236 0.0360  -0.0508 0.0544  216 HIS A O   
1614  C CB  . HIS A 224 ? 0.2068 0.2281 0.1769 0.0460  -0.0391 0.0475  216 HIS A CB  
1615  C CG  . HIS A 224 ? 0.2229 0.2490 0.2036 0.0504  -0.0327 0.0425  216 HIS A CG  
1616  N ND1 . HIS A 224 ? 0.2601 0.2964 0.2477 0.0503  -0.0294 0.0392  216 HIS A ND1 
1617  C CD2 . HIS A 224 ? 0.2512 0.2724 0.2354 0.0545  -0.0291 0.0403  216 HIS A CD2 
1618  C CE1 . HIS A 224 ? 0.2801 0.3177 0.2741 0.0545  -0.0236 0.0351  216 HIS A CE1 
1619  N NE2 . HIS A 224 ? 0.2723 0.3003 0.2640 0.0571  -0.0235 0.0354  216 HIS A NE2 
1620  N N   . ASP A 225 ? 0.2697 0.2745 0.1967 0.0324  -0.0404 0.0503  217 ASP A N   
1621  C CA  . ASP A 225 ? 0.2843 0.2817 0.1955 0.0284  -0.0452 0.0543  217 ASP A CA  
1622  C C   . ASP A 225 ? 0.2373 0.2340 0.1370 0.0245  -0.0430 0.0508  217 ASP A C   
1623  O O   . ASP A 225 ? 0.2347 0.2283 0.1269 0.0236  -0.0356 0.0477  217 ASP A O   
1624  C CB  . ASP A 225 ? 0.2762 0.2644 0.1773 0.0278  -0.0429 0.0574  217 ASP A CB  
1625  C CG  . ASP A 225 ? 0.3429 0.3229 0.2260 0.0238  -0.0475 0.0619  217 ASP A CG  
1626  O OD1 . ASP A 225 ? 0.3530 0.3319 0.2257 0.0207  -0.0496 0.0606  217 ASP A OD1 
1627  O OD2 . ASP A 225 ? 0.4197 0.3933 0.2979 0.0237  -0.0492 0.0668  217 ASP A OD2 
1628  N N   . THR A 226 ? 0.2773 0.2763 0.1758 0.0220  -0.0497 0.0515  218 THR A N   
1629  C CA  A THR A 226 ? 0.2714 0.2684 0.1591 0.0183  -0.0481 0.0478  218 THR A CA  
1630  C CA  B THR A 226 ? 0.2757 0.2726 0.1633 0.0182  -0.0483 0.0478  218 THR A CA  
1631  C C   . THR A 226 ? 0.2572 0.2422 0.1224 0.0156  -0.0454 0.0477  218 THR A C   
1632  O O   . THR A 226 ? 0.2568 0.2388 0.1134 0.0145  -0.0397 0.0434  218 THR A O   
1633  C CB  A THR A 226 ? 0.2480 0.2488 0.1386 0.0154  -0.0572 0.0492  218 THR A CB  
1634  C CB  B THR A 226 ? 0.2489 0.2494 0.1389 0.0153  -0.0577 0.0496  218 THR A CB  
1635  O OG1 A THR A 226 ? 0.2633 0.2584 0.1454 0.0132  -0.0661 0.0546  218 THR A OG1 
1636  O OG1 B THR A 226 ? 0.2541 0.2495 0.1310 0.0112  -0.0571 0.0459  218 THR A OG1 
1637  C CG2 A THR A 226 ? 0.2562 0.2707 0.1704 0.0184  -0.0583 0.0495  218 THR A CG2 
1638  C CG2 B THR A 226 ? 0.2861 0.2813 0.1694 0.0136  -0.0672 0.0557  218 THR A CG2 
1639  N N   . ALA A 227 ? 0.2894 0.2676 0.1452 0.0150  -0.0488 0.0526  219 ALA A N   
1640  C CA  . ALA A 227 ? 0.3018 0.2691 0.1357 0.0127  -0.0450 0.0530  219 ALA A CA  
1641  C C   . ALA A 227 ? 0.3021 0.2697 0.1369 0.0148  -0.0338 0.0506  219 ALA A C   
1642  O O   . ALA A 227 ? 0.3005 0.2632 0.1223 0.0139  -0.0274 0.0477  219 ALA A O   
1643  C CB  . ALA A 227 ? 0.2998 0.2603 0.1244 0.0114  -0.0509 0.0596  219 ALA A CB  
1644  N N   . ALA A 228 ? 0.2648 0.2378 0.1149 0.0178  -0.0315 0.0518  220 ALA A N   
1645  C CA  . ALA A 228 ? 0.2728 0.2469 0.1262 0.0192  -0.0222 0.0502  220 ALA A CA  
1646  C C   . ALA A 228 ? 0.2530 0.2320 0.1113 0.0198  -0.0168 0.0442  220 ALA A C   
1647  O O   . ALA A 228 ? 0.2442 0.2217 0.0976 0.0198  -0.0092 0.0424  220 ALA A O   
1648  C CB  . ALA A 228 ? 0.2853 0.2627 0.1539 0.0218  -0.0228 0.0525  220 ALA A CB  
1649  N N   . ILE A 229 ? 0.2363 0.2217 0.1054 0.0204  -0.0206 0.0415  221 ILE A N   
1650  C CA  . ILE A 229 ? 0.2321 0.2218 0.1059 0.0206  -0.0160 0.0363  221 ILE A CA  
1651  C C   . ILE A 229 ? 0.2357 0.2191 0.0936 0.0182  -0.0146 0.0339  221 ILE A C   
1652  O O   . ILE A 229 ? 0.2324 0.2151 0.0880 0.0186  -0.0080 0.0307  221 ILE A O   
1653  C CB  . ILE A 229 ? 0.2155 0.2141 0.1044 0.0215  -0.0200 0.0347  221 ILE A CB  
1654  C CG1 . ILE A 229 ? 0.2082 0.2115 0.1115 0.0248  -0.0205 0.0364  221 ILE A CG1 
1655  C CG2 . ILE A 229 ? 0.2065 0.2093 0.0997 0.0212  -0.0154 0.0299  221 ILE A CG2 
1656  C CD1 . ILE A 229 ? 0.2112 0.2232 0.1286 0.0264  -0.0250 0.0362  221 ILE A CD1 
1657  N N   . GLN A 230 ? 0.2611 0.2388 0.1072 0.0157  -0.0212 0.0355  222 GLN A N   
1658  C CA  A GLN A 230 ? 0.2787 0.2479 0.1074 0.0136  -0.0203 0.0325  222 GLN A CA  
1659  C CA  B GLN A 230 ? 0.2834 0.2523 0.1115 0.0135  -0.0205 0.0327  222 GLN A CA  
1660  C C   . GLN A 230 ? 0.2817 0.2442 0.0973 0.0147  -0.0115 0.0323  222 GLN A C   
1661  O O   . GLN A 230 ? 0.2815 0.2407 0.0907 0.0153  -0.0057 0.0284  222 GLN A O   
1662  C CB  A GLN A 230 ? 0.3147 0.2774 0.1313 0.0101  -0.0300 0.0345  222 GLN A CB  
1663  C CB  B GLN A 230 ? 0.3150 0.2770 0.1303 0.0102  -0.0300 0.0352  222 GLN A CB  
1664  C CG  A GLN A 230 ? 0.3251 0.2774 0.1230 0.0076  -0.0304 0.0305  222 GLN A CG  
1665  C CG  B GLN A 230 ? 0.3207 0.2887 0.1468 0.0081  -0.0392 0.0355  222 GLN A CG  
1666  C CD  A GLN A 230 ? 0.3890 0.3364 0.1788 0.0032  -0.0421 0.0320  222 GLN A CD  
1667  C CD  B GLN A 230 ? 0.4031 0.3643 0.2170 0.0043  -0.0498 0.0389  222 GLN A CD  
1668  O OE1 A GLN A 230 ? 0.4253 0.3769 0.2222 0.0022  -0.0498 0.0369  222 GLN A OE1 
1669  O OE1 B GLN A 230 ? 0.4517 0.4010 0.2445 0.0015  -0.0513 0.0372  222 GLN A OE1 
1670  N NE2 A GLN A 230 ? 0.3180 0.2568 0.0946 0.0005  -0.0438 0.0280  222 GLN A NE2 
1671  N NE2 B GLN A 230 ? 0.4113 0.3792 0.2379 0.0045  -0.0574 0.0438  222 GLN A NE2 
1672  N N   . THR A 231 ? 0.2838 0.2447 0.0964 0.0152  -0.0102 0.0370  223 THR A N   
1673  C CA  A THR A 231 ? 0.3088 0.2651 0.1107 0.0162  -0.0013 0.0380  223 THR A CA  
1674  C CA  B THR A 231 ? 0.3132 0.2693 0.1147 0.0162  -0.0012 0.0377  223 THR A CA  
1675  C C   . THR A 231 ? 0.2983 0.2614 0.1130 0.0186  0.0073  0.0358  223 THR A C   
1676  O O   . THR A 231 ? 0.3167 0.2771 0.1242 0.0198  0.0153  0.0342  223 THR A O   
1677  C CB  A THR A 231 ? 0.3452 0.2995 0.1439 0.0155  -0.0027 0.0444  223 THR A CB  
1678  C CB  B THR A 231 ? 0.3460 0.2992 0.1420 0.0154  -0.0020 0.0441  223 THR A CB  
1679  O OG1 A THR A 231 ? 0.3583 0.3059 0.1446 0.0130  -0.0117 0.0468  223 THR A OG1 
1680  O OG1 B THR A 231 ? 0.3232 0.2839 0.1378 0.0166  -0.0033 0.0470  223 THR A OG1 
1681  C CG2 A THR A 231 ? 0.3546 0.3063 0.1449 0.0157  0.0067  0.0461  223 THR A CG2 
1682  C CG2 B THR A 231 ? 0.3569 0.3029 0.1395 0.0126  -0.0114 0.0465  223 THR A CG2 
1683  N N   . ALA A 232 ? 0.2973 0.2689 0.1311 0.0195  0.0056  0.0360  224 ALA A N   
1684  C CA  . ALA A 232 ? 0.2854 0.2631 0.1311 0.0212  0.0124  0.0342  224 ALA A CA  
1685  C C   . ALA A 232 ? 0.2696 0.2472 0.1140 0.0216  0.0149  0.0289  224 ALA A C   
1686  O O   . ALA A 232 ? 0.2602 0.2387 0.1057 0.0231  0.0221  0.0277  224 ALA A O   
1687  C CB  . ALA A 232 ? 0.2534 0.2383 0.1171 0.0219  0.0094  0.0348  224 ALA A CB  
1688  N N   . ILE A 233 ? 0.2775 0.2546 0.1211 0.0204  0.0086  0.0262  225 ILE A N   
1689  C CA  . ILE A 233 ? 0.2660 0.2416 0.1076 0.0202  0.0101  0.0215  225 ILE A CA  
1690  C C   . ILE A 233 ? 0.2809 0.2466 0.1043 0.0208  0.0148  0.0198  225 ILE A C   
1691  O O   . ILE A 233 ? 0.2777 0.2422 0.1007 0.0225  0.0206  0.0169  225 ILE A O   
1692  C CB  . ILE A 233 ? 0.3034 0.2806 0.1482 0.0179  0.0016  0.0199  225 ILE A CB  
1693  C CG1 . ILE A 233 ? 0.2160 0.2040 0.0798 0.0185  -0.0009 0.0211  225 ILE A CG1 
1694  C CG2 . ILE A 233 ? 0.3279 0.3016 0.1685 0.0171  0.0023  0.0155  225 ILE A CG2 
1695  C CD1 . ILE A 233 ? 0.2598 0.2517 0.1292 0.0164  -0.0089 0.0210  225 ILE A CD1 
1696  N N   . GLU A 234 ? 0.2669 0.2247 0.0743 0.0197  0.0126  0.0217  226 GLU A N   
1697  C CA  . GLU A 234 ? 0.2820 0.2322 0.0767 0.0197  0.0177  0.0196  226 GLU A CA  
1698  C C   . GLU A 234 ? 0.3584 0.3130 0.1602 0.0224  0.0281  0.0205  226 GLU A C   
1699  O O   . GLU A 234 ? 0.2968 0.2488 0.0965 0.0240  0.0340  0.0171  226 GLU A O   
1700  C CB  . GLU A 234 ? 0.2986 0.2426 0.0800 0.0171  0.0135  0.0220  226 GLU A CB  
1701  N N   . ALA A 235 ? 0.2906 0.2517 0.1012 0.0229  0.0300  0.0254  227 ALA A N   
1702  C CA  . ALA A 235 ? 0.3408 0.3071 0.1598 0.0248  0.0390  0.0272  227 ALA A CA  
1703  C C   . ALA A 235 ? 0.2781 0.2494 0.1090 0.0270  0.0425  0.0244  227 ALA A C   
1704  O O   . ALA A 235 ? 0.2834 0.2563 0.1180 0.0289  0.0497  0.0237  227 ALA A O   
1705  C CB  . ALA A 235 ? 0.2983 0.2697 0.1243 0.0242  0.0390  0.0335  227 ALA A CB  
1706  N N   . ALA A 236 ? 0.2403 0.2146 0.0774 0.0270  0.0375  0.0232  228 ALA A N   
1707  C CA  . ALA A 236 ? 0.2285 0.2075 0.0770 0.0282  0.0396  0.0206  228 ALA A CA  
1708  C C   . ALA A 236 ? 0.2934 0.2656 0.1336 0.0294  0.0419  0.0158  228 ALA A C   
1709  O O   . ALA A 236 ? 0.2829 0.2571 0.1295 0.0317  0.0475  0.0149  228 ALA A O   
1710  C CB  . ALA A 236 ? 0.2148 0.1993 0.0751 0.0262  0.0322  0.0193  228 ALA A CB  
1711  N N   . ARG A 237 ? 0.2618 0.2254 0.0884 0.0277  0.0368  0.0130  229 ARG A N   
1712  C CA  . ARG A 237 ? 0.2940 0.2492 0.1120 0.0285  0.0379  0.0081  229 ARG A CA  
1713  C C   . ARG A 237 ? 0.3461 0.2981 0.1601 0.0313  0.0462  0.0076  229 ARG A C   
1714  O O   . ARG A 237 ? 0.3078 0.2559 0.1210 0.0340  0.0502  0.0044  229 ARG A O   
1715  C CB  . ARG A 237 ? 0.3007 0.2470 0.1046 0.0254  0.0297  0.0058  229 ARG A CB  
1716  C CG  . ARG A 237 ? 0.2624 0.2124 0.0715 0.0230  0.0215  0.0061  229 ARG A CG  
1717  C CD  . ARG A 237 ? 0.3264 0.2694 0.1235 0.0191  0.0121  0.0058  229 ARG A CD  
1718  N NE  . ARG A 237 ? 0.3631 0.2940 0.1460 0.0181  0.0112  0.0016  229 ARG A NE  
1719  C CZ  . ARG A 237 ? 0.4443 0.3694 0.2243 0.0171  0.0082  -0.0021 229 ARG A CZ  
1720  N NH1 . ARG A 237 ? 0.4181 0.3512 0.2125 0.0161  0.0059  -0.0018 229 ARG A NH1 
1721  N NH2 . ARG A 237 ? 0.4750 0.3872 0.2410 0.0164  0.0073  -0.0060 229 ARG A NH2 
1722  N N   . ALA A 238 ? 0.3472 0.3010 0.1588 0.0309  0.0490  0.0111  230 ALA A N   
1723  C CA  . ALA A 238 ? 0.3499 0.3017 0.1576 0.0336  0.0573  0.0112  230 ALA A CA  
1724  C C   . ALA A 238 ? 0.3667 0.3274 0.1904 0.0368  0.0649  0.0135  230 ALA A C   
1725  O O   . ALA A 238 ? 0.3290 0.2883 0.1518 0.0402  0.0722  0.0126  230 ALA A O   
1726  C CB  . ALA A 238 ? 0.3590 0.3103 0.1589 0.0315  0.0576  0.0150  230 ALA A CB  
1727  N N   . GLU A 239 ? 0.3251 0.2950 0.1634 0.0359  0.0633  0.0166  231 GLU A N   
1728  C CA  . GLU A 239 ? 0.3119 0.2908 0.1665 0.0383  0.0690  0.0194  231 GLU A CA  
1729  C C   . GLU A 239 ? 0.3333 0.3102 0.1912 0.0407  0.0690  0.0154  231 GLU A C   
1730  O O   . GLU A 239 ? 0.3247 0.3047 0.1892 0.0395  0.0646  0.0150  231 GLU A O   
1731  C CB  . GLU A 239 ? 0.3026 0.2905 0.1694 0.0360  0.0663  0.0243  231 GLU A CB  
1732  C CG  . GLU A 239 ? 0.5001 0.4980 0.3836 0.0372  0.0716  0.0290  231 GLU A CG  
1733  C CD  . GLU A 239 ? 0.5571 0.5578 0.4418 0.0379  0.0783  0.0332  231 GLU A CD  
1734  O OE1 . GLU A 239 ? 0.5716 0.5713 0.4505 0.0355  0.0773  0.0362  231 GLU A OE1 
1735  O OE2 . GLU A 239 ? 0.6443 0.6483 0.5360 0.0410  0.0847  0.0338  231 GLU A OE2 
1736  N N   . THR A 240 ? 0.2881 0.2591 0.1406 0.0442  0.0742  0.0124  232 THR A N   
1737  C CA  . THR A 240 ? 0.3415 0.3076 0.1938 0.0466  0.0737  0.0083  232 THR A CA  
1738  C C   . THR A 240 ? 0.3735 0.3487 0.2435 0.0494  0.0778  0.0112  232 THR A C   
1739  O O   . THR A 240 ? 0.3201 0.2928 0.1922 0.0508  0.0765  0.0088  232 THR A O   
1740  C CB  . THR A 240 ? 0.3617 0.3156 0.1997 0.0499  0.0773  0.0037  232 THR A CB  
1741  O OG1 . THR A 240 ? 0.3855 0.3430 0.2276 0.0536  0.0861  0.0061  232 THR A OG1 
1742  C CG2 . THR A 240 ? 0.3587 0.3026 0.1781 0.0466  0.0719  0.0008  232 THR A CG2 
1743  N N   . GLY A 241 ? 0.3426 0.3281 0.2254 0.0499  0.0824  0.0166  233 GLY A N   
1744  C CA  . GLY A 241 ? 0.3020 0.2966 0.2024 0.0522  0.0860  0.0202  233 GLY A CA  
1745  C C   . GLY A 241 ? 0.2313 0.2355 0.1444 0.0487  0.0815  0.0240  233 GLY A C   
1746  O O   . GLY A 241 ? 0.2382 0.2500 0.1662 0.0500  0.0833  0.0272  233 GLY A O   
1747  N N   . LYS A 242 ? 0.2636 0.2674 0.1717 0.0445  0.0755  0.0239  234 LYS A N   
1748  C CA  . LYS A 242 ? 0.2093 0.2211 0.1303 0.0404  0.0696  0.0268  234 LYS A CA  
1749  C C   . LYS A 242 ? 0.2209 0.2284 0.1353 0.0368  0.0612  0.0229  234 LYS A C   
1750  O O   . LYS A 242 ? 0.2474 0.2484 0.1480 0.0365  0.0598  0.0207  234 LYS A O   
1751  C CB  . LYS A 242 ? 0.1875 0.2056 0.1143 0.0384  0.0711  0.0326  234 LYS A CB  
1752  C CG  . LYS A 242 ? 0.2482 0.2707 0.1796 0.0412  0.0798  0.0373  234 LYS A CG  
1753  C CD  . LYS A 242 ? 0.2653 0.2921 0.1996 0.0379  0.0793  0.0429  234 LYS A CD  
1754  C CE  . LYS A 242 ? 0.4174 0.4504 0.3604 0.0389  0.0861  0.0482  234 LYS A CE  
1755  N NZ  . LYS A 242 ? 0.5225 0.5597 0.4694 0.0348  0.0846  0.0544  234 LYS A NZ  
1756  N N   . PRO A 243 ? 0.1940 0.2055 0.1179 0.0340  0.0554  0.0224  235 PRO A N   
1757  C CA  . PRO A 243 ? 0.1856 0.1956 0.1056 0.0308  0.0483  0.0199  235 PRO A CA  
1758  C C   . PRO A 243 ? 0.2262 0.2377 0.1450 0.0293  0.0469  0.0225  235 PRO A C   
1759  O O   . PRO A 243 ? 0.1879 0.2031 0.1124 0.0294  0.0500  0.0268  235 PRO A O   
1760  C CB  . PRO A 243 ? 0.1792 0.1942 0.1104 0.0286  0.0443  0.0198  235 PRO A CB  
1761  C CG  . PRO A 243 ? 0.1921 0.2126 0.1349 0.0294  0.0480  0.0240  235 PRO A CG  
1762  C CD  . PRO A 243 ? 0.1650 0.1833 0.1039 0.0335  0.0553  0.0250  235 PRO A CD  
1763  N N   . SER A 244 ? 0.1756 0.1841 0.0876 0.0278  0.0419  0.0204  236 SER A N   
1764  C CA  . SER A 244 ? 0.1827 0.1910 0.0924 0.0268  0.0400  0.0228  236 SER A CA  
1765  C C   . SER A 244 ? 0.2056 0.2168 0.1215 0.0249  0.0339  0.0219  236 SER A C   
1766  O O   . SER A 244 ? 0.2254 0.2371 0.1417 0.0242  0.0305  0.0187  236 SER A O   
1767  C CB  . SER A 244 ? 0.2430 0.2445 0.1379 0.0274  0.0393  0.0218  236 SER A CB  
1768  O OG  . SER A 244 ? 0.2013 0.1991 0.0881 0.0295  0.0458  0.0228  236 SER A OG  
1769  N N   . ILE A 245 ? 0.1630 0.1757 0.0834 0.0241  0.0327  0.0248  237 ILE A N   
1770  C CA  . ILE A 245 ? 0.1587 0.1723 0.0828 0.0233  0.0275  0.0238  237 ILE A CA  
1771  C C   . ILE A 245 ? 0.1988 0.2091 0.1178 0.0235  0.0255  0.0262  237 ILE A C   
1772  O O   . ILE A 245 ? 0.2053 0.2140 0.1227 0.0232  0.0279  0.0301  237 ILE A O   
1773  C CB  . ILE A 245 ? 0.1799 0.1963 0.1137 0.0221  0.0267  0.0244  237 ILE A CB  
1774  C CG1 . ILE A 245 ? 0.1500 0.1659 0.0861 0.0223  0.0222  0.0228  237 ILE A CG1 
1775  C CG2 . ILE A 245 ? 0.2304 0.2469 0.1680 0.0212  0.0292  0.0290  237 ILE A CG2 
1776  C CD1 . ILE A 245 ? 0.2097 0.2268 0.1523 0.0211  0.0210  0.0217  237 ILE A CD1 
1777  N N   . ILE A 246 ? 0.1942 0.2039 0.1113 0.0239  0.0210  0.0245  238 ILE A N   
1778  C CA  . ILE A 246 ? 0.1987 0.2051 0.1114 0.0242  0.0177  0.0270  238 ILE A CA  
1779  C C   . ILE A 246 ? 0.2173 0.2252 0.1383 0.0251  0.0140  0.0267  238 ILE A C   
1780  O O   . ILE A 246 ? 0.1998 0.2112 0.1254 0.0258  0.0119  0.0237  238 ILE A O   
1781  C CB  . ILE A 246 ? 0.2109 0.2151 0.1148 0.0241  0.0148  0.0259  238 ILE A CB  
1782  C CG1 . ILE A 246 ? 0.2097 0.2101 0.1031 0.0238  0.0190  0.0255  238 ILE A CG1 
1783  C CG2 . ILE A 246 ? 0.1974 0.1987 0.0981 0.0244  0.0101  0.0290  238 ILE A CG2 
1784  C CD1 . ILE A 246 ? 0.2572 0.2543 0.1415 0.0231  0.0159  0.0229  238 ILE A CD1 
1785  N N   . CYS A 247 ? 0.2004 0.2054 0.1233 0.0250  0.0135  0.0299  239 CYS A N   
1786  C CA  . CYS A 247 ? 0.1848 0.1889 0.1147 0.0262  0.0105  0.0292  239 CYS A CA  
1787  C C   . CYS A 247 ? 0.2374 0.2397 0.1663 0.0281  0.0058  0.0303  239 CYS A C   
1788  O O   . CYS A 247 ? 0.2579 0.2557 0.1831 0.0278  0.0040  0.0344  239 CYS A O   
1789  C CB  . CYS A 247 ? 0.2043 0.2048 0.1368 0.0247  0.0114  0.0323  239 CYS A CB  
1790  S SG  . CYS A 247 ? 0.2625 0.2665 0.1984 0.0222  0.0159  0.0320  239 CYS A SG  
1791  N N   . CYS A 248 ? 0.2093 0.2157 0.1427 0.0301  0.0037  0.0273  240 CYS A N   
1792  C CA  . CYS A 248 ? 0.1763 0.1830 0.1109 0.0321  -0.0010 0.0286  240 CYS A CA  
1793  C C   . CYS A 248 ? 0.2445 0.2496 0.1870 0.0355  -0.0029 0.0281  240 CYS A C   
1794  O O   . CYS A 248 ? 0.2145 0.2232 0.1631 0.0374  -0.0014 0.0244  240 CYS A O   
1795  C CB  . CYS A 248 ? 0.1795 0.1926 0.1155 0.0320  -0.0022 0.0264  240 CYS A CB  
1796  S SG  . CYS A 248 ? 0.2400 0.2523 0.1650 0.0284  -0.0009 0.0263  240 CYS A SG  
1797  N N   . LYS A 249 ? 0.2483 0.2473 0.1897 0.0363  -0.0059 0.0318  241 LYS A N   
1798  C CA  . LYS A 249 ? 0.2698 0.2650 0.2178 0.0401  -0.0082 0.0314  241 LYS A CA  
1799  C C   . LYS A 249 ? 0.2687 0.2691 0.2235 0.0439  -0.0115 0.0312  241 LYS A C   
1800  O O   . LYS A 249 ? 0.2400 0.2406 0.1931 0.0436  -0.0157 0.0351  241 LYS A O   
1801  C CB  . LYS A 249 ? 0.2755 0.2616 0.2201 0.0392  -0.0109 0.0363  241 LYS A CB  
1802  C CG  . LYS A 249 ? 0.2805 0.2631 0.2194 0.0347  -0.0078 0.0382  241 LYS A CG  
1803  C CD  . LYS A 249 ? 0.3579 0.3375 0.3005 0.0345  -0.0060 0.0352  241 LYS A CD  
1804  C CE  . LYS A 249 ? 0.4077 0.3840 0.3473 0.0298  -0.0041 0.0388  241 LYS A CE  
1805  N NZ  . LYS A 249 ? 0.4135 0.3863 0.3563 0.0288  -0.0037 0.0361  241 LYS A NZ  
1806  N N   . THR A 250 ? 0.3658 0.2583 0.3379 -0.1129 0.1373  -0.0441 242 THR A N   
1807  C CA  . THR A 250 ? 0.3648 0.2501 0.3387 -0.1026 0.1291  -0.0356 242 THR A CA  
1808  C C   . THR A 250 ? 0.3916 0.2626 0.3868 -0.1043 0.1396  -0.0411 242 THR A C   
1809  O O   . THR A 250 ? 0.4428 0.3133 0.4527 -0.1144 0.1518  -0.0549 242 THR A O   
1810  C CB  . THR A 250 ? 0.3395 0.2483 0.3099 -0.0988 0.1153  -0.0416 242 THR A CB  
1811  O OG1 . THR A 250 ? 0.3470 0.2739 0.3322 -0.1062 0.1197  -0.0606 242 THR A OG1 
1812  C CG2 . THR A 250 ? 0.3292 0.2502 0.2789 -0.0967 0.1053  -0.0370 242 THR A CG2 
1813  N N   . LEU A 251 ? 0.3858 0.2457 0.3831 -0.0941 0.1349  -0.0308 243 LEU A N   
1814  C CA  . LEU A 251 ? 0.5565 0.4013 0.5732 -0.0933 0.1441  -0.0346 243 LEU A CA  
1815  C C   . LEU A 251 ? 0.6087 0.4632 0.6302 -0.0843 0.1336  -0.0345 243 LEU A C   
1816  O O   . LEU A 251 ? 0.5821 0.4346 0.6211 -0.0844 0.1389  -0.0439 243 LEU A O   
1817  C CB  . LEU A 251 ? 0.6147 0.4282 0.6311 -0.0886 0.1541  -0.0183 243 LEU A CB  
1818  C CG  . LEU A 251 ? 0.6877 0.4878 0.7001 -0.0967 0.1663  -0.0146 243 LEU A CG  
1819  C CD1 . LEU A 251 ? 0.7650 0.5346 0.7764 -0.0889 0.1751  0.0052  243 LEU A CD1 
1820  C CD2 . LEU A 251 ? 0.6837 0.4870 0.7136 -0.1118 0.1793  -0.0354 243 LEU A CD2 
1821  N N   . GLU A 276 ? 0.6295 0.5803 0.7121 0.0289  0.0496  0.0265  268 GLU A N   
1822  C CA  . GLU A 276 ? 0.6709 0.6228 0.7467 0.0409  0.0424  0.0431  268 GLU A CA  
1823  C C   . GLU A 276 ? 0.7199 0.6428 0.7887 0.0484  0.0517  0.0547  268 GLU A C   
1824  O O   . GLU A 276 ? 0.7722 0.6936 0.8276 0.0545  0.0461  0.0688  268 GLU A O   
1825  C CB  . GLU A 276 ? 0.6488 0.6169 0.7380 0.0513  0.0392  0.0443  268 GLU A CB  
1826  N N   . ALA A 277 ? 0.6957 0.5962 0.7740 0.0481  0.0666  0.0486  269 ALA A N   
1827  C CA  . ALA A 277 ? 0.7095 0.5799 0.7826 0.0544  0.0776  0.0600  269 ALA A CA  
1828  C C   . ALA A 277 ? 0.7505 0.6120 0.8076 0.0453  0.0777  0.0632  269 ALA A C   
1829  O O   . ALA A 277 ? 0.8135 0.6686 0.8567 0.0522  0.0752  0.0790  269 ALA A O   
1830  C CB  . ALA A 277 ? 0.6974 0.5449 0.7865 0.0543  0.0942  0.0506  269 ALA A CB  
1831  N N   . THR A 278 ? 0.6785 0.5418 0.7372 0.0304  0.0805  0.0482  270 THR A N   
1832  C CA  . THR A 278 ? 0.6560 0.5152 0.6996 0.0213  0.0796  0.0497  270 THR A CA  
1833  C C   . THR A 278 ? 0.6085 0.4856 0.6360 0.0243  0.0639  0.0598  270 THR A C   
1834  O O   . THR A 278 ? 0.6029 0.4728 0.6149 0.0244  0.0627  0.0691  270 THR A O   
1835  C CB  . THR A 278 ? 0.6229 0.4900 0.6714 0.0060  0.0822  0.0309  270 THR A CB  
1836  N N   . ARG A 279 ? 0.5546 0.4559 0.5861 0.0266  0.0520  0.0575  271 ARG A N   
1837  C CA  . ARG A 279 ? 0.4795 0.3998 0.4989 0.0288  0.0367  0.0650  271 ARG A CA  
1838  C C   . ARG A 279 ? 0.6018 0.5145 0.6090 0.0408  0.0348  0.0827  271 ARG A C   
1839  O O   . ARG A 279 ? 0.6515 0.5617 0.6428 0.0387  0.0315  0.0882  271 ARG A O   
1840  C CB  . ARG A 279 ? 0.4780 0.4227 0.5084 0.0315  0.0273  0.0613  271 ARG A CB  
1841  C CG  . ARG A 279 ? 0.5390 0.5064 0.5632 0.0245  0.0133  0.0583  271 ARG A CG  
1842  C CD  . ARG A 279 ? 0.5170 0.5078 0.5526 0.0290  0.0048  0.0582  271 ARG A CD  
1843  N NE  . ARG A 279 ? 0.4662 0.4770 0.4965 0.0221  -0.0081 0.0564  271 ARG A NE  
1844  C CZ  . ARG A 279 ? 0.4316 0.4508 0.4641 0.0109  -0.0098 0.0461  271 ARG A CZ  
1845  N NH1 . ARG A 279 ? 0.4245 0.4373 0.4641 0.0056  0.0001  0.0361  271 ARG A NH1 
1846  N NH2 . ARG A 279 ? 0.3907 0.4253 0.4186 0.0052  -0.0209 0.0457  271 ARG A NH2 
1847  N N   . LYS A 280 ? 0.6385 0.5493 0.6526 0.0543  0.0369  0.0919  272 LYS A N   
1848  C CA  . LYS A 280 ? 0.7669 0.6733 0.7695 0.0678  0.0354  0.1098  272 LYS A CA  
1849  C C   . LYS A 280 ? 0.8827 0.7599 0.8785 0.0694  0.0494  0.1179  272 LYS A C   
1850  O O   . LYS A 280 ? 0.8886 0.7626 0.8709 0.0788  0.0484  0.1331  272 LYS A O   
1851  C CB  . LYS A 280 ? 0.7849 0.6986 0.7971 0.0832  0.0344  0.1180  272 LYS A CB  
1852  N N   . HIS A 281 ? 0.9146 0.7721 0.9197 0.0605  0.0627  0.1078  273 HIS A N   
1853  C CA  . HIS A 281 ? 0.9248 0.7552 0.9242 0.0588  0.0763  0.1140  273 HIS A CA  
1854  C C   . HIS A 281 ? 0.9549 0.7903 0.9372 0.0494  0.0711  0.1134  273 HIS A C   
1855  O O   . HIS A 281 ? 1.0265 0.8537 0.9948 0.0551  0.0731  0.1274  273 HIS A O   
1856  C CB  . HIS A 281 ? 0.9263 0.7366 0.9420 0.0501  0.0916  0.1009  273 HIS A CB  
1857  N N   . LEU A 282 ? 0.8526 0.7022 0.8356 0.0358  0.0646  0.0977  274 LEU A N   
1858  C CA  . LEU A 282 ? 0.7640 0.6207 0.7307 0.0278  0.0583  0.0963  274 LEU A CA  
1859  C C   . LEU A 282 ? 0.7359 0.6113 0.6879 0.0353  0.0430  0.1059  274 LEU A C   
1860  O O   . LEU A 282 ? 0.7395 0.6221 0.6775 0.0297  0.0365  0.1043  274 LEU A O   
1861  C CB  . LEU A 282 ? 0.6977 0.5660 0.6693 0.0132  0.0552  0.0777  274 LEU A CB  
1862  C CG  . LEU A 282 ? 0.6841 0.5384 0.6662 0.0025  0.0693  0.0654  274 LEU A CG  
1863  C CD1 . LEU A 282 ? 0.6951 0.5671 0.6805 -0.0095 0.0643  0.0485  274 LEU A CD1 
1864  C CD2 . LEU A 282 ? 0.6423 0.4775 0.6148 -0.0003 0.0797  0.0718  274 LEU A CD2 
1865  N N   . GLY A 283 ? 0.6740 0.5587 0.6293 0.0477  0.0372  0.1147  275 GLY A N   
1866  C CA  . GLY A 283 ? 0.7169 0.6208 0.6595 0.0557  0.0234  0.1237  275 GLY A CA  
1867  C C   . GLY A 283 ? 0.7242 0.6543 0.6692 0.0503  0.0079  0.1140  275 GLY A C   
1868  O O   . GLY A 283 ? 0.7479 0.6955 0.6827 0.0550  -0.0042 0.1190  275 GLY A O   
1869  N N   . TRP A 284 ? 0.6196 0.5539 0.5779 0.0405  0.0082  0.1001  276 TRP A N   
1870  C CA  . TRP A 284 ? 0.5467 0.5047 0.5092 0.0347  -0.0050 0.0916  276 TRP A CA  
1871  C C   . TRP A 284 ? 0.5010 0.4703 0.4794 0.0419  -0.0066 0.0926  276 TRP A C   
1872  O O   . TRP A 284 ? 0.4903 0.4538 0.4831 0.0399  0.0015  0.0859  276 TRP A O   
1873  C CB  . TRP A 284 ? 0.4486 0.4069 0.4143 0.0201  -0.0038 0.0769  276 TRP A CB  
1874  C CG  . TRP A 284 ? 0.4011 0.3817 0.3699 0.0139  -0.0165 0.0698  276 TRP A CG  
1875  C CD1 . TRP A 284 ? 0.4383 0.4325 0.4226 0.0113  -0.0187 0.0631  276 TRP A CD1 
1876  C CD2 . TRP A 284 ? 0.3687 0.3598 0.3251 0.0097  -0.0280 0.0689  276 TRP A CD2 
1877  N NE1 . TRP A 284 ? 0.4235 0.4352 0.4063 0.0052  -0.0304 0.0592  276 TRP A NE1 
1878  C CE2 . TRP A 284 ? 0.4187 0.4279 0.3848 0.0039  -0.0363 0.0620  276 TRP A CE2 
1879  C CE3 . TRP A 284 ? 0.4363 0.4234 0.3747 0.0104  -0.0318 0.0730  276 TRP A CE3 
1880  C CZ2 . TRP A 284 ? 0.3704 0.3914 0.3296 -0.0018 -0.0477 0.0588  276 TRP A CZ2 
1881  C CZ3 . TRP A 284 ? 0.4314 0.4315 0.3624 0.0052  -0.0437 0.0687  276 TRP A CZ3 
1882  C CH2 . TRP A 284 ? 0.3154 0.3311 0.2572 -0.0011 -0.0513 0.0615  276 TRP A CH2 
1883  N N   . ALA A 285 ? 0.4355 0.4230 0.4118 0.0505  -0.0172 0.1002  277 ALA A N   
1884  C CA  . ALA A 285 ? 0.4077 0.4082 0.3983 0.0591  -0.0190 0.1027  277 ALA A CA  
1885  C C   . ALA A 285 ? 0.4025 0.4306 0.4005 0.0531  -0.0319 0.0956  277 ALA A C   
1886  O O   . ALA A 285 ? 0.3535 0.3965 0.3640 0.0596  -0.0345 0.0971  277 ALA A O   
1887  C CB  . ALA A 285 ? 0.4651 0.4668 0.4501 0.0762  -0.0192 0.1185  277 ALA A CB  
1888  N N   . TYR A 286 ? 0.3691 0.4042 0.3606 0.0412  -0.0396 0.0881  278 TYR A N   
1889  C CA  . TYR A 286 ? 0.3716 0.4304 0.3717 0.0342  -0.0503 0.0814  278 TYR A CA  
1890  C C   . TYR A 286 ? 0.3512 0.4122 0.3682 0.0290  -0.0445 0.0730  278 TYR A C   
1891  O O   . TYR A 286 ? 0.3479 0.3923 0.3662 0.0245  -0.0343 0.0674  278 TYR A O   
1892  C CB  . TYR A 286 ? 0.3648 0.4266 0.3543 0.0227  -0.0582 0.0751  278 TYR A CB  
1893  C CG  . TYR A 286 ? 0.3291 0.3932 0.3021 0.0274  -0.0652 0.0815  278 TYR A CG  
1894  C CD1 . TYR A 286 ? 0.3686 0.4559 0.3419 0.0311  -0.0773 0.0841  278 TYR A CD1 
1895  C CD2 . TYR A 286 ? 0.3399 0.3852 0.2973 0.0283  -0.0598 0.0844  278 TYR A CD2 
1896  C CE1 . TYR A 286 ? 0.4015 0.4939 0.3595 0.0360  -0.0841 0.0888  278 TYR A CE1 
1897  C CE2 . TYR A 286 ? 0.3770 0.4265 0.3186 0.0334  -0.0661 0.0901  278 TYR A CE2 
1898  C CZ  . TYR A 286 ? 0.4177 0.4912 0.3595 0.0375  -0.0784 0.0920  278 TYR A CZ  
1899  O OH  . TYR A 286 ? 0.3688 0.4495 0.2947 0.0432  -0.0850 0.0967  278 TYR A OH  
1900  N N   . PRO A 287 ? 0.3027 0.3859 0.3332 0.0295  -0.0506 0.0716  279 PRO A N   
1901  C CA  . PRO A 287 ? 0.3277 0.4164 0.3739 0.0251  -0.0455 0.0637  279 PRO A CA  
1902  C C   . PRO A 287 ? 0.3675 0.4553 0.4121 0.0111  -0.0456 0.0542  279 PRO A C   
1903  O O   . PRO A 287 ? 0.3224 0.4076 0.3552 0.0043  -0.0513 0.0534  279 PRO A O   
1904  C CB  . PRO A 287 ? 0.3267 0.4429 0.3857 0.0288  -0.0537 0.0661  279 PRO A CB  
1905  C CG  . PRO A 287 ? 0.3770 0.5044 0.4264 0.0285  -0.0656 0.0709  279 PRO A CG  
1906  C CD  . PRO A 287 ? 0.3019 0.4088 0.3342 0.0342  -0.0624 0.0769  279 PRO A CD  
1907  N N   . ALA A 288 ? 0.3102 0.4014 0.3670 0.0076  -0.0390 0.0469  280 ALA A N   
1908  C CA  . ALA A 288 ? 0.2585 0.3501 0.3147 -0.0037 -0.0373 0.0384  280 ALA A CA  
1909  C C   . ALA A 288 ? 0.2353 0.3395 0.2880 -0.0118 -0.0481 0.0387  280 ALA A C   
1910  O O   . ALA A 288 ? 0.2311 0.3547 0.2929 -0.0116 -0.0555 0.0413  280 ALA A O   
1911  C CB  . ALA A 288 ? 0.2557 0.3587 0.3279 -0.0043 -0.0309 0.0315  280 ALA A CB  
1912  N N   . PHE A 289 ? 0.2871 0.3800 0.3272 -0.0190 -0.0485 0.0357  281 PHE A N   
1913  C CA  . PHE A 289 ? 0.2278 0.3269 0.2635 -0.0278 -0.0565 0.0342  281 PHE A CA  
1914  C C   . PHE A 289 ? 0.2374 0.3410 0.2666 -0.0265 -0.0673 0.0391  281 PHE A C   
1915  O O   . PHE A 289 ? 0.3065 0.4137 0.3321 -0.0341 -0.0743 0.0370  281 PHE A O   
1916  C CB  . PHE A 289 ? 0.2131 0.3309 0.2635 -0.0335 -0.0576 0.0314  281 PHE A CB  
1917  C CG  . PHE A 289 ? 0.2557 0.3740 0.3124 -0.0346 -0.0476 0.0257  281 PHE A CG  
1918  C CD1 . PHE A 289 ? 0.2575 0.3675 0.3062 -0.0405 -0.0435 0.0208  281 PHE A CD1 
1919  C CD2 . PHE A 289 ? 0.2164 0.3455 0.2872 -0.0291 -0.0425 0.0246  281 PHE A CD2 
1920  C CE1 . PHE A 289 ? 0.2403 0.3548 0.2949 -0.0410 -0.0346 0.0148  281 PHE A CE1 
1921  C CE2 . PHE A 289 ? 0.2434 0.3759 0.3202 -0.0300 -0.0335 0.0178  281 PHE A CE2 
1922  C CZ  . PHE A 289 ? 0.1850 0.3111 0.2537 -0.0361 -0.0297 0.0128  281 PHE A CZ  
1923  N N   . GLU A 290 ? 0.2518 0.3557 0.2793 -0.0168 -0.0687 0.0453  282 GLU A N   
1924  C CA  . GLU A 290 ? 0.3014 0.4114 0.3207 -0.0143 -0.0787 0.0496  282 GLU A CA  
1925  C C   . GLU A 290 ? 0.3566 0.4479 0.3564 -0.0139 -0.0777 0.0501  282 GLU A C   
1926  O O   . GLU A 290 ? 0.3124 0.3877 0.3058 -0.0080 -0.0691 0.0532  282 GLU A O   
1927  C CB  . GLU A 290 ? 0.2694 0.3904 0.2944 -0.0024 -0.0804 0.0571  282 GLU A CB  
1928  N N   . ILE A 291 ? 0.2721 0.3653 0.2629 -0.0203 -0.0859 0.0469  283 ILE A N   
1929  C CA  . ILE A 291 ? 0.2980 0.3766 0.2697 -0.0198 -0.0860 0.0469  283 ILE A CA  
1930  C C   . ILE A 291 ? 0.3053 0.3965 0.2698 -0.0182 -0.0980 0.0478  283 ILE A C   
1931  O O   . ILE A 291 ? 0.2880 0.3917 0.2585 -0.0259 -0.1063 0.0424  283 ILE A O   
1932  C CB  . ILE A 291 ? 0.2747 0.3409 0.2402 -0.0295 -0.0830 0.0395  283 ILE A CB  
1933  C CG1 . ILE A 291 ? 0.3191 0.3764 0.2914 -0.0305 -0.0712 0.0376  283 ILE A CG1 
1934  C CG2 . ILE A 291 ? 0.3143 0.3681 0.2597 -0.0285 -0.0842 0.0392  283 ILE A CG2 
1935  C CD1 . ILE A 291 ? 0.2562 0.3060 0.2244 -0.0390 -0.0680 0.0307  283 ILE A CD1 
1936  N N   . PRO A 292 ? 0.3307 0.4199 0.2828 -0.0087 -0.0989 0.0541  284 PRO A N   
1937  C CA  . PRO A 292 ? 0.3578 0.4634 0.3030 -0.0062 -0.1107 0.0542  284 PRO A CA  
1938  C C   . PRO A 292 ? 0.3877 0.4886 0.3213 -0.0151 -0.1165 0.0455  284 PRO A C   
1939  O O   . PRO A 292 ? 0.3341 0.4164 0.2587 -0.0190 -0.1104 0.0426  284 PRO A O   
1940  C CB  . PRO A 292 ? 0.3650 0.4677 0.2986 0.0080  -0.1075 0.0649  284 PRO A CB  
1941  C CG  . PRO A 292 ? 0.3340 0.4109 0.2617 0.0082  -0.0945 0.0671  284 PRO A CG  
1942  C CD  . PRO A 292 ? 0.3185 0.3912 0.2624 0.0005  -0.0887 0.0617  284 PRO A CD  
1943  N N   . GLN A 293 ? 0.3651 0.4843 0.2992 -0.0179 -0.1283 0.0406  285 GLN A N   
1944  C CA  . GLN A 293 ? 0.3615 0.4771 0.2863 -0.0266 -0.1346 0.0307  285 GLN A CA  
1945  C C   . GLN A 293 ? 0.3376 0.4384 0.2411 -0.0215 -0.1314 0.0321  285 GLN A C   
1946  O O   . GLN A 293 ? 0.3363 0.4232 0.2317 -0.0284 -0.1301 0.0252  285 GLN A O   
1947  C CB  . GLN A 293 ? 0.4254 0.5652 0.3540 -0.0290 -0.1478 0.0249  285 GLN A CB  
1948  C CG  . GLN A 293 ? 0.4611 0.5971 0.3858 -0.0405 -0.1542 0.0122  285 GLN A CG  
1949  C CD  . GLN A 293 ? 0.5681 0.6899 0.5040 -0.0523 -0.1489 0.0077  285 GLN A CD  
1950  O OE1 . GLN A 293 ? 0.6348 0.7647 0.5887 -0.0563 -0.1477 0.0095  285 GLN A OE1 
1951  N NE2 . GLN A 293 ? 0.5734 0.6753 0.4985 -0.0568 -0.1454 0.0027  285 GLN A NE2 
1952  N N   . GLU A 294 ? 0.3491 0.4535 0.2431 -0.0089 -0.1297 0.0417  286 GLU A N   
1953  C CA  . GLU A 294 ? 0.3606 0.4536 0.2342 -0.0034 -0.1265 0.0443  286 GLU A CA  
1954  C C   . GLU A 294 ? 0.3531 0.4212 0.2232 -0.0080 -0.1150 0.0437  286 GLU A C   
1955  O O   . GLU A 294 ? 0.3576 0.4156 0.2131 -0.0099 -0.1140 0.0399  286 GLU A O   
1956  C CB  . GLU A 294 ? 0.3746 0.4743 0.2409 0.0117  -0.1242 0.0575  286 GLU A CB  
1957  N N   . ILE A 295 ? 0.3419 0.4019 0.2254 -0.0097 -0.1064 0.0466  287 ILE A N   
1958  C CA  . ILE A 295 ? 0.3348 0.3746 0.2160 -0.0140 -0.0954 0.0451  287 ILE A CA  
1959  C C   . ILE A 295 ? 0.3237 0.3595 0.2072 -0.0257 -0.0977 0.0341  287 ILE A C   
1960  O O   . ILE A 295 ? 0.3233 0.3464 0.1963 -0.0287 -0.0932 0.0305  287 ILE A O   
1961  C CB  . ILE A 295 ? 0.3633 0.3971 0.2577 -0.0111 -0.0850 0.0509  287 ILE A CB  
1962  C CG1 . ILE A 295 ? 0.4180 0.4473 0.3054 0.0009  -0.0795 0.0626  287 ILE A CG1 
1963  C CG2 . ILE A 295 ? 0.3174 0.3361 0.2144 -0.0183 -0.0750 0.0458  287 ILE A CG2 
1964  C CD1 . ILE A 295 ? 0.5138 0.5363 0.4141 0.0051  -0.0694 0.0683  287 ILE A CD1 
1965  N N   . TYR A 296 ? 0.3224 0.3695 0.2194 -0.0319 -0.1043 0.0292  288 TYR A N   
1966  C CA  . TYR A 296 ? 0.3249 0.3678 0.2234 -0.0422 -0.1069 0.0199  288 TYR A CA  
1967  C C   . TYR A 296 ? 0.3598 0.3987 0.2412 -0.0432 -0.1129 0.0139  288 TYR A C   
1968  O O   . TYR A 296 ? 0.3320 0.3588 0.2068 -0.0481 -0.1101 0.0082  288 TYR A O   
1969  C CB  . TYR A 296 ? 0.3032 0.3602 0.2191 -0.0488 -0.1137 0.0166  288 TYR A CB  
1970  C CG  . TYR A 296 ? 0.3223 0.3814 0.2557 -0.0513 -0.1070 0.0191  288 TYR A CG  
1971  C CD1 . TYR A 296 ? 0.2986 0.3464 0.2335 -0.0558 -0.0988 0.0168  288 TYR A CD1 
1972  C CD2 . TYR A 296 ? 0.2850 0.3601 0.2334 -0.0487 -0.1093 0.0234  288 TYR A CD2 
1973  C CE1 . TYR A 296 ? 0.2868 0.3395 0.2374 -0.0575 -0.0929 0.0185  288 TYR A CE1 
1974  C CE2 . TYR A 296 ? 0.2720 0.3510 0.2363 -0.0505 -0.1033 0.0252  288 TYR A CE2 
1975  C CZ  . TYR A 296 ? 0.2794 0.3474 0.2446 -0.0550 -0.0952 0.0226  288 TYR A CZ  
1976  O OH  . TYR A 296 ? 0.2498 0.3244 0.2304 -0.0561 -0.0894 0.0239  288 TYR A OH  
1977  N N   . ASP A 297 ? 0.3337 0.3845 0.2079 -0.0380 -0.1212 0.0146  289 ASP A N   
1978  C CA  . ASP A 297 ? 0.3460 0.3962 0.2041 -0.0383 -0.1278 0.0076  289 ASP A CA  
1979  C C   . ASP A 297 ? 0.3863 0.4215 0.2267 -0.0339 -0.1202 0.0101  289 ASP A C   
1980  O O   . ASP A 297 ? 0.4073 0.4342 0.2369 -0.0372 -0.1213 0.0026  289 ASP A O   
1981  C CB  . ASP A 297 ? 0.3591 0.4295 0.2130 -0.0322 -0.1380 0.0083  289 ASP A CB  
1982  C CG  . ASP A 297 ? 0.5113 0.5993 0.3819 -0.0385 -0.1473 0.0027  289 ASP A CG  
1983  O OD1 . ASP A 297 ? 0.5011 0.5836 0.3839 -0.0490 -0.1471 -0.0035 289 ASP A OD1 
1984  O OD2 . ASP A 297 ? 0.5116 0.6203 0.3834 -0.0327 -0.1545 0.0050  289 ASP A OD2 
1985  N N   . ALA A 298 ? 0.3511 0.3826 0.1890 -0.0262 -0.1119 0.0206  290 ALA A N   
1986  C CA  . ALA A 298 ? 0.3791 0.3977 0.2018 -0.0226 -0.1037 0.0236  290 ALA A CA  
1987  C C   . ALA A 298 ? 0.3572 0.3612 0.1824 -0.0298 -0.0956 0.0187  290 ALA A C   
1988  O O   . ALA A 298 ? 0.3698 0.3651 0.1815 -0.0298 -0.0920 0.0161  290 ALA A O   
1989  C CB  . ALA A 298 ? 0.3975 0.4142 0.2194 -0.0136 -0.0956 0.0363  290 ALA A CB  
1990  N N   . TRP A 299 ? 0.3301 0.3335 0.1723 -0.0351 -0.0925 0.0178  291 TRP A N   
1991  C CA  . TRP A 299 ? 0.3184 0.3117 0.1641 -0.0408 -0.0845 0.0138  291 TRP A CA  
1992  C C   . TRP A 299 ? 0.3160 0.3073 0.1608 -0.0475 -0.0895 0.0047  291 TRP A C   
1993  O O   . TRP A 299 ? 0.3534 0.3363 0.1945 -0.0502 -0.0836 0.0012  291 TRP A O   
1994  C CB  . TRP A 299 ? 0.3052 0.3009 0.1695 -0.0426 -0.0783 0.0167  291 TRP A CB  
1995  C CG  . TRP A 299 ? 0.3032 0.2917 0.1680 -0.0395 -0.0666 0.0214  291 TRP A CG  
1996  C CD1 . TRP A 299 ? 0.3377 0.3268 0.2094 -0.0342 -0.0621 0.0287  291 TRP A CD1 
1997  C CD2 . TRP A 299 ? 0.2993 0.2788 0.1583 -0.0419 -0.0574 0.0183  291 TRP A CD2 
1998  N NE1 . TRP A 299 ? 0.3497 0.3290 0.2209 -0.0340 -0.0503 0.0298  291 TRP A NE1 
1999  C CE2 . TRP A 299 ? 0.3123 0.2872 0.1760 -0.0391 -0.0475 0.0231  291 TRP A CE2 
2000  C CE3 . TRP A 299 ? 0.2960 0.2716 0.1466 -0.0458 -0.0564 0.0116  291 TRP A CE3 
2001  C CZ2 . TRP A 299 ? 0.2975 0.2653 0.1585 -0.0413 -0.0369 0.0206  291 TRP A CZ2 
2002  C CZ3 . TRP A 299 ? 0.3912 0.3614 0.2383 -0.0469 -0.0462 0.0099  291 TRP A CZ3 
2003  C CH2 . TRP A 299 ? 0.2929 0.2600 0.1456 -0.0453 -0.0366 0.0139  291 TRP A CH2 
2004  N N   . ASN A 300 ? 0.3207 0.3196 0.1696 -0.0503 -0.0998 0.0007  292 ASN A N   
2005  C CA  . ASN A 300 ? 0.3775 0.3722 0.2290 -0.0576 -0.1034 -0.0075 292 ASN A CA  
2006  C C   . ASN A 300 ? 0.4095 0.3932 0.2431 -0.0567 -0.1024 -0.0132 292 ASN A C   
2007  O O   . ASN A 300 ? 0.3999 0.3843 0.2183 -0.0515 -0.1052 -0.0136 292 ASN A O   
2008  C CB  . ASN A 300 ? 0.3846 0.3896 0.2438 -0.0615 -0.1146 -0.0119 292 ASN A CB  
2009  C CG  . ASN A 300 ? 0.3960 0.3956 0.2640 -0.0704 -0.1164 -0.0187 292 ASN A CG  
2010  O OD1 . ASN A 300 ? 0.3812 0.3720 0.2398 -0.0725 -0.1192 -0.0263 292 ASN A OD1 
2011  N ND2 . ASN A 300 ? 0.4343 0.4385 0.3206 -0.0750 -0.1138 -0.0156 292 ASN A ND2 
2012  N N   . ALA A 301 ? 0.3469 0.3215 0.1821 -0.0608 -0.0981 -0.0170 293 ALA A N   
2013  C CA  . ALA A 301 ? 0.3288 0.2935 0.1493 -0.0585 -0.0951 -0.0220 293 ALA A CA  
2014  C C   . ALA A 301 ? 0.4191 0.3780 0.2427 -0.0618 -0.0988 -0.0303 293 ALA A C   
2015  O O   . ALA A 301 ? 0.4246 0.3755 0.2407 -0.0590 -0.0945 -0.0342 293 ALA A O   
2016  C CB  . ALA A 301 ? 0.3711 0.3307 0.1896 -0.0580 -0.0845 -0.0193 293 ALA A CB  
2017  N N   . LYS A 302 ? 0.3717 0.3346 0.2066 -0.0679 -0.1066 -0.0330 294 LYS A N   
2018  C CA  . LYS A 302 ? 0.4000 0.3542 0.2386 -0.0730 -0.1095 -0.0410 294 LYS A CA  
2019  C C   . LYS A 302 ? 0.3635 0.3164 0.1921 -0.0683 -0.1124 -0.0496 294 LYS A C   
2020  O O   . LYS A 302 ? 0.3829 0.3238 0.2068 -0.0686 -0.1105 -0.0554 294 LYS A O   
2021  C CB  . LYS A 302 ? 0.4150 0.3752 0.2710 -0.0819 -0.1161 -0.0419 294 LYS A CB  
2022  C CG  . LYS A 302 ? 0.4781 0.4398 0.3481 -0.0856 -0.1101 -0.0341 294 LYS A CG  
2023  C CD  . LYS A 302 ? 0.5436 0.5096 0.4335 -0.0943 -0.1135 -0.0347 294 LYS A CD  
2024  C CE  . LYS A 302 ? 0.5224 0.4872 0.4246 -0.0958 -0.1043 -0.0274 294 LYS A CE  
2025  N NZ  . LYS A 302 ? 0.5681 0.5402 0.4914 -0.1040 -0.1063 -0.0256 294 LYS A NZ  
2026  N N   . GLU A 303 ? 0.3947 0.3608 0.2197 -0.0634 -0.1170 -0.0504 295 GLU A N   
2027  C CA  . GLU A 303 ? 0.4265 0.3957 0.2425 -0.0587 -0.1198 -0.0592 295 GLU A CA  
2028  C C   . GLU A 303 ? 0.4419 0.4042 0.2446 -0.0516 -0.1119 -0.0583 295 GLU A C   
2029  O O   . GLU A 303 ? 0.4082 0.3638 0.2061 -0.0508 -0.1112 -0.0661 295 GLU A O   
2030  C CB  . GLU A 303 ? 0.4101 0.3984 0.2238 -0.0539 -0.1261 -0.0587 295 GLU A CB  
2031  C CG  . GLU A 303 ? 0.6613 0.6587 0.4668 -0.0495 -0.1297 -0.0686 295 GLU A CG  
2032  C CD  . GLU A 303 ? 0.7528 0.7726 0.5574 -0.0457 -0.1372 -0.0691 295 GLU A CD  
2033  O OE1 . GLU A 303 ? 0.7925 0.8193 0.6015 -0.0447 -0.1393 -0.0604 295 GLU A OE1 
2034  O OE2 . GLU A 303 ? 0.7807 0.8130 0.5801 -0.0439 -0.1409 -0.0780 295 GLU A OE2 
2035  N N   . LYS A 304 ? 0.4399 0.4043 0.2376 -0.0468 -0.1055 -0.0491 296 LYS A N   
2036  C CA  . LYS A 304 ? 0.4299 0.3912 0.2177 -0.0404 -0.0972 -0.0477 296 LYS A CA  
2037  C C   . LYS A 304 ? 0.3895 0.3377 0.1788 -0.0429 -0.0915 -0.0492 296 LYS A C   
2038  O O   . LYS A 304 ? 0.3684 0.3134 0.1511 -0.0388 -0.0877 -0.0531 296 LYS A O   
2039  C CB  . LYS A 304 ? 0.5056 0.4720 0.2897 -0.0364 -0.0918 -0.0378 296 LYS A CB  
2040  C CG  . LYS A 304 ? 0.5922 0.5598 0.3679 -0.0300 -0.0833 -0.0359 296 LYS A CG  
2041  C CD  . LYS A 304 ? 0.6392 0.6106 0.4106 -0.0273 -0.0794 -0.0265 296 LYS A CD  
2042  C CE  . LYS A 304 ? 0.7085 0.6846 0.4713 -0.0209 -0.0724 -0.0247 296 LYS A CE  
2043  N NZ  . LYS A 304 ? 0.7550 0.7352 0.5099 -0.0176 -0.0712 -0.0156 296 LYS A NZ  
2044  N N   . GLY A 305 ? 0.3641 0.3062 0.1617 -0.0492 -0.0908 -0.0456 297 GLY A N   
2045  C CA  . GLY A 305 ? 0.4058 0.3363 0.2034 -0.0513 -0.0860 -0.0465 297 GLY A CA  
2046  C C   . GLY A 305 ? 0.3745 0.2933 0.1694 -0.0535 -0.0903 -0.0553 297 GLY A C   
2047  O O   . GLY A 305 ? 0.3746 0.2844 0.1619 -0.0501 -0.0858 -0.0577 297 GLY A O   
2048  N N   . ALA A 306 ? 0.3801 0.2991 0.1815 -0.0590 -0.0989 -0.0608 298 ALA A N   
2049  C CA  . ALA A 306 ? 0.4673 0.3738 0.2676 -0.0622 -0.1028 -0.0708 298 ALA A CA  
2050  C C   . ALA A 306 ? 0.4930 0.4008 0.2813 -0.0541 -0.1011 -0.0771 298 ALA A C   
2051  O O   . ALA A 306 ? 0.4452 0.3386 0.2272 -0.0530 -0.0993 -0.0825 298 ALA A O   
2052  C CB  . ALA A 306 ? 0.4408 0.3522 0.2532 -0.0699 -0.1118 -0.0768 298 ALA A CB  
2053  N N   . LYS A 307 ? 0.4627 0.3879 0.2476 -0.0482 -0.1016 -0.0761 299 LYS A N   
2054  C CA  . LYS A 307 ? 0.5136 0.4442 0.2883 -0.0413 -0.0998 -0.0814 299 LYS A CA  
2055  C C   . LYS A 307 ? 0.4543 0.3802 0.2221 -0.0355 -0.0905 -0.0769 299 LYS A C   
2056  O O   . LYS A 307 ? 0.4148 0.3364 0.1753 -0.0319 -0.0885 -0.0826 299 LYS A O   
2057  C CB  . LYS A 307 ? 0.5037 0.4552 0.2757 -0.0370 -0.1018 -0.0794 299 LYS A CB  
2058  N N   . LEU A 308 ? 0.4066 0.3345 0.1774 -0.0347 -0.0846 -0.0672 300 LEU A N   
2059  C CA  . LEU A 308 ? 0.3982 0.3252 0.1653 -0.0298 -0.0755 -0.0632 300 LEU A CA  
2060  C C   . LEU A 308 ? 0.4246 0.3335 0.1873 -0.0307 -0.0747 -0.0675 300 LEU A C   
2061  O O   . LEU A 308 ? 0.4334 0.3406 0.1888 -0.0252 -0.0708 -0.0705 300 LEU A O   
2062  C CB  . LEU A 308 ? 0.3798 0.3121 0.1531 -0.0306 -0.0701 -0.0539 300 LEU A CB  
2063  C CG  . LEU A 308 ? 0.3607 0.2960 0.1339 -0.0265 -0.0604 -0.0501 300 LEU A CG  
2064  C CD1 . LEU A 308 ? 0.3912 0.3413 0.1624 -0.0200 -0.0552 -0.0494 300 LEU A CD1 
2065  C CD2 . LEU A 308 ? 0.3352 0.2727 0.1158 -0.0299 -0.0566 -0.0434 300 LEU A CD2 
2066  N N   . GLU A 309 ? 0.4037 0.2984 0.1699 -0.0379 -0.0781 -0.0674 301 GLU A N   
2067  C CA  . GLU A 309 ? 0.4470 0.3207 0.2064 -0.0387 -0.0768 -0.0703 301 GLU A CA  
2068  C C   . GLU A 309 ? 0.4932 0.3538 0.2467 -0.0380 -0.0815 -0.0813 301 GLU A C   
2069  O O   . GLU A 309 ? 0.4657 0.3115 0.2091 -0.0334 -0.0781 -0.0844 301 GLU A O   
2070  C CB  . GLU A 309 ? 0.4453 0.3070 0.2107 -0.0482 -0.0795 -0.0671 301 GLU A CB  
2071  C CG  . GLU A 309 ? 0.4578 0.2982 0.2214 -0.0487 -0.0762 -0.0681 301 GLU A CG  
2072  C CD  . GLU A 309 ? 0.4869 0.3314 0.2695 -0.0527 -0.0703 -0.0576 301 GLU A CD  
2073  O OE1 . GLU A 309 ? 0.4550 0.3155 0.2462 -0.0561 -0.0708 -0.0520 301 GLU A OE1 
2074  O OE2 . GLU A 309 ? 0.4804 0.3123 0.2689 -0.0520 -0.0649 -0.0547 301 GLU A OE2 
2075  N N   . ALA A 310 ? 0.5030 0.3696 0.2625 -0.0419 -0.0888 -0.0879 302 ALA A N   
2076  C CA  . ALA A 310 ? 0.4587 0.3171 0.2141 -0.0412 -0.0927 -0.1001 302 ALA A CA  
2077  C C   . ALA A 310 ? 0.4760 0.3426 0.2206 -0.0312 -0.0876 -0.1014 302 ALA A C   
2078  O O   . ALA A 310 ? 0.4771 0.3289 0.2136 -0.0278 -0.0865 -0.1084 302 ALA A O   
2079  C CB  . ALA A 310 ? 0.4635 0.3344 0.2279 -0.0467 -0.1008 -0.1070 302 ALA A CB  
2080  N N   . GLY A 311 ? 0.4935 0.3831 0.2388 -0.0269 -0.0839 -0.0945 303 GLY A N   
2081  C CA  . GLY A 311 ? 0.4995 0.3996 0.2373 -0.0193 -0.0783 -0.0944 303 GLY A CA  
2082  C C   . GLY A 311 ? 0.4896 0.3798 0.2217 -0.0140 -0.0710 -0.0910 303 GLY A C   
2083  O O   . GLY A 311 ? 0.4886 0.3746 0.2125 -0.0087 -0.0688 -0.0958 303 GLY A O   
2084  N N   . TRP A 312 ? 0.4261 0.3135 0.1619 -0.0150 -0.0671 -0.0829 304 TRP A N   
2085  C CA  . TRP A 312 ? 0.4261 0.3055 0.1557 -0.0096 -0.0601 -0.0798 304 TRP A CA  
2086  C C   . TRP A 312 ? 0.5858 0.4353 0.3043 -0.0086 -0.0630 -0.0875 304 TRP A C   
2087  O O   . TRP A 312 ? 0.5613 0.4038 0.2703 -0.0008 -0.0585 -0.0891 304 TRP A O   
2088  C CB  . TRP A 312 ? 0.4078 0.2918 0.1434 -0.0116 -0.0555 -0.0704 304 TRP A CB  
2089  C CG  . TRP A 312 ? 0.4056 0.2886 0.1358 -0.0049 -0.0474 -0.0666 304 TRP A CG  
2090  C CD1 . TRP A 312 ? 0.4001 0.3060 0.1359 -0.0000 -0.0395 -0.0622 304 TRP A CD1 
2091  C CD2 . TRP A 312 ? 0.4379 0.2963 0.1559 -0.0024 -0.0462 -0.0672 304 TRP A CD2 
2092  N NE1 . TRP A 312 ? 0.3920 0.2928 0.1218 0.0059  -0.0336 -0.0598 304 TRP A NE1 
2093  C CE2 . TRP A 312 ? 0.4143 0.2849 0.1311 0.0060  -0.0372 -0.0623 304 TRP A CE2 
2094  C CE3 . TRP A 312 ? 0.4633 0.2904 0.1723 -0.0071 -0.0515 -0.0717 304 TRP A CE3 
2095  C CZ2 . TRP A 312 ? 0.4291 0.2821 0.1327 0.0126  -0.0327 -0.0604 304 TRP A CZ2 
2096  C CZ3 . TRP A 312 ? 0.4571 0.2692 0.1629 -0.0018 -0.0450 -0.0679 304 TRP A CZ3 
2097  C CH2 . TRP A 312 ? 0.5455 0.3674 0.2418 0.0093  -0.0362 -0.0629 304 TRP A CH2 
2098  N N   . ASN A 313 ? 0.4669 0.2982 0.1878 -0.0167 -0.0702 -0.0926 305 ASN A N   
2099  C CA  . ASN A 313 ? 0.5397 0.3391 0.2528 -0.0173 -0.0722 -0.1009 305 ASN A CA  
2100  C C   . ASN A 313 ? 0.5707 0.3670 0.2776 -0.0114 -0.0733 -0.1113 305 ASN A C   
2101  O O   . ASN A 313 ? 0.5738 0.3465 0.2705 -0.0058 -0.0705 -0.1160 305 ASN A O   
2102  C CB  . ASN A 313 ? 0.5723 0.3570 0.2963 -0.0299 -0.0795 -0.1051 305 ASN A CB  
2103  C CG  . ASN A 313 ? 0.6158 0.3972 0.3494 -0.0352 -0.0756 -0.0940 305 ASN A CG  
2104  O OD1 . ASN A 313 ? 0.5809 0.3652 0.3126 -0.0282 -0.0664 -0.0845 305 ASN A OD1 
2105  N ND2 . ASN A 313 ? 0.6052 0.3890 0.3566 -0.0464 -0.0804 -0.0933 305 ASN A ND2 
2106  N N   . GLU A 314 ? 0.5070 0.3262 0.2190 -0.0120 -0.0766 -0.1149 306 GLU A N   
2107  C CA  . GLU A 314 ? 0.5238 0.3437 0.2293 -0.0067 -0.0771 -0.1247 306 GLU A CA  
2108  C C   . GLU A 314 ? 0.5194 0.3450 0.2151 0.0041  -0.0692 -0.1196 306 GLU A C   
2109  O O   . GLU A 314 ? 0.6671 0.4788 0.3536 0.0106  -0.0678 -0.1267 306 GLU A O   
2110  C CB  . GLU A 314 ? 0.5639 0.4089 0.2748 -0.0101 -0.0816 -0.1282 306 GLU A CB  
2111  C CG  . GLU A 314 ? 0.6818 0.5259 0.4030 -0.0202 -0.0898 -0.1349 306 GLU A CG  
2112  C CD  . GLU A 314 ? 0.8447 0.7172 0.5690 -0.0223 -0.0931 -0.1346 306 GLU A CD  
2113  O OE1 . GLU A 314 ? 0.8888 0.7772 0.6061 -0.0169 -0.0896 -0.1323 306 GLU A OE1 
2114  O OE2 . GLU A 314 ? 0.9122 0.7910 0.6458 -0.0296 -0.0989 -0.1361 306 GLU A OE2 
2115  N N   . LEU A 315 ? 0.4932 0.3402 0.1930 0.0059  -0.0635 -0.1078 307 LEU A N   
2116  C CA  . LEU A 315 ? 0.5478 0.4044 0.2428 0.0144  -0.0554 -0.1025 307 LEU A CA  
2117  C C   . LEU A 315 ? 0.5679 0.4004 0.2528 0.0213  -0.0515 -0.1019 307 LEU A C   
2118  O O   . LEU A 315 ? 0.5131 0.3401 0.1889 0.0303  -0.0478 -0.1044 307 LEU A O   
2119  C CB  . LEU A 315 ? 0.5174 0.4021 0.2235 0.0121  -0.0499 -0.0910 307 LEU A CB  
2120  C CG  . LEU A 315 ? 0.5375 0.4387 0.2445 0.0173  -0.0414 -0.0851 307 LEU A CG  
2121  C CD1 . LEU A 315 ? 0.5915 0.5024 0.2943 0.0191  -0.0415 -0.0894 307 LEU A CD1 
2122  C CD2 . LEU A 315 ? 0.5144 0.4386 0.2350 0.0124  -0.0362 -0.0753 307 LEU A CD2 
2123  N N   . PHE A 316 ? 0.5003 0.3173 0.1852 0.0175  -0.0519 -0.0982 308 PHE A N   
2124  C CA  . PHE A 316 ? 0.5169 0.3084 0.1892 0.0245  -0.0471 -0.0967 308 PHE A CA  
2125  C C   . PHE A 316 ? 0.5532 0.3107 0.2147 0.0280  -0.0495 -0.1084 308 PHE A C   
2126  O O   . PHE A 316 ? 0.5823 0.3214 0.2309 0.0388  -0.0433 -0.1083 308 PHE A O   
2127  C CB  . PHE A 316 ? 0.5116 0.2923 0.1853 0.0179  -0.0469 -0.0905 308 PHE A CB  
2128  C CG  . PHE A 316 ? 0.5431 0.3111 0.2130 0.0258  -0.0375 -0.0828 308 PHE A CG  
2129  C CD1 . PHE A 316 ? 0.5562 0.3425 0.2175 0.0362  -0.0296 -0.0755 308 PHE A CD1 
2130  C CD2 . PHE A 316 ? 0.5809 0.3255 0.2639 0.0228  -0.0352 -0.0807 308 PHE A CD2 
2131  C CE1 . PHE A 316 ? 0.5513 0.3347 0.2163 0.0445  -0.0199 -0.0658 308 PHE A CE1 
2132  C CE2 . PHE A 316 ? 0.5386 0.2777 0.2254 0.0310  -0.0248 -0.0698 308 PHE A CE2 
2133  C CZ  . PHE A 316 ? 0.5598 0.3193 0.2370 0.0425  -0.0173 -0.0622 308 PHE A CZ  
2134  N N   . ALA A 317 ? 0.5883 0.3384 0.2568 0.0194  -0.0576 -0.1188 309 ALA A N   
2135  C CA  . ALA A 317 ? 0.6075 0.3287 0.2717 0.0212  -0.0594 -0.1315 309 ALA A CA  
2136  C C   . ALA A 317 ? 0.6065 0.3367 0.2617 0.0329  -0.0563 -0.1356 309 ALA A C   
2137  O O   . ALA A 317 ? 0.6325 0.3374 0.2780 0.0418  -0.0522 -0.1404 309 ALA A O   
2138  C CB  . ALA A 317 ? 0.6061 0.3260 0.2843 0.0083  -0.0684 -0.1421 309 ALA A CB  
2139  N N   . GLN A 318 ? 0.5954 0.3604 0.2550 0.0329  -0.0575 -0.1333 310 GLN A N   
2140  C CA  . GLN A 318 ? 0.6226 0.3995 0.2750 0.0429  -0.0537 -0.1347 310 GLN A CA  
2141  C C   . GLN A 318 ? 0.5873 0.3610 0.2308 0.0547  -0.0450 -0.1257 310 GLN A C   
2142  O O   . GLN A 318 ? 0.6067 0.3696 0.2400 0.0656  -0.0415 -0.1296 310 GLN A O   
2143  C CB  . GLN A 318 ? 0.6709 0.4852 0.3312 0.0391  -0.0542 -0.1303 310 GLN A CB  
2144  C CG  . GLN A 318 ? 0.7621 0.5847 0.4280 0.0306  -0.0616 -0.1389 310 GLN A CG  
2145  C CD  . GLN A 318 ? 0.8248 0.6810 0.4960 0.0276  -0.0601 -0.1319 310 GLN A CD  
2146  O OE1 . GLN A 318 ? 0.8484 0.7190 0.5286 0.0201  -0.0617 -0.1258 310 GLN A OE1 
2147  N NE2 . GLN A 318 ? 0.8229 0.6898 0.4882 0.0334  -0.0568 -0.1322 310 GLN A NE2 
2148  N N   . TYR A 319 ? 0.5639 0.3492 0.2120 0.0531  -0.0410 -0.1137 311 TYR A N   
2149  C CA  . TYR A 319 ? 0.6584 0.4453 0.3001 0.0639  -0.0322 -0.1045 311 TYR A CA  
2150  C C   . TYR A 319 ? 0.6382 0.3838 0.2639 0.0730  -0.0289 -0.1083 311 TYR A C   
2151  O O   . TYR A 319 ? 0.6630 0.4016 0.2783 0.0866  -0.0227 -0.1074 311 TYR A O   
2152  C CB  . TYR A 319 ? 0.5288 0.3375 0.1816 0.0584  -0.0289 -0.0924 311 TYR A CB  
2153  C CG  . TYR A 319 ? 0.5179 0.3401 0.1704 0.0677  -0.0196 -0.0823 311 TYR A CG  
2154  C CD1 . TYR A 319 ? 0.5320 0.3329 0.1729 0.0755  -0.0143 -0.0778 311 TYR A CD1 
2155  C CD2 . TYR A 319 ? 0.4939 0.3508 0.1591 0.0676  -0.0156 -0.0770 311 TYR A CD2 
2156  C CE1 . TYR A 319 ? 0.5912 0.4103 0.2347 0.0845  -0.0056 -0.0678 311 TYR A CE1 
2157  C CE2 . TYR A 319 ? 0.4823 0.3553 0.1519 0.0742  -0.0079 -0.0686 311 TYR A CE2 
2158  C CZ  . TYR A 319 ? 0.5163 0.3728 0.1761 0.0832  -0.0033 -0.0639 311 TYR A CZ  
2159  O OH  . TYR A 319 ? 0.5476 0.4243 0.2143 0.0900  0.0042  -0.0553 311 TYR A OH  
2160  N N   . GLN A 320 ? 0.6085 0.3251 0.2339 0.0650  -0.0322 -0.1123 312 GLN A N   
2161  C CA  . GLN A 320 ? 0.6727 0.3509 0.2947 0.0704  -0.0262 -0.1124 312 GLN A CA  
2162  C C   . GLN A 320 ? 0.7121 0.3628 0.3234 0.0786  -0.0265 -0.1259 312 GLN A C   
2163  O O   . GLN A 320 ? 0.7305 0.3607 0.3413 0.0892  -0.0176 -0.1212 312 GLN A O   
2164  C CB  . GLN A 320 ? 0.6359 0.3022 0.2810 0.0543  -0.0290 -0.1094 312 GLN A CB  
2165  N N   . ALA A 321 ? 0.6736 0.3376 0.2914 0.0721  -0.0349 -0.1367 313 ALA A N   
2166  C CA  . ALA A 321 ? 0.7032 0.3507 0.3173 0.0786  -0.0349 -0.1485 313 ALA A CA  
2167  C C   . ALA A 321 ? 0.7351 0.3941 0.3362 0.0961  -0.0278 -0.1433 313 ALA A C   
2168  O O   . ALA A 321 ? 0.7349 0.3679 0.3283 0.1074  -0.0224 -0.1475 313 ALA A O   
2169  C CB  . ALA A 321 ? 0.6999 0.3659 0.3238 0.0682  -0.0445 -0.1606 313 ALA A CB  
2170  N N   . LYS A 322 ? 0.7412 0.4401 0.3434 0.0977  -0.0270 -0.1335 314 LYS A N   
2171  C CA  . LYS A 322 ? 0.6994 0.4158 0.2946 0.1118  -0.0210 -0.1278 314 LYS A CA  
2172  C C   . LYS A 322 ? 0.6666 0.3814 0.2548 0.1235  -0.0112 -0.1146 314 LYS A C   
2173  O O   . LYS A 322 ? 0.6787 0.3918 0.2580 0.1387  -0.0048 -0.1118 314 LYS A O   
2174  C CB  . LYS A 322 ? 0.7897 0.5512 0.3961 0.1056  -0.0238 -0.1236 314 LYS A CB  
2175  N N   . TYR A 323 ? 0.6289 0.3064 0.2482 0.0279  0.0070  -0.0933 315 TYR A N   
2176  C CA  . TYR A 323 ? 0.6193 0.3014 0.2528 0.0331  0.0086  -0.0908 315 TYR A CA  
2177  C C   . TYR A 323 ? 0.6806 0.3540 0.3155 0.0238  0.0002  -0.0864 315 TYR A C   
2178  O O   . TYR A 323 ? 0.6047 0.2904 0.2513 0.0192  -0.0010 -0.0813 315 TYR A O   
2179  C CB  . TYR A 323 ? 0.5584 0.2643 0.2074 0.0363  0.0151  -0.0877 315 TYR A CB  
2180  C CG  . TYR A 323 ? 0.6058 0.3224 0.2534 0.0433  0.0234  -0.0914 315 TYR A CG  
2181  C CD1 . TYR A 323 ? 0.6754 0.3933 0.3262 0.0549  0.0299  -0.0958 315 TYR A CD1 
2182  C CD2 . TYR A 323 ? 0.6455 0.3713 0.2885 0.0381  0.0246  -0.0904 315 TYR A CD2 
2183  C CE1 . TYR A 323 ? 0.7297 0.4590 0.3796 0.0606  0.0378  -0.0995 315 TYR A CE1 
2184  C CE2 . TYR A 323 ? 0.6841 0.4199 0.3251 0.0436  0.0324  -0.0936 315 TYR A CE2 
2185  C CZ  . TYR A 323 ? 0.7301 0.4681 0.3748 0.0546  0.0391  -0.0983 315 TYR A CZ  
2186  O OH  . TYR A 323 ? 0.8720 0.6215 0.5152 0.0595  0.0472  -0.1018 315 TYR A OH  
2187  N N   . PRO A 324 ? 0.7114 0.3636 0.3344 0.0208  -0.0056 -0.0882 316 PRO A N   
2188  C CA  . PRO A 324 ? 0.6930 0.3376 0.3161 0.0098  -0.0138 -0.0837 316 PRO A CA  
2189  C C   . PRO A 324 ? 0.6428 0.2909 0.2789 0.0121  -0.0139 -0.0799 316 PRO A C   
2190  O O   . PRO A 324 ? 0.6263 0.2804 0.2693 0.0029  -0.0182 -0.0750 316 PRO A O   
2191  C CB  . PRO A 324 ? 0.6984 0.3184 0.3038 0.0071  -0.0189 -0.0869 316 PRO A CB  
2192  C CG  . PRO A 324 ? 0.6916 0.3051 0.2911 0.0203  -0.0128 -0.0930 316 PRO A CG  
2193  C CD  . PRO A 324 ? 0.7280 0.3623 0.3356 0.0261  -0.0051 -0.0942 316 PRO A CD  
2194  N N   . ALA A 325 ? 0.6196 0.2645 0.2593 0.0240  -0.0094 -0.0821 317 ALA A N   
2195  C CA  . ALA A 325 ? 0.6070 0.2559 0.2593 0.0267  -0.0094 -0.0785 317 ALA A CA  
2196  C C   . ALA A 325 ? 0.5646 0.2370 0.2331 0.0264  -0.0055 -0.0749 317 ALA A C   
2197  O O   . ALA A 325 ? 0.5308 0.2080 0.2080 0.0207  -0.0085 -0.0703 317 ALA A O   
2198  C CB  . ALA A 325 ? 0.6273 0.2697 0.2807 0.0405  -0.0056 -0.0817 317 ALA A CB  
2199  N N   . GLU A 326 ? 0.5937 0.2809 0.2661 0.0321  0.0014  -0.0770 318 GLU A N   
2200  C CA  . GLU A 326 ? 0.5291 0.2379 0.2148 0.0309  0.0050  -0.0734 318 GLU A CA  
2201  C C   . GLU A 326 ? 0.5358 0.2484 0.2203 0.0178  -0.0009 -0.0695 318 GLU A C   
2202  O O   . GLU A 326 ? 0.4767 0.2011 0.1723 0.0142  -0.0016 -0.0653 318 GLU A O   
2203  C CB  . GLU A 326 ? 0.5977 0.3202 0.2850 0.0379  0.0131  -0.0761 318 GLU A CB  
2204  C CG  . GLU A 326 ? 0.6307 0.3573 0.3243 0.0511  0.0201  -0.0795 318 GLU A CG  
2205  C CD  . GLU A 326 ? 0.6954 0.4063 0.3760 0.0566  0.0202  -0.0854 318 GLU A CD  
2206  O OE1 . GLU A 326 ? 0.7089 0.4016 0.3756 0.0503  0.0138  -0.0865 318 GLU A OE1 
2207  O OE2 . GLU A 326 ? 0.7120 0.4298 0.3967 0.0672  0.0269  -0.0890 318 GLU A OE2 
2208  N N   . ALA A 327 ? 0.5817 0.2857 0.2534 0.0108  -0.0053 -0.0711 319 ALA A N   
2209  C CA  . ALA A 327 ? 0.5488 0.2582 0.2203 -0.0017 -0.0116 -0.0674 319 ALA A CA  
2210  C C   . ALA A 327 ? 0.5573 0.2631 0.2341 -0.0093 -0.0177 -0.0636 319 ALA A C   
2211  O O   . ALA A 327 ? 0.5008 0.2201 0.1871 -0.0159 -0.0201 -0.0595 319 ALA A O   
2212  C CB  . ALA A 327 ? 0.5287 0.2280 0.1852 -0.0076 -0.0157 -0.0700 319 ALA A CB  
2213  N N   . ALA A 328 ? 0.5611 0.2492 0.2319 -0.0085 -0.0202 -0.0648 320 ALA A N   
2214  C CA  . ALA A 328 ? 0.5131 0.1971 0.1881 -0.0164 -0.0258 -0.0609 320 ALA A CA  
2215  C C   . ALA A 328 ? 0.5371 0.2333 0.2273 -0.0120 -0.0225 -0.0579 320 ALA A C   
2216  O O   . ALA A 328 ? 0.5368 0.2403 0.2348 -0.0203 -0.0262 -0.0538 320 ALA A O   
2217  C CB  . ALA A 328 ? 0.5383 0.1992 0.2019 -0.0157 -0.0290 -0.0625 320 ALA A CB  
2218  N N   . GLU A 329 ? 0.5236 0.2234 0.2188 0.0007  -0.0155 -0.0601 321 GLU A N   
2219  C CA  . GLU A 329 ? 0.4806 0.1929 0.1904 0.0050  -0.0122 -0.0573 321 GLU A CA  
2220  C C   . GLU A 329 ? 0.4837 0.2160 0.2022 0.0005  -0.0109 -0.0546 321 GLU A C   
2221  O O   . GLU A 329 ? 0.4708 0.2167 0.2044 -0.0022 -0.0114 -0.0496 321 GLU A O   
2222  C CB  . GLU A 329 ? 0.5071 0.2213 0.2216 0.0196  -0.0049 -0.0601 321 GLU A CB  
2223  C CG  . GLU A 329 ? 0.5572 0.2553 0.2687 0.0251  -0.0068 -0.0609 321 GLU A CG  
2224  C CD  . GLU A 329 ? 0.5598 0.2578 0.2797 0.0213  -0.0102 -0.0563 321 GLU A CD  
2225  O OE1 . GLU A 329 ? 0.5568 0.2678 0.2899 0.0274  -0.0061 -0.0548 321 GLU A OE1 
2226  O OE2 . GLU A 329 ? 0.5729 0.2585 0.2862 0.0117  -0.0169 -0.0540 321 GLU A OE2 
2227  N N   . PHE A 330 ? 0.4785 0.2176 0.1925 -0.0002 -0.0093 -0.0559 322 PHE A N   
2228  C CA  . PHE A 330 ? 0.4921 0.2511 0.2150 -0.0041 -0.0086 -0.0523 322 PHE A CA  
2229  C C   . PHE A 330 ? 0.4690 0.2345 0.1980 -0.0163 -0.0162 -0.0476 322 PHE A C   
2230  O O   . PHE A 330 ? 0.4482 0.2331 0.1952 -0.0182 -0.0160 -0.0421 322 PHE A O   
2231  C CB  . PHE A 330 ? 0.4899 0.2517 0.2037 -0.0030 -0.0063 -0.0546 322 PHE A CB  
2232  C CG  . PHE A 330 ? 0.4833 0.2648 0.2058 -0.0058 -0.0056 -0.0503 322 PHE A CG  
2233  C CD1 . PHE A 330 ? 0.3923 0.1906 0.1295 0.0009  0.0013  -0.0473 322 PHE A CD1 
2234  C CD2 . PHE A 330 ? 0.4625 0.2476 0.1807 -0.0151 -0.0121 -0.0485 322 PHE A CD2 
2235  C CE1 . PHE A 330 ? 0.4404 0.2561 0.1865 -0.0016 0.0016  -0.0426 322 PHE A CE1 
2236  C CE2 . PHE A 330 ? 0.3964 0.2002 0.1244 -0.0166 -0.0120 -0.0437 322 PHE A CE2 
2237  C CZ  . PHE A 330 ? 0.4101 0.2281 0.1514 -0.0099 -0.0051 -0.0408 322 PHE A CZ  
2238  N N   . VAL A 331 ? 0.4674 0.2180 0.1824 -0.0247 -0.0229 -0.0497 323 VAL A N   
2239  C CA  . VAL A 331 ? 0.4837 0.2404 0.2028 -0.0373 -0.0303 -0.0461 323 VAL A CA  
2240  C C   . VAL A 331 ? 0.5086 0.2697 0.2415 -0.0388 -0.0308 -0.0420 323 VAL A C   
2241  O O   . VAL A 331 ? 0.4849 0.2656 0.2338 -0.0437 -0.0322 -0.0368 323 VAL A O   
2242  C CB  . VAL A 331 ? 0.5060 0.2500 0.2135 -0.0453 -0.0362 -0.0474 323 VAL A CB  
2243  C CG1 . VAL A 331 ? 0.5003 0.2507 0.2136 -0.0584 -0.0433 -0.0435 323 VAL A CG1 
2244  C CG2 . VAL A 331 ? 0.5020 0.2492 0.2021 -0.0451 -0.0362 -0.0494 323 VAL A CG2 
2245  N N   . ARG A 332 ? 0.4277 0.1703 0.1539 -0.0342 -0.0296 -0.0443 324 ARG A N   
2246  C CA  . ARG A 332 ? 0.4768 0.2218 0.2143 -0.0354 -0.0301 -0.0402 324 ARG A CA  
2247  C C   . ARG A 332 ? 0.4486 0.2189 0.2083 -0.0301 -0.0251 -0.0356 324 ARG A C   
2248  O O   . ARG A 332 ? 0.4297 0.2139 0.2027 -0.0360 -0.0270 -0.0307 324 ARG A O   
2249  C CB  . ARG A 332 ? 0.4368 0.1585 0.1639 -0.0280 -0.0289 -0.0435 324 ARG A CB  
2250  C CG  . ARG A 332 ? 0.4277 0.1504 0.1647 -0.0292 -0.0299 -0.0390 324 ARG A CG  
2251  C CD  . ARG A 332 ? 0.5204 0.2219 0.2490 -0.0198 -0.0287 -0.0417 324 ARG A CD  
2252  N NE  . ARG A 332 ? 0.4789 0.1860 0.2131 -0.0048 -0.0216 -0.0443 324 ARG A NE  
2253  C CZ  . ARG A 332 ? 0.4305 0.1559 0.1831 0.0020  -0.0170 -0.0410 324 ARG A CZ  
2254  N NH1 . ARG A 332 ? 0.4257 0.1651 0.1925 -0.0041 -0.0186 -0.0350 324 ARG A NH1 
2255  N NH2 . ARG A 332 ? 0.4567 0.1869 0.2133 0.0149  -0.0107 -0.0439 324 ARG A NH2 
2256  N N   . ARG A 333 ? 0.3806 0.1573 0.1441 -0.0194 -0.0186 -0.0372 325 ARG A N   
2257  C CA  . ARG A 333 ? 0.3550 0.1525 0.1380 -0.0139 -0.0136 -0.0332 325 ARG A CA  
2258  C C   . ARG A 333 ? 0.3368 0.1555 0.1306 -0.0190 -0.0145 -0.0294 325 ARG A C   
2259  O O   . ARG A 333 ? 0.3440 0.1788 0.1539 -0.0197 -0.0138 -0.0249 325 ARG A O   
2260  C CB  . ARG A 333 ? 0.3583 0.1557 0.1413 -0.0016 -0.0064 -0.0362 325 ARG A CB  
2261  C CG  . ARG A 333 ? 0.3762 0.1572 0.1540 0.0059  -0.0051 -0.0390 325 ARG A CG  
2262  C CD  . ARG A 333 ? 0.4238 0.2035 0.1985 0.0180  0.0018  -0.0435 325 ARG A CD  
2263  N NE  . ARG A 333 ? 0.3530 0.1556 0.1432 0.0219  0.0077  -0.0407 325 ARG A NE  
2264  C CZ  . ARG A 333 ? 0.3931 0.2018 0.1859 0.0315  0.0146  -0.0432 325 ARG A CZ  
2265  N NH1 . ARG A 333 ? 0.3856 0.1798 0.1671 0.0397  0.0168  -0.0490 325 ARG A NH1 
2266  N NH2 . ARG A 333 ? 0.3728 0.2020 0.1793 0.0329  0.0194  -0.0400 325 ARG A NH2 
2267  N N   . MET A 334 ? 0.3718 0.1900 0.1562 -0.0221 -0.0164 -0.0312 326 MET A N   
2268  C CA  . MET A 334 ? 0.3541 0.1910 0.1477 -0.0267 -0.0185 -0.0276 326 MET A CA  
2269  C C   . MET A 334 ? 0.3605 0.2041 0.1605 -0.0367 -0.0247 -0.0245 326 MET A C   
2270  O O   . MET A 334 ? 0.3594 0.2219 0.1732 -0.0386 -0.0256 -0.0206 326 MET A O   
2271  C CB  . MET A 334 ? 0.3423 0.1762 0.1230 -0.0280 -0.0200 -0.0300 326 MET A CB  
2272  C CG  . MET A 334 ? 0.3638 0.1969 0.1401 -0.0189 -0.0132 -0.0321 326 MET A CG  
2273  S SD  . MET A 334 ? 0.3701 0.2247 0.1659 -0.0129 -0.0073 -0.0271 326 MET A SD  
2274  C CE  . MET A 334 ? 0.3154 0.1862 0.1195 -0.0202 -0.0137 -0.0224 326 MET A CE  
2275  N N   . ASP A 335 ? 0.3522 0.1804 0.1417 -0.0433 -0.0291 -0.0264 327 ASP A N   
2276  C CA  . ASP A 335 ? 0.3702 0.2043 0.1653 -0.0538 -0.0345 -0.0235 327 ASP A CA  
2277  C C   . ASP A 335 ? 0.4131 0.2533 0.2214 -0.0522 -0.0320 -0.0200 327 ASP A C   
2278  O O   . ASP A 335 ? 0.4154 0.2621 0.2292 -0.0608 -0.0355 -0.0173 327 ASP A O   
2279  C CB  . ASP A 335 ? 0.3745 0.1879 0.1520 -0.0626 -0.0401 -0.0264 327 ASP A CB  
2280  C CG  . ASP A 335 ? 0.4533 0.2646 0.2192 -0.0683 -0.0447 -0.0290 327 ASP A CG  
2281  O OD1 . ASP A 335 ? 0.4378 0.2655 0.2103 -0.0662 -0.0443 -0.0279 327 ASP A OD1 
2282  O OD2 . ASP A 335 ? 0.4963 0.2881 0.2454 -0.0749 -0.0492 -0.0322 327 ASP A OD2 
2283  N N   . LYS A 336 ? 0.3700 0.2087 0.1830 -0.0419 -0.0262 -0.0202 328 LYS A N   
2284  C CA  . LYS A 336 ? 0.3739 0.2189 0.1993 -0.0395 -0.0238 -0.0169 328 LYS A CA  
2285  C C   . LYS A 336 ? 0.4457 0.2749 0.2635 -0.0457 -0.0274 -0.0166 328 LYS A C   
2286  O O   . LYS A 336 ? 0.4385 0.2758 0.2650 -0.0508 -0.0285 -0.0130 328 LYS A O   
2287  C CB  . LYS A 336 ? 0.3945 0.2640 0.2373 -0.0420 -0.0236 -0.0127 328 LYS A CB  
2288  C CG  . LYS A 336 ? 0.3941 0.2770 0.2429 -0.0364 -0.0208 -0.0125 328 LYS A CG  
2289  C CD  . LYS A 336 ? 0.4407 0.3458 0.3049 -0.0386 -0.0216 -0.0088 328 LYS A CD  
2290  C CE  . LYS A 336 ? 0.4420 0.3571 0.3098 -0.0329 -0.0194 -0.0084 328 LYS A CE  
2291  N NZ  . LYS A 336 ? 0.3775 0.3125 0.2591 -0.0337 -0.0206 -0.0051 328 LYS A NZ  
2292  N N   . LYS A 337 ? 0.3918 0.1973 0.1920 -0.0451 -0.0291 -0.0206 329 LYS A N   
2293  C CA  . LYS A 337 ? 0.4720 0.2574 0.2611 -0.0506 -0.0330 -0.0206 329 LYS A CA  
2294  C C   . LYS A 337 ? 0.5110 0.2796 0.2947 -0.0394 -0.0300 -0.0226 329 LYS A C   
2295  O O   . LYS A 337 ? 0.4318 0.1984 0.2137 -0.0289 -0.0257 -0.0261 329 LYS A O   
2296  C CB  . LYS A 337 ? 0.5180 0.2859 0.2885 -0.0597 -0.0387 -0.0238 329 LYS A CB  
2297  C CG  . LYS A 337 ? 0.5459 0.3299 0.3204 -0.0709 -0.0426 -0.0223 329 LYS A CG  
2298  C CD  . LYS A 337 ? 0.6080 0.3726 0.3626 -0.0801 -0.0486 -0.0258 329 LYS A CD  
2299  C CE  . LYS A 337 ? 0.6184 0.4002 0.3776 -0.0927 -0.0536 -0.0240 329 LYS A CE  
2300  N NZ  . LYS A 337 ? 0.6348 0.4041 0.3816 -0.1010 -0.0581 -0.0246 329 LYS A NZ  
2301  N N   . LEU A 338 ? 0.4505 0.2072 0.2312 -0.0419 -0.0323 -0.0205 330 LEU A N   
2302  C CA  . LEU A 338 ? 0.4537 0.1935 0.2288 -0.0312 -0.0306 -0.0222 330 LEU A CA  
2303  C C   . LEU A 338 ? 0.5250 0.2340 0.2771 -0.0312 -0.0343 -0.0270 330 LEU A C   
2304  O O   . LEU A 338 ? 0.4890 0.1880 0.2291 -0.0424 -0.0392 -0.0278 330 LEU A O   
2305  C CB  . LEU A 338 ? 0.4756 0.2159 0.2572 -0.0332 -0.0319 -0.0173 330 LEU A CB  
2306  C CG  . LEU A 338 ? 0.4636 0.2301 0.2665 -0.0289 -0.0274 -0.0136 330 LEU A CG  
2307  C CD1 . LEU A 338 ? 0.5279 0.2917 0.3340 -0.0311 -0.0291 -0.0092 330 LEU A CD1 
2308  C CD2 . LEU A 338 ? 0.5237 0.2973 0.3337 -0.0147 -0.0216 -0.0163 330 LEU A CD2 
2309  N N   . PRO A 339 ? 0.5073 0.2005 0.2525 -0.0186 -0.0322 -0.0304 331 PRO A N   
2310  C CA  . PRO A 339 ? 0.5664 0.2377 0.2951 -0.0168 -0.0351 -0.0330 331 PRO A CA  
2311  C C   . PRO A 339 ? 0.5414 0.2009 0.2628 -0.0276 -0.0412 -0.0286 331 PRO A C   
2312  O O   . PRO A 339 ? 0.5260 0.1899 0.2546 -0.0313 -0.0424 -0.0240 331 PRO A O   
2313  C CB  . PRO A 339 ? 0.5772 0.2435 0.3075 -0.0001 -0.0312 -0.0356 331 PRO A CB  
2314  C CG  . PRO A 339 ? 0.5786 0.2642 0.3241 0.0070  -0.0253 -0.0360 331 PRO A CG  
2315  C CD  . PRO A 339 ? 0.5512 0.2559 0.3097 -0.0046 -0.0265 -0.0303 331 PRO A CD  
2316  N N   . GLU A 340 ? 0.5570 0.2016 0.2636 -0.0329 -0.0450 -0.0300 332 GLU A N   
2317  C CA  . GLU A 340 ? 0.5998 0.2333 0.2976 -0.0447 -0.0508 -0.0258 332 GLU A CA  
2318  C C   . GLU A 340 ? 0.6769 0.2991 0.3727 -0.0394 -0.0522 -0.0231 332 GLU A C   
2319  O O   . GLU A 340 ? 0.7004 0.3209 0.3948 -0.0494 -0.0558 -0.0181 332 GLU A O   
2320  C CB  . GLU A 340 ? 0.6851 0.3019 0.3658 -0.0491 -0.0543 -0.0284 332 GLU A CB  
2321  N N   . ASN A 341 ? 0.6843 0.3003 0.3805 -0.0238 -0.0494 -0.0261 333 ASN A N   
2322  C CA  . ASN A 341 ? 0.7451 0.3496 0.4385 -0.0176 -0.0514 -0.0239 333 ASN A CA  
2323  C C   . ASN A 341 ? 0.7107 0.3308 0.4208 -0.0121 -0.0485 -0.0210 333 ASN A C   
2324  O O   . ASN A 341 ? 0.7158 0.3298 0.4264 -0.0027 -0.0490 -0.0202 333 ASN A O   
2325  C CB  . ASN A 341 ? 0.7975 0.3862 0.4813 -0.0034 -0.0507 -0.0288 333 ASN A CB  
2326  C CG  . ASN A 341 ? 0.8731 0.4754 0.5694 0.0118  -0.0442 -0.0328 333 ASN A CG  
2327  O OD1 . ASN A 341 ? 0.8432 0.4632 0.5502 0.0109  -0.0400 -0.0337 333 ASN A OD1 
2328  N ND2 . ASN A 341 ? 0.9465 0.5416 0.6416 0.0258  -0.0434 -0.0351 333 ASN A ND2 
2329  N N   . PHE A 342 ? 0.6155 0.2555 0.3390 -0.0178 -0.0458 -0.0193 334 PHE A N   
2330  C CA  . PHE A 342 ? 0.5938 0.2487 0.3333 -0.0112 -0.0423 -0.0171 334 PHE A CA  
2331  C C   . PHE A 342 ? 0.5634 0.2134 0.3030 -0.0132 -0.0457 -0.0119 334 PHE A C   
2332  O O   . PHE A 342 ? 0.5628 0.2137 0.3083 -0.0018 -0.0445 -0.0115 334 PHE A O   
2333  C CB  . PHE A 342 ? 0.5084 0.1836 0.2605 -0.0188 -0.0397 -0.0158 334 PHE A CB  
2334  C CG  . PHE A 342 ? 0.4942 0.1873 0.2638 -0.0111 -0.0354 -0.0137 334 PHE A CG  
2335  C CD1 . PHE A 342 ? 0.4569 0.1597 0.2351 0.0033  -0.0301 -0.0171 334 PHE A CD1 
2336  C CD2 . PHE A 342 ? 0.4454 0.1523 0.2257 -0.0183 -0.0361 -0.0078 334 PHE A CD2 
2337  C CE1 . PHE A 342 ? 0.4395 0.1648 0.2366 0.0099  -0.0260 -0.0146 334 PHE A CE1 
2338  C CE2 . PHE A 342 ? 0.4753 0.2040 0.2740 -0.0110 -0.0319 -0.0055 334 PHE A CE2 
2339  C CZ  . PHE A 342 ? 0.4580 0.1956 0.2651 0.0028  -0.0271 -0.0088 334 PHE A CZ  
2340  N N   . ASP A 343 ? 0.5207 0.1670 0.2540 -0.0277 -0.0499 -0.0078 335 ASP A N   
2341  C CA  . ASP A 343 ? 0.5870 0.2309 0.3203 -0.0311 -0.0528 -0.0025 335 ASP A CA  
2342  C C   . ASP A 343 ? 0.6447 0.2681 0.3664 -0.0216 -0.0559 -0.0035 335 ASP A C   
2343  O O   . ASP A 343 ? 0.5812 0.2051 0.3074 -0.0152 -0.0565 -0.0011 335 ASP A O   
2344  C CB  . ASP A 343 ? 0.6701 0.3157 0.3984 -0.0491 -0.0561 0.0017  335 ASP A CB  
2345  C CG  . ASP A 343 ? 0.7404 0.4099 0.4831 -0.0583 -0.0532 0.0036  335 ASP A CG  
2346  O OD1 . ASP A 343 ? 0.7505 0.4343 0.5075 -0.0520 -0.0493 0.0040  335 ASP A OD1 
2347  O OD2 . ASP A 343 ? 0.8077 0.4823 0.5476 -0.0719 -0.0549 0.0049  335 ASP A OD2 
2348  N N   . GLU A 344 ? 0.6176 0.2230 0.3240 -0.0206 -0.0583 -0.0069 336 GLU A N   
2349  C CA  . GLU A 344 ? 0.6378 0.2230 0.3324 -0.0110 -0.0614 -0.0083 336 GLU A CA  
2350  C C   . GLU A 344 ? 0.6043 0.1956 0.3092 0.0073  -0.0576 -0.0117 336 GLU A C   
2351  O O   . GLU A 344 ? 0.5894 0.1734 0.2929 0.0163  -0.0596 -0.0109 336 GLU A O   
2352  C CB  . GLU A 344 ? 0.6927 0.2575 0.3686 -0.0137 -0.0644 -0.0115 336 GLU A CB  
2353  N N   . TYR A 345 ? 0.5489 0.1547 0.2642 0.0129  -0.0521 -0.0154 337 TYR A N   
2354  C CA  . TYR A 345 ? 0.5797 0.1959 0.3068 0.0294  -0.0476 -0.0185 337 TYR A CA  
2355  C C   . TYR A 345 ? 0.5405 0.1703 0.2820 0.0322  -0.0470 -0.0141 337 TYR A C   
2356  O O   . TYR A 345 ? 0.5167 0.1466 0.2624 0.0443  -0.0472 -0.0145 337 TYR A O   
2357  C CB  . TYR A 345 ? 0.5340 0.1648 0.2694 0.0326  -0.0416 -0.0228 337 TYR A CB  
2358  C CG  . TYR A 345 ? 0.5323 0.1780 0.2817 0.0484  -0.0362 -0.0257 337 TYR A CG  
2359  C CD1 . TYR A 345 ? 0.5185 0.1582 0.2641 0.0615  -0.0348 -0.0305 337 TYR A CD1 
2360  C CD2 . TYR A 345 ? 0.5712 0.2379 0.3380 0.0499  -0.0324 -0.0234 337 TYR A CD2 
2361  C CE1 . TYR A 345 ? 0.5653 0.2216 0.3249 0.0753  -0.0297 -0.0331 337 TYR A CE1 
2362  C CE2 . TYR A 345 ? 0.5308 0.2130 0.3110 0.0637  -0.0275 -0.0258 337 TYR A CE2 
2363  C CZ  . TYR A 345 ? 0.5049 0.1827 0.2819 0.0760  -0.0260 -0.0306 337 TYR A CZ  
2364  O OH  . TYR A 345 ? 0.4862 0.1821 0.2775 0.0889  -0.0209 -0.0330 337 TYR A OH  
2365  N N   . VAL A 346 ? 0.4829 0.1252 0.2323 0.0211  -0.0464 -0.0099 338 VAL A N   
2366  C CA  . VAL A 346 ? 0.4720 0.1279 0.2349 0.0228  -0.0458 -0.0055 338 VAL A CA  
2367  C C   . VAL A 346 ? 0.5579 0.2008 0.3129 0.0221  -0.0513 -0.0018 338 VAL A C   
2368  O O   . VAL A 346 ? 0.5237 0.1716 0.2864 0.0312  -0.0515 -0.0003 338 VAL A O   
2369  C CB  . VAL A 346 ? 0.4421 0.1133 0.2137 0.0102  -0.0441 -0.0018 338 VAL A CB  
2370  C CG1 . VAL A 346 ? 0.4274 0.1099 0.2099 0.0099  -0.0444 0.0036  338 VAL A CG1 
2371  C CG2 . VAL A 346 ? 0.4661 0.1511 0.2468 0.0132  -0.0385 -0.0055 338 VAL A CG2 
2372  N N   . GLN A 347 ? 0.5327 0.1585 0.2716 0.0112  -0.0560 -0.0002 339 GLN A N   
2373  C CA  . GLN A 347 ? 0.6089 0.2205 0.3381 0.0096  -0.0614 0.0033  339 GLN A CA  
2374  C C   . GLN A 347 ? 0.5905 0.1905 0.3156 0.0256  -0.0630 0.0003  339 GLN A C   
2375  O O   . GLN A 347 ? 0.6006 0.1996 0.3280 0.0309  -0.0655 0.0030  339 GLN A O   
2376  C CB  . GLN A 347 ? 0.6228 0.2180 0.3344 -0.0050 -0.0659 0.0050  339 GLN A CB  
2377  N N   . THR A 348 ? 0.6386 0.2308 0.3581 0.0336  -0.0617 -0.0053 340 THR A N   
2378  C CA  . THR A 348 ? 0.6461 0.2299 0.3633 0.0496  -0.0626 -0.0087 340 THR A CA  
2379  C C   . THR A 348 ? 0.6361 0.2411 0.3732 0.0623  -0.0587 -0.0090 340 THR A C   
2380  O O   . THR A 348 ? 0.6123 0.2149 0.3511 0.0718  -0.0612 -0.0083 340 THR A O   
2381  C CB  . THR A 348 ? 0.7008 0.2747 0.4090 0.0550  -0.0610 -0.0150 340 THR A CB  
2382  O OG1 . THR A 348 ? 0.7377 0.2927 0.4275 0.0422  -0.0650 -0.0143 340 THR A OG1 
2383  C CG2 . THR A 348 ? 0.7625 0.3266 0.4668 0.0712  -0.0622 -0.0187 340 THR A CG2 
2384  N N   . ALA A 349 ? 0.5192 0.1454 0.2712 0.0623  -0.0528 -0.0101 341 ALA A N   
2385  C CA  . ALA A 349 ? 0.4978 0.1456 0.2689 0.0735  -0.0489 -0.0104 341 ALA A CA  
2386  C C   . ALA A 349 ? 0.4886 0.1428 0.2667 0.0708  -0.0518 -0.0043 341 ALA A C   
2387  O O   . ALA A 349 ? 0.5560 0.2199 0.3445 0.0817  -0.0517 -0.0040 341 ALA A O   
2388  C CB  . ALA A 349 ? 0.4866 0.1542 0.2703 0.0725  -0.0423 -0.0124 341 ALA A CB  
2389  N N   . LEU A 350 ? 0.4858 0.1362 0.2589 0.0560  -0.0542 0.0005  342 LEU A N   
2390  C CA  . LEU A 350 ? 0.4787 0.1346 0.2568 0.0522  -0.0569 0.0064  342 LEU A CA  
2391  C C   . LEU A 350 ? 0.5330 0.1738 0.3023 0.0589  -0.0625 0.0075  342 LEU A C   
2392  O O   . LEU A 350 ? 0.5461 0.1958 0.3246 0.0658  -0.0636 0.0098  342 LEU A O   
2393  C CB  . LEU A 350 ? 0.6026 0.2566 0.3749 0.0342  -0.0582 0.0109  342 LEU A CB  
2394  C CG  . LEU A 350 ? 0.5966 0.2602 0.3752 0.0278  -0.0596 0.0170  342 LEU A CG  
2395  C CD1 . LEU A 350 ? 0.5719 0.2594 0.3702 0.0338  -0.0550 0.0175  342 LEU A CD1 
2396  C CD2 . LEU A 350 ? 0.5431 0.2048 0.3146 0.0096  -0.0606 0.0207  342 LEU A CD2 
2397  N N   . LYS A 351 ? 0.5879 0.2053 0.3388 0.0570  -0.0664 0.0059  343 LYS A N   
2398  C CA  . LYS A 351 ? 0.6247 0.2251 0.3653 0.0639  -0.0721 0.0066  343 LYS A CA  
2399  C C   . LYS A 351 ? 0.6255 0.2347 0.3770 0.0823  -0.0707 0.0031  343 LYS A C   
2400  O O   . LYS A 351 ? 0.6474 0.2541 0.3997 0.0893  -0.0745 0.0051  343 LYS A O   
2401  C CB  . LYS A 351 ? 0.6670 0.2404 0.3854 0.0593  -0.0762 0.0048  343 LYS A CB  
2402  N N   . GLU A 352 ? 0.5806 0.2013 0.3409 0.0903  -0.0652 -0.0022 344 GLU A N   
2403  C CA  . GLU A 352 ? 0.6006 0.2336 0.3732 0.1073  -0.0630 -0.0058 344 GLU A CA  
2404  C C   . GLU A 352 ? 0.5776 0.2363 0.3707 0.1104  -0.0607 -0.0028 344 GLU A C   
2405  O O   . GLU A 352 ? 0.6186 0.2849 0.4201 0.1217  -0.0621 -0.0029 344 GLU A O   
2406  C CB  . GLU A 352 ? 0.5836 0.2221 0.3588 0.1139  -0.0573 -0.0124 344 GLU A CB  
2407  N N   . VAL A 353 ? 0.5306 0.2031 0.3321 0.1005  -0.0575 -0.0002 345 VAL A N   
2408  C CA  . VAL A 353 ? 0.5180 0.2135 0.3375 0.1020  -0.0558 0.0031  345 VAL A CA  
2409  C C   . VAL A 353 ? 0.5231 0.2122 0.3392 0.1007  -0.0620 0.0084  345 VAL A C   
2410  O O   . VAL A 353 ? 0.5163 0.2201 0.3450 0.1085  -0.0626 0.0099  345 VAL A O   
2411  C CB  . VAL A 353 ? 0.5035 0.2111 0.3293 0.0906  -0.0518 0.0051  345 VAL A CB  
2412  C CG1 . VAL A 353 ? 0.4662 0.1933 0.3069 0.0897  -0.0515 0.0097  345 VAL A CG1 
2413  C CG2 . VAL A 353 ? 0.4740 0.1920 0.3061 0.0943  -0.0452 -0.0003 345 VAL A CG2 
2414  N N   . CYS A 354 ? 0.5266 0.1942 0.3252 0.0904  -0.0667 0.0115  346 CYS A N   
2415  C CA  A CYS A 354 ? 0.5922 0.2520 0.3854 0.0884  -0.0727 0.0165  346 CYS A CA  
2416  C CA  B CYS A 354 ? 0.5925 0.2517 0.3853 0.0881  -0.0728 0.0166  346 CYS A CA  
2417  C C   . CYS A 354 ? 0.6279 0.2794 0.4184 0.1026  -0.0767 0.0146  346 CYS A C   
2418  O O   . CYS A 354 ? 0.6559 0.3128 0.4518 0.1072  -0.0800 0.0178  346 CYS A O   
2419  C CB  A CYS A 354 ? 0.6175 0.2571 0.3923 0.0732  -0.0763 0.0199  346 CYS A CB  
2420  C CB  B CYS A 354 ? 0.6176 0.2555 0.3911 0.0732  -0.0765 0.0197  346 CYS A CB  
2421  S SG  A CYS A 354 ? 0.5809 0.2353 0.3622 0.0568  -0.0722 0.0234  346 CYS A SG  
2422  S SG  B CYS A 354 ? 0.6376 0.2756 0.4081 0.0612  -0.0805 0.0275  346 CYS A SG  
2423  N N   . ALA A 355 ? 0.5860 0.2250 0.3684 0.1100  -0.0765 0.0094  347 ALA A N   
2424  C CA  . ALA A 355 ? 0.6331 0.2646 0.4131 0.1246  -0.0800 0.0070  347 ALA A CA  
2425  C C   . ALA A 355 ? 0.6524 0.3105 0.4543 0.1373  -0.0773 0.0059  347 ALA A C   
2426  O O   . ALA A 355 ? 0.7111 0.3678 0.5144 0.1481  -0.0812 0.0060  347 ALA A O   
2427  C CB  . ALA A 355 ? 0.5966 0.2123 0.3650 0.1303  -0.0791 0.0010  347 ALA A CB  
2428  N N   . LYS A 356 ? 0.5451 0.2277 0.3640 0.1361  -0.0708 0.0048  348 LYS A N   
2429  C CA  . LYS A 356 ? 0.5637 0.2734 0.4039 0.1471  -0.0680 0.0036  348 LYS A CA  
2430  C C   . LYS A 356 ? 0.6184 0.3400 0.4674 0.1435  -0.0710 0.0097  348 LYS A C   
2431  O O   . LYS A 356 ? 0.6091 0.3432 0.4690 0.1532  -0.0729 0.0101  348 LYS A O   
2432  C CB  . LYS A 356 ? 0.5747 0.3055 0.4287 0.1477  -0.0598 -0.0004 348 LYS A CB  
2433  N N   . ALA A 357 ? 0.6115 0.3300 0.4560 0.1294  -0.0714 0.0143  349 ALA A N   
2434  C CA  . ALA A 357 ? 0.5856 0.3130 0.4356 0.1242  -0.0744 0.0203  349 ALA A CA  
2435  C C   . ALA A 357 ? 0.5763 0.3335 0.4488 0.1323  -0.0718 0.0199  349 ALA A C   
2436  O O   . ALA A 357 ? 0.5085 0.2727 0.3870 0.1377  -0.0758 0.0225  349 ALA A O   
2437  C CB  . ALA A 357 ? 0.5828 0.2907 0.4192 0.1249  -0.0822 0.0239  349 ALA A CB  
2438  N N   . GLU A 358 ? 0.4212 0.1964 0.3061 0.1326  -0.0650 0.0166  350 GLU A N   
2439  C CA  . GLU A 358 ? 0.4875 0.2924 0.3941 0.1393  -0.0618 0.0157  350 GLU A CA  
2440  C C   . GLU A 358 ? 0.4778 0.2962 0.3919 0.1304  -0.0622 0.0208  350 GLU A C   
2441  O O   . GLU A 358 ? 0.4422 0.2547 0.3499 0.1190  -0.0608 0.0230  350 GLU A O   
2442  C CB  . GLU A 358 ? 0.5527 0.3715 0.4687 0.1430  -0.0541 0.0099  350 GLU A CB  
2443  C CG  . GLU A 358 ? 0.5745 0.3895 0.4891 0.1546  -0.0525 0.0041  350 GLU A CG  
2444  C CD  . GLU A 358 ? 0.6110 0.4439 0.5365 0.1575  -0.0443 -0.0012 350 GLU A CD  
2445  O OE1 . GLU A 358 ? 0.6039 0.4258 0.5200 0.1522  -0.0410 -0.0035 350 GLU A OE1 
2446  O OE2 . GLU A 358 ? 0.6261 0.4848 0.5697 0.1641  -0.0411 -0.0029 350 GLU A OE2 
2447  N N   . THR A 359 ? 0.4354 0.2727 0.3632 0.1355  -0.0641 0.0226  351 THR A N   
2448  C CA  . THR A 359 ? 0.4667 0.3214 0.4045 0.1287  -0.0639 0.0264  351 THR A CA  
2449  C C   . THR A 359 ? 0.4694 0.3515 0.4264 0.1329  -0.0573 0.0225  351 THR A C   
2450  O O   . THR A 359 ? 0.4740 0.3747 0.4451 0.1419  -0.0569 0.0205  351 THR A O   
2451  C CB  . THR A 359 ? 0.4562 0.3147 0.3960 0.1302  -0.0704 0.0310  351 THR A CB  
2452  O OG1 . THR A 359 ? 0.5334 0.3668 0.4541 0.1232  -0.0756 0.0351  351 THR A OG1 
2453  C CG2 . THR A 359 ? 0.4348 0.3154 0.3873 0.1249  -0.0699 0.0338  351 THR A CG2 
2454  N N   . VAL A 360 ? 0.4298 0.3143 0.3868 0.1261  -0.0521 0.0215  352 VAL A N   
2455  C CA  . VAL A 360 ? 0.3892 0.2980 0.3622 0.1279  -0.0453 0.0182  352 VAL A CA  
2456  C C   . VAL A 360 ? 0.3716 0.2859 0.3454 0.1170  -0.0436 0.0213  352 VAL A C   
2457  O O   . VAL A 360 ? 0.3942 0.2927 0.3556 0.1070  -0.0463 0.0249  352 VAL A O   
2458  C CB  . VAL A 360 ? 0.3918 0.2973 0.3629 0.1321  -0.0392 0.0123  352 VAL A CB  
2459  C CG1 . VAL A 360 ? 0.3356 0.2395 0.3078 0.1434  -0.0401 0.0086  352 VAL A CG1 
2460  C CG2 . VAL A 360 ? 0.3373 0.2172 0.2899 0.1244  -0.0393 0.0128  352 VAL A CG2 
2461  N N   . ALA A 361 ? 0.3206 0.2609 0.3108 0.1143  -0.0373 0.0193  353 ALA A N   
2462  C CA  . ALA A 361 ? 0.2968 0.2446 0.2890 0.1002  -0.0329 0.0206  353 ALA A CA  
2463  C C   . ALA A 361 ? 0.3474 0.2795 0.3281 0.0944  -0.0292 0.0189  353 ALA A C   
2464  O O   . ALA A 361 ? 0.3038 0.2283 0.2805 0.1013  -0.0271 0.0150  353 ALA A O   
2465  C CB  . ALA A 361 ? 0.3189 0.2950 0.3292 0.0990  -0.0269 0.0185  353 ALA A CB  
2466  N N   . THR A 362 ? 0.2600 0.1881 0.2353 0.0817  -0.0285 0.0214  354 THR A N   
2467  C CA  . THR A 362 ? 0.3302 0.2443 0.2948 0.0763  -0.0257 0.0198  354 THR A CA  
2468  C C   . THR A 362 ? 0.3496 0.2771 0.3223 0.0761  -0.0183 0.0158  354 THR A C   
2469  O O   . THR A 362 ? 0.3468 0.2630 0.3109 0.0741  -0.0162 0.0136  354 THR A O   
2470  C CB  . THR A 362 ? 0.2709 0.1768 0.2268 0.0632  -0.0271 0.0234  354 THR A CB  
2471  O OG1 . THR A 362 ? 0.2973 0.2220 0.2638 0.0566  -0.0248 0.0250  354 THR A OG1 
2472  C CG2 . THR A 362 ? 0.2472 0.1332 0.1896 0.0629  -0.0343 0.0273  354 THR A CG2 
2473  N N   . ARG A 363 ? 0.2960 0.2464 0.2841 0.0777  -0.0146 0.0148  355 ARG A N   
2474  C CA  . ARG A 363 ? 0.2805 0.2416 0.2746 0.0791  -0.0078 0.0109  355 ARG A CA  
2475  C C   . ARG A 363 ? 0.2530 0.2075 0.2439 0.0907  -0.0070 0.0069  355 ARG A C   
2476  O O   . ARG A 363 ? 0.3410 0.2929 0.3282 0.0911  -0.0025 0.0035  355 ARG A O   
2477  C CB  . ARG A 363 ? 0.2783 0.2646 0.2886 0.0776  -0.0041 0.0110  355 ARG A CB  
2478  C CG  . ARG A 363 ? 0.3196 0.3193 0.3408 0.0861  -0.0065 0.0111  355 ARG A CG  
2479  C CD  . ARG A 363 ? 0.2989 0.3240 0.3357 0.0841  -0.0018 0.0103  355 ARG A CD  
2480  N NE  . ARG A 363 ? 0.3324 0.3724 0.3806 0.0916  -0.0045 0.0105  355 ARG A NE  
2481  C CZ  . ARG A 363 ? 0.4146 0.4780 0.4772 0.0925  -0.0008 0.0092  355 ARG A CZ  
2482  N NH1 . ARG A 363 ? 0.3019 0.3746 0.3681 0.0862  0.0058  0.0079  355 ARG A NH1 
2483  N NH2 . ARG A 363 ? 0.3980 0.4757 0.4713 0.0993  -0.0041 0.0094  355 ARG A NH2 
2484  N N   . LYS A 364 ? 0.2998 0.2508 0.2910 0.1006  -0.0116 0.0070  356 LYS A N   
2485  C CA  . LYS A 364 ? 0.3302 0.2715 0.3161 0.1129  -0.0116 0.0027  356 LYS A CA  
2486  C C   . LYS A 364 ? 0.3842 0.2957 0.3504 0.1112  -0.0149 0.0025  356 LYS A C   
2487  O O   . LYS A 364 ? 0.3130 0.2146 0.2716 0.1160  -0.0124 -0.0018 356 LYS A O   
2488  C CB  . LYS A 364 ? 0.3842 0.3316 0.3771 0.1251  -0.0160 0.0029  356 LYS A CB  
2489  C CG  . LYS A 364 ? 0.4821 0.4214 0.4707 0.1365  -0.0158 -0.0019 356 LYS A CG  
2490  C CD  . LYS A 364 ? 0.5261 0.4786 0.5205 0.1389  -0.0074 -0.0072 356 LYS A CD  
2491  C CE  . LYS A 364 ? 0.5456 0.4889 0.5340 0.1477  -0.0069 -0.0121 356 LYS A CE  
2492  N NZ  . LYS A 364 ? 0.5017 0.4538 0.4919 0.1489  0.0012  -0.0172 356 LYS A NZ  
2493  N N   . ALA A 365 ? 0.4387 0.3357 0.3956 0.1036  -0.0205 0.0071  357 ALA A N   
2494  C CA  . ALA A 365 ? 0.3624 0.2324 0.3005 0.0986  -0.0234 0.0074  357 ALA A CA  
2495  C C   . ALA A 365 ? 0.3614 0.2322 0.2967 0.0903  -0.0179 0.0052  357 ALA A C   
2496  O O   . ALA A 365 ? 0.3617 0.2137 0.2835 0.0902  -0.0183 0.0027  357 ALA A O   
2497  C CB  . ALA A 365 ? 0.4246 0.2836 0.3550 0.0896  -0.0292 0.0132  357 ALA A CB  
2498  N N   . SER A 366 ? 0.3471 0.2389 0.2944 0.0832  -0.0132 0.0060  358 SER A N   
2499  C CA  . SER A 366 ? 0.3737 0.2685 0.3197 0.0763  -0.0082 0.0039  358 SER A CA  
2500  C C   . SER A 366 ? 0.3862 0.2812 0.3312 0.0850  -0.0038 -0.0016 358 SER A C   
2501  O O   . SER A 366 ? 0.3472 0.2283 0.2806 0.0830  -0.0030 -0.0041 358 SER A O   
2502  C CB  . SER A 366 ? 0.2777 0.1946 0.2369 0.0688  -0.0044 0.0059  358 SER A CB  
2503  O OG  . SER A 366 ? 0.2761 0.1957 0.2337 0.0630  0.0000  0.0041  358 SER A OG  
2504  N N   . GLN A 367 ? 0.3301 0.2415 0.2872 0.0944  -0.0009 -0.0036 359 GLN A N   
2505  C CA  . GLN A 367 ? 0.3364 0.2504 0.2932 0.1031  0.0040  -0.0091 359 GLN A CA  
2506  C C   . GLN A 367 ? 0.3952 0.2840 0.3361 0.1109  0.0005  -0.0123 359 GLN A C   
2507  O O   . GLN A 367 ? 0.3148 0.1958 0.2473 0.1134  0.0038  -0.0168 359 GLN A O   
2508  C CB  . GLN A 367 ? 0.3390 0.2766 0.3122 0.1119  0.0072  -0.0104 359 GLN A CB  
2509  C CG  . GLN A 367 ? 0.2963 0.2416 0.2713 0.1202  0.0136  -0.0161 359 GLN A CG  
2510  C CD  . GLN A 367 ? 0.4278 0.4000 0.4207 0.1272  0.0172  -0.0171 359 GLN A CD  
2511  O OE1 . GLN A 367 ? 0.4192 0.3978 0.4201 0.1319  0.0130  -0.0150 359 GLN A OE1 
2512  N NE2 . GLN A 367 ? 0.3964 0.3854 0.3956 0.1271  0.0249  -0.0200 359 GLN A NE2 
2513  N N   . ASN A 368 ? 0.3685 0.2429 0.3037 0.1149  -0.0063 -0.0100 360 ASN A N   
2514  C CA  . ASN A 368 ? 0.3643 0.2116 0.2824 0.1202  -0.0105 -0.0124 360 ASN A CA  
2515  C C   . ASN A 368 ? 0.3840 0.2096 0.2851 0.1099  -0.0119 -0.0122 360 ASN A C   
2516  O O   . ASN A 368 ? 0.3600 0.1701 0.2487 0.1117  -0.0118 -0.0162 360 ASN A O   
2517  C CB  . ASN A 368 ? 0.4360 0.2748 0.3521 0.1225  -0.0179 -0.0088 360 ASN A CB  
2518  C CG  . ASN A 368 ? 0.4895 0.3483 0.4211 0.1330  -0.0174 -0.0098 360 ASN A CG  
2519  O OD1 . ASN A 368 ? 0.4610 0.3382 0.4034 0.1391  -0.0115 -0.0138 360 ASN A OD1 
2520  N ND2 . ASN A 368 ? 0.4765 0.3320 0.4088 0.1344  -0.0236 -0.0059 360 ASN A ND2 
2521  N N   . SER A 369 ? 0.3497 0.1783 0.2519 0.0963  -0.0133 -0.0073 361 SER A N   
2522  C CA  . SER A 369 ? 0.3691 0.1825 0.2580 0.0845  -0.0145 -0.0068 361 SER A CA  
2523  C C   . SER A 369 ? 0.3443 0.1651 0.2337 0.0828  -0.0085 -0.0110 361 SER A C   
2524  O O   . SER A 369 ? 0.3770 0.1802 0.2519 0.0792  -0.0095 -0.0134 361 SER A O   
2525  C CB  . SER A 369 ? 0.3012 0.1217 0.1942 0.0712  -0.0163 -0.0010 361 SER A CB  
2526  O OG  . SER A 369 ? 0.3350 0.1477 0.2256 0.0717  -0.0219 0.0032  361 SER A OG  
2527  N N   . ILE A 370 ? 0.2896 0.1356 0.1946 0.0843  -0.0026 -0.0116 362 ILE A N   
2528  C CA  . ILE A 370 ? 0.3375 0.1909 0.2426 0.0832  0.0032  -0.0153 362 ILE A CA  
2529  C C   . ILE A 370 ? 0.3062 0.1456 0.2004 0.0935  0.0045  -0.0214 362 ILE A C   
2530  O O   . ILE A 370 ? 0.3517 0.1801 0.2341 0.0904  0.0055  -0.0245 362 ILE A O   
2531  C CB  . ILE A 370 ? 0.3077 0.1894 0.2307 0.0837  0.0092  -0.0146 362 ILE A CB  
2532  C CG1 . ILE A 370 ? 0.3110 0.2039 0.2424 0.0729  0.0080  -0.0093 362 ILE A CG1 
2533  C CG2 . ILE A 370 ? 0.3326 0.2208 0.2541 0.0835  0.0152  -0.0184 362 ILE A CG2 
2534  C CD1 . ILE A 370 ? 0.2506 0.1688 0.1992 0.0737  0.0122  -0.0079 362 ILE A CD1 
2535  N N   . GLU A 371 ? 0.3278 0.1675 0.2253 0.1064  0.0041  -0.0234 363 GLU A N   
2536  C CA  . GLU A 371 ? 0.3366 0.1646 0.2246 0.1165  0.0052  -0.0294 363 GLU A CA  
2537  C C   . GLU A 371 ? 0.4123 0.2112 0.2801 0.1113  -0.0003 -0.0301 363 GLU A C   
2538  O O   . GLU A 371 ? 0.4194 0.2094 0.2765 0.1109  0.0015  -0.0344 363 GLU A O   
2539  C CB  . GLU A 371 ? 0.3714 0.2089 0.2695 0.1271  0.0039  -0.0297 363 GLU A CB  
2540  C CG  . GLU A 371 ? 0.4305 0.2647 0.3242 0.1362  0.0058  -0.0354 363 GLU A CG  
2541  C CD  . GLU A 371 ? 0.4637 0.3210 0.3682 0.1400  0.0143  -0.0392 363 GLU A CD  
2542  O OE1 . GLU A 371 ? 0.4984 0.3802 0.4199 0.1407  0.0178  -0.0373 363 GLU A OE1 
2543  O OE2 . GLU A 371 ? 0.5566 0.4076 0.4519 0.1414  0.0174  -0.0439 363 GLU A OE2 
2544  N N   . ILE A 372 ? 0.3656 0.1499 0.2274 0.1061  -0.0072 -0.0256 364 ILE A N   
2545  C CA  . ILE A 372 ? 0.3878 0.1454 0.2305 0.0994  -0.0128 -0.0254 364 ILE A CA  
2546  C C   . ILE A 372 ? 0.4722 0.2231 0.3058 0.0887  -0.0115 -0.0264 364 ILE A C   
2547  O O   . ILE A 372 ? 0.4928 0.2285 0.3123 0.0865  -0.0125 -0.0297 364 ILE A O   
2548  C CB  . ILE A 372 ? 0.3924 0.1392 0.2318 0.0938  -0.0198 -0.0196 364 ILE A CB  
2549  C CG1 . ILE A 372 ? 0.4842 0.2344 0.3299 0.1047  -0.0222 -0.0190 364 ILE A CG1 
2550  C CG2 . ILE A 372 ? 0.5248 0.2461 0.3447 0.0839  -0.0251 -0.0188 364 ILE A CG2 
2551  C CD1 . ILE A 372 ? 0.4475 0.1917 0.2922 0.0996  -0.0283 -0.0128 364 ILE A CD1 
2552  N N   . LEU A 373 ? 0.4190 0.1855 0.2623 0.0800  -0.0095 -0.0229 365 LEU A N   
2553  C CA  . LEU A 373 ? 0.4608 0.2277 0.2992 0.0675  -0.0088 -0.0227 365 LEU A CA  
2554  C C   . LEU A 373 ? 0.4593 0.2316 0.2958 0.0716  -0.0032 -0.0282 365 LEU A C   
2555  O O   . LEU A 373 ? 0.4067 0.1673 0.2305 0.0652  -0.0042 -0.0304 365 LEU A O   
2556  C CB  . LEU A 373 ? 0.4575 0.2462 0.3104 0.0573  -0.0078 -0.0173 365 LEU A CB  
2557  C CG  . LEU A 373 ? 0.5856 0.3650 0.4321 0.0441  -0.0132 -0.0127 365 LEU A CG  
2558  C CD1 . LEU A 373 ? 0.6015 0.3615 0.4393 0.0467  -0.0189 -0.0106 365 LEU A CD1 
2559  C CD2 . LEU A 373 ? 0.5532 0.3564 0.4154 0.0363  -0.0113 -0.0081 365 LEU A CD2 
2560  N N   . ALA A 374 ? 0.4245 0.2153 0.2733 0.0815  0.0027  -0.0304 366 ALA A N   
2561  C CA  . ALA A 374 ? 0.4084 0.2068 0.2560 0.0850  0.0089  -0.0352 366 ALA A CA  
2562  C C   . ALA A 374 ? 0.4745 0.2490 0.3029 0.0908  0.0078  -0.0414 366 ALA A C   
2563  O O   . ALA A 374 ? 0.4075 0.1801 0.2278 0.0880  0.0105  -0.0449 366 ALA A O   
2564  C CB  . ALA A 374 ? 0.3516 0.1741 0.2157 0.0944  0.0154  -0.0362 366 ALA A CB  
2565  N N   . LYS A 375 ? 0.4542 0.2166 0.2787 0.0961  0.0034  -0.0415 367 LYS A N   
2566  C CA  . LYS A 375 ? 0.4669 0.2116 0.2765 0.0987  0.0015  -0.0457 367 LYS A CA  
2567  C C   . LYS A 375 ? 0.5101 0.2359 0.3031 0.0864  -0.0026 -0.0455 367 LYS A C   
2568  O O   . LYS A 375 ? 0.5307 0.2472 0.3120 0.0861  -0.0021 -0.0496 367 LYS A O   
2569  C CB  . LYS A 375 ? 0.4590 0.1918 0.2658 0.1057  -0.0034 -0.0451 367 LYS A CB  
2570  C CG  . LYS A 375 ? 0.5938 0.3435 0.4146 0.1192  0.0003  -0.0469 367 LYS A CG  
2571  C CD  . LYS A 375 ? 0.6882 0.4216 0.4998 0.1276  -0.0034 -0.0495 367 LYS A CD  
2572  C CE  . LYS A 375 ? 0.7576 0.4672 0.5565 0.1213  -0.0120 -0.0456 367 LYS A CE  
2573  N NZ  . LYS A 375 ? 0.8462 0.5368 0.6329 0.1290  -0.0158 -0.0483 367 LYS A NZ  
2574  N N   . GLU A 376 ? 0.4932 0.2146 0.2855 0.0756  -0.0069 -0.0406 368 GLU A N   
2575  C CA  . GLU A 376 ? 0.5495 0.2546 0.3275 0.0623  -0.0118 -0.0396 368 GLU A CA  
2576  C C   . GLU A 376 ? 0.4769 0.1919 0.2562 0.0538  -0.0091 -0.0401 368 GLU A C   
2577  O O   . GLU A 376 ? 0.4832 0.1881 0.2504 0.0448  -0.0117 -0.0413 368 GLU A O   
2578  C CB  . GLU A 376 ? 0.6151 0.3110 0.3917 0.0543  -0.0181 -0.0338 368 GLU A CB  
2579  C CG  . GLU A 376 ? 0.6590 0.3443 0.4250 0.0383  -0.0229 -0.0315 368 GLU A CG  
2580  C CD  . GLU A 376 ? 0.6844 0.3485 0.4325 0.0351  -0.0273 -0.0335 368 GLU A CD  
2581  O OE1 . GLU A 376 ? 0.6795 0.3366 0.4226 0.0459  -0.0260 -0.0376 368 GLU A OE1 
2582  O OE2 . GLU A 376 ? 0.6949 0.3501 0.4343 0.0216  -0.0321 -0.0310 368 GLU A OE2 
2583  N N   . LEU A 377 ? 0.4509 0.1926 0.2487 0.0551  -0.0040 -0.0376 369 LEU A N   
2584  C CA  . LEU A 377 ? 0.4218 0.1822 0.2272 0.0458  -0.0019 -0.0354 369 LEU A CA  
2585  C C   . LEU A 377 ? 0.3878 0.1640 0.1991 0.0531  0.0055  -0.0387 369 LEU A C   
2586  O O   . LEU A 377 ? 0.3430 0.1412 0.1710 0.0564  0.0099  -0.0363 369 LEU A O   
2587  C CB  . LEU A 377 ? 0.3807 0.1596 0.2027 0.0390  -0.0027 -0.0287 369 LEU A CB  
2588  C CG  . LEU A 377 ? 0.4119 0.1785 0.2296 0.0310  -0.0092 -0.0247 369 LEU A CG  
2589  C CD1 . LEU A 377 ? 0.3794 0.1670 0.2141 0.0251  -0.0089 -0.0187 369 LEU A CD1 
2590  C CD2 . LEU A 377 ? 0.4104 0.1604 0.2121 0.0200  -0.0141 -0.0257 369 LEU A CD2 
2591  N N   . PRO A 378 ? 0.4286 0.1943 0.2258 0.0549  0.0070  -0.0441 370 PRO A N   
2592  C CA  . PRO A 378 ? 0.4010 0.1825 0.2027 0.0602  0.0142  -0.0468 370 PRO A CA  
2593  C C   . PRO A 378 ? 0.3850 0.1885 0.1989 0.0520  0.0161  -0.0422 370 PRO A C   
2594  O O   . PRO A 378 ? 0.4019 0.2220 0.2234 0.0558  0.0223  -0.0427 370 PRO A O   
2595  C CB  . PRO A 378 ? 0.4723 0.2346 0.2532 0.0611  0.0139  -0.0532 370 PRO A CB  
2596  C CG  . PRO A 378 ? 0.4230 0.1657 0.1914 0.0503  0.0057  -0.0519 370 PRO A CG  
2597  C CD  . PRO A 378 ? 0.4062 0.1459 0.1822 0.0500  0.0018  -0.0475 370 PRO A CD  
2598  N N   . GLU A 379 ? 0.3687 0.1729 0.1846 0.0408  0.0109  -0.0377 371 GLU A N   
2599  C CA  . GLU A 379 ? 0.3637 0.1881 0.1913 0.0341  0.0120  -0.0334 371 GLU A CA  
2600  C C   . GLU A 379 ? 0.3590 0.2023 0.2056 0.0369  0.0149  -0.0292 371 GLU A C   
2601  O O   . GLU A 379 ? 0.3322 0.1920 0.1887 0.0329  0.0166  -0.0259 371 GLU A O   
2602  C CB  . GLU A 379 ? 0.3537 0.1746 0.1781 0.0220  0.0056  -0.0303 371 GLU A CB  
2603  C CG  . GLU A 379 ? 0.3958 0.2097 0.2225 0.0181  0.0007  -0.0274 371 GLU A CG  
2604  C CD  . GLU A 379 ? 0.4317 0.2197 0.2403 0.0161  -0.0043 -0.0304 371 GLU A CD  
2605  O OE1 . GLU A 379 ? 0.4291 0.2030 0.2269 0.0242  -0.0025 -0.0354 371 GLU A OE1 
2606  O OE2 . GLU A 379 ? 0.4689 0.2506 0.2738 0.0061  -0.0098 -0.0280 371 GLU A OE2 
2607  N N   . LEU A 380 ? 0.3323 0.1729 0.1836 0.0437  0.0152  -0.0293 372 LEU A N   
2608  C CA  . LEU A 380 ? 0.2787 0.1362 0.1474 0.0452  0.0168  -0.0251 372 LEU A CA  
2609  C C   . LEU A 380 ? 0.2967 0.1731 0.1753 0.0494  0.0236  -0.0254 372 LEU A C   
2610  O O   . LEU A 380 ? 0.3530 0.2289 0.2272 0.0565  0.0281  -0.0296 372 LEU A O   
2611  C CB  . LEU A 380 ? 0.2949 0.1443 0.1647 0.0522  0.0150  -0.0255 372 LEU A CB  
2612  C CG  . LEU A 380 ? 0.3074 0.1685 0.1917 0.0515  0.0138  -0.0206 372 LEU A CG  
2613  C CD1 . LEU A 380 ? 0.2804 0.1391 0.1644 0.0404  0.0087  -0.0163 372 LEU A CD1 
2614  C CD2 . LEU A 380 ? 0.4169 0.2687 0.3001 0.0608  0.0122  -0.0220 372 LEU A CD2 
2615  N N   . VAL A 381 ? 0.2935 0.1863 0.1847 0.0447  0.0244  -0.0209 373 VAL A N   
2616  C CA  . VAL A 381 ? 0.2664 0.1770 0.1673 0.0469  0.0303  -0.0202 373 VAL A CA  
2617  C C   . VAL A 381 ? 0.3120 0.2356 0.2284 0.0465  0.0301  -0.0161 373 VAL A C   
2618  O O   . VAL A 381 ? 0.3152 0.2414 0.2359 0.0399  0.0267  -0.0124 373 VAL A O   
2619  C CB  . VAL A 381 ? 0.2535 0.1691 0.1514 0.0404  0.0313  -0.0188 373 VAL A CB  
2620  C CG1 . VAL A 381 ? 0.2441 0.1770 0.1519 0.0413  0.0369  -0.0171 373 VAL A CG1 
2621  C CG2 . VAL A 381 ? 0.2759 0.1790 0.1575 0.0407  0.0316  -0.0231 373 VAL A CG2 
2622  N N   . GLY A 382 ? 0.2667 0.1992 0.1913 0.0537  0.0336  -0.0171 374 GLY A N   
2623  C CA  . GLY A 382 ? 0.2475 0.1921 0.1861 0.0537  0.0331  -0.0136 374 GLY A CA  
2624  C C   . GLY A 382 ? 0.1974 0.1599 0.1460 0.0511  0.0377  -0.0115 374 GLY A C   
2625  O O   . GLY A 382 ? 0.2123 0.1779 0.1568 0.0494  0.0415  -0.0124 374 GLY A O   
2626  N N   . GLY A 383 ? 0.1767 0.1501 0.1374 0.0504  0.0371  -0.0086 375 GLY A N   
2627  C CA  . GLY A 383 ? 0.2151 0.2050 0.1855 0.0483  0.0413  -0.0068 375 GLY A CA  
2628  C C   . GLY A 383 ? 0.2792 0.2774 0.2609 0.0462  0.0388  -0.0034 375 GLY A C   
2629  O O   . GLY A 383 ? 0.1538 0.1452 0.1355 0.0462  0.0339  -0.0023 375 GLY A O   
2630  N N   . SER A 384 ? 0.1688 0.1813 0.1593 0.0439  0.0421  -0.0018 376 SER A N   
2631  C CA  A SER A 384 ? 0.1699 0.1915 0.1710 0.0414  0.0401  0.0011  376 SER A CA  
2632  C CA  B SER A 384 ? 0.1682 0.1891 0.1689 0.0410  0.0399  0.0013  376 SER A CA  
2633  C C   . SER A 384 ? 0.1654 0.1969 0.1706 0.0353  0.0433  0.0033  376 SER A C   
2634  O O   . SER A 384 ? 0.1653 0.2007 0.1678 0.0348  0.0480  0.0024  376 SER A O   
2635  C CB  A SER A 384 ? 0.1651 0.1955 0.1751 0.0480  0.0402  0.0000  376 SER A CB  
2636  C CB  B SER A 384 ? 0.1680 0.1963 0.1771 0.0474  0.0393  0.0004  376 SER A CB  
2637  O OG  A SER A 384 ? 0.1692 0.2106 0.1897 0.0448  0.0388  0.0028  376 SER A OG  
2638  O OG  B SER A 384 ? 0.1376 0.1792 0.1524 0.0509  0.0447  -0.0015 376 SER A OG  
2639  N N   . ALA A 385 ? 0.1379 0.1729 0.1488 0.0307  0.0407  0.0062  377 ALA A N   
2640  C CA  . ALA A 385 ? 0.1227 0.1651 0.1368 0.0247  0.0428  0.0084  377 ALA A CA  
2641  C C   . ALA A 385 ? 0.1472 0.2051 0.1723 0.0252  0.0452  0.0086  377 ALA A C   
2642  O O   . ALA A 385 ? 0.1655 0.2291 0.1976 0.0223  0.0429  0.0104  377 ALA A O   
2643  C CB  . ALA A 385 ? 0.1083 0.1452 0.1215 0.0196  0.0388  0.0108  377 ALA A CB  
2644  N N   . ASP A 386 ? 0.1450 0.2109 0.1716 0.0290  0.0500  0.0064  378 ASP A N   
2645  C CA  . ASP A 386 ? 0.1379 0.2219 0.1758 0.0298  0.0532  0.0061  378 ASP A CA  
2646  C C   . ASP A 386 ? 0.1738 0.2633 0.2208 0.0347  0.0491  0.0058  378 ASP A C   
2647  O O   . ASP A 386 ? 0.1686 0.2722 0.2261 0.0329  0.0490  0.0069  378 ASP A O   
2648  C CB  . ASP A 386 ? 0.1119 0.2035 0.1529 0.0207  0.0550  0.0090  378 ASP A CB  
2649  C CG  . ASP A 386 ? 0.1706 0.2823 0.2216 0.0199  0.0598  0.0086  378 ASP A CG  
2650  O OD1 . ASP A 386 ? 0.2000 0.3183 0.2502 0.0235  0.0651  0.0062  378 ASP A OD1 
2651  O OD2 . ASP A 386 ? 0.2117 0.3335 0.2713 0.0151  0.0585  0.0105  378 ASP A OD2 
2652  N N   . LEU A 387 ? 0.1534 0.2313 0.1960 0.0406  0.0453  0.0046  379 LEU A N   
2653  C CA  . LEU A 387 ? 0.1845 0.2656 0.2339 0.0456  0.0408  0.0046  379 LEU A CA  
2654  C C   . LEU A 387 ? 0.2835 0.3579 0.3292 0.0557  0.0402  0.0015  379 LEU A C   
2655  O O   . LEU A 387 ? 0.3113 0.3773 0.3555 0.0596  0.0350  0.0018  379 LEU A O   
2656  C CB  . LEU A 387 ? 0.2294 0.3008 0.2764 0.0413  0.0350  0.0073  379 LEU A CB  
2657  C CG  . LEU A 387 ? 0.2961 0.3739 0.3475 0.0328  0.0344  0.0101  379 LEU A CG  
2658  C CD1 . LEU A 387 ? 0.2833 0.3497 0.3299 0.0293  0.0293  0.0120  379 LEU A CD1 
2659  C CD2 . LEU A 387 ? 0.2292 0.3250 0.2932 0.0330  0.0346  0.0105  379 LEU A CD2 
2660  N N   . THR A 388 ? 0.1919 0.2688 0.2349 0.0598  0.0455  -0.0016 380 THR A N   
2661  C CA  . THR A 388 ? 0.2789 0.3470 0.3162 0.0698  0.0450  -0.0053 380 THR A CA  
2662  C C   . THR A 388 ? 0.3109 0.3867 0.3572 0.0786  0.0420  -0.0061 380 THR A C   
2663  O O   . THR A 388 ? 0.3005 0.3617 0.3407 0.0844  0.0372  -0.0068 380 THR A O   
2664  C CB  . THR A 388 ? 0.3109 0.3824 0.3439 0.0726  0.0519  -0.0089 380 THR A CB  
2665  O OG1 . THR A 388 ? 0.2740 0.3376 0.2980 0.0643  0.0538  -0.0076 380 THR A OG1 
2666  C CG2 . THR A 388 ? 0.2917 0.3506 0.3162 0.0829  0.0513  -0.0132 380 THR A CG2 
2667  N N   . PRO A 389 ? 0.2827 0.3804 0.3431 0.0798  0.0441  -0.0059 381 PRO A N   
2668  C CA  . PRO A 389 ? 0.3674 0.4727 0.4366 0.0888  0.0402  -0.0066 381 PRO A CA  
2669  C C   . PRO A 389 ? 0.3653 0.4631 0.4348 0.0859  0.0325  -0.0028 381 PRO A C   
2670  O O   . PRO A 389 ? 0.2581 0.3565 0.3314 0.0938  0.0278  -0.0029 381 PRO A O   
2671  C CB  . PRO A 389 ? 0.3787 0.5122 0.4635 0.0884  0.0449  -0.0071 381 PRO A CB  
2672  C CG  . PRO A 389 ? 0.3333 0.4702 0.4175 0.0751  0.0479  -0.0042 381 PRO A CG  
2673  C CD  . PRO A 389 ? 0.2770 0.3938 0.3457 0.0726  0.0497  -0.0050 381 PRO A CD  
2674  N N   . SER A 390 ? 0.3363 0.4269 0.4015 0.0752  0.0310  0.0005  382 SER A N   
2675  C CA  . SER A 390 ? 0.2732 0.3567 0.3374 0.0713  0.0244  0.0039  382 SER A CA  
2676  C C   . SER A 390 ? 0.3702 0.4300 0.4203 0.0705  0.0206  0.0046  382 SER A C   
2677  O O   . SER A 390 ? 0.3445 0.3953 0.3916 0.0731  0.0148  0.0062  382 SER A O   
2678  C CB  . SER A 390 ? 0.2471 0.3387 0.3158 0.0602  0.0251  0.0068  382 SER A CB  
2679  O OG  . SER A 390 ? 0.3753 0.4887 0.4574 0.0594  0.0268  0.0070  382 SER A OG  
2680  N N   . ASN A 391 ? 0.3213 0.3710 0.3623 0.0664  0.0237  0.0037  383 ASN A N   
2681  C CA  . ASN A 391 ? 0.3412 0.3699 0.3691 0.0648  0.0203  0.0042  383 ASN A CA  
2682  C C   . ASN A 391 ? 0.3857 0.4014 0.4057 0.0739  0.0190  0.0014  383 ASN A C   
2683  O O   . ASN A 391 ? 0.3128 0.3104 0.3220 0.0730  0.0148  0.0021  383 ASN A O   
2684  C CB  . ASN A 391 ? 0.2533 0.2765 0.2744 0.0573  0.0233  0.0042  383 ASN A CB  
2685  C CG  . ASN A 391 ? 0.2541 0.2868 0.2809 0.0487  0.0244  0.0068  383 ASN A CG  
2686  O OD1 . ASN A 391 ? 0.2306 0.2659 0.2560 0.0446  0.0282  0.0065  383 ASN A OD1 
2687  N ND2 . ASN A 391 ? 0.2636 0.3003 0.2955 0.0462  0.0207  0.0093  383 ASN A ND2 
2688  N N   . LEU A 392 ? 0.2805 0.3048 0.3049 0.0823  0.0226  -0.0020 384 LEU A N   
2689  C CA  . LEU A 392 ? 0.2830 0.2945 0.2993 0.0923  0.0217  -0.0056 384 LEU A CA  
2690  C C   . LEU A 392 ? 0.3686 0.3603 0.3695 0.0889  0.0221  -0.0070 384 LEU A C   
2691  O O   . LEU A 392 ? 0.3426 0.3142 0.3320 0.0900  0.0174  -0.0069 384 LEU A O   
2692  C CB  . LEU A 392 ? 0.2211 0.2242 0.2365 0.0984  0.0146  -0.0040 384 LEU A CB  
2693  C CG  . LEU A 392 ? 0.2345 0.2583 0.2655 0.1026  0.0136  -0.0028 384 LEU A CG  
2694  C CD1 . LEU A 392 ? 0.3283 0.3425 0.3570 0.1103  0.0061  -0.0015 384 LEU A CD1 
2695  C CD2 . LEU A 392 ? 0.2978 0.3410 0.3390 0.1096  0.0198  -0.0067 384 LEU A CD2 
2696  N N   . THR A 393 ? 0.2857 0.2831 0.2859 0.0840  0.0276  -0.0082 385 THR A N   
2697  C CA  . THR A 393 ? 0.2242 0.2060 0.2110 0.0791  0.0279  -0.0092 385 THR A CA  
2698  C C   . THR A 393 ? 0.3899 0.3665 0.3688 0.0853  0.0320  -0.0142 385 THR A C   
2699  O O   . THR A 393 ? 0.3655 0.3271 0.3317 0.0821  0.0314  -0.0155 385 THR A O   
2700  C CB  . THR A 393 ? 0.2568 0.2458 0.2458 0.0685  0.0301  -0.0065 385 THR A CB  
2701  O OG1 . THR A 393 ? 0.3224 0.3319 0.3235 0.0681  0.0348  -0.0061 385 THR A OG1 
2702  C CG2 . THR A 393 ? 0.2669 0.2515 0.2562 0.0613  0.0250  -0.0024 385 THR A CG2 
2703  N N   . ASP A 394 ? 0.3436 0.3335 0.3298 0.0938  0.0364  -0.0172 386 ASP A N   
2704  C CA  . ASP A 394 ? 0.4188 0.4024 0.3961 0.1008  0.0404  -0.0227 386 ASP A CA  
2705  C C   . ASP A 394 ? 0.4565 0.4229 0.4259 0.1110  0.0359  -0.0255 386 ASP A C   
2706  O O   . ASP A 394 ? 0.3741 0.3377 0.3474 0.1136  0.0305  -0.0231 386 ASP A O   
2707  C CB  . ASP A 394 ? 0.3916 0.3978 0.3791 0.1052  0.0480  -0.0252 386 ASP A CB  
2708  C CG  . ASP A 394 ? 0.5006 0.5255 0.5044 0.1111  0.0476  -0.0243 386 ASP A CG  
2709  O OD1 . ASP A 394 ? 0.5719 0.5926 0.5792 0.1108  0.0413  -0.0211 386 ASP A OD1 
2710  O OD2 . ASP A 394 ? 0.5135 0.5577 0.5266 0.1147  0.0531  -0.0266 386 ASP A OD2 
2711  N N   . TRP A 395 ? 0.4770 0.4297 0.4334 0.1163  0.0376  -0.0304 387 TRP A N   
2712  C CA  . TRP A 395 ? 0.4301 0.3648 0.3776 0.1263  0.0334  -0.0336 387 TRP A CA  
2713  C C   . TRP A 395 ? 0.4265 0.3679 0.3741 0.1326  0.0382  -0.0390 387 TRP A C   
2714  O O   . TRP A 395 ? 0.4038 0.3637 0.3583 0.1309  0.0452  -0.0404 387 TRP A O   
2715  C CB  . TRP A 395 ? 0.3790 0.2843 0.3081 0.1212  0.0275  -0.0330 387 TRP A CB  
2716  C CG  . TRP A 395 ? 0.3768 0.2730 0.2934 0.1149  0.0302  -0.0354 387 TRP A CG  
2717  C CD1 . TRP A 395 ? 0.3560 0.2354 0.2574 0.1193  0.0307  -0.0408 387 TRP A CD1 
2718  C CD2 . TRP A 395 ? 0.3520 0.2557 0.2699 0.1024  0.0320  -0.0324 387 TRP A CD2 
2719  N NE1 . TRP A 395 ? 0.3404 0.2159 0.2329 0.1112  0.0331  -0.0416 387 TRP A NE1 
2720  C CE2 . TRP A 395 ? 0.3203 0.2112 0.2233 0.1006  0.0337  -0.0362 387 TRP A CE2 
2721  C CE3 . TRP A 395 ? 0.3576 0.2769 0.2873 0.0931  0.0322  -0.0270 387 TRP A CE3 
2722  C CZ2 . TRP A 395 ? 0.2925 0.1865 0.1926 0.0900  0.0350  -0.0344 387 TRP A CZ2 
2723  C CZ3 . TRP A 395 ? 0.3227 0.2442 0.2493 0.0833  0.0338  -0.0255 387 TRP A CZ3 
2724  C CH2 . TRP A 395 ? 0.3140 0.2233 0.2262 0.0819  0.0350  -0.0290 387 TRP A CH2 
2725  N N   . SER A 396 ? 0.3706 0.2968 0.3102 0.1397  0.0345  -0.0420 388 SER A N   
2726  C CA  . SER A 396 ? 0.3727 0.3069 0.3143 0.1474  0.0389  -0.0472 388 SER A CA  
2727  C C   . SER A 396 ? 0.4093 0.3436 0.3427 0.1436  0.0451  -0.0507 388 SER A C   
2728  O O   . SER A 396 ? 0.4482 0.3990 0.3880 0.1468  0.0514  -0.0540 388 SER A O   
2729  C CB  . SER A 396 ? 0.3834 0.2974 0.3152 0.1555  0.0334  -0.0498 388 SER A CB  
2730  O OG  . SER A 396 ? 0.3785 0.2647 0.2901 0.1517  0.0299  -0.0509 388 SER A OG  
2731  N N   . ASN A 397 ? 0.4160 0.3330 0.3352 0.1360  0.0435  -0.0499 389 ASN A N   
2732  C CA  . ASN A 397 ? 0.4226 0.3357 0.3307 0.1322  0.0481  -0.0532 389 ASN A CA  
2733  C C   . ASN A 397 ? 0.4352 0.3570 0.3446 0.1224  0.0515  -0.0499 389 ASN A C   
2734  O O   . ASN A 397 ? 0.5048 0.4182 0.4017 0.1174  0.0533  -0.0516 389 ASN A O   
2735  C CB  . ASN A 397 ? 0.4754 0.3588 0.3630 0.1317  0.0431  -0.0558 389 ASN A CB  
2736  C CG  . ASN A 397 ? 0.5493 0.4233 0.4334 0.1417  0.0407  -0.0596 389 ASN A CG  
2737  O OD1 . ASN A 397 ? 0.6891 0.5801 0.5843 0.1494  0.0448  -0.0620 389 ASN A OD1 
2738  N ND2 . ASN A 397 ? 0.5246 0.3717 0.3931 0.1413  0.0341  -0.0601 389 ASN A ND2 
2739  N N   . SER A 398 ? 0.3495 0.2876 0.2730 0.1195  0.0522  -0.0453 390 SER A N   
2740  C CA  . SER A 398 ? 0.3030 0.2504 0.2279 0.1104  0.0558  -0.0421 390 SER A CA  
2741  C C   . SER A 398 ? 0.3184 0.2843 0.2476 0.1097  0.0637  -0.0442 390 SER A C   
2742  O O   . SER A 398 ? 0.2907 0.2732 0.2314 0.1148  0.0669  -0.0459 390 SER A O   
2743  C CB  . SER A 398 ? 0.3482 0.3085 0.2885 0.1041  0.0528  -0.0357 390 SER A CB  
2744  O OG  . SER A 398 ? 0.3283 0.3049 0.2832 0.1120  0.0541  -0.0358 390 SER A OG  
2745  N N   . VAL A 399 ? 0.2873 0.2493 0.2062 0.1028  0.0664  -0.0440 391 VAL A N   
2746  C CA  . VAL A 399 ? 0.3111 0.2881 0.2313 0.0999  0.0736  -0.0452 391 VAL A CA  
2747  C C   . VAL A 399 ? 0.2645 0.2506 0.1881 0.0900  0.0753  -0.0396 391 VAL A C   
2748  O O   . VAL A 399 ? 0.2541 0.2275 0.1700 0.0820  0.0703  -0.0367 391 VAL A O   
2749  C CB  . VAL A 399 ? 0.2920 0.2547 0.1948 0.1002  0.0747  -0.0500 391 VAL A CB  
2750  C CG1 . VAL A 399 ? 0.3587 0.3357 0.2611 0.0952  0.0817  -0.0502 391 VAL A CG1 
2751  C CG2 . VAL A 399 ? 0.3315 0.2867 0.2321 0.1100  0.0734  -0.0555 391 VAL A CG2 
2752  N N   . SER A 400 ? 0.2803 0.2889 0.2177 0.0879  0.0801  -0.0374 392 SER A N   
2753  C CA  . SER A 400 ? 0.2657 0.2827 0.2082 0.0771  0.0803  -0.0314 392 SER A CA  
2754  C C   . SER A 400 ? 0.2729 0.2837 0.2015 0.0704  0.0828  -0.0311 392 SER A C   
2755  O O   . SER A 400 ? 0.2741 0.2890 0.1965 0.0726  0.0887  -0.0346 392 SER A O   
2756  C CB  . SER A 400 ? 0.2863 0.3282 0.2451 0.0767  0.0855  -0.0296 392 SER A CB  
2757  O OG  . SER A 400 ? 0.3162 0.3647 0.2884 0.0821  0.0823  -0.0293 392 SER A OG  
2758  N N   . VAL A 401 ? 0.2403 0.2420 0.1647 0.0618  0.0776  -0.0267 393 VAL A N   
2759  C CA  . VAL A 401 ? 0.2356 0.2322 0.1476 0.0551  0.0790  -0.0254 393 VAL A CA  
2760  C C   . VAL A 401 ? 0.2514 0.2650 0.1688 0.0503  0.0854  -0.0226 393 VAL A C   
2761  O O   . VAL A 401 ? 0.2296 0.2554 0.1607 0.0474  0.0855  -0.0189 393 VAL A O   
2762  C CB  . VAL A 401 ? 0.2871 0.2716 0.1951 0.0479  0.0713  -0.0214 393 VAL A CB  
2763  C CG1 . VAL A 401 ? 0.2919 0.2728 0.1882 0.0411  0.0721  -0.0193 393 VAL A CG1 
2764  C CG2 . VAL A 401 ? 0.2854 0.2527 0.1861 0.0510  0.0652  -0.0241 393 VAL A CG2 
2765  N N   . THR A 402 ? 0.2612 0.2751 0.1671 0.0489  0.0909  -0.0242 394 THR A N   
2766  C CA  . THR A 402 ? 0.2423 0.2708 0.1506 0.0430  0.0971  -0.0214 394 THR A CA  
2767  C C   . THR A 402 ? 0.3109 0.3291 0.2031 0.0357  0.0966  -0.0188 394 THR A C   
2768  O O   . THR A 402 ? 0.2966 0.2985 0.1764 0.0360  0.0919  -0.0200 394 THR A O   
2769  C CB  . THR A 402 ? 0.3221 0.3653 0.2360 0.0465  0.1031  -0.0263 394 THR A CB  
2770  O OG1 . THR A 402 ? 0.3207 0.3536 0.2207 0.0502  0.1039  -0.0316 394 THR A OG1 
2771  C CG2 . THR A 402 ? 0.3168 0.3700 0.2470 0.0541  0.1027  -0.0288 394 THR A CG2 
2772  N N   . ARG A 403 ? 0.3460 0.3744 0.2392 0.0283  0.1003  -0.0153 395 ARG A N   
2773  C CA  . ARG A 403 ? 0.3708 0.3904 0.2485 0.0214  0.0995  -0.0125 395 ARG A CA  
2774  C C   . ARG A 403 ? 0.3802 0.3924 0.2440 0.0247  0.1004  -0.0177 395 ARG A C   
2775  O O   . ARG A 403 ? 0.4619 0.4597 0.3110 0.0221  0.0965  -0.0167 395 ARG A O   
2776  C CB  . ARG A 403 ? 0.4110 0.4437 0.2918 0.0133  0.1037  -0.0083 395 ARG A CB  
2777  C CG  . ARG A 403 ? 0.4674 0.4914 0.3323 0.0064  0.1024  -0.0045 395 ARG A CG  
2778  C CD  . ARG A 403 ? 0.5383 0.5763 0.4055 -0.0004 0.1070  -0.0006 395 ARG A CD  
2779  N NE  . ARG A 403 ? 0.6792 0.7197 0.5553 -0.0060 0.1052  0.0054  395 ARG A NE  
2780  C CZ  . ARG A 403 ? 0.7063 0.7349 0.5748 -0.0125 0.1007  0.0113  395 ARG A CZ  
2781  N NH1 . ARG A 403 ? 0.6918 0.7064 0.5442 -0.0140 0.0974  0.0125  395 ARG A NH1 
2782  N NH2 . ARG A 403 ? 0.6433 0.6737 0.5202 -0.0173 0.0990  0.0159  395 ARG A NH2 
2783  N N   . ASP A 404 ? 0.3440 0.3657 0.2122 0.0304  0.1052  -0.0236 396 ASP A N   
2784  C CA  . ASP A 404 ? 0.3879 0.4042 0.2429 0.0329  0.1070  -0.0289 396 ASP A CA  
2785  C C   . ASP A 404 ? 0.3708 0.3731 0.2209 0.0413  0.1034  -0.0346 396 ASP A C   
2786  O O   . ASP A 404 ? 0.3946 0.3893 0.2321 0.0431  0.1039  -0.0390 396 ASP A O   
2787  C CB  . ASP A 404 ? 0.4454 0.4805 0.3060 0.0332  0.1151  -0.0325 396 ASP A CB  
2788  C CG  . ASP A 404 ? 0.5733 0.6210 0.4345 0.0236  0.1186  -0.0270 396 ASP A CG  
2789  O OD1 . ASP A 404 ? 0.6199 0.6580 0.4702 0.0175  0.1150  -0.0214 396 ASP A OD1 
2790  O OD2 . ASP A 404 ? 0.6157 0.6819 0.4882 0.0217  0.1248  -0.0283 396 ASP A OD2 
2791  N N   . LYS A 405 ? 0.3056 0.3038 0.1645 0.0461  0.0996  -0.0346 397 LYS A N   
2792  C CA  . LYS A 405 ? 0.3641 0.3491 0.2185 0.0540  0.0963  -0.0401 397 LYS A CA  
2793  C C   . LYS A 405 ? 0.3298 0.3027 0.1856 0.0545  0.0894  -0.0375 397 LYS A C   
2794  O O   . LYS A 405 ? 0.3791 0.3581 0.2443 0.0510  0.0885  -0.0323 397 LYS A O   
2795  C CB  . LYS A 405 ? 0.3735 0.3698 0.2396 0.0625  0.1003  -0.0453 397 LYS A CB  
2796  N N   . GLY A 406 ? 0.3359 0.2912 0.1818 0.0583  0.0846  -0.0413 398 GLY A N   
2797  C CA  . GLY A 406 ? 0.3194 0.2633 0.1671 0.0582  0.0775  -0.0396 398 GLY A CA  
2798  C C   . GLY A 406 ? 0.3332 0.2827 0.1953 0.0656  0.0774  -0.0409 398 GLY A C   
2799  O O   . GLY A 406 ? 0.3243 0.2886 0.1964 0.0707  0.0830  -0.0425 398 GLY A O   
2800  N N   . GLY A 407 ? 0.3023 0.2410 0.1667 0.0649  0.0699  -0.0395 399 GLY A N   
2801  C CA  . GLY A 407 ? 0.3120 0.2531 0.1880 0.0715  0.0684  -0.0403 399 GLY A CA  
2802  C C   . GLY A 407 ? 0.3123 0.2421 0.1900 0.0672  0.0597  -0.0370 399 GLY A C   
2803  O O   . GLY A 407 ? 0.3552 0.2744 0.2241 0.0602  0.0550  -0.0355 399 GLY A O   
2804  N N   . ASN A 408 ? 0.3519 0.2849 0.2411 0.0715  0.0577  -0.0361 400 ASN A N   
2805  C CA  . ASN A 408 ? 0.2657 0.1898 0.1573 0.0671  0.0500  -0.0327 400 ASN A CA  
2806  C C   . ASN A 408 ? 0.2815 0.2202 0.1907 0.0664  0.0495  -0.0282 400 ASN A C   
2807  O O   . ASN A 408 ? 0.2586 0.1912 0.1710 0.0652  0.0439  -0.0260 400 ASN A O   
2808  C CB  . ASN A 408 ? 0.2957 0.1997 0.1770 0.0723  0.0456  -0.0364 400 ASN A CB  
2809  C CG  . ASN A 408 ? 0.3194 0.2255 0.2042 0.0844  0.0488  -0.0405 400 ASN A CG  
2810  O OD1 . ASN A 408 ? 0.3030 0.2281 0.2009 0.0885  0.0538  -0.0400 400 ASN A OD1 
2811  N ND2 . ASN A 408 ? 0.3609 0.2471 0.2335 0.0903  0.0456  -0.0448 400 ASN A ND2 
2812  N N   . TYR A 409 ? 0.2501 0.2075 0.1698 0.0666  0.0550  -0.0268 401 TYR A N   
2813  C CA  . TYR A 409 ? 0.2415 0.2131 0.1773 0.0651  0.0544  -0.0226 401 TYR A CA  
2814  C C   . TYR A 409 ? 0.2187 0.2043 0.1599 0.0583  0.0582  -0.0192 401 TYR A C   
2815  O O   . TYR A 409 ? 0.2275 0.2202 0.1659 0.0590  0.0642  -0.0209 401 TYR A O   
2816  C CB  . TYR A 409 ? 0.2178 0.1990 0.1633 0.0747  0.0569  -0.0250 401 TYR A CB  
2817  C CG  . TYR A 409 ? 0.2957 0.2877 0.2561 0.0731  0.0542  -0.0209 401 TYR A CG  
2818  C CD1 . TYR A 409 ? 0.3059 0.3168 0.2781 0.0692  0.0578  -0.0180 401 TYR A CD1 
2819  C CD2 . TYR A 409 ? 0.2867 0.2689 0.2479 0.0747  0.0478  -0.0196 401 TYR A CD2 
2820  C CE1 . TYR A 409 ? 0.2981 0.3182 0.2829 0.0672  0.0550  -0.0145 401 TYR A CE1 
2821  C CE2 . TYR A 409 ? 0.2522 0.2440 0.2259 0.0730  0.0451  -0.0159 401 TYR A CE2 
2822  C CZ  . TYR A 409 ? 0.2728 0.2836 0.2582 0.0693  0.0487  -0.0135 401 TYR A CZ  
2823  O OH  . TYR A 409 ? 0.2939 0.3138 0.2908 0.0672  0.0459  -0.0100 401 TYR A OH  
2824  N N   . ILE A 410 ? 0.2064 0.1951 0.1544 0.0517  0.0547  -0.0145 402 ILE A N   
2825  C CA  . ILE A 410 ? 0.2073 0.2055 0.1587 0.0448  0.0570  -0.0109 402 ILE A CA  
2826  C C   . ILE A 410 ? 0.2113 0.2242 0.1777 0.0439  0.0578  -0.0081 402 ILE A C   
2827  O O   . ILE A 410 ? 0.2038 0.2154 0.1765 0.0437  0.0531  -0.0063 402 ILE A O   
2828  C CB  . ILE A 410 ? 0.2066 0.1957 0.1519 0.0378  0.0522  -0.0079 402 ILE A CB  
2829  C CG1 . ILE A 410 ? 0.2933 0.2691 0.2235 0.0379  0.0512  -0.0106 402 ILE A CG1 
2830  C CG2 . ILE A 410 ? 0.1721 0.1696 0.1207 0.0316  0.0541  -0.0040 402 ILE A CG2 
2831  C CD1 . ILE A 410 ? 0.2908 0.2577 0.2160 0.0321  0.0451  -0.0084 402 ILE A CD1 
2832  N N   . HIS A 411 ? 0.1745 0.2013 0.1458 0.0429  0.0636  -0.0077 403 HIS A N   
2833  C CA  . HIS A 411 ? 0.1870 0.2280 0.1715 0.0397  0.0642  -0.0046 403 HIS A CA  
2834  C C   . HIS A 411 ? 0.2033 0.2409 0.1854 0.0309  0.0622  -0.0003 403 HIS A C   
2835  O O   . HIS A 411 ? 0.1811 0.2200 0.1575 0.0265  0.0657  0.0009  403 HIS A O   
2836  C CB  . HIS A 411 ? 0.1633 0.2216 0.1542 0.0412  0.0713  -0.0059 403 HIS A CB  
2837  C CG  . HIS A 411 ? 0.2948 0.3590 0.2901 0.0512  0.0734  -0.0105 403 HIS A CG  
2838  N ND1 . HIS A 411 ? 0.2998 0.3727 0.3075 0.0559  0.0712  -0.0106 403 HIS A ND1 
2839  C CD2 . HIS A 411 ? 0.3102 0.3729 0.2987 0.0580  0.0776  -0.0152 403 HIS A CD2 
2840  C CE1 . HIS A 411 ? 0.3074 0.3839 0.3162 0.0657  0.0736  -0.0151 403 HIS A CE1 
2841  N NE2 . HIS A 411 ? 0.3136 0.3838 0.3108 0.0673  0.0777  -0.0182 403 HIS A NE2 
2842  N N   . TYR A 412 ? 0.1444 0.1769 0.1297 0.0287  0.0565  0.0019  404 TYR A N   
2843  C CA  . TYR A 412 ? 0.1401 0.1683 0.1226 0.0218  0.0541  0.0055  404 TYR A CA  
2844  C C   . TYR A 412 ? 0.1553 0.1940 0.1450 0.0166  0.0563  0.0084  404 TYR A C   
2845  O O   . TYR A 412 ? 0.1525 0.1866 0.1381 0.0112  0.0550  0.0112  404 TYR A O   
2846  C CB  . TYR A 412 ? 0.1740 0.1943 0.1574 0.0214  0.0478  0.0065  404 TYR A CB  
2847  C CG  . TYR A 412 ? 0.1915 0.1997 0.1657 0.0235  0.0449  0.0046  404 TYR A CG  
2848  C CD1 . TYR A 412 ? 0.1717 0.1723 0.1368 0.0202  0.0433  0.0055  404 TYR A CD1 
2849  C CD2 . TYR A 412 ? 0.1587 0.1626 0.1325 0.0285  0.0434  0.0020  404 TYR A CD2 
2850  C CE1 . TYR A 412 ? 0.1848 0.1754 0.1417 0.0211  0.0403  0.0037  404 TYR A CE1 
2851  C CE2 . TYR A 412 ? 0.1506 0.1423 0.1149 0.0292  0.0404  0.0003  404 TYR A CE2 
2852  C CZ  . TYR A 412 ? 0.1648 0.1507 0.1210 0.0250  0.0389  0.0012  404 TYR A CZ  
2853  O OH  . TYR A 412 ? 0.1941 0.1692 0.1411 0.0248  0.0357  -0.0005 404 TYR A OH  
2854  N N   . GLY A 413 ? 0.1329 0.1850 0.1325 0.0181  0.0592  0.0077  405 GLY A N   
2855  C CA  . GLY A 413 ? 0.1463 0.2078 0.1530 0.0121  0.0602  0.0105  405 GLY A CA  
2856  C C   . GLY A 413 ? 0.1200 0.1779 0.1313 0.0100  0.0545  0.0125  405 GLY A C   
2857  O O   . GLY A 413 ? 0.1441 0.1944 0.1546 0.0134  0.0502  0.0117  405 GLY A O   
2858  N N   . VAL A 414 ? 0.1178 0.1804 0.1328 0.0036  0.0546  0.0151  406 VAL A N   
2859  C CA  . VAL A 414 ? 0.1113 0.1710 0.1301 0.0013  0.0496  0.0166  406 VAL A CA  
2860  C C   . VAL A 414 ? 0.1261 0.1714 0.1355 -0.0010 0.0465  0.0180  406 VAL A C   
2861  O O   . VAL A 414 ? 0.1298 0.1712 0.1361 -0.0065 0.0459  0.0202  406 VAL A O   
2862  C CB  . VAL A 414 ? 0.1098 0.1801 0.1362 -0.0046 0.0505  0.0183  406 VAL A CB  
2863  C CG1 . VAL A 414 ? 0.1122 0.1807 0.1431 -0.0056 0.0453  0.0189  406 VAL A CG1 
2864  C CG2 . VAL A 414 ? 0.1284 0.2159 0.1643 -0.0024 0.0545  0.0168  406 VAL A CG2 
2865  N N   . ARG A 415 ? 0.1127 0.1498 0.1171 0.0033  0.0444  0.0166  407 ARG A N   
2866  C CA  . ARG A 415 ? 0.1178 0.1432 0.1132 0.0024  0.0418  0.0174  407 ARG A CA  
2867  C C   . ARG A 415 ? 0.1283 0.1488 0.1237 0.0061  0.0378  0.0159  407 ARG A C   
2868  O O   . ARG A 415 ? 0.1288 0.1439 0.1183 0.0085  0.0374  0.0146  407 ARG A O   
2869  C CB  . ARG A 415 ? 0.1390 0.1604 0.1252 0.0022  0.0448  0.0173  407 ARG A CB  
2870  C CG  . ARG A 415 ? 0.1303 0.1566 0.1147 -0.0024 0.0496  0.0190  407 ARG A CG  
2871  C CD  . ARG A 415 ? 0.1399 0.1611 0.1134 -0.0019 0.0522  0.0186  407 ARG A CD  
2872  N NE  . ARG A 415 ? 0.1802 0.2049 0.1495 -0.0068 0.0571  0.0204  407 ARG A NE  
2873  C CZ  . ARG A 415 ? 0.1901 0.2245 0.1608 -0.0062 0.0629  0.0189  407 ARG A CZ  
2874  N NH1 . ARG A 415 ? 0.1606 0.2012 0.1369 0.0002  0.0641  0.0153  407 ARG A NH1 
2875  N NH2 . ARG A 415 ? 0.1607 0.1984 0.1266 -0.0119 0.0675  0.0209  407 ARG A NH2 
2876  N N   . GLU A 416 ? 0.1249 0.1467 0.1258 0.0058  0.0347  0.0162  408 GLU A N   
2877  C CA  . GLU A 416 ? 0.1310 0.1491 0.1318 0.0084  0.0313  0.0151  408 GLU A CA  
2878  C C   . GLU A 416 ? 0.1310 0.1418 0.1252 0.0078  0.0288  0.0153  408 GLU A C   
2879  O O   . GLU A 416 ? 0.1504 0.1572 0.1407 0.0095  0.0275  0.0141  408 GLU A O   
2880  C CB  . GLU A 416 ? 0.1438 0.1654 0.1511 0.0078  0.0288  0.0156  408 GLU A CB  
2881  C CG  . GLU A 416 ? 0.1474 0.1775 0.1622 0.0090  0.0300  0.0154  408 GLU A CG  
2882  C CD  . GLU A 416 ? 0.1543 0.1910 0.1729 0.0053  0.0323  0.0166  408 GLU A CD  
2883  O OE1 . GLU A 416 ? 0.1588 0.1913 0.1733 0.0017  0.0324  0.0178  408 GLU A OE1 
2884  O OE2 . GLU A 416 ? 0.1939 0.2400 0.2193 0.0060  0.0338  0.0164  408 GLU A OE2 
2885  N N   . PHE A 417 ? 0.1143 0.1230 0.1068 0.0055  0.0279  0.0166  409 PHE A N   
2886  C CA  . PHE A 417 ? 0.1618 0.1653 0.1489 0.0059  0.0252  0.0166  409 PHE A CA  
2887  C C   . PHE A 417 ? 0.1838 0.1833 0.1635 0.0067  0.0262  0.0163  409 PHE A C   
2888  O O   . PHE A 417 ? 0.1707 0.1677 0.1471 0.0076  0.0239  0.0153  409 PHE A O   
2889  C CB  . PHE A 417 ? 0.1384 0.1392 0.1241 0.0045  0.0240  0.0180  409 PHE A CB  
2890  C CG  . PHE A 417 ? 0.1183 0.1168 0.1018 0.0060  0.0204  0.0176  409 PHE A CG  
2891  C CD1 . PHE A 417 ? 0.1219 0.1217 0.1050 0.0072  0.0186  0.0164  409 PHE A CD1 
2892  C CD2 . PHE A 417 ? 0.1095 0.1047 0.0914 0.0063  0.0188  0.0182  409 PHE A CD2 
2893  C CE1 . PHE A 417 ? 0.1679 0.1685 0.1504 0.0085  0.0154  0.0159  409 PHE A CE1 
2894  C CE2 . PHE A 417 ? 0.1325 0.1274 0.1135 0.0088  0.0156  0.0175  409 PHE A CE2 
2895  C CZ  . PHE A 417 ? 0.1904 0.1895 0.1725 0.0098  0.0140  0.0164  409 PHE A CZ  
2896  N N   . GLY A 418 ? 0.1515 0.1509 0.1283 0.0057  0.0296  0.0170  410 GLY A N   
2897  C CA  . GLY A 418 ? 0.1904 0.1860 0.1592 0.0064  0.0310  0.0165  410 GLY A CA  
2898  C C   . GLY A 418 ? 0.1680 0.1634 0.1363 0.0090  0.0311  0.0139  410 GLY A C   
2899  O O   . GLY A 418 ? 0.1368 0.1272 0.0985 0.0095  0.0293  0.0129  410 GLY A O   
2900  N N   . MET A 419 ? 0.1250 0.1250 0.0998 0.0106  0.0326  0.0128  411 MET A N   
2901  C CA  . MET A 419 ? 0.1490 0.1465 0.1224 0.0136  0.0322  0.0104  411 MET A CA  
2902  C C   . MET A 419 ? 0.1666 0.1590 0.1376 0.0127  0.0276  0.0101  411 MET A C   
2903  O O   . MET A 419 ? 0.1550 0.1413 0.1190 0.0132  0.0264  0.0085  411 MET A O   
2904  C CB  . MET A 419 ? 0.1925 0.1956 0.1739 0.0160  0.0334  0.0098  411 MET A CB  
2905  C CG  . MET A 419 ? 0.1256 0.1235 0.1048 0.0195  0.0319  0.0076  411 MET A CG  
2906  S SD  . MET A 419 ? 0.1569 0.1611 0.1449 0.0238  0.0328  0.0069  411 MET A SD  
2907  C CE  . MET A 419 ? 0.1646 0.1706 0.1588 0.0206  0.0285  0.0094  411 MET A CE  
2908  N N   . GLY A 420 ? 0.1439 0.1389 0.1203 0.0111  0.0250  0.0114  412 GLY A N   
2909  C CA  . GLY A 420 ? 0.1365 0.1291 0.1115 0.0097  0.0211  0.0111  412 GLY A CA  
2910  C C   . GLY A 420 ? 0.1648 0.1545 0.1334 0.0084  0.0191  0.0109  412 GLY A C   
2911  O O   . GLY A 420 ? 0.1695 0.1554 0.1335 0.0073  0.0169  0.0098  412 GLY A O   
2912  N N   . ALA A 421 ? 0.1385 0.1294 0.1061 0.0082  0.0196  0.0123  413 ALA A N   
2913  C CA  . ALA A 421 ? 0.1501 0.1388 0.1117 0.0076  0.0170  0.0124  413 ALA A CA  
2914  C C   . ALA A 421 ? 0.1683 0.1513 0.1209 0.0079  0.0182  0.0112  413 ALA A C   
2915  O O   . ALA A 421 ? 0.1836 0.1640 0.1304 0.0069  0.0152  0.0105  413 ALA A O   
2916  C CB  . ALA A 421 ? 0.1682 0.1581 0.1302 0.0080  0.0164  0.0143  413 ALA A CB  
2917  N N   . ILE A 422 ? 0.1377 0.1195 0.0888 0.0092  0.0225  0.0107  414 ILE A N   
2918  C CA  . ILE A 422 ? 0.1754 0.1519 0.1174 0.0101  0.0243  0.0088  414 ILE A CA  
2919  C C   . ILE A 422 ? 0.1666 0.1384 0.1061 0.0104  0.0223  0.0062  414 ILE A C   
2920  O O   . ILE A 422 ? 0.1856 0.1514 0.1161 0.0097  0.0208  0.0046  414 ILE A O   
2921  C CB  . ILE A 422 ? 0.1647 0.1434 0.1070 0.0117  0.0301  0.0085  414 ILE A CB  
2922  C CG1 . ILE A 422 ? 0.1518 0.1321 0.0920 0.0099  0.0319  0.0111  414 ILE A CG1 
2923  C CG2 . ILE A 422 ? 0.1949 0.1685 0.1286 0.0138  0.0325  0.0054  414 ILE A CG2 
2924  C CD1 . ILE A 422 ? 0.1526 0.1382 0.0956 0.0100  0.0378  0.0114  414 ILE A CD1 
2925  N N   . MET A 423 ? 0.1833 0.1567 0.1296 0.0111  0.0220  0.0059  415 MET A N   
2926  C CA  A MET A 423 ? 0.1766 0.1433 0.1190 0.0109  0.0197  0.0039  415 MET A CA  
2927  C CA  B MET A 423 ? 0.1782 0.1450 0.1209 0.0109  0.0196  0.0040  415 MET A CA  
2928  C C   . MET A 423 ? 0.1698 0.1348 0.1088 0.0067  0.0148  0.0042  415 MET A C   
2929  O O   . MET A 423 ? 0.1830 0.1402 0.1138 0.0052  0.0127  0.0022  415 MET A O   
2930  C CB  A MET A 423 ? 0.1535 0.1216 0.1031 0.0121  0.0196  0.0043  415 MET A CB  
2931  C CB  B MET A 423 ? 0.1499 0.1186 0.1001 0.0119  0.0194  0.0045  415 MET A CB  
2932  C CG  A MET A 423 ? 0.1700 0.1385 0.1214 0.0171  0.0236  0.0029  415 MET A CG  
2933  C CG  B MET A 423 ? 0.1715 0.1415 0.1248 0.0166  0.0232  0.0035  415 MET A CG  
2934  S SD  A MET A 423 ? 0.2206 0.1866 0.1764 0.0194  0.0219  0.0028  415 MET A SD  
2935  S SD  B MET A 423 ? 0.1670 0.1425 0.1309 0.0172  0.0223  0.0053  415 MET A SD  
2936  C CE  A MET A 423 ? 0.1514 0.1272 0.1179 0.0162  0.0205  0.0061  415 MET A CE  
2937  C CE  B MET A 423 ? 0.1440 0.1096 0.1026 0.0149  0.0174  0.0049  415 MET A CE  
2938  N N   . ASN A 424 ? 0.1549 0.1273 0.0998 0.0047  0.0128  0.0063  416 ASN A N   
2939  C CA  . ASN A 424 ? 0.1632 0.1372 0.1062 0.0011  0.0083  0.0065  416 ASN A CA  
2940  C C   . ASN A 424 ? 0.1894 0.1586 0.1225 0.0006  0.0071  0.0053  416 ASN A C   
2941  O O   . ASN A 424 ? 0.1974 0.1627 0.1245 -0.0026 0.0038  0.0040  416 ASN A O   
2942  C CB  . ASN A 424 ? 0.1868 0.1705 0.1378 0.0009  0.0071  0.0085  416 ASN A CB  
2943  C CG  . ASN A 424 ? 0.1284 0.1170 0.0879 0.0002  0.0073  0.0092  416 ASN A CG  
2944  O OD1 . ASN A 424 ? 0.1498 0.1343 0.1087 -0.0009 0.0076  0.0086  416 ASN A OD1 
2945  N ND2 . ASN A 424 ? 0.1471 0.1433 0.1133 0.0009  0.0070  0.0105  416 ASN A ND2 
2946  N N   . GLY A 425 ? 0.1583 0.1269 0.0884 0.0032  0.0099  0.0059  417 GLY A N   
2947  C CA  . GLY A 425 ? 0.2452 0.2084 0.1643 0.0028  0.0090  0.0050  417 GLY A CA  
2948  C C   . GLY A 425 ? 0.2670 0.2206 0.1768 0.0029  0.0102  0.0018  417 GLY A C   
2949  O O   . GLY A 425 ? 0.2090 0.1572 0.1094 0.0007  0.0071  0.0002  417 GLY A O   
2950  N N   . LEU A 426 ? 0.2154 0.1666 0.1273 0.0059  0.0143  0.0005  418 LEU A N   
2951  C CA  . LEU A 426 ? 0.2362 0.1772 0.1391 0.0073  0.0153  -0.0031 418 LEU A CA  
2952  C C   . LEU A 426 ? 0.2508 0.1852 0.1494 0.0032  0.0101  -0.0043 418 LEU A C   
2953  O O   . LEU A 426 ? 0.2191 0.1440 0.1060 0.0018  0.0083  -0.0069 418 LEU A O   
2954  C CB  . LEU A 426 ? 0.1906 0.1318 0.0986 0.0121  0.0197  -0.0041 418 LEU A CB  
2955  C CG  . LEU A 426 ? 0.1890 0.1360 0.0991 0.0157  0.0257  -0.0039 418 LEU A CG  
2956  C CD1 . LEU A 426 ? 0.2020 0.1535 0.1215 0.0199  0.0289  -0.0041 418 LEU A CD1 
2957  C CD2 . LEU A 426 ? 0.2036 0.1439 0.1009 0.0175  0.0284  -0.0070 418 LEU A CD2 
2958  N N   . VAL A 427 ? 0.2299 0.1691 0.1372 0.0007  0.0076  -0.0024 419 VAL A N   
2959  C CA  A VAL A 427 ? 0.2314 0.1643 0.1341 -0.0043 0.0030  -0.0034 419 VAL A CA  
2960  C CA  B VAL A 427 ? 0.2343 0.1685 0.1383 -0.0046 0.0028  -0.0030 419 VAL A CA  
2961  C C   . VAL A 427 ? 0.2311 0.1674 0.1302 -0.0096 -0.0017 -0.0030 419 VAL A C   
2962  O O   . VAL A 427 ? 0.2510 0.1790 0.1410 -0.0140 -0.0052 -0.0049 419 VAL A O   
2963  C CB  A VAL A 427 ? 0.2430 0.1795 0.1547 -0.0059 0.0021  -0.0015 419 VAL A CB  
2964  C CB  B VAL A 427 ? 0.2308 0.1724 0.1457 -0.0068 0.0016  -0.0005 419 VAL A CB  
2965  C CG1 A VAL A 427 ? 0.2042 0.1548 0.1263 -0.0084 0.0007  0.0014  419 VAL A CG1 
2966  C CG1 B VAL A 427 ? 0.2321 0.1702 0.1434 -0.0139 -0.0032 -0.0006 419 VAL A CG1 
2967  C CG2 A VAL A 427 ? 0.2648 0.1902 0.1690 -0.0106 -0.0016 -0.0026 419 VAL A CG2 
2968  C CG2 B VAL A 427 ? 0.2361 0.1756 0.1555 -0.0024 0.0048  -0.0003 419 VAL A CG2 
2969  N N   . LEU A 428 ? 0.2097 0.1572 0.1151 -0.0092 -0.0021 -0.0008 420 LEU A N   
2970  C CA  . LEU A 428 ? 0.2226 0.1746 0.1252 -0.0132 -0.0070 -0.0004 420 LEU A CA  
2971  C C   . LEU A 428 ? 0.2460 0.1881 0.1345 -0.0137 -0.0080 -0.0028 420 LEU A C   
2972  O O   . LEU A 428 ? 0.2561 0.1970 0.1387 -0.0187 -0.0130 -0.0038 420 LEU A O   
2973  C CB  . LEU A 428 ? 0.1869 0.1510 0.0978 -0.0108 -0.0072 0.0023  420 LEU A CB  
2974  C CG  . LEU A 428 ? 0.2185 0.1940 0.1425 -0.0112 -0.0076 0.0042  420 LEU A CG  
2975  C CD1 . LEU A 428 ? 0.1906 0.1728 0.1205 -0.0065 -0.0060 0.0064  420 LEU A CD1 
2976  C CD2 . LEU A 428 ? 0.1903 0.1740 0.1170 -0.0168 -0.0129 0.0042  420 LEU A CD2 
2977  N N   . HIS A 429 ? 0.2546 0.1900 0.1373 -0.0089 -0.0032 -0.0040 421 HIS A N   
2978  C CA  . HIS A 429 ? 0.2854 0.2119 0.1538 -0.0089 -0.0036 -0.0064 421 HIS A CA  
2979  C C   . HIS A 429 ? 0.2796 0.1939 0.1371 -0.0129 -0.0067 -0.0099 421 HIS A C   
2980  O O   . HIS A 429 ? 0.3047 0.2139 0.1511 -0.0161 -0.0103 -0.0115 421 HIS A O   
2981  C CB  . HIS A 429 ? 0.2310 0.1538 0.0956 -0.0032 0.0031  -0.0074 421 HIS A CB  
2982  C CG  . HIS A 429 ? 0.2468 0.1613 0.0961 -0.0030 0.0036  -0.0098 421 HIS A CG  
2983  N ND1 . HIS A 429 ? 0.2802 0.1818 0.1171 -0.0029 0.0039  -0.0143 421 HIS A ND1 
2984  C CD2 . HIS A 429 ? 0.2928 0.2092 0.1359 -0.0029 0.0036  -0.0084 421 HIS A CD2 
2985  C CE1 . HIS A 429 ? 0.3252 0.2219 0.1491 -0.0028 0.0044  -0.0158 421 HIS A CE1 
2986  N NE2 . HIS A 429 ? 0.2922 0.1978 0.1195 -0.0030 0.0042  -0.0121 421 HIS A NE2 
2987  N N   . GLY A 430 ? 0.2801 0.1885 0.1396 -0.0130 -0.0060 -0.0110 422 GLY A N   
2988  C CA  . GLY A 430 ? 0.3131 0.2054 0.1597 -0.0154 -0.0080 -0.0147 422 GLY A CA  
2989  C C   . GLY A 430 ? 0.3091 0.1902 0.1470 -0.0084 -0.0027 -0.0183 422 GLY A C   
2990  O O   . GLY A 430 ? 0.2937 0.1797 0.1322 -0.0035 0.0020  -0.0182 422 GLY A O   
2991  N N   . GLY A 431 ? 0.2931 0.1593 0.1231 -0.0078 -0.0032 -0.0213 423 GLY A N   
2992  C CA  . GLY A 431 ? 0.2986 0.1527 0.1189 -0.0006 0.0012  -0.0257 423 GLY A CA  
2993  C C   . GLY A 431 ? 0.3501 0.2061 0.1793 0.0072  0.0061  -0.0256 423 GLY A C   
2994  O O   . GLY A 431 ? 0.3397 0.1842 0.1610 0.0135  0.0087  -0.0297 423 GLY A O   
2995  N N   . VAL A 432 ? 0.2723 0.1427 0.1175 0.0073  0.0072  -0.0213 424 VAL A N   
2996  C CA  . VAL A 432 ? 0.2753 0.1493 0.1300 0.0141  0.0112  -0.0208 424 VAL A CA  
2997  C C   . VAL A 432 ? 0.3059 0.1855 0.1717 0.0103  0.0080  -0.0169 424 VAL A C   
2998  O O   . VAL A 432 ? 0.2557 0.1426 0.1260 0.0035  0.0046  -0.0140 424 VAL A O   
2999  C CB  . VAL A 432 ? 0.2921 0.1803 0.1554 0.0193  0.0176  -0.0199 424 VAL A CB  
3000  C CG1 . VAL A 432 ? 0.3544 0.2377 0.2062 0.0236  0.0218  -0.0240 424 VAL A CG1 
3001  C CG2 . VAL A 432 ? 0.2693 0.1718 0.1418 0.0144  0.0166  -0.0154 424 VAL A CG2 
3002  N N   . LYS A 433 ? 0.2813 0.1580 0.1515 0.0152  0.0092  -0.0169 425 LYS A N   
3003  C CA  . LYS A 433 ? 0.2551 0.1369 0.1354 0.0125  0.0069  -0.0131 425 LYS A CA  
3004  C C   . LYS A 433 ? 0.2704 0.1643 0.1634 0.0191  0.0115  -0.0118 425 LYS A C   
3005  O O   . LYS A 433 ? 0.2578 0.1467 0.1501 0.0264  0.0135  -0.0138 425 LYS A O   
3006  C CB  . LYS A 433 ? 0.2597 0.1244 0.1314 0.0111  0.0027  -0.0139 425 LYS A CB  
3007  C CG  . LYS A 433 ? 0.3002 0.1689 0.1806 0.0086  0.0006  -0.0100 425 LYS A CG  
3008  C CD  . LYS A 433 ? 0.4143 0.2639 0.2839 0.0059  -0.0041 -0.0102 425 LYS A CD  
3009  C CE  . LYS A 433 ? 0.3543 0.1949 0.2129 -0.0042 -0.0088 -0.0106 425 LYS A CE  
3010  N NZ  . LYS A 433 ? 0.3007 0.1581 0.1689 -0.0127 -0.0099 -0.0071 425 LYS A NZ  
3011  N N   . PRO A 434 ? 0.2666 0.1763 0.1710 0.0172  0.0131  -0.0086 426 PRO A N   
3012  C CA  . PRO A 434 ? 0.2972 0.2184 0.2127 0.0225  0.0174  -0.0075 426 PRO A CA  
3013  C C   . PRO A 434 ? 0.2480 0.1732 0.1727 0.0223  0.0157  -0.0048 426 PRO A C   
3014  O O   . PRO A 434 ? 0.2096 0.1342 0.1353 0.0165  0.0119  -0.0025 426 PRO A O   
3015  C CB  . PRO A 434 ? 0.2374 0.1709 0.1580 0.0198  0.0195  -0.0056 426 PRO A CB  
3016  C CG  . PRO A 434 ? 0.2522 0.1849 0.1710 0.0128  0.0147  -0.0039 426 PRO A CG  
3017  C CD  . PRO A 434 ? 0.2463 0.1639 0.1527 0.0108  0.0113  -0.0065 426 PRO A CD  
3018  N N   . PHE A 435 ? 0.2189 0.1494 0.1505 0.0286  0.0186  -0.0050 427 PHE A N   
3019  C CA  . PHE A 435 ? 0.2004 0.1387 0.1425 0.0286  0.0177  -0.0021 427 PHE A CA  
3020  C C   . PHE A 435 ? 0.2104 0.1634 0.1628 0.0317  0.0223  -0.0015 427 PHE A C   
3021  O O   . PHE A 435 ? 0.1712 0.1270 0.1223 0.0354  0.0265  -0.0037 427 PHE A O   
3022  C CB  . PHE A 435 ? 0.1874 0.1159 0.1271 0.0326  0.0150  -0.0025 427 PHE A CB  
3023  C CG  . PHE A 435 ? 0.1953 0.1230 0.1353 0.0422  0.0178  -0.0055 427 PHE A CG  
3024  C CD1 . PHE A 435 ? 0.1863 0.1278 0.1382 0.0468  0.0205  -0.0047 427 PHE A CD1 
3025  C CD2 . PHE A 435 ? 0.2128 0.1261 0.1411 0.0465  0.0176  -0.0093 427 PHE A CD2 
3026  C CE1 . PHE A 435 ? 0.2063 0.1496 0.1598 0.0561  0.0232  -0.0077 427 PHE A CE1 
3027  C CE2 . PHE A 435 ? 0.2437 0.1570 0.1726 0.0565  0.0204  -0.0126 427 PHE A CE2 
3028  C CZ  . PHE A 435 ? 0.2293 0.1588 0.1715 0.0614  0.0233  -0.0117 427 PHE A CZ  
3029  N N   . GLY A 436 ? 0.1697 0.1322 0.1318 0.0295  0.0217  0.0015  428 GLY A N   
3030  C CA  . GLY A 436 ? 0.1919 0.1680 0.1635 0.0310  0.0255  0.0023  428 GLY A CA  
3031  C C   . GLY A 436 ? 0.1957 0.1785 0.1765 0.0305  0.0237  0.0047  428 GLY A C   
3032  O O   . GLY A 436 ? 0.1503 0.1307 0.1310 0.0262  0.0203  0.0067  428 GLY A O   
3033  N N   . ALA A 437 ? 0.1632 0.1554 0.1520 0.0345  0.0260  0.0046  429 ALA A N   
3034  C CA  . ALA A 437 ? 0.1610 0.1587 0.1576 0.0348  0.0236  0.0066  429 ALA A CA  
3035  C C   . ALA A 437 ? 0.1191 0.1306 0.1252 0.0322  0.0258  0.0081  429 ALA A C   
3036  O O   . ALA A 437 ? 0.1732 0.1917 0.1813 0.0320  0.0300  0.0074  429 ALA A O   
3037  C CB  . ALA A 437 ? 0.1768 0.1730 0.1748 0.0423  0.0226  0.0052  429 ALA A CB  
3038  N N   . THR A 438 ? 0.1177 0.1322 0.1284 0.0294  0.0229  0.0103  430 THR A N   
3039  C CA  . THR A 438 ? 0.1451 0.1716 0.1647 0.0273  0.0239  0.0117  430 THR A CA  
3040  C C   . THR A 438 ? 0.1188 0.1460 0.1418 0.0274  0.0196  0.0133  430 THR A C   
3041  O O   . THR A 438 ? 0.1596 0.1778 0.1776 0.0291  0.0163  0.0135  430 THR A O   
3042  C CB  . THR A 438 ? 0.1136 0.1418 0.1325 0.0213  0.0253  0.0128  430 THR A CB  
3043  O OG1 . THR A 438 ? 0.1243 0.1624 0.1506 0.0187  0.0260  0.0140  430 THR A OG1 
3044  C CG2 . THR A 438 ? 0.1534 0.1739 0.1673 0.0178  0.0222  0.0137  430 THR A CG2 
3045  N N   . PHE A 439 ? 0.1161 0.1535 0.1467 0.0252  0.0194  0.0144  431 PHE A N   
3046  C CA  . PHE A 439 ? 0.1494 0.1870 0.1819 0.0242  0.0151  0.0161  431 PHE A CA  
3047  C C   . PHE A 439 ? 0.1283 0.1576 0.1542 0.0193  0.0132  0.0171  431 PHE A C   
3048  O O   . PHE A 439 ? 0.0918 0.1198 0.1153 0.0158  0.0151  0.0168  431 PHE A O   
3049  C CB  . PHE A 439 ? 0.0913 0.1412 0.1323 0.0216  0.0151  0.0170  431 PHE A CB  
3050  C CG  . PHE A 439 ? 0.1390 0.2008 0.1885 0.0260  0.0165  0.0162  431 PHE A CG  
3051  C CD1 . PHE A 439 ? 0.1757 0.2364 0.2257 0.0336  0.0156  0.0151  431 PHE A CD1 
3052  C CD2 . PHE A 439 ? 0.1980 0.2725 0.2551 0.0223  0.0185  0.0165  431 PHE A CD2 
3053  C CE1 . PHE A 439 ? 0.1731 0.2471 0.2321 0.0385  0.0170  0.0140  431 PHE A CE1 
3054  C CE2 . PHE A 439 ? 0.2300 0.3186 0.2963 0.0258  0.0200  0.0157  431 PHE A CE2 
3055  C CZ  . PHE A 439 ? 0.2144 0.3038 0.2823 0.0344  0.0194  0.0144  431 PHE A CZ  
3056  N N   . LEU A 440 ? 0.0979 0.1222 0.1209 0.0192  0.0093  0.0183  432 LEU A N   
3057  C CA  . LEU A 440 ? 0.1027 0.1213 0.1200 0.0144  0.0079  0.0191  432 LEU A CA  
3058  C C   . LEU A 440 ? 0.1137 0.1380 0.1336 0.0100  0.0091  0.0191  432 LEU A C   
3059  O O   . LEU A 440 ? 0.1168 0.1383 0.1330 0.0070  0.0099  0.0187  432 LEU A O   
3060  C CB  . LEU A 440 ? 0.1020 0.1159 0.1158 0.0141  0.0036  0.0209  432 LEU A CB  
3061  C CG  . LEU A 440 ? 0.1053 0.1154 0.1135 0.0085  0.0027  0.0217  432 LEU A CG  
3062  C CD1 . LEU A 440 ? 0.1127 0.1166 0.1153 0.0069  0.0041  0.0208  432 LEU A CD1 
3063  C CD2 . LEU A 440 ? 0.1314 0.1365 0.1349 0.0075  -0.0014 0.0239  432 LEU A CD2 
3064  N N   . MET A 441 ? 0.1184 0.1505 0.1443 0.0095  0.0091  0.0194  433 MET A N   
3065  C CA  . MET A 441 ? 0.0900 0.1249 0.1168 0.0052  0.0100  0.0191  433 MET A CA  
3066  C C   . MET A 441 ? 0.1201 0.1528 0.1448 0.0044  0.0132  0.0181  433 MET A C   
3067  O O   . MET A 441 ? 0.1010 0.1311 0.1226 0.0020  0.0134  0.0177  433 MET A O   
3068  C CB  . MET A 441 ? 0.0816 0.1249 0.1148 0.0039  0.0096  0.0194  433 MET A CB  
3069  C CG  . MET A 441 ? 0.0901 0.1335 0.1223 -0.0008 0.0100  0.0190  433 MET A CG  
3070  S SD  . MET A 441 ? 0.1292 0.1678 0.1555 -0.0032 0.0073  0.0188  433 MET A SD  
3071  C CE  . MET A 441 ? 0.0865 0.1301 0.1161 -0.0026 0.0033  0.0202  433 MET A CE  
3072  N N   . PHE A 442 ? 0.1126 0.1459 0.1382 0.0068  0.0156  0.0177  434 PHE A N   
3073  C CA  . PHE A 442 ? 0.1233 0.1546 0.1463 0.0057  0.0184  0.0171  434 PHE A CA  
3074  C C   . PHE A 442 ? 0.1071 0.1315 0.1240 0.0066  0.0183  0.0165  434 PHE A C   
3075  O O   . PHE A 442 ? 0.1418 0.1639 0.1556 0.0062  0.0200  0.0162  434 PHE A O   
3076  C CB  . PHE A 442 ? 0.1357 0.1723 0.1622 0.0069  0.0215  0.0170  434 PHE A CB  
3077  C CG  . PHE A 442 ? 0.2339 0.2793 0.2672 0.0051  0.0213  0.0176  434 PHE A CG  
3078  C CD1 . PHE A 442 ? 0.2172 0.2624 0.2506 0.0009  0.0195  0.0182  434 PHE A CD1 
3079  C CD2 . PHE A 442 ? 0.2527 0.3068 0.2923 0.0077  0.0224  0.0174  434 PHE A CD2 
3080  C CE1 . PHE A 442 ? 0.2677 0.3206 0.3068 -0.0017 0.0186  0.0187  434 PHE A CE1 
3081  C CE2 . PHE A 442 ? 0.2911 0.3550 0.3378 0.0054  0.0217  0.0181  434 PHE A CE2 
3082  C CZ  . PHE A 442 ? 0.2909 0.3539 0.3371 0.0002  0.0196  0.0188  434 PHE A CZ  
3083  N N   . SER A 443 ? 0.1026 0.1236 0.1171 0.0070  0.0159  0.0166  435 SER A N   
3084  C CA  . SER A 443 ? 0.1121 0.1287 0.1216 0.0056  0.0151  0.0163  435 SER A CA  
3085  C C   . SER A 443 ? 0.1005 0.1189 0.1100 0.0036  0.0155  0.0160  435 SER A C   
3086  O O   . SER A 443 ? 0.1435 0.1601 0.1499 0.0035  0.0156  0.0154  435 SER A O   
3087  C CB  . SER A 443 ? 0.1054 0.1193 0.1125 0.0044  0.0125  0.0168  435 SER A CB  
3088  O OG  . SER A 443 ? 0.1530 0.1704 0.1621 0.0024  0.0112  0.0175  435 SER A OG  
3089  N N   . GLU A 444 ? 0.1341 0.1555 0.1465 0.0024  0.0153  0.0162  436 GLU A N   
3090  C CA  . GLU A 444 ? 0.1419 0.1630 0.1531 0.0013  0.0153  0.0156  436 GLU A CA  
3091  C C   . GLU A 444 ? 0.1554 0.1739 0.1648 0.0018  0.0170  0.0156  436 GLU A C   
3092  O O   . GLU A 444 ? 0.1558 0.1718 0.1623 0.0022  0.0166  0.0151  436 GLU A O   
3093  C CB  . GLU A 444 ? 0.1120 0.1352 0.1252 -0.0005 0.0145  0.0155  436 GLU A CB  
3094  C CG  . GLU A 444 ? 0.1108 0.1357 0.1238 -0.0013 0.0126  0.0156  436 GLU A CG  
3095  C CD  . GLU A 444 ? 0.1491 0.1754 0.1621 -0.0032 0.0114  0.0151  436 GLU A CD  
3096  O OE1 . GLU A 444 ? 0.1313 0.1571 0.1451 -0.0043 0.0117  0.0147  436 GLU A OE1 
3097  O OE2 . GLU A 444 ? 0.1548 0.1822 0.1661 -0.0042 0.0102  0.0151  436 GLU A OE2 
3098  N N   . TYR A 445 ? 0.1382 0.1573 0.1487 0.0020  0.0188  0.0163  437 TYR A N   
3099  C CA  . TYR A 445 ? 0.1183 0.1344 0.1256 0.0018  0.0206  0.0167  437 TYR A CA  
3100  C C   . TYR A 445 ? 0.1231 0.1357 0.1258 0.0036  0.0205  0.0163  437 TYR A C   
3101  O O   . TYR A 445 ? 0.2035 0.2122 0.2018 0.0037  0.0209  0.0168  437 TYR A O   
3102  C CB  . TYR A 445 ? 0.1193 0.1389 0.1292 0.0011  0.0233  0.0174  437 TYR A CB  
3103  C CG  . TYR A 445 ? 0.1593 0.1822 0.1725 -0.0023 0.0237  0.0182  437 TYR A CG  
3104  C CD1 . TYR A 445 ? 0.1577 0.1830 0.1743 -0.0035 0.0215  0.0179  437 TYR A CD1 
3105  C CD2 . TYR A 445 ? 0.1145 0.1379 0.1266 -0.0050 0.0262  0.0192  437 TYR A CD2 
3106  C CE1 . TYR A 445 ? 0.0894 0.1176 0.1085 -0.0074 0.0214  0.0185  437 TYR A CE1 
3107  C CE2 . TYR A 445 ? 0.1438 0.1703 0.1586 -0.0093 0.0265  0.0201  437 TYR A CE2 
3108  C CZ  . TYR A 445 ? 0.1481 0.1769 0.1665 -0.0105 0.0239  0.0196  437 TYR A CZ  
3109  O OH  . TYR A 445 ? 0.1241 0.1559 0.1447 -0.0156 0.0237  0.0203  437 TYR A OH  
3110  N N   . GLU A 446 ? 0.1191 0.1322 0.1218 0.0048  0.0197  0.0157  438 GLU A N   
3111  C CA  . GLU A 446 ? 0.1745 0.1845 0.1725 0.0058  0.0191  0.0152  438 GLU A CA  
3112  C C   . GLU A 446 ? 0.1196 0.1307 0.1173 0.0052  0.0165  0.0146  438 GLU A C   
3113  O O   . GLU A 446 ? 0.1267 0.1363 0.1214 0.0050  0.0155  0.0141  438 GLU A O   
3114  C CB  . GLU A 446 ? 0.2048 0.2131 0.2012 0.0071  0.0204  0.0146  438 GLU A CB  
3115  C CG  . GLU A 446 ? 0.1268 0.1358 0.1258 0.0076  0.0193  0.0144  438 GLU A CG  
3116  C CD  . GLU A 446 ? 0.1909 0.1958 0.1867 0.0099  0.0199  0.0134  438 GLU A CD  
3117  O OE1 . GLU A 446 ? 0.1643 0.1655 0.1548 0.0104  0.0207  0.0125  438 GLU A OE1 
3118  O OE2 . GLU A 446 ? 0.1758 0.1804 0.1736 0.0114  0.0192  0.0133  438 GLU A OE2 
3119  N N   . ARG A 447 ? 0.1199 0.1339 0.1204 0.0045  0.0156  0.0145  439 ARG A N   
3120  C CA  . ARG A 447 ? 0.1332 0.1505 0.1344 0.0033  0.0139  0.0139  439 ARG A CA  
3121  C C   . ARG A 447 ? 0.1352 0.1540 0.1343 0.0036  0.0126  0.0132  439 ARG A C   
3122  O O   . ARG A 447 ? 0.1046 0.1250 0.1028 0.0016  0.0113  0.0130  439 ARG A O   
3123  C CB  . ARG A 447 ? 0.0828 0.1035 0.0867 0.0030  0.0137  0.0134  439 ARG A CB  
3124  C CG  . ARG A 447 ? 0.1114 0.1373 0.1159 0.0015  0.0126  0.0127  439 ARG A CG  
3125  C CD  . ARG A 447 ? 0.1536 0.1790 0.1572 -0.0013 0.0119  0.0136  439 ARG A CD  
3126  N NE  . ARG A 447 ? 0.1646 0.1956 0.1682 -0.0039 0.0112  0.0131  439 ARG A NE  
3127  C CZ  . ARG A 447 ? 0.1567 0.1890 0.1597 -0.0067 0.0109  0.0138  439 ARG A CZ  
3128  N NH1 . ARG A 447 ? 0.1183 0.1462 0.1208 -0.0066 0.0106  0.0150  439 ARG A NH1 
3129  N NH2 . ARG A 447 ? 0.0846 0.1234 0.0874 -0.0096 0.0109  0.0133  439 ARG A NH2 
3130  N N   . ASN A 448 ? 0.1082 0.1260 0.1059 0.0058  0.0124  0.0131  440 ASN A N   
3131  C CA  . ASN A 448 ? 0.1031 0.1243 0.0997 0.0065  0.0104  0.0124  440 ASN A CA  
3132  C C   . ASN A 448 ? 0.1687 0.1868 0.1612 0.0054  0.0097  0.0126  440 ASN A C   
3133  O O   . ASN A 448 ? 0.1319 0.1539 0.1239 0.0043  0.0076  0.0120  440 ASN A O   
3134  C CB  . ASN A 448 ? 0.1051 0.1254 0.1007 0.0101  0.0095  0.0122  440 ASN A CB  
3135  C CG  . ASN A 448 ? 0.1152 0.1423 0.1119 0.0118  0.0069  0.0111  440 ASN A CG  
3136  O OD1 . ASN A 448 ? 0.1360 0.1616 0.1296 0.0133  0.0052  0.0115  440 ASN A OD1 
3137  N ND2 . ASN A 448 ? 0.1603 0.1961 0.1616 0.0116  0.0067  0.0097  440 ASN A ND2 
3138  N N   . ALA A 449 ? 0.1326 0.1446 0.1223 0.0054  0.0115  0.0132  441 ALA A N   
3139  C CA  . ALA A 449 ? 0.1327 0.1406 0.1174 0.0045  0.0111  0.0129  441 ALA A CA  
3140  C C   . ALA A 449 ? 0.1057 0.1139 0.0903 0.0016  0.0099  0.0123  441 ALA A C   
3141  O O   . ALA A 449 ? 0.1320 0.1386 0.1126 -0.0004 0.0081  0.0117  441 ALA A O   
3142  C CB  . ALA A 449 ? 0.1426 0.1450 0.1244 0.0058  0.0139  0.0132  441 ALA A CB  
3143  N N   . LEU A 450 ? 0.0984 0.1073 0.0864 0.0009  0.0107  0.0127  442 LEU A N   
3144  C CA  . LEU A 450 ? 0.1061 0.1142 0.0931 -0.0024 0.0092  0.0128  442 LEU A CA  
3145  C C   . LEU A 450 ? 0.0996 0.1145 0.0876 -0.0057 0.0071  0.0125  442 LEU A C   
3146  O O   . LEU A 450 ? 0.1293 0.1425 0.1135 -0.0094 0.0053  0.0123  442 LEU A O   
3147  C CB  . LEU A 450 ? 0.1391 0.1478 0.1295 -0.0024 0.0100  0.0136  442 LEU A CB  
3148  C CG  . LEU A 450 ? 0.2760 0.2789 0.2657 -0.0002 0.0109  0.0140  442 LEU A CG  
3149  C CD1 . LEU A 450 ? 0.2229 0.2240 0.2121 0.0031  0.0131  0.0134  442 LEU A CD1 
3150  C CD2 . LEU A 450 ? 0.2293 0.2358 0.2236 -0.0001 0.0112  0.0149  442 LEU A CD2 
3151  N N   . ARG A 451 ? 0.1284 0.1513 0.1211 -0.0043 0.0074  0.0123  443 ARG A N   
3152  C CA  . ARG A 451 ? 0.1018 0.1343 0.0971 -0.0066 0.0058  0.0116  443 ARG A CA  
3153  C C   . ARG A 451 ? 0.1188 0.1525 0.1116 -0.0069 0.0036  0.0111  443 ARG A C   
3154  O O   . ARG A 451 ? 0.1436 0.1832 0.1365 -0.0111 0.0017  0.0108  443 ARG A O   
3155  C CB  . ARG A 451 ? 0.1342 0.1743 0.1347 -0.0033 0.0067  0.0109  443 ARG A CB  
3156  C CG  . ARG A 451 ? 0.1164 0.1690 0.1208 -0.0050 0.0057  0.0099  443 ARG A CG  
3157  C CD  . ARG A 451 ? 0.1174 0.1762 0.1261 -0.0003 0.0067  0.0085  443 ARG A CD  
3158  N NE  . ARG A 451 ? 0.1460 0.2181 0.1589 -0.0022 0.0069  0.0073  443 ARG A NE  
3159  C CZ  . ARG A 451 ? 0.1541 0.2378 0.1709 -0.0010 0.0054  0.0059  443 ARG A CZ  
3160  N NH1 . ARG A 451 ? 0.0985 0.1808 0.1146 0.0025  0.0031  0.0059  443 ARG A NH1 
3161  N NH2 . ARG A 451 ? 0.1211 0.2187 0.1424 -0.0032 0.0063  0.0047  443 ARG A NH2 
3162  N N   . MET A 452 ? 0.1000 0.1286 0.0902 -0.0032 0.0037  0.0111  444 MET A N   
3163  C CA  . MET A 452 ? 0.1197 0.1489 0.1065 -0.0033 0.0012  0.0107  444 MET A CA  
3164  C C   . MET A 452 ? 0.1254 0.1484 0.1061 -0.0078 -0.0000 0.0104  444 MET A C   
3165  O O   . MET A 452 ? 0.1683 0.1948 0.1471 -0.0108 -0.0029 0.0099  444 MET A O   
3166  C CB  . MET A 452 ? 0.1456 0.1692 0.1291 0.0014  0.0017  0.0112  444 MET A CB  
3167  C CG  . MET A 452 ? 0.1631 0.1914 0.1508 0.0057  0.0016  0.0113  444 MET A CG  
3168  S SD  . MET A 452 ? 0.1480 0.1896 0.1404 0.0070  -0.0022 0.0103  444 MET A SD  
3169  C CE  . MET A 452 ? 0.1609 0.1983 0.1461 0.0074  -0.0055 0.0108  444 MET A CE  
3170  N N   . ALA A 453 ? 0.1641 0.1775 0.1412 -0.0082 0.0019  0.0106  445 ALA A N   
3171  C CA  . ALA A 453 ? 0.1737 0.1790 0.1439 -0.0121 0.0005  0.0100  445 ALA A CA  
3172  C C   . ALA A 453 ? 0.1763 0.1868 0.1476 -0.0185 -0.0018 0.0102  445 ALA A C   
3173  O O   . ALA A 453 ? 0.1753 0.1838 0.1415 -0.0232 -0.0045 0.0096  445 ALA A O   
3174  C CB  . ALA A 453 ? 0.1701 0.1649 0.1371 -0.0101 0.0028  0.0100  445 ALA A CB  
3175  N N   . ALA A 454 ? 0.1165 0.1335 0.0936 -0.0194 -0.0007 0.0111  446 ALA A N   
3176  C CA  . ALA A 454 ? 0.1320 0.1550 0.1099 -0.0262 -0.0021 0.0116  446 ALA A CA  
3177  C C   . ALA A 454 ? 0.1464 0.1832 0.1284 -0.0285 -0.0043 0.0109  446 ALA A C   
3178  O O   . ALA A 454 ? 0.1729 0.2127 0.1527 -0.0356 -0.0066 0.0109  446 ALA A O   
3179  C CB  . ALA A 454 ? 0.1335 0.1612 0.1164 -0.0259 -0.0000 0.0126  446 ALA A CB  
3180  N N   . LEU A 455 ? 0.1214 0.1664 0.1091 -0.0227 -0.0038 0.0102  447 LEU A N   
3181  C CA  . LEU A 455 ? 0.1897 0.2488 0.1821 -0.0231 -0.0062 0.0094  447 LEU A CA  
3182  C C   . LEU A 455 ? 0.2073 0.2624 0.1937 -0.0257 -0.0096 0.0089  447 LEU A C   
3183  O O   . LEU A 455 ? 0.1667 0.2325 0.1552 -0.0302 -0.0126 0.0085  447 LEU A O   
3184  C CB  . LEU A 455 ? 0.1427 0.2076 0.1406 -0.0149 -0.0054 0.0089  447 LEU A CB  
3185  C CG  . LEU A 455 ? 0.1781 0.2576 0.1815 -0.0125 -0.0082 0.0079  447 LEU A CG  
3186  C CD1 . LEU A 455 ? 0.1635 0.2590 0.1728 -0.0186 -0.0088 0.0072  447 LEU A CD1 
3187  C CD2 . LEU A 455 ? 0.2253 0.3076 0.2331 -0.0041 -0.0070 0.0073  447 LEU A CD2 
3188  N N   . MET A 456 ? 0.1483 0.1891 0.1272 -0.0229 -0.0093 0.0089  448 MET A N   
3189  C CA  . MET A 456 ? 0.1447 0.1798 0.1161 -0.0251 -0.0124 0.0082  448 MET A CA  
3190  C C   . MET A 456 ? 0.1814 0.2089 0.1458 -0.0332 -0.0140 0.0079  448 MET A C   
3191  O O   . MET A 456 ? 0.1611 0.1842 0.1185 -0.0366 -0.0172 0.0069  448 MET A O   
3192  C CB  . MET A 456 ? 0.2083 0.2309 0.1733 -0.0194 -0.0108 0.0081  448 MET A CB  
3193  C CG  . MET A 456 ? 0.1807 0.2087 0.1491 -0.0130 -0.0109 0.0085  448 MET A CG  
3194  S SD  . MET A 456 ? 0.1900 0.2039 0.1482 -0.0089 -0.0096 0.0086  448 MET A SD  
3195  C CE  . MET A 456 ? 0.1626 0.1725 0.1247 -0.0040 -0.0043 0.0096  448 MET A CE  
3196  N N   . LYS A 457 ? 0.1609 0.1851 0.1256 -0.0365 -0.0123 0.0087  449 LYS A N   
3197  C CA  . LYS A 457 ? 0.1510 0.1645 0.1072 -0.0442 -0.0140 0.0087  449 LYS A CA  
3198  C C   . LYS A 457 ? 0.2164 0.2110 0.1612 -0.0421 -0.0144 0.0074  449 LYS A C   
3199  O O   . LYS A 457 ? 0.1767 0.1629 0.1123 -0.0477 -0.0175 0.0064  449 LYS A O   
3200  C CB  . LYS A 457 ? 0.2332 0.2568 0.1898 -0.0532 -0.0179 0.0086  449 LYS A CB  
3201  C CG  . LYS A 457 ? 0.3055 0.3492 0.2730 -0.0561 -0.0173 0.0094  449 LYS A CG  
3202  C CD  . LYS A 457 ? 0.4384 0.4927 0.4060 -0.0658 -0.0213 0.0092  449 LYS A CD  
3203  C CE  . LYS A 457 ? 0.5186 0.5985 0.4994 -0.0655 -0.0212 0.0090  449 LYS A CE  
3204  N NZ  . LYS A 457 ? 0.5333 0.6254 0.5150 -0.0742 -0.0256 0.0085  449 LYS A NZ  
3205  N N   . ILE A 458 ? 0.2074 0.1957 0.1523 -0.0341 -0.0111 0.0072  450 ILE A N   
3206  C CA  . ILE A 458 ? 0.2337 0.2057 0.1688 -0.0309 -0.0102 0.0057  450 ILE A CA  
3207  C C   . ILE A 458 ? 0.1690 0.1310 0.1027 -0.0284 -0.0079 0.0062  450 ILE A C   
3208  O O   . ILE A 458 ? 0.1670 0.1349 0.1073 -0.0290 -0.0069 0.0079  450 ILE A O   
3209  C CB  . ILE A 458 ? 0.2189 0.1924 0.1545 -0.0240 -0.0082 0.0049  450 ILE A CB  
3210  C CG1 . ILE A 458 ? 0.1499 0.1330 0.0960 -0.0188 -0.0050 0.0065  450 ILE A CG1 
3211  C CG2 . ILE A 458 ? 0.1984 0.1781 0.1321 -0.0264 -0.0116 0.0044  450 ILE A CG2 
3212  C CD1 . ILE A 458 ? 0.1791 0.1619 0.1247 -0.0126 -0.0027 0.0064  450 ILE A CD1 
3213  N N   . ASN A 459 ? 0.2047 0.1516 0.1293 -0.0252 -0.0072 0.0044  451 ASN A N   
3214  C CA  . ASN A 459 ? 0.1989 0.1356 0.1214 -0.0230 -0.0062 0.0048  451 ASN A CA  
3215  C C   . ASN A 459 ? 0.1826 0.1152 0.1060 -0.0140 -0.0024 0.0037  451 ASN A C   
3216  O O   . ASN A 459 ? 0.2562 0.1751 0.1721 -0.0110 -0.0025 0.0022  451 ASN A O   
3217  C CB  . ASN A 459 ? 0.2024 0.1224 0.1120 -0.0283 -0.0098 0.0038  451 ASN A CB  
3218  C CG  . ASN A 459 ? 0.2624 0.1713 0.1608 -0.0274 -0.0108 0.0005  451 ASN A CG  
3219  O OD1 . ASN A 459 ? 0.2372 0.1515 0.1372 -0.0232 -0.0088 -0.0007 451 ASN A OD1 
3220  N ND2 . ASN A 459 ? 0.2855 0.1775 0.1712 -0.0318 -0.0141 -0.0008 451 ASN A ND2 
3221  N N   . PRO A 460 ? 0.1862 0.1300 0.1184 -0.0094 0.0008  0.0043  452 PRO A N   
3222  C CA  . PRO A 460 ? 0.1775 0.1200 0.1125 -0.0021 0.0045  0.0038  452 PRO A CA  
3223  C C   . PRO A 460 ? 0.2150 0.1559 0.1537 -0.0012 0.0041  0.0054  452 PRO A C   
3224  O O   . PRO A 460 ? 0.1887 0.1331 0.1301 -0.0061 0.0020  0.0074  452 PRO A O   
3225  C CB  . PRO A 460 ? 0.1677 0.1230 0.1111 0.0001  0.0073  0.0049  452 PRO A CB  
3226  C CG  . PRO A 460 ? 0.1474 0.1119 0.0959 -0.0050 0.0049  0.0067  452 PRO A CG  
3227  C CD  . PRO A 460 ? 0.1608 0.1193 0.1015 -0.0108 0.0011  0.0058  452 PRO A CD  
3228  N N   . VAL A 461 ? 0.1714 0.1078 0.1101 0.0052  0.0061  0.0044  453 VAL A N   
3229  C CA  . VAL A 461 ? 0.1697 0.1041 0.1114 0.0072  0.0053  0.0059  453 VAL A CA  
3230  C C   . VAL A 461 ? 0.2135 0.1601 0.1662 0.0119  0.0086  0.0067  453 VAL A C   
3231  O O   . VAL A 461 ? 0.1903 0.1387 0.1444 0.0175  0.0118  0.0050  453 VAL A O   
3232  C CB  . VAL A 461 ? 0.2255 0.1437 0.1578 0.0112  0.0037  0.0041  453 VAL A CB  
3233  C CG1 . VAL A 461 ? 0.1936 0.1097 0.1288 0.0136  0.0021  0.0061  453 VAL A CG1 
3234  C CG2 . VAL A 461 ? 0.2302 0.1349 0.1503 0.0052  0.0000  0.0033  453 VAL A CG2 
3235  N N   . PHE A 462 ? 0.1471 0.1024 0.1071 0.0090  0.0081  0.0092  454 PHE A N   
3236  C CA  . PHE A 462 ? 0.1974 0.1636 0.1672 0.0121  0.0105  0.0101  454 PHE A CA  
3237  C C   . PHE A 462 ? 0.1397 0.1033 0.1113 0.0157  0.0092  0.0109  454 PHE A C   
3238  O O   . PHE A 462 ? 0.1454 0.1050 0.1149 0.0127  0.0061  0.0127  454 PHE A O   
3239  C CB  . PHE A 462 ? 0.1634 0.1393 0.1388 0.0076  0.0104  0.0118  454 PHE A CB  
3240  C CG  . PHE A 462 ? 0.1486 0.1272 0.1224 0.0050  0.0109  0.0111  454 PHE A CG  
3241  C CD1 . PHE A 462 ? 0.1822 0.1646 0.1575 0.0075  0.0137  0.0104  454 PHE A CD1 
3242  C CD2 . PHE A 462 ? 0.1466 0.1242 0.1168 -0.0001 0.0084  0.0114  454 PHE A CD2 
3243  C CE1 . PHE A 462 ? 0.1723 0.1561 0.1451 0.0056  0.0135  0.0101  454 PHE A CE1 
3244  C CE2 . PHE A 462 ? 0.1723 0.1534 0.1414 -0.0018 0.0082  0.0108  454 PHE A CE2 
3245  C CZ  . PHE A 462 ? 0.1519 0.1355 0.1220 0.0015  0.0105  0.0102  454 PHE A CZ  
3246  N N   . VAL A 463 ? 0.1401 0.1069 0.1157 0.0220  0.0115  0.0097  455 VAL A N   
3247  C CA  . VAL A 463 ? 0.1542 0.1197 0.1323 0.0269  0.0100  0.0102  455 VAL A CA  
3248  C C   . VAL A 463 ? 0.1648 0.1441 0.1537 0.0270  0.0111  0.0118  455 VAL A C   
3249  O O   . VAL A 463 ? 0.1342 0.1233 0.1288 0.0266  0.0145  0.0113  455 VAL A O   
3250  C CB  . VAL A 463 ? 0.1540 0.1150 0.1296 0.0348  0.0116  0.0073  455 VAL A CB  
3251  C CG1 . VAL A 463 ? 0.1681 0.1292 0.1473 0.0412  0.0095  0.0078  455 VAL A CG1 
3252  C CG2 . VAL A 463 ? 0.2275 0.1726 0.1905 0.0344  0.0101  0.0054  455 VAL A CG2 
3253  N N   . PHE A 464 ? 0.1472 0.1262 0.1379 0.0271  0.0079  0.0138  456 PHE A N   
3254  C CA  . PHE A 464 ? 0.1238 0.1149 0.1238 0.0267  0.0081  0.0152  456 PHE A CA  
3255  C C   . PHE A 464 ? 0.1343 0.1250 0.1366 0.0322  0.0052  0.0160  456 PHE A C   
3256  O O   . PHE A 464 ? 0.1624 0.1417 0.1576 0.0330  0.0014  0.0170  456 PHE A O   
3257  C CB  . PHE A 464 ? 0.1410 0.1339 0.1407 0.0198  0.0067  0.0172  456 PHE A CB  
3258  C CG  . PHE A 464 ? 0.1364 0.1311 0.1350 0.0155  0.0090  0.0165  456 PHE A CG  
3259  C CD1 . PHE A 464 ? 0.1089 0.1119 0.1128 0.0156  0.0123  0.0157  456 PHE A CD1 
3260  C CD2 . PHE A 464 ? 0.2028 0.1907 0.1944 0.0114  0.0077  0.0166  456 PHE A CD2 
3261  C CE1 . PHE A 464 ? 0.1046 0.1080 0.1065 0.0125  0.0139  0.0152  456 PHE A CE1 
3262  C CE2 . PHE A 464 ? 0.1508 0.1415 0.1420 0.0083  0.0094  0.0159  456 PHE A CE2 
3263  C CZ  . PHE A 464 ? 0.1287 0.1266 0.1248 0.0094  0.0123  0.0152  456 PHE A CZ  
3264  N N   . THR A 465 ? 0.1300 0.1331 0.1419 0.0357  0.0067  0.0156  457 THR A N   
3265  C CA  . THR A 465 ? 0.1293 0.1350 0.1451 0.0412  0.0034  0.0164  457 THR A CA  
3266  C C   . THR A 465 ? 0.1436 0.1616 0.1676 0.0377  0.0023  0.0183  457 THR A C   
3267  O O   . THR A 465 ? 0.1405 0.1639 0.1666 0.0316  0.0045  0.0185  457 THR A O   
3268  C CB  . THR A 465 ? 0.1868 0.1978 0.2074 0.0499  0.0056  0.0138  457 THR A CB  
3269  O OG1 . THR A 465 ? 0.1418 0.1690 0.1721 0.0484  0.0101  0.0129  457 THR A OG1 
3270  C CG2 . THR A 465 ? 0.1558 0.1539 0.1671 0.0533  0.0071  0.0113  457 THR A CG2 
3271  N N   . HIS A 466 ? 0.1242 0.1452 0.1516 0.0417  -0.0017 0.0195  458 HIS A N   
3272  C CA  . HIS A 466 ? 0.1266 0.1589 0.1611 0.0385  -0.0036 0.0212  458 HIS A CA  
3273  C C   . HIS A 466 ? 0.1144 0.1410 0.1427 0.0304  -0.0049 0.0230  458 HIS A C   
3274  O O   . HIS A 466 ? 0.1318 0.1641 0.1626 0.0248  -0.0025 0.0227  458 HIS A O   
3275  C CB  . HIS A 466 ? 0.1202 0.1689 0.1655 0.0373  0.0005  0.0198  458 HIS A CB  
3276  C CG  . HIS A 466 ? 0.1534 0.2117 0.2063 0.0451  0.0022  0.0180  458 HIS A CG  
3277  N ND1 . HIS A 466 ? 0.1943 0.2462 0.2434 0.0511  0.0046  0.0157  458 HIS A ND1 
3278  C CD2 . HIS A 466 ? 0.2334 0.3082 0.2977 0.0480  0.0018  0.0177  458 HIS A CD2 
3279  C CE1 . HIS A 466 ? 0.2383 0.3025 0.2962 0.0580  0.0061  0.0140  458 HIS A CE1 
3280  N NE2 . HIS A 466 ? 0.2069 0.2862 0.2748 0.0561  0.0044  0.0153  458 HIS A NE2 
3281  N N   . ASP A 467 ? 0.1229 0.1372 0.1422 0.0301  -0.0088 0.0248  459 ASP A N   
3282  C CA  . ASP A 467 ? 0.1221 0.1294 0.1336 0.0228  -0.0090 0.0259  459 ASP A CA  
3283  C C   . ASP A 467 ? 0.1273 0.1381 0.1384 0.0183  -0.0119 0.0279  459 ASP A C   
3284  O O   . ASP A 467 ? 0.1542 0.1610 0.1592 0.0125  -0.0116 0.0286  459 ASP A O   
3285  C CB  . ASP A 467 ? 0.1358 0.1273 0.1362 0.0230  -0.0111 0.0269  459 ASP A CB  
3286  C CG  . ASP A 467 ? 0.1967 0.1803 0.1917 0.0257  -0.0169 0.0296  459 ASP A CG  
3287  O OD1 . ASP A 467 ? 0.2136 0.2033 0.2148 0.0318  -0.0191 0.0297  459 ASP A OD1 
3288  O OD2 . ASP A 467 ? 0.2158 0.1877 0.2003 0.0214  -0.0193 0.0317  459 ASP A OD2 
3289  N N   . SER A 468 ? 0.1284 0.1472 0.1455 0.0208  -0.0147 0.0287  460 SER A N   
3290  C CA  . SER A 468 ? 0.1808 0.2012 0.1954 0.0165  -0.0180 0.0306  460 SER A CA  
3291  C C   . SER A 468 ? 0.1872 0.2209 0.2116 0.0181  -0.0198 0.0304  460 SER A C   
3292  O O   . SER A 468 ? 0.1138 0.1565 0.1472 0.0219  -0.0178 0.0289  460 SER A O   
3293  C CB  . SER A 468 ? 0.1520 0.1603 0.1564 0.0169  -0.0230 0.0336  460 SER A CB  
3294  O OG  . SER A 468 ? 0.1419 0.1503 0.1487 0.0242  -0.0276 0.0348  460 SER A OG  
3295  N N   . ILE A 469 ? 0.1201 0.1557 0.1421 0.0146  -0.0235 0.0320  461 ILE A N   
3296  C CA  . ILE A 469 ? 0.1190 0.1668 0.1494 0.0159  -0.0267 0.0323  461 ILE A CA  
3297  C C   . ILE A 469 ? 0.1567 0.2075 0.1924 0.0246  -0.0300 0.0331  461 ILE A C   
3298  O O   . ILE A 469 ? 0.1291 0.1936 0.1751 0.0271  -0.0317 0.0327  461 ILE A O   
3299  C CB  . ILE A 469 ? 0.1400 0.1867 0.1643 0.0110  -0.0311 0.0340  461 ILE A CB  
3300  C CG1 . ILE A 469 ? 0.1346 0.1675 0.1468 0.0115  -0.0347 0.0369  461 ILE A CG1 
3301  C CG2 . ILE A 469 ? 0.1201 0.1680 0.1423 0.0035  -0.0275 0.0321  461 ILE A CG2 
3302  C CD1 . ILE A 469 ? 0.1749 0.2065 0.1801 0.0079  -0.0401 0.0392  461 ILE A CD1 
3303  N N   . GLY A 470 ? 0.1722 0.2105 0.2011 0.0295  -0.0310 0.0339  462 GLY A N   
3304  C CA  . GLY A 470 ? 0.2068 0.2460 0.2398 0.0392  -0.0338 0.0341  462 GLY A CA  
3305  C C   . GLY A 470 ? 0.1331 0.1861 0.1787 0.0437  -0.0294 0.0310  462 GLY A C   
3306  O O   . GLY A 470 ? 0.1437 0.2027 0.1957 0.0524  -0.0316 0.0306  462 GLY A O   
3307  N N   . LEU A 471 ? 0.1224 0.1809 0.1715 0.0383  -0.0233 0.0290  463 LEU A N   
3308  C CA  . LEU A 471 ? 0.1506 0.2233 0.2112 0.0413  -0.0189 0.0265  463 LEU A CA  
3309  C C   . LEU A 471 ? 0.1277 0.2194 0.2003 0.0406  -0.0211 0.0267  463 LEU A C   
3310  O O   . LEU A 471 ? 0.1103 0.2165 0.1938 0.0447  -0.0188 0.0251  463 LEU A O   
3311  C CB  . LEU A 471 ? 0.1082 0.1796 0.1676 0.0355  -0.0122 0.0247  463 LEU A CB  
3312  C CG  . LEU A 471 ? 0.1004 0.1745 0.1593 0.0260  -0.0104 0.0247  463 LEU A CG  
3313  C CD1 . LEU A 471 ? 0.0953 0.1869 0.1656 0.0234  -0.0095 0.0242  463 LEU A CD1 
3314  C CD2 . LEU A 471 ? 0.0965 0.1627 0.1498 0.0224  -0.0052 0.0234  463 LEU A CD2 
3315  N N   . GLY A 472 ? 0.1124 0.2052 0.1832 0.0351  -0.0253 0.0285  464 GLY A N   
3316  C CA  . GLY A 472 ? 0.1115 0.2214 0.1926 0.0347  -0.0290 0.0290  464 GLY A CA  
3317  C C   . GLY A 472 ? 0.1072 0.2302 0.1959 0.0267  -0.0252 0.0276  464 GLY A C   
3318  O O   . GLY A 472 ? 0.0992 0.2151 0.1815 0.0187  -0.0231 0.0274  464 GLY A O   
3319  N N   . GLU A 473 ? 0.1003 0.2423 0.2023 0.0289  -0.0243 0.0266  465 GLU A N   
3320  C CA  . GLU A 473 ? 0.0953 0.2524 0.2054 0.0206  -0.0234 0.0262  465 GLU A CA  
3321  C C   . GLU A 473 ? 0.0899 0.2422 0.1964 0.0125  -0.0169 0.0249  465 GLU A C   
3322  O O   . GLU A 473 ? 0.0883 0.2459 0.1963 0.0037  -0.0170 0.0249  465 GLU A O   
3323  C CB  . GLU A 473 ? 0.0948 0.2750 0.2206 0.0251  -0.0235 0.0254  465 GLU A CB  
3324  C CG  . GLU A 473 ? 0.1005 0.2897 0.2317 0.0309  -0.0316 0.0269  465 GLU A CG  
3325  C CD  . GLU A 473 ? 0.1075 0.2908 0.2374 0.0442  -0.0340 0.0271  465 GLU A CD  
3326  O OE1 . GLU A 473 ? 0.1133 0.2798 0.2341 0.0478  -0.0306 0.0265  465 GLU A OE1 
3327  O OE2 . GLU A 473 ? 0.1127 0.3076 0.2502 0.0509  -0.0400 0.0279  465 GLU A OE2 
3328  N N   . ASP A 474 ? 0.0884 0.2308 0.1900 0.0152  -0.0116 0.0239  466 ASP A N   
3329  C CA  . ASP A 474 ? 0.1004 0.2381 0.1982 0.0081  -0.0060 0.0230  466 ASP A CA  
3330  C C   . ASP A 474 ? 0.1294 0.2551 0.2176 0.0004  -0.0077 0.0234  466 ASP A C   
3331  O O   . ASP A 474 ? 0.0854 0.2092 0.1714 -0.0066 -0.0047 0.0228  466 ASP A O   
3332  C CB  . ASP A 474 ? 0.0841 0.2116 0.1766 0.0127  -0.0010 0.0219  466 ASP A CB  
3333  C CG  . ASP A 474 ? 0.1738 0.3141 0.2750 0.0169  0.0037  0.0205  466 ASP A CG  
3334  O OD1 . ASP A 474 ? 0.1181 0.2768 0.2304 0.0155  0.0038  0.0204  466 ASP A OD1 
3335  O OD2 . ASP A 474 ? 0.1522 0.2847 0.2489 0.0214  0.0074  0.0194  466 ASP A OD2 
3336  N N   . GLY A 475 ? 0.1060 0.2232 0.1876 0.0015  -0.0124 0.0244  467 GLY A N   
3337  C CA  . GLY A 475 ? 0.0893 0.1989 0.1632 -0.0055 -0.0145 0.0244  467 GLY A CA  
3338  C C   . GLY A 475 ? 0.0886 0.1824 0.1516 -0.0073 -0.0114 0.0236  467 GLY A C   
3339  O O   . GLY A 475 ? 0.0868 0.1743 0.1474 -0.0034 -0.0080 0.0233  467 GLY A O   
3340  N N   . PRO A 476 ? 0.0907 0.1785 0.1470 -0.0131 -0.0127 0.0230  468 PRO A N   
3341  C CA  . PRO A 476 ? 0.0911 0.1654 0.1371 -0.0137 -0.0108 0.0221  468 PRO A CA  
3342  C C   . PRO A 476 ? 0.0880 0.1570 0.1325 -0.0139 -0.0054 0.0209  468 PRO A C   
3343  O O   . PRO A 476 ? 0.1194 0.1795 0.1573 -0.0125 -0.0038 0.0204  468 PRO A O   
3344  C CB  . PRO A 476 ? 0.0956 0.1667 0.1357 -0.0196 -0.0134 0.0211  468 PRO A CB  
3345  C CG  . PRO A 476 ? 0.0968 0.1782 0.1440 -0.0240 -0.0150 0.0211  468 PRO A CG  
3346  C CD  . PRO A 476 ? 0.0941 0.1877 0.1517 -0.0192 -0.0163 0.0228  468 PRO A CD  
3347  N N   . THR A 477 ? 0.0882 0.1628 0.1381 -0.0157 -0.0028 0.0206  469 THR A N   
3348  C CA  . THR A 477 ? 0.1138 0.1822 0.1608 -0.0153 0.0019  0.0199  469 THR A CA  
3349  C C   . THR A 477 ? 0.1666 0.2338 0.2144 -0.0091 0.0039  0.0203  469 THR A C   
3350  O O   . THR A 477 ? 0.1228 0.1827 0.1659 -0.0081 0.0067  0.0197  469 THR A O   
3351  C CB  . THR A 477 ? 0.0970 0.1708 0.1481 -0.0195 0.0045  0.0199  469 THR A CB  
3352  O OG1 . THR A 477 ? 0.1175 0.2045 0.1783 -0.0172 0.0052  0.0208  469 THR A OG1 
3353  C CG2 . THR A 477 ? 0.1310 0.2039 0.1800 -0.0267 0.0024  0.0195  469 THR A CG2 
3354  N N   . HIS A 478 ? 0.1056 0.1792 0.1586 -0.0047 0.0020  0.0212  470 HIS A N   
3355  C CA  . HIS A 478 ? 0.0929 0.1641 0.1458 0.0014  0.0035  0.0212  470 HIS A CA  
3356  C C   . HIS A 478 ? 0.1131 0.1767 0.1605 0.0046  0.0002  0.0220  470 HIS A C   
3357  O O   . HIS A 478 ? 0.1234 0.1801 0.1670 0.0080  0.0014  0.0219  470 HIS A O   
3358  C CB  . HIS A 478 ? 0.0821 0.1652 0.1443 0.0054  0.0042  0.0212  470 HIS A CB  
3359  C CG  . HIS A 478 ? 0.2571 0.3462 0.3230 0.0032  0.0091  0.0204  470 HIS A CG  
3360  N ND1 . HIS A 478 ? 0.2756 0.3660 0.3411 -0.0040 0.0103  0.0205  470 HIS A ND1 
3361  C CD2 . HIS A 478 ? 0.2802 0.3733 0.3490 0.0068  0.0131  0.0196  470 HIS A CD2 
3362  C CE1 . HIS A 478 ? 0.3185 0.4133 0.3863 -0.0052 0.0147  0.0202  470 HIS A CE1 
3363  N NE2 . HIS A 478 ? 0.2823 0.3796 0.3523 0.0013  0.0167  0.0196  470 HIS A NE2 
3364  N N   . GLN A 479 ? 0.0980 0.1624 0.1443 0.0030  -0.0041 0.0231  471 GLN A N   
3365  C CA  . GLN A 479 ? 0.0920 0.1491 0.1322 0.0052  -0.0077 0.0245  471 GLN A CA  
3366  C C   . GLN A 479 ? 0.1193 0.1662 0.1503 0.0023  -0.0062 0.0241  471 GLN A C   
3367  O O   . GLN A 479 ? 0.0998 0.1459 0.1276 -0.0023 -0.0061 0.0234  471 GLN A O   
3368  C CB  . GLN A 479 ? 0.0955 0.1569 0.1363 0.0036  -0.0128 0.0258  471 GLN A CB  
3369  C CG  . GLN A 479 ? 0.0966 0.1694 0.1470 0.0077  -0.0154 0.0265  471 GLN A CG  
3370  C CD  . GLN A 479 ? 0.1346 0.2145 0.1871 0.0043  -0.0200 0.0273  471 GLN A CD  
3371  O OE1 . GLN A 479 ? 0.0988 0.1754 0.1459 -0.0017 -0.0204 0.0268  471 GLN A OE1 
3372  N NE2 . GLN A 479 ? 0.1011 0.1913 0.1613 0.0084  -0.0238 0.0283  471 GLN A NE2 
3373  N N   . PRO A 480 ? 0.1360 0.1753 0.1626 0.0047  -0.0052 0.0244  472 PRO A N   
3374  C CA  . PRO A 480 ? 0.0947 0.1268 0.1136 0.0015  -0.0040 0.0241  472 PRO A CA  
3375  C C   . PRO A 480 ? 0.1155 0.1451 0.1285 -0.0016 -0.0072 0.0254  472 PRO A C   
3376  O O   . PRO A 480 ? 0.1389 0.1680 0.1510 -0.0001 -0.0111 0.0273  472 PRO A O   
3377  C CB  . PRO A 480 ? 0.1149 0.1398 0.1304 0.0045  -0.0034 0.0244  472 PRO A CB  
3378  C CG  . PRO A 480 ? 0.0969 0.1261 0.1191 0.0094  -0.0020 0.0236  472 PRO A CG  
3379  C CD  . PRO A 480 ? 0.1083 0.1458 0.1366 0.0104  -0.0048 0.0244  472 PRO A CD  
3380  N N   . ILE A 481 ? 0.0979 0.1265 0.1066 -0.0056 -0.0054 0.0243  473 ILE A N   
3381  C CA  . ILE A 481 ? 0.1556 0.1822 0.1573 -0.0092 -0.0073 0.0252  473 ILE A CA  
3382  C C   . ILE A 481 ? 0.1307 0.1538 0.1271 -0.0115 -0.0048 0.0247  473 ILE A C   
3383  O O   . ILE A 481 ? 0.1226 0.1407 0.1127 -0.0131 -0.0062 0.0267  473 ILE A O   
3384  C CB  . ILE A 481 ? 0.1199 0.1509 0.1217 -0.0120 -0.0075 0.0236  473 ILE A CB  
3385  C CG1 . ILE A 481 ? 0.1019 0.1378 0.1096 -0.0108 -0.0104 0.0241  473 ILE A CG1 
3386  C CG2 . ILE A 481 ? 0.1189 0.1479 0.1121 -0.0158 -0.0088 0.0241  473 ILE A CG2 
3387  C CD1 . ILE A 481 ? 0.1084 0.1435 0.1142 -0.0097 -0.0153 0.0270  473 ILE A CD1 
3388  N N   . GLU A 482 ? 0.1426 0.1684 0.1412 -0.0117 -0.0013 0.0222  474 GLU A N   
3389  C CA  . GLU A 482 ? 0.1339 0.1597 0.1290 -0.0138 0.0012  0.0213  474 GLU A CA  
3390  C C   . GLU A 482 ? 0.1300 0.1537 0.1269 -0.0120 0.0027  0.0211  474 GLU A C   
3391  O O   . GLU A 482 ? 0.1157 0.1404 0.1103 -0.0140 0.0043  0.0205  474 GLU A O   
3392  C CB  . GLU A 482 ? 0.0974 0.1277 0.0930 -0.0144 0.0036  0.0183  474 GLU A CB  
3393  C CG  . GLU A 482 ? 0.0898 0.1208 0.0906 -0.0115 0.0053  0.0164  474 GLU A CG  
3394  C CD  . GLU A 482 ? 0.1713 0.2025 0.1754 -0.0110 0.0039  0.0164  474 GLU A CD  
3395  O OE1 . GLU A 482 ? 0.1459 0.1773 0.1511 -0.0111 0.0013  0.0183  474 GLU A OE1 
3396  O OE2 . GLU A 482 ? 0.1579 0.1890 0.1633 -0.0106 0.0052  0.0145  474 GLU A OE2 
3397  N N   . GLN A 483 ? 0.1468 0.1121 0.1056 -0.0264 0.0085  -0.0033 475 GLN A N   
3398  C CA  . GLN A 483 ? 0.1305 0.1064 0.1029 -0.0198 0.0139  -0.0022 475 GLN A CA  
3399  C C   . GLN A 483 ? 0.1868 0.1718 0.1646 -0.0153 0.0156  -0.0012 475 GLN A C   
3400  O O   . GLN A 483 ? 0.1289 0.1164 0.1084 -0.0101 0.0208  -0.0015 475 GLN A O   
3401  C CB  . GLN A 483 ? 0.1221 0.1069 0.1096 -0.0214 0.0114  0.0008  475 GLN A CB  
3402  C CG  . GLN A 483 ? 0.1472 0.1239 0.1322 -0.0251 0.0119  0.0005  475 GLN A CG  
3403  C CD  . GLN A 483 ? 0.1521 0.1171 0.1258 -0.0339 0.0051  -0.0005 475 GLN A CD  
3404  O OE1 . GLN A 483 ? 0.1929 0.1617 0.1679 -0.0385 -0.0023 0.0014  475 GLN A OE1 
3405  N NE2 . GLN A 483 ? 0.1916 0.1402 0.1521 -0.0365 0.0070  -0.0033 475 GLN A NE2 
3406  N N   . THR A 484 ? 0.1362 0.1260 0.1173 -0.0176 0.0104  0.0008  476 THR A N   
3407  C CA  . THR A 484 ? 0.1487 0.1446 0.1338 -0.0144 0.0115  0.0019  476 THR A CA  
3408  C C   . THR A 484 ? 0.1215 0.1133 0.0976 -0.0125 0.0167  0.0009  476 THR A C   
3409  O O   . THR A 484 ? 0.1487 0.1464 0.1307 -0.0091 0.0198  0.0019  476 THR A O   
3410  C CB  . THR A 484 ? 0.2036 0.2027 0.1921 -0.0170 0.0053  0.0048  476 THR A CB  
3411  O OG1 . THR A 484 ? 0.1420 0.1475 0.1433 -0.0170 0.0024  0.0071  476 THR A OG1 
3412  C CG2 . THR A 484 ? 0.1355 0.1380 0.1268 -0.0145 0.0066  0.0060  476 THR A CG2 
3413  N N   . ALA A 485 ? 0.1304 0.1114 0.0915 -0.0149 0.0178  -0.0005 477 ALA A N   
3414  C CA  . ALA A 485 ? 0.1583 0.1348 0.1108 -0.0117 0.0256  -0.0008 477 ALA A CA  
3415  C C   . ALA A 485 ? 0.1349 0.1136 0.0933 -0.0058 0.0327  -0.0010 477 ALA A C   
3416  O O   . ALA A 485 ? 0.1465 0.1314 0.1105 -0.0017 0.0384  0.0015  477 ALA A O   
3417  C CB  . ALA A 485 ? 0.1616 0.1213 0.0918 -0.0149 0.0267  -0.0031 477 ALA A CB  
3418  N N   . THR A 486 ? 0.1520 0.1264 0.1104 -0.0054 0.0324  -0.0029 478 THR A N   
3419  C CA  . THR A 486 ? 0.1539 0.1299 0.1178 0.0007  0.0386  -0.0020 478 THR A CA  
3420  C C   . THR A 486 ? 0.1634 0.1545 0.1436 0.0029  0.0361  0.0011  478 THR A C   
3421  O O   . THR A 486 ? 0.1343 0.1316 0.1217 0.0076  0.0399  0.0040  478 THR A O   
3422  C CB  . THR A 486 ? 0.1417 0.1068 0.0999 0.0001  0.0390  -0.0043 478 THR A CB  
3423  O OG1 . THR A 486 ? 0.1476 0.1187 0.1139 -0.0038 0.0324  -0.0039 478 THR A OG1 
3424  C CG2 . THR A 486 ? 0.1672 0.1128 0.1051 -0.0035 0.0403  -0.0080 478 THR A CG2 
3425  N N   . LEU A 487 ? 0.1079 0.1042 0.0934 -0.0004 0.0298  0.0009  479 LEU A N   
3426  C CA  . LEU A 487 ? 0.1145 0.1202 0.1098 0.0011  0.0273  0.0028  479 LEU A CA  
3427  C C   . LEU A 487 ? 0.1628 0.1756 0.1633 0.0011  0.0270  0.0054  479 LEU A C   
3428  O O   . LEU A 487 ? 0.1380 0.1575 0.1455 0.0023  0.0254  0.0078  479 LEU A O   
3429  C CB  . LEU A 487 ? 0.1139 0.1206 0.1116 -0.0013 0.0227  0.0018  479 LEU A CB  
3430  C CG  . LEU A 487 ? 0.1372 0.1406 0.1347 -0.0016 0.0233  0.0011  479 LEU A CG  
3431  C CD1 . LEU A 487 ? 0.1913 0.1972 0.1939 -0.0033 0.0206  0.0016  479 LEU A CD1 
3432  C CD2 . LEU A 487 ? 0.1441 0.1478 0.1421 0.0019  0.0257  0.0020  479 LEU A CD2 
3433  N N   . ARG A 488 ? 0.1105 0.1216 0.1071 -0.0011 0.0278  0.0056  480 ARG A N   
3434  C CA  . ARG A 488 ? 0.1220 0.1401 0.1245 -0.0019 0.0282  0.0091  480 ARG A CA  
3435  C C   . ARG A 488 ? 0.1409 0.1651 0.1501 0.0022  0.0345  0.0130  480 ARG A C   
3436  O O   . ARG A 488 ? 0.1364 0.1703 0.1559 0.0012  0.0341  0.0176  480 ARG A O   
3437  C CB  . ARG A 488 ? 0.1579 0.1713 0.1527 -0.0049 0.0287  0.0093  480 ARG A CB  
3438  C CG  . ARG A 488 ? 0.1224 0.1334 0.1160 -0.0086 0.0217  0.0082  480 ARG A CG  
3439  C CD  . ARG A 488 ? 0.1314 0.1363 0.1149 -0.0115 0.0213  0.0091  480 ARG A CD  
3440  N NE  . ARG A 488 ? 0.1324 0.1363 0.1176 -0.0140 0.0145  0.0098  480 ARG A NE  
3441  C CZ  . ARG A 488 ? 0.1540 0.1527 0.1319 -0.0165 0.0104  0.0102  480 ARG A CZ  
3442  N NH1 . ARG A 488 ? 0.1701 0.1613 0.1349 -0.0180 0.0119  0.0087  480 ARG A NH1 
3443  N NH2 . ARG A 488 ? 0.1530 0.1526 0.1362 -0.0174 0.0046  0.0122  480 ARG A NH2 
3444  N N   . LEU A 489 ? 0.1058 0.1246 0.1107 0.0068  0.0402  0.0120  481 LEU A N   
3445  C CA  . LEU A 489 ? 0.1323 0.1567 0.1450 0.0127  0.0478  0.0166  481 LEU A CA  
3446  C C   . LEU A 489 ? 0.1625 0.1968 0.1884 0.0152  0.0441  0.0204  481 LEU A C   
3447  O O   . LEU A 489 ? 0.1233 0.1656 0.1604 0.0205  0.0491  0.0262  481 LEU A O   
3448  C CB  . LEU A 489 ? 0.1246 0.1347 0.1239 0.0174  0.0569  0.0139  481 LEU A CB  
3449  C CG  . LEU A 489 ? 0.2182 0.2154 0.1996 0.0143  0.0599  0.0102  481 LEU A CG  
3450  C CD1 . LEU A 489 ? 0.2545 0.2335 0.2189 0.0190  0.0695  0.0072  481 LEU A CD1 
3451  C CD2 . LEU A 489 ? 0.1921 0.1977 0.1785 0.0133  0.0630  0.0147  481 LEU A CD2 
3452  N N   . ILE A 490 ? 0.1113 0.1450 0.1358 0.0120  0.0359  0.0181  482 ILE A N   
3453  C CA  . ILE A 490 ? 0.1044 0.1451 0.1369 0.0133  0.0310  0.0217  482 ILE A CA  
3454  C C   . ILE A 490 ? 0.0904 0.1445 0.1361 0.0099  0.0254  0.0273  482 ILE A C   
3455  O O   . ILE A 490 ? 0.1136 0.1668 0.1568 0.0039  0.0202  0.0253  482 ILE A O   
3456  C CB  . ILE A 490 ? 0.1274 0.1608 0.1508 0.0108  0.0253  0.0174  482 ILE A CB  
3457  C CG1 . ILE A 490 ? 0.0995 0.1214 0.1131 0.0129  0.0302  0.0133  482 ILE A CG1 
3458  C CG2 . ILE A 490 ? 0.1554 0.1939 0.1828 0.0116  0.0196  0.0213  482 ILE A CG2 
3459  C CD1 . ILE A 490 ? 0.1257 0.1420 0.1326 0.0106  0.0267  0.0102  482 ILE A CD1 
3460  N N   . PRO A 491 ? 0.0958 0.1622 0.1564 0.0130  0.0257  0.0350  483 PRO A N   
3461  C CA  . PRO A 491 ? 0.1326 0.2131 0.2079 0.0078  0.0185  0.0415  483 PRO A CA  
3462  C C   . PRO A 491 ? 0.1646 0.2407 0.2320 0.0008  0.0059  0.0389  483 PRO A C   
3463  O O   . PRO A 491 ? 0.1527 0.2209 0.2096 0.0024  0.0030  0.0359  483 PRO A O   
3464  C CB  . PRO A 491 ? 0.1710 0.2664 0.2656 0.0137  0.0209  0.0515  483 PRO A CB  
3465  C CG  . PRO A 491 ? 0.1599 0.2468 0.2488 0.0235  0.0342  0.0494  483 PRO A CG  
3466  C CD  . PRO A 491 ? 0.1220 0.1903 0.1885 0.0216  0.0328  0.0391  483 PRO A CD  
3467  N N   . ASN A 492 ? 0.1090 0.1876 0.1792 -0.0070 -0.0009 0.0398  484 ASN A N   
3468  C CA  . ASN A 492 ? 0.1444 0.2149 0.2039 -0.0142 -0.0126 0.0369  484 ASN A CA  
3469  C C   . ASN A 492 ? 0.1965 0.2489 0.2348 -0.0130 -0.0109 0.0273  484 ASN A C   
3470  O O   . ASN A 492 ? 0.1389 0.1816 0.1641 -0.0148 -0.0169 0.0244  484 ASN A O   
3471  C CB  . ASN A 492 ? 0.1738 0.2509 0.2378 -0.0154 -0.0220 0.0427  484 ASN A CB  
3472  C CG  . ASN A 492 ? 0.1990 0.2675 0.2516 -0.0250 -0.0356 0.0412  484 ASN A CG  
3473  O OD1 . ASN A 492 ? 0.1655 0.2328 0.2199 -0.0324 -0.0398 0.0411  484 ASN A OD1 
3474  N ND2 . ASN A 492 ? 0.1571 0.2166 0.1948 -0.0252 -0.0421 0.0396  484 ASN A ND2 
3475  N N   . MET A 493 ? 0.1494 0.1968 0.1840 -0.0099 -0.0026 0.0231  485 MET A N   
3476  C CA  . MET A 493 ? 0.1907 0.2245 0.2107 -0.0087 -0.0005 0.0159  485 MET A CA  
3477  C C   . MET A 493 ? 0.1872 0.2168 0.2058 -0.0118 0.0003  0.0138  485 MET A C   
3478  O O   . MET A 493 ? 0.1624 0.1978 0.1880 -0.0118 0.0043  0.0163  485 MET A O   
3479  C CB  . MET A 493 ? 0.1604 0.1922 0.1780 -0.0027 0.0072  0.0139  485 MET A CB  
3480  C CG  . MET A 493 ? 0.1565 0.1781 0.1643 -0.0020 0.0097  0.0084  485 MET A CG  
3481  S SD  . MET A 493 ? 0.1760 0.1879 0.1719 -0.0017 0.0068  0.0056  485 MET A SD  
3482  C CE  . MET A 493 ? 0.1743 0.1870 0.1692 0.0028  0.0107  0.0072  485 MET A CE  
3483  N N   . ASP A 494 ? 0.1489 0.1671 0.1573 -0.0137 -0.0027 0.0097  486 ASP A N   
3484  C CA  . ASP A 494 ? 0.1806 0.1927 0.1869 -0.0151 -0.0017 0.0079  486 ASP A CA  
3485  C C   . ASP A 494 ? 0.2129 0.2208 0.2154 -0.0104 0.0035  0.0047  486 ASP A C   
3486  O O   . ASP A 494 ? 0.1802 0.1828 0.1768 -0.0074 0.0048  0.0021  486 ASP A O   
3487  C CB  . ASP A 494 ? 0.1780 0.1780 0.1759 -0.0192 -0.0074 0.0059  486 ASP A CB  
3488  C CG  . ASP A 494 ? 0.1793 0.1830 0.1831 -0.0267 -0.0140 0.0100  486 ASP A CG  
3489  O OD1 . ASP A 494 ? 0.2094 0.2275 0.2265 -0.0279 -0.0129 0.0154  486 ASP A OD1 
3490  O OD2 . ASP A 494 ? 0.2511 0.2422 0.2456 -0.0314 -0.0199 0.0081  486 ASP A OD2 
3491  N N   . VAL A 495 ? 0.1404 0.1506 0.1461 -0.0103 0.0060  0.0057  487 VAL A N   
3492  C CA  . VAL A 495 ? 0.1382 0.1459 0.1425 -0.0076 0.0086  0.0042  487 VAL A CA  
3493  C C   . VAL A 495 ? 0.1381 0.1407 0.1422 -0.0086 0.0066  0.0049  487 VAL A C   
3494  O O   . VAL A 495 ? 0.1515 0.1549 0.1564 -0.0116 0.0053  0.0074  487 VAL A O   
3495  C CB  . VAL A 495 ? 0.1692 0.1810 0.1742 -0.0072 0.0117  0.0050  487 VAL A CB  
3496  C CG1 . VAL A 495 ? 0.1972 0.2068 0.2016 -0.0068 0.0115  0.0044  487 VAL A CG1 
3497  C CG2 . VAL A 495 ? 0.2088 0.2236 0.2142 -0.0050 0.0145  0.0047  487 VAL A CG2 
3498  N N   . TRP A 496 ? 0.1495 0.1468 0.1530 -0.0055 0.0074  0.0036  488 TRP A N   
3499  C CA  . TRP A 496 ? 0.1888 0.1806 0.1935 -0.0044 0.0063  0.0051  488 TRP A CA  
3500  C C   . TRP A 496 ? 0.1938 0.1906 0.2055 -0.0019 0.0071  0.0075  488 TRP A C   
3501  O O   . TRP A 496 ? 0.1761 0.1764 0.1911 0.0006  0.0099  0.0068  488 TRP A O   
3502  C CB  . TRP A 496 ? 0.1611 0.1411 0.1602 -0.0017 0.0074  0.0027  488 TRP A CB  
3503  C CG  . TRP A 496 ? 0.1874 0.1597 0.1786 -0.0061 0.0038  0.0011  488 TRP A CG  
3504  C CD1 . TRP A 496 ? 0.1780 0.1493 0.1632 -0.0084 0.0021  -0.0011 488 TRP A CD1 
3505  C CD2 . TRP A 496 ? 0.2150 0.1790 0.2038 -0.0099 0.0002  0.0024  488 TRP A CD2 
3506  N NE1 . TRP A 496 ? 0.1875 0.1514 0.1676 -0.0142 -0.0033 -0.0011 488 TRP A NE1 
3507  C CE2 . TRP A 496 ? 0.2335 0.1923 0.2157 -0.0154 -0.0041 0.0009  488 TRP A CE2 
3508  C CE3 . TRP A 496 ? 0.2596 0.2198 0.2514 -0.0097 -0.0004 0.0056  488 TRP A CE3 
3509  C CZ2 . TRP A 496 ? 0.2283 0.1782 0.2073 -0.0216 -0.0090 0.0021  488 TRP A CZ2 
3510  C CZ3 . TRP A 496 ? 0.2646 0.2147 0.2521 -0.0148 -0.0042 0.0067  488 TRP A CZ3 
3511  C CH2 . TRP A 496 ? 0.2760 0.2210 0.2575 -0.0211 -0.0084 0.0048  488 TRP A CH2 
3512  N N   . ARG A 497 ? 0.1910 0.1883 0.2054 -0.0032 0.0039  0.0111  489 ARG A N   
3513  C CA  . ARG A 497 ? 0.1197 0.1226 0.1421 -0.0021 0.0019  0.0149  489 ARG A CA  
3514  C C   . ARG A 497 ? 0.1638 0.1625 0.1904 0.0004  -0.0002 0.0191  489 ARG A C   
3515  O O   . ARG A 497 ? 0.1549 0.1533 0.1797 -0.0027 -0.0049 0.0229  489 ARG A O   
3516  C CB  . ARG A 497 ? 0.1323 0.1393 0.1505 -0.0073 -0.0016 0.0159  489 ARG A CB  
3517  C CG  . ARG A 497 ? 0.1524 0.1655 0.1784 -0.0084 -0.0058 0.0199  489 ARG A CG  
3518  C CD  . ARG A 497 ? 0.1904 0.2023 0.2063 -0.0146 -0.0099 0.0196  489 ARG A CD  
3519  N NE  . ARG A 497 ? 0.1819 0.1989 0.2047 -0.0177 -0.0159 0.0233  489 ARG A NE  
3520  C CZ  . ARG A 497 ? 0.1735 0.1907 0.1949 -0.0218 -0.0245 0.0285  489 ARG A CZ  
3521  N NH1 . ARG A 497 ? 0.1354 0.1470 0.1473 -0.0225 -0.0267 0.0302  489 ARG A NH1 
3522  N NH2 . ARG A 497 ? 0.1554 0.1786 0.1851 -0.0259 -0.0316 0.0327  489 ARG A NH2 
3523  N N   . PRO A 498 ? 0.1359 0.1292 0.1663 0.0064  0.0040  0.0189  490 PRO A N   
3524  C CA  . PRO A 498 ? 0.1540 0.1393 0.1868 0.0100  0.0033  0.0225  490 PRO A CA  
3525  C C   . PRO A 498 ? 0.1411 0.1353 0.1878 0.0123  -0.0004 0.0303  490 PRO A C   
3526  O O   . PRO A 498 ? 0.1521 0.1580 0.2101 0.0132  -0.0005 0.0329  490 PRO A O   
3527  C CB  . PRO A 498 ? 0.2213 0.1959 0.2514 0.0169  0.0108  0.0190  490 PRO A CB  
3528  C CG  . PRO A 498 ? 0.1893 0.1719 0.2221 0.0181  0.0152  0.0166  490 PRO A CG  
3529  C CD  . PRO A 498 ? 0.1432 0.1337 0.1718 0.0104  0.0105  0.0147  490 PRO A CD  
3530  N N   . CYS A 499 ? 0.1333 0.1220 0.1801 0.0127  -0.0043 0.0352  491 CYS A N   
3531  C CA  . CYS A 499 ? 0.1765 0.1742 0.2361 0.0139  -0.0103 0.0442  491 CYS A CA  
3532  C C   . CYS A 499 ? 0.1964 0.1942 0.2724 0.0242  -0.0061 0.0500  491 CYS A C   
3533  O O   . CYS A 499 ? 0.2000 0.2094 0.2921 0.0259  -0.0113 0.0591  491 CYS A O   
3534  C CB  . CYS A 499 ? 0.2056 0.1981 0.2564 0.0088  -0.0177 0.0483  491 CYS A CB  
3535  S SG  . CYS A 499 ? 0.2225 0.1971 0.2693 0.0134  -0.0156 0.0508  491 CYS A SG  
3536  N N   . ASP A 500 ? 0.1779 0.1622 0.2496 0.0311  0.0030  0.0457  492 ASP A N   
3537  C CA  . ASP A 500 ? 0.1605 0.1423 0.2464 0.0429  0.0099  0.0513  492 ASP A CA  
3538  C C   . ASP A 500 ? 0.1712 0.1363 0.2453 0.0490  0.0218  0.0432  492 ASP A C   
3539  O O   . ASP A 500 ? 0.1827 0.1422 0.2408 0.0434  0.0228  0.0344  492 ASP A O   
3540  C CB  . ASP A 500 ? 0.1729 0.1472 0.2623 0.0462  0.0055  0.0589  492 ASP A CB  
3541  C CG  . ASP A 500 ? 0.2571 0.2086 0.3250 0.0427  0.0054  0.0532  492 ASP A CG  
3542  O OD1 . ASP A 500 ? 0.2308 0.1696 0.2826 0.0404  0.0103  0.0436  492 ASP A OD1 
3543  O OD2 . ASP A 500 ? 0.2377 0.1839 0.3051 0.0417  -0.0004 0.0593  492 ASP A OD2 
3544  N N   . THR A 501 ? 0.2153 0.1714 0.2966 0.0611  0.0309  0.0466  493 THR A N   
3545  C CA  . THR A 501 ? 0.2303 0.1670 0.2972 0.0682  0.0436  0.0391  493 THR A CA  
3546  C C   . THR A 501 ? 0.2237 0.1345 0.2621 0.0623  0.0416  0.0297  493 THR A C   
3547  O O   . THR A 501 ? 0.2601 0.1568 0.2798 0.0616  0.0470  0.0210  493 THR A O   
3548  C CB  . THR A 501 ? 0.2420 0.1714 0.3212 0.0836  0.0552  0.0454  493 THR A CB  
3549  O OG1 . THR A 501 ? 0.2711 0.1942 0.3556 0.0857  0.0496  0.0520  493 THR A OG1 
3550  C CG2 . THR A 501 ? 0.2098 0.1661 0.3181 0.0894  0.0597  0.0544  493 THR A CG2 
3551  N N   . ALA A 502 ? 0.2361 0.1397 0.2710 0.0574  0.0335  0.0320  494 ALA A N   
3552  C CA  . ALA A 502 ? 0.2848 0.1654 0.2955 0.0501  0.0305  0.0243  494 ALA A CA  
3553  C C   . ALA A 502 ? 0.2438 0.1345 0.2462 0.0377  0.0236  0.0187  494 ALA A C   
3554  O O   . ALA A 502 ? 0.2597 0.1370 0.2442 0.0337  0.0246  0.0108  494 ALA A O   
3555  C CB  . ALA A 502 ? 0.2859 0.1563 0.2964 0.0481  0.0244  0.0297  494 ALA A CB  
3556  N N   . GLU A 503 ? 0.1970 0.1103 0.2114 0.0317  0.0166  0.0231  495 GLU A N   
3557  C CA  . GLU A 503 ? 0.2138 0.1364 0.2218 0.0220  0.0121  0.0185  495 GLU A CA  
3558  C C   . GLU A 503 ? 0.1979 0.1240 0.2027 0.0244  0.0178  0.0131  495 GLU A C   
3559  O O   . GLU A 503 ? 0.2423 0.1664 0.2360 0.0182  0.0158  0.0076  495 GLU A O   
3560  C CB  . GLU A 503 ? 0.1651 0.1077 0.1834 0.0166  0.0055  0.0237  495 GLU A CB  
3561  C CG  . GLU A 503 ? 0.1803 0.1183 0.1958 0.0114  -0.0005 0.0283  495 GLU A CG  
3562  C CD  . GLU A 503 ? 0.2443 0.1977 0.2623 0.0049  -0.0062 0.0319  495 GLU A CD  
3563  O OE1 . GLU A 503 ? 0.1723 0.1391 0.1947 0.0043  -0.0061 0.0307  495 GLU A OE1 
3564  O OE2 . GLU A 503 ? 0.2515 0.2012 0.2651 0.0002  -0.0101 0.0360  495 GLU A OE2 
3565  N N   . SER A 504 ? 0.2325 0.1643 0.2481 0.0333  0.0248  0.0156  496 SER A N   
3566  C CA  . SER A 504 ? 0.2183 0.1531 0.2307 0.0357  0.0313  0.0116  496 SER A CA  
3567  C C   . SER A 504 ? 0.2515 0.1623 0.2409 0.0370  0.0361  0.0039  496 SER A C   
3568  O O   . SER A 504 ? 0.2567 0.1666 0.2346 0.0331  0.0359  -0.0012 496 SER A O   
3569  C CB  . SER A 504 ? 0.2137 0.1602 0.2450 0.0451  0.0390  0.0177  496 SER A CB  
3570  O OG  . SER A 504 ? 0.1951 0.1645 0.2456 0.0412  0.0322  0.0242  496 SER A OG  
3571  N N   . LEU A 505 ? 0.2210 0.1103 0.2016 0.0425  0.0402  0.0031  497 LEU A N   
3572  C CA  . LEU A 505 ? 0.2602 0.1212 0.2138 0.0428  0.0440  -0.0050 497 LEU A CA  
3573  C C   . LEU A 505 ? 0.3163 0.1713 0.2552 0.0296  0.0325  -0.0096 497 LEU A C   
3574  O O   . LEU A 505 ? 0.3136 0.1585 0.2339 0.0254  0.0313  -0.0156 497 LEU A O   
3575  C CB  . LEU A 505 ? 0.2846 0.1204 0.2306 0.0517  0.0510  -0.0048 497 LEU A CB  
3576  C CG  . LEU A 505 ? 0.3125 0.1123 0.2248 0.0509  0.0540  -0.0140 497 LEU A CG  
3577  C CD1 . LEU A 505 ? 0.3244 0.1205 0.2219 0.0537  0.0615  -0.0192 497 LEU A CD1 
3578  C CD2 . LEU A 505 ? 0.3464 0.1207 0.2513 0.0607  0.0623  -0.0137 497 LEU A CD2 
3579  N N   . VAL A 506 ? 0.2511 0.1133 0.1989 0.0227  0.0239  -0.0058 498 VAL A N   
3580  C CA  . VAL A 506 ? 0.2559 0.1162 0.1951 0.0101  0.0137  -0.0081 498 VAL A CA  
3581  C C   . VAL A 506 ? 0.2407 0.1211 0.1843 0.0053  0.0106  -0.0089 498 VAL A C   
3582  O O   . VAL A 506 ? 0.2685 0.1437 0.2002 -0.0020 0.0052  -0.0124 498 VAL A O   
3583  C CB  . VAL A 506 ? 0.2410 0.1069 0.1908 0.0047  0.0074  -0.0023 498 VAL A CB  
3584  C CG1 . VAL A 506 ? 0.2570 0.1268 0.2036 -0.0084 -0.0019 -0.0026 498 VAL A CG1 
3585  C CG2 . VAL A 506 ? 0.3026 0.1445 0.2454 0.0092  0.0100  -0.0015 498 VAL A CG2 
3586  N N   . ALA A 507 ? 0.2152 0.1180 0.1760 0.0089  0.0134  -0.0050 499 ALA A N   
3587  C CA  . ALA A 507 ? 0.2073 0.1268 0.1718 0.0055  0.0115  -0.0056 499 ALA A CA  
3588  C C   . ALA A 507 ? 0.2402 0.1499 0.1900 0.0079  0.0154  -0.0106 499 ALA A C   
3589  O O   . ALA A 507 ? 0.2059 0.1179 0.1489 0.0021  0.0105  -0.0124 499 ALA A O   
3590  C CB  . ALA A 507 ? 0.2341 0.1743 0.2166 0.0088  0.0139  -0.0011 499 ALA A CB  
3591  N N   . TRP A 508 ? 0.2687 0.1673 0.2132 0.0167  0.0245  -0.0120 500 TRP A N   
3592  C CA  . TRP A 508 ? 0.2674 0.1533 0.1937 0.0197  0.0298  -0.0166 500 TRP A CA  
3593  C C   . TRP A 508 ? 0.2942 0.1569 0.1951 0.0129  0.0233  -0.0223 500 TRP A C   
3594  O O   . TRP A 508 ? 0.2933 0.1533 0.1808 0.0086  0.0195  -0.0248 500 TRP A O   
3595  C CB  . TRP A 508 ? 0.2830 0.1600 0.2091 0.0316  0.0431  -0.0161 500 TRP A CB  
3596  C CG  . TRP A 508 ? 0.2878 0.1849 0.2308 0.0369  0.0503  -0.0118 500 TRP A CG  
3597  C CD1 . TRP A 508 ? 0.2484 0.1648 0.2172 0.0412  0.0533  -0.0050 500 TRP A CD1 
3598  C CD2 . TRP A 508 ? 0.2553 0.1542 0.1898 0.0375  0.0546  -0.0133 500 TRP A CD2 
3599  N NE1 . TRP A 508 ? 0.2207 0.1509 0.1988 0.0437  0.0591  -0.0023 500 TRP A NE1 
3600  C CE2 . TRP A 508 ? 0.2561 0.1756 0.2132 0.0419  0.0608  -0.0073 500 TRP A CE2 
3601  C CE3 . TRP A 508 ? 0.2602 0.1451 0.1700 0.0339  0.0528  -0.0184 500 TRP A CE3 
3602  C CZ2 . TRP A 508 ? 0.2628 0.1885 0.2188 0.0430  0.0664  -0.0064 500 TRP A CZ2 
3603  C CZ3 . TRP A 508 ? 0.2636 0.1547 0.1711 0.0359  0.0583  -0.0174 500 TRP A CZ3 
3604  C CH2 . TRP A 508 ? 0.2627 0.1737 0.1933 0.0405  0.0657  -0.0115 500 TRP A CH2 
3605  N N   . ALA A 509 ? 0.2958 0.1405 0.1891 0.0112  0.0208  -0.0236 501 ALA A N   
3606  C CA  . ALA A 509 ? 0.2915 0.1109 0.1593 0.0031  0.0133  -0.0289 501 ALA A CA  
3607  C C   . ALA A 509 ? 0.3036 0.1376 0.1770 -0.0097 -0.0004 -0.0269 501 ALA A C   
3608  O O   . ALA A 509 ? 0.3449 0.1675 0.1998 -0.0169 -0.0079 -0.0300 501 ALA A O   
3609  C CB  . ALA A 509 ? 0.3559 0.1528 0.2165 0.0033  0.0134  -0.0300 501 ALA A CB  
3610  N N   . GLU A 510 ? 0.2886 0.1474 0.1871 -0.0125 -0.0037 -0.0209 502 GLU A N   
3611  C CA  . GLU A 510 ? 0.2922 0.1680 0.2002 -0.0226 -0.0139 -0.0175 502 GLU A CA  
3612  C C   . GLU A 510 ? 0.2751 0.1646 0.1841 -0.0215 -0.0140 -0.0173 502 GLU A C   
3613  O O   . GLU A 510 ? 0.2678 0.1600 0.1730 -0.0292 -0.0230 -0.0163 502 GLU A O   
3614  C CB  . GLU A 510 ? 0.2785 0.1752 0.2103 -0.0240 -0.0144 -0.0113 502 GLU A CB  
3615  C CG  . GLU A 510 ? 0.2979 0.1817 0.2287 -0.0280 -0.0171 -0.0099 502 GLU A CG  
3616  C CD  . GLU A 510 ? 0.3360 0.2065 0.2559 -0.0400 -0.0276 -0.0106 502 GLU A CD  
3617  O OE1 . GLU A 510 ? 0.2908 0.1781 0.2207 -0.0477 -0.0346 -0.0068 502 GLU A OE1 
3618  O OE2 . GLU A 510 ? 0.3585 0.2014 0.2602 -0.0418 -0.0291 -0.0145 502 GLU A OE2 
3619  N N   . ALA A 511 ? 0.2416 0.1405 0.1573 -0.0124 -0.0046 -0.0171 503 ALA A N   
3620  C CA  . ALA A 511 ? 0.2060 0.1144 0.1205 -0.0110 -0.0038 -0.0167 503 ALA A CA  
3621  C C   . ALA A 511 ? 0.2532 0.1403 0.1406 -0.0128 -0.0063 -0.0212 503 ALA A C   
3622  O O   . ALA A 511 ? 0.3026 0.1946 0.1856 -0.0171 -0.0129 -0.0199 503 ALA A O   
3623  C CB  . ALA A 511 ? 0.1911 0.1101 0.1162 -0.0019 0.0069  -0.0155 503 ALA A CB  
3624  N N   . ALA A 512 ? 0.2603 0.1221 0.1278 -0.0091 -0.0011 -0.0263 504 ALA A N   
3625  C CA  . ALA A 512 ? 0.2939 0.1303 0.1293 -0.0105 -0.0025 -0.0315 504 ALA A CA  
3626  C C   . ALA A 512 ? 0.3382 0.1640 0.1608 -0.0236 -0.0184 -0.0323 504 ALA A C   
3627  O O   . ALA A 512 ? 0.3650 0.1814 0.1677 -0.0286 -0.0256 -0.0336 504 ALA A O   
3628  C CB  . ALA A 512 ? 0.3560 0.1654 0.1720 -0.0018 0.0097  -0.0368 504 ALA A CB  
3629  N N   . LYS A 513 ? 0.3277 0.1559 0.1623 -0.0299 -0.0248 -0.0304 505 LYS A N   
3630  C CA  . LYS A 513 ? 0.3691 0.1896 0.1964 -0.0440 -0.0406 -0.0296 505 LYS A CA  
3631  C C   . LYS A 513 ? 0.3471 0.1957 0.1940 -0.0511 -0.0511 -0.0224 505 LYS A C   
3632  O O   . LYS A 513 ? 0.3685 0.2118 0.2065 -0.0625 -0.0654 -0.0209 505 LYS A O   
3633  C CB  . LYS A 513 ? 0.3966 0.2144 0.2352 -0.0485 -0.0429 -0.0281 505 LYS A CB  
3634  C CG  . LYS A 513 ? 0.6230 0.4062 0.4383 -0.0454 -0.0374 -0.0346 505 LYS A CG  
3635  C CD  . LYS A 513 ? 0.6501 0.4308 0.4766 -0.0524 -0.0425 -0.0316 505 LYS A CD  
3636  C CE  . LYS A 513 ? 0.7184 0.5051 0.5490 -0.0693 -0.0597 -0.0274 505 LYS A CE  
3637  N NZ  . LYS A 513 ? 0.7717 0.5480 0.6051 -0.0771 -0.0648 -0.0251 505 LYS A NZ  
3638  N N   . ALA A 514 ? 0.3012 0.1790 0.1754 -0.0450 -0.0449 -0.0173 506 ALA A N   
3639  C CA  . ALA A 514 ? 0.2774 0.1817 0.1731 -0.0502 -0.0529 -0.0096 506 ALA A CA  
3640  C C   . ALA A 514 ? 0.3180 0.2184 0.1985 -0.0533 -0.0611 -0.0090 506 ALA A C   
3641  O O   . ALA A 514 ? 0.3410 0.2328 0.2058 -0.0461 -0.0542 -0.0126 506 ALA A O   
3642  C CB  . ALA A 514 ? 0.2742 0.2041 0.1951 -0.0416 -0.0427 -0.0057 506 ALA A CB  
3643  N N   . GLU A 515 ? 0.3207 0.2276 0.2062 -0.0646 -0.0761 -0.0035 507 GLU A N   
3644  C CA  . GLU A 515 ? 0.4234 0.3255 0.2931 -0.0693 -0.0872 -0.0018 507 GLU A CA  
3645  C C   . GLU A 515 ? 0.3940 0.3240 0.2855 -0.0640 -0.0861 0.0060  507 GLU A C   
3646  O O   . GLU A 515 ? 0.3795 0.3039 0.2552 -0.0619 -0.0885 0.0062  507 GLU A O   
3647  C CB  . GLU A 515 ? 0.5226 0.4187 0.3877 -0.0853 -0.1065 0.0017  507 GLU A CB  
3648  C CG  . GLU A 515 ? 0.6672 0.5278 0.5013 -0.0891 -0.1070 -0.0063 507 GLU A CG  
3649  C CD  . GLU A 515 ? 0.7541 0.6130 0.5913 -0.1015 -0.1208 -0.0007 507 GLU A CD  
3650  O OE1 . GLU A 515 ? 0.8159 0.6487 0.6333 -0.1052 -0.1212 -0.0057 507 GLU A OE1 
3651  O OE2 . GLU A 515 ? 0.7597 0.6431 0.6197 -0.1070 -0.1307 0.0093  507 GLU A OE2 
3652  N N   . ASP A 516 ? 0.2371 0.1948 0.1626 -0.0612 -0.0815 0.0127  508 ASP A N   
3653  C CA  . ASP A 516 ? 0.2205 0.2033 0.1676 -0.0578 -0.0830 0.0216  508 ASP A CA  
3654  C C   . ASP A 516 ? 0.2036 0.2033 0.1715 -0.0466 -0.0674 0.0227  508 ASP A C   
3655  O O   . ASP A 516 ? 0.1749 0.1971 0.1670 -0.0439 -0.0665 0.0308  508 ASP A O   
3656  C CB  . ASP A 516 ? 0.3074 0.3093 0.2770 -0.0680 -0.0970 0.0322  508 ASP A CB  
3657  C CG  . ASP A 516 ? 0.4067 0.4209 0.3995 -0.0713 -0.0935 0.0351  508 ASP A CG  
3658  O OD1 . ASP A 516 ? 0.3490 0.3540 0.3371 -0.0669 -0.0824 0.0284  508 ASP A OD1 
3659  O OD2 . ASP A 516 ? 0.4257 0.4597 0.4427 -0.0785 -0.1022 0.0454  508 ASP A OD2 
3660  N N   . HIS A 517 ? 0.1908 0.1793 0.1494 -0.0401 -0.0553 0.0150  509 HIS A N   
3661  C CA  . HIS A 517 ? 0.1900 0.1911 0.1638 -0.0309 -0.0424 0.0155  509 HIS A CA  
3662  C C   . HIS A 517 ? 0.2294 0.2155 0.1879 -0.0245 -0.0321 0.0077  509 HIS A C   
3663  O O   . HIS A 517 ? 0.2233 0.1912 0.1648 -0.0264 -0.0325 0.0021  509 HIS A O   
3664  C CB  . HIS A 517 ? 0.2012 0.2165 0.1966 -0.0320 -0.0389 0.0189  509 HIS A CB  
3665  C CG  . HIS A 517 ? 0.2251 0.2283 0.2139 -0.0363 -0.0390 0.0145  509 HIS A CG  
3666  N ND1 . HIS A 517 ? 0.2336 0.2340 0.2234 -0.0462 -0.0489 0.0169  509 HIS A ND1 
3667  C CD2 . HIS A 517 ? 0.2042 0.1980 0.1870 -0.0321 -0.0308 0.0091  509 HIS A CD2 
3668  C CE1 . HIS A 517 ? 0.2517 0.2393 0.2346 -0.0474 -0.0460 0.0125  509 HIS A CE1 
3669  N NE2 . HIS A 517 ? 0.2221 0.2064 0.2015 -0.0385 -0.0352 0.0081  509 HIS A NE2 
3670  N N   . PRO A 518 ? 0.1703 0.1632 0.1353 -0.0169 -0.0227 0.0078  510 PRO A N   
3671  C CA  . PRO A 518 ? 0.1514 0.1345 0.1079 -0.0114 -0.0130 0.0024  510 PRO A CA  
3672  C C   . PRO A 518 ? 0.1572 0.1440 0.1245 -0.0105 -0.0080 0.0011  510 PRO A C   
3673  O O   . PRO A 518 ? 0.1650 0.1612 0.1447 -0.0137 -0.0105 0.0040  510 PRO A O   
3674  C CB  . PRO A 518 ? 0.1407 0.1304 0.1011 -0.0058 -0.0073 0.0046  510 PRO A CB  
3675  C CG  . PRO A 518 ? 0.1630 0.1692 0.1417 -0.0063 -0.0097 0.0105  510 PRO A CG  
3676  C CD  . PRO A 518 ? 0.1424 0.1512 0.1225 -0.0132 -0.0208 0.0136  510 PRO A CD  
3677  N N   . SER A 519 ? 0.1524 0.1320 0.1150 -0.0061 -0.0007 -0.0025 511 SER A N   
3678  C CA  . SER A 519 ? 0.1749 0.1574 0.1467 -0.0050 0.0032  -0.0030 511 SER A CA  
3679  C C   . SER A 519 ? 0.1198 0.1051 0.0956 0.0002  0.0109  -0.0033 511 SER A C   
3680  O O   . SER A 519 ? 0.1541 0.1343 0.1225 0.0034  0.0148  -0.0042 511 SER A O   
3681  C CB  . SER A 519 ? 0.1926 0.1615 0.1561 -0.0061 0.0022  -0.0058 511 SER A CB  
3682  O OG  . SER A 519 ? 0.2251 0.1886 0.1832 -0.0127 -0.0061 -0.0056 511 SER A OG  
3683  N N   . CYS A 520 ? 0.1089 0.1022 0.0959 0.0003  0.0125  -0.0018 512 CYS A N   
3684  C CA  . CYS A 520 ? 0.1181 0.1143 0.1109 0.0031  0.0174  -0.0013 512 CYS A CA  
3685  C C   . CYS A 520 ? 0.1213 0.1154 0.1181 0.0037  0.0175  -0.0010 512 CYS A C   
3686  O O   . CYS A 520 ? 0.1834 0.1789 0.1827 0.0009  0.0139  -0.0000 512 CYS A O   
3687  C CB  . CYS A 520 ? 0.1673 0.1714 0.1667 0.0017  0.0177  0.0003  512 CYS A CB  
3688  S SG  . CYS A 520 ? 0.1930 0.1989 0.1899 0.0027  0.0190  0.0012  512 CYS A SG  
3689  N N   . LEU A 521 ? 0.1120 0.1027 0.1099 0.0079  0.0222  -0.0008 513 LEU A N   
3690  C CA  . LEU A 521 ? 0.1265 0.1159 0.1308 0.0103  0.0231  0.0010  513 LEU A CA  
3691  C C   . LEU A 521 ? 0.1615 0.1619 0.1802 0.0109  0.0244  0.0051  513 LEU A C   
3692  O O   . LEU A 521 ? 0.1733 0.1770 0.1959 0.0130  0.0293  0.0063  513 LEU A O   
3693  C CB  . LEU A 521 ? 0.1690 0.1456 0.1652 0.0157  0.0286  -0.0008 513 LEU A CB  
3694  C CG  . LEU A 521 ? 0.2066 0.1685 0.1845 0.0137  0.0260  -0.0054 513 LEU A CG  
3695  C CD1 . LEU A 521 ? 0.1985 0.1424 0.1637 0.0196  0.0326  -0.0080 513 LEU A CD1 
3696  C CD2 . LEU A 521 ? 0.1812 0.1428 0.1595 0.0079  0.0182  -0.0052 513 LEU A CD2 
3697  N N   . ILE A 522 ? 0.1730 0.1786 0.1988 0.0082  0.0194  0.0079  514 ILE A N   
3698  C CA  . ILE A 522 ? 0.1580 0.1735 0.1950 0.0057  0.0169  0.0118  514 ILE A CA  
3699  C C   . ILE A 522 ? 0.1159 0.1358 0.1657 0.0083  0.0155  0.0173  514 ILE A C   
3700  O O   . ILE A 522 ? 0.1450 0.1613 0.1928 0.0081  0.0118  0.0183  514 ILE A O   
3701  C CB  . ILE A 522 ? 0.1339 0.1502 0.1648 -0.0006 0.0114  0.0108  514 ILE A CB  
3702  C CG1 . ILE A 522 ? 0.1630 0.1766 0.1852 -0.0014 0.0141  0.0069  514 ILE A CG1 
3703  C CG2 . ILE A 522 ? 0.1290 0.1514 0.1670 -0.0047 0.0068  0.0144  514 ILE A CG2 
3704  C CD1 . ILE A 522 ? 0.1351 0.1472 0.1499 -0.0052 0.0117  0.0056  514 ILE A CD1 
3705  N N   . PHE A 523 ? 0.1025 0.1308 0.1670 0.0108  0.0186  0.0220  515 PHE A N   
3706  C CA  . PHE A 523 ? 0.1128 0.1471 0.1938 0.0158  0.0194  0.0288  515 PHE A CA  
3707  C C   . PHE A 523 ? 0.1286 0.1778 0.2278 0.0112  0.0131  0.0364  515 PHE A C   
3708  O O   . PHE A 523 ? 0.1177 0.1716 0.2182 0.0058  0.0119  0.0362  515 PHE A O   
3709  C CB  . PHE A 523 ? 0.1191 0.1500 0.2037 0.0250  0.0314  0.0292  515 PHE A CB  
3710  C CG  . PHE A 523 ? 0.1557 0.1686 0.2198 0.0287  0.0361  0.0219  515 PHE A CG  
3711  C CD1 . PHE A 523 ? 0.1405 0.1434 0.1995 0.0311  0.0342  0.0213  515 PHE A CD1 
3712  C CD2 . PHE A 523 ? 0.1753 0.1804 0.2246 0.0288  0.0412  0.0163  515 PHE A CD2 
3713  C CE1 . PHE A 523 ? 0.1954 0.1801 0.2347 0.0326  0.0369  0.0148  515 PHE A CE1 
3714  C CE2 . PHE A 523 ? 0.2137 0.2015 0.2428 0.0303  0.0431  0.0101  515 PHE A CE2 
3715  C CZ  . PHE A 523 ? 0.2181 0.1954 0.2421 0.0317  0.0406  0.0090  515 PHE A CZ  
3716  N N   . SER A 524 ? 0.1321 0.1880 0.2454 0.0130  0.0084  0.0437  516 SER A N   
3717  C CA  . SER A 524 ? 0.1188 0.1893 0.2497 0.0071  -0.0011 0.0523  516 SER A CA  
3718  C C   . SER A 524 ? 0.2137 0.2997 0.3721 0.0119  0.0048  0.0611  516 SER A C   
3719  O O   . SER A 524 ? 0.1923 0.2774 0.3581 0.0227  0.0165  0.0626  516 SER A O   
3720  C CB  . SER A 524 ? 0.1473 0.2185 0.2807 0.0063  -0.0108 0.0577  516 SER A CB  
3721  O OG  . SER A 524 ? 0.1910 0.2670 0.3427 0.0166  -0.0053 0.0648  516 SER A OG  
3722  N N   . ARG A 525 ? 0.2142 0.3138 0.3874 0.0037  -0.0032 0.0675  517 ARG A N   
3723  C CA  . ARG A 525 ? 0.1834 0.3024 0.3890 0.0069  0.0006  0.0790  517 ARG A CA  
3724  C C   . ARG A 525 ? 0.2599 0.3894 0.4859 0.0114  -0.0048 0.0898  517 ARG A C   
3725  O O   . ARG A 525 ? 0.2610 0.3943 0.5007 0.0202  0.0049  0.0954  517 ARG A O   
3726  C CB  . ARG A 525 ? 0.1875 0.3168 0.4025 -0.0054 -0.0076 0.0829  517 ARG A CB  
3727  C CG  . ARG A 525 ? 0.1762 0.3182 0.4144 -0.0037 -0.0050 0.0933  517 ARG A CG  
3728  C CD  . ARG A 525 ? 0.3261 0.4734 0.5684 -0.0175 -0.0170 0.0970  517 ARG A CD  
3729  N NE  . ARG A 525 ? 0.4487 0.6056 0.7092 -0.0157 -0.0096 0.1041  517 ARG A NE  
3730  C CZ  . ARG A 525 ? 0.5495 0.7189 0.8307 -0.0190 -0.0164 0.1155  517 ARG A CZ  
3731  N NH1 . ARG A 525 ? 0.5156 0.6885 0.8002 -0.0245 -0.0313 0.1208  517 ARG A NH1 
3732  N NH2 . ARG A 525 ? 0.5366 0.7151 0.8350 -0.0170 -0.0083 0.1221  517 ARG A NH2 
3733  N N   . GLN A 526 ? 0.2547 0.3828 0.4745 0.0051  -0.0197 0.0915  518 GLN A N   
3734  C CA  . GLN A 526 ? 0.2796 0.4137 0.5122 0.0067  -0.0272 0.1014  518 GLN A CA  
3735  C C   . GLN A 526 ? 0.2851 0.4097 0.5132 0.0184  -0.0213 0.1005  518 GLN A C   
3736  O O   . GLN A 526 ? 0.2210 0.3293 0.4265 0.0209  -0.0160 0.0903  518 GLN A O   
3737  C CB  . GLN A 526 ? 0.2092 0.3437 0.4332 -0.0073 -0.0471 0.1041  518 GLN A CB  
3738  C CG  . GLN A 526 ? 0.1657 0.2860 0.3633 -0.0110 -0.0548 0.0972  518 GLN A CG  
3739  C CD  . GLN A 526 ? 0.2250 0.3285 0.3924 -0.0167 -0.0503 0.0829  518 GLN A CD  
3740  O OE1 . GLN A 526 ? 0.2219 0.3269 0.3922 -0.0159 -0.0412 0.0787  518 GLN A OE1 
3741  N NE2 . GLN A 526 ? 0.2206 0.3081 0.3592 -0.0220 -0.0561 0.0763  518 GLN A NE2 
3742  N N   . ASN A 527 ? 0.2711 0.4005 0.5139 0.0239  -0.0214 0.1095  519 ASN A N   
3743  C CA  . ASN A 527 ? 0.2815 0.3996 0.5203 0.0353  -0.0147 0.1092  519 ASN A CA  
3744  C C   . ASN A 527 ? 0.2850 0.3918 0.5044 0.0310  -0.0260 0.1062  519 ASN A C   
3745  O O   . ASN A 527 ? 0.2424 0.3531 0.4566 0.0198  -0.0418 0.1092  519 ASN A O   
3746  C CB  . ASN A 527 ? 0.3120 0.4387 0.5716 0.0409  -0.0139 0.1205  519 ASN A CB  
3747  C CG  . ASN A 527 ? 0.2893 0.4236 0.5664 0.0485  0.0011  0.1241  519 ASN A CG  
3748  O OD1 . ASN A 527 ? 0.3050 0.4349 0.5754 0.0509  0.0125  0.1172  519 ASN A OD1 
3749  N ND2 . ASN A 527 ? 0.3622 0.5076 0.6613 0.0524  0.0013  0.1357  519 ASN A ND2 
3750  N N   . LEU A 528 ? 0.2960 0.3848 0.5000 0.0389  -0.0176 0.0996  520 LEU A N   
3751  C CA  . LEU A 528 ? 0.2958 0.3677 0.4733 0.0334  -0.0247 0.0941  520 LEU A CA  
3752  C C   . LEU A 528 ? 0.3451 0.4068 0.5259 0.0437  -0.0216 0.0994  520 LEU A C   
3753  O O   . LEU A 528 ? 0.2440 0.2979 0.4301 0.0556  -0.0079 0.0981  520 LEU A O   
3754  C CB  . LEU A 528 ? 0.2480 0.3033 0.3967 0.0292  -0.0183 0.0791  520 LEU A CB  
3755  C CG  . LEU A 528 ? 0.2363 0.2967 0.3773 0.0203  -0.0192 0.0723  520 LEU A CG  
3756  C CD1 . LEU A 528 ? 0.1851 0.2294 0.2977 0.0155  -0.0169 0.0605  520 LEU A CD1 
3757  C CD2 . LEU A 528 ? 0.2723 0.3457 0.4197 0.0099  -0.0335 0.0787  520 LEU A CD2 
3758  N N   . LYS A 529 ? 0.3702 0.4293 0.5454 0.0392  -0.0338 0.1052  521 LYS A N   
3759  C CA  . LYS A 529 ? 0.3495 0.3986 0.5279 0.0480  -0.0319 0.1112  521 LYS A CA  
3760  C C   . LYS A 529 ? 0.2494 0.2728 0.4045 0.0515  -0.0223 0.1010  521 LYS A C   
3761  O O   . LYS A 529 ? 0.2606 0.2740 0.3912 0.0420  -0.0245 0.0915  521 LYS A O   
3762  C CB  . LYS A 529 ? 0.4085 0.4603 0.5824 0.0403  -0.0475 0.1190  521 LYS A CB  
3763  N N   . PHE A 530 ? 0.2753 0.2872 0.4367 0.0643  -0.0111 0.1023  522 PHE A N   
3764  C CA  . PHE A 530 ? 0.3295 0.3137 0.4675 0.0665  -0.0034 0.0931  522 PHE A CA  
3765  C C   . PHE A 530 ? 0.3461 0.3187 0.4702 0.0604  -0.0131 0.0963  522 PHE A C   
3766  O O   . PHE A 530 ? 0.3436 0.3227 0.4792 0.0623  -0.0211 0.1078  522 PHE A O   
3767  C CB  . PHE A 530 ? 0.3341 0.3056 0.4771 0.0805  0.0109  0.0924  522 PHE A CB  
3768  C CG  . PHE A 530 ? 0.3432 0.2825 0.4614 0.0828  0.0183  0.0833  522 PHE A CG  
3769  C CD1 . PHE A 530 ? 0.3285 0.2557 0.4287 0.0805  0.0261  0.0709  522 PHE A CD1 
3770  C CD2 . PHE A 530 ? 0.4015 0.3225 0.5111 0.0846  0.0161  0.0859  522 PHE A CD2 
3771  C CE1 . PHE A 530 ? 0.4009 0.2981 0.4756 0.0795  0.0306  0.0617  522 PHE A CE1 
3772  C CE2 . PHE A 530 ? 0.4586 0.3484 0.5442 0.0844  0.0217  0.0773  522 PHE A CE2 
3773  C CZ  . PHE A 530 ? 0.4719 0.3491 0.5403 0.0818  0.0287  0.0655  522 PHE A CZ  
3774  N N   . GLN A 531 ? 0.2698 0.2259 0.3686 0.0524  -0.0124 0.0862  523 GLN A N   
3775  C CA  . GLN A 531 ? 0.2704 0.2146 0.3542 0.0455  -0.0197 0.0887  523 GLN A CA  
3776  C C   . GLN A 531 ? 0.2970 0.2139 0.3702 0.0509  -0.0125 0.0860  523 GLN A C   
3777  O O   . GLN A 531 ? 0.3057 0.2088 0.3676 0.0515  -0.0041 0.0756  523 GLN A O   
3778  C CB  . GLN A 531 ? 0.3119 0.2582 0.3769 0.0318  -0.0238 0.0809  523 GLN A CB  
3779  C CG  . GLN A 531 ? 0.2862 0.2538 0.3559 0.0257  -0.0299 0.0811  523 GLN A CG  
3780  C CD  . GLN A 531 ? 0.3578 0.3361 0.4353 0.0240  -0.0416 0.0931  523 GLN A CD  
3781  O OE1 . GLN A 531 ? 0.3974 0.3671 0.4649 0.0207  -0.0473 0.0987  523 GLN A OE1 
3782  N NE2 . GLN A 531 ? 0.4008 0.3977 0.4965 0.0256  -0.0459 0.0982  523 GLN A NE2 
3783  N N   . ALA A 532 ? 0.2944 0.2014 0.3689 0.0538  -0.0167 0.0955  524 ALA A N   
3784  C CA  . ALA A 532 ? 0.3489 0.2263 0.4110 0.0575  -0.0107 0.0932  524 ALA A CA  
3785  C C   . ALA A 532 ? 0.3702 0.2350 0.4092 0.0438  -0.0128 0.0849  524 ALA A C   
3786  O O   . ALA A 532 ? 0.3582 0.2357 0.3919 0.0331  -0.0200 0.0857  524 ALA A O   
3787  C CB  . ALA A 532 ? 0.3877 0.2595 0.4550 0.0631  -0.0149 0.1041  524 ALA A CB  
3788  N N   . ARG A 533 ? 0.3084 0.1474 0.3333 0.0442  -0.0063 0.0772  525 ARG A N   
3789  C CA  . ARG A 533 ? 0.2978 0.1267 0.3044 0.0307  -0.0085 0.0698  525 ARG A CA  
3790  C C   . ARG A 533 ? 0.4260 0.2212 0.4186 0.0306  -0.0059 0.0684  525 ARG A C   
3791  O O   . ARG A 533 ? 0.3473 0.1229 0.3386 0.0418  0.0013  0.0670  525 ARG A O   
3792  C CB  . ARG A 533 ? 0.2837 0.1195 0.2846 0.0263  -0.0051 0.0580  525 ARG A CB  
3793  C CG  . ARG A 533 ? 0.2737 0.1390 0.2824 0.0213  -0.0088 0.0577  525 ARG A CG  
3794  C CD  . ARG A 533 ? 0.2835 0.1531 0.2865 0.0179  -0.0052 0.0469  525 ARG A CD  
3795  N NE  . ARG A 533 ? 0.2872 0.1828 0.2991 0.0160  -0.0073 0.0471  525 ARG A NE  
3796  C CZ  . ARG A 533 ? 0.2547 0.1635 0.2799 0.0239  -0.0049 0.0490  525 ARG A CZ  
3797  N NH1 . ARG A 533 ? 0.2457 0.1459 0.2781 0.0354  0.0011  0.0511  525 ARG A NH1 
3798  N NH2 . ARG A 533 ? 0.2371 0.1667 0.2684 0.0204  -0.0079 0.0492  525 ARG A NH2 
3799  N N   . SER A 534 ? 0.3331 0.1205 0.3145 0.0178  -0.0110 0.0688  526 SER A N   
3800  C CA  . SER A 534 ? 0.3797 0.1341 0.3453 0.0135  -0.0097 0.0653  526 SER A CA  
3801  C C   . SER A 534 ? 0.3641 0.1093 0.3174 0.0087  -0.0070 0.0523  526 SER A C   
3802  O O   . SER A 534 ? 0.3413 0.1076 0.2987 0.0071  -0.0067 0.0469  526 SER A O   
3803  C CB  . SER A 534 ? 0.4120 0.1631 0.3721 0.0000  -0.0161 0.0714  526 SER A CB  
3804  O OG  . SER A 534 ? 0.3597 0.1293 0.3189 -0.0126 -0.0190 0.0670  526 SER A OG  
3805  N N   . GLU A 535 ? 0.4553 0.1705 0.3935 0.0058  -0.0057 0.0470  527 GLU A N   
3806  C CA  . GLU A 535 ? 0.4346 0.1408 0.3586 -0.0012 -0.0056 0.0350  527 GLU A CA  
3807  C C   . GLU A 535 ? 0.4033 0.1260 0.3275 -0.0169 -0.0134 0.0346  527 GLU A C   
3808  O O   . GLU A 535 ? 0.3690 0.1010 0.2901 -0.0198 -0.0137 0.0272  527 GLU A O   
3809  C CB  . GLU A 535 ? 0.4942 0.1731 0.4044 -0.0042 -0.0050 0.0297  527 GLU A CB  
3810  C CG  . GLU A 535 ? 0.5360 0.2033 0.4282 -0.0111 -0.0063 0.0176  527 GLU A CG  
3811  C CD  . GLU A 535 ? 0.5710 0.2077 0.4459 -0.0099 -0.0039 0.0116  527 GLU A CD  
3812  O OE1 . GLU A 535 ? 0.6383 0.2620 0.4952 -0.0108 -0.0027 0.0016  527 GLU A OE1 
3813  O OE2 . GLU A 535 ? 0.5653 0.1897 0.4431 -0.0081 -0.0033 0.0170  527 GLU A OE2 
3814  N N   . GLN A 536 ? 0.3743 0.1069 0.3056 -0.0264 -0.0185 0.0428  528 GLN A N   
3815  C CA  . GLN A 536 ? 0.3971 0.1517 0.3339 -0.0400 -0.0238 0.0436  528 GLN A CA  
3816  C C   . GLN A 536 ? 0.3982 0.1867 0.3477 -0.0349 -0.0215 0.0430  528 GLN A C   
3817  O O   . GLN A 536 ? 0.3055 0.1096 0.2573 -0.0411 -0.0231 0.0386  528 GLN A O   
3818  C CB  . GLN A 536 ? 0.4169 0.1770 0.3593 -0.0491 -0.0266 0.0532  528 GLN A CB  
3819  C CG  . GLN A 536 ? 0.4541 0.2366 0.4042 -0.0624 -0.0299 0.0552  528 GLN A CG  
3820  C CD  . GLN A 536 ? 0.5228 0.3004 0.4683 -0.0717 -0.0340 0.0475  528 GLN A CD  
3821  O OE1 . GLN A 536 ? 0.5228 0.2792 0.4589 -0.0745 -0.0358 0.0438  528 GLN A OE1 
3822  N NE2 . GLN A 536 ? 0.4937 0.2910 0.4455 -0.0764 -0.0359 0.0453  528 GLN A NE2 
3823  N N   . GLN A 537 ? 0.3100 0.1100 0.2683 -0.0242 -0.0186 0.0479  529 GLN A N   
3824  C CA  . GLN A 537 ? 0.2815 0.1106 0.2500 -0.0206 -0.0173 0.0472  529 GLN A CA  
3825  C C   . GLN A 537 ? 0.2842 0.1145 0.2509 -0.0150 -0.0137 0.0377  529 GLN A C   
3826  O O   . GLN A 537 ? 0.2564 0.1053 0.2265 -0.0183 -0.0140 0.0339  529 GLN A O   
3827  C CB  . GLN A 537 ? 0.2824 0.1216 0.2599 -0.0119 -0.0172 0.0552  529 GLN A CB  
3828  C CG  . GLN A 537 ? 0.2783 0.1215 0.2555 -0.0182 -0.0210 0.0649  529 GLN A CG  
3829  C CD  . GLN A 537 ? 0.3582 0.2049 0.3413 -0.0098 -0.0230 0.0739  529 GLN A CD  
3830  O OE1 . GLN A 537 ? 0.3398 0.1760 0.3275 0.0006  -0.0215 0.0755  529 GLN A OE1 
3831  N NE2 . GLN A 537 ? 0.3956 0.2566 0.3783 -0.0140 -0.0265 0.0805  529 GLN A NE2 
3832  N N   . LEU A 538 ? 0.3216 0.1308 0.2819 -0.0060 -0.0094 0.0342  530 LEU A N   
3833  C CA  . LEU A 538 ? 0.3152 0.1212 0.2697 -0.0009 -0.0047 0.0253  530 LEU A CA  
3834  C C   . LEU A 538 ? 0.2945 0.0993 0.2388 -0.0127 -0.0090 0.0184  530 LEU A C   
3835  O O   . LEU A 538 ? 0.3249 0.1441 0.2706 -0.0124 -0.0080 0.0138  530 LEU A O   
3836  C CB  . LEU A 538 ? 0.3359 0.1119 0.2796 0.0094  0.0020  0.0223  530 LEU A CB  
3837  C CG  . LEU A 538 ? 0.4178 0.2007 0.3757 0.0252  0.0092  0.0278  530 LEU A CG  
3838  C CD1 . LEU A 538 ? 0.4955 0.2445 0.4421 0.0357  0.0170  0.0263  530 LEU A CD1 
3839  C CD2 . LEU A 538 ? 0.3657 0.1705 0.3323 0.0305  0.0138  0.0244  530 LEU A CD2 
3840  N N   . ASN A 539 ? 0.3129 0.1004 0.2476 -0.0235 -0.0146 0.0187  531 ASN A N   
3841  C CA  . ASN A 539 ? 0.3158 0.1024 0.2428 -0.0359 -0.0207 0.0138  531 ASN A CA  
3842  C C   . ASN A 539 ? 0.2869 0.1060 0.2296 -0.0434 -0.0241 0.0181  531 ASN A C   
3843  O O   . ASN A 539 ? 0.3065 0.1325 0.2478 -0.0509 -0.0284 0.0149  531 ASN A O   
3844  C CB  . ASN A 539 ? 0.3672 0.1259 0.2812 -0.0468 -0.0267 0.0139  531 ASN A CB  
3845  C CG  . ASN A 539 ? 0.5125 0.2363 0.4050 -0.0408 -0.0233 0.0063  531 ASN A CG  
3846  O OD1 . ASN A 539 ? 0.6180 0.3359 0.5007 -0.0328 -0.0183 -0.0007 531 ASN A OD1 
3847  N ND2 . ASN A 539 ? 0.5619 0.2681 0.4490 -0.0434 -0.0244 0.0075  531 ASN A ND2 
3848  N N   . ASP A 540 ? 0.2918 0.1295 0.2479 -0.0412 -0.0223 0.0255  532 ASP A N   
3849  C CA  . ASP A 540 ? 0.2753 0.1410 0.2436 -0.0465 -0.0231 0.0290  532 ASP A CA  
3850  C C   . ASP A 540 ? 0.2667 0.1522 0.2410 -0.0385 -0.0191 0.0260  532 ASP A C   
3851  O O   . ASP A 540 ? 0.2668 0.1729 0.2491 -0.0416 -0.0187 0.0279  532 ASP A O   
3852  C CB  . ASP A 540 ? 0.2773 0.1502 0.2523 -0.0496 -0.0228 0.0384  532 ASP A CB  
3853  C CG  . ASP A 540 ? 0.3247 0.1852 0.2977 -0.0613 -0.0270 0.0429  532 ASP A CG  
3854  O OD1 . ASP A 540 ? 0.3221 0.1782 0.2933 -0.0699 -0.0315 0.0398  532 ASP A OD1 
3855  O OD2 . ASP A 540 ? 0.3622 0.2173 0.3355 -0.0626 -0.0264 0.0504  532 ASP A OD2 
3856  N N   . ILE A 541 ? 0.2795 0.1586 0.2506 -0.0281 -0.0153 0.0220  533 ILE A N   
3857  C CA  . ILE A 541 ? 0.2140 0.1113 0.1914 -0.0220 -0.0119 0.0196  533 ILE A CA  
3858  C C   . ILE A 541 ? 0.2341 0.1404 0.2103 -0.0273 -0.0135 0.0152  533 ILE A C   
3859  O O   . ILE A 541 ? 0.2097 0.1354 0.1935 -0.0272 -0.0123 0.0160  533 ILE A O   
3860  C CB  . ILE A 541 ? 0.2227 0.1116 0.1986 -0.0106 -0.0067 0.0168  533 ILE A CB  
3861  C CG1 . ILE A 541 ? 0.2798 0.1652 0.2620 -0.0044 -0.0058 0.0235  533 ILE A CG1 
3862  C CG2 . ILE A 541 ? 0.2044 0.1113 0.1868 -0.0059 -0.0035 0.0144  533 ILE A CG2 
3863  C CD1 . ILE A 541 ? 0.2267 0.1018 0.2102 0.0079  0.0004  0.0226  533 ILE A CD1 
3864  N N   . LYS A 542 ? 0.2134 0.1043 0.1792 -0.0326 -0.0171 0.0112  534 LYS A N   
3865  C CA  . LYS A 542 ? 0.2588 0.1570 0.2230 -0.0376 -0.0203 0.0079  534 LYS A CA  
3866  C C   . LYS A 542 ? 0.2499 0.1679 0.2268 -0.0460 -0.0237 0.0136  534 LYS A C   
3867  O O   . LYS A 542 ? 0.2203 0.1489 0.2003 -0.0493 -0.0264 0.0129  534 LYS A O   
3868  C CB  . LYS A 542 ? 0.2629 0.1367 0.2095 -0.0425 -0.0252 0.0026  534 LYS A CB  
3869  C CG  . LYS A 542 ? 0.2725 0.1312 0.2153 -0.0528 -0.0316 0.0054  534 LYS A CG  
3870  C CD  . LYS A 542 ? 0.4318 0.2652 0.3544 -0.0602 -0.0387 -0.0004 534 LYS A CD  
3871  C CE  . LYS A 542 ? 0.5163 0.3174 0.4171 -0.0520 -0.0334 -0.0073 534 LYS A CE  
3872  N NZ  . LYS A 542 ? 0.5010 0.2824 0.3990 -0.0519 -0.0323 -0.0047 534 LYS A NZ  
3873  N N   . ARG A 543 ? 0.2610 0.1836 0.2454 -0.0492 -0.0231 0.0200  535 ARG A N   
3874  C CA  . ARG A 543 ? 0.2384 0.1808 0.2359 -0.0552 -0.0231 0.0265  535 ARG A CA  
3875  C C   . ARG A 543 ? 0.1809 0.1412 0.1847 -0.0484 -0.0164 0.0278  535 ARG A C   
3876  O O   . ARG A 543 ? 0.2233 0.1985 0.2360 -0.0513 -0.0136 0.0331  535 ARG A O   
3877  C CB  . ARG A 543 ? 0.2003 0.1371 0.2005 -0.0627 -0.0247 0.0334  535 ARG A CB  
3878  C CG  . ARG A 543 ? 0.2369 0.1514 0.2284 -0.0707 -0.0320 0.0318  535 ARG A CG  
3879  C CD  . ARG A 543 ? 0.2578 0.1700 0.2553 -0.0810 -0.0344 0.0401  535 ARG A CD  
3880  N NE  . ARG A 543 ? 0.2849 0.2194 0.2990 -0.0892 -0.0358 0.0465  535 ARG A NE  
3881  C CZ  . ARG A 543 ? 0.2889 0.2261 0.3128 -0.1009 -0.0391 0.0547  535 ARG A CZ  
3882  N NH1 . ARG A 543 ? 0.3083 0.2261 0.3243 -0.1047 -0.0413 0.0559  535 ARG A NH1 
3883  N NH2 . ARG A 543 ? 0.2832 0.2450 0.3253 -0.1050 -0.0385 0.0607  535 ARG A NH2 
3884  N N   . GLY A 544 ? 0.1799 0.1382 0.1791 -0.0398 -0.0135 0.0235  536 GLY A N   
3885  C CA  . GLY A 544 ? 0.1608 0.1333 0.1635 -0.0347 -0.0088 0.0234  536 GLY A CA  
3886  C C   . GLY A 544 ? 0.1966 0.1707 0.1981 -0.0328 -0.0065 0.0275  536 GLY A C   
3887  O O   . GLY A 544 ? 0.1911 0.1696 0.1913 -0.0280 -0.0046 0.0261  536 GLY A O   
3888  N N   . ALA A 545 ? 0.2180 0.1878 0.2188 -0.0375 -0.0072 0.0331  537 ALA A N   
3889  C CA  . ALA A 545 ? 0.2009 0.1684 0.1970 -0.0363 -0.0064 0.0378  537 ALA A CA  
3890  C C   . ALA A 545 ? 0.2401 0.1956 0.2344 -0.0408 -0.0089 0.0430  537 ALA A C   
3891  O O   . ALA A 545 ? 0.2397 0.1926 0.2375 -0.0472 -0.0101 0.0443  537 ALA A O   
3892  C CB  . ALA A 545 ? 0.1539 0.1321 0.1478 -0.0375 -0.0013 0.0408  537 ALA A CB  
3893  N N   . TYR A 546 ? 0.1932 0.1411 0.1827 -0.0379 -0.0106 0.0467  538 TYR A N   
3894  C CA  . TYR A 546 ? 0.2266 0.1604 0.2134 -0.0410 -0.0130 0.0522  538 TYR A CA  
3895  C C   . TYR A 546 ? 0.2452 0.1767 0.2264 -0.0379 -0.0145 0.0584  538 TYR A C   
3896  O O   . TYR A 546 ? 0.2351 0.1742 0.2151 -0.0334 -0.0152 0.0573  538 TYR A O   
3897  C CB  . TYR A 546 ? 0.2147 0.1322 0.2014 -0.0385 -0.0158 0.0483  538 TYR A CB  
3898  C CG  . TYR A 546 ? 0.2224 0.1384 0.2104 -0.0283 -0.0157 0.0451  538 TYR A CG  
3899  C CD1 . TYR A 546 ? 0.1905 0.1160 0.1816 -0.0243 -0.0138 0.0386  538 TYR A CD1 
3900  C CD2 . TYR A 546 ? 0.2457 0.1518 0.2337 -0.0225 -0.0173 0.0499  538 TYR A CD2 
3901  C CE1 . TYR A 546 ? 0.1851 0.1113 0.1801 -0.0155 -0.0128 0.0370  538 TYR A CE1 
3902  C CE2 . TYR A 546 ? 0.2483 0.1563 0.2420 -0.0130 -0.0167 0.0489  538 TYR A CE2 
3903  C CZ  . TYR A 546 ? 0.2430 0.1616 0.2406 -0.0098 -0.0141 0.0424  538 TYR A CZ  
3904  O OH  . TYR A 546 ? 0.2484 0.1707 0.2541 -0.0008 -0.0125 0.0426  538 TYR A OH  
3905  N N   . VAL A 547 ? 0.2573 0.1776 0.2346 -0.0412 -0.0159 0.0655  539 VAL A N   
3906  C CA  . VAL A 547 ? 0.2816 0.1978 0.2525 -0.0386 -0.0189 0.0728  539 VAL A CA  
3907  C C   . VAL A 547 ? 0.2912 0.1988 0.2672 -0.0302 -0.0230 0.0727  539 VAL A C   
3908  O O   . VAL A 547 ? 0.3038 0.1958 0.2811 -0.0291 -0.0235 0.0735  539 VAL A O   
3909  C CB  . VAL A 547 ? 0.2523 0.1592 0.2164 -0.0450 -0.0182 0.0817  539 VAL A CB  
3910  C CG1 . VAL A 547 ? 0.2778 0.1792 0.2333 -0.0422 -0.0226 0.0901  539 VAL A CG1 
3911  C CG2 . VAL A 547 ? 0.2553 0.1728 0.2171 -0.0522 -0.0117 0.0830  539 VAL A CG2 
3912  N N   . ILE A 548 ? 0.2418 0.1588 0.2210 -0.0244 -0.0255 0.0721  540 ILE A N   
3913  C CA  . ILE A 548 ? 0.2549 0.1676 0.2431 -0.0153 -0.0283 0.0739  540 ILE A CA  
3914  C C   . ILE A 548 ? 0.3055 0.2128 0.2922 -0.0132 -0.0343 0.0851  540 ILE A C   
3915  O O   . ILE A 548 ? 0.3359 0.2354 0.3310 -0.0053 -0.0356 0.0892  540 ILE A O   
3916  C CB  . ILE A 548 ? 0.2554 0.1829 0.2522 -0.0105 -0.0284 0.0691  540 ILE A CB  
3917  C CG1 . ILE A 548 ? 0.2814 0.2057 0.2914 -0.0000 -0.0280 0.0706  540 ILE A CG1 
3918  C CG2 . ILE A 548 ? 0.2087 0.1483 0.2008 -0.0136 -0.0336 0.0728  540 ILE A CG2 
3919  C CD1 . ILE A 548 ? 0.3319 0.2695 0.3520 0.0044  -0.0258 0.0654  540 ILE A CD1 
3920  N N   . SER A 549 ? 0.3015 0.2110 0.2764 -0.0194 -0.0372 0.0909  541 SER A N   
3921  C CA  . SER A 549 ? 0.3445 0.2474 0.3150 -0.0183 -0.0440 0.1025  541 SER A CA  
3922  C C   . SER A 549 ? 0.3366 0.2344 0.2890 -0.0273 -0.0427 0.1070  541 SER A C   
3923  O O   . SER A 549 ? 0.3293 0.2349 0.2699 -0.0318 -0.0427 0.1060  541 SER A O   
3924  C CB  . SER A 549 ? 0.3533 0.2683 0.3287 -0.0146 -0.0522 0.1068  541 SER A CB  
3925  O OG  . SER A 549 ? 0.4315 0.3405 0.4050 -0.0127 -0.0603 0.1193  541 SER A OG  
3926  N N   . GLU A 550 ? 0.3168 0.2000 0.2659 -0.0299 -0.0405 0.1121  542 GLU A N   
3927  C CA  . GLU A 550 ? 0.3925 0.2723 0.3261 -0.0381 -0.0372 0.1169  542 GLU A CA  
3928  C C   . GLU A 550 ? 0.3780 0.2583 0.2992 -0.0369 -0.0428 0.1238  542 GLU A C   
3929  O O   . GLU A 550 ? 0.3365 0.2172 0.2638 -0.0305 -0.0507 0.1279  542 GLU A O   
3930  C CB  . GLU A 550 ? 0.4606 0.3273 0.3963 -0.0414 -0.0324 0.1184  542 GLU A CB  
3931  C CG  . GLU A 550 ? 0.5073 0.3752 0.4324 -0.0498 -0.0253 0.1212  542 GLU A CG  
3932  C CD  . GLU A 550 ? 0.4446 0.3268 0.3636 -0.0539 -0.0198 0.1173  542 GLU A CD  
3933  O OE1 . GLU A 550 ? 0.5957 0.4859 0.5228 -0.0538 -0.0191 0.1108  542 GLU A OE1 
3934  O OE2 . GLU A 550 ? 0.3858 0.2699 0.2908 -0.0565 -0.0152 0.1209  542 GLU A OE2 
3935  N N   . ALA A 551 ? 0.3598 0.2409 0.2639 -0.0429 -0.0384 0.1251  543 ALA A N   
3936  C CA  . ALA A 551 ? 0.4311 0.3093 0.3191 -0.0429 -0.0431 0.1313  543 ALA A CA  
3937  C C   . ALA A 551 ? 0.4507 0.3173 0.3410 -0.0404 -0.0454 0.1395  543 ALA A C   
3938  O O   . ALA A 551 ? 0.4292 0.2877 0.3266 -0.0416 -0.0398 0.1401  543 ALA A O   
3939  C CB  . ALA A 551 ? 0.4531 0.3314 0.3206 -0.0489 -0.0348 0.1306  543 ALA A CB  
3940  N N   . GLN A 552 ? 0.4912 0.3568 0.3758 -0.0372 -0.0543 0.1458  544 GLN A N   
3941  C CA  . GLN A 552 ? 0.5371 0.3913 0.4197 -0.0349 -0.0564 0.1548  544 GLN A CA  
3942  C C   . GLN A 552 ? 0.5279 0.3769 0.3870 -0.0410 -0.0520 0.1588  544 GLN A C   
3943  O O   . GLN A 552 ? 0.5744 0.4250 0.4175 -0.0420 -0.0578 0.1613  544 GLN A O   
3944  C CB  . GLN A 552 ? 0.5844 0.4416 0.4754 -0.0277 -0.0683 0.1605  544 GLN A CB  
3945  N N   . GLY A 553 ? 0.4987 0.3413 0.3558 -0.0454 -0.0413 0.1593  545 GLY A N   
3946  C CA  . GLY A 553 ? 0.5161 0.3556 0.3536 -0.0508 -0.0330 0.1624  545 GLY A CA  
3947  C C   . GLY A 553 ? 0.5411 0.3889 0.3791 -0.0552 -0.0219 0.1552  545 GLY A C   
3948  O O   . GLY A 553 ? 0.5788 0.4341 0.4322 -0.0549 -0.0214 0.1480  545 GLY A O   
3949  N N   . ASN A 554 ? 0.5288 0.3757 0.3501 -0.0586 -0.0122 0.1577  546 ASN A N   
3950  C CA  . ASN A 554 ? 0.5408 0.3967 0.3630 -0.0614 0.0000  0.1522  546 ASN A CA  
3951  C C   . ASN A 554 ? 0.5036 0.3669 0.3185 -0.0595 -0.0036 0.1438  546 ASN A C   
3952  O O   . ASN A 554 ? 0.4993 0.3589 0.2940 -0.0585 -0.0090 0.1441  546 ASN A O   
3953  C CB  . ASN A 554 ? 0.6143 0.4675 0.4215 -0.0638 0.0129  0.1583  546 ASN A CB  
3954  C CG  . ASN A 554 ? 0.7440 0.5930 0.5637 -0.0674 0.0201  0.1652  546 ASN A CG  
3955  O OD1 . ASN A 554 ? 0.7214 0.5675 0.5588 -0.0685 0.0145  0.1646  546 ASN A OD1 
3956  N ND2 . ASN A 554 ? 0.8331 0.6810 0.6432 -0.0692 0.0327  0.1719  546 ASN A ND2 
3957  N N   . ALA A 555 ? 0.5267 0.3997 0.3573 -0.0597 -0.0010 0.1364  547 ALA A N   
3958  C CA  . ALA A 555 ? 0.4546 0.3339 0.2797 -0.0581 -0.0040 0.1283  547 ALA A CA  
3959  C C   . ALA A 555 ? 0.4808 0.3587 0.2825 -0.0585 0.0053  0.1266  547 ALA A C   
3960  O O   . ALA A 555 ? 0.5194 0.3999 0.3207 -0.0594 0.0195  0.1288  547 ALA A O   
3961  C CB  . ALA A 555 ? 0.4109 0.3005 0.2571 -0.0584 -0.0010 0.1217  547 ALA A CB  
3962  N N   . GLN A 556 ? 0.4368 0.3106 0.2201 -0.0576 -0.0027 0.1229  548 GLN A N   
3963  C CA  . GLN A 556 ? 0.4591 0.3289 0.2182 -0.0577 0.0050  0.1187  548 GLN A CA  
3964  C C   . GLN A 556 ? 0.4794 0.3553 0.2413 -0.0565 0.0082  0.1085  548 GLN A C   
3965  O O   . GLN A 556 ? 0.4630 0.3359 0.2085 -0.0555 0.0182  0.1040  548 GLN A O   
3966  C CB  . GLN A 556 ? 0.4658 0.3241 0.1995 -0.0589 -0.0063 0.1203  548 GLN A CB  
3967  C CG  . GLN A 556 ? 0.6428 0.4941 0.3714 -0.0597 -0.0093 0.1310  548 GLN A CG  
3968  C CD  . GLN A 556 ? 0.7399 0.5817 0.4481 -0.0613 -0.0239 0.1336  548 GLN A CD  
3969  O OE1 . GLN A 556 ? 0.7965 0.6375 0.5130 -0.0609 -0.0354 0.1406  548 GLN A OE1 
3970  N NE2 . GLN A 556 ? 0.7357 0.5694 0.4171 -0.0633 -0.0234 0.1280  548 GLN A NE2 
3971  N N   . ALA A 557 ? 0.3993 0.2830 0.1814 -0.0561 0.0006  0.1050  549 ALA A N   
3972  C CA  . ALA A 557 ? 0.3755 0.2654 0.1626 -0.0550 0.0039  0.0961  549 ALA A CA  
3973  C C   . ALA A 557 ? 0.3532 0.2527 0.1672 -0.0547 -0.0033 0.0956  549 ALA A C   
3974  O O   . ALA A 557 ? 0.3601 0.2595 0.1867 -0.0548 -0.0114 0.1014  549 ALA A O   
3975  C CB  . ALA A 557 ? 0.4373 0.3198 0.2034 -0.0556 -0.0035 0.0895  549 ALA A CB  
3976  N N   . VAL A 558 ? 0.3387 0.2454 0.1611 -0.0539 0.0004  0.0887  550 VAL A N   
3977  C CA  . VAL A 558 ? 0.3153 0.2327 0.1650 -0.0518 -0.0056 0.0855  550 VAL A CA  
3978  C C   . VAL A 558 ? 0.3530 0.2741 0.2024 -0.0498 -0.0112 0.0772  550 VAL A C   
3979  O O   . VAL A 558 ? 0.3135 0.2323 0.1495 -0.0498 -0.0042 0.0714  550 VAL A O   
3980  C CB  . VAL A 558 ? 0.3534 0.2814 0.2253 -0.0509 0.0048  0.0832  550 VAL A CB  
3981  C CG1 . VAL A 558 ? 0.3580 0.2894 0.2227 -0.0504 0.0187  0.0798  550 VAL A CG1 
3982  C CG2 . VAL A 558 ? 0.2874 0.2253 0.1846 -0.0474 -0.0008 0.0768  550 VAL A CG2 
3983  N N   . ILE A 559 ? 0.2924 0.2183 0.1567 -0.0479 -0.0232 0.0773  551 ILE A N   
3984  C CA  . ILE A 559 ? 0.2677 0.1998 0.1385 -0.0463 -0.0287 0.0706  551 ILE A CA  
3985  C C   . ILE A 559 ? 0.2507 0.1948 0.1480 -0.0419 -0.0235 0.0646  551 ILE A C   
3986  O O   . ILE A 559 ? 0.2884 0.2355 0.2034 -0.0393 -0.0254 0.0672  551 ILE A O   
3987  C CB  . ILE A 559 ? 0.2772 0.2100 0.1515 -0.0468 -0.0444 0.0759  551 ILE A CB  
3988  C CG1 . ILE A 559 ? 0.3626 0.2822 0.2089 -0.0521 -0.0518 0.0835  551 ILE A CG1 
3989  C CG2 . ILE A 559 ? 0.2764 0.2164 0.1579 -0.0466 -0.0497 0.0699  551 ILE A CG2 
3990  C CD1 . ILE A 559 ? 0.3112 0.2337 0.1626 -0.0533 -0.0693 0.0900  551 ILE A CD1 
3991  N N   . ILE A 560 ? 0.2306 0.1790 0.1283 -0.0409 -0.0168 0.0568  552 ILE A N   
3992  C CA  . ILE A 560 ? 0.2481 0.2069 0.1676 -0.0371 -0.0132 0.0511  552 ILE A CA  
3993  C C   . ILE A 560 ? 0.2618 0.2253 0.1885 -0.0354 -0.0205 0.0475  552 ILE A C   
3994  O O   . ILE A 560 ? 0.2641 0.2241 0.1774 -0.0378 -0.0225 0.0449  552 ILE A O   
3995  C CB  . ILE A 560 ? 0.2424 0.2044 0.1605 -0.0364 -0.0015 0.0463  552 ILE A CB  
3996  C CG1 . ILE A 560 ? 0.2835 0.2430 0.1958 -0.0386 0.0068  0.0515  552 ILE A CG1 
3997  C CG2 . ILE A 560 ? 0.1818 0.1541 0.1212 -0.0331 0.0004  0.0414  552 ILE A CG2 
3998  C CD1 . ILE A 560 ? 0.2264 0.1899 0.1371 -0.0371 0.0192  0.0488  552 ILE A CD1 
3999  N N   . ALA A 561 ? 0.1845 0.1546 0.1313 -0.0316 -0.0240 0.0477  553 ALA A N   
4000  C CA  . ALA A 561 ? 0.1761 0.1528 0.1333 -0.0298 -0.0293 0.0456  553 ALA A CA  
4001  C C   . ALA A 561 ? 0.1842 0.1673 0.1594 -0.0247 -0.0244 0.0412  553 ALA A C   
4002  O O   . ALA A 561 ? 0.1778 0.1588 0.1582 -0.0229 -0.0203 0.0409  553 ALA A O   
4003  C CB  . ALA A 561 ? 0.1836 0.1616 0.1466 -0.0297 -0.0403 0.0534  553 ALA A CB  
4004  N N   . THR A 562 ? 0.1872 0.1768 0.1700 -0.0234 -0.0252 0.0378  554 THR A N   
4005  C CA  . THR A 562 ? 0.1359 0.1305 0.1329 -0.0185 -0.0205 0.0338  554 THR A CA  
4006  C C   . THR A 562 ? 0.1728 0.1747 0.1846 -0.0155 -0.0246 0.0367  554 THR A C   
4007  O O   . THR A 562 ? 0.1378 0.1430 0.1494 -0.0189 -0.0319 0.0405  554 THR A O   
4008  C CB  . THR A 562 ? 0.2063 0.2025 0.1992 -0.0191 -0.0144 0.0271  554 THR A CB  
4009  O OG1 . THR A 562 ? 0.2005 0.1993 0.1916 -0.0213 -0.0175 0.0262  554 THR A OG1 
4010  C CG2 . THR A 562 ? 0.1560 0.1478 0.1358 -0.0221 -0.0098 0.0259  554 THR A CG2 
4011  N N   . GLY A 563 ? 0.1642 0.1315 0.1852 0.0089  0.0042  0.0310  555 GLY A N   
4012  C CA  . GLY A 563 ? 0.1936 0.1578 0.2202 0.0134  0.0054  0.0275  555 GLY A CA  
4013  C C   . GLY A 563 ? 0.1744 0.1385 0.2073 0.0164  0.0023  0.0309  555 GLY A C   
4014  O O   . GLY A 563 ? 0.1665 0.1255 0.2013 0.0160  -0.0007 0.0358  555 GLY A O   
4015  N N   . SER A 564 ? 0.1630 0.1327 0.1995 0.0193  0.0023  0.0287  556 SER A N   
4016  C CA  . SER A 564 ? 0.2033 0.1743 0.2480 0.0223  -0.0014 0.0316  556 SER A CA  
4017  C C   . SER A 564 ? 0.2123 0.1860 0.2524 0.0200  -0.0073 0.0383  556 SER A C   
4018  O O   . SER A 564 ? 0.1807 0.1541 0.2274 0.0220  -0.0123 0.0422  556 SER A O   
4019  C CB  . SER A 564 ? 0.1521 0.1294 0.2009 0.0245  -0.0002 0.0274  556 SER A CB  
4020  O OG  . SER A 564 ? 0.1869 0.1705 0.2265 0.0224  0.0005  0.0256  556 SER A OG  
4021  N N   . GLU A 565 ? 0.1304 0.1065 0.1596 0.0157  -0.0070 0.0400  557 GLU A N   
4022  C CA  . GLU A 565 ? 0.1379 0.1161 0.1599 0.0125  -0.0116 0.0460  557 GLU A CA  
4023  C C   . GLU A 565 ? 0.1767 0.1472 0.1957 0.0095  -0.0139 0.0522  557 GLU A C   
4024  O O   . GLU A 565 ? 0.1885 0.1588 0.1999 0.0062  -0.0180 0.0580  557 GLU A O   
4025  C CB  . GLU A 565 ? 0.1600 0.1461 0.1715 0.0092  -0.0090 0.0439  557 GLU A CB  
4026  C CG  . GLU A 565 ? 0.1298 0.1221 0.1414 0.0111  -0.0093 0.0402  557 GLU A CG  
4027  C CD  . GLU A 565 ? 0.1975 0.1899 0.2176 0.0152  -0.0060 0.0341  557 GLU A CD  
4028  O OE1 . GLU A 565 ? 0.1679 0.1615 0.1858 0.0150  -0.0014 0.0300  557 GLU A OE1 
4029  O OE2 . GLU A 565 ? 0.1522 0.1435 0.1813 0.0183  -0.0080 0.0337  557 GLU A OE2 
4030  N N   . VAL A 566 ? 0.1826 0.1458 0.2062 0.0101  -0.0116 0.0511  558 VAL A N   
4031  C CA  . VAL A 566 ? 0.2023 0.1567 0.2229 0.0069  -0.0140 0.0571  558 VAL A CA  
4032  C C   . VAL A 566 ? 0.1871 0.1358 0.2120 0.0091  -0.0210 0.0638  558 VAL A C   
4033  O O   . VAL A 566 ? 0.2246 0.1693 0.2417 0.0050  -0.0252 0.0709  558 VAL A O   
4034  C CB  . VAL A 566 ? 0.2056 0.1517 0.2299 0.0069  -0.0103 0.0540  558 VAL A CB  
4035  C CG1 . VAL A 566 ? 0.2319 0.1667 0.2541 0.0039  -0.0132 0.0603  558 VAL A CG1 
4036  C CG2 . VAL A 566 ? 0.1809 0.1330 0.1997 0.0034  -0.0053 0.0492  558 VAL A CG2 
4037  N N   . GLY A 567 ? 0.2240 0.1721 0.2617 0.0152  -0.0225 0.0619  559 GLY A N   
4038  C CA  . GLY A 567 ? 0.2451 0.1889 0.2900 0.0181  -0.0302 0.0685  559 GLY A CA  
4039  C C   . GLY A 567 ? 0.2603 0.2092 0.2953 0.0145  -0.0368 0.0744  559 GLY A C   
4040  O O   . GLY A 567 ? 0.2123 0.1547 0.2431 0.0124  -0.0438 0.0827  559 GLY A O   
4041  N N   . LEU A 568 ? 0.2621 0.2215 0.2916 0.0132  -0.0347 0.0701  560 LEU A N   
4042  C CA  . LEU A 568 ? 0.2360 0.1997 0.2530 0.0089  -0.0397 0.0743  560 LEU A CA  
4043  C C   . LEU A 568 ? 0.2193 0.1784 0.2201 0.0018  -0.0395 0.0796  560 LEU A C   
4044  O O   . LEU A 568 ? 0.2087 0.1639 0.2000 -0.0019 -0.0464 0.0871  560 LEU A O   
4045  C CB  . LEU A 568 ? 0.1760 0.1502 0.1892 0.0085  -0.0352 0.0672  560 LEU A CB  
4046  C CG  . LEU A 568 ? 0.2779 0.2563 0.2753 0.0032  -0.0378 0.0690  560 LEU A CG  
4047  C CD1 . LEU A 568 ? 0.2683 0.2449 0.2662 0.0030  -0.0485 0.0758  560 LEU A CD1 
4048  C CD2 . LEU A 568 ? 0.2845 0.2715 0.2804 0.0040  -0.0323 0.0608  560 LEU A CD2 
4049  N N   . ALA A 569 ? 0.2036 0.1630 0.2006 -0.0007 -0.0319 0.0759  561 ALA A N   
4050  C CA  . ALA A 569 ? 0.2197 0.1757 0.2029 -0.0080 -0.0305 0.0805  561 ALA A CA  
4051  C C   . ALA A 569 ? 0.3067 0.2500 0.2897 -0.0094 -0.0367 0.0893  561 ALA A C   
4052  O O   . ALA A 569 ? 0.2715 0.2104 0.2409 -0.0155 -0.0402 0.0964  561 ALA A O   
4053  C CB  . ALA A 569 ? 0.1917 0.1514 0.1751 -0.0099 -0.0219 0.0749  561 ALA A CB  
4054  N N   . VAL A 570 ? 0.2515 0.1875 0.2484 -0.0040 -0.0378 0.0888  562 VAL A N   
4055  C CA  . VAL A 570 ? 0.2527 0.1748 0.2509 -0.0044 -0.0438 0.0969  562 VAL A CA  
4056  C C   . VAL A 570 ? 0.2627 0.1826 0.2591 -0.0036 -0.0541 0.1045  562 VAL A C   
4057  O O   . VAL A 570 ? 0.2997 0.2124 0.2866 -0.0077 -0.0580 0.1100  562 VAL A O   
4058  C CB  . VAL A 570 ? 0.2609 0.1755 0.2755 0.0020  -0.0419 0.0933  562 VAL A CB  
4059  C CG1 . VAL A 570 ? 0.3154 0.2169 0.3327 0.0031  -0.0473 0.0989  562 VAL A CG1 
4060  C CG2 . VAL A 570 ? 0.2810 0.1958 0.2936 -0.0007 -0.0331 0.0869  562 VAL A CG2 
4061  N N   . GLU A 571 ? 0.2465 0.1743 0.2516 0.0014  -0.0573 0.1021  563 GLU A N   
4062  C CA  . GLU A 571 ? 0.2690 0.1977 0.2728 0.0018  -0.0663 0.1062  563 GLU A CA  
4063  C C   . GLU A 571 ? 0.2927 0.2223 0.2737 -0.0069 -0.0685 0.1108  563 GLU A C   
4064  O O   . GLU A 571 ? 0.2917 0.2160 0.2651 -0.0098 -0.0751 0.1163  563 GLU A O   
4065  C CB  . GLU A 571 ? 0.2990 0.2373 0.3176 0.0080  -0.0686 0.1020  563 GLU A CB  
4066  N N   . ALA A 572 ? 0.2503 0.1864 0.2199 -0.0115 -0.0624 0.1080  564 ALA A N   
4067  C CA  . ALA A 572 ? 0.2944 0.2313 0.2410 -0.0204 -0.0620 0.1109  564 ALA A CA  
4068  C C   . ALA A 572 ? 0.2987 0.2265 0.2343 -0.0265 -0.0601 0.1154  564 ALA A C   
4069  O O   . ALA A 572 ? 0.3087 0.2329 0.2287 -0.0325 -0.0633 0.1195  564 ALA A O   
4070  C CB  . ALA A 572 ? 0.2769 0.2254 0.2177 -0.0223 -0.0516 0.1017  564 ALA A CB  
4071  N N   . GLN A 573 ? 0.3086 0.2323 0.2520 -0.0255 -0.0550 0.1144  565 GLN A N   
4072  C CA  . GLN A 573 ? 0.3048 0.2195 0.2393 -0.0314 -0.0535 0.1185  565 GLN A CA  
4073  C C   . GLN A 573 ? 0.3497 0.2545 0.2841 -0.0302 -0.0626 0.1245  565 GLN A C   
4074  O O   . GLN A 573 ? 0.3276 0.2266 0.2471 -0.0370 -0.0639 0.1293  565 GLN A O   
4075  C CB  . GLN A 573 ? 0.3205 0.2315 0.2653 -0.0301 -0.0477 0.1160  565 GLN A CB  
4076  C CG  . GLN A 573 ? 0.3313 0.2319 0.2693 -0.0356 -0.0468 0.1200  565 GLN A CG  
4077  C CD  . GLN A 573 ? 0.3669 0.2614 0.3169 -0.0332 -0.0431 0.1173  565 GLN A CD  
4078  O OE1 . GLN A 573 ? 0.3091 0.2012 0.2744 -0.0251 -0.0448 0.1141  565 GLN A OE1 
4079  N NE2 . GLN A 573 ? 0.3120 0.2043 0.2552 -0.0405 -0.0375 0.1177  565 GLN A NE2 
4080  N N   . LYS A 574 ? 0.3639 0.2671 0.3156 -0.0216 -0.0685 0.1240  566 LYS A N   
4081  C CA  . LYS A 574 ? 0.3731 0.2679 0.3273 -0.0198 -0.0775 0.1297  566 LYS A CA  
4082  C C   . LYS A 574 ? 0.3825 0.2796 0.3227 -0.0244 -0.0844 0.1338  566 LYS A C   
4083  O O   . LYS A 574 ? 0.3579 0.2466 0.2875 -0.0288 -0.0897 0.1401  566 LYS A O   
4084  C CB  . LYS A 574 ? 0.3463 0.2412 0.3241 -0.0094 -0.0811 0.1272  566 LYS A CB  
4085  N N   . VAL A 575 ? 0.3255 0.2330 0.2643 -0.0240 -0.0847 0.1303  567 VAL A N   
4086  C CA  . VAL A 575 ? 0.3927 0.3018 0.3166 -0.0291 -0.0910 0.1333  567 VAL A CA  
4087  C C   . VAL A 575 ? 0.3799 0.2851 0.2790 -0.0395 -0.0863 0.1356  567 VAL A C   
4088  O O   . VAL A 575 ? 0.3785 0.2776 0.2637 -0.0449 -0.0922 0.1409  567 VAL A O   
4089  C CB  . VAL A 575 ? 0.3617 0.2823 0.2885 -0.0270 -0.0911 0.1282  567 VAL A CB  
4090  C CG1 . VAL A 575 ? 0.3589 0.2803 0.2658 -0.0342 -0.0957 0.1301  567 VAL A CG1 
4091  C CG2 . VAL A 575 ? 0.3237 0.2484 0.2755 -0.0174 -0.0968 0.1266  567 VAL A CG2 
4092  N N   . LEU A 576 ? 0.3698 0.2787 0.2636 -0.0427 -0.0754 0.1316  568 LEU A N   
4093  C CA  . LEU A 576 ? 0.4097 0.3165 0.2825 -0.0525 -0.0690 0.1326  568 LEU A CA  
4094  C C   . LEU A 576 ? 0.4444 0.3390 0.3127 -0.0560 -0.0716 0.1392  568 LEU A C   
4095  O O   . LEU A 576 ? 0.5063 0.3960 0.3561 -0.0639 -0.0724 0.1429  568 LEU A O   
4096  C CB  . LEU A 576 ? 0.3734 0.2881 0.2462 -0.0544 -0.0566 0.1266  568 LEU A CB  
4097  C CG  . LEU A 576 ? 0.3440 0.2703 0.2138 -0.0539 -0.0521 0.1202  568 LEU A CG  
4098  C CD1 . LEU A 576 ? 0.3794 0.3136 0.2579 -0.0524 -0.0420 0.1147  568 LEU A CD1 
4099  C CD2 . LEU A 576 ? 0.3748 0.3024 0.2219 -0.0623 -0.0489 0.1194  568 LEU A CD2 
4100  N N   . ALA A 577 ? 0.3742 0.2632 0.2585 -0.0505 -0.0728 0.1403  569 ALA A N   
4101  C CA  . ALA A 577 ? 0.4094 0.2857 0.2900 -0.0534 -0.0755 0.1465  569 ALA A CA  
4102  C C   . ALA A 577 ? 0.5174 0.3863 0.3914 -0.0543 -0.0870 0.1533  569 ALA A C   
4103  O O   . ALA A 577 ? 0.5006 0.3610 0.3591 -0.0615 -0.0885 0.1588  569 ALA A O   
4104  C CB  . ALA A 577 ? 0.3843 0.2553 0.2842 -0.0464 -0.0750 0.1455  569 ALA A CB  
4105  N N   . GLY A 578 ? 0.4421 0.3144 0.3281 -0.0473 -0.0952 0.1532  570 GLY A N   
4106  C CA  . GLY A 578 ? 0.4324 0.2995 0.3140 -0.0480 -0.1071 0.1595  570 GLY A CA  
4107  C C   . GLY A 578 ? 0.4805 0.3481 0.3374 -0.0578 -0.1080 0.1613  570 GLY A C   
4108  O O   . GLY A 578 ? 0.5518 0.4124 0.4002 -0.0608 -0.1178 0.1677  570 GLY A O   
4109  N N   . GLN A 579 ? 0.4582 0.3334 0.3033 -0.0628 -0.0981 0.1558  571 GLN A N   
4110  C CA  . GLN A 579 ? 0.5099 0.3851 0.3301 -0.0726 -0.0959 0.1560  571 GLN A CA  
4111  C C   . GLN A 579 ? 0.5479 0.4180 0.3526 -0.0812 -0.0869 0.1572  571 GLN A C   
4112  O O   . GLN A 579 ? 0.6033 0.4743 0.3876 -0.0897 -0.0818 0.1559  571 GLN A O   
4113  C CB  . GLN A 579 ? 0.4965 0.3838 0.3137 -0.0726 -0.0900 0.1482  571 GLN A CB  
4114  C CG  . GLN A 579 ? 0.5641 0.4570 0.3943 -0.0657 -0.0988 0.1468  571 GLN A CG  
4115  C CD  . GLN A 579 ? 0.6685 0.5718 0.4929 -0.0668 -0.0931 0.1393  571 GLN A CD  
4116  O OE1 . GLN A 579 ? 0.6703 0.5757 0.4777 -0.0735 -0.0835 0.1355  571 GLN A OE1 
4117  N NE2 . GLN A 579 ? 0.6780 0.5881 0.5171 -0.0601 -0.0986 0.1367  571 GLN A NE2 
4118  N N   . GLY A 580 ? 0.5488 0.4135 0.3631 -0.0793 -0.0844 0.1593  572 GLY A N   
4119  C CA  . GLY A 580 ? 0.5240 0.3845 0.3261 -0.0875 -0.0758 0.1604  572 GLY A CA  
4120  C C   . GLY A 580 ? 0.4988 0.3706 0.3000 -0.0902 -0.0617 0.1527  572 GLY A C   
4121  O O   . GLY A 580 ? 0.5123 0.3839 0.2995 -0.0988 -0.0534 0.1524  572 GLY A O   
4122  N N   . ILE A 581 ? 0.4596 0.3414 0.2759 -0.0831 -0.0586 0.1465  573 ILE A N   
4123  C CA  . ILE A 581 ? 0.4743 0.3678 0.2922 -0.0848 -0.0459 0.1391  573 ILE A CA  
4124  C C   . ILE A 581 ? 0.4536 0.3487 0.2919 -0.0785 -0.0435 0.1371  573 ILE A C   
4125  O O   . ILE A 581 ? 0.4040 0.3012 0.2574 -0.0700 -0.0482 0.1353  573 ILE A O   
4126  C CB  . ILE A 581 ? 0.5214 0.4255 0.3364 -0.0829 -0.0438 0.1330  573 ILE A CB  
4127  C CG1 . ILE A 581 ? 0.5653 0.4667 0.3586 -0.0898 -0.0460 0.1344  573 ILE A CG1 
4128  C CG2 . ILE A 581 ? 0.5350 0.4515 0.3545 -0.0836 -0.0307 0.1253  573 ILE A CG2 
4129  C CD1 . ILE A 581 ? 0.5743 0.4836 0.3643 -0.0877 -0.0463 0.1288  573 ILE A CD1 
4130  N N   . ALA A 582 ? 0.4204 0.3144 0.2592 -0.0832 -0.0361 0.1370  574 ALA A N   
4131  C CA  . ALA A 582 ? 0.3828 0.2761 0.2390 -0.0788 -0.0341 0.1353  574 ALA A CA  
4132  C C   . ALA A 582 ? 0.3597 0.2669 0.2238 -0.0779 -0.0247 0.1277  574 ALA A C   
4133  O O   . ALA A 582 ? 0.3814 0.2970 0.2381 -0.0845 -0.0152 0.1246  574 ALA A O   
4134  C CB  . ALA A 582 ? 0.4168 0.3012 0.2698 -0.0849 -0.0318 0.1392  574 ALA A CB  
4135  N N   . VAL A 583 ? 0.3742 0.2842 0.2540 -0.0698 -0.0269 0.1246  575 VAL A N   
4136  C CA  . VAL A 583 ? 0.3577 0.2798 0.2466 -0.0686 -0.0190 0.1181  575 VAL A CA  
4137  C C   . VAL A 583 ? 0.3254 0.2430 0.2312 -0.0634 -0.0204 0.1170  575 VAL A C   
4138  O O   . VAL A 583 ? 0.3175 0.2243 0.2301 -0.0579 -0.0279 0.1198  575 VAL A O   
4139  C CB  . VAL A 583 ? 0.3454 0.2774 0.2344 -0.0642 -0.0191 0.1139  575 VAL A CB  
4140  C CG1 . VAL A 583 ? 0.3231 0.2577 0.1939 -0.0693 -0.0181 0.1142  575 VAL A CG1 
4141  C CG2 . VAL A 583 ? 0.3240 0.2515 0.2250 -0.0547 -0.0284 0.1148  575 VAL A CG2 
4142  N N   . ARG A 584 ? 0.2922 0.2184 0.2053 -0.0654 -0.0129 0.1124  576 ARG A N   
4143  C CA  . ARG A 584 ? 0.2792 0.2030 0.2076 -0.0610 -0.0131 0.1095  576 ARG A CA  
4144  C C   . ARG A 584 ? 0.3057 0.2401 0.2459 -0.0515 -0.0121 0.1007  576 ARG A C   
4145  O O   . ARG A 584 ? 0.2945 0.2410 0.2317 -0.0509 -0.0084 0.0964  576 ARG A O   
4146  C CB  . ARG A 584 ? 0.3044 0.2333 0.2355 -0.0680 -0.0056 0.1070  576 ARG A CB  
4147  C CG  . ARG A 584 ? 0.4005 0.3388 0.3468 -0.0633 -0.0017 0.0980  576 ARG A CG  
4148  C CD  . ARG A 584 ? 0.3008 0.2490 0.2490 -0.0715 0.0057  0.0959  576 ARG A CD  
4149  N NE  . ARG A 584 ? 0.3332 0.2699 0.2761 -0.0803 0.0050  0.1025  576 ARG A NE  
4150  C CZ  . ARG A 584 ? 0.3732 0.3154 0.3212 -0.0872 0.0096  0.1009  576 ARG A CZ  
4151  N NH1 . ARG A 584 ? 0.2801 0.2390 0.2390 -0.0860 0.0146  0.0936  576 ARG A NH1 
4152  N NH2 . ARG A 584 ? 0.3686 0.3008 0.3130 -0.0927 0.0090  0.1040  576 ARG A NH2 
4153  N N   . VAL A 585 ? 0.2491 0.1778 0.2021 -0.0443 -0.0150 0.0977  577 VAL A N   
4154  C CA  . VAL A 585 ? 0.2459 0.1834 0.2101 -0.0361 -0.0133 0.0892  577 VAL A CA  
4155  C C   . VAL A 585 ? 0.2368 0.1765 0.2099 -0.0362 -0.0086 0.0832  577 VAL A C   
4156  O O   . VAL A 585 ? 0.2632 0.1915 0.2392 -0.0374 -0.0101 0.0849  577 VAL A O   
4157  C CB  . VAL A 585 ? 0.2813 0.2117 0.2533 -0.0277 -0.0197 0.0898  577 VAL A CB  
4158  C CG1 . VAL A 585 ? 0.2228 0.1625 0.2051 -0.0206 -0.0168 0.0809  577 VAL A CG1 
4159  C CG2 . VAL A 585 ? 0.2860 0.2143 0.2497 -0.0281 -0.0261 0.0965  577 VAL A CG2 
4160  N N   . VAL A 586 ? 0.2058 0.1592 0.1825 -0.0350 -0.0035 0.0763  578 VAL A N   
4161  C CA  . VAL A 586 ? 0.1960 0.1531 0.1809 -0.0347 -0.0002 0.0702  578 VAL A CA  
4162  C C   . VAL A 586 ? 0.2078 0.1672 0.2000 -0.0264 -0.0006 0.0637  578 VAL A C   
4163  O O   . VAL A 586 ? 0.2202 0.1878 0.2119 -0.0227 -0.0000 0.0614  578 VAL A O   
4164  C CB  . VAL A 586 ? 0.2351 0.2063 0.2198 -0.0401 0.0054  0.0679  578 VAL A CB  
4165  C CG1 . VAL A 586 ? 0.1826 0.1602 0.1769 -0.0382 0.0073  0.0612  578 VAL A CG1 
4166  C CG2 . VAL A 586 ? 0.2062 0.1745 0.1854 -0.0496 0.0068  0.0738  578 VAL A CG2 
4167  N N   . SER A 587 ? 0.1846 0.1359 0.1825 -0.0240 -0.0014 0.0607  579 SER A N   
4168  C CA  . SER A 587 ? 0.2072 0.1607 0.2109 -0.0176 -0.0004 0.0540  579 SER A CA  
4169  C C   . SER A 587 ? 0.2217 0.1837 0.2273 -0.0200 0.0026  0.0492  579 SER A C   
4170  O O   . SER A 587 ? 0.2197 0.1791 0.2251 -0.0255 0.0028  0.0499  579 SER A O   
4171  C CB  . SER A 587 ? 0.1739 0.1134 0.1817 -0.0140 -0.0019 0.0527  579 SER A CB  
4172  O OG  . SER A 587 ? 0.1832 0.1246 0.1952 -0.0087 -0.0000 0.0461  579 SER A OG  
4173  N N   . MET A 588 ? 0.1872 0.1590 0.1949 -0.0162 0.0042  0.0446  580 MET A N   
4174  C CA  . MET A 588 ? 0.1693 0.1499 0.1800 -0.0177 0.0059  0.0406  580 MET A CA  
4175  C C   . MET A 588 ? 0.1914 0.1693 0.2039 -0.0126 0.0057  0.0350  580 MET A C   
4176  O O   . MET A 588 ? 0.1409 0.1267 0.1548 -0.0091 0.0067  0.0320  580 MET A O   
4177  C CB  . MET A 588 ? 0.1391 0.1341 0.1503 -0.0185 0.0086  0.0405  580 MET A CB  
4178  C CG  . MET A 588 ? 0.1558 0.1611 0.1731 -0.0198 0.0099  0.0371  580 MET A CG  
4179  S SD  . MET A 588 ? 0.1829 0.2052 0.2033 -0.0217 0.0147  0.0371  580 MET A SD  
4180  C CE  . MET A 588 ? 0.1432 0.1644 0.1605 -0.0306 0.0163  0.0432  580 MET A CE  
4181  N N   . PRO A 589 ? 0.1647 0.1306 0.1765 -0.0126 0.0047  0.0334  581 PRO A N   
4182  C CA  . PRO A 589 ? 0.2106 0.1729 0.2221 -0.0087 0.0053  0.0280  581 PRO A CA  
4183  C C   . PRO A 589 ? 0.1822 0.1524 0.1941 -0.0096 0.0049  0.0249  581 PRO A C   
4184  O O   . PRO A 589 ? 0.1598 0.1302 0.1707 -0.0059 0.0054  0.0213  581 PRO A O   
4185  C CB  . PRO A 589 ? 0.2100 0.1570 0.2191 -0.0104 0.0053  0.0267  581 PRO A CB  
4186  C CG  . PRO A 589 ? 0.2123 0.1562 0.2208 -0.0161 0.0039  0.0313  581 PRO A CG  
4187  C CD  . PRO A 589 ? 0.2190 0.1723 0.2291 -0.0158 0.0037  0.0361  581 PRO A CD  
4188  N N   . SER A 590 ? 0.1366 0.1134 0.1505 -0.0145 0.0036  0.0264  582 SER A N   
4189  C CA  . SER A 590 ? 0.1686 0.1545 0.1855 -0.0144 0.0022  0.0241  582 SER A CA  
4190  C C   . SER A 590 ? 0.1698 0.1699 0.1935 -0.0173 0.0029  0.0266  582 SER A C   
4191  O O   . SER A 590 ? 0.1511 0.1522 0.1770 -0.0233 0.0020  0.0289  582 SER A O   
4192  C CB  . SER A 590 ? 0.1497 0.1277 0.1632 -0.0179 -0.0010 0.0219  582 SER A CB  
4193  O OG  . SER A 590 ? 0.1629 0.1496 0.1800 -0.0173 -0.0036 0.0204  582 SER A OG  
4194  N N   . THR A 591 ? 0.1462 0.1571 0.1736 -0.0133 0.0050  0.0256  583 THR A N   
4195  C CA  . THR A 591 ? 0.1417 0.1672 0.1772 -0.0154 0.0068  0.0266  583 THR A CA  
4196  C C   . THR A 591 ? 0.1169 0.1477 0.1597 -0.0183 0.0032  0.0258  583 THR A C   
4197  O O   . THR A 591 ? 0.1465 0.1860 0.1965 -0.0233 0.0037  0.0278  583 THR A O   
4198  C CB  . THR A 591 ? 0.1715 0.2058 0.2093 -0.0098 0.0099  0.0243  583 THR A CB  
4199  O OG1 . THR A 591 ? 0.1259 0.1582 0.1644 -0.0051 0.0073  0.0209  583 THR A OG1 
4200  C CG2 . THR A 591 ? 0.1256 0.1551 0.1556 -0.0077 0.0124  0.0252  583 THR A CG2 
4201  N N   . SER A 592 ? 0.1476 0.1734 0.1887 -0.0155 -0.0007 0.0232  584 SER A N   
4202  C CA  . SER A 592 ? 0.1872 0.2170 0.2343 -0.0181 -0.0060 0.0228  584 SER A CA  
4203  C C   . SER A 592 ? 0.2026 0.2298 0.2502 -0.0262 -0.0083 0.0252  584 SER A C   
4204  O O   . SER A 592 ? 0.1875 0.2265 0.2459 -0.0302 -0.0099 0.0266  584 SER A O   
4205  C CB  . SER A 592 ? 0.1903 0.2090 0.2293 -0.0155 -0.0101 0.0203  584 SER A CB  
4206  O OG  . SER A 592 ? 0.1911 0.2049 0.2242 -0.0094 -0.0068 0.0183  584 SER A OG  
4207  N N   . VAL A 593 ? 0.1547 0.1668 0.1916 -0.0288 -0.0081 0.0255  585 VAL A N   
4208  C CA  . VAL A 593 ? 0.1422 0.1481 0.1773 -0.0367 -0.0104 0.0272  585 VAL A CA  
4209  C C   . VAL A 593 ? 0.1594 0.1736 0.2006 -0.0410 -0.0069 0.0309  585 VAL A C   
4210  O O   . VAL A 593 ? 0.1942 0.2132 0.2412 -0.0481 -0.0089 0.0328  585 VAL A O   
4211  C CB  . VAL A 593 ? 0.1846 0.1705 0.2066 -0.0370 -0.0102 0.0258  585 VAL A CB  
4212  C CG1 . VAL A 593 ? 0.1791 0.1559 0.1979 -0.0452 -0.0120 0.0272  585 VAL A CG1 
4213  C CG2 . VAL A 593 ? 0.1870 0.1645 0.2015 -0.0340 -0.0128 0.0218  585 VAL A CG2 
4214  N N   . PHE A 594 ? 0.1668 0.1823 0.2061 -0.0376 -0.0018 0.0323  586 PHE A N   
4215  C CA  . PHE A 594 ? 0.1426 0.1649 0.1852 -0.0424 0.0020  0.0362  586 PHE A CA  
4216  C C   . PHE A 594 ? 0.1613 0.2027 0.2175 -0.0451 0.0032  0.0363  586 PHE A C   
4217  O O   . PHE A 594 ? 0.1700 0.2168 0.2312 -0.0525 0.0043  0.0390  586 PHE A O   
4218  C CB  . PHE A 594 ? 0.1696 0.1908 0.2067 -0.0383 0.0065  0.0375  586 PHE A CB  
4219  C CG  . PHE A 594 ? 0.1514 0.1778 0.1885 -0.0439 0.0106  0.0419  586 PHE A CG  
4220  C CD1 . PHE A 594 ? 0.1710 0.1875 0.2034 -0.0507 0.0096  0.0459  586 PHE A CD1 
4221  C CD2 . PHE A 594 ? 0.1919 0.2319 0.2325 -0.0428 0.0158  0.0417  586 PHE A CD2 
4222  C CE1 . PHE A 594 ? 0.2417 0.2617 0.2724 -0.0568 0.0134  0.0504  586 PHE A CE1 
4223  C CE2 . PHE A 594 ? 0.2240 0.2678 0.2624 -0.0490 0.0203  0.0456  586 PHE A CE2 
4224  C CZ  . PHE A 594 ? 0.2622 0.2960 0.2954 -0.0562 0.0189  0.0503  586 PHE A CZ  
4225  N N   . ASP A 595 ? 0.1791 0.2308 0.2426 -0.0391 0.0031  0.0332  587 ASP A N   
4226  C CA  . ASP A 595 ? 0.1879 0.2590 0.2671 -0.0399 0.0051  0.0328  587 ASP A CA  
4227  C C   . ASP A 595 ? 0.2314 0.3085 0.3212 -0.0463 -0.0003 0.0337  587 ASP A C   
4228  O O   . ASP A 595 ? 0.2294 0.3234 0.3345 -0.0491 0.0019  0.0343  587 ASP A O   
4229  C CB  . ASP A 595 ? 0.1881 0.2664 0.2727 -0.0312 0.0055  0.0292  587 ASP A CB  
4230  C CG  . ASP A 595 ? 0.2314 0.3085 0.3087 -0.0260 0.0119  0.0281  587 ASP A CG  
4231  O OD1 . ASP A 595 ? 0.2789 0.3532 0.3491 -0.0294 0.0164  0.0305  587 ASP A OD1 
4232  O OD2 . ASP A 595 ? 0.2409 0.3192 0.3190 -0.0189 0.0120  0.0250  587 ASP A OD2 
4233  N N   . ARG A 596 ? 0.1837 0.2477 0.2660 -0.0490 -0.0072 0.0336  588 ARG A N   
4234  C CA  . ARG A 596 ? 0.2084 0.2768 0.2990 -0.0562 -0.0135 0.0346  588 ARG A CA  
4235  C C   . ARG A 596 ? 0.2038 0.2633 0.2886 -0.0659 -0.0134 0.0374  588 ARG A C   
4236  O O   . ARG A 596 ? 0.1887 0.2493 0.2781 -0.0733 -0.0191 0.0381  588 ARG A O   
4237  C CB  . ARG A 596 ? 0.2751 0.3353 0.3610 -0.0543 -0.0221 0.0324  588 ARG A CB  
4238  C CG  . ARG A 596 ? 0.2517 0.2894 0.3179 -0.0533 -0.0235 0.0308  588 ARG A CG  
4239  C CD  . ARG A 596 ? 0.3478 0.3789 0.4092 -0.0534 -0.0320 0.0289  588 ARG A CD  
4240  N NE  . ARG A 596 ? 0.3514 0.3609 0.3936 -0.0531 -0.0324 0.0264  588 ARG A NE  
4241  C CZ  . ARG A 596 ? 0.3138 0.3162 0.3478 -0.0459 -0.0307 0.0240  588 ARG A CZ  
4242  N NH1 . ARG A 596 ? 0.2063 0.2204 0.2486 -0.0387 -0.0289 0.0239  588 ARG A NH1 
4243  N NH2 . ARG A 596 ? 0.3568 0.3403 0.3747 -0.0463 -0.0301 0.0215  588 ARG A NH2 
4244  N N   . GLN A 597 ? 0.1833 0.2335 0.2579 -0.0662 -0.0077 0.0391  589 GLN A N   
4245  C CA  . GLN A 597 ? 0.2125 0.2549 0.2827 -0.0754 -0.0070 0.0425  589 GLN A CA  
4246  C C   . GLN A 597 ? 0.2045 0.2655 0.2893 -0.0822 -0.0033 0.0451  589 GLN A C   
4247  O O   . GLN A 597 ? 0.2543 0.3327 0.3503 -0.0784 0.0014  0.0443  589 GLN A O   
4248  C CB  . GLN A 597 ? 0.2168 0.2443 0.2731 -0.0733 -0.0027 0.0444  589 GLN A CB  
4249  C CG  . GLN A 597 ? 0.1831 0.1953 0.2282 -0.0657 -0.0048 0.0415  589 GLN A CG  
4250  C CD  . GLN A 597 ? 0.2848 0.2844 0.3246 -0.0690 -0.0109 0.0390  589 GLN A CD  
4251  O OE1 . GLN A 597 ? 0.2460 0.2355 0.2819 -0.0766 -0.0126 0.0405  589 GLN A OE1 
4252  N NE2 . GLN A 597 ? 0.2535 0.2529 0.2924 -0.0640 -0.0143 0.0352  589 GLN A NE2 
4253  N N   . ASP A 598 ? 0.2024 0.2594 0.2873 -0.0925 -0.0048 0.0478  590 ASP A N   
4254  C CA  . ASP A 598 ? 0.2693 0.3442 0.3689 -0.1004 -0.0009 0.0503  590 ASP A CA  
4255  C C   . ASP A 598 ? 0.2472 0.3267 0.3437 -0.0996 0.0089  0.0527  590 ASP A C   
4256  O O   . ASP A 598 ? 0.2163 0.2818 0.2976 -0.0952 0.0111  0.0537  590 ASP A O   
4257  C CB  . ASP A 598 ? 0.3080 0.3756 0.4067 -0.1127 -0.0047 0.0530  590 ASP A CB  
4258  C CG  . ASP A 598 ? 0.4173 0.4607 0.4967 -0.1158 -0.0038 0.0557  590 ASP A CG  
4259  O OD1 . ASP A 598 ? 0.4269 0.4696 0.5025 -0.1194 0.0026  0.0596  590 ASP A OD1 
4260  O OD2 . ASP A 598 ? 0.4598 0.4842 0.5277 -0.1149 -0.0093 0.0539  590 ASP A OD2 
4261  N N   . ALA A 599 ? 0.2479 0.3477 0.3595 -0.1040 0.0148  0.0535  591 ALA A N   
4262  C CA  . ALA A 599 ? 0.2310 0.3370 0.3394 -0.1033 0.0250  0.0548  591 ALA A CA  
4263  C C   . ALA A 599 ? 0.2231 0.3113 0.3131 -0.1097 0.0273  0.0600  591 ALA A C   
4264  O O   . ALA A 599 ? 0.2349 0.3170 0.3123 -0.1062 0.0319  0.0613  591 ALA A O   
4265  C CB  . ALA A 599 ? 0.1974 0.3284 0.3262 -0.1080 0.0320  0.0542  591 ALA A CB  
4266  N N   . ALA A 600 ? 0.2303 0.3094 0.3183 -0.1193 0.0235  0.0631  592 ALA A N   
4267  C CA  . ALA A 600 ? 0.3094 0.3699 0.3803 -0.1256 0.0250  0.0687  592 ALA A CA  
4268  C C   . ALA A 600 ? 0.2673 0.3067 0.3212 -0.1170 0.0211  0.0688  592 ALA A C   
4269  O O   . ALA A 600 ? 0.2290 0.2583 0.2695 -0.1168 0.0241  0.0728  592 ALA A O   
4270  C CB  . ALA A 600 ? 0.3054 0.3569 0.3766 -0.1347 0.0208  0.0700  592 ALA A CB  
4271  N N   . TYR A 601 ? 0.2218 0.2541 0.2759 -0.1103 0.0144  0.0647  593 TYR A N   
4272  C CA  . TYR A 601 ? 0.2480 0.2620 0.2885 -0.1019 0.0117  0.0643  593 TYR A CA  
4273  C C   . TYR A 601 ? 0.2363 0.2574 0.2743 -0.0932 0.0159  0.0633  593 TYR A C   
4274  O O   . TYR A 601 ? 0.2509 0.2598 0.2768 -0.0902 0.0164  0.0661  593 TYR A O   
4275  C CB  . TYR A 601 ? 0.2201 0.2257 0.2608 -0.0971 0.0050  0.0594  593 TYR A CB  
4276  C CG  . TYR A 601 ? 0.2236 0.2109 0.2522 -0.0889 0.0033  0.0586  593 TYR A CG  
4277  C CD1 . TYR A 601 ? 0.2226 0.1892 0.2408 -0.0915 0.0018  0.0619  593 TYR A CD1 
4278  C CD2 . TYR A 601 ? 0.1957 0.1868 0.2245 -0.0786 0.0034  0.0548  593 TYR A CD2 
4279  C CE1 . TYR A 601 ? 0.2658 0.2170 0.2759 -0.0836 0.0005  0.0611  593 TYR A CE1 
4280  C CE2 . TYR A 601 ? 0.2238 0.1999 0.2437 -0.0715 0.0023  0.0540  593 TYR A CE2 
4281  C CZ  . TYR A 601 ? 0.2711 0.2281 0.2827 -0.0738 0.0009  0.0571  593 TYR A CZ  
4282  O OH  . TYR A 601 ? 0.2201 0.1636 0.2260 -0.0664 0.0000  0.0563  593 TYR A OH  
4283  N N   . GLN A 602 ? 0.2291 0.2693 0.2785 -0.0891 0.0186  0.0593  594 GLN A N   
4284  C CA  . GLN A 602 ? 0.2470 0.2930 0.2933 -0.0812 0.0228  0.0577  594 GLN A CA  
4285  C C   . GLN A 602 ? 0.2122 0.2585 0.2498 -0.0860 0.0292  0.0622  594 GLN A C   
4286  O O   . GLN A 602 ? 0.2515 0.2917 0.2782 -0.0812 0.0303  0.0631  594 GLN A O   
4287  C CB  . GLN A 602 ? 0.2621 0.3279 0.3234 -0.0764 0.0249  0.0526  594 GLN A CB  
4288  C CG  . GLN A 602 ? 0.2858 0.3510 0.3541 -0.0717 0.0178  0.0485  594 GLN A CG  
4289  C CD  . GLN A 602 ? 0.3623 0.4436 0.4429 -0.0645 0.0191  0.0440  594 GLN A CD  
4290  O OE1 . GLN A 602 ? 0.3568 0.4437 0.4358 -0.0594 0.0245  0.0425  594 GLN A OE1 
4291  N NE2 . GLN A 602 ? 0.3677 0.4557 0.4601 -0.0644 0.0137  0.0419  594 GLN A NE2 
4292  N N   . ALA A 603 ? 0.2456 0.2990 0.2873 -0.0961 0.0334  0.0652  595 ALA A N   
4293  C CA  . ALA A 603 ? 0.2600 0.3122 0.2910 -0.1025 0.0398  0.0701  595 ALA A CA  
4294  C C   . ALA A 603 ? 0.2442 0.2732 0.2578 -0.1048 0.0353  0.0763  595 ALA A C   
4295  O O   . ALA A 603 ? 0.2545 0.2775 0.2544 -0.1057 0.0377  0.0802  595 ALA A O   
4296  C CB  . ALA A 603 ? 0.3269 0.3929 0.3678 -0.1136 0.0461  0.0716  595 ALA A CB  
4297  N N   . ALA A 604 ? 0.2584 0.2737 0.2721 -0.1059 0.0285  0.0774  596 ALA A N   
4298  C CA  . ALA A 604 ? 0.2654 0.2578 0.2649 -0.1067 0.0239  0.0829  596 ALA A CA  
4299  C C   . ALA A 604 ? 0.2487 0.2331 0.2409 -0.0958 0.0207  0.0820  596 ALA A C   
4300  O O   . ALA A 604 ? 0.3182 0.2887 0.2982 -0.0958 0.0185  0.0876  596 ALA A O   
4301  C CB  . ALA A 604 ? 0.2804 0.2595 0.2824 -0.1096 0.0181  0.0828  596 ALA A CB  
4302  N N   . VAL A 605 ? 0.2318 0.2249 0.2318 -0.0868 0.0199  0.0754  597 VAL A N   
4303  C CA  . VAL A 605 ? 0.2166 0.2039 0.2116 -0.0768 0.0173  0.0739  597 VAL A CA  
4304  C C   . VAL A 605 ? 0.3053 0.3022 0.2945 -0.0755 0.0218  0.0745  597 VAL A C   
4305  O O   . VAL A 605 ? 0.2745 0.2628 0.2539 -0.0720 0.0194  0.0774  597 VAL A O   
4306  C CB  . VAL A 605 ? 0.2009 0.1921 0.2050 -0.0688 0.0148  0.0668  597 VAL A CB  
4307  C CG1 . VAL A 605 ? 0.1938 0.1814 0.1939 -0.0591 0.0131  0.0650  597 VAL A CG1 
4308  C CG2 . VAL A 605 ? 0.2471 0.2262 0.2534 -0.0706 0.0104  0.0658  597 VAL A CG2 
4309  N N   . LEU A 606 ? 0.2111 0.2257 0.2068 -0.0782 0.0283  0.0715  598 LEU A N   
4310  C CA  . LEU A 606 ? 0.2282 0.2527 0.2189 -0.0770 0.0341  0.0703  598 LEU A CA  
4311  C C   . LEU A 606 ? 0.2354 0.2696 0.2255 -0.0871 0.0420  0.0725  598 LEU A C   
4312  O O   . LEU A 606 ? 0.2538 0.3053 0.2566 -0.0879 0.0480  0.0679  598 LEU A O   
4313  C CB  . LEU A 606 ? 0.2071 0.2445 0.2081 -0.0684 0.0358  0.0625  598 LEU A CB  
4314  C CG  . LEU A 606 ? 0.2138 0.2434 0.2163 -0.0588 0.0291  0.0595  598 LEU A CG  
4315  C CD1 . LEU A 606 ? 0.2236 0.2663 0.2367 -0.0518 0.0311  0.0523  598 LEU A CD1 
4316  C CD2 . LEU A 606 ? 0.2010 0.2185 0.1903 -0.0556 0.0258  0.0627  598 LEU A CD2 
4317  N N   . PRO A 607 ? 0.2574 0.2808 0.2336 -0.0952 0.0424  0.0798  599 PRO A N   
4318  C CA  . PRO A 607 ? 0.3116 0.3428 0.2868 -0.1058 0.0504  0.0819  599 PRO A CA  
4319  C C   . PRO A 607 ? 0.3291 0.3757 0.3041 -0.1049 0.0600  0.0770  599 PRO A C   
4320  O O   . PRO A 607 ? 0.2687 0.3141 0.2342 -0.1002 0.0603  0.0758  599 PRO A O   
4321  C CB  . PRO A 607 ? 0.3246 0.3362 0.2823 -0.1097 0.0465  0.0887  599 PRO A CB  
4322  C CG  . PRO A 607 ? 0.2705 0.2655 0.2260 -0.1046 0.0362  0.0920  599 PRO A CG  
4323  C CD  . PRO A 607 ? 0.2596 0.2620 0.2221 -0.0947 0.0347  0.0863  599 PRO A CD  
4324  N N   . GLU A 608 ? 0.3275 0.3881 0.3139 -0.1093 0.0679  0.0738  600 GLU A N   
4325  C CA  . GLU A 608 ? 0.3167 0.3913 0.3049 -0.1082 0.0781  0.0684  600 GLU A CA  
4326  C C   . GLU A 608 ? 0.3675 0.4306 0.3326 -0.1109 0.0806  0.0714  600 GLU A C   
4327  O O   . GLU A 608 ? 0.4339 0.4837 0.3867 -0.1169 0.0777  0.0777  600 GLU A O   
4328  C CB  . GLU A 608 ? 0.4094 0.5001 0.4158 -0.1125 0.0858  0.0653  600 GLU A CB  
4329  N N   . GLY A 609 ? 0.3916 0.4591 0.3503 -0.1065 0.0852  0.0670  601 GLY A N   
4330  C CA  . GLY A 609 ? 0.4147 0.4721 0.3509 -0.1092 0.0871  0.0691  601 GLY A CA  
4331  C C   . GLY A 609 ? 0.4311 0.4707 0.3491 -0.1071 0.0766  0.0745  601 GLY A C   
4332  O O   . GLY A 609 ? 0.4511 0.4823 0.3500 -0.1090 0.0766  0.0762  601 GLY A O   
4333  N N   . LEU A 610 ? 0.3782 0.4116 0.3019 -0.1033 0.0673  0.0774  602 LEU A N   
4334  C CA  . LEU A 610 ? 0.4534 0.4712 0.3634 -0.0999 0.0571  0.0822  602 LEU A CA  
4335  C C   . LEU A 610 ? 0.3782 0.4021 0.2893 -0.0926 0.0568  0.0772  602 LEU A C   
4336  O O   . LEU A 610 ? 0.3166 0.3501 0.2450 -0.0864 0.0569  0.0721  602 LEU A O   
4337  C CB  . LEU A 610 ? 0.4830 0.4898 0.3990 -0.0988 0.0476  0.0876  602 LEU A CB  
4338  C CG  . LEU A 610 ? 0.4542 0.4430 0.3586 -0.0955 0.0364  0.0939  602 LEU A CG  
4339  C CD1 . LEU A 610 ? 0.4943 0.4714 0.3813 -0.1010 0.0347  0.0994  602 LEU A CD1 
4340  C CD2 . LEU A 610 ? 0.4301 0.4100 0.3451 -0.0924 0.0287  0.0968  602 LEU A CD2 
4341  N N   . PRO A 611 ? 0.3936 0.4119 0.2882 -0.0916 0.0557  0.0770  603 PRO A N   
4342  C CA  . PRO A 611 ? 0.3650 0.3886 0.2600 -0.0850 0.0555  0.0717  603 PRO A CA  
4343  C C   . PRO A 611 ? 0.2560 0.2751 0.1641 -0.0750 0.0452  0.0712  603 PRO A C   
4344  O O   . PRO A 611 ? 0.2779 0.2846 0.1835 -0.0749 0.0362  0.0779  603 PRO A O   
4345  C CB  . PRO A 611 ? 0.3387 0.3519 0.2118 -0.0866 0.0525  0.0735  603 PRO A CB  
4346  C CG  . PRO A 611 ? 0.4110 0.4201 0.2743 -0.0945 0.0567  0.0765  603 PRO A CG  
4347  C CD  . PRO A 611 ? 0.4121 0.4201 0.2870 -0.0973 0.0553  0.0810  603 PRO A CD  
4348  N N   . ARG A 612 ? 0.2377 0.2664 0.1596 -0.0667 0.0470  0.0631  604 ARG A N   
4349  C CA  . ARG A 612 ? 0.2205 0.2463 0.1552 -0.0576 0.0391  0.0614  604 ARG A CA  
4350  C C   . ARG A 612 ? 0.2812 0.3052 0.2113 -0.0510 0.0356  0.0578  604 ARG A C   
4351  O O   . ARG A 612 ? 0.2655 0.2965 0.1919 -0.0503 0.0417  0.0522  604 ARG A O   
4352  C CB  . ARG A 612 ? 0.2295 0.2665 0.1841 -0.0537 0.0425  0.0557  604 ARG A CB  
4353  C CG  . ARG A 612 ? 0.2155 0.2563 0.1762 -0.0611 0.0462  0.0586  604 ARG A CG  
4354  C CD  . ARG A 612 ? 0.2116 0.2669 0.1916 -0.0584 0.0506  0.0526  604 ARG A CD  
4355  N NE  . ARG A 612 ? 0.2245 0.2844 0.2111 -0.0664 0.0538  0.0555  604 ARG A NE  
4356  C CZ  . ARG A 612 ? 0.3265 0.4012 0.3299 -0.0671 0.0587  0.0515  604 ARG A CZ  
4357  N NH1 . ARG A 612 ? 0.2764 0.3620 0.2915 -0.0597 0.0609  0.0447  604 ARG A NH1 
4358  N NH2 . ARG A 612 ? 0.2882 0.3668 0.2975 -0.0753 0.0610  0.0547  604 ARG A NH2 
4359  N N   . ILE A 613 ? 0.2255 0.2401 0.1568 -0.0463 0.0262  0.0607  605 ILE A N   
4360  C CA  . ILE A 613 ? 0.2365 0.2498 0.1669 -0.0398 0.0220  0.0574  605 ILE A CA  
4361  C C   . ILE A 613 ? 0.2199 0.2324 0.1663 -0.0320 0.0177  0.0548  605 ILE A C   
4362  O O   . ILE A 613 ? 0.2497 0.2544 0.2006 -0.0315 0.0124  0.0592  605 ILE A O   
4363  C CB  . ILE A 613 ? 0.2204 0.2233 0.1362 -0.0422 0.0143  0.0637  605 ILE A CB  
4364  C CG1 . ILE A 613 ? 0.2412 0.2428 0.1372 -0.0513 0.0184  0.0668  605 ILE A CG1 
4365  C CG2 . ILE A 613 ? 0.3322 0.3355 0.2486 -0.0363 0.0103  0.0597  605 ILE A CG2 
4366  C CD1 . ILE A 613 ? 0.3031 0.2978 0.1927 -0.0590 0.0178  0.0750  605 ILE A CD1 
4367  N N   . ALA A 614 ? 0.1758 0.1951 0.1300 -0.0262 0.0202  0.0475  606 ALA A N   
4368  C CA  . ALA A 614 ? 0.1615 0.1794 0.1284 -0.0195 0.0167  0.0447  606 ALA A CA  
4369  C C   . ALA A 614 ? 0.1969 0.2102 0.1622 -0.0149 0.0113  0.0440  606 ALA A C   
4370  O O   . ALA A 614 ? 0.2087 0.2241 0.1661 -0.0151 0.0120  0.0419  606 ALA A O   
4371  C CB  . ALA A 614 ? 0.1630 0.1902 0.1400 -0.0161 0.0219  0.0379  606 ALA A CB  
4372  N N   . VAL A 615 ? 0.1904 0.1976 0.1637 -0.0111 0.0063  0.0453  607 VAL A N   
4373  C CA  . VAL A 615 ? 0.1509 0.1547 0.1263 -0.0067 0.0011  0.0449  607 VAL A CA  
4374  C C   . VAL A 615 ? 0.1585 0.1620 0.1458 -0.0011 0.0018  0.0402  607 VAL A C   
4375  O O   . VAL A 615 ? 0.1531 0.1516 0.1467 -0.0004 0.0009  0.0415  607 VAL A O   
4376  C CB  . VAL A 615 ? 0.1608 0.1564 0.1343 -0.0078 -0.0060 0.0522  607 VAL A CB  
4377  C CG1 . VAL A 615 ? 0.1697 0.1646 0.1468 -0.0037 -0.0112 0.0514  607 VAL A CG1 
4378  C CG2 . VAL A 615 ? 0.2030 0.1968 0.1619 -0.0148 -0.0068 0.0579  607 VAL A CG2 
4379  N N   . GLU A 616 ? 0.1755 0.1830 0.1645 0.0022  0.0033  0.0347  608 GLU A N   
4380  C CA  . GLU A 616 ? 0.1264 0.1330 0.1241 0.0067  0.0042  0.0303  608 GLU A CA  
4381  C C   . GLU A 616 ? 0.1170 0.1256 0.1144 0.0095  0.0038  0.0263  608 GLU A C   
4382  O O   . GLU A 616 ? 0.1470 0.1596 0.1378 0.0083  0.0055  0.0243  608 GLU A O   
4383  C CB  . GLU A 616 ? 0.1273 0.1374 0.1277 0.0065  0.0085  0.0271  608 GLU A CB  
4384  C CG  . GLU A 616 ? 0.1530 0.1609 0.1592 0.0102  0.0091  0.0227  608 GLU A CG  
4385  C CD  . GLU A 616 ? 0.1171 0.1277 0.1260 0.0093  0.0113  0.0210  608 GLU A CD  
4386  O OE1 . GLU A 616 ? 0.1463 0.1636 0.1554 0.0099  0.0137  0.0184  608 GLU A OE1 
4387  O OE2 . GLU A 616 ? 0.1647 0.1705 0.1761 0.0080  0.0103  0.0222  608 GLU A OE2 
4388  N N   . ALA A 617 ? 0.1297 0.1350 0.1341 0.0127  0.0021  0.0249  609 ALA A N   
4389  C CA  . ALA A 617 ? 0.1425 0.1492 0.1476 0.0147  0.0015  0.0214  609 ALA A CA  
4390  C C   . ALA A 617 ? 0.2043 0.2125 0.2089 0.0164  0.0058  0.0157  609 ALA A C   
4391  O O   . ALA A 617 ? 0.1818 0.1876 0.1908 0.0187  0.0067  0.0126  609 ALA A O   
4392  C CB  . ALA A 617 ? 0.1515 0.1550 0.1657 0.0171  -0.0012 0.0220  609 ALA A CB  
4393  N N   . GLY A 618 ? 0.1893 0.2014 0.1887 0.0152  0.0085  0.0145  610 GLY A N   
4394  C CA  . GLY A 618 ? 0.1592 0.1729 0.1589 0.0172  0.0118  0.0098  610 GLY A CA  
4395  C C   . GLY A 618 ? 0.1458 0.1647 0.1401 0.0160  0.0149  0.0083  610 GLY A C   
4396  O O   . GLY A 618 ? 0.1446 0.1652 0.1328 0.0128  0.0147  0.0108  610 GLY A O   
4397  N N   . HIS A 619 ? 0.1337 0.1544 0.1300 0.0184  0.0179  0.0042  611 HIS A N   
4398  C CA  . HIS A 619 ? 0.1522 0.1781 0.1457 0.0182  0.0222  0.0015  611 HIS A CA  
4399  C C   . HIS A 619 ? 0.1333 0.1646 0.1267 0.0147  0.0244  0.0047  611 HIS A C   
4400  O O   . HIS A 619 ? 0.1399 0.1715 0.1385 0.0137  0.0229  0.0079  611 HIS A O   
4401  C CB  . HIS A 619 ? 0.1475 0.1745 0.1473 0.0223  0.0242  -0.0025 611 HIS A CB  
4402  C CG  . HIS A 619 ? 0.1412 0.1709 0.1387 0.0239  0.0288  -0.0072 611 HIS A CG  
4403  N ND1 . HIS A 619 ? 0.1465 0.1831 0.1440 0.0224  0.0340  -0.0081 611 HIS A ND1 
4404  C CD2 . HIS A 619 ? 0.1360 0.1614 0.1310 0.0266  0.0297  -0.0118 611 HIS A CD2 
4405  C CE1 . HIS A 619 ? 0.1669 0.2035 0.1623 0.0246  0.0383  -0.0134 611 HIS A CE1 
4406  N NE2 . HIS A 619 ? 0.1755 0.2048 0.1691 0.0272  0.0354  -0.0156 611 HIS A NE2 
4407  N N   . THR A 620 ? 0.1288 0.1634 0.1151 0.0121  0.0284  0.0036  612 THR A N   
4408  C CA  . THR A 620 ? 0.1885 0.2279 0.1727 0.0075  0.0314  0.0068  612 THR A CA  
4409  C C   . THR A 620 ? 0.2226 0.2705 0.2162 0.0085  0.0370  0.0044  612 THR A C   
4410  O O   . THR A 620 ? 0.1394 0.1919 0.1348 0.0045  0.0390  0.0076  612 THR A O   
4411  C CB  . THR A 620 ? 0.1670 0.2057 0.1372 0.0031  0.0340  0.0067  612 THR A CB  
4412  O OG1 . THR A 620 ? 0.1481 0.1890 0.1162 0.0052  0.0396  0.0001  612 THR A OG1 
4413  C CG2 . THR A 620 ? 0.1436 0.1749 0.1047 0.0013  0.0273  0.0099  612 THR A CG2 
4414  N N   . ASN A 621 ? 0.1623 0.2126 0.1627 0.0134  0.0392  -0.0008 613 ASN A N   
4415  C CA  A ASN A 621 ? 0.1818 0.2417 0.1908 0.0142  0.0458  -0.0037 613 ASN A CA  
4416  C CA  B ASN A 621 ? 0.1876 0.2475 0.1974 0.0147  0.0456  -0.0039 613 ASN A CA  
4417  C C   . ASN A 621 ? 0.1806 0.2471 0.2016 0.0129  0.0446  -0.0003 613 ASN A C   
4418  O O   . ASN A 621 ? 0.2034 0.2793 0.2304 0.0106  0.0502  -0.0007 613 ASN A O   
4419  C CB  A ASN A 621 ? 0.2250 0.2851 0.2397 0.0206  0.0478  -0.0098 613 ASN A CB  
4420  C CB  B ASN A 621 ? 0.2234 0.2831 0.2405 0.0214  0.0462  -0.0092 613 ASN A CB  
4421  C CG  A ASN A 621 ? 0.2615 0.3181 0.2646 0.0203  0.0528  -0.0146 613 ASN A CG  
4422  C CG  B ASN A 621 ? 0.2541 0.3245 0.2863 0.0240  0.0511  -0.0118 613 ASN A CG  
4423  O OD1 A ASN A 621 ? 0.2280 0.2864 0.2353 0.0243  0.0578  -0.0203 613 ASN A OD1 
4424  O OD1 B ASN A 621 ? 0.3135 0.3894 0.3462 0.0240  0.0589  -0.0158 613 ASN A OD1 
4425  N ND2 A ASN A 621 ? 0.3133 0.3645 0.3017 0.0154  0.0510  -0.0123 613 ASN A ND2 
4426  N ND2 B ASN A 621 ? 0.2660 0.3394 0.3107 0.0261  0.0464  -0.0096 613 ASN A ND2 
4427  N N   . GLY A 622 ? 0.2035 0.2650 0.2276 0.0135  0.0378  0.0028  614 GLY A N   
4428  C CA  . GLY A 622 ? 0.2350 0.3013 0.2688 0.0113  0.0359  0.0059  614 GLY A CA  
4429  C C   . GLY A 622 ? 0.2384 0.3063 0.2681 0.0045  0.0375  0.0104  614 GLY A C   
4430  O O   . GLY A 622 ? 0.2044 0.2786 0.2427 0.0014  0.0379  0.0124  614 GLY A O   
4431  N N   . TRP A 623 ? 0.1590 0.2210 0.1757 0.0015  0.0378  0.0125  615 TRP A N   
4432  C CA  . TRP A 623 ? 0.1680 0.2289 0.1792 -0.0052 0.0382  0.0178  615 TRP A CA  
4433  C C   . TRP A 623 ? 0.1334 0.2034 0.1439 -0.0098 0.0461  0.0173  615 TRP A C   
4434  O O   . TRP A 623 ? 0.1855 0.2555 0.1926 -0.0163 0.0471  0.0219  615 TRP A O   
4435  C CB  . TRP A 623 ? 0.1959 0.2462 0.1939 -0.0065 0.0340  0.0212  615 TRP A CB  
4436  C CG  . TRP A 623 ? 0.1686 0.2107 0.1696 -0.0032 0.0272  0.0225  615 TRP A CG  
4437  C CD1 . TRP A 623 ? 0.1892 0.2262 0.1893 0.0015  0.0241  0.0200  615 TRP A CD1 
4438  C CD2 . TRP A 623 ? 0.1736 0.2114 0.1790 -0.0050 0.0237  0.0260  615 TRP A CD2 
4439  N NE1 . TRP A 623 ? 0.1770 0.2073 0.1809 0.0029  0.0196  0.0216  615 TRP A NE1 
4440  C CE2 . TRP A 623 ? 0.1523 0.1823 0.1589 -0.0009 0.0192  0.0251  615 TRP A CE2 
4441  C CE3 . TRP A 623 ? 0.2013 0.2404 0.2094 -0.0102 0.0242  0.0295  615 TRP A CE3 
4442  C CZ2 . TRP A 623 ? 0.1732 0.1962 0.1828 -0.0015 0.0158  0.0270  615 TRP A CZ2 
4443  C CZ3 . TRP A 623 ? 0.1884 0.2201 0.1994 -0.0109 0.0200  0.0317  615 TRP A CZ3 
4444  C CH2 . TRP A 623 ? 0.1633 0.1867 0.1746 -0.0064 0.0160  0.0302  615 TRP A CH2 
4445  N N   . TYR A 624 ? 0.1345 0.2119 0.1484 -0.0070 0.0525  0.0117  616 TYR A N   
4446  C CA  . TYR A 624 ? 0.1439 0.2305 0.1579 -0.0116 0.0618  0.0104  616 TYR A CA  
4447  C C   . TYR A 624 ? 0.1403 0.2377 0.1705 -0.0140 0.0638  0.0117  616 TYR A C   
4448  O O   . TYR A 624 ? 0.1670 0.2711 0.1968 -0.0204 0.0706  0.0129  616 TYR A O   
4449  C CB  . TYR A 624 ? 0.1617 0.2526 0.1760 -0.0074 0.0689  0.0031  616 TYR A CB  
4450  C CG  . TYR A 624 ? 0.1838 0.2641 0.1788 -0.0080 0.0678  0.0023  616 TYR A CG  
4451  C CD1 . TYR A 624 ? 0.2220 0.2988 0.1997 -0.0155 0.0713  0.0048  616 TYR A CD1 
4452  C CD2 . TYR A 624 ? 0.2626 0.3359 0.2559 -0.0021 0.0626  -0.0004 616 TYR A CD2 
4453  C CE1 . TYR A 624 ? 0.2974 0.3644 0.2570 -0.0168 0.0688  0.0046  616 TYR A CE1 
4454  C CE2 . TYR A 624 ? 0.2599 0.3241 0.2364 -0.0034 0.0608  -0.0009 616 TYR A CE2 
4455  C CZ  . TYR A 624 ? 0.3491 0.4104 0.3090 -0.0107 0.0635  0.0016  616 TYR A CZ  
4456  O OH  . TYR A 624 ? 0.3496 0.4021 0.2927 -0.0126 0.0604  0.0015  616 TYR A OH  
4457  N N   . LYS A 625 ? 0.1291 0.2280 0.1727 -0.0099 0.0576  0.0117  617 LYS A N   
4458  C CA  . LYS A 625 ? 0.1602 0.2679 0.2184 -0.0132 0.0570  0.0140  617 LYS A CA  
4459  C C   . LYS A 625 ? 0.1593 0.2630 0.2094 -0.0220 0.0566  0.0201  617 LYS A C   
4460  O O   . LYS A 625 ? 0.1810 0.2942 0.2400 -0.0277 0.0605  0.0216  617 LYS A O   
4461  C CB  . LYS A 625 ? 0.1739 0.2789 0.2416 -0.0086 0.0481  0.0141  617 LYS A CB  
4462  C CG  . LYS A 625 ? 0.2739 0.3854 0.3543 -0.0130 0.0450  0.0171  617 LYS A CG  
4463  C CD  . LYS A 625 ? 0.4033 0.5057 0.4840 -0.0108 0.0352  0.0184  617 LYS A CD  
4464  C CE  . LYS A 625 ? 0.4455 0.5531 0.5369 -0.0163 0.0313  0.0212  617 LYS A CE  
4465  N NZ  . LYS A 625 ? 0.4444 0.5462 0.5388 -0.0134 0.0224  0.0210  617 LYS A NZ  
4466  N N   . TYR A 626 ? 0.1372 0.2270 0.1715 -0.0235 0.0520  0.0238  618 TYR A N   
4467  C CA  . TYR A 626 ? 0.2033 0.2861 0.2283 -0.0311 0.0505  0.0302  618 TYR A CA  
4468  C C   . TYR A 626 ? 0.1761 0.2567 0.1854 -0.0366 0.0562  0.0322  618 TYR A C   
4469  O O   . TYR A 626 ? 0.2037 0.2867 0.2102 -0.0445 0.0604  0.0357  618 TYR A O   
4470  C CB  . TYR A 626 ? 0.1945 0.2626 0.2130 -0.0291 0.0414  0.0335  618 TYR A CB  
4471  C CG  . TYR A 626 ? 0.1834 0.2509 0.2134 -0.0259 0.0358  0.0322  618 TYR A CG  
4472  C CD1 . TYR A 626 ? 0.2705 0.3392 0.3072 -0.0312 0.0341  0.0349  618 TYR A CD1 
4473  C CD2 . TYR A 626 ? 0.1886 0.2535 0.2212 -0.0184 0.0322  0.0284  618 TYR A CD2 
4474  C CE1 . TYR A 626 ? 0.3139 0.3809 0.3587 -0.0293 0.0285  0.0337  618 TYR A CE1 
4475  C CE2 . TYR A 626 ? 0.2317 0.2948 0.2721 -0.0165 0.0272  0.0274  618 TYR A CE2 
4476  C CZ  . TYR A 626 ? 0.2919 0.3559 0.3378 -0.0219 0.0251  0.0300  618 TYR A CZ  
4477  O OH  . TYR A 626 ? 0.2911 0.3522 0.3424 -0.0208 0.0195  0.0289  618 TYR A OH  
4478  N N   . VAL A 627 ? 0.1794 0.2543 0.1769 -0.0333 0.0560  0.0303  619 VAL A N   
4479  C CA  . VAL A 627 ? 0.2258 0.2956 0.2048 -0.0394 0.0593  0.0331  619 VAL A CA  
4480  C C   . VAL A 627 ? 0.2589 0.3390 0.2363 -0.0421 0.0708  0.0284  619 VAL A C   
4481  O O   . VAL A 627 ? 0.2262 0.3033 0.1879 -0.0496 0.0755  0.0310  619 VAL A O   
4482  C CB  . VAL A 627 ? 0.2420 0.3000 0.2071 -0.0362 0.0529  0.0341  619 VAL A CB  
4483  C CG1 . VAL A 627 ? 0.1723 0.2212 0.1420 -0.0323 0.0428  0.0376  619 VAL A CG1 
4484  C CG2 . VAL A 627 ? 0.1775 0.2391 0.1426 -0.0302 0.0560  0.0267  619 VAL A CG2 
4485  N N   . GLY A 628 ? 0.1786 0.2700 0.1713 -0.0364 0.0758  0.0214  620 GLY A N   
4486  C CA  . GLY A 628 ? 0.2280 0.3301 0.2223 -0.0384 0.0881  0.0160  620 GLY A CA  
4487  C C   . GLY A 628 ? 0.2344 0.3299 0.2085 -0.0396 0.0925  0.0129  620 GLY A C   
4488  O O   . GLY A 628 ? 0.2325 0.3165 0.1938 -0.0373 0.0853  0.0141  620 GLY A O   
4489  N N   . LEU A 629 ? 0.2133 0.3165 0.1850 -0.0436 0.1050  0.0086  621 LEU A N   
4490  C CA  . LEU A 629 ? 0.3504 0.4463 0.3032 -0.0440 0.1095  0.0043  621 LEU A CA  
4491  C C   . LEU A 629 ? 0.4010 0.4829 0.3270 -0.0522 0.1052  0.0109  621 LEU A C   
4492  O O   . LEU A 629 ? 0.4209 0.4935 0.3292 -0.0522 0.1038  0.0089  621 LEU A O   
4493  C CB  . LEU A 629 ? 0.2922 0.3960 0.2527 -0.0426 0.1207  -0.0018 621 LEU A CB  
4494  C CG  . LEU A 629 ? 0.2721 0.3883 0.2587 -0.0330 0.1239  -0.0085 621 LEU A CG  
4495  C CD1 . LEU A 629 ? 0.3089 0.4329 0.3026 -0.0316 0.1347  -0.0138 621 LEU A CD1 
4496  C CD2 . LEU A 629 ? 0.3199 0.4303 0.3052 -0.0252 0.1191  -0.0131 621 LEU A CD2 
4497  N N   . ASN A 630 ? 0.3785 0.4579 0.3014 -0.0591 0.1020  0.0190  622 ASN A N   
4498  C CA  . ASN A 630 ? 0.4081 0.4733 0.3067 -0.0665 0.0969  0.0260  622 ASN A CA  
4499  C C   . ASN A 630 ? 0.3809 0.4366 0.2735 -0.0674 0.0843  0.0343  622 ASN A C   
4500  O O   . ASN A 630 ? 0.3423 0.3852 0.2161 -0.0724 0.0778  0.0407  622 ASN A O   
4501  C CB  . ASN A 630 ? 0.4274 0.4938 0.3239 -0.0741 0.1025  0.0296  622 ASN A CB  
4502  C CG  . ASN A 630 ? 0.5153 0.5897 0.4145 -0.0739 0.1149  0.0221  622 ASN A CG  
4503  O OD1 . ASN A 630 ? 0.5443 0.6151 0.4325 -0.0718 0.1177  0.0166  622 ASN A OD1 
4504  N ND2 . ASN A 630 ? 0.5858 0.6712 0.5004 -0.0760 0.1222  0.0217  622 ASN A ND2 
4505  N N   . GLY A 631 ? 0.2542 0.3128 0.1662 -0.0593 0.0776  0.0337  623 GLY A N   
4506  C CA  . GLY A 631 ? 0.2344 0.2824 0.1459 -0.0557 0.0643  0.0393  623 GLY A CA  
4507  C C   . GLY A 631 ? 0.2408 0.2837 0.1469 -0.0496 0.0591  0.0357  623 GLY A C   
4508  O O   . GLY A 631 ? 0.2613 0.3052 0.1572 -0.0502 0.0646  0.0303  623 GLY A O   
4509  N N   . ALA A 632 ? 0.2230 0.2600 0.1359 -0.0440 0.0486  0.0384  624 ALA A N   
4510  C CA  . ALA A 632 ? 0.2624 0.2949 0.1717 -0.0387 0.0432  0.0354  624 ALA A CA  
4511  C C   . ALA A 632 ? 0.2088 0.2398 0.1339 -0.0311 0.0355  0.0358  624 ALA A C   
4512  O O   . ALA A 632 ? 0.2163 0.2474 0.1522 -0.0305 0.0334  0.0390  624 ALA A O   
4513  C CB  . ALA A 632 ? 0.2334 0.2556 0.1217 -0.0441 0.0371  0.0407  624 ALA A CB  
4514  N N   . VAL A 633 ? 0.1911 0.2202 0.1169 -0.0258 0.0319  0.0320  625 VAL A N   
4515  C CA  . VAL A 633 ? 0.1899 0.2177 0.1296 -0.0188 0.0261  0.0311  625 VAL A CA  
4516  C C   . VAL A 633 ? 0.2529 0.2743 0.1868 -0.0172 0.0187  0.0321  625 VAL A C   
4517  O O   . VAL A 633 ? 0.2435 0.2642 0.1665 -0.0187 0.0196  0.0291  625 VAL A O   
4518  C CB  . VAL A 633 ? 0.1617 0.1966 0.1143 -0.0129 0.0310  0.0237  625 VAL A CB  
4519  C CG1 . VAL A 633 ? 0.1786 0.2109 0.1437 -0.0073 0.0256  0.0238  625 VAL A CG1 
4520  C CG2 . VAL A 633 ? 0.1738 0.2175 0.1327 -0.0148 0.0391  0.0218  625 VAL A CG2 
4521  N N   . VAL A 634 ? 0.1707 0.1875 0.1126 -0.0142 0.0115  0.0358  626 VAL A N   
4522  C CA  . VAL A 634 ? 0.1889 0.2018 0.1314 -0.0116 0.0044  0.0363  626 VAL A CA  
4523  C C   . VAL A 634 ? 0.1624 0.1773 0.1194 -0.0049 0.0051  0.0314  626 VAL A C   
4524  O O   . VAL A 634 ? 0.1982 0.2114 0.1657 -0.0024 0.0037  0.0330  626 VAL A O   
4525  C CB  . VAL A 634 ? 0.1765 0.1827 0.1183 -0.0131 -0.0041 0.0445  626 VAL A CB  
4526  C CG1 . VAL A 634 ? 0.2103 0.2146 0.1566 -0.0099 -0.0114 0.0446  626 VAL A CG1 
4527  C CG2 . VAL A 634 ? 0.2392 0.2418 0.1638 -0.0207 -0.0052 0.0502  626 VAL A CG2 
4528  N N   . GLY A 635 ? 0.1497 0.1670 0.1061 -0.0026 0.0074  0.0252  627 GLY A N   
4529  C CA  . GLY A 635 ? 0.1688 0.1870 0.1364 0.0029  0.0084  0.0205  627 GLY A CA  
4530  C C   . GLY A 635 ? 0.2005 0.2178 0.1653 0.0044  0.0073  0.0161  627 GLY A C   
4531  O O   . GLY A 635 ? 0.1751 0.1906 0.1312 0.0014  0.0035  0.0176  627 GLY A O   
4532  N N   . ILE A 636 ? 0.1284 0.1463 0.0998 0.0084  0.0100  0.0110  628 ILE A N   
4533  C CA  . ILE A 636 ? 0.1304 0.1466 0.0996 0.0096  0.0093  0.0065  628 ILE A CA  
4534  C C   . ILE A 636 ? 0.1379 0.1549 0.1094 0.0129  0.0149  0.0007  628 ILE A C   
4535  O O   . ILE A 636 ? 0.1765 0.1940 0.1565 0.0159  0.0162  0.0004  628 ILE A O   
4536  C CB  . ILE A 636 ? 0.1448 0.1585 0.1220 0.0112  0.0043  0.0078  628 ILE A CB  
4537  C CG1 . ILE A 636 ? 0.1384 0.1502 0.1139 0.0118  0.0043  0.0028  628 ILE A CG1 
4538  C CG2 . ILE A 636 ? 0.1535 0.1664 0.1416 0.0145  0.0054  0.0084  628 ILE A CG2 
4539  C CD1 . ILE A 636 ? 0.1726 0.1834 0.1567 0.0124  -0.0002 0.0038  628 ILE A CD1 
4540  N N   . ASN A 637 ? 0.1328 0.1491 0.0963 0.0122  0.0179  -0.0039 629 ASN A N   
4541  C CA  . ASN A 637 ? 0.1574 0.1740 0.1237 0.0158  0.0232  -0.0094 629 ASN A CA  
4542  C C   . ASN A 637 ? 0.2026 0.2136 0.1671 0.0174  0.0224  -0.0140 629 ASN A C   
4543  O O   . ASN A 637 ? 0.2438 0.2533 0.2097 0.0206  0.0264  -0.0188 629 ASN A O   
4544  C CB  . ASN A 637 ? 0.1954 0.2155 0.1554 0.0143  0.0295  -0.0120 629 ASN A CB  
4545  C CG  . ASN A 637 ? 0.1759 0.2022 0.1399 0.0129  0.0317  -0.0081 629 ASN A CG  
4546  O OD1 . ASN A 637 ? 0.1694 0.1966 0.1412 0.0135  0.0283  -0.0038 629 ASN A OD1 
4547  N ND2 . ASN A 637 ? 0.2354 0.2656 0.1941 0.0105  0.0379  -0.0100 629 ASN A ND2 
4548  N N   . ARG A 638 ? 0.1688 0.1768 0.1311 0.0152  0.0174  -0.0127 630 ARG A N   
4549  C CA  . ARG A 638 ? 0.1414 0.1439 0.1022 0.0156  0.0163  -0.0167 630 ARG A CA  
4550  C C   . ARG A 638 ? 0.1582 0.1594 0.1285 0.0170  0.0130  -0.0146 630 ARG A C   
4551  O O   . ARG A 638 ? 0.1626 0.1666 0.1398 0.0175  0.0114  -0.0103 630 ARG A O   
4552  C CB  . ARG A 638 ? 0.2335 0.2340 0.1835 0.0107  0.0133  -0.0176 630 ARG A CB  
4553  C CG  . ARG A 638 ? 0.2010 0.2046 0.1512 0.0072  0.0071  -0.0115 630 ARG A CG  
4554  C CD  . ARG A 638 ? 0.2465 0.2477 0.1907 0.0027  0.0014  -0.0122 630 ARG A CD  
4555  N NE  . ARG A 638 ? 0.3205 0.3205 0.2749 0.0042  -0.0007 -0.0132 630 ARG A NE  
4556  C CZ  . ARG A 638 ? 0.3268 0.3257 0.2808 0.0008  -0.0055 -0.0140 630 ARG A CZ  
4557  N NH1 . ARG A 638 ? 0.2758 0.2736 0.2183 -0.0045 -0.0099 -0.0140 630 ARG A NH1 
4558  N NH2 . ARG A 638 ? 0.2072 0.2057 0.1717 0.0020  -0.0060 -0.0149 630 ARG A NH2 
4559  N N   . PHE A 639 ? 0.1304 0.1264 0.1006 0.0172  0.0127  -0.0180 631 PHE A N   
4560  C CA  . PHE A 639 ? 0.1212 0.1155 0.0994 0.0176  0.0108  -0.0166 631 PHE A CA  
4561  C C   . PHE A 639 ? 0.1592 0.1575 0.1415 0.0146  0.0061  -0.0129 631 PHE A C   
4562  O O   . PHE A 639 ? 0.1692 0.1696 0.1461 0.0115  0.0029  -0.0120 631 PHE A O   
4563  C CB  . PHE A 639 ? 0.1252 0.1124 0.1012 0.0175  0.0118  -0.0209 631 PHE A CB  
4564  C CG  . PHE A 639 ? 0.1508 0.1329 0.1255 0.0214  0.0154  -0.0236 631 PHE A CG  
4565  C CD1 . PHE A 639 ? 0.1746 0.1561 0.1548 0.0242  0.0162  -0.0215 631 PHE A CD1 
4566  C CD2 . PHE A 639 ? 0.1598 0.1371 0.1278 0.0222  0.0176  -0.0282 631 PHE A CD2 
4567  C CE1 . PHE A 639 ? 0.1624 0.1392 0.1423 0.0278  0.0180  -0.0233 631 PHE A CE1 
4568  C CE2 . PHE A 639 ? 0.1765 0.1492 0.1455 0.0266  0.0203  -0.0304 631 PHE A CE2 
4569  C CZ  . PHE A 639 ? 0.1785 0.1512 0.1538 0.0294  0.0199  -0.0275 631 PHE A CZ  
4570  N N   . GLY A 640 ? 0.1260 0.1251 0.1182 0.0155  0.0056  -0.0107 632 GLY A N   
4571  C CA  . GLY A 640 ? 0.1114 0.1149 0.1116 0.0139  0.0014  -0.0072 632 GLY A CA  
4572  C C   . GLY A 640 ? 0.1874 0.1913 0.1897 0.0107  -0.0016 -0.0089 632 GLY A C   
4573  O O   . GLY A 640 ? 0.1262 0.1263 0.1205 0.0089  -0.0010 -0.0127 632 GLY A O   
4574  N N   . GLU A 641 ? 0.1162 0.1248 0.1303 0.0099  -0.0049 -0.0062 633 GLU A N   
4575  C CA  . GLU A 641 ? 0.1335 0.1444 0.1532 0.0065  -0.0082 -0.0074 633 GLU A CA  
4576  C C   . GLU A 641 ? 0.1095 0.1244 0.1463 0.0076  -0.0069 -0.0062 633 GLU A C   
4577  O O   . GLU A 641 ? 0.1094 0.1263 0.1537 0.0107  -0.0062 -0.0032 633 GLU A O   
4578  C CB  . GLU A 641 ? 0.1306 0.1459 0.1480 0.0030  -0.0162 -0.0046 633 GLU A CB  
4579  C CG  . GLU A 641 ? 0.1691 0.1801 0.1683 0.0002  -0.0173 -0.0067 633 GLU A CG  
4580  C CD  . GLU A 641 ? 0.2117 0.2176 0.2040 -0.0028 -0.0158 -0.0123 633 GLU A CD  
4581  O OE1 . GLU A 641 ? 0.2236 0.2303 0.2254 -0.0041 -0.0156 -0.0138 633 GLU A OE1 
4582  O OE2 . GLU A 641 ? 0.2429 0.2433 0.2201 -0.0040 -0.0142 -0.0156 633 GLU A OE2 
4583  N N   . SER A 642 ? 0.1105 0.1261 0.1535 0.0049  -0.0059 -0.0089 634 SER A N   
4584  C CA  . SER A 642 ? 0.1060 0.1265 0.1667 0.0053  -0.0037 -0.0086 634 SER A CA  
4585  C C   . SER A 642 ? 0.1212 0.1513 0.1959 0.0047  -0.0113 -0.0045 634 SER A C   
4586  O O   . SER A 642 ? 0.1270 0.1612 0.2037 0.0006  -0.0170 -0.0046 634 SER A O   
4587  C CB  . SER A 642 ? 0.1257 0.1435 0.1877 0.0018  0.0005  -0.0128 634 SER A CB  
4588  O OG  . SER A 642 ? 0.1240 0.1477 0.2041 0.0015  0.0037  -0.0130 634 SER A OG  
4589  N N   . ALA A 643 ? 0.1130 0.1463 0.1977 0.0087  -0.0120 -0.0008 635 ALA A N   
4590  C CA  . ALA A 643 ? 0.1386 0.1805 0.2389 0.0093  -0.0197 0.0039  635 ALA A CA  
4591  C C   . ALA A 643 ? 0.1145 0.1566 0.2259 0.0146  -0.0171 0.0066  635 ALA A C   
4592  O O   . ALA A 643 ? 0.1130 0.1481 0.2160 0.0169  -0.0105 0.0050  635 ALA A O   
4593  C CB  . ALA A 643 ? 0.1121 0.1543 0.2004 0.0069  -0.0293 0.0078  635 ALA A CB  
4594  N N   . PRO A 644 ? 0.1122 0.1617 0.2430 0.0167  -0.0224 0.0105  636 PRO A N   
4595  C CA  . PRO A 644 ? 0.1051 0.1529 0.2455 0.0221  -0.0205 0.0132  636 PRO A CA  
4596  C C   . PRO A 644 ? 0.1313 0.1716 0.2542 0.0230  -0.0225 0.0165  636 PRO A C   
4597  O O   . PRO A 644 ? 0.1347 0.1742 0.2435 0.0200  -0.0291 0.0192  636 PRO A O   
4598  C CB  . PRO A 644 ? 0.1192 0.1764 0.2820 0.0238  -0.0291 0.0180  636 PRO A CB  
4599  C CG  . PRO A 644 ? 0.1026 0.1682 0.2742 0.0196  -0.0312 0.0155  636 PRO A CG  
4600  C CD  . PRO A 644 ? 0.1147 0.1744 0.2615 0.0144  -0.0301 0.0123  636 PRO A CD  
4601  N N   . ALA A 645 ? 0.1107 0.1453 0.2348 0.0267  -0.0166 0.0161  637 ALA A N   
4602  C CA  . ALA A 645 ? 0.1385 0.1658 0.2461 0.0269  -0.0168 0.0185  637 ALA A CA  
4603  C C   . ALA A 645 ? 0.1702 0.1985 0.2757 0.0265  -0.0269 0.0258  637 ALA A C   
4604  O O   . ALA A 645 ? 0.1858 0.2108 0.2736 0.0238  -0.0291 0.0277  637 ALA A O   
4605  C CB  . ALA A 645 ? 0.1354 0.1562 0.2464 0.0303  -0.0094 0.0169  637 ALA A CB  
4606  N N   . ASP A 646 ? 0.1343 0.1667 0.2578 0.0291  -0.0329 0.0301  638 ASP A N   
4607  C CA  A ASP A 646 ? 0.1912 0.2227 0.3116 0.0285  -0.0434 0.0380  638 ASP A CA  
4608  C CA  C ASP A 646 ? 0.1930 0.2248 0.3141 0.0285  -0.0436 0.0381  638 ASP A CA  
4609  C C   . ASP A 646 ? 0.2216 0.2553 0.3258 0.0227  -0.0504 0.0396  638 ASP A C   
4610  O O   . ASP A 646 ? 0.1672 0.1962 0.2546 0.0199  -0.0547 0.0439  638 ASP A O   
4611  C CB  A ASP A 646 ? 0.2400 0.2764 0.3849 0.0325  -0.0501 0.0425  638 ASP A CB  
4612  C CB  C ASP A 646 ? 0.2424 0.2796 0.3884 0.0325  -0.0502 0.0424  638 ASP A CB  
4613  C CG  A ASP A 646 ? 0.2685 0.2995 0.4260 0.0383  -0.0449 0.0427  638 ASP A CG  
4614  C CG  C ASP A 646 ? 0.3217 0.3696 0.4824 0.0312  -0.0531 0.0401  638 ASP A CG  
4615  O OD1 A ASP A 646 ? 0.3237 0.3462 0.4680 0.0382  -0.0384 0.0411  638 ASP A OD1 
4616  O OD1 C ASP A 646 ? 0.4319 0.4837 0.5869 0.0269  -0.0629 0.0435  638 ASP A OD1 
4617  O OD2 A ASP A 646 ? 0.3274 0.3618 0.5052 0.0418  -0.0463 0.0435  638 ASP A OD2 
4618  O OD2 C ASP A 646 ? 0.4087 0.4607 0.5859 0.0337  -0.0453 0.0349  638 ASP A OD2 
4619  N N   A LEU A 647 ? 0.1508 0.1906 0.2588 0.0203  -0.0509 0.0358  639 LEU A N   
4620  N N   B LEU A 647 ? 0.1552 0.1948 0.2629 0.0204  -0.0504 0.0356  639 LEU A N   
4621  C CA  A LEU A 647 ? 0.1358 0.1766 0.2275 0.0143  -0.0567 0.0360  639 LEU A CA  
4622  C CA  B LEU A 647 ? 0.1440 0.1847 0.2360 0.0145  -0.0568 0.0362  639 LEU A CA  
4623  C C   A LEU A 647 ? 0.1486 0.1827 0.2165 0.0117  -0.0501 0.0321  639 LEU A C   
4624  C C   B LEU A 647 ? 0.1464 0.1807 0.2146 0.0117  -0.0501 0.0320  639 LEU A C   
4625  O O   A LEU A 647 ? 0.1660 0.1975 0.2158 0.0072  -0.0543 0.0338  639 LEU A O   
4626  O O   B LEU A 647 ? 0.1595 0.1914 0.2097 0.0071  -0.0544 0.0336  639 LEU A O   
4627  C CB  A LEU A 647 ? 0.1373 0.1855 0.2399 0.0121  -0.0579 0.0321  639 LEU A CB  
4628  C CB  B LEU A 647 ? 0.1498 0.1984 0.2542 0.0124  -0.0590 0.0331  639 LEU A CB  
4629  C CG  A LEU A 647 ? 0.1472 0.2041 0.2749 0.0141  -0.0664 0.0367  639 LEU A CG  
4630  C CG  B LEU A 647 ? 0.1783 0.2272 0.2670 0.0058  -0.0636 0.0312  639 LEU A CG  
4631  C CD1 A LEU A 647 ? 0.1907 0.2563 0.3318 0.0114  -0.0673 0.0329  639 LEU A CD1 
4632  C CD1 B LEU A 647 ? 0.2449 0.3029 0.3502 0.0035  -0.0728 0.0330  639 LEU A CD1 
4633  C CD2 A LEU A 647 ? 0.1553 0.2111 0.2757 0.0117  -0.0797 0.0449  639 LEU A CD2 
4634  C CD2 B LEU A 647 ? 0.2790 0.3245 0.3593 0.0051  -0.0529 0.0233  639 LEU A CD2 
4635  N N   . LEU A 648 ? 0.1346 0.1659 0.2023 0.0142  -0.0396 0.0266  640 LEU A N   
4636  C CA  . LEU A 648 ? 0.1445 0.1707 0.1930 0.0125  -0.0336 0.0229  640 LEU A CA  
4637  C C   . LEU A 648 ? 0.1620 0.1839 0.1990 0.0122  -0.0343 0.0272  640 LEU A C   
4638  O O   . LEU A 648 ? 0.1570 0.1767 0.1768 0.0088  -0.0339 0.0267  640 LEU A O   
4639  C CB  . LEU A 648 ? 0.1390 0.1628 0.1907 0.0152  -0.0237 0.0171  640 LEU A CB  
4640  C CG  . LEU A 648 ? 0.1567 0.1830 0.2156 0.0143  -0.0211 0.0121  640 LEU A CG  
4641  C CD1 . LEU A 648 ? 0.1490 0.1712 0.2096 0.0166  -0.0118 0.0075  640 LEU A CD1 
4642  C CD2 . LEU A 648 ? 0.1282 0.1539 0.1737 0.0099  -0.0233 0.0095  640 LEU A CD2 
4643  N N   . PHE A 649 ? 0.1257 0.1460 0.1722 0.0154  -0.0346 0.0312  641 PHE A N   
4644  C CA  . PHE A 649 ? 0.1862 0.2019 0.2223 0.0144  -0.0355 0.0358  641 PHE A CA  
4645  C C   . PHE A 649 ? 0.1591 0.1746 0.1835 0.0098  -0.0442 0.0414  641 PHE A C   
4646  O O   . PHE A 649 ? 0.2174 0.2298 0.2248 0.0062  -0.0429 0.0425  641 PHE A O   
4647  C CB  . PHE A 649 ? 0.1412 0.1539 0.1904 0.0185  -0.0354 0.0393  641 PHE A CB  
4648  C CG  . PHE A 649 ? 0.1695 0.1792 0.2219 0.0213  -0.0260 0.0344  641 PHE A CG  
4649  C CD1 . PHE A 649 ? 0.1447 0.1522 0.1840 0.0195  -0.0203 0.0316  641 PHE A CD1 
4650  C CD2 . PHE A 649 ? 0.1633 0.1723 0.2321 0.0254  -0.0231 0.0327  641 PHE A CD2 
4651  C CE1 . PHE A 649 ? 0.1611 0.1655 0.2026 0.0215  -0.0133 0.0277  641 PHE A CE1 
4652  C CE2 . PHE A 649 ? 0.1930 0.1977 0.2621 0.0270  -0.0149 0.0282  641 PHE A CE2 
4653  C CZ  . PHE A 649 ? 0.1754 0.1776 0.2304 0.0249  -0.0107 0.0260  641 PHE A CZ  
4654  N N   . LYS A 650 ? 0.1764 0.1953 0.2095 0.0093  -0.0532 0.0448  642 LYS A N   
4655  C CA  . LYS A 650 ? 0.1659 0.1837 0.1859 0.0039  -0.0628 0.0503  642 LYS A CA  
4656  C C   . LYS A 650 ? 0.2145 0.2320 0.2154 -0.0013 -0.0604 0.0452  642 LYS A C   
4657  O O   . LYS A 650 ? 0.2584 0.2717 0.2393 -0.0062 -0.0611 0.0470  642 LYS A O   
4658  C CB  . LYS A 650 ? 0.2061 0.2285 0.2421 0.0047  -0.0740 0.0552  642 LYS A CB  
4659  N N   . ALA A 651 ? 0.2034 0.2246 0.2099 -0.0006 -0.0567 0.0384  643 ALA A N   
4660  C CA  . ALA A 651 ? 0.2445 0.2642 0.2341 -0.0052 -0.0543 0.0329  643 ALA A CA  
4661  C C   . ALA A 651 ? 0.2483 0.2637 0.2221 -0.0057 -0.0450 0.0293  643 ALA A C   
4662  O O   . ALA A 651 ? 0.2357 0.2482 0.1910 -0.0104 -0.0440 0.0270  643 ALA A O   
4663  C CB  . ALA A 651 ? 0.2524 0.2755 0.2522 -0.0040 -0.0513 0.0264  643 ALA A CB  
4664  N N   . PHE A 652 ? 0.2229 0.2380 0.2039 -0.0012 -0.0379 0.0285  644 PHE A N   
4665  C CA  . PHE A 652 ? 0.2380 0.2508 0.2078 -0.0012 -0.0291 0.0250  644 PHE A CA  
4666  C C   . PHE A 652 ? 0.2570 0.2676 0.2189 -0.0032 -0.0293 0.0305  644 PHE A C   
4667  O O   . PHE A 652 ? 0.2403 0.2505 0.1974 -0.0028 -0.0219 0.0284  644 PHE A O   
4668  C CB  . PHE A 652 ? 0.1500 0.1636 0.1308 0.0039  -0.0215 0.0202  644 PHE A CB  
4669  C CG  . PHE A 652 ? 0.1462 0.1601 0.1284 0.0046  -0.0188 0.0136  644 PHE A CG  
4670  C CD1 . PHE A 652 ? 0.2428 0.2546 0.2119 0.0026  -0.0149 0.0085  644 PHE A CD1 
4671  C CD2 . PHE A 652 ? 0.2166 0.2321 0.2130 0.0069  -0.0197 0.0125  644 PHE A CD2 
4672  C CE1 . PHE A 652 ? 0.2524 0.2626 0.2222 0.0030  -0.0127 0.0028  644 PHE A CE1 
4673  C CE2 . PHE A 652 ? 0.1651 0.1797 0.1617 0.0067  -0.0172 0.0069  644 PHE A CE2 
4674  C CZ  . PHE A 652 ? 0.2012 0.2127 0.1844 0.0047  -0.0142 0.0023  644 PHE A CZ  
4675  N N   . GLY A 653 ? 0.2430 0.2520 0.2037 -0.0056 -0.0379 0.0379  645 GLY A N   
4676  C CA  . GLY A 653 ? 0.2370 0.2422 0.1861 -0.0092 -0.0388 0.0437  645 GLY A CA  
4677  C C   . GLY A 653 ? 0.2313 0.2350 0.1907 -0.0059 -0.0369 0.0475  645 GLY A C   
4678  O O   . GLY A 653 ? 0.2365 0.2370 0.1861 -0.0092 -0.0354 0.0514  645 GLY A O   
4679  N N   . PHE A 654 ? 0.1673 0.1726 0.1454 -0.0001 -0.0363 0.0462  646 PHE A N   
4680  C CA  . PHE A 654 ? 0.1920 0.1941 0.1794 0.0028  -0.0351 0.0497  646 PHE A CA  
4681  C C   . PHE A 654 ? 0.2556 0.2544 0.2497 0.0032  -0.0451 0.0578  646 PHE A C   
4682  O O   . PHE A 654 ? 0.2301 0.2296 0.2420 0.0081  -0.0478 0.0584  646 PHE A O   
4683  C CB  . PHE A 654 ? 0.1999 0.2037 0.2015 0.0081  -0.0288 0.0439  646 PHE A CB  
4684  C CG  . PHE A 654 ? 0.1603 0.1664 0.1554 0.0078  -0.0205 0.0372  646 PHE A CG  
4685  C CD1 . PHE A 654 ? 0.1680 0.1731 0.1574 0.0063  -0.0153 0.0373  646 PHE A CD1 
4686  C CD2 . PHE A 654 ? 0.1684 0.1778 0.1632 0.0086  -0.0184 0.0313  646 PHE A CD2 
4687  C CE1 . PHE A 654 ? 0.1422 0.1504 0.1279 0.0064  -0.0085 0.0316  646 PHE A CE1 
4688  C CE2 . PHE A 654 ? 0.1504 0.1611 0.1399 0.0088  -0.0114 0.0257  646 PHE A CE2 
4689  C CZ  . PHE A 654 ? 0.1709 0.1815 0.1566 0.0080  -0.0067 0.0259  646 PHE A CZ  
4690  N N   . THR A 655 ? 0.2276 0.2226 0.2067 -0.0022 -0.0505 0.0640  647 THR A N   
4691  C CA  . THR A 655 ? 0.1993 0.1900 0.1807 -0.0029 -0.0618 0.0731  647 THR A CA  
4692  C C   . THR A 655 ? 0.2823 0.2651 0.2508 -0.0073 -0.0625 0.0799  647 THR A C   
4693  O O   . THR A 655 ? 0.2724 0.2546 0.2263 -0.0116 -0.0550 0.0777  647 THR A O   
4694  C CB  . THR A 655 ? 0.3213 0.3139 0.2938 -0.0071 -0.0706 0.0752  647 THR A CB  
4695  O OG1 . THR A 655 ? 0.3316 0.3214 0.2789 -0.0145 -0.0680 0.0748  647 THR A OG1 
4696  C CG2 . THR A 655 ? 0.3422 0.3424 0.3252 -0.0043 -0.0691 0.0678  647 THR A CG2 
4697  N N   . VAL A 656 ? 0.2700 0.2467 0.2448 -0.0061 -0.0715 0.0885  648 VAL A N   
4698  C CA  . VAL A 656 ? 0.3150 0.2823 0.2765 -0.0109 -0.0733 0.0962  648 VAL A CA  
4699  C C   . VAL A 656 ? 0.3205 0.2860 0.2555 -0.0201 -0.0748 0.0987  648 VAL A C   
4700  O O   . VAL A 656 ? 0.3072 0.2693 0.2269 -0.0256 -0.0683 0.0993  648 VAL A O   
4701  C CB  . VAL A 656 ? 0.3483 0.3084 0.3219 -0.0076 -0.0835 0.1046  648 VAL A CB  
4702  C CG1 . VAL A 656 ? 0.2975 0.2478 0.2559 -0.0134 -0.0842 0.1103  648 VAL A CG1 
4703  C CG2 . VAL A 656 ? 0.3999 0.3603 0.3977 0.0009  -0.0798 0.1015  648 VAL A CG2 
4704  N N   . ASP A 657 ? 0.3521 0.3198 0.2810 -0.0223 -0.0827 0.0997  649 ASP A N   
4705  C CA  . ASP A 657 ? 0.3808 0.3453 0.2830 -0.0315 -0.0837 0.1010  649 ASP A CA  
4706  C C   . ASP A 657 ? 0.3106 0.2790 0.1992 -0.0350 -0.0703 0.0929  649 ASP A C   
4707  O O   . ASP A 657 ? 0.3519 0.3159 0.2191 -0.0426 -0.0661 0.0947  649 ASP A O   
4708  C CB  . ASP A 657 ? 0.4117 0.3790 0.3125 -0.0328 -0.0927 0.1002  649 ASP A CB  
4709  C CG  . ASP A 657 ? 0.5069 0.4703 0.4176 -0.0313 -0.1043 0.1067  649 ASP A CG  
4710  O OD1 . ASP A 657 ? 0.5016 0.4588 0.4175 -0.0298 -0.1054 0.1119  649 ASP A OD1 
4711  O OD2 . ASP A 657 ? 0.5311 0.4977 0.4448 -0.0319 -0.1124 0.1065  649 ASP A OD2 
4712  N N   . ASN A 658 ? 0.2705 0.2473 0.1724 -0.0294 -0.0625 0.0833  650 ASN A N   
4713  C CA  . ASN A 658 ? 0.3659 0.3470 0.2583 -0.0315 -0.0499 0.0748  650 ASN A CA  
4714  C C   . ASN A 658 ? 0.3076 0.2880 0.2005 -0.0322 -0.0410 0.0751  650 ASN A C   
4715  O O   . ASN A 658 ? 0.2897 0.2705 0.1674 -0.0377 -0.0329 0.0729  650 ASN A O   
4716  C CB  . ASN A 658 ? 0.3166 0.3055 0.2231 -0.0254 -0.0450 0.0653  650 ASN A CB  
4717  C CG  . ASN A 658 ? 0.3718 0.3643 0.2681 -0.0273 -0.0336 0.0567  650 ASN A CG  
4718  O OD1 . ASN A 658 ? 0.3543 0.3442 0.2301 -0.0341 -0.0313 0.0566  650 ASN A OD1 
4719  N ND2 . ASN A 658 ? 0.2486 0.2467 0.1588 -0.0214 -0.0263 0.0496  650 ASN A ND2 
4720  N N   . VAL A 659 ? 0.2377 0.2172 0.1482 -0.0268 -0.0417 0.0772  651 VAL A N   
4721  C CA  . VAL A 659 ? 0.2524 0.2305 0.1634 -0.0283 -0.0346 0.0781  651 VAL A CA  
4722  C C   . VAL A 659 ? 0.2587 0.2289 0.1508 -0.0368 -0.0369 0.0864  651 VAL A C   
4723  O O   . VAL A 659 ? 0.3127 0.2842 0.1951 -0.0421 -0.0284 0.0852  651 VAL A O   
4724  C CB  . VAL A 659 ? 0.2861 0.2622 0.2176 -0.0217 -0.0360 0.0791  651 VAL A CB  
4725  C CG1 . VAL A 659 ? 0.2619 0.2357 0.1929 -0.0244 -0.0296 0.0803  651 VAL A CG1 
4726  C CG2 . VAL A 659 ? 0.2369 0.2201 0.1844 -0.0145 -0.0325 0.0707  651 VAL A CG2 
4727  N N   . VAL A 660 ? 0.2851 0.2475 0.1720 -0.0386 -0.0487 0.0950  652 VAL A N   
4728  C CA  . VAL A 660 ? 0.3440 0.2970 0.2119 -0.0469 -0.0519 0.1035  652 VAL A CA  
4729  C C   . VAL A 660 ? 0.3447 0.2996 0.1900 -0.0548 -0.0452 0.0994  652 VAL A C   
4730  O O   . VAL A 660 ? 0.3313 0.2840 0.1649 -0.0610 -0.0382 0.0999  652 VAL A O   
4731  C CB  . VAL A 660 ? 0.3583 0.3043 0.2309 -0.0448 -0.0650 0.1097  652 VAL A CB  
4732  C CG1 . VAL A 660 ? 0.3693 0.3073 0.2226 -0.0528 -0.0670 0.1142  652 VAL A CG1 
4733  C CG2 . VAL A 660 ? 0.3321 0.2744 0.2265 -0.0376 -0.0691 0.1131  652 VAL A CG2 
4734  N N   . ASP A 661 ? 0.3398 0.2988 0.1793 -0.0547 -0.0469 0.0949  653 ASP A N   
4735  C CA  . ASP A 661 ? 0.4028 0.3627 0.2214 -0.0616 -0.0397 0.0895  653 ASP A CA  
4736  C C   . ASP A 661 ? 0.3294 0.2966 0.1468 -0.0628 -0.0246 0.0828  653 ASP A C   
4737  O O   . ASP A 661 ? 0.3577 0.3246 0.1615 -0.0689 -0.0159 0.0800  653 ASP A O   
4738  C CB  . ASP A 661 ? 0.4425 0.4046 0.2565 -0.0609 -0.0443 0.0850  653 ASP A CB  
4739  C CG  . ASP A 661 ? 0.5551 0.5117 0.3711 -0.0605 -0.0592 0.0912  653 ASP A CG  
4740  O OD1 . ASP A 661 ? 0.5408 0.4904 0.3555 -0.0624 -0.0649 0.0984  653 ASP A OD1 
4741  O OD2 . ASP A 661 ? 0.5633 0.5230 0.3831 -0.0583 -0.0651 0.0885  653 ASP A OD2 
4742  N N   . THR A 662 ? 0.3155 0.2910 0.1553 -0.0544 -0.0201 0.0765  654 THR A N   
4743  C CA  . THR A 662 ? 0.3127 0.2967 0.1582 -0.0534 -0.0064 0.0686  654 THR A CA  
4744  C C   . THR A 662 ? 0.3264 0.3089 0.1697 -0.0584 -0.0012 0.0733  654 THR A C   
4745  O O   . THR A 662 ? 0.3545 0.3418 0.1905 -0.0632 0.0099  0.0694  654 THR A O   
4746  C CB  . THR A 662 ? 0.2604 0.2519 0.1301 -0.0434 -0.0047 0.0621  654 THR A CB  
4747  O OG1 . THR A 662 ? 0.3214 0.3141 0.1923 -0.0397 -0.0088 0.0576  654 THR A OG1 
4748  C CG2 . THR A 662 ? 0.2691 0.2695 0.1461 -0.0421 0.0078  0.0547  654 THR A CG2 
4749  N N   . VAL A 663 ? 0.3034 0.2795 0.1542 -0.0574 -0.0087 0.0812  655 VAL A N   
4750  C CA  . VAL A 663 ? 0.3057 0.2782 0.1527 -0.0634 -0.0050 0.0868  655 VAL A CA  
4751  C C   . VAL A 663 ? 0.3518 0.3194 0.1767 -0.0724 -0.0024 0.0888  655 VAL A C   
4752  O O   . VAL A 663 ? 0.3334 0.3047 0.1543 -0.0775 0.0079  0.0863  655 VAL A O   
4753  C CB  . VAL A 663 ? 0.3438 0.3072 0.2010 -0.0606 -0.0148 0.0950  655 VAL A CB  
4754  C CG1 . VAL A 663 ? 0.3093 0.2661 0.1599 -0.0674 -0.0126 0.1007  655 VAL A CG1 
4755  C CG2 . VAL A 663 ? 0.3025 0.2716 0.1847 -0.0511 -0.0136 0.0896  655 VAL A CG2 
4756  N N   . LYS A 664 ? 0.3813 0.3411 0.1947 -0.0736 -0.0118 0.0920  656 LYS A N   
4757  C CA  . LYS A 664 ? 0.4128 0.3672 0.2064 -0.0815 -0.0100 0.0930  656 LYS A CA  
4758  C C   . LYS A 664 ? 0.4341 0.3962 0.2185 -0.0849 0.0033  0.0838  656 LYS A C   
4759  O O   . LYS A 664 ? 0.4006 0.3609 0.1726 -0.0917 0.0101  0.0834  656 LYS A O   
4760  C CB  . LYS A 664 ? 0.4034 0.3496 0.1872 -0.0821 -0.0227 0.0971  656 LYS A CB  
4761  C CG  . LYS A 664 ? 0.5077 0.4450 0.2990 -0.0798 -0.0357 0.1064  656 LYS A CG  
4762  C CD  . LYS A 664 ? 0.5847 0.5153 0.3654 -0.0818 -0.0473 0.1100  656 LYS A CD  
4763  C CE  . LYS A 664 ? 0.6516 0.5770 0.4470 -0.0761 -0.0611 0.1173  656 LYS A CE  
4764  N NZ  . LYS A 664 ? 0.6259 0.5460 0.4128 -0.0783 -0.0731 0.1209  656 LYS A NZ  
4765  N N   . SER A 665 ? 0.4199 0.3902 0.2106 -0.0801 0.0074  0.0763  657 SER A N   
4766  C CA  . SER A 665 ? 0.4831 0.4598 0.2663 -0.0820 0.0197  0.0667  657 SER A CA  
4767  C C   . SER A 665 ? 0.4573 0.4428 0.2487 -0.0834 0.0336  0.0627  657 SER A C   
4768  O O   . SER A 665 ? 0.4144 0.4041 0.1995 -0.0860 0.0444  0.0557  657 SER A O   
4769  C CB  . SER A 665 ? 0.4556 0.4379 0.2446 -0.0760 0.0201  0.0595  657 SER A CB  
4770  O OG  . SER A 665 ? 0.3585 0.3500 0.1667 -0.0702 0.0243  0.0571  657 SER A OG  
4771  N N   . VAL A 666 ? 0.4115 0.4003 0.2180 -0.0817 0.0336  0.0666  658 VAL A N   
4772  C CA  . VAL A 666 ? 0.3575 0.3555 0.1738 -0.0836 0.0457  0.0633  658 VAL A CA  
4773  C C   . VAL A 666 ? 0.4680 0.4597 0.2783 -0.0906 0.0453  0.0703  658 VAL A C   
4774  O O   . VAL A 666 ? 0.4385 0.4372 0.2591 -0.0926 0.0533  0.0694  658 VAL A O   
4775  C CB  . VAL A 666 ? 0.3439 0.3518 0.1824 -0.0777 0.0476  0.0613  658 VAL A CB  
4776  C CG1 . VAL A 666 ? 0.3421 0.3552 0.1867 -0.0703 0.0474  0.0540  658 VAL A CG1 
4777  C CG2 . VAL A 666 ? 0.3610 0.3615 0.2063 -0.0766 0.0368  0.0704  658 VAL A CG2 
4778  N N   . LEU A 667 ? 0.4954 0.4743 0.2900 -0.0944 0.0360  0.0772  659 LEU A N   
4779  C CA  . LEU A 667 ? 0.6166 0.5877 0.4030 -0.1014 0.0350  0.0839  659 LEU A CA  
4780  C C   . LEU A 667 ? 0.7308 0.6993 0.4973 -0.1087 0.0412  0.0815  659 LEU A C   
4781  O O   . LEU A 667 ? 0.7308 0.6991 0.4871 -0.1081 0.0415  0.0767  659 LEU A O   
4782  C CB  . LEU A 667 ? 0.5560 0.5139 0.3395 -0.1007 0.0199  0.0937  659 LEU A CB  
4783  C CG  . LEU A 667 ? 0.5171 0.4745 0.3194 -0.0938 0.0128  0.0971  659 LEU A CG  
4784  C CD1 . LEU A 667 ? 0.5754 0.5192 0.3749 -0.0928 -0.0014 0.1062  659 LEU A CD1 
4785  C CD2 . LEU A 667 ? 0.5611 0.5244 0.3769 -0.0950 0.0205  0.0966  659 LEU A CD2 
4786  O OXT . LEU A 667 ? 0.7787 0.7447 0.5385 -0.1156 0.0460  0.0842  659 LEU A OXT 
4787  N N   . SER B 10  ? 0.4104 0.5922 0.6234 0.0080  0.0934  0.0979  2   SER B N   
4788  C CA  . SER B 10  ? 0.4350 0.6146 0.6617 0.0006  0.0844  0.0996  2   SER B CA  
4789  C C   . SER B 10  ? 0.3891 0.5656 0.6201 0.0008  0.0753  0.0929  2   SER B C   
4790  O O   . SER B 10  ? 0.2278 0.3988 0.4472 0.0048  0.0739  0.0871  2   SER B O   
4791  C CB  . SER B 10  ? 0.4940 0.6647 0.7134 -0.0041 0.0818  0.1027  2   SER B CB  
4792  O OG  . SER B 10  ? 0.5409 0.7076 0.7715 -0.0104 0.0721  0.1029  2   SER B OG  
4793  N N   . GLN B 11  ? 0.3353 0.5150 0.5829 -0.0035 0.0689  0.0938  3   GLN B N   
4794  C CA  . GLN B 11  ? 0.2912 0.4678 0.5425 -0.0031 0.0602  0.0878  3   GLN B CA  
4795  C C   . GLN B 11  ? 0.1940 0.3590 0.4368 -0.0058 0.0528  0.0845  3   GLN B C   
4796  O O   . GLN B 11  ? 0.1245 0.2851 0.3624 -0.0033 0.0482  0.0785  3   GLN B O   
4797  C CB  . GLN B 11  ? 0.3658 0.5483 0.6364 -0.0070 0.0547  0.0898  3   GLN B CB  
4798  C CG  . GLN B 11  ? 0.4071 0.6022 0.6881 -0.0037 0.0613  0.0921  3   GLN B CG  
4799  C CD  . GLN B 11  ? 0.4732 0.6709 0.7493 0.0037  0.0633  0.0863  3   GLN B CD  
4800  O OE1 . GLN B 11  ? 0.4694 0.6649 0.7309 0.0091  0.0695  0.0838  3   GLN B OE1 
4801  N NE2 . GLN B 11  ? 0.5354 0.7372 0.8236 0.0042  0.0574  0.0840  3   GLN B NE2 
4802  N N   . LEU B 12  ? 0.1845 0.3443 0.4254 -0.0106 0.0518  0.0884  4   LEU B N   
4803  C CA  . LEU B 12  ? 0.2209 0.3698 0.4546 -0.0131 0.0451  0.0854  4   LEU B CA  
4804  C C   . LEU B 12  ? 0.1887 0.3331 0.4059 -0.0082 0.0483  0.0812  4   LEU B C   
4805  O O   . LEU B 12  ? 0.1882 0.3254 0.4003 -0.0082 0.0425  0.0764  4   LEU B O   
4806  C CB  . LEU B 12  ? 0.2371 0.3815 0.4729 -0.0189 0.0437  0.0909  4   LEU B CB  
4807  C CG  . LEU B 12  ? 0.3594 0.5091 0.6118 -0.0237 0.0418  0.0960  4   LEU B CG  
4808  C CD1 . LEU B 12  ? 0.3897 0.5344 0.6436 -0.0292 0.0408  0.1018  4   LEU B CD1 
4809  C CD2 . LEU B 12  ? 0.3868 0.5352 0.6495 -0.0257 0.0321  0.0921  4   LEU B CD2 
4810  N N   . ALA B 13  ? 0.1565 0.3048 0.3651 -0.0037 0.0574  0.0828  5   ALA B N   
4811  C CA  . ALA B 13  ? 0.1682 0.3125 0.3615 0.0015  0.0603  0.0785  5   ALA B CA  
4812  C C   . ALA B 13  ? 0.1910 0.3381 0.3831 0.0073  0.0607  0.0728  5   ALA B C   
4813  O O   . ALA B 13  ? 0.1094 0.2511 0.2930 0.0101  0.0584  0.0675  5   ALA B O   
4814  C CB  . ALA B 13  ? 0.1461 0.2916 0.3282 0.0042  0.0692  0.0825  5   ALA B CB  
4815  N N   . ASN B 14  ? 0.1390 0.2944 0.3402 0.0091  0.0636  0.0740  6   ASN B N   
4816  C CA  . ASN B 14  ? 0.1234 0.2813 0.3236 0.0150  0.0642  0.0688  6   ASN B CA  
4817  C C   . ASN B 14  ? 0.1396 0.2931 0.3440 0.0139  0.0549  0.0640  6   ASN B C   
4818  O O   . ASN B 14  ? 0.1396 0.2910 0.3385 0.0188  0.0542  0.0590  6   ASN B O   
4819  C CB  . ASN B 14  ? 0.1212 0.2897 0.3320 0.0171  0.0691  0.0713  6   ASN B CB  
4820  C CG  . ASN B 14  ? 0.1515 0.3237 0.3538 0.0212  0.0796  0.0741  6   ASN B CG  
4821  O OD1 . ASN B 14  ? 0.1712 0.3376 0.3583 0.0232  0.0828  0.0734  6   ASN B OD1 
4822  N ND2 . ASN B 14  ? 0.1482 0.3302 0.3602 0.0225  0.0850  0.0773  6   ASN B ND2 
4823  N N   . VAL B 15  ? 0.1017 0.2529 0.3152 0.0077  0.0476  0.0656  7   VAL B N   
4824  C CA  . VAL B 15  ? 0.0950 0.2410 0.3106 0.0068  0.0387  0.0610  7   VAL B CA  
4825  C C   . VAL B 15  ? 0.1524 0.2898 0.3544 0.0087  0.0376  0.0567  7   VAL B C   
4826  O O   . VAL B 15  ? 0.0967 0.2306 0.2961 0.0112  0.0336  0.0520  7   VAL B O   
4827  C CB  . VAL B 15  ? 0.1141 0.2581 0.3406 -0.0001 0.0309  0.0633  7   VAL B CB  
4828  C CG1 . VAL B 15  ? 0.1227 0.2601 0.3441 -0.0047 0.0303  0.0656  7   VAL B CG1 
4829  C CG2 . VAL B 15  ? 0.1364 0.2758 0.3653 -0.0004 0.0218  0.0587  7   VAL B CG2 
4830  N N   . ILE B 16  ? 0.1310 0.2649 0.3244 0.0076  0.0411  0.0583  8   ILE B N   
4831  C CA  . ILE B 16  ? 0.0861 0.2129 0.2673 0.0098  0.0408  0.0544  8   ILE B CA  
4832  C C   . ILE B 16  ? 0.0883 0.2153 0.2601 0.0168  0.0452  0.0505  8   ILE B C   
4833  O O   . ILE B 16  ? 0.0869 0.2054 0.2486 0.0188  0.0414  0.0447  8   ILE B O   
4834  C CB  . ILE B 16  ? 0.0990 0.2210 0.2713 0.0074  0.0431  0.0568  8   ILE B CB  
4835  C CG1 . ILE B 16  ? 0.1257 0.2446 0.3058 0.0007  0.0373  0.0596  8   ILE B CG1 
4836  C CG2 . ILE B 16  ? 0.0913 0.2023 0.2448 0.0101  0.0419  0.0510  8   ILE B CG2 
4837  C CD1 . ILE B 16  ? 0.1520 0.2675 0.3264 -0.0019 0.0397  0.0637  8   ILE B CD1 
4838  N N   . ARG B 17  ? 0.1087 0.2427 0.2805 0.0204  0.0526  0.0529  9   ARG B N   
4839  C CA  . ARG B 17  ? 0.1754 0.3093 0.3386 0.0277  0.0571  0.0491  9   ARG B CA  
4840  C C   . ARG B 17  ? 0.0949 0.2283 0.2632 0.0302  0.0523  0.0451  9   ARG B C   
4841  O O   . ARG B 17  ? 0.1232 0.2493 0.2812 0.0339  0.0507  0.0399  9   ARG B O   
4842  C CB  . ARG B 17  ? 0.1080 0.2488 0.2702 0.0311  0.0654  0.0521  9   ARG B CB  
4843  C CG  . ARG B 17  ? 0.1134 0.2542 0.2687 0.0293  0.0706  0.0566  9   ARG B CG  
4844  C CD  . ARG B 17  ? 0.2125 0.3591 0.3638 0.0338  0.0797  0.0591  9   ARG B CD  
4845  N NE  . ARG B 17  ? 0.1698 0.3129 0.3073 0.0345  0.0846  0.0616  9   ARG B NE  
4846  C CZ  . ARG B 17  ? 0.1975 0.3423 0.3369 0.0299  0.0867  0.0680  9   ARG B CZ  
4847  N NH1 . ARG B 17  ? 0.1667 0.3166 0.3218 0.0242  0.0844  0.0724  9   ARG B NH1 
4848  N NH2 . ARG B 17  ? 0.2287 0.3693 0.3537 0.0312  0.0908  0.0701  9   ARG B NH2 
4849  N N   . PHE B 18  ? 0.0942 0.2329 0.2761 0.0276  0.0487  0.0469  10  PHE B N   
4850  C CA  . PHE B 18  ? 0.1293 0.2681 0.3162 0.0306  0.0441  0.0435  10  PHE B CA  
4851  C C   . PHE B 18  ? 0.0926 0.2235 0.2782 0.0283  0.0360  0.0407  10  PHE B C   
4852  O O   . PHE B 18  ? 0.0864 0.2114 0.2658 0.0319  0.0331  0.0364  10  PHE B O   
4853  C CB  . PHE B 18  ? 0.0956 0.2434 0.2975 0.0293  0.0431  0.0465  10  PHE B CB  
4854  C CG  . PHE B 18  ? 0.1375 0.2932 0.3404 0.0337  0.0516  0.0480  10  PHE B CG  
4855  C CD1 . PHE B 18  ? 0.1076 0.2635 0.3057 0.0412  0.0547  0.0442  10  PHE B CD1 
4856  C CD2 . PHE B 18  ? 0.1405 0.3025 0.3480 0.0308  0.0569  0.0533  10  PHE B CD2 
4857  C CE1 . PHE B 18  ? 0.1230 0.2857 0.3210 0.0458  0.0628  0.0452  10  PHE B CE1 
4858  C CE2 . PHE B 18  ? 0.1405 0.3095 0.3479 0.0352  0.0654  0.0548  10  PHE B CE2 
4859  C CZ  . PHE B 18  ? 0.1321 0.3016 0.3347 0.0428  0.0684  0.0505  10  PHE B CZ  
4860  N N   . LEU B 19  ? 0.0822 0.2102 0.2703 0.0220  0.0315  0.0424  11  LEU B N   
4861  C CA  . LEU B 19  ? 0.1118 0.2273 0.2900 0.0195  0.0240  0.0380  11  LEU B CA  
4862  C C   . LEU B 19  ? 0.0978 0.2034 0.2578 0.0224  0.0258  0.0333  11  LEU B C   
4863  O O   . LEU B 19  ? 0.1043 0.2018 0.2567 0.0236  0.0217  0.0293  11  LEU B O   
4864  C CB  . LEU B 19  ? 0.1214 0.2336 0.3015 0.0130  0.0202  0.0398  11  LEU B CB  
4865  C CG  . LEU B 19  ? 0.1665 0.2825 0.3618 0.0087  0.0137  0.0424  11  LEU B CG  
4866  C CD1 . LEU B 19  ? 0.1761 0.2860 0.3697 0.0029  0.0103  0.0433  11  LEU B CD1 
4867  C CD2 . LEU B 19  ? 0.1642 0.2751 0.3585 0.0101  0.0062  0.0386  11  LEU B CD2 
4868  N N   . SER B 20  ? 0.1035 0.2093 0.2561 0.0233  0.0317  0.0341  12  SER B N   
4869  C CA  . SER B 20  ? 0.0864 0.1826 0.2227 0.0254  0.0325  0.0297  12  SER B CA  
4870  C C   . SER B 20  ? 0.1034 0.1985 0.2352 0.0315  0.0342  0.0265  12  SER B C   
4871  O O   . SER B 20  ? 0.1367 0.2228 0.2599 0.0324  0.0308  0.0223  12  SER B O   
4872  C CB  . SER B 20  ? 0.0945 0.1908 0.2240 0.0250  0.0372  0.0315  12  SER B CB  
4873  O OG  . SER B 20  ? 0.0987 0.1944 0.2318 0.0195  0.0349  0.0343  12  SER B OG  
4874  N N   . ALA B 21  ? 0.0938 0.1978 0.2315 0.0359  0.0398  0.0285  13  ALA B N   
4875  C CA  . ALA B 21  ? 0.1359 0.2384 0.2696 0.0424  0.0415  0.0252  13  ALA B CA  
4876  C C   . ALA B 21  ? 0.0971 0.1969 0.2360 0.0429  0.0352  0.0234  13  ALA B C   
4877  O O   . ALA B 21  ? 0.1025 0.1936 0.2324 0.0458  0.0330  0.0193  13  ALA B O   
4878  C CB  . ALA B 21  ? 0.1036 0.2173 0.2443 0.0475  0.0492  0.0280  13  ALA B CB  
4879  N N   . ASP B 22  ? 0.1072 0.2137 0.2603 0.0399  0.0317  0.0266  14  ASP B N   
4880  C CA  . ASP B 22  ? 0.1238 0.2276 0.2812 0.0407  0.0251  0.0251  14  ASP B CA  
4881  C C   . ASP B 22  ? 0.0926 0.1827 0.2372 0.0377  0.0193  0.0217  14  ASP B C   
4882  O O   . ASP B 22  ? 0.1065 0.1898 0.2462 0.0402  0.0157  0.0192  14  ASP B O   
4883  C CB  . ASP B 22  ? 0.0894 0.2026 0.2645 0.0377  0.0214  0.0291  14  ASP B CB  
4884  C CG  . ASP B 22  ? 0.0971 0.2253 0.2882 0.0412  0.0270  0.0329  14  ASP B CG  
4885  O OD1 . ASP B 22  ? 0.1308 0.2607 0.3185 0.0475  0.0322  0.0313  14  ASP B OD1 
4886  O OD2 . ASP B 22  ? 0.1397 0.2748 0.3420 0.0366  0.0256  0.0364  14  ASP B OD2 
4887  N N   . ALA B 23  ? 0.0923 0.1785 0.2319 0.0325  0.0184  0.0220  15  ALA B N   
4888  C CA  . ALA B 23  ? 0.1112 0.1857 0.2398 0.0298  0.0138  0.0190  15  ALA B CA  
4889  C C   . ALA B 23  ? 0.1275 0.1935 0.2428 0.0323  0.0159  0.0155  15  ALA B C   
4890  O O   . ALA B 23  ? 0.1087 0.1659 0.2168 0.0326  0.0125  0.0133  15  ALA B O   
4891  C CB  . ALA B 23  ? 0.0890 0.1618 0.2165 0.0242  0.0126  0.0200  15  ALA B CB  
4892  N N   . VAL B 24  ? 0.1153 0.1833 0.2269 0.0341  0.0212  0.0152  16  VAL B N   
4893  C CA  . VAL B 24  ? 0.1148 0.1749 0.2148 0.0368  0.0226  0.0117  16  VAL B CA  
4894  C C   . VAL B 24  ? 0.1760 0.2337 0.2760 0.0419  0.0215  0.0100  16  VAL B C   
4895  O O   . VAL B 24  ? 0.1681 0.2159 0.2597 0.0425  0.0190  0.0073  16  VAL B O   
4896  C CB  . VAL B 24  ? 0.1274 0.1904 0.2233 0.0386  0.0279  0.0117  16  VAL B CB  
4897  C CG1 . VAL B 24  ? 0.1428 0.1977 0.2274 0.0425  0.0287  0.0076  16  VAL B CG1 
4898  C CG2 . VAL B 24  ? 0.1256 0.1880 0.2192 0.0336  0.0278  0.0129  16  VAL B CG2 
4899  N N   . GLN B 25  ? 0.1053 0.1720 0.2155 0.0457  0.0233  0.0119  17  GLN B N   
4900  C CA  . GLN B 25  ? 0.1112 0.1758 0.2221 0.0514  0.0222  0.0102  17  GLN B CA  
4901  C C   . GLN B 25  ? 0.1253 0.1826 0.2353 0.0497  0.0154  0.0098  17  GLN B C   
4902  O O   . GLN B 25  ? 0.1182 0.1662 0.2209 0.0524  0.0133  0.0074  17  GLN B O   
4903  C CB  . GLN B 25  ? 0.1116 0.1889 0.2359 0.0559  0.0256  0.0126  17  GLN B CB  
4904  C CG  . GLN B 25  ? 0.1196 0.1948 0.2429 0.0636  0.0267  0.0101  17  GLN B CG  
4905  C CD  . GLN B 25  ? 0.1984 0.2662 0.3079 0.0672  0.0307  0.0063  17  GLN B CD  
4906  O OE1 . GLN B 25  ? 0.1762 0.2470 0.2817 0.0665  0.0357  0.0066  17  GLN B OE1 
4907  N NE2 . GLN B 25  ? 0.2186 0.2757 0.3203 0.0710  0.0281  0.0027  17  GLN B NE2 
4908  N N   . LYS B 26  ? 0.1265 0.1869 0.2429 0.0454  0.0116  0.0122  18  LYS B N   
4909  C CA  . LYS B 26  ? 0.1460 0.1988 0.2595 0.0440  0.0050  0.0120  18  LYS B CA  
4910  C C   . LYS B 26  ? 0.1674 0.2072 0.2663 0.0415  0.0040  0.0097  18  LYS B C   
4911  O O   . LYS B 26  ? 0.1398 0.1706 0.2324 0.0428  0.0006  0.0089  18  LYS B O   
4912  C CB  . LYS B 26  ? 0.1285 0.1859 0.2499 0.0397  0.0009  0.0145  18  LYS B CB  
4913  C CG  . LYS B 26  ? 0.1590 0.2083 0.2761 0.0386  -0.0064 0.0143  18  LYS B CG  
4914  C CD  . LYS B 26  ? 0.1460 0.2010 0.2731 0.0356  -0.0115 0.0165  18  LYS B CD  
4915  C CE  . LYS B 26  ? 0.1736 0.2200 0.2954 0.0355  -0.0196 0.0162  18  LYS B CE  
4916  N NZ  . LYS B 26  ? 0.1630 0.1963 0.2676 0.0329  -0.0199 0.0144  18  LYS B NZ  
4917  N N   . ALA B 27  ? 0.1357 0.1745 0.2295 0.0380  0.0071  0.0090  19  ALA B N   
4918  C CA  . ALA B 27  ? 0.1410 0.1692 0.2233 0.0355  0.0069  0.0070  19  ALA B CA  
4919  C C   . ALA B 27  ? 0.1455 0.1677 0.2215 0.0390  0.0086  0.0046  19  ALA B C   
4920  O O   . ALA B 27  ? 0.1454 0.1580 0.2130 0.0372  0.0076  0.0033  19  ALA B O   
4921  C CB  . ALA B 27  ? 0.1061 0.1359 0.1866 0.0311  0.0093  0.0070  19  ALA B CB  
4922  N N   . ASN B 28  ? 0.1332 0.1606 0.2131 0.0440  0.0112  0.0040  20  ASN B N   
4923  C CA  . ASN B 28  ? 0.1693 0.1911 0.2424 0.0478  0.0132  0.0010  20  ASN B CA  
4924  C C   . ASN B 28  ? 0.2016 0.2185 0.2669 0.0439  0.0143  -0.0007 20  ASN B C   
4925  O O   . ASN B 28  ? 0.1589 0.1661 0.2166 0.0440  0.0131  -0.0031 20  ASN B O   
4926  C CB  . ASN B 28  ? 0.3049 0.3167 0.3736 0.0507  0.0097  -0.0003 20  ASN B CB  
4927  C CG  . ASN B 28  ? 0.3555 0.3617 0.4185 0.0558  0.0113  -0.0038 20  ASN B CG  
4928  O OD1 . ASN B 28  ? 0.3155 0.3280 0.3799 0.0594  0.0154  -0.0049 20  ASN B OD1 
4929  N ND2 . ASN B 28  ? 0.3388 0.3325 0.3947 0.0562  0.0081  -0.0054 20  ASN B ND2 
4930  N N   . SER B 29  ? 0.1415 0.1649 0.2095 0.0404  0.0162  0.0008  21  SER B N   
4931  C CA  . SER B 29  ? 0.1211 0.1408 0.1836 0.0364  0.0165  -0.0003 21  SER B CA  
4932  C C   . SER B 29  ? 0.1416 0.1700 0.2086 0.0342  0.0188  0.0018  21  SER B C   
4933  O O   . SER B 29  ? 0.1542 0.1886 0.2283 0.0327  0.0185  0.0044  21  SER B O   
4934  C CB  . SER B 29  ? 0.1525 0.1651 0.2122 0.0318  0.0136  -0.0001 21  SER B CB  
4935  O OG  . SER B 29  ? 0.1442 0.1549 0.2009 0.0280  0.0140  -0.0009 21  SER B OG  
4936  N N   . GLY B 30  ? 0.1327 0.1610 0.1953 0.0340  0.0205  0.0007  22  GLY B N   
4937  C CA  . GLY B 30  ? 0.1311 0.1659 0.1969 0.0315  0.0222  0.0029  22  GLY B CA  
4938  C C   . GLY B 30  ? 0.1264 0.1652 0.1895 0.0349  0.0259  0.0031  22  GLY B C   
4939  O O   . GLY B 30  ? 0.1667 0.2028 0.2244 0.0396  0.0272  0.0008  22  GLY B O   
4940  N N   . HIS B 31  ? 0.1269 0.1719 0.1933 0.0329  0.0276  0.0061  23  HIS B N   
4941  C CA  . HIS B 31  ? 0.1335 0.1812 0.1952 0.0350  0.0311  0.0070  23  HIS B CA  
4942  C C   . HIS B 31  ? 0.1159 0.1739 0.1858 0.0356  0.0352  0.0116  23  HIS B C   
4943  O O   . HIS B 31  ? 0.1642 0.2259 0.2399 0.0315  0.0347  0.0149  23  HIS B O   
4944  C CB  . HIS B 31  ? 0.1581 0.2027 0.2156 0.0314  0.0290  0.0070  23  HIS B CB  
4945  C CG  . HIS B 31  ? 0.2154 0.2513 0.2675 0.0300  0.0249  0.0031  23  HIS B CG  
4946  N ND1 . HIS B 31  ? 0.2459 0.2788 0.3020 0.0267  0.0221  0.0023  23  HIS B ND1 
4947  C CD2 . HIS B 31  ? 0.3225 0.3521 0.3658 0.0311  0.0230  0.0000  23  HIS B CD2 
4948  C CE1 . HIS B 31  ? 0.3134 0.3394 0.3647 0.0257  0.0193  -0.0007 23  HIS B CE1 
4949  N NE2 . HIS B 31  ? 0.2482 0.2720 0.2922 0.0281  0.0192  -0.0022 23  HIS B NE2 
4950  N N   . PRO B 32  ? 0.1453 0.2081 0.2166 0.0405  0.0394  0.0121  24  PRO B N   
4951  C CA  . PRO B 32  ? 0.1186 0.1926 0.2007 0.0406  0.0435  0.0171  24  PRO B CA  
4952  C C   . PRO B 32  ? 0.1480 0.2262 0.2257 0.0419  0.0490  0.0202  24  PRO B C   
4953  O O   . PRO B 32  ? 0.1237 0.2105 0.2105 0.0399  0.0521  0.0254  24  PRO B O   
4954  C CB  . PRO B 32  ? 0.1504 0.2280 0.2374 0.0459  0.0455  0.0160  24  PRO B CB  
4955  C CG  . PRO B 32  ? 0.1487 0.2170 0.2221 0.0506  0.0454  0.0107  24  PRO B CG  
4956  C CD  . PRO B 32  ? 0.1634 0.2217 0.2290 0.0460  0.0398  0.0081  24  PRO B CD  
4957  N N   . GLY B 33  ? 0.1265 0.1981 0.1900 0.0451  0.0500  0.0172  25  GLY B N   
4958  C CA  . GLY B 33  ? 0.1374 0.2123 0.1940 0.0479  0.0560  0.0199  25  GLY B CA  
4959  C C   . GLY B 33  ? 0.1614 0.2377 0.2183 0.0430  0.0556  0.0244  25  GLY B C   
4960  O O   . GLY B 33  ? 0.1465 0.2299 0.2061 0.0432  0.0612  0.0297  25  GLY B O   
4961  N N   . ALA B 34  ? 0.1502 0.2194 0.2044 0.0388  0.0494  0.0226  26  ALA B N   
4962  C CA  . ALA B 34  ? 0.1344 0.2040 0.1892 0.0345  0.0484  0.0266  26  ALA B CA  
4963  C C   . ALA B 34  ? 0.1270 0.2043 0.1971 0.0301  0.0490  0.0318  26  ALA B C   
4964  O O   . ALA B 34  ? 0.1547 0.2359 0.2269 0.0283  0.0518  0.0373  26  ALA B O   
4965  C CB  . ALA B 34  ? 0.1251 0.1861 0.1747 0.0316  0.0416  0.0232  26  ALA B CB  
4966  N N   . PRO B 35  ? 0.1332 0.2119 0.2137 0.0281  0.0459  0.0304  27  PRO B N   
4967  C CA  . PRO B 35  ? 0.1384 0.2246 0.2337 0.0244  0.0462  0.0352  27  PRO B CA  
4968  C C   . PRO B 35  ? 0.1459 0.2421 0.2473 0.0263  0.0532  0.0405  27  PRO B C   
4969  O O   . PRO B 35  ? 0.1445 0.2455 0.2538 0.0226  0.0546  0.0463  27  PRO B O   
4970  C CB  . PRO B 35  ? 0.1210 0.2064 0.2231 0.0239  0.0421  0.0319  27  PRO B CB  
4971  C CG  . PRO B 35  ? 0.1126 0.1882 0.2043 0.0242  0.0380  0.0264  27  PRO B CG  
4972  C CD  . PRO B 35  ? 0.1385 0.2113 0.2177 0.0283  0.0412  0.0249  27  PRO B CD  
4973  N N   . MET B 36  ? 0.1187 0.2180 0.2169 0.0320  0.0579  0.0390  28  MET B N   
4974  C CA  . MET B 36  ? 0.1199 0.2299 0.2245 0.0345  0.0658  0.0441  28  MET B CA  
4975  C C   . MET B 36  ? 0.1291 0.2388 0.2243 0.0346  0.0708  0.0484  28  MET B C   
4976  O O   . MET B 36  ? 0.1315 0.2499 0.2351 0.0330  0.0762  0.0553  28  MET B O   
4977  C CB  . MET B 36  ? 0.1375 0.2501 0.2399 0.0416  0.0699  0.0407  28  MET B CB  
4978  C CG  . MET B 36  ? 0.1333 0.2466 0.2459 0.0416  0.0650  0.0376  28  MET B CG  
4979  S SD  . MET B 36  ? 0.1478 0.2610 0.2559 0.0505  0.0682  0.0326  28  MET B SD  
4980  C CE  . MET B 36  ? 0.1381 0.2675 0.2594 0.0540  0.0782  0.0387  28  MET B CE  
4981  N N   . GLY B 37  ? 0.1573 0.2571 0.2351 0.0364  0.0689  0.0448  29  GLY B N   
4982  C CA  . GLY B 37  ? 0.1458 0.2439 0.2125 0.0368  0.0727  0.0488  29  GLY B CA  
4983  C C   . GLY B 37  ? 0.1739 0.2720 0.2470 0.0302  0.0700  0.0544  29  GLY B C   
4984  O O   . GLY B 37  ? 0.1945 0.2950 0.2646 0.0296  0.0748  0.0606  29  GLY B O   
4985  N N   . MET B 38  ? 0.1310 0.2259 0.2124 0.0254  0.0626  0.0524  30  MET B N   
4986  C CA  . MET B 38  ? 0.1281 0.2208 0.2145 0.0197  0.0589  0.0564  30  MET B CA  
4987  C C   . MET B 38  ? 0.2069 0.3075 0.3119 0.0150  0.0594  0.0617  30  MET B C   
4988  O O   . MET B 38  ? 0.1197 0.2176 0.2303 0.0100  0.0554  0.0645  30  MET B O   
4989  C CB  . MET B 38  ? 0.1216 0.2051 0.2048 0.0176  0.0506  0.0509  30  MET B CB  
4990  C CG  . MET B 38  ? 0.1286 0.2038 0.1953 0.0204  0.0487  0.0475  30  MET B CG  
4991  S SD  . MET B 38  ? 0.1663 0.2329 0.2328 0.0175  0.0397  0.0424  30  MET B SD  
4992  C CE  . MET B 38  ? 0.1821 0.2479 0.2501 0.0195  0.0380  0.0353  30  MET B CE  
4993  N N   . ALA B 39  ? 0.1209 0.2311 0.2361 0.0167  0.0639  0.0630  31  ALA B N   
4994  C CA  . ALA B 39  ? 0.1840 0.3014 0.3187 0.0120  0.0623  0.0668  31  ALA B CA  
4995  C C   . ALA B 39  ? 0.1187 0.2394 0.2605 0.0071  0.0646  0.0753  31  ALA B C   
4996  O O   . ALA B 39  ? 0.1764 0.2964 0.3300 0.0015  0.0594  0.0774  31  ALA B O   
4997  C CB  . ALA B 39  ? 0.1130 0.2409 0.2581 0.0154  0.0667  0.0669  31  ALA B CB  
4998  N N   . GLU B 40  ? 0.1291 0.2529 0.2637 0.0093  0.0725  0.0804  32  GLU B N   
4999  C CA  . GLU B 40  ? 0.1348 0.2612 0.2757 0.0044  0.0752  0.0894  32  GLU B CA  
5000  C C   . GLU B 40  ? 0.1359 0.2504 0.2688 0.0009  0.0685  0.0893  32  GLU B C   
5001  O O   . GLU B 40  ? 0.1363 0.2499 0.2788 -0.0050 0.0659  0.0947  32  GLU B O   
5002  C CB  . GLU B 40  ? 0.1635 0.2944 0.2958 0.0079  0.0852  0.0947  32  GLU B CB  
5003  C CG  . GLU B 40  ? 0.1532 0.2931 0.2951 0.0092  0.0896  0.0955  32  GLU B CG  
5004  C CD  . GLU B 40  ? 0.2067 0.3495 0.3468 0.0153  0.0906  0.0884  32  GLU B CD  
5005  O OE1 . GLU B 40  ? 0.1499 0.2883 0.2754 0.0205  0.0920  0.0841  32  GLU B OE1 
5006  O OE2 . GLU B 40  ? 0.1467 0.2956 0.2997 0.0151  0.0896  0.0872  32  GLU B OE2 
5007  N N   . MET B 41  ? 0.1375 0.2426 0.2531 0.0044  0.0655  0.0834  33  MET B N   
5008  C CA  . MET B 41  ? 0.1471 0.2414 0.2567 0.0017  0.0584  0.0824  33  MET B CA  
5009  C C   . MET B 41  ? 0.1409 0.2328 0.2635 -0.0029 0.0507  0.0797  33  MET B C   
5010  O O   . MET B 41  ? 0.1298 0.2170 0.2569 -0.0073 0.0466  0.0829  33  MET B O   
5011  C CB  . MET B 41  ? 0.1396 0.2257 0.2315 0.0063  0.0558  0.0756  33  MET B CB  
5012  C CG  . MET B 41  ? 0.1708 0.2563 0.2464 0.0110  0.0619  0.0779  33  MET B CG  
5013  S SD  . MET B 41  ? 0.2016 0.2801 0.2605 0.0170  0.0588  0.0680  33  MET B SD  
5014  C CE  . MET B 41  ? 0.1695 0.2378 0.2272 0.0140  0.0484  0.0644  33  MET B CE  
5015  N N   . ALA B 42  ? 0.1511 0.2454 0.2789 -0.0016 0.0485  0.0738  34  ALA B N   
5016  C CA  . ALA B 42  ? 0.1486 0.2400 0.2868 -0.0053 0.0412  0.0708  34  ALA B CA  
5017  C C   . ALA B 42  ? 0.1327 0.2295 0.2877 -0.0107 0.0409  0.0772  34  ALA B C   
5018  O O   . ALA B 42  ? 0.1177 0.2087 0.2780 -0.0150 0.0350  0.0780  34  ALA B O   
5019  C CB  . ALA B 42  ? 0.1150 0.2077 0.2539 -0.0025 0.0394  0.0640  34  ALA B CB  
5020  N N   . GLU B 43  ? 0.1216 0.2295 0.2857 -0.0103 0.0472  0.0820  35  GLU B N   
5021  C CA  . GLU B 43  ? 0.1594 0.2731 0.3411 -0.0158 0.0465  0.0882  35  GLU B CA  
5022  C C   . GLU B 43  ? 0.1811 0.2897 0.3631 -0.0204 0.0457  0.0947  35  GLU B C   
5023  O O   . GLU B 43  ? 0.1506 0.2545 0.3414 -0.0255 0.0391  0.0957  35  GLU B O   
5024  C CB  . GLU B 43  ? 0.1564 0.2798 0.3421 -0.0134 0.0529  0.0905  35  GLU B CB  
5025  C CG  . GLU B 43  ? 0.2116 0.3381 0.4120 -0.0184 0.0504  0.0948  35  GLU B CG  
5026  C CD  . GLU B 43  ? 0.2824 0.4185 0.4863 -0.0167 0.0585  0.0995  35  GLU B CD  
5027  O OE1 . GLU B 43  ? 0.3257 0.4641 0.5396 -0.0210 0.0585  0.1051  35  GLU B OE1 
5028  O OE2 . GLU B 43  ? 0.2713 0.4122 0.4679 -0.0109 0.0650  0.0975  35  GLU B OE2 
5029  N N   . THR B 44  ? 0.1286 0.2359 0.2985 -0.0183 0.0517  0.0987  36  THR B N   
5030  C CA  . THR B 44  ? 0.1643 0.2663 0.3336 -0.0225 0.0513  0.1058  36  THR B CA  
5031  C C   . THR B 44  ? 0.1352 0.2241 0.3007 -0.0245 0.0416  0.1015  36  THR B C   
5032  O O   . THR B 44  ? 0.1678 0.2525 0.3431 -0.0300 0.0369  0.1051  36  THR B O   
5033  C CB  . THR B 44  ? 0.2338 0.3353 0.3871 -0.0188 0.0587  0.1099  36  THR B CB  
5034  O OG1 . THR B 44  ? 0.1988 0.3112 0.3529 -0.0155 0.0676  0.1120  36  THR B OG1 
5035  C CG2 . THR B 44  ? 0.2534 0.3498 0.4068 -0.0234 0.0589  0.1189  36  THR B CG2 
5036  N N   . LEU B 45  ? 0.1314 0.2137 0.2835 -0.0201 0.0385  0.0936  37  LEU B N   
5037  C CA  . LEU B 45  ? 0.1302 0.2009 0.2787 -0.0212 0.0304  0.0894  37  LEU B CA  
5038  C C   . LEU B 45  ? 0.1245 0.1931 0.2859 -0.0249 0.0236  0.0864  37  LEU B C   
5039  O O   . LEU B 45  ? 0.1280 0.1889 0.2937 -0.0285 0.0180  0.0878  37  LEU B O   
5040  C CB  . LEU B 45  ? 0.1822 0.2481 0.3165 -0.0158 0.0288  0.0815  37  LEU B CB  
5041  C CG  . LEU B 45  ? 0.1413 0.1968 0.2735 -0.0162 0.0210  0.0764  37  LEU B CG  
5042  C CD1 . LEU B 45  ? 0.1367 0.1849 0.2679 -0.0186 0.0186  0.0819  37  LEU B CD1 
5043  C CD2 . LEU B 45  ? 0.1280 0.1805 0.2485 -0.0113 0.0201  0.0691  37  LEU B CD2 
5044  N N   . TRP B 46  ? 0.1296 0.2041 0.2962 -0.0237 0.0236  0.0820  38  TRP B N   
5045  C CA  . TRP B 46  ? 0.1643 0.2349 0.3392 -0.0263 0.0161  0.0776  38  TRP B CA  
5046  C C   . TRP B 46  ? 0.1874 0.2612 0.3792 -0.0324 0.0139  0.0836  38  TRP B C   
5047  O O   . TRP B 46  ? 0.1967 0.2626 0.3934 -0.0356 0.0063  0.0817  38  TRP B O   
5048  C CB  . TRP B 46  ? 0.1050 0.1794 0.2783 -0.0228 0.0159  0.0707  38  TRP B CB  
5049  C CG  . TRP B 46  ? 0.1302 0.1972 0.2893 -0.0185 0.0141  0.0632  38  TRP B CG  
5050  C CD1 . TRP B 46  ? 0.1032 0.1681 0.2499 -0.0149 0.0174  0.0623  38  TRP B CD1 
5051  C CD2 . TRP B 46  ? 0.1131 0.1738 0.2696 -0.0176 0.0086  0.0559  38  TRP B CD2 
5052  N NE1 . TRP B 46  ? 0.0995 0.1582 0.2381 -0.0123 0.0142  0.0551  38  TRP B NE1 
5053  C CE2 . TRP B 46  ? 0.0964 0.1526 0.2405 -0.0138 0.0094  0.0513  38  TRP B CE2 
5054  C CE3 . TRP B 46  ? 0.1183 0.1765 0.2814 -0.0197 0.0029  0.0530  38  TRP B CE3 
5055  C CZ2 . TRP B 46  ? 0.1289 0.1792 0.2679 -0.0121 0.0059  0.0445  38  TRP B CZ2 
5056  C CZ3 . TRP B 46  ? 0.1377 0.1890 0.2934 -0.0175 -0.0008 0.0459  38  TRP B CZ3 
5057  C CH2 . TRP B 46  ? 0.1544 0.2023 0.2986 -0.0138 0.0013  0.0419  38  TRP B CH2 
5058  N N   . THR B 47  ? 0.1531 0.2378 0.3540 -0.0340 0.0203  0.0909  39  THR B N   
5059  C CA  . THR B 47  ? 0.1453 0.2306 0.3578 -0.0384 0.0169  0.0945  39  THR B CA  
5060  C C   . THR B 47  ? 0.2159 0.2955 0.4291 -0.0423 0.0165  0.1013  39  THR B C   
5061  O O   . THR B 47  ? 0.2311 0.3070 0.4534 -0.0467 0.0109  0.1030  39  THR B O   
5062  C CB  . THR B 47  ? 0.1669 0.2642 0.3859 -0.0370 0.0225  0.0968  39  THR B CB  
5063  O OG1 . THR B 47  ? 0.1528 0.2559 0.3659 -0.0349 0.0320  0.1025  39  THR B OG1 
5064  C CG2 . THR B 47  ? 0.1418 0.2441 0.3600 -0.0329 0.0225  0.0904  39  THR B CG2 
5065  N N   . LYS B 48  ? 0.1639 0.2418 0.3671 -0.0408 0.0217  0.1052  40  LYS B N   
5066  C CA  . LYS B 48  ? 0.2376 0.3102 0.4404 -0.0442 0.0220  0.1125  40  LYS B CA  
5067  C C   . LYS B 48  ? 0.2317 0.2908 0.4280 -0.0452 0.0163  0.1119  40  LYS B C   
5068  O O   . LYS B 48  ? 0.2376 0.2898 0.4357 -0.0486 0.0135  0.1166  40  LYS B O   
5069  C CB  . LYS B 48  ? 0.2053 0.2848 0.4006 -0.0419 0.0322  0.1191  40  LYS B CB  
5070  C CG  . LYS B 48  ? 0.2689 0.3613 0.4707 -0.0406 0.0386  0.1205  40  LYS B CG  
5071  C CD  . LYS B 48  ? 0.3108 0.4053 0.5259 -0.0457 0.0371  0.1258  40  LYS B CD  
5072  C CE  . LYS B 48  ? 0.3301 0.4376 0.5506 -0.0441 0.0454  0.1291  40  LYS B CE  
5073  N NZ  . LYS B 48  ? 0.3058 0.4208 0.5322 -0.0412 0.0447  0.1228  40  LYS B NZ  
5074  N N   . PHE B 49  ? 0.1456 0.1998 0.3319 -0.0409 0.0139  0.1042  41  PHE B N   
5075  C CA  . PHE B 49  ? 0.1804 0.2218 0.3563 -0.0393 0.0090  0.1020  41  PHE B CA  
5076  C C   . PHE B 49  ? 0.1602 0.1936 0.3335 -0.0371 0.0016  0.0919  41  PHE B C   
5077  O O   . PHE B 49  ? 0.2333 0.2556 0.4065 -0.0382 -0.0047 0.0908  41  PHE B O   
5078  C CB  . PHE B 49  ? 0.1619 0.2038 0.3218 -0.0342 0.0143  0.1027  41  PHE B CB  
5079  C CG  . PHE B 49  ? 0.1902 0.2364 0.3486 -0.0359 0.0213  0.1130  41  PHE B CG  
5080  C CD1 . PHE B 49  ? 0.1910 0.2287 0.3475 -0.0385 0.0194  0.1200  41  PHE B CD1 
5081  C CD2 . PHE B 49  ? 0.2072 0.2655 0.3660 -0.0345 0.0299  0.1160  41  PHE B CD2 
5082  C CE1 . PHE B 49  ? 0.2362 0.2774 0.3902 -0.0401 0.0264  0.1302  41  PHE B CE1 
5083  C CE2 . PHE B 49  ? 0.2558 0.3183 0.4125 -0.0358 0.0374  0.1259  41  PHE B CE2 
5084  C CZ  . PHE B 49  ? 0.2665 0.3204 0.4203 -0.0387 0.0358  0.1332  41  PHE B CZ  
5085  N N   . LEU B 50  ? 0.1571 0.1953 0.3277 -0.0337 0.0024  0.0847  42  LEU B N   
5086  C CA  . LEU B 50  ? 0.1528 0.1836 0.3176 -0.0306 -0.0030 0.0754  42  LEU B CA  
5087  C C   . LEU B 50  ? 0.1919 0.2148 0.3651 -0.0341 -0.0107 0.0732  42  LEU B C   
5088  O O   . LEU B 50  ? 0.1445 0.1715 0.3286 -0.0379 -0.0124 0.0747  42  LEU B O   
5089  C CB  . LEU B 50  ? 0.1213 0.1590 0.2823 -0.0269 -0.0003 0.0692  42  LEU B CB  
5090  C CG  . LEU B 50  ? 0.1738 0.2052 0.3267 -0.0230 -0.0036 0.0602  42  LEU B CG  
5091  C CD1 . LEU B 50  ? 0.1500 0.1784 0.2922 -0.0192 -0.0020 0.0591  42  LEU B CD1 
5092  C CD2 . LEU B 50  ? 0.1627 0.2002 0.3145 -0.0209 -0.0019 0.0552  42  LEU B CD2 
5093  N N   . ASN B 51  ? 0.1648 0.1762 0.3331 -0.0327 -0.0159 0.0693  43  ASN B N   
5094  C CA  . ASN B 51  ? 0.1806 0.1820 0.3542 -0.0351 -0.0238 0.0661  43  ASN B CA  
5095  C C   . ASN B 51  ? 0.1725 0.1708 0.3394 -0.0309 -0.0262 0.0561  43  ASN B C   
5096  O O   . ASN B 51  ? 0.1878 0.1815 0.3458 -0.0264 -0.0259 0.0514  43  ASN B O   
5097  C CB  . ASN B 51  ? 0.2169 0.2067 0.3896 -0.0358 -0.0279 0.0685  43  ASN B CB  
5098  C CG  . ASN B 51  ? 0.1851 0.1762 0.3660 -0.0413 -0.0268 0.0790  43  ASN B CG  
5099  O OD1 . ASN B 51  ? 0.1619 0.1582 0.3539 -0.0463 -0.0269 0.0832  43  ASN B OD1 
5100  N ND2 . ASN B 51  ? 0.2010 0.1877 0.3768 -0.0403 -0.0256 0.0837  43  ASN B ND2 
5101  N N   . HIS B 52  ? 0.1508 0.1515 0.3222 -0.0325 -0.0285 0.0533  44  HIS B N   
5102  C CA  . HIS B 52  ? 0.1629 0.1611 0.3266 -0.0286 -0.0299 0.0447  44  HIS B CA  
5103  C C   . HIS B 52  ? 0.2159 0.2105 0.3854 -0.0316 -0.0365 0.0422  44  HIS B C   
5104  O O   . HIS B 52  ? 0.1838 0.1824 0.3651 -0.0366 -0.0386 0.0475  44  HIS B O   
5105  C CB  . HIS B 52  ? 0.1594 0.1682 0.3180 -0.0253 -0.0232 0.0435  44  HIS B CB  
5106  C CG  . HIS B 52  ? 0.1191 0.1389 0.2861 -0.0280 -0.0206 0.0480  44  HIS B CG  
5107  N ND1 . HIS B 52  ? 0.1139 0.1388 0.2801 -0.0265 -0.0200 0.0445  44  HIS B ND1 
5108  C CD2 . HIS B 52  ? 0.1363 0.1632 0.3131 -0.0317 -0.0181 0.0559  44  HIS B CD2 
5109  C CE1 . HIS B 52  ? 0.1721 0.2071 0.3481 -0.0289 -0.0176 0.0497  44  HIS B CE1 
5110  N NE2 . HIS B 52  ? 0.1645 0.2013 0.3471 -0.0321 -0.0159 0.0567  44  HIS B NE2 
5111  N N   . ASN B 53  ? 0.1657 0.1530 0.3269 -0.0284 -0.0399 0.0342  45  ASN B N   
5112  C CA  . ASN B 53  ? 0.1742 0.1564 0.3378 -0.0304 -0.0471 0.0308  45  ASN B CA  
5113  C C   . ASN B 53  ? 0.1708 0.1566 0.3266 -0.0269 -0.0454 0.0255  45  ASN B C   
5114  O O   . ASN B 53  ? 0.1442 0.1237 0.2879 -0.0224 -0.0447 0.0191  45  ASN B O   
5115  C CB  . ASN B 53  ? 0.2027 0.1691 0.3618 -0.0299 -0.0544 0.0259  45  ASN B CB  
5116  C CG  . ASN B 53  ? 0.2091 0.1687 0.3702 -0.0324 -0.0632 0.0224  45  ASN B CG  
5117  O OD1 . ASN B 53  ? 0.2223 0.1899 0.3911 -0.0353 -0.0645 0.0249  45  ASN B OD1 
5118  N ND2 . ASN B 53  ? 0.1801 0.1246 0.3341 -0.0308 -0.0697 0.0165  45  ASN B ND2 
5119  N N   . PRO B 54  ? 0.1491 0.1448 0.3118 -0.0288 -0.0447 0.0283  46  PRO B N   
5120  C CA  . PRO B 54  ? 0.2046 0.2026 0.3597 -0.0255 -0.0437 0.0237  46  PRO B CA  
5121  C C   . PRO B 54  ? 0.2545 0.2403 0.3997 -0.0237 -0.0503 0.0164  46  PRO B C   
5122  O O   . PRO B 54  ? 0.2367 0.2210 0.3704 -0.0197 -0.0480 0.0118  46  PRO B O   
5123  C CB  . PRO B 54  ? 0.2434 0.2526 0.4112 -0.0286 -0.0442 0.0285  46  PRO B CB  
5124  C CG  . PRO B 54  ? 0.2595 0.2756 0.4393 -0.0323 -0.0410 0.0362  46  PRO B CG  
5125  C CD  . PRO B 54  ? 0.1957 0.2008 0.3738 -0.0338 -0.0443 0.0360  46  PRO B CD  
5126  N N   . ALA B 55  ? 0.2198 0.1959 0.3683 -0.0266 -0.0585 0.0154  47  ALA B N   
5127  C CA  . ALA B 55  ? 0.2535 0.2163 0.3904 -0.0243 -0.0651 0.0080  47  ALA B CA  
5128  C C   . ALA B 55  ? 0.2721 0.2260 0.3948 -0.0191 -0.0616 0.0025  47  ALA B C   
5129  O O   . ALA B 55  ? 0.2217 0.1660 0.3314 -0.0157 -0.0643 -0.0041 47  ALA B O   
5130  C CB  . ALA B 55  ? 0.2483 0.2021 0.3928 -0.0289 -0.0757 0.0080  47  ALA B CB  
5131  N N   . ASN B 56  ? 0.2229 0.1799 0.3477 -0.0182 -0.0558 0.0050  48  ASN B N   
5132  C CA  . ASN B 56  ? 0.1772 0.1277 0.2910 -0.0130 -0.0520 0.0003  48  ASN B CA  
5133  C C   . ASN B 56  ? 0.1967 0.1579 0.3128 -0.0115 -0.0433 0.0039  48  ASN B C   
5134  O O   . ASN B 56  ? 0.2089 0.1708 0.3307 -0.0124 -0.0421 0.0075  48  ASN B O   
5135  C CB  . ASN B 56  ? 0.1824 0.1202 0.2963 -0.0129 -0.0573 -0.0017 48  ASN B CB  
5136  C CG  . ASN B 56  ? 0.1854 0.1172 0.2893 -0.0068 -0.0532 -0.0069 48  ASN B CG  
5137  O OD1 . ASN B 56  ? 0.2407 0.1778 0.3376 -0.0030 -0.0465 -0.0091 48  ASN B OD1 
5138  N ND2 . ASN B 56  ? 0.2235 0.1445 0.3276 -0.0059 -0.0571 -0.0086 48  ASN B ND2 
5139  N N   . PRO B 57  ? 0.2393 0.2078 0.3502 -0.0091 -0.0376 0.0029  49  PRO B N   
5140  C CA  . PRO B 57  ? 0.2046 0.1823 0.3168 -0.0077 -0.0301 0.0058  49  PRO B CA  
5141  C C   . PRO B 57  ? 0.1999 0.1734 0.3088 -0.0043 -0.0277 0.0036  49  PRO B C   
5142  O O   . PRO B 57  ? 0.1627 0.1429 0.2742 -0.0036 -0.0232 0.0065  49  PRO B O   
5143  C CB  . PRO B 57  ? 0.2167 0.1996 0.3223 -0.0056 -0.0260 0.0037  49  PRO B CB  
5144  C CG  . PRO B 57  ? 0.2575 0.2379 0.3629 -0.0075 -0.0315 0.0028  49  PRO B CG  
5145  C CD  . PRO B 57  ? 0.2085 0.1770 0.3127 -0.0082 -0.0385 -0.0001 49  PRO B CD  
5146  N N   . LYS B 58  ? 0.2073 0.1700 0.3105 -0.0017 -0.0307 -0.0015 50  LYS B N   
5147  C CA  . LYS B 58  ? 0.2237 0.1823 0.3248 0.0022  -0.0286 -0.0040 50  LYS B CA  
5148  C C   . LYS B 58  ? 0.1755 0.1264 0.2822 0.0011  -0.0337 -0.0024 50  LYS B C   
5149  O O   . LYS B 58  ? 0.2051 0.1506 0.3101 0.0049  -0.0333 -0.0052 50  LYS B O   
5150  C CB  . LYS B 58  ? 0.2080 0.1597 0.2982 0.0071  -0.0271 -0.0112 50  LYS B CB  
5151  C CG  . LYS B 58  ? 0.2404 0.1991 0.3246 0.0088  -0.0210 -0.0126 50  LYS B CG  
5152  C CD  . LYS B 58  ? 0.3666 0.3365 0.4566 0.0087  -0.0154 -0.0088 50  LYS B CD  
5153  C CE  . LYS B 58  ? 0.5046 0.4806 0.5895 0.0098  -0.0099 -0.0099 50  LYS B CE  
5154  N NZ  . LYS B 58  ? 0.5250 0.5116 0.6160 0.0081  -0.0066 -0.0055 50  LYS B NZ  
5155  N N   . PHE B 59  ? 0.2042 0.1543 0.3181 -0.0041 -0.0387 0.0022  51  PHE B N   
5156  C CA  . PHE B 59  ? 0.2023 0.1451 0.3225 -0.0061 -0.0436 0.0050  51  PHE B CA  
5157  C C   . PHE B 59  ? 0.1642 0.1091 0.2861 -0.0034 -0.0400 0.0072  51  PHE B C   
5158  O O   . PHE B 59  ? 0.1760 0.1314 0.3004 -0.0040 -0.0352 0.0116  51  PHE B O   
5159  C CB  . PHE B 59  ? 0.1771 0.1240 0.3073 -0.0128 -0.0467 0.0121  51  PHE B CB  
5160  C CG  . PHE B 59  ? 0.1984 0.1400 0.3363 -0.0159 -0.0503 0.0174  51  PHE B CG  
5161  C CD1 . PHE B 59  ? 0.2055 0.1328 0.3419 -0.0146 -0.0562 0.0141  51  PHE B CD1 
5162  C CD2 . PHE B 59  ? 0.2193 0.1696 0.3654 -0.0200 -0.0477 0.0260  51  PHE B CD2 
5163  C CE1 . PHE B 59  ? 0.1915 0.1130 0.3351 -0.0176 -0.0600 0.0196  51  PHE B CE1 
5164  C CE2 . PHE B 59  ? 0.2203 0.1653 0.3731 -0.0231 -0.0508 0.0318  51  PHE B CE2 
5165  C CZ  . PHE B 59  ? 0.1940 0.1244 0.3458 -0.0221 -0.0571 0.0287  51  PHE B CZ  
5166  N N   . TYR B 60  ? 0.1741 0.1085 0.2943 -0.0000 -0.0429 0.0038  52  TYR B N   
5167  C CA  . TYR B 60  ? 0.2608 0.1969 0.3818 0.0041  -0.0397 0.0043  52  TYR B CA  
5168  C C   . TYR B 60  ? 0.2254 0.1675 0.3532 0.0008  -0.0391 0.0126  52  TYR B C   
5169  O O   . TYR B 60  ? 0.2237 0.1728 0.3517 0.0031  -0.0351 0.0142  52  TYR B O   
5170  C CB  . TYR B 60  ? 0.2602 0.1831 0.3796 0.0083  -0.0438 -0.0002 52  TYR B CB  
5171  C CG  . TYR B 60  ? 0.2752 0.1909 0.3860 0.0131  -0.0436 -0.0089 52  TYR B CG  
5172  C CD1 . TYR B 60  ? 0.2532 0.1760 0.3578 0.0152  -0.0378 -0.0125 52  TYR B CD1 
5173  C CD2 . TYR B 60  ? 0.2838 0.1846 0.3918 0.0158  -0.0490 -0.0135 52  TYR B CD2 
5174  C CE1 . TYR B 60  ? 0.2345 0.1501 0.3294 0.0199  -0.0371 -0.0202 52  TYR B CE1 
5175  C CE2 . TYR B 60  ? 0.3427 0.2360 0.4409 0.0209  -0.0485 -0.0218 52  TYR B CE2 
5176  C CZ  . TYR B 60  ? 0.2942 0.1951 0.3856 0.0229  -0.0422 -0.0249 52  TYR B CZ  
5177  O OH  . TYR B 60  ? 0.3222 0.2150 0.4022 0.0282  -0.0411 -0.0328 52  TYR B OH  
5178  N N   . ASN B 61  ? 0.1979 0.1365 0.3312 -0.0046 -0.0434 0.0181  53  ASN B N   
5179  C CA  . ASN B 61  ? 0.2567 0.1988 0.3952 -0.0075 -0.0429 0.0265  53  ASN B CA  
5180  C C   . ASN B 61  ? 0.2203 0.1742 0.3617 -0.0121 -0.0390 0.0324  53  ASN B C   
5181  O O   . ASN B 61  ? 0.1625 0.1186 0.3083 -0.0157 -0.0387 0.0401  53  ASN B O   
5182  C CB  . ASN B 61  ? 0.2397 0.1700 0.3833 -0.0105 -0.0495 0.0301  53  ASN B CB  
5183  C CG  . ASN B 61  ? 0.2303 0.1613 0.3767 -0.0115 -0.0489 0.0380  53  ASN B CG  
5184  O OD1 . ASN B 61  ? 0.2347 0.1690 0.3779 -0.0072 -0.0462 0.0377  53  ASN B OD1 
5185  N ND2 . ASN B 61  ? 0.2024 0.1307 0.3549 -0.0175 -0.0516 0.0456  53  ASN B ND2 
5186  N N   . ARG B 62  ? 0.1531 0.1144 0.2918 -0.0117 -0.0358 0.0290  54  ARG B N   
5187  C CA  . ARG B 62  ? 0.1448 0.1176 0.2861 -0.0149 -0.0316 0.0339  54  ARG B CA  
5188  C C   . ARG B 62  ? 0.1915 0.1715 0.3305 -0.0133 -0.0267 0.0380  54  ARG B C   
5189  O O   . ARG B 62  ? 0.1751 0.1541 0.3097 -0.0090 -0.0256 0.0350  54  ARG B O   
5190  C CB  . ARG B 62  ? 0.1703 0.1484 0.3079 -0.0137 -0.0294 0.0289  54  ARG B CB  
5191  C CG  . ARG B 62  ? 0.1368 0.1184 0.2670 -0.0086 -0.0249 0.0240  54  ARG B CG  
5192  C CD  . ARG B 62  ? 0.1401 0.1244 0.2659 -0.0074 -0.0233 0.0190  54  ARG B CD  
5193  N NE  . ARG B 62  ? 0.1343 0.1223 0.2543 -0.0032 -0.0187 0.0153  54  ARG B NE  
5194  C CZ  . ARG B 62  ? 0.2007 0.1835 0.3166 0.0007  -0.0185 0.0100  54  ARG B CZ  
5195  N NH1 . ARG B 62  ? 0.1547 0.1274 0.2702 0.0017  -0.0227 0.0072  54  ARG B NH1 
5196  N NH2 . ARG B 62  ? 0.2106 0.1983 0.3234 0.0038  -0.0139 0.0075  54  ARG B NH2 
5197  N N   . ASP B 63  ? 0.1452 0.1325 0.2873 -0.0166 -0.0237 0.0449  55  ASP B N   
5198  C CA  . ASP B 63  ? 0.1381 0.1330 0.2754 -0.0146 -0.0186 0.0475  55  ASP B CA  
5199  C C   . ASP B 63  ? 0.1237 0.1245 0.2559 -0.0113 -0.0152 0.0415  55  ASP B C   
5200  O O   . ASP B 63  ? 0.1476 0.1498 0.2807 -0.0118 -0.0153 0.0378  55  ASP B O   
5201  C CB  . ASP B 63  ? 0.1677 0.1697 0.3080 -0.0182 -0.0149 0.0555  55  ASP B CB  
5202  C CG  . ASP B 63  ? 0.1757 0.1724 0.3205 -0.0217 -0.0172 0.0630  55  ASP B CG  
5203  O OD1 . ASP B 63  ? 0.1981 0.1858 0.3413 -0.0203 -0.0211 0.0627  55  ASP B OD1 
5204  O OD2 . ASP B 63  ? 0.1641 0.1661 0.3145 -0.0258 -0.0147 0.0696  55  ASP B OD2 
5205  N N   . ARG B 64  ? 0.1209 0.1246 0.2477 -0.0079 -0.0127 0.0406  56  ARG B N   
5206  C CA  . ARG B 64  ? 0.1291 0.1384 0.2514 -0.0053 -0.0095 0.0357  56  ARG B CA  
5207  C C   . ARG B 64  ? 0.1393 0.1567 0.2588 -0.0057 -0.0051 0.0394  56  ARG B C   
5208  O O   . ARG B 64  ? 0.2049 0.2230 0.3219 -0.0056 -0.0042 0.0441  56  ARG B O   
5209  C CB  . ARG B 64  ? 0.1296 0.1368 0.2491 -0.0013 -0.0101 0.0318  56  ARG B CB  
5210  C CG  . ARG B 64  ? 0.1928 0.1950 0.3132 0.0008  -0.0118 0.0254  56  ARG B CG  
5211  C CD  . ARG B 64  ? 0.1673 0.1604 0.2911 -0.0001 -0.0163 0.0256  56  ARG B CD  
5212  N NE  . ARG B 64  ? 0.1982 0.1859 0.3210 0.0033  -0.0174 0.0191  56  ARG B NE  
5213  C CZ  . ARG B 64  ? 0.1537 0.1319 0.2778 0.0038  -0.0214 0.0171  56  ARG B CZ  
5214  N NH1 . ARG B 64  ? 0.1388 0.1117 0.2663 0.0004  -0.0253 0.0214  56  ARG B NH1 
5215  N NH2 . ARG B 64  ? 0.1839 0.1578 0.3060 0.0077  -0.0213 0.0109  56  ARG B NH2 
5216  N N   . PHE B 65  ? 0.1443 0.1669 0.2634 -0.0058 -0.0025 0.0372  57  PHE B N   
5217  C CA  . PHE B 65  ? 0.1119 0.1417 0.2274 -0.0052 0.0019  0.0392  57  PHE B CA  
5218  C C   . PHE B 65  ? 0.1375 0.1690 0.2476 -0.0022 0.0033  0.0338  57  PHE B C   
5219  O O   . PHE B 65  ? 0.1113 0.1413 0.2220 -0.0016 0.0025  0.0290  57  PHE B O   
5220  C CB  . PHE B 65  ? 0.1198 0.1549 0.2402 -0.0074 0.0039  0.0415  57  PHE B CB  
5221  C CG  . PHE B 65  ? 0.1950 0.2373 0.3116 -0.0059 0.0089  0.0429  57  PHE B CG  
5222  C CD1 . PHE B 65  ? 0.1029 0.1479 0.2165 -0.0057 0.0120  0.0483  57  PHE B CD1 
5223  C CD2 . PHE B 65  ? 0.0928 0.1384 0.2078 -0.0042 0.0104  0.0388  57  PHE B CD2 
5224  C CE1 . PHE B 65  ? 0.1505 0.2013 0.2592 -0.0034 0.0168  0.0491  57  PHE B CE1 
5225  C CE2 . PHE B 65  ? 0.1469 0.1980 0.2580 -0.0021 0.0148  0.0397  57  PHE B CE2 
5226  C CZ  . PHE B 65  ? 0.1077 0.1615 0.2155 -0.0016 0.0181  0.0445  57  PHE B CZ  
5227  N N   . VAL B 66  ? 0.1319 0.1660 0.2363 -0.0003 0.0053  0.0347  58  VAL B N   
5228  C CA  . VAL B 66  ? 0.1158 0.1512 0.2156 0.0021  0.0062  0.0300  58  VAL B CA  
5229  C C   . VAL B 66  ? 0.1495 0.1893 0.2440 0.0032  0.0097  0.0314  58  VAL B C   
5230  O O   . VAL B 66  ? 0.1132 0.1538 0.2035 0.0037  0.0109  0.0353  58  VAL B O   
5231  C CB  . VAL B 66  ? 0.0961 0.1287 0.1939 0.0039  0.0036  0.0286  58  VAL B CB  
5232  C CG1 . VAL B 66  ? 0.1045 0.1390 0.1980 0.0057  0.0044  0.0248  58  VAL B CG1 
5233  C CG2 . VAL B 66  ? 0.0989 0.1272 0.2020 0.0039  0.0009  0.0261  58  VAL B CG2 
5234  N N   . LEU B 67  ? 0.1596 0.2016 0.2534 0.0039  0.0114  0.0281  59  LEU B N   
5235  C CA  . LEU B 67  ? 0.1082 0.1535 0.1965 0.0057  0.0145  0.0281  59  LEU B CA  
5236  C C   . LEU B 67  ? 0.1425 0.1855 0.2250 0.0076  0.0132  0.0242  59  LEU B C   
5237  O O   . LEU B 67  ? 0.1526 0.1947 0.2357 0.0078  0.0128  0.0202  59  LEU B O   
5238  C CB  . LEU B 67  ? 0.1272 0.1756 0.2187 0.0056  0.0164  0.0270  59  LEU B CB  
5239  C CG  . LEU B 67  ? 0.1501 0.2014 0.2365 0.0083  0.0196  0.0263  59  LEU B CG  
5240  C CD1 . LEU B 67  ? 0.1082 0.1637 0.1935 0.0090  0.0233  0.0312  59  LEU B CD1 
5241  C CD2 . LEU B 67  ? 0.1740 0.2267 0.2634 0.0086  0.0201  0.0239  59  LEU B CD2 
5242  N N   . SER B 68  ? 0.1282 0.1698 0.2050 0.0089  0.0122  0.0256  60  SER B N   
5243  C CA  . SER B 68  ? 0.1423 0.1814 0.2151 0.0103  0.0095  0.0219  60  SER B CA  
5244  C C   . SER B 68  ? 0.1495 0.1888 0.2166 0.0120  0.0111  0.0190  60  SER B C   
5245  O O   . SER B 68  ? 0.1812 0.2188 0.2487 0.0119  0.0093  0.0151  60  SER B O   
5246  C CB  . SER B 68  ? 0.1316 0.1684 0.1992 0.0113  0.0068  0.0242  60  SER B CB  
5247  O OG  . SER B 68  ? 0.1656 0.2002 0.2323 0.0120  0.0028  0.0206  60  SER B OG  
5248  N N   . ASN B 69  ? 0.1959 0.2373 0.2584 0.0135  0.0147  0.0210  61  ASN B N   
5249  C CA  . ASN B 69  ? 0.2277 0.2687 0.2851 0.0157  0.0164  0.0179  61  ASN B CA  
5250  C C   . ASN B 69  ? 0.1593 0.2023 0.2237 0.0146  0.0178  0.0165  61  ASN B C   
5251  O O   . ASN B 69  ? 0.2040 0.2507 0.2707 0.0153  0.0210  0.0183  61  ASN B O   
5252  C CB  . ASN B 69  ? 0.2389 0.2814 0.2883 0.0188  0.0201  0.0202  61  ASN B CB  
5253  C CG  . ASN B 69  ? 0.2037 0.2508 0.2569 0.0177  0.0235  0.0262  61  ASN B CG  
5254  O OD1 . ASN B 69  ? 0.3012 0.3498 0.3633 0.0147  0.0225  0.0282  61  ASN B OD1 
5255  N ND2 . ASN B 69  ? 0.2487 0.2976 0.2949 0.0204  0.0277  0.0290  61  ASN B ND2 
5256  N N   . GLY B 70  ? 0.2245 0.2651 0.2924 0.0130  0.0154  0.0134  62  GLY B N   
5257  C CA  . GLY B 70  ? 0.1873 0.2285 0.2611 0.0115  0.0159  0.0125  62  GLY B CA  
5258  C C   . GLY B 70  ? 0.2606 0.3020 0.3328 0.0131  0.0177  0.0111  62  GLY B C   
5259  O O   . GLY B 70  ? 0.2266 0.2691 0.3030 0.0123  0.0182  0.0115  62  GLY B O   
5260  N N   . HIS B 71  ? 0.2001 0.2397 0.2657 0.0156  0.0181  0.0094  63  HIS B N   
5261  C CA  . HIS B 71  ? 0.2612 0.3005 0.3250 0.0179  0.0198  0.0081  63  HIS B CA  
5262  C C   . HIS B 71  ? 0.2384 0.2836 0.3065 0.0190  0.0228  0.0113  63  HIS B C   
5263  O O   . HIS B 71  ? 0.2647 0.3108 0.3354 0.0200  0.0235  0.0108  63  HIS B O   
5264  C CB  . HIS B 71  ? 0.2997 0.3353 0.3547 0.0210  0.0197  0.0056  63  HIS B CB  
5265  C CG  . HIS B 71  ? 0.2875 0.3244 0.3368 0.0228  0.0208  0.0073  63  HIS B CG  
5266  N ND1 . HIS B 71  ? 0.3005 0.3346 0.3462 0.0217  0.0177  0.0069  63  HIS B ND1 
5267  C CD2 . HIS B 71  ? 0.3482 0.3890 0.3947 0.0256  0.0247  0.0098  63  HIS B CD2 
5268  C CE1 . HIS B 71  ? 0.3773 0.4124 0.4166 0.0239  0.0194  0.0090  63  HIS B CE1 
5269  N NE2 . HIS B 71  ? 0.3169 0.3563 0.3564 0.0263  0.0242  0.0110  63  HIS B NE2 
5270  N N   . ALA B 72  ? 0.1473 0.1965 0.2166 0.0187  0.0245  0.0148  64  ALA B N   
5271  C CA  . ALA B 72  ? 0.0948 0.1506 0.1704 0.0189  0.0275  0.0188  64  ALA B CA  
5272  C C   . ALA B 72  ? 0.1032 0.1606 0.1883 0.0156  0.0254  0.0200  64  ALA B C   
5273  O O   . ALA B 72  ? 0.1103 0.1723 0.2022 0.0138  0.0262  0.0239  64  ALA B O   
5274  C CB  . ALA B 72  ? 0.0990 0.1577 0.1728 0.0189  0.0299  0.0229  64  ALA B CB  
5275  N N   . SER B 73  ? 0.1123 0.1653 0.1971 0.0147  0.0226  0.0167  65  SER B N   
5276  C CA  . SER B 73  ? 0.1686 0.2207 0.2591 0.0118  0.0199  0.0169  65  SER B CA  
5277  C C   . SER B 73  ? 0.0804 0.1378 0.1791 0.0114  0.0200  0.0197  65  SER B C   
5278  O O   . SER B 73  ? 0.1106 0.1683 0.2150 0.0086  0.0177  0.0212  65  SER B O   
5279  C CB  . SER B 73  ? 0.1746 0.2212 0.2617 0.0117  0.0180  0.0133  65  SER B CB  
5280  O OG  . SER B 73  ? 0.1710 0.2173 0.2559 0.0143  0.0188  0.0120  65  SER B OG  
5281  N N   . MET B 74  ? 0.0819 0.1433 0.1821 0.0142  0.0221  0.0202  66  MET B N   
5282  C CA  . MET B 74  ? 0.1041 0.1717 0.2144 0.0138  0.0217  0.0230  66  MET B CA  
5283  C C   . MET B 74  ? 0.1006 0.1742 0.2181 0.0116  0.0235  0.0278  66  MET B C   
5284  O O   . MET B 74  ? 0.0852 0.1630 0.2130 0.0094  0.0217  0.0305  66  MET B O   
5285  C CB  . MET B 74  ? 0.0933 0.1650 0.2052 0.0179  0.0240  0.0226  66  MET B CB  
5286  C CG  . MET B 74  ? 0.0831 0.1497 0.1927 0.0192  0.0205  0.0194  66  MET B CG  
5287  S SD  . MET B 74  ? 0.1322 0.1971 0.2482 0.0155  0.0144  0.0199  66  MET B SD  
5288  C CE  . MET B 74  ? 0.0923 0.1687 0.2239 0.0145  0.0152  0.0249  66  MET B CE  
5289  N N   . LEU B 75  ? 0.1164 0.1899 0.2289 0.0119  0.0266  0.0293  67  LEU B N   
5290  C CA  . LEU B 75  ? 0.0961 0.1738 0.2146 0.0093  0.0280  0.0345  67  LEU B CA  
5291  C C   . LEU B 75  ? 0.0958 0.1694 0.2189 0.0049  0.0229  0.0347  67  LEU B C   
5292  O O   . LEU B 75  ? 0.1187 0.1959 0.2520 0.0019  0.0216  0.0382  67  LEU B O   
5293  C CB  . LEU B 75  ? 0.0891 0.1656 0.1987 0.0106  0.0314  0.0359  67  LEU B CB  
5294  C CG  . LEU B 75  ? 0.1339 0.2135 0.2485 0.0077  0.0329  0.0419  67  LEU B CG  
5295  C CD1 . LEU B 75  ? 0.1136 0.2032 0.2373 0.0083  0.0380  0.0470  67  LEU B CD1 
5296  C CD2 . LEU B 75  ? 0.1606 0.2363 0.2647 0.0086  0.0343  0.0431  67  LEU B CD2 
5297  N N   . LEU B 76  ? 0.1161 0.1820 0.2322 0.0045  0.0199  0.0308  68  LEU B N   
5298  C CA  . LEU B 76  ? 0.1235 0.1846 0.2426 0.0013  0.0154  0.0302  68  LEU B CA  
5299  C C   . LEU B 76  ? 0.1176 0.1783 0.2423 0.0001  0.0116  0.0289  68  LEU B C   
5300  O O   . LEU B 76  ? 0.1300 0.1901 0.2616 -0.0029 0.0082  0.0307  68  LEU B O   
5301  C CB  . LEU B 76  ? 0.0798 0.1338 0.1907 0.0019  0.0140  0.0262  68  LEU B CB  
5302  C CG  . LEU B 76  ? 0.0805 0.1286 0.1928 -0.0004 0.0099  0.0248  68  LEU B CG  
5303  C CD1 . LEU B 76  ? 0.1381 0.1869 0.2568 -0.0030 0.0088  0.0293  68  LEU B CD1 
5304  C CD2 . LEU B 76  ? 0.0803 0.1233 0.1861 0.0008  0.0097  0.0213  68  LEU B CD2 
5305  N N   . TYR B 77  ? 0.0938 0.1540 0.2152 0.0025  0.0115  0.0258  69  TYR B N   
5306  C CA  . TYR B 77  ? 0.0980 0.1571 0.2233 0.0017  0.0072  0.0247  69  TYR B CA  
5307  C C   . TYR B 77  ? 0.0789 0.1457 0.2170 0.0002  0.0064  0.0289  69  TYR B C   
5308  O O   . TYR B 77  ? 0.1128 0.1781 0.2568 -0.0023 0.0012  0.0291  69  TYR B O   
5309  C CB  . TYR B 77  ? 0.0920 0.1490 0.2112 0.0047  0.0074  0.0214  69  TYR B CB  
5310  C CG  . TYR B 77  ? 0.0901 0.1397 0.1985 0.0055  0.0079  0.0176  69  TYR B CG  
5311  C CD1 . TYR B 77  ? 0.1213 0.1655 0.2266 0.0037  0.0064  0.0162  69  TYR B CD1 
5312  C CD2 . TYR B 77  ? 0.1189 0.1669 0.2211 0.0082  0.0099  0.0156  69  TYR B CD2 
5313  C CE1 . TYR B 77  ? 0.1062 0.1451 0.2036 0.0044  0.0075  0.0130  69  TYR B CE1 
5314  C CE2 . TYR B 77  ? 0.0976 0.1395 0.1917 0.0083  0.0105  0.0126  69  TYR B CE2 
5315  C CZ  . TYR B 77  ? 0.1022 0.1403 0.1946 0.0064  0.0096  0.0116  69  TYR B CZ  
5316  O OH  . TYR B 77  ? 0.0949 0.1284 0.1811 0.0065  0.0107  0.0090  69  TYR B OH  
5317  N N   . SER B 78  ? 0.0883 0.1633 0.2307 0.0016  0.0115  0.0324  70  SER B N   
5318  C CA  . SER B 78  ? 0.1352 0.2192 0.2918 -0.0001 0.0120  0.0373  70  SER B CA  
5319  C C   . SER B 78  ? 0.1502 0.2328 0.3132 -0.0050 0.0092  0.0405  70  SER B C   
5320  O O   . SER B 78  ? 0.1057 0.1900 0.2795 -0.0081 0.0045  0.0422  70  SER B O   
5321  C CB  . SER B 78  ? 0.1048 0.1976 0.2633 0.0028  0.0195  0.0407  70  SER B CB  
5322  O OG  . SER B 78  ? 0.1238 0.2183 0.2785 0.0076  0.0215  0.0379  70  SER B OG  
5323  N N   . LEU B 79  ? 0.1516 0.2305 0.3082 -0.0057 0.0114  0.0414  71  LEU B N   
5324  C CA  . LEU B 79  ? 0.0953 0.1717 0.2574 -0.0101 0.0088  0.0447  71  LEU B CA  
5325  C C   . LEU B 79  ? 0.0855 0.1535 0.2481 -0.0125 0.0010  0.0412  71  LEU B C   
5326  O O   . LEU B 79  ? 0.1221 0.1898 0.2945 -0.0165 -0.0032 0.0438  71  LEU B O   
5327  C CB  . LEU B 79  ? 0.0855 0.1578 0.2386 -0.0095 0.0118  0.0454  71  LEU B CB  
5328  C CG  . LEU B 79  ? 0.1297 0.2092 0.2812 -0.0075 0.0191  0.0497  71  LEU B CG  
5329  C CD1 . LEU B 79  ? 0.0894 0.1634 0.2290 -0.0059 0.0208  0.0490  71  LEU B CD1 
5330  C CD2 . LEU B 79  ? 0.1503 0.2373 0.3144 -0.0108 0.0214  0.0571  71  LEU B CD2 
5331  N N   . LEU B 80  ? 0.0849 0.1456 0.2367 -0.0102 -0.0009 0.0353  72  LEU B N   
5332  C CA  . LEU B 80  ? 0.0897 0.1414 0.2392 -0.0116 -0.0076 0.0315  72  LEU B CA  
5333  C C   . LEU B 80  ? 0.0904 0.1442 0.2481 -0.0130 -0.0128 0.0316  72  LEU B C   
5334  O O   . LEU B 80  ? 0.1373 0.1867 0.3001 -0.0162 -0.0191 0.0316  72  LEU B O   
5335  C CB  . LEU B 80  ? 0.0896 0.1343 0.2257 -0.0085 -0.0070 0.0258  72  LEU B CB  
5336  C CG  . LEU B 80  ? 0.1304 0.1725 0.2601 -0.0074 -0.0034 0.0253  72  LEU B CG  
5337  C CD1 . LEU B 80  ? 0.1571 0.1949 0.2759 -0.0044 -0.0017 0.0204  72  LEU B CD1 
5338  C CD2 . LEU B 80  ? 0.1117 0.1478 0.2436 -0.0098 -0.0069 0.0259  72  LEU B CD2 
5339  N N   . HIS B 81  ? 0.0875 0.1478 0.2470 -0.0106 -0.0108 0.0317  73  HIS B N   
5340  C CA  . HIS B 81  ? 0.0921 0.1553 0.2606 -0.0116 -0.0162 0.0322  73  HIS B CA  
5341  C C   . HIS B 81  ? 0.1145 0.1852 0.3002 -0.0159 -0.0178 0.0379  73  HIS B C   
5342  O O   . HIS B 81  ? 0.1360 0.2041 0.3291 -0.0191 -0.0254 0.0379  73  HIS B O   
5343  C CB  . HIS B 81  ? 0.0866 0.1560 0.2550 -0.0077 -0.0134 0.0317  73  HIS B CB  
5344  C CG  . HIS B 81  ? 0.0886 0.1627 0.2685 -0.0083 -0.0190 0.0329  73  HIS B CG  
5345  N ND1 . HIS B 81  ? 0.1433 0.2095 0.3204 -0.0094 -0.0276 0.0297  73  HIS B ND1 
5346  C CD2 . HIS B 81  ? 0.1558 0.2419 0.3507 -0.0080 -0.0174 0.0370  73  HIS B CD2 
5347  C CE1 . HIS B 81  ? 0.1562 0.2292 0.3464 -0.0098 -0.0320 0.0318  73  HIS B CE1 
5348  N NE2 . HIS B 81  ? 0.1380 0.2237 0.3401 -0.0090 -0.0257 0.0363  73  HIS B NE2 
5349  N N   . LEU B 82  ? 0.1101 0.1897 0.3020 -0.0160 -0.0107 0.0429  74  LEU B N   
5350  C CA  . LEU B 82  ? 0.1101 0.1989 0.3198 -0.0200 -0.0106 0.0495  74  LEU B CA  
5351  C C   . LEU B 82  ? 0.1378 0.2197 0.3517 -0.0254 -0.0160 0.0511  74  LEU B C   
5352  O O   . LEU B 82  ? 0.1651 0.2503 0.3937 -0.0297 -0.0206 0.0546  74  LEU B O   
5353  C CB  . LEU B 82  ? 0.1010 0.1999 0.3133 -0.0183 -0.0007 0.0545  74  LEU B CB  
5354  C CG  . LEU B 82  ? 0.1068 0.2145 0.3197 -0.0132 0.0046  0.0540  74  LEU B CG  
5355  C CD1 . LEU B 82  ? 0.0819 0.1938 0.2878 -0.0101 0.0143  0.0563  74  LEU B CD1 
5356  C CD2 . LEU B 82  ? 0.1260 0.2409 0.3512 -0.0140 0.0030  0.0566  74  LEU B CD2 
5357  N N   . THR B 83  ? 0.1202 0.1921 0.3217 -0.0251 -0.0158 0.0487  75  THR B N   
5358  C CA  . THR B 83  ? 0.1594 0.2240 0.3645 -0.0297 -0.0205 0.0503  75  THR B CA  
5359  C C   . THR B 83  ? 0.1754 0.2285 0.3770 -0.0309 -0.0303 0.0447  75  THR B C   
5360  O O   . THR B 83  ? 0.1729 0.2189 0.3785 -0.0347 -0.0358 0.0455  75  THR B O   
5361  C CB  . THR B 83  ? 0.1567 0.2159 0.3516 -0.0287 -0.0162 0.0507  75  THR B CB  
5362  O OG1 . THR B 83  ? 0.1331 0.1860 0.3123 -0.0240 -0.0151 0.0443  75  THR B OG1 
5363  C CG2 . THR B 83  ? 0.0985 0.1680 0.2971 -0.0283 -0.0074 0.0573  75  THR B CG2 
5364  N N   . GLY B 84  ? 0.1061 0.1567 0.3002 -0.0276 -0.0329 0.0394  76  GLY B N   
5365  C CA  . GLY B 84  ? 0.2055 0.2461 0.3962 -0.0285 -0.0423 0.0345  76  GLY B CA  
5366  C C   . GLY B 84  ? 0.2074 0.2354 0.3795 -0.0250 -0.0434 0.0275  76  GLY B C   
5367  O O   . GLY B 84  ? 0.1865 0.2036 0.3538 -0.0258 -0.0511 0.0234  76  GLY B O   
5368  N N   . TYR B 85  ? 0.1725 0.2013 0.3340 -0.0211 -0.0359 0.0260  77  TYR B N   
5369  C CA  . TYR B 85  ? 0.1508 0.1697 0.2961 -0.0176 -0.0358 0.0198  77  TYR B CA  
5370  C C   . TYR B 85  ? 0.1449 0.1615 0.2835 -0.0153 -0.0390 0.0162  77  TYR B C   
5371  O O   . TYR B 85  ? 0.1212 0.1450 0.2677 -0.0158 -0.0405 0.0184  77  TYR B O   
5372  C CB  . TYR B 85  ? 0.1482 0.1700 0.2865 -0.0146 -0.0274 0.0198  77  TYR B CB  
5373  C CG  . TYR B 85  ? 0.1081 0.1287 0.2488 -0.0160 -0.0252 0.0223  77  TYR B CG  
5374  C CD1 . TYR B 85  ? 0.1051 0.1334 0.2568 -0.0187 -0.0229 0.0286  77  TYR B CD1 
5375  C CD2 . TYR B 85  ? 0.1720 0.1836 0.3041 -0.0142 -0.0254 0.0185  77  TYR B CD2 
5376  C CE1 . TYR B 85  ? 0.1567 0.1830 0.3097 -0.0199 -0.0214 0.0314  77  TYR B CE1 
5377  C CE2 . TYR B 85  ? 0.1707 0.1806 0.3052 -0.0151 -0.0242 0.0209  77  TYR B CE2 
5378  C CZ  . TYR B 85  ? 0.1987 0.2156 0.3432 -0.0181 -0.0225 0.0274  77  TYR B CZ  
5379  O OH  . TYR B 85  ? 0.1932 0.2076 0.3392 -0.0189 -0.0217 0.0303  77  TYR B OH  
5380  N N   . ASN B 86  ? 0.1360 0.1425 0.2598 -0.0126 -0.0397 0.0107  78  ASN B N   
5381  C CA  . ASN B 86  ? 0.1974 0.1995 0.3113 -0.0100 -0.0423 0.0073  78  ASN B CA  
5382  C C   . ASN B 86  ? 0.2565 0.2653 0.3667 -0.0071 -0.0350 0.0081  78  ASN B C   
5383  O O   . ASN B 86  ? 0.2783 0.2823 0.3760 -0.0043 -0.0314 0.0051  78  ASN B O   
5384  C CB  . ASN B 86  ? 0.2936 0.2823 0.3923 -0.0080 -0.0449 0.0015  78  ASN B CB  
5385  C CG  . ASN B 86  ? 0.4462 0.4288 0.5333 -0.0057 -0.0484 -0.0016 78  ASN B CG  
5386  O OD1 . ASN B 86  ? 0.5102 0.4968 0.6027 -0.0064 -0.0526 0.0002  78  ASN B OD1 
5387  N ND2 . ASN B 86  ? 0.5355 0.5082 0.6063 -0.0027 -0.0468 -0.0061 78  ASN B ND2 
5388  N N   . LEU B 87  ? 0.1749 0.1948 0.2968 -0.0079 -0.0326 0.0125  79  LEU B N   
5389  C CA  . LEU B 87  ? 0.1629 0.1889 0.2829 -0.0051 -0.0271 0.0134  79  LEU B CA  
5390  C C   . LEU B 87  ? 0.1863 0.2203 0.3181 -0.0056 -0.0302 0.0163  79  LEU B C   
5391  O O   . LEU B 87  ? 0.1435 0.1856 0.2893 -0.0080 -0.0302 0.0204  79  LEU B O   
5392  C CB  . LEU B 87  ? 0.1078 0.1398 0.2297 -0.0046 -0.0193 0.0155  79  LEU B CB  
5393  C CG  . LEU B 87  ? 0.1126 0.1477 0.2289 -0.0015 -0.0135 0.0151  79  LEU B CG  
5394  C CD1 . LEU B 87  ? 0.1315 0.1576 0.2339 0.0004  -0.0129 0.0109  79  LEU B CD1 
5395  C CD2 . LEU B 87  ? 0.1602 0.2013 0.2794 -0.0013 -0.0073 0.0175  79  LEU B CD2 
5396  N N   . SER B 88  ? 0.1630 0.1946 0.2895 -0.0032 -0.0330 0.0147  80  SER B N   
5397  C CA  . SER B 88  ? 0.1455 0.1828 0.2831 -0.0034 -0.0383 0.0167  80  SER B CA  
5398  C C   . SER B 88  ? 0.1182 0.1653 0.2615 -0.0005 -0.0329 0.0192  80  SER B C   
5399  O O   . SER B 88  ? 0.1056 0.1528 0.2415 0.0019  -0.0260 0.0185  80  SER B O   
5400  C CB  . SER B 88  ? 0.1613 0.1887 0.2890 -0.0023 -0.0462 0.0134  80  SER B CB  
5401  O OG  . SER B 88  ? 0.1620 0.1848 0.2760 0.0013  -0.0426 0.0114  80  SER B OG  
5402  N N   . ILE B 89  ? 0.1310 0.1860 0.2878 -0.0004 -0.0366 0.0217  81  ILE B N   
5403  C CA  . ILE B 89  ? 0.1211 0.1842 0.2828 0.0035  -0.0324 0.0233  81  ILE B CA  
5404  C C   . ILE B 89  ? 0.1851 0.2395 0.3310 0.0073  -0.0323 0.0200  81  ILE B C   
5405  O O   . ILE B 89  ? 0.1186 0.1749 0.2605 0.0104  -0.0259 0.0199  81  ILE B O   
5406  C CB  . ILE B 89  ? 0.1680 0.2409 0.3479 0.0033  -0.0375 0.0265  81  ILE B CB  
5407  C CG1 . ILE B 89  ? 0.1349 0.2202 0.3324 0.0004  -0.0334 0.0313  81  ILE B CG1 
5408  C CG2 . ILE B 89  ? 0.2360 0.3133 0.4173 0.0085  -0.0359 0.0266  81  ILE B CG2 
5409  C CD1 . ILE B 89  ? 0.1364 0.2291 0.3339 0.0032  -0.0225 0.0331  81  ILE B CD1 
5410  N N   . GLU B 90  ? 0.1755 0.2194 0.3112 0.0071  -0.0392 0.0173  82  GLU B N   
5411  C CA  . GLU B 90  ? 0.1785 0.2132 0.2982 0.0102  -0.0386 0.0148  82  GLU B CA  
5412  C C   . GLU B 90  ? 0.1144 0.1447 0.2225 0.0103  -0.0308 0.0132  82  GLU B C   
5413  O O   . GLU B 90  ? 0.1556 0.1832 0.2559 0.0129  -0.0270 0.0125  82  GLU B O   
5414  C CB  . GLU B 90  ? 0.2707 0.2941 0.3797 0.0099  -0.0471 0.0125  82  GLU B CB  
5415  C CG  . GLU B 90  ? 0.4539 0.4807 0.5734 0.0105  -0.0561 0.0139  82  GLU B CG  
5416  C CD  . GLU B 90  ? 0.4891 0.5226 0.6153 0.0146  -0.0544 0.0159  82  GLU B CD  
5417  O OE1 . GLU B 90  ? 0.4454 0.4724 0.5589 0.0176  -0.0516 0.0148  82  GLU B OE1 
5418  O OE2 . GLU B 90  ? 0.5329 0.5784 0.6778 0.0148  -0.0557 0.0186  82  GLU B OE2 
5419  N N   . ASP B 91  ? 0.1118 0.1413 0.2195 0.0074  -0.0287 0.0126  83  ASP B N   
5420  C CA  . ASP B 91  ? 0.1379 0.1652 0.2376 0.0076  -0.0215 0.0114  83  ASP B CA  
5421  C C   . ASP B 91  ? 0.1410 0.1767 0.2467 0.0094  -0.0153 0.0133  83  ASP B C   
5422  O O   . ASP B 91  ? 0.1574 0.1904 0.2553 0.0112  -0.0110 0.0122  83  ASP B O   
5423  C CB  . ASP B 91  ? 0.1417 0.1673 0.2417 0.0047  -0.0210 0.0108  83  ASP B CB  
5424  C CG  . ASP B 91  ? 0.1677 0.1827 0.2580 0.0038  -0.0262 0.0078  83  ASP B CG  
5425  O OD1 . ASP B 91  ? 0.2063 0.2135 0.2844 0.0056  -0.0273 0.0058  83  ASP B OD1 
5426  O OD2 . ASP B 91  ? 0.1560 0.1696 0.2500 0.0014  -0.0292 0.0075  83  ASP B OD2 
5427  N N   . LEU B 92  ? 0.1220 0.1679 0.2415 0.0090  -0.0147 0.0163  84  LEU B N   
5428  C CA  . LEU B 92  ? 0.1129 0.1664 0.2367 0.0114  -0.0084 0.0179  84  LEU B CA  
5429  C C   . LEU B 92  ? 0.1397 0.1924 0.2607 0.0155  -0.0083 0.0171  84  LEU B C   
5430  O O   . LEU B 92  ? 0.0968 0.1500 0.2139 0.0181  -0.0033 0.0164  84  LEU B O   
5431  C CB  . LEU B 92  ? 0.1135 0.1783 0.2527 0.0103  -0.0071 0.0217  84  LEU B CB  
5432  C CG  . LEU B 92  ? 0.1631 0.2285 0.3064 0.0059  -0.0077 0.0233  84  LEU B CG  
5433  C CD1 . LEU B 92  ? 0.1775 0.2548 0.3365 0.0047  -0.0051 0.0282  84  LEU B CD1 
5434  C CD2 . LEU B 92  ? 0.1295 0.1894 0.2621 0.0055  -0.0036 0.0216  84  LEU B CD2 
5435  N N   . LYS B 93  ? 0.1200 0.1707 0.2427 0.0164  -0.0144 0.0170  85  LYS B N   
5436  C CA  . LYS B 93  ? 0.1373 0.1857 0.2567 0.0206  -0.0152 0.0163  85  LYS B CA  
5437  C C   . LYS B 93  ? 0.1222 0.1592 0.2255 0.0211  -0.0140 0.0138  85  LYS B C   
5438  O O   . LYS B 93  ? 0.1223 0.1556 0.2212 0.0244  -0.0140 0.0133  85  LYS B O   
5439  C CB  . LYS B 93  ? 0.1595 0.2082 0.2849 0.0214  -0.0231 0.0172  85  LYS B CB  
5440  C CG  . LYS B 93  ? 0.1629 0.2246 0.3075 0.0216  -0.0243 0.0202  85  LYS B CG  
5441  C CD  . LYS B 93  ? 0.1818 0.2428 0.3320 0.0224  -0.0335 0.0208  85  LYS B CD  
5442  C CE  . LYS B 93  ? 0.2337 0.3089 0.4057 0.0224  -0.0352 0.0241  85  LYS B CE  
5443  N NZ  . LYS B 93  ? 0.3169 0.3908 0.4946 0.0228  -0.0457 0.0244  85  LYS B NZ  
5444  N N   . ASN B 94  ? 0.1063 0.1375 0.2013 0.0181  -0.0127 0.0124  86  ASN B N   
5445  C CA  . ASN B 94  ? 0.1102 0.1320 0.1917 0.0181  -0.0107 0.0106  86  ASN B CA  
5446  C C   . ASN B 94  ? 0.1181 0.1413 0.1979 0.0169  -0.0045 0.0098  86  ASN B C   
5447  O O   . ASN B 94  ? 0.1144 0.1313 0.1855 0.0156  -0.0026 0.0084  86  ASN B O   
5448  C CB  . ASN B 94  ? 0.1538 0.1668 0.2258 0.0163  -0.0145 0.0095  86  ASN B CB  
5449  C CG  . ASN B 94  ? 0.2308 0.2391 0.2999 0.0181  -0.0209 0.0100  86  ASN B CG  
5450  O OD1 . ASN B 94  ? 0.2849 0.2877 0.3470 0.0202  -0.0209 0.0101  86  ASN B OD1 
5451  N ND2 . ASN B 94  ? 0.2739 0.2846 0.3492 0.0174  -0.0270 0.0104  86  ASN B ND2 
5452  N N   . PHE B 95  ? 0.1271 0.1588 0.2154 0.0176  -0.0015 0.0109  87  PHE B N   
5453  C CA  . PHE B 95  ? 0.0949 0.1277 0.1811 0.0172  0.0035  0.0102  87  PHE B CA  
5454  C C   . PHE B 95  ? 0.0986 0.1244 0.1759 0.0184  0.0051  0.0084  87  PHE B C   
5455  O O   . PHE B 95  ? 0.1150 0.1385 0.1908 0.0212  0.0041  0.0083  87  PHE B O   
5456  C CB  . PHE B 95  ? 0.0913 0.1332 0.1859 0.0192  0.0064  0.0118  87  PHE B CB  
5457  C CG  . PHE B 95  ? 0.1146 0.1577 0.2063 0.0192  0.0108  0.0112  87  PHE B CG  
5458  C CD1 . PHE B 95  ? 0.0864 0.1286 0.1766 0.0161  0.0116  0.0111  87  PHE B CD1 
5459  C CD2 . PHE B 95  ? 0.1184 0.1633 0.2091 0.0227  0.0138  0.0107  87  PHE B CD2 
5460  C CE1 . PHE B 95  ? 0.1113 0.1544 0.1990 0.0164  0.0147  0.0108  87  PHE B CE1 
5461  C CE2 . PHE B 95  ? 0.1167 0.1619 0.2035 0.0230  0.0170  0.0100  87  PHE B CE2 
5462  C CZ  . PHE B 95  ? 0.0877 0.1322 0.1733 0.0197  0.0172  0.0102  87  PHE B CZ  
5463  N N   . ARG B 96  ? 0.0978 0.1200 0.1700 0.0162  0.0073  0.0072  88  ARG B N   
5464  C CA  . ARG B 96  ? 0.1063 0.1225 0.1719 0.0162  0.0090  0.0059  88  ARG B CA  
5465  C C   . ARG B 96  ? 0.1448 0.1529 0.2036 0.0164  0.0070  0.0060  88  ARG B C   
5466  O O   . ARG B 96  ? 0.1212 0.1238 0.1754 0.0168  0.0078  0.0055  88  ARG B O   
5467  C CB  . ARG B 96  ? 0.1136 0.1314 0.1801 0.0191  0.0105  0.0052  88  ARG B CB  
5468  C CG  . ARG B 96  ? 0.1183 0.1412 0.1873 0.0186  0.0131  0.0049  88  ARG B CG  
5469  C CD  . ARG B 96  ? 0.1022 0.1271 0.1708 0.0221  0.0148  0.0040  88  ARG B CD  
5470  N NE  . ARG B 96  ? 0.1091 0.1366 0.1774 0.0210  0.0165  0.0037  88  ARG B NE  
5471  C CZ  . ARG B 96  ? 0.1667 0.1898 0.2302 0.0204  0.0165  0.0018  88  ARG B CZ  
5472  N NH1 . ARG B 96  ? 0.1108 0.1269 0.1701 0.0206  0.0153  -0.0000 88  ARG B NH1 
5473  N NH2 . ARG B 96  ? 0.1752 0.2008 0.2387 0.0193  0.0172  0.0018  88  ARG B NH2 
5474  N N   . GLN B 97  ? 0.1111 0.1174 0.1683 0.0159  0.0041  0.0067  89  GLN B N   
5475  C CA  . GLN B 97  ? 0.1413 0.1391 0.1901 0.0161  0.0020  0.0071  89  GLN B CA  
5476  C C   . GLN B 97  ? 0.1621 0.1552 0.2039 0.0134  0.0037  0.0067  89  GLN B C   
5477  O O   . GLN B 97  ? 0.1511 0.1475 0.1955 0.0120  0.0044  0.0060  89  GLN B O   
5478  C CB  . GLN B 97  ? 0.1780 0.1759 0.2282 0.0181  -0.0032 0.0081  89  GLN B CB  
5479  C CG  . GLN B 97  ? 0.1502 0.1540 0.2089 0.0214  -0.0044 0.0087  89  GLN B CG  
5480  C CD  . GLN B 97  ? 0.1913 0.1914 0.2470 0.0233  -0.0021 0.0082  89  GLN B CD  
5481  O OE1 . GLN B 97  ? 0.1873 0.1787 0.2355 0.0239  -0.0035 0.0086  89  GLN B OE1 
5482  N NE2 . GLN B 97  ? 0.1278 0.1335 0.1886 0.0244  0.0012  0.0073  89  GLN B NE2 
5483  N N   . LEU B 98  ? 0.1506 0.1355 0.1834 0.0130  0.0045  0.0075  90  LEU B N   
5484  C CA  . LEU B 98  ? 0.2011 0.1815 0.2268 0.0109  0.0077  0.0074  90  LEU B CA  
5485  C C   . LEU B 98  ? 0.1754 0.1553 0.1982 0.0110  0.0053  0.0064  90  LEU B C   
5486  O O   . LEU B 98  ? 0.1435 0.1210 0.1638 0.0125  0.0002  0.0067  90  LEU B O   
5487  C CB  . LEU B 98  ? 0.1474 0.1185 0.1629 0.0107  0.0086  0.0092  90  LEU B CB  
5488  C CG  . LEU B 98  ? 0.1633 0.1305 0.1717 0.0086  0.0134  0.0097  90  LEU B CG  
5489  C CD1 . LEU B 98  ? 0.1727 0.1458 0.1892 0.0063  0.0184  0.0089  90  LEU B CD1 
5490  C CD2 . LEU B 98  ? 0.2172 0.1745 0.2144 0.0083  0.0144  0.0124  90  LEU B CD2 
5491  N N   . HIS B 99  ? 0.1498 0.1319 0.1736 0.0096  0.0085  0.0051  91  HIS B N   
5492  C CA  . HIS B 99  ? 0.2114 0.1917 0.2317 0.0097  0.0070  0.0035  91  HIS B CA  
5493  C C   . HIS B 99  ? 0.1491 0.1348 0.1781 0.0099  0.0023  0.0028  91  HIS B C   
5494  O O   . HIS B 99  ? 0.1672 0.1506 0.1937 0.0099  -0.0002 0.0013  91  HIS B O   
5495  C CB  . HIS B 99  ? 0.2291 0.1998 0.2358 0.0109  0.0044  0.0036  91  HIS B CB  
5496  C CG  . HIS B 99  ? 0.2666 0.2308 0.2633 0.0106  0.0091  0.0052  91  HIS B CG  
5497  N ND1 . HIS B 99  ? 0.3255 0.2904 0.3213 0.0093  0.0160  0.0051  91  HIS B ND1 
5498  C CD2 . HIS B 99  ? 0.2724 0.2294 0.2601 0.0113  0.0078  0.0074  91  HIS B CD2 
5499  C CE1 . HIS B 99  ? 0.2924 0.2512 0.2795 0.0089  0.0193  0.0074  91  HIS B CE1 
5500  N NE2 . HIS B 99  ? 0.3140 0.2672 0.2952 0.0101  0.0143  0.0089  91  HIS B NE2 
5501  N N   . SER B 100 ? 0.1422 0.1349 0.1812 0.0101  0.0013  0.0039  92  SER B N   
5502  C CA  . SER B 100 ? 0.1332 0.1314 0.1810 0.0099  -0.0027 0.0040  92  SER B CA  
5503  C C   . SER B 100 ? 0.1525 0.1545 0.2056 0.0084  -0.0006 0.0032  92  SER B C   
5504  O O   . SER B 100 ? 0.1392 0.1413 0.1911 0.0078  0.0039  0.0024  92  SER B O   
5505  C CB  . SER B 100 ? 0.1141 0.1192 0.1709 0.0111  -0.0032 0.0058  92  SER B CB  
5506  O OG  . SER B 100 ? 0.1276 0.1382 0.1896 0.0107  0.0012  0.0060  92  SER B OG  
5507  N N   . LYS B 101 ? 0.1450 0.1499 0.2048 0.0076  -0.0045 0.0035  93  LYS B N   
5508  C CA  . LYS B 101 ? 0.1468 0.1553 0.2128 0.0062  -0.0032 0.0034  93  LYS B CA  
5509  C C   . LYS B 101 ? 0.0988 0.1159 0.1741 0.0060  -0.0006 0.0056  93  LYS B C   
5510  O O   . LYS B 101 ? 0.1287 0.1491 0.2096 0.0048  0.0001  0.0063  93  LYS B O   
5511  C CB  . LYS B 101 ? 0.2031 0.2099 0.2722 0.0050  -0.0088 0.0031  93  LYS B CB  
5512  C CG  . LYS B 101 ? 0.2583 0.2552 0.3162 0.0055  -0.0108 -0.0000 93  LYS B CG  
5513  C CD  . LYS B 101 ? 0.3791 0.3730 0.4399 0.0043  -0.0174 -0.0008 93  LYS B CD  
5514  C CE  . LYS B 101 ? 0.5391 0.5220 0.5870 0.0055  -0.0193 -0.0046 93  LYS B CE  
5515  N NZ  . LYS B 101 ? 0.5951 0.5736 0.6454 0.0041  -0.0267 -0.0059 93  LYS B NZ  
5516  N N   . THR B 102 ? 0.0969 0.1167 0.1727 0.0074  0.0009  0.0066  94  THR B N   
5517  C CA  . THR B 102 ? 0.0908 0.1178 0.1731 0.0080  0.0036  0.0083  94  THR B CA  
5518  C C   . THR B 102 ? 0.1223 0.1477 0.1996 0.0092  0.0072  0.0073  94  THR B C   
5519  O O   . THR B 102 ? 0.1171 0.1439 0.1947 0.0112  0.0077  0.0077  94  THR B O   
5520  C CB  . THR B 102 ? 0.0902 0.1225 0.1796 0.0091  0.0016  0.0103  94  THR B CB  
5521  O OG1 . THR B 102 ? 0.0954 0.1233 0.1802 0.0106  -0.0011 0.0096  94  THR B OG1 
5522  C CG2 . THR B 102 ? 0.1230 0.1587 0.2207 0.0070  -0.0018 0.0120  94  THR B CG2 
5523  N N   . PRO B 103 ? 0.1725 0.1949 0.2459 0.0082  0.0094  0.0059  95  PRO B N   
5524  C CA  . PRO B 103 ? 0.1044 0.1255 0.1748 0.0087  0.0120  0.0051  95  PRO B CA  
5525  C C   . PRO B 103 ? 0.0974 0.1236 0.1715 0.0097  0.0133  0.0058  95  PRO B C   
5526  O O   . PRO B 103 ? 0.1182 0.1493 0.1971 0.0097  0.0132  0.0072  95  PRO B O   
5527  C CB  . PRO B 103 ? 0.0949 0.1136 0.1633 0.0071  0.0139  0.0038  95  PRO B CB  
5528  C CG  . PRO B 103 ? 0.0892 0.1097 0.1610 0.0063  0.0127  0.0040  95  PRO B CG  
5529  C CD  . PRO B 103 ? 0.1466 0.1665 0.2188 0.0067  0.0094  0.0048  95  PRO B CD  
5530  N N   . GLY B 104 ? 0.1591 0.1833 0.2301 0.0107  0.0144  0.0048  96  GLY B N   
5531  C CA  . GLY B 104 ? 0.1251 0.1524 0.1969 0.0126  0.0154  0.0049  96  GLY B CA  
5532  C C   . GLY B 104 ? 0.1346 0.1655 0.2085 0.0117  0.0161  0.0054  96  GLY B C   
5533  O O   . GLY B 104 ? 0.0964 0.1310 0.1710 0.0134  0.0171  0.0064  96  GLY B O   
5534  N N   . HIS B 105 ? 0.1387 0.1282 0.1573 0.0219  0.0027  0.0433  97  HIS B N   
5535  C CA  . HIS B 105 ? 0.1293 0.1245 0.1524 0.0179  0.0041  0.0407  97  HIS B CA  
5536  C C   . HIS B 105 ? 0.1244 0.1280 0.1525 0.0142  0.0005  0.0401  97  HIS B C   
5537  O O   . HIS B 105 ? 0.1451 0.1472 0.1688 0.0128  -0.0022 0.0405  97  HIS B O   
5538  C CB  . HIS B 105 ? 0.1584 0.1453 0.1732 0.0140  0.0066  0.0382  97  HIS B CB  
5539  C CG  . HIS B 105 ? 0.1938 0.1718 0.2032 0.0170  0.0100  0.0378  97  HIS B CG  
5540  N ND1 . HIS B 105 ? 0.2876 0.2533 0.2879 0.0183  0.0101  0.0385  97  HIS B ND1 
5541  C CD2 . HIS B 105 ? 0.2400 0.2192 0.2515 0.0193  0.0132  0.0367  97  HIS B CD2 
5542  C CE1 . HIS B 105 ? 0.2211 0.1799 0.2179 0.0213  0.0132  0.0372  97  HIS B CE1 
5543  N NE2 . HIS B 105 ? 0.2405 0.2080 0.2438 0.0221  0.0152  0.0359  97  HIS B NE2 
5544  N N   . PRO B 106 ? 0.1343 0.1461 0.1709 0.0128  0.0004  0.0394  98  PRO B N   
5545  C CA  . PRO B 106 ? 0.1394 0.1580 0.1810 0.0098  -0.0036 0.0386  98  PRO B CA  
5546  C C   . PRO B 106 ? 0.1505 0.1653 0.1854 0.0058  -0.0044 0.0357  98  PRO B C   
5547  O O   . PRO B 106 ? 0.1458 0.1566 0.1769 0.0041  -0.0019 0.0341  98  PRO B O   
5548  C CB  . PRO B 106 ? 0.1480 0.1733 0.1989 0.0085  -0.0027 0.0386  98  PRO B CB  
5549  C CG  . PRO B 106 ? 0.1890 0.2140 0.2410 0.0120  0.0015  0.0403  98  PRO B CG  
5550  C CD  . PRO B 106 ? 0.1829 0.1974 0.2242 0.0133  0.0037  0.0393  98  PRO B CD  
5551  N N   . GLU B 107 ? 0.1112 0.1285 0.1449 0.0045  -0.0082 0.0350  99  GLU B N   
5552  C CA  . GLU B 107 ? 0.1118 0.1272 0.1389 0.0014  -0.0088 0.0321  99  GLU B CA  
5553  C C   . GLU B 107 ? 0.1155 0.1362 0.1472 -0.0006 -0.0121 0.0291  99  GLU B C   
5554  O O   . GLU B 107 ? 0.1583 0.1836 0.1937 -0.0003 -0.0158 0.0295  99  GLU B O   
5555  C CB  . GLU B 107 ? 0.1371 0.1493 0.1556 0.0016  -0.0099 0.0335  99  GLU B CB  
5556  C CG  . GLU B 107 ? 0.1654 0.1692 0.1772 0.0026  -0.0068 0.0359  99  GLU B CG  
5557  C CD  . GLU B 107 ? 0.2079 0.2076 0.2112 0.0028  -0.0082 0.0386  99  GLU B CD  
5558  O OE1 . GLU B 107 ? 0.2255 0.2293 0.2258 0.0009  -0.0106 0.0377  99  GLU B OE1 
5559  O OE2 . GLU B 107 ? 0.1857 0.1776 0.1848 0.0051  -0.0069 0.0416  99  GLU B OE2 
5560  N N   . TYR B 108 ? 0.1195 0.1393 0.1506 -0.0025 -0.0111 0.0260  100 TYR B N   
5561  C CA  . TYR B 108 ? 0.1251 0.1473 0.1583 -0.0041 -0.0141 0.0223  100 TYR B CA  
5562  C C   . TYR B 108 ? 0.1106 0.1347 0.1375 -0.0045 -0.0167 0.0204  100 TYR B C   
5563  O O   . TYR B 108 ? 0.1232 0.1461 0.1424 -0.0048 -0.0150 0.0208  100 TYR B O   
5564  C CB  . TYR B 108 ? 0.1287 0.1490 0.1612 -0.0048 -0.0121 0.0196  100 TYR B CB  
5565  C CG  . TYR B 108 ? 0.1444 0.1655 0.1768 -0.0054 -0.0150 0.0149  100 TYR B CG  
5566  C CD1 . TYR B 108 ? 0.1693 0.1896 0.2083 -0.0061 -0.0178 0.0139  100 TYR B CD1 
5567  C CD2 . TYR B 108 ? 0.1439 0.1664 0.1695 -0.0053 -0.0149 0.0116  100 TYR B CD2 
5568  C CE1 . TYR B 108 ? 0.2431 0.2621 0.2813 -0.0063 -0.0206 0.0090  100 TYR B CE1 
5569  C CE2 . TYR B 108 ? 0.2511 0.2742 0.2761 -0.0048 -0.0173 0.0066  100 TYR B CE2 
5570  C CZ  . TYR B 108 ? 0.2774 0.2977 0.3084 -0.0051 -0.0204 0.0051  100 TYR B CZ  
5571  O OH  . TYR B 108 ? 0.2753 0.2942 0.3048 -0.0044 -0.0230 -0.0004 100 TYR B OH  
5572  N N   . GLY B 109 ? 0.1127 0.1399 0.1425 -0.0052 -0.0209 0.0182  101 GLY B N   
5573  C CA  . GLY B 109 ? 0.1809 0.2101 0.2040 -0.0057 -0.0234 0.0150  101 GLY B CA  
5574  C C   . GLY B 109 ? 0.1873 0.2207 0.2111 -0.0057 -0.0281 0.0157  101 GLY B C   
5575  O O   . GLY B 109 ? 0.1808 0.2164 0.2028 -0.0067 -0.0317 0.0115  101 GLY B O   
5576  N N   . TYR B 110 ? 0.1221 0.1569 0.1483 -0.0043 -0.0282 0.0207  102 TYR B N   
5577  C CA  . TYR B 110 ? 0.1300 0.1700 0.1561 -0.0036 -0.0327 0.0223  102 TYR B CA  
5578  C C   . TYR B 110 ? 0.2025 0.2467 0.2386 -0.0023 -0.0339 0.0261  102 TYR B C   
5579  O O   . TYR B 110 ? 0.2030 0.2531 0.2403 -0.0012 -0.0379 0.0280  102 TYR B O   
5580  C CB  . TYR B 110 ? 0.1725 0.2113 0.1884 -0.0021 -0.0321 0.0252  102 TYR B CB  
5581  C CG  . TYR B 110 ? 0.2092 0.2472 0.2156 -0.0038 -0.0313 0.0214  102 TYR B CG  
5582  C CD1 . TYR B 110 ? 0.1946 0.2371 0.1977 -0.0049 -0.0354 0.0172  102 TYR B CD1 
5583  C CD2 . TYR B 110 ? 0.2076 0.2413 0.2087 -0.0045 -0.0265 0.0215  102 TYR B CD2 
5584  C CE1 . TYR B 110 ? 0.2074 0.2506 0.2019 -0.0058 -0.0343 0.0132  102 TYR B CE1 
5585  C CE2 . TYR B 110 ? 0.2553 0.2908 0.2487 -0.0060 -0.0254 0.0180  102 TYR B CE2 
5586  C CZ  . TYR B 110 ? 0.2468 0.2871 0.2368 -0.0063 -0.0291 0.0138  102 TYR B CZ  
5587  O OH  . TYR B 110 ? 0.2492 0.2926 0.2314 -0.0071 -0.0278 0.0099  102 TYR B OH  
5588  N N   . THR B 111 ? 0.1624 0.2049 0.2053 -0.0021 -0.0306 0.0274  103 THR B N   
5589  C CA  . THR B 111 ? 0.1579 0.2065 0.2119 -0.0017 -0.0315 0.0302  103 THR B CA  
5590  C C   . THR B 111 ? 0.1133 0.1622 0.1743 -0.0057 -0.0324 0.0272  103 THR B C   
5591  O O   . THR B 111 ? 0.1515 0.1946 0.2117 -0.0065 -0.0290 0.0260  103 THR B O   
5592  C CB  . THR B 111 ? 0.1325 0.1792 0.1883 0.0019  -0.0267 0.0343  103 THR B CB  
5593  O OG1 . THR B 111 ? 0.1581 0.2011 0.2058 0.0055  -0.0258 0.0369  103 THR B OG1 
5594  C CG2 . THR B 111 ? 0.1306 0.1862 0.1981 0.0028  -0.0274 0.0373  103 THR B CG2 
5595  N N   . ASP B 112 ? 0.1712 0.2264 0.2386 -0.0086 -0.0374 0.0260  104 ASP B N   
5596  C CA  . ASP B 112 ? 0.1849 0.2385 0.2584 -0.0132 -0.0389 0.0233  104 ASP B CA  
5597  C C   . ASP B 112 ? 0.1612 0.2149 0.2424 -0.0136 -0.0346 0.0270  104 ASP B C   
5598  O O   . ASP B 112 ? 0.1365 0.1975 0.2239 -0.0117 -0.0331 0.0314  104 ASP B O   
5599  C CB  . ASP B 112 ? 0.1780 0.2391 0.2580 -0.0171 -0.0452 0.0220  104 ASP B CB  
5600  C CG  . ASP B 112 ? 0.1895 0.2490 0.2613 -0.0180 -0.0500 0.0168  104 ASP B CG  
5601  O OD1 . ASP B 112 ? 0.2208 0.2744 0.2823 -0.0157 -0.0482 0.0144  104 ASP B OD1 
5602  O OD2 . ASP B 112 ? 0.2462 0.3114 0.3221 -0.0215 -0.0558 0.0149  104 ASP B OD2 
5603  N N   . GLY B 113 ? 0.1214 0.1676 0.2020 -0.0156 -0.0328 0.0251  105 GLY B N   
5604  C CA  . GLY B 113 ? 0.1721 0.2182 0.2591 -0.0165 -0.0290 0.0286  105 GLY B CA  
5605  C C   . GLY B 113 ? 0.1823 0.2244 0.2643 -0.0126 -0.0232 0.0305  105 GLY B C   
5606  O O   . GLY B 113 ? 0.1873 0.2291 0.2731 -0.0132 -0.0198 0.0331  105 GLY B O   
5607  N N   . VAL B 114 ? 0.1022 0.1416 0.1756 -0.0092 -0.0220 0.0293  106 VAL B N   
5608  C CA  . VAL B 114 ? 0.1058 0.1406 0.1734 -0.0064 -0.0170 0.0303  106 VAL B CA  
5609  C C   . VAL B 114 ? 0.1322 0.1602 0.1946 -0.0075 -0.0166 0.0267  106 VAL B C   
5610  O O   . VAL B 114 ? 0.1832 0.2093 0.2398 -0.0075 -0.0185 0.0231  106 VAL B O   
5611  C CB  . VAL B 114 ? 0.1164 0.1507 0.1772 -0.0031 -0.0161 0.0311  106 VAL B CB  
5612  C CG1 . VAL B 114 ? 0.1161 0.1442 0.1699 -0.0016 -0.0115 0.0310  106 VAL B CG1 
5613  C CG2 . VAL B 114 ? 0.1220 0.1628 0.1880 -0.0005 -0.0163 0.0348  106 VAL B CG2 
5614  N N   . GLU B 115 ? 0.0982 0.1235 0.1624 -0.0080 -0.0139 0.0277  107 GLU B N   
5615  C CA  . GLU B 115 ? 0.1231 0.1427 0.1839 -0.0084 -0.0141 0.0246  107 GLU B CA  
5616  C C   . GLU B 115 ? 0.1877 0.2053 0.2406 -0.0063 -0.0112 0.0232  107 GLU B C   
5617  O O   . GLU B 115 ? 0.1494 0.1644 0.1987 -0.0059 -0.0118 0.0199  107 GLU B O   
5618  C CB  . GLU B 115 ? 0.0998 0.1171 0.1655 -0.0098 -0.0129 0.0270  107 GLU B CB  
5619  C CG  . GLU B 115 ? 0.1026 0.1217 0.1768 -0.0134 -0.0156 0.0288  107 GLU B CG  
5620  C CD  . GLU B 115 ? 0.1675 0.1818 0.2418 -0.0157 -0.0206 0.0246  107 GLU B CD  
5621  O OE1 . GLU B 115 ? 0.1751 0.1849 0.2430 -0.0137 -0.0215 0.0201  107 GLU B OE1 
5622  O OE2 . GLU B 115 ? 0.1441 0.1593 0.2249 -0.0196 -0.0235 0.0255  107 GLU B OE2 
5623  N N   . THR B 116 ? 0.1256 0.1444 0.1758 -0.0049 -0.0082 0.0256  108 THR B N   
5624  C CA  . THR B 116 ? 0.0989 0.1156 0.1418 -0.0040 -0.0055 0.0246  108 THR B CA  
5625  C C   . THR B 116 ? 0.1639 0.1804 0.2036 -0.0028 -0.0036 0.0268  108 THR B C   
5626  O O   . THR B 116 ? 0.1393 0.1575 0.1832 -0.0016 -0.0035 0.0295  108 THR B O   
5627  C CB  . THR B 116 ? 0.0938 0.1092 0.1367 -0.0038 -0.0029 0.0251  108 THR B CB  
5628  O OG1 . THR B 116 ? 0.1457 0.1603 0.1817 -0.0037 -0.0007 0.0239  108 THR B OG1 
5629  C CG2 . THR B 116 ? 0.1433 0.1595 0.1902 -0.0032 -0.0006 0.0290  108 THR B CG2 
5630  N N   . THR B 117 ? 0.1401 0.1542 0.1722 -0.0031 -0.0024 0.0257  109 THR B N   
5631  C CA  . THR B 117 ? 0.1544 0.1652 0.1818 -0.0022 -0.0006 0.0278  109 THR B CA  
5632  C C   . THR B 117 ? 0.1533 0.1613 0.1792 -0.0017 0.0030  0.0284  109 THR B C   
5633  O O   . THR B 117 ? 0.1372 0.1449 0.1602 -0.0034 0.0041  0.0267  109 THR B O   
5634  C CB  . THR B 117 ? 0.1216 0.1305 0.1410 -0.0038 -0.0008 0.0267  109 THR B CB  
5635  O OG1 . THR B 117 ? 0.1422 0.1544 0.1620 -0.0041 -0.0041 0.0257  109 THR B OG1 
5636  C CG2 . THR B 117 ? 0.1240 0.1267 0.1375 -0.0031 0.0008  0.0292  109 THR B CG2 
5637  N N   . THR B 118 ? 0.1541 0.1609 0.1819 0.0008  0.0046  0.0308  110 THR B N   
5638  C CA  . THR B 118 ? 0.1616 0.1656 0.1869 0.0016  0.0080  0.0309  110 THR B CA  
5639  C C   . THR B 118 ? 0.2065 0.2041 0.2265 0.0040  0.0096  0.0319  110 THR B C   
5640  O O   . THR B 118 ? 0.3056 0.3020 0.3255 0.0058  0.0081  0.0334  110 THR B O   
5641  C CB  . THR B 118 ? 0.1548 0.1635 0.1870 0.0028  0.0093  0.0324  110 THR B CB  
5642  O OG1 . THR B 118 ? 0.1785 0.1913 0.2173 0.0052  0.0086  0.0348  110 THR B OG1 
5643  C CG2 . THR B 118 ? 0.1565 0.1684 0.1923 0.0005  0.0077  0.0316  110 THR B CG2 
5644  N N   . GLY B 119 ? 0.2476 0.2409 0.2630 0.0043  0.0125  0.0310  111 GLY B N   
5645  C CA  . GLY B 119 ? 0.1869 0.1713 0.1952 0.0062  0.0142  0.0310  111 GLY B CA  
5646  C C   . GLY B 119 ? 0.2289 0.2082 0.2301 0.0037  0.0163  0.0285  111 GLY B C   
5647  O O   . GLY B 119 ? 0.2436 0.2204 0.2429 0.0063  0.0189  0.0278  111 GLY B O   
5648  N N   . PRO B 120 ? 0.2052 0.1840 0.2024 -0.0013 0.0153  0.0268  112 PRO B N   
5649  C CA  . PRO B 120 ? 0.1604 0.1377 0.1525 -0.0044 0.0167  0.0243  112 PRO B CA  
5650  C C   . PRO B 120 ? 0.1362 0.1209 0.1333 -0.0028 0.0177  0.0242  112 PRO B C   
5651  O O   . PRO B 120 ? 0.2144 0.2068 0.2179 -0.0030 0.0163  0.0251  112 PRO B O   
5652  C CB  . PRO B 120 ? 0.1905 0.1709 0.1809 -0.0097 0.0150  0.0232  112 PRO B CB  
5653  C CG  . PRO B 120 ? 0.1963 0.1749 0.1869 -0.0094 0.0133  0.0251  112 PRO B CG  
5654  C CD  . PRO B 120 ? 0.2285 0.2101 0.2262 -0.0043 0.0129  0.0271  112 PRO B CD  
5655  N N   . LEU B 121 ? 0.1887 0.1703 0.1819 -0.0012 0.0202  0.0232  113 LEU B N   
5656  C CA  . LEU B 121 ? 0.1255 0.1137 0.1229 0.0012  0.0217  0.0242  113 LEU B CA  
5657  C C   . LEU B 121 ? 0.1607 0.1551 0.1587 -0.0019 0.0205  0.0236  113 LEU B C   
5658  O O   . LEU B 121 ? 0.1541 0.1476 0.1476 -0.0057 0.0194  0.0214  113 LEU B O   
5659  C CB  . LEU B 121 ? 0.1593 0.1428 0.1511 0.0042  0.0248  0.0229  113 LEU B CB  
5660  C CG  . LEU B 121 ? 0.2092 0.1879 0.2018 0.0091  0.0261  0.0238  113 LEU B CG  
5661  C CD1 . LEU B 121 ? 0.2626 0.2364 0.2492 0.0132  0.0295  0.0218  113 LEU B CD1 
5662  C CD2 . LEU B 121 ? 0.2335 0.2213 0.2370 0.0118  0.0256  0.0275  113 LEU B CD2 
5663  N N   . GLY B 122 ? 0.1282 0.1293 0.1320 -0.0003 0.0208  0.0259  114 GLY B N   
5664  C CA  . GLY B 122 ? 0.1858 0.1924 0.1905 -0.0019 0.0196  0.0261  114 GLY B CA  
5665  C C   . GLY B 122 ? 0.1238 0.1338 0.1342 -0.0030 0.0166  0.0267  114 GLY B C   
5666  O O   . GLY B 122 ? 0.1446 0.1588 0.1586 -0.0026 0.0155  0.0282  114 GLY B O   
5667  N N   . GLN B 123 ? 0.1266 0.1345 0.1374 -0.0041 0.0152  0.0255  115 GLN B N   
5668  C CA  . GLN B 123 ? 0.1295 0.1409 0.1445 -0.0048 0.0125  0.0251  115 GLN B CA  
5669  C C   . GLN B 123 ? 0.1012 0.1139 0.1238 -0.0030 0.0113  0.0274  115 GLN B C   
5670  O O   . GLN B 123 ? 0.1145 0.1294 0.1406 -0.0029 0.0090  0.0270  115 GLN B O   
5671  C CB  . GLN B 123 ? 0.1011 0.1109 0.1133 -0.0069 0.0115  0.0231  115 GLN B CB  
5672  C CG  . GLN B 123 ? 0.1487 0.1585 0.1543 -0.0103 0.0121  0.0208  115 GLN B CG  
5673  C CD  . GLN B 123 ? 0.1352 0.1440 0.1377 -0.0131 0.0114  0.0196  115 GLN B CD  
5674  O OE1 . GLN B 123 ? 0.1543 0.1679 0.1597 -0.0132 0.0099  0.0189  115 GLN B OE1 
5675  N NE2 . GLN B 123 ? 0.1133 0.1152 0.1096 -0.0154 0.0127  0.0195  115 GLN B NE2 
5676  N N   . GLY B 124 ? 0.1202 0.1318 0.1455 -0.0016 0.0125  0.0295  116 GLY B N   
5677  C CA  . GLY B 124 ? 0.1291 0.1429 0.1622 -0.0010 0.0111  0.0318  116 GLY B CA  
5678  C C   . GLY B 124 ? 0.1599 0.1755 0.1960 -0.0011 0.0108  0.0338  116 GLY B C   
5679  O O   . GLY B 124 ? 0.1124 0.1279 0.1528 -0.0017 0.0081  0.0339  116 GLY B O   
5680  N N   . ILE B 125 ? 0.1176 0.1343 0.1508 -0.0005 0.0133  0.0353  117 ILE B N   
5681  C CA  . ILE B 125 ? 0.1040 0.1221 0.1392 -0.0006 0.0130  0.0380  117 ILE B CA  
5682  C C   . ILE B 125 ? 0.1304 0.1475 0.1642 -0.0006 0.0101  0.0360  117 ILE B C   
5683  O O   . ILE B 125 ? 0.1451 0.1610 0.1825 -0.0004 0.0081  0.0377  117 ILE B O   
5684  C CB  . ILE B 125 ? 0.1310 0.1511 0.1618 0.0002  0.0163  0.0399  117 ILE B CB  
5685  C CG1 . ILE B 125 ? 0.2017 0.2229 0.2334 0.0001  0.0158  0.0436  117 ILE B CG1 
5686  C CG2 . ILE B 125 ? 0.2027 0.2219 0.2252 0.0003  0.0172  0.0363  117 ILE B CG2 
5687  C CD1 . ILE B 125 ? 0.1836 0.2047 0.2230 -0.0011 0.0151  0.0478  117 ILE B CD1 
5688  N N   . ALA B 126 ? 0.1195 0.1373 0.1485 -0.0009 0.0098  0.0324  118 ALA B N   
5689  C CA  . ALA B 126 ? 0.1268 0.1462 0.1552 -0.0003 0.0074  0.0303  118 ALA B CA  
5690  C C   . ALA B 126 ? 0.1375 0.1551 0.1703 0.0001  0.0047  0.0287  118 ALA B C   
5691  O O   . ALA B 126 ? 0.1216 0.1385 0.1565 0.0017  0.0025  0.0285  118 ALA B O   
5692  C CB  . ALA B 126 ? 0.1241 0.1464 0.1468 -0.0015 0.0079  0.0270  118 ALA B CB  
5693  N N   . ASN B 127 ? 0.1447 0.1611 0.1784 -0.0011 0.0047  0.0276  119 ASN B N   
5694  C CA  . ASN B 127 ? 0.1124 0.1272 0.1500 -0.0009 0.0020  0.0261  119 ASN B CA  
5695  C C   . ASN B 127 ? 0.0998 0.1114 0.1427 -0.0007 0.0005  0.0287  119 ASN B C   
5696  O O   . ASN B 127 ? 0.1117 0.1207 0.1566 0.0002  -0.0023 0.0271  119 ASN B O   
5697  C CB  . ASN B 127 ? 0.0928 0.1071 0.1309 -0.0022 0.0020  0.0257  119 ASN B CB  
5698  C CG  . ASN B 127 ? 0.1295 0.1449 0.1618 -0.0030 0.0034  0.0238  119 ASN B CG  
5699  O OD1 . ASN B 127 ? 0.1467 0.1608 0.1783 -0.0034 0.0040  0.0247  119 ASN B OD1 
5700  N ND2 . ASN B 127 ? 0.1157 0.1335 0.1441 -0.0033 0.0037  0.0216  119 ASN B ND2 
5701  N N   . ALA B 128 ? 0.1240 0.1357 0.1692 -0.0016 0.0023  0.0328  120 ALA B N   
5702  C CA  . ALA B 128 ? 0.1115 0.1203 0.1620 -0.0026 0.0010  0.0361  120 ALA B CA  
5703  C C   . ALA B 128 ? 0.1204 0.1260 0.1695 -0.0011 -0.0002 0.0373  120 ALA B C   
5704  O O   . ALA B 128 ? 0.1204 0.1206 0.1728 -0.0015 -0.0028 0.0382  120 ALA B O   
5705  C CB  . ALA B 128 ? 0.1012 0.1129 0.1544 -0.0041 0.0039  0.0406  120 ALA B CB  
5706  N N   . VAL B 129 ? 0.1207 0.1292 0.1650 0.0007  0.0014  0.0374  121 VAL B N   
5707  C CA  . VAL B 129 ? 0.1431 0.1496 0.1858 0.0031  -0.0002 0.0383  121 VAL B CA  
5708  C C   . VAL B 129 ? 0.1663 0.1699 0.2100 0.0054  -0.0035 0.0341  121 VAL B C   
5709  O O   . VAL B 129 ? 0.1286 0.1263 0.1737 0.0073  -0.0060 0.0350  121 VAL B O   
5710  C CB  . VAL B 129 ? 0.1320 0.1441 0.1691 0.0045  0.0016  0.0383  121 VAL B CB  
5711  C CG1 . VAL B 129 ? 0.1235 0.1353 0.1593 0.0080  -0.0008 0.0385  121 VAL B CG1 
5712  C CG2 . VAL B 129 ? 0.1083 0.1221 0.1437 0.0031  0.0048  0.0427  121 VAL B CG2 
5713  N N   . GLY B 130 ? 0.1198 0.1269 0.1622 0.0054  -0.0036 0.0293  122 GLY B N   
5714  C CA  . GLY B 130 ? 0.1333 0.1389 0.1762 0.0077  -0.0063 0.0247  122 GLY B CA  
5715  C C   . GLY B 130 ? 0.1481 0.1460 0.1948 0.0068  -0.0090 0.0243  122 GLY B C   
5716  O O   . GLY B 130 ? 0.1195 0.1120 0.1666 0.0096  -0.0117 0.0220  122 GLY B O   
5717  N N   . MET B 131 ? 0.1332 0.1304 0.1827 0.0029  -0.0084 0.0262  123 MET B N   
5718  C CA  . MET B 131 ? 0.1165 0.1070 0.1701 0.0009  -0.0113 0.0261  123 MET B CA  
5719  C C   . MET B 131 ? 0.1428 0.1254 0.1986 0.0007  -0.0127 0.0301  123 MET B C   
5720  O O   . MET B 131 ? 0.1617 0.1358 0.2187 0.0009  -0.0161 0.0282  123 MET B O   
5721  C CB  . MET B 131 ? 0.1148 0.1086 0.1719 -0.0032 -0.0104 0.0280  123 MET B CB  
5722  C CG  . MET B 131 ? 0.1181 0.1175 0.1726 -0.0030 -0.0099 0.0244  123 MET B CG  
5723  S SD  . MET B 131 ? 0.1579 0.1621 0.2163 -0.0061 -0.0086 0.0275  123 MET B SD  
5724  C CE  . MET B 131 ? 0.1436 0.1522 0.1964 -0.0047 -0.0078 0.0239  123 MET B CE  
5725  N N   . ALA B 132 ? 0.1256 0.1101 0.1812 0.0001  -0.0101 0.0356  124 ALA B N   
5726  C CA  . ALA B 132 ? 0.1388 0.1154 0.1954 -0.0002 -0.0113 0.0404  124 ALA B CA  
5727  C C   . ALA B 132 ? 0.1872 0.1581 0.2406 0.0051  -0.0138 0.0383  124 ALA B C   
5728  O O   . ALA B 132 ? 0.1789 0.1390 0.2331 0.0056  -0.0167 0.0398  124 ALA B O   
5729  C CB  . ALA B 132 ? 0.1529 0.1343 0.2088 -0.0016 -0.0077 0.0468  124 ALA B CB  
5730  N N   . LEU B 133 ? 0.1515 0.1295 0.2012 0.0093  -0.0128 0.0349  125 LEU B N   
5731  C CA  . LEU B 133 ? 0.1799 0.1553 0.2273 0.0153  -0.0150 0.0325  125 LEU B CA  
5732  C C   . LEU B 133 ? 0.1675 0.1359 0.2157 0.0173  -0.0183 0.0266  125 LEU B C   
5733  O O   . LEU B 133 ? 0.1629 0.1218 0.2105 0.0214  -0.0212 0.0261  125 LEU B O   
5734  C CB  . LEU B 133 ? 0.1521 0.1395 0.1963 0.0182  -0.0131 0.0301  125 LEU B CB  
5735  C CG  . LEU B 133 ? 0.2351 0.2254 0.2774 0.0247  -0.0146 0.0283  125 LEU B CG  
5736  C CD1 . LEU B 133 ? 0.2266 0.2093 0.2683 0.0274  -0.0163 0.0340  125 LEU B CD1 
5737  C CD2 . LEU B 133 ? 0.2284 0.2324 0.2683 0.0245  -0.0121 0.0272  125 LEU B CD2 
5738  N N   . ALA B 134 ? 0.1408 0.1129 0.1898 0.0148  -0.0180 0.0222  126 ALA B N   
5739  C CA  . ALA B 134 ? 0.2033 0.1690 0.2522 0.0163  -0.0212 0.0162  126 ALA B CA  
5740  C C   . ALA B 134 ? 0.1665 0.1177 0.2177 0.0139  -0.0245 0.0181  126 ALA B C   
5741  O O   . ALA B 134 ? 0.2355 0.1765 0.2853 0.0177  -0.0277 0.0146  126 ALA B O   
5742  C CB  . ALA B 134 ? 0.1965 0.1691 0.2453 0.0131  -0.0204 0.0123  126 ALA B CB  
5743  N N   . GLU B 135 ? 0.1648 0.1146 0.2195 0.0076  -0.0237 0.0238  127 GLU B N   
5744  C CA  . GLU B 135 ? 0.1973 0.1338 0.2546 0.0039  -0.0267 0.0264  127 GLU B CA  
5745  C C   . GLU B 135 ? 0.2026 0.1282 0.2577 0.0080  -0.0283 0.0296  127 GLU B C   
5746  O O   . GLU B 135 ? 0.1968 0.1079 0.2513 0.0089  -0.0321 0.0278  127 GLU B O   
5747  C CB  . GLU B 135 ? 0.1663 0.1067 0.2285 -0.0036 -0.0248 0.0328  127 GLU B CB  
5748  C CG  . GLU B 135 ? 0.2009 0.1299 0.2670 -0.0098 -0.0280 0.0354  127 GLU B CG  
5749  C CD  . GLU B 135 ? 0.2989 0.2181 0.3648 -0.0108 -0.0282 0.0428  127 GLU B CD  
5750  O OE1 . GLU B 135 ? 0.2387 0.1605 0.3012 -0.0063 -0.0259 0.0461  127 GLU B OE1 
5751  O OE2 . GLU B 135 ? 0.2207 0.1298 0.2897 -0.0168 -0.0307 0.0456  127 GLU B OE2 
5752  N N   . LYS B 136 ? 0.2072 0.1390 0.2605 0.0107  -0.0256 0.0343  128 LYS B N   
5753  C CA  . LYS B 136 ? 0.1896 0.1122 0.2405 0.0152  -0.0271 0.0384  128 LYS B CA  
5754  C C   . LYS B 136 ? 0.1977 0.1144 0.2457 0.0235  -0.0302 0.0319  128 LYS B C   
5755  O O   . LYS B 136 ? 0.2221 0.1234 0.2686 0.0264  -0.0336 0.0327  128 LYS B O   
5756  C CB  . LYS B 136 ? 0.1951 0.1284 0.2440 0.0167  -0.0237 0.0439  128 LYS B CB  
5757  C CG  . LYS B 136 ? 0.3341 0.2608 0.3796 0.0224  -0.0254 0.0485  128 LYS B CG  
5758  C CD  . LYS B 136 ? 0.4396 0.3775 0.4824 0.0300  -0.0249 0.0448  128 LYS B CD  
5759  C CE  . LYS B 136 ? 0.4236 0.3651 0.4632 0.0332  -0.0243 0.0514  128 LYS B CE  
5760  N NZ  . LYS B 136 ? 0.4130 0.3386 0.4508 0.0360  -0.0276 0.0571  128 LYS B NZ  
5761  N N   . ILE B 137 ? 0.2243 0.1530 0.2712 0.0274  -0.0288 0.0255  129 ILE B N   
5762  C CA  . ILE B 137 ? 0.2651 0.1919 0.3096 0.0359  -0.0309 0.0186  129 ILE B CA  
5763  C C   . ILE B 137 ? 0.2592 0.1716 0.3033 0.0358  -0.0346 0.0130  129 ILE B C   
5764  O O   . ILE B 137 ? 0.2833 0.1837 0.3252 0.0423  -0.0377 0.0102  129 ILE B O   
5765  C CB  . ILE B 137 ? 0.3096 0.2545 0.3534 0.0381  -0.0281 0.0134  129 ILE B CB  
5766  C CG1 . ILE B 137 ? 0.3428 0.3005 0.3861 0.0401  -0.0255 0.0176  129 ILE B CG1 
5767  C CG2 . ILE B 137 ? 0.3474 0.2923 0.3894 0.0455  -0.0298 0.0049  129 ILE B CG2 
5768  C CD1 . ILE B 137 ? 0.3322 0.3072 0.3750 0.0404  -0.0227 0.0131  129 ILE B CD1 
5769  N N   . LEU B 138 ? 0.2311 0.1446 0.2770 0.0287  -0.0345 0.0109  130 LEU B N   
5770  C CA  . LEU B 138 ? 0.2390 0.1401 0.2841 0.0277  -0.0383 0.0048  130 LEU B CA  
5771  C C   . LEU B 138 ? 0.2426 0.1239 0.2884 0.0244  -0.0418 0.0090  130 LEU B C   
5772  O O   . LEU B 138 ? 0.2476 0.1134 0.2909 0.0270  -0.0458 0.0039  130 LEU B O   
5773  C CB  . LEU B 138 ? 0.2350 0.1444 0.2819 0.0207  -0.0375 0.0021  130 LEU B CB  
5774  C CG  . LEU B 138 ? 0.2073 0.1335 0.2522 0.0236  -0.0347 -0.0029 130 LEU B CG  
5775  C CD1 . LEU B 138 ? 0.1915 0.1265 0.2385 0.0163  -0.0336 -0.0026 130 LEU B CD1 
5776  C CD2 . LEU B 138 ? 0.2288 0.1520 0.2695 0.0305  -0.0367 -0.0121 130 LEU B CD2 
5777  N N   . ALA B 139 ? 0.2288 0.1098 0.2775 0.0184  -0.0404 0.0181  131 ALA B N   
5778  C CA  . ALA B 139 ? 0.2460 0.1084 0.2953 0.0145  -0.0434 0.0234  131 ALA B CA  
5779  C C   . ALA B 139 ? 0.2622 0.1106 0.3070 0.0234  -0.0459 0.0235  131 ALA B C   
5780  O O   . ALA B 139 ? 0.2821 0.1101 0.3249 0.0234  -0.0502 0.0223  131 ALA B O   
5781  C CB  . ALA B 139 ? 0.2769 0.1445 0.3298 0.0070  -0.0405 0.0338  131 ALA B CB  
5782  N N   . ALA B 140 ? 0.2549 0.1138 0.2980 0.0310  -0.0436 0.0250  132 ALA B N   
5783  C CA  . ALA B 140 ? 0.2698 0.1177 0.3090 0.0408  -0.0460 0.0257  132 ALA B CA  
5784  C C   . ALA B 140 ? 0.2807 0.1205 0.3170 0.0487  -0.0491 0.0152  132 ALA B C   
5785  O O   . ALA B 140 ? 0.3010 0.1223 0.3341 0.0548  -0.0528 0.0145  132 ALA B O   
5786  C CB  . ALA B 140 ? 0.3063 0.1708 0.3450 0.0468  -0.0430 0.0292  132 ALA B CB  
5787  N N   . GLU B 141 ? 0.2848 0.1379 0.3218 0.0490  -0.0475 0.0071  133 GLU B N   
5788  C CA  . GLU B 141 ? 0.3112 0.1593 0.3448 0.0570  -0.0497 -0.0034 133 GLU B CA  
5789  C C   . GLU B 141 ? 0.2955 0.1235 0.3273 0.0524  -0.0540 -0.0081 133 GLU B C   
5790  O O   . GLU B 141 ? 0.3148 0.1267 0.3425 0.0595  -0.0575 -0.0140 133 GLU B O   
5791  C CB  . GLU B 141 ? 0.2713 0.1416 0.3054 0.0586  -0.0463 -0.0099 133 GLU B CB  
5792  C CG  . GLU B 141 ? 0.3946 0.2632 0.4249 0.0672  -0.0478 -0.0210 133 GLU B CG  
5793  C CD  . GLU B 141 ? 0.4172 0.3081 0.4475 0.0678  -0.0441 -0.0266 133 GLU B CD  
5794  O OE1 . GLU B 141 ? 0.3899 0.2962 0.4230 0.0614  -0.0407 -0.0221 133 GLU B OE1 
5795  O OE2 . GLU B 141 ? 0.4108 0.3034 0.4378 0.0748  -0.0445 -0.0356 133 GLU B OE2 
5796  N N   . PHE B 142 ? 0.3010 0.1294 0.3359 0.0407  -0.0540 -0.0058 134 PHE B N   
5797  C CA  . PHE B 142 ? 0.3033 0.1172 0.3368 0.0354  -0.0581 -0.0118 134 PHE B CA  
5798  C C   . PHE B 142 ? 0.3200 0.1131 0.3547 0.0271  -0.0617 -0.0058 134 PHE B C   
5799  O O   . PHE B 142 ? 0.3547 0.1290 0.3865 0.0255  -0.0664 -0.0114 134 PHE B O   
5800  C CB  . PHE B 142 ? 0.3054 0.1355 0.3414 0.0281  -0.0565 -0.0152 134 PHE B CB  
5801  C CG  . PHE B 142 ? 0.2790 0.1230 0.3117 0.0352  -0.0547 -0.0243 134 PHE B CG  
5802  C CD1 . PHE B 142 ? 0.3684 0.2031 0.3958 0.0395  -0.0580 -0.0349 134 PHE B CD1 
5803  C CD2 . PHE B 142 ? 0.2759 0.1420 0.3102 0.0374  -0.0498 -0.0223 134 PHE B CD2 
5804  C CE1 . PHE B 142 ? 0.2871 0.1357 0.3110 0.0460  -0.0559 -0.0429 134 PHE B CE1 
5805  C CE2 . PHE B 142 ? 0.2616 0.1409 0.2928 0.0431  -0.0480 -0.0299 134 PHE B CE2 
5806  C CZ  . PHE B 142 ? 0.2672 0.1385 0.2933 0.0475  -0.0508 -0.0400 134 PHE B CZ  
5807  N N   . ASN B 143 ? 0.3761 0.1718 0.4147 0.0212  -0.0596 0.0054  135 ASN B N   
5808  C CA  . ASN B 143 ? 0.3627 0.1402 0.4029 0.0117  -0.0626 0.0118  135 ASN B CA  
5809  C C   . ASN B 143 ? 0.4019 0.1584 0.4356 0.0175  -0.0650 0.0112  135 ASN B C   
5810  O O   . ASN B 143 ? 0.3588 0.1149 0.3890 0.0283  -0.0641 0.0119  135 ASN B O   
5811  C CB  . ASN B 143 ? 0.3194 0.1067 0.3643 0.0049  -0.0589 0.0241  135 ASN B CB  
5812  C CG  . ASN B 143 ? 0.3229 0.1323 0.3738 -0.0029 -0.0553 0.0250  135 ASN B CG  
5813  O OD1 . ASN B 143 ? 0.2936 0.1087 0.3455 -0.0053 -0.0564 0.0174  135 ASN B OD1 
5814  N ND2 . ASN B 143 ? 0.3291 0.1508 0.3833 -0.0064 -0.0511 0.0342  135 ASN B ND2 
5815  N N   . LYS B 144 ? 0.4196 0.1609 0.4513 0.0101  -0.0676 0.0098  136 LYS B N   
5816  C CA  . LYS B 144 ? 0.5057 0.2264 0.5309 0.0139  -0.0693 0.0091  136 LYS B CA  
5817  C C   . LYS B 144 ? 0.5658 0.2770 0.5922 0.0022  -0.0691 0.0182  136 LYS B C   
5818  O O   . LYS B 144 ? 0.6035 0.3246 0.6358 -0.0090 -0.0679 0.0230  136 LYS B O   
5819  C CB  . LYS B 144 ? 0.5221 0.2312 0.5425 0.0171  -0.0730 -0.0034 136 LYS B CB  
5820  C CG  . LYS B 144 ? 0.4772 0.1960 0.4954 0.0291  -0.0729 -0.0133 136 LYS B CG  
5821  C CD  . LYS B 144 ? 0.5372 0.2583 0.5531 0.0423  -0.0708 -0.0108 136 LYS B CD  
5822  C CE  . LYS B 144 ? 0.6543 0.3740 0.6650 0.0551  -0.0716 -0.0224 136 LYS B CE  
5823  N NZ  . LYS B 144 ? 0.7092 0.4447 0.7211 0.0566  -0.0714 -0.0313 136 LYS B NZ  
5824  N N   . ASP B 145 ? 0.5800 0.2725 0.6008 0.0053  -0.0699 0.0206  137 ASP B N   
5825  C CA  . ASP B 145 ? 0.5684 0.2501 0.5892 -0.0047 -0.0694 0.0296  137 ASP B CA  
5826  C C   . ASP B 145 ? 0.5470 0.2294 0.5722 -0.0191 -0.0710 0.0282  137 ASP B C   
5827  O O   . ASP B 145 ? 0.5723 0.2443 0.5954 -0.0209 -0.0746 0.0193  137 ASP B O   
5828  C CB  . ASP B 145 ? 0.6355 0.2934 0.6490 0.0010  -0.0711 0.0293  137 ASP B CB  
5829  N N   . GLY B 146 ? 0.5506 0.2466 0.5820 -0.0291 -0.0682 0.0368  138 GLY B N   
5830  C CA  . GLY B 146 ? 0.6260 0.3265 0.6630 -0.0429 -0.0692 0.0367  138 GLY B CA  
5831  C C   . GLY B 146 ? 0.5959 0.3125 0.6382 -0.0450 -0.0705 0.0294  138 GLY B C   
5832  O O   . GLY B 146 ? 0.6527 0.3753 0.7004 -0.0562 -0.0716 0.0290  138 GLY B O   
5833  N N   . LEU B 147 ? 0.4656 0.1900 0.5069 -0.0348 -0.0704 0.0236  139 LEU B N   
5834  C CA  . LEU B 147 ? 0.4198 0.1571 0.4647 -0.0355 -0.0720 0.0155  139 LEU B CA  
5835  C C   . LEU B 147 ? 0.3890 0.1451 0.4376 -0.0296 -0.0685 0.0183  139 LEU B C   
5836  O O   . LEU B 147 ? 0.3585 0.1156 0.4036 -0.0186 -0.0687 0.0125  139 LEU B O   
5837  C CB  . LEU B 147 ? 0.4557 0.1802 0.4937 -0.0284 -0.0761 0.0029  139 LEU B CB  
5838  C CG  . LEU B 147 ? 0.4964 0.2014 0.5302 -0.0340 -0.0798 -0.0012 139 LEU B CG  
5839  C CD1 . LEU B 147 ? 0.5031 0.1959 0.5289 -0.0245 -0.0830 -0.0137 139 LEU B CD1 
5840  C CD2 . LEU B 147 ? 0.5089 0.2215 0.5488 -0.0481 -0.0815 -0.0010 139 LEU B CD2 
5841  N N   . ASN B 148 ? 0.3482 0.1202 0.4039 -0.0368 -0.0651 0.0269  140 ASN B N   
5842  C CA  . ASN B 148 ? 0.4441 0.2338 0.5035 -0.0323 -0.0614 0.0303  140 ASN B CA  
5843  C C   . ASN B 148 ? 0.3764 0.1814 0.4408 -0.0351 -0.0619 0.0243  140 ASN B C   
5844  O O   . ASN B 148 ? 0.3887 0.2096 0.4600 -0.0427 -0.0595 0.0289  140 ASN B O   
5845  C CB  . ASN B 148 ? 0.4483 0.2480 0.5114 -0.0374 -0.0565 0.0424  140 ASN B CB  
5846  C CG  . ASN B 148 ? 0.5457 0.3329 0.6024 -0.0331 -0.0554 0.0485  140 ASN B CG  
5847  O OD1 . ASN B 148 ? 0.5125 0.2869 0.5628 -0.0237 -0.0574 0.0443  140 ASN B OD1 
5848  N ND2 . ASN B 148 ? 0.6566 0.4484 0.7151 -0.0396 -0.0520 0.0584  140 ASN B ND2 
5849  N N   . ILE B 149 ? 0.3238 0.1280 0.3831 -0.0276 -0.0638 0.0136  141 ILE B N   
5850  C CA  . ILE B 149 ? 0.2927 0.1136 0.3541 -0.0294 -0.0635 0.0071  141 ILE B CA  
5851  C C   . ILE B 149 ? 0.2966 0.1413 0.3601 -0.0256 -0.0575 0.0101  141 ILE B C   
5852  O O   . ILE B 149 ? 0.2858 0.1458 0.3522 -0.0285 -0.0566 0.0077  141 ILE B O   
5853  C CB  . ILE B 149 ? 0.3019 0.1152 0.3564 -0.0230 -0.0672 -0.0053 141 ILE B CB  
5854  C CG1 . ILE B 149 ? 0.4071 0.2187 0.4552 -0.0096 -0.0651 -0.0086 141 ILE B CG1 
5855  C CG2 . ILE B 149 ? 0.3525 0.1426 0.4049 -0.0286 -0.0738 -0.0096 141 ILE B CG2 
5856  C CD1 . ILE B 149 ? 0.3061 0.1171 0.3476 -0.0022 -0.0670 -0.0209 141 ILE B CD1 
5857  N N   . VAL B 150 ? 0.2889 0.1367 0.3507 -0.0191 -0.0536 0.0151  142 VAL B N   
5858  C CA  . VAL B 150 ? 0.2402 0.1087 0.3040 -0.0169 -0.0480 0.0189  142 VAL B CA  
5859  C C   . VAL B 150 ? 0.2661 0.1366 0.3339 -0.0220 -0.0451 0.0299  142 VAL B C   
5860  O O   . VAL B 150 ? 0.3003 0.1613 0.3655 -0.0189 -0.0448 0.0348  142 VAL B O   
5861  C CB  . VAL B 150 ? 0.2627 0.1360 0.3209 -0.0058 -0.0458 0.0152  142 VAL B CB  
5862  C CG1 . VAL B 150 ? 0.2133 0.1070 0.2731 -0.0046 -0.0402 0.0188  142 VAL B CG1 
5863  C CG2 . VAL B 150 ? 0.2383 0.1095 0.2920 -0.0008 -0.0484 0.0043  142 VAL B CG2 
5864  N N   . ASP B 151 ? 0.2375 0.1213 0.3117 -0.0292 -0.0429 0.0340  143 ASP B N   
5865  C CA  . ASP B 151 ? 0.2583 0.1460 0.3366 -0.0346 -0.0397 0.0443  143 ASP B CA  
5866  C C   . ASP B 151 ? 0.2429 0.1501 0.3277 -0.0395 -0.0365 0.0464  143 ASP B C   
5867  O O   . ASP B 151 ? 0.2137 0.1230 0.3046 -0.0475 -0.0385 0.0469  143 ASP B O   
5868  C CB  . ASP B 151 ? 0.2461 0.1171 0.3266 -0.0423 -0.0433 0.0487  143 ASP B CB  
5869  C CG  . ASP B 151 ? 0.3587 0.2335 0.4426 -0.0478 -0.0397 0.0601  143 ASP B CG  
5870  O OD1 . ASP B 151 ? 0.3703 0.2604 0.4545 -0.0450 -0.0345 0.0640  143 ASP B OD1 
5871  O OD2 . ASP B 151 ? 0.4044 0.2678 0.4891 -0.0545 -0.0416 0.0644  143 ASP B OD2 
5872  N N   . HIS B 152 ? 0.2287 0.1501 0.3122 -0.0346 -0.0317 0.0474  144 HIS B N   
5873  C CA  . HIS B 152 ? 0.2379 0.1769 0.3268 -0.0376 -0.0284 0.0494  144 HIS B CA  
5874  C C   . HIS B 152 ? 0.1936 0.1427 0.2796 -0.0327 -0.0228 0.0531  144 HIS B C   
5875  O O   . HIS B 152 ? 0.2074 0.1521 0.2873 -0.0266 -0.0220 0.0526  144 HIS B O   
5876  C CB  . HIS B 152 ? 0.1825 0.1282 0.2719 -0.0366 -0.0304 0.0418  144 HIS B CB  
5877  C CG  . HIS B 152 ? 0.1886 0.1337 0.2707 -0.0284 -0.0303 0.0352  144 HIS B CG  
5878  N ND1 . HIS B 152 ? 0.2530 0.1870 0.3305 -0.0254 -0.0344 0.0282  144 HIS B ND1 
5879  C CD2 . HIS B 152 ? 0.2389 0.1933 0.3173 -0.0228 -0.0265 0.0345  144 HIS B CD2 
5880  C CE1 . HIS B 152 ? 0.2289 0.1672 0.3010 -0.0184 -0.0328 0.0239  144 HIS B CE1 
5881  N NE2 . HIS B 152 ? 0.1905 0.1408 0.2631 -0.0171 -0.0282 0.0277  144 HIS B NE2 
5882  N N   . TYR B 153 ? 0.1857 0.1491 0.2764 -0.0352 -0.0192 0.0564  145 TYR B N   
5883  C CA  . TYR B 153 ? 0.1900 0.1632 0.2783 -0.0317 -0.0137 0.0601  145 TYR B CA  
5884  C C   . TYR B 153 ? 0.1961 0.1788 0.2819 -0.0269 -0.0120 0.0549  145 TYR B C   
5885  O O   . TYR B 153 ? 0.2125 0.1972 0.3000 -0.0272 -0.0144 0.0499  145 TYR B O   
5886  C CB  . TYR B 153 ? 0.2421 0.2246 0.3365 -0.0371 -0.0102 0.0675  145 TYR B CB  
5887  C CG  . TYR B 153 ? 0.2568 0.2306 0.3514 -0.0412 -0.0104 0.0745  145 TYR B CG  
5888  C CD1 . TYR B 153 ? 0.3906 0.3531 0.4887 -0.0474 -0.0149 0.0754  145 TYR B CD1 
5889  C CD2 . TYR B 153 ? 0.3045 0.2799 0.3946 -0.0390 -0.0064 0.0803  145 TYR B CD2 
5890  C CE1 . TYR B 153 ? 0.4352 0.3877 0.5327 -0.0515 -0.0153 0.0823  145 TYR B CE1 
5891  C CE2 . TYR B 153 ? 0.3634 0.3301 0.4527 -0.0428 -0.0067 0.0875  145 TYR B CE2 
5892  C CZ  . TYR B 153 ? 0.4802 0.4350 0.5733 -0.0490 -0.0111 0.0887  145 TYR B CZ  
5893  O OH  . TYR B 153 ? 0.5891 0.5341 0.6800 -0.0527 -0.0115 0.0955  145 TYR B OH  
5894  N N   . THR B 154 ? 0.1527 0.1410 0.2341 -0.0228 -0.0078 0.0564  146 THR B N   
5895  C CA  . THR B 154 ? 0.1236 0.1200 0.2019 -0.0188 -0.0055 0.0527  146 THR B CA  
5896  C C   . THR B 154 ? 0.1606 0.1670 0.2403 -0.0191 -0.0005 0.0573  146 THR B C   
5897  O O   . THR B 154 ? 0.1699 0.1766 0.2463 -0.0181 0.0023  0.0612  146 THR B O   
5898  C CB  . THR B 154 ? 0.1581 0.1509 0.2288 -0.0135 -0.0056 0.0490  146 THR B CB  
5899  O OG1 . THR B 154 ? 0.1912 0.1749 0.2608 -0.0125 -0.0100 0.0449  146 THR B OG1 
5900  C CG2 . THR B 154 ? 0.1223 0.1222 0.1896 -0.0106 -0.0037 0.0451  146 THR B CG2 
5901  N N   . TYR B 155 ? 0.1193 0.1343 0.2036 -0.0201 0.0006  0.0569  147 TYR B N   
5902  C CA  . TYR B 155 ? 0.1409 0.1660 0.2269 -0.0194 0.0056  0.0605  147 TYR B CA  
5903  C C   . TYR B 155 ? 0.1604 0.1890 0.2414 -0.0145 0.0076  0.0566  147 TYR B C   
5904  O O   . TYR B 155 ? 0.1424 0.1696 0.2227 -0.0133 0.0050  0.0522  147 TYR B O   
5905  C CB  . TYR B 155 ? 0.1251 0.1588 0.2210 -0.0236 0.0056  0.0637  147 TYR B CB  
5906  C CG  . TYR B 155 ? 0.1451 0.1759 0.2467 -0.0300 0.0038  0.0684  147 TYR B CG  
5907  C CD1 . TYR B 155 ? 0.1354 0.1687 0.2374 -0.0322 0.0075  0.0749  147 TYR B CD1 
5908  C CD2 . TYR B 155 ? 0.1811 0.2063 0.2871 -0.0344 -0.0015 0.0664  147 TYR B CD2 
5909  C CE1 . TYR B 155 ? 0.1393 0.1691 0.2463 -0.0389 0.0059  0.0800  147 TYR B CE1 
5910  C CE2 . TYR B 155 ? 0.1834 0.2043 0.2944 -0.0413 -0.0034 0.0708  147 TYR B CE2 
5911  C CZ  . TYR B 155 ? 0.1832 0.2061 0.2948 -0.0436 0.0003  0.0779  147 TYR B CZ  
5912  O OH  . TYR B 155 ? 0.2653 0.2829 0.3813 -0.0510 -0.0014 0.0829  147 TYR B OH  
5913  N N   . VAL B 156 ? 0.1225 0.1552 0.1996 -0.0119 0.0122  0.0583  148 VAL B N   
5914  C CA  . VAL B 156 ? 0.1133 0.1471 0.1843 -0.0075 0.0142  0.0547  148 VAL B CA  
5915  C C   . VAL B 156 ? 0.1134 0.1556 0.1858 -0.0056 0.0190  0.0571  148 VAL B C   
5916  O O   . VAL B 156 ? 0.1424 0.1888 0.2156 -0.0065 0.0221  0.0612  148 VAL B O   
5917  C CB  . VAL B 156 ? 0.1154 0.1436 0.1772 -0.0055 0.0147  0.0525  148 VAL B CB  
5918  C CG1 . VAL B 156 ? 0.1178 0.1451 0.1734 -0.0025 0.0157  0.0481  148 VAL B CG1 
5919  C CG2 . VAL B 156 ? 0.1189 0.1403 0.1801 -0.0068 0.0106  0.0511  148 VAL B CG2 
5920  N N   . PHE B 157 ? 0.0985 0.1432 0.1708 -0.0025 0.0197  0.0546  149 PHE B N   
5921  C CA  . PHE B 157 ? 0.1208 0.1708 0.1910 0.0015  0.0245  0.0550  149 PHE B CA  
5922  C C   . PHE B 157 ? 0.1597 0.2022 0.2190 0.0046  0.0255  0.0508  149 PHE B C   
5923  O O   . PHE B 157 ? 0.1556 0.1918 0.2115 0.0046  0.0226  0.0474  149 PHE B O   
5924  C CB  . PHE B 157 ? 0.0991 0.1562 0.1761 0.0039  0.0247  0.0552  149 PHE B CB  
5925  C CG  . PHE B 157 ? 0.1256 0.1935 0.2140 0.0008  0.0247  0.0598  149 PHE B CG  
5926  C CD1 . PHE B 157 ? 0.1088 0.1773 0.2006 -0.0046 0.0243  0.0635  149 PHE B CD1 
5927  C CD2 . PHE B 157 ? 0.1661 0.2437 0.2622 0.0031  0.0251  0.0606  149 PHE B CD2 
5928  C CE1 . PHE B 157 ? 0.1010 0.1795 0.2035 -0.0087 0.0243  0.0679  149 PHE B CE1 
5929  C CE2 . PHE B 157 ? 0.2076 0.2972 0.3153 -0.0005 0.0250  0.0649  149 PHE B CE2 
5930  C CZ  . PHE B 157 ? 0.1224 0.2123 0.2333 -0.0071 0.0246  0.0685  149 PHE B CZ  
5931  N N   . MET B 158 ? 0.1432 0.1869 0.1968 0.0068  0.0296  0.0510  150 MET B N   
5932  C CA  . MET B 158 ? 0.1576 0.1941 0.2006 0.0090  0.0303  0.0466  150 MET B CA  
5933  C C   . MET B 158 ? 0.1325 0.1719 0.1712 0.0131  0.0353  0.0461  150 MET B C   
5934  O O   . MET B 158 ? 0.1573 0.2054 0.2004 0.0139  0.0385  0.0496  150 MET B O   
5935  C CB  . MET B 158 ? 0.2168 0.2486 0.2539 0.0064  0.0285  0.0457  150 MET B CB  
5936  C CG  . MET B 158 ? 0.2183 0.2537 0.2535 0.0055  0.0306  0.0489  150 MET B CG  
5937  S SD  . MET B 158 ? 0.2248 0.2553 0.2552 0.0031  0.0269  0.0481  150 MET B SD  
5938  C CE  . MET B 158 ? 0.2246 0.2500 0.2450 0.0041  0.0267  0.0419  150 MET B CE  
5939  N N   . GLY B 159 ? 0.1322 0.1642 0.1618 0.0155  0.0360  0.0417  151 GLY B N   
5940  C CA  . GLY B 159 ? 0.1792 0.2114 0.2030 0.0201  0.0404  0.0398  151 GLY B CA  
5941  C C   . GLY B 159 ? 0.2354 0.2614 0.2473 0.0196  0.0413  0.0362  151 GLY B C   
5942  O O   . GLY B 159 ? 0.1819 0.2053 0.1908 0.0155  0.0386  0.0357  151 GLY B O   
5943  N N   . ASP B 160 ? 0.2061 0.2306 0.2113 0.0240  0.0452  0.0334  152 ASP B N   
5944  C CA  . ASP B 160 ? 0.1566 0.1756 0.1496 0.0235  0.0462  0.0294  152 ASP B CA  
5945  C C   . ASP B 160 ? 0.1551 0.1633 0.1421 0.0198  0.0422  0.0256  152 ASP B C   
5946  O O   . ASP B 160 ? 0.1954 0.2024 0.1760 0.0163  0.0408  0.0239  152 ASP B O   
5947  C CB  . ASP B 160 ? 0.1863 0.2032 0.1727 0.0296  0.0506  0.0259  152 ASP B CB  
5948  C CG  . ASP B 160 ? 0.2534 0.2833 0.2453 0.0334  0.0554  0.0295  152 ASP B CG  
5949  O OD1 . ASP B 160 ? 0.2800 0.3175 0.2710 0.0312  0.0568  0.0323  152 ASP B OD1 
5950  O OD2 . ASP B 160 ? 0.3132 0.3464 0.3106 0.0386  0.0576  0.0299  152 ASP B OD2 
5951  N N   . GLY B 161 ? 0.1495 0.1509 0.1384 0.0203  0.0403  0.0244  153 GLY B N   
5952  C CA  . GLY B 161 ? 0.1513 0.1429 0.1343 0.0163  0.0370  0.0213  153 GLY B CA  
5953  C C   . GLY B 161 ? 0.1590 0.1552 0.1457 0.0109  0.0335  0.0230  153 GLY B C   
5954  O O   . GLY B 161 ? 0.1511 0.1446 0.1319 0.0070  0.0318  0.0205  153 GLY B O   
5955  N N   . OCS B 162 ? 0.1329 0.1363 0.1295 0.0109  0.0325  0.0272  154 OCS B N   
5956  C CA  . OCS B 162 ? 0.1978 0.2052 0.1982 0.0070  0.0293  0.0288  154 OCS B CA  
5957  C CB  . OCS B 162 ? 0.1654 0.1790 0.1765 0.0074  0.0285  0.0331  154 OCS B CB  
5958  S SG  . OCS B 162 ? 0.2268 0.2379 0.2435 0.0089  0.0271  0.0332  154 OCS B SG  
5959  C C   . OCS B 162 ? 0.1272 0.1383 0.1230 0.0056  0.0297  0.0288  154 OCS B C   
5960  O O   . OCS B 162 ? 0.1825 0.1937 0.1761 0.0026  0.0270  0.0275  154 OCS B O   
5961  O OD1 . OCS B 162 ? 0.2952 0.3134 0.3213 0.0099  0.0274  0.0370  154 OCS B OD1 
5962  O OD2 . OCS B 162 ? 0.1575 0.1658 0.1740 0.0058  0.0236  0.0318  154 OCS B OD2 
5963  O OD3 . OCS B 162 ? 0.4905 0.4962 0.5019 0.0120  0.0293  0.0310  154 OCS B OD3 
5964  N N   . LEU B 163 ? 0.1312 0.1462 0.1255 0.0081  0.0330  0.0304  155 LEU B N   
5965  C CA  . LEU B 163 ? 0.1353 0.1547 0.1248 0.0072  0.0334  0.0313  155 LEU B CA  
5966  C C   . LEU B 163 ? 0.1941 0.2092 0.1725 0.0058  0.0330  0.0262  155 LEU B C   
5967  O O   . LEU B 163 ? 0.1553 0.1738 0.1300 0.0038  0.0312  0.0262  155 LEU B O   
5968  C CB  . LEU B 163 ? 0.1376 0.1630 0.1277 0.0100  0.0375  0.0346  155 LEU B CB  
5969  C CG  . LEU B 163 ? 0.1818 0.2133 0.1826 0.0096  0.0374  0.0406  155 LEU B CG  
5970  C CD1 . LEU B 163 ? 0.1821 0.2210 0.1834 0.0120  0.0422  0.0441  155 LEU B CD1 
5971  C CD2 . LEU B 163 ? 0.1388 0.1712 0.1416 0.0067  0.0337  0.0434  155 LEU B CD2 
5972  N N   . MET B 164 ? 0.1480 0.1554 0.1211 0.0067  0.0343  0.0219  156 MET B N   
5973  C CA  . MET B 164 ? 0.1565 0.1583 0.1190 0.0042  0.0334  0.0166  156 MET B CA  
5974  C C   . MET B 164 ? 0.1698 0.1708 0.1331 -0.0009 0.0292  0.0154  156 MET B C   
5975  O O   . MET B 164 ? 0.1705 0.1730 0.1278 -0.0043 0.0273  0.0128  156 MET B O   
5976  C CB  . MET B 164 ? 0.1668 0.1580 0.1229 0.0066  0.0356  0.0123  156 MET B CB  
5977  C CG  . MET B 164 ? 0.2269 0.2196 0.1777 0.0115  0.0400  0.0113  156 MET B CG  
5978  S SD  . MET B 164 ? 0.1922 0.1709 0.1347 0.0156  0.0425  0.0055  156 MET B SD  
5979  C CE  . MET B 164 ? 0.2129 0.1964 0.1671 0.0221  0.0452  0.0102  156 MET B CE  
5980  N N   . GLU B 165 ? 0.1617 0.1617 0.1325 -0.0015 0.0276  0.0171  157 GLU B N   
5981  C CA  . GLU B 165 ? 0.1407 0.1410 0.1126 -0.0060 0.0242  0.0159  157 GLU B CA  
5982  C C   . GLU B 165 ? 0.1357 0.1455 0.1099 -0.0075 0.0218  0.0174  157 GLU B C   
5983  O O   . GLU B 165 ? 0.1658 0.1812 0.1453 -0.0050 0.0219  0.0212  157 GLU B O   
5984  C CB  . GLU B 165 ? 0.1437 0.1426 0.1232 -0.0055 0.0232  0.0180  157 GLU B CB  
5985  C CG  . GLU B 165 ? 0.1395 0.1286 0.1162 -0.0049 0.0242  0.0165  157 GLU B CG  
5986  C CD  . GLU B 165 ? 0.1518 0.1338 0.1209 -0.0099 0.0230  0.0129  157 GLU B CD  
5987  O OE1 . GLU B 165 ? 0.1583 0.1449 0.1252 -0.0142 0.0212  0.0112  157 GLU B OE1 
5988  O OE2 . GLU B 165 ? 0.1653 0.1372 0.1308 -0.0096 0.0236  0.0119  157 GLU B OE2 
5989  N N   . GLY B 166 ? 0.1407 0.1524 0.1112 -0.0118 0.0194  0.0144  158 GLY B N   
5990  C CA  . GLY B 166 ? 0.1425 0.1641 0.1153 -0.0125 0.0168  0.0156  158 GLY B CA  
5991  C C   . GLY B 166 ? 0.1242 0.1504 0.1065 -0.0105 0.0152  0.0189  158 GLY B C   
5992  O O   . GLY B 166 ? 0.1389 0.1714 0.1241 -0.0084 0.0138  0.0215  158 GLY B O   
5993  N N   . VAL B 167 ? 0.1202 0.1426 0.1068 -0.0108 0.0152  0.0188  159 VAL B N   
5994  C CA  . VAL B 167 ? 0.1220 0.1481 0.1166 -0.0089 0.0135  0.0211  159 VAL B CA  
5995  C C   . VAL B 167 ? 0.1467 0.1727 0.1458 -0.0051 0.0142  0.0253  159 VAL B C   
5996  O O   . VAL B 167 ? 0.1256 0.1547 0.1299 -0.0033 0.0122  0.0273  159 VAL B O   
5997  C CB  . VAL B 167 ? 0.1333 0.1558 0.1306 -0.0102 0.0133  0.0200  159 VAL B CB  
5998  C CG1 . VAL B 167 ? 0.1444 0.1597 0.1424 -0.0085 0.0154  0.0213  159 VAL B CG1 
5999  C CG2 . VAL B 167 ? 0.1244 0.1516 0.1285 -0.0087 0.0110  0.0207  159 VAL B CG2 
6000  N N   . SER B 168 ? 0.1145 0.1372 0.1115 -0.0038 0.0170  0.0267  160 SER B N   
6001  C CA  . SER B 168 ? 0.1588 0.1829 0.1599 -0.0013 0.0179  0.0312  160 SER B CA  
6002  C C   . SER B 168 ? 0.1798 0.2088 0.1785 -0.0005 0.0169  0.0334  160 SER B C   
6003  O O   . SER B 168 ? 0.1323 0.1626 0.1355 0.0010  0.0158  0.0375  160 SER B O   
6004  C CB  . SER B 168 ? 0.1689 0.1907 0.1687 0.0002  0.0217  0.0322  160 SER B CB  
6005  O OG  . SER B 168 ? 0.1747 0.1973 0.1665 0.0005  0.0238  0.0310  160 SER B OG  
6006  N N   . HIS B 169 ? 0.1360 0.1674 0.1271 -0.0017 0.0169  0.0308  161 HIS B N   
6007  C CA  . HIS B 169 ? 0.1546 0.1917 0.1427 -0.0008 0.0152  0.0328  161 HIS B CA  
6008  C C   . HIS B 169 ? 0.1645 0.2051 0.1581 0.0002  0.0115  0.0337  161 HIS B C   
6009  O O   . HIS B 169 ? 0.1486 0.1910 0.1442 0.0027  0.0101  0.0379  161 HIS B O   
6010  C CB  . HIS B 169 ? 0.1304 0.1700 0.1095 -0.0030 0.0152  0.0288  161 HIS B CB  
6011  C CG  . HIS B 169 ? 0.1332 0.1805 0.1095 -0.0025 0.0122  0.0298  161 HIS B CG  
6012  N ND1 . HIS B 169 ? 0.1627 0.2129 0.1371 0.0002  0.0123  0.0347  161 HIS B ND1 
6013  C CD2 . HIS B 169 ? 0.1331 0.1869 0.1084 -0.0043 0.0089  0.0270  161 HIS B CD2 
6014  C CE1 . HIS B 169 ? 0.2025 0.2600 0.1745 0.0006  0.0090  0.0349  161 HIS B CE1 
6015  N NE2 . HIS B 169 ? 0.1369 0.1975 0.1099 -0.0021 0.0068  0.0301  161 HIS B NE2 
6016  N N   . GLU B 170 ? 0.1164 0.1576 0.1122 -0.0015 0.0100  0.0299  162 GLU B N   
6017  C CA  . GLU B 170 ? 0.1561 0.2020 0.1568 0.0002  0.0067  0.0299  162 GLU B CA  
6018  C C   . GLU B 170 ? 0.1152 0.1566 0.1226 0.0032  0.0060  0.0332  162 GLU B C   
6019  O O   . GLU B 170 ? 0.1237 0.1665 0.1333 0.0064  0.0037  0.0359  162 GLU B O   
6020  C CB  . GLU B 170 ? 0.1101 0.1587 0.1115 -0.0027 0.0060  0.0251  162 GLU B CB  
6021  C CG  . GLU B 170 ? 0.1138 0.1666 0.1085 -0.0068 0.0061  0.0217  162 GLU B CG  
6022  C CD  . GLU B 170 ? 0.1303 0.1862 0.1260 -0.0107 0.0055  0.0178  162 GLU B CD  
6023  O OE1 . GLU B 170 ? 0.1230 0.1805 0.1245 -0.0091 0.0047  0.0178  162 GLU B OE1 
6024  O OE2 . GLU B 170 ? 0.1659 0.2225 0.1563 -0.0155 0.0058  0.0149  162 GLU B OE2 
6025  N N   . ALA B 171 ? 0.1086 0.1440 0.1191 0.0022  0.0077  0.0332  163 ALA B N   
6026  C CA  . ALA B 171 ? 0.1259 0.1569 0.1428 0.0039  0.0065  0.0354  163 ALA B CA  
6027  C C   . ALA B 171 ? 0.1475 0.1758 0.1654 0.0052  0.0070  0.0411  163 ALA B C   
6028  O O   . ALA B 171 ? 0.1145 0.1397 0.1361 0.0071  0.0048  0.0436  163 ALA B O   
6029  C CB  . ALA B 171 ? 0.1600 0.1870 0.1799 0.0022  0.0077  0.0337  163 ALA B CB  
6030  N N   . CYS B 172 ? 0.1493 0.1784 0.1635 0.0041  0.0100  0.0432  164 CYS B N   
6031  C CA  . CYS B 172 ? 0.1189 0.1466 0.1336 0.0047  0.0110  0.0492  164 CYS B CA  
6032  C C   . CYS B 172 ? 0.1317 0.1618 0.1426 0.0069  0.0089  0.0521  164 CYS B C   
6033  O O   . CYS B 172 ? 0.1624 0.1895 0.1750 0.0079  0.0081  0.0576  164 CYS B O   
6034  C CB  . CYS B 172 ? 0.1289 0.1582 0.1406 0.0034  0.0153  0.0503  164 CYS B CB  
6035  S SG  . CYS B 172 ? 0.1631 0.1897 0.1808 0.0020  0.0173  0.0486  164 CYS B SG  
6036  N N   . SER B 173 ? 0.1247 0.1605 0.1304 0.0074  0.0079  0.0489  165 SER B N   
6037  C CA  . SER B 173 ? 0.1654 0.2049 0.1680 0.0102  0.0051  0.0514  165 SER B CA  
6038  C C   . SER B 173 ? 0.1798 0.2159 0.1881 0.0134  0.0015  0.0526  165 SER B C   
6039  O O   . SER B 173 ? 0.1784 0.2116 0.1866 0.0160  -0.0002 0.0579  165 SER B O   
6040  C CB  . SER B 173 ? 0.1768 0.2245 0.1741 0.0095  0.0041  0.0468  165 SER B CB  
6041  O OG  . SER B 173 ? 0.2246 0.2778 0.2201 0.0128  0.0006  0.0489  165 SER B OG  
6042  N N   . LEU B 174 ? 0.1516 0.1873 0.1645 0.0134  0.0004  0.0477  166 LEU B N   
6043  C CA  . LEU B 174 ? 0.1653 0.1975 0.1831 0.0171  -0.0029 0.0476  166 LEU B CA  
6044  C C   . LEU B 174 ? 0.1535 0.1750 0.1751 0.0169  -0.0030 0.0517  166 LEU B C   
6045  O O   . LEU B 174 ? 0.1706 0.1864 0.1939 0.0203  -0.0058 0.0545  166 LEU B O   
6046  C CB  . LEU B 174 ? 0.1574 0.1928 0.1781 0.0167  -0.0034 0.0410  166 LEU B CB  
6047  C CG  . LEU B 174 ? 0.3454 0.3813 0.3699 0.0214  -0.0066 0.0386  166 LEU B CG  
6048  C CD1 . LEU B 174 ? 0.2520 0.2931 0.2749 0.0263  -0.0093 0.0408  166 LEU B CD1 
6049  C CD2 . LEU B 174 ? 0.3746 0.4176 0.4004 0.0198  -0.0060 0.0323  166 LEU B CD2 
6050  N N   . ALA B 175 ? 0.1624 0.1810 0.1856 0.0128  -0.0001 0.0523  167 ALA B N   
6051  C CA  . ALA B 175 ? 0.1683 0.1782 0.1959 0.0114  -0.0003 0.0563  167 ALA B CA  
6052  C C   . ALA B 175 ? 0.1519 0.1587 0.1770 0.0120  -0.0004 0.0638  167 ALA B C   
6053  O O   . ALA B 175 ? 0.2094 0.2073 0.2372 0.0124  -0.0025 0.0674  167 ALA B O   
6054  C CB  . ALA B 175 ? 0.1295 0.1398 0.1596 0.0071  0.0029  0.0558  167 ALA B CB  
6055  N N   . GLY B 176 ? 0.1423 0.1557 0.1614 0.0121  0.0015  0.0660  168 GLY B N   
6056  C CA  . GLY B 176 ? 0.1523 0.1638 0.1676 0.0128  0.0014  0.0737  168 GLY B CA  
6057  C C   . GLY B 176 ? 0.1983 0.2065 0.2123 0.0179  -0.0030 0.0755  168 GLY B C   
6058  O O   . GLY B 176 ? 0.1997 0.2001 0.2133 0.0187  -0.0046 0.0821  168 GLY B O   
6059  N N   . THR B 177 ? 0.1650 0.1794 0.1783 0.0214  -0.0052 0.0700  169 THR B N   
6060  C CA  A THR B 177 ? 0.1875 0.2005 0.2003 0.0275  -0.0097 0.0710  169 THR B CA  
6061  C CA  B THR B 177 ? 0.1890 0.2018 0.2018 0.0275  -0.0096 0.0712  169 THR B CA  
6062  C C   . THR B 177 ? 0.1679 0.1682 0.1860 0.0296  -0.0123 0.0713  169 THR B C   
6063  O O   . THR B 177 ? 0.2411 0.2337 0.2583 0.0338  -0.0154 0.0758  169 THR B O   
6064  C CB  A THR B 177 ? 0.1830 0.2076 0.1957 0.0301  -0.0110 0.0643  169 THR B CB  
6065  C CB  B THR B 177 ? 0.1924 0.2167 0.2047 0.0304  -0.0112 0.0648  169 THR B CB  
6066  O OG1 A THR B 177 ? 0.2064 0.2414 0.2129 0.0285  -0.0097 0.0646  169 THR B OG1 
6067  O OG1 B THR B 177 ? 0.1474 0.1724 0.1646 0.0288  -0.0104 0.0578  169 THR B OG1 
6068  C CG2 A THR B 177 ? 0.2213 0.2458 0.2355 0.0375  -0.0156 0.0642  169 THR B CG2 
6069  C CG2 B THR B 177 ? 0.1966 0.2319 0.2031 0.0278  -0.0092 0.0642  169 THR B CG2 
6070  N N   . LEU B 178 ? 0.1611 0.1584 0.1842 0.0267  -0.0113 0.0663  170 LEU B N   
6071  C CA  . LEU B 178 ? 0.1664 0.1520 0.1940 0.0283  -0.0139 0.0648  170 LEU B CA  
6072  C C   . LEU B 178 ? 0.2674 0.2410 0.2969 0.0237  -0.0134 0.0704  170 LEU B C   
6073  O O   . LEU B 178 ? 0.2353 0.1975 0.2681 0.0239  -0.0159 0.0692  170 LEU B O   
6074  C CB  . LEU B 178 ? 0.1938 0.1830 0.2252 0.0276  -0.0136 0.0564  170 LEU B CB  
6075  C CG  . LEU B 178 ? 0.2379 0.2386 0.2682 0.0322  -0.0144 0.0509  170 LEU B CG  
6076  C CD1 . LEU B 178 ? 0.3018 0.3077 0.3347 0.0300  -0.0131 0.0437  170 LEU B CD1 
6077  C CD2 . LEU B 178 ? 0.3044 0.3016 0.3350 0.0401  -0.0185 0.0508  170 LEU B CD2 
6078  N N   . GLY B 179 ? 0.2001 0.1763 0.2274 0.0192  -0.0103 0.0764  171 GLY B N   
6079  C CA  . GLY B 179 ? 0.1933 0.1598 0.2227 0.0144  -0.0098 0.0829  171 GLY B CA  
6080  C C   . GLY B 179 ? 0.2328 0.1941 0.2688 0.0097  -0.0098 0.0796  171 GLY B C   
6081  O O   . GLY B 179 ? 0.2252 0.1737 0.2637 0.0079  -0.0123 0.0819  171 GLY B O   
6082  N N   . LEU B 180 ? 0.1993 0.1698 0.2376 0.0076  -0.0072 0.0741  172 LEU B N   
6083  C CA  . LEU B 180 ? 0.1627 0.1305 0.2070 0.0036  -0.0075 0.0704  172 LEU B CA  
6084  C C   . LEU B 180 ? 0.1646 0.1331 0.2124 -0.0031 -0.0048 0.0763  172 LEU B C   
6085  O O   . LEU B 180 ? 0.1559 0.1342 0.2053 -0.0057 -0.0011 0.0757  172 LEU B O   
6086  C CB  . LEU B 180 ? 0.1808 0.1581 0.2256 0.0044  -0.0060 0.0630  172 LEU B CB  
6087  C CG  . LEU B 180 ? 0.2172 0.1975 0.2589 0.0101  -0.0079 0.0572  172 LEU B CG  
6088  C CD1 . LEU B 180 ? 0.1503 0.1394 0.1923 0.0093  -0.0060 0.0510  172 LEU B CD1 
6089  C CD2 . LEU B 180 ? 0.2789 0.2487 0.3221 0.0135  -0.0122 0.0546  172 LEU B CD2 
6090  N N   . GLY B 181 ? 0.1883 0.1463 0.2374 -0.0058 -0.0066 0.0823  173 GLY B N   
6091  C CA  . GLY B 181 ? 0.2648 0.2238 0.3177 -0.0129 -0.0041 0.0890  173 GLY B CA  
6092  C C   . GLY B 181 ? 0.2442 0.2060 0.3048 -0.0182 -0.0039 0.0860  173 GLY B C   
6093  O O   . GLY B 181 ? 0.2096 0.1770 0.2745 -0.0240 -0.0011 0.0910  173 GLY B O   
6094  N N   . LYS B 182 ? 0.2065 0.1661 0.2691 -0.0164 -0.0067 0.0781  174 LYS B N   
6095  C CA  . LYS B 182 ? 0.2277 0.1911 0.2972 -0.0211 -0.0070 0.0750  174 LYS B CA  
6096  C C   . LYS B 182 ? 0.2071 0.1842 0.2769 -0.0192 -0.0037 0.0710  174 LYS B C   
6097  O O   . LYS B 182 ? 0.2209 0.2025 0.2959 -0.0219 -0.0041 0.0681  174 LYS B O   
6098  C CB  . LYS B 182 ? 0.1842 0.1365 0.2550 -0.0207 -0.0123 0.0690  174 LYS B CB  
6099  C CG  . LYS B 182 ? 0.2985 0.2352 0.3700 -0.0241 -0.0159 0.0730  174 LYS B CG  
6100  C CD  . LYS B 182 ? 0.3984 0.3231 0.4695 -0.0223 -0.0212 0.0657  174 LYS B CD  
6101  C CE  . LYS B 182 ? 0.4005 0.3097 0.4741 -0.0283 -0.0251 0.0687  174 LYS B CE  
6102  N NZ  . LYS B 182 ? 0.4427 0.3391 0.5147 -0.0259 -0.0303 0.0606  174 LYS B NZ  
6103  N N   . LEU B 183 ? 0.1772 0.1604 0.2413 -0.0148 -0.0009 0.0707  175 LEU B N   
6104  C CA  . LEU B 183 ? 0.1347 0.1289 0.1978 -0.0131 0.0025  0.0674  175 LEU B CA  
6105  C C   . LEU B 183 ? 0.2039 0.2068 0.2681 -0.0155 0.0073  0.0730  175 LEU B C   
6106  O O   . LEU B 183 ? 0.2008 0.2036 0.2610 -0.0152 0.0091  0.0782  175 LEU B O   
6107  C CB  . LEU B 183 ? 0.1779 0.1734 0.2337 -0.0077 0.0027  0.0635  175 LEU B CB  
6108  C CG  . LEU B 183 ? 0.1923 0.1965 0.2453 -0.0061 0.0058  0.0599  175 LEU B CG  
6109  C CD1 . LEU B 183 ? 0.1954 0.2007 0.2520 -0.0067 0.0046  0.0547  175 LEU B CD1 
6110  C CD2 . LEU B 183 ? 0.1647 0.1702 0.2105 -0.0021 0.0057  0.0573  175 LEU B CD2 
6111  N N   . ILE B 184 ? 0.1711 0.1819 0.2405 -0.0174 0.0093  0.0722  176 ILE B N   
6112  C CA  . ILE B 184 ? 0.1292 0.1497 0.2010 -0.0193 0.0141  0.0773  176 ILE B CA  
6113  C C   . ILE B 184 ? 0.2289 0.2581 0.3005 -0.0163 0.0169  0.0732  176 ILE B C   
6114  O O   . ILE B 184 ? 0.1668 0.1974 0.2432 -0.0166 0.0151  0.0696  176 ILE B O   
6115  C CB  . ILE B 184 ? 0.1634 0.1855 0.2442 -0.0258 0.0136  0.0824  176 ILE B CB  
6116  C CG1 . ILE B 184 ? 0.1768 0.1880 0.2564 -0.0290 0.0110  0.0874  176 ILE B CG1 
6117  C CG2 . ILE B 184 ? 0.1814 0.2169 0.2655 -0.0272 0.0192  0.0871  176 ILE B CG2 
6118  C CD1 . ILE B 184 ? 0.2094 0.2197 0.2977 -0.0367 0.0095  0.0921  176 ILE B CD1 
6119  N N   . VAL B 185 ? 0.1408 0.1750 0.2063 -0.0132 0.0211  0.0735  177 VAL B N   
6120  C CA  . VAL B 185 ? 0.1492 0.1890 0.2124 -0.0094 0.0238  0.0693  177 VAL B CA  
6121  C C   . VAL B 185 ? 0.1450 0.1956 0.2116 -0.0095 0.0289  0.0729  177 VAL B C   
6122  O O   . VAL B 185 ? 0.1296 0.1839 0.1941 -0.0105 0.0320  0.0778  177 VAL B O   
6123  C CB  . VAL B 185 ? 0.1623 0.1988 0.2151 -0.0057 0.0245  0.0656  177 VAL B CB  
6124  C CG1 . VAL B 185 ? 0.1696 0.2096 0.2188 -0.0023 0.0274  0.0615  177 VAL B CG1 
6125  C CG2 . VAL B 185 ? 0.1502 0.1785 0.2008 -0.0054 0.0197  0.0620  177 VAL B CG2 
6126  N N   . LEU B 186 ? 0.1533 0.2099 0.2251 -0.0081 0.0299  0.0708  178 LEU B N   
6127  C CA  . LEU B 186 ? 0.1386 0.2066 0.2126 -0.0058 0.0352  0.0726  178 LEU B CA  
6128  C C   . LEU B 186 ? 0.1721 0.2382 0.2381 0.0002  0.0373  0.0671  178 LEU B C   
6129  O O   . LEU B 186 ? 0.1918 0.2535 0.2576 0.0022  0.0348  0.0627  178 LEU B O   
6130  C CB  . LEU B 186 ? 0.1206 0.1978 0.2066 -0.0077 0.0349  0.0745  178 LEU B CB  
6131  C CG  . LEU B 186 ? 0.1196 0.2015 0.2145 -0.0146 0.0342  0.0809  178 LEU B CG  
6132  C CD1 . LEU B 186 ? 0.2018 0.2719 0.2977 -0.0192 0.0280  0.0803  178 LEU B CD1 
6133  C CD2 . LEU B 186 ? 0.1597 0.2561 0.2666 -0.0159 0.0356  0.0831  178 LEU B CD2 
6134  N N   . TYR B 187 ? 0.1446 0.2132 0.2031 0.0028  0.0417  0.0674  179 TYR B N   
6135  C CA  . TYR B 187 ? 0.1559 0.2211 0.2051 0.0080  0.0437  0.0620  179 TYR B CA  
6136  C C   . TYR B 187 ? 0.1295 0.2038 0.1816 0.0126  0.0484  0.0616  179 TYR B C   
6137  O O   . TYR B 187 ? 0.1462 0.2309 0.2007 0.0128  0.0529  0.0655  179 TYR B O   
6138  C CB  . TYR B 187 ? 0.1844 0.2470 0.2228 0.0081  0.0453  0.0619  179 TYR B CB  
6139  C CG  . TYR B 187 ? 0.1307 0.1923 0.1588 0.0128  0.0488  0.0572  179 TYR B CG  
6140  C CD1 . TYR B 187 ? 0.1761 0.2317 0.2012 0.0163  0.0483  0.0514  179 TYR B CD1 
6141  C CD2 . TYR B 187 ? 0.1377 0.2033 0.1581 0.0136  0.0524  0.0586  179 TYR B CD2 
6142  C CE1 . TYR B 187 ? 0.1844 0.2368 0.1991 0.0203  0.0513  0.0466  179 TYR B CE1 
6143  C CE2 . TYR B 187 ? 0.1559 0.2198 0.1659 0.0177  0.0553  0.0536  179 TYR B CE2 
6144  C CZ  . TYR B 187 ? 0.1984 0.2550 0.2055 0.0210  0.0547  0.0474  179 TYR B CZ  
6145  O OH  . TYR B 187 ? 0.1973 0.2503 0.1933 0.0248  0.0574  0.0420  179 TYR B OH  
6146  N N   . ASP B 188 ? 0.1497 0.2202 0.2015 0.0165  0.0475  0.0571  180 ASP B N   
6147  C CA  . ASP B 188 ? 0.1244 0.2013 0.1780 0.0227  0.0513  0.0557  180 ASP B CA  
6148  C C   . ASP B 188 ? 0.1452 0.2190 0.1868 0.0272  0.0556  0.0520  180 ASP B C   
6149  O O   . ASP B 188 ? 0.1937 0.2567 0.2266 0.0302  0.0548  0.0466  180 ASP B O   
6150  C CB  . ASP B 188 ? 0.1221 0.1933 0.1779 0.0254  0.0480  0.0525  180 ASP B CB  
6151  C CG  . ASP B 188 ? 0.2371 0.3160 0.2970 0.0323  0.0513  0.0519  180 ASP B CG  
6152  O OD1 . ASP B 188 ? 0.2798 0.3724 0.3458 0.0334  0.0554  0.0553  180 ASP B OD1 
6153  O OD2 . ASP B 188 ? 0.2136 0.2851 0.2705 0.0369  0.0499  0.0484  180 ASP B OD2 
6154  N N   . ASP B 189 ? 0.1631 0.2465 0.2037 0.0274  0.0603  0.0550  181 ASP B N   
6155  C CA  . ASP B 189 ? 0.1592 0.2406 0.1873 0.0310  0.0644  0.0517  181 ASP B CA  
6156  C C   . ASP B 189 ? 0.1531 0.2409 0.1815 0.0390  0.0695  0.0490  181 ASP B C   
6157  O O   . ASP B 189 ? 0.1892 0.2912 0.2216 0.0409  0.0746  0.0523  181 ASP B O   
6158  C CB  . ASP B 189 ? 0.2052 0.2939 0.2313 0.0270  0.0666  0.0567  181 ASP B CB  
6159  C CG  . ASP B 189 ? 0.2505 0.3383 0.2629 0.0302  0.0704  0.0535  181 ASP B CG  
6160  O OD1 . ASP B 189 ? 0.2325 0.3142 0.2371 0.0357  0.0719  0.0469  181 ASP B OD1 
6161  O OD2 . ASP B 189 ? 0.2817 0.3744 0.2905 0.0271  0.0717  0.0576  181 ASP B OD2 
6162  N N   . ASN B 190 ? 0.1569 0.2342 0.1807 0.0439  0.0682  0.0433  182 ASN B N   
6163  C CA  . ASN B 190 ? 0.1634 0.2457 0.1891 0.0526  0.0723  0.0409  182 ASN B CA  
6164  C C   . ASN B 190 ? 0.2435 0.3153 0.2547 0.0590  0.0751  0.0337  182 ASN B C   
6165  O O   . ASN B 190 ? 0.2696 0.3420 0.2809 0.0673  0.0779  0.0308  182 ASN B O   
6166  C CB  . ASN B 190 ? 0.1584 0.2388 0.1932 0.0546  0.0686  0.0413  182 ASN B CB  
6167  C CG  . ASN B 190 ? 0.2362 0.2977 0.2635 0.0535  0.0635  0.0370  182 ASN B CG  
6168  O OD1 . ASN B 190 ? 0.2202 0.2697 0.2353 0.0520  0.0631  0.0329  182 ASN B OD1 
6169  N ND2 . ASN B 190 ? 0.1943 0.2538 0.2288 0.0538  0.0596  0.0381  182 ASN B ND2 
6170  N N   . ASN B 191 ? 0.2227 0.2847 0.2215 0.0555  0.0741  0.0306  183 ASN B N   
6171  C CA  . ASN B 191 ? 0.2343 0.2875 0.2183 0.0603  0.0769  0.0236  183 ASN B CA  
6172  C C   . ASN B 191 ? 0.2555 0.2915 0.2334 0.0647  0.0747  0.0174  183 ASN B C   
6173  O O   . ASN B 191 ? 0.2984 0.3257 0.2646 0.0701  0.0772  0.0110  183 ASN B O   
6174  C CB  . ASN B 191 ? 0.2995 0.3663 0.2827 0.0671  0.0842  0.0234  183 ASN B CB  
6175  C CG  . ASN B 191 ? 0.4327 0.4921 0.3990 0.0706  0.0871  0.0164  183 ASN B CG  
6176  O OD1 . ASN B 191 ? 0.3976 0.4504 0.3544 0.0649  0.0847  0.0149  183 ASN B OD1 
6177  N ND2 . ASN B 191 ? 0.4751 0.5359 0.4376 0.0802  0.0922  0.0118  183 ASN B ND2 
6178  N N   . ILE B 192 ? 0.2876 0.3172 0.2722 0.0623  0.0699  0.0191  184 ILE B N   
6179  C CA  . ILE B 192 ? 0.3507 0.3646 0.3307 0.0666  0.0678  0.0148  184 ILE B CA  
6180  C C   . ILE B 192 ? 0.3088 0.3104 0.2869 0.0589  0.0617  0.0148  184 ILE B C   
6181  O O   . ILE B 192 ? 0.2741 0.2824 0.2610 0.0529  0.0586  0.0196  184 ILE B O   
6182  C CB  . ILE B 192 ? 0.3399 0.3612 0.3312 0.0738  0.0688  0.0175  184 ILE B CB  
6183  C CG1 . ILE B 192 ? 0.3366 0.3674 0.3274 0.0836  0.0753  0.0156  184 ILE B CG1 
6184  C CG2 . ILE B 192 ? 0.3995 0.4043 0.3880 0.0760  0.0648  0.0154  184 ILE B CG2 
6185  C CD1 . ILE B 192 ? 0.4125 0.4267 0.3876 0.0900  0.0774  0.0075  184 ILE B CD1 
6186  N N   . SER B 193 ? 0.2830 0.2663 0.2493 0.0588  0.0599  0.0093  185 SER B N   
6187  C CA  . SER B 193 ? 0.3352 0.3073 0.3010 0.0529  0.0545  0.0097  185 SER B CA  
6188  C C   . SER B 193 ? 0.3882 0.3432 0.3474 0.0581  0.0537  0.0064  185 SER B C   
6189  O O   . SER B 193 ? 0.3531 0.3067 0.3105 0.0671  0.0572  0.0042  185 SER B O   
6190  C CB  . SER B 193 ? 0.3429 0.3103 0.3012 0.0441  0.0519  0.0078  185 SER B CB  
6191  O OG  . SER B 193 ? 0.3488 0.3032 0.2929 0.0443  0.0527  0.0013  185 SER B OG  
6192  N N   . ILE B 194 ? 0.3644 0.3067 0.3201 0.0527  0.0494  0.0062  186 ILE B N   
6193  C CA  . ILE B 194 ? 0.3439 0.2695 0.2943 0.0573  0.0481  0.0046  186 ILE B CA  
6194  C C   . ILE B 194 ? 0.3156 0.2264 0.2525 0.0621  0.0508  -0.0021 186 ILE B C   
6195  O O   . ILE B 194 ? 0.3566 0.2580 0.2907 0.0709  0.0520  -0.0036 186 ILE B O   
6196  C CB  . ILE B 194 ? 0.3738 0.2889 0.3218 0.0492  0.0432  0.0061  186 ILE B CB  
6197  C CG1 . ILE B 194 ? 0.3983 0.3271 0.3592 0.0462  0.0406  0.0121  186 ILE B CG1 
6198  C CG2 . ILE B 194 ? 0.3588 0.2536 0.2985 0.0529  0.0419  0.0045  186 ILE B CG2 
6199  C CD1 . ILE B 194 ? 0.4173 0.3374 0.3761 0.0395  0.0363  0.0138  186 ILE B CD1 
6200  N N   . ASP B 195 ? 0.3136 0.2219 0.2416 0.0571  0.0515  -0.0065 187 ASP B N   
6201  C CA  . ASP B 195 ? 0.3641 0.2569 0.2776 0.0606  0.0534  -0.0139 187 ASP B CA  
6202  C C   . ASP B 195 ? 0.3302 0.2317 0.2437 0.0709  0.0590  -0.0163 187 ASP B C   
6203  O O   . ASP B 195 ? 0.3715 0.2592 0.2732 0.0765  0.0611  -0.0228 187 ASP B O   
6204  C CB  . ASP B 195 ? 0.3893 0.2774 0.2930 0.0509  0.0516  -0.0180 187 ASP B CB  
6205  C CG  . ASP B 195 ? 0.4312 0.3021 0.3285 0.0424  0.0469  -0.0190 187 ASP B CG  
6206  O OD1 . ASP B 195 ? 0.3960 0.2620 0.2983 0.0424  0.0447  -0.0148 187 ASP B OD1 
6207  O OD2 . ASP B 195 ? 0.4369 0.2994 0.3236 0.0355  0.0454  -0.0239 187 ASP B OD2 
6208  N N   . GLY B 196 ? 0.3513 0.2749 0.2772 0.0733  0.0616  -0.0113 188 GLY B N   
6209  C CA  . GLY B 196 ? 0.3594 0.2948 0.2866 0.0827  0.0674  -0.0127 188 GLY B CA  
6210  C C   . GLY B 196 ? 0.3789 0.3362 0.3127 0.0791  0.0700  -0.0091 188 GLY B C   
6211  O O   . GLY B 196 ? 0.3419 0.3088 0.2848 0.0717  0.0672  -0.0034 188 GLY B O   
6212  N N   . LYS B 197 ? 0.3865 0.3513 0.3152 0.0846  0.0753  -0.0123 189 LYS B N   
6213  C CA  . LYS B 197 ? 0.3236 0.3077 0.2563 0.0808  0.0778  -0.0086 189 LYS B CA  
6214  C C   . LYS B 197 ? 0.3368 0.3156 0.2618 0.0703  0.0740  -0.0096 189 LYS B C   
6215  O O   . LYS B 197 ? 0.3513 0.3147 0.2624 0.0687  0.0725  -0.0164 189 LYS B O   
6216  C CB  . LYS B 197 ? 0.3777 0.3707 0.3047 0.0891  0.0847  -0.0121 189 LYS B CB  
6217  N N   . VAL B 198 ? 0.2965 0.2882 0.2306 0.0634  0.0722  -0.0030 190 VAL B N   
6218  C CA  . VAL B 198 ? 0.3029 0.2900 0.2329 0.0537  0.0673  -0.0029 190 VAL B CA  
6219  C C   . VAL B 198 ? 0.2724 0.2596 0.1892 0.0516  0.0685  -0.0072 190 VAL B C   
6220  O O   . VAL B 198 ? 0.2780 0.2594 0.1890 0.0444  0.0642  -0.0088 190 VAL B O   
6221  C CB  . VAL B 198 ? 0.3040 0.3041 0.2470 0.0478  0.0650  0.0052  190 VAL B CB  
6222  C CG1 . VAL B 198 ? 0.3178 0.3162 0.2725 0.0480  0.0624  0.0088  190 VAL B CG1 
6223  C CG2 . VAL B 198 ? 0.3162 0.3346 0.2647 0.0498  0.0695  0.0102  190 VAL B CG2 
6224  N N   . ASP B 199 ? 0.2805 0.2751 0.1921 0.0578  0.0740  -0.0091 191 ASP B N   
6225  C CA  . ASP B 199 ? 0.3303 0.3283 0.2298 0.0556  0.0751  -0.0121 191 ASP B CA  
6226  C C   . ASP B 199 ? 0.3467 0.3270 0.2308 0.0527  0.0719  -0.0209 191 ASP B C   
6227  O O   . ASP B 199 ? 0.3917 0.3741 0.2662 0.0485  0.0707  -0.0232 191 ASP B O   
6228  C CB  . ASP B 199 ? 0.5340 0.5435 0.4304 0.0636  0.0823  -0.0129 191 ASP B CB  
6229  C CG  . ASP B 199 ? 0.6778 0.7052 0.5901 0.0659  0.0856  -0.0042 191 ASP B CG  
6230  O OD1 . ASP B 199 ? 0.6988 0.7388 0.6168 0.0605  0.0851  0.0028  191 ASP B OD1 
6231  O OD2 . ASP B 199 ? 0.7102 0.7388 0.6298 0.0728  0.0882  -0.0042 191 ASP B OD2 
6232  N N   . GLY B 200 ? 0.3141 0.2770 0.1955 0.0544  0.0701  -0.0256 192 GLY B N   
6233  C CA  . GLY B 200 ? 0.3687 0.3139 0.2362 0.0497  0.0664  -0.0333 192 GLY B CA  
6234  C C   . GLY B 200 ? 0.3237 0.2669 0.1937 0.0387  0.0600  -0.0311 192 GLY B C   
6235  O O   . GLY B 200 ? 0.3157 0.2469 0.1747 0.0332  0.0566  -0.0371 192 GLY B O   
6236  N N   . TRP B 201 ? 0.2706 0.2254 0.1545 0.0355  0.0583  -0.0230 193 TRP B N   
6237  C CA  . TRP B 201 ? 0.2609 0.2150 0.1478 0.0262  0.0526  -0.0210 193 TRP B CA  
6238  C C   . TRP B 201 ? 0.2812 0.2522 0.1803 0.0236  0.0516  -0.0127 193 TRP B C   
6239  O O   . TRP B 201 ? 0.2839 0.2564 0.1859 0.0168  0.0471  -0.0109 193 TRP B O   
6240  C CB  . TRP B 201 ? 0.2606 0.2006 0.1508 0.0242  0.0498  -0.0214 193 TRP B CB  
6241  C CG  . TRP B 201 ? 0.2685 0.2102 0.1696 0.0308  0.0521  -0.0169 193 TRP B CG  
6242  C CD1 . TRP B 201 ? 0.2385 0.1910 0.1539 0.0301  0.0512  -0.0096 193 TRP B CD1 
6243  C CD2 . TRP B 201 ? 0.2656 0.1984 0.1641 0.0394  0.0555  -0.0197 193 TRP B CD2 
6244  N NE1 . TRP B 201 ? 0.2610 0.2128 0.1830 0.0371  0.0536  -0.0076 193 TRP B NE1 
6245  C CE2 . TRP B 201 ? 0.2764 0.2165 0.1886 0.0433  0.0563  -0.0135 193 TRP B CE2 
6246  C CE3 . TRP B 201 ? 0.2868 0.2057 0.1725 0.0445  0.0577  -0.0272 193 TRP B CE3 
6247  C CZ2 . TRP B 201 ? 0.2930 0.2287 0.2073 0.0524  0.0591  -0.0140 193 TRP B CZ2 
6248  C CZ3 . TRP B 201 ? 0.4022 0.3153 0.2895 0.0542  0.0608  -0.0280 193 TRP B CZ3 
6249  C CH2 . TRP B 201 ? 0.3292 0.2515 0.2310 0.0582  0.0615  -0.0212 193 TRP B CH2 
6250  N N   . PHE B 202 ? 0.2352 0.2188 0.1414 0.0286  0.0556  -0.0076 194 PHE B N   
6251  C CA  . PHE B 202 ? 0.2351 0.2322 0.1530 0.0259  0.0544  0.0005  194 PHE B CA  
6252  C C   . PHE B 202 ? 0.3007 0.3112 0.2184 0.0297  0.0591  0.0040  194 PHE B C   
6253  O O   . PHE B 202 ? 0.2220 0.2365 0.1435 0.0357  0.0637  0.0051  194 PHE B O   
6254  C CB  . PHE B 202 ? 0.2067 0.2037 0.1381 0.0267  0.0536  0.0049  194 PHE B CB  
6255  C CG  . PHE B 202 ? 0.2239 0.2323 0.1670 0.0238  0.0520  0.0126  194 PHE B CG  
6256  C CD1 . PHE B 202 ? 0.2085 0.2197 0.1513 0.0181  0.0479  0.0142  194 PHE B CD1 
6257  C CD2 . PHE B 202 ? 0.2838 0.3001 0.2384 0.0268  0.0542  0.0179  194 PHE B CD2 
6258  C CE1 . PHE B 202 ? 0.2404 0.2598 0.1933 0.0160  0.0462  0.0208  194 PHE B CE1 
6259  C CE2 . PHE B 202 ? 0.2938 0.3186 0.2587 0.0236  0.0524  0.0246  194 PHE B CE2 
6260  C CZ  . PHE B 202 ? 0.2679 0.2932 0.2315 0.0185  0.0485  0.0259  194 PHE B CZ  
6261  N N   . THR B 203 ? 0.2205 0.2384 0.1333 0.0264  0.0579  0.0058  195 THR B N   
6262  C CA  . THR B 203 ? 0.2561 0.2867 0.1667 0.0291  0.0622  0.0095  195 THR B CA  
6263  C C   . THR B 203 ? 0.2146 0.2549 0.1303 0.0247  0.0597  0.0173  195 THR B C   
6264  O O   . THR B 203 ? 0.2198 0.2691 0.1300 0.0252  0.0617  0.0203  195 THR B O   
6265  C CB  . THR B 203 ? 0.2980 0.3265 0.1919 0.0311  0.0644  0.0027  195 THR B CB  
6266  O OG1 . THR B 203 ? 0.2449 0.2675 0.1305 0.0255  0.0589  -0.0015 195 THR B OG1 
6267  C CG2 . THR B 203 ? 0.2532 0.2718 0.1418 0.0372  0.0679  -0.0047 195 THR B CG2 
6268  N N   . GLU B 204 ? 0.2022 0.2405 0.1277 0.0209  0.0552  0.0207  196 GLU B N   
6269  C CA  . GLU B 204 ? 0.1948 0.2403 0.1251 0.0175  0.0523  0.0277  196 GLU B CA  
6270  C C   . GLU B 204 ? 0.2464 0.3021 0.1830 0.0192  0.0564  0.0355  196 GLU B C   
6271  O O   . GLU B 204 ? 0.2032 0.2610 0.1470 0.0219  0.0601  0.0369  196 GLU B O   
6272  C CB  . GLU B 204 ? 0.1827 0.2237 0.1230 0.0141  0.0474  0.0291  196 GLU B CB  
6273  C CG  . GLU B 204 ? 0.2238 0.2568 0.1586 0.0111  0.0432  0.0225  196 GLU B CG  
6274  C CD  . GLU B 204 ? 0.2413 0.2714 0.1857 0.0081  0.0389  0.0239  196 GLU B CD  
6275  O OE1 . GLU B 204 ? 0.2281 0.2627 0.1820 0.0080  0.0382  0.0301  196 GLU B OE1 
6276  O OE2 . GLU B 204 ? 0.2347 0.2580 0.1766 0.0055  0.0363  0.0189  196 GLU B OE2 
6277  N N   . ASN B 205 ? 0.1949 0.2574 0.1286 0.0175  0.0556  0.0410  197 ASN B N   
6278  C CA  . ASN B 205 ? 0.1930 0.2642 0.1334 0.0172  0.0583  0.0501  197 ASN B CA  
6279  C C   . ASN B 205 ? 0.1878 0.2558 0.1405 0.0140  0.0538  0.0549  197 ASN B C   
6280  O O   . ASN B 205 ? 0.2138 0.2806 0.1659 0.0117  0.0494  0.0579  197 ASN B O   
6281  C CB  . ASN B 205 ? 0.2025 0.2809 0.1330 0.0168  0.0592  0.0543  197 ASN B CB  
6282  C CG  . ASN B 205 ? 0.2339 0.3211 0.1700 0.0159  0.0627  0.0643  197 ASN B CG  
6283  O OD1 . ASN B 205 ? 0.2057 0.2923 0.1543 0.0140  0.0620  0.0694  197 ASN B OD1 
6284  N ND2 . ASN B 205 ? 0.2256 0.3210 0.1519 0.0170  0.0663  0.0673  197 ASN B ND2 
6285  N N   . ILE B 206 ? 0.1739 0.2402 0.1375 0.0143  0.0547  0.0550  198 ILE B N   
6286  C CA  . ILE B 206 ? 0.2058 0.2677 0.1802 0.0114  0.0501  0.0577  198 ILE B CA  
6287  C C   . ILE B 206 ? 0.1957 0.2610 0.1742 0.0088  0.0490  0.0665  198 ILE B C   
6288  O O   . ILE B 206 ? 0.1853 0.2458 0.1657 0.0069  0.0439  0.0678  198 ILE B O   
6289  C CB  . ILE B 206 ? 0.1571 0.2173 0.1414 0.0124  0.0512  0.0561  198 ILE B CB  
6290  C CG1 . ILE B 206 ? 0.1579 0.2109 0.1371 0.0146  0.0507  0.0476  198 ILE B CG1 
6291  C CG2 . ILE B 206 ? 0.1480 0.2051 0.1435 0.0092  0.0470  0.0595  198 ILE B CG2 
6292  C CD1 . ILE B 206 ? 0.1555 0.2010 0.1306 0.0121  0.0453  0.0437  198 ILE B CD1 
6293  N N   . PRO B 207 ? 0.1690 0.2421 0.1488 0.0084  0.0533  0.0729  199 PRO B N   
6294  C CA  . PRO B 207 ? 0.1718 0.2461 0.1540 0.0053  0.0518  0.0818  199 PRO B CA  
6295  C C   . PRO B 207 ? 0.2049 0.2763 0.1776 0.0054  0.0479  0.0828  199 PRO B C   
6296  O O   . PRO B 207 ? 0.1955 0.2617 0.1718 0.0038  0.0433  0.0867  199 PRO B O   
6297  C CB  . PRO B 207 ? 0.1881 0.2730 0.1700 0.0050  0.0583  0.0875  199 PRO B CB  
6298  C CG  . PRO B 207 ? 0.2038 0.2926 0.1910 0.0075  0.0621  0.0825  199 PRO B CG  
6299  C CD  . PRO B 207 ? 0.1723 0.2538 0.1530 0.0107  0.0599  0.0728  199 PRO B CD  
6300  N N   . GLN B 208 ? 0.1838 0.2585 0.1444 0.0077  0.0493  0.0788  200 GLN B N   
6301  C CA  . GLN B 208 ? 0.2033 0.2773 0.1549 0.0079  0.0453  0.0796  200 GLN B CA  
6302  C C   . GLN B 208 ? 0.1818 0.2489 0.1363 0.0077  0.0391  0.0746  200 GLN B C   
6303  O O   . GLN B 208 ? 0.1829 0.2482 0.1371 0.0076  0.0345  0.0779  200 GLN B O   
6304  C CB  . GLN B 208 ? 0.2176 0.2973 0.1553 0.0099  0.0480  0.0756  200 GLN B CB  
6305  C CG  . GLN B 208 ? 0.2928 0.3747 0.2204 0.0101  0.0442  0.0779  200 GLN B CG  
6306  C CD  . GLN B 208 ? 0.3243 0.4123 0.2373 0.0118  0.0470  0.0738  200 GLN B CD  
6307  O OE1 . GLN B 208 ? 0.2571 0.3441 0.1667 0.0130  0.0496  0.0656  200 GLN B OE1 
6308  N NE2 . GLN B 208 ? 0.3262 0.4199 0.2299 0.0121  0.0463  0.0794  200 GLN B NE2 
6309  N N   . ARG B 209 ? 0.1752 0.2386 0.1323 0.0080  0.0391  0.0667  201 ARG B N   
6310  C CA  . ARG B 209 ? 0.1809 0.2389 0.1413 0.0073  0.0339  0.0621  201 ARG B CA  
6311  C C   . ARG B 209 ? 0.2113 0.2654 0.1823 0.0064  0.0307  0.0669  201 ARG B C   
6312  O O   . ARG B 209 ? 0.1623 0.2146 0.1340 0.0067  0.0259  0.0671  201 ARG B O   
6313  C CB  . ARG B 209 ? 0.1741 0.2281 0.1355 0.0073  0.0351  0.0541  201 ARG B CB  
6314  C CG  . ARG B 209 ? 0.1556 0.2046 0.1221 0.0060  0.0305  0.0501  201 ARG B CG  
6315  C CD  . ARG B 209 ? 0.1694 0.2134 0.1361 0.0057  0.0318  0.0432  201 ARG B CD  
6316  N NE  . ARG B 209 ? 0.1626 0.2027 0.1359 0.0041  0.0280  0.0411  201 ARG B NE  
6317  C CZ  . ARG B 209 ? 0.1806 0.2157 0.1577 0.0037  0.0285  0.0377  201 ARG B CZ  
6318  N NH1 . ARG B 209 ? 0.1601 0.1928 0.1353 0.0053  0.0323  0.0357  201 ARG B NH1 
6319  N NH2 . ARG B 209 ? 0.1822 0.2148 0.1645 0.0022  0.0252  0.0362  201 ARG B NH2 
6320  N N   . PHE B 210 ? 0.1594 0.2125 0.1386 0.0054  0.0332  0.0707  202 PHE B N   
6321  C CA  . PHE B 210 ? 0.1550 0.2028 0.1437 0.0042  0.0298  0.0741  202 PHE B CA  
6322  C C   . PHE B 210 ? 0.1625 0.2095 0.1500 0.0039  0.0279  0.0823  202 PHE B C   
6323  O O   . PHE B 210 ? 0.1857 0.2269 0.1770 0.0043  0.0234  0.0836  202 PHE B O   
6324  C CB  . PHE B 210 ? 0.1497 0.1965 0.1480 0.0026  0.0321  0.0746  202 PHE B CB  
6325  C CG  . PHE B 210 ? 0.1819 0.2255 0.1837 0.0030  0.0309  0.0672  202 PHE B CG  
6326  C CD1 . PHE B 210 ? 0.1414 0.1864 0.1371 0.0045  0.0330  0.0611  202 PHE B CD1 
6327  C CD2 . PHE B 210 ? 0.1354 0.1737 0.1451 0.0020  0.0273  0.0663  202 PHE B CD2 
6328  C CE1 . PHE B 210 ? 0.1614 0.2023 0.1593 0.0046  0.0317  0.0551  202 PHE B CE1 
6329  C CE2 . PHE B 210 ? 0.1289 0.1646 0.1406 0.0023  0.0262  0.0601  202 PHE B CE2 
6330  C CZ  . PHE B 210 ? 0.1984 0.2353 0.2043 0.0035  0.0284  0.0549  202 PHE B CZ  
6331  N N   . GLU B 211 ? 0.1801 0.2324 0.1612 0.0038  0.0312  0.0876  203 GLU B N   
6332  C CA  . GLU B 211 ? 0.1804 0.2314 0.1577 0.0040  0.0289  0.0953  203 GLU B CA  
6333  C C   . GLU B 211 ? 0.2237 0.2738 0.1956 0.0069  0.0237  0.0924  203 GLU B C   
6334  O O   . GLU B 211 ? 0.1869 0.2323 0.1600 0.0082  0.0195  0.0970  203 GLU B O   
6335  C CB  . GLU B 211 ? 0.3130 0.3713 0.2824 0.0034  0.0336  0.1013  203 GLU B CB  
6336  C CG  . GLU B 211 ? 0.4445 0.5054 0.4205 0.0002  0.0386  0.1061  203 GLU B CG  
6337  C CD  . GLU B 211 ? 0.5746 0.6399 0.5454 -0.0014 0.0414  0.1140  203 GLU B CD  
6338  O OE1 . GLU B 211 ? 0.6093 0.6765 0.5696 0.0005  0.0401  0.1153  203 GLU B OE1 
6339  O OE2 . GLU B 211 ? 0.6334 0.6999 0.6110 -0.0048 0.0440  0.1171  203 GLU B OE2 
6340  N N   . SER B 212 ? 0.1780 0.2325 0.1444 0.0080  0.0236  0.0846  204 SER B N   
6341  C CA  . SER B 212 ? 0.1788 0.2350 0.1410 0.0102  0.0185  0.0819  204 SER B CA  
6342  C C   . SER B 212 ? 0.1953 0.2461 0.1662 0.0111  0.0142  0.0792  204 SER B C   
6343  O O   . SER B 212 ? 0.1730 0.2253 0.1426 0.0136  0.0096  0.0790  204 SER B O   
6344  C CB  . SER B 212 ? 0.1784 0.2403 0.1326 0.0100  0.0192  0.0739  204 SER B CB  
6345  O OG  . SER B 212 ? 0.1799 0.2391 0.1392 0.0088  0.0188  0.0661  204 SER B OG  
6346  N N   . TYR B 213 ? 0.1638 0.2093 0.1434 0.0095  0.0154  0.0772  205 TYR B N   
6347  C CA  . TYR B 213 ? 0.1822 0.2224 0.1698 0.0104  0.0116  0.0748  205 TYR B CA  
6348  C C   . TYR B 213 ? 0.1866 0.2192 0.1788 0.0113  0.0094  0.0818  205 TYR B C   
6349  O O   . TYR B 213 ? 0.2132 0.2405 0.2115 0.0127  0.0061  0.0799  205 TYR B O   
6350  C CB  . TYR B 213 ? 0.1721 0.2096 0.1661 0.0083  0.0134  0.0694  205 TYR B CB  
6351  C CG  . TYR B 213 ? 0.1638 0.2053 0.1541 0.0073  0.0152  0.0621  205 TYR B CG  
6352  C CD1 . TYR B 213 ? 0.1959 0.2425 0.1797 0.0079  0.0132  0.0581  205 TYR B CD1 
6353  C CD2 . TYR B 213 ? 0.1397 0.1793 0.1330 0.0055  0.0184  0.0591  205 TYR B CD2 
6354  C CE1 . TYR B 213 ? 0.1612 0.2094 0.1412 0.0061  0.0145  0.0515  205 TYR B CE1 
6355  C CE2 . TYR B 213 ? 0.1419 0.1827 0.1313 0.0048  0.0198  0.0527  205 TYR B CE2 
6356  C CZ  . TYR B 213 ? 0.1838 0.2280 0.1663 0.0046  0.0178  0.0489  205 TYR B CZ  
6357  O OH  . TYR B 213 ? 0.1557 0.1993 0.1338 0.0030  0.0189  0.0426  205 TYR B OH  
6358  N N   . GLY B 214 ? 0.2022 0.2340 0.1917 0.0102  0.0114  0.0896  206 GLY B N   
6359  C CA  . GLY B 214 ? 0.2033 0.2258 0.1974 0.0096  0.0097  0.0966  206 GLY B CA  
6360  C C   . GLY B 214 ? 0.2305 0.2484 0.2331 0.0054  0.0119  0.0970  206 GLY B C   
6361  O O   . GLY B 214 ? 0.2048 0.2133 0.2126 0.0044  0.0095  0.1006  206 GLY B O   
6362  N N   . TRP B 215 ? 0.1944 0.2184 0.1986 0.0030  0.0162  0.0934  207 TRP B N   
6363  C CA  . TRP B 215 ? 0.1889 0.2109 0.2015 -0.0009 0.0184  0.0942  207 TRP B CA  
6364  C C   . TRP B 215 ? 0.2172 0.2416 0.2297 -0.0045 0.0221  0.1028  207 TRP B C   
6365  O O   . TRP B 215 ? 0.1975 0.2275 0.2022 -0.0038 0.0246  0.1069  207 TRP B O   
6366  C CB  . TRP B 215 ? 0.1543 0.1822 0.1691 -0.0011 0.0212  0.0870  207 TRP B CB  
6367  C CG  . TRP B 215 ? 0.1524 0.1771 0.1697 0.0006  0.0180  0.0793  207 TRP B CG  
6368  C CD1 . TRP B 215 ? 0.1546 0.1781 0.1682 0.0036  0.0144  0.0756  207 TRP B CD1 
6369  C CD2 . TRP B 215 ? 0.1379 0.1619 0.1617 -0.0006 0.0182  0.0744  207 TRP B CD2 
6370  N NE1 . TRP B 215 ? 0.1372 0.1593 0.1546 0.0040  0.0128  0.0690  207 TRP B NE1 
6371  C CE2 . TRP B 215 ? 0.1502 0.1719 0.1734 0.0015  0.0149  0.0682  207 TRP B CE2 
6372  C CE3 . TRP B 215 ? 0.1349 0.1609 0.1652 -0.0032 0.0207  0.0750  207 TRP B CE3 
6373  C CZ2 . TRP B 215 ? 0.1787 0.1991 0.2065 0.0009  0.0142  0.0629  207 TRP B CZ2 
6374  C CZ3 . TRP B 215 ? 0.1303 0.1551 0.1656 -0.0034 0.0195  0.0696  207 TRP B CZ3 
6375  C CH2 . TRP B 215 ? 0.1578 0.1793 0.1912 -0.0014 0.0163  0.0637  207 TRP B CH2 
6376  N N   . HIS B 216 ? 0.1731 0.1941 0.1944 -0.0087 0.0224  0.1055  208 HIS B N   
6377  C CA  . HIS B 216 ? 0.2582 0.2847 0.2820 -0.0133 0.0269  0.1126  208 HIS B CA  
6378  C C   . HIS B 216 ? 0.2010 0.2390 0.2273 -0.0132 0.0319  0.1080  208 HIS B C   
6379  O O   . HIS B 216 ? 0.1863 0.2237 0.2172 -0.0120 0.0307  0.1009  208 HIS B O   
6380  C CB  . HIS B 216 ? 0.1988 0.2169 0.2316 -0.0186 0.0244  0.1169  208 HIS B CB  
6381  C CG  . HIS B 216 ? 0.2257 0.2511 0.2640 -0.0239 0.0281  0.1196  208 HIS B CG  
6382  N ND1 . HIS B 216 ? 0.2460 0.2740 0.2946 -0.0274 0.0283  0.1172  208 HIS B ND1 
6383  C CD2 . HIS B 216 ? 0.2467 0.2778 0.2816 -0.0262 0.0314  0.1244  208 HIS B CD2 
6384  C CE1 . HIS B 216 ? 0.2242 0.2601 0.2761 -0.0316 0.0315  0.1204  208 HIS B CE1 
6385  N NE2 . HIS B 216 ? 0.2942 0.3320 0.3379 -0.0310 0.0337  0.1248  208 HIS B NE2 
6386  N N   . VAL B 217 ? 0.2279 0.2762 0.2502 -0.0136 0.0374  0.1117  209 VAL B N   
6387  C CA  . VAL B 217 ? 0.2207 0.2797 0.2440 -0.0120 0.0424  0.1071  209 VAL B CA  
6388  C C   . VAL B 217 ? 0.2202 0.2877 0.2492 -0.0156 0.0463  0.1111  209 VAL B C   
6389  O O   . VAL B 217 ? 0.2039 0.2725 0.2292 -0.0178 0.0472  0.1162  209 VAL B O   
6390  C CB  . VAL B 217 ? 0.2587 0.3227 0.2701 -0.0073 0.0450  0.1031  209 VAL B CB  
6391  C CG1 . VAL B 217 ? 0.1973 0.2706 0.2097 -0.0049 0.0502  0.0980  209 VAL B CG1 
6392  C CG2 . VAL B 217 ? 0.2431 0.2994 0.2493 -0.0041 0.0400  0.0968  209 VAL B CG2 
6393  N N   . VAL B 218 ? 0.2058 0.2797 0.2435 -0.0160 0.0484  0.1082  210 VAL B N   
6394  C CA  . VAL B 218 ? 0.2220 0.3074 0.2647 -0.0179 0.0526  0.1101  210 VAL B CA  
6395  C C   . VAL B 218 ? 0.2436 0.3391 0.2832 -0.0122 0.0578  0.1049  210 VAL B C   
6396  O O   . VAL B 218 ? 0.2153 0.3126 0.2605 -0.0100 0.0581  0.1006  210 VAL B O   
6397  C CB  . VAL B 218 ? 0.1801 0.2661 0.2362 -0.0229 0.0504  0.1114  210 VAL B CB  
6398  C CG1 . VAL B 218 ? 0.1715 0.2707 0.2327 -0.0255 0.0546  0.1143  210 VAL B CG1 
6399  C CG2 . VAL B 218 ? 0.2370 0.3097 0.2948 -0.0278 0.0447  0.1150  210 VAL B CG2 
6400  N N   . PRO B 219 ? 0.2393 0.3405 0.2692 -0.0095 0.0618  0.1050  211 PRO B N   
6401  C CA  . PRO B 219 ? 0.2401 0.3487 0.2651 -0.0035 0.0666  0.0992  211 PRO B CA  
6402  C C   . PRO B 219 ? 0.1845 0.3060 0.2169 -0.0027 0.0712  0.0991  211 PRO B C   
6403  O O   . PRO B 219 ? 0.2067 0.3336 0.2464 -0.0075 0.0713  0.1042  211 PRO B O   
6404  C CB  . PRO B 219 ? 0.2335 0.3423 0.2443 -0.0015 0.0683  0.0994  211 PRO B CB  
6405  C CG  . PRO B 219 ? 0.2399 0.3494 0.2521 -0.0069 0.0673  0.1071  211 PRO B CG  
6406  C CD  . PRO B 219 ? 0.2715 0.3727 0.2942 -0.0119 0.0622  0.1104  211 PRO B CD  
6407  N N   . ASN B 220 ? 0.2058 0.3321 0.2367 0.0036  0.0747  0.0931  212 ASN B N   
6408  C CA  A ASN B 220 ? 0.1740 0.3136 0.2086 0.0068  0.0799  0.0918  212 ASN B CA  
6409  C CA  B ASN B 220 ? 0.2406 0.3802 0.2751 0.0068  0.0799  0.0919  212 ASN B CA  
6410  C C   . ASN B 220 ? 0.1919 0.3394 0.2416 0.0024  0.0790  0.0958  212 ASN B C   
6411  O O   . ASN B 220 ? 0.2164 0.3749 0.2695 0.0006  0.0821  0.0992  212 ASN B O   
6412  C CB  A ASN B 220 ? 0.2929 0.4388 0.3176 0.0077  0.0840  0.0931  212 ASN B CB  
6413  C CB  B ASN B 220 ? 0.2890 0.4349 0.3138 0.0074  0.0840  0.0934  212 ASN B CB  
6414  C CG  A ASN B 220 ? 0.3131 0.4709 0.3374 0.0138  0.0900  0.0891  212 ASN B CG  
6415  C CG  B ASN B 220 ? 0.3059 0.4456 0.3151 0.0119  0.0849  0.0886  212 ASN B CG  
6416  O OD1 A ASN B 220 ? 0.2653 0.4232 0.2914 0.0197  0.0912  0.0833  212 ASN B OD1 
6417  O OD1 B ASN B 220 ? 0.3745 0.5106 0.3796 0.0174  0.0858  0.0819  212 ASN B OD1 
6418  N ND2 A ASN B 220 ? 0.2024 0.3701 0.2243 0.0127  0.0938  0.0922  212 ASN B ND2 
6419  N ND2 B ASN B 220 ? 0.3214 0.4596 0.3215 0.0093  0.0844  0.0920  212 ASN B ND2 
6420  N N   . VAL B 221 ? 0.1968 0.3392 0.2553 0.0007  0.0748  0.0953  213 VAL B N   
6421  C CA  . VAL B 221 ? 0.1582 0.3080 0.2309 -0.0033 0.0733  0.0980  213 VAL B CA  
6422  C C   . VAL B 221 ? 0.1834 0.3435 0.2616 0.0034  0.0764  0.0935  213 VAL B C   
6423  O O   . VAL B 221 ? 0.2037 0.3587 0.2784 0.0096  0.0767  0.0882  213 VAL B O   
6424  C CB  . VAL B 221 ? 0.2503 0.3895 0.3297 -0.0086 0.0668  0.0992  213 VAL B CB  
6425  C CG1 . VAL B 221 ? 0.2019 0.3495 0.2957 -0.0125 0.0649  0.1010  213 VAL B CG1 
6426  C CG2 . VAL B 221 ? 0.2211 0.3497 0.2953 -0.0144 0.0636  0.1037  213 VAL B CG2 
6427  N N   . ASN B 222 ? 0.1858 0.3602 0.2726 0.0025  0.0787  0.0956  214 ASN B N   
6428  C CA  . ASN B 222 ? 0.1560 0.3406 0.2499 0.0090  0.0807  0.0919  214 ASN B CA  
6429  C C   . ASN B 222 ? 0.1864 0.3666 0.2899 0.0074  0.0752  0.0910  214 ASN B C   
6430  O O   . ASN B 222 ? 0.1533 0.3370 0.2670 0.0006  0.0717  0.0946  214 ASN B O   
6431  C CB  . ASN B 222 ? 0.1812 0.3833 0.2828 0.0077  0.0840  0.0948  214 ASN B CB  
6432  C CG  . ASN B 222 ? 0.2482 0.4619 0.3562 0.0159  0.0864  0.0907  214 ASN B CG  
6433  O OD1 . ASN B 222 ? 0.1651 0.3732 0.2743 0.0212  0.0843  0.0866  214 ASN B OD1 
6434  N ND2 . ASN B 222 ? 0.2332 0.4629 0.3450 0.0173  0.0908  0.0919  214 ASN B ND2 
6435  N N   . GLY B 223 ? 0.1843 0.3563 0.2839 0.0137  0.0746  0.0861  215 GLY B N   
6436  C CA  . GLY B 223 ? 0.1308 0.2978 0.2380 0.0128  0.0695  0.0849  215 GLY B CA  
6437  C C   . GLY B 223 ? 0.1744 0.3538 0.2941 0.0147  0.0683  0.0847  215 GLY B C   
6438  O O   . GLY B 223 ? 0.1389 0.3152 0.2651 0.0140  0.0636  0.0838  215 GLY B O   
6439  N N   . HIS B 224 ? 0.2017 0.3956 0.3248 0.0173  0.0722  0.0854  216 HIS B N   
6440  C CA  . HIS B 224 ? 0.2200 0.4276 0.3555 0.0185  0.0709  0.0857  216 HIS B CA  
6441  C C   . HIS B 224 ? 0.1971 0.4164 0.3410 0.0098  0.0705  0.0909  216 HIS B C   
6442  O O   . HIS B 224 ? 0.1493 0.3830 0.3035 0.0103  0.0702  0.0915  216 HIS B O   
6443  C CB  . HIS B 224 ? 0.1397 0.3551 0.2734 0.0301  0.0754  0.0814  216 HIS B CB  
6444  C CG  . HIS B 224 ? 0.1802 0.3825 0.3057 0.0387  0.0754  0.0761  216 HIS B CG  
6445  N ND1 . HIS B 224 ? 0.1454 0.3396 0.2743 0.0390  0.0703  0.0750  216 HIS B ND1 
6446  C CD2 . HIS B 224 ? 0.1777 0.3726 0.2910 0.0466  0.0797  0.0716  216 HIS B CD2 
6447  C CE1 . HIS B 224 ? 0.1862 0.3686 0.3057 0.0469  0.0717  0.0704  216 HIS B CE1 
6448  N NE2 . HIS B 224 ? 0.1717 0.3537 0.2814 0.0516  0.0773  0.0680  216 HIS B NE2 
6449  N N   . ASP B 225 ? 0.2286 0.4417 0.3681 0.0018  0.0703  0.0948  217 ASP B N   
6450  C CA  . ASP B 225 ? 0.2171 0.4382 0.3629 -0.0075 0.0700  0.1002  217 ASP B CA  
6451  C C   . ASP B 225 ? 0.1730 0.3820 0.3220 -0.0166 0.0633  0.1024  217 ASP B C   
6452  O O   . ASP B 225 ? 0.1733 0.3678 0.3141 -0.0198 0.0619  0.1036  217 ASP B O   
6453  C CB  . ASP B 225 ? 0.1733 0.3952 0.3101 -0.0086 0.0751  0.1030  217 ASP B CB  
6454  C CG  . ASP B 225 ? 0.2151 0.4443 0.3575 -0.0185 0.0752  0.1092  217 ASP B CG  
6455  O OD1 . ASP B 225 ? 0.2390 0.4706 0.3916 -0.0253 0.0709  0.1112  217 ASP B OD1 
6456  O OD2 . ASP B 225 ? 0.2195 0.4519 0.3557 -0.0195 0.0796  0.1120  217 ASP B OD2 
6457  N N   . THR B 226 ? 0.1689 0.3837 0.3292 -0.0205 0.0588  0.1026  218 THR B N   
6458  C CA  . THR B 226 ? 0.2031 0.4053 0.3658 -0.0286 0.0521  0.1034  218 THR B CA  
6459  C C   . THR B 226 ? 0.2662 0.4622 0.4268 -0.0382 0.0515  0.1085  218 THR B C   
6460  O O   . THR B 226 ? 0.2670 0.4469 0.4238 -0.0430 0.0471  0.1089  218 THR B O   
6461  C CB  . THR B 226 ? 0.2116 0.4220 0.3863 -0.0310 0.0472  0.1022  218 THR B CB  
6462  O OG1 . THR B 226 ? 0.2160 0.4439 0.3993 -0.0343 0.0494  0.1050  218 THR B OG1 
6463  C CG2 . THR B 226 ? 0.2137 0.4270 0.3895 -0.0212 0.0468  0.0974  218 THR B CG2 
6464  N N   . ALA B 227 ? 0.2171 0.4252 0.3797 -0.0409 0.0557  0.1123  219 ALA B N   
6465  C CA  . ALA B 227 ? 0.1671 0.3686 0.3263 -0.0495 0.0557  0.1176  219 ALA B CA  
6466  C C   . ALA B 227 ? 0.1997 0.3864 0.3454 -0.0469 0.0571  0.1180  219 ALA B C   
6467  O O   . ALA B 227 ? 0.2364 0.4078 0.3777 -0.0525 0.0536  0.1203  219 ALA B O   
6468  C CB  . ALA B 227 ? 0.1771 0.3960 0.3407 -0.0522 0.0609  0.1216  219 ALA B CB  
6469  N N   . ALA B 228 ? 0.2537 0.4446 0.3923 -0.0381 0.0621  0.1156  220 ALA B N   
6470  C CA  . ALA B 228 ? 0.1787 0.3569 0.3042 -0.0351 0.0633  0.1154  220 ALA B CA  
6471  C C   . ALA B 228 ? 0.2132 0.3742 0.3356 -0.0347 0.0579  0.1125  220 ALA B C   
6472  O O   . ALA B 228 ? 0.2158 0.3630 0.3301 -0.0367 0.0561  0.1141  220 ALA B O   
6473  C CB  . ALA B 228 ? 0.2201 0.4062 0.3388 -0.0255 0.0694  0.1120  220 ALA B CB  
6474  N N   . ILE B 229 ? 0.1685 0.3306 0.2972 -0.0317 0.0552  0.1083  221 ILE B N   
6475  C CA  . ILE B 229 ? 0.1430 0.2898 0.2689 -0.0310 0.0504  0.1053  221 ILE B CA  
6476  C C   . ILE B 229 ? 0.1455 0.2809 0.2743 -0.0399 0.0445  0.1079  221 ILE B C   
6477  O O   . ILE B 229 ? 0.1571 0.2771 0.2793 -0.0407 0.0415  0.1076  221 ILE B O   
6478  C CB  . ILE B 229 ? 0.1315 0.2830 0.2633 -0.0257 0.0492  0.1004  221 ILE B CB  
6479  C CG1 . ILE B 229 ? 0.2108 0.3697 0.3375 -0.0159 0.0550  0.0973  221 ILE B CG1 
6480  C CG2 . ILE B 229 ? 0.1305 0.2673 0.2609 -0.0263 0.0438  0.0977  221 ILE B CG2 
6481  C CD1 . ILE B 229 ? 0.1846 0.3514 0.3184 -0.0099 0.0545  0.0935  221 ILE B CD1 
6482  N N   . GLN B 230 ? 0.1593 0.3020 0.2976 -0.0464 0.0427  0.1101  222 GLN B N   
6483  C CA  . GLN B 230 ? 0.1960 0.3269 0.3364 -0.0551 0.0372  0.1122  222 GLN B CA  
6484  C C   . GLN B 230 ? 0.1796 0.2995 0.3111 -0.0581 0.0381  0.1167  222 GLN B C   
6485  O O   . GLN B 230 ? 0.2126 0.3156 0.3399 -0.0607 0.0336  0.1168  222 GLN B O   
6486  C CB  . GLN B 230 ? 0.1775 0.3199 0.3292 -0.0618 0.0358  0.1139  222 GLN B CB  
6487  C CG  . GLN B 230 ? 0.2700 0.3998 0.4241 -0.0712 0.0298  0.1153  222 GLN B CG  
6488  C CD  . GLN B 230 ? 0.3791 0.5205 0.5449 -0.0779 0.0276  0.1157  222 GLN B CD  
6489  O OE1 . GLN B 230 ? 0.3991 0.5589 0.5719 -0.0751 0.0305  0.1151  222 GLN B OE1 
6490  N NE2 . GLN B 230 ? 0.4397 0.5698 0.6073 -0.0865 0.0224  0.1164  222 GLN B NE2 
6491  N N   . THR B 231 ? 0.2368 0.3660 0.3648 -0.0573 0.0437  0.1203  223 THR B N   
6492  C CA  . THR B 231 ? 0.2216 0.3413 0.3406 -0.0598 0.0446  0.1250  223 THR B CA  
6493  C C   . THR B 231 ? 0.1975 0.3036 0.3059 -0.0541 0.0435  0.1228  223 THR B C   
6494  O O   . THR B 231 ? 0.1990 0.2901 0.3015 -0.0567 0.0404  0.1252  223 THR B O   
6495  C CB  . THR B 231 ? 0.2311 0.3653 0.3481 -0.0592 0.0513  0.1288  223 THR B CB  
6496  O OG1 . THR B 231 ? 0.2179 0.3652 0.3454 -0.0650 0.0522  0.1310  223 THR B OG1 
6497  C CG2 . THR B 231 ? 0.2354 0.3602 0.3425 -0.0619 0.0522  0.1341  223 THR B CG2 
6498  N N   . ALA B 232 ? 0.1743 0.2850 0.2802 -0.0464 0.0457  0.1182  224 ALA B N   
6499  C CA  . ALA B 232 ? 0.1654 0.2647 0.2615 -0.0412 0.0447  0.1157  224 ALA B CA  
6500  C C   . ALA B 232 ? 0.2155 0.2993 0.3132 -0.0432 0.0381  0.1137  224 ALA B C   
6501  O O   . ALA B 232 ? 0.1839 0.2545 0.2742 -0.0427 0.0356  0.1146  224 ALA B O   
6502  C CB  . ALA B 232 ? 0.2031 0.3106 0.2967 -0.0331 0.0486  0.1108  224 ALA B CB  
6503  N N   . ILE B 233 ? 0.1874 0.2732 0.2944 -0.0450 0.0351  0.1106  225 ILE B N   
6504  C CA  . ILE B 233 ? 0.1694 0.2410 0.2780 -0.0470 0.0288  0.1081  225 ILE B CA  
6505  C C   . ILE B 233 ? 0.1902 0.2491 0.2976 -0.0534 0.0250  0.1119  225 ILE B C   
6506  O O   . ILE B 233 ? 0.1921 0.2353 0.2946 -0.0529 0.0210  0.1110  225 ILE B O   
6507  C CB  . ILE B 233 ? 0.2075 0.2853 0.3264 -0.0481 0.0262  0.1042  225 ILE B CB  
6508  C CG1 . ILE B 233 ? 0.1778 0.2651 0.2966 -0.0407 0.0296  0.1004  225 ILE B CG1 
6509  C CG2 . ILE B 233 ? 0.1958 0.2590 0.3162 -0.0508 0.0194  0.1012  225 ILE B CG2 
6510  C CD1 . ILE B 233 ? 0.1273 0.2214 0.2558 -0.0408 0.0270  0.0969  225 ILE B CD1 
6511  N N   . GLU B 234 ? 0.2001 0.2652 0.3115 -0.0594 0.0264  0.1162  226 GLU B N   
6512  C CA  . GLU B 234 ? 0.2451 0.2973 0.3544 -0.0657 0.0233  0.1202  226 GLU B CA  
6513  C C   . GLU B 234 ? 0.2665 0.3079 0.3642 -0.0625 0.0241  0.1233  226 GLU B C   
6514  O O   . GLU B 234 ? 0.2530 0.2774 0.3465 -0.0636 0.0197  0.1238  226 GLU B O   
6515  C CB  . GLU B 234 ? 0.2008 0.2633 0.3160 -0.0728 0.0256  0.1248  226 GLU B CB  
6516  C CG  . GLU B 234 ? 0.2043 0.2727 0.3308 -0.0780 0.0225  0.1221  226 GLU B CG  
6517  C CD  . GLU B 234 ? 0.3144 0.3995 0.4484 -0.0835 0.0259  0.1258  226 GLU B CD  
6518  O OE1 . GLU B 234 ? 0.3180 0.4109 0.4486 -0.0832 0.0312  0.1304  226 GLU B OE1 
6519  O OE2 . GLU B 234 ? 0.3604 0.4518 0.5039 -0.0880 0.0233  0.1239  226 GLU B OE2 
6520  N N   . ALA B 235 ? 0.2484 0.2997 0.3405 -0.0579 0.0294  0.1249  227 ALA B N   
6521  C CA  . ALA B 235 ? 0.2143 0.2571 0.2951 -0.0544 0.0299  0.1276  227 ALA B CA  
6522  C C   . ALA B 235 ? 0.2518 0.2825 0.3281 -0.0490 0.0260  0.1234  227 ALA B C   
6523  O O   . ALA B 235 ? 0.2523 0.2696 0.3218 -0.0479 0.0231  0.1254  227 ALA B O   
6524  C CB  . ALA B 235 ? 0.2149 0.2715 0.2901 -0.0503 0.0363  0.1290  227 ALA B CB  
6525  N N   . ALA B 236 ? 0.2426 0.2783 0.3227 -0.0454 0.0260  0.1178  228 ALA B N   
6526  C CA  . ALA B 236 ? 0.2043 0.2302 0.2808 -0.0406 0.0227  0.1136  228 ALA B CA  
6527  C C   . ALA B 236 ? 0.2176 0.2274 0.2967 -0.0435 0.0163  0.1126  228 ALA B C   
6528  O O   . ALA B 236 ? 0.2642 0.2617 0.3376 -0.0401 0.0130  0.1119  228 ALA B O   
6529  C CB  . ALA B 236 ? 0.1938 0.2287 0.2742 -0.0370 0.0244  0.1082  228 ALA B CB  
6530  N N   . ARG B 237 ? 0.2088 0.2186 0.2962 -0.0496 0.0142  0.1122  229 ARG B N   
6531  C CA  . ARG B 237 ? 0.2338 0.2275 0.3230 -0.0526 0.0079  0.1104  229 ARG B CA  
6532  C C   . ARG B 237 ? 0.2935 0.2736 0.3764 -0.0546 0.0061  0.1153  229 ARG B C   
6533  O O   . ARG B 237 ? 0.3672 0.3308 0.4467 -0.0529 0.0013  0.1135  229 ARG B O   
6534  C CB  . ARG B 237 ? 0.2911 0.2892 0.3903 -0.0592 0.0060  0.1085  229 ARG B CB  
6535  C CG  . ARG B 237 ? 0.2901 0.2996 0.3956 -0.0570 0.0065  0.1034  229 ARG B CG  
6536  C CD  . ARG B 237 ? 0.3591 0.3764 0.4746 -0.0635 0.0049  0.1024  229 ARG B CD  
6537  N NE  . ARG B 237 ? 0.4031 0.4057 0.5197 -0.0693 -0.0009 0.1015  229 ARG B NE  
6538  C CZ  . ARG B 237 ? 0.4167 0.4073 0.5333 -0.0687 -0.0064 0.0960  229 ARG B CZ  
6539  N NH1 . ARG B 237 ? 0.3959 0.3882 0.5119 -0.0629 -0.0067 0.0915  229 ARG B NH1 
6540  N NH2 . ARG B 237 ? 0.4524 0.4289 0.5689 -0.0738 -0.0115 0.0947  229 ARG B NH2 
6541  N N   . ALA B 238 ? 0.2966 0.2830 0.3773 -0.0575 0.0100  0.1213  230 ALA B N   
6542  C CA  . ALA B 238 ? 0.3027 0.2762 0.3766 -0.0593 0.0087  0.1267  230 ALA B CA  
6543  C C   . ALA B 238 ? 0.3730 0.3388 0.4371 -0.0517 0.0079  0.1273  230 ALA B C   
6544  O O   . ALA B 238 ? 0.3660 0.3170 0.4242 -0.0514 0.0050  0.1305  230 ALA B O   
6545  C CB  . ALA B 238 ? 0.2676 0.2512 0.3414 -0.0643 0.0135  0.1332  230 ALA B CB  
6546  N N   . GLU B 239 ? 0.3406 0.3160 0.4026 -0.0455 0.0102  0.1245  231 GLU B N   
6547  C CA  . GLU B 239 ? 0.3475 0.3178 0.4007 -0.0382 0.0092  0.1247  231 GLU B CA  
6548  C C   . GLU B 239 ? 0.3969 0.3560 0.4515 -0.0341 0.0040  0.1190  231 GLU B C   
6549  O O   . GLU B 239 ? 0.4407 0.4060 0.4992 -0.0319 0.0043  0.1139  231 GLU B O   
6550  C CB  . GLU B 239 ? 0.3634 0.3494 0.4129 -0.0341 0.0142  0.1242  231 GLU B CB  
6551  C CG  . GLU B 239 ? 0.4387 0.4220 0.4799 -0.0267 0.0129  0.1235  231 GLU B CG  
6552  C CD  . GLU B 239 ? 0.4782 0.4500 0.5119 -0.0252 0.0101  0.1286  231 GLU B CD  
6553  O OE1 . GLU B 239 ? 0.4325 0.4077 0.4616 -0.0276 0.0128  0.1342  231 GLU B OE1 
6554  O OE2 . GLU B 239 ? 0.4771 0.4364 0.5095 -0.0213 0.0050  0.1269  231 GLU B OE2 
6555  N N   . THR B 240 ? 0.4140 0.3561 0.4652 -0.0329 -0.0008 0.1199  232 THR B N   
6556  C CA  . THR B 240 ? 0.3512 0.2817 0.4043 -0.0292 -0.0060 0.1139  232 THR B CA  
6557  C C   . THR B 240 ? 0.3758 0.3042 0.4230 -0.0199 -0.0078 0.1123  232 THR B C   
6558  O O   . THR B 240 ? 0.3686 0.2910 0.4166 -0.0153 -0.0115 0.1051  232 THR B O   
6559  C CB  . THR B 240 ? 0.3789 0.2909 0.4319 -0.0325 -0.0105 0.1143  232 THR B CB  
6560  O OG1 . THR B 240 ? 0.3868 0.2901 0.4317 -0.0308 -0.0109 0.1204  232 THR B OG1 
6561  C CG2 . THR B 240 ? 0.4121 0.3274 0.4721 -0.0421 -0.0094 0.1151  232 THR B CG2 
6562  N N   . GLY B 241 ? 0.3362 0.2716 0.3766 -0.0166 -0.0052 0.1167  233 GLY B N   
6563  C CA  . GLY B 241 ? 0.3678 0.3031 0.4023 -0.0078 -0.0074 0.1144  233 GLY B CA  
6564  C C   . GLY B 241 ? 0.3335 0.2854 0.3658 -0.0041 -0.0043 0.1085  233 GLY B C   
6565  O O   . GLY B 241 ? 0.3162 0.2702 0.3446 0.0027  -0.0063 0.1043  233 GLY B O   
6566  N N   . LYS B 242 ? 0.2496 0.2137 0.2845 -0.0084 0.0005  0.1081  234 LYS B N   
6567  C CA  . LYS B 242 ? 0.2161 0.1941 0.2480 -0.0055 0.0036  0.1029  234 LYS B CA  
6568  C C   . LYS B 242 ? 0.1917 0.1764 0.2301 -0.0086 0.0060  0.0972  234 LYS B C   
6569  O O   . LYS B 242 ? 0.2194 0.2041 0.2638 -0.0143 0.0074  0.1003  234 LYS B O   
6570  C CB  . LYS B 242 ? 0.2455 0.2327 0.2710 -0.0061 0.0079  0.1090  234 LYS B CB  
6571  C CG  . LYS B 242 ? 0.3355 0.3176 0.3536 -0.0036 0.0061  0.1165  234 LYS B CG  
6572  C CD  . LYS B 242 ? 0.3620 0.3543 0.3743 -0.0058 0.0112  0.1229  234 LYS B CD  
6573  C CE  . LYS B 242 ? 0.4460 0.4357 0.4491 -0.0028 0.0095  0.1293  234 LYS B CE  
6574  N NZ  . LYS B 242 ? 0.5062 0.5067 0.5031 -0.0051 0.0145  0.1324  234 LYS B NZ  
6575  N N   . PRO B 243 ? 0.1904 0.1815 0.2280 -0.0054 0.0063  0.0893  235 PRO B N   
6576  C CA  . PRO B 243 ? 0.1709 0.1692 0.2132 -0.0078 0.0090  0.0851  235 PRO B CA  
6577  C C   . PRO B 243 ? 0.1962 0.2042 0.2377 -0.0102 0.0145  0.0894  235 PRO B C   
6578  O O   . PRO B 243 ? 0.2175 0.2290 0.2524 -0.0090 0.0165  0.0935  235 PRO B O   
6579  C CB  . PRO B 243 ? 0.1483 0.1505 0.1874 -0.0036 0.0084  0.0771  235 PRO B CB  
6580  C CG  . PRO B 243 ? 0.1489 0.1514 0.1804 0.0006  0.0072  0.0784  235 PRO B CG  
6581  C CD  . PRO B 243 ? 0.1813 0.1743 0.2132 0.0004  0.0044  0.0847  235 PRO B CD  
6582  N N   . SER B 244 ? 0.1631 0.1765 0.2111 -0.0133 0.0168  0.0884  236 SER B N   
6583  C CA  . SER B 244 ? 0.2378 0.2616 0.2867 -0.0154 0.0222  0.0926  236 SER B CA  
6584  C C   . SER B 244 ? 0.1749 0.2071 0.2238 -0.0128 0.0252  0.0866  236 SER B C   
6585  O O   . SER B 244 ? 0.1443 0.1749 0.1974 -0.0123 0.0232  0.0812  236 SER B O   
6586  C CB  . SER B 244 ? 0.2198 0.2443 0.2776 -0.0216 0.0227  0.0982  236 SER B CB  
6587  O OG  . SER B 244 ? 0.2285 0.2442 0.2856 -0.0247 0.0204  0.1049  236 SER B OG  
6588  N N   . ILE B 245 ? 0.1811 0.2216 0.2248 -0.0110 0.0301  0.0877  237 ILE B N   
6589  C CA  . ILE B 245 ? 0.1767 0.2247 0.2205 -0.0085 0.0336  0.0830  237 ILE B CA  
6590  C C   . ILE B 245 ? 0.1560 0.2149 0.2030 -0.0100 0.0391  0.0880  237 ILE B C   
6591  O O   . ILE B 245 ? 0.1957 0.2581 0.2381 -0.0108 0.0418  0.0935  237 ILE B O   
6592  C CB  . ILE B 245 ? 0.1483 0.1958 0.1819 -0.0040 0.0344  0.0774  237 ILE B CB  
6593  C CG1 . ILE B 245 ? 0.1307 0.1840 0.1641 -0.0012 0.0382  0.0730  237 ILE B CG1 
6594  C CG2 . ILE B 245 ? 0.1418 0.1914 0.1662 -0.0033 0.0362  0.0812  237 ILE B CG2 
6595  C CD1 . ILE B 245 ? 0.2112 0.2600 0.2367 0.0020  0.0372  0.0657  237 ILE B CD1 
6596  N N   . ILE B 246 ? 0.1338 0.1990 0.1888 -0.0101 0.0406  0.0866  238 ILE B N   
6597  C CA  . ILE B 246 ? 0.1362 0.2144 0.1965 -0.0111 0.0459  0.0908  238 ILE B CA  
6598  C C   . ILE B 246 ? 0.1438 0.2278 0.2004 -0.0050 0.0497  0.0851  238 ILE B C   
6599  O O   . ILE B 246 ? 0.1665 0.2480 0.2258 -0.0025 0.0478  0.0797  238 ILE B O   
6600  C CB  . ILE B 246 ? 0.1706 0.2527 0.2441 -0.0161 0.0442  0.0938  238 ILE B CB  
6601  C CG1 . ILE B 246 ? 0.1388 0.2116 0.2147 -0.0222 0.0398  0.0986  238 ILE B CG1 
6602  C CG2 . ILE B 246 ? 0.1629 0.2615 0.2432 -0.0170 0.0500  0.0981  238 ILE B CG2 
6603  C CD1 . ILE B 246 ? 0.2470 0.3204 0.3349 -0.0279 0.0365  0.1001  238 ILE B CD1 
6604  N N   . CYS B 247 ? 0.1396 0.2303 0.1890 -0.0023 0.0550  0.0861  239 CYS B N   
6605  C CA  . CYS B 247 ? 0.1726 0.2668 0.2166 0.0041  0.0587  0.0802  239 CYS B CA  
6606  C C   . CYS B 247 ? 0.1852 0.2931 0.2385 0.0057  0.0632  0.0819  239 CYS B C   
6607  O O   . CYS B 247 ? 0.1659 0.2857 0.2208 0.0047  0.0681  0.0871  239 CYS B O   
6608  C CB  . CYS B 247 ? 0.2200 0.3149 0.2509 0.0066  0.0620  0.0796  239 CYS B CB  
6609  S SG  . CYS B 247 ? 0.1969 0.2786 0.2180 0.0048  0.0564  0.0783  239 CYS B SG  
6610  N N   . CYS B 248 ? 0.1344 0.2418 0.1938 0.0084  0.0615  0.0778  240 CYS B N   
6611  C CA  . CYS B 248 ? 0.1921 0.3135 0.2623 0.0103  0.0647  0.0794  240 CYS B CA  
6612  C C   . CYS B 248 ? 0.1771 0.3017 0.2415 0.0191  0.0692  0.0738  240 CYS B C   
6613  O O   . CYS B 248 ? 0.1917 0.3063 0.2520 0.0233  0.0668  0.0677  240 CYS B O   
6614  C CB  . CYS B 248 ? 0.1910 0.3108 0.2722 0.0079  0.0595  0.0789  240 CYS B CB  
6615  S SG  . CYS B 248 ? 0.1728 0.2872 0.2608 -0.0022 0.0537  0.0843  240 CYS B SG  
6616  N N   . LYS B 249 ? 0.1438 0.2815 0.2073 0.0218  0.0759  0.0760  241 LYS B N   
6617  C CA  . LYS B 249 ? 0.1497 0.2911 0.2081 0.0310  0.0806  0.0706  241 LYS B CA  
6618  C C   . LYS B 249 ? 0.1459 0.2953 0.2163 0.0351  0.0804  0.0697  241 LYS B C   
6619  O O   . LYS B 249 ? 0.1650 0.3288 0.2470 0.0325  0.0813  0.0743  241 LYS B O   
6620  C CB  . LYS B 249 ? 0.1688 0.3215 0.2223 0.0325  0.0867  0.0722  241 LYS B CB  
6621  C CG  . LYS B 249 ? 0.1911 0.3381 0.2336 0.0277  0.0864  0.0745  241 LYS B CG  
6622  C CD  . LYS B 249 ? 0.2822 0.4148 0.3111 0.0309  0.0853  0.0686  241 LYS B CD  
6623  C CE  . LYS B 249 ? 0.3386 0.4695 0.3550 0.0285  0.0865  0.0703  241 LYS B CE  
6624  N NZ  . LYS B 249 ? 0.3080 0.4241 0.3104 0.0311  0.0838  0.0626  241 LYS B NZ  
6625  N N   . THR B 250 ? 0.2018 0.3400 0.2682 0.0409  0.0779  0.0634  242 THR B N   
6626  C CA  . THR B 250 ? 0.1529 0.2974 0.2291 0.0463  0.0773  0.0623  242 THR B CA  
6627  C C   . THR B 250 ? 0.2344 0.3734 0.3018 0.0571  0.0805  0.0556  242 THR B C   
6628  O O   . THR B 250 ? 0.1607 0.2873 0.2138 0.0592  0.0817  0.0508  242 THR B O   
6629  C CB  . THR B 250 ? 0.1361 0.2706 0.2172 0.0426  0.0698  0.0619  242 THR B CB  
6630  O OG1 . THR B 250 ? 0.1847 0.2991 0.2531 0.0435  0.0666  0.0564  242 THR B OG1 
6631  C CG2 . THR B 250 ? 0.1477 0.2851 0.2368 0.0323  0.0661  0.0675  242 THR B CG2 
6632  N N   . LEU B 251 ? 0.1992 0.3466 0.2752 0.0639  0.0812  0.0551  243 LEU B N   
6633  C CA  . LEU B 251 ? 0.2263 0.3649 0.2952 0.0747  0.0824  0.0487  243 LEU B CA  
6634  C C   . LEU B 251 ? 0.2742 0.3998 0.3447 0.0748  0.0756  0.0473  243 LEU B C   
6635  O O   . LEU B 251 ? 0.1805 0.3154 0.2640 0.0720  0.0722  0.0514  243 LEU B O   
6636  C CB  . LEU B 251 ? 0.2709 0.4280 0.3476 0.0838  0.0879  0.0491  243 LEU B CB  
6637  C CG  . LEU B 251 ? 0.2674 0.4357 0.3406 0.0829  0.0930  0.0494  243 LEU B CG  
6638  C CD1 . LEU B 251 ? 0.3104 0.4937 0.3910 0.0894  0.0952  0.0488  243 LEU B CD1 
6639  C CD2 . LEU B 251 ? 0.3057 0.4603 0.3612 0.0869  0.0965  0.0436  243 LEU B CD2 
6640  N N   . ILE B 252 ? 0.1666 0.2712 0.2240 0.0775  0.0735  0.0417  244 ILE B N   
6641  C CA  . ILE B 252 ? 0.1654 0.2582 0.2235 0.0787  0.0678  0.0407  244 ILE B CA  
6642  C C   . ILE B 252 ? 0.1881 0.2914 0.2550 0.0886  0.0691  0.0413  244 ILE B C   
6643  O O   . ILE B 252 ? 0.1833 0.2948 0.2498 0.0972  0.0748  0.0395  244 ILE B O   
6644  C CB  . ILE B 252 ? 0.1740 0.2425 0.2160 0.0794  0.0658  0.0348  244 ILE B CB  
6645  C CG1 . ILE B 252 ? 0.2188 0.2758 0.2617 0.0769  0.0592  0.0354  244 ILE B CG1 
6646  C CG2 . ILE B 252 ? 0.2241 0.2853 0.2568 0.0903  0.0700  0.0294  244 ILE B CG2 
6647  C CD1 . ILE B 252 ? 0.2590 0.2934 0.2872 0.0741  0.0566  0.0309  244 ILE B CD1 
6648  N N   . GLY B 253 ? 0.1788 0.2837 0.2544 0.0876  0.0638  0.0440  245 GLY B N   
6649  C CA  . GLY B 253 ? 0.1670 0.2837 0.2522 0.0969  0.0641  0.0454  245 GLY B CA  
6650  C C   . GLY B 253 ? 0.1631 0.3071 0.2625 0.0984  0.0686  0.0493  245 GLY B C   
6651  O O   . GLY B 253 ? 0.1710 0.3239 0.2744 0.1069  0.0701  0.0484  245 GLY B O   
6652  N N   . LYS B 254 ? 0.1830 0.3379 0.2881 0.0883  0.0695  0.0530  246 LYS B N   
6653  C CA  . LYS B 254 ? 0.1834 0.3609 0.2995 0.0859  0.0723  0.0566  246 LYS B CA  
6654  C C   . LYS B 254 ? 0.2165 0.4067 0.3454 0.0875  0.0681  0.0587  246 LYS B C   
6655  O O   . LYS B 254 ? 0.1440 0.3323 0.2787 0.0837  0.0622  0.0608  246 LYS B O   
6656  C CB  . LYS B 254 ? 0.1437 0.3271 0.2637 0.0734  0.0722  0.0612  246 LYS B CB  
6657  C CG  . LYS B 254 ? 0.1475 0.3511 0.2778 0.0681  0.0736  0.0651  246 LYS B CG  
6658  C CD  . LYS B 254 ? 0.2002 0.4099 0.3241 0.0714  0.0803  0.0637  246 LYS B CD  
6659  C CE  . LYS B 254 ? 0.2965 0.5272 0.4316 0.0666  0.0817  0.0678  246 LYS B CE  
6660  N NZ  . LYS B 254 ? 0.3900 0.6267 0.5190 0.0660  0.0878  0.0681  246 LYS B NZ  
6661  N N   . GLY B 255 ? 0.1601 0.3641 0.2931 0.0929  0.0710  0.0580  247 GLY B N   
6662  C CA  . GLY B 255 ? 0.1614 0.3789 0.3060 0.0956  0.0676  0.0596  247 GLY B CA  
6663  C C   . GLY B 255 ? 0.2423 0.4521 0.3823 0.1086  0.0670  0.0556  247 GLY B C   
6664  O O   . GLY B 255 ? 0.1881 0.4111 0.3365 0.1134  0.0659  0.0561  247 GLY B O   
6665  N N   . SER B 256 ? 0.1777 0.3657 0.3042 0.1144  0.0675  0.0516  248 SER B N   
6666  C CA  . SER B 256 ? 0.1914 0.3683 0.3114 0.1266  0.0668  0.0477  248 SER B CA  
6667  C C   . SER B 256 ? 0.2042 0.3925 0.3251 0.1347  0.0719  0.0450  248 SER B C   
6668  O O   . SER B 256 ? 0.2149 0.4086 0.3325 0.1331  0.0776  0.0438  248 SER B O   
6669  C CB  . SER B 256 ? 0.1973 0.3474 0.3010 0.1301  0.0672  0.0435  248 SER B CB  
6670  O OG  . SER B 256 ? 0.2590 0.3967 0.3546 0.1419  0.0675  0.0391  248 SER B OG  
6671  N N   . ALA B 257 ? 0.2136 0.4056 0.3386 0.1435  0.0698  0.0443  249 ALA B N   
6672  C CA  . ALA B 257 ? 0.2866 0.4908 0.4138 0.1520  0.0745  0.0419  249 ALA B CA  
6673  C C   . ALA B 257 ? 0.2994 0.4866 0.4109 0.1595  0.0795  0.0355  249 ALA B C   
6674  O O   . ALA B 257 ? 0.2611 0.4585 0.3717 0.1621  0.0854  0.0334  249 ALA B O   
6675  C CB  . ALA B 257 ? 0.2348 0.4451 0.3695 0.1604  0.0707  0.0425  249 ALA B CB  
6676  N N   . ASN B 258 ? 0.3234 0.4842 0.4218 0.1628  0.0772  0.0323  250 ASN B N   
6677  C CA  . ASN B 258 ? 0.3019 0.4440 0.3847 0.1705  0.0810  0.0255  250 ASN B CA  
6678  C C   . ASN B 258 ? 0.3673 0.4864 0.4356 0.1657  0.0809  0.0229  250 ASN B C   
6679  O O   . ASN B 258 ? 0.3490 0.4533 0.4036 0.1703  0.0844  0.0168  250 ASN B O   
6680  C CB  . ASN B 258 ? 0.3618 0.4911 0.4405 0.1825  0.0784  0.0225  250 ASN B CB  
6681  C CG  . ASN B 258 ? 0.2963 0.4482 0.3884 0.1889  0.0788  0.0244  250 ASN B CG  
6682  O OD1 . ASN B 258 ? 0.3232 0.4898 0.4179 0.1923  0.0843  0.0224  250 ASN B OD1 
6683  N ND2 . ASN B 258 ? 0.2967 0.4524 0.3974 0.1903  0.0731  0.0282  250 ASN B ND2 
6684  N N   . LYS B 259 ? 0.2463 0.3618 0.3170 0.1566  0.0772  0.0269  251 LYS B N   
6685  C CA  . LYS B 259 ? 0.2921 0.3858 0.3497 0.1522  0.0769  0.0246  251 LYS B CA  
6686  C C   . LYS B 259 ? 0.3210 0.4248 0.3819 0.1411  0.0790  0.0277  251 LYS B C   
6687  O O   . LYS B 259 ? 0.2701 0.3596 0.3239 0.1356  0.0777  0.0275  251 LYS B O   
6688  C CB  . LYS B 259 ? 0.2945 0.3698 0.3490 0.1519  0.0705  0.0261  251 LYS B CB  
6689  C CG  . LYS B 259 ? 0.3773 0.4382 0.4260 0.1623  0.0680  0.0233  251 LYS B CG  
6690  C CD  . LYS B 259 ? 0.3925 0.4349 0.4372 0.1607  0.0615  0.0256  251 LYS B CD  
6691  C CE  . LYS B 259 ? 0.4691 0.5011 0.5110 0.1702  0.0583  0.0247  251 LYS B CE  
6692  N NZ  . LYS B 259 ? 0.5030 0.5184 0.5410 0.1677  0.0517  0.0279  251 LYS B NZ  
6693  N N   . GLU B 260 ? 0.3052 0.4327 0.3764 0.1374  0.0820  0.0308  252 GLU B N   
6694  C CA  . GLU B 260 ? 0.2977 0.4341 0.3716 0.1264  0.0838  0.0342  252 GLU B CA  
6695  C C   . GLU B 260 ? 0.2947 0.4168 0.3525 0.1261  0.0879  0.0293  252 GLU B C   
6696  O O   . GLU B 260 ? 0.2821 0.4004 0.3307 0.1330  0.0918  0.0239  252 GLU B O   
6697  C CB  . GLU B 260 ? 0.2883 0.4509 0.3744 0.1229  0.0865  0.0381  252 GLU B CB  
6698  C CG  . GLU B 260 ? 0.3116 0.4849 0.4039 0.1102  0.0865  0.0436  252 GLU B CG  
6699  C CD  . GLU B 260 ? 0.3530 0.5510 0.4582 0.1065  0.0882  0.0479  252 GLU B CD  
6700  O OE1 . GLU B 260 ? 0.2259 0.4349 0.3443 0.1021  0.0841  0.0523  252 GLU B OE1 
6701  O OE2 . GLU B 260 ? 0.3922 0.5981 0.4937 0.1079  0.0936  0.0467  252 GLU B OE2 
6702  N N   . GLY B 261 ? 0.2849 0.3989 0.3391 0.1180  0.0866  0.0309  253 GLY B N   
6703  C CA  . GLY B 261 ? 0.2453 0.3437 0.2830 0.1144  0.0881  0.0262  253 GLY B CA  
6704  C C   . GLY B 261 ? 0.2972 0.3681 0.3192 0.1184  0.0856  0.0193  253 GLY B C   
6705  O O   . GLY B 261 ? 0.3836 0.4414 0.3916 0.1153  0.0865  0.0148  253 GLY B O   
6706  N N   . SER B 262 ? 0.3205 0.3820 0.3441 0.1248  0.0823  0.0187  254 SER B N   
6707  C CA  . SER B 262 ? 0.3777 0.4117 0.3860 0.1286  0.0801  0.0126  254 SER B CA  
6708  C C   . SER B 262 ? 0.4092 0.4271 0.4134 0.1177  0.0733  0.0140  254 SER B C   
6709  O O   . SER B 262 ? 0.4015 0.4254 0.4162 0.1134  0.0689  0.0193  254 SER B O   
6710  C CB  . SER B 262 ? 0.3748 0.4049 0.3853 0.1419  0.0800  0.0115  254 SER B CB  
6711  O OG  . SER B 262 ? 0.3582 0.3595 0.3548 0.1437  0.0765  0.0072  254 SER B OG  
6712  N N   . HIS B 263 ? 0.3535 0.3886 0.3273 0.1040  0.0455  0.0001  255 HIS B N   
6713  C CA  . HIS B 263 ? 0.4115 0.4388 0.3900 0.0924  0.0390  -0.0058 255 HIS B CA  
6714  C C   . HIS B 263 ? 0.3856 0.4084 0.3708 0.0831  0.0342  -0.0095 255 HIS B C   
6715  O O   . HIS B 263 ? 0.3451 0.3638 0.3376 0.0720  0.0311  -0.0120 255 HIS B O   
6716  C CB  . HIS B 263 ? 0.4816 0.4988 0.4469 0.0982  0.0318  -0.0138 255 HIS B CB  
6717  C CG  . HIS B 263 ? 0.6502 0.6596 0.6029 0.1073  0.0252  -0.0205 255 HIS B CG  
6718  N ND1 . HIS B 263 ? 0.6938 0.7051 0.6334 0.1226  0.0274  -0.0191 255 HIS B ND1 
6719  C CD2 . HIS B 263 ? 0.6985 0.6974 0.6494 0.1036  0.0163  -0.0286 255 HIS B CD2 
6720  C CE1 . HIS B 263 ? 0.7178 0.7197 0.6476 0.1281  0.0194  -0.0266 255 HIS B CE1 
6721  N NE2 . HIS B 263 ? 0.7239 0.7179 0.6608 0.1164  0.0126  -0.0324 255 HIS B NE2 
6722  N N   . LYS B 264 ? 0.3157 0.3393 0.2981 0.0882  0.0338  -0.0095 256 LYS B N   
6723  C CA  . LYS B 264 ? 0.3610 0.3803 0.3489 0.0803  0.0299  -0.0121 256 LYS B CA  
6724  C C   . LYS B 264 ? 0.3259 0.3518 0.3298 0.0690  0.0337  -0.0070 256 LYS B C   
6725  O O   . LYS B 264 ? 0.3493 0.3698 0.3577 0.0604  0.0300  -0.0097 256 LYS B O   
6726  C CB  . LYS B 264 ? 0.4081 0.4285 0.3900 0.0892  0.0297  -0.0122 256 LYS B CB  
6727  N N   . THR B 265 ? 0.2608 0.2978 0.2730 0.0694  0.0410  0.0005  257 THR B N   
6728  C CA  . THR B 265 ? 0.2920 0.3351 0.3200 0.0593  0.0437  0.0050  257 THR B CA  
6729  C C   . THR B 265 ? 0.2519 0.2899 0.2838 0.0495  0.0415  0.0031  257 THR B C   
6730  O O   . THR B 265 ? 0.2306 0.2716 0.2743 0.0411  0.0424  0.0058  257 THR B O   
6731  C CB  . THR B 265 ? 0.2345 0.2910 0.2722 0.0626  0.0521  0.0141  257 THR B CB  
6732  O OG1 . THR B 265 ? 0.2651 0.3226 0.2982 0.0663  0.0560  0.0168  257 THR B OG1 
6733  C CG2 . THR B 265 ? 0.1911 0.2544 0.2259 0.0731  0.0553  0.0167  257 THR B CG2 
6734  N N   . HIS B 266 ? 0.2575 0.2880 0.2801 0.0508  0.0381  -0.0018 258 HIS B N   
6735  C CA  . HIS B 266 ? 0.3485 0.3756 0.3751 0.0426  0.0366  -0.0034 258 HIS B CA  
6736  C C   . HIS B 266 ? 0.3592 0.3800 0.3904 0.0329  0.0324  -0.0069 258 HIS B C   
6737  O O   . HIS B 266 ? 0.3042 0.3266 0.3440 0.0251  0.0333  -0.0048 258 HIS B O   
6738  C CB  . HIS B 266 ? 0.4745 0.4958 0.4910 0.0469  0.0335  -0.0083 258 HIS B CB  
6739  C CG  . HIS B 266 ? 0.5966 0.6134 0.6170 0.0383  0.0306  -0.0115 258 HIS B CG  
6740  N ND1 . HIS B 266 ? 0.6259 0.6468 0.6522 0.0344  0.0339  -0.0078 258 HIS B ND1 
6741  C CD2 . HIS B 266 ? 0.6327 0.6417 0.6526 0.0328  0.0251  -0.0177 258 HIS B CD2 
6742  C CE1 . HIS B 266 ? 0.6390 0.6552 0.6675 0.0276  0.0305  -0.0119 258 HIS B CE1 
6743  N NE2 . HIS B 266 ? 0.6330 0.6423 0.6584 0.0263  0.0255  -0.0176 258 HIS B NE2 
6744  N N   . GLY B 267 ? 0.3603 0.3733 0.3851 0.0337  0.0276  -0.0121 259 GLY B N   
6745  C CA  . GLY B 267 ? 0.3513 0.3566 0.3785 0.0252  0.0240  -0.0154 259 GLY B CA  
6746  C C   . GLY B 267 ? 0.3571 0.3578 0.3826 0.0247  0.0217  -0.0166 259 GLY B C   
6747  O O   . GLY B 267 ? 0.3043 0.2966 0.3291 0.0191  0.0188  -0.0195 259 GLY B O   
6748  N N   . ALA B 268 ? 0.3232 0.3293 0.3481 0.0310  0.0234  -0.0141 260 ALA B N   
6749  C CA  . ALA B 268 ? 0.3084 0.3108 0.3318 0.0314  0.0212  -0.0150 260 ALA B CA  
6750  C C   . ALA B 268 ? 0.2432 0.2563 0.2758 0.0323  0.0246  -0.0098 260 ALA B C   
6751  O O   . ALA B 268 ? 0.2536 0.2770 0.2915 0.0355  0.0291  -0.0053 260 ALA B O   
6752  C CB  . ALA B 268 ? 0.3245 0.3214 0.3367 0.0399  0.0181  -0.0187 260 ALA B CB  
6753  N N   . PRO B 269 ? 0.2123 0.2232 0.2475 0.0296  0.0225  -0.0102 261 PRO B N   
6754  C CA  . PRO B 269 ? 0.2127 0.2342 0.2581 0.0311  0.0245  -0.0060 261 PRO B CA  
6755  C C   . PRO B 269 ? 0.2061 0.2364 0.2505 0.0407  0.0277  -0.0035 261 PRO B C   
6756  O O   . PRO B 269 ? 0.1822 0.2076 0.2150 0.0474  0.0264  -0.0064 261 PRO B O   
6757  C CB  . PRO B 269 ? 0.2583 0.2724 0.3013 0.0293  0.0201  -0.0088 261 PRO B CB  
6758  C CG  . PRO B 269 ? 0.2931 0.2945 0.3294 0.0231  0.0175  -0.0124 261 PRO B CG  
6759  C CD  . PRO B 269 ? 0.2446 0.2432 0.2744 0.0250  0.0182  -0.0141 261 PRO B CD  
6760  N N   . LEU B 270 ? 0.2084 0.2520 0.2658 0.0416  0.0320  0.0022  262 LEU B N   
6761  C CA  . LEU B 270 ? 0.2096 0.2634 0.2678 0.0511  0.0364  0.0058  262 LEU B CA  
6762  C C   . LEU B 270 ? 0.2352 0.2867 0.2873 0.0572  0.0330  0.0027  262 LEU B C   
6763  O O   . LEU B 270 ? 0.2958 0.3504 0.3407 0.0670  0.0349  0.0031  262 LEU B O   
6764  C CB  . LEU B 270 ? 0.1679 0.2369 0.2447 0.0494  0.0419  0.0131  262 LEU B CB  
6765  C CG  . LEU B 270 ? 0.2550 0.3281 0.3386 0.0453  0.0466  0.0178  262 LEU B CG  
6766  C CD1 . LEU B 270 ? 0.2122 0.3008 0.3149 0.0453  0.0526  0.0259  262 LEU B CD1 
6767  C CD2 . LEU B 270 ? 0.3196 0.3895 0.3893 0.0520  0.0494  0.0175  262 LEU B CD2 
6768  N N   . GLY B 271 ? 0.2141 0.2597 0.2677 0.0524  0.0280  -0.0004 263 GLY B N   
6769  C CA  . GLY B 271 ? 0.2398 0.2836 0.2889 0.0580  0.0247  -0.0029 263 GLY B CA  
6770  C C   . GLY B 271 ? 0.2328 0.2905 0.2984 0.0587  0.0262  0.0009  263 GLY B C   
6771  O O   . GLY B 271 ? 0.1761 0.2476 0.2562 0.0581  0.0316  0.0068  263 GLY B O   
6772  N N   . ALA B 272 ? 0.2043 0.2583 0.2686 0.0599  0.0211  -0.0023 264 ALA B N   
6773  C CA  . ALA B 272 ? 0.2102 0.2766 0.2917 0.0597  0.0208  0.0001  264 ALA B CA  
6774  C C   . ALA B 272 ? 0.1821 0.2655 0.2729 0.0679  0.0266  0.0051  264 ALA B C   
6775  O O   . ALA B 272 ? 0.1912 0.2894 0.3021 0.0657  0.0301  0.0104  264 ALA B O   
6776  C CB  . ALA B 272 ? 0.2901 0.3478 0.3660 0.0607  0.0135  -0.0050 264 ALA B CB  
6777  N N   . ASP B 273 ? 0.1912 0.2726 0.2681 0.0776  0.0278  0.0038  265 ASP B N   
6778  C CA  . ASP B 273 ? 0.2342 0.3320 0.3183 0.0869  0.0341  0.0089  265 ASP B CA  
6779  C C   . ASP B 273 ? 0.1890 0.2981 0.2837 0.0854  0.0426  0.0163  265 ASP B C   
6780  O O   . ASP B 273 ? 0.1862 0.3126 0.2988 0.0873  0.0486  0.0229  265 ASP B O   
6781  C CB  . ASP B 273 ? 0.2066 0.2979 0.2706 0.0986  0.0334  0.0056  265 ASP B CB  
6782  C CG  . ASP B 273 ? 0.3100 0.3940 0.3660 0.1027  0.0264  -0.0000 265 ASP B CG  
6783  O OD1 . ASP B 273 ? 0.3149 0.4008 0.3818 0.0978  0.0226  -0.0011 265 ASP B OD1 
6784  O OD2 . ASP B 273 ? 0.3055 0.3810 0.3436 0.1115  0.0243  -0.0037 265 ASP B OD2 
6785  N N   . GLU B 274 ? 0.1887 0.2881 0.2728 0.0822  0.0433  0.0154  266 GLU B N   
6786  C CA  . GLU B 274 ? 0.2227 0.3307 0.3139 0.0816  0.0513  0.0222  266 GLU B CA  
6787  C C   . GLU B 274 ? 0.1836 0.3004 0.2975 0.0714  0.0530  0.0270  266 GLU B C   
6788  O O   . GLU B 274 ? 0.1731 0.3035 0.3012 0.0722  0.0608  0.0349  266 GLU B O   
6789  C CB  . GLU B 274 ? 0.2335 0.3283 0.3079 0.0806  0.0502  0.0191  266 GLU B CB  
6790  C CG  . GLU B 274 ? 0.2317 0.3335 0.3108 0.0805  0.0579  0.0257  266 GLU B CG  
6791  C CD  . GLU B 274 ? 0.2525 0.3679 0.3332 0.0921  0.0667  0.0326  266 GLU B CD  
6792  O OE1 . GLU B 274 ? 0.2567 0.3725 0.3272 0.1024  0.0660  0.0304  266 GLU B OE1 
6793  O OE2 . GLU B 274 ? 0.2354 0.3610 0.3273 0.0913  0.0746  0.0405  266 GLU B OE2 
6794  N N   . ILE B 275 ? 0.1692 0.2778 0.2866 0.0621  0.0459  0.0225  267 ILE B N   
6795  C CA  . ILE B 275 ? 0.1604 0.2760 0.2991 0.0530  0.0460  0.0262  267 ILE B CA  
6796  C C   . ILE B 275 ? 0.1592 0.2918 0.3191 0.0554  0.0482  0.0306  267 ILE B C   
6797  O O   . ILE B 275 ? 0.1547 0.2995 0.3351 0.0517  0.0531  0.0375  267 ILE B O   
6798  C CB  . ILE B 275 ? 0.1566 0.2590 0.2922 0.0443  0.0374  0.0199  267 ILE B CB  
6799  C CG1 . ILE B 275 ? 0.1561 0.2452 0.2767 0.0404  0.0370  0.0173  267 ILE B CG1 
6800  C CG2 . ILE B 275 ? 0.1497 0.2593 0.3076 0.0366  0.0355  0.0223  267 ILE B CG2 
6801  C CD1 . ILE B 275 ? 0.1935 0.2688 0.3084 0.0330  0.0295  0.0114  267 ILE B CD1 
6802  N N   . GLU B 276 ? 0.1638 0.2974 0.3200 0.0616  0.0445  0.0270  268 GLU B N   
6803  C CA  . GLU B 276 ? 0.1631 0.3142 0.3404 0.0647  0.0466  0.0310  268 GLU B CA  
6804  C C   . GLU B 276 ? 0.1657 0.3325 0.3508 0.0714  0.0580  0.0400  268 GLU B C   
6805  O O   . GLU B 276 ? 0.1619 0.3449 0.3720 0.0691  0.0629  0.0470  268 GLU B O   
6806  C CB  . GLU B 276 ? 0.2510 0.3993 0.4198 0.0716  0.0405  0.0249  268 GLU B CB  
6807  C CG  . GLU B 276 ? 0.2685 0.4349 0.4600 0.0748  0.0411  0.0279  268 GLU B CG  
6808  C CD  . GLU B 276 ? 0.2486 0.4195 0.4636 0.0650  0.0355  0.0275  268 GLU B CD  
6809  O OE1 . GLU B 276 ? 0.2186 0.3766 0.4292 0.0566  0.0300  0.0239  268 GLU B OE1 
6810  O OE2 . GLU B 276 ? 0.2361 0.4237 0.4746 0.0663  0.0363  0.0307  268 GLU B OE2 
6811  N N   . ALA B 277 ? 0.1732 0.3352 0.3376 0.0801  0.0623  0.0401  269 ALA B N   
6812  C CA  . ALA B 277 ? 0.1778 0.3533 0.3462 0.0880  0.0737  0.0489  269 ALA B CA  
6813  C C   . ALA B 277 ? 0.1970 0.3772 0.3791 0.0805  0.0801  0.0564  269 ALA B C   
6814  O O   . ALA B 277 ? 0.1735 0.3695 0.3720 0.0831  0.0898  0.0660  269 ALA B O   
6815  C CB  . ALA B 277 ? 0.2059 0.3721 0.3463 0.0991  0.0754  0.0462  269 ALA B CB  
6816  N N   . THR B 278 ? 0.1676 0.3339 0.3428 0.0715  0.0753  0.0526  270 THR B N   
6817  C CA  . THR B 278 ? 0.1631 0.3318 0.3499 0.0643  0.0803  0.0590  270 THR B CA  
6818  C C   . THR B 278 ? 0.1741 0.3543 0.3915 0.0554  0.0798  0.0633  270 THR B C   
6819  O O   . THR B 278 ? 0.1622 0.3528 0.3969 0.0530  0.0878  0.0725  270 THR B O   
6820  C CB  . THR B 278 ? 0.1857 0.3365 0.3563 0.0578  0.0745  0.0528  270 THR B CB  
6821  O OG1 . THR B 278 ? 0.1682 0.3095 0.3130 0.0662  0.0749  0.0491  270 THR B OG1 
6822  C CG2 . THR B 278 ? 0.1565 0.3085 0.3374 0.0506  0.0790  0.0588  270 THR B CG2 
6823  N N   . ARG B 279 ? 0.1514 0.3292 0.3759 0.0507  0.0702  0.0569  271 ARG B N   
6824  C CA  . ARG B 279 ? 0.1461 0.3357 0.4007 0.0440  0.0683  0.0599  271 ARG B CA  
6825  C C   . ARG B 279 ? 0.1912 0.4019 0.4658 0.0500  0.0779  0.0692  271 ARG B C   
6826  O O   . ARG B 279 ? 0.1515 0.3672 0.4427 0.0433  0.0804  0.0749  271 ARG B O   
6827  C CB  . ARG B 279 ? 0.1442 0.3283 0.3995 0.0418  0.0563  0.0508  271 ARG B CB  
6828  C CG  . ARG B 279 ? 0.1405 0.3077 0.3876 0.0331  0.0469  0.0438  271 ARG B CG  
6829  C CD  . ARG B 279 ? 0.1403 0.3026 0.3899 0.0315  0.0354  0.0357  271 ARG B CD  
6830  N NE  . ARG B 279 ? 0.1592 0.3125 0.4144 0.0219  0.0282  0.0326  271 ARG B NE  
6831  C CZ  . ARG B 279 ? 0.2433 0.3799 0.4790 0.0185  0.0251  0.0282  271 ARG B CZ  
6832  N NH1 . ARG B 279 ? 0.1393 0.2664 0.3502 0.0231  0.0278  0.0260  271 ARG B NH1 
6833  N NH2 . ARG B 279 ? 0.1336 0.2629 0.3750 0.0108  0.0189  0.0258  271 ARG B NH2 
6834  N N   . LYS B 280 ? 0.1876 0.4030 0.4509 0.0613  0.0807  0.0684  272 LYS B N   
6835  C CA  . LYS B 280 ? 0.1859 0.4140 0.4570 0.0661  0.0873  0.0744  272 LYS B CA  
6836  C C   . LYS B 280 ? 0.1740 0.4013 0.4382 0.0670  0.0975  0.0829  272 LYS B C   
6837  O O   . LYS B 280 ? 0.1800 0.4154 0.4601 0.0636  0.1024  0.0900  272 LYS B O   
6838  C CB  . LYS B 280 ? 0.1763 0.4074 0.4334 0.0789  0.0871  0.0706  272 LYS B CB  
6839  C CG  . LYS B 280 ? 0.2775 0.5217 0.5414 0.0851  0.0932  0.0757  272 LYS B CG  
6840  C CD  . LYS B 280 ? 0.2517 0.4966 0.5005 0.0975  0.0907  0.0702  272 LYS B CD  
6841  C CE  . LYS B 280 ? 0.3168 0.5745 0.5709 0.1045  0.0969  0.0750  272 LYS B CE  
6842  N NZ  . LYS B 280 ? 0.2880 0.5450 0.5258 0.1169  0.0938  0.0692  272 LYS B NZ  
6843  N N   . HIS B 281 ? 0.1762 0.3932 0.4171 0.0719  0.1004  0.0822  273 HIS B N   
6844  C CA  . HIS B 281 ? 0.2096 0.4243 0.4408 0.0746  0.1093  0.0898  273 HIS B CA  
6845  C C   . HIS B 281 ? 0.2650 0.4787 0.5129 0.0630  0.1107  0.0954  273 HIS B C   
6846  O O   . HIS B 281 ? 0.1939 0.4113 0.4462 0.0637  0.1184  0.1041  273 HIS B O   
6847  C CB  . HIS B 281 ? 0.2754 0.4780 0.4784 0.0818  0.1097  0.0860  273 HIS B CB  
6848  C CG  . HIS B 281 ? 0.2531 0.4506 0.4452 0.0837  0.1170  0.0925  273 HIS B CG  
6849  N ND1 . HIS B 281 ? 0.2334 0.4360 0.4214 0.0912  0.1253  0.1005  273 HIS B ND1 
6850  C CD2 . HIS B 281 ? 0.2310 0.4187 0.4151 0.0799  0.1170  0.0923  273 HIS B CD2 
6851  C CE1 . HIS B 281 ? 0.2185 0.4142 0.3962 0.0921  0.1300  0.1050  273 HIS B CE1 
6852  N NE2 . HIS B 281 ? 0.2173 0.4040 0.3925 0.0853  0.1249  0.0999  273 HIS B NE2 
6853  N N   . LEU B 282 ? 0.1857 0.3936 0.4423 0.0530  0.1033  0.0907  274 LEU B N   
6854  C CA  . LEU B 282 ? 0.1706 0.3749 0.4407 0.0422  0.1030  0.0948  274 LEU B CA  
6855  C C   . LEU B 282 ? 0.1691 0.3813 0.4670 0.0338  0.0988  0.0960  274 LEU B C   
6856  O O   . LEU B 282 ? 0.2531 0.4617 0.5635 0.0249  0.0974  0.0989  274 LEU B O   
6857  C CB  . LEU B 282 ? 0.1605 0.3525 0.4231 0.0361  0.0969  0.0889  274 LEU B CB  
6858  C CG  . LEU B 282 ? 0.1622 0.3454 0.3990 0.0430  0.1006  0.0875  274 LEU B CG  
6859  C CD1 . LEU B 282 ? 0.1532 0.3251 0.3859 0.0356  0.0954  0.0830  274 LEU B CD1 
6860  C CD2 . LEU B 282 ? 0.1755 0.3593 0.4029 0.0492  0.1104  0.0960  274 LEU B CD2 
6861  N N   . GLY B 283 ? 0.2233 0.4454 0.5308 0.0369  0.0960  0.0934  275 GLY B N   
6862  C CA  . GLY B 283 ? 0.1683 0.3980 0.5024 0.0295  0.0911  0.0936  275 GLY B CA  
6863  C C   . GLY B 283 ? 0.1585 0.3806 0.5021 0.0198  0.0794  0.0866  275 GLY B C   
6864  O O   . GLY B 283 ? 0.1712 0.3942 0.5346 0.0115  0.0755  0.0879  275 GLY B O   
6865  N N   . TRP B 284 ? 0.1496 0.3636 0.4795 0.0211  0.0735  0.0790  276 TRP B N   
6866  C CA  . TRP B 284 ? 0.1412 0.3463 0.4766 0.0131  0.0623  0.0718  276 TRP B CA  
6867  C C   . TRP B 284 ? 0.1864 0.3958 0.5277 0.0161  0.0536  0.0643  276 TRP B C   
6868  O O   . TRP B 284 ? 0.1902 0.3984 0.5169 0.0238  0.0534  0.0604  276 TRP B O   
6869  C CB  . TRP B 284 ? 0.1534 0.3458 0.4692 0.0127  0.0624  0.0691  276 TRP B CB  
6870  C CG  . TRP B 284 ? 0.1643 0.3459 0.4832 0.0045  0.0521  0.0626  276 TRP B CG  
6871  C CD1 . TRP B 284 ? 0.1529 0.3224 0.4564 0.0048  0.0414  0.0521  276 TRP B CD1 
6872  C CD2 . TRP B 284 ? 0.2209 0.3939 0.5446 -0.0044 0.0495  0.0638  276 TRP B CD2 
6873  N NE1 . TRP B 284 ? 0.1260 0.2836 0.4298 -0.0030 0.0334  0.0477  276 TRP B NE1 
6874  C CE2 . TRP B 284 ? 0.1247 0.2863 0.4443 -0.0089 0.0383  0.0550  276 TRP B CE2 
6875  C CE3 . TRP B 284 ? 0.2054 0.3772 0.5338 -0.0084 0.0549  0.0710  276 TRP B CE3 
6876  C CZ2 . TRP B 284 ? 0.1520 0.3048 0.4773 -0.0170 0.0331  0.0540  276 TRP B CZ2 
6877  C CZ3 . TRP B 284 ? 0.1683 0.3296 0.4999 -0.0163 0.0494  0.0695  276 TRP B CZ3 
6878  C CH2 . TRP B 284 ? 0.1448 0.2967 0.4743 -0.0205 0.0385  0.0609  276 TRP B CH2 
6879  N N   . ALA B 285 ? 0.1380 0.3512 0.4998 0.0106  0.0457  0.0620  277 ALA B N   
6880  C CA  . ALA B 285 ? 0.1356 0.3529 0.5041 0.0140  0.0365  0.0547  277 ALA B CA  
6881  C C   . ALA B 285 ? 0.1296 0.3347 0.4967 0.0096  0.0235  0.0456  277 ALA B C   
6882  O O   . ALA B 285 ? 0.1679 0.3698 0.5293 0.0135  0.0147  0.0377  277 ALA B O   
6883  C CB  . ALA B 285 ? 0.1752 0.4047 0.5667 0.0122  0.0346  0.0566  277 ALA B CB  
6884  N N   . TYR B 286 ? 0.1275 0.3211 0.4910 0.0022  0.0216  0.0453  278 TYR B N   
6885  C CA  . TYR B 286 ? 0.1280 0.3056 0.4830 -0.0020 0.0085  0.0359  278 TYR B CA  
6886  C C   . TYR B 286 ? 0.1310 0.2927 0.4511 0.0037  0.0055  0.0282  278 TYR B C   
6887  O O   . TYR B 286 ? 0.1310 0.2870 0.4301 0.0063  0.0130  0.0302  278 TYR B O   
6888  C CB  . TYR B 286 ? 0.1743 0.3432 0.5322 -0.0105 0.0080  0.0379  278 TYR B CB  
6889  C CG  . TYR B 286 ? 0.1348 0.3097 0.5120 -0.0161 0.0111  0.0447  278 TYR B CG  
6890  C CD1 . TYR B 286 ? 0.1378 0.3160 0.5340 -0.0188 0.0026  0.0420  278 TYR B CD1 
6891  C CD2 . TYR B 286 ? 0.1348 0.3103 0.5087 -0.0178 0.0221  0.0534  278 TYR B CD2 
6892  C CE1 . TYR B 286 ? 0.2034 0.3856 0.6164 -0.0237 0.0053  0.0481  278 TYR B CE1 
6893  C CE2 . TYR B 286 ? 0.1430 0.3220 0.5327 -0.0223 0.0249  0.0596  278 TYR B CE2 
6894  C CZ  . TYR B 286 ? 0.1969 0.3795 0.6070 -0.0255 0.0166  0.0571  278 TYR B CZ  
6895  O OH  . TYR B 286 ? 0.2142 0.4002 0.6419 -0.0300 0.0191  0.0634  278 TYR B OH  
6896  N N   . PRO B 287 ? 0.1658 0.3197 0.4791 0.0059  -0.0055 0.0195  279 PRO B N   
6897  C CA  . PRO B 287 ? 0.1386 0.2758 0.4192 0.0105  -0.0083 0.0128  279 PRO B CA  
6898  C C   . PRO B 287 ? 0.1376 0.2592 0.4005 0.0056  -0.0078 0.0116  279 PRO B C   
6899  O O   . PRO B 287 ? 0.1348 0.2561 0.4097 -0.0012 -0.0085 0.0140  279 PRO B O   
6900  C CB  . PRO B 287 ? 0.1559 0.2878 0.4367 0.0130  -0.0208 0.0044  279 PRO B CB  
6901  C CG  . PRO B 287 ? 0.1927 0.3385 0.5080 0.0091  -0.0259 0.0059  279 PRO B CG  
6902  C CD  . PRO B 287 ? 0.2197 0.3821 0.5561 0.0059  -0.0148 0.0161  279 PRO B CD  
6903  N N   . ALA B 288 ? 0.1404 0.2494 0.3754 0.0093  -0.0065 0.0082  280 ALA B N   
6904  C CA  . ALA B 288 ? 0.1551 0.2500 0.3723 0.0055  -0.0054 0.0070  280 ALA B CA  
6905  C C   . ALA B 288 ? 0.1793 0.2657 0.4011 0.0000  -0.0141 0.0031  280 ALA B C   
6906  O O   . ALA B 288 ? 0.1556 0.2380 0.3790 0.0017  -0.0233 -0.0025 280 ALA B O   
6907  C CB  . ALA B 288 ? 0.1445 0.2260 0.3334 0.0102  -0.0053 0.0025  280 ALA B CB  
6908  N N   . PHE B 289 ? 0.1373 0.2208 0.3609 -0.0057 -0.0114 0.0059  281 PHE B N   
6909  C CA  . PHE B 289 ? 0.1506 0.2247 0.3759 -0.0107 -0.0185 0.0028  281 PHE B CA  
6910  C C   . PHE B 289 ? 0.1530 0.2349 0.4052 -0.0139 -0.0256 0.0029  281 PHE B C   
6911  O O   . PHE B 289 ? 0.1929 0.2663 0.4470 -0.0170 -0.0336 -0.0009 281 PHE B O   
6912  C CB  . PHE B 289 ? 0.1476 0.2052 0.3497 -0.0079 -0.0250 -0.0047 281 PHE B CB  
6913  C CG  . PHE B 289 ? 0.1452 0.1946 0.3232 -0.0057 -0.0186 -0.0049 281 PHE B CG  
6914  C CD1 . PHE B 289 ? 0.1771 0.2203 0.3458 -0.0093 -0.0144 -0.0034 281 PHE B CD1 
6915  C CD2 . PHE B 289 ? 0.1692 0.2173 0.3348 0.0000  -0.0171 -0.0065 281 PHE B CD2 
6916  C CE1 . PHE B 289 ? 0.2042 0.2406 0.3531 -0.0075 -0.0091 -0.0038 281 PHE B CE1 
6917  C CE2 . PHE B 289 ? 0.1543 0.1945 0.2996 0.0016  -0.0119 -0.0068 281 PHE B CE2 
6918  C CZ  . PHE B 289 ? 0.1717 0.2064 0.3095 -0.0023 -0.0080 -0.0055 281 PHE B CZ  
6919  N N   . GLU B 290 ? 0.1368 0.2346 0.4104 -0.0130 -0.0231 0.0070  282 GLU B N   
6920  C CA  . GLU B 290 ? 0.1485 0.2557 0.4523 -0.0170 -0.0290 0.0081  282 GLU B CA  
6921  C C   . GLU B 290 ? 0.2042 0.3222 0.5276 -0.0226 -0.0201 0.0177  282 GLU B C   
6922  O O   . GLU B 290 ? 0.2329 0.3614 0.5578 -0.0203 -0.0090 0.0245  282 GLU B O   
6923  C CB  . GLU B 290 ? 0.1988 0.3171 0.5162 -0.0124 -0.0329 0.0063  282 GLU B CB  
6924  C CG  . GLU B 290 ? 0.2495 0.3552 0.5478 -0.0067 -0.0430 -0.0034 282 GLU B CG  
6925  C CD  . GLU B 290 ? 0.3188 0.4343 0.6315 -0.0020 -0.0493 -0.0065 282 GLU B CD  
6926  O OE1 . GLU B 290 ? 0.3605 0.4931 0.7032 -0.0044 -0.0479 -0.0019 282 GLU B OE1 
6927  O OE2 . GLU B 290 ? 0.3155 0.4217 0.6099 0.0044  -0.0554 -0.0134 282 GLU B OE2 
6928  N N   . ILE B 291 ? 0.1480 0.2622 0.4846 -0.0291 -0.0248 0.0181  283 ILE B N   
6929  C CA  . ILE B 291 ? 0.1921 0.3120 0.5429 -0.0345 -0.0169 0.0270  283 ILE B CA  
6930  C C   . ILE B 291 ? 0.2095 0.3299 0.5791 -0.0379 -0.0236 0.0271  283 ILE B C   
6931  O O   . ILE B 291 ? 0.1955 0.3058 0.5660 -0.0394 -0.0358 0.0199  283 ILE B O   
6932  C CB  . ILE B 291 ? 0.1301 0.2378 0.4664 -0.0379 -0.0152 0.0273  283 ILE B CB  
6933  C CG1 . ILE B 291 ? 0.1298 0.2305 0.4349 -0.0328 -0.0087 0.0257  283 ILE B CG1 
6934  C CG2 . ILE B 291 ? 0.1888 0.2976 0.5308 -0.0414 -0.0073 0.0359  283 ILE B CG2 
6935  C CD1 . ILE B 291 ? 0.1290 0.2152 0.4153 -0.0351 -0.0093 0.0235  283 ILE B CD1 
6936  N N   . PRO B 292 ? 0.1997 0.3308 0.5842 -0.0388 -0.0163 0.0348  284 PRO B N   
6937  C CA  . PRO B 292 ? 0.2107 0.3426 0.6155 -0.0424 -0.0226 0.0351  284 PRO B CA  
6938  C C   . PRO B 292 ? 0.2491 0.3683 0.6536 -0.0476 -0.0267 0.0351  284 PRO B C   
6939  O O   . PRO B 292 ? 0.2181 0.3314 0.6099 -0.0489 -0.0205 0.0386  284 PRO B O   
6940  C CB  . PRO B 292 ? 0.2157 0.3626 0.6343 -0.0418 -0.0111 0.0448  284 PRO B CB  
6941  C CG  . PRO B 292 ? 0.2653 0.4139 0.6674 -0.0394 0.0018  0.0510  284 PRO B CG  
6942  C CD  . PRO B 292 ? 0.1687 0.3111 0.5515 -0.0361 -0.0017 0.0439  284 PRO B CD  
6943  N N   . GLN B 293 ? 0.2161 0.3310 0.6349 -0.0499 -0.0376 0.0311  285 GLN B N   
6944  C CA  . GLN B 293 ? 0.2739 0.3756 0.6922 -0.0538 -0.0438 0.0295  285 GLN B CA  
6945  C C   . GLN B 293 ? 0.3154 0.4186 0.7372 -0.0573 -0.0331 0.0395  285 GLN B C   
6946  O O   . GLN B 293 ? 0.2787 0.3710 0.6903 -0.0592 -0.0337 0.0395  285 GLN B O   
6947  C CB  . GLN B 293 ? 0.2591 0.3574 0.6951 -0.0550 -0.0569 0.0242  285 GLN B CB  
6948  C CG  . GLN B 293 ? 0.3129 0.3954 0.7454 -0.0571 -0.0666 0.0199  285 GLN B CG  
6949  C CD  . GLN B 293 ? 0.3856 0.4553 0.7935 -0.0539 -0.0729 0.0117  285 GLN B CD  
6950  O OE1 . GLN B 293 ? 0.4516 0.5207 0.8512 -0.0497 -0.0785 0.0048  285 GLN B OE1 
6951  N NE2 . GLN B 293 ? 0.3307 0.3901 0.7266 -0.0557 -0.0719 0.0126  285 GLN B NE2 
6952  N N   . GLU B 294 ? 0.2957 0.4121 0.7310 -0.0576 -0.0230 0.0481  286 GLU B N   
6953  C CA  . GLU B 294 ? 0.3095 0.4274 0.7492 -0.0602 -0.0127 0.0581  286 GLU B CA  
6954  C C   . GLU B 294 ? 0.1946 0.3087 0.6117 -0.0583 -0.0034 0.0612  286 GLU B C   
6955  O O   . GLU B 294 ? 0.2063 0.3145 0.6204 -0.0605 0.0005  0.0658  286 GLU B O   
6956  C CB  . GLU B 294 ? 0.4285 0.5619 0.8870 -0.0598 -0.0041 0.0663  286 GLU B CB  
6957  C CG  . GLU B 294 ? 0.5292 0.6694 0.9822 -0.0579 0.0117  0.0770  286 GLU B CG  
6958  C CD  . GLU B 294 ? 0.6139 0.7701 1.0846 -0.0564 0.0197  0.0844  286 GLU B CD  
6959  O OE1 . GLU B 294 ? 0.6277 0.7913 1.0910 -0.0524 0.0325  0.0919  286 GLU B OE1 
6960  O OE2 . GLU B 294 ? 0.6505 0.8119 1.1424 -0.0586 0.0131  0.0825  286 GLU B OE2 
6961  N N   . ILE B 295 ? 0.1929 0.3102 0.5945 -0.0540 -0.0001 0.0586  287 ILE B N   
6962  C CA  . ILE B 295 ? 0.1995 0.3123 0.5798 -0.0521 0.0076  0.0606  287 ILE B CA  
6963  C C   . ILE B 295 ? 0.2040 0.3018 0.5714 -0.0543 -0.0008 0.0537  287 ILE B C   
6964  O O   . ILE B 295 ? 0.1604 0.2516 0.5169 -0.0552 0.0035  0.0565  287 ILE B O   
6965  C CB  . ILE B 295 ? 0.2324 0.3530 0.6010 -0.0466 0.0134  0.0598  287 ILE B CB  
6966  C CG1 . ILE B 295 ? 0.2283 0.3635 0.6069 -0.0433 0.0237  0.0679  287 ILE B CG1 
6967  C CG2 . ILE B 295 ? 0.2048 0.3191 0.5509 -0.0446 0.0191  0.0598  287 ILE B CG2 
6968  C CD1 . ILE B 295 ? 0.2286 0.3717 0.5952 -0.0367 0.0301  0.0677  287 ILE B CD1 
6969  N N   . TYR B 296 ? 0.1715 0.2633 0.5395 -0.0546 -0.0132 0.0447  288 TYR B N   
6970  C CA  . TYR B 296 ? 0.1612 0.2383 0.5179 -0.0561 -0.0221 0.0380  288 TYR B CA  
6971  C C   . TYR B 296 ? 0.1704 0.2410 0.5350 -0.0599 -0.0237 0.0414  288 TYR B C   
6972  O O   . TYR B 296 ? 0.1920 0.2534 0.5440 -0.0609 -0.0231 0.0412  288 TYR B O   
6973  C CB  . TYR B 296 ? 0.2161 0.2881 0.5738 -0.0548 -0.0357 0.0280  288 TYR B CB  
6974  C CG  . TYR B 296 ? 0.1993 0.2705 0.5415 -0.0511 -0.0369 0.0222  288 TYR B CG  
6975  C CD1 . TYR B 296 ? 0.1867 0.2521 0.5094 -0.0506 -0.0324 0.0216  288 TYR B CD1 
6976  C CD2 . TYR B 296 ? 0.1997 0.2759 0.5474 -0.0481 -0.0430 0.0171  288 TYR B CD2 
6977  C CE1 . TYR B 296 ? 0.1412 0.2055 0.4513 -0.0476 -0.0336 0.0164  288 TYR B CE1 
6978  C CE2 . TYR B 296 ? 0.2022 0.2774 0.5365 -0.0445 -0.0445 0.0118  288 TYR B CE2 
6979  C CZ  . TYR B 296 ? 0.1638 0.2326 0.4786 -0.0443 -0.0395 0.0116  288 TYR B CZ  
6980  O OH  . TYR B 296 ? 0.1448 0.2071 0.4339 -0.0383 -0.0393 0.0064  288 TYR B OH  
6981  N N   . ASP B 297 ? 0.1788 0.2544 0.5649 -0.0621 -0.0258 0.0446  289 ASP B N   
6982  C CA  . ASP B 297 ? 0.2426 0.3119 0.6384 -0.0659 -0.0279 0.0478  289 ASP B CA  
6983  C C   . ASP B 297 ? 0.2376 0.3083 0.6279 -0.0667 -0.0155 0.0569  289 ASP B C   
6984  O O   . ASP B 297 ? 0.2668 0.3283 0.6536 -0.0688 -0.0170 0.0578  289 ASP B O   
6985  C CB  . ASP B 297 ? 0.2862 0.3617 0.7085 -0.0682 -0.0321 0.0499  289 ASP B CB  
6986  C CG  . ASP B 297 ? 0.3166 0.3887 0.7449 -0.0670 -0.0463 0.0401  289 ASP B CG  
6987  O OD1 . ASP B 297 ? 0.3374 0.3989 0.7499 -0.0648 -0.0549 0.0316  289 ASP B OD1 
6988  O OD2 . ASP B 297 ? 0.4014 0.4810 0.8504 -0.0679 -0.0491 0.0410  289 ASP B OD2 
6989  N N   . ALA B 298 ? 0.2336 0.3151 0.6217 -0.0643 -0.0033 0.0636  290 ALA B N   
6990  C CA  . ALA B 298 ? 0.1848 0.2670 0.5654 -0.0637 0.0084  0.0719  290 ALA B CA  
6991  C C   . ALA B 298 ? 0.2129 0.2857 0.5697 -0.0622 0.0091  0.0683  290 ALA B C   
6992  O O   . ALA B 298 ? 0.2111 0.2789 0.5618 -0.0628 0.0139  0.0727  290 ALA B O   
6993  C CB  . ALA B 298 ? 0.2613 0.3569 0.6438 -0.0600 0.0208  0.0794  290 ALA B CB  
6994  N N   . TRP B 299 ? 0.1814 0.2519 0.5250 -0.0602 0.0047  0.0607  291 TRP B N   
6995  C CA  . TRP B 299 ? 0.1634 0.2261 0.4854 -0.0588 0.0058  0.0574  291 TRP B CA  
6996  C C   . TRP B 299 ? 0.1663 0.2153 0.4822 -0.0610 -0.0049 0.0504  291 TRP B C   
6997  O O   . TRP B 299 ? 0.1642 0.2059 0.4647 -0.0606 -0.0032 0.0493  291 TRP B O   
6998  C CB  . TRP B 299 ? 0.1534 0.2198 0.4636 -0.0554 0.0069  0.0528  291 TRP B CB  
6999  C CG  . TRP B 299 ? 0.1490 0.2242 0.4521 -0.0514 0.0192  0.0588  291 TRP B CG  
7000  C CD1 . TRP B 299 ? 0.1994 0.2866 0.5092 -0.0483 0.0248  0.0622  291 TRP B CD1 
7001  C CD2 . TRP B 299 ? 0.1627 0.2352 0.4498 -0.0492 0.0271  0.0616  291 TRP B CD2 
7002  N NE1 . TRP B 299 ? 0.2143 0.3061 0.5125 -0.0438 0.0356  0.0670  291 TRP B NE1 
7003  C CE2 . TRP B 299 ? 0.1577 0.2405 0.4420 -0.0443 0.0370  0.0666  291 TRP B CE2 
7004  C CE3 . TRP B 299 ? 0.1471 0.2093 0.4218 -0.0504 0.0264  0.0602  291 TRP B CE3 
7005  C CZ2 . TRP B 299 ? 0.2116 0.2943 0.4809 -0.0403 0.0458  0.0700  291 TRP B CZ2 
7006  C CZ3 . TRP B 299 ? 0.1727 0.2355 0.4338 -0.0469 0.0353  0.0636  291 TRP B CZ3 
7007  C CH2 . TRP B 299 ? 0.1668 0.2396 0.4252 -0.0418 0.0448  0.0684  291 TRP B CH2 
7008  N N   . ASN B 300 ? 0.1717 0.2171 0.4987 -0.0627 -0.0160 0.0453  292 ASN B N   
7009  C CA  . ASN B 300 ? 0.2250 0.2572 0.5432 -0.0631 -0.0272 0.0372  292 ASN B CA  
7010  C C   . ASN B 300 ? 0.2417 0.2654 0.5565 -0.0651 -0.0267 0.0398  292 ASN B C   
7011  O O   . ASN B 300 ? 0.2043 0.2300 0.5329 -0.0675 -0.0242 0.0461  292 ASN B O   
7012  C CB  . ASN B 300 ? 0.2107 0.2408 0.5423 -0.0634 -0.0396 0.0315  292 ASN B CB  
7013  C CG  . ASN B 300 ? 0.2704 0.2867 0.5905 -0.0621 -0.0516 0.0224  292 ASN B CG  
7014  O OD1 . ASN B 300 ? 0.2469 0.2546 0.5671 -0.0634 -0.0560 0.0220  292 ASN B OD1 
7015  N ND2 . ASN B 300 ? 0.2654 0.2791 0.5743 -0.0589 -0.0566 0.0151  292 ASN B ND2 
7016  N N   . ALA B 301 ? 0.2314 0.2453 0.5278 -0.0640 -0.0290 0.0352  293 ALA B N   
7017  C CA  . ALA B 301 ? 0.1841 0.1895 0.4749 -0.0653 -0.0285 0.0371  293 ALA B CA  
7018  C C   . ALA B 301 ? 0.2056 0.1982 0.4935 -0.0652 -0.0415 0.0297  293 ALA B C   
7019  O O   . ALA B 301 ? 0.2063 0.1900 0.4853 -0.0655 -0.0424 0.0294  293 ALA B O   
7020  C CB  . ALA B 301 ? 0.1766 0.1807 0.4489 -0.0636 -0.0203 0.0383  293 ALA B CB  
7021  N N   . LYS B 302 ? 0.1960 0.1871 0.4907 -0.0643 -0.0518 0.0237  294 LYS B N   
7022  C CA  A LYS B 302 ? 0.2053 0.1837 0.4956 -0.0628 -0.0648 0.0161  294 LYS B CA  
7023  C CA  B LYS B 302 ? 0.2053 0.1837 0.4955 -0.0627 -0.0648 0.0161  294 LYS B CA  
7024  C C   . LYS B 302 ? 0.2165 0.1899 0.5179 -0.0654 -0.0679 0.0195  294 LYS B C   
7025  O O   . LYS B 302 ? 0.2268 0.1891 0.5181 -0.0645 -0.0729 0.0164  294 LYS B O   
7026  C CB  A LYS B 302 ? 0.2562 0.2345 0.5527 -0.0604 -0.0754 0.0094  294 LYS B CB  
7027  C CB  B LYS B 302 ? 0.2564 0.2344 0.5525 -0.0603 -0.0754 0.0092  294 LYS B CB  
7028  C CG  A LYS B 302 ? 0.2655 0.2310 0.5594 -0.0576 -0.0899 0.0017  294 LYS B CG  
7029  C CG  B LYS B 302 ? 0.2697 0.2483 0.5511 -0.0568 -0.0755 0.0038  294 LYS B CG  
7030  C CD  A LYS B 302 ? 0.2772 0.2438 0.5816 -0.0552 -0.1000 -0.0038 294 LYS B CD  
7031  C CD  B LYS B 302 ? 0.3031 0.2678 0.5655 -0.0525 -0.0849 -0.0050 294 LYS B CD  
7032  C CE  A LYS B 302 ? 0.2462 0.1993 0.5460 -0.0510 -0.1151 -0.0119 294 LYS B CE  
7033  C CE  B LYS B 302 ? 0.2413 0.2055 0.4865 -0.0496 -0.0823 -0.0091 294 LYS B CE  
7034  N NZ  A LYS B 302 ? 0.2540 0.2073 0.5623 -0.0474 -0.1256 -0.0179 294 LYS B NZ  
7035  N NZ  B LYS B 302 ? 0.2708 0.2299 0.5120 -0.0448 -0.0932 -0.0173 294 LYS B NZ  
7036  N N   . GLU B 303 ? 0.2207 0.2021 0.5433 -0.0687 -0.0647 0.0261  295 GLU B N   
7037  C CA  . GLU B 303 ? 0.2325 0.2090 0.5682 -0.0716 -0.0683 0.0294  295 GLU B CA  
7038  C C   . GLU B 303 ? 0.2683 0.2410 0.5952 -0.0731 -0.0601 0.0350  295 GLU B C   
7039  O O   . GLU B 303 ? 0.2414 0.2030 0.5638 -0.0732 -0.0663 0.0328  295 GLU B O   
7040  C CB  . GLU B 303 ? 0.2399 0.2263 0.6014 -0.0749 -0.0660 0.0356  295 GLU B CB  
7041  C CG  . GLU B 303 ? 0.3186 0.3004 0.6954 -0.0785 -0.0685 0.0401  295 GLU B CG  
7042  C CD  . GLU B 303 ? 0.4341 0.4254 0.8385 -0.0819 -0.0669 0.0461  295 GLU B CD  
7043  O OE1 . GLU B 303 ? 0.4084 0.4093 0.8206 -0.0810 -0.0659 0.0455  295 GLU B OE1 
7044  O OE2 . GLU B 303 ? 0.4575 0.4466 0.8761 -0.0854 -0.0666 0.0515  295 GLU B OE2 
7045  N N   . LYS B 304 ? 0.2361 0.2174 0.5599 -0.0736 -0.0466 0.0422  296 LYS B N   
7046  C CA  . LYS B 304 ? 0.2665 0.2435 0.5803 -0.0741 -0.0390 0.0473  296 LYS B CA  
7047  C C   . LYS B 304 ? 0.2553 0.2217 0.5467 -0.0713 -0.0431 0.0403  296 LYS B C   
7048  O O   . LYS B 304 ? 0.2364 0.1938 0.5207 -0.0716 -0.0434 0.0412  296 LYS B O   
7049  C CB  . LYS B 304 ? 0.2181 0.2060 0.5311 -0.0738 -0.0241 0.0558  296 LYS B CB  
7050  N N   . GLY B 305 ? 0.2334 0.2003 0.5137 -0.0685 -0.0464 0.0334  297 GLY B N   
7051  C CA  . GLY B 305 ? 0.2119 0.1694 0.4712 -0.0655 -0.0495 0.0270  297 GLY B CA  
7052  C C   . GLY B 305 ? 0.2233 0.1674 0.4788 -0.0642 -0.0622 0.0204  297 GLY B C   
7053  O O   . GLY B 305 ? 0.2900 0.2247 0.5323 -0.0627 -0.0632 0.0186  297 GLY B O   
7054  N N   . ALA B 306 ? 0.2305 0.1733 0.4972 -0.0639 -0.0724 0.0164  298 ALA B N   
7055  C CA  . ALA B 306 ? 0.2433 0.1733 0.5068 -0.0617 -0.0853 0.0101  298 ALA B CA  
7056  C C   . ALA B 306 ? 0.2528 0.1771 0.5223 -0.0645 -0.0846 0.0151  298 ALA B C   
7057  O O   . ALA B 306 ? 0.2705 0.1830 0.5286 -0.0622 -0.0910 0.0110  298 ALA B O   
7058  C CB  . ALA B 306 ? 0.3054 0.2358 0.5823 -0.0606 -0.0963 0.0056  298 ALA B CB  
7059  N N   . LYS B 307 ? 0.2538 0.1862 0.5409 -0.0692 -0.0771 0.0239  299 LYS B N   
7060  C CA  . LYS B 307 ? 0.2632 0.1903 0.5566 -0.0721 -0.0753 0.0296  299 LYS B CA  
7061  C C   . LYS B 307 ? 0.2774 0.1993 0.5524 -0.0709 -0.0678 0.0317  299 LYS B C   
7062  O O   . LYS B 307 ? 0.3083 0.2189 0.5774 -0.0706 -0.0718 0.0309  299 LYS B O   
7063  C CB  . LYS B 307 ? 0.2684 0.2060 0.5835 -0.0768 -0.0670 0.0394  299 LYS B CB  
7064  C CG  . LYS B 307 ? 0.3253 0.2672 0.6629 -0.0786 -0.0747 0.0385  299 LYS B CG  
7065  C CD  . LYS B 307 ? 0.3260 0.2817 0.6822 -0.0821 -0.0637 0.0482  299 LYS B CD  
7066  C CE  . LYS B 307 ? 0.3827 0.3412 0.7653 -0.0850 -0.0708 0.0492  299 LYS B CE  
7067  N NZ  . LYS B 307 ? 0.3227 0.2944 0.7245 -0.0883 -0.0597 0.0593  299 LYS B NZ  
7068  N N   . LEU B 308 ? 0.2467 0.1764 0.5130 -0.0701 -0.0573 0.0343  300 LEU B N   
7069  C CA  . LEU B 308 ? 0.3132 0.2387 0.5628 -0.0685 -0.0501 0.0362  300 LEU B CA  
7070  C C   . LEU B 308 ? 0.2467 0.1591 0.4784 -0.0647 -0.0589 0.0276  300 LEU B C   
7071  O O   . LEU B 308 ? 0.2531 0.1561 0.4763 -0.0639 -0.0588 0.0285  300 LEU B O   
7072  C CB  . LEU B 308 ? 0.2285 0.1648 0.4719 -0.0674 -0.0395 0.0385  300 LEU B CB  
7073  C CG  . LEU B 308 ? 0.2239 0.1561 0.4497 -0.0650 -0.0331 0.0393  300 LEU B CG  
7074  C CD1 . LEU B 308 ? 0.2297 0.1614 0.4592 -0.0663 -0.0242 0.0489  300 LEU B CD1 
7075  C CD2 . LEU B 308 ? 0.2264 0.1676 0.4448 -0.0632 -0.0267 0.0381  300 LEU B CD2 
7076  N N   . GLU B 309 ? 0.2796 0.1908 0.5045 -0.0616 -0.0666 0.0192  301 GLU B N   
7077  C CA  . GLU B 309 ? 0.2505 0.1495 0.4572 -0.0568 -0.0749 0.0109  301 GLU B CA  
7078  C C   . GLU B 309 ? 0.2648 0.1525 0.4747 -0.0560 -0.0863 0.0078  301 GLU B C   
7079  O O   . GLU B 309 ? 0.2720 0.1484 0.4682 -0.0527 -0.0903 0.0044  301 GLU B O   
7080  C CB  . GLU B 309 ? 0.2430 0.1437 0.4409 -0.0531 -0.0791 0.0033  301 GLU B CB  
7081  C CG  . GLU B 309 ? 0.2489 0.1375 0.4264 -0.0469 -0.0868 -0.0053 301 GLU B CG  
7082  C CD  . GLU B 309 ? 0.2890 0.1800 0.4543 -0.0433 -0.0862 -0.0108 301 GLU B CD  
7083  O OE1 . GLU B 309 ? 0.3298 0.2317 0.5021 -0.0459 -0.0798 -0.0080 301 GLU B OE1 
7084  O OE2 . GLU B 309 ? 0.3304 0.2121 0.4783 -0.0373 -0.0919 -0.0179 301 GLU B OE2 
7085  N N   . ALA B 310 ? 0.2816 0.1720 0.5100 -0.0586 -0.0919 0.0090  302 ALA B N   
7086  C CA  . ALA B 310 ? 0.3171 0.1970 0.5510 -0.0583 -0.1027 0.0068  302 ALA B CA  
7087  C C   . ALA B 310 ? 0.2942 0.1680 0.5273 -0.0607 -0.0979 0.0128  302 ALA B C   
7088  O O   . ALA B 310 ? 0.3529 0.2141 0.5767 -0.0578 -0.1054 0.0089  302 ALA B O   
7089  C CB  . ALA B 310 ? 0.3283 0.2136 0.5857 -0.0615 -0.1081 0.0084  302 ALA B CB  
7090  N N   . GLY B 311 ? 0.3177 0.1997 0.5594 -0.0651 -0.0853 0.0221  303 GLY B N   
7091  C CA  . GLY B 311 ? 0.2948 0.1704 0.5341 -0.0667 -0.0797 0.0283  303 GLY B CA  
7092  C C   . GLY B 311 ? 0.3260 0.1924 0.5420 -0.0620 -0.0789 0.0246  303 GLY B C   
7093  O O   . GLY B 311 ? 0.3048 0.1591 0.5139 -0.0606 -0.0826 0.0241  303 GLY B O   
7094  N N   . TRP B 312 ? 0.2974 0.1692 0.5012 -0.0593 -0.0741 0.0218  304 TRP B N   
7095  C CA  . TRP B 312 ? 0.2787 0.1422 0.4612 -0.0544 -0.0736 0.0178  304 TRP B CA  
7096  C C   . TRP B 312 ? 0.3559 0.2070 0.5263 -0.0491 -0.0867 0.0083  304 TRP B C   
7097  O O   . TRP B 312 ? 0.2974 0.1374 0.4547 -0.0455 -0.0890 0.0064  304 TRP B O   
7098  C CB  . TRP B 312 ? 0.2630 0.1351 0.4371 -0.0527 -0.0665 0.0165  304 TRP B CB  
7099  C CG  . TRP B 312 ? 0.2619 0.1265 0.4168 -0.0479 -0.0649 0.0134  304 TRP B CG  
7100  C CD1 . TRP B 312 ? 0.2597 0.1234 0.4099 -0.0476 -0.0562 0.0190  304 TRP B CD1 
7101  C CD2 . TRP B 312 ? 0.2838 0.1402 0.4215 -0.0417 -0.0726 0.0038  304 TRP B CD2 
7102  N NE1 . TRP B 312 ? 0.3052 0.1663 0.4332 -0.0403 -0.0566 0.0128  304 TRP B NE1 
7103  C CE2 . TRP B 312 ? 0.2852 0.1412 0.4062 -0.0370 -0.0664 0.0038  304 TRP B CE2 
7104  C CE3 . TRP B 312 ? 0.3038 0.1565 0.4354 -0.0379 -0.0827 -0.0047 304 TRP B CE3 
7105  C CZ2 . TRP B 312 ? 0.2884 0.1414 0.3887 -0.0292 -0.0695 -0.0042 304 TRP B CZ2 
7106  C CZ3 . TRP B 312 ? 0.2729 0.1176 0.3847 -0.0306 -0.0869 -0.0125 304 TRP B CZ3 
7107  C CH2 . TRP B 312 ? 0.2700 0.1175 0.3661 -0.0261 -0.0793 -0.0118 304 TRP B CH2 
7108  N N   . ASN B 313 ? 0.3332 0.1856 0.5070 -0.0476 -0.0956 0.0022  305 ASN B N   
7109  C CA  . ASN B 313 ? 0.3579 0.1987 0.5196 -0.0414 -0.1085 -0.0067 305 ASN B CA  
7110  C C   . ASN B 313 ? 0.3368 0.1668 0.5023 -0.0419 -0.1151 -0.0056 305 ASN B C   
7111  O O   . ASN B 313 ? 0.3484 0.1668 0.4985 -0.0360 -0.1222 -0.0112 305 ASN B O   
7112  C CB  . ASN B 313 ? 0.3896 0.2337 0.5567 -0.0397 -0.1171 -0.0122 305 ASN B CB  
7113  C CG  . ASN B 313 ? 0.4211 0.2703 0.5759 -0.0361 -0.1141 -0.0167 305 ASN B CG  
7114  O OD1 . ASN B 313 ? 0.3393 0.1864 0.4777 -0.0327 -0.1092 -0.0185 305 ASN B OD1 
7115  N ND2 . ASN B 313 ? 0.4044 0.2599 0.5674 -0.0364 -0.1175 -0.0187 305 ASN B ND2 
7116  N N   . GLU B 314 ? 0.3550 0.1886 0.5412 -0.0485 -0.1130 0.0015  306 GLU B N   
7117  C CA  . GLU B 314 ? 0.3770 0.1999 0.5681 -0.0496 -0.1188 0.0033  306 GLU B CA  
7118  C C   . GLU B 314 ? 0.4035 0.2183 0.5807 -0.0481 -0.1126 0.0062  306 GLU B C   
7119  O O   . GLU B 314 ? 0.4047 0.2066 0.5720 -0.0443 -0.1201 0.0027  306 GLU B O   
7120  C CB  . GLU B 314 ? 0.4329 0.2622 0.6501 -0.0573 -0.1163 0.0111  306 GLU B CB  
7121  C CG  . GLU B 314 ? 0.4277 0.2620 0.6599 -0.0579 -0.1256 0.0072  306 GLU B CG  
7122  C CD  . GLU B 314 ? 0.5367 0.3817 0.7951 -0.0653 -0.1200 0.0155  306 GLU B CD  
7123  O OE1 . GLU B 314 ? 0.5156 0.3669 0.7876 -0.0659 -0.1258 0.0131  306 GLU B OE1 
7124  O OE2 . GLU B 314 ? 0.5432 0.3902 0.8082 -0.0698 -0.1097 0.0245  306 GLU B OE2 
7125  N N   . LEU B 315 ? 0.3694 0.1913 0.5448 -0.0501 -0.0995 0.0125  307 LEU B N   
7126  C CA  . LEU B 315 ? 0.3534 0.1679 0.5148 -0.0476 -0.0935 0.0152  307 LEU B CA  
7127  C C   . LEU B 315 ? 0.4080 0.2144 0.5460 -0.0393 -0.0993 0.0060  307 LEU B C   
7128  O O   . LEU B 315 ? 0.3438 0.1385 0.4694 -0.0351 -0.1019 0.0046  307 LEU B O   
7129  C CB  . LEU B 315 ? 0.3188 0.1436 0.4830 -0.0505 -0.0789 0.0233  307 LEU B CB  
7130  C CG  . LEU B 315 ? 0.3726 0.1907 0.5226 -0.0472 -0.0718 0.0270  307 LEU B CG  
7131  C CD1 . LEU B 315 ? 0.4396 0.2488 0.5950 -0.0495 -0.0701 0.0342  307 LEU B CD1 
7132  C CD2 . LEU B 315 ? 0.3045 0.1340 0.4543 -0.0479 -0.0593 0.0324  307 LEU B CD2 
7133  N N   . PHE B 316 ? 0.4031 0.2156 0.5345 -0.0362 -0.1008 -0.0001 308 PHE B N   
7134  C CA  . PHE B 316 ? 0.3247 0.1307 0.4338 -0.0277 -0.1053 -0.0087 308 PHE B CA  
7135  C C   . PHE B 316 ? 0.3879 0.1826 0.4893 -0.0222 -0.1186 -0.0158 308 PHE B C   
7136  O O   . PHE B 316 ? 0.3751 0.1613 0.4575 -0.0146 -0.1221 -0.0211 308 PHE B O   
7137  C CB  . PHE B 316 ? 0.3445 0.1598 0.4493 -0.0259 -0.1030 -0.0130 308 PHE B CB  
7138  C CG  . PHE B 316 ? 0.4461 0.2568 0.5283 -0.0172 -0.1043 -0.0205 308 PHE B CG  
7139  C CD1 . PHE B 316 ? 0.4352 0.2475 0.5061 -0.0144 -0.0960 -0.0189 308 PHE B CD1 
7140  C CD2 . PHE B 316 ? 0.4522 0.2600 0.5232 -0.0106 -0.1126 -0.0289 308 PHE B CD2 
7141  C CE1 . PHE B 316 ? 0.3667 0.1818 0.4168 -0.0055 -0.0946 -0.0251 308 PHE B CE1 
7142  C CE2 . PHE B 316 ? 0.3718 0.1761 0.4217 -0.0018 -0.1126 -0.0354 308 PHE B CE2 
7143  C CZ  . PHE B 316 ? 0.3455 0.1559 0.3856 0.0005  -0.1027 -0.0331 308 PHE B CZ  
7144  N N   . ALA B 317 ? 0.4036 0.1984 0.5196 -0.0254 -0.1264 -0.0160 309 ALA B N   
7145  C CA  . ALA B 317 ? 0.4431 0.2264 0.5537 -0.0205 -0.1398 -0.0219 309 ALA B CA  
7146  C C   . ALA B 317 ? 0.4432 0.2154 0.5502 -0.0203 -0.1405 -0.0191 309 ALA B C   
7147  O O   . ALA B 317 ? 0.4402 0.2018 0.5309 -0.0128 -0.1482 -0.0249 309 ALA B O   
7148  C CB  . ALA B 317 ? 0.3932 0.1791 0.5230 -0.0244 -0.1481 -0.0221 309 ALA B CB  
7149  N N   . GLN B 318 ? 0.4472 0.2214 0.5683 -0.0278 -0.1321 -0.0098 310 GLN B N   
7150  C CA  . GLN B 318 ? 0.3897 0.1527 0.5056 -0.0273 -0.1311 -0.0063 310 GLN B CA  
7151  C C   . GLN B 318 ? 0.4047 0.1633 0.4972 -0.0196 -0.1273 -0.0095 310 GLN B C   
7152  O O   . GLN B 318 ? 0.4408 0.1877 0.5195 -0.0138 -0.1329 -0.0129 310 GLN B O   
7153  C CB  . GLN B 318 ? 0.5142 0.2811 0.6481 -0.0360 -0.1208 0.0051  310 GLN B CB  
7154  C CG  . GLN B 318 ? 0.6239 0.3948 0.7825 -0.0434 -0.1246 0.0087  310 GLN B CG  
7155  C CD  . GLN B 318 ? 0.6936 0.4680 0.8689 -0.0512 -0.1136 0.0205  310 GLN B CD  
7156  O OE1 . GLN B 318 ? 0.6956 0.4809 0.8751 -0.0541 -0.1016 0.0267  310 GLN B OE1 
7157  N NE2 . GLN B 318 ? 0.7166 0.4815 0.9011 -0.0542 -0.1175 0.0240  310 GLN B NE2 
7158  N N   . TYR B 319 ? 0.4087 0.1768 0.4967 -0.0192 -0.1183 -0.0088 311 TYR B N   
7159  C CA  . TYR B 319 ? 0.3946 0.1600 0.4618 -0.0117 -0.1145 -0.0120 311 TYR B CA  
7160  C C   . TYR B 319 ? 0.3934 0.1534 0.4417 -0.0018 -0.1240 -0.0226 311 TYR B C   
7161  O O   . TYR B 319 ? 0.4180 0.1699 0.4492 0.0057  -0.1259 -0.0259 311 TYR B O   
7162  C CB  . TYR B 319 ? 0.3588 0.1364 0.4278 -0.0137 -0.1041 -0.0096 311 TYR B CB  
7163  C CG  . TYR B 319 ? 0.3934 0.1721 0.4436 -0.0064 -0.0985 -0.0122 311 TYR B CG  
7164  C CD1 . TYR B 319 ? 0.3547 0.1375 0.3881 0.0018  -0.1007 -0.0209 311 TYR B CD1 
7165  C CD2 . TYR B 319 ? 0.3894 0.1728 0.4374 -0.0068 -0.0881 -0.0054 311 TYR B CD2 
7166  C CE1 . TYR B 319 ? 0.3970 0.1896 0.4145 0.0083  -0.0928 -0.0227 311 TYR B CE1 
7167  C CE2 . TYR B 319 ? 0.3960 0.1884 0.4268 0.0004  -0.0811 -0.0080 311 TYR B CE2 
7168  C CZ  . TYR B 319 ? 0.3843 0.1817 0.4012 0.0074  -0.0836 -0.0166 311 TYR B CZ  
7169  O OH  . TYR B 319 ? 0.3284 0.1357 0.3310 0.0141  -0.0768 -0.0191 311 TYR B OH  
7170  N N   . GLN B 320 ? 0.4527 0.2174 0.5028 -0.0009 -0.1297 -0.0277 312 GLN B N   
7171  C CA  . GLN B 320 ? 0.4728 0.2332 0.5041 0.0093  -0.1378 -0.0371 312 GLN B CA  
7172  C C   . GLN B 320 ? 0.4620 0.2098 0.4868 0.0139  -0.1487 -0.0402 312 GLN B C   
7173  O O   . GLN B 320 ? 0.4200 0.1622 0.4247 0.0238  -0.1527 -0.0463 312 GLN B O   
7174  C CB  . GLN B 320 ? 0.5161 0.2829 0.5514 0.0095  -0.1420 -0.0411 312 GLN B CB  
7175  C CG  . GLN B 320 ? 0.6043 0.3691 0.6179 0.0210  -0.1469 -0.0498 312 GLN B CG  
7176  C CD  . GLN B 320 ? 0.7551 0.5092 0.7602 0.0279  -0.1604 -0.0551 312 GLN B CD  
7177  O OE1 . GLN B 320 ? 0.8498 0.5985 0.8679 0.0232  -0.1676 -0.0530 312 GLN B OE1 
7178  N NE2 . GLN B 320 ? 0.7246 0.4760 0.7080 0.0394  -0.1636 -0.0618 312 GLN B NE2 
7179  N N   . ALA B 321 ? 0.4379 0.1814 0.4797 0.0069  -0.1532 -0.0359 313 ALA B N   
7180  C CA  . ALA B 321 ? 0.4885 0.2192 0.5260 0.0105  -0.1643 -0.0386 313 ALA B CA  
7181  C C   . ALA B 321 ? 0.5348 0.2571 0.5572 0.0153  -0.1615 -0.0381 313 ALA B C   
7182  O O   . ALA B 321 ? 0.6141 0.3272 0.6211 0.0236  -0.1700 -0.0437 313 ALA B O   
7183  C CB  . ALA B 321 ? 0.4727 0.2013 0.5341 0.0012  -0.1683 -0.0332 313 ALA B CB  
7184  N N   . LYS B 322 ? 0.4590 0.1843 0.4847 0.0111  -0.1499 -0.0313 314 LYS B N   
7185  C CA  . LYS B 322 ? 0.4337 0.1507 0.4455 0.0161  -0.1472 -0.0303 314 LYS B CA  
7186  C C   . LYS B 322 ? 0.5170 0.2388 0.5091 0.0248  -0.1415 -0.0347 314 LYS B C   
7187  O O   . LYS B 322 ? 0.5805 0.2958 0.5566 0.0324  -0.1421 -0.0369 314 LYS B O   
7188  C CB  . LYS B 322 ? 0.5346 0.2500 0.5598 0.0079  -0.1382 -0.0199 314 LYS B CB  
7189  N N   . TYR B 323 ? 0.4085 0.1418 0.4020 0.0243  -0.1360 -0.0360 315 TYR B N   
7190  C CA  . TYR B 323 ? 0.4503 0.1897 0.4282 0.0316  -0.1292 -0.0396 315 TYR B CA  
7191  C C   . TYR B 323 ? 0.4197 0.1668 0.3919 0.0358  -0.1311 -0.0461 315 TYR B C   
7192  O O   . TYR B 323 ? 0.3773 0.1342 0.3538 0.0332  -0.1239 -0.0453 315 TYR B O   
7193  C CB  . TYR B 323 ? 0.4483 0.1939 0.4343 0.0261  -0.1176 -0.0326 315 TYR B CB  
7194  C CG  . TYR B 323 ? 0.4579 0.1956 0.4486 0.0227  -0.1146 -0.0250 315 TYR B CG  
7195  C CD1 . TYR B 323 ? 0.4927 0.2250 0.4673 0.0305  -0.1135 -0.0262 315 TYR B CD1 
7196  C CD2 . TYR B 323 ? 0.4913 0.2289 0.5022 0.0120  -0.1120 -0.0163 315 TYR B CD2 
7197  C CE1 . TYR B 323 ? 0.4977 0.2210 0.4748 0.0283  -0.1108 -0.0190 315 TYR B CE1 
7198  C CE2 . TYR B 323 ? 0.5098 0.2398 0.5243 0.0094  -0.1082 -0.0085 315 TYR B CE2 
7199  C CZ  . TYR B 323 ? 0.5447 0.2664 0.5415 0.0177  -0.1079 -0.0098 315 TYR B CZ  
7200  O OH  . TYR B 323 ? 0.5854 0.2984 0.5840 0.0159  -0.1040 -0.0018 315 TYR B OH  
7201  N N   . PRO B 324 ? 0.4292 0.1716 0.3906 0.0430  -0.1407 -0.0525 316 PRO B N   
7202  C CA  . PRO B 324 ? 0.4492 0.1977 0.4055 0.0470  -0.1427 -0.0577 316 PRO B CA  
7203  C C   . PRO B 324 ? 0.4398 0.1973 0.3828 0.0539  -0.1340 -0.0610 316 PRO B C   
7204  O O   . PRO B 324 ? 0.4294 0.1947 0.3752 0.0525  -0.1303 -0.0618 316 PRO B O   
7205  C CB  . PRO B 324 ? 0.4735 0.2131 0.4187 0.0548  -0.1553 -0.0632 316 PRO B CB  
7206  C CG  . PRO B 324 ? 0.4411 0.1721 0.3781 0.0584  -0.1572 -0.0628 316 PRO B CG  
7207  C CD  . PRO B 324 ? 0.4769 0.2075 0.4301 0.0480  -0.1505 -0.0550 316 PRO B CD  
7208  N N   . ALA B 325 ? 0.4509 0.2081 0.3796 0.0617  -0.1307 -0.0630 317 ALA B N   
7209  C CA  . ALA B 325 ? 0.4217 0.1919 0.3401 0.0678  -0.1210 -0.0654 317 ALA B CA  
7210  C C   . ALA B 325 ? 0.4311 0.2194 0.3636 0.0580  -0.1081 -0.0587 317 ALA B C   
7211  O O   . ALA B 325 ? 0.4264 0.2290 0.3596 0.0576  -0.1008 -0.0588 317 ALA B O   
7212  C CB  . ALA B 325 ? 0.4987 0.2688 0.4014 0.0776  -0.1195 -0.0682 317 ALA B CB  
7213  N N   . GLU B 326 ? 0.3760 0.1634 0.3193 0.0507  -0.1051 -0.0525 318 GLU B N   
7214  C CA  . GLU B 326 ? 0.3459 0.1491 0.3018 0.0423  -0.0935 -0.0461 318 GLU B CA  
7215  C C   . GLU B 326 ? 0.3304 0.1375 0.2997 0.0346  -0.0935 -0.0442 318 GLU B C   
7216  O O   . GLU B 326 ? 0.3144 0.1370 0.2887 0.0311  -0.0844 -0.0421 318 GLU B O   
7217  C CB  . GLU B 326 ? 0.3620 0.1607 0.3254 0.0372  -0.0911 -0.0396 318 GLU B CB  
7218  C CG  . GLU B 326 ? 0.4008 0.1981 0.3511 0.0446  -0.0892 -0.0408 318 GLU B CG  
7219  C CD  . GLU B 326 ? 0.5560 0.3338 0.4960 0.0512  -0.1007 -0.0448 318 GLU B CD  
7220  O OE1 . GLU B 326 ? 0.5715 0.3362 0.5141 0.0503  -0.1108 -0.0472 318 GLU B OE1 
7221  O OE2 . GLU B 326 ? 0.5899 0.3649 0.5188 0.0578  -0.1002 -0.0460 318 GLU B OE2 
7222  N N   . ALA B 327 ? 0.3933 0.1862 0.3692 0.0320  -0.1041 -0.0451 319 ALA B N   
7223  C CA  . ALA B 327 ? 0.3686 0.1648 0.3583 0.0250  -0.1052 -0.0437 319 ALA B CA  
7224  C C   . ALA B 327 ? 0.3593 0.1637 0.3398 0.0302  -0.1037 -0.0487 319 ALA B C   
7225  O O   . ALA B 327 ? 0.3610 0.1770 0.3496 0.0252  -0.0974 -0.0463 319 ALA B O   
7226  C CB  . ALA B 327 ? 0.4099 0.1885 0.4091 0.0220  -0.1186 -0.0447 319 ALA B CB  
7227  N N   . ALA B 328 ? 0.3878 0.1857 0.3506 0.0409  -0.1090 -0.0555 320 ALA B N   
7228  C CA  . ALA B 328 ? 0.4135 0.2186 0.3658 0.0471  -0.1065 -0.0595 320 ALA B CA  
7229  C C   . ALA B 328 ? 0.3219 0.1465 0.2733 0.0461  -0.0920 -0.0565 320 ALA B C   
7230  O O   . ALA B 328 ? 0.3148 0.1491 0.2668 0.0453  -0.0866 -0.0563 320 ALA B O   
7231  C CB  . ALA B 328 ? 0.3580 0.1518 0.2905 0.0600  -0.1146 -0.0668 320 ALA B CB  
7232  N N   . GLU B 329 ? 0.3175 0.1476 0.2676 0.0464  -0.0860 -0.0543 321 GLU B N   
7233  C CA  . GLU B 329 ? 0.3390 0.1875 0.2903 0.0451  -0.0734 -0.0519 321 GLU B CA  
7234  C C   . GLU B 329 ? 0.3298 0.1878 0.2970 0.0346  -0.0670 -0.0463 321 GLU B C   
7235  O O   . GLU B 329 ? 0.2813 0.1529 0.2504 0.0330  -0.0586 -0.0453 321 GLU B O   
7236  C CB  . GLU B 329 ? 0.3473 0.1983 0.2939 0.0484  -0.0702 -0.0515 321 GLU B CB  
7237  C CG  . GLU B 329 ? 0.4036 0.2548 0.3341 0.0598  -0.0710 -0.0569 321 GLU B CG  
7238  C CD  . GLU B 329 ? 0.4050 0.2719 0.3330 0.0624  -0.0621 -0.0578 321 GLU B CD  
7239  O OE1 . GLU B 329 ? 0.3851 0.2667 0.3198 0.0589  -0.0529 -0.0553 321 GLU B OE1 
7240  O OE2 . GLU B 329 ? 0.3655 0.2296 0.2852 0.0679  -0.0643 -0.0608 321 GLU B OE2 
7241  N N   . PHE B 330 ? 0.3685 0.2195 0.3475 0.0275  -0.0705 -0.0423 322 PHE B N   
7242  C CA  . PHE B 330 ? 0.3060 0.1658 0.3001 0.0183  -0.0644 -0.0366 322 PHE B CA  
7243  C C   . PHE B 330 ? 0.2816 0.1447 0.2792 0.0164  -0.0652 -0.0379 322 PHE B C   
7244  O O   . PHE B 330 ? 0.2660 0.1415 0.2689 0.0126  -0.0572 -0.0355 322 PHE B O   
7245  C CB  . PHE B 330 ? 0.2836 0.1344 0.2900 0.0119  -0.0682 -0.0316 322 PHE B CB  
7246  C CG  . PHE B 330 ? 0.3070 0.1670 0.3287 0.0033  -0.0613 -0.0250 322 PHE B CG  
7247  C CD1 . PHE B 330 ? 0.2674 0.1387 0.2899 0.0020  -0.0513 -0.0211 322 PHE B CD1 
7248  C CD2 . PHE B 330 ? 0.3347 0.1922 0.3698 -0.0027 -0.0652 -0.0231 322 PHE B CD2 
7249  C CE1 . PHE B 330 ? 0.2953 0.1747 0.3303 -0.0046 -0.0449 -0.0152 322 PHE B CE1 
7250  C CE2 . PHE B 330 ? 0.3260 0.1927 0.3751 -0.0099 -0.0584 -0.0169 322 PHE B CE2 
7251  C CZ  . PHE B 330 ? 0.2697 0.1472 0.3180 -0.0106 -0.0481 -0.0128 322 PHE B CZ  
7252  N N   . VAL B 331 ? 0.2813 0.1325 0.2752 0.0196  -0.0753 -0.0422 323 VAL B N   
7253  C CA  . VAL B 331 ? 0.2797 0.1323 0.2749 0.0192  -0.0771 -0.0440 323 VAL B CA  
7254  C C   . VAL B 331 ? 0.2742 0.1370 0.2576 0.0247  -0.0694 -0.0462 323 VAL B C   
7255  O O   . VAL B 331 ? 0.2636 0.1360 0.2515 0.0212  -0.0633 -0.0442 323 VAL B O   
7256  C CB  . VAL B 331 ? 0.3089 0.1451 0.3011 0.0231  -0.0910 -0.0491 323 VAL B CB  
7257  C CG1 . VAL B 331 ? 0.3206 0.1574 0.3102 0.0252  -0.0934 -0.0520 323 VAL B CG1 
7258  C CG2 . VAL B 331 ? 0.3244 0.1516 0.3330 0.0158  -0.0982 -0.0461 323 VAL B CG2 
7259  N N   . ARG B 332 ? 0.2819 0.1430 0.2505 0.0334  -0.0693 -0.0498 324 ARG B N   
7260  C CA  . ARG B 332 ? 0.2886 0.1604 0.2476 0.0386  -0.0609 -0.0509 324 ARG B CA  
7261  C C   . ARG B 332 ? 0.2990 0.1869 0.2676 0.0319  -0.0494 -0.0464 324 ARG B C   
7262  O O   . ARG B 332 ? 0.2521 0.1481 0.2216 0.0306  -0.0434 -0.0454 324 ARG B O   
7263  C CB  . ARG B 332 ? 0.3438 0.2137 0.2885 0.0483  -0.0612 -0.0544 324 ARG B CB  
7264  C CG  . ARG B 332 ? 0.3378 0.2201 0.2749 0.0534  -0.0514 -0.0548 324 ARG B CG  
7265  C CD  . ARG B 332 ? 0.3224 0.2049 0.2470 0.0631  -0.0508 -0.0578 324 ARG B CD  
7266  N NE  . ARG B 332 ? 0.3707 0.2597 0.3011 0.0605  -0.0474 -0.0564 324 ARG B NE  
7267  C CZ  . ARG B 332 ? 0.2977 0.2024 0.2354 0.0570  -0.0376 -0.0540 324 ARG B CZ  
7268  N NH1 . ARG B 332 ? 0.2762 0.1916 0.2177 0.0546  -0.0298 -0.0522 324 ARG B NH1 
7269  N NH2 . ARG B 332 ? 0.3068 0.2157 0.2481 0.0559  -0.0361 -0.0535 324 ARG B NH2 
7270  N N   . ARG B 333 ? 0.2717 0.1635 0.2469 0.0281  -0.0465 -0.0437 325 ARG B N   
7271  C CA  . ARG B 333 ? 0.2380 0.1444 0.2204 0.0234  -0.0365 -0.0405 325 ARG B CA  
7272  C C   . ARG B 333 ? 0.2814 0.1916 0.2765 0.0150  -0.0343 -0.0364 325 ARG B C   
7273  O O   . ARG B 333 ? 0.2549 0.1763 0.2540 0.0121  -0.0268 -0.0348 325 ARG B O   
7274  C CB  . ARG B 333 ? 0.2367 0.1453 0.2199 0.0238  -0.0347 -0.0394 325 ARG B CB  
7275  C CG  . ARG B 333 ? 0.2440 0.1532 0.2153 0.0326  -0.0348 -0.0435 325 ARG B CG  
7276  C CD  . ARG B 333 ? 0.2475 0.1537 0.2177 0.0341  -0.0363 -0.0431 325 ARG B CD  
7277  N NE  . ARG B 333 ? 0.2361 0.1511 0.2156 0.0285  -0.0303 -0.0393 325 ARG B NE  
7278  C CZ  . ARG B 333 ? 0.2527 0.1673 0.2314 0.0298  -0.0298 -0.0383 325 ARG B CZ  
7279  N NH1 . ARG B 333 ? 0.2701 0.1761 0.2398 0.0360  -0.0349 -0.0408 325 ARG B NH1 
7280  N NH2 . ARG B 333 ? 0.2285 0.1507 0.2143 0.0257  -0.0245 -0.0350 325 ARG B NH2 
7281  N N   . MET B 334 ? 0.2500 0.1511 0.2523 0.0110  -0.0408 -0.0348 326 MET B N   
7282  C CA  . MET B 334 ? 0.2237 0.1290 0.2385 0.0037  -0.0389 -0.0310 326 MET B CA  
7283  C C   . MET B 334 ? 0.2682 0.1747 0.2803 0.0047  -0.0391 -0.0331 326 MET B C   
7284  O O   . MET B 334 ? 0.2626 0.1770 0.2815 0.0002  -0.0340 -0.0306 326 MET B O   
7285  C CB  . MET B 334 ? 0.2292 0.1252 0.2546 -0.0009 -0.0457 -0.0284 326 MET B CB  
7286  C CG  . MET B 334 ? 0.2666 0.1628 0.2987 -0.0042 -0.0430 -0.0236 326 MET B CG  
7287  S SD  . MET B 334 ? 0.2442 0.1556 0.2800 -0.0071 -0.0310 -0.0192 326 MET B SD  
7288  C CE  . MET B 334 ? 0.2223 0.1403 0.2706 -0.0135 -0.0284 -0.0159 326 MET B CE  
7289  N N   . ASP B 335 ? 0.2644 0.1625 0.2655 0.0112  -0.0451 -0.0376 327 ASP B N   
7290  C CA  . ASP B 335 ? 0.2947 0.1928 0.2898 0.0141  -0.0449 -0.0397 327 ASP B CA  
7291  C C   . ASP B 335 ? 0.3495 0.2579 0.3371 0.0172  -0.0352 -0.0396 327 ASP B C   
7292  O O   . ASP B 335 ? 0.3626 0.2709 0.3436 0.0204  -0.0337 -0.0407 327 ASP B O   
7293  C CB  . ASP B 335 ? 0.3321 0.2164 0.3167 0.0214  -0.0553 -0.0447 327 ASP B CB  
7294  C CG  . ASP B 335 ? 0.3182 0.1922 0.3129 0.0177  -0.0661 -0.0452 327 ASP B CG  
7295  O OD1 . ASP B 335 ? 0.3078 0.1866 0.3180 0.0094  -0.0644 -0.0411 327 ASP B OD1 
7296  O OD2 . ASP B 335 ? 0.3560 0.2171 0.3436 0.0234  -0.0764 -0.0497 327 ASP B OD2 
7297  N N   . LYS B 336 ? 0.3014 0.2181 0.2903 0.0166  -0.0290 -0.0384 328 LYS B N   
7298  C CA  . LYS B 336 ? 0.3600 0.2879 0.3458 0.0182  -0.0197 -0.0380 328 LYS B CA  
7299  C C   . LYS B 336 ? 0.3981 0.3229 0.3700 0.0270  -0.0194 -0.0409 328 LYS B C   
7300  O O   . LYS B 336 ? 0.4377 0.3673 0.4066 0.0283  -0.0135 -0.0401 328 LYS B O   
7301  C CB  . LYS B 336 ? 0.3548 0.2908 0.3489 0.0120  -0.0136 -0.0351 328 LYS B CB  
7302  C CG  . LYS B 336 ? 0.3589 0.2985 0.3657 0.0045  -0.0132 -0.0319 328 LYS B CG  
7303  C CD  . LYS B 336 ? 0.2889 0.2339 0.3028 -0.0007 -0.0092 -0.0294 328 LYS B CD  
7304  C CE  . LYS B 336 ? 0.3196 0.2685 0.3449 -0.0068 -0.0082 -0.0260 328 LYS B CE  
7305  N NZ  . LYS B 336 ? 0.3817 0.3363 0.4133 -0.0111 -0.0043 -0.0239 328 LYS B NZ  
7306  N N   . LYS B 337 ? 0.3450 0.2612 0.3076 0.0337  -0.0256 -0.0441 329 LYS B N   
7307  C CA  . LYS B 337 ? 0.2870 0.1996 0.2346 0.0438  -0.0256 -0.0469 329 LYS B CA  
7308  C C   . LYS B 337 ? 0.3325 0.2502 0.2759 0.0489  -0.0227 -0.0482 329 LYS B C   
7309  O O   . LYS B 337 ? 0.3258 0.2425 0.2737 0.0468  -0.0258 -0.0486 329 LYS B O   
7310  C CB  . LYS B 337 ? 0.3494 0.2457 0.2872 0.0497  -0.0371 -0.0506 329 LYS B CB  
7311  C CG  . LYS B 337 ? 0.3372 0.2281 0.2819 0.0442  -0.0420 -0.0498 329 LYS B CG  
7312  C CD  . LYS B 337 ? 0.4760 0.3506 0.4167 0.0477  -0.0558 -0.0539 329 LYS B CD  
7313  C CE  . LYS B 337 ? 0.4890 0.3541 0.4147 0.0570  -0.0606 -0.0576 329 LYS B CE  
7314  N NZ  . LYS B 337 ? 0.4816 0.3305 0.4057 0.0598  -0.0757 -0.0622 329 LYS B NZ  
7315  N N   . LEU B 338 ? 0.3094 0.2326 0.2443 0.0560  -0.0165 -0.0486 330 LEU B N   
7316  C CA  . LEU B 338 ? 0.3805 0.3095 0.3114 0.0619  -0.0136 -0.0502 330 LEU B CA  
7317  C C   . LEU B 338 ? 0.3937 0.3094 0.3097 0.0719  -0.0226 -0.0544 330 LEU B C   
7318  O O   . LEU B 338 ? 0.3825 0.2850 0.2901 0.0754  -0.0304 -0.0564 330 LEU B O   
7319  C CB  . LEU B 338 ? 0.3780 0.3196 0.3078 0.0654  -0.0025 -0.0482 330 LEU B CB  
7320  C CG  . LEU B 338 ? 0.3775 0.3334 0.3228 0.0563  0.0066  -0.0446 330 LEU B CG  
7321  C CD1 . LEU B 338 ? 0.4638 0.4310 0.4088 0.0601  0.0172  -0.0425 330 LEU B CD1 
7322  C CD2 . LEU B 338 ? 0.3979 0.3609 0.3548 0.0505  0.0061  -0.0450 330 LEU B CD2 
7323  N N   . PRO B 339 ? 0.4213 0.3398 0.3337 0.0772  -0.0226 -0.0564 331 PRO B N   
7324  C CA  . PRO B 339 ? 0.4159 0.3215 0.3124 0.0882  -0.0309 -0.0608 331 PRO B CA  
7325  C C   . PRO B 339 ? 0.4726 0.3757 0.3543 0.0986  -0.0286 -0.0617 331 PRO B C   
7326  O O   . PRO B 339 ? 0.4083 0.3232 0.2918 0.0989  -0.0179 -0.0586 331 PRO B O   
7327  C CB  . PRO B 339 ? 0.4220 0.3352 0.3187 0.0919  -0.0284 -0.0620 331 PRO B CB  
7328  C CG  . PRO B 339 ? 0.3875 0.3124 0.3013 0.0810  -0.0231 -0.0590 331 PRO B CG  
7329  C CD  . PRO B 339 ? 0.3734 0.3055 0.2957 0.0739  -0.0164 -0.0553 331 PRO B CD  
7330  N N   . GLU B 340 ? 0.4597 0.3462 0.3263 0.1075  -0.0391 -0.0659 332 GLU B N   
7331  C CA  . GLU B 340 ? 0.4737 0.3548 0.3232 0.1190  -0.0386 -0.0672 332 GLU B CA  
7332  C C   . GLU B 340 ? 0.4297 0.3229 0.2718 0.1283  -0.0277 -0.0660 332 GLU B C   
7333  O O   . GLU B 340 ? 0.5126 0.4101 0.3475 0.1339  -0.0198 -0.0635 332 GLU B O   
7334  C CB  . GLU B 340 ? 0.4991 0.3593 0.3333 0.1280  -0.0535 -0.0731 332 GLU B CB  
7335  N N   . ASN B 341 ? 0.4412 0.3406 0.2854 0.1303  -0.0268 -0.0673 333 ASN B N   
7336  C CA  . ASN B 341 ? 0.4950 0.4064 0.3331 0.1400  -0.0173 -0.0664 333 ASN B CA  
7337  C C   . ASN B 341 ? 0.4301 0.3634 0.2865 0.1317  -0.0034 -0.0613 333 ASN B C   
7338  O O   . ASN B 341 ? 0.4503 0.3965 0.3077 0.1373  0.0043  -0.0607 333 ASN B O   
7339  C CB  . ASN B 341 ? 0.5741 0.4814 0.4046 0.1480  -0.0237 -0.0710 333 ASN B CB  
7340  C CG  . ASN B 341 ? 0.6606 0.5747 0.5073 0.1379  -0.0246 -0.0708 333 ASN B CG  
7341  O OD1 . ASN B 341 ? 0.6231 0.5367 0.4833 0.1253  -0.0262 -0.0689 333 ASN B OD1 
7342  N ND2 . ASN B 341 ? 0.6501 0.5707 0.4948 0.1441  -0.0233 -0.0729 333 ASN B ND2 
7343  N N   . PHE B 342 ? 0.3642 0.2761 0.2529 0.0096  0.0260  -0.0843 334 PHE B N   
7344  C CA  . PHE B 342 ? 0.2982 0.2229 0.2005 0.0113  0.0312  -0.0775 334 PHE B CA  
7345  C C   . PHE B 342 ? 0.3290 0.2613 0.2227 0.0107  0.0428  -0.0806 334 PHE B C   
7346  O O   . PHE B 342 ? 0.3822 0.3244 0.2897 0.0145  0.0503  -0.0825 334 PHE B O   
7347  C CB  . PHE B 342 ? 0.3103 0.2385 0.2158 0.0074  0.0244  -0.0656 334 PHE B CB  
7348  C CG  . PHE B 342 ? 0.2978 0.2379 0.2177 0.0090  0.0288  -0.0592 334 PHE B CG  
7349  C CD1 . PHE B 342 ? 0.3038 0.2473 0.2430 0.0135  0.0272  -0.0574 334 PHE B CD1 
7350  C CD2 . PHE B 342 ? 0.3225 0.2693 0.2356 0.0060  0.0343  -0.0551 334 PHE B CD2 
7351  C CE1 . PHE B 342 ? 0.2877 0.2423 0.2395 0.0150  0.0304  -0.0523 334 PHE B CE1 
7352  C CE2 . PHE B 342 ? 0.3366 0.2939 0.2635 0.0070  0.0380  -0.0500 334 PHE B CE2 
7353  C CZ  . PHE B 342 ? 0.2562 0.2180 0.2025 0.0116  0.0358  -0.0491 334 PHE B CZ  
7354  N N   . ASP B 343 ? 0.3714 0.2996 0.2426 0.0058  0.0442  -0.0809 335 ASP B N   
7355  C CA  . ASP B 343 ? 0.4236 0.3579 0.2845 0.0038  0.0560  -0.0826 335 ASP B CA  
7356  C C   . ASP B 343 ? 0.4292 0.3662 0.2930 0.0082  0.0664  -0.0950 335 ASP B C   
7357  O O   . ASP B 343 ? 0.3728 0.3209 0.2443 0.0090  0.0773  -0.0969 335 ASP B O   
7358  C CB  . ASP B 343 ? 0.5555 0.4819 0.3882 -0.0020 0.0546  -0.0803 335 ASP B CB  
7359  C CG  . ASP B 343 ? 0.6654 0.5913 0.4960 -0.0056 0.0460  -0.0679 335 ASP B CG  
7360  O OD1 . ASP B 343 ? 0.6106 0.5449 0.4571 -0.0053 0.0474  -0.0608 335 ASP B OD1 
7361  O OD2 . ASP B 343 ? 0.7257 0.6429 0.5392 -0.0085 0.0375  -0.0657 335 ASP B OD2 
7362  N N   . GLU B 344 ? 0.4079 0.3351 0.2665 0.0109  0.0632  -0.1040 336 GLU B N   
7363  C CA  . GLU B 344 ? 0.4355 0.3644 0.2976 0.0161  0.0728  -0.1169 336 GLU B CA  
7364  C C   . GLU B 344 ? 0.4127 0.3512 0.3037 0.0233  0.0746  -0.1180 336 GLU B C   
7365  O O   . GLU B 344 ? 0.4426 0.3914 0.3428 0.0271  0.0854  -0.1251 336 GLU B O   
7366  C CB  . GLU B 344 ? 0.4565 0.3706 0.3059 0.0174  0.0679  -0.1265 336 GLU B CB  
7367  N N   . TYR B 345 ? 0.3817 0.3174 0.2874 0.0254  0.0642  -0.1112 337 TYR B N   
7368  C CA  . TYR B 345 ? 0.3912 0.3352 0.3225 0.0323  0.0643  -0.1105 337 TYR B CA  
7369  C C   . TYR B 345 ? 0.2957 0.2572 0.2375 0.0314  0.0720  -0.1065 337 TYR B C   
7370  O O   . TYR B 345 ? 0.3372 0.3098 0.2953 0.0371  0.0787  -0.1124 337 TYR B O   
7371  C CB  . TYR B 345 ? 0.3756 0.3128 0.3166 0.0330  0.0520  -0.1019 337 TYR B CB  
7372  C CG  . TYR B 345 ? 0.3106 0.2557 0.2751 0.0397  0.0509  -0.0991 337 TYR B CG  
7373  C CD1 . TYR B 345 ? 0.3544 0.2947 0.3307 0.0483  0.0500  -0.1062 337 TYR B CD1 
7374  C CD2 . TYR B 345 ? 0.2604 0.2170 0.2346 0.0380  0.0502  -0.0898 337 TYR B CD2 
7375  C CE1 . TYR B 345 ? 0.3067 0.2536 0.3031 0.0552  0.0478  -0.1033 337 TYR B CE1 
7376  C CE2 . TYR B 345 ? 0.3017 0.2656 0.2958 0.0444  0.0482  -0.0876 337 TYR B CE2 
7377  C CZ  . TYR B 345 ? 0.3064 0.2656 0.3113 0.0531  0.0467  -0.0941 337 TYR B CZ  
7378  O OH  . TYR B 345 ? 0.2572 0.2229 0.2804 0.0601  0.0437  -0.0915 337 TYR B OH  
7379  N N   . VAL B 346 ? 0.2961 0.2603 0.2297 0.0243  0.0709  -0.0968 338 VAL B N   
7380  C CA  . VAL B 346 ? 0.2928 0.2718 0.2357 0.0222  0.0780  -0.0927 338 VAL B CA  
7381  C C   . VAL B 346 ? 0.3575 0.3446 0.2956 0.0212  0.0921  -0.1016 338 VAL B C   
7382  O O   . VAL B 346 ? 0.2825 0.2844 0.2383 0.0239  0.0996  -0.1053 338 VAL B O   
7383  C CB  . VAL B 346 ? 0.2736 0.2507 0.2062 0.0149  0.0738  -0.0809 338 VAL B CB  
7384  C CG1 . VAL B 346 ? 0.2612 0.2514 0.1995 0.0112  0.0828  -0.0779 338 VAL B CG1 
7385  C CG2 . VAL B 346 ? 0.3078 0.2812 0.2504 0.0164  0.0616  -0.0726 338 VAL B CG2 
7386  N N   . GLN B 347 ? 0.3473 0.3251 0.2614 0.0174  0.0959  -0.1057 339 GLN B N   
7387  C CA  . GLN B 347 ? 0.3536 0.3382 0.2603 0.0156  0.1096  -0.1130 339 GLN B CA  
7388  C C   . GLN B 347 ? 0.3684 0.3623 0.2957 0.0243  0.1124  -0.1214 339 GLN B C   
7389  O O   . GLN B 347 ? 0.3443 0.3529 0.2844 0.0248  0.1199  -0.1218 339 GLN B O   
7390  C CB  . GLN B 347 ? 0.3651 0.3363 0.2415 0.0113  0.1098  -0.1149 339 GLN B CB  
7391  N N   . THR B 348 ? 0.3626 0.3471 0.2936 0.0311  0.1061  -0.1277 340 THR B N   
7392  C CA  . THR B 348 ? 0.4079 0.3986 0.3573 0.0404  0.1076  -0.1348 340 THR B CA  
7393  C C   . THR B 348 ? 0.3145 0.3206 0.2918 0.0446  0.1066  -0.1312 340 THR B C   
7394  O O   . THR B 348 ? 0.3808 0.4008 0.3723 0.0477  0.1125  -0.1339 340 THR B O   
7395  C CB  . THR B 348 ? 0.4016 0.3760 0.3486 0.0464  0.0997  -0.1407 340 THR B CB  
7396  O OG1 . THR B 348 ? 0.4452 0.4065 0.3662 0.0423  0.1004  -0.1452 340 THR B OG1 
7397  C CG2 . THR B 348 ? 0.4324 0.4110 0.3978 0.0566  0.1006  -0.1470 340 THR B CG2 
7398  N N   . ALA B 349 ? 0.2955 0.2997 0.2809 0.0447  0.0988  -0.1251 341 ALA B N   
7399  C CA  . ALA B 349 ? 0.3143 0.3323 0.3244 0.0488  0.0962  -0.1211 341 ALA B CA  
7400  C C   . ALA B 349 ? 0.3738 0.4088 0.3893 0.0430  0.1043  -0.1179 341 ALA B C   
7401  O O   . ALA B 349 ? 0.3564 0.4060 0.3923 0.0468  0.1053  -0.1185 341 ALA B O   
7402  C CB  . ALA B 349 ? 0.3334 0.3452 0.3471 0.0485  0.0863  -0.1137 341 ALA B CB  
7403  N N   . LEU B 350 ? 0.3307 0.3630 0.3275 0.0334  0.1097  -0.1142 342 LEU B N   
7404  C CA  . LEU B 350 ? 0.3354 0.3809 0.3354 0.0267  0.1174  -0.1104 342 LEU B CA  
7405  C C   . LEU B 350 ? 0.3698 0.4254 0.3758 0.0285  0.1260  -0.1171 342 LEU B C   
7406  O O   . LEU B 350 ? 0.3322 0.4034 0.3564 0.0282  0.1295  -0.1170 342 LEU B O   
7407  C CB  . LEU B 350 ? 0.3466 0.3830 0.3220 0.0166  0.1206  -0.1041 342 LEU B CB  
7408  C CG  . LEU B 350 ? 0.3456 0.3916 0.3218 0.0085  0.1280  -0.0986 342 LEU B CG  
7409  C CD1 . LEU B 350 ? 0.2674 0.3248 0.2659 0.0089  0.1241  -0.0943 342 LEU B CD1 
7410  C CD2 . LEU B 350 ? 0.3731 0.4061 0.3216 -0.0004 0.1297  -0.0917 342 LEU B CD2 
7411  N N   . LYS B 351 ? 0.3089 0.3558 0.2996 0.0301  0.1295  -0.1233 343 LYS B N   
7412  C CA  . LYS B 351 ? 0.3247 0.3807 0.3211 0.0327  0.1380  -0.1306 343 LYS B CA  
7413  C C   . LYS B 351 ? 0.3724 0.4403 0.3970 0.0420  0.1350  -0.1349 343 LYS B C   
7414  O O   . LYS B 351 ? 0.3599 0.4434 0.3994 0.0421  0.1414  -0.1377 343 LYS B O   
7415  C CB  . LYS B 351 ? 0.3485 0.3913 0.3241 0.0346  0.1403  -0.1374 343 LYS B CB  
7416  N N   . GLU B 352 ? 0.3825 0.4429 0.4147 0.0496  0.1247  -0.1350 344 GLU B N   
7417  C CA  . GLU B 352 ? 0.3879 0.4570 0.4447 0.0592  0.1201  -0.1379 344 GLU B CA  
7418  C C   . GLU B 352 ? 0.3867 0.4725 0.4634 0.0572  0.1184  -0.1327 344 GLU B C   
7419  O O   . GLU B 352 ? 0.4308 0.5311 0.5270 0.0614  0.1199  -0.1362 344 GLU B O   
7420  C CB  . GLU B 352 ? 0.4758 0.5298 0.5330 0.0671  0.1092  -0.1378 344 GLU B CB  
7421  C CG  . GLU B 352 ? 0.5829 0.6202 0.6243 0.0706  0.1098  -0.1447 344 GLU B CG  
7422  C CD  . GLU B 352 ? 0.6367 0.6561 0.6762 0.0760  0.0986  -0.1434 344 GLU B CD  
7423  O OE1 . GLU B 352 ? 0.6080 0.6281 0.6573 0.0769  0.0907  -0.1366 344 GLU B OE1 
7424  O OE2 . GLU B 352 ? 0.6617 0.6658 0.6896 0.0789  0.0977  -0.1491 344 GLU B OE2 
7425  N N   . VAL B 353 ? 0.3849 0.4687 0.4569 0.0510  0.1147  -0.1247 345 VAL B N   
7426  C CA  . VAL B 353 ? 0.3604 0.4589 0.4490 0.0480  0.1131  -0.1200 345 VAL B CA  
7427  C C   . VAL B 353 ? 0.4070 0.5204 0.5017 0.0422  0.1237  -0.1229 345 VAL B C   
7428  O O   . VAL B 353 ? 0.4259 0.5549 0.5416 0.0443  0.1233  -0.1248 345 VAL B O   
7429  C CB  . VAL B 353 ? 0.3746 0.4669 0.4535 0.0410  0.1094  -0.1113 345 VAL B CB  
7430  C CG1 . VAL B 353 ? 0.3717 0.4782 0.4630 0.0351  0.1108  -0.1071 345 VAL B CG1 
7431  C CG2 . VAL B 353 ? 0.4505 0.5326 0.5312 0.0475  0.0981  -0.1083 345 VAL B CG2 
7432  N N   . CYS B 354 ? 0.4751 0.5836 0.5510 0.0347  0.1330  -0.1232 346 CYS B N   
7433  C CA  A CYS B 354 ? 0.5551 0.6758 0.6345 0.0283  0.1439  -0.1256 346 CYS B CA  
7434  C CA  B CYS B 354 ? 0.5526 0.6738 0.6328 0.0284  0.1437  -0.1255 346 CYS B CA  
7435  C C   . CYS B 354 ? 0.6108 0.7430 0.7060 0.0354  0.1480  -0.1349 346 CYS B C   
7436  O O   . CYS B 354 ? 0.7125 0.8604 0.8221 0.0324  0.1544  -0.1376 346 CYS B O   
7437  C CB  A CYS B 354 ? 0.5777 0.6877 0.6300 0.0195  0.1523  -0.1234 346 CYS B CB  
7438  C CB  B CYS B 354 ? 0.5756 0.6866 0.6295 0.0192  0.1521  -0.1230 346 CYS B CB  
7439  S SG  A CYS B 354 ? 0.6315 0.7529 0.6832 0.0093  0.1666  -0.1242 346 CYS B SG  
7440  S SG  B CYS B 354 ? 0.5373 0.6353 0.5748 0.0120  0.1462  -0.1120 346 CYS B SG  
7441  N N   . ALA B 355 ? 0.6202 0.7441 0.7130 0.0448  0.1446  -0.1401 347 ALA B N   
7442  C CA  . ALA B 355 ? 0.6538 0.7875 0.7627 0.0531  0.1475  -0.1490 347 ALA B CA  
7443  C C   . ALA B 355 ? 0.6691 0.8179 0.8059 0.0584  0.1407  -0.1490 347 ALA B C   
7444  O O   . ALA B 355 ? 0.7100 0.8760 0.8643 0.0586  0.1461  -0.1539 347 ALA B O   
7445  C CB  . ALA B 355 ? 0.6719 0.7905 0.7713 0.0621  0.1439  -0.1539 347 ALA B CB  
7446  N N   . LYS B 356 ? 0.5991 0.7419 0.7401 0.0627  0.1287  -0.1437 348 LYS B N   
7447  C CA  . LYS B 356 ? 0.5990 0.7543 0.7634 0.0676  0.1206  -0.1426 348 LYS B CA  
7448  C C   . LYS B 356 ? 0.6387 0.8037 0.8079 0.0581  0.1205  -0.1367 348 LYS B C   
7449  O O   . LYS B 356 ? 0.7180 0.8995 0.9011 0.0540  0.1259  -0.1396 348 LYS B O   
7450  C CB  . LYS B 356 ? 0.5855 0.7287 0.7508 0.0769  0.1075  -0.1392 348 LYS B CB  
7451  N N   . GLN B 367 ? 0.7876 0.9227 0.9409 0.0445  0.0635  -0.0834 359 GLN B N   
7452  C CA  . GLN B 367 ? 0.7819 0.9087 0.9339 0.0542  0.0594  -0.0855 359 GLN B CA  
7453  C C   . GLN B 367 ? 0.6786 0.7921 0.8225 0.0581  0.0509  -0.0794 359 GLN B C   
7454  O O   . GLN B 367 ? 0.7605 0.8756 0.9062 0.0571  0.0450  -0.0742 359 GLN B O   
7455  C CB  . GLN B 367 ? 0.8570 0.9772 0.9986 0.0527  0.0685  -0.0901 359 GLN B CB  
7456  N N   . ASN B 368 ? 0.5250 0.6248 0.6598 0.0626  0.0503  -0.0803 360 ASN B N   
7457  C CA  . ASN B 368 ? 0.4092 0.4944 0.5350 0.0650  0.0436  -0.0748 360 ASN B CA  
7458  C C   . ASN B 368 ? 0.2793 0.3514 0.3880 0.0599  0.0492  -0.0753 360 ASN B C   
7459  O O   . ASN B 368 ? 0.2220 0.2814 0.3241 0.0641  0.0476  -0.0775 360 ASN B O   
7460  C CB  . ASN B 368 ? 0.4481 0.5251 0.5777 0.0753  0.0337  -0.0733 360 ASN B CB  
7461  C CG  . ASN B 368 ? 0.4830 0.5520 0.6088 0.0771  0.0244  -0.0650 360 ASN B CG  
7462  O OD1 . ASN B 368 ? 0.3127 0.3754 0.4261 0.0690  0.0250  -0.0583 360 ASN B OD1 
7463  N ND2 . ASN B 368 ? 0.5617 0.6277 0.6918 0.0846  0.0155  -0.0617 360 ASN B ND2 
7464  N N   . SER B 369 ? 0.2544 0.3270 0.3529 0.0498  0.0545  -0.0715 361 SER B N   
7465  C CA  . SER B 369 ? 0.2086 0.2657 0.2859 0.0436  0.0560  -0.0675 361 SER B CA  
7466  C C   . SER B 369 ? 0.1567 0.1981 0.2255 0.0455  0.0459  -0.0599 361 SER B C   
7467  O O   . SER B 369 ? 0.1736 0.2013 0.2295 0.0445  0.0448  -0.0596 361 SER B O   
7468  C CB  . SER B 369 ? 0.2320 0.2915 0.3005 0.0335  0.0613  -0.0629 361 SER B CB  
7469  O OG  . SER B 369 ? 0.2661 0.3409 0.3443 0.0306  0.0709  -0.0690 361 SER B OG  
7470  N N   . ILE B 370 ? 0.1622 0.2056 0.2376 0.0476  0.0387  -0.0537 362 ILE B N   
7471  C CA  . ILE B 370 ? 0.1630 0.1923 0.2307 0.0485  0.0302  -0.0460 362 ILE B CA  
7472  C C   . ILE B 370 ? 0.1573 0.1757 0.2252 0.0555  0.0267  -0.0493 362 ILE B C   
7473  O O   . ILE B 370 ? 0.1927 0.1963 0.2496 0.0535  0.0238  -0.0464 362 ILE B O   
7474  C CB  . ILE B 370 ? 0.1479 0.1821 0.2224 0.0501  0.0241  -0.0398 362 ILE B CB  
7475  C CG1 . ILE B 370 ? 0.1523 0.1957 0.2264 0.0430  0.0276  -0.0370 362 ILE B CG1 
7476  C CG2 . ILE B 370 ? 0.1947 0.2145 0.2610 0.0505  0.0167  -0.0317 362 ILE B CG2 
7477  C CD1 . ILE B 370 ? 0.1453 0.1945 0.2258 0.0446  0.0220  -0.0324 362 ILE B CD1 
7478  N N   . GLU B 371 ? 0.1939 0.2192 0.2752 0.0639  0.0267  -0.0559 363 GLU B N   
7479  C CA  . GLU B 371 ? 0.2699 0.2835 0.3520 0.0716  0.0234  -0.0596 363 GLU B CA  
7480  C C   . GLU B 371 ? 0.2505 0.2549 0.3218 0.0686  0.0287  -0.0655 363 GLU B C   
7481  O O   . GLU B 371 ? 0.2496 0.2372 0.3130 0.0697  0.0248  -0.0648 363 GLU B O   
7482  C CB  . GLU B 371 ? 0.2963 0.3211 0.3963 0.0819  0.0228  -0.0667 363 GLU B CB  
7483  C CG  . GLU B 371 ? 0.3692 0.3800 0.4713 0.0917  0.0170  -0.0687 363 GLU B CG  
7484  C CD  . GLU B 371 ? 0.4619 0.4681 0.5676 0.0977  0.0069  -0.0609 363 GLU B CD  
7485  O OE1 . GLU B 371 ? 0.4572 0.4782 0.5712 0.0982  0.0051  -0.0586 363 GLU B OE1 
7486  O OE2 . GLU B 371 ? 0.4827 0.4694 0.5800 0.0998  0.0011  -0.0558 363 GLU B OE2 
7487  N N   . ILE B 372 ? 0.2052 0.2199 0.2752 0.0643  0.0378  -0.0715 364 ILE B N   
7488  C CA  . ILE B 372 ? 0.2232 0.2294 0.2799 0.0609  0.0433  -0.0772 364 ILE B CA  
7489  C C   . ILE B 372 ? 0.2529 0.2446 0.2922 0.0534  0.0388  -0.0698 364 ILE B C   
7490  O O   . ILE B 372 ? 0.2920 0.2696 0.3215 0.0532  0.0369  -0.0724 364 ILE B O   
7491  C CB  . ILE B 372 ? 0.2667 0.2866 0.3228 0.0564  0.0545  -0.0833 364 ILE B CB  
7492  C CG1 . ILE B 372 ? 0.2852 0.3208 0.3607 0.0639  0.0597  -0.0927 364 ILE B CG1 
7493  C CG2 . ILE B 372 ? 0.3110 0.3209 0.3485 0.0515  0.0597  -0.0877 364 ILE B CG2 
7494  C CD1 . ILE B 372 ? 0.2672 0.3188 0.3450 0.0582  0.0714  -0.0973 364 ILE B CD1 
7495  N N   . LEU B 373 ? 0.2132 0.2088 0.2495 0.0473  0.0370  -0.0612 365 LEU B N   
7496  C CA  . LEU B 373 ? 0.2458 0.2305 0.2681 0.0405  0.0327  -0.0542 365 LEU B CA  
7497  C C   . LEU B 373 ? 0.2367 0.2082 0.2595 0.0429  0.0242  -0.0500 365 LEU B C   
7498  O O   . LEU B 373 ? 0.2770 0.2364 0.2896 0.0394  0.0212  -0.0497 365 LEU B O   
7499  C CB  . LEU B 373 ? 0.2969 0.2895 0.3186 0.0348  0.0327  -0.0463 365 LEU B CB  
7500  C CG  . LEU B 373 ? 0.3921 0.3806 0.3986 0.0268  0.0335  -0.0425 365 LEU B CG  
7501  C CD1 . LEU B 373 ? 0.4817 0.4726 0.4792 0.0242  0.0419  -0.0490 365 LEU B CD1 
7502  C CD2 . LEU B 373 ? 0.4209 0.4159 0.4300 0.0232  0.0324  -0.0345 365 LEU B CD2 
7503  N N   . ALA B 374 ? 0.2025 0.1759 0.2367 0.0485  0.0201  -0.0467 366 ALA B N   
7504  C CA  . ALA B 374 ? 0.1881 0.1483 0.2218 0.0501  0.0128  -0.0412 366 ALA B CA  
7505  C C   . ALA B 374 ? 0.2557 0.2007 0.2858 0.0531  0.0114  -0.0472 366 ALA B C   
7506  O O   . ALA B 374 ? 0.2919 0.2231 0.3164 0.0501  0.0067  -0.0436 366 ALA B O   
7507  C CB  . ALA B 374 ? 0.1988 0.1635 0.2433 0.0564  0.0090  -0.0370 366 ALA B CB  
7508  N N   . LYS B 375 ? 0.2660 0.2134 0.3001 0.0590  0.0157  -0.0570 367 LYS B N   
7509  C CA  . LYS B 375 ? 0.2992 0.2316 0.3294 0.0621  0.0150  -0.0641 367 LYS B CA  
7510  C C   . LYS B 375 ? 0.3248 0.2474 0.3401 0.0536  0.0147  -0.0650 367 LYS B C   
7511  O O   . LYS B 375 ? 0.3145 0.2207 0.3252 0.0530  0.0106  -0.0664 367 LYS B O   
7512  C CB  . LYS B 375 ? 0.3629 0.3025 0.3994 0.0691  0.0215  -0.0757 367 LYS B CB  
7513  C CG  . LYS B 375 ? 0.3971 0.3458 0.4504 0.0792  0.0206  -0.0768 367 LYS B CG  
7514  C CD  . LYS B 375 ? 0.4615 0.4198 0.5228 0.0856  0.0281  -0.0895 367 LYS B CD  
7515  C CE  . LYS B 375 ? 0.5328 0.4746 0.5870 0.0885  0.0291  -0.0984 367 LYS B CE  
7516  N NZ  . LYS B 375 ? 0.5474 0.4993 0.6046 0.0917  0.0385  -0.1100 367 LYS B NZ  
7517  N N   . GLU B 376 ? 0.3003 0.2323 0.3079 0.0469  0.0185  -0.0642 368 GLU B N   
7518  C CA  . GLU B 376 ? 0.3401 0.2653 0.3327 0.0394  0.0179  -0.0656 368 GLU B CA  
7519  C C   . GLU B 376 ? 0.3463 0.2684 0.3357 0.0324  0.0115  -0.0559 368 GLU B C   
7520  O O   . GLU B 376 ? 0.3033 0.2164 0.2833 0.0271  0.0078  -0.0568 368 GLU B O   
7521  C CB  . GLU B 376 ? 0.4089 0.3449 0.3933 0.0363  0.0254  -0.0694 368 GLU B CB  
7522  C CG  . GLU B 376 ? 0.4531 0.3842 0.4200 0.0284  0.0240  -0.0689 368 GLU B CG  
7523  C CD  . GLU B 376 ? 0.4818 0.4001 0.4378 0.0283  0.0234  -0.0784 368 GLU B CD  
7524  O OE1 . GLU B 376 ? 0.4150 0.3275 0.3773 0.0347  0.0248  -0.0856 368 GLU B OE1 
7525  O OE2 . GLU B 376 ? 0.5406 0.4542 0.4812 0.0223  0.0212  -0.0790 368 GLU B OE2 
7526  N N   . LEU B 377 ? 0.2757 0.2060 0.2733 0.0325  0.0100  -0.0473 369 LEU B N   
7527  C CA  . LEU B 377 ? 0.2457 0.1765 0.2417 0.0262  0.0055  -0.0382 369 LEU B CA  
7528  C C   . LEU B 377 ? 0.2923 0.2177 0.2970 0.0282  0.0010  -0.0318 369 LEU B C   
7529  O O   . LEU B 377 ? 0.2242 0.1575 0.2359 0.0307  0.0014  -0.0263 369 LEU B O   
7530  C CB  . LEU B 377 ? 0.2814 0.2260 0.2772 0.0238  0.0086  -0.0337 369 LEU B CB  
7531  C CG  . LEU B 377 ? 0.3032 0.2518 0.2879 0.0207  0.0133  -0.0383 369 LEU B CG  
7532  C CD1 . LEU B 377 ? 0.2804 0.2393 0.2643 0.0175  0.0154  -0.0323 369 LEU B CD1 
7533  C CD2 . LEU B 377 ? 0.3042 0.2428 0.2764 0.0160  0.0094  -0.0408 369 LEU B CD2 
7534  N N   . PRO B 378 ? 0.2987 0.2097 0.3020 0.0268  -0.0032 -0.0322 370 PRO B N   
7535  C CA  . PRO B 378 ? 0.3078 0.2119 0.3172 0.0273  -0.0068 -0.0248 370 PRO B CA  
7536  C C   . PRO B 378 ? 0.3178 0.2297 0.3289 0.0218  -0.0082 -0.0156 370 PRO B C   
7537  O O   . PRO B 378 ? 0.3136 0.2231 0.3291 0.0226  -0.0097 -0.0087 370 PRO B O   
7538  C CB  . PRO B 378 ? 0.3100 0.1964 0.3161 0.0245  -0.0102 -0.0280 370 PRO B CB  
7539  C CG  . PRO B 378 ? 0.2895 0.1773 0.2871 0.0194  -0.0101 -0.0347 370 PRO B CG  
7540  C CD  . PRO B 378 ? 0.3015 0.2013 0.2968 0.0237  -0.0047 -0.0393 370 PRO B CD  
7541  N N   . GLU B 379 ? 0.1945 0.1151 0.2017 0.0166  -0.0077 -0.0154 371 GLU B N   
7542  C CA  . GLU B 379 ? 0.1818 0.1109 0.1917 0.0124  -0.0087 -0.0077 371 GLU B CA  
7543  C C   . GLU B 379 ? 0.2064 0.1475 0.2201 0.0161  -0.0056 -0.0042 371 GLU B C   
7544  O O   . GLU B 379 ? 0.2197 0.1676 0.2360 0.0135  -0.0059 0.0019  371 GLU B O   
7545  C CB  . GLU B 379 ? 0.1943 0.1276 0.1989 0.0066  -0.0103 -0.0088 371 GLU B CB  
7546  C CG  . GLU B 379 ? 0.1927 0.1318 0.1897 0.0080  -0.0071 -0.0137 371 GLU B CG  
7547  C CD  . GLU B 379 ? 0.2319 0.1624 0.2203 0.0077  -0.0074 -0.0222 371 GLU B CD  
7548  O OE1 . GLU B 379 ? 0.2563 0.1777 0.2467 0.0109  -0.0072 -0.0264 371 GLU B OE1 
7549  O OE2 . GLU B 379 ? 0.2737 0.2056 0.2525 0.0046  -0.0080 -0.0247 371 GLU B OE2 
7550  N N   . LEU B 380 ? 0.1971 0.1417 0.2122 0.0219  -0.0025 -0.0085 372 LEU B N   
7551  C CA  . LEU B 380 ? 0.1659 0.1230 0.1850 0.0243  0.0003  -0.0066 372 LEU B CA  
7552  C C   . LEU B 380 ? 0.2046 0.1624 0.2291 0.0267  -0.0017 -0.0001 372 LEU B C   
7553  O O   . LEU B 380 ? 0.2742 0.2237 0.3005 0.0307  -0.0039 0.0005  372 LEU B O   
7554  C CB  . LEU B 380 ? 0.2057 0.1676 0.2271 0.0296  0.0042  -0.0137 372 LEU B CB  
7555  C CG  . LEU B 380 ? 0.2130 0.1890 0.2392 0.0308  0.0078  -0.0135 372 LEU B CG  
7556  C CD1 . LEU B 380 ? 0.2216 0.2028 0.2416 0.0249  0.0108  -0.0128 372 LEU B CD1 
7557  C CD2 . LEU B 380 ? 0.2324 0.2141 0.2652 0.0369  0.0112  -0.0207 372 LEU B CD2 
7558  N N   . VAL B 381 ? 0.2040 0.1707 0.2298 0.0246  -0.0010 0.0047  373 VAL B N   
7559  C CA  . VAL B 381 ? 0.1940 0.1625 0.2230 0.0267  -0.0024 0.0104  373 VAL B CA  
7560  C C   . VAL B 381 ? 0.1614 0.1424 0.1938 0.0290  -0.0003 0.0093  373 VAL B C   
7561  O O   . VAL B 381 ? 0.2213 0.2093 0.2530 0.0254  0.0021  0.0092  373 VAL B O   
7562  C CB  . VAL B 381 ? 0.1817 0.1484 0.2093 0.0214  -0.0035 0.0170  373 VAL B CB  
7563  C CG1 . VAL B 381 ? 0.1434 0.1129 0.1721 0.0234  -0.0038 0.0225  373 VAL B CG1 
7564  C CG2 . VAL B 381 ? 0.2050 0.1594 0.2309 0.0183  -0.0057 0.0177  373 VAL B CG2 
7565  N N   . GLY B 382 ? 0.1502 0.1337 0.1867 0.0350  -0.0014 0.0083  374 GLY B N   
7566  C CA  . GLY B 382 ? 0.1995 0.1955 0.2410 0.0370  -0.0000 0.0063  374 GLY B CA  
7567  C C   . GLY B 382 ? 0.1438 0.1428 0.1845 0.0369  -0.0020 0.0119  374 GLY B C   
7568  O O   . GLY B 382 ? 0.1551 0.1470 0.1912 0.0352  -0.0036 0.0177  374 GLY B O   
7569  N N   . GLY B 383 ? 0.1274 0.1373 0.1726 0.0384  -0.0014 0.0097  375 GLY B N   
7570  C CA  . GLY B 383 ? 0.1845 0.1973 0.2279 0.0389  -0.0035 0.0138  375 GLY B CA  
7571  C C   . GLY B 383 ? 0.1560 0.1814 0.2050 0.0389  -0.0024 0.0098  375 GLY B C   
7572  O O   . GLY B 383 ? 0.1112 0.1422 0.1646 0.0365  0.0013  0.0050  375 GLY B O   
7573  N N   . SER B 384 ? 0.1001 0.1293 0.1481 0.0409  -0.0052 0.0116  376 SER B N   
7574  C CA  . SER B 384 ? 0.1093 0.1500 0.1628 0.0400  -0.0045 0.0072  376 SER B CA  
7575  C C   . SER B 384 ? 0.1254 0.1667 0.1731 0.0401  -0.0068 0.0106  376 SER B C   
7576  O O   . SER B 384 ? 0.1477 0.1820 0.1880 0.0426  -0.0097 0.0159  376 SER B O   
7577  C CB  . SER B 384 ? 0.1117 0.1615 0.1751 0.0449  -0.0069 0.0008  376 SER B CB  
7578  O OG  . SER B 384 ? 0.1625 0.2123 0.2246 0.0513  -0.0135 0.0023  376 SER B OG  
7579  N N   . ALA B 385 ? 0.1329 0.1819 0.1835 0.0370  -0.0051 0.0075  377 ALA B N   
7580  C CA  . ALA B 385 ? 0.0921 0.1425 0.1373 0.0371  -0.0069 0.0089  377 ALA B CA  
7581  C C   . ALA B 385 ? 0.1162 0.1748 0.1650 0.0418  -0.0126 0.0048  377 ALA B C   
7582  O O   . ALA B 385 ? 0.1343 0.2022 0.1895 0.0401  -0.0128 -0.0010 377 ALA B O   
7583  C CB  . ALA B 385 ? 0.1541 0.2066 0.1999 0.0315  -0.0024 0.0074  377 ALA B CB  
7584  N N   . ASP B 386 ? 0.1305 0.1850 0.1753 0.0478  -0.0179 0.0077  378 ASP B N   
7585  C CA  . ASP B 386 ? 0.1534 0.2143 0.1997 0.0539  -0.0253 0.0050  378 ASP B CA  
7586  C C   . ASP B 386 ? 0.1906 0.2646 0.2528 0.0552  -0.0265 -0.0035 378 ASP B C   
7587  O O   . ASP B 386 ? 0.1419 0.2265 0.2094 0.0573  -0.0314 -0.0085 378 ASP B O   
7588  C CB  . ASP B 386 ? 0.1537 0.2171 0.1918 0.0531  -0.0276 0.0051  378 ASP B CB  
7589  C CG  . ASP B 386 ? 0.2506 0.3179 0.2855 0.0602  -0.0369 0.0040  378 ASP B CG  
7590  O OD1 . ASP B 386 ? 0.3148 0.3751 0.3452 0.0662  -0.0414 0.0083  378 ASP B OD1 
7591  O OD2 . ASP B 386 ? 0.2486 0.3250 0.2850 0.0599  -0.0403 -0.0012 378 ASP B OD2 
7592  N N   . LEU B 387 ? 0.1492 0.2236 0.2196 0.0538  -0.0220 -0.0057 379 LEU B N   
7593  C CA  . LEU B 387 ? 0.1354 0.2228 0.2217 0.0555  -0.0222 -0.0138 379 LEU B CA  
7594  C C   . LEU B 387 ? 0.1734 0.2611 0.2637 0.0650  -0.0289 -0.0145 379 LEU B C   
7595  O O   . LEU B 387 ? 0.2327 0.3073 0.3141 0.0688  -0.0308 -0.0085 379 LEU B O   
7596  C CB  . LEU B 387 ? 0.1597 0.2474 0.2517 0.0501  -0.0137 -0.0165 379 LEU B CB  
7597  C CG  . LEU B 387 ? 0.2220 0.3084 0.3109 0.0411  -0.0067 -0.0160 379 LEU B CG  
7598  C CD1 . LEU B 387 ? 0.1271 0.2158 0.2222 0.0364  0.0010  -0.0198 379 LEU B CD1 
7599  C CD2 . LEU B 387 ? 0.2527 0.3471 0.3444 0.0382  -0.0083 -0.0192 379 LEU B CD2 
7600  N N   . THR B 388 ? 0.1611 0.2637 0.2660 0.0687  -0.0326 -0.0220 380 THR B N   
7601  C CA  . THR B 388 ? 0.2064 0.3092 0.3173 0.0769  -0.0375 -0.0236 380 THR B CA  
7602  C C   . THR B 388 ? 0.2300 0.3278 0.3448 0.0768  -0.0310 -0.0248 380 THR B C   
7603  O O   . THR B 388 ? 0.1876 0.2925 0.3102 0.0709  -0.0231 -0.0296 380 THR B O   
7604  C CB  . THR B 388 ? 0.2573 0.3755 0.3816 0.0772  -0.0403 -0.0311 380 THR B CB  
7605  O OG1 . THR B 388 ? 0.2740 0.3953 0.3929 0.0785  -0.0480 -0.0301 380 THR B OG1 
7606  C CG2 . THR B 388 ? 0.3162 0.4341 0.4471 0.0840  -0.0433 -0.0328 380 THR B CG2 
7607  N N   . PRO B 389 ? 0.3247 0.4093 0.4334 0.0827  -0.0337 -0.0205 381 PRO B N   
7608  C CA  . PRO B 389 ? 0.3638 0.4427 0.4752 0.0827  -0.0277 -0.0225 381 PRO B CA  
7609  C C   . PRO B 389 ? 0.2765 0.3683 0.4028 0.0825  -0.0237 -0.0313 381 PRO B C   
7610  O O   . PRO B 389 ? 0.2070 0.3070 0.3410 0.0863  -0.0282 -0.0343 381 PRO B O   
7611  C CB  . PRO B 389 ? 0.4478 0.5091 0.5494 0.0894  -0.0330 -0.0163 381 PRO B CB  
7612  C CG  . PRO B 389 ? 0.3952 0.4510 0.4854 0.0912  -0.0402 -0.0091 381 PRO B CG  
7613  C CD  . PRO B 389 ? 0.3773 0.4503 0.4752 0.0892  -0.0421 -0.0138 381 PRO B CD  
7614  N N   . SER B 390 ? 0.2259 0.3197 0.3559 0.0779  -0.0149 -0.0355 382 SER B N   
7615  C CA  . SER B 390 ? 0.1953 0.3005 0.3377 0.0770  -0.0093 -0.0435 382 SER B CA  
7616  C C   . SER B 390 ? 0.1489 0.2478 0.2885 0.0747  -0.0011 -0.0459 382 SER B C   
7617  O O   . SER B 390 ? 0.1166 0.2036 0.2455 0.0728  0.0000  -0.0415 382 SER B O   
7618  C CB  . SER B 390 ? 0.1428 0.2641 0.2942 0.0698  -0.0056 -0.0480 382 SER B CB  
7619  O OG  . SER B 390 ? 0.1649 0.2856 0.3122 0.0613  0.0025  -0.0477 382 SER B OG  
7620  N N   . ASN B 391 ? 0.1552 0.2621 0.3035 0.0742  0.0049  -0.0530 383 ASN B N   
7621  C CA  . ASN B 391 ? 0.1672 0.2693 0.3118 0.0715  0.0136  -0.0565 383 ASN B CA  
7622  C C   . ASN B 391 ? 0.1379 0.2392 0.2755 0.0623  0.0205  -0.0550 383 ASN B C   
7623  O O   . ASN B 391 ? 0.2278 0.3185 0.3545 0.0591  0.0255  -0.0544 383 ASN B O   
7624  C CB  . ASN B 391 ? 0.2244 0.3376 0.3795 0.0715  0.0197  -0.0645 383 ASN B CB  
7625  C CG  . ASN B 391 ? 0.2989 0.4279 0.4622 0.0634  0.0251  -0.0676 383 ASN B CG  
7626  O OD1 . ASN B 391 ? 0.3502 0.4863 0.5184 0.0623  0.0199  -0.0658 383 ASN B OD1 
7627  N ND2 . ASN B 391 ? 0.3579 0.4912 0.5215 0.0575  0.0355  -0.0722 383 ASN B ND2 
7628  N N   . LEU B 392 ? 0.1197 0.2287 0.2591 0.0567  0.0204  -0.0530 384 LEU B N   
7629  C CA  . LEU B 392 ? 0.1246 0.2286 0.2528 0.0464  0.0264  -0.0490 384 LEU B CA  
7630  C C   . LEU B 392 ? 0.1656 0.2526 0.2768 0.0447  0.0218  -0.0393 384 LEU B C   
7631  O O   . LEU B 392 ? 0.2058 0.2855 0.3057 0.0374  0.0262  -0.0357 384 LEU B O   
7632  C CB  . LEU B 392 ? 0.1116 0.2286 0.2482 0.0407  0.0280  -0.0506 384 LEU B CB  
7633  C CG  . LEU B 392 ? 0.1534 0.2839 0.3020 0.0378  0.0336  -0.0577 384 LEU B CG  
7634  C CD1 . LEU B 392 ? 0.1951 0.3336 0.3483 0.0303  0.0346  -0.0579 384 LEU B CD1 
7635  C CD2 . LEU B 392 ? 0.2189 0.3467 0.3626 0.0336  0.0440  -0.0608 384 LEU B CD2 
7636  N N   . THR B 393 ? 0.1416 0.2224 0.2506 0.0510  0.0132  -0.0350 385 THR B N   
7637  C CA  . THR B 393 ? 0.1628 0.2304 0.2581 0.0487  0.0095  -0.0261 385 THR B CA  
7638  C C   . THR B 393 ? 0.1554 0.2094 0.2442 0.0545  0.0040  -0.0220 385 THR B C   
7639  O O   . THR B 393 ? 0.1407 0.1844 0.2193 0.0526  0.0011  -0.0147 385 THR B O   
7640  C CB  . THR B 393 ? 0.2420 0.3150 0.3384 0.0480  0.0051  -0.0230 385 THR B CB  
7641  O OG1 . THR B 393 ? 0.1705 0.2495 0.2750 0.0562  -0.0019 -0.0251 385 THR B OG1 
7642  C CG2 . THR B 393 ? 0.1830 0.2673 0.2853 0.0412  0.0104  -0.0268 385 THR B CG2 
7643  N N   . ASP B 394 ? 0.1413 0.1950 0.2365 0.0615  0.0028  -0.0268 386 ASP B N   
7644  C CA  . ASP B 394 ? 0.2191 0.2582 0.3087 0.0674  -0.0027 -0.0231 386 ASP B CA  
7645  C C   . ASP B 394 ? 0.2452 0.2824 0.3403 0.0723  -0.0003 -0.0304 386 ASP B C   
7646  O O   . ASP B 394 ? 0.2224 0.2717 0.3267 0.0719  0.0054  -0.0382 386 ASP B O   
7647  C CB  . ASP B 394 ? 0.2402 0.2801 0.3322 0.0744  -0.0112 -0.0196 386 ASP B CB  
7648  C CG  . ASP B 394 ? 0.2694 0.2907 0.3515 0.0785  -0.0166 -0.0129 386 ASP B CG  
7649  O OD1 . ASP B 394 ? 0.2476 0.2558 0.3219 0.0749  -0.0140 -0.0110 386 ASP B OD1 
7650  O OD2 . ASP B 394 ? 0.3235 0.3428 0.4051 0.0849  -0.0236 -0.0095 386 ASP B OD2 
7651  N N   . TRP B 395 ? 0.1765 0.1978 0.2657 0.0767  -0.0042 -0.0278 387 TRP B N   
7652  C CA  . TRP B 395 ? 0.2004 0.2176 0.2948 0.0832  -0.0031 -0.0350 387 TRP B CA  
7653  C C   . TRP B 395 ? 0.2176 0.2213 0.3110 0.0922  -0.0114 -0.0313 387 TRP B C   
7654  O O   . TRP B 395 ? 0.2098 0.2040 0.2946 0.0911  -0.0165 -0.0223 387 TRP B O   
7655  C CB  . TRP B 395 ? 0.2352 0.2426 0.3203 0.0772  0.0028  -0.0374 387 TRP B CB  
7656  C CG  . TRP B 395 ? 0.1973 0.1852 0.2690 0.0734  -0.0004 -0.0303 387 TRP B CG  
7657  C CD1 . TRP B 395 ? 0.1871 0.1585 0.2548 0.0768  -0.0026 -0.0314 387 TRP B CD1 
7658  C CD2 . TRP B 395 ? 0.2111 0.1948 0.2731 0.0652  -0.0011 -0.0220 387 TRP B CD2 
7659  N NE1 . TRP B 395 ? 0.1894 0.1471 0.2461 0.0705  -0.0047 -0.0243 387 TRP B NE1 
7660  C CE2 . TRP B 395 ? 0.2049 0.1707 0.2584 0.0636  -0.0038 -0.0185 387 TRP B CE2 
7661  C CE3 . TRP B 395 ? 0.2131 0.2063 0.2736 0.0593  0.0002  -0.0176 387 TRP B CE3 
7662  C CZ2 . TRP B 395 ? 0.2423 0.2015 0.2875 0.0561  -0.0049 -0.0110 387 TRP B CZ2 
7663  C CZ3 . TRP B 395 ? 0.2655 0.2513 0.3170 0.0527  -0.0010 -0.0102 387 TRP B CZ3 
7664  C CH2 . TRP B 395 ? 0.2462 0.2162 0.2908 0.0512  -0.0034 -0.0070 387 TRP B CH2 
7665  N N   . SER B 396 ? 0.2144 0.2171 0.3160 0.1006  -0.0121 -0.0379 388 SER B N   
7666  C CA  . SER B 396 ? 0.2742 0.2666 0.3740 0.1075  -0.0193 -0.0330 388 SER B CA  
7667  C C   . SER B 396 ? 0.2497 0.2178 0.3360 0.1068  -0.0232 -0.0253 388 SER B C   
7668  O O   . SER B 396 ? 0.2974 0.2564 0.3779 0.1095  -0.0293 -0.0173 388 SER B O   
7669  C CB  . SER B 396 ? 0.3085 0.3042 0.4175 0.1140  -0.0178 -0.0405 388 SER B CB  
7670  O OG  . SER B 396 ? 0.4266 0.4122 0.5327 0.1133  -0.0127 -0.0464 388 SER B OG  
7671  N N   . ASN B 397 ? 0.2330 0.1905 0.3128 0.1016  -0.0193 -0.0271 389 ASN B N   
7672  C CA  . ASN B 397 ? 0.3392 0.2737 0.4067 0.0984  -0.0218 -0.0204 389 ASN B CA  
7673  C C   . ASN B 397 ? 0.2548 0.1862 0.3117 0.0890  -0.0221 -0.0102 389 ASN B C   
7674  O O   . ASN B 397 ? 0.3018 0.2153 0.3496 0.0854  -0.0238 -0.0042 389 ASN B O   
7675  C CB  . ASN B 397 ? 0.3372 0.2625 0.4012 0.0946  -0.0169 -0.0271 389 ASN B CB  
7676  C CG  . ASN B 397 ? 0.3760 0.2974 0.4478 0.1045  -0.0170 -0.0362 389 ASN B CG  
7677  O OD1 . ASN B 397 ? 0.4165 0.3362 0.4912 0.1108  -0.0208 -0.0333 389 ASN B OD1 
7678  N ND2 . ASN B 397 ? 0.3835 0.3058 0.4555 0.1024  -0.0110 -0.0457 389 ASN B ND2 
7679  N N   . SER B 398 ? 0.1957 0.1438 0.2544 0.0848  -0.0204 -0.0083 390 SER B N   
7680  C CA  . SER B 398 ? 0.2267 0.1725 0.2763 0.0761  -0.0198 0.0002  390 SER B CA  
7681  C C   . SER B 398 ? 0.2466 0.1793 0.2888 0.0788  -0.0254 0.0096  390 SER B C   
7682  O O   . SER B 398 ? 0.2466 0.1777 0.2910 0.0879  -0.0308 0.0105  390 SER B O   
7683  C CB  . SER B 398 ? 0.2231 0.1880 0.2760 0.0720  -0.0170 -0.0002 390 SER B CB  
7684  O OG  . SER B 398 ? 0.2421 0.2161 0.2996 0.0781  -0.0212 0.0009  390 SER B OG  
7685  N N   . VAL B 399 ? 0.2025 0.1255 0.2356 0.0708  -0.0241 0.0168  391 VAL B N   
7686  C CA  . VAL B 399 ? 0.2312 0.1394 0.2549 0.0710  -0.0275 0.0265  391 VAL B CA  
7687  C C   . VAL B 399 ? 0.2785 0.1955 0.2975 0.0643  -0.0254 0.0325  391 VAL B C   
7688  O O   . VAL B 399 ? 0.2397 0.1601 0.2582 0.0556  -0.0209 0.0329  391 VAL B O   
7689  C CB  . VAL B 399 ? 0.2745 0.1621 0.2927 0.0665  -0.0268 0.0290  391 VAL B CB  
7690  C CG1 . VAL B 399 ? 0.2630 0.1358 0.2705 0.0641  -0.0285 0.0401  391 VAL B CG1 
7691  C CG2 . VAL B 399 ? 0.3606 0.2370 0.3827 0.0740  -0.0292 0.0225  391 VAL B CG2 
7692  N N   . SER B 400 ? 0.2688 0.1894 0.2841 0.0689  -0.0289 0.0369  392 SER B N   
7693  C CA  . SER B 400 ? 0.1995 0.1286 0.2097 0.0636  -0.0267 0.0417  392 SER B CA  
7694  C C   . SER B 400 ? 0.2679 0.1849 0.2693 0.0554  -0.0233 0.0495  392 SER B C   
7695  O O   . SER B 400 ? 0.2254 0.1250 0.2190 0.0565  -0.0252 0.0556  392 SER B O   
7696  C CB  . SER B 400 ? 0.3371 0.2698 0.3427 0.0707  -0.0320 0.0447  392 SER B CB  
7697  O OG  . SER B 400 ? 0.3765 0.3235 0.3928 0.0772  -0.0350 0.0369  392 SER B OG  
7698  N N   . VAL B 401 ? 0.2352 0.1615 0.2385 0.0473  -0.0183 0.0494  393 VAL B N   
7699  C CA  . VAL B 401 ? 0.2083 0.1277 0.2058 0.0393  -0.0145 0.0562  393 VAL B CA  
7700  C C   . VAL B 401 ? 0.2700 0.1870 0.2566 0.0407  -0.0149 0.0637  393 VAL B C   
7701  O O   . VAL B 401 ? 0.2223 0.1506 0.2079 0.0446  -0.0165 0.0623  393 VAL B O   
7702  C CB  . VAL B 401 ? 0.2048 0.1368 0.2088 0.0317  -0.0097 0.0533  393 VAL B CB  
7703  C CG1 . VAL B 401 ? 0.1845 0.1138 0.1851 0.0238  -0.0054 0.0598  393 VAL B CG1 
7704  C CG2 . VAL B 401 ? 0.2040 0.1361 0.2155 0.0299  -0.0097 0.0467  393 VAL B CG2 
7705  N N   . THR B 402 ? 0.2739 0.1756 0.2517 0.0371  -0.0134 0.0715  394 THR B N   
7706  C CA  . THR B 402 ? 0.3163 0.2136 0.2807 0.0378  -0.0129 0.0794  394 THR B CA  
7707  C C   . THR B 402 ? 0.2938 0.1870 0.2547 0.0276  -0.0057 0.0853  394 THR B C   
7708  O O   . THR B 402 ? 0.2452 0.1387 0.2149 0.0205  -0.0022 0.0832  394 THR B O   
7709  C CB  . THR B 402 ? 0.3127 0.1922 0.2661 0.0454  -0.0189 0.0847  394 THR B CB  
7710  O OG1 . THR B 402 ? 0.3499 0.2103 0.3019 0.0418  -0.0179 0.0882  394 THR B OG1 
7711  C CG2 . THR B 402 ? 0.3589 0.2441 0.3187 0.0561  -0.0264 0.0780  394 THR B CG2 
7712  N N   . ARG B 403 ? 0.3086 0.1981 0.2561 0.0267  -0.0034 0.0926  395 ARG B N   
7713  C CA  . ARG B 403 ? 0.3734 0.2595 0.3174 0.0169  0.0047  0.0985  395 ARG B CA  
7714  C C   . ARG B 403 ? 0.3680 0.2362 0.3128 0.0113  0.0061  0.1022  395 ARG B C   
7715  O O   . ARG B 403 ? 0.3674 0.2382 0.3205 0.0019  0.0119  0.1020  395 ARG B O   
7716  C CB  . ARG B 403 ? 0.3809 0.2633 0.3071 0.0175  0.0067  0.1055  395 ARG B CB  
7717  C CG  . ARG B 403 ? 0.4069 0.2909 0.3308 0.0068  0.0163  0.1094  395 ARG B CG  
7718  C CD  . ARG B 403 ? 0.4867 0.3649 0.3911 0.0062  0.0176  0.1152  395 ARG B CD  
7719  N NE  . ARG B 403 ? 0.5458 0.4308 0.4502 -0.0033 0.0280  0.1171  395 ARG B NE  
7720  C CZ  . ARG B 403 ? 0.5447 0.4464 0.4520 -0.0035 0.0334  0.1142  395 ARG B CZ  
7721  N NH1 . ARG B 403 ? 0.5377 0.4500 0.4467 0.0048  0.0291  0.1100  395 ARG B NH1 
7722  N NH2 . ARG B 403 ? 0.4268 0.3352 0.3359 -0.0120 0.0431  0.1151  395 ARG B NH2 
7723  N N   . ASP B 404 ? 0.3385 0.1904 0.2766 0.0164  -0.0005 0.1032  396 ASP B N   
7724  C CA  . ASP B 404 ? 0.4307 0.2640 0.3669 0.0104  -0.0002 0.1063  396 ASP B CA  
7725  C C   . ASP B 404 ? 0.4352 0.2620 0.3826 0.0118  -0.0030 0.1003  396 ASP B C   
7726  O O   . ASP B 404 ? 0.3972 0.2087 0.3441 0.0056  -0.0021 0.1015  396 ASP B O   
7727  C CB  . ASP B 404 ? 0.5781 0.3985 0.5029 0.0142  -0.0051 0.1132  396 ASP B CB  
7728  C CG  . ASP B 404 ? 0.6506 0.4747 0.5619 0.0113  -0.0015 0.1197  396 ASP B CG  
7729  O OD1 . ASP B 404 ? 0.6122 0.4436 0.5233 0.0027  0.0065  0.1201  396 ASP B OD1 
7730  O OD2 . ASP B 404 ? 0.7286 0.5490 0.6301 0.0180  -0.0062 0.1239  396 ASP B OD2 
7731  N N   . LYS B 405 ? 0.3480 0.1862 0.3056 0.0190  -0.0063 0.0934  397 LYS B N   
7732  C CA  . LYS B 405 ? 0.4028 0.2358 0.3700 0.0203  -0.0094 0.0862  397 LYS B CA  
7733  C C   . LYS B 405 ? 0.3513 0.2057 0.3314 0.0206  -0.0094 0.0763  397 LYS B C   
7734  O O   . LYS B 405 ? 0.3672 0.2389 0.3487 0.0231  -0.0090 0.0746  397 LYS B O   
7735  C CB  . LYS B 405 ? 0.5070 0.3266 0.4698 0.0313  -0.0160 0.0856  397 LYS B CB  
7736  N N   . GLY B 406 ? 0.3502 0.2023 0.3387 0.0178  -0.0100 0.0698  398 GLY B N   
7737  C CA  . GLY B 406 ? 0.2606 0.1299 0.2590 0.0180  -0.0102 0.0609  398 GLY B CA  
7738  C C   . GLY B 406 ? 0.2703 0.1450 0.2702 0.0286  -0.0142 0.0550  398 GLY B C   
7739  O O   . GLY B 406 ? 0.3308 0.1997 0.3255 0.0366  -0.0175 0.0577  398 GLY B O   
7740  N N   . GLY B 407 ? 0.2809 0.1673 0.2885 0.0285  -0.0139 0.0467  399 GLY B N   
7741  C CA  . GLY B 407 ? 0.2947 0.1897 0.3059 0.0370  -0.0160 0.0402  399 GLY B CA  
7742  C C   . GLY B 407 ? 0.2345 0.1455 0.2519 0.0338  -0.0135 0.0336  399 GLY B C   
7743  O O   . GLY B 407 ? 0.2570 0.1714 0.2756 0.0261  -0.0113 0.0339  399 GLY B O   
7744  N N   . ASN B 408 ? 0.1931 0.1139 0.2146 0.0400  -0.0141 0.0275  400 ASN B N   
7745  C CA  . ASN B 408 ? 0.2160 0.1504 0.2416 0.0373  -0.0112 0.0215  400 ASN B CA  
7746  C C   . ASN B 408 ? 0.2296 0.1793 0.2588 0.0413  -0.0105 0.0197  400 ASN B C   
7747  O O   . ASN B 408 ? 0.1901 0.1496 0.2233 0.0415  -0.0082 0.0135  400 ASN B O   
7748  C CB  . ASN B 408 ? 0.2222 0.1519 0.2492 0.0384  -0.0108 0.0135  400 ASN B CB  
7749  C CG  . ASN B 408 ? 0.2691 0.1932 0.2987 0.0476  -0.0130 0.0095  400 ASN B CG  
7750  O OD1 . ASN B 408 ? 0.2677 0.1935 0.2987 0.0537  -0.0154 0.0125  400 ASN B OD1 
7751  N ND2 . ASN B 408 ? 0.2529 0.1705 0.2832 0.0491  -0.0124 0.0023  400 ASN B ND2 
7752  N N   . TYR B 409 ? 0.1588 0.1107 0.1863 0.0439  -0.0123 0.0248  401 TYR B N   
7753  C CA  . TYR B 409 ? 0.1786 0.1452 0.2098 0.0467  -0.0121 0.0229  401 TYR B CA  
7754  C C   . TYR B 409 ? 0.1472 0.1156 0.1731 0.0448  -0.0125 0.0297  401 TYR B C   
7755  O O   . TYR B 409 ? 0.1913 0.1496 0.2109 0.0466  -0.0149 0.0355  401 TYR B O   
7756  C CB  . TYR B 409 ? 0.1824 0.1515 0.2186 0.0558  -0.0156 0.0186  401 TYR B CB  
7757  C CG  . TYR B 409 ? 0.1945 0.1809 0.2380 0.0570  -0.0144 0.0135  401 TYR B CG  
7758  C CD1 . TYR B 409 ? 0.2078 0.2020 0.2505 0.0582  -0.0165 0.0159  401 TYR B CD1 
7759  C CD2 . TYR B 409 ? 0.1355 0.1300 0.1858 0.0560  -0.0105 0.0059  401 TYR B CD2 
7760  C CE1 . TYR B 409 ? 0.2075 0.2173 0.2579 0.0582  -0.0153 0.0107  401 TYR B CE1 
7761  C CE2 . TYR B 409 ? 0.1928 0.2027 0.2503 0.0557  -0.0085 0.0013  401 TYR B CE2 
7762  C CZ  . TYR B 409 ? 0.2201 0.2375 0.2783 0.0567  -0.0111 0.0036  401 TYR B CZ  
7763  O OH  . TYR B 409 ? 0.2093 0.2415 0.2753 0.0555  -0.0092 -0.0015 401 TYR B OH  
7764  N N   . ILE B 410 ? 0.1376 0.1177 0.1653 0.0413  -0.0099 0.0289  402 ILE B N   
7765  C CA  . ILE B 410 ? 0.1333 0.1157 0.1560 0.0387  -0.0090 0.0342  402 ILE B CA  
7766  C C   . ILE B 410 ? 0.1816 0.1748 0.2057 0.0426  -0.0107 0.0317  402 ILE B C   
7767  O O   . ILE B 410 ? 0.1430 0.1465 0.1737 0.0419  -0.0092 0.0262  402 ILE B O   
7768  C CB  . ILE B 410 ? 0.1780 0.1640 0.2017 0.0315  -0.0048 0.0351  402 ILE B CB  
7769  C CG1 . ILE B 410 ? 0.2346 0.2110 0.2580 0.0273  -0.0041 0.0369  402 ILE B CG1 
7770  C CG2 . ILE B 410 ? 0.1303 0.1202 0.1500 0.0296  -0.0031 0.0394  402 ILE B CG2 
7771  C CD1 . ILE B 410 ? 0.2733 0.2547 0.2999 0.0214  -0.0015 0.0358  402 ILE B CD1 
7772  N N   . HIS B 411 ? 0.2190 0.2095 0.2365 0.0460  -0.0137 0.0359  403 HIS B N   
7773  C CA  . HIS B 411 ? 0.1353 0.1359 0.1526 0.0490  -0.0161 0.0337  403 HIS B CA  
7774  C C   . HIS B 411 ? 0.1440 0.1487 0.1571 0.0437  -0.0121 0.0358  403 HIS B C   
7775  O O   . HIS B 411 ? 0.1694 0.1680 0.1732 0.0424  -0.0112 0.0418  403 HIS B O   
7776  C CB  . HIS B 411 ? 0.1502 0.1452 0.1606 0.0560  -0.0224 0.0368  403 HIS B CB  
7777  C CG  . HIS B 411 ? 0.2924 0.2822 0.3076 0.0622  -0.0265 0.0347  403 HIS B CG  
7778  N ND1 . HIS B 411 ? 0.3056 0.3062 0.3332 0.0660  -0.0281 0.0267  403 HIS B ND1 
7779  C CD2 . HIS B 411 ? 0.2942 0.2690 0.3043 0.0654  -0.0289 0.0392  403 HIS B CD2 
7780  C CE1 . HIS B 411 ? 0.2760 0.2692 0.3062 0.0720  -0.0314 0.0259  403 HIS B CE1 
7781  N NE2 . HIS B 411 ? 0.2867 0.2632 0.3060 0.0719  -0.0324 0.0336  403 HIS B NE2 
7782  N N   . TYR B 412 ? 0.1321 0.1465 0.1519 0.0406  -0.0092 0.0309  404 TYR B N   
7783  C CA  . TYR B 412 ? 0.1164 0.1345 0.1339 0.0363  -0.0054 0.0319  404 TYR B CA  
7784  C C   . TYR B 412 ? 0.1594 0.1824 0.1714 0.0385  -0.0074 0.0311  404 TYR B C   
7785  O O   . TYR B 412 ? 0.1838 0.2081 0.1918 0.0357  -0.0040 0.0324  404 TYR B O   
7786  C CB  . TYR B 412 ? 0.1007 0.1249 0.1262 0.0325  -0.0020 0.0274  404 TYR B CB  
7787  C CG  . TYR B 412 ? 0.1427 0.1618 0.1709 0.0294  0.0000  0.0286  404 TYR B CG  
7788  C CD1 . TYR B 412 ? 0.1681 0.1840 0.1947 0.0255  0.0028  0.0324  404 TYR B CD1 
7789  C CD2 . TYR B 412 ? 0.1318 0.1499 0.1643 0.0306  -0.0008 0.0252  404 TYR B CD2 
7790  C CE1 . TYR B 412 ? 0.1398 0.1517 0.1689 0.0226  0.0035  0.0329  404 TYR B CE1 
7791  C CE2 . TYR B 412 ? 0.1233 0.1362 0.1565 0.0277  0.0006  0.0257  404 TYR B CE2 
7792  C CZ  . TYR B 412 ? 0.1682 0.1780 0.1996 0.0236  0.0023  0.0296  404 TYR B CZ  
7793  O OH  . TYR B 412 ? 0.1762 0.1814 0.2083 0.0206  0.0026  0.0296  404 TYR B OH  
7794  N N   . GLY B 413 ? 0.1436 0.1698 0.1556 0.0437  -0.0129 0.0285  405 GLY B N   
7795  C CA  . GLY B 413 ? 0.1260 0.1581 0.1330 0.0454  -0.0156 0.0263  405 GLY B CA  
7796  C C   . GLY B 413 ? 0.1275 0.1693 0.1427 0.0418  -0.0129 0.0197  405 GLY B C   
7797  O O   . GLY B 413 ? 0.1249 0.1690 0.1494 0.0389  -0.0099 0.0169  405 GLY B O   
7798  N N   . VAL B 414 ? 0.1408 0.1868 0.1510 0.0419  -0.0140 0.0173  406 VAL B N   
7799  C CA  . VAL B 414 ? 0.1413 0.1950 0.1588 0.0385  -0.0120 0.0105  406 VAL B CA  
7800  C C   . VAL B 414 ? 0.1370 0.1870 0.1530 0.0339  -0.0053 0.0124  406 VAL B C   
7801  O O   . VAL B 414 ? 0.1099 0.1602 0.1202 0.0330  -0.0036 0.0112  406 VAL B O   
7802  C CB  . VAL B 414 ? 0.1804 0.2403 0.1939 0.0406  -0.0170 0.0056  406 VAL B CB  
7803  C CG1 . VAL B 414 ? 0.1726 0.2403 0.1963 0.0367  -0.0158 -0.0023 406 VAL B CG1 
7804  C CG2 . VAL B 414 ? 0.1565 0.2193 0.1698 0.0466  -0.0251 0.0053  406 VAL B CG2 
7805  N N   . ARG B 415 ? 0.1049 0.1513 0.1261 0.0315  -0.0017 0.0149  407 ARG B N   
7806  C CA  . ARG B 415 ? 0.0959 0.1383 0.1163 0.0283  0.0035  0.0183  407 ARG B CA  
7807  C C   . ARG B 415 ? 0.0876 0.1293 0.1161 0.0254  0.0057  0.0173  407 ARG B C   
7808  O O   . ARG B 415 ? 0.1149 0.1524 0.1442 0.0245  0.0066  0.0209  407 ARG B O   
7809  C CB  . ARG B 415 ? 0.1015 0.1379 0.1154 0.0289  0.0044  0.0250  407 ARG B CB  
7810  C CG  . ARG B 415 ? 0.1400 0.1748 0.1425 0.0314  0.0030  0.0275  407 ARG B CG  
7811  C CD  . ARG B 415 ? 0.1991 0.2269 0.1961 0.0303  0.0056  0.0348  407 ARG B CD  
7812  N NE  . ARG B 415 ? 0.1342 0.1584 0.1177 0.0323  0.0050  0.0385  407 ARG B NE  
7813  C CZ  . ARG B 415 ? 0.1701 0.1881 0.1461 0.0356  0.0005  0.0422  407 ARG B CZ  
7814  N NH1 . ARG B 415 ? 0.1681 0.1835 0.1501 0.0376  -0.0036 0.0421  407 ARG B NH1 
7815  N NH2 . ARG B 415 ? 0.2111 0.2248 0.1724 0.0372  0.0001  0.0462  407 ARG B NH2 
7816  N N   . GLU B 416 ? 0.0916 0.1367 0.1252 0.0234  0.0066  0.0124  408 GLU B N   
7817  C CA  . GLU B 416 ? 0.0872 0.1308 0.1261 0.0206  0.0087  0.0116  408 GLU B CA  
7818  C C   . GLU B 416 ? 0.0775 0.1159 0.1154 0.0186  0.0116  0.0152  408 GLU B C   
7819  O O   . GLU B 416 ? 0.1224 0.1576 0.1611 0.0175  0.0120  0.0174  408 GLU B O   
7820  C CB  . GLU B 416 ? 0.0946 0.1423 0.1387 0.0182  0.0097  0.0057  408 GLU B CB  
7821  C CG  . GLU B 416 ? 0.0793 0.1347 0.1280 0.0200  0.0064  0.0011  408 GLU B CG  
7822  C CD  . GLU B 416 ? 0.1458 0.2052 0.1916 0.0223  0.0028  -0.0013 408 GLU B CD  
7823  O OE1 . GLU B 416 ? 0.1348 0.1910 0.1750 0.0217  0.0041  -0.0003 408 GLU B OE1 
7824  O OE2 . GLU B 416 ? 0.1280 0.1940 0.1767 0.0250  -0.0016 -0.0046 408 GLU B OE2 
7825  N N   . PHE B 417 ? 0.0788 0.1166 0.1152 0.0184  0.0132  0.0152  409 PHE B N   
7826  C CA  . PHE B 417 ? 0.1707 0.2048 0.2080 0.0175  0.0152  0.0183  409 PHE B CA  
7827  C C   . PHE B 417 ? 0.1424 0.1759 0.1790 0.0181  0.0146  0.0230  409 PHE B C   
7828  O O   . PHE B 417 ? 0.1089 0.1399 0.1475 0.0169  0.0143  0.0254  409 PHE B O   
7829  C CB  . PHE B 417 ? 0.1552 0.1896 0.1922 0.0183  0.0172  0.0167  409 PHE B CB  
7830  C CG  . PHE B 417 ? 0.1370 0.1676 0.1770 0.0180  0.0186  0.0183  409 PHE B CG  
7831  C CD1 . PHE B 417 ? 0.0932 0.1209 0.1347 0.0170  0.0175  0.0215  409 PHE B CD1 
7832  C CD2 . PHE B 417 ? 0.1117 0.1414 0.1525 0.0194  0.0206  0.0160  409 PHE B CD2 
7833  C CE1 . PHE B 417 ? 0.1161 0.1404 0.1599 0.0177  0.0175  0.0231  409 PHE B CE1 
7834  C CE2 . PHE B 417 ? 0.1586 0.1846 0.2028 0.0204  0.0211  0.0174  409 PHE B CE2 
7835  C CZ  . PHE B 417 ? 0.1364 0.1599 0.1821 0.0197  0.0191  0.0212  409 PHE B CZ  
7836  N N   . GLY B 418 ? 0.1280 0.1630 0.1609 0.0197  0.0143  0.0244  410 GLY B N   
7837  C CA  . GLY B 418 ? 0.1246 0.1576 0.1566 0.0193  0.0142  0.0290  410 GLY B CA  
7838  C C   . GLY B 418 ? 0.1323 0.1620 0.1657 0.0186  0.0118  0.0298  410 GLY B C   
7839  O O   . GLY B 418 ? 0.1158 0.1431 0.1513 0.0169  0.0117  0.0323  410 GLY B O   
7840  N N   . MET B 419 ? 0.1039 0.1340 0.1369 0.0199  0.0099  0.0267  411 MET B N   
7841  C CA  . MET B 419 ? 0.1308 0.1580 0.1652 0.0198  0.0084  0.0263  411 MET B CA  
7842  C C   . MET B 419 ? 0.1227 0.1480 0.1591 0.0170  0.0094  0.0261  411 MET B C   
7843  O O   . MET B 419 ? 0.1134 0.1349 0.1496 0.0158  0.0085  0.0279  411 MET B O   
7844  C CB  . MET B 419 ? 0.0810 0.1113 0.1170 0.0219  0.0069  0.0220  411 MET B CB  
7845  C CG  . MET B 419 ? 0.1074 0.1357 0.1456 0.0218  0.0066  0.0201  411 MET B CG  
7846  S SD  . MET B 419 ? 0.1196 0.1543 0.1628 0.0249  0.0053  0.0142  411 MET B SD  
7847  C CE  . MET B 419 ? 0.1150 0.1553 0.1619 0.0209  0.0090  0.0101  411 MET B CE  
7848  N N   . GLY B 420 ? 0.1087 0.1356 0.1461 0.0158  0.0110  0.0241  412 GLY B N   
7849  C CA  . GLY B 420 ? 0.1543 0.1779 0.1912 0.0135  0.0115  0.0245  412 GLY B CA  
7850  C C   . GLY B 420 ? 0.1342 0.1562 0.1720 0.0129  0.0102  0.0281  412 GLY B C   
7851  O O   . GLY B 420 ? 0.0884 0.1073 0.1250 0.0116  0.0085  0.0289  412 GLY B O   
7852  N N   . ALA B 421 ? 0.0758 0.1006 0.1161 0.0138  0.0111  0.0296  413 ALA B N   
7853  C CA  . ALA B 421 ? 0.1098 0.1356 0.1539 0.0132  0.0102  0.0323  413 ALA B CA  
7854  C C   . ALA B 421 ? 0.1235 0.1487 0.1685 0.0117  0.0091  0.0344  413 ALA B C   
7855  O O   . ALA B 421 ? 0.1173 0.1426 0.1658 0.0100  0.0072  0.0357  413 ALA B O   
7856  C CB  . ALA B 421 ? 0.1251 0.1551 0.1725 0.0147  0.0126  0.0325  413 ALA B CB  
7857  N N   . ILE B 422 ? 0.0983 0.1222 0.1404 0.0124  0.0097  0.0346  414 ILE B N   
7858  C CA  . ILE B 422 ? 0.1128 0.1331 0.1548 0.0108  0.0086  0.0368  414 ILE B CA  
7859  C C   . ILE B 422 ? 0.1513 0.1669 0.1921 0.0097  0.0059  0.0350  414 ILE B C   
7860  O O   . ILE B 422 ? 0.1268 0.1397 0.1694 0.0072  0.0042  0.0360  414 ILE B O   
7861  C CB  . ILE B 422 ? 0.1268 0.1448 0.1642 0.0127  0.0093  0.0381  414 ILE B CB  
7862  C CG1 . ILE B 422 ? 0.0894 0.1109 0.1262 0.0125  0.0125  0.0407  414 ILE B CG1 
7863  C CG2 . ILE B 422 ? 0.1083 0.1188 0.1439 0.0118  0.0075  0.0396  414 ILE B CG2 
7864  C CD1 . ILE B 422 ? 0.1078 0.1268 0.1370 0.0151  0.0127  0.0420  414 ILE B CD1 
7865  N N   . MET B 423 ? 0.1376 0.1523 0.1753 0.0113  0.0058  0.0319  415 MET B N   
7866  C CA  A MET B 423 ? 0.1482 0.1587 0.1832 0.0103  0.0042  0.0295  415 MET B CA  
7867  C CA  B MET B 423 ? 0.1380 0.1484 0.1731 0.0103  0.0042  0.0295  415 MET B CA  
7868  C C   . MET B 423 ? 0.0943 0.1043 0.1295 0.0079  0.0022  0.0302  415 MET B C   
7869  O O   . MET B 423 ? 0.1288 0.1348 0.1623 0.0061  -0.0002 0.0292  415 MET B O   
7870  C CB  A MET B 423 ? 0.0994 0.1109 0.1320 0.0117  0.0059  0.0258  415 MET B CB  
7871  C CB  B MET B 423 ? 0.1132 0.1244 0.1458 0.0118  0.0058  0.0258  415 MET B CB  
7872  C CG  A MET B 423 ? 0.0862 0.0991 0.1198 0.0148  0.0065  0.0239  415 MET B CG  
7873  C CG  B MET B 423 ? 0.1198 0.1312 0.1532 0.0148  0.0059  0.0240  415 MET B CG  
7874  S SD  A MET B 423 ? 0.1460 0.1644 0.1808 0.0154  0.0092  0.0193  415 MET B SD  
7875  S SD  B MET B 423 ? 0.1497 0.1634 0.1830 0.0159  0.0080  0.0183  415 MET B SD  
7876  C CE  A MET B 423 ? 0.1171 0.1315 0.1475 0.0128  0.0107  0.0168  415 MET B CE  
7877  C CE  B MET B 423 ? 0.1060 0.1251 0.1402 0.0142  0.0107  0.0179  415 MET B CE  
7878  N N   . ASN B 424 ? 0.0921 0.1056 0.1291 0.0081  0.0026  0.0314  416 ASN B N   
7879  C CA  . ASN B 424 ? 0.1385 0.1519 0.1762 0.0068  -0.0005 0.0324  416 ASN B CA  
7880  C C   . ASN B 424 ? 0.1442 0.1591 0.1877 0.0047  -0.0031 0.0337  416 ASN B C   
7881  O O   . ASN B 424 ? 0.1266 0.1395 0.1691 0.0028  -0.0070 0.0329  416 ASN B O   
7882  C CB  . ASN B 424 ? 0.1181 0.1347 0.1584 0.0085  0.0001  0.0338  416 ASN B CB  
7883  C CG  . ASN B 424 ? 0.1649 0.1778 0.1987 0.0092  0.0021  0.0325  416 ASN B CG  
7884  O OD1 . ASN B 424 ? 0.1518 0.1610 0.1795 0.0082  0.0030  0.0306  416 ASN B OD1 
7885  N ND2 . ASN B 424 ? 0.1260 0.1397 0.1615 0.0108  0.0032  0.0333  416 ASN B ND2 
7886  N N   . GLY B 425 ? 0.0951 0.1133 0.1441 0.0044  -0.0007 0.0355  417 GLY B N   
7887  C CA  . GLY B 425 ? 0.0891 0.1086 0.1445 0.0011  -0.0020 0.0367  417 GLY B CA  
7888  C C   . GLY B 425 ? 0.1325 0.1443 0.1842 -0.0011 -0.0035 0.0355  417 GLY B C   
7889  O O   . GLY B 425 ? 0.1167 0.1275 0.1721 -0.0046 -0.0064 0.0350  417 GLY B O   
7890  N N   . LEU B 426 ? 0.0965 0.1029 0.1417 0.0012  -0.0019 0.0345  418 LEU B N   
7891  C CA  . LEU B 426 ? 0.1698 0.1679 0.2113 0.0003  -0.0035 0.0326  418 LEU B CA  
7892  C C   . LEU B 426 ? 0.1286 0.1240 0.1670 -0.0013 -0.0071 0.0290  418 LEU B C   
7893  O O   . LEU B 426 ? 0.1597 0.1502 0.1987 -0.0043 -0.0098 0.0276  418 LEU B O   
7894  C CB  . LEU B 426 ? 0.1041 0.0988 0.1408 0.0044  -0.0016 0.0312  418 LEU B CB  
7895  C CG  . LEU B 426 ? 0.1231 0.1169 0.1599 0.0063  0.0004  0.0345  418 LEU B CG  
7896  C CD1 . LEU B 426 ? 0.1819 0.1765 0.2155 0.0112  0.0012  0.0323  418 LEU B CD1 
7897  C CD2 . LEU B 426 ? 0.1461 0.1310 0.1827 0.0044  -0.0003 0.0368  418 LEU B CD2 
7898  N N   . VAL B 427 ? 0.1403 0.1381 0.1742 0.0004  -0.0073 0.0276  419 VAL B N   
7899  C CA  A VAL B 427 ? 0.1836 0.1783 0.2113 -0.0009 -0.0107 0.0246  419 VAL B CA  
7900  C CA  B VAL B 427 ? 0.1693 0.1635 0.1971 -0.0010 -0.0107 0.0245  419 VAL B CA  
7901  C C   . VAL B 427 ? 0.1921 0.1897 0.2246 -0.0039 -0.0157 0.0255  419 VAL B C   
7902  O O   . VAL B 427 ? 0.1564 0.1502 0.1860 -0.0064 -0.0199 0.0227  419 VAL B O   
7903  C CB  A VAL B 427 ? 0.2222 0.2180 0.2432 0.0010  -0.0090 0.0243  419 VAL B CB  
7904  C CB  B VAL B 427 ? 0.2367 0.2307 0.2564 0.0010  -0.0088 0.0232  419 VAL B CB  
7905  C CG1 A VAL B 427 ? 0.2648 0.2563 0.2764 -0.0004 -0.0126 0.0221  419 VAL B CG1 
7906  C CG1 B VAL B 427 ? 0.1881 0.1877 0.2107 0.0023  -0.0076 0.0265  419 VAL B CG1 
7907  C CG2 A VAL B 427 ? 0.1904 0.1855 0.2087 0.0033  -0.0042 0.0225  419 VAL B CG2 
7908  C CG2 B VAL B 427 ? 0.2974 0.2869 0.3079 -0.0006 -0.0122 0.0205  419 VAL B CG2 
7909  N N   . LEU B 428 ? 0.1296 0.1349 0.1700 -0.0034 -0.0155 0.0288  420 LEU B N   
7910  C CA  . LEU B 428 ? 0.1636 0.1744 0.2112 -0.0054 -0.0206 0.0293  420 LEU B CA  
7911  C C   . LEU B 428 ? 0.1935 0.2037 0.2480 -0.0101 -0.0226 0.0281  420 LEU B C   
7912  O O   . LEU B 428 ? 0.1891 0.2009 0.2463 -0.0128 -0.0285 0.0260  420 LEU B O   
7913  C CB  . LEU B 428 ? 0.1489 0.1686 0.2056 -0.0033 -0.0189 0.0324  420 LEU B CB  
7914  C CG  . LEU B 428 ? 0.1789 0.1986 0.2303 0.0008  -0.0190 0.0334  420 LEU B CG  
7915  C CD1 . LEU B 428 ? 0.1427 0.1691 0.2021 0.0033  -0.0151 0.0356  420 LEU B CD1 
7916  C CD2 . LEU B 428 ? 0.1146 0.1346 0.1637 0.0013  -0.0264 0.0331  420 LEU B CD2 
7917  N N   . HIS B 429 ? 0.1541 0.1610 0.2107 -0.0114 -0.0181 0.0292  421 HIS B N   
7918  C CA  . HIS B 429 ? 0.1192 0.1237 0.1824 -0.0166 -0.0190 0.0288  421 HIS B CA  
7919  C C   . HIS B 429 ? 0.1832 0.1799 0.2408 -0.0192 -0.0241 0.0240  421 HIS B C   
7920  O O   . HIS B 429 ? 0.1613 0.1592 0.2260 -0.0243 -0.0280 0.0223  421 HIS B O   
7921  C CB  . HIS B 429 ? 0.1201 0.1186 0.1822 -0.0166 -0.0135 0.0315  421 HIS B CB  
7922  C CG  . HIS B 429 ? 0.1280 0.1224 0.1965 -0.0226 -0.0132 0.0323  421 HIS B CG  
7923  N ND1 . HIS B 429 ? 0.1720 0.1547 0.2364 -0.0252 -0.0156 0.0293  421 HIS B ND1 
7924  C CD2 . HIS B 429 ? 0.1283 0.1282 0.2070 -0.0272 -0.0104 0.0354  421 HIS B CD2 
7925  C CE1 . HIS B 429 ? 0.1904 0.1705 0.2621 -0.0313 -0.0145 0.0310  421 HIS B CE1 
7926  N NE2 . HIS B 429 ? 0.1883 0.1792 0.2689 -0.0330 -0.0110 0.0348  421 HIS B NE2 
7927  N N   . GLY B 430 ? 0.1818 0.1742 0.1793 0.0212  0.0076  -0.0057 422 GLY B N   
7928  C CA  . GLY B 430 ? 0.1732 0.1668 0.1729 0.0242  0.0060  -0.0081 422 GLY B CA  
7929  C C   . GLY B 430 ? 0.1873 0.1759 0.1879 0.0246  0.0041  -0.0073 422 GLY B C   
7930  O O   . GLY B 430 ? 0.2025 0.1851 0.2010 0.0217  0.0037  -0.0047 422 GLY B O   
7931  N N   . GLY B 431 ? 0.1620 0.1529 0.1661 0.0279  0.0028  -0.0098 423 GLY B N   
7932  C CA  . GLY B 431 ? 0.1665 0.1528 0.1747 0.0290  0.0001  -0.0100 423 GLY B CA  
7933  C C   . GLY B 431 ? 0.1372 0.1233 0.1467 0.0303  -0.0019 -0.0077 423 GLY B C   
7934  O O   . GLY B 431 ? 0.1672 0.1510 0.1830 0.0324  -0.0048 -0.0090 423 GLY B O   
7935  N N   . VAL B 432 ? 0.2188 0.2076 0.2239 0.0293  -0.0006 -0.0048 424 VAL B N   
7936  C CA  . VAL B 432 ? 0.1626 0.1519 0.1692 0.0304  -0.0025 -0.0028 424 VAL B CA  
7937  C C   . VAL B 432 ? 0.1865 0.1838 0.1915 0.0312  0.0002  -0.0033 424 VAL B C   
7938  O O   . VAL B 432 ? 0.1676 0.1677 0.1685 0.0299  0.0028  -0.0031 424 VAL B O   
7939  C CB  . VAL B 432 ? 0.1939 0.1763 0.1958 0.0268  -0.0047 0.0028  424 VAL B CB  
7940  C CG1 . VAL B 432 ? 0.2221 0.1958 0.2254 0.0254  -0.0084 0.0042  424 VAL B CG1 
7941  C CG2 . VAL B 432 ? 0.2775 0.2603 0.2722 0.0230  -0.0014 0.0046  424 VAL B CG2 
7942  N N   . LYS B 433 ? 0.1507 0.1514 0.1599 0.0334  -0.0008 -0.0042 425 LYS B N   
7943  C CA  A LYS B 433 ? 0.1412 0.1491 0.1489 0.0336  0.0015  -0.0043 425 LYS B CA  
7944  C CA  B LYS B 433 ? 0.1394 0.1473 0.1471 0.0336  0.0016  -0.0043 425 LYS B CA  
7945  C C   . LYS B 433 ? 0.1337 0.1399 0.1414 0.0331  -0.0004 -0.0007 425 LYS B C   
7946  O O   . LYS B 433 ? 0.1369 0.1434 0.1514 0.0352  -0.0030 -0.0019 425 LYS B O   
7947  C CB  A LYS B 433 ? 0.1632 0.1786 0.1762 0.0359  0.0031  -0.0099 425 LYS B CB  
7948  C CB  B LYS B 433 ? 0.1659 0.1813 0.1788 0.0359  0.0031  -0.0099 425 LYS B CB  
7949  C CG  A LYS B 433 ? 0.1158 0.1341 0.1272 0.0357  0.0051  -0.0136 425 LYS B CG  
7950  C CG  B LYS B 433 ? 0.1511 0.1740 0.1617 0.0352  0.0058  -0.0099 425 LYS B CG  
7951  C CD  A LYS B 433 ? 0.1216 0.1487 0.1362 0.0365  0.0075  -0.0195 425 LYS B CD  
7952  C CD  B LYS B 433 ? 0.1332 0.1645 0.1477 0.0361  0.0082  -0.0161 425 LYS B CD  
7953  C CE  A LYS B 433 ? 0.1419 0.1753 0.1523 0.0349  0.0099  -0.0180 425 LYS B CE  
7954  C CE  B LYS B 433 ? 0.1458 0.1797 0.1556 0.0347  0.0101  -0.0185 425 LYS B CE  
7955  N NZ  A LYS B 433 ? 0.1502 0.1828 0.1518 0.0322  0.0104  -0.0133 425 LYS B NZ  
7956  N NZ  B LYS B 433 ? 0.1448 0.1788 0.1457 0.0319  0.0109  -0.0138 425 LYS B NZ  
7957  N N   . PRO B 434 ? 0.1460 0.1507 0.1475 0.0303  0.0005  0.0032  426 PRO B N   
7958  C CA  . PRO B 434 ? 0.1648 0.1675 0.1655 0.0291  -0.0017 0.0066  426 PRO B CA  
7959  C C   . PRO B 434 ? 0.1391 0.1484 0.1411 0.0299  -0.0001 0.0064  426 PRO B C   
7960  O O   . PRO B 434 ? 0.1277 0.1422 0.1280 0.0297  0.0032  0.0053  426 PRO B O   
7961  C CB  . PRO B 434 ? 0.1953 0.1933 0.1885 0.0249  -0.0007 0.0099  426 PRO B CB  
7962  C CG  . PRO B 434 ? 0.1891 0.1907 0.1810 0.0247  0.0031  0.0079  426 PRO B CG  
7963  C CD  . PRO B 434 ? 0.1845 0.1886 0.1806 0.0278  0.0031  0.0042  426 PRO B CD  
7964  N N   . PHE B 435 ? 0.1186 0.1273 0.1236 0.0303  -0.0032 0.0078  427 PHE B N   
7965  C CA  . PHE B 435 ? 0.1432 0.1567 0.1484 0.0299  -0.0022 0.0087  427 PHE B CA  
7966  C C   . PHE B 435 ? 0.1703 0.1788 0.1719 0.0272  -0.0054 0.0130  427 PHE B C   
7967  O O   . PHE B 435 ? 0.1443 0.1461 0.1448 0.0262  -0.0095 0.0152  427 PHE B O   
7968  C CB  . PHE B 435 ? 0.1449 0.1650 0.1590 0.0330  -0.0023 0.0049  427 PHE B CB  
7969  C CG  . PHE B 435 ? 0.1811 0.1986 0.2036 0.0351  -0.0077 0.0045  427 PHE B CG  
7970  C CD1 . PHE B 435 ? 0.1790 0.1952 0.2027 0.0344  -0.0113 0.0075  427 PHE B CD1 
7971  C CD2 . PHE B 435 ? 0.1243 0.1411 0.1549 0.0380  -0.0096 0.0007  427 PHE B CD2 
7972  C CE1 . PHE B 435 ? 0.1962 0.2097 0.2291 0.0365  -0.0176 0.0075  427 PHE B CE1 
7973  C CE2 . PHE B 435 ? 0.2198 0.2338 0.2606 0.0403  -0.0154 0.0002  427 PHE B CE2 
7974  C CZ  . PHE B 435 ? 0.1937 0.2059 0.2358 0.0396  -0.0199 0.0039  427 PHE B CZ  
7975  N N   . GLY B 436 ? 0.1307 0.1424 0.1298 0.0255  -0.0037 0.0143  428 GLY B N   
7976  C CA  . GLY B 436 ? 0.1352 0.1432 0.1303 0.0224  -0.0065 0.0178  428 GLY B CA  
7977  C C   . GLY B 436 ? 0.1156 0.1291 0.1131 0.0225  -0.0059 0.0178  428 GLY B C   
7978  O O   . GLY B 436 ? 0.1644 0.1830 0.1622 0.0227  -0.0017 0.0164  428 GLY B O   
7979  N N   . ALA B 437 ? 0.1198 0.1317 0.1189 0.0220  -0.0106 0.0197  429 ALA B N   
7980  C CA  . ALA B 437 ? 0.1239 0.1417 0.1278 0.0227  -0.0107 0.0191  429 ALA B CA  
7981  C C   . ALA B 437 ? 0.1344 0.1501 0.1319 0.0184  -0.0121 0.0221  429 ALA B C   
7982  O O   . ALA B 437 ? 0.1460 0.1554 0.1374 0.0152  -0.0159 0.0252  429 ALA B O   
7983  C CB  . ALA B 437 ? 0.1427 0.1622 0.1574 0.0264  -0.0155 0.0176  429 ALA B CB  
7984  N N   . THR B 438 ? 0.1163 0.1376 0.1152 0.0179  -0.0091 0.0211  430 THR B N   
7985  C CA  . THR B 438 ? 0.1190 0.1401 0.1145 0.0143  -0.0107 0.0229  430 THR B CA  
7986  C C   . THR B 438 ? 0.1537 0.1822 0.1564 0.0161  -0.0092 0.0210  430 THR B C   
7987  O O   . THR B 438 ? 0.1374 0.1709 0.1470 0.0194  -0.0071 0.0185  430 THR B O   
7988  C CB  . THR B 438 ? 0.1333 0.1517 0.1197 0.0096  -0.0070 0.0233  430 THR B CB  
7989  O OG1 . THR B 438 ? 0.1527 0.1713 0.1354 0.0056  -0.0083 0.0243  430 THR B OG1 
7990  C CG2 . THR B 438 ? 0.1129 0.1350 0.1013 0.0107  -0.0011 0.0211  430 THR B CG2 
7991  N N   . PHE B 439 ? 0.1516 0.1811 0.1526 0.0132  -0.0104 0.0220  431 PHE B N   
7992  C CA  . PHE B 439 ? 0.1496 0.1860 0.1568 0.0139  -0.0081 0.0202  431 PHE B CA  
7993  C C   . PHE B 439 ? 0.1063 0.1453 0.1123 0.0134  -0.0016 0.0190  431 PHE B C   
7994  O O   . PHE B 439 ? 0.1064 0.1418 0.1065 0.0112  0.0006  0.0195  431 PHE B O   
7995  C CB  . PHE B 439 ? 0.1410 0.1777 0.1462 0.0105  -0.0107 0.0214  431 PHE B CB  
7996  C CG  . PHE B 439 ? 0.1992 0.2345 0.2075 0.0109  -0.0183 0.0230  431 PHE B CG  
7997  C CD1 . PHE B 439 ? 0.1948 0.2273 0.2073 0.0140  -0.0230 0.0237  431 PHE B CD1 
7998  C CD2 . PHE B 439 ? 0.3161 0.3528 0.3240 0.0081  -0.0214 0.0238  431 PHE B CD2 
7999  C CE1 . PHE B 439 ? 0.2739 0.3044 0.2909 0.0145  -0.0312 0.0255  431 PHE B CE1 
8000  C CE2 . PHE B 439 ? 0.3421 0.3772 0.3534 0.0083  -0.0296 0.0258  431 PHE B CE2 
8001  C CZ  . PHE B 439 ? 0.3190 0.3507 0.3351 0.0116  -0.0349 0.0269  431 PHE B CZ  
8002  N N   . LEU B 440 ? 0.1158 0.1611 0.1280 0.0150  0.0011  0.0173  432 LEU B N   
8003  C CA  . LEU B 440 ? 0.1225 0.1694 0.1333 0.0139  0.0060  0.0172  432 LEU B CA  
8004  C C   . LEU B 440 ? 0.1044 0.1490 0.1118 0.0104  0.0073  0.0182  432 LEU B C   
8005  O O   . LEU B 440 ? 0.0980 0.1404 0.1032 0.0094  0.0098  0.0185  432 LEU B O   
8006  C CB  . LEU B 440 ? 0.1236 0.1778 0.1404 0.0145  0.0085  0.0157  432 LEU B CB  
8007  C CG  . LEU B 440 ? 0.1045 0.1599 0.1194 0.0126  0.0125  0.0168  432 LEU B CG  
8008  C CD1 . LEU B 440 ? 0.1297 0.1816 0.1401 0.0133  0.0135  0.0175  432 LEU B CD1 
8009  C CD2 . LEU B 440 ? 0.0951 0.1579 0.1146 0.0119  0.0151  0.0154  432 LEU B CD2 
8010  N N   . MET B 441 ? 0.1101 0.1552 0.1178 0.0084  0.0053  0.0182  433 MET B N   
8011  C CA  . MET B 441 ? 0.1062 0.1497 0.1116 0.0048  0.0070  0.0179  433 MET B CA  
8012  C C   . MET B 441 ? 0.1644 0.2026 0.1640 0.0031  0.0079  0.0176  433 MET B C   
8013  O O   . MET B 441 ? 0.1238 0.1609 0.1240 0.0012  0.0108  0.0164  433 MET B O   
8014  C CB  . MET B 441 ? 0.1082 0.1528 0.1133 0.0023  0.0042  0.0176  433 MET B CB  
8015  C CG  . MET B 441 ? 0.1138 0.1572 0.1168 -0.0020 0.0064  0.0161  433 MET B CG  
8016  S SD  . MET B 441 ? 0.1281 0.1746 0.1384 -0.0020 0.0106  0.0153  433 MET B SD  
8017  C CE  . MET B 441 ? 0.1140 0.1666 0.1301 -0.0012 0.0091  0.0156  433 MET B CE  
8018  N N   . PHE B 442 ? 0.1068 0.1415 0.1018 0.0035  0.0053  0.0184  434 PHE B N   
8019  C CA  . PHE B 442 ? 0.1677 0.1976 0.1567 0.0009  0.0063  0.0178  434 PHE B CA  
8020  C C   . PHE B 442 ? 0.1064 0.1350 0.0966 0.0033  0.0086  0.0175  434 PHE B C   
8021  O O   . PHE B 442 ? 0.1265 0.1515 0.1129 0.0014  0.0098  0.0165  434 PHE B O   
8022  C CB  . PHE B 442 ? 0.1858 0.2120 0.1683 -0.0010 0.0020  0.0195  434 PHE B CB  
8023  C CG  . PHE B 442 ? 0.2759 0.3036 0.2573 -0.0036 -0.0012 0.0202  434 PHE B CG  
8024  C CD1 . PHE B 442 ? 0.2762 0.3066 0.2584 -0.0067 0.0015  0.0180  434 PHE B CD1 
8025  C CD2 . PHE B 442 ? 0.2517 0.2784 0.2331 -0.0026 -0.0073 0.0227  434 PHE B CD2 
8026  C CE1 . PHE B 442 ? 0.3505 0.3828 0.3318 -0.0093 -0.0015 0.0183  434 PHE B CE1 
8027  C CE2 . PHE B 442 ? 0.3284 0.3566 0.3094 -0.0049 -0.0110 0.0235  434 PHE B CE2 
8028  C CZ  . PHE B 442 ? 0.2843 0.3156 0.2647 -0.0084 -0.0079 0.0212  434 PHE B CZ  
8029  N N   . SER B 443 ? 0.1242 0.1558 0.1193 0.0066  0.0096  0.0179  435 SER B N   
8030  C CA  . SER B 443 ? 0.1554 0.1862 0.1520 0.0077  0.0120  0.0176  435 SER B CA  
8031  C C   . SER B 443 ? 0.1395 0.1689 0.1378 0.0048  0.0143  0.0159  435 SER B C   
8032  O O   . SER B 443 ? 0.1219 0.1492 0.1213 0.0048  0.0155  0.0149  435 SER B O   
8033  C CB  . SER B 443 ? 0.1086 0.1434 0.1089 0.0099  0.0127  0.0186  435 SER B CB  
8034  O OG  . SER B 443 ? 0.1272 0.1649 0.1310 0.0083  0.0136  0.0190  435 SER B OG  
8035  N N   . GLU B 444 ? 0.1499 0.1808 0.1497 0.0022  0.0148  0.0149  436 GLU B N   
8036  C CA  . GLU B 444 ? 0.1105 0.1405 0.1140 -0.0006 0.0171  0.0121  436 GLU B CA  
8037  C C   . GLU B 444 ? 0.1689 0.1964 0.1685 -0.0039 0.0186  0.0089  436 GLU B C   
8038  O O   . GLU B 444 ? 0.2278 0.2545 0.2321 -0.0055 0.0210  0.0055  436 GLU B O   
8039  C CB  . GLU B 444 ? 0.1328 0.1655 0.1396 -0.0027 0.0175  0.0112  436 GLU B CB  
8040  C CG  . GLU B 444 ? 0.1120 0.1474 0.1233 -0.0004 0.0168  0.0141  436 GLU B CG  
8041  C CD  . GLU B 444 ? 0.1859 0.2234 0.2024 -0.0025 0.0175  0.0133  436 GLU B CD  
8042  O OE1 . GLU B 444 ? 0.1669 0.2046 0.1827 -0.0056 0.0181  0.0103  436 GLU B OE1 
8043  O OE2 . GLU B 444 ? 0.1773 0.2162 0.1980 -0.0017 0.0174  0.0157  436 GLU B OE2 
8044  N N   . TYR B 445 ? 0.1076 0.1336 0.0991 -0.0053 0.0169  0.0099  437 TYR B N   
8045  C CA  . TYR B 445 ? 0.1339 0.1571 0.1196 -0.0094 0.0183  0.0075  437 TYR B CA  
8046  C C   . TYR B 445 ? 0.1829 0.2037 0.1696 -0.0074 0.0192  0.0071  437 TYR B C   
8047  O O   . TYR B 445 ? 0.2047 0.2241 0.1898 -0.0110 0.0218  0.0037  437 TYR B O   
8048  C CB  . TYR B 445 ? 0.1330 0.1543 0.1092 -0.0120 0.0149  0.0099  437 TYR B CB  
8049  C CG  . TYR B 445 ? 0.1242 0.1471 0.0965 -0.0169 0.0144  0.0089  437 TYR B CG  
8050  C CD1 . TYR B 445 ? 0.1209 0.1475 0.0991 -0.0160 0.0147  0.0081  437 TYR B CD1 
8051  C CD2 . TYR B 445 ? 0.1402 0.1606 0.1021 -0.0231 0.0134  0.0088  437 TYR B CD2 
8052  C CE1 . TYR B 445 ? 0.1694 0.1977 0.1441 -0.0207 0.0140  0.0068  437 TYR B CE1 
8053  C CE2 . TYR B 445 ? 0.1527 0.1747 0.1097 -0.0284 0.0125  0.0078  437 TYR B CE2 
8054  C CZ  . TYR B 445 ? 0.1480 0.1741 0.1118 -0.0269 0.0128  0.0066  437 TYR B CZ  
8055  O OH  . TYR B 445 ? 0.1622 0.1900 0.1210 -0.0324 0.0118  0.0053  437 TYR B OH  
8056  N N   . GLU B 446 ? 0.1441 0.1648 0.1331 -0.0024 0.0174  0.0100  438 GLU B N   
8057  C CA  . GLU B 446 ? 0.1082 0.1269 0.0978 -0.0005 0.0178  0.0097  438 GLU B CA  
8058  C C   . GLU B 446 ? 0.1010 0.1211 0.0984 0.0027  0.0182  0.0099  438 GLU B C   
8059  O O   . GLU B 446 ? 0.1455 0.1646 0.1434 0.0052  0.0176  0.0106  438 GLU B O   
8060  C CB  . GLU B 446 ? 0.1301 0.1470 0.1149 0.0020  0.0149  0.0127  438 GLU B CB  
8061  C CG  . GLU B 446 ? 0.1314 0.1511 0.1185 0.0058  0.0126  0.0153  438 GLU B CG  
8062  C CD  . GLU B 446 ? 0.1919 0.2105 0.1775 0.0089  0.0100  0.0168  438 GLU B CD  
8063  O OE1 . GLU B 446 ? 0.1482 0.1635 0.1317 0.0089  0.0099  0.0164  438 GLU B OE1 
8064  O OE2 . GLU B 446 ? 0.1591 0.1804 0.1470 0.0113  0.0081  0.0179  438 GLU B OE2 
8065  N N   . ARG B 447 ? 0.1089 0.1310 0.1120 0.0023  0.0189  0.0094  439 ARG B N   
8066  C CA  . ARG B 447 ? 0.1323 0.1554 0.1414 0.0049  0.0178  0.0114  439 ARG B CA  
8067  C C   . ARG B 447 ? 0.1447 0.1658 0.1582 0.0059  0.0176  0.0102  439 ARG B C   
8068  O O   . ARG B 447 ? 0.1183 0.1393 0.1315 0.0084  0.0157  0.0129  439 ARG B O   
8069  C CB  . ARG B 447 ? 0.1222 0.1467 0.1375 0.0034  0.0182  0.0110  439 ARG B CB  
8070  C CG  . ARG B 447 ? 0.0949 0.1193 0.1163 0.0049  0.0163  0.0139  439 ARG B CG  
8071  C CD  . ARG B 447 ? 0.0949 0.1210 0.1108 0.0070  0.0147  0.0183  439 ARG B CD  
8072  N NE  . ARG B 447 ? 0.1580 0.1836 0.1778 0.0070  0.0127  0.0217  439 ARG B NE  
8073  C CZ  . ARG B 447 ? 0.1426 0.1704 0.1615 0.0061  0.0121  0.0249  439 ARG B CZ  
8074  N NH1 . ARG B 447 ? 0.1503 0.1816 0.1658 0.0059  0.0137  0.0246  439 ARG B NH1 
8075  N NH2 . ARG B 447 ? 0.1223 0.1487 0.1438 0.0051  0.0097  0.0286  439 ARG B NH2 
8076  N N   . ASN B 448 ? 0.0964 0.1164 0.1144 0.0036  0.0196  0.0057  440 ASN B N   
8077  C CA  . ASN B 448 ? 0.1159 0.1344 0.1406 0.0049  0.0189  0.0043  440 ASN B CA  
8078  C C   . ASN B 448 ? 0.1504 0.1675 0.1690 0.0064  0.0184  0.0051  440 ASN B C   
8079  O O   . ASN B 448 ? 0.1025 0.1188 0.1252 0.0083  0.0167  0.0055  440 ASN B O   
8080  C CB  . ASN B 448 ? 0.0963 0.1148 0.1301 0.0021  0.0216  -0.0020 440 ASN B CB  
8081  C CG  . ASN B 448 ? 0.0953 0.1127 0.1405 0.0039  0.0196  -0.0034 440 ASN B CG  
8082  O OD1 . ASN B 448 ? 0.1201 0.1372 0.1680 0.0033  0.0210  -0.0072 440 ASN B OD1 
8083  N ND2 . ASN B 448 ? 0.1203 0.1369 0.1721 0.0058  0.0159  0.0001  440 ASN B ND2 
8084  N N   . ALA B 449 ? 0.1131 0.1298 0.1227 0.0056  0.0192  0.0057  441 ALA B N   
8085  C CA  . ALA B 449 ? 0.1022 0.1174 0.1071 0.0073  0.0182  0.0067  441 ALA B CA  
8086  C C   . ALA B 449 ? 0.1011 0.1175 0.1047 0.0110  0.0156  0.0105  441 ALA B C   
8087  O O   . ALA B 449 ? 0.0968 0.1125 0.1001 0.0128  0.0144  0.0107  441 ALA B O   
8088  C CB  . ALA B 449 ? 0.1296 0.1430 0.1260 0.0053  0.0187  0.0070  441 ALA B CB  
8089  N N   . LEU B 450 ? 0.1071 0.1257 0.1095 0.0116  0.0148  0.0129  442 LEU B N   
8090  C CA  . LEU B 450 ? 0.0958 0.1168 0.0972 0.0138  0.0132  0.0158  442 LEU B CA  
8091  C C   . LEU B 450 ? 0.1297 0.1501 0.1356 0.0140  0.0116  0.0168  442 LEU B C   
8092  O O   . LEU B 450 ? 0.1364 0.1572 0.1403 0.0152  0.0100  0.0180  442 LEU B O   
8093  C CB  . LEU B 450 ? 0.0999 0.1239 0.1008 0.0133  0.0133  0.0176  442 LEU B CB  
8094  C CG  . LEU B 450 ? 0.2352 0.2609 0.2324 0.0140  0.0134  0.0177  442 LEU B CG  
8095  C CD1 . LEU B 450 ? 0.1965 0.2193 0.1910 0.0133  0.0133  0.0162  442 LEU B CD1 
8096  C CD2 . LEU B 450 ? 0.2015 0.2300 0.2004 0.0128  0.0138  0.0187  442 LEU B CD2 
8097  N N   . ARG B 451 ? 0.1217 0.1411 0.1344 0.0125  0.0115  0.0162  443 ARG B N   
8098  C CA  . ARG B 451 ? 0.0969 0.1150 0.1158 0.0127  0.0086  0.0176  443 ARG B CA  
8099  C C   . ARG B 451 ? 0.1182 0.1345 0.1391 0.0137  0.0077  0.0155  443 ARG B C   
8100  O O   . ARG B 451 ? 0.0990 0.1148 0.1206 0.0145  0.0044  0.0177  443 ARG B O   
8101  C CB  . ARG B 451 ? 0.1243 0.1413 0.1527 0.0112  0.0084  0.0164  443 ARG B CB  
8102  C CG  . ARG B 451 ? 0.1497 0.1646 0.1854 0.0113  0.0038  0.0195  443 ARG B CG  
8103  C CD  . ARG B 451 ? 0.1899 0.2033 0.2381 0.0102  0.0031  0.0175  443 ARG B CD  
8104  N NE  . ARG B 451 ? 0.1292 0.1400 0.1832 0.0100  -0.0025 0.0224  443 ARG B NE  
8105  C CZ  . ARG B 451 ? 0.1404 0.1484 0.2040 0.0107  -0.0070 0.0224  443 ARG B CZ  
8106  N NH1 . ARG B 451 ? 0.1033 0.1114 0.1727 0.0119  -0.0057 0.0169  443 ARG B NH1 
8107  N NH2 . ARG B 451 ? 0.1110 0.1159 0.1787 0.0099  -0.0132 0.0282  443 ARG B NH2 
8108  N N   . MET B 452 ? 0.0958 0.1113 0.1173 0.0131  0.0106  0.0112  444 MET B N   
8109  C CA  . MET B 452 ? 0.1352 0.1494 0.1596 0.0137  0.0102  0.0085  444 MET B CA  
8110  C C   . MET B 452 ? 0.1747 0.1891 0.1915 0.0155  0.0089  0.0105  444 MET B C   
8111  O O   . MET B 452 ? 0.1337 0.1475 0.1531 0.0164  0.0067  0.0102  444 MET B O   
8112  C CB  . MET B 452 ? 0.1170 0.1305 0.1426 0.0114  0.0142  0.0034  444 MET B CB  
8113  C CG  . MET B 452 ? 0.1058 0.1198 0.1417 0.0092  0.0159  -0.0007 444 MET B CG  
8114  S SD  . MET B 452 ? 0.1244 0.1377 0.1760 0.0107  0.0122  -0.0024 444 MET B SD  
8115  C CE  . MET B 452 ? 0.1274 0.1404 0.1803 0.0104  0.0138  -0.0070 444 MET B CE  
8116  N N   . ALA B 453 ? 0.0970 0.1126 0.1058 0.0160  0.0100  0.0120  445 ALA B N   
8117  C CA  . ALA B 453 ? 0.1027 0.1193 0.1060 0.0177  0.0090  0.0129  445 ALA B CA  
8118  C C   . ALA B 453 ? 0.1165 0.1348 0.1192 0.0180  0.0061  0.0158  445 ALA B C   
8119  O O   . ALA B 453 ? 0.1316 0.1500 0.1327 0.0186  0.0044  0.0155  445 ALA B O   
8120  C CB  . ALA B 453 ? 0.1210 0.1390 0.1186 0.0183  0.0103  0.0132  445 ALA B CB  
8121  N N   . ALA B 454 ? 0.1349 0.1544 0.1384 0.0168  0.0052  0.0187  446 ALA B N   
8122  C CA  . ALA B 454 ? 0.1323 0.1529 0.1339 0.0157  0.0020  0.0225  446 ALA B CA  
8123  C C   . ALA B 454 ? 0.1078 0.1255 0.1155 0.0157  -0.0021 0.0231  446 ALA B C   
8124  O O   . ALA B 454 ? 0.1468 0.1648 0.1512 0.0151  -0.0052 0.0250  446 ALA B O   
8125  C CB  . ALA B 454 ? 0.1094 0.1310 0.1112 0.0139  0.0018  0.0258  446 ALA B CB  
8126  N N   . LEU B 455 ? 0.1046 0.1198 0.1218 0.0159  -0.0021 0.0210  447 LEU B N   
8127  C CA  . LEU B 455 ? 0.1062 0.1188 0.1326 0.0161  -0.0062 0.0206  447 LEU B CA  
8128  C C   . LEU B 455 ? 0.1675 0.1801 0.1928 0.0174  -0.0063 0.0177  447 LEU B C   
8129  O O   . LEU B 455 ? 0.1367 0.1483 0.1648 0.0174  -0.0111 0.0191  447 LEU B O   
8130  C CB  . LEU B 455 ? 0.1033 0.1145 0.1419 0.0160  -0.0049 0.0169  447 LEU B CB  
8131  C CG  . LEU B 455 ? 0.1043 0.1133 0.1567 0.0165  -0.0088 0.0148  447 LEU B CG  
8132  C CD1 . LEU B 455 ? 0.1628 0.1696 0.2179 0.0161  -0.0165 0.0208  447 LEU B CD1 
8133  C CD2 . LEU B 455 ? 0.1803 0.1892 0.2453 0.0158  -0.0061 0.0096  447 LEU B CD2 
8134  N N   . MET B 456 ? 0.1028 0.1162 0.1243 0.0180  -0.0017 0.0140  448 MET B N   
8135  C CA  . MET B 456 ? 0.1202 0.1333 0.1406 0.0190  -0.0015 0.0112  448 MET B CA  
8136  C C   . MET B 456 ? 0.1412 0.1561 0.1527 0.0194  -0.0033 0.0133  448 MET B C   
8137  O O   . MET B 456 ? 0.1343 0.1490 0.1454 0.0201  -0.0040 0.0112  448 MET B O   
8138  C CB  . MET B 456 ? 0.1269 0.1394 0.1454 0.0188  0.0034  0.0073  448 MET B CB  
8139  C CG  . MET B 456 ? 0.0984 0.1098 0.1258 0.0173  0.0057  0.0034  448 MET B CG  
8140  S SD  . MET B 456 ? 0.1346 0.1446 0.1581 0.0155  0.0106  -0.0008 448 MET B SD  
8141  C CE  . MET B 456 ? 0.1235 0.1337 0.1433 0.0132  0.0140  -0.0005 448 MET B CE  
8142  N N   . LYS B 457 ? 0.1544 0.1714 0.1589 0.0185  -0.0035 0.0167  449 LYS B N   
8143  C CA  . LYS B 457 ? 0.1496 0.1697 0.1455 0.0180  -0.0041 0.0176  449 LYS B CA  
8144  C C   . LYS B 457 ? 0.1806 0.2016 0.1735 0.0197  -0.0006 0.0134  449 LYS B C   
8145  O O   . LYS B 457 ? 0.1545 0.1768 0.1443 0.0199  -0.0014 0.0116  449 LYS B O   
8146  C CB  . LYS B 457 ? 0.1549 0.1745 0.1503 0.0168  -0.0093 0.0196  449 LYS B CB  
8147  C CG  . LYS B 457 ? 0.2002 0.2178 0.1994 0.0149  -0.0143 0.0246  449 LYS B CG  
8148  C CD  . LYS B 457 ? 0.3642 0.3819 0.3594 0.0126  -0.0204 0.0281  449 LYS B CD  
8149  C CE  . LYS B 457 ? 0.4920 0.5137 0.4736 0.0092  -0.0194 0.0304  449 LYS B CE  
8150  N NZ  . LYS B 457 ? 0.4870 0.5101 0.4614 0.0066  -0.0236 0.0316  449 LYS B NZ  
8151  N N   . ILE B 458 ? 0.1513 0.1714 0.1453 0.0206  0.0027  0.0118  450 ILE B N   
8152  C CA  . ILE B 458 ? 0.1560 0.1760 0.1480 0.0221  0.0051  0.0088  450 ILE B CA  
8153  C C   . ILE B 458 ? 0.1688 0.1920 0.1576 0.0223  0.0068  0.0093  450 ILE B C   
8154  O O   . ILE B 458 ? 0.1377 0.1628 0.1257 0.0211  0.0069  0.0118  450 ILE B O   
8155  C CB  . ILE B 458 ? 0.1707 0.1866 0.1663 0.0222  0.0066  0.0069  450 ILE B CB  
8156  C CG1 . ILE B 458 ? 0.1340 0.1491 0.1316 0.0209  0.0078  0.0084  450 ILE B CG1 
8157  C CG2 . ILE B 458 ? 0.1509 0.1648 0.1511 0.0218  0.0053  0.0052  450 ILE B CG2 
8158  C CD1 . ILE B 458 ? 0.1985 0.2101 0.1979 0.0195  0.0099  0.0063  450 ILE B CD1 
8159  N N   . ASN B 459 ? 0.1266 0.1501 0.1148 0.0238  0.0081  0.0065  451 ASN B N   
8160  C CA  . ASN B 459 ? 0.1149 0.1426 0.1020 0.0244  0.0094  0.0056  451 ASN B CA  
8161  C C   . ASN B 459 ? 0.1126 0.1383 0.1025 0.0258  0.0099  0.0048  451 ASN B C   
8162  O O   . ASN B 459 ? 0.1575 0.1852 0.1494 0.0274  0.0101  0.0021  451 ASN B O   
8163  C CB  . ASN B 459 ? 0.1726 0.2046 0.1581 0.0246  0.0099  0.0021  451 ASN B CB  
8164  C CG  . ASN B 459 ? 0.1845 0.2135 0.1723 0.0264  0.0093  -0.0013 451 ASN B CG  
8165  O OD1 . ASN B 459 ? 0.1473 0.1709 0.1374 0.0271  0.0086  -0.0006 451 ASN B OD1 
8166  N ND2 . ASN B 459 ? 0.1928 0.2257 0.1800 0.0266  0.0099  -0.0053 451 ASN B ND2 
8167  N N   . PRO B 460 ? 0.1473 0.1691 0.1377 0.0250  0.0097  0.0071  452 PRO B N   
8168  C CA  . PRO B 460 ? 0.1289 0.1492 0.1206 0.0256  0.0092  0.0074  452 PRO B CA  
8169  C C   . PRO B 460 ? 0.1501 0.1757 0.1428 0.0259  0.0099  0.0076  452 PRO B C   
8170  O O   . PRO B 460 ? 0.1464 0.1758 0.1377 0.0247  0.0110  0.0085  452 PRO B O   
8171  C CB  . PRO B 460 ? 0.1736 0.1897 0.1640 0.0233  0.0093  0.0095  452 PRO B CB  
8172  C CG  . PRO B 460 ? 0.1173 0.1351 0.1080 0.0221  0.0102  0.0104  452 PRO B CG  
8173  C CD  . PRO B 460 ? 0.1075 0.1271 0.0980 0.0231  0.0097  0.0091  452 PRO B CD  
8174  N N   . VAL B 461 ? 0.1483 0.1739 0.1440 0.0271  0.0088  0.0069  453 VAL B N   
8175  C CA  . VAL B 461 ? 0.1341 0.1654 0.1328 0.0276  0.0095  0.0061  453 VAL B CA  
8176  C C   . VAL B 461 ? 0.1419 0.1709 0.1410 0.0268  0.0080  0.0087  453 VAL B C   
8177  O O   . VAL B 461 ? 0.1456 0.1701 0.1458 0.0273  0.0051  0.0094  453 VAL B O   
8178  C CB  . VAL B 461 ? 0.1347 0.1695 0.1393 0.0301  0.0091  0.0016  453 VAL B CB  
8179  C CG1 . VAL B 461 ? 0.1204 0.1618 0.1296 0.0302  0.0102  -0.0000 453 VAL B CG1 
8180  C CG2 . VAL B 461 ? 0.1615 0.1992 0.1648 0.0302  0.0110  -0.0017 453 VAL B CG2 
8181  N N   . PHE B 462 ? 0.1038 0.1355 0.1017 0.0251  0.0094  0.0105  454 PHE B N   
8182  C CA  . PHE B 462 ? 0.1077 0.1379 0.1056 0.0237  0.0083  0.0126  454 PHE B CA  
8183  C C   . PHE B 462 ? 0.1248 0.1603 0.1278 0.0249  0.0079  0.0112  454 PHE B C   
8184  O O   . PHE B 462 ? 0.1387 0.1801 0.1430 0.0245  0.0104  0.0101  454 PHE B O   
8185  C CB  . PHE B 462 ? 0.1418 0.1716 0.1370 0.0211  0.0100  0.0147  454 PHE B CB  
8186  C CG  . PHE B 462 ? 0.1453 0.1708 0.1379 0.0201  0.0105  0.0150  454 PHE B CG  
8187  C CD1 . PHE B 462 ? 0.1470 0.1676 0.1375 0.0184  0.0098  0.0152  454 PHE B CD1 
8188  C CD2 . PHE B 462 ? 0.1302 0.1567 0.1225 0.0202  0.0114  0.0148  454 PHE B CD2 
8189  C CE1 . PHE B 462 ? 0.1600 0.1774 0.1494 0.0171  0.0109  0.0145  454 PHE B CE1 
8190  C CE2 . PHE B 462 ? 0.0984 0.1213 0.0903 0.0195  0.0115  0.0146  454 PHE B CE2 
8191  C CZ  . PHE B 462 ? 0.1144 0.1331 0.1055 0.0180  0.0116  0.0140  454 PHE B CZ  
8192  N N   . VAL B 463 ? 0.1537 0.1871 0.1598 0.0258  0.0045  0.0114  455 VAL B N   
8193  C CA  . VAL B 463 ? 0.1445 0.1828 0.1581 0.0274  0.0032  0.0094  455 VAL B CA  
8194  C C   . VAL B 463 ? 0.1263 0.1645 0.1391 0.0254  0.0019  0.0119  455 VAL B C   
8195  O O   . VAL B 463 ? 0.1183 0.1509 0.1260 0.0234  -0.0002 0.0149  455 VAL B O   
8196  C CB  . VAL B 463 ? 0.1247 0.1605 0.1448 0.0303  -0.0012 0.0077  455 VAL B CB  
8197  C CG1 . VAL B 463 ? 0.1243 0.1653 0.1550 0.0322  -0.0034 0.0051  455 VAL B CG1 
8198  C CG2 . VAL B 463 ? 0.1280 0.1647 0.1499 0.0322  0.0006  0.0042  455 VAL B CG2 
8199  N N   . PHE B 464 ? 0.1216 0.1665 0.1392 0.0254  0.0035  0.0104  456 PHE B N   
8200  C CA  . PHE B 464 ? 0.1164 0.1621 0.1341 0.0235  0.0025  0.0122  456 PHE B CA  
8201  C C   . PHE B 464 ? 0.1016 0.1531 0.1293 0.0253  0.0007  0.0095  456 PHE B C   
8202  O O   . PHE B 464 ? 0.1534 0.2116 0.1870 0.0265  0.0036  0.0056  456 PHE B O   
8203  C CB  . PHE B 464 ? 0.0987 0.1464 0.1123 0.0207  0.0067  0.0135  456 PHE B CB  
8204  C CG  . PHE B 464 ? 0.1665 0.2090 0.1731 0.0191  0.0080  0.0155  456 PHE B CG  
8205  C CD1 . PHE B 464 ? 0.1415 0.1785 0.1438 0.0172  0.0064  0.0173  456 PHE B CD1 
8206  C CD2 . PHE B 464 ? 0.1569 0.2002 0.1615 0.0192  0.0106  0.0153  456 PHE B CD2 
8207  C CE1 . PHE B 464 ? 0.0999 0.1328 0.0977 0.0156  0.0079  0.0179  456 PHE B CE1 
8208  C CE2 . PHE B 464 ? 0.1264 0.1650 0.1266 0.0181  0.0112  0.0166  456 PHE B CE2 
8209  C CZ  . PHE B 464 ? 0.0980 0.1316 0.0957 0.0165  0.0102  0.0175  456 PHE B CZ  
8210  N N   . THR B 465 ? 0.1256 0.1750 0.1555 0.0250  -0.0041 0.0111  457 THR B N   
8211  C CA  . THR B 465 ? 0.1395 0.1946 0.1802 0.0266  -0.0064 0.0085  457 THR B CA  
8212  C C   . THR B 465 ? 0.1239 0.1811 0.1630 0.0237  -0.0060 0.0101  457 THR B C   
8213  O O   . THR B 465 ? 0.1159 0.1704 0.1462 0.0207  -0.0035 0.0128  457 THR B O   
8214  C CB  . THR B 465 ? 0.1291 0.1799 0.1760 0.0290  -0.0141 0.0089  457 THR B CB  
8215  O OG1 . THR B 465 ? 0.1497 0.1930 0.1879 0.0261  -0.0186 0.0142  457 THR B OG1 
8216  C CG2 . THR B 465 ? 0.1520 0.1998 0.2006 0.0316  -0.0144 0.0072  457 THR B CG2 
8217  N N   . HIS B 466 ? 0.1042 0.1666 0.1531 0.0247  -0.0083 0.0080  458 HIS B N   
8218  C CA  . HIS B 466 ? 0.1325 0.1970 0.1808 0.0220  -0.0085 0.0092  458 HIS B CA  
8219  C C   . HIS B 466 ? 0.1211 0.1886 0.1642 0.0192  -0.0015 0.0094  458 HIS B C   
8220  O O   . HIS B 466 ? 0.1067 0.1707 0.1424 0.0162  -0.0007 0.0122  458 HIS B O   
8221  C CB  . HIS B 466 ? 0.1556 0.2126 0.1961 0.0196  -0.0140 0.0136  458 HIS B CB  
8222  C CG  . HIS B 466 ? 0.2297 0.2835 0.2755 0.0213  -0.0225 0.0147  458 HIS B CG  
8223  N ND1 . HIS B 466 ? 0.2441 0.2939 0.2924 0.0241  -0.0258 0.0148  458 HIS B ND1 
8224  C CD2 . HIS B 466 ? 0.2700 0.3236 0.3196 0.0205  -0.0291 0.0160  458 HIS B CD2 
8225  C CE1 . HIS B 466 ? 0.3040 0.3506 0.3578 0.0250  -0.0345 0.0164  458 HIS B CE1 
8226  N NE2 . HIS B 466 ? 0.2257 0.2746 0.2801 0.0227  -0.0369 0.0174  458 HIS B NE2 
8227  N N   . ASP B 467 ? 0.0979 0.1718 0.1453 0.0197  0.0033  0.0062  459 ASP B N   
8228  C CA  . ASP B 467 ? 0.0961 0.1709 0.1371 0.0170  0.0091  0.0074  459 ASP B CA  
8229  C C   . ASP B 467 ? 0.1240 0.2033 0.1667 0.0138  0.0118  0.0077  459 ASP B C   
8230  O O   . ASP B 467 ? 0.1566 0.2360 0.1945 0.0111  0.0157  0.0094  459 ASP B O   
8231  C CB  . ASP B 467 ? 0.0959 0.1751 0.1383 0.0178  0.0130  0.0043  459 ASP B CB  
8232  C CG  . ASP B 467 ? 0.1636 0.2528 0.2159 0.0175  0.0157  -0.0008 459 ASP B CG  
8233  O OD1 . ASP B 467 ? 0.1460 0.2382 0.2078 0.0190  0.0127  -0.0031 459 ASP B OD1 
8234  O OD2 . ASP B 467 ? 0.1627 0.2570 0.2133 0.0153  0.0209  -0.0028 459 ASP B OD2 
8235  N N   . SER B 468 ? 0.1061 0.1887 0.1558 0.0138  0.0093  0.0063  460 SER B N   
8236  C CA  . SER B 468 ? 0.0950 0.1824 0.1471 0.0105  0.0123  0.0062  460 SER B CA  
8237  C C   . SER B 468 ? 0.1169 0.2054 0.1747 0.0105  0.0080  0.0057  460 SER B C   
8238  O O   . SER B 468 ? 0.1182 0.2029 0.1763 0.0124  0.0023  0.0063  460 SER B O   
8239  C CB  . SER B 468 ? 0.0950 0.1912 0.1529 0.0095  0.0173  0.0024  460 SER B CB  
8240  O OG  . SER B 468 ? 0.0950 0.1978 0.1651 0.0118  0.0154  -0.0025 460 SER B OG  
8241  N N   . ILE B 469 ? 0.0952 0.1888 0.1571 0.0078  0.0104  0.0048  461 ILE B N   
8242  C CA  . ILE B 469 ? 0.1111 0.2076 0.1804 0.0077  0.0065  0.0033  461 ILE B CA  
8243  C C   . ILE B 469 ? 0.2100 0.3109 0.2904 0.0114  0.0025  -0.0005 461 ILE B C   
8244  O O   . ILE B 469 ? 0.1452 0.2466 0.2315 0.0121  -0.0034 -0.0009 461 ILE B O   
8245  C CB  . ILE B 469 ? 0.1119 0.2143 0.1853 0.0041  0.0106  0.0023  461 ILE B CB  
8246  C CG1 . ILE B 469 ? 0.0980 0.2078 0.1757 0.0030  0.0166  -0.0006 461 ILE B CG1 
8247  C CG2 . ILE B 469 ? 0.0955 0.1920 0.1600 0.0007  0.0125  0.0062  461 ILE B CG2 
8248  C CD1 . ILE B 469 ? 0.0996 0.2165 0.1834 -0.0010 0.0204  -0.0023 461 ILE B CD1 
8249  N N   . GLY B 470 ? 0.0961 0.2002 0.1804 0.0136  0.0049  -0.0035 462 GLY B N   
8250  C CA  . GLY B 470 ? 0.1067 0.2144 0.2037 0.0176  0.0007  -0.0078 462 GLY B CA  
8251  C C   . GLY B 470 ? 0.1002 0.2000 0.1960 0.0203  -0.0082 -0.0048 462 GLY B C   
8252  O O   . GLY B 470 ? 0.1050 0.2067 0.2131 0.0235  -0.0139 -0.0075 462 GLY B O   
8253  N N   . LEU B 471 ? 0.1016 0.1924 0.1833 0.0187  -0.0098 0.0008  463 LEU B N   
8254  C CA  . LEU B 471 ? 0.1123 0.1953 0.1909 0.0197  -0.0182 0.0042  463 LEU B CA  
8255  C C   . LEU B 471 ? 0.1504 0.2342 0.2331 0.0183  -0.0246 0.0052  463 LEU B C   
8256  O O   . LEU B 471 ? 0.1285 0.2075 0.2124 0.0192  -0.0333 0.0075  463 LEU B O   
8257  C CB  . LEU B 471 ? 0.1078 0.1820 0.1703 0.0174  -0.0172 0.0090  463 LEU B CB  
8258  C CG  . LEU B 471 ? 0.1463 0.2179 0.1981 0.0129  -0.0142 0.0115  463 LEU B CG  
8259  C CD1 . LEU B 471 ? 0.1133 0.1818 0.1616 0.0101  -0.0206 0.0138  463 LEU B CD1 
8260  C CD2 . LEU B 471 ? 0.1680 0.2335 0.2084 0.0118  -0.0106 0.0137  463 LEU B CD2 
8261  N N   . GLY B 472 ? 0.1630 0.2522 0.2475 0.0157  -0.0210 0.0038  464 GLY B N   
8262  C CA  . GLY B 472 ? 0.1388 0.2310 0.2305 0.0147  -0.0268 0.0032  464 GLY B CA  
8263  C C   . GLY B 472 ? 0.1410 0.2267 0.2203 0.0106  -0.0308 0.0078  464 GLY B C   
8264  O O   . GLY B 472 ? 0.1162 0.2001 0.1856 0.0071  -0.0255 0.0089  464 GLY B O   
8265  N N   . GLU B 473 ? 0.1229 0.2052 0.2034 0.0105  -0.0407 0.0100  465 GLU B N   
8266  C CA  . GLU B 473 ? 0.1495 0.2291 0.2217 0.0057  -0.0451 0.0127  465 GLU B CA  
8267  C C   . GLU B 473 ? 0.1596 0.2316 0.2133 0.0011  -0.0426 0.0161  465 GLU B C   
8268  O O   . GLU B 473 ? 0.1754 0.2470 0.2218 -0.0038 -0.0428 0.0165  465 GLU B O   
8269  C CB  . GLU B 473 ? 0.1376 0.2149 0.2151 0.0062  -0.0573 0.0149  465 GLU B CB  
8270  C CG  . GLU B 473 ? 0.1476 0.2336 0.2453 0.0096  -0.0608 0.0106  465 GLU B CG  
8271  C CD  . GLU B 473 ? 0.1551 0.2443 0.2687 0.0157  -0.0614 0.0071  465 GLU B CD  
8272  O OE1 . GLU B 473 ? 0.1459 0.2329 0.2557 0.0177  -0.0559 0.0069  465 GLU B OE1 
8273  O OE2 . GLU B 473 ? 0.1492 0.2438 0.2805 0.0186  -0.0673 0.0040  465 GLU B OE2 
8274  N N   . ASP B 474 ? 0.1801 0.2468 0.2268 0.0023  -0.0402 0.0178  466 ASP B N   
8275  C CA  . ASP B 474 ? 0.1770 0.2373 0.2076 -0.0023 -0.0374 0.0200  466 ASP B CA  
8276  C C   . ASP B 474 ? 0.1953 0.2587 0.2231 -0.0052 -0.0292 0.0175  466 ASP B C   
8277  O O   . ASP B 474 ? 0.2113 0.2713 0.2283 -0.0102 -0.0278 0.0178  466 ASP B O   
8278  C CB  . ASP B 474 ? 0.1331 0.1883 0.1589 -0.0001 -0.0352 0.0215  466 ASP B CB  
8279  C CG  . ASP B 474 ? 0.2880 0.3367 0.3109 0.0001  -0.0441 0.0254  466 ASP B CG  
8280  O OD1 . ASP B 474 ? 0.3373 0.3843 0.3594 -0.0023 -0.0525 0.0278  466 ASP B OD1 
8281  O OD2 . ASP B 474 ? 0.2813 0.3261 0.3027 0.0025  -0.0432 0.0263  466 ASP B OD2 
8282  N N   . GLY B 475 ? 0.1833 0.2529 0.2208 -0.0026 -0.0238 0.0146  467 GLY B N   
8283  C CA  . GLY B 475 ? 0.1184 0.1909 0.1559 -0.0056 -0.0180 0.0125  467 GLY B CA  
8284  C C   . GLY B 475 ? 0.1144 0.1841 0.1465 -0.0064 -0.0108 0.0124  467 GLY B C   
8285  O O   . GLY B 475 ? 0.1129 0.1793 0.1418 -0.0041 -0.0094 0.0136  467 GLY B O   
8286  N N   . PRO B 476 ? 0.1131 0.1838 0.1450 -0.0096 -0.0067 0.0107  468 PRO B N   
8287  C CA  . PRO B 476 ? 0.1417 0.2107 0.1731 -0.0096 -0.0003 0.0105  468 PRO B CA  
8288  C C   . PRO B 476 ? 0.1557 0.2185 0.1784 -0.0105 0.0010  0.0111  468 PRO B C   
8289  O O   . PRO B 476 ? 0.1217 0.1828 0.1450 -0.0091 0.0050  0.0115  468 PRO B O   
8290  C CB  . PRO B 476 ? 0.1190 0.1902 0.1540 -0.0132 0.0024  0.0083  468 PRO B CB  
8291  C CG  . PRO B 476 ? 0.1530 0.2254 0.1858 -0.0162 -0.0025 0.0070  468 PRO B CG  
8292  C CD  . PRO B 476 ? 0.1154 0.1896 0.1503 -0.0129 -0.0080 0.0088  468 PRO B CD  
8293  N N   . THR B 477 ? 0.1163 0.1757 0.1307 -0.0132 -0.0023 0.0112  469 THR B N   
8294  C CA  . THR B 477 ? 0.1390 0.1932 0.1458 -0.0144 -0.0004 0.0113  469 THR B CA  
8295  C C   . THR B 477 ? 0.1731 0.2251 0.1794 -0.0100 -0.0012 0.0138  469 THR B C   
8296  O O   . THR B 477 ? 0.1609 0.2093 0.1635 -0.0098 0.0015  0.0138  469 THR B O   
8297  C CB  . THR B 477 ? 0.1451 0.1962 0.1415 -0.0196 -0.0033 0.0109  469 THR B CB  
8298  O OG1 . THR B 477 ? 0.1318 0.1813 0.1249 -0.0186 -0.0101 0.0144  469 THR B OG1 
8299  C CG2 . THR B 477 ? 0.1300 0.1838 0.1260 -0.0247 -0.0029 0.0077  469 THR B CG2 
8300  N N   . HIS B 478 ? 0.1150 0.1694 0.1259 -0.0064 -0.0050 0.0154  470 HIS B N   
8301  C CA  . HIS B 478 ? 0.1136 0.1663 0.1252 -0.0023 -0.0062 0.0170  470 HIS B CA  
8302  C C   . HIS B 478 ? 0.1352 0.1927 0.1553 0.0016  -0.0030 0.0161  470 HIS B C   
8303  O O   . HIS B 478 ? 0.1355 0.1918 0.1555 0.0045  -0.0021 0.0166  470 HIS B O   
8304  C CB  . HIS B 478 ? 0.1570 0.2082 0.1683 -0.0014 -0.0136 0.0188  470 HIS B CB  
8305  C CG  . HIS B 478 ? 0.2348 0.2796 0.2349 -0.0054 -0.0171 0.0209  470 HIS B CG  
8306  N ND1 . HIS B 478 ? 0.2777 0.3210 0.2697 -0.0112 -0.0154 0.0200  470 HIS B ND1 
8307  C CD2 . HIS B 478 ? 0.2678 0.3073 0.2633 -0.0051 -0.0221 0.0238  470 HIS B CD2 
8308  C CE1 . HIS B 478 ? 0.3123 0.3501 0.2940 -0.0149 -0.0187 0.0221  470 HIS B CE1 
8309  N NE2 . HIS B 478 ? 0.2814 0.3162 0.2647 -0.0113 -0.0232 0.0250  470 HIS B NE2 
8310  N N   . GLN B 479 ? 0.1229 0.1860 0.1498 0.0012  -0.0013 0.0148  471 GLN B N   
8311  C CA  . GLN B 479 ? 0.1008 0.1693 0.1350 0.0036  0.0020  0.0137  471 GLN B CA  
8312  C C   . GLN B 479 ? 0.0981 0.1650 0.1294 0.0029  0.0072  0.0146  471 GLN B C   
8313  O O   . GLN B 479 ? 0.1174 0.1833 0.1482 0.0002  0.0095  0.0149  471 GLN B O   
8314  C CB  . GLN B 479 ? 0.1002 0.1751 0.1423 0.0025  0.0022  0.0120  471 GLN B CB  
8315  C CG  . GLN B 479 ? 0.1029 0.1804 0.1506 0.0038  -0.0038 0.0109  471 GLN B CG  
8316  C CD  . GLN B 479 ? 0.1032 0.1859 0.1572 0.0016  -0.0043 0.0093  471 GLN B CD  
8317  O OE1 . GLN B 479 ? 0.1464 0.2292 0.1988 -0.0014 -0.0008 0.0093  471 GLN B OE1 
8318  N NE2 . GLN B 479 ? 0.1196 0.2063 0.1819 0.0032  -0.0093 0.0077  471 GLN B NE2 
8319  N N   . PRO B 480 ? 0.1197 0.1861 0.1499 0.0052  0.0088  0.0150  472 PRO B N   
8320  C CA  . PRO B 480 ? 0.1100 0.1746 0.1373 0.0043  0.0126  0.0164  472 PRO B CA  
8321  C C   . PRO B 480 ? 0.0951 0.1643 0.1266 0.0021  0.0157  0.0167  472 PRO B C   
8322  O O   . PRO B 480 ? 0.1178 0.1933 0.1546 0.0022  0.0163  0.0149  472 PRO B O   
8323  C CB  . PRO B 480 ? 0.1192 0.1836 0.1447 0.0070  0.0129  0.0163  472 PRO B CB  
8324  C CG  . PRO B 480 ? 0.1364 0.1996 0.1625 0.0095  0.0088  0.0152  472 PRO B CG  
8325  C CD  . PRO B 480 ? 0.1255 0.1924 0.1571 0.0086  0.0064  0.0141  472 PRO B CD  
8326  N N   . ILE B 481 ? 0.1488 0.2148 0.1787 -0.0002 0.0174  0.0187  473 ILE B N   
8327  C CA  . ILE B 481 ? 0.0966 0.1655 0.1294 -0.0032 0.0199  0.0202  473 ILE B CA  
8328  C C   . ILE B 481 ? 0.0983 0.1636 0.1272 -0.0041 0.0210  0.0233  473 ILE B C   
8329  O O   . ILE B 481 ? 0.1157 0.1843 0.1429 -0.0053 0.0228  0.0245  473 ILE B O   
8330  C CB  . ILE B 481 ? 0.0970 0.1647 0.1337 -0.0059 0.0196  0.0201  473 ILE B CB  
8331  C CG1 . ILE B 481 ? 0.0964 0.1678 0.1364 -0.0055 0.0179  0.0172  473 ILE B CG1 
8332  C CG2 . ILE B 481 ? 0.1214 0.1909 0.1609 -0.0094 0.0218  0.0224  473 ILE B CG2 
8333  C CD1 . ILE B 481 ? 0.1263 0.2053 0.1711 -0.0053 0.0187  0.0156  473 ILE B CD1 
8334  N N   . GLU B 482 ? 0.1069 0.1658 0.1345 -0.0038 0.0197  0.0244  474 GLU B N   
8335  C CA  . GLU B 482 ? 0.1451 0.1998 0.1708 -0.0046 0.0194  0.0275  474 GLU B CA  
8336  C C   . GLU B 482 ? 0.1543 0.2066 0.1752 -0.0018 0.0187  0.0272  474 GLU B C   
8337  O O   . GLU B 482 ? 0.1108 0.1600 0.1298 -0.0023 0.0180  0.0299  474 GLU B O   
8338  C CB  . GLU B 482 ? 0.1006 0.1500 0.1312 -0.0062 0.0183  0.0281  474 GLU B CB  
8339  C CG  . GLU B 482 ? 0.0983 0.1443 0.1298 -0.0046 0.0177  0.0245  474 GLU B CG  
8340  C CD  . GLU B 482 ? 0.1437 0.1924 0.1764 -0.0053 0.0180  0.0211  474 GLU B CD  
8341  O OE1 . GLU B 482 ? 0.1258 0.1793 0.1575 -0.0050 0.0181  0.0208  474 GLU B OE1 
8342  O OE2 . GLU B 482 ? 0.1332 0.1795 0.1681 -0.0064 0.0181  0.0181  474 GLU B OE2 
8343  N N   . GLN B 483 ? 0.1484 0.1891 0.1390 -0.0155 0.0044  -0.0055 475 GLN B N   
8344  C CA  . GLN B 483 ? 0.1511 0.1846 0.1411 -0.0090 0.0037  -0.0032 475 GLN B CA  
8345  C C   . GLN B 483 ? 0.1473 0.1843 0.1441 -0.0027 0.0025  -0.0005 475 GLN B C   
8346  O O   . GLN B 483 ? 0.1227 0.1527 0.1218 -0.0002 0.0046  0.0010  475 GLN B O   
8347  C CB  . GLN B 483 ? 0.1304 0.1665 0.1144 -0.0065 -0.0012 -0.0026 475 GLN B CB  
8348  C CG  . GLN B 483 ? 0.1254 0.1538 0.0995 -0.0122 0.0006  -0.0047 475 GLN B CG  
8349  C CD  . GLN B 483 ? 0.1827 0.2167 0.1536 -0.0208 0.0010  -0.0084 475 GLN B CD  
8350  O OE1 . GLN B 483 ? 0.1307 0.1789 0.1055 -0.0216 -0.0032 -0.0085 475 GLN B OE1 
8351  N NE2 . GLN B 483 ? 0.1650 0.1878 0.1293 -0.0279 0.0069  -0.0121 475 GLN B NE2 
8352  N N   . THR B 484 ? 0.0999 0.1488 0.1000 -0.0004 -0.0007 -0.0002 476 THR B N   
8353  C CA  . THR B 484 ? 0.1211 0.1728 0.1253 0.0048  -0.0012 0.0013  476 THR B CA  
8354  C C   . THR B 484 ? 0.1131 0.1612 0.1199 0.0029  0.0026  0.0030  476 THR B C   
8355  O O   . THR B 484 ? 0.1119 0.1570 0.1199 0.0060  0.0025  0.0047  476 THR B O   
8356  C CB  . THR B 484 ? 0.1210 0.1859 0.1284 0.0073  -0.0036 0.0009  476 THR B CB  
8357  O OG1 . THR B 484 ? 0.1370 0.2053 0.1430 0.0108  -0.0074 0.0009  476 THR B OG1 
8358  C CG2 . THR B 484 ? 0.1121 0.1788 0.1215 0.0119  -0.0030 0.0014  476 THR B CG2 
8359  N N   . ALA B 485 ? 0.1019 0.1501 0.1096 -0.0024 0.0059  0.0028  477 ALA B N   
8360  C CA  . ALA B 485 ? 0.1532 0.1965 0.1634 -0.0035 0.0103  0.0059  477 ALA B CA  
8361  C C   . ALA B 485 ? 0.1272 0.1596 0.1383 -0.0018 0.0125  0.0079  477 ALA B C   
8362  O O   . ALA B 485 ? 0.1159 0.1476 0.1302 0.0013  0.0130  0.0119  477 ALA B O   
8363  C CB  . ALA B 485 ? 0.1050 0.1473 0.1154 -0.0103 0.0148  0.0049  477 ALA B CB  
8364  N N   . THR B 486 ? 0.1372 0.1623 0.1456 -0.0037 0.0138  0.0054  478 THR B N   
8365  C CA  . THR B 486 ? 0.1115 0.1273 0.1225 -0.0020 0.0170  0.0070  478 THR B CA  
8366  C C   . THR B 486 ? 0.1069 0.1258 0.1199 0.0030  0.0128  0.0084  478 THR B C   
8367  O O   . THR B 486 ? 0.1184 0.1352 0.1371 0.0053  0.0142  0.0114  478 THR B O   
8368  C CB  . THR B 486 ? 0.1307 0.1373 0.1368 -0.0060 0.0206  0.0034  478 THR B CB  
8369  O OG1 . THR B 486 ? 0.1643 0.1742 0.1645 -0.0056 0.0158  0.0010  478 THR B OG1 
8370  C CG2 . THR B 486 ? 0.1293 0.1314 0.1320 -0.0128 0.0255  0.0005  478 THR B CG2 
8371  N N   . LEU B 487 ? 0.0806 0.1044 0.0899 0.0045  0.0080  0.0062  479 LEU B N   
8372  C CA  . LEU B 487 ? 0.1000 0.1248 0.1104 0.0080  0.0050  0.0064  479 LEU B CA  
8373  C C   . LEU B 487 ? 0.1341 0.1654 0.1481 0.0100  0.0032  0.0089  479 LEU B C   
8374  O O   . LEU B 487 ? 0.0892 0.1211 0.1063 0.0111  0.0019  0.0098  479 LEU B O   
8375  C CB  . LEU B 487 ? 0.1167 0.1434 0.1221 0.0099  0.0015  0.0040  479 LEU B CB  
8376  C CG  . LEU B 487 ? 0.1470 0.1672 0.1471 0.0087  0.0022  0.0028  479 LEU B CG  
8377  C CD1 . LEU B 487 ? 0.1663 0.1897 0.1624 0.0119  -0.0015 0.0022  479 LEU B CD1 
8378  C CD2 . LEU B 487 ? 0.1344 0.1458 0.1351 0.0083  0.0046  0.0030  479 LEU B CD2 
8379  N N   . ARG B 488 ? 0.1198 0.1568 0.1332 0.0096  0.0032  0.0100  480 ARG B N   
8380  C CA  . ARG B 488 ? 0.1213 0.1648 0.1356 0.0109  0.0016  0.0128  480 ARG B CA  
8381  C C   . ARG B 488 ? 0.1188 0.1610 0.1386 0.0115  0.0031  0.0182  480 ARG B C   
8382  O O   . ARG B 488 ? 0.1262 0.1748 0.1464 0.0128  0.0005  0.0215  480 ARG B O   
8383  C CB  . ARG B 488 ? 0.1262 0.1754 0.1382 0.0099  0.0027  0.0132  480 ARG B CB  
8384  C CG  . ARG B 488 ? 0.1277 0.1824 0.1366 0.0109  0.0009  0.0088  480 ARG B CG  
8385  C CD  . ARG B 488 ? 0.1105 0.1719 0.1194 0.0090  0.0031  0.0090  480 ARG B CD  
8386  N NE  . ARG B 488 ? 0.1179 0.1866 0.1263 0.0111  0.0019  0.0055  480 ARG B NE  
8387  C CZ  . ARG B 488 ? 0.1122 0.1883 0.1234 0.0097  0.0029  0.0042  480 ARG B CZ  
8388  N NH1 . ARG B 488 ? 0.0992 0.1752 0.1122 0.0045  0.0053  0.0052  480 ARG B NH1 
8389  N NH2 . ARG B 488 ? 0.1047 0.1885 0.1174 0.0132  0.0021  0.0017  480 ARG B NH2 
8390  N N   . LEU B 489 ? 0.0855 0.1200 0.1093 0.0107  0.0074  0.0195  481 LEU B N   
8391  C CA  . LEU B 489 ? 0.1127 0.1458 0.1440 0.0127  0.0099  0.0255  481 LEU B CA  
8392  C C   . LEU B 489 ? 0.0970 0.1312 0.1348 0.0144  0.0085  0.0259  481 LEU B C   
8393  O O   . LEU B 489 ? 0.0942 0.1298 0.1407 0.0169  0.0102  0.0315  481 LEU B O   
8394  C CB  . LEU B 489 ? 0.1048 0.1272 0.1379 0.0111  0.0174  0.0264  481 LEU B CB  
8395  C CG  . LEU B 489 ? 0.1538 0.1750 0.1817 0.0079  0.0196  0.0258  481 LEU B CG  
8396  C CD1 . LEU B 489 ? 0.1518 0.1608 0.1812 0.0051  0.0280  0.0260  481 LEU B CD1 
8397  C CD2 . LEU B 489 ? 0.1501 0.1791 0.1774 0.0099  0.0172  0.0313  481 LEU B CD2 
8398  N N   . ILE B 490 ? 0.0825 0.1163 0.1171 0.0131  0.0061  0.0206  482 ILE B N   
8399  C CA  . ILE B 490 ? 0.1221 0.1577 0.1629 0.0134  0.0050  0.0204  482 ILE B CA  
8400  C C   . ILE B 490 ? 0.1530 0.2006 0.1963 0.0141  -0.0009 0.0229  482 ILE B C   
8401  O O   . ILE B 490 ? 0.1160 0.1675 0.1517 0.0130  -0.0048 0.0200  482 ILE B O   
8402  C CB  . ILE B 490 ? 0.1204 0.1504 0.1554 0.0113  0.0046  0.0144  482 ILE B CB  
8403  C CG1 . ILE B 490 ? 0.1328 0.1525 0.1631 0.0100  0.0095  0.0122  482 ILE B CG1 
8404  C CG2 . ILE B 490 ? 0.1326 0.1644 0.1741 0.0104  0.0041  0.0138  482 ILE B CG2 
8405  C CD1 . ILE B 490 ? 0.1381 0.1522 0.1608 0.0088  0.0087  0.0080  482 ILE B CD1 
8406  N N   . PRO B 491 ? 0.1111 0.1658 0.1650 0.0159  -0.0015 0.0284  483 PRO B N   
8407  C CA  . PRO B 491 ? 0.0992 0.1678 0.1547 0.0154  -0.0084 0.0305  483 PRO B CA  
8408  C C   . PRO B 491 ? 0.1316 0.2011 0.1825 0.0112  -0.0117 0.0231  483 PRO B C   
8409  O O   . PRO B 491 ? 0.1181 0.1805 0.1710 0.0096  -0.0087 0.0192  483 PRO B O   
8410  C CB  . PRO B 491 ? 0.0868 0.1632 0.1575 0.0183  -0.0079 0.0377  483 PRO B CB  
8411  C CG  . PRO B 491 ? 0.1054 0.1702 0.1805 0.0216  0.0004  0.0407  483 PRO B CG  
8412  C CD  . PRO B 491 ? 0.1011 0.1522 0.1662 0.0183  0.0043  0.0326  483 PRO B CD  
8413  N N   . ASN B 492 ? 0.1386 0.2156 0.1820 0.0090  -0.0171 0.0211  484 ASN B N   
8414  C CA  . ASN B 492 ? 0.1547 0.2320 0.1934 0.0043  -0.0197 0.0136  484 ASN B CA  
8415  C C   . ASN B 492 ? 0.1545 0.2171 0.1857 0.0040  -0.0156 0.0071  484 ASN B C   
8416  O O   . ASN B 492 ? 0.1490 0.2066 0.1797 0.0009  -0.0149 0.0021  484 ASN B O   
8417  C CB  . ASN B 492 ? 0.0900 0.1749 0.1399 0.0012  -0.0215 0.0138  484 ASN B CB  
8418  C CG  . ASN B 492 ? 0.1001 0.1886 0.1444 -0.0053 -0.0254 0.0066  484 ASN B CG  
8419  O OD1 . ASN B 492 ? 0.1405 0.2339 0.1750 -0.0073 -0.0292 0.0044  484 ASN B OD1 
8420  N ND2 . ASN B 492 ? 0.1103 0.1950 0.1597 -0.0094 -0.0234 0.0023  484 ASN B ND2 
8421  N N   . MET B 493 ? 0.1508 0.2071 0.1769 0.0071  -0.0128 0.0077  485 MET B N   
8422  C CA  . MET B 493 ? 0.1680 0.2135 0.1871 0.0079  -0.0101 0.0030  485 MET B CA  
8423  C C   . MET B 493 ? 0.1685 0.2162 0.1794 0.0093  -0.0109 0.0011  485 MET B C   
8424  O O   . MET B 493 ? 0.1600 0.2135 0.1707 0.0104  -0.0113 0.0049  485 MET B O   
8425  C CB  . MET B 493 ? 0.1303 0.1683 0.1514 0.0097  -0.0060 0.0051  485 MET B CB  
8426  C CG  . MET B 493 ? 0.1624 0.1923 0.1764 0.0112  -0.0044 0.0018  485 MET B CG  
8427  S SD  . MET B 493 ? 0.1633 0.1832 0.1738 0.0102  -0.0034 -0.0024 485 MET B SD  
8428  C CE  . MET B 493 ? 0.1436 0.1568 0.1585 0.0086  0.0005  -0.0001 485 MET B CE  
8429  N N   . ASP B 494 ? 0.1222 0.1647 0.1268 0.0093  -0.0104 -0.0046 486 ASP B N   
8430  C CA  . ASP B 494 ? 0.1388 0.1823 0.1371 0.0117  -0.0094 -0.0067 486 ASP B CA  
8431  C C   . ASP B 494 ? 0.1572 0.1952 0.1558 0.0154  -0.0069 -0.0063 486 ASP B C   
8432  O O   . ASP B 494 ? 0.1656 0.1949 0.1640 0.0164  -0.0056 -0.0077 486 ASP B O   
8433  C CB  . ASP B 494 ? 0.1766 0.2171 0.1681 0.0104  -0.0090 -0.0133 486 ASP B CB  
8434  C CG  . ASP B 494 ? 0.1732 0.2226 0.1610 0.0060  -0.0121 -0.0144 486 ASP B CG  
8435  O OD1 . ASP B 494 ? 0.1927 0.2514 0.1837 0.0053  -0.0149 -0.0086 486 ASP B OD1 
8436  O OD2 . ASP B 494 ? 0.1843 0.2308 0.1653 0.0032  -0.0116 -0.0209 486 ASP B OD2 
8437  N N   . VAL B 495 ? 0.0940 0.1377 0.0929 0.0170  -0.0062 -0.0043 487 VAL B N   
8438  C CA  . VAL B 495 ? 0.0987 0.1413 0.0985 0.0198  -0.0049 -0.0039 487 VAL B CA  
8439  C C   . VAL B 495 ? 0.1374 0.1847 0.1352 0.0230  -0.0036 -0.0065 487 VAL B C   
8440  O O   . VAL B 495 ? 0.1423 0.1968 0.1389 0.0220  -0.0029 -0.0064 487 VAL B O   
8441  C CB  . VAL B 495 ? 0.1462 0.1921 0.1493 0.0180  -0.0044 -0.0001 487 VAL B CB  
8442  C CG1 . VAL B 495 ? 0.1339 0.1816 0.1375 0.0196  -0.0042 -0.0003 487 VAL B CG1 
8443  C CG2 . VAL B 495 ? 0.1524 0.1926 0.1581 0.0156  -0.0041 0.0020  487 VAL B CG2 
8444  N N   . TRP B 496 ? 0.0912 0.1340 0.0886 0.0272  -0.0026 -0.0082 488 TRP B N   
8445  C CA  . TRP B 496 ? 0.1174 0.1641 0.1150 0.0318  -0.0003 -0.0106 488 TRP B CA  
8446  C C   . TRP B 496 ? 0.1604 0.2132 0.1632 0.0357  -0.0009 -0.0077 488 TRP B C   
8447  O O   . TRP B 496 ? 0.1726 0.2206 0.1756 0.0367  -0.0027 -0.0054 488 TRP B O   
8448  C CB  . TRP B 496 ? 0.1177 0.1536 0.1113 0.0346  0.0022  -0.0148 488 TRP B CB  
8449  C CG  . TRP B 496 ? 0.1743 0.2069 0.1619 0.0300  0.0029  -0.0193 488 TRP B CG  
8450  C CD1 . TRP B 496 ? 0.1311 0.1581 0.1164 0.0249  0.0010  -0.0203 488 TRP B CD1 
8451  C CD2 . TRP B 496 ? 0.1632 0.1994 0.1461 0.0296  0.0058  -0.0238 488 TRP B CD2 
8452  N NE1 . TRP B 496 ? 0.1454 0.1735 0.1247 0.0209  0.0014  -0.0251 488 TRP B NE1 
8453  C CE2 . TRP B 496 ? 0.1915 0.2242 0.1679 0.0236  0.0046  -0.0275 488 TRP B CE2 
8454  C CE3 . TRP B 496 ? 0.1586 0.2013 0.1422 0.0334  0.0096  -0.0253 488 TRP B CE3 
8455  C CZ2 . TRP B 496 ? 0.2344 0.2694 0.2028 0.0207  0.0066  -0.0328 488 TRP B CZ2 
8456  C CZ3 . TRP B 496 ? 0.2149 0.2587 0.1910 0.0311  0.0128  -0.0305 488 TRP B CZ3 
8457  C CH2 . TRP B 496 ? 0.2457 0.2851 0.2130 0.0245  0.0111  -0.0344 488 TRP B CH2 
8458  N N   . ARG B 497 ? 0.1114 0.1759 0.1183 0.0373  0.0005  -0.0078 489 ARG B N   
8459  C CA  . ARG B 497 ? 0.1002 0.1748 0.1139 0.0407  -0.0007 -0.0052 489 ARG B CA  
8460  C C   . ARG B 497 ? 0.1339 0.2159 0.1524 0.0468  0.0030  -0.0071 489 ARG B C   
8461  O O   . ARG B 497 ? 0.1361 0.2311 0.1595 0.0455  0.0048  -0.0074 489 ARG B O   
8462  C CB  . ARG B 497 ? 0.0852 0.1697 0.1019 0.0346  -0.0024 -0.0031 489 ARG B CB  
8463  C CG  . ARG B 497 ? 0.0836 0.1801 0.1068 0.0358  -0.0051 -0.0008 489 ARG B CG  
8464  C CD  . ARG B 497 ? 0.1121 0.2151 0.1364 0.0275  -0.0060 -0.0002 489 ARG B CD  
8465  N NE  . ARG B 497 ? 0.1244 0.2393 0.1534 0.0266  -0.0097 0.0013  489 ARG B NE  
8466  C CZ  . ARG B 497 ? 0.1658 0.2982 0.2032 0.0248  -0.0097 0.0011  489 ARG B CZ  
8467  N NH1 . ARG B 497 ? 0.1317 0.2698 0.1730 0.0241  -0.0052 -0.0004 489 ARG B NH1 
8468  N NH2 . ARG B 497 ? 0.1178 0.2629 0.1592 0.0231  -0.0142 0.0025  489 ARG B NH2 
8469  N N   . PRO B 498 ? 0.1414 0.2147 0.1591 0.0536  0.0054  -0.0084 490 PRO B N   
8470  C CA  . PRO B 498 ? 0.1461 0.2232 0.1677 0.0598  0.0110  -0.0113 490 PRO B CA  
8471  C C   . PRO B 498 ? 0.1776 0.2720 0.2116 0.0656  0.0108  -0.0078 490 PRO B C   
8472  O O   . PRO B 498 ? 0.1469 0.2469 0.1855 0.0674  0.0058  -0.0028 490 PRO B O   
8473  C CB  . PRO B 498 ? 0.1241 0.1835 0.1410 0.0651  0.0141  -0.0133 490 PRO B CB  
8474  C CG  . PRO B 498 ? 0.1806 0.2316 0.1949 0.0639  0.0092  -0.0092 490 PRO B CG  
8475  C CD  . PRO B 498 ? 0.1540 0.2111 0.1663 0.0551  0.0044  -0.0078 490 PRO B CD  
8476  N N   . CYS B 499 ? 0.1683 0.2723 0.2077 0.0682  0.0163  -0.0104 491 CYS B N   
8477  C CA  . CYS B 499 ? 0.1110 0.2349 0.1647 0.0733  0.0163  -0.0072 491 CYS B CA  
8478  C C   . CYS B 499 ? 0.1801 0.3036 0.2422 0.0859  0.0202  -0.0058 491 CYS B C   
8479  O O   . CYS B 499 ? 0.1865 0.3240 0.2605 0.0890  0.0180  -0.0013 491 CYS B O   
8480  C CB  . CYS B 499 ? 0.1562 0.2946 0.2140 0.0688  0.0208  -0.0099 491 CYS B CB  
8481  S SG  . CYS B 499 ? 0.2018 0.3349 0.2565 0.0731  0.0320  -0.0167 491 CYS B SG  
8482  N N   . ASP B 500 ? 0.1336 0.2375 0.1884 0.0904  0.0256  -0.0093 492 ASP B N   
8483  C CA  . ASP B 500 ? 0.1476 0.2460 0.2098 0.1010  0.0301  -0.0074 492 ASP B CA  
8484  C C   . ASP B 500 ? 0.1601 0.2325 0.2111 0.1042  0.0342  -0.0106 492 ASP B C   
8485  O O   . ASP B 500 ? 0.1818 0.2420 0.2203 0.0962  0.0318  -0.0136 492 ASP B O   
8486  C CB  . ASP B 500 ? 0.1969 0.3039 0.2677 0.1033  0.0379  -0.0108 492 ASP B CB  
8487  C CG  . ASP B 500 ? 0.2732 0.3717 0.3328 0.0989  0.0461  -0.0201 492 ASP B CG  
8488  O OD1 . ASP B 500 ? 0.2223 0.3038 0.2677 0.0964  0.0472  -0.0246 492 ASP B OD1 
8489  O OD2 . ASP B 500 ? 0.2732 0.3821 0.3375 0.0974  0.0516  -0.0229 492 ASP B OD2 
8490  N N   . THR B 501 ? 0.1767 0.2384 0.2323 0.1119  0.0398  -0.0100 493 THR B N   
8491  C CA  . THR B 501 ? 0.3537 0.3889 0.3994 0.1140  0.0442  -0.0126 493 THR B CA  
8492  C C   . THR B 501 ? 0.2522 0.2735 0.2845 0.1080  0.0513  -0.0236 493 THR B C   
8493  O O   . THR B 501 ? 0.2583 0.2600 0.2787 0.1043  0.0521  -0.0270 493 THR B O   
8494  C CB  . THR B 501 ? 0.3800 0.4073 0.4344 0.1233  0.0489  -0.0094 493 THR B CB  
8495  O OG1 . THR B 501 ? 0.4650 0.4958 0.5251 0.1254  0.0575  -0.0156 493 THR B OG1 
8496  C CG2 . THR B 501 ? 0.3767 0.4212 0.4435 0.1286  0.0410  0.0015  493 THR B CG2 
8497  N N   . ALA B 502 ? 0.1974 0.2287 0.2305 0.1054  0.0562  -0.0293 494 ALA B N   
8498  C CA  . ALA B 502 ? 0.2385 0.2590 0.2563 0.0979  0.0618  -0.0398 494 ALA B CA  
8499  C C   . ALA B 502 ? 0.2316 0.2540 0.2394 0.0850  0.0525  -0.0397 494 ALA B C   
8500  O O   . ALA B 502 ? 0.2074 0.2143 0.2027 0.0777  0.0524  -0.0449 494 ALA B O   
8501  C CB  . ALA B 502 ? 0.2230 0.2553 0.2433 0.0968  0.0686  -0.0448 494 ALA B CB  
8502  N N   . GLU B 503 ? 0.1950 0.2365 0.2089 0.0818  0.0450  -0.0338 495 GLU B N   
8503  C CA  . GLU B 503 ? 0.2056 0.2483 0.2118 0.0711  0.0370  -0.0327 495 GLU B CA  
8504  C C   . GLU B 503 ? 0.2045 0.2343 0.2082 0.0703  0.0320  -0.0294 495 GLU B C   
8505  O O   . GLU B 503 ? 0.1682 0.1917 0.1635 0.0619  0.0283  -0.0311 495 GLU B O   
8506  C CB  . GLU B 503 ? 0.1439 0.2072 0.1573 0.0680  0.0316  -0.0274 495 GLU B CB  
8507  C CG  . GLU B 503 ? 0.2163 0.2911 0.2286 0.0650  0.0364  -0.0308 495 GLU B CG  
8508  C CD  . GLU B 503 ? 0.2044 0.2958 0.2212 0.0594  0.0317  -0.0261 495 GLU B CD  
8509  O OE1 . GLU B 503 ? 0.1423 0.2367 0.1634 0.0578  0.0249  -0.0208 495 GLU B OE1 
8510  O OE2 . GLU B 503 ? 0.1866 0.2870 0.2018 0.0560  0.0357  -0.0279 495 GLU B OE2 
8511  N N   . SER B 504 ? 0.2053 0.2317 0.2163 0.0792  0.0319  -0.0242 496 SER B N   
8512  C CA  A SER B 504 ? 0.2050 0.2184 0.2125 0.0786  0.0281  -0.0205 496 SER B CA  
8513  C CA  B SER B 504 ? 0.2035 0.2169 0.2109 0.0785  0.0280  -0.0205 496 SER B CA  
8514  C C   . SER B 504 ? 0.1866 0.1774 0.1840 0.0756  0.0333  -0.0270 496 SER B C   
8515  O O   . SER B 504 ? 0.1872 0.1692 0.1782 0.0685  0.0299  -0.0274 496 SER B O   
8516  C CB  A SER B 504 ? 0.2201 0.2354 0.2364 0.0894  0.0270  -0.0125 496 SER B CB  
8517  C CB  B SER B 504 ? 0.2215 0.2371 0.2377 0.0891  0.0268  -0.0124 496 SER B CB  
8518  O OG  A SER B 504 ? 0.1542 0.1915 0.1793 0.0900  0.0208  -0.0067 496 SER B OG  
8519  O OG  B SER B 504 ? 0.2167 0.2162 0.2273 0.0888  0.0249  -0.0091 496 SER B OG  
8520  N N   . LEU B 505 ? 0.1961 0.1771 0.1924 0.0807  0.0423  -0.0326 497 LEU B N   
8521  C CA  . LEU B 505 ? 0.2507 0.2090 0.2365 0.0764  0.0482  -0.0402 497 LEU B CA  
8522  C C   . LEU B 505 ? 0.2444 0.2053 0.2202 0.0630  0.0451  -0.0471 497 LEU B C   
8523  O O   . LEU B 505 ? 0.2557 0.2049 0.2245 0.0554  0.0438  -0.0500 497 LEU B O   
8524  C CB  . LEU B 505 ? 0.2632 0.2101 0.2491 0.0839  0.0598  -0.0460 497 LEU B CB  
8525  C CG  . LEU B 505 ? 0.2655 0.1877 0.2392 0.0782  0.0678  -0.0562 497 LEU B CG  
8526  C CD1 . LEU B 505 ? 0.3119 0.2159 0.2832 0.0770  0.0666  -0.0528 497 LEU B CD1 
8527  C CD2 . LEU B 505 ? 0.2771 0.1919 0.2540 0.0840  0.0773  -0.0607 497 LEU B CD2 
8528  N N   . VAL B 506 ? 0.2066 0.1837 0.1818 0.0600  0.0439  -0.0491 498 VAL B N   
8529  C CA  . VAL B 506 ? 0.2186 0.1999 0.1840 0.0481  0.0403  -0.0540 498 VAL B CA  
8530  C C   . VAL B 506 ? 0.2008 0.1878 0.1681 0.0423  0.0310  -0.0482 498 VAL B C   
8531  O O   . VAL B 506 ? 0.2089 0.1915 0.1697 0.0336  0.0282  -0.0515 498 VAL B O   
8532  C CB  . VAL B 506 ? 0.2089 0.2062 0.1728 0.0468  0.0414  -0.0557 498 VAL B CB  
8533  C CG1 . VAL B 506 ? 0.2528 0.2566 0.2067 0.0353  0.0360  -0.0582 498 VAL B CG1 
8534  C CG2 . VAL B 506 ? 0.2139 0.2041 0.1746 0.0515  0.0523  -0.0632 498 VAL B CG2 
8535  N N   . ALA B 507 ? 0.1675 0.1647 0.1440 0.0468  0.0263  -0.0396 499 ALA B N   
8536  C CA  . ALA B 507 ? 0.1731 0.1741 0.1515 0.0419  0.0190  -0.0344 499 ALA B CA  
8537  C C   . ALA B 507 ? 0.1693 0.1540 0.1451 0.0399  0.0194  -0.0351 499 ALA B C   
8538  O O   . ALA B 507 ? 0.1752 0.1596 0.1488 0.0323  0.0158  -0.0357 499 ALA B O   
8539  C CB  . ALA B 507 ? 0.1813 0.1936 0.1685 0.0467  0.0153  -0.0265 499 ALA B CB  
8540  N N   . TRP B 508 ? 0.2026 0.1740 0.1792 0.0469  0.0243  -0.0346 500 TRP B N   
8541  C CA  . TRP B 508 ? 0.1832 0.1367 0.1565 0.0447  0.0261  -0.0352 500 TRP B CA  
8542  C C   . TRP B 508 ? 0.2557 0.1999 0.2211 0.0356  0.0291  -0.0446 500 TRP B C   
8543  O O   . TRP B 508 ? 0.2501 0.1894 0.2136 0.0279  0.0271  -0.0458 500 TRP B O   
8544  C CB  . TRP B 508 ? 0.2190 0.1587 0.1941 0.0549  0.0317  -0.0321 500 TRP B CB  
8545  C CG  . TRP B 508 ? 0.2207 0.1644 0.2008 0.0609  0.0274  -0.0220 500 TRP B CG  
8546  C CD1 . TRP B 508 ? 0.2219 0.1789 0.2092 0.0693  0.0250  -0.0156 500 TRP B CD1 
8547  C CD2 . TRP B 508 ? 0.2272 0.1626 0.2049 0.0580  0.0251  -0.0174 500 TRP B CD2 
8548  N NE1 . TRP B 508 ? 0.2615 0.2190 0.2496 0.0716  0.0207  -0.0075 500 TRP B NE1 
8549  C CE2 . TRP B 508 ? 0.2353 0.1788 0.2169 0.0649  0.0211  -0.0084 500 TRP B CE2 
8550  C CE3 . TRP B 508 ? 0.2339 0.1569 0.2066 0.0496  0.0263  -0.0202 500 TRP B CE3 
8551  C CZ2 . TRP B 508 ? 0.1847 0.1227 0.1632 0.0638  0.0186  -0.0022 500 TRP B CZ2 
8552  C CZ3 . TRP B 508 ? 0.2476 0.1652 0.2190 0.0489  0.0245  -0.0140 500 TRP B CZ3 
8553  C CH2 . TRP B 508 ? 0.2498 0.1743 0.2231 0.0560  0.0209  -0.0051 500 TRP B CH2 
8554  N N   . ALA B 509 ? 0.2068 0.1488 0.1675 0.0360  0.0344  -0.0519 501 ALA B N   
8555  C CA  . ALA B 509 ? 0.2384 0.1719 0.1896 0.0261  0.0373  -0.0621 501 ALA B CA  
8556  C C   . ALA B 509 ? 0.2640 0.2132 0.2134 0.0156  0.0292  -0.0626 501 ALA B C   
8557  O O   . ALA B 509 ? 0.2434 0.1882 0.1891 0.0061  0.0279  -0.0673 501 ALA B O   
8558  C CB  . ALA B 509 ? 0.2370 0.1664 0.1821 0.0284  0.0450  -0.0700 501 ALA B CB  
8559  N N   . GLU B 510 ? 0.2291 0.1970 0.1817 0.0172  0.0240  -0.0578 502 GLU B N   
8560  C CA  . GLU B 510 ? 0.1874 0.1703 0.1394 0.0090  0.0164  -0.0563 502 GLU B CA  
8561  C C   . GLU B 510 ? 0.1729 0.1564 0.1322 0.0064  0.0116  -0.0508 502 GLU B C   
8562  O O   . GLU B 510 ? 0.1955 0.1843 0.1545 -0.0019 0.0075  -0.0523 502 GLU B O   
8563  C CB  . GLU B 510 ? 0.1966 0.1966 0.1505 0.0119  0.0133  -0.0513 502 GLU B CB  
8564  C CG  . GLU B 510 ? 0.2378 0.2402 0.1827 0.0114  0.0177  -0.0576 502 GLU B CG  
8565  C CD  . GLU B 510 ? 0.3436 0.3463 0.2769 0.0009  0.0164  -0.0654 502 GLU B CD  
8566  O OE1 . GLU B 510 ? 0.2394 0.2537 0.1729 -0.0054 0.0089  -0.0622 502 GLU B OE1 
8567  O OE2 . GLU B 510 ? 0.3127 0.3045 0.2367 -0.0011 0.0231  -0.0749 502 GLU B OE2 
8568  N N   . ALA B 511 ? 0.1655 0.1445 0.1313 0.0133  0.0122  -0.0443 503 ALA B N   
8569  C CA  . ALA B 511 ? 0.2052 0.1827 0.1766 0.0109  0.0094  -0.0397 503 ALA B CA  
8570  C C   . ALA B 511 ? 0.2366 0.2001 0.2051 0.0047  0.0125  -0.0450 503 ALA B C   
8571  O O   . ALA B 511 ? 0.2306 0.1977 0.2030 -0.0019 0.0096  -0.0443 503 ALA B O   
8572  C CB  . ALA B 511 ? 0.2002 0.1746 0.1759 0.0190  0.0100  -0.0325 503 ALA B CB  
8573  N N   . ALA B 512 ? 0.2027 0.1496 0.1654 0.0067  0.0193  -0.0504 504 ALA B N   
8574  C CA  . ALA B 512 ? 0.2749 0.2056 0.2340 -0.0002 0.0238  -0.0565 504 ALA B CA  
8575  C C   . ALA B 512 ? 0.2740 0.2127 0.2294 -0.0122 0.0210  -0.0645 504 ALA B C   
8576  O O   . ALA B 512 ? 0.2832 0.2196 0.2404 -0.0211 0.0205  -0.0673 504 ALA B O   
8577  C CB  . ALA B 512 ? 0.2535 0.1627 0.2069 0.0054  0.0329  -0.0604 504 ALA B CB  
8578  N N   . LYS B 513 ? 0.2470 0.1961 0.1971 -0.0129 0.0193  -0.0682 505 LYS B N   
8579  C CA  . LYS B 513 ? 0.2536 0.2120 0.1976 -0.0243 0.0159  -0.0758 505 LYS B CA  
8580  C C   . LYS B 513 ? 0.2634 0.2424 0.2154 -0.0298 0.0066  -0.0704 505 LYS B C   
8581  O O   . LYS B 513 ? 0.3056 0.2920 0.2559 -0.0406 0.0030  -0.0755 505 LYS B O   
8582  C CB  . LYS B 513 ? 0.2488 0.2140 0.1838 -0.0229 0.0165  -0.0797 505 LYS B CB  
8583  C CG  . LYS B 513 ? 0.4537 0.4000 0.3795 -0.0200 0.0267  -0.0881 505 LYS B CG  
8584  C CD  . LYS B 513 ? 0.4228 0.3777 0.3383 -0.0213 0.0276  -0.0934 505 LYS B CD  
8585  C CE  . LYS B 513 ? 0.4644 0.4316 0.3710 -0.0353 0.0214  -0.0996 505 LYS B CE  
8586  N NZ  . LYS B 513 ? 0.5596 0.5283 0.4508 -0.0393 0.0249  -0.1084 505 LYS B NZ  
8587  N N   . ALA B 514 ? 0.2161 0.2054 0.1765 -0.0226 0.0027  -0.0603 506 ALA B N   
8588  C CA  . ALA B 514 ? 0.2545 0.2631 0.2233 -0.0258 -0.0051 -0.0541 506 ALA B CA  
8589  C C   . ALA B 514 ? 0.2557 0.2632 0.2321 -0.0329 -0.0058 -0.0550 506 ALA B C   
8590  O O   . ALA B 514 ? 0.3560 0.3500 0.3361 -0.0305 -0.0011 -0.0535 506 ALA B O   
8591  C CB  . ALA B 514 ? 0.1760 0.1905 0.1520 -0.0168 -0.0067 -0.0441 506 ALA B CB  
8592  N N   . GLU B 515 ? 0.2529 0.2759 0.2317 -0.0420 -0.0116 -0.0572 507 GLU B N   
8593  C CA  . GLU B 515 ? 0.3421 0.3664 0.3296 -0.0500 -0.0119 -0.0589 507 GLU B CA  
8594  C C   . GLU B 515 ? 0.2697 0.3076 0.2727 -0.0470 -0.0156 -0.0492 507 GLU B C   
8595  O O   . GLU B 515 ? 0.2660 0.3007 0.2780 -0.0504 -0.0130 -0.0489 507 GLU B O   
8596  C CB  . GLU B 515 ? 0.4159 0.4518 0.3998 -0.0628 -0.0165 -0.0670 507 GLU B CB  
8597  C CG  . GLU B 515 ? 0.6214 0.6544 0.5887 -0.0656 -0.0161 -0.0748 507 GLU B CG  
8598  C CD  . GLU B 515 ? 0.7462 0.7853 0.7074 -0.0805 -0.0187 -0.0855 507 GLU B CD  
8599  O OE1 . GLU B 515 ? 0.7941 0.8132 0.7466 -0.0865 -0.0112 -0.0961 507 GLU B OE1 
8600  O OE2 . GLU B 515 ? 0.7878 0.8516 0.7530 -0.0865 -0.0282 -0.0831 507 GLU B OE2 
8601  N N   . ASP B 516 ? 0.2023 0.2544 0.2088 -0.0407 -0.0204 -0.0413 508 ASP B N   
8602  C CA  . ASP B 516 ? 0.1898 0.2572 0.2116 -0.0388 -0.0241 -0.0327 508 ASP B CA  
8603  C C   . ASP B 516 ? 0.1417 0.2066 0.1665 -0.0283 -0.0223 -0.0241 508 ASP B C   
8604  O O   . ASP B 516 ? 0.1558 0.2339 0.1911 -0.0253 -0.0253 -0.0165 508 ASP B O   
8605  C CB  . ASP B 516 ? 0.2061 0.2978 0.2318 -0.0436 -0.0329 -0.0306 508 ASP B CB  
8606  C CG  . ASP B 516 ? 0.2883 0.3866 0.3046 -0.0389 -0.0366 -0.0270 508 ASP B CG  
8607  O OD1 . ASP B 516 ? 0.3000 0.3842 0.3050 -0.0345 -0.0322 -0.0296 508 ASP B OD1 
8608  O OD2 . ASP B 516 ? 0.3709 0.4890 0.3916 -0.0393 -0.0437 -0.0210 508 ASP B OD2 
8609  N N   . HIS B 517 ? 0.1591 0.2079 0.1754 -0.0227 -0.0174 -0.0252 509 HIS B N   
8610  C CA  . HIS B 517 ? 0.1797 0.2262 0.1989 -0.0146 -0.0155 -0.0181 509 HIS B CA  
8611  C C   . HIS B 517 ? 0.1538 0.1824 0.1658 -0.0105 -0.0100 -0.0203 509 HIS B C   
8612  O O   . HIS B 517 ? 0.1232 0.1423 0.1264 -0.0115 -0.0080 -0.0262 509 HIS B O   
8613  C CB  . HIS B 517 ? 0.1057 0.1627 0.1222 -0.0108 -0.0191 -0.0137 509 HIS B CB  
8614  C CG  . HIS B 517 ? 0.1420 0.1957 0.1457 -0.0107 -0.0190 -0.0188 509 HIS B CG  
8615  N ND1 . HIS B 517 ? 0.1651 0.2266 0.1622 -0.0164 -0.0226 -0.0233 509 HIS B ND1 
8616  C CD2 . HIS B 517 ? 0.1440 0.1885 0.1406 -0.0058 -0.0154 -0.0202 509 HIS B CD2 
8617  C CE1 . HIS B 517 ? 0.2027 0.2582 0.1886 -0.0148 -0.0202 -0.0278 509 HIS B CE1 
8618  N NE2 . HIS B 517 ? 0.1687 0.2146 0.1553 -0.0080 -0.0158 -0.0256 509 HIS B NE2 
8619  N N   . PRO B 518 ? 0.1447 0.1686 0.1597 -0.0057 -0.0074 -0.0154 510 PRO B N   
8620  C CA  . PRO B 518 ? 0.1207 0.1305 0.1289 -0.0012 -0.0035 -0.0158 510 PRO B CA  
8621  C C   . PRO B 518 ? 0.1502 0.1629 0.1533 0.0040  -0.0046 -0.0147 510 PRO B C   
8622  O O   . PRO B 518 ? 0.1674 0.1913 0.1716 0.0042  -0.0075 -0.0130 510 PRO B O   
8623  C CB  . PRO B 518 ? 0.1032 0.1097 0.1165 -0.0000 -0.0009 -0.0112 510 PRO B CB  
8624  C CG  . PRO B 518 ? 0.0944 0.1144 0.1162 -0.0001 -0.0034 -0.0070 510 PRO B CG  
8625  C CD  . PRO B 518 ? 0.0970 0.1277 0.1223 -0.0048 -0.0074 -0.0094 510 PRO B CD  
8626  N N   . SER B 519 ? 0.1262 0.1293 0.1242 0.0085  -0.0019 -0.0149 511 SER B N   
8627  C CA  . SER B 519 ? 0.1417 0.1490 0.1370 0.0135  -0.0025 -0.0136 511 SER B CA  
8628  C C   . SER B 519 ? 0.1289 0.1316 0.1237 0.0175  -0.0013 -0.0099 511 SER B C   
8629  O O   . SER B 519 ? 0.1280 0.1203 0.1209 0.0177  0.0008  -0.0093 511 SER B O   
8630  C CB  . SER B 519 ? 0.2146 0.2185 0.2042 0.0154  -0.0010 -0.0185 511 SER B CB  
8631  O OG  . SER B 519 ? 0.2337 0.2410 0.2212 0.0102  -0.0020 -0.0231 511 SER B OG  
8632  N N   . CYS B 520 ? 0.0977 0.1084 0.0934 0.0199  -0.0026 -0.0074 512 CYS B N   
8633  C CA  . CYS B 520 ? 0.1489 0.1586 0.1433 0.0234  -0.0025 -0.0046 512 CYS B CA  
8634  C C   . CYS B 520 ? 0.1883 0.2026 0.1821 0.0285  -0.0027 -0.0055 512 CYS B C   
8635  O O   . CYS B 520 ? 0.1542 0.1778 0.1498 0.0283  -0.0031 -0.0066 512 CYS B O   
8636  C CB  . CYS B 520 ? 0.1587 0.1748 0.1555 0.0210  -0.0033 -0.0019 512 CYS B CB  
8637  S SG  . CYS B 520 ? 0.1850 0.1956 0.1839 0.0163  -0.0014 -0.0004 512 CYS B SG  
8638  N N   . LEU B 521 ? 0.1079 0.1160 0.0995 0.0335  -0.0018 -0.0045 513 LEU B N   
8639  C CA  . LEU B 521 ? 0.1117 0.1245 0.1050 0.0400  -0.0011 -0.0046 513 LEU B CA  
8640  C C   . LEU B 521 ? 0.1136 0.1343 0.1088 0.0429  -0.0040 0.0002  513 LEU B C   
8641  O O   . LEU B 521 ? 0.1611 0.1752 0.1528 0.0443  -0.0048 0.0037  513 LEU B O   
8642  C CB  . LEU B 521 ? 0.1739 0.1734 0.1643 0.0446  0.0026  -0.0064 513 LEU B CB  
8643  C CG  . LEU B 521 ? 0.1723 0.1623 0.1593 0.0396  0.0053  -0.0121 513 LEU B CG  
8644  C CD1 . LEU B 521 ? 0.1853 0.1597 0.1689 0.0439  0.0105  -0.0147 513 LEU B CD1 
8645  C CD2 . LEU B 521 ? 0.1680 0.1683 0.1556 0.0362  0.0048  -0.0162 513 LEU B CD2 
8646  N N   . ILE B 522 ? 0.1349 0.1702 0.1350 0.0432  -0.0054 0.0004  514 ILE B N   
8647  C CA  . ILE B 522 ? 0.1334 0.1800 0.1358 0.0428  -0.0089 0.0039  514 ILE B CA  
8648  C C   . ILE B 522 ? 0.1126 0.1702 0.1215 0.0503  -0.0093 0.0056  514 ILE B C   
8649  O O   . ILE B 522 ? 0.1514 0.2159 0.1652 0.0519  -0.0068 0.0029  514 ILE B O   
8650  C CB  . ILE B 522 ? 0.1510 0.2062 0.1554 0.0355  -0.0094 0.0026  514 ILE B CB  
8651  C CG1 . ILE B 522 ? 0.1338 0.1785 0.1336 0.0296  -0.0085 0.0020  514 ILE B CG1 
8652  C CG2 . ILE B 522 ? 0.0969 0.1647 0.1037 0.0336  -0.0126 0.0047  514 ILE B CG2 
8653  C CD1 . ILE B 522 ? 0.1388 0.1887 0.1408 0.0235  -0.0076 0.0013  514 ILE B CD1 
8654  N N   . PHE B 523 ? 0.1102 0.1700 0.1192 0.0551  -0.0123 0.0104  515 PHE B N   
8655  C CA  . PHE B 523 ? 0.1643 0.2349 0.1814 0.0643  -0.0127 0.0135  515 PHE B CA  
8656  C C   . PHE B 523 ? 0.1880 0.2773 0.2095 0.0638  -0.0188 0.0179  515 PHE B C   
8657  O O   . PHE B 523 ? 0.2016 0.2906 0.2164 0.0578  -0.0227 0.0195  515 PHE B O   
8658  C CB  . PHE B 523 ? 0.1895 0.2454 0.2040 0.0733  -0.0103 0.0167  515 PHE B CB  
8659  C CG  . PHE B 523 ? 0.2054 0.2435 0.2158 0.0732  -0.0040 0.0114  515 PHE B CG  
8660  C CD1 . PHE B 523 ? 0.2102 0.2497 0.2257 0.0773  0.0012  0.0073  515 PHE B CD1 
8661  C CD2 . PHE B 523 ? 0.1738 0.1949 0.1752 0.0678  -0.0028 0.0099  515 PHE B CD2 
8662  C CE1 . PHE B 523 ? 0.2311 0.2547 0.2411 0.0755  0.0068  0.0013  515 PHE B CE1 
8663  C CE2 . PHE B 523 ? 0.1857 0.1924 0.1836 0.0661  0.0024  0.0043  515 PHE B CE2 
8664  C CZ  . PHE B 523 ? 0.2477 0.2556 0.2491 0.0695  0.0068  -0.0002 515 PHE B CZ  
8665  N N   . SER B 524 ? 0.2013 0.3078 0.2343 0.0699  -0.0193 0.0196  516 SER B N   
8666  C CA  . SER B 524 ? 0.2613 0.3881 0.3006 0.0720  -0.0258 0.0251  516 SER B CA  
8667  C C   . SER B 524 ? 0.2972 0.4217 0.3422 0.0832  -0.0246 0.0304  516 SER B C   
8668  O O   . SER B 524 ? 0.3504 0.4602 0.3952 0.0905  -0.0186 0.0296  516 SER B O   
8669  C CB  . SER B 524 ? 0.3171 0.4648 0.3661 0.0655  -0.0266 0.0220  516 SER B CB  
8670  O OG  . SER B 524 ? 0.3920 0.5450 0.4517 0.0716  -0.0215 0.0208  516 SER B OG  
8671  N N   . ARG B 525 ? 0.3499 0.4887 0.4000 0.0838  -0.0300 0.0355  517 ARG B N   
8672  C CA  . ARG B 525 ? 0.3261 0.4653 0.3837 0.0943  -0.0293 0.0413  517 ARG B CA  
8673  C C   . ARG B 525 ? 0.3846 0.5343 0.4570 0.0990  -0.0242 0.0388  517 ARG B C   
8674  O O   . ARG B 525 ? 0.3745 0.5244 0.4550 0.1084  -0.0225 0.0432  517 ARG B O   
8675  C CB  . ARG B 525 ? 0.2994 0.4518 0.3572 0.0933  -0.0377 0.0480  517 ARG B CB  
8676  N N   . GLN B 526 ? 0.4046 0.5626 0.4809 0.0927  -0.0214 0.0323  518 GLN B N   
8677  C CA  . GLN B 526 ? 0.5473 0.7169 0.6372 0.0959  -0.0164 0.0299  518 GLN B CA  
8678  C C   . GLN B 526 ? 0.6552 0.8085 0.7436 0.1012  -0.0068 0.0250  518 GLN B C   
8679  O O   . GLN B 526 ? 0.7611 0.8969 0.8380 0.0998  -0.0044 0.0219  518 GLN B O   
8680  C CB  . GLN B 526 ? 0.5410 0.7288 0.6355 0.0854  -0.0178 0.0257  518 GLN B CB  
8681  N N   . ASN B 527 ? 0.6099 0.7692 0.7099 0.1071  -0.0010 0.0239  519 ASN B N   
8682  C CA  . ASN B 527 ? 0.6110 0.7561 0.7093 0.1112  0.0091  0.0179  519 ASN B CA  
8683  C C   . ASN B 527 ? 0.5197 0.6784 0.6320 0.1139  0.0151  0.0155  519 ASN B C   
8684  O O   . ASN B 527 ? 0.4793 0.6594 0.6015 0.1097  0.0117  0.0168  519 ASN B O   
8685  C CB  . ASN B 527 ? 0.6757 0.7982 0.7690 0.1201  0.0129  0.0198  519 ASN B CB  
8686  N N   . PHE B 530 ? 0.6659 0.8294 0.7883 0.1134  0.0412  -0.0021 522 PHE B N   
8687  C CA  . PHE B 530 ? 0.7285 0.8757 0.8466 0.1177  0.0527  -0.0091 522 PHE B CA  
8688  C C   . PHE B 530 ? 0.7330 0.8905 0.8558 0.1143  0.0614  -0.0149 522 PHE B C   
8689  O O   . PHE B 530 ? 0.7212 0.8908 0.8600 0.1193  0.0654  -0.0141 522 PHE B O   
8690  C CB  . PHE B 530 ? 0.7656 0.9040 0.8922 0.1294  0.0557  -0.0065 522 PHE B CB  
8691  N N   . GLN B 531 ? 0.7702 0.9231 0.8789 0.1058  0.0644  -0.0204 523 GLN B N   
8692  C CA  . GLN B 531 ? 0.7565 0.9154 0.8649 0.1015  0.0736  -0.0261 523 GLN B CA  
8693  C C   . GLN B 531 ? 0.7085 0.8469 0.8033 0.1024  0.0842  -0.0350 523 GLN B C   
8694  O O   . GLN B 531 ? 0.7306 0.8505 0.8111 0.1021  0.0829  -0.0376 523 GLN B O   
8695  C CB  . GLN B 531 ? 0.7491 0.9176 0.8493 0.0902  0.0697  -0.0256 523 GLN B CB  
8696  N N   . ALA B 532 ? 0.6212 0.7629 0.7202 0.1028  0.0950  -0.0405 524 ALA B N   
8697  C CA  . ALA B 532 ? 0.5428 0.6660 0.6288 0.1028  0.1058  -0.0507 524 ALA B CA  
8698  C C   . ALA B 532 ? 0.5312 0.6441 0.5927 0.0923  0.1063  -0.0552 524 ALA B C   
8699  O O   . ALA B 532 ? 0.4545 0.5781 0.5110 0.0851  0.1013  -0.0512 524 ALA B O   
8700  C CB  . ALA B 532 ? 0.5546 0.6863 0.6513 0.1053  0.1171  -0.0563 524 ALA B CB  
8701  N N   . ARG B 533 ? 0.5050 0.5978 0.5506 0.0910  0.1114  -0.0639 525 ARG B N   
8702  C CA  . ARG B 533 ? 0.4207 0.5022 0.4410 0.0810  0.1114  -0.0682 525 ARG B CA  
8703  C C   . ARG B 533 ? 0.3818 0.4516 0.3882 0.0776  0.1198  -0.0810 525 ARG B C   
8704  O O   . ARG B 533 ? 0.3526 0.4171 0.3606 0.0880  0.1213  -0.0858 525 ARG B O   
8705  C CB  . ARG B 533 ? 0.3799 0.4515 0.3910 0.0797  0.1011  -0.0659 525 ARG B CB  
8706  C CG  . ARG B 533 ? 0.3432 0.4305 0.3606 0.0782  0.0888  -0.0565 525 ARG B CG  
8707  C CD  . ARG B 533 ? 0.2423 0.3186 0.2498 0.0765  0.0803  -0.0561 525 ARG B CD  
8708  N NE  . ARG B 533 ? 0.2755 0.3648 0.2924 0.0769  0.0696  -0.0475 525 ARG B NE  
8709  C CZ  . ARG B 533 ? 0.2537 0.3468 0.2860 0.0842  0.0655  -0.0408 525 ARG B CZ  
8710  N NH1 . ARG B 533 ? 0.2881 0.3737 0.3295 0.0926  0.0707  -0.0409 525 ARG B NH1 
8711  N NH2 . ARG B 533 ? 0.2918 0.3958 0.3297 0.0822  0.0558  -0.0339 525 ARG B NH2 
8712  N N   . SER B 534 ? 0.3695 0.4308 0.3475 0.0747  0.1232  -0.0765 526 SER B N   
8713  C CA  . SER B 534 ? 0.3849 0.4391 0.3418 0.0734  0.1259  -0.0879 526 SER B CA  
8714  C C   . SER B 534 ? 0.3711 0.4069 0.3147 0.0673  0.1199  -0.0927 526 SER B C   
8715  O O   . SER B 534 ? 0.3458 0.3806 0.2930 0.0657  0.1122  -0.0880 526 SER B O   
8716  C CB  . SER B 534 ? 0.4481 0.5053 0.3885 0.0632  0.1288  -0.0879 526 SER B CB  
8717  O OG  . SER B 534 ? 0.3412 0.4001 0.2736 0.0523  0.1195  -0.0841 526 SER B OG  
8718  N N   . GLU B 535 ? 0.3452 0.3655 0.2732 0.0629  0.1242  -0.1021 527 GLU B N   
8719  C CA  . GLU B 535 ? 0.3791 0.3824 0.2931 0.0548  0.1187  -0.1068 527 GLU B CA  
8720  C C   . GLU B 535 ? 0.3345 0.3442 0.2369 0.0436  0.1091  -0.1031 527 GLU B C   
8721  O O   . GLU B 535 ? 0.3144 0.3187 0.2152 0.0395  0.1014  -0.1025 527 GLU B O   
8722  C CB  . GLU B 535 ? 0.4361 0.4232 0.3338 0.0495  0.1251  -0.1176 527 GLU B CB  
8723  C CG  . GLU B 535 ? 0.6014 0.5728 0.4851 0.0395  0.1193  -0.1228 527 GLU B CG  
8724  C CD  . GLU B 535 ? 0.7840 0.7416 0.6498 0.0315  0.1249  -0.1336 527 GLU B CD  
8725  O OE1 . GLU B 535 ? 0.8346 0.7741 0.6985 0.0300  0.1271  -0.1395 527 GLU B OE1 
8726  O OE2 . GLU B 535 ? 0.8275 0.7917 0.6806 0.0261  0.1273  -0.1360 527 GLU B OE2 
8727  N N   . GLN B 536 ? 0.3651 0.3868 0.2601 0.0384  0.1092  -0.1004 528 GLN B N   
8728  C CA  . GLN B 536 ? 0.3522 0.3819 0.2369 0.0276  0.0992  -0.0963 528 GLN B CA  
8729  C C   . GLN B 536 ? 0.3272 0.3688 0.2281 0.0300  0.0917  -0.0879 528 GLN B C   
8730  O O   . GLN B 536 ? 0.2715 0.3148 0.1684 0.0241  0.0817  -0.0858 528 GLN B O   
8731  C CB  . GLN B 536 ? 0.3929 0.4322 0.2667 0.0222  0.1015  -0.0944 528 GLN B CB  
8732  C CG  . GLN B 536 ? 0.3402 0.3885 0.2034 0.0122  0.0906  -0.0886 528 GLN B CG  
8733  C CD  . GLN B 536 ? 0.3897 0.4293 0.2363 0.0033  0.0835  -0.0937 528 GLN B CD  
8734  O OE1 . GLN B 536 ? 0.3792 0.4088 0.2125 0.0000  0.0879  -0.1018 528 GLN B OE1 
8735  N NE2 . GLN B 536 ? 0.4036 0.4480 0.2520 -0.0008 0.0722  -0.0890 528 GLN B NE2 
8736  N N   . GLN B 537 ? 0.2700 0.3217 0.1902 0.0386  0.0957  -0.0827 529 GLN B N   
8737  C CA  . GLN B 537 ? 0.2434 0.3079 0.1801 0.0415  0.0875  -0.0750 529 GLN B CA  
8738  C C   . GLN B 537 ? 0.2648 0.3189 0.2056 0.0450  0.0826  -0.0766 529 GLN B C   
8739  O O   . GLN B 537 ? 0.2768 0.3332 0.2190 0.0415  0.0717  -0.0707 529 GLN B O   
8740  C CB  . GLN B 537 ? 0.2380 0.3158 0.1960 0.0496  0.0918  -0.0694 529 GLN B CB  
8741  C CG  . GLN B 537 ? 0.2327 0.3244 0.1898 0.0448  0.0941  -0.0656 529 GLN B CG  
8742  C CD  . GLN B 537 ? 0.3793 0.4826 0.3574 0.0518  0.1006  -0.0623 529 GLN B CD  
8743  O OE1 . GLN B 537 ? 0.3990 0.4960 0.3852 0.0593  0.1090  -0.0657 529 GLN B OE1 
8744  N NE2 . GLN B 537 ? 0.3750 0.4949 0.3626 0.0490  0.0968  -0.0554 529 GLN B NE2 
8745  N N   . LEU B 538 ? 0.2921 0.3301 0.2349 0.0513  0.0902  -0.0819 530 LEU B N   
8746  C CA  . LEU B 538 ? 0.3315 0.3559 0.2764 0.0538  0.0869  -0.0837 530 LEU B CA  
8747  C C   . LEU B 538 ? 0.2998 0.3176 0.2288 0.0418  0.0784  -0.0860 530 LEU B C   
8748  O O   . LEU B 538 ? 0.3099 0.3256 0.2437 0.0407  0.0691  -0.0805 530 LEU B O   
8749  C CB  . LEU B 538 ? 0.3878 0.3941 0.3327 0.0608  0.0957  -0.0891 530 LEU B CB  
8750  C CG  . LEU B 538 ? 0.3636 0.3767 0.3320 0.0736  0.0994  -0.0852 530 LEU B CG  
8751  C CD1 . LEU B 538 ? 0.3968 0.3921 0.3645 0.0785  0.1064  -0.0908 530 LEU B CD1 
8752  C CD2 . LEU B 538 ? 0.2791 0.2940 0.2603 0.0777  0.0919  -0.0755 530 LEU B CD2 
8753  N N   . ASN B 539 ? 0.3397 0.3546 0.2502 0.0327  0.0803  -0.0925 531 ASN B N   
8754  C CA  . ASN B 539 ? 0.3206 0.3314 0.2162 0.0210  0.0724  -0.0955 531 ASN B CA  
8755  C C   . ASN B 539 ? 0.3125 0.3403 0.2094 0.0160  0.0606  -0.0865 531 ASN B C   
8756  O O   . ASN B 539 ? 0.3076 0.3341 0.1997 0.0090  0.0518  -0.0856 531 ASN B O   
8757  C CB  . ASN B 539 ? 0.4010 0.4052 0.2779 0.0134  0.0757  -0.1023 531 ASN B CB  
8758  C CG  . ASN B 539 ? 0.5016 0.4866 0.3769 0.0173  0.0850  -0.1106 531 ASN B CG  
8759  O OD1 . ASN B 539 ? 0.4885 0.4608 0.3713 0.0212  0.0860  -0.1121 531 ASN B OD1 
8760  N ND2 . ASN B 539 ? 0.5465 0.5293 0.4121 0.0161  0.0921  -0.1158 531 ASN B ND2 
8761  N N   . ASP B 540 ? 0.2824 0.3253 0.1873 0.0195  0.0601  -0.0787 532 ASP B N   
8762  C CA  . ASP B 540 ? 0.2530 0.3090 0.1603 0.0157  0.0498  -0.0685 532 ASP B CA  
8763  C C   . ASP B 540 ? 0.2198 0.2779 0.1450 0.0210  0.0433  -0.0598 532 ASP B C   
8764  O O   . ASP B 540 ? 0.2373 0.3036 0.1650 0.0179  0.0355  -0.0518 532 ASP B O   
8765  C CB  . ASP B 540 ? 0.2225 0.2920 0.1274 0.0150  0.0532  -0.0646 532 ASP B CB  
8766  C CG  . ASP B 540 ? 0.3355 0.4044 0.2195 0.0071  0.0563  -0.0698 532 ASP B CG  
8767  O OD1 . ASP B 540 ? 0.2877 0.3503 0.1595 0.0003  0.0510  -0.0733 532 ASP B OD1 
8768  O OD2 . ASP B 540 ? 0.2896 0.3624 0.1710 0.0076  0.0628  -0.0688 532 ASP B OD2 
8769  N N   . ILE B 541 ? 0.1984 0.2492 0.1355 0.0290  0.0466  -0.0607 533 ILE B N   
8770  C CA  . ILE B 541 ? 0.1802 0.2328 0.1314 0.0330  0.0399  -0.0528 533 ILE B CA  
8771  C C   . ILE B 541 ? 0.1748 0.2231 0.1217 0.0265  0.0312  -0.0506 533 ILE B C   
8772  O O   . ILE B 541 ? 0.1651 0.2195 0.1191 0.0258  0.0246  -0.0430 533 ILE B O   
8773  C CB  . ILE B 541 ? 0.1825 0.2265 0.1444 0.0424  0.0443  -0.0538 533 ILE B CB  
8774  C CG1 . ILE B 541 ? 0.1870 0.2384 0.1569 0.0501  0.0529  -0.0547 533 ILE B CG1 
8775  C CG2 . ILE B 541 ? 0.2045 0.2501 0.1777 0.0452  0.0368  -0.0456 533 ILE B CG2 
8776  C CD1 . ILE B 541 ? 0.2020 0.2442 0.1818 0.0609  0.0585  -0.0557 533 ILE B CD1 
8777  N N   . LYS B 542 ? 0.2049 0.2431 0.1406 0.0211  0.0317  -0.0578 534 LYS B N   
8778  C CA  A LYS B 542 ? 0.2454 0.2813 0.1788 0.0147  0.0238  -0.0562 534 LYS B CA  
8779  C CA  B LYS B 542 ? 0.2496 0.2855 0.1831 0.0148  0.0238  -0.0562 534 LYS B CA  
8780  C C   . LYS B 542 ? 0.2505 0.3001 0.1806 0.0090  0.0166  -0.0500 534 LYS B C   
8781  O O   . LYS B 542 ? 0.2097 0.2608 0.1416 0.0049  0.0096  -0.0467 534 LYS B O   
8782  C CB  A LYS B 542 ? 0.2253 0.2489 0.1474 0.0087  0.0263  -0.0663 534 LYS B CB  
8783  C CB  B LYS B 542 ? 0.2182 0.2417 0.1406 0.0089  0.0263  -0.0663 534 LYS B CB  
8784  C CG  A LYS B 542 ? 0.2717 0.2990 0.1774 0.0019  0.0289  -0.0734 534 LYS B CG  
8785  C CG  B LYS B 542 ? 0.2766 0.3038 0.1823 0.0014  0.0283  -0.0732 534 LYS B CG  
8786  C CD  A LYS B 542 ? 0.2854 0.3011 0.1791 -0.0064 0.0304  -0.0841 534 LYS B CD  
8787  C CD  B LYS B 542 ? 0.2845 0.2994 0.1790 -0.0065 0.0300  -0.0840 534 LYS B CD  
8788  C CE  A LYS B 542 ? 0.2860 0.3054 0.1611 -0.0139 0.0334  -0.0920 534 LYS B CE  
8789  C CE  B LYS B 542 ? 0.2911 0.2866 0.1863 -0.0010 0.0411  -0.0921 534 LYS B CE  
8790  N NZ  A LYS B 542 ? 0.4352 0.4414 0.2990 -0.0224 0.0355  -0.1027 534 LYS B NZ  
8791  N NZ  B LYS B 542 ? 0.2871 0.2809 0.1741 0.0017  0.0513  -0.0985 534 LYS B NZ  
8792  N N   . ARG B 543 ? 0.1965 0.2560 0.1223 0.0088  0.0187  -0.0478 535 ARG B N   
8793  C CA  . ARG B 543 ? 0.1962 0.2674 0.1189 0.0046  0.0128  -0.0402 535 ARG B CA  
8794  C C   . ARG B 543 ? 0.2023 0.2793 0.1382 0.0087  0.0107  -0.0306 535 ARG B C   
8795  O O   . ARG B 543 ? 0.1591 0.2440 0.0938 0.0064  0.0074  -0.0233 535 ARG B O   
8796  C CB  . ARG B 543 ? 0.1879 0.2653 0.0962 0.0011  0.0167  -0.0427 535 ARG B CB  
8797  C CG  . ARG B 543 ? 0.2088 0.2800 0.1012 -0.0047 0.0191  -0.0536 535 ARG B CG  
8798  C CD  . ARG B 543 ? 0.3144 0.3934 0.1891 -0.0102 0.0211  -0.0548 535 ARG B CD  
8799  N NE  . ARG B 543 ? 0.2963 0.3860 0.1652 -0.0158 0.0112  -0.0469 535 ARG B NE  
8800  C CZ  . ARG B 543 ? 0.3093 0.4035 0.1648 -0.0211 0.0093  -0.0446 535 ARG B CZ  
8801  N NH1 . ARG B 543 ? 0.2788 0.3678 0.1231 -0.0226 0.0170  -0.0508 535 ARG B NH1 
8802  N NH2 . ARG B 543 ? 0.2922 0.3954 0.1471 -0.0242 -0.0002 -0.0353 535 ARG B NH2 
8803  N N   . GLY B 544 ? 0.1526 0.2251 0.1003 0.0145  0.0127  -0.0303 536 GLY B N   
8804  C CA  . GLY B 544 ? 0.1315 0.2076 0.0908 0.0167  0.0099  -0.0228 536 GLY B CA  
8805  C C   . GLY B 544 ? 0.1887 0.2734 0.1527 0.0187  0.0140  -0.0198 536 GLY B C   
8806  O O   . GLY B 544 ? 0.1278 0.2145 0.1024 0.0213  0.0137  -0.0165 536 GLY B O   
8807  N N   . ALA B 545 ? 0.1618 0.2520 0.1176 0.0166  0.0181  -0.0209 537 ALA B N   
8808  C CA  . ALA B 545 ? 0.1607 0.2593 0.1217 0.0181  0.0236  -0.0194 537 ALA B CA  
8809  C C   . ALA B 545 ? 0.1827 0.2837 0.1332 0.0172  0.0305  -0.0248 537 ALA B C   
8810  O O   . ALA B 545 ? 0.2071 0.3049 0.1434 0.0132  0.0294  -0.0274 537 ALA B O   
8811  C CB  . ALA B 545 ? 0.1508 0.2548 0.1144 0.0146  0.0217  -0.0110 537 ALA B CB  
8812  N N   . TYR B 546 ? 0.1921 0.2994 0.1495 0.0207  0.0376  -0.0268 538 TYR B N   
8813  C CA  . TYR B 546 ? 0.2005 0.3099 0.1492 0.0205  0.0462  -0.0328 538 TYR B CA  
8814  C C   . TYR B 546 ? 0.2324 0.3536 0.1934 0.0234  0.0531  -0.0315 538 TYR B C   
8815  O O   . TYR B 546 ? 0.1934 0.3207 0.1699 0.0259  0.0507  -0.0275 538 TYR B O   
8816  C CB  . TYR B 546 ? 0.1900 0.2892 0.1347 0.0242  0.0497  -0.0420 538 TYR B CB  
8817  C CG  . TYR B 546 ? 0.1707 0.2686 0.1322 0.0327  0.0512  -0.0428 538 TYR B CG  
8818  C CD1 . TYR B 546 ? 0.1635 0.2568 0.1330 0.0346  0.0435  -0.0389 538 TYR B CD1 
8819  C CD2 . TYR B 546 ? 0.1769 0.2793 0.1466 0.0393  0.0604  -0.0466 538 TYR B CD2 
8820  C CE1 . TYR B 546 ? 0.2246 0.3175 0.2080 0.0425  0.0441  -0.0383 538 TYR B CE1 
8821  C CE2 . TYR B 546 ? 0.1714 0.2744 0.1571 0.0481  0.0610  -0.0457 538 TYR B CE2 
8822  C CZ  . TYR B 546 ? 0.1933 0.2915 0.1850 0.0496  0.0525  -0.0413 538 TYR B CZ  
8823  O OH  . TYR B 546 ? 0.1650 0.2645 0.1712 0.0585  0.0525  -0.0392 538 TYR B OH  
8824  N N   . VAL B 547 ? 0.1778 0.3032 0.1316 0.0223  0.0621  -0.0354 539 VAL B N   
8825  C CA  . VAL B 547 ? 0.1769 0.3142 0.1433 0.0245  0.0696  -0.0347 539 VAL B CA  
8826  C C   . VAL B 547 ? 0.1775 0.3142 0.1578 0.0334  0.0737  -0.0396 539 VAL B C   
8827  O O   . VAL B 547 ? 0.1928 0.3205 0.1667 0.0360  0.0801  -0.0463 539 VAL B O   
8828  C CB  . VAL B 547 ? 0.2107 0.3472 0.1648 0.0192  0.0768  -0.0353 539 VAL B CB  
8829  C CG1 . VAL B 547 ? 0.2856 0.4326 0.2547 0.0206  0.0844  -0.0341 539 VAL B CG1 
8830  C CG2 . VAL B 547 ? 0.1957 0.3312 0.1355 0.0114  0.0718  -0.0287 539 VAL B CG2 
8831  N N   . ILE B 548 ? 0.1628 0.3084 0.1621 0.0379  0.0702  -0.0358 540 ILE B N   
8832  C CA  . ILE B 548 ? 0.1644 0.3098 0.1780 0.0473  0.0729  -0.0382 540 ILE B CA  
8833  C C   . ILE B 548 ? 0.1713 0.3268 0.1973 0.0491  0.0811  -0.0383 540 ILE B C   
8834  O O   . ILE B 548 ? 0.1807 0.3333 0.2145 0.0565  0.0873  -0.0416 540 ILE B O   
8835  C CB  . ILE B 548 ? 0.1651 0.3148 0.1919 0.0516  0.0642  -0.0335 540 ILE B CB  
8836  C CG1 . ILE B 548 ? 0.1692 0.3156 0.2083 0.0620  0.0662  -0.0346 540 ILE B CG1 
8837  C CG2 . ILE B 548 ? 0.1619 0.3273 0.2007 0.0470  0.0603  -0.0273 540 ILE B CG2 
8838  C CD1 . ILE B 548 ? 0.1818 0.3271 0.2280 0.0663  0.0572  -0.0302 540 ILE B CD1 
8839  N N   . SER B 549 ? 0.2123 0.3789 0.2408 0.0424  0.0821  -0.0346 541 SER B N   
8840  C CA  . SER B 549 ? 0.2076 0.3845 0.2476 0.0429  0.0906  -0.0349 541 SER B CA  
8841  C C   . SER B 549 ? 0.2036 0.3818 0.2317 0.0335  0.0947  -0.0334 541 SER B C   
8842  O O   . SER B 549 ? 0.2045 0.3896 0.2352 0.0271  0.0904  -0.0282 541 SER B O   
8843  C CB  . SER B 549 ? 0.1939 0.3870 0.2574 0.0457  0.0865  -0.0304 541 SER B CB  
8844  O OG  . SER B 549 ? 0.1924 0.3964 0.2685 0.0464  0.0949  -0.0310 541 SER B OG  
8845  N N   . GLU B 550 ? 0.2010 0.3711 0.2151 0.0325  0.1036  -0.0377 542 GLU B N   
8846  C CA  . GLU B 550 ? 0.2108 0.3804 0.2113 0.0240  0.1077  -0.0354 542 GLU B CA  
8847  C C   . GLU B 550 ? 0.2758 0.4598 0.2924 0.0214  0.1125  -0.0318 542 GLU B C   
8848  O O   . GLU B 550 ? 0.2074 0.4016 0.2440 0.0269  0.1160  -0.0329 542 GLU B O   
8849  C CB  . GLU B 550 ? 0.2448 0.4026 0.2259 0.0238  0.1163  -0.0409 542 GLU B CB  
8850  C CG  . GLU B 550 ? 0.3449 0.5005 0.3083 0.0153  0.1195  -0.0377 542 GLU B CG  
8851  C CD  . GLU B 550 ? 0.4290 0.5807 0.3797 0.0088  0.1093  -0.0320 542 GLU B CD  
8852  O OE1 . GLU B 550 ? 0.4356 0.5772 0.3703 0.0082  0.1041  -0.0342 542 GLU B OE1 
8853  O OE2 . GLU B 550 ? 0.2301 0.3884 0.1875 0.0044  0.1067  -0.0252 542 GLU B OE2 
8854  N N   . ALA B 551 ? 0.2117 0.3960 0.2197 0.0129  0.1126  -0.0270 543 ALA B N   
8855  C CA  . ALA B 551 ? 0.2153 0.4106 0.2346 0.0088  0.1190  -0.0241 543 ALA B CA  
8856  C C   . ALA B 551 ? 0.3075 0.5040 0.3271 0.0122  0.1315  -0.0282 543 ALA B C   
8857  O O   . ALA B 551 ? 0.2577 0.4426 0.2577 0.0127  0.1364  -0.0314 543 ALA B O   
8858  C CB  . ALA B 551 ? 0.2195 0.4100 0.2252 -0.0007 0.1183  -0.0181 543 ALA B CB  
8859  N N   . GLN B 552 ? 0.2569 0.4679 0.2987 0.0144  0.1367  -0.0281 544 GLN B N   
8860  C CA  . GLN B 552 ? 0.2745 0.4888 0.3201 0.0183  0.1498  -0.0310 544 GLN B CA  
8861  C C   . GLN B 552 ? 0.3176 0.5361 0.3589 0.0101  0.1566  -0.0269 544 GLN B C   
8862  O O   . GLN B 552 ? 0.3651 0.5985 0.4259 0.0077  0.1591  -0.0244 544 GLN B O   
8863  C CB  . GLN B 552 ? 0.2925 0.5209 0.3663 0.0266  0.1518  -0.0325 544 GLN B CB  
8864  N N   . GLY B 553 ? 0.2986 0.5042 0.3139 0.0055  0.1595  -0.0261 545 GLY B N   
8865  C CA  . GLY B 553 ? 0.3050 0.5101 0.3110 -0.0033 0.1632  -0.0205 545 GLY B CA  
8866  C C   . GLY B 553 ? 0.3230 0.5154 0.3090 -0.0093 0.1544  -0.0161 545 GLY B C   
8867  O O   . GLY B 553 ? 0.2721 0.4573 0.2518 -0.0070 0.1453  -0.0178 545 GLY B O   
8868  N N   . ASN B 554 ? 0.2924 0.4817 0.2688 -0.0168 0.1576  -0.0098 546 ASN B N   
8869  C CA  . ASN B 554 ? 0.2921 0.4692 0.2505 -0.0219 0.1501  -0.0038 546 ASN B CA  
8870  C C   . ASN B 554 ? 0.2697 0.4501 0.2430 -0.0238 0.1406  -0.0012 546 ASN B C   
8871  O O   . ASN B 554 ? 0.3382 0.5270 0.3281 -0.0278 0.1426  0.0012  546 ASN B O   
8872  C CB  . ASN B 554 ? 0.4009 0.5726 0.3455 -0.0284 0.1570  0.0033  546 ASN B CB  
8873  N N   . ALA B 555 ? 0.3527 0.5264 0.3194 -0.0214 0.1305  -0.0017 547 ALA B N   
8874  C CA  . ALA B 555 ? 0.2914 0.4680 0.2712 -0.0221 0.1214  0.0002  547 ALA B CA  
8875  C C   . ALA B 555 ? 0.3545 0.5265 0.3331 -0.0299 0.1217  0.0081  547 ALA B C   
8876  O O   . ALA B 555 ? 0.3942 0.5547 0.3542 -0.0331 0.1235  0.0142  547 ALA B O   
8877  C CB  . ALA B 555 ? 0.2814 0.4507 0.2515 -0.0182 0.1115  -0.0009 547 ALA B CB  
8878  N N   . GLN B 556 ? 0.3100 0.4903 0.3081 -0.0328 0.1202  0.0082  548 GLN B N   
8879  C CA  . GLN B 556 ? 0.2300 0.4042 0.2288 -0.0403 0.1205  0.0147  548 GLN B CA  
8880  C C   . GLN B 556 ? 0.2490 0.4176 0.2491 -0.0403 0.1108  0.0163  548 GLN B C   
8881  O O   . GLN B 556 ? 0.3188 0.4773 0.3152 -0.0456 0.1111  0.0224  548 GLN B O   
8882  C CB  . GLN B 556 ? 0.2303 0.4167 0.2489 -0.0456 0.1257  0.0134  548 GLN B CB  
8883  C CG  . GLN B 556 ? 0.2887 0.4799 0.3066 -0.0473 0.1371  0.0138  548 GLN B CG  
8884  C CD  . GLN B 556 ? 0.3400 0.5443 0.3781 -0.0536 0.1416  0.0132  548 GLN B CD  
8885  O OE1 . GLN B 556 ? 0.3918 0.6119 0.4449 -0.0514 0.1453  0.0087  548 GLN B OE1 
8886  N NE2 . GLN B 556 ? 0.3504 0.5480 0.3894 -0.0616 0.1414  0.0178  548 GLN B NE2 
8887  N N   . ALA B 557 ? 0.1999 0.3738 0.2052 -0.0341 0.1032  0.0114  549 ALA B N   
8888  C CA  . ALA B 557 ? 0.1862 0.3552 0.1921 -0.0332 0.0943  0.0128  549 ALA B CA  
8889  C C   . ALA B 557 ? 0.2073 0.3800 0.2128 -0.0247 0.0879  0.0078  549 ALA B C   
8890  O O   . ALA B 557 ? 0.1970 0.3759 0.2042 -0.0199 0.0908  0.0028  549 ALA B O   
8891  C CB  . ALA B 557 ? 0.1891 0.3643 0.2124 -0.0383 0.0922  0.0118  549 ALA B CB  
8892  N N   . VAL B 558 ? 0.1644 0.3322 0.1682 -0.0228 0.0801  0.0092  550 VAL B N   
8893  C CA  . VAL B 558 ? 0.1793 0.3500 0.1850 -0.0151 0.0738  0.0046  550 VAL B CA  
8894  C C   . VAL B 558 ? 0.1652 0.3400 0.1843 -0.0152 0.0674  0.0040  550 VAL B C   
8895  O O   . VAL B 558 ? 0.1732 0.3413 0.1908 -0.0203 0.0656  0.0083  550 VAL B O   
8896  C CB  . VAL B 558 ? 0.2359 0.3960 0.2233 -0.0121 0.0702  0.0067  550 VAL B CB  
8897  C CG1 . VAL B 558 ? 0.3075 0.4573 0.2860 -0.0169 0.0684  0.0153  550 VAL B CG1 
8898  C CG2 . VAL B 558 ? 0.2137 0.3738 0.2042 -0.0053 0.0632  0.0025  550 VAL B CG2 
8899  N N   . ILE B 559 ? 0.1298 0.3145 0.1614 -0.0096 0.0644  -0.0010 551 ILE B N   
8900  C CA  . ILE B 559 ? 0.1310 0.3190 0.1723 -0.0083 0.0570  -0.0017 551 ILE B CA  
8901  C C   . ILE B 559 ? 0.1177 0.2945 0.1505 -0.0011 0.0508  -0.0026 551 ILE B C   
8902  O O   . ILE B 559 ? 0.1180 0.2956 0.1486 0.0058  0.0519  -0.0061 551 ILE B O   
8903  C CB  . ILE B 559 ? 0.1229 0.3259 0.1820 -0.0059 0.0554  -0.0051 551 ILE B CB  
8904  C CG1 . ILE B 559 ? 0.1277 0.3392 0.1949 -0.0132 0.0612  -0.0048 551 ILE B CG1 
8905  C CG2 . ILE B 559 ? 0.1018 0.3079 0.1685 -0.0062 0.0471  -0.0051 551 ILE B CG2 
8906  C CD1 . ILE B 559 ? 0.1187 0.3475 0.2040 -0.0100 0.0602  -0.0075 551 ILE B CD1 
8907  N N   . ILE B 560 ? 0.1086 0.2728 0.1365 -0.0030 0.0447  0.0003  552 ILE B N   
8908  C CA  . ILE B 560 ? 0.1042 0.2576 0.1268 0.0028  0.0379  -0.0005 552 ILE B CA  
8909  C C   . ILE B 560 ? 0.1910 0.3492 0.2248 0.0051  0.0325  -0.0023 552 ILE B C   
8910  O O   . ILE B 560 ? 0.1386 0.2997 0.1783 -0.0006 0.0312  -0.0010 552 ILE B O   
8911  C CB  . ILE B 560 ? 0.1060 0.2440 0.1177 0.0000  0.0349  0.0042  552 ILE B CB  
8912  C CG1 . ILE B 560 ? 0.1172 0.2521 0.1170 -0.0025 0.0396  0.0077  552 ILE B CG1 
8913  C CG2 . ILE B 560 ? 0.1019 0.2305 0.1093 0.0054  0.0284  0.0028  552 ILE B CG2 
8914  C CD1 . ILE B 560 ? 0.1761 0.2995 0.1695 -0.0063 0.0385  0.0148  552 ILE B CD1 
8915  N N   . ALA B 561 ? 0.0929 0.2511 0.1287 0.0129  0.0296  -0.0051 553 ALA B N   
8916  C CA  . ALA B 561 ? 0.0864 0.2485 0.1310 0.0161  0.0240  -0.0055 553 ALA B CA  
8917  C C   . ALA B 561 ? 0.1104 0.2591 0.1484 0.0224  0.0198  -0.0063 553 ALA B C   
8918  O O   . ALA B 561 ? 0.0912 0.2314 0.1207 0.0252  0.0219  -0.0081 553 ALA B O   
8919  C CB  . ALA B 561 ? 0.0860 0.2674 0.1451 0.0202  0.0258  -0.0070 553 ALA B CB  
8920  N N   . THR B 562 ? 0.0816 0.2287 0.1230 0.0238  0.0141  -0.0053 554 THR B N   
8921  C CA  . THR B 562 ? 0.0821 0.2166 0.1184 0.0293  0.0105  -0.0057 554 THR B CA  
8922  C C   . THR B 562 ? 0.0814 0.2232 0.1262 0.0351  0.0070  -0.0047 554 THR B C   
8923  O O   . THR B 562 ? 0.0981 0.2543 0.1515 0.0327  0.0049  -0.0032 554 THR B O   
8924  C CB  . THR B 562 ? 0.1010 0.2217 0.1294 0.0245  0.0070  -0.0040 554 THR B CB  
8925  O OG1 . THR B 562 ? 0.1089 0.2333 0.1412 0.0209  0.0035  -0.0024 554 THR B OG1 
8926  C CG2 . THR B 562 ? 0.1162 0.2326 0.1385 0.0185  0.0098  -0.0027 554 THR B CG2 
8927  N N   . GLY B 563 ? 0.1263 0.2230 0.1328 0.0433  0.0365  -0.0038 555 GLY B N   
8928  C CA  . GLY B 563 ? 0.1404 0.2299 0.1449 0.0502  0.0373  -0.0050 555 GLY B CA  
8929  C C   . GLY B 563 ? 0.1549 0.2561 0.1614 0.0533  0.0359  -0.0056 555 GLY B C   
8930  O O   . GLY B 563 ? 0.1313 0.2457 0.1406 0.0530  0.0367  -0.0075 555 GLY B O   
8931  N N   . SER B 564 ? 0.1731 0.2702 0.1783 0.0564  0.0336  -0.0043 556 SER B N   
8932  C CA  . SER B 564 ? 0.1853 0.2930 0.1928 0.0605  0.0314  -0.0055 556 SER B CA  
8933  C C   . SER B 564 ? 0.1764 0.3013 0.1905 0.0544  0.0296  -0.0049 556 SER B C   
8934  O O   . SER B 564 ? 0.1619 0.2989 0.1800 0.0572  0.0282  -0.0071 556 SER B O   
8935  C CB  . SER B 564 ? 0.1744 0.2736 0.1783 0.0645  0.0287  -0.0042 556 SER B CB  
8936  O OG  . SER B 564 ? 0.1724 0.2662 0.1763 0.0584  0.0269  -0.0012 556 SER B OG  
8937  N N   . GLU B 565 ? 0.1302 0.2563 0.1456 0.0463  0.0295  -0.0022 557 GLU B N   
8938  C CA  . GLU B 565 ? 0.1362 0.2770 0.1570 0.0399  0.0285  -0.0011 557 GLU B CA  
8939  C C   . GLU B 565 ? 0.1147 0.2670 0.1369 0.0374  0.0315  -0.0026 557 GLU B C   
8940  O O   . GLU B 565 ? 0.1290 0.2941 0.1554 0.0321  0.0318  -0.0019 557 GLU B O   
8941  C CB  . GLU B 565 ? 0.1485 0.2840 0.1696 0.0324  0.0265  0.0034  557 GLU B CB  
8942  C CG  . GLU B 565 ? 0.1171 0.2477 0.1393 0.0329  0.0232  0.0042  557 GLU B CG  
8943  C CD  . GLU B 565 ? 0.1828 0.2992 0.1996 0.0397  0.0229  0.0032  557 GLU B CD  
8944  O OE1 . GLU B 565 ? 0.1594 0.2629 0.1727 0.0385  0.0238  0.0048  557 GLU B OE1 
8945  O OE2 . GLU B 565 ? 0.1564 0.2745 0.1722 0.0465  0.0220  0.0007  557 GLU B OE2 
8946  N N   . VAL B 566 ? 0.1104 0.2587 0.1294 0.0408  0.0343  -0.0049 558 VAL B N   
8947  C CA  . VAL B 566 ? 0.1111 0.2711 0.1309 0.0385  0.0373  -0.0069 558 VAL B CA  
8948  C C   . VAL B 566 ? 0.1777 0.3538 0.2031 0.0409  0.0383  -0.0105 558 VAL B C   
8949  O O   . VAL B 566 ? 0.1202 0.3099 0.1483 0.0358  0.0401  -0.0108 558 VAL B O   
8950  C CB  . VAL B 566 ? 0.1333 0.2859 0.1491 0.0420  0.0400  -0.0099 558 VAL B CB  
8951  C CG1 . VAL B 566 ? 0.1557 0.3203 0.1719 0.0402  0.0428  -0.0130 558 VAL B CG1 
8952  C CG2 . VAL B 566 ? 0.1513 0.2912 0.1631 0.0385  0.0390  -0.0070 558 VAL B CG2 
8953  N N   . GLY B 567 ? 0.1804 0.3554 0.2077 0.0489  0.0371  -0.0134 559 GLY B N   
8954  C CA  . GLY B 567 ? 0.2006 0.3882 0.2337 0.0511  0.0364  -0.0171 559 GLY B CA  
8955  C C   . GLY B 567 ? 0.1889 0.3913 0.2285 0.0448  0.0356  -0.0159 559 GLY B C   
8956  O O   . GLY B 567 ? 0.1725 0.3869 0.2165 0.0411  0.0368  -0.0181 559 GLY B O   
8957  N N   . LEU B 568 ? 0.1192 0.3155 0.1585 0.0422  0.0326  -0.0123 560 LEU B N   
8958  C CA  . LEU B 568 ? 0.1752 0.3815 0.2204 0.0348  0.0314  -0.0109 560 LEU B CA  
8959  C C   . LEU B 568 ? 0.1430 0.3556 0.1879 0.0255  0.0350  -0.0083 560 LEU B C   
8960  O O   . LEU B 568 ? 0.1116 0.3390 0.1628 0.0203  0.0367  -0.0094 560 LEU B O   
8961  C CB  . LEU B 568 ? 0.1291 0.3232 0.1723 0.0331  0.0275  -0.0072 560 LEU B CB  
8962  C CG  . LEU B 568 ? 0.1227 0.3216 0.1707 0.0241  0.0264  -0.0047 560 LEU B CG  
8963  C CD1 . LEU B 568 ? 0.1550 0.3726 0.2131 0.0236  0.0261  -0.0092 560 LEU B CD1 
8964  C CD2 . LEU B 568 ? 0.1637 0.3482 0.2088 0.0239  0.0227  -0.0018 560 LEU B CD2 
8965  N N   . ALA B 569 ? 0.1089 0.3107 0.1463 0.0233  0.0362  -0.0050 561 ALA B N   
8966  C CA  . ALA B 569 ? 0.1460 0.3527 0.1810 0.0152  0.0391  -0.0019 561 ALA B CA  
8967  C C   . ALA B 569 ? 0.1892 0.4106 0.2263 0.0153  0.0432  -0.0063 561 ALA B C   
8968  O O   . ALA B 569 ? 0.1177 0.3473 0.1558 0.0081  0.0454  -0.0051 561 ALA B O   
8969  C CB  . ALA B 569 ? 0.1344 0.3271 0.1610 0.0142  0.0387  0.0016  561 ALA B CB  
8970  N N   . VAL B 570 ? 0.1261 0.3443 0.1622 0.0228  0.0430  -0.0111 562 VAL B N   
8971  C CA  . VAL B 570 ? 0.1381 0.3637 0.1752 0.0228  0.0452  -0.0154 562 VAL B CA  
8972  C C   . VAL B 570 ? 0.1401 0.3790 0.1860 0.0219  0.0452  -0.0187 562 VAL B C   
8973  O O   . VAL B 570 ? 0.1596 0.4079 0.2074 0.0175  0.0479  -0.0204 562 VAL B O   
8974  C CB  . VAL B 570 ? 0.1441 0.3617 0.1787 0.0307  0.0451  -0.0197 562 VAL B CB  
8975  C CG1 . VAL B 570 ? 0.2229 0.4491 0.2603 0.0316  0.0473  -0.0249 562 VAL B CG1 
8976  C CG2 . VAL B 570 ? 0.1232 0.3296 0.1499 0.0300  0.0458  -0.0176 562 VAL B CG2 
8977  N N   . GLU B 571 ? 0.1307 0.3709 0.1822 0.0262  0.0420  -0.0198 563 GLU B N   
8978  C CA  . GLU B 571 ? 0.1574 0.4111 0.2183 0.0250  0.0413  -0.0233 563 GLU B CA  
8979  C C   . GLU B 571 ? 0.1201 0.3814 0.1838 0.0142  0.0436  -0.0202 563 GLU B C   
8980  O O   . GLU B 571 ? 0.1496 0.4222 0.2189 0.0101  0.0459  -0.0231 563 GLU B O   
8981  C CB  . GLU B 571 ? 0.1482 0.4011 0.2134 0.0320  0.0366  -0.0250 563 GLU B CB  
8982  C CG  . GLU B 571 ? 0.3213 0.5695 0.3855 0.0429  0.0344  -0.0291 563 GLU B CG  
8983  C CD  . GLU B 571 ? 0.4672 0.7123 0.5328 0.0502  0.0294  -0.0297 563 GLU B CD  
8984  O OE1 . GLU B 571 ? 0.5489 0.7803 0.6077 0.0548  0.0282  -0.0269 563 GLU B OE1 
8985  O OE2 . GLU B 571 ? 0.5725 0.8288 0.6458 0.0514  0.0267  -0.0334 563 GLU B OE2 
8986  N N   . ALA B 572 ? 0.1169 0.3715 0.1771 0.0094  0.0433  -0.0142 564 ALA B N   
8987  C CA  . ALA B 572 ? 0.1193 0.3779 0.1808 -0.0014 0.0458  -0.0101 564 ALA B CA  
8988  C C   . ALA B 572 ? 0.1269 0.3871 0.1827 -0.0069 0.0503  -0.0089 564 ALA B C   
8989  O O   . ALA B 572 ? 0.1823 0.4499 0.2412 -0.0144 0.0534  -0.0085 564 ALA B O   
8990  C CB  . ALA B 572 ? 0.1155 0.3643 0.1732 -0.0047 0.0443  -0.0034 564 ALA B CB  
8991  N N   . GLN B 573 ? 0.1281 0.3814 0.1755 -0.0033 0.0508  -0.0085 565 GLN B N   
8992  C CA  . GLN B 573 ? 0.1360 0.3913 0.1774 -0.0075 0.0546  -0.0081 565 GLN B CA  
8993  C C   . GLN B 573 ? 0.1752 0.4429 0.2232 -0.0076 0.0572  -0.0141 565 GLN B C   
8994  O O   . GLN B 573 ? 0.1634 0.4364 0.2098 -0.0145 0.0613  -0.0132 565 GLN B O   
8995  C CB  . GLN B 573 ? 0.1361 0.3829 0.1692 -0.0023 0.0540  -0.0087 565 GLN B CB  
8996  C CG  . GLN B 573 ? 0.1448 0.3946 0.1715 -0.0054 0.0575  -0.0095 565 GLN B CG  
8997  C CD  . GLN B 573 ? 0.1527 0.3955 0.1737 0.0006  0.0567  -0.0123 565 GLN B CD  
8998  O OE1 . GLN B 573 ? 0.1866 0.4272 0.2117 0.0081  0.0551  -0.0170 565 GLN B OE1 
8999  N NE2 . GLN B 573 ? 0.1617 0.4006 0.1732 -0.0026 0.0576  -0.0093 565 GLN B NE2 
9000  N N   . LYS B 574 ? 0.1375 0.4093 0.1926 0.0001  0.0551  -0.0203 566 LYS B N   
9001  C CA  . LYS B 574 ? 0.1890 0.4728 0.2511 0.0008  0.0572  -0.0265 566 LYS B CA  
9002  C C   . LYS B 574 ? 0.1901 0.4847 0.2612 -0.0055 0.0585  -0.0273 566 LYS B C   
9003  O O   . LYS B 574 ? 0.1509 0.4553 0.2258 -0.0096 0.0625  -0.0303 566 LYS B O   
9004  C CB  . LYS B 574 ? 0.2561 0.5400 0.3225 0.0115  0.0541  -0.0324 566 LYS B CB  
9005  C CG  . LYS B 574 ? 0.3725 0.6498 0.4321 0.0160  0.0551  -0.0341 566 LYS B CG  
9006  C CD  . LYS B 574 ? 0.4441 0.7108 0.5021 0.0256  0.0514  -0.0352 566 LYS B CD  
9007  C CE  . LYS B 574 ? 0.4622 0.7200 0.5125 0.0277  0.0529  -0.0356 566 LYS B CE  
9008  N NZ  . LYS B 574 ? 0.3824 0.6360 0.4243 0.0204  0.0548  -0.0304 566 LYS B NZ  
9009  N N   . VAL B 575 ? 0.1916 0.4846 0.2667 -0.0067 0.0556  -0.0250 567 VAL B N   
9010  C CA  . VAL B 575 ? 0.2113 0.5132 0.2952 -0.0140 0.0570  -0.0256 567 VAL B CA  
9011  C C   . VAL B 575 ? 0.1788 0.4786 0.2571 -0.0249 0.0622  -0.0199 567 VAL B C   
9012  O O   . VAL B 575 ? 0.1942 0.5026 0.2775 -0.0313 0.0664  -0.0217 567 VAL B O   
9013  C CB  . VAL B 575 ? 0.1787 0.4784 0.2678 -0.0127 0.0522  -0.0246 567 VAL B CB  
9014  C CG1 . VAL B 575 ? 0.1969 0.5035 0.2943 -0.0219 0.0541  -0.0244 567 VAL B CG1 
9015  C CG2 . VAL B 575 ? 0.1767 0.4800 0.2715 -0.0018 0.0471  -0.0307 567 VAL B CG2 
9016  N N   . LEU B 576 ? 0.1642 0.4519 0.2318 -0.0271 0.0621  -0.0128 568 LEU B N   
9017  C CA  . LEU B 576 ? 0.1572 0.4407 0.2170 -0.0364 0.0666  -0.0065 568 LEU B CA  
9018  C C   . LEU B 576 ? 0.2166 0.5061 0.2728 -0.0380 0.0715  -0.0091 568 LEU B C   
9019  O O   . LEU B 576 ? 0.2622 0.5549 0.3179 -0.0461 0.0765  -0.0072 568 LEU B O   
9020  C CB  . LEU B 576 ? 0.1555 0.4251 0.2038 -0.0364 0.0645  0.0009  568 LEU B CB  
9021  C CG  . LEU B 576 ? 0.2327 0.4957 0.2839 -0.0380 0.0610  0.0051  568 LEU B CG  
9022  C CD1 . LEU B 576 ? 0.1548 0.4054 0.1970 -0.0340 0.0577  0.0098  568 LEU B CD1 
9023  C CD2 . LEU B 576 ? 0.1572 0.4182 0.2091 -0.0487 0.0641  0.0104  568 LEU B CD2 
9024  N N   . ALA B 577 ? 0.2263 0.5167 0.2799 -0.0305 0.0704  -0.0134 569 ALA B N   
9025  C CA  . ALA B 577 ? 0.2154 0.5119 0.2660 -0.0317 0.0749  -0.0165 569 ALA B CA  
9026  C C   . ALA B 577 ? 0.2554 0.5657 0.3173 -0.0344 0.0784  -0.0223 569 ALA B C   
9027  O O   . ALA B 577 ? 0.2452 0.5607 0.3051 -0.0401 0.0840  -0.0226 569 ALA B O   
9028  C CB  . ALA B 577 ? 0.1894 0.4839 0.2371 -0.0227 0.0728  -0.0210 569 ALA B CB  
9029  N N   . GLY B 578 ? 0.2012 0.5178 0.2751 -0.0303 0.0751  -0.0271 570 GLY B N   
9030  C CA  . GLY B 578 ? 0.2411 0.5715 0.3272 -0.0333 0.0777  -0.0328 570 GLY B CA  
9031  C C   . GLY B 578 ? 0.2464 0.5779 0.3340 -0.0445 0.0823  -0.0288 570 GLY B C   
9032  O O   . GLY B 578 ? 0.2902 0.6327 0.3858 -0.0489 0.0866  -0.0329 570 GLY B O   
9033  N N   . GLN B 579 ? 0.2343 0.5545 0.3150 -0.0491 0.0816  -0.0209 571 GLN B N   
9034  C CA  . GLN B 579 ? 0.2484 0.5664 0.3287 -0.0599 0.0862  -0.0159 571 GLN B CA  
9035  C C   . GLN B 579 ? 0.3232 0.6330 0.3888 -0.0656 0.0911  -0.0090 571 GLN B C   
9036  O O   . GLN B 579 ? 0.3670 0.6704 0.4288 -0.0741 0.0945  -0.0026 571 GLN B O   
9037  C CB  . GLN B 579 ? 0.3046 0.6146 0.3870 -0.0620 0.0823  -0.0114 571 GLN B CB  
9038  C CG  . GLN B 579 ? 0.3696 0.6869 0.4651 -0.0562 0.0768  -0.0179 571 GLN B CG  
9039  C CD  . GLN B 579 ? 0.4297 0.7386 0.5265 -0.0582 0.0729  -0.0135 571 GLN B CD  
9040  O OE1 . GLN B 579 ? 0.4196 0.7196 0.5115 -0.0663 0.0755  -0.0065 571 GLN B OE1 
9041  N NE2 . GLN B 579 ? 0.4744 0.7855 0.5774 -0.0506 0.0667  -0.0175 571 GLN B NE2 
9042  N N   . GLY B 580 ? 0.2924 0.6016 0.3495 -0.0608 0.0914  -0.0101 572 GLY B N   
9043  C CA  . GLY B 580 ? 0.3200 0.6221 0.3624 -0.0653 0.0954  -0.0042 572 GLY B CA  
9044  C C   . GLY B 580 ? 0.3141 0.6011 0.3439 -0.0655 0.0920  0.0045  572 GLY B C   
9045  O O   . GLY B 580 ? 0.2898 0.5696 0.3067 -0.0701 0.0950  0.0107  572 GLY B O   
9046  N N   . ILE B 581 ? 0.2374 0.5193 0.2701 -0.0604 0.0858  0.0050  573 ILE B N   
9047  C CA  . ILE B 581 ? 0.2882 0.5564 0.3106 -0.0601 0.0821  0.0126  573 ILE B CA  
9048  C C   . ILE B 581 ? 0.2603 0.5264 0.2782 -0.0510 0.0779  0.0097  573 ILE B C   
9049  O O   . ILE B 581 ? 0.2249 0.4926 0.2502 -0.0442 0.0738  0.0054  573 ILE B O   
9050  C CB  . ILE B 581 ? 0.2849 0.5481 0.3142 -0.0618 0.0787  0.0156  573 ILE B CB  
9051  C CG1 . ILE B 581 ? 0.2815 0.5489 0.3189 -0.0703 0.0831  0.0160  573 ILE B CG1 
9052  C CG2 . ILE B 581 ? 0.2444 0.4927 0.2625 -0.0627 0.0756  0.0244  573 ILE B CG2 
9053  C CD1 . ILE B 581 ? 0.3127 0.5741 0.3562 -0.0731 0.0800  0.0191  573 ILE B CD1 
9054  N N   . ALA B 582 ? 0.2352 0.4972 0.2407 -0.0508 0.0790  0.0120  574 ALA B N   
9055  C CA  . ALA B 582 ? 0.1941 0.4530 0.1951 -0.0429 0.0752  0.0093  574 ALA B CA  
9056  C C   . ALA B 582 ? 0.2255 0.4724 0.2206 -0.0415 0.0703  0.0155  574 ALA B C   
9057  O O   . ALA B 582 ? 0.2422 0.4812 0.2285 -0.0468 0.0705  0.0233  574 ALA B O   
9058  C CB  . ALA B 582 ? 0.2049 0.4654 0.1957 -0.0432 0.0780  0.0083  574 ALA B CB  
9059  N N   . VAL B 583 ? 0.1763 0.4212 0.1764 -0.0341 0.0662  0.0121  575 VAL B N   
9060  C CA  . VAL B 583 ? 0.1837 0.4179 0.1789 -0.0318 0.0618  0.0167  575 VAL B CA  
9061  C C   . VAL B 583 ? 0.1648 0.3972 0.1587 -0.0235 0.0594  0.0114  575 VAL B C   
9062  O O   . VAL B 583 ? 0.1947 0.4329 0.1945 -0.0186 0.0602  0.0042  575 VAL B O   
9063  C CB  . VAL B 583 ? 0.2365 0.4676 0.2399 -0.0321 0.0592  0.0190  575 VAL B CB  
9064  C CG1 . VAL B 583 ? 0.2324 0.4654 0.2389 -0.0408 0.0619  0.0231  575 VAL B CG1 
9065  C CG2 . VAL B 583 ? 0.1511 0.3874 0.1653 -0.0248 0.0576  0.0116  575 VAL B CG2 
9066  N N   . ARG B 584 ? 0.1641 0.3878 0.1503 -0.0221 0.0566  0.0151  576 ARG B N   
9067  C CA  . ARG B 584 ? 0.1722 0.3923 0.1575 -0.0148 0.0544  0.0104  576 ARG B CA  
9068  C C   . ARG B 584 ? 0.1755 0.3897 0.1674 -0.0103 0.0514  0.0102  576 ARG B C   
9069  O O   . ARG B 584 ? 0.1450 0.3556 0.1380 -0.0136 0.0501  0.0159  576 ARG B O   
9070  C CB  . ARG B 584 ? 0.1842 0.3993 0.1577 -0.0159 0.0530  0.0137  576 ARG B CB  
9071  C CG  . ARG B 584 ? 0.2613 0.4692 0.2336 -0.0106 0.0496  0.0124  576 ARG B CG  
9072  C CD  . ARG B 584 ? 0.2312 0.4354 0.1915 -0.0129 0.0476  0.0172  576 ARG B CD  
9073  N NE  . ARG B 584 ? 0.2161 0.4258 0.1694 -0.0136 0.0492  0.0139  576 ARG B NE  
9074  C CZ  . ARG B 584 ? 0.1986 0.4066 0.1418 -0.0133 0.0470  0.0147  576 ARG B CZ  
9075  N NH1 . ARG B 584 ? 0.1896 0.3903 0.1292 -0.0123 0.0427  0.0187  576 ARG B NH1 
9076  N NH2 . ARG B 584 ? 0.2291 0.4427 0.1664 -0.0137 0.0487  0.0111  576 ARG B NH2 
9077  N N   . VAL B 585 ? 0.1790 0.3915 0.1752 -0.0029 0.0506  0.0039  577 VAL B N   
9078  C CA  . VAL B 585 ? 0.1758 0.3809 0.1763 0.0021  0.0481  0.0036  577 VAL B CA  
9079  C C   . VAL B 585 ? 0.1318 0.3285 0.1273 0.0060  0.0468  0.0020  577 VAL B C   
9080  O O   . VAL B 585 ? 0.1343 0.3313 0.1286 0.0095  0.0478  -0.0036 577 VAL B O   
9081  C CB  . VAL B 585 ? 0.1579 0.3651 0.1671 0.0081  0.0481  -0.0020 577 VAL B CB  
9082  C CG1 . VAL B 585 ? 0.1409 0.3384 0.1526 0.0134  0.0456  -0.0017 577 VAL B CG1 
9083  C CG2 . VAL B 585 ? 0.1287 0.3457 0.1443 0.0042  0.0491  -0.0015 577 VAL B CG2 
9084  N N   . VAL B 586 ? 0.1304 0.3137 0.1243 0.0054  0.0426  0.0062  578 VAL B N   
9085  C CA  . VAL B 586 ? 0.1296 0.3025 0.1208 0.0088  0.0404  0.0043  578 VAL B CA  
9086  C C   . VAL B 586 ? 0.1333 0.2958 0.1302 0.0141  0.0391  0.0021  578 VAL B C   
9087  O O   . VAL B 586 ? 0.1482 0.3057 0.1484 0.0131  0.0370  0.0056  578 VAL B O   
9088  C CB  . VAL B 586 ? 0.1338 0.2997 0.1192 0.0045  0.0367  0.0101  578 VAL B CB  
9089  C CG1 . VAL B 586 ? 0.1312 0.2850 0.1171 0.0080  0.0336  0.0082  578 VAL B CG1 
9090  C CG2 . VAL B 586 ? 0.1426 0.3178 0.1195 0.0007  0.0383  0.0114  578 VAL B CG2 
9091  N N   . SER B 587 ? 0.1288 0.2879 0.1267 0.0197  0.0406  -0.0038 579 SER B N   
9092  C CA  . SER B 587 ? 0.1580 0.3044 0.1591 0.0245  0.0398  -0.0055 579 SER B CA  
9093  C C   . SER B 587 ? 0.1185 0.2540 0.1176 0.0234  0.0373  -0.0046 579 SER B C   
9094  O O   . SER B 587 ? 0.1374 0.2750 0.1336 0.0227  0.0376  -0.0071 579 SER B O   
9095  C CB  . SER B 587 ? 0.1302 0.2767 0.1332 0.0311  0.0432  -0.0121 579 SER B CB  
9096  O OG  . SER B 587 ? 0.1374 0.2706 0.1421 0.0357  0.0430  -0.0130 579 SER B OG  
9097  N N   . MET B 588 ? 0.1285 0.2532 0.1295 0.0231  0.0348  -0.0015 580 MET B N   
9098  C CA  . MET B 588 ? 0.1156 0.2302 0.1165 0.0222  0.0325  -0.0011 580 MET B CA  
9099  C C   . MET B 588 ? 0.1133 0.2156 0.1173 0.0265  0.0339  -0.0040 580 MET B C   
9100  O O   . MET B 588 ? 0.1328 0.2266 0.1384 0.0260  0.0322  -0.0012 580 MET B O   
9101  C CB  . MET B 588 ? 0.1474 0.2598 0.1477 0.0173  0.0284  0.0054  580 MET B CB  
9102  C CG  . MET B 588 ? 0.1388 0.2423 0.1397 0.0165  0.0252  0.0057  580 MET B CG  
9103  S SD  . MET B 588 ? 0.1406 0.2429 0.1397 0.0111  0.0202  0.0137  580 MET B SD  
9104  C CE  . MET B 588 ? 0.1430 0.2584 0.1345 0.0079  0.0205  0.0159  580 MET B CE  
9105  N N   . PRO B 589 ? 0.1288 0.2292 0.1331 0.0308  0.0375  -0.0098 581 PRO B N   
9106  C CA  . PRO B 589 ? 0.1306 0.2178 0.1364 0.0348  0.0398  -0.0122 581 PRO B CA  
9107  C C   . PRO B 589 ? 0.1644 0.2411 0.1723 0.0329  0.0386  -0.0123 581 PRO B C   
9108  O O   . PRO B 589 ? 0.1508 0.2162 0.1596 0.0349  0.0400  -0.0125 581 PRO B O   
9109  C CB  . PRO B 589 ? 0.1886 0.2763 0.1944 0.0389  0.0442  -0.0185 581 PRO B CB  
9110  C CG  . PRO B 589 ? 0.1920 0.2917 0.1966 0.0360  0.0435  -0.0204 581 PRO B CG  
9111  C CD  . PRO B 589 ? 0.1176 0.2270 0.1205 0.0321  0.0402  -0.0144 581 PRO B CD  
9112  N N   . SER B 590 ? 0.1139 0.1942 0.1224 0.0294  0.0358  -0.0124 582 SER B N   
9113  C CA  . SER B 590 ? 0.1402 0.2119 0.1520 0.0277  0.0339  -0.0127 582 SER B CA  
9114  C C   . SER B 590 ? 0.1820 0.2594 0.1932 0.0236  0.0285  -0.0086 582 SER B C   
9115  O O   . SER B 590 ? 0.1432 0.2279 0.1528 0.0225  0.0270  -0.0104 582 SER B O   
9116  C CB  . SER B 590 ? 0.1350 0.2017 0.1500 0.0291  0.0369  -0.0199 582 SER B CB  
9117  O OG  . SER B 590 ? 0.1213 0.1814 0.1407 0.0273  0.0349  -0.0206 582 SER B OG  
9118  N N   . THR B 591 ? 0.1399 0.2132 0.1520 0.0216  0.0255  -0.0032 583 THR B N   
9119  C CA  . THR B 591 ? 0.1349 0.2102 0.1469 0.0182  0.0203  0.0008  583 THR B CA  
9120  C C   . THR B 591 ? 0.1465 0.2189 0.1621 0.0187  0.0185  -0.0036 583 THR B C   
9121  O O   . THR B 591 ? 0.1266 0.2043 0.1403 0.0173  0.0144  -0.0024 583 THR B O   
9122  C CB  . THR B 591 ? 0.1436 0.2126 0.1574 0.0164  0.0180  0.0062  583 THR B CB  
9123  O OG1 . THR B 591 ? 0.1337 0.1921 0.1523 0.0181  0.0196  0.0031  583 THR B OG1 
9124  C CG2 . THR B 591 ? 0.1252 0.1982 0.1366 0.0158  0.0195  0.0097  583 THR B CG2 
9125  N N   . SER B 592 ? 0.1189 0.1828 0.1397 0.0206  0.0215  -0.0087 584 SER B N   
9126  C CA  . SER B 592 ? 0.1630 0.2242 0.1896 0.0206  0.0201  -0.0139 584 SER B CA  
9127  C C   . SER B 592 ? 0.1683 0.2385 0.1934 0.0210  0.0194  -0.0185 584 SER B C   
9128  O O   . SER B 592 ? 0.1290 0.2033 0.1554 0.0202  0.0146  -0.0194 584 SER B O   
9129  C CB  . SER B 592 ? 0.1106 0.1612 0.1425 0.0222  0.0254  -0.0191 584 SER B CB  
9130  O OG  . SER B 592 ? 0.1490 0.1927 0.1788 0.0228  0.0278  -0.0152 584 SER B OG  
9131  N N   . VAL B 593 ? 0.1161 0.1896 0.1382 0.0225  0.0240  -0.0217 585 VAL B N   
9132  C CA  . VAL B 593 ? 0.1243 0.2066 0.1449 0.0228  0.0240  -0.0271 585 VAL B CA  
9133  C C   . VAL B 593 ? 0.1606 0.2536 0.1738 0.0211  0.0194  -0.0220 585 VAL B C   
9134  O O   . VAL B 593 ? 0.1484 0.2483 0.1600 0.0207  0.0160  -0.0247 585 VAL B O   
9135  C CB  . VAL B 593 ? 0.1200 0.2019 0.1397 0.0251  0.0306  -0.0319 585 VAL B CB  
9136  C CG1 . VAL B 593 ? 0.1300 0.2219 0.1478 0.0253  0.0308  -0.0379 585 VAL B CG1 
9137  C CG2 . VAL B 593 ? 0.1260 0.1955 0.1518 0.0267  0.0357  -0.0365 585 VAL B CG2 
9138  N N   . PHE B 594 ? 0.1226 0.2175 0.1309 0.0200  0.0195  -0.0149 586 PHE B N   
9139  C CA  . PHE B 594 ? 0.1275 0.2320 0.1281 0.0178  0.0164  -0.0098 586 PHE B CA  
9140  C C   . PHE B 594 ? 0.1439 0.2477 0.1434 0.0164  0.0098  -0.0063 586 PHE B C   
9141  O O   . PHE B 594 ? 0.1398 0.2512 0.1331 0.0156  0.0066  -0.0057 586 PHE B O   
9142  C CB  . PHE B 594 ? 0.1300 0.2360 0.1272 0.0161  0.0178  -0.0030 586 PHE B CB  
9143  C CG  . PHE B 594 ? 0.1432 0.2581 0.1323 0.0130  0.0157  0.0026  586 PHE B CG  
9144  C CD1 . PHE B 594 ? 0.1377 0.2629 0.1211 0.0131  0.0173  -0.0005 586 PHE B CD1 
9145  C CD2 . PHE B 594 ? 0.1353 0.2476 0.1221 0.0100  0.0125  0.0108  586 PHE B CD2 
9146  C CE1 . PHE B 594 ? 0.1507 0.2839 0.1254 0.0099  0.0161  0.0048  586 PHE B CE1 
9147  C CE2 . PHE B 594 ? 0.1431 0.2622 0.1216 0.0067  0.0114  0.0164  586 PHE B CE2 
9148  C CZ  . PHE B 594 ? 0.1989 0.3287 0.1708 0.0067  0.0133  0.0135  586 PHE B CZ  
9149  N N   . ASP B 595 ? 0.1305 0.2250 0.1357 0.0163  0.0075  -0.0043 587 ASP B N   
9150  C CA  . ASP B 595 ? 0.1842 0.2769 0.1894 0.0156  0.0008  -0.0006 587 ASP B CA  
9151  C C   . ASP B 595 ? 0.2001 0.2971 0.2074 0.0174  -0.0026 -0.0071 587 ASP B C   
9152  O O   . ASP B 595 ? 0.1845 0.2828 0.1893 0.0175  -0.0091 -0.0041 587 ASP B O   
9153  C CB  . ASP B 595 ? 0.2494 0.3313 0.2621 0.0156  -0.0002 0.0014  587 ASP B CB  
9154  C CG  . ASP B 595 ? 0.3447 0.4231 0.3552 0.0135  0.0013  0.0085  587 ASP B CG  
9155  O OD1 . ASP B 595 ? 0.3397 0.4239 0.3428 0.0114  0.0014  0.0137  587 ASP B OD1 
9156  O OD2 . ASP B 595 ? 0.3312 0.4012 0.3475 0.0137  0.0026  0.0085  587 ASP B OD2 
9157  N N   . ARG B 596 ? 0.1524 0.2509 0.1643 0.0189  0.0013  -0.0162 588 ARG B N   
9158  C CA  . ARG B 596 ? 0.2200 0.3239 0.2351 0.0203  -0.0015 -0.0241 588 ARG B CA  
9159  C C   . ARG B 596 ? 0.1974 0.3128 0.2034 0.0203  -0.0024 -0.0258 588 ARG B C   
9160  O O   . ARG B 596 ? 0.2339 0.3553 0.2409 0.0214  -0.0061 -0.0318 588 ARG B O   
9161  C CB  . ARG B 596 ? 0.2193 0.3189 0.2445 0.0213  0.0039  -0.0339 588 ARG B CB  
9162  C CG  . ARG B 596 ? 0.2959 0.3847 0.3308 0.0214  0.0051  -0.0348 588 ARG B CG  
9163  C CD  . ARG B 596 ? 0.3147 0.4010 0.3596 0.0219  0.0094  -0.0457 588 ARG B CD  
9164  N NE  . ARG B 596 ? 0.3150 0.3983 0.3589 0.0223  0.0174  -0.0495 588 ARG B NE  
9165  C CZ  . ARG B 596 ? 0.2962 0.3693 0.3408 0.0225  0.0233  -0.0475 588 ARG B CZ  
9166  N NH1 . ARG B 596 ? 0.2497 0.3156 0.2960 0.0220  0.0221  -0.0421 588 ARG B NH1 
9167  N NH2 . ARG B 596 ? 0.3560 0.4260 0.3993 0.0236  0.0301  -0.0509 588 ARG B NH2 
9168  N N   . GLN B 597 ? 0.1600 0.2793 0.1579 0.0191  0.0011  -0.0216 589 GLN B N   
9169  C CA  . GLN B 597 ? 0.1512 0.2818 0.1403 0.0189  0.0010  -0.0237 589 GLN B CA  
9170  C C   . GLN B 597 ? 0.1611 0.2964 0.1411 0.0183  -0.0064 -0.0180 589 GLN B C   
9171  O O   . GLN B 597 ? 0.2056 0.3351 0.1843 0.0176  -0.0104 -0.0099 589 GLN B O   
9172  C CB  . GLN B 597 ? 0.1956 0.3298 0.1790 0.0176  0.0068  -0.0206 589 GLN B CB  
9173  C CG  . GLN B 597 ? 0.1995 0.3282 0.1905 0.0190  0.0137  -0.0248 589 GLN B CG  
9174  C CD  . GLN B 597 ? 0.2088 0.3365 0.2069 0.0211  0.0162  -0.0357 589 GLN B CD  
9175  O OE1 . GLN B 597 ? 0.1893 0.3252 0.1847 0.0216  0.0174  -0.0419 589 GLN B OE1 
9176  N NE2 . GLN B 597 ? 0.1539 0.2714 0.1612 0.0220  0.0175  -0.0384 589 GLN B NE2 
9177  N N   . ASP B 598 ? 0.1689 0.3144 0.1418 0.0189  -0.0080 -0.0221 590 ASP B N   
9178  C CA  . ASP B 598 ? 0.3378 0.4879 0.2998 0.0189  -0.0152 -0.0168 590 ASP B CA  
9179  C C   . ASP B 598 ? 0.2683 0.4172 0.2191 0.0160  -0.0144 -0.0050 590 ASP B C   
9180  O O   . ASP B 598 ? 0.2019 0.3508 0.1524 0.0139  -0.0079 -0.0028 590 ASP B O   
9181  C CB  . ASP B 598 ? 0.3200 0.4820 0.2755 0.0200  -0.0166 -0.0244 590 ASP B CB  
9182  C CG  . ASP B 598 ? 0.4005 0.5696 0.3510 0.0185  -0.0091 -0.0273 590 ASP B CG  
9183  O OD1 . ASP B 598 ? 0.3563 0.5290 0.2952 0.0163  -0.0075 -0.0200 590 ASP B OD1 
9184  O OD2 . ASP B 598 ? 0.4822 0.6531 0.4407 0.0195  -0.0044 -0.0372 590 ASP B OD2 
9185  N N   . ALA B 599 ? 0.2608 0.4084 0.2028 0.0161  -0.0210 0.0026  591 ALA B N   
9186  C CA  . ALA B 599 ? 0.2506 0.3949 0.1826 0.0129  -0.0203 0.0145  591 ALA B CA  
9187  C C   . ALA B 599 ? 0.2951 0.4485 0.2170 0.0100  -0.0140 0.0153  591 ALA B C   
9188  O O   . ALA B 599 ? 0.2303 0.3819 0.1503 0.0065  -0.0092 0.0215  591 ALA B O   
9189  C CB  . ALA B 599 ? 0.2544 0.3956 0.1767 0.0141  -0.0286 0.0220  591 ALA B CB  
9190  N N   . ALA B 600 ? 0.2150 0.3788 0.1307 0.0112  -0.0140 0.0084  592 ALA B N   
9191  C CA  . ALA B 600 ? 0.3003 0.4736 0.2063 0.0086  -0.0079 0.0083  592 ALA B CA  
9192  C C   . ALA B 600 ? 0.2351 0.4092 0.1509 0.0073  0.0004  0.0047  592 ALA B C   
9193  O O   . ALA B 600 ? 0.2097 0.3873 0.1207 0.0040  0.0058  0.0092  592 ALA B O   
9194  C CB  . ALA B 600 ? 0.2566 0.4410 0.1560 0.0106  -0.0093 -0.0004 592 ALA B CB  
9195  N N   . TYR B 601 ? 0.2108 0.3817 0.1402 0.0100  0.0017  -0.0034 593 TYR B N   
9196  C CA  . TYR B 601 ? 0.2113 0.3815 0.1494 0.0098  0.0089  -0.0064 593 TYR B CA  
9197  C C   . TYR B 601 ? 0.2361 0.3986 0.1775 0.0075  0.0100  0.0022  593 TYR B C   
9198  O O   . TYR B 601 ? 0.1766 0.3422 0.1186 0.0058  0.0155  0.0037  593 TYR B O   
9199  C CB  . TYR B 601 ? 0.2040 0.3702 0.1546 0.0132  0.0101  -0.0162 593 TYR B CB  
9200  C CG  . TYR B 601 ? 0.1658 0.3309 0.1236 0.0138  0.0172  -0.0190 593 TYR B CG  
9201  C CD1 . TYR B 601 ? 0.2490 0.4233 0.2044 0.0141  0.0226  -0.0242 593 TYR B CD1 
9202  C CD2 . TYR B 601 ? 0.1568 0.3117 0.1232 0.0144  0.0183  -0.0164 593 TYR B CD2 
9203  C CE1 . TYR B 601 ? 0.2357 0.4091 0.1975 0.0156  0.0284  -0.0266 593 TYR B CE1 
9204  C CE2 . TYR B 601 ? 0.1503 0.3041 0.1222 0.0157  0.0241  -0.0186 593 TYR B CE2 
9205  C CZ  . TYR B 601 ? 0.1925 0.3556 0.1621 0.0165  0.0289  -0.0236 593 TYR B CZ  
9206  O OH  . TYR B 601 ? 0.1500 0.3124 0.1249 0.0187  0.0341  -0.0260 593 TYR B OH  
9207  N N   . GLN B 602 ? 0.1786 0.3313 0.1229 0.0077  0.0048  0.0073  594 GLN B N   
9208  C CA  . GLN B 602 ? 0.2059 0.3510 0.1538 0.0054  0.0058  0.0148  594 GLN B CA  
9209  C C   . GLN B 602 ? 0.1906 0.3400 0.1285 0.0009  0.0079  0.0231  594 GLN B C   
9210  O O   . GLN B 602 ? 0.2011 0.3506 0.1422 -0.0015 0.0123  0.0257  594 GLN B O   
9211  C CB  . GLN B 602 ? 0.1965 0.3305 0.1490 0.0064  -0.0003 0.0184  594 GLN B CB  
9212  C CG  . GLN B 602 ? 0.1941 0.3231 0.1585 0.0100  -0.0011 0.0102  594 GLN B CG  
9213  C CD  . GLN B 602 ? 0.2667 0.3846 0.2377 0.0105  -0.0054 0.0138  594 GLN B CD  
9214  O OE1 . GLN B 602 ? 0.3372 0.4494 0.3083 0.0082  -0.0052 0.0210  594 GLN B OE1 
9215  N NE2 . GLN B 602 ? 0.2029 0.3181 0.1803 0.0133  -0.0092 0.0083  594 GLN B NE2 
9216  N N   . ALA B 603 ? 0.2259 0.3790 0.1513 -0.0003 0.0049  0.0270  595 ALA B N   
9217  C CA  . ALA B 603 ? 0.2490 0.4057 0.1635 -0.0051 0.0077  0.0349  595 ALA B CA  
9218  C C   . ALA B 603 ? 0.2653 0.4341 0.1783 -0.0068 0.0153  0.0304  595 ALA B C   
9219  O O   . ALA B 603 ? 0.2362 0.4080 0.1467 -0.0112 0.0200  0.0353  595 ALA B O   
9220  C CB  . ALA B 603 ? 0.2690 0.4255 0.1688 -0.0054 0.0026  0.0405  595 ALA B CB  
9221  N N   . ALA B 604 ? 0.2026 0.3787 0.1179 -0.0034 0.0168  0.0206  596 ALA B N   
9222  C CA  . ALA B 604 ? 0.2069 0.3942 0.1223 -0.0044 0.0240  0.0155  596 ALA B CA  
9223  C C   . ALA B 604 ? 0.1889 0.3746 0.1164 -0.0044 0.0283  0.0146  596 ALA B C   
9224  O O   . ALA B 604 ? 0.2165 0.4103 0.1439 -0.0070 0.0339  0.0149  596 ALA B O   
9225  C CB  . ALA B 604 ? 0.2001 0.3945 0.1163 -0.0005 0.0247  0.0046  596 ALA B CB  
9226  N N   . VAL B 605 ? 0.1785 0.3542 0.1164 -0.0016 0.0257  0.0135  597 VAL B N   
9227  C CA  . VAL B 605 ? 0.1853 0.3587 0.1336 -0.0011 0.0289  0.0130  597 VAL B CA  
9228  C C   . VAL B 605 ? 0.2905 0.4603 0.2384 -0.0058 0.0286  0.0220  597 VAL B C   
9229  O O   . VAL B 605 ? 0.1668 0.3415 0.1189 -0.0077 0.0329  0.0224  597 VAL B O   
9230  C CB  . VAL B 605 ? 0.1581 0.3217 0.1162 0.0035  0.0267  0.0083  597 VAL B CB  
9231  C CG1 . VAL B 605 ? 0.1489 0.3085 0.1161 0.0044  0.0291  0.0086  597 VAL B CG1 
9232  C CG2 . VAL B 605 ? 0.1569 0.3243 0.1164 0.0075  0.0284  -0.0013 597 VAL B CG2 
9233  N N   . LEU B 606 ? 0.1757 0.3370 0.1191 -0.0076 0.0236  0.0289  598 LEU B N   
9234  C CA  . LEU B 606 ? 0.2212 0.3765 0.1645 -0.0121 0.0230  0.0376  598 LEU B CA  
9235  C C   . LEU B 606 ? 0.1942 0.3493 0.1243 -0.0160 0.0214  0.0453  598 LEU B C   
9236  O O   . LEU B 606 ? 0.1998 0.3456 0.1261 -0.0154 0.0156  0.0500  598 LEU B O   
9237  C CB  . LEU B 606 ? 0.2448 0.3873 0.1962 -0.0102 0.0185  0.0390  598 LEU B CB  
9238  C CG  . LEU B 606 ? 0.1967 0.3367 0.1597 -0.0062 0.0199  0.0325  598 LEU B CG  
9239  C CD1 . LEU B 606 ? 0.1782 0.3052 0.1473 -0.0050 0.0155  0.0344  598 LEU B CD1 
9240  C CD2 . LEU B 606 ? 0.1808 0.3276 0.1486 -0.0079 0.0250  0.0316  598 LEU B CD2 
9241  N N   . PRO B 607 ? 0.2026 0.3675 0.1250 -0.0200 0.0264  0.0469  599 PRO B N   
9242  C CA  . PRO B 607 ? 0.2201 0.3845 0.1272 -0.0234 0.0255  0.0542  599 PRO B CA  
9243  C C   . PRO B 607 ? 0.2517 0.4038 0.1564 -0.0270 0.0226  0.0646  599 PRO B C   
9244  O O   . PRO B 607 ? 0.2221 0.3707 0.1353 -0.0300 0.0247  0.0669  599 PRO B O   
9245  C CB  . PRO B 607 ? 0.2258 0.4034 0.1281 -0.0278 0.0333  0.0532  599 PRO B CB  
9246  C CG  . PRO B 607 ? 0.2547 0.4414 0.1679 -0.0240 0.0367  0.0427  599 PRO B CG  
9247  C CD  . PRO B 607 ? 0.1976 0.3749 0.1244 -0.0208 0.0333  0.0411  599 PRO B CD  
9248  N N   . GLU B 608 ? 0.2689 0.4146 0.1617 -0.0265 0.0176  0.0706  600 GLU B N   
9249  C CA  . GLU B 608 ? 0.3244 0.4573 0.2132 -0.0297 0.0149  0.0811  600 GLU B CA  
9250  C C   . GLU B 608 ? 0.3723 0.5076 0.2570 -0.0375 0.0222  0.0872  600 GLU B C   
9251  O O   . GLU B 608 ? 0.3387 0.4831 0.2160 -0.0402 0.0276  0.0858  600 GLU B O   
9252  C CB  . GLU B 608 ? 0.3402 0.4669 0.2149 -0.0271 0.0082  0.0867  600 GLU B CB  
9253  N N   . GLY B 609 ? 0.4228 0.5488 0.3145 -0.0410 0.0226  0.0923  601 GLY B N   
9254  C CA  . GLY B 609 ? 0.4331 0.5598 0.3222 -0.0491 0.0295  0.0980  601 GLY B CA  
9255  C C   . GLY B 609 ? 0.4172 0.5558 0.3186 -0.0519 0.0365  0.0909  601 GLY B C   
9256  O O   . GLY B 609 ? 0.3837 0.5220 0.2872 -0.0580 0.0419  0.0928  601 GLY B O   
9257  N N   . LEU B 610 ? 0.3043 0.4518 0.2152 -0.0468 0.0360  0.0815  602 LEU B N   
9258  C CA  . LEU B 610 ? 0.2739 0.4325 0.1973 -0.0483 0.0415  0.0748  602 LEU B CA  
9259  C C   . LEU B 610 ? 0.2147 0.3657 0.1522 -0.0468 0.0384  0.0734  602 LEU B C   
9260  O O   . LEU B 610 ? 0.2288 0.3735 0.1704 -0.0406 0.0328  0.0702  602 LEU B O   
9261  C CB  . LEU B 610 ? 0.2629 0.4340 0.1884 -0.0430 0.0429  0.0651  602 LEU B CB  
9262  C CG  . LEU B 610 ? 0.3398 0.5230 0.2766 -0.0433 0.0484  0.0571  602 LEU B CG  
9263  C CD1 . LEU B 610 ? 0.3841 0.5714 0.3172 -0.0491 0.0539  0.0580  602 LEU B CD1 
9264  C CD2 . LEU B 610 ? 0.3023 0.4934 0.2423 -0.0364 0.0481  0.0477  602 LEU B CD2 
9265  N N   . PRO B 611 ? 0.2745 0.4256 0.2194 -0.0524 0.0417  0.0753  603 PRO B N   
9266  C CA  . PRO B 611 ? 0.2470 0.3908 0.2045 -0.0509 0.0385  0.0736  603 PRO B CA  
9267  C C   . PRO B 611 ? 0.2277 0.3774 0.1946 -0.0438 0.0369  0.0643  603 PRO B C   
9268  O O   . PRO B 611 ? 0.2212 0.3837 0.1897 -0.0421 0.0406  0.0582  603 PRO B O   
9269  C CB  . PRO B 611 ? 0.2066 0.3548 0.1706 -0.0587 0.0438  0.0752  603 PRO B CB  
9270  C CG  . PRO B 611 ? 0.3395 0.4902 0.2917 -0.0652 0.0489  0.0815  603 PRO B CG  
9271  C CD  . PRO B 611 ? 0.3186 0.4758 0.2608 -0.0606 0.0488  0.0788  603 PRO B CD  
9272  N N   . ARG B 612 ? 0.1787 0.3181 0.1517 -0.0398 0.0318  0.0631  604 ARG B N   
9273  C CA  . ARG B 612 ? 0.1666 0.3078 0.1465 -0.0327 0.0301  0.0554  604 ARG B CA  
9274  C C   . ARG B 612 ? 0.2481 0.3868 0.2392 -0.0326 0.0294  0.0530  604 ARG B C   
9275  O O   . ARG B 612 ? 0.1596 0.2889 0.1530 -0.0358 0.0273  0.0574  604 ARG B O   
9276  C CB  . ARG B 612 ? 0.1636 0.2949 0.1402 -0.0273 0.0248  0.0550  604 ARG B CB  
9277  C CG  . ARG B 612 ? 0.2011 0.3342 0.1662 -0.0269 0.0242  0.0570  604 ARG B CG  
9278  C CD  . ARG B 612 ? 0.1877 0.3097 0.1502 -0.0230 0.0180  0.0584  604 ARG B CD  
9279  N NE  . ARG B 612 ? 0.2067 0.3315 0.1579 -0.0223 0.0167  0.0599  604 ARG B NE  
9280  C CZ  . ARG B 612 ? 0.2965 0.4134 0.2429 -0.0199 0.0110  0.0625  604 ARG B CZ  
9281  N NH1 . ARG B 612 ? 0.2159 0.3215 0.1687 -0.0182 0.0065  0.0638  604 ARG B NH1 
9282  N NH2 . ARG B 612 ? 0.2844 0.4055 0.2200 -0.0191 0.0097  0.0633  604 ARG B NH2 
9283  N N   . ILE B 613 ? 0.2066 0.3536 0.2041 -0.0285 0.0309  0.0460  605 ILE B N   
9284  C CA  . ILE B 613 ? 0.1901 0.3360 0.1972 -0.0269 0.0298  0.0426  605 ILE B CA  
9285  C C   . ILE B 613 ? 0.1823 0.3251 0.1911 -0.0187 0.0278  0.0369  605 ILE B C   
9286  O O   . ILE B 613 ? 0.2078 0.3579 0.2149 -0.0148 0.0299  0.0326  605 ILE B O   
9287  C CB  . ILE B 613 ? 0.1388 0.2988 0.1525 -0.0299 0.0337  0.0396  605 ILE B CB  
9288  C CG1 . ILE B 613 ? 0.2208 0.3837 0.2329 -0.0390 0.0369  0.0451  605 ILE B CG1 
9289  C CG2 . ILE B 613 ? 0.1958 0.3552 0.2186 -0.0274 0.0316  0.0355  605 ILE B CG2 
9290  C CD1 . ILE B 613 ? 0.2327 0.4049 0.2371 -0.0416 0.0414  0.0464  605 ILE B CD1 
9291  N N   . ALA B 614 ? 0.1311 0.2628 0.1430 -0.0163 0.0244  0.0367  606 ALA B N   
9292  C CA  . ALA B 614 ? 0.1203 0.2473 0.1333 -0.0090 0.0233  0.0318  606 ALA B CA  
9293  C C   . ALA B 614 ? 0.1352 0.2652 0.1544 -0.0064 0.0233  0.0279  606 ALA B C   
9294  O O   . ALA B 614 ? 0.1690 0.2987 0.1925 -0.0101 0.0223  0.0294  606 ALA B O   
9295  C CB  . ALA B 614 ? 0.1579 0.2704 0.1696 -0.0077 0.0198  0.0336  606 ALA B CB  
9296  N N   . VAL B 615 ? 0.1117 0.2447 0.1311 0.0001  0.0245  0.0227  607 VAL B N   
9297  C CA  . VAL B 615 ? 0.1504 0.2862 0.1741 0.0042  0.0240  0.0189  607 VAL B CA  
9298  C C   . VAL B 615 ? 0.1421 0.2674 0.1632 0.0114  0.0234  0.0160  607 VAL B C   
9299  O O   . VAL B 615 ? 0.1063 0.2320 0.1246 0.0156  0.0254  0.0134  607 VAL B O   
9300  C CB  . VAL B 615 ? 0.1085 0.2602 0.1354 0.0054  0.0265  0.0153  607 VAL B CB  
9301  C CG1 . VAL B 615 ? 0.1298 0.2846 0.1614 0.0099  0.0248  0.0115  607 VAL B CG1 
9302  C CG2 . VAL B 615 ? 0.1119 0.2742 0.1411 -0.0025 0.0284  0.0179  607 VAL B CG2 
9303  N N   . GLU B 616 ? 0.1291 0.2450 0.1512 0.0126  0.0211  0.0162  608 GLU B N   
9304  C CA  . GLU B 616 ? 0.1188 0.2230 0.1376 0.0186  0.0212  0.0140  608 GLU B CA  
9305  C C   . GLU B 616 ? 0.1049 0.2040 0.1251 0.0198  0.0189  0.0135  608 GLU B C   
9306  O O   . GLU B 616 ? 0.1225 0.2200 0.1456 0.0146  0.0169  0.0159  608 GLU B O   
9307  C CB  . GLU B 616 ? 0.1337 0.2271 0.1502 0.0173  0.0212  0.0155  608 GLU B CB  
9308  C CG  . GLU B 616 ? 0.1177 0.1984 0.1317 0.0224  0.0222  0.0131  608 GLU B CG  
9309  C CD  . GLU B 616 ? 0.1264 0.1993 0.1396 0.0211  0.0226  0.0133  608 GLU B CD  
9310  O OE1 . GLU B 616 ? 0.1328 0.2000 0.1479 0.0175  0.0204  0.0157  608 GLU B OE1 
9311  O OE2 . GLU B 616 ? 0.1300 0.2033 0.1414 0.0237  0.0250  0.0106  608 GLU B OE2 
9312  N N   . ALA B 617 ? 0.1062 0.2020 0.1237 0.0266  0.0192  0.0105  609 ALA B N   
9313  C CA  . ALA B 617 ? 0.1214 0.2132 0.1387 0.0283  0.0168  0.0097  609 ALA B CA  
9314  C C   . ALA B 617 ? 0.1847 0.2609 0.1993 0.0276  0.0168  0.0108  609 ALA B C   
9315  O O   . ALA B 617 ? 0.1616 0.2279 0.1712 0.0326  0.0178  0.0093  609 ALA B O   
9316  C CB  . ALA B 617 ? 0.1109 0.2050 0.1250 0.0363  0.0168  0.0065  609 ALA B CB  
9317  N N   . GLY B 618 ? 0.1669 0.2410 0.1849 0.0212  0.0158  0.0135  610 GLY B N   
9318  C CA  . GLY B 618 ? 0.1506 0.2115 0.1680 0.0199  0.0156  0.0141  610 GLY B CA  
9319  C C   . GLY B 618 ? 0.1340 0.1948 0.1563 0.0130  0.0135  0.0173  610 GLY B C   
9320  O O   . GLY B 618 ? 0.1225 0.1929 0.1478 0.0088  0.0127  0.0194  610 GLY B O   
9321  N N   . HIS B 619 ? 0.1422 0.1918 0.1652 0.0119  0.0131  0.0177  611 HIS B N   
9322  C CA  . HIS B 619 ? 0.1219 0.1690 0.1494 0.0061  0.0108  0.0208  611 HIS B CA  
9323  C C   . HIS B 619 ? 0.1257 0.1795 0.1538 0.0026  0.0105  0.0244  611 HIS B C   
9324  O O   . HIS B 619 ? 0.1794 0.2357 0.2047 0.0048  0.0120  0.0240  611 HIS B O   
9325  C CB  . HIS B 619 ? 0.1077 0.1422 0.1364 0.0065  0.0107  0.0200  611 HIS B CB  
9326  C CG  . HIS B 619 ? 0.1336 0.1631 0.1672 0.0022  0.0081  0.0216  611 HIS B CG  
9327  N ND1 . HIS B 619 ? 0.1196 0.1497 0.1565 -0.0024 0.0060  0.0258  611 HIS B ND1 
9328  C CD2 . HIS B 619 ? 0.1261 0.1497 0.1616 0.0018  0.0074  0.0195  611 HIS B CD2 
9329  C CE1 . HIS B 619 ? 0.1820 0.2061 0.2233 -0.0054 0.0042  0.0262  611 HIS B CE1 
9330  N NE2 . HIS B 619 ? 0.1472 0.1677 0.1880 -0.0030 0.0050  0.0220  611 HIS B NE2 
9331  N N   . THR B 620 ? 0.1100 0.1661 0.1415 -0.0029 0.0088  0.0279  612 THR B N   
9332  C CA  . THR B 620 ? 0.1290 0.1909 0.1594 -0.0067 0.0088  0.0321  612 THR B CA  
9333  C C   . THR B 620 ? 0.1525 0.2065 0.1823 -0.0080 0.0069  0.0353  612 THR B C   
9334  O O   . THR B 620 ? 0.1552 0.2134 0.1818 -0.0095 0.0069  0.0384  612 THR B O   
9335  C CB  . THR B 620 ? 0.1413 0.2088 0.1750 -0.0128 0.0084  0.0348  612 THR B CB  
9336  O OG1 . THR B 620 ? 0.1344 0.1923 0.1720 -0.0160 0.0062  0.0366  612 THR B OG1 
9337  C CG2 . THR B 620 ? 0.1485 0.2260 0.1844 -0.0119 0.0096  0.0310  612 THR B CG2 
9338  N N   . ASN B 621 ? 0.1331 0.1762 0.1658 -0.0071 0.0051  0.0345  613 ASN B N   
9339  C CA  A ASN B 621 ? 0.1913 0.2279 0.2251 -0.0092 0.0024  0.0384  613 ASN B CA  
9340  C CA  B ASN B 621 ? 0.1999 0.2358 0.2339 -0.0088 0.0023  0.0381  613 ASN B CA  
9341  C C   . ASN B 621 ? 0.2087 0.2468 0.2389 -0.0067 0.0019  0.0387  613 ASN B C   
9342  O O   . ASN B 621 ? 0.1858 0.2230 0.2141 -0.0087 -0.0005 0.0432  613 ASN B O   
9343  C CB  A ASN B 621 ? 0.2164 0.2418 0.2555 -0.0087 0.0006  0.0367  613 ASN B CB  
9344  C CB  B ASN B 621 ? 0.1939 0.2187 0.2326 -0.0072 0.0010  0.0354  613 ASN B CB  
9345  C CG  A ASN B 621 ? 0.2308 0.2541 0.2737 -0.0131 -0.0002 0.0383  613 ASN B CG  
9346  C CG  B ASN B 621 ? 0.1920 0.2100 0.2328 -0.0072 -0.0023 0.0379  613 ASN B CG  
9347  O OD1 A ASN B 621 ? 0.2650 0.2958 0.3073 -0.0164 0.0010  0.0398  613 ASN B OD1 
9348  O OD1 B ASN B 621 ? 0.2411 0.2581 0.2815 -0.0039 -0.0026 0.0356  613 ASN B OD1 
9349  N ND2 A ASN B 621 ? 0.1859 0.1993 0.2336 -0.0135 -0.0019 0.0374  613 ASN B ND2 
9350  N ND2 B ASN B 621 ? 0.2303 0.2434 0.2734 -0.0108 -0.0048 0.0423  613 ASN B ND2 
9351  N N   . GLY B 622 ? 0.2156 0.2559 0.2442 -0.0024 0.0041  0.0339  614 GLY B N   
9352  C CA  . GLY B 622 ? 0.2289 0.2717 0.2548 -0.0003 0.0038  0.0331  614 GLY B CA  
9353  C C   . GLY B 622 ? 0.2440 0.2966 0.2643 -0.0022 0.0042  0.0363  614 GLY B C   
9354  O O   . GLY B 622 ? 0.2282 0.2826 0.2454 -0.0016 0.0027  0.0372  614 GLY B O   
9355  N N   . TRP B 623 ? 0.1200 0.1797 0.1390 -0.0046 0.0064  0.0377  615 TRP B N   
9356  C CA  . TRP B 623 ? 0.1527 0.2226 0.1665 -0.0064 0.0079  0.0398  615 TRP B CA  
9357  C C   . TRP B 623 ? 0.2321 0.3013 0.2425 -0.0110 0.0057  0.0466  615 TRP B C   
9358  O O   . TRP B 623 ? 0.2290 0.3055 0.2334 -0.0125 0.0068  0.0487  615 TRP B O   
9359  C CB  . TRP B 623 ? 0.1306 0.2097 0.1453 -0.0071 0.0112  0.0381  615 TRP B CB  
9360  C CG  . TRP B 623 ? 0.1499 0.2307 0.1651 -0.0016 0.0134  0.0321  615 TRP B CG  
9361  C CD1 . TRP B 623 ? 0.1108 0.1880 0.1290 0.0013  0.0140  0.0287  615 TRP B CD1 
9362  C CD2 . TRP B 623 ? 0.1403 0.2254 0.1523 0.0019  0.0153  0.0287  615 TRP B CD2 
9363  N NE1 . TRP B 623 ? 0.1860 0.2643 0.2026 0.0066  0.0164  0.0241  615 TRP B NE1 
9364  C CE2 . TRP B 623 ? 0.1658 0.2490 0.1792 0.0068  0.0173  0.0237  615 TRP B CE2 
9365  C CE3 . TRP B 623 ? 0.1471 0.2375 0.1547 0.0013  0.0154  0.0293  615 TRP B CE3 
9366  C CZ2 . TRP B 623 ? 0.1300 0.2155 0.1414 0.0110  0.0199  0.0193  615 TRP B CZ2 
9367  C CZ3 . TRP B 623 ? 0.1533 0.2472 0.1592 0.0054  0.0178  0.0242  615 TRP B CZ3 
9368  C CH2 . TRP B 623 ? 0.1113 0.2023 0.1196 0.0101  0.0201  0.0193  615 TRP B CH2 
9369  N N   . TYR B 624 ? 0.1354 0.1952 0.1488 -0.0132 0.0029  0.0501  616 TYR B N   
9370  C CA  . TYR B 624 ? 0.1919 0.2488 0.2012 -0.0173 0.0009  0.0573  616 TYR B CA  
9371  C C   . TYR B 624 ? 0.1602 0.2163 0.1638 -0.0147 -0.0021 0.0588  616 TYR B C   
9372  O O   . TYR B 624 ? 0.1730 0.2294 0.1696 -0.0173 -0.0032 0.0648  616 TYR B O   
9373  C CB  . TYR B 624 ? 0.1684 0.2142 0.1830 -0.0196 -0.0016 0.0603  616 TYR B CB  
9374  C CG  . TYR B 624 ? 0.2096 0.2578 0.2286 -0.0236 0.0012  0.0598  616 TYR B CG  
9375  C CD1 . TYR B 624 ? 0.2349 0.2879 0.2514 -0.0295 0.0036  0.0644  616 TYR B CD1 
9376  C CD2 . TYR B 624 ? 0.1969 0.2435 0.2224 -0.0216 0.0017  0.0543  616 TYR B CD2 
9377  C CE1 . TYR B 624 ? 0.2641 0.3209 0.2861 -0.0334 0.0061  0.0628  616 TYR B CE1 
9378  C CE2 . TYR B 624 ? 0.2168 0.2670 0.2464 -0.0249 0.0036  0.0531  616 TYR B CE2 
9379  C CZ  . TYR B 624 ? 0.2890 0.3447 0.3177 -0.0308 0.0057  0.0570  616 TYR B CZ  
9380  O OH  . TYR B 624 ? 0.2944 0.3550 0.3287 -0.0343 0.0075  0.0547  616 TYR B OH  
9381  N N   . LYS B 625 ? 0.1656 0.2208 0.1715 -0.0097 -0.0033 0.0531  617 LYS B N   
9382  C CA  . LYS B 625 ? 0.1641 0.2207 0.1653 -0.0070 -0.0063 0.0530  617 LYS B CA  
9383  C C   . LYS B 625 ? 0.1787 0.2461 0.1711 -0.0084 -0.0039 0.0542  617 LYS B C   
9384  O O   . LYS B 625 ? 0.2064 0.2752 0.1915 -0.0082 -0.0067 0.0574  617 LYS B O   
9385  C CB  . LYS B 625 ? 0.1641 0.2194 0.1709 -0.0021 -0.0067 0.0453  617 LYS B CB  
9386  C CG  . LYS B 625 ? 0.2733 0.3314 0.2768 0.0008  -0.0100 0.0435  617 LYS B CG  
9387  C CD  . LYS B 625 ? 0.3155 0.3718 0.3263 0.0048  -0.0094 0.0351  617 LYS B CD  
9388  C CE  . LYS B 625 ? 0.4504 0.5150 0.4580 0.0071  -0.0086 0.0299  617 LYS B CE  
9389  N NZ  . LYS B 625 ? 0.4515 0.5130 0.4672 0.0104  -0.0077 0.0216  617 LYS B NZ  
9390  N N   . TYR B 626 ? 0.1594 0.2348 0.1522 -0.0095 0.0011  0.0516  618 TYR B N   
9391  C CA  . TYR B 626 ? 0.1985 0.2851 0.1841 -0.0110 0.0042  0.0519  618 TYR B CA  
9392  C C   . TYR B 626 ? 0.2071 0.2967 0.1891 -0.0170 0.0067  0.0582  618 TYR B C   
9393  O O   . TYR B 626 ? 0.2093 0.3035 0.1825 -0.0195 0.0075  0.0622  618 TYR B O   
9394  C CB  . TYR B 626 ? 0.1888 0.2831 0.1776 -0.0080 0.0084  0.0444  618 TYR B CB  
9395  C CG  . TYR B 626 ? 0.2510 0.3414 0.2436 -0.0027 0.0072  0.0379  618 TYR B CG  
9396  C CD1 . TYR B 626 ? 0.3146 0.4082 0.3034 -0.0003 0.0059  0.0349  618 TYR B CD1 
9397  C CD2 . TYR B 626 ? 0.2756 0.3590 0.2757 -0.0003 0.0076  0.0345  618 TYR B CD2 
9398  C CE1 . TYR B 626 ? 0.2742 0.3644 0.2678 0.0039  0.0054  0.0283  618 TYR B CE1 
9399  C CE2 . TYR B 626 ? 0.3233 0.4023 0.3270 0.0038  0.0075  0.0285  618 TYR B CE2 
9400  C CZ  . TYR B 626 ? 0.3134 0.3960 0.3145 0.0057  0.0066  0.0253  618 TYR B CZ  
9401  O OH  . TYR B 626 ? 0.3501 0.4285 0.3560 0.0092  0.0071  0.0188  618 TYR B OH  
9402  N N   . VAL B 627 ? 0.2150 0.3021 0.2034 -0.0197 0.0082  0.0590  619 VAL B N   
9403  C CA  . VAL B 627 ? 0.2381 0.3300 0.2248 -0.0259 0.0117  0.0634  619 VAL B CA  
9404  C C   . VAL B 627 ? 0.2264 0.3083 0.2103 -0.0305 0.0095  0.0717  619 VAL B C   
9405  O O   . VAL B 627 ? 0.1942 0.2792 0.1739 -0.0363 0.0127  0.0767  619 VAL B O   
9406  C CB  . VAL B 627 ? 0.2219 0.3186 0.2174 -0.0270 0.0147  0.0593  619 VAL B CB  
9407  C CG1 . VAL B 627 ? 0.2032 0.3076 0.2013 -0.0215 0.0164  0.0516  619 VAL B CG1 
9408  C CG2 . VAL B 627 ? 0.1514 0.2373 0.1541 -0.0274 0.0120  0.0599  619 VAL B CG2 
9409  N N   . GLY B 628 ? 0.2334 0.3032 0.2197 -0.0281 0.0046  0.0732  620 GLY B N   
9410  C CA  . GLY B 628 ? 0.2335 0.2926 0.2165 -0.0315 0.0021  0.0813  620 GLY B CA  
9411  C C   . GLY B 628 ? 0.2371 0.2929 0.2258 -0.0375 0.0048  0.0837  620 GLY B C   
9412  O O   . GLY B 628 ? 0.3006 0.3625 0.2969 -0.0385 0.0077  0.0786  620 GLY B O   
9413  N N   . LEU B 629 ? 0.2214 0.2673 0.2063 -0.0414 0.0037  0.0917  621 LEU B N   
9414  C CA  . LEU B 629 ? 0.2806 0.3213 0.2717 -0.0475 0.0060  0.0940  621 LEU B CA  
9415  C C   . LEU B 629 ? 0.3075 0.3587 0.2976 -0.0543 0.0126  0.0947  621 LEU B C   
9416  O O   . LEU B 629 ? 0.3556 0.4063 0.3533 -0.0594 0.0152  0.0939  621 LEU B O   
9417  C CB  . LEU B 629 ? 0.2707 0.2956 0.2581 -0.0493 0.0028  0.1024  621 LEU B CB  
9418  C CG  . LEU B 629 ? 0.2906 0.3056 0.2802 -0.0424 -0.0040 0.1014  621 LEU B CG  
9419  C CD1 . LEU B 629 ? 0.3532 0.3536 0.3367 -0.0430 -0.0077 0.1106  621 LEU B CD1 
9420  C CD2 . LEU B 629 ? 0.3101 0.3222 0.3127 -0.0407 -0.0051 0.0945  621 LEU B CD2 
9421  N N   . ASN B 630 ? 0.2536 0.3148 0.2350 -0.0546 0.0155  0.0955  622 ASN B N   
9422  C CA  . ASN B 630 ? 0.3432 0.4154 0.3238 -0.0612 0.0224  0.0958  622 ASN B CA  
9423  C C   . ASN B 630 ? 0.2906 0.3794 0.2759 -0.0586 0.0252  0.0871  622 ASN B C   
9424  O O   . ASN B 630 ? 0.2503 0.3503 0.2371 -0.0636 0.0309  0.0858  622 ASN B O   
9425  C CB  . ASN B 630 ? 0.3999 0.4710 0.3660 -0.0647 0.0248  0.1038  622 ASN B CB  
9426  C CG  . ASN B 630 ? 0.4839 0.5379 0.4446 -0.0681 0.0229  0.1135  622 ASN B CG  
9427  O OD1 . ASN B 630 ? 0.4524 0.4993 0.4207 -0.0729 0.0242  0.1150  622 ASN B OD1 
9428  N ND2 . ASN B 630 ? 0.5597 0.6068 0.5072 -0.0652 0.0196  0.1199  622 ASN B ND2 
9429  N N   . GLY B 631 ? 0.3026 0.3932 0.2905 -0.0511 0.0217  0.0811  623 GLY B N   
9430  C CA  . GLY B 631 ? 0.2495 0.3535 0.2428 -0.0477 0.0239  0.0728  623 GLY B CA  
9431  C C   . GLY B 631 ? 0.2271 0.3313 0.2323 -0.0475 0.0235  0.0679  623 GLY B C   
9432  O O   . GLY B 631 ? 0.2412 0.3385 0.2511 -0.0520 0.0231  0.0705  623 GLY B O   
9433  N N   . ALA B 632 ? 0.1672 0.2792 0.1768 -0.0421 0.0235  0.0605  624 ALA B N   
9434  C CA  . ALA B 632 ? 0.1581 0.2718 0.1776 -0.0411 0.0229  0.0554  624 ALA B CA  
9435  C C   . ALA B 632 ? 0.1525 0.2677 0.1733 -0.0328 0.0211  0.0490  624 ALA B C   
9436  O O   . ALA B 632 ? 0.1555 0.2737 0.1711 -0.0287 0.0216  0.0475  624 ALA B O   
9437  C CB  . ALA B 632 ? 0.1502 0.2772 0.1756 -0.0462 0.0272  0.0531  624 ALA B CB  
9438  N N   . VAL B 633 ? 0.1608 0.2730 0.1882 -0.0305 0.0192  0.0452  625 VAL B N   
9439  C CA  . VAL B 633 ? 0.1416 0.2533 0.1696 -0.0228 0.0180  0.0395  625 VAL B CA  
9440  C C   . VAL B 633 ? 0.1744 0.2938 0.2090 -0.0217 0.0183  0.0345  625 VAL B C   
9441  O O   . VAL B 633 ? 0.1783 0.2964 0.2183 -0.0258 0.0173  0.0348  625 VAL B O   
9442  C CB  . VAL B 633 ? 0.1430 0.2399 0.1702 -0.0195 0.0146  0.0399  625 VAL B CB  
9443  C CG1 . VAL B 633 ? 0.1754 0.2714 0.2016 -0.0119 0.0146  0.0346  625 VAL B CG1 
9444  C CG2 . VAL B 633 ? 0.1614 0.2505 0.1835 -0.0210 0.0131  0.0450  625 VAL B CG2 
9445  N N   . VAL B 634 ? 0.1289 0.2560 0.1633 -0.0158 0.0193  0.0296  626 VAL B N   
9446  C CA  . VAL B 634 ? 0.1440 0.2767 0.1835 -0.0123 0.0183  0.0244  626 VAL B CA  
9447  C C   . VAL B 634 ? 0.1508 0.2724 0.1868 -0.0051 0.0162  0.0222  626 VAL B C   
9448  O O   . VAL B 634 ? 0.1367 0.2577 0.1686 0.0005  0.0174  0.0205  626 VAL B O   
9449  C CB  . VAL B 634 ? 0.1108 0.2596 0.1528 -0.0102 0.0207  0.0205  626 VAL B CB  
9450  C CG1 . VAL B 634 ? 0.1219 0.2763 0.1689 -0.0060 0.0186  0.0152  626 VAL B CG1 
9451  C CG2 . VAL B 634 ? 0.1151 0.2744 0.1599 -0.0182 0.0238  0.0227  626 VAL B CG2 
9452  N N   . GLY B 635 ? 0.1485 0.2746 0.1429 -0.0440 0.0199  0.0114  627 GLY B N   
9453  C CA  . GLY B 635 ? 0.1280 0.2479 0.1222 -0.0389 0.0172  0.0074  627 GLY B CA  
9454  C C   . GLY B 635 ? 0.1292 0.2360 0.1268 -0.0370 0.0130  0.0085  627 GLY B C   
9455  O O   . GLY B 635 ? 0.1293 0.2345 0.1315 -0.0405 0.0125  0.0104  627 GLY B O   
9456  N N   . ILE B 636 ? 0.1435 0.2417 0.1386 -0.0322 0.0101  0.0071  628 ILE B N   
9457  C CA  . ILE B 636 ? 0.1453 0.2296 0.1414 -0.0302 0.0063  0.0077  628 ILE B CA  
9458  C C   . ILE B 636 ? 0.1279 0.2015 0.1169 -0.0255 0.0039  0.0105  628 ILE B C   
9459  O O   . ILE B 636 ? 0.1235 0.2016 0.1112 -0.0220 0.0044  0.0078  628 ILE B O   
9460  C CB  . ILE B 636 ? 0.2065 0.2918 0.2099 -0.0277 0.0067  0.0013  628 ILE B CB  
9461  C CG1 . ILE B 636 ? 0.1628 0.2340 0.1656 -0.0252 0.0023  0.0014  628 ILE B CG1 
9462  C CG2 . ILE B 636 ? 0.2892 0.3800 0.2924 -0.0244 0.0104  -0.0046 628 ILE B CG2 
9463  C CD1 . ILE B 636 ? 0.2710 0.3441 0.2802 -0.0217 0.0027  -0.0037 628 ILE B CD1 
9464  N N   . ASN B 637 ? 0.1436 0.2034 0.1275 -0.0258 0.0020  0.0161  629 ASN B N   
9465  C CA  . ASN B 637 ? 0.1431 0.1917 0.1192 -0.0204 0.0009  0.0207  629 ASN B CA  
9466  C C   . ASN B 637 ? 0.2063 0.2364 0.1804 -0.0182 -0.0014 0.0198  629 ASN B C   
9467  O O   . ASN B 637 ? 0.2372 0.2539 0.2038 -0.0137 -0.0014 0.0245  629 ASN B O   
9468  C CB  . ASN B 637 ? 0.1631 0.2077 0.1310 -0.0209 0.0027  0.0297  629 ASN B CB  
9469  C CG  . ASN B 637 ? 0.2299 0.2930 0.1973 -0.0213 0.0046  0.0317  629 ASN B CG  
9470  O OD1 . ASN B 637 ? 0.2042 0.2822 0.1764 -0.0215 0.0046  0.0258  629 ASN B OD1 
9471  N ND2 . ASN B 637 ? 0.2442 0.3053 0.2041 -0.0215 0.0068  0.0399  629 ASN B ND2 
9472  N N   . ARG B 638 ? 0.1754 0.2045 0.1552 -0.0209 -0.0030 0.0144  630 ARG B N   
9473  C CA  . ARG B 638 ? 0.1858 0.1987 0.1628 -0.0196 -0.0056 0.0128  630 ARG B CA  
9474  C C   . ARG B 638 ? 0.1721 0.1901 0.1555 -0.0158 -0.0066 0.0060  630 ARG B C   
9475  O O   . ARG B 638 ? 0.1631 0.1957 0.1528 -0.0151 -0.0046 0.0024  630 ARG B O   
9476  C CB  . ARG B 638 ? 0.2910 0.2971 0.2668 -0.0275 -0.0068 0.0136  630 ARG B CB  
9477  C CG  . ARG B 638 ? 0.3296 0.3534 0.3157 -0.0329 -0.0072 0.0104  630 ARG B CG  
9478  C CD  . ARG B 638 ? 0.5191 0.5377 0.5040 -0.0421 -0.0089 0.0111  630 ARG B CD  
9479  N NE  . ARG B 638 ? 0.6809 0.7182 0.6772 -0.0461 -0.0103 0.0078  630 ARG B NE  
9480  C CZ  . ARG B 638 ? 0.7947 0.8457 0.7969 -0.0529 -0.0083 0.0092  630 ARG B CZ  
9481  N NH1 . ARG B 638 ? 0.8231 0.8696 0.8196 -0.0568 -0.0047 0.0138  630 ARG B NH1 
9482  N NH2 . ARG B 638 ? 0.8356 0.9054 0.8491 -0.0551 -0.0094 0.0067  630 ARG B NH2 
9483  N N   . PHE B 639 ? 0.1371 0.1410 0.1171 -0.0129 -0.0088 0.0043  631 PHE B N   
9484  C CA  . PHE B 639 ? 0.1383 0.1444 0.1226 -0.0083 -0.0091 -0.0014 631 PHE B CA  
9485  C C   . PHE B 639 ? 0.2007 0.2192 0.1929 -0.0112 -0.0098 -0.0042 631 PHE B C   
9486  O O   . PHE B 639 ? 0.1742 0.1970 0.1683 -0.0177 -0.0114 -0.0022 631 PHE B O   
9487  C CB  . PHE B 639 ? 0.1636 0.1513 0.1413 -0.0046 -0.0112 -0.0021 631 PHE B CB  
9488  C CG  . PHE B 639 ? 0.1653 0.1420 0.1364 0.0004  -0.0096 0.0007  631 PHE B CG  
9489  C CD1 . PHE B 639 ? 0.1804 0.1638 0.1541 0.0054  -0.0071 -0.0015 631 PHE B CD1 
9490  C CD2 . PHE B 639 ? 0.2024 0.1621 0.1642 -0.0000 -0.0099 0.0054  631 PHE B CD2 
9491  C CE1 . PHE B 639 ? 0.2150 0.1922 0.1842 0.0102  -0.0057 0.0015  631 PHE B CE1 
9492  C CE2 . PHE B 639 ? 0.2297 0.1806 0.1860 0.0062  -0.0077 0.0091  631 PHE B CE2 
9493  C CZ  . PHE B 639 ? 0.1513 0.1128 0.1122 0.0115  -0.0061 0.0073  631 PHE B CZ  
9494  N N   . GLY B 640 ? 0.1367 0.1609 0.1334 -0.0061 -0.0077 -0.0086 632 GLY B N   
9495  C CA  . GLY B 640 ? 0.1802 0.2174 0.1849 -0.0061 -0.0070 -0.0104 632 GLY B CA  
9496  C C   . GLY B 640 ? 0.1649 0.1994 0.1699 -0.0061 -0.0118 -0.0104 632 GLY B C   
9497  O O   . GLY B 640 ? 0.1775 0.1998 0.1760 -0.0093 -0.0159 -0.0090 632 GLY B O   
9498  N N   . GLU B 641 ? 0.1617 0.2078 0.1734 -0.0020 -0.0107 -0.0119 633 GLU B N   
9499  C CA  . GLU B 641 ? 0.2004 0.2509 0.2141 -0.0017 -0.0156 -0.0114 633 GLU B CA  
9500  C C   . GLU B 641 ? 0.1501 0.2063 0.1675 0.0086  -0.0121 -0.0130 633 GLU B C   
9501  O O   . GLU B 641 ? 0.1572 0.2209 0.1791 0.0126  -0.0055 -0.0138 633 GLU B O   
9502  C CB  . GLU B 641 ? 0.2219 0.2904 0.2433 -0.0101 -0.0184 -0.0090 633 GLU B CB  
9503  C CG  . GLU B 641 ? 0.2457 0.3064 0.2618 -0.0211 -0.0217 -0.0072 633 GLU B CG  
9504  C CD  . GLU B 641 ? 0.2616 0.3059 0.2678 -0.0240 -0.0270 -0.0080 633 GLU B CD  
9505  O OE1 . GLU B 641 ? 0.2135 0.2579 0.2188 -0.0190 -0.0299 -0.0097 633 GLU B OE1 
9506  O OE2 . GLU B 641 ? 0.2849 0.3148 0.2829 -0.0311 -0.0274 -0.0067 633 GLU B OE2 
9507  N N   . SER B 642 ? 0.1191 0.1707 0.1331 0.0130  -0.0159 -0.0132 634 SER B N   
9508  C CA  . SER B 642 ? 0.1188 0.1766 0.1357 0.0239  -0.0125 -0.0132 634 SER B CA  
9509  C C   . SER B 642 ? 0.1467 0.2302 0.1748 0.0236  -0.0138 -0.0100 634 SER B C   
9510  O O   . SER B 642 ? 0.1727 0.2668 0.2029 0.0188  -0.0213 -0.0083 634 SER B O   
9511  C CB  . SER B 642 ? 0.1738 0.2187 0.1824 0.0292  -0.0162 -0.0138 634 SER B CB  
9512  O OG  . SER B 642 ? 0.1694 0.2193 0.1796 0.0410  -0.0121 -0.0129 634 SER B OG  
9513  N N   . ALA B 643 ? 0.1473 0.2411 0.1821 0.0286  -0.0061 -0.0095 635 ALA B N   
9514  C CA  . ALA B 643 ? 0.1145 0.2338 0.1609 0.0309  -0.0051 -0.0058 635 ALA B CA  
9515  C C   . ALA B 643 ? 0.1373 0.2583 0.1865 0.0395  0.0065  -0.0061 635 ALA B C   
9516  O O   . ALA B 643 ? 0.1412 0.2448 0.1832 0.0398  0.0128  -0.0100 635 ALA B O   
9517  C CB  . ALA B 643 ? 0.1348 0.2689 0.1881 0.0178  -0.0100 -0.0043 635 ALA B CB  
9518  N N   . PRO B 644 ? 0.1142 0.2560 0.1730 0.0461  0.0103  -0.0022 636 PRO B N   
9519  C CA  . PRO B 644 ? 0.1162 0.2581 0.1764 0.0530  0.0229  -0.0025 636 PRO B CA  
9520  C C   . PRO B 644 ? 0.1498 0.2891 0.2097 0.0423  0.0257  -0.0055 636 PRO B C   
9521  O O   . PRO B 644 ? 0.1303 0.2782 0.1942 0.0310  0.0187  -0.0046 636 PRO B O   
9522  C CB  . PRO B 644 ? 0.1801 0.3495 0.2528 0.0604  0.0244  0.0037  636 PRO B CB  
9523  C CG  . PRO B 644 ? 0.1809 0.3599 0.2552 0.0629  0.0141  0.0068  636 PRO B CG  
9524  C CD  . PRO B 644 ? 0.1158 0.2816 0.1835 0.0493  0.0040  0.0029  636 PRO B CD  
9525  N N   . ALA B 645 ? 0.1626 0.2892 0.2162 0.0458  0.0367  -0.0091 637 ALA B N   
9526  C CA  . ALA B 645 ? 0.1138 0.2365 0.1644 0.0360  0.0396  -0.0125 637 ALA B CA  
9527  C C   . ALA B 645 ? 0.1455 0.2893 0.2061 0.0303  0.0392  -0.0090 637 ALA B C   
9528  O O   . ALA B 645 ? 0.1292 0.2741 0.1891 0.0195  0.0356  -0.0097 637 ALA B O   
9529  C CB  . ALA B 645 ? 0.1630 0.2707 0.2047 0.0403  0.0524  -0.0175 637 ALA B CB  
9530  N N   . ASP B 646 ? 0.1789 0.3400 0.2488 0.0379  0.0437  -0.0049 638 ASP B N   
9531  C CA  . ASP B 646 ? 0.1531 0.3346 0.2328 0.0321  0.0446  -0.0018 638 ASP B CA  
9532  C C   . ASP B 646 ? 0.1377 0.3311 0.2236 0.0205  0.0323  0.0007  638 ASP B C   
9533  O O   . ASP B 646 ? 0.1050 0.3039 0.1928 0.0103  0.0315  0.0010  638 ASP B O   
9534  C CB  . ASP B 646 ? 0.1942 0.3941 0.2837 0.0437  0.0525  0.0030  638 ASP B CB  
9535  C CG  . ASP B 646 ? 0.2854 0.4979 0.3816 0.0529  0.0469  0.0078  638 ASP B CG  
9536  O OD1 . ASP B 646 ? 0.2725 0.4761 0.3640 0.0509  0.0378  0.0066  638 ASP B OD1 
9537  O OD2 . ASP B 646 ? 0.2760 0.5015 0.3791 0.0608  0.0505  0.0128  638 ASP B OD2 
9538  N N   . LEU B 647 ? 0.1054 0.3006 0.1926 0.0213  0.0233  0.0021  639 LEU B N   
9539  C CA  . LEU B 647 ? 0.1273 0.3305 0.2179 0.0089  0.0126  0.0034  639 LEU B CA  
9540  C C   . LEU B 647 ? 0.1373 0.3189 0.2167 -0.0008 0.0092  0.0001  639 LEU B C   
9541  O O   . LEU B 647 ? 0.1040 0.2888 0.1844 -0.0125 0.0048  0.0012  639 LEU B O   
9542  C CB  . LEU B 647 ? 0.1221 0.3323 0.2150 0.0118  0.0042  0.0051  639 LEU B CB  
9543  C CG  . LEU B 647 ? 0.1297 0.3683 0.2355 0.0208  0.0055  0.0101  639 LEU B CG  
9544  C CD1 . LEU B 647 ? 0.1877 0.4311 0.2927 0.0246  -0.0031 0.0114  639 LEU B CD1 
9545  C CD2 . LEU B 647 ? 0.1448 0.4111 0.2642 0.0121  0.0045  0.0134  639 LEU B CD2 
9546  N N   . LEU B 648 ? 0.1031 0.2631 0.1718 0.0041  0.0121  -0.0035 640 LEU B N   
9547  C CA  . LEU B 648 ? 0.1030 0.2449 0.1617 -0.0031 0.0097  -0.0058 640 LEU B CA  
9548  C C   . LEU B 648 ? 0.1466 0.2919 0.2048 -0.0094 0.0145  -0.0056 640 LEU B C   
9549  O O   . LEU B 648 ? 0.1045 0.2464 0.1596 -0.0184 0.0108  -0.0042 640 LEU B O   
9550  C CB  . LEU B 648 ? 0.1031 0.2252 0.1521 0.0038  0.0122  -0.0096 640 LEU B CB  
9551  C CG  . LEU B 648 ? 0.1464 0.2608 0.1929 0.0090  0.0068  -0.0097 640 LEU B CG  
9552  C CD1 . LEU B 648 ? 0.1053 0.2000 0.1423 0.0154  0.0108  -0.0137 640 LEU B CD1 
9553  C CD2 . LEU B 648 ? 0.1728 0.2838 0.2170 0.0002  -0.0026 -0.0081 640 LEU B CD2 
9554  N N   . PHE B 649 ? 0.1128 0.2630 0.1725 -0.0045 0.0236  -0.0071 641 PHE B N   
9555  C CA  . PHE B 649 ? 0.1047 0.2586 0.1627 -0.0107 0.0282  -0.0071 641 PHE B CA  
9556  C C   . PHE B 649 ? 0.1404 0.3096 0.2063 -0.0189 0.0250  -0.0026 641 PHE B C   
9557  O O   . PHE B 649 ? 0.1310 0.2980 0.1929 -0.0271 0.0242  -0.0014 641 PHE B O   
9558  C CB  . PHE B 649 ? 0.1077 0.2645 0.1653 -0.0046 0.0396  -0.0096 641 PHE B CB  
9559  C CG  . PHE B 649 ? 0.1101 0.2496 0.1564 -0.0012 0.0444  -0.0153 641 PHE B CG  
9560  C CD1 . PHE B 649 ? 0.1301 0.2609 0.1674 -0.0079 0.0422  -0.0176 641 PHE B CD1 
9561  C CD2 . PHE B 649 ? 0.1966 0.3293 0.2411 0.0084  0.0517  -0.0181 641 PHE B CD2 
9562  C CE1 . PHE B 649 ? 0.1499 0.2679 0.1776 -0.0064 0.0464  -0.0232 641 PHE B CE1 
9563  C CE2 . PHE B 649 ? 0.1843 0.3004 0.2178 0.0097  0.0571  -0.0241 641 PHE B CE2 
9564  C CZ  . PHE B 649 ? 0.1987 0.3088 0.2244 0.0014  0.0540  -0.0270 641 PHE B CZ  
9565  N N   . LYS B 650 ? 0.1161 0.3018 0.1933 -0.0171 0.0232  0.0001  642 LYS B N   
9566  C CA  . LYS B 650 ? 0.1058 0.3072 0.1911 -0.0266 0.0199  0.0038  642 LYS B CA  
9567  C C   . LYS B 650 ? 0.1335 0.3230 0.2124 -0.0365 0.0117  0.0042  642 LYS B C   
9568  O O   . LYS B 650 ? 0.1417 0.3304 0.2185 -0.0461 0.0117  0.0061  642 LYS B O   
9569  C CB  . LYS B 650 ? 0.1080 0.3327 0.2073 -0.0227 0.0190  0.0065  642 LYS B CB  
9570  C CG  . LYS B 650 ? 0.1349 0.3768 0.2429 -0.0346 0.0142  0.0095  642 LYS B CG  
9571  C CD  . LYS B 650 ? 0.1643 0.4349 0.2877 -0.0306 0.0130  0.0126  642 LYS B CD  
9572  C CE  . LYS B 650 ? 0.2325 0.5210 0.3641 -0.0448 0.0078  0.0146  642 LYS B CE  
9573  N NZ  . LYS B 650 ? 0.3069 0.6172 0.4491 -0.0398 0.0054  0.0174  642 LYS B NZ  
9574  N N   . ALA B 651 ? 0.1086 0.2873 0.1833 -0.0339 0.0055  0.0028  643 ALA B N   
9575  C CA  . ALA B 651 ? 0.1781 0.3442 0.2458 -0.0430 -0.0013 0.0032  643 ALA B CA  
9576  C C   . ALA B 651 ? 0.1476 0.2949 0.2036 -0.0466 0.0003  0.0035  643 ALA B C   
9577  O O   . ALA B 651 ? 0.2183 0.3573 0.2689 -0.0557 -0.0020 0.0055  643 ALA B O   
9578  C CB  . ALA B 651 ? 0.1275 0.2833 0.1908 -0.0383 -0.0072 0.0012  643 ALA B CB  
9579  N N   . PHE B 652 ? 0.1560 0.2964 0.2071 -0.0397 0.0047  0.0018  644 PHE B N   
9580  C CA  . PHE B 652 ? 0.1223 0.2486 0.1627 -0.0416 0.0057  0.0027  644 PHE B CA  
9581  C C   . PHE B 652 ? 0.1188 0.2538 0.1594 -0.0454 0.0113  0.0046  644 PHE B C   
9582  O O   . PHE B 652 ? 0.1433 0.2706 0.1752 -0.0456 0.0128  0.0056  644 PHE B O   
9583  C CB  . PHE B 652 ? 0.1129 0.2277 0.1469 -0.0335 0.0065  -0.0006 644 PHE B CB  
9584  C CG  . PHE B 652 ? 0.1782 0.2784 0.2077 -0.0309 0.0009  -0.0015 644 PHE B CG  
9585  C CD1 . PHE B 652 ? 0.2671 0.3520 0.2876 -0.0342 -0.0024 0.0010  644 PHE B CD1 
9586  C CD2 . PHE B 652 ? 0.1564 0.2577 0.1897 -0.0245 -0.0002 -0.0042 644 PHE B CD2 
9587  C CE1 . PHE B 652 ? 0.3259 0.3960 0.3412 -0.0318 -0.0066 0.0002  644 PHE B CE1 
9588  C CE2 . PHE B 652 ? 0.2138 0.3013 0.2418 -0.0222 -0.0051 -0.0050 644 PHE B CE2 
9589  C CZ  . PHE B 652 ? 0.3025 0.3742 0.3215 -0.0262 -0.0082 -0.0032 644 PHE B CZ  
9590  N N   . GLY B 653 ? 0.1182 0.2705 0.1686 -0.0480 0.0145  0.0055  645 GLY B N   
9591  C CA  . GLY B 653 ? 0.1221 0.2825 0.1726 -0.0530 0.0197  0.0079  645 GLY B CA  
9592  C C   . GLY B 653 ? 0.1241 0.2899 0.1732 -0.0479 0.0269  0.0054  645 GLY B C   
9593  O O   . GLY B 653 ? 0.1344 0.3036 0.1798 -0.0519 0.0311  0.0071  645 GLY B O   
9594  N N   . PHE B 654 ? 0.1495 0.3146 0.1999 -0.0397 0.0291  0.0012  646 PHE B N   
9595  C CA  . PHE B 654 ? 0.1282 0.2965 0.1759 -0.0360 0.0376  -0.0022 646 PHE B CA  
9596  C C   . PHE B 654 ? 0.1713 0.3558 0.2299 -0.0335 0.0439  -0.0012 646 PHE B C   
9597  O O   . PHE B 654 ? 0.1491 0.3359 0.2114 -0.0253 0.0487  -0.0035 646 PHE B O   
9598  C CB  . PHE B 654 ? 0.1134 0.2697 0.1546 -0.0294 0.0386  -0.0073 646 PHE B CB  
9599  C CG  . PHE B 654 ? 0.1237 0.2678 0.1553 -0.0318 0.0331  -0.0075 646 PHE B CG  
9600  C CD1 . PHE B 654 ? 0.2033 0.3470 0.2258 -0.0354 0.0353  -0.0082 646 PHE B CD1 
9601  C CD2 . PHE B 654 ? 0.1327 0.2673 0.1641 -0.0305 0.0257  -0.0062 646 PHE B CD2 
9602  C CE1 . PHE B 654 ? 0.1223 0.2580 0.1369 -0.0366 0.0302  -0.0070 646 PHE B CE1 
9603  C CE2 . PHE B 654 ? 0.1843 0.3081 0.2071 -0.0317 0.0215  -0.0054 646 PHE B CE2 
9604  C CZ  . PHE B 654 ? 0.1554 0.2809 0.1705 -0.0342 0.0237  -0.0053 646 PHE B CZ  
9605  N N   . THR B 655 ? 0.1185 0.3141 0.1821 -0.0404 0.0442  0.0029  647 THR B N   
9606  C CA  . THR B 655 ? 0.1196 0.3337 0.1946 -0.0397 0.0503  0.0050  647 THR B CA  
9607  C C   . THR B 655 ? 0.1267 0.3420 0.1961 -0.0442 0.0569  0.0057  647 THR B C   
9608  O O   . THR B 655 ? 0.1806 0.3887 0.2401 -0.0505 0.0553  0.0064  647 THR B O   
9609  C CB  . THR B 655 ? 0.1773 0.4048 0.2642 -0.0453 0.0444  0.0092  647 THR B CB  
9610  O OG1 . THR B 655 ? 0.1584 0.3812 0.2402 -0.0562 0.0415  0.0119  647 THR B OG1 
9611  C CG2 . THR B 655 ? 0.1139 0.3374 0.2033 -0.0421 0.0362  0.0084  647 THR B CG2 
9612  N N   . VAL B 656 ? 0.1549 0.3761 0.2292 -0.0396 0.0638  0.0060  648 VAL B N   
9613  C CA  . VAL B 656 ? 0.1543 0.3735 0.2226 -0.0429 0.0696  0.0068  648 VAL B CA  
9614  C C   . VAL B 656 ? 0.1797 0.4040 0.2497 -0.0530 0.0656  0.0114  648 VAL B C   
9615  O O   . VAL B 656 ? 0.1880 0.4057 0.2474 -0.0580 0.0667  0.0122  648 VAL B O   
9616  C CB  . VAL B 656 ? 0.1489 0.3737 0.2236 -0.0359 0.0785  0.0070  648 VAL B CB  
9617  C CG1 . VAL B 656 ? 0.1690 0.3932 0.2388 -0.0402 0.0841  0.0083  648 VAL B CG1 
9618  C CG2 . VAL B 656 ? 0.2359 0.4493 0.3045 -0.0265 0.0848  0.0024  648 VAL B CG2 
9619  N N   . ASP B 657 ? 0.1418 0.3772 0.2239 -0.0563 0.0611  0.0145  649 ASP B N   
9620  C CA  . ASP B 657 ? 0.2085 0.4459 0.2913 -0.0668 0.0584  0.0184  649 ASP B CA  
9621  C C   . ASP B 657 ? 0.1796 0.4033 0.2497 -0.0731 0.0544  0.0194  649 ASP B C   
9622  O O   . ASP B 657 ? 0.1983 0.4168 0.2610 -0.0794 0.0562  0.0225  649 ASP B O   
9623  C CB  . ASP B 657 ? 0.1654 0.4153 0.2616 -0.0706 0.0532  0.0203  649 ASP B CB  
9624  C CG  . ASP B 657 ? 0.3039 0.5701 0.4125 -0.0681 0.0577  0.0218  649 ASP B CG  
9625  O OD1 . ASP B 657 ? 0.3117 0.5778 0.4184 -0.0637 0.0656  0.0217  649 ASP B OD1 
9626  O OD2 . ASP B 657 ? 0.3855 0.6648 0.5053 -0.0709 0.0532  0.0231  649 ASP B OD2 
9627  N N   . ASN B 658 ? 0.1581 0.3755 0.2252 -0.0708 0.0495  0.0174  650 ASN B N   
9628  C CA  . ASN B 658 ? 0.1736 0.3743 0.2277 -0.0744 0.0451  0.0190  650 ASN B CA  
9629  C C   . ASN B 658 ? 0.1810 0.3757 0.2221 -0.0723 0.0492  0.0187  650 ASN B C   
9630  O O   . ASN B 658 ? 0.1828 0.3691 0.2134 -0.0763 0.0486  0.0226  650 ASN B O   
9631  C CB  . ASN B 658 ? 0.1384 0.3276 0.1908 -0.0699 0.0377  0.0165  650 ASN B CB  
9632  C CG  . ASN B 658 ? 0.2139 0.3843 0.2535 -0.0725 0.0332  0.0192  650 ASN B CG  
9633  O OD1 . ASN B 658 ? 0.2267 0.3923 0.2625 -0.0800 0.0335  0.0236  650 ASN B OD1 
9634  N ND2 . ASN B 658 ? 0.1408 0.3003 0.1733 -0.0662 0.0300  0.0169  650 ASN B ND2 
9635  N N   . VAL B 659 ? 0.1443 0.3430 0.1846 -0.0661 0.0537  0.0140  651 VAL B N   
9636  C CA  . VAL B 659 ? 0.1825 0.3758 0.2093 -0.0652 0.0569  0.0127  651 VAL B CA  
9637  C C   . VAL B 659 ? 0.1887 0.3846 0.2127 -0.0693 0.0612  0.0162  651 VAL B C   
9638  O O   . VAL B 659 ? 0.2110 0.4025 0.2233 -0.0723 0.0611  0.0193  651 VAL B O   
9639  C CB  . VAL B 659 ? 0.1491 0.3399 0.1737 -0.0582 0.0609  0.0057  651 VAL B CB  
9640  C CG1 . VAL B 659 ? 0.1742 0.3603 0.1846 -0.0590 0.0639  0.0035  651 VAL B CG1 
9641  C CG2 . VAL B 659 ? 0.1398 0.3260 0.1648 -0.0544 0.0570  0.0021  651 VAL B CG2 
9642  N N   . VAL B 660 ? 0.1634 0.3670 0.1982 -0.0692 0.0651  0.0167  652 VAL B N   
9643  C CA  . VAL B 660 ? 0.1799 0.3862 0.2130 -0.0730 0.0701  0.0199  652 VAL B CA  
9644  C C   . VAL B 660 ? 0.1849 0.3875 0.2140 -0.0810 0.0674  0.0260  652 VAL B C   
9645  O O   . VAL B 660 ? 0.1958 0.3941 0.2143 -0.0836 0.0702  0.0293  652 VAL B O   
9646  C CB  . VAL B 660 ? 0.1750 0.3919 0.2222 -0.0709 0.0748  0.0196  652 VAL B CB  
9647  C CG1 . VAL B 660 ? 0.1862 0.4067 0.2340 -0.0765 0.0792  0.0238  652 VAL B CG1 
9648  C CG2 . VAL B 660 ? 0.1919 0.4081 0.2384 -0.0626 0.0807  0.0148  652 VAL B CG2 
9649  N N   . ASP B 661 ? 0.1878 0.3905 0.2242 -0.0850 0.0626  0.0279  653 ASP B N   
9650  C CA  . ASP B 661 ? 0.1857 0.3806 0.2167 -0.0933 0.0615  0.0336  653 ASP B CA  
9651  C C   . ASP B 661 ? 0.1901 0.3730 0.2044 -0.0924 0.0601  0.0369  653 ASP B C   
9652  O O   . ASP B 661 ? 0.2219 0.3968 0.2259 -0.0962 0.0626  0.0427  653 ASP B O   
9653  C CB  . ASP B 661 ? 0.2578 0.4531 0.2981 -0.0985 0.0565  0.0337  653 ASP B CB  
9654  C CG  . ASP B 661 ? 0.3568 0.5660 0.4128 -0.1009 0.0577  0.0322  653 ASP B CG  
9655  O OD1 . ASP B 661 ? 0.3432 0.5589 0.4016 -0.1007 0.0635  0.0330  653 ASP B OD1 
9656  O OD2 . ASP B 661 ? 0.4295 0.6441 0.4951 -0.1027 0.0528  0.0305  653 ASP B OD2 
9657  N N   . THR B 662 ? 0.2026 0.3836 0.2139 -0.0863 0.0561  0.0336  654 THR B N   
9658  C CA  . THR B 662 ? 0.2713 0.4407 0.2677 -0.0826 0.0530  0.0363  654 THR B CA  
9659  C C   . THR B 662 ? 0.2669 0.4421 0.2522 -0.0822 0.0579  0.0381  654 THR B C   
9660  O O   . THR B 662 ? 0.2198 0.3880 0.1923 -0.0819 0.0577  0.0444  654 THR B O   
9661  C CB  . THR B 662 ? 0.1969 0.3629 0.1939 -0.0757 0.0473  0.0311  654 THR B CB  
9662  O OG1 . THR B 662 ? 0.2142 0.3735 0.2194 -0.0760 0.0424  0.0301  654 THR B OG1 
9663  C CG2 . THR B 662 ? 0.2128 0.3710 0.1960 -0.0715 0.0440  0.0342  654 THR B CG2 
9664  N N   . VAL B 663 ? 0.1910 0.3737 0.1801 -0.0797 0.0612  0.0321  655 VAL B N   
9665  C CA  . VAL B 663 ? 0.2015 0.3855 0.1799 -0.0788 0.0648  0.0323  655 VAL B CA  
9666  C C   . VAL B 663 ? 0.2443 0.4257 0.2192 -0.0833 0.0688  0.0393  655 VAL B C   
9667  O O   . VAL B 663 ? 0.2898 0.4680 0.2514 -0.0829 0.0695  0.0441  655 VAL B O   
9668  C CB  . VAL B 663 ? 0.1994 0.3884 0.1822 -0.0759 0.0690  0.0245  655 VAL B CB  
9669  C CG1 . VAL B 663 ? 0.2127 0.4026 0.1853 -0.0767 0.0737  0.0249  655 VAL B CG1 
9670  C CG2 . VAL B 663 ? 0.2312 0.4191 0.2126 -0.0716 0.0660  0.0176  655 VAL B CG2 
9671  N N   . LYS B 664 ? 0.2322 0.4154 0.2189 -0.0876 0.0715  0.0400  656 LYS B N   
9672  C CA  . LYS B 664 ? 0.2715 0.4511 0.2553 -0.0928 0.0763  0.0460  656 LYS B CA  
9673  C C   . LYS B 664 ? 0.2576 0.4245 0.2293 -0.0950 0.0748  0.0539  656 LYS B C   
9674  O O   . LYS B 664 ? 0.2683 0.4291 0.2294 -0.0962 0.0791  0.0598  656 LYS B O   
9675  C CB  . LYS B 664 ? 0.2669 0.4518 0.2668 -0.0979 0.0784  0.0450  656 LYS B CB  
9676  C CG  . LYS B 664 ? 0.3090 0.5056 0.3197 -0.0947 0.0822  0.0398  656 LYS B CG  
9677  C CD  . LYS B 664 ? 0.3360 0.5406 0.3629 -0.0993 0.0834  0.0400  656 LYS B CD  
9678  C CE  . LYS B 664 ? 0.4032 0.6198 0.4413 -0.0942 0.0876  0.0360  656 LYS B CE  
9679  N NZ  . LYS B 664 ? 0.3995 0.6267 0.4523 -0.0988 0.0904  0.0376  656 LYS B NZ  
9680  N N   . SER B 665 ? 0.2332 0.3944 0.2053 -0.0947 0.0696  0.0547  657 SER B N   
9681  C CA  . SER B 665 ? 0.3388 0.4843 0.2993 -0.0961 0.0692  0.0628  657 SER B CA  
9682  C C   . SER B 665 ? 0.3542 0.4956 0.2974 -0.0891 0.0689  0.0685  657 SER B C   
9683  O O   . SER B 665 ? 0.3398 0.4666 0.2710 -0.0883 0.0705  0.0770  657 SER B O   
9684  C CB  . SER B 665 ? 0.3150 0.4523 0.2802 -0.0953 0.0629  0.0609  657 SER B CB  
9685  O OG  . SER B 665 ? 0.3250 0.4629 0.2857 -0.0863 0.0571  0.0588  657 SER B OG  
9686  N N   . VAL B 666 ? 0.2968 0.4499 0.2378 -0.0837 0.0668  0.0641  658 VAL B N   
9687  C CA  . VAL B 666 ? 0.2858 0.4387 0.2115 -0.0772 0.0653  0.0690  658 VAL B CA  
9688  C C   . VAL B 666 ? 0.4229 0.5815 0.3426 -0.0775 0.0699  0.0688  658 VAL B C   
9689  O O   . VAL B 666 ? 0.4001 0.5609 0.3072 -0.0725 0.0685  0.0724  658 VAL B O   
9690  C CB  . VAL B 666 ? 0.3196 0.4807 0.2444 -0.0714 0.0585  0.0644  658 VAL B CB  
9691  C CG1 . VAL B 666 ? 0.2827 0.4369 0.2123 -0.0707 0.0546  0.0653  658 VAL B CG1 
9692  C CG2 . VAL B 666 ? 0.3231 0.4965 0.2556 -0.0725 0.0584  0.0534  658 VAL B CG2 
9693  N N   . LEU B 667 ? 0.3844 0.5456 0.3126 -0.0829 0.0752  0.0653  659 LEU B N   
9694  C CA  . LEU B 667 ? 0.5100 0.6747 0.4322 -0.0835 0.0806  0.0656  659 LEU B CA  
9695  C C   . LEU B 667 ? 0.6536 0.8067 0.5642 -0.0841 0.0855  0.0758  659 LEU B C   
9696  O O   . LEU B 667 ? 0.6638 0.8059 0.5774 -0.0884 0.0886  0.0802  659 LEU B O   
9697  C CB  . LEU B 667 ? 0.4554 0.6264 0.3913 -0.0878 0.0854  0.0592  659 LEU B CB  
9698  C CG  . LEU B 667 ? 0.3729 0.5529 0.3181 -0.0857 0.0828  0.0493  659 LEU B CG  
9699  C CD1 . LEU B 667 ? 0.3963 0.5814 0.3535 -0.0878 0.0889  0.0450  659 LEU B CD1 
9700  C CD2 . LEU B 667 ? 0.3605 0.5446 0.2939 -0.0818 0.0804  0.0458  659 LEU B CD2 
9701  O OXT . LEU B 667 ? 0.7315 0.8849 0.6286 -0.0806 0.0870  0.0796  659 LEU B OXT 
9702  N N   . SER C 10  ? 0.7609 0.9777 0.6624 0.1653  0.0644  -0.0945 2   SER C N   
9703  C CA  . SER C 10  ? 0.6668 0.8578 0.5842 0.1655  0.0549  -0.1050 2   SER C CA  
9704  C C   . SER C 10  ? 0.5531 0.7648 0.4980 0.1525  0.0660  -0.0885 2   SER C C   
9705  O O   . SER C 10  ? 0.4571 0.6505 0.4178 0.1436  0.0611  -0.0896 2   SER C O   
9706  C CB  . SER C 10  ? 0.7219 0.9052 0.6327 0.1892  0.0433  -0.1246 2   SER C CB  
9707  O OG  . SER C 10  ? 0.7157 0.8658 0.6405 0.1893  0.0283  -0.1359 2   SER C OG  
9708  N N   . GLN C 11  ? 0.4481 0.6994 0.4000 0.1520  0.0797  -0.0724 3   GLN C N   
9709  C CA  . GLN C 11  ? 0.3764 0.6479 0.3576 0.1388  0.0877  -0.0548 3   GLN C CA  
9710  C C   . GLN C 11  ? 0.3093 0.5745 0.3024 0.1162  0.0879  -0.0419 3   GLN C C   
9711  O O   . GLN C 11  ? 0.2637 0.5306 0.2807 0.1055  0.0873  -0.0343 3   GLN C O   
9712  C CB  . GLN C 11  ? 0.4251 0.7413 0.4145 0.1427  0.1001  -0.0379 3   GLN C CB  
9713  N N   . LEU C 12  ? 0.3295 0.5879 0.3067 0.1098  0.0870  -0.0403 4   LEU C N   
9714  C CA  . LEU C 12  ? 0.3261 0.5783 0.3148 0.0899  0.0852  -0.0308 4   LEU C CA  
9715  C C   . LEU C 12  ? 0.3485 0.5680 0.3404 0.0866  0.0758  -0.0446 4   LEU C C   
9716  O O   . LEU C 12  ? 0.3279 0.5381 0.3376 0.0690  0.0706  -0.0359 4   LEU C O   
9717  C CB  . LEU C 12  ? 0.3664 0.6180 0.3367 0.0848  0.0853  -0.0272 4   LEU C CB  
9718  C CG  . LEU C 12  ? 0.4545 0.7412 0.4205 0.0870  0.0938  -0.0099 4   LEU C CG  
9719  C CD1 . LEU C 12  ? 0.4366 0.7237 0.3913 0.0762  0.0923  -0.0013 4   LEU C CD1 
9720  C CD2 . LEU C 12  ? 0.3671 0.6885 0.3654 0.0786  0.1002  0.0133  4   LEU C CD2 
9721  N N   . ALA C 13  ? 0.3669 0.5602 0.3438 0.1003  0.0681  -0.0638 5   ALA C N   
9722  C CA  . ALA C 13  ? 0.2944 0.4531 0.2796 0.0932  0.0558  -0.0698 5   ALA C CA  
9723  C C   . ALA C 13  ? 0.2978 0.4634 0.3013 0.0977  0.0556  -0.0687 5   ALA C C   
9724  O O   . ALA C 13  ? 0.2738 0.4258 0.2904 0.0858  0.0497  -0.0633 5   ALA C O   
9725  C CB  . ALA C 13  ? 0.3090 0.4344 0.2779 0.1032  0.0428  -0.0868 5   ALA C CB  
9726  N N   . ASN C 14  ? 0.2738 0.4627 0.2778 0.1158  0.0619  -0.0735 6   ASN C N   
9727  C CA  . ASN C 14  ? 0.3123 0.5068 0.3351 0.1219  0.0601  -0.0739 6   ASN C CA  
9728  C C   . ASN C 14  ? 0.2630 0.4741 0.3086 0.1054  0.0644  -0.0559 6   ASN C C   
9729  O O   . ASN C 14  ? 0.2395 0.4401 0.2988 0.1017  0.0573  -0.0543 6   ASN C O   
9730  C CB  . ASN C 14  ? 0.3254 0.5348 0.3443 0.1389  0.0629  -0.0789 6   ASN C CB  
9731  C CG  . ASN C 14  ? 0.3766 0.5588 0.3828 0.1568  0.0487  -0.1001 6   ASN C CG  
9732  O OD1 . ASN C 14  ? 0.3274 0.4780 0.3340 0.1560  0.0354  -0.1091 6   ASN C OD1 
9733  N ND2 . ASN C 14  ? 0.3466 0.5416 0.3443 0.1739  0.0493  -0.1080 6   ASN C ND2 
9734  N N   . VAL C 15  ? 0.2520 0.4879 0.3031 0.0954  0.0730  -0.0417 7   VAL C N   
9735  C CA  . VAL C 15  ? 0.1975 0.4465 0.2740 0.0808  0.0718  -0.0257 7   VAL C CA  
9736  C C   . VAL C 15  ? 0.2216 0.4392 0.2979 0.0667  0.0595  -0.0273 7   VAL C C   
9737  O O   . VAL C 15  ? 0.2295 0.4467 0.3215 0.0617  0.0533  -0.0227 7   VAL C O   
9738  C CB  . VAL C 15  ? 0.2081 0.4879 0.2955 0.0716  0.0789  -0.0077 7   VAL C CB  
9739  C CG1 . VAL C 15  ? 0.2035 0.4663 0.2730 0.0618  0.0761  -0.0085 7   VAL C CG1 
9740  C CG2 . VAL C 15  ? 0.1816 0.4728 0.3015 0.0579  0.0722  0.0082  7   VAL C CG2 
9741  N N   . ILE C 16  ? 0.1920 0.3853 0.2502 0.0616  0.0557  -0.0339 8   ILE C N   
9742  C CA  . ILE C 16  ? 0.1657 0.3358 0.2225 0.0516  0.0463  -0.0352 8   ILE C CA  
9743  C C   . ILE C 16  ? 0.2341 0.3912 0.2919 0.0581  0.0409  -0.0395 8   ILE C C   
9744  O O   . ILE C 16  ? 0.2312 0.3849 0.2951 0.0531  0.0351  -0.0356 8   ILE C O   
9745  C CB  . ILE C 16  ? 0.2033 0.3541 0.2443 0.0458  0.0440  -0.0399 8   ILE C CB  
9746  C CG1 . ILE C 16  ? 0.2299 0.3924 0.2708 0.0386  0.0472  -0.0342 8   ILE C CG1 
9747  C CG2 . ILE C 16  ? 0.2911 0.4268 0.3322 0.0377  0.0367  -0.0396 8   ILE C CG2 
9748  C CD1 . ILE C 16  ? 0.2097 0.3530 0.2353 0.0342  0.0444  -0.0396 8   ILE C CD1 
9749  N N   . ARG C 17  ? 0.2850 0.4351 0.3369 0.0707  0.0408  -0.0479 9   ARG C N   
9750  C CA  . ARG C 17  ? 0.3029 0.4373 0.3592 0.0768  0.0319  -0.0510 9   ARG C CA  
9751  C C   . ARG C 17  ? 0.2991 0.4478 0.3719 0.0790  0.0312  -0.0455 9   ARG C C   
9752  O O   . ARG C 17  ? 0.2613 0.4000 0.3387 0.0749  0.0232  -0.0405 9   ARG C O   
9753  C CB  . ARG C 17  ? 0.3639 0.4884 0.4132 0.0930  0.0283  -0.0643 9   ARG C CB  
9754  C CG  . ARG C 17  ? 0.3787 0.4790 0.4347 0.0991  0.0131  -0.0686 9   ARG C CG  
9755  C CD  . ARG C 17  ? 0.3362 0.4204 0.3830 0.1155  0.0045  -0.0855 9   ARG C CD  
9756  N NE  . ARG C 17  ? 0.3253 0.3835 0.3651 0.1073  -0.0048 -0.0855 9   ARG C NE  
9757  C CZ  . ARG C 17  ? 0.2933 0.3475 0.3163 0.1107  -0.0030 -0.0941 9   ARG C CZ  
9758  N NH1 . ARG C 17  ? 0.2902 0.3676 0.2989 0.1227  0.0092  -0.1024 9   ARG C NH1 
9759  N NH2 . ARG C 17  ? 0.3041 0.3333 0.3258 0.1020  -0.0138 -0.0926 9   ARG C NH2 
9760  N N   . PHE C 18  ? 0.2156 0.3903 0.2987 0.0851  0.0391  -0.0441 10  PHE C N   
9761  C CA  . PHE C 18  ? 0.1871 0.3746 0.2895 0.0881  0.0367  -0.0391 10  PHE C CA  
9762  C C   . PHE C 18  ? 0.1720 0.3688 0.2856 0.0751  0.0341  -0.0281 10  PHE C C   
9763  O O   . PHE C 18  ? 0.1863 0.3818 0.3106 0.0745  0.0263  -0.0246 10  PHE C O   
9764  C CB  . PHE C 18  ? 0.2580 0.4725 0.3716 0.1037  0.0451  -0.0423 10  PHE C CB  
9765  C CG  . PHE C 18  ? 0.3532 0.5555 0.4576 0.1217  0.0415  -0.0578 10  PHE C CG  
9766  C CD1 . PHE C 18  ? 0.4653 0.6552 0.5809 0.1302  0.0303  -0.0629 10  PHE C CD1 
9767  C CD2 . PHE C 18  ? 0.3263 0.5261 0.4114 0.1305  0.0456  -0.0683 10  PHE C CD2 
9768  C CE1 . PHE C 18  ? 0.5222 0.6966 0.6330 0.1478  0.0215  -0.0791 10  PHE C CE1 
9769  C CE2 . PHE C 18  ? 0.3799 0.5642 0.4569 0.1494  0.0370  -0.0860 10  PHE C CE2 
9770  C CZ  . PHE C 18  ? 0.5089 0.6798 0.6003 0.1582  0.0240  -0.0918 10  PHE C CZ  
9771  N N   . LEU C 19  ? 0.1648 0.3687 0.2769 0.0654  0.0373  -0.0234 11  LEU C N   
9772  C CA  . LEU C 19  ? 0.2586 0.4627 0.3799 0.0544  0.0284  -0.0171 11  LEU C CA  
9773  C C   . LEU C 19  ? 0.2085 0.3917 0.3156 0.0524  0.0194  -0.0211 11  LEU C C   
9774  O O   . LEU C 19  ? 0.2118 0.3954 0.3253 0.0515  0.0096  -0.0189 11  LEU C O   
9775  C CB  . LEU C 19  ? 0.2068 0.4149 0.3278 0.0445  0.0290  -0.0134 11  LEU C CB  
9776  C CG  . LEU C 19  ? 0.2509 0.4845 0.3977 0.0390  0.0294  -0.0002 11  LEU C CG  
9777  C CD1 . LEU C 19  ? 0.2485 0.4774 0.3938 0.0277  0.0247  0.0027  11  LEU C CD1 
9778  C CD2 . LEU C 19  ? 0.1545 0.3967 0.3286 0.0371  0.0175  0.0069  11  LEU C CD2 
9779  N N   . SER C 20  ? 0.1714 0.3385 0.2598 0.0523  0.0218  -0.0257 12  SER C N   
9780  C CA  . SER C 20  ? 0.1808 0.3356 0.2572 0.0502  0.0156  -0.0247 12  SER C CA  
9781  C C   . SER C 20  ? 0.2125 0.3644 0.2938 0.0558  0.0099  -0.0209 12  SER C C   
9782  O O   . SER C 20  ? 0.1773 0.3307 0.2551 0.0552  0.0028  -0.0168 12  SER C O   
9783  C CB  . SER C 20  ? 0.2010 0.3424 0.2638 0.0475  0.0190  -0.0265 12  SER C CB  
9784  O OG  . SER C 20  ? 0.1978 0.3411 0.2564 0.0420  0.0227  -0.0299 12  SER C OG  
9785  N N   . ALA C 21  ? 0.1798 0.3277 0.2684 0.0631  0.0113  -0.0232 13  ALA C N   
9786  C CA  . ALA C 21  ? 0.2082 0.3514 0.3054 0.0687  0.0031  -0.0197 13  ALA C CA  
9787  C C   . ALA C 21  ? 0.2064 0.3634 0.3172 0.0704  -0.0008 -0.0170 13  ALA C C   
9788  O O   . ALA C 21  ? 0.2380 0.3919 0.3498 0.0706  -0.0101 -0.0112 13  ALA C O   
9789  C CB  . ALA C 21  ? 0.2871 0.4227 0.3918 0.0793  0.0022  -0.0269 13  ALA C CB  
9790  N N   . ASP C 22  ? 0.1789 0.3527 0.3025 0.0714  0.0050  -0.0189 14  ASP C N   
9791  C CA  . ASP C 22  ? 0.2066 0.3940 0.3501 0.0721  -0.0010 -0.0144 14  ASP C CA  
9792  C C   . ASP C 22  ? 0.2011 0.3844 0.3375 0.0656  -0.0121 -0.0120 14  ASP C C   
9793  O O   . ASP C 22  ? 0.1830 0.3664 0.3264 0.0678  -0.0233 -0.0092 14  ASP C O   
9794  C CB  . ASP C 22  ? 0.1687 0.3799 0.3328 0.0728  0.0072  -0.0118 14  ASP C CB  
9795  C CG  . ASP C 22  ? 0.2258 0.4490 0.3974 0.0852  0.0173  -0.0158 14  ASP C CG  
9796  O OD1 . ASP C 22  ? 0.2601 0.4732 0.4323 0.0941  0.0124  -0.0207 14  ASP C OD1 
9797  O OD2 . ASP C 22  ? 0.2057 0.4497 0.3823 0.0873  0.0290  -0.0141 14  ASP C OD2 
9798  N N   . ALA C 23  ? 0.2143 0.3941 0.3362 0.0595  -0.0108 -0.0147 15  ALA C N   
9799  C CA  . ALA C 23  ? 0.1760 0.3533 0.2893 0.0577  -0.0231 -0.0167 15  ALA C CA  
9800  C C   . ALA C 23  ? 0.2089 0.3793 0.3005 0.0616  -0.0277 -0.0151 15  ALA C C   
9801  O O   . ALA C 23  ? 0.1998 0.3714 0.2860 0.0655  -0.0403 -0.0159 15  ALA C O   
9802  C CB  . ALA C 23  ? 0.1699 0.3460 0.2750 0.0523  -0.0218 -0.0218 15  ALA C CB  
9803  N N   . VAL C 24  ? 0.1960 0.3603 0.2760 0.0608  -0.0192 -0.0113 16  VAL C N   
9804  C CA  . VAL C 24  ? 0.2106 0.3730 0.2752 0.0627  -0.0231 -0.0031 16  VAL C CA  
9805  C C   . VAL C 24  ? 0.2142 0.3756 0.2897 0.0670  -0.0328 0.0024  16  VAL C C   
9806  O O   . VAL C 24  ? 0.2281 0.3934 0.2915 0.0701  -0.0418 0.0077  16  VAL C O   
9807  C CB  . VAL C 24  ? 0.2177 0.3728 0.2780 0.0590  -0.0155 0.0034  16  VAL C CB  
9808  C CG1 . VAL C 24  ? 0.2641 0.4194 0.3186 0.0590  -0.0215 0.0188  16  VAL C CG1 
9809  C CG2 . VAL C 24  ? 0.2211 0.3788 0.2685 0.0549  -0.0079 -0.0003 16  VAL C CG2 
9810  N N   . GLN C 25  ? 0.2313 0.3898 0.3291 0.0689  -0.0315 0.0007  17  GLN C N   
9811  C CA  . GLN C 25  ? 0.2639 0.4212 0.3760 0.0736  -0.0416 0.0051  17  GLN C CA  
9812  C C   . GLN C 25  ? 0.2218 0.3863 0.3389 0.0755  -0.0527 0.0031  17  GLN C C   
9813  O O   . GLN C 25  ? 0.2360 0.3985 0.3504 0.0787  -0.0649 0.0085  17  GLN C O   
9814  C CB  . GLN C 25  ? 0.2521 0.4091 0.3882 0.0786  -0.0374 0.0009  17  GLN C CB  
9815  C CG  . GLN C 25  ? 0.3851 0.5361 0.5354 0.0841  -0.0487 0.0058  17  GLN C CG  
9816  C CD  . GLN C 25  ? 0.4030 0.5404 0.5397 0.0808  -0.0564 0.0170  17  GLN C CD  
9817  O OE1 . GLN C 25  ? 0.4898 0.6198 0.6177 0.0772  -0.0515 0.0189  17  GLN C OE1 
9818  N NE2 . GLN C 25  ? 0.3842 0.5199 0.5212 0.0813  -0.0696 0.0269  17  GLN C NE2 
9819  N N   . LYS C 26  ? 0.2276 0.3993 0.3540 0.0735  -0.0517 -0.0034 18  LYS C N   
9820  C CA  . LYS C 26  ? 0.2425 0.4176 0.3794 0.0751  -0.0675 -0.0055 18  LYS C CA  
9821  C C   . LYS C 26  ? 0.2605 0.4317 0.3674 0.0790  -0.0792 -0.0088 18  LYS C C   
9822  O O   . LYS C 26  ? 0.2764 0.4461 0.3833 0.0843  -0.0964 -0.0097 18  LYS C O   
9823  C CB  . LYS C 26  ? 0.2035 0.3869 0.3624 0.0703  -0.0671 -0.0083 18  LYS C CB  
9824  C CG  . LYS C 26  ? 0.2144 0.3998 0.3960 0.0709  -0.0880 -0.0085 18  LYS C CG  
9825  C CD  . LYS C 26  ? 0.2291 0.4246 0.4410 0.0635  -0.0897 -0.0055 18  LYS C CD  
9826  C CE  . LYS C 26  ? 0.3054 0.5017 0.5492 0.0628  -0.1149 -0.0027 18  LYS C CE  
9827  N NZ  . LYS C 26  ? 0.2787 0.4580 0.5018 0.0681  -0.1391 -0.0157 18  LYS C NZ  
9828  N N   . ALA C 27  ? 0.2730 0.4448 0.3538 0.0782  -0.0706 -0.0111 19  ALA C N   
9829  C CA  . ALA C 27  ? 0.2526 0.4284 0.3012 0.0854  -0.0782 -0.0136 19  ALA C CA  
9830  C C   . ALA C 27  ? 0.3329 0.5116 0.3662 0.0880  -0.0781 -0.0000 19  ALA C C   
9831  O O   . ALA C 27  ? 0.3290 0.5158 0.3367 0.0964  -0.0870 0.0008  19  ALA C O   
9832  C CB  . ALA C 27  ? 0.2770 0.4577 0.3066 0.0844  -0.0676 -0.0188 19  ALA C CB  
9833  N N   . ASN C 28  ? 0.2922 0.4652 0.3413 0.0822  -0.0703 0.0108  20  ASN C N   
9834  C CA  . ASN C 28  ? 0.3090 0.4829 0.3493 0.0818  -0.0717 0.0276  20  ASN C CA  
9835  C C   . ASN C 28  ? 0.2862 0.4745 0.2969 0.0823  -0.0647 0.0364  20  ASN C C   
9836  O O   . ASN C 28  ? 0.3071 0.5070 0.3002 0.0855  -0.0695 0.0509  20  ASN C O   
9837  C CB  . ASN C 28  ? 0.4234 0.5963 0.4649 0.0874  -0.0886 0.0319  20  ASN C CB  
9838  C CG  . ASN C 28  ? 0.5712 0.7411 0.6164 0.0845  -0.0924 0.0514  20  ASN C CG  
9839  O OD1 . ASN C 28  ? 0.6426 0.8048 0.7025 0.0783  -0.0856 0.0585  20  ASN C OD1 
9840  N ND2 . ASN C 28  ? 0.6476 0.8219 0.6802 0.0894  -0.1062 0.0603  20  ASN C ND2 
9841  N N   . SER C 29  ? 0.2725 0.4635 0.2790 0.0794  -0.0528 0.0292  21  SER C N   
9842  C CA  . SER C 29  ? 0.3217 0.5308 0.3038 0.0813  -0.0444 0.0347  21  SER C CA  
9843  C C   . SER C 29  ? 0.2591 0.4628 0.2493 0.0750  -0.0323 0.0267  21  SER C C   
9844  O O   . SER C 29  ? 0.2442 0.4364 0.2473 0.0737  -0.0329 0.0112  21  SER C O   
9845  C CB  . SER C 29  ? 0.3333 0.5583 0.2875 0.0951  -0.0526 0.0230  21  SER C CB  
9846  O OG  . SER C 29  ? 0.3066 0.5553 0.2363 0.1006  -0.0432 0.0262  21  SER C OG  
9847  N N   . GLY C 30  ? 0.2596 0.4725 0.2450 0.0703  -0.0224 0.0399  22  GLY C N   
9848  C CA  . GLY C 30  ? 0.3957 0.6037 0.3870 0.0646  -0.0122 0.0335  22  GLY C CA  
9849  C C   . GLY C 30  ? 0.3974 0.5919 0.4082 0.0544  -0.0088 0.0468  22  GLY C C   
9850  O O   . GLY C 30  ? 0.3485 0.5366 0.3708 0.0514  -0.0154 0.0615  22  GLY C O   
9851  N N   . HIS C 31  ? 0.3739 0.5616 0.3898 0.0496  -0.0014 0.0402  23  HIS C N   
9852  C CA  . HIS C 31  ? 0.4427 0.6170 0.4754 0.0413  -0.0007 0.0507  23  HIS C CA  
9853  C C   . HIS C 31  ? 0.3703 0.5219 0.4139 0.0406  -0.0003 0.0333  23  HIS C C   
9854  O O   . HIS C 31  ? 0.3973 0.5486 0.4355 0.0398  0.0062  0.0209  23  HIS C O   
9855  C CB  . HIS C 31  ? 0.5347 0.7241 0.5636 0.0370  0.0068  0.0613  23  HIS C CB  
9856  C CG  . HIS C 31  ? 0.6843 0.9075 0.6955 0.0422  0.0111  0.0738  23  HIS C CG  
9857  N ND1 . HIS C 31  ? 0.7038 0.9433 0.6927 0.0530  0.0141  0.0574  23  HIS C ND1 
9858  C CD2 . HIS C 31  ? 0.7330 0.9797 0.7453 0.0397  0.0121  0.1017  23  HIS C CD2 
9859  C CE1 . HIS C 31  ? 0.7306 1.0032 0.7032 0.0597  0.0178  0.0714  23  HIS C CE1 
9860  N NE2 . HIS C 31  ? 0.7339 1.0143 0.7203 0.0510  0.0183  0.1007  23  HIS C NE2 
9861  N N   . PRO C 32  ? 0.3575 0.4920 0.4158 0.0421  -0.0073 0.0317  24  PRO C N   
9862  C CA  . PRO C 32  ? 0.3173 0.4375 0.3822 0.0452  -0.0051 0.0147  24  PRO C CA  
9863  C C   . PRO C 32  ? 0.3489 0.4514 0.4211 0.0425  -0.0081 0.0146  24  PRO C C   
9864  O O   . PRO C 32  ? 0.3317 0.4261 0.4022 0.0457  -0.0044 0.0003  24  PRO C O   
9865  C CB  . PRO C 32  ? 0.2886 0.4041 0.3651 0.0523  -0.0119 0.0112  24  PRO C CB  
9866  C CG  . PRO C 32  ? 0.3500 0.4632 0.4332 0.0499  -0.0227 0.0293  24  PRO C CG  
9867  C CD  . PRO C 32  ? 0.3584 0.4896 0.4268 0.0438  -0.0180 0.0433  24  PRO C CD  
9868  N N   . GLY C 33  ? 0.3417 0.4394 0.4234 0.0368  -0.0162 0.0320  25  GLY C N   
9869  C CA  . GLY C 33  ? 0.2333 0.3086 0.3287 0.0351  -0.0260 0.0321  25  GLY C CA  
9870  C C   . GLY C 33  ? 0.2928 0.3660 0.3805 0.0314  -0.0187 0.0247  25  GLY C C   
9871  O O   . GLY C 33  ? 0.2622 0.3165 0.3511 0.0358  -0.0231 0.0106  25  GLY C O   
9872  N N   . ALA C 34  ? 0.2686 0.3620 0.3474 0.0251  -0.0084 0.0330  26  ALA C N   
9873  C CA  . ALA C 34  ? 0.2411 0.3331 0.3147 0.0214  -0.0025 0.0263  26  ALA C CA  
9874  C C   . ALA C 34  ? 0.2438 0.3317 0.3039 0.0266  0.0045  0.0043  26  ALA C C   
9875  O O   . ALA C 34  ? 0.2451 0.3183 0.3044 0.0264  0.0029  -0.0047 26  ALA C O   
9876  C CB  . ALA C 34  ? 0.3088 0.4275 0.3771 0.0165  0.0064  0.0388  26  ALA C CB  
9877  N N   . PRO C 35  ? 0.2435 0.3446 0.2947 0.0308  0.0109  -0.0031 27  PRO C N   
9878  C CA  . PRO C 35  ? 0.2843 0.3843 0.3291 0.0339  0.0160  -0.0183 27  PRO C CA  
9879  C C   . PRO C 35  ? 0.2872 0.3730 0.3349 0.0414  0.0126  -0.0270 27  PRO C C   
9880  O O   . PRO C 35  ? 0.3047 0.3859 0.3457 0.0432  0.0155  -0.0363 27  PRO C O   
9881  C CB  . PRO C 35  ? 0.2989 0.4155 0.3420 0.0364  0.0187  -0.0197 27  PRO C CB  
9882  C CG  . PRO C 35  ? 0.2277 0.3554 0.2676 0.0348  0.0170  -0.0097 27  PRO C CG  
9883  C CD  . PRO C 35  ? 0.2778 0.3969 0.3251 0.0325  0.0121  0.0033  27  PRO C CD  
9884  N N   . MET C 36  ? 0.2556 0.3352 0.3123 0.0476  0.0052  -0.0250 28  MET C N   
9885  C CA  . MET C 36  ? 0.2481 0.3153 0.3068 0.0594  -0.0002 -0.0372 28  MET C CA  
9886  C C   . MET C 36  ? 0.2923 0.3373 0.3492 0.0599  -0.0090 -0.0423 28  MET C C   
9887  O O   . MET C 36  ? 0.3270 0.3673 0.3739 0.0691  -0.0081 -0.0566 28  MET C O   
9888  C CB  . MET C 36  ? 0.2905 0.3522 0.3627 0.0665  -0.0105 -0.0347 28  MET C CB  
9889  C CG  . MET C 36  ? 0.2840 0.3662 0.3590 0.0686  -0.0036 -0.0326 28  MET C CG  
9890  S SD  . MET C 36  ? 0.3658 0.4413 0.4584 0.0752  -0.0175 -0.0274 28  MET C SD  
9891  C CE  . MET C 36  ? 0.3792 0.4395 0.4769 0.0941  -0.0264 -0.0474 28  MET C CE  
9892  N N   . GLY C 37  ? 0.2616 0.2955 0.3290 0.0503  -0.0180 -0.0292 29  GLY C N   
9893  C CA  . GLY C 37  ? 0.2449 0.2553 0.3167 0.0496  -0.0304 -0.0321 29  GLY C CA  
9894  C C   . GLY C 37  ? 0.2846 0.2972 0.3418 0.0460  -0.0216 -0.0393 29  GLY C C   
9895  O O   . GLY C 37  ? 0.3228 0.3162 0.3754 0.0515  -0.0307 -0.0505 29  GLY C O   
9896  N N   . MET C 38  ? 0.2149 0.2489 0.2644 0.0380  -0.0067 -0.0343 30  MET C N   
9897  C CA  . MET C 38  ? 0.2061 0.2418 0.2458 0.0326  -0.0006 -0.0387 30  MET C CA  
9898  C C   . MET C 38  ? 0.2326 0.2775 0.2569 0.0388  0.0083  -0.0508 30  MET C C   
9899  O O   . MET C 38  ? 0.2159 0.2638 0.2329 0.0334  0.0127  -0.0528 30  MET C O   
9900  C CB  . MET C 38  ? 0.1891 0.2426 0.2319 0.0222  0.0069  -0.0276 30  MET C CB  
9901  C CG  . MET C 38  ? 0.1929 0.2448 0.2517 0.0147  0.0007  -0.0116 30  MET C CG  
9902  S SD  . MET C 38  ? 0.2418 0.3225 0.3001 0.0080  0.0116  -0.0022 30  MET C SD  
9903  C CE  . MET C 38  ? 0.3148 0.4180 0.3656 0.0132  0.0179  0.0010  30  MET C CE  
9904  N N   . ALA C 39  ? 0.2101 0.2614 0.2316 0.0500  0.0103  -0.0571 31  ALA C N   
9905  C CA  . ALA C 39  ? 0.2064 0.2767 0.2182 0.0548  0.0210  -0.0621 31  ALA C CA  
9906  C C   . ALA C 39  ? 0.2176 0.2813 0.2139 0.0583  0.0206  -0.0702 31  ALA C C   
9907  O O   . ALA C 39  ? 0.2272 0.3054 0.2180 0.0530  0.0284  -0.0670 31  ALA C O   
9908  C CB  . ALA C 39  ? 0.2152 0.2972 0.2298 0.0685  0.0234  -0.0666 31  ALA C CB  
9909  N N   . GLU C 40  ? 0.2396 0.2808 0.2298 0.0678  0.0090  -0.0805 32  GLU C N   
9910  C CA  . GLU C 40  ? 0.2550 0.2889 0.2267 0.0733  0.0066  -0.0898 32  GLU C CA  
9911  C C   . GLU C 40  ? 0.2639 0.2874 0.2376 0.0573  0.0043  -0.0833 32  GLU C C   
9912  O O   . GLU C 40  ? 0.2466 0.2736 0.2066 0.0561  0.0071  -0.0852 32  GLU C O   
9913  C CB  . GLU C 40  ? 0.3006 0.3093 0.2650 0.0904  -0.0102 -0.1059 32  GLU C CB  
9914  C CG  . GLU C 40  ? 0.3258 0.3490 0.2791 0.1133  -0.0075 -0.1191 32  GLU C CG  
9915  C CD  . GLU C 40  ? 0.3851 0.4140 0.3576 0.1152  -0.0075 -0.1152 32  GLU C CD  
9916  O OE1 . GLU C 40  ? 0.3464 0.3605 0.3386 0.1013  -0.0150 -0.1042 32  GLU C OE1 
9917  O OE2 . GLU C 40  ? 0.3813 0.4324 0.3499 0.1308  0.0002  -0.1216 32  GLU C OE2 
9918  N N   . MET C 41  ? 0.2319 0.2453 0.2231 0.0458  -0.0010 -0.0745 33  MET C N   
9919  C CA  . MET C 41  ? 0.2833 0.2939 0.2794 0.0319  -0.0010 -0.0681 33  MET C CA  
9920  C C   . MET C 41  ? 0.2000 0.2333 0.1935 0.0247  0.0109  -0.0637 33  MET C C   
9921  O O   . MET C 41  ? 0.2151 0.2470 0.2040 0.0186  0.0105  -0.0641 33  MET C O   
9922  C CB  . MET C 41  ? 0.2753 0.2814 0.2920 0.0231  -0.0060 -0.0568 33  MET C CB  
9923  C CG  . MET C 41  ? 0.2374 0.2184 0.2653 0.0268  -0.0231 -0.0569 33  MET C CG  
9924  S SD  . MET C 41  ? 0.2322 0.2194 0.2876 0.0183  -0.0268 -0.0363 33  MET C SD  
9925  C CE  . MET C 41  ? 0.2280 0.2353 0.2910 0.0048  -0.0165 -0.0244 33  MET C CE  
9926  N N   . ALA C 42  ? 0.1890 0.2414 0.1879 0.0253  0.0186  -0.0592 34  ALA C N   
9927  C CA  . ALA C 42  ? 0.1741 0.2452 0.1764 0.0185  0.0246  -0.0546 34  ALA C CA  
9928  C C   . ALA C 42  ? 0.1808 0.2621 0.1736 0.0207  0.0285  -0.0546 34  ALA C C   
9929  O O   . ALA C 42  ? 0.1869 0.2729 0.1819 0.0121  0.0273  -0.0504 34  ALA C O   
9930  C CB  . ALA C 42  ? 0.1646 0.2516 0.1767 0.0196  0.0283  -0.0501 34  ALA C CB  
9931  N N   . GLU C 43  ? 0.1953 0.2831 0.1784 0.0332  0.0326  -0.0582 35  GLU C N   
9932  C CA  . GLU C 43  ? 0.2055 0.3116 0.1776 0.0378  0.0387  -0.0553 35  GLU C CA  
9933  C C   . GLU C 43  ? 0.2147 0.3072 0.1734 0.0337  0.0332  -0.0576 35  GLU C C   
9934  O O   . GLU C 43  ? 0.2853 0.3911 0.2446 0.0257  0.0350  -0.0479 35  GLU C O   
9935  C CB  . GLU C 43  ? 0.2256 0.3417 0.1853 0.0571  0.0435  -0.0630 35  GLU C CB  
9936  C CG  . GLU C 43  ? 0.2780 0.4233 0.2246 0.0645  0.0529  -0.0574 35  GLU C CG  
9937  C CD  . GLU C 43  ? 0.3651 0.5169 0.2904 0.0891  0.0552  -0.0714 35  GLU C CD  
9938  O OE1 . GLU C 43  ? 0.3584 0.4931 0.2853 0.1001  0.0484  -0.0848 35  GLU C OE1 
9939  O OE2 . GLU C 43  ? 0.3983 0.5731 0.3056 0.0982  0.0620  -0.0686 35  GLU C OE2 
9940  N N   . THR C 44  ? 0.2782 0.3430 0.2282 0.0380  0.0238  -0.0686 36  THR C N   
9941  C CA  . THR C 44  ? 0.2458 0.2952 0.1825 0.0357  0.0163  -0.0722 36  THR C CA  
9942  C C   . THR C 44  ? 0.2202 0.2670 0.1709 0.0178  0.0134  -0.0638 36  THR C C   
9943  O O   . THR C 44  ? 0.2239 0.2763 0.1686 0.0123  0.0124  -0.0584 36  THR C O   
9944  C CB  . THR C 44  ? 0.2954 0.3132 0.2267 0.0434  0.0027  -0.0850 36  THR C CB  
9945  O OG1 . THR C 44  ? 0.3057 0.3242 0.2253 0.0627  0.0016  -0.0959 36  THR C OG1 
9946  C CG2 . THR C 44  ? 0.2738 0.2748 0.1898 0.0429  -0.0070 -0.0899 36  THR C CG2 
9947  N N   . LEU C 45  ? 0.2022 0.2428 0.1718 0.0099  0.0112  -0.0625 37  LEU C N   
9948  C CA  . LEU C 45  ? 0.1876 0.2269 0.1705 -0.0030 0.0070  -0.0585 37  LEU C CA  
9949  C C   . LEU C 45  ? 0.2451 0.3047 0.2352 -0.0095 0.0095  -0.0497 37  LEU C C   
9950  O O   . LEU C 45  ? 0.1867 0.2449 0.1793 -0.0175 0.0033  -0.0457 37  LEU C O   
9951  C CB  . LEU C 45  ? 0.1737 0.2112 0.1728 -0.0061 0.0062  -0.0588 37  LEU C CB  
9952  C CG  . LEU C 45  ? 0.1808 0.2216 0.1934 -0.0148 0.0017  -0.0582 37  LEU C CG  
9953  C CD1 . LEU C 45  ? 0.1681 0.1917 0.1795 -0.0198 -0.0068 -0.0608 37  LEU C CD1 
9954  C CD2 . LEU C 45  ? 0.2010 0.2499 0.2255 -0.0135 0.0038  -0.0581 37  LEU C CD2 
9955  N N   . TRP C 46  ? 0.2068 0.2847 0.2038 -0.0067 0.0159  -0.0451 38  TRP C N   
9956  C CA  . TRP C 46  ? 0.2277 0.3230 0.2407 -0.0145 0.0136  -0.0350 38  TRP C CA  
9957  C C   . TRP C 46  ? 0.2450 0.3570 0.2530 -0.0162 0.0165  -0.0224 38  TRP C C   
9958  O O   . TRP C 46  ? 0.2023 0.3211 0.2253 -0.0272 0.0086  -0.0115 38  TRP C O   
9959  C CB  . TRP C 46  ? 0.1550 0.2637 0.1805 -0.0114 0.0168  -0.0334 38  TRP C CB  
9960  C CG  . TRP C 46  ? 0.1779 0.2780 0.2122 -0.0125 0.0106  -0.0413 38  TRP C CG  
9961  C CD1 . TRP C 46  ? 0.1684 0.2563 0.1961 -0.0091 0.0117  -0.0489 38  TRP C CD1 
9962  C CD2 . TRP C 46  ? 0.1376 0.2440 0.1892 -0.0157 0.0010  -0.0417 38  TRP C CD2 
9963  N NE1 . TRP C 46  ? 0.1370 0.2286 0.1736 -0.0088 0.0069  -0.0532 38  TRP C NE1 
9964  C CE2 . TRP C 46  ? 0.1342 0.2349 0.1835 -0.0113 -0.0008 -0.0516 38  TRP C CE2 
9965  C CE3 . TRP C 46  ? 0.2114 0.3286 0.2824 -0.0211 -0.0083 -0.0338 38  TRP C CE3 
9966  C CZ2 . TRP C 46  ? 0.1322 0.2378 0.1917 -0.0087 -0.0111 -0.0582 38  TRP C CZ2 
9967  C CZ3 . TRP C 46  ? 0.2563 0.3725 0.3418 -0.0202 -0.0223 -0.0407 38  TRP C CZ3 
9968  C CH2 . TRP C 46  ? 0.2017 0.3120 0.2782 -0.0124 -0.0232 -0.0548 38  TRP C CH2 
9969  N N   . THR C 47  ? 0.1911 0.3119 0.1791 -0.0047 0.0263  -0.0231 39  THR C N   
9970  C CA  . THR C 47  ? 0.2050 0.3505 0.1860 -0.0043 0.0313  -0.0086 39  THR C CA  
9971  C C   . THR C 47  ? 0.2208 0.3537 0.1827 -0.0061 0.0256  -0.0097 39  THR C C   
9972  O O   . THR C 47  ? 0.2304 0.3836 0.1916 -0.0114 0.0261  0.0072  39  THR C O   
9973  C CB  . THR C 47  ? 0.2674 0.4376 0.2336 0.0130  0.0454  -0.0087 39  THR C CB  
9974  O OG1 . THR C 47  ? 0.2379 0.3882 0.1762 0.0285  0.0450  -0.0278 39  THR C OG1 
9975  C CG2 . THR C 47  ? 0.2328 0.4150 0.2182 0.0156  0.0504  -0.0078 39  THR C CG2 
9976  N N   . LYS C 48  ? 0.2254 0.3270 0.1741 -0.0023 0.0190  -0.0266 40  LYS C N   
9977  C CA  . LYS C 48  ? 0.2444 0.3317 0.1729 -0.0017 0.0118  -0.0295 40  LYS C CA  
9978  C C   . LYS C 48  ? 0.2336 0.2975 0.1768 -0.0166 -0.0019 -0.0304 40  LYS C C   
9979  O O   . LYS C 48  ? 0.2477 0.3039 0.1799 -0.0202 -0.0095 -0.0274 40  LYS C O   
9980  C CB  . LYS C 48  ? 0.2653 0.3326 0.1685 0.0154  0.0098  -0.0483 40  LYS C CB  
9981  C CG  . LYS C 48  ? 0.2828 0.3703 0.1680 0.0357  0.0206  -0.0535 40  LYS C CG  
9982  C CD  . LYS C 48  ? 0.4189 0.5422 0.2845 0.0432  0.0302  -0.0411 40  LYS C CD  
9983  C CE  . LYS C 48  ? 0.4617 0.6093 0.3097 0.0673  0.0415  -0.0490 40  LYS C CE  
9984  N NZ  . LYS C 48  ? 0.4992 0.6957 0.3341 0.0743  0.0555  -0.0311 40  LYS C NZ  
9985  N N   . PHE C 49  ? 0.2456 0.2260 0.1158 0.0446  0.0111  -0.0599 41  PHE C N   
9986  C CA  . PHE C 49  ? 0.2484 0.2245 0.1298 0.0293  0.0070  -0.0528 41  PHE C CA  
9987  C C   . PHE C 49  ? 0.2950 0.2910 0.2009 0.0184  0.0170  -0.0454 41  PHE C C   
9988  O O   . PHE C 49  ? 0.2574 0.2582 0.1695 0.0107  0.0203  -0.0393 41  PHE C O   
9989  C CB  . PHE C 49  ? 0.2719 0.2244 0.1520 0.0238  -0.0099 -0.0527 41  PHE C CB  
9990  C CG  . PHE C 49  ? 0.2852 0.2094 0.1389 0.0312  -0.0253 -0.0591 41  PHE C CG  
9991  C CD1 . PHE C 49  ? 0.3292 0.2420 0.1737 0.0264  -0.0331 -0.0559 41  PHE C CD1 
9992  C CD2 . PHE C 49  ? 0.3000 0.2063 0.1359 0.0438  -0.0337 -0.0684 41  PHE C CD2 
9993  C CE1 . PHE C 49  ? 0.3241 0.2060 0.1406 0.0330  -0.0504 -0.0623 41  PHE C CE1 
9994  C CE2 . PHE C 49  ? 0.3391 0.2129 0.1456 0.0520  -0.0506 -0.0754 41  PHE C CE2 
9995  C CZ  . PHE C 49  ? 0.3517 0.2125 0.1481 0.0461  -0.0595 -0.0724 41  PHE C CZ  
9996  N N   . LEU C 50  ? 0.2004 0.2055 0.1180 0.0183  0.0205  -0.0460 42  LEU C N   
9997  C CA  . LEU C 50  ? 0.1808 0.1960 0.1166 0.0084  0.0254  -0.0401 42  LEU C CA  
9998  C C   . LEU C 50  ? 0.1951 0.2252 0.1366 0.0047  0.0349  -0.0355 42  LEU C C   
9999  O O   . LEU C 50  ? 0.2371 0.2815 0.1785 0.0093  0.0412  -0.0352 42  LEU C O   
10000 C CB  . LEU C 50  ? 0.1645 0.1847 0.1085 0.0099  0.0258  -0.0422 42  LEU C CB  
10001 C CG  . LEU C 50  ? 0.2246 0.2486 0.1816 0.0018  0.0277  -0.0378 42  LEU C CG  
10002 C CD1 . LEU C 50  ? 0.2119 0.2249 0.1704 -0.0020 0.0209  -0.0342 42  LEU C CD1 
10003 C CD2 . LEU C 50  ? 0.2105 0.2426 0.1740 0.0040  0.0290  -0.0401 42  LEU C CD2 
10004 N N   . ASN C 51  ? 0.1867 0.2144 0.1337 -0.0032 0.0356  -0.0303 43  ASN C N   
10005 C CA  . ASN C 51  ? 0.1789 0.2156 0.1308 -0.0081 0.0418  -0.0251 43  ASN C CA  
10006 C C   . ASN C 51  ? 0.1938 0.2326 0.1559 -0.0131 0.0429  -0.0235 43  ASN C C   
10007 O O   . ASN C 51  ? 0.1861 0.2159 0.1495 -0.0151 0.0407  -0.0227 43  ASN C O   
10008 C CB  . ASN C 51  ? 0.2212 0.2509 0.1699 -0.0117 0.0408  -0.0208 43  ASN C CB  
10009 C CG  . ASN C 51  ? 0.2394 0.2660 0.1753 -0.0074 0.0386  -0.0220 43  ASN C CG  
10010 O OD1 . ASN C 51  ? 0.3105 0.3257 0.2413 -0.0080 0.0318  -0.0215 43  ASN C OD1 
10011 N ND2 . ASN C 51  ? 0.2361 0.2735 0.1665 -0.0025 0.0438  -0.0225 43  ASN C ND2 
10012 N N   . HIS C 52  ? 0.2163 0.2673 0.1848 -0.0145 0.0457  -0.0219 44  HIS C N   
10013 C CA  . HIS C 52  ? 0.1515 0.2011 0.1273 -0.0199 0.0435  -0.0207 44  HIS C CA  
10014 C C   . HIS C 52  ? 0.2170 0.2809 0.2016 -0.0255 0.0449  -0.0139 44  HIS C C   
10015 O O   . HIS C 52  ? 0.2179 0.2986 0.2047 -0.0226 0.0497  -0.0102 44  HIS C O   
10016 C CB  . HIS C 52  ? 0.1547 0.2038 0.1324 -0.0162 0.0409  -0.0256 44  HIS C CB  
10017 C CG  . HIS C 52  ? 0.1608 0.2250 0.1421 -0.0106 0.0429  -0.0267 44  HIS C CG  
10018 N ND1 . HIS C 52  ? 0.1986 0.2734 0.1892 -0.0116 0.0418  -0.0254 44  HIS C ND1 
10019 C CD2 . HIS C 52  ? 0.2323 0.3020 0.2071 -0.0020 0.0455  -0.0289 44  HIS C CD2 
10020 C CE1 . HIS C 52  ? 0.2486 0.3377 0.2404 -0.0031 0.0451  -0.0259 44  HIS C CE1 
10021 N NE2 . HIS C 52  ? 0.2589 0.3437 0.2391 0.0038  0.0475  -0.0288 44  HIS C NE2 
10022 N N   . ASN C 53  ? 0.2042 0.2614 0.1931 -0.0331 0.0399  -0.0112 45  ASN C N   
10023 C CA  . ASN C 53  ? 0.2098 0.2796 0.2102 -0.0418 0.0375  -0.0019 45  ASN C CA  
10024 C C   . ASN C 53  ? 0.1642 0.2345 0.1717 -0.0454 0.0308  -0.0021 45  ASN C C   
10025 O O   . ASN C 53  ? 0.1731 0.2221 0.1737 -0.0490 0.0230  -0.0054 45  ASN C O   
10026 C CB  . ASN C 53  ? 0.1701 0.2266 0.1681 -0.0503 0.0329  0.0036  45  ASN C CB  
10027 C CG  . ASN C 53  ? 0.2401 0.3109 0.2524 -0.0616 0.0285  0.0167  45  ASN C CG  
10028 O OD1 . ASN C 53  ? 0.1926 0.2889 0.2184 -0.0620 0.0312  0.0231  45  ASN C OD1 
10029 N ND2 . ASN C 53  ? 0.1860 0.2413 0.1961 -0.0706 0.0212  0.0224  45  ASN C ND2 
10030 N N   . PRO C 54  ? 0.1789 0.2724 0.1982 -0.0433 0.0334  0.0015  46  PRO C N   
10031 C CA  . PRO C 54  ? 0.2110 0.3070 0.2391 -0.0479 0.0258  0.0031  46  PRO C CA  
10032 C C   . PRO C 54  ? 0.2649 0.3506 0.2977 -0.0621 0.0139  0.0108  46  PRO C C   
10033 O O   . PRO C 54  ? 0.2379 0.3098 0.2684 -0.0661 0.0039  0.0082  46  PRO C O   
10034 C CB  . PRO C 54  ? 0.2696 0.3990 0.3128 -0.0427 0.0322  0.0099  46  PRO C CB  
10035 C CG  . PRO C 54  ? 0.2890 0.4241 0.3227 -0.0304 0.0427  0.0053  46  PRO C CG  
10036 C CD  . PRO C 54  ? 0.1870 0.3055 0.2105 -0.0347 0.0430  0.0047  46  PRO C CD  
10037 N N   . ALA C 55  ? 0.2274 0.3168 0.2649 -0.0699 0.0132  0.0205  47  ALA C N   
10038 C CA  . ALA C 55  ? 0.1917 0.2663 0.2322 -0.0847 -0.0013 0.0287  47  ALA C CA  
10039 C C   . ALA C 55  ? 0.2540 0.2869 0.2714 -0.0836 -0.0100 0.0176  47  ALA C C   
10040 O O   . ALA C 55  ? 0.2377 0.2489 0.2510 -0.0933 -0.0258 0.0202  47  ALA C O   
10041 C CB  . ALA C 55  ? 0.2584 0.3476 0.3097 -0.0931 0.0000  0.0433  47  ALA C CB  
10042 N N   . ASN C 56  ? 0.2510 0.2718 0.2526 -0.0715 -0.0012 0.0063  48  ASN C N   
10043 C CA  . ASN C 56  ? 0.2759 0.2620 0.2550 -0.0663 -0.0066 -0.0030 48  ASN C CA  
10044 C C   . ASN C 56  ? 0.2552 0.2411 0.2251 -0.0526 0.0028  -0.0133 48  ASN C C   
10045 O O   . ASN C 56  ? 0.2165 0.2048 0.1825 -0.0455 0.0119  -0.0155 48  ASN C O   
10046 C CB  . ASN C 56  ? 0.3030 0.2745 0.2740 -0.0674 -0.0068 -0.0005 48  ASN C CB  
10047 C CG  . ASN C 56  ? 0.3437 0.2805 0.2899 -0.0583 -0.0113 -0.0096 48  ASN C CG  
10048 O OD1 . ASN C 56  ? 0.2686 0.1902 0.2021 -0.0526 -0.0161 -0.0168 48  ASN C OD1 
10049 N ND2 . ASN C 56  ? 0.2821 0.2074 0.2202 -0.0553 -0.0092 -0.0086 48  ASN C ND2 
10050 N N   . PRO C 57  ? 0.2689 0.2523 0.2361 -0.0497 -0.0006 -0.0182 49  PRO C N   
10051 C CA  . PRO C 57  ? 0.2289 0.2128 0.1888 -0.0379 0.0070  -0.0254 49  PRO C CA  
10052 C C   . PRO C 57  ? 0.2210 0.1849 0.1623 -0.0287 0.0092  -0.0296 49  PRO C C   
10053 O O   . PRO C 57  ? 0.2460 0.2151 0.1850 -0.0200 0.0163  -0.0318 49  PRO C O   
10054 C CB  . PRO C 57  ? 0.2886 0.2708 0.2480 -0.0382 0.0003  -0.0282 49  PRO C CB  
10055 C CG  . PRO C 57  ? 0.2883 0.2802 0.2623 -0.0506 -0.0082 -0.0209 49  PRO C CG  
10056 C CD  . PRO C 57  ? 0.2747 0.2582 0.2484 -0.0582 -0.0120 -0.0151 49  PRO C CD  
10057 N N   . LYS C 58  ? 0.2599 0.2017 0.1886 -0.0297 0.0026  -0.0294 50  LYS C N   
10058 C CA  . LYS C 58  ? 0.3119 0.2361 0.2221 -0.0180 0.0057  -0.0324 50  LYS C CA  
10059 C C   . LYS C 58  ? 0.2258 0.1530 0.1398 -0.0186 0.0110  -0.0279 50  LYS C C   
10060 O O   . LYS C 58  ? 0.3070 0.2186 0.2063 -0.0092 0.0122  -0.0289 50  LYS C O   
10061 C CB  . LYS C 58  ? 0.3333 0.2242 0.2195 -0.0140 -0.0063 -0.0371 50  LYS C CB  
10062 C CG  . LYS C 58  ? 0.3824 0.2668 0.2594 -0.0108 -0.0120 -0.0421 50  LYS C CG  
10063 C CD  . LYS C 58  ? 0.3709 0.2683 0.2447 0.0026  -0.0002 -0.0437 50  LYS C CD  
10064 C CE  . LYS C 58  ? 0.5050 0.3930 0.3653 0.0076  -0.0061 -0.0485 50  LYS C CE  
10065 N NZ  . LYS C 58  ? 0.5017 0.4080 0.3643 0.0180  0.0052  -0.0468 50  LYS C NZ  
10066 N N   . PHE C 59  ? 0.2086 0.1558 0.1404 -0.0276 0.0145  -0.0228 51  PHE C N   
10067 C CA  . PHE C 59  ? 0.2269 0.1795 0.1623 -0.0279 0.0200  -0.0183 51  PHE C CA  
10068 C C   . PHE C 59  ? 0.2279 0.1806 0.1570 -0.0161 0.0275  -0.0193 51  PHE C C   
10069 O O   . PHE C 59  ? 0.2060 0.1716 0.1400 -0.0119 0.0325  -0.0202 51  PHE C O   
10070 C CB  . PHE C 59  ? 0.1970 0.1751 0.1494 -0.0348 0.0250  -0.0141 51  PHE C CB  
10071 C CG  . PHE C 59  ? 0.2606 0.2453 0.2151 -0.0344 0.0306  -0.0100 51  PHE C CG  
10072 C CD1 . PHE C 59  ? 0.2516 0.2219 0.1994 -0.0354 0.0280  -0.0066 51  PHE C CD1 
10073 C CD2 . PHE C 59  ? 0.2393 0.2418 0.2001 -0.0324 0.0369  -0.0098 51  PHE C CD2 
10074 C CE1 . PHE C 59  ? 0.2270 0.2036 0.1766 -0.0352 0.0325  -0.0023 51  PHE C CE1 
10075 C CE2 . PHE C 59  ? 0.2366 0.2430 0.1968 -0.0320 0.0403  -0.0063 51  PHE C CE2 
10076 C CZ  . PHE C 59  ? 0.2183 0.2134 0.1741 -0.0338 0.0386  -0.0021 51  PHE C CZ  
10077 N N   . TYR C 60  ? 0.2620 0.2005 0.1809 -0.0107 0.0274  -0.0176 52  TYR C N   
10078 C CA  . TYR C 60  ? 0.2685 0.2078 0.1811 0.0025  0.0340  -0.0163 52  TYR C CA  
10079 C C   . TYR C 60  ? 0.2562 0.2190 0.1839 0.0012  0.0408  -0.0115 52  TYR C C   
10080 O O   . TYR C 60  ? 0.2378 0.2095 0.1671 0.0087  0.0450  -0.0088 52  TYR C O   
10081 C CB  . TYR C 60  ? 0.2309 0.1534 0.1318 0.0092  0.0330  -0.0141 52  TYR C CB  
10082 C CG  . TYR C 60  ? 0.2839 0.1748 0.1633 0.0139  0.0237  -0.0193 52  TYR C CG  
10083 C CD1 . TYR C 60  ? 0.3017 0.1800 0.1682 0.0183  0.0188  -0.0258 52  TYR C CD1 
10084 C CD2 . TYR C 60  ? 0.3350 0.2054 0.2049 0.0141  0.0180  -0.0179 52  TYR C CD2 
10085 C CE1 . TYR C 60  ? 0.3123 0.1558 0.1548 0.0229  0.0070  -0.0314 52  TYR C CE1 
10086 C CE2 . TYR C 60  ? 0.3822 0.2177 0.2295 0.0184  0.0063  -0.0231 52  TYR C CE2 
10087 C CZ  . TYR C 60  ? 0.3876 0.2084 0.2202 0.0229  0.0002  -0.0302 52  TYR C CZ  
10088 O OH  . TYR C 60  ? 0.3814 0.1618 0.1873 0.0275  -0.0145 -0.0361 52  TYR C OH  
10089 N N   . ASN C 61  ? 0.2806 0.2528 0.2182 -0.0079 0.0409  -0.0092 53  ASN C N   
10090 C CA  . ASN C 61  ? 0.2188 0.2066 0.1658 -0.0089 0.0441  -0.0052 53  ASN C CA  
10091 C C   . ASN C 61  ? 0.2173 0.2162 0.1713 -0.0136 0.0433  -0.0085 53  ASN C C   
10092 O O   . ASN C 61  ? 0.2208 0.2274 0.1787 -0.0156 0.0431  -0.0069 53  ASN C O   
10093 C CB  . ASN C 61  ? 0.2129 0.2015 0.1613 -0.0127 0.0444  -0.0007 53  ASN C CB  
10094 C CG  . ASN C 61  ? 0.1772 0.1758 0.1314 -0.0113 0.0454  0.0049  53  ASN C CG  
10095 O OD1 . ASN C 61  ? 0.1764 0.1791 0.1334 -0.0053 0.0466  0.0093  53  ASN C OD1 
10096 N ND2 . ASN C 61  ? 0.2031 0.2065 0.1589 -0.0168 0.0441  0.0059  53  ASN C ND2 
10097 N N   . ARG C 62  ? 0.1737 0.1717 0.1274 -0.0143 0.0416  -0.0133 54  ARG C N   
10098 C CA  . ARG C 62  ? 0.1586 0.1667 0.1181 -0.0161 0.0409  -0.0164 54  ARG C CA  
10099 C C   . ARG C 62  ? 0.1396 0.1514 0.1018 -0.0125 0.0402  -0.0146 54  ARG C C   
10100 O O   . ARG C 62  ? 0.1969 0.2074 0.1585 -0.0081 0.0412  -0.0104 54  ARG C O   
10101 C CB  . ARG C 62  ? 0.2105 0.2175 0.1704 -0.0172 0.0386  -0.0205 54  ARG C CB  
10102 C CG  . ARG C 62  ? 0.1517 0.1507 0.1056 -0.0114 0.0377  -0.0217 54  ARG C CG  
10103 C CD  . ARG C 62  ? 0.1925 0.1869 0.1441 -0.0130 0.0334  -0.0258 54  ARG C CD  
10104 N NE  . ARG C 62  ? 0.1991 0.1869 0.1423 -0.0056 0.0331  -0.0270 54  ARG C NE  
10105 C CZ  . ARG C 62  ? 0.2327 0.2063 0.1617 0.0014  0.0329  -0.0271 54  ARG C CZ  
10106 N NH1 . ARG C 62  ? 0.2223 0.1840 0.1447 0.0008  0.0316  -0.0267 54  ARG C NH1 
10107 N NH2 . ARG C 62  ? 0.2301 0.2007 0.1499 0.0104  0.0339  -0.0274 54  ARG C NH2 
10108 N N   . ASP C 63  ? 0.1536 0.1699 0.1178 -0.0136 0.0378  -0.0164 55  ASP C N   
10109 C CA  . ASP C 63  ? 0.1350 0.1517 0.1021 -0.0121 0.0334  -0.0147 55  ASP C CA  
10110 C C   . ASP C 63  ? 0.1778 0.1952 0.1466 -0.0099 0.0336  -0.0165 55  ASP C C   
10111 O O   . ASP C 63  ? 0.1947 0.2120 0.1620 -0.0101 0.0350  -0.0215 55  ASP C O   
10112 C CB  . ASP C 63  ? 0.1664 0.1812 0.1305 -0.0120 0.0282  -0.0188 55  ASP C CB  
10113 C CG  . ASP C 63  ? 0.2012 0.2128 0.1600 -0.0131 0.0259  -0.0172 55  ASP C CG  
10114 O OD1 . ASP C 63  ? 0.1848 0.1964 0.1464 -0.0155 0.0259  -0.0103 55  ASP C OD1 
10115 O OD2 . ASP C 63  ? 0.1964 0.2056 0.1468 -0.0102 0.0241  -0.0226 55  ASP C OD2 
10116 N N   . ARG C 64  ? 0.1665 0.1858 0.1391 -0.0083 0.0315  -0.0106 56  ARG C N   
10117 C CA  . ARG C 64  ? 0.1742 0.1950 0.1472 -0.0055 0.0315  -0.0107 56  ARG C CA  
10118 C C   . ARG C 64  ? 0.1589 0.1792 0.1359 -0.0073 0.0245  -0.0118 56  ARG C C   
10119 O O   . ARG C 64  ? 0.2196 0.2387 0.2005 -0.0100 0.0183  -0.0063 56  ARG C O   
10120 C CB  . ARG C 64  ? 0.1463 0.1726 0.1205 -0.0007 0.0348  -0.0010 56  ARG C CB  
10121 C CG  . ARG C 64  ? 0.2329 0.2544 0.1964 0.0061  0.0409  -0.0030 56  ARG C CG  
10122 C CD  . ARG C 64  ? 0.2343 0.2488 0.1931 0.0049  0.0428  -0.0060 56  ARG C CD  
10123 N NE  . ARG C 64  ? 0.2018 0.2070 0.1476 0.0131  0.0462  -0.0070 56  ARG C NE  
10124 C CZ  . ARG C 64  ? 0.2283 0.2240 0.1675 0.0140  0.0470  -0.0083 56  ARG C CZ  
10125 N NH1 . ARG C 64  ? 0.2251 0.2227 0.1712 0.0064  0.0459  -0.0079 56  ARG C NH1 
10126 N NH2 . ARG C 64  ? 0.2467 0.2290 0.1701 0.0236  0.0481  -0.0100 56  ARG C NH2 
10127 N N   . PHE C 65  ? 0.1873 0.2067 0.1629 -0.0061 0.0237  -0.0184 57  PHE C N   
10128 C CA  . PHE C 65  ? 0.1716 0.1884 0.1493 -0.0060 0.0167  -0.0198 57  PHE C CA  
10129 C C   . PHE C 65  ? 0.2297 0.2496 0.2098 -0.0045 0.0162  -0.0160 57  PHE C C   
10130 O O   . PHE C 65  ? 0.1862 0.2078 0.1626 -0.0023 0.0208  -0.0187 57  PHE C O   
10131 C CB  . PHE C 65  ? 0.1943 0.2101 0.1691 -0.0036 0.0162  -0.0293 57  PHE C CB  
10132 C CG  . PHE C 65  ? 0.2073 0.2179 0.1819 -0.0008 0.0087  -0.0318 57  PHE C CG  
10133 C CD1 . PHE C 65  ? 0.2223 0.2215 0.1926 -0.0001 -0.0004 -0.0317 57  PHE C CD1 
10134 C CD2 . PHE C 65  ? 0.2299 0.2443 0.2073 0.0012  0.0087  -0.0341 57  PHE C CD2 
10135 C CE1 . PHE C 65  ? 0.1903 0.1800 0.1582 0.0032  -0.0094 -0.0343 57  PHE C CE1 
10136 C CE2 . PHE C 65  ? 0.2042 0.2127 0.1812 0.0045  0.0012  -0.0361 57  PHE C CE2 
10137 C CZ  . PHE C 65  ? 0.2497 0.2448 0.2214 0.0059  -0.0079 -0.0365 57  PHE C CZ  
10138 N N   . VAL C 66  ? 0.1399 0.1589 0.1250 -0.0061 0.0092  -0.0093 58  VAL C N   
10139 C CA  . VAL C 66  ? 0.1369 0.1607 0.1247 -0.0047 0.0084  -0.0035 58  VAL C CA  
10140 C C   . VAL C 66  ? 0.1425 0.1591 0.1328 -0.0062 -0.0018 -0.0049 58  VAL C C   
10141 O O   . VAL C 66  ? 0.1877 0.1966 0.1808 -0.0099 -0.0113 -0.0008 58  VAL C O   
10142 C CB  . VAL C 66  ? 0.1368 0.1712 0.1307 -0.0051 0.0103  0.0120  58  VAL C CB  
10143 C CG1 . VAL C 66  ? 0.1502 0.1914 0.1471 -0.0035 0.0088  0.0202  58  VAL C CG1 
10144 C CG2 . VAL C 66  ? 0.1571 0.1968 0.1451 0.0001  0.0209  0.0125  58  VAL C CG2 
10145 N N   . LEU C 67  ? 0.1666 0.1832 0.1548 -0.0032 -0.0015 -0.0105 59  LEU C N   
10146 C CA  . LEU C 67  ? 0.1615 0.1714 0.1515 -0.0029 -0.0109 -0.0111 59  LEU C CA  
10147 C C   . LEU C 67  ? 0.2046 0.2209 0.2000 -0.0050 -0.0131 0.0018  59  LEU C C   
10148 O O   . LEU C 67  ? 0.2018 0.2247 0.1948 -0.0019 -0.0086 0.0021  59  LEU C O   
10149 C CB  . LEU C 67  ? 0.1608 0.1711 0.1478 0.0018  -0.0090 -0.0219 59  LEU C CB  
10150 C CG  . LEU C 67  ? 0.2256 0.2290 0.2137 0.0044  -0.0181 -0.0236 59  LEU C CG  
10151 C CD1 . LEU C 67  ? 0.1846 0.1733 0.1682 0.0070  -0.0269 -0.0279 59  LEU C CD1 
10152 C CD2 . LEU C 67  ? 0.2811 0.2912 0.2695 0.0087  -0.0147 -0.0307 59  LEU C CD2 
10153 N N   . SER C 68  ? 0.1650 0.1804 0.1678 -0.0105 -0.0209 0.0143  60  SER C N   
10154 C CA  . SER C 68  ? 0.1865 0.2141 0.1972 -0.0127 -0.0217 0.0311  60  SER C CA  
10155 C C   . SER C 68  ? 0.2423 0.2654 0.2533 -0.0123 -0.0287 0.0311  60  SER C C   
10156 O O   . SER C 68  ? 0.2525 0.2876 0.2640 -0.0098 -0.0240 0.0390  60  SER C O   
10157 C CB  . SER C 68  ? 0.1616 0.1921 0.1844 -0.0210 -0.0305 0.0480  60  SER C CB  
10158 O OG  . SER C 68  ? 0.2001 0.2504 0.2334 -0.0225 -0.0283 0.0684  60  SER C OG  
10159 N N   . ASN C 69  ? 0.2332 0.2382 0.2416 -0.0128 -0.0397 0.0221  61  ASN C N   
10160 C CA  . ASN C 69  ? 0.2882 0.2868 0.2961 -0.0110 -0.0470 0.0206  61  ASN C CA  
10161 C C   . ASN C 69  ? 0.2920 0.2950 0.2928 -0.0035 -0.0376 0.0067  61  ASN C C   
10162 O O   . ASN C 69  ? 0.3112 0.3055 0.3079 0.0013  -0.0399 -0.0057 61  ASN C O   
10163 C CB  . ASN C 69  ? 0.3336 0.3086 0.3393 -0.0124 -0.0640 0.0171  61  ASN C CB  
10164 C CG  . ASN C 69  ? 0.3717 0.3334 0.3687 -0.0095 -0.0653 0.0052  61  ASN C CG  
10165 O OD1 . ASN C 69  ? 0.3669 0.3387 0.3622 -0.0082 -0.0535 0.0008  61  ASN C OD1 
10166 N ND2 . ASN C 69  ? 0.4454 0.3820 0.4343 -0.0074 -0.0808 -0.0001 61  ASN C ND2 
10167 N N   . GLY C 70  ? 0.2590 0.2761 0.2578 -0.0017 -0.0276 0.0103  62  GLY C N   
10168 C CA  . GLY C 70  ? 0.2472 0.2675 0.2388 0.0032  -0.0202 -0.0010 62  GLY C CA  
10169 C C   . GLY C 70  ? 0.3131 0.3297 0.3048 0.0060  -0.0258 -0.0073 62  GLY C C   
10170 O O   . GLY C 70  ? 0.3000 0.3190 0.2891 0.0085  -0.0224 -0.0164 62  GLY C O   
10171 N N   . HIS C 71  ? 0.3134 0.3245 0.3093 0.0049  -0.0355 -0.0011 63  HIS C N   
10172 C CA  . HIS C 71  ? 0.3278 0.3343 0.3246 0.0089  -0.0417 -0.0072 63  HIS C CA  
10173 C C   . HIS C 71  ? 0.3365 0.3374 0.3331 0.0141  -0.0423 -0.0195 63  HIS C C   
10174 O O   . HIS C 71  ? 0.3394 0.3436 0.3375 0.0194  -0.0430 -0.0256 63  HIS C O   
10175 C CB  . HIS C 71  ? 0.3390 0.3369 0.3397 0.0067  -0.0539 0.0023  63  HIS C CB  
10176 C CG  . HIS C 71  ? 0.3540 0.3387 0.3572 0.0025  -0.0630 0.0074  63  HIS C CG  
10177 N ND1 . HIS C 71  ? 0.3629 0.3530 0.3713 -0.0051 -0.0635 0.0219  63  HIS C ND1 
10178 C CD2 . HIS C 71  ? 0.3937 0.3590 0.3934 0.0054  -0.0732 0.0004  63  HIS C CD2 
10179 C CE1 . HIS C 71  ? 0.4082 0.3820 0.4181 -0.0092 -0.0754 0.0243  63  HIS C CE1 
10180 N NE2 . HIS C 71  ? 0.3918 0.3478 0.3940 -0.0022 -0.0818 0.0101  63  HIS C NE2 
10181 N N   . ALA C 72  ? 0.2621 0.2564 0.2567 0.0138  -0.0421 -0.0219 64  ALA C N   
10182 C CA  . ALA C 72  ? 0.2156 0.2062 0.2068 0.0211  -0.0409 -0.0327 64  ALA C CA  
10183 C C   . ALA C 72  ? 0.2175 0.2241 0.2105 0.0215  -0.0290 -0.0376 64  ALA C C   
10184 O O   . ALA C 72  ? 0.2218 0.2298 0.2124 0.0249  -0.0247 -0.0429 64  ALA C O   
10185 C CB  . ALA C 72  ? 0.1985 0.1735 0.1836 0.0206  -0.0467 -0.0331 64  ALA C CB  
10186 N N   . SER C 73  ? 0.2014 0.2186 0.1973 0.0179  -0.0250 -0.0353 65  SER C N   
10187 C CA  . SER C 73  ? 0.1715 0.1994 0.1682 0.0154  -0.0170 -0.0378 65  SER C CA  
10188 C C   . SER C 73  ? 0.2177 0.2558 0.2200 0.0202  -0.0140 -0.0430 65  SER C C   
10189 O O   . SER C 73  ? 0.1980 0.2430 0.2014 0.0177  -0.0078 -0.0439 65  SER C O   
10190 C CB  . SER C 73  ? 0.2373 0.2691 0.2327 0.0123  -0.0180 -0.0354 65  SER C CB  
10191 O OG  . SER C 73  ? 0.2352 0.2702 0.2359 0.0157  -0.0239 -0.0359 65  SER C OG  
10192 N N   . MET C 74  ? 0.2193 0.2603 0.2256 0.0279  -0.0178 -0.0449 66  MET C N   
10193 C CA  . MET C 74  ? 0.1743 0.2314 0.1874 0.0346  -0.0131 -0.0470 66  MET C CA  
10194 C C   . MET C 74  ? 0.2297 0.2845 0.2364 0.0399  -0.0080 -0.0504 66  MET C C   
10195 O O   . MET C 74  ? 0.1964 0.2684 0.2085 0.0430  -0.0010 -0.0497 66  MET C O   
10196 C CB  . MET C 74  ? 0.2157 0.2772 0.2332 0.0453  -0.0175 -0.0479 66  MET C CB  
10197 C CG  . MET C 74  ? 0.2044 0.2813 0.2341 0.0414  -0.0197 -0.0433 66  MET C CG  
10198 S SD  . MET C 74  ? 0.1875 0.2881 0.2301 0.0326  -0.0140 -0.0379 66  MET C SD  
10199 C CE  . MET C 74  ? 0.1547 0.2742 0.2022 0.0452  -0.0045 -0.0377 66  MET C CE  
10200 N N   . LEU C 75  ? 0.2444 0.2791 0.2399 0.0407  -0.0123 -0.0528 67  LEU C N   
10201 C CA  . LEU C 75  ? 0.2272 0.2569 0.2140 0.0444  -0.0090 -0.0561 67  LEU C CA  
10202 C C   . LEU C 75  ? 0.1847 0.2261 0.1759 0.0354  -0.0005 -0.0531 67  LEU C C   
10203 O O   . LEU C 75  ? 0.2149 0.2674 0.2060 0.0393  0.0063  -0.0538 67  LEU C O   
10204 C CB  . LEU C 75  ? 0.2705 0.2748 0.2460 0.0430  -0.0186 -0.0569 67  LEU C CB  
10205 C CG  . LEU C 75  ? 0.3137 0.3071 0.2774 0.0453  -0.0187 -0.0600 67  LEU C CG  
10206 C CD1 . LEU C 75  ? 0.3326 0.3144 0.2815 0.0616  -0.0230 -0.0679 67  LEU C CD1 
10207 C CD2 . LEU C 75  ? 0.3975 0.3734 0.3585 0.0351  -0.0275 -0.0549 67  LEU C CD2 
10208 N N   . LEU C 76  ? 0.2317 0.2705 0.2255 0.0245  -0.0008 -0.0491 68  LEU C N   
10209 C CA  . LEU C 76  ? 0.1526 0.1973 0.1478 0.0169  0.0055  -0.0468 68  LEU C CA  
10210 C C   . LEU C 76  ? 0.1787 0.2410 0.1836 0.0144  0.0089  -0.0447 68  LEU C C   
10211 O O   . LEU C 76  ? 0.1813 0.2519 0.1888 0.0114  0.0139  -0.0428 68  LEU C O   
10212 C CB  . LEU C 76  ? 0.1403 0.1762 0.1322 0.0098  0.0040  -0.0432 68  LEU C CB  
10213 C CG  . LEU C 76  ? 0.1971 0.2345 0.1871 0.0038  0.0091  -0.0416 68  LEU C CG  
10214 C CD1 . LEU C 76  ? 0.1999 0.2374 0.1880 0.0039  0.0134  -0.0421 68  LEU C CD1 
10215 C CD2 . LEU C 76  ? 0.2271 0.2565 0.2105 0.0015  0.0087  -0.0380 68  LEU C CD2 
10216 N N   . TYR C 77  ? 0.1680 0.2365 0.1796 0.0146  0.0050  -0.0435 69  TYR C N   
10217 C CA  . TYR C 77  ? 0.1485 0.2356 0.1725 0.0111  0.0055  -0.0390 69  TYR C CA  
10218 C C   . TYR C 77  ? 0.1382 0.2451 0.1699 0.0191  0.0118  -0.0369 69  TYR C C   
10219 O O   . TYR C 77  ? 0.1711 0.2949 0.2127 0.0141  0.0152  -0.0305 69  TYR C O   
10220 C CB  . TYR C 77  ? 0.1509 0.2411 0.1808 0.0107  -0.0013 -0.0375 69  TYR C CB  
10221 C CG  . TYR C 77  ? 0.1424 0.2155 0.1625 0.0043  -0.0070 -0.0385 69  TYR C CG  
10222 C CD1 . TYR C 77  ? 0.2616 0.3227 0.2717 -0.0018 -0.0059 -0.0389 69  TYR C CD1 
10223 C CD2 . TYR C 77  ? 0.1925 0.2618 0.2118 0.0064  -0.0131 -0.0385 69  TYR C CD2 
10224 C CE1 . TYR C 77  ? 0.2454 0.2917 0.2429 -0.0037 -0.0098 -0.0396 69  TYR C CE1 
10225 C CE2 . TYR C 77  ? 0.2172 0.2725 0.2247 0.0028  -0.0173 -0.0385 69  TYR C CE2 
10226 C CZ  . TYR C 77  ? 0.2715 0.3157 0.2673 -0.0012 -0.0151 -0.0392 69  TYR C CZ  
10227 O OH  . TYR C 77  ? 0.2427 0.2741 0.2236 -0.0010 -0.0180 -0.0390 69  TYR C OH  
10228 N N   . SER C 78  ? 0.1984 0.3032 0.2245 0.0324  0.0128  -0.0412 70  SER C N   
10229 C CA  . SER C 78  ? 0.1725 0.2953 0.2005 0.0446  0.0200  -0.0399 70  SER C CA  
10230 C C   . SER C 78  ? 0.2235 0.3469 0.2459 0.0419  0.0263  -0.0391 70  SER C C   
10231 O O   . SER C 78  ? 0.2064 0.3536 0.2377 0.0436  0.0334  -0.0321 70  SER C O   
10232 C CB  . SER C 78  ? 0.1725 0.2833 0.1878 0.0617  0.0177  -0.0472 70  SER C CB  
10233 O OG  . SER C 78  ? 0.2368 0.3515 0.2591 0.0663  0.0126  -0.0465 70  SER C OG  
10234 N N   . LEU C 79  ? 0.1849 0.2844 0.1940 0.0374  0.0237  -0.0444 71  LEU C N   
10235 C CA  . LEU C 79  ? 0.2040 0.3021 0.2069 0.0348  0.0288  -0.0437 71  LEU C CA  
10236 C C   . LEU C 79  ? 0.2233 0.3347 0.2383 0.0218  0.0317  -0.0358 71  LEU C C   
10237 O O   . LEU C 79  ? 0.2007 0.3264 0.2187 0.0218  0.0379  -0.0308 71  LEU C O   
10238 C CB  . LEU C 79  ? 0.2286 0.3003 0.2183 0.0311  0.0238  -0.0487 71  LEU C CB  
10239 C CG  . LEU C 79  ? 0.2506 0.3044 0.2253 0.0424  0.0182  -0.0554 71  LEU C CG  
10240 C CD1 . LEU C 79  ? 0.1910 0.2220 0.1601 0.0348  0.0098  -0.0559 71  LEU C CD1 
10241 C CD2 . LEU C 79  ? 0.2697 0.3255 0.2326 0.0520  0.0229  -0.0577 71  LEU C CD2 
10242 N N   . LEU C 80  ? 0.2010 0.3061 0.2214 0.0112  0.0260  -0.0343 72  LEU C N   
10243 C CA  . LEU C 80  ? 0.1864 0.2963 0.2144 -0.0014 0.0249  -0.0278 72  LEU C CA  
10244 C C   . LEU C 80  ? 0.1888 0.3274 0.2349 -0.0029 0.0264  -0.0176 72  LEU C C   
10245 O O   . LEU C 80  ? 0.1924 0.3426 0.2458 -0.0098 0.0286  -0.0095 72  LEU C O   
10246 C CB  . LEU C 80  ? 0.1943 0.2869 0.2182 -0.0091 0.0169  -0.0298 72  LEU C CB  
10247 C CG  . LEU C 80  ? 0.2146 0.2840 0.2233 -0.0086 0.0161  -0.0355 72  LEU C CG  
10248 C CD1 . LEU C 80  ? 0.1504 0.2070 0.1534 -0.0124 0.0093  -0.0365 72  LEU C CD1 
10249 C CD2 . LEU C 80  ? 0.2280 0.2906 0.2308 -0.0122 0.0198  -0.0345 72  LEU C CD2 
10250 N N   . HIS C 81  ? 0.1319 0.2842 0.1870 0.0031  0.0249  -0.0160 73  HIS C N   
10251 C CA  . HIS C 81  ? 0.1389 0.3247 0.2148 0.0030  0.0271  -0.0034 73  HIS C CA  
10252 C C   . HIS C 81  ? 0.1495 0.3571 0.2266 0.0132  0.0386  0.0016  73  HIS C C   
10253 O O   . HIS C 81  ? 0.1950 0.4273 0.2876 0.0067  0.0413  0.0152  73  HIS C O   
10254 C CB  . HIS C 81  ? 0.1696 0.3671 0.2538 0.0113  0.0246  -0.0030 73  HIS C CB  
10255 C CG  . HIS C 81  ? 0.1587 0.3964 0.2666 0.0139  0.0281  0.0121  73  HIS C CG  
10256 N ND1 . HIS C 81  ? 0.1702 0.4253 0.2986 -0.0025 0.0219  0.0269  73  HIS C ND1 
10257 C CD2 . HIS C 81  ? 0.1412 0.4063 0.2558 0.0317  0.0367  0.0165  73  HIS C CD2 
10258 C CE1 . HIS C 81  ? 0.1587 0.4546 0.3093 0.0035  0.0270  0.0418  73  HIS C CE1 
10259 N NE2 . HIS C 81  ? 0.1642 0.4679 0.3062 0.0258  0.0373  0.0355  73  HIS C NE2 
10260 N N   . LEU C 82  ? 0.2051 0.4030 0.2649 0.0293  0.0443  -0.0083 74  LEU C N   
10261 C CA  . LEU C 82  ? 0.2097 0.4274 0.2655 0.0438  0.0552  -0.0048 74  LEU C CA  
10262 C C   . LEU C 82  ? 0.1589 0.3756 0.2111 0.0354  0.0590  -0.0008 74  LEU C C   
10263 O O   . LEU C 82  ? 0.2022 0.4468 0.2610 0.0404  0.0677  0.0100  74  LEU C O   
10264 C CB  . LEU C 82  ? 0.2233 0.4223 0.2558 0.0636  0.0565  -0.0183 74  LEU C CB  
10265 C CG  . LEU C 82  ? 0.2271 0.4330 0.2606 0.0795  0.0556  -0.0208 74  LEU C CG  
10266 C CD1 . LEU C 82  ? 0.3392 0.5117 0.3453 0.0940  0.0510  -0.0361 74  LEU C CD1 
10267 C CD2 . LEU C 82  ? 0.2137 0.4536 0.2577 0.0912  0.0640  -0.0082 74  LEU C CD2 
10268 N N   . THR C 83  ? 0.1538 0.3406 0.1956 0.0240  0.0532  -0.0081 75  THR C N   
10269 C CA  . THR C 83  ? 0.2032 0.3864 0.2397 0.0177  0.0564  -0.0051 75  THR C CA  
10270 C C   . THR C 83  ? 0.2238 0.4192 0.2783 0.0001  0.0533  0.0080  75  THR C C   
10271 O O   . THR C 83  ? 0.2551 0.4539 0.3088 -0.0050 0.0564  0.0140  75  THR C O   
10272 C CB  . THR C 83  ? 0.2575 0.4059 0.2757 0.0149  0.0519  -0.0168 75  THR C CB  
10273 O OG1 . THR C 83  ? 0.2414 0.3720 0.2619 0.0049  0.0436  -0.0202 75  THR C OG1 
10274 C CG2 . THR C 83  ? 0.2045 0.3394 0.2040 0.0307  0.0525  -0.0275 75  THR C CG2 
10275 N N   . GLY C 84  ? 0.2107 0.4106 0.2801 -0.0097 0.0454  0.0132  76  GLY C N   
10276 C CA  . GLY C 84  ? 0.2384 0.4511 0.3258 -0.0262 0.0396  0.0281  76  GLY C CA  
10277 C C   . GLY C 84  ? 0.2279 0.4111 0.3116 -0.0415 0.0258  0.0247  76  GLY C C   
10278 O O   . GLY C 84  ? 0.2067 0.3908 0.3004 -0.0564 0.0176  0.0356  76  GLY C O   
10279 N N   . TYR C 85  ? 0.1943 0.3508 0.2624 -0.0374 0.0224  0.0105  77  TYR C N   
10280 C CA  . TYR C 85  ? 0.1910 0.3192 0.2509 -0.0475 0.0101  0.0062  77  TYR C CA  
10281 C C   . TYR C 85  ? 0.2420 0.3798 0.3171 -0.0567 -0.0012 0.0147  77  TYR C C   
10282 O O   . TYR C 85  ? 0.1950 0.3630 0.2886 -0.0538 0.0016  0.0232  77  TYR C O   
10283 C CB  . TYR C 85  ? 0.1965 0.3003 0.2375 -0.0388 0.0109  -0.0082 77  TYR C CB  
10284 C CG  . TYR C 85  ? 0.2064 0.2964 0.2330 -0.0336 0.0178  -0.0145 77  TYR C CG  
10285 C CD1 . TYR C 85  ? 0.1801 0.2820 0.2061 -0.0243 0.0273  -0.0159 77  TYR C CD1 
10286 C CD2 . TYR C 85  ? 0.2060 0.2705 0.2182 -0.0370 0.0141  -0.0186 77  TYR C CD2 
10287 C CE1 . TYR C 85  ? 0.1726 0.2617 0.1863 -0.0210 0.0314  -0.0204 77  TYR C CE1 
10288 C CE2 . TYR C 85  ? 0.2186 0.2739 0.2206 -0.0324 0.0201  -0.0222 77  TYR C CE2 
10289 C CZ  . TYR C 85  ? 0.2247 0.2926 0.2287 -0.0258 0.0281  -0.0226 77  TYR C CZ  
10290 O OH  . TYR C 85  ? 0.2967 0.3553 0.2913 -0.0226 0.0320  -0.0252 77  TYR C OH  
10291 N N   . ASN C 86  ? 0.2713 0.3817 0.3369 -0.0669 -0.0150 0.0126  78  ASN C N   
10292 C CA  . ASN C 86  ? 0.3096 0.4209 0.3852 -0.0774 -0.0301 0.0194  78  ASN C CA  
10293 C C   . ASN C 86  ? 0.3568 0.4659 0.4274 -0.0682 -0.0298 0.0108  78  ASN C C   
10294 O O   . ASN C 86  ? 0.4675 0.5490 0.5204 -0.0684 -0.0388 0.0022  78  ASN C O   
10295 C CB  . ASN C 86  ? 0.4478 0.5237 0.5084 -0.0894 -0.0471 0.0184  78  ASN C CB  
10296 C CG  . ASN C 86  ? 0.5980 0.6683 0.6646 -0.1008 -0.0663 0.0245  78  ASN C CG  
10297 O OD1 . ASN C 86  ? 0.7230 0.7629 0.7680 -0.0986 -0.0761 0.0140  78  ASN C OD1 
10298 N ND2 . ASN C 86  ? 0.5912 0.6927 0.6874 -0.1123 -0.0720 0.0427  78  ASN C ND2 
10299 N N   . LEU C 87  ? 0.2321 0.3706 0.3167 -0.0583 -0.0192 0.0133  79  LEU C N   
10300 C CA  . LEU C 87  ? 0.1744 0.3151 0.2582 -0.0495 -0.0192 0.0075  79  LEU C CA  
10301 C C   . LEU C 87  ? 0.2029 0.3842 0.3118 -0.0443 -0.0132 0.0189  79  LEU C C   
10302 O O   . LEU C 87  ? 0.1645 0.3635 0.2762 -0.0334 0.0001  0.0197  79  LEU C O   
10303 C CB  . LEU C 87  ? 0.1981 0.3215 0.2623 -0.0363 -0.0102 -0.0067 79  LEU C CB  
10304 C CG  . LEU C 87  ? 0.2267 0.3418 0.2842 -0.0290 -0.0128 -0.0138 79  LEU C CG  
10305 C CD1 . LEU C 87  ? 0.1607 0.2540 0.2076 -0.0371 -0.0261 -0.0158 79  LEU C CD1 
10306 C CD2 . LEU C 87  ? 0.2001 0.3015 0.2423 -0.0181 -0.0048 -0.0237 79  LEU C CD2 
10307 N N   . SER C 88  ? 0.1638 0.3599 0.2898 -0.0509 -0.0232 0.0285  80  SER C N   
10308 C CA  . SER C 88  ? 0.1810 0.4213 0.3352 -0.0472 -0.0185 0.0442  80  SER C CA  
10309 C C   . SER C 88  ? 0.1391 0.3903 0.2945 -0.0305 -0.0128 0.0387  80  SER C C   
10310 O O   . SER C 88  ? 0.1587 0.3829 0.2957 -0.0255 -0.0155 0.0247  80  SER C O   
10311 C CB  . SER C 88  ? 0.1935 0.4479 0.3706 -0.0661 -0.0347 0.0619  80  SER C CB  
10312 O OG  . SER C 88  ? 0.2279 0.4617 0.3980 -0.0708 -0.0490 0.0561  80  SER C OG  
10313 N N   . ILE C 89  ? 0.1355 0.4282 0.3132 -0.0211 -0.0049 0.0517  81  ILE C N   
10314 C CA  . ILE C 89  ? 0.1347 0.4399 0.3162 -0.0050 -0.0017 0.0491  81  ILE C CA  
10315 C C   . ILE C 89  ? 0.1389 0.4315 0.3240 -0.0156 -0.0178 0.0489  81  ILE C C   
10316 O O   . ILE C 89  ? 0.1812 0.4576 0.3541 -0.0061 -0.0191 0.0377  81  ILE C O   
10317 C CB  . ILE C 89  ? 0.2253 0.5820 0.4322 0.0076  0.0091  0.0663  81  ILE C CB  
10318 C CG1 . ILE C 89  ? 0.2489 0.6093 0.4397 0.0293  0.0266  0.0587  81  ILE C CG1 
10319 C CG2 . ILE C 89  ? 0.2751 0.6501 0.4958 0.0168  0.0059  0.0712  81  ILE C CG2 
10320 C CD1 . ILE C 89  ? 0.2029 0.5359 0.3685 0.0487  0.0296  0.0390  81  ILE C CD1 
10321 N N   . GLU C 90  ? 0.1443 0.4422 0.3449 -0.0358 -0.0321 0.0619  82  GLU C N   
10322 C CA  . GLU C 90  ? 0.1840 0.4652 0.3835 -0.0460 -0.0496 0.0609  82  GLU C CA  
10323 C C   . GLU C 90  ? 0.1848 0.4173 0.3496 -0.0453 -0.0535 0.0403  82  GLU C C   
10324 O O   . GLU C 90  ? 0.2239 0.4433 0.3803 -0.0418 -0.0598 0.0337  82  GLU C O   
10325 C CB  . GLU C 90  ? 0.2640 0.5515 0.4814 -0.0693 -0.0679 0.0777  82  GLU C CB  
10326 C CG  . GLU C 90  ? 0.3609 0.6891 0.6080 -0.0692 -0.0642 0.0996  82  GLU C CG  
10327 C CD  . GLU C 90  ? 0.4476 0.7984 0.7070 -0.0554 -0.0606 0.1029  82  GLU C CD  
10328 O OE1 . GLU C 90  ? 0.4417 0.7758 0.6941 -0.0570 -0.0720 0.0948  82  GLU C OE1 
10329 O OE2 . GLU C 90  ? 0.4724 0.8560 0.7459 -0.0421 -0.0465 0.1136  82  GLU C OE2 
10330 N N   . ASP C 91  ? 0.1878 0.3956 0.3329 -0.0477 -0.0494 0.0313  83  ASP C N   
10331 C CA  . ASP C 91  ? 0.1735 0.3415 0.2875 -0.0440 -0.0500 0.0141  83  ASP C CA  
10332 C C   . ASP C 91  ? 0.2225 0.3904 0.3292 -0.0268 -0.0397 0.0047  83  ASP C C   
10333 O O   . ASP C 91  ? 0.1713 0.3188 0.2632 -0.0241 -0.0446 -0.0032 83  ASP C O   
10334 C CB  . ASP C 91  ? 0.1714 0.3189 0.2689 -0.0472 -0.0454 0.0081  83  ASP C CB  
10335 C CG  . ASP C 91  ? 0.2595 0.3949 0.3569 -0.0644 -0.0594 0.0149  83  ASP C CG  
10336 O OD1 . ASP C 91  ? 0.2718 0.3947 0.3666 -0.0735 -0.0760 0.0171  83  ASP C OD1 
10337 O OD2 . ASP C 91  ? 0.2634 0.3994 0.3619 -0.0688 -0.0553 0.0180  83  ASP C OD2 
10338 N N   . LEU C 92  ? 0.1455 0.3345 0.2607 -0.0143 -0.0265 0.0059  84  LEU C N   
10339 C CA  . LEU C 92  ? 0.1596 0.3437 0.2660 0.0022  -0.0199 -0.0029 84  LEU C CA  
10340 C C   . LEU C 92  ? 0.2141 0.4085 0.3307 0.0068  -0.0265 0.0005  84  LEU C C   
10341 O O   . LEU C 92  ? 0.2061 0.3833 0.3104 0.0142  -0.0282 -0.0077 84  LEU C O   
10342 C CB  . LEU C 92  ? 0.1622 0.3640 0.2718 0.0166  -0.0065 -0.0025 84  LEU C CB  
10343 C CG  . LEU C 92  ? 0.2281 0.4216 0.3280 0.0131  0.0003  -0.0051 84  LEU C CG  
10344 C CD1 . LEU C 92  ? 0.2508 0.4558 0.3468 0.0306  0.0123  -0.0074 84  LEU C CD1 
10345 C CD2 . LEU C 92  ? 0.1653 0.3226 0.2432 0.0068  -0.0033 -0.0159 84  LEU C CD2 
10346 N N   . LYS C 93  ? 0.1468 0.3707 0.2876 0.0019  -0.0310 0.0141  85  LYS C N   
10347 C CA  . LYS C 93  ? 0.1504 0.3855 0.3028 0.0049  -0.0388 0.0189  85  LYS C CA  
10348 C C   . LYS C 93  ? 0.1717 0.3790 0.3107 -0.0069 -0.0533 0.0142  85  LYS C C   
10349 O O   . LYS C 93  ? 0.1705 0.3814 0.3148 -0.0044 -0.0607 0.0164  85  LYS C O   
10350 C CB  . LYS C 93  ? 0.1493 0.4271 0.3344 0.0012  -0.0411 0.0380  85  LYS C CB  
10351 C CG  . LYS C 93  ? 0.1909 0.5040 0.3903 0.0176  -0.0253 0.0455  85  LYS C CG  
10352 C CD  . LYS C 93  ? 0.2138 0.5750 0.4493 0.0126  -0.0276 0.0688  85  LYS C CD  
10353 C CE  . LYS C 93  ? 0.2607 0.6517 0.5030 0.0313  -0.0096 0.0760  85  LYS C CE  
10354 N NZ  . LYS C 93  ? 0.3183 0.7380 0.5829 0.0260  -0.0099 0.0969  85  LYS C NZ  
10355 N N   . ASN C 94  ? 0.1794 0.3596 0.3003 -0.0182 -0.0578 0.0085  86  ASN C N   
10356 C CA  . ASN C 94  ? 0.2356 0.3865 0.3370 -0.0257 -0.0702 0.0028  86  ASN C CA  
10357 C C   . ASN C 94  ? 0.2538 0.3767 0.3287 -0.0180 -0.0639 -0.0101 86  ASN C C   
10358 O O   . ASN C 94  ? 0.1947 0.2919 0.2481 -0.0226 -0.0706 -0.0152 86  ASN C O   
10359 C CB  . ASN C 94  ? 0.1993 0.3370 0.2956 -0.0421 -0.0823 0.0063  86  ASN C CB  
10360 C CG  . ASN C 94  ? 0.2724 0.4353 0.3959 -0.0537 -0.0942 0.0221  86  ASN C CG  
10361 O OD1 . ASN C 94  ? 0.3117 0.4946 0.4520 -0.0512 -0.0986 0.0292  86  ASN C OD1 
10362 N ND2 . ASN C 94  ? 0.3232 0.4857 0.4522 -0.0672 -0.1007 0.0293  86  ASN C ND2 
10363 N N   . PHE C 95  ? 0.1657 0.2933 0.2410 -0.0060 -0.0520 -0.0142 87  PHE C N   
10364 C CA  . PHE C 95  ? 0.1659 0.2709 0.2211 0.0002  -0.0476 -0.0228 87  PHE C CA  
10365 C C   . PHE C 95  ? 0.2948 0.3857 0.3387 -0.0003 -0.0565 -0.0238 87  PHE C C   
10366 O O   . PHE C 95  ? 0.1783 0.2792 0.2323 0.0020  -0.0626 -0.0201 87  PHE C O   
10367 C CB  . PHE C 95  ? 0.1678 0.2796 0.2277 0.0132  -0.0391 -0.0253 87  PHE C CB  
10368 C CG  . PHE C 95  ? 0.1609 0.2510 0.2040 0.0176  -0.0368 -0.0313 87  PHE C CG  
10369 C CD1 . PHE C 95  ? 0.2064 0.2821 0.2363 0.0127  -0.0330 -0.0340 87  PHE C CD1 
10370 C CD2 . PHE C 95  ? 0.2065 0.2914 0.2486 0.0266  -0.0394 -0.0325 87  PHE C CD2 
10371 C CE1 . PHE C 95  ? 0.2406 0.3010 0.2592 0.0157  -0.0315 -0.0359 87  PHE C CE1 
10372 C CE2 . PHE C 95  ? 0.2286 0.2946 0.2583 0.0284  -0.0396 -0.0349 87  PHE C CE2 
10373 C CZ  . PHE C 95  ? 0.2231 0.2789 0.2426 0.0224  -0.0355 -0.0356 87  PHE C CZ  
10374 N N   . ARG C 96  ? 0.2728 0.3421 0.2952 -0.0025 -0.0568 -0.0278 88  ARG C N   
10375 C CA  . ARG C 96  ? 0.2724 0.3281 0.2796 -0.0007 -0.0627 -0.0282 88  ARG C CA  
10376 C C   . ARG C 96  ? 0.3051 0.3584 0.3095 -0.0068 -0.0758 -0.0258 88  ARG C C   
10377 O O   . ARG C 96  ? 0.2857 0.3329 0.2815 -0.0043 -0.0819 -0.0248 88  ARG C O   
10378 C CB  . ARG C 96  ? 0.2033 0.2628 0.2166 0.0074  -0.0611 -0.0269 88  ARG C CB  
10379 C CG  . ARG C 96  ? 0.1926 0.2431 0.1984 0.0115  -0.0531 -0.0284 88  ARG C CG  
10380 C CD  . ARG C 96  ? 0.2699 0.3199 0.2819 0.0184  -0.0545 -0.0268 88  ARG C CD  
10381 N NE  . ARG C 96  ? 0.2649 0.3050 0.2702 0.0192  -0.0498 -0.0263 88  ARG C NE  
10382 C CZ  . ARG C 96  ? 0.2764 0.3082 0.2737 0.0187  -0.0516 -0.0206 88  ARG C CZ  
10383 N NH1 . ARG C 96  ? 0.2805 0.3115 0.2733 0.0187  -0.0574 -0.0160 88  ARG C NH1 
10384 N NH2 . ARG C 96  ? 0.3562 0.3822 0.3511 0.0178  -0.0483 -0.0178 88  ARG C NH2 
10385 N N   . GLN C 97  ? 0.2127 0.2696 0.2236 -0.0156 -0.0821 -0.0238 89  GLN C N   
10386 C CA  . GLN C 97  ? 0.2358 0.2881 0.2445 -0.0236 -0.0982 -0.0205 89  GLN C CA  
10387 C C   . GLN C 97  ? 0.2530 0.2768 0.2336 -0.0284 -0.1057 -0.0254 89  GLN C C   
10388 O O   . GLN C 97  ? 0.3014 0.3166 0.2736 -0.0280 -0.0982 -0.0292 89  GLN C O   
10389 C CB  . GLN C 97  ? 0.2346 0.3129 0.2738 -0.0313 -0.1038 -0.0112 89  GLN C CB  
10390 C CG  . GLN C 97  ? 0.2317 0.3387 0.2963 -0.0224 -0.0959 -0.0064 89  GLN C CG  
10391 C CD  . GLN C 97  ? 0.2770 0.3778 0.3340 -0.0143 -0.0982 -0.0086 89  GLN C CD  
10392 O OE1 . GLN C 97  ? 0.2591 0.3546 0.3116 -0.0185 -0.1112 -0.0059 89  GLN C OE1 
10393 N NE2 . GLN C 97  ? 0.2246 0.3242 0.2791 -0.0033 -0.0872 -0.0128 89  GLN C NE2 
10394 N N   . LEU C 98  ? 0.2777 0.2849 0.2416 -0.0317 -0.1213 -0.0257 90  LEU C N   
10395 C CA  . LEU C 98  ? 0.3612 0.3345 0.2892 -0.0315 -0.1298 -0.0325 90  LEU C CA  
10396 C C   . LEU C 98  ? 0.4132 0.3777 0.3424 -0.0405 -0.1341 -0.0327 90  LEU C C   
10397 O O   . LEU C 98  ? 0.3328 0.3092 0.2848 -0.0535 -0.1450 -0.0250 90  LEU C O   
10398 C CB  . LEU C 98  ? 0.3928 0.3487 0.3030 -0.0346 -0.1497 -0.0323 90  LEU C CB  
10399 C CG  . LEU C 98  ? 0.3783 0.2935 0.2424 -0.0296 -0.1594 -0.0411 90  LEU C CG  
10400 C CD1 . LEU C 98  ? 0.3787 0.2873 0.2174 -0.0123 -0.1424 -0.0464 90  LEU C CD1 
10401 C CD2 . LEU C 98  ? 0.4092 0.3090 0.2622 -0.0328 -0.1747 -0.0390 90  LEU C CD2 
10402 N N   . HIS C 99  ? 0.3359 0.2816 0.2419 -0.0336 -0.1256 -0.0398 91  HIS C N   
10403 C CA  . HIS C 99  ? 0.3971 0.3274 0.2965 -0.0395 -0.1291 -0.0416 91  HIS C CA  
10404 C C   . HIS C 99  ? 0.3992 0.3580 0.3341 -0.0473 -0.1199 -0.0347 91  HIS C C   
10405 O O   . HIS C 99  ? 0.4444 0.3947 0.3802 -0.0556 -0.1253 -0.0331 91  HIS C O   
10406 C CB  . HIS C 99  ? 0.4387 0.3403 0.3211 -0.0499 -0.1546 -0.0418 91  HIS C CB  
10407 C CG  . HIS C 99  ? 0.4839 0.3549 0.3283 -0.0376 -0.1577 -0.0485 91  HIS C CG  
10408 N ND1 . HIS C 99  ? 0.5182 0.3729 0.3317 -0.0208 -0.1453 -0.0565 91  HIS C ND1 
10409 C CD2 . HIS C 99  ? 0.5153 0.3716 0.3485 -0.0387 -0.1709 -0.0471 91  HIS C CD2 
10410 C CE1 . HIS C 99  ? 0.5457 0.3783 0.3309 -0.0114 -0.1503 -0.0595 91  HIS C CE1 
10411 N NE2 . HIS C 99  ? 0.5650 0.3958 0.3599 -0.0222 -0.1665 -0.0548 91  HIS C NE2 
10412 N N   . SER C 100 ? 0.3494 0.3398 0.3107 -0.0436 -0.1064 -0.0306 92  SER C N   
10413 C CA  . SER C 100 ? 0.3162 0.3322 0.3052 -0.0472 -0.0961 -0.0249 92  SER C CA  
10414 C C   . SER C 100 ? 0.3318 0.3382 0.3085 -0.0413 -0.0827 -0.0308 92  SER C C   
10415 O O   . SER C 100 ? 0.3633 0.3504 0.3150 -0.0323 -0.0779 -0.0379 92  SER C O   
10416 C CB  . SER C 100 ? 0.2633 0.3109 0.2779 -0.0412 -0.0861 -0.0206 92  SER C CB  
10417 O OG  . SER C 100 ? 0.2509 0.2958 0.2562 -0.0292 -0.0723 -0.0269 92  SER C OG  
10418 N N   . LYS C 101 ? 0.2939 0.3167 0.2894 -0.0460 -0.0764 -0.0260 93  LYS C N   
10419 C CA  . LYS C 101 ? 0.3090 0.3283 0.2982 -0.0407 -0.0628 -0.0301 93  LYS C CA  
10420 C C   . LYS C 101 ? 0.2573 0.2910 0.2526 -0.0298 -0.0478 -0.0325 93  LYS C C   
10421 O O   . LYS C 101 ? 0.2673 0.3000 0.2594 -0.0257 -0.0373 -0.0348 93  LYS C O   
10422 C CB  . LYS C 101 ? 0.3362 0.3682 0.3426 -0.0497 -0.0621 -0.0231 93  LYS C CB  
10423 C CG  . LYS C 101 ? 0.4180 0.4303 0.4169 -0.0624 -0.0792 -0.0198 93  LYS C CG  
10424 C CD  . LYS C 101 ? 0.5715 0.5973 0.5878 -0.0713 -0.0769 -0.0112 93  LYS C CD  
10425 C CE  . LYS C 101 ? 0.7011 0.7032 0.7097 -0.0855 -0.0966 -0.0067 93  LYS C CE  
10426 N NZ  . LYS C 101 ? 0.7597 0.7757 0.7857 -0.0946 -0.0941 0.0034  93  LYS C NZ  
10427 N N   . THR C 102 ? 0.2250 0.2699 0.2285 -0.0253 -0.0483 -0.0315 94  THR C N   
10428 C CA  . THR C 102 ? 0.1978 0.2521 0.2062 -0.0156 -0.0379 -0.0333 94  THR C CA  
10429 C C   . THR C 102 ? 0.2587 0.3030 0.2553 -0.0100 -0.0407 -0.0353 94  THR C C   
10430 O O   . THR C 102 ? 0.2277 0.2819 0.2342 -0.0064 -0.0427 -0.0335 94  THR C O   
10431 C CB  . THR C 102 ? 0.1740 0.2542 0.2060 -0.0132 -0.0350 -0.0286 94  THR C CB  
10432 O OG1 . THR C 102 ? 0.1897 0.2807 0.2335 -0.0181 -0.0451 -0.0229 94  THR C OG1 
10433 C CG2 . THR C 102 ? 0.1889 0.2819 0.2311 -0.0158 -0.0283 -0.0255 94  THR C CG2 
10434 N N   . PRO C 103 ? 0.2199 0.2455 0.1947 -0.0079 -0.0406 -0.0380 95  PRO C N   
10435 C CA  . PRO C 103 ? 0.1970 0.2167 0.1608 -0.0019 -0.0418 -0.0374 95  PRO C CA  
10436 C C   . PRO C 103 ? 0.1834 0.2112 0.1566 0.0032  -0.0348 -0.0352 95  PRO C C   
10437 O O   . PRO C 103 ? 0.2191 0.2520 0.2008 0.0037  -0.0284 -0.0359 95  PRO C O   
10438 C CB  . PRO C 103 ? 0.3016 0.3030 0.2394 0.0018  -0.0403 -0.0393 95  PRO C CB  
10439 C CG  . PRO C 103 ? 0.2178 0.2167 0.1562 -0.0005 -0.0347 -0.0413 95  PRO C CG  
10440 C CD  . PRO C 103 ? 0.2280 0.2382 0.1864 -0.0090 -0.0387 -0.0407 95  PRO C CD  
10441 N N   . GLY C 104 ? 0.2340 0.2608 0.2042 0.0069  -0.0379 -0.0321 96  GLY C N   
10442 C CA  . GLY C 104 ? 0.2013 0.2322 0.1808 0.0103  -0.0360 -0.0290 96  GLY C CA  
10443 C C   . GLY C 104 ? 0.2454 0.2734 0.2227 0.0111  -0.0289 -0.0268 96  GLY C C   
10444 O O   . GLY C 104 ? 0.2079 0.2366 0.1941 0.0122  -0.0289 -0.0262 96  GLY C O   
10445 N N   . HIS C 105 ? 0.1858 0.2827 0.2776 0.0003  -0.0788 0.0077  97  HIS C N   
10446 C CA  . HIS C 105 ? 0.1560 0.2423 0.2301 0.0016  -0.0644 0.0018  97  HIS C CA  
10447 C C   . HIS C 105 ? 0.1706 0.2599 0.2443 -0.0062 -0.0587 -0.0006 97  HIS C C   
10448 O O   . HIS C 105 ? 0.1616 0.2502 0.2339 -0.0152 -0.0679 0.0006  97  HIS C O   
10449 C CB  . HIS C 105 ? 0.2371 0.3003 0.2795 0.0004  -0.0660 -0.0003 97  HIS C CB  
10450 C CG  . HIS C 105 ? 0.3870 0.4443 0.4272 0.0073  -0.0713 0.0028  97  HIS C CG  
10451 N ND1 . HIS C 105 ? 0.4645 0.5081 0.4870 0.0044  -0.0827 0.0059  97  HIS C ND1 
10452 C CD2 . HIS C 105 ? 0.4459 0.5068 0.4977 0.0171  -0.0665 0.0032  97  HIS C CD2 
10453 C CE1 . HIS C 105 ? 0.4605 0.5006 0.4854 0.0120  -0.0849 0.0090  97  HIS C CE1 
10454 N NE2 . HIS C 105 ? 0.3919 0.4422 0.4351 0.0198  -0.0752 0.0071  97  HIS C NE2 
10455 N N   . PRO C 106 ? 0.1885 0.2798 0.2624 -0.0032 -0.0445 -0.0038 98  PRO C N   
10456 C CA  . PRO C 106 ? 0.1857 0.2804 0.2613 -0.0099 -0.0385 -0.0050 98  PRO C CA  
10457 C C   . PRO C 106 ? 0.1938 0.2710 0.2452 -0.0188 -0.0429 -0.0074 98  PRO C C   
10458 O O   . PRO C 106 ? 0.1806 0.2414 0.2093 -0.0176 -0.0420 -0.0101 98  PRO C O   
10459 C CB  . PRO C 106 ? 0.1415 0.2360 0.2138 -0.0036 -0.0236 -0.0080 98  PRO C CB  
10460 C CG  . PRO C 106 ? 0.2226 0.3178 0.2983 0.0068  -0.0221 -0.0085 98  PRO C CG  
10461 C CD  . PRO C 106 ? 0.1807 0.2676 0.2490 0.0058  -0.0344 -0.0068 98  PRO C CD  
10462 N N   . GLU C 107 ? 0.1605 0.2406 0.2172 -0.0277 -0.0466 -0.0065 99  GLU C N   
10463 C CA  . GLU C 107 ? 0.2054 0.2668 0.2385 -0.0363 -0.0511 -0.0093 99  GLU C CA  
10464 C C   . GLU C 107 ? 0.1602 0.2186 0.1906 -0.0404 -0.0412 -0.0112 99  GLU C C   
10465 O O   . GLU C 107 ? 0.2206 0.2914 0.2702 -0.0448 -0.0401 -0.0088 99  GLU C O   
10466 C CB  . GLU C 107 ? 0.2536 0.3145 0.2891 -0.0446 -0.0676 -0.0072 99  GLU C CB  
10467 C CG  . GLU C 107 ? 0.2375 0.2915 0.2621 -0.0414 -0.0787 -0.0057 99  GLU C CG  
10468 C CD  . GLU C 107 ? 0.2624 0.3144 0.2867 -0.0498 -0.0972 -0.0034 99  GLU C CD  
10469 O OE1 . GLU C 107 ? 0.2785 0.3268 0.3013 -0.0598 -0.1015 -0.0049 99  GLU C OE1 
10470 O OE2 . GLU C 107 ? 0.2674 0.3210 0.2932 -0.0467 -0.1084 0.0002  99  GLU C OE2 
10471 N N   . TYR C 108 ? 0.1623 0.2048 0.1709 -0.0388 -0.0337 -0.0147 100 TYR C N   
10472 C CA  . TYR C 108 ? 0.1610 0.1974 0.1645 -0.0426 -0.0255 -0.0161 100 TYR C CA  
10473 C C   . TYR C 108 ? 0.1940 0.2233 0.1950 -0.0535 -0.0332 -0.0165 100 TYR C C   
10474 O O   . TYR C 108 ? 0.1976 0.2146 0.1840 -0.0581 -0.0433 -0.0182 100 TYR C O   
10475 C CB  . TYR C 108 ? 0.2020 0.2216 0.1835 -0.0391 -0.0182 -0.0194 100 TYR C CB  
10476 C CG  . TYR C 108 ? 0.1970 0.2078 0.1722 -0.0426 -0.0109 -0.0203 100 TYR C CG  
10477 C CD1 . TYR C 108 ? 0.1909 0.2106 0.1765 -0.0398 -0.0022 -0.0184 100 TYR C CD1 
10478 C CD2 . TYR C 108 ? 0.2061 0.1979 0.1633 -0.0484 -0.0125 -0.0231 100 TYR C CD2 
10479 C CE1 . TYR C 108 ? 0.2470 0.2579 0.2268 -0.0425 0.0041  -0.0183 100 TYR C CE1 
10480 C CE2 . TYR C 108 ? 0.2119 0.1943 0.1641 -0.0508 -0.0055 -0.0237 100 TYR C CE2 
10481 C CZ  . TYR C 108 ? 0.3132 0.3058 0.2777 -0.0478 0.0024  -0.0209 100 TYR C CZ  
10482 O OH  . TYR C 108 ? 0.4082 0.3908 0.3678 -0.0497 0.0089  -0.0205 100 TYR C OH  
10483 N N   . GLY C 109 ? 0.1945 0.2295 0.2076 -0.0581 -0.0284 -0.0148 101 GLY C N   
10484 C CA  . GLY C 109 ? 0.2711 0.2972 0.2819 -0.0692 -0.0342 -0.0155 101 GLY C CA  
10485 C C   . GLY C 109 ? 0.3356 0.3785 0.3726 -0.0764 -0.0439 -0.0116 101 GLY C C   
10486 O O   . GLY C 109 ? 0.4344 0.4760 0.4790 -0.0856 -0.0450 -0.0106 101 GLY C O   
10487 N N   . TYR C 110 ? 0.3290 0.3877 0.3816 -0.0726 -0.0510 -0.0088 102 TYR C N   
10488 C CA  . TYR C 110 ? 0.4006 0.4775 0.4822 -0.0790 -0.0616 -0.0042 102 TYR C CA  
10489 C C   . TYR C 110 ? 0.3297 0.4329 0.4447 -0.0736 -0.0516 0.0014  102 TYR C C   
10490 O O   . TYR C 110 ? 0.3167 0.4364 0.4605 -0.0801 -0.0558 0.0061  102 TYR C O   
10491 C CB  . TYR C 110 ? 0.4805 0.5578 0.5602 -0.0788 -0.0781 -0.0036 102 TYR C CB  
10492 N N   . THR C 111 ? 0.2103 0.3170 0.3219 -0.0621 -0.0386 0.0009  103 THR C N   
10493 C CA  . THR C 111 ? 0.1464 0.2745 0.2839 -0.0553 -0.0270 0.0053  103 THR C CA  
10494 C C   . THR C 111 ? 0.1422 0.2633 0.2669 -0.0520 -0.0106 0.0041  103 THR C C   
10495 O O   . THR C 111 ? 0.1677 0.2741 0.2674 -0.0464 -0.0066 -0.0001 103 THR C O   
10496 C CB  . THR C 111 ? 0.1850 0.3216 0.3281 -0.0438 -0.0274 0.0055  103 THR C CB  
10497 O OG1 . THR C 111 ? 0.2715 0.4121 0.4234 -0.0467 -0.0443 0.0072  103 THR C OG1 
10498 C CG2 . THR C 111 ? 0.2167 0.3742 0.3863 -0.0363 -0.0146 0.0097  103 THR C CG2 
10499 N N   . ASP C 112 ? 0.1425 0.2739 0.2847 -0.0558 -0.0017 0.0085  104 ASP C N   
10500 C CA  . ASP C 112 ? 0.1484 0.2731 0.2781 -0.0526 0.0135  0.0087  104 ASP C CA  
10501 C C   . ASP C 112 ? 0.1602 0.2864 0.2807 -0.0395 0.0228  0.0068  104 ASP C C   
10502 O O   . ASP C 112 ? 0.1565 0.2976 0.2940 -0.0328 0.0251  0.0084  104 ASP C O   
10503 C CB  . ASP C 112 ? 0.2551 0.3932 0.4081 -0.0579 0.0228  0.0153  104 ASP C CB  
10504 C CG  . ASP C 112 ? 0.3058 0.4372 0.4632 -0.0719 0.0155  0.0167  104 ASP C CG  
10505 O OD1 . ASP C 112 ? 0.3213 0.4349 0.4591 -0.0768 0.0044  0.0118  104 ASP C OD1 
10506 O OD2 . ASP C 112 ? 0.2639 0.4067 0.4438 -0.0780 0.0215  0.0228  104 ASP C OD2 
10507 N N   . GLY C 113 ? 0.1601 0.2702 0.2545 -0.0358 0.0279  0.0035  105 GLY C N   
10508 C CA  . GLY C 113 ? 0.1547 0.2633 0.2377 -0.0249 0.0358  0.0013  105 GLY C CA  
10509 C C   . GLY C 113 ? 0.2127 0.3125 0.2814 -0.0194 0.0283  -0.0039 105 GLY C C   
10510 O O   . GLY C 113 ? 0.2680 0.3617 0.3227 -0.0119 0.0331  -0.0066 105 GLY C O   
10511 N N   . VAL C 114 ? 0.2065 0.3046 0.2776 -0.0235 0.0163  -0.0050 106 VAL C N   
10512 C CA  . VAL C 114 ? 0.1411 0.2292 0.1976 -0.0194 0.0096  -0.0090 106 VAL C CA  
10513 C C   . VAL C 114 ? 0.1914 0.2612 0.2248 -0.0218 0.0099  -0.0119 106 VAL C C   
10514 O O   . VAL C 114 ? 0.1711 0.2329 0.1994 -0.0295 0.0064  -0.0119 106 VAL C O   
10515 C CB  . VAL C 114 ? 0.1497 0.2410 0.2146 -0.0228 -0.0032 -0.0083 106 VAL C CB  
10516 C CG1 . VAL C 114 ? 0.1284 0.2077 0.1763 -0.0186 -0.0088 -0.0115 106 VAL C CG1 
10517 C CG2 . VAL C 114 ? 0.1252 0.2367 0.2179 -0.0198 -0.0039 -0.0043 106 VAL C CG2 
10518 N N   . GLU C 115 ? 0.1505 0.2132 0.1709 -0.0152 0.0137  -0.0145 107 GLU C N   
10519 C CA  . GLU C 115 ? 0.1682 0.2161 0.1711 -0.0162 0.0153  -0.0163 107 GLU C CA  
10520 C C   . GLU C 115 ? 0.1684 0.2049 0.1601 -0.0174 0.0090  -0.0187 107 GLU C C   
10521 O O   . GLU C 115 ? 0.1717 0.1959 0.1513 -0.0194 0.0106  -0.0197 107 GLU C O   
10522 C CB  . GLU C 115 ? 0.1568 0.2027 0.1523 -0.0093 0.0214  -0.0173 107 GLU C CB  
10523 C CG  . GLU C 115 ? 0.1769 0.2310 0.1776 -0.0070 0.0293  -0.0150 107 GLU C CG  
10524 C CD  . GLU C 115 ? 0.2432 0.2937 0.2417 -0.0122 0.0337  -0.0118 107 GLU C CD  
10525 O OE1 . GLU C 115 ? 0.2302 0.2711 0.2231 -0.0172 0.0307  -0.0121 107 GLU C OE1 
10526 O OE2 . GLU C 115 ? 0.2075 0.2637 0.2092 -0.0111 0.0411  -0.0088 107 GLU C OE2 
10527 N N   . THR C 116 ? 0.1587 0.1982 0.1538 -0.0157 0.0028  -0.0191 108 THR C N   
10528 C CA  . THR C 116 ? 0.1450 0.1725 0.1274 -0.0165 -0.0022 -0.0206 108 THR C CA  
10529 C C   . THR C 116 ? 0.2013 0.2343 0.1905 -0.0163 -0.0108 -0.0193 108 THR C C   
10530 O O   . THR C 116 ? 0.1781 0.2246 0.1832 -0.0127 -0.0114 -0.0178 108 THR C O   
10531 C CB  . THR C 116 ? 0.2097 0.2307 0.1841 -0.0109 0.0018  -0.0222 108 THR C CB  
10532 O OG1 . THR C 116 ? 0.2044 0.2135 0.1670 -0.0121 -0.0011 -0.0228 108 THR C OG1 
10533 C CG2 . THR C 116 ? 0.2223 0.2520 0.2056 -0.0042 0.0022  -0.0225 108 THR C CG2 
10534 N N   . THR C 117 ? 0.1631 0.1846 0.1395 -0.0196 -0.0171 -0.0196 109 THR C N   
10535 C CA  . THR C 117 ? 0.1879 0.2119 0.1675 -0.0191 -0.0268 -0.0176 109 THR C CA  
10536 C C   . THR C 117 ? 0.2151 0.2347 0.1900 -0.0123 -0.0253 -0.0177 109 THR C C   
10537 O O   . THR C 117 ? 0.2058 0.2118 0.1648 -0.0124 -0.0220 -0.0188 109 THR C O   
10538 C CB  . THR C 117 ? 0.1910 0.2022 0.1549 -0.0263 -0.0353 -0.0177 109 THR C CB  
10539 O OG1 . THR C 117 ? 0.1938 0.2084 0.1636 -0.0335 -0.0376 -0.0179 109 THR C OG1 
10540 C CG2 . THR C 117 ? 0.1790 0.1919 0.1446 -0.0255 -0.0472 -0.0146 109 THR C CG2 
10541 N N   . THR C 118 ? 0.1978 0.2282 0.1874 -0.0064 -0.0269 -0.0162 110 THR C N   
10542 C CA  . THR C 118 ? 0.2084 0.2335 0.1947 -0.0003 -0.0260 -0.0163 110 THR C CA  
10543 C C   . THR C 118 ? 0.2609 0.2888 0.2539 0.0023  -0.0353 -0.0128 110 THR C C   
10544 O O   . THR C 118 ? 0.2986 0.3390 0.3072 0.0021  -0.0407 -0.0104 110 THR C O   
10545 C CB  . THR C 118 ? 0.1850 0.2158 0.1794 0.0060  -0.0180 -0.0187 110 THR C CB  
10546 O OG1 . THR C 118 ? 0.2338 0.2796 0.2462 0.0094  -0.0171 -0.0180 110 THR C OG1 
10547 C CG2 . THR C 118 ? 0.1864 0.2132 0.1732 0.0039  -0.0105 -0.0213 110 THR C CG2 
10548 N N   . GLY C 119 ? 0.2714 0.2877 0.2537 0.0048  -0.0370 -0.0117 111 GLY C N   
10549 C CA  . GLY C 119 ? 0.3200 0.3351 0.3051 0.0078  -0.0460 -0.0075 111 GLY C CA  
10550 C C   . GLY C 119 ? 0.2720 0.2715 0.2427 0.0098  -0.0440 -0.0068 111 GLY C C   
10551 O O   . GLY C 119 ? 0.2751 0.2741 0.2530 0.0160  -0.0431 -0.0063 111 GLY C O   
10552 N N   . PRO C 120 ? 0.2876 0.2729 0.2377 0.0045  -0.0422 -0.0067 112 PRO C N   
10553 C CA  . PRO C 120 ? 0.2428 0.2139 0.1811 0.0057  -0.0374 -0.0056 112 PRO C CA  
10554 C C   . PRO C 120 ? 0.2366 0.2119 0.1854 0.0089  -0.0288 -0.0094 112 PRO C C   
10555 O O   . PRO C 120 ? 0.2058 0.1862 0.1572 0.0071  -0.0230 -0.0129 112 PRO C O   
10556 C CB  . PRO C 120 ? 0.2585 0.2162 0.1750 -0.0005 -0.0342 -0.0056 112 PRO C CB  
10557 C CG  . PRO C 120 ? 0.3164 0.2769 0.2286 -0.0049 -0.0426 -0.0055 112 PRO C CG  
10558 C CD  . PRO C 120 ? 0.3029 0.2830 0.2392 -0.0028 -0.0440 -0.0075 112 PRO C CD  
10559 N N   . LEU C 121 ? 0.2108 0.1827 0.1650 0.0136  -0.0291 -0.0084 113 LEU C N   
10560 C CA  . LEU C 121 ? 0.1675 0.1432 0.1321 0.0171  -0.0239 -0.0126 113 LEU C CA  
10561 C C   . LEU C 121 ? 0.2266 0.1962 0.1857 0.0134  -0.0169 -0.0141 113 LEU C C   
10562 O O   . LEU C 121 ? 0.2232 0.1832 0.1714 0.0095  -0.0144 -0.0113 113 LEU C O   
10563 C CB  . LEU C 121 ? 0.2101 0.1812 0.1811 0.0229  -0.0267 -0.0115 113 LEU C CB  
10564 C CG  . LEU C 121 ? 0.2478 0.2276 0.2299 0.0284  -0.0328 -0.0099 113 LEU C CG  
10565 C CD1 . LEU C 121 ? 0.2404 0.2128 0.2280 0.0350  -0.0349 -0.0087 113 LEU C CD1 
10566 C CD2 . LEU C 121 ? 0.2870 0.2821 0.2810 0.0305  -0.0295 -0.0140 113 LEU C CD2 
10567 N N   . GLY C 122 ? 0.1899 0.1648 0.1567 0.0149  -0.0136 -0.0185 114 GLY C N   
10568 C CA  . GLY C 122 ? 0.2081 0.1802 0.1743 0.0119  -0.0086 -0.0198 114 GLY C CA  
10569 C C   . GLY C 122 ? 0.1929 0.1697 0.1560 0.0085  -0.0046 -0.0204 114 GLY C C   
10570 O O   . GLY C 122 ? 0.1811 0.1601 0.1480 0.0078  -0.0014 -0.0221 114 GLY C O   
10571 N N   . GLN C 123 ? 0.1549 0.1324 0.1111 0.0063  -0.0054 -0.0189 115 GLN C N   
10572 C CA  . GLN C 123 ? 0.1950 0.1733 0.1468 0.0029  -0.0010 -0.0196 115 GLN C CA  
10573 C C   . GLN C 123 ? 0.1858 0.1749 0.1449 0.0040  -0.0003 -0.0224 115 GLN C C   
10574 O O   . GLN C 123 ? 0.1839 0.1734 0.1423 0.0023  0.0040  -0.0230 115 GLN C O   
10575 C CB  . GLN C 123 ? 0.2076 0.1798 0.1467 -0.0008 -0.0026 -0.0178 115 GLN C CB  
10576 C CG  . GLN C 123 ? 0.2159 0.1742 0.1426 -0.0022 -0.0003 -0.0146 115 GLN C CG  
10577 C CD  . GLN C 123 ? 0.2680 0.2163 0.1765 -0.0061 -0.0018 -0.0135 115 GLN C CD  
10578 O OE1 . GLN C 123 ? 0.2051 0.1511 0.1074 -0.0089 0.0016  -0.0155 115 GLN C OE1 
10579 N NE2 . GLN C 123 ? 0.2221 0.1625 0.1201 -0.0062 -0.0075 -0.0103 115 GLN C NE2 
10580 N N   . GLY C 124 ? 0.1615 0.1586 0.1277 0.0072  -0.0036 -0.0237 116 GLY C N   
10581 C CA  . GLY C 124 ? 0.1702 0.1765 0.1417 0.0084  -0.0014 -0.0257 116 GLY C CA  
10582 C C   . GLY C 124 ? 0.1868 0.1924 0.1585 0.0098  0.0017  -0.0277 116 GLY C C   
10583 O O   . GLY C 124 ? 0.1525 0.1607 0.1232 0.0085  0.0047  -0.0279 116 GLY C O   
10584 N N   . ILE C 125 ? 0.1395 0.1405 0.1124 0.0123  0.0000  -0.0291 117 ILE C N   
10585 C CA  . ILE C 125 ? 0.1786 0.1780 0.1516 0.0127  0.0005  -0.0309 117 ILE C CA  
10586 C C   . ILE C 125 ? 0.1945 0.1920 0.1676 0.0091  0.0031  -0.0284 117 ILE C C   
10587 O O   . ILE C 125 ? 0.1598 0.1593 0.1333 0.0090  0.0040  -0.0285 117 ILE C O   
10588 C CB  . ILE C 125 ? 0.1930 0.1862 0.1679 0.0148  -0.0032 -0.0330 117 ILE C CB  
10589 C CG1 . ILE C 125 ? 0.1595 0.1507 0.1347 0.0141  -0.0052 -0.0348 117 ILE C CG1 
10590 C CG2 . ILE C 125 ? 0.1723 0.1589 0.1491 0.0126  -0.0039 -0.0301 117 ILE C CG2 
10591 C CD1 . ILE C 125 ? 0.2042 0.1989 0.1732 0.0166  -0.0048 -0.0374 117 ILE C CD1 
10592 N N   . ALA C 126 ? 0.1788 0.1713 0.1507 0.0065  0.0049  -0.0257 118 ALA C N   
10593 C CA  . ALA C 126 ? 0.1979 0.1877 0.1701 0.0040  0.0097  -0.0234 118 ALA C CA  
10594 C C   . ALA C 126 ? 0.1731 0.1655 0.1413 0.0030  0.0125  -0.0234 118 ALA C C   
10595 O O   . ALA C 126 ? 0.1362 0.1289 0.1071 0.0029  0.0153  -0.0223 118 ALA C O   
10596 C CB  . ALA C 126 ? 0.1316 0.1132 0.0994 0.0019  0.0129  -0.0207 118 ALA C CB  
10597 N N   . ASN C 127 ? 0.1397 0.1337 0.1029 0.0020  0.0112  -0.0241 119 ASN C N   
10598 C CA  . ASN C 127 ? 0.1460 0.1423 0.1068 0.0001  0.0133  -0.0240 119 ASN C CA  
10599 C C   . ASN C 127 ? 0.1701 0.1722 0.1349 0.0025  0.0138  -0.0244 119 ASN C C   
10600 O O   . ASN C 127 ? 0.1785 0.1794 0.1424 0.0016  0.0169  -0.0231 119 ASN C O   
10601 C CB  . ASN C 127 ? 0.1627 0.1629 0.1224 -0.0016 0.0102  -0.0244 119 ASN C CB  
10602 C CG  . ASN C 127 ? 0.1887 0.1821 0.1414 -0.0043 0.0073  -0.0237 119 ASN C CG  
10603 O OD1 . ASN C 127 ? 0.2016 0.1995 0.1564 -0.0049 0.0022  -0.0234 119 ASN C OD1 
10604 N ND2 . ASN C 127 ? 0.1472 0.1298 0.0914 -0.0057 0.0105  -0.0229 119 ASN C ND2 
10605 N N   . ALA C 128 ? 0.1654 0.1720 0.1326 0.0057  0.0109  -0.0262 120 ALA C N   
10606 C CA  . ALA C 128 ? 0.1881 0.1979 0.1543 0.0081  0.0112  -0.0269 120 ALA C CA  
10607 C C   . ALA C 128 ? 0.1595 0.1660 0.1268 0.0085  0.0101  -0.0257 120 ALA C C   
10608 O O   . ALA C 128 ? 0.1545 0.1616 0.1192 0.0091  0.0108  -0.0243 120 ALA C O   
10609 C CB  . ALA C 128 ? 0.1961 0.2083 0.1617 0.0119  0.0091  -0.0298 120 ALA C CB  
10610 N N   . VAL C 129 ? 0.1219 0.1252 0.0942 0.0080  0.0082  -0.0255 121 VAL C N   
10611 C CA  . VAL C 129 ? 0.1199 0.1222 0.0983 0.0080  0.0070  -0.0233 121 VAL C CA  
10612 C C   . VAL C 129 ? 0.1529 0.1542 0.1320 0.0071  0.0123  -0.0201 121 VAL C C   
10613 O O   . VAL C 129 ? 0.1652 0.1675 0.1469 0.0083  0.0113  -0.0178 121 VAL C O   
10614 C CB  . VAL C 129 ? 0.1194 0.1192 0.1064 0.0068  0.0059  -0.0227 121 VAL C CB  
10615 C CG1 . VAL C 129 ? 0.1192 0.1202 0.1180 0.0064  0.0061  -0.0190 121 VAL C CG1 
10616 C CG2 . VAL C 129 ? 0.1296 0.1282 0.1158 0.0078  -0.0003 -0.0260 121 VAL C CG2 
10617 N N   . GLY C 130 ? 0.1491 0.1470 0.1247 0.0050  0.0173  -0.0199 122 GLY C N   
10618 C CA  . GLY C 130 ? 0.1535 0.1473 0.1275 0.0041  0.0228  -0.0178 122 GLY C CA  
10619 C C   . GLY C 130 ? 0.1487 0.1442 0.1184 0.0042  0.0228  -0.0171 122 GLY C C   
10620 O O   . GLY C 130 ? 0.1485 0.1413 0.1197 0.0051  0.0254  -0.0143 122 GLY C O   
10621 N N   . MET C 131 ? 0.1333 0.1332 0.0985 0.0037  0.0208  -0.0189 123 MET C N   
10622 C CA  . MET C 131 ? 0.1964 0.1982 0.1577 0.0036  0.0222  -0.0175 123 MET C CA  
10623 C C   . MET C 131 ? 0.1734 0.1761 0.1337 0.0070  0.0195  -0.0156 123 MET C C   
10624 O O   . MET C 131 ? 0.1690 0.1694 0.1264 0.0073  0.0213  -0.0123 123 MET C O   
10625 C CB  . MET C 131 ? 0.2238 0.2316 0.1835 0.0029  0.0220  -0.0193 123 MET C CB  
10626 C CG  . MET C 131 ? 0.1790 0.1868 0.1402 -0.0009 0.0222  -0.0204 123 MET C CG  
10627 S SD  . MET C 131 ? 0.1788 0.1968 0.1446 -0.0008 0.0214  -0.0213 123 MET C SD  
10628 C CE  . MET C 131 ? 0.1628 0.1790 0.1304 -0.0060 0.0181  -0.0218 123 MET C CE  
10629 N N   . ALA C 132 ? 0.1430 0.1474 0.1045 0.0092  0.0142  -0.0175 124 ALA C N   
10630 C CA  . ALA C 132 ? 0.1785 0.1823 0.1373 0.0118  0.0092  -0.0161 124 ALA C CA  
10631 C C   . ALA C 132 ? 0.1796 0.1818 0.1475 0.0123  0.0081  -0.0119 124 ALA C C   
10632 O O   . ALA C 132 ? 0.1571 0.1580 0.1228 0.0141  0.0053  -0.0083 124 ALA C O   
10633 C CB  . ALA C 132 ? 0.1634 0.1675 0.1208 0.0132  0.0027  -0.0200 124 ALA C CB  
10634 N N   . LEU C 133 ? 0.1689 0.1708 0.1472 0.0112  0.0108  -0.0117 125 LEU C N   
10635 C CA  . LEU C 133 ? 0.1864 0.1872 0.1762 0.0124  0.0125  -0.0074 125 LEU C CA  
10636 C C   . LEU C 133 ? 0.2005 0.1964 0.1863 0.0129  0.0184  -0.0044 125 LEU C C   
10637 O O   . LEU C 133 ? 0.1594 0.1544 0.1514 0.0156  0.0175  0.0003  125 LEU C O   
10638 C CB  . LEU C 133 ? 0.1728 0.1727 0.1717 0.0112  0.0172  -0.0081 125 LEU C CB  
10639 C CG  . LEU C 133 ? 0.2953 0.2964 0.3112 0.0129  0.0198  -0.0041 125 LEU C CG  
10640 C CD1 . LEU C 133 ? 0.2953 0.3030 0.3230 0.0144  0.0099  -0.0014 125 LEU C CD1 
10641 C CD2 . LEU C 133 ? 0.2569 0.2562 0.2764 0.0110  0.0249  -0.0055 125 LEU C CD2 
10642 N N   . ALA C 134 ? 0.1813 0.1737 0.1578 0.0102  0.0235  -0.0066 126 ALA C N   
10643 C CA  . ALA C 134 ? 0.2234 0.2094 0.1955 0.0095  0.0287  -0.0041 126 ALA C CA  
10644 C C   . ALA C 134 ? 0.1628 0.1496 0.1299 0.0114  0.0254  -0.0003 126 ALA C C   
10645 O O   . ALA C 134 ? 0.2481 0.2300 0.2171 0.0135  0.0268  0.0044  126 ALA C O   
10646 C CB  . ALA C 134 ? 0.1754 0.1584 0.1395 0.0049  0.0325  -0.0072 126 ALA C CB  
10647 N N   . GLU C 135 ? 0.1479 0.1393 0.1072 0.0112  0.0215  -0.0020 127 GLU C N   
10648 C CA  . GLU C 135 ? 0.1923 0.1826 0.1423 0.0132  0.0190  0.0015  127 GLU C CA  
10649 C C   . GLU C 135 ? 0.2068 0.1963 0.1614 0.0170  0.0120  0.0057  127 GLU C C   
10650 O O   . GLU C 135 ? 0.2085 0.1934 0.1599 0.0189  0.0115  0.0113  127 GLU C O   
10651 C CB  . GLU C 135 ? 0.1682 0.1624 0.1080 0.0132  0.0172  -0.0021 127 GLU C CB  
10652 C CG  . GLU C 135 ? 0.1769 0.1678 0.1017 0.0147  0.0179  0.0013  127 GLU C CG  
10653 C CD  . GLU C 135 ? 0.2021 0.1901 0.1185 0.0183  0.0088  0.0027  127 GLU C CD  
10654 O OE1 . GLU C 135 ? 0.2076 0.1975 0.1326 0.0192  0.0012  0.0010  127 GLU C OE1 
10655 O OE2 . GLU C 135 ? 0.2383 0.2212 0.1387 0.0199  0.0089  0.0060  127 GLU C OE2 
10656 N N   . LYS C 136 ? 0.1619 0.1559 0.1258 0.0178  0.0059  0.0035  128 LYS C N   
10657 C CA  . LYS C 136 ? 0.1627 0.1580 0.1353 0.0207  -0.0027 0.0077  128 LYS C CA  
10658 C C   . LYS C 136 ? 0.1781 0.1712 0.1636 0.0231  0.0013  0.0137  128 LYS C C   
10659 O O   . LYS C 136 ? 0.1769 0.1683 0.1635 0.0262  -0.0038 0.0197  128 LYS C O   
10660 C CB  . LYS C 136 ? 0.3122 0.3132 0.2966 0.0199  -0.0086 0.0044  128 LYS C CB  
10661 C CG  . LYS C 136 ? 0.2793 0.2844 0.2808 0.0219  -0.0175 0.0092  128 LYS C CG  
10662 C CD  . LYS C 136 ? 0.2570 0.2680 0.2757 0.0199  -0.0197 0.0068  128 LYS C CD  
10663 C CE  . LYS C 136 ? 0.1914 0.2089 0.2358 0.0217  -0.0245 0.0131  128 LYS C CE  
10664 N NZ  . LYS C 136 ? 0.2270 0.2458 0.2711 0.0228  -0.0399 0.0167  128 LYS C NZ  
10665 N N   . ILE C 137 ? 0.1678 0.1595 0.1617 0.0220  0.0106  0.0120  129 ILE C N   
10666 C CA  . ILE C 137 ? 0.2273 0.2144 0.2325 0.0248  0.0172  0.0164  129 ILE C CA  
10667 C C   . ILE C 137 ? 0.2133 0.1918 0.2078 0.0256  0.0202  0.0204  129 ILE C C   
10668 O O   . ILE C 137 ? 0.2238 0.1993 0.2255 0.0299  0.0190  0.0268  129 ILE C O   
10669 C CB  . ILE C 137 ? 0.2147 0.1984 0.2234 0.0229  0.0274  0.0123  129 ILE C CB  
10670 C CG1 . ILE C 137 ? 0.2995 0.2905 0.3231 0.0232  0.0261  0.0111  129 ILE C CG1 
10671 C CG2 . ILE C 137 ? 0.2271 0.2005 0.2383 0.0251  0.0370  0.0148  129 ILE C CG2 
10672 C CD1 . ILE C 137 ? 0.2622 0.2479 0.2839 0.0211  0.0363  0.0071  129 ILE C CD1 
10673 N N   . LEU C 138 ? 0.1946 0.1692 0.1735 0.0215  0.0241  0.0171  130 LEU C N   
10674 C CA  . LEU C 138 ? 0.2422 0.2080 0.2114 0.0209  0.0280  0.0210  130 LEU C CA  
10675 C C   . LEU C 138 ? 0.2311 0.1967 0.1927 0.0239  0.0207  0.0272  130 LEU C C   
10676 O O   . LEU C 138 ? 0.2253 0.1830 0.1855 0.0262  0.0220  0.0337  130 LEU C O   
10677 C CB  . LEU C 138 ? 0.2368 0.2012 0.1948 0.0149  0.0332  0.0166  130 LEU C CB  
10678 C CG  . LEU C 138 ? 0.2245 0.1854 0.1858 0.0114  0.0393  0.0112  130 LEU C CG  
10679 C CD1 . LEU C 138 ? 0.2355 0.1990 0.1891 0.0054  0.0408  0.0070  130 LEU C CD1 
10680 C CD2 . LEU C 138 ? 0.2421 0.1897 0.2053 0.0120  0.0460  0.0134  130 LEU C CD2 
10681 N N   . ALA C 139 ? 0.2022 0.1743 0.1564 0.0238  0.0131  0.0252  131 ALA C N   
10682 C CA  . ALA C 139 ? 0.2072 0.1770 0.1502 0.0268  0.0049  0.0307  131 ALA C CA  
10683 C C   . ALA C 139 ? 0.2688 0.2381 0.2255 0.0318  -0.0021 0.0376  131 ALA C C   
10684 O O   . ALA C 139 ? 0.2459 0.2082 0.1965 0.0347  -0.0045 0.0452  131 ALA C O   
10685 C CB  . ALA C 139 ? 0.2085 0.1831 0.1407 0.0262  -0.0027 0.0260  131 ALA C CB  
10686 N N   . ALA C 140 ? 0.2215 0.1984 0.1984 0.0330  -0.0052 0.0359  132 ALA C N   
10687 C CA  . ALA C 140 ? 0.2060 0.1855 0.2015 0.0380  -0.0120 0.0429  132 ALA C CA  
10688 C C   . ALA C 140 ? 0.3257 0.2968 0.3282 0.0415  -0.0033 0.0487  132 ALA C C   
10689 O O   . ALA C 140 ? 0.2233 0.1921 0.2322 0.0465  -0.0090 0.0572  132 ALA C O   
10690 C CB  . ALA C 140 ? 0.1933 0.1834 0.2122 0.0380  -0.0141 0.0401  132 ALA C CB  
10691 N N   . GLU C 141 ? 0.2416 0.2068 0.2419 0.0389  0.0099  0.0444  133 GLU C N   
10692 C CA  . GLU C 141 ? 0.2141 0.1684 0.2199 0.0420  0.0189  0.0486  133 GLU C CA  
10693 C C   . GLU C 141 ? 0.2295 0.1722 0.2174 0.0412  0.0199  0.0536  133 GLU C C   
10694 O O   . GLU C 141 ? 0.2422 0.1764 0.2349 0.0461  0.0207  0.0611  133 GLU C O   
10695 C CB  . GLU C 141 ? 0.2069 0.1562 0.2143 0.0389  0.0315  0.0415  133 GLU C CB  
10696 C CG  . GLU C 141 ? 0.3190 0.2532 0.3286 0.0416  0.0417  0.0442  133 GLU C CG  
10697 C CD  . GLU C 141 ? 0.2802 0.2063 0.2857 0.0377  0.0530  0.0362  133 GLU C CD  
10698 O OE1 . GLU C 141 ? 0.3245 0.2574 0.3248 0.0327  0.0523  0.0295  133 GLU C OE1 
10699 O OE2 . GLU C 141 ? 0.2847 0.1960 0.2905 0.0397  0.0620  0.0366  133 GLU C OE2 
10700 N N   . PHE C 142 ? 0.2341 0.1760 0.2025 0.0356  0.0208  0.0501  134 PHE C N   
10701 C CA  . PHE C 142 ? 0.2446 0.1750 0.1976 0.0336  0.0252  0.0547  134 PHE C CA  
10702 C C   . PHE C 142 ? 0.2795 0.2089 0.2160 0.0352  0.0171  0.0612  134 PHE C C   
10703 O O   . PHE C 142 ? 0.3220 0.2402 0.2498 0.0364  0.0190  0.0689  134 PHE C O   
10704 C CB  . PHE C 142 ? 0.2390 0.1677 0.1829 0.0259  0.0341  0.0481  134 PHE C CB  
10705 C CG  . PHE C 142 ? 0.2496 0.1706 0.2018 0.0237  0.0430  0.0439  134 PHE C CG  
10706 C CD1 . PHE C 142 ? 0.3005 0.2061 0.2505 0.0231  0.0494  0.0480  134 PHE C CD1 
10707 C CD2 . PHE C 142 ? 0.2851 0.2119 0.2454 0.0223  0.0448  0.0362  134 PHE C CD2 
10708 C CE1 . PHE C 142 ? 0.2897 0.1848 0.2439 0.0209  0.0573  0.0432  134 PHE C CE1 
10709 C CE2 . PHE C 142 ? 0.2483 0.1651 0.2116 0.0204  0.0529  0.0320  134 PHE C CE2 
10710 C CZ  . PHE C 142 ? 0.2638 0.1642 0.2234 0.0196  0.0590  0.0351  134 PHE C CZ  
10711 N N   . ASN C 143 ? 0.2844 0.2227 0.2138 0.0351  0.0085  0.0584  135 ASN C N   
10712 C CA  . ASN C 143 ? 0.2961 0.2299 0.2036 0.0363  0.0018  0.0638  135 ASN C CA  
10713 C C   . ASN C 143 ? 0.2985 0.2261 0.2087 0.0426  -0.0074 0.0744  135 ASN C C   
10714 O O   . ASN C 143 ? 0.2936 0.2274 0.2242 0.0467  -0.0149 0.0759  135 ASN C O   
10715 C CB  . ASN C 143 ? 0.2736 0.2155 0.1716 0.0355  -0.0065 0.0577  135 ASN C CB  
10716 C CG  . ASN C 143 ? 0.3123 0.2587 0.2034 0.0302  0.0026  0.0490  135 ASN C CG  
10717 O OD1 . ASN C 143 ? 0.3322 0.2760 0.2236 0.0266  0.0140  0.0484  135 ASN C OD1 
10718 N ND2 . ASN C 143 ? 0.2902 0.2428 0.1760 0.0298  -0.0032 0.0425  135 ASN C ND2 
10719 N N   . LYS C 144 ? 0.3154 0.2310 0.2063 0.0434  -0.0066 0.0826  136 LYS C N   
10720 C CA  . LYS C 144 ? 0.3351 0.2430 0.2261 0.0497  -0.0160 0.0941  136 LYS C CA  
10721 C C   . LYS C 144 ? 0.3845 0.2829 0.2432 0.0501  -0.0222 0.1004  136 LYS C C   
10722 O O   . LYS C 144 ? 0.3713 0.2646 0.2088 0.0458  -0.0128 0.0985  136 LYS C O   
10723 C CB  . LYS C 144 ? 0.3703 0.2673 0.2722 0.0517  -0.0067 0.1007  136 LYS C CB  
10724 C CG  . LYS C 144 ? 0.4442 0.3453 0.3725 0.0514  0.0024  0.0945  136 LYS C CG  
10725 C CD  . LYS C 144 ? 0.5318 0.4357 0.4856 0.0593  -0.0040 0.0998  136 LYS C CD  
10726 C CE  . LYS C 144 ? 0.5117 0.4088 0.4836 0.0608  0.0091  0.0979  136 LYS C CE  
10727 N NZ  . LYS C 144 ? 0.5523 0.4532 0.5249 0.0541  0.0196  0.0858  136 LYS C NZ  
10728 N N   . ASP C 145 ? 0.4028 0.2987 0.2582 0.0555  -0.0381 0.1082  137 ASP C N   
10729 C CA  . ASP C 145 ? 0.4225 0.3051 0.2447 0.0572  -0.0455 0.1167  137 ASP C CA  
10730 C C   . ASP C 145 ? 0.4268 0.3071 0.2179 0.0527  -0.0414 0.1098  137 ASP C C   
10731 O O   . ASP C 145 ? 0.5197 0.3868 0.2810 0.0520  -0.0358 0.1153  137 ASP C O   
10732 C CB  . ASP C 145 ? 0.5244 0.3915 0.3393 0.0588  -0.0368 0.1280  137 ASP C CB  
10733 C CG  . ASP C 145 ? 0.5707 0.4379 0.4165 0.0641  -0.0382 0.1343  137 ASP C CG  
10734 O OD1 . ASP C 145 ? 0.5595 0.4370 0.4274 0.0686  -0.0510 0.1347  137 ASP C OD1 
10735 O OD2 . ASP C 145 ? 0.6211 0.4776 0.4699 0.0637  -0.0258 0.1389  137 ASP C OD2 
10736 N N   . GLY C 146 ? 0.5078 0.4001 0.3056 0.0500  -0.0432 0.0981  138 GLY C N   
10737 C CA  . GLY C 146 ? 0.5744 0.4648 0.3459 0.0466  -0.0376 0.0906  138 GLY C CA  
10738 C C   . GLY C 146 ? 0.6340 0.5243 0.4030 0.0421  -0.0169 0.0877  138 GLY C C   
10739 O O   . GLY C 146 ? 0.6788 0.5677 0.4273 0.0401  -0.0100 0.0825  138 GLY C O   
10740 N N   . LEU C 147 ? 0.4943 0.3852 0.2837 0.0406  -0.0068 0.0911  139 LEU C N   
10741 C CA  . LEU C 147 ? 0.3764 0.2694 0.1705 0.0350  0.0109  0.0876  139 LEU C CA  
10742 C C   . LEU C 147 ? 0.3546 0.2627 0.1728 0.0322  0.0127  0.0761  139 LEU C C   
10743 O O   . LEU C 147 ? 0.3631 0.2749 0.2055 0.0316  0.0141  0.0747  139 LEU C O   
10744 C CB  . LEU C 147 ? 0.4654 0.3493 0.2686 0.0339  0.0191  0.0961  139 LEU C CB  
10745 C CG  . LEU C 147 ? 0.4968 0.3638 0.2794 0.0370  0.0175  0.1096  139 LEU C CG  
10746 C CD1 . LEU C 147 ? 0.4505 0.3084 0.2427 0.0336  0.0298  0.1157  139 LEU C CD1 
10747 C CD2 . LEU C 147 ? 0.5494 0.4096 0.2972 0.0368  0.0198  0.1121  139 LEU C CD2 
10748 N N   . ASN C 148 ? 0.3472 0.2622 0.1569 0.0309  0.0130  0.0677  140 ASN C N   
10749 C CA  . ASN C 148 ? 0.3509 0.2792 0.1806 0.0290  0.0121  0.0572  140 ASN C CA  
10750 C C   . ASN C 148 ? 0.3418 0.2755 0.1807 0.0236  0.0264  0.0529  140 ASN C C   
10751 O O   . ASN C 148 ? 0.2938 0.2331 0.1271 0.0218  0.0317  0.0471  140 ASN C O   
10752 C CB  . ASN C 148 ? 0.3812 0.3126 0.1983 0.0307  0.0035  0.0505  140 ASN C CB  
10753 C CG  . ASN C 148 ? 0.5469 0.4729 0.3555 0.0349  -0.0131 0.0547  140 ASN C CG  
10754 O OD1 . ASN C 148 ? 0.5629 0.4883 0.3860 0.0371  -0.0196 0.0610  140 ASN C OD1 
10755 N ND2 . ASN C 148 ? 0.5865 0.5077 0.3716 0.0362  -0.0205 0.0511  140 ASN C ND2 
10756 N N   . ILE C 149 ? 0.3149 0.2463 0.1693 0.0210  0.0321  0.0559  141 ILE C N   
10757 C CA  . ILE C 149 ? 0.2776 0.2135 0.1425 0.0149  0.0432  0.0520  141 ILE C CA  
10758 C C   . ILE C 149 ? 0.3110 0.2589 0.1905 0.0131  0.0417  0.0419  141 ILE C C   
10759 O O   . ILE C 149 ? 0.2715 0.2248 0.1583 0.0081  0.0489  0.0381  141 ILE C O   
10760 C CB  . ILE C 149 ? 0.2794 0.2066 0.1549 0.0120  0.0484  0.0568  141 ILE C CB  
10761 C CG1 . ILE C 149 ? 0.3084 0.2343 0.1993 0.0153  0.0423  0.0553  141 ILE C CG1 
10762 C CG2 . ILE C 149 ? 0.3041 0.2183 0.1650 0.0129  0.0515  0.0677  141 ILE C CG2 
10763 C CD1 . ILE C 149 ? 0.2991 0.2142 0.1998 0.0125  0.0487  0.0577  141 ILE C CD1 
10764 N N   . VAL C 150 ? 0.2837 0.2358 0.1689 0.0168  0.0323  0.0381  142 VAL C N   
10765 C CA  . VAL C 150 ? 0.2475 0.2098 0.1429 0.0156  0.0306  0.0292  142 VAL C CA  
10766 C C   . VAL C 150 ? 0.2725 0.2378 0.1560 0.0188  0.0235  0.0260  142 VAL C C   
10767 O O   . VAL C 150 ? 0.2636 0.2269 0.1452 0.0224  0.0133  0.0275  142 VAL C O   
10768 C CB  . VAL C 150 ? 0.2259 0.1900 0.1393 0.0162  0.0271  0.0267  142 VAL C CB  
10769 C CG1 . VAL C 150 ? 0.1965 0.1697 0.1177 0.0143  0.0266  0.0184  142 VAL C CG1 
10770 C CG2 . VAL C 150 ? 0.2574 0.2142 0.1788 0.0138  0.0338  0.0295  142 VAL C CG2 
10771 N N   . ASP C 151 ? 0.2663 0.2361 0.1431 0.0176  0.0285  0.0213  143 ASP C N   
10772 C CA  . ASP C 151 ? 0.2462 0.2155 0.1079 0.0208  0.0234  0.0174  143 ASP C CA  
10773 C C   . ASP C 151 ? 0.2547 0.2309 0.1175 0.0197  0.0308  0.0112  143 ASP C C   
10774 O O   . ASP C 151 ? 0.2636 0.2388 0.1156 0.0198  0.0400  0.0130  143 ASP C O   
10775 C CB  . ASP C 151 ? 0.2843 0.2430 0.1212 0.0236  0.0228  0.0234  143 ASP C CB  
10776 C CG  . ASP C 151 ? 0.3718 0.3259 0.1878 0.0270  0.0170  0.0188  143 ASP C CG  
10777 O OD1 . ASP C 151 ? 0.3627 0.3213 0.1856 0.0274  0.0106  0.0115  143 ASP C OD1 
10778 O OD2 . ASP C 151 ? 0.3676 0.3119 0.1583 0.0292  0.0192  0.0225  143 ASP C OD2 
10779 N N   . HIS C 152 ? 0.2290 0.2123 0.1057 0.0189  0.0277  0.0048  144 HIS C N   
10780 C CA  . HIS C 152 ? 0.2383 0.2282 0.1177 0.0188  0.0338  -0.0005 144 HIS C CA  
10781 C C   . HIS C 152 ? 0.2343 0.2273 0.1209 0.0199  0.0264  -0.0074 144 HIS C C   
10782 O O   . HIS C 152 ? 0.2383 0.2302 0.1319 0.0196  0.0181  -0.0077 144 HIS C O   
10783 C CB  . HIS C 152 ? 0.2104 0.2076 0.1052 0.0142  0.0424  0.0011  144 HIS C CB  
10784 C CG  . HIS C 152 ? 0.2426 0.2413 0.1533 0.0106  0.0389  0.0009  144 HIS C CG  
10785 N ND1 . HIS C 152 ? 0.1906 0.1840 0.1043 0.0079  0.0403  0.0060  144 HIS C ND1 
10786 C CD2 . HIS C 152 ? 0.2370 0.2398 0.1594 0.0095  0.0350  -0.0037 144 HIS C CD2 
10787 C CE1 . HIS C 152 ? 0.2403 0.2340 0.1658 0.0057  0.0379  0.0038  144 HIS C CE1 
10788 N NE2 . HIS C 152 ? 0.2226 0.2222 0.1531 0.0064  0.0347  -0.0018 144 HIS C NE2 
10789 N N   . TYR C 153 ? 0.2144 0.2111 0.1004 0.0215  0.0302  -0.0123 145 TYR C N   
10790 C CA  . TYR C 153 ? 0.2116 0.2089 0.1016 0.0231  0.0240  -0.0188 145 TYR C CA  
10791 C C   . TYR C 153 ? 0.2252 0.2313 0.1344 0.0205  0.0261  -0.0206 145 TYR C C   
10792 O O   . TYR C 153 ? 0.2324 0.2445 0.1504 0.0178  0.0326  -0.0179 145 TYR C O   
10793 C CB  . TYR C 153 ? 0.2114 0.2036 0.0850 0.0278  0.0263  -0.0235 145 TYR C CB  
10794 C CG  . TYR C 153 ? 0.2637 0.2437 0.1153 0.0300  0.0188  -0.0240 145 TYR C CG  
10795 C CD1 . TYR C 153 ? 0.3778 0.3518 0.2125 0.0308  0.0217  -0.0187 145 TYR C CD1 
10796 C CD2 . TYR C 153 ? 0.2673 0.2411 0.1148 0.0309  0.0079  -0.0293 145 TYR C CD2 
10797 C CE1 . TYR C 153 ? 0.4388 0.4004 0.2511 0.0327  0.0127  -0.0187 145 TYR C CE1 
10798 C CE2 . TYR C 153 ? 0.3245 0.2867 0.1521 0.0320  -0.0014 -0.0299 145 TYR C CE2 
10799 C CZ  . TYR C 153 ? 0.4611 0.4171 0.2703 0.0331  0.0004  -0.0246 145 TYR C CZ  
10800 O OH  . TYR C 153 ? 0.5522 0.4956 0.3396 0.0342  -0.0110 -0.0251 145 TYR C OH  
10801 N N   . THR C 154 ? 0.2302 0.2358 0.1452 0.0210  0.0198  -0.0248 146 THR C N   
10802 C CA  . THR C 154 ? 0.2088 0.2204 0.1384 0.0193  0.0203  -0.0266 146 THR C CA  
10803 C C   . THR C 154 ? 0.2141 0.2242 0.1412 0.0232  0.0189  -0.0320 146 THR C C   
10804 O O   . THR C 154 ? 0.1771 0.1805 0.0995 0.0244  0.0121  -0.0351 146 THR C O   
10805 C CB  . THR C 154 ? 0.1482 0.1587 0.0874 0.0162  0.0152  -0.0256 146 THR C CB  
10806 O OG1 . THR C 154 ? 0.1937 0.2028 0.1332 0.0140  0.0164  -0.0210 146 THR C OG1 
10807 C CG2 . THR C 154 ? 0.1435 0.1583 0.0934 0.0139  0.0165  -0.0263 146 THR C CG2 
10808 N N   . TYR C 155 ? 0.1760 0.1919 0.1075 0.0253  0.0252  -0.0328 147 TYR C N   
10809 C CA  . TYR C 155 ? 0.1824 0.1965 0.1128 0.0302  0.0257  -0.0376 147 TYR C CA  
10810 C C   . TYR C 155 ? 0.1734 0.1932 0.1198 0.0292  0.0235  -0.0377 147 TYR C C   
10811 O O   . TYR C 155 ? 0.1789 0.2071 0.1367 0.0257  0.0252  -0.0341 147 TYR C O   
10812 C CB  . TYR C 155 ? 0.1776 0.1944 0.1029 0.0348  0.0356  -0.0380 147 TYR C CB  
10813 C CG  . TYR C 155 ? 0.2028 0.2115 0.1074 0.0367  0.0389  -0.0378 147 TYR C CG  
10814 C CD1 . TYR C 155 ? 0.2136 0.2090 0.0987 0.0405  0.0351  -0.0431 147 TYR C CD1 
10815 C CD2 . TYR C 155 ? 0.2227 0.2354 0.1256 0.0343  0.0453  -0.0321 147 TYR C CD2 
10816 C CE1 . TYR C 155 ? 0.2343 0.2202 0.0964 0.0422  0.0370  -0.0427 147 TYR C CE1 
10817 C CE2 . TYR C 155 ? 0.2225 0.2262 0.1038 0.0362  0.0484  -0.0310 147 TYR C CE2 
10818 C CZ  . TYR C 155 ? 0.2358 0.2261 0.0957 0.0403  0.0440  -0.0363 147 TYR C CZ  
10819 O OH  . TYR C 155 ? 0.2572 0.2377 0.0964 0.0405  0.0449  -0.0344 147 TYR C OH  
10820 N N   . VAL C 156 ? 0.1952 0.2091 0.1413 0.0318  0.0190  -0.0417 148 VAL C N   
10821 C CA  . VAL C 156 ? 0.2165 0.2330 0.1750 0.0312  0.0157  -0.0411 148 VAL C CA  
10822 C C   . VAL C 156 ? 0.2125 0.2260 0.1720 0.0376  0.0169  -0.0449 148 VAL C C   
10823 O O   . VAL C 156 ? 0.2068 0.2100 0.1548 0.0411  0.0160  -0.0497 148 VAL C O   
10824 C CB  . VAL C 156 ? 0.1557 0.1657 0.1147 0.0272  0.0085  -0.0409 148 VAL C CB  
10825 C CG1 . VAL C 156 ? 0.2071 0.2191 0.1761 0.0258  0.0061  -0.0388 148 VAL C CG1 
10826 C CG2 . VAL C 156 ? 0.1498 0.1605 0.1068 0.0225  0.0081  -0.0378 148 VAL C CG2 
10827 N N   . PHE C 157 ? 0.1514 0.1728 0.1245 0.0394  0.0181  -0.0428 149 PHE C N   
10828 C CA  . PHE C 157 ? 0.1710 0.1890 0.1487 0.0457  0.0179  -0.0453 149 PHE C CA  
10829 C C   . PHE C 157 ? 0.2046 0.2184 0.1876 0.0430  0.0100  -0.0435 149 PHE C C   
10830 O O   . PHE C 157 ? 0.1757 0.1957 0.1654 0.0381  0.0071  -0.0390 149 PHE C O   
10831 C CB  . PHE C 157 ? 0.1586 0.1891 0.1507 0.0505  0.0244  -0.0430 149 PHE C CB  
10832 C CG  . PHE C 157 ? 0.1870 0.2187 0.1732 0.0559  0.0350  -0.0453 149 PHE C CG  
10833 C CD1 . PHE C 157 ? 0.1797 0.2018 0.1458 0.0551  0.0371  -0.0486 149 PHE C CD1 
10834 C CD2 . PHE C 157 ? 0.2116 0.2539 0.2124 0.0621  0.0430  -0.0437 149 PHE C CD2 
10835 C CE1 . PHE C 157 ? 0.1947 0.2155 0.1509 0.0602  0.0477  -0.0505 149 PHE C CE1 
10836 C CE2 . PHE C 157 ? 0.2444 0.2870 0.2389 0.0676  0.0552  -0.0454 149 PHE C CE2 
10837 C CZ  . PHE C 157 ? 0.2215 0.2522 0.1913 0.0666  0.0579  -0.0490 149 PHE C CZ  
10838 N N   . MET C 158 ? 0.1843 0.1859 0.1628 0.0458  0.0067  -0.0470 150 MET C N   
10839 C CA  . MET C 158 ? 0.2283 0.2248 0.2109 0.0429  0.0002  -0.0444 150 MET C CA  
10840 C C   . MET C 158 ? 0.2120 0.1982 0.1959 0.0490  -0.0014 -0.0470 150 MET C C   
10841 O O   . MET C 158 ? 0.2657 0.2451 0.2435 0.0545  0.0019  -0.0525 150 MET C O   
10842 C CB  . MET C 158 ? 0.2447 0.2353 0.2211 0.0358  -0.0035 -0.0438 150 MET C CB  
10843 C CG  . MET C 158 ? 0.3424 0.3211 0.3109 0.0353  -0.0065 -0.0483 150 MET C CG  
10844 S SD  . MET C 158 ? 0.3063 0.2847 0.2752 0.0269  -0.0097 -0.0452 150 MET C SD  
10845 C CE  . MET C 158 ? 0.2028 0.1789 0.1790 0.0238  -0.0110 -0.0397 150 MET C CE  
10846 N N   . GLY C 159 ? 0.1715 0.1553 0.1618 0.0484  -0.0059 -0.0429 151 GLY C N   
10847 C CA  . GLY C 159 ? 0.2146 0.1886 0.2082 0.0545  -0.0077 -0.0438 151 GLY C CA  
10848 C C   . GLY C 159 ? 0.2110 0.1710 0.2006 0.0502  -0.0132 -0.0425 151 GLY C C   
10849 O O   . GLY C 159 ? 0.2324 0.1912 0.2178 0.0428  -0.0149 -0.0411 151 GLY C O   
10850 N N   . ASP C 160 ? 0.1985 0.1476 0.1908 0.0554  -0.0152 -0.0427 152 ASP C N   
10851 C CA  . ASP C 160 ? 0.2267 0.1605 0.2161 0.0515  -0.0196 -0.0412 152 ASP C CA  
10852 C C   . ASP C 160 ? 0.2669 0.2036 0.2568 0.0448  -0.0222 -0.0333 152 ASP C C   
10853 O O   . ASP C 160 ? 0.2030 0.1323 0.1898 0.0383  -0.0232 -0.0319 152 ASP C O   
10854 C CB  . ASP C 160 ? 0.2830 0.2041 0.2757 0.0588  -0.0211 -0.0415 152 ASP C CB  
10855 C CG  . ASP C 160 ? 0.4339 0.3440 0.4212 0.0646  -0.0184 -0.0505 152 ASP C CG  
10856 O OD1 . ASP C 160 ? 0.4832 0.3892 0.4614 0.0604  -0.0184 -0.0564 152 ASP C OD1 
10857 O OD2 . ASP C 160 ? 0.4874 0.3916 0.4788 0.0736  -0.0166 -0.0518 152 ASP C OD2 
10858 N N   . GLY C 161 ? 0.1992 0.1456 0.1930 0.0464  -0.0232 -0.0280 153 GLY C N   
10859 C CA  . GLY C 161 ? 0.1919 0.1382 0.1814 0.0404  -0.0255 -0.0211 153 GLY C CA  
10860 C C   . GLY C 161 ? 0.1929 0.1436 0.1769 0.0328  -0.0223 -0.0220 153 GLY C C   
10861 O O   . GLY C 161 ? 0.2143 0.1584 0.1932 0.0273  -0.0215 -0.0184 153 GLY C O   
10862 N N   . OCS C 162 ? 0.1789 0.1406 0.1646 0.0331  -0.0194 -0.0262 154 OCS C N   
10863 C CA  . OCS C 162 ? 0.1975 0.1631 0.1793 0.0271  -0.0164 -0.0271 154 OCS C CA  
10864 C CB  . OCS C 162 ? 0.2139 0.1904 0.1971 0.0288  -0.0135 -0.0313 154 OCS C CB  
10865 S SG  . OCS C 162 ? 0.2290 0.2191 0.2177 0.0312  -0.0135 -0.0289 154 OCS C SG  
10866 C C   . OCS C 162 ? 0.2264 0.1828 0.2076 0.0236  -0.0160 -0.0285 154 OCS C C   
10867 O O   . OCS C 162 ? 0.1739 0.1295 0.1540 0.0181  -0.0139 -0.0257 154 OCS C O   
10868 O OD1 . OCS C 162 ? 0.2981 0.2963 0.2894 0.0341  -0.0093 -0.0328 154 OCS C OD1 
10869 O OD2 . OCS C 162 ? 0.2199 0.2128 0.2044 0.0252  -0.0139 -0.0255 154 OCS C OD2 
10870 O OD3 . OCS C 162 ? 0.4900 0.4787 0.4845 0.0361  -0.0171 -0.0265 154 OCS C OD3 
10871 N N   . LEU C 163 ? 0.2219 0.1712 0.2047 0.0267  -0.0180 -0.0330 155 LEU C N   
10872 C CA  . LEU C 163 ? 0.1789 0.1197 0.1630 0.0226  -0.0197 -0.0350 155 LEU C CA  
10873 C C   . LEU C 163 ? 0.2181 0.1487 0.2052 0.0188  -0.0204 -0.0296 155 LEU C C   
10874 O O   . LEU C 163 ? 0.2314 0.1587 0.2233 0.0132  -0.0204 -0.0284 155 LEU C O   
10875 C CB  . LEU C 163 ? 0.1896 0.1226 0.1712 0.0268  -0.0225 -0.0422 155 LEU C CB  
10876 C CG  . LEU C 163 ? 0.2422 0.1824 0.2180 0.0296  -0.0209 -0.0477 155 LEU C CG  
10877 C CD1 . LEU C 163 ? 0.2422 0.1709 0.2111 0.0349  -0.0226 -0.0553 155 LEU C CD1 
10878 C CD2 . LEU C 163 ? 0.2385 0.1842 0.2145 0.0236  -0.0219 -0.0473 155 LEU C CD2 
10879 N N   . MET C 164 ? 0.1926 0.1180 0.1779 0.0221  -0.0211 -0.0258 156 MET C N   
10880 C CA  . MET C 164 ? 0.2020 0.1163 0.1875 0.0186  -0.0209 -0.0194 156 MET C CA  
10881 C C   . MET C 164 ? 0.2000 0.1183 0.1823 0.0131  -0.0160 -0.0136 156 MET C C   
10882 O O   . MET C 164 ? 0.2032 0.1141 0.1876 0.0082  -0.0130 -0.0089 156 MET C O   
10883 C CB  . MET C 164 ? 0.2129 0.1198 0.1957 0.0241  -0.0237 -0.0159 156 MET C CB  
10884 C CG  . MET C 164 ? 0.2256 0.1201 0.2120 0.0286  -0.0270 -0.0198 156 MET C CG  
10885 S SD  . MET C 164 ? 0.2680 0.1531 0.2536 0.0361  -0.0304 -0.0142 156 MET C SD  
10886 C CE  . MET C 164 ? 0.2774 0.1755 0.2675 0.0458  -0.0308 -0.0201 156 MET C CE  
10887 N N   . GLU C 165 ? 0.1881 0.1169 0.1654 0.0138  -0.0144 -0.0137 157 GLU C N   
10888 C CA  . GLU C 165 ? 0.2134 0.1433 0.1841 0.0094  -0.0093 -0.0091 157 GLU C CA  
10889 C C   . GLU C 165 ? 0.1893 0.1219 0.1674 0.0046  -0.0042 -0.0094 157 GLU C C   
10890 O O   . GLU C 165 ? 0.1921 0.1320 0.1775 0.0048  -0.0057 -0.0143 157 GLU C O   
10891 C CB  . GLU C 165 ? 0.1802 0.1198 0.1446 0.0108  -0.0098 -0.0103 157 GLU C CB  
10892 C CG  . GLU C 165 ? 0.2164 0.1542 0.1743 0.0141  -0.0151 -0.0074 157 GLU C CG  
10893 C CD  . GLU C 165 ? 0.2034 0.1291 0.1479 0.0114  -0.0144 -0.0005 157 GLU C CD  
10894 O OE1 . GLU C 165 ? 0.2141 0.1327 0.1540 0.0072  -0.0076 0.0023  157 GLU C OE1 
10895 O OE2 . GLU C 165 ? 0.2193 0.1425 0.1577 0.0139  -0.0206 0.0028  157 GLU C OE2 
10896 N N   . GLY C 166 ? 0.2087 0.1581 0.1042 -0.0158 -0.0358 0.0076  158 GLY C N   
10897 C CA  . GLY C 166 ? 0.2017 0.1481 0.0987 -0.0239 -0.0300 0.0003  158 GLY C CA  
10898 C C   . GLY C 166 ? 0.2185 0.1787 0.1262 -0.0258 -0.0285 -0.0065 158 GLY C C   
10899 O O   . GLY C 166 ? 0.1972 0.1570 0.1114 -0.0277 -0.0246 -0.0118 158 GLY C O   
10900 N N   . VAL C 167 ? 0.2020 0.1752 0.1122 -0.0253 -0.0312 -0.0063 159 VAL C N   
10901 C CA  . VAL C 167 ? 0.1956 0.1785 0.1155 -0.0279 -0.0277 -0.0127 159 VAL C CA  
10902 C C   . VAL C 167 ? 0.1963 0.1799 0.1264 -0.0210 -0.0272 -0.0144 159 VAL C C   
10903 O O   . VAL C 167 ? 0.2010 0.1876 0.1382 -0.0222 -0.0232 -0.0185 159 VAL C O   
10904 C CB  . VAL C 167 ? 0.1665 0.1628 0.0866 -0.0309 -0.0292 -0.0137 159 VAL C CB  
10905 C CG1 . VAL C 167 ? 0.1683 0.1728 0.0927 -0.0231 -0.0348 -0.0103 159 VAL C CG1 
10906 C CG2 . VAL C 167 ? 0.1564 0.1584 0.0849 -0.0358 -0.0227 -0.0207 159 VAL C CG2 
10907 N N   . SER C 168 ? 0.2129 0.1933 0.1435 -0.0136 -0.0307 -0.0112 160 SER C N   
10908 C CA  . SER C 168 ? 0.1949 0.1755 0.1330 -0.0083 -0.0296 -0.0136 160 SER C CA  
10909 C C   . SER C 168 ? 0.2039 0.1777 0.1416 -0.0109 -0.0265 -0.0167 160 SER C C   
10910 O O   . SER C 168 ? 0.1895 0.1681 0.1333 -0.0098 -0.0247 -0.0197 160 SER C O   
10911 C CB  . SER C 168 ? 0.2173 0.1953 0.1563 -0.0004 -0.0327 -0.0106 160 SER C CB  
10912 O OG  . SER C 168 ? 0.2519 0.2157 0.1849 0.0005  -0.0323 -0.0087 160 SER C OG  
10913 N N   . HIS C 169 ? 0.1621 0.1255 0.0926 -0.0147 -0.0258 -0.0158 161 HIS C N   
10914 C CA  . HIS C 169 ? 0.1817 0.1412 0.1127 -0.0190 -0.0225 -0.0200 161 HIS C CA  
10915 C C   . HIS C 169 ? 0.1618 0.1307 0.0989 -0.0230 -0.0198 -0.0233 161 HIS C C   
10916 O O   . HIS C 169 ? 0.1817 0.1564 0.1254 -0.0222 -0.0186 -0.0265 161 HIS C O   
10917 C CB  . HIS C 169 ? 0.1885 0.1346 0.1103 -0.0238 -0.0209 -0.0185 161 HIS C CB  
10918 C CG  . HIS C 169 ? 0.1827 0.1274 0.1055 -0.0309 -0.0167 -0.0238 161 HIS C CG  
10919 N ND1 . HIS C 169 ? 0.2059 0.1507 0.1328 -0.0313 -0.0154 -0.0289 161 HIS C ND1 
10920 C CD2 . HIS C 169 ? 0.1779 0.1227 0.0987 -0.0385 -0.0133 -0.0256 161 HIS C CD2 
10921 C CE1 . HIS C 169 ? 0.2463 0.1930 0.1749 -0.0386 -0.0119 -0.0334 161 HIS C CE1 
10922 N NE2 . HIS C 169 ? 0.1777 0.1237 0.1030 -0.0428 -0.0102 -0.0314 161 HIS C NE2 
10923 N N   . GLU C 170 ? 0.1716 0.1427 0.1068 -0.0273 -0.0184 -0.0226 162 GLU C N   
10924 C CA  . GLU C 170 ? 0.1848 0.1626 0.1268 -0.0310 -0.0140 -0.0261 162 GLU C CA  
10925 C C   . GLU C 170 ? 0.1858 0.1720 0.1375 -0.0255 -0.0134 -0.0263 162 GLU C C   
10926 O O   . GLU C 170 ? 0.1421 0.1331 0.1015 -0.0243 -0.0110 -0.0279 162 GLU C O   
10927 C CB  . GLU C 170 ? 0.1858 0.1640 0.1231 -0.0374 -0.0116 -0.0264 162 GLU C CB  
10928 C CG  . GLU C 170 ? 0.1735 0.1433 0.0996 -0.0440 -0.0109 -0.0256 162 GLU C CG  
10929 C CD  . GLU C 170 ? 0.1767 0.1487 0.0959 -0.0511 -0.0089 -0.0262 162 GLU C CD  
10930 O OE1 . GLU C 170 ? 0.2164 0.1820 0.1229 -0.0555 -0.0098 -0.0233 162 GLU C OE1 
10931 O OE2 . GLU C 170 ? 0.2155 0.1950 0.1409 -0.0527 -0.0058 -0.0297 162 GLU C OE2 
10932 N N   . ALA C 171 ? 0.1763 0.1651 0.1279 -0.0218 -0.0155 -0.0243 163 ALA C N   
10933 C CA  . ALA C 171 ? 0.1640 0.1591 0.1236 -0.0175 -0.0135 -0.0242 163 ALA C CA  
10934 C C   . ALA C 171 ? 0.1925 0.1895 0.1547 -0.0118 -0.0152 -0.0234 163 ALA C C   
10935 O O   . ALA C 171 ? 0.1634 0.1652 0.1317 -0.0091 -0.0127 -0.0228 163 ALA C O   
10936 C CB  . ALA C 171 ? 0.1683 0.1667 0.1274 -0.0163 -0.0146 -0.0233 163 ALA C CB  
10937 N N   . CYS C 172 ? 0.1851 0.1784 0.1424 -0.0098 -0.0190 -0.0234 164 CYS C N   
10938 C CA  . CYS C 172 ? 0.1734 0.1695 0.1319 -0.0058 -0.0202 -0.0242 164 CYS C CA  
10939 C C   . CYS C 172 ? 0.1568 0.1560 0.1171 -0.0084 -0.0198 -0.0266 164 CYS C C   
10940 O O   . CYS C 172 ? 0.1499 0.1571 0.1130 -0.0056 -0.0205 -0.0270 164 CYS C O   
10941 C CB  . CYS C 172 ? 0.1632 0.1534 0.1169 -0.0034 -0.0228 -0.0247 164 CYS C CB  
10942 S SG  . CYS C 172 ? 0.1839 0.1759 0.1389 0.0014  -0.0238 -0.0222 164 CYS C SG  
10943 N N   . SER C 173 ? 0.1555 0.1501 0.1141 -0.0141 -0.0187 -0.0284 165 SER C N   
10944 C CA  . SER C 173 ? 0.1387 0.1392 0.1015 -0.0173 -0.0176 -0.0316 165 SER C CA  
10945 C C   . SER C 173 ? 0.1215 0.1326 0.0938 -0.0142 -0.0157 -0.0297 165 SER C C   
10946 O O   . SER C 173 ? 0.1399 0.1618 0.1172 -0.0114 -0.0170 -0.0300 165 SER C O   
10947 C CB  . SER C 173 ? 0.1547 0.1477 0.1140 -0.0248 -0.0153 -0.0339 165 SER C CB  
10948 O OG  . SER C 173 ? 0.2006 0.2013 0.1661 -0.0285 -0.0136 -0.0379 165 SER C OG  
10949 N N   . LEU C 174 ? 0.2173 0.2257 0.1919 -0.0144 -0.0122 -0.0278 166 LEU C N   
10950 C CA  . LEU C 174 ? 0.1773 0.1922 0.1617 -0.0111 -0.0082 -0.0256 166 LEU C CA  
10951 C C   . LEU C 174 ? 0.1369 0.1568 0.1231 -0.0035 -0.0093 -0.0212 166 LEU C C   
10952 O O   . LEU C 174 ? 0.1520 0.1800 0.1457 0.0014  -0.0081 -0.0181 166 LEU C O   
10953 C CB  . LEU C 174 ? 0.1164 0.1250 0.1017 -0.0148 -0.0027 -0.0262 166 LEU C CB  
10954 C CG  . LEU C 174 ? 0.2055 0.2167 0.2017 -0.0123 0.0041  -0.0249 166 LEU C CG  
10955 C CD1 . LEU C 174 ? 0.2214 0.2398 0.2265 -0.0120 0.0055  -0.0263 166 LEU C CD1 
10956 C CD2 . LEU C 174 ? 0.2085 0.2127 0.2035 -0.0184 0.0102  -0.0279 166 LEU C CD2 
10957 N N   . ALA C 175 ? 0.1224 0.1383 0.1022 -0.0020 -0.0113 -0.0202 167 ALA C N   
10958 C CA  . ALA C 175 ? 0.1293 0.1496 0.1091 0.0043  -0.0117 -0.0164 167 ALA C CA  
10959 C C   . ALA C 175 ? 0.1520 0.1821 0.1309 0.0071  -0.0160 -0.0161 167 ALA C C   
10960 O O   . ALA C 175 ? 0.1873 0.2247 0.1681 0.0126  -0.0158 -0.0115 167 ALA C O   
10961 C CB  . ALA C 175 ? 0.1759 0.1913 0.1499 0.0045  -0.0128 -0.0169 167 ALA C CB  
10962 N N   . GLY C 176 ? 0.1342 0.1645 0.1094 0.0029  -0.0194 -0.0212 168 GLY C N   
10963 C CA  . GLY C 176 ? 0.1728 0.2146 0.1472 0.0035  -0.0232 -0.0231 168 GLY C CA  
10964 C C   . GLY C 176 ? 0.1623 0.2169 0.1457 0.0051  -0.0234 -0.0213 168 GLY C C   
10965 O O   . GLY C 176 ? 0.1800 0.2487 0.1647 0.0093  -0.0263 -0.0187 168 GLY C O   
10966 N N   . THR C 177 ? 0.1685 0.2198 0.1585 0.0021  -0.0201 -0.0225 169 THR C N   
10967 C CA  . THR C 177 ? 0.1594 0.2233 0.1609 0.0046  -0.0192 -0.0208 169 THR C CA  
10968 C C   . THR C 177 ? 0.1733 0.2414 0.1805 0.0139  -0.0171 -0.0120 169 THR C C   
10969 O O   . THR C 177 ? 0.1335 0.2170 0.1478 0.0196  -0.0193 -0.0080 169 THR C O   
10970 C CB  . THR C 177 ? 0.2100 0.2674 0.2172 -0.0011 -0.0144 -0.0244 169 THR C CB  
10971 O OG1 . THR C 177 ? 0.1787 0.2324 0.1801 -0.0096 -0.0158 -0.0315 169 THR C OG1 
10972 C CG2 . THR C 177 ? 0.2408 0.3113 0.2627 0.0025  -0.0121 -0.0227 169 THR C CG2 
10973 N N   . LEU C 178 ? 0.1322 0.1873 0.1364 0.0155  -0.0127 -0.0087 170 LEU C N   
10974 C CA  . LEU C 178 ? 0.1512 0.2058 0.1602 0.0235  -0.0084 -0.0004 170 LEU C CA  
10975 C C   . LEU C 178 ? 0.1823 0.2410 0.1833 0.0288  -0.0115 0.0050  170 LEU C C   
10976 O O   . LEU C 178 ? 0.1686 0.2258 0.1717 0.0356  -0.0075 0.0132  170 LEU C O   
10977 C CB  . LEU C 178 ? 0.1703 0.2092 0.1811 0.0209  -0.0002 -0.0008 170 LEU C CB  
10978 C CG  . LEU C 178 ? 0.2163 0.2521 0.2355 0.0161  0.0046  -0.0055 170 LEU C CG  
10979 C CD1 . LEU C 178 ? 0.2392 0.2610 0.2579 0.0113  0.0124  -0.0081 170 LEU C CD1 
10980 C CD2 . LEU C 178 ? 0.2320 0.2772 0.2649 0.0229  0.0073  -0.0012 170 LEU C CD2 
10981 N N   . GLY C 179 ? 0.1955 0.2585 0.1871 0.0255  -0.0174 0.0006  171 GLY C N   
10982 C CA  . GLY C 179 ? 0.1784 0.2482 0.1617 0.0297  -0.0204 0.0046  171 GLY C CA  
10983 C C   . GLY C 179 ? 0.1963 0.2548 0.1753 0.0324  -0.0150 0.0094  171 GLY C C   
10984 O O   . GLY C 179 ? 0.2200 0.2821 0.1965 0.0387  -0.0136 0.0175  171 GLY C O   
10985 N N   . LEU C 180 ? 0.1694 0.2150 0.1471 0.0274  -0.0118 0.0045  172 LEU C N   
10986 C CA  . LEU C 180 ? 0.1734 0.2093 0.1496 0.0285  -0.0057 0.0074  172 LEU C CA  
10987 C C   . LEU C 180 ? 0.1874 0.2260 0.1539 0.0291  -0.0077 0.0069  172 LEU C C   
10988 O O   . LEU C 180 ? 0.1544 0.1887 0.1177 0.0254  -0.0083 0.0011  172 LEU C O   
10989 C CB  . LEU C 180 ? 0.1964 0.2220 0.1758 0.0225  -0.0023 0.0019  172 LEU C CB  
10990 C CG  . LEU C 180 ? 0.1529 0.1748 0.1407 0.0201  0.0011  0.0008  172 LEU C CG  
10991 C CD1 . LEU C 180 ? 0.1519 0.1657 0.1399 0.0134  0.0040  -0.0047 172 LEU C CD1 
10992 C CD2 . LEU C 180 ? 0.1285 0.1488 0.1236 0.0255  0.0078  0.0078  172 LEU C CD2 
10993 N N   . GLY C 181 ? 0.1522 0.1984 0.1140 0.0344  -0.0083 0.0136  173 GLY C N   
10994 C CA  . GLY C 181 ? 0.1984 0.2494 0.1497 0.0346  -0.0101 0.0128  173 GLY C CA  
10995 C C   . GLY C 181 ? 0.2012 0.2430 0.1497 0.0336  -0.0037 0.0127  173 GLY C C   
10996 O O   . GLY C 181 ? 0.2383 0.2828 0.1790 0.0326  -0.0042 0.0097  173 GLY C O   
10997 N N   . LYS C 182 ? 0.1614 0.1930 0.1167 0.0331  0.0030  0.0146  174 LYS C N   
10998 C CA  . LYS C 182 ? 0.1502 0.1751 0.1047 0.0309  0.0095  0.0132  174 LYS C CA  
10999 C C   . LYS C 182 ? 0.1741 0.1960 0.1336 0.0255  0.0085  0.0043  174 LYS C C   
11000 O O   . LYS C 182 ? 0.1843 0.2033 0.1457 0.0230  0.0134  0.0018  174 LYS C O   
11001 C CB  . LYS C 182 ? 0.1749 0.1910 0.1333 0.0327  0.0188  0.0203  174 LYS C CB  
11002 C CG  . LYS C 182 ? 0.2262 0.2446 0.1781 0.0396  0.0205  0.0315  174 LYS C CG  
11003 C CD  . LYS C 182 ? 0.3074 0.3135 0.2642 0.0419  0.0313  0.0391  174 LYS C CD  
11004 C CE  . LYS C 182 ? 0.3010 0.3041 0.2482 0.0460  0.0373  0.0486  174 LYS C CE  
11005 N NZ  . LYS C 182 ? 0.3176 0.3078 0.2695 0.0507  0.0474  0.0588  174 LYS C NZ  
11006 N N   . LEU C 183 ? 0.1568 0.1805 0.1184 0.0236  0.0022  -0.0003 175 LEU C N   
11007 C CA  . LEU C 183 ? 0.1273 0.1489 0.0919 0.0197  -0.0000 -0.0071 175 LEU C CA  
11008 C C   . LEU C 183 ? 0.2009 0.2258 0.1605 0.0204  -0.0043 -0.0115 175 LEU C C   
11009 O O   . LEU C 183 ? 0.1956 0.2236 0.1508 0.0210  -0.0086 -0.0125 175 LEU C O   
11010 C CB  . LEU C 183 ? 0.1221 0.1415 0.0905 0.0170  -0.0031 -0.0088 175 LEU C CB  
11011 C CG  . LEU C 183 ? 0.1622 0.1796 0.1316 0.0136  -0.0065 -0.0140 175 LEU C CG  
11012 C CD1 . LEU C 183 ? 0.2226 0.2400 0.1966 0.0111  -0.0027 -0.0156 175 LEU C CD1 
11013 C CD2 . LEU C 183 ? 0.1554 0.1703 0.1259 0.0106  -0.0090 -0.0150 175 LEU C CD2 
11014 N N   . ILE C 184 ? 0.1313 0.1563 0.0925 0.0201  -0.0024 -0.0148 176 ILE C N   
11015 C CA  . ILE C 184 ? 0.1313 0.1581 0.0894 0.0213  -0.0045 -0.0195 176 ILE C CA  
11016 C C   . ILE C 184 ? 0.1828 0.2083 0.1475 0.0210  -0.0058 -0.0233 176 ILE C C   
11017 O O   . ILE C 184 ? 0.1834 0.2115 0.1541 0.0202  -0.0029 -0.0235 176 ILE C O   
11018 C CB  . ILE C 184 ? 0.1536 0.1842 0.1071 0.0227  0.0002  -0.0192 176 ILE C CB  
11019 C CG1 . ILE C 184 ? 0.1914 0.2250 0.1366 0.0239  0.0002  -0.0138 176 ILE C CG1 
11020 C CG2 . ILE C 184 ? 0.1550 0.1869 0.1067 0.0236  -0.0004 -0.0257 176 ILE C CG2 
11021 C CD1 . ILE C 184 ? 0.1981 0.2348 0.1363 0.0250  0.0057  -0.0114 176 ILE C CD1 
11022 N N   . VAL C 185 ? 0.1667 0.1887 0.1304 0.0217  -0.0100 -0.0262 177 VAL C N   
11023 C CA  . VAL C 185 ? 0.1655 0.1855 0.1346 0.0229  -0.0124 -0.0278 177 VAL C CA  
11024 C C   . VAL C 185 ? 0.1918 0.2112 0.1618 0.0266  -0.0112 -0.0320 177 VAL C C   
11025 O O   . VAL C 185 ? 0.1972 0.2133 0.1613 0.0264  -0.0105 -0.0350 177 VAL C O   
11026 C CB  . VAL C 185 ? 0.2320 0.2454 0.1989 0.0211  -0.0167 -0.0268 177 VAL C CB  
11027 C CG1 . VAL C 185 ? 0.1980 0.2085 0.1686 0.0238  -0.0194 -0.0267 177 VAL C CG1 
11028 C CG2 . VAL C 185 ? 0.2279 0.2422 0.1949 0.0172  -0.0168 -0.0237 177 VAL C CG2 
11029 N N   . LEU C 186 ? 0.1774 0.2010 0.1555 0.0296  -0.0104 -0.0329 178 LEU C N   
11030 C CA  . LEU C 186 ? 0.1746 0.1965 0.1567 0.0344  -0.0091 -0.0366 178 LEU C CA  
11031 C C   . LEU C 186 ? 0.1753 0.1929 0.1620 0.0380  -0.0136 -0.0341 178 LEU C C   
11032 O O   . LEU C 186 ? 0.1841 0.2093 0.1771 0.0388  -0.0165 -0.0311 178 LEU C O   
11033 C CB  . LEU C 186 ? 0.2297 0.2613 0.2194 0.0366  -0.0044 -0.0394 178 LEU C CB  
11034 C CG  . LEU C 186 ? 0.2149 0.2484 0.1980 0.0343  0.0014  -0.0424 178 LEU C CG  
11035 C CD1 . LEU C 186 ? 0.1934 0.2295 0.1712 0.0298  0.0025  -0.0382 178 LEU C CD1 
11036 C CD2 . LEU C 186 ? 0.2658 0.3064 0.2566 0.0369  0.0071  -0.0470 178 LEU C CD2 
11037 N N   . TYR C 187 ? 0.1796 0.1855 0.1625 0.0396  -0.0138 -0.0353 179 TYR C N   
11038 C CA  . TYR C 187 ? 0.1987 0.1967 0.1834 0.0431  -0.0173 -0.0313 179 TYR C CA  
11039 C C   . TYR C 187 ? 0.2204 0.2172 0.2144 0.0515  -0.0150 -0.0324 179 TYR C C   
11040 O O   . TYR C 187 ? 0.2037 0.1950 0.1979 0.0529  -0.0095 -0.0383 179 TYR C O   
11041 C CB  . TYR C 187 ? 0.1649 0.1488 0.1400 0.0390  -0.0174 -0.0318 179 TYR C CB  
11042 C CG  . TYR C 187 ? 0.2245 0.1942 0.1995 0.0431  -0.0177 -0.0291 179 TYR C CG  
11043 C CD1 . TYR C 187 ? 0.2243 0.1955 0.2038 0.0485  -0.0218 -0.0220 179 TYR C CD1 
11044 C CD2 . TYR C 187 ? 0.2888 0.2435 0.2583 0.0409  -0.0135 -0.0335 179 TYR C CD2 
11045 C CE1 . TYR C 187 ? 0.3141 0.2706 0.2924 0.0533  -0.0217 -0.0175 179 TYR C CE1 
11046 C CE2 . TYR C 187 ? 0.2879 0.2262 0.2568 0.0445  -0.0121 -0.0305 179 TYR C CE2 
11047 C CZ  . TYR C 187 ? 0.3038 0.2423 0.2768 0.0513  -0.0162 -0.0216 179 TYR C CZ  
11048 O OH  . TYR C 187 ? 0.3378 0.2586 0.3094 0.0560  -0.0144 -0.0167 179 TYR C OH  
11049 N N   . ASP C 188 ? 0.2116 0.2153 0.2138 0.0571  -0.0191 -0.0271 180 ASP C N   
11050 C CA  . ASP C 188 ? 0.2098 0.2145 0.2236 0.0671  -0.0178 -0.0263 180 ASP C CA  
11051 C C   . ASP C 188 ? 0.2110 0.1962 0.2209 0.0715  -0.0175 -0.0225 180 ASP C C   
11052 O O   . ASP C 188 ? 0.2494 0.2320 0.2578 0.0744  -0.0227 -0.0144 180 ASP C O   
11053 C CB  . ASP C 188 ? 0.1797 0.2035 0.2043 0.0713  -0.0233 -0.0217 180 ASP C CB  
11054 C CG  . ASP C 188 ? 0.2717 0.2996 0.3109 0.0834  -0.0228 -0.0196 180 ASP C CG  
11055 O OD1 . ASP C 188 ? 0.2781 0.2961 0.3212 0.0879  -0.0159 -0.0243 180 ASP C OD1 
11056 O OD2 . ASP C 188 ? 0.2499 0.2920 0.2970 0.0886  -0.0292 -0.0135 180 ASP C OD2 
11057 N N   . ASP C 189 ? 0.2436 0.2143 0.2508 0.0711  -0.0104 -0.0288 181 ASP C N   
11058 C CA  . ASP C 189 ? 0.2788 0.2273 0.2818 0.0736  -0.0071 -0.0273 181 ASP C CA  
11059 C C   . ASP C 189 ? 0.2687 0.2136 0.2853 0.0860  -0.0033 -0.0258 181 ASP C C   
11060 O O   . ASP C 189 ? 0.2719 0.2105 0.2930 0.0878  0.0050  -0.0339 181 ASP C O   
11061 C CB  . ASP C 189 ? 0.2788 0.2155 0.2719 0.0647  -0.0009 -0.0367 181 ASP C CB  
11062 C CG  . ASP C 189 ? 0.3764 0.2887 0.3648 0.0649  0.0043  -0.0370 181 ASP C CG  
11063 O OD1 . ASP C 189 ? 0.3663 0.2679 0.3609 0.0744  0.0053  -0.0304 181 ASP C OD1 
11064 O OD2 . ASP C 189 ? 0.4540 0.3583 0.4329 0.0555  0.0078  -0.0441 181 ASP C OD2 
11065 N N   . ASN C 190 ? 0.2707 0.2205 0.2940 0.0949  -0.0092 -0.0153 182 ASN C N   
11066 C CA  . ASN C 190 ? 0.3763 0.3266 0.4153 0.1090  -0.0069 -0.0117 182 ASN C CA  
11067 C C   . ASN C 190 ? 0.5173 0.4414 0.5541 0.1162  -0.0029 -0.0052 182 ASN C C   
11068 O O   . ASN C 190 ? 0.5434 0.4678 0.5901 0.1293  -0.0052 0.0048  182 ASN C O   
11069 C CB  . ASN C 190 ? 0.3875 0.3633 0.4373 0.1156  -0.0161 -0.0039 182 ASN C CB  
11070 C CG  . ASN C 190 ? 0.4718 0.4505 0.5113 0.1129  -0.0257 0.0065  182 ASN C CG  
11071 O OD1 . ASN C 190 ? 0.4551 0.4137 0.4812 0.1091  -0.0251 0.0102  182 ASN C OD1 
11072 N ND2 . ASN C 190 ? 0.4915 0.4960 0.5372 0.1137  -0.0340 0.0103  182 ASN C ND2 
11073 N N   . ASN C 191 ? 0.5674 0.4689 0.5918 0.1079  0.0036  -0.0106 183 ASN C N   
11074 C CA  . ASN C 191 ? 0.6224 0.4952 0.6429 0.1123  0.0096  -0.0057 183 ASN C CA  
11075 C C   . ASN C 191 ? 0.6933 0.5474 0.7181 0.1124  0.0233  -0.0173 183 ASN C C   
11076 O O   . ASN C 191 ? 0.7200 0.5818 0.7439 0.1043  0.0273  -0.0302 183 ASN C O   
11077 C CB  . ASN C 191 ? 0.5886 0.4494 0.5913 0.1010  0.0073  -0.0032 183 ASN C CB  
11078 C CG  . ASN C 191 ? 0.5883 0.4683 0.5856 0.0984  -0.0049 0.0055  183 ASN C CG  
11079 O OD1 . ASN C 191 ? 0.5883 0.4733 0.5887 0.1077  -0.0112 0.0179  183 ASN C OD1 
11080 N ND2 . ASN C 191 ? 0.5087 0.4004 0.4981 0.0859  -0.0081 -0.0010 183 ASN C ND2 
11081 N N   . ASP C 199 ? 0.8282 0.5896 0.7844 0.1106  0.0116  0.0513  191 ASP C N   
11082 C CA  . ASP C 199 ? 0.8189 0.5447 0.7663 0.1045  0.0249  0.0482  191 ASP C CA  
11083 C C   . ASP C 199 ? 0.8015 0.5133 0.7334 0.1022  0.0232  0.0624  191 ASP C C   
11084 O O   . ASP C 199 ? 0.8361 0.5300 0.7552 0.0889  0.0300  0.0575  191 ASP C O   
11085 C CB  . ASP C 199 ? 0.8534 0.5664 0.8160 0.1124  0.0345  0.0459  191 ASP C CB  
11086 N N   . GLY C 200 ? 0.7264 0.4505 0.6606 0.1135  0.0138  0.0791  192 GLY C N   
11087 C CA  . GLY C 200 ? 0.7058 0.4210 0.6252 0.1110  0.0113  0.0931  192 GLY C CA  
11088 C C   . GLY C 200 ? 0.6201 0.3426 0.5207 0.0995  0.0051  0.0932  192 GLY C C   
11089 O O   . GLY C 200 ? 0.6431 0.3539 0.5289 0.0931  0.0064  0.1011  192 GLY C O   
11090 N N   . TRP C 201 ? 0.5213 0.2713 0.4268 0.0930  -0.0019 0.0818  193 TRP C N   
11091 C CA  . TRP C 201 ? 0.5006 0.2664 0.3943 0.0788  -0.0082 0.0787  193 TRP C CA  
11092 C C   . TRP C 201 ? 0.4497 0.2353 0.3501 0.0674  -0.0094 0.0610  193 TRP C C   
11093 O O   . TRP C 201 ? 0.4297 0.2276 0.3222 0.0559  -0.0133 0.0575  193 TRP C O   
11094 C CB  . TRP C 201 ? 0.5523 0.3419 0.4419 0.0849  -0.0214 0.0920  193 TRP C CB  
11095 C CG  . TRP C 201 ? 0.5463 0.3643 0.4530 0.0955  -0.0298 0.0913  193 TRP C CG  
11096 C CD1 . TRP C 201 ? 0.4901 0.3359 0.4057 0.0896  -0.0351 0.0796  193 TRP C CD1 
11097 C CD2 . TRP C 201 ? 0.5792 0.4009 0.4972 0.1139  -0.0331 0.1028  193 TRP C CD2 
11098 N NE1 . TRP C 201 ? 0.5433 0.4096 0.4745 0.1019  -0.0411 0.0823  193 TRP C NE1 
11099 C CE2 . TRP C 201 ? 0.6192 0.4728 0.5530 0.1172  -0.0404 0.0963  193 TRP C CE2 
11100 C CE3 . TRP C 201 ? 0.6390 0.4450 0.5599 0.1245  -0.0301 0.1159  193 TRP C CE3 
11101 C CZ2 . TRP C 201 ? 0.6864 0.5547 0.6366 0.1333  -0.0450 0.1034  193 TRP C CZ2 
11102 C CZ3 . TRP C 201 ? 0.6858 0.5095 0.6257 0.1376  -0.0354 0.1213  193 TRP C CZ3 
11103 C CH2 . TRP C 201 ? 0.6996 0.5545 0.6543 0.1415  -0.0426 0.1148  193 TRP C CH2 
11104 N N   . PHE C 202 ? 0.4290 0.2184 0.3432 0.0702  -0.0059 0.0502  194 PHE C N   
11105 C CA  . PHE C 202 ? 0.4503 0.2581 0.3693 0.0600  -0.0070 0.0351  194 PHE C CA  
11106 C C   . PHE C 202 ? 0.4837 0.2783 0.4094 0.0579  0.0031  0.0224  194 PHE C C   
11107 O O   . PHE C 202 ? 0.4595 0.2543 0.3967 0.0678  0.0055  0.0211  194 PHE C O   
11108 C CB  . PHE C 202 ? 0.4455 0.2843 0.3746 0.0651  -0.0168 0.0352  194 PHE C CB  
11109 C CG  . PHE C 202 ? 0.4025 0.2591 0.3353 0.0554  -0.0178 0.0220  194 PHE C CG  
11110 C CD1 . PHE C 202 ? 0.3541 0.2128 0.2781 0.0426  -0.0179 0.0171  194 PHE C CD1 
11111 C CD2 . PHE C 202 ? 0.4602 0.3312 0.4054 0.0597  -0.0181 0.0152  194 PHE C CD2 
11112 C CE1 . PHE C 202 ? 0.3377 0.2124 0.2655 0.0354  -0.0188 0.0069  194 PHE C CE1 
11113 C CE2 . PHE C 202 ? 0.4367 0.3228 0.3838 0.0516  -0.0188 0.0049  194 PHE C CE2 
11114 C CZ  . PHE C 202 ? 0.4085 0.2963 0.3471 0.0400  -0.0194 0.0014  194 PHE C CZ  
11115 N N   . THR C 203 ? 0.4522 0.2373 0.3710 0.0445  0.0094  0.0124  195 THR C N   
11116 C CA  . THR C 203 ? 0.4218 0.1943 0.3444 0.0397  0.0196  -0.0010 195 THR C CA  
11117 C C   . THR C 203 ? 0.3643 0.1523 0.2855 0.0258  0.0190  -0.0149 195 THR C C   
11118 O O   . THR C 203 ? 0.4048 0.1829 0.3252 0.0174  0.0274  -0.0267 195 THR C O   
11119 C CB  . THR C 203 ? 0.4808 0.2193 0.3964 0.0373  0.0313  0.0006  195 THR C CB  
11120 O OG1 . THR C 203 ? 0.4307 0.1645 0.3341 0.0260  0.0312  0.0024  195 THR C OG1 
11121 C CG2 . THR C 203 ? 0.4128 0.1338 0.3303 0.0530  0.0328  0.0159  195 THR C CG2 
11122 N N   . GLU C 204 ? 0.3440 0.1563 0.2652 0.0232  0.0096  -0.0137 196 GLU C N   
11123 C CA  . GLU C 204 ? 0.3300 0.1578 0.2504 0.0117  0.0084  -0.0245 196 GLU C CA  
11124 C C   . GLU C 204 ? 0.3730 0.2095 0.3003 0.0116  0.0110  -0.0358 196 GLU C C   
11125 O O   . GLU C 204 ? 0.3088 0.1516 0.2433 0.0208  0.0095  -0.0343 196 GLU C O   
11126 C CB  . GLU C 204 ? 0.3258 0.1762 0.2464 0.0109  -0.0011 -0.0201 196 GLU C CB  
11127 C CG  . GLU C 204 ? 0.3396 0.1854 0.2519 0.0088  -0.0039 -0.0105 196 GLU C CG  
11128 C CD  . GLU C 204 ? 0.3402 0.2083 0.2538 0.0073  -0.0117 -0.0082 196 GLU C CD  
11129 O OE1 . GLU C 204 ? 0.2955 0.1803 0.2154 0.0057  -0.0137 -0.0149 196 GLU C OE1 
11130 O OE2 . GLU C 204 ? 0.3565 0.2250 0.2641 0.0076  -0.0152 0.0002  196 GLU C OE2 
11131 N N   . ASN C 205 ? 0.2864 0.1248 0.2113 0.0006  0.0150  -0.0474 197 ASN C N   
11132 C CA  . ASN C 205 ? 0.2784 0.1306 0.2071 -0.0018 0.0159  -0.0585 197 ASN C CA  
11133 C C   . ASN C 205 ? 0.3455 0.2242 0.2762 -0.0017 0.0068  -0.0564 197 ASN C C   
11134 O O   . ASN C 205 ? 0.2434 0.1336 0.1719 -0.0096 0.0041  -0.0594 197 ASN C O   
11135 C CB  . ASN C 205 ? 0.2901 0.1366 0.2150 -0.0141 0.0232  -0.0716 197 ASN C CB  
11136 C CG  . ASN C 205 ? 0.2847 0.1471 0.2113 -0.0177 0.0240  -0.0834 197 ASN C CG  
11137 O OD1 . ASN C 205 ? 0.2680 0.1492 0.1974 -0.0127 0.0178  -0.0813 197 ASN C OD1 
11138 N ND2 . ASN C 205 ? 0.3397 0.1947 0.2636 -0.0273 0.0321  -0.0963 197 ASN C ND2 
11139 N N   . ILE C 206 ? 0.2702 0.1586 0.2062 0.0075  0.0027  -0.0512 198 ILE C N   
11140 C CA  . ILE C 206 ? 0.2586 0.1681 0.1967 0.0085  -0.0047 -0.0473 198 ILE C CA  
11141 C C   . ILE C 206 ? 0.2394 0.1651 0.1766 0.0025  -0.0054 -0.0554 198 ILE C C   
11142 O O   . ILE C 206 ? 0.2235 0.1620 0.1602 -0.0012 -0.0096 -0.0537 198 ILE C O   
11143 C CB  . ILE C 206 ? 0.2668 0.1827 0.2114 0.0186  -0.0077 -0.0410 198 ILE C CB  
11144 C CG1 . ILE C 206 ? 0.2892 0.1959 0.2341 0.0243  -0.0101 -0.0308 198 ILE C CG1 
11145 C CG2 . ILE C 206 ? 0.2037 0.1400 0.1507 0.0185  -0.0128 -0.0395 198 ILE C CG2 
11146 C CD1 . ILE C 206 ? 0.3353 0.2452 0.2750 0.0192  -0.0145 -0.0254 198 ILE C CD1 
11147 N N   . PRO C 207 ? 0.2189 0.1455 0.1558 0.0014  -0.0011 -0.0639 199 PRO C N   
11148 C CA  . PRO C 207 ? 0.2238 0.1677 0.1577 -0.0049 -0.0025 -0.0707 199 PRO C CA  
11149 C C   . PRO C 207 ? 0.2682 0.2160 0.1992 -0.0141 -0.0037 -0.0741 199 PRO C C   
11150 O O   . PRO C 207 ? 0.2362 0.2017 0.1675 -0.0160 -0.0087 -0.0727 199 PRO C O   
11151 C CB  . PRO C 207 ? 0.2443 0.1839 0.1764 -0.0064 0.0040  -0.0809 199 PRO C CB  
11152 C CG  . PRO C 207 ? 0.2341 0.1625 0.1718 0.0033  0.0067  -0.0764 199 PRO C CG  
11153 C CD  . PRO C 207 ? 0.2605 0.1756 0.2001 0.0066  0.0050  -0.0674 199 PRO C CD  
11154 N N   . GLN C 208 ? 0.2591 0.1902 0.1881 -0.0194 0.0013  -0.0780 200 GLN C N   
11155 C CA  . GLN C 208 ? 0.2519 0.1873 0.1793 -0.0292 0.0012  -0.0825 200 GLN C CA  
11156 C C   . GLN C 208 ? 0.2752 0.2162 0.2048 -0.0279 -0.0041 -0.0734 200 GLN C C   
11157 O O   . GLN C 208 ? 0.2451 0.2019 0.1766 -0.0328 -0.0072 -0.0752 200 GLN C O   
11158 C CB  . GLN C 208 ? 0.2537 0.1670 0.1781 -0.0358 0.0097  -0.0887 200 GLN C CB  
11159 C CG  . GLN C 208 ? 0.2690 0.1895 0.1939 -0.0470 0.0109  -0.0950 200 GLN C CG  
11160 C CD  . GLN C 208 ? 0.3352 0.2352 0.2594 -0.0524 0.0202  -0.0990 200 GLN C CD  
11161 O OE1 . GLN C 208 ? 0.3858 0.2596 0.3065 -0.0488 0.0255  -0.0951 200 GLN C OE1 
11162 N NE2 . GLN C 208 ? 0.3077 0.2192 0.2350 -0.0609 0.0226  -0.1061 200 GLN C NE2 
11163 N N   . ARG C 209 ? 0.2139 0.1432 0.1437 -0.0213 -0.0049 -0.0639 201 ARG C N   
11164 C CA  . ARG C 209 ? 0.2029 0.1373 0.1339 -0.0210 -0.0090 -0.0563 201 ARG C CA  
11165 C C   . ARG C 209 ? 0.2542 0.2099 0.1896 -0.0183 -0.0143 -0.0543 201 ARG C C   
11166 O O   . ARG C 209 ? 0.2056 0.1712 0.1435 -0.0216 -0.0162 -0.0533 201 ARG C O   
11167 C CB  . ARG C 209 ? 0.2552 0.1764 0.1845 -0.0144 -0.0097 -0.0469 201 ARG C CB  
11168 C CG  . ARG C 209 ? 0.2565 0.1862 0.1870 -0.0132 -0.0142 -0.0397 201 ARG C CG  
11169 C CD  . ARG C 209 ? 0.2864 0.2058 0.2140 -0.0077 -0.0155 -0.0307 201 ARG C CD  
11170 N NE  . ARG C 209 ? 0.2500 0.1809 0.1790 -0.0073 -0.0196 -0.0259 201 ARG C NE  
11171 C CZ  . ARG C 209 ? 0.2691 0.2020 0.1982 -0.0021 -0.0228 -0.0194 201 ARG C CZ  
11172 N NH1 . ARG C 209 ? 0.2189 0.1439 0.1478 0.0050  -0.0232 -0.0154 201 ARG C NH1 
11173 N NH2 . ARG C 209 ? 0.2425 0.1864 0.1729 -0.0039 -0.0252 -0.0173 201 ARG C NH2 
11174 N N   . PHE C 210 ? 0.2267 0.1889 0.1635 -0.0121 -0.0157 -0.0534 202 PHE C N   
11175 C CA  . PHE C 210 ? 0.2463 0.2259 0.1866 -0.0091 -0.0195 -0.0500 202 PHE C CA  
11176 C C   . PHE C 210 ? 0.2407 0.2361 0.1811 -0.0132 -0.0208 -0.0553 202 PHE C C   
11177 O O   . PHE C 210 ? 0.2493 0.2580 0.1933 -0.0121 -0.0236 -0.0516 202 PHE C O   
11178 C CB  . PHE C 210 ? 0.1631 0.1437 0.1047 -0.0017 -0.0198 -0.0466 202 PHE C CB  
11179 C CG  . PHE C 210 ? 0.1582 0.1340 0.1024 0.0023  -0.0210 -0.0394 202 PHE C CG  
11180 C CD1 . PHE C 210 ? 0.2193 0.1811 0.1619 0.0032  -0.0202 -0.0372 202 PHE C CD1 
11181 C CD2 . PHE C 210 ? 0.1707 0.1561 0.1184 0.0044  -0.0227 -0.0347 202 PHE C CD2 
11182 C CE1 . PHE C 210 ? 0.2201 0.1808 0.1640 0.0061  -0.0224 -0.0306 202 PHE C CE1 
11183 C CE2 . PHE C 210 ? 0.1574 0.1405 0.1071 0.0062  -0.0237 -0.0297 202 PHE C CE2 
11184 C CZ  . PHE C 210 ? 0.1976 0.1700 0.1452 0.0068  -0.0242 -0.0278 202 PHE C CZ  
11185 N N   . GLU C 211 ? 0.2227 0.2176 0.1596 -0.0181 -0.0185 -0.0640 203 GLU C N   
11186 C CA  . GLU C 211 ? 0.2259 0.2386 0.1629 -0.0238 -0.0205 -0.0698 203 GLU C CA  
11187 C C   . GLU C 211 ? 0.2508 0.2679 0.1926 -0.0285 -0.0216 -0.0693 203 GLU C C   
11188 O O   . GLU C 211 ? 0.1907 0.2270 0.1370 -0.0284 -0.0253 -0.0681 203 GLU C O   
11189 C CB  . GLU C 211 ? 0.2491 0.2594 0.1813 -0.0306 -0.0166 -0.0812 203 GLU C CB  
11190 C CG  . GLU C 211 ? 0.4132 0.4246 0.3409 -0.0267 -0.0153 -0.0832 203 GLU C CG  
11191 C CD  . GLU C 211 ? 0.4918 0.5009 0.4169 -0.0328 -0.0106 -0.0917 203 GLU C CD  
11192 O OE1 . GLU C 211 ? 0.4344 0.4537 0.3618 -0.0393 -0.0112 -0.0947 203 GLU C OE1 
11193 O OE2 . GLU C 211 ? 0.5614 0.5593 0.4834 -0.0311 -0.0057 -0.0959 203 GLU C OE2 
11194 N N   . SER C 212 ? 0.2011 0.2009 0.1423 -0.0320 -0.0180 -0.0694 204 SER C N   
11195 C CA  . SER C 212 ? 0.1751 0.1781 0.1205 -0.0374 -0.0177 -0.0697 204 SER C CA  
11196 C C   . SER C 212 ? 0.2116 0.2235 0.1629 -0.0319 -0.0209 -0.0613 204 SER C C   
11197 O O   . SER C 212 ? 0.1870 0.2090 0.1444 -0.0351 -0.0212 -0.0621 204 SER C O   
11198 C CB  . SER C 212 ? 0.2384 0.2186 0.1795 -0.0423 -0.0124 -0.0706 204 SER C CB  
11199 O OG  . SER C 212 ? 0.2070 0.1764 0.1468 -0.0371 -0.0129 -0.0613 204 SER C OG  
11200 N N   . TYR C 213 ? 0.1859 0.1946 0.1364 -0.0240 -0.0224 -0.0540 205 TYR C N   
11201 C CA  . TYR C 213 ? 0.1764 0.1928 0.1326 -0.0192 -0.0239 -0.0471 205 TYR C CA  
11202 C C   . TYR C 213 ? 0.2236 0.2589 0.1841 -0.0147 -0.0269 -0.0452 205 TYR C C   
11203 O O   . TYR C 213 ? 0.2046 0.2456 0.1708 -0.0103 -0.0269 -0.0392 205 TYR C O   
11204 C CB  . TYR C 213 ? 0.2145 0.2208 0.1687 -0.0138 -0.0235 -0.0409 205 TYR C CB  
11205 C CG  . TYR C 213 ? 0.2018 0.1916 0.1514 -0.0160 -0.0217 -0.0397 205 TYR C CG  
11206 C CD1 . TYR C 213 ? 0.2332 0.2168 0.1815 -0.0226 -0.0196 -0.0415 205 TYR C CD1 
11207 C CD2 . TYR C 213 ? 0.2286 0.2104 0.1753 -0.0114 -0.0221 -0.0363 205 TYR C CD2 
11208 C CE1 . TYR C 213 ? 0.2413 0.2097 0.1834 -0.0242 -0.0181 -0.0388 205 TYR C CE1 
11209 C CE2 . TYR C 213 ? 0.2148 0.1837 0.1571 -0.0121 -0.0215 -0.0335 205 TYR C CE2 
11210 C CZ  . TYR C 213 ? 0.2139 0.1755 0.1528 -0.0185 -0.0196 -0.0342 205 TYR C CZ  
11211 O OH  . TYR C 213 ? 0.2184 0.1670 0.1510 -0.0189 -0.0192 -0.0299 205 TYR C OH  
11212 N N   . GLY C 214 ? 0.2226 0.2671 0.1798 -0.0155 -0.0288 -0.0496 206 GLY C N   
11213 C CA  . GLY C 214 ? 0.1817 0.2442 0.1401 -0.0105 -0.0321 -0.0461 206 GLY C CA  
11214 C C   . GLY C 214 ? 0.2043 0.2629 0.1580 -0.0040 -0.0316 -0.0409 206 GLY C C   
11215 O O   . GLY C 214 ? 0.2033 0.2734 0.1578 0.0015  -0.0333 -0.0350 206 GLY C O   
11216 N N   . TRP C 215 ? 0.1492 0.1921 0.0986 -0.0041 -0.0290 -0.0426 207 TRP C N   
11217 C CA  . TRP C 215 ? 0.1731 0.2134 0.1191 0.0012  -0.0279 -0.0391 207 TRP C CA  
11218 C C   . TRP C 215 ? 0.1707 0.2174 0.1095 -0.0000 -0.0280 -0.0446 207 TRP C C   
11219 O O   . TRP C 215 ? 0.1870 0.2357 0.1230 -0.0059 -0.0282 -0.0528 207 TRP C O   
11220 C CB  . TRP C 215 ? 0.1579 0.1818 0.1042 0.0024  -0.0253 -0.0385 207 TRP C CB  
11221 C CG  . TRP C 215 ? 0.1643 0.1835 0.1156 0.0039  -0.0247 -0.0328 207 TRP C CG  
11222 C CD1 . TRP C 215 ? 0.1917 0.2111 0.1471 0.0012  -0.0248 -0.0315 207 TRP C CD1 
11223 C CD2 . TRP C 215 ? 0.1655 0.1797 0.1186 0.0074  -0.0230 -0.0291 207 TRP C CD2 
11224 N NE1 . TRP C 215 ? 0.1719 0.1862 0.1302 0.0024  -0.0232 -0.0274 207 TRP C NE1 
11225 C CE2 . TRP C 215 ? 0.1783 0.1901 0.1354 0.0060  -0.0224 -0.0259 207 TRP C CE2 
11226 C CE3 . TRP C 215 ? 0.1560 0.1690 0.1082 0.0109  -0.0216 -0.0289 207 TRP C CE3 
11227 C CZ2 . TRP C 215 ? 0.1682 0.1773 0.1279 0.0072  -0.0207 -0.0231 207 TRP C CZ2 
11228 C CZ3 . TRP C 215 ? 0.1780 0.1891 0.1341 0.0127  -0.0202 -0.0257 207 TRP C CZ3 
11229 C CH2 . TRP C 215 ? 0.1558 0.1654 0.1153 0.0105  -0.0199 -0.0231 207 TRP C CH2 
11230 N N   . HIS C 216 ? 0.1792 0.2295 0.1148 0.0047  -0.0271 -0.0407 208 HIS C N   
11231 C CA  . HIS C 216 ? 0.1996 0.2526 0.1274 0.0037  -0.0255 -0.0461 208 HIS C CA  
11232 C C   . HIS C 216 ? 0.2117 0.2485 0.1406 0.0043  -0.0213 -0.0499 208 HIS C C   
11233 O O   . HIS C 216 ? 0.1851 0.2136 0.1194 0.0081  -0.0202 -0.0449 208 HIS C O   
11234 C CB  . HIS C 216 ? 0.1989 0.2620 0.1223 0.0084  -0.0254 -0.0394 208 HIS C CB  
11235 C CG  . HIS C 216 ? 0.2029 0.2666 0.1183 0.0078  -0.0221 -0.0441 208 HIS C CG  
11236 N ND1 . HIS C 216 ? 0.2139 0.2712 0.1297 0.0117  -0.0177 -0.0410 208 HIS C ND1 
11237 C CD2 . HIS C 216 ? 0.2620 0.3330 0.1689 0.0030  -0.0217 -0.0526 208 HIS C CD2 
11238 C CE1 . HIS C 216 ? 0.2729 0.3328 0.1811 0.0098  -0.0146 -0.0471 208 HIS C CE1 
11239 N NE2 . HIS C 216 ? 0.2550 0.3227 0.1572 0.0044  -0.0168 -0.0543 208 HIS C NE2 
11240 N N   . VAL C 217 ? 0.2389 0.2718 0.1637 0.0005  -0.0186 -0.0591 209 VAL C N   
11241 C CA  . VAL C 217 ? 0.1999 0.2167 0.1274 0.0021  -0.0141 -0.0627 209 VAL C CA  
11242 C C   . VAL C 217 ? 0.2456 0.2640 0.1682 0.0019  -0.0095 -0.0694 209 VAL C C   
11243 O O   . VAL C 217 ? 0.2136 0.2398 0.1290 -0.0038 -0.0088 -0.0770 209 VAL C O   
11244 C CB  . VAL C 217 ? 0.2064 0.2103 0.1352 -0.0025 -0.0127 -0.0680 209 VAL C CB  
11245 C CG1 . VAL C 217 ? 0.2541 0.2406 0.1863 0.0012  -0.0078 -0.0698 209 VAL C CG1 
11246 C CG2 . VAL C 217 ? 0.2026 0.2052 0.1353 -0.0033 -0.0164 -0.0620 209 VAL C CG2 
11247 N N   . VAL C 218 ? 0.1865 0.1990 0.1134 0.0074  -0.0062 -0.0675 210 VAL C N   
11248 C CA  . VAL C 218 ? 0.2176 0.2280 0.1422 0.0074  0.0000  -0.0753 210 VAL C CA  
11249 C C   . VAL C 218 ? 0.2203 0.2133 0.1526 0.0103  0.0041  -0.0785 210 VAL C C   
11250 O O   . VAL C 218 ? 0.2472 0.2354 0.1880 0.0170  0.0037  -0.0725 210 VAL C O   
11251 C CB  . VAL C 218 ? 0.2123 0.2306 0.1370 0.0116  0.0020  -0.0714 210 VAL C CB  
11252 C CG1 . VAL C 218 ? 0.2209 0.2396 0.1415 0.0100  0.0092  -0.0810 210 VAL C CG1 
11253 C CG2 . VAL C 218 ? 0.1987 0.2307 0.1171 0.0108  -0.0022 -0.0641 210 VAL C CG2 
11254 N N   . PRO C 219 ? 0.2355 0.2189 0.1653 0.0056  0.0082  -0.0875 211 PRO C N   
11255 C CA  . PRO C 219 ? 0.2759 0.2398 0.2128 0.0093  0.0129  -0.0889 211 PRO C CA  
11256 C C   . PRO C 219 ? 0.2689 0.2274 0.2106 0.0138  0.0207  -0.0947 211 PRO C C   
11257 O O   . PRO C 219 ? 0.3059 0.2737 0.2427 0.0110  0.0243  -0.1014 211 PRO C O   
11258 C CB  . PRO C 219 ? 0.2842 0.2395 0.2157 0.0006  0.0155  -0.0970 211 PRO C CB  
11259 C CG  . PRO C 219 ? 0.2998 0.2716 0.2218 -0.0075 0.0157  -0.1056 211 PRO C CG  
11260 C CD  . PRO C 219 ? 0.2263 0.2166 0.1465 -0.0039 0.0089  -0.0967 211 PRO C CD  
11261 N N   . ASN C 220 ? 0.3059 0.2495 0.2573 0.0214  0.0236  -0.0915 212 ASN C N   
11262 C CA  . ASN C 220 ? 0.3421 0.2760 0.3005 0.0263  0.0328  -0.0981 212 ASN C CA  
11263 C C   . ASN C 220 ? 0.3322 0.2807 0.2930 0.0288  0.0352  -0.1007 212 ASN C C   
11264 O O   . ASN C 220 ? 0.3124 0.2598 0.2714 0.0261  0.0437  -0.1115 212 ASN C O   
11265 C CB  . ASN C 220 ? 0.3959 0.3168 0.3483 0.0183  0.0416  -0.1112 212 ASN C CB  
11266 C CG  . ASN C 220 ? 0.4858 0.3897 0.4474 0.0243  0.0526  -0.1171 212 ASN C CG  
11267 O OD1 . ASN C 220 ? 0.5242 0.4195 0.4976 0.0356  0.0525  -0.1087 212 ASN C OD1 
11268 N ND2 . ASN C 220 ? 0.4857 0.3880 0.4425 0.0173  0.0602  -0.1279 212 ASN C ND2 
11269 N N   . VAL C 221 ? 0.2477 0.2095 0.2122 0.0330  0.0288  -0.0915 213 VAL C N   
11270 C CA  . VAL C 221 ? 0.2556 0.2304 0.2237 0.0355  0.0316  -0.0927 213 VAL C CA  
11271 C C   . VAL C 221 ? 0.2359 0.2064 0.2207 0.0459  0.0358  -0.0918 213 VAL C C   
11272 O O   . VAL C 221 ? 0.2886 0.2547 0.2823 0.0527  0.0311  -0.0835 213 VAL C O   
11273 C CB  . VAL C 221 ? 0.2869 0.2768 0.2523 0.0346  0.0244  -0.0839 213 VAL C CB  
11274 C CG1 . VAL C 221 ? 0.2553 0.2573 0.2245 0.0364  0.0288  -0.0852 213 VAL C CG1 
11275 C CG2 . VAL C 221 ? 0.2846 0.2798 0.2356 0.0263  0.0201  -0.0834 213 VAL C CG2 
11276 N N   . ASN C 222 ? 0.2947 0.2675 0.2836 0.0471  0.0447  -0.1003 214 ASN C N   
11277 C CA  . ASN C 222 ? 0.2622 0.2360 0.2692 0.0575  0.0490  -0.0998 214 ASN C CA  
11278 C C   . ASN C 222 ? 0.2480 0.2384 0.2628 0.0614  0.0418  -0.0904 214 ASN C C   
11279 O O   . ASN C 222 ? 0.2233 0.2275 0.2346 0.0572  0.0428  -0.0917 214 ASN C O   
11280 C CB  . ASN C 222 ? 0.2909 0.2665 0.2997 0.0561  0.0609  -0.1122 214 ASN C CB  
11281 C CG  . ASN C 222 ? 0.3363 0.3141 0.3665 0.0676  0.0665  -0.1129 214 ASN C CG  
11282 O OD1 . ASN C 222 ? 0.3819 0.3674 0.4252 0.0759  0.0602  -0.1034 214 ASN C OD1 
11283 N ND2 . ASN C 222 ? 0.3656 0.3383 0.3974 0.0668  0.0770  -0.1212 214 ASN C ND2 
11284 N N   . GLY C 223 ? 0.2553 0.2447 0.2802 0.0689  0.0351  -0.0812 215 GLY C N   
11285 C CA  . GLY C 223 ? 0.2541 0.2599 0.2853 0.0706  0.0279  -0.0732 215 GLY C CA  
11286 C C   . GLY C 223 ? 0.2255 0.2474 0.2725 0.0758  0.0316  -0.0754 215 GLY C C   
11287 O O   . GLY C 223 ? 0.2717 0.3087 0.3244 0.0757  0.0265  -0.0704 215 GLY C O   
11288 N N   . HIS C 224 ? 0.2218 0.2415 0.2768 0.0796  0.0413  -0.0838 216 HIS C N   
11289 C CA  . HIS C 224 ? 0.2427 0.2792 0.3132 0.0834  0.0466  -0.0879 216 HIS C CA  
11290 C C   . HIS C 224 ? 0.2991 0.3377 0.3611 0.0757  0.0568  -0.0984 216 HIS C C   
11291 O O   . HIS C 224 ? 0.2828 0.3323 0.3574 0.0784  0.0644  -0.1044 216 HIS C O   
11292 C CB  . HIS C 224 ? 0.2775 0.3131 0.3696 0.0968  0.0495  -0.0879 216 HIS C CB  
11293 C CG  . HIS C 224 ? 0.2629 0.2980 0.3624 0.1052  0.0392  -0.0761 216 HIS C CG  
11294 N ND1 . HIS C 224 ? 0.2927 0.3456 0.3962 0.1048  0.0295  -0.0685 216 HIS C ND1 
11295 C CD2 . HIS C 224 ? 0.3136 0.3322 0.4157 0.1134  0.0375  -0.0707 216 HIS C CD2 
11296 C CE1 . HIS C 224 ? 0.3039 0.3531 0.4114 0.1124  0.0215  -0.0587 216 HIS C CE1 
11297 N NE2 . HIS C 224 ? 0.3200 0.3477 0.4267 0.1182  0.0262  -0.0591 216 HIS C NE2 
11298 N N   . ASP C 225 ? 0.3165 0.3464 0.3574 0.0662  0.0573  -0.1009 217 ASP C N   
11299 C CA  . ASP C 225 ? 0.3236 0.3563 0.3521 0.0579  0.0660  -0.1097 217 ASP C CA  
11300 C C   . ASP C 225 ? 0.3433 0.3855 0.3587 0.0503  0.0610  -0.1034 217 ASP C C   
11301 O O   . ASP C 225 ? 0.2183 0.2551 0.2188 0.0454  0.0546  -0.0986 217 ASP C O   
11302 C CB  . ASP C 225 ? 0.3002 0.3180 0.3147 0.0529  0.0702  -0.1174 217 ASP C CB  
11303 C CG  . ASP C 225 ? 0.3254 0.3463 0.3236 0.0429  0.0768  -0.1232 217 ASP C CG  
11304 O OD1 . ASP C 225 ? 0.3149 0.3479 0.3071 0.0387  0.0774  -0.1210 217 ASP C OD1 
11305 O OD2 . ASP C 225 ? 0.4626 0.4732 0.4533 0.0389  0.0814  -0.1294 217 ASP C OD2 
11306 N N   . THR C 226 ? 0.2175 0.2733 0.2390 0.0494  0.0649  -0.1035 218 THR C N   
11307 C CA  . THR C 226 ? 0.2844 0.3468 0.2951 0.0429  0.0616  -0.0966 218 THR C CA  
11308 C C   . THR C 226 ? 0.2468 0.3049 0.2337 0.0347  0.0635  -0.0973 218 THR C C   
11309 O O   . THR C 226 ? 0.2249 0.2828 0.2001 0.0309  0.0579  -0.0893 218 THR C O   
11310 C CB  . THR C 226 ? 0.2057 0.2823 0.2276 0.0423  0.0677  -0.0979 218 THR C CB  
11311 O OG1 . THR C 226 ? 0.2610 0.3400 0.2823 0.0404  0.0790  -0.1072 218 THR C OG1 
11312 C CG2 . THR C 226 ? 0.3594 0.4451 0.4052 0.0501  0.0637  -0.0962 218 THR C CG2 
11313 N N   . ALA C 227 ? 0.2318 0.2875 0.2113 0.0319  0.0715  -0.1069 219 ALA C N   
11314 C CA  . ALA C 227 ? 0.2784 0.3325 0.2342 0.0239  0.0718  -0.1073 219 ALA C CA  
11315 C C   . ALA C 227 ? 0.2713 0.3179 0.2186 0.0230  0.0626  -0.1042 219 ALA C C   
11316 O O   . ALA C 227 ? 0.2498 0.2991 0.1817 0.0186  0.0573  -0.0979 219 ALA C O   
11317 C CB  . ALA C 227 ? 0.2609 0.3117 0.2114 0.0200  0.0795  -0.1149 219 ALA C CB  
11318 N N   . ALA C 228 ? 0.2385 0.2756 0.1966 0.0275  0.0610  -0.1078 220 ALA C N   
11319 C CA  . ALA C 228 ? 0.2401 0.2692 0.1914 0.0259  0.0531  -0.1051 220 ALA C CA  
11320 C C   . ALA C 228 ? 0.2528 0.2841 0.2051 0.0275  0.0432  -0.0927 220 ALA C C   
11321 O O   . ALA C 228 ? 0.2177 0.2492 0.1584 0.0235  0.0371  -0.0885 220 ALA C O   
11322 C CB  . ALA C 228 ? 0.2593 0.2751 0.2223 0.0307  0.0550  -0.1106 220 ALA C CB  
11323 N N   . ILE C 229 ? 0.2279 0.2625 0.1948 0.0330  0.0418  -0.0872 221 ILE C N   
11324 C CA  . ILE C 229 ? 0.1997 0.2365 0.1675 0.0334  0.0338  -0.0768 221 ILE C CA  
11325 C C   . ILE C 229 ? 0.1948 0.2380 0.1492 0.0281  0.0341  -0.0718 221 ILE C C   
11326 O O   . ILE C 229 ? 0.1888 0.2312 0.1366 0.0264  0.0279  -0.0647 221 ILE C O   
11327 C CB  . ILE C 229 ? 0.1864 0.2280 0.1721 0.0390  0.0329  -0.0737 221 ILE C CB  
11328 C CG1 . ILE C 229 ? 0.2208 0.2557 0.2192 0.0460  0.0317  -0.0762 221 ILE C CG1 
11329 C CG2 . ILE C 229 ? 0.2065 0.2507 0.1921 0.0376  0.0261  -0.0646 221 ILE C CG2 
11330 C CD1 . ILE C 229 ? 0.2022 0.2466 0.2204 0.0529  0.0321  -0.0751 221 ILE C CD1 
11331 N N   . GLN C 230 ? 0.2026 0.2519 0.1529 0.0259  0.0419  -0.0750 222 GLN C N   
11332 C CA  . GLN C 230 ? 0.2053 0.2593 0.1423 0.0217  0.0433  -0.0686 222 GLN C CA  
11333 C C   . GLN C 230 ? 0.2118 0.2657 0.1310 0.0183  0.0387  -0.0664 222 GLN C C   
11334 O O   . GLN C 230 ? 0.2263 0.2816 0.1385 0.0177  0.0345  -0.0571 222 GLN C O   
11335 C CB  . GLN C 230 ? 0.2155 0.2753 0.1500 0.0194  0.0536  -0.0728 222 GLN C CB  
11336 C CG  . GLN C 230 ? 0.3650 0.4276 0.2839 0.0155  0.0560  -0.0647 222 GLN C CG  
11337 C CD  . GLN C 230 ? 0.3913 0.4580 0.3112 0.0130  0.0668  -0.0661 222 GLN C CD  
11338 O OE1 . GLN C 230 ? 0.3906 0.4606 0.3240 0.0141  0.0725  -0.0745 222 GLN C OE1 
11339 N NE2 . GLN C 230 ? 0.3556 0.4222 0.2620 0.0101  0.0700  -0.0575 222 GLN C NE2 
11340 N N   . THR C 231 ? 0.2233 0.2766 0.1359 0.0158  0.0400  -0.0754 223 THR C N   
11341 C CA  . THR C 231 ? 0.2293 0.2867 0.1253 0.0114  0.0353  -0.0746 223 THR C CA  
11342 C C   . THR C 231 ? 0.2464 0.3001 0.1464 0.0127  0.0260  -0.0701 223 THR C C   
11343 O O   . THR C 231 ? 0.2195 0.2792 0.1094 0.0108  0.0204  -0.0646 223 THR C O   
11344 C CB  . THR C 231 ? 0.2967 0.3555 0.1842 0.0063  0.0403  -0.0876 223 THR C CB  
11345 O OG1 . THR C 231 ? 0.3683 0.4168 0.2683 0.0081  0.0412  -0.0959 223 THR C OG1 
11346 C CG2 . THR C 231 ? 0.2949 0.3555 0.1800 0.0046  0.0496  -0.0907 223 THR C CG2 
11347 N N   . ALA C 232 ? 0.2219 0.2666 0.1366 0.0163  0.0244  -0.0715 224 ALA C N   
11348 C CA  . ALA C 232 ? 0.2192 0.2597 0.1380 0.0173  0.0166  -0.0665 224 ALA C CA  
11349 C C   . ALA C 232 ? 0.2561 0.2999 0.1756 0.0191  0.0128  -0.0550 224 ALA C C   
11350 O O   . ALA C 232 ? 0.1994 0.2451 0.1152 0.0181  0.0070  -0.0501 224 ALA C O   
11351 C CB  . ALA C 232 ? 0.1945 0.2245 0.1276 0.0213  0.0163  -0.0691 224 ALA C CB  
11352 N N   . ILE C 233 ? 0.1856 0.2303 0.1112 0.0213  0.0169  -0.0514 225 ILE C N   
11353 C CA  . ILE C 233 ? 0.2350 0.2807 0.1615 0.0222  0.0156  -0.0415 225 ILE C CA  
11354 C C   . ILE C 233 ? 0.2088 0.2603 0.1208 0.0208  0.0158  -0.0354 225 ILE C C   
11355 O O   . ILE C 233 ? 0.1841 0.2360 0.0948 0.0219  0.0122  -0.0271 225 ILE C O   
11356 C CB  . ILE C 233 ? 0.2579 0.3038 0.1947 0.0234  0.0212  -0.0409 225 ILE C CB  
11357 C CG1 . ILE C 233 ? 0.2382 0.2813 0.1899 0.0259  0.0187  -0.0445 225 ILE C CG1 
11358 C CG2 . ILE C 233 ? 0.2416 0.2871 0.1773 0.0228  0.0229  -0.0319 225 ILE C CG2 
11359 C CD1 . ILE C 233 ? 0.1749 0.2227 0.1383 0.0266  0.0237  -0.0456 225 ILE C CD1 
11360 N N   . GLU C 234 ? 0.2424 0.2990 0.1436 0.0187  0.0204  -0.0389 226 GLU C N   
11361 C CA  . GLU C 234 ? 0.2242 0.2885 0.1092 0.0176  0.0196  -0.0325 226 GLU C CA  
11362 C C   . GLU C 234 ? 0.2105 0.2802 0.0914 0.0172  0.0108  -0.0311 226 GLU C C   
11363 O O   . GLU C 234 ? 0.2511 0.3260 0.1265 0.0194  0.0072  -0.0211 226 GLU C O   
11364 C CB  . GLU C 234 ? 0.2487 0.3190 0.1212 0.0139  0.0252  -0.0390 226 GLU C CB  
11365 C CG  . GLU C 234 ? 0.2353 0.3026 0.1104 0.0136  0.0352  -0.0403 226 GLU C CG  
11366 C CD  . GLU C 234 ? 0.2468 0.3191 0.1116 0.0092  0.0417  -0.0499 226 GLU C CD  
11367 O OE1 . GLU C 234 ? 0.3190 0.3964 0.1751 0.0060  0.0387  -0.0570 226 GLU C OE1 
11368 O OE2 . GLU C 234 ? 0.3645 0.4361 0.2301 0.0082  0.0505  -0.0512 226 GLU C OE2 
11369 N N   . ALA C 235 ? 0.2255 0.2943 0.1095 0.0146  0.0079  -0.0410 227 ALA C N   
11370 C CA  . ALA C 235 ? 0.2491 0.3241 0.1302 0.0127  0.0003  -0.0416 227 ALA C CA  
11371 C C   . ALA C 235 ? 0.2295 0.3003 0.1209 0.0162  -0.0044 -0.0338 227 ALA C C   
11372 O O   . ALA C 235 ? 0.1946 0.2739 0.0833 0.0169  -0.0099 -0.0283 227 ALA C O   
11373 C CB  . ALA C 235 ? 0.2109 0.2827 0.0934 0.0080  0.0006  -0.0550 227 ALA C CB  
11374 N N   . ALA C 236 ? 0.2223 0.2817 0.1260 0.0183  -0.0023 -0.0336 228 ALA C N   
11375 C CA  . ALA C 236 ? 0.1728 0.2280 0.0855 0.0206  -0.0056 -0.0271 228 ALA C CA  
11376 C C   . ALA C 236 ? 0.2130 0.2714 0.1233 0.0239  -0.0045 -0.0158 228 ALA C C   
11377 O O   . ALA C 236 ? 0.2606 0.3217 0.1736 0.0256  -0.0083 -0.0100 228 ALA C O   
11378 C CB  . ALA C 236 ? 0.1637 0.2085 0.0882 0.0215  -0.0034 -0.0292 228 ALA C CB  
11379 N N   . ARG C 237 ? 0.2112 0.2687 0.1173 0.0249  0.0018  -0.0124 229 ARG C N   
11380 C CA  . ARG C 237 ? 0.1861 0.2434 0.0895 0.0283  0.0047  -0.0008 229 ARG C CA  
11381 C C   . ARG C 237 ? 0.2421 0.3111 0.1348 0.0306  -0.0002 0.0058  229 ARG C C   
11382 O O   . ARG C 237 ? 0.2499 0.3196 0.1447 0.0350  -0.0012 0.0159  229 ARG C O   
11383 C CB  . ARG C 237 ? 0.2284 0.2815 0.1285 0.0278  0.0136  0.0006  229 ARG C CB  
11384 C CG  . ARG C 237 ? 0.1838 0.2285 0.0972 0.0262  0.0183  -0.0039 229 ARG C CG  
11385 C CD  . ARG C 237 ? 0.2170 0.2606 0.1284 0.0243  0.0272  -0.0058 229 ARG C CD  
11386 N NE  . ARG C 237 ? 0.3305 0.3722 0.2321 0.0254  0.0334  0.0042  229 ARG C NE  
11387 C CZ  . ARG C 237 ? 0.3492 0.3826 0.2552 0.0263  0.0387  0.0119  229 ARG C CZ  
11388 N NH1 . ARG C 237 ? 0.3330 0.3614 0.2528 0.0253  0.0383  0.0095  229 ARG C NH1 
11389 N NH2 . ARG C 237 ? 0.3218 0.3515 0.2175 0.0280  0.0451  0.0221  229 ARG C NH2 
11390 N N   . ALA C 238 ? 0.2370 0.3165 0.1189 0.0276  -0.0031 -0.0001 230 ALA C N   
11391 C CA  . ALA C 238 ? 0.2457 0.3408 0.1167 0.0291  -0.0089 0.0055  230 ALA C CA  
11392 C C   . ALA C 238 ? 0.2838 0.3857 0.1631 0.0304  -0.0167 0.0064  230 ALA C C   
11393 O O   . ALA C 238 ? 0.2632 0.3773 0.1394 0.0339  -0.0213 0.0148  230 ALA C O   
11394 C CB  . ALA C 238 ? 0.2262 0.3312 0.0850 0.0232  -0.0099 -0.0036 230 ALA C CB  
11395 N N   . GLU C 239 ? 0.2607 0.3547 0.1516 0.0275  -0.0179 -0.0017 231 GLU C N   
11396 C CA  . GLU C 239 ? 0.2839 0.3836 0.1831 0.0274  -0.0241 -0.0022 231 GLU C CA  
11397 C C   . GLU C 239 ? 0.2746 0.3658 0.1848 0.0328  -0.0219 0.0073  231 GLU C C   
11398 O O   . GLU C 239 ? 0.2824 0.3601 0.2017 0.0315  -0.0188 0.0044  231 GLU C O   
11399 C CB  . GLU C 239 ? 0.2966 0.3901 0.2010 0.0211  -0.0252 -0.0150 231 GLU C CB  
11400 C CG  . GLU C 239 ? 0.3869 0.4832 0.3009 0.0200  -0.0298 -0.0161 231 GLU C CG  
11401 C CD  . GLU C 239 ? 0.4251 0.5422 0.3369 0.0208  -0.0361 -0.0129 231 GLU C CD  
11402 O OE1 . GLU C 239 ? 0.4259 0.5501 0.3332 0.0152  -0.0372 -0.0191 231 GLU C OE1 
11403 O OE2 . GLU C 239 ? 0.3771 0.4994 0.2958 0.0264  -0.0379 -0.0038 231 GLU C OE2 
11404 N N   . THR C 240 ? 0.2592 0.3589 0.1686 0.0390  -0.0234 0.0187  232 THR C N   
11405 C CA  . THR C 240 ? 0.2530 0.3429 0.1724 0.0446  -0.0190 0.0281  232 THR C CA  
11406 C C   . THR C 240 ? 0.2813 0.3740 0.2137 0.0452  -0.0225 0.0271  232 THR C C   
11407 O O   . THR C 240 ? 0.2455 0.3287 0.1876 0.0488  -0.0178 0.0328  232 THR C O   
11408 C CB  . THR C 240 ? 0.3387 0.4331 0.2517 0.0526  -0.0169 0.0427  232 THR C CB  
11409 O OG1 . THR C 240 ? 0.3014 0.4175 0.2104 0.0558  -0.0254 0.0467  232 THR C OG1 
11410 C CG2 . THR C 240 ? 0.3302 0.4197 0.2300 0.0512  -0.0115 0.0439  232 THR C CG2 
11411 N N   . GLY C 241 ? 0.2249 0.3298 0.1579 0.0409  -0.0294 0.0191  233 GLY C N   
11412 C CA  . GLY C 241 ? 0.2371 0.3461 0.1825 0.0408  -0.0321 0.0177  233 GLY C CA  
11413 C C   . GLY C 241 ? 0.2612 0.3587 0.2123 0.0334  -0.0311 0.0069  233 GLY C C   
11414 O O   . GLY C 241 ? 0.2169 0.3153 0.1781 0.0325  -0.0317 0.0055  233 GLY C O   
11415 N N   . LYS C 242 ? 0.2091 0.2960 0.1541 0.0285  -0.0292 -0.0002 234 LYS C N   
11416 C CA  . LYS C 242 ? 0.1589 0.2345 0.1077 0.0224  -0.0285 -0.0089 234 LYS C CA  
11417 C C   . LYS C 242 ? 0.1592 0.2196 0.1067 0.0221  -0.0237 -0.0097 234 LYS C C   
11418 O O   . LYS C 242 ? 0.1961 0.2565 0.1373 0.0239  -0.0216 -0.0084 234 LYS C O   
11419 C CB  . LYS C 242 ? 0.2166 0.2972 0.1604 0.0160  -0.0321 -0.0191 234 LYS C CB  
11420 C CG  . LYS C 242 ? 0.1985 0.2992 0.1420 0.0147  -0.0375 -0.0207 234 LYS C CG  
11421 C CD  . LYS C 242 ? 0.1548 0.2576 0.0922 0.0065  -0.0389 -0.0328 234 LYS C CD  
11422 C CE  . LYS C 242 ? 0.2616 0.3844 0.1996 0.0033  -0.0431 -0.0352 234 LYS C CE  
11423 N NZ  . LYS C 242 ? 0.3172 0.4354 0.2516 -0.0059 -0.0410 -0.0468 234 LYS C NZ  
11424 N N   . PRO C 243 ? 0.1662 0.2154 0.1196 0.0197  -0.0218 -0.0120 235 PRO C N   
11425 C CA  . PRO C 243 ? 0.1531 0.1918 0.1059 0.0188  -0.0188 -0.0141 235 PRO C CA  
11426 C C   . PRO C 243 ? 0.1749 0.2124 0.1220 0.0166  -0.0204 -0.0211 235 PRO C C   
11427 O O   . PRO C 243 ? 0.1682 0.2089 0.1128 0.0135  -0.0233 -0.0260 235 PRO C O   
11428 C CB  . PRO C 243 ? 0.1245 0.1551 0.0835 0.0160  -0.0180 -0.0152 235 PRO C CB  
11429 C CG  . PRO C 243 ? 0.1840 0.2188 0.1451 0.0135  -0.0210 -0.0169 235 PRO C CG  
11430 C CD  . PRO C 243 ? 0.1660 0.2136 0.1265 0.0170  -0.0226 -0.0132 235 PRO C CD  
11431 N N   . SER C 244 ? 0.1511 0.1843 0.0971 0.0180  -0.0175 -0.0222 236 SER C N   
11432 C CA  . SER C 244 ? 0.1998 0.2313 0.1416 0.0170  -0.0173 -0.0289 236 SER C CA  
11433 C C   . SER C 244 ? 0.1631 0.1848 0.1099 0.0174  -0.0163 -0.0314 236 SER C C   
11434 O O   . SER C 244 ? 0.1864 0.2065 0.1384 0.0190  -0.0149 -0.0281 236 SER C O   
11435 C CB  . SER C 244 ? 0.1833 0.2204 0.1195 0.0189  -0.0141 -0.0286 236 SER C CB  
11436 O OG  . SER C 244 ? 0.1796 0.2273 0.1091 0.0191  -0.0158 -0.0254 236 SER C OG  
11437 N N   . ILE C 245 ? 0.1729 0.1887 0.1182 0.0161  -0.0167 -0.0372 237 ILE C N   
11438 C CA  . ILE C 245 ? 0.1835 0.1907 0.1333 0.0185  -0.0156 -0.0386 237 ILE C CA  
11439 C C   . ILE C 245 ? 0.1888 0.1942 0.1367 0.0197  -0.0120 -0.0450 237 ILE C C   
11440 O O   . ILE C 245 ? 0.2101 0.2148 0.1522 0.0163  -0.0112 -0.0507 237 ILE C O   
11441 C CB  . ILE C 245 ? 0.1574 0.1549 0.1082 0.0168  -0.0179 -0.0381 237 ILE C CB  
11442 C CG1 . ILE C 245 ? 0.2064 0.1964 0.1620 0.0211  -0.0174 -0.0373 237 ILE C CG1 
11443 C CG2 . ILE C 245 ? 0.2364 0.2300 0.1821 0.0121  -0.0177 -0.0436 237 ILE C CG2 
11444 C CD1 . ILE C 245 ? 0.2284 0.2091 0.1837 0.0202  -0.0198 -0.0339 237 ILE C CD1 
11445 N N   . ILE C 246 ? 0.1635 0.1694 0.1169 0.0240  -0.0094 -0.0449 238 ILE C N   
11446 C CA  . ILE C 246 ? 0.1738 0.1780 0.1276 0.0259  -0.0046 -0.0513 238 ILE C CA  
11447 C C   . ILE C 246 ? 0.2075 0.2019 0.1692 0.0306  -0.0040 -0.0517 238 ILE C C   
11448 O O   . ILE C 246 ? 0.1698 0.1668 0.1394 0.0348  -0.0060 -0.0469 238 ILE C O   
11449 C CB  . ILE C 246 ? 0.1947 0.2085 0.1499 0.0276  -0.0010 -0.0510 238 ILE C CB  
11450 C CG1 . ILE C 246 ? 0.1986 0.2207 0.1445 0.0240  -0.0013 -0.0485 238 ILE C CG1 
11451 C CG2 . ILE C 246 ? 0.2023 0.2147 0.1599 0.0298  0.0051  -0.0584 238 ILE C CG2 
11452 C CD1 . ILE C 246 ? 0.2210 0.2503 0.1679 0.0251  0.0022  -0.0447 238 ILE C CD1 
11453 N N   . CYS C 247 ? 0.1830 0.1663 0.1427 0.0300  -0.0011 -0.0573 239 CYS C N   
11454 C CA  . CYS C 247 ? 0.2476 0.2182 0.2139 0.0353  -0.0000 -0.0561 239 CYS C CA  
11455 C C   . CYS C 247 ? 0.2486 0.2195 0.2233 0.0416  0.0056  -0.0601 239 CYS C C   
11456 O O   . CYS C 247 ? 0.2432 0.2090 0.2155 0.0399  0.0122  -0.0686 239 CYS C O   
11457 C CB  . CYS C 247 ? 0.2035 0.1591 0.1640 0.0311  0.0021  -0.0601 239 CYS C CB  
11458 S SG  . CYS C 247 ? 0.2780 0.2350 0.2308 0.0236  -0.0038 -0.0563 239 CYS C SG  
11459 N N   . CYS C 248 ? 0.1925 0.1708 0.1776 0.0483  0.0036  -0.0548 240 CYS C N   
11460 C CA  . CYS C 248 ? 0.2288 0.2119 0.2246 0.0546  0.0089  -0.0585 240 CYS C CA  
11461 C C   . CYS C 248 ? 0.3067 0.2785 0.3123 0.0636  0.0102  -0.0561 240 CYS C C   
11462 O O   . CYS C 248 ? 0.2401 0.2142 0.2516 0.0689  0.0043  -0.0475 240 CYS C O   
11463 C CB  . CYS C 248 ? 0.1844 0.1852 0.1874 0.0561  0.0064  -0.0550 240 CYS C CB  
11464 S SG  . CYS C 248 ? 0.2276 0.2388 0.2197 0.0472  0.0063  -0.0556 240 CYS C SG  
11465 N N   . LYS C 249 ? 0.2341 0.1940 0.2414 0.0655  0.0184  -0.0635 241 LYS C N   
11466 C CA  . LYS C 249 ? 0.2907 0.2372 0.3084 0.0754  0.0220  -0.0613 241 LYS C CA  
11467 C C   . LYS C 249 ? 0.2770 0.2376 0.3120 0.0853  0.0229  -0.0599 241 LYS C C   
11468 O O   . LYS C 249 ? 0.2428 0.2095 0.2824 0.0850  0.0301  -0.0685 241 LYS C O   
11469 C CB  . LYS C 249 ? 0.3553 0.2831 0.3692 0.0727  0.0324  -0.0715 241 LYS C CB  
11470 C CG  . LYS C 249 ? 0.3905 0.3075 0.3884 0.0614  0.0322  -0.0750 241 LYS C CG  
11471 C CD  . LYS C 249 ? 0.4348 0.3354 0.4311 0.0639  0.0291  -0.0664 241 LYS C CD  
11472 C CE  . LYS C 249 ? 0.4438 0.3342 0.4261 0.0520  0.0301  -0.0713 241 LYS C CE  
11473 N NZ  . LYS C 249 ? 0.4323 0.3035 0.4126 0.0539  0.0296  -0.0638 241 LYS C NZ  
11474 N N   . THR C 250 ? 0.2520 0.2197 0.2963 0.0935  0.0157  -0.0495 242 THR C N   
11475 C CA  . THR C 250 ? 0.2918 0.2761 0.3547 0.1035  0.0157  -0.0479 242 THR C CA  
11476 C C   . THR C 250 ? 0.3552 0.3279 0.4308 0.1173  0.0179  -0.0424 242 THR C C   
11477 O O   . THR C 250 ? 0.4057 0.3575 0.4742 0.1189  0.0181  -0.0374 242 THR C O   
11478 C CB  . THR C 250 ? 0.2530 0.2596 0.3192 0.1026  0.0056  -0.0408 242 THR C CB  
11479 O OG1 . THR C 250 ? 0.3009 0.3017 0.3608 0.1037  -0.0028 -0.0304 242 THR C OG1 
11480 C CG2 . THR C 250 ? 0.2087 0.2253 0.2645 0.0902  0.0054  -0.0459 242 THR C CG2 
11481 N N   . LEU C 251 ? 0.3505 0.3367 0.4455 0.1277  0.0204  -0.0430 243 LEU C N   
11482 C CA  . LEU C 251 ? 0.5284 0.5038 0.6382 0.1429  0.0242  -0.0380 243 LEU C CA  
11483 C C   . LEU C 251 ? 0.5929 0.5893 0.7179 0.1548  0.0141  -0.0258 243 LEU C C   
11484 O O   . LEU C 251 ? 0.6285 0.6415 0.7743 0.1645  0.0161  -0.0266 243 LEU C O   
11485 C CB  . LEU C 251 ? 0.5314 0.5034 0.6542 0.1472  0.0376  -0.0496 243 LEU C CB  
11486 N N   . ALA C 268 ? 0.5966 0.8227 0.7124 0.1414  -0.1139 0.0662  260 ALA C N   
11487 C CA  . ALA C 268 ? 0.5851 0.8407 0.7171 0.1465  -0.1214 0.0688  260 ALA C CA  
11488 C C   . ALA C 268 ? 0.5109 0.7824 0.6684 0.1503  -0.1155 0.0594  260 ALA C C   
11489 O O   . ALA C 268 ? 0.4793 0.7333 0.6429 0.1543  -0.1058 0.0548  260 ALA C O   
11490 C CB  . ALA C 268 ? 0.5794 0.8257 0.7117 0.1612  -0.1276 0.0845  260 ALA C CB  
11491 N N   . PRO C 269 ? 0.5248 0.8298 0.6966 0.1484  -0.1207 0.0558  261 PRO C N   
11492 C CA  . PRO C 269 ? 0.5408 0.8625 0.7384 0.1527  -0.1152 0.0476  261 PRO C CA  
11493 C C   . PRO C 269 ? 0.5427 0.8466 0.7556 0.1700  -0.1104 0.0539  261 PRO C C   
11494 O O   . PRO C 269 ? 0.5388 0.8273 0.7476 0.1812  -0.1149 0.0667  261 PRO C O   
11495 C CB  . PRO C 269 ? 0.4887 0.8478 0.6976 0.1510  -0.1244 0.0475  261 PRO C CB  
11496 C CG  . PRO C 269 ? 0.4930 0.8570 0.6790 0.1381  -0.1312 0.0482  261 PRO C CG  
11497 C CD  . PRO C 269 ? 0.5085 0.8382 0.6725 0.1404  -0.1310 0.0574  261 PRO C CD  
11498 N N   . LEU C 270 ? 0.4853 0.7902 0.7152 0.1716  -0.1001 0.0443  262 LEU C N   
11499 C CA  . LEU C 270 ? 0.4822 0.7694 0.7282 0.1866  -0.0929 0.0472  262 LEU C CA  
11500 C C   . LEU C 270 ? 0.5109 0.8110 0.7750 0.2013  -0.1007 0.0576  262 LEU C C   
11501 O O   . LEU C 270 ? 0.5590 0.8426 0.8361 0.2152  -0.0959 0.0617  262 LEU C O   
11502 C CB  . LEU C 270 ? 0.4576 0.7498 0.7199 0.1842  -0.0804 0.0336  262 LEU C CB  
11503 C CG  . LEU C 270 ? 0.4967 0.7682 0.7445 0.1748  -0.0695 0.0235  262 LEU C CG  
11504 C CD1 . LEU C 270 ? 0.5095 0.7781 0.7746 0.1782  -0.0559 0.0135  262 LEU C CD1 
11505 C CD2 . LEU C 270 ? 0.5221 0.7586 0.7485 0.1772  -0.0688 0.0304  262 LEU C CD2 
11506 N N   . ILE C 275 ? 0.4941 0.8315 0.8510 0.2109  -0.0592 0.0197  267 ILE C N   
11507 C CA  . ILE C 275 ? 0.5022 0.8447 0.8524 0.1965  -0.0492 0.0057  267 ILE C CA  
11508 C C   . ILE C 275 ? 0.5161 0.8670 0.8905 0.2006  -0.0360 -0.0025 267 ILE C C   
11509 O O   . ILE C 275 ? 0.5106 0.8470 0.8782 0.1950  -0.0226 -0.0123 267 ILE C O   
11510 C CB  . ILE C 275 ? 0.4934 0.8642 0.8349 0.1819  -0.0579 0.0011  267 ILE C CB  
11511 C CG1 . ILE C 275 ? 0.4938 0.8505 0.8063 0.1745  -0.0662 0.0061  267 ILE C CG1 
11512 C CG2 . ILE C 275 ? 0.4540 0.8347 0.7959 0.1686  -0.0471 -0.0145 267 ILE C CG2 
11513 C CD1 . ILE C 275 ? 0.4815 0.8634 0.7849 0.1600  -0.0741 0.0017  267 ILE C CD1 
11514 N N   . GLU C 276 ? 0.5929 0.9675 0.9948 0.2106  -0.0400 0.0016  268 GLU C N   
11515 C CA  . GLU C 276 ? 0.6313 1.0139 1.0585 0.2163  -0.0269 -0.0047 268 GLU C CA  
11516 C C   . GLU C 276 ? 0.6599 1.0076 1.0886 0.2259  -0.0130 -0.0040 268 GLU C C   
11517 O O   . GLU C 276 ? 0.6690 1.0128 1.1025 0.2250  0.0031  -0.0125 268 GLU C O   
11518 C CB  . GLU C 276 ? 0.6116 1.0253 1.0698 0.2272  -0.0350 0.0011  268 GLU C CB  
11519 N N   . ALA C 277 ? 0.6625 0.9837 1.0843 0.2343  -0.0186 0.0048  269 ALA C N   
11520 C CA  . ALA C 277 ? 0.6190 0.9038 1.0402 0.2410  -0.0054 0.0029  269 ALA C CA  
11521 C C   . ALA C 277 ? 0.5761 0.8391 0.9671 0.2285  0.0056  -0.0047 269 ALA C C   
11522 O O   . ALA C 277 ? 0.5915 0.8354 0.9763 0.2291  0.0226  -0.0108 269 ALA C O   
11523 C CB  . ALA C 277 ? 0.6135 0.8752 1.0310 0.2525  -0.0171 0.0104  269 ALA C CB  
11524 N N   . THR C 278 ? 0.5577 0.8228 0.9240 0.2168  -0.0042 -0.0049 270 THR C N   
11525 C CA  . THR C 278 ? 0.5555 0.8012 0.8942 0.2048  0.0035  -0.0138 270 THR C CA  
11526 C C   . THR C 278 ? 0.4770 0.7368 0.8157 0.1950  0.0140  -0.0278 270 THR C C   
11527 O O   . THR C 278 ? 0.4607 0.7009 0.7832 0.1889  0.0250  -0.0372 270 THR C O   
11528 C CB  . THR C 278 ? 0.5397 0.7858 0.8551 0.1950  -0.0097 -0.0108 270 THR C CB  
11529 O OG1 . THR C 278 ? 0.5929 0.8336 0.9087 0.2037  -0.0219 0.0027  270 THR C OG1 
11530 C CG2 . THR C 278 ? 0.5111 0.7296 0.7999 0.1862  -0.0031 -0.0176 270 THR C CG2 
11531 N N   . ARG C 279 ? 0.4140 0.7071 0.7699 0.1925  0.0100  -0.0300 271 ARG C N   
11532 C CA  . ARG C 279 ? 0.4548 0.7613 0.8126 0.1826  0.0198  -0.0437 271 ARG C CA  
11533 C C   . ARG C 279 ? 0.5241 0.8169 0.8882 0.1898  0.0363  -0.0491 271 ARG C C   
11534 O O   . ARG C 279 ? 0.5084 0.7931 0.8603 0.1799  0.0467  -0.0616 271 ARG C O   
11535 C CB  . ARG C 279 ? 0.4660 0.8110 0.8440 0.1801  0.0128  -0.0444 271 ARG C CB  
11536 C CG  . ARG C 279 ? 0.3938 0.7539 0.7583 0.1653  0.0022  -0.0473 271 ARG C CG  
11537 C CD  . ARG C 279 ? 0.3914 0.7897 0.7753 0.1619  -0.0034 -0.0497 271 ARG C CD  
11538 N NE  . ARG C 279 ? 0.3863 0.7955 0.7575 0.1433  -0.0030 -0.0607 271 ARG C NE  
11539 C CZ  . ARG C 279 ? 0.3873 0.7962 0.7403 0.1336  -0.0119 -0.0595 271 ARG C CZ  
11540 N NH1 . ARG C 279 ? 0.4501 0.8492 0.7940 0.1404  -0.0228 -0.0478 271 ARG C NH1 
11541 N NH2 . ARG C 279 ? 0.3036 0.7206 0.6470 0.1168  -0.0091 -0.0700 271 ARG C NH2 
11542 N N   . LYS C 280 ? 0.5551 0.8445 0.9371 0.2068  0.0391  -0.0398 272 LYS C N   
11543 C CA  . LYS C 280 ? 0.5452 0.8230 0.9304 0.2155  0.0552  -0.0452 272 LYS C CA  
11544 C C   . LYS C 280 ? 0.5471 0.7872 0.9041 0.2139  0.0637  -0.0507 272 LYS C C   
11545 O O   . LYS C 280 ? 0.5656 0.7953 0.9143 0.2103  0.0756  -0.0635 272 LYS C O   
11546 C CB  . LYS C 280 ? 0.5584 0.8442 0.9695 0.2360  0.0563  -0.0325 272 LYS C CB  
11547 N N   . HIS C 281 ? 0.5580 0.7774 0.9005 0.2150  0.0571  -0.0425 273 HIS C N   
11548 C CA  . HIS C 281 ? 0.5280 0.7119 0.8434 0.2133  0.0640  -0.0487 273 HIS C CA  
11549 C C   . HIS C 281 ? 0.5148 0.6923 0.8115 0.1935  0.0672  -0.0625 273 HIS C C   
11550 O O   . HIS C 281 ? 0.4744 0.6291 0.7548 0.1887  0.0766  -0.0726 273 HIS C O   
11551 C CB  . HIS C 281 ? 0.5231 0.6872 0.8275 0.2183  0.0556  -0.0362 273 HIS C CB  
11552 N N   . LEU C 282 ? 0.6368 0.6488 0.7117 0.2172  0.0542  -0.1320 274 LEU C N   
11553 C CA  . LEU C 282 ? 0.6475 0.6612 0.7024 0.2055  0.0427  -0.1440 274 LEU C CA  
11554 C C   . LEU C 282 ? 0.5720 0.6181 0.5744 0.2131  0.0462  -0.1462 274 LEU C C   
11555 O O   . LEU C 282 ? 0.5649 0.6169 0.5472 0.2050  0.0400  -0.1515 274 LEU C O   
11556 C CB  . LEU C 282 ? 0.6370 0.6570 0.7082 0.1799  0.0496  -0.1218 274 LEU C CB  
11557 C CG  . LEU C 282 ? 0.6544 0.6433 0.7822 0.1725  0.0487  -0.1136 274 LEU C CG  
11558 C CD1 . LEU C 282 ? 0.6638 0.6659 0.8006 0.1559  0.0624  -0.0848 274 LEU C CD1 
11559 C CD2 . LEU C 282 ? 0.6804 0.6347 0.8356 0.1702  0.0252  -0.1404 274 LEU C CD2 
11560 N N   . GLY C 283 ? 0.5814 0.6476 0.5657 0.2238  0.0564  -0.1360 275 GLY C N   
11561 C CA  . GLY C 283 ? 0.5719 0.6674 0.5177 0.2271  0.0605  -0.1292 275 GLY C CA  
11562 C C   . GLY C 283 ? 0.5858 0.7152 0.5273 0.2087  0.0716  -0.1071 275 GLY C C   
11563 O O   . GLY C 283 ? 0.6085 0.7508 0.5295 0.2045  0.0703  -0.1047 275 GLY C O   
11564 N N   . TRP C 284 ? 0.5571 0.7000 0.5194 0.1984  0.0813  -0.0899 276 TRP C N   
11565 C CA  . TRP C 284 ? 0.4563 0.6280 0.4207 0.1798  0.0872  -0.0712 276 TRP C CA  
11566 C C   . TRP C 284 ? 0.4479 0.6452 0.4217 0.1805  0.0951  -0.0526 276 TRP C C   
11567 O O   . TRP C 284 ? 0.4540 0.6474 0.4434 0.1809  0.0975  -0.0461 276 TRP C O   
11568 C CB  . TRP C 284 ? 0.3735 0.5330 0.3533 0.1667  0.0849  -0.0714 276 TRP C CB  
11569 C CG  . TRP C 284 ? 0.3218 0.5053 0.3015 0.1478  0.0862  -0.0567 276 TRP C CG  
11570 C CD1 . TRP C 284 ? 0.3357 0.5375 0.3261 0.1426  0.0892  -0.0417 276 TRP C CD1 
11571 C CD2 . TRP C 284 ? 0.3210 0.5111 0.2902 0.1339  0.0823  -0.0574 276 TRP C CD2 
11572 N NE1 . TRP C 284 ? 0.2689 0.4863 0.2582 0.1259  0.0847  -0.0360 276 TRP C NE1 
11573 C CE2 . TRP C 284 ? 0.2710 0.4812 0.2493 0.1190  0.0820  -0.0436 276 TRP C CE2 
11574 C CE3 . TRP C 284 ? 0.3297 0.5104 0.2820 0.1352  0.0778  -0.0690 276 TRP C CE3 
11575 C CZ2 . TRP C 284 ? 0.2813 0.5005 0.2576 0.1030  0.0783  -0.0401 276 TRP C CZ2 
11576 C CZ3 . TRP C 284 ? 0.3221 0.5143 0.2693 0.1202  0.0768  -0.0625 276 TRP C CZ3 
11577 C CH2 . TRP C 284 ? 0.2936 0.5038 0.2553 0.1031  0.0775  -0.0477 276 TRP C CH2 
11578 N N   . ALA C 285 ? 0.4329 0.6567 0.3996 0.1826  0.0990  -0.0423 277 ALA C N   
11579 C CA  . ALA C 285 ? 0.4151 0.6647 0.3946 0.1846  0.1041  -0.0265 277 ALA C CA  
11580 C C   . ALA C 285 ? 0.3419 0.6222 0.3380 0.1684  0.1029  -0.0127 277 ALA C C   
11581 O O   . ALA C 285 ? 0.3694 0.6741 0.3806 0.1702  0.1039  -0.0016 277 ALA C O   
11582 C CB  . ALA C 285 ? 0.4588 0.7212 0.4283 0.2006  0.1097  -0.0221 277 ALA C CB  
11583 N N   . TYR C 286 ? 0.3020 0.5819 0.2978 0.1540  0.0993  -0.0148 278 TYR C N   
11584 C CA  . TYR C 286 ? 0.2996 0.6107 0.3153 0.1398  0.0969  -0.0041 278 TYR C CA  
11585 C C   . TYR C 286 ? 0.2663 0.5858 0.2945 0.1378  0.0899  -0.0029 278 TYR C C   
11586 O O   . TYR C 286 ? 0.3173 0.6106 0.3348 0.1403  0.0877  -0.0093 278 TYR C O   
11587 C CB  . TYR C 286 ? 0.2692 0.5744 0.2800 0.1260  0.0946  -0.0077 278 TYR C CB  
11588 C CG  . TYR C 286 ? 0.3696 0.6678 0.3636 0.1321  0.1004  -0.0080 278 TYR C CG  
11589 C CD1 . TYR C 286 ? 0.3500 0.6760 0.3555 0.1347  0.1087  0.0087  278 TYR C CD1 
11590 C CD2 . TYR C 286 ? 0.3585 0.6238 0.3272 0.1382  0.0971  -0.0240 278 TYR C CD2 
11591 C CE1 . TYR C 286 ? 0.3886 0.7087 0.3737 0.1457  0.1147  0.0109  278 TYR C CE1 
11592 C CE2 . TYR C 286 ? 0.4551 0.7153 0.4035 0.1488  0.0995  -0.0260 278 TYR C CE2 
11593 C CZ  . TYR C 286 ? 0.4306 0.7180 0.3839 0.1537  0.1089  -0.0077 278 TYR C CZ  
11594 O OH  . TYR C 286 ? 0.4406 0.7239 0.3700 0.1689  0.1118  -0.0073 278 TYR C OH  
11595 N N   . PRO C 287 ? 0.2563 0.6139 0.3099 0.1357  0.0859  0.0060  279 PRO C N   
11596 C CA  . PRO C 287 ? 0.2491 0.6189 0.3108 0.1399  0.0757  0.0046  279 PRO C CA  
11597 C C   . PRO C 287 ? 0.2423 0.5892 0.2928 0.1273  0.0643  -0.0031 279 PRO C C   
11598 O O   . PRO C 287 ? 0.2355 0.5713 0.2842 0.1118  0.0629  -0.0058 279 PRO C O   
11599 C CB  . PRO C 287 ? 0.2455 0.6608 0.3449 0.1364  0.0676  0.0127  279 PRO C CB  
11600 C CG  . PRO C 287 ? 0.2506 0.6758 0.3589 0.1372  0.0815  0.0238  279 PRO C CG  
11601 C CD  . PRO C 287 ? 0.2557 0.6484 0.3360 0.1328  0.0900  0.0189  279 PRO C CD  
11602 N N   . ALA C 288 ? 0.2804 0.6202 0.3207 0.1372  0.0569  -0.0048 280 ALA C N   
11603 C CA  . ALA C 288 ? 0.2477 0.5651 0.2726 0.1314  0.0476  -0.0102 280 ALA C CA  
11604 C C   . ALA C 288 ? 0.3495 0.6777 0.3897 0.1121  0.0312  -0.0157 280 ALA C C   
11605 O O   . ALA C 288 ? 0.2373 0.5954 0.3047 0.1089  0.0186  -0.0159 280 ALA C O   
11606 C CB  . ALA C 288 ? 0.2620 0.5799 0.2726 0.1526  0.0428  -0.0079 280 ALA C CB  
11607 N N   . PHE C 289 ? 0.2333 0.5370 0.2621 0.0988  0.0311  -0.0197 281 PHE C N   
11608 C CA  . PHE C 289 ? 0.2467 0.5519 0.2879 0.0804  0.0169  -0.0247 281 PHE C CA  
11609 C C   . PHE C 289 ? 0.3000 0.6270 0.3732 0.0653  0.0201  -0.0181 281 PHE C C   
11610 O O   . PHE C 289 ? 0.2989 0.6318 0.3951 0.0498  0.0079  -0.0193 281 PHE C O   
11611 C CB  . PHE C 289 ? 0.2369 0.5520 0.2825 0.0860  -0.0068 -0.0334 281 PHE C CB  
11612 C CG  . PHE C 289 ? 0.2519 0.5481 0.2613 0.1065  -0.0076 -0.0361 281 PHE C CG  
11613 C CD1 . PHE C 289 ? 0.2538 0.5217 0.2401 0.1039  -0.0057 -0.0380 281 PHE C CD1 
11614 C CD2 . PHE C 289 ? 0.2661 0.5747 0.2657 0.1309  -0.0075 -0.0332 281 PHE C CD2 
11615 C CE1 . PHE C 289 ? 0.2703 0.5239 0.2264 0.1261  -0.0019 -0.0346 281 PHE C CE1 
11616 C CE2 . PHE C 289 ? 0.3794 0.6732 0.3461 0.1542  -0.0039 -0.0300 281 PHE C CE2 
11617 C CZ  . PHE C 289 ? 0.3396 0.6064 0.2856 0.1523  0.0000  -0.0294 281 PHE C CZ  
11618 N N   . GLU C 290 ? 0.2175 0.5561 0.2940 0.0717  0.0374  -0.0095 282 GLU C N   
11619 C CA  . GLU C 290 ? 0.2367 0.6002 0.3417 0.0641  0.0462  0.0026  282 GLU C CA  
11620 C C   . GLU C 290 ? 0.3782 0.7233 0.4572 0.0657  0.0629  0.0041  282 GLU C C   
11621 O O   . GLU C 290 ? 0.4102 0.7523 0.4706 0.0817  0.0759  0.0040  282 GLU C O   
11622 C CB  . GLU C 290 ? 0.2171 0.6151 0.3460 0.0763  0.0525  0.0126  282 GLU C CB  
11623 N N   . ILE C 291 ? 0.2130 0.5463 0.2915 0.0514  0.0604  0.0043  283 ILE C N   
11624 C CA  . ILE C 291 ? 0.2294 0.5428 0.2795 0.0540  0.0712  0.0022  283 ILE C CA  
11625 C C   . ILE C 291 ? 0.2628 0.6021 0.3298 0.0552  0.0850  0.0199  283 ILE C C   
11626 O O   . ILE C 291 ? 0.2662 0.6214 0.3685 0.0401  0.0815  0.0317  283 ILE C O   
11627 C CB  . ILE C 291 ? 0.2186 0.5016 0.2537 0.0407  0.0610  -0.0075 283 ILE C CB  
11628 C CG1 . ILE C 291 ? 0.2121 0.4723 0.2316 0.0442  0.0521  -0.0191 283 ILE C CG1 
11629 C CG2 . ILE C 291 ? 0.2592 0.5252 0.2688 0.0442  0.0693  -0.0104 283 ILE C CG2 
11630 C CD1 . ILE C 291 ? 0.2077 0.4425 0.2160 0.0332  0.0427  -0.0257 283 ILE C CD1 
11631 N N   . PRO C 292 ? 0.2723 0.6160 0.3166 0.0748  0.1008  0.0229  284 PRO C N   
11632 C CA  . PRO C 292 ? 0.2982 0.6604 0.3535 0.0806  0.1147  0.0439  284 PRO C CA  
11633 C C   . PRO C 292 ? 0.2890 0.6455 0.3437 0.0696  0.1163  0.0498  284 PRO C C   
11634 O O   . PRO C 292 ? 0.2944 0.6247 0.3218 0.0648  0.1084  0.0333  284 PRO C O   
11635 C CB  . PRO C 292 ? 0.3433 0.6864 0.3586 0.1052  0.1200  0.0376  284 PRO C CB  
11636 C CG  . PRO C 292 ? 0.3691 0.6786 0.3541 0.1076  0.1086  0.0114  284 PRO C CG  
11637 C CD  . PRO C 292 ? 0.2794 0.5954 0.2864 0.0922  0.1005  0.0064  284 PRO C CD  
11638 N N   . GLN C 293 ? 0.3050 0.6834 0.3939 0.0655  0.1261  0.0750  285 GLN C N   
11639 C CA  . GLN C 293 ? 0.3228 0.6986 0.4239 0.0523  0.1277  0.0853  285 GLN C CA  
11640 C C   . GLN C 293 ? 0.3335 0.6810 0.3798 0.0666  0.1306  0.0759  285 GLN C C   
11641 O O   . GLN C 293 ? 0.2858 0.6215 0.3267 0.0553  0.1268  0.0731  285 GLN C O   
11642 C CB  . GLN C 293 ? 0.3755 0.7754 0.5282 0.0481  0.1387  0.1167  285 GLN C CB  
11643 C CG  . GLN C 293 ? 0.3671 0.7637 0.5479 0.0307  0.1386  0.1299  285 GLN C CG  
11644 C CD  . GLN C 293 ? 0.4946 0.8870 0.7000 0.0045  0.1183  0.1143  285 GLN C CD  
11645 O OE1 . GLN C 293 ? 0.5429 0.9385 0.7766 -0.0065 0.1003  0.1032  285 GLN C OE1 
11646 N NE2 . GLN C 293 ? 0.5291 0.8934 0.7098 -0.0032 0.1128  0.1062  285 GLN C NE2 
11647 N N   . GLU C 294 ? 0.3051 0.6420 0.3129 0.0917  0.1343  0.0697  286 GLU C N   
11648 C CA  . GLU C 294 ? 0.3284 0.6404 0.2893 0.1072  0.1312  0.0573  286 GLU C CA  
11649 C C   . GLU C 294 ? 0.3664 0.6491 0.3049 0.0972  0.1150  0.0288  286 GLU C C   
11650 O O   . GLU C 294 ? 0.4180 0.6824 0.3336 0.0984  0.1097  0.0206  286 GLU C O   
11651 C CB  . GLU C 294 ? 0.3736 0.6825 0.3029 0.1375  0.1336  0.0535  286 GLU C CB  
11652 N N   . ILE C 295 ? 0.3191 0.5974 0.2660 0.0885  0.1071  0.0148  287 ILE C N   
11653 C CA  . ILE C 295 ? 0.3087 0.5597 0.2406 0.0796  0.0933  -0.0085 287 ILE C CA  
11654 C C   . ILE C 295 ? 0.3326 0.5801 0.2820 0.0550  0.0877  -0.0038 287 ILE C C   
11655 O O   . ILE C 295 ? 0.3450 0.5674 0.2780 0.0493  0.0787  -0.0155 287 ILE C O   
11656 C CB  . ILE C 295 ? 0.3158 0.5611 0.2531 0.0809  0.0878  -0.0210 287 ILE C CB  
11657 C CG1 . ILE C 295 ? 0.3158 0.5505 0.2338 0.1043  0.0878  -0.0296 287 ILE C CG1 
11658 C CG2 . ILE C 295 ? 0.2914 0.5042 0.2270 0.0673  0.0733  -0.0371 287 ILE C CG2 
11659 C CD1 . ILE C 295 ? 0.3141 0.5398 0.2382 0.1084  0.0839  -0.0408 287 ILE C CD1 
11660 N N   . TYR C 296 ? 0.2643 0.5322 0.2512 0.0400  0.0896  0.0129  288 TYR C N   
11661 C CA  . TYR C 296 ? 0.2732 0.5315 0.2791 0.0178  0.0803  0.0161  288 TYR C CA  
11662 C C   . TYR C 296 ? 0.2602 0.5166 0.2551 0.0193  0.0882  0.0259  288 TYR C C   
11663 O O   . TYR C 296 ? 0.2605 0.4950 0.2483 0.0074  0.0791  0.0191  288 TYR C O   
11664 C CB  . TYR C 296 ? 0.2320 0.5133 0.2876 0.0038  0.0772  0.0299  288 TYR C CB  
11665 C CG  . TYR C 296 ? 0.2081 0.4843 0.2749 -0.0028 0.0607  0.0166  288 TYR C CG  
11666 C CD1 . TYR C 296 ? 0.2472 0.4950 0.2964 -0.0097 0.0456  -0.0002 288 TYR C CD1 
11667 C CD2 . TYR C 296 ? 0.2064 0.5094 0.3024 0.0007  0.0610  0.0232  288 TYR C CD2 
11668 C CE1 . TYR C 296 ? 0.2863 0.5322 0.3407 -0.0092 0.0319  -0.0101 288 TYR C CE1 
11669 C CE2 . TYR C 296 ? 0.2785 0.5794 0.3819 -0.0011 0.0450  0.0112  288 TYR C CE2 
11670 C CZ  . TYR C 296 ? 0.2754 0.5479 0.3555 -0.0044 0.0308  -0.0053 288 TYR C CZ  
11671 O OH  . TYR C 296 ? 0.2434 0.5167 0.3254 0.0003  0.0162  -0.0154 288 TYR C OH  
11672 N N   . ASP C 297 ? 0.2974 0.5786 0.2902 0.0368  0.1068  0.0445  289 ASP C N   
11673 C CA  . ASP C 297 ? 0.3684 0.6502 0.3475 0.0435  0.1165  0.0571  289 ASP C CA  
11674 C C   . ASP C 297 ? 0.4334 0.6838 0.3629 0.0546  0.1055  0.0328  289 ASP C C   
11675 O O   . ASP C 297 ? 0.4721 0.7110 0.3909 0.0504  0.1033  0.0335  289 ASP C O   
11676 C CB  . ASP C 297 ? 0.4037 0.7013 0.3885 0.0632  0.1320  0.0804  289 ASP C CB  
11677 C CG  . ASP C 297 ? 0.4006 0.7271 0.4451 0.0512  0.1412  0.1063  289 ASP C CG  
11678 O OD1 . ASP C 297 ? 0.4038 0.7371 0.4915 0.0254  0.1343  0.1096  289 ASP C OD1 
11679 O OD2 . ASP C 297 ? 0.4422 0.7844 0.4938 0.0680  0.1526  0.1228  289 ASP C OD2 
11680 N N   . ALA C 298 ? 0.4318 0.6675 0.3371 0.0684  0.0970  0.0116  290 ALA C N   
11681 C CA  . ALA C 298 ? 0.4155 0.6215 0.2878 0.0774  0.0826  -0.0123 290 ALA C CA  
11682 C C   . ALA C 298 ? 0.3683 0.5564 0.2443 0.0568  0.0708  -0.0264 290 ALA C C   
11683 O O   . ALA C 298 ? 0.3602 0.5279 0.2195 0.0582  0.0606  -0.0383 290 ALA C O   
11684 C CB  . ALA C 298 ? 0.3668 0.5616 0.2240 0.0955  0.0749  -0.0307 290 ALA C CB  
11685 N N   . TRP C 299 ? 0.3359 0.5218 0.2406 0.0366  0.0671  -0.0235 291 TRP C N   
11686 C CA  . TRP C 299 ? 0.2432 0.4041 0.1554 0.0188  0.0541  -0.0337 291 TRP C CA  
11687 C C   . TRP C 299 ? 0.2866 0.4455 0.2116 0.0012  0.0528  -0.0226 291 TRP C C   
11688 O O   . TRP C 299 ? 0.2873 0.4248 0.2102 -0.0086 0.0435  -0.0303 291 TRP C O   
11689 C CB  . TRP C 299 ? 0.2296 0.3887 0.1587 0.0131  0.0502  -0.0371 291 TRP C CB  
11690 C CG  . TRP C 299 ? 0.2961 0.4376 0.2184 0.0224  0.0449  -0.0526 291 TRP C CG  
11691 C CD1 . TRP C 299 ? 0.3205 0.4676 0.2419 0.0365  0.0481  -0.0576 291 TRP C CD1 
11692 C CD2 . TRP C 299 ? 0.3238 0.4386 0.2466 0.0186  0.0360  -0.0634 291 TRP C CD2 
11693 N NE1 . TRP C 299 ? 0.2984 0.4218 0.2227 0.0408  0.0406  -0.0714 291 TRP C NE1 
11694 C CE2 . TRP C 299 ? 0.3198 0.4245 0.2482 0.0296  0.0336  -0.0739 291 TRP C CE2 
11695 C CE3 . TRP C 299 ? 0.3243 0.4237 0.2480 0.0077  0.0304  -0.0635 291 TRP C CE3 
11696 C CZ2 . TRP C 299 ? 0.2893 0.3697 0.2318 0.0285  0.0262  -0.0824 291 TRP C CZ2 
11697 C CZ3 . TRP C 299 ? 0.3077 0.3853 0.2411 0.0078  0.0240  -0.0716 291 TRP C CZ3 
11698 C CH2 . TRP C 299 ? 0.2722 0.3409 0.2187 0.0174  0.0221  -0.0799 291 TRP C CH2 
11699 N N   . ASN C 300 ? 0.3221 0.5025 0.2651 -0.0022 0.0624  -0.0033 292 ASN C N   
11700 C CA  . ASN C 300 ? 0.3247 0.5009 0.2896 -0.0202 0.0586  0.0062  292 ASN C CA  
11701 C C   . ASN C 300 ? 0.3265 0.4856 0.2707 -0.0203 0.0572  0.0042  292 ASN C C   
11702 O O   . ASN C 300 ? 0.2986 0.4643 0.2215 -0.0050 0.0658  0.0087  292 ASN C O   
11703 C CB  . ASN C 300 ? 0.3510 0.5548 0.3522 -0.0236 0.0699  0.0302  292 ASN C CB  
11704 C CG  . ASN C 300 ? 0.3223 0.5196 0.3596 -0.0442 0.0602  0.0357  292 ASN C CG  
11705 O OD1 . ASN C 300 ? 0.3231 0.5136 0.3647 -0.0494 0.0631  0.0454  292 ASN C OD1 
11706 N ND2 . ASN C 300 ? 0.2872 0.4852 0.3493 -0.0538 0.0464  0.0276  292 ASN C ND2 
11707 N N   . ALA C 301 ? 0.2834 0.4213 0.2309 -0.0342 0.0458  -0.0028 293 ALA C N   
11708 C CA  . ALA C 301 ? 0.2941 0.4150 0.2241 -0.0351 0.0431  -0.0052 293 ALA C CA  
11709 C C   . ALA C 301 ? 0.2750 0.3944 0.2244 -0.0471 0.0445  0.0093  293 ALA C C   
11710 O O   . ALA C 301 ? 0.3150 0.4179 0.2525 -0.0499 0.0408  0.0072  293 ALA C O   
11711 C CB  . ALA C 301 ? 0.2960 0.3929 0.2148 -0.0383 0.0313  -0.0220 293 ALA C CB  
11712 N N   . LYS C 302 ? 0.2592 0.3952 0.2440 -0.0543 0.0490  0.0244  294 LYS C N   
11713 C CA  . LYS C 302 ? 0.2643 0.3954 0.2793 -0.0675 0.0473  0.0372  294 LYS C CA  
11714 C C   . LYS C 302 ? 0.3071 0.4408 0.3108 -0.0599 0.0614  0.0543  294 LYS C C   
11715 O O   . LYS C 302 ? 0.3361 0.4514 0.3369 -0.0663 0.0566  0.0543  294 LYS C O   
11716 C CB  . LYS C 302 ? 0.2317 0.3826 0.3000 -0.0767 0.0482  0.0512  294 LYS C CB  
11717 N N   . GLU C 303 ? 0.2582 0.4154 0.2518 -0.0426 0.0792  0.0695  295 GLU C N   
11718 C CA  . GLU C 303 ? 0.2777 0.4417 0.2570 -0.0290 0.0944  0.0889  295 GLU C CA  
11719 C C   . GLU C 303 ? 0.3381 0.4804 0.2725 -0.0223 0.0845  0.0701  295 GLU C C   
11720 O O   . GLU C 303 ? 0.2882 0.4210 0.2208 -0.0240 0.0865  0.0791  295 GLU C O   
11721 C CB  . GLU C 303 ? 0.3778 0.5727 0.3444 -0.0033 0.1153  0.1068  295 GLU C CB  
11722 C CG  . GLU C 303 ? 0.4869 0.6834 0.4287 0.0192  0.1271  0.1214  295 GLU C CG  
11723 C CD  . GLU C 303 ? 0.6625 0.8775 0.5974 0.0469  0.1397  0.1344  295 GLU C CD  
11724 O OE1 . GLU C 303 ? 0.7088 0.9391 0.6623 0.0471  0.1439  0.1377  295 GLU C OE1 
11725 O OE2 . GLU C 303 ? 0.7459 0.9622 0.6571 0.0703  0.1449  0.1422  295 GLU C OE2 
11726 N N   . LYS C 304 ? 0.3525 0.4869 0.2563 -0.0147 0.0734  0.0448  296 LYS C N   
11727 C CA  . LYS C 304 ? 0.3437 0.4596 0.2158 -0.0089 0.0620  0.0269  296 LYS C CA  
11728 C C   . LYS C 304 ? 0.2732 0.3648 0.1582 -0.0290 0.0505  0.0205  296 LYS C C   
11729 O O   . LYS C 304 ? 0.2925 0.3726 0.1641 -0.0273 0.0474  0.0200  296 LYS C O   
11730 C CB  . LYS C 304 ? 0.3235 0.4355 0.1744 0.0022  0.0511  0.0023  296 LYS C CB  
11731 N N   . GLY C 305 ? 0.2474 0.3317 0.1553 -0.0446 0.0436  0.0152  297 GLY C N   
11732 C CA  . GLY C 305 ? 0.2387 0.3003 0.1529 -0.0577 0.0326  0.0082  297 GLY C CA  
11733 C C   . GLY C 305 ? 0.3097 0.3653 0.2391 -0.0651 0.0357  0.0233  297 GLY C C   
11734 O O   . GLY C 305 ? 0.2721 0.3096 0.1917 -0.0675 0.0303  0.0198  297 GLY C O   
11735 N N   . ALA C 306 ? 0.2692 0.3406 0.2277 -0.0681 0.0457  0.0427  298 ALA C N   
11736 C CA  . ALA C 306 ? 0.2646 0.3301 0.2487 -0.0756 0.0500  0.0607  298 ALA C CA  
11737 C C   . ALA C 306 ? 0.3626 0.4282 0.3195 -0.0627 0.0604  0.0715  298 ALA C C   
11738 O O   . ALA C 306 ? 0.3287 0.3774 0.2891 -0.0678 0.0578  0.0757  298 ALA C O   
11739 C CB  . ALA C 306 ? 0.3107 0.3968 0.3436 -0.0809 0.0607  0.0839  298 ALA C CB  
11740 N N   . LYS C 307 ? 0.2874 0.3721 0.2156 -0.0431 0.0710  0.0752  299 LYS C N   
11741 C CA  . LYS C 307 ? 0.3053 0.3916 0.2016 -0.0256 0.0773  0.0817  299 LYS C CA  
11742 C C   . LYS C 307 ? 0.3226 0.3863 0.1948 -0.0284 0.0605  0.0588  299 LYS C C   
11743 O O   . LYS C 307 ? 0.3079 0.3643 0.1678 -0.0232 0.0614  0.0646  299 LYS C O   
11744 C CB  . LYS C 307 ? 0.3236 0.4340 0.1883 0.0015  0.0870  0.0840  299 LYS C CB  
11745 N N   . LEU C 308 ? 0.2802 0.3344 0.1487 -0.0350 0.0467  0.0356  300 LEU C N   
11746 C CA  . LEU C 308 ? 0.3148 0.3508 0.1698 -0.0369 0.0332  0.0179  300 LEU C CA  
11747 C C   . LEU C 308 ? 0.3174 0.3334 0.1843 -0.0495 0.0301  0.0226  300 LEU C C   
11748 O O   . LEU C 308 ? 0.2886 0.2953 0.1432 -0.0456 0.0272  0.0222  300 LEU C O   
11749 C CB  . LEU C 308 ? 0.2569 0.2889 0.1150 -0.0405 0.0237  -0.0009 300 LEU C CB  
11750 C CG  . LEU C 308 ? 0.2540 0.2692 0.1113 -0.0434 0.0129  -0.0140 300 LEU C CG  
11751 C CD1 . LEU C 308 ? 0.2801 0.2985 0.1240 -0.0305 0.0057  -0.0236 300 LEU C CD1 
11752 C CD2 . LEU C 308 ? 0.2469 0.2582 0.1164 -0.0484 0.0092  -0.0231 300 LEU C CD2 
11753 N N   . GLU C 309 ? 0.2636 0.2725 0.1548 -0.0627 0.0286  0.0253  301 GLU C N   
11754 C CA  . GLU C 309 ? 0.3064 0.2931 0.2072 -0.0715 0.0219  0.0251  301 GLU C CA  
11755 C C   . GLU C 309 ? 0.2908 0.2750 0.2020 -0.0719 0.0303  0.0446  301 GLU C C   
11756 O O   . GLU C 309 ? 0.2884 0.2546 0.1941 -0.0725 0.0265  0.0445  301 GLU C O   
11757 C CB  . GLU C 309 ? 0.2628 0.2421 0.1860 -0.0815 0.0126  0.0174  301 GLU C CB  
11758 C CG  . GLU C 309 ? 0.3290 0.2825 0.2579 -0.0859 0.0011  0.0114  301 GLU C CG  
11759 C CD  . GLU C 309 ? 0.3650 0.3099 0.3004 -0.0871 -0.0137 -0.0050 301 GLU C CD  
11760 O OE1 . GLU C 309 ? 0.3639 0.3235 0.2999 -0.0859 -0.0137 -0.0103 301 GLU C OE1 
11761 O OE2 . GLU C 309 ? 0.3218 0.2451 0.2595 -0.0864 -0.0265 -0.0137 301 GLU C OE2 
11762 N N   . ALA C 310 ? 0.3108 0.3139 0.2381 -0.0693 0.0438  0.0643  302 ALA C N   
11763 C CA  . ALA C 310 ? 0.3092 0.3124 0.2488 -0.0662 0.0561  0.0887  302 ALA C CA  
11764 C C   . ALA C 310 ? 0.3178 0.3209 0.2191 -0.0507 0.0589  0.0890  302 ALA C C   
11765 O O   . ALA C 310 ? 0.3314 0.3215 0.2346 -0.0503 0.0612  0.0992  302 ALA C O   
11766 C CB  . ALA C 310 ? 0.3199 0.3492 0.2841 -0.0609 0.0750  0.1154  302 ALA C CB  
11767 N N   . GLY C 311 ? 0.3238 0.3406 0.1926 -0.0368 0.0565  0.0763  303 GLY C N   
11768 C CA  . GLY C 311 ? 0.3601 0.3778 0.1964 -0.0210 0.0535  0.0719  303 GLY C CA  
11769 C C   . GLY C 311 ? 0.3150 0.3099 0.1490 -0.0296 0.0403  0.0579  303 GLY C C   
11770 O O   . GLY C 311 ? 0.3317 0.3209 0.1547 -0.0228 0.0408  0.0640  303 GLY C O   
11771 N N   . TRP C 312 ? 0.2963 0.2797 0.1400 -0.0418 0.0300  0.0413  304 TRP C N   
11772 C CA  . TRP C 312 ? 0.3259 0.2896 0.1681 -0.0463 0.0211  0.0324  304 TRP C CA  
11773 C C   . TRP C 312 ? 0.3467 0.2913 0.2004 -0.0528 0.0236  0.0436  304 TRP C C   
11774 O O   . TRP C 312 ? 0.3318 0.2644 0.1768 -0.0490 0.0215  0.0448  304 TRP C O   
11775 C CB  . TRP C 312 ? 0.2734 0.2314 0.1218 -0.0524 0.0132  0.0167  304 TRP C CB  
11776 C CG  . TRP C 312 ? 0.2999 0.2418 0.1453 -0.0513 0.0078  0.0115  304 TRP C CG  
11777 C CD1 . TRP C 312 ? 0.2999 0.2449 0.1433 -0.0450 0.0041  0.0062  304 TRP C CD1 
11778 C CD2 . TRP C 312 ? 0.3479 0.2691 0.1948 -0.0539 0.0055  0.0122  304 TRP C CD2 
11779 N NE1 . TRP C 312 ? 0.2883 0.2184 0.1315 -0.0429 0.0035  0.0076  304 TRP C NE1 
11780 C CE2 . TRP C 312 ? 0.2845 0.1990 0.1246 -0.0464 0.0038  0.0097  304 TRP C CE2 
11781 C CE3 . TRP C 312 ? 0.3235 0.2308 0.1802 -0.0602 0.0029  0.0137  304 TRP C CE3 
11782 C CZ2 . TRP C 312 ? 0.3214 0.2162 0.1548 -0.0415 0.0017  0.0090  304 TRP C CZ2 
11783 C CZ3 . TRP C 312 ? 0.4043 0.2892 0.2561 -0.0564 -0.0038 0.0085  304 TRP C CZ3 
11784 C CH2 . TRP C 312 ? 0.3519 0.2310 0.1874 -0.0454 -0.0033 0.0063  304 TRP C CH2 
11785 N N   . ASN C 313 ? 0.3058 0.2473 0.1839 -0.0622 0.0268  0.0519  305 ASN C N   
11786 C CA  . ASN C 313 ? 0.3209 0.2419 0.2188 -0.0685 0.0263  0.0614  305 ASN C CA  
11787 C C   . ASN C 313 ? 0.3513 0.2742 0.2425 -0.0596 0.0376  0.0811  305 ASN C C   
11788 O O   . ASN C 313 ? 0.3479 0.2504 0.2400 -0.0596 0.0350  0.0837  305 ASN C O   
11789 C CB  . ASN C 313 ? 0.3259 0.2470 0.2644 -0.0804 0.0266  0.0689  305 ASN C CB  
11790 C CG  . ASN C 313 ? 0.4101 0.3221 0.3569 -0.0879 0.0106  0.0473  305 ASN C CG  
11791 O OD1 . ASN C 313 ? 0.4763 0.3970 0.4529 -0.0959 0.0086  0.0487  305 ASN C OD1 
11792 N ND2 . ASN C 313 ? 0.3429 0.2395 0.2646 -0.0826 -0.0000 0.0294  305 ASN C ND2 
11793 N N   . GLU C 314 ? 0.3548 0.3026 0.2364 -0.0484 0.0505  0.0956  306 GLU C N   
11794 C CA  . GLU C 314 ? 0.3619 0.3150 0.2305 -0.0341 0.0619  0.1153  306 GLU C CA  
11795 C C   . GLU C 314 ? 0.3692 0.3156 0.2078 -0.0255 0.0522  0.1018  306 GLU C C   
11796 O O   . GLU C 314 ? 0.3737 0.3093 0.2091 -0.0205 0.0555  0.1127  306 GLU C O   
11797 C CB  . GLU C 314 ? 0.4771 0.4610 0.3319 -0.0161 0.0766  0.1311  306 GLU C CB  
11798 C CG  . GLU C 314 ? 0.5477 0.5435 0.4384 -0.0214 0.0915  0.1530  306 GLU C CG  
11799 C CD  . GLU C 314 ? 0.7096 0.7334 0.5887 0.0025  0.1059  0.1674  306 GLU C CD  
11800 O OE1 . GLU C 314 ? 0.7377 0.7702 0.5805 0.0234  0.1024  0.1596  306 GLU C OE1 
11801 O OE2 . GLU C 314 ? 0.7472 0.7843 0.6583 0.0016  0.1178  0.1837  306 GLU C OE2 
11802 N N   . LEU C 315 ? 0.3485 0.3018 0.1706 -0.0235 0.0406  0.0798  307 LEU C N   
11803 C CA  . LEU C 315 ? 0.3830 0.3320 0.1892 -0.0171 0.0305  0.0681  307 LEU C CA  
11804 C C   . LEU C 315 ? 0.3843 0.3072 0.2002 -0.0264 0.0264  0.0654  307 LEU C C   
11805 O O   . LEU C 315 ? 0.3788 0.2943 0.1867 -0.0197 0.0254  0.0692  307 LEU C O   
11806 C CB  . LEU C 315 ? 0.3447 0.3055 0.1459 -0.0151 0.0189  0.0472  307 LEU C CB  
11807 C CG  . LEU C 315 ? 0.3313 0.2903 0.1312 -0.0105 0.0074  0.0360  307 LEU C CG  
11808 C CD1 . LEU C 315 ? 0.3741 0.3456 0.1566 0.0072  0.0044  0.0399  307 LEU C CD1 
11809 C CD2 . LEU C 315 ? 0.3523 0.3182 0.1642 -0.0134 -0.0031 0.0180  307 LEU C CD2 
11810 N N   . PHE C 316 ? 0.3290 0.2383 0.1598 -0.0386 0.0229  0.0580  308 PHE C N   
11811 C CA  . PHE C 316 ? 0.3968 0.2803 0.2305 -0.0414 0.0174  0.0533  308 PHE C CA  
11812 C C   . PHE C 316 ? 0.4076 0.2733 0.2510 -0.0420 0.0218  0.0677  308 PHE C C   
11813 O O   . PHE C 316 ? 0.4271 0.2736 0.2638 -0.0371 0.0186  0.0665  308 PHE C O   
11814 C CB  . PHE C 316 ? 0.3284 0.2022 0.1716 -0.0490 0.0099  0.0398  308 PHE C CB  
11815 C CG  . PHE C 316 ? 0.3987 0.2481 0.2345 -0.0438 0.0021  0.0305  308 PHE C CG  
11816 C CD1 . PHE C 316 ? 0.3871 0.2382 0.2070 -0.0331 0.0023  0.0265  308 PHE C CD1 
11817 C CD2 . PHE C 316 ? 0.4187 0.2438 0.2661 -0.0470 -0.0059 0.0263  308 PHE C CD2 
11818 C CE1 . PHE C 316 ? 0.3484 0.1793 0.1563 -0.0222 -0.0020 0.0205  308 PHE C CE1 
11819 C CE2 . PHE C 316 ? 0.4102 0.2118 0.2435 -0.0361 -0.0150 0.0148  308 PHE C CE2 
11820 C CZ  . PHE C 316 ? 0.3718 0.1774 0.1812 -0.0219 -0.0112 0.0131  308 PHE C CZ  
11821 N N   . ALA C 317 ? 0.3656 0.2373 0.2279 -0.0463 0.0306  0.0838  309 ALA C N   
11822 C CA  . ALA C 317 ? 0.3885 0.2439 0.2680 -0.0461 0.0371  0.1023  309 ALA C CA  
11823 C C   . ALA C 317 ? 0.4462 0.3065 0.3014 -0.0313 0.0438  0.1131  309 ALA C C   
11824 O O   . ALA C 317 ? 0.4137 0.2526 0.2714 -0.0286 0.0436  0.1188  309 ALA C O   
11825 C CB  . ALA C 317 ? 0.4393 0.3057 0.3519 -0.0515 0.0496  0.1244  309 ALA C CB  
11826 N N   . GLN C 318 ? 0.4632 0.3511 0.2951 -0.0198 0.0476  0.1143  310 GLN C N   
11827 C CA  A GLN C 318 ? 0.4807 0.3766 0.2892 -0.0034 0.0496  0.1208  310 GLN C CA  
11828 C CA  B GLN C 318 ? 0.4797 0.3754 0.2884 -0.0035 0.0497  0.1209  310 GLN C CA  
11829 C C   . GLN C 318 ? 0.4683 0.3489 0.2688 -0.0032 0.0388  0.1065  310 GLN C C   
11830 O O   . GLN C 318 ? 0.4263 0.2966 0.2211 0.0047  0.0411  0.1155  310 GLN C O   
11831 C CB  A GLN C 318 ? 0.4555 0.3830 0.2415 0.0107  0.0483  0.1162  310 GLN C CB  
11832 C CB  B GLN C 318 ? 0.4581 0.3854 0.2438 0.0112  0.0487  0.1170  310 GLN C CB  
11833 C CG  A GLN C 318 ? 0.4943 0.4376 0.2620 0.0307  0.0479  0.1216  310 GLN C CG  
11834 C CG  B GLN C 318 ? 0.4862 0.4334 0.2751 0.0189  0.0616  0.1332  310 GLN C CG  
11835 C CD  A GLN C 318 ? 0.5703 0.5429 0.3214 0.0463  0.0418  0.1107  310 GLN C CD  
11836 C CD  B GLN C 318 ? 0.5804 0.5566 0.3462 0.0381  0.0553  0.1217  310 GLN C CD  
11837 O OE1 A GLN C 318 ? 0.6002 0.5820 0.3520 0.0435  0.0430  0.1057  310 GLN C OE1 
11838 O OE1 B GLN C 318 ? 0.5781 0.5591 0.3280 0.0433  0.0400  0.1022  310 GLN C OE1 
11839 N NE2 A GLN C 318 ? 0.5435 0.5297 0.2798 0.0646  0.0340  0.1056  310 GLN C NE2 
11840 N NE2 B GLN C 318 ? 0.6223 0.6167 0.3892 0.0508  0.0663  0.1335  310 GLN C NE2 
11841 N N   . TYR C 319 ? 0.3739 0.2543 0.1753 -0.0098 0.0290  0.0871  311 TYR C N   
11842 C CA  . TYR C 319 ? 0.4329 0.3023 0.2301 -0.0068 0.0224  0.0776  311 TYR C CA  
11843 C C   . TYR C 319 ? 0.4539 0.2917 0.2542 -0.0078 0.0227  0.0801  311 TYR C C   
11844 O O   . TYR C 319 ? 0.4999 0.3277 0.2919 0.0017  0.0230  0.0835  311 TYR C O   
11845 C CB  . TYR C 319 ? 0.4195 0.2962 0.2215 -0.0119 0.0160  0.0616  311 TYR C CB  
11846 C CG  . TYR C 319 ? 0.3803 0.2516 0.1822 -0.0056 0.0132  0.0564  311 TYR C CG  
11847 C CD1 . TYR C 319 ? 0.3849 0.2330 0.1819 -0.0031 0.0131  0.0530  311 TYR C CD1 
11848 C CD2 . TYR C 319 ? 0.3301 0.2208 0.1402 0.0002  0.0101  0.0552  311 TYR C CD2 
11849 C CE1 . TYR C 319 ? 0.3522 0.1983 0.1463 0.0081  0.0145  0.0525  311 TYR C CE1 
11850 C CE2 . TYR C 319 ? 0.3260 0.2153 0.1445 0.0072  0.0115  0.0565  311 TYR C CE2 
11851 C CZ  . TYR C 319 ? 0.4433 0.3111 0.2506 0.0126  0.0160  0.0571  311 TYR C CZ  
11852 O OH  . TYR C 319 ? 0.3865 0.2549 0.1981 0.0252  0.0213  0.0624  311 TYR C OH  
11853 N N   . GLN C 320 ? 0.4281 0.2495 0.2427 -0.0179 0.0206  0.0770  312 GLN C N   
11854 C CA  . GLN C 320 ? 0.4428 0.2306 0.2635 -0.0173 0.0152  0.0736  312 GLN C CA  
11855 C C   . GLN C 320 ? 0.5170 0.2923 0.3419 -0.0121 0.0222  0.0913  312 GLN C C   
11856 O O   . GLN C 320 ? 0.5559 0.3069 0.3740 -0.0038 0.0184  0.0886  312 GLN C O   
11857 C CB  . GLN C 320 ? 0.4211 0.1959 0.2661 -0.0298 0.0075  0.0657  312 GLN C CB  
11858 N N   . ALA C 321 ? 0.4428 0.2350 0.2770 -0.0135 0.0336  0.1110  313 ALA C N   
11859 C CA  . ALA C 321 ? 0.4638 0.2467 0.3034 -0.0062 0.0434  0.1325  313 ALA C CA  
11860 C C   . ALA C 321 ? 0.5198 0.3043 0.3325 0.0090  0.0432  0.1325  313 ALA C C   
11861 O O   . ALA C 321 ? 0.5699 0.3326 0.3842 0.0157  0.0455  0.1412  313 ALA C O   
11862 C CB  . ALA C 321 ? 0.4717 0.2800 0.3187 -0.0033 0.0588  0.1566  313 ALA C CB  
11863 N N   . LYS C 322 ? 0.4439 0.2535 0.2373 0.0145  0.0395  0.1228  314 LYS C N   
11864 C CA  . LYS C 322 ? 0.4986 0.3162 0.2769 0.0281  0.0379  0.1231  314 LYS C CA  
11865 C C   . LYS C 322 ? 0.5160 0.3177 0.2886 0.0310  0.0315  0.1098  314 LYS C C   
11866 O O   . LYS C 322 ? 0.5077 0.3055 0.2762 0.0423  0.0323  0.1130  314 LYS C O   
11867 C CB  . LYS C 322 ? 0.5042 0.3598 0.2763 0.0339  0.0343  0.1194  314 LYS C CB  
11868 N N   . TYR C 323 ? 0.4492 0.2683 0.2552 0.0294  0.0061  0.1038  315 TYR C N   
11869 C CA  . TYR C 323 ? 0.3966 0.2181 0.2148 0.0335  0.0050  0.0997  315 TYR C CA  
11870 C C   . TYR C 323 ? 0.4371 0.2533 0.2593 0.0280  0.0121  0.0963  315 TYR C C   
11871 O O   . TYR C 323 ? 0.4633 0.2861 0.2898 0.0256  0.0147  0.0913  315 TYR C O   
11872 C CB  . TYR C 323 ? 0.4208 0.2557 0.2427 0.0362  0.0013  0.0956  315 TYR C CB  
11873 C CG  . TYR C 323 ? 0.4061 0.2475 0.2240 0.0405  -0.0060 0.0984  315 TYR C CG  
11874 C CD1 . TYR C 323 ? 0.4778 0.3200 0.3020 0.0476  -0.0124 0.1008  315 TYR C CD1 
11875 C CD2 . TYR C 323 ? 0.4089 0.2560 0.2169 0.0372  -0.0064 0.0985  315 TYR C CD2 
11876 C CE1 . TYR C 323 ? 0.4831 0.3320 0.3042 0.0510  -0.0194 0.1034  315 TYR C CE1 
11877 C CE2 . TYR C 323 ? 0.4077 0.2605 0.2116 0.0406  -0.0134 0.1008  315 TYR C CE2 
11878 C CZ  . TYR C 323 ? 0.5201 0.3739 0.3307 0.0473  -0.0200 0.1035  315 TYR C CZ  
11879 O OH  . TYR C 323 ? 0.5209 0.3812 0.3282 0.0501  -0.0271 0.1060  315 TYR C OH  
11880 N N   . PRO C 324 ? 0.4574 0.2615 0.2783 0.0256  0.0153  0.0987  316 PRO C N   
11881 C CA  . PRO C 324 ? 0.4223 0.2219 0.2468 0.0192  0.0219  0.0952  316 PRO C CA  
11882 C C   . PRO C 324 ? 0.4422 0.2435 0.2780 0.0220  0.0220  0.0902  316 PRO C C   
11883 O O   . PRO C 324 ? 0.4252 0.2292 0.2645 0.0166  0.0265  0.0858  316 PRO C O   
11884 C CB  . PRO C 324 ? 0.4806 0.2664 0.3006 0.0170  0.0239  0.0994  316 PRO C CB  
11885 C CG  . PRO C 324 ? 0.4892 0.2714 0.3079 0.0249  0.0176  0.1041  316 PRO C CG  
11886 C CD  . PRO C 324 ? 0.5037 0.2979 0.3198 0.0283  0.0128  0.1047  316 PRO C CD  
11887 N N   . ALA C 325 ? 0.4816 0.2824 0.3236 0.0300  0.0171  0.0905  317 ALA C N   
11888 C CA  . ALA C 325 ? 0.4678 0.2710 0.3207 0.0327  0.0175  0.0855  317 ALA C CA  
11889 C C   . ALA C 325 ? 0.4271 0.2483 0.2874 0.0314  0.0163  0.0797  317 ALA C C   
11890 O O   . ALA C 325 ? 0.3996 0.2267 0.2682 0.0273  0.0193  0.0736  317 ALA C O   
11891 C CB  . ALA C 325 ? 0.4343 0.2360 0.2938 0.0417  0.0126  0.0867  317 ALA C CB  
11892 N N   . GLU C 326 ? 0.3305 0.1612 0.1886 0.0345  0.0114  0.0810  318 GLU C N   
11893 C CA  . GLU C 326 ? 0.4243 0.2719 0.2893 0.0331  0.0099  0.0752  318 GLU C CA  
11894 C C   . GLU C 326 ? 0.3499 0.2014 0.2125 0.0249  0.0153  0.0720  318 GLU C C   
11895 O O   . GLU C 326 ? 0.3130 0.1753 0.1842 0.0224  0.0164  0.0659  318 GLU C O   
11896 C CB  . GLU C 326 ? 0.4659 0.3209 0.3268 0.0374  0.0038  0.0775  318 GLU C CB  
11897 C CG  . GLU C 326 ? 0.4709 0.3272 0.3374 0.0457  -0.0024 0.0795  318 GLU C CG  
11898 C CD  . GLU C 326 ? 0.5299 0.3724 0.3878 0.0504  -0.0043 0.0874  318 GLU C CD  
11899 O OE1 . GLU C 326 ? 0.5610 0.3914 0.4096 0.0465  -0.0001 0.0909  318 GLU C OE1 
11900 O OE2 . GLU C 326 ? 0.5989 0.4438 0.4603 0.0576  -0.0101 0.0900  318 GLU C OE2 
11901 N N   . ALA C 327 ? 0.3652 0.2082 0.2164 0.0206  0.0188  0.0764  319 ALA C N   
11902 C CA  . ALA C 327 ? 0.3614 0.2090 0.2110 0.0128  0.0243  0.0737  319 ALA C CA  
11903 C C   . ALA C 327 ? 0.3795 0.2263 0.2379 0.0083  0.0287  0.0692  319 ALA C C   
11904 O O   . ALA C 327 ? 0.3535 0.2110 0.2183 0.0042  0.0310  0.0639  319 ALA C O   
11905 C CB  . ALA C 327 ? 0.3361 0.1743 0.1714 0.0090  0.0275  0.0797  319 ALA C CB  
11906 N N   . ALA C 328 ? 0.3537 0.1878 0.2125 0.0092  0.0296  0.0712  320 ALA C N   
11907 C CA  . ALA C 328 ? 0.3479 0.1803 0.2142 0.0046  0.0335  0.0668  320 ALA C CA  
11908 C C   . ALA C 328 ? 0.3996 0.2440 0.2786 0.0072  0.0311  0.0602  320 ALA C C   
11909 O O   . ALA C 328 ? 0.3648 0.2158 0.2504 0.0024  0.0337  0.0552  320 ALA C O   
11910 C CB  . ALA C 328 ? 0.3749 0.1894 0.2377 0.0053  0.0349  0.0701  320 ALA C CB  
11911 N N   . GLU C 329 ? 0.3283 0.1762 0.2109 0.0147  0.0259  0.0604  321 GLU C N   
11912 C CA  . GLU C 329 ? 0.3238 0.1834 0.2178 0.0171  0.0236  0.0547  321 GLU C CA  
11913 C C   . GLU C 329 ? 0.3277 0.2018 0.2245 0.0140  0.0235  0.0508  321 GLU C C   
11914 O O   . GLU C 329 ? 0.2655 0.1476 0.1706 0.0119  0.0242  0.0454  321 GLU C O   
11915 C CB  . GLU C 329 ? 0.3163 0.1773 0.2134 0.0254  0.0181  0.0563  321 GLU C CB  
11916 C CG  . GLU C 329 ? 0.2791 0.1290 0.1789 0.0293  0.0186  0.0573  321 GLU C CG  
11917 C CD  . GLU C 329 ? 0.3413 0.1937 0.2502 0.0270  0.0212  0.0512  321 GLU C CD  
11918 O OE1 . GLU C 329 ? 0.3556 0.2184 0.2732 0.0300  0.0187  0.0475  321 GLU C OE1 
11919 O OE2 . GLU C 329 ? 0.3189 0.1632 0.2260 0.0218  0.0257  0.0500  321 GLU C OE2 
11920 N N   . PHE C 330 ? 0.2907 0.1677 0.1798 0.0138  0.0225  0.0534  322 PHE C N   
11921 C CA  . PHE C 330 ? 0.2860 0.1755 0.1767 0.0113  0.0227  0.0497  322 PHE C CA  
11922 C C   . PHE C 330 ? 0.2918 0.1841 0.1855 0.0045  0.0281  0.0466  322 PHE C C   
11923 O O   . PHE C 330 ? 0.3029 0.2055 0.2040 0.0031  0.0282  0.0415  322 PHE C O   
11924 C CB  . PHE C 330 ? 0.3267 0.2167 0.2067 0.0120  0.0215  0.0534  322 PHE C CB  
11925 C CG  . PHE C 330 ? 0.3152 0.2171 0.1957 0.0103  0.0217  0.0495  322 PHE C CG  
11926 C CD1 . PHE C 330 ? 0.3050 0.2159 0.1913 0.0137  0.0173  0.0458  322 PHE C CD1 
11927 C CD2 . PHE C 330 ? 0.3024 0.2062 0.1778 0.0053  0.0266  0.0494  322 PHE C CD2 
11928 C CE1 . PHE C 330 ? 0.3276 0.2480 0.2139 0.0124  0.0176  0.0420  322 PHE C CE1 
11929 C CE2 . PHE C 330 ? 0.2890 0.2033 0.1651 0.0045  0.0271  0.0455  322 PHE C CE2 
11930 C CZ  . PHE C 330 ? 0.2957 0.2175 0.1769 0.0082  0.0225  0.0418  322 PHE C CZ  
11931 N N   . VAL C 331 ? 0.3046 0.1878 0.1924 -0.0001 0.0324  0.0497  323 VAL C N   
11932 C CA  . VAL C 331 ? 0.2971 0.1833 0.1882 -0.0072 0.0374  0.0471  323 VAL C CA  
11933 C C   . VAL C 331 ? 0.2926 0.1809 0.1940 -0.0080 0.0373  0.0423  323 VAL C C   
11934 O O   . VAL C 331 ? 0.2889 0.1874 0.1973 -0.0110 0.0384  0.0378  323 VAL C O   
11935 C CB  . VAL C 331 ? 0.3279 0.2024 0.2105 -0.0122 0.0419  0.0518  323 VAL C CB  
11936 C CG1 . VAL C 331 ? 0.2870 0.1640 0.1746 -0.0200 0.0466  0.0488  323 VAL C CG1 
11937 C CG2 . VAL C 331 ? 0.3706 0.2453 0.2426 -0.0128 0.0430  0.0559  323 VAL C CG2 
11938 N N   . ARG C 332 ? 0.2756 0.1541 0.1779 -0.0051 0.0359  0.0433  324 ARG C N   
11939 C CA  . ARG C 332 ? 0.2824 0.1618 0.1933 -0.0059 0.0360  0.0387  324 ARG C CA  
11940 C C   . ARG C 332 ? 0.3101 0.2032 0.2293 -0.0033 0.0329  0.0339  324 ARG C C   
11941 O O   . ARG C 332 ? 0.2515 0.1514 0.1772 -0.0068 0.0340  0.0296  324 ARG C O   
11942 C CB  . ARG C 332 ? 0.2509 0.1179 0.1608 -0.0016 0.0348  0.0404  324 ARG C CB  
11943 C CG  . ARG C 332 ? 0.2432 0.1109 0.1612 -0.0017 0.0349  0.0355  324 ARG C CG  
11944 C CD  . ARG C 332 ? 0.2985 0.1553 0.2163 0.0039  0.0338  0.0368  324 ARG C CD  
11945 N NE  . ARG C 332 ? 0.2593 0.1211 0.1797 0.0118  0.0294  0.0380  324 ARG C NE  
11946 C CZ  . ARG C 332 ? 0.2805 0.1531 0.2090 0.0146  0.0268  0.0342  324 ARG C CZ  
11947 N NH1 . ARG C 332 ? 0.2556 0.1350 0.1897 0.0106  0.0281  0.0290  324 ARG C NH1 
11948 N NH2 . ARG C 332 ? 0.2351 0.1120 0.1659 0.0213  0.0228  0.0356  324 ARG C NH2 
11949 N N   . ARG C 333 ? 0.2387 0.1358 0.1576 0.0025  0.0289  0.0349  325 ARG C N   
11950 C CA  . ARG C 333 ? 0.2293 0.1377 0.1557 0.0050  0.0258  0.0307  325 ARG C CA  
11951 C C   . ARG C 333 ? 0.2531 0.1722 0.1807 0.0020  0.0266  0.0281  325 ARG C C   
11952 O O   . ARG C 333 ? 0.2542 0.1813 0.1888 0.0012  0.0260  0.0238  325 ARG C O   
11953 C CB  . ARG C 333 ? 0.2300 0.1393 0.1558 0.0116  0.0210  0.0326  325 ARG C CB  
11954 C CG  . ARG C 333 ? 0.2682 0.1694 0.1960 0.0156  0.0200  0.0340  325 ARG C CG  
11955 C CD  . ARG C 333 ? 0.2907 0.1925 0.2173 0.0220  0.0154  0.0371  325 ARG C CD  
11956 N NE  . ARG C 333 ? 0.2998 0.2136 0.2302 0.0235  0.0117  0.0346  325 ARG C NE  
11957 C CZ  . ARG C 333 ? 0.3265 0.2440 0.2575 0.0283  0.0070  0.0362  325 ARG C CZ  
11958 N NH1 . ARG C 333 ? 0.2160 0.1269 0.1447 0.0329  0.0052  0.0406  325 ARG C NH1 
11959 N NH2 . ARG C 333 ? 0.2427 0.1703 0.1766 0.0286  0.0039  0.0335  325 ARG C NH2 
11960 N N   . MET C 334 ? 0.2453 0.1646 0.1658 0.0006  0.0282  0.0307  326 MET C N   
11961 C CA  . MET C 334 ? 0.2295 0.1588 0.1513 -0.0021 0.0298  0.0280  326 MET C CA  
11962 C C   . MET C 334 ? 0.2746 0.2068 0.2018 -0.0077 0.0335  0.0254  326 MET C C   
11963 O O   . MET C 334 ? 0.2849 0.2271 0.2177 -0.0088 0.0337  0.0217  326 MET C O   
11964 C CB  . MET C 334 ? 0.2422 0.1706 0.1546 -0.0028 0.0316  0.0313  326 MET C CB  
11965 C CG  . MET C 334 ? 0.2565 0.1855 0.1633 0.0022  0.0274  0.0328  326 MET C CG  
11966 S SD  . MET C 334 ? 0.2573 0.1969 0.1709 0.0058  0.0230  0.0276  326 MET C SD  
11967 C CE  . MET C 334 ? 0.2349 0.1841 0.1508 0.0023  0.0269  0.0237  326 MET C CE  
11968 N N   . ASP C 335 ? 0.2645 0.1881 0.1902 -0.0114 0.0363  0.0273  327 ASP C N   
11969 C CA  . ASP C 335 ? 0.2547 0.1810 0.1856 -0.0173 0.0392  0.0247  327 ASP C CA  
11970 C C   . ASP C 335 ? 0.3024 0.2304 0.2410 -0.0165 0.0371  0.0208  327 ASP C C   
11971 O O   . ASP C 335 ? 0.3280 0.2578 0.2707 -0.0214 0.0388  0.0184  327 ASP C O   
11972 C CB  . ASP C 335 ? 0.2991 0.2145 0.2249 -0.0223 0.0430  0.0279  327 ASP C CB  
11973 C CG  . ASP C 335 ? 0.3824 0.2978 0.3012 -0.0253 0.0464  0.0314  327 ASP C CG  
11974 O OD1 . ASP C 335 ? 0.3735 0.2986 0.2923 -0.0238 0.0464  0.0307  327 ASP C OD1 
11975 O OD2 . ASP C 335 ? 0.3446 0.2497 0.2576 -0.0293 0.0494  0.0349  327 ASP C OD2 
11976 N N   . LYS C 336 ? 0.2632 0.1905 0.2032 -0.0109 0.0333  0.0201  328 LYS C N   
11977 C CA  . LYS C 336 ? 0.3017 0.2318 0.2485 -0.0098 0.0313  0.0163  328 LYS C CA  
11978 C C   . LYS C 336 ? 0.3739 0.2950 0.3210 -0.0128 0.0331  0.0158  328 LYS C C   
11979 O O   . LYS C 336 ? 0.3628 0.2868 0.3147 -0.0154 0.0332  0.0122  328 LYS C O   
11980 C CB  . LYS C 336 ? 0.2653 0.2075 0.2182 -0.0117 0.0308  0.0125  328 LYS C CB  
11981 C CG  . LYS C 336 ? 0.2436 0.1937 0.1956 -0.0086 0.0293  0.0126  328 LYS C CG  
11982 C CD  . LYS C 336 ? 0.2967 0.2578 0.2545 -0.0098 0.0290  0.0091  328 LYS C CD  
11983 C CE  . LYS C 336 ? 0.2730 0.2401 0.2292 -0.0062 0.0273  0.0086  328 LYS C CE  
11984 N NZ  . LYS C 336 ? 0.1993 0.1765 0.1610 -0.0067 0.0274  0.0054  328 LYS C NZ  
11985 N N   . LYS C 337 ? 0.2995 0.2086 0.2406 -0.0122 0.0345  0.0193  329 LYS C N   
11986 C CA  . LYS C 337 ? 0.3332 0.2309 0.2729 -0.0144 0.0365  0.0191  329 LYS C CA  
11987 C C   . LYS C 337 ? 0.2891 0.1793 0.2285 -0.0080 0.0347  0.0199  329 LYS C C   
11988 O O   . LYS C 337 ? 0.2890 0.1793 0.2265 -0.0025 0.0324  0.0229  329 LYS C O   
11989 C CB  . LYS C 337 ? 0.3357 0.2235 0.2683 -0.0189 0.0400  0.0228  329 LYS C CB  
11990 C CG  . LYS C 337 ? 0.4058 0.3006 0.3393 -0.0262 0.0427  0.0221  329 LYS C CG  
11991 C CD  . LYS C 337 ? 0.3793 0.2629 0.3054 -0.0311 0.0464  0.0259  329 LYS C CD  
11992 C CE  . LYS C 337 ? 0.3976 0.2899 0.3247 -0.0381 0.0495  0.0259  329 LYS C CE  
11993 N NZ  . LYS C 337 ? 0.4063 0.2879 0.3253 -0.0428 0.0532  0.0304  329 LYS C NZ  
11994 N N   . LEU C 338 ? 0.3608 0.2446 0.3018 -0.0087 0.0357  0.0173  330 LEU C N   
11995 C CA  . LEU C 338 ? 0.2605 0.1365 0.2016 -0.0027 0.0349  0.0178  330 LEU C CA  
11996 C C   . LEU C 338 ? 0.2988 0.1593 0.2326 -0.0017 0.0368  0.0221  330 LEU C C   
11997 O O   . LEU C 338 ? 0.3243 0.1786 0.2529 -0.0072 0.0394  0.0239  330 LEU C O   
11998 C CB  . LEU C 338 ? 0.2581 0.1328 0.2030 -0.0040 0.0359  0.0129  330 LEU C CB  
11999 C CG  . LEU C 338 ? 0.3386 0.2270 0.2904 -0.0035 0.0337  0.0090  330 LEU C CG  
12000 C CD1 . LEU C 338 ? 0.3479 0.2331 0.3016 -0.0050 0.0350  0.0046  330 LEU C CD1 
12001 C CD2 . LEU C 338 ? 0.3938 0.2889 0.3489 0.0034  0.0304  0.0105  330 LEU C CD2 
12002 N N   . PRO C 339 ? 0.3119 0.1659 0.2455 0.0054  0.0356  0.0239  331 PRO C N   
12003 C CA  . PRO C 339 ? 0.3378 0.1752 0.2645 0.0070  0.0374  0.0279  331 PRO C CA  
12004 C C   . PRO C 339 ? 0.4001 0.2257 0.3238 0.0013  0.0413  0.0252  331 PRO C C   
12005 O O   . PRO C 339 ? 0.3523 0.1817 0.2803 -0.0014 0.0422  0.0200  331 PRO C O   
12006 C CB  . PRO C 339 ? 0.3194 0.1551 0.2492 0.0164  0.0351  0.0290  331 PRO C CB  
12007 C CG  . PRO C 339 ? 0.3190 0.1716 0.2558 0.0192  0.0314  0.0274  331 PRO C CG  
12008 C CD  . PRO C 339 ? 0.2850 0.1469 0.2251 0.0123  0.0325  0.0228  331 PRO C CD  
12009 N N   . GLU C 340 ? 0.3792 0.1898 0.2949 -0.0008 0.0437  0.0290  332 GLU C N   
12010 C CA  . GLU C 340 ? 0.4292 0.2274 0.3408 -0.0076 0.0475  0.0266  332 GLU C CA  
12011 C C   . GLU C 340 ? 0.4129 0.2025 0.3262 -0.0039 0.0485  0.0227  332 GLU C C   
12012 O O   . GLU C 340 ? 0.4872 0.2728 0.4001 -0.0098 0.0508  0.0181  332 GLU C O   
12013 C CB  . GLU C 340 ? 0.4591 0.2415 0.3610 -0.0104 0.0497  0.0320  332 GLU C CB  
12014 N N   . ASN C 341 ? 0.3452 0.1325 0.2605 0.0056  0.0469  0.0243  333 ASN C N   
12015 C CA  . ASN C 341 ? 0.3790 0.1583 0.2960 0.0102  0.0485  0.0207  333 ASN C CA  
12016 C C   . ASN C 341 ? 0.3270 0.1212 0.2530 0.0125  0.0471  0.0156  333 ASN C C   
12017 O O   . ASN C 341 ? 0.3985 0.1890 0.3271 0.0182  0.0481  0.0131  333 ASN C O   
12018 C CB  . ASN C 341 ? 0.5460 0.3188 0.4627 0.0195  0.0469  0.0248  333 ASN C CB  
12019 C CG  . ASN C 341 ? 0.5929 0.3761 0.5150 0.0279  0.0435  0.0276  333 ASN C CG  
12020 O OD1 . ASN C 341 ? 0.5158 0.3143 0.4412 0.0256  0.0408  0.0279  333 ASN C OD1 
12021 N ND2 . ASN C 341 ? 0.6715 0.4536 0.5974 0.0369  0.0420  0.0287  333 ASN C ND2 
12022 N N   . PHE C 342 ? 0.2801 0.0908 0.2106 0.0084  0.0451  0.0140  334 PHE C N   
12023 C CA  . PHE C 342 ? 0.2885 0.1136 0.2272 0.0112  0.0434  0.0102  334 PHE C CA  
12024 C C   . PHE C 342 ? 0.3044 0.1245 0.2437 0.0100  0.0462  0.0044  334 PHE C C   
12025 O O   . PHE C 342 ? 0.2693 0.0921 0.2131 0.0161  0.0462  0.0025  334 PHE C O   
12026 C CB  . PHE C 342 ? 0.3102 0.1512 0.2523 0.0061  0.0411  0.0092  334 PHE C CB  
12027 C CG  . PHE C 342 ? 0.3194 0.1746 0.2691 0.0090  0.0389  0.0063  334 PHE C CG  
12028 C CD1 . PHE C 342 ? 0.2910 0.1538 0.2451 0.0160  0.0360  0.0087  334 PHE C CD1 
12029 C CD2 . PHE C 342 ? 0.3006 0.1616 0.2527 0.0045  0.0395  0.0012  334 PHE C CD2 
12030 C CE1 . PHE C 342 ? 0.3151 0.1907 0.2762 0.0180  0.0341  0.0061  334 PHE C CE1 
12031 C CE2 . PHE C 342 ? 0.2807 0.1539 0.2391 0.0069  0.0377  -0.0011 334 PHE C CE2 
12032 C CZ  . PHE C 342 ? 0.3142 0.1946 0.2771 0.0134  0.0351  0.0013  334 PHE C CZ  
12033 N N   . ASP C 343 ? 0.3380 0.1518 0.2727 0.0019  0.0485  0.0014  335 ASP C N   
12034 C CA  . ASP C 343 ? 0.3553 0.1648 0.2894 -0.0002 0.0509  -0.0046 335 ASP C CA  
12035 C C   . ASP C 343 ? 0.3773 0.1721 0.3088 0.0062  0.0537  -0.0051 335 ASP C C   
12036 O O   . ASP C 343 ? 0.3801 0.1777 0.3149 0.0098  0.0547  -0.0090 335 ASP C O   
12037 C CB  . ASP C 343 ? 0.4083 0.2129 0.3373 -0.0107 0.0524  -0.0073 335 ASP C CB  
12038 C CG  . ASP C 343 ? 0.4091 0.2303 0.3422 -0.0165 0.0498  -0.0081 335 ASP C CG  
12039 O OD1 . ASP C 343 ? 0.4110 0.2456 0.3501 -0.0137 0.0477  -0.0095 335 ASP C OD1 
12040 O OD2 . ASP C 343 ? 0.4743 0.2953 0.4049 -0.0239 0.0500  -0.0072 335 ASP C OD2 
12041 N N   . GLU C 344 ? 0.2978 0.0823 0.2251 0.0077  0.0538  -0.0011 336 GLU C N   
12042 C CA  . GLU C 344 ? 0.3689 0.1445 0.2956 0.0143  0.0548  -0.0010 336 GLU C CA  
12043 C C   . GLU C 344 ? 0.3572 0.1400 0.2911 0.0247  0.0536  0.0003  336 GLU C C   
12044 O O   . GLU C 344 ? 0.3487 0.1314 0.2857 0.0296  0.0550  -0.0028 336 GLU C O   
12045 C CB  . GLU C 344 ? 0.4435 0.2071 0.3641 0.0138  0.0547  0.0038  336 GLU C CB  
12046 C CG  . GLU C 344 ? 0.6313 0.3831 0.5498 0.0190  0.0559  0.0037  336 GLU C CG  
12047 C CD  . GLU C 344 ? 0.7222 0.4617 0.6339 0.0172  0.0558  0.0085  336 GLU C CD  
12048 O OE1 . GLU C 344 ? 0.7402 0.4820 0.6496 0.0134  0.0545  0.0126  336 GLU C OE1 
12049 O OE2 . GLU C 344 ? 0.7133 0.4405 0.6216 0.0193  0.0571  0.0081  336 GLU C OE2 
12050 N N   . TYR C 345 ? 0.3226 0.1128 0.2595 0.0281  0.0509  0.0049  337 TYR C N   
12051 C CA  . TYR C 345 ? 0.2997 0.0993 0.2444 0.0373  0.0490  0.0063  337 TYR C CA  
12052 C C   . TYR C 345 ? 0.3020 0.1120 0.2529 0.0376  0.0502  0.0007  337 TYR C C   
12053 O O   . TYR C 345 ? 0.2947 0.1083 0.2514 0.0445  0.0509  -0.0007 337 TYR C O   
12054 C CB  . TYR C 345 ? 0.3143 0.1244 0.2612 0.0385  0.0447  0.0116  337 TYR C CB  
12055 C CG  . TYR C 345 ? 0.3274 0.1515 0.2835 0.0465  0.0417  0.0127  337 TYR C CG  
12056 C CD1 . TYR C 345 ? 0.3772 0.1970 0.3352 0.0557  0.0405  0.0168  337 TYR C CD1 
12057 C CD2 . TYR C 345 ? 0.3212 0.1625 0.2842 0.0446  0.0399  0.0098  337 TYR C CD2 
12058 C CE1 . TYR C 345 ? 0.3732 0.2071 0.3405 0.0627  0.0375  0.0178  337 TYR C CE1 
12059 C CE2 . TYR C 345 ? 0.2988 0.1531 0.2705 0.0511  0.0371  0.0108  337 TYR C CE2 
12060 C CZ  . TYR C 345 ? 0.3251 0.1762 0.2992 0.0599  0.0359  0.0147  337 TYR C CZ  
12061 O OH  . TYR C 345 ? 0.3340 0.1993 0.3175 0.0659  0.0329  0.0155  337 TYR C OH  
12062 N N   . VAL C 346 ? 0.2713 0.0902 0.2223 0.0296  0.0496  -0.0023 338 VAL C N   
12063 C CA  . VAL C 346 ? 0.2807 0.1105 0.2369 0.0290  0.0503  -0.0073 338 VAL C CA  
12064 C C   . VAL C 346 ? 0.2907 0.1090 0.2438 0.0300  0.0551  -0.0123 338 VAL C C   
12065 O O   . VAL C 346 ? 0.3059 0.1301 0.2642 0.0347  0.0564  -0.0150 338 VAL C O   
12066 C CB  . VAL C 346 ? 0.2558 0.0960 0.2118 0.0204  0.0484  -0.0092 338 VAL C CB  
12067 C CG1 . VAL C 346 ? 0.2756 0.1237 0.2346 0.0188  0.0496  -0.0145 338 VAL C CG1 
12068 C CG2 . VAL C 346 ? 0.2343 0.0879 0.1948 0.0213  0.0439  -0.0051 338 VAL C CG2 
12069 N N   . GLN C 347 ? 0.3322 0.1386 0.2778 0.0246  0.0565  -0.0135 339 GLN C N   
12070 C CA  . GLN C 347 ? 0.3785 0.1787 0.3213 0.0239  0.0594  -0.0183 339 GLN C CA  
12071 C C   . GLN C 347 ? 0.3976 0.1951 0.3442 0.0336  0.0605  -0.0175 339 GLN C C   
12072 O O   . GLN C 347 ? 0.3875 0.1868 0.3361 0.0361  0.0629  -0.0216 339 GLN C O   
12073 C CB  . GLN C 347 ? 0.4180 0.2059 0.3523 0.0164  0.0603  -0.0192 339 GLN C CB  
12074 N N   . THR C 348 ? 0.3155 0.1091 0.2632 0.0391  0.0587  -0.0120 340 THR C N   
12075 C CA  . THR C 348 ? 0.3641 0.1562 0.3164 0.0487  0.0590  -0.0108 340 THR C CA  
12076 C C   . THR C 348 ? 0.3724 0.1798 0.3348 0.0552  0.0584  -0.0112 340 THR C C   
12077 O O   . THR C 348 ? 0.3567 0.1665 0.3236 0.0607  0.0604  -0.0138 340 THR C O   
12078 C CB  . THR C 348 ? 0.4371 0.2218 0.3874 0.0524  0.0565  -0.0043 340 THR C CB  
12079 O OG1 . THR C 348 ? 0.5156 0.2857 0.4566 0.0462  0.0577  -0.0043 340 THR C OG1 
12080 C CG2 . THR C 348 ? 0.4695 0.2537 0.4254 0.0629  0.0562  -0.0027 340 THR C CG2 
12081 N N   . ALA C 349 ? 0.3376 0.1557 0.3037 0.0543  0.0558  -0.0088 341 ALA C N   
12082 C CA  . ALA C 349 ? 0.2709 0.1044 0.2469 0.0596  0.0550  -0.0090 341 ALA C CA  
12083 C C   . ALA C 349 ? 0.3029 0.1423 0.2807 0.0570  0.0584  -0.0152 341 ALA C C   
12084 O O   . ALA C 349 ? 0.3417 0.1910 0.3275 0.0625  0.0594  -0.0166 341 ALA C O   
12085 C CB  . ALA C 349 ? 0.2764 0.1196 0.2548 0.0578  0.0513  -0.0054 341 ALA C CB  
12086 N N   . LEU C 350 ? 0.2922 0.1266 0.2628 0.0483  0.0600  -0.0190 342 LEU C N   
12087 C CA  . LEU C 350 ? 0.3058 0.1452 0.2764 0.0450  0.0628  -0.0248 342 LEU C CA  
12088 C C   . LEU C 350 ? 0.3679 0.2020 0.3381 0.0489  0.0663  -0.0280 342 LEU C C   
12089 O O   . LEU C 350 ? 0.3581 0.2004 0.3328 0.0512  0.0686  -0.0313 342 LEU C O   
12090 C CB  . LEU C 350 ? 0.3177 0.1530 0.2802 0.0347  0.0628  -0.0275 342 LEU C CB  
12091 C CG  . LEU C 350 ? 0.3535 0.1934 0.3140 0.0297  0.0650  -0.0332 342 LEU C CG  
12092 C CD1 . LEU C 350 ? 0.3413 0.1961 0.3097 0.0324  0.0650  -0.0337 342 LEU C CD1 
12093 C CD2 . LEU C 350 ? 0.3400 0.1768 0.2932 0.0197  0.0637  -0.0348 342 LEU C CD2 
12094 N N   . LYS C 351 ? 0.3490 0.1692 0.3136 0.0496  0.0669  -0.0274 343 LYS C N   
12095 C CA  . LYS C 351 ? 0.3829 0.1971 0.3473 0.0545  0.0700  -0.0302 343 LYS C CA  
12096 C C   . LYS C 351 ? 0.4060 0.2298 0.3810 0.0646  0.0699  -0.0284 343 LYS C C   
12097 O O   . LYS C 351 ? 0.4054 0.2328 0.3838 0.0684  0.0731  -0.0320 343 LYS C O   
12098 C CB  . LYS C 351 ? 0.3994 0.1966 0.3564 0.0540  0.0702  -0.0289 343 LYS C CB  
12099 C CG  . LYS C 351 ? 0.4791 0.2664 0.4257 0.0440  0.0710  -0.0318 343 LYS C CG  
12100 C CD  . LYS C 351 ? 0.5667 0.3374 0.5067 0.0439  0.0713  -0.0302 343 LYS C CD  
12101 C CE  . LYS C 351 ? 0.6728 0.4349 0.6032 0.0332  0.0715  -0.0323 343 LYS C CE  
12102 N NZ  . LYS C 351 ? 0.6919 0.4383 0.6160 0.0324  0.0714  -0.0299 343 LYS C NZ  
12103 N N   . GLU C 352 ? 0.4361 0.2647 0.4166 0.0691  0.0662  -0.0227 344 GLU C N   
12104 C CA  . GLU C 352 ? 0.4761 0.3162 0.4679 0.0784  0.0653  -0.0206 344 GLU C CA  
12105 C C   . GLU C 352 ? 0.4692 0.3260 0.4685 0.0781  0.0665  -0.0232 344 GLU C C   
12106 O O   . GLU C 352 ? 0.5079 0.3728 0.5147 0.0837  0.0686  -0.0251 344 GLU C O   
12107 C CB  . GLU C 352 ? 0.4389 0.2809 0.4339 0.0822  0.0603  -0.0137 344 GLU C CB  
12108 N N   . VAL C 353 ? 0.4035 0.2656 0.4010 0.0714  0.0654  -0.0234 345 VAL C N   
12109 C CA  . VAL C 353 ? 0.4093 0.2863 0.4130 0.0700  0.0667  -0.0259 345 VAL C CA  
12110 C C   . VAL C 353 ? 0.4560 0.3321 0.4573 0.0686  0.0716  -0.0319 345 VAL C C   
12111 O O   . VAL C 353 ? 0.4798 0.3675 0.4888 0.0722  0.0738  -0.0336 345 VAL C O   
12112 C CB  . VAL C 353 ? 0.3278 0.2078 0.3280 0.0624  0.0648  -0.0256 345 VAL C CB  
12113 C CG1 . VAL C 353 ? 0.3879 0.2795 0.3910 0.0588  0.0670  -0.0294 345 VAL C CG1 
12114 C CG2 . VAL C 353 ? 0.3163 0.2037 0.3215 0.0643  0.0593  -0.0196 345 VAL C CG2 
12115 N N   . CYS C 354 ? 0.3947 0.2574 0.3852 0.0630  0.0734  -0.0350 346 CYS C N   
12116 C CA  . CYS C 354 ? 0.4685 0.3295 0.4553 0.0611  0.0779  -0.0407 346 CYS C CA  
12117 C C   . CYS C 354 ? 0.5057 0.3667 0.4978 0.0699  0.0806  -0.0417 346 CYS C C   
12118 O O   . CYS C 354 ? 0.5251 0.3937 0.5205 0.0715  0.0842  -0.0453 346 CYS C O   
12119 C CB  . CYS C 354 ? 0.5496 0.3959 0.5237 0.0534  0.0787  -0.0435 346 CYS C CB  
12120 S SG  . CYS C 354 ? 0.6509 0.4939 0.6184 0.0503  0.0838  -0.0506 346 CYS C SG  
12121 N N   . ALA C 355 ? 0.5001 0.3529 0.4932 0.0756  0.0790  -0.0386 347 ALA C N   
12122 C CA  . ALA C 355 ? 0.5866 0.4398 0.5857 0.0846  0.0812  -0.0394 347 ALA C CA  
12123 C C   . ALA C 355 ? 0.6304 0.5026 0.6430 0.0906  0.0809  -0.0381 347 ALA C C   
12124 O O   . ALA C 355 ? 0.7174 0.5958 0.7350 0.0950  0.0845  -0.0413 347 ALA C O   
12125 C CB  . ALA C 355 ? 0.5413 0.3823 0.5389 0.0894  0.0787  -0.0355 347 ALA C CB  
12126 N N   . LYS C 356 ? 0.5836 0.4657 0.6023 0.0908  0.0767  -0.0335 348 LYS C N   
12127 C CA  . LYS C 356 ? 0.5988 0.5002 0.6309 0.0956  0.0757  -0.0318 348 LYS C CA  
12128 C C   . LYS C 356 ? 0.5762 0.4890 0.6105 0.0919  0.0798  -0.0362 348 LYS C C   
12129 O O   . LYS C 356 ? 0.5648 0.4761 0.5923 0.0838  0.0807  -0.0382 348 LYS C O   
12130 C CB  . LYS C 356 ? 0.6065 0.5149 0.6426 0.0947  0.0702  -0.0262 348 LYS C CB  
12131 N N   . ASN C 368 ? 0.3509 0.3246 0.3997 0.0650  0.0385  -0.0084 360 ASN C N   
12132 C CA  . ASN C 368 ? 0.2675 0.2418 0.3119 0.0605  0.0329  -0.0056 360 ASN C CA  
12133 C C   . ASN C 368 ? 0.2925 0.2510 0.3256 0.0579  0.0334  -0.0052 360 ASN C C   
12134 O O   . ASN C 368 ? 0.2894 0.2393 0.3200 0.0622  0.0327  -0.0023 360 ASN C O   
12135 C CB  . ASN C 368 ? 0.3401 0.3230 0.3911 0.0653  0.0275  -0.0010 360 ASN C CB  
12136 C CG  . ASN C 368 ? 0.2946 0.2822 0.3425 0.0601  0.0217  0.0011  360 ASN C CG  
12137 O OD1 . ASN C 368 ? 0.3421 0.3217 0.3812 0.0552  0.0213  0.0007  360 ASN C OD1 
12138 N ND2 . ASN C 368 ? 0.2959 0.2967 0.3513 0.0612  0.0174  0.0030  360 ASN C ND2 
12139 N N   . SER C 369 ? 0.2193 0.1744 0.2458 0.0505  0.0344  -0.0079 361 SER C N   
12140 C CA  . SER C 369 ? 0.2431 0.1858 0.2598 0.0467  0.0345  -0.0076 361 SER C CA  
12141 C C   . SER C 369 ? 0.2563 0.1997 0.2709 0.0465  0.0295  -0.0033 361 SER C C   
12142 O O   . SER C 369 ? 0.2533 0.1861 0.2618 0.0467  0.0295  -0.0013 361 SER C O   
12143 C CB  . SER C 369 ? 0.2968 0.2389 0.3084 0.0390  0.0358  -0.0112 361 SER C CB  
12144 O OG  . SER C 369 ? 0.3285 0.2708 0.3411 0.0387  0.0403  -0.0153 361 SER C OG  
12145 N N   . ILE C 370 ? 0.1842 0.1396 0.2032 0.0455  0.0253  -0.0019 362 ILE C N   
12146 C CA  . ILE C 370 ? 0.1874 0.1440 0.2038 0.0450  0.0205  0.0018  362 ILE C CA  
12147 C C   . ILE C 370 ? 0.1880 0.1402 0.2048 0.0515  0.0192  0.0059  362 ILE C C   
12148 O O   . ILE C 370 ? 0.2094 0.1549 0.2199 0.0512  0.0175  0.0088  362 ILE C O   
12149 C CB  . ILE C 370 ? 0.2443 0.2143 0.2655 0.0431  0.0164  0.0020  362 ILE C CB  
12150 C CG1 . ILE C 370 ? 0.2335 0.2063 0.2531 0.0366  0.0175  -0.0016 362 ILE C CG1 
12151 C CG2 . ILE C 370 ? 0.2138 0.1848 0.2317 0.0432  0.0115  0.0056  362 ILE C CG2 
12152 C CD1 . ILE C 370 ? 0.2109 0.1960 0.2361 0.0350  0.0146  -0.0020 362 ILE C CD1 
12153 N N   . GLU C 371 ? 0.2409 0.1972 0.2653 0.0578  0.0199  0.0062  363 GLU C N   
12154 C CA  . GLU C 371 ? 0.2074 0.1595 0.2328 0.0650  0.0184  0.0104  363 GLU C CA  
12155 C C   . GLU C 371 ? 0.2590 0.1938 0.2759 0.0656  0.0217  0.0111  363 GLU C C   
12156 O O   . GLU C 371 ? 0.2542 0.1820 0.2662 0.0679  0.0194  0.0154  363 GLU C O   
12157 C CB  . GLU C 371 ? 0.2143 0.1743 0.2504 0.0718  0.0195  0.0100  363 GLU C CB  
12158 C CG  . GLU C 371 ? 0.2576 0.2170 0.2969 0.0802  0.0166  0.0148  363 GLU C CG  
12159 C CD  . GLU C 371 ? 0.2749 0.2476 0.3189 0.0809  0.0099  0.0181  363 GLU C CD  
12160 O OE1 . GLU C 371 ? 0.2475 0.2345 0.2995 0.0790  0.0087  0.0162  363 GLU C OE1 
12161 O OE2 . GLU C 371 ? 0.2921 0.2607 0.3312 0.0829  0.0058  0.0226  363 GLU C OE2 
12162 N N   . ILE C 372 ? 0.2123 0.1395 0.2266 0.0631  0.0269  0.0070  364 ILE C N   
12163 C CA  . ILE C 372 ? 0.2216 0.1317 0.2272 0.0623  0.0302  0.0070  364 ILE C CA  
12164 C C   . ILE C 372 ? 0.2771 0.1826 0.2743 0.0559  0.0283  0.0088  364 ILE C C   
12165 O O   . ILE C 372 ? 0.2958 0.1902 0.2866 0.0567  0.0281  0.0121  364 ILE C O   
12166 C CB  . ILE C 372 ? 0.2210 0.1253 0.2251 0.0597  0.0358  0.0014  364 ILE C CB  
12167 C CG1 . ILE C 372 ? 0.3226 0.2310 0.3349 0.0668  0.0385  -0.0004 364 ILE C CG1 
12168 C CG2 . ILE C 372 ? 0.2374 0.1237 0.2319 0.0573  0.0390  0.0010  364 ILE C CG2 
12169 C CD1 . ILE C 372 ? 0.3240 0.2294 0.3351 0.0639  0.0441  -0.0063 364 ILE C CD1 
12170 N N   . LEU C 373 ? 0.2497 0.1636 0.2467 0.0495  0.0269  0.0067  365 LEU C N   
12171 C CA  . LEU C 373 ? 0.3007 0.2118 0.2908 0.0436  0.0255  0.0080  365 LEU C CA  
12172 C C   . LEU C 373 ? 0.2825 0.1957 0.2710 0.0462  0.0212  0.0131  365 LEU C C   
12173 O O   . LEU C 373 ? 0.2670 0.1719 0.2482 0.0443  0.0212  0.0158  365 LEU C O   
12174 C CB  . LEU C 373 ? 0.3200 0.2402 0.3111 0.0373  0.0248  0.0047  365 LEU C CB  
12175 C CG  . LEU C 373 ? 0.4397 0.3529 0.4247 0.0306  0.0276  0.0021  365 LEU C CG  
12176 C CD1 . LEU C 373 ? 0.5061 0.4135 0.4913 0.0304  0.0318  -0.0019 365 LEU C CD1 
12177 C CD2 . LEU C 373 ? 0.4408 0.3632 0.4261 0.0251  0.0256  0.0005  365 LEU C CD2 
12178 N N   . ALA C 374 ? 0.2197 0.1442 0.2147 0.0501  0.0174  0.0145  366 ALA C N   
12179 C CA  . ALA C 374 ? 0.2401 0.1677 0.2329 0.0520  0.0128  0.0190  366 ALA C CA  
12180 C C   . ALA C 374 ? 0.3341 0.2502 0.3220 0.0567  0.0128  0.0237  366 ALA C C   
12181 O O   . ALA C 374 ? 0.2900 0.2029 0.2712 0.0559  0.0106  0.0275  366 ALA C O   
12182 C CB  . ALA C 374 ? 0.2460 0.1877 0.2471 0.0553  0.0086  0.0194  366 ALA C CB  
12183 N N   . LYS C 375 ? 0.3088 0.2180 0.2992 0.0617  0.0155  0.0235  367 LYS C N   
12184 C CA  . LYS C 375 ? 0.2771 0.1739 0.2628 0.0667  0.0156  0.0281  367 LYS C CA  
12185 C C   . LYS C 375 ? 0.2849 0.1679 0.2596 0.0613  0.0181  0.0293  367 LYS C C   
12186 O O   . LYS C 375 ? 0.3096 0.1844 0.2776 0.0630  0.0167  0.0343  367 LYS C O   
12187 C CB  . LYS C 375 ? 0.3482 0.2396 0.3389 0.0730  0.0189  0.0266  367 LYS C CB  
12188 C CG  . LYS C 375 ? 0.4283 0.3097 0.4173 0.0810  0.0181  0.0316  367 LYS C CG  
12189 C CD  . LYS C 375 ? 0.4566 0.3344 0.4520 0.0874  0.0219  0.0290  367 LYS C CD  
12190 C CE  . LYS C 375 ? 0.6150 0.4758 0.6049 0.0922  0.0234  0.0321  367 LYS C CE  
12191 N NZ  . LYS C 375 ? 0.6659 0.5226 0.6599 0.0944  0.0278  0.0273  367 LYS C NZ  
12192 N N   . GLU C 376 ? 0.2526 0.1337 0.2252 0.0543  0.0216  0.0249  368 GLU C N   
12193 C CA  . GLU C 376 ? 0.2759 0.1454 0.2394 0.0481  0.0244  0.0253  368 GLU C CA  
12194 C C   . GLU C 376 ? 0.2696 0.1462 0.2296 0.0421  0.0224  0.0260  368 GLU C C   
12195 O O   . GLU C 376 ? 0.3060 0.1744 0.2583 0.0379  0.0238  0.0281  368 GLU C O   
12196 C CB  . GLU C 376 ? 0.3600 0.2240 0.3235 0.0438  0.0291  0.0199  368 GLU C CB  
12197 C CG  . GLU C 376 ? 0.3373 0.1927 0.2932 0.0356  0.0318  0.0190  368 GLU C CG  
12198 C CD  . GLU C 376 ? 0.3769 0.2150 0.3246 0.0362  0.0338  0.0227  368 GLU C CD  
12199 O OE1 . GLU C 376 ? 0.4080 0.2396 0.3555 0.0435  0.0330  0.0262  368 GLU C OE1 
12200 O OE2 . GLU C 376 ? 0.3893 0.2204 0.3309 0.0291  0.0361  0.0224  368 GLU C OE2 
12201 N N   . LEU C 377 ? 0.2372 0.1283 0.2025 0.0417  0.0194  0.0244  369 LEU C N   
12202 C CA  . LEU C 377 ? 0.2573 0.1555 0.2200 0.0361  0.0180  0.0240  369 LEU C CA  
12203 C C   . LEU C 377 ? 0.2855 0.1926 0.2489 0.0393  0.0131  0.0269  369 LEU C C   
12204 O O   . LEU C 377 ? 0.2276 0.1463 0.1970 0.0399  0.0105  0.0247  369 LEU C O   
12205 C CB  . LEU C 377 ? 0.2365 0.1427 0.2038 0.0315  0.0192  0.0186  369 LEU C CB  
12206 C CG  . LEU C 377 ? 0.3034 0.2023 0.2695 0.0271  0.0236  0.0152  369 LEU C CG  
12207 C CD1 . LEU C 377 ? 0.3141 0.2225 0.2845 0.0231  0.0236  0.0104  369 LEU C CD1 
12208 C CD2 . LEU C 377 ? 0.2534 0.1433 0.2118 0.0222  0.0258  0.0169  369 LEU C CD2 
12209 N N   . PRO C 378 ? 0.2704 0.1721 0.2269 0.0409  0.0116  0.0318  370 PRO C N   
12210 C CA  . PRO C 378 ? 0.2266 0.1367 0.1824 0.0433  0.0066  0.0343  370 PRO C CA  
12211 C C   . PRO C 378 ? 0.2639 0.1829 0.2186 0.0382  0.0057  0.0317  370 PRO C C   
12212 O O   . PRO C 378 ? 0.2974 0.2246 0.2526 0.0397  0.0015  0.0324  370 PRO C O   
12213 C CB  . PRO C 378 ? 0.2668 0.1666 0.2134 0.0453  0.0060  0.0403  370 PRO C CB  
12214 C CG  . PRO C 378 ? 0.3128 0.2003 0.2542 0.0411  0.0113  0.0402  370 PRO C CG  
12215 C CD  . PRO C 378 ? 0.2406 0.1278 0.1890 0.0402  0.0143  0.0353  370 PRO C CD  
12216 N N   . GLU C 379 ? 0.2433 0.1611 0.1968 0.0325  0.0094  0.0287  371 GLU C N   
12217 C CA  . GLU C 379 ? 0.2480 0.1744 0.2017 0.0283  0.0088  0.0258  371 GLU C CA  
12218 C C   . GLU C 379 ? 0.2463 0.1823 0.2083 0.0285  0.0072  0.0216  371 GLU C C   
12219 O O   . GLU C 379 ? 0.2121 0.1549 0.1746 0.0257  0.0064  0.0191  371 GLU C O   
12220 C CB  . GLU C 379 ? 0.2405 0.1632 0.1911 0.0224  0.0132  0.0243  371 GLU C CB  
12221 C CG  . GLU C 379 ? 0.1928 0.1117 0.1475 0.0203  0.0164  0.0212  371 GLU C CG  
12222 C CD  . GLU C 379 ? 0.2269 0.1328 0.1773 0.0201  0.0195  0.0236  371 GLU C CD  
12223 O OE1 . GLU C 379 ? 0.2456 0.1453 0.1937 0.0249  0.0183  0.0273  371 GLU C OE1 
12224 O OE2 . GLU C 379 ? 0.2456 0.1471 0.1947 0.0151  0.0230  0.0219  371 GLU C OE2 
12225 N N   . LEU C 380 ? 0.2643 0.2006 0.2325 0.0316  0.0071  0.0208  372 LEU C N   
12226 C CA  . LEU C 380 ? 0.2430 0.1878 0.2186 0.0311  0.0063  0.0169  372 LEU C CA  
12227 C C   . LEU C 380 ? 0.2300 0.1843 0.2075 0.0324  0.0016  0.0171  372 LEU C C   
12228 O O   . LEU C 380 ? 0.2299 0.1854 0.2072 0.0364  -0.0016 0.0202  372 LEU C O   
12229 C CB  . LEU C 380 ? 0.1977 0.1409 0.1793 0.0345  0.0077  0.0161  372 LEU C CB  
12230 C CG  . LEU C 380 ? 0.2351 0.1849 0.2232 0.0326  0.0087  0.0117  372 LEU C CG  
12231 C CD1 . LEU C 380 ? 0.2444 0.1912 0.2298 0.0270  0.0118  0.0087  372 LEU C CD1 
12232 C CD2 . LEU C 380 ? 0.2414 0.1907 0.2355 0.0368  0.0102  0.0111  372 LEU C CD2 
12233 N N   . VAL C 381 ? 0.1740 0.1345 0.1530 0.0290  0.0009  0.0139  373 VAL C N   
12234 C CA  . VAL C 381 ? 0.2191 0.1880 0.2000 0.0293  -0.0033 0.0133  373 VAL C CA  
12235 C C   . VAL C 381 ? 0.2024 0.1771 0.1903 0.0277  -0.0031 0.0097  373 VAL C C   
12236 O O   . VAL C 381 ? 0.2369 0.2111 0.2246 0.0242  -0.0009 0.0070  373 VAL C O   
12237 C CB  . VAL C 381 ? 0.2266 0.1962 0.2011 0.0267  -0.0044 0.0128  373 VAL C CB  
12238 C CG1 . VAL C 381 ? 0.2344 0.2114 0.2105 0.0265  -0.0088 0.0114  373 VAL C CG1 
12239 C CG2 . VAL C 381 ? 0.1931 0.1571 0.1597 0.0279  -0.0044 0.0165  373 VAL C CG2 
12240 N N   . GLY C 382 ? 0.1867 0.1674 0.1808 0.0302  -0.0055 0.0100  374 GLY C N   
12241 C CA  . GLY C 382 ? 0.1679 0.1545 0.1684 0.0284  -0.0051 0.0070  374 GLY C CA  
12242 C C   . GLY C 382 ? 0.1899 0.1830 0.1908 0.0260  -0.0088 0.0057  374 GLY C C   
12243 O O   . GLY C 382 ? 0.1794 0.1727 0.1755 0.0258  -0.0118 0.0066  374 GLY C O   
12244 N N   . GLY C 383 ? 0.1766 0.1745 0.1827 0.0239  -0.0085 0.0033  375 GLY C N   
12245 C CA  . GLY C 383 ? 0.1479 0.1513 0.1549 0.0214  -0.0119 0.0020  375 GLY C CA  
12246 C C   . GLY C 383 ? 0.1835 0.1902 0.1953 0.0185  -0.0103 -0.0004 375 GLY C C   
12247 O O   . GLY C 383 ? 0.1529 0.1571 0.1659 0.0181  -0.0064 -0.0015 375 GLY C O   
12248 N N   . SER C 384 ? 0.1325 0.1445 0.1462 0.0161  -0.0134 -0.0013 376 SER C N   
12249 C CA  . SER C 384 ? 0.1345 0.1492 0.1515 0.0126  -0.0122 -0.0034 376 SER C CA  
12250 C C   . SER C 384 ? 0.1733 0.1892 0.1879 0.0091  -0.0159 -0.0044 376 SER C C   
12251 O O   . SER C 384 ? 0.1822 0.1993 0.1946 0.0097  -0.0197 -0.0037 376 SER C O   
12252 C CB  . SER C 384 ? 0.1221 0.1439 0.1478 0.0137  -0.0109 -0.0031 376 SER C CB  
12253 O OG  . SER C 384 ? 0.1679 0.1974 0.1981 0.0138  -0.0149 -0.0021 376 SER C OG  
12254 N N   . ALA C 385 ? 0.1569 0.1717 0.1710 0.0055  -0.0148 -0.0062 377 ALA C N   
12255 C CA  . ALA C 385 ? 0.1437 0.1583 0.1554 0.0018  -0.0180 -0.0073 377 ALA C CA  
12256 C C   . ALA C 385 ? 0.1779 0.2004 0.1966 -0.0007 -0.0193 -0.0072 377 ALA C C   
12257 O O   . ALA C 385 ? 0.1551 0.1784 0.1756 -0.0041 -0.0177 -0.0081 377 ALA C O   
12258 C CB  . ALA C 385 ? 0.1564 0.1647 0.1632 -0.0006 -0.0165 -0.0088 377 ALA C CB  
12259 N N   . ASP C 386 ? 0.1157 0.1445 0.1385 0.0010  -0.0221 -0.0060 378 ASP C N   
12260 C CA  . ASP C 386 ? 0.1583 0.1966 0.1887 -0.0014 -0.0240 -0.0058 378 ASP C CA  
12261 C C   . ASP C 386 ? 0.1844 0.2282 0.2226 -0.0013 -0.0196 -0.0057 378 ASP C C   
12262 O O   . ASP C 386 ? 0.1902 0.2398 0.2333 -0.0052 -0.0194 -0.0063 378 ASP C O   
12263 C CB  . ASP C 386 ? 0.1630 0.1997 0.1902 -0.0071 -0.0270 -0.0073 378 ASP C CB  
12264 C CG  . ASP C 386 ? 0.2612 0.3081 0.2959 -0.0103 -0.0300 -0.0070 378 ASP C CG  
12265 O OD1 . ASP C 386 ? 0.2267 0.2807 0.2657 -0.0075 -0.0327 -0.0057 378 ASP C OD1 
12266 O OD2 . ASP C 386 ? 0.2281 0.2763 0.2643 -0.0156 -0.0297 -0.0080 378 ASP C OD2 
12267 N N   . LEU C 387 ? 0.1549 0.1968 0.1940 0.0030  -0.0159 -0.0052 379 LEU C N   
12268 C CA  . LEU C 387 ? 0.1347 0.1820 0.1811 0.0040  -0.0115 -0.0053 379 LEU C CA  
12269 C C   . LEU C 387 ? 0.1836 0.2410 0.2393 0.0078  -0.0128 -0.0037 379 LEU C C   
12270 O O   . LEU C 387 ? 0.2106 0.2681 0.2656 0.0114  -0.0160 -0.0020 379 LEU C O   
12271 C CB  . LEU C 387 ? 0.1675 0.2075 0.2105 0.0069  -0.0068 -0.0058 379 LEU C CB  
12272 C CG  . LEU C 387 ? 0.1811 0.2122 0.2161 0.0039  -0.0049 -0.0072 379 LEU C CG  
12273 C CD1 . LEU C 387 ? 0.1957 0.2229 0.2300 0.0057  0.0002  -0.0081 379 LEU C CD1 
12274 C CD2 . LEU C 387 ? 0.2041 0.2367 0.2386 -0.0018 -0.0055 -0.0082 379 LEU C CD2 
12275 N N   . THR C 388 ? 0.1669 0.2331 0.2313 0.0072  -0.0101 -0.0041 380 THR C N   
12276 C CA  . THR C 388 ? 0.1978 0.2742 0.2724 0.0119  -0.0104 -0.0026 380 THR C CA  
12277 C C   . THR C 388 ? 0.2198 0.2902 0.2930 0.0187  -0.0075 -0.0018 380 THR C C   
12278 O O   . THR C 388 ? 0.2100 0.2728 0.2790 0.0188  -0.0027 -0.0032 380 THR C O   
12279 C CB  . THR C 388 ? 0.2693 0.3565 0.3536 0.0099  -0.0070 -0.0035 380 THR C CB  
12280 O OG1 . THR C 388 ? 0.2787 0.3717 0.3646 0.0033  -0.0104 -0.0038 380 THR C OG1 
12281 C CG2 . THR C 388 ? 0.2996 0.3976 0.3953 0.0160  -0.0063 -0.0021 380 THR C CG2 
12282 N N   . PRO C 389 ? 0.2730 0.3456 0.3486 0.0240  -0.0106 0.0006  381 PRO C N   
12283 C CA  . PRO C 389 ? 0.3314 0.3964 0.4046 0.0303  -0.0079 0.0017  381 PRO C CA  
12284 C C   . PRO C 389 ? 0.1986 0.2660 0.2785 0.0334  -0.0018 0.0004  381 PRO C C   
12285 O O   . PRO C 389 ? 0.2563 0.3355 0.3463 0.0335  -0.0007 -0.0000 381 PRO C O   
12286 C CB  . PRO C 389 ? 0.4144 0.4835 0.4903 0.0351  -0.0131 0.0049  381 PRO C CB  
12287 C CG  . PRO C 389 ? 0.4235 0.4991 0.4992 0.0303  -0.0190 0.0051  381 PRO C CG  
12288 C CD  . PRO C 389 ? 0.3758 0.4574 0.4560 0.0245  -0.0169 0.0026  381 PRO C CD  
12289 N N   . SER C 390 ? 0.1560 0.2124 0.2301 0.0358  0.0024  -0.0003 382 SER C N   
12290 C CA  . SER C 390 ? 0.1888 0.2447 0.2671 0.0392  0.0086  -0.0019 382 SER C CA  
12291 C C   . SER C 390 ? 0.2097 0.2516 0.2802 0.0426  0.0110  -0.0018 382 SER C C   
12292 O O   . SER C 390 ? 0.2075 0.2411 0.2696 0.0413  0.0084  -0.0006 382 SER C O   
12293 C CB  . SER C 390 ? 0.2069 0.2642 0.2847 0.0338  0.0130  -0.0051 382 SER C CB  
12294 O OG  . SER C 390 ? 0.1680 0.2136 0.2348 0.0298  0.0142  -0.0066 382 SER C OG  
12295 N N   . ASN C 391 ? 0.2124 0.2516 0.2855 0.0467  0.0164  -0.0031 383 ASN C N   
12296 C CA  . ASN C 391 ? 0.2541 0.2790 0.3196 0.0495  0.0192  -0.0033 383 ASN C CA  
12297 C C   . ASN C 391 ? 0.2372 0.2521 0.2921 0.0433  0.0207  -0.0054 383 ASN C C   
12298 O O   . ASN C 391 ? 0.2508 0.2539 0.2985 0.0441  0.0218  -0.0052 383 ASN C O   
12299 C CB  . ASN C 391 ? 0.3398 0.3632 0.4100 0.0551  0.0250  -0.0049 383 ASN C CB  
12300 C CG  . ASN C 391 ? 0.4565 0.4869 0.5310 0.0523  0.0297  -0.0085 383 ASN C CG  
12301 O OD1 . ASN C 391 ? 0.4338 0.4673 0.5057 0.0455  0.0291  -0.0099 383 ASN C OD1 
12302 N ND2 . ASN C 391 ? 0.5962 0.6285 0.6767 0.0577  0.0347  -0.0100 383 ASN C ND2 
12303 N N   . LEU C 392 ? 0.1946 0.2137 0.2484 0.0371  0.0204  -0.0073 384 LEU C N   
12304 C CA  . LEU C 392 ? 0.1277 0.1385 0.1719 0.0315  0.0210  -0.0089 384 LEU C CA  
12305 C C   . LEU C 392 ? 0.1974 0.2053 0.2363 0.0294  0.0160  -0.0068 384 LEU C C   
12306 O O   . LEU C 392 ? 0.2263 0.2265 0.2575 0.0261  0.0164  -0.0077 384 LEU C O   
12307 C CB  . LEU C 392 ? 0.1906 0.2062 0.2350 0.0260  0.0225  -0.0113 384 LEU C CB  
12308 C CG  . LEU C 392 ? 0.2084 0.2260 0.2560 0.0269  0.0284  -0.0139 384 LEU C CG  
12309 C CD1 . LEU C 392 ? 0.1805 0.2036 0.2279 0.0210  0.0294  -0.0156 384 LEU C CD1 
12310 C CD2 . LEU C 392 ? 0.2154 0.2210 0.2560 0.0277  0.0325  -0.0160 384 LEU C CD2 
12311 N N   . THR C 393 ? 0.1884 0.2027 0.2310 0.0311  0.0114  -0.0043 385 THR C N   
12312 C CA  . THR C 393 ? 0.1581 0.1705 0.1951 0.0286  0.0069  -0.0029 385 THR C CA  
12313 C C   . THR C 393 ? 0.1822 0.1950 0.2196 0.0328  0.0031  0.0004  385 THR C C   
12314 O O   . THR C 393 ? 0.1977 0.2099 0.2306 0.0310  -0.0007 0.0016  385 THR C O   
12315 C CB  . THR C 393 ? 0.2016 0.2212 0.2402 0.0239  0.0041  -0.0037 385 THR C CB  
12316 O OG1 . THR C 393 ? 0.1941 0.2245 0.2415 0.0257  0.0022  -0.0027 385 THR C OG1 
12317 C CG2 . THR C 393 ? 0.2220 0.2406 0.2590 0.0193  0.0074  -0.0065 385 THR C CG2 
12318 N N   . ASP C 394 ? 0.1684 0.1820 0.2105 0.0385  0.0040  0.0021  386 ASP C N   
12319 C CA  . ASP C 394 ? 0.1884 0.2040 0.2317 0.0429  -0.0002 0.0057  386 ASP C CA  
12320 C C   . ASP C 394 ? 0.2263 0.2370 0.2718 0.0495  0.0024  0.0072  386 ASP C C   
12321 O O   . ASP C 394 ? 0.2023 0.2102 0.2499 0.0506  0.0074  0.0050  386 ASP C O   
12322 C CB  . ASP C 394 ? 0.2239 0.2529 0.2751 0.0428  -0.0045 0.0064  386 ASP C CB  
12323 C CG  . ASP C 394 ? 0.2283 0.2595 0.2782 0.0454  -0.0104 0.0100  386 ASP C CG  
12324 O OD1 . ASP C 394 ? 0.1810 0.2032 0.2233 0.0472  -0.0111 0.0121  386 ASP C OD1 
12325 O OD2 . ASP C 394 ? 0.2383 0.2807 0.2946 0.0451  -0.0145 0.0106  386 ASP C OD2 
12326 N N   . TRP C 395 ? 0.1937 0.2025 0.2378 0.0539  -0.0010 0.0111  387 TRP C N   
12327 C CA  . TRP C 395 ? 0.2022 0.2058 0.2483 0.0609  0.0009  0.0132  387 TRP C CA  
12328 C C   . TRP C 395 ? 0.2115 0.2216 0.2616 0.0662  -0.0047 0.0175  387 TRP C C   
12329 O O   . TRP C 395 ? 0.2186 0.2358 0.2683 0.0638  -0.0099 0.0187  387 TRP C O   
12330 C CB  . TRP C 395 ? 0.2300 0.2177 0.2662 0.0607  0.0040  0.0137  387 TRP C CB  
12331 C CG  . TRP C 395 ? 0.2336 0.2153 0.2609 0.0597  0.0005  0.0171  387 TRP C CG  
12332 C CD1 . TRP C 395 ? 0.2531 0.2280 0.2768 0.0646  -0.0012 0.0214  387 TRP C CD1 
12333 C CD2 . TRP C 395 ? 0.1857 0.1674 0.2063 0.0536  -0.0015 0.0164  387 TRP C CD2 
12334 N NE1 . TRP C 395 ? 0.2199 0.1908 0.2346 0.0614  -0.0039 0.0235  387 TRP C NE1 
12335 C CE2 . TRP C 395 ? 0.1985 0.1737 0.2115 0.0549  -0.0040 0.0203  387 TRP C CE2 
12336 C CE3 . TRP C 395 ? 0.1410 0.1271 0.1610 0.0475  -0.0014 0.0130  387 TRP C CE3 
12337 C CZ2 . TRP C 395 ? 0.2401 0.2139 0.2454 0.0504  -0.0058 0.0205  387 TRP C CZ2 
12338 C CZ3 . TRP C 395 ? 0.2581 0.2423 0.2708 0.0434  -0.0034 0.0133  387 TRP C CZ3 
12339 C CH2 . TRP C 395 ? 0.2449 0.2235 0.2506 0.0449  -0.0054 0.0168  387 TRP C CH2 
12340 N N   . SER C 396 ? 0.1909 0.1978 0.2445 0.0736  -0.0036 0.0198  388 SER C N   
12341 C CA  . SER C 396 ? 0.2240 0.2393 0.2839 0.0798  -0.0088 0.0240  388 SER C CA  
12342 C C   . SER C 396 ? 0.2277 0.2394 0.2789 0.0793  -0.0146 0.0281  388 SER C C   
12343 O O   . SER C 396 ? 0.2177 0.2393 0.2732 0.0816  -0.0206 0.0309  388 SER C O   
12344 C CB  . SER C 396 ? 0.2447 0.2553 0.3093 0.0886  -0.0061 0.0257  388 SER C CB  
12345 O OG  . SER C 396 ? 0.2329 0.2263 0.2868 0.0902  -0.0045 0.0280  388 SER C OG  
12346 N N   . ASN C 397 ? 0.2557 0.2539 0.2949 0.0761  -0.0130 0.0285  389 ASN C N   
12347 C CA  . ASN C 397 ? 0.2629 0.2562 0.2926 0.0760  -0.0174 0.0326  389 ASN C CA  
12348 C C   . ASN C 397 ? 0.2480 0.2423 0.2705 0.0683  -0.0190 0.0306  389 ASN C C   
12349 O O   . ASN C 397 ? 0.3150 0.3020 0.3272 0.0667  -0.0204 0.0329  389 ASN C O   
12350 C CB  . ASN C 397 ? 0.3161 0.2928 0.3371 0.0787  -0.0144 0.0353  389 ASN C CB  
12351 C CG  . ASN C 397 ? 0.3384 0.3126 0.3649 0.0875  -0.0141 0.0384  389 ASN C CG  
12352 O OD1 . ASN C 397 ? 0.3914 0.3528 0.4147 0.0899  -0.0095 0.0385  389 ASN C OD1 
12353 N ND2 . ASN C 397 ? 0.2276 0.2141 0.2627 0.0924  -0.0192 0.0407  389 ASN C ND2 
12354 N N   . SER C 398 ? 0.1679 0.1709 0.1954 0.0635  -0.0185 0.0265  390 SER C N   
12355 C CA  . SER C 398 ? 0.1801 0.1843 0.2013 0.0570  -0.0204 0.0246  390 SER C CA  
12356 C C   . SER C 398 ? 0.1981 0.2096 0.2180 0.0573  -0.0273 0.0270  390 SER C C   
12357 O O   . SER C 398 ? 0.2149 0.2374 0.2434 0.0598  -0.0311 0.0278  390 SER C O   
12358 C CB  . SER C 398 ? 0.1889 0.1994 0.2155 0.0521  -0.0182 0.0198  390 SER C CB  
12359 O OG  . SER C 398 ? 0.2278 0.2504 0.2657 0.0540  -0.0198 0.0194  390 SER C OG  
12360 N N   . VAL C 399 ? 0.2091 0.2151 0.2181 0.0544  -0.0290 0.0279  391 VAL C N   
12361 C CA  . VAL C 399 ? 0.2173 0.2284 0.2222 0.0539  -0.0355 0.0297  391 VAL C CA  
12362 C C   . VAL C 399 ? 0.1951 0.2076 0.1953 0.0473  -0.0360 0.0258  391 VAL C C   
12363 O O   . VAL C 399 ? 0.2106 0.2150 0.2032 0.0443  -0.0324 0.0244  391 VAL C O   
12364 C CB  . VAL C 399 ? 0.2458 0.2483 0.2403 0.0568  -0.0371 0.0344  391 VAL C CB  
12365 C CG1 . VAL C 399 ? 0.2858 0.2931 0.2740 0.0555  -0.0438 0.0359  391 VAL C CG1 
12366 C CG2 . VAL C 399 ? 0.2024 0.2025 0.2012 0.0639  -0.0370 0.0386  391 VAL C CG2 
12367 N N   . SER C 400 ? 0.1978 0.2204 0.2026 0.0451  -0.0404 0.0242  392 SER C N   
12368 C CA  . SER C 400 ? 0.2115 0.2349 0.2127 0.0390  -0.0408 0.0202  392 SER C CA  
12369 C C   . SER C 400 ? 0.1946 0.2120 0.1829 0.0372  -0.0428 0.0207  392 SER C C   
12370 O O   . SER C 400 ? 0.2115 0.2306 0.1955 0.0390  -0.0477 0.0235  392 SER C O   
12371 C CB  . SER C 400 ? 0.2605 0.2957 0.2698 0.0367  -0.0451 0.0186  392 SER C CB  
12372 O OG  . SER C 400 ? 0.2446 0.2856 0.2656 0.0375  -0.0422 0.0175  392 SER C OG  
12373 N N   . VAL C 401 ? 0.1502 0.1611 0.1323 0.0338  -0.0390 0.0179  393 VAL C N   
12374 C CA  . VAL C 401 ? 0.1789 0.1849 0.1491 0.0317  -0.0402 0.0173  393 VAL C CA  
12375 C C   . VAL C 401 ? 0.2122 0.2239 0.1813 0.0285  -0.0455 0.0149  393 VAL C C   
12376 O O   . VAL C 401 ? 0.2148 0.2310 0.1904 0.0257  -0.0458 0.0119  393 VAL C O   
12377 C CB  . VAL C 401 ? 0.2389 0.2378 0.2046 0.0292  -0.0346 0.0148  393 VAL C CB  
12378 C CG1 . VAL C 401 ? 0.2323 0.2272 0.1865 0.0271  -0.0353 0.0135  393 VAL C CG1 
12379 C CG2 . VAL C 401 ? 0.1966 0.1893 0.1622 0.0316  -0.0298 0.0172  393 VAL C CG2 
12380 N N   . THR C 402 ? 0.2320 0.2429 0.1921 0.0288  -0.0497 0.0164  394 THR C N   
12381 C CA  . THR C 402 ? 0.2522 0.2676 0.2096 0.0255  -0.0552 0.0140  394 THR C CA  
12382 C C   . THR C 402 ? 0.2807 0.2890 0.2238 0.0238  -0.0553 0.0126  394 THR C C   
12383 O O   . THR C 402 ? 0.2403 0.2416 0.1762 0.0253  -0.0513 0.0140  394 THR C O   
12384 C CB  . THR C 402 ? 0.2804 0.3044 0.2419 0.0273  -0.0620 0.0170  394 THR C CB  
12385 O OG1 . THR C 402 ? 0.3014 0.3218 0.2546 0.0308  -0.0637 0.0213  394 THR C OG1 
12386 C CG2 . THR C 402 ? 0.2375 0.2693 0.2139 0.0298  -0.0614 0.0185  394 THR C CG2 
12387 N N   . ARG C 403 ? 0.2737 0.2840 0.2125 0.0204  -0.0598 0.0098  395 ARG C N   
12388 C CA  A ARG C 403 ? 0.3242 0.3282 0.2486 0.0190  -0.0604 0.0081  395 ARG C CA  
12389 C CA  B ARG C 403 ? 0.3251 0.3291 0.2495 0.0190  -0.0604 0.0081  395 ARG C CA  
12390 C C   . ARG C 403 ? 0.3252 0.3268 0.2408 0.0221  -0.0618 0.0126  395 ARG C C   
12391 O O   . ARG C 403 ? 0.3294 0.3239 0.2337 0.0223  -0.0586 0.0125  395 ARG C O   
12392 C CB  A ARG C 403 ? 0.3595 0.3662 0.2808 0.0148  -0.0660 0.0045  395 ARG C CB  
12393 C CB  B ARG C 403 ? 0.3596 0.3665 0.2810 0.0149  -0.0662 0.0046  395 ARG C CB  
12394 C CG  A ARG C 403 ? 0.4095 0.4097 0.3151 0.0134  -0.0671 0.0024  395 ARG C CG  
12395 C CG  B ARG C 403 ? 0.4044 0.4044 0.3104 0.0132  -0.0668 0.0020  395 ARG C CG  
12396 C CD  A ARG C 403 ? 0.4288 0.4315 0.3314 0.0090  -0.0734 -0.0011 395 ARG C CD  
12397 C CD  B ARG C 403 ? 0.4283 0.4305 0.3311 0.0088  -0.0730 -0.0015 395 ARG C CD  
12398 N NE  A ARG C 403 ? 0.4331 0.4352 0.3421 0.0055  -0.0720 -0.0054 395 ARG C NE  
12399 N NE  B ARG C 403 ? 0.4594 0.4529 0.3487 0.0067  -0.0715 -0.0060 395 ARG C NE  
12400 C CZ  A ARG C 403 ? 0.4439 0.4379 0.3460 0.0036  -0.0689 -0.0100 395 ARG C CZ  
12401 C CZ  B ARG C 403 ? 0.4529 0.4410 0.3423 0.0049  -0.0677 -0.0105 395 ARG C CZ  
12402 N NH1 A ARG C 403 ? 0.4613 0.4480 0.3505 0.0049  -0.0665 -0.0112 395 ARG C NH1 
12403 N NH1 B ARG C 403 ? 0.4443 0.4349 0.3460 0.0044  -0.0653 -0.0109 395 ARG C NH1 
12404 N NH2 A ARG C 403 ? 0.4648 0.4580 0.3728 0.0006  -0.0680 -0.0133 395 ARG C NH2 
12405 N NH2 B ARG C 403 ? 0.3591 0.3392 0.2361 0.0038  -0.0663 -0.0146 395 ARG C NH2 
12406 N N   . ASP C 404 ? 0.2656 0.2733 0.1862 0.0248  -0.0663 0.0169  396 ASP C N   
12407 C CA  . ASP C 404 ? 0.3731 0.3785 0.2843 0.0277  -0.0690 0.0216  396 ASP C CA  
12408 C C   . ASP C 404 ? 0.3806 0.3822 0.2942 0.0323  -0.0650 0.0266  396 ASP C C   
12409 O O   . ASP C 404 ? 0.3836 0.3807 0.2874 0.0344  -0.0659 0.0307  396 ASP C O   
12410 C CB  . ASP C 404 ? 0.4289 0.4430 0.3422 0.0281  -0.0777 0.0236  396 ASP C CB  
12411 C CG  . ASP C 404 ? 0.4932 0.5097 0.4015 0.0230  -0.0824 0.0189  396 ASP C CG  
12412 O OD1 . ASP C 404 ? 0.5174 0.5264 0.4139 0.0204  -0.0800 0.0155  396 ASP C OD1 
12413 O OD2 . ASP C 404 ? 0.5596 0.5856 0.4761 0.0214  -0.0882 0.0184  396 ASP C OD2 
12414 N N   . LYS C 405 ? 0.3237 0.3263 0.2490 0.0336  -0.0607 0.0264  397 LYS C N   
12415 C CA  . LYS C 405 ? 0.3373 0.3361 0.2655 0.0379  -0.0576 0.0310  397 LYS C CA  
12416 C C   . LYS C 405 ? 0.3116 0.3057 0.2447 0.0371  -0.0499 0.0289  397 LYS C C   
12417 O O   . LYS C 405 ? 0.2696 0.2664 0.2088 0.0342  -0.0481 0.0244  397 LYS C O   
12418 C CB  . LYS C 405 ? 0.3590 0.3657 0.2987 0.0420  -0.0619 0.0343  397 LYS C CB  
12419 C CG  . LYS C 405 ? 0.4789 0.4905 0.4141 0.0438  -0.0700 0.0377  397 LYS C CG  
12420 C CD  . LYS C 405 ? 0.5390 0.5482 0.4743 0.0500  -0.0712 0.0443  397 LYS C CD  
12421 C CE  . LYS C 405 ? 0.5865 0.6000 0.5155 0.0518  -0.0796 0.0482  397 LYS C CE  
12422 N NZ  . LYS C 405 ? 0.6087 0.6166 0.5210 0.0478  -0.0807 0.0469  397 LYS C NZ  
12423 N N   . GLY C 406 ? 0.2565 0.2431 0.1864 0.0394  -0.0458 0.0322  398 GLY C N   
12424 C CA  . GLY C 406 ? 0.2704 0.2528 0.2053 0.0386  -0.0390 0.0307  398 GLY C CA  
12425 C C   . GLY C 406 ? 0.2654 0.2523 0.2139 0.0410  -0.0387 0.0306  398 GLY C C   
12426 O O   . GLY C 406 ? 0.2727 0.2675 0.2282 0.0428  -0.0434 0.0311  398 GLY C O   
12427 N N   . GLY C 407 ? 0.2559 0.2379 0.2079 0.0409  -0.0329 0.0299  399 GLY C N   
12428 C CA  . GLY C 407 ? 0.2349 0.2201 0.1987 0.0430  -0.0316 0.0294  399 GLY C CA  
12429 C C   . GLY C 407 ? 0.2818 0.2618 0.2478 0.0408  -0.0251 0.0268  399 GLY C C   
12430 O O   . GLY C 407 ? 0.2300 0.2039 0.1889 0.0382  -0.0217 0.0262  399 GLY C O   
12431 N N   . ASN C 408 ? 0.2125 0.1958 0.1886 0.0418  -0.0235 0.0252  400 ASN C N   
12432 C CA  . ASN C 408 ? 0.1764 0.1552 0.1549 0.0398  -0.0177 0.0227  400 ASN C CA  
12433 C C   . ASN C 408 ? 0.2030 0.1887 0.1902 0.0378  -0.0171 0.0186  400 ASN C C   
12434 O O   . ASN C 408 ? 0.2009 0.1841 0.1918 0.0371  -0.0129 0.0168  400 ASN C O   
12435 C CB  . ASN C 408 ? 0.2417 0.2129 0.2209 0.0434  -0.0146 0.0253  400 ASN C CB  
12436 C CG  . ASN C 408 ? 0.2660 0.2420 0.2537 0.0487  -0.0169 0.0271  400 ASN C CG  
12437 O OD1 . ASN C 408 ? 0.2335 0.2196 0.2282 0.0490  -0.0200 0.0258  400 ASN C OD1 
12438 N ND2 . ASN C 408 ? 0.2641 0.2326 0.2512 0.0530  -0.0151 0.0302  400 ASN C ND2 
12439 N N   . TYR C 409 ? 0.1630 0.1570 0.1531 0.0365  -0.0212 0.0172  401 TYR C N   
12440 C CA  . TYR C 409 ? 0.1590 0.1592 0.1565 0.0340  -0.0207 0.0137  401 TYR C CA  
12441 C C   . TYR C 409 ? 0.1915 0.1958 0.1864 0.0302  -0.0241 0.0115  401 TYR C C   
12442 O O   . TYR C 409 ? 0.1785 0.1865 0.1714 0.0308  -0.0289 0.0128  401 TYR C O   
12443 C CB  . TYR C 409 ? 0.1325 0.1402 0.1402 0.0371  -0.0219 0.0146  401 TYR C CB  
12444 C CG  . TYR C 409 ? 0.1248 0.1365 0.1399 0.0348  -0.0189 0.0113  401 TYR C CG  
12445 C CD1 . TYR C 409 ? 0.2780 0.2966 0.2960 0.0308  -0.0211 0.0088  401 TYR C CD1 
12446 C CD2 . TYR C 409 ? 0.1644 0.1723 0.1825 0.0362  -0.0140 0.0105  401 TYR C CD2 
12447 C CE1 . TYR C 409 ? 0.2494 0.2710 0.2731 0.0284  -0.0182 0.0062  401 TYR C CE1 
12448 C CE2 . TYR C 409 ? 0.1670 0.1781 0.1905 0.0338  -0.0111 0.0076  401 TYR C CE2 
12449 C CZ  . TYR C 409 ? 0.1825 0.2006 0.2088 0.0299  -0.0132 0.0056  401 TYR C CZ  
12450 O OH  . TYR C 409 ? 0.2150 0.2358 0.2458 0.0275  -0.0101 0.0030  401 TYR C OH  
12451 N N   . ILE C 410 ? 0.1861 0.1894 0.1806 0.0264  -0.0219 0.0082  402 ILE C N   
12452 C CA  . ILE C 410 ? 0.1573 0.1618 0.1480 0.0229  -0.0245 0.0058  402 ILE C CA  
12453 C C   . ILE C 410 ? 0.1856 0.1962 0.1834 0.0202  -0.0254 0.0035  402 ILE C C   
12454 O O   . ILE C 410 ? 0.1648 0.1752 0.1670 0.0192  -0.0219 0.0022  402 ILE C O   
12455 C CB  . ILE C 410 ? 0.1721 0.1701 0.1561 0.0209  -0.0214 0.0040  402 ILE C CB  
12456 C CG1 . ILE C 410 ? 0.2366 0.2294 0.2132 0.0229  -0.0204 0.0065  402 ILE C CG1 
12457 C CG2 . ILE C 410 ? 0.1712 0.1699 0.1521 0.0177  -0.0236 0.0011  402 ILE C CG2 
12458 C CD1 . ILE C 410 ? 0.2746 0.2620 0.2471 0.0214  -0.0160 0.0054  402 ILE C CD1 
12459 N N   . HIS C 411 ? 0.1389 0.1545 0.1372 0.0186  -0.0301 0.0030  403 HIS C N   
12460 C CA  . HIS C 411 ? 0.1278 0.1487 0.1318 0.0150  -0.0312 0.0009  403 HIS C CA  
12461 C C   . HIS C 411 ? 0.1200 0.1356 0.1176 0.0113  -0.0312 -0.0020 403 HIS C C   
12462 O O   . HIS C 411 ? 0.1382 0.1524 0.1299 0.0099  -0.0346 -0.0029 403 HIS C O   
12463 C CB  . HIS C 411 ? 0.1336 0.1632 0.1422 0.0147  -0.0364 0.0018  403 HIS C CB  
12464 C CG  . HIS C 411 ? 0.2365 0.2720 0.2523 0.0193  -0.0366 0.0049  403 HIS C CG  
12465 N ND1 . HIS C 411 ? 0.2619 0.3021 0.2871 0.0206  -0.0335 0.0051  403 HIS C ND1 
12466 C CD2 . HIS C 411 ? 0.3173 0.3543 0.3318 0.0232  -0.0397 0.0080  403 HIS C CD2 
12467 C CE1 . HIS C 411 ? 0.2941 0.3386 0.3242 0.0255  -0.0344 0.0079  403 HIS C CE1 
12468 N NE2 . HIS C 411 ? 0.2767 0.3191 0.3004 0.0272  -0.0384 0.0100  403 HIS C NE2 
12469 N N   . TYR C 412 ? 0.1116 0.1239 0.1100 0.0098  -0.0273 -0.0036 404 TYR C N   
12470 C CA  . TYR C 412 ? 0.1356 0.1422 0.1280 0.0073  -0.0271 -0.0060 404 TYR C CA  
12471 C C   . TYR C 412 ? 0.1739 0.1821 0.1673 0.0031  -0.0299 -0.0078 404 TYR C C   
12472 O O   . TYR C 412 ? 0.1428 0.1457 0.1303 0.0013  -0.0308 -0.0098 404 TYR C O   
12473 C CB  . TYR C 412 ? 0.1534 0.1561 0.1461 0.0072  -0.0225 -0.0066 404 TYR C CB  
12474 C CG  . TYR C 412 ? 0.1595 0.1588 0.1494 0.0102  -0.0197 -0.0053 404 TYR C CG  
12475 C CD1 . TYR C 412 ? 0.1675 0.1622 0.1505 0.0108  -0.0193 -0.0059 404 TYR C CD1 
12476 C CD2 . TYR C 412 ? 0.1351 0.1355 0.1292 0.0123  -0.0171 -0.0036 404 TYR C CD2 
12477 C CE1 . TYR C 412 ? 0.1683 0.1602 0.1487 0.0128  -0.0164 -0.0045 404 TYR C CE1 
12478 C CE2 . TYR C 412 ? 0.1621 0.1584 0.1532 0.0143  -0.0144 -0.0024 404 TYR C CE2 
12479 C CZ  . TYR C 412 ? 0.1918 0.1842 0.1762 0.0142  -0.0141 -0.0027 404 TYR C CZ  
12480 O OH  . TYR C 412 ? 0.1640 0.1527 0.1453 0.0155  -0.0113 -0.0014 404 TYR C OH  
12481 N N   . GLY C 413 ? 0.1486 0.1641 0.1495 0.0016  -0.0313 -0.0072 405 GLY C N   
12482 C CA  . GLY C 413 ? 0.1428 0.1595 0.1447 -0.0032 -0.0335 -0.0089 405 GLY C CA  
12483 C C   . GLY C 413 ? 0.1556 0.1683 0.1577 -0.0055 -0.0302 -0.0100 405 GLY C C   
12484 O O   . GLY C 413 ? 0.1410 0.1520 0.1441 -0.0035 -0.0263 -0.0095 405 GLY C O   
12485 N N   . VAL C 414 ? 0.1486 0.1591 0.1490 -0.0100 -0.0320 -0.0115 406 VAL C N   
12486 C CA  . VAL C 414 ? 0.1320 0.1384 0.1320 -0.0124 -0.0292 -0.0121 406 VAL C CA  
12487 C C   . VAL C 414 ? 0.1918 0.1886 0.1838 -0.0109 -0.0285 -0.0133 406 VAL C C   
12488 O O   . VAL C 414 ? 0.1421 0.1326 0.1291 -0.0133 -0.0301 -0.0147 406 VAL C O   
12489 C CB  . VAL C 414 ? 0.1690 0.1767 0.1708 -0.0182 -0.0311 -0.0128 406 VAL C CB  
12490 C CG1 . VAL C 414 ? 0.1528 0.1578 0.1552 -0.0206 -0.0278 -0.0126 406 VAL C CG1 
12491 C CG2 . VAL C 414 ? 0.2227 0.2415 0.2329 -0.0195 -0.0326 -0.0118 406 VAL C CG2 
12492 N N   . ARG C 415 ? 0.1304 0.1262 0.1214 -0.0068 -0.0259 -0.0127 407 ARG C N   
12493 C CA  . ARG C 415 ? 0.1119 0.1010 0.0965 -0.0045 -0.0253 -0.0137 407 ARG C CA  
12494 C C   . ARG C 415 ? 0.1384 0.1277 0.1247 -0.0022 -0.0214 -0.0128 407 ARG C C   
12495 O O   . ARG C 415 ? 0.1567 0.1465 0.1421 0.0008  -0.0201 -0.0121 407 ARG C O   
12496 C CB  . ARG C 415 ? 0.1157 0.1041 0.0959 -0.0023 -0.0272 -0.0140 407 ARG C CB  
12497 C CG  . ARG C 415 ? 0.1446 0.1330 0.1223 -0.0047 -0.0315 -0.0151 407 ARG C CG  
12498 C CD  . ARG C 415 ? 0.1505 0.1374 0.1221 -0.0020 -0.0329 -0.0154 407 ARG C CD  
12499 N NE  . ARG C 415 ? 0.1660 0.1525 0.1337 -0.0043 -0.0374 -0.0168 407 ARG C NE  
12500 C CZ  . ARG C 415 ? 0.1825 0.1754 0.1528 -0.0049 -0.0404 -0.0156 407 ARG C CZ  
12501 N NH1 . ARG C 415 ? 0.1291 0.1291 0.1064 -0.0028 -0.0393 -0.0128 407 ARG C NH1 
12502 N NH2 . ARG C 415 ? 0.2009 0.1931 0.1669 -0.0074 -0.0448 -0.0171 407 ARG C NH2 
12503 N N   . GLU C 416 ? 0.1605 0.1491 0.1486 -0.0039 -0.0195 -0.0127 408 GLU C N   
12504 C CA  . GLU C 416 ? 0.1163 0.1056 0.1062 -0.0024 -0.0161 -0.0120 408 GLU C CA  
12505 C C   . GLU C 416 ? 0.1118 0.0974 0.0977 -0.0002 -0.0153 -0.0125 408 GLU C C   
12506 O O   . GLU C 416 ? 0.1677 0.1543 0.1543 0.0017  -0.0131 -0.0119 408 GLU C O   
12507 C CB  . GLU C 416 ? 0.1587 0.1484 0.1507 -0.0052 -0.0145 -0.0119 408 GLU C CB  
12508 C CG  . GLU C 416 ? 0.1389 0.1340 0.1361 -0.0072 -0.0141 -0.0113 408 GLU C CG  
12509 C CD  . GLU C 416 ? 0.1766 0.1716 0.1735 -0.0106 -0.0170 -0.0117 408 GLU C CD  
12510 O OE1 . GLU C 416 ? 0.1886 0.1777 0.1803 -0.0114 -0.0192 -0.0125 408 GLU C OE1 
12511 O OE2 . GLU C 416 ? 0.1964 0.1973 0.1984 -0.0125 -0.0172 -0.0113 408 GLU C OE2 
12512 N N   . PHE C 417 ? 0.1279 0.1090 0.1098 -0.0005 -0.0167 -0.0136 409 PHE C N   
12513 C CA  . PHE C 417 ? 0.1047 0.0835 0.0838 0.0020  -0.0158 -0.0142 409 PHE C CA  
12514 C C   . PHE C 417 ? 0.1490 0.1286 0.1260 0.0045  -0.0156 -0.0143 409 PHE C C   
12515 O O   . PHE C 417 ? 0.1575 0.1383 0.1347 0.0063  -0.0134 -0.0139 409 PHE C O   
12516 C CB  . PHE C 417 ? 0.1134 0.0869 0.0887 0.0019  -0.0177 -0.0153 409 PHE C CB  
12517 C CG  . PHE C 417 ? 0.1292 0.1015 0.1035 0.0044  -0.0166 -0.0157 409 PHE C CG  
12518 C CD1 . PHE C 417 ? 0.1452 0.1215 0.1218 0.0057  -0.0141 -0.0151 409 PHE C CD1 
12519 C CD2 . PHE C 417 ? 0.1633 0.1306 0.1345 0.0054  -0.0182 -0.0165 409 PHE C CD2 
12520 C CE1 . PHE C 417 ? 0.1910 0.1679 0.1677 0.0077  -0.0133 -0.0154 409 PHE C CE1 
12521 C CE2 . PHE C 417 ? 0.1424 0.1098 0.1137 0.0082  -0.0174 -0.0168 409 PHE C CE2 
12522 C CZ  . PHE C 417 ? 0.1682 0.1412 0.1427 0.0093  -0.0150 -0.0162 409 PHE C CZ  
12523 N N   . GLY C 418 ? 0.1595 0.1384 0.1343 0.0043  -0.0180 -0.0148 410 GLY C N   
12524 C CA  . GLY C 418 ? 0.1708 0.1506 0.1429 0.0063  -0.0181 -0.0146 410 GLY C CA  
12525 C C   . GLY C 418 ? 0.1507 0.1342 0.1260 0.0073  -0.0159 -0.0125 410 GLY C C   
12526 O O   . GLY C 418 ? 0.1446 0.1280 0.1179 0.0091  -0.0141 -0.0120 410 GLY C O   
12527 N N   . MET C 419 ? 0.1562 0.1427 0.1365 0.0060  -0.0158 -0.0115 411 MET C N   
12528 C CA  . MET C 419 ? 0.1355 0.1243 0.1188 0.0073  -0.0137 -0.0096 411 MET C CA  
12529 C C   . MET C 419 ? 0.1531 0.1404 0.1361 0.0078  -0.0103 -0.0095 411 MET C C   
12530 O O   . MET C 419 ? 0.1173 0.1041 0.0990 0.0093  -0.0087 -0.0083 411 MET C O   
12531 C CB  . MET C 419 ? 0.1468 0.1390 0.1358 0.0061  -0.0136 -0.0090 411 MET C CB  
12532 C CG  . MET C 419 ? 0.1622 0.1556 0.1544 0.0079  -0.0110 -0.0074 411 MET C CG  
12533 S SD  . MET C 419 ? 0.1514 0.1495 0.1508 0.0073  -0.0102 -0.0070 411 MET C SD  
12534 C CE  . MET C 419 ? 0.1391 0.1352 0.1385 0.0042  -0.0078 -0.0087 411 MET C CE  
12535 N N   . GLY C 420 ? 0.1314 0.1180 0.1155 0.0063  -0.0094 -0.0105 412 GLY C N   
12536 C CA  . GLY C 420 ? 0.0976 0.0838 0.0822 0.0062  -0.0066 -0.0104 412 GLY C CA  
12537 C C   . GLY C 420 ? 0.1305 0.1161 0.1120 0.0076  -0.0058 -0.0106 412 GLY C C   
12538 O O   . GLY C 420 ? 0.1603 0.1461 0.1418 0.0078  -0.0034 -0.0098 412 GLY C O   
12539 N N   . ALA C 421 ? 0.1293 0.1139 0.1078 0.0086  -0.0076 -0.0118 413 ALA C N   
12540 C CA  . ALA C 421 ? 0.1252 0.1099 0.1009 0.0102  -0.0063 -0.0123 413 ALA C CA  
12541 C C   . ALA C 421 ? 0.1345 0.1189 0.1067 0.0115  -0.0058 -0.0111 413 ALA C C   
12542 O O   . ALA C 421 ? 0.1522 0.1373 0.1227 0.0122  -0.0033 -0.0107 413 ALA C O   
12543 C CB  . ALA C 421 ? 0.1197 0.1026 0.0930 0.0114  -0.0080 -0.0142 413 ALA C CB  
12544 N N   . ILE C 422 ? 0.1437 0.1274 0.1149 0.0115  -0.0080 -0.0104 414 ILE C N   
12545 C CA  . ILE C 422 ? 0.1136 0.0970 0.0815 0.0127  -0.0080 -0.0087 414 ILE C CA  
12546 C C   . ILE C 422 ? 0.1578 0.1413 0.1279 0.0126  -0.0052 -0.0065 414 ILE C C   
12547 O O   . ILE C 422 ? 0.1727 0.1552 0.1395 0.0132  -0.0033 -0.0050 414 ILE C O   
12548 C CB  . ILE C 422 ? 0.1282 0.1120 0.0955 0.0128  -0.0117 -0.0083 414 ILE C CB  
12549 C CG1 . ILE C 422 ? 0.1744 0.1565 0.1371 0.0127  -0.0142 -0.0106 414 ILE C CG1 
12550 C CG2 . ILE C 422 ? 0.1550 0.1389 0.1199 0.0143  -0.0119 -0.0057 414 ILE C CG2 
12551 C CD1 . ILE C 422 ? 0.1216 0.1047 0.0844 0.0116  -0.0184 -0.0109 414 ILE C CD1 
12552 N N   . MET C 423 ? 0.1165 0.1006 0.0917 0.0115  -0.0047 -0.0063 415 MET C N   
12553 C CA  . MET C 423 ? 0.1826 0.1654 0.1594 0.0112  -0.0019 -0.0047 415 MET C CA  
12554 C C   . MET C 423 ? 0.1619 0.1442 0.1374 0.0101  0.0011  -0.0049 415 MET C C   
12555 O O   . MET C 423 ? 0.1589 0.1391 0.1325 0.0100  0.0034  -0.0031 415 MET C O   
12556 C CB  . MET C 423 ? 0.1205 0.1037 0.1023 0.0100  -0.0014 -0.0053 415 MET C CB  
12557 C CG  . MET C 423 ? 0.1761 0.1605 0.1606 0.0113  -0.0032 -0.0044 415 MET C CG  
12558 S SD  . MET C 423 ? 0.2859 0.2717 0.2758 0.0096  -0.0023 -0.0058 415 MET C SD  
12559 C CE  . MET C 423 ? 0.2303 0.2125 0.2197 0.0083  0.0018  -0.0060 415 MET C CE  
12560 N N   . ASN C 424 ? 0.1305 0.1149 0.1070 0.0092  0.0012  -0.0068 416 ASN C N   
12561 C CA  . ASN C 424 ? 0.1762 0.1620 0.1525 0.0082  0.0039  -0.0070 416 ASN C CA  
12562 C C   . ASN C 424 ? 0.1742 0.1597 0.1459 0.0093  0.0054  -0.0059 416 ASN C C   
12563 O O   . ASN C 424 ? 0.1791 0.1644 0.1502 0.0079  0.0083  -0.0047 416 ASN C O   
12564 C CB  . ASN C 424 ? 0.1402 0.1291 0.1187 0.0081  0.0031  -0.0092 416 ASN C CB  
12565 C CG  . ASN C 424 ? 0.1275 0.1168 0.1098 0.0062  0.0024  -0.0099 416 ASN C CG  
12566 O OD1 . ASN C 424 ? 0.1559 0.1434 0.1394 0.0048  0.0032  -0.0092 416 ASN C OD1 
12567 N ND2 . ASN C 424 ? 0.1666 0.1576 0.1502 0.0065  0.0008  -0.0113 416 ASN C ND2 
12568 N N   . GLY C 425 ? 0.1548 0.1397 0.1226 0.0113  0.0034  -0.0063 417 GLY C N   
12569 C CA  . GLY C 425 ? 0.1393 0.1235 0.1013 0.0123  0.0048  -0.0052 417 GLY C CA  
12570 C C   . GLY C 425 ? 0.1331 0.1140 0.0923 0.0122  0.0053  -0.0021 417 GLY C C   
12571 O O   . GLY C 425 ? 0.1682 0.1481 0.1237 0.0117  0.0081  -0.0004 417 GLY C O   
12572 N N   . LEU C 426 ? 0.1346 0.1138 0.0957 0.0128  0.0029  -0.0011 418 LEU C N   
12573 C CA  . LEU C 426 ? 0.1890 0.1646 0.1482 0.0135  0.0033  0.0022  418 LEU C CA  
12574 C C   . LEU C 426 ? 0.1659 0.1392 0.1261 0.0114  0.0072  0.0034  418 LEU C C   
12575 O O   . LEU C 426 ? 0.1812 0.1509 0.1368 0.0113  0.0091  0.0061  418 LEU C O   
12576 C CB  . LEU C 426 ? 0.1738 0.1494 0.1369 0.0148  0.0004  0.0026  418 LEU C CB  
12577 C CG  . LEU C 426 ? 0.1278 0.1055 0.0897 0.0165  -0.0039 0.0024  418 LEU C CG  
12578 C CD1 . LEU C 426 ? 0.1922 0.1721 0.1607 0.0169  -0.0059 0.0019  418 LEU C CD1 
12579 C CD2 . LEU C 426 ? 0.1389 0.1143 0.0948 0.0184  -0.0052 0.0055  418 LEU C CD2 
12580 N N   . VAL C 427 ? 0.1713 0.1459 0.1367 0.0095  0.0084  0.0015  419 VAL C N   
12581 C CA  . VAL C 427 ? 0.2116 0.1842 0.1782 0.0067  0.0119  0.0021  419 VAL C CA  
12582 C C   . VAL C 427 ? 0.1681 0.1427 0.1320 0.0049  0.0147  0.0024  419 VAL C C   
12583 O O   . VAL C 427 ? 0.1858 0.1571 0.1474 0.0029  0.0176  0.0044  419 VAL C O   
12584 C CB  . VAL C 427 ? 0.2665 0.2411 0.2387 0.0047  0.0119  -0.0004 419 VAL C CB  
12585 C CG1 . VAL C 427 ? 0.3294 0.3029 0.3025 0.0010  0.0152  -0.0004 419 VAL C CG1 
12586 C CG2 . VAL C 427 ? 0.3482 0.3205 0.3228 0.0059  0.0105  -0.0005 419 VAL C CG2 
12587 N N   . LEU C 428 ? 0.1548 0.1349 0.1196 0.0054  0.0142  0.0002  420 LEU C N   
12588 C CA  . LEU C 428 ? 0.1654 0.1491 0.1290 0.0040  0.0173  0.0001  420 LEU C CA  
12589 C C   . LEU C 428 ? 0.2081 0.1885 0.1646 0.0044  0.0191  0.0029  420 LEU C C   
12590 O O   . LEU C 428 ? 0.2294 0.2105 0.1844 0.0019  0.0228  0.0041  420 LEU C O   
12591 C CB  . LEU C 428 ? 0.1252 0.1145 0.0904 0.0058  0.0163  -0.0027 420 LEU C CB  
12592 C CG  . LEU C 428 ? 0.1785 0.1719 0.1506 0.0049  0.0153  -0.0050 420 LEU C CG  
12593 C CD1 . LEU C 428 ? 0.2327 0.2288 0.2054 0.0078  0.0130  -0.0074 420 LEU C CD1 
12594 C CD2 . LEU C 428 ? 0.1808 0.1789 0.1566 0.0018  0.0185  -0.0050 420 LEU C CD2 
12595 N N   . HIS C 429 ? 0.2248 0.2018 0.1765 0.0072  0.0164  0.0040  421 HIS C N   
12596 C CA  . HIS C 429 ? 0.2047 0.1787 0.1483 0.0078  0.0175  0.0067  421 HIS C CA  
12597 C C   . HIS C 429 ? 0.2061 0.1746 0.1474 0.0055  0.0203  0.0103  421 HIS C C   
12598 O O   . HIS C 429 ? 0.2110 0.1782 0.1465 0.0040  0.0233  0.0124  421 HIS C O   
12599 C CB  . HIS C 429 ? 0.1836 0.1551 0.1228 0.0110  0.0132  0.0075  421 HIS C CB  
12600 C CG  . HIS C 429 ? 0.1825 0.1509 0.1123 0.0117  0.0136  0.0103  421 HIS C CG  
12601 N ND1 . HIS C 429 ? 0.1964 0.1588 0.1219 0.0115  0.0143  0.0146  421 HIS C ND1 
12602 C CD2 . HIS C 429 ? 0.1764 0.1463 0.0993 0.0127  0.0136  0.0095  421 HIS C CD2 
12603 C CE1 . HIS C 429 ? 0.2183 0.1790 0.1346 0.0122  0.0144  0.0166  421 HIS C CE1 
12604 N NE2 . HIS C 429 ? 0.2229 0.1881 0.1373 0.0128  0.0141  0.0133  421 HIS C NE2 
12605 N N   . GLY C 430 ? 0.1935 0.1579 0.1383 0.0051  0.0194  0.0110  422 GLY C N   
12606 C CA  . GLY C 430 ? 0.2366 0.1935 0.1780 0.0037  0.0215  0.0146  422 GLY C CA  
12607 C C   . GLY C 430 ? 0.2558 0.2070 0.1928 0.0074  0.0184  0.0177  422 GLY C C   
12608 O O   . GLY C 430 ? 0.2207 0.1741 0.1544 0.0102  0.0154  0.0179  422 GLY C O   
12609 N N   . GLY C 431 ? 0.2254 0.1692 0.1625 0.0076  0.0189  0.0201  423 GLY C N   
12610 C CA  . GLY C 431 ? 0.1810 0.1190 0.1141 0.0114  0.0163  0.0237  423 GLY C CA  
12611 C C   . GLY C 431 ? 0.2080 0.1468 0.1472 0.0150  0.0128  0.0227  423 GLY C C   
12612 O O   . GLY C 431 ? 0.2217 0.1551 0.1594 0.0183  0.0113  0.0258  423 GLY C O   
12613 N N   . VAL C 432 ? 0.2000 0.1456 0.1461 0.0147  0.0117  0.0186  424 VAL C N   
12614 C CA  . VAL C 432 ? 0.2383 0.1857 0.1905 0.0176  0.0090  0.0174  424 VAL C CA  
12615 C C   . VAL C 432 ? 0.2421 0.1915 0.2008 0.0150  0.0109  0.0137  424 VAL C C   
12616 O O   . VAL C 432 ? 0.2297 0.1817 0.1889 0.0115  0.0128  0.0116  424 VAL C O   
12617 C CB  . VAL C 432 ? 0.2656 0.2199 0.2188 0.0199  0.0045  0.0165  424 VAL C CB  
12618 C CG1 . VAL C 432 ? 0.2192 0.1716 0.1654 0.0224  0.0020  0.0201  424 VAL C CG1 
12619 C CG2 . VAL C 432 ? 0.2083 0.1685 0.1622 0.0174  0.0047  0.0129  424 VAL C CG2 
12620 N N   . LYS C 433 ? 0.2028 0.1513 0.1664 0.0170  0.0102  0.0130  425 LYS C N   
12621 C CA  A LYS C 433 ? 0.2066 0.1569 0.1755 0.0148  0.0116  0.0095  425 LYS C CA  
12622 C CA  B LYS C 433 ? 0.2078 0.1580 0.1767 0.0148  0.0116  0.0095  425 LYS C CA  
12623 C C   . LYS C 433 ? 0.1846 0.1411 0.1589 0.0170  0.0087  0.0078  425 LYS C C   
12624 O O   . LYS C 433 ? 0.1997 0.1554 0.1768 0.0204  0.0078  0.0088  425 LYS C O   
12625 C CB  A LYS C 433 ? 0.2004 0.1426 0.1694 0.0142  0.0148  0.0097  425 LYS C CB  
12626 C CB  B LYS C 433 ? 0.1998 0.1420 0.1688 0.0145  0.0147  0.0098  425 LYS C CB  
12627 C CG  A LYS C 433 ? 0.1701 0.1064 0.1342 0.0103  0.0181  0.0108  425 LYS C CG  
12628 C CG  B LYS C 433 ? 0.1638 0.1069 0.1371 0.0122  0.0162  0.0061  425 LYS C CG  
12629 C CD  A LYS C 433 ? 0.2005 0.1277 0.1641 0.0090  0.0211  0.0104  425 LYS C CD  
12630 C CD  B LYS C 433 ? 0.1807 0.1143 0.1528 0.0116  0.0195  0.0060  425 LYS C CD  
12631 C CE  A LYS C 433 ? 0.2253 0.1552 0.1932 0.0063  0.0221  0.0061  425 LYS C CE  
12632 C CE  B LYS C 433 ? 0.1991 0.1264 0.1660 0.0075  0.0222  0.0072  425 LYS C CE  
12633 N NZ  A LYS C 433 ? 0.1892 0.1248 0.1576 0.0012  0.0226  0.0040  425 LYS C NZ  
12634 N NZ  B LYS C 433 ? 0.2237 0.1566 0.1915 0.0022  0.0228  0.0047  425 LYS C NZ  
12635 N N   . PRO C 434 ? 0.2223 0.1851 0.1984 0.0154  0.0072  0.0053  426 PRO C N   
12636 C CA  . PRO C 434 ? 0.2178 0.1863 0.1983 0.0169  0.0043  0.0040  426 PRO C CA  
12637 C C   . PRO C 434 ? 0.1776 0.1477 0.1630 0.0154  0.0055  0.0014  426 PRO C C   
12638 O O   . PRO C 434 ? 0.1472 0.1158 0.1323 0.0124  0.0078  -0.0004 426 PRO C O   
12639 C CB  . PRO C 434 ? 0.1945 0.1674 0.1729 0.0157  0.0021  0.0029  426 PRO C CB  
12640 C CG  . PRO C 434 ? 0.2107 0.1822 0.1871 0.0127  0.0048  0.0018  426 PRO C CG  
12641 C CD  . PRO C 434 ? 0.1937 0.1589 0.1674 0.0126  0.0078  0.0041  426 PRO C CD  
12642 N N   . PHE C 435 ? 0.1859 0.1596 0.1759 0.0174  0.0040  0.0011  427 PHE C N   
12643 C CA  . PHE C 435 ? 0.1749 0.1519 0.1691 0.0158  0.0045  -0.0014 427 PHE C CA  
12644 C C   . PHE C 435 ? 0.1621 0.1457 0.1590 0.0160  0.0010  -0.0018 427 PHE C C   
12645 O O   . PHE C 435 ? 0.1580 0.1437 0.1545 0.0180  -0.0018 -0.0000 427 PHE C O   
12646 C CB  . PHE C 435 ? 0.1496 0.1244 0.1472 0.0174  0.0073  -0.0018 427 PHE C CB  
12647 C CG  . PHE C 435 ? 0.1513 0.1292 0.1534 0.0217  0.0059  -0.0001 427 PHE C CG  
12648 C CD1 . PHE C 435 ? 0.1860 0.1715 0.1938 0.0219  0.0044  -0.0010 427 PHE C CD1 
12649 C CD2 . PHE C 435 ? 0.1417 0.1150 0.1429 0.0255  0.0064  0.0026  427 PHE C CD2 
12650 C CE1 . PHE C 435 ? 0.1785 0.1685 0.1918 0.0259  0.0031  0.0006  427 PHE C CE1 
12651 C CE2 . PHE C 435 ? 0.2064 0.1834 0.2126 0.0301  0.0049  0.0044  427 PHE C CE2 
12652 C CZ  . PHE C 435 ? 0.1727 0.1589 0.1855 0.0303  0.0032  0.0033  427 PHE C CZ  
12653 N N   . GLY C 436 ? 0.1172 0.1036 0.1160 0.0133  0.0009  -0.0040 428 GLY C N   
12654 C CA  . GLY C 436 ? 0.1223 0.1142 0.1236 0.0127  -0.0022 -0.0044 428 GLY C CA  
12655 C C   . GLY C 436 ? 0.1421 0.1365 0.1469 0.0105  -0.0009 -0.0062 428 GLY C C   
12656 O O   . GLY C 436 ? 0.1540 0.1458 0.1569 0.0083  0.0011  -0.0077 428 GLY C O   
12657 N N   . ALA C 437 ? 0.1130 0.1129 0.1228 0.0109  -0.0020 -0.0061 429 ALA C N   
12658 C CA  . ALA C 437 ? 0.1202 0.1229 0.1336 0.0089  0.0001  -0.0075 429 ALA C CA  
12659 C C   . ALA C 437 ? 0.1040 0.1106 0.1184 0.0056  -0.0024 -0.0082 429 ALA C C   
12660 O O   . ALA C 437 ? 0.1282 0.1377 0.1432 0.0057  -0.0060 -0.0074 429 ALA C O   
12661 C CB  . ALA C 437 ? 0.1102 0.1168 0.1299 0.0119  0.0020  -0.0069 429 ALA C CB  
12662 N N   . THR C 438 ? 0.1146 0.1207 0.1284 0.0025  -0.0006 -0.0095 430 THR C N   
12663 C CA  . THR C 438 ? 0.1272 0.1364 0.1420 -0.0011 -0.0021 -0.0099 430 THR C CA  
12664 C C   . THR C 438 ? 0.1482 0.1581 0.1640 -0.0033 0.0016  -0.0110 430 THR C C   
12665 O O   . THR C 438 ? 0.1190 0.1268 0.1345 -0.0019 0.0050  -0.0116 430 THR C O   
12666 C CB  . THR C 438 ? 0.1477 0.1523 0.1567 -0.0031 -0.0051 -0.0102 430 THR C CB  
12667 O OG1 . THR C 438 ? 0.1438 0.1502 0.1534 -0.0068 -0.0067 -0.0104 430 THR C OG1 
12668 C CG2 . THR C 438 ? 0.0929 0.0920 0.0970 -0.0038 -0.0035 -0.0109 430 THR C CG2 
12669 N N   . PHE C 439 ? 0.1238 0.1361 0.1403 -0.0071 0.0011  -0.0112 431 PHE C N   
12670 C CA  . PHE C 439 ? 0.1620 0.1739 0.1774 -0.0098 0.0046  -0.0120 431 PHE C CA  
12671 C C   . PHE C 439 ? 0.0961 0.1007 0.1041 -0.0109 0.0048  -0.0126 431 PHE C C   
12672 O O   . PHE C 439 ? 0.1339 0.1346 0.1379 -0.0112 0.0017  -0.0122 431 PHE C O   
12673 C CB  . PHE C 439 ? 0.1542 0.1695 0.1708 -0.0143 0.0040  -0.0117 431 PHE C CB  
12674 C CG  . PHE C 439 ? 0.1913 0.2159 0.2164 -0.0142 0.0043  -0.0113 431 PHE C CG  
12675 C CD1 . PHE C 439 ? 0.1616 0.1909 0.1927 -0.0096 0.0046  -0.0111 431 PHE C CD1 
12676 C CD2 . PHE C 439 ? 0.3307 0.3594 0.3578 -0.0189 0.0041  -0.0110 431 PHE C CD2 
12677 C CE1 . PHE C 439 ? 0.2392 0.2784 0.2790 -0.0092 0.0045  -0.0105 431 PHE C CE1 
12678 C CE2 . PHE C 439 ? 0.3405 0.3793 0.3764 -0.0192 0.0042  -0.0106 431 PHE C CE2 
12679 C CZ  . PHE C 439 ? 0.3093 0.3538 0.3519 -0.0141 0.0043  -0.0104 431 PHE C CZ  
12680 N N   . LEU C 440 ? 0.0980 0.1012 0.1042 -0.0116 0.0085  -0.0137 432 LEU C N   
12681 C CA  . LEU C 440 ? 0.0995 0.0968 0.0990 -0.0131 0.0084  -0.0142 432 LEU C CA  
12682 C C   . LEU C 440 ? 0.1477 0.1423 0.1428 -0.0161 0.0053  -0.0133 432 LEU C C   
12683 O O   . LEU C 440 ? 0.1238 0.1144 0.1149 -0.0157 0.0031  -0.0131 432 LEU C O   
12684 C CB  . LEU C 440 ? 0.1375 0.1339 0.1350 -0.0143 0.0128  -0.0157 432 LEU C CB  
12685 C CG  . LEU C 440 ? 0.1489 0.1400 0.1392 -0.0165 0.0125  -0.0163 432 LEU C CG  
12686 C CD1 . LEU C 440 ? 0.1682 0.1562 0.1572 -0.0145 0.0106  -0.0163 432 LEU C CD1 
12687 C CD2 . LEU C 440 ? 0.1645 0.1545 0.1520 -0.0180 0.0170  -0.0182 432 LEU C CD2 
12688 N N   . MET C 441 ? 0.1413 0.1381 0.1374 -0.0189 0.0049  -0.0126 433 MET C N   
12689 C CA  . MET C 441 ? 0.1163 0.1089 0.1075 -0.0217 0.0019  -0.0115 433 MET C CA  
12690 C C   . MET C 441 ? 0.1488 0.1387 0.1393 -0.0194 -0.0022 -0.0111 433 MET C C   
12691 O O   . MET C 441 ? 0.1461 0.1309 0.1317 -0.0196 -0.0045 -0.0107 433 MET C O   
12692 C CB  . MET C 441 ? 0.1558 0.1510 0.1485 -0.0256 0.0022  -0.0107 433 MET C CB  
12693 C CG  . MET C 441 ? 0.1636 0.1529 0.1506 -0.0287 -0.0009 -0.0094 433 MET C CG  
12694 S SD  . MET C 441 ? 0.1681 0.1513 0.1465 -0.0303 -0.0003 -0.0088 433 MET C SD  
12695 C CE  . MET C 441 ? 0.1206 0.1085 0.0999 -0.0339 0.0050  -0.0092 433 MET C CE  
12696 N N   . PHE C 442 ? 0.1561 0.1491 0.1509 -0.0169 -0.0030 -0.0113 434 PHE C N   
12697 C CA  . PHE C 442 ? 0.1761 0.1663 0.1693 -0.0150 -0.0065 -0.0112 434 PHE C CA  
12698 C C   . PHE C 442 ? 0.1583 0.1468 0.1502 -0.0116 -0.0063 -0.0116 434 PHE C C   
12699 O O   . PHE C 442 ? 0.1788 0.1655 0.1693 -0.0096 -0.0085 -0.0117 434 PHE C O   
12700 C CB  . PHE C 442 ? 0.1889 0.1831 0.1863 -0.0148 -0.0081 -0.0111 434 PHE C CB  
12701 C CG  . PHE C 442 ? 0.2411 0.2378 0.2403 -0.0190 -0.0081 -0.0107 434 PHE C CG  
12702 C CD1 . PHE C 442 ? 0.2407 0.2323 0.2351 -0.0225 -0.0088 -0.0102 434 PHE C CD1 
12703 C CD2 . PHE C 442 ? 0.2627 0.2670 0.2686 -0.0195 -0.0069 -0.0106 434 PHE C CD2 
12704 C CE1 . PHE C 442 ? 0.2681 0.2617 0.2637 -0.0271 -0.0083 -0.0096 434 PHE C CE1 
12705 C CE2 . PHE C 442 ? 0.3101 0.3178 0.3183 -0.0239 -0.0064 -0.0102 434 PHE C CE2 
12706 C CZ  . PHE C 442 ? 0.3135 0.3156 0.3163 -0.0281 -0.0069 -0.0097 434 PHE C CZ  
12707 N N   . SER C 443 ? 0.1192 0.1078 0.1108 -0.0114 -0.0036 -0.0120 435 SER C N   
12708 C CA  . SER C 443 ? 0.1412 0.1274 0.1303 -0.0098 -0.0038 -0.0123 435 SER C CA  
12709 C C   . SER C 443 ? 0.1924 0.1751 0.1776 -0.0102 -0.0068 -0.0119 435 SER C C   
12710 O O   . SER C 443 ? 0.1599 0.1417 0.1442 -0.0081 -0.0079 -0.0120 435 SER C O   
12711 C CB  . SER C 443 ? 0.1501 0.1361 0.1382 -0.0110 -0.0010 -0.0130 435 SER C CB  
12712 O OG  . SER C 443 ? 0.1600 0.1448 0.1450 -0.0141 -0.0007 -0.0129 435 SER C OG  
12713 N N   . GLU C 444 ? 0.1218 0.1025 0.1048 -0.0128 -0.0079 -0.0113 436 GLU C N   
12714 C CA  . GLU C 444 ? 0.1202 0.0964 0.0992 -0.0128 -0.0107 -0.0107 436 GLU C CA  
12715 C C   . GLU C 444 ? 0.1297 0.1038 0.1084 -0.0106 -0.0132 -0.0110 436 GLU C C   
12716 O O   . GLU C 444 ? 0.2386 0.2094 0.2148 -0.0087 -0.0152 -0.0109 436 GLU C O   
12717 C CB  . GLU C 444 ? 0.1642 0.1376 0.1399 -0.0164 -0.0111 -0.0096 436 GLU C CB  
12718 C CG  . GLU C 444 ? 0.1829 0.1577 0.1572 -0.0186 -0.0087 -0.0095 436 GLU C CG  
12719 C CD  . GLU C 444 ? 0.2029 0.1736 0.1718 -0.0219 -0.0096 -0.0080 436 GLU C CD  
12720 O OE1 . GLU C 444 ? 0.2010 0.1681 0.1681 -0.0233 -0.0114 -0.0070 436 GLU C OE1 
12721 O OE2 . GLU C 444 ? 0.2188 0.1896 0.1847 -0.0233 -0.0085 -0.0079 436 GLU C OE2 
12722 N N   . TYR C 445 ? 0.1231 0.0994 0.1044 -0.0108 -0.0131 -0.0114 437 TYR C N   
12723 C CA  . TYR C 445 ? 0.1234 0.0976 0.1036 -0.0089 -0.0154 -0.0120 437 TYR C CA  
12724 C C   . TYR C 445 ? 0.2319 0.2074 0.2124 -0.0051 -0.0149 -0.0127 437 TYR C C   
12725 O O   . TYR C 445 ? 0.2605 0.2333 0.2386 -0.0030 -0.0165 -0.0134 437 TYR C O   
12726 C CB  . TYR C 445 ? 0.1295 0.1063 0.1122 -0.0105 -0.0161 -0.0122 437 TYR C CB  
12727 C CG  . TYR C 445 ? 0.1745 0.1488 0.1559 -0.0145 -0.0177 -0.0119 437 TYR C CG  
12728 C CD1 . TYR C 445 ? 0.1797 0.1529 0.1602 -0.0177 -0.0165 -0.0109 437 TYR C CD1 
12729 C CD2 . TYR C 445 ? 0.1829 0.1559 0.1636 -0.0156 -0.0202 -0.0126 437 TYR C CD2 
12730 C CE1 . TYR C 445 ? 0.1536 0.1243 0.1327 -0.0220 -0.0177 -0.0103 437 TYR C CE1 
12731 C CE2 . TYR C 445 ? 0.1944 0.1650 0.1740 -0.0201 -0.0216 -0.0123 437 TYR C CE2 
12732 C CZ  . TYR C 445 ? 0.1918 0.1614 0.1709 -0.0234 -0.0202 -0.0110 437 TYR C CZ  
12733 O OH  . TYR C 445 ? 0.1883 0.1552 0.1660 -0.0284 -0.0213 -0.0105 437 TYR C OH  
12734 N N   . GLU C 446 ? 0.1429 0.1223 0.1262 -0.0044 -0.0124 -0.0125 438 GLU C N   
12735 C CA  . GLU C 446 ? 0.1117 0.0925 0.0953 -0.0015 -0.0115 -0.0128 438 GLU C CA  
12736 C C   . GLU C 446 ? 0.1399 0.1213 0.1235 -0.0011 -0.0102 -0.0128 438 GLU C C   
12737 O O   . GLU C 446 ? 0.1448 0.1282 0.1294 0.0003  -0.0087 -0.0128 438 GLU C O   
12738 C CB  . GLU C 446 ? 0.1579 0.1418 0.1443 -0.0008 -0.0098 -0.0124 438 GLU C CB  
12739 C CG  . GLU C 446 ? 0.1692 0.1551 0.1583 -0.0024 -0.0074 -0.0121 438 GLU C CG  
12740 C CD  . GLU C 446 ? 0.2084 0.1964 0.2001 -0.0008 -0.0056 -0.0115 438 GLU C CD  
12741 O OE1 . GLU C 446 ? 0.1689 0.1568 0.1597 0.0014  -0.0060 -0.0111 438 GLU C OE1 
12742 O OE2 . GLU C 446 ? 0.1711 0.1606 0.1654 -0.0016 -0.0037 -0.0115 438 GLU C OE2 
12743 N N   . ARG C 447 ? 0.1333 0.1131 0.1155 -0.0025 -0.0112 -0.0125 439 ARG C N   
12744 C CA  . ARG C 447 ? 0.1501 0.1315 0.1326 -0.0033 -0.0102 -0.0124 439 ARG C CA  
12745 C C   . ARG C 447 ? 0.1785 0.1622 0.1621 -0.0009 -0.0100 -0.0127 439 ARG C C   
12746 O O   . ARG C 447 ? 0.1496 0.1361 0.1348 -0.0016 -0.0082 -0.0129 439 ARG C O   
12747 C CB  . ARG C 447 ? 0.1347 0.1136 0.1145 -0.0048 -0.0121 -0.0117 439 ARG C CB  
12748 C CG  . ARG C 447 ? 0.1348 0.1157 0.1144 -0.0057 -0.0120 -0.0115 439 ARG C CG  
12749 C CD  . ARG C 447 ? 0.1564 0.1392 0.1367 -0.0082 -0.0092 -0.0121 439 ARG C CD  
12750 N NE  . ARG C 447 ? 0.1656 0.1500 0.1449 -0.0097 -0.0096 -0.0122 439 ARG C NE  
12751 C CZ  . ARG C 447 ? 0.1901 0.1739 0.1668 -0.0128 -0.0088 -0.0124 439 ARG C CZ  
12752 N NH1 . ARG C 447 ? 0.1411 0.1229 0.1165 -0.0146 -0.0068 -0.0126 439 ARG C NH1 
12753 N NH2 . ARG C 447 ? 0.1676 0.1531 0.1430 -0.0143 -0.0098 -0.0126 439 ARG C NH2 
12754 N N   . ASN C 448 ? 0.1459 0.1285 0.1286 0.0018  -0.0117 -0.0130 440 ASN C N   
12755 C CA  . ASN C 448 ? 0.1708 0.1568 0.1552 0.0041  -0.0111 -0.0133 440 ASN C CA  
12756 C C   . ASN C 448 ? 0.1571 0.1456 0.1428 0.0047  -0.0085 -0.0136 440 ASN C C   
12757 O O   . ASN C 448 ? 0.1474 0.1397 0.1352 0.0051  -0.0070 -0.0137 440 ASN C O   
12758 C CB  . ASN C 448 ? 0.1588 0.1430 0.1420 0.0075  -0.0130 -0.0138 440 ASN C CB  
12759 C CG  . ASN C 448 ? 0.1765 0.1658 0.1626 0.0099  -0.0125 -0.0140 440 ASN C CG  
12760 O OD1 . ASN C 448 ? 0.1867 0.1778 0.1734 0.0126  -0.0112 -0.0149 440 ASN C OD1 
12761 N ND2 . ASN C 448 ? 0.1623 0.1546 0.1502 0.0087  -0.0134 -0.0132 440 ASN C ND2 
12762 N N   . ALA C 449 ? 0.1668 0.1532 0.1513 0.0046  -0.0081 -0.0135 441 ALA C N   
12763 C CA  . ALA C 449 ? 0.2012 0.1892 0.1862 0.0050  -0.0059 -0.0132 441 ALA C CA  
12764 C C   . ALA C 449 ? 0.1857 0.1751 0.1727 0.0027  -0.0037 -0.0127 441 ALA C C   
12765 O O   . ALA C 449 ? 0.1449 0.1359 0.1325 0.0027  -0.0016 -0.0124 441 ALA C O   
12766 C CB  . ALA C 449 ? 0.1857 0.1716 0.1691 0.0055  -0.0066 -0.0130 441 ALA C CB  
12767 N N   . LEU C 450 ? 0.1211 0.1094 0.1085 0.0006  -0.0039 -0.0128 442 LEU C N   
12768 C CA  . LEU C 450 ? 0.1622 0.1509 0.1505 -0.0018 -0.0018 -0.0128 442 LEU C CA  
12769 C C   . LEU C 450 ? 0.1615 0.1531 0.1507 -0.0027 -0.0016 -0.0132 442 LEU C C   
12770 O O   . LEU C 450 ? 0.1524 0.1449 0.1425 -0.0041 0.0005  -0.0132 442 LEU C O   
12771 C CB  . LEU C 450 ? 0.1417 0.1289 0.1295 -0.0039 -0.0020 -0.0132 442 LEU C CB  
12772 C CG  . LEU C 450 ? 0.2926 0.2784 0.2810 -0.0040 -0.0008 -0.0130 442 LEU C CG  
12773 C CD1 . LEU C 450 ? 0.1928 0.1788 0.1817 -0.0018 -0.0022 -0.0124 442 LEU C CD1 
12774 C CD2 . LEU C 450 ? 0.2910 0.2762 0.2785 -0.0062 -0.0011 -0.0134 442 LEU C CD2 
12775 N N   . ARG C 451 ? 0.1592 0.1524 0.1485 -0.0020 -0.0040 -0.0133 443 ARG C N   
12776 C CA  . ARG C 451 ? 0.1236 0.1212 0.1149 -0.0026 -0.0044 -0.0135 443 ARG C CA  
12777 C C   . ARG C 451 ? 0.1384 0.1395 0.1318 -0.0011 -0.0027 -0.0134 443 ARG C C   
12778 O O   . ARG C 451 ? 0.1077 0.1125 0.1032 -0.0031 -0.0014 -0.0135 443 ARG C O   
12779 C CB  . ARG C 451 ? 0.1203 0.1186 0.1113 -0.0012 -0.0076 -0.0132 443 ARG C CB  
12780 C CG  . ARG C 451 ? 0.1119 0.1160 0.1058 -0.0016 -0.0087 -0.0132 443 ARG C CG  
12781 C CD  . ARG C 451 ? 0.1507 0.1547 0.1441 0.0006  -0.0122 -0.0126 443 ARG C CD  
12782 N NE  . ARG C 451 ? 0.1506 0.1598 0.1459 -0.0011 -0.0140 -0.0122 443 ARG C NE  
12783 C CZ  . ARG C 451 ? 0.1493 0.1658 0.1494 0.0005  -0.0145 -0.0122 443 ARG C CZ  
12784 N NH1 . ARG C 451 ? 0.1652 0.1843 0.1682 0.0040  -0.0129 -0.0127 443 ARG C NH1 
12785 N NH2 . ARG C 451 ? 0.1558 0.1776 0.1578 -0.0015 -0.0167 -0.0119 443 ARG C NH2 
12786 N N   . MET C 452 ? 0.1043 0.1043 0.0967 0.0020  -0.0026 -0.0134 444 MET C N   
12787 C CA  . MET C 452 ? 0.1371 0.1403 0.1305 0.0035  -0.0006 -0.0134 444 MET C CA  
12788 C C   . MET C 452 ? 0.1430 0.1454 0.1360 0.0012  0.0024  -0.0126 444 MET C C   
12789 O O   . MET C 452 ? 0.1508 0.1569 0.1454 0.0003  0.0046  -0.0124 444 MET C O   
12790 C CB  . MET C 452 ? 0.1152 0.1161 0.1059 0.0070  -0.0012 -0.0137 444 MET C CB  
12791 C CG  . MET C 452 ? 0.1231 0.1241 0.1140 0.0099  -0.0036 -0.0146 444 MET C CG  
12792 S SD  . MET C 452 ? 0.1687 0.1777 0.1646 0.0115  -0.0031 -0.0149 444 MET C SD  
12793 C CE  . MET C 452 ? 0.2108 0.2229 0.2064 0.0133  0.0006  -0.0154 444 MET C CE  
12794 N N   . ALA C 453 ? 0.1432 0.1407 0.1341 0.0002  0.0027  -0.0122 445 ALA C N   
12795 C CA  . ALA C 453 ? 0.1360 0.1312 0.1262 -0.0018 0.0054  -0.0114 445 ALA C CA  
12796 C C   . ALA C 453 ? 0.1487 0.1459 0.1408 -0.0055 0.0065  -0.0118 445 ALA C C   
12797 O O   . ALA C 453 ? 0.1592 0.1573 0.1517 -0.0073 0.0089  -0.0113 445 ALA C O   
12798 C CB  . ALA C 453 ? 0.1334 0.1236 0.1220 -0.0016 0.0052  -0.0110 445 ALA C CB  
12799 N N   . ALA C 454 ? 0.0958 0.0938 0.0888 -0.0071 0.0048  -0.0128 446 ALA C N   
12800 C CA  . ALA C 454 ? 0.0978 0.0978 0.0920 -0.0111 0.0054  -0.0135 446 ALA C CA  
12801 C C   . ALA C 454 ? 0.1211 0.1285 0.1190 -0.0115 0.0053  -0.0134 446 ALA C C   
12802 O O   . ALA C 454 ? 0.1464 0.1559 0.1456 -0.0150 0.0071  -0.0135 446 ALA C O   
12803 C CB  . ALA C 454 ? 0.1498 0.1490 0.1431 -0.0124 0.0031  -0.0144 446 ALA C CB  
12804 N N   . LEU C 455 ? 0.1494 0.1609 0.1490 -0.0081 0.0034  -0.0134 447 LEU C N   
12805 C CA  . LEU C 455 ? 0.1562 0.1759 0.1602 -0.0074 0.0036  -0.0134 447 LEU C CA  
12806 C C   . LEU C 455 ? 0.1688 0.1900 0.1732 -0.0079 0.0072  -0.0128 447 LEU C C   
12807 O O   . LEU C 455 ? 0.1502 0.1779 0.1584 -0.0103 0.0087  -0.0127 447 LEU C O   
12808 C CB  . LEU C 455 ? 0.1266 0.1485 0.1316 -0.0026 0.0012  -0.0136 447 LEU C CB  
12809 C CG  . LEU C 455 ? 0.2176 0.2483 0.2276 -0.0003 0.0016  -0.0138 447 LEU C CG  
12810 C CD1 . LEU C 455 ? 0.2685 0.3073 0.2838 -0.0037 0.0009  -0.0139 447 LEU C CD1 
12811 C CD2 . LEU C 455 ? 0.2660 0.2963 0.2759 0.0048  -0.0010 -0.0142 447 LEU C CD2 
12812 N N   . MET C 456 ? 0.1351 0.1508 0.1356 -0.0058 0.0086  -0.0121 448 MET C N   
12813 C CA  . MET C 456 ? 0.1332 0.1490 0.1325 -0.0062 0.0121  -0.0111 448 MET C CA  
12814 C C   . MET C 456 ? 0.1213 0.1334 0.1192 -0.0109 0.0145  -0.0102 448 MET C C   
12815 O O   . MET C 456 ? 0.1556 0.1674 0.1522 -0.0120 0.0175  -0.0090 448 MET C O   
12816 C CB  . MET C 456 ? 0.1247 0.1355 0.1192 -0.0025 0.0122  -0.0105 448 MET C CB  
12817 C CG  . MET C 456 ? 0.1816 0.1952 0.1764 0.0019  0.0107  -0.0115 448 MET C CG  
12818 S SD  . MET C 456 ? 0.1977 0.2060 0.1861 0.0052  0.0113  -0.0110 448 MET C SD  
12819 C CE  . MET C 456 ? 0.1968 0.1999 0.1835 0.0071  0.0070  -0.0119 448 MET C CE  
12820 N N   . LYS C 457 ? 0.1341 0.1423 0.1315 -0.0135 0.0134  -0.0108 449 LYS C N   
12821 C CA  A LYS C 457 ? 0.1404 0.1428 0.1357 -0.0176 0.0156  -0.0104 449 LYS C CA  
12822 C CA  B LYS C 457 ? 0.1453 0.1478 0.1406 -0.0176 0.0156  -0.0104 449 LYS C CA  
12823 C C   . LYS C 457 ? 0.1717 0.1666 0.1624 -0.0158 0.0176  -0.0086 449 LYS C C   
12824 O O   . LYS C 457 ? 0.1979 0.1895 0.1866 -0.0183 0.0204  -0.0073 449 LYS C O   
12825 C CB  A LYS C 457 ? 0.1720 0.1798 0.1703 -0.0225 0.0175  -0.0105 449 LYS C CB  
12826 C CB  B LYS C 457 ? 0.1727 0.1805 0.1709 -0.0224 0.0176  -0.0104 449 LYS C CB  
12827 C CG  A LYS C 457 ? 0.2085 0.2250 0.2119 -0.0241 0.0149  -0.0120 449 LYS C CG  
12828 C CG  B LYS C 457 ? 0.2113 0.2275 0.2146 -0.0245 0.0152  -0.0119 449 LYS C CG  
12829 C CD  A LYS C 457 ? 0.2569 0.2812 0.2648 -0.0288 0.0166  -0.0120 449 LYS C CD  
12830 C CD  B LYS C 457 ? 0.2528 0.2754 0.2598 -0.0297 0.0171  -0.0119 449 LYS C CD  
12831 C CE  A LYS C 457 ? 0.2967 0.3149 0.3020 -0.0351 0.0184  -0.0122 449 LYS C CE  
12832 C CE  B LYS C 457 ? 0.2743 0.3043 0.2858 -0.0328 0.0141  -0.0134 449 LYS C CE  
12833 N NZ  A LYS C 457 ? 0.3535 0.3793 0.3631 -0.0406 0.0202  -0.0120 449 LYS C NZ  
12834 N NZ  B LYS C 457 ? 0.3577 0.3922 0.3721 -0.0396 0.0159  -0.0136 449 LYS C NZ  
12835 N N   . ILE C 458 ? 0.1620 0.1539 0.1507 -0.0116 0.0159  -0.0084 450 ILE C N   
12836 C CA  . ILE C 458 ? 0.1726 0.1579 0.1573 -0.0094 0.0168  -0.0066 450 ILE C CA  
12837 C C   . ILE C 458 ? 0.2012 0.1809 0.1852 -0.0088 0.0158  -0.0071 450 ILE C C   
12838 O O   . ILE C 458 ? 0.1413 0.1223 0.1272 -0.0098 0.0145  -0.0089 450 ILE C O   
12839 C CB  . ILE C 458 ? 0.1793 0.1666 0.1624 -0.0053 0.0156  -0.0058 450 ILE C CB  
12840 C CG1 . ILE C 458 ? 0.1524 0.1426 0.1375 -0.0029 0.0123  -0.0075 450 ILE C CG1 
12841 C CG2 . ILE C 458 ? 0.1422 0.1347 0.1255 -0.0059 0.0176  -0.0054 450 ILE C CG2 
12842 C CD1 . ILE C 458 ? 0.2533 0.2444 0.2362 0.0009  0.0108  -0.0074 450 ILE C CD1 
12843 N N   . ASN C 459 ? 0.1681 0.1416 0.1493 -0.0068 0.0166  -0.0054 451 ASN C N   
12844 C CA  . ASN C 459 ? 0.2045 0.1724 0.1855 -0.0062 0.0167  -0.0059 451 ASN C CA  
12845 C C   . ASN C 459 ? 0.1441 0.1110 0.1251 -0.0018 0.0150  -0.0049 451 ASN C C   
12846 O O   . ASN C 459 ? 0.1855 0.1469 0.1655 -0.0002 0.0159  -0.0038 451 ASN C O   
12847 C CB  . ASN C 459 ? 0.1736 0.1339 0.1520 -0.0085 0.0197  -0.0050 451 ASN C CB  
12848 C CG  . ASN C 459 ? 0.2207 0.1769 0.1955 -0.0068 0.0209  -0.0018 451 ASN C CG  
12849 O OD1 . ASN C 459 ? 0.2006 0.1603 0.1747 -0.0042 0.0195  -0.0004 451 ASN C OD1 
12850 N ND2 . ASN C 459 ? 0.1878 0.1359 0.1597 -0.0086 0.0235  -0.0006 451 ASN C ND2 
12851 N N   . PRO C 460 ? 0.1316 0.1037 0.1140 0.0001  0.0123  -0.0055 452 PRO C N   
12852 C CA  . PRO C 460 ? 0.1348 0.1069 0.1182 0.0032  0.0104  -0.0051 452 PRO C CA  
12853 C C   . PRO C 460 ? 0.1298 0.1009 0.1157 0.0025  0.0109  -0.0067 452 PRO C C   
12854 O O   . PRO C 460 ? 0.1587 0.1299 0.1449 -0.0004 0.0118  -0.0085 452 PRO C O   
12855 C CB  . PRO C 460 ? 0.1850 0.1623 0.1689 0.0041  0.0076  -0.0058 452 PRO C CB  
12856 C CG  . PRO C 460 ? 0.1885 0.1686 0.1733 0.0015  0.0080  -0.0075 452 PRO C CG  
12857 C CD  . PRO C 460 ? 0.1523 0.1303 0.1360 -0.0008 0.0108  -0.0069 452 PRO C CD  
12858 N N   . VAL C 461 ? 0.1268 0.0972 0.1142 0.0053  0.0104  -0.0060 453 VAL C N   
12859 C CA  . VAL C 461 ? 0.1288 0.0983 0.1185 0.0051  0.0117  -0.0075 453 VAL C CA  
12860 C C   . VAL C 461 ? 0.1536 0.1287 0.1463 0.0059  0.0093  -0.0081 453 VAL C C   
12861 O O   . VAL C 461 ? 0.1495 0.1270 0.1439 0.0085  0.0074  -0.0068 453 VAL C O   
12862 C CB  . VAL C 461 ? 0.1167 0.0811 0.1068 0.0078  0.0138  -0.0064 453 VAL C CB  
12863 C CG1 . VAL C 461 ? 0.1510 0.1147 0.1432 0.0076  0.0158  -0.0086 453 VAL C CG1 
12864 C CG2 . VAL C 461 ? 0.1904 0.1480 0.1767 0.0064  0.0161  -0.0056 453 VAL C CG2 
12865 N N   . PHE C 462 ? 0.1444 0.1215 0.1375 0.0033  0.0091  -0.0100 454 PHE C N   
12866 C CA  . PHE C 462 ? 0.1419 0.1233 0.1370 0.0031  0.0071  -0.0105 454 PHE C CA  
12867 C C   . PHE C 462 ? 0.1647 0.1465 0.1624 0.0033  0.0092  -0.0114 454 PHE C C   
12868 O O   . PHE C 462 ? 0.1585 0.1377 0.1549 0.0014  0.0117  -0.0130 454 PHE C O   
12869 C CB  . PHE C 462 ? 0.1141 0.0967 0.1074 0.0003  0.0057  -0.0116 454 PHE C CB  
12870 C CG  . PHE C 462 ? 0.1493 0.1323 0.1408 0.0006  0.0040  -0.0110 454 PHE C CG  
12871 C CD1 . PHE C 462 ? 0.2090 0.1938 0.2002 0.0023  0.0015  -0.0103 454 PHE C CD1 
12872 C CD2 . PHE C 462 ? 0.1536 0.1355 0.1435 -0.0009 0.0052  -0.0114 454 PHE C CD2 
12873 C CE1 . PHE C 462 ? 0.1987 0.1837 0.1878 0.0029  0.0006  -0.0101 454 PHE C CE1 
12874 C CE2 . PHE C 462 ? 0.1374 0.1208 0.1263 -0.0004 0.0042  -0.0109 454 PHE C CE2 
12875 C CZ  . PHE C 462 ? 0.1593 0.1440 0.1476 0.0018  0.0022  -0.0104 454 PHE C CZ  
12876 N N   . VAL C 463 ? 0.1570 0.1424 0.1585 0.0055  0.0083  -0.0105 455 VAL C N   
12877 C CA  . VAL C 463 ? 0.1734 0.1607 0.1787 0.0064  0.0107  -0.0113 455 VAL C CA  
12878 C C   . VAL C 463 ? 0.1234 0.1157 0.1306 0.0040  0.0096  -0.0120 455 VAL C C   
12879 O O   . VAL C 463 ? 0.1271 0.1224 0.1348 0.0034  0.0063  -0.0112 455 VAL C O   
12880 C CB  . VAL C 463 ? 0.1572 0.1460 0.1666 0.0109  0.0105  -0.0095 455 VAL C CB  
12881 C CG1 . VAL C 463 ? 0.1377 0.1303 0.1524 0.0124  0.0129  -0.0103 455 VAL C CG1 
12882 C CG2 . VAL C 463 ? 0.1575 0.1395 0.1639 0.0129  0.0121  -0.0086 455 VAL C CG2 
12883 N N   . PHE C 464 ? 0.1266 0.1192 0.1342 0.0024  0.0126  -0.0136 456 PHE C N   
12884 C CA  . PHE C 464 ? 0.1072 0.1041 0.1160 -0.0004 0.0123  -0.0141 456 PHE C CA  
12885 C C   . PHE C 464 ? 0.1072 0.1077 0.1205 0.0006  0.0160  -0.0150 456 PHE C C   
12886 O O   . PHE C 464 ? 0.1771 0.1742 0.1892 0.0016  0.0197  -0.0165 456 PHE C O   
12887 C CB  . PHE C 464 ? 0.1292 0.1227 0.1322 -0.0043 0.0121  -0.0151 456 PHE C CB  
12888 C CG  . PHE C 464 ? 0.1282 0.1193 0.1279 -0.0048 0.0086  -0.0143 456 PHE C CG  
12889 C CD1 . PHE C 464 ? 0.1209 0.1139 0.1211 -0.0050 0.0051  -0.0132 456 PHE C CD1 
12890 C CD2 . PHE C 464 ? 0.1577 0.1447 0.1539 -0.0050 0.0091  -0.0148 456 PHE C CD2 
12891 C CE1 . PHE C 464 ? 0.1511 0.1419 0.1484 -0.0048 0.0025  -0.0128 456 PHE C CE1 
12892 C CE2 . PHE C 464 ? 0.1482 0.1342 0.1423 -0.0050 0.0063  -0.0141 456 PHE C CE2 
12893 C CZ  . PHE C 464 ? 0.1365 0.1243 0.1310 -0.0046 0.0032  -0.0131 456 PHE C CZ  
12894 N N   . THR C 465 ? 0.1022 0.1097 0.1207 0.0001  0.0151  -0.0144 457 THR C N   
12895 C CA  . THR C 465 ? 0.1462 0.1594 0.1700 0.0006  0.0187  -0.0152 457 THR C CA  
12896 C C   . THR C 465 ? 0.1469 0.1628 0.1693 -0.0045 0.0191  -0.0156 457 THR C C   
12897 O O   . THR C 465 ? 0.1621 0.1747 0.1794 -0.0078 0.0162  -0.0151 457 THR C O   
12898 C CB  . THR C 465 ? 0.1603 0.1810 0.1927 0.0043  0.0174  -0.0138 457 THR C CB  
12899 O OG1 . THR C 465 ? 0.1610 0.1861 0.1950 0.0020  0.0129  -0.0124 457 THR C OG1 
12900 C CG2 . THR C 465 ? 0.1908 0.2075 0.2232 0.0093  0.0166  -0.0127 457 THR C CG2 
12901 N N   . HIS C 466 ? 0.1032 0.1248 0.1299 -0.0051 0.0229  -0.0165 458 HIS C N   
12902 C CA  . HIS C 466 ? 0.1212 0.1455 0.1463 -0.0104 0.0239  -0.0166 458 HIS C CA  
12903 C C   . HIS C 466 ? 0.1720 0.1881 0.1870 -0.0139 0.0241  -0.0174 458 HIS C C   
12904 O O   . HIS C 466 ? 0.1563 0.1698 0.1669 -0.0174 0.0209  -0.0163 458 HIS C O   
12905 C CB  . HIS C 466 ? 0.1404 0.1692 0.1685 -0.0129 0.0194  -0.0148 458 HIS C CB  
12906 C CG  . HIS C 466 ? 0.2440 0.2827 0.2824 -0.0105 0.0188  -0.0140 458 HIS C CG  
12907 N ND1 . HIS C 466 ? 0.2615 0.3013 0.3040 -0.0052 0.0170  -0.0133 458 HIS C ND1 
12908 C CD2 . HIS C 466 ? 0.2965 0.3448 0.3419 -0.0129 0.0195  -0.0135 458 HIS C CD2 
12909 C CE1 . HIS C 466 ? 0.2835 0.3336 0.3354 -0.0039 0.0164  -0.0125 458 HIS C CE1 
12910 N NE2 . HIS C 466 ? 0.2078 0.2637 0.2621 -0.0087 0.0179  -0.0127 458 HIS C NE2 
12911 N N   . ASP C 467 ? 0.1568 0.1685 0.1680 -0.0128 0.0279  -0.0194 459 ASP C N   
12912 C CA  . ASP C 467 ? 0.1260 0.1298 0.1280 -0.0152 0.0271  -0.0201 459 ASP C CA  
12913 C C   . ASP C 467 ? 0.1634 0.1660 0.1590 -0.0201 0.0291  -0.0206 459 ASP C C   
12914 O O   . ASP C 467 ? 0.1576 0.1543 0.1454 -0.0223 0.0279  -0.0210 459 ASP C O   
12915 C CB  . ASP C 467 ? 0.1549 0.1535 0.1548 -0.0123 0.0295  -0.0220 459 ASP C CB  
12916 C CG  . ASP C 467 ? 0.2190 0.2177 0.2183 -0.0120 0.0355  -0.0246 459 ASP C CG  
12917 O OD1 . ASP C 467 ? 0.2252 0.2308 0.2303 -0.0113 0.0384  -0.0247 459 ASP C OD1 
12918 O OD2 . ASP C 467 ? 0.2174 0.2096 0.2104 -0.0126 0.0375  -0.0267 459 ASP C OD2 
12919 N N   . SER C 468 ? 0.1378 0.1462 0.1365 -0.0220 0.0320  -0.0206 460 SER C N   
12920 C CA  . SER C 468 ? 0.1488 0.1554 0.1401 -0.0268 0.0345  -0.0211 460 SER C CA  
12921 C C   . SER C 468 ? 0.1629 0.1768 0.1586 -0.0298 0.0363  -0.0199 460 SER C C   
12922 O O   . SER C 468 ? 0.1670 0.1874 0.1714 -0.0285 0.0350  -0.0188 460 SER C O   
12923 C CB  . SER C 468 ? 0.1441 0.1480 0.1313 -0.0261 0.0400  -0.0242 460 SER C CB  
12924 O OG  . SER C 468 ? 0.1614 0.1723 0.1558 -0.0241 0.0453  -0.0255 460 SER C OG  
12925 N N   . ILE C 469 ? 0.1585 0.1714 0.1477 -0.0344 0.0394  -0.0201 461 ILE C N   
12926 C CA  . ILE C 469 ? 0.1826 0.2025 0.1751 -0.0381 0.0424  -0.0192 461 ILE C CA  
12927 C C   . ILE C 469 ? 0.1854 0.2151 0.1892 -0.0344 0.0469  -0.0208 461 ILE C C   
12928 O O   . ILE C 469 ? 0.2188 0.2572 0.2296 -0.0365 0.0484  -0.0198 461 ILE C O   
12929 C CB  . ILE C 469 ? 0.2087 0.2251 0.1909 -0.0432 0.0460  -0.0195 461 ILE C CB  
12930 C CG1 . ILE C 469 ? 0.1755 0.1883 0.1525 -0.0409 0.0504  -0.0230 461 ILE C CG1 
12931 C CG2 . ILE C 469 ? 0.1493 0.1575 0.1217 -0.0471 0.0407  -0.0169 461 ILE C CG2 
12932 C CD1 . ILE C 469 ? 0.1853 0.1967 0.1530 -0.0456 0.0557  -0.0240 461 ILE C CD1 
12933 N N   . GLY C 470 ? 0.2039 0.2325 0.2100 -0.0289 0.0490  -0.0231 462 GLY C N   
12934 C CA  . GLY C 470 ? 0.2463 0.2837 0.2636 -0.0242 0.0529  -0.0244 462 GLY C CA  
12935 C C   . GLY C 470 ? 0.2112 0.2567 0.2397 -0.0221 0.0488  -0.0222 462 GLY C C   
12936 O O   . GLY C 470 ? 0.2264 0.2812 0.2654 -0.0185 0.0515  -0.0228 462 GLY C O   
12937 N N   . LEU C 471 ? 0.1616 0.2038 0.1882 -0.0240 0.0423  -0.0199 463 LEU C N   
12938 C CA  . LEU C 471 ? 0.1683 0.2182 0.2044 -0.0230 0.0384  -0.0181 463 LEU C CA  
12939 C C   . LEU C 471 ? 0.2475 0.3071 0.2893 -0.0279 0.0400  -0.0171 463 LEU C C   
12940 O O   . LEU C 471 ? 0.2216 0.2907 0.2735 -0.0270 0.0381  -0.0161 463 LEU C O   
12941 C CB  . LEU C 471 ? 0.2163 0.2595 0.2482 -0.0237 0.0314  -0.0163 463 LEU C CB  
12942 C CG  . LEU C 471 ? 0.1959 0.2325 0.2192 -0.0295 0.0282  -0.0148 463 LEU C CG  
12943 C CD1 . LEU C 471 ? 0.1752 0.2177 0.2023 -0.0347 0.0266  -0.0131 463 LEU C CD1 
12944 C CD2 . LEU C 471 ? 0.1626 0.1907 0.1806 -0.0276 0.0227  -0.0141 463 LEU C CD2 
12945 N N   . GLY C 472 ? 0.2020 0.2595 0.2371 -0.0335 0.0432  -0.0171 464 GLY C N   
12946 C CA  . GLY C 472 ? 0.1630 0.2306 0.2037 -0.0382 0.0467  -0.0165 464 GLY C CA  
12947 C C   . GLY C 472 ? 0.1823 0.2497 0.2219 -0.0446 0.0420  -0.0139 464 GLY C C   
12948 O O   . GLY C 472 ? 0.2034 0.2602 0.2324 -0.0481 0.0390  -0.0126 464 GLY C O   
12949 N N   . GLU C 473 ? 0.1483 0.2274 0.1992 -0.0460 0.0412  -0.0130 465 GLU C N   
12950 C CA  . GLU C 473 ? 0.1764 0.2575 0.2274 -0.0537 0.0389  -0.0109 465 GLU C CA  
12951 C C   . GLU C 473 ? 0.2188 0.2893 0.2628 -0.0557 0.0315  -0.0093 465 GLU C C   
12952 O O   . GLU C 473 ? 0.2609 0.3274 0.3000 -0.0625 0.0299  -0.0076 465 GLU C O   
12953 C CB  . GLU C 473 ? 0.1450 0.2426 0.2110 -0.0544 0.0395  -0.0107 465 GLU C CB  
12954 C CG  . GLU C 473 ? 0.1499 0.2594 0.2227 -0.0556 0.0475  -0.0117 465 GLU C CG  
12955 C CD  . GLU C 473 ? 0.1923 0.3085 0.2728 -0.0469 0.0518  -0.0140 465 GLU C CD  
12956 O OE1 . GLU C 473 ? 0.1974 0.3062 0.2751 -0.0403 0.0491  -0.0149 465 GLU C OE1 
12957 O OE2 . GLU C 473 ? 0.1561 0.2848 0.2454 -0.0467 0.0580  -0.0150 465 GLU C OE2 
12958 N N   . ASP C 474 ? 0.1507 0.2160 0.1938 -0.0499 0.0271  -0.0098 466 ASP C N   
12959 C CA  . ASP C 474 ? 0.1854 0.2410 0.2221 -0.0514 0.0204  -0.0086 466 ASP C CA  
12960 C C   . ASP C 474 ? 0.2239 0.2666 0.2474 -0.0551 0.0200  -0.0076 466 ASP C C   
12961 O O   . ASP C 474 ? 0.2597 0.2951 0.2780 -0.0586 0.0156  -0.0063 466 ASP C O   
12962 C CB  . ASP C 474 ? 0.1819 0.2345 0.2194 -0.0443 0.0167  -0.0094 466 ASP C CB  
12963 C CG  . ASP C 474 ? 0.2828 0.3453 0.3309 -0.0421 0.0137  -0.0093 466 ASP C CG  
12964 O OD1 . ASP C 474 ? 0.2225 0.2944 0.2778 -0.0464 0.0137  -0.0087 466 ASP C OD1 
12965 O OD2 . ASP C 474 ? 0.2658 0.3267 0.3148 -0.0363 0.0112  -0.0097 466 ASP C OD2 
12966 N N   . GLY C 475 ? 0.2008 0.2399 0.2184 -0.0544 0.0243  -0.0083 467 GLY C N   
12967 C CA  . GLY C 475 ? 0.1370 0.1665 0.1430 -0.0591 0.0246  -0.0068 467 GLY C CA  
12968 C C   . GLY C 475 ? 0.1744 0.1915 0.1706 -0.0565 0.0206  -0.0065 467 GLY C C   
12969 O O   . GLY C 475 ? 0.1504 0.1662 0.1481 -0.0508 0.0184  -0.0077 467 GLY C O   
12970 N N   . PRO C 476 ? 0.1449 0.1528 0.1307 -0.0607 0.0194  -0.0045 468 PRO C N   
12971 C CA  . PRO C 476 ? 0.1462 0.1437 0.1226 -0.0582 0.0165  -0.0042 468 PRO C CA  
12972 C C   . PRO C 476 ? 0.1416 0.1341 0.1185 -0.0541 0.0106  -0.0042 468 PRO C C   
12973 O O   . PRO C 476 ? 0.1467 0.1337 0.1188 -0.0507 0.0087  -0.0045 468 PRO C O   
12974 C CB  . PRO C 476 ? 0.1660 0.1558 0.1322 -0.0640 0.0163  -0.0015 468 PRO C CB  
12975 C CG  . PRO C 476 ? 0.2028 0.1967 0.1732 -0.0696 0.0173  -0.0002 468 PRO C CG  
12976 C CD  . PRO C 476 ? 0.1537 0.1611 0.1359 -0.0680 0.0215  -0.0025 468 PRO C CD  
12977 N N   . THR C 477 ? 0.1400 0.1340 0.1218 -0.0549 0.0077  -0.0039 469 THR C N   
12978 C CA  . THR C 477 ? 0.1968 0.1860 0.1783 -0.0508 0.0027  -0.0043 469 THR C CA  
12979 C C   . THR C 477 ? 0.2042 0.1990 0.1919 -0.0447 0.0032  -0.0063 469 THR C C   
12980 O O   . THR C 477 ? 0.1838 0.1743 0.1698 -0.0407 0.0001  -0.0067 469 THR C O   
12981 C CB  . THR C 477 ? 0.1741 0.1628 0.1582 -0.0535 -0.0006 -0.0038 469 THR C CB  
12982 O OG1 . THR C 477 ? 0.1969 0.1971 0.1911 -0.0538 0.0010  -0.0049 469 THR C OG1 
12983 C CG2 . THR C 477 ? 0.2236 0.2058 0.2014 -0.0601 -0.0010 -0.0016 469 THR C CG2 
12984 N N   . HIS C 478 ? 0.1396 0.1438 0.1345 -0.0439 0.0072  -0.0075 470 HIS C N   
12985 C CA  . HIS C 478 ? 0.1172 0.1259 0.1178 -0.0382 0.0080  -0.0091 470 HIS C CA  
12986 C C   . HIS C 478 ? 0.1378 0.1465 0.1365 -0.0361 0.0122  -0.0104 470 HIS C C   
12987 O O   . HIS C 478 ? 0.1644 0.1733 0.1650 -0.0314 0.0123  -0.0115 470 HIS C O   
12988 C CB  . HIS C 478 ? 0.1728 0.1922 0.1839 -0.0377 0.0090  -0.0095 470 HIS C CB  
12989 C CG  . HIS C 478 ? 0.2595 0.2794 0.2731 -0.0382 0.0042  -0.0089 470 HIS C CG  
12990 N ND1 . HIS C 478 ? 0.3061 0.3202 0.3148 -0.0428 0.0010  -0.0079 470 HIS C ND1 
12991 C CD2 . HIS C 478 ? 0.2674 0.2923 0.2872 -0.0349 0.0018  -0.0093 470 HIS C CD2 
12992 C CE1 . HIS C 478 ? 0.3175 0.3329 0.3292 -0.0424 -0.0030 -0.0080 470 HIS C CE1 
12993 N NE2 . HIS C 478 ? 0.2840 0.3063 0.3023 -0.0377 -0.0027 -0.0088 470 HIS C NE2 
12994 N N   . GLN C 479 ? 0.1222 0.1304 0.1167 -0.0396 0.0158  -0.0103 471 GLN C N   
12995 C CA  . GLN C 479 ? 0.1234 0.1315 0.1156 -0.0380 0.0201  -0.0120 471 GLN C CA  
12996 C C   . GLN C 479 ? 0.1676 0.1672 0.1514 -0.0369 0.0178  -0.0121 471 GLN C C   
12997 O O   . GLN C 479 ? 0.1748 0.1687 0.1510 -0.0401 0.0158  -0.0105 471 GLN C O   
12998 C CB  . GLN C 479 ? 0.1299 0.1406 0.1197 -0.0425 0.0251  -0.0120 471 GLN C CB  
12999 C CG  . GLN C 479 ? 0.1465 0.1679 0.1460 -0.0432 0.0288  -0.0125 471 GLN C CG  
13000 C CD  . GLN C 479 ? 0.1516 0.1752 0.1479 -0.0492 0.0329  -0.0117 471 GLN C CD  
13001 O OE1 . GLN C 479 ? 0.1583 0.1744 0.1448 -0.0531 0.0319  -0.0103 471 GLN C OE1 
13002 N NE2 . GLN C 479 ? 0.1457 0.1798 0.1505 -0.0499 0.0374  -0.0125 471 GLN C NE2 
13003 N N   . PRO C 480 ? 0.1208 0.1196 0.1058 -0.0326 0.0178  -0.0136 472 PRO C N   
13004 C CA  . PRO C 480 ? 0.1219 0.1141 0.1000 -0.0320 0.0156  -0.0137 472 PRO C CA  
13005 C C   . PRO C 480 ? 0.1421 0.1313 0.1122 -0.0353 0.0182  -0.0143 472 PRO C C   
13006 O O   . PRO C 480 ? 0.1568 0.1489 0.1272 -0.0364 0.0231  -0.0158 472 PRO C O   
13007 C CB  . PRO C 480 ? 0.1294 0.1223 0.1114 -0.0274 0.0163  -0.0155 472 PRO C CB  
13008 C CG  . PRO C 480 ? 0.1430 0.1419 0.1340 -0.0249 0.0167  -0.0153 472 PRO C CG  
13009 C CD  . PRO C 480 ? 0.1312 0.1349 0.1242 -0.0282 0.0195  -0.0150 472 PRO C CD  
13010 N N   . ILE C 481 ? 0.1463 0.1299 0.1091 -0.0366 0.0148  -0.0131 473 ILE C N   
13011 C CA  . ILE C 481 ? 0.1516 0.1318 0.1055 -0.0396 0.0159  -0.0135 473 ILE C CA  
13012 C C   . ILE C 481 ? 0.1383 0.1152 0.0892 -0.0377 0.0129  -0.0141 473 ILE C C   
13013 O O   . ILE C 481 ? 0.1818 0.1582 0.1305 -0.0376 0.0151  -0.0165 473 ILE C O   
13014 C CB  . ILE C 481 ? 0.1836 0.1603 0.1307 -0.0438 0.0141  -0.0106 473 ILE C CB  
13015 C CG1 . ILE C 481 ? 0.1784 0.1589 0.1288 -0.0465 0.0174  -0.0099 473 ILE C CG1 
13016 C CG2 . ILE C 481 ? 0.2616 0.2343 0.1982 -0.0467 0.0145  -0.0107 473 ILE C CG2 
13017 C CD1 . ILE C 481 ? 0.1578 0.1425 0.1081 -0.0482 0.0241  -0.0121 473 ILE C CD1 
13018 N N   . GLU C 482 ? 0.1555 0.1305 0.1067 -0.0363 0.0078  -0.0122 474 GLU C N   
13019 C CA  . GLU C 482 ? 0.1353 0.1084 0.0840 -0.0349 0.0045  -0.0124 474 GLU C CA  
13020 C C   . GLU C 482 ? 0.1681 0.1433 0.1237 -0.0309 0.0037  -0.0135 474 GLU C C   
13021 O O   . GLU C 482 ? 0.1716 0.1466 0.1265 -0.0301 0.0018  -0.0140 474 GLU C O   
13022 C CB  . GLU C 482 ? 0.2208 0.1904 0.1650 -0.0355 -0.0006 -0.0094 474 GLU C CB  
13023 C CG  . GLU C 482 ? 0.1351 0.1039 0.0837 -0.0330 -0.0036 -0.0077 474 GLU C CG  
13024 C CD  . GLU C 482 ? 0.1855 0.1530 0.1340 -0.0353 -0.0026 -0.0063 474 GLU C CD  
13025 O OE1 . GLU C 482 ? 0.1432 0.1134 0.0928 -0.0377 0.0017  -0.0072 474 GLU C OE1 
13026 O OE2 . GLU C 482 ? 0.1876 0.1513 0.1351 -0.0349 -0.0059 -0.0043 474 GLU C OE2 
13027 N N   . GLN C 483 ? 0.1663 0.1441 0.1286 -0.0288 0.0052  -0.0138 475 GLN C N   
13028 C CA  . GLN C 483 ? 0.1471 0.1263 0.1149 -0.0251 0.0038  -0.0141 475 GLN C CA  
13029 C C   . GLN C 483 ? 0.1192 0.0985 0.0874 -0.0242 0.0057  -0.0161 475 GLN C C   
13030 O O   . GLN C 483 ? 0.1615 0.1408 0.1307 -0.0227 0.0036  -0.0160 475 GLN C O   
13031 C CB  . GLN C 483 ? 0.1746 0.1566 0.1486 -0.0233 0.0049  -0.0139 475 GLN C CB  
13032 C CG  . GLN C 483 ? 0.1668 0.1480 0.1410 -0.0238 0.0018  -0.0120 475 GLN C CG  
13033 C CD  . GLN C 483 ? 0.2037 0.1833 0.1733 -0.0279 0.0023  -0.0109 475 GLN C CD  
13034 O OE1 . GLN C 483 ? 0.1631 0.1445 0.1321 -0.0300 0.0061  -0.0117 475 GLN C OE1 
13035 N NE2 . GLN C 483 ? 0.1685 0.1442 0.1345 -0.0288 -0.0012 -0.0091 475 GLN C NE2 
13036 N N   . THR C 484 ? 0.1194 0.0986 0.0870 -0.0251 0.0099  -0.0180 476 THR C N   
13037 C CA  . THR C 484 ? 0.1738 0.1514 0.1411 -0.0246 0.0118  -0.0201 476 THR C CA  
13038 C C   . THR C 484 ? 0.1873 0.1632 0.1493 -0.0270 0.0092  -0.0203 476 THR C C   
13039 O O   . THR C 484 ? 0.1657 0.1415 0.1290 -0.0263 0.0081  -0.0208 476 THR C O   
13040 C CB  . THR C 484 ? 0.1594 0.1360 0.1257 -0.0252 0.0169  -0.0224 476 THR C CB  
13041 O OG1 . THR C 484 ? 0.1901 0.1698 0.1630 -0.0223 0.0190  -0.0220 476 THR C OG1 
13042 C CG2 . THR C 484 ? 0.2100 0.1831 0.1747 -0.0250 0.0189  -0.0247 476 THR C CG2 
13043 N N   . ALA C 485 ? 0.1687 0.1437 0.1247 -0.0300 0.0079  -0.0197 477 ALA C N   
13044 C CA  . ALA C 485 ? 0.1786 0.1529 0.1298 -0.0322 0.0047  -0.0196 477 ALA C CA  
13045 C C   . ALA C 485 ? 0.1922 0.1688 0.1472 -0.0298 0.0002  -0.0177 477 ALA C C   
13046 O O   . ALA C 485 ? 0.1563 0.1343 0.1113 -0.0304 -0.0017 -0.0182 477 ALA C O   
13047 C CB  . ALA C 485 ? 0.1543 0.1269 0.0978 -0.0355 0.0037  -0.0187 477 ALA C CB  
13048 N N   . THR C 486 ? 0.1534 0.1307 0.1116 -0.0274 -0.0014 -0.0157 478 THR C N   
13049 C CA  . THR C 486 ? 0.1791 0.1583 0.1408 -0.0247 -0.0052 -0.0142 478 THR C CA  
13050 C C   . THR C 486 ? 0.1468 0.1282 0.1140 -0.0224 -0.0039 -0.0153 478 THR C C   
13051 O O   . THR C 486 ? 0.1193 0.1031 0.0886 -0.0213 -0.0060 -0.0150 478 THR C O   
13052 C CB  . THR C 486 ? 0.1375 0.1154 0.1000 -0.0228 -0.0071 -0.0122 478 THR C CB  
13053 O OG1 . THR C 486 ? 0.1436 0.1219 0.1101 -0.0216 -0.0046 -0.0127 478 THR C OG1 
13054 C CG2 . THR C 486 ? 0.1835 0.1585 0.1398 -0.0255 -0.0084 -0.0106 478 THR C CG2 
13055 N N   . LEU C 487 ? 0.1599 0.1406 0.1297 -0.0215 -0.0004 -0.0164 479 LEU C N   
13056 C CA  . LEU C 487 ? 0.1144 0.0960 0.0884 -0.0195 0.0010  -0.0170 479 LEU C CA  
13057 C C   . LEU C 487 ? 0.1530 0.1344 0.1256 -0.0217 0.0017  -0.0185 479 LEU C C   
13058 O O   . LEU C 487 ? 0.1427 0.1258 0.1182 -0.0208 0.0014  -0.0184 479 LEU C O   
13059 C CB  . LEU C 487 ? 0.1437 0.1242 0.1202 -0.0180 0.0043  -0.0175 479 LEU C CB  
13060 C CG  . LEU C 487 ? 0.1455 0.1272 0.1247 -0.0159 0.0034  -0.0162 479 LEU C CG  
13061 C CD1 . LEU C 487 ? 0.1259 0.1078 0.1080 -0.0147 0.0066  -0.0167 479 LEU C CD1 
13062 C CD2 . LEU C 487 ? 0.1880 0.1710 0.1697 -0.0132 0.0010  -0.0151 479 LEU C CD2 
13063 N N   . ARG C 488 ? 0.1275 0.1069 0.0953 -0.0250 0.0028  -0.0199 480 ARG C N   
13064 C CA  . ARG C 488 ? 0.1594 0.1381 0.1251 -0.0280 0.0032  -0.0216 480 ARG C CA  
13065 C C   . ARG C 488 ? 0.1989 0.1821 0.1655 -0.0289 -0.0009 -0.0206 480 ARG C C   
13066 O O   . ARG C 488 ? 0.1474 0.1315 0.1140 -0.0313 -0.0010 -0.0218 480 ARG C O   
13067 C CB  . ARG C 488 ? 0.1548 0.1300 0.1139 -0.0316 0.0050  -0.0237 480 ARG C CB  
13068 C CG  . ARG C 488 ? 0.2046 0.1756 0.1633 -0.0307 0.0100  -0.0255 480 ARG C CG  
13069 C CD  . ARG C 488 ? 0.1552 0.1231 0.1068 -0.0339 0.0122  -0.0275 480 ARG C CD  
13070 N NE  . ARG C 488 ? 0.2057 0.1699 0.1575 -0.0325 0.0175  -0.0296 480 ARG C NE  
13071 C CZ  . ARG C 488 ? 0.1761 0.1394 0.1251 -0.0329 0.0205  -0.0306 480 ARG C CZ  
13072 N NH1 . ARG C 488 ? 0.1988 0.1640 0.1437 -0.0351 0.0189  -0.0295 480 ARG C NH1 
13073 N NH2 . ARG C 488 ? 0.1827 0.1433 0.1330 -0.0309 0.0255  -0.0326 480 ARG C NH2 
13074 N N   . LEU C 489 ? 0.1846 0.1705 0.1521 -0.0270 -0.0044 -0.0185 481 LEU C N   
13075 C CA  . LEU C 489 ? 0.1474 0.1381 0.1163 -0.0270 -0.0084 -0.0175 481 LEU C CA  
13076 C C   . LEU C 489 ? 0.1444 0.1391 0.1199 -0.0238 -0.0088 -0.0167 481 LEU C C   
13077 O O   . LEU C 489 ? 0.1806 0.1808 0.1589 -0.0234 -0.0117 -0.0159 481 LEU C O   
13078 C CB  . LEU C 489 ? 0.1185 0.1093 0.0844 -0.0263 -0.0121 -0.0155 481 LEU C CB  
13079 C CG  . LEU C 489 ? 0.1688 0.1560 0.1270 -0.0300 -0.0119 -0.0160 481 LEU C CG  
13080 C CD1 . LEU C 489 ? 0.2287 0.2152 0.1833 -0.0293 -0.0158 -0.0134 481 LEU C CD1 
13081 C CD2 . LEU C 489 ? 0.1811 0.1693 0.1362 -0.0343 -0.0120 -0.0180 481 LEU C CD2 
13082 N N   . ILE C 490 ? 0.1126 0.1054 0.0906 -0.0214 -0.0060 -0.0167 482 ILE C N   
13083 C CA  . ILE C 490 ? 0.1571 0.1533 0.1402 -0.0187 -0.0059 -0.0161 482 ILE C CA  
13084 C C   . ILE C 490 ? 0.1434 0.1421 0.1282 -0.0215 -0.0046 -0.0171 482 ILE C C   
13085 O O   . ILE C 490 ? 0.1200 0.1147 0.1028 -0.0240 -0.0017 -0.0185 482 ILE C O   
13086 C CB  . ILE C 490 ? 0.1402 0.1334 0.1245 -0.0158 -0.0036 -0.0158 482 ILE C CB  
13087 C CG1 . ILE C 490 ? 0.1075 0.0983 0.0901 -0.0140 -0.0049 -0.0149 482 ILE C CG1 
13088 C CG2 . ILE C 490 ? 0.1491 0.1457 0.1373 -0.0132 -0.0033 -0.0151 482 ILE C CG2 
13089 C CD1 . ILE C 490 ? 0.1928 0.1813 0.1765 -0.0118 -0.0031 -0.0147 482 ILE C CD1 
13090 N N   . PRO C 491 ? 0.1612 0.1664 0.1498 -0.0213 -0.0064 -0.0166 483 PRO C N   
13091 C CA  . PRO C 491 ? 0.2104 0.2186 0.2012 -0.0247 -0.0050 -0.0175 483 PRO C CA  
13092 C C   . PRO C 491 ? 0.1734 0.1781 0.1651 -0.0239 -0.0010 -0.0175 483 PRO C C   
13093 O O   . PRO C 491 ? 0.1852 0.1889 0.1778 -0.0199 -0.0003 -0.0165 483 PRO C O   
13094 C CB  . PRO C 491 ? 0.1451 0.1626 0.1413 -0.0235 -0.0077 -0.0166 483 PRO C CB  
13095 C CG  . PRO C 491 ? 0.1427 0.1607 0.1376 -0.0205 -0.0115 -0.0155 483 PRO C CG  
13096 C CD  . PRO C 491 ? 0.1467 0.1571 0.1381 -0.0181 -0.0099 -0.0153 483 PRO C CD  
13097 N N   . ASN C 492 ? 0.1628 0.1647 0.1532 -0.0279 0.0014  -0.0187 484 ASN C N   
13098 C CA  . ASN C 492 ? 0.1801 0.1777 0.1706 -0.0277 0.0051  -0.0183 484 ASN C CA  
13099 C C   . ASN C 492 ? 0.1917 0.1825 0.1797 -0.0242 0.0067  -0.0179 484 ASN C C   
13100 O O   . ASN C 492 ? 0.1574 0.1467 0.1462 -0.0215 0.0084  -0.0166 484 ASN C O   
13101 C CB  . ASN C 492 ? 0.1514 0.1550 0.1463 -0.0260 0.0055  -0.0169 484 ASN C CB  
13102 C CG  . ASN C 492 ? 0.2063 0.2058 0.2005 -0.0276 0.0092  -0.0163 484 ASN C CG  
13103 O OD1 . ASN C 492 ? 0.1953 0.1902 0.1872 -0.0318 0.0109  -0.0174 484 ASN C OD1 
13104 N ND2 . ASN C 492 ? 0.1402 0.1405 0.1355 -0.0242 0.0106  -0.0147 484 ASN C ND2 
13105 N N   . MET C 493 ? 0.1938 0.1809 0.1786 -0.0243 0.0064  -0.0189 485 MET C N   
13106 C CA  . MET C 493 ? 0.1934 0.1756 0.1770 -0.0213 0.0080  -0.0186 485 MET C CA  
13107 C C   . MET C 493 ? 0.2353 0.2113 0.2151 -0.0235 0.0103  -0.0205 485 MET C C   
13108 O O   . MET C 493 ? 0.2390 0.2150 0.2160 -0.0267 0.0094  -0.0220 485 MET C O   
13109 C CB  . MET C 493 ? 0.2020 0.1867 0.1860 -0.0185 0.0055  -0.0178 485 MET C CB  
13110 C CG  . MET C 493 ? 0.2144 0.1953 0.1976 -0.0163 0.0069  -0.0177 485 MET C CG  
13111 S SD  . MET C 493 ? 0.1906 0.1703 0.1762 -0.0123 0.0082  -0.0161 485 MET C SD  
13112 C CE  . MET C 493 ? 0.1463 0.1308 0.1337 -0.0096 0.0048  -0.0148 485 MET C CE  
13113 N N   . ASP C 494 ? 0.1935 0.1638 0.1727 -0.0217 0.0132  -0.0204 486 ASP C N   
13114 C CA  . ASP C 494 ? 0.2089 0.1728 0.1849 -0.0226 0.0160  -0.0224 486 ASP C CA  
13115 C C   . ASP C 494 ? 0.2576 0.2223 0.2345 -0.0193 0.0162  -0.0221 486 ASP C C   
13116 O O   . ASP C 494 ? 0.2206 0.1869 0.2006 -0.0156 0.0159  -0.0203 486 ASP C O   
13117 C CB  . ASP C 494 ? 0.2388 0.1957 0.2140 -0.0219 0.0193  -0.0223 486 ASP C CB  
13118 C CG  . ASP C 494 ? 0.2533 0.2073 0.2261 -0.0267 0.0200  -0.0234 486 ASP C CG  
13119 O OD1 . ASP C 494 ? 0.2026 0.1609 0.1749 -0.0306 0.0178  -0.0245 486 ASP C OD1 
13120 O OD2 . ASP C 494 ? 0.2573 0.2047 0.2290 -0.0267 0.0225  -0.0231 486 ASP C OD2 
13121 N N   . VAL C 495 ? 0.1613 0.1252 0.1351 -0.0212 0.0168  -0.0240 487 VAL C N   
13122 C CA  . VAL C 495 ? 0.1507 0.1156 0.1253 -0.0189 0.0177  -0.0239 487 VAL C CA  
13123 C C   . VAL C 495 ? 0.1946 0.1537 0.1670 -0.0187 0.0220  -0.0262 487 VAL C C   
13124 O O   . VAL C 495 ? 0.1888 0.1440 0.1563 -0.0221 0.0235  -0.0287 487 VAL C O   
13125 C CB  . VAL C 495 ? 0.1448 0.1133 0.1172 -0.0211 0.0153  -0.0240 487 VAL C CB  
13126 C CG1 . VAL C 495 ? 0.1673 0.1369 0.1404 -0.0197 0.0169  -0.0240 487 VAL C CG1 
13127 C CG2 . VAL C 495 ? 0.1889 0.1624 0.1636 -0.0205 0.0111  -0.0218 487 VAL C CG2 
13128 N N   . TRP C 496 ? 0.1391 0.0977 0.1152 -0.0145 0.0240  -0.0255 488 TRP C N   
13129 C CA  . TRP C 496 ? 0.1789 0.1324 0.1541 -0.0128 0.0284  -0.0275 488 TRP C CA  
13130 C C   . TRP C 496 ? 0.1855 0.1436 0.1636 -0.0107 0.0298  -0.0276 488 TRP C C   
13131 O O   . TRP C 496 ? 0.1615 0.1256 0.1445 -0.0086 0.0277  -0.0253 488 TRP C O   
13132 C CB  . TRP C 496 ? 0.1972 0.1464 0.1751 -0.0088 0.0299  -0.0262 488 TRP C CB  
13133 C CG  . TRP C 496 ? 0.1755 0.1185 0.1502 -0.0111 0.0299  -0.0263 488 TRP C CG  
13134 C CD1 . TRP C 496 ? 0.2172 0.1620 0.1928 -0.0120 0.0272  -0.0241 488 TRP C CD1 
13135 C CD2 . TRP C 496 ? 0.1699 0.1034 0.1397 -0.0129 0.0331  -0.0289 488 TRP C CD2 
13136 N NE1 . TRP C 496 ? 0.2192 0.1572 0.1914 -0.0147 0.0285  -0.0248 488 TRP C NE1 
13137 C CE2 . TRP C 496 ? 0.2301 0.1606 0.1984 -0.0156 0.0319  -0.0278 488 TRP C CE2 
13138 C CE3 . TRP C 496 ? 0.2028 0.1300 0.1690 -0.0129 0.0371  -0.0322 488 TRP C CE3 
13139 C CZ2 . TRP C 496 ? 0.2349 0.1557 0.1982 -0.0186 0.0343  -0.0298 488 TRP C CZ2 
13140 C CZ3 . TRP C 496 ? 0.2267 0.1436 0.1874 -0.0155 0.0394  -0.0344 488 TRP C CZ3 
13141 C CH2 . TRP C 496 ? 0.2660 0.1795 0.2253 -0.0185 0.0379  -0.0331 488 TRP C CH2 
13142 N N   . ARG C 497 ? 0.1552 0.1106 0.1300 -0.0117 0.0335  -0.0304 489 ARG C N   
13143 C CA  . ARG C 497 ? 0.1550 0.1150 0.1326 -0.0101 0.0359  -0.0309 489 ARG C CA  
13144 C C   . ARG C 497 ? 0.1889 0.1437 0.1661 -0.0074 0.0414  -0.0336 489 ARG C C   
13145 O O   . ARG C 497 ? 0.1936 0.1452 0.1652 -0.0097 0.0447  -0.0368 489 ARG C O   
13146 C CB  . ARG C 497 ? 0.1635 0.1264 0.1366 -0.0146 0.0351  -0.0316 489 ARG C CB  
13147 C CG  . ARG C 497 ? 0.1379 0.1072 0.1147 -0.0136 0.0370  -0.0312 489 ARG C CG  
13148 C CD  . ARG C 497 ? 0.1916 0.1629 0.1629 -0.0185 0.0357  -0.0311 489 ARG C CD  
13149 N NE  . ARG C 497 ? 0.2026 0.1800 0.1772 -0.0185 0.0375  -0.0303 489 ARG C NE  
13150 C CZ  . ARG C 497 ? 0.2119 0.1899 0.1836 -0.0199 0.0422  -0.0324 489 ARG C CZ  
13151 N NH1 . ARG C 497 ? 0.1970 0.1688 0.1615 -0.0213 0.0454  -0.0357 489 ARG C NH1 
13152 N NH2 . ARG C 497 ? 0.2228 0.2073 0.1984 -0.0203 0.0437  -0.0314 489 ARG C NH2 
13153 N N   . PRO C 498 ? 0.1634 0.1168 0.1457 -0.0022 0.0425  -0.0325 490 PRO C N   
13154 C CA  . PRO C 498 ? 0.1905 0.1370 0.1720 0.0011  0.0476  -0.0351 490 PRO C CA  
13155 C C   . PRO C 498 ? 0.1817 0.1328 0.1661 0.0033  0.0520  -0.0370 490 PRO C C   
13156 O O   . PRO C 498 ? 0.1839 0.1449 0.1745 0.0042  0.0509  -0.0352 490 PRO C O   
13157 C CB  . PRO C 498 ? 0.2271 0.1722 0.2141 0.0065  0.0464  -0.0323 490 PRO C CB  
13158 C CG  . PRO C 498 ? 0.2551 0.2102 0.2481 0.0070  0.0418  -0.0286 490 PRO C CG  
13159 C CD  . PRO C 498 ? 0.1414 0.0984 0.1296 0.0008  0.0388  -0.0288 490 PRO C CD  
13160 N N   . CYS C 499 ? 0.1955 0.1393 0.1756 0.0042  0.0572  -0.0408 491 CYS C N   
13161 C CA  . CYS C 499 ? 0.2264 0.1745 0.2086 0.0061  0.0623  -0.0431 491 CYS C CA  
13162 C C   . CYS C 499 ? 0.2882 0.2380 0.2789 0.0140  0.0656  -0.0428 491 CYS C C   
13163 O O   . CYS C 499 ? 0.2556 0.2121 0.2508 0.0163  0.0697  -0.0442 491 CYS C O   
13164 C CB  . CYS C 499 ? 0.2963 0.2364 0.2682 0.0025  0.0667  -0.0480 491 CYS C CB  
13165 S SG  . CYS C 499 ? 0.2914 0.2157 0.2577 0.0056  0.0713  -0.0519 491 CYS C SG  
13166 N N   . ASP C 500 ? 0.2170 0.1612 0.2101 0.0182  0.0641  -0.0410 492 ASP C N   
13167 C CA  . ASP C 500 ? 0.2433 0.1889 0.2445 0.0264  0.0668  -0.0403 492 ASP C CA  
13168 C C   . ASP C 500 ? 0.2214 0.1625 0.2247 0.0297  0.0627  -0.0364 492 ASP C C   
13169 O O   . ASP C 500 ? 0.2191 0.1582 0.2187 0.0255  0.0582  -0.0344 492 ASP C O   
13170 C CB  . ASP C 500 ? 0.2845 0.2212 0.2819 0.0295  0.0738  -0.0449 492 ASP C CB  
13171 C CG  . ASP C 500 ? 0.3136 0.2338 0.3002 0.0269  0.0747  -0.0474 492 ASP C CG  
13172 O OD1 . ASP C 500 ? 0.3250 0.2399 0.3094 0.0253  0.0704  -0.0447 492 ASP C OD1 
13173 O OD2 . ASP C 500 ? 0.3824 0.2948 0.3623 0.0262  0.0799  -0.0522 492 ASP C OD2 
13174 N N   . THR C 501 ? 0.2167 0.1566 0.2261 0.0375  0.0645  -0.0354 493 THR C N   
13175 C CA  . THR C 501 ? 0.2845 0.2211 0.2963 0.0412  0.0606  -0.0311 493 THR C CA  
13176 C C   . THR C 501 ? 0.2567 0.1775 0.2586 0.0385  0.0605  -0.0317 493 THR C C   
13177 O O   . THR C 501 ? 0.2328 0.1513 0.2336 0.0378  0.0563  -0.0281 493 THR C O   
13178 C CB  . THR C 501 ? 0.3672 0.3062 0.3878 0.0507  0.0625  -0.0297 493 THR C CB  
13179 O OG1 . THR C 501 ? 0.4544 0.3826 0.4714 0.0542  0.0687  -0.0336 493 THR C OG1 
13180 C CG2 . THR C 501 ? 0.2875 0.2438 0.3190 0.0527  0.0623  -0.0290 493 THR C CG2 
13181 N N   . ALA C 502 ? 0.2416 0.1515 0.2359 0.0366  0.0652  -0.0362 494 ALA C N   
13182 C CA  . ALA C 502 ? 0.2619 0.1570 0.2467 0.0329  0.0651  -0.0369 494 ALA C CA  
13183 C C   . ALA C 502 ? 0.2255 0.1237 0.2058 0.0245  0.0607  -0.0361 494 ALA C C   
13184 O O   . ALA C 502 ? 0.2291 0.1232 0.2073 0.0227  0.0574  -0.0332 494 ALA C O   
13185 C CB  . ALA C 502 ? 0.2985 0.1810 0.2755 0.0322  0.0710  -0.0425 494 ALA C CB  
13186 N N   . GLU C 503 ? 0.2093 0.1149 0.1882 0.0196  0.0606  -0.0384 495 GLU C N   
13187 C CA  . GLU C 503 ? 0.2137 0.1233 0.1893 0.0124  0.0562  -0.0374 495 GLU C CA  
13188 C C   . GLU C 503 ? 0.2055 0.1245 0.1877 0.0138  0.0511  -0.0325 495 GLU C C   
13189 O O   . GLU C 503 ? 0.2032 0.1223 0.1829 0.0096  0.0474  -0.0308 495 GLU C O   
13190 C CB  . GLU C 503 ? 0.1884 0.1042 0.1614 0.0077  0.0569  -0.0403 495 GLU C CB  
13191 C CG  . GLU C 503 ? 0.2010 0.1074 0.1653 0.0048  0.0616  -0.0456 495 GLU C CG  
13192 C CD  . GLU C 503 ? 0.2847 0.1961 0.2438 -0.0016 0.0608  -0.0477 495 GLU C CD  
13193 O OE1 . GLU C 503 ? 0.2324 0.1548 0.1957 -0.0028 0.0575  -0.0451 495 GLU C OE1 
13194 O OE2 . GLU C 503 ? 0.2872 0.1909 0.2375 -0.0055 0.0634  -0.0519 495 GLU C OE2 
13195 N N   . SER C 504 ? 0.1918 0.1189 0.1822 0.0194  0.0507  -0.0303 496 SER C N   
13196 C CA  A SER C 504 ? 0.2168 0.1521 0.2126 0.0207  0.0457  -0.0259 496 SER C CA  
13197 C CA  B SER C 504 ? 0.2174 0.1527 0.2132 0.0207  0.0457  -0.0259 496 SER C CA  
13198 C C   . SER C 504 ? 0.1685 0.0961 0.1622 0.0222  0.0439  -0.0230 496 SER C C   
13199 O O   . SER C 504 ? 0.1835 0.1135 0.1761 0.0194  0.0400  -0.0205 496 SER C O   
13200 C CB  A SER C 504 ? 0.2212 0.1667 0.2264 0.0262  0.0457  -0.0244 496 SER C CB  
13201 C CB  B SER C 504 ? 0.2218 0.1673 0.2270 0.0262  0.0457  -0.0244 496 SER C CB  
13202 O OG  A SER C 504 ? 0.2235 0.1778 0.2309 0.0237  0.0467  -0.0263 496 SER C OG  
13203 O OG  B SER C 504 ? 0.2451 0.1976 0.2547 0.0274  0.0407  -0.0204 496 SER C OG  
13204 N N   . LEU C 505 ? 0.1972 0.1152 0.1899 0.0267  0.0468  -0.0230 497 LEU C N   
13205 C CA  . LEU C 505 ? 0.1897 0.0992 0.1796 0.0281  0.0454  -0.0199 497 LEU C CA  
13206 C C   . LEU C 505 ? 0.2262 0.1289 0.2083 0.0208  0.0448  -0.0207 497 LEU C C   
13207 O O   . LEU C 505 ? 0.1946 0.0979 0.1756 0.0190  0.0417  -0.0176 497 LEU C O   
13208 C CB  . LEU C 505 ? 0.1984 0.0970 0.1879 0.0343  0.0490  -0.0200 497 LEU C CB  
13209 C CG  . LEU C 505 ? 0.2065 0.0942 0.1917 0.0355  0.0479  -0.0164 497 LEU C CG  
13210 C CD1 . LEU C 505 ? 0.3015 0.1979 0.2903 0.0367  0.0427  -0.0114 497 LEU C CD1 
13211 C CD2 . LEU C 505 ? 0.2205 0.0975 0.2060 0.0429  0.0510  -0.0160 497 LEU C CD2 
13212 N N   . VAL C 506 ? 0.2537 0.1507 0.2304 0.0164  0.0477  -0.0251 498 VAL C N   
13213 C CA  . VAL C 506 ? 0.2468 0.1388 0.2169 0.0090  0.0468  -0.0261 498 VAL C CA  
13214 C C   . VAL C 506 ? 0.2289 0.1325 0.2012 0.0051  0.0424  -0.0244 498 VAL C C   
13215 O O   . VAL C 506 ? 0.2125 0.1153 0.1828 0.0016  0.0404  -0.0226 498 VAL C O   
13216 C CB  . VAL C 506 ? 0.2294 0.1146 0.1933 0.0047  0.0503  -0.0314 498 VAL C CB  
13217 C CG1 . VAL C 506 ? 0.2287 0.1115 0.1869 -0.0035 0.0485  -0.0323 498 VAL C CG1 
13218 C CG2 . VAL C 506 ? 0.2346 0.1057 0.1951 0.0086  0.0549  -0.0333 498 VAL C CG2 
13219 N N   . ALA C 507 ? 0.2187 0.1329 0.1950 0.0054  0.0412  -0.0251 499 ALA C N   
13220 C CA  . ALA C 507 ? 0.1599 0.0840 0.1379 0.0022  0.0371  -0.0236 499 ALA C CA  
13221 C C   . ALA C 507 ? 0.1751 0.1023 0.1561 0.0047  0.0340  -0.0194 499 ALA C C   
13222 O O   . ALA C 507 ? 0.2066 0.1357 0.1862 0.0013  0.0317  -0.0181 499 ALA C O   
13223 C CB  . ALA C 507 ? 0.1798 0.1135 0.1616 0.0028  0.0365  -0.0246 499 ALA C CB  
13224 N N   . TRP C 508 ? 0.2432 0.1713 0.2284 0.0107  0.0340  -0.0171 500 TRP C N   
13225 C CA  . TRP C 508 ? 0.2241 0.1542 0.2110 0.0133  0.0311  -0.0130 500 TRP C CA  
13226 C C   . TRP C 508 ? 0.2299 0.1509 0.2115 0.0112  0.0317  -0.0116 500 TRP C C   
13227 O O   . TRP C 508 ? 0.2141 0.1377 0.1945 0.0092  0.0294  -0.0094 500 TRP C O   
13228 C CB  . TRP C 508 ? 0.1987 0.1305 0.1907 0.0203  0.0311  -0.0110 500 TRP C CB  
13229 C CG  . TRP C 508 ? 0.2200 0.1639 0.2183 0.0219  0.0284  -0.0105 500 TRP C CG  
13230 C CD1 . TRP C 508 ? 0.2304 0.1802 0.2336 0.0236  0.0299  -0.0123 500 TRP C CD1 
13231 C CD2 . TRP C 508 ? 0.2228 0.1743 0.2228 0.0215  0.0241  -0.0081 500 TRP C CD2 
13232 N NE1 . TRP C 508 ? 0.2079 0.1683 0.2159 0.0238  0.0265  -0.0111 500 TRP C NE1 
13233 C CE2 . TRP C 508 ? 0.1919 0.1531 0.1978 0.0227  0.0228  -0.0086 500 TRP C CE2 
13234 C CE3 . TRP C 508 ? 0.1661 0.1169 0.1628 0.0201  0.0214  -0.0057 500 TRP C CE3 
13235 C CZ2 . TRP C 508 ? 0.2255 0.1948 0.2338 0.0223  0.0186  -0.0069 500 TRP C CZ2 
13236 C CZ3 . TRP C 508 ? 0.2003 0.1592 0.1991 0.0203  0.0176  -0.0042 500 TRP C CZ3 
13237 C CH2 . TRP C 508 ? 0.2210 0.1885 0.2253 0.0213  0.0160  -0.0049 500 TRP C CH2 
13238 N N   . ALA C 509 ? 0.1717 0.0814 0.1496 0.0116  0.0352  -0.0127 501 ALA C N   
13239 C CA  . ALA C 509 ? 0.2119 0.1115 0.1844 0.0092  0.0362  -0.0112 501 ALA C CA  
13240 C C   . ALA C 509 ? 0.2488 0.1504 0.2183 0.0017  0.0354  -0.0125 501 ALA C C   
13241 O O   . ALA C 509 ? 0.2279 0.1284 0.1953 -0.0005 0.0345  -0.0100 501 ALA C O   
13242 C CB  . ALA C 509 ? 0.2196 0.1056 0.1882 0.0106  0.0402  -0.0129 501 ALA C CB  
13243 N N   . GLU C 510 ? 0.2126 0.1171 0.1815 -0.0022 0.0359  -0.0163 502 GLU C N   
13244 C CA  . GLU C 510 ? 0.1879 0.0957 0.1549 -0.0090 0.0347  -0.0175 502 GLU C CA  
13245 C C   . GLU C 510 ? 0.2304 0.1497 0.2012 -0.0090 0.0311  -0.0153 502 GLU C C   
13246 O O   . GLU C 510 ? 0.2269 0.1485 0.1969 -0.0128 0.0301  -0.0144 502 GLU C O   
13247 C CB  . GLU C 510 ? 0.2511 0.1598 0.2164 -0.0129 0.0354  -0.0219 502 GLU C CB  
13248 C CG  . GLU C 510 ? 0.2606 0.1569 0.2205 -0.0144 0.0391  -0.0250 502 GLU C CG  
13249 C CD  . GLU C 510 ? 0.3157 0.2029 0.2709 -0.0192 0.0402  -0.0246 502 GLU C CD  
13250 O OE1 . GLU C 510 ? 0.2918 0.1839 0.2468 -0.0249 0.0383  -0.0246 502 GLU C OE1 
13251 O OE2 . GLU C 510 ? 0.2751 0.1502 0.2271 -0.0172 0.0430  -0.0243 502 GLU C OE2 
13252 N N   . ALA C 511 ? 0.1846 0.1113 0.1596 -0.0049 0.0292  -0.0146 503 ALA C N   
13253 C CA  . ALA C 511 ? 0.2071 0.1432 0.1849 -0.0044 0.0259  -0.0127 503 ALA C CA  
13254 C C   . ALA C 511 ? 0.2177 0.1521 0.1945 -0.0029 0.0254  -0.0092 503 ALA C C   
13255 O O   . ALA C 511 ? 0.1708 0.1100 0.1476 -0.0050 0.0240  -0.0082 503 ALA C O   
13256 C CB  . ALA C 511 ? 0.1532 0.0960 0.1352 -0.0005 0.0242  -0.0126 503 ALA C CB  
13257 N N   . ALA C 512 ? 0.2011 0.1288 0.1770 0.0010  0.0267  -0.0072 504 ALA C N   
13258 C CA  . ALA C 512 ? 0.2156 0.1403 0.1892 0.0025  0.0263  -0.0034 504 ALA C CA  
13259 C C   . ALA C 512 ? 0.2285 0.1471 0.1977 -0.0025 0.0284  -0.0031 504 ALA C C   
13260 O O   . ALA C 512 ? 0.2441 0.1636 0.2114 -0.0035 0.0280  -0.0005 504 ALA C O   
13261 C CB  . ALA C 512 ? 0.2641 0.1826 0.2376 0.0083  0.0268  -0.0011 504 ALA C CB  
13262 N N   . LYS C 513 ? 0.2171 0.1293 0.1843 -0.0061 0.0308  -0.0057 505 LYS C N   
13263 C CA  . LYS C 513 ? 0.3060 0.2119 0.2691 -0.0118 0.0328  -0.0056 505 LYS C CA  
13264 C C   . LYS C 513 ? 0.2867 0.2022 0.2516 -0.0171 0.0315  -0.0068 505 LYS C C   
13265 O O   . LYS C 513 ? 0.2825 0.1969 0.2456 -0.0213 0.0326  -0.0056 505 LYS C O   
13266 C CB  . LYS C 513 ? 0.3888 0.2841 0.3486 -0.0140 0.0356  -0.0086 505 LYS C CB  
13267 C CG  . LYS C 513 ? 0.5856 0.4708 0.5402 -0.0194 0.0381  -0.0081 505 LYS C CG  
13268 C CD  . LYS C 513 ? 0.5765 0.4501 0.5273 -0.0210 0.0408  -0.0116 505 LYS C CD  
13269 C CE  . LYS C 513 ? 0.5908 0.4542 0.5361 -0.0279 0.0430  -0.0118 505 LYS C CE  
13270 N NZ  . LYS C 513 ? 0.5524 0.4050 0.4933 -0.0306 0.0454  -0.0162 505 LYS C NZ  
13271 N N   . ALA C 514 ? 0.2323 0.1361 0.1994 -0.0161 0.0845  0.0213  506 ALA C N   
13272 C CA  . ALA C 514 ? 0.2760 0.2033 0.2510 -0.0246 0.0769  0.0163  506 ALA C CA  
13273 C C   . ALA C 514 ? 0.3121 0.2484 0.2873 -0.0176 0.0753  0.0225  506 ALA C C   
13274 O O   . ALA C 514 ? 0.3690 0.3084 0.3415 -0.0029 0.0680  0.0292  506 ALA C O   
13275 C CB  . ALA C 514 ? 0.2325 0.1771 0.2118 -0.0229 0.0622  0.0126  506 ALA C CB  
13276 N N   . GLU C 515 ? 0.2926 0.2333 0.2714 -0.0280 0.0824  0.0196  507 GLU C N   
13277 C CA  . GLU C 515 ? 0.3147 0.2632 0.2930 -0.0218 0.0830  0.0253  507 GLU C CA  
13278 C C   . GLU C 515 ? 0.3179 0.2960 0.3050 -0.0209 0.0681  0.0217  507 GLU C C   
13279 O O   . GLU C 515 ? 0.3188 0.3054 0.3041 -0.0098 0.0631  0.0276  507 GLU C O   
13280 C CB  . GLU C 515 ? 0.3781 0.3167 0.3565 -0.0332 0.0997  0.0244  507 GLU C CB  
13281 C CG  . GLU C 515 ? 0.5798 0.4860 0.5474 -0.0344 0.1152  0.0281  507 GLU C CG  
13282 C CD  . GLU C 515 ? 0.7614 0.6549 0.7252 -0.0398 0.1307  0.0309  507 GLU C CD  
13283 O OE1 . GLU C 515 ? 0.8369 0.7178 0.7888 -0.0267 0.1338  0.0401  507 GLU C OE1 
13284 O OE2 . GLU C 515 ? 0.8442 0.7428 0.8177 -0.0550 0.1354  0.0221  507 GLU C OE2 
13285 N N   . ASP C 516 ? 0.2298 0.2229 0.2250 -0.0311 0.0602  0.0120  508 ASP C N   
13286 C CA  . ASP C 516 ? 0.1713 0.1916 0.1746 -0.0321 0.0475  0.0069  508 ASP C CA  
13287 C C   . ASP C 516 ? 0.1664 0.1978 0.1698 -0.0295 0.0312  0.0030  508 ASP C C   
13288 O O   . ASP C 516 ? 0.1487 0.2000 0.1577 -0.0333 0.0204  -0.0040 508 ASP C O   
13289 C CB  . ASP C 516 ? 0.1923 0.2231 0.2058 -0.0479 0.0534  -0.0031 508 ASP C CB  
13290 C CG  . ASP C 516 ? 0.3333 0.3591 0.3493 -0.0607 0.0544  -0.0130 508 ASP C CG  
13291 O OD1 . ASP C 516 ? 0.3029 0.3115 0.3111 -0.0587 0.0562  -0.0107 508 ASP C OD1 
13292 O OD2 . ASP C 516 ? 0.3097 0.3494 0.3357 -0.0724 0.0533  -0.0238 508 ASP C OD2 
13293 N N   . HIS C 517 ? 0.1446 0.1632 0.1417 -0.0231 0.0293  0.0070  509 HIS C N   
13294 C CA  . HIS C 517 ? 0.1310 0.1584 0.1272 -0.0208 0.0153  0.0042  509 HIS C CA  
13295 C C   . HIS C 517 ? 0.1277 0.1429 0.1193 -0.0098 0.0143  0.0111  509 HIS C C   
13296 O O   . HIS C 517 ? 0.1754 0.1726 0.1639 -0.0071 0.0253  0.0153  509 HIS C O   
13297 C CB  . HIS C 517 ? 0.1470 0.1744 0.1431 -0.0341 0.0150  -0.0061 509 HIS C CB  
13298 C CG  . HIS C 517 ? 0.2335 0.2398 0.2260 -0.0404 0.0279  -0.0074 509 HIS C CG  
13299 N ND1 . HIS C 517 ? 0.2455 0.2433 0.2406 -0.0507 0.0406  -0.0114 509 HIS C ND1 
13300 C CD2 . HIS C 517 ? 0.2522 0.2446 0.2392 -0.0380 0.0302  -0.0059 509 HIS C CD2 
13301 C CE1 . HIS C 517 ? 0.2551 0.2336 0.2453 -0.0539 0.0494  -0.0121 509 HIS C CE1 
13302 N NE2 . HIS C 517 ? 0.2700 0.2456 0.2553 -0.0461 0.0433  -0.0090 509 HIS C NE2 
13303 N N   . PRO C 518 ? 0.1459 0.1703 0.1374 -0.0033 0.0012  0.0120  510 PRO C N   
13304 C CA  . PRO C 518 ? 0.1377 0.1533 0.1282 0.0062  -0.0003 0.0170  510 PRO C CA  
13305 C C   . PRO C 518 ? 0.1547 0.1605 0.1426 -0.0013 0.0036  0.0124  510 PRO C C   
13306 O O   . PRO C 518 ? 0.1611 0.1671 0.1464 -0.0129 0.0054  0.0054  510 PRO C O   
13307 C CB  . PRO C 518 ? 0.0946 0.1257 0.0870 0.0146  -0.0161 0.0189  510 PRO C CB  
13308 C CG  . PRO C 518 ? 0.1088 0.1534 0.1001 0.0051  -0.0234 0.0118  510 PRO C CG  
13309 C CD  . PRO C 518 ? 0.1321 0.1762 0.1252 -0.0032 -0.0133 0.0086  510 PRO C CD  
13310 N N   . SER C 519 ? 0.1187 0.1165 0.1077 0.0062  0.0045  0.0158  511 SER C N   
13311 C CA  . SER C 519 ? 0.1361 0.1248 0.1230 0.0008  0.0090  0.0119  511 SER C CA  
13312 C C   . SER C 519 ? 0.1572 0.1504 0.1482 0.0084  0.0013  0.0142  511 SER C C   
13313 O O   . SER C 519 ? 0.1392 0.1364 0.1359 0.0202  -0.0038 0.0193  511 SER C O   
13314 C CB  . SER C 519 ? 0.1885 0.1588 0.1744 0.0005  0.0231  0.0122  511 SER C CB  
13315 O OG  . SER C 519 ? 0.1888 0.1530 0.1715 -0.0077 0.0315  0.0100  511 SER C OG  
13316 N N   . CYS C 520 ? 0.1133 0.1050 0.1008 0.0014  0.0008  0.0099  512 CYS C N   
13317 C CA  . CYS C 520 ? 0.1463 0.1384 0.1378 0.0056  -0.0021 0.0108  512 CYS C CA  
13318 C C   . CYS C 520 ? 0.1872 0.1659 0.1793 0.0029  0.0104  0.0082  512 CYS C C   
13319 O O   . CYS C 520 ? 0.2026 0.1737 0.1865 -0.0071 0.0170  0.0034  512 CYS C O   
13320 C CB  . CYS C 520 ? 0.1052 0.1036 0.0901 -0.0002 -0.0109 0.0083  512 CYS C CB  
13321 S SG  . CYS C 520 ? 0.1935 0.2080 0.1777 0.0044  -0.0275 0.0107  512 CYS C SG  
13322 N N   . LEU C 521 ? 0.1188 0.0950 0.1206 0.0124  0.0132  0.0107  513 LEU C N   
13323 C CA  . LEU C 521 ? 0.1292 0.0942 0.1338 0.0122  0.0245  0.0079  513 LEU C CA  
13324 C C   . LEU C 521 ? 0.1676 0.1378 0.1800 0.0135  0.0226  0.0066  513 LEU C C   
13325 O O   . LEU C 521 ? 0.1548 0.1337 0.1783 0.0227  0.0153  0.0092  513 LEU C O   
13326 C CB  . LEU C 521 ? 0.1340 0.0916 0.1444 0.0231  0.0294  0.0105  513 LEU C CB  
13327 C CG  . LEU C 521 ? 0.1973 0.1485 0.2006 0.0235  0.0320  0.0133  513 LEU C CG  
13328 C CD1 . LEU C 521 ? 0.1827 0.1223 0.1886 0.0354  0.0377  0.0159  513 LEU C CD1 
13329 C CD2 . LEU C 521 ? 0.1871 0.1304 0.1803 0.0095  0.0395  0.0088  513 LEU C CD2 
13330 N N   . ILE C 522 ? 0.1328 0.0973 0.1393 0.0042  0.0295  0.0021  514 ILE C N   
13331 C CA  . ILE C 522 ? 0.1515 0.1199 0.1617 0.0019  0.0287  0.0008  514 ILE C CA  
13332 C C   . ILE C 522 ? 0.2292 0.1909 0.2467 0.0025  0.0411  -0.0031 514 ILE C C   
13333 O O   . ILE C 522 ? 0.1922 0.1429 0.2005 -0.0036 0.0508  -0.0068 514 ILE C O   
13334 C CB  . ILE C 522 ? 0.1769 0.1434 0.1707 -0.0093 0.0263  -0.0011 514 ILE C CB  
13335 C CG1 . ILE C 522 ? 0.1804 0.1555 0.1687 -0.0085 0.0127  0.0019  514 ILE C CG1 
13336 C CG2 . ILE C 522 ? 0.1467 0.1130 0.1414 -0.0128 0.0286  -0.0023 514 ILE C CG2 
13337 C CD1 . ILE C 522 ? 0.1603 0.1323 0.1300 -0.0184 0.0089  -0.0010 514 ILE C CD1 
13338 N N   . PHE C 523 ? 0.1333 0.1021 0.1677 0.0096  0.0405  -0.0033 515 PHE C N   
13339 C CA  . PHE C 523 ? 0.1403 0.1058 0.1862 0.0130  0.0512  -0.0077 515 PHE C CA  
13340 C C   . PHE C 523 ? 0.2039 0.1754 0.2599 0.0095  0.0546  -0.0105 515 PHE C C   
13341 O O   . PHE C 523 ? 0.2023 0.1831 0.2646 0.0100  0.0463  -0.0083 515 PHE C O   
13342 C CB  . PHE C 523 ? 0.1459 0.1145 0.2069 0.0277  0.0483  -0.0068 515 PHE C CB  
13343 C CG  . PHE C 523 ? 0.2073 0.1667 0.2580 0.0315  0.0480  -0.0039 515 PHE C CG  
13344 C CD1 . PHE C 523 ? 0.2486 0.1940 0.2925 0.0301  0.0588  -0.0067 515 PHE C CD1 
13345 C CD2 . PHE C 523 ? 0.1543 0.1181 0.2016 0.0361  0.0376  0.0016  515 PHE C CD2 
13346 C CE1 . PHE C 523 ? 0.2227 0.1578 0.2569 0.0327  0.0597  -0.0039 515 PHE C CE1 
13347 C CE2 . PHE C 523 ? 0.1789 0.1334 0.2165 0.0388  0.0392  0.0044  515 PHE C CE2 
13348 C CZ  . PHE C 523 ? 0.1954 0.1350 0.2265 0.0366  0.0505  0.0018  515 PHE C CZ  
13349 N N   . SER C 524 ? 0.2214 0.1870 0.2789 0.0058  0.0676  -0.0157 516 SER C N   
13350 C CA  . SER C 524 ? 0.2690 0.2413 0.3417 0.0044  0.0737  -0.0195 516 SER C CA  
13351 C C   . SER C 524 ? 0.3887 0.3670 0.4844 0.0161  0.0770  -0.0239 516 SER C C   
13352 O O   . SER C 524 ? 0.4014 0.3756 0.4973 0.0252  0.0751  -0.0235 516 SER C O   
13353 C CB  . SER C 524 ? 0.3232 0.2857 0.3820 -0.0075 0.0867  -0.0230 516 SER C CB  
13354 O OG  . SER C 524 ? 0.3725 0.3241 0.4226 -0.0075 0.0953  -0.0263 516 SER C OG  
13355 N N   . ARG C 525 ? 0.4473 0.4345 0.5620 0.0160  0.0826  -0.0288 517 ARG C N   
13356 C CA  . ARG C 525 ? 0.5072 0.5015 0.6444 0.0265  0.0854  -0.0347 517 ARG C CA  
13357 C C   . ARG C 525 ? 0.6033 0.5864 0.7305 0.0256  0.0954  -0.0381 517 ARG C C   
13358 O O   . ARG C 525 ? 0.6088 0.5815 0.7223 0.0160  0.1082  -0.0401 517 ARG C O   
13359 C CB  . ARG C 525 ? 0.4538 0.4610 0.6111 0.0232  0.0875  -0.0390 517 ARG C CB  
13360 N N   . GLN C 531 ? 0.7243 0.5631 0.7055 -0.0072 0.1617  -0.0611 523 GLN C N   
13361 C CA  . GLN C 531 ? 0.7651 0.5897 0.7268 -0.0169 0.1642  -0.0629 523 GLN C CA  
13362 C C   . GLN C 531 ? 0.6993 0.5104 0.6558 -0.0139 0.1642  -0.0629 523 GLN C C   
13363 O O   . GLN C 531 ? 0.7047 0.5135 0.6634 -0.0100 0.1593  -0.0585 523 GLN C O   
13364 C CB  . GLN C 531 ? 0.8120 0.6377 0.7651 -0.0244 0.1592  -0.0604 523 GLN C CB  
13365 C CG  . GLN C 531 ? 0.8432 0.6805 0.7988 -0.0275 0.1583  -0.0598 523 GLN C CG  
13366 C CD  . GLN C 531 ? 0.8432 0.6786 0.7902 -0.0334 0.1650  -0.0640 523 GLN C CD  
13367 O OE1 . GLN C 531 ? 0.8317 0.6562 0.7665 -0.0372 0.1689  -0.0677 523 GLN C OE1 
13368 N NE2 . GLN C 531 ? 0.8548 0.7004 0.8079 -0.0342 0.1664  -0.0632 523 GLN C NE2 
13369 N N   . ALA C 532 ? 0.6220 0.4234 0.5707 -0.0158 0.1699  -0.0677 524 ALA C N   
13370 C CA  . ALA C 532 ? 0.6079 0.3946 0.5500 -0.0140 0.1705  -0.0681 524 ALA C CA  
13371 C C   . ALA C 532 ? 0.5279 0.3061 0.4577 -0.0236 0.1683  -0.0672 524 ALA C C   
13372 O O   . ALA C 532 ? 0.5310 0.3112 0.4523 -0.0328 0.1677  -0.0693 524 ALA C O   
13373 C CB  . ALA C 532 ? 0.6061 0.3848 0.5427 -0.0136 0.1769  -0.0742 524 ALA C CB  
13374 N N   . ARG C 533 ? 0.4816 0.2504 0.4101 -0.0212 0.1666  -0.0642 525 ARG C N   
13375 C CA  . ARG C 533 ? 0.4599 0.2223 0.3797 -0.0302 0.1647  -0.0637 525 ARG C CA  
13376 C C   . ARG C 533 ? 0.4823 0.2286 0.3965 -0.0295 0.1674  -0.0640 525 ARG C C   
13377 O O   . ARG C 533 ? 0.5678 0.3084 0.4859 -0.0199 0.1681  -0.0610 525 ARG C O   
13378 C CB  . ARG C 533 ? 0.4379 0.2085 0.3632 -0.0295 0.1589  -0.0578 525 ARG C CB  
13379 C CG  . ARG C 533 ? 0.3865 0.1707 0.3133 -0.0339 0.1551  -0.0581 525 ARG C CG  
13380 C CD  . ARG C 533 ? 0.4470 0.2379 0.3789 -0.0326 0.1489  -0.0526 525 ARG C CD  
13381 N NE  . ARG C 533 ? 0.4025 0.2065 0.3376 -0.0339 0.1447  -0.0522 525 ARG C NE  
13382 C CZ  . ARG C 533 ? 0.3793 0.1933 0.3254 -0.0258 0.1438  -0.0498 525 ARG C CZ  
13383 N NH1 . ARG C 533 ? 0.4063 0.2203 0.3620 -0.0154 0.1455  -0.0480 525 ARG C NH1 
13384 N NH2 . ARG C 533 ? 0.3954 0.2202 0.3432 -0.0279 0.1404  -0.0497 525 ARG C NH2 
13385 N N   . SER C 534 ? 0.4388 0.1777 0.3437 -0.0396 0.1684  -0.0681 526 SER C N   
13386 C CA  . SER C 534 ? 0.4850 0.2090 0.3850 -0.0414 0.1707  -0.0682 526 SER C CA  
13387 C C   . SER C 534 ? 0.5084 0.2329 0.4117 -0.0411 0.1682  -0.0618 526 SER C C   
13388 O O   . SER C 534 ? 0.4601 0.1970 0.3690 -0.0406 0.1638  -0.0581 526 SER C O   
13389 C CB  . SER C 534 ? 0.5018 0.2206 0.3933 -0.0527 0.1713  -0.0753 526 SER C CB  
13390 O OG  . SER C 534 ? 0.5177 0.2477 0.4094 -0.0613 0.1661  -0.0763 526 SER C OG  
13391 N N   . GLU C 535 ? 0.5448 0.2549 0.4439 -0.0413 0.1712  -0.0605 527 GLU C N   
13392 C CA  . GLU C 535 ? 0.5581 0.2670 0.4584 -0.0425 0.1702  -0.0549 527 GLU C CA  
13393 C C   . GLU C 535 ? 0.4421 0.1625 0.3444 -0.0541 0.1666  -0.0576 527 GLU C C   
13394 O O   . GLU C 535 ? 0.4619 0.1915 0.3690 -0.0536 0.1629  -0.0530 527 GLU C O   
13395 C CB  . GLU C 535 ? 0.5786 0.2682 0.4722 -0.0426 0.1754  -0.0541 527 GLU C CB  
13396 C CG  . GLU C 535 ? 0.6267 0.3134 0.5199 -0.0476 0.1764  -0.0504 527 GLU C CG  
13397 C CD  . GLU C 535 ? 0.6548 0.3216 0.5405 -0.0507 0.1826  -0.0516 527 GLU C CD  
13398 O OE1 . GLU C 535 ? 0.6261 0.2858 0.5084 -0.0554 0.1847  -0.0583 527 GLU C OE1 
13399 O OE2 . GLU C 535 ? 0.6282 0.2858 0.5107 -0.0480 0.1854  -0.0457 527 GLU C OE2 
13400 N N   . GLN C 536 ? 0.5072 0.2278 0.4060 -0.0639 0.1664  -0.0653 528 GLN C N   
13401 C CA  . GLN C 536 ? 0.5071 0.2401 0.4081 -0.0741 0.1610  -0.0690 528 GLN C CA  
13402 C C   . GLN C 536 ? 0.4673 0.2166 0.3718 -0.0722 0.1549  -0.0671 528 GLN C C   
13403 O O   . GLN C 536 ? 0.4434 0.2036 0.3523 -0.0757 0.1498  -0.0655 528 GLN C O   
13404 C CB  . GLN C 536 ? 0.5569 0.2875 0.4529 -0.0829 0.1604  -0.0783 528 GLN C CB  
13405 C CG  . GLN C 536 ? 0.6336 0.3771 0.5324 -0.0930 0.1535  -0.0831 528 GLN C CG  
13406 C CD  . GLN C 536 ? 0.6953 0.4401 0.6010 -0.0975 0.1538  -0.0809 528 GLN C CD  
13407 O OE1 . GLN C 536 ? 0.7704 0.5062 0.6766 -0.1030 0.1573  -0.0844 528 GLN C OE1 
13408 N NE2 . GLN C 536 ? 0.7028 0.4586 0.6140 -0.0952 0.1504  -0.0753 528 GLN C NE2 
13409 N N   . GLN C 537 ? 0.4184 0.1697 0.3213 -0.0668 0.1555  -0.0675 529 GLN C N   
13410 C CA  . GLN C 537 ? 0.3927 0.1582 0.2983 -0.0653 0.1504  -0.0660 529 GLN C CA  
13411 C C   . GLN C 537 ? 0.3769 0.1478 0.2907 -0.0580 0.1482  -0.0580 529 GLN C C   
13412 O O   . GLN C 537 ? 0.3610 0.1432 0.2777 -0.0604 0.1421  -0.0564 529 GLN C O   
13413 C CB  . GLN C 537 ? 0.3949 0.1607 0.2978 -0.0611 0.1531  -0.0682 529 GLN C CB  
13414 C CG  . GLN C 537 ? 0.4922 0.2558 0.3853 -0.0685 0.1530  -0.0758 529 GLN C CG  
13415 C CD  . GLN C 537 ? 0.5550 0.3159 0.4450 -0.0637 0.1579  -0.0779 529 GLN C CD  
13416 O OE1 . GLN C 537 ? 0.5345 0.2905 0.4298 -0.0556 0.1628  -0.0755 529 GLN C OE1 
13417 N NE2 . GLN C 537 ? 0.5913 0.3557 0.4726 -0.0683 0.1563  -0.0823 529 GLN C NE2 
13418 N N   . LEU C 538 ? 0.3973 0.1598 0.3140 -0.0482 0.1522  -0.0530 530 LEU C N   
13419 C CA  . LEU C 538 ? 0.3947 0.1607 0.3179 -0.0400 0.1495  -0.0452 530 LEU C CA  
13420 C C   . LEU C 538 ? 0.3666 0.1349 0.2899 -0.0463 0.1469  -0.0432 530 LEU C C   
13421 O O   . LEU C 538 ? 0.3500 0.1284 0.2782 -0.0445 0.1416  -0.0391 530 LEU C O   
13422 C CB  . LEU C 538 ? 0.4320 0.1866 0.3555 -0.0288 0.1532  -0.0408 530 LEU C CB  
13423 C CG  . LEU C 538 ? 0.5156 0.2729 0.4441 -0.0184 0.1534  -0.0410 530 LEU C CG  
13424 C CD1 . LEU C 538 ? 0.5077 0.2517 0.4336 -0.0088 0.1560  -0.0385 530 LEU C CD1 
13425 C CD2 . LEU C 538 ? 0.4173 0.1902 0.3561 -0.0110 0.1473  -0.0372 530 LEU C CD2 
13426 N N   . ASN C 539 ? 0.3901 0.1499 0.3091 -0.0539 0.1505  -0.0463 531 ASN C N   
13427 C CA  . ASN C 539 ? 0.4041 0.1665 0.3250 -0.0603 0.1491  -0.0451 531 ASN C CA  
13428 C C   . ASN C 539 ? 0.3657 0.1448 0.2900 -0.0692 0.1415  -0.0492 531 ASN C C   
13429 O O   . ASN C 539 ? 0.3677 0.1539 0.2965 -0.0728 0.1386  -0.0473 531 ASN C O   
13430 C CB  . ASN C 539 ? 0.4296 0.1792 0.3463 -0.0669 0.1552  -0.0487 531 ASN C CB  
13431 C CG  . ASN C 539 ? 0.4769 0.2090 0.3889 -0.0585 0.1619  -0.0431 531 ASN C CG  
13432 O OD1 . ASN C 539 ? 0.5405 0.2715 0.4530 -0.0478 0.1612  -0.0356 531 ASN C OD1 
13433 N ND2 . ASN C 539 ? 0.4836 0.2015 0.3904 -0.0629 0.1678  -0.0467 531 ASN C ND2 
13434 N N   . ASP C 540 ? 0.3620 0.1472 0.2837 -0.0728 0.1383  -0.0549 532 ASP C N   
13435 C CA  . ASP C 540 ? 0.4184 0.2185 0.3409 -0.0807 0.1299  -0.0593 532 ASP C CA  
13436 C C   . ASP C 540 ? 0.3501 0.1614 0.2748 -0.0761 0.1236  -0.0554 532 ASP C C   
13437 O O   . ASP C 540 ? 0.3285 0.1525 0.2532 -0.0818 0.1155  -0.0582 532 ASP C O   
13438 C CB  . ASP C 540 ? 0.3608 0.1602 0.2761 -0.0872 0.1289  -0.0680 532 ASP C CB  
13439 C CG  . ASP C 540 ? 0.4260 0.2192 0.3413 -0.0947 0.1316  -0.0737 532 ASP C CG  
13440 O OD1 . ASP C 540 ? 0.3985 0.1923 0.3201 -0.0974 0.1328  -0.0718 532 ASP C OD1 
13441 O OD2 . ASP C 540 ? 0.4708 0.2584 0.3800 -0.0979 0.1328  -0.0801 532 ASP C OD2 
13442 N N   . ILE C 541 ? 0.3254 0.1330 0.2528 -0.0658 0.1263  -0.0492 533 ILE C N   
13443 C CA  . ILE C 541 ? 0.3093 0.1273 0.2408 -0.0613 0.1201  -0.0451 533 ILE C CA  
13444 C C   . ILE C 541 ? 0.2986 0.1270 0.2349 -0.0646 0.1134  -0.0417 533 ILE C C   
13445 O O   . ILE C 541 ? 0.2894 0.1346 0.2268 -0.0660 0.1038  -0.0415 533 ILE C O   
13446 C CB  . ILE C 541 ? 0.3034 0.1165 0.2401 -0.0482 0.1237  -0.0392 533 ILE C CB  
13447 C CG1 . ILE C 541 ? 0.3138 0.1207 0.2476 -0.0452 0.1298  -0.0432 533 ILE C CG1 
13448 C CG2 . ILE C 541 ? 0.3194 0.1503 0.2634 -0.0418 0.1149  -0.0336 533 ILE C CG2 
13449 C CD1 . ILE C 541 ? 0.3143 0.1177 0.2550 -0.0315 0.1332  -0.0386 533 ILE C CD1 
13450 N N   . LYS C 542 ? 0.2994 0.1233 0.2387 -0.0640 0.1167  -0.0383 534 LYS C N   
13451 C CA  . LYS C 542 ? 0.2883 0.1230 0.2330 -0.0666 0.1116  -0.0347 534 LYS C CA  
13452 C C   . LYS C 542 ? 0.2963 0.1434 0.2413 -0.0788 0.1054  -0.0425 534 LYS C C   
13453 O O   . LYS C 542 ? 0.2773 0.1367 0.2279 -0.0817 0.1002  -0.0410 534 LYS C O   
13454 C CB  . LYS C 542 ? 0.2983 0.1237 0.2443 -0.0629 0.1180  -0.0293 534 LYS C CB  
13455 C CG  . LYS C 542 ? 0.3183 0.1338 0.2612 -0.0702 0.1249  -0.0351 534 LYS C CG  
13456 C CD  . LYS C 542 ? 0.3297 0.1354 0.2724 -0.0668 0.1314  -0.0292 534 LYS C CD  
13457 C CE  . LYS C 542 ? 0.4887 0.2792 0.4267 -0.0709 0.1399  -0.0334 534 LYS C CE  
13458 N NZ  . LYS C 542 ? 0.5078 0.2842 0.4392 -0.0628 0.1443  -0.0325 534 LYS C NZ  
13459 N N   . ARG C 543 ? 0.3189 0.1640 0.2583 -0.0849 0.1053  -0.0511 535 ARG C N   
13460 C CA  . ARG C 543 ? 0.2939 0.1516 0.2327 -0.0942 0.0974  -0.0593 535 ARG C CA  
13461 C C   . ARG C 543 ? 0.2827 0.1503 0.2157 -0.0937 0.0878  -0.0612 535 ARG C C   
13462 O O   . ARG C 543 ? 0.2827 0.1607 0.2126 -0.0990 0.0794  -0.0681 535 ARG C O   
13463 C CB  . ARG C 543 ? 0.3126 0.1630 0.2474 -0.1001 0.1014  -0.0673 535 ARG C CB  
13464 C CG  . ARG C 543 ? 0.3530 0.1920 0.2921 -0.1012 0.1110  -0.0659 535 ARG C CG  
13465 C CD  . ARG C 543 ? 0.4003 0.2362 0.3389 -0.1094 0.1127  -0.0749 535 ARG C CD  
13466 N NE  . ARG C 543 ? 0.3862 0.2382 0.3322 -0.1172 0.1051  -0.0813 535 ARG C NE  
13467 C CZ  . ARG C 543 ? 0.3882 0.2406 0.3383 -0.1247 0.1057  -0.0892 535 ARG C CZ  
13468 N NH1 . ARG C 543 ? 0.3959 0.2323 0.3424 -0.1261 0.1138  -0.0912 535 ARG C NH1 
13469 N NH2 . ARG C 543 ? 0.3839 0.2529 0.3425 -0.1305 0.0979  -0.0953 535 ARG C NH2 
13470 N N   . GLY C 544 ? 0.2734 0.1410 0.2053 -0.0849 0.0873  -0.0543 536 GLY C N   
13471 C CA  . GLY C 544 ? 0.2607 0.1417 0.1886 -0.0815 0.0771  -0.0530 536 GLY C CA  
13472 C C   . GLY C 544 ? 0.3024 0.1762 0.2175 -0.0833 0.0782  -0.0584 536 GLY C C   
13473 O O   . GLY C 544 ? 0.2721 0.1508 0.1839 -0.0782 0.0749  -0.0547 536 GLY C O   
13474 N N   . ALA C 545 ? 0.2890 0.1523 0.1970 -0.0900 0.0827  -0.0667 537 ALA C N   
13475 C CA  . ALA C 545 ? 0.3013 0.1576 0.1973 -0.0896 0.0854  -0.0701 537 ALA C CA  
13476 C C   . ALA C 545 ? 0.3583 0.2036 0.2539 -0.0922 0.0935  -0.0742 537 ALA C C   
13477 O O   . ALA C 545 ? 0.3291 0.1755 0.2309 -0.0965 0.0933  -0.0768 537 ALA C O   
13478 C CB  . ALA C 545 ? 0.3077 0.1729 0.1925 -0.0919 0.0743  -0.0740 537 ALA C CB  
13479 N N   . TYR C 546 ? 0.3370 0.1719 0.2259 -0.0895 0.1009  -0.0748 538 TYR C N   
13480 C CA  . TYR C 546 ? 0.3813 0.2045 0.2690 -0.0908 0.1088  -0.0784 538 TYR C CA  
13481 C C   . TYR C 546 ? 0.4017 0.2176 0.2787 -0.0886 0.1136  -0.0803 538 TYR C C   
13482 O O   . TYR C 546 ? 0.3522 0.1706 0.2258 -0.0850 0.1139  -0.0773 538 TYR C O   
13483 C CB  . TYR C 546 ? 0.3552 0.1705 0.2529 -0.0866 0.1172  -0.0738 538 TYR C CB  
13484 C CG  . TYR C 546 ? 0.3397 0.1524 0.2409 -0.0778 0.1224  -0.0680 538 TYR C CG  
13485 C CD1 . TYR C 546 ? 0.3810 0.2020 0.2886 -0.0737 0.1181  -0.0625 538 TYR C CD1 
13486 C CD2 . TYR C 546 ? 0.3511 0.1541 0.2506 -0.0732 0.1309  -0.0685 538 TYR C CD2 
13487 C CE1 . TYR C 546 ? 0.3612 0.1812 0.2744 -0.0648 0.1222  -0.0580 538 TYR C CE1 
13488 C CE2 . TYR C 546 ? 0.3544 0.1577 0.2600 -0.0644 0.1350  -0.0642 538 TYR C CE2 
13489 C CZ  . TYR C 546 ? 0.3585 0.1706 0.2715 -0.0601 0.1306  -0.0591 538 TYR C CZ  
13490 O OH  . TYR C 546 ? 0.3577 0.1721 0.2793 -0.0507 0.1340  -0.0556 538 TYR C OH  
13491 N N   . VAL C 547 ? 0.3767 0.1833 0.2487 -0.0909 0.1177  -0.0855 539 VAL C N   
13492 C CA  . VAL C 547 ? 0.4023 0.2010 0.2641 -0.0887 0.1231  -0.0876 539 VAL C CA  
13493 C C   . VAL C 547 ? 0.4150 0.2077 0.2843 -0.0819 0.1334  -0.0831 539 VAL C C   
13494 O O   . VAL C 547 ? 0.4422 0.2271 0.3176 -0.0801 0.1388  -0.0829 539 VAL C O   
13495 C CB  . VAL C 547 ? 0.4726 0.2630 0.3268 -0.0926 0.1233  -0.0951 539 VAL C CB  
13496 C CG1 . VAL C 547 ? 0.4441 0.2265 0.2867 -0.0900 0.1288  -0.0971 539 VAL C CG1 
13497 C CG2 . VAL C 547 ? 0.4397 0.2378 0.2898 -0.0978 0.1118  -0.1001 539 VAL C CG2 
13498 N N   . ILE C 548 ? 0.4247 0.2215 0.2943 -0.0776 0.1355  -0.0796 540 ILE C N   
13499 C CA  . ILE C 548 ? 0.4090 0.2031 0.2883 -0.0700 0.1440  -0.0763 540 ILE C CA  
13500 C C   . ILE C 548 ? 0.4410 0.2271 0.3143 -0.0685 0.1515  -0.0799 540 ILE C C   
13501 O O   . ILE C 548 ? 0.3995 0.1818 0.2812 -0.0623 0.1582  -0.0789 540 ILE C O   
13502 C CB  . ILE C 548 ? 0.3959 0.2000 0.2825 -0.0654 0.1428  -0.0713 540 ILE C CB  
13503 C CG1 . ILE C 548 ? 0.4475 0.2520 0.3492 -0.0560 0.1491  -0.0677 540 ILE C CG1 
13504 C CG2 . ILE C 548 ? 0.3733 0.1801 0.2495 -0.0677 0.1430  -0.0725 540 ILE C CG2 
13505 C CD1 . ILE C 548 ? 0.4606 0.2768 0.3733 -0.0505 0.1469  -0.0632 540 ILE C CD1 
13506 N N   . SER C 549 ? 0.4089 0.1925 0.2676 -0.0733 0.1500  -0.0842 541 SER C N   
13507 C CA  . SER C 549 ? 0.5074 0.2826 0.3590 -0.0719 0.1571  -0.0881 541 SER C CA  
13508 C C   . SER C 549 ? 0.4746 0.2443 0.3092 -0.0776 0.1524  -0.0939 541 SER C C   
13509 O O   . SER C 549 ? 0.4682 0.2410 0.2914 -0.0799 0.1476  -0.0941 541 SER C O   
13510 C CB  . SER C 549 ? 0.4838 0.2635 0.3370 -0.0683 0.1627  -0.0857 541 SER C CB  
13511 O OG  . SER C 549 ? 0.4644 0.2365 0.3112 -0.0668 0.1700  -0.0896 541 SER C OG  
13512 N N   . GLU C 550 ? 0.4583 0.2195 0.2912 -0.0791 0.1530  -0.0988 542 GLU C N   
13513 C CA  . GLU C 550 ? 0.5481 0.3045 0.3669 -0.0835 0.1473  -0.1055 542 GLU C CA  
13514 C C   . GLU C 550 ? 0.5363 0.2866 0.3405 -0.0815 0.1517  -0.1083 542 GLU C C   
13515 O O   . GLU C 550 ? 0.5322 0.2796 0.3392 -0.0772 0.1610  -0.1067 542 GLU C O   
13516 C CB  . GLU C 550 ? 0.6556 0.4040 0.4779 -0.0857 0.1474  -0.1104 542 GLU C CB  
13517 C CG  . GLU C 550 ? 0.7588 0.5033 0.5694 -0.0900 0.1401  -0.1187 542 GLU C CG  
13518 C CD  . GLU C 550 ? 0.8255 0.5808 0.6346 -0.0939 0.1282  -0.1195 542 GLU C CD  
13519 O OE1 . GLU C 550 ? 0.8468 0.6085 0.6679 -0.0971 0.1242  -0.1183 542 GLU C OE1 
13520 O OE2 . GLU C 550 ? 0.4997 0.2570 0.2952 -0.0931 0.1226  -0.1212 542 GLU C OE2 
13521 N N   . ALA C 551 ? 0.5437 0.2925 0.3325 -0.0840 0.1445  -0.1126 543 ALA C N   
13522 C CA  . ALA C 551 ? 0.5536 0.2945 0.3256 -0.0819 0.1481  -0.1158 543 ALA C CA  
13523 C C   . ALA C 551 ? 0.5771 0.3073 0.3483 -0.0800 0.1547  -0.1214 543 ALA C C   
13524 O O   . ALA C 551 ? 0.5797 0.3066 0.3583 -0.0817 0.1528  -0.1248 543 ALA C O   
13525 C CB  . ALA C 551 ? 0.5373 0.2780 0.2924 -0.0834 0.1373  -0.1198 543 ALA C CB  
13526 N N   . GLN C 552 ? 0.6059 0.3302 0.3681 -0.0765 0.1628  -0.1223 544 GLN C N   
13527 C CA  . GLN C 552 ? 0.6656 0.3789 0.4223 -0.0740 0.1681  -0.1287 544 GLN C CA  
13528 C C   . GLN C 552 ? 0.6890 0.3956 0.4258 -0.0749 0.1608  -0.1357 544 GLN C C   
13529 O O   . GLN C 552 ? 0.6716 0.3764 0.3926 -0.0733 0.1614  -0.1354 544 GLN C O   
13530 C CB  . GLN C 552 ? 0.6562 0.3679 0.4140 -0.0691 0.1802  -0.1268 544 GLN C CB  
13531 N N   . GLY C 553 ? 0.6665 0.3693 0.4042 -0.0772 0.1537  -0.1423 545 GLY C N   
13532 C CA  . GLY C 553 ? 0.6713 0.3708 0.3935 -0.0778 0.1435  -0.1497 545 GLY C CA  
13533 C C   . GLY C 553 ? 0.6897 0.3999 0.4144 -0.0810 0.1317  -0.1479 545 GLY C C   
13534 O O   . GLY C 553 ? 0.6700 0.3895 0.4081 -0.0833 0.1317  -0.1410 545 GLY C O   
13535 N N   . ASN C 554 ? 0.6757 0.3849 0.3871 -0.0802 0.1208  -0.1548 546 ASN C N   
13536 C CA  . ASN C 554 ? 0.6455 0.3656 0.3598 -0.0821 0.1077  -0.1549 546 ASN C CA  
13537 C C   . ASN C 554 ? 0.6463 0.3727 0.3549 -0.0806 0.1080  -0.1460 546 ASN C C   
13538 O O   . ASN C 554 ? 0.6150 0.3354 0.3067 -0.0770 0.1124  -0.1439 546 ASN C O   
13539 C CB  . ASN C 554 ? 0.6754 0.3931 0.3773 -0.0797 0.0950  -0.1657 546 ASN C CB  
13540 N N   . ALA C 555 ? 0.6846 0.4227 0.4072 -0.0835 0.1036  -0.1408 547 ALA C N   
13541 C CA  . ALA C 555 ? 0.6677 0.4118 0.3866 -0.0824 0.1036  -0.1322 547 ALA C CA  
13542 C C   . ALA C 555 ? 0.6429 0.3872 0.3433 -0.0786 0.0924  -0.1347 547 ALA C C   
13543 O O   . ALA C 555 ? 0.5827 0.3309 0.2822 -0.0777 0.0798  -0.1424 547 ALA C O   
13544 C CB  . ALA C 555 ? 0.5352 0.2920 0.2736 -0.0858 0.1005  -0.1268 547 ALA C CB  
13545 N N   . GLN C 556 ? 0.5969 0.3368 0.2831 -0.0761 0.0973  -0.1286 548 GLN C N   
13546 C CA  . GLN C 556 ? 0.6702 0.4097 0.3382 -0.0720 0.0876  -0.1286 548 GLN C CA  
13547 C C   . GLN C 556 ? 0.6573 0.4074 0.3314 -0.0725 0.0813  -0.1212 548 GLN C C   
13548 O O   . GLN C 556 ? 0.5800 0.3323 0.2424 -0.0686 0.0706  -0.1217 548 GLN C O   
13549 C CB  . GLN C 556 ? 0.7001 0.4259 0.3461 -0.0690 0.0971  -0.1263 548 GLN C CB  
13550 C CG  . GLN C 556 ? 0.8099 0.5249 0.4488 -0.0677 0.1040  -0.1334 548 GLN C CG  
13551 C CD  . GLN C 556 ? 0.8605 0.5623 0.4775 -0.0646 0.1139  -0.1310 548 GLN C CD  
13552 O OE1 . GLN C 556 ? 0.8573 0.5545 0.4550 -0.0612 0.1089  -0.1297 548 GLN C OE1 
13553 N NE2 . GLN C 556 ? 0.9956 0.6912 0.6158 -0.0654 0.1282  -0.1305 548 GLN C NE2 
13554 N N   . ALA C 557 ? 0.5781 0.3349 0.2700 -0.0763 0.0874  -0.1147 549 ALA C N   
13555 C CA  . ALA C 557 ? 0.5272 0.2951 0.2273 -0.0768 0.0810  -0.1082 549 ALA C CA  
13556 C C   . ALA C 557 ? 0.5208 0.2959 0.2436 -0.0810 0.0878  -0.1043 549 ALA C C   
13557 O O   . ALA C 557 ? 0.5042 0.2745 0.2346 -0.0828 0.0984  -0.1058 549 ALA C O   
13558 C CB  . ALA C 557 ? 0.5334 0.2957 0.2189 -0.0749 0.0843  -0.1006 549 ALA C CB  
13559 N N   . VAL C 558 ? 0.4806 0.2671 0.2138 -0.0816 0.0816  -0.0994 550 VAL C N   
13560 C CA  . VAL C 558 ? 0.4573 0.2510 0.2109 -0.0844 0.0871  -0.0953 550 VAL C CA  
13561 C C   . VAL C 558 ? 0.4443 0.2417 0.1986 -0.0835 0.0887  -0.0869 550 VAL C C   
13562 O O   . VAL C 558 ? 0.4477 0.2489 0.1938 -0.0815 0.0789  -0.0845 550 VAL C O   
13563 C CB  . VAL C 558 ? 0.4828 0.2879 0.2518 -0.0865 0.0777  -0.0987 550 VAL C CB  
13564 C CG1 . VAL C 558 ? 0.5344 0.3489 0.2988 -0.0840 0.0619  -0.1000 550 VAL C CG1 
13565 C CG2 . VAL C 558 ? 0.4193 0.2314 0.2070 -0.0883 0.0829  -0.0934 550 VAL C CG2 
13566 N N   . ILE C 559 ? 0.4358 0.2320 0.2004 -0.0841 0.1008  -0.0829 551 ILE C N   
13567 C CA  . ILE C 559 ? 0.4214 0.2224 0.1913 -0.0834 0.1030  -0.0759 551 ILE C CA  
13568 C C   . ILE C 559 ? 0.3966 0.2092 0.1859 -0.0837 0.0997  -0.0741 551 ILE C C   
13569 O O   . ILE C 559 ? 0.3910 0.2036 0.1941 -0.0838 0.1068  -0.0756 551 ILE C O   
13570 C CB  . ILE C 559 ? 0.4273 0.2220 0.1997 -0.0826 0.1180  -0.0735 551 ILE C CB  
13571 C CG1 . ILE C 559 ? 0.4543 0.2365 0.2069 -0.0824 0.1227  -0.0755 551 ILE C CG1 
13572 C CG2 . ILE C 559 ? 0.4121 0.2133 0.1923 -0.0818 0.1195  -0.0671 551 ILE C CG2 
13573 C CD1 . ILE C 559 ? 0.4606 0.2384 0.2185 -0.0818 0.1377  -0.0742 551 ILE C CD1 
13574 N N   . ILE C 560 ? 0.3832 0.2049 0.1733 -0.0831 0.0889  -0.0708 552 ILE C N   
13575 C CA  . ILE C 560 ? 0.4128 0.2456 0.2196 -0.0828 0.0852  -0.0685 552 ILE C CA  
13576 C C   . ILE C 560 ? 0.3694 0.2046 0.1820 -0.0807 0.0908  -0.0627 552 ILE C C   
13577 O O   . ILE C 560 ? 0.3754 0.2096 0.1779 -0.0801 0.0880  -0.0591 552 ILE C O   
13578 C CB  . ILE C 560 ? 0.3518 0.1954 0.1579 -0.0827 0.0691  -0.0688 552 ILE C CB  
13579 C CG1 . ILE C 560 ? 0.3641 0.2070 0.1661 -0.0840 0.0631  -0.0758 552 ILE C CG1 
13580 C CG2 . ILE C 560 ? 0.3379 0.1928 0.1610 -0.0824 0.0657  -0.0665 552 ILE C CG2 
13581 C CD1 . ILE C 560 ? 0.3577 0.2125 0.1608 -0.0821 0.0472  -0.0773 552 ILE C CD1 
13582 N N   . ALA C 561 ? 0.3363 0.1746 0.1660 -0.0787 0.0983  -0.0618 553 ALA C N   
13583 C CA  . ALA C 561 ? 0.3246 0.1678 0.1636 -0.0753 0.1035  -0.0571 553 ALA C CA  
13584 C C   . ALA C 561 ? 0.3014 0.1571 0.1639 -0.0707 0.0992  -0.0526 553 ALA C C   
13585 O O   . ALA C 561 ? 0.3334 0.1882 0.2025 -0.0708 0.0988  -0.0549 553 ALA C O   
13586 C CB  . ALA C 561 ? 0.3336 0.1716 0.1779 -0.0736 0.1178  -0.0571 553 ALA C CB  
13587 N N   . THR C 562 ? 0.2849 0.1519 0.1602 -0.0664 0.0956  -0.0457 554 THR C N   
13588 C CA  . THR C 562 ? 0.2635 0.1427 0.1605 -0.0603 0.0904  -0.0405 554 THR C CA  
13589 C C   . THR C 562 ? 0.2544 0.1399 0.1695 -0.0541 0.0965  -0.0367 554 THR C C   
13590 O O   . THR C 562 ? 0.2609 0.1448 0.1727 -0.0557 0.1021  -0.0368 554 THR C O   
13591 C CB  . THR C 562 ? 0.3173 0.2075 0.2140 -0.0598 0.0754  -0.0364 554 THR C CB  
13592 O OG1 . THR C 562 ? 0.2611 0.1556 0.1562 -0.0588 0.0724  -0.0323 554 THR C OG1 
13593 C CG2 . THR C 562 ? 0.2931 0.1792 0.1716 -0.0661 0.0678  -0.0417 554 THR C CG2 
13594 N N   . GLY C 563 ? 0.2308 0.1620 0.2031 -0.0039 0.0660  -0.0400 555 GLY C N   
13595 C CA  . GLY C 563 ? 0.1787 0.1149 0.1647 0.0046  0.0674  -0.0362 555 GLY C CA  
13596 C C   . GLY C 563 ? 0.1840 0.1161 0.1693 0.0059  0.0764  -0.0379 555 GLY C C   
13597 O O   . GLY C 563 ? 0.1989 0.1202 0.1763 0.0041  0.0852  -0.0426 555 GLY C O   
13598 N N   . SER C 564 ? 0.2175 0.1583 0.2111 0.0089  0.0744  -0.0341 556 SER C N   
13599 C CA  . SER C 564 ? 0.2399 0.1799 0.2369 0.0106  0.0833  -0.0350 556 SER C CA  
13600 C C   . SER C 564 ? 0.2958 0.2280 0.2755 0.0030  0.0896  -0.0392 556 SER C C   
13601 O O   . SER C 564 ? 0.2899 0.2201 0.2708 0.0039  0.0992  -0.0408 556 SER C O   
13602 C CB  . SER C 564 ? 0.1962 0.1479 0.2058 0.0140  0.0785  -0.0295 556 SER C CB  
13603 O OG  . SER C 564 ? 0.2542 0.2103 0.2563 0.0094  0.0691  -0.0268 556 SER C OG  
13604 N N   . GLU C 565 ? 0.2369 0.1646 0.2007 -0.0045 0.0846  -0.0412 557 GLU C N   
13605 C CA  . GLU C 565 ? 0.2254 0.1436 0.1698 -0.0123 0.0894  -0.0451 557 GLU C CA  
13606 C C   . GLU C 565 ? 0.2618 0.1652 0.1930 -0.0157 0.0967  -0.0514 557 GLU C C   
13607 O O   . GLU C 565 ? 0.2629 0.1556 0.1758 -0.0221 0.1018  -0.0552 557 GLU C O   
13608 C CB  . GLU C 565 ? 0.3103 0.2313 0.2432 -0.0190 0.0784  -0.0434 557 GLU C CB  
13609 C CG  . GLU C 565 ? 0.2870 0.2166 0.2240 -0.0181 0.0739  -0.0384 557 GLU C CG  
13610 C CD  . GLU C 565 ? 0.1964 0.1382 0.1542 -0.0102 0.0687  -0.0332 557 GLU C CD  
13611 O OE1 . GLU C 565 ? 0.1997 0.1470 0.1615 -0.0087 0.0589  -0.0310 557 GLU C OE1 
13612 O OE2 . GLU C 565 ? 0.2153 0.1609 0.1854 -0.0054 0.0747  -0.0316 557 GLU C OE2 
13613 N N   . VAL C 566 ? 0.2582 0.1589 0.1961 -0.0122 0.0973  -0.0525 558 VAL C N   
13614 C CA  . VAL C 566 ? 0.2757 0.1626 0.2019 -0.0158 0.1020  -0.0567 558 VAL C CA  
13615 C C   . VAL C 566 ? 0.2714 0.1529 0.1968 -0.0137 0.1109  -0.0569 558 VAL C C   
13616 O O   . VAL C 566 ? 0.2916 0.1611 0.2005 -0.0195 0.1149  -0.0602 558 VAL C O   
13617 C CB  . VAL C 566 ? 0.2645 0.1508 0.1997 -0.0122 0.0994  -0.0557 558 VAL C CB  
13618 C CG1 . VAL C 566 ? 0.3055 0.1779 0.2297 -0.0156 0.1039  -0.0587 558 VAL C CG1 
13619 C CG2 . VAL C 566 ? 0.2412 0.1329 0.1762 -0.0158 0.0903  -0.0555 558 VAL C CG2 
13620 N N   . GLY C 567 ? 0.2976 0.1881 0.2408 -0.0057 0.1139  -0.0533 559 GLY C N   
13621 C CA  . GLY C 567 ? 0.3059 0.1929 0.2505 -0.0033 0.1225  -0.0538 559 GLY C CA  
13622 C C   . GLY C 567 ? 0.3403 0.2226 0.2703 -0.0096 0.1276  -0.0559 559 GLY C C   
13623 O O   . GLY C 567 ? 0.3383 0.2100 0.2578 -0.0117 0.1346  -0.0585 559 GLY C O   
13624 N N   . LEU C 568 ? 0.3098 0.1987 0.2375 -0.0127 0.1239  -0.0546 560 LEU C N   
13625 C CA  . LEU C 568 ? 0.3268 0.2097 0.2366 -0.0201 0.1269  -0.0562 560 LEU C CA  
13626 C C   . LEU C 568 ? 0.3502 0.2172 0.2358 -0.0284 0.1256  -0.0604 560 LEU C C   
13627 O O   . LEU C 568 ? 0.3742 0.2305 0.2452 -0.0327 0.1315  -0.0625 560 LEU C O   
13628 C CB  . LEU C 568 ? 0.3335 0.2252 0.2427 -0.0225 0.1209  -0.0538 560 LEU C CB  
13629 C CG  . LEU C 568 ? 0.3595 0.2460 0.2494 -0.0304 0.1214  -0.0541 560 LEU C CG  
13630 C CD1 . LEU C 568 ? 0.4224 0.3082 0.3159 -0.0293 0.1320  -0.0535 560 LEU C CD1 
13631 C CD2 . LEU C 568 ? 0.3331 0.2307 0.2274 -0.0311 0.1113  -0.0492 560 LEU C CD2 
13632 N N   . ALA C 569 ? 0.3541 0.2193 0.2356 -0.0309 0.1179  -0.0617 561 ALA C N   
13633 C CA  . ALA C 569 ? 0.3312 0.1826 0.1910 -0.0396 0.1149  -0.0654 561 ALA C CA  
13634 C C   . ALA C 569 ? 0.3729 0.2117 0.2276 -0.0390 0.1229  -0.0677 561 ALA C C   
13635 O O   . ALA C 569 ? 0.4327 0.2580 0.2675 -0.0457 0.1251  -0.0704 561 ALA C O   
13636 C CB  . ALA C 569 ? 0.3210 0.1756 0.1814 -0.0422 0.1051  -0.0662 561 ALA C CB  
13637 N N   . VAL C 570 ? 0.3644 0.2064 0.2357 -0.0310 0.1268  -0.0666 562 VAL C N   
13638 C CA  . VAL C 570 ? 0.3922 0.2218 0.2584 -0.0297 0.1342  -0.0687 562 VAL C CA  
13639 C C   . VAL C 570 ? 0.4825 0.3077 0.3446 -0.0286 0.1438  -0.0693 562 VAL C C   
13640 O O   . VAL C 570 ? 0.4958 0.3059 0.3417 -0.0321 0.1494  -0.0723 562 VAL C O   
13641 C CB  . VAL C 570 ? 0.4090 0.2434 0.2934 -0.0210 0.1347  -0.0668 562 VAL C CB  
13642 C CG1 . VAL C 570 ? 0.4403 0.2624 0.3202 -0.0183 0.1429  -0.0687 562 VAL C CG1 
13643 C CG2 . VAL C 570 ? 0.3692 0.2040 0.2534 -0.0237 0.1265  -0.0669 562 VAL C CG2 
13644 N N   . GLU C 571 ? 0.3902 0.2282 0.2665 -0.0240 0.1461  -0.0665 563 GLU C N   
13645 C CA  . GLU C 571 ? 0.4013 0.2363 0.2744 -0.0236 0.1556  -0.0671 563 GLU C CA  
13646 C C   . GLU C 571 ? 0.4426 0.2649 0.2897 -0.0337 0.1557  -0.0695 563 GLU C C   
13647 O O   . GLU C 571 ? 0.4862 0.2960 0.3204 -0.0358 0.1638  -0.0719 563 GLU C O   
13648 C CB  . GLU C 571 ? 0.3917 0.2440 0.2854 -0.0181 0.1570  -0.0634 563 GLU C CB  
13649 N N   . ALA C 572 ? 0.4404 0.2649 0.2787 -0.0399 0.1464  -0.0688 564 ALA C N   
13650 C CA  . ALA C 572 ? 0.4670 0.2788 0.2792 -0.0498 0.1439  -0.0706 564 ALA C CA  
13651 C C   . ALA C 572 ? 0.4603 0.2544 0.2538 -0.0550 0.1441  -0.0742 564 ALA C C   
13652 O O   . ALA C 572 ? 0.5313 0.3107 0.3045 -0.0607 0.1480  -0.0762 564 ALA C O   
13653 C CB  . ALA C 572 ? 0.4522 0.2711 0.2600 -0.0546 0.1319  -0.0688 564 ALA C CB  
13654 N N   . GLN C 573 ? 0.4281 0.2225 0.2272 -0.0536 0.1400  -0.0751 565 GLN C N   
13655 C CA  . GLN C 573 ? 0.4504 0.2279 0.2326 -0.0585 0.1404  -0.0783 565 GLN C CA  
13656 C C   . GLN C 573 ? 0.4733 0.2380 0.2492 -0.0559 0.1527  -0.0803 565 GLN C C   
13657 O O   . GLN C 573 ? 0.5449 0.2920 0.2983 -0.0624 0.1547  -0.0829 565 GLN C O   
13658 C CB  . GLN C 573 ? 0.4377 0.2188 0.2306 -0.0561 0.1359  -0.0784 565 GLN C CB  
13659 C CG  . GLN C 573 ? 0.4894 0.2530 0.2666 -0.0606 0.1372  -0.0816 565 GLN C CG  
13660 C CD  . GLN C 573 ? 0.4877 0.2547 0.2771 -0.0573 0.1345  -0.0813 565 GLN C CD  
13661 O OE1 . GLN C 573 ? 0.4878 0.2642 0.2970 -0.0480 0.1378  -0.0792 565 GLN C OE1 
13662 N NE2 . GLN C 573 ? 0.4577 0.2173 0.2353 -0.0651 0.1279  -0.0832 565 GLN C NE2 
13663 N N   . LYS C 574 ? 0.4720 0.2451 0.2672 -0.0463 0.1608  -0.0789 566 LYS C N   
13664 C CA  . LYS C 574 ? 0.4858 0.2482 0.2769 -0.0428 0.1728  -0.0809 566 LYS C CA  
13665 C C   . LYS C 574 ? 0.5061 0.2602 0.2805 -0.0481 0.1783  -0.0819 566 LYS C C   
13666 O O   . LYS C 574 ? 0.5396 0.2758 0.2949 -0.0515 0.1847  -0.0848 566 LYS C O   
13667 C CB  . LYS C 574 ? 0.5415 0.3177 0.3593 -0.0312 0.1788  -0.0788 566 LYS C CB  
13668 N N   . VAL C 575 ? 0.5273 0.2932 0.3076 -0.0491 0.1758  -0.0794 567 VAL C N   
13669 C CA  . VAL C 575 ? 0.5967 0.3543 0.3603 -0.0547 0.1806  -0.0800 567 VAL C CA  
13670 C C   . VAL C 575 ? 0.6373 0.3759 0.3707 -0.0654 0.1750  -0.0821 567 VAL C C   
13671 O O   . VAL C 575 ? 0.5910 0.3126 0.3045 -0.0695 0.1818  -0.0844 567 VAL C O   
13672 C CB  . VAL C 575 ? 0.5629 0.3361 0.3368 -0.0548 0.1773  -0.0765 567 VAL C CB  
13673 C CG1 . VAL C 575 ? 0.5782 0.3406 0.3312 -0.0621 0.1807  -0.0769 567 VAL C CG1 
13674 C CG2 . VAL C 575 ? 0.5261 0.3172 0.3292 -0.0448 0.1836  -0.0742 567 VAL C CG2 
13675 N N   . LEU C 576 ? 0.5890 0.3303 0.3187 -0.0700 0.1622  -0.0815 568 LEU C N   
13676 C CA  . LEU C 576 ? 0.5516 0.2767 0.2544 -0.0803 0.1549  -0.0831 568 LEU C CA  
13677 C C   . LEU C 576 ? 0.6242 0.3305 0.3129 -0.0817 0.1611  -0.0866 568 LEU C C   
13678 O O   . LEU C 576 ? 0.6866 0.3744 0.3508 -0.0883 0.1633  -0.0884 568 LEU C O   
13679 C CB  . LEU C 576 ? 0.5298 0.2642 0.2356 -0.0840 0.1400  -0.0818 568 LEU C CB  
13680 C CG  . LEU C 576 ? 0.5740 0.3210 0.2831 -0.0858 0.1312  -0.0785 568 LEU C CG  
13681 C CD1 . LEU C 576 ? 0.4893 0.2501 0.2097 -0.0860 0.1184  -0.0772 568 LEU C CD1 
13682 C CD2 . LEU C 576 ? 0.6236 0.3576 0.3070 -0.0947 0.1268  -0.0782 568 LEU C CD2 
13683 N N   . ALA C 577 ? 0.5824 0.2919 0.2852 -0.0755 0.1637  -0.0874 569 ALA C N   
13684 C CA  . ALA C 577 ? 0.6346 0.3257 0.3241 -0.0763 0.1696  -0.0906 569 ALA C CA  
13685 C C   . ALA C 577 ? 0.6664 0.3447 0.3459 -0.0743 0.1832  -0.0924 569 ALA C C   
13686 O O   . ALA C 577 ? 0.6774 0.3346 0.3332 -0.0795 0.1866  -0.0952 569 ALA C O   
13687 C CB  . ALA C 577 ? 0.6431 0.3408 0.3515 -0.0686 0.1710  -0.0906 569 ALA C CB  
13688 N N   . GLY C 578 ? 0.6596 0.3504 0.3566 -0.0670 0.1909  -0.0909 570 GLY C N   
13689 C CA  . GLY C 578 ? 0.6940 0.3746 0.3832 -0.0651 0.2043  -0.0926 570 GLY C CA  
13690 C C   . GLY C 578 ? 0.7795 0.4445 0.4411 -0.0748 0.2040  -0.0935 570 GLY C C   
13691 O O   . GLY C 578 ? 0.8282 0.4791 0.4766 -0.0750 0.2152  -0.0957 570 GLY C O   
13692 N N   . GLN C 579 ? 0.8027 0.4696 0.4549 -0.0827 0.1914  -0.0918 571 GLN C N   
13693 C CA  . GLN C 579 ? 0.8172 0.4695 0.4426 -0.0924 0.1885  -0.0919 571 GLN C CA  
13694 C C   . GLN C 579 ? 0.8076 0.4429 0.4084 -0.1015 0.1788  -0.0933 571 GLN C C   
13695 O O   . GLN C 579 ? 0.8520 0.4776 0.4318 -0.1102 0.1716  -0.0926 571 GLN C O   
13696 C CB  . GLN C 579 ? 0.8382 0.5053 0.4704 -0.0944 0.1807  -0.0883 571 GLN C CB  
13697 C CG  . GLN C 579 ? 0.8648 0.5500 0.5219 -0.0861 0.1891  -0.0865 571 GLN C CG  
13698 C CD  . GLN C 579 ? 0.8750 0.5738 0.5376 -0.0884 0.1810  -0.0828 571 GLN C CD  
13699 O OE1 . GLN C 579 ? 0.8263 0.5213 0.4743 -0.0957 0.1687  -0.0814 571 GLN C OE1 
13700 N NE2 . GLN C 579 ? 0.9145 0.6293 0.5982 -0.0822 0.1875  -0.0809 571 GLN C NE2 
13701 N N   . GLY C 580 ? 0.8018 0.4334 0.4051 -0.1000 0.1778  -0.0952 572 GLY C N   
13702 C CA  . GLY C 580 ? 0.8220 0.4387 0.4039 -0.1088 0.1686  -0.0965 572 GLY C CA  
13703 C C   . GLY C 580 ? 0.8344 0.4641 0.4217 -0.1136 0.1518  -0.0943 572 GLY C C   
13704 O O   . GLY C 580 ? 0.7719 0.3907 0.3401 -0.1225 0.1420  -0.0948 572 GLY C O   
13705 N N   . ILE C 581 ? 0.7865 0.4394 0.3997 -0.1079 0.1480  -0.0919 573 ILE C N   
13706 C CA  . ILE C 581 ? 0.7337 0.4010 0.3542 -0.1114 0.1326  -0.0897 573 ILE C CA  
13707 C C   . ILE C 581 ? 0.6856 0.3660 0.3286 -0.1057 0.1314  -0.0899 573 ILE C C   
13708 O O   . ILE C 581 ? 0.6433 0.3378 0.3090 -0.0967 0.1374  -0.0887 573 ILE C O   
13709 C CB  . ILE C 581 ? 0.6962 0.3781 0.3251 -0.1103 0.1280  -0.0863 573 ILE C CB  
13710 C CG1 . ILE C 581 ? 0.7103 0.3773 0.3156 -0.1162 0.1299  -0.0859 573 ILE C CG1 
13711 C CG2 . ILE C 581 ? 0.6914 0.3880 0.3278 -0.1134 0.1118  -0.0842 573 ILE C CG2 
13712 C CD1 . ILE C 581 ? 0.6787 0.3576 0.2898 -0.1154 0.1262  -0.0824 573 ILE C CD1 
13713 N N   . ALA C 582 ? 0.6507 0.3264 0.2875 -0.1111 0.1235  -0.0912 574 ALA C N   
13714 C CA  . ALA C 582 ? 0.6193 0.3045 0.2744 -0.1069 0.1223  -0.0916 574 ALA C CA  
13715 C C   . ALA C 582 ? 0.5895 0.2948 0.2596 -0.1081 0.1094  -0.0893 574 ALA C C   
13716 O O   . ALA C 582 ? 0.6267 0.3322 0.2869 -0.1163 0.0972  -0.0890 574 ALA C O   
13717 C CB  . ALA C 582 ? 0.7199 0.3884 0.3600 -0.1126 0.1215  -0.0944 574 ALA C CB  
13718 N N   . VAL C 583 ? 0.5514 0.2736 0.2459 -0.0996 0.1118  -0.0876 575 VAL C N   
13719 C CA  . VAL C 583 ? 0.5086 0.2496 0.2189 -0.0995 0.1009  -0.0857 575 VAL C CA  
13720 C C   . VAL C 583 ? 0.4898 0.2386 0.2199 -0.0932 0.1038  -0.0858 575 VAL C C   
13721 O O   . VAL C 583 ? 0.5027 0.2464 0.2386 -0.0864 0.1144  -0.0863 575 VAL C O   
13722 C CB  . VAL C 583 ? 0.5609 0.3158 0.2803 -0.0958 0.0989  -0.0827 575 VAL C CB  
13723 C CG1 . VAL C 583 ? 0.5114 0.2563 0.2098 -0.1017 0.0971  -0.0823 575 VAL C CG1 
13724 C CG2 . VAL C 583 ? 0.5283 0.2905 0.2660 -0.0850 0.1104  -0.0816 575 VAL C CG2 
13725 N N   . ARG C 584 ? 0.4724 0.2335 0.2126 -0.0955 0.0936  -0.0851 576 ARG C N   
13726 C CA  . ARG C 584 ? 0.4528 0.2227 0.2121 -0.0903 0.0945  -0.0847 576 ARG C CA  
13727 C C   . ARG C 584 ? 0.4234 0.2119 0.2025 -0.0833 0.0925  -0.0819 576 ARG C C   
13728 O O   . ARG C 584 ? 0.4295 0.2254 0.2063 -0.0853 0.0862  -0.0806 576 ARG C O   
13729 C CB  . ARG C 584 ? 0.4562 0.2263 0.2127 -0.0988 0.0848  -0.0860 576 ARG C CB  
13730 C CG  . ARG C 584 ? 0.5750 0.3597 0.3514 -0.0965 0.0803  -0.0850 576 ARG C CG  
13731 C CD  . ARG C 584 ? 0.4767 0.2648 0.2500 -0.1071 0.0686  -0.0860 576 ARG C CD  
13732 N NE  . ARG C 584 ? 0.4912 0.2640 0.2522 -0.1131 0.0708  -0.0883 576 ARG C NE  
13733 C CZ  . ARG C 584 ? 0.5160 0.2915 0.2789 -0.1210 0.0635  -0.0891 576 ARG C CZ  
13734 N NH1 . ARG C 584 ? 0.4603 0.2541 0.2385 -0.1234 0.0540  -0.0878 576 ARG C NH1 
13735 N NH2 . ARG C 584 ? 0.5110 0.2712 0.2613 -0.1267 0.0658  -0.0911 576 ARG C NH2 
13736 N N   . VAL C 585 ? 0.4211 0.2162 0.2186 -0.0746 0.0977  -0.0806 577 VAL C N   
13737 C CA  . VAL C 585 ? 0.3788 0.1908 0.1957 -0.0675 0.0958  -0.0778 577 VAL C CA  
13738 C C   . VAL C 585 ? 0.3636 0.1832 0.1934 -0.0671 0.0907  -0.0775 577 VAL C C   
13739 O O   . VAL C 585 ? 0.4305 0.2441 0.2641 -0.0647 0.0951  -0.0777 577 VAL C O   
13740 C CB  . VAL C 585 ? 0.3743 0.1893 0.2041 -0.0566 0.1058  -0.0755 577 VAL C CB  
13741 C CG1 . VAL C 585 ? 0.3546 0.1869 0.2043 -0.0497 0.1027  -0.0723 577 VAL C CG1 
13742 C CG2 . VAL C 585 ? 0.4102 0.2183 0.2280 -0.0577 0.1116  -0.0759 577 VAL C CG2 
13743 N N   . VAL C 586 ? 0.3484 0.1805 0.1843 -0.0695 0.0815  -0.0768 578 VAL C N   
13744 C CA  . VAL C 586 ? 0.3333 0.1741 0.1823 -0.0696 0.0766  -0.0766 578 VAL C CA  
13745 C C   . VAL C 586 ? 0.3082 0.1633 0.1769 -0.0592 0.0771  -0.0725 578 VAL C C   
13746 O O   . VAL C 586 ? 0.2986 0.1641 0.1708 -0.0567 0.0732  -0.0693 578 VAL C O   
13747 C CB  . VAL C 586 ? 0.3349 0.1821 0.1794 -0.0803 0.0640  -0.0778 578 VAL C CB  
13748 C CG1 . VAL C 586 ? 0.3113 0.1779 0.1785 -0.0773 0.0571  -0.0732 578 VAL C CG1 
13749 C CG2 . VAL C 586 ? 0.3586 0.1932 0.1878 -0.0899 0.0628  -0.0804 578 VAL C CG2 
13750 N N   . SER C 587 ? 0.2980 0.1545 0.1802 -0.0527 0.0809  -0.0710 579 SER C N   
13751 C CA  . SER C 587 ? 0.2732 0.1458 0.1762 -0.0430 0.0785  -0.0651 579 SER C CA  
13752 C C   . SER C 587 ? 0.2763 0.1632 0.1897 -0.0458 0.0683  -0.0620 579 SER C C   
13753 O O   . SER C 587 ? 0.3218 0.2043 0.2331 -0.0514 0.0677  -0.0640 579 SER C O   
13754 C CB  . SER C 587 ? 0.3147 0.1805 0.2262 -0.0338 0.0874  -0.0648 579 SER C CB  
13755 O OG  . SER C 587 ? 0.2594 0.1398 0.1896 -0.0251 0.0837  -0.0590 579 SER C OG  
13756 N N   . MET C 588 ? 0.2857 0.1892 0.2100 -0.0421 0.0607  -0.0573 580 MET C N   
13757 C CA  . MET C 588 ? 0.2705 0.1889 0.2057 -0.0436 0.0515  -0.0543 580 MET C CA  
13758 C C   . MET C 588 ? 0.2619 0.1909 0.2139 -0.0333 0.0506  -0.0490 580 MET C C   
13759 O O   . MET C 588 ? 0.2046 0.1460 0.1634 -0.0298 0.0438  -0.0452 580 MET C O   
13760 C CB  . MET C 588 ? 0.2298 0.1573 0.1603 -0.0495 0.0414  -0.0538 580 MET C CB  
13761 C CG  . MET C 588 ? 0.2192 0.1627 0.1616 -0.0517 0.0321  -0.0514 580 MET C CG  
13762 S SD  . MET C 588 ? 0.2432 0.1959 0.1796 -0.0596 0.0192  -0.0517 580 MET C SD  
13763 C CE  . MET C 588 ? 0.2521 0.1880 0.1693 -0.0727 0.0214  -0.0583 580 MET C CE  
13764 N N   . PRO C 589 ? 0.2512 0.1740 0.2088 -0.0281 0.0569  -0.0486 581 PRO C N   
13765 C CA  . PRO C 589 ? 0.1893 0.1200 0.1608 -0.0183 0.0556  -0.0435 581 PRO C CA  
13766 C C   . PRO C 589 ? 0.1761 0.1218 0.1572 -0.0180 0.0475  -0.0400 581 PRO C C   
13767 O O   . PRO C 589 ? 0.1717 0.1253 0.1618 -0.0105 0.0441  -0.0357 581 PRO C O   
13768 C CB  . PRO C 589 ? 0.2395 0.1577 0.2117 -0.0147 0.0634  -0.0445 581 PRO C CB  
13769 C CG  . PRO C 589 ? 0.2690 0.1756 0.2294 -0.0240 0.0670  -0.0495 581 PRO C CG  
13770 C CD  . PRO C 589 ? 0.2558 0.1619 0.2054 -0.0307 0.0652  -0.0526 581 PRO C CD  
13771 N N   . SER C 590 ? 0.1858 0.1359 0.1657 -0.0259 0.0441  -0.0417 582 SER C N   
13772 C CA  . SER C 590 ? 0.1938 0.1600 0.1842 -0.0251 0.0367  -0.0386 582 SER C CA  
13773 C C   . SER C 590 ? 0.1940 0.1676 0.1813 -0.0345 0.0302  -0.0409 582 SER C C   
13774 O O   . SER C 590 ? 0.1852 0.1557 0.1697 -0.0427 0.0318  -0.0440 582 SER C O   
13775 C CB  . SER C 590 ? 0.1648 0.1315 0.1628 -0.0230 0.0399  -0.0371 582 SER C CB  
13776 O OG  . SER C 590 ? 0.1544 0.1372 0.1628 -0.0219 0.0338  -0.0343 582 SER C OG  
13777 N N   . THR C 591 ? 0.1865 0.1695 0.1741 -0.0335 0.0224  -0.0392 583 THR C N   
13778 C CA  . THR C 591 ? 0.2015 0.1941 0.1888 -0.0411 0.0140  -0.0405 583 THR C CA  
13779 C C   . THR C 591 ? 0.1794 0.1853 0.1806 -0.0424 0.0119  -0.0394 583 THR C C   
13780 O O   . THR C 591 ? 0.1853 0.1956 0.1871 -0.0515 0.0089  -0.0419 583 THR C O   
13781 C CB  . THR C 591 ? 0.2162 0.2167 0.2025 -0.0379 0.0052  -0.0379 583 THR C CB  
13782 O OG1 . THR C 591 ? 0.2103 0.2212 0.2090 -0.0283 0.0028  -0.0332 583 THR C OG1 
13783 C CG2 . THR C 591 ? 0.1996 0.1873 0.1718 -0.0373 0.0080  -0.0387 583 THR C CG2 
13784 N N   . SER C 592 ? 0.1606 0.1730 0.1730 -0.0337 0.0135  -0.0356 584 SER C N   
13785 C CA  . SER C 592 ? 0.2114 0.2369 0.2374 -0.0339 0.0128  -0.0343 584 SER C CA  
13786 C C   . SER C 592 ? 0.2116 0.2314 0.2364 -0.0429 0.0189  -0.0375 584 SER C C   
13787 O O   . SER C 592 ? 0.2197 0.2512 0.2526 -0.0499 0.0160  -0.0385 584 SER C O   
13788 C CB  . SER C 592 ? 0.1492 0.1761 0.1823 -0.0230 0.0160  -0.0302 584 SER C CB  
13789 O OG  . SER C 592 ? 0.1464 0.1699 0.1754 -0.0151 0.0132  -0.0278 584 SER C OG  
13790 N N   . VAL C 593 ? 0.1668 0.1688 0.1822 -0.0429 0.0272  -0.0390 585 VAL C N   
13791 C CA  . VAL C 593 ? 0.2119 0.2051 0.2241 -0.0510 0.0335  -0.0419 585 VAL C CA  
13792 C C   . VAL C 593 ? 0.1942 0.1831 0.1971 -0.0629 0.0307  -0.0465 585 VAL C C   
13793 O O   . VAL C 593 ? 0.2174 0.2095 0.2229 -0.0726 0.0305  -0.0484 585 VAL C O   
13794 C CB  . VAL C 593 ? 0.2233 0.1971 0.2274 -0.0460 0.0427  -0.0419 585 VAL C CB  
13795 C CG1 . VAL C 593 ? 0.2482 0.2091 0.2454 -0.0550 0.0489  -0.0452 585 VAL C CG1 
13796 C CG2 . VAL C 593 ? 0.2145 0.1920 0.2271 -0.0355 0.0446  -0.0373 585 VAL C CG2 
13797 N N   . PHE C 594 ? 0.1999 0.1808 0.1910 -0.0630 0.0285  -0.0482 586 PHE C N   
13798 C CA  . PHE C 594 ? 0.2449 0.2191 0.2239 -0.0744 0.0255  -0.0527 586 PHE C CA  
13799 C C   . PHE C 594 ? 0.2307 0.2234 0.2193 -0.0819 0.0156  -0.0526 586 PHE C C   
13800 O O   . PHE C 594 ? 0.2484 0.2389 0.2337 -0.0934 0.0141  -0.0559 586 PHE C O   
13801 C CB  . PHE C 594 ? 0.2233 0.1877 0.1882 -0.0724 0.0244  -0.0540 586 PHE C CB  
13802 C CG  . PHE C 594 ? 0.3111 0.2660 0.2603 -0.0839 0.0212  -0.0587 586 PHE C CG  
13803 C CD1 . PHE C 594 ? 0.2748 0.2125 0.2122 -0.0918 0.0274  -0.0632 586 PHE C CD1 
13804 C CD2 . PHE C 594 ? 0.2924 0.2538 0.2369 -0.0869 0.0114  -0.0587 586 PHE C CD2 
13805 C CE1 . PHE C 594 ? 0.3216 0.2485 0.2422 -0.1027 0.0242  -0.0677 586 PHE C CE1 
13806 C CE2 . PHE C 594 ? 0.3085 0.2594 0.2363 -0.0978 0.0078  -0.0630 586 PHE C CE2 
13807 C CZ  . PHE C 594 ? 0.3320 0.2655 0.2477 -0.1059 0.0142  -0.0676 586 PHE C CZ  
13808 N N   . ASP C 595 ? 0.2445 0.2553 0.2456 -0.0753 0.0083  -0.0489 587 ASP C N   
13809 C CA  . ASP C 595 ? 0.1999 0.2306 0.2127 -0.0802 -0.0020 -0.0483 587 ASP C CA  
13810 C C   . ASP C 595 ? 0.2452 0.2864 0.2719 -0.0869 0.0003  -0.0487 587 ASP C C   
13811 O O   . ASP C 595 ? 0.2591 0.3145 0.2942 -0.0948 -0.0077 -0.0496 587 ASP C O   
13812 C CB  . ASP C 595 ? 0.1892 0.2357 0.2135 -0.0693 -0.0083 -0.0438 587 ASP C CB  
13813 C CG  . ASP C 595 ? 0.2803 0.3198 0.2916 -0.0656 -0.0135 -0.0432 587 ASP C CG  
13814 O OD1 . ASP C 595 ? 0.3621 0.3882 0.3568 -0.0728 -0.0143 -0.0466 587 ASP C OD1 
13815 O OD2 . ASP C 595 ? 0.3190 0.3655 0.3358 -0.0557 -0.0166 -0.0395 587 ASP C OD2 
13816 N N   . ARG C 596 ? 0.2622 0.2968 0.2915 -0.0841 0.0106  -0.0479 588 ARG C N   
13817 C CA  . ARG C 596 ? 0.2746 0.3168 0.3154 -0.0907 0.0147  -0.0481 588 ARG C CA  
13818 C C   . ARG C 596 ? 0.3282 0.3544 0.3569 -0.1038 0.0188  -0.0525 588 ARG C C   
13819 O O   . ARG C 596 ? 0.2704 0.3024 0.3077 -0.1117 0.0217  -0.0529 588 ARG C O   
13820 C CB  . ARG C 596 ? 0.3664 0.4067 0.4133 -0.0817 0.0240  -0.0449 588 ARG C CB  
13821 C CG  . ARG C 596 ? 0.4025 0.4567 0.4608 -0.0690 0.0212  -0.0406 588 ARG C CG  
13822 C CD  . ARG C 596 ? 0.4075 0.4642 0.4745 -0.0642 0.0295  -0.0379 588 ARG C CD  
13823 N NE  . ARG C 596 ? 0.3757 0.4103 0.4298 -0.0599 0.0383  -0.0375 588 ARG C NE  
13824 C CZ  . ARG C 596 ? 0.2732 0.3000 0.3223 -0.0483 0.0391  -0.0351 588 ARG C CZ  
13825 N NH1 . ARG C 596 ? 0.2404 0.2782 0.2946 -0.0407 0.0320  -0.0329 588 ARG C NH1 
13826 N NH2 . ARG C 596 ? 0.3369 0.3446 0.3759 -0.0445 0.0463  -0.0347 588 ARG C NH2 
13827 N N   . GLN C 597 ? 0.2550 0.2604 0.2636 -0.1062 0.0200  -0.0557 589 GLN C N   
13828 C CA  . GLN C 597 ? 0.2537 0.2407 0.2482 -0.1181 0.0241  -0.0601 589 GLN C CA  
13829 C C   . GLN C 597 ? 0.3065 0.3034 0.3034 -0.1321 0.0147  -0.0628 589 GLN C C   
13830 O O   . GLN C 597 ? 0.3229 0.3348 0.3255 -0.1319 0.0041  -0.0620 589 GLN C O   
13831 C CB  . GLN C 597 ? 0.2658 0.2273 0.2378 -0.1156 0.0287  -0.0631 589 GLN C CB  
13832 C CG  . GLN C 597 ? 0.2546 0.2078 0.2257 -0.1016 0.0366  -0.0604 589 GLN C CG  
13833 C CD  . GLN C 597 ? 0.2883 0.2376 0.2655 -0.0992 0.0450  -0.0586 589 GLN C CD  
13834 O OE1 . GLN C 597 ? 0.3062 0.2405 0.2747 -0.1071 0.0504  -0.0612 589 GLN C OE1 
13835 N NE2 . GLN C 597 ? 0.2786 0.2397 0.2691 -0.0886 0.0459  -0.0539 589 GLN C NE2 
13836 N N   . ASP C 598 ? 0.3310 0.3183 0.3226 -0.1447 0.0179  -0.0658 590 ASP C N   
13837 C CA  . ASP C 598 ? 0.3863 0.3824 0.3802 -0.1594 0.0084  -0.0683 590 ASP C CA  
13838 C C   . ASP C 598 ? 0.3822 0.3676 0.3576 -0.1624 0.0002  -0.0714 590 ASP C C   
13839 O O   . ASP C 598 ? 0.3281 0.2942 0.2855 -0.1557 0.0047  -0.0726 590 ASP C O   
13840 C CB  . ASP C 598 ? 0.5277 0.5117 0.5162 -0.1714 0.0138  -0.0705 590 ASP C CB  
13841 C CG  . ASP C 598 ? 0.6639 0.6143 0.6255 -0.1704 0.0223  -0.0733 590 ASP C CG  
13842 O OD1 . ASP C 598 ? 0.6225 0.5588 0.5656 -0.1714 0.0185  -0.0758 590 ASP C OD1 
13843 O OD2 . ASP C 598 ? 0.7257 0.6636 0.6845 -0.1681 0.0329  -0.0728 590 ASP C OD2 
13844 N N   . ALA C 599 ? 0.3924 0.3911 0.3731 -0.1701 -0.0119 -0.0714 591 ALA C N   
13845 C CA  . ALA C 599 ? 0.4311 0.4225 0.3959 -0.1703 -0.0213 -0.0726 591 ALA C CA  
13846 C C   . ALA C 599 ? 0.4115 0.3715 0.3474 -0.1734 -0.0156 -0.0761 591 ALA C C   
13847 O O   . ALA C 599 ? 0.4149 0.3614 0.3326 -0.1698 -0.0167 -0.0773 591 ALA C O   
13848 C CB  . ALA C 599 ? 0.4995 0.5106 0.4770 -0.1762 -0.0355 -0.0711 591 ALA C CB  
13849 N N   . ALA C 600 ? 0.4203 0.3685 0.3514 -0.1798 -0.0091 -0.0774 592 ALA C N   
13850 C CA  . ALA C 600 ? 0.4618 0.3800 0.3659 -0.1817 -0.0026 -0.0805 592 ALA C CA  
13851 C C   . ALA C 600 ? 0.4342 0.3352 0.3258 -0.1711 0.0082  -0.0814 592 ALA C C   
13852 O O   . ALA C 600 ? 0.4645 0.3473 0.3352 -0.1686 0.0101  -0.0833 592 ALA C O   
13853 C CB  . ALA C 600 ? 0.4638 0.3734 0.3668 -0.1892 0.0029  -0.0812 592 ALA C CB  
13854 N N   . TYR C 601 ? 0.4065 0.3129 0.3110 -0.1643 0.0158  -0.0800 593 TYR C N   
13855 C CA  . TYR C 601 ? 0.3759 0.2669 0.2709 -0.1534 0.0257  -0.0806 593 TYR C CA  
13856 C C   . TYR C 601 ? 0.3792 0.2748 0.2709 -0.1475 0.0209  -0.0805 593 TYR C C   
13857 O O   . TYR C 601 ? 0.4368 0.3153 0.3122 -0.1416 0.0266  -0.0819 593 TYR C O   
13858 C CB  . TYR C 601 ? 0.3605 0.2566 0.2707 -0.1471 0.0337  -0.0786 593 TYR C CB  
13859 C CG  . TYR C 601 ? 0.3733 0.2541 0.2755 -0.1341 0.0433  -0.0785 593 TYR C CG  
13860 C CD1 . TYR C 601 ? 0.4236 0.2802 0.3097 -0.1315 0.0527  -0.0801 593 TYR C CD1 
13861 C CD2 . TYR C 601 ? 0.3524 0.2465 0.2649 -0.1214 0.0420  -0.0745 593 TYR C CD2 
13862 C CE1 . TYR C 601 ? 0.3995 0.2444 0.2807 -0.1193 0.0609  -0.0797 593 TYR C CE1 
13863 C CE2 . TYR C 601 ? 0.3416 0.2241 0.2490 -0.1096 0.0501  -0.0738 593 TYR C CE2 
13864 C CZ  . TYR C 601 ? 0.3504 0.2076 0.2423 -0.1095 0.0598  -0.0773 593 TYR C CZ  
13865 O OH  . TYR C 601 ? 0.3338 0.1812 0.2229 -0.0973 0.0675  -0.0766 593 TYR C OH  
13866 N N   . GLN C 602 ? 0.3446 0.2639 0.2522 -0.1482 0.0107  -0.0783 594 GLN C N   
13867 C CA  . GLN C 602 ? 0.3497 0.2742 0.2542 -0.1405 0.0055  -0.0766 594 GLN C CA  
13868 C C   . GLN C 602 ? 0.3940 0.3021 0.2747 -0.1462 0.0016  -0.0795 594 GLN C C   
13869 O O   . GLN C 602 ? 0.3699 0.2685 0.2378 -0.1403 0.0038  -0.0798 594 GLN C O   
13870 C CB  . GLN C 602 ? 0.3538 0.3075 0.2804 -0.1378 -0.0057 -0.0721 594 GLN C CB  
13871 C CG  . GLN C 602 ? 0.3512 0.3222 0.3015 -0.1282 -0.0013 -0.0675 594 GLN C CG  
13872 C CD  . GLN C 602 ? 0.3825 0.3785 0.3507 -0.1215 -0.0108 -0.0630 594 GLN C CD  
13873 O OE1 . GLN C 602 ? 0.4482 0.4451 0.4091 -0.1192 -0.0184 -0.0624 594 GLN C OE1 
13874 N NE2 . GLN C 602 ? 0.3492 0.3645 0.3397 -0.1180 -0.0103 -0.0598 594 GLN C NE2 
13875 N N   . ALA C 603 ? 0.4142 0.3196 0.2896 -0.1557 -0.0038 -0.0804 595 ALA C N   
13876 C CA  . ALA C 603 ? 0.4481 0.3378 0.3011 -0.1595 -0.0072 -0.0819 595 ALA C CA  
13877 C C   . ALA C 603 ? 0.4535 0.3161 0.2855 -0.1569 0.0058  -0.0845 595 ALA C C   
13878 O O   . ALA C 603 ? 0.4367 0.2849 0.2494 -0.1557 0.0070  -0.0855 595 ALA C O   
13879 C CB  . ALA C 603 ? 0.4936 0.3891 0.3485 -0.1705 -0.0176 -0.0821 595 ALA C CB  
13880 N N   . ALA C 604 ? 0.4310 0.2862 0.2663 -0.1555 0.0157  -0.0853 596 ALA C N   
13881 C CA  . ALA C 604 ? 0.4938 0.3249 0.3117 -0.1509 0.0283  -0.0872 596 ALA C CA  
13882 C C   . ALA C 604 ? 0.4650 0.2930 0.2812 -0.1393 0.0354  -0.0866 596 ALA C C   
13883 O O   . ALA C 604 ? 0.4390 0.2501 0.2388 -0.1357 0.0425  -0.0878 596 ALA C O   
13884 C CB  . ALA C 604 ? 0.4927 0.3175 0.3157 -0.1507 0.0365  -0.0874 596 ALA C CB  
13885 N N   . VAL C 605 ? 0.4575 0.3022 0.2912 -0.1336 0.0336  -0.0847 597 VAL C N   
13886 C CA  . VAL C 605 ? 0.4071 0.2506 0.2410 -0.1228 0.0396  -0.0839 597 VAL C CA  
13887 C C   . VAL C 605 ? 0.3842 0.2300 0.2082 -0.1238 0.0326  -0.0834 597 VAL C C   
13888 O O   . VAL C 605 ? 0.3992 0.2344 0.2119 -0.1183 0.0392  -0.0835 597 VAL C O   
13889 C CB  . VAL C 605 ? 0.3575 0.2163 0.2126 -0.1164 0.0403  -0.0820 597 VAL C CB  
13890 C CG1 . VAL C 605 ? 0.3637 0.2239 0.2214 -0.1042 0.0454  -0.0797 597 VAL C CG1 
13891 C CG2 . VAL C 605 ? 0.3669 0.2208 0.2297 -0.1151 0.0478  -0.0819 597 VAL C CG2 
13892 N N   . LEU C 606 ? 0.4168 0.2772 0.2459 -0.1305 0.0191  -0.0822 598 LEU C N   
13893 C CA  . LEU C 606 ? 0.4035 0.2677 0.2245 -0.1312 0.0103  -0.0808 598 LEU C CA  
13894 C C   . LEU C 606 ? 0.4603 0.3222 0.2716 -0.1413 0.0003  -0.0813 598 LEU C C   
13895 O O   . LEU C 606 ? 0.4533 0.3326 0.2769 -0.1457 -0.0123 -0.0796 598 LEU C O   
13896 C CB  . LEU C 606 ? 0.3613 0.2473 0.1996 -0.1273 0.0019  -0.0779 598 LEU C CB  
13897 C CG  . LEU C 606 ? 0.3376 0.2306 0.1902 -0.1150 0.0099  -0.0752 598 LEU C CG  
13898 C CD1 . LEU C 606 ? 0.3155 0.2324 0.1868 -0.1087 0.0001  -0.0695 598 LEU C CD1 
13899 C CD2 . LEU C 606 ? 0.3456 0.2215 0.1827 -0.1093 0.0205  -0.0766 598 LEU C CD2 
13900 N N   . PRO C 607 ? 0.4837 0.3249 0.2739 -0.1448 0.0052  -0.0834 599 PRO C N   
13901 C CA  . PRO C 607 ? 0.5159 0.3527 0.2958 -0.1549 -0.0041 -0.0842 599 PRO C CA  
13902 C C   . PRO C 607 ? 0.5538 0.4003 0.3319 -0.1568 -0.0179 -0.0819 599 PRO C C   
13903 O O   . PRO C 607 ? 0.4657 0.3108 0.2377 -0.1512 -0.0174 -0.0803 599 PRO C O   
13904 C CB  . PRO C 607 ? 0.5284 0.3388 0.2837 -0.1562 0.0061  -0.0868 599 PRO C CB  
13905 C CG  . PRO C 607 ? 0.5404 0.3444 0.2999 -0.1476 0.0209  -0.0876 599 PRO C CG  
13906 C CD  . PRO C 607 ? 0.4834 0.3045 0.2599 -0.1396 0.0201  -0.0852 599 PRO C CD  
13907 N N   . GLU C 608 ? 0.5439 0.4000 0.3279 -0.1646 -0.0304 -0.0815 600 GLU C N   
13908 C CA  . GLU C 608 ? 0.5981 0.4633 0.3814 -0.1660 -0.0447 -0.0791 600 GLU C CA  
13909 C C   . GLU C 608 ? 0.6359 0.4796 0.3912 -0.1668 -0.0431 -0.0795 600 GLU C C   
13910 O O   . GLU C 608 ? 0.6164 0.4390 0.3524 -0.1711 -0.0357 -0.0822 600 GLU C O   
13911 C CB  . GLU C 608 ? 0.5463 0.4237 0.3405 -0.1746 -0.0573 -0.0791 600 GLU C CB  
13912 N N   . GLY C 609 ? 0.6459 0.4943 0.3986 -0.1626 -0.0497 -0.0767 601 GLY C N   
13913 C CA  . GLY C 609 ? 0.6820 0.5110 0.4088 -0.1636 -0.0487 -0.0765 601 GLY C CA  
13914 C C   . GLY C 609 ? 0.6988 0.5106 0.4110 -0.1583 -0.0326 -0.0774 601 GLY C C   
13915 O O   . GLY C 609 ? 0.6971 0.4929 0.3881 -0.1590 -0.0305 -0.0770 601 GLY C O   
13916 N N   . LEU C 610 ? 0.5951 0.4095 0.3185 -0.1532 -0.0210 -0.0787 602 LEU C N   
13917 C CA  . LEU C 610 ? 0.6097 0.4110 0.3237 -0.1469 -0.0057 -0.0794 602 LEU C CA  
13918 C C   . LEU C 610 ? 0.5589 0.3724 0.2826 -0.1391 -0.0066 -0.0763 602 LEU C C   
13919 O O   . LEU C 610 ? 0.4708 0.3025 0.2158 -0.1350 -0.0097 -0.0751 602 LEU C O   
13920 C CB  . LEU C 610 ? 0.6128 0.4105 0.3346 -0.1442 0.0069  -0.0821 602 LEU C CB  
13921 C CG  . LEU C 610 ? 0.6305 0.4129 0.3432 -0.1380 0.0238  -0.0835 602 LEU C CG  
13922 C CD1 . LEU C 610 ? 0.6982 0.4575 0.3848 -0.1431 0.0283  -0.0852 602 LEU C CD1 
13923 C CD2 . LEU C 610 ? 0.5483 0.3318 0.2745 -0.1335 0.0339  -0.0852 602 LEU C CD2 
13924 N N   . PRO C 611 ? 0.6034 0.4071 0.3118 -0.1373 -0.0041 -0.0747 603 PRO C N   
13925 C CA  . PRO C 611 ? 0.5460 0.3606 0.2624 -0.1306 -0.0059 -0.0712 603 PRO C CA  
13926 C C   . PRO C 611 ? 0.4676 0.2897 0.2002 -0.1228 0.0049  -0.0718 603 PRO C C   
13927 O O   . PRO C 611 ? 0.4706 0.2829 0.2014 -0.1209 0.0184  -0.0745 603 PRO C O   
13928 C CB  . PRO C 611 ? 0.5286 0.3259 0.2224 -0.1314 -0.0011 -0.0702 603 PRO C CB  
13929 C CG  . PRO C 611 ? 0.5256 0.3073 0.2004 -0.1397 -0.0041 -0.0722 603 PRO C CG  
13930 C CD  . PRO C 611 ? 0.6143 0.3961 0.2965 -0.1423 -0.0006 -0.0757 603 PRO C CD  
13931 N N   . ARG C 612 ? 0.4286 0.2679 0.1770 -0.1177 -0.0014 -0.0689 604 ARG C N   
13932 C CA  . ARG C 612 ? 0.4201 0.2686 0.1857 -0.1106 0.0064  -0.0692 604 ARG C CA  
13933 C C   . ARG C 612 ? 0.4175 0.2687 0.1831 -0.1043 0.0090  -0.0661 604 ARG C C   
13934 O O   . ARG C 612 ? 0.4391 0.2948 0.2008 -0.1046 -0.0014 -0.0626 604 ARG C O   
13935 C CB  . ARG C 612 ? 0.4745 0.3420 0.2612 -0.1105 -0.0028 -0.0687 604 ARG C CB  
13936 C CG  . ARG C 612 ? 0.3894 0.2565 0.1773 -0.1181 -0.0075 -0.0711 604 ARG C CG  
13937 C CD  . ARG C 612 ? 0.3834 0.2722 0.1929 -0.1190 -0.0189 -0.0696 604 ARG C CD  
13938 N NE  . ARG C 612 ? 0.4213 0.3103 0.2336 -0.1268 -0.0219 -0.0718 604 ARG C NE  
13939 C CZ  . ARG C 612 ? 0.4259 0.3330 0.2552 -0.1302 -0.0329 -0.0706 604 ARG C CZ  
13940 N NH1 . ARG C 612 ? 0.3892 0.3161 0.2345 -0.1258 -0.0422 -0.0671 604 ARG C NH1 
13941 N NH2 . ARG C 612 ? 0.4852 0.3908 0.3157 -0.1379 -0.0344 -0.0727 604 ARG C NH2 
13942 N N   . ILE C 613 ? 0.4014 0.2497 0.1721 -0.0983 0.0227  -0.0673 605 ILE C N   
13943 C CA  . ILE C 613 ? 0.3945 0.2463 0.1680 -0.0921 0.0271  -0.0647 605 ILE C CA  
13944 C C   . ILE C 613 ? 0.3744 0.2401 0.1730 -0.0834 0.0318  -0.0633 605 ILE C C   
13945 O O   . ILE C 613 ? 0.4239 0.2854 0.2286 -0.0808 0.0424  -0.0661 605 ILE C O   
13946 C CB  . ILE C 613 ? 0.4194 0.2566 0.1799 -0.0914 0.0405  -0.0652 605 ILE C CB  
13947 C CG1 . ILE C 613 ? 0.4710 0.2945 0.2091 -0.0989 0.0363  -0.0650 605 ILE C CG1 
13948 C CG2 . ILE C 613 ? 0.3830 0.2257 0.1489 -0.0855 0.0453  -0.0624 605 ILE C CG2 
13949 C CD1 . ILE C 613 ? 0.5099 0.3200 0.2384 -0.1036 0.0415  -0.0689 605 ILE C CD1 
13950 N N   . ALA C 614 ? 0.3235 0.2061 0.1386 -0.0774 0.0238  -0.0575 606 ALA C N   
13951 C CA  . ALA C 614 ? 0.2971 0.1940 0.1380 -0.0678 0.0271  -0.0542 606 ALA C CA  
13952 C C   . ALA C 614 ? 0.3450 0.2422 0.1895 -0.0615 0.0349  -0.0514 606 ALA C C   
13953 O O   . ALA C 614 ? 0.2992 0.1927 0.1317 -0.0636 0.0324  -0.0495 606 ALA C O   
13954 C CB  . ALA C 614 ? 0.2970 0.2120 0.1545 -0.0647 0.0140  -0.0499 606 ALA C CB  
13955 N N   . VAL C 615 ? 0.2859 0.1867 0.1464 -0.0544 0.0443  -0.0510 607 VAL C N   
13956 C CA  . VAL C 615 ? 0.2803 0.1835 0.1484 -0.0483 0.0520  -0.0483 607 VAL C CA  
13957 C C   . VAL C 615 ? 0.2911 0.2088 0.1838 -0.0394 0.0497  -0.0441 607 VAL C C   
13958 O O   . VAL C 615 ? 0.2388 0.1572 0.1419 -0.0361 0.0538  -0.0457 607 VAL C O   
13959 C CB  . VAL C 615 ? 0.3004 0.1912 0.1619 -0.0483 0.0676  -0.0525 607 VAL C CB  
13960 C CG1 . VAL C 615 ? 0.3267 0.2224 0.1978 -0.0428 0.0748  -0.0493 607 VAL C CG1 
13961 C CG2 . VAL C 615 ? 0.3386 0.2118 0.1726 -0.0576 0.0706  -0.0575 607 VAL C CG2 
13962 N N   . GLU C 616 ? 0.2493 0.1766 0.1496 -0.0356 0.0430  -0.0388 608 GLU C N   
13963 C CA  . GLU C 616 ? 0.2104 0.1499 0.1317 -0.0273 0.0398  -0.0347 608 GLU C CA  
13964 C C   . GLU C 616 ? 0.2523 0.1971 0.1768 -0.0244 0.0361  -0.0296 608 GLU C C   
13965 O O   . GLU C 616 ? 0.2150 0.1580 0.1274 -0.0284 0.0292  -0.0281 608 GLU C O   
13966 C CB  . GLU C 616 ? 0.2008 0.1486 0.1285 -0.0267 0.0297  -0.0337 608 GLU C CB  
13967 C CG  . GLU C 616 ? 0.1900 0.1485 0.1365 -0.0182 0.0265  -0.0294 608 GLU C CG  
13968 C CD  . GLU C 616 ? 0.1936 0.1593 0.1466 -0.0178 0.0197  -0.0294 608 GLU C CD  
13969 O OE1 . GLU C 616 ? 0.2136 0.1855 0.1646 -0.0190 0.0098  -0.0276 608 GLU C OE1 
13970 O OE2 . GLU C 616 ? 0.2186 0.1836 0.1787 -0.0164 0.0245  -0.0311 608 GLU C OE2 
13971 N N   . ALA C 617 ? 0.2067 0.1570 0.1469 -0.0177 0.0399  -0.0269 609 ALA C N   
13972 C CA  . ALA C 617 ? 0.2412 0.1955 0.1847 -0.0157 0.0372  -0.0222 609 ALA C CA  
13973 C C   . ALA C 617 ? 0.2490 0.2108 0.1975 -0.0121 0.0245  -0.0177 609 ALA C C   
13974 O O   . ALA C 617 ? 0.2261 0.1941 0.1881 -0.0058 0.0219  -0.0142 609 ALA C O   
13975 C CB  . ALA C 617 ? 0.1892 0.1465 0.1477 -0.0106 0.0458  -0.0211 609 ALA C CB  
13976 N N   . GLY C 618 ? 0.1984 0.1590 0.1352 -0.0159 0.0161  -0.0180 610 GLY C N   
13977 C CA  . GLY C 618 ? 0.2074 0.1743 0.1473 -0.0122 0.0041  -0.0140 610 GLY C CA  
13978 C C   . GLY C 618 ? 0.1833 0.1476 0.1084 -0.0174 -0.0043 -0.0148 610 GLY C C   
13979 O O   . GLY C 618 ? 0.1993 0.1553 0.1097 -0.0244 -0.0011 -0.0180 610 GLY C O   
13980 N N   . HIS C 619 ? 0.1954 0.1663 0.1242 -0.0135 -0.0153 -0.0120 611 HIS C N   
13981 C CA  . HIS C 619 ? 0.1876 0.1572 0.1041 -0.0170 -0.0255 -0.0118 611 HIS C CA  
13982 C C   . HIS C 619 ? 0.2264 0.1941 0.1363 -0.0237 -0.0244 -0.0168 611 HIS C C   
13983 O O   . HIS C 619 ? 0.2684 0.2397 0.1878 -0.0237 -0.0188 -0.0197 611 HIS C O   
13984 C CB  . HIS C 619 ? 0.1769 0.1563 0.1031 -0.0099 -0.0362 -0.0085 611 HIS C CB  
13985 C CG  . HIS C 619 ? 0.2419 0.2188 0.1559 -0.0108 -0.0480 -0.0063 611 HIS C CG  
13986 N ND1 . HIS C 619 ? 0.2487 0.2246 0.1530 -0.0164 -0.0540 -0.0086 611 HIS C ND1 
13987 C CD2 . HIS C 619 ? 0.2531 0.2269 0.1618 -0.0069 -0.0553 -0.0019 611 HIS C CD2 
13988 C CE1 . HIS C 619 ? 0.2855 0.2580 0.1794 -0.0153 -0.0649 -0.0056 611 HIS C CE1 
13989 N NE2 . HIS C 619 ? 0.2525 0.2232 0.1485 -0.0096 -0.0655 -0.0015 611 HIS C NE2 
13990 N N   . THR C 620 ? 0.2338 0.1942 0.1259 -0.0300 -0.0303 -0.0176 612 THR C N   
13991 C CA  . THR C 620 ? 0.2663 0.2220 0.1484 -0.0378 -0.0300 -0.0223 612 THR C CA  
13992 C C   . THR C 620 ? 0.2856 0.2513 0.1735 -0.0382 -0.0415 -0.0227 612 THR C C   
13993 O O   . THR C 620 ? 0.2786 0.2431 0.1633 -0.0444 -0.0410 -0.0268 612 THR C O   
13994 C CB  . THR C 620 ? 0.3033 0.2436 0.1600 -0.0457 -0.0303 -0.0235 612 THR C CB  
13995 O OG1 . THR C 620 ? 0.2603 0.2002 0.1083 -0.0450 -0.0435 -0.0199 612 THR C OG1 
13996 C CG2 . THR C 620 ? 0.3065 0.2373 0.1568 -0.0464 -0.0181 -0.0233 612 THR C CG2 
13997 N N   . ASN C 621 ? 0.2600 0.2353 0.1562 -0.0318 -0.0519 -0.0186 613 ASN C N   
13998 C CA  A ASN C 621 ? 0.2704 0.2536 0.1680 -0.0334 -0.0641 -0.0190 613 ASN C CA  
13999 C CA  B ASN C 621 ? 0.2699 0.2544 0.1695 -0.0325 -0.0644 -0.0186 613 ASN C CA  
14000 C C   . ASN C 621 ? 0.2862 0.2810 0.2001 -0.0348 -0.0620 -0.0221 613 ASN C C   
14001 O O   . ASN C 621 ? 0.2758 0.2735 0.1869 -0.0408 -0.0689 -0.0244 613 ASN C O   
14002 C CB  A ASN C 621 ? 0.2988 0.2888 0.2011 -0.0256 -0.0754 -0.0140 613 ASN C CB  
14003 C CB  B ASN C 621 ? 0.2734 0.2677 0.1833 -0.0230 -0.0737 -0.0138 613 ASN C CB  
14004 C CG  A ASN C 621 ? 0.3410 0.3170 0.2210 -0.0278 -0.0819 -0.0116 613 ASN C CG  
14005 C CG  B ASN C 621 ? 0.2830 0.2931 0.2068 -0.0210 -0.0836 -0.0140 613 ASN C CG  
14006 O OD1 A ASN C 621 ? 0.3055 0.2670 0.1675 -0.0347 -0.0758 -0.0132 613 ASN C OD1 
14007 O OD1 B ASN C 621 ? 0.3282 0.3509 0.2711 -0.0174 -0.0800 -0.0146 613 ASN C OD1 
14008 N ND2 A ASN C 621 ? 0.2572 0.2400 0.1446 -0.0204 -0.0884 -0.0077 613 ASN C ND2 
14009 N ND2 B ASN C 621 ? 0.2543 0.2642 0.1699 -0.0229 -0.0949 -0.0132 613 ASN C ND2 
14010 N N   . GLY C 622 ? 0.2685 0.2686 0.1975 -0.0302 -0.0527 -0.0222 614 GLY C N   
14011 C CA  . GLY C 622 ? 0.2775 0.2867 0.2200 -0.0324 -0.0499 -0.0251 614 GLY C CA  
14012 C C   . GLY C 622 ? 0.2954 0.2952 0.2267 -0.0427 -0.0452 -0.0302 614 GLY C C   
14013 O O   . GLY C 622 ? 0.3378 0.3445 0.2763 -0.0474 -0.0471 -0.0327 614 GLY C O   
14014 N N   . TRP C 623 ? 0.2582 0.2418 0.1716 -0.0468 -0.0390 -0.0320 615 TRP C N   
14015 C CA  . TRP C 623 ? 0.2714 0.2431 0.1722 -0.0559 -0.0328 -0.0372 615 TRP C CA  
14016 C C   . TRP C 623 ? 0.2676 0.2362 0.1549 -0.0650 -0.0431 -0.0395 615 TRP C C   
14017 O O   . TRP C 623 ? 0.2803 0.2398 0.1578 -0.0733 -0.0398 -0.0441 615 TRP C O   
14018 C CB  . TRP C 623 ? 0.2802 0.2358 0.1668 -0.0564 -0.0214 -0.0385 615 TRP C CB  
14019 C CG  . TRP C 623 ? 0.2291 0.1872 0.1302 -0.0491 -0.0106 -0.0376 615 TRP C CG  
14020 C CD1 . TRP C 623 ? 0.2535 0.2140 0.1615 -0.0414 -0.0076 -0.0337 615 TRP C CD1 
14021 C CD2 . TRP C 623 ? 0.2265 0.1849 0.1372 -0.0489 -0.0025 -0.0403 615 TRP C CD2 
14022 N NE1 . TRP C 623 ? 0.2786 0.2412 0.2001 -0.0362 0.0013  -0.0338 615 TRP C NE1 
14023 C CE2 . TRP C 623 ? 0.2748 0.2354 0.1975 -0.0405 0.0048  -0.0378 615 TRP C CE2 
14024 C CE3 . TRP C 623 ? 0.2357 0.1913 0.1448 -0.0555 -0.0011 -0.0444 615 TRP C CE3 
14025 C CZ2 . TRP C 623 ? 0.2433 0.2030 0.1759 -0.0378 0.0131  -0.0392 615 TRP C CZ2 
14026 C CZ3 . TRP C 623 ? 0.3043 0.2585 0.2228 -0.0532 0.0079  -0.0459 615 TRP C CZ3 
14027 C CH2 . TRP C 623 ? 0.2444 0.2003 0.1741 -0.0442 0.0148  -0.0433 615 TRP C CH2 
14028 N N   . TYR C 624 ? 0.3044 0.2792 0.1901 -0.0636 -0.0562 -0.0364 616 TYR C N   
14029 C CA  . TYR C 624 ? 0.3083 0.2800 0.1812 -0.0723 -0.0675 -0.0384 616 TYR C CA  
14030 C C   . TYR C 624 ? 0.3262 0.3111 0.2143 -0.0766 -0.0719 -0.0406 616 TYR C C   
14031 O O   . TYR C 624 ? 0.3241 0.3040 0.2010 -0.0863 -0.0785 -0.0437 616 TYR C O   
14032 C CB  . TYR C 624 ? 0.3244 0.2990 0.1920 -0.0689 -0.0812 -0.0341 616 TYR C CB  
14033 C CG  . TYR C 624 ? 0.3203 0.2779 0.1680 -0.0679 -0.0761 -0.0326 616 TYR C CG  
14034 C CD1 . TYR C 624 ? 0.3926 0.3332 0.2193 -0.0743 -0.0730 -0.0345 616 TYR C CD1 
14035 C CD2 . TYR C 624 ? 0.3875 0.3462 0.2397 -0.0600 -0.0724 -0.0288 616 TYR C CD2 
14036 C CE1 . TYR C 624 ? 0.4294 0.3551 0.2391 -0.0740 -0.0670 -0.0329 616 TYR C CE1 
14037 C CE2 . TYR C 624 ? 0.4523 0.3954 0.2857 -0.0609 -0.0676 -0.0276 616 TYR C CE2 
14038 C CZ  . TYR C 624 ? 0.4331 0.3607 0.2467 -0.0676 -0.0641 -0.0295 616 TYR C CZ  
14039 O OH  . TYR C 624 ? 0.4160 0.3294 0.2135 -0.0684 -0.0577 -0.0279 616 TYR C OH  
14040 N N   . LYS C 625 ? 0.2706 0.2712 0.1828 -0.0704 -0.0680 -0.0392 617 LYS C N   
14041 C CA  . LYS C 625 ? 0.2696 0.2821 0.1967 -0.0755 -0.0695 -0.0415 617 LYS C CA  
14042 C C   . LYS C 625 ? 0.2907 0.2880 0.2046 -0.0857 -0.0615 -0.0469 617 LYS C C   
14043 O O   . LYS C 625 ? 0.3075 0.3091 0.2243 -0.0943 -0.0662 -0.0496 617 LYS C O   
14044 C CB  . LYS C 625 ? 0.2896 0.3176 0.2416 -0.0670 -0.0636 -0.0391 617 LYS C CB  
14045 C CG  . LYS C 625 ? 0.3449 0.3870 0.3139 -0.0722 -0.0647 -0.0409 617 LYS C CG  
14046 C CD  . LYS C 625 ? 0.3881 0.4450 0.3800 -0.0635 -0.0592 -0.0382 617 LYS C CD  
14047 C CE  . LYS C 625 ? 0.4010 0.4464 0.3909 -0.0619 -0.0444 -0.0395 617 LYS C CE  
14048 N NZ  . LYS C 625 ? 0.4342 0.4928 0.4447 -0.0553 -0.0393 -0.0373 617 LYS C NZ  
14049 N N   . TYR C 626 ? 0.2701 0.2499 0.1701 -0.0849 -0.0495 -0.0486 618 TYR C N   
14050 C CA  . TYR C 626 ? 0.2876 0.2498 0.1721 -0.0936 -0.0411 -0.0539 618 TYR C CA  
14051 C C   . TYR C 626 ? 0.3857 0.3288 0.2415 -0.1011 -0.0440 -0.0566 618 TYR C C   
14052 O O   . TYR C 626 ? 0.4283 0.3621 0.2716 -0.1110 -0.0467 -0.0605 618 TYR C O   
14053 C CB  . TYR C 626 ? 0.2803 0.2345 0.1677 -0.0877 -0.0252 -0.0546 618 TYR C CB  
14054 C CG  . TYR C 626 ? 0.3291 0.2988 0.2414 -0.0806 -0.0217 -0.0520 618 TYR C CG  
14055 C CD1 . TYR C 626 ? 0.3619 0.3360 0.2837 -0.0857 -0.0201 -0.0542 618 TYR C CD1 
14056 C CD2 . TYR C 626 ? 0.4169 0.3954 0.3418 -0.0695 -0.0201 -0.0474 618 TYR C CD2 
14057 C CE1 . TYR C 626 ? 0.3145 0.3012 0.2571 -0.0795 -0.0162 -0.0517 618 TYR C CE1 
14058 C CE2 . TYR C 626 ? 0.4386 0.4291 0.3836 -0.0631 -0.0169 -0.0451 618 TYR C CE2 
14059 C CZ  . TYR C 626 ? 0.3969 0.3913 0.3503 -0.0680 -0.0147 -0.0473 618 TYR C CZ  
14060 O OH  . TYR C 626 ? 0.4627 0.4675 0.4341 -0.0619 -0.0109 -0.0448 618 TYR C OH  
14061 N N   . VAL C 627 ? 0.3415 0.2776 0.1859 -0.0964 -0.0434 -0.0542 619 VAL C N   
14062 C CA  . VAL C 627 ? 0.3419 0.2578 0.1593 -0.1018 -0.0420 -0.0561 619 VAL C CA  
14063 C C   . VAL C 627 ? 0.4025 0.3216 0.2152 -0.1037 -0.0563 -0.0531 619 VAL C C   
14064 O O   . VAL C 627 ? 0.3783 0.2822 0.1721 -0.1087 -0.0558 -0.0541 619 VAL C O   
14065 C CB  . VAL C 627 ? 0.3417 0.2471 0.1483 -0.0967 -0.0327 -0.0549 619 VAL C CB  
14066 C CG1 . VAL C 627 ? 0.3256 0.2319 0.1456 -0.0903 -0.0174 -0.0557 619 VAL C CG1 
14067 C CG2 . VAL C 627 ? 0.3311 0.2466 0.1428 -0.0904 -0.0422 -0.0492 619 VAL C CG2 
14068 N N   . GLY C 628 ? 0.3993 0.3372 0.2289 -0.0994 -0.0686 -0.0495 620 GLY C N   
14069 C CA  . GLY C 628 ? 0.3753 0.3163 0.2019 -0.0999 -0.0817 -0.0470 620 GLY C CA  
14070 C C   . GLY C 628 ? 0.4285 0.3568 0.2371 -0.0970 -0.0824 -0.0439 620 GLY C C   
14071 O O   . GLY C 628 ? 0.4142 0.3343 0.2154 -0.0937 -0.0737 -0.0428 620 GLY C O   
14072 N N   . LEU C 629 ? 0.4071 0.3337 0.2088 -0.0989 -0.0929 -0.0424 621 LEU C N   
14073 C CA  . LEU C 629 ? 0.4673 0.3825 0.2527 -0.0965 -0.0949 -0.0390 621 LEU C CA  
14074 C C   . LEU C 629 ? 0.5023 0.3930 0.2611 -0.1028 -0.0845 -0.0410 621 LEU C C   
14075 O O   . LEU C 629 ? 0.5393 0.4187 0.2845 -0.1010 -0.0812 -0.0384 621 LEU C O   
14076 C CB  . LEU C 629 ? 0.5217 0.4431 0.3087 -0.0960 -0.1098 -0.0369 621 LEU C CB  
14077 C CG  . LEU C 629 ? 0.4784 0.4249 0.2921 -0.0888 -0.1203 -0.0347 621 LEU C CG  
14078 C CD1 . LEU C 629 ? 0.5370 0.4876 0.3500 -0.0888 -0.1338 -0.0332 621 LEU C CD1 
14079 C CD2 . LEU C 629 ? 0.4551 0.4089 0.2786 -0.0789 -0.1179 -0.0309 621 LEU C CD2 
14080 N N   . ASN C 630 ? 0.5163 0.3983 0.2679 -0.1100 -0.0786 -0.0455 622 ASN C N   
14081 C CA  . ASN C 630 ? 0.5717 0.4302 0.2984 -0.1157 -0.0679 -0.0478 622 ASN C CA  
14082 C C   . ASN C 630 ? 0.6164 0.4690 0.3431 -0.1152 -0.0512 -0.0510 622 ASN C C   
14083 O O   . ASN C 630 ? 0.5918 0.4258 0.3001 -0.1192 -0.0404 -0.0533 622 ASN C O   
14084 C CB  . ASN C 630 ? 0.5960 0.4456 0.3112 -0.1241 -0.0729 -0.0504 622 ASN C CB  
14085 C CG  . ASN C 630 ? 0.6876 0.5415 0.4013 -0.1247 -0.0891 -0.0475 622 ASN C CG  
14086 O OD1 . ASN C 630 ? 0.6541 0.5033 0.3593 -0.1216 -0.0926 -0.0439 622 ASN C OD1 
14087 N ND2 . ASN C 630 ? 0.6908 0.5539 0.4134 -0.1287 -0.0989 -0.0491 622 ASN C ND2 
14088 N N   . GLY C 631 ? 0.5315 0.3990 0.2784 -0.1100 -0.0486 -0.0511 623 GLY C N   
14089 C CA  . GLY C 631 ? 0.4761 0.3389 0.2247 -0.1076 -0.0331 -0.0536 623 GLY C CA  
14090 C C   . GLY C 631 ? 0.5040 0.3648 0.2495 -0.1022 -0.0280 -0.0504 623 GLY C C   
14091 O O   . GLY C 631 ? 0.5077 0.3652 0.2442 -0.1017 -0.0345 -0.0466 623 GLY C O   
14092 N N   . ALA C 632 ? 0.4335 0.2959 0.1869 -0.0981 -0.0162 -0.0520 624 ALA C N   
14093 C CA  . ALA C 632 ? 0.4386 0.3006 0.1912 -0.0931 -0.0109 -0.0490 624 ALA C CA  
14094 C C   . ALA C 632 ? 0.3844 0.2561 0.1543 -0.0873 -0.0033 -0.0503 624 ALA C C   
14095 O O   . ALA C 632 ? 0.4226 0.2984 0.2041 -0.0868 0.0013  -0.0535 624 ALA C O   
14096 C CB  . ALA C 632 ? 0.4587 0.3025 0.1921 -0.0960 0.0012  -0.0499 624 ALA C CB  
14097 N N   . VAL C 633 ? 0.3453 0.2232 0.1226 -0.0812 -0.0024 -0.0459 625 VAL C N   
14098 C CA  . VAL C 633 ? 0.3184 0.2103 0.1220 -0.0719 0.0041  -0.0434 625 VAL C CA  
14099 C C   . VAL C 633 ? 0.3734 0.2605 0.1744 -0.0691 0.0145  -0.0414 625 VAL C C   
14100 O O   . VAL C 633 ? 0.3762 0.2574 0.1632 -0.0713 0.0105  -0.0387 625 VAL C O   
14101 C CB  . VAL C 633 ? 0.3360 0.2463 0.1597 -0.0654 -0.0084 -0.0385 625 VAL C CB  
14102 C CG1 . VAL C 633 ? 0.2712 0.1935 0.1198 -0.0566 -0.0015 -0.0367 625 VAL C CG1 
14103 C CG2 . VAL C 633 ? 0.3766 0.2933 0.2024 -0.0691 -0.0203 -0.0400 625 VAL C CG2 
14104 N N   . VAL C 634 ? 0.3538 0.2431 0.1682 -0.0645 0.0275  -0.0427 626 VAL C N   
14105 C CA  . VAL C 634 ? 0.3207 0.2113 0.1414 -0.0604 0.0369  -0.0401 626 VAL C CA  
14106 C C   . VAL C 634 ? 0.3082 0.2158 0.1549 -0.0515 0.0321  -0.0354 626 VAL C C   
14107 O O   . VAL C 634 ? 0.2821 0.1968 0.1461 -0.0466 0.0358  -0.0364 626 VAL C O   
14108 C CB  . VAL C 634 ? 0.3123 0.1946 0.1319 -0.0604 0.0541  -0.0445 626 VAL C CB  
14109 C CG1 . VAL C 634 ? 0.3054 0.1922 0.1354 -0.0561 0.0634  -0.0415 626 VAL C CG1 
14110 C CG2 . VAL C 634 ? 0.3708 0.2336 0.1615 -0.0693 0.0591  -0.0497 626 VAL C CG2 
14111 N N   . GLY C 635 ? 0.2698 0.1824 0.1175 -0.0496 0.0236  -0.0302 627 GLY C N   
14112 C CA  . GLY C 635 ? 0.2461 0.1727 0.1154 -0.0415 0.0181  -0.0257 627 GLY C CA  
14113 C C   . GLY C 635 ? 0.2533 0.1805 0.1215 -0.0400 0.0155  -0.0206 627 GLY C C   
14114 O O   . GLY C 635 ? 0.2592 0.1774 0.1144 -0.0447 0.0220  -0.0206 627 GLY C O   
14115 N N   . ILE C 636 ? 0.2357 0.1725 0.1165 -0.0339 0.0063  -0.0161 628 ILE C N   
14116 C CA  . ILE C 636 ? 0.2350 0.1711 0.1137 -0.0326 0.0021  -0.0110 628 ILE C CA  
14117 C C   . ILE C 636 ? 0.2507 0.1928 0.1331 -0.0277 -0.0123 -0.0075 628 ILE C C   
14118 O O   . ILE C 636 ? 0.2302 0.1821 0.1286 -0.0215 -0.0151 -0.0073 628 ILE C O   
14119 C CB  . ILE C 636 ? 0.2314 0.1727 0.1263 -0.0288 0.0106  -0.0090 628 ILE C CB  
14120 C CG1 . ILE C 636 ? 0.2418 0.1823 0.1350 -0.0280 0.0048  -0.0034 628 ILE C CG1 
14121 C CG2 . ILE C 636 ? 0.2600 0.2117 0.1765 -0.0213 0.0116  -0.0095 628 ILE C CG2 
14122 C CD1 . ILE C 636 ? 0.2727 0.2177 0.1805 -0.0263 0.0132  -0.0013 628 ILE C CD1 
14123 N N   . ASN C 637 ? 0.2462 0.1813 0.1125 -0.0303 -0.0211 -0.0047 629 ASN C N   
14124 C CA  . ASN C 637 ? 0.2270 0.1664 0.0949 -0.0251 -0.0351 -0.0015 629 ASN C CA  
14125 C C   . ASN C 637 ? 0.2719 0.2083 0.1382 -0.0219 -0.0401 0.0039  629 ASN C C   
14126 O O   . ASN C 637 ? 0.3041 0.2414 0.1686 -0.0174 -0.0518 0.0068  629 ASN C O   
14127 C CB  . ASN C 637 ? 0.2438 0.1775 0.0945 -0.0296 -0.0444 -0.0028 629 ASN C CB  
14128 C CG  . ASN C 637 ? 0.3362 0.2742 0.1902 -0.0323 -0.0426 -0.0078 629 ASN C CG  
14129 O OD1 . ASN C 637 ? 0.2395 0.1853 0.1096 -0.0298 -0.0351 -0.0101 629 ASN C OD1 
14130 N ND2 . ASN C 637 ? 0.3608 0.2927 0.1988 -0.0378 -0.0499 -0.0095 629 ASN C ND2 
14131 N N   . ARG C 638 ? 0.2303 0.1632 0.0975 -0.0241 -0.0317 0.0054  630 ARG C N   
14132 C CA  . ARG C 638 ? 0.2329 0.1622 0.0987 -0.0223 -0.0359 0.0105  630 ARG C CA  
14133 C C   . ARG C 638 ? 0.2444 0.1826 0.1314 -0.0169 -0.0312 0.0118  630 ARG C C   
14134 O O   . ARG C 638 ? 0.2253 0.1714 0.1268 -0.0149 -0.0237 0.0088  630 ARG C O   
14135 C CB  . ARG C 638 ? 0.2529 0.1697 0.1006 -0.0309 -0.0311 0.0119  630 ARG C CB  
14136 C CG  . ARG C 638 ? 0.2651 0.1819 0.1149 -0.0366 -0.0158 0.0082  630 ARG C CG  
14137 C CD  . ARG C 638 ? 0.3414 0.2511 0.1839 -0.0428 -0.0088 0.0109  630 ARG C CD  
14138 N NE  . ARG C 638 ? 0.3046 0.2222 0.1654 -0.0385 -0.0089 0.0145  630 ARG C NE  
14139 C CZ  . ARG C 638 ? 0.3568 0.2719 0.2178 -0.0429 -0.0040 0.0176  630 ARG C CZ  
14140 N NH1 . ARG C 638 ? 0.3156 0.2203 0.1589 -0.0519 0.0025  0.0176  630 ARG C NH1 
14141 N NH2 . ARG C 638 ? 0.2533 0.1759 0.1317 -0.0390 -0.0058 0.0208  630 ARG C NH2 
14142 N N   . PHE C 639 ? 0.2063 0.1421 0.0942 -0.0144 -0.0365 0.0165  631 PHE C N   
14143 C CA  . PHE C 639 ? 0.1948 0.1377 0.1013 -0.0099 -0.0331 0.0181  631 PHE C CA  
14144 C C   . PHE C 639 ? 0.2102 0.1552 0.1237 -0.0152 -0.0202 0.0168  631 PHE C C   
14145 O O   . PHE C 639 ? 0.2061 0.1450 0.1077 -0.0227 -0.0141 0.0158  631 PHE C O   
14146 C CB  . PHE C 639 ? 0.2622 0.2000 0.1658 -0.0070 -0.0422 0.0233  631 PHE C CB  
14147 C CG  . PHE C 639 ? 0.2555 0.1925 0.1558 0.0004  -0.0539 0.0245  631 PHE C CG  
14148 C CD1 . PHE C 639 ? 0.2690 0.2150 0.1839 0.0083  -0.0550 0.0232  631 PHE C CD1 
14149 C CD2 . PHE C 639 ? 0.2242 0.1557 0.1140 -0.0002 -0.0594 0.0251  631 PHE C CD2 
14150 C CE1 . PHE C 639 ? 0.2047 0.1572 0.1270 0.0140  -0.0577 0.0217  631 PHE C CE1 
14151 C CE2 . PHE C 639 ? 0.2014 0.1407 0.1018 0.0064  -0.0617 0.0232  631 PHE C CE2 
14152 C CZ  . PHE C 639 ? 0.1836 0.1336 0.0996 0.0128  -0.0603 0.0217  631 PHE C CZ  
14153 N N   . GLY C 640 ? 0.1774 0.1309 0.1104 -0.0109 -0.0159 0.0168  632 GLY C N   
14154 C CA  . GLY C 640 ? 0.1862 0.1441 0.1303 -0.0141 -0.0040 0.0156  632 GLY C CA  
14155 C C   . GLY C 640 ? 0.2000 0.1556 0.1437 -0.0192 -0.0026 0.0196  632 GLY C C   
14156 O O   . GLY C 640 ? 0.1936 0.1406 0.1224 -0.0226 -0.0096 0.0229  632 GLY C O   
14157 N N   . GLU C 641 ? 0.1976 0.1609 0.1582 -0.0198 0.0063  0.0195  633 GLU C N   
14158 C CA  . GLU C 641 ? 0.1936 0.1577 0.1582 -0.0254 0.0093  0.0230  633 GLU C CA  
14159 C C   . GLU C 641 ? 0.1699 0.1459 0.1602 -0.0213 0.0126  0.0239  633 GLU C C   
14160 O O   . GLU C 641 ? 0.1662 0.1491 0.1692 -0.0168 0.0191  0.0204  633 GLU C O   
14161 C CB  . GLU C 641 ? 0.2156 0.1765 0.1711 -0.0341 0.0214  0.0211  633 GLU C CB  
14162 C CG  . GLU C 641 ? 0.2968 0.2437 0.2245 -0.0401 0.0180  0.0213  633 GLU C CG  
14163 C CD  . GLU C 641 ? 0.3088 0.2474 0.2252 -0.0440 0.0088  0.0268  633 GLU C CD  
14164 O OE1 . GLU C 641 ? 0.3269 0.2708 0.2571 -0.0437 0.0066  0.0304  633 GLU C OE1 
14165 O OE2 . GLU C 641 ? 0.3256 0.2514 0.2185 -0.0474 0.0032  0.0275  633 GLU C OE2 
14166 N N   . SER C 642 ? 0.1694 0.1471 0.1667 -0.0234 0.0080  0.0285  634 SER C N   
14167 C CA  . SER C 642 ? 0.2167 0.2061 0.2389 -0.0208 0.0105  0.0299  634 SER C CA  
14168 C C   . SER C 642 ? 0.1974 0.1950 0.2305 -0.0261 0.0253  0.0280  634 SER C C   
14169 O O   . SER C 642 ? 0.2473 0.2428 0.2743 -0.0347 0.0294  0.0300  634 SER C O   
14170 C CB  . SER C 642 ? 0.1740 0.1615 0.1987 -0.0224 -0.0002 0.0355  634 SER C CB  
14171 O OG  . SER C 642 ? 0.1804 0.1797 0.2298 -0.0201 0.0009  0.0370  634 SER C OG  
14172 N N   . ALA C 643 ? 0.1704 0.1766 0.2192 -0.0209 0.0340  0.0242  635 ALA C N   
14173 C CA  . ALA C 643 ? 0.1946 0.2084 0.2541 -0.0239 0.0496  0.0214  635 ALA C CA  
14174 C C   . ALA C 643 ? 0.1732 0.1946 0.2501 -0.0154 0.0555  0.0176  635 ALA C C   
14175 O O   . ALA C 643 ? 0.2103 0.2282 0.2849 -0.0086 0.0485  0.0165  635 ALA C O   
14176 C CB  . ALA C 643 ? 0.1829 0.1866 0.2193 -0.0308 0.0581  0.0183  635 ALA C CB  
14177 N N   . PRO C 644 ? 0.2064 0.2376 0.3006 -0.0152 0.0684  0.0157  636 PRO C N   
14178 C CA  . PRO C 644 ? 0.1829 0.2185 0.2906 -0.0066 0.0744  0.0117  636 PRO C CA  
14179 C C   . PRO C 644 ? 0.2147 0.2385 0.3022 -0.0055 0.0783  0.0064  636 PRO C C   
14180 O O   . PRO C 644 ? 0.2048 0.2196 0.2713 -0.0122 0.0826  0.0044  636 PRO C O   
14181 C CB  . PRO C 644 ? 0.2717 0.3192 0.3990 -0.0078 0.0889  0.0105  636 PRO C CB  
14182 C CG  . PRO C 644 ? 0.2512 0.3053 0.3847 -0.0156 0.0862  0.0157  636 PRO C CG  
14183 C CD  . PRO C 644 ? 0.2483 0.2880 0.3531 -0.0222 0.0775  0.0175  636 PRO C CD  
14184 N N   . ALA C 645 ? 0.1524 0.1756 0.2461 0.0027  0.0764  0.0041  637 ALA C N   
14185 C CA  . ALA C 645 ? 0.2288 0.2410 0.3046 0.0038  0.0775  -0.0005 637 ALA C CA  
14186 C C   . ALA C 645 ? 0.2944 0.3011 0.3596 -0.0003 0.0922  -0.0058 637 ALA C C   
14187 O O   . ALA C 645 ? 0.2767 0.2724 0.3191 -0.0050 0.0923  -0.0084 637 ALA C O   
14188 C CB  . ALA C 645 ? 0.2877 0.3005 0.3744 0.0130  0.0744  -0.0017 637 ALA C CB  
14189 N N   . ASP C 646 ? 0.2881 0.3017 0.3693 0.0020  0.1046  -0.0076 638 ASP C N   
14190 C CA  . ASP C 646 ? 0.3815 0.3884 0.4513 -0.0015 0.1198  -0.0129 638 ASP C CA  
14191 C C   . ASP C 646 ? 0.3993 0.3988 0.4468 -0.0119 0.1216  -0.0124 638 ASP C C   
14192 O O   . ASP C 646 ? 0.3483 0.3348 0.3727 -0.0163 0.1264  -0.0166 638 ASP C O   
14193 C CB  . ASP C 646 ? 0.4214 0.4391 0.5142 0.0026  0.1334  -0.0142 638 ASP C CB  
14194 C CG  . ASP C 646 ? 0.5789 0.5969 0.6834 0.0125  0.1299  -0.0158 638 ASP C CG  
14195 O OD1 . ASP C 646 ? 0.5606 0.5727 0.6600 0.0162  0.1226  -0.0164 638 ASP C OD1 
14196 O OD2 . ASP C 646 ? 0.6766 0.7004 0.7946 0.0163  0.1344  -0.0163 638 ASP C OD2 
14197 N N   . LEU C 647 ? 0.2096 0.2158 0.2625 -0.0164 0.1169  -0.0072 639 LEU C N   
14198 C CA  . LEU C 647 ? 0.2673 0.2653 0.2986 -0.0265 0.1180  -0.0060 639 LEU C CA  
14199 C C   . LEU C 647 ? 0.2769 0.2618 0.2826 -0.0293 0.1055  -0.0058 639 LEU C C   
14200 O O   . LEU C 647 ? 0.2706 0.2434 0.2516 -0.0365 0.1082  -0.0074 639 LEU C O   
14201 C CB  . LEU C 647 ? 0.2445 0.2526 0.2891 -0.0306 0.1151  -0.0001 639 LEU C CB  
14202 C CG  . LEU C 647 ? 0.3747 0.3762 0.4015 -0.0416 0.1196  0.0018  639 LEU C CG  
14203 C CD1 . LEU C 647 ? 0.4314 0.4470 0.4804 -0.0448 0.1237  0.0061  639 LEU C CD1 
14204 C CD2 . LEU C 647 ? 0.4795 0.4691 0.4833 -0.0455 0.1045  0.0048  639 LEU C CD2 
14205 N N   . LEU C 648 ? 0.2410 0.2279 0.2519 -0.0235 0.0921  -0.0039 640 LEU C N   
14206 C CA  . LEU C 648 ? 0.2219 0.1989 0.2119 -0.0253 0.0799  -0.0034 640 LEU C CA  
14207 C C   . LEU C 648 ? 0.2979 0.2648 0.2711 -0.0261 0.0838  -0.0092 640 LEU C C   
14208 O O   . LEU C 648 ? 0.2787 0.2348 0.2286 -0.0317 0.0794  -0.0099 640 LEU C O   
14209 C CB  . LEU C 648 ? 0.2412 0.2236 0.2423 -0.0186 0.0659  -0.0001 640 LEU C CB  
14210 C CG  . LEU C 648 ? 0.2670 0.2558 0.2788 -0.0190 0.0588  0.0060  640 LEU C CG  
14211 C CD1 . LEU C 648 ? 0.2207 0.2143 0.2451 -0.0112 0.0471  0.0087  640 LEU C CD1 
14212 C CD2 . LEU C 648 ? 0.2858 0.2657 0.2768 -0.0266 0.0528  0.0089  640 LEU C CD2 
14213 N N   . PHE C 649 ? 0.2327 0.2016 0.2164 -0.0207 0.0912  -0.0132 641 PHE C N   
14214 C CA  . PHE C 649 ? 0.2805 0.2384 0.2476 -0.0224 0.0957  -0.0189 641 PHE C CA  
14215 C C   . PHE C 649 ? 0.2886 0.2360 0.2352 -0.0305 0.1061  -0.0218 641 PHE C C   
14216 O O   . PHE C 649 ? 0.2785 0.2135 0.2015 -0.0357 0.1035  -0.0244 641 PHE C O   
14217 C CB  . PHE C 649 ? 0.2312 0.1918 0.2131 -0.0152 0.1031  -0.0226 641 PHE C CB  
14218 C CG  . PHE C 649 ? 0.2349 0.2001 0.2278 -0.0085 0.0924  -0.0211 641 PHE C CG  
14219 C CD1 . PHE C 649 ? 0.2282 0.1885 0.2080 -0.0103 0.0816  -0.0212 641 PHE C CD1 
14220 C CD2 . PHE C 649 ? 0.2614 0.2357 0.2777 -0.0005 0.0930  -0.0194 641 PHE C CD2 
14221 C CE1 . PHE C 649 ? 0.2889 0.2533 0.2784 -0.0044 0.0730  -0.0198 641 PHE C CE1 
14222 C CE2 . PHE C 649 ? 0.2491 0.2257 0.2730 0.0053  0.0835  -0.0179 641 PHE C CE2 
14223 C CZ  . PHE C 649 ? 0.2605 0.2321 0.2707 0.0032  0.0743  -0.0182 641 PHE C CZ  
14224 N N   . LYS C 650 ? 0.2648 0.2166 0.2197 -0.0321 0.1176  -0.0211 642 LYS C N   
14225 C CA  . LYS C 650 ? 0.4054 0.3462 0.3395 -0.0402 0.1287  -0.0236 642 LYS C CA  
14226 C C   . LYS C 650 ? 0.3412 0.2737 0.2532 -0.0482 0.1190  -0.0201 642 LYS C C   
14227 O O   . LYS C 650 ? 0.3753 0.2926 0.2598 -0.0546 0.1195  -0.0227 642 LYS C O   
14228 C CB  . LYS C 650 ? 0.4376 0.3873 0.3886 -0.0399 0.1439  -0.0233 642 LYS C CB  
14229 N N   . ALA C 651 ? 0.2878 0.2288 0.2102 -0.0479 0.1093  -0.0140 643 ALA C N   
14230 C CA  . ALA C 651 ? 0.3111 0.2435 0.2132 -0.0551 0.1009  -0.0101 643 ALA C CA  
14231 C C   . ALA C 651 ? 0.3225 0.2442 0.2036 -0.0559 0.0876  -0.0110 643 ALA C C   
14232 O O   . ALA C 651 ? 0.3048 0.2138 0.1609 -0.0629 0.0834  -0.0099 643 ALA C O   
14233 C CB  . ALA C 651 ? 0.3675 0.3103 0.2859 -0.0538 0.0925  -0.0036 643 ALA C CB  
14234 N N   . PHE C 652 ? 0.2695 0.1961 0.1602 -0.0492 0.0808  -0.0127 644 PHE C N   
14235 C CA  . PHE C 652 ? 0.2990 0.2189 0.1745 -0.0495 0.0679  -0.0134 644 PHE C CA  
14236 C C   . PHE C 652 ? 0.3402 0.2509 0.2020 -0.0517 0.0730  -0.0197 644 PHE C C   
14237 O O   . PHE C 652 ? 0.3398 0.2479 0.1942 -0.0513 0.0629  -0.0209 644 PHE C O   
14238 C CB  . PHE C 652 ? 0.2621 0.1933 0.1561 -0.0415 0.0558  -0.0107 644 PHE C CB  
14239 C CG  . PHE C 652 ? 0.2897 0.2255 0.1895 -0.0403 0.0467  -0.0044 644 PHE C CG  
14240 C CD1 . PHE C 652 ? 0.3625 0.2892 0.2426 -0.0450 0.0376  -0.0014 644 PHE C CD1 
14241 C CD2 . PHE C 652 ? 0.2881 0.2356 0.2115 -0.0345 0.0465  -0.0015 644 PHE C CD2 
14242 C CE1 . PHE C 652 ? 0.4019 0.3305 0.2854 -0.0439 0.0290  0.0043  644 PHE C CE1 
14243 C CE2 . PHE C 652 ? 0.3481 0.2977 0.2748 -0.0340 0.0376  0.0041  644 PHE C CE2 
14244 C CZ  . PHE C 652 ? 0.3259 0.2658 0.2325 -0.0386 0.0292  0.0069  644 PHE C CZ  
14245 N N   . GLY C 653 ? 0.3587 0.2641 0.2168 -0.0542 0.0886  -0.0238 645 GLY C N   
14246 C CA  . GLY C 653 ? 0.3865 0.2789 0.2257 -0.0578 0.0937  -0.0299 645 GLY C CA  
14247 C C   . GLY C 653 ? 0.3603 0.2561 0.2116 -0.0523 0.0954  -0.0340 645 GLY C C   
14248 O O   . GLY C 653 ? 0.3943 0.2790 0.2288 -0.0558 0.0950  -0.0386 645 GLY C O   
14249 N N   . PHE C 654 ? 0.3500 0.2596 0.2286 -0.0441 0.0967  -0.0325 646 PHE C N   
14250 C CA  . PHE C 654 ? 0.2771 0.1880 0.1663 -0.0387 0.1002  -0.0364 646 PHE C CA  
14251 C C   . PHE C 654 ? 0.2906 0.1979 0.1836 -0.0371 0.1181  -0.0405 646 PHE C C   
14252 O O   . PHE C 654 ? 0.3199 0.2371 0.2359 -0.0299 0.1241  -0.0398 646 PHE C O   
14253 C CB  . PHE C 654 ? 0.2507 0.1759 0.1644 -0.0307 0.0916  -0.0327 646 PHE C CB  
14254 C CG  . PHE C 654 ? 0.2853 0.2135 0.1949 -0.0315 0.0753  -0.0293 646 PHE C CG  
14255 C CD1 . PHE C 654 ? 0.2884 0.2125 0.1895 -0.0331 0.0686  -0.0320 646 PHE C CD1 
14256 C CD2 . PHE C 654 ? 0.2331 0.1677 0.1467 -0.0310 0.0669  -0.0236 646 PHE C CD2 
14257 C CE1 . PHE C 654 ? 0.2484 0.1767 0.1475 -0.0333 0.0542  -0.0291 646 PHE C CE1 
14258 C CE2 . PHE C 654 ? 0.2266 0.1632 0.1360 -0.0309 0.0524  -0.0208 646 PHE C CE2 
14259 C CZ  . PHE C 654 ? 0.2432 0.1775 0.1461 -0.0317 0.0463  -0.0235 646 PHE C CZ  
14260 N N   . THR C 655 ? 0.3466 0.2385 0.2153 -0.0439 0.1263  -0.0448 647 THR C N   
14261 C CA  . THR C 655 ? 0.3591 0.2468 0.2317 -0.0425 0.1382  -0.0472 647 THR C CA  
14262 C C   . THR C 655 ? 0.3899 0.2620 0.2449 -0.0455 0.1386  -0.0521 647 THR C C   
14263 O O   . THR C 655 ? 0.3890 0.2521 0.2246 -0.0512 0.1299  -0.0534 647 THR C O   
14264 C CB  . THR C 655 ? 0.4124 0.2972 0.2763 -0.0477 0.1444  -0.0456 647 THR C CB  
14265 O OG1 . THR C 655 ? 0.4181 0.2873 0.2519 -0.0567 0.1390  -0.0466 647 THR C OG1 
14266 C CG2 . THR C 655 ? 0.3547 0.2535 0.2328 -0.0470 0.1428  -0.0401 647 THR C CG2 
14267 N N   . VAL C 656 ? 0.4054 0.2741 0.2674 -0.0417 0.1482  -0.0545 648 VAL C N   
14268 C CA  . VAL C 656 ? 0.4701 0.3225 0.3150 -0.0448 0.1499  -0.0588 648 VAL C CA  
14269 C C   . VAL C 656 ? 0.5018 0.3390 0.3177 -0.0546 0.1485  -0.0600 648 VAL C C   
14270 O O   . VAL C 656 ? 0.4181 0.2439 0.2152 -0.0602 0.1414  -0.0620 648 VAL C O   
14271 C CB  . VAL C 656 ? 0.5295 0.3805 0.3857 -0.0388 0.1613  -0.0607 648 VAL C CB  
14272 C CG1 . VAL C 656 ? 0.5894 0.4210 0.4243 -0.0430 0.1643  -0.0650 648 VAL C CG1 
14273 C CG2 . VAL C 656 ? 0.4803 0.3440 0.3627 -0.0292 0.1600  -0.0593 648 VAL C CG2 
14274 N N   . ASP C 657 ? 0.4628 0.2998 0.2751 -0.0571 0.1544  -0.0584 649 ASP C N   
14275 C CA  . ASP C 657 ? 0.5206 0.3417 0.3049 -0.0662 0.1534  -0.0591 649 ASP C CA  
14276 C C   . ASP C 657 ? 0.5255 0.3431 0.2933 -0.0723 0.1386  -0.0575 649 ASP C C   
14277 O O   . ASP C 657 ? 0.4549 0.2573 0.1989 -0.0793 0.1335  -0.0591 649 ASP C O   
14278 C CB  . ASP C 657 ? 0.5882 0.4120 0.3738 -0.0677 0.1614  -0.0569 649 ASP C CB  
14279 C CG  . ASP C 657 ? 0.7781 0.5994 0.5707 -0.0642 0.1763  -0.0594 649 ASP C CG  
14280 O OD1 . ASP C 657 ? 0.8379 0.6511 0.6282 -0.0619 0.1801  -0.0630 649 ASP C OD1 
14281 O OD2 . ASP C 657 ? 0.8618 0.6894 0.6621 -0.0640 0.1842  -0.0576 649 ASP C OD2 
14282 N N   . ASN C 658 ? 0.4118 0.2435 0.1920 -0.0697 0.1308  -0.0542 650 ASN C N   
14283 C CA  . ASN C 658 ? 0.4680 0.2976 0.2335 -0.0747 0.1158  -0.0523 650 ASN C CA  
14284 C C   . ASN C 658 ? 0.4061 0.2330 0.1683 -0.0751 0.1072  -0.0551 650 ASN C C   
14285 O O   . ASN C 658 ? 0.4947 0.3136 0.2389 -0.0812 0.0960  -0.0550 650 ASN C O   
14286 C CB  . ASN C 658 ? 0.4587 0.3030 0.2368 -0.0718 0.1100  -0.0476 650 ASN C CB  
14287 C CG  . ASN C 658 ? 0.4682 0.3092 0.2297 -0.0767 0.0939  -0.0449 650 ASN C CG  
14288 O OD1 . ASN C 658 ? 0.4841 0.3120 0.2241 -0.0833 0.0892  -0.0447 650 ASN C OD1 
14289 N ND2 . ASN C 658 ? 0.4142 0.2682 0.1894 -0.0724 0.0835  -0.0420 650 ASN C ND2 
14290 N N   . VAL C 659 ? 0.4394 0.2733 0.2199 -0.0688 0.1115  -0.0572 651 VAL C N   
14291 C CA  . VAL C 659 ? 0.4602 0.2906 0.2372 -0.0701 0.1043  -0.0600 651 VAL C CA  
14292 C C   . VAL C 659 ? 0.4709 0.2832 0.2268 -0.0766 0.1063  -0.0631 651 VAL C C   
14293 O O   . VAL C 659 ? 0.4688 0.2750 0.2110 -0.0825 0.0959  -0.0640 651 VAL C O   
14294 C CB  . VAL C 659 ? 0.4151 0.2548 0.2153 -0.0620 0.1091  -0.0613 651 VAL C CB  
14295 C CG1 . VAL C 659 ? 0.3933 0.2279 0.1890 -0.0645 0.1027  -0.0643 651 VAL C CG1 
14296 C CG2 . VAL C 659 ? 0.3797 0.2362 0.1993 -0.0559 0.1057  -0.0580 651 VAL C CG2 
14297 N N   . VAL C 660 ? 0.4497 0.2538 0.2033 -0.0757 0.1194  -0.0646 652 VAL C N   
14298 C CA  . VAL C 660 ? 0.4831 0.2682 0.2150 -0.0816 0.1225  -0.0676 652 VAL C CA  
14299 C C   . VAL C 660 ? 0.5118 0.2869 0.2196 -0.0904 0.1130  -0.0661 652 VAL C C   
14300 O O   . VAL C 660 ? 0.5008 0.2653 0.1922 -0.0964 0.1053  -0.0675 652 VAL C O   
14301 C CB  . VAL C 660 ? 0.5354 0.3143 0.2697 -0.0784 0.1386  -0.0691 652 VAL C CB  
14302 C CG1 . VAL C 660 ? 0.5756 0.3327 0.2834 -0.0854 0.1422  -0.0718 652 VAL C CG1 
14303 C CG2 . VAL C 660 ? 0.4829 0.2689 0.2390 -0.0697 0.1460  -0.0706 652 VAL C CG2 
14304 N N   . ASP C 661 ? 0.4965 0.2748 0.2022 -0.0913 0.1127  -0.0629 653 ASP C N   
14305 C CA  . ASP C 661 ? 0.5402 0.3080 0.2229 -0.0990 0.1033  -0.0608 653 ASP C CA  
14306 C C   . ASP C 661 ? 0.5593 0.3327 0.2401 -0.1013 0.0854  -0.0591 653 ASP C C   
14307 O O   . ASP C 661 ? 0.5500 0.3128 0.2122 -0.1077 0.0759  -0.0587 653 ASP C O   
14308 C CB  . ASP C 661 ? 0.5697 0.3404 0.2521 -0.0992 0.1062  -0.0572 653 ASP C CB  
14309 N N   . THR C 662 ? 0.5143 0.3049 0.2151 -0.0959 0.0802  -0.0579 654 THR C N   
14310 C CA  . THR C 662 ? 0.4527 0.2510 0.1551 -0.0972 0.0633  -0.0564 654 THR C CA  
14311 C C   . THR C 662 ? 0.5327 0.3248 0.2295 -0.1009 0.0592  -0.0598 654 THR C C   
14312 O O   . THR C 662 ? 0.5732 0.3636 0.2609 -0.1056 0.0456  -0.0587 654 THR C O   
14313 C CB  . THR C 662 ? 0.4823 0.2992 0.2073 -0.0903 0.0605  -0.0550 654 THR C CB  
14314 O OG1 . THR C 662 ? 0.4689 0.2905 0.1969 -0.0879 0.0630  -0.0513 654 THR C OG1 
14315 C CG2 . THR C 662 ? 0.5376 0.3635 0.2663 -0.0912 0.0432  -0.0536 654 THR C CG2 
14316 N N   . VAL C 663 ? 0.5188 0.3078 0.2221 -0.0985 0.0704  -0.0637 655 VAL C N   
14317 C CA  . VAL C 663 ? 0.5040 0.2847 0.1999 -0.1028 0.0678  -0.0669 655 VAL C CA  
14318 C C   . VAL C 663 ? 0.6057 0.3680 0.2755 -0.1107 0.0655  -0.0671 655 VAL C C   
14319 O O   . VAL C 663 ? 0.5195 0.2780 0.1799 -0.1164 0.0542  -0.0675 655 VAL C O   
14320 C CB  . VAL C 663 ? 0.4738 0.2518 0.1796 -0.0983 0.0813  -0.0704 655 VAL C CB  
14321 C CG1 . VAL C 663 ? 0.5377 0.3032 0.2314 -0.1040 0.0794  -0.0736 655 VAL C CG1 
14322 C CG2 . VAL C 663 ? 0.4810 0.2763 0.2121 -0.0908 0.0817  -0.0699 655 VAL C CG2 
14323 N N   . LYS C 664 ? 0.5767 0.3275 0.2349 -0.1113 0.0760  -0.0670 656 LYS C N   
14324 C CA  . LYS C 664 ? 0.6609 0.3922 0.2927 -0.1189 0.0745  -0.0673 656 LYS C CA  
14325 C C   . LYS C 664 ? 0.7003 0.4329 0.3223 -0.1235 0.0573  -0.0636 656 LYS C C   
14326 O O   . LYS C 664 ? 0.6747 0.3948 0.2784 -0.1300 0.0501  -0.0640 656 LYS C O   
14327 C CB  . LYS C 664 ? 0.6295 0.3492 0.2519 -0.1185 0.0891  -0.0676 656 LYS C CB  
14328 C CG  . LYS C 664 ? 0.6490 0.3628 0.2765 -0.1147 0.1056  -0.0716 656 LYS C CG  
14329 C CD  . LYS C 664 ? 0.7357 0.4394 0.3552 -0.1145 0.1196  -0.0720 656 LYS C CD  
14330 C CE  . LYS C 664 ? 0.7831 0.4872 0.4157 -0.1079 0.1357  -0.0751 656 LYS C CE  
14331 N NZ  . LYS C 664 ? 0.7894 0.4851 0.4159 -0.1074 0.1497  -0.0757 656 LYS C NZ  
14332 N N   . SER C 665 ? 0.6981 0.4458 0.3325 -0.1198 0.0501  -0.0598 657 SER C N   
14333 C CA  . SER C 665 ? 0.6815 0.4308 0.3084 -0.1227 0.0338  -0.0557 657 SER C CA  
14334 C C   . SER C 665 ? 0.7022 0.4587 0.3333 -0.1248 0.0185  -0.0559 657 SER C C   
14335 O O   . SER C 665 ? 0.7766 0.5324 0.4002 -0.1275 0.0046  -0.0529 657 SER C O   
14336 C CB  . SER C 665 ? 0.6147 0.3784 0.2551 -0.1174 0.0302  -0.0515 657 SER C CB  
14337 O OG  . SER C 665 ? 0.6029 0.3860 0.2666 -0.1118 0.0255  -0.0515 657 SER C OG  
14338 N N   . VAL C 666 ? 0.6127 0.3762 0.2566 -0.1236 0.0204  -0.0593 658 VAL C N   
14339 C CA  . VAL C 666 ? 0.6121 0.3835 0.2619 -0.1262 0.0066  -0.0597 658 VAL C CA  
14340 C C   . VAL C 666 ? 0.6644 0.4210 0.3004 -0.1326 0.0096  -0.0637 658 VAL C C   
14341 O O   . VAL C 666 ? 0.6623 0.4246 0.3035 -0.1357 -0.0002 -0.0648 658 VAL C O   
14342 C CB  . VAL C 666 ? 0.6707 0.4633 0.3470 -0.1208 0.0037  -0.0600 658 VAL C CB  
14343 C CG1 . VAL C 666 ? 0.5890 0.3953 0.2775 -0.1146 -0.0005 -0.0559 658 VAL C CG1 
14344 C CG2 . VAL C 666 ? 0.6963 0.4870 0.3805 -0.1181 0.0187  -0.0641 658 VAL C CG2 
14345 N N   . LEU C 667 ? 0.7181 0.4556 0.3368 -0.1347 0.0230  -0.0658 659 LEU C N   
14346 C CA  . LEU C 667 ? 0.7606 0.4809 0.3627 -0.1409 0.0259  -0.0692 659 LEU C CA  
14347 C C   . LEU C 667 ? 0.8754 0.5806 0.4532 -0.1482 0.0166  -0.0677 659 LEU C C   
14348 O O   . LEU C 667 ? 0.8874 0.5930 0.4599 -0.1478 0.0108  -0.0640 659 LEU C O   
14349 C CB  . LEU C 667 ? 0.7720 0.4787 0.3680 -0.1389 0.0452  -0.0724 659 LEU C CB  
14350 C CG  . LEU C 667 ? 0.7014 0.4206 0.3206 -0.1312 0.0556  -0.0741 659 LEU C CG  
14351 C CD1 . LEU C 667 ? 0.7269 0.4325 0.3403 -0.1283 0.0742  -0.0767 659 LEU C CD1 
14352 C CD2 . LEU C 667 ? 0.6938 0.4205 0.3246 -0.1321 0.0500  -0.0762 659 LEU C CD2 
14353 N N   . MET D 9   ? 0.5735 0.6267 0.6224 -0.0090 -0.1545 -0.0861 1   MET D N   
14354 C CA  . MET D 9   ? 0.4957 0.5498 0.5545 -0.0163 -0.1412 -0.0809 1   MET D CA  
14355 C C   . MET D 9   ? 0.4558 0.5214 0.5499 -0.0268 -0.1356 -0.0818 1   MET D C   
14356 O O   . MET D 9   ? 0.4555 0.5342 0.5732 -0.0274 -0.1394 -0.0831 1   MET D O   
14357 C CB  . MET D 9   ? 0.5066 0.5643 0.5620 -0.0115 -0.1374 -0.0733 1   MET D CB  
14358 C CG  . MET D 9   ? 0.5413 0.5833 0.5593 -0.0029 -0.1358 -0.0688 1   MET D CG  
14359 S SD  . MET D 9   ? 0.5971 0.6410 0.6065 0.0073  -0.1348 -0.0598 1   MET D SD  
14360 C CE  . MET D 9   ? 0.6268 0.6763 0.6358 0.0157  -0.1554 -0.0668 1   MET D CE  
14361 N N   . SER D 10  ? 0.4007 0.4603 0.4978 -0.0346 -0.1259 -0.0807 2   SER D N   
14362 C CA  . SER D 10  ? 0.3378 0.4049 0.4642 -0.0443 -0.1187 -0.0801 2   SER D CA  
14363 C C   . SER D 10  ? 0.2951 0.3711 0.4369 -0.0475 -0.1075 -0.0723 2   SER D C   
14364 O O   . SER D 10  ? 0.2852 0.3590 0.4140 -0.0439 -0.1043 -0.0678 2   SER D O   
14365 C CB  . SER D 10  ? 0.2892 0.3444 0.4111 -0.0505 -0.1133 -0.0817 2   SER D CB  
14366 O OG  . SER D 10  ? 0.3783 0.4248 0.4861 -0.0514 -0.1042 -0.0762 2   SER D OG  
14367 N N   . GLN D 11  ? 0.3229 0.4085 0.4924 -0.0542 -0.1014 -0.0710 3   GLN D N   
14368 C CA  . GLN D 11  ? 0.3125 0.4050 0.4956 -0.0580 -0.0885 -0.0637 3   GLN D CA  
14369 C C   . GLN D 11  ? 0.2523 0.3335 0.4206 -0.0612 -0.0787 -0.0584 3   GLN D C   
14370 O O   . GLN D 11  ? 0.2899 0.3734 0.4572 -0.0607 -0.0709 -0.0528 3   GLN D O   
14371 C CB  . GLN D 11  ? 0.3090 0.4104 0.5213 -0.0649 -0.0819 -0.0629 3   GLN D CB  
14372 C CG  . GLN D 11  ? 0.3693 0.4841 0.6018 -0.0620 -0.0903 -0.0676 3   GLN D CG  
14373 C CD  . GLN D 11  ? 0.4065 0.5319 0.6423 -0.0554 -0.0909 -0.0651 3   GLN D CD  
14374 O OE1 . GLN D 11  ? 0.4596 0.5839 0.6801 -0.0473 -0.1016 -0.0675 3   GLN D OE1 
14375 N NE2 . GLN D 11  ? 0.4028 0.5375 0.6575 -0.0583 -0.0787 -0.0601 3   GLN D NE2 
14376 N N   . LEU D 12  ? 0.2068 0.2753 0.3639 -0.0640 -0.0790 -0.0604 4   LEU D N   
14377 C CA  . LEU D 12  ? 0.2428 0.3000 0.3874 -0.0668 -0.0702 -0.0553 4   LEU D CA  
14378 C C   . LEU D 12  ? 0.2577 0.3085 0.3758 -0.0594 -0.0695 -0.0519 4   LEU D C   
14379 O O   . LEU D 12  ? 0.2393 0.2855 0.3479 -0.0594 -0.0591 -0.0443 4   LEU D O   
14380 C CB  . LEU D 12  ? 0.3108 0.3556 0.4492 -0.0700 -0.0711 -0.0586 4   LEU D CB  
14381 C CG  . LEU D 12  ? 0.3616 0.4088 0.5207 -0.0764 -0.0689 -0.0598 4   LEU D CG  
14382 C CD1 . LEU D 12  ? 0.3838 0.4166 0.5361 -0.0798 -0.0666 -0.0607 4   LEU D CD1 
14383 C CD2 . LEU D 12  ? 0.3300 0.3861 0.5082 -0.0811 -0.0577 -0.0524 4   LEU D CD2 
14384 N N   . ALA D 13  ? 0.2482 0.2972 0.3517 -0.0523 -0.0798 -0.0566 5   ALA D N   
14385 C CA  . ALA D 13  ? 0.2555 0.2977 0.3335 -0.0445 -0.0771 -0.0517 5   ALA D CA  
14386 C C   . ALA D 13  ? 0.1899 0.2419 0.2735 -0.0408 -0.0746 -0.0470 5   ALA D C   
14387 O O   . ALA D 13  ? 0.2185 0.2661 0.2895 -0.0377 -0.0669 -0.0406 5   ALA D O   
14388 C CB  . ALA D 13  ? 0.2560 0.2904 0.3130 -0.0376 -0.0873 -0.0572 5   ALA D CB  
14389 N N   . ASN D 14  ? 0.1938 0.2592 0.2983 -0.0408 -0.0813 -0.0508 6   ASN D N   
14390 C CA  . ASN D 14  ? 0.1605 0.2351 0.2713 -0.0361 -0.0795 -0.0472 6   ASN D CA  
14391 C C   . ASN D 14  ? 0.1887 0.2664 0.3082 -0.0403 -0.0653 -0.0407 6   ASN D C   
14392 O O   . ASN D 14  ? 0.1441 0.2228 0.2581 -0.0356 -0.0605 -0.0363 6   ASN D O   
14393 C CB  . ASN D 14  ? 0.1686 0.2579 0.3025 -0.0346 -0.0910 -0.0534 6   ASN D CB  
14394 C CG  . ASN D 14  ? 0.2263 0.3117 0.3442 -0.0264 -0.1063 -0.0585 6   ASN D CG  
14395 O OD1 . ASN D 14  ? 0.2689 0.3406 0.3572 -0.0210 -0.1060 -0.0558 6   ASN D OD1 
14396 N ND2 . ASN D 14  ? 0.1883 0.2849 0.3247 -0.0250 -0.1187 -0.0651 6   ASN D ND2 
14397 N N   . VAL D 15  ? 0.1946 0.2723 0.3257 -0.0485 -0.0583 -0.0399 7   VAL D N   
14398 C CA  . VAL D 15  ? 0.2059 0.2839 0.3392 -0.0514 -0.0448 -0.0333 7   VAL D CA  
14399 C C   . VAL D 15  ? 0.2385 0.3046 0.3461 -0.0477 -0.0397 -0.0282 7   VAL D C   
14400 O O   . VAL D 15  ? 0.1991 0.2660 0.3032 -0.0458 -0.0323 -0.0241 7   VAL D O   
14401 C CB  . VAL D 15  ? 0.2379 0.3156 0.3852 -0.0603 -0.0379 -0.0320 7   VAL D CB  
14402 C CG1 . VAL D 15  ? 0.2521 0.3161 0.3852 -0.0630 -0.0391 -0.0321 7   VAL D CG1 
14403 C CG2 . VAL D 15  ? 0.2121 0.2908 0.3603 -0.0620 -0.0240 -0.0251 7   VAL D CG2 
14404 N N   . ILE D 16  ? 0.1383 0.1933 0.2285 -0.0464 -0.0438 -0.0292 8   ILE D N   
14405 C CA  . ILE D 16  ? 0.1792 0.2240 0.2488 -0.0428 -0.0396 -0.0250 8   ILE D CA  
14406 C C   . ILE D 16  ? 0.1974 0.2440 0.2606 -0.0356 -0.0412 -0.0238 8   ILE D C   
14407 O O   . ILE D 16  ? 0.1960 0.2397 0.2527 -0.0337 -0.0351 -0.0199 8   ILE D O   
14408 C CB  . ILE D 16  ? 0.1798 0.2132 0.2348 -0.0424 -0.0427 -0.0266 8   ILE D CB  
14409 C CG1 . ILE D 16  ? 0.2082 0.2378 0.2694 -0.0492 -0.0400 -0.0269 8   ILE D CG1 
14410 C CG2 . ILE D 16  ? 0.1886 0.2131 0.2262 -0.0383 -0.0385 -0.0225 8   ILE D CG2 
14411 C CD1 . ILE D 16  ? 0.1743 0.1929 0.2236 -0.0485 -0.0430 -0.0298 8   ILE D CD1 
14412 N N   . ARG D 17  ? 0.2138 0.2642 0.2780 -0.0311 -0.0504 -0.0274 9   ARG D N   
14413 C CA  . ARG D 17  ? 0.2088 0.2598 0.2670 -0.0234 -0.0526 -0.0257 9   ARG D CA  
14414 C C   . ARG D 17  ? 0.1726 0.2317 0.2435 -0.0231 -0.0463 -0.0235 9   ARG D C   
14415 O O   . ARG D 17  ? 0.1563 0.2109 0.2190 -0.0190 -0.0420 -0.0201 9   ARG D O   
14416 C CB  . ARG D 17  ? 0.1581 0.2138 0.2184 -0.0183 -0.0650 -0.0302 9   ARG D CB  
14417 C CG  . ARG D 17  ? 0.1702 0.2163 0.2133 -0.0168 -0.0719 -0.0334 9   ARG D CG  
14418 C CD  . ARG D 17  ? 0.1996 0.2471 0.2368 -0.0092 -0.0853 -0.0372 9   ARG D CD  
14419 N NE  . ARG D 17  ? 0.2938 0.3269 0.3042 -0.0054 -0.0874 -0.0376 9   ARG D NE  
14420 C CZ  . ARG D 17  ? 0.2849 0.3137 0.2901 -0.0079 -0.0926 -0.0438 9   ARG D CZ  
14421 N NH1 . ARG D 17  ? 0.2116 0.2496 0.2384 -0.0146 -0.0976 -0.0502 9   ARG D NH1 
14422 N NH2 . ARG D 17  ? 0.2851 0.2999 0.2641 -0.0036 -0.0922 -0.0437 9   ARG D NH2 
14423 N N   . PHE D 18  ? 0.1808 0.2515 0.2728 -0.0274 -0.0449 -0.0256 10  PHE D N   
14424 C CA  . PHE D 18  ? 0.1915 0.2704 0.2958 -0.0259 -0.0383 -0.0241 10  PHE D CA  
14425 C C   . PHE D 18  ? 0.1859 0.2593 0.2831 -0.0293 -0.0267 -0.0204 10  PHE D C   
14426 O O   . PHE D 18  ? 0.1418 0.2147 0.2364 -0.0257 -0.0214 -0.0189 10  PHE D O   
14427 C CB  . PHE D 18  ? 0.1834 0.2777 0.3149 -0.0284 -0.0402 -0.0277 10  PHE D CB  
14428 C CG  . PHE D 18  ? 0.2169 0.3184 0.3567 -0.0225 -0.0528 -0.0316 10  PHE D CG  
14429 C CD1 . PHE D 18  ? 0.1392 0.2436 0.2795 -0.0144 -0.0545 -0.0305 10  PHE D CD1 
14430 C CD2 . PHE D 18  ? 0.2257 0.3293 0.3702 -0.0243 -0.0640 -0.0365 10  PHE D CD2 
14431 C CE1 . PHE D 18  ? 0.1471 0.2569 0.2928 -0.0076 -0.0675 -0.0334 10  PHE D CE1 
14432 C CE2 . PHE D 18  ? 0.2266 0.3356 0.3753 -0.0178 -0.0775 -0.0405 10  PHE D CE2 
14433 C CZ  . PHE D 18  ? 0.2392 0.3516 0.3885 -0.0092 -0.0795 -0.0384 10  PHE D CZ  
14434 N N   . LEU D 19  ? 0.1999 0.2681 0.2928 -0.0355 -0.0233 -0.0192 11  LEU D N   
14435 C CA  . LEU D 19  ? 0.1995 0.2602 0.2810 -0.0373 -0.0147 -0.0156 11  LEU D CA  
14436 C C   . LEU D 19  ? 0.2008 0.2520 0.2654 -0.0326 -0.0155 -0.0143 11  LEU D C   
14437 O O   . LEU D 19  ? 0.2019 0.2505 0.2613 -0.0308 -0.0102 -0.0132 11  LEU D O   
14438 C CB  . LEU D 19  ? 0.1977 0.2526 0.2758 -0.0435 -0.0129 -0.0140 11  LEU D CB  
14439 C CG  . LEU D 19  ? 0.1506 0.2110 0.2430 -0.0494 -0.0070 -0.0129 11  LEU D CG  
14440 C CD1 . LEU D 19  ? 0.1992 0.2505 0.2852 -0.0543 -0.0066 -0.0107 11  LEU D CD1 
14441 C CD2 . LEU D 19  ? 0.1696 0.2324 0.2614 -0.0486 0.0032  -0.0101 11  LEU D CD2 
14442 N N   . SER D 20  ? 0.1361 0.1813 0.1921 -0.0306 -0.0216 -0.0147 12  SER D N   
14443 C CA  . SER D 20  ? 0.1545 0.1901 0.1969 -0.0268 -0.0211 -0.0128 12  SER D CA  
14444 C C   . SER D 20  ? 0.1776 0.2152 0.2219 -0.0207 -0.0209 -0.0127 12  SER D C   
14445 O O   . SER D 20  ? 0.1697 0.2019 0.2090 -0.0191 -0.0168 -0.0116 12  SER D O   
14446 C CB  . SER D 20  ? 0.2051 0.2337 0.2378 -0.0256 -0.0258 -0.0127 12  SER D CB  
14447 O OG  . SER D 20  ? 0.1975 0.2235 0.2293 -0.0307 -0.0255 -0.0133 12  SER D OG  
14448 N N   . ALA D 21  ? 0.1717 0.2165 0.2241 -0.0171 -0.0263 -0.0142 13  ALA D N   
14449 C CA  . ALA D 21  ? 0.2005 0.2470 0.2560 -0.0104 -0.0269 -0.0137 13  ALA D CA  
14450 C C   . ALA D 21  ? 0.1766 0.2283 0.2412 -0.0107 -0.0197 -0.0147 13  ALA D C   
14451 O O   . ALA D 21  ? 0.1620 0.2084 0.2228 -0.0069 -0.0164 -0.0141 13  ALA D O   
14452 C CB  . ALA D 21  ? 0.1762 0.2309 0.2405 -0.0061 -0.0357 -0.0156 13  ALA D CB  
14453 N N   . ASP D 22  ? 0.1868 0.2478 0.2632 -0.0152 -0.0164 -0.0163 14  ASP D N   
14454 C CA  . ASP D 22  ? 0.1626 0.2285 0.2463 -0.0149 -0.0080 -0.0172 14  ASP D CA  
14455 C C   . ASP D 22  ? 0.1863 0.2417 0.2548 -0.0164 -0.0019 -0.0164 14  ASP D C   
14456 O O   . ASP D 22  ? 0.1530 0.2071 0.2204 -0.0131 0.0033  -0.0179 14  ASP D O   
14457 C CB  . ASP D 22  ? 0.1296 0.2065 0.2286 -0.0201 -0.0041 -0.0180 14  ASP D CB  
14458 C CG  . ASP D 22  ? 0.2082 0.2983 0.3285 -0.0184 -0.0101 -0.0204 14  ASP D CG  
14459 O OD1 . ASP D 22  ? 0.2345 0.3268 0.3583 -0.0116 -0.0158 -0.0213 14  ASP D OD1 
14460 O OD2 . ASP D 22  ? 0.1719 0.2701 0.3067 -0.0238 -0.0096 -0.0213 14  ASP D OD2 
14461 N N   . ALA D 23  ? 0.1315 0.1796 0.1890 -0.0209 -0.0030 -0.0148 15  ALA D N   
14462 C CA  . ALA D 23  ? 0.1917 0.2308 0.2361 -0.0223 0.0009  -0.0146 15  ALA D CA  
14463 C C   . ALA D 23  ? 0.1833 0.2137 0.2209 -0.0183 -0.0011 -0.0152 15  ALA D C   
14464 O O   . ALA D 23  ? 0.1820 0.2072 0.2139 -0.0170 0.0020  -0.0173 15  ALA D O   
14465 C CB  . ALA D 23  ? 0.1794 0.2137 0.2167 -0.0277 -0.0005 -0.0125 15  ALA D CB  
14466 N N   . VAL D 24  ? 0.1873 0.2149 0.2248 -0.0163 -0.0061 -0.0137 16  VAL D N   
14467 C CA  . VAL D 24  ? 0.1511 0.1700 0.1844 -0.0124 -0.0067 -0.0132 16  VAL D CA  
14468 C C   . VAL D 24  ? 0.1892 0.2100 0.2286 -0.0070 -0.0044 -0.0152 16  VAL D C   
14469 O O   . VAL D 24  ? 0.2032 0.2163 0.2399 -0.0050 -0.0022 -0.0167 16  VAL D O   
14470 C CB  . VAL D 24  ? 0.1708 0.1858 0.2009 -0.0105 -0.0110 -0.0101 16  VAL D CB  
14471 C CG1 . VAL D 24  ? 0.2099 0.2158 0.2376 -0.0055 -0.0102 -0.0083 16  VAL D CG1 
14472 C CG2 . VAL D 24  ? 0.1891 0.1995 0.2126 -0.0153 -0.0117 -0.0088 16  VAL D CG2 
14473 N N   . GLN D 25  ? 0.1507 0.1819 0.2005 -0.0044 -0.0051 -0.0156 17  GLN D N   
14474 C CA  . GLN D 25  ? 0.1521 0.1857 0.2098 0.0017  -0.0029 -0.0174 17  GLN D CA  
14475 C C   . GLN D 25  ? 0.1741 0.2070 0.2304 0.0010  0.0044  -0.0213 17  GLN D C   
14476 O O   . GLN D 25  ? 0.2391 0.2662 0.2950 0.0053  0.0069  -0.0237 17  GLN D O   
14477 C CB  . GLN D 25  ? 0.1876 0.2344 0.2601 0.0046  -0.0058 -0.0176 17  GLN D CB  
14478 C CG  . GLN D 25  ? 0.2200 0.2685 0.3020 0.0127  -0.0058 -0.0184 17  GLN D CG  
14479 C CD  . GLN D 25  ? 0.1902 0.2269 0.2641 0.0179  -0.0104 -0.0149 17  GLN D CD  
14480 O OE1 . GLN D 25  ? 0.1833 0.2163 0.2493 0.0173  -0.0161 -0.0115 17  GLN D OE1 
14481 N NE2 . GLN D 25  ? 0.1995 0.2291 0.2746 0.0232  -0.0072 -0.0156 17  GLN D NE2 
14482 N N   . LYS D 26  ? 0.1492 0.1865 0.2032 -0.0041 0.0080  -0.0219 18  LYS D N   
14483 C CA  . LYS D 26  ? 0.2595 0.2950 0.3077 -0.0040 0.0154  -0.0254 18  LYS D CA  
14484 C C   . LYS D 26  ? 0.2618 0.2839 0.2960 -0.0042 0.0141  -0.0277 18  LYS D C   
14485 O O   . LYS D 26  ? 0.2164 0.2337 0.2465 -0.0010 0.0179  -0.0323 18  LYS D O   
14486 C CB  . LYS D 26  ? 0.2296 0.2705 0.2758 -0.0092 0.0198  -0.0239 18  LYS D CB  
14487 C CG  . LYS D 26  ? 0.2286 0.2679 0.2666 -0.0081 0.0290  -0.0267 18  LYS D CG  
14488 C CD  . LYS D 26  ? 0.1777 0.2220 0.2147 -0.0129 0.0347  -0.0234 18  LYS D CD  
14489 C CE  . LYS D 26  ? 0.2383 0.2796 0.2632 -0.0111 0.0452  -0.0253 18  LYS D CE  
14490 N NZ  . LYS D 26  ? 0.2251 0.2524 0.2262 -0.0106 0.0420  -0.0276 18  LYS D NZ  
14491 N N   . ALA D 27  ? 0.2432 0.2593 0.2715 -0.0079 0.0088  -0.0254 19  ALA D N   
14492 C CA  . ALA D 27  ? 0.2086 0.2133 0.2289 -0.0085 0.0064  -0.0278 19  ALA D CA  
14493 C C   . ALA D 27  ? 0.2468 0.2448 0.2727 -0.0042 0.0053  -0.0287 19  ALA D C   
14494 O O   . ALA D 27  ? 0.2058 0.1943 0.2286 -0.0042 0.0043  -0.0322 19  ALA D O   
14495 C CB  . ALA D 27  ? 0.1724 0.1741 0.1888 -0.0134 0.0019  -0.0247 19  ALA D CB  
14496 N N   . ASN D 28  ? 0.2024 0.2048 0.2371 -0.0003 0.0050  -0.0257 20  ASN D N   
14497 C CA  . ASN D 28  ? 0.2542 0.2487 0.2931 0.0040  0.0037  -0.0241 20  ASN D CA  
14498 C C   . ASN D 28  ? 0.2598 0.2442 0.2948 0.0006  0.0015  -0.0220 20  ASN D C   
14499 O O   . ASN D 28  ? 0.2346 0.2086 0.2718 0.0021  0.0023  -0.0228 20  ASN D O   
14500 C CB  . ASN D 28  ? 0.3620 0.3515 0.4041 0.0089  0.0071  -0.0292 20  ASN D CB  
14501 C CG  . ASN D 28  ? 0.4664 0.4491 0.5152 0.0148  0.0064  -0.0262 20  ASN D CG  
14502 O OD1 . ASN D 28  ? 0.4170 0.4024 0.4680 0.0171  0.0035  -0.0203 20  ASN D OD1 
14503 N ND2 . ASN D 28  ? 0.5732 0.5459 0.6242 0.0176  0.0087  -0.0304 20  ASN D ND2 
14504 N N   . SER D 29  ? 0.2012 0.1885 0.2321 -0.0041 -0.0006 -0.0192 21  SER D N   
14505 C CA  . SER D 29  ? 0.2245 0.2040 0.2538 -0.0077 -0.0017 -0.0175 21  SER D CA  
14506 C C   . SER D 29  ? 0.2108 0.1953 0.2366 -0.0110 -0.0035 -0.0138 21  SER D C   
14507 O O   . SER D 29  ? 0.2264 0.2188 0.2501 -0.0131 -0.0044 -0.0148 21  SER D O   
14508 C CB  . SER D 29  ? 0.1911 0.1661 0.2193 -0.0110 -0.0024 -0.0231 21  SER D CB  
14509 O OG  . SER D 29  ? 0.1982 0.1676 0.2291 -0.0147 -0.0037 -0.0219 21  SER D OG  
14510 N N   . GLY D 30  ? 0.1969 0.1757 0.2220 -0.0113 -0.0032 -0.0096 22  GLY D N   
14511 C CA  . GLY D 30  ? 0.1943 0.1764 0.2156 -0.0143 -0.0046 -0.0072 22  GLY D CA  
14512 C C   . GLY D 30  ? 0.1987 0.1792 0.2152 -0.0109 -0.0049 -0.0025 22  GLY D C   
14513 O O   . GLY D 30  ? 0.2673 0.2430 0.2827 -0.0059 -0.0039 0.0003  22  GLY D O   
14514 N N   . HIS D 31  ? 0.1887 0.1723 0.2010 -0.0131 -0.0066 -0.0018 23  HIS D N   
14515 C CA  . HIS D 31  ? 0.1908 0.1703 0.1950 -0.0103 -0.0067 0.0019  23  HIS D CA  
14516 C C   . HIS D 31  ? 0.2145 0.2021 0.2158 -0.0100 -0.0121 0.0002  23  HIS D C   
14517 O O   . HIS D 31  ? 0.2081 0.1986 0.2092 -0.0141 -0.0133 -0.0015 23  HIS D O   
14518 C CB  . HIS D 31  ? 0.2251 0.1985 0.2276 -0.0132 -0.0029 0.0035  23  HIS D CB  
14519 C CG  . HIS D 31  ? 0.3000 0.2663 0.3097 -0.0143 0.0022  0.0046  23  HIS D CG  
14520 N ND1 . HIS D 31  ? 0.2843 0.2526 0.3032 -0.0178 0.0012  0.0007  23  HIS D ND1 
14521 C CD2 . HIS D 31  ? 0.3020 0.2586 0.3115 -0.0125 0.0082  0.0090  23  HIS D CD2 
14522 C CE1 . HIS D 31  ? 0.3078 0.2688 0.3341 -0.0184 0.0052  0.0017  23  HIS D CE1 
14523 N NE2 . HIS D 31  ? 0.3029 0.2568 0.3250 -0.0156 0.0104  0.0071  23  HIS D NE2 
14524 N N   . PRO D 32  ? 0.2028 0.1942 0.2038 -0.0052 -0.0160 0.0004  24  PRO D N   
14525 C CA  . PRO D 32  ? 0.2008 0.2015 0.2038 -0.0054 -0.0224 -0.0024 24  PRO D CA  
14526 C C   . PRO D 32  ? 0.1954 0.1919 0.1863 -0.0023 -0.0266 -0.0016 24  PRO D C   
14527 O O   . PRO D 32  ? 0.1877 0.1902 0.1800 -0.0042 -0.0320 -0.0052 24  PRO D O   
14528 C CB  . PRO D 32  ? 0.2558 0.2636 0.2673 -0.0012 -0.0251 -0.0033 24  PRO D CB  
14529 C CG  . PRO D 32  ? 0.2690 0.2671 0.2758 0.0041  -0.0219 0.0007  24  PRO D CG  
14530 C CD  . PRO D 32  ? 0.2520 0.2409 0.2554 0.0002  -0.0153 0.0022  24  PRO D CD  
14531 N N   . GLY D 33  ? 0.2488 0.2341 0.2271 0.0025  -0.0239 0.0029  25  GLY D N   
14532 C CA  . GLY D 33  ? 0.2774 0.2574 0.2400 0.0076  -0.0282 0.0038  25  GLY D CA  
14533 C C   . GLY D 33  ? 0.2649 0.2420 0.2202 0.0041  -0.0273 0.0014  25  GLY D C   
14534 O O   . GLY D 33  ? 0.2027 0.1812 0.1506 0.0058  -0.0344 -0.0021 25  GLY D O   
14535 N N   . ALA D 34  ? 0.2155 0.1884 0.1736 -0.0004 -0.0194 0.0027  26  ALA D N   
14536 C CA  . ALA D 34  ? 0.2324 0.2021 0.1851 -0.0031 -0.0179 0.0003  26  ALA D CA  
14537 C C   . ALA D 34  ? 0.2253 0.2046 0.1884 -0.0088 -0.0237 -0.0055 26  ALA D C   
14538 O O   . ALA D 34  ? 0.2231 0.2009 0.1799 -0.0090 -0.0273 -0.0092 26  ALA D O   
14539 C CB  . ALA D 34  ? 0.2346 0.1981 0.1908 -0.0060 -0.0081 0.0032  26  ALA D CB  
14540 N N   . PRO D 35  ? 0.2197 0.2076 0.1979 -0.0133 -0.0242 -0.0065 27  PRO D N   
14541 C CA  . PRO D 35  ? 0.1957 0.1920 0.1836 -0.0182 -0.0289 -0.0109 27  PRO D CA  
14542 C C   . PRO D 35  ? 0.2103 0.2115 0.1975 -0.0157 -0.0377 -0.0149 27  PRO D C   
14543 O O   . PRO D 35  ? 0.2395 0.2420 0.2286 -0.0187 -0.0418 -0.0192 27  PRO D O   
14544 C CB  . PRO D 35  ? 0.1913 0.1948 0.1921 -0.0213 -0.0265 -0.0101 27  PRO D CB  
14545 C CG  . PRO D 35  ? 0.1875 0.1843 0.1856 -0.0207 -0.0202 -0.0066 27  PRO D CG  
14546 C CD  . PRO D 35  ? 0.1832 0.1718 0.1696 -0.0148 -0.0191 -0.0039 27  PRO D CD  
14547 N N   . MET D 36  ? 0.1755 0.1792 0.1610 -0.0102 -0.0416 -0.0138 28  MET D N   
14548 C CA  . MET D 36  ? 0.1810 0.1898 0.1665 -0.0069 -0.0520 -0.0180 28  MET D CA  
14549 C C   . MET D 36  ? 0.2350 0.2341 0.2013 -0.0033 -0.0560 -0.0203 28  MET D C   
14550 O O   . MET D 36  ? 0.2570 0.2593 0.2248 -0.0042 -0.0645 -0.0266 28  MET D O   
14551 C CB  . MET D 36  ? 0.2041 0.2164 0.1909 -0.0002 -0.0555 -0.0156 28  MET D CB  
14552 C CG  . MET D 36  ? 0.2265 0.2488 0.2327 -0.0032 -0.0518 -0.0150 28  MET D CG  
14553 S SD  . MET D 36  ? 0.2482 0.2722 0.2561 0.0055  -0.0541 -0.0116 28  MET D SD  
14554 C CE  . MET D 36  ? 0.2366 0.2700 0.2498 0.0102  -0.0690 -0.0167 28  MET D CE  
14555 N N   . GLY D 37  ? 0.2435 0.2305 0.1919 0.0009  -0.0495 -0.0156 29  GLY D N   
14556 C CA  . GLY D 37  ? 0.2259 0.2022 0.1530 0.0052  -0.0510 -0.0173 29  GLY D CA  
14557 C C   . GLY D 37  ? 0.2231 0.1976 0.1523 -0.0005 -0.0496 -0.0224 29  GLY D C   
14558 O O   . GLY D 37  ? 0.2665 0.2354 0.1823 0.0021  -0.0548 -0.0276 29  GLY D O   
14559 N N   . MET D 38  ? 0.2054 0.1834 0.1501 -0.0076 -0.0430 -0.0213 30  MET D N   
14560 C CA  . MET D 38  ? 0.2029 0.1781 0.1508 -0.0125 -0.0409 -0.0250 30  MET D CA  
14561 C C   . MET D 38  ? 0.2189 0.2031 0.1842 -0.0189 -0.0474 -0.0303 30  MET D C   
14562 O O   . MET D 38  ? 0.2232 0.2053 0.1945 -0.0237 -0.0453 -0.0326 30  MET D O   
14563 C CB  . MET D 38  ? 0.1923 0.1645 0.1459 -0.0157 -0.0302 -0.0201 30  MET D CB  
14564 C CG  . MET D 38  ? 0.2693 0.2313 0.2091 -0.0107 -0.0216 -0.0155 30  MET D CG  
14565 S SD  . MET D 38  ? 0.2654 0.2254 0.2174 -0.0152 -0.0112 -0.0120 30  MET D SD  
14566 C CE  . MET D 38  ? 0.2903 0.2577 0.2556 -0.0174 -0.0106 -0.0076 30  MET D CE  
14567 N N   . ALA D 39  ? 0.1959 0.1901 0.1712 -0.0189 -0.0549 -0.0322 31  ALA D N   
14568 C CA  . ALA D 39  ? 0.2161 0.2198 0.2123 -0.0258 -0.0586 -0.0360 31  ALA D CA  
14569 C C   . ALA D 39  ? 0.2130 0.2130 0.2092 -0.0283 -0.0648 -0.0437 31  ALA D C   
14570 O O   . ALA D 39  ? 0.2352 0.2363 0.2452 -0.0351 -0.0627 -0.0451 31  ALA D O   
14571 C CB  . ALA D 39  ? 0.1898 0.2058 0.1991 -0.0247 -0.0647 -0.0368 31  ALA D CB  
14572 N N   . GLU D 40  ? 0.2117 0.2059 0.1915 -0.0224 -0.0725 -0.0489 32  GLU D N   
14573 C CA  . GLU D 40  ? 0.2239 0.2130 0.2022 -0.0244 -0.0790 -0.0577 32  GLU D CA  
14574 C C   . GLU D 40  ? 0.2979 0.2753 0.2678 -0.0259 -0.0701 -0.0570 32  GLU D C   
14575 O O   . GLU D 40  ? 0.2622 0.2370 0.2413 -0.0310 -0.0715 -0.0621 32  GLU D O   
14576 C CB  . GLU D 40  ? 0.2469 0.2315 0.2061 -0.0167 -0.0905 -0.0643 32  GLU D CB  
14577 C CG  . GLU D 40  ? 0.2840 0.2810 0.2584 -0.0166 -0.1038 -0.0693 32  GLU D CG  
14578 C CD  . GLU D 40  ? 0.3369 0.3429 0.3160 -0.0130 -0.1026 -0.0620 32  GLU D CD  
14579 O OE1 . GLU D 40  ? 0.3162 0.3150 0.2757 -0.0067 -0.0964 -0.0551 32  GLU D OE1 
14580 O OE2 . GLU D 40  ? 0.2559 0.2758 0.2596 -0.0164 -0.1072 -0.0632 32  GLU D OE2 
14581 N N   . MET D 41  ? 0.2489 0.2191 0.2034 -0.0215 -0.0609 -0.0507 33  MET D N   
14582 C CA  . MET D 41  ? 0.2249 0.1861 0.1762 -0.0228 -0.0516 -0.0493 33  MET D CA  
14583 C C   . MET D 41  ? 0.2190 0.1853 0.1924 -0.0308 -0.0478 -0.0466 33  MET D C   
14584 O O   . MET D 41  ? 0.2546 0.2153 0.2328 -0.0340 -0.0462 -0.0494 33  MET D O   
14585 C CB  . MET D 41  ? 0.2259 0.1815 0.1637 -0.0177 -0.0417 -0.0421 33  MET D CB  
14586 C CG  . MET D 41  ? 0.2585 0.2060 0.1707 -0.0089 -0.0431 -0.0430 33  MET D CG  
14587 S SD  . MET D 41  ? 0.2969 0.2405 0.1995 -0.0039 -0.0313 -0.0323 33  MET D SD  
14588 C CE  . MET D 41  ? 0.2607 0.1986 0.1702 -0.0067 -0.0181 -0.0299 33  MET D CE  
14589 N N   . ALA D 42  ? 0.1920 0.1678 0.1774 -0.0335 -0.0460 -0.0408 34  ALA D N   
14590 C CA  . ALA D 42  ? 0.2072 0.1869 0.2097 -0.0401 -0.0421 -0.0373 34  ALA D CA  
14591 C C   . ALA D 42  ? 0.2586 0.2409 0.2756 -0.0459 -0.0475 -0.0425 34  ALA D C   
14592 O O   . ALA D 42  ? 0.2484 0.2265 0.2738 -0.0505 -0.0445 -0.0418 34  ALA D O   
14593 C CB  . ALA D 42  ? 0.1979 0.1863 0.2069 -0.0407 -0.0392 -0.0312 34  ALA D CB  
14594 N N   . GLU D 43  ? 0.2369 0.2263 0.2591 -0.0458 -0.0557 -0.0474 35  GLU D N   
14595 C CA  . GLU D 43  ? 0.2553 0.2480 0.2954 -0.0520 -0.0611 -0.0531 35  GLU D CA  
14596 C C   . GLU D 43  ? 0.2291 0.2100 0.2652 -0.0532 -0.0628 -0.0592 35  GLU D C   
14597 O O   . GLU D 43  ? 0.2143 0.1923 0.2642 -0.0593 -0.0599 -0.0588 35  GLU D O   
14598 C CB  . GLU D 43  ? 0.2259 0.2279 0.2724 -0.0505 -0.0718 -0.0592 35  GLU D CB  
14599 C CG  . GLU D 43  ? 0.3208 0.3263 0.3891 -0.0573 -0.0785 -0.0667 35  GLU D CG  
14600 C CD  . GLU D 43  ? 0.3753 0.3907 0.4513 -0.0552 -0.0905 -0.0736 35  GLU D CD  
14601 O OE1 . GLU D 43  ? 0.3952 0.4144 0.4876 -0.0595 -0.0925 -0.0769 35  GLU D OE1 
14602 O OE2 . GLU D 43  ? 0.3490 0.3677 0.4128 -0.0482 -0.0959 -0.0736 35  GLU D OE2 
14603 N N   . THR D 44  ? 0.2410 0.2139 0.2571 -0.0469 -0.0665 -0.0645 36  THR D N   
14604 C CA  . THR D 44  ? 0.2352 0.1960 0.2455 -0.0469 -0.0681 -0.0719 36  THR D CA  
14605 C C   . THR D 44  ? 0.2220 0.1751 0.2350 -0.0490 -0.0579 -0.0665 36  THR D C   
14606 O O   . THR D 44  ? 0.2785 0.2264 0.3038 -0.0540 -0.0579 -0.0693 36  THR D O   
14607 C CB  . THR D 44  ? 0.2711 0.2238 0.2548 -0.0382 -0.0717 -0.0775 36  THR D CB  
14608 O OG1 . THR D 44  ? 0.3250 0.2846 0.3047 -0.0351 -0.0824 -0.0816 36  THR D OG1 
14609 C CG2 . THR D 44  ? 0.2652 0.2050 0.2421 -0.0377 -0.0744 -0.0873 36  THR D CG2 
14610 N N   . LEU D 45  ? 0.2366 0.1887 0.2398 -0.0451 -0.0497 -0.0589 37  LEU D N   
14611 C CA  . LEU D 45  ? 0.2327 0.1783 0.2393 -0.0460 -0.0415 -0.0542 37  LEU D CA  
14612 C C   . LEU D 45  ? 0.2726 0.2216 0.2986 -0.0531 -0.0398 -0.0491 37  LEU D C   
14613 O O   . LEU D 45  ? 0.2389 0.1802 0.2725 -0.0559 -0.0384 -0.0501 37  LEU D O   
14614 C CB  . LEU D 45  ? 0.2028 0.1491 0.2001 -0.0413 -0.0340 -0.0470 37  LEU D CB  
14615 C CG  . LEU D 45  ? 0.2194 0.1605 0.2233 -0.0420 -0.0271 -0.0425 37  LEU D CG  
14616 C CD1 . LEU D 45  ? 0.2210 0.1504 0.2213 -0.0399 -0.0258 -0.0489 37  LEU D CD1 
14617 C CD2 . LEU D 45  ? 0.2138 0.1573 0.2142 -0.0385 -0.0205 -0.0357 37  LEU D CD2 
14618 N N   . TRP D 46  ? 0.1879 0.1472 0.2210 -0.0556 -0.0394 -0.0435 38  TRP D N   
14619 C CA  . TRP D 46  ? 0.2278 0.1892 0.2748 -0.0611 -0.0356 -0.0370 38  TRP D CA  
14620 C C   . TRP D 46  ? 0.2553 0.2162 0.3187 -0.0677 -0.0387 -0.0407 38  TRP D C   
14621 O O   . TRP D 46  ? 0.2511 0.2068 0.3239 -0.0718 -0.0347 -0.0362 38  TRP D O   
14622 C CB  . TRP D 46  ? 0.2204 0.1921 0.2682 -0.0611 -0.0330 -0.0305 38  TRP D CB  
14623 C CG  . TRP D 46  ? 0.1764 0.1466 0.2144 -0.0569 -0.0283 -0.0247 38  TRP D CG  
14624 C CD1 . TRP D 46  ? 0.2049 0.1722 0.2313 -0.0515 -0.0275 -0.0260 38  TRP D CD1 
14625 C CD2 . TRP D 46  ? 0.2018 0.1725 0.2417 -0.0580 -0.0239 -0.0171 38  TRP D CD2 
14626 N NE1 . TRP D 46  ? 0.2257 0.1928 0.2503 -0.0498 -0.0232 -0.0201 38  TRP D NE1 
14627 C CE2 . TRP D 46  ? 0.1903 0.1595 0.2220 -0.0534 -0.0220 -0.0151 38  TRP D CE2 
14628 C CE3 . TRP D 46  ? 0.2486 0.2204 0.2956 -0.0621 -0.0213 -0.0118 38  TRP D CE3 
14629 C CZ2 . TRP D 46  ? 0.1931 0.1625 0.2243 -0.0528 -0.0197 -0.0093 38  TRP D CZ2 
14630 C CZ3 . TRP D 46  ? 0.2684 0.2392 0.3107 -0.0607 -0.0183 -0.0054 38  TRP D CZ3 
14631 C CH2 . TRP D 46  ? 0.1895 0.1594 0.2244 -0.0561 -0.0186 -0.0047 38  TRP D CH2 
14632 N N   . THR D 47  ? 0.2098 0.1754 0.2778 -0.0687 -0.0460 -0.0486 39  THR D N   
14633 C CA  . THR D 47  ? 0.2667 0.2324 0.3546 -0.0758 -0.0490 -0.0528 39  THR D CA  
14634 C C   . THR D 47  ? 0.3011 0.2547 0.3863 -0.0755 -0.0513 -0.0596 39  THR D C   
14635 O O   . THR D 47  ? 0.3377 0.2881 0.4348 -0.0800 -0.0488 -0.0584 39  THR D O   
14636 C CB  . THR D 47  ? 0.2627 0.2410 0.3585 -0.0764 -0.0551 -0.0571 39  THR D CB  
14637 O OG1 . THR D 47  ? 0.2733 0.2501 0.3569 -0.0713 -0.0647 -0.0668 39  THR D OG1 
14638 C CG2 . THR D 47  ? 0.2433 0.2337 0.3429 -0.0761 -0.0526 -0.0512 39  THR D CG2 
14639 N N   . LYS D 48  ? 0.3137 0.2595 0.3831 -0.0701 -0.0555 -0.0669 40  LYS D N   
14640 C CA  . LYS D 48  ? 0.2998 0.2340 0.3654 -0.0691 -0.0579 -0.0751 40  LYS D CA  
14641 C C   . LYS D 48  ? 0.2982 0.2188 0.3590 -0.0671 -0.0519 -0.0734 40  LYS D C   
14642 O O   . LYS D 48  ? 0.2819 0.1925 0.3449 -0.0677 -0.0516 -0.0777 40  LYS D O   
14643 C CB  . LYS D 48  ? 0.2913 0.2239 0.3400 -0.0634 -0.0667 -0.0861 40  LYS D CB  
14644 C CG  . LYS D 48  ? 0.3640 0.3094 0.4177 -0.0640 -0.0749 -0.0893 40  LYS D CG  
14645 C CD  . LYS D 48  ? 0.3993 0.3492 0.4751 -0.0710 -0.0754 -0.0892 40  LYS D CD  
14646 C CE  . LYS D 48  ? 0.5032 0.4627 0.5832 -0.0702 -0.0856 -0.0960 40  LYS D CE  
14647 N NZ  . LYS D 48  ? 0.5896 0.5401 0.6534 -0.0654 -0.0940 -0.1075 40  LYS D NZ  
14648 N N   . PHE D 49  ? 0.2341 0.1563 0.2850 -0.0627 -0.0448 -0.0647 41  PHE D N   
14649 C CA  . PHE D 49  ? 0.2982 0.2094 0.3441 -0.0589 -0.0389 -0.0632 41  PHE D CA  
14650 C C   . PHE D 49  ? 0.2766 0.1891 0.3291 -0.0597 -0.0322 -0.0512 41  PHE D C   
14651 O O   . PHE D 49  ? 0.2896 0.1926 0.3482 -0.0596 -0.0291 -0.0493 41  PHE D O   
14652 C CB  . PHE D 49  ? 0.2912 0.2000 0.3168 -0.0507 -0.0369 -0.0668 41  PHE D CB  
14653 C CG  . PHE D 49  ? 0.2569 0.1615 0.2699 -0.0480 -0.0437 -0.0788 41  PHE D CG  
14654 C CD1 . PHE D 49  ? 0.2753 0.1665 0.2837 -0.0459 -0.0444 -0.0882 41  PHE D CD1 
14655 C CD2 . PHE D 49  ? 0.2653 0.1784 0.2699 -0.0468 -0.0499 -0.0809 41  PHE D CD2 
14656 C CE1 . PHE D 49  ? 0.3908 0.2770 0.3845 -0.0426 -0.0517 -0.1003 41  PHE D CE1 
14657 C CE2 . PHE D 49  ? 0.2759 0.1846 0.2665 -0.0432 -0.0578 -0.0921 41  PHE D CE2 
14658 C CZ  . PHE D 49  ? 0.3318 0.2268 0.3159 -0.0412 -0.0590 -0.1021 41  PHE D CZ  
14659 N N   . LEU D 50  ? 0.2768 0.1999 0.3274 -0.0597 -0.0305 -0.0437 42  LEU D N   
14660 C CA  . LEU D 50  ? 0.2549 0.1790 0.3072 -0.0586 -0.0254 -0.0336 42  LEU D CA  
14661 C C   . LEU D 50  ? 0.2750 0.1933 0.3396 -0.0632 -0.0240 -0.0279 42  LEU D C   
14662 O O   . LEU D 50  ? 0.2805 0.2015 0.3538 -0.0690 -0.0248 -0.0267 42  LEU D O   
14663 C CB  . LEU D 50  ? 0.1871 0.1230 0.2348 -0.0581 -0.0248 -0.0282 42  LEU D CB  
14664 C CG  . LEU D 50  ? 0.1796 0.1168 0.2259 -0.0557 -0.0212 -0.0199 42  LEU D CG  
14665 C CD1 . LEU D 50  ? 0.1965 0.1299 0.2379 -0.0499 -0.0189 -0.0216 42  LEU D CD1 
14666 C CD2 . LEU D 50  ? 0.1928 0.1403 0.2357 -0.0560 -0.0209 -0.0152 42  LEU D CD2 
14667 N N   . ASN D 51  ? 0.2663 0.1764 0.3324 -0.0604 -0.0214 -0.0238 43  ASN D N   
14668 C CA  . ASN D 51  ? 0.2520 0.1539 0.3273 -0.0633 -0.0198 -0.0170 43  ASN D CA  
14669 C C   . ASN D 51  ? 0.2552 0.1608 0.3263 -0.0613 -0.0181 -0.0064 43  ASN D C   
14670 O O   . ASN D 51  ? 0.2957 0.2006 0.3640 -0.0559 -0.0182 -0.0043 43  ASN D O   
14671 C CB  . ASN D 51  ? 0.2799 0.1683 0.3600 -0.0607 -0.0193 -0.0203 43  ASN D CB  
14672 C CG  . ASN D 51  ? 0.2860 0.1680 0.3710 -0.0637 -0.0217 -0.0310 43  ASN D CG  
14673 O OD1 . ASN D 51  ? 0.2677 0.1531 0.3573 -0.0692 -0.0230 -0.0321 43  ASN D OD1 
14674 N ND2 . ASN D 51  ? 0.2661 0.1404 0.3478 -0.0591 -0.0216 -0.0390 43  ASN D ND2 
14675 N N   . HIS D 52  ? 0.2256 0.1353 0.2972 -0.0654 -0.0167 -0.0001 44  HIS D N   
14676 C CA  . HIS D 52  ? 0.2017 0.1147 0.2657 -0.0632 -0.0157 0.0089  44  HIS D CA  
14677 C C   . HIS D 52  ? 0.2821 0.1918 0.3480 -0.0677 -0.0120 0.0169  44  HIS D C   
14678 O O   . HIS D 52  ? 0.2691 0.1784 0.3444 -0.0736 -0.0098 0.0147  44  HIS D O   
14679 C CB  . HIS D 52  ? 0.2231 0.1489 0.2793 -0.0614 -0.0167 0.0068  44  HIS D CB  
14680 C CG  . HIS D 52  ? 0.2535 0.1878 0.3117 -0.0657 -0.0158 0.0034  44  HIS D CG  
14681 N ND1 . HIS D 52  ? 0.2511 0.1935 0.3051 -0.0667 -0.0138 0.0075  44  HIS D ND1 
14682 C CD2 . HIS D 52  ? 0.2756 0.2120 0.3406 -0.0688 -0.0173 -0.0041 44  HIS D CD2 
14683 C CE1 . HIS D 52  ? 0.2600 0.2098 0.3201 -0.0703 -0.0136 0.0031  44  HIS D CE1 
14684 N NE2 . HIS D 52  ? 0.2928 0.2393 0.3596 -0.0716 -0.0165 -0.0041 44  HIS D NE2 
14685 N N   . ASN D 53  ? 0.2206 0.1275 0.2775 -0.0649 -0.0112 0.0260  45  ASN D N   
14686 C CA  . ASN D 53  ? 0.2263 0.1289 0.2806 -0.0681 -0.0059 0.0352  45  ASN D CA  
14687 C C   . ASN D 53  ? 0.2230 0.1339 0.2639 -0.0663 -0.0047 0.0390  45  ASN D C   
14688 O O   . ASN D 53  ? 0.2498 0.1584 0.2785 -0.0608 -0.0079 0.0435  45  ASN D O   
14689 C CB  . ASN D 53  ? 0.2747 0.1619 0.3269 -0.0658 -0.0055 0.0441  45  ASN D CB  
14690 C CG  . ASN D 53  ? 0.2733 0.1534 0.3218 -0.0692 0.0020  0.0546  45  ASN D CG  
14691 O OD1 . ASN D 53  ? 0.2876 0.1750 0.3384 -0.0740 0.0076  0.0544  45  ASN D OD1 
14692 N ND2 . ASN D 53  ? 0.3033 0.1686 0.3466 -0.0663 0.0026  0.0642  45  ASN D ND2 
14693 N N   . PRO D 54  ? 0.3090 0.2293 0.3524 -0.0703 -0.0005 0.0371  46  PRO D N   
14694 C CA  . PRO D 54  ? 0.2828 0.2100 0.3131 -0.0682 0.0016  0.0402  46  PRO D CA  
14695 C C   . PRO D 54  ? 0.2946 0.2121 0.3098 -0.0655 0.0049  0.0510  46  PRO D C   
14696 O O   . PRO D 54  ? 0.3048 0.2248 0.3045 -0.0611 0.0032  0.0527  46  PRO D O   
14697 C CB  . PRO D 54  ? 0.3264 0.2634 0.3670 -0.0736 0.0072  0.0371  46  PRO D CB  
14698 C CG  . PRO D 54  ? 0.3423 0.2803 0.4002 -0.0776 0.0044  0.0296  46  PRO D CG  
14699 C CD  . PRO D 54  ? 0.3020 0.2264 0.3616 -0.0769 0.0025  0.0321  46  PRO D CD  
14700 N N   . ALA D 55  ? 0.2859 0.1913 0.3039 -0.0678 0.0095  0.0585  47  ALA D N   
14701 C CA  . ALA D 55  ? 0.3502 0.2440 0.3501 -0.0641 0.0126  0.0700  47  ALA D CA  
14702 C C   . ALA D 55  ? 0.3614 0.2480 0.3498 -0.0566 0.0029  0.0722  47  ALA D C   
14703 O O   . ALA D 55  ? 0.3548 0.2327 0.3241 -0.0517 0.0025  0.0808  47  ALA D O   
14704 C CB  . ALA D 55  ? 0.3927 0.2741 0.3993 -0.0688 0.0216  0.0787  47  ALA D CB  
14705 N N   . ASN D 56  ? 0.2903 0.1799 0.2899 -0.0550 -0.0049 0.0648  48  ASN D N   
14706 C CA  . ASN D 56  ? 0.2672 0.1530 0.2609 -0.0477 -0.0144 0.0656  48  ASN D CA  
14707 C C   . ASN D 56  ? 0.2553 0.1528 0.2597 -0.0468 -0.0201 0.0546  48  ASN D C   
14708 O O   . ASN D 56  ? 0.2796 0.1760 0.2981 -0.0472 -0.0216 0.0498  48  ASN D O   
14709 C CB  . ASN D 56  ? 0.2820 0.1529 0.2805 -0.0457 -0.0158 0.0718  48  ASN D CB  
14710 C CG  . ASN D 56  ? 0.2978 0.1664 0.2940 -0.0376 -0.0265 0.0721  48  ASN D CG  
14711 O OD1 . ASN D 56  ? 0.3153 0.1917 0.3035 -0.0337 -0.0328 0.0694  48  ASN D OD1 
14712 N ND2 . ASN D 56  ? 0.2971 0.1551 0.3024 -0.0350 -0.0288 0.0750  48  ASN D ND2 
14713 N N   . PRO D 57  ? 0.2849 0.1927 0.2823 -0.0452 -0.0226 0.0506  49  PRO D N   
14714 C CA  . PRO D 57  ? 0.2941 0.2119 0.3012 -0.0442 -0.0268 0.0414  49  PRO D CA  
14715 C C   . PRO D 57  ? 0.2449 0.1600 0.2588 -0.0388 -0.0341 0.0405  49  PRO D C   
14716 O O   . PRO D 57  ? 0.2549 0.1769 0.2795 -0.0381 -0.0356 0.0335  49  PRO D O   
14717 C CB  . PRO D 57  ? 0.3393 0.2658 0.3360 -0.0433 -0.0276 0.0391  49  PRO D CB  
14718 C CG  . PRO D 57  ? 0.3382 0.2612 0.3222 -0.0455 -0.0212 0.0453  49  PRO D CG  
14719 C CD  . PRO D 57  ? 0.3180 0.2277 0.2982 -0.0444 -0.0204 0.0541  49  PRO D CD  
14720 N N   . LYS D 58  ? 0.2568 0.1622 0.2654 -0.0347 -0.0384 0.0477  50  LYS D N   
14721 C CA  . LYS D 58  ? 0.2469 0.1498 0.2651 -0.0291 -0.0458 0.0473  50  LYS D CA  
14722 C C   . LYS D 58  ? 0.2429 0.1359 0.2724 -0.0291 -0.0434 0.0493  50  LYS D C   
14723 O O   . LYS D 58  ? 0.2742 0.1627 0.3113 -0.0236 -0.0492 0.0509  50  LYS D O   
14724 C CB  . LYS D 58  ? 0.3304 0.2289 0.3357 -0.0229 -0.0548 0.0533  50  LYS D CB  
14725 C CG  . LYS D 58  ? 0.4267 0.3335 0.4203 -0.0222 -0.0584 0.0502  50  LYS D CG  
14726 C CD  . LYS D 58  ? 0.5024 0.4215 0.5121 -0.0220 -0.0619 0.0409  50  LYS D CD  
14727 C CE  . LYS D 58  ? 0.5551 0.4803 0.5551 -0.0202 -0.0681 0.0377  50  LYS D CE  
14728 N NZ  . LYS D 58  ? 0.5587 0.4952 0.5761 -0.0211 -0.0695 0.0291  50  LYS D NZ  
14729 N N   . PHE D 59  ? 0.2423 0.1315 0.2744 -0.0349 -0.0355 0.0487  51  PHE D N   
14730 C CA  . PHE D 59  ? 0.2492 0.1279 0.2927 -0.0354 -0.0332 0.0491  51  PHE D CA  
14731 C C   . PHE D 59  ? 0.2404 0.1223 0.2989 -0.0315 -0.0359 0.0418  51  PHE D C   
14732 O O   . PHE D 59  ? 0.2547 0.1465 0.3179 -0.0330 -0.0340 0.0334  51  PHE D O   
14733 C CB  . PHE D 59  ? 0.2468 0.1243 0.2941 -0.0431 -0.0254 0.0462  51  PHE D CB  
14734 C CG  . PHE D 59  ? 0.2747 0.1425 0.3355 -0.0443 -0.0233 0.0429  51  PHE D CG  
14735 C CD1 . PHE D 59  ? 0.2827 0.1363 0.3469 -0.0406 -0.0248 0.0496  51  PHE D CD1 
14736 C CD2 . PHE D 59  ? 0.3519 0.2236 0.4210 -0.0484 -0.0204 0.0328  51  PHE D CD2 
14737 C CE1 . PHE D 59  ? 0.3171 0.1607 0.3944 -0.0414 -0.0227 0.0458  51  PHE D CE1 
14738 C CE2 . PHE D 59  ? 0.3118 0.1736 0.3922 -0.0492 -0.0189 0.0284  51  PHE D CE2 
14739 C CZ  . PHE D 59  ? 0.2907 0.1382 0.3759 -0.0459 -0.0197 0.0347  51  PHE D CZ  
14740 N N   . TYR D 60  ? 0.2689 0.1417 0.3347 -0.0261 -0.0397 0.0454  52  TYR D N   
14741 C CA  . TYR D 60  ? 0.2911 0.1679 0.3725 -0.0209 -0.0423 0.0396  52  TYR D CA  
14742 C C   . TYR D 60  ? 0.3189 0.1985 0.4093 -0.0239 -0.0355 0.0294  52  TYR D C   
14743 O O   . TYR D 60  ? 0.2246 0.1129 0.3229 -0.0216 -0.0348 0.0230  52  TYR D O   
14744 C CB  . TYR D 60  ? 0.2610 0.1258 0.3507 -0.0146 -0.0465 0.0452  52  TYR D CB  
14745 C CG  . TYR D 60  ? 0.2756 0.1358 0.3552 -0.0095 -0.0551 0.0554  52  TYR D CG  
14746 C CD1 . TYR D 60  ? 0.3615 0.2314 0.4303 -0.0084 -0.0610 0.0564  52  TYR D CD1 
14747 C CD2 . TYR D 60  ? 0.3498 0.1947 0.4296 -0.0051 -0.0577 0.0640  52  TYR D CD2 
14748 C CE1 . TYR D 60  ? 0.3542 0.2187 0.4105 -0.0027 -0.0701 0.0650  52  TYR D CE1 
14749 C CE2 . TYR D 60  ? 0.3872 0.2264 0.4543 0.0008  -0.0664 0.0739  52  TYR D CE2 
14750 C CZ  . TYR D 60  ? 0.4098 0.2590 0.4642 0.0021  -0.0728 0.0741  52  TYR D CZ  
14751 O OH  . TYR D 60  ? 0.4404 0.2829 0.4789 0.0087  -0.0825 0.0832  52  TYR D OH  
14752 N N   . ASN D 61  ? 0.2578 0.1292 0.3473 -0.0288 -0.0304 0.0276  53  ASN D N   
14753 C CA  . ASN D 61  ? 0.2936 0.1647 0.3899 -0.0303 -0.0254 0.0174  53  ASN D CA  
14754 C C   . ASN D 61  ? 0.2888 0.1678 0.3770 -0.0364 -0.0223 0.0116  53  ASN D C   
14755 O O   . ASN D 61  ? 0.2279 0.1041 0.3179 -0.0385 -0.0192 0.0034  53  ASN D O   
14756 C CB  . ASN D 61  ? 0.2679 0.1235 0.3717 -0.0307 -0.0233 0.0166  53  ASN D CB  
14757 C CG  . ASN D 61  ? 0.2759 0.1293 0.3873 -0.0286 -0.0195 0.0055  53  ASN D CG  
14758 O OD1 . ASN D 61  ? 0.3089 0.1687 0.4253 -0.0233 -0.0186 0.0020  53  ASN D OD1 
14759 N ND2 . ASN D 61  ? 0.2685 0.1127 0.3810 -0.0327 -0.0169 -0.0004 53  ASN D ND2 
14760 N N   . ARG D 62  ? 0.2489 0.1373 0.3279 -0.0386 -0.0237 0.0150  54  ARG D N   
14761 C CA  . ARG D 62  ? 0.2572 0.1543 0.3299 -0.0431 -0.0214 0.0098  54  ARG D CA  
14762 C C   . ARG D 62  ? 0.2313 0.1346 0.3050 -0.0404 -0.0195 0.0015  54  ARG D C   
14763 O O   . ARG D 62  ? 0.2163 0.1223 0.2951 -0.0354 -0.0197 0.0014  54  ARG D O   
14764 C CB  . ARG D 62  ? 0.2145 0.1201 0.2779 -0.0447 -0.0229 0.0151  54  ARG D CB  
14765 C CG  . ARG D 62  ? 0.1964 0.1096 0.2588 -0.0398 -0.0261 0.0160  54  ARG D CG  
14766 C CD  . ARG D 62  ? 0.1933 0.1125 0.2452 -0.0407 -0.0284 0.0208  54  ARG D CD  
14767 N NE  . ARG D 62  ? 0.2193 0.1461 0.2724 -0.0369 -0.0321 0.0196  54  ARG D NE  
14768 C CZ  . ARG D 62  ? 0.2507 0.1758 0.3084 -0.0321 -0.0378 0.0225  54  ARG D CZ  
14769 N NH1 . ARG D 62  ? 0.2194 0.1348 0.2789 -0.0297 -0.0403 0.0277  54  ARG D NH1 
14770 N NH2 . ARG D 62  ? 0.2011 0.1342 0.2631 -0.0295 -0.0415 0.0202  54  ARG D NH2 
14771 N N   . ASP D 63  ? 0.2594 0.1647 0.3287 -0.0434 -0.0175 -0.0054 55  ASP D N   
14772 C CA  . ASP D 63  ? 0.2760 0.1879 0.3409 -0.0409 -0.0152 -0.0113 55  ASP D CA  
14773 C C   . ASP D 63  ? 0.2677 0.1901 0.3292 -0.0401 -0.0161 -0.0070 55  ASP D C   
14774 O O   . ASP D 63  ? 0.1968 0.1229 0.2550 -0.0429 -0.0186 -0.0020 55  ASP D O   
14775 C CB  . ASP D 63  ? 0.2395 0.1521 0.2972 -0.0438 -0.0150 -0.0185 55  ASP D CB  
14776 C CG  . ASP D 63  ? 0.2431 0.1448 0.3034 -0.0441 -0.0147 -0.0254 55  ASP D CG  
14777 O OD1 . ASP D 63  ? 0.2455 0.1397 0.3116 -0.0402 -0.0124 -0.0264 55  ASP D OD1 
14778 O OD2 . ASP D 63  ? 0.2602 0.1611 0.3182 -0.0480 -0.0171 -0.0305 55  ASP D OD2 
14779 N N   . ARG D 64  ? 0.1776 0.1042 0.2407 -0.0362 -0.0134 -0.0091 56  ARG D N   
14780 C CA  . ARG D 64  ? 0.1980 0.1339 0.2598 -0.0357 -0.0139 -0.0065 56  ARG D CA  
14781 C C   . ARG D 64  ? 0.2358 0.1759 0.2879 -0.0365 -0.0110 -0.0105 56  ARG D C   
14782 O O   . ARG D 64  ? 0.2852 0.2219 0.3337 -0.0343 -0.0068 -0.0154 56  ARG D O   
14783 C CB  . ARG D 64  ? 0.2082 0.1461 0.2817 -0.0312 -0.0126 -0.0058 56  ARG D CB  
14784 C CG  . ARG D 64  ? 0.2372 0.1758 0.3189 -0.0299 -0.0190 -0.0002 56  ARG D CG  
14785 C CD  . ARG D 64  ? 0.2342 0.1635 0.3182 -0.0294 -0.0217 0.0025  56  ARG D CD  
14786 N NE  . ARG D 64  ? 0.2237 0.1524 0.3152 -0.0262 -0.0283 0.0078  56  ARG D NE  
14787 C CZ  . ARG D 64  ? 0.2683 0.1881 0.3627 -0.0244 -0.0313 0.0118  56  ARG D CZ  
14788 N NH1 . ARG D 64  ? 0.2522 0.1628 0.3446 -0.0263 -0.0277 0.0105  56  ARG D NH1 
14789 N NH2 . ARG D 64  ? 0.2191 0.1382 0.3187 -0.0204 -0.0385 0.0168  56  ARG D NH2 
14790 N N   . PHE D 65  ? 0.1972 0.1437 0.2437 -0.0389 -0.0131 -0.0083 57  PHE D N   
14791 C CA  . PHE D 65  ? 0.1990 0.1498 0.2370 -0.0387 -0.0111 -0.0109 57  PHE D CA  
14792 C C   . PHE D 65  ? 0.2000 0.1567 0.2402 -0.0374 -0.0101 -0.0082 57  PHE D C   
14793 O O   . PHE D 65  ? 0.1742 0.1340 0.2179 -0.0385 -0.0137 -0.0048 57  PHE D O   
14794 C CB  . PHE D 65  ? 0.1771 0.1308 0.2093 -0.0425 -0.0143 -0.0113 57  PHE D CB  
14795 C CG  . PHE D 65  ? 0.2015 0.1602 0.2258 -0.0415 -0.0137 -0.0131 57  PHE D CG  
14796 C CD1 . PHE D 65  ? 0.2358 0.1915 0.2522 -0.0392 -0.0125 -0.0179 57  PHE D CD1 
14797 C CD2 . PHE D 65  ? 0.1840 0.1493 0.2076 -0.0423 -0.0145 -0.0101 57  PHE D CD2 
14798 C CE1 . PHE D 65  ? 0.2467 0.2059 0.2545 -0.0373 -0.0127 -0.0186 57  PHE D CE1 
14799 C CE2 . PHE D 65  ? 0.1445 0.1135 0.1617 -0.0407 -0.0141 -0.0113 57  PHE D CE2 
14800 C CZ  . PHE D 65  ? 0.1980 0.1640 0.2073 -0.0381 -0.0134 -0.0151 57  PHE D CZ  
14801 N N   . VAL D 66  ? 0.1662 0.1233 0.2033 -0.0348 -0.0053 -0.0099 58  VAL D N   
14802 C CA  . VAL D 66  ? 0.1777 0.1393 0.2189 -0.0339 -0.0033 -0.0078 58  VAL D CA  
14803 C C   . VAL D 66  ? 0.1822 0.1446 0.2121 -0.0330 -0.0009 -0.0085 58  VAL D C   
14804 O O   . VAL D 66  ? 0.1594 0.1174 0.1804 -0.0305 0.0031  -0.0106 58  VAL D O   
14805 C CB  . VAL D 66  ? 0.1790 0.1394 0.2322 -0.0312 0.0021  -0.0077 58  VAL D CB  
14806 C CG1 . VAL D 66  ? 0.1446 0.1091 0.2041 -0.0310 0.0047  -0.0060 58  VAL D CG1 
14807 C CG2 . VAL D 66  ? 0.1827 0.1431 0.2485 -0.0312 -0.0021 -0.0068 58  VAL D CG2 
14808 N N   . LEU D 67  ? 0.1401 0.1073 0.1692 -0.0344 -0.0035 -0.0067 59  LEU D N   
14809 C CA  . LEU D 67  ? 0.1587 0.1266 0.1793 -0.0328 -0.0015 -0.0065 59  LEU D CA  
14810 C C   . LEU D 67  ? 0.1419 0.1088 0.1694 -0.0312 0.0041  -0.0045 59  LEU D C   
14811 O O   . LEU D 67  ? 0.1825 0.1526 0.2179 -0.0326 0.0023  -0.0034 59  LEU D O   
14812 C CB  . LEU D 67  ? 0.1927 0.1658 0.2108 -0.0348 -0.0064 -0.0060 59  LEU D CB  
14813 C CG  . LEU D 67  ? 0.2205 0.1947 0.2319 -0.0326 -0.0052 -0.0054 59  LEU D CG  
14814 C CD1 . LEU D 67  ? 0.2267 0.1983 0.2270 -0.0302 -0.0056 -0.0073 59  LEU D CD1 
14815 C CD2 . LEU D 67  ? 0.2161 0.1960 0.2287 -0.0343 -0.0090 -0.0051 59  LEU D CD2 
14816 N N   . SER D 68  ? 0.2019 0.1637 0.2269 -0.0282 0.0116  -0.0042 60  SER D N   
14817 C CA  . SER D 68  ? 0.1759 0.1367 0.2116 -0.0273 0.0186  -0.0018 60  SER D CA  
14818 C C   . SER D 68  ? 0.2192 0.1798 0.2509 -0.0268 0.0197  0.0006  60  SER D C   
14819 O O   . SER D 68  ? 0.2478 0.2099 0.2928 -0.0282 0.0213  0.0019  60  SER D O   
14820 C CB  . SER D 68  ? 0.1623 0.1169 0.1958 -0.0238 0.0288  -0.0013 60  SER D CB  
14821 O OG  . SER D 68  ? 0.2296 0.1846 0.2803 -0.0240 0.0363  0.0011  60  SER D OG  
14822 N N   . ASN D 69  ? 0.2126 0.1713 0.2276 -0.0247 0.0180  0.0009  61  ASN D N   
14823 C CA  . ASN D 69  ? 0.2815 0.2393 0.2925 -0.0234 0.0186  0.0034  61  ASN D CA  
14824 C C   . ASN D 69  ? 0.3142 0.2789 0.3308 -0.0265 0.0105  0.0016  61  ASN D C   
14825 O O   . ASN D 69  ? 0.3354 0.3029 0.3438 -0.0259 0.0055  0.0007  61  ASN D O   
14826 C CB  . ASN D 69  ? 0.2489 0.2017 0.2402 -0.0186 0.0194  0.0046  61  ASN D CB  
14827 C CG  . ASN D 69  ? 0.2553 0.2091 0.2359 -0.0181 0.0138  0.0005  61  ASN D CG  
14828 O OD1 . ASN D 69  ? 0.3110 0.2687 0.2992 -0.0216 0.0099  -0.0025 61  ASN D OD1 
14829 N ND2 . ASN D 69  ? 0.2923 0.2416 0.2553 -0.0135 0.0127  0.0004  61  ASN D ND2 
14830 N N   . GLY D 70  ? 0.2970 0.2643 0.3282 -0.0294 0.0093  0.0009  62  GLY D N   
14831 C CA  . GLY D 70  ? 0.3466 0.3193 0.3814 -0.0320 0.0019  -0.0014 62  GLY D CA  
14832 C C   . GLY D 70  ? 0.2952 0.2692 0.3248 -0.0311 -0.0001 -0.0016 62  GLY D C   
14833 O O   . GLY D 70  ? 0.2548 0.2330 0.2827 -0.0325 -0.0051 -0.0035 62  GLY D O   
14834 N N   . HIS D 71  ? 0.2035 0.1731 0.2305 -0.0284 0.0045  0.0007  63  HIS D N   
14835 C CA  . HIS D 71  ? 0.2878 0.2583 0.3104 -0.0266 0.0026  0.0006  63  HIS D CA  
14836 C C   . HIS D 71  ? 0.2892 0.2646 0.3022 -0.0255 -0.0017 -0.0003 63  HIS D C   
14837 O O   . HIS D 71  ? 0.2624 0.2418 0.2752 -0.0249 -0.0044 -0.0017 63  HIS D O   
14838 C CB  . HIS D 71  ? 0.2828 0.2460 0.3033 -0.0230 0.0086  0.0045  63  HIS D CB  
14839 C CG  . HIS D 71  ? 0.3319 0.2900 0.3424 -0.0200 0.0134  0.0079  63  HIS D CG  
14840 N ND1 . HIS D 71  ? 0.3723 0.3260 0.3874 -0.0207 0.0202  0.0097  63  HIS D ND1 
14841 C CD2 . HIS D 71  ? 0.3658 0.3223 0.3611 -0.0157 0.0122  0.0094  63  HIS D CD2 
14842 C CE1 . HIS D 71  ? 0.3651 0.3137 0.3658 -0.0168 0.0240  0.0122  63  HIS D CE1 
14843 N NE2 . HIS D 71  ? 0.3384 0.2883 0.3261 -0.0136 0.0184  0.0119  63  HIS D NE2 
14844 N N   . ALA D 72  ? 0.2427 0.2182 0.2495 -0.0251 -0.0021 -0.0002 64  ALA D N   
14845 C CA  . ALA D 72  ? 0.2196 0.2003 0.2211 -0.0250 -0.0070 -0.0021 64  ALA D CA  
14846 C C   . ALA D 72  ? 0.2168 0.2034 0.2240 -0.0294 -0.0102 -0.0042 64  ALA D C   
14847 O O   . ALA D 72  ? 0.2129 0.2023 0.2191 -0.0310 -0.0128 -0.0057 64  ALA D O   
14848 C CB  . ALA D 72  ? 0.1782 0.1554 0.1708 -0.0232 -0.0070 -0.0024 64  ALA D CB  
14849 N N   . SER D 73  ? 0.1366 0.1240 0.1490 -0.0310 -0.0100 -0.0045 65  SER D N   
14850 C CA  . SER D 73  ? 0.1297 0.1201 0.1442 -0.0344 -0.0122 -0.0055 65  SER D CA  
14851 C C   . SER D 73  ? 0.1863 0.1825 0.1997 -0.0356 -0.0136 -0.0060 65  SER D C   
14852 O O   . SER D 73  ? 0.1718 0.1688 0.1859 -0.0385 -0.0144 -0.0056 65  SER D O   
14853 C CB  . SER D 73  ? 0.1818 0.1715 0.1984 -0.0346 -0.0127 -0.0065 65  SER D CB  
14854 O OG  . SER D 73  ? 0.2046 0.1955 0.2206 -0.0322 -0.0116 -0.0074 65  SER D OG  
14855 N N   . MET D 74  ? 0.1911 0.1913 0.2046 -0.0334 -0.0136 -0.0067 66  MET D N   
14856 C CA  . MET D 74  ? 0.1864 0.1938 0.2035 -0.0349 -0.0143 -0.0075 66  MET D CA  
14857 C C   . MET D 74  ? 0.1966 0.2051 0.2155 -0.0369 -0.0168 -0.0083 66  MET D C   
14858 O O   . MET D 74  ? 0.1971 0.2105 0.2219 -0.0399 -0.0168 -0.0088 66  MET D O   
14859 C CB  . MET D 74  ? 0.1668 0.1793 0.1867 -0.0313 -0.0143 -0.0085 66  MET D CB  
14860 C CG  . MET D 74  ? 0.1899 0.2039 0.2106 -0.0306 -0.0111 -0.0091 66  MET D CG  
14861 S SD  . MET D 74  ? 0.1904 0.2071 0.2107 -0.0346 -0.0076 -0.0086 66  MET D SD  
14862 C CE  . MET D 74  ? 0.1459 0.1712 0.1768 -0.0374 -0.0078 -0.0085 66  MET D CE  
14863 N N   . LEU D 75  ? 0.1473 0.1506 0.1614 -0.0353 -0.0183 -0.0087 67  LEU D N   
14864 C CA  . LEU D 75  ? 0.1651 0.1676 0.1797 -0.0372 -0.0210 -0.0107 67  LEU D CA  
14865 C C   . LEU D 75  ? 0.1780 0.1785 0.1963 -0.0418 -0.0195 -0.0097 67  LEU D C   
14866 O O   . LEU D 75  ? 0.1684 0.1715 0.1927 -0.0452 -0.0206 -0.0106 67  LEU D O   
14867 C CB  . LEU D 75  ? 0.1533 0.1487 0.1590 -0.0339 -0.0212 -0.0114 67  LEU D CB  
14868 C CG  . LEU D 75  ? 0.2430 0.2353 0.2468 -0.0351 -0.0241 -0.0148 67  LEU D CG  
14869 C CD1 . LEU D 75  ? 0.2821 0.2806 0.2897 -0.0354 -0.0302 -0.0185 67  LEU D CD1 
14870 C CD2 . LEU D 75  ? 0.2300 0.2137 0.2221 -0.0309 -0.0221 -0.0152 67  LEU D CD2 
14871 N N   . LEU D 76  ? 0.1452 0.1410 0.1613 -0.0417 -0.0173 -0.0075 68  LEU D N   
14872 C CA  . LEU D 76  ? 0.1800 0.1727 0.1982 -0.0447 -0.0169 -0.0058 68  LEU D CA  
14873 C C   . LEU D 76  ? 0.1887 0.1851 0.2086 -0.0472 -0.0155 -0.0038 68  LEU D C   
14874 O O   . LEU D 76  ? 0.1520 0.1472 0.1749 -0.0504 -0.0149 -0.0023 68  LEU D O   
14875 C CB  . LEU D 76  ? 0.1560 0.1439 0.1732 -0.0432 -0.0163 -0.0044 68  LEU D CB  
14876 C CG  . LEU D 76  ? 0.1844 0.1683 0.2034 -0.0449 -0.0172 -0.0023 68  LEU D CG  
14877 C CD1 . LEU D 76  ? 0.2400 0.2205 0.2615 -0.0466 -0.0175 -0.0031 68  LEU D CD1 
14878 C CD2 . LEU D 76  ? 0.1626 0.1436 0.1843 -0.0429 -0.0180 -0.0019 68  LEU D CD2 
14879 N N   . TYR D 77  ? 0.1506 0.1505 0.1683 -0.0455 -0.0141 -0.0035 69  TYR D N   
14880 C CA  . TYR D 77  ? 0.1417 0.1445 0.1590 -0.0471 -0.0111 -0.0016 69  TYR D CA  
14881 C C   . TYR D 77  ? 0.1675 0.1760 0.1935 -0.0500 -0.0095 -0.0020 69  TYR D C   
14882 O O   . TYR D 77  ? 0.1884 0.1967 0.2165 -0.0531 -0.0060 0.0008  69  TYR D O   
14883 C CB  . TYR D 77  ? 0.1371 0.1422 0.1505 -0.0442 -0.0096 -0.0027 69  TYR D CB  
14884 C CG  . TYR D 77  ? 0.1339 0.1333 0.1412 -0.0421 -0.0118 -0.0031 69  TYR D CG  
14885 C CD1 . TYR D 77  ? 0.1880 0.1818 0.1923 -0.0430 -0.0143 -0.0013 69  TYR D CD1 
14886 C CD2 . TYR D 77  ? 0.1797 0.1794 0.1864 -0.0392 -0.0120 -0.0056 69  TYR D CD2 
14887 C CE1 . TYR D 77  ? 0.1995 0.1896 0.2018 -0.0411 -0.0177 -0.0025 69  TYR D CE1 
14888 C CE2 . TYR D 77  ? 0.1763 0.1712 0.1809 -0.0379 -0.0146 -0.0069 69  TYR D CE2 
14889 C CZ  . TYR D 77  ? 0.1791 0.1699 0.1822 -0.0390 -0.0178 -0.0057 69  TYR D CZ  
14890 O OH  . TYR D 77  ? 0.1940 0.1814 0.1984 -0.0379 -0.0216 -0.0078 69  TYR D OH  
14891 N N   . SER D 78  ? 0.1737 0.1871 0.2055 -0.0489 -0.0122 -0.0053 70  SER D N   
14892 C CA  . SER D 78  ? 0.1924 0.2122 0.2361 -0.0519 -0.0127 -0.0070 70  SER D CA  
14893 C C   . SER D 78  ? 0.1891 0.2039 0.2366 -0.0563 -0.0133 -0.0065 70  SER D C   
14894 O O   . SER D 78  ? 0.1833 0.2004 0.2402 -0.0606 -0.0101 -0.0051 70  SER D O   
14895 C CB  . SER D 78  ? 0.2145 0.2391 0.2616 -0.0489 -0.0182 -0.0113 70  SER D CB  
14896 O OG  . SER D 78  ? 0.1975 0.2268 0.2438 -0.0447 -0.0173 -0.0114 70  SER D OG  
14897 N N   . LEU D 79  ? 0.1873 0.1947 0.2285 -0.0552 -0.0166 -0.0076 71  LEU D N   
14898 C CA  . LEU D 79  ? 0.1784 0.1798 0.2236 -0.0588 -0.0175 -0.0080 71  LEU D CA  
14899 C C   . LEU D 79  ? 0.2191 0.2156 0.2639 -0.0616 -0.0127 -0.0022 71  LEU D C   
14900 O O   . LEU D 79  ? 0.2280 0.2222 0.2811 -0.0659 -0.0110 -0.0010 71  LEU D O   
14901 C CB  . LEU D 79  ? 0.1859 0.1800 0.2238 -0.0560 -0.0205 -0.0104 71  LEU D CB  
14902 C CG  . LEU D 79  ? 0.1853 0.1811 0.2201 -0.0528 -0.0250 -0.0159 71  LEU D CG  
14903 C CD1 . LEU D 79  ? 0.2151 0.2033 0.2395 -0.0488 -0.0247 -0.0166 71  LEU D CD1 
14904 C CD2 . LEU D 79  ? 0.2240 0.2212 0.2674 -0.0559 -0.0295 -0.0211 71  LEU D CD2 
14905 N N   . LEU D 80  ? 0.1922 0.1864 0.2273 -0.0590 -0.0108 0.0015  72  LEU D N   
14906 C CA  . LEU D 80  ? 0.2204 0.2085 0.2508 -0.0602 -0.0074 0.0075  72  LEU D CA  
14907 C C   . LEU D 80  ? 0.2047 0.1967 0.2391 -0.0632 -0.0011 0.0107  72  LEU D C   
14908 O O   . LEU D 80  ? 0.2166 0.2031 0.2529 -0.0663 0.0029  0.0154  72  LEU D O   
14909 C CB  . LEU D 80  ? 0.2162 0.2014 0.2347 -0.0561 -0.0089 0.0092  72  LEU D CB  
14910 C CG  . LEU D 80  ? 0.2121 0.1930 0.2298 -0.0535 -0.0136 0.0072  72  LEU D CG  
14911 C CD1 . LEU D 80  ? 0.1988 0.1792 0.2094 -0.0499 -0.0158 0.0074  72  LEU D CD1 
14912 C CD2 . LEU D 80  ? 0.2004 0.1731 0.2203 -0.0547 -0.0146 0.0098  72  LEU D CD2 
14913 N N   . HIS D 81  ? 0.1860 0.1868 0.2223 -0.0620 0.0010  0.0086  73  HIS D N   
14914 C CA  . HIS D 81  ? 0.1953 0.2012 0.2381 -0.0645 0.0086  0.0112  73  HIS D CA  
14915 C C   . HIS D 81  ? 0.2057 0.2148 0.2673 -0.0701 0.0095  0.0101  73  HIS D C   
14916 O O   . HIS D 81  ? 0.1938 0.2005 0.2612 -0.0741 0.0167  0.0149  73  HIS D O   
14917 C CB  . HIS D 81  ? 0.1978 0.2132 0.2419 -0.0614 0.0101  0.0080  73  HIS D CB  
14918 C CG  . HIS D 81  ? 0.2285 0.2515 0.2841 -0.0639 0.0185  0.0096  73  HIS D CG  
14919 N ND1 . HIS D 81  ? 0.2224 0.2414 0.2700 -0.0643 0.0281  0.0155  73  HIS D ND1 
14920 C CD2 . HIS D 81  ? 0.1817 0.2159 0.2572 -0.0659 0.0193  0.0062  73  HIS D CD2 
14921 C CE1 . HIS D 81  ? 0.2343 0.2620 0.2973 -0.0667 0.0360  0.0159  73  HIS D CE1 
14922 N NE2 . HIS D 81  ? 0.1836 0.2214 0.2656 -0.0679 0.0302  0.0101  73  HIS D NE2 
14923 N N   . LEU D 82  ? 0.2139 0.2274 0.2848 -0.0704 0.0024  0.0036  74  LEU D N   
14924 C CA  . LEU D 82  ? 0.2178 0.2357 0.3086 -0.0756 0.0013  0.0004  74  LEU D CA  
14925 C C   . LEU D 82  ? 0.2105 0.2178 0.3042 -0.0799 0.0023  0.0029  74  LEU D C   
14926 O O   . LEU D 82  ? 0.2371 0.2455 0.3477 -0.0857 0.0060  0.0037  74  LEU D O   
14927 C CB  . LEU D 82  ? 0.1632 0.1870 0.2593 -0.0735 -0.0083 -0.0078 74  LEU D CB  
14928 C CG  . LEU D 82  ? 0.2185 0.2537 0.3174 -0.0695 -0.0103 -0.0108 74  LEU D CG  
14929 C CD1 . LEU D 82  ? 0.2172 0.2521 0.3087 -0.0647 -0.0201 -0.0165 74  LEU D CD1 
14930 C CD2 . LEU D 82  ? 0.2826 0.3297 0.4053 -0.0733 -0.0083 -0.0127 74  LEU D CD2 
14931 N N   . THR D 83  ? 0.2136 0.2104 0.2933 -0.0774 -0.0007 0.0043  75  THR D N   
14932 C CA  . THR D 83  ? 0.2353 0.2212 0.3187 -0.0807 -0.0005 0.0062  75  THR D CA  
14933 C C   . THR D 83  ? 0.2459 0.2239 0.3241 -0.0822 0.0077  0.0160  75  THR D C   
14934 O O   . THR D 83  ? 0.2568 0.2248 0.3397 -0.0852 0.0093  0.0192  75  THR D O   
14935 C CB  . THR D 83  ? 0.2187 0.1968 0.2922 -0.0769 -0.0069 0.0031  75  THR D CB  
14936 O OG1 . THR D 83  ? 0.1785 0.1550 0.2361 -0.0717 -0.0068 0.0066  75  THR D OG1 
14937 C CG2 . THR D 83  ? 0.2352 0.2186 0.3119 -0.0755 -0.0142 -0.0062 75  THR D CG2 
14938 N N   . GLY D 84  ? 0.1968 0.1777 0.2643 -0.0796 0.0131  0.0209  76  GLY D N   
14939 C CA  . GLY D 84  ? 0.2077 0.1809 0.2678 -0.0805 0.0219  0.0305  76  GLY D CA  
14940 C C   . GLY D 84  ? 0.2030 0.1673 0.2399 -0.0747 0.0202  0.0356  76  GLY D C   
14941 O O   . GLY D 84  ? 0.2468 0.2012 0.2741 -0.0745 0.0258  0.0442  76  GLY D O   
14942 N N   . TYR D 85  ? 0.1942 0.1610 0.2224 -0.0699 0.0125  0.0309  77  TYR D N   
14943 C CA  . TYR D 85  ? 0.2408 0.2010 0.2498 -0.0645 0.0096  0.0345  77  TYR D CA  
14944 C C   . TYR D 85  ? 0.3298 0.2921 0.3254 -0.0622 0.0156  0.0376  77  TYR D C   
14945 O O   . TYR D 85  ? 0.2293 0.1999 0.2319 -0.0643 0.0221  0.0362  77  TYR D O   
14946 C CB  . TYR D 85  ? 0.2708 0.2342 0.2782 -0.0607 0.0008  0.0281  77  TYR D CB  
14947 C CG  . TYR D 85  ? 0.2351 0.1937 0.2508 -0.0611 -0.0043 0.0259  77  TYR D CG  
14948 C CD1 . TYR D 85  ? 0.2060 0.1682 0.2352 -0.0643 -0.0049 0.0204  77  TYR D CD1 
14949 C CD2 . TYR D 85  ? 0.2649 0.2152 0.2746 -0.0576 -0.0089 0.0286  77  TYR D CD2 
14950 C CE1 . TYR D 85  ? 0.2197 0.1764 0.2545 -0.0641 -0.0087 0.0175  77  TYR D CE1 
14951 C CE2 . TYR D 85  ? 0.3119 0.2579 0.3301 -0.0574 -0.0123 0.0263  77  TYR D CE2 
14952 C CZ  . TYR D 85  ? 0.3122 0.2609 0.3420 -0.0607 -0.0116 0.0206  77  TYR D CZ  
14953 O OH  . TYR D 85  ? 0.3606 0.3038 0.3969 -0.0599 -0.0143 0.0174  77  TYR D OH  
14954 N N   . ASN D 86  ? 0.2645 0.2191 0.2406 -0.0573 0.0128  0.0412  78  ASN D N   
14955 C CA  . ASN D 86  ? 0.2967 0.2505 0.2550 -0.0539 0.0175  0.0436  78  ASN D CA  
14956 C C   . ASN D 86  ? 0.3944 0.3575 0.3521 -0.0512 0.0140  0.0354  78  ASN D C   
14957 O O   . ASN D 86  ? 0.3514 0.3117 0.2936 -0.0464 0.0092  0.0337  78  ASN D O   
14958 C CB  . ASN D 86  ? 0.3550 0.2960 0.2908 -0.0488 0.0136  0.0496  78  ASN D CB  
14959 C CG  . ASN D 86  ? 0.5132 0.4502 0.4262 -0.0450 0.0200  0.0531  78  ASN D CG  
14960 O OD1 . ASN D 86  ? 0.6122 0.5559 0.5278 -0.0464 0.0291  0.0514  78  ASN D OD1 
14961 N ND2 . ASN D 86  ? 0.5725 0.4980 0.4625 -0.0394 0.0151  0.0576  78  ASN D ND2 
14962 N N   . LEU D 87  ? 0.3123 0.2861 0.2875 -0.0542 0.0155  0.0302  79  LEU D N   
14963 C CA  . LEU D 87  ? 0.2269 0.2091 0.2037 -0.0518 0.0135  0.0234  79  LEU D CA  
14964 C C   . LEU D 87  ? 0.2313 0.2226 0.2197 -0.0542 0.0224  0.0227  79  LEU D C   
14965 O O   . LEU D 87  ? 0.2462 0.2430 0.2528 -0.0585 0.0233  0.0219  79  LEU D O   
14966 C CB  . LEU D 87  ? 0.1979 0.1837 0.1850 -0.0517 0.0051  0.0177  79  LEU D CB  
14967 C CG  . LEU D 87  ? 0.2521 0.2431 0.2386 -0.0484 0.0020  0.0117  79  LEU D CG  
14968 C CD1 . LEU D 87  ? 0.2127 0.1978 0.1833 -0.0443 -0.0015 0.0111  79  LEU D CD1 
14969 C CD2 . LEU D 87  ? 0.1873 0.1809 0.1845 -0.0486 -0.0038 0.0078  79  LEU D CD2 
14970 N N   . SER D 88  ? 0.2230 0.2160 0.2020 -0.0513 0.0286  0.0224  80  SER D N   
14971 C CA  . SER D 88  ? 0.2116 0.2125 0.2017 -0.0533 0.0394  0.0233  80  SER D CA  
14972 C C   . SER D 88  ? 0.1975 0.2100 0.2004 -0.0515 0.0377  0.0162  80  SER D C   
14973 O O   . SER D 88  ? 0.1819 0.1945 0.1816 -0.0485 0.0294  0.0113  80  SER D O   
14974 C CB  . SER D 88  ? 0.2339 0.2288 0.2052 -0.0505 0.0498  0.0279  80  SER D CB  
14975 O OG  . SER D 88  ? 0.2888 0.2825 0.2445 -0.0446 0.0472  0.0229  80  SER D OG  
14976 N N   . ILE D 89  ? 0.1947 0.2167 0.2132 -0.0532 0.0464  0.0161  81  ILE D N   
14977 C CA  . ILE D 89  ? 0.2215 0.2543 0.2520 -0.0504 0.0457  0.0101  81  ILE D CA  
14978 C C   . ILE D 89  ? 0.2519 0.2804 0.2638 -0.0442 0.0465  0.0073  81  ILE D C   
14979 O O   . ILE D 89  ? 0.2235 0.2547 0.2375 -0.0408 0.0402  0.0019  81  ILE D O   
14980 C CB  . ILE D 89  ? 0.2511 0.2956 0.3040 -0.0530 0.0556  0.0108  81  ILE D CB  
14981 C CG1 . ILE D 89  ? 0.2466 0.2982 0.3236 -0.0585 0.0498  0.0096  81  ILE D CG1 
14982 C CG2 . ILE D 89  ? 0.2291 0.2826 0.2885 -0.0480 0.0585  0.0059  81  ILE D CG2 
14983 C CD1 . ILE D 89  ? 0.1570 0.2124 0.2389 -0.0562 0.0365  0.0035  81  ILE D CD1 
14984 N N   . GLU D 90  ? 0.2439 0.2644 0.2363 -0.0423 0.0541  0.0106  82  GLU D N   
14985 C CA  . GLU D 90  ? 0.2842 0.2991 0.2570 -0.0362 0.0537  0.0065  82  GLU D CA  
14986 C C   . GLU D 90  ? 0.2175 0.2258 0.1813 -0.0346 0.0401  0.0029  82  GLU D C   
14987 O O   . GLU D 90  ? 0.2713 0.2792 0.2321 -0.0307 0.0362  -0.0031 82  GLU D O   
14988 C CB  . GLU D 90  ? 0.3320 0.3374 0.2811 -0.0339 0.0633  0.0109  82  GLU D CB  
14989 C CG  . GLU D 90  ? 0.5216 0.5203 0.4485 -0.0271 0.0631  0.0053  82  GLU D CG  
14990 C CD  . GLU D 90  ? 0.6407 0.6482 0.5791 -0.0239 0.0701  -0.0005 82  GLU D CD  
14991 O OE1 . GLU D 90  ? 0.6492 0.6671 0.6073 -0.0260 0.0802  0.0018  82  GLU D OE1 
14992 O OE2 . GLU D 90  ? 0.6790 0.6830 0.6086 -0.0191 0.0652  -0.0076 82  GLU D OE2 
14993 N N   . ASP D 91  ? 0.2260 0.2290 0.1874 -0.0375 0.0334  0.0065  83  ASP D N   
14994 C CA  . ASP D 91  ? 0.2196 0.2183 0.1783 -0.0366 0.0215  0.0032  83  ASP D CA  
14995 C C   . ASP D 91  ? 0.2230 0.2293 0.1989 -0.0366 0.0173  -0.0014 83  ASP D C   
14996 O O   . ASP D 91  ? 0.2149 0.2190 0.1884 -0.0338 0.0119  -0.0059 83  ASP D O   
14997 C CB  . ASP D 91  ? 0.2212 0.2145 0.1790 -0.0397 0.0164  0.0079  83  ASP D CB  
14998 C CG  . ASP D 91  ? 0.2819 0.2649 0.2191 -0.0381 0.0179  0.0128  83  ASP D CG  
14999 O OD1 . ASP D 91  ? 0.3269 0.3047 0.2462 -0.0337 0.0175  0.0104  83  ASP D OD1 
15000 O OD2 . ASP D 91  ? 0.2671 0.2461 0.2050 -0.0409 0.0188  0.0189  83  ASP D OD2 
15001 N N   . LEU D 92  ? 0.1925 0.2073 0.1859 -0.0395 0.0195  -0.0003 84  LEU D N   
15002 C CA  . LEU D 92  ? 0.1793 0.2002 0.1859 -0.0385 0.0147  -0.0040 84  LEU D CA  
15003 C C   . LEU D 92  ? 0.2335 0.2577 0.2410 -0.0338 0.0175  -0.0080 84  LEU D C   
15004 O O   . LEU D 92  ? 0.2066 0.2301 0.2166 -0.0311 0.0126  -0.0111 84  LEU D O   
15005 C CB  . LEU D 92  ? 0.2236 0.2527 0.2476 -0.0419 0.0148  -0.0029 84  LEU D CB  
15006 C CG  . LEU D 92  ? 0.2534 0.2787 0.2789 -0.0465 0.0121  0.0002  84  LEU D CG  
15007 C CD1 . LEU D 92  ? 0.2512 0.2848 0.2951 -0.0495 0.0106  -0.0010 84  LEU D CD1 
15008 C CD2 . LEU D 92  ? 0.1943 0.2119 0.2117 -0.0457 0.0046  -0.0004 84  LEU D CD2 
15009 N N   . LYS D 93  ? 0.2074 0.2342 0.2129 -0.0326 0.0264  -0.0078 85  LYS D N   
15010 C CA  . LYS D 93  ? 0.1738 0.2028 0.1796 -0.0275 0.0301  -0.0123 85  LYS D CA  
15011 C C   . LYS D 93  ? 0.2680 0.2867 0.2571 -0.0240 0.0262  -0.0162 85  LYS D C   
15012 O O   . LYS D 93  ? 0.2437 0.2621 0.2333 -0.0196 0.0278  -0.0208 85  LYS D O   
15013 C CB  . LYS D 93  ? 0.1851 0.2188 0.1921 -0.0267 0.0422  -0.0112 85  LYS D CB  
15014 C CG  . LYS D 93  ? 0.2019 0.2484 0.2325 -0.0297 0.0467  -0.0090 85  LYS D CG  
15015 C CD  . LYS D 93  ? 0.2643 0.3149 0.2968 -0.0292 0.0610  -0.0073 85  LYS D CD  
15016 C CE  . LYS D 93  ? 0.3112 0.3766 0.3730 -0.0318 0.0655  -0.0065 85  LYS D CE  
15017 N NZ  . LYS D 93  ? 0.3303 0.4000 0.3963 -0.0314 0.0818  -0.0043 85  LYS D NZ  
15018 N N   . ASN D 94  ? 0.2464 0.2565 0.2225 -0.0257 0.0207  -0.0150 86  ASN D N   
15019 C CA  . ASN D 94  ? 0.2104 0.2115 0.1742 -0.0230 0.0149  -0.0197 86  ASN D CA  
15020 C C   . ASN D 94  ? 0.2131 0.2115 0.1836 -0.0249 0.0056  -0.0199 86  ASN D C   
15021 O O   . ASN D 94  ? 0.2121 0.2033 0.1750 -0.0244 -0.0006 -0.0225 86  ASN D O   
15022 C CB  . ASN D 94  ? 0.3009 0.2939 0.2432 -0.0219 0.0159  -0.0193 86  ASN D CB  
15023 C CG  . ASN D 94  ? 0.3285 0.3214 0.2606 -0.0182 0.0262  -0.0211 86  ASN D CG  
15024 O OD1 . ASN D 94  ? 0.4118 0.4007 0.3370 -0.0139 0.0262  -0.0277 86  ASN D OD1 
15025 N ND2 . ASN D 94  ? 0.3291 0.3264 0.2623 -0.0199 0.0357  -0.0155 86  ASN D ND2 
15026 N N   . PHE D 95  ? 0.2137 0.2180 0.1987 -0.0266 0.0048  -0.0176 87  PHE D N   
15027 C CA  . PHE D 95  ? 0.1571 0.1590 0.1489 -0.0274 -0.0013 -0.0176 87  PHE D CA  
15028 C C   . PHE D 95  ? 0.1962 0.1921 0.1870 -0.0246 -0.0040 -0.0225 87  PHE D C   
15029 O O   . PHE D 95  ? 0.1881 0.1843 0.1802 -0.0212 -0.0009 -0.0256 87  PHE D O   
15030 C CB  . PHE D 95  ? 0.1469 0.1555 0.1511 -0.0274 -0.0008 -0.0156 87  PHE D CB  
15031 C CG  . PHE D 95  ? 0.1691 0.1743 0.1776 -0.0276 -0.0051 -0.0147 87  PHE D CG  
15032 C CD1 . PHE D 95  ? 0.1426 0.1439 0.1493 -0.0304 -0.0083 -0.0130 87  PHE D CD1 
15033 C CD2 . PHE D 95  ? 0.2020 0.2074 0.2163 -0.0244 -0.0053 -0.0149 87  PHE D CD2 
15034 C CE1 . PHE D 95  ? 0.1736 0.1716 0.1844 -0.0303 -0.0102 -0.0119 87  PHE D CE1 
15035 C CE2 . PHE D 95  ? 0.1731 0.1742 0.1892 -0.0241 -0.0075 -0.0130 87  PHE D CE2 
15036 C CZ  . PHE D 95  ? 0.1753 0.1727 0.1898 -0.0272 -0.0093 -0.0117 87  PHE D CZ  
15037 N N   . ARG D 96  ? 0.2118 0.2019 0.2018 -0.0260 -0.0096 -0.0234 88  ARG D N   
15038 C CA  . ARG D 96  ? 0.1969 0.1808 0.1905 -0.0247 -0.0128 -0.0281 88  ARG D CA  
15039 C C   . ARG D 96  ? 0.1964 0.1756 0.1801 -0.0220 -0.0134 -0.0345 88  ARG D C   
15040 O O   . ARG D 96  ? 0.2287 0.2028 0.2168 -0.0204 -0.0150 -0.0395 88  ARG D O   
15041 C CB  . ARG D 96  ? 0.1583 0.1425 0.1629 -0.0230 -0.0103 -0.0270 88  ARG D CB  
15042 C CG  . ARG D 96  ? 0.1598 0.1447 0.1718 -0.0251 -0.0111 -0.0222 88  ARG D CG  
15043 C CD  . ARG D 96  ? 0.2326 0.2166 0.2511 -0.0226 -0.0083 -0.0195 88  ARG D CD  
15044 N NE  . ARG D 96  ? 0.2018 0.1836 0.2240 -0.0244 -0.0086 -0.0157 88  ARG D NE  
15045 C CZ  . ARG D 96  ? 0.2542 0.2295 0.2831 -0.0244 -0.0075 -0.0149 88  ARG D CZ  
15046 N NH1 . ARG D 96  ? 0.2724 0.2421 0.3060 -0.0230 -0.0067 -0.0178 88  ARG D NH1 
15047 N NH2 . ARG D 96  ? 0.2604 0.2341 0.2920 -0.0259 -0.0061 -0.0113 88  ARG D NH2 
15048 N N   . GLN D 97  ? 0.1884 0.1680 0.1580 -0.0212 -0.0117 -0.0345 89  GLN D N   
15049 C CA  . GLN D 97  ? 0.2265 0.2003 0.1819 -0.0178 -0.0120 -0.0410 89  GLN D CA  
15050 C C   . GLN D 97  ? 0.2321 0.1997 0.1757 -0.0183 -0.0205 -0.0432 89  GLN D C   
15051 O O   . GLN D 97  ? 0.2384 0.2074 0.1824 -0.0209 -0.0238 -0.0382 89  GLN D O   
15052 C CB  . GLN D 97  ? 0.2508 0.2282 0.1962 -0.0154 -0.0027 -0.0395 89  GLN D CB  
15053 C CG  . GLN D 97  ? 0.2293 0.2146 0.1892 -0.0145 0.0044  -0.0375 89  GLN D CG  
15054 C CD  . GLN D 97  ? 0.3020 0.2842 0.2721 -0.0119 0.0029  -0.0424 89  GLN D CD  
15055 O OE1 . GLN D 97  ? 0.3241 0.2999 0.2875 -0.0085 0.0031  -0.0494 89  GLN D OE1 
15056 N NE2 . GLN D 97  ? 0.2318 0.2171 0.2168 -0.0132 0.0014  -0.0387 89  GLN D NE2 
15057 N N   . LEU D 98  ? 0.2464 0.2066 0.1798 -0.0153 -0.0248 -0.0515 90  LEU D N   
15058 C CA  . LEU D 98  ? 0.2966 0.2506 0.2202 -0.0150 -0.0358 -0.0555 90  LEU D CA  
15059 C C   . LEU D 98  ? 0.2938 0.2476 0.2009 -0.0147 -0.0362 -0.0491 90  LEU D C   
15060 O O   . LEU D 98  ? 0.2701 0.2233 0.1604 -0.0123 -0.0282 -0.0463 90  LEU D O   
15061 C CB  . LEU D 98  ? 0.3265 0.2718 0.2361 -0.0107 -0.0396 -0.0662 90  LEU D CB  
15062 C CG  . LEU D 98  ? 0.2838 0.2228 0.1852 -0.0100 -0.0540 -0.0718 90  LEU D CG  
15063 C CD1 . LEU D 98  ? 0.3234 0.2642 0.2519 -0.0143 -0.0621 -0.0742 90  LEU D CD1 
15064 C CD2 . LEU D 98  ? 0.3142 0.2433 0.1935 -0.0048 -0.0584 -0.0827 90  LEU D CD2 
15065 N N   . HIS D 99  ? 0.2696 0.2238 0.1830 -0.0169 -0.0446 -0.0464 91  HIS D N   
15066 C CA  . HIS D 99  ? 0.3477 0.2997 0.2464 -0.0162 -0.0475 -0.0404 91  HIS D CA  
15067 C C   . HIS D 99  ? 0.3012 0.2576 0.1979 -0.0179 -0.0361 -0.0307 91  HIS D C   
15068 O O   . HIS D 99  ? 0.3203 0.2730 0.2008 -0.0166 -0.0351 -0.0251 91  HIS D O   
15069 C CB  . HIS D 99  ? 0.4102 0.3528 0.2807 -0.0108 -0.0532 -0.0453 91  HIS D CB  
15070 C CG  . HIS D 99  ? 0.4084 0.3464 0.2817 -0.0094 -0.0677 -0.0553 91  HIS D CG  
15071 N ND1 . HIS D 99  ? 0.4295 0.3606 0.2893 -0.0055 -0.0712 -0.0657 91  HIS D ND1 
15072 C CD2 . HIS D 99  ? 0.3718 0.3115 0.2625 -0.0114 -0.0797 -0.0573 91  HIS D CD2 
15073 C CE1 . HIS D 99  ? 0.3966 0.3253 0.2658 -0.0057 -0.0857 -0.0740 91  HIS D CE1 
15074 N NE2 . HIS D 99  ? 0.4023 0.3367 0.2913 -0.0093 -0.0908 -0.0688 91  HIS D NE2 
15075 N N   . SER D 100 ? 0.2329 0.1968 0.1467 -0.0208 -0.0282 -0.0284 92  SER D N   
15076 C CA  . SER D 100 ? 0.2559 0.2247 0.1726 -0.0232 -0.0194 -0.0203 92  SER D CA  
15077 C C   . SER D 100 ? 0.2669 0.2370 0.1937 -0.0265 -0.0238 -0.0150 92  SER D C   
15078 O O   . SER D 100 ? 0.2338 0.2027 0.1690 -0.0270 -0.0324 -0.0173 92  SER D O   
15079 C CB  . SER D 100 ? 0.2623 0.2390 0.1940 -0.0245 -0.0113 -0.0206 92  SER D CB  
15080 O OG  . SER D 100 ? 0.2289 0.2095 0.1796 -0.0271 -0.0145 -0.0203 92  SER D OG  
15081 N N   . LYS D 101 ? 0.2304 0.2029 0.1582 -0.0288 -0.0174 -0.0080 93  LYS D N   
15082 C CA  . LYS D 101 ? 0.2712 0.2444 0.2093 -0.0318 -0.0201 -0.0033 93  LYS D CA  
15083 C C   . LYS D 101 ? 0.2373 0.2171 0.1953 -0.0345 -0.0191 -0.0045 93  LYS D C   
15084 O O   . LYS D 101 ? 0.2072 0.1875 0.1742 -0.0368 -0.0207 -0.0016 93  LYS D O   
15085 C CB  . LYS D 101 ? 0.2932 0.2647 0.2251 -0.0335 -0.0136 0.0042  93  LYS D CB  
15086 C CG  . LYS D 101 ? 0.3764 0.3384 0.2868 -0.0303 -0.0161 0.0078  93  LYS D CG  
15087 C CD  . LYS D 101 ? 0.4749 0.4336 0.3797 -0.0321 -0.0078 0.0165  93  LYS D CD  
15088 C CE  . LYS D 101 ? 0.6427 0.5898 0.5229 -0.0279 -0.0107 0.0213  93  LYS D CE  
15089 N NZ  . LYS D 101 ? 0.7159 0.6579 0.5873 -0.0291 0.0005  0.0306  93  LYS D NZ  
15090 N N   . THR D 102 ? 0.2449 0.2286 0.2087 -0.0337 -0.0167 -0.0087 94  THR D N   
15091 C CA  . THR D 102 ? 0.2012 0.1900 0.1801 -0.0352 -0.0153 -0.0091 94  THR D CA  
15092 C C   . THR D 102 ? 0.1905 0.1779 0.1752 -0.0334 -0.0183 -0.0139 94  THR D C   
15093 O O   . THR D 102 ? 0.1806 0.1704 0.1690 -0.0320 -0.0150 -0.0159 94  THR D O   
15094 C CB  . THR D 102 ? 0.2082 0.2034 0.1906 -0.0356 -0.0083 -0.0080 94  THR D CB  
15095 O OG1 . THR D 102 ? 0.1831 0.1782 0.1571 -0.0330 -0.0044 -0.0103 94  THR D OG1 
15096 C CG2 . THR D 102 ? 0.1912 0.1881 0.1747 -0.0387 -0.0052 -0.0030 94  THR D CG2 
15097 N N   . PRO D 103 ? 0.1797 0.1632 0.1673 -0.0335 -0.0244 -0.0157 95  PRO D N   
15098 C CA  . PRO D 103 ? 0.1615 0.1433 0.1586 -0.0328 -0.0263 -0.0198 95  PRO D CA  
15099 C C   . PRO D 103 ? 0.1850 0.1691 0.1932 -0.0335 -0.0221 -0.0174 95  PRO D C   
15100 O O   . PRO D 103 ? 0.1624 0.1493 0.1715 -0.0346 -0.0197 -0.0136 95  PRO D O   
15101 C CB  . PRO D 103 ? 0.1704 0.1490 0.1721 -0.0334 -0.0339 -0.0216 95  PRO D CB  
15102 C CG  . PRO D 103 ? 0.1587 0.1380 0.1568 -0.0344 -0.0350 -0.0168 95  PRO D CG  
15103 C CD  . PRO D 103 ? 0.1660 0.1464 0.1506 -0.0341 -0.0300 -0.0139 95  PRO D CD  
15104 N N   . GLY D 104 ? 0.2024 0.1840 0.2178 -0.0325 -0.0212 -0.0199 96  GLY D N   
15105 C CA  . GLY D 104 ? 0.1681 0.1501 0.1898 -0.0317 -0.0166 -0.0170 96  GLY D CA  
15106 C C   . GLY D 104 ? 0.2350 0.2168 0.2622 -0.0332 -0.0155 -0.0134 96  GLY D C   
15107 O O   . GLY D 104 ? 0.2310 0.2134 0.2571 -0.0322 -0.0120 -0.0103 96  GLY D O   
15108 N N   . HIS D 105 ? 0.1513 0.1164 0.1522 -0.0196 -0.0007 -0.0156 97  HIS D N   
15109 C CA  . HIS D 105 ? 0.1821 0.1446 0.1833 -0.0204 -0.0044 -0.0130 97  HIS D CA  
15110 C C   . HIS D 105 ? 0.1598 0.1275 0.1637 -0.0251 -0.0053 -0.0101 97  HIS D C   
15111 O O   . HIS D 105 ? 0.2473 0.2190 0.2493 -0.0285 -0.0030 -0.0095 97  HIS D O   
15112 C CB  . HIS D 105 ? 0.2255 0.1804 0.2202 -0.0202 -0.0043 -0.0132 97  HIS D CB  
15113 C CG  . HIS D 105 ? 0.3332 0.2815 0.3248 -0.0157 -0.0037 -0.0150 97  HIS D CG  
15114 N ND1 . HIS D 105 ? 0.4259 0.3699 0.4134 -0.0148 -0.0001 -0.0172 97  HIS D ND1 
15115 C CD2 . HIS D 105 ? 0.3924 0.3375 0.3843 -0.0119 -0.0062 -0.0147 97  HIS D CD2 
15116 C CE1 . HIS D 105 ? 0.4073 0.3448 0.3928 -0.0104 -0.0004 -0.0175 97  HIS D CE1 
15117 N NE2 . HIS D 105 ? 0.4266 0.3654 0.4143 -0.0086 -0.0043 -0.0158 97  HIS D NE2 
15118 N N   . PRO D 106 ? 0.1841 0.1521 0.1925 -0.0255 -0.0085 -0.0081 98  PRO D N   
15119 C CA  . PRO D 106 ? 0.2291 0.2010 0.2409 -0.0298 -0.0091 -0.0046 98  PRO D CA  
15120 C C   . PRO D 106 ? 0.2143 0.1846 0.2218 -0.0322 -0.0090 -0.0019 98  PRO D C   
15121 O O   . PRO D 106 ? 0.2236 0.1889 0.2279 -0.0306 -0.0099 -0.0025 98  PRO D O   
15122 C CB  . PRO D 106 ? 0.1942 0.1640 0.2114 -0.0292 -0.0124 -0.0041 98  PRO D CB  
15123 C CG  . PRO D 106 ? 0.1770 0.1455 0.1944 -0.0247 -0.0133 -0.0079 98  PRO D CG  
15124 C CD  . PRO D 106 ? 0.1683 0.1327 0.1787 -0.0224 -0.0114 -0.0092 98  PRO D CD  
15125 N N   . GLU D 107 ? 0.1996 0.1753 0.2070 -0.0362 -0.0079 0.0012  99  GLU D N   
15126 C CA  . GLU D 107 ? 0.1890 0.1659 0.1922 -0.0387 -0.0080 0.0042  99  GLU D CA  
15127 C C   . GLU D 107 ? 0.2136 0.1920 0.2208 -0.0413 -0.0101 0.0101  99  GLU D C   
15128 O O   . GLU D 107 ? 0.2460 0.2288 0.2559 -0.0441 -0.0094 0.0126  99  GLU D O   
15129 C CB  . GLU D 107 ? 0.1831 0.1660 0.1810 -0.0415 -0.0047 0.0028  99  GLU D CB  
15130 C CG  . GLU D 107 ? 0.2114 0.1906 0.2049 -0.0391 -0.0023 -0.0028 99  GLU D CG  
15131 C CD  . GLU D 107 ? 0.2542 0.2386 0.2426 -0.0421 0.0015  -0.0054 99  GLU D CD  
15132 O OE1 . GLU D 107 ? 0.2775 0.2690 0.2641 -0.0464 0.0018  -0.0024 99  GLU D OE1 
15133 O OE2 . GLU D 107 ? 0.2144 0.1955 0.2004 -0.0401 0.0043  -0.0104 99  GLU D OE2 
15134 N N   . TYR D 108 ? 0.1472 0.1219 0.1548 -0.0401 -0.0125 0.0126  100 TYR D N   
15135 C CA  . TYR D 108 ? 0.1500 0.1251 0.1612 -0.0418 -0.0145 0.0189  100 TYR D CA  
15136 C C   . TYR D 108 ? 0.1535 0.1365 0.1606 -0.0459 -0.0135 0.0233  100 TYR D C   
15137 O O   . TYR D 108 ? 0.1888 0.1762 0.1899 -0.0469 -0.0123 0.0216  100 TYR D O   
15138 C CB  . TYR D 108 ? 0.2052 0.1757 0.2178 -0.0390 -0.0170 0.0199  100 TYR D CB  
15139 C CG  . TYR D 108 ? 0.1882 0.1587 0.2046 -0.0398 -0.0191 0.0270  100 TYR D CG  
15140 C CD1 . TYR D 108 ? 0.2064 0.1713 0.2296 -0.0396 -0.0203 0.0294  100 TYR D CD1 
15141 C CD2 . TYR D 108 ? 0.2133 0.1894 0.2267 -0.0407 -0.0200 0.0313  100 TYR D CD2 
15142 C CE1 . TYR D 108 ? 0.2597 0.2229 0.2867 -0.0399 -0.0221 0.0365  100 TYR D CE1 
15143 C CE2 . TYR D 108 ? 0.2709 0.2470 0.2881 -0.0407 -0.0223 0.0388  100 TYR D CE2 
15144 C CZ  . TYR D 108 ? 0.2881 0.2569 0.3121 -0.0400 -0.0232 0.0416  100 TYR D CZ  
15145 O OH  . TYR D 108 ? 0.4187 0.3859 0.4469 -0.0396 -0.0253 0.0495  100 TYR D OH  
15146 N N   . GLY D 109 ? 0.1575 0.1425 0.1676 -0.0487 -0.0139 0.0290  101 GLY D N   
15147 C CA  . GLY D 109 ? 0.2071 0.2000 0.2129 -0.0526 -0.0136 0.0346  101 GLY D CA  
15148 C C   . GLY D 109 ? 0.3651 0.3644 0.3699 -0.0572 -0.0110 0.0364  101 GLY D C   
15149 O O   . GLY D 109 ? 0.4861 0.4885 0.4911 -0.0604 -0.0117 0.0438  101 GLY D O   
15150 N N   . TYR D 110 ? 0.3503 0.3520 0.3542 -0.0574 -0.0080 0.0300  102 TYR D N   
15151 C CA  . TYR D 110 ? 0.3479 0.3577 0.3507 -0.0618 -0.0048 0.0306  102 TYR D CA  
15152 C C   . TYR D 110 ? 0.3499 0.3582 0.3597 -0.0615 -0.0037 0.0280  102 TYR D C   
15153 O O   . TYR D 110 ? 0.3594 0.3746 0.3701 -0.0656 -0.0012 0.0295  102 TYR D O   
15154 C CB  . TYR D 110 ? 0.3824 0.3993 0.3784 -0.0628 -0.0013 0.0249  102 TYR D CB  
15155 N N   . THR D 111 ? 0.2683 0.2692 0.2828 -0.0573 -0.0053 0.0240  103 THR D N   
15156 C CA  . THR D 111 ? 0.2142 0.2144 0.2358 -0.0571 -0.0051 0.0216  103 THR D CA  
15157 C C   . THR D 111 ? 0.2118 0.2042 0.2390 -0.0575 -0.0082 0.0257  103 THR D C   
15158 O O   . THR D 111 ? 0.1893 0.1741 0.2170 -0.0539 -0.0108 0.0251  103 THR D O   
15159 C CB  . THR D 111 ? 0.2616 0.2597 0.2839 -0.0520 -0.0050 0.0141  103 THR D CB  
15160 O OG1 . THR D 111 ? 0.2933 0.2967 0.3104 -0.0514 -0.0018 0.0103  103 THR D OG1 
15161 C CG2 . THR D 111 ? 0.2076 0.2075 0.2376 -0.0518 -0.0051 0.0113  103 THR D CG2 
15162 N N   . ASP D 112 ? 0.2350 0.2293 0.2665 -0.0621 -0.0075 0.0299  104 ASP D N   
15163 C CA  . ASP D 112 ? 0.2091 0.1948 0.2464 -0.0631 -0.0099 0.0338  104 ASP D CA  
15164 C C   . ASP D 112 ? 0.2002 0.1796 0.2425 -0.0593 -0.0119 0.0276  104 ASP D C   
15165 O O   . ASP D 112 ? 0.1815 0.1653 0.2257 -0.0584 -0.0111 0.0217  104 ASP D O   
15166 C CB  . ASP D 112 ? 0.3038 0.2926 0.3454 -0.0694 -0.0082 0.0382  104 ASP D CB  
15167 C CG  . ASP D 112 ? 0.3778 0.3700 0.4148 -0.0735 -0.0072 0.0468  104 ASP D CG  
15168 O OD1 . ASP D 112 ? 0.3566 0.3493 0.3876 -0.0713 -0.0082 0.0493  104 ASP D OD1 
15169 O OD2 . ASP D 112 ? 0.4152 0.4105 0.4546 -0.0793 -0.0053 0.0512  104 ASP D OD2 
15170 N N   . GLY D 113 ? 0.2080 0.1776 0.2525 -0.0571 -0.0145 0.0290  105 GLY D N   
15171 C CA  . GLY D 113 ? 0.2251 0.1888 0.2741 -0.0545 -0.0163 0.0232  105 GLY D CA  
15172 C C   . GLY D 113 ? 0.2361 0.1988 0.2810 -0.0489 -0.0174 0.0178  105 GLY D C   
15173 O O   . GLY D 113 ? 0.2437 0.2016 0.2913 -0.0465 -0.0190 0.0132  105 GLY D O   
15174 N N   . VAL D 114 ? 0.1815 0.1484 0.2197 -0.0472 -0.0163 0.0180  106 VAL D N   
15175 C CA  . VAL D 114 ? 0.1743 0.1391 0.2082 -0.0424 -0.0170 0.0138  106 VAL D CA  
15176 C C   . VAL D 114 ? 0.2584 0.2173 0.2917 -0.0406 -0.0187 0.0167  106 VAL D C   
15177 O O   . VAL D 114 ? 0.2144 0.1752 0.2456 -0.0420 -0.0185 0.0220  106 VAL D O   
15178 C CB  . VAL D 114 ? 0.1559 0.1268 0.1834 -0.0418 -0.0147 0.0121  106 VAL D CB  
15179 C CG1 . VAL D 114 ? 0.1948 0.1622 0.2176 -0.0376 -0.0152 0.0084  106 VAL D CG1 
15180 C CG2 . VAL D 114 ? 0.1708 0.1481 0.2003 -0.0427 -0.0129 0.0090  106 VAL D CG2 
15181 N N   . GLU D 115 ? 0.2204 0.1732 0.2556 -0.0374 -0.0203 0.0131  107 GLU D N   
15182 C CA  . GLU D 115 ? 0.1548 0.1022 0.1913 -0.0353 -0.0217 0.0154  107 GLU D CA  
15183 C C   . GLU D 115 ? 0.1597 0.1091 0.1905 -0.0327 -0.0215 0.0145  107 GLU D C   
15184 O O   . GLU D 115 ? 0.2297 0.1781 0.2613 -0.0314 -0.0225 0.0177  107 GLU D O   
15185 C CB  . GLU D 115 ? 0.1755 0.1159 0.2172 -0.0335 -0.0231 0.0113  107 GLU D CB  
15186 C CG  . GLU D 115 ? 0.2321 0.1692 0.2805 -0.0368 -0.0233 0.0116  107 GLU D CG  
15187 C CD  . GLU D 115 ? 0.2344 0.1674 0.2871 -0.0389 -0.0235 0.0188  107 GLU D CD  
15188 O OE1 . GLU D 115 ? 0.2557 0.1886 0.3068 -0.0372 -0.0239 0.0237  107 GLU D OE1 
15189 O OE2 . GLU D 115 ? 0.2569 0.1870 0.3149 -0.0426 -0.0232 0.0199  107 GLU D OE2 
15190 N N   . THR D 116 ? 0.1785 0.1306 0.2040 -0.0317 -0.0203 0.0102  108 THR D N   
15191 C CA  . THR D 116 ? 0.1948 0.1481 0.2146 -0.0300 -0.0197 0.0087  108 THR D CA  
15192 C C   . THR D 116 ? 0.1488 0.1053 0.1633 -0.0304 -0.0176 0.0056  108 THR D C   
15193 O O   . THR D 116 ? 0.1982 0.1556 0.2141 -0.0306 -0.0171 0.0038  108 THR D O   
15194 C CB  . THR D 116 ? 0.2200 0.1685 0.2405 -0.0267 -0.0207 0.0051  108 THR D CB  
15195 O OG1 . THR D 116 ? 0.2142 0.1644 0.2294 -0.0257 -0.0197 0.0040  108 THR D OG1 
15196 C CG2 . THR D 116 ? 0.2253 0.1713 0.2460 -0.0253 -0.0209 0.0002  108 THR D CG2 
15197 N N   . THR D 117 ? 0.1422 0.1005 0.1509 -0.0305 -0.0163 0.0050  109 THR D N   
15198 C CA  . THR D 117 ? 0.1653 0.1247 0.1688 -0.0304 -0.0139 0.0016  109 THR D CA  
15199 C C   . THR D 117 ? 0.1619 0.1159 0.1629 -0.0272 -0.0139 -0.0022 109 THR D C   
15200 O O   . THR D 117 ? 0.2152 0.1674 0.2144 -0.0266 -0.0143 -0.0026 109 THR D O   
15201 C CB  . THR D 117 ? 0.2137 0.1773 0.2120 -0.0331 -0.0120 0.0024  109 THR D CB  
15202 O OG1 . THR D 117 ? 0.2078 0.1773 0.2076 -0.0363 -0.0122 0.0066  109 THR D OG1 
15203 C CG2 . THR D 117 ? 0.2090 0.1721 0.2023 -0.0330 -0.0090 -0.0017 109 THR D CG2 
15204 N N   . THR D 118 ? 0.1685 0.1210 0.1697 -0.0252 -0.0137 -0.0048 110 THR D N   
15205 C CA  . THR D 118 ? 0.2319 0.1797 0.2298 -0.0222 -0.0138 -0.0077 110 THR D CA  
15206 C C   . THR D 118 ? 0.2776 0.2243 0.2714 -0.0208 -0.0116 -0.0096 110 THR D C   
15207 O O   . THR D 118 ? 0.3327 0.2828 0.3277 -0.0216 -0.0101 -0.0096 110 THR D O   
15208 C CB  . THR D 118 ? 0.1721 0.1187 0.1740 -0.0202 -0.0164 -0.0089 110 THR D CB  
15209 O OG1 . THR D 118 ? 0.2285 0.1787 0.2344 -0.0202 -0.0168 -0.0092 110 THR D OG1 
15210 C CG2 . THR D 118 ? 0.2264 0.1723 0.2327 -0.0212 -0.0181 -0.0077 110 THR D CG2 
15211 N N   . GLY D 119 ? 0.2553 0.1971 0.2445 -0.0186 -0.0111 -0.0111 111 GLY D N   
15212 C CA  . GLY D 119 ? 0.2856 0.2239 0.2703 -0.0170 -0.0086 -0.0125 111 GLY D CA  
15213 C C   . GLY D 119 ? 0.2869 0.2190 0.2658 -0.0160 -0.0080 -0.0130 111 GLY D C   
15214 O O   . GLY D 119 ? 0.3012 0.2297 0.2779 -0.0127 -0.0086 -0.0133 111 GLY D O   
15215 N N   . PRO D 120 ? 0.2710 0.2024 0.2470 -0.0190 -0.0068 -0.0130 112 PRO D N   
15216 C CA  . PRO D 120 ? 0.2002 0.1268 0.1713 -0.0188 -0.0063 -0.0134 112 PRO D CA  
15217 C C   . PRO D 120 ? 0.2227 0.1504 0.1959 -0.0168 -0.0092 -0.0133 112 PRO D C   
15218 O O   . PRO D 120 ? 0.2455 0.1773 0.2238 -0.0175 -0.0111 -0.0130 112 PRO D O   
15219 C CB  . PRO D 120 ? 0.2370 0.1660 0.2069 -0.0230 -0.0048 -0.0136 112 PRO D CB  
15220 C CG  . PRO D 120 ? 0.2651 0.1983 0.2368 -0.0252 -0.0038 -0.0135 112 PRO D CG  
15221 C CD  . PRO D 120 ? 0.2834 0.2195 0.2605 -0.0229 -0.0060 -0.0124 112 PRO D CD  
15222 N N   . LEU D 121 ? 0.1971 0.1208 0.1665 -0.0141 -0.0095 -0.0135 113 LEU D N   
15223 C CA  . LEU D 121 ? 0.1703 0.0958 0.1413 -0.0121 -0.0123 -0.0141 113 LEU D CA  
15224 C C   . LEU D 121 ? 0.2115 0.1383 0.1826 -0.0137 -0.0124 -0.0152 113 LEU D C   
15225 O O   . LEU D 121 ? 0.2261 0.1517 0.1940 -0.0158 -0.0102 -0.0152 113 LEU D O   
15226 C CB  . LEU D 121 ? 0.1991 0.1211 0.1650 -0.0089 -0.0128 -0.0135 113 LEU D CB  
15227 C CG  . LEU D 121 ? 0.2604 0.1822 0.2279 -0.0063 -0.0129 -0.0126 113 LEU D CG  
15228 C CD1 . LEU D 121 ? 0.2843 0.2024 0.2467 -0.0023 -0.0135 -0.0110 113 LEU D CD1 
15229 C CD2 . LEU D 121 ? 0.3088 0.2373 0.2841 -0.0060 -0.0154 -0.0134 113 LEU D CD2 
15230 N N   . GLY D 122 ? 0.1889 0.1185 0.1640 -0.0127 -0.0149 -0.0166 114 GLY D N   
15231 C CA  . GLY D 122 ? 0.1945 0.1255 0.1708 -0.0134 -0.0150 -0.0184 114 GLY D CA  
15232 C C   . GLY D 122 ? 0.1942 0.1280 0.1776 -0.0147 -0.0153 -0.0181 114 GLY D C   
15233 O O   . GLY D 122 ? 0.1937 0.1288 0.1812 -0.0142 -0.0162 -0.0199 114 GLY D O   
15234 N N   . GLN D 123 ? 0.1730 0.1079 0.1579 -0.0163 -0.0145 -0.0157 115 GLN D N   
15235 C CA  . GLN D 123 ? 0.1688 0.1069 0.1596 -0.0175 -0.0150 -0.0142 115 GLN D CA  
15236 C C   . GLN D 123 ? 0.2024 0.1410 0.2004 -0.0170 -0.0173 -0.0136 115 GLN D C   
15237 O O   . GLN D 123 ? 0.1986 0.1383 0.2023 -0.0168 -0.0181 -0.0128 115 GLN D O   
15238 C CB  . GLN D 123 ? 0.1992 0.1395 0.1884 -0.0200 -0.0136 -0.0119 115 GLN D CB  
15239 C CG  . GLN D 123 ? 0.1848 0.1251 0.1686 -0.0216 -0.0112 -0.0128 115 GLN D CG  
15240 C CD  . GLN D 123 ? 0.2160 0.1594 0.1984 -0.0248 -0.0099 -0.0114 115 GLN D CD  
15241 O OE1 . GLN D 123 ? 0.1775 0.1263 0.1642 -0.0259 -0.0110 -0.0093 115 GLN D OE1 
15242 N NE2 . GLN D 123 ? 0.1931 0.1331 0.1694 -0.0263 -0.0075 -0.0124 115 GLN D NE2 
15243 N N   . GLY D 124 ? 0.1797 0.1177 0.1781 -0.0166 -0.0183 -0.0139 116 GLY D N   
15244 C CA  . GLY D 124 ? 0.1666 0.1051 0.1718 -0.0170 -0.0201 -0.0136 116 GLY D CA  
15245 C C   . GLY D 124 ? 0.1593 0.0960 0.1686 -0.0159 -0.0213 -0.0164 116 GLY D C   
15246 O O   . GLY D 124 ? 0.1578 0.0935 0.1736 -0.0164 -0.0221 -0.0153 116 GLY D O   
15247 N N   . ILE D 125 ? 0.1918 0.1276 0.1970 -0.0145 -0.0214 -0.0200 117 ILE D N   
15248 C CA  . ILE D 125 ? 0.2187 0.1532 0.2272 -0.0137 -0.0221 -0.0238 117 ILE D CA  
15249 C C   . ILE D 125 ? 0.2002 0.1342 0.2121 -0.0130 -0.0209 -0.0233 117 ILE D C   
15250 O O   . ILE D 125 ? 0.1988 0.1308 0.2175 -0.0124 -0.0214 -0.0246 117 ILE D O   
15251 C CB  . ILE D 125 ? 0.2283 0.1633 0.2304 -0.0126 -0.0222 -0.0278 117 ILE D CB  
15252 C CG1 . ILE D 125 ? 0.1714 0.1057 0.1765 -0.0121 -0.0224 -0.0328 117 ILE D CG1 
15253 C CG2 . ILE D 125 ? 0.2580 0.1933 0.2523 -0.0122 -0.0202 -0.0265 117 ILE D CG2 
15254 C CD1 . ILE D 125 ? 0.1991 0.1316 0.2121 -0.0132 -0.0240 -0.0348 117 ILE D CD1 
15255 N N   . ALA D 126 ? 0.1651 0.1011 0.1731 -0.0132 -0.0193 -0.0212 118 ALA D N   
15256 C CA  . ALA D 126 ? 0.2005 0.1382 0.2125 -0.0124 -0.0185 -0.0202 118 ALA D CA  
15257 C C   . ALA D 126 ? 0.2306 0.1682 0.2498 -0.0127 -0.0198 -0.0159 118 ALA D C   
15258 O O   . ALA D 126 ? 0.1676 0.1046 0.1936 -0.0109 -0.0201 -0.0157 118 ALA D O   
15259 C CB  . ALA D 126 ? 0.1775 0.1183 0.1837 -0.0134 -0.0166 -0.0191 118 ALA D CB  
15260 N N   . ASN D 127 ? 0.1531 0.0916 0.1709 -0.0147 -0.0202 -0.0122 119 ASN D N   
15261 C CA  . ASN D 127 ? 0.2021 0.1405 0.2259 -0.0155 -0.0215 -0.0076 119 ASN D CA  
15262 C C   . ASN D 127 ? 0.1737 0.1071 0.2046 -0.0146 -0.0226 -0.0090 119 ASN D C   
15263 O O   . ASN D 127 ? 0.1750 0.1066 0.2127 -0.0136 -0.0233 -0.0061 119 ASN D O   
15264 C CB  . ASN D 127 ? 0.1843 0.1246 0.2054 -0.0181 -0.0215 -0.0046 119 ASN D CB  
15265 C CG  . ASN D 127 ? 0.1835 0.1278 0.1976 -0.0195 -0.0199 -0.0037 119 ASN D CG  
15266 O OD1 . ASN D 127 ? 0.1869 0.1320 0.1975 -0.0211 -0.0192 -0.0035 119 ASN D OD1 
15267 N ND2 . ASN D 127 ? 0.1423 0.0893 0.1550 -0.0192 -0.0192 -0.0037 119 ASN D ND2 
15268 N N   . ALA D 128 ? 0.1935 0.1247 0.2231 -0.0150 -0.0229 -0.0134 120 ALA D N   
15269 C CA  . ALA D 128 ? 0.2038 0.1302 0.2399 -0.0153 -0.0238 -0.0157 120 ALA D CA  
15270 C C   . ALA D 128 ? 0.1604 0.0836 0.2010 -0.0126 -0.0233 -0.0191 120 ALA D C   
15271 O O   . ALA D 128 ? 0.2107 0.1287 0.2588 -0.0122 -0.0237 -0.0190 120 ALA D O   
15272 C CB  . ALA D 128 ? 0.1565 0.0834 0.1897 -0.0166 -0.0245 -0.0201 120 ALA D CB  
15273 N N   . VAL D 129 ? 0.1609 0.0868 0.1970 -0.0108 -0.0222 -0.0224 121 VAL D N   
15274 C CA  . VAL D 129 ? 0.1955 0.1199 0.2362 -0.0079 -0.0211 -0.0259 121 VAL D CA  
15275 C C   . VAL D 129 ? 0.2035 0.1272 0.2517 -0.0060 -0.0214 -0.0206 121 VAL D C   
15276 O O   . VAL D 129 ? 0.1869 0.1057 0.2430 -0.0037 -0.0213 -0.0218 121 VAL D O   
15277 C CB  . VAL D 129 ? 0.1984 0.1275 0.2324 -0.0069 -0.0194 -0.0293 121 VAL D CB  
15278 C CG1 . VAL D 129 ? 0.1951 0.1248 0.2345 -0.0037 -0.0179 -0.0323 121 VAL D CG1 
15279 C CG2 . VAL D 129 ? 0.2072 0.1362 0.2343 -0.0082 -0.0195 -0.0346 121 VAL D CG2 
15280 N N   . GLY D 130 ? 0.1898 0.1180 0.2356 -0.0069 -0.0219 -0.0144 122 GLY D N   
15281 C CA  . GLY D 130 ? 0.1978 0.1270 0.2500 -0.0052 -0.0228 -0.0083 122 GLY D CA  
15282 C C   . GLY D 130 ? 0.1828 0.1055 0.2414 -0.0059 -0.0241 -0.0044 122 GLY D C   
15283 O O   . GLY D 130 ? 0.1984 0.1177 0.2649 -0.0032 -0.0246 -0.0013 122 GLY D O   
15284 N N   . MET D 131 ? 0.1712 0.0918 0.2267 -0.0096 -0.0245 -0.0042 123 MET D N   
15285 C CA  . MET D 131 ? 0.1807 0.0949 0.2423 -0.0112 -0.0253 -0.0009 123 MET D CA  
15286 C C   . MET D 131 ? 0.1941 0.0997 0.2629 -0.0096 -0.0248 -0.0060 123 MET D C   
15287 O O   . MET D 131 ? 0.1962 0.0949 0.2726 -0.0087 -0.0252 -0.0024 123 MET D O   
15288 C CB  . MET D 131 ? 0.2040 0.1195 0.2613 -0.0157 -0.0255 -0.0007 123 MET D CB  
15289 C CG  . MET D 131 ? 0.2311 0.1539 0.2826 -0.0177 -0.0256 0.0046  123 MET D CG  
15290 S SD  . MET D 131 ? 0.2040 0.1293 0.2513 -0.0220 -0.0253 0.0031  123 MET D SD  
15291 C CE  . MET D 131 ? 0.2122 0.1461 0.2519 -0.0232 -0.0245 0.0073  123 MET D CE  
15292 N N   . ALA D 132 ? 0.2320 0.1374 0.2981 -0.0093 -0.0240 -0.0143 124 ALA D N   
15293 C CA  . ALA D 132 ? 0.2361 0.1339 0.3086 -0.0080 -0.0232 -0.0206 124 ALA D CA  
15294 C C   . ALA D 132 ? 0.2587 0.1543 0.3377 -0.0028 -0.0222 -0.0204 124 ALA D C   
15295 O O   . ALA D 132 ? 0.2515 0.1384 0.3389 -0.0011 -0.0216 -0.0223 124 ALA D O   
15296 C CB  . ALA D 132 ? 0.2542 0.1543 0.3211 -0.0092 -0.0226 -0.0297 124 ALA D CB  
15297 N N   . LEU D 133 ? 0.2478 0.1514 0.3236 -0.0002 -0.0220 -0.0186 125 LEU D N   
15298 C CA  . LEU D 133 ? 0.2529 0.1570 0.3358 0.0051  -0.0212 -0.0180 125 LEU D CA  
15299 C C   . LEU D 133 ? 0.2733 0.1730 0.3641 0.0070  -0.0227 -0.0092 125 LEU D C   
15300 O O   . LEU D 133 ? 0.2570 0.1506 0.3573 0.0113  -0.0222 -0.0094 125 LEU D O   
15301 C CB  . LEU D 133 ? 0.2238 0.1388 0.3011 0.0063  -0.0207 -0.0179 125 LEU D CB  
15302 C CG  . LEU D 133 ? 0.3103 0.2291 0.3942 0.0116  -0.0194 -0.0196 125 LEU D CG  
15303 C CD1 . LEU D 133 ? 0.3031 0.2160 0.3919 0.0141  -0.0171 -0.0287 125 LEU D CD1 
15304 C CD2 . LEU D 133 ? 0.3056 0.2359 0.3826 0.0110  -0.0186 -0.0202 125 LEU D CD2 
15305 N N   . ALA D 134 ? 0.2510 0.1539 0.3381 0.0039  -0.0245 -0.0013 126 ALA D N   
15306 C CA  . ALA D 134 ? 0.2154 0.1146 0.3088 0.0051  -0.0261 0.0082  126 ALA D CA  
15307 C C   . ALA D 134 ? 0.2401 0.1257 0.3409 0.0046  -0.0256 0.0075  126 ALA D C   
15308 O O   . ALA D 134 ? 0.2749 0.1538 0.3846 0.0084  -0.0260 0.0123  126 ALA D O   
15309 C CB  . ALA D 134 ? 0.1917 0.0971 0.2782 0.0008  -0.0276 0.0157  126 ALA D CB  
15310 N N   . GLU D 135 ? 0.2075 0.0888 0.3051 -0.0001 -0.0248 0.0019  127 GLU D N   
15311 C CA  . GLU D 135 ? 0.2246 0.0929 0.3294 -0.0016 -0.0240 0.0002  127 GLU D CA  
15312 C C   . GLU D 135 ? 0.2454 0.1063 0.3586 0.0036  -0.0224 -0.0062 127 GLU D C   
15313 O O   . GLU D 135 ? 0.2428 0.0950 0.3625 0.0054  -0.0214 -0.0035 127 GLU D O   
15314 C CB  . GLU D 135 ? 0.2164 0.0841 0.3165 -0.0078 -0.0236 -0.0061 127 GLU D CB  
15315 C CG  . GLU D 135 ? 0.2523 0.1102 0.3568 -0.0112 -0.0225 -0.0065 127 GLU D CG  
15316 C CD  . GLU D 135 ? 0.2981 0.1507 0.4049 -0.0098 -0.0201 -0.0164 127 GLU D CD  
15317 O OE1 . GLU D 135 ? 0.2841 0.1400 0.3900 -0.0065 -0.0195 -0.0234 127 GLU D OE1 
15318 O OE2 . GLU D 135 ? 0.2578 0.1031 0.3670 -0.0126 -0.0187 -0.0173 127 GLU D OE2 
15319 N N   . LYS D 136 ? 0.3121 0.1791 0.4222 0.0059  -0.0211 -0.0144 128 LYS D N   
15320 C CA  A LYS D 136 ? 0.3490 0.2104 0.4666 0.0109  -0.0190 -0.0217 128 LYS D CA  
15321 C CA  B LYS D 136 ? 0.3487 0.2101 0.4663 0.0109  -0.0190 -0.0217 128 LYS D CA  
15322 C C   . LYS D 136 ? 0.2352 0.0954 0.3619 0.0178  -0.0194 -0.0148 128 LYS D C   
15323 O O   . LYS D 136 ? 0.2585 0.1110 0.3921 0.0211  -0.0176 -0.0156 128 LYS D O   
15324 C CB  A LYS D 136 ? 0.3577 0.2282 0.4688 0.0115  -0.0175 -0.0310 128 LYS D CB  
15325 C CB  B LYS D 136 ? 0.3571 0.2275 0.4681 0.0114  -0.0175 -0.0310 128 LYS D CB  
15326 C CG  A LYS D 136 ? 0.3765 0.2449 0.4950 0.0174  -0.0149 -0.0382 128 LYS D CG  
15327 C CG  B LYS D 136 ? 0.3785 0.2451 0.4964 0.0160  -0.0147 -0.0402 128 LYS D CG  
15328 C CD  A LYS D 136 ? 0.3312 0.2122 0.4431 0.0186  -0.0136 -0.0433 128 LYS D CD  
15329 C CD  B LYS D 136 ? 0.3675 0.2387 0.4774 0.0131  -0.0131 -0.0513 128 LYS D CD  
15330 C CE  A LYS D 136 ? 0.3154 0.1972 0.4359 0.0254  -0.0110 -0.0482 128 LYS D CE  
15331 C CE  B LYS D 136 ? 0.3322 0.2028 0.4460 0.0169  -0.0096 -0.0604 128 LYS D CE  
15332 N NZ  A LYS D 136 ? 0.2510 0.1241 0.3759 0.0259  -0.0081 -0.0589 128 LYS D NZ  
15333 N NZ  B LYS D 136 ? 0.2368 0.1115 0.3417 0.0129  -0.0081 -0.0705 128 LYS D NZ  
15334 N N   . ILE D 137 ? 0.2671 0.1388 0.3904 0.0195  -0.0211 -0.0077 129 ILE D N   
15335 C CA  . ILE D 137 ? 0.3405 0.2143 0.4720 0.0261  -0.0221 -0.0003 129 ILE D CA  
15336 C C   . ILE D 137 ? 0.3316 0.1938 0.4706 0.0269  -0.0235 0.0091  129 ILE D C   
15337 O O   . ILE D 137 ? 0.2847 0.1408 0.4331 0.0329  -0.0229 0.0111  129 ILE D O   
15338 C CB  . ILE D 137 ? 0.3241 0.2137 0.4489 0.0258  -0.0241 0.0056  129 ILE D CB  
15339 C CG1 . ILE D 137 ? 0.3738 0.2737 0.4931 0.0260  -0.0222 -0.0032 129 ILE D CG1 
15340 C CG2 . ILE D 137 ? 0.3760 0.2696 0.5087 0.0317  -0.0262 0.0152  129 ILE D CG2 
15341 C CD1 . ILE D 137 ? 0.2702 0.1848 0.3823 0.0244  -0.0237 0.0013  129 ILE D CD1 
15342 N N   . LEU D 138 ? 0.2645 0.1251 0.3976 0.0207  -0.0250 0.0149  130 LEU D N   
15343 C CA  . LEU D 138 ? 0.2708 0.1234 0.4073 0.0200  -0.0259 0.0249  130 LEU D CA  
15344 C C   . LEU D 138 ? 0.2660 0.1066 0.4050 0.0192  -0.0228 0.0197  130 LEU D C   
15345 O O   . LEU D 138 ? 0.2960 0.1295 0.4399 0.0219  -0.0226 0.0261  130 LEU D O   
15346 C CB  . LEU D 138 ? 0.2833 0.1389 0.4122 0.0128  -0.0277 0.0316  130 LEU D CB  
15347 C CG  . LEU D 138 ? 0.2921 0.1638 0.4136 0.0127  -0.0300 0.0379  130 LEU D CG  
15348 C CD1 . LEU D 138 ? 0.2855 0.1621 0.3973 0.0050  -0.0305 0.0410  130 LEU D CD1 
15349 C CD2 . LEU D 138 ? 0.2839 0.1576 0.4116 0.0182  -0.0324 0.0492  130 LEU D CD2 
15350 N N   . ALA D 139 ? 0.2645 0.1029 0.4000 0.0155  -0.0205 0.0083  131 ALA D N   
15351 C CA  . ALA D 139 ? 0.2789 0.1063 0.4167 0.0145  -0.0176 0.0025  131 ALA D CA  
15352 C C   . ALA D 139 ? 0.3555 0.1787 0.5014 0.0223  -0.0158 -0.0006 131 ALA D C   
15353 O O   . ALA D 139 ? 0.3080 0.1206 0.4587 0.0241  -0.0144 0.0016  131 ALA D O   
15354 C CB  . ALA D 139 ? 0.2748 0.1031 0.4065 0.0087  -0.0160 -0.0088 131 ALA D CB  
15355 N N   . ALA D 140 ? 0.3421 0.1734 0.4897 0.0270  -0.0156 -0.0058 132 ALA D N   
15356 C CA  . ALA D 140 ? 0.3353 0.1647 0.4915 0.0349  -0.0138 -0.0088 132 ALA D CA  
15357 C C   . ALA D 140 ? 0.3237 0.1506 0.4871 0.0407  -0.0156 0.0033  132 ALA D C   
15358 O O   . ALA D 140 ? 0.3584 0.1774 0.5286 0.0459  -0.0139 0.0031  132 ALA D O   
15359 C CB  . ALA D 140 ? 0.2782 0.1190 0.4351 0.0386  -0.0134 -0.0155 132 ALA D CB  
15360 N N   . GLU D 141 ? 0.2902 0.1238 0.4515 0.0399  -0.0192 0.0141  133 GLU D N   
15361 C CA  . GLU D 141 ? 0.3907 0.2247 0.5578 0.0455  -0.0215 0.0264  133 GLU D CA  
15362 C C   . GLU D 141 ? 0.4146 0.2361 0.5812 0.0428  -0.0212 0.0336  133 GLU D C   
15363 O O   . GLU D 141 ? 0.3492 0.1644 0.5222 0.0485  -0.0211 0.0389  133 GLU D O   
15364 C CB  . GLU D 141 ? 0.3666 0.2139 0.5311 0.0452  -0.0256 0.0353  133 GLU D CB  
15365 C CG  . GLU D 141 ? 0.3106 0.1607 0.4791 0.0498  -0.0286 0.0492  133 GLU D CG  
15366 C CD  . GLU D 141 ? 0.2983 0.1639 0.4643 0.0498  -0.0327 0.0569  133 GLU D CD  
15367 O OE1 . GLU D 141 ? 0.3691 0.2413 0.5389 0.0546  -0.0357 0.0673  133 GLU D OE1 
15368 O OE2 . GLU D 141 ? 0.3336 0.2050 0.4936 0.0448  -0.0332 0.0525  133 GLU D OE2 
15369 N N   . PHE D 142 ? 0.3694 0.1872 0.5285 0.0343  -0.0211 0.0338  134 PHE D N   
15370 C CA  . PHE D 142 ? 0.3469 0.1553 0.5048 0.0310  -0.0212 0.0426  134 PHE D CA  
15371 C C   . PHE D 142 ? 0.3656 0.1594 0.5236 0.0272  -0.0178 0.0357  134 PHE D C   
15372 O O   . PHE D 142 ? 0.4057 0.1887 0.5659 0.0274  -0.0172 0.0422  134 PHE D O   
15373 C CB  . PHE D 142 ? 0.3840 0.1992 0.5339 0.0238  -0.0235 0.0497  134 PHE D CB  
15374 C CG  . PHE D 142 ? 0.3943 0.2211 0.5439 0.0269  -0.0273 0.0609  134 PHE D CG  
15375 C CD1 . PHE D 142 ? 0.3795 0.2043 0.5308 0.0295  -0.0291 0.0735  134 PHE D CD1 
15376 C CD2 . PHE D 142 ? 0.3165 0.1564 0.4637 0.0273  -0.0292 0.0589  134 PHE D CD2 
15377 C CE1 . PHE D 142 ? 0.3484 0.1857 0.4987 0.0320  -0.0329 0.0838  134 PHE D CE1 
15378 C CE2 . PHE D 142 ? 0.3296 0.1812 0.4763 0.0298  -0.0329 0.0691  134 PHE D CE2 
15379 C CZ  . PHE D 142 ? 0.3516 0.2026 0.4997 0.0320  -0.0348 0.0815  134 PHE D CZ  
15380 N N   . ASN D 143 ? 0.3601 0.1535 0.5156 0.0236  -0.0155 0.0230  135 ASN D N   
15381 C CA  . ASN D 143 ? 0.3481 0.1289 0.5030 0.0189  -0.0126 0.0167  135 ASN D CA  
15382 C C   . ASN D 143 ? 0.4065 0.1751 0.5691 0.0251  -0.0103 0.0148  135 ASN D C   
15383 O O   . ASN D 143 ? 0.3740 0.1456 0.5418 0.0323  -0.0097 0.0107  135 ASN D O   
15384 C CB  . ASN D 143 ? 0.3389 0.1237 0.4889 0.0137  -0.0110 0.0034  135 ASN D CB  
15385 C CG  . ASN D 143 ? 0.3242 0.1175 0.4665 0.0062  -0.0127 0.0048  135 ASN D CG  
15386 O OD1 . ASN D 143 ? 0.3837 0.1789 0.5240 0.0039  -0.0146 0.0151  135 ASN D OD1 
15387 N ND2 . ASN D 143 ? 0.3150 0.1138 0.4526 0.0024  -0.0120 -0.0057 135 ASN D ND2 
15388 N N   . LYS D 144 ? 0.3861 0.1407 0.5494 0.0221  -0.0089 0.0178  136 LYS D N   
15389 C CA  . LYS D 144 ? 0.4135 0.1536 0.5835 0.0268  -0.0065 0.0160  136 LYS D CA  
15390 C C   . LYS D 144 ? 0.5487 0.2779 0.7166 0.0200  -0.0035 0.0060  136 LYS D C   
15391 O O   . LYS D 144 ? 0.5563 0.2883 0.7178 0.0113  -0.0036 0.0036  136 LYS D O   
15392 C CB  . LYS D 144 ? 0.4415 0.1732 0.6145 0.0299  -0.0079 0.0302  136 LYS D CB  
15393 C CG  . LYS D 144 ? 0.4722 0.2159 0.6461 0.0353  -0.0116 0.0416  136 LYS D CG  
15394 C CD  . LYS D 144 ? 0.5140 0.2642 0.6949 0.0452  -0.0119 0.0386  136 LYS D CD  
15395 C CE  . LYS D 144 ? 0.5448 0.3041 0.7281 0.0514  -0.0157 0.0520  136 LYS D CE  
15396 N NZ  . LYS D 144 ? 0.5691 0.3374 0.7596 0.0609  -0.0162 0.0491  136 LYS D NZ  
15397 N N   . ASP D 145 ? 0.5478 0.2649 0.7214 0.0239  -0.0007 0.0001  137 ASP D N   
15398 C CA  . ASP D 145 ? 0.5667 0.2736 0.7390 0.0179  0.0023  -0.0107 137 ASP D CA  
15399 C C   . ASP D 145 ? 0.6009 0.3009 0.7684 0.0084  0.0021  -0.0061 137 ASP D C   
15400 O O   . ASP D 145 ? 0.5917 0.2827 0.7605 0.0086  0.0015  0.0051  137 ASP D O   
15401 C CB  . ASP D 145 ? 0.5927 0.2847 0.7727 0.0240  0.0051  -0.0145 137 ASP D CB  
15402 N N   . GLY D 146 ? 0.6850 0.3904 0.8466 -0.0001 0.0024  -0.0145 138 GLY D N   
15403 C CA  . GLY D 146 ? 0.7086 0.4099 0.8656 -0.0098 0.0023  -0.0116 138 GLY D CA  
15404 C C   . GLY D 146 ? 0.6556 0.3674 0.8081 -0.0129 -0.0004 -0.0009 138 GLY D C   
15405 O O   . GLY D 146 ? 0.7325 0.4445 0.8807 -0.0216 -0.0004 0.0001  138 GLY D O   
15406 N N   . LEU D 147 ? 0.5296 0.2506 0.6830 -0.0062 -0.0026 0.0068  139 LEU D N   
15407 C CA  . LEU D 147 ? 0.5242 0.2542 0.6737 -0.0084 -0.0052 0.0182  139 LEU D CA  
15408 C C   . LEU D 147 ? 0.4510 0.1987 0.5975 -0.0065 -0.0074 0.0158  139 LEU D C   
15409 O O   . LEU D 147 ? 0.4014 0.1557 0.5501 0.0004  -0.0093 0.0217  139 LEU D O   
15410 C CB  . LEU D 147 ? 0.5115 0.2349 0.6647 -0.0026 -0.0062 0.0320  139 LEU D CB  
15411 C CG  . LEU D 147 ? 0.5384 0.2431 0.6939 -0.0047 -0.0042 0.0366  139 LEU D CG  
15412 C CD1 . LEU D 147 ? 0.5336 0.2336 0.6926 0.0025  -0.0057 0.0503  139 LEU D CD1 
15413 C CD2 . LEU D 147 ? 0.5168 0.2191 0.6668 -0.0157 -0.0034 0.0383  139 LEU D CD2 
15414 N N   . ASN D 148 ? 0.4283 0.1840 0.5698 -0.0127 -0.0073 0.0074  140 ASN D N   
15415 C CA  . ASN D 148 ? 0.4173 0.1886 0.5553 -0.0114 -0.0092 0.0039  140 ASN D CA  
15416 C C   . ASN D 148 ? 0.4607 0.2413 0.5940 -0.0157 -0.0114 0.0126  140 ASN D C   
15417 O O   . ASN D 148 ? 0.4484 0.2353 0.5769 -0.0225 -0.0117 0.0092  140 ASN D O   
15418 C CB  . ASN D 148 ? 0.4772 0.2523 0.6121 -0.0151 -0.0081 -0.0098 140 ASN D CB  
15419 C CG  . ASN D 148 ? 0.5533 0.3210 0.6925 -0.0108 -0.0058 -0.0190 140 ASN D CG  
15420 O OD1 . ASN D 148 ? 0.4823 0.2484 0.6263 -0.0028 -0.0056 -0.0172 140 ASN D OD1 
15421 N ND2 . ASN D 148 ? 0.6814 0.4452 0.8189 -0.0160 -0.0041 -0.0290 140 ASN D ND2 
15422 N N   . ILE D 149 ? 0.4473 0.2296 0.5820 -0.0114 -0.0132 0.0241  141 ILE D N   
15423 C CA  . ILE D 149 ? 0.4056 0.1967 0.5358 -0.0152 -0.0152 0.0332  141 ILE D CA  
15424 C C   . ILE D 149 ? 0.4062 0.2120 0.5323 -0.0151 -0.0172 0.0301  141 ILE D C   
15425 O O   . ILE D 149 ? 0.3529 0.1667 0.4743 -0.0197 -0.0184 0.0349  141 ILE D O   
15426 C CB  . ILE D 149 ? 0.3833 0.1722 0.5157 -0.0110 -0.0167 0.0469  141 ILE D CB  
15427 C CG1 . ILE D 149 ? 0.3630 0.1555 0.4999 -0.0014 -0.0182 0.0477  141 ILE D CG1 
15428 C CG2 . ILE D 149 ? 0.3604 0.1339 0.4957 -0.0123 -0.0146 0.0509  141 ILE D CG2 
15429 C CD1 . ILE D 149 ? 0.3548 0.1519 0.4923 0.0025  -0.0210 0.0615  141 ILE D CD1 
15430 N N   . VAL D 150 ? 0.3607 0.1701 0.4882 -0.0102 -0.0173 0.0222  142 VAL D N   
15431 C CA  . VAL D 150 ? 0.3371 0.1586 0.4600 -0.0108 -0.0187 0.0173  142 VAL D CA  
15432 C C   . VAL D 150 ? 0.3394 0.1606 0.4605 -0.0134 -0.0170 0.0041  142 VAL D C   
15433 O O   . VAL D 150 ? 0.3343 0.1515 0.4584 -0.0095 -0.0156 -0.0032 142 VAL D O   
15434 C CB  . VAL D 150 ? 0.3228 0.1506 0.4480 -0.0034 -0.0204 0.0192  142 VAL D CB  
15435 C CG1 . VAL D 150 ? 0.2574 0.0965 0.3768 -0.0050 -0.0218 0.0147  142 VAL D CG1 
15436 C CG2 . VAL D 150 ? 0.3660 0.1945 0.4935 -0.0002 -0.0224 0.0325  142 VAL D CG2 
15437 N N   . ASP D 151 ? 0.3071 0.1334 0.4231 -0.0201 -0.0173 0.0011  143 ASP D N   
15438 C CA  . ASP D 151 ? 0.3154 0.1431 0.4291 -0.0233 -0.0163 -0.0108 143 ASP D CA  
15439 C C   . ASP D 151 ? 0.2620 0.0994 0.3702 -0.0292 -0.0177 -0.0114 143 ASP D C   
15440 O O   . ASP D 151 ? 0.2676 0.1037 0.3756 -0.0353 -0.0172 -0.0096 143 ASP D O   
15441 C CB  . ASP D 151 ? 0.3404 0.1570 0.4571 -0.0263 -0.0140 -0.0147 143 ASP D CB  
15442 C CG  . ASP D 151 ? 0.3594 0.1784 0.4733 -0.0302 -0.0132 -0.0267 143 ASP D CG  
15443 O OD1 . ASP D 151 ? 0.3625 0.1905 0.4726 -0.0287 -0.0142 -0.0327 143 ASP D OD1 
15444 O OD2 . ASP D 151 ? 0.4464 0.2585 0.5615 -0.0351 -0.0118 -0.0300 143 ASP D OD2 
15445 N N   . HIS D 152 ? 0.2481 0.0951 0.3522 -0.0274 -0.0193 -0.0139 144 HIS D N   
15446 C CA  . HIS D 152 ? 0.3031 0.1595 0.4025 -0.0323 -0.0207 -0.0152 144 HIS D CA  
15447 C C   . HIS D 152 ? 0.3292 0.1936 0.4238 -0.0298 -0.0219 -0.0218 144 HIS D C   
15448 O O   . HIS D 152 ? 0.2545 0.1184 0.3493 -0.0245 -0.0216 -0.0238 144 HIS D O   
15449 C CB  . HIS D 152 ? 0.2674 0.1274 0.3659 -0.0343 -0.0218 -0.0048 144 HIS D CB  
15450 C CG  . HIS D 152 ? 0.2681 0.1300 0.3663 -0.0292 -0.0231 0.0019  144 HIS D CG  
15451 N ND1 . HIS D 152 ? 0.2587 0.1148 0.3609 -0.0262 -0.0230 0.0103  144 HIS D ND1 
15452 C CD2 . HIS D 152 ? 0.2757 0.1451 0.3699 -0.0268 -0.0247 0.0017  144 HIS D CD2 
15453 C CE1 . HIS D 152 ? 0.2816 0.1424 0.3828 -0.0222 -0.0247 0.0149  144 HIS D CE1 
15454 N NE2 . HIS D 152 ? 0.2655 0.1353 0.3604 -0.0225 -0.0253 0.0095  144 HIS D NE2 
15455 N N   . TYR D 153 ? 0.2195 0.0918 0.3101 -0.0337 -0.0231 -0.0252 145 TYR D N   
15456 C CA  . TYR D 153 ? 0.2832 0.1629 0.3684 -0.0321 -0.0244 -0.0318 145 TYR D CA  
15457 C C   . TYR D 153 ? 0.2553 0.1435 0.3349 -0.0308 -0.0257 -0.0265 145 TYR D C   
15458 O O   . TYR D 153 ? 0.2389 0.1289 0.3186 -0.0324 -0.0258 -0.0187 145 TYR D O   
15459 C CB  . TYR D 153 ? 0.3327 0.2173 0.4161 -0.0365 -0.0249 -0.0396 145 TYR D CB  
15460 C CG  . TYR D 153 ? 0.3263 0.2055 0.4112 -0.0368 -0.0233 -0.0471 145 TYR D CG  
15461 C CD1 . TYR D 153 ? 0.4284 0.2985 0.5185 -0.0390 -0.0214 -0.0456 145 TYR D CD1 
15462 C CD2 . TYR D 153 ? 0.2873 0.1703 0.3679 -0.0350 -0.0234 -0.0555 145 TYR D CD2 
15463 C CE1 . TYR D 153 ? 0.5154 0.3799 0.6069 -0.0393 -0.0197 -0.0528 145 TYR D CE1 
15464 C CE2 . TYR D 153 ? 0.3632 0.2416 0.4449 -0.0354 -0.0217 -0.0627 145 TYR D CE2 
15465 C CZ  . TYR D 153 ? 0.5283 0.3973 0.6157 -0.0376 -0.0199 -0.0615 145 TYR D CZ  
15466 O OH  . TYR D 153 ? 0.6669 0.5306 0.7554 -0.0382 -0.0181 -0.0690 145 TYR D OH  
15467 N N   . THR D 154 ? 0.2136 0.1082 0.2864 -0.0277 -0.0260 -0.0305 146 THR D N   
15468 C CA  . THR D 154 ? 0.2132 0.1167 0.2783 -0.0262 -0.0265 -0.0266 146 THR D CA  
15469 C C   . THR D 154 ? 0.2104 0.1211 0.2697 -0.0271 -0.0275 -0.0325 146 THR D C   
15470 O O   . THR D 154 ? 0.2048 0.1158 0.2612 -0.0253 -0.0275 -0.0388 146 THR D O   
15471 C CB  . THR D 154 ? 0.2203 0.1243 0.2828 -0.0213 -0.0257 -0.0245 146 THR D CB  
15472 O OG1 . THR D 154 ? 0.2326 0.1302 0.3017 -0.0199 -0.0252 -0.0192 146 THR D OG1 
15473 C CG2 . THR D 154 ? 0.1719 0.0839 0.2268 -0.0207 -0.0258 -0.0201 146 THR D CG2 
15474 N N   . TYR D 155 ? 0.1760 0.0928 0.2335 -0.0297 -0.0283 -0.0304 147 TYR D N   
15475 C CA  . TYR D 155 ? 0.1836 0.1081 0.2363 -0.0301 -0.0297 -0.0347 147 TYR D CA  
15476 C C   . TYR D 155 ? 0.2259 0.1565 0.2713 -0.0274 -0.0296 -0.0309 147 TYR D C   
15477 O O   . TYR D 155 ? 0.2153 0.1465 0.2607 -0.0276 -0.0287 -0.0250 147 TYR D O   
15478 C CB  . TYR D 155 ? 0.2137 0.1417 0.2713 -0.0348 -0.0307 -0.0358 147 TYR D CB  
15479 C CG  . TYR D 155 ? 0.2246 0.1465 0.2895 -0.0387 -0.0308 -0.0404 147 TYR D CG  
15480 C CD1 . TYR D 155 ? 0.2235 0.1460 0.2880 -0.0395 -0.0318 -0.0488 147 TYR D CD1 
15481 C CD2 . TYR D 155 ? 0.2339 0.1493 0.3060 -0.0422 -0.0296 -0.0363 147 TYR D CD2 
15482 C CE1 . TYR D 155 ? 0.2351 0.1515 0.3066 -0.0437 -0.0315 -0.0540 147 TYR D CE1 
15483 C CE2 . TYR D 155 ? 0.2573 0.1657 0.3365 -0.0462 -0.0292 -0.0405 147 TYR D CE2 
15484 C CZ  . TYR D 155 ? 0.2503 0.1588 0.3293 -0.0470 -0.0301 -0.0498 147 TYR D CZ  
15485 O OH  . TYR D 155 ? 0.2232 0.1262 0.3060 -0.0504 -0.0285 -0.0533 147 TYR D OH  
15486 N N   . VAL D 156 ? 0.1777 0.1126 0.2165 -0.0252 -0.0304 -0.0344 148 VAL D N   
15487 C CA  . VAL D 156 ? 0.1720 0.1110 0.2036 -0.0225 -0.0300 -0.0313 148 VAL D CA  
15488 C C   . VAL D 156 ? 0.1865 0.1323 0.2144 -0.0218 -0.0319 -0.0338 148 VAL D C   
15489 O O   . VAL D 156 ? 0.2000 0.1477 0.2271 -0.0222 -0.0335 -0.0389 148 VAL D O   
15490 C CB  . VAL D 156 ? 0.2285 0.1645 0.2544 -0.0195 -0.0287 -0.0317 148 VAL D CB  
15491 C CG1 . VAL D 156 ? 0.2055 0.1439 0.2246 -0.0175 -0.0276 -0.0278 148 VAL D CG1 
15492 C CG2 . VAL D 156 ? 0.2008 0.1312 0.2318 -0.0194 -0.0274 -0.0303 148 VAL D CG2 
15493 N N   . PHE D 157 ? 0.1550 0.1050 0.1809 -0.0208 -0.0316 -0.0302 149 PHE D N   
15494 C CA  . PHE D 157 ? 0.1733 0.1292 0.1945 -0.0184 -0.0331 -0.0310 149 PHE D CA  
15495 C C   . PHE D 157 ? 0.1980 0.1508 0.2109 -0.0150 -0.0316 -0.0286 149 PHE D C   
15496 O O   . PHE D 157 ? 0.2247 0.1745 0.2368 -0.0149 -0.0293 -0.0251 149 PHE D O   
15497 C CB  . PHE D 157 ? 0.1529 0.1153 0.1780 -0.0188 -0.0336 -0.0291 149 PHE D CB  
15498 C CG  . PHE D 157 ? 0.1680 0.1356 0.2009 -0.0225 -0.0354 -0.0321 149 PHE D CG  
15499 C CD1 . PHE D 157 ? 0.2500 0.2146 0.2861 -0.0255 -0.0363 -0.0362 149 PHE D CD1 
15500 C CD2 . PHE D 157 ? 0.1904 0.1662 0.2280 -0.0232 -0.0360 -0.0312 149 PHE D CD2 
15501 C CE1 . PHE D 157 ? 0.2563 0.2250 0.2996 -0.0298 -0.0377 -0.0394 149 PHE D CE1 
15502 C CE2 . PHE D 157 ? 0.1780 0.1595 0.2232 -0.0274 -0.0375 -0.0341 149 PHE D CE2 
15503 C CZ  . PHE D 157 ? 0.2212 0.1988 0.2691 -0.0310 -0.0384 -0.0382 149 PHE D CZ  
15504 N N   . MET D 158 ? 0.2025 0.1564 0.2090 -0.0127 -0.0327 -0.0304 150 MET D N   
15505 C CA  . MET D 158 ? 0.2116 0.1621 0.2101 -0.0101 -0.0309 -0.0278 150 MET D CA  
15506 C C   . MET D 158 ? 0.1989 0.1529 0.1915 -0.0071 -0.0328 -0.0276 150 MET D C   
15507 O O   . MET D 158 ? 0.2007 0.1605 0.1945 -0.0072 -0.0357 -0.0302 150 MET D O   
15508 C CB  . MET D 158 ? 0.3012 0.2468 0.2968 -0.0107 -0.0291 -0.0291 150 MET D CB  
15509 C CG  . MET D 158 ? 0.3564 0.3032 0.3494 -0.0108 -0.0303 -0.0337 150 MET D CG  
15510 S SD  . MET D 158 ? 0.2860 0.2280 0.2785 -0.0115 -0.0275 -0.0355 150 MET D SD  
15511 C CE  . MET D 158 ? 0.2742 0.2138 0.2584 -0.0100 -0.0249 -0.0311 150 MET D CE  
15512 N N   . GLY D 159 ? 0.2064 0.1569 0.1925 -0.0046 -0.0310 -0.0241 151 GLY D N   
15513 C CA  . GLY D 159 ? 0.2292 0.1815 0.2095 -0.0011 -0.0325 -0.0222 151 GLY D CA  
15514 C C   . GLY D 159 ? 0.2001 0.1474 0.1706 -0.0002 -0.0310 -0.0210 151 GLY D C   
15515 O O   . GLY D 159 ? 0.2138 0.1574 0.1826 -0.0025 -0.0288 -0.0223 151 GLY D O   
15516 N N   . ASP D 160 ? 0.1796 0.1275 0.1441 0.0032  -0.0323 -0.0182 152 ASP D N   
15517 C CA  . ASP D 160 ? 0.2316 0.1752 0.1860 0.0039  -0.0311 -0.0162 152 ASP D CA  
15518 C C   . ASP D 160 ? 0.2489 0.1838 0.2003 0.0025  -0.0266 -0.0143 152 ASP D C   
15519 O O   . ASP D 160 ? 0.2317 0.1636 0.1773 0.0005  -0.0245 -0.0147 152 ASP D O   
15520 C CB  . ASP D 160 ? 0.3179 0.2627 0.2669 0.0083  -0.0333 -0.0119 152 ASP D CB  
15521 C CG  . ASP D 160 ? 0.4202 0.3756 0.3713 0.0095  -0.0382 -0.0138 152 ASP D CG  
15522 O OD1 . ASP D 160 ? 0.4127 0.3725 0.3621 0.0068  -0.0396 -0.0180 152 ASP D OD1 
15523 O OD2 . ASP D 160 ? 0.4568 0.4168 0.4116 0.0131  -0.0407 -0.0117 152 ASP D OD2 
15524 N N   . GLY D 161 ? 0.1829 0.1144 0.1380 0.0032  -0.0248 -0.0124 153 GLY D N   
15525 C CA  . GLY D 161 ? 0.1866 0.1107 0.1390 0.0013  -0.0206 -0.0111 153 GLY D CA  
15526 C C   . GLY D 161 ? 0.2119 0.1368 0.1669 -0.0028 -0.0191 -0.0141 153 GLY D C   
15527 O O   . GLY D 161 ? 0.2147 0.1359 0.1650 -0.0049 -0.0164 -0.0139 153 GLY D O   
15528 N N   . OCS D 162 ? 0.1710 0.1008 0.1338 -0.0039 -0.0208 -0.0165 154 OCS D N   
15529 C CA  . OCS D 162 ? 0.1666 0.0977 0.1332 -0.0067 -0.0201 -0.0191 154 OCS D CA  
15530 C CB  . OCS D 162 ? 0.1621 0.0975 0.1373 -0.0074 -0.0224 -0.0212 154 OCS D CB  
15531 S SG  . OCS D 162 ? 0.2687 0.2053 0.2500 -0.0076 -0.0223 -0.0190 154 OCS D SG  
15532 C C   . OCS D 162 ? 0.1940 0.1254 0.1558 -0.0074 -0.0197 -0.0212 154 OCS D C   
15533 O O   . OCS D 162 ? 0.2170 0.1474 0.1783 -0.0092 -0.0174 -0.0220 154 OCS D O   
15534 O OD1 . OCS D 162 ? 0.2774 0.2185 0.2657 -0.0082 -0.0248 -0.0208 154 OCS D OD1 
15535 O OD2 . OCS D 162 ? 0.2438 0.1785 0.2267 -0.0098 -0.0200 -0.0178 154 OCS D OD2 
15536 O OD3 . OCS D 162 ? 0.5720 0.5076 0.5500 -0.0051 -0.0220 -0.0169 154 OCS D OD3 
15537 N N   . LEU D 163 ? 0.1912 0.1254 0.1498 -0.0059 -0.0220 -0.0224 155 LEU D N   
15538 C CA  . LEU D 163 ? 0.1792 0.1153 0.1331 -0.0067 -0.0218 -0.0253 155 LEU D CA  
15539 C C   . LEU D 163 ? 0.1898 0.1223 0.1342 -0.0071 -0.0189 -0.0227 155 LEU D C   
15540 O O   . LEU D 163 ? 0.1874 0.1211 0.1288 -0.0088 -0.0171 -0.0251 155 LEU D O   
15541 C CB  . LEU D 163 ? 0.1831 0.1246 0.1357 -0.0055 -0.0254 -0.0274 155 LEU D CB  
15542 C CG  . LEU D 163 ? 0.1915 0.1370 0.1532 -0.0065 -0.0278 -0.0317 155 LEU D CG  
15543 C CD1 . LEU D 163 ? 0.2409 0.1928 0.2007 -0.0057 -0.0316 -0.0337 155 LEU D CD1 
15544 C CD2 . LEU D 163 ? 0.2074 0.1523 0.1730 -0.0085 -0.0260 -0.0364 155 LEU D CD2 
15545 N N   . MET D 164 ? 0.1918 0.1195 0.1318 -0.0057 -0.0183 -0.0181 156 MET D N   
15546 C CA  . MET D 164 ? 0.2023 0.1248 0.1335 -0.0068 -0.0151 -0.0151 156 MET D CA  
15547 C C   . MET D 164 ? 0.2120 0.1323 0.1453 -0.0101 -0.0113 -0.0160 156 MET D C   
15548 O O   . MET D 164 ? 0.1999 0.1188 0.1275 -0.0124 -0.0084 -0.0157 156 MET D O   
15549 C CB  . MET D 164 ? 0.2011 0.1177 0.1280 -0.0042 -0.0151 -0.0100 156 MET D CB  
15550 C CG  . MET D 164 ? 0.2833 0.2014 0.2032 -0.0012 -0.0177 -0.0073 156 MET D CG  
15551 S SD  . MET D 164 ? 0.2599 0.1700 0.1757 0.0031  -0.0178 -0.0006 156 MET D SD  
15552 C CE  . MET D 164 ? 0.2576 0.1745 0.1837 0.0070  -0.0220 -0.0018 156 MET D CE  
15553 N N   . GLU D 165 ? 0.1837 0.1046 0.1250 -0.0106 -0.0114 -0.0168 157 GLU D N   
15554 C CA  . GLU D 165 ? 0.2180 0.1384 0.1617 -0.0137 -0.0085 -0.0173 157 GLU D CA  
15555 C C   . GLU D 165 ? 0.2062 0.1318 0.1524 -0.0153 -0.0077 -0.0208 157 GLU D C   
15556 O O   . GLU D 165 ? 0.2021 0.1317 0.1531 -0.0140 -0.0098 -0.0237 157 GLU D O   
15557 C CB  . GLU D 165 ? 0.1993 0.1207 0.1509 -0.0137 -0.0094 -0.0172 157 GLU D CB  
15558 C CG  . GLU D 165 ? 0.1749 0.0915 0.1248 -0.0130 -0.0087 -0.0146 157 GLU D CG  
15559 C CD  . GLU D 165 ? 0.2091 0.1203 0.1536 -0.0157 -0.0048 -0.0134 157 GLU D CD  
15560 O OE1 . GLU D 165 ? 0.2049 0.1173 0.1474 -0.0187 -0.0028 -0.0143 157 GLU D OE1 
15561 O OE2 . GLU D 165 ? 0.2076 0.1136 0.1503 -0.0150 -0.0037 -0.0118 157 GLU D OE2 
15562 N N   . GLY D 166 ? 0.1797 0.1052 0.1235 -0.0182 -0.0044 -0.0207 158 GLY D N   
15563 C CA  . GLY D 166 ? 0.1782 0.1096 0.1251 -0.0193 -0.0031 -0.0241 158 GLY D CA  
15564 C C   . GLY D 166 ? 0.1849 0.1208 0.1425 -0.0183 -0.0048 -0.0261 158 GLY D C   
15565 O O   . GLY D 166 ? 0.1866 0.1267 0.1482 -0.0173 -0.0049 -0.0295 158 GLY D O   
15566 N N   . VAL D 167 ? 0.1690 0.1038 0.1311 -0.0183 -0.0060 -0.0240 159 VAL D N   
15567 C CA  . VAL D 167 ? 0.1678 0.1064 0.1397 -0.0173 -0.0077 -0.0247 159 VAL D CA  
15568 C C   . VAL D 167 ? 0.2422 0.1806 0.2182 -0.0147 -0.0103 -0.0270 159 VAL D C   
15569 O O   . VAL D 167 ? 0.1920 0.1327 0.1757 -0.0136 -0.0111 -0.0287 159 VAL D O   
15570 C CB  . VAL D 167 ? 0.1605 0.0986 0.1349 -0.0185 -0.0082 -0.0216 159 VAL D CB  
15571 C CG1 . VAL D 167 ? 0.1739 0.1079 0.1466 -0.0174 -0.0098 -0.0200 159 VAL D CG1 
15572 C CG2 . VAL D 167 ? 0.2089 0.1516 0.1927 -0.0179 -0.0096 -0.0211 159 VAL D CG2 
15573 N N   . SER D 168 ? 0.1630 0.0988 0.1344 -0.0138 -0.0117 -0.0272 160 SER D N   
15574 C CA  . SER D 168 ? 0.2183 0.1550 0.1934 -0.0122 -0.0141 -0.0303 160 SER D CA  
15575 C C   . SER D 168 ? 0.1852 0.1245 0.1593 -0.0119 -0.0129 -0.0349 160 SER D C   
15576 O O   . SER D 168 ? 0.2066 0.1469 0.1869 -0.0110 -0.0139 -0.0387 160 SER D O   
15577 C CB  . SER D 168 ? 0.2338 0.1692 0.2045 -0.0113 -0.0163 -0.0294 160 SER D CB  
15578 O OG  . SER D 168 ? 0.2735 0.2089 0.2350 -0.0111 -0.0156 -0.0296 160 SER D OG  
15579 N N   . HIS D 169 ? 0.1859 0.1261 0.1523 -0.0130 -0.0105 -0.0350 161 HIS D N   
15580 C CA  . HIS D 169 ? 0.2231 0.1670 0.1885 -0.0131 -0.0085 -0.0396 161 HIS D CA  
15581 C C   . HIS D 169 ? 0.2225 0.1692 0.1976 -0.0124 -0.0073 -0.0417 161 HIS D C   
15582 O O   . HIS D 169 ? 0.1741 0.1227 0.1540 -0.0111 -0.0071 -0.0466 161 HIS D O   
15583 C CB  . HIS D 169 ? 0.1806 0.1252 0.1361 -0.0151 -0.0056 -0.0381 161 HIS D CB  
15584 C CG  . HIS D 169 ? 0.1841 0.1340 0.1391 -0.0159 -0.0025 -0.0425 161 HIS D CG  
15585 N ND1 . HIS D 169 ? 0.1886 0.1417 0.1429 -0.0150 -0.0027 -0.0480 161 HIS D ND1 
15586 C CD2 . HIS D 169 ? 0.1842 0.1378 0.1396 -0.0176 0.0010  -0.0428 161 HIS D CD2 
15587 C CE1 . HIS D 169 ? 0.2589 0.2172 0.2132 -0.0159 0.0009  -0.0515 161 HIS D CE1 
15588 N NE2 . HIS D 169 ? 0.2125 0.1715 0.1676 -0.0175 0.0031  -0.0483 161 HIS D NE2 
15589 N N   . GLU D 170 ? 0.1678 0.1152 0.1459 -0.0132 -0.0064 -0.0382 162 GLU D N   
15590 C CA  . GLU D 170 ? 0.2243 0.1757 0.2117 -0.0121 -0.0055 -0.0394 162 GLU D CA  
15591 C C   . GLU D 170 ? 0.2343 0.1835 0.2313 -0.0096 -0.0080 -0.0403 162 GLU D C   
15592 O O   . GLU D 170 ? 0.1655 0.1163 0.1694 -0.0074 -0.0074 -0.0442 162 GLU D O   
15593 C CB  . GLU D 170 ? 0.1775 0.1312 0.1656 -0.0140 -0.0046 -0.0351 162 GLU D CB  
15594 C CG  . GLU D 170 ? 0.2003 0.1553 0.1795 -0.0172 -0.0016 -0.0345 162 GLU D CG  
15595 C CD  . GLU D 170 ? 0.2130 0.1707 0.1930 -0.0199 -0.0006 -0.0313 162 GLU D CD  
15596 O OE1 . GLU D 170 ? 0.2077 0.1684 0.1957 -0.0188 -0.0023 -0.0297 162 GLU D OE1 
15597 O OE2 . GLU D 170 ? 0.1915 0.1483 0.1641 -0.0234 0.0019  -0.0303 162 GLU D OE2 
15598 N N   . ALA D 171 ? 0.1608 0.1061 0.1586 -0.0099 -0.0106 -0.0369 163 ALA D N   
15599 C CA  . ALA D 171 ? 0.2167 0.1592 0.2235 -0.0083 -0.0128 -0.0367 163 ALA D CA  
15600 C C   . ALA D 171 ? 0.1994 0.1396 0.2078 -0.0073 -0.0134 -0.0424 163 ALA D C   
15601 O O   . ALA D 171 ? 0.1701 0.1086 0.1870 -0.0055 -0.0135 -0.0448 163 ALA D O   
15602 C CB  . ALA D 171 ? 0.1775 0.1174 0.1841 -0.0095 -0.0149 -0.0319 163 ALA D CB  
15603 N N   . CYS D 172 ? 0.1907 0.1308 0.1912 -0.0085 -0.0138 -0.0446 164 CYS D N   
15604 C CA  . CYS D 172 ? 0.1750 0.1142 0.1768 -0.0082 -0.0146 -0.0506 164 CYS D CA  
15605 C C   . CYS D 172 ? 0.2044 0.1462 0.2069 -0.0071 -0.0119 -0.0568 164 CYS D C   
15606 O O   . CYS D 172 ? 0.1930 0.1331 0.2008 -0.0064 -0.0119 -0.0625 164 CYS D O   
15607 C CB  . CYS D 172 ? 0.2491 0.1892 0.2422 -0.0097 -0.0164 -0.0509 164 CYS D CB  
15608 S SG  . CYS D 172 ? 0.2211 0.1589 0.2159 -0.0104 -0.0193 -0.0451 164 CYS D SG  
15609 N N   . SER D 173 ? 0.1859 0.1319 0.1834 -0.0073 -0.0093 -0.0562 165 SER D N   
15610 C CA  . SER D 173 ? 0.2003 0.1502 0.1998 -0.0062 -0.0062 -0.0620 165 SER D CA  
15611 C C   . SER D 173 ? 0.2041 0.1524 0.2167 -0.0032 -0.0058 -0.0632 165 SER D C   
15612 O O   . SER D 173 ? 0.1866 0.1340 0.2045 -0.0015 -0.0047 -0.0697 165 SER D O   
15613 C CB  . SER D 173 ? 0.1810 0.1363 0.1740 -0.0075 -0.0032 -0.0601 165 SER D CB  
15614 O OG  . SER D 173 ? 0.2307 0.1914 0.2260 -0.0065 0.0003  -0.0658 165 SER D OG  
15615 N N   . LEU D 174 ? 0.1972 0.1448 0.2150 -0.0024 -0.0069 -0.0569 166 LEU D N   
15616 C CA  . LEU D 174 ? 0.2104 0.1568 0.2406 0.0010  -0.0069 -0.0565 166 LEU D CA  
15617 C C   . LEU D 174 ? 0.1942 0.1328 0.2309 0.0018  -0.0088 -0.0581 166 LEU D C   
15618 O O   . LEU D 174 ? 0.2086 0.1445 0.2547 0.0049  -0.0078 -0.0618 166 LEU D O   
15619 C CB  . LEU D 174 ? 0.2006 0.1495 0.2335 0.0010  -0.0080 -0.0487 166 LEU D CB  
15620 C CG  . LEU D 174 ? 0.2701 0.2199 0.3154 0.0050  -0.0082 -0.0466 166 LEU D CG  
15621 C CD1 . LEU D 174 ? 0.2564 0.2118 0.3068 0.0081  -0.0050 -0.0523 166 LEU D CD1 
15622 C CD2 . LEU D 174 ? 0.2628 0.2168 0.3086 0.0042  -0.0097 -0.0389 166 LEU D CD2 
15623 N N   . ALA D 175 ? 0.1925 0.1273 0.2249 -0.0009 -0.0114 -0.0558 167 ALA D N   
15624 C CA  . ALA D 175 ? 0.1922 0.1202 0.2302 -0.0013 -0.0130 -0.0578 167 ALA D CA  
15625 C C   . ALA D 175 ? 0.2044 0.1311 0.2431 -0.0010 -0.0115 -0.0674 167 ALA D C   
15626 O O   . ALA D 175 ? 0.1959 0.1164 0.2431 0.0000  -0.0114 -0.0709 167 ALA D O   
15627 C CB  . ALA D 175 ? 0.2148 0.1416 0.2472 -0.0045 -0.0157 -0.0545 167 ALA D CB  
15628 N N   . GLY D 176 ? 0.2159 0.1482 0.2453 -0.0022 -0.0101 -0.0718 168 GLY D N   
15629 C CA  . GLY D 176 ? 0.1996 0.1324 0.2285 -0.0023 -0.0083 -0.0815 168 GLY D CA  
15630 C C   . GLY D 176 ? 0.2562 0.1885 0.2944 0.0015  -0.0050 -0.0860 168 GLY D C   
15631 O O   . GLY D 176 ? 0.2395 0.1669 0.2843 0.0024  -0.0040 -0.0930 168 GLY D O   
15632 N N   . THR D 177 ? 0.2181 0.1556 0.2574 0.0037  -0.0032 -0.0825 169 THR D N   
15633 C CA  A THR D 177 ? 0.2448 0.1837 0.2937 0.0080  -0.0000 -0.0867 169 THR D CA  
15634 C CA  B THR D 177 ? 0.2491 0.1880 0.2981 0.0081  -0.0000 -0.0866 169 THR D CA  
15635 C C   . THR D 177 ? 0.3157 0.2458 0.3781 0.0114  -0.0011 -0.0850 169 THR D C   
15636 O O   . THR D 177 ? 0.2613 0.1881 0.3326 0.0148  0.0013  -0.0914 169 THR D O   
15637 C CB  A THR D 177 ? 0.2353 0.1830 0.2834 0.0093  0.0016  -0.0823 169 THR D CB  
15638 C CB  B THR D 177 ? 0.2321 0.1795 0.2809 0.0095  0.0015  -0.0820 169 THR D CB  
15639 O OG1 A THR D 177 ? 0.2372 0.1917 0.2725 0.0058  0.0031  -0.0839 169 THR D OG1 
15640 O OG1 B THR D 177 ? 0.1991 0.1447 0.2523 0.0103  -0.0013 -0.0727 169 THR D OG1 
15641 C CG2 A THR D 177 ? 0.2246 0.1755 0.2839 0.0143  0.0048  -0.0865 169 THR D CG2 
15642 C CG2 B THR D 177 ? 0.2384 0.1924 0.2736 0.0056  0.0023  -0.0815 169 THR D CG2 
15643 N N   . LEU D 178 ? 0.2347 0.1605 0.2988 0.0106  -0.0044 -0.0765 170 LEU D N   
15644 C CA  . LEU D 178 ? 0.2653 0.1827 0.3412 0.0135  -0.0056 -0.0728 170 LEU D CA  
15645 C C   . LEU D 178 ? 0.2867 0.1939 0.3653 0.0112  -0.0066 -0.0767 170 LEU D C   
15646 O O   . LEU D 178 ? 0.3342 0.2325 0.4226 0.0131  -0.0073 -0.0740 170 LEU D O   
15647 C CB  . LEU D 178 ? 0.2160 0.1350 0.2920 0.0132  -0.0085 -0.0615 170 LEU D CB  
15648 C CG  . LEU D 178 ? 0.2611 0.1901 0.3377 0.0157  -0.0075 -0.0577 170 LEU D CG  
15649 C CD1 . LEU D 178 ? 0.2323 0.1634 0.3087 0.0149  -0.0104 -0.0472 170 LEU D CD1 
15650 C CD2 . LEU D 178 ? 0.3076 0.2376 0.3959 0.0217  -0.0052 -0.0611 170 LEU D CD2 
15651 N N   . GLY D 179 ? 0.2711 0.1795 0.3410 0.0070  -0.0068 -0.0829 171 GLY D N   
15652 C CA  . GLY D 179 ? 0.2474 0.1477 0.3197 0.0041  -0.0074 -0.0885 171 GLY D CA  
15653 C C   . GLY D 179 ? 0.2460 0.1394 0.3219 0.0017  -0.0104 -0.0812 171 GLY D C   
15654 O O   . GLY D 179 ? 0.2414 0.1271 0.3238 0.0016  -0.0099 -0.0808 171 GLY D O   
15655 N N   . LEU D 180 ? 0.2539 0.1525 0.3230 -0.0004 -0.0129 -0.0735 172 LEU D N   
15656 C CA  . LEU D 180 ? 0.2210 0.1150 0.2928 -0.0027 -0.0154 -0.0658 172 LEU D CA  
15657 C C   . LEU D 180 ? 0.2925 0.1844 0.3620 -0.0079 -0.0168 -0.0704 172 LEU D C   
15658 O O   . LEU D 180 ? 0.2188 0.1163 0.2809 -0.0110 -0.0189 -0.0681 172 LEU D O   
15659 C CB  . LEU D 180 ? 0.2279 0.1288 0.2936 -0.0030 -0.0169 -0.0569 172 LEU D CB  
15660 C CG  . LEU D 180 ? 0.2718 0.1768 0.3394 0.0013  -0.0159 -0.0524 172 LEU D CG  
15661 C CD1 . LEU D 180 ? 0.2102 0.1216 0.2710 -0.0002 -0.0173 -0.0447 172 LEU D CD1 
15662 C CD2 . LEU D 180 ? 0.2618 0.1599 0.3414 0.0049  -0.0156 -0.0488 172 LEU D CD2 
15663 N N   . GLY D 181 ? 0.2688 0.1549 0.3429 -0.0086 -0.0153 -0.0748 173 GLY D N   
15664 C CA  . GLY D 181 ? 0.2810 0.1676 0.3520 -0.0137 -0.0160 -0.0791 173 GLY D CA  
15665 C C   . GLY D 181 ? 0.2991 0.1841 0.3716 -0.0177 -0.0183 -0.0728 173 GLY D C   
15666 O O   . GLY D 181 ? 0.3306 0.2185 0.4000 -0.0223 -0.0196 -0.0761 173 GLY D O   
15667 N N   . LYS D 182 ? 0.2511 0.1324 0.3282 -0.0163 -0.0189 -0.0639 174 LYS D N   
15668 C CA  . LYS D 182 ? 0.2181 0.0989 0.2963 -0.0202 -0.0208 -0.0576 174 LYS D CA  
15669 C C   . LYS D 182 ? 0.2953 0.1837 0.3679 -0.0212 -0.0233 -0.0541 174 LYS D C   
15670 O O   . LYS D 182 ? 0.2594 0.1492 0.3325 -0.0243 -0.0246 -0.0488 174 LYS D O   
15671 C CB  . LYS D 182 ? 0.2226 0.0954 0.3082 -0.0188 -0.0201 -0.0493 174 LYS D CB  
15672 C CG  . LYS D 182 ? 0.3713 0.2350 0.4629 -0.0178 -0.0177 -0.0519 174 LYS D CG  
15673 C CD  . LYS D 182 ? 0.3984 0.2545 0.4957 -0.0190 -0.0176 -0.0432 174 LYS D CD  
15674 C CE  . LYS D 182 ? 0.4043 0.2499 0.5080 -0.0165 -0.0152 -0.0443 174 LYS D CE  
15675 N NZ  . LYS D 182 ? 0.3869 0.2247 0.4951 -0.0183 -0.0151 -0.0357 174 LYS D NZ  
15676 N N   . LEU D 183 ? 0.2586 0.1540 0.3237 -0.0183 -0.0231 -0.0558 175 LEU D N   
15677 C CA  . LEU D 183 ? 0.2449 0.1494 0.3013 -0.0186 -0.0244 -0.0519 175 LEU D CA  
15678 C C   . LEU D 183 ? 0.3071 0.2175 0.3579 -0.0213 -0.0259 -0.0580 175 LEU D C   
15679 O O   . LEU D 183 ? 0.2417 0.1535 0.2896 -0.0208 -0.0254 -0.0654 175 LEU D O   
15680 C CB  . LEU D 183 ? 0.2022 0.1107 0.2534 -0.0146 -0.0232 -0.0499 175 LEU D CB  
15681 C CG  . LEU D 183 ? 0.2158 0.1322 0.2572 -0.0147 -0.0240 -0.0470 175 LEU D CG  
15682 C CD1 . LEU D 183 ? 0.2521 0.1698 0.2937 -0.0162 -0.0251 -0.0394 175 LEU D CD1 
15683 C CD2 . LEU D 183 ? 0.1755 0.0953 0.2116 -0.0117 -0.0224 -0.0466 175 LEU D CD2 
15684 N N   . ILE D 184 ? 0.1878 0.1027 0.2370 -0.0240 -0.0278 -0.0550 176 ILE D N   
15685 C CA  . ILE D 184 ? 0.2221 0.1439 0.2673 -0.0265 -0.0298 -0.0601 176 ILE D CA  
15686 C C   . ILE D 184 ? 0.2880 0.2175 0.3267 -0.0255 -0.0312 -0.0548 176 ILE D C   
15687 O O   . ILE D 184 ? 0.2340 0.1641 0.2754 -0.0264 -0.0313 -0.0490 176 ILE D O   
15688 C CB  . ILE D 184 ? 0.2335 0.1532 0.2860 -0.0314 -0.0308 -0.0636 176 ILE D CB  
15689 C CG1 . ILE D 184 ? 0.2046 0.1155 0.2629 -0.0323 -0.0291 -0.0704 176 ILE D CG1 
15690 C CG2 . ILE D 184 ? 0.2459 0.1755 0.2946 -0.0341 -0.0335 -0.0679 176 ILE D CG2 
15691 C CD1 . ILE D 184 ? 0.2191 0.1272 0.2834 -0.0373 -0.0287 -0.0725 176 ILE D CD1 
15692 N N   . VAL D 185 ? 0.1999 0.1353 0.2301 -0.0236 -0.0319 -0.0568 177 VAL D N   
15693 C CA  . VAL D 185 ? 0.2266 0.1678 0.2503 -0.0217 -0.0328 -0.0519 177 VAL D CA  
15694 C C   . VAL D 185 ? 0.2180 0.1674 0.2393 -0.0230 -0.0358 -0.0548 177 VAL D C   
15695 O O   . VAL D 185 ? 0.2035 0.1558 0.2222 -0.0239 -0.0370 -0.0610 177 VAL D O   
15696 C CB  . VAL D 185 ? 0.2165 0.1575 0.2319 -0.0184 -0.0313 -0.0507 177 VAL D CB  
15697 C CG1 . VAL D 185 ? 0.2030 0.1485 0.2115 -0.0165 -0.0321 -0.0460 177 VAL D CG1 
15698 C CG2 . VAL D 185 ? 0.2180 0.1530 0.2366 -0.0171 -0.0287 -0.0478 177 VAL D CG2 
15699 N N   . LEU D 186 ? 0.2095 0.1635 0.2318 -0.0230 -0.0370 -0.0505 178 LEU D N   
15700 C CA  . LEU D 186 ? 0.1870 0.1505 0.2068 -0.0227 -0.0401 -0.0517 178 LEU D CA  
15701 C C   . LEU D 186 ? 0.1701 0.1355 0.1821 -0.0183 -0.0399 -0.0466 178 LEU D C   
15702 O O   . LEU D 186 ? 0.1811 0.1441 0.1938 -0.0169 -0.0383 -0.0413 178 LEU D O   
15703 C CB  . LEU D 186 ? 0.1999 0.1686 0.2278 -0.0257 -0.0415 -0.0513 178 LEU D CB  
15704 C CG  . LEU D 186 ? 0.2207 0.1893 0.2557 -0.0310 -0.0423 -0.0576 178 LEU D CG  
15705 C CD1 . LEU D 186 ? 0.2207 0.1782 0.2614 -0.0330 -0.0394 -0.0570 178 LEU D CD1 
15706 C CD2 . LEU D 186 ? 0.1972 0.1753 0.2385 -0.0342 -0.0446 -0.0583 178 LEU D CD2 
15707 N N   . TYR D 187 ? 0.2196 0.1886 0.2237 -0.0164 -0.0414 -0.0482 179 TYR D N   
15708 C CA  . TYR D 187 ? 0.2200 0.1891 0.2157 -0.0123 -0.0410 -0.0434 179 TYR D CA  
15709 C C   . TYR D 187 ? 0.2445 0.2223 0.2402 -0.0102 -0.0442 -0.0413 179 TYR D C   
15710 O O   . TYR D 187 ? 0.2488 0.2349 0.2451 -0.0113 -0.0476 -0.0450 179 TYR D O   
15711 C CB  . TYR D 187 ? 0.2607 0.2285 0.2475 -0.0115 -0.0405 -0.0457 179 TYR D CB  
15712 C CG  . TYR D 187 ? 0.2058 0.1753 0.1827 -0.0080 -0.0410 -0.0416 179 TYR D CG  
15713 C CD1 . TYR D 187 ? 0.2371 0.2031 0.2122 -0.0051 -0.0397 -0.0353 179 TYR D CD1 
15714 C CD2 . TYR D 187 ? 0.2216 0.1955 0.1905 -0.0079 -0.0426 -0.0440 179 TYR D CD2 
15715 C CE1 . TYR D 187 ? 0.2416 0.2073 0.2077 -0.0018 -0.0400 -0.0311 179 TYR D CE1 
15716 C CE2 . TYR D 187 ? 0.2448 0.2194 0.2040 -0.0048 -0.0431 -0.0393 179 TYR D CE2 
15717 C CZ  . TYR D 187 ? 0.2894 0.2592 0.2475 -0.0016 -0.0417 -0.0326 179 TYR D CZ  
15718 O OH  . TYR D 187 ? 0.2466 0.2156 0.1953 0.0015  -0.0420 -0.0275 179 TYR D OH  
15719 N N   . ASP D 188 ? 0.1786 0.1551 0.1743 -0.0072 -0.0432 -0.0359 180 ASP D N   
15720 C CA  . ASP D 188 ? 0.1725 0.1567 0.1690 -0.0039 -0.0457 -0.0332 180 ASP D CA  
15721 C C   . ASP D 188 ? 0.2187 0.2031 0.2049 0.0001  -0.0469 -0.0306 180 ASP D C   
15722 O O   . ASP D 188 ? 0.2759 0.2538 0.2568 0.0032  -0.0446 -0.0260 180 ASP D O   
15723 C CB  . ASP D 188 ? 0.2022 0.1841 0.2032 -0.0024 -0.0433 -0.0292 180 ASP D CB  
15724 C CG  . ASP D 188 ? 0.2592 0.2494 0.2625 0.0017  -0.0455 -0.0267 180 ASP D CG  
15725 O OD1 . ASP D 188 ? 0.3119 0.3117 0.3163 0.0023  -0.0495 -0.0285 180 ASP D OD1 
15726 O OD2 . ASP D 188 ? 0.2587 0.2461 0.2631 0.0045  -0.0431 -0.0232 180 ASP D OD2 
15727 N N   . ASP D 189 ? 0.2163 0.2084 0.1994 -0.0004 -0.0505 -0.0336 181 ASP D N   
15728 C CA  . ASP D 189 ? 0.2435 0.2366 0.2157 0.0026  -0.0519 -0.0311 181 ASP D CA  
15729 C C   . ASP D 189 ? 0.2319 0.2333 0.2047 0.0074  -0.0555 -0.0268 181 ASP D C   
15730 O O   . ASP D 189 ? 0.2483 0.2615 0.2223 0.0073  -0.0600 -0.0290 181 ASP D O   
15731 C CB  . ASP D 189 ? 0.2467 0.2445 0.2145 -0.0008 -0.0537 -0.0369 181 ASP D CB  
15732 C CG  . ASP D 189 ? 0.3380 0.3371 0.2932 0.0016  -0.0548 -0.0342 181 ASP D CG  
15733 O OD1 . ASP D 189 ? 0.3381 0.3344 0.2883 0.0061  -0.0547 -0.0272 181 ASP D OD1 
15734 O OD2 . ASP D 189 ? 0.3562 0.3587 0.3063 -0.0013 -0.0554 -0.0391 181 ASP D OD2 
15735 N N   . ASN D 190 ? 0.2437 0.2394 0.2163 0.0118  -0.0536 -0.0210 182 ASN D N   
15736 C CA  . ASN D 190 ? 0.2333 0.2365 0.2086 0.0173  -0.0566 -0.0170 182 ASN D CA  
15737 C C   . ASN D 190 ? 0.3780 0.3773 0.3431 0.0227  -0.0573 -0.0104 182 ASN D C   
15738 O O   . ASN D 190 ? 0.4847 0.4837 0.4515 0.0285  -0.0576 -0.0054 182 ASN D O   
15739 C CB  . ASN D 190 ? 0.2818 0.2831 0.2665 0.0188  -0.0541 -0.0157 182 ASN D CB  
15740 C CG  . ASN D 190 ? 0.4307 0.4178 0.4120 0.0193  -0.0487 -0.0129 182 ASN D CG  
15741 O OD1 . ASN D 190 ? 0.4053 0.3837 0.3772 0.0198  -0.0470 -0.0105 182 ASN D OD1 
15742 N ND2 . ASN D 190 ? 0.4251 0.4104 0.4139 0.0188  -0.0459 -0.0132 182 ASN D ND2 
15743 N N   . ASP D 199 ? 0.7445 0.6796 0.6318 0.0310  -0.0428 0.0281  191 ASP D N   
15744 C CA  . ASP D 199 ? 0.7113 0.6494 0.5857 0.0285  -0.0435 0.0303  191 ASP D CA  
15745 C C   . ASP D 199 ? 0.5911 0.5144 0.4555 0.0276  -0.0386 0.0369  191 ASP D C   
15746 O O   . ASP D 199 ? 0.5869 0.5104 0.4403 0.0238  -0.0372 0.0382  191 ASP D O   
15747 C CB  . ASP D 199 ? 0.8057 0.7559 0.6763 0.0331  -0.0503 0.0345  191 ASP D CB  
15748 N N   . GLY D 200 ? 0.4952 0.4057 0.3633 0.0307  -0.0357 0.0408  192 GLY D N   
15749 C CA  . GLY D 200 ? 0.4392 0.3340 0.2991 0.0289  -0.0303 0.0462  192 GLY D CA  
15750 C C   . GLY D 200 ? 0.4153 0.3044 0.2763 0.0216  -0.0244 0.0403  192 GLY D C   
15751 O O   . GLY D 200 ? 0.4675 0.3462 0.3206 0.0181  -0.0197 0.0436  192 GLY D O   
15752 N N   . TRP D 201 ? 0.3664 0.2625 0.2373 0.0190  -0.0245 0.0318  193 TRP D N   
15753 C CA  . TRP D 201 ? 0.3943 0.2869 0.2674 0.0126  -0.0195 0.0263  193 TRP D CA  
15754 C C   . TRP D 201 ? 0.3245 0.2291 0.2034 0.0092  -0.0209 0.0179  193 TRP D C   
15755 O O   . TRP D 201 ? 0.4047 0.3079 0.2859 0.0043  -0.0172 0.0135  193 TRP D O   
15756 C CB  . TRP D 201 ? 0.3484 0.2313 0.2290 0.0130  -0.0161 0.0254  193 TRP D CB  
15757 C CG  . TRP D 201 ? 0.4006 0.2891 0.2922 0.0173  -0.0195 0.0230  193 TRP D CG  
15758 C CD1 . TRP D 201 ? 0.3501 0.2468 0.2513 0.0155  -0.0205 0.0163  193 TRP D CD1 
15759 C CD2 . TRP D 201 ? 0.4161 0.3029 0.3104 0.0244  -0.0220 0.0276  193 TRP D CD2 
15760 N NE1 . TRP D 201 ? 0.4395 0.3400 0.3488 0.0203  -0.0234 0.0163  193 TRP D NE1 
15761 C CE2 . TRP D 201 ? 0.4440 0.3392 0.3497 0.0260  -0.0244 0.0228  193 TRP D CE2 
15762 C CE3 . TRP D 201 ? 0.4649 0.3438 0.3535 0.0296  -0.0224 0.0355  193 TRP D CE3 
15763 C CZ2 . TRP D 201 ? 0.4761 0.3734 0.3881 0.0326  -0.0269 0.0251  193 TRP D CZ2 
15764 C CZ3 . TRP D 201 ? 0.4686 0.3489 0.3637 0.0369  -0.0253 0.0380  193 TRP D CZ3 
15765 C CH2 . TRP D 201 ? 0.4695 0.3596 0.3764 0.0383  -0.0274 0.0326  193 TRP D CH2 
15766 N N   . PHE D 202 ? 0.2873 0.2035 0.1692 0.0114  -0.0261 0.0156  194 PHE D N   
15767 C CA  . PHE D 202 ? 0.3008 0.2267 0.1894 0.0083  -0.0273 0.0073  194 PHE D CA  
15768 C C   . PHE D 202 ? 0.3120 0.2495 0.1964 0.0090  -0.0320 0.0059  194 PHE D C   
15769 O O   . PHE D 202 ? 0.2626 0.2059 0.1493 0.0132  -0.0367 0.0079  194 PHE D O   
15770 C CB  . PHE D 202 ? 0.2934 0.2205 0.1948 0.0095  -0.0282 0.0038  194 PHE D CB  
15771 C CG  . PHE D 202 ? 0.2373 0.1718 0.1461 0.0062  -0.0290 -0.0039 194 PHE D CG  
15772 C CD1 . PHE D 202 ? 0.2589 0.1923 0.1673 0.0017  -0.0255 -0.0080 194 PHE D CD1 
15773 C CD2 . PHE D 202 ? 0.3462 0.2889 0.2633 0.0076  -0.0330 -0.0071 194 PHE D CD2 
15774 C CE1 . PHE D 202 ? 0.3415 0.2804 0.2575 -0.0006 -0.0260 -0.0148 194 PHE D CE1 
15775 C CE2 . PHE D 202 ? 0.3458 0.2936 0.2699 0.0044  -0.0334 -0.0140 194 PHE D CE2 
15776 C CZ  . PHE D 202 ? 0.3717 0.3170 0.2954 0.0006  -0.0299 -0.0176 194 PHE D CZ  
15777 N N   . THR D 203 ? 0.2871 0.2291 0.1657 0.0049  -0.0306 0.0021  195 THR D N   
15778 C CA  . THR D 203 ? 0.2619 0.2156 0.1351 0.0045  -0.0345 -0.0003 195 THR D CA  
15779 C C   . THR D 203 ? 0.2701 0.2301 0.1462 -0.0001 -0.0331 -0.0099 195 THR D C   
15780 O O   . THR D 203 ? 0.2628 0.2310 0.1318 -0.0020 -0.0342 -0.0128 195 THR D O   
15781 C CB  . THR D 203 ? 0.3276 0.2805 0.1860 0.0048  -0.0342 0.0065  195 THR D CB  
15782 O OG1 . THR D 203 ? 0.3297 0.2743 0.1828 0.0010  -0.0282 0.0074  195 THR D OG1 
15783 C CG2 . THR D 203 ? 0.3335 0.2814 0.1893 0.0106  -0.0369 0.0162  195 THR D CG2 
15784 N N   . GLU D 204 ? 0.2446 0.2010 0.1310 -0.0019 -0.0304 -0.0147 196 GLU D N   
15785 C CA  . GLU D 204 ? 0.2636 0.2245 0.1538 -0.0055 -0.0288 -0.0234 196 GLU D CA  
15786 C C   . GLU D 204 ? 0.2919 0.2629 0.1858 -0.0056 -0.0333 -0.0294 196 GLU D C   
15787 O O   . GLU D 204 ? 0.2734 0.2469 0.1731 -0.0033 -0.0373 -0.0283 196 GLU D O   
15788 C CB  . GLU D 204 ? 0.2799 0.2349 0.1812 -0.0065 -0.0258 -0.0260 196 GLU D CB  
15789 C CG  . GLU D 204 ? 0.3111 0.2577 0.2094 -0.0075 -0.0211 -0.0217 196 GLU D CG  
15790 C CD  . GLU D 204 ? 0.2985 0.2412 0.2073 -0.0087 -0.0186 -0.0242 196 GLU D CD  
15791 O OE1 . GLU D 204 ? 0.2385 0.1848 0.1562 -0.0090 -0.0199 -0.0297 196 GLU D OE1 
15792 O OE2 . GLU D 204 ? 0.2819 0.2180 0.1899 -0.0095 -0.0154 -0.0205 196 GLU D OE2 
15793 N N   . ASN D 205 ? 0.2436 0.2209 0.1342 -0.0086 -0.0325 -0.0363 197 ASN D N   
15794 C CA  . ASN D 205 ? 0.2434 0.2293 0.1385 -0.0101 -0.0357 -0.0443 197 ASN D CA  
15795 C C   . ASN D 205 ? 0.2331 0.2144 0.1414 -0.0114 -0.0335 -0.0502 197 ASN D C   
15796 O O   . ASN D 205 ? 0.2591 0.2389 0.1691 -0.0134 -0.0297 -0.0556 197 ASN D O   
15797 C CB  . ASN D 205 ? 0.2538 0.2480 0.1389 -0.0129 -0.0353 -0.0496 197 ASN D CB  
15798 C CG  . ASN D 205 ? 0.2866 0.2897 0.1759 -0.0152 -0.0383 -0.0592 197 ASN D CG  
15799 O OD1 . ASN D 205 ? 0.2518 0.2532 0.1531 -0.0155 -0.0393 -0.0634 197 ASN D OD1 
15800 N ND2 . ASN D 205 ? 0.2838 0.2964 0.1629 -0.0174 -0.0393 -0.0630 197 ASN D ND2 
15801 N N   . ILE D 206 ? 0.2254 0.2043 0.1434 -0.0099 -0.0358 -0.0486 198 ILE D N   
15802 C CA  . ILE D 206 ? 0.2162 0.1894 0.1462 -0.0107 -0.0336 -0.0518 198 ILE D CA  
15803 C C   . ILE D 206 ? 0.2174 0.1936 0.1530 -0.0135 -0.0334 -0.0615 198 ILE D C   
15804 O O   . ILE D 206 ? 0.2142 0.1856 0.1554 -0.0143 -0.0298 -0.0647 198 ILE D O   
15805 C CB  . ILE D 206 ? 0.2089 0.1797 0.1470 -0.0089 -0.0359 -0.0474 198 ILE D CB  
15806 C CG1 . ILE D 206 ? 0.2075 0.1723 0.1417 -0.0062 -0.0344 -0.0389 198 ILE D CG1 
15807 C CG2 . ILE D 206 ? 0.2300 0.1967 0.1805 -0.0104 -0.0346 -0.0511 198 ILE D CG2 
15808 C CD1 . ILE D 206 ? 0.2132 0.1707 0.1467 -0.0071 -0.0294 -0.0376 198 ILE D CD1 
15809 N N   . PRO D 207 ? 0.2498 0.2338 0.1846 -0.0151 -0.0368 -0.0667 199 PRO D N   
15810 C CA  . PRO D 207 ? 0.2450 0.2308 0.1841 -0.0182 -0.0357 -0.0770 199 PRO D CA  
15811 C C   . PRO D 207 ? 0.2985 0.2835 0.2324 -0.0190 -0.0311 -0.0810 199 PRO D C   
15812 O O   . PRO D 207 ? 0.2666 0.2471 0.2081 -0.0196 -0.0279 -0.0867 199 PRO D O   
15813 C CB  . PRO D 207 ? 0.2334 0.2298 0.1683 -0.0201 -0.0403 -0.0810 199 PRO D CB  
15814 C CG  . PRO D 207 ? 0.2351 0.2336 0.1714 -0.0178 -0.0443 -0.0734 199 PRO D CG  
15815 C CD  . PRO D 207 ? 0.2254 0.2171 0.1575 -0.0143 -0.0420 -0.0639 199 PRO D CD  
15816 N N   . GLN D 208 ? 0.2682 0.2576 0.1894 -0.0187 -0.0306 -0.0779 200 GLN D N   
15817 C CA  . GLN D 208 ? 0.2850 0.2751 0.2007 -0.0198 -0.0259 -0.0817 200 GLN D CA  
15818 C C   . GLN D 208 ? 0.2626 0.2445 0.1846 -0.0184 -0.0215 -0.0788 200 GLN D C   
15819 O O   . GLN D 208 ? 0.2353 0.2164 0.1615 -0.0189 -0.0175 -0.0849 200 GLN D O   
15820 C CB  . GLN D 208 ? 0.2778 0.2740 0.1780 -0.0202 -0.0261 -0.0774 200 GLN D CB  
15821 C CG  . GLN D 208 ? 0.3035 0.3033 0.1970 -0.0223 -0.0213 -0.0828 200 GLN D CG  
15822 C CD  . GLN D 208 ? 0.3478 0.3546 0.2249 -0.0234 -0.0218 -0.0786 200 GLN D CD  
15823 O OE1 . GLN D 208 ? 0.3640 0.3683 0.2350 -0.0217 -0.0235 -0.0684 200 GLN D OE1 
15824 N NE2 . GLN D 208 ? 0.3729 0.3882 0.2428 -0.0263 -0.0200 -0.0863 200 GLN D NE2 
15825 N N   . ARG D 209 ? 0.2281 0.2045 0.1511 -0.0164 -0.0221 -0.0699 201 ARG D N   
15826 C CA  . ARG D 209 ? 0.2282 0.1980 0.1570 -0.0155 -0.0184 -0.0670 201 ARG D CA  
15827 C C   . ARG D 209 ? 0.2198 0.1861 0.1624 -0.0151 -0.0177 -0.0720 201 ARG D C   
15828 O O   . ARG D 209 ? 0.2144 0.1790 0.1618 -0.0148 -0.0140 -0.0746 201 ARG D O   
15829 C CB  . ARG D 209 ? 0.2160 0.1807 0.1437 -0.0139 -0.0195 -0.0574 201 ARG D CB  
15830 C CG  . ARG D 209 ? 0.2081 0.1668 0.1431 -0.0133 -0.0165 -0.0546 201 ARG D CG  
15831 C CD  . ARG D 209 ? 0.2555 0.2092 0.1895 -0.0121 -0.0177 -0.0464 201 ARG D CD  
15832 N NE  . ARG D 209 ? 0.2536 0.2027 0.1956 -0.0120 -0.0157 -0.0444 201 ARG D NE  
15833 C CZ  . ARG D 209 ? 0.2392 0.1841 0.1837 -0.0111 -0.0166 -0.0392 201 ARG D CZ  
15834 N NH1 . ARG D 209 ? 0.2207 0.1648 0.1611 -0.0097 -0.0192 -0.0354 201 ARG D NH1 
15835 N NH2 . ARG D 209 ? 0.2842 0.2263 0.2354 -0.0115 -0.0149 -0.0379 201 ARG D NH2 
15836 N N   . PHE D 210 ? 0.2129 0.1781 0.1623 -0.0152 -0.0212 -0.0734 202 PHE D N   
15837 C CA  . PHE D 210 ? 0.2356 0.1958 0.1979 -0.0149 -0.0204 -0.0769 202 PHE D CA  
15838 C C   . PHE D 210 ? 0.2220 0.1837 0.1877 -0.0160 -0.0185 -0.0870 202 PHE D C   
15839 O O   . PHE D 210 ? 0.2646 0.2215 0.2401 -0.0150 -0.0162 -0.0898 202 PHE D O   
15840 C CB  . PHE D 210 ? 0.2182 0.1762 0.1871 -0.0151 -0.0241 -0.0741 202 PHE D CB  
15841 C CG  . PHE D 210 ? 0.2174 0.1710 0.1886 -0.0135 -0.0241 -0.0655 202 PHE D CG  
15842 C CD1 . PHE D 210 ? 0.2609 0.2157 0.2236 -0.0125 -0.0247 -0.0590 202 PHE D CD1 
15843 C CD2 . PHE D 210 ? 0.2111 0.1593 0.1926 -0.0131 -0.0234 -0.0638 202 PHE D CD2 
15844 C CE1 . PHE D 210 ? 0.2256 0.1763 0.1902 -0.0114 -0.0242 -0.0521 202 PHE D CE1 
15845 C CE2 . PHE D 210 ? 0.2354 0.1807 0.2183 -0.0121 -0.0232 -0.0564 202 PHE D CE2 
15846 C CZ  . PHE D 210 ? 0.2301 0.1767 0.2046 -0.0114 -0.0235 -0.0511 202 PHE D CZ  
15847 N N   . GLU D 211 ? 0.2238 0.1921 0.1816 -0.0180 -0.0193 -0.0927 203 GLU D N   
15848 C CA  . GLU D 211 ? 0.2314 0.2015 0.1911 -0.0191 -0.0164 -0.1032 203 GLU D CA  
15849 C C   . GLU D 211 ? 0.2313 0.2012 0.1906 -0.0174 -0.0114 -0.1035 203 GLU D C   
15850 O O   . GLU D 211 ? 0.2541 0.2215 0.2219 -0.0164 -0.0082 -0.1099 203 GLU D O   
15851 C CB  . GLU D 211 ? 0.3102 0.2893 0.2594 -0.0219 -0.0181 -0.1090 203 GLU D CB  
15852 C CG  . GLU D 211 ? 0.3491 0.3303 0.3001 -0.0240 -0.0230 -0.1108 203 GLU D CG  
15853 C CD  . GLU D 211 ? 0.4811 0.4721 0.4235 -0.0274 -0.0243 -0.1192 203 GLU D CD  
15854 O OE1 . GLU D 211 ? 0.5027 0.4965 0.4414 -0.0283 -0.0205 -0.1266 203 GLU D OE1 
15855 O OE2 . GLU D 211 ? 0.5595 0.5565 0.4989 -0.0291 -0.0291 -0.1184 203 GLU D OE2 
15856 N N   . SER D 212 ? 0.2295 0.2021 0.1798 -0.0171 -0.0104 -0.0966 204 SER D N   
15857 C CA  . SER D 212 ? 0.2294 0.2033 0.1792 -0.0162 -0.0055 -0.0966 204 SER D CA  
15858 C C   . SER D 212 ? 0.2619 0.2298 0.2250 -0.0136 -0.0040 -0.0947 204 SER D C   
15859 O O   . SER D 212 ? 0.2615 0.2313 0.2284 -0.0124 0.0002  -0.0976 204 SER D O   
15860 C CB  . SER D 212 ? 0.2551 0.2315 0.1931 -0.0171 -0.0049 -0.0885 204 SER D CB  
15861 O OG  . SER D 212 ? 0.2363 0.2070 0.1777 -0.0158 -0.0059 -0.0797 204 SER D OG  
15862 N N   . TYR D 213 ? 0.2518 0.2135 0.2217 -0.0127 -0.0072 -0.0897 205 TYR D N   
15863 C CA  . TYR D 213 ? 0.2749 0.2312 0.2572 -0.0103 -0.0064 -0.0873 205 TYR D CA  
15864 C C   . TYR D 213 ? 0.2383 0.1906 0.2318 -0.0091 -0.0060 -0.0946 205 TYR D C   
15865 O O   . TYR D 213 ? 0.2602 0.2080 0.2645 -0.0066 -0.0052 -0.0927 205 TYR D O   
15866 C CB  . TYR D 213 ? 0.2177 0.1694 0.2019 -0.0102 -0.0099 -0.0789 205 TYR D CB  
15867 C CG  . TYR D 213 ? 0.2352 0.1883 0.2109 -0.0108 -0.0100 -0.0710 205 TYR D CG  
15868 C CD1 . TYR D 213 ? 0.2070 0.1637 0.1768 -0.0112 -0.0067 -0.0699 205 TYR D CD1 
15869 C CD2 . TYR D 213 ? 0.1925 0.1430 0.1664 -0.0112 -0.0132 -0.0650 205 TYR D CD2 
15870 C CE1 . TYR D 213 ? 0.2348 0.1911 0.1970 -0.0122 -0.0065 -0.0629 205 TYR D CE1 
15871 C CE2 . TYR D 213 ? 0.1987 0.1489 0.1655 -0.0115 -0.0131 -0.0582 205 TYR D CE2 
15872 C CZ  . TYR D 213 ? 0.2009 0.1534 0.1618 -0.0122 -0.0098 -0.0572 205 TYR D CZ  
15873 O OH  . TYR D 213 ? 0.1911 0.1418 0.1450 -0.0129 -0.0094 -0.0507 205 TYR D OH  
15874 N N   . GLY D 214 ? 0.2470 0.2005 0.2385 -0.0109 -0.0066 -0.1024 206 GLY D N   
15875 C CA  . GLY D 214 ? 0.3002 0.2479 0.3024 -0.0104 -0.0062 -0.1095 206 GLY D CA  
15876 C C   . GLY D 214 ? 0.2574 0.1990 0.2651 -0.0118 -0.0101 -0.1065 206 GLY D C   
15877 O O   . GLY D 214 ? 0.2615 0.1958 0.2801 -0.0112 -0.0097 -0.1096 206 GLY D O   
15878 N N   . TRP D 215 ? 0.2359 0.1802 0.2367 -0.0137 -0.0136 -0.1005 207 TRP D N   
15879 C CA  . TRP D 215 ? 0.2299 0.1703 0.2357 -0.0154 -0.0172 -0.0979 207 TRP D CA  
15880 C C   . TRP D 215 ? 0.3062 0.2495 0.3099 -0.0190 -0.0190 -0.1060 207 TRP D C   
15881 O O   . TRP D 215 ? 0.2526 0.2031 0.2473 -0.0203 -0.0188 -0.1113 207 TRP D O   
15882 C CB  . TRP D 215 ? 0.2263 0.1692 0.2266 -0.0154 -0.0199 -0.0883 207 TRP D CB  
15883 C CG  . TRP D 215 ? 0.2596 0.1986 0.2639 -0.0130 -0.0189 -0.0801 207 TRP D CG  
15884 C CD1 . TRP D 215 ? 0.1974 0.1362 0.2028 -0.0106 -0.0158 -0.0786 207 TRP D CD1 
15885 C CD2 . TRP D 215 ? 0.2003 0.1368 0.2078 -0.0132 -0.0210 -0.0725 207 TRP D CD2 
15886 N NE1 . TRP D 215 ? 0.1900 0.1262 0.1988 -0.0095 -0.0162 -0.0705 207 TRP D NE1 
15887 C CE2 . TRP D 215 ? 0.1870 0.1216 0.1967 -0.0110 -0.0192 -0.0668 207 TRP D CE2 
15888 C CE3 . TRP D 215 ? 0.1989 0.1356 0.2077 -0.0151 -0.0241 -0.0704 207 TRP D CE3 
15889 C CZ2 . TRP D 215 ? 0.1805 0.1131 0.1930 -0.0109 -0.0204 -0.0593 207 TRP D CZ2 
15890 C CZ3 . TRP D 215 ? 0.2027 0.1373 0.2147 -0.0148 -0.0249 -0.0629 207 TRP D CZ3 
15891 C CH2 . TRP D 215 ? 0.1792 0.1116 0.1926 -0.0128 -0.0231 -0.0575 207 TRP D CH2 
15892 N N   . HIS D 216 ? 0.2243 0.1626 0.2364 -0.0211 -0.0209 -0.1070 208 HIS D N   
15893 C CA  . HIS D 216 ? 0.2678 0.2104 0.2779 -0.0253 -0.0236 -0.1124 208 HIS D CA  
15894 C C   . HIS D 216 ? 0.2239 0.1738 0.2273 -0.0260 -0.0277 -0.1058 208 HIS D C   
15895 O O   . HIS D 216 ? 0.2628 0.2103 0.2682 -0.0242 -0.0285 -0.0968 208 HIS D O   
15896 C CB  . HIS D 216 ? 0.2343 0.1693 0.2550 -0.0272 -0.0231 -0.1125 208 HIS D CB  
15897 C CG  . HIS D 216 ? 0.2574 0.1973 0.2773 -0.0319 -0.0262 -0.1152 208 HIS D CG  
15898 N ND1 . HIS D 216 ? 0.2856 0.2241 0.3112 -0.0341 -0.0287 -0.1107 208 HIS D ND1 
15899 C CD2 . HIS D 216 ? 0.2821 0.2292 0.2965 -0.0351 -0.0271 -0.1221 208 HIS D CD2 
15900 C CE1 . HIS D 216 ? 0.3010 0.2459 0.3252 -0.0385 -0.0311 -0.1148 208 HIS D CE1 
15901 N NE2 . HIS D 216 ? 0.2909 0.2411 0.3081 -0.0391 -0.0304 -0.1217 208 HIS D NE2 
15902 N N   . VAL D 217 ? 0.2288 0.1882 0.2236 -0.0282 -0.0302 -0.1097 209 VAL D N   
15903 C CA  . VAL D 217 ? 0.3061 0.2734 0.2940 -0.0277 -0.0340 -0.1028 209 VAL D CA  
15904 C C   . VAL D 217 ? 0.2644 0.2392 0.2532 -0.0318 -0.0381 -0.1076 209 VAL D C   
15905 O O   . VAL D 217 ? 0.2456 0.2255 0.2314 -0.0348 -0.0385 -0.1167 209 VAL D O   
15906 C CB  . VAL D 217 ? 0.3598 0.3336 0.3344 -0.0256 -0.0337 -0.1002 209 VAL D CB  
15907 C CG1 . VAL D 217 ? 0.2577 0.2391 0.2258 -0.0247 -0.0380 -0.0932 209 VAL D CG1 
15908 C CG2 . VAL D 217 ? 0.3050 0.2726 0.2791 -0.0223 -0.0297 -0.0953 209 VAL D CG2 
15909 N N   . VAL D 218 ? 0.2316 0.2084 0.2245 -0.0320 -0.0411 -0.1017 210 VAL D N   
15910 C CA  . VAL D 218 ? 0.2334 0.2206 0.2265 -0.0354 -0.0455 -0.1048 210 VAL D CA  
15911 C C   . VAL D 218 ? 0.2305 0.2271 0.2149 -0.0321 -0.0489 -0.0973 210 VAL D C   
15912 O O   . VAL D 218 ? 0.2281 0.2237 0.2156 -0.0296 -0.0497 -0.0892 210 VAL D O   
15913 C CB  . VAL D 218 ? 0.2430 0.2270 0.2483 -0.0386 -0.0464 -0.1047 210 VAL D CB  
15914 C CG1 . VAL D 218 ? 0.2640 0.2602 0.2703 -0.0433 -0.0507 -0.1104 210 VAL D CG1 
15915 C CG2 . VAL D 218 ? 0.2267 0.1978 0.2410 -0.0405 -0.0424 -0.1093 210 VAL D CG2 
15916 N N   . PRO D 219 ? 0.2652 0.2710 0.2388 -0.0319 -0.0508 -0.0994 211 PRO D N   
15917 C CA  . PRO D 219 ? 0.2447 0.2577 0.2097 -0.0280 -0.0537 -0.0910 211 PRO D CA  
15918 C C   . PRO D 219 ? 0.2656 0.2906 0.2332 -0.0288 -0.0592 -0.0901 211 PRO D C   
15919 O O   . PRO D 219 ? 0.2412 0.2715 0.2150 -0.0335 -0.0611 -0.0974 211 PRO D O   
15920 C CB  . PRO D 219 ? 0.2645 0.2825 0.2166 -0.0280 -0.0533 -0.0941 211 PRO D CB  
15921 C CG  . PRO D 219 ? 0.3478 0.3691 0.3025 -0.0334 -0.0531 -0.1063 211 PRO D CG  
15922 C CD  . PRO D 219 ? 0.2753 0.2853 0.2437 -0.0353 -0.0502 -0.1096 211 PRO D CD  
15923 N N   . ASN D 220 ? 0.2683 0.2974 0.2316 -0.0241 -0.0615 -0.0810 212 ASN D N   
15924 C CA  . ASN D 220 ? 0.2291 0.2725 0.1923 -0.0233 -0.0673 -0.0790 212 ASN D CA  
15925 C C   . ASN D 220 ? 0.2363 0.2847 0.2123 -0.0273 -0.0693 -0.0835 212 ASN D C   
15926 O O   . ASN D 220 ? 0.2905 0.3520 0.2676 -0.0308 -0.0735 -0.0889 212 ASN D O   
15927 C CB  . ASN D 220 ? 0.3345 0.3899 0.2865 -0.0245 -0.0707 -0.0826 212 ASN D CB  
15928 C CG  . ASN D 220 ? 0.3758 0.4463 0.3257 -0.0217 -0.0770 -0.0777 212 ASN D CG  
15929 O OD1 . ASN D 220 ? 0.3827 0.4520 0.3340 -0.0162 -0.0778 -0.0685 212 ASN D OD1 
15930 N ND2 . ASN D 220 ? 0.4102 0.4954 0.3572 -0.0253 -0.0814 -0.0841 212 ASN D ND2 
15931 N N   . VAL D 221 ? 0.2178 0.2566 0.2035 -0.0274 -0.0663 -0.0810 213 VAL D N   
15932 C CA  . VAL D 221 ? 0.2542 0.2971 0.2522 -0.0313 -0.0675 -0.0838 213 VAL D CA  
15933 C C   . VAL D 221 ? 0.2180 0.2700 0.2190 -0.0272 -0.0706 -0.0765 213 VAL D C   
15934 O O   . VAL D 221 ? 0.2592 0.3058 0.2578 -0.0215 -0.0691 -0.0683 213 VAL D O   
15935 C CB  . VAL D 221 ? 0.2239 0.2523 0.2305 -0.0336 -0.0627 -0.0842 213 VAL D CB  
15936 C CG1 . VAL D 221 ? 0.2118 0.2444 0.2308 -0.0382 -0.0637 -0.0863 213 VAL D CG1 
15937 C CG2 . VAL D 221 ? 0.2149 0.2344 0.2196 -0.0368 -0.0596 -0.0915 213 VAL D CG2 
15938 N N   . ASN D 222 ? 0.2482 0.3145 0.2553 -0.0301 -0.0748 -0.0798 214 ASN D N   
15939 C CA  . ASN D 222 ? 0.2082 0.2848 0.2209 -0.0264 -0.0776 -0.0739 214 ASN D CA  
15940 C C   . ASN D 222 ? 0.2326 0.2999 0.2548 -0.0266 -0.0735 -0.0705 214 ASN D C   
15941 O O   . ASN D 222 ? 0.2497 0.3167 0.2815 -0.0326 -0.0723 -0.0749 214 ASN D O   
15942 C CB  . ASN D 222 ? 0.2512 0.3467 0.2696 -0.0304 -0.0829 -0.0793 214 ASN D CB  
15943 C CG  . ASN D 222 ? 0.2876 0.3962 0.3124 -0.0258 -0.0861 -0.0734 214 ASN D CG  
15944 O OD1 . ASN D 222 ? 0.2310 0.3332 0.2598 -0.0216 -0.0833 -0.0670 214 ASN D OD1 
15945 N ND2 . ASN D 222 ? 0.3601 0.4880 0.3861 -0.0265 -0.0920 -0.0759 214 ASN D ND2 
15946 N N   . GLY D 223 ? 0.2096 0.2694 0.2289 -0.0203 -0.0711 -0.0624 215 GLY D N   
15947 C CA  . GLY D 223 ? 0.1870 0.2375 0.2132 -0.0203 -0.0669 -0.0589 215 GLY D CA  
15948 C C   . GLY D 223 ? 0.2009 0.2617 0.2383 -0.0213 -0.0679 -0.0580 215 GLY D C   
15949 O O   . GLY D 223 ? 0.2033 0.2577 0.2463 -0.0219 -0.0642 -0.0552 215 GLY D O   
15950 N N   . HIS D 224 ? 0.2414 0.3191 0.2822 -0.0216 -0.0727 -0.0602 216 HIS D N   
15951 C CA  . HIS D 224 ? 0.1927 0.2827 0.2455 -0.0232 -0.0736 -0.0604 216 HIS D CA  
15952 C C   . HIS D 224 ? 0.2203 0.3208 0.2800 -0.0316 -0.0762 -0.0685 216 HIS D C   
15953 O O   . HIS D 224 ? 0.2381 0.3537 0.3071 -0.0334 -0.0785 -0.0698 216 HIS D O   
15954 C CB  . HIS D 224 ? 0.2479 0.3505 0.3009 -0.0153 -0.0769 -0.0550 216 HIS D CB  
15955 C CG  . HIS D 224 ? 0.2585 0.3496 0.3054 -0.0075 -0.0739 -0.0475 216 HIS D CG  
15956 N ND1 . HIS D 224 ? 0.2024 0.2822 0.2523 -0.0076 -0.0686 -0.0447 216 HIS D ND1 
15957 C CD2 . HIS D 224 ? 0.2647 0.3536 0.3025 -0.0001 -0.0754 -0.0423 216 HIS D CD2 
15958 C CE1 . HIS D 224 ? 0.2426 0.3138 0.2857 -0.0008 -0.0668 -0.0389 216 HIS D CE1 
15959 N NE2 . HIS D 224 ? 0.2610 0.3367 0.2968 0.0039  -0.0707 -0.0371 216 HIS D NE2 
15960 N N   . ASP D 225 ? 0.2288 0.3217 0.2843 -0.0369 -0.0757 -0.0746 217 ASP D N   
15961 C CA  . ASP D 225 ? 0.2009 0.3002 0.2623 -0.0458 -0.0772 -0.0835 217 ASP D CA  
15962 C C   . ASP D 225 ? 0.1972 0.2793 0.2627 -0.0517 -0.0719 -0.0857 217 ASP D C   
15963 O O   . ASP D 225 ? 0.2315 0.2997 0.2906 -0.0518 -0.0695 -0.0875 217 ASP D O   
15964 C CB  . ASP D 225 ? 0.2219 0.3269 0.2745 -0.0468 -0.0810 -0.0893 217 ASP D CB  
15965 C CG  . ASP D 225 ? 0.3102 0.4213 0.3682 -0.0566 -0.0824 -0.0998 217 ASP D CG  
15966 O OD1 . ASP D 225 ? 0.2864 0.3940 0.3547 -0.0630 -0.0799 -0.1024 217 ASP D OD1 
15967 O OD2 . ASP D 225 ? 0.3254 0.4440 0.3766 -0.0581 -0.0856 -0.1050 217 ASP D OD2 
15968 N N   . THR D 226 ? 0.2537 0.3370 0.3301 -0.0563 -0.0699 -0.0852 218 THR D N   
15969 C CA  . THR D 226 ? 0.2730 0.3393 0.3531 -0.0611 -0.0648 -0.0855 218 THR D CA  
15970 C C   . THR D 226 ? 0.2802 0.3396 0.3604 -0.0681 -0.0645 -0.0944 218 THR D C   
15971 O O   . THR D 226 ? 0.2969 0.3391 0.3767 -0.0696 -0.0606 -0.0945 218 THR D O   
15972 C CB  . THR D 226 ? 0.2772 0.3472 0.3685 -0.0655 -0.0627 -0.0831 218 THR D CB  
15973 O OG1 . THR D 226 ? 0.2369 0.3236 0.3361 -0.0717 -0.0659 -0.0890 218 THR D OG1 
15974 C CG2 . THR D 226 ? 0.3175 0.3916 0.4087 -0.0584 -0.0617 -0.0747 218 THR D CG2 
15975 N N   . ALA D 227 ? 0.2931 0.3659 0.3741 -0.0722 -0.0685 -0.1018 219 ALA D N   
15976 C CA  . ALA D 227 ? 0.2874 0.3510 0.3646 -0.0770 -0.0665 -0.1075 219 ALA D CA  
15977 C C   . ALA D 227 ? 0.2976 0.3517 0.3641 -0.0726 -0.0659 -0.1092 219 ALA D C   
15978 O O   . ALA D 227 ? 0.2897 0.3280 0.3545 -0.0744 -0.0618 -0.1115 219 ALA D O   
15979 C CB  . ALA D 227 ? 0.2852 0.3645 0.3629 -0.0812 -0.0700 -0.1125 219 ALA D CB  
15980 N N   . ALA D 228 ? 0.2772 0.3408 0.3364 -0.0664 -0.0697 -0.1077 220 ALA D N   
15981 C CA  . ALA D 228 ? 0.2751 0.3305 0.3237 -0.0624 -0.0688 -0.1089 220 ALA D CA  
15982 C C   . ALA D 228 ? 0.2194 0.2561 0.2676 -0.0588 -0.0637 -0.1031 220 ALA D C   
15983 O O   . ALA D 228 ? 0.2199 0.2446 0.2643 -0.0588 -0.0609 -0.1064 220 ALA D O   
15984 C CB  . ALA D 228 ? 0.2548 0.3225 0.2936 -0.0556 -0.0730 -0.1047 220 ALA D CB  
15985 N N   . ILE D 229 ? 0.2075 0.2424 0.2599 -0.0558 -0.0624 -0.0947 221 ILE D N   
15986 C CA  . ILE D 229 ? 0.2121 0.2308 0.2643 -0.0528 -0.0578 -0.0888 221 ILE D CA  
15987 C C   . ILE D 229 ? 0.2348 0.2404 0.2942 -0.0586 -0.0544 -0.0929 221 ILE D C   
15988 O O   . ILE D 229 ? 0.2087 0.2006 0.2658 -0.0569 -0.0512 -0.0925 221 ILE D O   
15989 C CB  . ILE D 229 ? 0.2313 0.2526 0.2867 -0.0492 -0.0571 -0.0798 221 ILE D CB  
15990 C CG1 . ILE D 229 ? 0.2452 0.2766 0.2933 -0.0423 -0.0600 -0.0753 221 ILE D CG1 
15991 C CG2 . ILE D 229 ? 0.2228 0.2287 0.2779 -0.0470 -0.0526 -0.0740 221 ILE D CG2 
15992 C CD1 . ILE D 229 ? 0.2786 0.3169 0.3316 -0.0394 -0.0601 -0.0687 221 ILE D CD1 
15993 N N   . GLN D 230 ? 0.2600 0.2696 0.3286 -0.0657 -0.0549 -0.0967 222 GLN D N   
15994 C CA  . GLN D 230 ? 0.2432 0.2386 0.3166 -0.0704 -0.0506 -0.0979 222 GLN D CA  
15995 C C   . GLN D 230 ? 0.2417 0.2293 0.3089 -0.0703 -0.0490 -0.1037 222 GLN D C   
15996 O O   . GLN D 230 ? 0.2505 0.2228 0.3181 -0.0694 -0.0450 -0.1026 222 GLN D O   
15997 C CB  . GLN D 230 ? 0.2904 0.2918 0.3717 -0.0775 -0.0507 -0.0989 222 GLN D CB  
15998 C CG  . GLN D 230 ? 0.3601 0.3464 0.4449 -0.0824 -0.0465 -0.0996 222 GLN D CG  
15999 C CD  . GLN D 230 ? 0.4234 0.4155 0.5155 -0.0899 -0.0467 -0.1006 222 GLN D CD  
16000 O OE1 . GLN D 230 ? 0.4474 0.4519 0.5444 -0.0913 -0.0485 -0.0979 222 GLN D OE1 
16001 N NE2 . GLN D 230 ? 0.4653 0.4486 0.5586 -0.0948 -0.0447 -0.1048 222 GLN D NE2 
16002 N N   . THR D 231 ? 0.2454 0.2440 0.3071 -0.0711 -0.0519 -0.1097 223 THR D N   
16003 C CA  . THR D 231 ? 0.2448 0.2374 0.3004 -0.0711 -0.0502 -0.1158 223 THR D CA  
16004 C C   . THR D 231 ? 0.2769 0.2610 0.3264 -0.0649 -0.0482 -0.1139 223 THR D C   
16005 O O   . THR D 231 ? 0.3161 0.2883 0.3648 -0.0641 -0.0444 -0.1161 223 THR D O   
16006 C CB  . THR D 231 ? 0.2816 0.2898 0.3315 -0.0729 -0.0542 -0.1218 223 THR D CB  
16007 O OG1 . THR D 231 ? 0.2933 0.3100 0.3497 -0.0789 -0.0560 -0.1236 223 THR D OG1 
16008 C CG2 . THR D 231 ? 0.2852 0.2879 0.3290 -0.0734 -0.0521 -0.1287 223 THR D CG2 
16009 N N   . ALA D 232 ? 0.2675 0.2578 0.3133 -0.0601 -0.0506 -0.1097 224 ALA D N   
16010 C CA  . ALA D 232 ? 0.2373 0.2203 0.2771 -0.0544 -0.0488 -0.1076 224 ALA D CA  
16011 C C   . ALA D 232 ? 0.2698 0.2370 0.3155 -0.0531 -0.0445 -0.1029 224 ALA D C   
16012 O O   . ALA D 232 ? 0.2662 0.2243 0.3093 -0.0503 -0.0413 -0.1036 224 ALA D O   
16013 C CB  . ALA D 232 ? 0.2339 0.2259 0.2672 -0.0491 -0.0517 -0.1011 224 ALA D CB  
16014 N N   . ILE D 233 ? 0.2342 0.1992 0.2879 -0.0549 -0.0443 -0.0977 225 ILE D N   
16015 C CA  . ILE D 233 ? 0.2175 0.1687 0.2763 -0.0537 -0.0406 -0.0920 225 ILE D CA  
16016 C C   . ILE D 233 ? 0.2553 0.1958 0.3170 -0.0561 -0.0370 -0.0953 225 ILE D C   
16017 O O   . ILE D 233 ? 0.2484 0.1776 0.3108 -0.0530 -0.0338 -0.0932 225 ILE D O   
16018 C CB  . ILE D 233 ? 0.2959 0.2485 0.3617 -0.0556 -0.0413 -0.0855 225 ILE D CB  
16019 C CG1 . ILE D 233 ? 0.2485 0.2109 0.3078 -0.0506 -0.0430 -0.0789 225 ILE D CG1 
16020 C CG2 . ILE D 233 ? 0.3171 0.2560 0.3876 -0.0550 -0.0375 -0.0791 225 ILE D CG2 
16021 C CD1 . ILE D 233 ? 0.2387 0.2051 0.3031 -0.0517 -0.0429 -0.0719 225 ILE D CD1 
16022 N N   . GLU D 234 ? 0.2396 0.1838 0.3032 -0.0616 -0.0377 -0.1005 226 GLU D N   
16023 C CA  . GLU D 234 ? 0.2517 0.1855 0.3178 -0.0641 -0.0346 -0.1047 226 GLU D CA  
16024 C C   . GLU D 234 ? 0.3023 0.2324 0.3627 -0.0601 -0.0328 -0.1097 226 GLU D C   
16025 O O   . GLU D 234 ? 0.2884 0.2062 0.3516 -0.0583 -0.0292 -0.1097 226 GLU D O   
16026 C CB  . GLU D 234 ? 0.3407 0.2810 0.4090 -0.0710 -0.0362 -0.1104 226 GLU D CB  
16027 C CG  . GLU D 234 ? 0.3064 0.2478 0.3820 -0.0757 -0.0366 -0.1055 226 GLU D CG  
16028 C CD  . GLU D 234 ? 0.3926 0.3433 0.4706 -0.0826 -0.0387 -0.1109 226 GLU D CD  
16029 O OE1 . GLU D 234 ? 0.3983 0.3552 0.4719 -0.0837 -0.0402 -0.1184 226 GLU D OE1 
16030 O OE2 . GLU D 234 ? 0.3443 0.2966 0.4286 -0.0871 -0.0388 -0.1075 226 GLU D OE2 
16031 N N   . ALA D 235 ? 0.3128 0.2538 0.3655 -0.0587 -0.0351 -0.1138 227 ALA D N   
16032 C CA  . ALA D 235 ? 0.3215 0.2603 0.3682 -0.0551 -0.0331 -0.1184 227 ALA D CA  
16033 C C   . ALA D 235 ? 0.2779 0.2085 0.3251 -0.0491 -0.0306 -0.1128 227 ALA D C   
16034 O O   . ALA D 235 ? 0.2871 0.2099 0.3348 -0.0465 -0.0272 -0.1152 227 ALA D O   
16035 C CB  . ALA D 235 ? 0.3746 0.3276 0.4118 -0.0548 -0.0364 -0.1225 227 ALA D CB  
16036 N N   . ALA D 236 ? 0.2394 0.1719 0.2870 -0.0470 -0.0323 -0.1057 228 ALA D N   
16037 C CA  . ALA D 236 ? 0.3159 0.2415 0.3644 -0.0418 -0.0303 -0.0998 228 ALA D CA  
16038 C C   . ALA D 236 ? 0.2824 0.1950 0.3389 -0.0412 -0.0269 -0.0968 228 ALA D C   
16039 O O   . ALA D 236 ? 0.2812 0.1874 0.3385 -0.0370 -0.0241 -0.0966 228 ALA D O   
16040 C CB  . ALA D 236 ? 0.2757 0.2057 0.3238 -0.0405 -0.0329 -0.0928 228 ALA D CB  
16041 N N   . ARG D 237 ? 0.2411 0.1501 0.3038 -0.0452 -0.0270 -0.0942 229 ARG D N   
16042 C CA  . ARG D 237 ? 0.2915 0.1878 0.3613 -0.0448 -0.0241 -0.0905 229 ARG D CA  
16043 C C   . ARG D 237 ? 0.3767 0.2661 0.4477 -0.0445 -0.0213 -0.0975 229 ARG D C   
16044 O O   . ARG D 237 ? 0.3492 0.2283 0.4250 -0.0413 -0.0186 -0.0952 229 ARG D O   
16045 C CB  . ARG D 237 ? 0.2754 0.1702 0.3505 -0.0500 -0.0248 -0.0863 229 ARG D CB  
16046 C CG  . ARG D 237 ? 0.2869 0.1880 0.3620 -0.0499 -0.0270 -0.0790 229 ARG D CG  
16047 C CD  . ARG D 237 ? 0.3116 0.2152 0.3912 -0.0561 -0.0280 -0.0769 229 ARG D CD  
16048 N NE  . ARG D 237 ? 0.3720 0.2642 0.4571 -0.0591 -0.0253 -0.0757 229 ARG D NE  
16049 C CZ  . ARG D 237 ? 0.4344 0.3173 0.5234 -0.0576 -0.0234 -0.0678 229 ARG D CZ  
16050 N NH1 . ARG D 237 ? 0.3307 0.2150 0.4189 -0.0535 -0.0239 -0.0607 229 ARG D NH1 
16051 N NH2 . ARG D 237 ? 0.4547 0.3268 0.5481 -0.0603 -0.0212 -0.0668 229 ARG D NH2 
16052 N N   . ALA D 238 ? 0.3264 0.2219 0.3933 -0.0476 -0.0221 -0.1062 230 ALA D N   
16053 C CA  . ALA D 238 ? 0.3670 0.2566 0.4347 -0.0477 -0.0194 -0.1138 230 ALA D CA  
16054 C C   . ALA D 238 ? 0.3643 0.2536 0.4293 -0.0416 -0.0172 -0.1161 230 ALA D C   
16055 O O   . ALA D 238 ? 0.3446 0.2263 0.4128 -0.0397 -0.0141 -0.1203 230 ALA D O   
16056 C CB  . ALA D 238 ? 0.3915 0.2892 0.4553 -0.0531 -0.0210 -0.1225 230 ALA D CB  
16057 N N   . GLU D 239 ? 0.3424 0.2399 0.4016 -0.0387 -0.0187 -0.1136 231 GLU D N   
16058 C CA  . GLU D 239 ? 0.3453 0.2433 0.4018 -0.0332 -0.0166 -0.1151 231 GLU D CA  
16059 C C   . GLU D 239 ? 0.3714 0.2610 0.4346 -0.0285 -0.0150 -0.1073 231 GLU D C   
16060 O O   . GLU D 239 ? 0.4539 0.3457 0.5167 -0.0272 -0.0168 -0.1000 231 GLU D O   
16061 C CB  . GLU D 239 ? 0.4096 0.3195 0.4565 -0.0326 -0.0188 -0.1157 231 GLU D CB  
16062 C CG  . GLU D 239 ? 0.4567 0.3675 0.5009 -0.0273 -0.0165 -0.1160 231 GLU D CG  
16063 C CD  . GLU D 239 ? 0.4776 0.3854 0.5234 -0.0258 -0.0127 -0.1235 231 GLU D CD  
16064 O OE1 . GLU D 239 ? 0.4782 0.3910 0.5190 -0.0289 -0.0127 -0.1312 231 GLU D OE1 
16065 O OE2 . GLU D 239 ? 0.5135 0.4143 0.5660 -0.0215 -0.0099 -0.1219 231 GLU D OE2 
16066 N N   . THR D 240 ? 0.3687 0.2491 0.4385 -0.0258 -0.0119 -0.1087 232 THR D N   
16067 C CA  . THR D 240 ? 0.3488 0.2212 0.4260 -0.0215 -0.0108 -0.1007 232 THR D CA  
16068 C C   . THR D 240 ? 0.3427 0.2179 0.4199 -0.0154 -0.0094 -0.1001 232 THR D C   
16069 O O   . THR D 240 ? 0.3732 0.2444 0.4559 -0.0115 -0.0093 -0.0927 232 THR D O   
16070 C CB  . THR D 240 ? 0.4413 0.3015 0.5268 -0.0213 -0.0085 -0.1012 232 THR D CB  
16071 O OG1 . THR D 240 ? 0.4908 0.3496 0.5768 -0.0194 -0.0055 -0.1102 232 THR D OG1 
16072 C CG2 . THR D 240 ? 0.4571 0.3140 0.5434 -0.0279 -0.0097 -0.1013 232 THR D CG2 
16073 N N   . GLY D 241 ? 0.3074 0.1898 0.3786 -0.0146 -0.0082 -0.1074 233 GLY D N   
16074 C CA  . GLY D 241 ? 0.3527 0.2377 0.4248 -0.0091 -0.0061 -0.1080 233 GLY D CA  
16075 C C   . GLY D 241 ? 0.3225 0.2163 0.3877 -0.0084 -0.0078 -0.1048 233 GLY D C   
16076 O O   . GLY D 241 ? 0.3684 0.2641 0.4355 -0.0040 -0.0064 -0.1034 233 GLY D O   
16077 N N   . LYS D 242 ? 0.2555 0.1548 0.3129 -0.0126 -0.0108 -0.1040 234 LYS D N   
16078 C CA  . LYS D 242 ? 0.2703 0.1776 0.3197 -0.0124 -0.0125 -0.1018 234 LYS D CA  
16079 C C   . LYS D 242 ? 0.2823 0.1896 0.3311 -0.0147 -0.0162 -0.0944 234 LYS D C   
16080 O O   . LYS D 242 ? 0.2901 0.1955 0.3406 -0.0184 -0.0178 -0.0939 234 LYS D O   
16081 C CB  . LYS D 242 ? 0.2607 0.1771 0.2993 -0.0150 -0.0127 -0.1090 234 LYS D CB  
16082 C CG  . LYS D 242 ? 0.3943 0.3123 0.4320 -0.0139 -0.0091 -0.1175 234 LYS D CG  
16083 C CD  . LYS D 242 ? 0.4008 0.3284 0.4269 -0.0174 -0.0101 -0.1235 234 LYS D CD  
16084 C CE  . LYS D 242 ? 0.4723 0.4030 0.4963 -0.0167 -0.0063 -0.1320 234 LYS D CE  
16085 N NZ  . LYS D 242 ? 0.5073 0.4487 0.5186 -0.0199 -0.0074 -0.1366 234 LYS D NZ  
16086 N N   . PRO D 243 ? 0.2675 0.1781 0.3130 -0.0130 -0.0172 -0.0880 235 PRO D N   
16087 C CA  . PRO D 243 ? 0.2224 0.1362 0.2640 -0.0152 -0.0202 -0.0807 235 PRO D CA  
16088 C C   . PRO D 243 ? 0.2731 0.1944 0.3061 -0.0183 -0.0223 -0.0849 235 PRO D C   
16089 O O   . PRO D 243 ? 0.2486 0.1748 0.2749 -0.0181 -0.0215 -0.0909 235 PRO D O   
16090 C CB  . PRO D 243 ? 0.2154 0.1328 0.2526 -0.0122 -0.0197 -0.0729 235 PRO D CB  
16091 C CG  . PRO D 243 ? 0.2000 0.1202 0.2345 -0.0097 -0.0169 -0.0776 235 PRO D CG  
16092 C CD  . PRO D 243 ? 0.2095 0.1239 0.2522 -0.0091 -0.0150 -0.0857 235 PRO D CD  
16093 N N   . SER D 244 ? 0.2640 0.1870 0.2972 -0.0210 -0.0252 -0.0816 236 SER D N   
16094 C CA  . SER D 244 ? 0.2773 0.2082 0.3042 -0.0239 -0.0279 -0.0851 236 SER D CA  
16095 C C   . SER D 244 ? 0.2319 0.1691 0.2523 -0.0229 -0.0300 -0.0773 236 SER D C   
16096 O O   . SER D 244 ? 0.2190 0.1538 0.2427 -0.0222 -0.0301 -0.0701 236 SER D O   
16097 C CB  . SER D 244 ? 0.2506 0.1798 0.2846 -0.0285 -0.0296 -0.0892 236 SER D CB  
16098 O OG  . SER D 244 ? 0.2964 0.2195 0.3355 -0.0295 -0.0270 -0.0955 236 SER D OG  
16099 N N   . ILE D 245 ? 0.2117 0.1571 0.2227 -0.0227 -0.0316 -0.0789 237 ILE D N   
16100 C CA  . ILE D 245 ? 0.2194 0.1706 0.2249 -0.0217 -0.0340 -0.0725 237 ILE D CA  
16101 C C   . ILE D 245 ? 0.2244 0.1842 0.2278 -0.0241 -0.0376 -0.0765 237 ILE D C   
16102 O O   . ILE D 245 ? 0.2047 0.1687 0.2038 -0.0256 -0.0382 -0.0834 237 ILE D O   
16103 C CB  . ILE D 245 ? 0.2091 0.1618 0.2048 -0.0184 -0.0327 -0.0682 237 ILE D CB  
16104 C CG1 . ILE D 245 ? 0.2236 0.1808 0.2145 -0.0169 -0.0349 -0.0616 237 ILE D CG1 
16105 C CG2 . ILE D 245 ? 0.2268 0.1835 0.2147 -0.0186 -0.0320 -0.0743 237 ILE D CG2 
16106 C CD1 . ILE D 245 ? 0.1944 0.1501 0.1771 -0.0140 -0.0330 -0.0559 237 ILE D CD1 
16107 N N   . ILE D 246 ? 0.1937 0.1571 0.2006 -0.0249 -0.0400 -0.0726 238 ILE D N   
16108 C CA  . ILE D 246 ? 0.2069 0.1802 0.2135 -0.0271 -0.0439 -0.0755 238 ILE D CA  
16109 C C   . ILE D 246 ? 0.2134 0.1935 0.2132 -0.0233 -0.0459 -0.0688 238 ILE D C   
16110 O O   . ILE D 246 ? 0.1870 0.1650 0.1894 -0.0213 -0.0453 -0.0622 238 ILE D O   
16111 C CB  . ILE D 246 ? 0.2182 0.1915 0.2357 -0.0310 -0.0448 -0.0766 238 ILE D CB  
16112 C CG1 . ILE D 246 ? 0.2818 0.2462 0.3064 -0.0345 -0.0424 -0.0826 238 ILE D CG1 
16113 C CG2 . ILE D 246 ? 0.2060 0.1919 0.2238 -0.0335 -0.0490 -0.0797 238 ILE D CG2 
16114 C CD1 . ILE D 246 ? 0.2601 0.2211 0.2956 -0.0385 -0.0422 -0.0818 238 ILE D CD1 
16115 N N   . CYS D 247 ? 0.2119 0.1997 0.2029 -0.0223 -0.0483 -0.0704 239 CYS D N   
16116 C CA  . CYS D 247 ? 0.2412 0.2339 0.2250 -0.0180 -0.0501 -0.0635 239 CYS D CA  
16117 C C   . CYS D 247 ? 0.2186 0.2218 0.2067 -0.0182 -0.0543 -0.0627 239 CYS D C   
16118 O O   . CYS D 247 ? 0.2102 0.2236 0.1966 -0.0201 -0.0579 -0.0673 239 CYS D O   
16119 C CB  . CYS D 247 ? 0.2116 0.2073 0.1832 -0.0166 -0.0505 -0.0642 239 CYS D CB  
16120 S SG  . CYS D 247 ? 0.2723 0.2577 0.2401 -0.0166 -0.0451 -0.0658 239 CYS D SG  
16121 N N   . CYS D 248 ? 0.1910 0.1931 0.1849 -0.0163 -0.0540 -0.0571 240 CYS D N   
16122 C CA  . CYS D 248 ? 0.2424 0.2550 0.2427 -0.0164 -0.0573 -0.0564 240 CYS D CA  
16123 C C   . CYS D 248 ? 0.2202 0.2390 0.2148 -0.0105 -0.0598 -0.0502 240 CYS D C   
16124 O O   . CYS D 248 ? 0.2088 0.2215 0.2022 -0.0065 -0.0575 -0.0439 240 CYS D O   
16125 C CB  . CYS D 248 ? 0.2410 0.2495 0.2516 -0.0180 -0.0551 -0.0545 240 CYS D CB  
16126 S SG  . CYS D 248 ? 0.2706 0.2718 0.2891 -0.0248 -0.0527 -0.0609 240 CYS D SG  
16127 N N   . LYS D 249 ? 0.2176 0.2483 0.2085 -0.0101 -0.0643 -0.0519 241 LYS D N   
16128 C CA  A LYS D 249 ? 0.2446 0.2822 0.2307 -0.0040 -0.0673 -0.0456 241 LYS D CA  
16129 C CA  B LYS D 249 ? 0.2429 0.2805 0.2290 -0.0040 -0.0674 -0.0456 241 LYS D CA  
16130 C C   . LYS D 249 ? 0.2072 0.2519 0.2037 -0.0020 -0.0687 -0.0429 241 LYS D C   
16131 O O   . LYS D 249 ? 0.1990 0.2552 0.2032 -0.0052 -0.0717 -0.0472 241 LYS D O   
16132 C CB  A LYS D 249 ? 0.2901 0.3401 0.2692 -0.0043 -0.0723 -0.0481 241 LYS D CB  
16133 C CB  B LYS D 249 ? 0.2904 0.3405 0.2696 -0.0044 -0.0723 -0.0482 241 LYS D CB  
16134 C CG  A LYS D 249 ? 0.3315 0.3765 0.2999 -0.0066 -0.0708 -0.0515 241 LYS D CG  
16135 C CG  B LYS D 249 ? 0.3278 0.3732 0.2969 -0.0071 -0.0708 -0.0523 241 LYS D CG  
16136 C CD  A LYS D 249 ? 0.3686 0.4033 0.3270 -0.0020 -0.0679 -0.0444 241 LYS D CD  
16137 C CD  B LYS D 249 ? 0.3812 0.4163 0.3401 -0.0028 -0.0679 -0.0454 241 LYS D CD  
16138 C CE  A LYS D 249 ? 0.3662 0.3998 0.3130 -0.0041 -0.0670 -0.0473 241 LYS D CE  
16139 C CE  B LYS D 249 ? 0.3697 0.4023 0.3182 -0.0055 -0.0663 -0.0494 241 LYS D CE  
16140 N NZ  A LYS D 249 ? 0.3511 0.3794 0.3014 -0.0097 -0.0636 -0.0559 241 LYS D NZ  
16141 N NZ  B LYS D 249 ? 0.3256 0.3485 0.2645 -0.0020 -0.0631 -0.0425 241 LYS D NZ  
16142 N N   . THR D 250 ? 0.1962 0.2343 0.1931 0.0031  -0.0662 -0.0363 242 THR D N   
16143 C CA  . THR D 250 ? 0.2034 0.2478 0.2102 0.0055  -0.0666 -0.0340 242 THR D CA  
16144 C C   . THR D 250 ? 0.2721 0.3183 0.2754 0.0137  -0.0679 -0.0268 242 THR D C   
16145 O O   . THR D 250 ? 0.2684 0.3076 0.2614 0.0172  -0.0675 -0.0227 242 THR D O   
16146 C CB  . THR D 250 ? 0.2149 0.2494 0.2278 0.0033  -0.0614 -0.0336 242 THR D CB  
16147 O OG1 . THR D 250 ? 0.2608 0.2815 0.2660 0.0063  -0.0576 -0.0292 242 THR D OG1 
16148 C CG2 . THR D 250 ? 0.2006 0.2321 0.2181 -0.0043 -0.0600 -0.0396 242 THR D CG2 
16149 N N   . LEU D 251 ? 0.1999 0.2552 0.2126 0.0167  -0.0691 -0.0253 243 LEU D N   
16150 C CA  . LEU D 251 ? 0.2435 0.2985 0.2559 0.0251  -0.0691 -0.0186 243 LEU D CA  
16151 C C   . LEU D 251 ? 0.2647 0.3100 0.2822 0.0258  -0.0634 -0.0173 243 LEU D C   
16152 O O   . LEU D 251 ? 0.2439 0.2942 0.2711 0.0220  -0.0620 -0.0207 243 LEU D O   
16153 C CB  . LEU D 251 ? 0.2984 0.3719 0.3184 0.0291  -0.0743 -0.0179 243 LEU D CB  
16154 C CG  . LEU D 251 ? 0.2847 0.3710 0.2998 0.0288  -0.0807 -0.0190 243 LEU D CG  
16155 C CD1 . LEU D 251 ? 0.3022 0.4088 0.3272 0.0322  -0.0858 -0.0188 243 LEU D CD1 
16156 C CD2 . LEU D 251 ? 0.3109 0.3892 0.3126 0.0339  -0.0815 -0.0129 243 LEU D CD2 
16157 N N   . ILE D 252 ? 0.2303 0.2621 0.2408 0.0299  -0.0600 -0.0126 244 ILE D N   
16158 C CA  . ILE D 252 ? 0.2127 0.2367 0.2276 0.0310  -0.0548 -0.0116 244 ILE D CA  
16159 C C   . ILE D 252 ? 0.1853 0.2211 0.2108 0.0360  -0.0559 -0.0108 244 ILE D C   
16160 O O   . ILE D 252 ? 0.2246 0.2692 0.2511 0.0421  -0.0599 -0.0079 244 ILE D O   
16161 C CB  . ILE D 252 ? 0.2669 0.2747 0.2723 0.0344  -0.0511 -0.0072 244 ILE D CB  
16162 C CG1 . ILE D 252 ? 0.3163 0.3157 0.3253 0.0333  -0.0453 -0.0078 244 ILE D CG1 
16163 C CG2 . ILE D 252 ? 0.2937 0.3019 0.2957 0.0429  -0.0533 -0.0014 244 ILE D CG2 
16164 C CD1 . ILE D 252 ? 0.3088 0.2918 0.3085 0.0343  -0.0411 -0.0048 244 ILE D CD1 
16165 N N   . GLY D 253 ? 0.2123 0.2496 0.2462 0.0333  -0.0523 -0.0133 245 GLY D N   
16166 C CA  . GLY D 253 ? 0.1781 0.2283 0.2232 0.0373  -0.0528 -0.0135 245 GLY D CA  
16167 C C   . GLY D 253 ? 0.2286 0.2976 0.2813 0.0358  -0.0583 -0.0161 245 GLY D C   
16168 O O   . GLY D 253 ? 0.2269 0.3089 0.2878 0.0412  -0.0604 -0.0152 245 GLY D O   
16169 N N   . LYS D 254 ? 0.1851 0.2563 0.2355 0.0286  -0.0607 -0.0197 246 LYS D N   
16170 C CA  . LYS D 254 ? 0.1824 0.2714 0.2396 0.0256  -0.0658 -0.0233 246 LYS D CA  
16171 C C   . LYS D 254 ? 0.2294 0.3323 0.3006 0.0248  -0.0649 -0.0255 246 LYS D C   
16172 O O   . LYS D 254 ? 0.2319 0.3300 0.3073 0.0208  -0.0599 -0.0269 246 LYS D O   
16173 C CB  . LYS D 254 ? 0.2340 0.3198 0.2881 0.0164  -0.0664 -0.0283 246 LYS D CB  
16174 C CG  . LYS D 254 ? 0.2706 0.3737 0.3322 0.0111  -0.0710 -0.0335 246 LYS D CG  
16175 C CD  . LYS D 254 ? 0.3277 0.4421 0.3849 0.0149  -0.0775 -0.0328 246 LYS D CD  
16176 C CE  . LYS D 254 ? 0.3020 0.4348 0.3670 0.0088  -0.0820 -0.0389 246 LYS D CE  
16177 N NZ  . LYS D 254 ? 0.4045 0.5526 0.4670 0.0135  -0.0889 -0.0376 246 LYS D NZ  
16178 N N   . GLY D 255 ? 0.2415 0.3627 0.3200 0.0286  -0.0697 -0.0255 247 GLY D N   
16179 C CA  . GLY D 255 ? 0.2691 0.4062 0.3617 0.0286  -0.0690 -0.0275 247 GLY D CA  
16180 C C   . GLY D 255 ? 0.2260 0.3651 0.3234 0.0386  -0.0670 -0.0235 247 GLY D C   
16181 O O   . GLY D 255 ? 0.1910 0.3468 0.3009 0.0404  -0.0673 -0.0250 247 GLY D O   
16182 N N   . SER D 256 ? 0.2080 0.3307 0.2964 0.0449  -0.0646 -0.0189 248 SER D N   
16183 C CA  . SER D 256 ? 0.1881 0.3112 0.2810 0.0551  -0.0626 -0.0153 248 SER D CA  
16184 C C   . SER D 256 ? 0.1874 0.3278 0.2860 0.0631  -0.0690 -0.0126 248 SER D C   
16185 O O   . SER D 256 ? 0.2687 0.4123 0.3608 0.0635  -0.0748 -0.0108 248 SER D O   
16186 C CB  . SER D 256 ? 0.2648 0.3655 0.3460 0.0595  -0.0589 -0.0110 248 SER D CB  
16187 O OG  . SER D 256 ? 0.2977 0.3975 0.3829 0.0699  -0.0573 -0.0075 248 SER D OG  
16188 N N   . ALA D 257 ? 0.2138 0.3666 0.3249 0.0696  -0.0680 -0.0125 249 ALA D N   
16189 C CA  . ALA D 257 ? 0.2736 0.4458 0.3923 0.0776  -0.0745 -0.0100 249 ALA D CA  
16190 C C   . ALA D 257 ? 0.3215 0.4841 0.4313 0.0880  -0.0774 -0.0023 249 ALA D C   
16191 O O   . ALA D 257 ? 0.3506 0.5264 0.4606 0.0925  -0.0846 0.0009  249 ALA D O   
16192 C CB  . ALA D 257 ? 0.1924 0.3801 0.3275 0.0826  -0.0720 -0.0119 249 ALA D CB  
16193 N N   . ASN D 258 ? 0.2710 0.4110 0.3727 0.0916  -0.0721 0.0008  250 ASN D N   
16194 C CA  . ASN D 258 ? 0.2284 0.3569 0.3222 0.1018  -0.0737 0.0086  250 ASN D CA  
16195 C C   . ASN D 258 ? 0.2731 0.3761 0.3507 0.0987  -0.0702 0.0111  250 ASN D C   
16196 O O   . ASN D 258 ? 0.3095 0.4028 0.3784 0.1052  -0.0722 0.0179  250 ASN D O   
16197 C CB  . ASN D 258 ? 0.2416 0.3693 0.3450 0.1131  -0.0703 0.0110  250 ASN D CB  
16198 C CG  . ASN D 258 ? 0.2610 0.4152 0.3813 0.1182  -0.0740 0.0095  250 ASN D CG  
16199 O OD1 . ASN D 258 ? 0.2614 0.4293 0.3842 0.1250  -0.0811 0.0141  250 ASN D OD1 
16200 N ND2 . ASN D 258 ? 0.2454 0.4080 0.3774 0.1150  -0.0692 0.0032  250 ASN D ND2 
16201 N N   . LYS D 259 ? 0.2257 0.3179 0.2992 0.0891  -0.0651 0.0061  251 LYS D N   
16202 C CA  . LYS D 259 ? 0.2271 0.2964 0.2864 0.0858  -0.0615 0.0079  251 LYS D CA  
16203 C C   . LYS D 259 ? 0.2270 0.2954 0.2780 0.0756  -0.0635 0.0050  251 LYS D C   
16204 O O   . LYS D 259 ? 0.2792 0.3309 0.3203 0.0709  -0.0598 0.0048  251 LYS D O   
16205 C CB  . LYS D 259 ? 0.2636 0.3193 0.3244 0.0843  -0.0533 0.0052  251 LYS D CB  
16206 C CG  . LYS D 259 ? 0.2525 0.3087 0.3221 0.0944  -0.0506 0.0068  251 LYS D CG  
16207 C CD  . LYS D 259 ? 0.2195 0.2605 0.2883 0.0926  -0.0422 0.0037  251 LYS D CD  
16208 C CE  . LYS D 259 ? 0.2327 0.2702 0.3084 0.1037  -0.0390 0.0056  251 LYS D CE  
16209 N NZ  . LYS D 259 ? 0.2798 0.3030 0.3543 0.1014  -0.0306 0.0016  251 LYS D NZ  
16210 N N   . GLU D 260 ? 0.2852 0.3715 0.3405 0.0721  -0.0690 0.0023  252 GLU D N   
16211 C CA  . GLU D 260 ? 0.2577 0.3432 0.3059 0.0626  -0.0708 -0.0012 252 GLU D CA  
16212 C C   . GLU D 260 ? 0.3045 0.3779 0.3377 0.0641  -0.0723 0.0034  252 GLU D C   
16213 O O   . GLU D 260 ? 0.3073 0.3838 0.3370 0.0715  -0.0763 0.0093  252 GLU D O   
16214 C CB  . GLU D 260 ? 0.2728 0.3805 0.3285 0.0593  -0.0768 -0.0050 252 GLU D CB  
16215 C CG  . GLU D 260 ? 0.2738 0.3812 0.3235 0.0494  -0.0784 -0.0099 252 GLU D CG  
16216 C CD  . GLU D 260 ? 0.3020 0.4310 0.3609 0.0448  -0.0833 -0.0151 252 GLU D CD  
16217 O OE1 . GLU D 260 ? 0.3792 0.5212 0.4361 0.0474  -0.0897 -0.0137 252 GLU D OE1 
16218 O OE2 . GLU D 260 ? 0.2521 0.3856 0.3203 0.0385  -0.0808 -0.0202 252 GLU D OE2 
16219 N N   . GLY D 261 ? 0.3161 0.3760 0.3406 0.0569  -0.0691 0.0011  253 GLY D N   
16220 C CA  . GLY D 261 ? 0.3749 0.4228 0.3853 0.0570  -0.0694 0.0047  253 GLY D CA  
16221 C C   . GLY D 261 ? 0.3595 0.3897 0.3636 0.0626  -0.0650 0.0105  253 GLY D C   
16222 O O   . GLY D 261 ? 0.3862 0.4055 0.3782 0.0622  -0.0646 0.0139  253 GLY D O   
16223 N N   . SER D 262 ? 0.3421 0.3689 0.3539 0.0672  -0.0614 0.0113  254 SER D N   
16224 C CA  . SER D 262 ? 0.3819 0.3919 0.3886 0.0729  -0.0573 0.0164  254 SER D CA  
16225 C C   . SER D 262 ? 0.3736 0.3675 0.3758 0.0666  -0.0506 0.0134  254 SER D C   
16226 O O   . SER D 262 ? 0.3516 0.3478 0.3606 0.0620  -0.0476 0.0081  254 SER D O   
16227 C CB  . SER D 262 ? 0.4183 0.4325 0.4359 0.0816  -0.0564 0.0181  254 SER D CB  
16228 O OG  . SER D 262 ? 0.4222 0.4181 0.4355 0.0860  -0.0512 0.0216  254 SER D OG  
16229 N N   . HIS D 263 ? 0.5765 0.4366 0.5380 -0.0073 0.0485  0.0839  255 HIS D N   
16230 C CA  . HIS D 263 ? 0.5741 0.4485 0.5780 -0.0192 0.0594  0.0839  255 HIS D CA  
16231 C C   . HIS D 263 ? 0.5160 0.3955 0.5540 -0.0250 0.0442  0.0753  255 HIS D C   
16232 O O   . HIS D 263 ? 0.4258 0.3204 0.4985 -0.0341 0.0461  0.0700  255 HIS D O   
16233 C CB  . HIS D 263 ? 0.7052 0.5668 0.7114 -0.0251 0.0812  0.1034  255 HIS D CB  
16234 C CG  . HIS D 263 ? 0.8089 0.6522 0.8305 -0.0311 0.0770  0.1135  255 HIS D CG  
16235 N ND1 . HIS D 263 ? 0.8542 0.6733 0.8487 -0.0234 0.0655  0.1193  255 HIS D ND1 
16236 C CD2 . HIS D 263 ? 0.8186 0.6626 0.8809 -0.0440 0.0814  0.1187  255 HIS D CD2 
16237 C CE1 . HIS D 263 ? 0.8788 0.6825 0.8953 -0.0308 0.0641  0.1274  255 HIS D CE1 
16238 N NE2 . HIS D 263 ? 0.8483 0.6663 0.9057 -0.0441 0.0732  0.1268  255 HIS D NE2 
16239 N N   . LYS D 264 ? 0.5306 0.3973 0.5587 -0.0189 0.0286  0.0732  256 LYS D N   
16240 C CA  . LYS D 264 ? 0.5158 0.3848 0.5713 -0.0223 0.0154  0.0633  256 LYS D CA  
16241 C C   . LYS D 264 ? 0.4593 0.3524 0.5280 -0.0222 0.0067  0.0456  256 LYS D C   
16242 O O   . LYS D 264 ? 0.3773 0.2740 0.4678 -0.0262 -0.0012 0.0366  256 LYS D O   
16243 C CB  . LYS D 264 ? 0.6020 0.4513 0.6442 -0.0132 0.0025  0.0652  256 LYS D CB  
16244 C CG  . LYS D 264 ? 0.6911 0.5488 0.7147 -0.0009 -0.0108 0.0564  256 LYS D CG  
16245 C CD  . LYS D 264 ? 0.7729 0.6093 0.7811 0.0099  -0.0216 0.0632  256 LYS D CD  
16246 C CE  . LYS D 264 ? 0.7693 0.6120 0.7535 0.0217  -0.0331 0.0606  256 LYS D CE  
16247 N NZ  . LYS D 264 ? 0.7964 0.6210 0.7697 0.0340  -0.0466 0.0668  256 LYS D NZ  
16248 N N   . THR D 265 ? 0.3171 0.2239 0.3706 -0.0179 0.0077  0.0406  257 THR D N   
16249 C CA  . THR D 265 ? 0.3060 0.2341 0.3725 -0.0192 0.0013  0.0261  257 THR D CA  
16250 C C   . THR D 265 ? 0.3083 0.2496 0.3969 -0.0281 0.0104  0.0248  257 THR D C   
16251 O O   . THR D 265 ? 0.2685 0.2253 0.3681 -0.0299 0.0053  0.0144  257 THR D O   
16252 C CB  . THR D 265 ? 0.3599 0.2954 0.4040 -0.0118 -0.0038 0.0205  257 THR D CB  
16253 O OG1 . THR D 265 ? 0.3378 0.2705 0.3635 -0.0111 0.0083  0.0262  257 THR D OG1 
16254 C CG2 . THR D 265 ? 0.4089 0.3341 0.4349 -0.0023 -0.0156 0.0219  257 THR D CG2 
16255 N N   . HIS D 266 ? 0.3182 0.2542 0.4155 -0.0336 0.0240  0.0363  258 HIS D N   
16256 C CA  . HIS D 266 ? 0.3197 0.2711 0.4439 -0.0411 0.0323  0.0358  258 HIS D CA  
16257 C C   . HIS D 266 ? 0.2565 0.2149 0.4104 -0.0487 0.0204  0.0275  258 HIS D C   
16258 O O   . HIS D 266 ? 0.2691 0.2429 0.4347 -0.0502 0.0157  0.0189  258 HIS D O   
16259 C CB  . HIS D 266 ? 0.3713 0.3177 0.5041 -0.0457 0.0510  0.0511  258 HIS D CB  
16260 C CG  . HIS D 266 ? 0.4742 0.4396 0.6420 -0.0528 0.0599  0.0518  258 HIS D CG  
16261 N ND1 . HIS D 266 ? 0.4624 0.4324 0.6696 -0.0641 0.0572  0.0545  258 HIS D ND1 
16262 C CD2 . HIS D 266 ? 0.4782 0.4589 0.6494 -0.0496 0.0698  0.0495  258 HIS D CD2 
16263 C CE1 . HIS D 266 ? 0.4560 0.4459 0.6922 -0.0675 0.0646  0.0548  258 HIS D CE1 
16264 N NE2 . HIS D 266 ? 0.4703 0.4668 0.6852 -0.0581 0.0734  0.0519  258 HIS D NE2 
16265 N N   . GLY D 267 ? 0.2582 0.2024 0.4214 -0.0530 0.0143  0.0298  259 GLY D N   
16266 C CA  . GLY D 267 ? 0.2682 0.2149 0.4579 -0.0613 0.0034  0.0225  259 GLY D CA  
16267 C C   . GLY D 267 ? 0.3217 0.2541 0.5033 -0.0585 -0.0112 0.0131  259 GLY D C   
16268 O O   . GLY D 267 ? 0.2703 0.1959 0.4689 -0.0654 -0.0205 0.0081  259 GLY D O   
16269 N N   . ALA D 268 ? 0.2840 0.2117 0.4405 -0.0480 -0.0138 0.0100  260 ALA D N   
16270 C CA  . ALA D 268 ? 0.2999 0.2159 0.4498 -0.0427 -0.0250 0.0008  260 ALA D CA  
16271 C C   . ALA D 268 ? 0.2661 0.1949 0.4000 -0.0329 -0.0286 -0.0079 260 ALA D C   
16272 O O   . ALA D 268 ? 0.2594 0.1986 0.3822 -0.0291 -0.0238 -0.0043 260 ALA D O   
16273 C CB  . ALA D 268 ? 0.3601 0.2515 0.5029 -0.0391 -0.0249 0.0091  260 ALA D CB  
16274 N N   . PRO D 269 ? 0.2634 0.1911 0.3959 -0.0289 -0.0365 -0.0195 261 PRO D N   
16275 C CA  . PRO D 269 ? 0.2331 0.1744 0.3556 -0.0201 -0.0382 -0.0262 261 PRO D CA  
16276 C C   . PRO D 269 ? 0.2683 0.2063 0.3804 -0.0110 -0.0379 -0.0196 261 PRO D C   
16277 O O   . PRO D 269 ? 0.2684 0.1879 0.3773 -0.0086 -0.0381 -0.0119 261 PRO D O   
16278 C CB  . PRO D 269 ? 0.2952 0.2298 0.4178 -0.0161 -0.0438 -0.0380 261 PRO D CB  
16279 C CG  . PRO D 269 ? 0.3142 0.2373 0.4449 -0.0259 -0.0475 -0.0404 261 PRO D CG  
16280 C CD  . PRO D 269 ? 0.2966 0.2110 0.4368 -0.0328 -0.0437 -0.0276 261 PRO D CD  
16281 N N   . LEU D 270 ? 0.2306 0.1857 0.3375 -0.0063 -0.0388 -0.0221 262 LEU D N   
16282 C CA  . LEU D 270 ? 0.2809 0.2347 0.3780 0.0026  -0.0425 -0.0169 262 LEU D CA  
16283 C C   . LEU D 270 ? 0.3133 0.2585 0.4142 0.0130  -0.0484 -0.0193 262 LEU D C   
16284 O O   . LEU D 270 ? 0.3405 0.2750 0.4337 0.0206  -0.0529 -0.0118 262 LEU D O   
16285 C CB  . LEU D 270 ? 0.2499 0.2243 0.3452 0.0038  -0.0449 -0.0207 262 LEU D CB  
16286 C CG  . LEU D 270 ? 0.2595 0.2399 0.3468 -0.0029 -0.0403 -0.0184 262 LEU D CG  
16287 C CD1 . LEU D 270 ? 0.3094 0.3056 0.3952 -0.0009 -0.0460 -0.0231 262 LEU D CD1 
16288 C CD2 . LEU D 270 ? 0.2501 0.2145 0.3210 -0.0025 -0.0360 -0.0075 262 LEU D CD2 
16289 N N   . GLY D 271 ? 0.2867 0.2354 0.3977 0.0148  -0.0484 -0.0296 263 GLY D N   
16290 C CA  . GLY D 271 ? 0.2633 0.2069 0.3799 0.0271  -0.0522 -0.0341 263 GLY D CA  
16291 C C   . GLY D 271 ? 0.2490 0.2183 0.3760 0.0333  -0.0524 -0.0410 263 GLY D C   
16292 O O   . GLY D 271 ? 0.2356 0.2224 0.3632 0.0304  -0.0540 -0.0384 263 GLY D O   
16293 N N   . ALA D 272 ? 0.2546 0.2259 0.3902 0.0417  -0.0499 -0.0501 264 ALA D N   
16294 C CA  . ALA D 272 ? 0.2415 0.2401 0.3911 0.0462  -0.0464 -0.0560 264 ALA D CA  
16295 C C   . ALA D 272 ? 0.2543 0.2684 0.4170 0.0537  -0.0542 -0.0504 264 ALA D C   
16296 O O   . ALA D 272 ? 0.2329 0.2711 0.4060 0.0501  -0.0548 -0.0504 264 ALA D O   
16297 C CB  . ALA D 272 ? 0.2595 0.2555 0.4141 0.0559  -0.0395 -0.0665 264 ALA D CB  
16298 N N   . ASP D 273 ? 0.2601 0.2594 0.4229 0.0641  -0.0617 -0.0452 265 ASP D N   
16299 C CA  . ASP D 273 ? 0.2636 0.2765 0.4383 0.0724  -0.0727 -0.0398 265 ASP D CA  
16300 C C   . ASP D 273 ? 0.2565 0.2735 0.4176 0.0627  -0.0795 -0.0329 265 ASP D C   
16301 O O   . ASP D 273 ? 0.2496 0.2878 0.4227 0.0633  -0.0873 -0.0329 265 ASP D O   
16302 C CB  . ASP D 273 ? 0.3954 0.3867 0.5685 0.0860  -0.0809 -0.0341 265 ASP D CB  
16303 C CG  . ASP D 273 ? 0.4085 0.4006 0.6009 0.1003  -0.0760 -0.0424 265 ASP D CG  
16304 O OD1 . ASP D 273 ? 0.3886 0.3966 0.5915 0.0990  -0.0645 -0.0525 265 ASP D OD1 
16305 O OD2 . ASP D 273 ? 0.3989 0.3742 0.5942 0.1136  -0.0831 -0.0385 265 ASP D OD2 
16306 N N   . GLU D 274 ? 0.2607 0.2574 0.3980 0.0537  -0.0765 -0.0277 266 GLU D N   
16307 C CA  . GLU D 274 ? 0.2594 0.2565 0.3796 0.0461  -0.0804 -0.0221 266 GLU D CA  
16308 C C   . GLU D 274 ? 0.2510 0.2706 0.3790 0.0365  -0.0767 -0.0287 266 GLU D C   
16309 O O   . GLU D 274 ? 0.2346 0.2626 0.3581 0.0340  -0.0843 -0.0277 266 GLU D O   
16310 C CB  . GLU D 274 ? 0.3003 0.2725 0.3975 0.0394  -0.0740 -0.0145 266 GLU D CB  
16311 C CG  . GLU D 274 ? 0.2751 0.2460 0.3517 0.0326  -0.0738 -0.0097 266 GLU D CG  
16312 C CD  . GLU D 274 ? 0.2944 0.2627 0.3565 0.0404  -0.0873 -0.0043 266 GLU D CD  
16313 O OE1 . GLU D 274 ? 0.3284 0.2904 0.3939 0.0513  -0.0966 -0.0005 266 GLU D OE1 
16314 O OE2 . GLU D 274 ? 0.2975 0.2681 0.3431 0.0365  -0.0897 -0.0043 266 GLU D OE2 
16315 N N   . ILE D 275 ? 0.2394 0.2660 0.3765 0.0309  -0.0663 -0.0354 267 ILE D N   
16316 C CA  . ILE D 275 ? 0.2028 0.2492 0.3481 0.0224  -0.0627 -0.0403 267 ILE D CA  
16317 C C   . ILE D 275 ? 0.2685 0.3390 0.4370 0.0269  -0.0688 -0.0430 267 ILE D C   
16318 O O   . ILE D 275 ? 0.1870 0.2704 0.3601 0.0206  -0.0737 -0.0435 267 ILE D O   
16319 C CB  . ILE D 275 ? 0.1883 0.2348 0.3352 0.0170  -0.0514 -0.0459 267 ILE D CB  
16320 C CG1 . ILE D 275 ? 0.2337 0.2613 0.3636 0.0096  -0.0480 -0.0430 267 ILE D CG1 
16321 C CG2 . ILE D 275 ? 0.1723 0.2391 0.3291 0.0099  -0.0474 -0.0496 267 ILE D CG2 
16322 C CD1 . ILE D 275 ? 0.2180 0.2409 0.3471 0.0054  -0.0413 -0.0485 267 ILE D CD1 
16323 N N   . GLU D 276 ? 0.2264 0.3032 0.4126 0.0379  -0.0688 -0.0449 268 GLU D N   
16324 C CA  . GLU D 276 ? 0.2359 0.3390 0.4520 0.0434  -0.0744 -0.0464 268 GLU D CA  
16325 C C   . GLU D 276 ? 0.2125 0.3174 0.4269 0.0444  -0.0926 -0.0416 268 GLU D C   
16326 O O   . GLU D 276 ? 0.2189 0.3438 0.4502 0.0390  -0.0995 -0.0430 268 GLU D O   
16327 C CB  . GLU D 276 ? 0.2080 0.3140 0.4423 0.0581  -0.0708 -0.0488 268 GLU D CB  
16328 C CG  . GLU D 276 ? 0.4524 0.5891 0.7256 0.0661  -0.0753 -0.0498 268 GLU D CG  
16329 C CD  . GLU D 276 ? 0.5590 0.6952 0.8492 0.0838  -0.0719 -0.0521 268 GLU D CD  
16330 O OE1 . GLU D 276 ? 0.5890 0.7047 0.8686 0.0936  -0.0825 -0.0479 268 GLU D OE1 
16331 O OE2 . GLU D 276 ? 0.6077 0.7622 0.9202 0.0885  -0.0575 -0.0577 268 GLU D OE2 
16332 N N   . ALA D 277 ? 0.2269 0.3084 0.4186 0.0505  -0.1011 -0.0356 269 ALA D N   
16333 C CA  . ALA D 277 ? 0.2436 0.3211 0.4234 0.0522  -0.1194 -0.0309 269 ALA D CA  
16334 C C   . ALA D 277 ? 0.2386 0.3136 0.3992 0.0394  -0.1201 -0.0324 269 ALA D C   
16335 O O   . ALA D 277 ? 0.2796 0.3605 0.4392 0.0379  -0.1355 -0.0331 269 ALA D O   
16336 C CB  . ALA D 277 ? 0.2713 0.3196 0.4235 0.0610  -0.1251 -0.0223 269 ALA D CB  
16337 N N   . THR D 278 ? 0.2268 0.2921 0.3726 0.0306  -0.1051 -0.0336 270 THR D N   
16338 C CA  . THR D 278 ? 0.2244 0.2848 0.3520 0.0203  -0.1042 -0.0353 270 THR D CA  
16339 C C   . THR D 278 ? 0.2275 0.3110 0.3794 0.0121  -0.1060 -0.0416 270 THR D C   
16340 O O   . THR D 278 ? 0.2163 0.2987 0.3598 0.0065  -0.1150 -0.0440 270 THR D O   
16341 C CB  . THR D 278 ? 0.2177 0.2628 0.3282 0.0146  -0.0883 -0.0338 270 THR D CB  
16342 O OG1 . THR D 278 ? 0.3127 0.3353 0.4015 0.0204  -0.0873 -0.0263 270 THR D OG1 
16343 C CG2 . THR D 278 ? 0.2413 0.2830 0.3375 0.0054  -0.0852 -0.0362 270 THR D CG2 
16344 N N   . ARG D 279 ? 0.1929 0.2956 0.3738 0.0115  -0.0971 -0.0443 271 ARG D N   
16345 C CA  . ARG D 279 ? 0.1777 0.3040 0.3862 0.0038  -0.0978 -0.0480 271 ARG D CA  
16346 C C   . ARG D 279 ? 0.2138 0.3535 0.4404 0.0058  -0.1175 -0.0484 271 ARG D C   
16347 O O   . ARG D 279 ? 0.2188 0.3656 0.4532 -0.0036 -0.1256 -0.0512 271 ARG D O   
16348 C CB  . ARG D 279 ? 0.2254 0.3697 0.4599 0.0055  -0.0831 -0.0494 271 ARG D CB  
16349 C CG  . ARG D 279 ? 0.1540 0.2900 0.3745 -0.0012 -0.0666 -0.0506 271 ARG D CG  
16350 C CD  . ARG D 279 ? 0.1939 0.3462 0.4343 0.0003  -0.0516 -0.0524 271 ARG D CD  
16351 N NE  . ARG D 279 ? 0.2008 0.3477 0.4283 -0.0093 -0.0404 -0.0527 271 ARG D NE  
16352 C CZ  . ARG D 279 ? 0.2227 0.3499 0.4247 -0.0098 -0.0350 -0.0534 271 ARG D CZ  
16353 N NH1 . ARG D 279 ? 0.1495 0.2603 0.3378 -0.0026 -0.0380 -0.0538 271 ARG D NH1 
16354 N NH2 . ARG D 279 ? 0.1774 0.3005 0.3691 -0.0180 -0.0277 -0.0530 271 ARG D NH2 
16355 N N   . LYS D 280 ? 0.2006 0.3430 0.4355 0.0180  -0.1273 -0.0458 272 LYS D N   
16356 C CA  . LYS D 280 ? 0.2144 0.3697 0.4677 0.0210  -0.1498 -0.0459 272 LYS D CA  
16357 C C   . LYS D 280 ? 0.2976 0.4302 0.5135 0.0180  -0.1666 -0.0463 272 LYS D C   
16358 O O   . LYS D 280 ? 0.2711 0.4096 0.4932 0.0119  -0.1810 -0.0492 272 LYS D O   
16359 C CB  . LYS D 280 ? 0.2348 0.3954 0.5037 0.0369  -0.1570 -0.0421 272 LYS D CB  
16360 C CG  . LYS D 280 ? 0.2945 0.4659 0.5787 0.0407  -0.1789 -0.0404 272 LYS D CG  
16361 C CD  . LYS D 280 ? 0.3314 0.5041 0.6277 0.0580  -0.1857 -0.0356 272 LYS D CD  
16362 C CE  . LYS D 280 ? 0.3500 0.5419 0.6813 0.0646  -0.1658 -0.0369 272 LYS D CE  
16363 N NZ  . LYS D 280 ? 0.4111 0.6019 0.7544 0.0826  -0.1715 -0.0327 272 LYS D NZ  
16364 N N   . HIS D 281 ? 0.2865 0.3896 0.4591 0.0220  -0.1615 -0.0427 273 HIS D N   
16365 C CA  . HIS D 281 ? 0.3027 0.3814 0.4335 0.0215  -0.1739 -0.0427 273 HIS D CA  
16366 C C   . HIS D 281 ? 0.3211 0.3985 0.4458 0.0087  -0.1729 -0.0498 273 HIS D C   
16367 O O   . HIS D 281 ? 0.2981 0.3683 0.4090 0.0064  -0.1914 -0.0543 273 HIS D O   
16368 C CB  . HIS D 281 ? 0.3156 0.3656 0.4059 0.0272  -0.1620 -0.0359 273 HIS D CB  
16369 C CG  . HIS D 281 ? 0.4520 0.4749 0.4940 0.0276  -0.1683 -0.0351 273 HIS D CG  
16370 N ND1 . HIS D 281 ? 0.4979 0.5110 0.5191 0.0337  -0.1916 -0.0348 273 HIS D ND1 
16371 C CD2 . HIS D 281 ? 0.4912 0.4942 0.5003 0.0238  -0.1536 -0.0346 273 HIS D CD2 
16372 C CE1 . HIS D 281 ? 0.5714 0.5574 0.5441 0.0337  -0.1899 -0.0347 273 HIS D CE1 
16373 N NE2 . HIS D 281 ? 0.5359 0.5167 0.5027 0.0280  -0.1657 -0.0344 273 HIS D NE2 
16374 N N   . LEU D 282 ? 0.2844 0.3668 0.4185 0.0007  -0.1531 -0.0514 274 LEU D N   
16375 C CA  . LEU D 282 ? 0.2985 0.3773 0.4279 -0.0107 -0.1508 -0.0572 274 LEU D CA  
16376 C C   . LEU D 282 ? 0.2926 0.3972 0.4649 -0.0203 -0.1553 -0.0609 274 LEU D C   
16377 O O   . LEU D 282 ? 0.2792 0.3789 0.4485 -0.0302 -0.1504 -0.0638 274 LEU D O   
16378 C CB  . LEU D 282 ? 0.2647 0.3332 0.3804 -0.0140 -0.1285 -0.0557 274 LEU D CB  
16379 C CG  . LEU D 282 ? 0.2870 0.3322 0.3664 -0.0067 -0.1202 -0.0508 274 LEU D CG  
16380 C CD1 . LEU D 282 ? 0.2272 0.2668 0.3021 -0.0114 -0.1006 -0.0498 274 LEU D CD1 
16381 C CD2 . LEU D 282 ? 0.3111 0.3347 0.3532 -0.0034 -0.1321 -0.0528 274 LEU D CD2 
16382 N N   . GLY D 283 ? 0.2516 0.3790 0.4570 -0.0166 -0.1563 -0.0574 275 GLY D N   
16383 C CA  . GLY D 283 ? 0.2698 0.4184 0.5084 -0.0250 -0.1503 -0.0561 275 GLY D CA  
16384 C C   . GLY D 283 ? 0.3083 0.4623 0.5558 -0.0337 -0.1297 -0.0551 275 GLY D C   
16385 O O   . GLY D 283 ? 0.2819 0.4389 0.5376 -0.0443 -0.1265 -0.0547 275 GLY D O   
16386 N N   . TRP D 284 ? 0.2076 0.3607 0.4520 -0.0292 -0.1167 -0.0546 276 TRP D N   
16387 C CA  . TRP D 284 ? 0.2479 0.4033 0.4957 -0.0361 -0.0980 -0.0535 276 TRP D CA  
16388 C C   . TRP D 284 ? 0.2940 0.4744 0.5743 -0.0338 -0.0856 -0.0506 276 TRP D C   
16389 O O   . TRP D 284 ? 0.2740 0.4606 0.5616 -0.0236 -0.0810 -0.0515 276 TRP D O   
16390 C CB  . TRP D 284 ? 0.2301 0.3659 0.4485 -0.0325 -0.0890 -0.0539 276 TRP D CB  
16391 C CG  . TRP D 284 ? 0.2343 0.3695 0.4513 -0.0385 -0.0722 -0.0525 276 TRP D CG  
16392 C CD1 . TRP D 284 ? 0.2470 0.3873 0.4671 -0.0346 -0.0580 -0.0509 276 TRP D CD1 
16393 C CD2 . TRP D 284 ? 0.2155 0.3415 0.4245 -0.0485 -0.0694 -0.0526 276 TRP D CD2 
16394 N NE1 . TRP D 284 ? 0.2437 0.3790 0.4563 -0.0419 -0.0476 -0.0494 276 TRP D NE1 
16395 C CE2 . TRP D 284 ? 0.2471 0.3743 0.4547 -0.0503 -0.0542 -0.0498 276 TRP D CE2 
16396 C CE3 . TRP D 284 ? 0.2079 0.3216 0.4068 -0.0548 -0.0782 -0.0546 276 TRP D CE3 
16397 C CZ2 . TRP D 284 ? 0.1762 0.2947 0.3765 -0.0585 -0.0490 -0.0479 276 TRP D CZ2 
16398 C CZ3 . TRP D 284 ? 0.2226 0.3264 0.4139 -0.0622 -0.0711 -0.0529 276 TRP D CZ3 
16399 C CH2 . TRP D 284 ? 0.2089 0.3164 0.4038 -0.0644 -0.0577 -0.0494 276 TRP D CH2 
16400 N N   . ALA D 285 ? 0.2572 0.4506 0.5561 -0.0428 -0.0792 -0.0472 277 ALA D N   
16401 C CA  . ALA D 285 ? 0.2180 0.4379 0.5508 -0.0406 -0.0674 -0.0439 277 ALA D CA  
16402 C C   . ALA D 285 ? 0.2079 0.4323 0.5420 -0.0409 -0.0460 -0.0434 277 ALA D C   
16403 O O   . ALA D 285 ? 0.2779 0.5238 0.6377 -0.0387 -0.0321 -0.0408 277 ALA D O   
16404 C CB  . ALA D 285 ? 0.2177 0.4515 0.5729 -0.0509 -0.0701 -0.0399 277 ALA D CB  
16405 N N   . TYR D 286 ? 0.2234 0.4284 0.5304 -0.0430 -0.0423 -0.0460 278 TYR D N   
16406 C CA  . TYR D 286 ? 0.1392 0.3428 0.4368 -0.0447 -0.0225 -0.0436 278 TYR D CA  
16407 C C   . TYR D 286 ? 0.1658 0.3555 0.4379 -0.0328 -0.0153 -0.0467 278 TYR D C   
16408 O O   . TYR D 286 ? 0.1620 0.3335 0.4127 -0.0282 -0.0248 -0.0492 278 TYR D O   
16409 C CB  . TYR D 286 ? 0.2030 0.3894 0.4806 -0.0564 -0.0219 -0.0411 278 TYR D CB  
16410 C CG  . TYR D 286 ? 0.2567 0.4459 0.5481 -0.0673 -0.0313 -0.0380 278 TYR D CG  
16411 C CD1 . TYR D 286 ? 0.2661 0.4737 0.5833 -0.0741 -0.0234 -0.0318 278 TYR D CD1 
16412 C CD2 . TYR D 286 ? 0.2442 0.4133 0.5151 -0.0695 -0.0466 -0.0404 278 TYR D CD2 
16413 C CE1 . TYR D 286 ? 0.2985 0.5042 0.6221 -0.0839 -0.0325 -0.0289 278 TYR D CE1 
16414 C CE2 . TYR D 286 ? 0.2857 0.4518 0.5608 -0.0781 -0.0551 -0.0387 278 TYR D CE2 
16415 C CZ  . TYR D 286 ? 0.3272 0.5113 0.6292 -0.0858 -0.0490 -0.0332 278 TYR D CZ  
16416 O OH  . TYR D 286 ? 0.3948 0.5752 0.7028 -0.0953 -0.0581 -0.0327 278 TYR D OH  
16417 N N   . PRO D 287 ? 0.1400 0.3365 0.4131 -0.0280 0.0019  -0.0466 279 PRO D N   
16418 C CA  . PRO D 287 ? 0.1596 0.3401 0.4078 -0.0171 0.0075  -0.0512 279 PRO D CA  
16419 C C   . PRO D 287 ? 0.2008 0.3551 0.4133 -0.0220 0.0049  -0.0515 279 PRO D C   
16420 O O   . PRO D 287 ? 0.2310 0.3805 0.4372 -0.0325 0.0024  -0.0478 279 PRO D O   
16421 C CB  . PRO D 287 ? 0.1806 0.3739 0.4355 -0.0121 0.0279  -0.0514 279 PRO D CB  
16422 C CG  . PRO D 287 ? 0.2345 0.4559 0.5265 -0.0193 0.0333  -0.0457 279 PRO D CG  
16423 C CD  . PRO D 287 ? 0.2348 0.4522 0.5300 -0.0327 0.0181  -0.0421 279 PRO D CD  
16424 N N   . ALA D 288 ? 0.1910 0.3282 0.3828 -0.0141 0.0048  -0.0561 280 ALA D N   
16425 C CA  . ALA D 288 ? 0.2051 0.3194 0.3688 -0.0181 0.0005  -0.0566 280 ALA D CA  
16426 C C   . ALA D 288 ? 0.1864 0.2979 0.3365 -0.0259 0.0077  -0.0536 280 ALA D C   
16427 O O   . ALA D 288 ? 0.1965 0.3140 0.3436 -0.0238 0.0205  -0.0536 280 ALA D O   
16428 C CB  . ALA D 288 ? 0.2032 0.3007 0.3507 -0.0092 0.0005  -0.0625 280 ALA D CB  
16429 N N   . PHE D 289 ? 0.1571 0.2585 0.2981 -0.0338 0.0002  -0.0503 281 PHE D N   
16430 C CA  . PHE D 289 ? 0.2260 0.3195 0.3514 -0.0407 0.0032  -0.0463 281 PHE D CA  
16431 C C   . PHE D 289 ? 0.2396 0.3467 0.3775 -0.0474 0.0119  -0.0401 281 PHE D C   
16432 O O   . PHE D 289 ? 0.2853 0.3853 0.4084 -0.0523 0.0168  -0.0351 281 PHE D O   
16433 C CB  . PHE D 289 ? 0.2195 0.2990 0.3186 -0.0362 0.0070  -0.0497 281 PHE D CB  
16434 C CG  . PHE D 289 ? 0.2411 0.3056 0.3310 -0.0320 -0.0028 -0.0553 281 PHE D CG  
16435 C CD1 . PHE D 289 ? 0.2581 0.3118 0.3435 -0.0368 -0.0132 -0.0534 281 PHE D CD1 
16436 C CD2 . PHE D 289 ? 0.2175 0.2789 0.3066 -0.0232 -0.0011 -0.0619 281 PHE D CD2 
16437 C CE1 . PHE D 289 ? 0.2458 0.2877 0.3283 -0.0345 -0.0212 -0.0571 281 PHE D CE1 
16438 C CE2 . PHE D 289 ? 0.2048 0.2507 0.2879 -0.0210 -0.0102 -0.0661 281 PHE D CE2 
16439 C CZ  . PHE D 289 ? 0.2604 0.2976 0.3414 -0.0276 -0.0200 -0.0632 281 PHE D CZ  
16440 N N   . GLU D 290 ? 0.1749 0.3007 0.3407 -0.0482 0.0129  -0.0395 282 GLU D N   
16441 C CA  . GLU D 290 ? 0.1617 0.3019 0.3473 -0.0570 0.0196  -0.0330 282 GLU D CA  
16442 C C   . GLU D 290 ? 0.2695 0.4089 0.4693 -0.0647 0.0059  -0.0321 282 GLU D C   
16443 O O   . GLU D 290 ? 0.2354 0.3788 0.4461 -0.0612 -0.0048 -0.0366 282 GLU D O   
16444 C CB  . GLU D 290 ? 0.1966 0.3613 0.4090 -0.0526 0.0309  -0.0330 282 GLU D CB  
16445 C CG  . GLU D 290 ? 0.3760 0.5395 0.5704 -0.0454 0.0486  -0.0335 282 GLU D CG  
16446 C CD  . GLU D 290 ? 0.4942 0.6829 0.7167 -0.0385 0.0628  -0.0342 282 GLU D CD  
16447 O OE1 . GLU D 290 ? 0.5106 0.7224 0.7724 -0.0435 0.0612  -0.0308 282 GLU D OE1 
16448 O OE2 . GLU D 290 ? 0.4979 0.6830 0.7040 -0.0275 0.0751  -0.0388 282 GLU D OE2 
16449 N N   . ILE D 291 ? 0.2679 0.3988 0.4640 -0.0745 0.0055  -0.0265 283 ILE D N   
16450 C CA  . ILE D 291 ? 0.1847 0.3085 0.3883 -0.0815 -0.0073 -0.0270 283 ILE D CA  
16451 C C   . ILE D 291 ? 0.2108 0.3419 0.4351 -0.0936 -0.0032 -0.0201 283 ILE D C   
16452 O O   . ILE D 291 ? 0.2275 0.3532 0.4427 -0.0983 0.0074  -0.0123 283 ILE D O   
16453 C CB  . ILE D 291 ? 0.1902 0.2905 0.3685 -0.0807 -0.0137 -0.0275 283 ILE D CB  
16454 C CG1 . ILE D 291 ? 0.1609 0.2553 0.3236 -0.0706 -0.0169 -0.0331 283 ILE D CG1 
16455 C CG2 . ILE D 291 ? 0.2344 0.3252 0.4184 -0.0865 -0.0248 -0.0292 283 ILE D CG2 
16456 C CD1 . ILE D 291 ? 0.1481 0.2243 0.2910 -0.0693 -0.0202 -0.0323 283 ILE D CD1 
16457 N N   . PRO D 292 ? 0.2134 0.3551 0.4651 -0.0997 -0.0123 -0.0220 284 PRO D N   
16458 C CA  . PRO D 292 ? 0.2085 0.3550 0.4773 -0.1114 -0.0088 -0.0141 284 PRO D CA  
16459 C C   . PRO D 292 ? 0.2382 0.3598 0.4908 -0.1193 -0.0113 -0.0101 284 PRO D C   
16460 O O   . PRO D 292 ? 0.2434 0.3449 0.4745 -0.1151 -0.0205 -0.0150 284 PRO D O   
16461 C CB  . PRO D 292 ? 0.1893 0.3424 0.4696 -0.1109 -0.0228 -0.0185 284 PRO D CB  
16462 C CG  . PRO D 292 ? 0.1924 0.3314 0.4509 -0.1015 -0.0359 -0.0273 284 PRO D CG  
16463 C CD  . PRO D 292 ? 0.1859 0.3269 0.4357 -0.0931 -0.0274 -0.0290 284 PRO D CD  
16464 N N   . GLN D 293 ? 0.2432 0.3663 0.5073 -0.1303 -0.0022 -0.0002 285 GLN D N   
16465 C CA  . GLN D 293 ? 0.2864 0.3841 0.5363 -0.1376 -0.0033 0.0058  285 GLN D CA  
16466 C C   . GLN D 293 ? 0.2212 0.2984 0.4608 -0.1374 -0.0203 -0.0023 285 GLN D C   
16467 O O   . GLN D 293 ? 0.2545 0.3074 0.4767 -0.1369 -0.0248 -0.0020 285 GLN D O   
16468 C CB  . GLN D 293 ? 0.3404 0.4422 0.6040 -0.1497 0.0108  0.0193  285 GLN D CB  
16469 C CG  . GLN D 293 ? 0.3541 0.4273 0.6012 -0.1566 0.0112  0.0288  285 GLN D CG  
16470 C CD  . GLN D 293 ? 0.4300 0.4892 0.6410 -0.1464 0.0152  0.0315  285 GLN D CD  
16471 O OE1 . GLN D 293 ? 0.4948 0.5647 0.6927 -0.1407 0.0290  0.0351  285 GLN D OE1 
16472 N NE2 . GLN D 293 ? 0.4405 0.4749 0.6318 -0.1421 0.0027  0.0282  285 GLN D NE2 
16473 N N   . GLU D 294 ? 0.2230 0.3089 0.4734 -0.1373 -0.0297 -0.0093 286 GLU D N   
16474 C CA  . GLU D 294 ? 0.2873 0.3525 0.5265 -0.1369 -0.0445 -0.0176 286 GLU D CA  
16475 C C   . GLU D 294 ? 0.2773 0.3269 0.4910 -0.1255 -0.0509 -0.0252 286 GLU D C   
16476 O O   . GLU D 294 ? 0.2738 0.2999 0.4734 -0.1244 -0.0577 -0.0295 286 GLU D O   
16477 C CB  . GLU D 294 ? 0.3716 0.4493 0.6264 -0.1386 -0.0548 -0.0234 286 GLU D CB  
16478 C CG  . GLU D 294 ? 0.4684 0.5721 0.7345 -0.1313 -0.0540 -0.0250 286 GLU D CG  
16479 C CD  . GLU D 294 ? 0.5694 0.7007 0.8663 -0.1373 -0.0421 -0.0166 286 GLU D CD  
16480 O OE1 . GLU D 294 ? 0.5934 0.7233 0.8974 -0.1465 -0.0303 -0.0077 286 GLU D OE1 
16481 O OE2 . GLU D 294 ? 0.5975 0.7513 0.9117 -0.1324 -0.0438 -0.0183 286 GLU D OE2 
16482 N N   . ILE D 295 ? 0.2999 0.3620 0.5093 -0.1166 -0.0480 -0.0272 287 ILE D N   
16483 C CA  . ILE D 295 ? 0.2616 0.3107 0.4497 -0.1064 -0.0524 -0.0336 287 ILE D CA  
16484 C C   . ILE D 295 ? 0.1981 0.2327 0.3760 -0.1059 -0.0472 -0.0292 287 ILE D C   
16485 O O   . ILE D 295 ? 0.2029 0.2190 0.3671 -0.1011 -0.0519 -0.0333 287 ILE D O   
16486 C CB  . ILE D 295 ? 0.2550 0.3203 0.4433 -0.0977 -0.0517 -0.0368 287 ILE D CB  
16487 C CG1 . ILE D 295 ? 0.3005 0.3730 0.4944 -0.0960 -0.0619 -0.0422 287 ILE D CG1 
16488 C CG2 . ILE D 295 ? 0.2364 0.2906 0.4063 -0.0888 -0.0520 -0.0408 287 ILE D CG2 
16489 C CD1 . ILE D 295 ? 0.3238 0.4085 0.5174 -0.0866 -0.0630 -0.0451 287 ILE D CD1 
16490 N N   . TYR D 296 ? 0.1953 0.2377 0.3810 -0.1109 -0.0377 -0.0203 288 TYR D N   
16491 C CA  . TYR D 296 ? 0.2029 0.2289 0.3743 -0.1102 -0.0344 -0.0136 288 TYR D CA  
16492 C C   . TYR D 296 ? 0.2481 0.2510 0.4206 -0.1164 -0.0409 -0.0118 288 TYR D C   
16493 O O   . TYR D 296 ? 0.2821 0.2666 0.4404 -0.1102 -0.0444 -0.0123 288 TYR D O   
16494 C CB  . TYR D 296 ? 0.2508 0.2854 0.4190 -0.1132 -0.0216 -0.0029 288 TYR D CB  
16495 C CG  . TYR D 296 ? 0.2195 0.2646 0.3737 -0.1036 -0.0158 -0.0048 288 TYR D CG  
16496 C CD1 . TYR D 296 ? 0.1931 0.2295 0.3308 -0.0942 -0.0214 -0.0094 288 TYR D CD1 
16497 C CD2 . TYR D 296 ? 0.2504 0.3136 0.4096 -0.1040 -0.0042 -0.0022 288 TYR D CD2 
16498 C CE1 . TYR D 296 ? 0.1923 0.2354 0.3182 -0.0869 -0.0180 -0.0117 288 TYR D CE1 
16499 C CE2 . TYR D 296 ? 0.2261 0.2947 0.3703 -0.0947 0.0003  -0.0054 288 TYR D CE2 
16500 C CZ  . TYR D 296 ? 0.2118 0.2691 0.3389 -0.0869 -0.0077 -0.0103 288 TYR D CZ  
16501 O OH  . TYR D 296 ? 0.2104 0.2702 0.3236 -0.0792 -0.0051 -0.0140 288 TYR D OH  
16502 N N   . ASP D 297 ? 0.3050 0.3086 0.4890 -0.1252 -0.0407 -0.0099 289 ASP D N   
16503 C CA  . ASP D 297 ? 0.2979 0.2771 0.4792 -0.1298 -0.0459 -0.0088 289 ASP D CA  
16504 C C   . ASP D 297 ? 0.2837 0.2469 0.4530 -0.1213 -0.0564 -0.0212 289 ASP D C   
16505 O O   . ASP D 297 ? 0.3278 0.2667 0.4890 -0.1189 -0.0604 -0.0216 289 ASP D O   
16506 C CB  . ASP D 297 ? 0.2746 0.2596 0.4730 -0.1416 -0.0441 -0.0054 289 ASP D CB  
16507 C CG  . ASP D 297 ? 0.3690 0.3640 0.5786 -0.1511 -0.0306 0.0095  289 ASP D CG  
16508 O OD1 . ASP D 297 ? 0.3712 0.3623 0.5707 -0.1493 -0.0245 0.0184  289 ASP D OD1 
16509 O OD2 . ASP D 297 ? 0.3580 0.3647 0.5862 -0.1607 -0.0261 0.0132  289 ASP D OD2 
16510 N N   . ALA D 298 ? 0.2964 0.2713 0.4639 -0.1163 -0.0608 -0.0309 290 ALA D N   
16511 C CA  . ALA D 298 ? 0.2829 0.2416 0.4362 -0.1084 -0.0693 -0.0425 290 ALA D CA  
16512 C C   . ALA D 298 ? 0.2715 0.2214 0.4141 -0.0982 -0.0671 -0.0441 290 ALA D C   
16513 O O   . ALA D 298 ? 0.3324 0.2613 0.4652 -0.0922 -0.0714 -0.0514 290 ALA D O   
16514 C CB  . ALA D 298 ? 0.3380 0.3102 0.4899 -0.1055 -0.0749 -0.0504 290 ALA D CB  
16515 N N   . TRP D 299 ? 0.2621 0.2274 0.4078 -0.0959 -0.0605 -0.0381 291 TRP D N   
16516 C CA  . TRP D 299 ? 0.2872 0.2497 0.4238 -0.0853 -0.0575 -0.0389 291 TRP D CA  
16517 C C   . TRP D 299 ? 0.3247 0.2753 0.4593 -0.0839 -0.0555 -0.0301 291 TRP D C   
16518 O O   . TRP D 299 ? 0.2682 0.2128 0.3977 -0.0740 -0.0548 -0.0312 291 TRP D O   
16519 C CB  . TRP D 299 ? 0.2128 0.1975 0.3485 -0.0813 -0.0520 -0.0374 291 TRP D CB  
16520 C CG  . TRP D 299 ? 0.1946 0.1845 0.3239 -0.0742 -0.0531 -0.0458 291 TRP D CG  
16521 C CD1 . TRP D 299 ? 0.2634 0.2664 0.3958 -0.0755 -0.0554 -0.0493 291 TRP D CD1 
16522 C CD2 . TRP D 299 ? 0.2307 0.2128 0.3496 -0.0640 -0.0509 -0.0502 291 TRP D CD2 
16523 N NE1 . TRP D 299 ? 0.2348 0.2357 0.3551 -0.0670 -0.0557 -0.0550 291 TRP D NE1 
16524 C CE2 . TRP D 299 ? 0.2519 0.2405 0.3638 -0.0602 -0.0515 -0.0555 291 TRP D CE2 
16525 C CE3 . TRP D 299 ? 0.2429 0.2137 0.3596 -0.0571 -0.0479 -0.0495 291 TRP D CE3 
16526 C CZ2 . TRP D 299 ? 0.2292 0.2124 0.3291 -0.0507 -0.0471 -0.0592 291 TRP D CZ2 
16527 C CZ3 . TRP D 299 ? 0.2609 0.2297 0.3707 -0.0474 -0.0429 -0.0539 291 TRP D CZ3 
16528 C CH2 . TRP D 299 ? 0.2481 0.2224 0.3482 -0.0448 -0.0416 -0.0584 291 TRP D CH2 
16529 N N   . ASN D 300 ? 0.2681 0.2153 0.4075 -0.0934 -0.0545 -0.0204 292 ASN D N   
16530 C CA  . ASN D 300 ? 0.2511 0.1880 0.3842 -0.0917 -0.0532 -0.0096 292 ASN D CA  
16531 C C   . ASN D 300 ? 0.2689 0.1811 0.4005 -0.0855 -0.0589 -0.0114 292 ASN D C   
16532 O O   . ASN D 300 ? 0.2855 0.1806 0.4210 -0.0894 -0.0632 -0.0162 292 ASN D O   
16533 C CB  . ASN D 300 ? 0.2783 0.2140 0.4136 -0.1037 -0.0491 0.0025  292 ASN D CB  
16534 C CG  . ASN D 300 ? 0.3720 0.2987 0.4935 -0.1010 -0.0478 0.0150  292 ASN D CG  
16535 O OD1 . ASN D 300 ? 0.3762 0.2807 0.4945 -0.0991 -0.0530 0.0201  292 ASN D OD1 
16536 N ND2 . ASN D 300 ? 0.4048 0.3463 0.5158 -0.0997 -0.0421 0.0193  292 ASN D ND2 
16537 N N   . ALA D 301 ? 0.2679 0.1778 0.3957 -0.0754 -0.0598 -0.0080 293 ALA D N   
16538 C CA  . ALA D 301 ? 0.2843 0.1736 0.4143 -0.0663 -0.0641 -0.0095 293 ALA D CA  
16539 C C   . ALA D 301 ? 0.3269 0.1996 0.4540 -0.0665 -0.0687 0.0040  293 ALA D C   
16540 O O   . ALA D 301 ? 0.3181 0.1762 0.4495 -0.0564 -0.0731 0.0045  293 ALA D O   
16541 C CB  . ALA D 301 ? 0.2698 0.1702 0.4041 -0.0529 -0.0622 -0.0161 293 ALA D CB  
16542 N N   . LYS D 302 ? 0.2916 0.2096 0.3945 -0.1237 0.0069  -0.0011 294 LYS D N   
16543 C CA  . LYS D 302 ? 0.3498 0.2590 0.4484 -0.1272 0.0105  0.0092  294 LYS D CA  
16544 C C   . LYS D 302 ? 0.3080 0.2039 0.4084 -0.1293 0.0102  0.0104  294 LYS D C   
16545 O O   . LYS D 302 ? 0.3190 0.2026 0.4145 -0.1274 0.0111  0.0162  294 LYS D O   
16546 C CB  . LYS D 302 ? 0.4059 0.3253 0.5069 -0.1330 0.0151  0.0145  294 LYS D CB  
16547 C CG  . LYS D 302 ? 0.5258 0.4567 0.6231 -0.1306 0.0174  0.0143  294 LYS D CG  
16548 C CD  . LYS D 302 ? 0.6257 0.5565 0.7155 -0.1330 0.0225  0.0243  294 LYS D CD  
16549 C CE  . LYS D 302 ? 0.6088 0.5513 0.6900 -0.1315 0.0242  0.0228  294 LYS D CE  
16550 N NZ  . LYS D 302 ? 0.6285 0.5858 0.7175 -0.1325 0.0255  0.0141  294 LYS D NZ  
16551 N N   . GLU D 303 ? 0.2945 0.1929 0.4028 -0.1327 0.0092  0.0047  295 GLU D N   
16552 C CA  . GLU D 303 ? 0.3099 0.1961 0.4210 -0.1354 0.0094  0.0056  295 GLU D CA  
16553 C C   . GLU D 303 ? 0.3111 0.1868 0.4206 -0.1291 0.0060  0.0010  295 GLU D C   
16554 O O   . GLU D 303 ? 0.3227 0.1851 0.4309 -0.1283 0.0068  0.0054  295 GLU D O   
16555 C CB  . GLU D 303 ? 0.3141 0.2066 0.4347 -0.1408 0.0092  0.0003  295 GLU D CB  
16556 C CG  . GLU D 303 ? 0.3301 0.2099 0.4546 -0.1434 0.0091  -0.0003 295 GLU D CG  
16557 C CD  . GLU D 303 ? 0.3366 0.2222 0.4707 -0.1501 0.0098  -0.0039 295 GLU D CD  
16558 O OE1 . GLU D 303 ? 0.3564 0.2565 0.4949 -0.1516 0.0096  -0.0077 295 GLU D OE1 
16559 O OE2 . GLU D 303 ? 0.3513 0.2267 0.4890 -0.1535 0.0105  -0.0030 295 GLU D OE2 
16560 N N   . LYS D 304 ? 0.3139 0.1959 0.4236 -0.1244 0.0023  -0.0076 296 LYS D N   
16561 C CA  . LYS D 304 ? 0.3005 0.1742 0.4084 -0.1185 -0.0008 -0.0125 296 LYS D CA  
16562 C C   . LYS D 304 ? 0.2992 0.1651 0.4002 -0.1132 -0.0003 -0.0060 296 LYS D C   
16563 O O   . LYS D 304 ? 0.3071 0.1615 0.4078 -0.1100 -0.0009 -0.0054 296 LYS D O   
16564 C CB  . LYS D 304 ? 0.4304 0.3143 0.5387 -0.1151 -0.0048 -0.0225 296 LYS D CB  
16565 C CG  . LYS D 304 ? 0.5021 0.3796 0.6081 -0.1096 -0.0078 -0.0287 296 LYS D CG  
16566 C CD  . LYS D 304 ? 0.5025 0.3912 0.6078 -0.1072 -0.0117 -0.0378 296 LYS D CD  
16567 C CE  . LYS D 304 ? 0.5331 0.4167 0.6346 -0.1018 -0.0143 -0.0438 296 LYS D CE  
16568 N NZ  . LYS D 304 ? 0.5657 0.4605 0.6652 -0.0998 -0.0182 -0.0519 296 LYS D NZ  
16569 N N   . GLY D 305 ? 0.2929 0.1653 0.3892 -0.1123 0.0009  -0.0011 297 GLY D N   
16570 C CA  . GLY D 305 ? 0.3174 0.1838 0.4074 -0.1074 0.0010  0.0057  297 GLY D CA  
16571 C C   . GLY D 305 ? 0.3078 0.1635 0.3968 -0.1094 0.0040  0.0157  297 GLY D C   
16572 O O   . GLY D 305 ? 0.3389 0.1855 0.4253 -0.1044 0.0029  0.0199  297 GLY D O   
16573 N N   . ALA D 306 ? 0.3107 0.1679 0.4016 -0.1165 0.0075  0.0201  298 ALA D N   
16574 C CA  . ALA D 306 ? 0.3264 0.1732 0.4162 -0.1188 0.0104  0.0297  298 ALA D CA  
16575 C C   . ALA D 306 ? 0.3795 0.2132 0.4743 -0.1171 0.0087  0.0272  298 ALA D C   
16576 O O   . ALA D 306 ? 0.3483 0.1713 0.4418 -0.1140 0.0087  0.0339  298 ALA D O   
16577 C CB  . ALA D 306 ? 0.3653 0.2170 0.4560 -0.1275 0.0150  0.0340  298 ALA D CB  
16578 N N   . LYS D 307 ? 0.3780 0.2130 0.4790 -0.1189 0.0070  0.0175  299 LYS D N   
16579 C CA  . LYS D 307 ? 0.3867 0.2102 0.4932 -0.1174 0.0057  0.0139  299 LYS D CA  
16580 C C   . LYS D 307 ? 0.3466 0.1645 0.4512 -0.1089 0.0028  0.0114  299 LYS D C   
16581 O O   . LYS D 307 ? 0.3585 0.1647 0.4659 -0.1062 0.0026  0.0135  299 LYS D O   
16582 C CB  . LYS D 307 ? 0.4391 0.2673 0.5523 -0.1211 0.0043  0.0035  299 LYS D CB  
16583 C CG  . LYS D 307 ? 0.5542 0.3857 0.6717 -0.1297 0.0069  0.0058  299 LYS D CG  
16584 C CD  . LYS D 307 ? 0.5860 0.4253 0.7102 -0.1326 0.0049  -0.0049 299 LYS D CD  
16585 C CE  . LYS D 307 ? 0.5168 0.3490 0.6447 -0.1288 0.0022  -0.0134 299 LYS D CE  
16586 N NZ  . LYS D 307 ? 0.5063 0.3466 0.6403 -0.1321 0.0003  -0.0233 299 LYS D NZ  
16587 N N   . LEU D 308 ? 0.3309 0.1575 0.4314 -0.1047 0.0007  0.0067  300 LEU D N   
16588 C CA  . LEU D 308 ? 0.3563 0.1791 0.4545 -0.0968 -0.0018 0.0043  300 LEU D CA  
16589 C C   . LEU D 308 ? 0.3316 0.1467 0.4268 -0.0932 -0.0011 0.0151  300 LEU D C   
16590 O O   . LEU D 308 ? 0.3388 0.1446 0.4364 -0.0885 -0.0021 0.0155  300 LEU D O   
16591 C CB  . LEU D 308 ? 0.3089 0.1432 0.4024 -0.0937 -0.0040 -0.0012 300 LEU D CB  
16592 C CG  . LEU D 308 ? 0.3539 0.1863 0.4443 -0.0858 -0.0064 -0.0041 300 LEU D CG  
16593 C CD1 . LEU D 308 ? 0.3456 0.1749 0.4396 -0.0838 -0.0080 -0.0146 300 LEU D CD1 
16594 C CD2 . LEU D 308 ? 0.3477 0.1908 0.4323 -0.0835 -0.0080 -0.0053 300 LEU D CD2 
16595 N N   . GLU D 309 ? 0.3286 0.1483 0.4186 -0.0952 0.0005  0.0241  301 GLU D N   
16596 C CA  . GLU D 309 ? 0.3334 0.1477 0.4196 -0.0915 0.0005  0.0348  301 GLU D CA  
16597 C C   . GLU D 309 ? 0.3524 0.1549 0.4425 -0.0936 0.0021  0.0417  301 GLU D C   
16598 O O   . GLU D 309 ? 0.3595 0.1543 0.4496 -0.0888 0.0008  0.0478  301 GLU D O   
16599 C CB  . GLU D 309 ? 0.3851 0.2088 0.4640 -0.0933 0.0017  0.0424  301 GLU D CB  
16600 C CG  . GLU D 309 ? 0.3859 0.2056 0.4595 -0.0893 0.0008  0.0538  301 GLU D CG  
16601 C CD  . GLU D 309 ? 0.4213 0.2519 0.4865 -0.0893 0.0006  0.0591  301 GLU D CD  
16602 O OE1 . GLU D 309 ? 0.3716 0.2121 0.4357 -0.0913 0.0009  0.0531  301 GLU D OE1 
16603 O OE2 . GLU D 309 ? 0.4065 0.2360 0.4661 -0.0871 -0.0002 0.0691  301 GLU D OE2 
16604 N N   . ALA D 310 ? 0.3613 0.1625 0.4553 -0.1007 0.0046  0.0407  302 ALA D N   
16605 C CA  . ALA D 310 ? 0.4157 0.2049 0.5142 -0.1029 0.0060  0.0466  302 ALA D CA  
16606 C C   . ALA D 310 ? 0.4777 0.2567 0.5834 -0.0980 0.0037  0.0405  302 ALA D C   
16607 O O   . ALA D 310 ? 0.3996 0.1684 0.5079 -0.0948 0.0032  0.0469  302 ALA D O   
16608 C CB  . ALA D 310 ? 0.3885 0.1790 0.4900 -0.1120 0.0092  0.0460  302 ALA D CB  
16609 N N   . GLY D 311 ? 0.3800 0.1624 0.4892 -0.0972 0.0023  0.0281  303 GLY D N   
16610 C CA  . GLY D 311 ? 0.4441 0.2181 0.5599 -0.0926 0.0007  0.0213  303 GLY D CA  
16611 C C   . GLY D 311 ? 0.4266 0.1977 0.5407 -0.0842 -0.0013 0.0241  303 GLY D C   
16612 O O   . GLY D 311 ? 0.3943 0.1554 0.5144 -0.0804 -0.0019 0.0249  303 GLY D O   
16613 N N   . TRP D 312 ? 0.4477 0.2276 0.5544 -0.0811 -0.0025 0.0256  304 TRP D N   
16614 C CA  . TRP D 312 ? 0.4185 0.1968 0.5234 -0.0733 -0.0046 0.0286  304 TRP D CA  
16615 C C   . TRP D 312 ? 0.3759 0.1472 0.4807 -0.0720 -0.0045 0.0419  304 TRP D C   
16616 O O   . TRP D 312 ? 0.4187 0.1833 0.5276 -0.0661 -0.0061 0.0440  304 TRP D O   
16617 C CB  . TRP D 312 ? 0.3458 0.1355 0.4428 -0.0709 -0.0059 0.0272  304 TRP D CB  
16618 C CG  . TRP D 312 ? 0.3414 0.1301 0.4374 -0.0629 -0.0082 0.0286  304 TRP D CG  
16619 C CD1 . TRP D 312 ? 0.3360 0.1252 0.4340 -0.0577 -0.0096 0.0194  304 TRP D CD1 
16620 C CD2 . TRP D 312 ? 0.3433 0.1309 0.4360 -0.0594 -0.0094 0.0400  304 TRP D CD2 
16621 N NE1 . TRP D 312 ? 0.3338 0.1221 0.4308 -0.0511 -0.0114 0.0241  304 TRP D NE1 
16622 C CE2 . TRP D 312 ? 0.3381 0.1257 0.4319 -0.0520 -0.0116 0.0368  304 TRP D CE2 
16623 C CE3 . TRP D 312 ? 0.3494 0.1370 0.4380 -0.0621 -0.0089 0.0524  304 TRP D CE3 
16624 C CZ2 . TRP D 312 ? 0.4451 0.2327 0.5367 -0.0470 -0.0137 0.0456  304 TRP D CZ2 
16625 C CZ3 . TRP D 312 ? 0.3925 0.1804 0.4779 -0.0572 -0.0111 0.0614  304 TRP D CZ3 
16626 C CH2 . TRP D 312 ? 0.4543 0.2422 0.5416 -0.0497 -0.0137 0.0579  304 TRP D CH2 
16627 N N   . ASN D 313 ? 0.3797 0.1531 0.4799 -0.0774 -0.0027 0.0509  305 ASN D N   
16628 C CA  . ASN D 313 ? 0.3927 0.1601 0.4918 -0.0768 -0.0028 0.0641  305 ASN D CA  
16629 C C   . ASN D 313 ? 0.4470 0.2011 0.5557 -0.0762 -0.0026 0.0650  305 ASN D C   
16630 O O   . ASN D 313 ? 0.4207 0.1683 0.5316 -0.0715 -0.0044 0.0725  305 ASN D O   
16631 C CB  . ASN D 313 ? 0.4229 0.1956 0.5154 -0.0839 -0.0001 0.0726  305 ASN D CB  
16632 C CG  . ASN D 313 ? 0.4455 0.2305 0.5283 -0.0831 -0.0006 0.0757  305 ASN D CG  
16633 O OD1 . ASN D 313 ? 0.4969 0.2849 0.5773 -0.0767 -0.0035 0.0750  305 ASN D OD1 
16634 N ND2 . ASN D 313 ? 0.4364 0.2289 0.5139 -0.0897 0.0023  0.0791  305 ASN D ND2 
16635 N N   . GLU D 314 ? 0.4170 0.1671 0.5319 -0.0807 -0.0009 0.0570  306 GLU D N   
16636 C CA  . GLU D 314 ? 0.4812 0.2184 0.6062 -0.0803 -0.0007 0.0568  306 GLU D CA  
16637 C C   . GLU D 314 ? 0.4844 0.2175 0.6158 -0.0721 -0.0030 0.0506  306 GLU D C   
16638 O O   . GLU D 314 ? 0.5016 0.2251 0.6397 -0.0685 -0.0039 0.0557  306 GLU D O   
16639 C CB  . GLU D 314 ? 0.4784 0.2136 0.6086 -0.0873 0.0015  0.0489  306 GLU D CB  
16640 C CG  . GLU D 314 ? 0.6074 0.3289 0.7484 -0.0879 0.0021  0.0490  306 GLU D CG  
16641 C CD  . GLU D 314 ? 0.7168 0.4370 0.8633 -0.0952 0.0040  0.0410  306 GLU D CD  
16642 O OE1 . GLU D 314 ? 0.7348 0.4653 0.8773 -0.0987 0.0044  0.0337  306 GLU D OE1 
16643 O OE2 . GLU D 314 ? 0.7471 0.4562 0.9022 -0.0973 0.0050  0.0422  306 GLU D OE2 
16644 N N   . LEU D 315 ? 0.4939 0.2343 0.6237 -0.0693 -0.0039 0.0396  307 LEU D N   
16645 C CA  . LEU D 315 ? 0.4790 0.2172 0.6140 -0.0616 -0.0056 0.0334  307 LEU D CA  
16646 C C   . LEU D 315 ? 0.4642 0.2021 0.5970 -0.0552 -0.0078 0.0432  307 LEU D C   
16647 O O   . LEU D 315 ? 0.5084 0.2393 0.6490 -0.0498 -0.0090 0.0443  307 LEU D O   
16648 C CB  . LEU D 315 ? 0.4567 0.2044 0.5880 -0.0604 -0.0060 0.0209  307 LEU D CB  
16649 C CG  . LEU D 315 ? 0.3983 0.1452 0.5344 -0.0534 -0.0071 0.0120  307 LEU D CG  
16650 C CD1 . LEU D 315 ? 0.4117 0.1508 0.5579 -0.0546 -0.0058 0.0032  307 LEU D CD1 
16651 C CD2 . LEU D 315 ? 0.3871 0.1455 0.5158 -0.0518 -0.0078 0.0037  307 LEU D CD2 
16652 N N   . PHE D 316 ? 0.4060 0.1522 0.5288 -0.0559 -0.0085 0.0505  308 PHE D N   
16653 C CA  . PHE D 316 ? 0.4050 0.1526 0.5251 -0.0501 -0.0111 0.0601  308 PHE D CA  
16654 C C   . PHE D 316 ? 0.4240 0.1624 0.5480 -0.0503 -0.0116 0.0722  308 PHE D C   
16655 O O   . PHE D 316 ? 0.5052 0.2416 0.6315 -0.0444 -0.0142 0.0786  308 PHE D O   
16656 C CB  . PHE D 316 ? 0.4231 0.1822 0.5313 -0.0515 -0.0116 0.0646  308 PHE D CB  
16657 C CG  . PHE D 316 ? 0.4301 0.1928 0.5348 -0.0455 -0.0147 0.0725  308 PHE D CG  
16658 C CD1 . PHE D 316 ? 0.4375 0.2022 0.5451 -0.0384 -0.0167 0.0665  308 PHE D CD1 
16659 C CD2 . PHE D 316 ? 0.5232 0.2880 0.6213 -0.0470 -0.0156 0.0857  308 PHE D CD2 
16660 C CE1 . PHE D 316 ? 0.4214 0.1899 0.5263 -0.0330 -0.0197 0.0736  308 PHE D CE1 
16661 C CE2 . PHE D 316 ? 0.4642 0.2333 0.5589 -0.0416 -0.0189 0.0928  308 PHE D CE2 
16662 C CZ  . PHE D 316 ? 0.4198 0.1907 0.5183 -0.0346 -0.0211 0.0867  308 PHE D CZ  
16663 N N   . ALA D 317 ? 0.4608 0.1939 0.5859 -0.0571 -0.0092 0.0756  309 ALA D N   
16664 C CA  . ALA D 317 ? 0.4896 0.2128 0.6191 -0.0577 -0.0096 0.0868  309 ALA D CA  
16665 C C   . ALA D 317 ? 0.4963 0.2087 0.6392 -0.0526 -0.0105 0.0828  309 ALA D C   
16666 O O   . ALA D 317 ? 0.5312 0.2381 0.6786 -0.0482 -0.0128 0.0915  309 ALA D O   
16667 C CB  . ALA D 317 ? 0.5218 0.2418 0.6496 -0.0667 -0.0063 0.0904  309 ALA D CB  
16668 N N   . GLN D 318 ? 0.4671 0.1770 0.6170 -0.0533 -0.0090 0.0696  310 GLN D N   
16669 C CA  . GLN D 318 ? 0.4775 0.1785 0.6404 -0.0481 -0.0095 0.0640  310 GLN D CA  
16670 C C   . GLN D 318 ? 0.4693 0.1744 0.6336 -0.0394 -0.0123 0.0635  310 GLN D C   
16671 O O   . GLN D 318 ? 0.4810 0.1792 0.6548 -0.0341 -0.0138 0.0668  310 GLN D O   
16672 C CB  . GLN D 318 ? 0.5241 0.2243 0.6923 -0.0507 -0.0073 0.0488  310 GLN D CB  
16673 C CG  . GLN D 318 ? 0.5952 0.2924 0.7632 -0.0595 -0.0048 0.0478  310 GLN D CG  
16674 C CD  . GLN D 318 ? 0.7159 0.4153 0.8872 -0.0620 -0.0033 0.0322  310 GLN D CD  
16675 O OE1 . GLN D 318 ? 0.7785 0.4868 0.9424 -0.0664 -0.0025 0.0270  310 GLN D OE1 
16676 N NE2 . GLN D 318 ? 0.7368 0.4288 0.9197 -0.0592 -0.0029 0.0245  310 GLN D NE2 
16677 N N   . TYR D 319 ? 0.4498 0.1662 0.6050 -0.0378 -0.0129 0.0594  311 TYR D N   
16678 C CA  . TYR D 319 ? 0.4656 0.1871 0.6212 -0.0300 -0.0154 0.0590  311 TYR D CA  
16679 C C   . TYR D 319 ? 0.4484 0.1689 0.6030 -0.0267 -0.0184 0.0738  311 TYR D C   
16680 O O   . TYR D 319 ? 0.5806 0.2987 0.7430 -0.0200 -0.0205 0.0753  311 TYR D O   
16681 C CB  . TYR D 319 ? 0.4194 0.1532 0.5644 -0.0301 -0.0154 0.0530  311 TYR D CB  
16682 C CG  . TYR D 319 ? 0.4091 0.1487 0.5547 -0.0225 -0.0173 0.0498  311 TYR D CG  
16683 C CD1 . TYR D 319 ? 0.4267 0.1712 0.5676 -0.0189 -0.0202 0.0599  311 TYR D CD1 
16684 C CD2 . TYR D 319 ? 0.4227 0.1636 0.5731 -0.0194 -0.0162 0.0364  311 TYR D CD2 
16685 C CE1 . TYR D 319 ? 0.3958 0.1460 0.5377 -0.0122 -0.0220 0.0569  311 TYR D CE1 
16686 C CE2 . TYR D 319 ? 0.4299 0.1765 0.5809 -0.0128 -0.0176 0.0334  311 TYR D CE2 
16687 C CZ  . TYR D 319 ? 0.3905 0.1416 0.5377 -0.0092 -0.0205 0.0436  311 TYR D CZ  
16688 O OH  . TYR D 319 ? 0.3961 0.1532 0.5443 -0.0029 -0.0219 0.0406  311 TYR D OH  
16689 N N   . GLN D 320 ? 0.4500 0.1729 0.5952 -0.0315 -0.0186 0.0846  312 GLN D N   
16690 C CA  . GLN D 320 ? 0.5288 0.2522 0.6713 -0.0289 -0.0217 0.0990  312 GLN D CA  
16691 C C   . GLN D 320 ? 0.5411 0.2524 0.6955 -0.0269 -0.0227 0.1052  312 GLN D C   
16692 O O   . GLN D 320 ? 0.5066 0.2170 0.6653 -0.0210 -0.0261 0.1121  312 GLN D O   
16693 C CB  . GLN D 320 ? 0.5344 0.2635 0.6639 -0.0354 -0.0211 0.1086  312 GLN D CB  
16694 C CG  . GLN D 320 ? 0.5782 0.3150 0.6993 -0.0326 -0.0247 0.1203  312 GLN D CG  
16695 C CD  . GLN D 320 ? 0.7131 0.4435 0.8368 -0.0319 -0.0270 0.1343  312 GLN D CD  
16696 O OE1 . GLN D 320 ? 0.6609 0.3822 0.7966 -0.0276 -0.0284 0.1350  312 GLN D OE1 
16697 N NE2 . GLN D 320 ? 0.8164 0.5519 0.9288 -0.0363 -0.0274 0.1454  312 GLN D NE2 
16698 N N   . ALA D 321 ? 0.5716 0.2733 0.7318 -0.0318 -0.0199 0.1028  313 ALA D N   
16699 C CA  . ALA D 321 ? 0.5714 0.2605 0.7438 -0.0303 -0.0206 0.1085  313 ALA D CA  
16700 C C   . ALA D 321 ? 0.5823 0.2683 0.7677 -0.0219 -0.0223 0.1024  313 ALA D C   
16701 O O   . ALA D 321 ? 0.6032 0.2836 0.7967 -0.0174 -0.0250 0.1106  313 ALA D O   
16702 C CB  . ALA D 321 ? 0.5317 0.2116 0.7090 -0.0371 -0.0170 0.1042  313 ALA D CB  
16703 N N   . LYS D 322 ? 0.5254 0.2157 0.7130 -0.0198 -0.0208 0.0880  314 LYS D N   
16704 C CA  . LYS D 322 ? 0.5394 0.2274 0.7397 -0.0125 -0.0215 0.0802  314 LYS D CA  
16705 C C   . LYS D 322 ? 0.5093 0.2069 0.7066 -0.0057 -0.0245 0.0824  314 LYS D C   
16706 O O   . LYS D 322 ? 0.5362 0.2311 0.7441 0.0009  -0.0265 0.0837  314 LYS D O   
16707 C CB  . LYS D 322 ? 0.5606 0.2489 0.7645 -0.0140 -0.0180 0.0632  314 LYS D CB  
16708 C CG  . LYS D 322 ? 0.6477 0.3294 0.8677 -0.0088 -0.0172 0.0545  314 LYS D CG  
16709 C CD  . LYS D 322 ? 0.6970 0.3789 0.9191 -0.0119 -0.0136 0.0383  314 LYS D CD  
16710 C CE  . LYS D 322 ? 0.7535 0.4281 0.9924 -0.0076 -0.0123 0.0298  314 LYS D CE  
16711 N NZ  . LYS D 322 ? 0.7854 0.4618 1.0314 0.0008  -0.0147 0.0334  314 LYS D NZ  
16712 N N   . TYR D 323 ? 0.4745 0.1831 0.6579 -0.0073 -0.0250 0.0828  315 TYR D N   
16713 C CA  . TYR D 323 ? 0.4895 0.2084 0.6690 -0.0015 -0.0276 0.0831  315 TYR D CA  
16714 C C   . TYR D 323 ? 0.5279 0.2543 0.6938 -0.0038 -0.0301 0.0955  315 TYR D C   
16715 O O   . TYR D 323 ? 0.5709 0.3067 0.7253 -0.0059 -0.0296 0.0927  315 TYR D O   
16716 C CB  . TYR D 323 ? 0.4426 0.1686 0.6190 -0.0009 -0.0253 0.0685  315 TYR D CB  
16717 C CG  . TYR D 323 ? 0.4742 0.1942 0.6621 0.0003  -0.0224 0.0552  315 TYR D CG  
16718 C CD1 . TYR D 323 ? 0.4688 0.1864 0.6696 0.0071  -0.0230 0.0513  315 TYR D CD1 
16719 C CD2 . TYR D 323 ? 0.5200 0.2376 0.7063 -0.0055 -0.0191 0.0462  315 TYR D CD2 
16720 C CE1 . TYR D 323 ? 0.5218 0.2346 0.7330 0.0079  -0.0200 0.0386  315 TYR D CE1 
16721 C CE2 . TYR D 323 ? 0.5202 0.2331 0.7164 -0.0048 -0.0165 0.0336  315 TYR D CE2 
16722 C CZ  . TYR D 323 ? 0.5340 0.2445 0.7425 0.0019  -0.0168 0.0298  315 TYR D CZ  
16723 O OH  . TYR D 323 ? 0.5585 0.2650 0.7769 0.0024  -0.0140 0.0168  315 TYR D OH  
16724 N N   . PRO D 324 ? 0.4808 0.2035 0.6475 -0.0035 -0.0328 0.1092  316 PRO D N   
16725 C CA  . PRO D 324 ? 0.4802 0.2102 0.6328 -0.0069 -0.0348 0.1210  316 PRO D CA  
16726 C C   . PRO D 324 ? 0.5195 0.2621 0.6649 -0.0028 -0.0377 0.1221  316 PRO D C   
16727 O O   . PRO D 324 ? 0.5350 0.2864 0.6669 -0.0066 -0.0377 0.1251  316 PRO D O   
16728 C CB  . PRO D 324 ? 0.4894 0.2117 0.6466 -0.0068 -0.0372 0.1348  316 PRO D CB  
16729 C CG  . PRO D 324 ? 0.4999 0.2140 0.6742 -0.0004 -0.0382 0.1309  316 PRO D CG  
16730 C CD  . PRO D 324 ? 0.5119 0.2233 0.6920 -0.0009 -0.0341 0.1148  316 PRO D CD  
16731 N N   . ALA D 325 ? 0.5168 0.2608 0.6710 0.0047  -0.0402 0.1197  317 ALA D N   
16732 C CA  . ALA D 325 ? 0.4792 0.2354 0.6272 0.0085  -0.0431 0.1209  317 ALA D CA  
16733 C C   . ALA D 325 ? 0.4158 0.1792 0.5569 0.0073  -0.0405 0.1092  317 ALA D C   
16734 O O   . ALA D 325 ? 0.4033 0.1769 0.5327 0.0058  -0.0416 0.1115  317 ALA D O   
16735 C CB  . ALA D 325 ? 0.4900 0.2457 0.6504 0.0167  -0.0462 0.1211  317 ALA D CB  
16736 N N   . GLU D 326 ? 0.4371 0.1959 0.5856 0.0078  -0.0371 0.0963  318 GLU D N   
16737 C CA  . GLU D 326 ? 0.4158 0.1812 0.5578 0.0063  -0.0346 0.0851  318 GLU D CA  
16738 C C   . GLU D 326 ? 0.3884 0.1562 0.5181 -0.0014 -0.0327 0.0866  318 GLU D C   
16739 O O   . GLU D 326 ? 0.3726 0.1489 0.4933 -0.0029 -0.0322 0.0825  318 GLU D O   
16740 C CB  . GLU D 326 ? 0.4318 0.1919 0.5835 0.0078  -0.0313 0.0710  318 GLU D CB  
16741 C CG  . GLU D 326 ? 0.5476 0.3044 0.7134 0.0150  -0.0322 0.0682  318 GLU D CG  
16742 C CD  . GLU D 326 ? 0.6195 0.3644 0.7967 0.0149  -0.0321 0.0722  318 GLU D CD  
16743 O OE1 . GLU D 326 ? 0.6017 0.3433 0.7764 0.0126  -0.0342 0.0847  318 GLU D OE1 
16744 O OE2 . GLU D 326 ? 0.6947 0.4338 0.8832 0.0169  -0.0297 0.0627  318 GLU D OE2 
16745 N N   . ALA D 327 ? 0.4014 0.1620 0.5314 -0.0064 -0.0315 0.0923  319 ALA D N   
16746 C CA  . ALA D 327 ? 0.4235 0.1868 0.5427 -0.0140 -0.0294 0.0940  319 ALA D CA  
16747 C C   . ALA D 327 ? 0.4354 0.2086 0.5422 -0.0153 -0.0317 0.1038  319 ALA D C   
16748 O O   . ALA D 327 ? 0.4451 0.2263 0.5424 -0.0188 -0.0306 0.1010  319 ALA D O   
16749 C CB  . ALA D 327 ? 0.4142 0.1674 0.5371 -0.0191 -0.0275 0.0984  319 ALA D CB  
16750 N N   . ALA D 328 ? 0.4012 0.1746 0.5082 -0.0127 -0.0352 0.1153  320 ALA D N   
16751 C CA  . ALA D 328 ? 0.4471 0.2309 0.5419 -0.0139 -0.0378 0.1245  320 ALA D CA  
16752 C C   . ALA D 328 ? 0.3782 0.1724 0.4690 -0.0102 -0.0392 0.1186  320 ALA D C   
16753 O O   . ALA D 328 ? 0.4002 0.2040 0.4794 -0.0133 -0.0395 0.1206  320 ALA D O   
16754 C CB  . ALA D 328 ? 0.4585 0.2409 0.5553 -0.0112 -0.0418 0.1372  320 ALA D CB  
16755 N N   . GLU D 329 ? 0.4394 0.2320 0.5398 -0.0038 -0.0400 0.1112  321 GLU D N   
16756 C CA  . GLU D 329 ? 0.3807 0.1823 0.4781 -0.0004 -0.0409 0.1046  321 GLU D CA  
16757 C C   . GLU D 329 ? 0.3433 0.1477 0.4344 -0.0047 -0.0375 0.0953  321 GLU D C   
16758 O O   . GLU D 329 ? 0.3301 0.1437 0.4125 -0.0054 -0.0382 0.0942  321 GLU D O   
16759 C CB  . GLU D 329 ? 0.4235 0.2222 0.5335 0.0070  -0.0416 0.0978  321 GLU D CB  
16760 C CG  . GLU D 329 ? 0.3964 0.1983 0.5105 0.0125  -0.0461 0.1060  321 GLU D CG  
16761 C CD  . GLU D 329 ? 0.4405 0.2550 0.5441 0.0129  -0.0490 0.1100  321 GLU D CD  
16762 O OE1 . GLU D 329 ? 0.4762 0.2964 0.5804 0.0161  -0.0488 0.1022  321 GLU D OE1 
16763 O OE2 . GLU D 329 ? 0.3830 0.2019 0.4774 0.0097  -0.0512 0.1204  321 GLU D OE2 
16764 N N   . PHE D 330 ? 0.3782 0.1749 0.4740 -0.0077 -0.0340 0.0882  322 PHE D N   
16765 C CA  . PHE D 330 ? 0.3801 0.1798 0.4706 -0.0120 -0.0311 0.0793  322 PHE D CA  
16766 C C   . PHE D 330 ? 0.3305 0.1366 0.4090 -0.0183 -0.0308 0.0859  322 PHE D C   
16767 O O   . PHE D 330 ? 0.3282 0.1418 0.3996 -0.0201 -0.0303 0.0816  322 PHE D O   
16768 C CB  . PHE D 330 ? 0.3851 0.1758 0.4829 -0.0146 -0.0277 0.0712  322 PHE D CB  
16769 C CG  . PHE D 330 ? 0.4064 0.2005 0.4996 -0.0190 -0.0250 0.0614  322 PHE D CG  
16770 C CD1 . PHE D 330 ? 0.3647 0.1620 0.4592 -0.0161 -0.0245 0.0501  322 PHE D CD1 
16771 C CD2 . PHE D 330 ? 0.3307 0.1253 0.4185 -0.0263 -0.0231 0.0636  322 PHE D CD2 
16772 C CE1 . PHE D 330 ? 0.4495 0.2505 0.5397 -0.0201 -0.0226 0.0414  322 PHE D CE1 
16773 C CE2 . PHE D 330 ? 0.3286 0.1270 0.4133 -0.0302 -0.0211 0.0548  322 PHE D CE2 
16774 C CZ  . PHE D 330 ? 0.3610 0.1627 0.4467 -0.0270 -0.0211 0.0437  322 PHE D CZ  
16775 N N   . VAL D 331 ? 0.3807 0.1843 0.4569 -0.0218 -0.0309 0.0961  323 VAL D N   
16776 C CA  . VAL D 331 ? 0.4259 0.2364 0.4905 -0.0282 -0.0301 0.1026  323 VAL D CA  
16777 C C   . VAL D 331 ? 0.3758 0.1975 0.4314 -0.0262 -0.0332 0.1070  323 VAL D C   
16778 O O   . VAL D 331 ? 0.3275 0.1573 0.3744 -0.0296 -0.0323 0.1048  323 VAL D O   
16779 C CB  . VAL D 331 ? 0.4503 0.2556 0.5144 -0.0322 -0.0294 0.1129  323 VAL D CB  
16780 C CG1 . VAL D 331 ? 0.3926 0.2068 0.4439 -0.0383 -0.0287 0.1203  323 VAL D CG1 
16781 C CG2 . VAL D 331 ? 0.4150 0.2102 0.4867 -0.0357 -0.0259 0.1075  323 VAL D CG2 
16782 N N   . ARG D 332 ? 0.4120 0.2345 0.4698 -0.0207 -0.0369 0.1128  324 ARG D N   
16783 C CA  . ARG D 332 ? 0.3641 0.1979 0.4136 -0.0188 -0.0401 0.1168  324 ARG D CA  
16784 C C   . ARG D 332 ? 0.3332 0.1724 0.3811 -0.0170 -0.0398 0.1070  324 ARG D C   
16785 O O   . ARG D 332 ? 0.3474 0.1960 0.3851 -0.0196 -0.0403 0.1078  324 ARG D O   
16786 C CB  . ARG D 332 ? 0.3734 0.2069 0.4282 -0.0126 -0.0444 0.1231  324 ARG D CB  
16787 C CG  . ARG D 332 ? 0.3537 0.1991 0.4015 -0.0099 -0.0481 0.1256  324 ARG D CG  
16788 C CD  . ARG D 332 ? 0.3761 0.2215 0.4315 -0.0033 -0.0523 0.1304  324 ARG D CD  
16789 N NE  . ARG D 332 ? 0.4098 0.2504 0.4777 0.0031  -0.0521 0.1215  324 ARG D NE  
16790 C CZ  . ARG D 332 ? 0.3637 0.2100 0.4319 0.0063  -0.0524 0.1139  324 ARG D CZ  
16791 N NH1 . ARG D 332 ? 0.3319 0.1883 0.3890 0.0038  -0.0531 0.1140  324 ARG D NH1 
16792 N NH2 . ARG D 332 ? 0.3603 0.2023 0.4401 0.0118  -0.0516 0.1058  324 ARG D NH2 
16793 N N   . ARG D 333 ? 0.3502 0.1835 0.4077 -0.0130 -0.0388 0.0974  325 ARG D N   
16794 C CA  . ARG D 333 ? 0.2922 0.1304 0.3485 -0.0108 -0.0387 0.0883  325 ARG D CA  
16795 C C   . ARG D 333 ? 0.2832 0.1233 0.3333 -0.0166 -0.0359 0.0823  325 ARG D C   
16796 O O   . ARG D 333 ? 0.3115 0.1590 0.3547 -0.0173 -0.0365 0.0797  325 ARG D O   
16797 C CB  . ARG D 333 ? 0.2923 0.1247 0.3603 -0.0047 -0.0383 0.0796  325 ARG D CB  
16798 C CG  . ARG D 333 ? 0.2982 0.1313 0.3728 0.0019  -0.0415 0.0846  325 ARG D CG  
16799 C CD  . ARG D 333 ? 0.3580 0.1847 0.4456 0.0073  -0.0403 0.0762  325 ARG D CD  
16800 N NE  . ARG D 333 ? 0.3149 0.1432 0.4028 0.0081  -0.0380 0.0640  325 ARG D NE  
16801 C CZ  . ARG D 333 ? 0.3160 0.1411 0.4131 0.0123  -0.0362 0.0546  325 ARG D CZ  
16802 N NH1 . ARG D 333 ? 0.3131 0.1329 0.4210 0.0163  -0.0367 0.0561  325 ARG D NH1 
16803 N NH2 . ARG D 333 ? 0.2790 0.1066 0.3745 0.0124  -0.0341 0.0438  325 ARG D NH2 
16804 N N   . MET D 334 ? 0.2889 0.1228 0.3418 -0.0210 -0.0328 0.0802  326 MET D N   
16805 C CA  . MET D 334 ? 0.2810 0.1177 0.3289 -0.0269 -0.0303 0.0748  326 MET D CA  
16806 C C   . MET D 334 ? 0.3196 0.1648 0.3561 -0.0321 -0.0305 0.0823  326 MET D C   
16807 O O   . MET D 334 ? 0.2947 0.1479 0.3244 -0.0349 -0.0288 0.0767  326 MET D O   
16808 C CB  . MET D 334 ? 0.2885 0.1174 0.3427 -0.0306 -0.0271 0.0707  326 MET D CB  
16809 C CG  . MET D 334 ? 0.2889 0.1112 0.3528 -0.0268 -0.0261 0.0603  326 MET D CG  
16810 S SD  . MET D 334 ? 0.3153 0.1433 0.3771 -0.0249 -0.0262 0.0478  326 MET D SD  
16811 C CE  . MET D 334 ? 0.3235 0.1577 0.3775 -0.0328 -0.0247 0.0465  326 MET D CE  
16812 N N   . ASP D 335 ? 0.3099 0.1564 0.3429 -0.0330 -0.0316 0.0930  327 ASP D N   
16813 C CA  . ASP D 335 ? 0.3749 0.2310 0.3959 -0.0377 -0.0316 0.1002  327 ASP D CA  
16814 C C   . ASP D 335 ? 0.3876 0.2529 0.4015 -0.0347 -0.0348 0.1011  327 ASP D C   
16815 O O   . ASP D 335 ? 0.4406 0.3159 0.4436 -0.0383 -0.0346 0.1054  327 ASP D O   
16816 C CB  . ASP D 335 ? 0.3440 0.1988 0.3630 -0.0398 -0.0318 0.1111  327 ASP D CB  
16817 C CG  . ASP D 335 ? 0.4304 0.2787 0.4527 -0.0452 -0.0279 0.1113  327 ASP D CG  
16818 O OD1 . ASP D 335 ? 0.3658 0.2132 0.3904 -0.0484 -0.0251 0.1032  327 ASP D OD1 
16819 O OD2 . ASP D 335 ? 0.4479 0.2921 0.4710 -0.0464 -0.0279 0.1194  327 ASP D OD2 
16820 N N   . LYS D 336 ? 0.3619 0.2263 0.3813 -0.0279 -0.0368 0.0954  328 LYS D N   
16821 C CA  . LYS D 336 ? 0.3722 0.2476 0.3855 -0.0242 -0.0386 0.0932  328 LYS D CA  
16822 C C   . LYS D 336 ? 0.3907 0.2709 0.3987 -0.0241 -0.0425 0.1051  328 LYS D C   
16823 O O   . LYS D 336 ? 0.4659 0.3579 0.4641 -0.0252 -0.0431 0.1053  328 LYS D O   
16824 C CB  . LYS D 336 ? 0.3760 0.2621 0.3803 -0.0272 -0.0354 0.0847  328 LYS D CB  
16825 C CG  . LYS D 336 ? 0.4705 0.3528 0.4795 -0.0276 -0.0322 0.0738  328 LYS D CG  
16826 C CD  . LYS D 336 ? 0.4569 0.3491 0.4582 -0.0310 -0.0292 0.0668  328 LYS D CD  
16827 C CE  . LYS D 336 ? 0.4876 0.3764 0.4940 -0.0313 -0.0268 0.0567  328 LYS D CE  
16828 N NZ  . LYS D 336 ? 0.4166 0.3146 0.4173 -0.0344 -0.0242 0.0503  328 LYS D NZ  
16829 N N   . LYS D 337 ? 0.3685 0.2422 0.3827 -0.0222 -0.0441 0.1122  329 LYS D N   
16830 C CA  . LYS D 337 ? 0.3719 0.2513 0.3819 -0.0212 -0.0475 0.1219  329 LYS D CA  
16831 C C   . LYS D 337 ? 0.4260 0.3040 0.4454 -0.0132 -0.0512 0.1220  329 LYS D C   
16832 O O   . LYS D 337 ? 0.3984 0.2676 0.4295 -0.0089 -0.0505 0.1167  329 LYS D O   
16833 C CB  . LYS D 337 ? 0.4170 0.2916 0.4267 -0.0248 -0.0463 0.1300  329 LYS D CB  
16834 C CG  . LYS D 337 ? 0.4691 0.3462 0.4700 -0.0330 -0.0423 0.1308  329 LYS D CG  
16835 C CD  . LYS D 337 ? 0.5391 0.4090 0.5423 -0.0361 -0.0407 0.1378  329 LYS D CD  
16836 C CE  . LYS D 337 ? 0.5492 0.4221 0.5447 -0.0445 -0.0361 0.1381  329 LYS D CE  
16837 N NZ  . LYS D 337 ? 0.5530 0.4169 0.5528 -0.0475 -0.0339 0.1434  329 LYS D NZ  
16838 N N   . LEU D 338 ? 0.4759 0.3635 0.4901 -0.0116 -0.0551 0.1275  330 LEU D N   
16839 C CA  . LEU D 338 ? 0.4646 0.3526 0.4876 -0.0045 -0.0591 0.1289  330 LEU D CA  
16840 C C   . LEU D 338 ? 0.4581 0.3402 0.4866 -0.0032 -0.0608 0.1375  330 LEU D C   
16841 O O   . LEU D 338 ? 0.4213 0.3022 0.4436 -0.0083 -0.0597 0.1441  330 LEU D O   
16842 C CB  . LEU D 338 ? 0.4669 0.3686 0.4822 -0.0036 -0.0627 0.1308  330 LEU D CB  
16843 C CG  . LEU D 338 ? 0.4614 0.3696 0.4721 -0.0039 -0.0618 0.1227  330 LEU D CG  
16844 C CD1 . LEU D 338 ? 0.4848 0.4068 0.4885 -0.0033 -0.0656 0.1251  330 LEU D CD1 
16845 C CD2 . LEU D 338 ? 0.5158 0.4170 0.5384 0.0016  -0.0608 0.1140  330 LEU D CD2 
16846 N N   . PRO D 339 ? 0.3984 0.2767 0.4390 0.0035  -0.0634 0.1376  331 PRO D N   
16847 C CA  . PRO D 339 ? 0.4521 0.3254 0.4983 0.0051  -0.0658 0.1466  331 PRO D CA  
16848 C C   . PRO D 339 ? 0.4589 0.3419 0.4935 0.0020  -0.0692 0.1569  331 PRO D C   
16849 O O   . PRO D 339 ? 0.4363 0.3314 0.4625 0.0013  -0.0712 0.1565  331 PRO D O   
16850 C CB  . PRO D 339 ? 0.4231 0.2944 0.4835 0.0133  -0.0683 0.1437  331 PRO D CB  
16851 C CG  . PRO D 339 ? 0.4092 0.2794 0.4738 0.0153  -0.0653 0.1315  331 PRO D CG  
16852 C CD  . PRO D 339 ? 0.3959 0.2742 0.4464 0.0099  -0.0639 0.1293  331 PRO D CD  
16853 N N   . GLU D 340 ? 0.5207 0.3984 0.5550 -0.0003 -0.0698 0.1659  332 GLU D N   
16854 C CA  . GLU D 340 ? 0.5440 0.4305 0.5664 -0.0042 -0.0726 0.1759  332 GLU D CA  
16855 C C   . GLU D 340 ? 0.5273 0.4233 0.5506 0.0005  -0.0786 0.1798  332 GLU D C   
16856 O O   . GLU D 340 ? 0.6159 0.5233 0.6272 -0.0028 -0.0810 0.1849  332 GLU D O   
16857 C CB  . GLU D 340 ? 0.5625 0.4402 0.5860 -0.0070 -0.0721 0.1850  332 GLU D CB  
16858 N N   . ASN D 341 ? 0.4538 0.3461 0.4913 0.0079  -0.0809 0.1771  333 ASN D N   
16859 C CA  . ASN D 341 ? 0.5134 0.4143 0.5539 0.0127  -0.0866 0.1808  333 ASN D CA  
16860 C C   . ASN D 341 ? 0.4768 0.3874 0.5171 0.0154  -0.0872 0.1721  333 ASN D C   
16861 O O   . ASN D 341 ? 0.3634 0.2793 0.4109 0.0209  -0.0913 0.1724  333 ASN D O   
16862 C CB  . ASN D 341 ? 0.5811 0.4726 0.6383 0.0193  -0.0891 0.1838  333 ASN D CB  
16863 C CG  . ASN D 341 ? 0.6555 0.5388 0.7268 0.0242  -0.0859 0.1731  333 ASN D CG  
16864 O OD1 . ASN D 341 ? 0.6507 0.5308 0.7196 0.0217  -0.0810 0.1649  333 ASN D OD1 
16865 N ND2 . ASN D 341 ? 0.6671 0.5475 0.7533 0.0312  -0.0885 0.1729  333 ASN D ND2 
16866 N N   . PHE D 342 ? 0.4449 0.3582 0.4774 0.0116  -0.0833 0.1646  334 PHE D N   
16867 C CA  . PHE D 342 ? 0.3984 0.3181 0.4329 0.0145  -0.0831 0.1554  334 PHE D CA  
16868 C C   . PHE D 342 ? 0.4394 0.3743 0.4675 0.0149  -0.0877 0.1578  334 PHE D C   
16869 O O   . PHE D 342 ? 0.3921 0.3315 0.4287 0.0205  -0.0903 0.1545  334 PHE D O   
16870 C CB  . PHE D 342 ? 0.4045 0.3235 0.4314 0.0099  -0.0781 0.1478  334 PHE D CB  
16871 C CG  . PHE D 342 ? 0.3614 0.2859 0.3905 0.0127  -0.0776 0.1384  334 PHE D CG  
16872 C CD1 . PHE D 342 ? 0.3717 0.2887 0.4140 0.0181  -0.0759 0.1310  334 PHE D CD1 
16873 C CD2 . PHE D 342 ? 0.3512 0.2883 0.3691 0.0096  -0.0785 0.1366  334 PHE D CD2 
16874 C CE1 . PHE D 342 ? 0.3714 0.2934 0.4157 0.0205  -0.0753 0.1226  334 PHE D CE1 
16875 C CE2 . PHE D 342 ? 0.2812 0.2230 0.3013 0.0120  -0.0781 0.1283  334 PHE D CE2 
16876 C CZ  . PHE D 342 ? 0.3209 0.2551 0.3542 0.0175  -0.0766 0.1216  334 PHE D CZ  
16877 N N   . ASP D 343 ? 0.4498 0.3932 0.4630 0.0089  -0.0885 0.1627  335 ASP D N   
16878 C CA  . ASP D 343 ? 0.4563 0.4147 0.4626 0.0085  -0.0927 0.1640  335 ASP D CA  
16879 C C   . ASP D 343 ? 0.4398 0.4000 0.4555 0.0142  -0.0985 0.1703  335 ASP D C   
16880 O O   . ASP D 343 ? 0.3792 0.3489 0.3983 0.0176  -0.1019 0.1678  335 ASP D O   
16881 C CB  . ASP D 343 ? 0.5022 0.4691 0.4909 0.0006  -0.0921 0.1680  335 ASP D CB  
16882 C CG  . ASP D 343 ? 0.5101 0.4788 0.4894 -0.0048 -0.0867 0.1603  335 ASP D CG  
16883 O OD1 . ASP D 343 ? 0.5071 0.4762 0.4905 -0.0024 -0.0853 0.1518  335 ASP D OD1 
16884 O OD2 . ASP D 343 ? 0.5658 0.5356 0.5337 -0.0113 -0.0840 0.1629  335 ASP D OD2 
16885 N N   . GLU D 344 ? 0.4616 0.4128 0.4826 0.0153  -0.0996 0.1784  336 GLU D N   
16886 C CA  . GLU D 344 ? 0.3743 0.3262 0.4053 0.0209  -0.1053 0.1850  336 GLU D CA  
16887 C C   . GLU D 344 ? 0.4216 0.3696 0.4701 0.0288  -0.1056 0.1783  336 GLU D C   
16888 O O   . GLU D 344 ? 0.4238 0.3794 0.4791 0.0335  -0.1101 0.1791  336 GLU D O   
16889 C CB  . GLU D 344 ? 0.4218 0.3635 0.4550 0.0201  -0.1061 0.1951  336 GLU D CB  
16890 N N   . TYR D 345 ? 0.4207 0.3576 0.4768 0.0302  -0.1005 0.1713  337 TYR D N   
16891 C CA  . TYR D 345 ? 0.4719 0.4057 0.5438 0.0370  -0.0997 0.1633  337 TYR D CA  
16892 C C   . TYR D 345 ? 0.4350 0.3819 0.5049 0.0382  -0.1008 0.1565  337 TYR D C   
16893 O O   . TYR D 345 ? 0.3682 0.3199 0.4492 0.0441  -0.1036 0.1545  337 TYR D O   
16894 C CB  . TYR D 345 ? 0.3424 0.2632 0.4199 0.0369  -0.0936 0.1558  337 TYR D CB  
16895 C CG  . TYR D 345 ? 0.3578 0.2761 0.4502 0.0433  -0.0917 0.1461  337 TYR D CG  
16896 C CD1 . TYR D 345 ? 0.3423 0.2532 0.4512 0.0493  -0.0924 0.1463  337 TYR D CD1 
16897 C CD2 . TYR D 345 ? 0.3591 0.2826 0.4493 0.0431  -0.0891 0.1365  337 TYR D CD2 
16898 C CE1 . TYR D 345 ? 0.4440 0.3534 0.5663 0.0548  -0.0902 0.1367  337 TYR D CE1 
16899 C CE2 . TYR D 345 ? 0.3815 0.3034 0.4849 0.0487  -0.0871 0.1274  337 TYR D CE2 
16900 C CZ  . TYR D 345 ? 0.4034 0.3185 0.5227 0.0544  -0.0874 0.1272  337 TYR D CZ  
16901 O OH  . TYR D 345 ? 0.3740 0.2881 0.5064 0.0596  -0.0847 0.1175  337 TYR D OH  
16902 N N   . VAL D 346 ? 0.3795 0.3324 0.4356 0.0327  -0.0985 0.1528  338 VAL D N   
16903 C CA  . VAL D 346 ? 0.3874 0.3525 0.4412 0.0331  -0.0993 0.1460  338 VAL D CA  
16904 C C   . VAL D 346 ? 0.3770 0.3555 0.4286 0.0341  -0.1053 0.1511  338 VAL D C   
16905 O O   . VAL D 346 ? 0.3726 0.3592 0.4318 0.0382  -0.1075 0.1467  338 VAL D O   
16906 C CB  . VAL D 346 ? 0.3605 0.3287 0.3997 0.0265  -0.0956 0.1415  338 VAL D CB  
16907 C CG1 . VAL D 346 ? 0.3181 0.2997 0.3537 0.0262  -0.0968 0.1352  338 VAL D CG1 
16908 C CG2 . VAL D 346 ? 0.2902 0.2457 0.3330 0.0262  -0.0900 0.1355  338 VAL D CG2 
16909 N N   . GLN D 347 ? 0.3671 0.3486 0.4086 0.0301  -0.1082 0.1601  339 GLN D N   
16910 C CA  . GLN D 347 ? 0.4441 0.4388 0.4823 0.0305  -0.1142 0.1649  339 GLN D CA  
16911 C C   . GLN D 347 ? 0.4935 0.4874 0.5486 0.0383  -0.1185 0.1677  339 GLN D C   
16912 O O   . GLN D 347 ? 0.4828 0.4880 0.5418 0.0411  -0.1224 0.1660  339 GLN D O   
16913 C CB  . GLN D 347 ? 0.4550 0.4522 0.4790 0.0245  -0.1160 0.1742  339 GLN D CB  
16914 N N   . THR D 348 ? 0.4795 0.4601 0.5452 0.0418  -0.1177 0.1715  340 THR D N   
16915 C CA  . THR D 348 ? 0.4171 0.3957 0.5005 0.0495  -0.1211 0.1732  340 THR D CA  
16916 C C   . THR D 348 ? 0.4336 0.4148 0.5293 0.0545  -0.1189 0.1623  340 THR D C   
16917 O O   . THR D 348 ? 0.3796 0.3695 0.4847 0.0593  -0.1227 0.1615  340 THR D O   
16918 C CB  . THR D 348 ? 0.4208 0.3837 0.5131 0.0516  -0.1197 0.1782  340 THR D CB  
16919 O OG1 . THR D 348 ? 0.3956 0.3573 0.4772 0.0471  -0.1222 0.1893  340 THR D OG1 
16920 C CG2 . THR D 348 ? 0.4296 0.3898 0.5415 0.0598  -0.1225 0.1788  340 THR D CG2 
16921 N N   . ALA D 349 ? 0.3541 0.3284 0.4499 0.0534  -0.1128 0.1538  341 ALA D N   
16922 C CA  . ALA D 349 ? 0.4043 0.3809 0.5108 0.0575  -0.1101 0.1432  341 ALA D CA  
16923 C C   . ALA D 349 ? 0.3779 0.3710 0.4794 0.0565  -0.1127 0.1397  341 ALA D C   
16924 O O   . ALA D 349 ? 0.3656 0.3650 0.4790 0.0613  -0.1133 0.1341  341 ALA D O   
16925 C CB  . ALA D 349 ? 0.3426 0.3095 0.4471 0.0553  -0.1033 0.1353  341 ALA D CB  
16926 N N   . LEU D 350 ? 0.3490 0.3495 0.4332 0.0499  -0.1138 0.1422  342 LEU D N   
16927 C CA  . LEU D 350 ? 0.3275 0.3437 0.4061 0.0480  -0.1159 0.1382  342 LEU D CA  
16928 C C   . LEU D 350 ? 0.3776 0.4046 0.4633 0.0518  -0.1224 0.1423  342 LEU D C   
16929 O O   . LEU D 350 ? 0.3679 0.4050 0.4611 0.0546  -0.1236 0.1365  342 LEU D O   
16930 C CB  . LEU D 350 ? 0.3400 0.3612 0.3984 0.0398  -0.1153 0.1396  342 LEU D CB  
16931 C CG  . LEU D 350 ? 0.3361 0.3729 0.3865 0.0362  -0.1165 0.1342  342 LEU D CG  
16932 C CD1 . LEU D 350 ? 0.3654 0.4046 0.4258 0.0393  -0.1138 0.1241  342 LEU D CD1 
16933 C CD2 . LEU D 350 ? 0.3188 0.3576 0.3503 0.0280  -0.1140 0.1340  342 LEU D CD2 
16934 N N   . LYS D 351 ? 0.3895 0.4146 0.4734 0.0521  -0.1266 0.1524  343 LYS D N   
16935 C CA  . LYS D 351 ? 0.4439 0.4789 0.5346 0.0559  -0.1333 0.1572  343 LYS D CA  
16936 C C   . LYS D 351 ? 0.4777 0.5112 0.5896 0.0641  -0.1334 0.1529  343 LYS D C   
16937 O O   . LYS D 351 ? 0.4758 0.5213 0.5952 0.0673  -0.1372 0.1510  343 LYS D O   
16938 C CB  . LYS D 351 ? 0.4984 0.5297 0.5841 0.0548  -0.1376 0.1694  343 LYS D CB  
16939 N N   . GLU D 352 ? 0.4585 0.4777 0.5808 0.0675  -0.1289 0.1507  344 GLU D N   
16940 C CA  . GLU D 352 ? 0.4134 0.4312 0.5560 0.0749  -0.1277 0.1451  344 GLU D CA  
16941 C C   . GLU D 352 ? 0.4643 0.4908 0.6104 0.0753  -0.1245 0.1337  344 GLU D C   
16942 O O   . GLU D 352 ? 0.4890 0.5237 0.6486 0.0803  -0.1260 0.1298  344 GLU D O   
16943 C CB  . GLU D 352 ? 0.3828 0.3832 0.5346 0.0776  -0.1231 0.1441  344 GLU D CB  
16944 N N   . VAL D 353 ? 0.4054 0.4307 0.5399 0.0701  -0.1201 0.1284  345 VAL D N   
16945 C CA  . VAL D 353 ? 0.4271 0.4611 0.5641 0.0699  -0.1173 0.1182  345 VAL D CA  
16946 C C   . VAL D 353 ? 0.4883 0.5402 0.6224 0.0686  -0.1225 0.1186  345 VAL D C   
16947 O O   . VAL D 353 ? 0.5437 0.6050 0.6887 0.0716  -0.1224 0.1122  345 VAL D O   
16948 C CB  . VAL D 353 ? 0.4093 0.4379 0.5339 0.0643  -0.1121 0.1134  345 VAL D CB  
16949 C CG1 . VAL D 353 ? 0.3406 0.3809 0.4638 0.0624  -0.1107 0.1049  345 VAL D CG1 
16950 C CG2 . VAL D 353 ? 0.4339 0.4469 0.5658 0.0667  -0.1063 0.1093  345 VAL D CG2 
16951 N N   . CYS D 354 ? 0.5125 0.5695 0.6319 0.0638  -0.1269 0.1258  346 CYS D N   
16952 C CA  . CYS D 354 ? 0.5189 0.5930 0.6348 0.0622  -0.1321 0.1259  346 CYS D CA  
16953 C C   . CYS D 354 ? 0.5443 0.6246 0.6761 0.0689  -0.1371 0.1286  346 CYS D C   
16954 O O   . CYS D 354 ? 0.5903 0.6849 0.7269 0.0697  -0.1399 0.1247  346 CYS D O   
16955 C CB  . CYS D 354 ? 0.5532 0.6307 0.6496 0.0555  -0.1353 0.1328  346 CYS D CB  
16956 S SG  . CYS D 354 ? 0.5962 0.6947 0.6838 0.0510  -0.1404 0.1303  346 CYS D SG  
16957 N N   . ALA D 355 ? 0.5212 0.5912 0.6620 0.0737  -0.1382 0.1350  347 ALA D N   
16958 C CA  . ALA D 355 ? 0.5054 0.5805 0.6631 0.0806  -0.1426 0.1373  347 ALA D CA  
16959 C C   . ALA D 355 ? 0.5484 0.6266 0.7236 0.0856  -0.1386 0.1270  347 ALA D C   
16960 O O   . ALA D 355 ? 0.6048 0.6963 0.7898 0.0885  -0.1417 0.1244  347 ALA D O   
16961 C CB  . ALA D 355 ? 0.4637 0.5259 0.6273 0.0843  -0.1443 0.1463  347 ALA D CB  
16962 N N   . LYS D 356 ? 0.5167 0.5833 0.6960 0.0863  -0.1315 0.1208  348 LYS D N   
16963 C CA  . LYS D 356 ? 0.4955 0.5641 0.6911 0.0908  -0.1267 0.1106  348 LYS D CA  
16964 C C   . LYS D 356 ? 0.4665 0.5501 0.6599 0.0878  -0.1258 0.1028  348 LYS D C   
16965 O O   . LYS D 356 ? 0.4973 0.5833 0.6754 0.0814  -0.1250 0.1016  348 LYS D O   
16966 C CB  . LYS D 356 ? 0.4707 0.5236 0.6687 0.0912  -0.1191 0.1052  348 LYS D CB  
16967 N N   . ASN D 368 ? 0.4512 0.4452 0.6169 0.0751  -0.0772 0.0592  360 ASN D N   
16968 C CA  . ASN D 368 ? 0.4102 0.3921 0.5657 0.0714  -0.0716 0.0548  360 ASN D CA  
16969 C C   . ASN D 368 ? 0.3462 0.3204 0.4900 0.0675  -0.0752 0.0647  360 ASN D C   
16970 O O   . ASN D 368 ? 0.3085 0.2734 0.4560 0.0690  -0.0760 0.0697  360 ASN D O   
16971 C CB  . ASN D 368 ? 0.5035 0.4750 0.6727 0.0760  -0.0668 0.0480  360 ASN D CB  
16972 C CG  . ASN D 368 ? 0.5136 0.4748 0.6715 0.0716  -0.0602 0.0410  360 ASN D CG  
16973 O OD1 . ASN D 368 ? 0.5402 0.4975 0.6831 0.0662  -0.0607 0.0449  360 ASN D OD1 
16974 N ND2 . ASN D 368 ? 0.5656 0.5234 0.7311 0.0738  -0.0540 0.0304  360 ASN D ND2 
16975 N N   . SER D 369 ? 0.2894 0.2684 0.4153 0.0609  -0.0748 0.0654  361 SER D N   
16976 C CA  . SER D 369 ? 0.3051 0.2779 0.4182 0.0562  -0.0769 0.0735  361 SER D CA  
16977 C C   . SER D 369 ? 0.3112 0.2687 0.4240 0.0555  -0.0725 0.0710  361 SER D C   
16978 O O   . SER D 369 ? 0.2913 0.2402 0.4027 0.0546  -0.0751 0.0793  361 SER D O   
16979 C CB  . SER D 369 ? 0.3073 0.2882 0.4023 0.0492  -0.0758 0.0718  361 SER D CB  
16980 O OG  . SER D 369 ? 0.3310 0.3262 0.4258 0.0491  -0.0801 0.0740  361 SER D OG  
16981 N N   . ILE D 370 ? 0.3148 0.2691 0.4285 0.0555  -0.0658 0.0596  362 ILE D N   
16982 C CA  . ILE D 370 ? 0.2890 0.2298 0.4020 0.0543  -0.0615 0.0559  362 ILE D CA  
16983 C C   . ILE D 370 ? 0.2677 0.1982 0.3969 0.0598  -0.0636 0.0599  362 ILE D C   
16984 O O   . ILE D 370 ? 0.3219 0.2420 0.4487 0.0577  -0.0635 0.0641  362 ILE D O   
16985 C CB  . ILE D 370 ? 0.2805 0.2217 0.3917 0.0535  -0.0545 0.0429  362 ILE D CB  
16986 C CG1 . ILE D 370 ? 0.2858 0.2362 0.3818 0.0481  -0.0526 0.0397  362 ILE D CG1 
16987 C CG2 . ILE D 370 ? 0.2446 0.1727 0.3556 0.0522  -0.0504 0.0384  362 ILE D CG2 
16988 C CD1 . ILE D 370 ? 0.2418 0.1940 0.3355 0.0472  -0.0462 0.0282  362 ILE D CD1 
16989 N N   . GLU D 371 ? 0.2721 0.2069 0.4159 0.0656  -0.0641 0.0574  363 GLU D N   
16990 C CA  . GLU D 371 ? 0.2864 0.2143 0.4416 0.0692  -0.0640 0.0592  363 GLU D CA  
16991 C C   . GLU D 371 ? 0.3406 0.2656 0.4903 0.0671  -0.0689 0.0718  363 GLU D C   
16992 O O   . GLU D 371 ? 0.3621 0.2762 0.5139 0.0665  -0.0679 0.0742  363 GLU D O   
16993 C CB  . GLU D 371 ? 0.3529 0.2888 0.5229 0.0752  -0.0644 0.0558  363 GLU D CB  
16994 C CG  . GLU D 371 ? 0.3613 0.2895 0.5454 0.0794  -0.0631 0.0549  363 GLU D CG  
16995 C CD  . GLU D 371 ? 0.4486 0.3713 0.6405 0.0811  -0.0560 0.0418  363 GLU D CD  
16996 O OE1 . GLU D 371 ? 0.3932 0.3233 0.5871 0.0821  -0.0526 0.0330  363 GLU D OE1 
16997 O OE2 . GLU D 371 ? 0.5044 0.4158 0.7003 0.0810  -0.0536 0.0401  363 GLU D OE2 
16998 N N   . ILE D 372 ? 0.3474 0.2826 0.4894 0.0654  -0.0741 0.0796  364 ILE D N   
16999 C CA  . ILE D 372 ? 0.3311 0.2652 0.4661 0.0628  -0.0786 0.0915  364 ILE D CA  
17000 C C   . ILE D 372 ? 0.3412 0.2660 0.4641 0.0569  -0.0765 0.0939  364 ILE D C   
17001 O O   . ILE D 372 ? 0.3946 0.3115 0.5171 0.0557  -0.0773 0.1005  364 ILE D O   
17002 C CB  . ILE D 372 ? 0.2793 0.2279 0.4067 0.0614  -0.0841 0.0975  364 ILE D CB  
17003 C CG1 . ILE D 372 ? 0.3049 0.2628 0.4459 0.0674  -0.0866 0.0960  364 ILE D CG1 
17004 C CG2 . ILE D 372 ? 0.2763 0.2243 0.3933 0.0576  -0.0881 0.1092  364 ILE D CG2 
17005 C CD1 . ILE D 372 ? 0.3360 0.3094 0.4707 0.0660  -0.0916 0.0996  364 ILE D CD1 
17006 N N   . LEU D 373 ? 0.3352 0.2608 0.4486 0.0531  -0.0737 0.0887  365 LEU D N   
17007 C CA  . LEU D 373 ? 0.3982 0.3163 0.4999 0.0471  -0.0717 0.0907  365 LEU D CA  
17008 C C   . LEU D 373 ? 0.2625 0.1667 0.3713 0.0477  -0.0672 0.0859  365 LEU D C   
17009 O O   . LEU D 373 ? 0.3262 0.2226 0.4303 0.0440  -0.0666 0.0907  365 LEU D O   
17010 C CB  . LEU D 373 ? 0.4131 0.3359 0.5038 0.0432  -0.0702 0.0859  365 LEU D CB  
17011 C CG  . LEU D 373 ? 0.5125 0.4396 0.5863 0.0363  -0.0715 0.0921  365 LEU D CG  
17012 C CD1 . LEU D 373 ? 0.5839 0.5233 0.6535 0.0361  -0.0770 0.0999  365 LEU D CD1 
17013 C CD2 . LEU D 373 ? 0.4607 0.3923 0.5224 0.0315  -0.0660 0.0822  365 LEU D CD2 
17014 N N   . ALA D 374 ? 0.3266 0.2281 0.4464 0.0519  -0.0638 0.0759  366 ALA D N   
17015 C CA  . ALA D 374 ? 0.3415 0.2309 0.4673 0.0519  -0.0591 0.0695  366 ALA D CA  
17016 C C   . ALA D 374 ? 0.3492 0.2309 0.4823 0.0531  -0.0604 0.0760  366 ALA D C   
17017 O O   . ALA D 374 ? 0.4082 0.2798 0.5406 0.0502  -0.0580 0.0757  366 ALA D O   
17018 C CB  . ALA D 374 ? 0.3542 0.2441 0.4902 0.0561  -0.0550 0.0572  366 ALA D CB  
17019 N N   . LYS D 375 ? 0.3738 0.2603 0.5147 0.0574  -0.0645 0.0820  367 LYS D N   
17020 C CA  . LYS D 375 ? 0.3856 0.2645 0.5340 0.0589  -0.0662 0.0889  367 LYS D CA  
17021 C C   . LYS D 375 ? 0.4053 0.2799 0.5423 0.0531  -0.0678 0.0986  367 LYS D C   
17022 O O   . LYS D 375 ? 0.4029 0.2673 0.5442 0.0523  -0.0669 0.1015  367 LYS D O   
17023 C CB  . LYS D 375 ? 0.3577 0.2440 0.5152 0.0642  -0.0711 0.0945  367 LYS D CB  
17024 N N   . GLU D 376 ? 0.3645 0.2469 0.4871 0.0488  -0.0698 0.1032  368 GLU D N   
17025 C CA  . GLU D 376 ? 0.4084 0.2887 0.5190 0.0428  -0.0709 0.1123  368 GLU D CA  
17026 C C   . GLU D 376 ? 0.4089 0.2827 0.5116 0.0372  -0.0663 0.1075  368 GLU D C   
17027 O O   . GLU D 376 ? 0.3764 0.2439 0.4745 0.0329  -0.0655 0.1129  368 GLU D O   
17028 C CB  . GLU D 376 ? 0.4352 0.3285 0.5339 0.0405  -0.0753 0.1193  368 GLU D CB  
17029 C CG  . GLU D 376 ? 0.4157 0.3096 0.4994 0.0334  -0.0758 0.1273  368 GLU D CG  
17030 C CD  . GLU D 376 ? 0.5475 0.4366 0.6329 0.0330  -0.0784 0.1380  368 GLU D CD  
17031 O OE1 . GLU D 376 ? 0.5528 0.4361 0.6517 0.0381  -0.0796 0.1390  368 GLU D OE1 
17032 O OE2 . GLU D 376 ? 0.5678 0.4592 0.6410 0.0273  -0.0791 0.1453  368 GLU D OE2 
17033 N N   . LEU D 377 ? 0.3503 0.2256 0.4518 0.0371  -0.0631 0.0974  369 LEU D N   
17034 C CA  . LEU D 377 ? 0.3005 0.1712 0.3938 0.0317  -0.0592 0.0926  369 LEU D CA  
17035 C C   . LEU D 377 ? 0.3318 0.1937 0.4344 0.0335  -0.0546 0.0814  369 LEU D C   
17036 O O   . LEU D 377 ? 0.3136 0.1784 0.4176 0.0353  -0.0525 0.0720  369 LEU D O   
17037 C CB  . LEU D 377 ? 0.3136 0.1937 0.3955 0.0291  -0.0596 0.0905  369 LEU D CB  
17038 C CG  . LEU D 377 ? 0.3880 0.2789 0.4589 0.0266  -0.0638 0.0997  369 LEU D CG  
17039 C CD1 . LEU D 377 ? 0.3916 0.2914 0.4534 0.0246  -0.0638 0.0954  369 LEU D CD1 
17040 C CD2 . LEU D 377 ? 0.3494 0.2375 0.4115 0.0207  -0.0639 0.1081  369 LEU D CD2 
17041 N N   . PRO D 378 ? 0.3835 0.2351 0.4923 0.0328  -0.0527 0.0816  370 PRO D N   
17042 C CA  . PRO D 378 ? 0.3596 0.2036 0.4757 0.0335  -0.0480 0.0700  370 PRO D CA  
17043 C C   . PRO D 378 ? 0.2866 0.1307 0.3938 0.0289  -0.0448 0.0625  370 PRO D C   
17044 O O   . PRO D 378 ? 0.3396 0.1807 0.4510 0.0297  -0.0412 0.0514  370 PRO D O   
17045 C CB  . PRO D 378 ? 0.3794 0.2127 0.5017 0.0323  -0.0473 0.0739  370 PRO D CB  
17046 C CG  . PRO D 378 ? 0.4270 0.2620 0.5407 0.0286  -0.0505 0.0869  370 PRO D CG  
17047 C CD  . PRO D 378 ? 0.3906 0.2371 0.5001 0.0312  -0.0547 0.0921  370 PRO D CD  
17048 N N   . GLU D 379 ? 0.3102 0.1582 0.4050 0.0238  -0.0459 0.0679  371 GLU D N   
17049 C CA  . GLU D 379 ? 0.2999 0.1489 0.3865 0.0195  -0.0434 0.0612  371 GLU D CA  
17050 C C   . GLU D 379 ? 0.2906 0.1471 0.3748 0.0221  -0.0437 0.0549  371 GLU D C   
17051 O O   . GLU D 379 ? 0.2876 0.1478 0.3635 0.0188  -0.0406 0.0472  371 GLU D O   
17052 C CB  . GLU D 379 ? 0.3343 0.1854 0.4089 0.0130  -0.0443 0.0690  371 GLU D CB  
17053 C CG  . GLU D 379 ? 0.3642 0.2250 0.4306 0.0129  -0.0483 0.0780  371 GLU D CG  
17054 C CD  . GLU D 379 ? 0.3865 0.2473 0.4543 0.0134  -0.0511 0.0892  371 GLU D CD  
17055 O OE1 . GLU D 379 ? 0.3163 0.1715 0.3952 0.0176  -0.0514 0.0894  371 GLU D OE1 
17056 O OE2 . GLU D 379 ? 0.2900 0.1566 0.3476 0.0095  -0.0530 0.0975  371 GLU D OE2 
17057 N N   . LEU D 380 ? 0.3566 0.2192 0.4456 0.0274  -0.0461 0.0566  372 LEU D N   
17058 C CA  . LEU D 380 ? 0.2902 0.1638 0.3744 0.0289  -0.0450 0.0498  372 LEU D CA  
17059 C C   . LEU D 380 ? 0.2698 0.1412 0.3576 0.0301  -0.0403 0.0365  372 LEU D C   
17060 O O   . LEU D 380 ? 0.2884 0.1514 0.3886 0.0334  -0.0391 0.0325  372 LEU D O   
17061 C CB  . LEU D 380 ? 0.3095 0.1895 0.4007 0.0345  -0.0487 0.0543  372 LEU D CB  
17062 C CG  . LEU D 380 ? 0.2602 0.1538 0.3444 0.0349  -0.0483 0.0501  372 LEU D CG  
17063 C CD1 . LEU D 380 ? 0.2531 0.1542 0.3217 0.0293  -0.0492 0.0546  372 LEU D CD1 
17064 C CD2 . LEU D 380 ? 0.2919 0.1909 0.3865 0.0409  -0.0519 0.0538  372 LEU D CD2 
17065 N N   . VAL D 381 ? 0.2514 0.1303 0.3282 0.0271  -0.0376 0.0298  373 VAL D N   
17066 C CA  . VAL D 381 ? 0.2329 0.1121 0.3104 0.0276  -0.0333 0.0177  373 VAL D CA  
17067 C C   . VAL D 381 ? 0.2552 0.1465 0.3265 0.0286  -0.0325 0.0144  373 VAL D C   
17068 O O   . VAL D 381 ? 0.2985 0.1967 0.3585 0.0252  -0.0330 0.0166  373 VAL D O   
17069 C CB  . VAL D 381 ? 0.2462 0.1216 0.3162 0.0222  -0.0308 0.0130  373 VAL D CB  
17070 C CG1 . VAL D 381 ? 0.2790 0.1568 0.3477 0.0224  -0.0269 0.0009  373 VAL D CG1 
17071 C CG2 . VAL D 381 ? 0.2648 0.1281 0.3420 0.0208  -0.0313 0.0160  373 VAL D CG2 
17072 N N   . GLY D 382 ? 0.2117 0.1056 0.2912 0.0333  -0.0312 0.0090  374 GLY D N   
17073 C CA  . GLY D 382 ? 0.2013 0.1064 0.2763 0.0341  -0.0300 0.0055  374 GLY D CA  
17074 C C   . GLY D 382 ? 0.1960 0.1035 0.2638 0.0316  -0.0255 -0.0043 374 GLY D C   
17075 O O   . GLY D 382 ? 0.2458 0.1469 0.3120 0.0293  -0.0236 -0.0090 374 GLY D O   
17076 N N   . GLY D 383 ? 0.1886 0.1056 0.2520 0.0318  -0.0241 -0.0071 375 GLY D N   
17077 C CA  . GLY D 383 ? 0.2028 0.1228 0.2595 0.0297  -0.0201 -0.0156 375 GLY D CA  
17078 C C   . GLY D 383 ? 0.2514 0.1819 0.3037 0.0297  -0.0191 -0.0163 375 GLY D C   
17079 O O   . GLY D 383 ? 0.2124 0.1481 0.2639 0.0300  -0.0218 -0.0102 375 GLY D O   
17080 N N   . SER D 384 ? 0.1755 0.1094 0.2245 0.0290  -0.0151 -0.0239 376 SER D N   
17081 C CA  . SER D 384 ? 0.2180 0.1613 0.2616 0.0280  -0.0137 -0.0245 376 SER D CA  
17082 C C   . SER D 384 ? 0.2040 0.1487 0.2390 0.0250  -0.0101 -0.0310 376 SER D C   
17083 O O   . SER D 384 ? 0.2154 0.1555 0.2506 0.0246  -0.0081 -0.0366 376 SER D O   
17084 C CB  . SER D 384 ? 0.1796 0.1291 0.2331 0.0320  -0.0129 -0.0256 376 SER D CB  
17085 O OG  . SER D 384 ? 0.2256 0.1754 0.2845 0.0339  -0.0086 -0.0338 376 SER D OG  
17086 N N   . ALA D 385 ? 0.1879 0.1392 0.2152 0.0226  -0.0093 -0.0299 377 ALA D N   
17087 C CA  . ALA D 385 ? 0.1941 0.1479 0.2126 0.0197  -0.0063 -0.0345 377 ALA D CA  
17088 C C   . ALA D 385 ? 0.1687 0.1288 0.1907 0.0212  -0.0022 -0.0396 377 ALA D C   
17089 O O   . ALA D 385 ? 0.2257 0.1925 0.2449 0.0201  -0.0008 -0.0386 377 ALA D O   
17090 C CB  . ALA D 385 ? 0.1718 0.1284 0.1810 0.0163  -0.0077 -0.0301 377 ALA D CB  
17091 N N   . ASP D 386 ? 0.2420 0.1998 0.2713 0.0238  0.0000  -0.0454 378 ASP D N   
17092 C CA  . ASP D 386 ? 0.2491 0.2128 0.2829 0.0253  0.0048  -0.0519 378 ASP D CA  
17093 C C   . ASP D 386 ? 0.2815 0.2521 0.3234 0.0278  0.0047  -0.0491 378 ASP D C   
17094 O O   . ASP D 386 ? 0.2249 0.2031 0.2662 0.0271  0.0084  -0.0519 378 ASP D O   
17095 C CB  . ASP D 386 ? 0.3066 0.2746 0.3288 0.0213  0.0084  -0.0558 378 ASP D CB  
17096 C CG  . ASP D 386 ? 0.3321 0.3057 0.3579 0.0222  0.0141  -0.0639 378 ASP D CG  
17097 O OD1 . ASP D 386 ? 0.3762 0.3472 0.4116 0.0253  0.0157  -0.0694 378 ASP D OD1 
17098 O OD2 . ASP D 386 ? 0.3276 0.3082 0.3471 0.0197  0.0173  -0.0647 378 ASP D OD2 
17099 N N   . LEU D 387 ? 0.1893 0.1580 0.2391 0.0306  0.0005  -0.0435 379 LEU D N   
17100 C CA  . LEU D 387 ? 0.2278 0.2035 0.2871 0.0335  -0.0002 -0.0413 379 LEU D CA  
17101 C C   . LEU D 387 ? 0.2725 0.2488 0.3463 0.0384  0.0019  -0.0464 379 LEU D C   
17102 O O   . LEU D 387 ? 0.3251 0.2942 0.4034 0.0402  0.0024  -0.0497 379 LEU D O   
17103 C CB  . LEU D 387 ? 0.1735 0.1481 0.2344 0.0342  -0.0060 -0.0327 379 LEU D CB  
17104 C CG  . LEU D 387 ? 0.2736 0.2495 0.3225 0.0298  -0.0079 -0.0279 379 LEU D CG  
17105 C CD1 . LEU D 387 ? 0.2860 0.2646 0.3377 0.0305  -0.0129 -0.0206 379 LEU D CD1 
17106 C CD2 . LEU D 387 ? 0.2620 0.2447 0.3051 0.0269  -0.0041 -0.0310 379 LEU D CD2 
17107 N N   . THR D 388 ? 0.1909 0.1759 0.2731 0.0404  0.0034  -0.0474 380 THR D N   
17108 C CA  . THR D 388 ? 0.2745 0.2610 0.3731 0.0458  0.0048  -0.0515 380 THR D CA  
17109 C C   . THR D 388 ? 0.2804 0.2618 0.3886 0.0498  -0.0014 -0.0446 380 THR D C   
17110 O O   . THR D 388 ? 0.2887 0.2728 0.3948 0.0491  -0.0062 -0.0369 380 THR D O   
17111 C CB  . THR D 388 ? 0.3294 0.3279 0.4352 0.0468  0.0078  -0.0541 380 THR D CB  
17112 O OG1 . THR D 388 ? 0.4162 0.4190 0.5131 0.0429  0.0140  -0.0604 380 THR D OG1 
17113 C CG2 . THR D 388 ? 0.3720 0.3727 0.4971 0.0529  0.0088  -0.0581 380 THR D CG2 
17114 N N   . PRO D 389 ? 0.3718 0.3460 0.4906 0.0537  -0.0016 -0.0470 381 PRO D N   
17115 C CA  . PRO D 389 ? 0.3708 0.3390 0.4980 0.0572  -0.0078 -0.0391 381 PRO D CA  
17116 C C   . PRO D 389 ? 0.3336 0.3105 0.4718 0.0608  -0.0113 -0.0342 381 PRO D C   
17117 O O   . PRO D 389 ? 0.3606 0.3455 0.5096 0.0637  -0.0083 -0.0394 381 PRO D O   
17118 C CB  . PRO D 389 ? 0.4236 0.3830 0.5625 0.0609  -0.0058 -0.0447 381 PRO D CB  
17119 C CG  . PRO D 389 ? 0.4742 0.4339 0.6061 0.0580  0.0011  -0.0554 381 PRO D CG  
17120 C CD  . PRO D 389 ? 0.3987 0.3702 0.5232 0.0551  0.0041  -0.0573 381 PRO D CD  
17121 N N   . SER D 390 ? 0.3021 0.2785 0.4376 0.0604  -0.0178 -0.0243 382 SER D N   
17122 C CA  . SER D 390 ? 0.2861 0.2708 0.4320 0.0639  -0.0224 -0.0186 382 SER D CA  
17123 C C   . SER D 390 ? 0.3164 0.2953 0.4616 0.0645  -0.0297 -0.0078 382 SER D C   
17124 O O   . SER D 390 ? 0.2635 0.2328 0.3996 0.0618  -0.0305 -0.0050 382 SER D O   
17125 C CB  . SER D 390 ? 0.2422 0.2390 0.3814 0.0604  -0.0218 -0.0186 382 SER D CB  
17126 O OG  . SER D 390 ? 0.2623 0.2580 0.3861 0.0554  -0.0248 -0.0127 382 SER D OG  
17127 N N   . ASN D 391 ? 0.2429 0.2288 0.3978 0.0679  -0.0351 -0.0015 383 ASN D N   
17128 C CA  . ASN D 391 ? 0.2979 0.2800 0.4518 0.0684  -0.0424 0.0098  383 ASN D CA  
17129 C C   . ASN D 391 ? 0.2494 0.2316 0.3843 0.0619  -0.0441 0.0145  383 ASN D C   
17130 O O   . ASN D 391 ? 0.2786 0.2555 0.4091 0.0608  -0.0487 0.0229  383 ASN D O   
17131 C CB  . ASN D 391 ? 0.3532 0.3453 0.5202 0.0728  -0.0481 0.0154  383 ASN D CB  
17132 C CG  . ASN D 391 ? 0.4800 0.4863 0.6419 0.0699  -0.0480 0.0137  383 ASN D CG  
17133 O OD1 . ASN D 391 ? 0.5410 0.5532 0.7054 0.0695  -0.0425 0.0051  383 ASN D OD1 
17134 N ND2 . ASN D 391 ? 0.5053 0.5171 0.6596 0.0673  -0.0539 0.0217  383 ASN D ND2 
17135 N N   . LEU D 392 ? 0.2080 0.1963 0.3321 0.0573  -0.0403 0.0094  384 LEU D N   
17136 C CA  . LEU D 392 ? 0.1864 0.1751 0.2936 0.0513  -0.0414 0.0128  384 LEU D CA  
17137 C C   . LEU D 392 ? 0.2906 0.2680 0.3876 0.0481  -0.0388 0.0116  384 LEU D C   
17138 O O   . LEU D 392 ? 0.2644 0.2402 0.3495 0.0438  -0.0406 0.0160  384 LEU D O   
17139 C CB  . LEU D 392 ? 0.2195 0.2179 0.3203 0.0477  -0.0382 0.0077  384 LEU D CB  
17140 C CG  . LEU D 392 ? 0.3102 0.3215 0.4186 0.0492  -0.0410 0.0089  384 LEU D CG  
17141 C CD1 . LEU D 392 ? 0.2482 0.2673 0.3506 0.0451  -0.0367 0.0032  384 LEU D CD1 
17142 C CD2 . LEU D 392 ? 0.3041 0.3190 0.4100 0.0485  -0.0482 0.0182  384 LEU D CD2 
17143 N N   . THR D 393 ? 0.2571 0.2274 0.3584 0.0497  -0.0344 0.0051  385 THR D N   
17144 C CA  . THR D 393 ? 0.3035 0.2645 0.3951 0.0462  -0.0317 0.0027  385 THR D CA  
17145 C C   . THR D 393 ? 0.2899 0.2399 0.3901 0.0492  -0.0308 0.0008  385 THR D C   
17146 O O   . THR D 393 ? 0.2463 0.1892 0.3402 0.0465  -0.0280 -0.0031 385 THR D O   
17147 C CB  . THR D 393 ? 0.3269 0.2910 0.4101 0.0430  -0.0261 -0.0055 385 THR D CB  
17148 O OG1 . THR D 393 ? 0.3412 0.3076 0.4341 0.0463  -0.0220 -0.0131 385 THR D OG1 
17149 C CG2 . THR D 393 ? 0.3606 0.3342 0.4357 0.0397  -0.0265 -0.0041 385 THR D CG2 
17150 N N   . ASP D 394 ? 0.2978 0.2465 0.4131 0.0547  -0.0332 0.0032  386 ASP D N   
17151 C CA  . ASP D 394 ? 0.2768 0.2151 0.4030 0.0580  -0.0316 -0.0002 386 ASP D CA  
17152 C C   . ASP D 394 ? 0.2766 0.2129 0.4177 0.0634  -0.0368 0.0075  386 ASP D C   
17153 O O   . ASP D 394 ? 0.2635 0.2081 0.4064 0.0647  -0.0413 0.0140  386 ASP D O   
17154 C CB  . ASP D 394 ? 0.3109 0.2515 0.4428 0.0597  -0.0253 -0.0121 386 ASP D CB  
17155 C CG  . ASP D 394 ? 0.3535 0.2830 0.4932 0.0614  -0.0224 -0.0180 386 ASP D CG  
17156 O OD1 . ASP D 394 ? 0.3151 0.2342 0.4559 0.0611  -0.0251 -0.0129 386 ASP D OD1 
17157 O OD2 . ASP D 394 ? 0.3828 0.3142 0.5276 0.0628  -0.0170 -0.0283 386 ASP D OD2 
17158 N N   . TRP D 395 ? 0.3255 0.2507 0.4775 0.0665  -0.0366 0.0067  387 TRP D N   
17159 C CA  . TRP D 395 ? 0.3235 0.2458 0.4920 0.0723  -0.0413 0.0137  387 TRP D CA  
17160 C C   . TRP D 395 ? 0.3362 0.2523 0.5155 0.0748  -0.0365 0.0058  387 TRP D C   
17161 O O   . TRP D 395 ? 0.3187 0.2308 0.4956 0.0731  -0.0308 -0.0044 387 TRP D O   
17162 C CB  . TRP D 395 ? 0.3259 0.2426 0.4878 0.0697  -0.0467 0.0262  387 TRP D CB  
17163 C CG  . TRP D 395 ? 0.3472 0.2510 0.5047 0.0663  -0.0445 0.0257  387 TRP D CG  
17164 C CD1 . TRP D 395 ? 0.3616 0.2567 0.5262 0.0674  -0.0445 0.0281  387 TRP D CD1 
17165 C CD2 . TRP D 395 ? 0.3052 0.2036 0.4505 0.0612  -0.0423 0.0227  387 TRP D CD2 
17166 N NE1 . TRP D 395 ? 0.3465 0.2317 0.5044 0.0630  -0.0422 0.0265  387 TRP D NE1 
17167 C CE2 . TRP D 395 ? 0.3298 0.2169 0.4757 0.0591  -0.0408 0.0231  387 TRP D CE2 
17168 C CE3 . TRP D 395 ? 0.2674 0.1729 0.3963 0.0560  -0.0398 0.0187  387 TRP D CE3 
17169 C CZ2 . TRP D 395 ? 0.2873 0.1676 0.4235 0.0539  -0.0386 0.0204  387 TRP D CZ2 
17170 C CZ3 . TRP D 395 ? 0.2769 0.1765 0.3945 0.0505  -0.0373 0.0161  387 TRP D CZ3 
17171 C CH2 . TRP D 395 ? 0.2426 0.1295 0.3649 0.0498  -0.0370 0.0169  387 TRP D CH2 
17172 N N   . SER D 396 ? 0.3545 0.2698 0.5454 0.0786  -0.0391 0.0107  388 SER D N   
17173 C CA  . SER D 396 ? 0.3837 0.2972 0.5884 0.0823  -0.0350 0.0027  388 SER D CA  
17174 C C   . SER D 396 ? 0.3849 0.2868 0.5883 0.0799  -0.0304 -0.0040 388 SER D C   
17175 O O   . SER D 396 ? 0.3879 0.2901 0.5961 0.0806  -0.0246 -0.0155 388 SER D O   
17176 C CB  . SER D 396 ? 0.3725 0.2865 0.5896 0.0868  -0.0396 0.0109  388 SER D CB  
17177 O OG  . SER D 396 ? 0.3372 0.2414 0.5506 0.0849  -0.0434 0.0207  388 SER D OG  
17178 N N   . ASN D 397 ? 0.3897 0.2820 0.5867 0.0767  -0.0328 0.0028  389 ASN D N   
17179 C CA  . ASN D 397 ? 0.4421 0.3234 0.6394 0.0743  -0.0291 -0.0027 389 ASN D CA  
17180 C C   . ASN D 397 ? 0.4085 0.2856 0.5908 0.0683  -0.0277 -0.0045 389 ASN D C   
17181 O O   . ASN D 397 ? 0.4866 0.3541 0.6666 0.0652  -0.0270 -0.0042 389 ASN D O   
17182 C CB  . ASN D 397 ? 0.5570 0.4297 0.7622 0.0757  -0.0325 0.0057  389 ASN D CB  
17183 C CG  . ASN D 397 ? 0.5743 0.4479 0.7736 0.0747  -0.0390 0.0203  389 ASN D CG  
17184 O OD1 . ASN D 397 ? 0.5013 0.3772 0.6873 0.0708  -0.0405 0.0239  389 ASN D OD1 
17185 N ND2 . ASN D 397 ? 0.5789 0.4513 0.7878 0.0782  -0.0431 0.0285  389 ASN D ND2 
17186 N N   . SER D 398 ? 0.3321 0.2162 0.5045 0.0665  -0.0273 -0.0065 390 SER D N   
17187 C CA  . SER D 398 ? 0.2743 0.1553 0.4334 0.0611  -0.0252 -0.0105 390 SER D CA  
17188 C C   . SER D 398 ? 0.3021 0.1789 0.4624 0.0596  -0.0193 -0.0230 390 SER D C   
17189 O O   . SER D 398 ? 0.2854 0.1667 0.4529 0.0624  -0.0154 -0.0318 390 SER D O   
17190 C CB  . SER D 398 ? 0.2648 0.1548 0.4154 0.0603  -0.0254 -0.0120 390 SER D CB  
17191 O OG  . SER D 398 ? 0.2560 0.1543 0.4130 0.0636  -0.0218 -0.0206 390 SER D OG  
17192 N N   . VAL D 399 ? 0.2556 0.1247 0.4086 0.0549  -0.0185 -0.0240 391 VAL D N   
17193 C CA  . VAL D 399 ? 0.3414 0.2065 0.4940 0.0525  -0.0135 -0.0353 391 VAL D CA  
17194 C C   . VAL D 399 ? 0.3419 0.2095 0.4802 0.0476  -0.0116 -0.0410 391 VAL D C   
17195 O O   . VAL D 399 ? 0.2479 0.1127 0.3773 0.0439  -0.0143 -0.0352 391 VAL D O   
17196 C CB  . VAL D 399 ? 0.3587 0.2131 0.5157 0.0507  -0.0142 -0.0324 391 VAL D CB  
17197 C CG1 . VAL D 399 ? 0.2784 0.1295 0.4334 0.0474  -0.0095 -0.0444 391 VAL D CG1 
17198 C CG2 . VAL D 399 ? 0.2836 0.1352 0.4554 0.0557  -0.0161 -0.0272 391 VAL D CG2 
17199 N N   . SER D 400 ? 0.3133 0.1867 0.4494 0.0475  -0.0069 -0.0524 392 SER D N   
17200 C CA  . SER D 400 ? 0.2611 0.1379 0.3835 0.0429  -0.0051 -0.0583 392 SER D CA  
17201 C C   . SER D 400 ? 0.2904 0.1602 0.4068 0.0378  -0.0048 -0.0608 392 SER D C   
17202 O O   . SER D 400 ? 0.2615 0.1269 0.3836 0.0374  -0.0025 -0.0660 392 SER D O   
17203 C CB  . SER D 400 ? 0.3158 0.2011 0.4370 0.0436  0.0002  -0.0698 392 SER D CB  
17204 O OG  . SER D 400 ? 0.3314 0.2243 0.4581 0.0480  0.0003  -0.0681 392 SER D OG  
17205 N N   . VAL D 401 ? 0.2606 0.1296 0.3660 0.0336  -0.0071 -0.0572 393 VAL D N   
17206 C CA  . VAL D 401 ? 0.2776 0.1424 0.3761 0.0282  -0.0065 -0.0610 393 VAL D CA  
17207 C C   . VAL D 401 ? 0.3271 0.1977 0.4193 0.0261  -0.0022 -0.0734 393 VAL D C   
17208 O O   . VAL D 401 ? 0.2779 0.1566 0.3645 0.0267  -0.0006 -0.0772 393 VAL D O   
17209 C CB  . VAL D 401 ? 0.2815 0.1467 0.3693 0.0241  -0.0100 -0.0534 393 VAL D CB  
17210 C CG1 . VAL D 401 ? 0.3139 0.1756 0.3955 0.0185  -0.0096 -0.0582 393 VAL D CG1 
17211 C CG2 . VAL D 401 ? 0.2969 0.1572 0.3900 0.0256  -0.0140 -0.0409 393 VAL D CG2 
17212 N N   . THR D 402 ? 0.3213 0.1884 0.4142 0.0233  -0.0004 -0.0796 394 THR D N   
17213 C CA  . THR D 402 ? 0.3629 0.2358 0.4492 0.0208  0.0034  -0.0911 394 THR D CA  
17214 C C   . THR D 402 ? 0.3347 0.2048 0.4137 0.0150  0.0024  -0.0938 394 THR D C   
17215 O O   . THR D 402 ? 0.3067 0.1704 0.3871 0.0130  -0.0005 -0.0872 394 THR D O   
17216 C CB  . THR D 402 ? 0.3696 0.2426 0.4660 0.0237  0.0073  -0.0984 394 THR D CB  
17217 O OG1 . THR D 402 ? 0.3358 0.1996 0.4418 0.0236  0.0066  -0.0971 394 THR D OG1 
17218 C CG2 . THR D 402 ? 0.2892 0.1658 0.3943 0.0296  0.0081  -0.0957 394 THR D CG2 
17219 N N   . ARG D 403 ? 0.3795 0.2555 0.4508 0.0119  0.0050  -0.1034 395 ARG D N   
17220 C CA  . ARG D 403 ? 0.3589 0.2339 0.4234 0.0064  0.0039  -0.1068 395 ARG D CA  
17221 C C   . ARG D 403 ? 0.3597 0.2253 0.4344 0.0057  0.0036  -0.1062 395 ARG D C   
17222 O O   . ARG D 403 ? 0.3785 0.2402 0.4511 0.0019  0.0011  -0.1032 395 ARG D O   
17223 C CB  . ARG D 403 ? 0.4149 0.2984 0.4705 0.0038  0.0068  -0.1173 395 ARG D CB  
17224 C CG  . ARG D 403 ? 0.4433 0.3274 0.4915 -0.0020 0.0053  -0.1213 395 ARG D CG  
17225 C CD  . ARG D 403 ? 0.4425 0.3353 0.4822 -0.0044 0.0080  -0.1313 395 ARG D CD  
17226 N NE  . ARG D 403 ? 0.5232 0.4189 0.5536 -0.0100 0.0054  -0.1334 395 ARG D NE  
17227 C CZ  . ARG D 403 ? 0.5573 0.4596 0.5752 -0.0126 0.0027  -0.1309 395 ARG D CZ  
17228 N NH1 . ARG D 403 ? 0.5796 0.4861 0.5928 -0.0104 0.0027  -0.1266 395 ARG D NH1 
17229 N NH2 . ARG D 403 ? 0.4335 0.3387 0.4444 -0.0175 -0.0001 -0.1326 395 ARG D NH2 
17230 N N   . ASP D 404 ? 0.3369 0.1988 0.4233 0.0093  0.0060  -0.1089 396 ASP D N   
17231 C CA  . ASP D 404 ? 0.4131 0.2667 0.5091 0.0084  0.0063  -0.1104 396 ASP D CA  
17232 C C   . ASP D 404 ? 0.3764 0.2209 0.4848 0.0120  0.0046  -0.1010 396 ASP D C   
17233 O O   . ASP D 404 ? 0.4564 0.2931 0.5735 0.0113  0.0048  -0.1012 396 ASP D O   
17234 C CB  . ASP D 404 ? 0.5050 0.3610 0.6055 0.0090  0.0105  -0.1219 396 ASP D CB  
17235 C CG  . ASP D 404 ? 0.6556 0.5209 0.7431 0.0048  0.0121  -0.1309 396 ASP D CG  
17236 O OD1 . ASP D 404 ? 0.5749 0.4412 0.6533 -0.0000 0.0097  -0.1306 396 ASP D OD1 
17237 O OD2 . ASP D 404 ? 0.7538 0.6260 0.8400 0.0063  0.0155  -0.1380 396 ASP D OD2 
17238 N N   . LYS D 405 ? 0.3501 0.1955 0.4595 0.0156  0.0028  -0.0924 397 LYS D N   
17239 C CA  . LYS D 405 ? 0.3125 0.1504 0.4333 0.0192  0.0008  -0.0829 397 LYS D CA  
17240 C C   . LYS D 405 ? 0.3424 0.1815 0.4585 0.0201  -0.0028 -0.0717 397 LYS D C   
17241 O O   . LYS D 405 ? 0.3341 0.1808 0.4422 0.0205  -0.0029 -0.0723 397 LYS D O   
17242 C CB  . LYS D 405 ? 0.3715 0.2099 0.5046 0.0249  0.0031  -0.0860 397 LYS D CB  
17243 N N   . GLY D 406 ? 0.3344 0.1664 0.4558 0.0204  -0.0056 -0.0613 398 GLY D N   
17244 C CA  . GLY D 406 ? 0.2798 0.1127 0.3975 0.0211  -0.0092 -0.0499 398 GLY D CA  
17245 C C   . GLY D 406 ? 0.3537 0.1913 0.4762 0.0270  -0.0099 -0.0466 398 GLY D C   
17246 O O   . GLY D 406 ? 0.3644 0.2048 0.4936 0.0307  -0.0074 -0.0532 398 GLY D O   
17247 N N   . GLY D 407 ? 0.3051 0.1442 0.4243 0.0278  -0.0135 -0.0362 399 GLY D N   
17248 C CA  . GLY D 407 ? 0.3032 0.1472 0.4273 0.0332  -0.0150 -0.0317 399 GLY D CA  
17249 C C   . GLY D 407 ? 0.3284 0.1745 0.4463 0.0325  -0.0193 -0.0203 399 GLY D C   
17250 O O   . GLY D 407 ? 0.3168 0.1595 0.4282 0.0280  -0.0210 -0.0149 399 GLY D O   
17251 N N   . ASN D 408 ? 0.2904 0.1430 0.4104 0.0368  -0.0210 -0.0170 400 ASN D N   
17252 C CA  . ASN D 408 ? 0.2864 0.1424 0.4001 0.0362  -0.0253 -0.0065 400 ASN D CA  
17253 C C   . ASN D 408 ? 0.2928 0.1613 0.3994 0.0374  -0.0247 -0.0090 400 ASN D C   
17254 O O   . ASN D 408 ? 0.2930 0.1680 0.3959 0.0381  -0.0278 -0.0008 400 ASN D O   
17255 C CB  . ASN D 408 ? 0.2510 0.1052 0.3717 0.0389  -0.0291 0.0052  400 ASN D CB  
17256 C CG  . ASN D 408 ? 0.3274 0.1843 0.4607 0.0452  -0.0287 0.0034  400 ASN D CG  
17257 O OD1 . ASN D 408 ? 0.3086 0.1702 0.4451 0.0476  -0.0255 -0.0062 400 ASN D OD1 
17258 N ND2 . ASN D 408 ? 0.3257 0.1803 0.4661 0.0476  -0.0319 0.0126  400 ASN D ND2 
17259 N N   . TYR D 409 ? 0.2288 0.1019 0.3322 0.0370  -0.0205 -0.0200 401 TYR D N   
17260 C CA  . TYR D 409 ? 0.2191 0.1044 0.3150 0.0374  -0.0193 -0.0223 401 TYR D CA  
17261 C C   . TYR D 409 ? 0.2252 0.1137 0.3112 0.0337  -0.0153 -0.0321 401 TYR D C   
17262 O O   . TYR D 409 ? 0.2365 0.1214 0.3275 0.0342  -0.0120 -0.0414 401 TYR D O   
17263 C CB  . TYR D 409 ? 0.2352 0.1248 0.3431 0.0434  -0.0185 -0.0246 401 TYR D CB  
17264 C CG  . TYR D 409 ? 0.2107 0.1129 0.3119 0.0436  -0.0186 -0.0232 401 TYR D CG  
17265 C CD1 . TYR D 409 ? 0.2049 0.1144 0.2976 0.0415  -0.0146 -0.0310 401 TYR D CD1 
17266 C CD2 . TYR D 409 ? 0.2504 0.1572 0.3536 0.0456  -0.0228 -0.0138 401 TYR D CD2 
17267 C CE1 . TYR D 409 ? 0.2806 0.2009 0.3679 0.0413  -0.0145 -0.0294 401 TYR D CE1 
17268 C CE2 . TYR D 409 ? 0.2258 0.1440 0.3237 0.0454  -0.0229 -0.0130 401 TYR D CE2 
17269 C CZ  . TYR D 409 ? 0.2869 0.2113 0.3772 0.0432  -0.0186 -0.0208 401 TYR D CZ  
17270 O OH  . TYR D 409 ? 0.2653 0.2005 0.3511 0.0428  -0.0185 -0.0197 401 TYR D OH  
17271 N N   . ILE D 410 ? 0.2257 0.1212 0.2981 0.0300  -0.0158 -0.0300 402 ILE D N   
17272 C CA  . ILE D 410 ? 0.2517 0.1503 0.3134 0.0260  -0.0131 -0.0371 402 ILE D CA  
17273 C C   . ILE D 410 ? 0.2208 0.1297 0.2777 0.0268  -0.0106 -0.0409 402 ILE D C   
17274 O O   . ILE D 410 ? 0.2460 0.1614 0.2993 0.0272  -0.0121 -0.0353 402 ILE D O   
17275 C CB  . ILE D 410 ? 0.1993 0.0978 0.2501 0.0212  -0.0153 -0.0321 402 ILE D CB  
17276 C CG1 . ILE D 410 ? 0.3039 0.1924 0.3597 0.0197  -0.0172 -0.0285 402 ILE D CG1 
17277 C CG2 . ILE D 410 ? 0.1959 0.0991 0.2359 0.0175  -0.0133 -0.0384 402 ILE D CG2 
17278 C CD1 . ILE D 410 ? 0.2679 0.1571 0.3158 0.0158  -0.0199 -0.0206 402 ILE D CD1 
17279 N N   . HIS D 411 ? 0.2012 0.1119 0.2576 0.0267  -0.0067 -0.0506 403 HIS D N   
17280 C CA  . HIS D 411 ? 0.1967 0.1171 0.2465 0.0262  -0.0037 -0.0545 403 HIS D CA  
17281 C C   . HIS D 411 ? 0.2407 0.1641 0.2759 0.0212  -0.0041 -0.0542 403 HIS D C   
17282 O O   . HIS D 411 ? 0.2303 0.1522 0.2607 0.0185  -0.0026 -0.0606 403 HIS D O   
17283 C CB  . HIS D 411 ? 0.2034 0.1252 0.2590 0.0280  0.0010  -0.0649 403 HIS D CB  
17284 C CG  . HIS D 411 ? 0.2805 0.1993 0.3524 0.0335  0.0015  -0.0658 403 HIS D CG  
17285 N ND1 . HIS D 411 ? 0.3045 0.2292 0.3830 0.0371  0.0011  -0.0619 403 HIS D ND1 
17286 C CD2 . HIS D 411 ? 0.3208 0.2314 0.4050 0.0360  0.0022  -0.0701 403 HIS D CD2 
17287 C CE1 . HIS D 411 ? 0.3097 0.2304 0.4039 0.0420  0.0013  -0.0635 403 HIS D CE1 
17288 N NE2 . HIS D 411 ? 0.3137 0.2252 0.4117 0.0415  0.0021  -0.0683 403 HIS D NE2 
17289 N N   . TYR D 412 ? 0.2102 0.1381 0.2389 0.0199  -0.0063 -0.0471 404 TYR D N   
17290 C CA  . TYR D 412 ? 0.1801 0.1108 0.1966 0.0156  -0.0070 -0.0463 404 TYR D CA  
17291 C C   . TYR D 412 ? 0.2179 0.1556 0.2270 0.0142  -0.0037 -0.0513 404 TYR D C   
17292 O O   . TYR D 412 ? 0.2412 0.1808 0.2406 0.0108  -0.0042 -0.0516 404 TYR D O   
17293 C CB  . TYR D 412 ? 0.1731 0.1059 0.1858 0.0146  -0.0100 -0.0377 404 TYR D CB  
17294 C CG  . TYR D 412 ? 0.2284 0.1550 0.2452 0.0146  -0.0132 -0.0321 404 TYR D CG  
17295 C CD1 . TYR D 412 ? 0.1741 0.0966 0.1868 0.0113  -0.0147 -0.0313 404 TYR D CD1 
17296 C CD2 . TYR D 412 ? 0.1926 0.1178 0.2175 0.0177  -0.0148 -0.0273 404 TYR D CD2 
17297 C CE1 . TYR D 412 ? 0.2454 0.1625 0.2614 0.0107  -0.0171 -0.0259 404 TYR D CE1 
17298 C CE2 . TYR D 412 ? 0.2063 0.1261 0.2340 0.0173  -0.0177 -0.0213 404 TYR D CE2 
17299 C CZ  . TYR D 412 ? 0.2453 0.1609 0.2683 0.0136  -0.0185 -0.0207 404 TYR D CZ  
17300 O OH  . TYR D 412 ? 0.2633 0.1737 0.2888 0.0126  -0.0209 -0.0145 404 TYR D OH  
17301 N N   . GLY D 413 ? 0.2164 0.1584 0.2300 0.0167  -0.0005 -0.0551 405 GLY D N   
17302 C CA  . GLY D 413 ? 0.2367 0.1861 0.2428 0.0149  0.0029  -0.0588 405 GLY D CA  
17303 C C   . GLY D 413 ? 0.2084 0.1628 0.2080 0.0133  0.0015  -0.0520 405 GLY D C   
17304 O O   . GLY D 413 ? 0.2055 0.1589 0.2081 0.0143  -0.0014 -0.0456 405 GLY D O   
17305 N N   . VAL D 414 ? 0.2058 0.1655 0.1961 0.0105  0.0035  -0.0534 406 VAL D N   
17306 C CA  . VAL D 414 ? 0.2270 0.1913 0.2124 0.0091  0.0029  -0.0476 406 VAL D CA  
17307 C C   . VAL D 414 ? 0.2267 0.1882 0.2054 0.0065  -0.0009 -0.0429 406 VAL D C   
17308 O O   . VAL D 414 ? 0.1856 0.1494 0.1555 0.0037  -0.0008 -0.0423 406 VAL D O   
17309 C CB  . VAL D 414 ? 0.1710 0.1422 0.1505 0.0073  0.0070  -0.0503 406 VAL D CB  
17310 C CG1 . VAL D 414 ? 0.2097 0.1850 0.1873 0.0062  0.0068  -0.0444 406 VAL D CG1 
17311 C CG2 . VAL D 414 ? 0.2544 0.2287 0.2412 0.0096  0.0113  -0.0568 406 VAL D CG2 
17312 N N   . ARG D 415 ? 0.1843 0.1410 0.1672 0.0074  -0.0041 -0.0392 407 ARG D N   
17313 C CA  . ARG D 415 ? 0.1755 0.1290 0.1541 0.0052  -0.0074 -0.0362 407 ARG D CA  
17314 C C   . ARG D 415 ? 0.1642 0.1159 0.1469 0.0060  -0.0100 -0.0304 407 ARG D C   
17315 O O   . ARG D 415 ? 0.2029 0.1498 0.1891 0.0063  -0.0119 -0.0292 407 ARG D O   
17316 C CB  . ARG D 415 ? 0.1654 0.1138 0.1443 0.0045  -0.0081 -0.0405 407 ARG D CB  
17317 C CG  . ARG D 415 ? 0.1767 0.1270 0.1512 0.0034  -0.0056 -0.0475 407 ARG D CG  
17318 C CD  . ARG D 415 ? 0.1927 0.1376 0.1687 0.0023  -0.0068 -0.0519 407 ARG D CD  
17319 N NE  . ARG D 415 ? 0.2102 0.1571 0.1816 0.0006  -0.0047 -0.0596 407 ARG D NE  
17320 C CZ  . ARG D 415 ? 0.2421 0.1877 0.2185 0.0021  -0.0016 -0.0667 407 ARG D CZ  
17321 N NH1 . ARG D 415 ? 0.2382 0.1802 0.2254 0.0057  -0.0006 -0.0665 407 ARG D NH1 
17322 N NH2 . ARG D 415 ? 0.2552 0.2034 0.2264 -0.0000 0.0003  -0.0742 407 ARG D NH2 
17323 N N   . GLU D 416 ? 0.1486 0.1045 0.1306 0.0058  -0.0100 -0.0267 408 GLU D N   
17324 C CA  . GLU D 416 ? 0.1443 0.0999 0.1300 0.0065  -0.0121 -0.0219 408 GLU D CA  
17325 C C   . GLU D 416 ? 0.1458 0.0986 0.1286 0.0043  -0.0146 -0.0190 408 GLU D C   
17326 O O   . GLU D 416 ? 0.1435 0.0935 0.1294 0.0046  -0.0164 -0.0164 408 GLU D O   
17327 C CB  . GLU D 416 ? 0.1528 0.1141 0.1388 0.0064  -0.0113 -0.0197 408 GLU D CB  
17328 C CG  . GLU D 416 ? 0.1846 0.1497 0.1755 0.0086  -0.0089 -0.0221 408 GLU D CG  
17329 C CD  . GLU D 416 ? 0.2105 0.1783 0.1973 0.0076  -0.0056 -0.0259 408 GLU D CD  
17330 O OE1 . GLU D 416 ? 0.2269 0.1939 0.2064 0.0052  -0.0057 -0.0257 408 GLU D OE1 
17331 O OE2 . GLU D 416 ? 0.2982 0.2692 0.2890 0.0092  -0.0029 -0.0290 408 GLU D OE2 
17332 N N   . PHE D 417 ? 0.1838 0.1376 0.1609 0.0020  -0.0147 -0.0191 409 PHE D N   
17333 C CA  . PHE D 417 ? 0.2143 0.1663 0.1899 0.0001  -0.0168 -0.0171 409 PHE D CA  
17334 C C   . PHE D 417 ? 0.2026 0.1496 0.1799 -0.0002 -0.0178 -0.0189 409 PHE D C   
17335 O O   . PHE D 417 ? 0.1713 0.1159 0.1508 -0.0011 -0.0192 -0.0164 409 PHE D O   
17336 C CB  . PHE D 417 ? 0.1950 0.1492 0.1656 -0.0018 -0.0171 -0.0170 409 PHE D CB  
17337 C CG  . PHE D 417 ? 0.2181 0.1723 0.1888 -0.0034 -0.0188 -0.0144 409 PHE D CG  
17338 C CD1 . PHE D 417 ? 0.1491 0.1017 0.1229 -0.0039 -0.0197 -0.0126 409 PHE D CD1 
17339 C CD2 . PHE D 417 ? 0.1810 0.1372 0.1491 -0.0046 -0.0194 -0.0136 409 PHE D CD2 
17340 C CE1 . PHE D 417 ? 0.2042 0.1577 0.1785 -0.0056 -0.0207 -0.0110 409 PHE D CE1 
17341 C CE2 . PHE D 417 ? 0.1794 0.1361 0.1491 -0.0059 -0.0208 -0.0118 409 PHE D CE2 
17342 C CZ  . PHE D 417 ? 0.1858 0.1414 0.1585 -0.0065 -0.0211 -0.0110 409 PHE D CZ  
17343 N N   . GLY D 418 ? 0.1632 0.1088 0.1395 0.0000  -0.0169 -0.0234 410 GLY D N   
17344 C CA  . GLY D 418 ? 0.1925 0.1329 0.1715 -0.0003 -0.0175 -0.0259 410 GLY D CA  
17345 C C   . GLY D 418 ? 0.1624 0.0989 0.1483 0.0014  -0.0179 -0.0236 410 GLY D C   
17346 O O   . GLY D 418 ? 0.1777 0.1100 0.1660 0.0003  -0.0192 -0.0219 410 GLY D O   
17347 N N   . MET D 419 ? 0.1544 0.0926 0.1436 0.0042  -0.0167 -0.0231 411 MET D N   
17348 C CA  . MET D 419 ? 0.1563 0.0913 0.1525 0.0063  -0.0176 -0.0200 411 MET D CA  
17349 C C   . MET D 419 ? 0.1534 0.0883 0.1488 0.0047  -0.0198 -0.0139 411 MET D C   
17350 O O   . MET D 419 ? 0.2004 0.1303 0.1991 0.0043  -0.0211 -0.0114 411 MET D O   
17351 C CB  . MET D 419 ? 0.1554 0.0942 0.1554 0.0094  -0.0165 -0.0201 411 MET D CB  
17352 C CG  . MET D 419 ? 0.1874 0.1243 0.1947 0.0118  -0.0183 -0.0155 411 MET D CG  
17353 S SD  . MET D 419 ? 0.2204 0.1626 0.2346 0.0159  -0.0173 -0.0161 411 MET D SD  
17354 C CE  . MET D 419 ? 0.1729 0.1233 0.1813 0.0140  -0.0179 -0.0127 411 MET D CE  
17355 N N   . GLY D 420 ? 0.1643 0.1047 0.1556 0.0036  -0.0200 -0.0115 412 GLY D N   
17356 C CA  . GLY D 420 ? 0.1455 0.0867 0.1357 0.0018  -0.0216 -0.0066 412 GLY D CA  
17357 C C   . GLY D 420 ? 0.2036 0.1413 0.1925 -0.0010 -0.0222 -0.0062 412 GLY D C   
17358 O O   . GLY D 420 ? 0.1813 0.1166 0.1718 -0.0021 -0.0233 -0.0024 412 GLY D O   
17359 N N   . ALA D 421 ? 0.1830 0.1207 0.1692 -0.0024 -0.0217 -0.0099 413 ALA D N   
17360 C CA  . ALA D 421 ? 0.2117 0.1471 0.1975 -0.0053 -0.0224 -0.0099 413 ALA D CA  
17361 C C   . ALA D 421 ? 0.1836 0.1122 0.1736 -0.0055 -0.0227 -0.0110 413 ALA D C   
17362 O O   . ALA D 421 ? 0.1844 0.1105 0.1759 -0.0080 -0.0232 -0.0091 413 ALA D O   
17363 C CB  . ALA D 421 ? 0.1941 0.1322 0.1763 -0.0067 -0.0224 -0.0132 413 ALA D CB  
17364 N N   . ILE D 422 ? 0.1957 0.1215 0.1884 -0.0031 -0.0219 -0.0143 414 ILE D N   
17365 C CA  . ILE D 422 ? 0.1735 0.0921 0.1718 -0.0030 -0.0220 -0.0157 414 ILE D CA  
17366 C C   . ILE D 422 ? 0.2022 0.1174 0.2049 -0.0022 -0.0230 -0.0094 414 ILE D C   
17367 O O   . ILE D 422 ? 0.2152 0.1247 0.2216 -0.0039 -0.0235 -0.0075 414 ILE D O   
17368 C CB  . ILE D 422 ? 0.1805 0.0973 0.1813 -0.0004 -0.0206 -0.0217 414 ILE D CB  
17369 C CG1 . ILE D 422 ? 0.2233 0.1429 0.2190 -0.0022 -0.0199 -0.0278 414 ILE D CG1 
17370 C CG2 . ILE D 422 ? 0.2225 0.1311 0.2315 0.0005  -0.0204 -0.0228 414 ILE D CG2 
17371 C CD1 . ILE D 422 ? 0.2332 0.1529 0.2297 -0.0003 -0.0179 -0.0343 414 ILE D CD1 
17372 N N   . MET D 423 ? 0.1778 0.0968 0.1804 0.0001  -0.0234 -0.0058 415 MET D N   
17373 C CA  . MET D 423 ? 0.1991 0.1164 0.2049 0.0009  -0.0249 0.0010  415 MET D CA  
17374 C C   . MET D 423 ? 0.1684 0.0861 0.1707 -0.0031 -0.0256 0.0057  415 MET D C   
17375 O O   . MET D 423 ? 0.1744 0.0877 0.1796 -0.0040 -0.0267 0.0109  415 MET D O   
17376 C CB  . MET D 423 ? 0.1728 0.0962 0.1781 0.0035  -0.0256 0.0034  415 MET D CB  
17377 C CG  . MET D 423 ? 0.2418 0.1646 0.2531 0.0078  -0.0250 0.0004  415 MET D CG  
17378 S SD  . MET D 423 ? 0.3479 0.2799 0.3586 0.0101  -0.0257 0.0027  415 MET D SD  
17379 C CE  . MET D 423 ? 0.3670 0.3000 0.3773 0.0090  -0.0290 0.0118  415 MET D CE  
17380 N N   . ASN D 424 ? 0.2085 0.1317 0.2051 -0.0055 -0.0250 0.0043  416 ASN D N   
17381 C CA  . ASN D 424 ? 0.2090 0.1334 0.2030 -0.0095 -0.0249 0.0075  416 ASN D CA  
17382 C C   . ASN D 424 ? 0.2137 0.1313 0.2113 -0.0119 -0.0247 0.0070  416 ASN D C   
17383 O O   . ASN D 424 ? 0.1999 0.1154 0.1982 -0.0145 -0.0249 0.0120  416 ASN D O   
17384 C CB  . ASN D 424 ? 0.1551 0.0861 0.1444 -0.0112 -0.0240 0.0047  416 ASN D CB  
17385 C CG  . ASN D 424 ? 0.2303 0.1679 0.2165 -0.0099 -0.0240 0.0058  416 ASN D CG  
17386 O OD1 . ASN D 424 ? 0.2094 0.1478 0.1963 -0.0083 -0.0249 0.0091  416 ASN D OD1 
17387 N ND2 . ASN D 424 ? 0.1920 0.1344 0.1755 -0.0107 -0.0231 0.0030  416 ASN D ND2 
17388 N N   . GLY D 425 ? 0.2215 0.1358 0.2214 -0.0113 -0.0243 0.0011  417 GLY D N   
17389 C CA  . GLY D 425 ? 0.2257 0.1336 0.2297 -0.0138 -0.0241 -0.0003 417 GLY D CA  
17390 C C   . GLY D 425 ? 0.2005 0.1001 0.2110 -0.0125 -0.0246 0.0029  417 GLY D C   
17391 O O   . GLY D 425 ? 0.2033 0.0976 0.2172 -0.0155 -0.0245 0.0055  417 GLY D O   
17392 N N   . LEU D 426 ? 0.1854 0.0838 0.1987 -0.0082 -0.0250 0.0028  418 LEU D N   
17393 C CA  . LEU D 426 ? 0.1941 0.0846 0.2149 -0.0062 -0.0258 0.0068  418 LEU D CA  
17394 C C   . LEU D 426 ? 0.1973 0.0876 0.2169 -0.0083 -0.0271 0.0163  418 LEU D C   
17395 O O   . LEU D 426 ? 0.2258 0.1085 0.2506 -0.0096 -0.0276 0.0205  418 LEU D O   
17396 C CB  . LEU D 426 ? 0.1938 0.0851 0.2183 -0.0009 -0.0262 0.0056  418 LEU D CB  
17397 C CG  . LEU D 426 ? 0.2219 0.1122 0.2493 0.0015  -0.0245 -0.0035 418 LEU D CG  
17398 C CD1 . LEU D 426 ? 0.2320 0.1262 0.2616 0.0064  -0.0245 -0.0039 418 LEU D CD1 
17399 C CD2 . LEU D 426 ? 0.2199 0.1000 0.2559 0.0014  -0.0238 -0.0067 418 LEU D CD2 
17400 N N   . VAL D 427 ? 0.2116 0.1102 0.2244 -0.0087 -0.0277 0.0197  419 VAL D N   
17401 C CA  . VAL D 427 ? 0.2749 0.1752 0.2847 -0.0111 -0.0288 0.0284  419 VAL D CA  
17402 C C   . VAL D 427 ? 0.2299 0.1284 0.2381 -0.0166 -0.0274 0.0298  419 VAL D C   
17403 O O   . VAL D 427 ? 0.2343 0.1287 0.2439 -0.0190 -0.0279 0.0367  419 VAL D O   
17404 C CB  . VAL D 427 ? 0.3045 0.2151 0.3071 -0.0108 -0.0292 0.0299  419 VAL D CB  
17405 C CG1 . VAL D 427 ? 0.3271 0.2408 0.3249 -0.0145 -0.0299 0.0377  419 VAL D CG1 
17406 C CG2 . VAL D 427 ? 0.4126 0.3253 0.4177 -0.0059 -0.0308 0.0298  419 VAL D CG2 
17407 N N   . LEU D 428 ? 0.2214 0.1239 0.2266 -0.0188 -0.0257 0.0237  420 LEU D N   
17408 C CA  . LEU D 428 ? 0.1927 0.0955 0.1970 -0.0241 -0.0242 0.0244  420 LEU D CA  
17409 C C   . LEU D 428 ? 0.2539 0.1469 0.2652 -0.0260 -0.0240 0.0250  420 LEU D C   
17410 O O   . LEU D 428 ? 0.3180 0.2094 0.3298 -0.0306 -0.0230 0.0290  420 LEU D O   
17411 C CB  . LEU D 428 ? 0.1913 0.1003 0.1931 -0.0254 -0.0230 0.0172  420 LEU D CB  
17412 C CG  . LEU D 428 ? 0.2345 0.1532 0.2300 -0.0253 -0.0225 0.0169  420 LEU D CG  
17413 C CD1 . LEU D 428 ? 0.2451 0.1682 0.2398 -0.0248 -0.0221 0.0098  420 LEU D CD1 
17414 C CD2 . LEU D 428 ? 0.1917 0.1147 0.1840 -0.0297 -0.0212 0.0215  420 LEU D CD2 
17415 N N   . HIS D 429 ? 0.2423 0.1287 0.2596 -0.0227 -0.0246 0.0207  421 HIS D N   
17416 C CA  . HIS D 429 ? 0.2137 0.0903 0.2388 -0.0246 -0.0242 0.0199  421 HIS D CA  
17417 C C   . HIS D 429 ? 0.2241 0.0939 0.2526 -0.0257 -0.0249 0.0296  421 HIS D C   
17418 O O   . HIS D 429 ? 0.2373 0.1012 0.2697 -0.0299 -0.0240 0.0319  421 HIS D O   
17419 C CB  . HIS D 429 ? 0.2984 0.1697 0.3293 -0.0206 -0.0243 0.0126  421 HIS D CB  
17420 C CG  . HIS D 429 ? 0.2251 0.0861 0.2649 -0.0226 -0.0237 0.0102  421 HIS D CG  
17421 N ND1 . HIS D 429 ? 0.2358 0.0868 0.2834 -0.0216 -0.0243 0.0158  421 HIS D ND1 
17422 C CD2 . HIS D 429 ? 0.2370 0.0960 0.2795 -0.0257 -0.0227 0.0027  421 HIS D CD2 
17423 C CE1 . HIS D 429 ? 0.3128 0.1556 0.3681 -0.0241 -0.0233 0.0116  421 HIS D CE1 
17424 N NE2 . HIS D 429 ? 0.2488 0.0967 0.3009 -0.0268 -0.0223 0.0033  421 HIS D NE2 
17425 N N   . GLY D 430 ? 0.2544 0.1254 0.2816 -0.0222 -0.0267 0.0358  422 GLY D N   
17426 C CA  . GLY D 430 ? 0.2363 0.1004 0.2677 -0.0220 -0.0283 0.0456  422 GLY D CA  
17427 C C   . GLY D 430 ? 0.3161 0.1701 0.3583 -0.0173 -0.0294 0.0442  422 GLY D C   
17428 O O   . GLY D 430 ? 0.3052 0.1555 0.3527 -0.0160 -0.0282 0.0351  422 GLY D O   
17429 N N   . GLY D 431 ? 0.2715 0.1217 0.3175 -0.0146 -0.0319 0.0532  423 GLY D N   
17430 C CA  . GLY D 431 ? 0.2599 0.0997 0.3182 -0.0101 -0.0331 0.0534  423 GLY D CA  
17431 C C   . GLY D 431 ? 0.2554 0.0988 0.3169 -0.0032 -0.0346 0.0504  423 GLY D C   
17432 O O   . GLY D 431 ? 0.2987 0.1366 0.3699 0.0013  -0.0355 0.0517  423 GLY D O   
17433 N N   . VAL D 432 ? 0.2951 0.1495 0.3484 -0.0021 -0.0341 0.0453  424 VAL D N   
17434 C CA  . VAL D 432 ? 0.3018 0.1610 0.3577 0.0038  -0.0352 0.0424  424 VAL D CA  
17435 C C   . VAL D 432 ? 0.2923 0.1637 0.3376 0.0034  -0.0365 0.0459  424 VAL D C   
17436 O O   . VAL D 432 ? 0.2661 0.1432 0.3017 -0.0012 -0.0356 0.0467  424 VAL D O   
17437 C CB  . VAL D 432 ? 0.2575 0.1172 0.3159 0.0060  -0.0324 0.0297  424 VAL D CB  
17438 C CG1 . VAL D 432 ? 0.2610 0.1087 0.3308 0.0066  -0.0310 0.0249  424 VAL D CG1 
17439 C CG2 . VAL D 432 ? 0.2935 0.1605 0.3411 0.0020  -0.0303 0.0236  424 VAL D CG2 
17440 N N   . LYS D 433 ? 0.2492 0.1249 0.2976 0.0084  -0.0387 0.0476  425 LYS D N   
17441 C CA  A LYS D 433 ? 0.2690 0.1566 0.3090 0.0085  -0.0400 0.0496  425 LYS D CA  
17442 C CA  B LYS D 433 ? 0.2621 0.1498 0.3020 0.0085  -0.0400 0.0495  425 LYS D CA  
17443 C C   . LYS D 433 ? 0.2560 0.1488 0.2983 0.0126  -0.0388 0.0411  425 LYS D C   
17444 O O   . LYS D 433 ? 0.2545 0.1466 0.3059 0.0178  -0.0402 0.0414  425 LYS D O   
17445 C CB  A LYS D 433 ? 0.2394 0.1291 0.2805 0.0099  -0.0444 0.0608  425 LYS D CB  
17446 C CB  B LYS D 433 ? 0.2481 0.1381 0.2889 0.0098  -0.0443 0.0607  425 LYS D CB  
17447 C CG  A LYS D 433 ? 0.2210 0.1236 0.2532 0.0094  -0.0459 0.0625  425 LYS D CG  
17448 C CG  B LYS D 433 ? 0.2520 0.1401 0.2866 0.0045  -0.0453 0.0698  425 LYS D CG  
17449 C CD  A LYS D 433 ? 0.2335 0.1392 0.2643 0.0093  -0.0506 0.0743  425 LYS D CD  
17450 C CD  B LYS D 433 ? 0.2480 0.1411 0.2801 0.0050  -0.0499 0.0810  425 LYS D CD  
17451 C CE  A LYS D 433 ? 0.2672 0.1707 0.2902 0.0032  -0.0504 0.0814  425 LYS D CE  
17452 C CE  B LYS D 433 ? 0.2619 0.1690 0.2840 0.0040  -0.0504 0.0794  425 LYS D CE  
17453 N NZ  A LYS D 433 ? 0.2693 0.1790 0.2814 -0.0020 -0.0467 0.0756  425 LYS D NZ  
17454 N NZ  B LYS D 433 ? 0.2618 0.1735 0.2730 -0.0018 -0.0468 0.0750  425 LYS D NZ  
17455 N N   . PRO D 434 ? 0.2438 0.1422 0.2790 0.0106  -0.0360 0.0338  426 PRO D N   
17456 C CA  . PRO D 434 ? 0.2391 0.1416 0.2764 0.0140  -0.0343 0.0257  426 PRO D CA  
17457 C C   . PRO D 434 ? 0.2395 0.1529 0.2721 0.0150  -0.0353 0.0267  426 PRO D C   
17458 O O   . PRO D 434 ? 0.2558 0.1749 0.2802 0.0118  -0.0363 0.0306  426 PRO D O   
17459 C CB  . PRO D 434 ? 0.2504 0.1521 0.2823 0.0109  -0.0310 0.0178  426 PRO D CB  
17460 C CG  . PRO D 434 ? 0.2751 0.1793 0.2985 0.0058  -0.0314 0.0221  426 PRO D CG  
17461 C CD  . PRO D 434 ? 0.2681 0.1681 0.2943 0.0052  -0.0341 0.0319  426 PRO D CD  
17462 N N   . PHE D 435 ? 0.2401 0.1565 0.2785 0.0192  -0.0348 0.0226  427 PHE D N   
17463 C CA  . PHE D 435 ? 0.1799 0.1066 0.2142 0.0197  -0.0344 0.0205  427 PHE D CA  
17464 C C   . PHE D 435 ? 0.2630 0.1907 0.2981 0.0208  -0.0306 0.0112  427 PHE D C   
17465 O O   . PHE D 435 ? 0.2213 0.1427 0.2620 0.0224  -0.0288 0.0065  427 PHE D O   
17466 C CB  . PHE D 435 ? 0.1940 0.1261 0.2345 0.0234  -0.0378 0.0256  427 PHE D CB  
17467 C CG  . PHE D 435 ? 0.2286 0.1579 0.2822 0.0290  -0.0377 0.0231  427 PHE D CG  
17468 C CD1 . PHE D 435 ? 0.2210 0.1553 0.2780 0.0313  -0.0348 0.0157  427 PHE D CD1 
17469 C CD2 . PHE D 435 ? 0.2475 0.1697 0.3107 0.0319  -0.0404 0.0286  427 PHE D CD2 
17470 C CE1 . PHE D 435 ? 0.2129 0.1455 0.2828 0.0365  -0.0343 0.0127  427 PHE D CE1 
17471 C CE2 . PHE D 435 ? 0.2423 0.1622 0.3192 0.0375  -0.0403 0.0260  427 PHE D CE2 
17472 C CZ  . PHE D 435 ? 0.2242 0.1496 0.3045 0.0398  -0.0371 0.0176  427 PHE D CZ  
17473 N N   . GLY D 436 ? 0.2039 0.1394 0.2327 0.0195  -0.0293 0.0084  428 GLY D N   
17474 C CA  . GLY D 436 ? 0.1925 0.1302 0.2208 0.0201  -0.0258 0.0006  428 GLY D CA  
17475 C C   . GLY D 436 ? 0.1896 0.1367 0.2164 0.0206  -0.0253 -0.0002 428 GLY D C   
17476 O O   . GLY D 436 ? 0.1854 0.1373 0.2061 0.0180  -0.0264 0.0028  428 GLY D O   
17477 N N   . ALA D 437 ? 0.1784 0.1284 0.2113 0.0235  -0.0232 -0.0047 429 ALA D N   
17478 C CA  . ALA D 437 ? 0.1954 0.1545 0.2291 0.0242  -0.0228 -0.0051 429 ALA D CA  
17479 C C   . ALA D 437 ? 0.1911 0.1534 0.2201 0.0226  -0.0186 -0.0113 429 ALA D C   
17480 O O   . ALA D 437 ? 0.1844 0.1431 0.2134 0.0229  -0.0158 -0.0165 429 ALA D O   
17481 C CB  . ALA D 437 ? 0.1569 0.1186 0.2026 0.0289  -0.0239 -0.0046 429 ALA D CB  
17482 N N   . THR D 438 ? 0.1998 0.1691 0.2251 0.0207  -0.0183 -0.0106 430 THR D N   
17483 C CA  . THR D 438 ? 0.1878 0.1616 0.2104 0.0195  -0.0145 -0.0151 430 THR D CA  
17484 C C   . THR D 438 ? 0.1889 0.1711 0.2139 0.0191  -0.0150 -0.0135 430 THR D C   
17485 O O   . THR D 438 ? 0.1778 0.1626 0.2062 0.0200  -0.0185 -0.0093 430 THR D O   
17486 C CB  . THR D 438 ? 0.2267 0.1976 0.2392 0.0158  -0.0131 -0.0163 430 THR D CB  
17487 O OG1 . THR D 438 ? 0.1913 0.1663 0.2009 0.0145  -0.0095 -0.0199 430 THR D OG1 
17488 C CG2 . THR D 438 ? 0.1360 0.1073 0.1431 0.0130  -0.0156 -0.0119 430 THR D CG2 
17489 N N   . PHE D 439 ? 0.1597 0.1467 0.1831 0.0177  -0.0116 -0.0167 431 PHE D N   
17490 C CA  . PHE D 439 ? 0.1649 0.1596 0.1900 0.0163  -0.0118 -0.0156 431 PHE D CA  
17491 C C   . PHE D 439 ? 0.1524 0.1464 0.1706 0.0130  -0.0141 -0.0122 431 PHE D C   
17492 O O   . PHE D 439 ? 0.1842 0.1729 0.1952 0.0110  -0.0138 -0.0119 431 PHE D O   
17493 C CB  . PHE D 439 ? 0.1304 0.1294 0.1546 0.0147  -0.0072 -0.0193 431 PHE D CB  
17494 C CG  . PHE D 439 ? 0.2685 0.2713 0.3008 0.0175  -0.0042 -0.0234 431 PHE D CG  
17495 C CD1 . PHE D 439 ? 0.2868 0.2874 0.3266 0.0216  -0.0054 -0.0243 431 PHE D CD1 
17496 C CD2 . PHE D 439 ? 0.3948 0.4035 0.4278 0.0159  0.0000  -0.0263 431 PHE D CD2 
17497 C CE1 . PHE D 439 ? 0.3053 0.3100 0.3538 0.0244  -0.0022 -0.0289 431 PHE D CE1 
17498 C CE2 . PHE D 439 ? 0.3746 0.3879 0.4154 0.0181  0.0034  -0.0307 431 PHE D CE2 
17499 C CZ  . PHE D 439 ? 0.2851 0.2965 0.3339 0.0225  0.0024  -0.0323 431 PHE D CZ  
17500 N N   . LEU D 440 ? 0.1503 0.1506 0.1712 0.0122  -0.0162 -0.0102 432 LEU D N   
17501 C CA  . LEU D 440 ? 0.1232 0.1238 0.1382 0.0089  -0.0180 -0.0079 432 LEU D CA  
17502 C C   . LEU D 440 ? 0.1699 0.1681 0.1788 0.0058  -0.0149 -0.0098 432 LEU D C   
17503 O O   . LEU D 440 ? 0.1295 0.1242 0.1327 0.0037  -0.0157 -0.0086 432 LEU D O   
17504 C CB  . LEU D 440 ? 0.1218 0.1307 0.1408 0.0081  -0.0202 -0.0068 432 LEU D CB  
17505 C CG  . LEU D 440 ? 0.1313 0.1415 0.1446 0.0044  -0.0217 -0.0056 432 LEU D CG  
17506 C CD1 . LEU D 440 ? 0.2199 0.2249 0.2279 0.0042  -0.0240 -0.0024 432 LEU D CD1 
17507 C CD2 . LEU D 440 ? 0.1446 0.1642 0.1618 0.0033  -0.0242 -0.0052 432 LEU D CD2 
17508 N N   . MET D 441 ? 0.1535 0.1539 0.1637 0.0053  -0.0115 -0.0125 433 MET D N   
17509 C CA  . MET D 441 ? 0.1813 0.1794 0.1861 0.0024  -0.0089 -0.0132 433 MET D CA  
17510 C C   . MET D 441 ? 0.1928 0.1837 0.1913 0.0023  -0.0092 -0.0127 433 MET D C   
17511 O O   . MET D 441 ? 0.1846 0.1729 0.1787 0.0001  -0.0092 -0.0118 433 MET D O   
17512 C CB  . MET D 441 ? 0.1536 0.1547 0.1602 0.0019  -0.0050 -0.0155 433 MET D CB  
17513 C CG  . MET D 441 ? 0.1644 0.1628 0.1654 -0.0012 -0.0027 -0.0150 433 MET D CG  
17514 S SD  . MET D 441 ? 0.1894 0.1896 0.1915 -0.0045 -0.0038 -0.0138 433 MET D SD  
17515 C CE  . MET D 441 ? 0.1458 0.1549 0.1562 -0.0051 -0.0024 -0.0156 433 MET D CE  
17516 N N   . PHE D 442 ? 0.1660 0.1537 0.1648 0.0047  -0.0095 -0.0135 434 PHE D N   
17517 C CA  . PHE D 442 ? 0.1634 0.1449 0.1568 0.0044  -0.0095 -0.0138 434 PHE D CA  
17518 C C   . PHE D 442 ? 0.1940 0.1717 0.1859 0.0043  -0.0126 -0.0115 434 PHE D C   
17519 O O   . PHE D 442 ? 0.1883 0.1610 0.1767 0.0040  -0.0130 -0.0118 434 PHE D O   
17520 C CB  . PHE D 442 ? 0.1858 0.1659 0.1802 0.0064  -0.0075 -0.0170 434 PHE D CB  
17521 C CG  . PHE D 442 ? 0.2699 0.2549 0.2657 0.0062  -0.0039 -0.0194 434 PHE D CG  
17522 C CD1 . PHE D 442 ? 0.3136 0.3007 0.3057 0.0033  -0.0022 -0.0185 434 PHE D CD1 
17523 C CD2 . PHE D 442 ? 0.2795 0.2675 0.2815 0.0087  -0.0021 -0.0223 434 PHE D CD2 
17524 C CE1 . PHE D 442 ? 0.3602 0.3519 0.3535 0.0025  0.0015  -0.0201 434 PHE D CE1 
17525 C CE2 . PHE D 442 ? 0.3030 0.2963 0.3066 0.0081  0.0017  -0.0247 434 PHE D CE2 
17526 C CZ  . PHE D 442 ? 0.2801 0.2754 0.2789 0.0048  0.0036  -0.0234 434 PHE D CZ  
17527 N N   . SER D 443 ? 0.1930 0.1735 0.1871 0.0040  -0.0147 -0.0092 435 SER D N   
17528 C CA  . SER D 443 ? 0.1690 0.1473 0.1599 0.0023  -0.0167 -0.0070 435 SER D CA  
17529 C C   . SER D 443 ? 0.1878 0.1643 0.1744 -0.0001 -0.0155 -0.0078 435 SER D C   
17530 O O   . SER D 443 ? 0.1957 0.1690 0.1796 -0.0012 -0.0164 -0.0070 435 SER D O   
17531 C CB  . SER D 443 ? 0.1538 0.1372 0.1464 0.0014  -0.0186 -0.0050 435 SER D CB  
17532 O OG  . SER D 443 ? 0.1496 0.1379 0.1431 -0.0003 -0.0172 -0.0065 435 SER D OG  
17533 N N   . GLU D 444 ? 0.1333 0.1119 0.1197 -0.0010 -0.0134 -0.0090 436 GLU D N   
17534 C CA  . GLU D 444 ? 0.1600 0.1368 0.1434 -0.0029 -0.0126 -0.0090 436 GLU D CA  
17535 C C   . GLU D 444 ? 0.1777 0.1501 0.1573 -0.0026 -0.0125 -0.0094 436 GLU D C   
17536 O O   . GLU D 444 ? 0.2188 0.1892 0.1963 -0.0038 -0.0130 -0.0088 436 GLU D O   
17537 C CB  . GLU D 444 ? 0.1837 0.1634 0.1685 -0.0042 -0.0104 -0.0095 436 GLU D CB  
17538 C CG  . GLU D 444 ? 0.1189 0.1034 0.1077 -0.0053 -0.0107 -0.0098 436 GLU D CG  
17539 C CD  . GLU D 444 ? 0.1798 0.1662 0.1706 -0.0074 -0.0086 -0.0104 436 GLU D CD  
17540 O OE1 . GLU D 444 ? 0.2093 0.1939 0.1987 -0.0077 -0.0067 -0.0099 436 GLU D OE1 
17541 O OE2 . GLU D 444 ? 0.2082 0.1980 0.2020 -0.0090 -0.0088 -0.0113 436 GLU D OE2 
17542 N N   . TYR D 445 ? 0.1700 0.1414 0.1493 -0.0009 -0.0119 -0.0109 437 TYR D N   
17543 C CA  . TYR D 445 ? 0.1817 0.1496 0.1571 -0.0009 -0.0121 -0.0120 437 TYR D CA  
17544 C C   . TYR D 445 ? 0.2119 0.1762 0.1874 -0.0009 -0.0144 -0.0115 437 TYR D C   
17545 O O   . TYR D 445 ? 0.2718 0.2337 0.2444 -0.0018 -0.0152 -0.0120 437 TYR D O   
17546 C CB  . TYR D 445 ? 0.1318 0.1000 0.1072 0.0006  -0.0103 -0.0149 437 TYR D CB  
17547 C CG  . TYR D 445 ? 0.1647 0.1359 0.1374 -0.0003 -0.0075 -0.0157 437 TYR D CG  
17548 C CD1 . TYR D 445 ? 0.2181 0.1927 0.1924 -0.0013 -0.0062 -0.0140 437 TYR D CD1 
17549 C CD2 . TYR D 445 ? 0.1657 0.1367 0.1342 -0.0005 -0.0061 -0.0183 437 TYR D CD2 
17550 C CE1 . TYR D 445 ? 0.2289 0.2062 0.2008 -0.0026 -0.0034 -0.0142 437 TYR D CE1 
17551 C CE2 . TYR D 445 ? 0.1601 0.1343 0.1251 -0.0018 -0.0033 -0.0186 437 TYR D CE2 
17552 C CZ  . TYR D 445 ? 0.1870 0.1642 0.1539 -0.0028 -0.0019 -0.0163 437 TYR D CZ  
17553 O OH  . TYR D 445 ? 0.1889 0.1693 0.1525 -0.0045 0.0012  -0.0160 437 TYR D OH  
17554 N N   . GLU D 446 ? 0.1682 0.1324 0.1470 -0.0002 -0.0155 -0.0103 438 GLU D N   
17555 C CA  . GLU D 446 ? 0.1560 0.1168 0.1351 -0.0006 -0.0173 -0.0093 438 GLU D CA  
17556 C C   . GLU D 446 ? 0.1685 0.1310 0.1475 -0.0024 -0.0182 -0.0070 438 GLU D C   
17557 O O   . GLU D 446 ? 0.1949 0.1558 0.1745 -0.0030 -0.0195 -0.0054 438 GLU D O   
17558 C CB  . GLU D 446 ? 0.2421 0.2007 0.2248 0.0015  -0.0179 -0.0091 438 GLU D CB  
17559 C CG  . GLU D 446 ? 0.2305 0.1930 0.2169 0.0029  -0.0182 -0.0074 438 GLU D CG  
17560 C CD  . GLU D 446 ? 0.2508 0.2108 0.2419 0.0052  -0.0196 -0.0059 438 GLU D CD  
17561 O OE1 . GLU D 446 ? 0.2147 0.1692 0.2062 0.0052  -0.0203 -0.0059 438 GLU D OE1 
17562 O OE2 . GLU D 446 ? 0.2016 0.1650 0.1968 0.0069  -0.0203 -0.0046 438 GLU D OE2 
17563 N N   . ARG D 447 ? 0.1657 0.1314 0.1442 -0.0035 -0.0174 -0.0070 439 ARG D N   
17564 C CA  . ARG D 447 ? 0.2349 0.2037 0.2143 -0.0051 -0.0178 -0.0059 439 ARG D CA  
17565 C C   . ARG D 447 ? 0.1621 0.1293 0.1406 -0.0068 -0.0185 -0.0052 439 ARG D C   
17566 O O   . ARG D 447 ? 0.1735 0.1421 0.1518 -0.0079 -0.0192 -0.0037 439 ARG D O   
17567 C CB  . ARG D 447 ? 0.1757 0.1473 0.1557 -0.0062 -0.0164 -0.0069 439 ARG D CB  
17568 C CG  . ARG D 447 ? 0.1812 0.1562 0.1622 -0.0083 -0.0163 -0.0071 439 ARG D CG  
17569 C CD  . ARG D 447 ? 0.1623 0.1410 0.1435 -0.0085 -0.0173 -0.0061 439 ARG D CD  
17570 N NE  . ARG D 447 ? 0.1595 0.1422 0.1406 -0.0110 -0.0170 -0.0070 439 ARG D NE  
17571 C CZ  . ARG D 447 ? 0.1898 0.1779 0.1720 -0.0121 -0.0169 -0.0081 439 ARG D CZ  
17572 N NH1 . ARG D 447 ? 0.1757 0.1658 0.1598 -0.0107 -0.0173 -0.0079 439 ARG D NH1 
17573 N NH2 . ARG D 447 ? 0.1471 0.1390 0.1288 -0.0148 -0.0164 -0.0098 439 ARG D NH2 
17574 N N   . ASN D 448 ? 0.1480 0.1127 0.1258 -0.0072 -0.0185 -0.0062 440 ASN D N   
17575 C CA  . ASN D 448 ? 0.1369 0.1011 0.1150 -0.0091 -0.0190 -0.0060 440 ASN D CA  
17576 C C   . ASN D 448 ? 0.1313 0.0925 0.1092 -0.0092 -0.0199 -0.0047 440 ASN D C   
17577 O O   . ASN D 448 ? 0.1319 0.0936 0.1101 -0.0112 -0.0199 -0.0037 440 ASN D O   
17578 C CB  . ASN D 448 ? 0.1828 0.1462 0.1615 -0.0094 -0.0192 -0.0072 440 ASN D CB  
17579 C CG  . ASN D 448 ? 0.1519 0.1168 0.1328 -0.0114 -0.0190 -0.0076 440 ASN D CG  
17580 O OD1 . ASN D 448 ? 0.1768 0.1402 0.1584 -0.0121 -0.0198 -0.0078 440 ASN D OD1 
17581 N ND2 . ASN D 448 ? 0.1985 0.1668 0.1811 -0.0125 -0.0177 -0.0082 440 ASN D ND2 
17582 N N   . ALA D 449 ? 0.1410 0.0992 0.1190 -0.0074 -0.0204 -0.0047 441 ALA D N   
17583 C CA  . ALA D 449 ? 0.1858 0.1402 0.1648 -0.0074 -0.0213 -0.0031 441 ALA D CA  
17584 C C   . ALA D 449 ? 0.1682 0.1246 0.1474 -0.0078 -0.0218 0.0003  441 ALA D C   
17585 O O   . ALA D 449 ? 0.1539 0.1085 0.1333 -0.0092 -0.0224 0.0029  441 ALA D O   
17586 C CB  . ALA D 449 ? 0.1902 0.1408 0.1704 -0.0051 -0.0214 -0.0048 441 ALA D CB  
17587 N N   . LEU D 450 ? 0.1737 0.1342 0.1529 -0.0067 -0.0217 0.0006  442 LEU D N   
17588 C CA  . LEU D 450 ? 0.1676 0.1316 0.1463 -0.0075 -0.0227 0.0038  442 LEU D CA  
17589 C C   . LEU D 450 ? 0.1711 0.1383 0.1473 -0.0109 -0.0220 0.0043  442 LEU D C   
17590 O O   . LEU D 450 ? 0.1880 0.1561 0.1626 -0.0126 -0.0228 0.0076  442 LEU D O   
17591 C CB  . LEU D 450 ? 0.1375 0.1065 0.1171 -0.0061 -0.0228 0.0032  442 LEU D CB  
17592 C CG  . LEU D 450 ? 0.3020 0.2709 0.2851 -0.0029 -0.0237 0.0037  442 LEU D CG  
17593 C CD1 . LEU D 450 ? 0.1660 0.1295 0.1512 -0.0007 -0.0230 0.0018  442 LEU D CD1 
17594 C CD2 . LEU D 450 ? 0.2900 0.2645 0.2739 -0.0026 -0.0228 0.0016  442 LEU D CD2 
17595 N N   . ARG D 451 ? 0.1606 0.1298 0.1366 -0.0120 -0.0205 0.0010  443 ARG D N   
17596 C CA  . ARG D 451 ? 0.1260 0.0986 0.1009 -0.0151 -0.0192 0.0003  443 ARG D CA  
17597 C C   . ARG D 451 ? 0.1289 0.0986 0.1037 -0.0168 -0.0191 0.0016  443 ARG D C   
17598 O O   . ARG D 451 ? 0.1399 0.1124 0.1130 -0.0197 -0.0184 0.0030  443 ARG D O   
17599 C CB  . ARG D 451 ? 0.1494 0.1235 0.1262 -0.0152 -0.0177 -0.0035 443 ARG D CB  
17600 C CG  . ARG D 451 ? 0.1564 0.1351 0.1334 -0.0181 -0.0160 -0.0054 443 ARG D CG  
17601 C CD  . ARG D 451 ? 0.1579 0.1373 0.1387 -0.0179 -0.0146 -0.0089 443 ARG D CD  
17602 N NE  . ARG D 451 ? 0.1356 0.1202 0.1177 -0.0204 -0.0125 -0.0118 443 ARG D NE  
17603 C CZ  . ARG D 451 ? 0.1804 0.1669 0.1645 -0.0223 -0.0108 -0.0136 443 ARG D CZ  
17604 N NH1 . ARG D 451 ? 0.1661 0.1499 0.1516 -0.0222 -0.0114 -0.0125 443 ARG D NH1 
17605 N NH2 . ARG D 451 ? 0.1608 0.1525 0.1463 -0.0246 -0.0085 -0.0171 443 ARG D NH2 
17606 N N   . MET D 452 ? 0.1649 0.1294 0.1415 -0.0155 -0.0197 0.0011  444 MET D N   
17607 C CA  . MET D 452 ? 0.1323 0.0940 0.1096 -0.0175 -0.0195 0.0019  444 MET D CA  
17608 C C   . MET D 452 ? 0.1431 0.1024 0.1194 -0.0185 -0.0204 0.0064  444 MET D C   
17609 O O   . MET D 452 ? 0.2085 0.1681 0.1845 -0.0216 -0.0196 0.0081  444 MET D O   
17610 C CB  . MET D 452 ? 0.1320 0.0892 0.1115 -0.0162 -0.0202 -0.0004 444 MET D CB  
17611 C CG  . MET D 452 ? 0.1827 0.1424 0.1635 -0.0160 -0.0198 -0.0038 444 MET D CG  
17612 S SD  . MET D 452 ? 0.2013 0.1656 0.1846 -0.0191 -0.0183 -0.0050 444 MET D SD  
17613 C CE  . MET D 452 ? 0.2384 0.1992 0.2237 -0.0212 -0.0188 -0.0047 444 MET D CE  
17614 N N   . ALA D 453 ? 0.1985 0.1559 0.1749 -0.0160 -0.0219 0.0087  445 ALA D N   
17615 C CA  . ALA D 453 ? 0.1784 0.1336 0.1543 -0.0166 -0.0232 0.0140  445 ALA D CA  
17616 C C   . ALA D 453 ? 0.1644 0.1259 0.1361 -0.0197 -0.0228 0.0169  445 ALA D C   
17617 O O   . ALA D 453 ? 0.1943 0.1550 0.1644 -0.0225 -0.0228 0.0211  445 ALA D O   
17618 C CB  . ALA D 453 ? 0.1742 0.1273 0.1524 -0.0128 -0.0251 0.0157  445 ALA D CB  
17619 N N   . ALA D 454 ? 0.1444 0.1123 0.1142 -0.0197 -0.0223 0.0145  446 ALA D N   
17620 C CA  . ALA D 454 ? 0.1818 0.1568 0.1472 -0.0230 -0.0217 0.0158  446 ALA D CA  
17621 C C   . ALA D 454 ? 0.1849 0.1618 0.1494 -0.0268 -0.0189 0.0140  446 ALA D C   
17622 O O   . ALA D 454 ? 0.1942 0.1745 0.1548 -0.0304 -0.0182 0.0170  446 ALA D O   
17623 C CB  . ALA D 454 ? 0.1784 0.1595 0.1433 -0.0222 -0.0214 0.0122  446 ALA D CB  
17624 N N   . LEU D 455 ? 0.1856 0.1608 0.1536 -0.0263 -0.0174 0.0094  447 LEU D N   
17625 C CA  . LEU D 455 ? 0.1417 0.1192 0.1108 -0.0296 -0.0148 0.0072  447 LEU D CA  
17626 C C   . LEU D 455 ? 0.1736 0.1472 0.1427 -0.0318 -0.0147 0.0110  447 LEU D C   
17627 O O   . LEU D 455 ? 0.1889 0.1662 0.1563 -0.0359 -0.0126 0.0119  447 LEU D O   
17628 C CB  . LEU D 455 ? 0.1411 0.1178 0.1151 -0.0279 -0.0140 0.0020  447 LEU D CB  
17629 C CG  . LEU D 455 ? 0.2463 0.2253 0.2237 -0.0305 -0.0117 -0.0009 447 LEU D CG  
17630 C CD1 . LEU D 455 ? 0.3022 0.2885 0.2776 -0.0342 -0.0088 -0.0020 447 LEU D CD1 
17631 C CD2 . LEU D 455 ? 0.2925 0.2713 0.2751 -0.0281 -0.0118 -0.0053 447 LEU D CD2 
17632 N N   . MET D 456 ? 0.1555 0.1217 0.1269 -0.0296 -0.0167 0.0131  448 MET D N   
17633 C CA  . MET D 456 ? 0.1846 0.1459 0.1572 -0.0318 -0.0167 0.0166  448 MET D CA  
17634 C C   . MET D 456 ? 0.2102 0.1713 0.1788 -0.0336 -0.0176 0.0237  448 MET D C   
17635 O O   . MET D 456 ? 0.2240 0.1811 0.1934 -0.0362 -0.0173 0.0276  448 MET D O   
17636 C CB  . MET D 456 ? 0.1988 0.1520 0.1758 -0.0289 -0.0184 0.0157  448 MET D CB  
17637 C CG  . MET D 456 ? 0.2001 0.1533 0.1808 -0.0282 -0.0179 0.0098  448 MET D CG  
17638 S SD  . MET D 456 ? 0.2176 0.1619 0.2024 -0.0263 -0.0196 0.0087  448 MET D SD  
17639 C CE  . MET D 456 ? 0.2419 0.1866 0.2260 -0.0215 -0.0209 0.0048  448 MET D CE  
17640 N N   . LYS D 457 ? 0.1993 0.1648 0.1639 -0.0326 -0.0188 0.0255  449 LYS D N   
17641 C CA  . LYS D 457 ? 0.2247 0.1913 0.1849 -0.0341 -0.0205 0.0328  449 LYS D CA  
17642 C C   . LYS D 457 ? 0.2366 0.1941 0.2006 -0.0317 -0.0231 0.0382  449 LYS D C   
17643 O O   . LYS D 457 ? 0.2235 0.1784 0.1860 -0.0342 -0.0237 0.0450  449 LYS D O   
17644 C CB  . LYS D 457 ? 0.2850 0.2567 0.2404 -0.0399 -0.0179 0.0351  449 LYS D CB  
17645 C CG  . LYS D 457 ? 0.2635 0.2443 0.2167 -0.0422 -0.0147 0.0287  449 LYS D CG  
17646 C CD  . LYS D 457 ? 0.3828 0.3694 0.3316 -0.0483 -0.0114 0.0303  449 LYS D CD  
17647 C CE  . LYS D 457 ? 0.4896 0.4818 0.4299 -0.0510 -0.0126 0.0362  449 LYS D CE  
17648 N NZ  . LYS D 457 ? 0.6000 0.5977 0.5352 -0.0574 -0.0090 0.0382  449 LYS D NZ  
17649 N N   . ILE D 458 ? 0.2244 0.1769 0.1936 -0.0271 -0.0245 0.0351  450 ILE D N   
17650 C CA  . ILE D 458 ? 0.2125 0.1564 0.1867 -0.0241 -0.0268 0.0387  450 ILE D CA  
17651 C C   . ILE D 458 ? 0.2258 0.1716 0.2009 -0.0198 -0.0296 0.0402  450 ILE D C   
17652 O O   . ILE D 458 ? 0.1936 0.1468 0.1654 -0.0193 -0.0296 0.0378  450 ILE D O   
17653 C CB  . ILE D 458 ? 0.1910 0.1279 0.1710 -0.0225 -0.0258 0.0333  450 ILE D CB  
17654 C CG1 . ILE D 458 ? 0.1664 0.1070 0.1465 -0.0199 -0.0251 0.0261  450 ILE D CG1 
17655 C CG2 . ILE D 458 ? 0.2297 0.1647 0.2102 -0.0270 -0.0235 0.0326  450 ILE D CG2 
17656 C CD1 . ILE D 458 ? 0.2423 0.1771 0.2270 -0.0180 -0.0247 0.0207  450 ILE D CD1 
17657 N N   . ASN D 459 ? 0.1839 0.1229 0.1644 -0.0166 -0.0319 0.0442  451 ASN D N   
17658 C CA  . ASN D 459 ? 0.1854 0.1269 0.1677 -0.0128 -0.0351 0.0474  451 ASN D CA  
17659 C C   . ASN D 459 ? 0.2621 0.1983 0.2526 -0.0074 -0.0358 0.0440  451 ASN D C   
17660 O O   . ASN D 459 ? 0.2227 0.1561 0.2186 -0.0041 -0.0386 0.0485  451 ASN D O   
17661 C CB  . ASN D 459 ? 0.2176 0.1582 0.1986 -0.0140 -0.0380 0.0574  451 ASN D CB  
17662 C CG  . ASN D 459 ? 0.2449 0.1744 0.2319 -0.0140 -0.0383 0.0617  451 ASN D CG  
17663 O OD1 . ASN D 459 ? 0.2408 0.1634 0.2328 -0.0132 -0.0363 0.0565  451 ASN D OD1 
17664 N ND2 . ASN D 459 ? 0.2234 0.1511 0.2098 -0.0151 -0.0410 0.0715  451 ASN D ND2 
17665 N N   . PRO D 460 ? 0.1976 0.1333 0.1894 -0.0061 -0.0335 0.0360  452 PRO D N   
17666 C CA  . PRO D 460 ? 0.2385 0.1721 0.2367 -0.0012 -0.0338 0.0321  452 PRO D CA  
17667 C C   . PRO D 460 ? 0.2281 0.1697 0.2259 0.0010  -0.0355 0.0331  452 PRO D C   
17668 O O   . PRO D 460 ? 0.2520 0.2012 0.2437 -0.0014 -0.0358 0.0341  452 PRO D O   
17669 C CB  . PRO D 460 ? 0.2397 0.1729 0.2367 -0.0017 -0.0309 0.0240  452 PRO D CB  
17670 C CG  . PRO D 460 ? 0.2115 0.1506 0.2013 -0.0057 -0.0297 0.0235  452 PRO D CG  
17671 C CD  . PRO D 460 ? 0.1695 0.1078 0.1569 -0.0090 -0.0306 0.0302  452 PRO D CD  
17672 N N   . VAL D 461 ? 0.2155 0.1557 0.2206 0.0056  -0.0365 0.0322  453 VAL D N   
17673 C CA  . VAL D 461 ? 0.2320 0.1800 0.2390 0.0082  -0.0384 0.0331  453 VAL D CA  
17674 C C   . VAL D 461 ? 0.2244 0.1746 0.2337 0.0103  -0.0358 0.0253  453 VAL D C   
17675 O O   . VAL D 461 ? 0.2035 0.1487 0.2192 0.0134  -0.0346 0.0218  453 VAL D O   
17676 C CB  . VAL D 461 ? 0.1963 0.1423 0.2112 0.0119  -0.0421 0.0393  453 VAL D CB  
17677 C CG1 . VAL D 461 ? 0.2237 0.1789 0.2415 0.0146  -0.0443 0.0396  453 VAL D CG1 
17678 C CG2 . VAL D 461 ? 0.2019 0.1456 0.2135 0.0092  -0.0449 0.0482  453 VAL D CG2 
17679 N N   . PHE D 462 ? 0.1807 0.1384 0.1850 0.0085  -0.0347 0.0225  454 PHE D N   
17680 C CA  . PHE D 462 ? 0.1659 0.1262 0.1714 0.0099  -0.0321 0.0160  454 PHE D CA  
17681 C C   . PHE D 462 ? 0.1646 0.1315 0.1756 0.0128  -0.0336 0.0165  454 PHE D C   
17682 O O   . PHE D 462 ? 0.2305 0.2044 0.2396 0.0116  -0.0358 0.0195  454 PHE D O   
17683 C CB  . PHE D 462 ? 0.1610 0.1248 0.1592 0.0062  -0.0300 0.0129  454 PHE D CB  
17684 C CG  . PHE D 462 ? 0.2090 0.1674 0.2028 0.0034  -0.0287 0.0123  454 PHE D CG  
17685 C CD1 . PHE D 462 ? 0.2224 0.1754 0.2171 0.0040  -0.0268 0.0082  454 PHE D CD1 
17686 C CD2 . PHE D 462 ? 0.1779 0.1375 0.1670 -0.0000 -0.0295 0.0157  454 PHE D CD2 
17687 C CE1 . PHE D 462 ? 0.2506 0.1995 0.2422 0.0014  -0.0260 0.0075  454 PHE D CE1 
17688 C CE2 . PHE D 462 ? 0.2301 0.1856 0.2164 -0.0026 -0.0282 0.0149  454 PHE D CE2 
17689 C CZ  . PHE D 462 ? 0.2243 0.1745 0.2123 -0.0019 -0.0267 0.0109  454 PHE D CZ  
17690 N N   . VAL D 463 ? 0.1834 0.1489 0.2019 0.0165  -0.0324 0.0132  455 VAL D N   
17691 C CA  . VAL D 463 ? 0.1553 0.1270 0.1814 0.0199  -0.0337 0.0134  455 VAL D CA  
17692 C C   . VAL D 463 ? 0.1646 0.1415 0.1902 0.0195  -0.0302 0.0073  455 VAL D C   
17693 O O   . VAL D 463 ? 0.1690 0.1422 0.1930 0.0192  -0.0267 0.0024  455 VAL D O   
17694 C CB  . VAL D 463 ? 0.1769 0.1436 0.2135 0.0246  -0.0346 0.0140  455 VAL D CB  
17695 C CG1 . VAL D 463 ? 0.2154 0.1893 0.2617 0.0285  -0.0354 0.0131  455 VAL D CG1 
17696 C CG2 . VAL D 463 ? 0.1820 0.1430 0.2194 0.0247  -0.0383 0.0213  455 VAL D CG2 
17697 N N   . PHE D 464 ? 0.1758 0.1616 0.2030 0.0192  -0.0313 0.0076  456 PHE D N   
17698 C CA  . PHE D 464 ? 0.1504 0.1415 0.1777 0.0184  -0.0280 0.0025  456 PHE D CA  
17699 C C   . PHE D 464 ? 0.1958 0.1946 0.2328 0.0213  -0.0290 0.0021  456 PHE D C   
17700 O O   . PHE D 464 ? 0.2012 0.2052 0.2411 0.0219  -0.0331 0.0063  456 PHE D O   
17701 C CB  . PHE D 464 ? 0.1355 0.1301 0.1548 0.0139  -0.0274 0.0022  456 PHE D CB  
17702 C CG  . PHE D 464 ? 0.1656 0.1535 0.1767 0.0112  -0.0262 0.0022  456 PHE D CG  
17703 C CD1 . PHE D 464 ? 0.1581 0.1411 0.1668 0.0109  -0.0229 -0.0016 456 PHE D CD1 
17704 C CD2 . PHE D 464 ? 0.1949 0.1821 0.2010 0.0088  -0.0286 0.0059  456 PHE D CD2 
17705 C CE1 . PHE D 464 ? 0.1793 0.1570 0.1816 0.0086  -0.0223 -0.0016 456 PHE D CE1 
17706 C CE2 . PHE D 464 ? 0.1529 0.1346 0.1529 0.0064  -0.0273 0.0056  456 PHE D CE2 
17707 C CZ  . PHE D 464 ? 0.1311 0.1082 0.1297 0.0064  -0.0244 0.0018  456 PHE D CZ  
17708 N N   . THR D 465 ? 0.2082 0.2083 0.2501 0.0230  -0.0253 -0.0029 457 THR D N   
17709 C CA  . THR D 465 ? 0.1883 0.1968 0.2403 0.0255  -0.0253 -0.0044 457 THR D CA  
17710 C C   . THR D 465 ? 0.1671 0.1815 0.2165 0.0223  -0.0216 -0.0084 457 THR D C   
17711 O O   . THR D 465 ? 0.1412 0.1526 0.1815 0.0187  -0.0193 -0.0095 457 THR D O   
17712 C CB  . THR D 465 ? 0.1817 0.1876 0.2435 0.0302  -0.0235 -0.0074 457 THR D CB  
17713 O OG1 . THR D 465 ? 0.2047 0.2072 0.2627 0.0290  -0.0179 -0.0132 457 THR D OG1 
17714 C CG2 . THR D 465 ? 0.2585 0.2562 0.3226 0.0329  -0.0267 -0.0034 457 THR D CG2 
17715 N N   . HIS D 466 ? 0.1481 0.1713 0.2064 0.0237  -0.0211 -0.0102 458 HIS D N   
17716 C CA  . HIS D 466 ? 0.1514 0.1804 0.2088 0.0205  -0.0172 -0.0139 458 HIS D CA  
17717 C C   . HIS D 466 ? 0.1986 0.2286 0.2477 0.0158  -0.0185 -0.0122 458 HIS D C   
17718 O O   . HIS D 466 ? 0.1846 0.2110 0.2262 0.0125  -0.0154 -0.0137 458 HIS D O   
17719 C CB  . HIS D 466 ? 0.1971 0.2219 0.2512 0.0199  -0.0113 -0.0184 458 HIS D CB  
17720 C CG  . HIS D 466 ? 0.2721 0.2974 0.3351 0.0241  -0.0091 -0.0218 458 HIS D CG  
17721 N ND1 . HIS D 466 ? 0.3376 0.3571 0.4045 0.0280  -0.0112 -0.0208 458 HIS D ND1 
17722 C CD2 . HIS D 466 ? 0.3512 0.3822 0.4209 0.0248  -0.0045 -0.0265 458 HIS D CD2 
17723 C CE1 . HIS D 466 ? 0.3092 0.3306 0.3852 0.0313  -0.0081 -0.0253 458 HIS D CE1 
17724 N NE2 . HIS D 466 ? 0.3041 0.3330 0.3817 0.0294  -0.0039 -0.0289 458 HIS D NE2 
17725 N N   . ASP D 467 ? 0.1674 0.2027 0.2184 0.0155  -0.0232 -0.0090 459 ASP D N   
17726 C CA  . ASP D 467 ? 0.1738 0.2086 0.2164 0.0115  -0.0251 -0.0072 459 ASP D CA  
17727 C C   . ASP D 467 ? 0.1974 0.2389 0.2400 0.0074  -0.0235 -0.0099 459 ASP D C   
17728 O O   . ASP D 467 ? 0.1872 0.2285 0.2235 0.0039  -0.0246 -0.0095 459 ASP D O   
17729 C CB  . ASP D 467 ? 0.1952 0.2323 0.2378 0.0126  -0.0310 -0.0022 459 ASP D CB  
17730 C CG  . ASP D 467 ? 0.2111 0.2596 0.2613 0.0129  -0.0344 -0.0017 459 ASP D CG  
17731 O OD1 . ASP D 467 ? 0.2400 0.2937 0.2995 0.0149  -0.0329 -0.0043 459 ASP D OD1 
17732 O OD2 . ASP D 467 ? 0.2263 0.2793 0.2730 0.0109  -0.0387 0.0011  459 ASP D OD2 
17733 N N   . SER D 468 ? 0.1796 0.2269 0.2293 0.0074  -0.0207 -0.0131 460 SER D N   
17734 C CA  . SER D 468 ? 0.1433 0.1968 0.1941 0.0031  -0.0194 -0.0156 460 SER D CA  
17735 C C   . SER D 468 ? 0.1463 0.2035 0.2037 0.0029  -0.0146 -0.0191 460 SER D C   
17736 O O   . SER D 468 ? 0.1794 0.2342 0.2394 0.0059  -0.0120 -0.0200 460 SER D O   
17737 C CB  . SER D 468 ? 0.1585 0.2215 0.2132 0.0023  -0.0245 -0.0146 460 SER D CB  
17738 O OG  . SER D 468 ? 0.1682 0.2395 0.2340 0.0055  -0.0261 -0.0148 460 SER D OG  
17739 N N   . ILE D 469 ? 0.1459 0.2096 0.2068 -0.0009 -0.0133 -0.0215 461 ILE D N   
17740 C CA  . ILE D 469 ? 0.1782 0.2473 0.2465 -0.0019 -0.0087 -0.0246 461 ILE D CA  
17741 C C   . ILE D 469 ? 0.2402 0.3165 0.3193 0.0026  -0.0099 -0.0252 461 ILE D C   
17742 O O   . ILE D 469 ? 0.2206 0.3010 0.3064 0.0030  -0.0056 -0.0280 461 ILE D O   
17743 C CB  . ILE D 469 ? 0.1993 0.2749 0.2711 -0.0070 -0.0079 -0.0269 461 ILE D CB  
17744 C CG1 . ILE D 469 ? 0.1984 0.2824 0.2739 -0.0072 -0.0140 -0.0266 461 ILE D CG1 
17745 C CG2 . ILE D 469 ? 0.2533 0.3208 0.3166 -0.0112 -0.0052 -0.0270 461 ILE D CG2 
17746 C CD1 . ILE D 469 ? 0.2008 0.2929 0.2815 -0.0124 -0.0136 -0.0300 461 ILE D CD1 
17747 N N   . GLY D 470 ? 0.1813 0.2596 0.2627 0.0060  -0.0158 -0.0224 462 GLY D N   
17748 C CA  . GLY D 470 ? 0.1364 0.2202 0.2288 0.0113  -0.0178 -0.0221 462 GLY D CA  
17749 C C   . GLY D 470 ? 0.1533 0.2313 0.2472 0.0149  -0.0135 -0.0237 462 GLY D C   
17750 O O   . GLY D 470 ? 0.1573 0.2406 0.2626 0.0190  -0.0136 -0.0250 462 GLY D O   
17751 N N   . LEU D 471 ? 0.1616 0.2293 0.2449 0.0135  -0.0100 -0.0239 463 LEU D N   
17752 C CA  . LEU D 471 ? 0.1690 0.2322 0.2533 0.0163  -0.0057 -0.0264 463 LEU D CA  
17753 C C   . LEU D 471 ? 0.2482 0.3177 0.3379 0.0146  0.0007  -0.0310 463 LEU D C   
17754 O O   . LEU D 471 ? 0.2274 0.2965 0.3209 0.0172  0.0045  -0.0342 463 LEU D O   
17755 C CB  . LEU D 471 ? 0.1708 0.2221 0.2421 0.0151  -0.0043 -0.0254 463 LEU D CB  
17756 C CG  . LEU D 471 ? 0.1527 0.1999 0.2134 0.0100  -0.0011 -0.0255 463 LEU D CG  
17757 C CD1 . LEU D 471 ? 0.2051 0.2536 0.2655 0.0084  0.0056  -0.0291 463 LEU D CD1 
17758 C CD2 . LEU D 471 ? 0.1574 0.1940 0.2070 0.0097  -0.0028 -0.0230 463 LEU D CD2 
17759 N N   . GLY D 472 ? 0.1708 0.2458 0.2607 0.0100  0.0023  -0.0317 464 GLY D N   
17760 C CA  . GLY D 472 ? 0.1524 0.2351 0.2494 0.0082  0.0080  -0.0356 464 GLY D CA  
17761 C C   . GLY D 472 ? 0.1755 0.2526 0.2632 0.0049  0.0146  -0.0369 464 GLY D C   
17762 O O   . GLY D 472 ? 0.2355 0.3058 0.3126 0.0013  0.0147  -0.0346 464 GLY D O   
17763 N N   . GLU D 473 ? 0.1463 0.2265 0.2383 0.0063  0.0199  -0.0407 465 GLU D N   
17764 C CA  . GLU D 473 ? 0.1933 0.2734 0.2795 0.0020  0.0270  -0.0425 465 GLU D CA  
17765 C C   . GLU D 473 ? 0.2109 0.2799 0.2816 0.0002  0.0281  -0.0402 465 GLU D C   
17766 O O   . GLU D 473 ? 0.1927 0.2608 0.2568 -0.0043 0.0327  -0.0397 465 GLU D O   
17767 C CB  . GLU D 473 ? 0.1699 0.2572 0.2647 0.0041  0.0325  -0.0478 465 GLU D CB  
17768 C CG  . GLU D 473 ? 0.1733 0.2736 0.2841 0.0045  0.0335  -0.0505 465 GLU D CG  
17769 C CD  . GLU D 473 ? 0.2365 0.3411 0.3602 0.0108  0.0279  -0.0511 465 GLU D CD  
17770 O OE1 . GLU D 473 ? 0.2291 0.3266 0.3488 0.0137  0.0217  -0.0477 465 GLU D OE1 
17771 O OE2 . GLU D 473 ? 0.2372 0.3528 0.3756 0.0127  0.0298  -0.0548 465 GLU D OE2 
17772 N N   . ASP D 474 ? 0.1898 0.2507 0.2551 0.0034  0.0239  -0.0387 466 ASP D N   
17773 C CA  . ASP D 474 ? 0.2281 0.2794 0.2794 0.0016  0.0245  -0.0367 466 ASP D CA  
17774 C C   . ASP D 474 ? 0.2711 0.3189 0.3152 -0.0032 0.0239  -0.0327 466 ASP D C   
17775 O O   . ASP D 474 ? 0.2909 0.3329 0.3245 -0.0057 0.0258  -0.0310 466 ASP D O   
17776 C CB  . ASP D 474 ? 0.1695 0.2131 0.2175 0.0055  0.0197  -0.0356 466 ASP D CB  
17777 C CG  . ASP D 474 ? 0.2934 0.3366 0.3445 0.0093  0.0218  -0.0399 466 ASP D CG  
17778 O OD1 . ASP D 474 ? 0.2701 0.3194 0.3257 0.0092  0.0271  -0.0443 466 ASP D OD1 
17779 O OD2 . ASP D 474 ? 0.2766 0.3132 0.3259 0.0123  0.0183  -0.0393 466 ASP D OD2 
17780 N N   . GLY D 475 ? 0.2116 0.2627 0.2612 -0.0044 0.0209  -0.0313 467 GLY D N   
17781 C CA  . GLY D 475 ? 0.1680 0.2174 0.2141 -0.0093 0.0216  -0.0288 467 GLY D CA  
17782 C C   . GLY D 475 ? 0.1717 0.2123 0.2094 -0.0100 0.0178  -0.0254 467 GLY D C   
17783 O O   . GLY D 475 ? 0.1476 0.1839 0.1824 -0.0069 0.0138  -0.0247 467 GLY D O   
17784 N N   . PRO D 476 ? 0.1838 0.2213 0.2180 -0.0142 0.0191  -0.0232 468 PRO D N   
17785 C CA  . PRO D 476 ? 0.1920 0.2231 0.2218 -0.0151 0.0154  -0.0209 468 PRO D CA  
17786 C C   . PRO D 476 ? 0.1994 0.2220 0.2198 -0.0132 0.0136  -0.0188 468 PRO D C   
17787 O O   . PRO D 476 ? 0.1941 0.2126 0.2122 -0.0128 0.0100  -0.0176 468 PRO D O   
17788 C CB  . PRO D 476 ? 0.1673 0.1971 0.1975 -0.0200 0.0182  -0.0194 468 PRO D CB  
17789 C CG  . PRO D 476 ? 0.1843 0.2173 0.2148 -0.0218 0.0237  -0.0195 468 PRO D CG  
17790 C CD  . PRO D 476 ? 0.1905 0.2312 0.2268 -0.0186 0.0242  -0.0231 468 PRO D CD  
17791 N N   . THR D 477 ? 0.1669 0.1875 0.1820 -0.0122 0.0160  -0.0188 469 THR D N   
17792 C CA  . THR D 477 ? 0.1303 0.1435 0.1371 -0.0106 0.0137  -0.0173 469 THR D CA  
17793 C C   . THR D 477 ? 0.2083 0.2210 0.2169 -0.0066 0.0099  -0.0187 469 THR D C   
17794 O O   . THR D 477 ? 0.2214 0.2283 0.2250 -0.0056 0.0071  -0.0173 469 THR D O   
17795 C CB  . THR D 477 ? 0.1742 0.1858 0.1740 -0.0110 0.0169  -0.0173 469 THR D CB  
17796 O OG1 . THR D 477 ? 0.2229 0.2397 0.2267 -0.0087 0.0190  -0.0212 469 THR D OG1 
17797 C CG2 . THR D 477 ? 0.1662 0.1783 0.1635 -0.0152 0.0206  -0.0148 469 THR D CG2 
17798 N N   . HIS D 478 ? 0.1261 0.1449 0.1426 -0.0044 0.0098  -0.0211 470 HIS D N   
17799 C CA  . HIS D 478 ? 0.1907 0.2089 0.2100 -0.0005 0.0063  -0.0217 470 HIS D CA  
17800 C C   . HIS D 478 ? 0.1353 0.1573 0.1604 0.0001  0.0023  -0.0207 470 HIS D C   
17801 O O   . HIS D 478 ? 0.1795 0.1994 0.2047 0.0026  -0.0015 -0.0195 470 HIS D O   
17802 C CB  . HIS D 478 ? 0.1943 0.2162 0.2190 0.0025  0.0086  -0.0250 470 HIS D CB  
17803 C CG  . HIS D 478 ? 0.2312 0.2487 0.2494 0.0030  0.0113  -0.0268 470 HIS D CG  
17804 N ND1 . HIS D 478 ? 0.3380 0.3532 0.3477 -0.0003 0.0142  -0.0260 470 HIS D ND1 
17805 C CD2 . HIS D 478 ? 0.2989 0.3142 0.3180 0.0062  0.0114  -0.0295 470 HIS D CD2 
17806 C CE1 . HIS D 478 ? 0.3270 0.3395 0.3319 0.0006  0.0158  -0.0283 470 HIS D CE1 
17807 N NE2 . HIS D 478 ? 0.2823 0.2946 0.2930 0.0045  0.0144  -0.0309 470 HIS D NE2 
17808 N N   . GLN D 479 ? 0.1647 0.1925 0.1944 -0.0026 0.0030  -0.0211 471 GLN D N   
17809 C CA  . GLN D 479 ? 0.1678 0.2013 0.2034 -0.0023 -0.0008 -0.0208 471 GLN D CA  
17810 C C   . GLN D 479 ? 0.1657 0.1952 0.1957 -0.0042 -0.0039 -0.0190 471 GLN D C   
17811 O O   . GLN D 479 ? 0.1529 0.1802 0.1801 -0.0077 -0.0023 -0.0190 471 GLN D O   
17812 C CB  . GLN D 479 ? 0.1311 0.1731 0.1743 -0.0049 0.0012  -0.0228 471 GLN D CB  
17813 C CG  . GLN D 479 ? 0.1483 0.1969 0.1994 -0.0031 0.0042  -0.0253 471 GLN D CG  
17814 C CD  . GLN D 479 ? 0.1806 0.2359 0.2374 -0.0070 0.0079  -0.0272 471 GLN D CD  
17815 O OE1 . GLN D 479 ? 0.1845 0.2373 0.2380 -0.0111 0.0093  -0.0265 471 GLN D OE1 
17816 N NE2 . GLN D 479 ? 0.1855 0.2493 0.2519 -0.0056 0.0098  -0.0297 471 GLN D NE2 
17817 N N   . PRO D 480 ? 0.1700 0.1986 0.1988 -0.0021 -0.0082 -0.0173 472 PRO D N   
17818 C CA  . PRO D 480 ? 0.2323 0.2579 0.2556 -0.0042 -0.0106 -0.0160 472 PRO D CA  
17819 C C   . PRO D 480 ? 0.1598 0.1917 0.1863 -0.0076 -0.0112 -0.0176 472 PRO D C   
17820 O O   . PRO D 480 ? 0.1616 0.2017 0.1950 -0.0077 -0.0121 -0.0188 472 PRO D O   
17821 C CB  . PRO D 480 ? 0.2029 0.2277 0.2253 -0.0012 -0.0148 -0.0135 472 PRO D CB  
17822 C CG  . PRO D 480 ? 0.1853 0.2083 0.2107 0.0025  -0.0138 -0.0135 472 PRO D CG  
17823 C CD  . PRO D 480 ? 0.1321 0.1611 0.1640 0.0022  -0.0106 -0.0162 472 PRO D CD  
17824 N N   . ILE D 481 ? 0.1939 0.2222 0.2162 -0.0106 -0.0106 -0.0181 473 ILE D N   
17825 C CA  . ILE D 481 ? 0.1878 0.2210 0.2126 -0.0144 -0.0110 -0.0205 473 ILE D CA  
17826 C C   . ILE D 481 ? 0.1544 0.1854 0.1736 -0.0154 -0.0134 -0.0202 473 ILE D C   
17827 O O   . ILE D 481 ? 0.1676 0.2046 0.1868 -0.0162 -0.0166 -0.0206 473 ILE D O   
17828 C CB  . ILE D 481 ? 0.1235 0.1542 0.1503 -0.0177 -0.0068 -0.0224 473 ILE D CB  
17829 C CG1 . ILE D 481 ? 0.1503 0.1836 0.1821 -0.0173 -0.0038 -0.0226 473 ILE D CG1 
17830 C CG2 . ILE D 481 ? 0.1457 0.1808 0.1758 -0.0217 -0.0072 -0.0258 473 ILE D CG2 
17831 C CD1 . ILE D 481 ? 0.1441 0.1876 0.1835 -0.0172 -0.0051 -0.0244 473 ILE D CD1 
17832 N N   . GLU D 482 ? 0.1117 0.1345 0.1259 -0.0154 -0.0118 -0.0193 474 GLU D N   
17833 C CA  . GLU D 482 ? 0.1717 0.1924 0.1815 -0.0168 -0.0130 -0.0197 474 GLU D CA  
17834 C C   . GLU D 482 ? 0.1358 0.1530 0.1403 -0.0142 -0.0152 -0.0165 474 GLU D C   
17835 O O   . GLU D 482 ? 0.1442 0.1605 0.1449 -0.0155 -0.0161 -0.0166 474 GLU D O   
17836 C CB  . GLU D 482 ? 0.1567 0.1714 0.1663 -0.0188 -0.0100 -0.0212 474 GLU D CB  
17837 C CG  . GLU D 482 ? 0.1661 0.1727 0.1728 -0.0167 -0.0085 -0.0185 474 GLU D CG  
17838 C CD  . GLU D 482 ? 0.1793 0.1850 0.1883 -0.0161 -0.0061 -0.0176 474 GLU D CD  
17839 O OE1 . GLU D 482 ? 0.1418 0.1531 0.1544 -0.0158 -0.0061 -0.0182 474 GLU D OE1 
17840 O OE2 . GLU D 482 ? 0.1593 0.1592 0.1663 -0.0159 -0.0043 -0.0160 474 GLU D OE2 
17841 N N   . GLN D 483 ? 0.1304 0.1457 0.1351 -0.0109 -0.0158 -0.0140 475 GLN D N   
17842 C CA  . GLN D 483 ? 0.1500 0.1599 0.1503 -0.0087 -0.0172 -0.0113 475 GLN D CA  
17843 C C   . GLN D 483 ? 0.1527 0.1659 0.1507 -0.0091 -0.0206 -0.0093 475 GLN D C   
17844 O O   . GLN D 483 ? 0.1520 0.1618 0.1455 -0.0099 -0.0210 -0.0082 475 GLN D O   
17845 C CB  . GLN D 483 ? 0.2057 0.2131 0.2077 -0.0052 -0.0169 -0.0099 475 GLN D CB  
17846 C CG  . GLN D 483 ? 0.1702 0.1727 0.1713 -0.0051 -0.0136 -0.0110 475 GLN D CG  
17847 C CD  . GLN D 483 ? 0.1794 0.1852 0.1838 -0.0071 -0.0109 -0.0130 475 GLN D CD  
17848 O OE1 . GLN D 483 ? 0.1638 0.1761 0.1733 -0.0073 -0.0112 -0.0140 475 GLN D OE1 
17849 N NE2 . GLN D 483 ? 0.1853 0.1870 0.1877 -0.0088 -0.0086 -0.0133 475 GLN D NE2 
17850 N N   . THR D 484 ? 0.1463 0.1667 0.1475 -0.0086 -0.0232 -0.0085 476 THR D N   
17851 C CA  . THR D 484 ? 0.1648 0.1891 0.1631 -0.0091 -0.0269 -0.0057 476 THR D CA  
17852 C C   . THR D 484 ? 0.1777 0.2042 0.1712 -0.0133 -0.0264 -0.0078 476 THR D C   
17853 O O   . THR D 484 ? 0.1677 0.1927 0.1559 -0.0142 -0.0274 -0.0056 476 THR D O   
17854 C CB  . THR D 484 ? 0.1570 0.1898 0.1603 -0.0079 -0.0301 -0.0045 476 THR D CB  
17855 O OG1 . THR D 484 ? 0.1639 0.1944 0.1728 -0.0036 -0.0303 -0.0028 476 THR D OG1 
17856 C CG2 . THR D 484 ? 0.1421 0.1796 0.1417 -0.0087 -0.0346 -0.0006 476 THR D CG2 
17857 N N   . ALA D 485 ? 0.1459 0.1758 0.1416 -0.0161 -0.0244 -0.0124 477 ALA D N   
17858 C CA  . ALA D 485 ? 0.1856 0.2173 0.1779 -0.0200 -0.0232 -0.0157 477 ALA D CA  
17859 C C   . ALA D 485 ? 0.1863 0.2101 0.1751 -0.0200 -0.0210 -0.0155 477 ALA D C   
17860 O O   . ALA D 485 ? 0.1644 0.1895 0.1489 -0.0223 -0.0209 -0.0161 477 ALA D O   
17861 C CB  . ALA D 485 ? 0.1426 0.1776 0.1396 -0.0228 -0.0209 -0.0212 477 ALA D CB  
17862 N N   . THR D 486 ? 0.1438 0.1602 0.1344 -0.0176 -0.0190 -0.0148 478 THR D N   
17863 C CA  . THR D 486 ? 0.1319 0.1418 0.1201 -0.0176 -0.0174 -0.0147 478 THR D CA  
17864 C C   . THR D 486 ? 0.1281 0.1357 0.1119 -0.0164 -0.0193 -0.0108 478 THR D C   
17865 O O   . THR D 486 ? 0.1509 0.1567 0.1321 -0.0178 -0.0185 -0.0110 478 THR D O   
17866 C CB  . THR D 486 ? 0.1482 0.1514 0.1388 -0.0158 -0.0153 -0.0147 478 THR D CB  
17867 O OG1 . THR D 486 ? 0.1412 0.1422 0.1318 -0.0127 -0.0163 -0.0118 478 THR D OG1 
17868 C CG2 . THR D 486 ? 0.1789 0.1833 0.1741 -0.0173 -0.0131 -0.0178 478 THR D CG2 
17869 N N   . LEU D 487 ? 0.1459 0.1537 0.1301 -0.0139 -0.0217 -0.0072 479 LEU D N   
17870 C CA  . LEU D 487 ? 0.1785 0.1835 0.1594 -0.0129 -0.0235 -0.0030 479 LEU D CA  
17871 C C   . LEU D 487 ? 0.1635 0.1737 0.1399 -0.0160 -0.0250 -0.0018 479 LEU D C   
17872 O O   . LEU D 487 ? 0.1523 0.1598 0.1252 -0.0168 -0.0251 0.0006  479 LEU D O   
17873 C CB  . LEU D 487 ? 0.1786 0.1827 0.1624 -0.0094 -0.0258 0.0003  479 LEU D CB  
17874 C CG  . LEU D 487 ? 0.1568 0.1551 0.1439 -0.0064 -0.0241 -0.0008 479 LEU D CG  
17875 C CD1 . LEU D 487 ? 0.1389 0.1385 0.1307 -0.0031 -0.0258 0.0010  479 LEU D CD1 
17876 C CD2 . LEU D 487 ? 0.1222 0.1130 0.1068 -0.0060 -0.0232 0.0000  479 LEU D CD2 
17877 N N   . ARG D 488 ? 0.1332 0.1514 0.1095 -0.0180 -0.0259 -0.0035 480 ARG D N   
17878 C CA  . ARG D 488 ? 0.1737 0.1984 0.1445 -0.0215 -0.0273 -0.0027 480 ARG D CA  
17879 C C   . ARG D 488 ? 0.2105 0.2347 0.1783 -0.0249 -0.0240 -0.0064 480 ARG D C   
17880 O O   . ARG D 488 ? 0.1970 0.2254 0.1593 -0.0279 -0.0243 -0.0054 480 ARG D O   
17881 C CB  . ARG D 488 ? 0.1489 0.1833 0.1204 -0.0233 -0.0292 -0.0047 480 ARG D CB  
17882 C CG  . ARG D 488 ? 0.1488 0.1860 0.1241 -0.0201 -0.0330 -0.0008 480 ARG D CG  
17883 C CD  . ARG D 488 ? 0.1742 0.2225 0.1507 -0.0225 -0.0351 -0.0035 480 ARG D CD  
17884 N NE  . ARG D 488 ? 0.1675 0.2202 0.1478 -0.0195 -0.0395 0.0009  480 ARG D NE  
17885 C CZ  . ARG D 488 ? 0.1625 0.2200 0.1497 -0.0184 -0.0403 -0.0013 480 ARG D CZ  
17886 N NH1 . ARG D 488 ? 0.1759 0.2342 0.1664 -0.0204 -0.0370 -0.0077 480 ARG D NH1 
17887 N NH2 . ARG D 488 ? 0.1488 0.2104 0.1404 -0.0153 -0.0445 0.0030  480 ARG D NH2 
17888 N N   . LEU D 489 ? 0.1757 0.1952 0.1472 -0.0244 -0.0208 -0.0105 481 LEU D N   
17889 C CA  . LEU D 489 ? 0.1275 0.1465 0.0982 -0.0271 -0.0176 -0.0144 481 LEU D CA  
17890 C C   . LEU D 489 ? 0.2304 0.2431 0.1999 -0.0262 -0.0168 -0.0118 481 LEU D C   
17891 O O   . LEU D 489 ? 0.1824 0.1953 0.1522 -0.0281 -0.0142 -0.0148 481 LEU D O   
17892 C CB  . LEU D 489 ? 0.1306 0.1478 0.1073 -0.0271 -0.0148 -0.0199 481 LEU D CB  
17893 C CG  . LEU D 489 ? 0.2089 0.2319 0.1881 -0.0285 -0.0151 -0.0233 481 LEU D CG  
17894 C CD1 . LEU D 489 ? 0.2336 0.2533 0.2193 -0.0286 -0.0121 -0.0280 481 LEU D CD1 
17895 C CD2 . LEU D 489 ? 0.2358 0.2678 0.2105 -0.0326 -0.0155 -0.0258 481 LEU D CD2 
17896 N N   . ILE D 490 ? 0.1642 0.1719 0.1335 -0.0233 -0.0188 -0.0069 482 ILE D N   
17897 C CA  . ILE D 490 ? 0.1411 0.1435 0.1092 -0.0230 -0.0183 -0.0045 482 ILE D CA  
17898 C C   . ILE D 490 ? 0.1824 0.1890 0.1451 -0.0264 -0.0186 -0.0022 482 ILE D C   
17899 O O   . ILE D 490 ? 0.1649 0.1746 0.1243 -0.0266 -0.0213 0.0021  482 ILE D O   
17900 C CB  . ILE D 490 ? 0.1281 0.1240 0.0976 -0.0194 -0.0203 -0.0004 482 ILE D CB  
17901 C CG1 . ILE D 490 ? 0.1236 0.1162 0.0973 -0.0166 -0.0197 -0.0028 482 ILE D CG1 
17902 C CG2 . ILE D 490 ? 0.1560 0.1466 0.1246 -0.0198 -0.0198 0.0015  482 ILE D CG2 
17903 C CD1 . ILE D 490 ? 0.1434 0.1311 0.1188 -0.0131 -0.0213 -0.0000 482 ILE D CD1 
17904 N N   . PRO D 491 ? 0.1672 0.1746 0.1290 -0.0291 -0.0159 -0.0045 483 PRO D N   
17905 C CA  . PRO D 491 ? 0.1912 0.2027 0.1472 -0.0327 -0.0156 -0.0018 483 PRO D CA  
17906 C C   . PRO D 491 ? 0.1807 0.1872 0.1349 -0.0314 -0.0182 0.0055  483 PRO D C   
17907 O O   . PRO D 491 ? 0.1813 0.1803 0.1392 -0.0286 -0.0186 0.0067  483 PRO D O   
17908 C CB  . PRO D 491 ? 0.2045 0.2164 0.1624 -0.0350 -0.0117 -0.0061 483 PRO D CB  
17909 C CG  . PRO D 491 ? 0.1579 0.1686 0.1222 -0.0332 -0.0101 -0.0121 483 PRO D CG  
17910 C CD  . PRO D 491 ? 0.2186 0.2238 0.1852 -0.0290 -0.0129 -0.0095 483 PRO D CD  
17911 N N   . ASN D 492 ? 0.1821 0.1929 0.1306 -0.0336 -0.0201 0.0104  484 ASN D N   
17912 C CA  . ASN D 492 ? 0.2469 0.2529 0.1938 -0.0329 -0.0226 0.0181  484 ASN D CA  
17913 C C   . ASN D 492 ? 0.2316 0.2316 0.1834 -0.0278 -0.0258 0.0209  484 ASN D C   
17914 O O   . ASN D 492 ? 0.2550 0.2477 0.2090 -0.0260 -0.0269 0.0251  484 ASN D O   
17915 C CB  . ASN D 492 ? 0.2619 0.2626 0.2097 -0.0345 -0.0201 0.0188  484 ASN D CB  
17916 C CG  . ASN D 492 ? 0.2686 0.2661 0.2135 -0.0357 -0.0220 0.0270  484 ASN D CG  
17917 O OD1 . ASN D 492 ? 0.2414 0.2438 0.1807 -0.0377 -0.0239 0.0320  484 ASN D OD1 
17918 N ND2 . ASN D 492 ? 0.1673 0.1563 0.1163 -0.0345 -0.0217 0.0288  484 ASN D ND2 
17919 N N   . MET D 493 ? 0.1977 0.2006 0.1519 -0.0255 -0.0269 0.0182  485 MET D N   
17920 C CA  . MET D 493 ? 0.2185 0.2176 0.1776 -0.0208 -0.0297 0.0204  485 MET D CA  
17921 C C   . MET D 493 ? 0.2156 0.2220 0.1732 -0.0207 -0.0333 0.0237  485 MET D C   
17922 O O   . MET D 493 ? 0.2403 0.2548 0.1952 -0.0231 -0.0330 0.0204  485 MET D O   
17923 C CB  . MET D 493 ? 0.1837 0.1804 0.1479 -0.0182 -0.0279 0.0146  485 MET D CB  
17924 C CG  . MET D 493 ? 0.2270 0.2218 0.1963 -0.0138 -0.0301 0.0158  485 MET D CG  
17925 S SD  . MET D 493 ? 0.2053 0.1902 0.1784 -0.0105 -0.0312 0.0198  485 MET D SD  
17926 C CE  . MET D 493 ? 0.1629 0.1419 0.1373 -0.0102 -0.0276 0.0141  485 MET D CE  
17927 N N   . ASP D 494 ? 0.1955 0.1991 0.1556 -0.0178 -0.0368 0.0298  486 ASP D N   
17928 C CA  . ASP D 494 ? 0.2109 0.2214 0.1719 -0.0165 -0.0409 0.0330  486 ASP D CA  
17929 C C   . ASP D 494 ? 0.2215 0.2308 0.1905 -0.0119 -0.0413 0.0298  486 ASP D C   
17930 O O   . ASP D 494 ? 0.2413 0.2426 0.2157 -0.0085 -0.0405 0.0297  486 ASP D O   
17931 C CB  . ASP D 494 ? 0.2154 0.2241 0.1756 -0.0157 -0.0450 0.0423  486 ASP D CB  
17932 C CG  . ASP D 494 ? 0.2687 0.2824 0.2194 -0.0209 -0.0455 0.0466  486 ASP D CG  
17933 O OD1 . ASP D 494 ? 0.2881 0.3075 0.2331 -0.0252 -0.0425 0.0415  486 ASP D OD1 
17934 O OD2 . ASP D 494 ? 0.2403 0.2523 0.1897 -0.0209 -0.0487 0.0552  486 ASP D OD2 
17935 N N   . VAL D 495 ? 0.1543 0.1720 0.1242 -0.0123 -0.0423 0.0268  487 VAL D N   
17936 C CA  . VAL D 495 ? 0.1755 0.1940 0.1532 -0.0086 -0.0426 0.0239  487 VAL D CA  
17937 C C   . VAL D 495 ? 0.1961 0.2218 0.1768 -0.0069 -0.0477 0.0285  487 VAL D C   
17938 O O   . VAL D 495 ? 0.1945 0.2296 0.1708 -0.0100 -0.0500 0.0293  487 VAL D O   
17939 C CB  . VAL D 495 ? 0.1816 0.2040 0.1596 -0.0106 -0.0393 0.0163  487 VAL D CB  
17940 C CG1 . VAL D 495 ? 0.1987 0.2222 0.1847 -0.0073 -0.0391 0.0136  487 VAL D CG1 
17941 C CG2 . VAL D 495 ? 0.1645 0.1801 0.1402 -0.0121 -0.0349 0.0125  487 VAL D CG2 
17942 N N   . TRP D 496 ? 0.1601 0.1821 0.1488 -0.0020 -0.0496 0.0314  488 TRP D N   
17943 C CA  . TRP D 496 ? 0.2020 0.2308 0.1963 0.0007  -0.0547 0.0358  488 TRP D CA  
17944 C C   . TRP D 496 ? 0.1775 0.2092 0.1813 0.0040  -0.0537 0.0309  488 TRP D C   
17945 O O   . TRP D 496 ? 0.2026 0.2273 0.2109 0.0065  -0.0501 0.0273  488 TRP D O   
17946 C CB  . TRP D 496 ? 0.1677 0.1903 0.1654 0.0041  -0.0581 0.0439  488 TRP D CB  
17947 C CG  . TRP D 496 ? 0.1795 0.2009 0.1684 0.0007  -0.0601 0.0507  488 TRP D CG  
17948 C CD1 . TRP D 496 ? 0.2636 0.2768 0.2470 -0.0017 -0.0570 0.0512  488 TRP D CD1 
17949 C CD2 . TRP D 496 ? 0.2296 0.2586 0.2144 -0.0009 -0.0655 0.0583  488 TRP D CD2 
17950 N NE1 . TRP D 496 ? 0.2224 0.2375 0.1985 -0.0048 -0.0596 0.0586  488 TRP D NE1 
17951 C CE2 . TRP D 496 ? 0.2330 0.2578 0.2092 -0.0045 -0.0650 0.0632  488 TRP D CE2 
17952 C CE3 . TRP D 496 ? 0.2168 0.2565 0.2044 0.0002  -0.0710 0.0615  488 TRP D CE3 
17953 C CZ2 . TRP D 496 ? 0.2058 0.2364 0.1751 -0.0072 -0.0695 0.0715  488 TRP D CZ2 
17954 C CZ3 . TRP D 496 ? 0.2161 0.2619 0.1969 -0.0023 -0.0760 0.0697  488 TRP D CZ3 
17955 C CH2 . TRP D 496 ? 0.2697 0.3107 0.2409 -0.0061 -0.0752 0.0749  488 TRP D CH2 
17956 N N   . ARG D 497 ? 0.1907 0.2333 0.1974 0.0037  -0.0569 0.0307  489 ARG D N   
17957 C CA  . ARG D 497 ? 0.1842 0.2314 0.2009 0.0065  -0.0563 0.0266  489 ARG D CA  
17958 C C   . ARG D 497 ? 0.1928 0.2486 0.2162 0.0092  -0.0627 0.0319  489 ARG D C   
17959 O O   . ARG D 497 ? 0.1914 0.2587 0.2150 0.0070  -0.0654 0.0307  489 ARG D O   
17960 C CB  . ARG D 497 ? 0.1907 0.2434 0.2052 0.0025  -0.0529 0.0192  489 ARG D CB  
17961 C CG  . ARG D 497 ? 0.1391 0.1956 0.1635 0.0046  -0.0509 0.0142  489 ARG D CG  
17962 C CD  . ARG D 497 ? 0.1976 0.2571 0.2195 0.0002  -0.0468 0.0074  489 ARG D CD  
17963 N NE  . ARG D 497 ? 0.2486 0.3099 0.2793 0.0018  -0.0438 0.0030  489 ARG D NE  
17964 C CZ  . ARG D 497 ? 0.2165 0.2881 0.2542 0.0012  -0.0452 0.0007  489 ARG D CZ  
17965 N NH1 . ARG D 497 ? 0.1574 0.2389 0.1941 -0.0010 -0.0500 0.0021  489 ARG D NH1 
17966 N NH2 . ARG D 497 ? 0.1848 0.2575 0.2304 0.0024  -0.0417 -0.0032 489 ARG D NH2 
17967 N N   . PRO D 498 ? 0.2036 0.2544 0.2331 0.0140  -0.0655 0.0378  490 PRO D N   
17968 C CA  . PRO D 498 ? 0.1829 0.2415 0.2187 0.0167  -0.0726 0.0446  490 PRO D CA  
17969 C C   . PRO D 498 ? 0.2157 0.2839 0.2636 0.0196  -0.0738 0.0411  490 PRO D C   
17970 O O   . PRO D 498 ? 0.1895 0.2554 0.2443 0.0215  -0.0690 0.0347  490 PRO D O   
17971 C CB  . PRO D 498 ? 0.1914 0.2395 0.2323 0.0214  -0.0741 0.0511  490 PRO D CB  
17972 C CG  . PRO D 498 ? 0.2186 0.2554 0.2607 0.0225  -0.0673 0.0449  490 PRO D CG  
17973 C CD  . PRO D 498 ? 0.1851 0.2227 0.2164 0.0168  -0.0626 0.0387  490 PRO D CD  
17974 N N   . CYS D 499 ? 0.2323 0.3122 0.2830 0.0198  -0.0804 0.0455  491 CYS D N   
17975 C CA  . CYS D 499 ? 0.2039 0.2951 0.2662 0.0217  -0.0820 0.0419  491 CYS D CA  
17976 C C   . CYS D 499 ? 0.2082 0.3002 0.2863 0.0289  -0.0858 0.0462  491 CYS D C   
17977 O O   . CYS D 499 ? 0.2227 0.3231 0.3127 0.0312  -0.0859 0.0422  491 CYS D O   
17978 C CB  . CYS D 499 ? 0.2013 0.3072 0.2587 0.0172  -0.0870 0.0424  491 CYS D CB  
17979 S SG  . CYS D 499 ? 0.2291 0.3429 0.2859 0.0187  -0.0975 0.0544  491 CYS D SG  
17980 N N   . ASP D 500 ? 0.2148 0.2984 0.2942 0.0326  -0.0887 0.0540  492 ASP D N   
17981 C CA  . ASP D 500 ? 0.2232 0.3068 0.3191 0.0399  -0.0926 0.0585  492 ASP D CA  
17982 C C   . ASP D 500 ? 0.1954 0.2644 0.2909 0.0428  -0.0927 0.0647  492 ASP D C   
17983 O O   . ASP D 500 ? 0.1902 0.2500 0.2729 0.0390  -0.0895 0.0652  492 ASP D O   
17984 C CB  . ASP D 500 ? 0.2411 0.3391 0.3425 0.0410  -0.1015 0.0649  492 ASP D CB  
17985 C CG  . ASP D 500 ? 0.2818 0.3816 0.3697 0.0373  -0.1076 0.0743  492 ASP D CG  
17986 O OD1 . ASP D 500 ? 0.2465 0.3347 0.3250 0.0359  -0.1061 0.0785  492 ASP D OD1 
17987 O OD2 . ASP D 500 ? 0.2741 0.3875 0.3603 0.0353  -0.1136 0.0771  492 ASP D OD2 
17988 N N   . THR D 501 ? 0.2229 0.2898 0.3336 0.0497  -0.0963 0.0696  493 THR D N   
17989 C CA  . THR D 501 ? 0.2384 0.2906 0.3514 0.0528  -0.0961 0.0751  493 THR D CA  
17990 C C   . THR D 501 ? 0.2126 0.2616 0.3127 0.0492  -0.1009 0.0856  493 THR D C   
17991 O O   . THR D 501 ? 0.2894 0.3253 0.3848 0.0486  -0.0986 0.0883  493 THR D O   
17992 C CB  . THR D 501 ? 0.2809 0.3320 0.4143 0.0611  -0.0994 0.0782  493 THR D CB  
17993 O OG1 . THR D 501 ? 0.3375 0.3988 0.4711 0.0616  -0.1054 0.0843  493 THR D OG1 
17994 C CG2 . THR D 501 ? 0.3160 0.3706 0.4630 0.0646  -0.0941 0.0674  493 THR D CG2 
17995 N N   . ALA D 502 ? 0.2179 0.2786 0.3109 0.0463  -0.1063 0.0904  494 ALA D N   
17996 C CA  . ALA D 502 ? 0.2287 0.2866 0.3066 0.0420  -0.1084 0.0984  494 ALA D CA  
17997 C C   . ALA D 502 ? 0.2430 0.2981 0.3051 0.0351  -0.1050 0.0961  494 ALA D C   
17998 O O   . ALA D 502 ? 0.2275 0.2723 0.2813 0.0328  -0.1032 0.1003  494 ALA D O   
17999 C CB  . ALA D 502 ? 0.2375 0.3088 0.3111 0.0405  -0.1142 0.1025  494 ALA D CB  
18000 N N   . GLU D 503 ? 0.2117 0.2752 0.2689 0.0313  -0.1020 0.0874  495 GLU D N   
18001 C CA  . GLU D 503 ? 0.2063 0.2654 0.2485 0.0249  -0.0959 0.0819  495 GLU D CA  
18002 C C   . GLU D 503 ? 0.2018 0.2455 0.2462 0.0266  -0.0891 0.0776  495 GLU D C   
18003 O O   . GLU D 503 ? 0.2023 0.2386 0.2360 0.0227  -0.0859 0.0780  495 GLU D O   
18004 C CB  . GLU D 503 ? 0.1970 0.2666 0.2350 0.0209  -0.0930 0.0723  495 GLU D CB  
18005 C CG  . GLU D 503 ? 0.2019 0.2875 0.2350 0.0176  -0.0994 0.0753  495 GLU D CG  
18006 C CD  . GLU D 503 ? 0.2254 0.3195 0.2515 0.0118  -0.0957 0.0655  495 GLU D CD  
18007 O OE1 . GLU D 503 ? 0.2234 0.3114 0.2501 0.0112  -0.0886 0.0569  495 GLU D OE1 
18008 O OE2 . GLU D 503 ? 0.2136 0.3205 0.2335 0.0078  -0.1000 0.0664  495 GLU D OE2 
18009 N N   . SER D 504 ? 0.1980 0.2375 0.2565 0.0323  -0.0870 0.0734  496 SER D N   
18010 C CA  A SER D 504 ? 0.2068 0.2326 0.2672 0.0336  -0.0807 0.0686  496 SER D CA  
18011 C CA  B SER D 504 ? 0.2081 0.2339 0.2686 0.0337  -0.0807 0.0686  496 SER D CA  
18012 C C   . SER D 504 ? 0.2039 0.2179 0.2634 0.0345  -0.0823 0.0767  496 SER D C   
18013 O O   . SER D 504 ? 0.2025 0.2068 0.2550 0.0318  -0.0778 0.0745  496 SER D O   
18014 C CB  A SER D 504 ? 0.2176 0.2425 0.2934 0.0394  -0.0781 0.0623  496 SER D CB  
18015 C CB  B SER D 504 ? 0.2145 0.2396 0.2905 0.0395  -0.0783 0.0624  496 SER D CB  
18016 O OG  A SER D 504 ? 0.1957 0.2294 0.2713 0.0377  -0.0748 0.0538  496 SER D OG  
18017 O OG  B SER D 504 ? 0.1885 0.2010 0.2667 0.0409  -0.0726 0.0578  496 SER D OG  
18018 N N   . LEU D 505 ? 0.2142 0.2288 0.2814 0.0382  -0.0888 0.0863  497 LEU D N   
18019 C CA  . LEU D 505 ? 0.2556 0.2584 0.3226 0.0388  -0.0904 0.0949  497 LEU D CA  
18020 C C   . LEU D 505 ? 0.2468 0.2495 0.2962 0.0316  -0.0903 0.0994  497 LEU D C   
18021 O O   . LEU D 505 ? 0.2304 0.2219 0.2754 0.0295  -0.0871 0.1005  497 LEU D O   
18022 C CB  . LEU D 505 ? 0.2744 0.2782 0.3515 0.0436  -0.0957 0.1029  497 LEU D CB  
18023 C CG  . LEU D 505 ? 0.2953 0.2872 0.3707 0.0432  -0.0956 0.1104  497 LEU D CG  
18024 C CD1 . LEU D 505 ? 0.2638 0.2408 0.3468 0.0455  -0.0906 0.1059  497 LEU D CD1 
18025 C CD2 . LEU D 505 ? 0.3302 0.3244 0.4134 0.0472  -0.1003 0.1175  497 LEU D CD2 
18026 N N   . VAL D 506 ? 0.2712 0.2868 0.3106 0.0274  -0.0933 0.1011  498 VAL D N   
18027 C CA  . VAL D 506 ? 0.2314 0.2485 0.2540 0.0203  -0.0928 0.1045  498 VAL D CA  
18028 C C   . VAL D 506 ? 0.2212 0.2334 0.2359 0.0162  -0.0848 0.0946  498 VAL D C   
18029 O O   . VAL D 506 ? 0.2263 0.2318 0.2325 0.0122  -0.0822 0.0966  498 VAL D O   
18030 C CB  . VAL D 506 ? 0.2845 0.3173 0.2984 0.0166  -0.0969 0.1063  498 VAL D CB  
18031 C CG1 . VAL D 506 ? 0.2377 0.2728 0.2341 0.0089  -0.0948 0.1075  498 VAL D CG1 
18032 C CG2 . VAL D 506 ? 0.2713 0.3077 0.2912 0.0203  -0.1019 0.1132  498 VAL D CG2 
18033 N N   . ALA D 507 ? 0.2097 0.2256 0.2274 0.0170  -0.0810 0.0841  499 ALA D N   
18034 C CA  . ALA D 507 ? 0.2004 0.2116 0.2119 0.0137  -0.0739 0.0750  499 ALA D CA  
18035 C C   . ALA D 507 ? 0.2477 0.2443 0.2626 0.0152  -0.0704 0.0748  499 ALA D C   
18036 O O   . ALA D 507 ? 0.2094 0.2010 0.2159 0.0111  -0.0668 0.0734  499 ALA D O   
18037 C CB  . ALA D 507 ? 0.2084 0.2250 0.2248 0.0151  -0.0709 0.0651  499 ALA D CB  
18038 N N   . TRP D 508 ? 0.2380 0.2282 0.2659 0.0212  -0.0715 0.0759  500 TRP D N   
18039 C CA  . TRP D 508 ? 0.2528 0.2291 0.2852 0.0227  -0.0685 0.0755  500 TRP D CA  
18040 C C   . TRP D 508 ? 0.2169 0.1870 0.2437 0.0197  -0.0705 0.0848  500 TRP D C   
18041 O O   . TRP D 508 ? 0.2324 0.1942 0.2548 0.0168  -0.0666 0.0831  500 TRP D O   
18042 C CB  . TRP D 508 ? 0.2978 0.2695 0.3465 0.0298  -0.0696 0.0749  500 TRP D CB  
18043 C CG  . TRP D 508 ? 0.1996 0.1709 0.2538 0.0320  -0.0646 0.0638  500 TRP D CG  
18044 C CD1 . TRP D 508 ? 0.1939 0.1739 0.2545 0.0349  -0.0645 0.0588  500 TRP D CD1 
18045 C CD2 . TRP D 508 ? 0.1957 0.1579 0.2493 0.0314  -0.0589 0.0565  500 TRP D CD2 
18046 N NE1 . TRP D 508 ? 0.2161 0.1929 0.2793 0.0357  -0.0587 0.0491  500 TRP D NE1 
18047 C CE2 . TRP D 508 ? 0.2129 0.1789 0.2717 0.0337  -0.0555 0.0475  500 TRP D CE2 
18048 C CE3 . TRP D 508 ? 0.2236 0.1754 0.2728 0.0287  -0.0564 0.0567  500 TRP D CE3 
18049 C CZ2 . TRP D 508 ? 0.2302 0.1900 0.2888 0.0335  -0.0499 0.0391  500 TRP D CZ2 
18050 C CZ3 . TRP D 508 ? 0.2515 0.1974 0.3015 0.0286  -0.0512 0.0479  500 TRP D CZ3 
18051 C CH2 . TRP D 508 ? 0.2205 0.1705 0.2747 0.0310  -0.0481 0.0394  500 TRP D CH2 
18052 N N   . ALA D 509 ? 0.2653 0.2396 0.2923 0.0203  -0.0766 0.0952  501 ALA D N   
18053 C CA  . ALA D 509 ? 0.2526 0.2211 0.2742 0.0172  -0.0786 0.1054  501 ALA D CA  
18054 C C   . ALA D 509 ? 0.2789 0.2510 0.2845 0.0096  -0.0754 0.1041  501 ALA D C   
18055 O O   . ALA D 509 ? 0.2482 0.2121 0.2497 0.0062  -0.0730 0.1068  501 ALA D O   
18056 C CB  . ALA D 509 ? 0.2503 0.2245 0.2740 0.0190  -0.0850 0.1156  501 ALA D CB  
18057 N N   . GLU D 510 ? 0.2300 0.2144 0.2273 0.0066  -0.0752 0.0996  502 GLU D N   
18058 C CA  . GLU D 510 ? 0.2412 0.2296 0.2245 -0.0005 -0.0716 0.0971  502 GLU D CA  
18059 C C   . GLU D 510 ? 0.2594 0.2401 0.2426 -0.0017 -0.0649 0.0879  502 GLU D C   
18060 O O   . GLU D 510 ? 0.2519 0.2298 0.2275 -0.0066 -0.0617 0.0882  502 GLU D O   
18061 C CB  . GLU D 510 ? 0.2825 0.2856 0.2587 -0.0031 -0.0727 0.0931  502 GLU D CB  
18062 C CG  . GLU D 510 ? 0.2444 0.2570 0.2169 -0.0038 -0.0795 0.1027  502 GLU D CG  
18063 C CD  . GLU D 510 ? 0.2750 0.2859 0.2377 -0.0087 -0.0807 0.1125  502 GLU D CD  
18064 O OE1 . GLU D 510 ? 0.2932 0.3052 0.2455 -0.0146 -0.0761 0.1091  502 GLU D OE1 
18065 O OE2 . GLU D 510 ? 0.3263 0.3346 0.2932 -0.0063 -0.0837 0.1203  502 GLU D OE2 
18066 N N   . ALA D 511 ? 0.2417 0.2197 0.2333 0.0025  -0.0626 0.0798  503 ALA D N   
18067 C CA  . ALA D 511 ? 0.2021 0.1728 0.1940 0.0017  -0.0570 0.0718  503 ALA D CA  
18068 C C   . ALA D 511 ? 0.2624 0.2206 0.2579 0.0018  -0.0560 0.0756  503 ALA D C   
18069 O O   . ALA D 511 ? 0.3007 0.2545 0.2919 -0.0017 -0.0521 0.0724  503 ALA D O   
18070 C CB  . ALA D 511 ? 0.1930 0.1637 0.1928 0.0061  -0.0551 0.0634  503 ALA D CB  
18071 N N   . ALA D 512 ? 0.2565 0.2090 0.2607 0.0058  -0.0597 0.0825  504 ALA D N   
18072 C CA  . ALA D 512 ? 0.2674 0.2074 0.2762 0.0057  -0.0590 0.0866  504 ALA D CA  
18073 C C   . ALA D 512 ? 0.2994 0.2392 0.2985 -0.0004 -0.0592 0.0944  504 ALA D C   
18074 O O   . ALA D 512 ? 0.3089 0.2401 0.3079 -0.0030 -0.0564 0.0946  504 ALA D O   
18075 C CB  . ALA D 512 ? 0.2436 0.1775 0.2654 0.0116  -0.0631 0.0925  504 ALA D CB  
18076 N N   . LYS D 513 ? 0.2820 0.2318 0.2728 -0.0029 -0.0625 0.1005  505 LYS D N   
18077 C CA  . LYS D 513 ? 0.3181 0.2692 0.2991 -0.0090 -0.0628 0.1087  505 LYS D CA  
18078 C C   . LYS D 513 ? 0.3111 0.2667 0.2816 -0.0151 -0.0575 0.1021  505 LYS D C   
18079 O O   . LYS D 513 ? 0.3385 0.2922 0.3028 -0.0204 -0.0557 0.1066  505 LYS D O   
18080 C CB  . LYS D 513 ? 0.3551 0.3165 0.3302 -0.0097 -0.0684 0.1176  505 LYS D CB  
18081 C CG  . LYS D 513 ? 0.4626 0.4200 0.4467 -0.0051 -0.0729 0.1259  505 LYS D CG  
18082 C CD  . LYS D 513 ? 0.5199 0.4905 0.4985 -0.0054 -0.0772 0.1303  505 LYS D CD  
18083 C CE  . LYS D 513 ? 0.5911 0.5699 0.5541 -0.0130 -0.0758 0.1333  505 LYS D CE  
18084 N NZ  . LYS D 513 ? 0.6024 0.5945 0.5598 -0.0136 -0.0800 0.1365  505 LYS D NZ  
18085 N N   . ALA D 514 ? 0.2744 0.1927 0.2450 -0.0436 -0.0463 0.1097  506 ALA D N   
18086 C CA  . ALA D 514 ? 0.3664 0.3199 0.3430 -0.0465 -0.0331 0.1018  506 ALA D CA  
18087 C C   . ALA D 514 ? 0.3598 0.3146 0.3458 -0.0580 -0.0363 0.1063  506 ALA D C   
18088 O O   . ALA D 514 ? 0.4009 0.3268 0.3920 -0.0535 -0.0447 0.1031  506 ALA D O   
18089 C CB  . ALA D 514 ? 0.2333 0.1890 0.2143 -0.0284 -0.0255 0.0818  506 ALA D CB  
18090 N N   . GLU D 515 ? 0.2829 0.2739 0.2711 -0.0735 -0.0299 0.1135  507 GLU D N   
18091 C CA  . GLU D 515 ? 0.3201 0.3186 0.3192 -0.0877 -0.0334 0.1196  507 GLU D CA  
18092 C C   . GLU D 515 ? 0.3663 0.3899 0.3807 -0.0782 -0.0242 0.1018  507 GLU D C   
18093 O O   . GLU D 515 ? 0.3745 0.3877 0.3994 -0.0811 -0.0302 0.1005  507 GLU D O   
18094 C CB  . GLU D 515 ? 0.4369 0.4653 0.4314 -0.1137 -0.0328 0.1398  507 GLU D CB  
18095 C CG  . GLU D 515 ? 0.5348 0.5306 0.5128 -0.1252 -0.0471 0.1597  507 GLU D CG  
18096 C CD  . GLU D 515 ? 0.6717 0.6940 0.6447 -0.1481 -0.0492 0.1737  507 GLU D CD  
18097 O OE1 . GLU D 515 ? 0.7285 0.7266 0.6902 -0.1527 -0.0623 0.1819  507 GLU D OE1 
18098 O OE2 . GLU D 515 ? 0.7086 0.7783 0.6899 -0.1610 -0.0382 0.1755  507 GLU D OE2 
18099 N N   . ASP D 516 ? 0.2647 0.3170 0.2795 -0.0656 -0.0123 0.0870  508 ASP D N   
18100 C CA  . ASP D 516 ? 0.2370 0.3169 0.2663 -0.0567 -0.0059 0.0702  508 ASP D CA  
18101 C C   . ASP D 516 ? 0.2043 0.2674 0.2316 -0.0339 -0.0049 0.0506  508 ASP D C   
18102 O O   . ASP D 516 ? 0.1951 0.2820 0.2306 -0.0237 -0.0006 0.0350  508 ASP D O   
18103 C CB  . ASP D 516 ? 0.2469 0.3855 0.2808 -0.0637 0.0055  0.0686  508 ASP D CB  
18104 C CG  . ASP D 516 ? 0.2692 0.4212 0.2889 -0.0542 0.0129  0.0619  508 ASP D CG  
18105 O OD1 . ASP D 516 ? 0.2641 0.3809 0.2703 -0.0485 0.0084  0.0649  508 ASP D OD1 
18106 O OD2 . ASP D 516 ? 0.2884 0.4877 0.3107 -0.0518 0.0226  0.0524  508 ASP D OD2 
18107 N N   . HIS D 517 ? 0.2031 0.2274 0.2197 -0.0260 -0.0098 0.0507  509 HIS D N   
18108 C CA  . HIS D 517 ? 0.2251 0.2346 0.2386 -0.0088 -0.0099 0.0348  509 HIS D CA  
18109 C C   . HIS D 517 ? 0.2193 0.1887 0.2259 -0.0043 -0.0162 0.0369  509 HIS D C   
18110 O O   . HIS D 517 ? 0.2015 0.1562 0.2032 -0.0101 -0.0199 0.0485  509 HIS D O   
18111 C CB  . HIS D 517 ? 0.1876 0.2142 0.1927 -0.0010 -0.0042 0.0269  509 HIS D CB  
18112 C CG  . HIS D 517 ? 0.2350 0.2587 0.2283 -0.0065 -0.0032 0.0382  509 HIS D CG  
18113 N ND1 . HIS D 517 ? 0.2520 0.3013 0.2419 -0.0189 0.0007  0.0496  509 HIS D ND1 
18114 C CD2 . HIS D 517 ? 0.2465 0.2473 0.2304 -0.0016 -0.0062 0.0398  509 HIS D CD2 
18115 C CE1 . HIS D 517 ? 0.3124 0.3501 0.2902 -0.0208 -0.0014 0.0581  509 HIS D CE1 
18116 N NE2 . HIS D 517 ? 0.2741 0.2838 0.2498 -0.0096 -0.0055 0.0517  509 HIS D NE2 
18117 N N   . PRO D 518 ? 0.2146 0.1670 0.2199 0.0060  -0.0185 0.0256  510 PRO D N   
18118 C CA  . PRO D 518 ? 0.2501 0.1726 0.2482 0.0108  -0.0225 0.0255  510 PRO D CA  
18119 C C   . PRO D 518 ? 0.2219 0.1437 0.2111 0.0159  -0.0197 0.0240  510 PRO D C   
18120 O O   . PRO D 518 ? 0.2089 0.1478 0.1955 0.0169  -0.0161 0.0215  510 PRO D O   
18121 C CB  . PRO D 518 ? 0.1841 0.0944 0.1827 0.0166  -0.0258 0.0151  510 PRO D CB  
18122 C CG  . PRO D 518 ? 0.1791 0.1104 0.1814 0.0204  -0.0239 0.0062  510 PRO D CG  
18123 C CD  . PRO D 518 ? 0.1857 0.1474 0.1960 0.0134  -0.0188 0.0123  510 PRO D CD  
18124 N N   . SER D 519 ? 0.2608 0.1644 0.2457 0.0196  -0.0220 0.0243  511 SER D N   
18125 C CA  . SER D 519 ? 0.2583 0.1629 0.2371 0.0233  -0.0201 0.0231  511 SER D CA  
18126 C C   . SER D 519 ? 0.2416 0.1338 0.2160 0.0276  -0.0209 0.0167  511 SER D C   
18127 O O   . SER D 519 ? 0.2362 0.1159 0.2113 0.0293  -0.0233 0.0149  511 SER D O   
18128 C CB  . SER D 519 ? 0.2097 0.1140 0.1891 0.0225  -0.0220 0.0321  511 SER D CB  
18129 O OG  . SER D 519 ? 0.2351 0.1519 0.2148 0.0155  -0.0215 0.0403  511 SER D OG  
18130 N N   . CYS D 520 ? 0.1902 0.0867 0.1586 0.0280  -0.0196 0.0136  512 CYS D N   
18131 C CA  . CYS D 520 ? 0.2231 0.1152 0.1862 0.0285  -0.0193 0.0104  512 CYS D CA  
18132 C C   . CYS D 520 ? 0.2366 0.1402 0.2026 0.0300  -0.0174 0.0136  512 CYS D C   
18133 O O   . CYS D 520 ? 0.2224 0.1348 0.1877 0.0280  -0.0176 0.0162  512 CYS D O   
18134 C CB  . CYS D 520 ? 0.2338 0.1214 0.1874 0.0247  -0.0219 0.0064  512 CYS D CB  
18135 S SG  . CYS D 520 ? 0.2545 0.1279 0.2055 0.0254  -0.0274 0.0009  512 CYS D SG  
18136 N N   . LEU D 521 ? 0.2433 0.1481 0.2127 0.0347  -0.0166 0.0120  513 LEU D N   
18137 C CA  . LEU D 521 ? 0.2374 0.1567 0.2126 0.0384  -0.0159 0.0130  513 LEU D CA  
18138 C C   . LEU D 521 ? 0.2495 0.1821 0.2216 0.0359  -0.0120 0.0084  513 LEU D C   
18139 O O   . LEU D 521 ? 0.2122 0.1429 0.1811 0.0383  -0.0101 0.0030  513 LEU D O   
18140 C CB  . LEU D 521 ? 0.2110 0.1247 0.1941 0.0478  -0.0201 0.0129  513 LEU D CB  
18141 C CG  . LEU D 521 ? 0.2540 0.1524 0.2380 0.0462  -0.0255 0.0199  513 LEU D CG  
18142 C CD1 . LEU D 521 ? 0.2108 0.0986 0.2007 0.0549  -0.0339 0.0207  513 LEU D CD1 
18143 C CD2 . LEU D 521 ? 0.2396 0.1462 0.2215 0.0394  -0.0248 0.0275  513 LEU D CD2 
18144 N N   . ILE D 522 ? 0.1850 0.1320 0.1566 0.0296  -0.0113 0.0112  514 ILE D N   
18145 C CA  . ILE D 522 ? 0.1846 0.1456 0.1508 0.0209  -0.0086 0.0102  514 ILE D CA  
18146 C C   . ILE D 522 ? 0.1915 0.1822 0.1697 0.0237  -0.0059 0.0094  514 ILE D C   
18147 O O   . ILE D 522 ? 0.2035 0.2014 0.1882 0.0238  -0.0090 0.0132  514 ILE D O   
18148 C CB  . ILE D 522 ? 0.1875 0.1388 0.1426 0.0087  -0.0132 0.0145  514 ILE D CB  
18149 C CG1 . ILE D 522 ? 0.2288 0.1543 0.1741 0.0083  -0.0169 0.0127  514 ILE D CG1 
18150 C CG2 . ILE D 522 ? 0.1958 0.1609 0.1443 -0.0046 -0.0128 0.0170  514 ILE D CG2 
18151 C CD1 . ILE D 522 ? 0.2801 0.1916 0.2149 0.0009  -0.0250 0.0138  514 ILE D CD1 
18152 N N   . PHE D 523 ? 0.1880 0.1988 0.1690 0.0262  -0.0004 0.0036  515 PHE D N   
18153 C CA  . PHE D 523 ? 0.1969 0.2425 0.1934 0.0329  0.0024  -0.0007 515 PHE D CA  
18154 C C   . PHE D 523 ? 0.2498 0.3287 0.2442 0.0199  0.0089  -0.0006 515 PHE D C   
18155 O O   . PHE D 523 ? 0.2165 0.2929 0.1966 0.0106  0.0126  -0.0006 515 PHE D O   
18156 C CB  . PHE D 523 ? 0.1930 0.2402 0.1988 0.0528  0.0023  -0.0114 515 PHE D CB  
18157 C CG  . PHE D 523 ? 0.2153 0.2305 0.2230 0.0626  -0.0061 -0.0091 515 PHE D CG  
18158 C CD1 . PHE D 523 ? 0.3039 0.3203 0.3223 0.0689  -0.0128 -0.0053 515 PHE D CD1 
18159 C CD2 . PHE D 523 ? 0.2344 0.2193 0.2323 0.0633  -0.0082 -0.0093 515 PHE D CD2 
18160 C CE1 . PHE D 523 ? 0.2636 0.2514 0.2808 0.0741  -0.0212 -0.0005 515 PHE D CE1 
18161 C CE2 . PHE D 523 ? 0.2253 0.1842 0.2247 0.0683  -0.0161 -0.0049 515 PHE D CE2 
18162 C CZ  . PHE D 523 ? 0.2651 0.2254 0.2731 0.0727  -0.0224 0.0002  515 PHE D CZ  
18163 N N   . SER D 524 ? 0.2676 0.3799 0.2759 0.0178  0.0096  0.0004  516 SER D N   
18164 C CA  . SER D 524 ? 0.3272 0.4784 0.3357 0.0024  0.0159  0.0022  516 SER D CA  
18165 C C   . SER D 524 ? 0.4639 0.6553 0.4842 0.0155  0.0248  -0.0109 516 SER D C   
18166 O O   . SER D 524 ? 0.4253 0.6185 0.4599 0.0387  0.0230  -0.0217 516 SER D O   
18167 C CB  . SER D 524 ? 0.3371 0.5102 0.3562 -0.0085 0.0118  0.0096  516 SER D CB  
18168 O OG  . SER D 524 ? 0.3335 0.5268 0.3751 0.0097  0.0100  0.0031  516 SER D OG  
18169 N N   . ARG D 525 ? 0.6894 0.9128 0.7021 0.0003  0.0333  -0.0102 517 ARG D N   
18170 C CA  . ARG D 525 ? 0.8142 1.0886 0.8386 0.0114  0.0436  -0.0243 517 ARG D CA  
18171 C C   . ARG D 525 ? 0.8234 1.1411 0.8773 0.0237  0.0433  -0.0308 517 ARG D C   
18172 O O   . ARG D 525 ? 0.8123 1.1469 0.8829 0.0501  0.0436  -0.0472 517 ARG D O   
18173 C CB  . ARG D 525 ? 0.8490 1.1558 0.8579 -0.0131 0.0531  -0.0188 517 ARG D CB  
18174 N N   . GLN D 526 ? 0.8452 1.1784 0.9058 0.0056  0.0401  -0.0187 518 GLN D N   
18175 C CA  . GLN D 526 ? 0.8251 1.2023 0.9147 0.0149  0.0385  -0.0237 518 GLN D CA  
18176 C C   . GLN D 526 ? 0.7710 1.1133 0.8715 0.0385  0.0265  -0.0274 518 GLN D C   
18177 O O   . GLN D 526 ? 0.7001 0.9925 0.7875 0.0330  0.0180  -0.0167 518 GLN D O   
18178 C CB  . GLN D 526 ? 0.8209 1.2199 0.9124 -0.0138 0.0363  -0.0082 518 GLN D CB  
18179 N N   . ASN D 527 ? 0.8056 1.1750 0.9292 0.0650  0.0249  -0.0431 519 ASN D N   
18180 C CA  . ASN D 527 ? 0.7600 1.1022 0.8952 0.0849  0.0108  -0.0446 519 ASN D CA  
18181 C C   . ASN D 527 ? 0.6906 1.0453 0.8357 0.0713  0.0042  -0.0326 519 ASN D C   
18182 O O   . ASN D 527 ? 0.7128 1.1235 0.8765 0.0643  0.0082  -0.0343 519 ASN D O   
18183 C CB  . ASN D 527 ? 0.7496 1.1184 0.9075 0.1172  0.0073  -0.0653 519 ASN D CB  
18184 N N   . LEU D 528 ? 0.5742 0.8799 0.7067 0.0667  -0.0059 -0.0207 520 LEU D N   
18185 C CA  . LEU D 528 ? 0.5535 0.8616 0.6877 0.0508  -0.0129 -0.0084 520 LEU D CA  
18186 C C   . LEU D 528 ? 0.5353 0.8511 0.6897 0.0692  -0.0256 -0.0117 520 LEU D C   
18187 O O   . LEU D 528 ? 0.5534 0.8432 0.7093 0.0908  -0.0334 -0.0174 520 LEU D O   
18188 C CB  . LEU D 528 ? 0.5361 0.7899 0.6431 0.0360  -0.0168 0.0044  520 LEU D CB  
18189 C CG  . LEU D 528 ? 0.4581 0.6928 0.5443 0.0244  -0.0077 0.0058  520 LEU D CG  
18190 C CD1 . LEU D 528 ? 0.3753 0.5553 0.4381 0.0186  -0.0127 0.0138  520 LEU D CD1 
18191 C CD2 . LEU D 528 ? 0.4954 0.7640 0.5797 0.0006  -0.0013 0.0107  520 LEU D CD2 
18192 N N   . LYS D 529 ? 0.5575 0.9072 0.7265 0.0591  -0.0298 -0.0071 521 LYS D N   
18193 C CA  . LYS D 529 ? 0.5806 0.9434 0.7706 0.0758  -0.0433 -0.0103 521 LYS D CA  
18194 C C   . LYS D 529 ? 0.5764 0.8809 0.7488 0.0819  -0.0564 -0.0019 521 LYS D C   
18195 O O   . LYS D 529 ? 0.5846 0.8497 0.7315 0.0667  -0.0553 0.0087  521 LYS D O   
18196 C CB  . LYS D 529 ? 0.5568 0.9635 0.7628 0.0592  -0.0463 -0.0047 521 LYS D CB  
18197 N N   . PHE D 530 ? 0.6297 0.9306 0.8158 0.1044  -0.0699 -0.0071 522 PHE D N   
18198 C CA  . PHE D 530 ? 0.6538 0.9021 0.8228 0.1103  -0.0835 0.0016  522 PHE D CA  
18199 C C   . PHE D 530 ? 0.6865 0.9343 0.8530 0.0996  -0.0946 0.0127  522 PHE D C   
18200 O O   . PHE D 530 ? 0.7224 1.0062 0.9121 0.1060  -0.1031 0.0091  522 PHE D O   
18201 C CB  . PHE D 530 ? 0.6134 0.8504 0.7945 0.1387  -0.0965 -0.0079 522 PHE D CB  
18202 C CG  . PHE D 530 ? 0.5861 0.7643 0.7448 0.1406  -0.1091 0.0032  522 PHE D CG  
18203 C CD1 . PHE D 530 ? 0.5636 0.7039 0.7039 0.1407  -0.1051 0.0047  522 PHE D CD1 
18204 C CD2 . PHE D 530 ? 0.5741 0.7357 0.7280 0.1386  -0.1238 0.0137  522 PHE D CD2 
18205 C CE1 . PHE D 530 ? 0.5753 0.6661 0.6944 0.1372  -0.1148 0.0169  522 PHE D CE1 
18206 C CE2 . PHE D 530 ? 0.5883 0.7002 0.7183 0.1354  -0.1327 0.0260  522 PHE D CE2 
18207 C CZ  . PHE D 530 ? 0.5762 0.6545 0.6893 0.1336  -0.1276 0.0279  522 PHE D CZ  
18208 N N   . GLN D 531 ? 0.6468 0.8563 0.7856 0.0845  -0.0951 0.0249  523 GLN D N   
18209 C CA  . GLN D 531 ? 0.5955 0.7982 0.7258 0.0750  -0.1064 0.0347  523 GLN D CA  
18210 C C   . GLN D 531 ? 0.5436 0.7181 0.6683 0.0890  -0.1232 0.0399  523 GLN D C   
18211 O O   . GLN D 531 ? 0.5570 0.6989 0.6702 0.0970  -0.1243 0.0414  523 GLN D O   
18212 C CB  . GLN D 531 ? 0.5991 0.7755 0.7006 0.0544  -0.1000 0.0428  523 GLN D CB  
18213 N N   . ALA D 532 ? 0.5131 0.6992 0.6449 0.0903  -0.1379 0.0438  524 ALA D N   
18214 C CA  . ALA D 532 ? 0.4559 0.6129 0.5784 0.1004  -0.1564 0.0514  524 ALA D CA  
18215 C C   . ALA D 532 ? 0.4759 0.5913 0.5615 0.0864  -0.1551 0.0642  524 ALA D C   
18216 O O   . ALA D 532 ? 0.4579 0.5730 0.5275 0.0694  -0.1453 0.0668  524 ALA D O   
18217 C CB  . ALA D 532 ? 0.4935 0.6723 0.6277 0.1009  -0.1680 0.0532  524 ALA D CB  
18218 N N   . ARG D 533 ? 0.4868 0.5681 0.5559 0.0910  -0.1592 0.0703  525 ARG D N   
18219 C CA  . ARG D 533 ? 0.3139 0.3630 0.3497 0.0776  -0.1558 0.0814  525 ARG D CA  
18220 C C   . ARG D 533 ? 0.4007 0.4255 0.4200 0.0776  -0.1660 0.0904  525 ARG D C   
18221 O O   . ARG D 533 ? 0.4643 0.4808 0.4945 0.0895  -0.1742 0.0886  525 ARG D O   
18222 C CB  . ARG D 533 ? 0.3270 0.3581 0.3563 0.0764  -0.1449 0.0807  525 ARG D CB  
18223 C CG  . ARG D 533 ? 0.3396 0.3853 0.3693 0.0671  -0.1284 0.0745  525 ARG D CG  
18224 C CD  . ARG D 533 ? 0.3915 0.4162 0.4091 0.0635  -0.1166 0.0748  525 ARG D CD  
18225 N NE  . ARG D 533 ? 0.3745 0.4134 0.3982 0.0590  -0.1005 0.0652  525 ARG D NE  
18226 C CZ  . ARG D 533 ? 0.3279 0.3839 0.3722 0.0674  -0.0954 0.0551  525 ARG D CZ  
18227 N NH1 . ARG D 533 ? 0.3317 0.3944 0.3946 0.0838  -0.1050 0.0507  525 ARG D NH1 
18228 N NH2 . ARG D 533 ? 0.3693 0.4359 0.4144 0.0601  -0.0818 0.0489  525 ARG D NH2 
18229 N N   . SER D 534 ? 0.3572 0.3712 0.3496 0.0638  -0.1658 0.0995  526 SER D N   
18230 C CA  . SER D 534 ? 0.3897 0.3798 0.3615 0.0591  -0.1739 0.1101  526 SER D CA  
18231 C C   . SER D 534 ? 0.3970 0.3620 0.3560 0.0541  -0.1681 0.1157  526 SER D C   
18232 O O   . SER D 534 ? 0.3756 0.3415 0.3382 0.0533  -0.1566 0.1116  526 SER D O   
18233 C CB  . SER D 534 ? 0.3996 0.3919 0.3465 0.0458  -0.1739 0.1163  526 SER D CB  
18234 O OG  . SER D 534 ? 0.4119 0.4042 0.3414 0.0345  -0.1600 0.1164  526 SER D OG  
18235 N N   . GLU D 535 ? 0.4613 0.4037 0.4053 0.0491  -0.1772 0.1259  527 GLU D N   
18236 C CA  . GLU D 535 ? 0.4783 0.3988 0.4089 0.0399  -0.1729 0.1331  527 GLU D CA  
18237 C C   . GLU D 535 ? 0.4550 0.3840 0.3674 0.0256  -0.1570 0.1360  527 GLU D C   
18238 O O   . GLU D 535 ? 0.4329 0.3575 0.3463 0.0227  -0.1472 0.1347  527 GLU D O   
18239 C CB  . GLU D 535 ? 0.5357 0.4324 0.4509 0.0327  -0.1873 0.1454  527 GLU D CB  
18240 N N   . GLN D 536 ? 0.4907 0.4329 0.3864 0.0175  -0.1545 0.1384  528 GLN D N   
18241 C CA  . GLN D 536 ? 0.4666 0.4201 0.3445 0.0059  -0.1399 0.1384  528 GLN D CA  
18242 C C   . GLN D 536 ? 0.4530 0.4181 0.3447 0.0114  -0.1290 0.1273  528 GLN D C   
18243 O O   . GLN D 536 ? 0.3787 0.3450 0.2641 0.0054  -0.1173 0.1268  528 GLN D O   
18244 C CB  . GLN D 536 ? 0.4659 0.4320 0.3241 -0.0005 -0.1410 0.1393  528 GLN D CB  
18245 C CG  . GLN D 536 ? 0.4604 0.4416 0.2999 -0.0092 -0.1266 0.1353  528 GLN D CG  
18246 C CD  . GLN D 536 ? 0.5151 0.4941 0.3383 -0.0216 -0.1188 0.1441  528 GLN D CD  
18247 O OE1 . GLN D 536 ? 0.5907 0.5593 0.4042 -0.0293 -0.1260 0.1559  528 GLN D OE1 
18248 N NE2 . GLN D 536 ? 0.4553 0.4457 0.2759 -0.0247 -0.1048 0.1386  528 GLN D NE2 
18249 N N   . GLN D 537 ? 0.4275 0.4030 0.3387 0.0218  -0.1331 0.1188  529 GLN D N   
18250 C CA  . GLN D 537 ? 0.4178 0.4040 0.3429 0.0254  -0.1247 0.1095  529 GLN D CA  
18251 C C   . GLN D 537 ? 0.3574 0.3317 0.2938 0.0300  -0.1197 0.1086  529 GLN D C   
18252 O O   . GLN D 537 ? 0.3912 0.3672 0.3259 0.0266  -0.1091 0.1055  529 GLN D O   
18253 C CB  . GLN D 537 ? 0.3662 0.3697 0.3132 0.0338  -0.1316 0.1020  529 GLN D CB  
18254 C CG  . GLN D 537 ? 0.3846 0.4017 0.3213 0.0270  -0.1342 0.0997  529 GLN D CG  
18255 C CD  . GLN D 537 ? 0.4283 0.4655 0.3892 0.0328  -0.1430 0.0942  529 GLN D CD  
18256 O OE1 . GLN D 537 ? 0.4291 0.4699 0.4076 0.0431  -0.1517 0.0943  529 GLN D OE1 
18257 N NE2 . GLN D 537 ? 0.3990 0.4505 0.3615 0.0261  -0.1393 0.0873  529 GLN D NE2 
18258 N N   . LEU D 538 ? 0.4362 0.3971 0.3835 0.0382  -0.1281 0.1102  530 LEU D N   
18259 C CA  . LEU D 538 ? 0.3803 0.3271 0.3367 0.0429  -0.1247 0.1077  530 LEU D CA  
18260 C C   . LEU D 538 ? 0.4222 0.3576 0.3600 0.0291  -0.1166 0.1154  530 LEU D C   
18261 O O   . LEU D 538 ? 0.4115 0.3431 0.3538 0.0290  -0.1084 0.1119  530 LEU D O   
18262 C CB  . LEU D 538 ? 0.4247 0.3567 0.3921 0.0534  -0.1375 0.1072  530 LEU D CB  
18263 C CG  . LEU D 538 ? 0.4475 0.3936 0.4414 0.0716  -0.1435 0.0953  530 LEU D CG  
18264 C CD1 . LEU D 538 ? 0.5290 0.4582 0.5275 0.0801  -0.1586 0.0961  530 LEU D CD1 
18265 C CD2 . LEU D 538 ? 0.4120 0.3648 0.4219 0.0800  -0.1343 0.0838  530 LEU D CD2 
18266 N N   . ASN D 539 ? 0.3617 0.2944 0.2792 0.0170  -0.1187 0.1258  531 ASN D N   
18267 C CA  . ASN D 539 ? 0.4095 0.3392 0.3111 0.0026  -0.1106 0.1333  531 ASN D CA  
18268 C C   . ASN D 539 ? 0.3464 0.2959 0.2400 -0.0026 -0.0963 0.1286  531 ASN D C   
18269 O O   . ASN D 539 ? 0.4289 0.3812 0.3159 -0.0116 -0.0876 0.1315  531 ASN D O   
18270 C CB  . ASN D 539 ? 0.4951 0.4205 0.3776 -0.0100 -0.1171 0.1459  531 ASN D CB  
18271 C CG  . ASN D 539 ? 0.4824 0.3829 0.3702 -0.0077 -0.1328 0.1518  531 ASN D CG  
18272 O OD1 . ASN D 539 ? 0.5113 0.3969 0.4137 -0.0002 -0.1362 0.1475  531 ASN D OD1 
18273 N ND2 . ASN D 539 ? 0.4874 0.3826 0.3626 -0.0138 -0.1434 0.1610  531 ASN D ND2 
18274 N N   . ASP D 540 ? 0.3317 0.2957 0.2262 0.0024  -0.0949 0.1210  532 ASP D N   
18275 C CA  . ASP D 540 ? 0.3564 0.3375 0.2421 -0.0014 -0.0831 0.1136  532 ASP D CA  
18276 C C   . ASP D 540 ? 0.3013 0.2827 0.2063 0.0064  -0.0733 0.0995  532 ASP D C   
18277 O O   . ASP D 540 ? 0.2946 0.2857 0.1954 0.0049  -0.0623 0.0895  532 ASP D O   
18278 C CB  . ASP D 540 ? 0.3188 0.3132 0.1943 -0.0011 -0.0857 0.1080  532 ASP D CB  
18279 C CG  . ASP D 540 ? 0.3722 0.3727 0.2234 -0.0104 -0.0872 0.1156  532 ASP D CG  
18280 O OD1 . ASP D 540 ? 0.4447 0.4462 0.2863 -0.0192 -0.0815 0.1227  532 ASP D OD1 
18281 O OD2 . ASP D 540 ? 0.3946 0.4004 0.2375 -0.0096 -0.0932 0.1131  532 ASP D OD2 
18282 N N   . ILE D 541 ? 0.2813 0.2524 0.2057 0.0152  -0.0779 0.0977  533 ILE D N   
18283 C CA  . ILE D 541 ? 0.2591 0.2311 0.1986 0.0207  -0.0685 0.0858  533 ILE D CA  
18284 C C   . ILE D 541 ? 0.2600 0.2288 0.1937 0.0151  -0.0586 0.0851  533 ILE D C   
18285 O O   . ILE D 541 ? 0.2512 0.2253 0.1870 0.0157  -0.0493 0.0745  533 ILE D O   
18286 C CB  . ILE D 541 ? 0.2868 0.2507 0.2458 0.0317  -0.0750 0.0839  533 ILE D CB  
18287 C CG1 . ILE D 541 ? 0.2602 0.2352 0.2299 0.0387  -0.0842 0.0820  533 ILE D CG1 
18288 C CG2 . ILE D 541 ? 0.2727 0.2382 0.2431 0.0356  -0.0646 0.0724  533 ILE D CG2 
18289 C CD1 . ILE D 541 ? 0.2666 0.2376 0.2559 0.0528  -0.0928 0.0786  533 ILE D CD1 
18290 N N   . LYS D 542 ? 0.2948 0.2549 0.2207 0.0083  -0.0620 0.0971  534 LYS D N   
18291 C CA  . LYS D 542 ? 0.3086 0.2701 0.2319 0.0018  -0.0530 0.0969  534 LYS D CA  
18292 C C   . LYS D 542 ? 0.3065 0.2899 0.2179 -0.0035 -0.0425 0.0908  534 LYS D C   
18293 O O   . LYS D 542 ? 0.3070 0.2976 0.2194 -0.0069 -0.0343 0.0875  534 LYS D O   
18294 C CB  . LYS D 542 ? 0.2893 0.2378 0.2066 -0.0078 -0.0608 0.1133  534 LYS D CB  
18295 C CG  . LYS D 542 ? 0.3135 0.2689 0.2117 -0.0190 -0.0664 0.1272  534 LYS D CG  
18296 C CD  . LYS D 542 ? 0.4297 0.3749 0.3247 -0.0312 -0.0703 0.1381  534 LYS D CD  
18297 C CE  . LYS D 542 ? 0.5277 0.4608 0.4161 -0.0339 -0.0827 0.1462  534 LYS D CE  
18298 N NZ  . LYS D 542 ? 0.5026 0.4149 0.4057 -0.0180 -0.0939 0.1401  534 LYS D NZ  
18299 N N   . ARG D 543 ? 0.2859 0.2807 0.1865 -0.0030 -0.0437 0.0878  535 ARG D N   
18300 C CA  . ARG D 543 ? 0.2665 0.2811 0.1552 -0.0042 -0.0355 0.0778  535 ARG D CA  
18301 C C   . ARG D 543 ? 0.2497 0.2622 0.1458 0.0048  -0.0324 0.0604  535 ARG D C   
18302 O O   . ARG D 543 ? 0.2525 0.2766 0.1389 0.0072  -0.0292 0.0490  535 ARG D O   
18303 C CB  . ARG D 543 ? 0.3279 0.3539 0.1973 -0.0082 -0.0401 0.0820  535 ARG D CB  
18304 C CG  . ARG D 543 ? 0.3338 0.3601 0.1913 -0.0199 -0.0454 0.1017  535 ARG D CG  
18305 C CD  . ARG D 543 ? 0.3479 0.3931 0.1802 -0.0268 -0.0463 0.1052  535 ARG D CD  
18306 N NE  . ARG D 543 ? 0.3641 0.4384 0.1859 -0.0300 -0.0333 0.0964  535 ARG D NE  
18307 C CZ  . ARG D 543 ? 0.3543 0.4524 0.1544 -0.0368 -0.0298 0.0972  535 ARG D CZ  
18308 N NH1 . ARG D 543 ? 0.3760 0.4654 0.1652 -0.0411 -0.0382 0.1052  535 ARG D NH1 
18309 N NH2 . ARG D 543 ? 0.3887 0.5182 0.1836 -0.0370 -0.0170 0.0858  535 ARG D NH2 
18310 N N   . GLY D 544 ? 0.2581 0.2560 0.1696 0.0096  -0.0344 0.0580  536 GLY D N   
18311 C CA  . GLY D 544 ? 0.2626 0.2557 0.1793 0.0145  -0.0325 0.0447  536 GLY D CA  
18312 C C   . GLY D 544 ? 0.2463 0.2378 0.1609 0.0155  -0.0393 0.0398  536 GLY D C   
18313 O O   . GLY D 544 ? 0.2321 0.2163 0.1549 0.0163  -0.0406 0.0351  536 GLY D O   
18314 N N   . ALA D 545 ? 0.3063 0.3054 0.2090 0.0137  -0.0442 0.0419  537 ALA D N   
18315 C CA  . ALA D 545 ? 0.2994 0.2976 0.2003 0.0129  -0.0528 0.0392  537 ALA D CA  
18316 C C   . ALA D 545 ? 0.3014 0.3074 0.1926 0.0106  -0.0591 0.0475  537 ALA D C   
18317 O O   . ALA D 545 ? 0.3019 0.3150 0.1797 0.0087  -0.0563 0.0518  537 ALA D O   
18318 C CB  . ALA D 545 ? 0.2508 0.2442 0.1406 0.0139  -0.0561 0.0255  537 ALA D CB  
18319 N N   . TYR D 546 ? 0.2601 0.2670 0.1578 0.0097  -0.0679 0.0503  538 TYR D N   
18320 C CA  . TYR D 546 ? 0.2908 0.3033 0.1811 0.0080  -0.0768 0.0587  538 TYR D CA  
18321 C C   . TYR D 546 ? 0.3063 0.3224 0.2048 0.0066  -0.0868 0.0565  538 TYR D C   
18322 O O   . TYR D 546 ? 0.3183 0.3345 0.2307 0.0055  -0.0859 0.0514  538 TYR D O   
18323 C CB  . TYR D 546 ? 0.2773 0.2874 0.1757 0.0095  -0.0786 0.0719  538 TYR D CB  
18324 C CG  . TYR D 546 ? 0.2960 0.3051 0.2197 0.0150  -0.0798 0.0719  538 TYR D CG  
18325 C CD1 . TYR D 546 ? 0.2474 0.2515 0.1820 0.0176  -0.0706 0.0673  538 TYR D CD1 
18326 C CD2 . TYR D 546 ? 0.3298 0.3460 0.2666 0.0185  -0.0902 0.0750  538 TYR D CD2 
18327 C CE1 . TYR D 546 ? 0.2366 0.2437 0.1924 0.0234  -0.0707 0.0653  538 TYR D CE1 
18328 C CE2 . TYR D 546 ? 0.2924 0.3149 0.2535 0.0253  -0.0902 0.0722  538 TYR D CE2 
18329 C CZ  . TYR D 546 ? 0.2474 0.2657 0.2167 0.0276  -0.0798 0.0670  538 TYR D CZ  
18330 O OH  . TYR D 546 ? 0.2724 0.3006 0.2636 0.0349  -0.0788 0.0625  538 TYR D OH  
18331 N N   . VAL D 547 ? 0.3433 0.3641 0.2326 0.0049  -0.0970 0.0613  539 VAL D N   
18332 C CA  . VAL D 547 ? 0.2950 0.3224 0.1929 0.0022  -0.1083 0.0601  539 VAL D CA  
18333 C C   . VAL D 547 ? 0.3126 0.3498 0.2364 0.0064  -0.1119 0.0674  539 VAL D C   
18334 O O   . VAL D 547 ? 0.2998 0.3369 0.2233 0.0104  -0.1185 0.0763  539 VAL D O   
18335 C CB  . VAL D 547 ? 0.3968 0.4252 0.2733 -0.0008 -0.1195 0.0609  539 VAL D CB  
18336 C CG1 . VAL D 547 ? 0.4060 0.4410 0.2923 -0.0055 -0.1323 0.0588  539 VAL D CG1 
18337 C CG2 . VAL D 547 ? 0.3930 0.4149 0.2424 -0.0012 -0.1150 0.0510  539 VAL D CG2 
18338 N N   . ILE D 548 ? 0.2696 0.3161 0.2151 0.0059  -0.1087 0.0632  540 ILE D N   
18339 C CA  . ILE D 548 ? 0.2613 0.3235 0.2336 0.0127  -0.1110 0.0662  540 ILE D CA  
18340 C C   . ILE D 548 ? 0.3328 0.4148 0.3176 0.0107  -0.1241 0.0677  540 ILE D C   
18341 O O   . ILE D 548 ? 0.2938 0.3892 0.2976 0.0196  -0.1309 0.0706  540 ILE D O   
18342 C CB  . ILE D 548 ? 0.2425 0.3122 0.2320 0.0132  -0.0998 0.0605  540 ILE D CB  
18343 C CG1 . ILE D 548 ? 0.2657 0.3541 0.2821 0.0242  -0.1010 0.0604  540 ILE D CG1 
18344 C CG2 . ILE D 548 ? 0.2849 0.3631 0.2757 0.0007  -0.0997 0.0559  540 ILE D CG2 
18345 C CD1 . ILE D 548 ? 0.2781 0.3743 0.3079 0.0264  -0.0890 0.0542  540 ILE D CD1 
18346 N N   . SER D 549 ? 0.3611 0.4444 0.3360 -0.0001 -0.1299 0.0652  541 SER D N   
18347 C CA  . SER D 549 ? 0.3167 0.4194 0.3032 -0.0042 -0.1439 0.0671  541 SER D CA  
18348 C C   . SER D 549 ? 0.3427 0.4306 0.3023 -0.0133 -0.1534 0.0655  541 SER D C   
18349 O O   . SER D 549 ? 0.3143 0.3944 0.2654 -0.0231 -0.1531 0.0600  541 SER D O   
18350 C CB  . SER D 549 ? 0.2709 0.4013 0.2844 -0.0110 -0.1418 0.0642  541 SER D CB  
18351 O OG  . SER D 549 ? 0.2797 0.4322 0.3058 -0.0168 -0.1558 0.0663  541 SER D OG  
18352 N N   . GLU D 550 ? 0.3743 0.4559 0.3195 -0.0092 -0.1612 0.0688  542 GLU D N   
18353 C CA  . GLU D 550 ? 0.4087 0.4765 0.3275 -0.0145 -0.1659 0.0634  542 GLU D CA  
18354 C C   . GLU D 550 ? 0.4382 0.5163 0.3676 -0.0240 -0.1763 0.0600  542 GLU D C   
18355 O O   . GLU D 550 ? 0.3951 0.4966 0.3526 -0.0257 -0.1808 0.0634  542 GLU D O   
18356 C CB  . GLU D 550 ? 0.4525 0.5140 0.3531 -0.0086 -0.1689 0.0678  542 GLU D CB  
18357 C CG  . GLU D 550 ? 0.5389 0.5896 0.4095 -0.0120 -0.1723 0.0610  542 GLU D CG  
18358 C CD  . GLU D 550 ? 0.5744 0.6122 0.4243 -0.0128 -0.1635 0.0517  542 GLU D CD  
18359 O OE1 . GLU D 550 ? 0.6125 0.6469 0.4512 -0.0086 -0.1536 0.0542  542 GLU D OE1 
18360 O OE2 . GLU D 550 ? 0.4342 0.4648 0.2796 -0.0175 -0.1674 0.0416  542 GLU D OE2 
18361 N N   . ALA D 551 ? 0.3686 0.4303 0.2763 -0.0301 -0.1801 0.0522  543 ALA D N   
18362 C CA  . ALA D 551 ? 0.4181 0.4840 0.3317 -0.0404 -0.1916 0.0495  543 ALA D CA  
18363 C C   . ALA D 551 ? 0.4867 0.5650 0.4044 -0.0372 -0.2013 0.0536  543 ALA D C   
18364 O O   . ALA D 551 ? 0.4223 0.4944 0.3233 -0.0287 -0.2008 0.0555  543 ALA D O   
18365 C CB  . ALA D 551 ? 0.4705 0.5110 0.3577 -0.0446 -0.1953 0.0389  543 ALA D CB  
18366 N N   . GLN D 552 ? 0.5150 0.6121 0.4551 -0.0451 -0.2103 0.0557  544 GLN D N   
18367 C CA  . GLN D 552 ? 0.4985 0.6057 0.4417 -0.0436 -0.2223 0.0577  544 GLN D CA  
18368 C C   . GLN D 552 ? 0.5568 0.6439 0.4749 -0.0510 -0.2310 0.0509  544 GLN D C   
18369 O O   . GLN D 552 ? 0.5601 0.6480 0.4854 -0.0635 -0.2384 0.0488  544 GLN D O   
18370 C CB  . GLN D 552 ? 0.4435 0.5848 0.4243 -0.0479 -0.2279 0.0616  544 GLN D CB  
18371 N N   . GLY D 553 ? 0.6041 0.6739 0.4920 -0.0436 -0.2303 0.0474  545 GLY D N   
18372 C CA  . GLY D 553 ? 0.5944 0.6452 0.4552 -0.0468 -0.2372 0.0381  545 GLY D CA  
18373 C C   . GLY D 553 ? 0.6000 0.6310 0.4375 -0.0427 -0.2275 0.0290  545 GLY D C   
18374 O O   . GLY D 553 ? 0.5466 0.5781 0.3885 -0.0385 -0.2154 0.0309  545 GLY D O   
18375 N N   . ASN D 554 ? 0.5180 0.5327 0.3312 -0.0431 -0.2337 0.0178  546 ASN D N   
18376 C CA  . ASN D 554 ? 0.5495 0.5480 0.3415 -0.0373 -0.2262 0.0059  546 ASN D CA  
18377 C C   . ASN D 554 ? 0.5081 0.4942 0.3144 -0.0431 -0.2237 0.0042  546 ASN D C   
18378 O O   . ASN D 554 ? 0.5595 0.5363 0.3757 -0.0540 -0.2340 0.0043  546 ASN D O   
18379 C CB  . ASN D 554 ? 0.6115 0.5964 0.3771 -0.0356 -0.2355 -0.0076 546 ASN D CB  
18380 N N   . ALA D 555 ? 0.4868 0.4728 0.2935 -0.0371 -0.2106 0.0039  547 ALA D N   
18381 C CA  . ALA D 555 ? 0.4724 0.4475 0.2923 -0.0426 -0.2077 0.0039  547 ALA D CA  
18382 C C   . ALA D 555 ? 0.6196 0.5661 0.4258 -0.0448 -0.2165 -0.0087 547 ALA D C   
18383 O O   . ALA D 555 ? 0.5539 0.4893 0.3375 -0.0352 -0.2173 -0.0219 547 ALA D O   
18384 C CB  . ALA D 555 ? 0.4477 0.4269 0.2678 -0.0342 -0.1925 0.0050  547 ALA D CB  
18385 N N   . GLN D 556 ? 0.5019 0.4372 0.3220 -0.0581 -0.2238 -0.0041 548 GLN D N   
18386 C CA  . GLN D 556 ? 0.5290 0.4310 0.3379 -0.0608 -0.2333 -0.0131 548 GLN D CA  
18387 C C   . GLN D 556 ? 0.5160 0.4044 0.3260 -0.0572 -0.2251 -0.0156 548 GLN D C   
18388 O O   . GLN D 556 ? 0.5401 0.3986 0.3375 -0.0534 -0.2320 -0.0255 548 GLN D O   
18389 C CB  . GLN D 556 ? 0.5471 0.4407 0.3670 -0.0799 -0.2476 -0.0043 548 GLN D CB  
18390 C CG  . GLN D 556 ? 0.5686 0.4692 0.3862 -0.0846 -0.2596 -0.0034 548 GLN D CG  
18391 C CD  . GLN D 556 ? 0.7090 0.5958 0.5337 -0.1041 -0.2755 0.0041  548 GLN D CD  
18392 O OE1 . GLN D 556 ? 0.7025 0.5574 0.5188 -0.1096 -0.2836 0.0024  548 GLN D OE1 
18393 N NE2 . GLN D 556 ? 0.7113 0.6222 0.5515 -0.1149 -0.2809 0.0136  548 GLN D NE2 
18394 N N   . ALA D 557 ? 0.4814 0.3897 0.3062 -0.0575 -0.2120 -0.0070 549 ALA D N   
18395 C CA  . ALA D 557 ? 0.4682 0.3652 0.2946 -0.0546 -0.2042 -0.0086 549 ALA D CA  
18396 C C   . ALA D 557 ? 0.5037 0.4279 0.3428 -0.0505 -0.1892 -0.0006 549 ALA D C   
18397 O O   . ALA D 557 ? 0.4180 0.3676 0.2680 -0.0521 -0.1868 0.0081  549 ALA D O   
18398 C CB  . ALA D 557 ? 0.4782 0.3578 0.3131 -0.0712 -0.2122 -0.0009 549 ALA D CB  
18399 N N   . VAL D 558 ? 0.4873 0.4042 0.3251 -0.0443 -0.1804 -0.0037 550 VAL D N   
18400 C CA  . VAL D 558 ? 0.4455 0.3832 0.2949 -0.0409 -0.1674 0.0043  550 VAL D CA  
18401 C C   . VAL D 558 ? 0.4339 0.3652 0.2944 -0.0496 -0.1647 0.0095  550 VAL D C   
18402 O O   . VAL D 558 ? 0.3878 0.2935 0.2392 -0.0484 -0.1675 0.0022  550 VAL D O   
18403 C CB  . VAL D 558 ? 0.4626 0.4031 0.2980 -0.0244 -0.1573 -0.0033 550 VAL D CB  
18404 C CG1 . VAL D 558 ? 0.4970 0.4147 0.3186 -0.0156 -0.1576 -0.0186 550 VAL D CG1 
18405 C CG2 . VAL D 558 ? 0.3741 0.3309 0.2213 -0.0222 -0.1456 0.0070  550 VAL D CG2 
18406 N N   . ILE D 559 ? 0.3892 0.3454 0.2698 -0.0580 -0.1600 0.0221  551 ILE D N   
18407 C CA  . ILE D 559 ? 0.3833 0.3415 0.2742 -0.0661 -0.1550 0.0280  551 ILE D CA  
18408 C C   . ILE D 559 ? 0.3311 0.2972 0.2280 -0.0506 -0.1358 0.0268  551 ILE D C   
18409 O O   . ILE D 559 ? 0.3112 0.2998 0.2204 -0.0427 -0.1262 0.0313  551 ILE D O   
18410 C CB  . ILE D 559 ? 0.3305 0.3194 0.2449 -0.0822 -0.1552 0.0404  551 ILE D CB  
18411 C CG1 . ILE D 559 ? 0.3559 0.3391 0.2688 -0.0960 -0.1682 0.0421  551 ILE D CG1 
18412 C CG2 . ILE D 559 ? 0.3443 0.3368 0.2674 -0.0911 -0.1464 0.0454  551 ILE D CG2 
18413 C CD1 . ILE D 559 ? 0.3763 0.3970 0.3139 -0.1124 -0.1682 0.0537  551 ILE D CD1 
18414 N N   . ILE D 560 ? 0.3160 0.2615 0.2039 -0.0464 -0.1322 0.0207  552 ILE D N   
18415 C CA  . ILE D 560 ? 0.2943 0.2455 0.1892 -0.0348 -0.1150 0.0201  552 ILE D CA  
18416 C C   . ILE D 560 ? 0.3070 0.2679 0.2176 -0.0437 -0.1078 0.0277  552 ILE D C   
18417 O O   . ILE D 560 ? 0.3515 0.2971 0.2560 -0.0557 -0.1157 0.0285  552 ILE D O   
18418 C CB  . ILE D 560 ? 0.3039 0.2312 0.1818 -0.0242 -0.1157 0.0079  552 ILE D CB  
18419 C CG1 . ILE D 560 ? 0.3757 0.2955 0.2347 -0.0162 -0.1247 -0.0027 552 ILE D CG1 
18420 C CG2 . ILE D 560 ? 0.2821 0.2182 0.1684 -0.0137 -0.0986 0.0083  552 ILE D CG2 
18421 C CD1 . ILE D 560 ? 0.3659 0.2658 0.2094 -0.0041 -0.1277 -0.0185 552 ILE D CD1 
18422 N N   . ALA D 561 ? 0.2641 0.2488 0.1926 -0.0378 -0.0941 0.0327  553 ALA D N   
18423 C CA  . ALA D 561 ? 0.2679 0.2667 0.2106 -0.0440 -0.0860 0.0376  553 ALA D CA  
18424 C C   . ALA D 561 ? 0.2287 0.2314 0.1791 -0.0301 -0.0718 0.0361  553 ALA D C   
18425 O O   . ALA D 561 ? 0.2337 0.2366 0.1841 -0.0183 -0.0685 0.0351  553 ALA D O   
18426 C CB  . ALA D 561 ? 0.2642 0.2968 0.2259 -0.0529 -0.0868 0.0445  553 ALA D CB  
18427 N N   . THR D 562 ? 0.2225 0.2276 0.1776 -0.0334 -0.0647 0.0369  554 THR D N   
18428 C CA  . THR D 562 ? 0.2452 0.2524 0.2076 -0.0216 -0.0531 0.0351  554 THR D CA  
18429 C C   . THR D 562 ? 0.2098 0.2433 0.1879 -0.0241 -0.0456 0.0370  554 THR D C   
18430 O O   . THR D 562 ? 0.2069 0.2551 0.1870 -0.0383 -0.0477 0.0403  554 THR D O   
18431 C CB  . THR D 562 ? 0.2210 0.2018 0.1701 -0.0199 -0.0517 0.0307  554 THR D CB  
18432 O OG1 . THR D 562 ? 0.2365 0.2129 0.1805 -0.0327 -0.0539 0.0325  554 THR D OG1 
18433 C CG2 . THR D 562 ? 0.2224 0.1819 0.1558 -0.0174 -0.0599 0.0256  554 THR D CG2 
18434 N N   . GLY D 563 ? 0.1890 0.2041 0.1785 0.0273  -0.0795 0.0099  555 GLY D N   
18435 C CA  . GLY D 563 ? 0.1737 0.1963 0.1752 0.0326  -0.0777 0.0107  555 GLY D CA  
18436 C C   . GLY D 563 ? 0.1961 0.2332 0.2096 0.0316  -0.0806 0.0113  555 GLY D C   
18437 O O   . GLY D 563 ? 0.1964 0.2397 0.2120 0.0302  -0.0870 0.0130  555 GLY D O   
18438 N N   . SER D 564 ? 0.1848 0.2277 0.2065 0.0319  -0.0759 0.0103  556 SER D N   
18439 C CA  . SER D 564 ? 0.2274 0.2862 0.2627 0.0315  -0.0772 0.0115  556 SER D CA  
18440 C C   . SER D 564 ? 0.2456 0.3095 0.2819 0.0230  -0.0816 0.0115  556 SER D C   
18441 O O   . SER D 564 ? 0.2581 0.3367 0.3070 0.0218  -0.0841 0.0133  556 SER D O   
18442 C CB  . SER D 564 ? 0.2157 0.2786 0.2577 0.0333  -0.0702 0.0106  556 SER D CB  
18443 O OG  . SER D 564 ? 0.2193 0.2717 0.2531 0.0287  -0.0657 0.0084  556 SER D OG  
18444 N N   . GLU D 565 ? 0.1749 0.2272 0.1983 0.0172  -0.0827 0.0096  557 GLU D N   
18445 C CA  . GLU D 565 ? 0.1820 0.2362 0.2039 0.0087  -0.0873 0.0091  557 GLU D CA  
18446 C C   . GLU D 565 ? 0.1962 0.2497 0.2124 0.0068  -0.0957 0.0103  557 GLU D C   
18447 O O   . GLU D 565 ? 0.2304 0.2850 0.2446 -0.0003 -0.1010 0.0100  557 GLU D O   
18448 C CB  . GLU D 565 ? 0.2308 0.2713 0.2408 0.0033  -0.0837 0.0056  557 GLU D CB  
18449 C CG  . GLU D 565 ? 0.2283 0.2710 0.2447 0.0015  -0.0779 0.0049  557 GLU D CG  
18450 C CD  . GLU D 565 ? 0.2115 0.2549 0.2324 0.0090  -0.0716 0.0054  557 GLU D CD  
18451 O OE1 . GLU D 565 ? 0.1895 0.2208 0.2015 0.0119  -0.0681 0.0039  557 GLU D OE1 
18452 O OE2 . GLU D 565 ? 0.2001 0.2562 0.2332 0.0121  -0.0703 0.0075  557 GLU D OE2 
18453 N N   . VAL D 566 ? 0.2244 0.2752 0.2371 0.0126  -0.0976 0.0119  558 VAL D N   
18454 C CA  . VAL D 566 ? 0.2016 0.2513 0.2079 0.0106  -0.1060 0.0136  558 VAL D CA  
18455 C C   . VAL D 566 ? 0.2710 0.3367 0.2918 0.0090  -0.1132 0.0164  558 VAL D C   
18456 O O   . VAL D 566 ? 0.2492 0.3153 0.2662 0.0028  -0.1207 0.0170  558 VAL D O   
18457 C CB  . VAL D 566 ? 0.2159 0.2594 0.2160 0.0170  -0.1068 0.0155  558 VAL D CB  
18458 C CG1 . VAL D 566 ? 0.2139 0.2573 0.2081 0.0150  -0.1163 0.0180  558 VAL D CG1 
18459 C CG2 . VAL D 566 ? 0.2159 0.2444 0.2018 0.0172  -0.1004 0.0132  558 VAL D CG2 
18460 N N   . GLY D 567 ? 0.2181 0.2976 0.2562 0.0144  -0.1109 0.0183  559 GLY D N   
18461 C CA  . GLY D 567 ? 0.2650 0.3621 0.3198 0.0134  -0.1170 0.0214  559 GLY D CA  
18462 C C   . GLY D 567 ? 0.2233 0.3257 0.2816 0.0037  -0.1191 0.0210  559 GLY D C   
18463 O O   . GLY D 567 ? 0.2275 0.3382 0.2917 -0.0010 -0.1278 0.0235  559 GLY D O   
18464 N N   . LEU D 568 ? 0.2539 0.3507 0.3085 0.0002  -0.1120 0.0183  560 LEU D N   
18465 C CA  . LEU D 568 ? 0.2113 0.3099 0.2671 -0.0097 -0.1143 0.0178  560 LEU D CA  
18466 C C   . LEU D 568 ? 0.2782 0.3637 0.3172 -0.0168 -0.1220 0.0162  560 LEU D C   
18467 O O   . LEU D 568 ? 0.2212 0.3116 0.2635 -0.0247 -0.1296 0.0175  560 LEU D O   
18468 C CB  . LEU D 568 ? 0.1943 0.2863 0.2469 -0.0115 -0.1054 0.0151  560 LEU D CB  
18469 C CG  . LEU D 568 ? 0.2797 0.3661 0.3272 -0.0220 -0.1073 0.0136  560 LEU D CG  
18470 C CD1 . LEU D 568 ? 0.2257 0.3307 0.2912 -0.0278 -0.1117 0.0176  560 LEU D CD1 
18471 C CD2 . LEU D 568 ? 0.3170 0.3929 0.3582 -0.0223 -0.0985 0.0107  560 LEU D CD2 
18472 N N   . ALA D 569 ? 0.2641 0.3327 0.2848 -0.0144 -0.1201 0.0134  561 ALA D N   
18473 C CA  . ALA D 569 ? 0.2378 0.2926 0.2400 -0.0202 -0.1263 0.0114  561 ALA D CA  
18474 C C   . ALA D 569 ? 0.2413 0.3029 0.2457 -0.0217 -0.1374 0.0149  561 ALA D C   
18475 O O   . ALA D 569 ? 0.2550 0.3119 0.2511 -0.0295 -0.1454 0.0144  561 ALA D O   
18476 C CB  . ALA D 569 ? 0.2973 0.3351 0.2811 -0.0162 -0.1207 0.0084  561 ALA D CB  
18477 N N   . VAL D 570 ? 0.2347 0.3062 0.2495 -0.0144 -0.1386 0.0183  562 VAL D N   
18478 C CA  . VAL D 570 ? 0.2432 0.3210 0.2609 -0.0152 -0.1491 0.0219  562 VAL D CA  
18479 C C   . VAL D 570 ? 0.2439 0.3379 0.2794 -0.0203 -0.1535 0.0243  562 VAL D C   
18480 O O   . VAL D 570 ? 0.2910 0.3845 0.3231 -0.0254 -0.1601 0.0250  562 VAL D O   
18481 C CB  . VAL D 570 ? 0.2905 0.3730 0.3145 -0.0051 -0.1471 0.0245  562 VAL D CB  
18482 C CG1 . VAL D 570 ? 0.4087 0.4986 0.4379 -0.0048 -0.1534 0.0275  562 VAL D CG1 
18483 C CG2 . VAL D 570 ? 0.3576 0.4229 0.3624 -0.0018 -0.1435 0.0228  562 VAL D CG2 
18484 N N   . GLU D 571 ? 0.2929 0.4015 0.3473 -0.0193 -0.1498 0.0257  563 GLU D N   
18485 C CA  . GLU D 571 ? 0.3230 0.4481 0.3952 -0.0248 -0.1531 0.0283  563 GLU D CA  
18486 C C   . GLU D 571 ? 0.3208 0.4359 0.3817 -0.0365 -0.1575 0.0263  563 GLU D C   
18487 O O   . GLU D 571 ? 0.3487 0.4700 0.4154 -0.0422 -0.1636 0.0281  563 GLU D O   
18488 C CB  . GLU D 571 ? 0.2561 0.3984 0.3494 -0.0216 -0.1462 0.0302  563 GLU D CB  
18489 N N   . ALA D 572 ? 0.2463 0.3449 0.2905 -0.0398 -0.1544 0.0222  564 ALA D N   
18490 C CA  . ALA D 572 ? 0.2610 0.3463 0.2912 -0.0500 -0.1584 0.0193  564 ALA D CA  
18491 C C   . ALA D 572 ? 0.2791 0.3512 0.2913 -0.0519 -0.1645 0.0179  564 ALA D C   
18492 O O   . ALA D 572 ? 0.3112 0.3790 0.3187 -0.0597 -0.1703 0.0175  564 ALA D O   
18493 C CB  . ALA D 572 ? 0.2602 0.3286 0.2757 -0.0505 -0.1500 0.0142  564 ALA D CB  
18494 N N   . GLN D 573 ? 0.3042 0.3693 0.3055 -0.0450 -0.1631 0.0173  565 GLN D N   
18495 C CA  . GLN D 573 ? 0.3280 0.3823 0.3130 -0.0465 -0.1685 0.0168  565 GLN D CA  
18496 C C   . GLN D 573 ? 0.3035 0.3709 0.3023 -0.0494 -0.1763 0.0208  565 GLN D C   
18497 O O   . GLN D 573 ? 0.3215 0.3802 0.3091 -0.0557 -0.1827 0.0201  565 GLN D O   
18498 C CB  . GLN D 573 ? 0.3367 0.3855 0.3127 -0.0383 -0.1655 0.0171  565 GLN D CB  
18499 C CG  . GLN D 573 ? 0.3587 0.3977 0.3187 -0.0397 -0.1709 0.0174  565 GLN D CG  
18500 C CD  . GLN D 573 ? 0.3979 0.4340 0.3521 -0.0320 -0.1682 0.0191  565 GLN D CD  
18501 O OE1 . GLN D 573 ? 0.3662 0.4144 0.3363 -0.0251 -0.1660 0.0221  565 GLN D OE1 
18502 N NE2 . GLN D 573 ? 0.4143 0.4339 0.3452 -0.0331 -0.1680 0.0172  565 GLN D NE2 
18503 N N   . LYS D 574 ? 0.3015 0.3895 0.3246 -0.0446 -0.1757 0.0250  566 LYS D N   
18504 C CA  . LYS D 574 ? 0.3340 0.4360 0.3723 -0.0466 -0.1827 0.0290  566 LYS D CA  
18505 C C   . LYS D 574 ? 0.3789 0.4844 0.4233 -0.0567 -0.1868 0.0294  566 LYS D C   
18506 O O   . LYS D 574 ? 0.3179 0.4239 0.3625 -0.0619 -0.1948 0.0312  566 LYS D O   
18507 C CB  . LYS D 574 ? 0.3513 0.4747 0.4142 -0.0380 -0.1798 0.0328  566 LYS D CB  
18508 C CG  . LYS D 574 ? 0.3372 0.4573 0.3952 -0.0281 -0.1774 0.0332  566 LYS D CG  
18509 C CD  . LYS D 574 ? 0.4223 0.5625 0.5042 -0.0193 -0.1749 0.0364  566 LYS D CD  
18510 C CE  . LYS D 574 ? 0.5051 0.6406 0.5812 -0.0104 -0.1745 0.0372  566 LYS D CE  
18511 N NZ  . LYS D 574 ? 0.5797 0.6981 0.6371 -0.0078 -0.1689 0.0344  566 LYS D NZ  
18512 N N   . VAL D 575 ? 0.3455 0.4529 0.3951 -0.0597 -0.1817 0.0282  567 VAL D N   
18513 C CA  . VAL D 575 ? 0.3545 0.4639 0.4092 -0.0698 -0.1852 0.0289  567 VAL D CA  
18514 C C   . VAL D 575 ? 0.3500 0.4361 0.3793 -0.0773 -0.1904 0.0250  567 VAL D C   
18515 O O   . VAL D 575 ? 0.3888 0.4741 0.4186 -0.0848 -0.1978 0.0264  567 VAL D O   
18516 C CB  . VAL D 575 ? 0.3563 0.4722 0.4215 -0.0714 -0.1781 0.0287  567 VAL D CB  
18517 C CG1 . VAL D 575 ? 0.3906 0.5074 0.4604 -0.0824 -0.1817 0.0299  567 VAL D CG1 
18518 C CG2 . VAL D 575 ? 0.3186 0.4579 0.4087 -0.0635 -0.1725 0.0326  567 VAL D CG2 
18519 N N   . LEU D 576 ? 0.3337 0.4003 0.3403 -0.0749 -0.1864 0.0199  568 LEU D N   
18520 C CA  . LEU D 576 ? 0.3479 0.3912 0.3282 -0.0803 -0.1900 0.0155  568 LEU D CA  
18521 C C   . LEU D 576 ? 0.3644 0.4046 0.3374 -0.0811 -0.1979 0.0171  568 LEU D C   
18522 O O   . LEU D 576 ? 0.3848 0.4132 0.3456 -0.0883 -0.2044 0.0159  568 LEU D O   
18523 C CB  . LEU D 576 ? 0.3872 0.4127 0.3464 -0.0758 -0.1829 0.0101  568 LEU D CB  
18524 C CG  . LEU D 576 ? 0.3552 0.3776 0.3160 -0.0767 -0.1761 0.0073  568 LEU D CG  
18525 C CD1 . LEU D 576 ? 0.3326 0.3465 0.2824 -0.0690 -0.1681 0.0041  568 LEU D CD1 
18526 C CD2 . LEU D 576 ? 0.3541 0.3597 0.3008 -0.0850 -0.1785 0.0034  568 LEU D CD2 
18527 N N   . ALA D 577 ? 0.3573 0.4066 0.3366 -0.0739 -0.1979 0.0200  569 ALA D N   
18528 C CA  . ALA D 577 ? 0.3732 0.4202 0.3465 -0.0747 -0.2058 0.0221  569 ALA D CA  
18529 C C   . ALA D 577 ? 0.3951 0.4529 0.3835 -0.0817 -0.2144 0.0260  569 ALA D C   
18530 O O   . ALA D 577 ? 0.4031 0.4506 0.3792 -0.0874 -0.2223 0.0259  569 ALA D O   
18531 C CB  . ALA D 577 ? 0.3630 0.4198 0.3441 -0.0655 -0.2043 0.0252  569 ALA D CB  
18532 N N   . GLY D 578 ? 0.3667 0.4452 0.3814 -0.0816 -0.2128 0.0294  570 GLY D N   
18533 C CA  . GLY D 578 ? 0.3738 0.4647 0.4053 -0.0886 -0.2201 0.0336  570 GLY D CA  
18534 C C   . GLY D 578 ? 0.4613 0.5387 0.4818 -0.0992 -0.2238 0.0315  570 GLY D C   
18535 O O   . GLY D 578 ? 0.4900 0.5736 0.5199 -0.1062 -0.2315 0.0350  570 GLY D O   
18536 N N   . GLN D 579 ? 0.4512 0.5102 0.4523 -0.1004 -0.2186 0.0260  571 GLN D N   
18537 C CA  . GLN D 579 ? 0.4772 0.5196 0.4643 -0.1096 -0.2220 0.0232  571 GLN D CA  
18538 C C   . GLN D 579 ? 0.5090 0.5256 0.4649 -0.1108 -0.2253 0.0183  571 GLN D C   
18539 O O   . GLN D 579 ? 0.4895 0.4878 0.4287 -0.1166 -0.2265 0.0144  571 GLN D O   
18540 C CB  . GLN D 579 ? 0.4376 0.4773 0.4259 -0.1105 -0.2140 0.0205  571 GLN D CB  
18541 C CG  . GLN D 579 ? 0.4198 0.4839 0.4379 -0.1118 -0.2115 0.0257  571 GLN D CG  
18542 C CD  . GLN D 579 ? 0.4767 0.5385 0.4960 -0.1122 -0.2032 0.0234  571 GLN D CD  
18543 O OE1 . GLN D 579 ? 0.4828 0.5231 0.4807 -0.1134 -0.2008 0.0178  571 GLN D OE1 
18544 N NE2 . GLN D 579 ? 0.4936 0.5774 0.5377 -0.1109 -0.1986 0.0277  571 GLN D NE2 
18545 N N   . GLY D 580 ? 0.4357 0.4500 0.3830 -0.1054 -0.2266 0.0185  572 GLY D N   
18546 C CA  . GLY D 580 ? 0.4686 0.4597 0.3865 -0.1065 -0.2294 0.0144  572 GLY D CA  
18547 C C   . GLY D 580 ? 0.4725 0.4463 0.3688 -0.1020 -0.2203 0.0080  572 GLY D C   
18548 O O   . GLY D 580 ? 0.4787 0.4310 0.3493 -0.1041 -0.2212 0.0033  572 GLY D O   
18549 N N   . ILE D 581 ? 0.4569 0.4396 0.3627 -0.0954 -0.2114 0.0076  573 ILE D N   
18550 C CA  . ILE D 581 ? 0.4311 0.3993 0.3192 -0.0909 -0.2022 0.0019  573 ILE D CA  
18551 C C   . ILE D 581 ? 0.4160 0.3919 0.3070 -0.0819 -0.1971 0.0037  573 ILE D C   
18552 O O   . ILE D 581 ? 0.3936 0.3860 0.3046 -0.0774 -0.1931 0.0065  573 ILE D O   
18553 C CB  . ILE D 581 ? 0.4190 0.3877 0.3144 -0.0922 -0.1963 -0.0004 573 ILE D CB  
18554 C CG1 . ILE D 581 ? 0.4839 0.4459 0.3785 -0.1015 -0.2021 -0.0010 573 ILE D CG1 
18555 C CG2 . ILE D 581 ? 0.4914 0.4438 0.3676 -0.0874 -0.1873 -0.0065 573 ILE D CG2 
18556 C CD1 . ILE D 581 ? 0.4917 0.4553 0.3954 -0.1037 -0.1972 -0.0022 573 ILE D CD1 
18557 N N   . ALA D 582 ? 0.4294 0.3930 0.3001 -0.0793 -0.1971 0.0022  574 ALA D N   
18558 C CA  . ALA D 582 ? 0.4183 0.3868 0.2893 -0.0714 -0.1926 0.0041  574 ALA D CA  
18559 C C   . ALA D 582 ? 0.4084 0.3689 0.2701 -0.0665 -0.1821 -0.0000 574 ALA D C   
18560 O O   . ALA D 582 ? 0.4662 0.4084 0.3056 -0.0676 -0.1786 -0.0054 574 ALA D O   
18561 C CB  . ALA D 582 ? 0.4381 0.3966 0.2908 -0.0713 -0.1967 0.0048  574 ALA D CB  
18562 N N   . VAL D 583 ? 0.4050 0.3788 0.2835 -0.0607 -0.1771 0.0023  575 VAL D N   
18563 C CA  . VAL D 583 ? 0.3920 0.3589 0.2625 -0.0555 -0.1678 -0.0008 575 VAL D CA  
18564 C C   . VAL D 583 ? 0.4321 0.4070 0.3085 -0.0479 -0.1648 0.0031  575 VAL D C   
18565 O O   . VAL D 583 ? 0.4082 0.3976 0.3012 -0.0457 -0.1689 0.0081  575 VAL D O   
18566 C CB  . VAL D 583 ? 0.3612 0.3327 0.2443 -0.0562 -0.1635 -0.0025 575 VAL D CB  
18567 C CG1 . VAL D 583 ? 0.4221 0.3867 0.3020 -0.0643 -0.1673 -0.0054 575 VAL D CG1 
18568 C CG2 . VAL D 583 ? 0.3608 0.3542 0.2715 -0.0526 -0.1637 0.0027  575 VAL D CG2 
18569 N N   . ARG D 584 ? 0.3940 0.3586 0.2562 -0.0436 -0.1574 0.0007  576 ARG D N   
18570 C CA  . ARG D 584 ? 0.3688 0.3385 0.2350 -0.0363 -0.1535 0.0041  576 ARG D CA  
18571 C C   . ARG D 584 ? 0.3615 0.3375 0.2410 -0.0320 -0.1475 0.0039  576 ARG D C   
18572 O O   . ARG D 584 ? 0.3962 0.3657 0.2718 -0.0340 -0.1441 -0.0004 576 ARG D O   
18573 C CB  . ARG D 584 ? 0.4222 0.3765 0.2636 -0.0349 -0.1492 0.0024  576 ARG D CB  
18574 C CG  . ARG D 584 ? 0.4988 0.4519 0.3386 -0.0283 -0.1414 0.0033  576 ARG D CG  
18575 C CD  . ARG D 584 ? 0.4787 0.4154 0.2925 -0.0281 -0.1353 0.0002  576 ARG D CD  
18576 N NE  . ARG D 584 ? 0.4634 0.3957 0.2640 -0.0298 -0.1387 0.0024  576 ARG D NE  
18577 C CZ  . ARG D 584 ? 0.4492 0.3714 0.2303 -0.0284 -0.1335 0.0023  576 ARG D CZ  
18578 N NH1 . ARG D 584 ? 0.4285 0.3447 0.2018 -0.0250 -0.1244 0.0001  576 ARG D NH1 
18579 N NH2 . ARG D 584 ? 0.4500 0.3687 0.2198 -0.0304 -0.1372 0.0048  576 ARG D NH2 
18580 N N   . VAL D 585 ? 0.3145 0.3024 0.2097 -0.0258 -0.1466 0.0083  577 VAL D N   
18581 C CA  . VAL D 585 ? 0.2953 0.2888 0.2034 -0.0204 -0.1392 0.0082  577 VAL D CA  
18582 C C   . VAL D 585 ? 0.3136 0.3008 0.2137 -0.0141 -0.1324 0.0092  577 VAL D C   
18583 O O   . VAL D 585 ? 0.3121 0.3008 0.2103 -0.0116 -0.1369 0.0134  577 VAL D O   
18584 C CB  . VAL D 585 ? 0.3173 0.3296 0.2513 -0.0175 -0.1420 0.0121  577 VAL D CB  
18585 C CG1 . VAL D 585 ? 0.2882 0.3045 0.2340 -0.0113 -0.1312 0.0113  577 VAL D CG1 
18586 C CG2 . VAL D 585 ? 0.3182 0.3385 0.2619 -0.0244 -0.1483 0.0119  577 VAL D CG2 
18587 N N   . VAL D 586 ? 0.2873 0.2674 0.1832 -0.0120 -0.1220 0.0058  578 VAL D N   
18588 C CA  . VAL D 586 ? 0.2825 0.2581 0.1741 -0.0064 -0.1145 0.0070  578 VAL D CA  
18589 C C   . VAL D 586 ? 0.2787 0.2629 0.1893 -0.0010 -0.1088 0.0081  578 VAL D C   
18590 O O   . VAL D 586 ? 0.3068 0.2931 0.2253 -0.0018 -0.1047 0.0052  578 VAL D O   
18591 C CB  . VAL D 586 ? 0.2925 0.2541 0.1658 -0.0076 -0.1069 0.0026  578 VAL D CB  
18592 C CG1 . VAL D 586 ? 0.2985 0.2583 0.1738 -0.0020 -0.0974 0.0037  578 VAL D CG1 
18593 C CG2 . VAL D 586 ? 0.3145 0.2663 0.1658 -0.0115 -0.1117 0.0023  578 VAL D CG2 
18594 N N   . SER D 587 ? 0.2868 0.2751 0.2038 0.0044  -0.1091 0.0123  579 SER D N   
18595 C CA  . SER D 587 ? 0.2415 0.2341 0.1719 0.0100  -0.1029 0.0129  579 SER D CA  
18596 C C   . SER D 587 ? 0.2722 0.2548 0.1930 0.0118  -0.0947 0.0120  579 SER D C   
18597 O O   . SER D 587 ? 0.2549 0.2312 0.1635 0.0117  -0.0951 0.0141  579 SER D O   
18598 C CB  . SER D 587 ? 0.2336 0.2342 0.1756 0.0154  -0.1075 0.0175  579 SER D CB  
18599 O OG  . SER D 587 ? 0.2445 0.2475 0.1974 0.0208  -0.1016 0.0175  579 SER D OG  
18600 N N   . MET D 588 ? 0.2367 0.2182 0.1632 0.0132  -0.0874 0.0094  580 MET D N   
18601 C CA  . MET D 588 ? 0.2772 0.2506 0.1976 0.0150  -0.0796 0.0087  580 MET D CA  
18602 C C   . MET D 588 ? 0.2522 0.2286 0.1853 0.0201  -0.0760 0.0105  580 MET D C   
18603 O O   . MET D 588 ? 0.2079 0.1829 0.1457 0.0207  -0.0706 0.0080  580 MET D O   
18604 C CB  . MET D 588 ? 0.2848 0.2514 0.1977 0.0119  -0.0744 0.0036  580 MET D CB  
18605 C CG  . MET D 588 ? 0.2876 0.2465 0.1934 0.0138  -0.0665 0.0031  580 MET D CG  
18606 S SD  . MET D 588 ? 0.2784 0.2274 0.1724 0.0110  -0.0609 -0.0033 580 MET D SD  
18607 C CE  . MET D 588 ? 0.2947 0.2379 0.1684 0.0069  -0.0653 -0.0042 580 MET D CE  
18608 N N   . PRO D 589 ? 0.2606 0.2398 0.1983 0.0239  -0.0794 0.0148  581 PRO D N   
18609 C CA  . PRO D 589 ? 0.2610 0.2413 0.2091 0.0288  -0.0768 0.0161  581 PRO D CA  
18610 C C   . PRO D 589 ? 0.2891 0.2624 0.2348 0.0295  -0.0698 0.0158  581 PRO D C   
18611 O O   . PRO D 589 ? 0.2093 0.1825 0.1630 0.0323  -0.0671 0.0155  581 PRO D O   
18612 C CB  . PRO D 589 ? 0.2515 0.2332 0.2014 0.0323  -0.0827 0.0208  581 PRO D CB  
18613 C CG  . PRO D 589 ? 0.2760 0.2553 0.2139 0.0288  -0.0870 0.0226  581 PRO D CG  
18614 C CD  . PRO D 589 ? 0.3052 0.2859 0.2387 0.0239  -0.0867 0.0185  581 PRO D CD  
18615 N N   . SER D 590 ? 0.2292 0.1968 0.1641 0.0270  -0.0666 0.0158  582 SER D N   
18616 C CA  . SER D 590 ? 0.2138 0.1764 0.1484 0.0278  -0.0596 0.0156  582 SER D CA  
18617 C C   . SER D 590 ? 0.2609 0.2191 0.1843 0.0247  -0.0551 0.0125  582 SER D C   
18618 O O   . SER D 590 ? 0.2866 0.2427 0.1992 0.0230  -0.0555 0.0142  582 SER D O   
18619 C CB  . SER D 590 ? 0.2102 0.1707 0.1456 0.0300  -0.0597 0.0209  582 SER D CB  
18620 O OG  . SER D 590 ? 0.2429 0.2000 0.1798 0.0304  -0.0531 0.0211  582 SER D OG  
18621 N N   . THR D 591 ? 0.2602 0.2163 0.1854 0.0240  -0.0508 0.0081  583 THR D N   
18622 C CA  . THR D 591 ? 0.2593 0.2096 0.1742 0.0223  -0.0455 0.0046  583 THR D CA  
18623 C C   . THR D 591 ? 0.2802 0.2285 0.1930 0.0242  -0.0397 0.0075  583 THR D C   
18624 O O   . THR D 591 ? 0.2799 0.2250 0.1811 0.0232  -0.0362 0.0068  583 THR D O   
18625 C CB  . THR D 591 ? 0.2664 0.2139 0.1852 0.0219  -0.0426 -0.0003 583 THR D CB  
18626 O OG1 . THR D 591 ? 0.2660 0.2141 0.1961 0.0249  -0.0395 0.0013  583 THR D OG1 
18627 C CG2 . THR D 591 ? 0.2150 0.1656 0.1371 0.0192  -0.0481 -0.0024 583 THR D CG2 
18628 N N   . SER D 592 ? 0.2569 0.2070 0.1807 0.0269  -0.0386 0.0110  584 SER D N   
18629 C CA  . SER D 592 ? 0.3330 0.2827 0.2581 0.0283  -0.0335 0.0147  584 SER D CA  
18630 C C   . SER D 592 ? 0.2953 0.2456 0.2106 0.0267  -0.0344 0.0188  584 SER D C   
18631 O O   . SER D 592 ? 0.3132 0.2622 0.2207 0.0262  -0.0285 0.0191  584 SER D O   
18632 C CB  . SER D 592 ? 0.2685 0.2196 0.2066 0.0305  -0.0352 0.0185  584 SER D CB  
18633 O OG  . SER D 592 ? 0.2659 0.2168 0.2114 0.0314  -0.0372 0.0153  584 SER D OG  
18634 N N   . VAL D 593 ? 0.2500 0.2020 0.1651 0.0262  -0.0416 0.0220  585 VAL D N   
18635 C CA  . VAL D 593 ? 0.2529 0.2047 0.1589 0.0245  -0.0439 0.0269  585 VAL D CA  
18636 C C   . VAL D 593 ? 0.2930 0.2424 0.1832 0.0218  -0.0431 0.0238  585 VAL D C   
18637 O O   . VAL D 593 ? 0.2585 0.2062 0.1379 0.0203  -0.0395 0.0262  585 VAL D O   
18638 C CB  . VAL D 593 ? 0.2281 0.1814 0.1389 0.0254  -0.0528 0.0306  585 VAL D CB  
18639 C CG1 . VAL D 593 ? 0.2404 0.1924 0.1405 0.0232  -0.0566 0.0358  585 VAL D CG1 
18640 C CG2 . VAL D 593 ? 0.2195 0.1730 0.1432 0.0282  -0.0533 0.0337  585 VAL D CG2 
18641 N N   . PHE D 594 ? 0.2676 0.2163 0.1555 0.0207  -0.0465 0.0186  586 PHE D N   
18642 C CA  . PHE D 594 ? 0.2719 0.2166 0.1435 0.0177  -0.0467 0.0152  586 PHE D CA  
18643 C C   . PHE D 594 ? 0.3004 0.2407 0.1629 0.0180  -0.0372 0.0123  586 PHE D C   
18644 O O   . PHE D 594 ? 0.3309 0.2674 0.1773 0.0162  -0.0352 0.0122  586 PHE D O   
18645 C CB  . PHE D 594 ? 0.2769 0.2215 0.1497 0.0160  -0.0518 0.0101  586 PHE D CB  
18646 C CG  . PHE D 594 ? 0.3669 0.3058 0.2221 0.0124  -0.0536 0.0064  586 PHE D CG  
18647 C CD1 . PHE D 594 ? 0.3197 0.2578 0.1638 0.0099  -0.0596 0.0096  586 PHE D CD1 
18648 C CD2 . PHE D 594 ? 0.4395 0.3725 0.2883 0.0115  -0.0497 -0.0001 586 PHE D CD2 
18649 C CE1 . PHE D 594 ? 0.3105 0.2420 0.1369 0.0063  -0.0620 0.0062  586 PHE D CE1 
18650 C CE2 . PHE D 594 ? 0.4478 0.3737 0.2788 0.0081  -0.0519 -0.0037 586 PHE D CE2 
18651 C CZ  . PHE D 594 ? 0.3175 0.2427 0.1369 0.0053  -0.0582 -0.0006 586 PHE D CZ  
18652 N N   . ASP D 595 ? 0.2945 0.2351 0.1670 0.0207  -0.0310 0.0101  587 ASP D N   
18653 C CA  . ASP D 595 ? 0.3173 0.2542 0.1831 0.0220  -0.0217 0.0067  587 ASP D CA  
18654 C C   . ASP D 595 ? 0.3711 0.3098 0.2311 0.0224  -0.0156 0.0116  587 ASP D C   
18655 O O   . ASP D 595 ? 0.4348 0.3701 0.2829 0.0230  -0.0084 0.0089  587 ASP D O   
18656 C CB  . ASP D 595 ? 0.3452 0.2826 0.2251 0.0250  -0.0175 0.0042  587 ASP D CB  
18657 C CG  . ASP D 595 ? 0.3908 0.3243 0.2715 0.0241  -0.0210 -0.0020 587 ASP D CG  
18658 O OD1 . ASP D 595 ? 0.4388 0.3686 0.3080 0.0211  -0.0254 -0.0051 587 ASP D OD1 
18659 O OD2 . ASP D 595 ? 0.3978 0.3315 0.2903 0.0259  -0.0196 -0.0035 587 ASP D OD2 
18660 N N   . ARG D 596 ? 0.3276 0.2712 0.1950 0.0221  -0.0183 0.0190  588 ARG D N   
18661 C CA  . ARG D 596 ? 0.3513 0.2973 0.2138 0.0215  -0.0126 0.0247  588 ARG D CA  
18662 C C   . ARG D 596 ? 0.3765 0.3205 0.2233 0.0180  -0.0172 0.0284  588 ARG D C   
18663 O O   . ARG D 596 ? 0.3992 0.3455 0.2422 0.0167  -0.0138 0.0346  588 ARG D O   
18664 C CB  . ARG D 596 ? 0.4515 0.4031 0.3312 0.0227  -0.0121 0.0313  588 ARG D CB  
18665 C CG  . ARG D 596 ? 0.4710 0.4234 0.3595 0.0220  -0.0221 0.0355  588 ARG D CG  
18666 C CD  . ARG D 596 ? 0.4481 0.4041 0.3519 0.0230  -0.0211 0.0416  588 ARG D CD  
18667 N NE  . ARG D 596 ? 0.4113 0.3662 0.3224 0.0230  -0.0305 0.0452  588 ARG D NE  
18668 C CZ  . ARG D 596 ? 0.3321 0.2865 0.2549 0.0254  -0.0340 0.0429  588 ARG D CZ  
18669 N NH1 . ARG D 596 ? 0.3100 0.2646 0.2386 0.0273  -0.0295 0.0377  588 ARG D NH1 
18670 N NH2 . ARG D 596 ? 0.4082 0.3610 0.3359 0.0261  -0.0421 0.0458  588 ARG D NH2 
18671 N N   . GLN D 597 ? 0.3076 0.2476 0.1453 0.0160  -0.0248 0.0252  589 GLN D N   
18672 C CA  . GLN D 597 ? 0.3560 0.2932 0.1774 0.0126  -0.0296 0.0285  589 GLN D CA  
18673 C C   . GLN D 597 ? 0.4025 0.3345 0.2034 0.0115  -0.0220 0.0252  589 GLN D C   
18674 O O   . GLN D 597 ? 0.4244 0.3535 0.2226 0.0135  -0.0156 0.0185  589 GLN D O   
18675 C CB  . GLN D 597 ? 0.3488 0.2841 0.1684 0.0108  -0.0410 0.0265  589 GLN D CB  
18676 C CG  . GLN D 597 ? 0.2986 0.2389 0.1373 0.0127  -0.0481 0.0290  589 GLN D CG  
18677 C CD  . GLN D 597 ? 0.3424 0.2852 0.1871 0.0130  -0.0501 0.0374  589 GLN D CD  
18678 O OE1 . GLN D 597 ? 0.3736 0.3143 0.2077 0.0105  -0.0541 0.0424  589 GLN D OE1 
18679 N NE2 . GLN D 597 ? 0.2798 0.2259 0.1407 0.0157  -0.0478 0.0391  589 GLN D NE2 
18680 N N   . ASP D 598 ? 0.3881 0.3180 0.1735 0.0084  -0.0230 0.0301  590 ASP D N   
18681 C CA  . ASP D 598 ? 0.4608 0.3852 0.2241 0.0074  -0.0155 0.0274  590 ASP D CA  
18682 C C   . ASP D 598 ? 0.4814 0.3973 0.2317 0.0070  -0.0185 0.0183  590 ASP D C   
18683 O O   . ASP D 598 ? 0.3904 0.3052 0.1460 0.0057  -0.0285 0.0160  590 ASP D O   
18684 C CB  . ASP D 598 ? 0.5244 0.4469 0.2715 0.0034  -0.0181 0.0345  590 ASP D CB  
18685 C CG  . ASP D 598 ? 0.5742 0.4927 0.3154 -0.0000 -0.0324 0.0360  590 ASP D CG  
18686 O OD1 . ASP D 598 ? 0.5570 0.4680 0.2812 -0.0021 -0.0363 0.0310  590 ASP D OD1 
18687 O OD2 . ASP D 598 ? 0.5258 0.4485 0.2796 -0.0006 -0.0400 0.0424  590 ASP D OD2 
18688 N N   . ALA D 599 ? 0.4837 0.3937 0.2173 0.0081  -0.0094 0.0131  591 ALA D N   
18689 C CA  . ALA D 599 ? 0.5364 0.4367 0.2579 0.0081  -0.0111 0.0037  591 ALA D CA  
18690 C C   . ALA D 599 ? 0.5008 0.3941 0.2067 0.0030  -0.0234 0.0033  591 ALA D C   
18691 O O   . ALA D 599 ? 0.5191 0.4077 0.2250 0.0016  -0.0308 -0.0022 591 ALA D O   
18692 C CB  . ALA D 599 ? 0.5183 0.4122 0.2226 0.0110  0.0014  -0.0018 591 ALA D CB  
18693 N N   . ALA D 600 ? 0.5148 0.4074 0.2075 -0.0003 -0.0263 0.0096  592 ALA D N   
18694 C CA  . ALA D 600 ? 0.5293 0.4152 0.2068 -0.0052 -0.0388 0.0100  592 ALA D CA  
18695 C C   . ALA D 600 ? 0.5054 0.3974 0.2031 -0.0063 -0.0513 0.0119  592 ALA D C   
18696 O O   . ALA D 600 ? 0.4856 0.3732 0.1789 -0.0092 -0.0610 0.0083  592 ALA D O   
18697 C CB  . ALA D 600 ? 0.5825 0.4665 0.2428 -0.0084 -0.0395 0.0173  592 ALA D CB  
18698 N N   . TYR D 601 ? 0.4228 0.3250 0.1431 -0.0040 -0.0512 0.0175  593 TYR D N   
18699 C CA  . TYR D 601 ? 0.3964 0.3049 0.1362 -0.0039 -0.0619 0.0192  593 TYR D CA  
18700 C C   . TYR D 601 ? 0.4275 0.3366 0.1784 -0.0026 -0.0621 0.0118  593 TYR D C   
18701 O O   . TYR D 601 ? 0.4117 0.3218 0.1675 -0.0047 -0.0720 0.0104  593 TYR D O   
18702 C CB  . TYR D 601 ? 0.4558 0.3731 0.2152 -0.0012 -0.0612 0.0261  593 TYR D CB  
18703 C CG  . TYR D 601 ? 0.4533 0.3767 0.2316 -0.0003 -0.0713 0.0273  593 TYR D CG  
18704 C CD1 . TYR D 601 ? 0.4327 0.3561 0.2080 -0.0026 -0.0832 0.0311  593 TYR D CD1 
18705 C CD2 . TYR D 601 ? 0.4243 0.3536 0.2231 0.0032  -0.0689 0.0246  593 TYR D CD2 
18706 C CE1 . TYR D 601 ? 0.4006 0.3307 0.1940 -0.0009 -0.0917 0.0321  593 TYR D CE1 
18707 C CE2 . TYR D 601 ? 0.3251 0.2604 0.1403 0.0044  -0.0771 0.0255  593 TYR D CE2 
18708 C CZ  . TYR D 601 ? 0.3556 0.2918 0.1684 0.0026  -0.0882 0.0292  593 TYR D CZ  
18709 O OH  . TYR D 601 ? 0.3261 0.2693 0.1560 0.0046  -0.0958 0.0301  593 TYR D OH  
18710 N N   . GLN D 602 ? 0.3786 0.2877 0.1351 0.0007  -0.0515 0.0077  594 GLN D N   
18711 C CA  . GLN D 602 ? 0.3759 0.2842 0.1416 0.0016  -0.0516 0.0010  594 GLN D CA  
18712 C C   . GLN D 602 ? 0.4355 0.3345 0.1843 -0.0025 -0.0580 -0.0047 594 GLN D C   
18713 O O   . GLN D 602 ? 0.4145 0.3151 0.1719 -0.0045 -0.0657 -0.0069 594 GLN D O   
18714 C CB  . GLN D 602 ? 0.4541 0.3614 0.2238 0.0058  -0.0393 -0.0027 594 GLN D CB  
18715 C CG  . GLN D 602 ? 0.4730 0.3892 0.2602 0.0094  -0.0335 0.0031  594 GLN D CG  
18716 C CD  . GLN D 602 ? 0.5213 0.4385 0.3206 0.0134  -0.0250 -0.0007 594 GLN D CD  
18717 O OE1 . GLN D 602 ? 0.6039 0.5177 0.4064 0.0136  -0.0263 -0.0066 594 GLN D OE1 
18718 N NE2 . GLN D 602 ? 0.4876 0.4097 0.2943 0.0164  -0.0167 0.0031  594 GLN D NE2 
18719 N N   . ALA D 603 ? 0.4626 0.3519 0.1868 -0.0040 -0.0551 -0.0067 595 ALA D N   
18720 C CA  . ALA D 603 ? 0.5472 0.4254 0.2518 -0.0084 -0.0620 -0.0120 595 ALA D CA  
18721 C C   . ALA D 603 ? 0.5283 0.4094 0.2342 -0.0132 -0.0766 -0.0078 595 ALA D C   
18722 O O   . ALA D 603 ? 0.5174 0.3941 0.2199 -0.0171 -0.0853 -0.0115 595 ALA D O   
18723 C CB  . ALA D 603 ? 0.5867 0.4534 0.2627 -0.0086 -0.0553 -0.0145 595 ALA D CB  
18724 N N   . ALA D 604 ? 0.4834 0.3715 0.1942 -0.0131 -0.0800 0.0000  596 ALA D N   
18725 C CA  . ALA D 604 ? 0.4490 0.3407 0.1634 -0.0167 -0.0941 0.0043  596 ALA D CA  
18726 C C   . ALA D 604 ? 0.4361 0.3376 0.1756 -0.0162 -0.1000 0.0036  596 ALA D C   
18727 O O   . ALA D 604 ? 0.4205 0.3247 0.1648 -0.0197 -0.1101 0.0037  596 ALA D O   
18728 C CB  . ALA D 604 ? 0.5092 0.4066 0.2270 -0.0158 -0.0959 0.0129  596 ALA D CB  
18729 N N   . VAL D 605 ? 0.4551 0.3636 0.2138 -0.0118 -0.0924 0.0030  597 VAL D N   
18730 C CA  . VAL D 605 ? 0.4199 0.3382 0.2021 -0.0110 -0.0967 0.0028  597 VAL D CA  
18731 C C   . VAL D 605 ? 0.3699 0.2833 0.1506 -0.0136 -0.0966 -0.0043 597 VAL D C   
18732 O O   . VAL D 605 ? 0.3661 0.2842 0.1562 -0.0166 -0.1050 -0.0048 597 VAL D O   
18733 C CB  . VAL D 605 ? 0.4189 0.3455 0.2205 -0.0054 -0.0894 0.0056  597 VAL D CB  
18734 C CG1 . VAL D 605 ? 0.3246 0.2603 0.1486 -0.0042 -0.0918 0.0046  597 VAL D CG1 
18735 C CG2 . VAL D 605 ? 0.3598 0.2903 0.1634 -0.0036 -0.0919 0.0130  597 VAL D CG2 
18736 N N   . LEU D 606 ? 0.4186 0.3226 0.1876 -0.0124 -0.0873 -0.0097 598 LEU D N   
18737 C CA  . LEU D 606 ? 0.3832 0.2801 0.1493 -0.0144 -0.0864 -0.0168 598 LEU D CA  
18738 C C   . LEU D 606 ? 0.4262 0.3072 0.1638 -0.0166 -0.0849 -0.0219 598 LEU D C   
18739 O O   . LEU D 606 ? 0.4331 0.3069 0.1616 -0.0130 -0.0743 -0.0258 598 LEU D O   
18740 C CB  . LEU D 606 ? 0.3670 0.2661 0.1469 -0.0097 -0.0763 -0.0191 598 LEU D CB  
18741 C CG  . LEU D 606 ? 0.4069 0.3197 0.2128 -0.0069 -0.0761 -0.0148 598 LEU D CG  
18742 C CD1 . LEU D 606 ? 0.3287 0.2409 0.1445 -0.0029 -0.0667 -0.0175 598 LEU D CD1 
18743 C CD2 . LEU D 606 ? 0.4560 0.3759 0.2740 -0.0107 -0.0863 -0.0137 598 LEU D CD2 
18744 N N   . PRO D 607 ? 0.4679 0.3431 0.1907 -0.0221 -0.0953 -0.0221 599 PRO D N   
18745 C CA  . PRO D 607 ? 0.4738 0.3336 0.1687 -0.0240 -0.0936 -0.0269 599 PRO D CA  
18746 C C   . PRO D 607 ? 0.5438 0.3913 0.2302 -0.0233 -0.0881 -0.0354 599 PRO D C   
18747 O O   . PRO D 607 ? 0.4645 0.3128 0.1629 -0.0251 -0.0918 -0.0380 599 PRO D O   
18748 C CB  . PRO D 607 ? 0.5410 0.4028 0.2365 -0.0299 -0.1051 -0.0246 599 PRO D CB  
18749 C CG  . PRO D 607 ? 0.5496 0.4272 0.2670 -0.0300 -0.1122 -0.0173 599 PRO D CG  
18750 C CD  . PRO D 607 ? 0.5210 0.4049 0.2548 -0.0264 -0.1084 -0.0176 599 PRO D CD  
18751 N N   . GLU D 608 ? 0.5401 0.3764 0.2063 -0.0206 -0.0791 -0.0397 600 GLU D N   
18752 C CA  . GLU D 608 ? 0.5783 0.4019 0.2358 -0.0190 -0.0736 -0.0481 600 GLU D CA  
18753 C C   . GLU D 608 ? 0.6531 0.4701 0.3078 -0.0253 -0.0835 -0.0511 600 GLU D C   
18754 O O   . GLU D 608 ? 0.7147 0.5314 0.3622 -0.0297 -0.0908 -0.0487 600 GLU D O   
18755 C CB  . GLU D 608 ? 0.5932 0.4077 0.2302 -0.0142 -0.0615 -0.0516 600 GLU D CB  
18756 N N   . GLY D 609 ? 0.6595 0.4712 0.3206 -0.0260 -0.0843 -0.0560 601 GLY D N   
18757 C CA  . GLY D 609 ? 0.7369 0.5417 0.3962 -0.0322 -0.0935 -0.0586 601 GLY D CA  
18758 C C   . GLY D 609 ? 0.6888 0.5058 0.3682 -0.0384 -0.1053 -0.0533 601 GLY D C   
18759 O O   . GLY D 609 ? 0.7209 0.5336 0.4007 -0.0442 -0.1136 -0.0545 601 GLY D O   
18760 N N   . LEU D 610 ? 0.5545 0.3868 0.2509 -0.0371 -0.1063 -0.0474 602 LEU D N   
18761 C CA  . LEU D 610 ? 0.5564 0.4026 0.2743 -0.0418 -0.1163 -0.0422 602 LEU D CA  
18762 C C   . LEU D 610 ? 0.5082 0.3589 0.2430 -0.0409 -0.1143 -0.0433 602 LEU D C   
18763 O O   . LEU D 610 ? 0.5627 0.4177 0.3032 -0.0354 -0.1071 -0.0425 602 LEU D O   
18764 C CB  . LEU D 610 ? 0.5703 0.4309 0.2975 -0.0406 -0.1194 -0.0347 602 LEU D CB  
18765 C CG  . LEU D 610 ? 0.5741 0.4506 0.3236 -0.0446 -0.1297 -0.0288 602 LEU D CG  
18766 C CD1 . LEU D 610 ? 0.6052 0.4780 0.3501 -0.0513 -0.1390 -0.0290 602 LEU D CD1 
18767 C CD2 . LEU D 610 ? 0.5375 0.4272 0.2966 -0.0412 -0.1306 -0.0219 602 LEU D CD2 
18768 N N   . PRO D 611 ? 0.4764 0.3264 0.2198 -0.0463 -0.1201 -0.0445 603 PRO D N   
18769 C CA  . PRO D 611 ? 0.4831 0.3366 0.2418 -0.0460 -0.1180 -0.0454 603 PRO D CA  
18770 C C   . PRO D 611 ? 0.4326 0.3056 0.2141 -0.0431 -0.1171 -0.0390 603 PRO D C   
18771 O O   . PRO D 611 ? 0.4181 0.3033 0.2079 -0.0449 -0.1240 -0.0335 603 PRO D O   
18772 C CB  . PRO D 611 ? 0.5503 0.4027 0.3156 -0.0538 -0.1263 -0.0456 603 PRO D CB  
18773 C CG  . PRO D 611 ? 0.5875 0.4282 0.3339 -0.0567 -0.1301 -0.0479 603 PRO D CG  
18774 C CD  . PRO D 611 ? 0.4926 0.3380 0.2317 -0.0533 -0.1291 -0.0449 603 PRO D CD  
18775 N N   . ARG D 612 ? 0.4180 0.2950 0.2123 -0.0377 -0.1073 -0.0393 604 ARG D N   
18776 C CA  . ARG D 612 ? 0.3612 0.2559 0.1779 -0.0331 -0.1029 -0.0335 604 ARG D CA  
18777 C C   . ARG D 612 ? 0.4250 0.3277 0.2618 -0.0350 -0.1029 -0.0323 604 ARG D C   
18778 O O   . ARG D 612 ? 0.4175 0.3103 0.2514 -0.0361 -0.1002 -0.0365 604 ARG D O   
18779 C CB  . ARG D 612 ? 0.3543 0.2473 0.1688 -0.0249 -0.0912 -0.0339 604 ARG D CB  
18780 C CG  . ARG D 612 ? 0.3705 0.2560 0.1646 -0.0229 -0.0894 -0.0346 604 ARG D CG  
18781 C CD  . ARG D 612 ? 0.4163 0.2978 0.2066 -0.0158 -0.0770 -0.0361 604 ARG D CD  
18782 N NE  . ARG D 612 ? 0.4487 0.3240 0.2194 -0.0142 -0.0745 -0.0363 604 ARG D NE  
18783 C CZ  . ARG D 612 ? 0.5190 0.3888 0.2808 -0.0089 -0.0640 -0.0383 604 ARG D CZ  
18784 N NH1 . ARG D 612 ? 0.4861 0.3554 0.2575 -0.0044 -0.0556 -0.0404 604 ARG D NH1 
18785 N NH2 . ARG D 612 ? 0.5299 0.3951 0.2735 -0.0082 -0.0618 -0.0378 604 ARG D NH2 
18786 N N   . ILE D 613 ? 0.3823 0.3025 0.2390 -0.0350 -0.1059 -0.0265 605 ILE D N   
18787 C CA  . ILE D 613 ? 0.3362 0.2664 0.2127 -0.0360 -0.1046 -0.0245 605 ILE D CA  
18788 C C   . ILE D 613 ? 0.3526 0.2961 0.2446 -0.0290 -0.0986 -0.0202 605 ILE D C   
18789 O O   . ILE D 613 ? 0.3273 0.2809 0.2246 -0.0271 -0.1019 -0.0161 605 ILE D O   
18790 C CB  . ILE D 613 ? 0.3438 0.2832 0.2305 -0.0439 -0.1146 -0.0218 605 ILE D CB  
18791 C CG1 . ILE D 613 ? 0.3372 0.2617 0.2071 -0.0517 -0.1221 -0.0260 605 ILE D CG1 
18792 C CG2 . ILE D 613 ? 0.2985 0.2490 0.2054 -0.0448 -0.1118 -0.0193 605 ILE D CG2 
18793 C CD1 . ILE D 613 ? 0.3876 0.3088 0.2437 -0.0545 -0.1308 -0.0256 605 ILE D CD1 
18794 N N   . ALA D 614 ? 0.3181 0.2607 0.2169 -0.0252 -0.0906 -0.0210 606 ALA D N   
18795 C CA  . ALA D 614 ? 0.2609 0.2142 0.1735 -0.0188 -0.0853 -0.0172 606 ALA D CA  
18796 C C   . ALA D 614 ? 0.2483 0.2144 0.1794 -0.0206 -0.0865 -0.0142 606 ALA D C   
18797 O O   . ALA D 614 ? 0.2853 0.2488 0.2184 -0.0255 -0.0873 -0.0158 606 ALA D O   
18798 C CB  . ALA D 614 ? 0.2778 0.2225 0.1866 -0.0134 -0.0762 -0.0194 606 ALA D CB  
18799 N N   . VAL D 615 ? 0.2644 0.2441 0.2083 -0.0165 -0.0866 -0.0099 607 VAL D N   
18800 C CA  . VAL D 615 ? 0.2454 0.2390 0.2070 -0.0169 -0.0866 -0.0069 607 VAL D CA  
18801 C C   . VAL D 615 ? 0.2484 0.2467 0.2180 -0.0091 -0.0804 -0.0049 607 VAL D C   
18802 O O   . VAL D 615 ? 0.2206 0.2222 0.1906 -0.0042 -0.0812 -0.0028 607 VAL D O   
18803 C CB  . VAL D 615 ? 0.2645 0.2718 0.2353 -0.0200 -0.0946 -0.0035 607 VAL D CB  
18804 C CG1 . VAL D 615 ? 0.2197 0.2426 0.2095 -0.0201 -0.0933 -0.0004 607 VAL D CG1 
18805 C CG2 . VAL D 615 ? 0.2712 0.2723 0.2325 -0.0282 -0.1021 -0.0053 607 VAL D CG2 
18806 N N   . GLU D 616 ? 0.2030 0.2002 0.1779 -0.0083 -0.0748 -0.0054 608 GLU D N   
18807 C CA  . GLU D 616 ? 0.1916 0.1911 0.1725 -0.0014 -0.0693 -0.0038 608 GLU D CA  
18808 C C   . GLU D 616 ? 0.1969 0.1985 0.1853 -0.0029 -0.0654 -0.0037 608 GLU D C   
18809 O O   . GLU D 616 ? 0.2178 0.2113 0.2015 -0.0076 -0.0646 -0.0059 608 GLU D O   
18810 C CB  . GLU D 616 ? 0.2264 0.2136 0.1969 0.0026  -0.0654 -0.0055 608 GLU D CB  
18811 C CG  . GLU D 616 ? 0.2268 0.2133 0.2020 0.0087  -0.0603 -0.0041 608 GLU D CG  
18812 C CD  . GLU D 616 ? 0.2424 0.2191 0.2090 0.0121  -0.0574 -0.0047 608 GLU D CD  
18813 O OE1 . GLU D 616 ? 0.2290 0.1961 0.1899 0.0110  -0.0539 -0.0072 608 GLU D OE1 
18814 O OE2 . GLU D 616 ? 0.2589 0.2378 0.2250 0.0158  -0.0587 -0.0023 608 GLU D OE2 
18815 N N   . ALA D 617 ? 0.1770 0.1885 0.1760 0.0013  -0.0630 -0.0012 609 ALA D N   
18816 C CA  . ALA D 617 ? 0.1728 0.1871 0.1782 0.0001  -0.0589 -0.0005 609 ALA D CA  
18817 C C   . ALA D 617 ? 0.2199 0.2213 0.2189 0.0029  -0.0539 -0.0020 609 ALA D C   
18818 O O   . ALA D 617 ? 0.2231 0.2255 0.2255 0.0076  -0.0502 -0.0009 609 ALA D O   
18819 C CB  . ALA D 617 ? 0.1661 0.1953 0.1837 0.0042  -0.0577 0.0024  609 ALA D CB  
18820 N N   . GLY D 618 ? 0.2296 0.2186 0.2193 -0.0001 -0.0540 -0.0047 610 GLY D N   
18821 C CA  . GLY D 618 ? 0.1947 0.1717 0.1795 0.0020  -0.0499 -0.0061 610 GLY D CA  
18822 C C   . GLY D 618 ? 0.1857 0.1506 0.1617 -0.0023 -0.0505 -0.0094 610 GLY D C   
18823 O O   . GLY D 618 ? 0.2032 0.1682 0.1761 -0.0075 -0.0544 -0.0107 610 GLY D O   
18824 N N   . HIS D 619 ? 0.1859 0.1398 0.1580 0.0001  -0.0471 -0.0107 611 HIS D N   
18825 C CA  . HIS D 619 ? 0.2371 0.1782 0.2012 -0.0027 -0.0471 -0.0141 611 HIS D CA  
18826 C C   . HIS D 619 ? 0.2328 0.1708 0.1882 -0.0036 -0.0494 -0.0168 611 HIS D C   
18827 O O   . HIS D 619 ? 0.2469 0.1892 0.2011 0.0000  -0.0493 -0.0159 611 HIS D O   
18828 C CB  . HIS D 619 ? 0.2053 0.1367 0.1681 0.0019  -0.0430 -0.0147 611 HIS D CB  
18829 C CG  . HIS D 619 ? 0.2027 0.1214 0.1608 -0.0008 -0.0427 -0.0175 611 HIS D CG  
18830 N ND1 . HIS D 619 ? 0.2207 0.1303 0.1699 -0.0022 -0.0436 -0.0215 611 HIS D ND1 
18831 C CD2 . HIS D 619 ? 0.2299 0.1427 0.1902 -0.0023 -0.0420 -0.0168 611 HIS D CD2 
18832 C CE1 . HIS D 619 ? 0.2734 0.1717 0.2201 -0.0041 -0.0436 -0.0234 611 HIS D CE1 
18833 N NE2 . HIS D 619 ? 0.2448 0.1450 0.1984 -0.0044 -0.0428 -0.0203 611 HIS D NE2 
18834 N N   . THR D 620 ? 0.2280 0.1577 0.1763 -0.0086 -0.0519 -0.0200 612 THR D N   
18835 C CA  . THR D 620 ? 0.2443 0.1691 0.1817 -0.0101 -0.0547 -0.0230 612 THR D CA  
18836 C C   . THR D 620 ? 0.2779 0.1908 0.2054 -0.0056 -0.0506 -0.0266 612 THR D C   
18837 O O   . THR D 620 ? 0.2455 0.1553 0.1629 -0.0053 -0.0515 -0.0287 612 THR D O   
18838 C CB  . THR D 620 ? 0.2970 0.2161 0.2294 -0.0179 -0.0600 -0.0253 612 THR D CB  
18839 O OG1 . THR D 620 ? 0.2482 0.1540 0.1769 -0.0188 -0.0583 -0.0279 612 THR D OG1 
18840 C CG2 . THR D 620 ? 0.2359 0.1683 0.1791 -0.0233 -0.0641 -0.0214 612 THR D CG2 
18841 N N   . ASN D 621 ? 0.2614 0.1679 0.1913 -0.0020 -0.0461 -0.0271 613 ASN D N   
18842 C CA  . ASN D 621 ? 0.3230 0.2164 0.2433 0.0009  -0.0428 -0.0315 613 ASN D CA  
18843 C C   . ASN D 621 ? 0.3745 0.2702 0.2908 0.0064  -0.0388 -0.0314 613 ASN D C   
18844 O O   . ASN D 621 ? 0.3710 0.2581 0.2762 0.0081  -0.0366 -0.0353 613 ASN D O   
18845 C CB  . ASN D 621 ? 0.3696 0.2553 0.2945 0.0030  -0.0399 -0.0319 613 ASN D CB  
18846 C CG  . ASN D 621 ? 0.4661 0.3417 0.3875 -0.0028 -0.0438 -0.0344 613 ASN D CG  
18847 O OD1 . ASN D 621 ? 0.4265 0.2914 0.3475 -0.0013 -0.0424 -0.0361 613 ASN D OD1 
18848 N ND2 . ASN D 621 ? 0.3512 0.2300 0.2703 -0.0095 -0.0493 -0.0343 613 ASN D ND2 
18849 N N   . GLY D 622 ? 0.3293 0.2361 0.2532 0.0090  -0.0380 -0.0268 614 GLY D N   
18850 C CA  . GLY D 622 ? 0.2727 0.1819 0.1926 0.0130  -0.0348 -0.0259 614 GLY D CA  
18851 C C   . GLY D 622 ? 0.3480 0.2579 0.2567 0.0104  -0.0380 -0.0271 614 GLY D C   
18852 O O   . GLY D 622 ? 0.4154 0.3242 0.3166 0.0131  -0.0350 -0.0272 614 GLY D O   
18853 N N   . TRP D 623 ? 0.2902 0.2023 0.1978 0.0050  -0.0443 -0.0275 615 TRP D N   
18854 C CA  . TRP D 623 ? 0.3352 0.2483 0.2329 0.0020  -0.0488 -0.0280 615 TRP D CA  
18855 C C   . TRP D 623 ? 0.3368 0.2365 0.2172 0.0006  -0.0485 -0.0337 615 TRP D C   
18856 O O   . TRP D 623 ? 0.3620 0.2606 0.2311 -0.0011 -0.0515 -0.0343 615 TRP D O   
18857 C CB  . TRP D 623 ? 0.2991 0.2205 0.2033 -0.0034 -0.0562 -0.0260 615 TRP D CB  
18858 C CG  . TRP D 623 ? 0.2486 0.1834 0.1660 -0.0008 -0.0567 -0.0206 615 TRP D CG  
18859 C CD1 . TRP D 623 ? 0.2234 0.1653 0.1544 -0.0002 -0.0559 -0.0181 615 TRP D CD1 
18860 C CD2 . TRP D 623 ? 0.2659 0.2074 0.1830 0.0019  -0.0578 -0.0173 615 TRP D CD2 
18861 N NE1 . TRP D 623 ? 0.2747 0.2268 0.2135 0.0032  -0.0565 -0.0140 615 TRP D NE1 
18862 C CE2 . TRP D 623 ? 0.2463 0.1983 0.1774 0.0045  -0.0580 -0.0133 615 TRP D CE2 
18863 C CE3 . TRP D 623 ? 0.2892 0.2279 0.1946 0.0024  -0.0587 -0.0174 615 TRP D CE3 
18864 C CZ2 . TRP D 623 ? 0.2381 0.1970 0.1722 0.0077  -0.0596 -0.0094 615 TRP D CZ2 
18865 C CZ3 . TRP D 623 ? 0.2951 0.2415 0.2038 0.0050  -0.0604 -0.0129 615 TRP D CZ3 
18866 C CH2 . TRP D 623 ? 0.2981 0.2541 0.2213 0.0077  -0.0611 -0.0090 615 TRP D CH2 
18867 N N   . TYR D 624 ? 0.3009 0.1897 0.1781 0.0017  -0.0452 -0.0378 616 TYR D N   
18868 C CA  . TYR D 624 ? 0.3042 0.1786 0.1638 0.0010  -0.0448 -0.0439 616 TYR D CA  
18869 C C   . TYR D 624 ? 0.3762 0.2482 0.2251 0.0062  -0.0386 -0.0450 616 TYR D C   
18870 O O   . TYR D 624 ? 0.3590 0.2208 0.1903 0.0054  -0.0390 -0.0495 616 TYR D O   
18871 C CB  . TYR D 624 ? 0.3598 0.2222 0.2192 0.0016  -0.0430 -0.0481 616 TYR D CB  
18872 C CG  . TYR D 624 ? 0.3833 0.2449 0.2475 -0.0056 -0.0504 -0.0477 616 TYR D CG  
18873 C CD1 . TYR D 624 ? 0.3804 0.2362 0.2338 -0.0122 -0.0578 -0.0501 616 TYR D CD1 
18874 C CD2 . TYR D 624 ? 0.3819 0.2491 0.2614 -0.0062 -0.0502 -0.0444 616 TYR D CD2 
18875 C CE1 . TYR D 624 ? 0.4039 0.2605 0.2631 -0.0195 -0.0647 -0.0489 616 TYR D CE1 
18876 C CE2 . TYR D 624 ? 0.4735 0.3413 0.3576 -0.0133 -0.0563 -0.0433 616 TYR D CE2 
18877 C CZ  . TYR D 624 ? 0.4556 0.3187 0.3303 -0.0200 -0.0635 -0.0454 616 TYR D CZ  
18878 O OH  . TYR D 624 ? 0.4808 0.3457 0.3615 -0.0277 -0.0697 -0.0436 616 TYR D OH  
18879 N N   . LYS D 625 ? 0.3461 0.2272 0.2049 0.0112  -0.0330 -0.0407 617 LYS D N   
18880 C CA  . LYS D 625 ? 0.4105 0.2924 0.2610 0.0152  -0.0272 -0.0401 617 LYS D CA  
18881 C C   . LYS D 625 ? 0.3797 0.2623 0.2169 0.0114  -0.0323 -0.0395 617 LYS D C   
18882 O O   . LYS D 625 ? 0.3767 0.2532 0.1980 0.0128  -0.0288 -0.0418 617 LYS D O   
18883 C CB  . LYS D 625 ? 0.4128 0.3061 0.2782 0.0192  -0.0230 -0.0340 617 LYS D CB  
18884 C CG  . LYS D 625 ? 0.5263 0.4225 0.3854 0.0225  -0.0172 -0.0317 617 LYS D CG  
18885 C CD  . LYS D 625 ? 0.5830 0.4906 0.4574 0.0247  -0.0157 -0.0247 617 LYS D CD  
18886 C CE  . LYS D 625 ? 0.6269 0.5383 0.4950 0.0264  -0.0114 -0.0211 617 LYS D CE  
18887 N NZ  . LYS D 625 ? 0.5972 0.5184 0.4799 0.0280  -0.0110 -0.0141 617 LYS D NZ  
18888 N N   . TYR D 626 ? 0.3328 0.2228 0.1763 0.0068  -0.0404 -0.0363 618 TYR D N   
18889 C CA  . TYR D 626 ? 0.3400 0.2309 0.1725 0.0027  -0.0470 -0.0352 618 TYR D CA  
18890 C C   . TYR D 626 ? 0.3879 0.2692 0.2087 -0.0032 -0.0542 -0.0399 618 TYR D C   
18891 O O   . TYR D 626 ? 0.4105 0.2842 0.2131 -0.0053 -0.0568 -0.0423 618 TYR D O   
18892 C CB  . TYR D 626 ? 0.3334 0.2385 0.1800 0.0015  -0.0524 -0.0287 618 TYR D CB  
18893 C CG  . TYR D 626 ? 0.3295 0.2426 0.1863 0.0067  -0.0469 -0.0238 618 TYR D CG  
18894 C CD1 . TYR D 626 ? 0.4450 0.3582 0.2930 0.0088  -0.0437 -0.0214 618 TYR D CD1 
18895 C CD2 . TYR D 626 ? 0.4431 0.3628 0.3176 0.0090  -0.0451 -0.0214 618 TYR D CD2 
18896 C CE1 . TYR D 626 ? 0.3793 0.2993 0.2370 0.0128  -0.0392 -0.0164 618 TYR D CE1 
18897 C CE2 . TYR D 626 ? 0.4909 0.4165 0.3741 0.0133  -0.0410 -0.0168 618 TYR D CE2 
18898 C CZ  . TYR D 626 ? 0.4689 0.3948 0.3442 0.0149  -0.0383 -0.0143 618 TYR D CZ  
18899 O OH  . TYR D 626 ? 0.5323 0.4636 0.4165 0.0184  -0.0350 -0.0093 618 TYR D OH  
18900 N N   . VAL D 627 ? 0.3508 0.2316 0.1808 -0.0065 -0.0580 -0.0411 619 VAL D N   
18901 C CA  . VAL D 627 ? 0.3806 0.2543 0.2017 -0.0136 -0.0668 -0.0441 619 VAL D CA  
18902 C C   . VAL D 627 ? 0.4151 0.2701 0.2202 -0.0139 -0.0651 -0.0515 619 VAL D C   
18903 O O   . VAL D 627 ? 0.4419 0.2871 0.2334 -0.0195 -0.0724 -0.0549 619 VAL D O   
18904 C CB  . VAL D 627 ? 0.4304 0.3139 0.2690 -0.0185 -0.0732 -0.0408 619 VAL D CB  
18905 C CG1 . VAL D 627 ? 0.3349 0.2363 0.1900 -0.0168 -0.0740 -0.0340 619 VAL D CG1 
18906 C CG2 . VAL D 627 ? 0.3856 0.2645 0.2325 -0.0180 -0.0696 -0.0428 619 VAL D CG2 
18907 N N   . GLY D 628 ? 0.4187 0.2681 0.2247 -0.0078 -0.0562 -0.0542 620 GLY D N   
18908 C CA  . GLY D 628 ? 0.4358 0.2667 0.2259 -0.0067 -0.0540 -0.0616 620 GLY D CA  
18909 C C   . GLY D 628 ? 0.4713 0.2934 0.2622 -0.0129 -0.0614 -0.0643 620 GLY D C   
18910 O O   . GLY D 628 ? 0.4602 0.2920 0.2668 -0.0176 -0.0665 -0.0600 620 GLY D O   
18911 N N   . LEU D 629 ? 0.4392 0.2420 0.2120 -0.0130 -0.0619 -0.0715 621 LEU D N   
18912 C CA  . LEU D 629 ? 0.4901 0.2810 0.2615 -0.0187 -0.0686 -0.0746 621 LEU D CA  
18913 C C   . LEU D 629 ? 0.5287 0.3189 0.2949 -0.0288 -0.0809 -0.0735 621 LEU D C   
18914 O O   . LEU D 629 ? 0.5687 0.3556 0.3407 -0.0352 -0.0875 -0.0730 621 LEU D O   
18915 C CB  . LEU D 629 ? 0.5676 0.3364 0.3209 -0.0144 -0.0650 -0.0830 621 LEU D CB  
18916 C CG  . LEU D 629 ? 0.4957 0.2631 0.2557 -0.0047 -0.0538 -0.0846 621 LEU D CG  
18917 C CD1 . LEU D 629 ? 0.4846 0.2351 0.2320 -0.0003 -0.0499 -0.0913 621 LEU D CD1 
18918 C CD2 . LEU D 629 ? 0.4992 0.2756 0.2818 -0.0058 -0.0542 -0.0798 621 LEU D CD2 
18919 N N   . ASN D 630 ? 0.5299 0.3237 0.2862 -0.0304 -0.0842 -0.0724 622 ASN D N   
18920 C CA  . ASN D 630 ? 0.6000 0.3960 0.3546 -0.0393 -0.0952 -0.0701 622 ASN D CA  
18921 C C   . ASN D 630 ? 0.5865 0.4022 0.3568 -0.0435 -0.1013 -0.0630 622 ASN D C   
18922 O O   . ASN D 630 ? 0.4576 0.2786 0.2318 -0.0510 -0.1105 -0.0598 622 ASN D O   
18923 C CB  . ASN D 630 ? 0.6635 0.4501 0.3974 -0.0386 -0.0954 -0.0732 622 ASN D CB  
18924 C CG  . ASN D 630 ? 0.7515 0.5199 0.4705 -0.0335 -0.0888 -0.0803 622 ASN D CG  
18925 O OD1 . ASN D 630 ? 0.6985 0.4587 0.4214 -0.0345 -0.0892 -0.0826 622 ASN D OD1 
18926 N ND2 . ASN D 630 ? 0.8698 0.6324 0.5720 -0.0279 -0.0824 -0.0835 622 ASN D ND2 
18927 N N   . GLY D 631 ? 0.5285 0.3601 0.3149 -0.0374 -0.0936 -0.0583 623 GLY D N   
18928 C CA  . GLY D 631 ? 0.4717 0.3244 0.2784 -0.0394 -0.0969 -0.0508 623 GLY D CA  
18929 C C   . GLY D 631 ? 0.4102 0.2711 0.2369 -0.0422 -0.0975 -0.0479 623 GLY D C   
18930 O O   . GLY D 631 ? 0.4365 0.2858 0.2604 -0.0450 -0.0982 -0.0512 623 GLY D O   
18931 N N   . ALA D 632 ? 0.3527 0.2331 0.1991 -0.0414 -0.0971 -0.0415 624 ALA D N   
18932 C CA  . ALA D 632 ? 0.4308 0.3207 0.2962 -0.0438 -0.0968 -0.0381 624 ALA D CA  
18933 C C   . ALA D 632 ? 0.3822 0.2903 0.2650 -0.0381 -0.0918 -0.0327 624 ALA D C   
18934 O O   . ALA D 632 ? 0.3044 0.2186 0.1859 -0.0340 -0.0908 -0.0309 624 ALA D O   
18935 C CB  . ALA D 632 ? 0.4642 0.3584 0.3348 -0.0537 -0.1072 -0.0360 624 ALA D CB  
18936 N N   . VAL D 633 ? 0.3360 0.2515 0.2342 -0.0382 -0.0888 -0.0301 625 VAL D N   
18937 C CA  . VAL D 633 ? 0.2991 0.2301 0.2133 -0.0329 -0.0841 -0.0254 625 VAL D CA  
18938 C C   . VAL D 633 ? 0.3161 0.2605 0.2468 -0.0378 -0.0870 -0.0212 625 VAL D C   
18939 O O   . VAL D 633 ? 0.3378 0.2770 0.2693 -0.0435 -0.0886 -0.0219 625 VAL D O   
18940 C CB  . VAL D 633 ? 0.2897 0.2152 0.2047 -0.0260 -0.0751 -0.0265 625 VAL D CB  
18941 C CG1 . VAL D 633 ? 0.2462 0.1858 0.1747 -0.0202 -0.0711 -0.0219 625 VAL D CG1 
18942 C CG2 . VAL D 633 ? 0.3007 0.2120 0.1997 -0.0219 -0.0713 -0.0311 625 VAL D CG2 
18943 N N   . VAL D 634 ? 0.2705 0.2319 0.2143 -0.0353 -0.0873 -0.0166 626 VAL D N   
18944 C CA  . VAL D 634 ? 0.2442 0.2207 0.2055 -0.0373 -0.0871 -0.0122 626 VAL D CA  
18945 C C   . VAL D 634 ? 0.2594 0.2397 0.2277 -0.0296 -0.0790 -0.0109 626 VAL D C   
18946 O O   . VAL D 634 ? 0.2351 0.2208 0.2054 -0.0231 -0.0771 -0.0095 626 VAL D O   
18947 C CB  . VAL D 634 ? 0.2381 0.2314 0.2100 -0.0394 -0.0934 -0.0082 626 VAL D CB  
18948 C CG1 . VAL D 634 ? 0.2439 0.2545 0.2350 -0.0406 -0.0916 -0.0037 626 VAL D CG1 
18949 C CG2 . VAL D 634 ? 0.2882 0.2763 0.2521 -0.0476 -0.1026 -0.0094 626 VAL D CG2 
18950 N N   . GLY D 635 ? 0.2378 0.2139 0.2086 -0.0305 -0.0747 -0.0112 627 GLY D N   
18951 C CA  . GLY D 635 ? 0.2566 0.2331 0.2315 -0.0237 -0.0676 -0.0103 627 GLY D CA  
18952 C C   . GLY D 635 ? 0.2919 0.2698 0.2736 -0.0267 -0.0648 -0.0086 627 GLY D C   
18953 O O   . GLY D 635 ? 0.2397 0.2230 0.2265 -0.0339 -0.0681 -0.0070 627 GLY D O   
18954 N N   . ILE D 636 ? 0.2011 0.1741 0.1829 -0.0218 -0.0592 -0.0087 628 ILE D N   
18955 C CA  . ILE D 636 ? 0.1991 0.1720 0.1855 -0.0243 -0.0563 -0.0069 628 ILE D CA  
18956 C C   . ILE D 636 ? 0.1997 0.1575 0.1791 -0.0208 -0.0526 -0.0090 628 ILE D C   
18957 O O   . ILE D 636 ? 0.1937 0.1495 0.1718 -0.0138 -0.0497 -0.0094 628 ILE D O   
18958 C CB  . ILE D 636 ? 0.2445 0.2333 0.2425 -0.0215 -0.0534 -0.0030 628 ILE D CB  
18959 C CG1 . ILE D 636 ? 0.1882 0.1759 0.1888 -0.0238 -0.0496 -0.0010 628 ILE D CG1 
18960 C CG2 . ILE D 636 ? 0.2757 0.2666 0.2741 -0.0124 -0.0507 -0.0029 628 ILE D CG2 
18961 C CD1 . ILE D 636 ? 0.2642 0.2667 0.2744 -0.0206 -0.0459 0.0024  628 ILE D CD1 
18962 N N   . ASN D 637 ? 0.2193 0.1659 0.1942 -0.0257 -0.0534 -0.0102 629 ASN D N   
18963 C CA  . ASN D 637 ? 0.2455 0.1772 0.2145 -0.0226 -0.0508 -0.0122 629 ASN D CA  
18964 C C   . ASN D 637 ? 0.2780 0.2074 0.2501 -0.0249 -0.0488 -0.0096 629 ASN D C   
18965 O O   . ASN D 637 ? 0.3053 0.2212 0.2727 -0.0242 -0.0481 -0.0109 629 ASN D O   
18966 C CB  . ASN D 637 ? 0.2239 0.1406 0.1828 -0.0251 -0.0535 -0.0166 629 ASN D CB  
18967 C CG  . ASN D 637 ? 0.2429 0.1591 0.1957 -0.0220 -0.0545 -0.0196 629 ASN D CG  
18968 O OD1 . ASN D 637 ? 0.2494 0.1752 0.2057 -0.0174 -0.0530 -0.0181 629 ASN D OD1 
18969 N ND2 . ASN D 637 ? 0.3021 0.2061 0.2446 -0.0245 -0.0572 -0.0238 629 ASN D ND2 
18970 N N   . ARG D 638 ? 0.2550 0.1974 0.2347 -0.0274 -0.0479 -0.0058 630 ARG D N   
18971 C CA  . ARG D 638 ? 0.2356 0.1769 0.2172 -0.0298 -0.0456 -0.0028 630 ARG D CA  
18972 C C   . ARG D 638 ? 0.2805 0.2334 0.2678 -0.0244 -0.0413 -0.0001 630 ARG D C   
18973 O O   . ARG D 638 ? 0.2349 0.1979 0.2262 -0.0198 -0.0409 -0.0003 630 ARG D O   
18974 C CB  . ARG D 638 ? 0.2365 0.1816 0.2207 -0.0396 -0.0481 -0.0003 630 ARG D CB  
18975 C CG  . ARG D 638 ? 0.2847 0.2482 0.2776 -0.0423 -0.0493 0.0018  630 ARG D CG  
18976 C CD  . ARG D 638 ? 0.3846 0.3577 0.3841 -0.0502 -0.0487 0.0065  630 ARG D CD  
18977 N NE  . ARG D 638 ? 0.3787 0.3591 0.3818 -0.0461 -0.0426 0.0094  630 ARG D NE  
18978 C CZ  . ARG D 638 ? 0.3859 0.3761 0.3944 -0.0511 -0.0397 0.0139  630 ARG D CZ  
18979 N NH1 . ARG D 638 ? 0.4033 0.3978 0.4157 -0.0611 -0.0429 0.0166  630 ARG D NH1 
18980 N NH2 . ARG D 638 ? 0.3542 0.3492 0.3634 -0.0464 -0.0338 0.0157  630 ARG D NH2 
18981 N N   . PHE D 639 ? 0.1950 0.1450 0.1817 -0.0248 -0.0385 0.0023  631 PHE D N   
18982 C CA  . PHE D 639 ? 0.1882 0.1469 0.1780 -0.0196 -0.0344 0.0044  631 PHE D CA  
18983 C C   . PHE D 639 ? 0.1889 0.1664 0.1874 -0.0217 -0.0331 0.0068  631 PHE D C   
18984 O O   . PHE D 639 ? 0.1981 0.1813 0.2003 -0.0291 -0.0352 0.0080  631 PHE D O   
18985 C CB  . PHE D 639 ? 0.2517 0.2016 0.2368 -0.0202 -0.0321 0.0064  631 PHE D CB  
18986 C CG  . PHE D 639 ? 0.2046 0.1379 0.1834 -0.0166 -0.0334 0.0046  631 PHE D CG  
18987 C CD1 . PHE D 639 ? 0.2613 0.1930 0.2398 -0.0088 -0.0329 0.0032  631 PHE D CD1 
18988 C CD2 . PHE D 639 ? 0.2015 0.1208 0.1753 -0.0210 -0.0356 0.0046  631 PHE D CD2 
18989 C CE1 . PHE D 639 ? 0.2899 0.2081 0.2646 -0.0057 -0.0342 0.0022  631 PHE D CE1 
18990 C CE2 . PHE D 639 ? 0.2026 0.1079 0.1725 -0.0172 -0.0369 0.0032  631 PHE D CE2 
18991 C CZ  . PHE D 639 ? 0.1953 0.1008 0.1662 -0.0096 -0.0360 0.0022  631 PHE D CZ  
18992 N N   . GLY D 640 ? 0.1879 0.1749 0.1900 -0.0151 -0.0298 0.0075  632 GLY D N   
18993 C CA  . GLY D 640 ? 0.2146 0.2206 0.2263 -0.0150 -0.0280 0.0096  632 GLY D CA  
18994 C C   . GLY D 640 ? 0.2140 0.2276 0.2284 -0.0194 -0.0236 0.0132  632 GLY D C   
18995 O O   . GLY D 640 ? 0.2272 0.2313 0.2361 -0.0251 -0.0233 0.0145  632 GLY D O   
18996 N N   . GLU D 641 ? 0.1895 0.2208 0.2127 -0.0166 -0.0200 0.0151  633 GLU D N   
18997 C CA  . GLU D 641 ? 0.2046 0.2472 0.2320 -0.0198 -0.0145 0.0188  633 GLU D CA  
18998 C C   . GLU D 641 ? 0.2208 0.2752 0.2522 -0.0104 -0.0091 0.0187  633 GLU D C   
18999 O O   . GLU D 641 ? 0.1736 0.2345 0.2105 -0.0040 -0.0110 0.0170  633 GLU D O   
19000 C CB  . GLU D 641 ? 0.2403 0.2980 0.2790 -0.0289 -0.0161 0.0222  633 GLU D CB  
19001 C CG  . GLU D 641 ? 0.2142 0.2605 0.2486 -0.0394 -0.0212 0.0228  633 GLU D CG  
19002 C CD  . GLU D 641 ? 0.2943 0.3299 0.3203 -0.0446 -0.0184 0.0251  633 GLU D CD  
19003 O OE1 . GLU D 641 ? 0.2754 0.3166 0.3005 -0.0420 -0.0118 0.0273  633 GLU D OE1 
19004 O OE2 . GLU D 641 ? 0.2818 0.3024 0.3012 -0.0511 -0.0230 0.0247  633 GLU D OE2 
19005 N N   . SER D 642 ? 0.1849 0.2412 0.2128 -0.0096 -0.0026 0.0206  634 SER D N   
19006 C CA  . SER D 642 ? 0.1847 0.2527 0.2160 -0.0007 0.0035  0.0205  634 SER D CA  
19007 C C   . SER D 642 ? 0.2052 0.2980 0.2530 -0.0031 0.0061  0.0236  634 SER D C   
19008 O O   . SER D 642 ? 0.1887 0.2903 0.2405 -0.0110 0.0095  0.0276  634 SER D O   
19009 C CB  . SER D 642 ? 0.2176 0.2774 0.2370 0.0010  0.0097  0.0211  634 SER D CB  
19010 O OG  . SER D 642 ? 0.2368 0.3076 0.2582 0.0099  0.0163  0.0206  634 SER D OG  
19011 N N   . ALA D 643 ? 0.1774 0.2817 0.2352 0.0033  0.0042  0.0223  635 ALA D N   
19012 C CA  . ALA D 643 ? 0.1755 0.3044 0.2513 0.0023  0.0055  0.0253  635 ALA D CA  
19013 C C   . ALA D 643 ? 0.1856 0.3207 0.2682 0.0121  0.0024  0.0228  635 ALA D C   
19014 O O   . ALA D 643 ? 0.1934 0.3128 0.2669 0.0168  -0.0021 0.0193  635 ALA D O   
19015 C CB  . ALA D 643 ? 0.1867 0.3209 0.2703 -0.0101 -0.0001 0.0283  635 ALA D CB  
19016 N N   . PRO D 644 ? 0.1682 0.3260 0.2674 0.0152  0.0046  0.0250  636 PRO D N   
19017 C CA  . PRO D 644 ? 0.1853 0.3489 0.2919 0.0238  0.0003  0.0232  636 PRO D CA  
19018 C C   . PRO D 644 ? 0.1860 0.3413 0.2914 0.0190  -0.0100 0.0222  636 PRO D C   
19019 O O   . PRO D 644 ? 0.2114 0.3661 0.3181 0.0083  -0.0141 0.0241  636 PRO D O   
19020 C CB  . PRO D 644 ? 0.1898 0.3815 0.3170 0.0252  0.0040  0.0268  636 PRO D CB  
19021 C CG  . PRO D 644 ? 0.2154 0.4134 0.3413 0.0230  0.0142  0.0291  636 PRO D CG  
19022 C CD  . PRO D 644 ? 0.2053 0.3843 0.3164 0.0127  0.0124  0.0292  636 PRO D CD  
19023 N N   . ALA D 645 ? 0.1679 0.3159 0.2698 0.0271  -0.0143 0.0194  637 ALA D N   
19024 C CA  . ALA D 645 ? 0.2118 0.3478 0.3079 0.0236  -0.0231 0.0179  637 ALA D CA  
19025 C C   . ALA D 645 ? 0.1528 0.3025 0.2614 0.0164  -0.0294 0.0206  637 ALA D C   
19026 O O   . ALA D 645 ? 0.1836 0.3235 0.2861 0.0089  -0.0355 0.0201  637 ALA D O   
19027 C CB  . ALA D 645 ? 0.2792 0.4064 0.3699 0.0338  -0.0260 0.0152  637 ALA D CB  
19028 N N   . ASP D 646 ? 0.1523 0.3242 0.2782 0.0189  -0.0285 0.0235  638 ASP D N   
19029 C CA  . ASP D 646 ? 0.3214 0.5071 0.4603 0.0116  -0.0355 0.0267  638 ASP D CA  
19030 C C   . ASP D 646 ? 0.3265 0.5100 0.4637 -0.0019 -0.0367 0.0287  638 ASP D C   
19031 O O   . ASP D 646 ? 0.2710 0.4480 0.4048 -0.0096 -0.0447 0.0285  638 ASP D O   
19032 C CB  . ASP D 646 ? 0.3505 0.5626 0.5106 0.0165  -0.0332 0.0301  638 ASP D CB  
19033 N N   . LEU D 647 ? 0.2427 0.4306 0.3810 -0.0048 -0.0288 0.0305  639 LEU D N   
19034 C CA  . LEU D 647 ? 0.2029 0.3878 0.3394 -0.0178 -0.0299 0.0328  639 LEU D CA  
19035 C C   . LEU D 647 ? 0.2108 0.3691 0.3278 -0.0218 -0.0341 0.0290  639 LEU D C   
19036 O O   . LEU D 647 ? 0.1993 0.3514 0.3135 -0.0321 -0.0398 0.0297  639 LEU D O   
19037 C CB  . LEU D 647 ? 0.2476 0.4407 0.3870 -0.0195 -0.0201 0.0357  639 LEU D CB  
19038 C CG  . LEU D 647 ? 0.4081 0.6297 0.5679 -0.0164 -0.0142 0.0401  639 LEU D CG  
19039 C CD1 . LEU D 647 ? 0.4591 0.6861 0.6183 -0.0195 -0.0040 0.0430  639 LEU D CD1 
19040 C CD2 . LEU D 647 ? 0.4093 0.6497 0.5876 -0.0241 -0.0215 0.0445  639 LEU D CD2 
19041 N N   . LEU D 648 ? 0.1625 0.3046 0.2660 -0.0138 -0.0313 0.0250  640 LEU D N   
19042 C CA  . LEU D 648 ? 0.1646 0.2829 0.2512 -0.0167 -0.0343 0.0216  640 LEU D CA  
19043 C C   . LEU D 648 ? 0.2605 0.3723 0.3440 -0.0197 -0.0433 0.0198  640 LEU D C   
19044 O O   . LEU D 648 ? 0.2082 0.3081 0.2840 -0.0277 -0.0475 0.0188  640 LEU D O   
19045 C CB  . LEU D 648 ? 0.1618 0.2661 0.2368 -0.0073 -0.0302 0.0183  640 LEU D CB  
19046 C CG  . LEU D 648 ? 0.1762 0.2808 0.2488 -0.0052 -0.0218 0.0194  640 LEU D CG  
19047 C CD1 . LEU D 648 ? 0.2013 0.2906 0.2619 0.0040  -0.0196 0.0160  640 LEU D CD1 
19048 C CD2 . LEU D 648 ? 0.2154 0.3124 0.2827 -0.0155 -0.0210 0.0210  640 LEU D CD2 
19049 N N   . PHE D 649 ? 0.1944 0.3127 0.2826 -0.0131 -0.0466 0.0192  641 PHE D N   
19050 C CA  . PHE D 649 ? 0.2504 0.3625 0.3342 -0.0159 -0.0552 0.0178  641 PHE D CA  
19051 C C   . PHE D 649 ? 0.2260 0.3443 0.3155 -0.0273 -0.0611 0.0201  641 PHE D C   
19052 O O   . PHE D 649 ? 0.2333 0.3379 0.3123 -0.0333 -0.0668 0.0180  641 PHE D O   
19053 C CB  . PHE D 649 ? 0.1616 0.2824 0.2516 -0.0078 -0.0582 0.0180  641 PHE D CB  
19054 C CG  . PHE D 649 ? 0.1974 0.3053 0.2768 0.0017  -0.0560 0.0150  641 PHE D CG  
19055 C CD1 . PHE D 649 ? 0.1629 0.2509 0.2266 0.0007  -0.0572 0.0119  641 PHE D CD1 
19056 C CD2 . PHE D 649 ? 0.1951 0.3108 0.2807 0.0117  -0.0528 0.0155  641 PHE D CD2 
19057 C CE1 . PHE D 649 ? 0.1721 0.2494 0.2275 0.0086  -0.0555 0.0099  641 PHE D CE1 
19058 C CE2 . PHE D 649 ? 0.1777 0.2806 0.2535 0.0196  -0.0518 0.0132  641 PHE D CE2 
19059 C CZ  . PHE D 649 ? 0.2160 0.3003 0.2773 0.0176  -0.0532 0.0107  641 PHE D CZ  
19060 N N   . LYS D 650 ? 0.2275 0.3662 0.3335 -0.0306 -0.0597 0.0246  642 LYS D N   
19061 C CA  . LYS D 650 ? 0.2265 0.3721 0.3395 -0.0424 -0.0658 0.0277  642 LYS D CA  
19062 C C   . LYS D 650 ? 0.2407 0.3711 0.3430 -0.0514 -0.0651 0.0270  642 LYS D C   
19063 O O   . LYS D 650 ? 0.3016 0.4213 0.3968 -0.0597 -0.0725 0.0259  642 LYS D O   
19064 C CB  . LYS D 650 ? 0.2505 0.4235 0.3857 -0.0436 -0.0636 0.0334  642 LYS D CB  
19065 N N   . ALA D 651 ? 0.2436 0.3715 0.3435 -0.0497 -0.0567 0.0274  643 ALA D N   
19066 C CA  . ALA D 651 ? 0.1896 0.3031 0.2800 -0.0581 -0.0562 0.0273  643 ALA D CA  
19067 C C   . ALA D 651 ? 0.2565 0.3445 0.3283 -0.0582 -0.0604 0.0219  643 ALA D C   
19068 O O   . ALA D 651 ? 0.3170 0.3923 0.3814 -0.0668 -0.0644 0.0213  643 ALA D O   
19069 C CB  . ALA D 651 ? 0.2310 0.3454 0.3205 -0.0551 -0.0465 0.0287  643 ALA D CB  
19070 N N   . PHE D 652 ? 0.2209 0.3011 0.2853 -0.0487 -0.0595 0.0180  644 PHE D N   
19071 C CA  . PHE D 652 ? 0.2559 0.3135 0.3036 -0.0477 -0.0621 0.0131  644 PHE D CA  
19072 C C   . PHE D 652 ? 0.2802 0.3344 0.3237 -0.0495 -0.0702 0.0110  644 PHE D C   
19073 O O   . PHE D 652 ? 0.2540 0.2915 0.2839 -0.0468 -0.0715 0.0067  644 PHE D O   
19074 C CB  . PHE D 652 ? 0.1860 0.2357 0.2271 -0.0372 -0.0562 0.0105  644 PHE D CB  
19075 C CG  . PHE D 652 ? 0.2134 0.2578 0.2519 -0.0367 -0.0497 0.0114  644 PHE D CG  
19076 C CD1 . PHE D 652 ? 0.2822 0.3093 0.3105 -0.0416 -0.0503 0.0098  644 PHE D CD1 
19077 C CD2 . PHE D 652 ? 0.1874 0.2432 0.2328 -0.0313 -0.0434 0.0136  644 PHE D CD2 
19078 C CE1 . PHE D 652 ? 0.2747 0.2961 0.3000 -0.0416 -0.0452 0.0110  644 PHE D CE1 
19079 C CE2 . PHE D 652 ? 0.2441 0.2937 0.2852 -0.0312 -0.0378 0.0145  644 PHE D CE2 
19080 C CZ  . PHE D 652 ? 0.2912 0.3236 0.3223 -0.0367 -0.0390 0.0134  644 PHE D CZ  
19081 N N   . GLY D 653 ? 0.3043 0.3740 0.3591 -0.0540 -0.0755 0.0141  645 GLY D N   
19082 C CA  . GLY D 653 ? 0.2247 0.2895 0.2740 -0.0580 -0.0846 0.0125  645 GLY D CA  
19083 C C   . GLY D 653 ? 0.2375 0.3041 0.2846 -0.0500 -0.0866 0.0110  645 GLY D C   
19084 O O   . GLY D 653 ? 0.2144 0.2720 0.2517 -0.0524 -0.0933 0.0087  645 GLY D O   
19085 N N   . PHE D 654 ? 0.2081 0.2849 0.2628 -0.0408 -0.0812 0.0122  646 PHE D N   
19086 C CA  . PHE D 654 ? 0.2053 0.2849 0.2594 -0.0336 -0.0839 0.0117  646 PHE D CA  
19087 C C   . PHE D 654 ? 0.2320 0.3327 0.3029 -0.0352 -0.0892 0.0160  646 PHE D C   
19088 O O   . PHE D 654 ? 0.2727 0.3882 0.3561 -0.0282 -0.0866 0.0184  646 PHE D O   
19089 C CB  . PHE D 654 ? 0.2206 0.2977 0.2728 -0.0230 -0.0766 0.0106  646 PHE D CB  
19090 C CG  . PHE D 654 ? 0.2173 0.2745 0.2544 -0.0217 -0.0725 0.0068  646 PHE D CG  
19091 C CD1 . PHE D 654 ? 0.2176 0.2602 0.2406 -0.0206 -0.0752 0.0036  646 PHE D CD1 
19092 C CD2 . PHE D 654 ? 0.2170 0.2700 0.2536 -0.0224 -0.0663 0.0066  646 PHE D CD2 
19093 C CE1 . PHE D 654 ? 0.1903 0.2160 0.2010 -0.0193 -0.0713 0.0003  646 PHE D CE1 
19094 C CE2 . PHE D 654 ? 0.2331 0.2681 0.2570 -0.0213 -0.0634 0.0034  646 PHE D CE2 
19095 C CZ  . PHE D 654 ? 0.2799 0.3019 0.2917 -0.0196 -0.0657 0.0002  646 PHE D CZ  
19096 N N   . THR D 655 ? 0.2219 0.3228 0.2928 -0.0447 -0.0973 0.0170  647 THR D N   
19097 C CA  . THR D 655 ? 0.2241 0.3444 0.3114 -0.0487 -0.1042 0.0216  647 THR D CA  
19098 C C   . THR D 655 ? 0.2780 0.3900 0.3553 -0.0525 -0.1150 0.0203  647 THR D C   
19099 O O   . THR D 655 ? 0.2388 0.3301 0.2966 -0.0551 -0.1169 0.0160  647 THR D O   
19100 C CB  . THR D 655 ? 0.2845 0.4148 0.3832 -0.0590 -0.1049 0.0252  647 THR D CB  
19101 O OG1 . THR D 655 ? 0.2808 0.3931 0.3650 -0.0687 -0.1104 0.0227  647 THR D OG1 
19102 C CG2 . THR D 655 ? 0.2318 0.3673 0.3365 -0.0561 -0.0938 0.0262  647 THR D CG2 
19103 N N   . VAL D 656 ? 0.2610 0.3893 0.3516 -0.0524 -0.1219 0.0242  648 VAL D N   
19104 C CA  . VAL D 656 ? 0.2622 0.3833 0.3432 -0.0562 -0.1331 0.0236  648 VAL D CA  
19105 C C   . VAL D 656 ? 0.2910 0.3994 0.3613 -0.0684 -0.1397 0.0221  648 VAL D C   
19106 O O   . VAL D 656 ? 0.2903 0.3791 0.3398 -0.0707 -0.1445 0.0180  648 VAL D O   
19107 C CB  . VAL D 656 ? 0.3377 0.4804 0.4379 -0.0548 -0.1403 0.0289  648 VAL D CB  
19108 C CG1 . VAL D 656 ? 0.3834 0.5200 0.4755 -0.0625 -0.1538 0.0294  648 VAL D CG1 
19109 C CG2 . VAL D 656 ? 0.3272 0.4749 0.4310 -0.0420 -0.1360 0.0290  648 VAL D CG2 
19110 N N   . ASP D 657 ? 0.3096 0.4286 0.3931 -0.0763 -0.1400 0.0254  649 ASP D N   
19111 C CA  . ASP D 657 ? 0.3504 0.4573 0.4248 -0.0887 -0.1470 0.0244  649 ASP D CA  
19112 C C   . ASP D 657 ? 0.3480 0.4275 0.3980 -0.0885 -0.1430 0.0177  649 ASP D C   
19113 O O   . ASP D 657 ? 0.3714 0.4327 0.4039 -0.0946 -0.1503 0.0143  649 ASP D O   
19114 C CB  . ASP D 657 ? 0.3836 0.5067 0.4772 -0.0966 -0.1458 0.0297  649 ASP D CB  
19115 C CG  . ASP D 657 ? 0.5182 0.6650 0.6337 -0.0993 -0.1515 0.0359  649 ASP D CG  
19116 O OD1 . ASP D 657 ? 0.5718 0.7217 0.6875 -0.0939 -0.1557 0.0359  649 ASP D OD1 
19117 O OD2 . ASP D 657 ? 0.4942 0.6546 0.6254 -0.1058 -0.1501 0.0406  649 ASP D OD2 
19118 N N   . ASN D 658 ? 0.2520 0.3279 0.3004 -0.0815 -0.1315 0.0158  650 ASN D N   
19119 C CA  . ASN D 658 ? 0.3118 0.3632 0.3395 -0.0809 -0.1275 0.0099  650 ASN D CA  
19120 C C   . ASN D 658 ? 0.3290 0.3641 0.3371 -0.0756 -0.1292 0.0049  650 ASN D C   
19121 O O   . ASN D 658 ? 0.3527 0.3668 0.3416 -0.0788 -0.1315 0.0001  650 ASN D O   
19122 C CB  . ASN D 658 ? 0.3584 0.4105 0.3898 -0.0745 -0.1155 0.0095  650 ASN D CB  
19123 C CG  . ASN D 658 ? 0.3617 0.3899 0.3745 -0.0743 -0.1118 0.0041  650 ASN D CG  
19124 O OD1 . ASN D 658 ? 0.3825 0.3957 0.3834 -0.0816 -0.1176 0.0015  650 ASN D OD1 
19125 N ND2 . ASN D 658 ? 0.3127 0.3368 0.3229 -0.0657 -0.1026 0.0023  650 ASN D ND2 
19126 N N   . VAL D 659 ? 0.3114 0.3554 0.3236 -0.0673 -0.1278 0.0061  651 VAL D N   
19127 C CA  . VAL D 659 ? 0.3314 0.3615 0.3254 -0.0627 -0.1294 0.0024  651 VAL D CA  
19128 C C   . VAL D 659 ? 0.3454 0.3677 0.3282 -0.0705 -0.1412 0.0016  651 VAL D C   
19129 O O   . VAL D 659 ? 0.3477 0.3501 0.3087 -0.0712 -0.1426 -0.0034 651 VAL D O   
19130 C CB  . VAL D 659 ? 0.2514 0.2933 0.2534 -0.0529 -0.1266 0.0049  651 VAL D CB  
19131 C CG1 . VAL D 659 ? 0.2816 0.3098 0.2647 -0.0493 -0.1289 0.0020  651 VAL D CG1 
19132 C CG2 . VAL D 659 ? 0.2351 0.2814 0.2450 -0.0451 -0.1154 0.0051  651 VAL D CG2 
19133 N N   . VAL D 660 ? 0.3287 0.3667 0.3260 -0.0765 -0.1499 0.0064  652 VAL D N   
19134 C CA  . VAL D 660 ? 0.3277 0.3583 0.3151 -0.0841 -0.1610 0.0060  652 VAL D CA  
19135 C C   . VAL D 660 ? 0.3685 0.3785 0.3397 -0.0913 -0.1618 0.0014  652 VAL D C   
19136 O O   . VAL D 660 ? 0.3508 0.3420 0.3009 -0.0923 -0.1645 -0.0029 652 VAL D O   
19137 C CB  . VAL D 660 ? 0.3198 0.3721 0.3296 -0.0877 -0.1662 0.0124  652 VAL D CB  
19138 C CG1 . VAL D 660 ? 0.3248 0.3674 0.3247 -0.0951 -0.1745 0.0118  652 VAL D CG1 
19139 C CG2 . VAL D 660 ? 0.3274 0.3972 0.3507 -0.0794 -0.1659 0.0162  652 VAL D CG2 
19140 N N   . ASP D 661 ? 0.3367 0.3497 0.3174 -0.0962 -0.1594 0.0025  653 ASP D N   
19141 C CA  . ASP D 661 ? 0.3990 0.3920 0.3655 -0.1026 -0.1601 -0.0014 653 ASP D CA  
19142 C C   . ASP D 661 ? 0.4013 0.3708 0.3441 -0.0975 -0.1552 -0.0088 653 ASP D C   
19143 O O   . ASP D 661 ? 0.3872 0.3361 0.3110 -0.0998 -0.1570 -0.0136 653 ASP D O   
19144 C CB  . ASP D 661 ? 0.4701 0.4713 0.4518 -0.1082 -0.1574 0.0018  653 ASP D CB  
19145 C CG  . ASP D 661 ? 0.6081 0.6313 0.6122 -0.1145 -0.1617 0.0091  653 ASP D CG  
19146 O OD1 . ASP D 661 ? 0.6206 0.6461 0.6246 -0.1170 -0.1686 0.0106  653 ASP D OD1 
19147 O OD2 . ASP D 661 ? 0.6542 0.6926 0.6763 -0.1169 -0.1579 0.0135  653 ASP D OD2 
19148 N N   . THR D 662 ? 0.3754 0.3481 0.3205 -0.0882 -0.1459 -0.0096 654 THR D N   
19149 C CA  . THR D 662 ? 0.4072 0.3602 0.3330 -0.0816 -0.1387 -0.0159 654 THR D CA  
19150 C C   . THR D 662 ? 0.3579 0.2990 0.2638 -0.0799 -0.1431 -0.0195 654 THR D C   
19151 O O   . THR D 662 ? 0.3759 0.2957 0.2605 -0.0797 -0.1425 -0.0256 654 THR D O   
19152 C CB  . THR D 662 ? 0.3830 0.3444 0.3181 -0.0713 -0.1270 -0.0149 654 THR D CB  
19153 O OG1 . THR D 662 ? 0.3991 0.3691 0.3496 -0.0731 -0.1226 -0.0121 654 THR D OG1 
19154 C CG2 . THR D 662 ? 0.3193 0.2623 0.2364 -0.0644 -0.1196 -0.0207 654 THR D CG2 
19155 N N   . VAL D 663 ? 0.3382 0.2926 0.2503 -0.0783 -0.1475 -0.0156 655 VAL D N   
19156 C CA  . VAL D 663 ? 0.4105 0.3546 0.3039 -0.0768 -0.1513 -0.0180 655 VAL D CA  
19157 C C   . VAL D 663 ? 0.4423 0.3724 0.3230 -0.0837 -0.1567 -0.0206 655 VAL D C   
19158 O O   . VAL D 663 ? 0.4349 0.3459 0.2932 -0.0822 -0.1552 -0.0260 655 VAL D O   
19159 C CB  . VAL D 663 ? 0.3885 0.3505 0.2939 -0.0741 -0.1552 -0.0124 655 VAL D CB  
19160 C CG1 . VAL D 663 ? 0.3649 0.3173 0.2535 -0.0748 -0.1598 -0.0136 655 VAL D CG1 
19161 C CG2 . VAL D 663 ? 0.4050 0.3755 0.3174 -0.0643 -0.1470 -0.0108 655 VAL D CG2 
19162 N N   . LYS D 664 ? 0.4344 0.3741 0.3294 -0.0911 -0.1628 -0.0166 656 LYS D N   
19163 C CA  . LYS D 664 ? 0.5037 0.4302 0.3875 -0.0981 -0.1690 -0.0184 656 LYS D CA  
19164 C C   . LYS D 664 ? 0.4918 0.3959 0.3587 -0.0986 -0.1650 -0.0248 656 LYS D C   
19165 O O   . LYS D 664 ? 0.5095 0.3956 0.3578 -0.1007 -0.1678 -0.0288 656 LYS D O   
19166 C CB  . LYS D 664 ? 0.5068 0.4492 0.4113 -0.1061 -0.1759 -0.0121 656 LYS D CB  
19167 C CG  . LYS D 664 ? 0.5487 0.5118 0.4689 -0.1053 -0.1808 -0.0061 656 LYS D CG  
19168 C CD  . LYS D 664 ? 0.5938 0.5791 0.5412 -0.1106 -0.1837 0.0007  656 LYS D CD  
19169 C CE  . LYS D 664 ? 0.6592 0.6454 0.6091 -0.1188 -0.1934 0.0037  656 LYS D CE  
19170 N NZ  . LYS D 664 ? 0.6589 0.6680 0.6364 -0.1239 -0.1953 0.0107  656 LYS D NZ  
19171 N N   . SER D 665 ? 0.5005 0.4047 0.3733 -0.0962 -0.1582 -0.0259 657 SER D N   
19172 C CA  . SER D 665 ? 0.4920 0.3756 0.3511 -0.0961 -0.1542 -0.0316 657 SER D CA  
19173 C C   . SER D 665 ? 0.5020 0.3663 0.3368 -0.0892 -0.1494 -0.0386 657 SER D C   
19174 O O   . SER D 665 ? 0.5009 0.3458 0.3209 -0.0893 -0.1479 -0.0438 657 SER D O   
19175 C CB  . SER D 665 ? 0.4193 0.3078 0.2907 -0.0946 -0.1480 -0.0308 657 SER D CB  
19176 O OG  . SER D 665 ? 0.4305 0.3199 0.2990 -0.0859 -0.1409 -0.0329 657 SER D OG  
19177 N N   . VAL D 666 ? 0.4621 0.3313 0.2925 -0.0830 -0.1466 -0.0386 658 VAL D N   
19178 C CA  . VAL D 666 ? 0.4974 0.3501 0.3052 -0.0764 -0.1408 -0.0447 658 VAL D CA  
19179 C C   . VAL D 666 ? 0.6164 0.4629 0.4093 -0.0782 -0.1462 -0.0453 658 VAL D C   
19180 O O   . VAL D 666 ? 0.6109 0.4455 0.3846 -0.0730 -0.1416 -0.0497 658 VAL D O   
19181 C CB  . VAL D 666 ? 0.4698 0.3289 0.2792 -0.0680 -0.1332 -0.0446 658 VAL D CB  
19182 C CG1 . VAL D 666 ? 0.4866 0.3511 0.3103 -0.0664 -0.1285 -0.0439 658 VAL D CG1 
19183 C CG2 . VAL D 666 ? 0.4562 0.3323 0.2739 -0.0674 -0.1371 -0.0390 658 VAL D CG2 
19184 N N   . LEU D 667 ? 0.5773 0.4319 0.3786 -0.0854 -0.1557 -0.0409 659 LEU D N   
19185 C CA  . LEU D 667 ? 0.6603 0.5089 0.4482 -0.0880 -0.1621 -0.0409 659 LEU D CA  
19186 C C   . LEU D 667 ? 0.6622 0.4932 0.4377 -0.0937 -0.1672 -0.0443 659 LEU D C   
19187 O O   . LEU D 667 ? 0.6451 0.4722 0.4266 -0.0969 -0.1670 -0.0450 659 LEU D O   
19188 C CB  . LEU D 667 ? 0.6224 0.4913 0.4279 -0.0917 -0.1700 -0.0335 659 LEU D CB  
19189 C CG  . LEU D 667 ? 0.6184 0.5043 0.4359 -0.0855 -0.1659 -0.0298 659 LEU D CG  
19190 C CD1 . LEU D 667 ? 0.6312 0.5380 0.4692 -0.0888 -0.1735 -0.0224 659 LEU D CD1 
19191 C CD2 . LEU D 667 ? 0.6059 0.4822 0.4033 -0.0791 -0.1612 -0.0328 659 LEU D CD2 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -7  ?   ?   ?   A . n 
A 1 2   ALA 2   -6  ?   ?   ?   A . n 
A 1 3   HIS 3   -5  ?   ?   ?   A . n 
A 1 4   HIS 4   -4  ?   ?   ?   A . n 
A 1 5   HIS 5   -3  ?   ?   ?   A . n 
A 1 6   HIS 6   -2  ?   ?   ?   A . n 
A 1 7   HIS 7   -1  ?   ?   ?   A . n 
A 1 8   HIS 8   0   ?   ?   ?   A . n 
A 1 9   MET 9   1   ?   ?   ?   A . n 
A 1 10  SER 10  2   2   SER SER A . n 
A 1 11  GLN 11  3   3   GLN GLN A . n 
A 1 12  LEU 12  4   4   LEU LEU A . n 
A 1 13  ALA 13  5   5   ALA ALA A . n 
A 1 14  ASN 14  6   6   ASN ASN A . n 
A 1 15  VAL 15  7   7   VAL VAL A . n 
A 1 16  ILE 16  8   8   ILE ILE A . n 
A 1 17  ARG 17  9   9   ARG ARG A . n 
A 1 18  PHE 18  10  10  PHE PHE A . n 
A 1 19  LEU 19  11  11  LEU LEU A . n 
A 1 20  SER 20  12  12  SER SER A . n 
A 1 21  ALA 21  13  13  ALA ALA A . n 
A 1 22  ASP 22  14  14  ASP ASP A . n 
A 1 23  ALA 23  15  15  ALA ALA A . n 
A 1 24  VAL 24  16  16  VAL VAL A . n 
A 1 25  GLN 25  17  17  GLN GLN A . n 
A 1 26  LYS 26  18  18  LYS LYS A . n 
A 1 27  ALA 27  19  19  ALA ALA A . n 
A 1 28  ASN 28  20  20  ASN ASN A . n 
A 1 29  SER 29  21  21  SER SER A . n 
A 1 30  GLY 30  22  22  GLY GLY A . n 
A 1 31  HIS 31  23  23  HIS HIS A . n 
A 1 32  PRO 32  24  24  PRO PRO A . n 
A 1 33  GLY 33  25  25  GLY GLY A . n 
A 1 34  ALA 34  26  26  ALA ALA A . n 
A 1 35  PRO 35  27  27  PRO PRO A . n 
A 1 36  MET 36  28  28  MET MET A . n 
A 1 37  GLY 37  29  29  GLY GLY A . n 
A 1 38  MET 38  30  30  MET MET A . n 
A 1 39  ALA 39  31  31  ALA ALA A . n 
A 1 40  GLU 40  32  32  GLU GLU A . n 
A 1 41  MET 41  33  33  MET MET A . n 
A 1 42  ALA 42  34  34  ALA ALA A . n 
A 1 43  GLU 43  35  35  GLU GLU A . n 
A 1 44  THR 44  36  36  THR THR A . n 
A 1 45  LEU 45  37  37  LEU LEU A . n 
A 1 46  TRP 46  38  38  TRP TRP A . n 
A 1 47  THR 47  39  39  THR THR A . n 
A 1 48  LYS 48  40  40  LYS LYS A . n 
A 1 49  PHE 49  41  41  PHE PHE A . n 
A 1 50  LEU 50  42  42  LEU LEU A . n 
A 1 51  ASN 51  43  43  ASN ASN A . n 
A 1 52  HIS 52  44  44  HIS HIS A . n 
A 1 53  ASN 53  45  45  ASN ASN A . n 
A 1 54  PRO 54  46  46  PRO PRO A . n 
A 1 55  ALA 55  47  47  ALA ALA A . n 
A 1 56  ASN 56  48  48  ASN ASN A . n 
A 1 57  PRO 57  49  49  PRO PRO A . n 
A 1 58  LYS 58  50  50  LYS LYS A . n 
A 1 59  PHE 59  51  51  PHE PHE A . n 
A 1 60  TYR 60  52  52  TYR TYR A . n 
A 1 61  ASN 61  53  53  ASN ASN A . n 
A 1 62  ARG 62  54  54  ARG ARG A . n 
A 1 63  ASP 63  55  55  ASP ASP A . n 
A 1 64  ARG 64  56  56  ARG ARG A . n 
A 1 65  PHE 65  57  57  PHE PHE A . n 
A 1 66  VAL 66  58  58  VAL VAL A . n 
A 1 67  LEU 67  59  59  LEU LEU A . n 
A 1 68  SER 68  60  60  SER SER A . n 
A 1 69  ASN 69  61  61  ASN ASN A . n 
A 1 70  GLY 70  62  62  GLY GLY A . n 
A 1 71  HIS 71  63  63  HIS HIS A . n 
A 1 72  ALA 72  64  64  ALA ALA A . n 
A 1 73  SER 73  65  65  SER SER A . n 
A 1 74  MET 74  66  66  MET MET A . n 
A 1 75  LEU 75  67  67  LEU LEU A . n 
A 1 76  LEU 76  68  68  LEU LEU A . n 
A 1 77  TYR 77  69  69  TYR TYR A . n 
A 1 78  SER 78  70  70  SER SER A . n 
A 1 79  LEU 79  71  71  LEU LEU A . n 
A 1 80  LEU 80  72  72  LEU LEU A . n 
A 1 81  HIS 81  73  73  HIS HIS A . n 
A 1 82  LEU 82  74  74  LEU LEU A . n 
A 1 83  THR 83  75  75  THR THR A . n 
A 1 84  GLY 84  76  76  GLY GLY A . n 
A 1 85  TYR 85  77  77  TYR TYR A . n 
A 1 86  ASN 86  78  78  ASN ASN A . n 
A 1 87  LEU 87  79  79  LEU LEU A . n 
A 1 88  SER 88  80  80  SER SER A . n 
A 1 89  ILE 89  81  81  ILE ILE A . n 
A 1 90  GLU 90  82  82  GLU GLU A . n 
A 1 91  ASP 91  83  83  ASP ASP A . n 
A 1 92  LEU 92  84  84  LEU LEU A . n 
A 1 93  LYS 93  85  85  LYS LYS A . n 
A 1 94  ASN 94  86  86  ASN ASN A . n 
A 1 95  PHE 95  87  87  PHE PHE A . n 
A 1 96  ARG 96  88  88  ARG ARG A . n 
A 1 97  GLN 97  89  89  GLN GLN A . n 
A 1 98  LEU 98  90  90  LEU LEU A . n 
A 1 99  HIS 99  91  91  HIS HIS A . n 
A 1 100 SER 100 92  92  SER SER A . n 
A 1 101 LYS 101 93  93  LYS LYS A . n 
A 1 102 THR 102 94  94  THR THR A . n 
A 1 103 PRO 103 95  95  PRO PRO A . n 
A 1 104 GLY 104 96  96  GLY GLY A . n 
A 1 105 HIS 105 97  97  HIS HIS A . n 
A 1 106 PRO 106 98  98  PRO PRO A . n 
A 1 107 GLU 107 99  99  GLU GLU A . n 
A 1 108 TYR 108 100 100 TYR TYR A . n 
A 1 109 GLY 109 101 101 GLY GLY A . n 
A 1 110 TYR 110 102 102 TYR TYR A . n 
A 1 111 THR 111 103 103 THR THR A . n 
A 1 112 ASP 112 104 104 ASP ASP A . n 
A 1 113 GLY 113 105 105 GLY GLY A . n 
A 1 114 VAL 114 106 106 VAL VAL A . n 
A 1 115 GLU 115 107 107 GLU GLU A . n 
A 1 116 THR 116 108 108 THR THR A . n 
A 1 117 THR 117 109 109 THR THR A . n 
A 1 118 THR 118 110 110 THR THR A . n 
A 1 119 GLY 119 111 111 GLY GLY A . n 
A 1 120 PRO 120 112 112 PRO PRO A . n 
A 1 121 LEU 121 113 113 LEU LEU A . n 
A 1 122 GLY 122 114 114 GLY GLY A . n 
A 1 123 GLN 123 115 115 GLN GLN A . n 
A 1 124 GLY 124 116 116 GLY GLY A . n 
A 1 125 ILE 125 117 117 ILE ILE A . n 
A 1 126 ALA 126 118 118 ALA ALA A . n 
A 1 127 ASN 127 119 119 ASN ASN A . n 
A 1 128 ALA 128 120 120 ALA ALA A . n 
A 1 129 VAL 129 121 121 VAL VAL A . n 
A 1 130 GLY 130 122 122 GLY GLY A . n 
A 1 131 MET 131 123 123 MET MET A . n 
A 1 132 ALA 132 124 124 ALA ALA A . n 
A 1 133 LEU 133 125 125 LEU LEU A . n 
A 1 134 ALA 134 126 126 ALA ALA A . n 
A 1 135 GLU 135 127 127 GLU GLU A . n 
A 1 136 LYS 136 128 128 LYS LYS A . n 
A 1 137 ILE 137 129 129 ILE ILE A . n 
A 1 138 LEU 138 130 130 LEU LEU A . n 
A 1 139 ALA 139 131 131 ALA ALA A . n 
A 1 140 ALA 140 132 132 ALA ALA A . n 
A 1 141 GLU 141 133 133 GLU GLU A . n 
A 1 142 PHE 142 134 134 PHE PHE A . n 
A 1 143 ASN 143 135 135 ASN ASN A . n 
A 1 144 LYS 144 136 136 LYS LYS A . n 
A 1 145 ASP 145 137 137 ASP ASP A . n 
A 1 146 GLY 146 138 138 GLY GLY A . n 
A 1 147 LEU 147 139 139 LEU LEU A . n 
A 1 148 ASN 148 140 140 ASN ASN A . n 
A 1 149 ILE 149 141 141 ILE ILE A . n 
A 1 150 VAL 150 142 142 VAL VAL A . n 
A 1 151 ASP 151 143 143 ASP ASP A . n 
A 1 152 HIS 152 144 144 HIS HIS A . n 
A 1 153 TYR 153 145 145 TYR TYR A . n 
A 1 154 THR 154 146 146 THR THR A . n 
A 1 155 TYR 155 147 147 TYR TYR A . n 
A 1 156 VAL 156 148 148 VAL VAL A . n 
A 1 157 PHE 157 149 149 PHE PHE A . n 
A 1 158 MET 158 150 150 MET MET A . n 
A 1 159 GLY 159 151 151 GLY GLY A . n 
A 1 160 ASP 160 152 152 ASP ASP A . n 
A 1 161 GLY 161 153 153 GLY GLY A . n 
A 1 162 OCS 162 154 154 OCS OCS A . n 
A 1 163 LEU 163 155 155 LEU LEU A . n 
A 1 164 MET 164 156 156 MET MET A . n 
A 1 165 GLU 165 157 157 GLU GLU A . n 
A 1 166 GLY 166 158 158 GLY GLY A . n 
A 1 167 VAL 167 159 159 VAL VAL A . n 
A 1 168 SER 168 160 160 SER SER A . n 
A 1 169 HIS 169 161 161 HIS HIS A . n 
A 1 170 GLU 170 162 162 GLU GLU A . n 
A 1 171 ALA 171 163 163 ALA ALA A . n 
A 1 172 CYS 172 164 164 CYS CYS A . n 
A 1 173 SER 173 165 165 SER SER A . n 
A 1 174 LEU 174 166 166 LEU LEU A . n 
A 1 175 ALA 175 167 167 ALA ALA A . n 
A 1 176 GLY 176 168 168 GLY GLY A . n 
A 1 177 THR 177 169 169 THR THR A . n 
A 1 178 LEU 178 170 170 LEU LEU A . n 
A 1 179 GLY 179 171 171 GLY GLY A . n 
A 1 180 LEU 180 172 172 LEU LEU A . n 
A 1 181 GLY 181 173 173 GLY GLY A . n 
A 1 182 LYS 182 174 174 LYS LYS A . n 
A 1 183 LEU 183 175 175 LEU LEU A . n 
A 1 184 ILE 184 176 176 ILE ILE A . n 
A 1 185 VAL 185 177 177 VAL VAL A . n 
A 1 186 LEU 186 178 178 LEU LEU A . n 
A 1 187 TYR 187 179 179 TYR TYR A . n 
A 1 188 ASP 188 180 180 ASP ASP A . n 
A 1 189 ASP 189 181 181 ASP ASP A . n 
A 1 190 ASN 190 182 182 ASN ASN A . n 
A 1 191 ASN 191 183 183 ASN ASN A . n 
A 1 192 ILE 192 184 184 ILE ILE A . n 
A 1 193 SER 193 185 ?   ?   ?   A . n 
A 1 194 ILE 194 186 ?   ?   ?   A . n 
A 1 195 ASP 195 187 ?   ?   ?   A . n 
A 1 196 GLY 196 188 ?   ?   ?   A . n 
A 1 197 LYS 197 189 ?   ?   ?   A . n 
A 1 198 VAL 198 190 ?   ?   ?   A . n 
A 1 199 ASP 199 191 ?   ?   ?   A . n 
A 1 200 GLY 200 192 192 GLY GLY A . n 
A 1 201 TRP 201 193 193 TRP TRP A . n 
A 1 202 PHE 202 194 194 PHE PHE A . n 
A 1 203 THR 203 195 195 THR THR A . n 
A 1 204 GLU 204 196 196 GLU GLU A . n 
A 1 205 ASN 205 197 197 ASN ASN A . n 
A 1 206 ILE 206 198 198 ILE ILE A . n 
A 1 207 PRO 207 199 199 PRO PRO A . n 
A 1 208 GLN 208 200 200 GLN GLN A . n 
A 1 209 ARG 209 201 201 ARG ARG A . n 
A 1 210 PHE 210 202 202 PHE PHE A . n 
A 1 211 GLU 211 203 203 GLU GLU A . n 
A 1 212 SER 212 204 204 SER SER A . n 
A 1 213 TYR 213 205 205 TYR TYR A . n 
A 1 214 GLY 214 206 206 GLY GLY A . n 
A 1 215 TRP 215 207 207 TRP TRP A . n 
A 1 216 HIS 216 208 208 HIS HIS A . n 
A 1 217 VAL 217 209 209 VAL VAL A . n 
A 1 218 VAL 218 210 210 VAL VAL A . n 
A 1 219 PRO 219 211 211 PRO PRO A . n 
A 1 220 ASN 220 212 212 ASN ASN A . n 
A 1 221 VAL 221 213 213 VAL VAL A . n 
A 1 222 ASN 222 214 214 ASN ASN A . n 
A 1 223 GLY 223 215 215 GLY GLY A . n 
A 1 224 HIS 224 216 216 HIS HIS A . n 
A 1 225 ASP 225 217 217 ASP ASP A . n 
A 1 226 THR 226 218 218 THR THR A . n 
A 1 227 ALA 227 219 219 ALA ALA A . n 
A 1 228 ALA 228 220 220 ALA ALA A . n 
A 1 229 ILE 229 221 221 ILE ILE A . n 
A 1 230 GLN 230 222 222 GLN GLN A . n 
A 1 231 THR 231 223 223 THR THR A . n 
A 1 232 ALA 232 224 224 ALA ALA A . n 
A 1 233 ILE 233 225 225 ILE ILE A . n 
A 1 234 GLU 234 226 226 GLU GLU A . n 
A 1 235 ALA 235 227 227 ALA ALA A . n 
A 1 236 ALA 236 228 228 ALA ALA A . n 
A 1 237 ARG 237 229 229 ARG ARG A . n 
A 1 238 ALA 238 230 230 ALA ALA A . n 
A 1 239 GLU 239 231 231 GLU GLU A . n 
A 1 240 THR 240 232 232 THR THR A . n 
A 1 241 GLY 241 233 233 GLY GLY A . n 
A 1 242 LYS 242 234 234 LYS LYS A . n 
A 1 243 PRO 243 235 235 PRO PRO A . n 
A 1 244 SER 244 236 236 SER SER A . n 
A 1 245 ILE 245 237 237 ILE ILE A . n 
A 1 246 ILE 246 238 238 ILE ILE A . n 
A 1 247 CYS 247 239 239 CYS CYS A . n 
A 1 248 CYS 248 240 240 CYS CYS A . n 
A 1 249 LYS 249 241 241 LYS LYS A . n 
A 1 250 THR 250 242 242 THR THR A . n 
A 1 251 LEU 251 243 243 LEU LEU A . n 
A 1 252 ILE 252 244 ?   ?   ?   A . n 
A 1 253 GLY 253 245 ?   ?   ?   A . n 
A 1 254 LYS 254 246 ?   ?   ?   A . n 
A 1 255 GLY 255 247 ?   ?   ?   A . n 
A 1 256 SER 256 248 ?   ?   ?   A . n 
A 1 257 ALA 257 249 ?   ?   ?   A . n 
A 1 258 ASN 258 250 ?   ?   ?   A . n 
A 1 259 LYS 259 251 ?   ?   ?   A . n 
A 1 260 GLU 260 252 ?   ?   ?   A . n 
A 1 261 GLY 261 253 ?   ?   ?   A . n 
A 1 262 SER 262 254 ?   ?   ?   A . n 
A 1 263 HIS 263 255 ?   ?   ?   A . n 
A 1 264 LYS 264 256 ?   ?   ?   A . n 
A 1 265 THR 265 257 ?   ?   ?   A . n 
A 1 266 HIS 266 258 ?   ?   ?   A . n 
A 1 267 GLY 267 259 ?   ?   ?   A . n 
A 1 268 ALA 268 260 ?   ?   ?   A . n 
A 1 269 PRO 269 261 ?   ?   ?   A . n 
A 1 270 LEU 270 262 ?   ?   ?   A . n 
A 1 271 GLY 271 263 ?   ?   ?   A . n 
A 1 272 ALA 272 264 ?   ?   ?   A . n 
A 1 273 ASP 273 265 ?   ?   ?   A . n 
A 1 274 GLU 274 266 ?   ?   ?   A . n 
A 1 275 ILE 275 267 ?   ?   ?   A . n 
A 1 276 GLU 276 268 268 GLU GLU A . n 
A 1 277 ALA 277 269 269 ALA ALA A . n 
A 1 278 THR 278 270 270 THR THR A . n 
A 1 279 ARG 279 271 271 ARG ARG A . n 
A 1 280 LYS 280 272 272 LYS LYS A . n 
A 1 281 HIS 281 273 273 HIS HIS A . n 
A 1 282 LEU 282 274 274 LEU LEU A . n 
A 1 283 GLY 283 275 275 GLY GLY A . n 
A 1 284 TRP 284 276 276 TRP TRP A . n 
A 1 285 ALA 285 277 277 ALA ALA A . n 
A 1 286 TYR 286 278 278 TYR TYR A . n 
A 1 287 PRO 287 279 279 PRO PRO A . n 
A 1 288 ALA 288 280 280 ALA ALA A . n 
A 1 289 PHE 289 281 281 PHE PHE A . n 
A 1 290 GLU 290 282 282 GLU GLU A . n 
A 1 291 ILE 291 283 283 ILE ILE A . n 
A 1 292 PRO 292 284 284 PRO PRO A . n 
A 1 293 GLN 293 285 285 GLN GLN A . n 
A 1 294 GLU 294 286 286 GLU GLU A . n 
A 1 295 ILE 295 287 287 ILE ILE A . n 
A 1 296 TYR 296 288 288 TYR TYR A . n 
A 1 297 ASP 297 289 289 ASP ASP A . n 
A 1 298 ALA 298 290 290 ALA ALA A . n 
A 1 299 TRP 299 291 291 TRP TRP A . n 
A 1 300 ASN 300 292 292 ASN ASN A . n 
A 1 301 ALA 301 293 293 ALA ALA A . n 
A 1 302 LYS 302 294 294 LYS LYS A . n 
A 1 303 GLU 303 295 295 GLU GLU A . n 
A 1 304 LYS 304 296 296 LYS LYS A . n 
A 1 305 GLY 305 297 297 GLY GLY A . n 
A 1 306 ALA 306 298 298 ALA ALA A . n 
A 1 307 LYS 307 299 299 LYS LYS A . n 
A 1 308 LEU 308 300 300 LEU LEU A . n 
A 1 309 GLU 309 301 301 GLU GLU A . n 
A 1 310 ALA 310 302 302 ALA ALA A . n 
A 1 311 GLY 311 303 303 GLY GLY A . n 
A 1 312 TRP 312 304 304 TRP TRP A . n 
A 1 313 ASN 313 305 305 ASN ASN A . n 
A 1 314 GLU 314 306 306 GLU GLU A . n 
A 1 315 LEU 315 307 307 LEU LEU A . n 
A 1 316 PHE 316 308 308 PHE PHE A . n 
A 1 317 ALA 317 309 309 ALA ALA A . n 
A 1 318 GLN 318 310 310 GLN GLN A . n 
A 1 319 TYR 319 311 311 TYR TYR A . n 
A 1 320 GLN 320 312 312 GLN GLN A . n 
A 1 321 ALA 321 313 313 ALA ALA A . n 
A 1 322 LYS 322 314 314 LYS LYS A . n 
A 1 323 TYR 323 315 315 TYR TYR A . n 
A 1 324 PRO 324 316 316 PRO PRO A . n 
A 1 325 ALA 325 317 317 ALA ALA A . n 
A 1 326 GLU 326 318 318 GLU GLU A . n 
A 1 327 ALA 327 319 319 ALA ALA A . n 
A 1 328 ALA 328 320 320 ALA ALA A . n 
A 1 329 GLU 329 321 321 GLU GLU A . n 
A 1 330 PHE 330 322 322 PHE PHE A . n 
A 1 331 VAL 331 323 323 VAL VAL A . n 
A 1 332 ARG 332 324 324 ARG ARG A . n 
A 1 333 ARG 333 325 325 ARG ARG A . n 
A 1 334 MET 334 326 326 MET MET A . n 
A 1 335 ASP 335 327 327 ASP ASP A . n 
A 1 336 LYS 336 328 328 LYS LYS A . n 
A 1 337 LYS 337 329 329 LYS LYS A . n 
A 1 338 LEU 338 330 330 LEU LEU A . n 
A 1 339 PRO 339 331 331 PRO PRO A . n 
A 1 340 GLU 340 332 332 GLU GLU A . n 
A 1 341 ASN 341 333 333 ASN ASN A . n 
A 1 342 PHE 342 334 334 PHE PHE A . n 
A 1 343 ASP 343 335 335 ASP ASP A . n 
A 1 344 GLU 344 336 336 GLU GLU A . n 
A 1 345 TYR 345 337 337 TYR TYR A . n 
A 1 346 VAL 346 338 338 VAL VAL A . n 
A 1 347 GLN 347 339 339 GLN GLN A . n 
A 1 348 THR 348 340 340 THR THR A . n 
A 1 349 ALA 349 341 341 ALA ALA A . n 
A 1 350 LEU 350 342 342 LEU LEU A . n 
A 1 351 LYS 351 343 343 LYS LYS A . n 
A 1 352 GLU 352 344 344 GLU GLU A . n 
A 1 353 VAL 353 345 345 VAL VAL A . n 
A 1 354 CYS 354 346 346 CYS CYS A . n 
A 1 355 ALA 355 347 347 ALA ALA A . n 
A 1 356 LYS 356 348 348 LYS LYS A . n 
A 1 357 ALA 357 349 349 ALA ALA A . n 
A 1 358 GLU 358 350 350 GLU GLU A . n 
A 1 359 THR 359 351 351 THR THR A . n 
A 1 360 VAL 360 352 352 VAL VAL A . n 
A 1 361 ALA 361 353 353 ALA ALA A . n 
A 1 362 THR 362 354 354 THR THR A . n 
A 1 363 ARG 363 355 355 ARG ARG A . n 
A 1 364 LYS 364 356 356 LYS LYS A . n 
A 1 365 ALA 365 357 357 ALA ALA A . n 
A 1 366 SER 366 358 358 SER SER A . n 
A 1 367 GLN 367 359 359 GLN GLN A . n 
A 1 368 ASN 368 360 360 ASN ASN A . n 
A 1 369 SER 369 361 361 SER SER A . n 
A 1 370 ILE 370 362 362 ILE ILE A . n 
A 1 371 GLU 371 363 363 GLU GLU A . n 
A 1 372 ILE 372 364 364 ILE ILE A . n 
A 1 373 LEU 373 365 365 LEU LEU A . n 
A 1 374 ALA 374 366 366 ALA ALA A . n 
A 1 375 LYS 375 367 367 LYS LYS A . n 
A 1 376 GLU 376 368 368 GLU GLU A . n 
A 1 377 LEU 377 369 369 LEU LEU A . n 
A 1 378 PRO 378 370 370 PRO PRO A . n 
A 1 379 GLU 379 371 371 GLU GLU A . n 
A 1 380 LEU 380 372 372 LEU LEU A . n 
A 1 381 VAL 381 373 373 VAL VAL A . n 
A 1 382 GLY 382 374 374 GLY GLY A . n 
A 1 383 GLY 383 375 375 GLY GLY A . n 
A 1 384 SER 384 376 376 SER SER A . n 
A 1 385 ALA 385 377 377 ALA ALA A . n 
A 1 386 ASP 386 378 378 ASP ASP A . n 
A 1 387 LEU 387 379 379 LEU LEU A . n 
A 1 388 THR 388 380 380 THR THR A . n 
A 1 389 PRO 389 381 381 PRO PRO A . n 
A 1 390 SER 390 382 382 SER SER A . n 
A 1 391 ASN 391 383 383 ASN ASN A . n 
A 1 392 LEU 392 384 384 LEU LEU A . n 
A 1 393 THR 393 385 385 THR THR A . n 
A 1 394 ASP 394 386 386 ASP ASP A . n 
A 1 395 TRP 395 387 387 TRP TRP A . n 
A 1 396 SER 396 388 388 SER SER A . n 
A 1 397 ASN 397 389 389 ASN ASN A . n 
A 1 398 SER 398 390 390 SER SER A . n 
A 1 399 VAL 399 391 391 VAL VAL A . n 
A 1 400 SER 400 392 392 SER SER A . n 
A 1 401 VAL 401 393 393 VAL VAL A . n 
A 1 402 THR 402 394 394 THR THR A . n 
A 1 403 ARG 403 395 395 ARG ARG A . n 
A 1 404 ASP 404 396 396 ASP ASP A . n 
A 1 405 LYS 405 397 397 LYS LYS A . n 
A 1 406 GLY 406 398 398 GLY GLY A . n 
A 1 407 GLY 407 399 399 GLY GLY A . n 
A 1 408 ASN 408 400 400 ASN ASN A . n 
A 1 409 TYR 409 401 401 TYR TYR A . n 
A 1 410 ILE 410 402 402 ILE ILE A . n 
A 1 411 HIS 411 403 403 HIS HIS A . n 
A 1 412 TYR 412 404 404 TYR TYR A . n 
A 1 413 GLY 413 405 405 GLY GLY A . n 
A 1 414 VAL 414 406 406 VAL VAL A . n 
A 1 415 ARG 415 407 407 ARG ARG A . n 
A 1 416 GLU 416 408 408 GLU GLU A . n 
A 1 417 PHE 417 409 409 PHE PHE A . n 
A 1 418 GLY 418 410 410 GLY GLY A . n 
A 1 419 MET 419 411 411 MET MET A . n 
A 1 420 GLY 420 412 412 GLY GLY A . n 
A 1 421 ALA 421 413 413 ALA ALA A . n 
A 1 422 ILE 422 414 414 ILE ILE A . n 
A 1 423 MET 423 415 415 MET MET A . n 
A 1 424 ASN 424 416 416 ASN ASN A . n 
A 1 425 GLY 425 417 417 GLY GLY A . n 
A 1 426 LEU 426 418 418 LEU LEU A . n 
A 1 427 VAL 427 419 419 VAL VAL A . n 
A 1 428 LEU 428 420 420 LEU LEU A . n 
A 1 429 HIS 429 421 421 HIS HIS A . n 
A 1 430 GLY 430 422 422 GLY GLY A . n 
A 1 431 GLY 431 423 423 GLY GLY A . n 
A 1 432 VAL 432 424 424 VAL VAL A . n 
A 1 433 LYS 433 425 425 LYS LYS A . n 
A 1 434 PRO 434 426 426 PRO PRO A . n 
A 1 435 PHE 435 427 427 PHE PHE A . n 
A 1 436 GLY 436 428 428 GLY GLY A . n 
A 1 437 ALA 437 429 429 ALA ALA A . n 
A 1 438 THR 438 430 430 THR THR A . n 
A 1 439 PHE 439 431 431 PHE PHE A . n 
A 1 440 LEU 440 432 432 LEU LEU A . n 
A 1 441 MET 441 433 433 MET MET A . n 
A 1 442 PHE 442 434 434 PHE PHE A . n 
A 1 443 SER 443 435 435 SER SER A . n 
A 1 444 GLU 444 436 436 GLU GLU A . n 
A 1 445 TYR 445 437 437 TYR TYR A . n 
A 1 446 GLU 446 438 438 GLU GLU A . n 
A 1 447 ARG 447 439 439 ARG ARG A . n 
A 1 448 ASN 448 440 440 ASN ASN A . n 
A 1 449 ALA 449 441 441 ALA ALA A . n 
A 1 450 LEU 450 442 442 LEU LEU A . n 
A 1 451 ARG 451 443 443 ARG ARG A . n 
A 1 452 MET 452 444 444 MET MET A . n 
A 1 453 ALA 453 445 445 ALA ALA A . n 
A 1 454 ALA 454 446 446 ALA ALA A . n 
A 1 455 LEU 455 447 447 LEU LEU A . n 
A 1 456 MET 456 448 448 MET MET A . n 
A 1 457 LYS 457 449 449 LYS LYS A . n 
A 1 458 ILE 458 450 450 ILE ILE A . n 
A 1 459 ASN 459 451 451 ASN ASN A . n 
A 1 460 PRO 460 452 452 PRO PRO A . n 
A 1 461 VAL 461 453 453 VAL VAL A . n 
A 1 462 PHE 462 454 454 PHE PHE A . n 
A 1 463 VAL 463 455 455 VAL VAL A . n 
A 1 464 PHE 464 456 456 PHE PHE A . n 
A 1 465 THR 465 457 457 THR THR A . n 
A 1 466 HIS 466 458 458 HIS HIS A . n 
A 1 467 ASP 467 459 459 ASP ASP A . n 
A 1 468 SER 468 460 460 SER SER A . n 
A 1 469 ILE 469 461 461 ILE ILE A . n 
A 1 470 GLY 470 462 462 GLY GLY A . n 
A 1 471 LEU 471 463 463 LEU LEU A . n 
A 1 472 GLY 472 464 464 GLY GLY A . n 
A 1 473 GLU 473 465 465 GLU GLU A . n 
A 1 474 ASP 474 466 466 ASP ASP A . n 
A 1 475 GLY 475 467 467 GLY GLY A . n 
A 1 476 PRO 476 468 468 PRO PRO A . n 
A 1 477 THR 477 469 469 THR THR A . n 
A 1 478 HIS 478 470 470 HIS HIS A . n 
A 1 479 GLN 479 471 471 GLN GLN A . n 
A 1 480 PRO 480 472 472 PRO PRO A . n 
A 1 481 ILE 481 473 473 ILE ILE A . n 
A 1 482 GLU 482 474 474 GLU GLU A . n 
A 1 483 GLN 483 475 475 GLN GLN A . n 
A 1 484 THR 484 476 476 THR THR A . n 
A 1 485 ALA 485 477 477 ALA ALA A . n 
A 1 486 THR 486 478 478 THR THR A . n 
A 1 487 LEU 487 479 479 LEU LEU A . n 
A 1 488 ARG 488 480 480 ARG ARG A . n 
A 1 489 LEU 489 481 481 LEU LEU A . n 
A 1 490 ILE 490 482 482 ILE ILE A . n 
A 1 491 PRO 491 483 483 PRO PRO A . n 
A 1 492 ASN 492 484 484 ASN ASN A . n 
A 1 493 MET 493 485 485 MET MET A . n 
A 1 494 ASP 494 486 486 ASP ASP A . n 
A 1 495 VAL 495 487 487 VAL VAL A . n 
A 1 496 TRP 496 488 488 TRP TRP A . n 
A 1 497 ARG 497 489 489 ARG ARG A . n 
A 1 498 PRO 498 490 490 PRO PRO A . n 
A 1 499 CYS 499 491 491 CYS CYS A . n 
A 1 500 ASP 500 492 492 ASP ASP A . n 
A 1 501 THR 501 493 493 THR THR A . n 
A 1 502 ALA 502 494 494 ALA ALA A . n 
A 1 503 GLU 503 495 495 GLU GLU A . n 
A 1 504 SER 504 496 496 SER SER A . n 
A 1 505 LEU 505 497 497 LEU LEU A . n 
A 1 506 VAL 506 498 498 VAL VAL A . n 
A 1 507 ALA 507 499 499 ALA ALA A . n 
A 1 508 TRP 508 500 500 TRP TRP A . n 
A 1 509 ALA 509 501 501 ALA ALA A . n 
A 1 510 GLU 510 502 502 GLU GLU A . n 
A 1 511 ALA 511 503 503 ALA ALA A . n 
A 1 512 ALA 512 504 504 ALA ALA A . n 
A 1 513 LYS 513 505 505 LYS LYS A . n 
A 1 514 ALA 514 506 506 ALA ALA A . n 
A 1 515 GLU 515 507 507 GLU GLU A . n 
A 1 516 ASP 516 508 508 ASP ASP A . n 
A 1 517 HIS 517 509 509 HIS HIS A . n 
A 1 518 PRO 518 510 510 PRO PRO A . n 
A 1 519 SER 519 511 511 SER SER A . n 
A 1 520 CYS 520 512 512 CYS CYS A . n 
A 1 521 LEU 521 513 513 LEU LEU A . n 
A 1 522 ILE 522 514 514 ILE ILE A . n 
A 1 523 PHE 523 515 515 PHE PHE A . n 
A 1 524 SER 524 516 516 SER SER A . n 
A 1 525 ARG 525 517 517 ARG ARG A . n 
A 1 526 GLN 526 518 518 GLN GLN A . n 
A 1 527 ASN 527 519 519 ASN ASN A . n 
A 1 528 LEU 528 520 520 LEU LEU A . n 
A 1 529 LYS 529 521 521 LYS LYS A . n 
A 1 530 PHE 530 522 522 PHE PHE A . n 
A 1 531 GLN 531 523 523 GLN GLN A . n 
A 1 532 ALA 532 524 524 ALA ALA A . n 
A 1 533 ARG 533 525 525 ARG ARG A . n 
A 1 534 SER 534 526 526 SER SER A . n 
A 1 535 GLU 535 527 527 GLU GLU A . n 
A 1 536 GLN 536 528 528 GLN GLN A . n 
A 1 537 GLN 537 529 529 GLN GLN A . n 
A 1 538 LEU 538 530 530 LEU LEU A . n 
A 1 539 ASN 539 531 531 ASN ASN A . n 
A 1 540 ASP 540 532 532 ASP ASP A . n 
A 1 541 ILE 541 533 533 ILE ILE A . n 
A 1 542 LYS 542 534 534 LYS LYS A . n 
A 1 543 ARG 543 535 535 ARG ARG A . n 
A 1 544 GLY 544 536 536 GLY GLY A . n 
A 1 545 ALA 545 537 537 ALA ALA A . n 
A 1 546 TYR 546 538 538 TYR TYR A . n 
A 1 547 VAL 547 539 539 VAL VAL A . n 
A 1 548 ILE 548 540 540 ILE ILE A . n 
A 1 549 SER 549 541 541 SER SER A . n 
A 1 550 GLU 550 542 542 GLU GLU A . n 
A 1 551 ALA 551 543 543 ALA ALA A . n 
A 1 552 GLN 552 544 544 GLN GLN A . n 
A 1 553 GLY 553 545 545 GLY GLY A . n 
A 1 554 ASN 554 546 546 ASN ASN A . n 
A 1 555 ALA 555 547 547 ALA ALA A . n 
A 1 556 GLN 556 548 548 GLN GLN A . n 
A 1 557 ALA 557 549 549 ALA ALA A . n 
A 1 558 VAL 558 550 550 VAL VAL A . n 
A 1 559 ILE 559 551 551 ILE ILE A . n 
A 1 560 ILE 560 552 552 ILE ILE A . n 
A 1 561 ALA 561 553 553 ALA ALA A . n 
A 1 562 THR 562 554 554 THR THR A . n 
A 1 563 GLY 563 555 555 GLY GLY A . n 
A 1 564 SER 564 556 556 SER SER A . n 
A 1 565 GLU 565 557 557 GLU GLU A . n 
A 1 566 VAL 566 558 558 VAL VAL A . n 
A 1 567 GLY 567 559 559 GLY GLY A . n 
A 1 568 LEU 568 560 560 LEU LEU A . n 
A 1 569 ALA 569 561 561 ALA ALA A . n 
A 1 570 VAL 570 562 562 VAL VAL A . n 
A 1 571 GLU 571 563 563 GLU GLU A . n 
A 1 572 ALA 572 564 564 ALA ALA A . n 
A 1 573 GLN 573 565 565 GLN GLN A . n 
A 1 574 LYS 574 566 566 LYS LYS A . n 
A 1 575 VAL 575 567 567 VAL VAL A . n 
A 1 576 LEU 576 568 568 LEU LEU A . n 
A 1 577 ALA 577 569 569 ALA ALA A . n 
A 1 578 GLY 578 570 570 GLY GLY A . n 
A 1 579 GLN 579 571 571 GLN GLN A . n 
A 1 580 GLY 580 572 572 GLY GLY A . n 
A 1 581 ILE 581 573 573 ILE ILE A . n 
A 1 582 ALA 582 574 574 ALA ALA A . n 
A 1 583 VAL 583 575 575 VAL VAL A . n 
A 1 584 ARG 584 576 576 ARG ARG A . n 
A 1 585 VAL 585 577 577 VAL VAL A . n 
A 1 586 VAL 586 578 578 VAL VAL A . n 
A 1 587 SER 587 579 579 SER SER A . n 
A 1 588 MET 588 580 580 MET MET A . n 
A 1 589 PRO 589 581 581 PRO PRO A . n 
A 1 590 SER 590 582 582 SER SER A . n 
A 1 591 THR 591 583 583 THR THR A . n 
A 1 592 SER 592 584 584 SER SER A . n 
A 1 593 VAL 593 585 585 VAL VAL A . n 
A 1 594 PHE 594 586 586 PHE PHE A . n 
A 1 595 ASP 595 587 587 ASP ASP A . n 
A 1 596 ARG 596 588 588 ARG ARG A . n 
A 1 597 GLN 597 589 589 GLN GLN A . n 
A 1 598 ASP 598 590 590 ASP ASP A . n 
A 1 599 ALA 599 591 591 ALA ALA A . n 
A 1 600 ALA 600 592 592 ALA ALA A . n 
A 1 601 TYR 601 593 593 TYR TYR A . n 
A 1 602 GLN 602 594 594 GLN GLN A . n 
A 1 603 ALA 603 595 595 ALA ALA A . n 
A 1 604 ALA 604 596 596 ALA ALA A . n 
A 1 605 VAL 605 597 597 VAL VAL A . n 
A 1 606 LEU 606 598 598 LEU LEU A . n 
A 1 607 PRO 607 599 599 PRO PRO A . n 
A 1 608 GLU 608 600 600 GLU GLU A . n 
A 1 609 GLY 609 601 601 GLY GLY A . n 
A 1 610 LEU 610 602 602 LEU LEU A . n 
A 1 611 PRO 611 603 603 PRO PRO A . n 
A 1 612 ARG 612 604 604 ARG ARG A . n 
A 1 613 ILE 613 605 605 ILE ILE A . n 
A 1 614 ALA 614 606 606 ALA ALA A . n 
A 1 615 VAL 615 607 607 VAL VAL A . n 
A 1 616 GLU 616 608 608 GLU GLU A . n 
A 1 617 ALA 617 609 609 ALA ALA A . n 
A 1 618 GLY 618 610 610 GLY GLY A . n 
A 1 619 HIS 619 611 611 HIS HIS A . n 
A 1 620 THR 620 612 612 THR THR A . n 
A 1 621 ASN 621 613 613 ASN ASN A . n 
A 1 622 GLY 622 614 614 GLY GLY A . n 
A 1 623 TRP 623 615 615 TRP TRP A . n 
A 1 624 TYR 624 616 616 TYR TYR A . n 
A 1 625 LYS 625 617 617 LYS LYS A . n 
A 1 626 TYR 626 618 618 TYR TYR A . n 
A 1 627 VAL 627 619 619 VAL VAL A . n 
A 1 628 GLY 628 620 620 GLY GLY A . n 
A 1 629 LEU 629 621 621 LEU LEU A . n 
A 1 630 ASN 630 622 622 ASN ASN A . n 
A 1 631 GLY 631 623 623 GLY GLY A . n 
A 1 632 ALA 632 624 624 ALA ALA A . n 
A 1 633 VAL 633 625 625 VAL VAL A . n 
A 1 634 VAL 634 626 626 VAL VAL A . n 
A 1 635 GLY 635 627 627 GLY GLY A . n 
A 1 636 ILE 636 628 628 ILE ILE A . n 
A 1 637 ASN 637 629 629 ASN ASN A . n 
A 1 638 ARG 638 630 630 ARG ARG A . n 
A 1 639 PHE 639 631 631 PHE PHE A . n 
A 1 640 GLY 640 632 632 GLY GLY A . n 
A 1 641 GLU 641 633 633 GLU GLU A . n 
A 1 642 SER 642 634 634 SER SER A . n 
A 1 643 ALA 643 635 635 ALA ALA A . n 
A 1 644 PRO 644 636 636 PRO PRO A . n 
A 1 645 ALA 645 637 637 ALA ALA A . n 
A 1 646 ASP 646 638 638 ASP ASP A . n 
A 1 647 LEU 647 639 639 LEU LEU A . n 
A 1 648 LEU 648 640 640 LEU LEU A . n 
A 1 649 PHE 649 641 641 PHE PHE A . n 
A 1 650 LYS 650 642 642 LYS LYS A . n 
A 1 651 ALA 651 643 643 ALA ALA A . n 
A 1 652 PHE 652 644 644 PHE PHE A . n 
A 1 653 GLY 653 645 645 GLY GLY A . n 
A 1 654 PHE 654 646 646 PHE PHE A . n 
A 1 655 THR 655 647 647 THR THR A . n 
A 1 656 VAL 656 648 648 VAL VAL A . n 
A 1 657 ASP 657 649 649 ASP ASP A . n 
A 1 658 ASN 658 650 650 ASN ASN A . n 
A 1 659 VAL 659 651 651 VAL VAL A . n 
A 1 660 VAL 660 652 652 VAL VAL A . n 
A 1 661 ASP 661 653 653 ASP ASP A . n 
A 1 662 THR 662 654 654 THR THR A . n 
A 1 663 VAL 663 655 655 VAL VAL A . n 
A 1 664 LYS 664 656 656 LYS LYS A . n 
A 1 665 SER 665 657 657 SER SER A . n 
A 1 666 VAL 666 658 658 VAL VAL A . n 
A 1 667 LEU 667 659 659 LEU LEU A . n 
B 1 1   MET 1   -7  ?   ?   ?   B . n 
B 1 2   ALA 2   -6  ?   ?   ?   B . n 
B 1 3   HIS 3   -5  ?   ?   ?   B . n 
B 1 4   HIS 4   -4  ?   ?   ?   B . n 
B 1 5   HIS 5   -3  ?   ?   ?   B . n 
B 1 6   HIS 6   -2  ?   ?   ?   B . n 
B 1 7   HIS 7   -1  ?   ?   ?   B . n 
B 1 8   HIS 8   0   ?   ?   ?   B . n 
B 1 9   MET 9   1   ?   ?   ?   B . n 
B 1 10  SER 10  2   2   SER SER B . n 
B 1 11  GLN 11  3   3   GLN GLN B . n 
B 1 12  LEU 12  4   4   LEU LEU B . n 
B 1 13  ALA 13  5   5   ALA ALA B . n 
B 1 14  ASN 14  6   6   ASN ASN B . n 
B 1 15  VAL 15  7   7   VAL VAL B . n 
B 1 16  ILE 16  8   8   ILE ILE B . n 
B 1 17  ARG 17  9   9   ARG ARG B . n 
B 1 18  PHE 18  10  10  PHE PHE B . n 
B 1 19  LEU 19  11  11  LEU LEU B . n 
B 1 20  SER 20  12  12  SER SER B . n 
B 1 21  ALA 21  13  13  ALA ALA B . n 
B 1 22  ASP 22  14  14  ASP ASP B . n 
B 1 23  ALA 23  15  15  ALA ALA B . n 
B 1 24  VAL 24  16  16  VAL VAL B . n 
B 1 25  GLN 25  17  17  GLN GLN B . n 
B 1 26  LYS 26  18  18  LYS LYS B . n 
B 1 27  ALA 27  19  19  ALA ALA B . n 
B 1 28  ASN 28  20  20  ASN ASN B . n 
B 1 29  SER 29  21  21  SER SER B . n 
B 1 30  GLY 30  22  22  GLY GLY B . n 
B 1 31  HIS 31  23  23  HIS HIS B . n 
B 1 32  PRO 32  24  24  PRO PRO B . n 
B 1 33  GLY 33  25  25  GLY GLY B . n 
B 1 34  ALA 34  26  26  ALA ALA B . n 
B 1 35  PRO 35  27  27  PRO PRO B . n 
B 1 36  MET 36  28  28  MET MET B . n 
B 1 37  GLY 37  29  29  GLY GLY B . n 
B 1 38  MET 38  30  30  MET MET B . n 
B 1 39  ALA 39  31  31  ALA ALA B . n 
B 1 40  GLU 40  32  32  GLU GLU B . n 
B 1 41  MET 41  33  33  MET MET B . n 
B 1 42  ALA 42  34  34  ALA ALA B . n 
B 1 43  GLU 43  35  35  GLU GLU B . n 
B 1 44  THR 44  36  36  THR THR B . n 
B 1 45  LEU 45  37  37  LEU LEU B . n 
B 1 46  TRP 46  38  38  TRP TRP B . n 
B 1 47  THR 47  39  39  THR THR B . n 
B 1 48  LYS 48  40  40  LYS LYS B . n 
B 1 49  PHE 49  41  41  PHE PHE B . n 
B 1 50  LEU 50  42  42  LEU LEU B . n 
B 1 51  ASN 51  43  43  ASN ASN B . n 
B 1 52  HIS 52  44  44  HIS HIS B . n 
B 1 53  ASN 53  45  45  ASN ASN B . n 
B 1 54  PRO 54  46  46  PRO PRO B . n 
B 1 55  ALA 55  47  47  ALA ALA B . n 
B 1 56  ASN 56  48  48  ASN ASN B . n 
B 1 57  PRO 57  49  49  PRO PRO B . n 
B 1 58  LYS 58  50  50  LYS LYS B . n 
B 1 59  PHE 59  51  51  PHE PHE B . n 
B 1 60  TYR 60  52  52  TYR TYR B . n 
B 1 61  ASN 61  53  53  ASN ASN B . n 
B 1 62  ARG 62  54  54  ARG ARG B . n 
B 1 63  ASP 63  55  55  ASP ASP B . n 
B 1 64  ARG 64  56  56  ARG ARG B . n 
B 1 65  PHE 65  57  57  PHE PHE B . n 
B 1 66  VAL 66  58  58  VAL VAL B . n 
B 1 67  LEU 67  59  59  LEU LEU B . n 
B 1 68  SER 68  60  60  SER SER B . n 
B 1 69  ASN 69  61  61  ASN ASN B . n 
B 1 70  GLY 70  62  62  GLY GLY B . n 
B 1 71  HIS 71  63  63  HIS HIS B . n 
B 1 72  ALA 72  64  64  ALA ALA B . n 
B 1 73  SER 73  65  65  SER SER B . n 
B 1 74  MET 74  66  66  MET MET B . n 
B 1 75  LEU 75  67  67  LEU LEU B . n 
B 1 76  LEU 76  68  68  LEU LEU B . n 
B 1 77  TYR 77  69  69  TYR TYR B . n 
B 1 78  SER 78  70  70  SER SER B . n 
B 1 79  LEU 79  71  71  LEU LEU B . n 
B 1 80  LEU 80  72  72  LEU LEU B . n 
B 1 81  HIS 81  73  73  HIS HIS B . n 
B 1 82  LEU 82  74  74  LEU LEU B . n 
B 1 83  THR 83  75  75  THR THR B . n 
B 1 84  GLY 84  76  76  GLY GLY B . n 
B 1 85  TYR 85  77  77  TYR TYR B . n 
B 1 86  ASN 86  78  78  ASN ASN B . n 
B 1 87  LEU 87  79  79  LEU LEU B . n 
B 1 88  SER 88  80  80  SER SER B . n 
B 1 89  ILE 89  81  81  ILE ILE B . n 
B 1 90  GLU 90  82  82  GLU GLU B . n 
B 1 91  ASP 91  83  83  ASP ASP B . n 
B 1 92  LEU 92  84  84  LEU LEU B . n 
B 1 93  LYS 93  85  85  LYS LYS B . n 
B 1 94  ASN 94  86  86  ASN ASN B . n 
B 1 95  PHE 95  87  87  PHE PHE B . n 
B 1 96  ARG 96  88  88  ARG ARG B . n 
B 1 97  GLN 97  89  89  GLN GLN B . n 
B 1 98  LEU 98  90  90  LEU LEU B . n 
B 1 99  HIS 99  91  91  HIS HIS B . n 
B 1 100 SER 100 92  92  SER SER B . n 
B 1 101 LYS 101 93  93  LYS LYS B . n 
B 1 102 THR 102 94  94  THR THR B . n 
B 1 103 PRO 103 95  95  PRO PRO B . n 
B 1 104 GLY 104 96  96  GLY GLY B . n 
B 1 105 HIS 105 97  97  HIS HIS B . n 
B 1 106 PRO 106 98  98  PRO PRO B . n 
B 1 107 GLU 107 99  99  GLU GLU B . n 
B 1 108 TYR 108 100 100 TYR TYR B . n 
B 1 109 GLY 109 101 101 GLY GLY B . n 
B 1 110 TYR 110 102 102 TYR TYR B . n 
B 1 111 THR 111 103 103 THR THR B . n 
B 1 112 ASP 112 104 104 ASP ASP B . n 
B 1 113 GLY 113 105 105 GLY GLY B . n 
B 1 114 VAL 114 106 106 VAL VAL B . n 
B 1 115 GLU 115 107 107 GLU GLU B . n 
B 1 116 THR 116 108 108 THR THR B . n 
B 1 117 THR 117 109 109 THR THR B . n 
B 1 118 THR 118 110 110 THR THR B . n 
B 1 119 GLY 119 111 111 GLY GLY B . n 
B 1 120 PRO 120 112 112 PRO PRO B . n 
B 1 121 LEU 121 113 113 LEU LEU B . n 
B 1 122 GLY 122 114 114 GLY GLY B . n 
B 1 123 GLN 123 115 115 GLN GLN B . n 
B 1 124 GLY 124 116 116 GLY GLY B . n 
B 1 125 ILE 125 117 117 ILE ILE B . n 
B 1 126 ALA 126 118 118 ALA ALA B . n 
B 1 127 ASN 127 119 119 ASN ASN B . n 
B 1 128 ALA 128 120 120 ALA ALA B . n 
B 1 129 VAL 129 121 121 VAL VAL B . n 
B 1 130 GLY 130 122 122 GLY GLY B . n 
B 1 131 MET 131 123 123 MET MET B . n 
B 1 132 ALA 132 124 124 ALA ALA B . n 
B 1 133 LEU 133 125 125 LEU LEU B . n 
B 1 134 ALA 134 126 126 ALA ALA B . n 
B 1 135 GLU 135 127 127 GLU GLU B . n 
B 1 136 LYS 136 128 128 LYS LYS B . n 
B 1 137 ILE 137 129 129 ILE ILE B . n 
B 1 138 LEU 138 130 130 LEU LEU B . n 
B 1 139 ALA 139 131 131 ALA ALA B . n 
B 1 140 ALA 140 132 132 ALA ALA B . n 
B 1 141 GLU 141 133 133 GLU GLU B . n 
B 1 142 PHE 142 134 134 PHE PHE B . n 
B 1 143 ASN 143 135 135 ASN ASN B . n 
B 1 144 LYS 144 136 136 LYS LYS B . n 
B 1 145 ASP 145 137 137 ASP ASP B . n 
B 1 146 GLY 146 138 138 GLY GLY B . n 
B 1 147 LEU 147 139 139 LEU LEU B . n 
B 1 148 ASN 148 140 140 ASN ASN B . n 
B 1 149 ILE 149 141 141 ILE ILE B . n 
B 1 150 VAL 150 142 142 VAL VAL B . n 
B 1 151 ASP 151 143 143 ASP ASP B . n 
B 1 152 HIS 152 144 144 HIS HIS B . n 
B 1 153 TYR 153 145 145 TYR TYR B . n 
B 1 154 THR 154 146 146 THR THR B . n 
B 1 155 TYR 155 147 147 TYR TYR B . n 
B 1 156 VAL 156 148 148 VAL VAL B . n 
B 1 157 PHE 157 149 149 PHE PHE B . n 
B 1 158 MET 158 150 150 MET MET B . n 
B 1 159 GLY 159 151 151 GLY GLY B . n 
B 1 160 ASP 160 152 152 ASP ASP B . n 
B 1 161 GLY 161 153 153 GLY GLY B . n 
B 1 162 OCS 162 154 154 OCS OCS B . n 
B 1 163 LEU 163 155 155 LEU LEU B . n 
B 1 164 MET 164 156 156 MET MET B . n 
B 1 165 GLU 165 157 157 GLU GLU B . n 
B 1 166 GLY 166 158 158 GLY GLY B . n 
B 1 167 VAL 167 159 159 VAL VAL B . n 
B 1 168 SER 168 160 160 SER SER B . n 
B 1 169 HIS 169 161 161 HIS HIS B . n 
B 1 170 GLU 170 162 162 GLU GLU B . n 
B 1 171 ALA 171 163 163 ALA ALA B . n 
B 1 172 CYS 172 164 164 CYS CYS B . n 
B 1 173 SER 173 165 165 SER SER B . n 
B 1 174 LEU 174 166 166 LEU LEU B . n 
B 1 175 ALA 175 167 167 ALA ALA B . n 
B 1 176 GLY 176 168 168 GLY GLY B . n 
B 1 177 THR 177 169 169 THR THR B . n 
B 1 178 LEU 178 170 170 LEU LEU B . n 
B 1 179 GLY 179 171 171 GLY GLY B . n 
B 1 180 LEU 180 172 172 LEU LEU B . n 
B 1 181 GLY 181 173 173 GLY GLY B . n 
B 1 182 LYS 182 174 174 LYS LYS B . n 
B 1 183 LEU 183 175 175 LEU LEU B . n 
B 1 184 ILE 184 176 176 ILE ILE B . n 
B 1 185 VAL 185 177 177 VAL VAL B . n 
B 1 186 LEU 186 178 178 LEU LEU B . n 
B 1 187 TYR 187 179 179 TYR TYR B . n 
B 1 188 ASP 188 180 180 ASP ASP B . n 
B 1 189 ASP 189 181 181 ASP ASP B . n 
B 1 190 ASN 190 182 182 ASN ASN B . n 
B 1 191 ASN 191 183 183 ASN ASN B . n 
B 1 192 ILE 192 184 184 ILE ILE B . n 
B 1 193 SER 193 185 185 SER SER B . n 
B 1 194 ILE 194 186 186 ILE ILE B . n 
B 1 195 ASP 195 187 187 ASP ASP B . n 
B 1 196 GLY 196 188 188 GLY GLY B . n 
B 1 197 LYS 197 189 189 LYS LYS B . n 
B 1 198 VAL 198 190 190 VAL VAL B . n 
B 1 199 ASP 199 191 191 ASP ASP B . n 
B 1 200 GLY 200 192 192 GLY GLY B . n 
B 1 201 TRP 201 193 193 TRP TRP B . n 
B 1 202 PHE 202 194 194 PHE PHE B . n 
B 1 203 THR 203 195 195 THR THR B . n 
B 1 204 GLU 204 196 196 GLU GLU B . n 
B 1 205 ASN 205 197 197 ASN ASN B . n 
B 1 206 ILE 206 198 198 ILE ILE B . n 
B 1 207 PRO 207 199 199 PRO PRO B . n 
B 1 208 GLN 208 200 200 GLN GLN B . n 
B 1 209 ARG 209 201 201 ARG ARG B . n 
B 1 210 PHE 210 202 202 PHE PHE B . n 
B 1 211 GLU 211 203 203 GLU GLU B . n 
B 1 212 SER 212 204 204 SER SER B . n 
B 1 213 TYR 213 205 205 TYR TYR B . n 
B 1 214 GLY 214 206 206 GLY GLY B . n 
B 1 215 TRP 215 207 207 TRP TRP B . n 
B 1 216 HIS 216 208 208 HIS HIS B . n 
B 1 217 VAL 217 209 209 VAL VAL B . n 
B 1 218 VAL 218 210 210 VAL VAL B . n 
B 1 219 PRO 219 211 211 PRO PRO B . n 
B 1 220 ASN 220 212 212 ASN ASN B . n 
B 1 221 VAL 221 213 213 VAL VAL B . n 
B 1 222 ASN 222 214 214 ASN ASN B . n 
B 1 223 GLY 223 215 215 GLY GLY B . n 
B 1 224 HIS 224 216 216 HIS HIS B . n 
B 1 225 ASP 225 217 217 ASP ASP B . n 
B 1 226 THR 226 218 218 THR THR B . n 
B 1 227 ALA 227 219 219 ALA ALA B . n 
B 1 228 ALA 228 220 220 ALA ALA B . n 
B 1 229 ILE 229 221 221 ILE ILE B . n 
B 1 230 GLN 230 222 222 GLN GLN B . n 
B 1 231 THR 231 223 223 THR THR B . n 
B 1 232 ALA 232 224 224 ALA ALA B . n 
B 1 233 ILE 233 225 225 ILE ILE B . n 
B 1 234 GLU 234 226 226 GLU GLU B . n 
B 1 235 ALA 235 227 227 ALA ALA B . n 
B 1 236 ALA 236 228 228 ALA ALA B . n 
B 1 237 ARG 237 229 229 ARG ARG B . n 
B 1 238 ALA 238 230 230 ALA ALA B . n 
B 1 239 GLU 239 231 231 GLU GLU B . n 
B 1 240 THR 240 232 232 THR THR B . n 
B 1 241 GLY 241 233 233 GLY GLY B . n 
B 1 242 LYS 242 234 234 LYS LYS B . n 
B 1 243 PRO 243 235 235 PRO PRO B . n 
B 1 244 SER 244 236 236 SER SER B . n 
B 1 245 ILE 245 237 237 ILE ILE B . n 
B 1 246 ILE 246 238 238 ILE ILE B . n 
B 1 247 CYS 247 239 239 CYS CYS B . n 
B 1 248 CYS 248 240 240 CYS CYS B . n 
B 1 249 LYS 249 241 241 LYS LYS B . n 
B 1 250 THR 250 242 242 THR THR B . n 
B 1 251 LEU 251 243 243 LEU LEU B . n 
B 1 252 ILE 252 244 244 ILE ILE B . n 
B 1 253 GLY 253 245 245 GLY GLY B . n 
B 1 254 LYS 254 246 246 LYS LYS B . n 
B 1 255 GLY 255 247 247 GLY GLY B . n 
B 1 256 SER 256 248 248 SER SER B . n 
B 1 257 ALA 257 249 249 ALA ALA B . n 
B 1 258 ASN 258 250 250 ASN ASN B . n 
B 1 259 LYS 259 251 251 LYS LYS B . n 
B 1 260 GLU 260 252 252 GLU GLU B . n 
B 1 261 GLY 261 253 253 GLY GLY B . n 
B 1 262 SER 262 254 254 SER SER B . n 
B 1 263 HIS 263 255 255 HIS HIS B . n 
B 1 264 LYS 264 256 256 LYS LYS B . n 
B 1 265 THR 265 257 257 THR THR B . n 
B 1 266 HIS 266 258 258 HIS HIS B . n 
B 1 267 GLY 267 259 259 GLY GLY B . n 
B 1 268 ALA 268 260 260 ALA ALA B . n 
B 1 269 PRO 269 261 261 PRO PRO B . n 
B 1 270 LEU 270 262 262 LEU LEU B . n 
B 1 271 GLY 271 263 263 GLY GLY B . n 
B 1 272 ALA 272 264 264 ALA ALA B . n 
B 1 273 ASP 273 265 265 ASP ASP B . n 
B 1 274 GLU 274 266 266 GLU GLU B . n 
B 1 275 ILE 275 267 267 ILE ILE B . n 
B 1 276 GLU 276 268 268 GLU GLU B . n 
B 1 277 ALA 277 269 269 ALA ALA B . n 
B 1 278 THR 278 270 270 THR THR B . n 
B 1 279 ARG 279 271 271 ARG ARG B . n 
B 1 280 LYS 280 272 272 LYS LYS B . n 
B 1 281 HIS 281 273 273 HIS HIS B . n 
B 1 282 LEU 282 274 274 LEU LEU B . n 
B 1 283 GLY 283 275 275 GLY GLY B . n 
B 1 284 TRP 284 276 276 TRP TRP B . n 
B 1 285 ALA 285 277 277 ALA ALA B . n 
B 1 286 TYR 286 278 278 TYR TYR B . n 
B 1 287 PRO 287 279 279 PRO PRO B . n 
B 1 288 ALA 288 280 280 ALA ALA B . n 
B 1 289 PHE 289 281 281 PHE PHE B . n 
B 1 290 GLU 290 282 282 GLU GLU B . n 
B 1 291 ILE 291 283 283 ILE ILE B . n 
B 1 292 PRO 292 284 284 PRO PRO B . n 
B 1 293 GLN 293 285 285 GLN GLN B . n 
B 1 294 GLU 294 286 286 GLU GLU B . n 
B 1 295 ILE 295 287 287 ILE ILE B . n 
B 1 296 TYR 296 288 288 TYR TYR B . n 
B 1 297 ASP 297 289 289 ASP ASP B . n 
B 1 298 ALA 298 290 290 ALA ALA B . n 
B 1 299 TRP 299 291 291 TRP TRP B . n 
B 1 300 ASN 300 292 292 ASN ASN B . n 
B 1 301 ALA 301 293 293 ALA ALA B . n 
B 1 302 LYS 302 294 294 LYS LYS B . n 
B 1 303 GLU 303 295 295 GLU GLU B . n 
B 1 304 LYS 304 296 296 LYS LYS B . n 
B 1 305 GLY 305 297 297 GLY GLY B . n 
B 1 306 ALA 306 298 298 ALA ALA B . n 
B 1 307 LYS 307 299 299 LYS LYS B . n 
B 1 308 LEU 308 300 300 LEU LEU B . n 
B 1 309 GLU 309 301 301 GLU GLU B . n 
B 1 310 ALA 310 302 302 ALA ALA B . n 
B 1 311 GLY 311 303 303 GLY GLY B . n 
B 1 312 TRP 312 304 304 TRP TRP B . n 
B 1 313 ASN 313 305 305 ASN ASN B . n 
B 1 314 GLU 314 306 306 GLU GLU B . n 
B 1 315 LEU 315 307 307 LEU LEU B . n 
B 1 316 PHE 316 308 308 PHE PHE B . n 
B 1 317 ALA 317 309 309 ALA ALA B . n 
B 1 318 GLN 318 310 310 GLN GLN B . n 
B 1 319 TYR 319 311 311 TYR TYR B . n 
B 1 320 GLN 320 312 312 GLN GLN B . n 
B 1 321 ALA 321 313 313 ALA ALA B . n 
B 1 322 LYS 322 314 314 LYS LYS B . n 
B 1 323 TYR 323 315 315 TYR TYR B . n 
B 1 324 PRO 324 316 316 PRO PRO B . n 
B 1 325 ALA 325 317 317 ALA ALA B . n 
B 1 326 GLU 326 318 318 GLU GLU B . n 
B 1 327 ALA 327 319 319 ALA ALA B . n 
B 1 328 ALA 328 320 320 ALA ALA B . n 
B 1 329 GLU 329 321 321 GLU GLU B . n 
B 1 330 PHE 330 322 322 PHE PHE B . n 
B 1 331 VAL 331 323 323 VAL VAL B . n 
B 1 332 ARG 332 324 324 ARG ARG B . n 
B 1 333 ARG 333 325 325 ARG ARG B . n 
B 1 334 MET 334 326 326 MET MET B . n 
B 1 335 ASP 335 327 327 ASP ASP B . n 
B 1 336 LYS 336 328 328 LYS LYS B . n 
B 1 337 LYS 337 329 329 LYS LYS B . n 
B 1 338 LEU 338 330 330 LEU LEU B . n 
B 1 339 PRO 339 331 331 PRO PRO B . n 
B 1 340 GLU 340 332 332 GLU GLU B . n 
B 1 341 ASN 341 333 333 ASN ASN B . n 
B 1 342 PHE 342 334 334 PHE PHE B . n 
B 1 343 ASP 343 335 335 ASP ASP B . n 
B 1 344 GLU 344 336 336 GLU GLU B . n 
B 1 345 TYR 345 337 337 TYR TYR B . n 
B 1 346 VAL 346 338 338 VAL VAL B . n 
B 1 347 GLN 347 339 339 GLN GLN B . n 
B 1 348 THR 348 340 340 THR THR B . n 
B 1 349 ALA 349 341 341 ALA ALA B . n 
B 1 350 LEU 350 342 342 LEU LEU B . n 
B 1 351 LYS 351 343 343 LYS LYS B . n 
B 1 352 GLU 352 344 344 GLU GLU B . n 
B 1 353 VAL 353 345 345 VAL VAL B . n 
B 1 354 CYS 354 346 346 CYS CYS B . n 
B 1 355 ALA 355 347 347 ALA ALA B . n 
B 1 356 LYS 356 348 348 LYS LYS B . n 
B 1 357 ALA 357 349 ?   ?   ?   B . n 
B 1 358 GLU 358 350 ?   ?   ?   B . n 
B 1 359 THR 359 351 ?   ?   ?   B . n 
B 1 360 VAL 360 352 ?   ?   ?   B . n 
B 1 361 ALA 361 353 ?   ?   ?   B . n 
B 1 362 THR 362 354 ?   ?   ?   B . n 
B 1 363 ARG 363 355 ?   ?   ?   B . n 
B 1 364 LYS 364 356 ?   ?   ?   B . n 
B 1 365 ALA 365 357 ?   ?   ?   B . n 
B 1 366 SER 366 358 ?   ?   ?   B . n 
B 1 367 GLN 367 359 359 GLN GLN B . n 
B 1 368 ASN 368 360 360 ASN ASN B . n 
B 1 369 SER 369 361 361 SER SER B . n 
B 1 370 ILE 370 362 362 ILE ILE B . n 
B 1 371 GLU 371 363 363 GLU GLU B . n 
B 1 372 ILE 372 364 364 ILE ILE B . n 
B 1 373 LEU 373 365 365 LEU LEU B . n 
B 1 374 ALA 374 366 366 ALA ALA B . n 
B 1 375 LYS 375 367 367 LYS LYS B . n 
B 1 376 GLU 376 368 368 GLU GLU B . n 
B 1 377 LEU 377 369 369 LEU LEU B . n 
B 1 378 PRO 378 370 370 PRO PRO B . n 
B 1 379 GLU 379 371 371 GLU GLU B . n 
B 1 380 LEU 380 372 372 LEU LEU B . n 
B 1 381 VAL 381 373 373 VAL VAL B . n 
B 1 382 GLY 382 374 374 GLY GLY B . n 
B 1 383 GLY 383 375 375 GLY GLY B . n 
B 1 384 SER 384 376 376 SER SER B . n 
B 1 385 ALA 385 377 377 ALA ALA B . n 
B 1 386 ASP 386 378 378 ASP ASP B . n 
B 1 387 LEU 387 379 379 LEU LEU B . n 
B 1 388 THR 388 380 380 THR THR B . n 
B 1 389 PRO 389 381 381 PRO PRO B . n 
B 1 390 SER 390 382 382 SER SER B . n 
B 1 391 ASN 391 383 383 ASN ASN B . n 
B 1 392 LEU 392 384 384 LEU LEU B . n 
B 1 393 THR 393 385 385 THR THR B . n 
B 1 394 ASP 394 386 386 ASP ASP B . n 
B 1 395 TRP 395 387 387 TRP TRP B . n 
B 1 396 SER 396 388 388 SER SER B . n 
B 1 397 ASN 397 389 389 ASN ASN B . n 
B 1 398 SER 398 390 390 SER SER B . n 
B 1 399 VAL 399 391 391 VAL VAL B . n 
B 1 400 SER 400 392 392 SER SER B . n 
B 1 401 VAL 401 393 393 VAL VAL B . n 
B 1 402 THR 402 394 394 THR THR B . n 
B 1 403 ARG 403 395 395 ARG ARG B . n 
B 1 404 ASP 404 396 396 ASP ASP B . n 
B 1 405 LYS 405 397 397 LYS LYS B . n 
B 1 406 GLY 406 398 398 GLY GLY B . n 
B 1 407 GLY 407 399 399 GLY GLY B . n 
B 1 408 ASN 408 400 400 ASN ASN B . n 
B 1 409 TYR 409 401 401 TYR TYR B . n 
B 1 410 ILE 410 402 402 ILE ILE B . n 
B 1 411 HIS 411 403 403 HIS HIS B . n 
B 1 412 TYR 412 404 404 TYR TYR B . n 
B 1 413 GLY 413 405 405 GLY GLY B . n 
B 1 414 VAL 414 406 406 VAL VAL B . n 
B 1 415 ARG 415 407 407 ARG ARG B . n 
B 1 416 GLU 416 408 408 GLU GLU B . n 
B 1 417 PHE 417 409 409 PHE PHE B . n 
B 1 418 GLY 418 410 410 GLY GLY B . n 
B 1 419 MET 419 411 411 MET MET B . n 
B 1 420 GLY 420 412 412 GLY GLY B . n 
B 1 421 ALA 421 413 413 ALA ALA B . n 
B 1 422 ILE 422 414 414 ILE ILE B . n 
B 1 423 MET 423 415 415 MET MET B . n 
B 1 424 ASN 424 416 416 ASN ASN B . n 
B 1 425 GLY 425 417 417 GLY GLY B . n 
B 1 426 LEU 426 418 418 LEU LEU B . n 
B 1 427 VAL 427 419 419 VAL VAL B . n 
B 1 428 LEU 428 420 420 LEU LEU B . n 
B 1 429 HIS 429 421 421 HIS HIS B . n 
B 1 430 GLY 430 422 422 GLY GLY B . n 
B 1 431 GLY 431 423 423 GLY GLY B . n 
B 1 432 VAL 432 424 424 VAL VAL B . n 
B 1 433 LYS 433 425 425 LYS LYS B . n 
B 1 434 PRO 434 426 426 PRO PRO B . n 
B 1 435 PHE 435 427 427 PHE PHE B . n 
B 1 436 GLY 436 428 428 GLY GLY B . n 
B 1 437 ALA 437 429 429 ALA ALA B . n 
B 1 438 THR 438 430 430 THR THR B . n 
B 1 439 PHE 439 431 431 PHE PHE B . n 
B 1 440 LEU 440 432 432 LEU LEU B . n 
B 1 441 MET 441 433 433 MET MET B . n 
B 1 442 PHE 442 434 434 PHE PHE B . n 
B 1 443 SER 443 435 435 SER SER B . n 
B 1 444 GLU 444 436 436 GLU GLU B . n 
B 1 445 TYR 445 437 437 TYR TYR B . n 
B 1 446 GLU 446 438 438 GLU GLU B . n 
B 1 447 ARG 447 439 439 ARG ARG B . n 
B 1 448 ASN 448 440 440 ASN ASN B . n 
B 1 449 ALA 449 441 441 ALA ALA B . n 
B 1 450 LEU 450 442 442 LEU LEU B . n 
B 1 451 ARG 451 443 443 ARG ARG B . n 
B 1 452 MET 452 444 444 MET MET B . n 
B 1 453 ALA 453 445 445 ALA ALA B . n 
B 1 454 ALA 454 446 446 ALA ALA B . n 
B 1 455 LEU 455 447 447 LEU LEU B . n 
B 1 456 MET 456 448 448 MET MET B . n 
B 1 457 LYS 457 449 449 LYS LYS B . n 
B 1 458 ILE 458 450 450 ILE ILE B . n 
B 1 459 ASN 459 451 451 ASN ASN B . n 
B 1 460 PRO 460 452 452 PRO PRO B . n 
B 1 461 VAL 461 453 453 VAL VAL B . n 
B 1 462 PHE 462 454 454 PHE PHE B . n 
B 1 463 VAL 463 455 455 VAL VAL B . n 
B 1 464 PHE 464 456 456 PHE PHE B . n 
B 1 465 THR 465 457 457 THR THR B . n 
B 1 466 HIS 466 458 458 HIS HIS B . n 
B 1 467 ASP 467 459 459 ASP ASP B . n 
B 1 468 SER 468 460 460 SER SER B . n 
B 1 469 ILE 469 461 461 ILE ILE B . n 
B 1 470 GLY 470 462 462 GLY GLY B . n 
B 1 471 LEU 471 463 463 LEU LEU B . n 
B 1 472 GLY 472 464 464 GLY GLY B . n 
B 1 473 GLU 473 465 465 GLU GLU B . n 
B 1 474 ASP 474 466 466 ASP ASP B . n 
B 1 475 GLY 475 467 467 GLY GLY B . n 
B 1 476 PRO 476 468 468 PRO PRO B . n 
B 1 477 THR 477 469 469 THR THR B . n 
B 1 478 HIS 478 470 470 HIS HIS B . n 
B 1 479 GLN 479 471 471 GLN GLN B . n 
B 1 480 PRO 480 472 472 PRO PRO B . n 
B 1 481 ILE 481 473 473 ILE ILE B . n 
B 1 482 GLU 482 474 474 GLU GLU B . n 
B 1 483 GLN 483 475 475 GLN GLN B . n 
B 1 484 THR 484 476 476 THR THR B . n 
B 1 485 ALA 485 477 477 ALA ALA B . n 
B 1 486 THR 486 478 478 THR THR B . n 
B 1 487 LEU 487 479 479 LEU LEU B . n 
B 1 488 ARG 488 480 480 ARG ARG B . n 
B 1 489 LEU 489 481 481 LEU LEU B . n 
B 1 490 ILE 490 482 482 ILE ILE B . n 
B 1 491 PRO 491 483 483 PRO PRO B . n 
B 1 492 ASN 492 484 484 ASN ASN B . n 
B 1 493 MET 493 485 485 MET MET B . n 
B 1 494 ASP 494 486 486 ASP ASP B . n 
B 1 495 VAL 495 487 487 VAL VAL B . n 
B 1 496 TRP 496 488 488 TRP TRP B . n 
B 1 497 ARG 497 489 489 ARG ARG B . n 
B 1 498 PRO 498 490 490 PRO PRO B . n 
B 1 499 CYS 499 491 491 CYS CYS B . n 
B 1 500 ASP 500 492 492 ASP ASP B . n 
B 1 501 THR 501 493 493 THR THR B . n 
B 1 502 ALA 502 494 494 ALA ALA B . n 
B 1 503 GLU 503 495 495 GLU GLU B . n 
B 1 504 SER 504 496 496 SER SER B . n 
B 1 505 LEU 505 497 497 LEU LEU B . n 
B 1 506 VAL 506 498 498 VAL VAL B . n 
B 1 507 ALA 507 499 499 ALA ALA B . n 
B 1 508 TRP 508 500 500 TRP TRP B . n 
B 1 509 ALA 509 501 501 ALA ALA B . n 
B 1 510 GLU 510 502 502 GLU GLU B . n 
B 1 511 ALA 511 503 503 ALA ALA B . n 
B 1 512 ALA 512 504 504 ALA ALA B . n 
B 1 513 LYS 513 505 505 LYS LYS B . n 
B 1 514 ALA 514 506 506 ALA ALA B . n 
B 1 515 GLU 515 507 507 GLU GLU B . n 
B 1 516 ASP 516 508 508 ASP ASP B . n 
B 1 517 HIS 517 509 509 HIS HIS B . n 
B 1 518 PRO 518 510 510 PRO PRO B . n 
B 1 519 SER 519 511 511 SER SER B . n 
B 1 520 CYS 520 512 512 CYS CYS B . n 
B 1 521 LEU 521 513 513 LEU LEU B . n 
B 1 522 ILE 522 514 514 ILE ILE B . n 
B 1 523 PHE 523 515 515 PHE PHE B . n 
B 1 524 SER 524 516 516 SER SER B . n 
B 1 525 ARG 525 517 517 ARG ARG B . n 
B 1 526 GLN 526 518 518 GLN GLN B . n 
B 1 527 ASN 527 519 519 ASN ASN B . n 
B 1 528 LEU 528 520 ?   ?   ?   B . n 
B 1 529 LYS 529 521 ?   ?   ?   B . n 
B 1 530 PHE 530 522 522 PHE PHE B . n 
B 1 531 GLN 531 523 523 GLN GLN B . n 
B 1 532 ALA 532 524 524 ALA ALA B . n 
B 1 533 ARG 533 525 525 ARG ARG B . n 
B 1 534 SER 534 526 526 SER SER B . n 
B 1 535 GLU 535 527 527 GLU GLU B . n 
B 1 536 GLN 536 528 528 GLN GLN B . n 
B 1 537 GLN 537 529 529 GLN GLN B . n 
B 1 538 LEU 538 530 530 LEU LEU B . n 
B 1 539 ASN 539 531 531 ASN ASN B . n 
B 1 540 ASP 540 532 532 ASP ASP B . n 
B 1 541 ILE 541 533 533 ILE ILE B . n 
B 1 542 LYS 542 534 534 LYS LYS B . n 
B 1 543 ARG 543 535 535 ARG ARG B . n 
B 1 544 GLY 544 536 536 GLY GLY B . n 
B 1 545 ALA 545 537 537 ALA ALA B . n 
B 1 546 TYR 546 538 538 TYR TYR B . n 
B 1 547 VAL 547 539 539 VAL VAL B . n 
B 1 548 ILE 548 540 540 ILE ILE B . n 
B 1 549 SER 549 541 541 SER SER B . n 
B 1 550 GLU 550 542 542 GLU GLU B . n 
B 1 551 ALA 551 543 543 ALA ALA B . n 
B 1 552 GLN 552 544 544 GLN GLN B . n 
B 1 553 GLY 553 545 545 GLY GLY B . n 
B 1 554 ASN 554 546 546 ASN ASN B . n 
B 1 555 ALA 555 547 547 ALA ALA B . n 
B 1 556 GLN 556 548 548 GLN GLN B . n 
B 1 557 ALA 557 549 549 ALA ALA B . n 
B 1 558 VAL 558 550 550 VAL VAL B . n 
B 1 559 ILE 559 551 551 ILE ILE B . n 
B 1 560 ILE 560 552 552 ILE ILE B . n 
B 1 561 ALA 561 553 553 ALA ALA B . n 
B 1 562 THR 562 554 554 THR THR B . n 
B 1 563 GLY 563 555 555 GLY GLY B . n 
B 1 564 SER 564 556 556 SER SER B . n 
B 1 565 GLU 565 557 557 GLU GLU B . n 
B 1 566 VAL 566 558 558 VAL VAL B . n 
B 1 567 GLY 567 559 559 GLY GLY B . n 
B 1 568 LEU 568 560 560 LEU LEU B . n 
B 1 569 ALA 569 561 561 ALA ALA B . n 
B 1 570 VAL 570 562 562 VAL VAL B . n 
B 1 571 GLU 571 563 563 GLU GLU B . n 
B 1 572 ALA 572 564 564 ALA ALA B . n 
B 1 573 GLN 573 565 565 GLN GLN B . n 
B 1 574 LYS 574 566 566 LYS LYS B . n 
B 1 575 VAL 575 567 567 VAL VAL B . n 
B 1 576 LEU 576 568 568 LEU LEU B . n 
B 1 577 ALA 577 569 569 ALA ALA B . n 
B 1 578 GLY 578 570 570 GLY GLY B . n 
B 1 579 GLN 579 571 571 GLN GLN B . n 
B 1 580 GLY 580 572 572 GLY GLY B . n 
B 1 581 ILE 581 573 573 ILE ILE B . n 
B 1 582 ALA 582 574 574 ALA ALA B . n 
B 1 583 VAL 583 575 575 VAL VAL B . n 
B 1 584 ARG 584 576 576 ARG ARG B . n 
B 1 585 VAL 585 577 577 VAL VAL B . n 
B 1 586 VAL 586 578 578 VAL VAL B . n 
B 1 587 SER 587 579 579 SER SER B . n 
B 1 588 MET 588 580 580 MET MET B . n 
B 1 589 PRO 589 581 581 PRO PRO B . n 
B 1 590 SER 590 582 582 SER SER B . n 
B 1 591 THR 591 583 583 THR THR B . n 
B 1 592 SER 592 584 584 SER SER B . n 
B 1 593 VAL 593 585 585 VAL VAL B . n 
B 1 594 PHE 594 586 586 PHE PHE B . n 
B 1 595 ASP 595 587 587 ASP ASP B . n 
B 1 596 ARG 596 588 588 ARG ARG B . n 
B 1 597 GLN 597 589 589 GLN GLN B . n 
B 1 598 ASP 598 590 590 ASP ASP B . n 
B 1 599 ALA 599 591 591 ALA ALA B . n 
B 1 600 ALA 600 592 592 ALA ALA B . n 
B 1 601 TYR 601 593 593 TYR TYR B . n 
B 1 602 GLN 602 594 594 GLN GLN B . n 
B 1 603 ALA 603 595 595 ALA ALA B . n 
B 1 604 ALA 604 596 596 ALA ALA B . n 
B 1 605 VAL 605 597 597 VAL VAL B . n 
B 1 606 LEU 606 598 598 LEU LEU B . n 
B 1 607 PRO 607 599 599 PRO PRO B . n 
B 1 608 GLU 608 600 600 GLU GLU B . n 
B 1 609 GLY 609 601 601 GLY GLY B . n 
B 1 610 LEU 610 602 602 LEU LEU B . n 
B 1 611 PRO 611 603 603 PRO PRO B . n 
B 1 612 ARG 612 604 604 ARG ARG B . n 
B 1 613 ILE 613 605 605 ILE ILE B . n 
B 1 614 ALA 614 606 606 ALA ALA B . n 
B 1 615 VAL 615 607 607 VAL VAL B . n 
B 1 616 GLU 616 608 608 GLU GLU B . n 
B 1 617 ALA 617 609 609 ALA ALA B . n 
B 1 618 GLY 618 610 610 GLY GLY B . n 
B 1 619 HIS 619 611 611 HIS HIS B . n 
B 1 620 THR 620 612 612 THR THR B . n 
B 1 621 ASN 621 613 613 ASN ASN B . n 
B 1 622 GLY 622 614 614 GLY GLY B . n 
B 1 623 TRP 623 615 615 TRP TRP B . n 
B 1 624 TYR 624 616 616 TYR TYR B . n 
B 1 625 LYS 625 617 617 LYS LYS B . n 
B 1 626 TYR 626 618 618 TYR TYR B . n 
B 1 627 VAL 627 619 619 VAL VAL B . n 
B 1 628 GLY 628 620 620 GLY GLY B . n 
B 1 629 LEU 629 621 621 LEU LEU B . n 
B 1 630 ASN 630 622 622 ASN ASN B . n 
B 1 631 GLY 631 623 623 GLY GLY B . n 
B 1 632 ALA 632 624 624 ALA ALA B . n 
B 1 633 VAL 633 625 625 VAL VAL B . n 
B 1 634 VAL 634 626 626 VAL VAL B . n 
B 1 635 GLY 635 627 627 GLY GLY B . n 
B 1 636 ILE 636 628 628 ILE ILE B . n 
B 1 637 ASN 637 629 629 ASN ASN B . n 
B 1 638 ARG 638 630 630 ARG ARG B . n 
B 1 639 PHE 639 631 631 PHE PHE B . n 
B 1 640 GLY 640 632 632 GLY GLY B . n 
B 1 641 GLU 641 633 633 GLU GLU B . n 
B 1 642 SER 642 634 634 SER SER B . n 
B 1 643 ALA 643 635 635 ALA ALA B . n 
B 1 644 PRO 644 636 636 PRO PRO B . n 
B 1 645 ALA 645 637 637 ALA ALA B . n 
B 1 646 ASP 646 638 638 ASP ASP B . n 
B 1 647 LEU 647 639 639 LEU LEU B . n 
B 1 648 LEU 648 640 640 LEU LEU B . n 
B 1 649 PHE 649 641 641 PHE PHE B . n 
B 1 650 LYS 650 642 642 LYS LYS B . n 
B 1 651 ALA 651 643 643 ALA ALA B . n 
B 1 652 PHE 652 644 644 PHE PHE B . n 
B 1 653 GLY 653 645 645 GLY GLY B . n 
B 1 654 PHE 654 646 646 PHE PHE B . n 
B 1 655 THR 655 647 647 THR THR B . n 
B 1 656 VAL 656 648 648 VAL VAL B . n 
B 1 657 ASP 657 649 649 ASP ASP B . n 
B 1 658 ASN 658 650 650 ASN ASN B . n 
B 1 659 VAL 659 651 651 VAL VAL B . n 
B 1 660 VAL 660 652 652 VAL VAL B . n 
B 1 661 ASP 661 653 653 ASP ASP B . n 
B 1 662 THR 662 654 654 THR THR B . n 
B 1 663 VAL 663 655 655 VAL VAL B . n 
B 1 664 LYS 664 656 656 LYS LYS B . n 
B 1 665 SER 665 657 657 SER SER B . n 
B 1 666 VAL 666 658 658 VAL VAL B . n 
B 1 667 LEU 667 659 659 LEU LEU B . n 
C 1 1   MET 1   -7  ?   ?   ?   C . n 
C 1 2   ALA 2   -6  ?   ?   ?   C . n 
C 1 3   HIS 3   -5  ?   ?   ?   C . n 
C 1 4   HIS 4   -4  ?   ?   ?   C . n 
C 1 5   HIS 5   -3  ?   ?   ?   C . n 
C 1 6   HIS 6   -2  ?   ?   ?   C . n 
C 1 7   HIS 7   -1  ?   ?   ?   C . n 
C 1 8   HIS 8   0   ?   ?   ?   C . n 
C 1 9   MET 9   1   ?   ?   ?   C . n 
C 1 10  SER 10  2   2   SER SER C . n 
C 1 11  GLN 11  3   3   GLN GLN C . n 
C 1 12  LEU 12  4   4   LEU LEU C . n 
C 1 13  ALA 13  5   5   ALA ALA C . n 
C 1 14  ASN 14  6   6   ASN ASN C . n 
C 1 15  VAL 15  7   7   VAL VAL C . n 
C 1 16  ILE 16  8   8   ILE ILE C . n 
C 1 17  ARG 17  9   9   ARG ARG C . n 
C 1 18  PHE 18  10  10  PHE PHE C . n 
C 1 19  LEU 19  11  11  LEU LEU C . n 
C 1 20  SER 20  12  12  SER SER C . n 
C 1 21  ALA 21  13  13  ALA ALA C . n 
C 1 22  ASP 22  14  14  ASP ASP C . n 
C 1 23  ALA 23  15  15  ALA ALA C . n 
C 1 24  VAL 24  16  16  VAL VAL C . n 
C 1 25  GLN 25  17  17  GLN GLN C . n 
C 1 26  LYS 26  18  18  LYS LYS C . n 
C 1 27  ALA 27  19  19  ALA ALA C . n 
C 1 28  ASN 28  20  20  ASN ASN C . n 
C 1 29  SER 29  21  21  SER SER C . n 
C 1 30  GLY 30  22  22  GLY GLY C . n 
C 1 31  HIS 31  23  23  HIS HIS C . n 
C 1 32  PRO 32  24  24  PRO PRO C . n 
C 1 33  GLY 33  25  25  GLY GLY C . n 
C 1 34  ALA 34  26  26  ALA ALA C . n 
C 1 35  PRO 35  27  27  PRO PRO C . n 
C 1 36  MET 36  28  28  MET MET C . n 
C 1 37  GLY 37  29  29  GLY GLY C . n 
C 1 38  MET 38  30  30  MET MET C . n 
C 1 39  ALA 39  31  31  ALA ALA C . n 
C 1 40  GLU 40  32  32  GLU GLU C . n 
C 1 41  MET 41  33  33  MET MET C . n 
C 1 42  ALA 42  34  34  ALA ALA C . n 
C 1 43  GLU 43  35  35  GLU GLU C . n 
C 1 44  THR 44  36  36  THR THR C . n 
C 1 45  LEU 45  37  37  LEU LEU C . n 
C 1 46  TRP 46  38  38  TRP TRP C . n 
C 1 47  THR 47  39  39  THR THR C . n 
C 1 48  LYS 48  40  40  LYS LYS C . n 
C 1 49  PHE 49  41  41  PHE PHE C . n 
C 1 50  LEU 50  42  42  LEU LEU C . n 
C 1 51  ASN 51  43  43  ASN ASN C . n 
C 1 52  HIS 52  44  44  HIS HIS C . n 
C 1 53  ASN 53  45  45  ASN ASN C . n 
C 1 54  PRO 54  46  46  PRO PRO C . n 
C 1 55  ALA 55  47  47  ALA ALA C . n 
C 1 56  ASN 56  48  48  ASN ASN C . n 
C 1 57  PRO 57  49  49  PRO PRO C . n 
C 1 58  LYS 58  50  50  LYS LYS C . n 
C 1 59  PHE 59  51  51  PHE PHE C . n 
C 1 60  TYR 60  52  52  TYR TYR C . n 
C 1 61  ASN 61  53  53  ASN ASN C . n 
C 1 62  ARG 62  54  54  ARG ARG C . n 
C 1 63  ASP 63  55  55  ASP ASP C . n 
C 1 64  ARG 64  56  56  ARG ARG C . n 
C 1 65  PHE 65  57  57  PHE PHE C . n 
C 1 66  VAL 66  58  58  VAL VAL C . n 
C 1 67  LEU 67  59  59  LEU LEU C . n 
C 1 68  SER 68  60  60  SER SER C . n 
C 1 69  ASN 69  61  61  ASN ASN C . n 
C 1 70  GLY 70  62  62  GLY GLY C . n 
C 1 71  HIS 71  63  63  HIS HIS C . n 
C 1 72  ALA 72  64  64  ALA ALA C . n 
C 1 73  SER 73  65  65  SER SER C . n 
C 1 74  MET 74  66  66  MET MET C . n 
C 1 75  LEU 75  67  67  LEU LEU C . n 
C 1 76  LEU 76  68  68  LEU LEU C . n 
C 1 77  TYR 77  69  69  TYR TYR C . n 
C 1 78  SER 78  70  70  SER SER C . n 
C 1 79  LEU 79  71  71  LEU LEU C . n 
C 1 80  LEU 80  72  72  LEU LEU C . n 
C 1 81  HIS 81  73  73  HIS HIS C . n 
C 1 82  LEU 82  74  74  LEU LEU C . n 
C 1 83  THR 83  75  75  THR THR C . n 
C 1 84  GLY 84  76  76  GLY GLY C . n 
C 1 85  TYR 85  77  77  TYR TYR C . n 
C 1 86  ASN 86  78  78  ASN ASN C . n 
C 1 87  LEU 87  79  79  LEU LEU C . n 
C 1 88  SER 88  80  80  SER SER C . n 
C 1 89  ILE 89  81  81  ILE ILE C . n 
C 1 90  GLU 90  82  82  GLU GLU C . n 
C 1 91  ASP 91  83  83  ASP ASP C . n 
C 1 92  LEU 92  84  84  LEU LEU C . n 
C 1 93  LYS 93  85  85  LYS LYS C . n 
C 1 94  ASN 94  86  86  ASN ASN C . n 
C 1 95  PHE 95  87  87  PHE PHE C . n 
C 1 96  ARG 96  88  88  ARG ARG C . n 
C 1 97  GLN 97  89  89  GLN GLN C . n 
C 1 98  LEU 98  90  90  LEU LEU C . n 
C 1 99  HIS 99  91  91  HIS HIS C . n 
C 1 100 SER 100 92  92  SER SER C . n 
C 1 101 LYS 101 93  93  LYS LYS C . n 
C 1 102 THR 102 94  94  THR THR C . n 
C 1 103 PRO 103 95  95  PRO PRO C . n 
C 1 104 GLY 104 96  96  GLY GLY C . n 
C 1 105 HIS 105 97  97  HIS HIS C . n 
C 1 106 PRO 106 98  98  PRO PRO C . n 
C 1 107 GLU 107 99  99  GLU GLU C . n 
C 1 108 TYR 108 100 100 TYR TYR C . n 
C 1 109 GLY 109 101 101 GLY GLY C . n 
C 1 110 TYR 110 102 102 TYR TYR C . n 
C 1 111 THR 111 103 103 THR THR C . n 
C 1 112 ASP 112 104 104 ASP ASP C . n 
C 1 113 GLY 113 105 105 GLY GLY C . n 
C 1 114 VAL 114 106 106 VAL VAL C . n 
C 1 115 GLU 115 107 107 GLU GLU C . n 
C 1 116 THR 116 108 108 THR THR C . n 
C 1 117 THR 117 109 109 THR THR C . n 
C 1 118 THR 118 110 110 THR THR C . n 
C 1 119 GLY 119 111 111 GLY GLY C . n 
C 1 120 PRO 120 112 112 PRO PRO C . n 
C 1 121 LEU 121 113 113 LEU LEU C . n 
C 1 122 GLY 122 114 114 GLY GLY C . n 
C 1 123 GLN 123 115 115 GLN GLN C . n 
C 1 124 GLY 124 116 116 GLY GLY C . n 
C 1 125 ILE 125 117 117 ILE ILE C . n 
C 1 126 ALA 126 118 118 ALA ALA C . n 
C 1 127 ASN 127 119 119 ASN ASN C . n 
C 1 128 ALA 128 120 120 ALA ALA C . n 
C 1 129 VAL 129 121 121 VAL VAL C . n 
C 1 130 GLY 130 122 122 GLY GLY C . n 
C 1 131 MET 131 123 123 MET MET C . n 
C 1 132 ALA 132 124 124 ALA ALA C . n 
C 1 133 LEU 133 125 125 LEU LEU C . n 
C 1 134 ALA 134 126 126 ALA ALA C . n 
C 1 135 GLU 135 127 127 GLU GLU C . n 
C 1 136 LYS 136 128 128 LYS LYS C . n 
C 1 137 ILE 137 129 129 ILE ILE C . n 
C 1 138 LEU 138 130 130 LEU LEU C . n 
C 1 139 ALA 139 131 131 ALA ALA C . n 
C 1 140 ALA 140 132 132 ALA ALA C . n 
C 1 141 GLU 141 133 133 GLU GLU C . n 
C 1 142 PHE 142 134 134 PHE PHE C . n 
C 1 143 ASN 143 135 135 ASN ASN C . n 
C 1 144 LYS 144 136 136 LYS LYS C . n 
C 1 145 ASP 145 137 137 ASP ASP C . n 
C 1 146 GLY 146 138 138 GLY GLY C . n 
C 1 147 LEU 147 139 139 LEU LEU C . n 
C 1 148 ASN 148 140 140 ASN ASN C . n 
C 1 149 ILE 149 141 141 ILE ILE C . n 
C 1 150 VAL 150 142 142 VAL VAL C . n 
C 1 151 ASP 151 143 143 ASP ASP C . n 
C 1 152 HIS 152 144 144 HIS HIS C . n 
C 1 153 TYR 153 145 145 TYR TYR C . n 
C 1 154 THR 154 146 146 THR THR C . n 
C 1 155 TYR 155 147 147 TYR TYR C . n 
C 1 156 VAL 156 148 148 VAL VAL C . n 
C 1 157 PHE 157 149 149 PHE PHE C . n 
C 1 158 MET 158 150 150 MET MET C . n 
C 1 159 GLY 159 151 151 GLY GLY C . n 
C 1 160 ASP 160 152 152 ASP ASP C . n 
C 1 161 GLY 161 153 153 GLY GLY C . n 
C 1 162 OCS 162 154 154 OCS OCS C . n 
C 1 163 LEU 163 155 155 LEU LEU C . n 
C 1 164 MET 164 156 156 MET MET C . n 
C 1 165 GLU 165 157 157 GLU GLU C . n 
C 1 166 GLY 166 158 158 GLY GLY C . n 
C 1 167 VAL 167 159 159 VAL VAL C . n 
C 1 168 SER 168 160 160 SER SER C . n 
C 1 169 HIS 169 161 161 HIS HIS C . n 
C 1 170 GLU 170 162 162 GLU GLU C . n 
C 1 171 ALA 171 163 163 ALA ALA C . n 
C 1 172 CYS 172 164 164 CYS CYS C . n 
C 1 173 SER 173 165 165 SER SER C . n 
C 1 174 LEU 174 166 166 LEU LEU C . n 
C 1 175 ALA 175 167 167 ALA ALA C . n 
C 1 176 GLY 176 168 168 GLY GLY C . n 
C 1 177 THR 177 169 169 THR THR C . n 
C 1 178 LEU 178 170 170 LEU LEU C . n 
C 1 179 GLY 179 171 171 GLY GLY C . n 
C 1 180 LEU 180 172 172 LEU LEU C . n 
C 1 181 GLY 181 173 173 GLY GLY C . n 
C 1 182 LYS 182 174 174 LYS LYS C . n 
C 1 183 LEU 183 175 175 LEU LEU C . n 
C 1 184 ILE 184 176 176 ILE ILE C . n 
C 1 185 VAL 185 177 177 VAL VAL C . n 
C 1 186 LEU 186 178 178 LEU LEU C . n 
C 1 187 TYR 187 179 179 TYR TYR C . n 
C 1 188 ASP 188 180 180 ASP ASP C . n 
C 1 189 ASP 189 181 181 ASP ASP C . n 
C 1 190 ASN 190 182 182 ASN ASN C . n 
C 1 191 ASN 191 183 183 ASN ASN C . n 
C 1 192 ILE 192 184 ?   ?   ?   C . n 
C 1 193 SER 193 185 ?   ?   ?   C . n 
C 1 194 ILE 194 186 ?   ?   ?   C . n 
C 1 195 ASP 195 187 ?   ?   ?   C . n 
C 1 196 GLY 196 188 ?   ?   ?   C . n 
C 1 197 LYS 197 189 ?   ?   ?   C . n 
C 1 198 VAL 198 190 ?   ?   ?   C . n 
C 1 199 ASP 199 191 191 ASP ASP C . n 
C 1 200 GLY 200 192 192 GLY GLY C . n 
C 1 201 TRP 201 193 193 TRP TRP C . n 
C 1 202 PHE 202 194 194 PHE PHE C . n 
C 1 203 THR 203 195 195 THR THR C . n 
C 1 204 GLU 204 196 196 GLU GLU C . n 
C 1 205 ASN 205 197 197 ASN ASN C . n 
C 1 206 ILE 206 198 198 ILE ILE C . n 
C 1 207 PRO 207 199 199 PRO PRO C . n 
C 1 208 GLN 208 200 200 GLN GLN C . n 
C 1 209 ARG 209 201 201 ARG ARG C . n 
C 1 210 PHE 210 202 202 PHE PHE C . n 
C 1 211 GLU 211 203 203 GLU GLU C . n 
C 1 212 SER 212 204 204 SER SER C . n 
C 1 213 TYR 213 205 205 TYR TYR C . n 
C 1 214 GLY 214 206 206 GLY GLY C . n 
C 1 215 TRP 215 207 207 TRP TRP C . n 
C 1 216 HIS 216 208 208 HIS HIS C . n 
C 1 217 VAL 217 209 209 VAL VAL C . n 
C 1 218 VAL 218 210 210 VAL VAL C . n 
C 1 219 PRO 219 211 211 PRO PRO C . n 
C 1 220 ASN 220 212 212 ASN ASN C . n 
C 1 221 VAL 221 213 213 VAL VAL C . n 
C 1 222 ASN 222 214 214 ASN ASN C . n 
C 1 223 GLY 223 215 215 GLY GLY C . n 
C 1 224 HIS 224 216 216 HIS HIS C . n 
C 1 225 ASP 225 217 217 ASP ASP C . n 
C 1 226 THR 226 218 218 THR THR C . n 
C 1 227 ALA 227 219 219 ALA ALA C . n 
C 1 228 ALA 228 220 220 ALA ALA C . n 
C 1 229 ILE 229 221 221 ILE ILE C . n 
C 1 230 GLN 230 222 222 GLN GLN C . n 
C 1 231 THR 231 223 223 THR THR C . n 
C 1 232 ALA 232 224 224 ALA ALA C . n 
C 1 233 ILE 233 225 225 ILE ILE C . n 
C 1 234 GLU 234 226 226 GLU GLU C . n 
C 1 235 ALA 235 227 227 ALA ALA C . n 
C 1 236 ALA 236 228 228 ALA ALA C . n 
C 1 237 ARG 237 229 229 ARG ARG C . n 
C 1 238 ALA 238 230 230 ALA ALA C . n 
C 1 239 GLU 239 231 231 GLU GLU C . n 
C 1 240 THR 240 232 232 THR THR C . n 
C 1 241 GLY 241 233 233 GLY GLY C . n 
C 1 242 LYS 242 234 234 LYS LYS C . n 
C 1 243 PRO 243 235 235 PRO PRO C . n 
C 1 244 SER 244 236 236 SER SER C . n 
C 1 245 ILE 245 237 237 ILE ILE C . n 
C 1 246 ILE 246 238 238 ILE ILE C . n 
C 1 247 CYS 247 239 239 CYS CYS C . n 
C 1 248 CYS 248 240 240 CYS CYS C . n 
C 1 249 LYS 249 241 241 LYS LYS C . n 
C 1 250 THR 250 242 242 THR THR C . n 
C 1 251 LEU 251 243 243 LEU LEU C . n 
C 1 252 ILE 252 244 ?   ?   ?   C . n 
C 1 253 GLY 253 245 ?   ?   ?   C . n 
C 1 254 LYS 254 246 ?   ?   ?   C . n 
C 1 255 GLY 255 247 ?   ?   ?   C . n 
C 1 256 SER 256 248 ?   ?   ?   C . n 
C 1 257 ALA 257 249 ?   ?   ?   C . n 
C 1 258 ASN 258 250 ?   ?   ?   C . n 
C 1 259 LYS 259 251 ?   ?   ?   C . n 
C 1 260 GLU 260 252 ?   ?   ?   C . n 
C 1 261 GLY 261 253 ?   ?   ?   C . n 
C 1 262 SER 262 254 ?   ?   ?   C . n 
C 1 263 HIS 263 255 ?   ?   ?   C . n 
C 1 264 LYS 264 256 ?   ?   ?   C . n 
C 1 265 THR 265 257 ?   ?   ?   C . n 
C 1 266 HIS 266 258 ?   ?   ?   C . n 
C 1 267 GLY 267 259 ?   ?   ?   C . n 
C 1 268 ALA 268 260 260 ALA ALA C . n 
C 1 269 PRO 269 261 261 PRO PRO C . n 
C 1 270 LEU 270 262 262 LEU LEU C . n 
C 1 271 GLY 271 263 ?   ?   ?   C . n 
C 1 272 ALA 272 264 ?   ?   ?   C . n 
C 1 273 ASP 273 265 ?   ?   ?   C . n 
C 1 274 GLU 274 266 ?   ?   ?   C . n 
C 1 275 ILE 275 267 267 ILE ILE C . n 
C 1 276 GLU 276 268 268 GLU GLU C . n 
C 1 277 ALA 277 269 269 ALA ALA C . n 
C 1 278 THR 278 270 270 THR THR C . n 
C 1 279 ARG 279 271 271 ARG ARG C . n 
C 1 280 LYS 280 272 272 LYS LYS C . n 
C 1 281 HIS 281 273 273 HIS HIS C . n 
C 1 282 LEU 282 274 274 LEU LEU C . n 
C 1 283 GLY 283 275 275 GLY GLY C . n 
C 1 284 TRP 284 276 276 TRP TRP C . n 
C 1 285 ALA 285 277 277 ALA ALA C . n 
C 1 286 TYR 286 278 278 TYR TYR C . n 
C 1 287 PRO 287 279 279 PRO PRO C . n 
C 1 288 ALA 288 280 280 ALA ALA C . n 
C 1 289 PHE 289 281 281 PHE PHE C . n 
C 1 290 GLU 290 282 282 GLU GLU C . n 
C 1 291 ILE 291 283 283 ILE ILE C . n 
C 1 292 PRO 292 284 284 PRO PRO C . n 
C 1 293 GLN 293 285 285 GLN GLN C . n 
C 1 294 GLU 294 286 286 GLU GLU C . n 
C 1 295 ILE 295 287 287 ILE ILE C . n 
C 1 296 TYR 296 288 288 TYR TYR C . n 
C 1 297 ASP 297 289 289 ASP ASP C . n 
C 1 298 ALA 298 290 290 ALA ALA C . n 
C 1 299 TRP 299 291 291 TRP TRP C . n 
C 1 300 ASN 300 292 292 ASN ASN C . n 
C 1 301 ALA 301 293 293 ALA ALA C . n 
C 1 302 LYS 302 294 294 LYS LYS C . n 
C 1 303 GLU 303 295 295 GLU GLU C . n 
C 1 304 LYS 304 296 296 LYS LYS C . n 
C 1 305 GLY 305 297 297 GLY GLY C . n 
C 1 306 ALA 306 298 298 ALA ALA C . n 
C 1 307 LYS 307 299 299 LYS LYS C . n 
C 1 308 LEU 308 300 300 LEU LEU C . n 
C 1 309 GLU 309 301 301 GLU GLU C . n 
C 1 310 ALA 310 302 302 ALA ALA C . n 
C 1 311 GLY 311 303 303 GLY GLY C . n 
C 1 312 TRP 312 304 304 TRP TRP C . n 
C 1 313 ASN 313 305 305 ASN ASN C . n 
C 1 314 GLU 314 306 306 GLU GLU C . n 
C 1 315 LEU 315 307 307 LEU LEU C . n 
C 1 316 PHE 316 308 308 PHE PHE C . n 
C 1 317 ALA 317 309 309 ALA ALA C . n 
C 1 318 GLN 318 310 310 GLN GLN C . n 
C 1 319 TYR 319 311 311 TYR TYR C . n 
C 1 320 GLN 320 312 312 GLN GLN C . n 
C 1 321 ALA 321 313 313 ALA ALA C . n 
C 1 322 LYS 322 314 314 LYS LYS C . n 
C 1 323 TYR 323 315 315 TYR TYR C . n 
C 1 324 PRO 324 316 316 PRO PRO C . n 
C 1 325 ALA 325 317 317 ALA ALA C . n 
C 1 326 GLU 326 318 318 GLU GLU C . n 
C 1 327 ALA 327 319 319 ALA ALA C . n 
C 1 328 ALA 328 320 320 ALA ALA C . n 
C 1 329 GLU 329 321 321 GLU GLU C . n 
C 1 330 PHE 330 322 322 PHE PHE C . n 
C 1 331 VAL 331 323 323 VAL VAL C . n 
C 1 332 ARG 332 324 324 ARG ARG C . n 
C 1 333 ARG 333 325 325 ARG ARG C . n 
C 1 334 MET 334 326 326 MET MET C . n 
C 1 335 ASP 335 327 327 ASP ASP C . n 
C 1 336 LYS 336 328 328 LYS LYS C . n 
C 1 337 LYS 337 329 329 LYS LYS C . n 
C 1 338 LEU 338 330 330 LEU LEU C . n 
C 1 339 PRO 339 331 331 PRO PRO C . n 
C 1 340 GLU 340 332 332 GLU GLU C . n 
C 1 341 ASN 341 333 333 ASN ASN C . n 
C 1 342 PHE 342 334 334 PHE PHE C . n 
C 1 343 ASP 343 335 335 ASP ASP C . n 
C 1 344 GLU 344 336 336 GLU GLU C . n 
C 1 345 TYR 345 337 337 TYR TYR C . n 
C 1 346 VAL 346 338 338 VAL VAL C . n 
C 1 347 GLN 347 339 339 GLN GLN C . n 
C 1 348 THR 348 340 340 THR THR C . n 
C 1 349 ALA 349 341 341 ALA ALA C . n 
C 1 350 LEU 350 342 342 LEU LEU C . n 
C 1 351 LYS 351 343 343 LYS LYS C . n 
C 1 352 GLU 352 344 344 GLU GLU C . n 
C 1 353 VAL 353 345 345 VAL VAL C . n 
C 1 354 CYS 354 346 346 CYS CYS C . n 
C 1 355 ALA 355 347 347 ALA ALA C . n 
C 1 356 LYS 356 348 348 LYS LYS C . n 
C 1 357 ALA 357 349 ?   ?   ?   C . n 
C 1 358 GLU 358 350 ?   ?   ?   C . n 
C 1 359 THR 359 351 ?   ?   ?   C . n 
C 1 360 VAL 360 352 ?   ?   ?   C . n 
C 1 361 ALA 361 353 ?   ?   ?   C . n 
C 1 362 THR 362 354 ?   ?   ?   C . n 
C 1 363 ARG 363 355 ?   ?   ?   C . n 
C 1 364 LYS 364 356 ?   ?   ?   C . n 
C 1 365 ALA 365 357 ?   ?   ?   C . n 
C 1 366 SER 366 358 ?   ?   ?   C . n 
C 1 367 GLN 367 359 ?   ?   ?   C . n 
C 1 368 ASN 368 360 360 ASN ASN C . n 
C 1 369 SER 369 361 361 SER SER C . n 
C 1 370 ILE 370 362 362 ILE ILE C . n 
C 1 371 GLU 371 363 363 GLU GLU C . n 
C 1 372 ILE 372 364 364 ILE ILE C . n 
C 1 373 LEU 373 365 365 LEU LEU C . n 
C 1 374 ALA 374 366 366 ALA ALA C . n 
C 1 375 LYS 375 367 367 LYS LYS C . n 
C 1 376 GLU 376 368 368 GLU GLU C . n 
C 1 377 LEU 377 369 369 LEU LEU C . n 
C 1 378 PRO 378 370 370 PRO PRO C . n 
C 1 379 GLU 379 371 371 GLU GLU C . n 
C 1 380 LEU 380 372 372 LEU LEU C . n 
C 1 381 VAL 381 373 373 VAL VAL C . n 
C 1 382 GLY 382 374 374 GLY GLY C . n 
C 1 383 GLY 383 375 375 GLY GLY C . n 
C 1 384 SER 384 376 376 SER SER C . n 
C 1 385 ALA 385 377 377 ALA ALA C . n 
C 1 386 ASP 386 378 378 ASP ASP C . n 
C 1 387 LEU 387 379 379 LEU LEU C . n 
C 1 388 THR 388 380 380 THR THR C . n 
C 1 389 PRO 389 381 381 PRO PRO C . n 
C 1 390 SER 390 382 382 SER SER C . n 
C 1 391 ASN 391 383 383 ASN ASN C . n 
C 1 392 LEU 392 384 384 LEU LEU C . n 
C 1 393 THR 393 385 385 THR THR C . n 
C 1 394 ASP 394 386 386 ASP ASP C . n 
C 1 395 TRP 395 387 387 TRP TRP C . n 
C 1 396 SER 396 388 388 SER SER C . n 
C 1 397 ASN 397 389 389 ASN ASN C . n 
C 1 398 SER 398 390 390 SER SER C . n 
C 1 399 VAL 399 391 391 VAL VAL C . n 
C 1 400 SER 400 392 392 SER SER C . n 
C 1 401 VAL 401 393 393 VAL VAL C . n 
C 1 402 THR 402 394 394 THR THR C . n 
C 1 403 ARG 403 395 395 ARG ARG C . n 
C 1 404 ASP 404 396 396 ASP ASP C . n 
C 1 405 LYS 405 397 397 LYS LYS C . n 
C 1 406 GLY 406 398 398 GLY GLY C . n 
C 1 407 GLY 407 399 399 GLY GLY C . n 
C 1 408 ASN 408 400 400 ASN ASN C . n 
C 1 409 TYR 409 401 401 TYR TYR C . n 
C 1 410 ILE 410 402 402 ILE ILE C . n 
C 1 411 HIS 411 403 403 HIS HIS C . n 
C 1 412 TYR 412 404 404 TYR TYR C . n 
C 1 413 GLY 413 405 405 GLY GLY C . n 
C 1 414 VAL 414 406 406 VAL VAL C . n 
C 1 415 ARG 415 407 407 ARG ARG C . n 
C 1 416 GLU 416 408 408 GLU GLU C . n 
C 1 417 PHE 417 409 409 PHE PHE C . n 
C 1 418 GLY 418 410 410 GLY GLY C . n 
C 1 419 MET 419 411 411 MET MET C . n 
C 1 420 GLY 420 412 412 GLY GLY C . n 
C 1 421 ALA 421 413 413 ALA ALA C . n 
C 1 422 ILE 422 414 414 ILE ILE C . n 
C 1 423 MET 423 415 415 MET MET C . n 
C 1 424 ASN 424 416 416 ASN ASN C . n 
C 1 425 GLY 425 417 417 GLY GLY C . n 
C 1 426 LEU 426 418 418 LEU LEU C . n 
C 1 427 VAL 427 419 419 VAL VAL C . n 
C 1 428 LEU 428 420 420 LEU LEU C . n 
C 1 429 HIS 429 421 421 HIS HIS C . n 
C 1 430 GLY 430 422 422 GLY GLY C . n 
C 1 431 GLY 431 423 423 GLY GLY C . n 
C 1 432 VAL 432 424 424 VAL VAL C . n 
C 1 433 LYS 433 425 425 LYS LYS C . n 
C 1 434 PRO 434 426 426 PRO PRO C . n 
C 1 435 PHE 435 427 427 PHE PHE C . n 
C 1 436 GLY 436 428 428 GLY GLY C . n 
C 1 437 ALA 437 429 429 ALA ALA C . n 
C 1 438 THR 438 430 430 THR THR C . n 
C 1 439 PHE 439 431 431 PHE PHE C . n 
C 1 440 LEU 440 432 432 LEU LEU C . n 
C 1 441 MET 441 433 433 MET MET C . n 
C 1 442 PHE 442 434 434 PHE PHE C . n 
C 1 443 SER 443 435 435 SER SER C . n 
C 1 444 GLU 444 436 436 GLU GLU C . n 
C 1 445 TYR 445 437 437 TYR TYR C . n 
C 1 446 GLU 446 438 438 GLU GLU C . n 
C 1 447 ARG 447 439 439 ARG ARG C . n 
C 1 448 ASN 448 440 440 ASN ASN C . n 
C 1 449 ALA 449 441 441 ALA ALA C . n 
C 1 450 LEU 450 442 442 LEU LEU C . n 
C 1 451 ARG 451 443 443 ARG ARG C . n 
C 1 452 MET 452 444 444 MET MET C . n 
C 1 453 ALA 453 445 445 ALA ALA C . n 
C 1 454 ALA 454 446 446 ALA ALA C . n 
C 1 455 LEU 455 447 447 LEU LEU C . n 
C 1 456 MET 456 448 448 MET MET C . n 
C 1 457 LYS 457 449 449 LYS LYS C . n 
C 1 458 ILE 458 450 450 ILE ILE C . n 
C 1 459 ASN 459 451 451 ASN ASN C . n 
C 1 460 PRO 460 452 452 PRO PRO C . n 
C 1 461 VAL 461 453 453 VAL VAL C . n 
C 1 462 PHE 462 454 454 PHE PHE C . n 
C 1 463 VAL 463 455 455 VAL VAL C . n 
C 1 464 PHE 464 456 456 PHE PHE C . n 
C 1 465 THR 465 457 457 THR THR C . n 
C 1 466 HIS 466 458 458 HIS HIS C . n 
C 1 467 ASP 467 459 459 ASP ASP C . n 
C 1 468 SER 468 460 460 SER SER C . n 
C 1 469 ILE 469 461 461 ILE ILE C . n 
C 1 470 GLY 470 462 462 GLY GLY C . n 
C 1 471 LEU 471 463 463 LEU LEU C . n 
C 1 472 GLY 472 464 464 GLY GLY C . n 
C 1 473 GLU 473 465 465 GLU GLU C . n 
C 1 474 ASP 474 466 466 ASP ASP C . n 
C 1 475 GLY 475 467 467 GLY GLY C . n 
C 1 476 PRO 476 468 468 PRO PRO C . n 
C 1 477 THR 477 469 469 THR THR C . n 
C 1 478 HIS 478 470 470 HIS HIS C . n 
C 1 479 GLN 479 471 471 GLN GLN C . n 
C 1 480 PRO 480 472 472 PRO PRO C . n 
C 1 481 ILE 481 473 473 ILE ILE C . n 
C 1 482 GLU 482 474 474 GLU GLU C . n 
C 1 483 GLN 483 475 475 GLN GLN C . n 
C 1 484 THR 484 476 476 THR THR C . n 
C 1 485 ALA 485 477 477 ALA ALA C . n 
C 1 486 THR 486 478 478 THR THR C . n 
C 1 487 LEU 487 479 479 LEU LEU C . n 
C 1 488 ARG 488 480 480 ARG ARG C . n 
C 1 489 LEU 489 481 481 LEU LEU C . n 
C 1 490 ILE 490 482 482 ILE ILE C . n 
C 1 491 PRO 491 483 483 PRO PRO C . n 
C 1 492 ASN 492 484 484 ASN ASN C . n 
C 1 493 MET 493 485 485 MET MET C . n 
C 1 494 ASP 494 486 486 ASP ASP C . n 
C 1 495 VAL 495 487 487 VAL VAL C . n 
C 1 496 TRP 496 488 488 TRP TRP C . n 
C 1 497 ARG 497 489 489 ARG ARG C . n 
C 1 498 PRO 498 490 490 PRO PRO C . n 
C 1 499 CYS 499 491 491 CYS CYS C . n 
C 1 500 ASP 500 492 492 ASP ASP C . n 
C 1 501 THR 501 493 493 THR THR C . n 
C 1 502 ALA 502 494 494 ALA ALA C . n 
C 1 503 GLU 503 495 495 GLU GLU C . n 
C 1 504 SER 504 496 496 SER SER C . n 
C 1 505 LEU 505 497 497 LEU LEU C . n 
C 1 506 VAL 506 498 498 VAL VAL C . n 
C 1 507 ALA 507 499 499 ALA ALA C . n 
C 1 508 TRP 508 500 500 TRP TRP C . n 
C 1 509 ALA 509 501 501 ALA ALA C . n 
C 1 510 GLU 510 502 502 GLU GLU C . n 
C 1 511 ALA 511 503 503 ALA ALA C . n 
C 1 512 ALA 512 504 504 ALA ALA C . n 
C 1 513 LYS 513 505 505 LYS LYS C . n 
C 1 514 ALA 514 506 506 ALA ALA C . n 
C 1 515 GLU 515 507 507 GLU GLU C . n 
C 1 516 ASP 516 508 508 ASP ASP C . n 
C 1 517 HIS 517 509 509 HIS HIS C . n 
C 1 518 PRO 518 510 510 PRO PRO C . n 
C 1 519 SER 519 511 511 SER SER C . n 
C 1 520 CYS 520 512 512 CYS CYS C . n 
C 1 521 LEU 521 513 513 LEU LEU C . n 
C 1 522 ILE 522 514 514 ILE ILE C . n 
C 1 523 PHE 523 515 515 PHE PHE C . n 
C 1 524 SER 524 516 516 SER SER C . n 
C 1 525 ARG 525 517 517 ARG ARG C . n 
C 1 526 GLN 526 518 ?   ?   ?   C . n 
C 1 527 ASN 527 519 ?   ?   ?   C . n 
C 1 528 LEU 528 520 ?   ?   ?   C . n 
C 1 529 LYS 529 521 ?   ?   ?   C . n 
C 1 530 PHE 530 522 ?   ?   ?   C . n 
C 1 531 GLN 531 523 523 GLN GLN C . n 
C 1 532 ALA 532 524 524 ALA ALA C . n 
C 1 533 ARG 533 525 525 ARG ARG C . n 
C 1 534 SER 534 526 526 SER SER C . n 
C 1 535 GLU 535 527 527 GLU GLU C . n 
C 1 536 GLN 536 528 528 GLN GLN C . n 
C 1 537 GLN 537 529 529 GLN GLN C . n 
C 1 538 LEU 538 530 530 LEU LEU C . n 
C 1 539 ASN 539 531 531 ASN ASN C . n 
C 1 540 ASP 540 532 532 ASP ASP C . n 
C 1 541 ILE 541 533 533 ILE ILE C . n 
C 1 542 LYS 542 534 534 LYS LYS C . n 
C 1 543 ARG 543 535 535 ARG ARG C . n 
C 1 544 GLY 544 536 536 GLY GLY C . n 
C 1 545 ALA 545 537 537 ALA ALA C . n 
C 1 546 TYR 546 538 538 TYR TYR C . n 
C 1 547 VAL 547 539 539 VAL VAL C . n 
C 1 548 ILE 548 540 540 ILE ILE C . n 
C 1 549 SER 549 541 541 SER SER C . n 
C 1 550 GLU 550 542 542 GLU GLU C . n 
C 1 551 ALA 551 543 543 ALA ALA C . n 
C 1 552 GLN 552 544 544 GLN GLN C . n 
C 1 553 GLY 553 545 545 GLY GLY C . n 
C 1 554 ASN 554 546 546 ASN ASN C . n 
C 1 555 ALA 555 547 547 ALA ALA C . n 
C 1 556 GLN 556 548 548 GLN GLN C . n 
C 1 557 ALA 557 549 549 ALA ALA C . n 
C 1 558 VAL 558 550 550 VAL VAL C . n 
C 1 559 ILE 559 551 551 ILE ILE C . n 
C 1 560 ILE 560 552 552 ILE ILE C . n 
C 1 561 ALA 561 553 553 ALA ALA C . n 
C 1 562 THR 562 554 554 THR THR C . n 
C 1 563 GLY 563 555 555 GLY GLY C . n 
C 1 564 SER 564 556 556 SER SER C . n 
C 1 565 GLU 565 557 557 GLU GLU C . n 
C 1 566 VAL 566 558 558 VAL VAL C . n 
C 1 567 GLY 567 559 559 GLY GLY C . n 
C 1 568 LEU 568 560 560 LEU LEU C . n 
C 1 569 ALA 569 561 561 ALA ALA C . n 
C 1 570 VAL 570 562 562 VAL VAL C . n 
C 1 571 GLU 571 563 563 GLU GLU C . n 
C 1 572 ALA 572 564 564 ALA ALA C . n 
C 1 573 GLN 573 565 565 GLN GLN C . n 
C 1 574 LYS 574 566 566 LYS LYS C . n 
C 1 575 VAL 575 567 567 VAL VAL C . n 
C 1 576 LEU 576 568 568 LEU LEU C . n 
C 1 577 ALA 577 569 569 ALA ALA C . n 
C 1 578 GLY 578 570 570 GLY GLY C . n 
C 1 579 GLN 579 571 571 GLN GLN C . n 
C 1 580 GLY 580 572 572 GLY GLY C . n 
C 1 581 ILE 581 573 573 ILE ILE C . n 
C 1 582 ALA 582 574 574 ALA ALA C . n 
C 1 583 VAL 583 575 575 VAL VAL C . n 
C 1 584 ARG 584 576 576 ARG ARG C . n 
C 1 585 VAL 585 577 577 VAL VAL C . n 
C 1 586 VAL 586 578 578 VAL VAL C . n 
C 1 587 SER 587 579 579 SER SER C . n 
C 1 588 MET 588 580 580 MET MET C . n 
C 1 589 PRO 589 581 581 PRO PRO C . n 
C 1 590 SER 590 582 582 SER SER C . n 
C 1 591 THR 591 583 583 THR THR C . n 
C 1 592 SER 592 584 584 SER SER C . n 
C 1 593 VAL 593 585 585 VAL VAL C . n 
C 1 594 PHE 594 586 586 PHE PHE C . n 
C 1 595 ASP 595 587 587 ASP ASP C . n 
C 1 596 ARG 596 588 588 ARG ARG C . n 
C 1 597 GLN 597 589 589 GLN GLN C . n 
C 1 598 ASP 598 590 590 ASP ASP C . n 
C 1 599 ALA 599 591 591 ALA ALA C . n 
C 1 600 ALA 600 592 592 ALA ALA C . n 
C 1 601 TYR 601 593 593 TYR TYR C . n 
C 1 602 GLN 602 594 594 GLN GLN C . n 
C 1 603 ALA 603 595 595 ALA ALA C . n 
C 1 604 ALA 604 596 596 ALA ALA C . n 
C 1 605 VAL 605 597 597 VAL VAL C . n 
C 1 606 LEU 606 598 598 LEU LEU C . n 
C 1 607 PRO 607 599 599 PRO PRO C . n 
C 1 608 GLU 608 600 600 GLU GLU C . n 
C 1 609 GLY 609 601 601 GLY GLY C . n 
C 1 610 LEU 610 602 602 LEU LEU C . n 
C 1 611 PRO 611 603 603 PRO PRO C . n 
C 1 612 ARG 612 604 604 ARG ARG C . n 
C 1 613 ILE 613 605 605 ILE ILE C . n 
C 1 614 ALA 614 606 606 ALA ALA C . n 
C 1 615 VAL 615 607 607 VAL VAL C . n 
C 1 616 GLU 616 608 608 GLU GLU C . n 
C 1 617 ALA 617 609 609 ALA ALA C . n 
C 1 618 GLY 618 610 610 GLY GLY C . n 
C 1 619 HIS 619 611 611 HIS HIS C . n 
C 1 620 THR 620 612 612 THR THR C . n 
C 1 621 ASN 621 613 613 ASN ASN C . n 
C 1 622 GLY 622 614 614 GLY GLY C . n 
C 1 623 TRP 623 615 615 TRP TRP C . n 
C 1 624 TYR 624 616 616 TYR TYR C . n 
C 1 625 LYS 625 617 617 LYS LYS C . n 
C 1 626 TYR 626 618 618 TYR TYR C . n 
C 1 627 VAL 627 619 619 VAL VAL C . n 
C 1 628 GLY 628 620 620 GLY GLY C . n 
C 1 629 LEU 629 621 621 LEU LEU C . n 
C 1 630 ASN 630 622 622 ASN ASN C . n 
C 1 631 GLY 631 623 623 GLY GLY C . n 
C 1 632 ALA 632 624 624 ALA ALA C . n 
C 1 633 VAL 633 625 625 VAL VAL C . n 
C 1 634 VAL 634 626 626 VAL VAL C . n 
C 1 635 GLY 635 627 627 GLY GLY C . n 
C 1 636 ILE 636 628 628 ILE ILE C . n 
C 1 637 ASN 637 629 629 ASN ASN C . n 
C 1 638 ARG 638 630 630 ARG ARG C . n 
C 1 639 PHE 639 631 631 PHE PHE C . n 
C 1 640 GLY 640 632 632 GLY GLY C . n 
C 1 641 GLU 641 633 633 GLU GLU C . n 
C 1 642 SER 642 634 634 SER SER C . n 
C 1 643 ALA 643 635 635 ALA ALA C . n 
C 1 644 PRO 644 636 636 PRO PRO C . n 
C 1 645 ALA 645 637 637 ALA ALA C . n 
C 1 646 ASP 646 638 638 ASP ASP C . n 
C 1 647 LEU 647 639 639 LEU LEU C . n 
C 1 648 LEU 648 640 640 LEU LEU C . n 
C 1 649 PHE 649 641 641 PHE PHE C . n 
C 1 650 LYS 650 642 642 LYS LYS C . n 
C 1 651 ALA 651 643 643 ALA ALA C . n 
C 1 652 PHE 652 644 644 PHE PHE C . n 
C 1 653 GLY 653 645 645 GLY GLY C . n 
C 1 654 PHE 654 646 646 PHE PHE C . n 
C 1 655 THR 655 647 647 THR THR C . n 
C 1 656 VAL 656 648 648 VAL VAL C . n 
C 1 657 ASP 657 649 649 ASP ASP C . n 
C 1 658 ASN 658 650 650 ASN ASN C . n 
C 1 659 VAL 659 651 651 VAL VAL C . n 
C 1 660 VAL 660 652 652 VAL VAL C . n 
C 1 661 ASP 661 653 653 ASP ASP C . n 
C 1 662 THR 662 654 654 THR THR C . n 
C 1 663 VAL 663 655 655 VAL VAL C . n 
C 1 664 LYS 664 656 656 LYS LYS C . n 
C 1 665 SER 665 657 657 SER SER C . n 
C 1 666 VAL 666 658 658 VAL VAL C . n 
C 1 667 LEU 667 659 659 LEU LEU C . n 
D 1 1   MET 1   -7  ?   ?   ?   D . n 
D 1 2   ALA 2   -6  ?   ?   ?   D . n 
D 1 3   HIS 3   -5  ?   ?   ?   D . n 
D 1 4   HIS 4   -4  ?   ?   ?   D . n 
D 1 5   HIS 5   -3  ?   ?   ?   D . n 
D 1 6   HIS 6   -2  ?   ?   ?   D . n 
D 1 7   HIS 7   -1  ?   ?   ?   D . n 
D 1 8   HIS 8   0   ?   ?   ?   D . n 
D 1 9   MET 9   1   1   MET MET D . n 
D 1 10  SER 10  2   2   SER SER D . n 
D 1 11  GLN 11  3   3   GLN GLN D . n 
D 1 12  LEU 12  4   4   LEU LEU D . n 
D 1 13  ALA 13  5   5   ALA ALA D . n 
D 1 14  ASN 14  6   6   ASN ASN D . n 
D 1 15  VAL 15  7   7   VAL VAL D . n 
D 1 16  ILE 16  8   8   ILE ILE D . n 
D 1 17  ARG 17  9   9   ARG ARG D . n 
D 1 18  PHE 18  10  10  PHE PHE D . n 
D 1 19  LEU 19  11  11  LEU LEU D . n 
D 1 20  SER 20  12  12  SER SER D . n 
D 1 21  ALA 21  13  13  ALA ALA D . n 
D 1 22  ASP 22  14  14  ASP ASP D . n 
D 1 23  ALA 23  15  15  ALA ALA D . n 
D 1 24  VAL 24  16  16  VAL VAL D . n 
D 1 25  GLN 25  17  17  GLN GLN D . n 
D 1 26  LYS 26  18  18  LYS LYS D . n 
D 1 27  ALA 27  19  19  ALA ALA D . n 
D 1 28  ASN 28  20  20  ASN ASN D . n 
D 1 29  SER 29  21  21  SER SER D . n 
D 1 30  GLY 30  22  22  GLY GLY D . n 
D 1 31  HIS 31  23  23  HIS HIS D . n 
D 1 32  PRO 32  24  24  PRO PRO D . n 
D 1 33  GLY 33  25  25  GLY GLY D . n 
D 1 34  ALA 34  26  26  ALA ALA D . n 
D 1 35  PRO 35  27  27  PRO PRO D . n 
D 1 36  MET 36  28  28  MET MET D . n 
D 1 37  GLY 37  29  29  GLY GLY D . n 
D 1 38  MET 38  30  30  MET MET D . n 
D 1 39  ALA 39  31  31  ALA ALA D . n 
D 1 40  GLU 40  32  32  GLU GLU D . n 
D 1 41  MET 41  33  33  MET MET D . n 
D 1 42  ALA 42  34  34  ALA ALA D . n 
D 1 43  GLU 43  35  35  GLU GLU D . n 
D 1 44  THR 44  36  36  THR THR D . n 
D 1 45  LEU 45  37  37  LEU LEU D . n 
D 1 46  TRP 46  38  38  TRP TRP D . n 
D 1 47  THR 47  39  39  THR THR D . n 
D 1 48  LYS 48  40  40  LYS LYS D . n 
D 1 49  PHE 49  41  41  PHE PHE D . n 
D 1 50  LEU 50  42  42  LEU LEU D . n 
D 1 51  ASN 51  43  43  ASN ASN D . n 
D 1 52  HIS 52  44  44  HIS HIS D . n 
D 1 53  ASN 53  45  45  ASN ASN D . n 
D 1 54  PRO 54  46  46  PRO PRO D . n 
D 1 55  ALA 55  47  47  ALA ALA D . n 
D 1 56  ASN 56  48  48  ASN ASN D . n 
D 1 57  PRO 57  49  49  PRO PRO D . n 
D 1 58  LYS 58  50  50  LYS LYS D . n 
D 1 59  PHE 59  51  51  PHE PHE D . n 
D 1 60  TYR 60  52  52  TYR TYR D . n 
D 1 61  ASN 61  53  53  ASN ASN D . n 
D 1 62  ARG 62  54  54  ARG ARG D . n 
D 1 63  ASP 63  55  55  ASP ASP D . n 
D 1 64  ARG 64  56  56  ARG ARG D . n 
D 1 65  PHE 65  57  57  PHE PHE D . n 
D 1 66  VAL 66  58  58  VAL VAL D . n 
D 1 67  LEU 67  59  59  LEU LEU D . n 
D 1 68  SER 68  60  60  SER SER D . n 
D 1 69  ASN 69  61  61  ASN ASN D . n 
D 1 70  GLY 70  62  62  GLY GLY D . n 
D 1 71  HIS 71  63  63  HIS HIS D . n 
D 1 72  ALA 72  64  64  ALA ALA D . n 
D 1 73  SER 73  65  65  SER SER D . n 
D 1 74  MET 74  66  66  MET MET D . n 
D 1 75  LEU 75  67  67  LEU LEU D . n 
D 1 76  LEU 76  68  68  LEU LEU D . n 
D 1 77  TYR 77  69  69  TYR TYR D . n 
D 1 78  SER 78  70  70  SER SER D . n 
D 1 79  LEU 79  71  71  LEU LEU D . n 
D 1 80  LEU 80  72  72  LEU LEU D . n 
D 1 81  HIS 81  73  73  HIS HIS D . n 
D 1 82  LEU 82  74  74  LEU LEU D . n 
D 1 83  THR 83  75  75  THR THR D . n 
D 1 84  GLY 84  76  76  GLY GLY D . n 
D 1 85  TYR 85  77  77  TYR TYR D . n 
D 1 86  ASN 86  78  78  ASN ASN D . n 
D 1 87  LEU 87  79  79  LEU LEU D . n 
D 1 88  SER 88  80  80  SER SER D . n 
D 1 89  ILE 89  81  81  ILE ILE D . n 
D 1 90  GLU 90  82  82  GLU GLU D . n 
D 1 91  ASP 91  83  83  ASP ASP D . n 
D 1 92  LEU 92  84  84  LEU LEU D . n 
D 1 93  LYS 93  85  85  LYS LYS D . n 
D 1 94  ASN 94  86  86  ASN ASN D . n 
D 1 95  PHE 95  87  87  PHE PHE D . n 
D 1 96  ARG 96  88  88  ARG ARG D . n 
D 1 97  GLN 97  89  89  GLN GLN D . n 
D 1 98  LEU 98  90  90  LEU LEU D . n 
D 1 99  HIS 99  91  91  HIS HIS D . n 
D 1 100 SER 100 92  92  SER SER D . n 
D 1 101 LYS 101 93  93  LYS LYS D . n 
D 1 102 THR 102 94  94  THR THR D . n 
D 1 103 PRO 103 95  95  PRO PRO D . n 
D 1 104 GLY 104 96  96  GLY GLY D . n 
D 1 105 HIS 105 97  97  HIS HIS D . n 
D 1 106 PRO 106 98  98  PRO PRO D . n 
D 1 107 GLU 107 99  99  GLU GLU D . n 
D 1 108 TYR 108 100 100 TYR TYR D . n 
D 1 109 GLY 109 101 101 GLY GLY D . n 
D 1 110 TYR 110 102 102 TYR TYR D . n 
D 1 111 THR 111 103 103 THR THR D . n 
D 1 112 ASP 112 104 104 ASP ASP D . n 
D 1 113 GLY 113 105 105 GLY GLY D . n 
D 1 114 VAL 114 106 106 VAL VAL D . n 
D 1 115 GLU 115 107 107 GLU GLU D . n 
D 1 116 THR 116 108 108 THR THR D . n 
D 1 117 THR 117 109 109 THR THR D . n 
D 1 118 THR 118 110 110 THR THR D . n 
D 1 119 GLY 119 111 111 GLY GLY D . n 
D 1 120 PRO 120 112 112 PRO PRO D . n 
D 1 121 LEU 121 113 113 LEU LEU D . n 
D 1 122 GLY 122 114 114 GLY GLY D . n 
D 1 123 GLN 123 115 115 GLN GLN D . n 
D 1 124 GLY 124 116 116 GLY GLY D . n 
D 1 125 ILE 125 117 117 ILE ILE D . n 
D 1 126 ALA 126 118 118 ALA ALA D . n 
D 1 127 ASN 127 119 119 ASN ASN D . n 
D 1 128 ALA 128 120 120 ALA ALA D . n 
D 1 129 VAL 129 121 121 VAL VAL D . n 
D 1 130 GLY 130 122 122 GLY GLY D . n 
D 1 131 MET 131 123 123 MET MET D . n 
D 1 132 ALA 132 124 124 ALA ALA D . n 
D 1 133 LEU 133 125 125 LEU LEU D . n 
D 1 134 ALA 134 126 126 ALA ALA D . n 
D 1 135 GLU 135 127 127 GLU GLU D . n 
D 1 136 LYS 136 128 128 LYS LYS D . n 
D 1 137 ILE 137 129 129 ILE ILE D . n 
D 1 138 LEU 138 130 130 LEU LEU D . n 
D 1 139 ALA 139 131 131 ALA ALA D . n 
D 1 140 ALA 140 132 132 ALA ALA D . n 
D 1 141 GLU 141 133 133 GLU GLU D . n 
D 1 142 PHE 142 134 134 PHE PHE D . n 
D 1 143 ASN 143 135 135 ASN ASN D . n 
D 1 144 LYS 144 136 136 LYS LYS D . n 
D 1 145 ASP 145 137 137 ASP ASP D . n 
D 1 146 GLY 146 138 138 GLY GLY D . n 
D 1 147 LEU 147 139 139 LEU LEU D . n 
D 1 148 ASN 148 140 140 ASN ASN D . n 
D 1 149 ILE 149 141 141 ILE ILE D . n 
D 1 150 VAL 150 142 142 VAL VAL D . n 
D 1 151 ASP 151 143 143 ASP ASP D . n 
D 1 152 HIS 152 144 144 HIS HIS D . n 
D 1 153 TYR 153 145 145 TYR TYR D . n 
D 1 154 THR 154 146 146 THR THR D . n 
D 1 155 TYR 155 147 147 TYR TYR D . n 
D 1 156 VAL 156 148 148 VAL VAL D . n 
D 1 157 PHE 157 149 149 PHE PHE D . n 
D 1 158 MET 158 150 150 MET MET D . n 
D 1 159 GLY 159 151 151 GLY GLY D . n 
D 1 160 ASP 160 152 152 ASP ASP D . n 
D 1 161 GLY 161 153 153 GLY GLY D . n 
D 1 162 OCS 162 154 154 OCS OCS D . n 
D 1 163 LEU 163 155 155 LEU LEU D . n 
D 1 164 MET 164 156 156 MET MET D . n 
D 1 165 GLU 165 157 157 GLU GLU D . n 
D 1 166 GLY 166 158 158 GLY GLY D . n 
D 1 167 VAL 167 159 159 VAL VAL D . n 
D 1 168 SER 168 160 160 SER SER D . n 
D 1 169 HIS 169 161 161 HIS HIS D . n 
D 1 170 GLU 170 162 162 GLU GLU D . n 
D 1 171 ALA 171 163 163 ALA ALA D . n 
D 1 172 CYS 172 164 164 CYS CYS D . n 
D 1 173 SER 173 165 165 SER SER D . n 
D 1 174 LEU 174 166 166 LEU LEU D . n 
D 1 175 ALA 175 167 167 ALA ALA D . n 
D 1 176 GLY 176 168 168 GLY GLY D . n 
D 1 177 THR 177 169 169 THR THR D . n 
D 1 178 LEU 178 170 170 LEU LEU D . n 
D 1 179 GLY 179 171 171 GLY GLY D . n 
D 1 180 LEU 180 172 172 LEU LEU D . n 
D 1 181 GLY 181 173 173 GLY GLY D . n 
D 1 182 LYS 182 174 174 LYS LYS D . n 
D 1 183 LEU 183 175 175 LEU LEU D . n 
D 1 184 ILE 184 176 176 ILE ILE D . n 
D 1 185 VAL 185 177 177 VAL VAL D . n 
D 1 186 LEU 186 178 178 LEU LEU D . n 
D 1 187 TYR 187 179 179 TYR TYR D . n 
D 1 188 ASP 188 180 180 ASP ASP D . n 
D 1 189 ASP 189 181 181 ASP ASP D . n 
D 1 190 ASN 190 182 182 ASN ASN D . n 
D 1 191 ASN 191 183 ?   ?   ?   D . n 
D 1 192 ILE 192 184 ?   ?   ?   D . n 
D 1 193 SER 193 185 ?   ?   ?   D . n 
D 1 194 ILE 194 186 ?   ?   ?   D . n 
D 1 195 ASP 195 187 ?   ?   ?   D . n 
D 1 196 GLY 196 188 ?   ?   ?   D . n 
D 1 197 LYS 197 189 ?   ?   ?   D . n 
D 1 198 VAL 198 190 ?   ?   ?   D . n 
D 1 199 ASP 199 191 191 ASP ASP D . n 
D 1 200 GLY 200 192 192 GLY GLY D . n 
D 1 201 TRP 201 193 193 TRP TRP D . n 
D 1 202 PHE 202 194 194 PHE PHE D . n 
D 1 203 THR 203 195 195 THR THR D . n 
D 1 204 GLU 204 196 196 GLU GLU D . n 
D 1 205 ASN 205 197 197 ASN ASN D . n 
D 1 206 ILE 206 198 198 ILE ILE D . n 
D 1 207 PRO 207 199 199 PRO PRO D . n 
D 1 208 GLN 208 200 200 GLN GLN D . n 
D 1 209 ARG 209 201 201 ARG ARG D . n 
D 1 210 PHE 210 202 202 PHE PHE D . n 
D 1 211 GLU 211 203 203 GLU GLU D . n 
D 1 212 SER 212 204 204 SER SER D . n 
D 1 213 TYR 213 205 205 TYR TYR D . n 
D 1 214 GLY 214 206 206 GLY GLY D . n 
D 1 215 TRP 215 207 207 TRP TRP D . n 
D 1 216 HIS 216 208 208 HIS HIS D . n 
D 1 217 VAL 217 209 209 VAL VAL D . n 
D 1 218 VAL 218 210 210 VAL VAL D . n 
D 1 219 PRO 219 211 211 PRO PRO D . n 
D 1 220 ASN 220 212 212 ASN ASN D . n 
D 1 221 VAL 221 213 213 VAL VAL D . n 
D 1 222 ASN 222 214 214 ASN ASN D . n 
D 1 223 GLY 223 215 215 GLY GLY D . n 
D 1 224 HIS 224 216 216 HIS HIS D . n 
D 1 225 ASP 225 217 217 ASP ASP D . n 
D 1 226 THR 226 218 218 THR THR D . n 
D 1 227 ALA 227 219 219 ALA ALA D . n 
D 1 228 ALA 228 220 220 ALA ALA D . n 
D 1 229 ILE 229 221 221 ILE ILE D . n 
D 1 230 GLN 230 222 222 GLN GLN D . n 
D 1 231 THR 231 223 223 THR THR D . n 
D 1 232 ALA 232 224 224 ALA ALA D . n 
D 1 233 ILE 233 225 225 ILE ILE D . n 
D 1 234 GLU 234 226 226 GLU GLU D . n 
D 1 235 ALA 235 227 227 ALA ALA D . n 
D 1 236 ALA 236 228 228 ALA ALA D . n 
D 1 237 ARG 237 229 229 ARG ARG D . n 
D 1 238 ALA 238 230 230 ALA ALA D . n 
D 1 239 GLU 239 231 231 GLU GLU D . n 
D 1 240 THR 240 232 232 THR THR D . n 
D 1 241 GLY 241 233 233 GLY GLY D . n 
D 1 242 LYS 242 234 234 LYS LYS D . n 
D 1 243 PRO 243 235 235 PRO PRO D . n 
D 1 244 SER 244 236 236 SER SER D . n 
D 1 245 ILE 245 237 237 ILE ILE D . n 
D 1 246 ILE 246 238 238 ILE ILE D . n 
D 1 247 CYS 247 239 239 CYS CYS D . n 
D 1 248 CYS 248 240 240 CYS CYS D . n 
D 1 249 LYS 249 241 241 LYS LYS D . n 
D 1 250 THR 250 242 242 THR THR D . n 
D 1 251 LEU 251 243 243 LEU LEU D . n 
D 1 252 ILE 252 244 244 ILE ILE D . n 
D 1 253 GLY 253 245 245 GLY GLY D . n 
D 1 254 LYS 254 246 246 LYS LYS D . n 
D 1 255 GLY 255 247 247 GLY GLY D . n 
D 1 256 SER 256 248 248 SER SER D . n 
D 1 257 ALA 257 249 249 ALA ALA D . n 
D 1 258 ASN 258 250 250 ASN ASN D . n 
D 1 259 LYS 259 251 251 LYS LYS D . n 
D 1 260 GLU 260 252 252 GLU GLU D . n 
D 1 261 GLY 261 253 253 GLY GLY D . n 
D 1 262 SER 262 254 254 SER SER D . n 
D 1 263 HIS 263 255 255 HIS HIS D . n 
D 1 264 LYS 264 256 256 LYS LYS D . n 
D 1 265 THR 265 257 257 THR THR D . n 
D 1 266 HIS 266 258 258 HIS HIS D . n 
D 1 267 GLY 267 259 259 GLY GLY D . n 
D 1 268 ALA 268 260 260 ALA ALA D . n 
D 1 269 PRO 269 261 261 PRO PRO D . n 
D 1 270 LEU 270 262 262 LEU LEU D . n 
D 1 271 GLY 271 263 263 GLY GLY D . n 
D 1 272 ALA 272 264 264 ALA ALA D . n 
D 1 273 ASP 273 265 265 ASP ASP D . n 
D 1 274 GLU 274 266 266 GLU GLU D . n 
D 1 275 ILE 275 267 267 ILE ILE D . n 
D 1 276 GLU 276 268 268 GLU GLU D . n 
D 1 277 ALA 277 269 269 ALA ALA D . n 
D 1 278 THR 278 270 270 THR THR D . n 
D 1 279 ARG 279 271 271 ARG ARG D . n 
D 1 280 LYS 280 272 272 LYS LYS D . n 
D 1 281 HIS 281 273 273 HIS HIS D . n 
D 1 282 LEU 282 274 274 LEU LEU D . n 
D 1 283 GLY 283 275 275 GLY GLY D . n 
D 1 284 TRP 284 276 276 TRP TRP D . n 
D 1 285 ALA 285 277 277 ALA ALA D . n 
D 1 286 TYR 286 278 278 TYR TYR D . n 
D 1 287 PRO 287 279 279 PRO PRO D . n 
D 1 288 ALA 288 280 280 ALA ALA D . n 
D 1 289 PHE 289 281 281 PHE PHE D . n 
D 1 290 GLU 290 282 282 GLU GLU D . n 
D 1 291 ILE 291 283 283 ILE ILE D . n 
D 1 292 PRO 292 284 284 PRO PRO D . n 
D 1 293 GLN 293 285 285 GLN GLN D . n 
D 1 294 GLU 294 286 286 GLU GLU D . n 
D 1 295 ILE 295 287 287 ILE ILE D . n 
D 1 296 TYR 296 288 288 TYR TYR D . n 
D 1 297 ASP 297 289 289 ASP ASP D . n 
D 1 298 ALA 298 290 290 ALA ALA D . n 
D 1 299 TRP 299 291 291 TRP TRP D . n 
D 1 300 ASN 300 292 292 ASN ASN D . n 
D 1 301 ALA 301 293 293 ALA ALA D . n 
D 1 302 LYS 302 294 294 LYS LYS D . n 
D 1 303 GLU 303 295 295 GLU GLU D . n 
D 1 304 LYS 304 296 296 LYS LYS D . n 
D 1 305 GLY 305 297 297 GLY GLY D . n 
D 1 306 ALA 306 298 298 ALA ALA D . n 
D 1 307 LYS 307 299 299 LYS LYS D . n 
D 1 308 LEU 308 300 300 LEU LEU D . n 
D 1 309 GLU 309 301 301 GLU GLU D . n 
D 1 310 ALA 310 302 302 ALA ALA D . n 
D 1 311 GLY 311 303 303 GLY GLY D . n 
D 1 312 TRP 312 304 304 TRP TRP D . n 
D 1 313 ASN 313 305 305 ASN ASN D . n 
D 1 314 GLU 314 306 306 GLU GLU D . n 
D 1 315 LEU 315 307 307 LEU LEU D . n 
D 1 316 PHE 316 308 308 PHE PHE D . n 
D 1 317 ALA 317 309 309 ALA ALA D . n 
D 1 318 GLN 318 310 310 GLN GLN D . n 
D 1 319 TYR 319 311 311 TYR TYR D . n 
D 1 320 GLN 320 312 312 GLN GLN D . n 
D 1 321 ALA 321 313 313 ALA ALA D . n 
D 1 322 LYS 322 314 314 LYS LYS D . n 
D 1 323 TYR 323 315 315 TYR TYR D . n 
D 1 324 PRO 324 316 316 PRO PRO D . n 
D 1 325 ALA 325 317 317 ALA ALA D . n 
D 1 326 GLU 326 318 318 GLU GLU D . n 
D 1 327 ALA 327 319 319 ALA ALA D . n 
D 1 328 ALA 328 320 320 ALA ALA D . n 
D 1 329 GLU 329 321 321 GLU GLU D . n 
D 1 330 PHE 330 322 322 PHE PHE D . n 
D 1 331 VAL 331 323 323 VAL VAL D . n 
D 1 332 ARG 332 324 324 ARG ARG D . n 
D 1 333 ARG 333 325 325 ARG ARG D . n 
D 1 334 MET 334 326 326 MET MET D . n 
D 1 335 ASP 335 327 327 ASP ASP D . n 
D 1 336 LYS 336 328 328 LYS LYS D . n 
D 1 337 LYS 337 329 329 LYS LYS D . n 
D 1 338 LEU 338 330 330 LEU LEU D . n 
D 1 339 PRO 339 331 331 PRO PRO D . n 
D 1 340 GLU 340 332 332 GLU GLU D . n 
D 1 341 ASN 341 333 333 ASN ASN D . n 
D 1 342 PHE 342 334 334 PHE PHE D . n 
D 1 343 ASP 343 335 335 ASP ASP D . n 
D 1 344 GLU 344 336 336 GLU GLU D . n 
D 1 345 TYR 345 337 337 TYR TYR D . n 
D 1 346 VAL 346 338 338 VAL VAL D . n 
D 1 347 GLN 347 339 339 GLN GLN D . n 
D 1 348 THR 348 340 340 THR THR D . n 
D 1 349 ALA 349 341 341 ALA ALA D . n 
D 1 350 LEU 350 342 342 LEU LEU D . n 
D 1 351 LYS 351 343 343 LYS LYS D . n 
D 1 352 GLU 352 344 344 GLU GLU D . n 
D 1 353 VAL 353 345 345 VAL VAL D . n 
D 1 354 CYS 354 346 346 CYS CYS D . n 
D 1 355 ALA 355 347 347 ALA ALA D . n 
D 1 356 LYS 356 348 348 LYS LYS D . n 
D 1 357 ALA 357 349 ?   ?   ?   D . n 
D 1 358 GLU 358 350 ?   ?   ?   D . n 
D 1 359 THR 359 351 ?   ?   ?   D . n 
D 1 360 VAL 360 352 ?   ?   ?   D . n 
D 1 361 ALA 361 353 ?   ?   ?   D . n 
D 1 362 THR 362 354 ?   ?   ?   D . n 
D 1 363 ARG 363 355 ?   ?   ?   D . n 
D 1 364 LYS 364 356 ?   ?   ?   D . n 
D 1 365 ALA 365 357 ?   ?   ?   D . n 
D 1 366 SER 366 358 ?   ?   ?   D . n 
D 1 367 GLN 367 359 ?   ?   ?   D . n 
D 1 368 ASN 368 360 360 ASN ASN D . n 
D 1 369 SER 369 361 361 SER SER D . n 
D 1 370 ILE 370 362 362 ILE ILE D . n 
D 1 371 GLU 371 363 363 GLU GLU D . n 
D 1 372 ILE 372 364 364 ILE ILE D . n 
D 1 373 LEU 373 365 365 LEU LEU D . n 
D 1 374 ALA 374 366 366 ALA ALA D . n 
D 1 375 LYS 375 367 367 LYS LYS D . n 
D 1 376 GLU 376 368 368 GLU GLU D . n 
D 1 377 LEU 377 369 369 LEU LEU D . n 
D 1 378 PRO 378 370 370 PRO PRO D . n 
D 1 379 GLU 379 371 371 GLU GLU D . n 
D 1 380 LEU 380 372 372 LEU LEU D . n 
D 1 381 VAL 381 373 373 VAL VAL D . n 
D 1 382 GLY 382 374 374 GLY GLY D . n 
D 1 383 GLY 383 375 375 GLY GLY D . n 
D 1 384 SER 384 376 376 SER SER D . n 
D 1 385 ALA 385 377 377 ALA ALA D . n 
D 1 386 ASP 386 378 378 ASP ASP D . n 
D 1 387 LEU 387 379 379 LEU LEU D . n 
D 1 388 THR 388 380 380 THR THR D . n 
D 1 389 PRO 389 381 381 PRO PRO D . n 
D 1 390 SER 390 382 382 SER SER D . n 
D 1 391 ASN 391 383 383 ASN ASN D . n 
D 1 392 LEU 392 384 384 LEU LEU D . n 
D 1 393 THR 393 385 385 THR THR D . n 
D 1 394 ASP 394 386 386 ASP ASP D . n 
D 1 395 TRP 395 387 387 TRP TRP D . n 
D 1 396 SER 396 388 388 SER SER D . n 
D 1 397 ASN 397 389 389 ASN ASN D . n 
D 1 398 SER 398 390 390 SER SER D . n 
D 1 399 VAL 399 391 391 VAL VAL D . n 
D 1 400 SER 400 392 392 SER SER D . n 
D 1 401 VAL 401 393 393 VAL VAL D . n 
D 1 402 THR 402 394 394 THR THR D . n 
D 1 403 ARG 403 395 395 ARG ARG D . n 
D 1 404 ASP 404 396 396 ASP ASP D . n 
D 1 405 LYS 405 397 397 LYS LYS D . n 
D 1 406 GLY 406 398 398 GLY GLY D . n 
D 1 407 GLY 407 399 399 GLY GLY D . n 
D 1 408 ASN 408 400 400 ASN ASN D . n 
D 1 409 TYR 409 401 401 TYR TYR D . n 
D 1 410 ILE 410 402 402 ILE ILE D . n 
D 1 411 HIS 411 403 403 HIS HIS D . n 
D 1 412 TYR 412 404 404 TYR TYR D . n 
D 1 413 GLY 413 405 405 GLY GLY D . n 
D 1 414 VAL 414 406 406 VAL VAL D . n 
D 1 415 ARG 415 407 407 ARG ARG D . n 
D 1 416 GLU 416 408 408 GLU GLU D . n 
D 1 417 PHE 417 409 409 PHE PHE D . n 
D 1 418 GLY 418 410 410 GLY GLY D . n 
D 1 419 MET 419 411 411 MET MET D . n 
D 1 420 GLY 420 412 412 GLY GLY D . n 
D 1 421 ALA 421 413 413 ALA ALA D . n 
D 1 422 ILE 422 414 414 ILE ILE D . n 
D 1 423 MET 423 415 415 MET MET D . n 
D 1 424 ASN 424 416 416 ASN ASN D . n 
D 1 425 GLY 425 417 417 GLY GLY D . n 
D 1 426 LEU 426 418 418 LEU LEU D . n 
D 1 427 VAL 427 419 419 VAL VAL D . n 
D 1 428 LEU 428 420 420 LEU LEU D . n 
D 1 429 HIS 429 421 421 HIS HIS D . n 
D 1 430 GLY 430 422 422 GLY GLY D . n 
D 1 431 GLY 431 423 423 GLY GLY D . n 
D 1 432 VAL 432 424 424 VAL VAL D . n 
D 1 433 LYS 433 425 425 LYS LYS D . n 
D 1 434 PRO 434 426 426 PRO PRO D . n 
D 1 435 PHE 435 427 427 PHE PHE D . n 
D 1 436 GLY 436 428 428 GLY GLY D . n 
D 1 437 ALA 437 429 429 ALA ALA D . n 
D 1 438 THR 438 430 430 THR THR D . n 
D 1 439 PHE 439 431 431 PHE PHE D . n 
D 1 440 LEU 440 432 432 LEU LEU D . n 
D 1 441 MET 441 433 433 MET MET D . n 
D 1 442 PHE 442 434 434 PHE PHE D . n 
D 1 443 SER 443 435 435 SER SER D . n 
D 1 444 GLU 444 436 436 GLU GLU D . n 
D 1 445 TYR 445 437 437 TYR TYR D . n 
D 1 446 GLU 446 438 438 GLU GLU D . n 
D 1 447 ARG 447 439 439 ARG ARG D . n 
D 1 448 ASN 448 440 440 ASN ASN D . n 
D 1 449 ALA 449 441 441 ALA ALA D . n 
D 1 450 LEU 450 442 442 LEU LEU D . n 
D 1 451 ARG 451 443 443 ARG ARG D . n 
D 1 452 MET 452 444 444 MET MET D . n 
D 1 453 ALA 453 445 445 ALA ALA D . n 
D 1 454 ALA 454 446 446 ALA ALA D . n 
D 1 455 LEU 455 447 447 LEU LEU D . n 
D 1 456 MET 456 448 448 MET MET D . n 
D 1 457 LYS 457 449 449 LYS LYS D . n 
D 1 458 ILE 458 450 450 ILE ILE D . n 
D 1 459 ASN 459 451 451 ASN ASN D . n 
D 1 460 PRO 460 452 452 PRO PRO D . n 
D 1 461 VAL 461 453 453 VAL VAL D . n 
D 1 462 PHE 462 454 454 PHE PHE D . n 
D 1 463 VAL 463 455 455 VAL VAL D . n 
D 1 464 PHE 464 456 456 PHE PHE D . n 
D 1 465 THR 465 457 457 THR THR D . n 
D 1 466 HIS 466 458 458 HIS HIS D . n 
D 1 467 ASP 467 459 459 ASP ASP D . n 
D 1 468 SER 468 460 460 SER SER D . n 
D 1 469 ILE 469 461 461 ILE ILE D . n 
D 1 470 GLY 470 462 462 GLY GLY D . n 
D 1 471 LEU 471 463 463 LEU LEU D . n 
D 1 472 GLY 472 464 464 GLY GLY D . n 
D 1 473 GLU 473 465 465 GLU GLU D . n 
D 1 474 ASP 474 466 466 ASP ASP D . n 
D 1 475 GLY 475 467 467 GLY GLY D . n 
D 1 476 PRO 476 468 468 PRO PRO D . n 
D 1 477 THR 477 469 469 THR THR D . n 
D 1 478 HIS 478 470 470 HIS HIS D . n 
D 1 479 GLN 479 471 471 GLN GLN D . n 
D 1 480 PRO 480 472 472 PRO PRO D . n 
D 1 481 ILE 481 473 473 ILE ILE D . n 
D 1 482 GLU 482 474 474 GLU GLU D . n 
D 1 483 GLN 483 475 475 GLN GLN D . n 
D 1 484 THR 484 476 476 THR THR D . n 
D 1 485 ALA 485 477 477 ALA ALA D . n 
D 1 486 THR 486 478 478 THR THR D . n 
D 1 487 LEU 487 479 479 LEU LEU D . n 
D 1 488 ARG 488 480 480 ARG ARG D . n 
D 1 489 LEU 489 481 481 LEU LEU D . n 
D 1 490 ILE 490 482 482 ILE ILE D . n 
D 1 491 PRO 491 483 483 PRO PRO D . n 
D 1 492 ASN 492 484 484 ASN ASN D . n 
D 1 493 MET 493 485 485 MET MET D . n 
D 1 494 ASP 494 486 486 ASP ASP D . n 
D 1 495 VAL 495 487 487 VAL VAL D . n 
D 1 496 TRP 496 488 488 TRP TRP D . n 
D 1 497 ARG 497 489 489 ARG ARG D . n 
D 1 498 PRO 498 490 490 PRO PRO D . n 
D 1 499 CYS 499 491 491 CYS CYS D . n 
D 1 500 ASP 500 492 492 ASP ASP D . n 
D 1 501 THR 501 493 493 THR THR D . n 
D 1 502 ALA 502 494 494 ALA ALA D . n 
D 1 503 GLU 503 495 495 GLU GLU D . n 
D 1 504 SER 504 496 496 SER SER D . n 
D 1 505 LEU 505 497 497 LEU LEU D . n 
D 1 506 VAL 506 498 498 VAL VAL D . n 
D 1 507 ALA 507 499 499 ALA ALA D . n 
D 1 508 TRP 508 500 500 TRP TRP D . n 
D 1 509 ALA 509 501 501 ALA ALA D . n 
D 1 510 GLU 510 502 502 GLU GLU D . n 
D 1 511 ALA 511 503 503 ALA ALA D . n 
D 1 512 ALA 512 504 504 ALA ALA D . n 
D 1 513 LYS 513 505 505 LYS LYS D . n 
D 1 514 ALA 514 506 506 ALA ALA D . n 
D 1 515 GLU 515 507 507 GLU GLU D . n 
D 1 516 ASP 516 508 508 ASP ASP D . n 
D 1 517 HIS 517 509 509 HIS HIS D . n 
D 1 518 PRO 518 510 510 PRO PRO D . n 
D 1 519 SER 519 511 511 SER SER D . n 
D 1 520 CYS 520 512 512 CYS CYS D . n 
D 1 521 LEU 521 513 513 LEU LEU D . n 
D 1 522 ILE 522 514 514 ILE ILE D . n 
D 1 523 PHE 523 515 515 PHE PHE D . n 
D 1 524 SER 524 516 516 SER SER D . n 
D 1 525 ARG 525 517 517 ARG ARG D . n 
D 1 526 GLN 526 518 518 GLN GLN D . n 
D 1 527 ASN 527 519 519 ASN ASN D . n 
D 1 528 LEU 528 520 520 LEU LEU D . n 
D 1 529 LYS 529 521 521 LYS LYS D . n 
D 1 530 PHE 530 522 522 PHE PHE D . n 
D 1 531 GLN 531 523 523 GLN GLN D . n 
D 1 532 ALA 532 524 524 ALA ALA D . n 
D 1 533 ARG 533 525 525 ARG ARG D . n 
D 1 534 SER 534 526 526 SER SER D . n 
D 1 535 GLU 535 527 527 GLU GLU D . n 
D 1 536 GLN 536 528 528 GLN GLN D . n 
D 1 537 GLN 537 529 529 GLN GLN D . n 
D 1 538 LEU 538 530 530 LEU LEU D . n 
D 1 539 ASN 539 531 531 ASN ASN D . n 
D 1 540 ASP 540 532 532 ASP ASP D . n 
D 1 541 ILE 541 533 533 ILE ILE D . n 
D 1 542 LYS 542 534 534 LYS LYS D . n 
D 1 543 ARG 543 535 535 ARG ARG D . n 
D 1 544 GLY 544 536 536 GLY GLY D . n 
D 1 545 ALA 545 537 537 ALA ALA D . n 
D 1 546 TYR 546 538 538 TYR TYR D . n 
D 1 547 VAL 547 539 539 VAL VAL D . n 
D 1 548 ILE 548 540 540 ILE ILE D . n 
D 1 549 SER 549 541 541 SER SER D . n 
D 1 550 GLU 550 542 542 GLU GLU D . n 
D 1 551 ALA 551 543 543 ALA ALA D . n 
D 1 552 GLN 552 544 544 GLN GLN D . n 
D 1 553 GLY 553 545 545 GLY GLY D . n 
D 1 554 ASN 554 546 546 ASN ASN D . n 
D 1 555 ALA 555 547 547 ALA ALA D . n 
D 1 556 GLN 556 548 548 GLN GLN D . n 
D 1 557 ALA 557 549 549 ALA ALA D . n 
D 1 558 VAL 558 550 550 VAL VAL D . n 
D 1 559 ILE 559 551 551 ILE ILE D . n 
D 1 560 ILE 560 552 552 ILE ILE D . n 
D 1 561 ALA 561 553 553 ALA ALA D . n 
D 1 562 THR 562 554 554 THR THR D . n 
D 1 563 GLY 563 555 555 GLY GLY D . n 
D 1 564 SER 564 556 556 SER SER D . n 
D 1 565 GLU 565 557 557 GLU GLU D . n 
D 1 566 VAL 566 558 558 VAL VAL D . n 
D 1 567 GLY 567 559 559 GLY GLY D . n 
D 1 568 LEU 568 560 560 LEU LEU D . n 
D 1 569 ALA 569 561 561 ALA ALA D . n 
D 1 570 VAL 570 562 562 VAL VAL D . n 
D 1 571 GLU 571 563 563 GLU GLU D . n 
D 1 572 ALA 572 564 564 ALA ALA D . n 
D 1 573 GLN 573 565 565 GLN GLN D . n 
D 1 574 LYS 574 566 566 LYS LYS D . n 
D 1 575 VAL 575 567 567 VAL VAL D . n 
D 1 576 LEU 576 568 568 LEU LEU D . n 
D 1 577 ALA 577 569 569 ALA ALA D . n 
D 1 578 GLY 578 570 570 GLY GLY D . n 
D 1 579 GLN 579 571 571 GLN GLN D . n 
D 1 580 GLY 580 572 572 GLY GLY D . n 
D 1 581 ILE 581 573 573 ILE ILE D . n 
D 1 582 ALA 582 574 574 ALA ALA D . n 
D 1 583 VAL 583 575 575 VAL VAL D . n 
D 1 584 ARG 584 576 576 ARG ARG D . n 
D 1 585 VAL 585 577 577 VAL VAL D . n 
D 1 586 VAL 586 578 578 VAL VAL D . n 
D 1 587 SER 587 579 579 SER SER D . n 
D 1 588 MET 588 580 580 MET MET D . n 
D 1 589 PRO 589 581 581 PRO PRO D . n 
D 1 590 SER 590 582 582 SER SER D . n 
D 1 591 THR 591 583 583 THR THR D . n 
D 1 592 SER 592 584 584 SER SER D . n 
D 1 593 VAL 593 585 585 VAL VAL D . n 
D 1 594 PHE 594 586 586 PHE PHE D . n 
D 1 595 ASP 595 587 587 ASP ASP D . n 
D 1 596 ARG 596 588 588 ARG ARG D . n 
D 1 597 GLN 597 589 589 GLN GLN D . n 
D 1 598 ASP 598 590 590 ASP ASP D . n 
D 1 599 ALA 599 591 591 ALA ALA D . n 
D 1 600 ALA 600 592 592 ALA ALA D . n 
D 1 601 TYR 601 593 593 TYR TYR D . n 
D 1 602 GLN 602 594 594 GLN GLN D . n 
D 1 603 ALA 603 595 595 ALA ALA D . n 
D 1 604 ALA 604 596 596 ALA ALA D . n 
D 1 605 VAL 605 597 597 VAL VAL D . n 
D 1 606 LEU 606 598 598 LEU LEU D . n 
D 1 607 PRO 607 599 599 PRO PRO D . n 
D 1 608 GLU 608 600 600 GLU GLU D . n 
D 1 609 GLY 609 601 601 GLY GLY D . n 
D 1 610 LEU 610 602 602 LEU LEU D . n 
D 1 611 PRO 611 603 603 PRO PRO D . n 
D 1 612 ARG 612 604 604 ARG ARG D . n 
D 1 613 ILE 613 605 605 ILE ILE D . n 
D 1 614 ALA 614 606 606 ALA ALA D . n 
D 1 615 VAL 615 607 607 VAL VAL D . n 
D 1 616 GLU 616 608 608 GLU GLU D . n 
D 1 617 ALA 617 609 609 ALA ALA D . n 
D 1 618 GLY 618 610 610 GLY GLY D . n 
D 1 619 HIS 619 611 611 HIS HIS D . n 
D 1 620 THR 620 612 612 THR THR D . n 
D 1 621 ASN 621 613 613 ASN ASN D . n 
D 1 622 GLY 622 614 614 GLY GLY D . n 
D 1 623 TRP 623 615 615 TRP TRP D . n 
D 1 624 TYR 624 616 616 TYR TYR D . n 
D 1 625 LYS 625 617 617 LYS LYS D . n 
D 1 626 TYR 626 618 618 TYR TYR D . n 
D 1 627 VAL 627 619 619 VAL VAL D . n 
D 1 628 GLY 628 620 620 GLY GLY D . n 
D 1 629 LEU 629 621 621 LEU LEU D . n 
D 1 630 ASN 630 622 622 ASN ASN D . n 
D 1 631 GLY 631 623 623 GLY GLY D . n 
D 1 632 ALA 632 624 624 ALA ALA D . n 
D 1 633 VAL 633 625 625 VAL VAL D . n 
D 1 634 VAL 634 626 626 VAL VAL D . n 
D 1 635 GLY 635 627 627 GLY GLY D . n 
D 1 636 ILE 636 628 628 ILE ILE D . n 
D 1 637 ASN 637 629 629 ASN ASN D . n 
D 1 638 ARG 638 630 630 ARG ARG D . n 
D 1 639 PHE 639 631 631 PHE PHE D . n 
D 1 640 GLY 640 632 632 GLY GLY D . n 
D 1 641 GLU 641 633 633 GLU GLU D . n 
D 1 642 SER 642 634 634 SER SER D . n 
D 1 643 ALA 643 635 635 ALA ALA D . n 
D 1 644 PRO 644 636 636 PRO PRO D . n 
D 1 645 ALA 645 637 637 ALA ALA D . n 
D 1 646 ASP 646 638 638 ASP ASP D . n 
D 1 647 LEU 647 639 639 LEU LEU D . n 
D 1 648 LEU 648 640 640 LEU LEU D . n 
D 1 649 PHE 649 641 641 PHE PHE D . n 
D 1 650 LYS 650 642 642 LYS LYS D . n 
D 1 651 ALA 651 643 643 ALA ALA D . n 
D 1 652 PHE 652 644 644 PHE PHE D . n 
D 1 653 GLY 653 645 645 GLY GLY D . n 
D 1 654 PHE 654 646 646 PHE PHE D . n 
D 1 655 THR 655 647 647 THR THR D . n 
D 1 656 VAL 656 648 648 VAL VAL D . n 
D 1 657 ASP 657 649 649 ASP ASP D . n 
D 1 658 ASN 658 650 650 ASN ASN D . n 
D 1 659 VAL 659 651 651 VAL VAL D . n 
D 1 660 VAL 660 652 652 VAL VAL D . n 
D 1 661 ASP 661 653 653 ASP ASP D . n 
D 1 662 THR 662 654 654 THR THR D . n 
D 1 663 VAL 663 655 655 VAL VAL D . n 
D 1 664 LYS 664 656 656 LYS LYS D . n 
D 1 665 SER 665 657 657 SER SER D . n 
D 1 666 VAL 666 658 658 VAL VAL D . n 
D 1 667 LEU 667 659 659 LEU LEU D . n 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 EDO 1   701  5    EDO EDO A . 
F 3 CA  1   702  4    CA  CA  A . 
G 3 CA  1   703  10   CA  CA  A . 
H 3 CA  1   704  11   CA  CA  A . 
I 3 CA  1   701  3    CA  CA  B . 
J 3 CA  1   702  5    CA  CA  B . 
K 3 CA  1   703  12   CA  CA  B . 
L 2 EDO 1   701  1    EDO EDO C . 
M 2 EDO 1   702  6    EDO EDO C . 
N 3 CA  1   703  1    CA  CA  C . 
O 3 CA  1   704  2    CA  CA  C . 
P 3 CA  1   705  7    CA  CA  C . 
Q 2 EDO 1   701  2    EDO EDO D . 
R 2 EDO 1   702  3    EDO EDO D . 
S 2 EDO 1   703  4    EDO EDO D . 
T 3 CA  1   704  6    CA  CA  D . 
U 3 CA  1   705  8    CA  CA  D . 
V 3 CA  1   706  9    CA  CA  D . 
W 4 HOH 1   801  1702 HOH HOH A . 
W 4 HOH 2   802  1679 HOH HOH A . 
W 4 HOH 3   803  778  HOH HOH A . 
W 4 HOH 4   804  959  HOH HOH A . 
W 4 HOH 5   805  1970 HOH HOH A . 
W 4 HOH 6   806  1723 HOH HOH A . 
W 4 HOH 7   807  2082 HOH HOH A . 
W 4 HOH 8   808  2055 HOH HOH A . 
W 4 HOH 9   809  828  HOH HOH A . 
W 4 HOH 10  810  2081 HOH HOH A . 
W 4 HOH 11  811  1682 HOH HOH A . 
W 4 HOH 12  812  714  HOH HOH A . 
W 4 HOH 13  813  453  HOH HOH A . 
W 4 HOH 14  814  1049 HOH HOH A . 
W 4 HOH 15  815  1674 HOH HOH A . 
W 4 HOH 16  816  1683 HOH HOH A . 
W 4 HOH 17  817  1011 HOH HOH A . 
W 4 HOH 18  818  831  HOH HOH A . 
W 4 HOH 19  819  1978 HOH HOH A . 
W 4 HOH 20  820  1543 HOH HOH A . 
W 4 HOH 21  821  834  HOH HOH A . 
W 4 HOH 22  822  1695 HOH HOH A . 
W 4 HOH 23  823  1719 HOH HOH A . 
W 4 HOH 24  824  1655 HOH HOH A . 
W 4 HOH 25  825  1666 HOH HOH A . 
W 4 HOH 26  826  930  HOH HOH A . 
W 4 HOH 27  827  965  HOH HOH A . 
W 4 HOH 28  828  719  HOH HOH A . 
W 4 HOH 29  829  564  HOH HOH A . 
W 4 HOH 30  830  1578 HOH HOH A . 
W 4 HOH 31  831  546  HOH HOH A . 
W 4 HOH 32  832  1533 HOH HOH A . 
W 4 HOH 33  833  1398 HOH HOH A . 
W 4 HOH 34  834  416  HOH HOH A . 
W 4 HOH 35  835  269  HOH HOH A . 
W 4 HOH 36  836  24   HOH HOH A . 
W 4 HOH 37  837  731  HOH HOH A . 
W 4 HOH 38  838  1665 HOH HOH A . 
W 4 HOH 39  839  617  HOH HOH A . 
W 4 HOH 40  840  441  HOH HOH A . 
W 4 HOH 41  841  394  HOH HOH A . 
W 4 HOH 42  842  1656 HOH HOH A . 
W 4 HOH 43  843  1158 HOH HOH A . 
W 4 HOH 44  844  1197 HOH HOH A . 
W 4 HOH 45  845  766  HOH HOH A . 
W 4 HOH 46  846  271  HOH HOH A . 
W 4 HOH 47  847  1735 HOH HOH A . 
W 4 HOH 48  848  974  HOH HOH A . 
W 4 HOH 49  849  358  HOH HOH A . 
W 4 HOH 50  850  2085 HOH HOH A . 
W 4 HOH 51  851  422  HOH HOH A . 
W 4 HOH 52  852  85   HOH HOH A . 
W 4 HOH 53  853  2080 HOH HOH A . 
W 4 HOH 54  854  1974 HOH HOH A . 
W 4 HOH 55  855  597  HOH HOH A . 
W 4 HOH 56  856  505  HOH HOH A . 
W 4 HOH 57  857  1567 HOH HOH A . 
W 4 HOH 58  858  1688 HOH HOH A . 
W 4 HOH 59  859  314  HOH HOH A . 
W 4 HOH 60  860  1022 HOH HOH A . 
W 4 HOH 61  861  347  HOH HOH A . 
W 4 HOH 62  862  1544 HOH HOH A . 
W 4 HOH 63  863  1035 HOH HOH A . 
W 4 HOH 64  864  595  HOH HOH A . 
W 4 HOH 65  865  1259 HOH HOH A . 
W 4 HOH 66  866  1263 HOH HOH A . 
W 4 HOH 67  867  500  HOH HOH A . 
W 4 HOH 68  868  26   HOH HOH A . 
W 4 HOH 69  869  489  HOH HOH A . 
W 4 HOH 70  870  362  HOH HOH A . 
W 4 HOH 71  871  224  HOH HOH A . 
W 4 HOH 72  872  184  HOH HOH A . 
W 4 HOH 73  873  469  HOH HOH A . 
W 4 HOH 74  874  395  HOH HOH A . 
W 4 HOH 75  875  1714 HOH HOH A . 
W 4 HOH 76  876  319  HOH HOH A . 
W 4 HOH 77  877  1722 HOH HOH A . 
W 4 HOH 78  878  430  HOH HOH A . 
W 4 HOH 79  879  154  HOH HOH A . 
W 4 HOH 80  880  679  HOH HOH A . 
W 4 HOH 81  881  414  HOH HOH A . 
W 4 HOH 82  882  675  HOH HOH A . 
W 4 HOH 83  883  496  HOH HOH A . 
W 4 HOH 84  884  447  HOH HOH A . 
W 4 HOH 85  885  1874 HOH HOH A . 
W 4 HOH 86  886  1524 HOH HOH A . 
W 4 HOH 87  887  740  HOH HOH A . 
W 4 HOH 88  888  1681 HOH HOH A . 
W 4 HOH 89  889  1228 HOH HOH A . 
W 4 HOH 90  890  373  HOH HOH A . 
W 4 HOH 91  891  713  HOH HOH A . 
W 4 HOH 92  892  338  HOH HOH A . 
W 4 HOH 93  893  1115 HOH HOH A . 
W 4 HOH 94  894  340  HOH HOH A . 
W 4 HOH 95  895  443  HOH HOH A . 
W 4 HOH 96  896  1429 HOH HOH A . 
W 4 HOH 97  897  1931 HOH HOH A . 
W 4 HOH 98  898  337  HOH HOH A . 
W 4 HOH 99  899  670  HOH HOH A . 
W 4 HOH 100 900  439  HOH HOH A . 
W 4 HOH 101 901  151  HOH HOH A . 
W 4 HOH 102 902  1597 HOH HOH A . 
W 4 HOH 103 903  1671 HOH HOH A . 
W 4 HOH 104 904  842  HOH HOH A . 
W 4 HOH 105 905  4    HOH HOH A . 
W 4 HOH 106 906  937  HOH HOH A . 
W 4 HOH 107 907  2    HOH HOH A . 
W 4 HOH 108 908  192  HOH HOH A . 
W 4 HOH 109 909  426  HOH HOH A . 
W 4 HOH 110 910  124  HOH HOH A . 
W 4 HOH 111 911  1205 HOH HOH A . 
W 4 HOH 112 912  1325 HOH HOH A . 
W 4 HOH 113 913  688  HOH HOH A . 
W 4 HOH 114 914  356  HOH HOH A . 
W 4 HOH 115 915  1644 HOH HOH A . 
W 4 HOH 116 916  202  HOH HOH A . 
W 4 HOH 117 917  61   HOH HOH A . 
W 4 HOH 118 918  437  HOH HOH A . 
W 4 HOH 119 919  641  HOH HOH A . 
W 4 HOH 120 920  371  HOH HOH A . 
W 4 HOH 121 921  393  HOH HOH A . 
W 4 HOH 122 922  1432 HOH HOH A . 
W 4 HOH 123 923  548  HOH HOH A . 
W 4 HOH 124 924  1068 HOH HOH A . 
W 4 HOH 125 925  1132 HOH HOH A . 
W 4 HOH 126 926  1150 HOH HOH A . 
W 4 HOH 127 927  1585 HOH HOH A . 
W 4 HOH 128 928  682  HOH HOH A . 
W 4 HOH 129 929  35   HOH HOH A . 
W 4 HOH 130 930  578  HOH HOH A . 
W 4 HOH 131 931  315  HOH HOH A . 
W 4 HOH 132 932  268  HOH HOH A . 
W 4 HOH 133 933  1731 HOH HOH A . 
W 4 HOH 134 934  1443 HOH HOH A . 
W 4 HOH 135 935  249  HOH HOH A . 
W 4 HOH 136 936  815  HOH HOH A . 
W 4 HOH 137 937  401  HOH HOH A . 
W 4 HOH 138 938  2078 HOH HOH A . 
W 4 HOH 139 939  316  HOH HOH A . 
W 4 HOH 140 940  160  HOH HOH A . 
W 4 HOH 141 941  916  HOH HOH A . 
W 4 HOH 142 942  90   HOH HOH A . 
W 4 HOH 143 943  206  HOH HOH A . 
W 4 HOH 144 944  1082 HOH HOH A . 
W 4 HOH 145 945  707  HOH HOH A . 
W 4 HOH 146 946  897  HOH HOH A . 
W 4 HOH 147 947  31   HOH HOH A . 
W 4 HOH 148 948  1982 HOH HOH A . 
W 4 HOH 149 949  554  HOH HOH A . 
W 4 HOH 150 950  56   HOH HOH A . 
W 4 HOH 151 951  391  HOH HOH A . 
W 4 HOH 152 952  310  HOH HOH A . 
W 4 HOH 153 953  20   HOH HOH A . 
W 4 HOH 154 954  1262 HOH HOH A . 
W 4 HOH 155 955  442  HOH HOH A . 
W 4 HOH 156 956  1560 HOH HOH A . 
W 4 HOH 157 957  640  HOH HOH A . 
W 4 HOH 158 958  428  HOH HOH A . 
W 4 HOH 159 959  389  HOH HOH A . 
W 4 HOH 160 960  1691 HOH HOH A . 
W 4 HOH 161 961  819  HOH HOH A . 
W 4 HOH 162 962  260  HOH HOH A . 
W 4 HOH 163 963  1973 HOH HOH A . 
W 4 HOH 164 964  1031 HOH HOH A . 
W 4 HOH 165 965  938  HOH HOH A . 
W 4 HOH 166 966  1523 HOH HOH A . 
W 4 HOH 167 967  862  HOH HOH A . 
W 4 HOH 168 968  188  HOH HOH A . 
W 4 HOH 169 969  484  HOH HOH A . 
W 4 HOH 170 970  306  HOH HOH A . 
W 4 HOH 171 971  1734 HOH HOH A . 
W 4 HOH 172 972  605  HOH HOH A . 
W 4 HOH 173 973  1724 HOH HOH A . 
W 4 HOH 174 974  711  HOH HOH A . 
W 4 HOH 175 975  1579 HOH HOH A . 
W 4 HOH 176 976  1440 HOH HOH A . 
W 4 HOH 177 977  1083 HOH HOH A . 
W 4 HOH 178 978  134  HOH HOH A . 
W 4 HOH 179 979  866  HOH HOH A . 
W 4 HOH 180 980  1670 HOH HOH A . 
W 4 HOH 181 981  1450 HOH HOH A . 
W 4 HOH 182 982  519  HOH HOH A . 
W 4 HOH 183 983  1217 HOH HOH A . 
W 4 HOH 184 984  1473 HOH HOH A . 
W 4 HOH 185 985  259  HOH HOH A . 
W 4 HOH 186 986  1356 HOH HOH A . 
W 4 HOH 187 987  1661 HOH HOH A . 
W 4 HOH 188 988  613  HOH HOH A . 
W 4 HOH 189 989  363  HOH HOH A . 
W 4 HOH 190 990  1981 HOH HOH A . 
W 4 HOH 191 991  45   HOH HOH A . 
W 4 HOH 192 992  1332 HOH HOH A . 
W 4 HOH 193 993  10   HOH HOH A . 
W 4 HOH 194 994  1592 HOH HOH A . 
W 4 HOH 195 995  235  HOH HOH A . 
W 4 HOH 196 996  928  HOH HOH A . 
W 4 HOH 197 997  375  HOH HOH A . 
W 4 HOH 198 998  1323 HOH HOH A . 
W 4 HOH 199 999  1485 HOH HOH A . 
W 4 HOH 200 1000 1582 HOH HOH A . 
W 4 HOH 201 1001 177  HOH HOH A . 
W 4 HOH 202 1002 285  HOH HOH A . 
W 4 HOH 203 1003 138  HOH HOH A . 
W 4 HOH 204 1004 811  HOH HOH A . 
W 4 HOH 205 1005 1278 HOH HOH A . 
W 4 HOH 206 1006 101  HOH HOH A . 
W 4 HOH 207 1007 607  HOH HOH A . 
W 4 HOH 208 1008 1678 HOH HOH A . 
W 4 HOH 209 1009 952  HOH HOH A . 
W 4 HOH 210 1010 573  HOH HOH A . 
W 4 HOH 211 1011 1408 HOH HOH A . 
W 4 HOH 212 1012 290  HOH HOH A . 
W 4 HOH 213 1013 745  HOH HOH A . 
W 4 HOH 214 1014 97   HOH HOH A . 
W 4 HOH 215 1015 54   HOH HOH A . 
W 4 HOH 216 1016 1948 HOH HOH A . 
W 4 HOH 217 1017 1694 HOH HOH A . 
W 4 HOH 218 1018 757  HOH HOH A . 
W 4 HOH 219 1019 34   HOH HOH A . 
W 4 HOH 220 1020 1254 HOH HOH A . 
W 4 HOH 221 1021 1209 HOH HOH A . 
W 4 HOH 222 1022 557  HOH HOH A . 
W 4 HOH 223 1023 169  HOH HOH A . 
W 4 HOH 224 1024 326  HOH HOH A . 
W 4 HOH 225 1025 712  HOH HOH A . 
W 4 HOH 226 1026 625  HOH HOH A . 
W 4 HOH 227 1027 374  HOH HOH A . 
W 4 HOH 228 1028 368  HOH HOH A . 
W 4 HOH 229 1029 1690 HOH HOH A . 
W 4 HOH 230 1030 1040 HOH HOH A . 
W 4 HOH 231 1031 1703 HOH HOH A . 
W 4 HOH 232 1032 1596 HOH HOH A . 
W 4 HOH 233 1033 1096 HOH HOH A . 
W 4 HOH 234 1034 359  HOH HOH A . 
W 4 HOH 235 1035 751  HOH HOH A . 
W 4 HOH 236 1036 1507 HOH HOH A . 
W 4 HOH 237 1037 971  HOH HOH A . 
W 4 HOH 238 1038 1080 HOH HOH A . 
W 4 HOH 239 1039 263  HOH HOH A . 
W 4 HOH 240 1040 956  HOH HOH A . 
W 4 HOH 241 1041 106  HOH HOH A . 
W 4 HOH 242 1042 99   HOH HOH A . 
W 4 HOH 243 1043 760  HOH HOH A . 
W 4 HOH 244 1044 2061 HOH HOH A . 
W 4 HOH 245 1045 629  HOH HOH A . 
W 4 HOH 246 1046 680  HOH HOH A . 
W 4 HOH 247 1047 36   HOH HOH A . 
W 4 HOH 248 1048 1715 HOH HOH A . 
W 4 HOH 249 1049 1964 HOH HOH A . 
W 4 HOH 250 1050 1172 HOH HOH A . 
W 4 HOH 251 1051 187  HOH HOH A . 
W 4 HOH 252 1052 1304 HOH HOH A . 
W 4 HOH 253 1053 1390 HOH HOH A . 
W 4 HOH 254 1054 1003 HOH HOH A . 
W 4 HOH 255 1055 1231 HOH HOH A . 
W 4 HOH 256 1056 494  HOH HOH A . 
W 4 HOH 257 1057 1232 HOH HOH A . 
W 4 HOH 258 1058 1426 HOH HOH A . 
W 4 HOH 259 1059 1692 HOH HOH A . 
W 4 HOH 260 1060 284  HOH HOH A . 
W 4 HOH 261 1061 64   HOH HOH A . 
W 4 HOH 262 1062 1000 HOH HOH A . 
W 4 HOH 263 1063 2087 HOH HOH A . 
W 4 HOH 264 1064 1182 HOH HOH A . 
W 4 HOH 265 1065 654  HOH HOH A . 
W 4 HOH 266 1066 103  HOH HOH A . 
W 4 HOH 267 1067 116  HOH HOH A . 
W 4 HOH 268 1068 1238 HOH HOH A . 
W 4 HOH 269 1069 913  HOH HOH A . 
W 4 HOH 270 1070 1047 HOH HOH A . 
W 4 HOH 271 1071 524  HOH HOH A . 
W 4 HOH 272 1072 1038 HOH HOH A . 
W 4 HOH 273 1073 1709 HOH HOH A . 
W 4 HOH 274 1074 1472 HOH HOH A . 
W 4 HOH 275 1075 130  HOH HOH A . 
W 4 HOH 276 1076 664  HOH HOH A . 
W 4 HOH 277 1077 644  HOH HOH A . 
W 4 HOH 278 1078 972  HOH HOH A . 
W 4 HOH 279 1079 342  HOH HOH A . 
W 4 HOH 280 1080 487  HOH HOH A . 
W 4 HOH 281 1081 1976 HOH HOH A . 
W 4 HOH 282 1082 896  HOH HOH A . 
W 4 HOH 283 1083 434  HOH HOH A . 
W 4 HOH 284 1084 2059 HOH HOH A . 
W 4 HOH 285 1085 209  HOH HOH A . 
W 4 HOH 286 1086 1057 HOH HOH A . 
W 4 HOH 287 1087 1645 HOH HOH A . 
W 4 HOH 288 1088 217  HOH HOH A . 
W 4 HOH 289 1089 1584 HOH HOH A . 
W 4 HOH 290 1090 1704 HOH HOH A . 
W 4 HOH 291 1091 131  HOH HOH A . 
W 4 HOH 292 1092 178  HOH HOH A . 
W 4 HOH 293 1093 1102 HOH HOH A . 
W 4 HOH 294 1094 215  HOH HOH A . 
W 4 HOH 295 1095 1196 HOH HOH A . 
W 4 HOH 296 1096 1311 HOH HOH A . 
W 4 HOH 297 1097 624  HOH HOH A . 
W 4 HOH 298 1098 1689 HOH HOH A . 
W 4 HOH 299 1099 331  HOH HOH A . 
W 4 HOH 300 1100 1465 HOH HOH A . 
W 4 HOH 301 1101 1663 HOH HOH A . 
W 4 HOH 302 1102 412  HOH HOH A . 
W 4 HOH 303 1103 1079 HOH HOH A . 
W 4 HOH 304 1104 1457 HOH HOH A . 
W 4 HOH 305 1105 919  HOH HOH A . 
W 4 HOH 306 1106 1194 HOH HOH A . 
W 4 HOH 307 1107 1367 HOH HOH A . 
W 4 HOH 308 1108 801  HOH HOH A . 
W 4 HOH 309 1109 1716 HOH HOH A . 
W 4 HOH 310 1110 464  HOH HOH A . 
W 4 HOH 311 1111 1233 HOH HOH A . 
W 4 HOH 312 1112 1446 HOH HOH A . 
W 4 HOH 313 1113 686  HOH HOH A . 
W 4 HOH 314 1114 1686 HOH HOH A . 
W 4 HOH 315 1115 486  HOH HOH A . 
W 4 HOH 316 1116 1962 HOH HOH A . 
W 4 HOH 317 1117 357  HOH HOH A . 
W 4 HOH 318 1118 348  HOH HOH A . 
W 4 HOH 319 1119 1454 HOH HOH A . 
W 4 HOH 320 1120 837  HOH HOH A . 
W 4 HOH 321 1121 1664 HOH HOH A . 
W 4 HOH 322 1122 1489 HOH HOH A . 
W 4 HOH 323 1123 1264 HOH HOH A . 
W 4 HOH 324 1124 1210 HOH HOH A . 
W 4 HOH 325 1125 2062 HOH HOH A . 
W 4 HOH 326 1126 107  HOH HOH A . 
W 4 HOH 327 1127 1192 HOH HOH A . 
W 4 HOH 328 1128 1728 HOH HOH A . 
W 4 HOH 329 1129 312  HOH HOH A . 
W 4 HOH 330 1130 1983 HOH HOH A . 
W 4 HOH 331 1131 1397 HOH HOH A . 
W 4 HOH 332 1132 764  HOH HOH A . 
W 4 HOH 333 1133 673  HOH HOH A . 
W 4 HOH 334 1134 165  HOH HOH A . 
W 4 HOH 335 1135 861  HOH HOH A . 
W 4 HOH 336 1136 294  HOH HOH A . 
W 4 HOH 337 1137 1697 HOH HOH A . 
W 4 HOH 338 1138 1265 HOH HOH A . 
W 4 HOH 339 1139 1191 HOH HOH A . 
W 4 HOH 340 1140 361  HOH HOH A . 
W 4 HOH 341 1141 2079 HOH HOH A . 
W 4 HOH 342 1142 1338 HOH HOH A . 
W 4 HOH 343 1143 1039 HOH HOH A . 
W 4 HOH 344 1144 1097 HOH HOH A . 
W 4 HOH 345 1145 67   HOH HOH A . 
W 4 HOH 346 1146 1015 HOH HOH A . 
W 4 HOH 347 1147 515  HOH HOH A . 
W 4 HOH 348 1148 863  HOH HOH A . 
W 4 HOH 349 1149 1110 HOH HOH A . 
W 4 HOH 350 1150 307  HOH HOH A . 
W 4 HOH 351 1151 583  HOH HOH A . 
W 4 HOH 352 1152 678  HOH HOH A . 
W 4 HOH 353 1153 1600 HOH HOH A . 
W 4 HOH 354 1154 697  HOH HOH A . 
W 4 HOH 355 1155 1219 HOH HOH A . 
W 4 HOH 356 1156 708  HOH HOH A . 
W 4 HOH 357 1157 1436 HOH HOH A . 
W 4 HOH 358 1158 1960 HOH HOH A . 
W 4 HOH 359 1159 1133 HOH HOH A . 
W 4 HOH 360 1160 1478 HOH HOH A . 
W 4 HOH 361 1161 379  HOH HOH A . 
W 4 HOH 362 1162 535  HOH HOH A . 
W 4 HOH 363 1163 1712 HOH HOH A . 
W 4 HOH 364 1164 1189 HOH HOH A . 
W 4 HOH 365 1165 1675 HOH HOH A . 
W 4 HOH 366 1166 328  HOH HOH A . 
W 4 HOH 367 1167 1471 HOH HOH A . 
W 4 HOH 368 1168 1718 HOH HOH A . 
W 4 HOH 369 1169 2063 HOH HOH A . 
W 4 HOH 370 1170 1296 HOH HOH A . 
W 4 HOH 371 1171 1698 HOH HOH A . 
W 4 HOH 372 1172 1497 HOH HOH A . 
W 4 HOH 373 1173 1966 HOH HOH A . 
W 4 HOH 374 1174 1725 HOH HOH A . 
W 4 HOH 375 1175 569  HOH HOH A . 
W 4 HOH 376 1176 1672 HOH HOH A . 
W 4 HOH 377 1177 1713 HOH HOH A . 
W 4 HOH 378 1178 695  HOH HOH A . 
W 4 HOH 379 1179 1037 HOH HOH A . 
W 4 HOH 380 1180 1407 HOH HOH A . 
W 4 HOH 381 1181 1010 HOH HOH A . 
W 4 HOH 382 1182 576  HOH HOH A . 
W 4 HOH 383 1183 1242 HOH HOH A . 
W 4 HOH 384 1184 776  HOH HOH A . 
W 4 HOH 385 1185 1717 HOH HOH A . 
W 4 HOH 386 1186 1168 HOH HOH A . 
W 4 HOH 387 1187 887  HOH HOH A . 
W 4 HOH 388 1188 1971 HOH HOH A . 
W 4 HOH 389 1189 1932 HOH HOH A . 
W 4 HOH 390 1190 1241 HOH HOH A . 
W 4 HOH 391 1191 681  HOH HOH A . 
W 4 HOH 392 1192 1677 HOH HOH A . 
W 4 HOH 393 1193 382  HOH HOH A . 
W 4 HOH 394 1194 1065 HOH HOH A . 
W 4 HOH 395 1195 2129 HOH HOH A . 
W 4 HOH 396 1196 939  HOH HOH A . 
W 4 HOH 397 1197 1185 HOH HOH A . 
W 4 HOH 398 1198 787  HOH HOH A . 
W 4 HOH 399 1199 1653 HOH HOH A . 
W 4 HOH 400 1200 1669 HOH HOH A . 
W 4 HOH 401 1201 1934 HOH HOH A . 
W 4 HOH 402 1202 1140 HOH HOH A . 
W 4 HOH 403 1203 1469 HOH HOH A . 
W 4 HOH 404 1204 1701 HOH HOH A . 
W 4 HOH 405 1205 1673 HOH HOH A . 
W 4 HOH 406 1206 1657 HOH HOH A . 
W 4 HOH 407 1207 1726 HOH HOH A . 
W 4 HOH 408 1208 1149 HOH HOH A . 
W 4 HOH 409 1209 1696 HOH HOH A . 
W 4 HOH 410 1210 2083 HOH HOH A . 
W 4 HOH 411 1211 1416 HOH HOH A . 
W 4 HOH 412 1212 47   HOH HOH A . 
W 4 HOH 413 1213 1177 HOH HOH A . 
W 4 HOH 414 1214 869  HOH HOH A . 
W 4 HOH 415 1215 892  HOH HOH A . 
W 4 HOH 416 1216 1668 HOH HOH A . 
W 4 HOH 417 1217 1647 HOH HOH A . 
W 4 HOH 418 1218 1424 HOH HOH A . 
W 4 HOH 419 1219 1130 HOH HOH A . 
W 4 HOH 420 1220 2124 HOH HOH A . 
W 4 HOH 421 1221 2058 HOH HOH A . 
W 4 HOH 422 1222 1479 HOH HOH A . 
W 4 HOH 423 1223 1157 HOH HOH A . 
W 4 HOH 424 1224 1733 HOH HOH A . 
W 4 HOH 425 1225 181  HOH HOH A . 
W 4 HOH 426 1226 1078 HOH HOH A . 
W 4 HOH 427 1227 1249 HOH HOH A . 
W 4 HOH 428 1228 1933 HOH HOH A . 
W 4 HOH 429 1229 1269 HOH HOH A . 
W 4 HOH 430 1230 1977 HOH HOH A . 
W 4 HOH 431 1231 1727 HOH HOH A . 
W 4 HOH 432 1232 1595 HOH HOH A . 
W 4 HOH 433 1233 1730 HOH HOH A . 
W 4 HOH 434 1234 1321 HOH HOH A . 
W 4 HOH 435 1235 634  HOH HOH A . 
W 4 HOH 436 1236 785  HOH HOH A . 
W 4 HOH 437 1237 1947 HOH HOH A . 
W 4 HOH 438 1238 931  HOH HOH A . 
W 4 HOH 439 1239 1968 HOH HOH A . 
W 4 HOH 440 1240 399  HOH HOH A . 
W 4 HOH 441 1241 1967 HOH HOH A . 
W 4 HOH 442 1242 660  HOH HOH A . 
W 4 HOH 443 1243 1676 HOH HOH A . 
W 4 HOH 444 1244 1274 HOH HOH A . 
W 4 HOH 445 1245 1700 HOH HOH A . 
W 4 HOH 446 1246 1280 HOH HOH A . 
W 4 HOH 447 1247 1032 HOH HOH A . 
W 4 HOH 448 1248 1462 HOH HOH A . 
W 4 HOH 449 1249 1594 HOH HOH A . 
W 4 HOH 450 1250 1662 HOH HOH A . 
W 4 HOH 451 1251 1369 HOH HOH A . 
W 4 HOH 452 1252 1464 HOH HOH A . 
W 4 HOH 453 1253 662  HOH HOH A . 
W 4 HOH 454 1254 2066 HOH HOH A . 
W 4 HOH 455 1255 623  HOH HOH A . 
W 4 HOH 456 1256 2065 HOH HOH A . 
W 4 HOH 457 1257 1680 HOH HOH A . 
W 4 HOH 458 1258 1693 HOH HOH A . 
W 4 HOH 459 1259 1393 HOH HOH A . 
W 4 HOH 460 1260 1073 HOH HOH A . 
W 4 HOH 461 1261 677  HOH HOH A . 
W 4 HOH 462 1262 1333 HOH HOH A . 
W 4 HOH 463 1263 1502 HOH HOH A . 
W 4 HOH 464 1264 1969 HOH HOH A . 
W 4 HOH 465 1265 2130 HOH HOH A . 
W 4 HOH 466 1266 1315 HOH HOH A . 
W 4 HOH 467 1267 1711 HOH HOH A . 
W 4 HOH 468 1268 2128 HOH HOH A . 
W 4 HOH 469 1269 246  HOH HOH A . 
W 4 HOH 470 1270 1514 HOH HOH A . 
W 4 HOH 471 1271 1965 HOH HOH A . 
W 4 HOH 472 1272 1145 HOH HOH A . 
W 4 HOH 473 1273 1453 HOH HOH A . 
W 4 HOH 474 1274 1720 HOH HOH A . 
W 4 HOH 475 1275 1553 HOH HOH A . 
W 4 HOH 476 1276 1401 HOH HOH A . 
W 4 HOH 477 1277 1008 HOH HOH A . 
W 4 HOH 478 1278 1972 HOH HOH A . 
W 4 HOH 479 1279 1618 HOH HOH A . 
W 4 HOH 480 1280 2084 HOH HOH A . 
W 4 HOH 481 1281 1961 HOH HOH A . 
W 4 HOH 482 1282 770  HOH HOH A . 
W 4 HOH 483 1283 1975 HOH HOH A . 
W 4 HOH 484 1284 838  HOH HOH A . 
W 4 HOH 485 1285 868  HOH HOH A . 
W 4 HOH 486 1286 1354 HOH HOH A . 
W 4 HOH 487 1287 2125 HOH HOH A . 
W 4 HOH 488 1288 1721 HOH HOH A . 
W 4 HOH 489 1289 2057 HOH HOH A . 
W 4 HOH 490 1290 1699 HOH HOH A . 
W 4 HOH 491 1291 1979 HOH HOH A . 
W 4 HOH 492 1292 1312 HOH HOH A . 
X 4 HOH 1   801  1944 HOH HOH B . 
X 4 HOH 2   802  1438 HOH HOH B . 
X 4 HOH 3   803  1787 HOH HOH B . 
X 4 HOH 4   804  722  HOH HOH B . 
X 4 HOH 5   805  1993 HOH HOH B . 
X 4 HOH 6   806  1095 HOH HOH B . 
X 4 HOH 7   807  1007 HOH HOH B . 
X 4 HOH 8   808  1226 HOH HOH B . 
X 4 HOH 9   809  1121 HOH HOH B . 
X 4 HOH 10  810  995  HOH HOH B . 
X 4 HOH 11  811  385  HOH HOH B . 
X 4 HOH 12  812  1364 HOH HOH B . 
X 4 HOH 13  813  898  HOH HOH B . 
X 4 HOH 14  814  758  HOH HOH B . 
X 4 HOH 15  815  482  HOH HOH B . 
X 4 HOH 16  816  2077 HOH HOH B . 
X 4 HOH 17  817  968  HOH HOH B . 
X 4 HOH 18  818  1564 HOH HOH B . 
X 4 HOH 19  819  1559 HOH HOH B . 
X 4 HOH 20  820  935  HOH HOH B . 
X 4 HOH 21  821  619  HOH HOH B . 
X 4 HOH 22  822  1455 HOH HOH B . 
X 4 HOH 23  823  1599 HOH HOH B . 
X 4 HOH 24  824  998  HOH HOH B . 
X 4 HOH 25  825  452  HOH HOH B . 
X 4 HOH 26  826  901  HOH HOH B . 
X 4 HOH 27  827  1161 HOH HOH B . 
X 4 HOH 28  828  762  HOH HOH B . 
X 4 HOH 29  829  1936 HOH HOH B . 
X 4 HOH 30  830  612  HOH HOH B . 
X 4 HOH 31  831  1518 HOH HOH B . 
X 4 HOH 32  832  477  HOH HOH B . 
X 4 HOH 33  833  926  HOH HOH B . 
X 4 HOH 34  834  1997 HOH HOH B . 
X 4 HOH 35  835  754  HOH HOH B . 
X 4 HOH 36  836  381  HOH HOH B . 
X 4 HOH 37  837  1127 HOH HOH B . 
X 4 HOH 38  838  29   HOH HOH B . 
X 4 HOH 39  839  687  HOH HOH B . 
X 4 HOH 40  840  2088 HOH HOH B . 
X 4 HOH 41  841  586  HOH HOH B . 
X 4 HOH 42  842  2004 HOH HOH B . 
X 4 HOH 43  843  1070 HOH HOH B . 
X 4 HOH 44  844  1235 HOH HOH B . 
X 4 HOH 45  845  1752 HOH HOH B . 
X 4 HOH 46  846  1996 HOH HOH B . 
X 4 HOH 47  847  1780 HOH HOH B . 
X 4 HOH 48  848  1361 HOH HOH B . 
X 4 HOH 49  849  917  HOH HOH B . 
X 4 HOH 50  850  1427 HOH HOH B . 
X 4 HOH 51  851  283  HOH HOH B . 
X 4 HOH 52  852  111  HOH HOH B . 
X 4 HOH 53  853  473  HOH HOH B . 
X 4 HOH 54  854  551  HOH HOH B . 
X 4 HOH 55  855  602  HOH HOH B . 
X 4 HOH 56  856  1377 HOH HOH B . 
X 4 HOH 57  857  514  HOH HOH B . 
X 4 HOH 58  858  2073 HOH HOH B . 
X 4 HOH 59  859  661  HOH HOH B . 
X 4 HOH 60  860  2091 HOH HOH B . 
X 4 HOH 61  861  796  HOH HOH B . 
X 4 HOH 62  862  1641 HOH HOH B . 
X 4 HOH 63  863  894  HOH HOH B . 
X 4 HOH 64  864  1777 HOH HOH B . 
X 4 HOH 65  865  5    HOH HOH B . 
X 4 HOH 66  866  990  HOH HOH B . 
X 4 HOH 67  867  836  HOH HOH B . 
X 4 HOH 68  868  1128 HOH HOH B . 
X 4 HOH 69  869  609  HOH HOH B . 
X 4 HOH 70  870  86   HOH HOH B . 
X 4 HOH 71  871  1743 HOH HOH B . 
X 4 HOH 72  872  1802 HOH HOH B . 
X 4 HOH 73  873  275  HOH HOH B . 
X 4 HOH 74  874  2086 HOH HOH B . 
X 4 HOH 75  875  538  HOH HOH B . 
X 4 HOH 76  876  699  HOH HOH B . 
X 4 HOH 77  877  2102 HOH HOH B . 
X 4 HOH 78  878  520  HOH HOH B . 
X 4 HOH 79  879  333  HOH HOH B . 
X 4 HOH 80  880  1792 HOH HOH B . 
X 4 HOH 81  881  2002 HOH HOH B . 
X 4 HOH 82  882  961  HOH HOH B . 
X 4 HOH 83  883  814  HOH HOH B . 
X 4 HOH 84  884  992  HOH HOH B . 
X 4 HOH 85  885  299  HOH HOH B . 
X 4 HOH 86  886  2101 HOH HOH B . 
X 4 HOH 87  887  448  HOH HOH B . 
X 4 HOH 88  888  1807 HOH HOH B . 
X 4 HOH 89  889  1795 HOH HOH B . 
X 4 HOH 90  890  1782 HOH HOH B . 
X 4 HOH 91  891  419  HOH HOH B . 
X 4 HOH 92  892  853  HOH HOH B . 
X 4 HOH 93  893  1751 HOH HOH B . 
X 4 HOH 94  894  851  HOH HOH B . 
X 4 HOH 95  895  281  HOH HOH B . 
X 4 HOH 96  896  330  HOH HOH B . 
X 4 HOH 97  897  167  HOH HOH B . 
X 4 HOH 98  898  50   HOH HOH B . 
X 4 HOH 99  899  274  HOH HOH B . 
X 4 HOH 100 900  575  HOH HOH B . 
X 4 HOH 101 901  345  HOH HOH B . 
X 4 HOH 102 902  418  HOH HOH B . 
X 4 HOH 103 903  197  HOH HOH B . 
X 4 HOH 104 904  1395 HOH HOH B . 
X 4 HOH 105 905  182  HOH HOH B . 
X 4 HOH 106 906  1155 HOH HOH B . 
X 4 HOH 107 907  83   HOH HOH B . 
X 4 HOH 108 908  292  HOH HOH B . 
X 4 HOH 109 909  13   HOH HOH B . 
X 4 HOH 110 910  497  HOH HOH B . 
X 4 HOH 111 911  822  HOH HOH B . 
X 4 HOH 112 912  797  HOH HOH B . 
X 4 HOH 113 913  689  HOH HOH B . 
X 4 HOH 114 914  93   HOH HOH B . 
X 4 HOH 115 915  1744 HOH HOH B . 
X 4 HOH 116 916  68   HOH HOH B . 
X 4 HOH 117 917  483  HOH HOH B . 
X 4 HOH 118 918  1055 HOH HOH B . 
X 4 HOH 119 919  2094 HOH HOH B . 
X 4 HOH 120 920  696  HOH HOH B . 
X 4 HOH 121 921  480  HOH HOH B . 
X 4 HOH 122 922  755  HOH HOH B . 
X 4 HOH 123 923  857  HOH HOH B . 
X 4 HOH 124 924  1417 HOH HOH B . 
X 4 HOH 125 925  1111 HOH HOH B . 
X 4 HOH 126 926  1535 HOH HOH B . 
X 4 HOH 127 927  179  HOH HOH B . 
X 4 HOH 128 928  1418 HOH HOH B . 
X 4 HOH 129 929  642  HOH HOH B . 
X 4 HOH 130 930  559  HOH HOH B . 
X 4 HOH 131 931  1760 HOH HOH B . 
X 4 HOH 132 932  214  HOH HOH B . 
X 4 HOH 133 933  376  HOH HOH B . 
X 4 HOH 134 934  772  HOH HOH B . 
X 4 HOH 135 935  1282 HOH HOH B . 
X 4 HOH 136 936  74   HOH HOH B . 
X 4 HOH 137 937  256  HOH HOH B . 
X 4 HOH 138 938  149  HOH HOH B . 
X 4 HOH 139 939  1750 HOH HOH B . 
X 4 HOH 140 940  933  HOH HOH B . 
X 4 HOH 141 941  180  HOH HOH B . 
X 4 HOH 142 942  1173 HOH HOH B . 
X 4 HOH 143 943  239  HOH HOH B . 
X 4 HOH 144 944  652  HOH HOH B . 
X 4 HOH 145 945  1937 HOH HOH B . 
X 4 HOH 146 946  100  HOH HOH B . 
X 4 HOH 147 947  122  HOH HOH B . 
X 4 HOH 148 948  1054 HOH HOH B . 
X 4 HOH 149 949  288  HOH HOH B . 
X 4 HOH 150 950  1135 HOH HOH B . 
X 4 HOH 151 951  702  HOH HOH B . 
X 4 HOH 152 952  2071 HOH HOH B . 
X 4 HOH 153 953  1538 HOH HOH B . 
X 4 HOH 154 954  324  HOH HOH B . 
X 4 HOH 155 955  808  HOH HOH B . 
X 4 HOH 156 956  1085 HOH HOH B . 
X 4 HOH 157 957  1284 HOH HOH B . 
X 4 HOH 158 958  1117 HOH HOH B . 
X 4 HOH 159 959  245  HOH HOH B . 
X 4 HOH 160 960  1013 HOH HOH B . 
X 4 HOH 161 961  1437 HOH HOH B . 
X 4 HOH 162 962  1345 HOH HOH B . 
X 4 HOH 163 963  291  HOH HOH B . 
X 4 HOH 164 964  537  HOH HOH B . 
X 4 HOH 165 965  492  HOH HOH B . 
X 4 HOH 166 966  593  HOH HOH B . 
X 4 HOH 167 967  88   HOH HOH B . 
X 4 HOH 168 968  243  HOH HOH B . 
X 4 HOH 169 969  318  HOH HOH B . 
X 4 HOH 170 970  80   HOH HOH B . 
X 4 HOH 171 971  1759 HOH HOH B . 
X 4 HOH 172 972  468  HOH HOH B . 
X 4 HOH 173 973  173  HOH HOH B . 
X 4 HOH 174 974  78   HOH HOH B . 
X 4 HOH 175 975  120  HOH HOH B . 
X 4 HOH 176 976  1651 HOH HOH B . 
X 4 HOH 177 977  1018 HOH HOH B . 
X 4 HOH 178 978  69   HOH HOH B . 
X 4 HOH 179 979  710  HOH HOH B . 
X 4 HOH 180 980  947  HOH HOH B . 
X 4 HOH 181 981  944  HOH HOH B . 
X 4 HOH 182 982  798  HOH HOH B . 
X 4 HOH 183 983  1945 HOH HOH B . 
X 4 HOH 184 984  267  HOH HOH B . 
X 4 HOH 185 985  1193 HOH HOH B . 
X 4 HOH 186 986  1092 HOH HOH B . 
X 4 HOH 187 987  1707 HOH HOH B . 
X 4 HOH 188 988  1215 HOH HOH B . 
X 4 HOH 189 989  1074 HOH HOH B . 
X 4 HOH 190 990  728  HOH HOH B . 
X 4 HOH 191 991  91   HOH HOH B . 
X 4 HOH 192 992  57   HOH HOH B . 
X 4 HOH 193 993  1756 HOH HOH B . 
X 4 HOH 194 994  119  HOH HOH B . 
X 4 HOH 195 995  1500 HOH HOH B . 
X 4 HOH 196 996  400  HOH HOH B . 
X 4 HOH 197 997  653  HOH HOH B . 
X 4 HOH 198 998  121  HOH HOH B . 
X 4 HOH 199 999  807  HOH HOH B . 
X 4 HOH 200 1000 1176 HOH HOH B . 
X 4 HOH 201 1001 62   HOH HOH B . 
X 4 HOH 202 1002 572  HOH HOH B . 
X 4 HOH 203 1003 71   HOH HOH B . 
X 4 HOH 204 1004 1319 HOH HOH B . 
X 4 HOH 205 1005 415  HOH HOH B . 
X 4 HOH 206 1006 936  HOH HOH B . 
X 4 HOH 207 1007 1763 HOH HOH B . 
X 4 HOH 208 1008 1106 HOH HOH B . 
X 4 HOH 209 1009 967  HOH HOH B . 
X 4 HOH 210 1010 19   HOH HOH B . 
X 4 HOH 211 1011 58   HOH HOH B . 
X 4 HOH 212 1012 1510 HOH HOH B . 
X 4 HOH 213 1013 166  HOH HOH B . 
X 4 HOH 214 1014 1788 HOH HOH B . 
X 4 HOH 215 1015 656  HOH HOH B . 
X 4 HOH 216 1016 1271 HOH HOH B . 
X 4 HOH 217 1017 621  HOH HOH B . 
X 4 HOH 218 1018 502  HOH HOH B . 
X 4 HOH 219 1019 1313 HOH HOH B . 
X 4 HOH 220 1020 534  HOH HOH B . 
X 4 HOH 221 1021 317  HOH HOH B . 
X 4 HOH 222 1022 1685 HOH HOH B . 
X 4 HOH 223 1023 38   HOH HOH B . 
X 4 HOH 224 1024 146  HOH HOH B . 
X 4 HOH 225 1025 1    HOH HOH B . 
X 4 HOH 226 1026 59   HOH HOH B . 
X 4 HOH 227 1027 136  HOH HOH B . 
X 4 HOH 228 1028 211  HOH HOH B . 
X 4 HOH 229 1029 280  HOH HOH B . 
X 4 HOH 230 1030 1705 HOH HOH B . 
X 4 HOH 231 1031 571  HOH HOH B . 
X 4 HOH 232 1032 874  HOH HOH B . 
X 4 HOH 233 1033 716  HOH HOH B . 
X 4 HOH 234 1034 1413 HOH HOH B . 
X 4 HOH 235 1035 1774 HOH HOH B . 
X 4 HOH 236 1036 1402 HOH HOH B . 
X 4 HOH 237 1037 65   HOH HOH B . 
X 4 HOH 238 1038 1783 HOH HOH B . 
X 4 HOH 239 1039 542  HOH HOH B . 
X 4 HOH 240 1040 49   HOH HOH B . 
X 4 HOH 241 1041 2001 HOH HOH B . 
X 4 HOH 242 1042 96   HOH HOH B . 
X 4 HOH 243 1043 7    HOH HOH B . 
X 4 HOH 244 1044 1090 HOH HOH B . 
X 4 HOH 245 1045 1542 HOH HOH B . 
X 4 HOH 246 1046 334  HOH HOH B . 
X 4 HOH 247 1047 87   HOH HOH B . 
X 4 HOH 248 1048 1745 HOH HOH B . 
X 4 HOH 249 1049 951  HOH HOH B . 
X 4 HOH 250 1050 387  HOH HOH B . 
X 4 HOH 251 1051 355  HOH HOH B . 
X 4 HOH 252 1052 42   HOH HOH B . 
X 4 HOH 253 1053 311  HOH HOH B . 
X 4 HOH 254 1054 1742 HOH HOH B . 
X 4 HOH 255 1055 2090 HOH HOH B . 
X 4 HOH 256 1056 1326 HOH HOH B . 
X 4 HOH 257 1057 189  HOH HOH B . 
X 4 HOH 258 1058 986  HOH HOH B . 
X 4 HOH 259 1059 1801 HOH HOH B . 
X 4 HOH 260 1060 1516 HOH HOH B . 
X 4 HOH 261 1061 1772 HOH HOH B . 
X 4 HOH 262 1062 1371 HOH HOH B . 
X 4 HOH 263 1063 1093 HOH HOH B . 
X 4 HOH 264 1064 44   HOH HOH B . 
X 4 HOH 265 1065 1512 HOH HOH B . 
X 4 HOH 266 1066 743  HOH HOH B . 
X 4 HOH 267 1067 1765 HOH HOH B . 
X 4 HOH 268 1068 1791 HOH HOH B . 
X 4 HOH 269 1069 1557 HOH HOH B . 
X 4 HOH 270 1070 985  HOH HOH B . 
X 4 HOH 271 1071 1048 HOH HOH B . 
X 4 HOH 272 1072 1081 HOH HOH B . 
X 4 HOH 273 1073 335  HOH HOH B . 
X 4 HOH 274 1074 301  HOH HOH B . 
X 4 HOH 275 1075 72   HOH HOH B . 
X 4 HOH 276 1076 1598 HOH HOH B . 
X 4 HOH 277 1077 127  HOH HOH B . 
X 4 HOH 278 1078 1299 HOH HOH B . 
X 4 HOH 279 1079 1153 HOH HOH B . 
X 4 HOH 280 1080 41   HOH HOH B . 
X 4 HOH 281 1081 1749 HOH HOH B . 
X 4 HOH 282 1082 1294 HOH HOH B . 
X 4 HOH 283 1083 172  HOH HOH B . 
X 4 HOH 284 1084 1771 HOH HOH B . 
X 4 HOH 285 1085 123  HOH HOH B . 
X 4 HOH 286 1086 988  HOH HOH B . 
X 4 HOH 287 1087 39   HOH HOH B . 
X 4 HOH 288 1088 1589 HOH HOH B . 
X 4 HOH 289 1089 611  HOH HOH B . 
X 4 HOH 290 1090 55   HOH HOH B . 
X 4 HOH 291 1091 109  HOH HOH B . 
X 4 HOH 292 1092 253  HOH HOH B . 
X 4 HOH 293 1093 250  HOH HOH B . 
X 4 HOH 294 1094 1989 HOH HOH B . 
X 4 HOH 295 1095 457  HOH HOH B . 
X 4 HOH 296 1096 729  HOH HOH B . 
X 4 HOH 297 1097 278  HOH HOH B . 
X 4 HOH 298 1098 1105 HOH HOH B . 
X 4 HOH 299 1099 40   HOH HOH B . 
X 4 HOH 300 1100 904  HOH HOH B . 
X 4 HOH 301 1101 683  HOH HOH B . 
X 4 HOH 302 1102 2126 HOH HOH B . 
X 4 HOH 303 1103 156  HOH HOH B . 
X 4 HOH 304 1104 1577 HOH HOH B . 
X 4 HOH 305 1105 1388 HOH HOH B . 
X 4 HOH 306 1106 2096 HOH HOH B . 
X 4 HOH 307 1107 351  HOH HOH B . 
X 4 HOH 308 1108 2003 HOH HOH B . 
X 4 HOH 309 1109 199  HOH HOH B . 
X 4 HOH 310 1110 1748 HOH HOH B . 
X 4 HOH 311 1111 327  HOH HOH B . 
X 4 HOH 312 1112 960  HOH HOH B . 
X 4 HOH 313 1113 777  HOH HOH B . 
X 4 HOH 314 1114 140  HOH HOH B . 
X 4 HOH 315 1115 1137 HOH HOH B . 
X 4 HOH 316 1116 565  HOH HOH B . 
X 4 HOH 317 1117 859  HOH HOH B . 
X 4 HOH 318 1118 1029 HOH HOH B . 
X 4 HOH 319 1119 1519 HOH HOH B . 
X 4 HOH 320 1120 51   HOH HOH B . 
X 4 HOH 321 1121 1650 HOH HOH B . 
X 4 HOH 322 1122 218  HOH HOH B . 
X 4 HOH 323 1123 860  HOH HOH B . 
X 4 HOH 324 1124 1329 HOH HOH B . 
X 4 HOH 325 1125 1784 HOH HOH B . 
X 4 HOH 326 1126 2074 HOH HOH B . 
X 4 HOH 327 1127 589  HOH HOH B . 
X 4 HOH 328 1128 161  HOH HOH B . 
X 4 HOH 329 1129 549  HOH HOH B . 
X 4 HOH 330 1130 1554 HOH HOH B . 
X 4 HOH 331 1131 531  HOH HOH B . 
X 4 HOH 332 1132 1365 HOH HOH B . 
X 4 HOH 333 1133 1107 HOH HOH B . 
X 4 HOH 334 1134 1476 HOH HOH B . 
X 4 HOH 335 1135 1275 HOH HOH B . 
X 4 HOH 336 1136 1061 HOH HOH B . 
X 4 HOH 337 1137 1779 HOH HOH B . 
X 4 HOH 338 1138 1687 HOH HOH B . 
X 4 HOH 339 1139 1796 HOH HOH B . 
X 4 HOH 340 1140 81   HOH HOH B . 
X 4 HOH 341 1141 978  HOH HOH B . 
X 4 HOH 342 1142 203  HOH HOH B . 
X 4 HOH 343 1143 378  HOH HOH B . 
X 4 HOH 344 1144 372  HOH HOH B . 
X 4 HOH 345 1145 943  HOH HOH B . 
X 4 HOH 346 1146 1289 HOH HOH B . 
X 4 HOH 347 1147 193  HOH HOH B . 
X 4 HOH 348 1148 1318 HOH HOH B . 
X 4 HOH 349 1149 1156 HOH HOH B . 
X 4 HOH 350 1150 543  HOH HOH B . 
X 4 HOH 351 1151 303  HOH HOH B . 
X 4 HOH 352 1152 741  HOH HOH B . 
X 4 HOH 353 1153 1803 HOH HOH B . 
X 4 HOH 354 1154 558  HOH HOH B . 
X 4 HOH 355 1155 341  HOH HOH B . 
X 4 HOH 356 1156 1769 HOH HOH B . 
X 4 HOH 357 1157 108  HOH HOH B . 
X 4 HOH 358 1158 839  HOH HOH B . 
X 4 HOH 359 1159 433  HOH HOH B . 
X 4 HOH 360 1160 313  HOH HOH B . 
X 4 HOH 361 1161 1287 HOH HOH B . 
X 4 HOH 362 1162 279  HOH HOH B . 
X 4 HOH 363 1163 343  HOH HOH B . 
X 4 HOH 364 1164 95   HOH HOH B . 
X 4 HOH 365 1165 1562 HOH HOH B . 
X 4 HOH 366 1166 1963 HOH HOH B . 
X 4 HOH 367 1167 455  HOH HOH B . 
X 4 HOH 368 1168 615  HOH HOH B . 
X 4 HOH 369 1169 1991 HOH HOH B . 
X 4 HOH 370 1170 579  HOH HOH B . 
X 4 HOH 371 1171 2099 HOH HOH B . 
X 4 HOH 372 1172 902  HOH HOH B . 
X 4 HOH 373 1173 1448 HOH HOH B . 
X 4 HOH 374 1174 1794 HOH HOH B . 
X 4 HOH 375 1175 1410 HOH HOH B . 
X 4 HOH 376 1176 1638 HOH HOH B . 
X 4 HOH 377 1177 584  HOH HOH B . 
X 4 HOH 378 1178 539  HOH HOH B . 
X 4 HOH 379 1179 407  HOH HOH B . 
X 4 HOH 380 1180 354  HOH HOH B . 
X 4 HOH 381 1181 509  HOH HOH B . 
X 4 HOH 382 1182 1399 HOH HOH B . 
X 4 HOH 383 1183 1640 HOH HOH B . 
X 4 HOH 384 1184 2098 HOH HOH B . 
X 4 HOH 385 1185 461  HOH HOH B . 
X 4 HOH 386 1186 945  HOH HOH B . 
X 4 HOH 387 1187 2093 HOH HOH B . 
X 4 HOH 388 1188 920  HOH HOH B . 
X 4 HOH 389 1189 631  HOH HOH B . 
X 4 HOH 390 1190 1314 HOH HOH B . 
X 4 HOH 391 1191 658  HOH HOH B . 
X 4 HOH 392 1192 715  HOH HOH B . 
X 4 HOH 393 1193 942  HOH HOH B . 
X 4 HOH 394 1194 495  HOH HOH B . 
X 4 HOH 395 1195 377  HOH HOH B . 
X 4 HOH 396 1196 79   HOH HOH B . 
X 4 HOH 397 1197 1985 HOH HOH B . 
X 4 HOH 398 1198 1362 HOH HOH B . 
X 4 HOH 399 1199 1797 HOH HOH B . 
X 4 HOH 400 1200 207  HOH HOH B . 
X 4 HOH 401 1201 590  HOH HOH B . 
X 4 HOH 402 1202 157  HOH HOH B . 
X 4 HOH 403 1203 153  HOH HOH B . 
X 4 HOH 404 1204 2100 HOH HOH B . 
X 4 HOH 405 1205 1786 HOH HOH B . 
X 4 HOH 406 1206 449  HOH HOH B . 
X 4 HOH 407 1207 1806 HOH HOH B . 
X 4 HOH 408 1208 924  HOH HOH B . 
X 4 HOH 409 1209 1415 HOH HOH B . 
X 4 HOH 410 1210 1374 HOH HOH B . 
X 4 HOH 411 1211 1136 HOH HOH B . 
X 4 HOH 412 1212 1770 HOH HOH B . 
X 4 HOH 413 1213 962  HOH HOH B . 
X 4 HOH 414 1214 1207 HOH HOH B . 
X 4 HOH 415 1215 272  HOH HOH B . 
X 4 HOH 416 1216 1528 HOH HOH B . 
X 4 HOH 417 1217 864  HOH HOH B . 
X 4 HOH 418 1218 1998 HOH HOH B . 
X 4 HOH 419 1219 1738 HOH HOH B . 
X 4 HOH 420 1220 1305 HOH HOH B . 
X 4 HOH 421 1221 1267 HOH HOH B . 
X 4 HOH 422 1222 1515 HOH HOH B . 
X 4 HOH 423 1223 2000 HOH HOH B . 
X 4 HOH 424 1224 953  HOH HOH B . 
X 4 HOH 425 1225 1747 HOH HOH B . 
X 4 HOH 426 1226 724  HOH HOH B . 
X 4 HOH 427 1227 735  HOH HOH B . 
X 4 HOH 428 1228 1163 HOH HOH B . 
X 4 HOH 429 1229 1255 HOH HOH B . 
X 4 HOH 430 1230 1317 HOH HOH B . 
X 4 HOH 431 1231 1800 HOH HOH B . 
X 4 HOH 432 1232 899  HOH HOH B . 
X 4 HOH 433 1233 220  HOH HOH B . 
X 4 HOH 434 1234 1222 HOH HOH B . 
X 4 HOH 435 1235 889  HOH HOH B . 
X 4 HOH 436 1236 1458 HOH HOH B . 
X 4 HOH 437 1237 1999 HOH HOH B . 
X 4 HOH 438 1238 463  HOH HOH B . 
X 4 HOH 439 1239 870  HOH HOH B . 
X 4 HOH 440 1240 388  HOH HOH B . 
X 4 HOH 441 1241 1342 HOH HOH B . 
X 4 HOH 442 1242 102  HOH HOH B . 
X 4 HOH 443 1243 1799 HOH HOH B . 
X 4 HOH 444 1244 241  HOH HOH B . 
X 4 HOH 445 1245 1820 HOH HOH B . 
X 4 HOH 446 1246 1642 HOH HOH B . 
X 4 HOH 447 1247 1573 HOH HOH B . 
X 4 HOH 448 1248 1790 HOH HOH B . 
X 4 HOH 449 1249 1781 HOH HOH B . 
X 4 HOH 450 1250 1755 HOH HOH B . 
X 4 HOH 451 1251 684  HOH HOH B . 
X 4 HOH 452 1252 1789 HOH HOH B . 
X 4 HOH 453 1253 1277 HOH HOH B . 
X 4 HOH 454 1254 1736 HOH HOH B . 
X 4 HOH 455 1255 225  HOH HOH B . 
X 4 HOH 456 1256 737  HOH HOH B . 
X 4 HOH 457 1257 1120 HOH HOH B . 
X 4 HOH 458 1258 1223 HOH HOH B . 
X 4 HOH 459 1259 1652 HOH HOH B . 
X 4 HOH 460 1260 1071 HOH HOH B . 
X 4 HOH 461 1261 1648 HOH HOH B . 
X 4 HOH 462 1262 1355 HOH HOH B . 
X 4 HOH 463 1263 1943 HOH HOH B . 
X 4 HOH 464 1264 544  HOH HOH B . 
X 4 HOH 465 1265 2070 HOH HOH B . 
X 4 HOH 466 1266 1593 HOH HOH B . 
X 4 HOH 467 1267 1753 HOH HOH B . 
X 4 HOH 468 1268 1946 HOH HOH B . 
X 4 HOH 469 1269 1558 HOH HOH B . 
X 4 HOH 470 1270 66   HOH HOH B . 
X 4 HOH 471 1271 1649 HOH HOH B . 
X 4 HOH 472 1272 646  HOH HOH B . 
X 4 HOH 473 1273 1818 HOH HOH B . 
X 4 HOH 474 1274 1773 HOH HOH B . 
X 4 HOH 475 1275 821  HOH HOH B . 
X 4 HOH 476 1276 232  HOH HOH B . 
X 4 HOH 477 1277 782  HOH HOH B . 
X 4 HOH 478 1278 1383 HOH HOH B . 
X 4 HOH 479 1279 198  HOH HOH B . 
X 4 HOH 480 1280 2095 HOH HOH B . 
X 4 HOH 481 1281 532  HOH HOH B . 
X 4 HOH 482 1282 1409 HOH HOH B . 
X 4 HOH 483 1283 693  HOH HOH B . 
X 4 HOH 484 1284 1053 HOH HOH B . 
X 4 HOH 485 1285 765  HOH HOH B . 
X 4 HOH 486 1286 925  HOH HOH B . 
X 4 HOH 487 1287 2097 HOH HOH B . 
X 4 HOH 488 1288 1785 HOH HOH B . 
X 4 HOH 489 1289 1637 HOH HOH B . 
X 4 HOH 490 1290 1370 HOH HOH B . 
X 4 HOH 491 1291 370  HOH HOH B . 
X 4 HOH 492 1292 2092 HOH HOH B . 
X 4 HOH 493 1293 1201 HOH HOH B . 
X 4 HOH 494 1294 221  HOH HOH B . 
X 4 HOH 495 1295 1768 HOH HOH B . 
X 4 HOH 496 1296 846  HOH HOH B . 
X 4 HOH 497 1297 907  HOH HOH B . 
X 4 HOH 498 1298 1555 HOH HOH B . 
X 4 HOH 499 1299 1385 HOH HOH B . 
X 4 HOH 500 1300 1684 HOH HOH B . 
X 4 HOH 501 1301 1091 HOH HOH B . 
X 4 HOH 502 1302 603  HOH HOH B . 
X 4 HOH 503 1303 727  HOH HOH B . 
X 4 HOH 504 1304 1451 HOH HOH B . 
X 4 HOH 505 1305 1286 HOH HOH B . 
X 4 HOH 506 1306 973  HOH HOH B . 
X 4 HOH 507 1307 1754 HOH HOH B . 
X 4 HOH 508 1308 1986 HOH HOH B . 
X 4 HOH 509 1309 1990 HOH HOH B . 
X 4 HOH 510 1310 1643 HOH HOH B . 
X 4 HOH 511 1311 1987 HOH HOH B . 
X 4 HOH 512 1312 1045 HOH HOH B . 
X 4 HOH 513 1313 1798 HOH HOH B . 
X 4 HOH 514 1314 60   HOH HOH B . 
X 4 HOH 515 1315 1939 HOH HOH B . 
X 4 HOH 516 1316 1351 HOH HOH B . 
X 4 HOH 517 1317 1227 HOH HOH B . 
X 4 HOH 518 1318 1639 HOH HOH B . 
X 4 HOH 519 1319 1043 HOH HOH B . 
X 4 HOH 520 1320 2076 HOH HOH B . 
X 4 HOH 521 1321 1805 HOH HOH B . 
X 4 HOH 522 1322 1475 HOH HOH B . 
X 4 HOH 523 1323 1576 HOH HOH B . 
X 4 HOH 524 1324 1316 HOH HOH B . 
X 4 HOH 525 1325 2089 HOH HOH B . 
X 4 HOH 526 1326 1467 HOH HOH B . 
X 4 HOH 527 1327 1300 HOH HOH B . 
X 4 HOH 528 1328 784  HOH HOH B . 
X 4 HOH 529 1329 431  HOH HOH B . 
X 4 HOH 530 1330 1099 HOH HOH B . 
X 4 HOH 531 1331 1636 HOH HOH B . 
X 4 HOH 532 1332 2075 HOH HOH B . 
X 4 HOH 533 1333 1766 HOH HOH B . 
X 4 HOH 534 1334 1328 HOH HOH B . 
X 4 HOH 535 1335 1793 HOH HOH B . 
X 4 HOH 536 1336 1882 HOH HOH B . 
X 4 HOH 537 1337 1301 HOH HOH B . 
X 4 HOH 538 1338 1537 HOH HOH B . 
X 4 HOH 539 1339 637  HOH HOH B . 
X 4 HOH 540 1340 560  HOH HOH B . 
X 4 HOH 541 1341 287  HOH HOH B . 
X 4 HOH 542 1342 1942 HOH HOH B . 
X 4 HOH 543 1343 1776 HOH HOH B . 
X 4 HOH 544 1344 405  HOH HOH B . 
X 4 HOH 545 1345 1764 HOH HOH B . 
X 4 HOH 546 1346 780  HOH HOH B . 
X 4 HOH 547 1347 598  HOH HOH B . 
X 4 HOH 548 1348 1452 HOH HOH B . 
X 4 HOH 549 1349 1230 HOH HOH B . 
X 4 HOH 550 1350 668  HOH HOH B . 
X 4 HOH 551 1351 1404 HOH HOH B . 
X 4 HOH 552 1352 581  HOH HOH B . 
X 4 HOH 553 1353 1580 HOH HOH B . 
X 4 HOH 554 1354 975  HOH HOH B . 
X 4 HOH 555 1355 1336 HOH HOH B . 
X 4 HOH 556 1356 1940 HOH HOH B . 
X 4 HOH 557 1357 1938 HOH HOH B . 
X 4 HOH 558 1358 1183 HOH HOH B . 
X 4 HOH 559 1359 1344 HOH HOH B . 
X 4 HOH 560 1360 852  HOH HOH B . 
X 4 HOH 561 1361 562  HOH HOH B . 
X 4 HOH 562 1362 1706 HOH HOH B . 
X 4 HOH 563 1363 1591 HOH HOH B . 
X 4 HOH 564 1364 1195 HOH HOH B . 
X 4 HOH 565 1365 1547 HOH HOH B . 
X 4 HOH 566 1366 1243 HOH HOH B . 
X 4 HOH 567 1367 1762 HOH HOH B . 
X 4 HOH 568 1368 1739 HOH HOH B . 
X 4 HOH 569 1369 1225 HOH HOH B . 
X 4 HOH 570 1370 1757 HOH HOH B . 
X 4 HOH 571 1371 1941 HOH HOH B . 
X 4 HOH 572 1372 800  HOH HOH B . 
X 4 HOH 573 1373 1994 HOH HOH B . 
X 4 HOH 574 1374 1881 HOH HOH B . 
X 4 HOH 575 1375 1575 HOH HOH B . 
X 4 HOH 576 1376 1587 HOH HOH B . 
X 4 HOH 577 1377 848  HOH HOH B . 
X 4 HOH 578 1378 1041 HOH HOH B . 
X 4 HOH 579 1379 1167 HOH HOH B . 
X 4 HOH 580 1380 2069 HOH HOH B . 
X 4 HOH 581 1381 1819 HOH HOH B . 
X 4 HOH 582 1382 384  HOH HOH B . 
X 4 HOH 583 1383 574  HOH HOH B . 
Y 4 HOH 1   801  1112 HOH HOH C . 
Y 4 HOH 2   802  454  HOH HOH C . 
Y 4 HOH 3   803  2035 HOH HOH C . 
Y 4 HOH 4   804  2019 HOH HOH C . 
Y 4 HOH 5   805  1843 HOH HOH C . 
Y 4 HOH 6   806  2106 HOH HOH C . 
Y 4 HOH 7   807  1143 HOH HOH C . 
Y 4 HOH 8   808  1411 HOH HOH C . 
Y 4 HOH 9   809  1375 HOH HOH C . 
Y 4 HOH 10  810  732  HOH HOH C . 
Y 4 HOH 11  811  1746 HOH HOH C . 
Y 4 HOH 12  812  771  HOH HOH C . 
Y 4 HOH 13  813  1292 HOH HOH C . 
Y 4 HOH 14  814  1521 HOH HOH C . 
Y 4 HOH 15  815  1483 HOH HOH C . 
Y 4 HOH 16  816  922  HOH HOH C . 
Y 4 HOH 17  817  1480 HOH HOH C . 
Y 4 HOH 18  818  1849 HOH HOH C . 
Y 4 HOH 19  819  1838 HOH HOH C . 
Y 4 HOH 20  820  635  HOH HOH C . 
Y 4 HOH 21  821  906  HOH HOH C . 
Y 4 HOH 22  822  1484 HOH HOH C . 
Y 4 HOH 23  823  478  HOH HOH C . 
Y 4 HOH 24  824  746  HOH HOH C . 
Y 4 HOH 25  825  645  HOH HOH C . 
Y 4 HOH 26  826  983  HOH HOH C . 
Y 4 HOH 27  827  1186 HOH HOH C . 
Y 4 HOH 28  828  910  HOH HOH C . 
Y 4 HOH 29  829  847  HOH HOH C . 
Y 4 HOH 30  830  1627 HOH HOH C . 
Y 4 HOH 31  831  1610 HOH HOH C . 
Y 4 HOH 32  832  1855 HOH HOH C . 
Y 4 HOH 33  833  890  HOH HOH C . 
Y 4 HOH 34  834  977  HOH HOH C . 
Y 4 HOH 35  835  876  HOH HOH C . 
Y 4 HOH 36  836  692  HOH HOH C . 
Y 4 HOH 37  837  659  HOH HOH C . 
Y 4 HOH 38  838  436  HOH HOH C . 
Y 4 HOH 39  839  261  HOH HOH C . 
Y 4 HOH 40  840  432  HOH HOH C . 
Y 4 HOH 41  841  94   HOH HOH C . 
Y 4 HOH 42  842  339  HOH HOH C . 
Y 4 HOH 43  843  465  HOH HOH C . 
Y 4 HOH 44  844  501  HOH HOH C . 
Y 4 HOH 45  845  125  HOH HOH C . 
Y 4 HOH 46  846  155  HOH HOH C . 
Y 4 HOH 47  847  270  HOH HOH C . 
Y 4 HOH 48  848  367  HOH HOH C . 
Y 4 HOH 49  849  1122 HOH HOH C . 
Y 4 HOH 50  850  114  HOH HOH C . 
Y 4 HOH 51  851  498  HOH HOH C . 
Y 4 HOH 52  852  14   HOH HOH C . 
Y 4 HOH 53  853  1503 HOH HOH C . 
Y 4 HOH 54  854  1846 HOH HOH C . 
Y 4 HOH 55  855  914  HOH HOH C . 
Y 4 HOH 56  856  506  HOH HOH C . 
Y 4 HOH 57  857  1291 HOH HOH C . 
Y 4 HOH 58  858  1297 HOH HOH C . 
Y 4 HOH 59  859  1151 HOH HOH C . 
Y 4 HOH 60  860  148  HOH HOH C . 
Y 4 HOH 61  861  1423 HOH HOH C . 
Y 4 HOH 62  862  1178 HOH HOH C . 
Y 4 HOH 63  863  513  HOH HOH C . 
Y 4 HOH 64  864  1624 HOH HOH C . 
Y 4 HOH 65  865  671  HOH HOH C . 
Y 4 HOH 66  866  236  HOH HOH C . 
Y 4 HOH 67  867  76   HOH HOH C . 
Y 4 HOH 68  868  1213 HOH HOH C . 
Y 4 HOH 69  869  392  HOH HOH C . 
Y 4 HOH 70  870  152  HOH HOH C . 
Y 4 HOH 71  871  43   HOH HOH C . 
Y 4 HOH 72  872  949  HOH HOH C . 
Y 4 HOH 73  873  733  HOH HOH C . 
Y 4 HOH 74  874  231  HOH HOH C . 
Y 4 HOH 75  875  1864 HOH HOH C . 
Y 4 HOH 76  876  176  HOH HOH C . 
Y 4 HOH 77  877  2009 HOH HOH C . 
Y 4 HOH 78  878  191  HOH HOH C . 
Y 4 HOH 79  879  871  HOH HOH C . 
Y 4 HOH 80  880  1308 HOH HOH C . 
Y 4 HOH 81  881  1088 HOH HOH C . 
Y 4 HOH 82  882  2029 HOH HOH C . 
Y 4 HOH 83  883  105  HOH HOH C . 
Y 4 HOH 84  884  2016 HOH HOH C . 
Y 4 HOH 85  885  627  HOH HOH C . 
Y 4 HOH 86  886  1775 HOH HOH C . 
Y 4 HOH 87  887  230  HOH HOH C . 
Y 4 HOH 88  888  1873 HOH HOH C . 
Y 4 HOH 89  889  567  HOH HOH C . 
Y 4 HOH 90  890  577  HOH HOH C . 
Y 4 HOH 91  891  1324 HOH HOH C . 
Y 4 HOH 92  892  2026 HOH HOH C . 
Y 4 HOH 93  893  1494 HOH HOH C . 
Y 4 HOH 94  894  404  HOH HOH C . 
Y 4 HOH 95  895  1220 HOH HOH C . 
Y 4 HOH 96  896  1498 HOH HOH C . 
Y 4 HOH 97  897  490  HOH HOH C . 
Y 4 HOH 98  898  1339 HOH HOH C . 
Y 4 HOH 99  899  1623 HOH HOH C . 
Y 4 HOH 100 900  27   HOH HOH C . 
Y 4 HOH 101 901  1870 HOH HOH C . 
Y 4 HOH 102 902  248  HOH HOH C . 
Y 4 HOH 103 903  2030 HOH HOH C . 
Y 4 HOH 104 904  608  HOH HOH C . 
Y 4 HOH 105 905  1428 HOH HOH C . 
Y 4 HOH 106 906  320  HOH HOH C . 
Y 4 HOH 107 907  2109 HOH HOH C . 
Y 4 HOH 108 908  791  HOH HOH C . 
Y 4 HOH 109 909  266  HOH HOH C . 
Y 4 HOH 110 910  950  HOH HOH C . 
Y 4 HOH 111 911  1433 HOH HOH C . 
Y 4 HOH 112 912  1602 HOH HOH C . 
Y 4 HOH 113 913  1396 HOH HOH C . 
Y 4 HOH 114 914  720  HOH HOH C . 
Y 4 HOH 115 915  626  HOH HOH C . 
Y 4 HOH 116 916  750  HOH HOH C . 
Y 4 HOH 117 917  648  HOH HOH C . 
Y 4 HOH 118 918  141  HOH HOH C . 
Y 4 HOH 119 919  1412 HOH HOH C . 
Y 4 HOH 120 920  110  HOH HOH C . 
Y 4 HOH 121 921  18   HOH HOH C . 
Y 4 HOH 122 922  46   HOH HOH C . 
Y 4 HOH 123 923  865  HOH HOH C . 
Y 4 HOH 124 924  504  HOH HOH C . 
Y 4 HOH 125 925  1357 HOH HOH C . 
Y 4 HOH 126 926  588  HOH HOH C . 
Y 4 HOH 127 927  242  HOH HOH C . 
Y 4 HOH 128 928  1853 HOH HOH C . 
Y 4 HOH 129 929  1854 HOH HOH C . 
Y 4 HOH 130 930  1349 HOH HOH C . 
Y 4 HOH 131 931  752  HOH HOH C . 
Y 4 HOH 132 932  1659 HOH HOH C . 
Y 4 HOH 133 933  293  HOH HOH C . 
Y 4 HOH 134 934  997  HOH HOH C . 
Y 4 HOH 135 935  164  HOH HOH C . 
Y 4 HOH 136 936  25   HOH HOH C . 
Y 4 HOH 137 937  1062 HOH HOH C . 
Y 4 HOH 138 938  429  HOH HOH C . 
Y 4 HOH 139 939  701  HOH HOH C . 
Y 4 HOH 140 940  296  HOH HOH C . 
Y 4 HOH 141 941  450  HOH HOH C . 
Y 4 HOH 142 942  53   HOH HOH C . 
Y 4 HOH 143 943  726  HOH HOH C . 
Y 4 HOH 144 944  830  HOH HOH C . 
Y 4 HOH 145 945  289  HOH HOH C . 
Y 4 HOH 146 946  817  HOH HOH C . 
Y 4 HOH 147 947  812  HOH HOH C . 
Y 4 HOH 148 948  233  HOH HOH C . 
Y 4 HOH 149 949  329  HOH HOH C . 
Y 4 HOH 150 950  873  HOH HOH C . 
Y 4 HOH 151 951  213  HOH HOH C . 
Y 4 HOH 152 952  674  HOH HOH C . 
Y 4 HOH 153 953  1042 HOH HOH C . 
Y 4 HOH 154 954  601  HOH HOH C . 
Y 4 HOH 155 955  2108 HOH HOH C . 
Y 4 HOH 156 956  1495 HOH HOH C . 
Y 4 HOH 157 957  767  HOH HOH C . 
Y 4 HOH 158 958  139  HOH HOH C . 
Y 4 HOH 159 959  810  HOH HOH C . 
Y 4 HOH 160 960  1551 HOH HOH C . 
Y 4 HOH 161 961  881  HOH HOH C . 
Y 4 HOH 162 962  204  HOH HOH C . 
Y 4 HOH 163 963  1845 HOH HOH C . 
Y 4 HOH 164 964  17   HOH HOH C . 
Y 4 HOH 165 965  921  HOH HOH C . 
Y 4 HOH 166 966  210  HOH HOH C . 
Y 4 HOH 167 967  1256 HOH HOH C . 
Y 4 HOH 168 968  587  HOH HOH C . 
Y 4 HOH 169 969  1152 HOH HOH C . 
Y 4 HOH 170 970  255  HOH HOH C . 
Y 4 HOH 171 971  481  HOH HOH C . 
Y 4 HOH 172 972  421  HOH HOH C . 
Y 4 HOH 173 973  1337 HOH HOH C . 
Y 4 HOH 174 974  622  HOH HOH C . 
Y 4 HOH 175 975  435  HOH HOH C . 
Y 4 HOH 176 976  1590 HOH HOH C . 
Y 4 HOH 177 977  734  HOH HOH C . 
Y 4 HOH 178 978  703  HOH HOH C . 
Y 4 HOH 179 979  9    HOH HOH C . 
Y 4 HOH 180 980  1468 HOH HOH C . 
Y 4 HOH 181 981  1859 HOH HOH C . 
Y 4 HOH 182 982  273  HOH HOH C . 
Y 4 HOH 183 983  1381 HOH HOH C . 
Y 4 HOH 184 984  911  HOH HOH C . 
Y 4 HOH 185 985  398  HOH HOH C . 
Y 4 HOH 186 986  1200 HOH HOH C . 
Y 4 HOH 187 987  456  HOH HOH C . 
Y 4 HOH 188 988  984  HOH HOH C . 
Y 4 HOH 189 989  932  HOH HOH C . 
Y 4 HOH 190 990  417  HOH HOH C . 
Y 4 HOH 191 991  1470 HOH HOH C . 
Y 4 HOH 192 992  649  HOH HOH C . 
Y 4 HOH 193 993  16   HOH HOH C . 
Y 4 HOH 194 994  132  HOH HOH C . 
Y 4 HOH 195 995  541  HOH HOH C . 
Y 4 HOH 196 996  957  HOH HOH C . 
Y 4 HOH 197 997  1250 HOH HOH C . 
Y 4 HOH 198 998  606  HOH HOH C . 
Y 4 HOH 199 999  888  HOH HOH C . 
Y 4 HOH 200 1000 2036 HOH HOH C . 
Y 4 HOH 201 1001 143  HOH HOH C . 
Y 4 HOH 202 1002 360  HOH HOH C . 
Y 4 HOH 203 1003 349  HOH HOH C . 
Y 4 HOH 204 1004 350  HOH HOH C . 
Y 4 HOH 205 1005 1959 HOH HOH C . 
Y 4 HOH 206 1006 669  HOH HOH C . 
Y 4 HOH 207 1007 2010 HOH HOH C . 
Y 4 HOH 208 1008 1306 HOH HOH C . 
Y 4 HOH 209 1009 596  HOH HOH C . 
Y 4 HOH 210 1010 799  HOH HOH C . 
Y 4 HOH 211 1011 2033 HOH HOH C . 
Y 4 HOH 212 1012 1839 HOH HOH C . 
Y 4 HOH 213 1013 553  HOH HOH C . 
Y 4 HOH 214 1014 570  HOH HOH C . 
Y 4 HOH 215 1015 135  HOH HOH C . 
Y 4 HOH 216 1016 1033 HOH HOH C . 
Y 4 HOH 217 1017 201  HOH HOH C . 
Y 4 HOH 218 1018 628  HOH HOH C . 
Y 4 HOH 219 1019 1828 HOH HOH C . 
Y 4 HOH 220 1020 1309 HOH HOH C . 
Y 4 HOH 221 1021 1830 HOH HOH C . 
Y 4 HOH 222 1022 1810 HOH HOH C . 
Y 4 HOH 223 1023 137  HOH HOH C . 
Y 4 HOH 224 1024 2107 HOH HOH C . 
Y 4 HOH 225 1025 162  HOH HOH C . 
Y 4 HOH 226 1026 118  HOH HOH C . 
Y 4 HOH 227 1027 2005 HOH HOH C . 
Y 4 HOH 228 1028 723  HOH HOH C . 
Y 4 HOH 229 1029 1825 HOH HOH C . 
Y 4 HOH 230 1030 2008 HOH HOH C . 
Y 4 HOH 231 1031 1817 HOH HOH C . 
Y 4 HOH 232 1032 1822 HOH HOH C . 
Y 4 HOH 233 1033 749  HOH HOH C . 
Y 4 HOH 234 1034 1837 HOH HOH C . 
Y 4 HOH 235 1035 989  HOH HOH C . 
Y 4 HOH 236 1036 216  HOH HOH C . 
Y 4 HOH 237 1037 98   HOH HOH C . 
Y 4 HOH 238 1038 1248 HOH HOH C . 
Y 4 HOH 239 1039 309  HOH HOH C . 
Y 4 HOH 240 1040 75   HOH HOH C . 
Y 4 HOH 241 1041 1283 HOH HOH C . 
Y 4 HOH 242 1042 594  HOH HOH C . 
Y 4 HOH 243 1043 196  HOH HOH C . 
Y 4 HOH 244 1044 792  HOH HOH C . 
Y 4 HOH 245 1045 1858 HOH HOH C . 
Y 4 HOH 246 1046 1539 HOH HOH C . 
Y 4 HOH 247 1047 168  HOH HOH C . 
Y 4 HOH 248 1048 1865 HOH HOH C . 
Y 4 HOH 249 1049 21   HOH HOH C . 
Y 4 HOH 250 1050 730  HOH HOH C . 
Y 4 HOH 251 1051 1631 HOH HOH C . 
Y 4 HOH 252 1052 444  HOH HOH C . 
Y 4 HOH 253 1053 1842 HOH HOH C . 
Y 4 HOH 254 1054 503  HOH HOH C . 
Y 4 HOH 255 1055 1848 HOH HOH C . 
Y 4 HOH 256 1056 1366 HOH HOH C . 
Y 4 HOH 257 1057 802  HOH HOH C . 
Y 4 HOH 258 1058 237  HOH HOH C . 
Y 4 HOH 259 1059 979  HOH HOH C . 
Y 4 HOH 260 1060 147  HOH HOH C . 
Y 4 HOH 261 1061 1868 HOH HOH C . 
Y 4 HOH 262 1062 1075 HOH HOH C . 
Y 4 HOH 263 1063 410  HOH HOH C . 
Y 4 HOH 264 1064 175  HOH HOH C . 
Y 4 HOH 265 1065 1811 HOH HOH C . 
Y 4 HOH 266 1066 1084 HOH HOH C . 
Y 4 HOH 267 1067 1565 HOH HOH C . 
Y 4 HOH 268 1068 1841 HOH HOH C . 
Y 4 HOH 269 1069 856  HOH HOH C . 
Y 4 HOH 270 1070 1382 HOH HOH C . 
Y 4 HOH 271 1071 2006 HOH HOH C . 
Y 4 HOH 272 1072 1216 HOH HOH C . 
Y 4 HOH 273 1073 1154 HOH HOH C . 
Y 4 HOH 274 1074 1445 HOH HOH C . 
Y 4 HOH 275 1075 8    HOH HOH C . 
Y 4 HOH 276 1076 761  HOH HOH C . 
Y 4 HOH 277 1077 550  HOH HOH C . 
Y 4 HOH 278 1078 1303 HOH HOH C . 
Y 4 HOH 279 1079 704  HOH HOH C . 
Y 4 HOH 280 1080 592  HOH HOH C . 
Y 4 HOH 281 1081 685  HOH HOH C . 
Y 4 HOH 282 1082 1406 HOH HOH C . 
Y 4 HOH 283 1083 1002 HOH HOH C . 
Y 4 HOH 284 1084 1052 HOH HOH C . 
Y 4 HOH 285 1085 1622 HOH HOH C . 
Y 4 HOH 286 1086 1334 HOH HOH C . 
Y 4 HOH 287 1087 1419 HOH HOH C . 
Y 4 HOH 288 1088 1273 HOH HOH C . 
Y 4 HOH 289 1089 786  HOH HOH C . 
Y 4 HOH 290 1090 1632 HOH HOH C . 
Y 4 HOH 291 1091 1066 HOH HOH C . 
Y 4 HOH 292 1092 286  HOH HOH C . 
Y 4 HOH 293 1093 1101 HOH HOH C . 
Y 4 HOH 294 1094 1449 HOH HOH C . 
Y 4 HOH 295 1095 466  HOH HOH C . 
Y 4 HOH 296 1096 238  HOH HOH C . 
Y 4 HOH 297 1097 742  HOH HOH C . 
Y 4 HOH 298 1098 633  HOH HOH C . 
Y 4 HOH 299 1099 781  HOH HOH C . 
Y 4 HOH 300 1100 1950 HOH HOH C . 
Y 4 HOH 301 1101 2111 HOH HOH C . 
Y 4 HOH 302 1102 1171 HOH HOH C . 
Y 4 HOH 303 1103 604  HOH HOH C . 
Y 4 HOH 304 1104 295  HOH HOH C . 
Y 4 HOH 305 1105 1425 HOH HOH C . 
Y 4 HOH 306 1106 1980 HOH HOH C . 
Y 4 HOH 307 1107 403  HOH HOH C . 
Y 4 HOH 308 1108 739  HOH HOH C . 
Y 4 HOH 309 1109 523  HOH HOH C . 
Y 4 HOH 310 1110 1444 HOH HOH C . 
Y 4 HOH 311 1111 1237 HOH HOH C . 
Y 4 HOH 312 1112 1628 HOH HOH C . 
Y 4 HOH 313 1113 1844 HOH HOH C . 
Y 4 HOH 314 1114 1442 HOH HOH C . 
Y 4 HOH 315 1115 129  HOH HOH C . 
Y 4 HOH 316 1116 803  HOH HOH C . 
Y 4 HOH 317 1117 507  HOH HOH C . 
Y 4 HOH 318 1118 276  HOH HOH C . 
Y 4 HOH 319 1119 1821 HOH HOH C . 
Y 4 HOH 320 1120 212  HOH HOH C . 
Y 4 HOH 321 1121 365  HOH HOH C . 
Y 4 HOH 322 1122 113  HOH HOH C . 
Y 4 HOH 323 1123 1601 HOH HOH C . 
Y 4 HOH 324 1124 479  HOH HOH C . 
Y 4 HOH 325 1125 226  HOH HOH C . 
Y 4 HOH 326 1126 1188 HOH HOH C . 
Y 4 HOH 327 1127 987  HOH HOH C . 
Y 4 HOH 328 1128 2017 HOH HOH C . 
Y 4 HOH 329 1129 32   HOH HOH C . 
Y 4 HOH 330 1130 566  HOH HOH C . 
Y 4 HOH 331 1131 1422 HOH HOH C . 
Y 4 HOH 332 1132 1293 HOH HOH C . 
Y 4 HOH 333 1133 582  HOH HOH C . 
Y 4 HOH 334 1134 1104 HOH HOH C . 
Y 4 HOH 335 1135 1867 HOH HOH C . 
Y 4 HOH 336 1136 1813 HOH HOH C . 
Y 4 HOH 337 1137 918  HOH HOH C . 
Y 4 HOH 338 1138 1260 HOH HOH C . 
Y 4 HOH 339 1139 1952 HOH HOH C . 
Y 4 HOH 340 1140 1246 HOH HOH C . 
Y 4 HOH 341 1141 521  HOH HOH C . 
Y 4 HOH 342 1142 1823 HOH HOH C . 
Y 4 HOH 343 1143 1566 HOH HOH C . 
Y 4 HOH 344 1144 2032 HOH HOH C . 
Y 4 HOH 345 1145 409  HOH HOH C . 
Y 4 HOH 346 1146 1368 HOH HOH C . 
Y 4 HOH 347 1147 666  HOH HOH C . 
Y 4 HOH 348 1148 142  HOH HOH C . 
Y 4 HOH 349 1149 826  HOH HOH C . 
Y 4 HOH 350 1150 533  HOH HOH C . 
Y 4 HOH 351 1151 1400 HOH HOH C . 
Y 4 HOH 352 1152 1626 HOH HOH C . 
Y 4 HOH 353 1153 472  HOH HOH C . 
Y 4 HOH 354 1154 390  HOH HOH C . 
Y 4 HOH 355 1155 1814 HOH HOH C . 
Y 4 HOH 356 1156 2021 HOH HOH C . 
Y 4 HOH 357 1157 1871 HOH HOH C . 
Y 4 HOH 358 1158 948  HOH HOH C . 
Y 4 HOH 359 1159 1244 HOH HOH C . 
Y 4 HOH 360 1160 1229 HOH HOH C . 
Y 4 HOH 361 1161 1358 HOH HOH C . 
Y 4 HOH 362 1162 1621 HOH HOH C . 
Y 4 HOH 363 1163 2007 HOH HOH C . 
Y 4 HOH 364 1164 1863 HOH HOH C . 
Y 4 HOH 365 1165 525  HOH HOH C . 
Y 4 HOH 366 1166 1060 HOH HOH C . 
Y 4 HOH 367 1167 1298 HOH HOH C . 
Y 4 HOH 368 1168 159  HOH HOH C . 
Y 4 HOH 369 1169 1372 HOH HOH C . 
Y 4 HOH 370 1170 667  HOH HOH C . 
Y 4 HOH 371 1171 1509 HOH HOH C . 
Y 4 HOH 372 1172 6    HOH HOH C . 
Y 4 HOH 373 1173 2014 HOH HOH C . 
Y 4 HOH 374 1174 1824 HOH HOH C . 
Y 4 HOH 375 1175 1190 HOH HOH C . 
Y 4 HOH 376 1176 2104 HOH HOH C . 
Y 4 HOH 377 1177 718  HOH HOH C . 
Y 4 HOH 378 1178 1862 HOH HOH C . 
Y 4 HOH 379 1179 1441 HOH HOH C . 
Y 4 HOH 380 1180 1857 HOH HOH C . 
Y 4 HOH 381 1181 1629 HOH HOH C . 
Y 4 HOH 382 1182 657  HOH HOH C . 
Y 4 HOH 383 1183 1044 HOH HOH C . 
Y 4 HOH 384 1184 1279 HOH HOH C . 
Y 4 HOH 385 1185 1850 HOH HOH C . 
Y 4 HOH 386 1186 2034 HOH HOH C . 
Y 4 HOH 387 1187 1414 HOH HOH C . 
Y 4 HOH 388 1188 923  HOH HOH C . 
Y 4 HOH 389 1189 1536 HOH HOH C . 
Y 4 HOH 390 1190 408  HOH HOH C . 
Y 4 HOH 391 1191 511  HOH HOH C . 
Y 4 HOH 392 1192 555  HOH HOH C . 
Y 4 HOH 393 1193 1826 HOH HOH C . 
Y 4 HOH 394 1194 1956 HOH HOH C . 
Y 4 HOH 395 1195 1214 HOH HOH C . 
Y 4 HOH 396 1196 1239 HOH HOH C . 
Y 4 HOH 397 1197 884  HOH HOH C . 
Y 4 HOH 398 1198 1570 HOH HOH C . 
Y 4 HOH 399 1199 1257 HOH HOH C . 
Y 4 HOH 400 1200 1808 HOH HOH C . 
Y 4 HOH 401 1201 638  HOH HOH C . 
Y 4 HOH 402 1202 2103 HOH HOH C . 
Y 4 HOH 403 1203 1835 HOH HOH C . 
Y 4 HOH 404 1204 1430 HOH HOH C . 
Y 4 HOH 405 1205 927  HOH HOH C . 
Y 4 HOH 406 1206 1087 HOH HOH C . 
Y 4 HOH 407 1207 2012 HOH HOH C . 
Y 4 HOH 408 1208 2105 HOH HOH C . 
Y 4 HOH 409 1209 768  HOH HOH C . 
Y 4 HOH 410 1210 827  HOH HOH C . 
Y 4 HOH 411 1211 2110 HOH HOH C . 
Y 4 HOH 412 1212 2122 HOH HOH C . 
Y 4 HOH 413 1213 1836 HOH HOH C . 
Y 4 HOH 414 1214 1951 HOH HOH C . 
Y 4 HOH 415 1215 647  HOH HOH C . 
Y 4 HOH 416 1216 1488 HOH HOH C . 
Y 4 HOH 417 1217 1405 HOH HOH C . 
Y 4 HOH 418 1218 909  HOH HOH C . 
Y 4 HOH 419 1219 133  HOH HOH C . 
Y 4 HOH 420 1220 1827 HOH HOH C . 
Y 4 HOH 421 1221 1625 HOH HOH C . 
Y 4 HOH 422 1222 1583 HOH HOH C . 
Y 4 HOH 423 1223 630  HOH HOH C . 
Y 4 HOH 424 1224 1268 HOH HOH C . 
Y 4 HOH 425 1225 1036 HOH HOH C . 
Y 4 HOH 426 1226 493  HOH HOH C . 
Y 4 HOH 427 1227 1729 HOH HOH C . 
Y 4 HOH 428 1228 1586 HOH HOH C . 
Y 4 HOH 429 1229 2072 HOH HOH C . 
Y 4 HOH 430 1230 1561 HOH HOH C . 
Y 4 HOH 431 1231 908  HOH HOH C . 
Y 4 HOH 432 1232 690  HOH HOH C . 
Y 4 HOH 433 1233 2024 HOH HOH C . 
Y 4 HOH 434 1234 813  HOH HOH C . 
Y 4 HOH 435 1235 2060 HOH HOH C . 
Y 4 HOH 436 1236 2031 HOH HOH C . 
Y 4 HOH 437 1237 1620 HOH HOH C . 
Y 4 HOH 438 1238 1005 HOH HOH C . 
Y 4 HOH 439 1239 2054 HOH HOH C . 
Y 4 HOH 440 1240 1021 HOH HOH C . 
Y 4 HOH 441 1241 1633 HOH HOH C . 
Y 4 HOH 442 1242 1026 HOH HOH C . 
Y 4 HOH 443 1243 1508 HOH HOH C . 
Y 4 HOH 444 1244 1829 HOH HOH C . 
Y 4 HOH 445 1245 1098 HOH HOH C . 
Y 4 HOH 446 1246 1487 HOH HOH C . 
Y 4 HOH 447 1247 1995 HOH HOH C . 
Y 4 HOH 448 1248 1852 HOH HOH C . 
Y 4 HOH 449 1249 1058 HOH HOH C . 
Y 4 HOH 450 1250 1434 HOH HOH C . 
Y 4 HOH 451 1251 1861 HOH HOH C . 
Y 4 HOH 452 1252 1630 HOH HOH C . 
Y 4 HOH 453 1253 262  HOH HOH C . 
Y 4 HOH 454 1254 144  HOH HOH C . 
Y 4 HOH 455 1255 1270 HOH HOH C . 
Y 4 HOH 456 1256 1046 HOH HOH C . 
Y 4 HOH 457 1257 872  HOH HOH C . 
Y 4 HOH 458 1258 1617 HOH HOH C . 
Y 4 HOH 459 1259 1609 HOH HOH C . 
Y 4 HOH 460 1260 1809 HOH HOH C . 
Y 4 HOH 461 1261 499  HOH HOH C . 
Y 4 HOH 462 1262 1295 HOH HOH C . 
Y 4 HOH 463 1263 1833 HOH HOH C . 
Y 4 HOH 464 1264 2011 HOH HOH C . 
Y 4 HOH 465 1265 1028 HOH HOH C . 
Y 4 HOH 466 1266 1872 HOH HOH C . 
Y 4 HOH 467 1267 2023 HOH HOH C . 
Y 4 HOH 468 1268 2056 HOH HOH C . 
Y 4 HOH 469 1269 1635 HOH HOH C . 
Y 4 HOH 470 1270 1954 HOH HOH C . 
Y 4 HOH 471 1271 1634 HOH HOH C . 
Y 4 HOH 472 1272 756  HOH HOH C . 
Y 4 HOH 473 1273 816  HOH HOH C . 
Y 4 HOH 474 1274 1059 HOH HOH C . 
Y 4 HOH 475 1275 773  HOH HOH C . 
Y 4 HOH 476 1276 2022 HOH HOH C . 
Y 4 HOH 477 1277 1534 HOH HOH C . 
Y 4 HOH 478 1278 980  HOH HOH C . 
Y 4 HOH 479 1279 1327 HOH HOH C . 
Y 4 HOH 480 1280 1832 HOH HOH C . 
Y 4 HOH 481 1281 1089 HOH HOH C . 
Y 4 HOH 482 1282 1221 HOH HOH C . 
Y 4 HOH 483 1283 1169 HOH HOH C . 
Y 4 HOH 484 1284 2028 HOH HOH C . 
Y 4 HOH 485 1285 1860 HOH HOH C . 
Y 4 HOH 486 1286 2127 HOH HOH C . 
Y 4 HOH 487 1287 934  HOH HOH C . 
Y 4 HOH 488 1288 958  HOH HOH C . 
Y 4 HOH 489 1289 1463 HOH HOH C . 
Y 4 HOH 490 1290 2018 HOH HOH C . 
Y 4 HOH 491 1291 1004 HOH HOH C . 
Y 4 HOH 492 1292 2027 HOH HOH C . 
Y 4 HOH 493 1293 1108 HOH HOH C . 
Y 4 HOH 494 1294 1072 HOH HOH C . 
Y 4 HOH 495 1295 825  HOH HOH C . 
Y 4 HOH 496 1296 994  HOH HOH C . 
Y 4 HOH 497 1297 1506 HOH HOH C . 
Y 4 HOH 498 1298 1856 HOH HOH C . 
Y 4 HOH 499 1299 1030 HOH HOH C . 
Y 4 HOH 500 1300 1552 HOH HOH C . 
Y 4 HOH 501 1301 1129 HOH HOH C . 
Y 4 HOH 502 1302 1109 HOH HOH C . 
Y 4 HOH 503 1303 2015 HOH HOH C . 
Y 4 HOH 504 1304 325  HOH HOH C . 
Y 4 HOH 505 1305 1331 HOH HOH C . 
Y 4 HOH 506 1306 2020 HOH HOH C . 
Y 4 HOH 507 1307 878  HOH HOH C . 
Y 4 HOH 508 1308 1340 HOH HOH C . 
Y 4 HOH 509 1309 2025 HOH HOH C . 
Z 4 HOH 1   801  1919 HOH HOH D . 
Z 4 HOH 2   802  1896 HOH HOH D . 
Z 4 HOH 3   803  2050 HOH HOH D . 
Z 4 HOH 4   804  2053 HOH HOH D . 
Z 4 HOH 5   805  2047 HOH HOH D . 
Z 4 HOH 6   806  1420 HOH HOH D . 
Z 4 HOH 7   807  1540 HOH HOH D . 
Z 4 HOH 8   808  1892 HOH HOH D . 
Z 4 HOH 9   809  1100 HOH HOH D . 
Z 4 HOH 10  810  1343 HOH HOH D . 
Z 4 HOH 11  811  11   HOH HOH D . 
Z 4 HOH 12  812  383  HOH HOH D . 
Z 4 HOH 13  813  1899 HOH HOH D . 
Z 4 HOH 14  814  880  HOH HOH D . 
Z 4 HOH 15  815  843  HOH HOH D . 
Z 4 HOH 16  816  903  HOH HOH D . 
Z 4 HOH 17  817  84   HOH HOH D . 
Z 4 HOH 18  818  1887 HOH HOH D . 
Z 4 HOH 19  819  1505 HOH HOH D . 
Z 4 HOH 20  820  1019 HOH HOH D . 
Z 4 HOH 21  821  620  HOH HOH D . 
Z 4 HOH 22  822  1923 HOH HOH D . 
Z 4 HOH 23  823  1023 HOH HOH D . 
Z 4 HOH 24  824  402  HOH HOH D . 
Z 4 HOH 25  825  297  HOH HOH D . 
Z 4 HOH 26  826  1604 HOH HOH D . 
Z 4 HOH 27  827  665  HOH HOH D . 
Z 4 HOH 28  828  850  HOH HOH D . 
Z 4 HOH 29  829  1917 HOH HOH D . 
Z 4 HOH 30  830  832  HOH HOH D . 
Z 4 HOH 31  831  485  HOH HOH D . 
Z 4 HOH 32  832  265  HOH HOH D . 
Z 4 HOH 33  833  1138 HOH HOH D . 
Z 4 HOH 34  834  885  HOH HOH D . 
Z 4 HOH 35  835  1572 HOH HOH D . 
Z 4 HOH 36  836  858  HOH HOH D . 
Z 4 HOH 37  837  247  HOH HOH D . 
Z 4 HOH 38  838  185  HOH HOH D . 
Z 4 HOH 39  839  1615 HOH HOH D . 
Z 4 HOH 40  840  1847 HOH HOH D . 
Z 4 HOH 41  841  2048 HOH HOH D . 
Z 4 HOH 42  842  1541 HOH HOH D . 
Z 4 HOH 43  843  300  HOH HOH D . 
Z 4 HOH 44  844  1957 HOH HOH D . 
Z 4 HOH 45  845  1460 HOH HOH D . 
Z 4 HOH 46  846  28   HOH HOH D . 
Z 4 HOH 47  847  1526 HOH HOH D . 
Z 4 HOH 48  848  471  HOH HOH D . 
Z 4 HOH 49  849  1889 HOH HOH D . 
Z 4 HOH 50  850  981  HOH HOH D . 
Z 4 HOH 51  851  1607 HOH HOH D . 
Z 4 HOH 52  852  1116 HOH HOH D . 
Z 4 HOH 53  853  92   HOH HOH D . 
Z 4 HOH 54  854  451  HOH HOH D . 
Z 4 HOH 55  855  1174 HOH HOH D . 
Z 4 HOH 56  856  353  HOH HOH D . 
Z 4 HOH 57  857  174  HOH HOH D . 
Z 4 HOH 58  858  446  HOH HOH D . 
Z 4 HOH 59  859  229  HOH HOH D . 
Z 4 HOH 60  860  228  HOH HOH D . 
Z 4 HOH 61  861  1926 HOH HOH D . 
Z 4 HOH 62  862  705  HOH HOH D . 
Z 4 HOH 63  863  530  HOH HOH D . 
Z 4 HOH 64  864  1611 HOH HOH D . 
Z 4 HOH 65  865  282  HOH HOH D . 
Z 4 HOH 66  866  440  HOH HOH D . 
Z 4 HOH 67  867  835  HOH HOH D . 
Z 4 HOH 68  868  352  HOH HOH D . 
Z 4 HOH 69  869  112  HOH HOH D . 
Z 4 HOH 70  870  23   HOH HOH D . 
Z 4 HOH 71  871  1335 HOH HOH D . 
Z 4 HOH 72  872  600  HOH HOH D . 
Z 4 HOH 73  873  614  HOH HOH D . 
Z 4 HOH 74  874  561  HOH HOH D . 
Z 4 HOH 75  875  955  HOH HOH D . 
Z 4 HOH 76  876  1001 HOH HOH D . 
Z 4 HOH 77  877  240  HOH HOH D . 
Z 4 HOH 78  878  2040 HOH HOH D . 
Z 4 HOH 79  879  882  HOH HOH D . 
Z 4 HOH 80  880  1403 HOH HOH D . 
Z 4 HOH 81  881  2039 HOH HOH D . 
Z 4 HOH 82  882  1281 HOH HOH D . 
Z 4 HOH 83  883  163  HOH HOH D . 
Z 4 HOH 84  884  1212 HOH HOH D . 
Z 4 HOH 85  885  460  HOH HOH D . 
Z 4 HOH 86  886  1353 HOH HOH D . 
Z 4 HOH 87  887  552  HOH HOH D . 
Z 4 HOH 88  888  277  HOH HOH D . 
Z 4 HOH 89  889  2116 HOH HOH D . 
Z 4 HOH 90  890  1307 HOH HOH D . 
Z 4 HOH 91  891  1925 HOH HOH D . 
Z 4 HOH 92  892  879  HOH HOH D . 
Z 4 HOH 93  893  877  HOH HOH D . 
Z 4 HOH 94  894  528  HOH HOH D . 
Z 4 HOH 95  895  999  HOH HOH D . 
Z 4 HOH 96  896  258  HOH HOH D . 
Z 4 HOH 97  897  1522 HOH HOH D . 
Z 4 HOH 98  898  748  HOH HOH D . 
Z 4 HOH 99  899  305  HOH HOH D . 
Z 4 HOH 100 900  1208 HOH HOH D . 
Z 4 HOH 101 901  517  HOH HOH D . 
Z 4 HOH 102 902  1955 HOH HOH D . 
Z 4 HOH 103 903  386  HOH HOH D . 
Z 4 HOH 104 904  73   HOH HOH D . 
Z 4 HOH 105 905  22   HOH HOH D . 
Z 4 HOH 106 906  332  HOH HOH D . 
Z 4 HOH 107 907  941  HOH HOH D . 
Z 4 HOH 108 908  397  HOH HOH D . 
Z 4 HOH 109 909  344  HOH HOH D . 
Z 4 HOH 110 910  1359 HOH HOH D . 
Z 4 HOH 111 911  2043 HOH HOH D . 
Z 4 HOH 112 912  663  HOH HOH D . 
Z 4 HOH 113 913  763  HOH HOH D . 
Z 4 HOH 114 914  744  HOH HOH D . 
Z 4 HOH 115 915  721  HOH HOH D . 
Z 4 HOH 116 916  643  HOH HOH D . 
Z 4 HOH 117 917  1064 HOH HOH D . 
Z 4 HOH 118 918  491  HOH HOH D . 
Z 4 HOH 119 919  346  HOH HOH D . 
Z 4 HOH 120 920  1020 HOH HOH D . 
Z 4 HOH 121 921  804  HOH HOH D . 
Z 4 HOH 122 922  70   HOH HOH D . 
Z 4 HOH 123 923  1804 HOH HOH D . 
Z 4 HOH 124 924  364  HOH HOH D . 
Z 4 HOH 125 925  227  HOH HOH D . 
Z 4 HOH 126 926  1492 HOH HOH D . 
Z 4 HOH 127 927  194  HOH HOH D . 
Z 4 HOH 128 928  33   HOH HOH D . 
Z 4 HOH 129 929  753  HOH HOH D . 
Z 4 HOH 130 930  1876 HOH HOH D . 
Z 4 HOH 131 931  1499 HOH HOH D . 
Z 4 HOH 132 932  1204 HOH HOH D . 
Z 4 HOH 133 933  254  HOH HOH D . 
Z 4 HOH 134 934  1184 HOH HOH D . 
Z 4 HOH 135 935  128  HOH HOH D . 
Z 4 HOH 136 936  982  HOH HOH D . 
Z 4 HOH 137 937  3    HOH HOH D . 
Z 4 HOH 138 938  1883 HOH HOH D . 
Z 4 HOH 139 939  996  HOH HOH D . 
Z 4 HOH 140 940  518  HOH HOH D . 
Z 4 HOH 141 941  510  HOH HOH D . 
Z 4 HOH 142 942  63   HOH HOH D . 
Z 4 HOH 143 943  809  HOH HOH D . 
Z 4 HOH 144 944  1588 HOH HOH D . 
Z 4 HOH 145 945  396  HOH HOH D . 
Z 4 HOH 146 946  736  HOH HOH D . 
Z 4 HOH 147 947  1884 HOH HOH D . 
Z 4 HOH 148 948  190  HOH HOH D . 
Z 4 HOH 149 949  1482 HOH HOH D . 
Z 4 HOH 150 950  954  HOH HOH D . 
Z 4 HOH 151 951  793  HOH HOH D . 
Z 4 HOH 152 952  1569 HOH HOH D . 
Z 4 HOH 153 953  476  HOH HOH D . 
Z 4 HOH 154 954  610  HOH HOH D . 
Z 4 HOH 155 955  1141 HOH HOH D . 
Z 4 HOH 156 956  244  HOH HOH D . 
Z 4 HOH 157 957  1387 HOH HOH D . 
Z 4 HOH 158 958  12   HOH HOH D . 
Z 4 HOH 159 959  1131 HOH HOH D . 
Z 4 HOH 160 960  186  HOH HOH D . 
Z 4 HOH 161 961  302  HOH HOH D . 
Z 4 HOH 162 962  380  HOH HOH D . 
Z 4 HOH 163 963  694  HOH HOH D . 
Z 4 HOH 164 964  48   HOH HOH D . 
Z 4 HOH 165 965  700  HOH HOH D . 
Z 4 HOH 166 966  706  HOH HOH D . 
Z 4 HOH 167 967  1910 HOH HOH D . 
Z 4 HOH 168 968  672  HOH HOH D . 
Z 4 HOH 169 969  891  HOH HOH D . 
Z 4 HOH 170 970  1341 HOH HOH D . 
Z 4 HOH 171 971  970  HOH HOH D . 
Z 4 HOH 172 972  251  HOH HOH D . 
Z 4 HOH 173 973  1421 HOH HOH D . 
Z 4 HOH 174 974  1949 HOH HOH D . 
Z 4 HOH 175 975  1069 HOH HOH D . 
Z 4 HOH 176 976  205  HOH HOH D . 
Z 4 HOH 177 977  1253 HOH HOH D . 
Z 4 HOH 178 978  976  HOH HOH D . 
Z 4 HOH 179 979  150  HOH HOH D . 
Z 4 HOH 180 980  171  HOH HOH D . 
Z 4 HOH 181 981  833  HOH HOH D . 
Z 4 HOH 182 982  366  HOH HOH D . 
Z 4 HOH 183 983  474  HOH HOH D . 
Z 4 HOH 184 984  1024 HOH HOH D . 
Z 4 HOH 185 985  1915 HOH HOH D . 
Z 4 HOH 186 986  425  HOH HOH D . 
Z 4 HOH 187 987  438  HOH HOH D . 
Z 4 HOH 188 988  536  HOH HOH D . 
Z 4 HOH 189 989  208  HOH HOH D . 
Z 4 HOH 190 990  2052 HOH HOH D . 
Z 4 HOH 191 991  1146 HOH HOH D . 
Z 4 HOH 192 992  183  HOH HOH D . 
Z 4 HOH 193 993  1009 HOH HOH D . 
Z 4 HOH 194 994  264  HOH HOH D . 
Z 4 HOH 195 995  709  HOH HOH D . 
Z 4 HOH 196 996  1616 HOH HOH D . 
Z 4 HOH 197 997  117  HOH HOH D . 
Z 4 HOH 198 998  540  HOH HOH D . 
Z 4 HOH 199 999  783  HOH HOH D . 
Z 4 HOH 200 1000 2121 HOH HOH D . 
Z 4 HOH 201 1001 1890 HOH HOH D . 
Z 4 HOH 202 1002 1203 HOH HOH D . 
Z 4 HOH 203 1003 527  HOH HOH D . 
Z 4 HOH 204 1004 257  HOH HOH D . 
Z 4 HOH 205 1005 806  HOH HOH D . 
Z 4 HOH 206 1006 1908 HOH HOH D . 
Z 4 HOH 207 1007 1920 HOH HOH D . 
Z 4 HOH 208 1008 1251 HOH HOH D . 
Z 4 HOH 209 1009 855  HOH HOH D . 
Z 4 HOH 210 1010 905  HOH HOH D . 
Z 4 HOH 211 1011 1142 HOH HOH D . 
Z 4 HOH 212 1012 805  HOH HOH D . 
Z 4 HOH 213 1013 1392 HOH HOH D . 
Z 4 HOH 214 1014 323  HOH HOH D . 
Z 4 HOH 215 1015 691  HOH HOH D . 
Z 4 HOH 216 1016 1170 HOH HOH D . 
Z 4 HOH 217 1017 145  HOH HOH D . 
Z 4 HOH 218 1018 1930 HOH HOH D . 
Z 4 HOH 219 1019 618  HOH HOH D . 
Z 4 HOH 220 1020 1530 HOH HOH D . 
Z 4 HOH 221 1021 1888 HOH HOH D . 
Z 4 HOH 222 1022 676  HOH HOH D . 
Z 4 HOH 223 1023 1125 HOH HOH D . 
Z 4 HOH 224 1024 1898 HOH HOH D . 
Z 4 HOH 225 1025 1477 HOH HOH D . 
Z 4 HOH 226 1026 963  HOH HOH D . 
Z 4 HOH 227 1027 747  HOH HOH D . 
Z 4 HOH 228 1028 1134 HOH HOH D . 
Z 4 HOH 229 1029 1606 HOH HOH D . 
Z 4 HOH 230 1030 717  HOH HOH D . 
Z 4 HOH 231 1031 1234 HOH HOH D . 
Z 4 HOH 232 1032 2112 HOH HOH D . 
Z 4 HOH 233 1033 841  HOH HOH D . 
Z 4 HOH 234 1034 893  HOH HOH D . 
Z 4 HOH 235 1035 1878 HOH HOH D . 
Z 4 HOH 236 1036 1050 HOH HOH D . 
Z 4 HOH 237 1037 2051 HOH HOH D . 
Z 4 HOH 238 1038 1350 HOH HOH D . 
Z 4 HOH 239 1039 585  HOH HOH D . 
Z 4 HOH 240 1040 1346 HOH HOH D . 
Z 4 HOH 241 1041 1211 HOH HOH D . 
Z 4 HOH 242 1042 1812 HOH HOH D . 
Z 4 HOH 243 1043 200  HOH HOH D . 
Z 4 HOH 244 1044 1139 HOH HOH D . 
Z 4 HOH 245 1045 423  HOH HOH D . 
Z 4 HOH 246 1046 1373 HOH HOH D . 
Z 4 HOH 247 1047 2037 HOH HOH D . 
Z 4 HOH 248 1048 1247 HOH HOH D . 
Z 4 HOH 249 1049 1218 HOH HOH D . 
Z 4 HOH 250 1050 1608 HOH HOH D . 
Z 4 HOH 251 1051 1386 HOH HOH D . 
Z 4 HOH 252 1052 790  HOH HOH D . 
Z 4 HOH 253 1053 52   HOH HOH D . 
Z 4 HOH 254 1054 1352 HOH HOH D . 
Z 4 HOH 255 1055 195  HOH HOH D . 
Z 4 HOH 256 1056 406  HOH HOH D . 
Z 4 HOH 257 1057 234  HOH HOH D . 
Z 4 HOH 258 1058 321  HOH HOH D . 
Z 4 HOH 259 1059 840  HOH HOH D . 
Z 4 HOH 260 1060 158  HOH HOH D . 
Z 4 HOH 261 1061 2049 HOH HOH D . 
Z 4 HOH 262 1062 545  HOH HOH D . 
Z 4 HOH 263 1063 1379 HOH HOH D . 
Z 4 HOH 264 1064 2046 HOH HOH D . 
Z 4 HOH 265 1065 775  HOH HOH D . 
Z 4 HOH 266 1066 788  HOH HOH D . 
Z 4 HOH 267 1067 77   HOH HOH D . 
Z 4 HOH 268 1068 759  HOH HOH D . 
Z 4 HOH 269 1069 526  HOH HOH D . 
Z 4 HOH 270 1070 104  HOH HOH D . 
Z 4 HOH 271 1071 458  HOH HOH D . 
Z 4 HOH 272 1072 1490 HOH HOH D . 
Z 4 HOH 273 1073 115  HOH HOH D . 
Z 4 HOH 274 1074 222  HOH HOH D . 
Z 4 HOH 275 1075 1921 HOH HOH D . 
Z 4 HOH 276 1076 1900 HOH HOH D . 
Z 4 HOH 277 1077 1376 HOH HOH D . 
Z 4 HOH 278 1078 1571 HOH HOH D . 
Z 4 HOH 279 1079 1252 HOH HOH D . 
Z 4 HOH 280 1080 1056 HOH HOH D . 
Z 4 HOH 281 1081 1907 HOH HOH D . 
Z 4 HOH 282 1082 445  HOH HOH D . 
Z 4 HOH 283 1083 522  HOH HOH D . 
Z 4 HOH 284 1084 304  HOH HOH D . 
Z 4 HOH 285 1085 1435 HOH HOH D . 
Z 4 HOH 286 1086 1486 HOH HOH D . 
Z 4 HOH 287 1087 2119 HOH HOH D . 
Z 4 HOH 288 1088 993  HOH HOH D . 
Z 4 HOH 289 1089 1076 HOH HOH D . 
Z 4 HOH 290 1090 1330 HOH HOH D . 
Z 4 HOH 291 1091 488  HOH HOH D . 
Z 4 HOH 292 1092 223  HOH HOH D . 
Z 4 HOH 293 1093 1302 HOH HOH D . 
Z 4 HOH 294 1094 82   HOH HOH D . 
Z 4 HOH 295 1095 769  HOH HOH D . 
Z 4 HOH 296 1096 369  HOH HOH D . 
Z 4 HOH 297 1097 2115 HOH HOH D . 
Z 4 HOH 298 1098 1815 HOH HOH D . 
Z 4 HOH 299 1099 462  HOH HOH D . 
Z 4 HOH 300 1100 420  HOH HOH D . 
Z 4 HOH 301 1101 1894 HOH HOH D . 
Z 4 HOH 302 1102 298  HOH HOH D . 
Z 4 HOH 303 1103 844  HOH HOH D . 
Z 4 HOH 304 1104 1144 HOH HOH D . 
Z 4 HOH 305 1105 126  HOH HOH D . 
Z 4 HOH 306 1106 1895 HOH HOH D . 
Z 4 HOH 307 1107 1613 HOH HOH D . 
Z 4 HOH 308 1108 1603 HOH HOH D . 
Z 4 HOH 309 1109 1378 HOH HOH D . 
Z 4 HOH 310 1110 883  HOH HOH D . 
Z 4 HOH 311 1111 632  HOH HOH D . 
Z 4 HOH 312 1112 1202 HOH HOH D . 
Z 4 HOH 313 1113 849  HOH HOH D . 
Z 4 HOH 314 1114 1909 HOH HOH D . 
Z 4 HOH 315 1115 655  HOH HOH D . 
Z 4 HOH 316 1116 411  HOH HOH D . 
Z 4 HOH 317 1117 1546 HOH HOH D . 
Z 4 HOH 318 1118 1904 HOH HOH D . 
Z 4 HOH 319 1119 1913 HOH HOH D . 
Z 4 HOH 320 1120 794  HOH HOH D . 
Z 4 HOH 321 1121 1288 HOH HOH D . 
Z 4 HOH 322 1122 1958 HOH HOH D . 
Z 4 HOH 323 1123 636  HOH HOH D . 
Z 4 HOH 324 1124 1067 HOH HOH D . 
Z 4 HOH 325 1125 1027 HOH HOH D . 
Z 4 HOH 326 1126 1123 HOH HOH D . 
Z 4 HOH 327 1127 1548 HOH HOH D . 
Z 4 HOH 328 1128 1017 HOH HOH D . 
Z 4 HOH 329 1129 1119 HOH HOH D . 
Z 4 HOH 330 1130 467  HOH HOH D . 
Z 4 HOH 331 1131 946  HOH HOH D . 
Z 4 HOH 332 1132 1924 HOH HOH D . 
Z 4 HOH 333 1133 940  HOH HOH D . 
Z 4 HOH 334 1134 1016 HOH HOH D . 
Z 4 HOH 335 1135 1877 HOH HOH D . 
Z 4 HOH 336 1136 818  HOH HOH D . 
Z 4 HOH 337 1137 2114 HOH HOH D . 
Z 4 HOH 338 1138 1474 HOH HOH D . 
Z 4 HOH 339 1139 1549 HOH HOH D . 
Z 4 HOH 340 1140 1459 HOH HOH D . 
Z 4 HOH 341 1141 867  HOH HOH D . 
Z 4 HOH 342 1142 1614 HOH HOH D . 
Z 4 HOH 343 1143 824  HOH HOH D . 
Z 4 HOH 344 1144 795  HOH HOH D . 
Z 4 HOH 345 1145 252  HOH HOH D . 
Z 4 HOH 346 1146 1918 HOH HOH D . 
Z 4 HOH 347 1147 1113 HOH HOH D . 
Z 4 HOH 348 1148 30   HOH HOH D . 
Z 4 HOH 349 1149 1187 HOH HOH D . 
Z 4 HOH 350 1150 336  HOH HOH D . 
Z 4 HOH 351 1151 1236 HOH HOH D . 
Z 4 HOH 352 1152 1198 HOH HOH D . 
Z 4 HOH 353 1153 1181 HOH HOH D . 
Z 4 HOH 354 1154 1568 HOH HOH D . 
Z 4 HOH 355 1155 1394 HOH HOH D . 
Z 4 HOH 356 1156 1740 HOH HOH D . 
Z 4 HOH 357 1157 1893 HOH HOH D . 
Z 4 HOH 358 1158 1124 HOH HOH D . 
Z 4 HOH 359 1159 2041 HOH HOH D . 
Z 4 HOH 360 1160 89   HOH HOH D . 
Z 4 HOH 361 1161 1162 HOH HOH D . 
Z 4 HOH 362 1162 1605 HOH HOH D . 
Z 4 HOH 363 1163 774  HOH HOH D . 
Z 4 HOH 364 1164 1012 HOH HOH D . 
Z 4 HOH 365 1165 568  HOH HOH D . 
Z 4 HOH 366 1166 1461 HOH HOH D . 
Z 4 HOH 367 1167 1851 HOH HOH D . 
Z 4 HOH 368 1168 1180 HOH HOH D . 
Z 4 HOH 369 1169 512  HOH HOH D . 
Z 4 HOH 370 1170 2120 HOH HOH D . 
Z 4 HOH 371 1171 912  HOH HOH D . 
Z 4 HOH 372 1172 1266 HOH HOH D . 
Z 4 HOH 373 1173 2113 HOH HOH D . 
Z 4 HOH 374 1174 1563 HOH HOH D . 
Z 4 HOH 375 1175 1911 HOH HOH D . 
Z 4 HOH 376 1176 1761 HOH HOH D . 
Z 4 HOH 377 1177 1491 HOH HOH D . 
Z 4 HOH 378 1178 895  HOH HOH D . 
Z 4 HOH 379 1179 1816 HOH HOH D . 
Z 4 HOH 380 1180 1532 HOH HOH D . 
Z 4 HOH 381 1181 2118 HOH HOH D . 
Z 4 HOH 382 1182 639  HOH HOH D . 
Z 4 HOH 383 1183 580  HOH HOH D . 
Z 4 HOH 384 1184 1902 HOH HOH D . 
Z 4 HOH 385 1185 2117 HOH HOH D . 
Z 4 HOH 386 1186 616  HOH HOH D . 
Z 4 HOH 387 1187 1916 HOH HOH D . 
Z 4 HOH 388 1188 547  HOH HOH D . 
Z 4 HOH 389 1189 37   HOH HOH D . 
Z 4 HOH 390 1190 1456 HOH HOH D . 
Z 4 HOH 391 1191 516  HOH HOH D . 
Z 4 HOH 392 1192 1114 HOH HOH D . 
Z 4 HOH 393 1193 2044 HOH HOH D . 
Z 4 HOH 394 1194 2123 HOH HOH D . 
Z 4 HOH 395 1195 1879 HOH HOH D . 
Z 4 HOH 396 1196 1929 HOH HOH D . 
Z 4 HOH 397 1197 1880 HOH HOH D . 
Z 4 HOH 398 1198 1014 HOH HOH D . 
Z 4 HOH 399 1199 1891 HOH HOH D . 
Z 4 HOH 400 1200 529  HOH HOH D . 
Z 4 HOH 401 1201 1159 HOH HOH D . 
Z 4 HOH 402 1202 1903 HOH HOH D . 
Z 4 HOH 403 1203 322  HOH HOH D . 
Z 4 HOH 404 1204 1612 HOH HOH D . 
Z 4 HOH 405 1205 1927 HOH HOH D . 
Z 4 HOH 406 1206 1556 HOH HOH D . 
Z 4 HOH 407 1207 2045 HOH HOH D . 
Z 4 HOH 408 1208 1086 HOH HOH D . 
Z 4 HOH 409 1209 1574 HOH HOH D . 
Z 4 HOH 410 1210 599  HOH HOH D . 
Z 4 HOH 411 1211 820  HOH HOH D . 
Z 4 HOH 412 1212 1389 HOH HOH D . 
Z 4 HOH 413 1213 725  HOH HOH D . 
Z 4 HOH 414 1214 845  HOH HOH D . 
Z 4 HOH 415 1215 563  HOH HOH D . 
Z 4 HOH 416 1216 1245 HOH HOH D . 
Z 4 HOH 417 1217 1513 HOH HOH D . 
Z 4 HOH 418 1218 1905 HOH HOH D . 
Z 4 HOH 419 1219 929  HOH HOH D . 
Z 4 HOH 420 1220 413  HOH HOH D . 
Z 4 HOH 421 1221 779  HOH HOH D . 
Z 4 HOH 422 1222 1199 HOH HOH D . 
Z 4 HOH 423 1223 1897 HOH HOH D . 
Z 4 HOH 424 1224 1276 HOH HOH D . 
Z 4 HOH 425 1225 1206 HOH HOH D . 
Z 4 HOH 426 1226 823  HOH HOH D . 
Z 4 HOH 427 1227 1914 HOH HOH D . 
Z 4 HOH 428 1228 2064 HOH HOH D . 
Z 4 HOH 429 1229 1118 HOH HOH D . 
Z 4 HOH 430 1230 1240 HOH HOH D . 
Z 4 HOH 431 1231 2038 HOH HOH D . 
Z 4 HOH 432 1232 1063 HOH HOH D . 
Z 4 HOH 433 1233 1511 HOH HOH D . 
Z 4 HOH 434 1234 1869 HOH HOH D . 
Z 4 HOH 435 1235 854  HOH HOH D . 
Z 4 HOH 436 1236 470  HOH HOH D . 
Z 4 HOH 437 1237 1928 HOH HOH D . 
Z 4 HOH 438 1238 1320 HOH HOH D . 
Z 4 HOH 439 1239 1906 HOH HOH D . 
Z 4 HOH 440 1240 1741 HOH HOH D . 
Z 4 HOH 441 1241 1481 HOH HOH D . 
Z 4 HOH 442 1242 886  HOH HOH D . 
Z 4 HOH 443 1243 2042 HOH HOH D . 
Z 4 HOH 444 1244 1885 HOH HOH D . 
Z 4 HOH 445 1245 1886 HOH HOH D . 
Z 4 HOH 446 1246 475  HOH HOH D . 
Z 4 HOH 447 1247 1322 HOH HOH D . 
Z 4 HOH 448 1248 1496 HOH HOH D . 
Z 4 HOH 449 1249 1310 HOH HOH D . 
Z 4 HOH 450 1250 875  HOH HOH D . 
Z 4 HOH 451 1251 1922 HOH HOH D . 
Z 4 HOH 452 1252 1034 HOH HOH D . 
Z 4 HOH 453 1253 424  HOH HOH D . 
Z 4 HOH 454 1254 1912 HOH HOH D . 
Z 4 HOH 455 1255 1077 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A OCS 162 A OCS 154 ? CYS 'modified residue' 
2 B OCS 162 B OCS 154 ? CYS 'modified residue' 
3 C OCS 162 C OCS 154 ? CYS 'modified residue' 
4 D OCS 162 D OCS 154 ? CYS 'modified residue' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,H,W     
2 1 B,I,J,K,X       
3 1 C,L,M,N,O,P,Y   
4 1 D,Q,R,S,T,U,V,Z 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD2 ? A ASP 160 ? A ASP 152  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 OD1 ? A ASN 190 ? A ASN 182  ? 1_555 84.4  ? 
2   OD2 ? A ASP 160 ? A ASP 152  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 OD1 ? A ASN 191 ? A ASN 183  ? 1_555 75.6  ? 
3   OD1 ? A ASN 190 ? A ASN 182  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 OD1 ? A ASN 191 ? A ASN 183  ? 1_555 88.4  ? 
4   OD2 ? A ASP 160 ? A ASP 152  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 842  ? 1_555 83.4  ? 
5   OD1 ? A ASN 190 ? A ASN 182  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 842  ? 1_555 62.9  ? 
6   OD1 ? A ASN 191 ? A ASN 183  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 842  ? 1_555 146.0 ? 
7   OD2 ? A ASP 160 ? A ASP 152  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 1206 ? 1_555 159.9 ? 
8   OD1 ? A ASN 190 ? A ASN 182  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 1206 ? 1_555 79.6  ? 
9   OD1 ? A ASN 191 ? A ASN 183  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 1206 ? 1_555 91.8  ? 
10  O   ? W HOH .   ? A HOH 842  ? 1_555 CA ? G CA . ? A CA 703 ? 1_555 O   ? W HOH .   ? A HOH 1206 ? 1_555 99.9  ? 
11  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 OE2 ? A GLU 641 ? A GLU 633  ? 1_555 51.5  ? 
12  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1196 ? 1_555 121.4 ? 
13  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1196 ? 1_555 81.2  ? 
14  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1000 ? 1_555 82.4  ? 
15  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1000 ? 1_555 99.0  ? 
16  O   ? W HOH .   ? A HOH 1196 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1000 ? 1_555 72.0  ? 
17  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1201 ? 1_555 78.2  ? 
18  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1201 ? 1_555 129.7 ? 
19  O   ? W HOH .   ? A HOH 1196 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1201 ? 1_555 133.3 ? 
20  O   ? X HOH .   ? B HOH 1000 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1201 ? 1_555 69.3  ? 
21  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1339 ? 1_555 149.4 ? 
22  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1339 ? 1_555 158.4 ? 
23  O   ? W HOH .   ? A HOH 1196 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1339 ? 1_555 84.5  ? 
24  O   ? X HOH .   ? B HOH 1000 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1339 ? 1_555 91.8  ? 
25  O   ? X HOH .   ? B HOH 1201 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1339 ? 1_555 71.7  ? 
26  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 116.6 ? 
27  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 78.8  ? 
28  O   ? W HOH .   ? A HOH 1196 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 78.1  ? 
29  O   ? X HOH .   ? B HOH 1000 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 149.9 ? 
30  O   ? X HOH .   ? B HOH 1201 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 134.6 ? 
31  O   ? X HOH .   ? B HOH 1339 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1152 ? 1_555 82.4  ? 
32  OE1 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 77.1  ? 
33  OE2 ? A GLU 641 ? A GLU 633  ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 98.9  ? 
34  O   ? W HOH .   ? A HOH 1196 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 152.0 ? 
35  O   ? X HOH .   ? B HOH 1000 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 134.8 ? 
36  O   ? X HOH .   ? B HOH 1201 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 67.2  ? 
37  O   ? X HOH .   ? B HOH 1339 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 86.2  ? 
38  O   ? W HOH .   ? A HOH 1152 ? 1_555 CA ? F CA . ? A CA 702 ? 1_555 O   ? W HOH .   ? A HOH 1181 ? 1_555 74.5  ? 
39  OD2 ? B ASP 160 ? B ASP 152  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 OD1 ? B ASN 190 ? B ASN 182  ? 1_555 82.6  ? 
40  OD2 ? B ASP 160 ? B ASP 152  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? B ILE 192 ? B ILE 184  ? 1_555 97.9  ? 
41  OD1 ? B ASN 190 ? B ASN 182  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? B ILE 192 ? B ILE 184  ? 1_555 90.7  ? 
42  OD2 ? B ASP 160 ? B ASP 152  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1281 ? 1_555 103.3 ? 
43  OD1 ? B ASN 190 ? B ASN 182  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1281 ? 1_555 173.9 ? 
44  O   ? B ILE 192 ? B ILE 184  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1281 ? 1_555 89.7  ? 
45  OD2 ? B ASP 160 ? B ASP 152  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1242 ? 1_555 170.7 ? 
46  OD1 ? B ASN 190 ? B ASN 182  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1242 ? 1_555 92.7  ? 
47  O   ? B ILE 192 ? B ILE 184  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1242 ? 1_555 90.2  ? 
48  O   ? X HOH .   ? B HOH 1281 ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 1242 ? 1_555 81.2  ? 
49  OD2 ? B ASP 160 ? B ASP 152  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 998  ? 1_555 81.8  ? 
50  OD1 ? B ASN 190 ? B ASN 182  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 998  ? 1_555 92.9  ? 
51  O   ? B ILE 192 ? B ILE 184  ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 998  ? 1_555 176.3 ? 
52  O   ? X HOH .   ? B HOH 1281 ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 998  ? 1_555 86.8  ? 
53  O   ? X HOH .   ? B HOH 1242 ? 1_555 CA ? J CA . ? B CA 702 ? 1_555 O   ? X HOH .   ? B HOH 998  ? 1_555 90.4  ? 
54  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 OE2 ? B GLU 641 ? B GLU 633  ? 1_555 52.0  ? 
55  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 906  ? 1_555 85.2  ? 
56  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 906  ? 1_555 135.3 ? 
57  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1252 ? 1_555 159.1 ? 
58  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1252 ? 1_555 148.9 ? 
59  O   ? W HOH .   ? A HOH 906  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1252 ? 1_555 74.3  ? 
60  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1261 ? 1_555 78.5  ? 
61  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1261 ? 1_555 105.9 ? 
62  O   ? W HOH .   ? A HOH 906  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1261 ? 1_555 72.4  ? 
63  O   ? W HOH .   ? A HOH 1252 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1261 ? 1_555 91.2  ? 
64  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1157 ? 1_555 81.6  ? 
65  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1157 ? 1_555 91.4  ? 
66  O   ? W HOH .   ? A HOH 906  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1157 ? 1_555 67.2  ? 
67  O   ? W HOH .   ? A HOH 1252 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1157 ? 1_555 94.0  ? 
68  O   ? X HOH .   ? B HOH 1261 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? W HOH .   ? A HOH 1157 ? 1_555 136.0 ? 
69  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 114.3 ? 
70  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 80.7  ? 
71  O   ? W HOH .   ? A HOH 906  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 136.3 ? 
72  O   ? W HOH .   ? A HOH 1252 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 79.3  ? 
73  O   ? X HOH .   ? B HOH 1261 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 74.0  ? 
74  O   ? W HOH .   ? A HOH 1157 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1271 ? 1_555 149.7 ? 
75  OE1 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 120.4 ? 
76  OE2 ? B GLU 641 ? B GLU 633  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 75.7  ? 
77  O   ? W HOH .   ? A HOH 906  ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 127.6 ? 
78  O   ? W HOH .   ? A HOH 1252 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 76.8  ? 
79  O   ? X HOH .   ? B HOH 1261 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 150.6 ? 
80  O   ? W HOH .   ? A HOH 1157 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 72.4  ? 
81  O   ? X HOH .   ? B HOH 1271 ? 1_555 CA ? I CA . ? B CA 701 ? 1_555 O   ? X HOH .   ? B HOH 1217 ? 1_555 77.4  ? 
82  OD2 ? C ASP 160 ? C ASP 152  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 OD1 ? C ASN 190 ? C ASN 182  ? 1_555 83.1  ? 
83  OD2 ? C ASP 160 ? C ASP 152  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 OD1 ? C ASN 191 ? C ASN 183  ? 1_555 79.8  ? 
84  OD1 ? C ASN 190 ? C ASN 182  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 OD1 ? C ASN 191 ? C ASN 183  ? 1_555 92.0  ? 
85  OD2 ? C ASP 160 ? C ASP 152  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 893  ? 1_555 75.7  ? 
86  OD1 ? C ASN 190 ? C ASN 182  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 893  ? 1_555 63.3  ? 
87  OD1 ? C ASN 191 ? C ASN 183  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 893  ? 1_555 146.8 ? 
88  OD2 ? C ASP 160 ? C ASP 152  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1212 ? 1_555 165.8 ? 
89  OD1 ? C ASN 190 ? C ASN 182  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1212 ? 1_555 93.1  ? 
90  OD1 ? C ASN 191 ? C ASN 183  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1212 ? 1_555 86.7  ? 
91  O   ? Y HOH .   ? C HOH 893  ? 1_555 CA ? P CA . ? C CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1212 ? 1_555 114.8 ? 
92  O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 OG  ? C SER 398 ? C SER 390  ? 1_555 75.7  ? 
93  O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O1  ? L EDO .   ? C EDO 701  ? 1_555 135.8 ? 
94  OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O1  ? L EDO .   ? C EDO 701  ? 1_555 75.1  ? 
95  O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O2  ? L EDO .   ? C EDO 701  ? 1_555 77.5  ? 
96  OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O2  ? L EDO .   ? C EDO 701  ? 1_555 80.1  ? 
97  O1  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O2  ? L EDO .   ? C EDO 701  ? 1_555 65.3  ? 
98  O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1098 ? 1_555 73.3  ? 
99  OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1098 ? 1_555 108.6 ? 
100 O1  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1098 ? 1_555 148.3 ? 
101 O2  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1098 ? 1_555 146.0 ? 
102 O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1192 ? 1_555 80.1  ? 
103 OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1192 ? 1_555 149.5 ? 
104 O1  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1192 ? 1_555 111.8 ? 
105 O2  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1192 ? 1_555 76.7  ? 
106 O   ? Y HOH .   ? C HOH 1098 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1192 ? 1_555 81.4  ? 
107 O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 146.2 ? 
108 OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 137.0 ? 
109 O1  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 73.1  ? 
110 O2  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 111.0 ? 
111 O   ? Y HOH .   ? C HOH 1098 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 85.4  ? 
112 O   ? Y HOH .   ? C HOH 1192 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 1095 ? 1_555 70.9  ? 
113 O   ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 121.2 ? 
114 OG  ? C SER 398 ? C SER 390  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 68.4  ? 
115 O1  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 76.4  ? 
116 O2  ? L EDO .   ? C EDO 701  ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 135.5 ? 
117 O   ? Y HOH .   ? C HOH 1098 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 76.1  ? 
118 O   ? Y HOH .   ? C HOH 1192 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 141.6 ? 
119 O   ? Y HOH .   ? C HOH 1095 ? 1_555 CA ? N CA . ? C CA 703 ? 1_555 O   ? Y HOH .   ? C HOH 869  ? 1_555 76.6  ? 
120 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 49.2  ? 
121 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1187 ? 1_555 72.3  ? 
122 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1187 ? 1_555 121.4 ? 
123 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 875  ? 1_555 82.9  ? 
124 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 875  ? 1_555 103.7 ? 
125 O   ? Y HOH .   ? C HOH 1187 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 875  ? 1_555 68.3  ? 
126 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 1222 ? 1_555 157.8 ? 
127 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 1222 ? 1_555 152.6 ? 
128 O   ? Y HOH .   ? C HOH 1187 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 1222 ? 1_555 85.5  ? 
129 O   ? Z HOH .   ? D HOH 875  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 1222 ? 1_555 90.2  ? 
130 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1162 ? 1_555 73.7  ? 
131 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1162 ? 1_555 95.2  ? 
132 O   ? Y HOH .   ? C HOH 1187 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1162 ? 1_555 60.3  ? 
133 O   ? Z HOH .   ? D HOH 875  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1162 ? 1_555 127.7 ? 
134 O   ? Z HOH .   ? D HOH 1222 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1162 ? 1_555 94.5  ? 
135 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 101.8 ? 
136 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 77.2  ? 
137 O   ? Y HOH .   ? C HOH 1187 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 116.2 ? 
138 O   ? Z HOH .   ? D HOH 875  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 174.2 ? 
139 O   ? Z HOH .   ? D HOH 1222 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 86.7  ? 
140 O   ? Y HOH .   ? C HOH 1162 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1188 ? 1_555 57.5  ? 
141 OE1 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 126.0 ? 
142 OE2 ? C GLU 641 ? C GLU 633  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 81.2  ? 
143 O   ? Y HOH .   ? C HOH 1187 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 151.8 ? 
144 O   ? Z HOH .   ? D HOH 875  ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 91.2  ? 
145 O   ? Z HOH .   ? D HOH 1222 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 75.0  ? 
146 O   ? Y HOH .   ? C HOH 1162 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 140.2 ? 
147 O   ? Y HOH .   ? C HOH 1188 ? 1_555 CA ? O CA . ? C CA 704 ? 1_555 O   ? Y HOH .   ? C HOH 1199 ? 1_555 83.3  ? 
148 OD2 ? D ASP 160 ? D ASP 152  ? 1_555 CA ? T CA . ? D CA 704 ? 1_555 OD1 ? D ASN 190 ? D ASN 182  ? 1_555 83.8  ? 
149 OD2 ? D ASP 160 ? D ASP 152  ? 1_555 CA ? T CA . ? D CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 924  ? 1_555 84.3  ? 
150 OD1 ? D ASN 190 ? D ASN 182  ? 1_555 CA ? T CA . ? D CA 704 ? 1_555 O   ? Z HOH .   ? D HOH 924  ? 1_555 90.6  ? 
151 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 OG  ? D SER 398 ? D SER 390  ? 1_555 73.8  ? 
152 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O1  ? Q EDO .   ? D EDO 701  ? 1_555 74.7  ? 
153 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O1  ? Q EDO .   ? D EDO 701  ? 1_555 76.7  ? 
154 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O2  ? Q EDO .   ? D EDO 701  ? 1_555 134.3 ? 
155 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O2  ? Q EDO .   ? D EDO 701  ? 1_555 74.3  ? 
156 O1  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O2  ? Q EDO .   ? D EDO 701  ? 1_555 66.7  ? 
157 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1151 ? 1_555 78.9  ? 
158 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1151 ? 1_555 144.3 ? 
159 O1  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1151 ? 1_555 74.2  ? 
160 O2  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1151 ? 1_555 111.5 ? 
161 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1031 ? 1_555 125.7 ? 
162 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1031 ? 1_555 75.1  ? 
163 O1  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1031 ? 1_555 137.2 ? 
164 O2  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1031 ? 1_555 75.1  ? 
165 O   ? Z HOH .   ? D HOH 1151 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1031 ? 1_555 140.4 ? 
166 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 79.8  ? 
167 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 115.1 ? 
168 O1  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 147.5 ? 
169 O2  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 144.2 ? 
170 O   ? Z HOH .   ? D HOH 1151 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 81.4  ? 
171 O   ? Z HOH .   ? D HOH 1031 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? Z HOH .   ? D HOH 1057 ? 1_555 74.6  ? 
172 O   ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 145.5 ? 
173 OG  ? D SER 398 ? D SER 390  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 140.3 ? 
174 O1  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 112.1 ? 
175 O2  ? Q EDO .   ? D EDO 701  ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 74.6  ? 
176 O   ? Z HOH .   ? D HOH 1151 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 71.3  ? 
177 O   ? Z HOH .   ? D HOH 1031 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 73.5  ? 
178 O   ? Z HOH .   ? D HOH 1057 ? 1_555 CA ? V CA . ? D CA 706 ? 1_555 O   ? X HOH .   ? B HOH 1213 ? 2_646 78.9  ? 
179 OE1 ? D GLU 641 ? D GLU 633  ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 OE2 ? D GLU 641 ? D GLU 633  ? 1_555 53.5  ? 
180 OE1 ? D GLU 641 ? D GLU 633  ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1020 ? 1_555 80.5  ? 
181 OE2 ? D GLU 641 ? D GLU 633  ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1020 ? 1_555 133.5 ? 
182 OE1 ? D GLU 641 ? D GLU 633  ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1086 ? 1_555 85.0  ? 
183 OE2 ? D GLU 641 ? D GLU 633  ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1086 ? 1_555 103.3 ? 
184 O   ? Y HOH .   ? C HOH 1020 ? 1_555 CA ? U CA . ? D CA 705 ? 1_555 O   ? Y HOH .   ? C HOH 1086 ? 1_555 76.4  ? 
185 O   ? X HOH .   ? B HOH 1281 ? 1_555 CA ? K CA . ? B CA 703 ? 1_555 O   ? X HOH .   ? B HOH 962  ? 1_555 71.3  ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2017-05-17 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined -6.6770  6.7306   4.5183   0.1527 0.2069 0.1642 -0.0198 -0.0354 0.0269  8.2281 3.2708 2.2983 
-2.1219 -4.2302 0.4929  0.0991  0.0360  -0.1546 -0.0583 0.4287  0.1537  -0.0750 -0.1015 -0.1401 
'X-RAY DIFFRACTION' 2  ? refined -5.5988  -5.2523  8.2386   0.1393 0.2019 0.0976 -0.0319 -0.0399 0.0266  2.0583 1.8026 3.5127 
-1.1159 -2.1618 1.5866  0.0099  0.0347  -0.0461 0.0429  -0.0068 0.1230  -0.0429 0.1371  -0.1652 
'X-RAY DIFFRACTION' 3  ? refined 12.1430  0.3558   5.3860   0.1444 0.1642 0.0720 0.0201  0.0223  0.0115  0.6563 1.1759 0.8389 
0.1306  0.2615  -0.4451 0.0133  -0.0353 0.0234  0.0620  0.0180  -0.0242 -0.1572 0.0396  -0.0292 
'X-RAY DIFFRACTION' 4  ? refined -6.7738  -5.2121  -3.1070  0.3069 0.2791 0.1394 -0.0540 -0.0788 -0.0063 1.8515 0.2638 1.4017 
-0.4772 -0.5186 0.1461  0.1279  -0.0281 -0.0699 0.2748  -0.0182 0.2483  -0.2889 0.0663  -0.1532 
'X-RAY DIFFRACTION' 5  ? refined 19.7190  -17.7374 21.1184  0.1842 0.1190 0.1309 0.0382  0.0167  -0.0025 0.5025 0.6691 1.3945 
0.1358  0.2340  0.0688  0.0614  -0.0033 -0.0579 0.0767  -0.1267 -0.1267 -0.1220 0.3258  0.1311  
'X-RAY DIFFRACTION' 6  ? refined 15.0490  -24.8506 36.2286  0.1348 0.1023 0.1393 -0.0081 -0.0033 0.0180  0.9241 2.3492 1.6558 
0.1474  -0.1244 -0.9866 0.0544  -0.0569 -0.0013 -0.0724 -0.2076 -0.1108 -0.0418 0.2584  0.0116  
'X-RAY DIFFRACTION' 7  ? refined 16.3498  -19.9791 49.1020  0.1624 0.1666 0.1298 -0.0149 0.0050  0.0499  0.7550 1.4902 0.8840 
0.5130  0.0379  0.0077  0.1093  -0.0889 -0.0141 -0.2601 -0.1463 -0.0158 0.2648  0.1482  -0.1203 
'X-RAY DIFFRACTION' 8  ? refined 42.9266  7.7474   35.3621  0.0789 0.1474 0.2142 -0.0007 0.0123  0.0329  0.6474 1.1722 0.6722 
-0.2006 0.2578  -0.1336 -0.0184 -0.0597 0.0642  0.1107  0.1365  -0.2172 -0.0108 -0.0281 0.1527  
'X-RAY DIFFRACTION' 9  ? refined 32.7263  12.7308  22.7336  0.1082 0.1443 0.1622 -0.0037 0.0235  0.0596  0.8548 0.5392 1.2420 
-0.0260 0.1317  -0.0469 -0.0242 -0.0505 0.0480  0.1552  0.1301  -0.1473 -0.0877 -0.0424 0.1346  
'X-RAY DIFFRACTION' 10 ? refined 41.9584  16.4483  37.9039  0.1517 0.1431 0.3499 -0.0535 -0.0125 0.0211  0.6398 1.0763 0.6795 
-0.7628 0.2312  -0.0022 -0.0594 -0.0380 0.0593  0.0837  0.3083  -0.4180 0.0712  -0.1286 0.1255  
'X-RAY DIFFRACTION' 11 ? refined 9.6602   20.7097  36.1317  0.1260 0.1257 0.1716 0.0391  0.0063  -0.0080 0.9854 1.3571 1.1553 
0.0106  0.0190  0.3758  -0.0002 -0.1212 0.0719  -0.0416 0.1966  0.1652  0.0715  -0.2039 -0.1775 
'X-RAY DIFFRACTION' 12 ? refined 9.2952   6.1189   33.6277  0.0985 0.1319 0.0962 0.0149  0.0092  0.0180  1.0403 0.9077 0.3255 
0.6276  0.2675  0.3727  -0.0566 0.0260  0.0345  -0.0194 0.0193  0.0680  -0.0471 -0.0362 -0.0836 
'X-RAY DIFFRACTION' 13 ? refined 2.4773   7.8891   49.1843  0.1184 0.1867 0.1080 0.0366  0.0154  -0.0236 1.3381 1.2566 1.4639 
0.3540  -0.7130 -0.1233 0.0832  -0.0366 -0.0860 -0.2009 0.1605  0.1411  0.1622  -0.2022 -0.1790 
'X-RAY DIFFRACTION' 14 ? refined -3.0061  -2.7420  52.2007  0.1293 0.2700 0.1238 -0.0050 0.0277  0.0278  0.7718 0.7940 0.6881 
-0.0718 -0.1667 0.4540  0.0627  -0.0459 -0.0254 -0.2701 -0.0675 0.0485  0.1408  0.0811  -0.2260 
'X-RAY DIFFRACTION' 15 ? refined -11.1688 -6.0286  38.7109  0.1189 0.2707 0.1613 -0.0468 0.0218  0.0050  0.7683 0.7329 1.8743 
0.0475  -0.9677 -0.2130 0.0978  -0.0209 -0.0907 -0.1749 -0.0495 0.2223  0.0661  0.1193  -0.2992 
'X-RAY DIFFRACTION' 16 ? refined 48.5101  2.5001   68.7259  0.1714 0.2968 0.2180 0.0497  0.0309  -0.0403 4.2269 2.3811 1.7205 
-1.2867 2.6878  -0.9058 0.1184  -0.0724 -0.0490 0.1191  -0.2477 -0.1924 -0.1135 0.2609  0.3204  
'X-RAY DIFFRACTION' 17 ? refined 45.5730  14.1985  72.3258  0.1361 0.1963 0.1409 -0.0097 0.0107  -0.0370 1.4815 1.7886 2.5099 
-0.8292 1.3583  -1.5833 0.0125  -0.0684 0.0622  0.1065  0.0439  -0.2527 0.0955  -0.0711 0.3193  
'X-RAY DIFFRACTION' 18 ? refined 30.6959  14.7286  71.5697  0.1235 0.1395 0.0845 0.0057  0.0197  -0.0227 1.0158 2.4082 1.1477 
-0.0330 -0.0473 -0.4600 0.0888  -0.0392 -0.0475 0.1200  0.0093  -0.0442 -0.0838 -0.0344 0.1229  
'X-RAY DIFFRACTION' 19 ? refined 30.6033  -0.2938  66.5143  0.1599 0.1495 0.1263 0.0316  -0.0132 -0.0394 1.7054 1.0830 1.5233 
0.3978  -0.9310 0.3054  -0.0375 0.0051  0.0483  0.1195  -0.2339 -0.1675 -0.0526 0.2381  0.0885  
'X-RAY DIFFRACTION' 20 ? refined 46.1745  18.8024  60.4284  0.2239 0.3244 0.1503 -0.0444 0.0361  -0.0071 4.6710 3.8477 1.4673 
-3.6896 0.4852  -0.9805 0.1685  -0.2895 0.0907  0.5074  0.3307  -0.4191 -0.2613 -0.0385 0.4157  
'X-RAY DIFFRACTION' 21 ? refined 20.1710  22.6614  86.1857  0.1130 0.0861 0.1108 0.0140  0.0102  -0.0048 0.4834 0.6249 0.8412 
0.1086  -0.0247 -0.0179 0.0669  -0.0219 -0.0386 0.0320  0.1053  0.0944  -0.0281 -0.1273 -0.0717 
'X-RAY DIFFRACTION' 22 ? refined 22.1947  32.3620  103.7673 0.3043 0.1350 0.2148 -0.0697 0.1127  -0.0582 0.5476 1.4034 1.1234 
-0.5356 0.0234  0.7252  0.2057  -0.0434 -0.1181 -0.1550 0.3141  0.0650  0.2661  -0.3296 0.0676  
'X-RAY DIFFRACTION' 23 ? refined 20.4503  22.9202  112.9638 0.2938 0.1839 0.1408 -0.0604 0.0464  -0.0553 0.2607 1.4056 1.1415 
0.1275  0.0765  -0.0389 0.2179  -0.1072 -0.0745 -0.2091 0.1271  0.0374  0.5013  -0.1997 0.0908  
'X-RAY DIFFRACTION' 24 ? refined -1.5722  -7.4314  95.8337  0.1298 0.1326 0.1561 -0.0489 -0.0160 -0.0058 1.3459 2.1689 0.7749 
-0.5098 -0.1277 0.1710  0.0259  -0.0377 0.0072  -0.0169 -0.1375 0.1338  0.0119  0.0605  -0.1475 
'X-RAY DIFFRACTION' 25 ? refined 10.1320  -10.7378 83.6788  0.1679 0.1060 0.1879 -0.0186 -0.0304 -0.0448 1.0649 0.4875 0.9004 
0.2012  -0.1775 0.0989  0.0041  -0.0097 0.0027  0.1431  -0.2355 0.0354  -0.0908 0.0781  -0.0867 
'X-RAY DIFFRACTION' 26 ? refined -13.2887 -2.4256  92.5951  0.1396 0.2257 0.2906 -0.0305 -0.0495 -0.0494 2.0062 3.6885 1.9424 
-0.4731 0.3356  -0.2992 0.0527  -0.0499 0.0068  0.0248  0.0027  0.3742  -0.1662 -0.0493 -0.3277 
'X-RAY DIFFRACTION' 27 ? refined 29.0901  -12.5176 99.5028  0.1901 0.1101 0.2226 0.0164  -0.0387 0.0336  1.1070 0.6278 0.4678 
0.2503  -0.0497 0.1270  0.0373  -0.0272 0.0048  -0.1284 -0.3670 -0.1375 0.0687  0.1915  0.0837  
'X-RAY DIFFRACTION' 28 ? refined 41.5244  -2.5838  114.6455 0.2187 0.2271 0.1826 0.0220  -0.0609 0.0551  2.4026 1.6524 3.3236 
0.3854  2.1383  0.3700  0.0573  -0.0379 -0.0988 -0.2510 -0.2139 -0.2651 0.2656  0.0653  0.2814  
'X-RAY DIFFRACTION' 29 ? refined 44.1424  9.8307   112.0365 0.2474 0.2245 0.1825 -0.0200 -0.0928 -0.0104 0.5476 1.0797 0.8960 
0.0757  0.3769  -0.2803 0.0247  -0.0677 0.0277  -0.1510 0.0567  -0.2046 0.3030  -0.1859 0.2372  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 2   A 40  
;chain 'A' and (resid 2 through 40 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 41  A 96  
;chain 'A' and (resid 41 through 96 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 97  A 241 
;chain 'A' and (resid 97 through 241 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 242 A 314 
;chain 'A' and (resid 242 through 314 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 315 A 474 
;chain 'A' and (resid 315 through 474 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 475 A 554 
;chain 'A' and (resid 475 through 554 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  A 555 A 659 
;chain 'A' and (resid 555 through 659 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B 2   B 96  
;chain 'B' and (resid 2 through 96 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 97  B 254 
;chain 'B' and (resid 97 through 254 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 255 B 333 
;chain 'B' and (resid 255 through 333 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 334 B 421 
;chain 'B' and (resid 334 through 421 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 422 B 474 
;chain 'B' and (resid 422 through 474 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 B 475 B 554 
;chain 'B' and (resid 475 through 554 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 B 555 B 626 
;chain 'B' and (resid 555 through 626 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 B 627 B 659 
;chain 'B' and (resid 627 through 659 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 C 2   C 40  
;chain 'C' and (resid 2 through 40 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 C 41  C 96  
;chain 'C' and (resid 41 through 96 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 C 97  C 157 
;chain 'C' and (resid 97 through 157 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 19 19 C 158 C 273 
;chain 'C' and (resid 158 through 273 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 20 20 C 274 C 314 
;chain 'C' and (resid 274 through 314 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 21 21 C 315 C 505 
;chain 'C' and (resid 315 through 505 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 22 22 C 506 C 554 
;chain 'C' and (resid 506 through 554 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 23 23 C 555 C 659 
;chain 'C' and (resid 555 through 659 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 24 24 D 1   D 96  
;chain 'D' and (resid 1 through 96 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 25 25 D 97  D 254 
;chain 'D' and (resid 97 through 254 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 26 26 D 255 D 293 
;chain 'D' and (resid 255 through 293 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 27 27 D 294 D 505 
;chain 'D' and (resid 294 through 505 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 28 28 D 506 D 554 
;chain 'D' and (resid 506 through 554 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 29 29 D 555 D 659 
;chain 'D' and (resid 555 through 659 )
;
? ? ? ? ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .    1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22 3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   C HOH 890  ? ? O  C HOH 1088 ? ? 2.04 
2 1 O   C HOH 1088 ? ? O  C HOH 1223 ? ? 2.08 
3 1 OD1 A ASP 137  ? ? OH A TYR 315  ? ? 2.14 
4 1 O   D HOH 1164 ? ? O  D HOH 1214 ? ? 2.16 
5 1 OD2 D ASP 396  ? ? O  D HOH 801  ? ? 2.17 
6 1 O   C GLU 332  ? ? O  C HOH 801  ? ? 2.17 
7 1 O   C HOH 1302 ? ? O  C HOH 1307 ? ? 2.17 
8 1 OE2 C GLU 226  ? ? O  C HOH 802  ? ? 2.18 
9 1 ND1 B HIS 258  ? ? O  B HOH 801  ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 64  ? ? -73.42  32.93  
2  1 ASP A 137 ? ? 26.12   66.62  
3  1 ASP A 143 ? ? -164.98 84.96  
4  1 TRP A 193 ? ? -140.84 -5.24  
5  1 LEU A 274 ? ? -67.42  1.06   
6  1 PHE A 281 ? ? 71.98   -0.54  
7  1 ILE A 473 ? ? -128.31 -59.10 
8  1 SER B 21  ? ? -170.89 136.10 
9  1 PHE B 41  ? ? -133.55 -41.43 
10 1 ALA B 64  ? ? -71.08  34.94  
11 1 ASP B 143 ? ? -167.05 91.22  
12 1 TRP B 193 ? ? -151.72 -3.63  
13 1 ILE B 473 ? ? -129.56 -60.23 
14 1 PHE C 41  ? ? -132.45 -41.06 
15 1 ALA C 64  ? ? -78.92  31.28  
16 1 ASP C 143 ? ? -165.57 87.16  
17 1 ASN C 182 ? ? -97.10  36.87  
18 1 TRP C 193 ? ? -151.43 -2.94  
19 1 ILE C 473 ? ? -127.65 -60.70 
20 1 ALA D 64  ? ? -75.65  35.31  
21 1 ASP D 143 ? ? -164.72 92.19  
22 1 TRP D 193 ? ? -141.40 -3.37  
23 1 ILE D 473 ? ? -127.68 -61.29 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLN 17  ? CG  ? A GLN 25  CG  
2   1 Y 1 A GLN 17  ? CD  ? A GLN 25  CD  
3   1 Y 1 A GLN 17  ? OE1 ? A GLN 25  OE1 
4   1 Y 1 A GLN 17  ? NE2 ? A GLN 25  NE2 
5   1 Y 1 A HIS 23  ? CG  ? A HIS 31  CG  
6   1 Y 1 A HIS 23  ? ND1 ? A HIS 31  ND1 
7   1 Y 1 A HIS 23  ? CD2 ? A HIS 31  CD2 
8   1 Y 1 A HIS 23  ? CE1 ? A HIS 31  CE1 
9   1 Y 1 A HIS 23  ? NE2 ? A HIS 31  NE2 
10  1 Y 1 A ILE 184 ? CG1 ? A ILE 192 CG1 
11  1 Y 1 A ILE 184 ? CG2 ? A ILE 192 CG2 
12  1 Y 1 A ILE 184 ? CD1 ? A ILE 192 CD1 
13  1 Y 1 A GLU 226 ? CG  ? A GLU 234 CG  
14  1 Y 1 A GLU 226 ? CD  ? A GLU 234 CD  
15  1 Y 1 A GLU 226 ? OE1 ? A GLU 234 OE1 
16  1 Y 1 A GLU 226 ? OE2 ? A GLU 234 OE2 
17  1 Y 1 A GLU 268 ? CG  ? A GLU 276 CG  
18  1 Y 1 A GLU 268 ? CD  ? A GLU 276 CD  
19  1 Y 1 A GLU 268 ? OE1 ? A GLU 276 OE1 
20  1 Y 1 A GLU 268 ? OE2 ? A GLU 276 OE2 
21  1 Y 1 A THR 270 ? OG1 ? A THR 278 OG1 
22  1 Y 1 A THR 270 ? CG2 ? A THR 278 CG2 
23  1 Y 1 A LYS 272 ? CG  ? A LYS 280 CG  
24  1 Y 1 A LYS 272 ? CD  ? A LYS 280 CD  
25  1 Y 1 A LYS 272 ? CE  ? A LYS 280 CE  
26  1 Y 1 A LYS 272 ? NZ  ? A LYS 280 NZ  
27  1 Y 1 A HIS 273 ? CG  ? A HIS 281 CG  
28  1 Y 1 A HIS 273 ? ND1 ? A HIS 281 ND1 
29  1 Y 1 A HIS 273 ? CD2 ? A HIS 281 CD2 
30  1 Y 1 A HIS 273 ? CE1 ? A HIS 281 CE1 
31  1 Y 1 A HIS 273 ? NE2 ? A HIS 281 NE2 
32  1 Y 1 A GLU 282 ? CG  ? A GLU 290 CG  
33  1 Y 1 A GLU 282 ? CD  ? A GLU 290 CD  
34  1 Y 1 A GLU 282 ? OE1 ? A GLU 290 OE1 
35  1 Y 1 A GLU 282 ? OE2 ? A GLU 290 OE2 
36  1 Y 1 A GLU 286 ? CG  ? A GLU 294 CG  
37  1 Y 1 A GLU 286 ? CD  ? A GLU 294 CD  
38  1 Y 1 A GLU 286 ? OE1 ? A GLU 294 OE1 
39  1 Y 1 A GLU 286 ? OE2 ? A GLU 294 OE2 
40  1 Y 1 A LYS 299 ? CG  ? A LYS 307 CG  
41  1 Y 1 A LYS 299 ? CD  ? A LYS 307 CD  
42  1 Y 1 A LYS 299 ? CE  ? A LYS 307 CE  
43  1 Y 1 A LYS 299 ? NZ  ? A LYS 307 NZ  
44  1 Y 1 A GLN 312 ? CG  ? A GLN 320 CG  
45  1 Y 1 A GLN 312 ? CD  ? A GLN 320 CD  
46  1 Y 1 A GLN 312 ? OE1 ? A GLN 320 OE1 
47  1 Y 1 A GLN 312 ? NE2 ? A GLN 320 NE2 
48  1 Y 1 A LYS 314 ? CG  ? A LYS 322 CG  
49  1 Y 1 A LYS 314 ? CD  ? A LYS 322 CD  
50  1 Y 1 A LYS 314 ? CE  ? A LYS 322 CE  
51  1 Y 1 A LYS 314 ? NZ  ? A LYS 322 NZ  
52  1 Y 1 A GLU 332 ? CG  ? A GLU 340 CG  
53  1 Y 1 A GLU 332 ? CD  ? A GLU 340 CD  
54  1 Y 1 A GLU 332 ? OE1 ? A GLU 340 OE1 
55  1 Y 1 A GLU 332 ? OE2 ? A GLU 340 OE2 
56  1 Y 1 A GLU 336 ? CG  ? A GLU 344 CG  
57  1 Y 1 A GLU 336 ? CD  ? A GLU 344 CD  
58  1 Y 1 A GLU 336 ? OE1 ? A GLU 344 OE1 
59  1 Y 1 A GLU 336 ? OE2 ? A GLU 344 OE2 
60  1 Y 1 A GLN 339 ? CG  ? A GLN 347 CG  
61  1 Y 1 A GLN 339 ? CD  ? A GLN 347 CD  
62  1 Y 1 A GLN 339 ? OE1 ? A GLN 347 OE1 
63  1 Y 1 A GLN 339 ? NE2 ? A GLN 347 NE2 
64  1 Y 1 A LYS 343 ? CG  ? A LYS 351 CG  
65  1 Y 1 A LYS 343 ? CD  ? A LYS 351 CD  
66  1 Y 1 A LYS 343 ? CE  ? A LYS 351 CE  
67  1 Y 1 A LYS 343 ? NZ  ? A LYS 351 NZ  
68  1 Y 1 A GLU 344 ? CG  ? A GLU 352 CG  
69  1 Y 1 A GLU 344 ? CD  ? A GLU 352 CD  
70  1 Y 1 A GLU 344 ? OE1 ? A GLU 352 OE1 
71  1 Y 1 A GLU 344 ? OE2 ? A GLU 352 OE2 
72  1 Y 1 A LYS 348 ? CG  ? A LYS 356 CG  
73  1 Y 1 A LYS 348 ? CD  ? A LYS 356 CD  
74  1 Y 1 A LYS 348 ? CE  ? A LYS 356 CE  
75  1 Y 1 A LYS 348 ? NZ  ? A LYS 356 NZ  
76  1 Y 1 A LYS 397 ? CG  ? A LYS 405 CG  
77  1 Y 1 A LYS 397 ? CD  ? A LYS 405 CD  
78  1 Y 1 A LYS 397 ? CE  ? A LYS 405 CE  
79  1 Y 1 A LYS 397 ? NZ  ? A LYS 405 NZ  
80  1 Y 1 A LYS 521 ? CG  ? A LYS 529 CG  
81  1 Y 1 A LYS 521 ? CD  ? A LYS 529 CD  
82  1 Y 1 A LYS 521 ? CE  ? A LYS 529 CE  
83  1 Y 1 A LYS 521 ? NZ  ? A LYS 529 NZ  
84  1 Y 1 A GLN 544 ? CG  ? A GLN 552 CG  
85  1 Y 1 A GLN 544 ? CD  ? A GLN 552 CD  
86  1 Y 1 A GLN 544 ? OE1 ? A GLN 552 OE1 
87  1 Y 1 A GLN 544 ? NE2 ? A GLN 552 NE2 
88  1 Y 1 A GLU 563 ? CG  ? A GLU 571 CG  
89  1 Y 1 A GLU 563 ? CD  ? A GLU 571 CD  
90  1 Y 1 A GLU 563 ? OE1 ? A GLU 571 OE1 
91  1 Y 1 A GLU 563 ? OE2 ? A GLU 571 OE2 
92  1 Y 1 A LYS 566 ? CG  ? A LYS 574 CG  
93  1 Y 1 A LYS 566 ? CD  ? A LYS 574 CD  
94  1 Y 1 A LYS 566 ? CE  ? A LYS 574 CE  
95  1 Y 1 A LYS 566 ? NZ  ? A LYS 574 NZ  
96  1 Y 1 A GLU 600 ? CG  ? A GLU 608 CG  
97  1 Y 1 A GLU 600 ? CD  ? A GLU 608 CD  
98  1 Y 1 A GLU 600 ? OE1 ? A GLU 608 OE1 
99  1 Y 1 A GLU 600 ? OE2 ? A GLU 608 OE2 
100 1 Y 1 A LYS 642 ? CG  ? A LYS 650 CG  
101 1 Y 1 A LYS 642 ? CD  ? A LYS 650 CD  
102 1 Y 1 A LYS 642 ? CE  ? A LYS 650 CE  
103 1 Y 1 A LYS 642 ? NZ  ? A LYS 650 NZ  
104 1 Y 1 B ASP 137 ? CG  ? B ASP 145 CG  
105 1 Y 1 B ASP 137 ? OD1 ? B ASP 145 OD1 
106 1 Y 1 B ASP 137 ? OD2 ? B ASP 145 OD2 
107 1 Y 1 B LYS 189 ? CG  ? B LYS 197 CG  
108 1 Y 1 B LYS 189 ? CD  ? B LYS 197 CD  
109 1 Y 1 B LYS 189 ? CE  ? B LYS 197 CE  
110 1 Y 1 B LYS 189 ? NZ  ? B LYS 197 NZ  
111 1 Y 1 B LYS 256 ? CG  ? B LYS 264 CG  
112 1 Y 1 B LYS 256 ? CD  ? B LYS 264 CD  
113 1 Y 1 B LYS 256 ? CE  ? B LYS 264 CE  
114 1 Y 1 B LYS 256 ? NZ  ? B LYS 264 NZ  
115 1 Y 1 B LYS 296 ? CG  ? B LYS 304 CG  
116 1 Y 1 B LYS 296 ? CD  ? B LYS 304 CD  
117 1 Y 1 B LYS 296 ? CE  ? B LYS 304 CE  
118 1 Y 1 B LYS 296 ? NZ  ? B LYS 304 NZ  
119 1 Y 1 B LYS 314 ? CG  ? B LYS 322 CG  
120 1 Y 1 B LYS 314 ? CD  ? B LYS 322 CD  
121 1 Y 1 B LYS 314 ? CE  ? B LYS 322 CE  
122 1 Y 1 B LYS 314 ? NZ  ? B LYS 322 NZ  
123 1 Y 1 B GLU 332 ? CG  ? B GLU 340 CG  
124 1 Y 1 B GLU 332 ? CD  ? B GLU 340 CD  
125 1 Y 1 B GLU 332 ? OE1 ? B GLU 340 OE1 
126 1 Y 1 B GLU 332 ? OE2 ? B GLU 340 OE2 
127 1 Y 1 B GLU 336 ? CG  ? B GLU 344 CG  
128 1 Y 1 B GLU 336 ? CD  ? B GLU 344 CD  
129 1 Y 1 B GLU 336 ? OE1 ? B GLU 344 OE1 
130 1 Y 1 B GLU 336 ? OE2 ? B GLU 344 OE2 
131 1 Y 1 B GLN 339 ? CG  ? B GLN 347 CG  
132 1 Y 1 B GLN 339 ? CD  ? B GLN 347 CD  
133 1 Y 1 B GLN 339 ? OE1 ? B GLN 347 OE1 
134 1 Y 1 B GLN 339 ? NE2 ? B GLN 347 NE2 
135 1 Y 1 B LYS 343 ? CG  ? B LYS 351 CG  
136 1 Y 1 B LYS 343 ? CD  ? B LYS 351 CD  
137 1 Y 1 B LYS 343 ? CE  ? B LYS 351 CE  
138 1 Y 1 B LYS 343 ? NZ  ? B LYS 351 NZ  
139 1 Y 1 B LYS 348 ? CG  ? B LYS 356 CG  
140 1 Y 1 B LYS 348 ? CD  ? B LYS 356 CD  
141 1 Y 1 B LYS 348 ? CE  ? B LYS 356 CE  
142 1 Y 1 B LYS 348 ? NZ  ? B LYS 356 NZ  
143 1 Y 1 B GLN 359 ? CG  ? B GLN 367 CG  
144 1 Y 1 B GLN 359 ? CD  ? B GLN 367 CD  
145 1 Y 1 B GLN 359 ? OE1 ? B GLN 367 OE1 
146 1 Y 1 B GLN 359 ? NE2 ? B GLN 367 NE2 
147 1 Y 1 B LYS 397 ? CG  ? B LYS 405 CG  
148 1 Y 1 B LYS 397 ? CD  ? B LYS 405 CD  
149 1 Y 1 B LYS 397 ? CE  ? B LYS 405 CE  
150 1 Y 1 B LYS 397 ? NZ  ? B LYS 405 NZ  
151 1 Y 1 B ARG 517 ? CG  ? B ARG 525 CG  
152 1 Y 1 B ARG 517 ? CD  ? B ARG 525 CD  
153 1 Y 1 B ARG 517 ? NE  ? B ARG 525 NE  
154 1 Y 1 B ARG 517 ? CZ  ? B ARG 525 CZ  
155 1 Y 1 B ARG 517 ? NH1 ? B ARG 525 NH1 
156 1 Y 1 B ARG 517 ? NH2 ? B ARG 525 NH2 
157 1 Y 1 B GLN 518 ? CG  ? B GLN 526 CG  
158 1 Y 1 B GLN 518 ? CD  ? B GLN 526 CD  
159 1 Y 1 B GLN 518 ? OE1 ? B GLN 526 OE1 
160 1 Y 1 B GLN 518 ? NE2 ? B GLN 526 NE2 
161 1 Y 1 B ASN 519 ? CG  ? B ASN 527 CG  
162 1 Y 1 B ASN 519 ? OD1 ? B ASN 527 OD1 
163 1 Y 1 B ASN 519 ? ND2 ? B ASN 527 ND2 
164 1 Y 1 B PHE 522 ? CG  ? B PHE 530 CG  
165 1 Y 1 B PHE 522 ? CD1 ? B PHE 530 CD1 
166 1 Y 1 B PHE 522 ? CD2 ? B PHE 530 CD2 
167 1 Y 1 B PHE 522 ? CE1 ? B PHE 530 CE1 
168 1 Y 1 B PHE 522 ? CE2 ? B PHE 530 CE2 
169 1 Y 1 B PHE 522 ? CZ  ? B PHE 530 CZ  
170 1 Y 1 B GLN 523 ? CG  ? B GLN 531 CG  
171 1 Y 1 B GLN 523 ? CD  ? B GLN 531 CD  
172 1 Y 1 B GLN 523 ? OE1 ? B GLN 531 OE1 
173 1 Y 1 B GLN 523 ? NE2 ? B GLN 531 NE2 
174 1 Y 1 B GLN 544 ? CG  ? B GLN 552 CG  
175 1 Y 1 B GLN 544 ? CD  ? B GLN 552 CD  
176 1 Y 1 B GLN 544 ? OE1 ? B GLN 552 OE1 
177 1 Y 1 B GLN 544 ? NE2 ? B GLN 552 NE2 
178 1 Y 1 B ASN 546 ? CG  ? B ASN 554 CG  
179 1 Y 1 B ASN 546 ? OD1 ? B ASN 554 OD1 
180 1 Y 1 B ASN 546 ? ND2 ? B ASN 554 ND2 
181 1 Y 1 B GLU 600 ? CG  ? B GLU 608 CG  
182 1 Y 1 B GLU 600 ? CD  ? B GLU 608 CD  
183 1 Y 1 B GLU 600 ? OE1 ? B GLU 608 OE1 
184 1 Y 1 B GLU 600 ? OE2 ? B GLU 608 OE2 
185 1 Y 1 C GLN 3   ? CG  ? C GLN 11  CG  
186 1 Y 1 C GLN 3   ? CD  ? C GLN 11  CD  
187 1 Y 1 C GLN 3   ? OE1 ? C GLN 11  OE1 
188 1 Y 1 C GLN 3   ? NE2 ? C GLN 11  NE2 
189 1 Y 1 C TYR 102 ? CG  ? C TYR 110 CG  
190 1 Y 1 C TYR 102 ? CD1 ? C TYR 110 CD1 
191 1 Y 1 C TYR 102 ? CD2 ? C TYR 110 CD2 
192 1 Y 1 C TYR 102 ? CE1 ? C TYR 110 CE1 
193 1 Y 1 C TYR 102 ? CE2 ? C TYR 110 CE2 
194 1 Y 1 C TYR 102 ? CZ  ? C TYR 110 CZ  
195 1 Y 1 C TYR 102 ? OH  ? C TYR 110 OH  
196 1 Y 1 C ASP 191 ? CG  ? C ASP 199 CG  
197 1 Y 1 C ASP 191 ? OD1 ? C ASP 199 OD1 
198 1 Y 1 C ASP 191 ? OD2 ? C ASP 199 OD2 
199 1 Y 1 C LEU 243 ? CG  ? C LEU 251 CG  
200 1 Y 1 C LEU 243 ? CD1 ? C LEU 251 CD1 
201 1 Y 1 C LEU 243 ? CD2 ? C LEU 251 CD2 
202 1 Y 1 C GLU 268 ? CG  ? C GLU 276 CG  
203 1 Y 1 C GLU 268 ? CD  ? C GLU 276 CD  
204 1 Y 1 C GLU 268 ? OE1 ? C GLU 276 OE1 
205 1 Y 1 C GLU 268 ? OE2 ? C GLU 276 OE2 
206 1 Y 1 C LYS 272 ? CG  ? C LYS 280 CG  
207 1 Y 1 C LYS 272 ? CD  ? C LYS 280 CD  
208 1 Y 1 C LYS 272 ? CE  ? C LYS 280 CE  
209 1 Y 1 C LYS 272 ? NZ  ? C LYS 280 NZ  
210 1 Y 1 C HIS 273 ? CG  ? C HIS 281 CG  
211 1 Y 1 C HIS 273 ? ND1 ? C HIS 281 ND1 
212 1 Y 1 C HIS 273 ? CD2 ? C HIS 281 CD2 
213 1 Y 1 C HIS 273 ? CE1 ? C HIS 281 CE1 
214 1 Y 1 C HIS 273 ? NE2 ? C HIS 281 NE2 
215 1 Y 1 C GLU 282 ? CG  ? C GLU 290 CG  
216 1 Y 1 C GLU 282 ? CD  ? C GLU 290 CD  
217 1 Y 1 C GLU 282 ? OE1 ? C GLU 290 OE1 
218 1 Y 1 C GLU 282 ? OE2 ? C GLU 290 OE2 
219 1 Y 1 C GLU 286 ? CG  ? C GLU 294 CG  
220 1 Y 1 C GLU 286 ? CD  ? C GLU 294 CD  
221 1 Y 1 C GLU 286 ? OE1 ? C GLU 294 OE1 
222 1 Y 1 C GLU 286 ? OE2 ? C GLU 294 OE2 
223 1 Y 1 C LYS 294 ? CG  ? C LYS 302 CG  
224 1 Y 1 C LYS 294 ? CD  ? C LYS 302 CD  
225 1 Y 1 C LYS 294 ? CE  ? C LYS 302 CE  
226 1 Y 1 C LYS 294 ? NZ  ? C LYS 302 NZ  
227 1 Y 1 C LYS 296 ? CG  ? C LYS 304 CG  
228 1 Y 1 C LYS 296 ? CD  ? C LYS 304 CD  
229 1 Y 1 C LYS 296 ? CE  ? C LYS 304 CE  
230 1 Y 1 C LYS 296 ? NZ  ? C LYS 304 NZ  
231 1 Y 1 C LYS 299 ? CG  ? C LYS 307 CG  
232 1 Y 1 C LYS 299 ? CD  ? C LYS 307 CD  
233 1 Y 1 C LYS 299 ? CE  ? C LYS 307 CE  
234 1 Y 1 C LYS 299 ? NZ  ? C LYS 307 NZ  
235 1 Y 1 C GLN 312 ? CG  ? C GLN 320 CG  
236 1 Y 1 C GLN 312 ? CD  ? C GLN 320 CD  
237 1 Y 1 C GLN 312 ? OE1 ? C GLN 320 OE1 
238 1 Y 1 C GLN 312 ? NE2 ? C GLN 320 NE2 
239 1 Y 1 C LYS 314 ? CG  ? C LYS 322 CG  
240 1 Y 1 C LYS 314 ? CD  ? C LYS 322 CD  
241 1 Y 1 C LYS 314 ? CE  ? C LYS 322 CE  
242 1 Y 1 C LYS 314 ? NZ  ? C LYS 322 NZ  
243 1 Y 1 C GLU 332 ? CG  ? C GLU 340 CG  
244 1 Y 1 C GLU 332 ? CD  ? C GLU 340 CD  
245 1 Y 1 C GLU 332 ? OE1 ? C GLU 340 OE1 
246 1 Y 1 C GLU 332 ? OE2 ? C GLU 340 OE2 
247 1 Y 1 C GLN 339 ? CG  ? C GLN 347 CG  
248 1 Y 1 C GLN 339 ? CD  ? C GLN 347 CD  
249 1 Y 1 C GLN 339 ? OE1 ? C GLN 347 OE1 
250 1 Y 1 C GLN 339 ? NE2 ? C GLN 347 NE2 
251 1 Y 1 C GLU 344 ? CG  ? C GLU 352 CG  
252 1 Y 1 C GLU 344 ? CD  ? C GLU 352 CD  
253 1 Y 1 C GLU 344 ? OE1 ? C GLU 352 OE1 
254 1 Y 1 C GLU 344 ? OE2 ? C GLU 352 OE2 
255 1 Y 1 C LYS 348 ? CG  ? C LYS 356 CG  
256 1 Y 1 C LYS 348 ? CD  ? C LYS 356 CD  
257 1 Y 1 C LYS 348 ? CE  ? C LYS 356 CE  
258 1 Y 1 C LYS 348 ? NZ  ? C LYS 356 NZ  
259 1 Y 1 C ARG 517 ? CG  ? C ARG 525 CG  
260 1 Y 1 C ARG 517 ? CD  ? C ARG 525 CD  
261 1 Y 1 C ARG 517 ? NE  ? C ARG 525 NE  
262 1 Y 1 C ARG 517 ? CZ  ? C ARG 525 CZ  
263 1 Y 1 C ARG 517 ? NH1 ? C ARG 525 NH1 
264 1 Y 1 C ARG 517 ? NH2 ? C ARG 525 NH2 
265 1 Y 1 C GLN 544 ? CG  ? C GLN 552 CG  
266 1 Y 1 C GLN 544 ? CD  ? C GLN 552 CD  
267 1 Y 1 C GLN 544 ? OE1 ? C GLN 552 OE1 
268 1 Y 1 C GLN 544 ? NE2 ? C GLN 552 NE2 
269 1 Y 1 C ASN 546 ? CG  ? C ASN 554 CG  
270 1 Y 1 C ASN 546 ? OD1 ? C ASN 554 OD1 
271 1 Y 1 C ASN 546 ? ND2 ? C ASN 554 ND2 
272 1 Y 1 C GLU 563 ? CG  ? C GLU 571 CG  
273 1 Y 1 C GLU 563 ? CD  ? C GLU 571 CD  
274 1 Y 1 C GLU 563 ? OE1 ? C GLU 571 OE1 
275 1 Y 1 C GLU 563 ? OE2 ? C GLU 571 OE2 
276 1 Y 1 C LYS 566 ? CG  ? C LYS 574 CG  
277 1 Y 1 C LYS 566 ? CD  ? C LYS 574 CD  
278 1 Y 1 C LYS 566 ? CE  ? C LYS 574 CE  
279 1 Y 1 C LYS 566 ? NZ  ? C LYS 574 NZ  
280 1 Y 1 C GLU 600 ? CG  ? C GLU 608 CG  
281 1 Y 1 C GLU 600 ? CD  ? C GLU 608 CD  
282 1 Y 1 C GLU 600 ? OE1 ? C GLU 608 OE1 
283 1 Y 1 C GLU 600 ? OE2 ? C GLU 608 OE2 
284 1 Y 1 C LYS 642 ? CG  ? C LYS 650 CG  
285 1 Y 1 C LYS 642 ? CD  ? C LYS 650 CD  
286 1 Y 1 C LYS 642 ? CE  ? C LYS 650 CE  
287 1 Y 1 C LYS 642 ? NZ  ? C LYS 650 NZ  
288 1 Y 1 C ASP 653 ? CG  ? C ASP 661 CG  
289 1 Y 1 C ASP 653 ? OD1 ? C ASP 661 OD1 
290 1 Y 1 C ASP 653 ? OD2 ? C ASP 661 OD2 
291 1 Y 1 D TYR 102 ? CG  ? D TYR 110 CG  
292 1 Y 1 D TYR 102 ? CD1 ? D TYR 110 CD1 
293 1 Y 1 D TYR 102 ? CD2 ? D TYR 110 CD2 
294 1 Y 1 D TYR 102 ? CE1 ? D TYR 110 CE1 
295 1 Y 1 D TYR 102 ? CE2 ? D TYR 110 CE2 
296 1 Y 1 D TYR 102 ? CZ  ? D TYR 110 CZ  
297 1 Y 1 D TYR 102 ? OH  ? D TYR 110 OH  
298 1 Y 1 D ASP 137 ? CG  ? D ASP 145 CG  
299 1 Y 1 D ASP 137 ? OD1 ? D ASP 145 OD1 
300 1 Y 1 D ASP 137 ? OD2 ? D ASP 145 OD2 
301 1 Y 1 D ASP 191 ? CG  ? D ASP 199 CG  
302 1 Y 1 D ASP 191 ? OD1 ? D ASP 199 OD1 
303 1 Y 1 D ASP 191 ? OD2 ? D ASP 199 OD2 
304 1 Y 1 D GLU 332 ? CG  ? D GLU 340 CG  
305 1 Y 1 D GLU 332 ? CD  ? D GLU 340 CD  
306 1 Y 1 D GLU 332 ? OE1 ? D GLU 340 OE1 
307 1 Y 1 D GLU 332 ? OE2 ? D GLU 340 OE2 
308 1 Y 1 D GLU 336 ? CG  ? D GLU 344 CG  
309 1 Y 1 D GLU 336 ? CD  ? D GLU 344 CD  
310 1 Y 1 D GLU 336 ? OE1 ? D GLU 344 OE1 
311 1 Y 1 D GLU 336 ? OE2 ? D GLU 344 OE2 
312 1 Y 1 D GLN 339 ? CG  ? D GLN 347 CG  
313 1 Y 1 D GLN 339 ? CD  ? D GLN 347 CD  
314 1 Y 1 D GLN 339 ? OE1 ? D GLN 347 OE1 
315 1 Y 1 D GLN 339 ? NE2 ? D GLN 347 NE2 
316 1 Y 1 D LYS 343 ? CG  ? D LYS 351 CG  
317 1 Y 1 D LYS 343 ? CD  ? D LYS 351 CD  
318 1 Y 1 D LYS 343 ? CE  ? D LYS 351 CE  
319 1 Y 1 D LYS 343 ? NZ  ? D LYS 351 NZ  
320 1 Y 1 D GLU 344 ? CG  ? D GLU 352 CG  
321 1 Y 1 D GLU 344 ? CD  ? D GLU 352 CD  
322 1 Y 1 D GLU 344 ? OE1 ? D GLU 352 OE1 
323 1 Y 1 D GLU 344 ? OE2 ? D GLU 352 OE2 
324 1 Y 1 D LYS 348 ? CG  ? D LYS 356 CG  
325 1 Y 1 D LYS 348 ? CD  ? D LYS 356 CD  
326 1 Y 1 D LYS 348 ? CE  ? D LYS 356 CE  
327 1 Y 1 D LYS 348 ? NZ  ? D LYS 356 NZ  
328 1 Y 1 D LYS 367 ? CG  ? D LYS 375 CG  
329 1 Y 1 D LYS 367 ? CD  ? D LYS 375 CD  
330 1 Y 1 D LYS 367 ? CE  ? D LYS 375 CE  
331 1 Y 1 D LYS 367 ? NZ  ? D LYS 375 NZ  
332 1 Y 1 D LYS 397 ? CG  ? D LYS 405 CG  
333 1 Y 1 D LYS 397 ? CD  ? D LYS 405 CD  
334 1 Y 1 D LYS 397 ? CE  ? D LYS 405 CE  
335 1 Y 1 D LYS 397 ? NZ  ? D LYS 405 NZ  
336 1 Y 1 D ARG 517 ? CG  ? D ARG 525 CG  
337 1 Y 1 D ARG 517 ? CD  ? D ARG 525 CD  
338 1 Y 1 D ARG 517 ? NE  ? D ARG 525 NE  
339 1 Y 1 D ARG 517 ? CZ  ? D ARG 525 CZ  
340 1 Y 1 D ARG 517 ? NH1 ? D ARG 525 NH1 
341 1 Y 1 D ARG 517 ? NH2 ? D ARG 525 NH2 
342 1 Y 1 D GLN 518 ? CG  ? D GLN 526 CG  
343 1 Y 1 D GLN 518 ? CD  ? D GLN 526 CD  
344 1 Y 1 D GLN 518 ? OE1 ? D GLN 526 OE1 
345 1 Y 1 D GLN 518 ? NE2 ? D GLN 526 NE2 
346 1 Y 1 D ASN 519 ? CG  ? D ASN 527 CG  
347 1 Y 1 D ASN 519 ? OD1 ? D ASN 527 OD1 
348 1 Y 1 D ASN 519 ? ND2 ? D ASN 527 ND2 
349 1 Y 1 D LYS 521 ? CG  ? D LYS 529 CG  
350 1 Y 1 D LYS 521 ? CD  ? D LYS 529 CD  
351 1 Y 1 D LYS 521 ? CE  ? D LYS 529 CE  
352 1 Y 1 D LYS 521 ? NZ  ? D LYS 529 NZ  
353 1 Y 1 D GLN 523 ? CG  ? D GLN 531 CG  
354 1 Y 1 D GLN 523 ? CD  ? D GLN 531 CD  
355 1 Y 1 D GLN 523 ? OE1 ? D GLN 531 OE1 
356 1 Y 1 D GLN 523 ? NE2 ? D GLN 531 NE2 
357 1 Y 1 D GLU 527 ? CG  ? D GLU 535 CG  
358 1 Y 1 D GLU 527 ? CD  ? D GLU 535 CD  
359 1 Y 1 D GLU 527 ? OE1 ? D GLU 535 OE1 
360 1 Y 1 D GLU 527 ? OE2 ? D GLU 535 OE2 
361 1 Y 1 D GLN 544 ? CG  ? D GLN 552 CG  
362 1 Y 1 D GLN 544 ? CD  ? D GLN 552 CD  
363 1 Y 1 D GLN 544 ? OE1 ? D GLN 552 OE1 
364 1 Y 1 D GLN 544 ? NE2 ? D GLN 552 NE2 
365 1 Y 1 D ASN 546 ? CG  ? D ASN 554 CG  
366 1 Y 1 D ASN 546 ? OD1 ? D ASN 554 OD1 
367 1 Y 1 D ASN 546 ? ND2 ? D ASN 554 ND2 
368 1 Y 1 D GLU 563 ? CG  ? D GLU 571 CG  
369 1 Y 1 D GLU 563 ? CD  ? D GLU 571 CD  
370 1 Y 1 D GLU 563 ? OE1 ? D GLU 571 OE1 
371 1 Y 1 D GLU 563 ? OE2 ? D GLU 571 OE2 
372 1 Y 1 D GLU 600 ? CG  ? D GLU 608 CG  
373 1 Y 1 D GLU 600 ? CD  ? D GLU 608 CD  
374 1 Y 1 D GLU 600 ? OE1 ? D GLU 608 OE1 
375 1 Y 1 D GLU 600 ? OE2 ? D GLU 608 OE2 
376 1 Y 1 D ASP 638 ? CG  ? D ASP 646 CG  
377 1 Y 1 D ASP 638 ? OD1 ? D ASP 646 OD1 
378 1 Y 1 D ASP 638 ? OD2 ? D ASP 646 OD2 
379 1 Y 1 D LYS 642 ? CG  ? D LYS 650 CG  
380 1 Y 1 D LYS 642 ? CD  ? D LYS 650 CD  
381 1 Y 1 D LYS 642 ? CE  ? D LYS 650 CE  
382 1 Y 1 D LYS 642 ? NZ  ? D LYS 650 NZ  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -7  ? A MET 1   
2   1 Y 1 A ALA -6  ? A ALA 2   
3   1 Y 1 A HIS -5  ? A HIS 3   
4   1 Y 1 A HIS -4  ? A HIS 4   
5   1 Y 1 A HIS -3  ? A HIS 5   
6   1 Y 1 A HIS -2  ? A HIS 6   
7   1 Y 1 A HIS -1  ? A HIS 7   
8   1 Y 1 A HIS 0   ? A HIS 8   
9   1 Y 1 A MET 1   ? A MET 9   
10  1 Y 1 A SER 185 ? A SER 193 
11  1 Y 1 A ILE 186 ? A ILE 194 
12  1 Y 1 A ASP 187 ? A ASP 195 
13  1 Y 1 A GLY 188 ? A GLY 196 
14  1 Y 1 A LYS 189 ? A LYS 197 
15  1 Y 1 A VAL 190 ? A VAL 198 
16  1 Y 1 A ASP 191 ? A ASP 199 
17  1 Y 1 A ILE 244 ? A ILE 252 
18  1 Y 1 A GLY 245 ? A GLY 253 
19  1 Y 1 A LYS 246 ? A LYS 254 
20  1 Y 1 A GLY 247 ? A GLY 255 
21  1 Y 1 A SER 248 ? A SER 256 
22  1 Y 1 A ALA 249 ? A ALA 257 
23  1 Y 1 A ASN 250 ? A ASN 258 
24  1 Y 1 A LYS 251 ? A LYS 259 
25  1 Y 1 A GLU 252 ? A GLU 260 
26  1 Y 1 A GLY 253 ? A GLY 261 
27  1 Y 1 A SER 254 ? A SER 262 
28  1 Y 1 A HIS 255 ? A HIS 263 
29  1 Y 1 A LYS 256 ? A LYS 264 
30  1 Y 1 A THR 257 ? A THR 265 
31  1 Y 1 A HIS 258 ? A HIS 266 
32  1 Y 1 A GLY 259 ? A GLY 267 
33  1 Y 1 A ALA 260 ? A ALA 268 
34  1 Y 1 A PRO 261 ? A PRO 269 
35  1 Y 1 A LEU 262 ? A LEU 270 
36  1 Y 1 A GLY 263 ? A GLY 271 
37  1 Y 1 A ALA 264 ? A ALA 272 
38  1 Y 1 A ASP 265 ? A ASP 273 
39  1 Y 1 A GLU 266 ? A GLU 274 
40  1 Y 1 A ILE 267 ? A ILE 275 
41  1 Y 1 B MET -7  ? B MET 1   
42  1 Y 1 B ALA -6  ? B ALA 2   
43  1 Y 1 B HIS -5  ? B HIS 3   
44  1 Y 1 B HIS -4  ? B HIS 4   
45  1 Y 1 B HIS -3  ? B HIS 5   
46  1 Y 1 B HIS -2  ? B HIS 6   
47  1 Y 1 B HIS -1  ? B HIS 7   
48  1 Y 1 B HIS 0   ? B HIS 8   
49  1 Y 1 B MET 1   ? B MET 9   
50  1 Y 1 B ALA 349 ? B ALA 357 
51  1 Y 1 B GLU 350 ? B GLU 358 
52  1 Y 1 B THR 351 ? B THR 359 
53  1 Y 1 B VAL 352 ? B VAL 360 
54  1 Y 1 B ALA 353 ? B ALA 361 
55  1 Y 1 B THR 354 ? B THR 362 
56  1 Y 1 B ARG 355 ? B ARG 363 
57  1 Y 1 B LYS 356 ? B LYS 364 
58  1 Y 1 B ALA 357 ? B ALA 365 
59  1 Y 1 B SER 358 ? B SER 366 
60  1 Y 1 B LEU 520 ? B LEU 528 
61  1 Y 1 B LYS 521 ? B LYS 529 
62  1 Y 1 C MET -7  ? C MET 1   
63  1 Y 1 C ALA -6  ? C ALA 2   
64  1 Y 1 C HIS -5  ? C HIS 3   
65  1 Y 1 C HIS -4  ? C HIS 4   
66  1 Y 1 C HIS -3  ? C HIS 5   
67  1 Y 1 C HIS -2  ? C HIS 6   
68  1 Y 1 C HIS -1  ? C HIS 7   
69  1 Y 1 C HIS 0   ? C HIS 8   
70  1 Y 1 C MET 1   ? C MET 9   
71  1 Y 1 C ILE 184 ? C ILE 192 
72  1 Y 1 C SER 185 ? C SER 193 
73  1 Y 1 C ILE 186 ? C ILE 194 
74  1 Y 1 C ASP 187 ? C ASP 195 
75  1 Y 1 C GLY 188 ? C GLY 196 
76  1 Y 1 C LYS 189 ? C LYS 197 
77  1 Y 1 C VAL 190 ? C VAL 198 
78  1 Y 1 C ILE 244 ? C ILE 252 
79  1 Y 1 C GLY 245 ? C GLY 253 
80  1 Y 1 C LYS 246 ? C LYS 254 
81  1 Y 1 C GLY 247 ? C GLY 255 
82  1 Y 1 C SER 248 ? C SER 256 
83  1 Y 1 C ALA 249 ? C ALA 257 
84  1 Y 1 C ASN 250 ? C ASN 258 
85  1 Y 1 C LYS 251 ? C LYS 259 
86  1 Y 1 C GLU 252 ? C GLU 260 
87  1 Y 1 C GLY 253 ? C GLY 261 
88  1 Y 1 C SER 254 ? C SER 262 
89  1 Y 1 C HIS 255 ? C HIS 263 
90  1 Y 1 C LYS 256 ? C LYS 264 
91  1 Y 1 C THR 257 ? C THR 265 
92  1 Y 1 C HIS 258 ? C HIS 266 
93  1 Y 1 C GLY 259 ? C GLY 267 
94  1 Y 1 C GLY 263 ? C GLY 271 
95  1 Y 1 C ALA 264 ? C ALA 272 
96  1 Y 1 C ASP 265 ? C ASP 273 
97  1 Y 1 C GLU 266 ? C GLU 274 
98  1 Y 1 C ALA 349 ? C ALA 357 
99  1 Y 1 C GLU 350 ? C GLU 358 
100 1 Y 1 C THR 351 ? C THR 359 
101 1 Y 1 C VAL 352 ? C VAL 360 
102 1 Y 1 C ALA 353 ? C ALA 361 
103 1 Y 1 C THR 354 ? C THR 362 
104 1 Y 1 C ARG 355 ? C ARG 363 
105 1 Y 1 C LYS 356 ? C LYS 364 
106 1 Y 1 C ALA 357 ? C ALA 365 
107 1 Y 1 C SER 358 ? C SER 366 
108 1 Y 1 C GLN 359 ? C GLN 367 
109 1 Y 1 C GLN 518 ? C GLN 526 
110 1 Y 1 C ASN 519 ? C ASN 527 
111 1 Y 1 C LEU 520 ? C LEU 528 
112 1 Y 1 C LYS 521 ? C LYS 529 
113 1 Y 1 C PHE 522 ? C PHE 530 
114 1 Y 1 D MET -7  ? D MET 1   
115 1 Y 1 D ALA -6  ? D ALA 2   
116 1 Y 1 D HIS -5  ? D HIS 3   
117 1 Y 1 D HIS -4  ? D HIS 4   
118 1 Y 1 D HIS -3  ? D HIS 5   
119 1 Y 1 D HIS -2  ? D HIS 6   
120 1 Y 1 D HIS -1  ? D HIS 7   
121 1 Y 1 D HIS 0   ? D HIS 8   
122 1 Y 1 D ASN 183 ? D ASN 191 
123 1 Y 1 D ILE 184 ? D ILE 192 
124 1 Y 1 D SER 185 ? D SER 193 
125 1 Y 1 D ILE 186 ? D ILE 194 
126 1 Y 1 D ASP 187 ? D ASP 195 
127 1 Y 1 D GLY 188 ? D GLY 196 
128 1 Y 1 D LYS 189 ? D LYS 197 
129 1 Y 1 D VAL 190 ? D VAL 198 
130 1 Y 1 D ALA 349 ? D ALA 357 
131 1 Y 1 D GLU 350 ? D GLU 358 
132 1 Y 1 D THR 351 ? D THR 359 
133 1 Y 1 D VAL 352 ? D VAL 360 
134 1 Y 1 D ALA 353 ? D ALA 361 
135 1 Y 1 D THR 354 ? D THR 362 
136 1 Y 1 D ARG 355 ? D ARG 363 
137 1 Y 1 D LYS 356 ? D LYS 364 
138 1 Y 1 D ALA 357 ? D ALA 365 
139 1 Y 1 D SER 358 ? D SER 366 
140 1 Y 1 D GLN 359 ? D GLN 367 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL EDO 
3 'CALCIUM ION'  CA  
4 water          HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
