data_6AZW
# 
_entry.id   6AZW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.292 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6AZW         
WWPDB D_1000230076 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 6AZU unspecified 
PDB . 6AZV unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6AZW 
_pdbx_database_status.recvd_initial_deposition_date   2017-09-13 
_pdbx_database_status.SG_entry                        N 
_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 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lewis, H.A.'     1 ? 
'Lammens, A.'     2 ? 
'Steinbacher, S.' 3 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Proc. Natl. Acad. Sci. U.S.A.' 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            115 
_citation.language                  ? 
_citation.page_first                3249 
_citation.page_last                 3254 
_citation.title                     
'Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.1719190115 
_citation.pdbx_database_id_PubMed   29531094 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Nelp, M.T.'     1  
primary 'Kates, P.A.'    2  
primary 'Hunt, J.T.'     3  
primary 'Newitt, J.A.'   4  
primary 'Balog, A.'      5  
primary 'Maley, D.'      6  
primary 'Zhu, X.'        7  
primary 'Abell, L.'      8  
primary 'Allentoff, A.'  9  
primary 'Borzilleri, R.' 10 
primary 'Lewis, H.A.'    11 
primary 'Lin, Z.'        12 
primary 'Seitz, S.P.'    13 
primary 'Yan, C.'        14 
primary 'Groves, J.T.'   15 
# 
_cell.entry_id           6AZW 
_cell.length_a           85.206 
_cell.length_b           92.555 
_cell.length_c           128.698 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         6AZW 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 'Indoleamine 2,3-dioxygenase 1'                                         44355.102 2 1.13.11.52 ? ? ? 
2 non-polymer syn '(2R)-N-(4-cyanophenyl)-2-[cis-4-(quinolin-4-yl)cyclohexyl]propanamide' 383.486   2 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IDO-1,Indoleamine-pyrrole 2,3-dioxygenase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMA
YVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLL
VEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVY
EGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLR
EAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMA
YVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLL
VEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVY
EGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLR
EAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   ILE n 
1 3   SER n 
1 4   LYS n 
1 5   GLU n 
1 6   TYR n 
1 7   HIS n 
1 8   ILE n 
1 9   ASP n 
1 10  GLU n 
1 11  GLU n 
1 12  VAL n 
1 13  GLY n 
1 14  PHE n 
1 15  ALA n 
1 16  LEU n 
1 17  PRO n 
1 18  ASN n 
1 19  PRO n 
1 20  GLN n 
1 21  GLU n 
1 22  ASN n 
1 23  LEU n 
1 24  PRO n 
1 25  ASP n 
1 26  PHE n 
1 27  TYR n 
1 28  ASN n 
1 29  ASP n 
1 30  TRP n 
1 31  MET n 
1 32  PHE n 
1 33  ILE n 
1 34  ALA n 
1 35  LYS n 
1 36  HIS n 
1 37  LEU n 
1 38  PRO n 
1 39  ASP n 
1 40  LEU n 
1 41  ILE n 
1 42  GLU n 
1 43  SER n 
1 44  GLY n 
1 45  GLN n 
1 46  LEU n 
1 47  ARG n 
1 48  GLU n 
1 49  ARG n 
1 50  VAL n 
1 51  GLU n 
1 52  LYS n 
1 53  LEU n 
1 54  ASN n 
1 55  MET n 
1 56  LEU n 
1 57  SER n 
1 58  ILE n 
1 59  ASP n 
1 60  HIS n 
1 61  LEU n 
1 62  THR n 
1 63  ASP n 
1 64  HIS n 
1 65  LYS n 
1 66  SER n 
1 67  GLN n 
1 68  ARG n 
1 69  LEU n 
1 70  ALA n 
1 71  ARG n 
1 72  LEU n 
1 73  VAL n 
1 74  LEU n 
1 75  GLY n 
1 76  CYS n 
1 77  ILE n 
1 78  THR n 
1 79  MET n 
1 80  ALA n 
1 81  TYR n 
1 82  VAL n 
1 83  TRP n 
1 84  GLY n 
1 85  LYS n 
1 86  GLY n 
1 87  HIS n 
1 88  GLY n 
1 89  ASP n 
1 90  VAL n 
1 91  ARG n 
1 92  LYS n 
1 93  VAL n 
1 94  LEU n 
1 95  PRO n 
1 96  ARG n 
1 97  ASN n 
1 98  ILE n 
1 99  ALA n 
1 100 VAL n 
1 101 PRO n 
1 102 TYR n 
1 103 CYS n 
1 104 GLN n 
1 105 LEU n 
1 106 SER n 
1 107 LYS n 
1 108 LYS n 
1 109 LEU n 
1 110 GLU n 
1 111 LEU n 
1 112 PRO n 
1 113 PRO n 
1 114 ILE n 
1 115 LEU n 
1 116 VAL n 
1 117 TYR n 
1 118 ALA n 
1 119 ASP n 
1 120 CYS n 
1 121 VAL n 
1 122 LEU n 
1 123 ALA n 
1 124 ASN n 
1 125 TRP n 
1 126 LYS n 
1 127 LYS n 
1 128 LYS n 
1 129 ASP n 
1 130 PRO n 
1 131 ASN n 
1 132 LYS n 
1 133 PRO n 
1 134 LEU n 
1 135 THR n 
1 136 TYR n 
1 137 GLU n 
1 138 ASN n 
1 139 MET n 
1 140 ASP n 
1 141 VAL n 
1 142 LEU n 
1 143 PHE n 
1 144 SER n 
1 145 PHE n 
1 146 ARG n 
1 147 ASP n 
1 148 GLY n 
1 149 ASP n 
1 150 CYS n 
1 151 SER n 
1 152 LYS n 
1 153 GLY n 
1 154 PHE n 
1 155 PHE n 
1 156 LEU n 
1 157 VAL n 
1 158 SER n 
1 159 LEU n 
1 160 LEU n 
1 161 VAL n 
1 162 GLU n 
1 163 ILE n 
1 164 ALA n 
1 165 ALA n 
1 166 ALA n 
1 167 SER n 
1 168 ALA n 
1 169 ILE n 
1 170 LYS n 
1 171 VAL n 
1 172 ILE n 
1 173 PRO n 
1 174 THR n 
1 175 VAL n 
1 176 PHE n 
1 177 LYS n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 MET n 
1 182 GLN n 
1 183 GLU n 
1 184 ARG n 
1 185 ASP n 
1 186 THR n 
1 187 LEU n 
1 188 LEU n 
1 189 LYS n 
1 190 ALA n 
1 191 LEU n 
1 192 LEU n 
1 193 GLU n 
1 194 ILE n 
1 195 ALA n 
1 196 SER n 
1 197 CYS n 
1 198 LEU n 
1 199 GLU n 
1 200 LYS n 
1 201 ALA n 
1 202 LEU n 
1 203 GLN n 
1 204 VAL n 
1 205 PHE n 
1 206 HIS n 
1 207 GLN n 
1 208 ILE n 
1 209 HIS n 
1 210 ASP n 
1 211 HIS n 
1 212 VAL n 
1 213 ASN n 
1 214 PRO n 
1 215 LYS n 
1 216 ALA n 
1 217 PHE n 
1 218 PHE n 
1 219 SER n 
1 220 VAL n 
1 221 LEU n 
1 222 ARG n 
1 223 ILE n 
1 224 TYR n 
1 225 LEU n 
1 226 SER n 
1 227 GLY n 
1 228 TRP n 
1 229 LYS n 
1 230 GLY n 
1 231 ASN n 
1 232 PRO n 
1 233 GLN n 
1 234 LEU n 
1 235 SER n 
1 236 ASP n 
1 237 GLY n 
1 238 LEU n 
1 239 VAL n 
1 240 TYR n 
1 241 GLU n 
1 242 GLY n 
1 243 PHE n 
1 244 TRP n 
1 245 GLU n 
1 246 ASP n 
1 247 PRO n 
1 248 LYS n 
1 249 GLU n 
1 250 PHE n 
1 251 ALA n 
1 252 GLY n 
1 253 GLY n 
1 254 SER n 
1 255 ALA n 
1 256 GLY n 
1 257 GLN n 
1 258 SER n 
1 259 SER n 
1 260 VAL n 
1 261 PHE n 
1 262 GLN n 
1 263 CYS n 
1 264 PHE n 
1 265 ASP n 
1 266 VAL n 
1 267 LEU n 
1 268 LEU n 
1 269 GLY n 
1 270 ILE n 
1 271 GLN n 
1 272 GLN n 
1 273 THR n 
1 274 ALA n 
1 275 GLY n 
1 276 GLY n 
1 277 GLY n 
1 278 HIS n 
1 279 ALA n 
1 280 ALA n 
1 281 GLN n 
1 282 PHE n 
1 283 LEU n 
1 284 GLN n 
1 285 ASP n 
1 286 MET n 
1 287 ARG n 
1 288 ARG n 
1 289 TYR n 
1 290 MET n 
1 291 PRO n 
1 292 PRO n 
1 293 ALA n 
1 294 HIS n 
1 295 ARG n 
1 296 ASN n 
1 297 PHE n 
1 298 LEU n 
1 299 CYS n 
1 300 SER n 
1 301 LEU n 
1 302 GLU n 
1 303 SER n 
1 304 ASN n 
1 305 PRO n 
1 306 SER n 
1 307 VAL n 
1 308 ARG n 
1 309 GLU n 
1 310 PHE n 
1 311 VAL n 
1 312 LEU n 
1 313 SER n 
1 314 LYS n 
1 315 GLY n 
1 316 ASP n 
1 317 ALA n 
1 318 GLY n 
1 319 LEU n 
1 320 ARG n 
1 321 GLU n 
1 322 ALA n 
1 323 TYR n 
1 324 ASP n 
1 325 ALA n 
1 326 CYS n 
1 327 VAL n 
1 328 LYS n 
1 329 ALA n 
1 330 LEU n 
1 331 VAL n 
1 332 SER n 
1 333 LEU n 
1 334 ARG n 
1 335 SER n 
1 336 TYR n 
1 337 HIS n 
1 338 LEU n 
1 339 GLN n 
1 340 ILE n 
1 341 VAL n 
1 342 THR n 
1 343 LYS n 
1 344 TYR n 
1 345 ILE n 
1 346 LEU n 
1 347 ILE n 
1 348 PRO n 
1 349 ALA n 
1 350 SER n 
1 351 GLN n 
1 352 GLN n 
1 353 PRO n 
1 354 LYS n 
1 355 GLU n 
1 356 ASN n 
1 357 LYS n 
1 358 THR n 
1 359 SER n 
1 360 GLU n 
1 361 ASP n 
1 362 PRO n 
1 363 SER n 
1 364 LYS n 
1 365 LEU n 
1 366 GLU n 
1 367 ALA n 
1 368 LYS n 
1 369 GLY n 
1 370 THR n 
1 371 GLY n 
1 372 GLY n 
1 373 THR n 
1 374 ASP n 
1 375 LEU n 
1 376 MET n 
1 377 ASN n 
1 378 PHE n 
1 379 LEU n 
1 380 LYS n 
1 381 THR n 
1 382 VAL n 
1 383 ARG n 
1 384 SER n 
1 385 THR n 
1 386 THR n 
1 387 GLU n 
1 388 LYS n 
1 389 SER n 
1 390 LEU n 
1 391 LEU n 
1 392 LYS n 
1 393 GLU n 
1 394 GLY 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                   394 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IDO1, IDO, INDO' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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                    I23O1_HUMAN 
_struct_ref.pdbx_db_accession          P14902 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAY
VWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLV
EIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYE
GFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLRE
AYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_struct_ref.pdbx_align_begin           11 
# 
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 6AZW A 2 ? 394 ? P14902 11 ? 403 ? 11 403 
2 1 6AZW B 2 ? 394 ? P14902 11 ? 403 ? 11 403 
# 
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 6AZW MET A 1 ? UNP P14902 ? ? 'initiating methionine' 10 1 
2 6AZW MET B 1 ? UNP P14902 ? ? 'initiating methionine' 10 2 
# 
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 
C51 non-polymer         . '(2R)-N-(4-cyanophenyl)-2-[cis-4-(quinolin-4-yl)cyclohexyl]propanamide' ? 'C25 H25 N3 O'   383.486 
CYS 'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'   121.158 
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 
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 
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                   6AZW 
_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            2.86 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         57.00 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '16% PEG 8K, 0.2 M NH4 acetate, 0.1 M CHES pH 8.75' 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-12-01 
# 
_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   1.00 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate            70.280 
_reflns.entry_id                         6AZW 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.780 
_reflns.d_resolution_low                 46.278 
_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                       25234 
_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             96.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.661 
_reflns.pdbx_Rmerge_I_obs                0.046 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            18.670 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 1.079 
_reflns.pdbx_scaling_rejects             541 
_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                  0.053 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         92390 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.999 
_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 
2.780  3.030  ? 3.150  ? ? ? ? 5670 96.400 ? ? ? ? 0.435 ? ? ? ? ? ? ? ? 3.760 ? ? ? ? 0.506 ? ? 1 1 0.919 ? 
3.030  3.340  ? 6.390  ? ? ? ? 4873 95.600 ? ? ? ? 0.203 ? ? ? ? ? ? ? ? 3.545 ? ? ? ? 0.238 ? ? 2 1 0.971 ? 
3.340  3.840  ? 14.880 ? ? ? ? 4976 97.600 ? ? ? ? 0.084 ? ? ? ? ? ? ? ? 3.855 ? ? ? ? 0.097 ? ? 3 1 0.994 ? 
3.840  4.680  ? 25.930 ? ? ? ? 4275 95.300 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 3.534 ? ? ? ? 0.045 ? ? 4 1 0.998 ? 
4.680  5.930  ? 36.330 ? ? ? ? 2687 94.800 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 3.642 ? ? ? ? 0.032 ? ? 5 1 0.999 ? 
5.930  7.620  ? 44.010 ? ? ? ? 1411 95.700 ? ? ? ? 0.023 ? ? ? ? ? ? ? ? 3.592 ? ? ? ? 0.027 ? ? 6 1 0.999 ? 
7.620  11.110 ? 55.530 ? ? ? ? 898  97.300 ? ? ? ? 0.017 ? ? ? ? ? ? ? ? 3.540 ? ? ? ? 0.020 ? ? 7 1 1.000 ? 
11.110 17.790 ? 61.730 ? ? ? ? 333  93.300 ? ? ? ? 0.014 ? ? ? ? ? ? ? ? 3.285 ? ? ? ? 0.017 ? ? 8 1 0.999 ? 
17.790 46.278 ? 64.560 ? ? ? ? 111  88.800 ? ? ? ? 0.016 ? ? ? ? ? ? ? ? 3.441 ? ? ? ? 0.019 ? ? 9 1 1.000 ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 6AZW 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25191 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             46.278 
_refine.ls_d_res_high                            2.780 
_refine.ls_percent_reflns_obs                    95.88 
_refine.ls_R_factor_obs                          0.2191 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2166 
_refine.ls_R_factor_R_free                       0.2986 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.93 
_refine.ls_number_reflns_R_free                  739 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.54 
_refine.pdbx_overall_phase_error                 38.82 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5655 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               5713 
_refine_hist.d_res_high                       2.780 
_refine_hist.d_res_low                        46.278 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.016  ? ? 5854 'X-RAY DIFFRACTION' ? 
f_angle_d          1.462  ? ? 7967 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 11.709 ? ? 3501 'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.067  ? ? 910  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.012  ? ? 1056 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 2.7800 2.9946  4840 0.3238 96.00 0.4511 . . 128 . . 
'X-RAY DIFFRACTION' . 2.9946 3.2959  4772 0.3061 95.00 0.3978 . . 146 . . 
'X-RAY DIFFRACTION' . 3.2959 3.7726  4949 0.2342 98.00 0.3647 . . 150 . . 
'X-RAY DIFFRACTION' . 3.7726 4.7524  4844 0.1986 95.00 0.2374 . . 157 . . 
'X-RAY DIFFRACTION' . 4.7524 46.2839 5047 0.1843 95.00 0.2700 . . 158 . . 
# 
_struct.entry_id                     6AZW 
_struct.title                        'IDO1/FXB-001116 crystal structure' 
_struct.pdbx_descriptor              'Indoleamine 2,3-dioxygenase 1 (E.C.1.13.11.52)' 
_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        6AZW 
_struct_keywords.text            'IDO1/FXB-001116 crystal structure, oxidoreductase-oxidoreductase inhibitor complex' 
_struct_keywords.pdbx_keywords   'oxidoreductase/oxidoreductase inhibitor' 
# 
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 2 ? 
D N N 2 ? 
# 
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 3   ? HIS A 7   ? SER A 12  HIS A 16  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 24  ? PHE A 26  ? PRO A 33  PHE A 35  5 ? 3  
HELX_P HELX_P3  AA3 TYR A 27  ? LYS A 35  ? TYR A 36  LYS A 44  1 ? 9  
HELX_P HELX_P4  AA4 HIS A 36  ? GLY A 44  ? HIS A 45  GLY A 53  1 ? 9  
HELX_P HELX_P5  AA5 GLN A 45  ? LYS A 52  ? GLN A 54  LYS A 61  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 63  ? GLY A 84  ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P7  AA7 PRO A 95  ? GLU A 110 ? PRO A 104 GLU A 119 1 ? 16 
HELX_P HELX_P8  AA8 VAL A 116 ? VAL A 121 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P9  AA9 THR A 135 ? GLU A 137 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P10 AB1 CYS A 150 ? LYS A 170 ? CYS A 159 LYS A 179 1 ? 21 
HELX_P HELX_P11 AB2 VAL A 171 ? GLN A 182 ? VAL A 180 GLN A 191 1 ? 12 
HELX_P HELX_P12 AB3 GLU A 183 ? GLN A 207 ? GLU A 192 GLN A 216 1 ? 25 
HELX_P HELX_P13 AB4 GLN A 207 ? VAL A 212 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P14 AB5 ASN A 213 ? VAL A 220 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P15 AB6 VAL A 220 ? LEU A 225 ? VAL A 229 LEU A 234 1 ? 6  
HELX_P HELX_P16 AB7 ASN A 231 ? SER A 235 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P17 AB8 SER A 254 ? SER A 258 ? SER A 263 SER A 267 5 ? 5  
HELX_P HELX_P18 AB9 SER A 259 ? LEU A 268 ? SER A 268 LEU A 277 1 ? 10 
HELX_P HELX_P19 AC1 GLY A 277 ? ARG A 288 ? GLY A 286 ARG A 297 1 ? 12 
HELX_P HELX_P20 AC2 PRO A 291 ? SER A 303 ? PRO A 300 SER A 312 1 ? 13 
HELX_P HELX_P21 AC3 SER A 306 ? GLY A 315 ? SER A 315 GLY A 324 1 ? 10 
HELX_P HELX_P22 AC4 ASP A 316 ? ILE A 345 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P23 AC5 ILE A 345 ? SER A 350 ? ILE A 354 SER A 359 1 ? 6  
HELX_P HELX_P24 AC6 THR A 373 ? LYS A 388 ? THR A 382 LYS A 397 1 ? 16 
HELX_P HELX_P25 AC7 SER B 3   ? HIS B 7   ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P26 AC8 PRO B 24  ? PHE B 26  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P27 AC9 TYR B 27  ? LYS B 35  ? TYR B 36  LYS B 44  1 ? 9  
HELX_P HELX_P28 AD1 HIS B 36  ? SER B 43  ? HIS B 45  SER B 52  1 ? 8  
HELX_P HELX_P29 AD2 GLN B 45  ? LYS B 52  ? GLN B 54  LYS B 61  1 ? 8  
HELX_P HELX_P30 AD3 ASP B 63  ? GLY B 84  ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P31 AD4 PRO B 95  ? GLU B 110 ? PRO B 104 GLU B 119 1 ? 16 
HELX_P HELX_P32 AD5 VAL B 116 ? VAL B 121 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P33 AD6 THR B 135 ? GLU B 137 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P34 AD7 CYS B 150 ? LYS B 170 ? CYS B 159 LYS B 179 1 ? 21 
HELX_P HELX_P35 AD8 VAL B 171 ? MET B 181 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P36 AD9 GLU B 183 ? HIS B 206 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P37 AE1 GLN B 207 ? VAL B 212 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P38 AE2 ASN B 213 ? VAL B 220 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P39 AE3 ARG B 222 ? SER B 226 ? ARG B 231 SER B 235 5 ? 5  
HELX_P HELX_P40 AE4 ASN B 231 ? SER B 235 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P41 AE5 SER B 254 ? GLN B 257 ? SER B 263 GLN B 266 5 ? 4  
HELX_P HELX_P42 AE6 SER B 258 ? LEU B 268 ? SER B 267 LEU B 277 1 ? 11 
HELX_P HELX_P43 AE7 GLY B 277 ? MET B 286 ? GLY B 286 MET B 295 1 ? 10 
HELX_P HELX_P44 AE8 ARG B 287 ? MET B 290 ? ARG B 296 MET B 299 5 ? 4  
HELX_P HELX_P45 AE9 PRO B 291 ? ASN B 304 ? PRO B 300 ASN B 313 1 ? 14 
HELX_P HELX_P46 AF1 SER B 306 ? LYS B 314 ? SER B 315 LYS B 323 1 ? 9  
HELX_P HELX_P47 AF2 ASP B 316 ? ILE B 345 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P48 AF3 ILE B 345 ? GLN B 351 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P49 AF4 THR B 373 ? LYS B 388 ? THR B 382 LYS B 397 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            299 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            299 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             308 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             308 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.013 
_struct_conn.pdbx_value_order              ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-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 VAL A 93  ? LEU A 94  ? VAL A 102 LEU A 103 
AA1 2 LEU A 238 ? TYR A 240 ? LEU A 247 TYR A 249 
AA1 3 PRO A 247 ? LYS A 248 ? PRO A 256 LYS A 257 
AA2 1 TRP A 125 ? LYS A 127 ? TRP A 134 LYS A 136 
AA2 2 MET A 139 ? VAL A 141 ? MET A 148 VAL A 150 
AA3 1 VAL B 93  ? LEU B 94  ? VAL B 102 LEU B 103 
AA3 2 LEU B 238 ? TYR B 240 ? LEU B 247 TYR B 249 
AA3 3 PRO B 247 ? LYS B 248 ? PRO B 256 LYS B 257 
AA4 1 TRP B 125 ? LYS B 127 ? TRP B 134 LYS B 136 
AA4 2 MET B 139 ? VAL B 141 ? MET B 148 VAL B 150 
# 
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 LEU A 94  ? N LEU A 103 O VAL A 239 ? O VAL A 248 
AA1 2 3 N LEU A 238 ? N LEU A 247 O LYS A 248 ? O LYS A 257 
AA2 1 2 N LYS A 126 ? N LYS A 135 O ASP A 140 ? O ASP A 149 
AA3 1 2 N LEU B 94  ? N LEU B 103 O VAL B 239 ? O VAL B 248 
AA3 2 3 N LEU B 238 ? N LEU B 247 O LYS B 248 ? O LYS B 257 
AA4 1 2 N LYS B 126 ? N LYS B 135 O ASP B 140 ? O ASP B 149 
# 
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 C51 501 ? 14 'binding site for residue C51 A 501' 
AC2 Software B C51 501 ? 10 'binding site for residue C51 B 501' 
# 
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 14 TYR A 117 ? TYR A 126 . ? 1_555 ? 
2  AC1 14 CYS A 120 ? CYS A 129 . ? 1_555 ? 
3  AC1 14 VAL A 121 ? VAL A 130 . ? 1_555 ? 
4  AC1 14 PHE A 154 ? PHE A 163 . ? 1_555 ? 
5  AC1 14 SER A 158 ? SER A 167 . ? 1_555 ? 
6  AC1 14 PHE A 205 ? PHE A 214 . ? 1_555 ? 
7  AC1 14 GLY A 253 ? GLY A 262 . ? 1_555 ? 
8  AC1 14 SER A 254 ? SER A 263 . ? 1_555 ? 
9  AC1 14 ALA A 255 ? ALA A 264 . ? 1_555 ? 
10 AC1 14 VAL A 260 ? VAL A 269 . ? 1_555 ? 
11 AC1 14 PHE A 261 ? PHE A 270 . ? 1_555 ? 
12 AC1 14 LEU A 333 ? LEU A 342 . ? 1_555 ? 
13 AC1 14 ARG A 334 ? ARG A 343 . ? 1_555 ? 
14 AC1 14 HIS A 337 ? HIS A 346 . ? 1_555 ? 
15 AC2 10 TYR B 117 ? TYR B 126 . ? 1_555 ? 
16 AC2 10 PHE B 154 ? PHE B 163 . ? 1_555 ? 
17 AC2 10 SER B 158 ? SER B 167 . ? 1_555 ? 
18 AC2 10 GLY B 253 ? GLY B 262 . ? 1_555 ? 
19 AC2 10 SER B 254 ? SER B 263 . ? 1_555 ? 
20 AC2 10 ALA B 255 ? ALA B 264 . ? 1_555 ? 
21 AC2 10 VAL B 260 ? VAL B 269 . ? 1_555 ? 
22 AC2 10 PHE B 261 ? PHE B 270 . ? 1_555 ? 
23 AC2 10 ARG B 334 ? ARG B 343 . ? 1_555 ? 
24 AC2 10 HIS B 337 ? HIS B 346 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6AZW 
_atom_sites.fract_transf_matrix[1][1]   0.011736 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010804 
_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]   0.007770 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
H 
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    . MET A 1 1   ? 25.768  -34.925 65.841  1.00 118.47 1  10  MET A N    1 
ATOM   2     C CA   . MET A 1 1   ? 26.890  -34.855 66.779  1.00 131.38 ?  10  MET A CA   1 
ATOM   3     C C    . MET A 1 1   ? 27.000  -33.478 67.423  1.00 144.24 ?  10  MET A C    1 
ATOM   4     O O    . MET A 1 1   ? 26.703  -32.472 66.787  1.00 91.15  ?  10  MET A O    1 
ATOM   5     C CB   . MET A 1 1   ? 28.200  -35.201 66.068  1.00 122.51 ?  10  MET A CB   1 
ATOM   6     H HA   . MET A 1 1   ? 26.751  -35.514 67.477  1.00 157.65 ?  10  MET A HA   1 
ATOM   7     N N    . ILE A 1 2   ? 27.504  -33.436 68.661  1.00 177.74 ?  11  ILE A N    1 
ATOM   8     C CA   . ILE A 1 2   ? 27.599  -32.180 69.395  1.00 227.20 ?  11  ILE A CA   1 
ATOM   9     C C    . ILE A 1 2   ? 28.735  -31.330 68.854  1.00 128.48 ?  11  ILE A C    1 
ATOM   10    O O    . ILE A 1 2   ? 29.736  -31.841 68.339  1.00 135.75 ?  11  ILE A O    1 
ATOM   11    C CB   . ILE A 1 2   ? 27.823  -32.429 70.895  1.00 312.27 ?  11  ILE A CB   1 
ATOM   12    C CG1  . ILE A 1 2   ? 26.686  -33.248 71.492  1.00 219.31 ?  11  ILE A CG1  1 
ATOM   13    C CG2  . ILE A 1 2   ? 27.932  -31.094 71.625  1.00 188.47 ?  11  ILE A CG2  1 
ATOM   14    C CD1  . ILE A 1 2   ? 26.945  -33.673 72.921  1.00 244.93 ?  11  ILE A CD1  1 
ATOM   15    H H    . ILE A 1 2   ? 27.796  -34.120 69.092  1.00 213.28 ?  11  ILE A H    1 
ATOM   16    H HA   . ILE A 1 2   ? 26.772  -31.684 69.289  1.00 272.64 ?  11  ILE A HA   1 
ATOM   17    H HB   . ILE A 1 2   ? 28.653  -32.918 71.010  1.00 374.72 ?  11  ILE A HB   1 
ATOM   18    H HG12 . ILE A 1 2   ? 25.875  -32.715 71.482  1.00 263.18 ?  11  ILE A HG12 1 
ATOM   19    H HG13 . ILE A 1 2   ? 26.562  -34.049 70.960  1.00 263.18 ?  11  ILE A HG13 1 
ATOM   20    H HG21 . ILE A 1 2   ? 28.073  -31.262 72.570  1.00 226.17 ?  11  ILE A HG21 1 
ATOM   21    H HG22 . ILE A 1 2   ? 28.682  -30.597 71.261  1.00 226.17 ?  11  ILE A HG22 1 
ATOM   22    H HG23 . ILE A 1 2   ? 27.110  -30.596 71.496  1.00 226.17 ?  11  ILE A HG23 1 
ATOM   23    H HD11 . ILE A 1 2   ? 26.188  -34.187 73.240  1.00 293.92 ?  11  ILE A HD11 1 
ATOM   24    H HD12 . ILE A 1 2   ? 27.749  -34.215 72.948  1.00 293.92 ?  11  ILE A HD12 1 
ATOM   25    H HD13 . ILE A 1 2   ? 27.062  -32.881 73.469  1.00 293.92 ?  11  ILE A HD13 1 
ATOM   26    N N    . SER A 1 3   ? 28.590  -30.016 69.004  1.00 107.85 ?  12  SER A N    1 
ATOM   27    C CA   . SER A 1 3   ? 29.611  -29.090 68.549  1.00 161.96 ?  12  SER A CA   1 
ATOM   28    C C    . SER A 1 3   ? 30.870  -29.144 69.414  1.00 231.39 ?  12  SER A C    1 
ATOM   29    O O    . SER A 1 3   ? 30.811  -29.063 70.646  1.00 79.32  ?  12  SER A O    1 
ATOM   30    C CB   . SER A 1 3   ? 29.039  -27.681 68.543  1.00 108.73 ?  12  SER A CB   1 
ATOM   31    O OG   . SER A 1 3   ? 30.028  -26.763 68.136  1.00 128.87 ?  12  SER A OG   1 
ATOM   32    H H    . SER A 1 3   ? 27.908  -29.638 69.367  1.00 129.42 ?  12  SER A H    1 
ATOM   33    H HA   . SER A 1 3   ? 29.862  -29.317 67.640  1.00 194.35 ?  12  SER A HA   1 
ATOM   34    H HB2  . SER A 1 3   ? 28.295  -27.642 67.922  1.00 130.48 ?  12  SER A HB2  1 
ATOM   35    H HB3  . SER A 1 3   ? 28.742  -27.454 69.437  1.00 130.48 ?  12  SER A HB3  1 
ATOM   36    H HG   . SER A 1 3   ? 29.713  -25.984 68.132  1.00 154.65 ?  12  SER A HG   1 
ATOM   37    N N    . LYS A 1 4   ? 32.024  -29.217 68.753  1.00 165.08 ?  13  LYS A N    1 
ATOM   38    C CA   . LYS A 1 4   ? 33.290  -29.259 69.466  1.00 144.05 ?  13  LYS A CA   1 
ATOM   39    C C    . LYS A 1 4   ? 33.645  -27.899 70.041  1.00 161.62 ?  13  LYS A C    1 
ATOM   40    O O    . LYS A 1 4   ? 34.502  -27.815 70.926  1.00 199.48 ?  13  LYS A O    1 
ATOM   41    C CB   . LYS A 1 4   ? 34.397  -29.753 68.534  1.00 148.97 ?  13  LYS A CB   1 
ATOM   42    H H    . LYS A 1 4   ? 32.097  -29.243 67.897  1.00 198.10 ?  13  LYS A H    1 
ATOM   43    H HA   . LYS A 1 4   ? 33.217  -29.886 70.203  1.00 172.86 ?  13  LYS A HA   1 
ATOM   44    N N    . GLU A 1 5   ? 32.995  -26.837 69.557  1.00 135.76 ?  14  GLU A N    1 
ATOM   45    C CA   . GLU A 1 5   ? 33.207  -25.494 70.068  1.00 101.51 ?  14  GLU A CA   1 
ATOM   46    C C    . GLU A 1 5   ? 32.687  -25.315 71.480  1.00 83.46  ?  14  GLU A C    1 
ATOM   47    O O    . GLU A 1 5   ? 32.936  -24.268 72.087  1.00 102.18 ?  14  GLU A O    1 
ATOM   48    C CB   . GLU A 1 5   ? 32.515  -24.485 69.169  1.00 99.60  ?  14  GLU A CB   1 
ATOM   49    C CG   . GLU A 1 5   ? 31.033  -24.351 69.446  1.00 193.08 ?  14  GLU A CG   1 
ATOM   50    H H    . GLU A 1 5   ? 32.418  -26.877 68.920  1.00 162.91 ?  14  GLU A H    1 
ATOM   51    H HA   . GLU A 1 5   ? 34.157  -25.299 70.068  1.00 121.82 ?  14  GLU A HA   1 
ATOM   52    H HB2  . GLU A 1 5   ? 32.922  -23.615 69.301  1.00 119.52 ?  14  GLU A HB2  1 
ATOM   53    H HB3  . GLU A 1 5   ? 32.621  -24.762 68.245  1.00 119.52 ?  14  GLU A HB3  1 
ATOM   54    H HG2  . GLU A 1 5   ? 30.673  -25.225 69.666  1.00 231.69 ?  14  GLU A HG2  1 
ATOM   55    H HG3  . GLU A 1 5   ? 30.905  -23.743 70.191  1.00 231.69 ?  14  GLU A HG3  1 
ATOM   56    N N    . TYR A 1 6   ? 31.952  -26.292 72.005  1.00 111.71 ?  15  TYR A N    1 
ATOM   57    C CA   . TYR A 1 6   ? 31.567  -26.328 73.408  1.00 91.35  ?  15  TYR A CA   1 
ATOM   58    C C    . TYR A 1 6   ? 32.518  -27.218 74.231  1.00 85.73  ?  15  TYR A C    1 
ATOM   59    O O    . TYR A 1 6   ? 32.405  -27.276 75.470  1.00 61.85  ?  15  TYR A O    1 
ATOM   60    C CB   . TYR A 1 6   ? 30.103  -26.806 73.533  1.00 84.54  ?  15  TYR A CB   1 
ATOM   61    C CG   . TYR A 1 6   ? 29.023  -25.857 73.026  1.00 121.62 ?  15  TYR A CG   1 
ATOM   62    C CD1  . TYR A 1 6   ? 28.771  -24.658 73.663  1.00 82.38  ?  15  TYR A CD1  1 
ATOM   63    C CD2  . TYR A 1 6   ? 28.249  -26.170 71.911  1.00 147.82 ?  15  TYR A CD2  1 
ATOM   64    C CE1  . TYR A 1 6   ? 27.785  -23.780 73.194  1.00 60.24  ?  15  TYR A CE1  1 
ATOM   65    C CE2  . TYR A 1 6   ? 27.269  -25.310 71.449  1.00 96.44  ?  15  TYR A CE2  1 
ATOM   66    C CZ   . TYR A 1 6   ? 27.046  -24.122 72.089  1.00 87.82  ?  15  TYR A CZ   1 
ATOM   67    O OH   . TYR A 1 6   ? 26.068  -23.262 71.636  1.00 73.82  ?  15  TYR A OH   1 
ATOM   68    H H    . TYR A 1 6   ? 31.657  -26.961 71.553  1.00 134.05 ?  15  TYR A H    1 
ATOM   69    H HA   . TYR A 1 6   ? 31.617  -25.429 73.769  1.00 109.62 ?  15  TYR A HA   1 
ATOM   70    H HB2  . TYR A 1 6   ? 30.012  -27.634 73.036  1.00 101.45 ?  15  TYR A HB2  1 
ATOM   71    H HB3  . TYR A 1 6   ? 29.919  -26.974 74.471  1.00 101.45 ?  15  TYR A HB3  1 
ATOM   72    H HD1  . TYR A 1 6   ? 29.275  -24.422 74.408  1.00 98.86  ?  15  TYR A HD1  1 
ATOM   73    H HD2  . TYR A 1 6   ? 28.397  -26.973 71.466  1.00 177.38 ?  15  TYR A HD2  1 
ATOM   74    H HE1  . TYR A 1 6   ? 27.628  -22.975 73.632  1.00 72.29  ?  15  TYR A HE1  1 
ATOM   75    H HE2  . TYR A 1 6   ? 26.767  -25.538 70.700  1.00 115.73 ?  15  TYR A HE2  1 
ATOM   76    H HH   . TYR A 1 6   ? 25.692  -23.586 70.958  1.00 88.58  ?  15  TYR A HH   1 
ATOM   77    N N    . HIS A 1 7   ? 33.466  -27.900 73.581  1.00 84.01  ?  16  HIS A N    1 
ATOM   78    C CA   . HIS A 1 7   ? 34.492  -28.655 74.293  1.00 86.36  ?  16  HIS A CA   1 
ATOM   79    C C    . HIS A 1 7   ? 33.869  -29.707 75.195  1.00 68.23  ?  16  HIS A C    1 
ATOM   80    O O    . HIS A 1 7   ? 34.181  -29.834 76.379  1.00 92.27  ?  16  HIS A O    1 
ATOM   81    C CB   . HIS A 1 7   ? 35.392  -27.718 75.073  1.00 106.62 ?  16  HIS A CB   1 
ATOM   82    C CG   . HIS A 1 7   ? 36.108  -26.738 74.203  1.00 113.74 ?  16  HIS A CG   1 
ATOM   83    N ND1  . HIS A 1 7   ? 36.513  -27.037 72.920  1.00 125.80 ?  16  HIS A ND1  1 
ATOM   84    C CD2  . HIS A 1 7   ? 36.436  -25.445 74.410  1.00 92.81  ?  16  HIS A CD2  1 
ATOM   85    C CE1  . HIS A 1 7   ? 37.092  -25.977 72.387  1.00 123.13 ?  16  HIS A CE1  1 
ATOM   86    N NE2  . HIS A 1 7   ? 37.050  -24.995 73.268  1.00 99.11  ?  16  HIS A NE2  1 
ATOM   87    H H    . HIS A 1 7   ? 33.534  -27.939 72.725  1.00 100.82 ?  16  HIS A H    1 
ATOM   88    H HA   . HIS A 1 7   ? 35.043  -29.116 73.642  1.00 103.63 ?  16  HIS A HA   1 
ATOM   89    H HB2  . HIS A 1 7   ? 34.854  -27.218 75.706  1.00 127.94 ?  16  HIS A HB2  1 
ATOM   90    H HB3  . HIS A 1 7   ? 36.058  -28.242 75.545  1.00 127.94 ?  16  HIS A HB3  1 
ATOM   91    H HD2  . HIS A 1 7   ? 36.283  -24.954 75.185  1.00 111.37 ?  16  HIS A HD2  1 
ATOM   92    H HE1  . HIS A 1 7   ? 37.457  -25.927 71.533  1.00 147.75 ?  16  HIS A HE1  1 
ATOM   93    N N    . ILE A 1 8   ? 32.965  -30.465 74.595  1.00 53.93  ?  17  ILE A N    1 
ATOM   94    C CA   . ILE A 1 8   ? 32.411  -31.670 75.165  1.00 62.47  ?  17  ILE A CA   1 
ATOM   95    C C    . ILE A 1 8   ? 32.945  -32.831 74.335  1.00 89.61  ?  17  ILE A C    1 
ATOM   96    O O    . ILE A 1 8   ? 32.858  -32.839 73.097  1.00 101.79 ?  17  ILE A O    1 
ATOM   97    C CB   . ILE A 1 8   ? 30.871  -31.623 75.183  1.00 75.52  ?  17  ILE A CB   1 
ATOM   98    C CG1  . ILE A 1 8   ? 30.410  -30.541 76.143  1.00 103.97 ?  17  ILE A CG1  1 
ATOM   99    C CG2  . ILE A 1 8   ? 30.308  -32.961 75.624  1.00 91.99  ?  17  ILE A CG2  1 
ATOM   100   C CD1  . ILE A 1 8   ? 29.036  -30.124 75.948  1.00 118.03 ?  17  ILE A CD1  1 
ATOM   101   H H    . ILE A 1 8   ? 32.645  -30.287 73.816  1.00 64.72  ?  17  ILE A H    1 
ATOM   102   H HA   . ILE A 1 8   ? 32.727  -31.772 76.077  1.00 74.97  ?  17  ILE A HA   1 
ATOM   103   H HB   . ILE A 1 8   ? 30.547  -31.419 74.292  1.00 90.63  ?  17  ILE A HB   1 
ATOM   104   H HG12 . ILE A 1 8   ? 30.492  -30.874 77.051  1.00 124.76 ?  17  ILE A HG12 1 
ATOM   105   H HG13 . ILE A 1 8   ? 30.975  -29.761 76.028  1.00 124.76 ?  17  ILE A HG13 1 
ATOM   106   H HG21 . ILE A 1 8   ? 29.340  -32.910 75.628  1.00 110.39 ?  17  ILE A HG21 1 
ATOM   107   H HG22 . ILE A 1 8   ? 30.601  -33.646 75.003  1.00 110.39 ?  17  ILE A HG22 1 
ATOM   108   H HG23 . ILE A 1 8   ? 30.633  -33.161 76.516  1.00 110.39 ?  17  ILE A HG23 1 
ATOM   109   H HD11 . ILE A 1 8   ? 28.820  -29.435 76.595  1.00 141.64 ?  17  ILE A HD11 1 
ATOM   110   H HD12 . ILE A 1 8   ? 28.937  -29.775 75.048  1.00 141.64 ?  17  ILE A HD12 1 
ATOM   111   H HD13 . ILE A 1 8   ? 28.453  -30.890 76.072  1.00 141.64 ?  17  ILE A HD13 1 
ATOM   112   N N    . ASP A 1 9   ? 33.523  -33.781 75.020  1.00 95.93  ?  18  ASP A N    1 
ATOM   113   C CA   . ASP A 1 9   ? 34.192  -34.868 74.373  1.00 109.69 ?  18  ASP A CA   1 
ATOM   114   C C    . ASP A 1 9   ? 33.191  -35.983 74.254  1.00 80.93  ?  18  ASP A C    1 
ATOM   115   O O    . ASP A 1 9   ? 32.516  -36.315 75.229  1.00 64.61  ?  18  ASP A O    1 
ATOM   116   C CB   . ASP A 1 9   ? 35.402  -35.257 75.218  1.00 91.18  ?  18  ASP A CB   1 
ATOM   117   C CG   . ASP A 1 9   ? 36.266  -36.308 74.582  1.00 104.48 ?  18  ASP A CG   1 
ATOM   118   O OD1  . ASP A 1 9   ? 36.951  -36.017 73.581  1.00 85.42  ?  18  ASP A OD1  1 
ATOM   119   O OD2  . ASP A 1 9   ? 36.288  -37.429 75.130  1.00 119.79 -1 18  ASP A OD2  1 
ATOM   120   H H    . ASP A 1 9   ? 33.542  -33.818 75.879  1.00 115.12 ?  18  ASP A H    1 
ATOM   121   H HA   . ASP A 1 9   ? 34.488  -34.604 73.488  1.00 131.63 ?  18  ASP A HA   1 
ATOM   122   H HB2  . ASP A 1 9   ? 35.950  -34.469 75.362  1.00 109.42 ?  18  ASP A HB2  1 
ATOM   123   H HB3  . ASP A 1 9   ? 35.092  -35.602 76.070  1.00 109.42 ?  18  ASP A HB3  1 
ATOM   124   N N    . GLU A 1 10  ? 33.146  -36.587 73.068  1.00 73.55  ?  19  GLU A N    1 
ATOM   125   C CA   . GLU A 1 10  ? 32.248  -37.694 72.834  1.00 130.09 ?  19  GLU A CA   1 
ATOM   126   C C    . GLU A 1 10  ? 32.468  -38.761 73.900  1.00 100.61 ?  19  GLU A C    1 
ATOM   127   O O    . GLU A 1 10  ? 31.506  -39.375 74.378  1.00 69.00  ?  19  GLU A O    1 
ATOM   128   C CB   . GLU A 1 10  ? 32.491  -38.192 71.408  1.00 59.82  ?  19  GLU A CB   1 
ATOM   129   H H    . GLU A 1 10  ? 33.626  -36.369 72.389  1.00 88.26  ?  19  GLU A H    1 
ATOM   130   H HA   . GLU A 1 10  ? 31.331  -37.384 72.897  1.00 156.11 ?  19  GLU A HA   1 
ATOM   131   N N    . GLU A 1 11  ? 33.714  -38.905 74.362  1.00 104.65 ?  20  GLU A N    1 
ATOM   132   C CA   . GLU A 1 11  ? 34.092  -39.842 75.418  1.00 82.56  ?  20  GLU A CA   1 
ATOM   133   C C    . GLU A 1 11  ? 34.010  -39.223 76.818  1.00 67.46  ?  20  GLU A C    1 
ATOM   134   O O    . GLU A 1 11  ? 33.275  -39.695 77.684  1.00 61.68  ?  20  GLU A O    1 
ATOM   135   C CB   . GLU A 1 11  ? 35.495  -40.374 75.123  1.00 96.14  ?  20  GLU A CB   1 
ATOM   136   C CG   . GLU A 1 11  ? 36.192  -41.220 76.228  1.00 115.42 ?  20  GLU A CG   1 
ATOM   137   C CD   . GLU A 1 11  ? 37.755  -41.227 76.105  1.00 130.94 ?  20  GLU A CD   1 
ATOM   138   O OE1  . GLU A 1 11  ? 38.331  -40.523 75.229  1.00 156.61 ?  20  GLU A OE1  1 
ATOM   139   O OE2  . GLU A 1 11  ? 38.411  -41.931 76.906  1.00 125.92 -1 20  GLU A OE2  1 
ATOM   140   H H    . GLU A 1 11  ? 34.381  -38.451 74.065  1.00 125.58 ?  20  GLU A H    1 
ATOM   141   H HA   . GLU A 1 11  ? 33.481  -40.595 75.396  1.00 99.08  ?  20  GLU A HA   1 
ATOM   142   H HB2  . GLU A 1 11  ? 35.444  -40.930 74.331  1.00 115.36 ?  20  GLU A HB2  1 
ATOM   143   H HB3  . GLU A 1 11  ? 36.071  -39.615 74.942  1.00 115.36 ?  20  GLU A HB3  1 
ATOM   144   H HG2  . GLU A 1 11  ? 35.962  -40.853 77.097  1.00 138.51 ?  20  GLU A HG2  1 
ATOM   145   H HG3  . GLU A 1 11  ? 35.883  -42.137 76.164  1.00 138.51 ?  20  GLU A HG3  1 
ATOM   146   N N    . VAL A 1 12  ? 34.746  -38.161 77.097  1.00 94.87  ?  21  VAL A N    1 
ATOM   147   C CA   . VAL A 1 12  ? 34.749  -37.741 78.492  1.00 79.91  ?  21  VAL A CA   1 
ATOM   148   C C    . VAL A 1 12  ? 33.846  -36.556 78.738  1.00 81.24  ?  21  VAL A C    1 
ATOM   149   O O    . VAL A 1 12  ? 33.747  -36.096 79.884  1.00 70.50  ?  21  VAL A O    1 
ATOM   150   C CB   . VAL A 1 12  ? 36.176  -37.453 79.019  1.00 92.43  ?  21  VAL A CB   1 
ATOM   151   C CG1  . VAL A 1 12  ? 36.995  -38.671 78.925  1.00 80.64  ?  21  VAL A CG1  1 
ATOM   152   C CG2  . VAL A 1 12  ? 36.846  -36.318 78.258  1.00 122.52 ?  21  VAL A CG2  1 
ATOM   153   H H    . VAL A 1 12  ? 35.218  -37.695 76.549  1.00 113.84 ?  21  VAL A H    1 
ATOM   154   H HA   . VAL A 1 12  ? 34.399  -38.475 79.021  1.00 95.89  ?  21  VAL A HA   1 
ATOM   155   H HB   . VAL A 1 12  ? 36.123  -37.198 79.953  1.00 110.92 ?  21  VAL A HB   1 
ATOM   156   H HG11 . VAL A 1 12  ? 37.886  -38.478 79.258  1.00 96.77  ?  21  VAL A HG11 1 
ATOM   157   H HG12 . VAL A 1 12  ? 36.585  -39.368 79.461  1.00 96.77  ?  21  VAL A HG12 1 
ATOM   158   H HG13 . VAL A 1 12  ? 37.041  -38.950 77.998  1.00 96.77  ?  21  VAL A HG13 1 
ATOM   159   H HG21 . VAL A 1 12  ? 37.733  -36.175 78.623  1.00 147.03 ?  21  VAL A HG21 1 
ATOM   160   H HG22 . VAL A 1 12  ? 36.907  -36.560 77.321  1.00 147.03 ?  21  VAL A HG22 1 
ATOM   161   H HG23 . VAL A 1 12  ? 36.313  -35.514 78.359  1.00 147.03 ?  21  VAL A HG23 1 
ATOM   162   N N    . GLY A 1 13  ? 33.121  -36.085 77.739  1.00 88.59  ?  22  GLY A N    1 
ATOM   163   C CA   . GLY A 1 13  ? 32.196  -35.022 78.082  1.00 72.12  ?  22  GLY A CA   1 
ATOM   164   C C    . GLY A 1 13  ? 32.822  -33.708 78.540  1.00 66.39  ?  22  GLY A C    1 
ATOM   165   O O    . GLY A 1 13  ? 33.576  -33.075 77.787  1.00 66.61  ?  22  GLY A O    1 
ATOM   166   H H    . GLY A 1 13  ? 33.139  -36.338 76.917  1.00 106.31 ?  22  GLY A H    1 
ATOM   167   H HA2  . GLY A 1 13  ? 31.643  -34.831 77.308  1.00 86.54  ?  22  GLY A HA2  1 
ATOM   168   H HA3  . GLY A 1 13  ? 31.614  -35.335 78.792  1.00 86.54  ?  22  GLY A HA3  1 
ATOM   169   N N    . PHE A 1 14  ? 32.490  -33.260 79.759  1.00 54.83  ?  23  PHE A N    1 
ATOM   170   C CA   . PHE A 1 14  ? 32.969  -31.960 80.265  1.00 57.77  ?  23  PHE A CA   1 
ATOM   171   C C    . PHE A 1 14  ? 34.355  -32.036 80.878  1.00 76.02  ?  23  PHE A C    1 
ATOM   172   O O    . PHE A 1 14  ? 34.918  -30.991 81.219  1.00 105.34 ?  23  PHE A O    1 
ATOM   173   C CB   . PHE A 1 14  ? 32.081  -31.386 81.361  1.00 67.27  ?  23  PHE A CB   1 
ATOM   174   C CG   . PHE A 1 14  ? 30.738  -30.963 80.921  1.00 94.07  ?  23  PHE A CG   1 
ATOM   175   C CD1  . PHE A 1 14  ? 30.557  -29.844 80.112  1.00 60.30  ?  23  PHE A CD1  1 
ATOM   176   C CD2  . PHE A 1 14  ? 29.620  -31.666 81.371  1.00 59.25  ?  23  PHE A CD2  1 
ATOM   177   C CE1  . PHE A 1 14  ? 29.282  -29.475 79.713  1.00 85.62  ?  23  PHE A CE1  1 
ATOM   178   C CE2  . PHE A 1 14  ? 28.306  -31.269 80.969  1.00 52.57  ?  23  PHE A CE2  1 
ATOM   179   C CZ   . PHE A 1 14  ? 28.153  -30.188 80.144  1.00 66.08  ?  23  PHE A CZ   1 
ATOM   180   H H    . PHE A 1 14  ? 31.991  -33.689 80.313  1.00 65.80  ?  23  PHE A H    1 
ATOM   181   H HA   . PHE A 1 14  ? 32.995  -31.324 79.533  1.00 69.32  ?  23  PHE A HA   1 
ATOM   182   H HB2  . PHE A 1 14  ? 31.965  -32.060 82.048  1.00 80.73  ?  23  PHE A HB2  1 
ATOM   183   H HB3  . PHE A 1 14  ? 32.522  -30.609 81.740  1.00 80.73  ?  23  PHE A HB3  1 
ATOM   184   H HD1  . PHE A 1 14  ? 31.295  -29.368 79.806  1.00 72.36  ?  23  PHE A HD1  1 
ATOM   185   H HD2  . PHE A 1 14  ? 29.731  -32.408 81.921  1.00 71.10  ?  23  PHE A HD2  1 
ATOM   186   H HE1  . PHE A 1 14  ? 29.172  -28.734 79.162  1.00 102.75 ?  23  PHE A HE1  1 
ATOM   187   H HE2  . PHE A 1 14  ? 27.563  -31.748 81.257  1.00 63.09  ?  23  PHE A HE2  1 
ATOM   188   H HZ   . PHE A 1 14  ? 27.302  -29.919 79.881  1.00 79.30  ?  23  PHE A HZ   1 
ATOM   189   N N    . ALA A 1 15  ? 34.867  -33.237 81.136  1.00 72.47  ?  24  ALA A N    1 
ATOM   190   C CA   . ALA A 1 15  ? 36.242  -33.347 81.560  1.00 72.79  ?  24  ALA A CA   1 
ATOM   191   C C    . ALA A 1 15  ? 37.170  -32.936 80.431  1.00 62.07  ?  24  ALA A C    1 
ATOM   192   O O    . ALA A 1 15  ? 36.830  -32.958 79.243  1.00 67.33  ?  24  ALA A O    1 
ATOM   193   C CB   . ALA A 1 15  ? 36.569  -34.763 82.019  1.00 86.54  ?  24  ALA A CB   1 
ATOM   194   H H    . ALA A 1 15  ? 34.444  -33.983 81.073  1.00 86.96  ?  24  ALA A H    1 
ATOM   195   H HA   . ALA A 1 15  ? 36.392  -32.746 82.307  1.00 87.35  ?  24  ALA A HA   1 
ATOM   196   H HB1  . ALA A 1 15  ? 37.498  -34.798 82.296  1.00 103.85 ?  24  ALA A HB1  1 
ATOM   197   H HB2  . ALA A 1 15  ? 35.993  -34.994 82.765  1.00 103.85 ?  24  ALA A HB2  1 
ATOM   198   H HB3  . ALA A 1 15  ? 36.420  -35.376 81.283  1.00 103.85 ?  24  ALA A HB3  1 
ATOM   199   N N    . LEU A 1 16  ? 38.323  -32.526 80.818  1.00 66.28  ?  25  LEU A N    1 
ATOM   200   C CA   . LEU A 1 16  ? 39.332  -32.193 79.849  1.00 53.17  ?  25  LEU A CA   1 
ATOM   201   C C    . LEU A 1 16  ? 40.024  -33.484 79.459  1.00 54.35  ?  25  LEU A C    1 
ATOM   202   O O    . LEU A 1 16  ? 40.377  -34.271 80.347  1.00 75.57  ?  25  LEU A O    1 
ATOM   203   C CB   . LEU A 1 16  ? 40.307  -31.209 80.450  1.00 68.39  ?  25  LEU A CB   1 
ATOM   204   C CG   . LEU A 1 16  ? 41.256  -30.567 79.460  1.00 65.59  ?  25  LEU A CG   1 
ATOM   205   C CD1  . LEU A 1 16  ? 40.514  -29.738 78.441  1.00 66.27  ?  25  LEU A CD1  1 
ATOM   206   C CD2  . LEU A 1 16  ? 42.187  -29.784 80.338  1.00 67.61  ?  25  LEU A CD2  1 
ATOM   207   H H    . LEU A 1 16  ? 38.563  -32.426 81.638  1.00 79.54  ?  25  LEU A H    1 
ATOM   208   H HA   . LEU A 1 16  ? 38.924  -31.799 79.062  1.00 63.80  ?  25  LEU A HA   1 
ATOM   209   H HB2  . LEU A 1 16  ? 39.804  -30.498 80.877  1.00 82.07  ?  25  LEU A HB2  1 
ATOM   210   H HB3  . LEU A 1 16  ? 40.844  -31.671 81.112  1.00 82.07  ?  25  LEU A HB3  1 
ATOM   211   H HG   . LEU A 1 16  ? 41.763  -31.253 78.998  1.00 78.71  ?  25  LEU A HG   1 
ATOM   212   H HD11 . LEU A 1 16  ? 41.155  -29.345 77.828  1.00 79.53  ?  25  LEU A HD11 1 
ATOM   213   H HD12 . LEU A 1 16  ? 39.899  -30.310 77.956  1.00 79.53  ?  25  LEU A HD12 1 
ATOM   214   H HD13 . LEU A 1 16  ? 40.024  -29.038 78.900  1.00 79.53  ?  25  LEU A HD13 1 
ATOM   215   H HD21 . LEU A 1 16  ? 42.840  -29.332 79.782  1.00 81.14  ?  25  LEU A HD21 1 
ATOM   216   H HD22 . LEU A 1 16  ? 41.673  -29.133 80.842  1.00 81.14  ?  25  LEU A HD22 1 
ATOM   217   H HD23 . LEU A 1 16  ? 42.635  -30.394 80.946  1.00 81.14  ?  25  LEU A HD23 1 
ATOM   218   N N    . PRO A 1 17  ? 40.118  -33.803 78.170  1.00 58.89  ?  26  PRO A N    1 
ATOM   219   C CA   . PRO A 1 17  ? 40.702  -35.109 77.771  1.00 82.61  ?  26  PRO A CA   1 
ATOM   220   C C    . PRO A 1 17  ? 42.220  -35.090 77.773  1.00 90.30  ?  26  PRO A C    1 
ATOM   221   O O    . PRO A 1 17  ? 42.837  -34.186 77.209  1.00 110.16 ?  26  PRO A O    1 
ATOM   222   C CB   . PRO A 1 17  ? 40.148  -35.349 76.361  1.00 81.96  ?  26  PRO A CB   1 
ATOM   223   C CG   . PRO A 1 17  ? 39.803  -33.950 75.824  1.00 62.38  ?  26  PRO A CG   1 
ATOM   224   C CD   . PRO A 1 17  ? 39.440  -33.097 77.066  1.00 47.29  ?  26  PRO A CD   1 
ATOM   225   H HA   . PRO A 1 17  ? 40.389  -35.812 78.362  1.00 99.13  ?  26  PRO A HA   1 
ATOM   226   H HB2  . PRO A 1 17  ? 40.826  -35.771 75.811  1.00 98.35  ?  26  PRO A HB2  1 
ATOM   227   H HB3  . PRO A 1 17  ? 39.353  -35.903 76.412  1.00 98.35  ?  26  PRO A HB3  1 
ATOM   228   H HG2  . PRO A 1 17  ? 40.575  -33.578 75.369  1.00 74.86  ?  26  PRO A HG2  1 
ATOM   229   H HG3  . PRO A 1 17  ? 39.047  -34.012 75.219  1.00 74.86  ?  26  PRO A HG3  1 
ATOM   230   H HD2  . PRO A 1 17  ? 39.790  -32.197 76.973  1.00 56.75  ?  26  PRO A HD2  1 
ATOM   231   H HD3  . PRO A 1 17  ? 38.480  -33.094 77.205  1.00 56.75  ?  26  PRO A HD3  1 
ATOM   232   N N    . ASN A 1 18  ? 42.817  -36.136 78.374  1.00 93.84  ?  27  ASN A N    1 
ATOM   233   C CA   . ASN A 1 18  ? 44.263  -36.363 78.537  1.00 72.27  ?  27  ASN A CA   1 
ATOM   234   C C    . ASN A 1 18  ? 44.950  -35.049 78.903  1.00 73.10  ?  27  ASN A C    1 
ATOM   235   O O    . ASN A 1 18  ? 45.695  -34.451 78.107  1.00 96.10  ?  27  ASN A O    1 
ATOM   236   C CB   . ASN A 1 18  ? 44.849  -37.027 77.285  1.00 67.36  ?  27  ASN A CB   1 
ATOM   237   C CG   . ASN A 1 18  ? 44.473  -38.509 77.182  1.00 130.60 ?  27  ASN A CG   1 
ATOM   238   H H    . ASN A 1 18  ? 42.360  -36.777 78.721  1.00 112.61 ?  27  ASN A H    1 
ATOM   239   H HA   . ASN A 1 18  ? 44.396  -36.975 79.278  1.00 86.72  ?  27  ASN A HA   1 
ATOM   240   H HB2  . ASN A 1 18  ? 44.510  -36.575 76.497  1.00 80.83  ?  27  ASN A HB2  1 
ATOM   241   H HB3  . ASN A 1 18  ? 45.816  -36.963 77.315  1.00 80.83  ?  27  ASN A HB3  1 
ATOM   242   N N    . PRO A 1 19  ? 44.737  -34.617 80.144  1.00 82.12  ?  28  PRO A N    1 
ATOM   243   C CA   . PRO A 1 19  ? 45.285  -33.341 80.626  1.00 68.18  ?  28  PRO A CA   1 
ATOM   244   C C    . PRO A 1 19  ? 46.807  -33.314 80.757  1.00 67.26  ?  28  PRO A C    1 
ATOM   245   O O    . PRO A 1 19  ? 47.449  -34.334 80.983  1.00 53.72  ?  28  PRO A O    1 
ATOM   246   C CB   . PRO A 1 19  ? 44.628  -33.185 82.001  1.00 56.37  ?  28  PRO A CB   1 
ATOM   247   C CG   . PRO A 1 19  ? 43.374  -33.974 81.907  1.00 79.31  ?  28  PRO A CG   1 
ATOM   248   C CD   . PRO A 1 19  ? 43.690  -35.139 81.028  1.00 68.72  ?  28  PRO A CD   1 
ATOM   249   H HA   . PRO A 1 19  ? 45.000  -32.614 80.050  1.00 81.81  ?  28  PRO A HA   1 
ATOM   250   H HB2  . PRO A 1 19  ? 45.211  -33.545 82.687  1.00 67.64  ?  28  PRO A HB2  1 
ATOM   251   H HB3  . PRO A 1 19  ? 44.435  -32.249 82.168  1.00 67.64  ?  28  PRO A HB3  1 
ATOM   252   H HG2  . PRO A 1 19  ? 43.112  -34.274 82.791  1.00 95.17  ?  28  PRO A HG2  1 
ATOM   253   H HG3  . PRO A 1 19  ? 42.676  -33.428 81.511  1.00 95.17  ?  28  PRO A HG3  1 
ATOM   254   H HD2  . PRO A 1 19  ? 44.030  -35.879 81.556  1.00 82.46  ?  28  PRO A HD2  1 
ATOM   255   H HD3  . PRO A 1 19  ? 42.910  -35.397 80.513  1.00 82.46  ?  28  PRO A HD3  1 
ATOM   256   N N    . GLN A 1 20  ? 47.380  -32.120 80.568  1.00 66.75  ?  29  GLN A N    1 
ATOM   257   C CA   . GLN A 1 20  ? 48.823  -32.012 80.570  1.00 64.16  ?  29  GLN A CA   1 
ATOM   258   C C    . GLN A 1 20  ? 49.270  -32.275 81.988  1.00 64.31  ?  29  GLN A C    1 
ATOM   259   O O    . GLN A 1 20  ? 48.667  -31.764 82.930  1.00 55.21  ?  29  GLN A O    1 
ATOM   260   C CB   . GLN A 1 20  ? 49.264  -30.640 80.066  1.00 123.81 ?  29  GLN A CB   1 
ATOM   261   C CG   . GLN A 1 20  ? 50.698  -30.525 79.702  1.00 103.16 ?  29  GLN A CG   1 
ATOM   262   C CD   . GLN A 1 20  ? 50.926  -29.400 78.748  1.00 96.16  ?  29  GLN A CD   1 
ATOM   263   O OE1  . GLN A 1 20  ? 50.079  -29.163 77.884  1.00 76.60  ?  29  GLN A OE1  1 
ATOM   264   N NE2  . GLN A 1 20  ? 52.047  -28.633 78.934  1.00 103.15 ?  29  GLN A NE2  1 
ATOM   265   H H    . GLN A 1 20  ? 46.959  -31.381 80.440  1.00 80.10  ?  29  GLN A H    1 
ATOM   266   H HA   . GLN A 1 20  ? 49.204  -32.692 79.992  1.00 76.99  ?  29  GLN A HA   1 
ATOM   267   H HB2  . GLN A 1 20  ? 48.745  -30.422 79.276  1.00 148.57 ?  29  GLN A HB2  1 
ATOM   268   H HB3  . GLN A 1 20  ? 49.087  -29.987 80.761  1.00 148.57 ?  29  GLN A HB3  1 
ATOM   269   H HG2  . GLN A 1 20  ? 51.220  -30.357 80.502  1.00 123.79 ?  29  GLN A HG2  1 
ATOM   270   H HG3  . GLN A 1 20  ? 50.988  -31.348 79.277  1.00 123.79 ?  29  GLN A HG3  1 
ATOM   271   H HE21 . GLN A 1 20  ? 52.586  -28.809 79.581  1.00 123.78 ?  29  GLN A HE21 1 
ATOM   272   H HE22 . GLN A 1 20  ? 52.211  -27.976 78.404  1.00 123.78 ?  29  GLN A HE22 1 
ATOM   273   N N    . GLU A 1 21  ? 50.301  -33.106 82.149  1.00 81.99  ?  30  GLU A N    1 
ATOM   274   C CA   . GLU A 1 21  ? 50.813  -33.399 83.479  1.00 82.32  ?  30  GLU A CA   1 
ATOM   275   C C    . GLU A 1 21  ? 51.992  -32.498 83.871  1.00 81.03  ?  30  GLU A C    1 
ATOM   276   O O    . GLU A 1 21  ? 52.272  -32.325 85.069  1.00 72.62  ?  30  GLU A O    1 
ATOM   277   C CB   . GLU A 1 21  ? 51.248  -34.854 83.564  1.00 98.59  ?  30  GLU A CB   1 
ATOM   278   C CG   . GLU A 1 21  ? 50.204  -35.896 83.339  1.00 100.12 ?  30  GLU A CG   1 
ATOM   279   C CD   . GLU A 1 21  ? 50.759  -37.281 83.607  1.00 110.25 ?  30  GLU A CD   1 
ATOM   280   O OE1  . GLU A 1 21  ? 51.668  -37.398 84.469  1.00 103.48 ?  30  GLU A OE1  1 
ATOM   281   O OE2  . GLU A 1 21  ? 50.289  -38.241 82.959  1.00 120.57 -1 30  GLU A OE2  1 
ATOM   282   H H    . GLU A 1 21  ? 50.715  -33.506 81.510  1.00 98.39  ?  30  GLU A H    1 
ATOM   283   H HA   . GLU A 1 21  ? 50.104  -33.260 84.126  1.00 98.79  ?  30  GLU A HA   1 
ATOM   284   H HB2  . GLU A 1 21  ? 51.942  -35.000 82.902  1.00 118.30 ?  30  GLU A HB2  1 
ATOM   285   H HB3  . GLU A 1 21  ? 51.615  -35.006 84.449  1.00 118.30 ?  30  GLU A HB3  1 
ATOM   286   H HG2  . GLU A 1 21  ? 49.460  -35.742 83.943  1.00 120.14 ?  30  GLU A HG2  1 
ATOM   287   H HG3  . GLU A 1 21  ? 49.904  -35.858 82.417  1.00 120.14 ?  30  GLU A HG3  1 
ATOM   288   N N    . ASN A 1 22  ? 52.650  -31.865 82.900  1.00 93.44  ?  31  ASN A N    1 
ATOM   289   C CA   . ASN A 1 22  ? 53.894  -31.169 83.160  1.00 85.51  ?  31  ASN A CA   1 
ATOM   290   C C    . ASN A 1 22  ? 53.882  -29.830 82.469  1.00 85.36  ?  31  ASN A C    1 
ATOM   291   O O    . ASN A 1 22  ? 53.538  -29.722 81.291  1.00 93.47  ?  31  ASN A O    1 
ATOM   292   C CB   . ASN A 1 22  ? 55.061  -32.003 82.675  1.00 96.36  ?  31  ASN A CB   1 
ATOM   293   C CG   . ASN A 1 22  ? 55.160  -33.284 83.414  1.00 148.95 ?  31  ASN A CG   1 
ATOM   294   O OD1  . ASN A 1 22  ? 55.493  -33.305 84.595  1.00 146.83 ?  31  ASN A OD1  1 
ATOM   295   N ND2  . ASN A 1 22  ? 54.834  -34.374 82.736  1.00 94.92  ?  31  ASN A ND2  1 
ATOM   296   H H    . ASN A 1 22  ? 52.390  -31.826 82.081  1.00 112.13 ?  31  ASN A H    1 
ATOM   297   H HA   . ASN A 1 22  ? 53.992  -31.024 84.114  1.00 102.61 ?  31  ASN A HA   1 
ATOM   298   H HB2  . ASN A 1 22  ? 54.941  -32.203 81.733  1.00 115.64 ?  31  ASN A HB2  1 
ATOM   299   H HB3  . ASN A 1 22  ? 55.885  -31.509 82.811  1.00 115.64 ?  31  ASN A HB3  1 
ATOM   300   H HD21 . ASN A 1 22  ? 54.873  -35.144 83.117  1.00 113.90 ?  31  ASN A HD21 1 
ATOM   301   H HD22 . ASN A 1 22  ? 54.583  -34.312 81.916  1.00 113.90 ?  31  ASN A HD22 1 
ATOM   302   N N    . LEU A 1 23  ? 54.285  -28.827 83.205  1.00 100.01 ?  32  LEU A N    1 
ATOM   303   C CA   . LEU A 1 23  ? 54.461  -27.521 82.634  1.00 92.05  ?  32  LEU A CA   1 
ATOM   304   C C    . LEU A 1 23  ? 55.813  -27.447 81.945  1.00 105.94 ?  32  LEU A C    1 
ATOM   305   O O    . LEU A 1 23  ? 56.739  -28.207 82.262  1.00 92.45  ?  32  LEU A O    1 
ATOM   306   C CB   . LEU A 1 23  ? 54.389  -26.451 83.721  1.00 69.85  ?  32  LEU A CB   1 
ATOM   307   C CG   . LEU A 1 23  ? 53.060  -26.329 84.470  1.00 78.40  ?  32  LEU A CG   1 
ATOM   308   C CD1  . LEU A 1 23  ? 53.213  -25.386 85.704  1.00 80.16  ?  32  LEU A CD1  1 
ATOM   309   C CD2  . LEU A 1 23  ? 51.911  -25.897 83.481  1.00 52.69  ?  32  LEU A CD2  1 
ATOM   310   H H    . LEU A 1 23  ? 54.464  -28.876 84.045  1.00 120.02 ?  32  LEU A H    1 
ATOM   311   H HA   . LEU A 1 23  ? 53.765  -27.351 81.980  1.00 110.46 ?  32  LEU A HA   1 
ATOM   312   H HB2  . LEU A 1 23  ? 55.074  -26.642 84.381  1.00 83.82  ?  32  LEU A HB2  1 
ATOM   313   H HB3  . LEU A 1 23  ? 54.569  -25.590 83.312  1.00 83.82  ?  32  LEU A HB3  1 
ATOM   314   H HG   . LEU A 1 23  ? 52.826  -27.206 84.810  1.00 94.08  ?  32  LEU A HG   1 
ATOM   315   H HD11 . LEU A 1 23  ? 52.360  -25.324 86.162  1.00 96.19  ?  32  LEU A HD11 1 
ATOM   316   H HD12 . LEU A 1 23  ? 53.883  -25.755 86.301  1.00 96.19  ?  32  LEU A HD12 1 
ATOM   317   H HD13 . LEU A 1 23  ? 53.489  -24.508 85.399  1.00 96.19  ?  32  LEU A HD13 1 
ATOM   318   H HD21 . LEU A 1 23  ? 51.079  -25.826 83.975  1.00 63.23  ?  32  LEU A HD21 1 
ATOM   319   H HD22 . LEU A 1 23  ? 52.137  -25.039 83.089  1.00 63.23  ?  32  LEU A HD22 1 
ATOM   320   H HD23 . LEU A 1 23  ? 51.826  -26.567 82.784  1.00 63.23  ?  32  LEU A HD23 1 
ATOM   321   N N    . PRO A 1 24  ? 55.952  -26.547 80.982  1.00 90.13  ?  33  PRO A N    1 
ATOM   322   C CA   . PRO A 1 24  ? 57.280  -26.284 80.451  1.00 81.05  ?  33  PRO A CA   1 
ATOM   323   C C    . PRO A 1 24  ? 58.248  -26.089 81.608  1.00 72.53  ?  33  PRO A C    1 
ATOM   324   O O    . PRO A 1 24  ? 57.863  -25.649 82.696  1.00 75.22  ?  33  PRO A O    1 
ATOM   325   C CB   . PRO A 1 24  ? 57.078  -25.019 79.629  1.00 66.28  ?  33  PRO A CB   1 
ATOM   326   C CG   . PRO A 1 24  ? 55.642  -25.078 79.204  1.00 133.82 ?  33  PRO A CG   1 
ATOM   327   C CD   . PRO A 1 24  ? 54.903  -25.790 80.280  1.00 79.89  ?  33  PRO A CD   1 
ATOM   328   H HA   . PRO A 1 24  ? 57.579  -27.009 79.881  1.00 97.26  ?  33  PRO A HA   1 
ATOM   329   H HB2  . PRO A 1 24  ? 57.244  -24.238 80.180  1.00 79.54  ?  33  PRO A HB2  1 
ATOM   330   H HB3  . PRO A 1 24  ? 57.667  -25.030 78.858  1.00 79.54  ?  33  PRO A HB3  1 
ATOM   331   H HG2  . PRO A 1 24  ? 55.300  -24.176 79.099  1.00 160.58 ?  33  PRO A HG2  1 
ATOM   332   H HG3  . PRO A 1 24  ? 55.573  -25.565 78.368  1.00 160.58 ?  33  PRO A HG3  1 
ATOM   333   H HD2  . PRO A 1 24  ? 54.487  -25.153 80.881  1.00 95.87  ?  33  PRO A HD2  1 
ATOM   334   H HD3  . PRO A 1 24  ? 54.249  -26.395 79.896  1.00 95.87  ?  33  PRO A HD3  1 
ATOM   335   N N    . ASP A 1 25  ? 59.521  -26.427 81.363  1.00 101.49 ?  34  ASP A N    1 
ATOM   336   C CA   . ASP A 1 25  ? 60.519  -26.400 82.432  1.00 97.33  ?  34  ASP A CA   1 
ATOM   337   C C    . ASP A 1 25  ? 60.731  -25.016 83.023  1.00 72.30  ?  34  ASP A C    1 
ATOM   338   O O    . ASP A 1 25  ? 61.196  -24.903 84.161  1.00 79.86  ?  34  ASP A O    1 
ATOM   339   C CB   . ASP A 1 25  ? 61.839  -26.984 81.950  1.00 128.93 ?  34  ASP A CB   1 
ATOM   340   C CG   . ASP A 1 25  ? 61.790  -28.498 81.807  1.00 157.01 ?  34  ASP A CG   1 
ATOM   341   O OD1  . ASP A 1 25  ? 60.928  -29.134 82.469  1.00 160.54 ?  34  ASP A OD1  1 
ATOM   342   O OD2  . ASP A 1 25  ? 62.637  -29.054 81.070  1.00 170.14 -1 34  ASP A OD2  1 
ATOM   343   H H    . ASP A 1 25  ? 59.825  -26.672 80.597  1.00 121.79 ?  34  ASP A H    1 
ATOM   344   H HA   . ASP A 1 25  ? 60.202  -26.969 83.150  1.00 116.80 ?  34  ASP A HA   1 
ATOM   345   H HB2  . ASP A 1 25  ? 62.054  -26.607 81.082  1.00 154.72 ?  34  ASP A HB2  1 
ATOM   346   H HB3  . ASP A 1 25  ? 62.534  -26.765 82.589  1.00 154.72 ?  34  ASP A HB3  1 
ATOM   347   N N    . PHE A 1 26  ? 60.328  -23.961 82.333  1.00 82.37  ?  35  PHE A N    1 
ATOM   348   C CA   . PHE A 1 26  ? 60.390  -22.651 82.951  1.00 93.81  ?  35  PHE A CA   1 
ATOM   349   C C    . PHE A 1 26  ? 59.688  -22.673 84.302  1.00 99.23  ?  35  PHE A C    1 
ATOM   350   O O    . PHE A 1 26  ? 60.224  -22.189 85.313  1.00 64.90  ?  35  PHE A O    1 
ATOM   351   C CB   . PHE A 1 26  ? 59.729  -21.684 81.990  1.00 107.90 ?  35  PHE A CB   1 
ATOM   352   C CG   . PHE A 1 26  ? 59.749  -20.277 82.402  1.00 122.96 ?  35  PHE A CG   1 
ATOM   353   C CD1  . PHE A 1 26  ? 60.827  -19.491 82.123  1.00 100.25 ?  35  PHE A CD1  1 
ATOM   354   C CD2  . PHE A 1 26  ? 58.632  -19.716 82.998  1.00 83.27  ?  35  PHE A CD2  1 
ATOM   355   C CE1  . PHE A 1 26  ? 60.829  -18.175 82.455  1.00 100.34 ?  35  PHE A CE1  1 
ATOM   356   C CE2  . PHE A 1 26  ? 58.624  -18.393 83.336  1.00 80.94  ?  35  PHE A CE2  1 
ATOM   357   C CZ   . PHE A 1 26  ? 59.732  -17.605 83.038  1.00 78.63  ?  35  PHE A CZ   1 
ATOM   358   H H    . PHE A 1 26  ? 60.022  -23.975 81.529  1.00 98.85  ?  35  PHE A H    1 
ATOM   359   H HA   . PHE A 1 26  ? 61.314  -22.387 83.079  1.00 112.57 ?  35  PHE A HA   1 
ATOM   360   H HB2  . PHE A 1 26  ? 60.183  -21.744 81.134  1.00 129.49 ?  35  PHE A HB2  1 
ATOM   361   H HB3  . PHE A 1 26  ? 58.801  -21.944 81.883  1.00 129.49 ?  35  PHE A HB3  1 
ATOM   362   H HD1  . PHE A 1 26  ? 61.571  -19.862 81.706  1.00 120.30 ?  35  PHE A HD1  1 
ATOM   363   H HD2  . PHE A 1 26  ? 57.887  -20.244 83.173  1.00 99.93  ?  35  PHE A HD2  1 
ATOM   364   H HE1  . PHE A 1 26  ? 61.574  -17.652 82.267  1.00 120.40 ?  35  PHE A HE1  1 
ATOM   365   H HE2  . PHE A 1 26  ? 57.877  -18.018 83.744  1.00 97.13  ?  35  PHE A HE2  1 
ATOM   366   H HZ   . PHE A 1 26  ? 59.747  -16.708 83.283  1.00 94.36  ?  35  PHE A HZ   1 
ATOM   367   N N    . TYR A 1 27  ? 58.564  -23.385 84.381  1.00 85.90  ?  36  TYR A N    1 
ATOM   368   C CA   . TYR A 1 27  ? 57.742  -23.264 85.568  1.00 76.15  ?  36  TYR A CA   1 
ATOM   369   C C    . TYR A 1 27  ? 58.061  -24.302 86.614  1.00 71.45  ?  36  TYR A C    1 
ATOM   370   O O    . TYR A 1 27  ? 57.177  -24.617 87.417  1.00 79.74  ?  36  TYR A O    1 
ATOM   371   C CB   . TYR A 1 27  ? 56.279  -23.345 85.188  1.00 77.55  ?  36  TYR A CB   1 
ATOM   372   C CG   . TYR A 1 27  ? 55.846  -22.265 84.223  1.00 63.89  ?  36  TYR A CG   1 
ATOM   373   C CD1  . TYR A 1 27  ? 55.713  -20.978 84.644  1.00 61.31  ?  36  TYR A CD1  1 
ATOM   374   C CD2  . TYR A 1 27  ? 55.580  -22.545 82.889  1.00 94.83  ?  36  TYR A CD2  1 
ATOM   375   C CE1  . TYR A 1 27  ? 55.342  -19.959 83.765  1.00 75.85  ?  36  TYR A CE1  1 
ATOM   376   C CE2  . TYR A 1 27  ? 55.208  -21.545 82.014  1.00 81.16  ?  36  TYR A CE2  1 
ATOM   377   C CZ   . TYR A 1 27  ? 55.089  -20.243 82.464  1.00 93.81  ?  36  TYR A CZ   1 
ATOM   378   O OH   . TYR A 1 27  ? 54.727  -19.202 81.626  1.00 122.52 ?  36  TYR A OH   1 
ATOM   379   H H    . TYR A 1 27  ? 58.268  -23.925 83.781  1.00 103.08 ?  36  TYR A H    1 
ATOM   380   H HA   . TYR A 1 27  ? 57.896  -22.392 85.964  1.00 91.39  ?  36  TYR A HA   1 
ATOM   381   H HB2  . TYR A 1 27  ? 56.112  -24.204 84.768  1.00 93.06  ?  36  TYR A HB2  1 
ATOM   382   H HB3  . TYR A 1 27  ? 55.741  -23.260 85.990  1.00 93.06  ?  36  TYR A HB3  1 
ATOM   383   H HD1  . TYR A 1 27  ? 55.894  -20.770 85.532  1.00 73.57  ?  36  TYR A HD1  1 
ATOM   384   H HD2  . TYR A 1 27  ? 55.667  -23.417 82.578  1.00 113.80 ?  36  TYR A HD2  1 
ATOM   385   H HE1  . TYR A 1 27  ? 55.263  -19.086 84.074  1.00 91.02  ?  36  TYR A HE1  1 
ATOM   386   H HE2  . TYR A 1 27  ? 55.038  -21.747 81.122  1.00 97.40  ?  36  TYR A HE2  1 
ATOM   387   H HH   . TYR A 1 27  ? 54.708  -18.480 82.056  1.00 147.03 ?  36  TYR A HH   1 
ATOM   388   N N    . ASN A 1 28  ? 59.300  -24.839 86.648  1.00 61.01  ?  37  ASN A N    1 
ATOM   389   C CA   . ASN A 1 28  ? 59.631  -25.882 87.611  1.00 73.10  ?  37  ASN A CA   1 
ATOM   390   C C    . ASN A 1 28  ? 59.434  -25.452 89.053  1.00 67.21  ?  37  ASN A C    1 
ATOM   391   O O    . ASN A 1 28  ? 59.210  -26.306 89.921  1.00 104.40 ?  37  ASN A O    1 
ATOM   392   C CB   . ASN A 1 28  ? 61.079  -26.331 87.444  1.00 87.33  ?  37  ASN A CB   1 
ATOM   393   C CG   . ASN A 1 28  ? 61.282  -27.149 86.219  1.00 111.69 ?  37  ASN A CG   1 
ATOM   394   O OD1  . ASN A 1 28  ? 60.331  -27.685 85.652  1.00 125.05 ?  37  ASN A OD1  1 
ATOM   395   N ND2  . ASN A 1 28  ? 62.523  -27.251 85.781  1.00 129.90 ?  37  ASN A ND2  1 
ATOM   396   H H    . ASN A 1 28  ? 59.948  -24.613 86.130  1.00 73.21  ?  37  ASN A H    1 
ATOM   397   H HA   . ASN A 1 28  ? 59.061  -26.650 87.449  1.00 87.72  ?  37  ASN A HA   1 
ATOM   398   H HB2  . ASN A 1 28  ? 61.648  -25.548 87.381  1.00 104.79 ?  37  ASN A HB2  1 
ATOM   399   H HB3  . ASN A 1 28  ? 61.335  -26.868 88.210  1.00 104.79 ?  37  ASN A HB3  1 
ATOM   400   H HD21 . ASN A 1 28  ? 62.693  -27.714 85.076  1.00 155.88 ?  37  ASN A HD21 1 
ATOM   401   H HD22 . ASN A 1 28  ? 63.161  -26.856 86.200  1.00 155.88 ?  37  ASN A HD22 1 
ATOM   402   N N    . ASP A 1 29  ? 59.457  -24.153 89.327  1.00 90.09  ?  38  ASP A N    1 
ATOM   403   C CA   . ASP A 1 29  ? 59.385  -23.719 90.718  1.00 89.19  ?  38  ASP A CA   1 
ATOM   404   C C    . ASP A 1 29  ? 57.971  -23.792 91.249  1.00 79.64  ?  38  ASP A C    1 
ATOM   405   O O    . ASP A 1 29  ? 57.755  -24.171 92.401  1.00 78.92  ?  38  ASP A O    1 
ATOM   406   C CB   . ASP A 1 29  ? 59.920  -22.296 90.862  1.00 99.06  ?  38  ASP A CB   1 
ATOM   407   C CG   . ASP A 1 29  ? 61.467  -22.241 90.868  1.00 104.55 ?  38  ASP A CG   1 
ATOM   408   O OD1  . ASP A 1 29  ? 62.116  -23.310 91.122  1.00 96.70  ?  38  ASP A OD1  1 
ATOM   409   O OD2  . ASP A 1 29  ? 62.018  -21.114 90.707  1.00 96.15  -1 38  ASP A OD2  1 
ATOM   410   H H    . ASP A 1 29  ? 59.511  -23.520 88.747  1.00 108.11 ?  38  ASP A H    1 
ATOM   411   H HA   . ASP A 1 29  ? 59.939  -24.303 91.259  1.00 107.03 ?  38  ASP A HA   1 
ATOM   412   H HB2  . ASP A 1 29  ? 59.603  -21.762 90.116  1.00 118.87 ?  38  ASP A HB2  1 
ATOM   413   H HB3  . ASP A 1 29  ? 59.602  -21.922 91.698  1.00 118.87 ?  38  ASP A HB3  1 
ATOM   414   N N    . TRP A 1 30  ? 57.001  -23.459 90.414  1.00 86.14  ?  39  TRP A N    1 
ATOM   415   C CA   . TRP A 1 30  ? 55.614  -23.624 90.808  1.00 53.82  ?  39  TRP A CA   1 
ATOM   416   C C    . TRP A 1 30  ? 55.317  -25.102 91.000  1.00 57.33  ?  39  TRP A C    1 
ATOM   417   O O    . TRP A 1 30  ? 54.858  -25.534 92.074  1.00 62.23  ?  39  TRP A O    1 
ATOM   418   C CB   . TRP A 1 30  ? 54.705  -23.059 89.727  1.00 51.60  ?  39  TRP A CB   1 
ATOM   419   C CG   . TRP A 1 30  ? 54.612  -21.532 89.517  1.00 51.37  ?  39  TRP A CG   1 
ATOM   420   C CD1  . TRP A 1 30  ? 55.085  -20.552 90.315  1.00 52.16  ?  39  TRP A CD1  1 
ATOM   421   C CD2  . TRP A 1 30  ? 54.031  -20.874 88.397  1.00 99.27  ?  39  TRP A CD2  1 
ATOM   422   N NE1  . TRP A 1 30  ? 54.817  -19.309 89.779  1.00 67.36  ?  39  TRP A NE1  1 
ATOM   423   C CE2  . TRP A 1 30  ? 54.170  -19.484 88.595  1.00 72.72  ?  39  TRP A CE2  1 
ATOM   424   C CE3  . TRP A 1 30  ? 53.390  -21.321 87.257  1.00 51.09  ?  39  TRP A CE3  1 
ATOM   425   C CZ2  . TRP A 1 30  ? 53.678  -18.531 87.692  1.00 151.57 ?  39  TRP A CZ2  1 
ATOM   426   C CZ3  . TRP A 1 30  ? 52.878  -20.339 86.343  1.00 62.90  ?  39  TRP A CZ3  1 
ATOM   427   C CH2  . TRP A 1 30  ? 53.045  -18.986 86.576  1.00 109.74 ?  39  TRP A CH2  1 
ATOM   428   H H    . TRP A 1 30  ? 57.116  -23.140 89.624  1.00 103.37 ?  39  TRP A H    1 
ATOM   429   H HA   . TRP A 1 30  ? 55.446  -23.156 91.640  1.00 64.58  ?  39  TRP A HA   1 
ATOM   430   H HB2  . TRP A 1 30  ? 54.991  -23.435 88.880  1.00 61.92  ?  39  TRP A HB2  1 
ATOM   431   H HB3  . TRP A 1 30  ? 53.805  -23.365 89.915  1.00 61.92  ?  39  TRP A HB3  1 
ATOM   432   H HD1  . TRP A 1 30  ? 55.533  -20.695 91.118  1.00 62.59  ?  39  TRP A HD1  1 
ATOM   433   H HE1  . TRP A 1 30  ? 55.031  -18.553 90.129  1.00 80.83  ?  39  TRP A HE1  1 
ATOM   434   H HE3  . TRP A 1 30  ? 53.268  -22.230 87.101  1.00 61.31  ?  39  TRP A HE3  1 
ATOM   435   H HZ2  . TRP A 1 30  ? 53.785  -17.620 87.847  1.00 181.88 ?  39  TRP A HZ2  1 
ATOM   436   H HZ3  . TRP A 1 30  ? 52.451  -20.619 85.565  1.00 75.48  ?  39  TRP A HZ3  1 
ATOM   437   H HH2  . TRP A 1 30  ? 52.718  -18.373 85.957  1.00 131.68 ?  39  TRP A HH2  1 
ATOM   438   N N    . MET A 1 31  ? 55.676  -25.907 89.994  1.00 62.16  ?  40  MET A N    1 
ATOM   439   C CA   . MET A 1 31  ? 55.363  -27.326 90.019  1.00 81.28  ?  40  MET A CA   1 
ATOM   440   C C    . MET A 1 31  ? 55.870  -28.003 91.285  1.00 84.84  ?  40  MET A C    1 
ATOM   441   O O    . MET A 1 31  ? 55.214  -28.922 91.785  1.00 103.15 ?  40  MET A O    1 
ATOM   442   C CB   . MET A 1 31  ? 55.947  -28.002 88.786  1.00 81.02  ?  40  MET A CB   1 
ATOM   443   C CG   . MET A 1 31  ? 55.345  -29.373 88.580  1.00 92.48  ?  40  MET A CG   1 
ATOM   444   S SD   . MET A 1 31  ? 53.620  -29.256 88.017  1.00 79.14  ?  40  MET A SD   1 
ATOM   445   C CE   . MET A 1 31  ? 53.877  -29.076 86.264  1.00 121.40 ?  40  MET A CE   1 
ATOM   446   H H    . MET A 1 31  ? 56.100  -25.650 89.291  1.00 74.59  ?  40  MET A H    1 
ATOM   447   H HA   . MET A 1 31  ? 54.400  -27.430 89.980  1.00 97.53  ?  40  MET A HA   1 
ATOM   448   H HB2  . MET A 1 31  ? 55.754  -27.463 88.003  1.00 97.22  ?  40  MET A HB2  1 
ATOM   449   H HB3  . MET A 1 31  ? 56.905  -28.102 88.898  1.00 97.22  ?  40  MET A HB3  1 
ATOM   450   H HG2  . MET A 1 31  ? 55.855  -29.849 87.905  1.00 110.98 ?  40  MET A HG2  1 
ATOM   451   H HG3  . MET A 1 31  ? 55.360  -29.860 89.418  1.00 110.98 ?  40  MET A HG3  1 
ATOM   452   H HE1  . MET A 1 31  ? 53.015  -29.000 85.825  1.00 145.68 ?  40  MET A HE1  1 
ATOM   453   H HE2  . MET A 1 31  ? 54.402  -28.276 86.103  1.00 145.68 ?  40  MET A HE2  1 
ATOM   454   H HE3  . MET A 1 31  ? 54.351  -29.855 85.933  1.00 145.68 ?  40  MET A HE3  1 
ATOM   455   N N    . PHE A 1 32  ? 57.006  -27.545 91.836  1.00 73.04  ?  41  PHE A N    1 
ATOM   456   C CA   . PHE A 1 32  ? 57.615  -28.237 92.974  1.00 66.28  ?  41  PHE A CA   1 
ATOM   457   C C    . PHE A 1 32  ? 56.781  -28.068 94.246  1.00 86.00  ?  41  PHE A C    1 
ATOM   458   O O    . PHE A 1 32  ? 56.771  -28.956 95.112  1.00 77.64  ?  41  PHE A O    1 
ATOM   459   C CB   . PHE A 1 32  ? 59.054  -27.782 93.210  1.00 57.30  ?  41  PHE A CB   1 
ATOM   460   C CG   . PHE A 1 32  ? 59.551  -28.169 94.580  1.00 58.50  ?  41  PHE A CG   1 
ATOM   461   C CD1  . PHE A 1 32  ? 59.941  -29.469 94.855  1.00 60.30  ?  41  PHE A CD1  1 
ATOM   462   C CD2  . PHE A 1 32  ? 59.550  -27.259 95.621  1.00 58.04  ?  41  PHE A CD2  1 
ATOM   463   C CE1  . PHE A 1 32  ? 60.368  -29.839 96.129  1.00 119.05 ?  41  PHE A CE1  1 
ATOM   464   C CE2  . PHE A 1 32  ? 59.965  -27.636 96.909  1.00 59.40  ?  41  PHE A CE2  1 
ATOM   465   C CZ   . PHE A 1 32  ? 60.385  -28.925 97.150  1.00 98.80  ?  41  PHE A CZ   1 
ATOM   466   H H    . PHE A 1 32  ? 57.434  -26.848 91.572  1.00 87.65  ?  41  PHE A H    1 
ATOM   467   H HA   . PHE A 1 32  ? 57.642  -29.185 92.772  1.00 79.54  ?  41  PHE A HA   1 
ATOM   468   H HB2  . PHE A 1 32  ? 59.631  -28.198 92.551  1.00 68.76  ?  41  PHE A HB2  1 
ATOM   469   H HB3  . PHE A 1 32  ? 59.099  -26.816 93.133  1.00 68.76  ?  41  PHE A HB3  1 
ATOM   470   H HD1  . PHE A 1 32  ? 59.941  -30.100 94.172  1.00 72.35  ?  41  PHE A HD1  1 
ATOM   471   H HD2  . PHE A 1 32  ? 59.273  -26.385 95.466  1.00 69.64  ?  41  PHE A HD2  1 
ATOM   472   H HE1  . PHE A 1 32  ? 60.643  -30.713 96.287  1.00 142.86 ?  41  PHE A HE1  1 
ATOM   473   H HE2  . PHE A 1 32  ? 59.980  -27.007 97.595  1.00 71.28  ?  41  PHE A HE2  1 
ATOM   474   H HZ   . PHE A 1 32  ? 60.668  -29.175 98.000  1.00 118.56 ?  41  PHE A HZ   1 
ATOM   475   N N    . ILE A 1 33  ? 56.220  -26.881 94.442  1.00 72.01  ?  42  ILE A N    1 
ATOM   476   C CA   . ILE A 1 33  ? 55.347  -26.612 95.582  1.00 120.82 ?  42  ILE A CA   1 
ATOM   477   C C    . ILE A 1 33  ? 54.023  -27.392 95.493  1.00 100.71 ?  42  ILE A C    1 
ATOM   478   O O    . ILE A 1 33  ? 53.587  -28.038 96.454  1.00 56.08  ?  42  ILE A O    1 
ATOM   479   C CB   . ILE A 1 33  ? 55.125  -25.099 95.650  1.00 93.54  ?  42  ILE A CB   1 
ATOM   480   C CG1  . ILE A 1 33  ? 56.491  -24.481 95.961  1.00 51.04  ?  42  ILE A CG1  1 
ATOM   481   C CG2  . ILE A 1 33  ? 54.000  -24.753 96.609  1.00 82.92  ?  42  ILE A CG2  1 
ATOM   482   C CD1  . ILE A 1 33  ? 56.579  -23.029 95.817  1.00 51.18  ?  42  ILE A CD1  1 
ATOM   483   H H    . ILE A 1 33  ? 56.330  -26.204 93.923  1.00 86.41  ?  42  ILE A H    1 
ATOM   484   H HA   . ILE A 1 33  ? 55.799  -26.885 96.396  1.00 144.99 ?  42  ILE A HA   1 
ATOM   485   H HB   . ILE A 1 33  ? 54.860  -24.799 94.767  1.00 112.25 ?  42  ILE A HB   1 
ATOM   486   H HG12 . ILE A 1 33  ? 56.722  -24.695 96.879  1.00 61.24  ?  42  ILE A HG12 1 
ATOM   487   H HG13 . ILE A 1 33  ? 57.147  -24.871 95.364  1.00 61.24  ?  42  ILE A HG13 1 
ATOM   488   H HG21 . ILE A 1 33  ? 53.887  -23.789 96.628  1.00 99.50  ?  42  ILE A HG21 1 
ATOM   489   H HG22 . ILE A 1 33  ? 53.183  -25.176 96.303  1.00 99.50  ?  42  ILE A HG22 1 
ATOM   490   H HG23 . ILE A 1 33  ? 54.230  -25.076 97.494  1.00 99.50  ?  42  ILE A HG23 1 
ATOM   491   H HD11 . ILE A 1 33  ? 57.479  -22.744 96.037  1.00 61.42  ?  42  ILE A HD11 1 
ATOM   492   H HD12 . ILE A 1 33  ? 56.370  -22.790 94.901  1.00 61.42  ?  42  ILE A HD12 1 
ATOM   493   H HD13 . ILE A 1 33  ? 55.943  -22.613 96.421  1.00 61.42  ?  42  ILE A HD13 1 
ATOM   494   N N    . ALA A 1 34  ? 53.349  -27.318 94.345  1.00 69.75  ?  43  ALA A N    1 
ATOM   495   C CA   . ALA A 1 34  ? 52.069  -27.972 94.170  1.00 68.42  ?  43  ALA A CA   1 
ATOM   496   C C    . ALA A 1 34  ? 52.229  -29.463 94.322  1.00 100.22 ?  43  ALA A C    1 
ATOM   497   O O    . ALA A 1 34  ? 51.286  -30.187 94.749  1.00 50.70  ?  43  ALA A O    1 
ATOM   498   C CB   . ALA A 1 34  ? 51.547  -27.669 92.790  1.00 82.39  ?  43  ALA A CB   1 
ATOM   499   H H    . ALA A 1 34  ? 53.621  -26.890 93.650  1.00 83.70  ?  43  ALA A H    1 
ATOM   500   H HA   . ALA A 1 34  ? 51.435  -27.649 94.830  1.00 82.10  ?  43  ALA A HA   1 
ATOM   501   H HB1  . ALA A 1 34  ? 50.690  -28.107 92.674  1.00 98.87  ?  43  ALA A HB1  1 
ATOM   502   H HB2  . ALA A 1 34  ? 51.444  -26.709 92.695  1.00 98.87  ?  43  ALA A HB2  1 
ATOM   503   H HB3  . ALA A 1 34  ? 52.180  -28.000 92.134  1.00 98.87  ?  43  ALA A HB3  1 
ATOM   504   N N    . LYS A 1 35  ? 53.408  -29.955 93.946  1.00 90.43  ?  44  LYS A N    1 
ATOM   505   C CA   . LYS A 1 35  ? 53.575  -31.371 94.093  1.00 48.85  ?  44  LYS A CA   1 
ATOM   506   C C    . LYS A 1 35  ? 53.806  -31.786 95.536  1.00 49.87  ?  44  LYS A C    1 
ATOM   507   O O    . LYS A 1 35  ? 53.731  -32.991 95.854  1.00 57.05  ?  44  LYS A O    1 
ATOM   508   C CB   . LYS A 1 35  ? 54.663  -31.884 93.189  1.00 73.04  ?  44  LYS A CB   1 
ATOM   509   C CG   . LYS A 1 35  ? 54.266  -31.923 91.722  1.00 64.54  ?  44  LYS A CG   1 
ATOM   510   C CD   . LYS A 1 35  ? 53.351  -33.079 91.396  1.00 106.27 ?  44  LYS A CD   1 
ATOM   511   C CE   . LYS A 1 35  ? 52.903  -33.072 89.925  1.00 101.68 ?  44  LYS A CE   1 
ATOM   512   N NZ   . LYS A 1 35  ? 51.850  -34.104 89.626  1.00 70.84  1  44  LYS A NZ   1 
ATOM   513   H H    . LYS A 1 35  ? 54.075  -29.516 93.626  1.00 108.51 ?  44  LYS A H    1 
ATOM   514   H HA   . LYS A 1 35  ? 52.751  -31.796 93.809  1.00 58.62  ?  44  LYS A HA   1 
ATOM   515   H HB2  . LYS A 1 35  ? 55.438  -31.307 93.272  1.00 87.65  ?  44  LYS A HB2  1 
ATOM   516   H HB3  . LYS A 1 35  ? 54.894  -32.787 93.458  1.00 87.65  ?  44  LYS A HB3  1 
ATOM   517   H HG2  . LYS A 1 35  ? 53.803  -31.101 91.498  1.00 77.45  ?  44  LYS A HG2  1 
ATOM   518   H HG3  . LYS A 1 35  ? 55.066  -32.011 91.180  1.00 77.45  ?  44  LYS A HG3  1 
ATOM   519   H HD2  . LYS A 1 35  ? 53.820  -33.912 91.564  1.00 127.53 ?  44  LYS A HD2  1 
ATOM   520   H HD3  . LYS A 1 35  ? 52.559  -33.024 91.953  1.00 127.53 ?  44  LYS A HD3  1 
ATOM   521   H HE2  . LYS A 1 35  ? 52.536  -32.200 89.711  1.00 122.02 ?  44  LYS A HE2  1 
ATOM   522   H HE3  . LYS A 1 35  ? 53.670  -33.256 89.360  1.00 122.02 ?  44  LYS A HE3  1 
ATOM   523   H HZ1  . LYS A 1 35  ? 51.621  -34.064 88.767  1.00 85.01  ?  44  LYS A HZ1  1 
ATOM   524   H HZ2  . LYS A 1 35  ? 52.163  -34.918 89.805  1.00 85.01  ?  44  LYS A HZ2  1 
ATOM   525   H HZ3  . LYS A 1 35  ? 51.128  -33.955 90.125  1.00 85.01  ?  44  LYS A HZ3  1 
ATOM   526   N N    . HIS A 1 36  ? 53.973  -30.844 96.439  1.00 59.64  ?  45  HIS A N    1 
ATOM   527   C CA   . HIS A 1 36  ? 54.388  -31.220 97.779  1.00 58.95  ?  45  HIS A CA   1 
ATOM   528   C C    . HIS A 1 36  ? 53.674  -30.409 98.824  1.00 91.56  ?  45  HIS A C    1 
ATOM   529   O O    . HIS A 1 36  ? 54.227  -30.163 99.906  1.00 102.85 ?  45  HIS A O    1 
ATOM   530   C CB   . HIS A 1 36  ? 55.892  -31.031 97.966  1.00 73.28  ?  45  HIS A CB   1 
ATOM   531   C CG   . HIS A 1 36  ? 56.724  -31.877 97.058  1.00 71.26  ?  45  HIS A CG   1 
ATOM   532   N ND1  . HIS A 1 36  ? 57.165  -31.446 95.824  1.00 81.30  ?  45  HIS A ND1  1 
ATOM   533   C CD2  . HIS A 1 36  ? 57.135  -33.157 97.170  1.00 58.24  ?  45  HIS A CD2  1 
ATOM   534   C CE1  . HIS A 1 36  ? 57.859  -32.410 95.242  1.00 119.89 ?  45  HIS A CE1  1 
ATOM   535   N NE2  . HIS A 1 36  ? 57.860  -33.456 96.042  1.00 102.56 ?  45  HIS A NE2  1 
ATOM   536   H H    . HIS A 1 36  ? 53.859  -30.002 96.311  1.00 71.57  ?  45  HIS A H    1 
ATOM   537   H HA   . HIS A 1 36  ? 54.180  -32.156 97.926  1.00 70.74  ?  45  HIS A HA   1 
ATOM   538   H HB2  . HIS A 1 36  ? 56.115  -30.102 97.793  1.00 87.94  ?  45  HIS A HB2  1 
ATOM   539   H HB3  . HIS A 1 36  ? 56.125  -31.259 98.880  1.00 87.94  ?  45  HIS A HB3  1 
ATOM   540   H HD1  . HIS A 1 36  ? 57.036  -30.661 95.497  1.00 97.56  ?  45  HIS A HD1  1 
ATOM   541   H HD2  . HIS A 1 36  ? 56.991  -33.718 97.897  1.00 69.89  ?  45  HIS A HD2  1 
ATOM   542   H HE1  . HIS A 1 36  ? 58.270  -32.360 94.409  1.00 143.86 ?  45  HIS A HE1  1 
ATOM   543   N N    . LEU A 1 37  ? 52.472  -29.950 98.528  1.00 69.16  ?  46  LEU A N    1 
ATOM   544   C CA   . LEU A 1 37  ? 51.744  -29.211 99.542  1.00 55.90  ?  46  LEU A CA   1 
ATOM   545   C C    . LEU A 1 37  ? 51.664  -29.960 100.865 1.00 70.05  ?  46  LEU A C    1 
ATOM   546   O O    . LEU A 1 37  ? 51.899  -29.344 101.922 1.00 88.05  ?  46  LEU A O    1 
ATOM   547   C CB   . LEU A 1 37  ? 50.348  -28.910 98.998  1.00 77.40  ?  46  LEU A CB   1 
ATOM   548   C CG   . LEU A 1 37  ? 50.379  -28.044 97.750  1.00 62.12  ?  46  LEU A CG   1 
ATOM   549   C CD1  . LEU A 1 37  ? 48.942  -28.037 97.147  1.00 50.97  ?  46  LEU A CD1  1 
ATOM   550   C CD2  . LEU A 1 37  ? 50.865  -26.617 98.102  1.00 43.44  ?  46  LEU A CD2  1 
ATOM   551   H H    . LEU A 1 37  ? 52.067  -30.046 97.776  1.00 83.00  ?  46  LEU A H    1 
ATOM   552   H HA   . LEU A 1 37  ? 52.193  -28.366 99.703  1.00 67.08  ?  46  LEU A HA   1 
ATOM   553   H HB2  . LEU A 1 37  ? 49.910  -29.746 98.773  1.00 92.88  ?  46  LEU A HB2  1 
ATOM   554   H HB3  . LEU A 1 37  ? 49.839  -28.440 99.677  1.00 92.88  ?  46  LEU A HB3  1 
ATOM   555   H HG   . LEU A 1 37  ? 50.987  -28.429 97.099  1.00 74.54  ?  46  LEU A HG   1 
ATOM   556   H HD11 . LEU A 1 37  ? 48.938  -27.489 96.347  1.00 61.17  ?  46  LEU A HD11 1 
ATOM   557   H HD12 . LEU A 1 37  ? 48.688  -28.947 96.927  1.00 61.17  ?  46  LEU A HD12 1 
ATOM   558   H HD13 . LEU A 1 37  ? 48.327  -27.672 97.802  1.00 61.17  ?  46  LEU A HD13 1 
ATOM   559   H HD21 . LEU A 1 37  ? 50.878  -26.080 97.294  1.00 52.12  ?  46  LEU A HD21 1 
ATOM   560   H HD22 . LEU A 1 37  ? 50.257  -26.227 98.749  1.00 52.12  ?  46  LEU A HD22 1 
ATOM   561   H HD23 . LEU A 1 37  ? 51.758  -26.671 98.478  1.00 52.12  ?  46  LEU A HD23 1 
ATOM   562   N N    . PRO A 1 38  ? 51.410  -31.256 100.880 1.00 74.22  ?  47  PRO A N    1 
ATOM   563   C CA   . PRO A 1 38  ? 51.366  -31.954 102.161 1.00 115.66 ?  47  PRO A CA   1 
ATOM   564   C C    . PRO A 1 38  ? 52.604  -31.761 102.976 1.00 81.50  ?  47  PRO A C    1 
ATOM   565   O O    . PRO A 1 38  ? 52.534  -31.326 104.128 1.00 103.46 ?  47  PRO A O    1 
ATOM   566   C CB   . PRO A 1 38  ? 51.198  -33.393 101.750 1.00 51.71  ?  47  PRO A CB   1 
ATOM   567   C CG   . PRO A 1 38  ? 50.467  -33.330 100.341 1.00 49.19  ?  47  PRO A CG   1 
ATOM   568   C CD   . PRO A 1 38  ? 50.986  -32.091 99.735  1.00 48.41  ?  47  PRO A CD   1 
ATOM   569   H HA   . PRO A 1 38  ? 50.593  -31.672 102.675 1.00 138.79 ?  47  PRO A HA   1 
ATOM   570   H HB2  . PRO A 1 38  ? 52.068  -33.814 101.667 1.00 62.05  ?  47  PRO A HB2  1 
ATOM   571   H HB3  . PRO A 1 38  ? 50.650  -33.858 102.401 1.00 62.05  ?  47  PRO A HB3  1 
ATOM   572   H HG2  . PRO A 1 38  ? 50.706  -34.104 99.809  1.00 59.03  ?  47  PRO A HG2  1 
ATOM   573   H HG3  . PRO A 1 38  ? 49.506  -33.278 100.469 1.00 59.03  ?  47  PRO A HG3  1 
ATOM   574   H HD2  . PRO A 1 38  ? 51.746  -32.290 99.167  1.00 58.09  ?  47  PRO A HD2  1 
ATOM   575   H HD3  . PRO A 1 38  ? 50.284  -31.643 99.238  1.00 58.09  ?  47  PRO A HD3  1 
ATOM   576   N N    . ASP A 1 39  ? 53.756  -32.037 102.386 1.00 73.18  ?  48  ASP A N    1 
ATOM   577   C CA   . ASP A 1 39  ? 55.004  -31.962 103.131 1.00 77.97  ?  48  ASP A CA   1 
ATOM   578   C C    . ASP A 1 39  ? 55.295  -30.534 103.565 1.00 79.43  ?  48  ASP A C    1 
ATOM   579   O O    . ASP A 1 39  ? 55.551  -30.268 104.746 1.00 89.80  ?  48  ASP A O    1 
ATOM   580   C CB   . ASP A 1 39  ? 56.113  -32.536 102.263 1.00 85.78  ?  48  ASP A CB   1 
ATOM   581   C CG   . ASP A 1 39  ? 55.737  -33.884 101.674 1.00 102.22 ?  48  ASP A CG   1 
ATOM   582   O OD1  . ASP A 1 39  ? 55.010  -34.625 102.358 1.00 104.32 ?  48  ASP A OD1  1 
ATOM   583   O OD2  . ASP A 1 39  ? 56.134  -34.192 100.537 1.00 148.94 -1 48  ASP A OD2  1 
ATOM   584   H H    . ASP A 1 39  ? 53.844  -32.268 101.562 1.00 87.82  ?  48  ASP A H    1 
ATOM   585   H HA   . ASP A 1 39  ? 54.931  -32.509 103.929 1.00 93.56  ?  48  ASP A HA   1 
ATOM   586   H HB2  . ASP A 1 39  ? 56.292  -31.926 101.530 1.00 102.94 ?  48  ASP A HB2  1 
ATOM   587   H HB3  . ASP A 1 39  ? 56.911  -32.654 102.802 1.00 102.94 ?  48  ASP A HB3  1 
ATOM   588   N N    . LEU A 1 40  ? 55.145  -29.590 102.645 1.00 79.62  ?  49  LEU A N    1 
ATOM   589   C CA   . LEU A 1 40  ? 55.480  -28.212 102.947 1.00 63.67  ?  49  LEU A CA   1 
ATOM   590   C C    . LEU A 1 40  ? 54.540  -27.614 103.967 1.00 83.18  ?  49  LEU A C    1 
ATOM   591   O O    . LEU A 1 40  ? 54.924  -26.711 104.719 1.00 55.66  ?  49  LEU A O    1 
ATOM   592   C CB   . LEU A 1 40  ? 55.449  -27.389 101.689 1.00 53.30  ?  49  LEU A CB   1 
ATOM   593   C CG   . LEU A 1 40  ? 56.481  -27.857 100.670 1.00 64.92  ?  49  LEU A CG   1 
ATOM   594   C CD1  . LEU A 1 40  ? 56.374  -27.069 99.434  1.00 52.95  ?  49  LEU A CD1  1 
ATOM   595   C CD2  . LEU A 1 40  ? 57.839  -27.829 101.208 1.00 57.44  ?  49  LEU A CD2  1 
ATOM   596   H H    . LEU A 1 40  ? 54.854  -29.722 101.846 1.00 95.54  ?  49  LEU A H    1 
ATOM   597   H HA   . LEU A 1 40  ? 56.379  -28.176 103.309 1.00 76.40  ?  49  LEU A HA   1 
ATOM   598   H HB2  . LEU A 1 40  ? 54.571  -27.460 101.284 1.00 63.96  ?  49  LEU A HB2  1 
ATOM   599   H HB3  . LEU A 1 40  ? 55.641  -26.464 101.910 1.00 63.96  ?  49  LEU A HB3  1 
ATOM   600   H HG   . LEU A 1 40  ? 56.283  -28.779 100.441 1.00 77.90  ?  49  LEU A HG   1 
ATOM   601   H HD11 . LEU A 1 40  ? 57.038  -27.383 98.801  1.00 63.55  ?  49  LEU A HD11 1 
ATOM   602   H HD12 . LEU A 1 40  ? 55.484  -27.181 99.064  1.00 63.55  ?  49  LEU A HD12 1 
ATOM   603   H HD13 . LEU A 1 40  ? 56.530  -26.134 99.642  1.00 63.55  ?  49  LEU A HD13 1 
ATOM   604   H HD21 . LEU A 1 40  ? 58.455  -28.135 100.524 1.00 68.93  ?  49  LEU A HD21 1 
ATOM   605   H HD22 . LEU A 1 40  ? 58.057  -26.920 101.467 1.00 68.93  ?  49  LEU A HD22 1 
ATOM   606   H HD23 . LEU A 1 40  ? 57.885  -28.414 101.980 1.00 68.93  ?  49  LEU A HD23 1 
ATOM   607   N N    . ILE A 1 41  ? 53.299  -28.058 103.992 1.00 52.91  ?  50  ILE A N    1 
ATOM   608   C CA   . ILE A 1 41  ? 52.421  -27.591 105.047 1.00 52.93  ?  50  ILE A CA   1 
ATOM   609   C C    . ILE A 1 41  ? 52.859  -28.151 106.386 1.00 55.86  ?  50  ILE A C    1 
ATOM   610   O O    . ILE A 1 41  ? 53.118  -27.415 107.338 1.00 63.82  ?  50  ILE A O    1 
ATOM   611   C CB   . ILE A 1 41  ? 50.977  -27.997 104.703 1.00 55.16  ?  50  ILE A CB   1 
ATOM   612   C CG1  . ILE A 1 41  ? 50.530  -27.173 103.516 1.00 48.33  ?  50  ILE A CG1  1 
ATOM   613   C CG2  . ILE A 1 41  ? 49.985  -27.798 105.873 1.00 63.36  ?  50  ILE A CG2  1 
ATOM   614   C CD1  . ILE A 1 41  ? 49.192  -27.625 102.972 1.00 46.35  ?  50  ILE A CD1  1 
ATOM   615   H H    . ILE A 1 41  ? 52.948  -28.610 103.433 1.00 63.49  ?  50  ILE A H    1 
ATOM   616   H HA   . ILE A 1 41  ? 52.462  -26.623 105.094 1.00 63.51  ?  50  ILE A HA   1 
ATOM   617   H HB   . ILE A 1 41  ? 50.971  -28.933 104.449 1.00 66.20  ?  50  ILE A HB   1 
ATOM   618   H HG12 . ILE A 1 41  ? 50.447  -26.245 103.787 1.00 58.00  ?  50  ILE A HG12 1 
ATOM   619   H HG13 . ILE A 1 41  ? 51.187  -27.256 102.807 1.00 58.00  ?  50  ILE A HG13 1 
ATOM   620   H HG21 . ILE A 1 41  ? 49.100  -28.073 105.586 1.00 76.03  ?  50  ILE A HG21 1 
ATOM   621   H HG22 . ILE A 1 41  ? 50.272  -28.339 106.625 1.00 76.03  ?  50  ILE A HG22 1 
ATOM   622   H HG23 . ILE A 1 41  ? 49.976  -26.861 106.123 1.00 76.03  ?  50  ILE A HG23 1 
ATOM   623   H HD11 . ILE A 1 41  ? 48.954  -27.066 102.216 1.00 55.62  ?  50  ILE A HD11 1 
ATOM   624   H HD12 . ILE A 1 41  ? 49.263  -28.551 102.691 1.00 55.62  ?  50  ILE A HD12 1 
ATOM   625   H HD13 . ILE A 1 41  ? 48.524  -27.541 103.670 1.00 55.62  ?  50  ILE A HD13 1 
ATOM   626   N N    . GLU A 1 42  ? 52.984  -29.465 106.464 1.00 86.66  ?  51  GLU A N    1 
ATOM   627   C CA   . GLU A 1 42  ? 53.221  -30.068 107.753 1.00 64.88  ?  51  GLU A CA   1 
ATOM   628   C C    . GLU A 1 42  ? 54.515  -29.574 108.331 1.00 70.60  ?  51  GLU A C    1 
ATOM   629   O O    . GLU A 1 42  ? 54.665  -29.478 109.555 1.00 65.04  ?  51  GLU A O    1 
ATOM   630   C CB   . GLU A 1 42  ? 53.190  -31.556 107.606 1.00 90.51  ?  51  GLU A CB   1 
ATOM   631   C CG   . GLU A 1 42  ? 51.805  -32.123 107.680 1.00 112.31 ?  51  GLU A CG   1 
ATOM   632   C CD   . GLU A 1 42  ? 51.817  -33.490 108.312 1.00 135.17 ?  51  GLU A CD   1 
ATOM   633   O OE1  . GLU A 1 42  ? 52.529  -34.365 107.781 1.00 140.49 ?  51  GLU A OE1  1 
ATOM   634   O OE2  . GLU A 1 42  ? 51.156  -33.679 109.359 1.00 140.63 -1 51  GLU A OE2  1 
ATOM   635   H H    . GLU A 1 42  ? 52.936  -30.014 105.804 1.00 103.99 ?  51  GLU A H    1 
ATOM   636   H HA   . GLU A 1 42  ? 52.507  -29.812 108.357 1.00 77.85  ?  51  GLU A HA   1 
ATOM   637   H HB2  . GLU A 1 42  ? 53.565  -31.795 106.744 1.00 108.61 ?  51  GLU A HB2  1 
ATOM   638   H HB3  . GLU A 1 42  ? 53.714  -31.954 108.317 1.00 108.61 ?  51  GLU A HB3  1 
ATOM   639   H HG2  . GLU A 1 42  ? 51.248  -31.541 108.220 1.00 134.78 ?  51  GLU A HG2  1 
ATOM   640   H HG3  . GLU A 1 42  ? 51.442  -32.203 106.784 1.00 134.78 ?  51  GLU A HG3  1 
ATOM   641   N N    . SER A 1 43  ? 55.465  -29.269 107.464 1.00 67.18  ?  52  SER A N    1 
ATOM   642   C CA   . SER A 1 43  ? 56.699  -28.690 107.945 1.00 84.79  ?  52  SER A CA   1 
ATOM   643   C C    . SER A 1 43  ? 56.452  -27.302 108.513 1.00 92.29  ?  52  SER A C    1 
ATOM   644   O O    . SER A 1 43  ? 56.998  -26.955 109.573 1.00 97.03  ?  52  SER A O    1 
ATOM   645   C CB   . SER A 1 43  ? 57.702  -28.619 106.807 1.00 81.70  ?  52  SER A CB   1 
ATOM   646   O OG   . SER A 1 43  ? 58.521  -27.494 107.016 1.00 86.24  ?  52  SER A OG   1 
ATOM   647   H H    . SER A 1 43  ? 55.422  -29.385 106.613 1.00 80.62  ?  52  SER A H    1 
ATOM   648   H HA   . SER A 1 43  ? 57.068  -29.249 108.647 1.00 101.74 ?  52  SER A HA   1 
ATOM   649   H HB2  . SER A 1 43  ? 58.248  -29.421 106.804 1.00 98.04  ?  52  SER A HB2  1 
ATOM   650   H HB3  . SER A 1 43  ? 57.231  -28.524 105.964 1.00 98.04  ?  52  SER A HB3  1 
ATOM   651   H HG   . SER A 1 43  ? 59.087  -27.432 106.399 1.00 103.49 ?  52  SER A HG   1 
ATOM   652   N N    . GLY A 1 44  ? 55.578  -26.527 107.862 1.00 68.23  ?  53  GLY A N    1 
ATOM   653   C CA   . GLY A 1 44  ? 55.390  -25.145 108.210 1.00 82.67  ?  53  GLY A CA   1 
ATOM   654   C C    . GLY A 1 44  ? 56.255  -24.274 107.365 1.00 87.18  ?  53  GLY A C    1 
ATOM   655   O O    . GLY A 1 44  ? 56.656  -23.202 107.805 1.00 96.51  ?  53  GLY A O    1 
ATOM   656   H H    . GLY A 1 44  ? 55.083  -26.794 107.211 1.00 81.87  ?  53  GLY A H    1 
ATOM   657   H HA2  . GLY A 1 44  ? 54.463  -24.893 108.075 1.00 99.20  ?  53  GLY A HA2  1 
ATOM   658   H HA3  . GLY A 1 44  ? 55.620  -25.005 109.142 1.00 99.20  ?  53  GLY A HA3  1 
ATOM   659   N N    . GLN A 1 45  ? 56.629  -24.755 106.196 1.00 128.29 ?  54  GLN A N    1 
ATOM   660   C CA   . GLN A 1 45  ? 57.473  -24.009 105.294 1.00 66.86  ?  54  GLN A CA   1 
ATOM   661   C C    . GLN A 1 45  ? 56.788  -23.825 103.962 1.00 69.41  ?  54  GLN A C    1 
ATOM   662   O O    . GLN A 1 45  ? 57.457  -23.638 102.949 1.00 88.19  ?  54  GLN A O    1 
ATOM   663   C CB   . GLN A 1 45  ? 58.832  -24.679 105.152 1.00 122.16 ?  54  GLN A CB   1 
ATOM   664   C CG   . GLN A 1 45  ? 59.657  -24.527 106.445 1.00 154.24 ?  54  GLN A CG   1 
ATOM   665   C CD   . GLN A 1 45  ? 61.120  -24.875 106.288 1.00 179.91 ?  54  GLN A CD   1 
ATOM   666   O OE1  . GLN A 1 45  ? 61.480  -25.762 105.525 1.00 176.43 ?  54  GLN A OE1  1 
ATOM   667   N NE2  . GLN A 1 45  ? 61.971  -24.177 107.018 1.00 202.62 ?  54  GLN A NE2  1 
ATOM   668   H H    . GLN A 1 45  ? 56.402  -25.529 105.898 1.00 153.95 ?  54  GLN A H    1 
ATOM   669   H HA   . GLN A 1 45  ? 57.621  -23.127 105.669 1.00 80.23  ?  54  GLN A HA   1 
ATOM   670   H HB2  . GLN A 1 45  ? 58.708  -25.625 104.978 1.00 146.60 ?  54  GLN A HB2  1 
ATOM   671   H HB3  . GLN A 1 45  ? 59.323  -24.264 104.426 1.00 146.60 ?  54  GLN A HB3  1 
ATOM   672   H HG2  . GLN A 1 45  ? 59.603  -23.606 106.743 1.00 185.08 ?  54  GLN A HG2  1 
ATOM   673   H HG3  . GLN A 1 45  ? 59.286  -25.113 107.123 1.00 185.08 ?  54  GLN A HG3  1 
ATOM   674   H HE21 . GLN A 1 45  ? 61.682  -23.563 107.546 1.00 243.14 ?  54  GLN A HE21 1 
ATOM   675   H HE22 . GLN A 1 45  ? 62.814  -24.336 106.965 1.00 243.14 ?  54  GLN A HE22 1 
ATOM   676   N N    . LEU A 1 46  ? 55.464  -23.971 103.923 1.00 97.23  ?  55  LEU A N    1 
ATOM   677   C CA   . LEU A 1 46  ? 54.754  -23.690 102.682 1.00 80.03  ?  55  LEU A CA   1 
ATOM   678   C C    . LEU A 1 46  ? 54.769  -22.190 102.366 1.00 76.14  ?  55  LEU A C    1 
ATOM   679   O O    . LEU A 1 46  ? 55.098  -21.768 101.252 1.00 75.69  ?  55  LEU A O    1 
ATOM   680   C CB   . LEU A 1 46  ? 53.318  -24.204 102.774 1.00 58.35  ?  55  LEU A CB   1 
ATOM   681   C CG   . LEU A 1 46  ? 52.452  -24.182 101.478 1.00 69.31  ?  55  LEU A CG   1 
ATOM   682   C CD1  . LEU A 1 46  ? 51.707  -22.891 101.282 1.00 62.23  ?  55  LEU A CD1  1 
ATOM   683   C CD2  . LEU A 1 46  ? 53.281  -24.425 100.217 1.00 95.90  ?  55  LEU A CD2  1 
ATOM   684   H H    . LEU A 1 46  ? 54.969  -24.225 104.579 1.00 116.68 ?  55  LEU A H    1 
ATOM   685   H HA   . LEU A 1 46  ? 55.194  -24.155 101.954 1.00 96.04  ?  55  LEU A HA   1 
ATOM   686   H HB2  . LEU A 1 46  ? 53.350  -25.125 103.076 1.00 70.01  ?  55  LEU A HB2  1 
ATOM   687   H HB3  . LEU A 1 46  ? 52.851  -23.670 103.435 1.00 70.01  ?  55  LEU A HB3  1 
ATOM   688   H HG   . LEU A 1 46  ? 51.794  -24.892 101.536 1.00 83.18  ?  55  LEU A HG   1 
ATOM   689   H HD11 . LEU A 1 46  ? 51.192  -22.946 100.461 1.00 74.68  ?  55  LEU A HD11 1 
ATOM   690   H HD12 . LEU A 1 46  ? 51.114  -22.751 102.036 1.00 74.68  ?  55  LEU A HD12 1 
ATOM   691   H HD13 . LEU A 1 46  ? 52.346  -22.164 101.223 1.00 74.68  ?  55  LEU A HD13 1 
ATOM   692   H HD21 . LEU A 1 46  ? 52.694  -24.400 99.445  1.00 115.08 ?  55  LEU A HD21 1 
ATOM   693   H HD22 . LEU A 1 46  ? 53.954  -23.731 100.144 1.00 115.08 ?  55  LEU A HD22 1 
ATOM   694   H HD23 . LEU A 1 46  ? 53.707  -25.294 100.282 1.00 115.08 ?  55  LEU A HD23 1 
ATOM   695   N N    . ARG A 1 47  ? 54.434  -21.365 103.336 1.00 73.07  ?  56  ARG A N    1 
ATOM   696   C CA   . ARG A 1 47  ? 54.429  -19.935 103.062 1.00 76.52  ?  56  ARG A CA   1 
ATOM   697   C C    . ARG A 1 47  ? 55.841  -19.415 102.779 1.00 93.77  ?  56  ARG A C    1 
ATOM   698   O O    . ARG A 1 47  ? 56.031  -18.579 101.883 1.00 91.64  ?  56  ARG A O    1 
ATOM   699   C CB   . ARG A 1 47  ? 53.751  -19.245 104.235 1.00 66.52  ?  56  ARG A CB   1 
ATOM   700   C CG   . ARG A 1 47  ? 52.321  -19.669 104.268 1.00 76.72  ?  56  ARG A CG   1 
ATOM   701   C CD   . ARG A 1 47  ? 51.671  -19.310 105.562 1.00 82.98  ?  56  ARG A CD   1 
ATOM   702   N NE   . ARG A 1 47  ? 50.214  -19.444 105.471 1.00 77.19  ?  56  ARG A NE   1 
ATOM   703   C CZ   . ARG A 1 47  ? 49.400  -19.488 106.513 1.00 77.95  ?  56  ARG A CZ   1 
ATOM   704   N NH1  . ARG A 1 47  ? 49.872  -19.435 107.753 1.00 94.91  1  56  ARG A NH1  1 
ATOM   705   N NH2  . ARG A 1 47  ? 48.109  -19.574 106.304 1.00 51.89  1  56  ARG A NH2  1 
ATOM   706   H H    . ARG A 1 47  ? 54.211  -21.591 104.135 1.00 87.69  ?  56  ARG A H    1 
ATOM   707   H HA   . ARG A 1 47  ? 53.891  -19.771 102.272 1.00 91.82  ?  56  ARG A HA   1 
ATOM   708   H HB2  . ARG A 1 47  ? 54.177  -19.511 105.065 1.00 79.83  ?  56  ARG A HB2  1 
ATOM   709   H HB3  . ARG A 1 47  ? 53.790  -18.283 104.119 1.00 79.83  ?  56  ARG A HB3  1 
ATOM   710   H HG2  . ARG A 1 47  ? 51.839  -19.225 103.553 1.00 92.06  ?  56  ARG A HG2  1 
ATOM   711   H HG3  . ARG A 1 47  ? 52.270  -20.632 104.160 1.00 92.06  ?  56  ARG A HG3  1 
ATOM   712   H HD2  . ARG A 1 47  ? 51.990  -19.906 106.259 1.00 99.57  ?  56  ARG A HD2  1 
ATOM   713   H HD3  . ARG A 1 47  ? 51.881  -18.389 105.783 1.00 99.57  ?  56  ARG A HD3  1 
ATOM   714   H HE   . ARG A 1 47  ? 49.864  -19.497 104.687 1.00 92.63  ?  56  ARG A HE   1 
ATOM   715   H HH11 . ARG A 1 47  ? 50.718  -19.368 107.889 1.00 113.89 ?  56  ARG A HH11 1 
ATOM   716   H HH12 . ARG A 1 47  ? 49.330  -19.468 108.421 1.00 113.89 ?  56  ARG A HH12 1 
ATOM   717   H HH21 . ARG A 1 47  ? 47.805  -19.614 105.500 1.00 62.27  ?  56  ARG A HH21 1 
ATOM   718   H HH22 . ARG A 1 47  ? 47.567  -19.617 106.971 1.00 62.27  ?  56  ARG A HH22 1 
ATOM   719   N N    . GLU A 1 48  ? 56.848  -19.975 103.453 1.00 81.39  ?  57  GLU A N    1 
ATOM   720   C CA   . GLU A 1 48  ? 58.221  -19.588 103.168 1.00 75.84  ?  57  GLU A CA   1 
ATOM   721   C C    . GLU A 1 48  ? 58.541  -19.763 101.687 1.00 77.67  ?  57  GLU A C    1 
ATOM   722   O O    . GLU A 1 48  ? 59.177  -18.899 101.076 1.00 98.58  ?  57  GLU A O    1 
ATOM   723   C CB   . GLU A 1 48  ? 59.191  -20.423 104.019 1.00 117.51 ?  57  GLU A CB   1 
ATOM   724   C CG   . GLU A 1 48  ? 59.300  -20.025 105.488 1.00 143.60 ?  57  GLU A CG   1 
ATOM   725   C CD   . GLU A 1 48  ? 59.948  -21.097 106.335 1.00 91.70  ?  57  GLU A CD   1 
ATOM   726   H H    . GLU A 1 48  ? 56.761  -20.569 104.068 1.00 97.67  ?  57  GLU A H    1 
ATOM   727   H HA   . GLU A 1 48  ? 58.344  -18.653 103.397 1.00 91.00  ?  57  GLU A HA   1 
ATOM   728   H HB2  . GLU A 1 48  ? 58.904  -21.348 103.990 1.00 141.02 ?  57  GLU A HB2  1 
ATOM   729   H HB3  . GLU A 1 48  ? 60.078  -20.348 103.633 1.00 141.02 ?  57  GLU A HB3  1 
ATOM   730   H HG2  . GLU A 1 48  ? 59.837  -19.220 105.559 1.00 172.32 ?  57  GLU A HG2  1 
ATOM   731   H HG3  . GLU A 1 48  ? 58.410  -19.863 105.838 1.00 172.32 ?  57  GLU A HG3  1 
ATOM   732   N N    . ARG A 1 49  ? 58.104  -20.864 101.080 1.00 74.28  ?  58  ARG A N    1 
ATOM   733   C CA   . ARG A 1 49  ? 58.503  -21.119 99.703  1.00 75.63  ?  58  ARG A CA   1 
ATOM   734   C C    . ARG A 1 49  ? 57.815  -20.153 98.778  1.00 78.05  ?  58  ARG A C    1 
ATOM   735   O O    . ARG A 1 49  ? 58.446  -19.527 97.917  1.00 112.01 ?  58  ARG A O    1 
ATOM   736   C CB   . ARG A 1 49  ? 58.185  -22.559 99.293  1.00 84.13  ?  58  ARG A CB   1 
ATOM   737   C CG   . ARG A 1 49  ? 59.105  -23.639 99.890  1.00 76.18  ?  58  ARG A CG   1 
ATOM   738   C CD   . ARG A 1 49  ? 60.567  -23.519 99.523  1.00 83.03  ?  58  ARG A CD   1 
ATOM   739   N NE   . ARG A 1 49  ? 61.351  -22.986 100.640 1.00 119.50 ?  58  ARG A NE   1 
ATOM   740   C CZ   . ARG A 1 49  ? 62.589  -22.509 100.530 1.00 131.91 ?  58  ARG A CZ   1 
ATOM   741   N NH1  . ARG A 1 49  ? 63.194  -22.501 99.349  1.00 136.12 1  58  ARG A NH1  1 
ATOM   742   N NH2  . ARG A 1 49  ? 63.226  -22.032 101.598 1.00 125.67 1  58  ARG A NH2  1 
ATOM   743   H H    . ARG A 1 49  ? 57.593  -21.460 101.432 1.00 89.14  ?  58  ARG A H    1 
ATOM   744   H HA   . ARG A 1 49  ? 59.460  -20.987 99.620  1.00 90.75  ?  58  ARG A HA   1 
ATOM   745   H HB2  . ARG A 1 49  ? 57.279  -22.764 99.570  1.00 100.96 ?  58  ARG A HB2  1 
ATOM   746   H HB3  . ARG A 1 49  ? 58.250  -22.624 98.327  1.00 100.96 ?  58  ARG A HB3  1 
ATOM   747   H HG2  . ARG A 1 49  ? 59.043  -23.594 100.857 1.00 91.41  ?  58  ARG A HG2  1 
ATOM   748   H HG3  . ARG A 1 49  ? 58.798  -24.507 99.585  1.00 91.41  ?  58  ARG A HG3  1 
ATOM   749   H HD2  . ARG A 1 49  ? 60.914  -24.396 99.297  1.00 99.63  ?  58  ARG A HD2  1 
ATOM   750   H HD3  . ARG A 1 49  ? 60.660  -22.915 98.770  1.00 99.63  ?  58  ARG A HD3  1 
ATOM   751   H HE   . ARG A 1 49  ? 60.988  -22.982 101.419 1.00 143.40 ?  58  ARG A HE   1 
ATOM   752   H HH11 . ARG A 1 49  ? 62.787  -22.804 98.655  1.00 163.34 ?  58  ARG A HH11 1 
ATOM   753   H HH12 . ARG A 1 49  ? 63.994  -22.193 99.278  1.00 163.34 ?  58  ARG A HH12 1 
ATOM   754   H HH21 . ARG A 1 49  ? 62.839  -22.037 102.366 1.00 150.81 ?  58  ARG A HH21 1 
ATOM   755   H HH22 . ARG A 1 49  ? 64.027  -21.729 101.521 1.00 150.81 ?  58  ARG A HH22 1 
ATOM   756   N N    . VAL A 1 50  ? 56.529  -19.986 98.980  1.00 72.43  ?  59  VAL A N    1 
ATOM   757   C CA   . VAL A 1 50  ? 55.765  -19.125 98.103  1.00 105.23 ?  59  VAL A CA   1 
ATOM   758   C C    . VAL A 1 50  ? 56.298  -17.711 98.166  1.00 72.80  ?  59  VAL A C    1 
ATOM   759   O O    . VAL A 1 50  ? 56.462  -17.047 97.138  1.00 93.36  ?  59  VAL A O    1 
ATOM   760   C CB   . VAL A 1 50  ? 54.284  -19.196 98.492  1.00 79.84  ?  59  VAL A CB   1 
ATOM   761   C CG1  . VAL A 1 50  ? 53.494  -18.106 97.830  1.00 66.54  ?  59  VAL A CG1  1 
ATOM   762   C CG2  . VAL A 1 50  ? 53.758  -20.531 98.136  1.00 93.95  ?  59  VAL A CG2  1 
ATOM   763   H H    . VAL A 1 50  ? 56.075  -20.355 99.611  1.00 86.92  ?  59  VAL A H    1 
ATOM   764   H HA   . VAL A 1 50  ? 55.854  -19.440 97.190  1.00 126.28 ?  59  VAL A HA   1 
ATOM   765   H HB   . VAL A 1 50  ? 54.202  -19.086 99.452  1.00 95.81  ?  59  VAL A HB   1 
ATOM   766   H HG11 . VAL A 1 50  ? 52.565  -18.182 98.099  1.00 79.85  ?  59  VAL A HG11 1 
ATOM   767   H HG12 . VAL A 1 50  ? 53.849  -17.247 98.107  1.00 79.85  ?  59  VAL A HG12 1 
ATOM   768   H HG13 . VAL A 1 50  ? 53.570  -18.201 96.868  1.00 79.85  ?  59  VAL A HG13 1 
ATOM   769   H HG21 . VAL A 1 50  ? 52.821  -20.578 98.381  1.00 112.75 ?  59  VAL A HG21 1 
ATOM   770   H HG22 . VAL A 1 50  ? 53.857  -20.664 97.180  1.00 112.75 ?  59  VAL A HG22 1 
ATOM   771   H HG23 . VAL A 1 50  ? 54.261  -21.207 98.618  1.00 112.75 ?  59  VAL A HG23 1 
ATOM   772   N N    . GLU A 1 51  ? 56.560  -17.220 99.373  1.00 71.59  ?  60  GLU A N    1 
ATOM   773   C CA   . GLU A 1 51  ? 56.977  -15.847 99.513  1.00 118.98 ?  60  GLU A CA   1 
ATOM   774   C C    . GLU A 1 51  ? 58.326  -15.607 98.856  1.00 103.87 ?  60  GLU A C    1 
ATOM   775   O O    . GLU A 1 51  ? 58.611  -14.483 98.435  1.00 118.85 ?  60  GLU A O    1 
ATOM   776   C CB   . GLU A 1 51  ? 56.982  -15.517 100.993 1.00 58.25  ?  60  GLU A CB   1 
ATOM   777   C CG   . GLU A 1 51  ? 55.621  -15.382 101.513 1.00 56.74  ?  60  GLU A CG   1 
ATOM   778   C CD   . GLU A 1 51  ? 55.518  -15.561 102.985 1.00 94.29  ?  60  GLU A CD   1 
ATOM   779   O OE1  . GLU A 1 51  ? 56.585  -15.673 103.635 1.00 146.56 ?  60  GLU A OE1  1 
ATOM   780   O OE2  . GLU A 1 51  ? 54.366  -15.517 103.496 1.00 88.71  -1 60  GLU A OE2  1 
ATOM   781   H H    . GLU A 1 51  ? 56.503  -17.659 100.111 1.00 85.91  ?  60  GLU A H    1 
ATOM   782   H HA   . GLU A 1 51  ? 56.326  -15.273 99.079  1.00 142.78 ?  60  GLU A HA   1 
ATOM   783   H HB2  . GLU A 1 51  ? 57.424  -16.231 101.479 1.00 69.91  ?  60  GLU A HB2  1 
ATOM   784   H HB3  . GLU A 1 51  ? 57.446  -14.677 101.133 1.00 69.91  ?  60  GLU A HB3  1 
ATOM   785   H HG2  . GLU A 1 51  ? 55.291  -14.496 101.298 1.00 68.08  ?  60  GLU A HG2  1 
ATOM   786   H HG3  . GLU A 1 51  ? 55.059  -16.052 101.094 1.00 68.08  ?  60  GLU A HG3  1 
ATOM   787   N N    . LYS A 1 52  ? 59.110  -16.665 98.679  1.00 103.92 ?  61  LYS A N    1 
ATOM   788   C CA   . LYS A 1 52  ? 60.410  -16.607 98.048  1.00 92.82  ?  61  LYS A CA   1 
ATOM   789   C C    . LYS A 1 52  ? 60.377  -16.982 96.567  1.00 133.99 ?  61  LYS A C    1 
ATOM   790   O O    . LYS A 1 52  ? 61.404  -17.386 96.026  1.00 63.14  ?  61  LYS A O    1 
ATOM   791   C CB   . LYS A 1 52  ? 61.352  -17.530 98.814  1.00 111.03 ?  61  LYS A CB   1 
ATOM   792   C CG   . LYS A 1 52  ? 61.700  -17.022 100.203 1.00 134.70 ?  61  LYS A CG   1 
ATOM   793   C CD   . LYS A 1 52  ? 62.770  -17.878 100.881 1.00 145.86 ?  61  LYS A CD   1 
ATOM   794   C CE   . LYS A 1 52  ? 63.349  -17.162 102.082 1.00 159.88 ?  61  LYS A CE   1 
ATOM   795   N NZ   . LYS A 1 52  ? 64.398  -17.961 102.753 1.00 175.97 1  61  LYS A NZ   1 
ATOM   796   H H    . LYS A 1 52  ? 58.894  -17.459 98.929  1.00 124.70 ?  61  LYS A H    1 
ATOM   797   H HA   . LYS A 1 52  ? 60.754  -15.703 98.120  1.00 111.39 ?  61  LYS A HA   1 
ATOM   798   H HB2  . LYS A 1 52  ? 60.931  -18.398 98.911  1.00 133.24 ?  61  LYS A HB2  1 
ATOM   799   H HB3  . LYS A 1 52  ? 62.179  -17.619 98.314  1.00 133.24 ?  61  LYS A HB3  1 
ATOM   800   H HG2  . LYS A 1 52  ? 62.037  -16.116 100.134 1.00 161.64 ?  61  LYS A HG2  1 
ATOM   801   H HG3  . LYS A 1 52  ? 60.903  -17.041 100.756 1.00 161.64 ?  61  LYS A HG3  1 
ATOM   802   H HD2  . LYS A 1 52  ? 62.374  -18.711 101.182 1.00 175.03 ?  61  LYS A HD2  1 
ATOM   803   H HD3  . LYS A 1 52  ? 63.488  -18.054 100.253 1.00 175.03 ?  61  LYS A HD3  1 
ATOM   804   H HE2  . LYS A 1 52  ? 63.745  -16.325 101.793 1.00 191.85 ?  61  LYS A HE2  1 
ATOM   805   H HE3  . LYS A 1 52  ? 62.641  -16.993 102.724 1.00 191.85 ?  61  LYS A HE3  1 
ATOM   806   H HZ1  . LYS A 1 52  ? 64.719  -17.515 103.453 1.00 211.17 ?  61  LYS A HZ1  1 
ATOM   807   H HZ2  . LYS A 1 52  ? 64.059  -18.735 103.033 1.00 211.17 ?  61  LYS A HZ2  1 
ATOM   808   H HZ3  . LYS A 1 52  ? 65.064  -18.126 102.185 1.00 211.17 ?  61  LYS A HZ3  1 
ATOM   809   N N    . LEU A 1 53  ? 59.257  -16.811 95.877  1.00 65.53  ?  62  LEU A N    1 
ATOM   810   C CA   . LEU A 1 53  ? 59.253  -17.060 94.447  1.00 58.97  ?  62  LEU A CA   1 
ATOM   811   C C    . LEU A 1 53  ? 59.329  -15.782 93.646  1.00 88.62  ?  62  LEU A C    1 
ATOM   812   O O    . LEU A 1 53  ? 58.836  -14.732 94.064  1.00 149.43 ?  62  LEU A O    1 
ATOM   813   C CB   . LEU A 1 53  ? 57.987  -17.759 94.042  1.00 72.16  ?  62  LEU A CB   1 
ATOM   814   C CG   . LEU A 1 53  ? 57.542  -19.147 94.463  1.00 74.05  ?  62  LEU A CG   1 
ATOM   815   C CD1  . LEU A 1 53  ? 56.105  -19.225 93.941  1.00 60.85  ?  62  LEU A CD1  1 
ATOM   816   C CD2  . LEU A 1 53  ? 58.383  -20.248 93.831  1.00 87.94  ?  62  LEU A CD2  1 
ATOM   817   H H    . LEU A 1 53  ? 58.503  -16.557 96.205  1.00 78.63  ?  62  LEU A H    1 
ATOM   818   H HA   . LEU A 1 53  ? 60.008  -17.621 94.211  1.00 70.76  ?  62  LEU A HA   1 
ATOM   819   H HB2  . LEU A 1 53  ? 57.263  -17.173 94.312  1.00 86.60  ?  62  LEU A HB2  1 
ATOM   820   H HB3  . LEU A 1 53  ? 57.998  -17.785 93.072  1.00 86.60  ?  62  LEU A HB3  1 
ATOM   821   H HG   . LEU A 1 53  ? 57.547  -19.235 95.429  1.00 88.86  ?  62  LEU A HG   1 
ATOM   822   H HD11 . LEU A 1 53  ? 55.734  -20.092 94.169  1.00 73.02  ?  62  LEU A HD11 1 
ATOM   823   H HD12 . LEU A 1 53  ? 55.580  -18.522 94.355  1.00 73.02  ?  62  LEU A HD12 1 
ATOM   824   H HD13 . LEU A 1 53  ? 56.112  -19.110 92.978  1.00 73.02  ?  62  LEU A HD13 1 
ATOM   825   H HD21 . LEU A 1 53  ? 58.054  -21.109 94.135  1.00 105.53 ?  62  LEU A HD21 1 
ATOM   826   H HD22 . LEU A 1 53  ? 58.309  -20.187 92.866  1.00 105.53 ?  62  LEU A HD22 1 
ATOM   827   H HD23 . LEU A 1 53  ? 59.307  -20.132 94.101  1.00 105.53 ?  62  LEU A HD23 1 
ATOM   828   N N    . ASN A 1 54  ? 59.868  -15.914 92.439  1.00 98.63  ?  63  ASN A N    1 
ATOM   829   C CA   . ASN A 1 54  ? 59.855  -14.803 91.513  1.00 113.86 ?  63  ASN A CA   1 
ATOM   830   C C    . ASN A 1 54  ? 58.545  -14.757 90.742  1.00 109.43 ?  63  ASN A C    1 
ATOM   831   O O    . ASN A 1 54  ? 57.875  -15.763 90.514  1.00 147.64 ?  63  ASN A O    1 
ATOM   832   C CB   . ASN A 1 54  ? 61.002  -14.862 90.496  1.00 115.19 ?  63  ASN A CB   1 
ATOM   833   C CG   . ASN A 1 54  ? 62.389  -14.849 91.137  1.00 94.75  ?  63  ASN A CG   1 
ATOM   834   O OD1  . ASN A 1 54  ? 63.303  -15.544 90.679  1.00 75.13  ?  63  ASN A OD1  1 
ATOM   835   N ND2  . ASN A 1 54  ? 62.546  -14.097 92.207  1.00 106.88 ?  63  ASN A ND2  1 
ATOM   836   H H    . ASN A 1 54  ? 60.240  -16.629 92.140  1.00 118.35 ?  63  ASN A H    1 
ATOM   837   H HA   . ASN A 1 54  ? 59.939  -13.975 92.012  1.00 136.63 ?  63  ASN A HA   1 
ATOM   838   H HB2  . ASN A 1 54  ? 60.921  -15.679 89.980  1.00 138.23 ?  63  ASN A HB2  1 
ATOM   839   H HB3  . ASN A 1 54  ? 60.939  -14.094 89.907  1.00 138.23 ?  63  ASN A HB3  1 
ATOM   840   H HD21 . ASN A 1 54  ? 63.311  -14.061 92.599  1.00 128.26 ?  63  ASN A HD21 1 
ATOM   841   H HD22 . ASN A 1 54  ? 61.884  -13.642 92.514  1.00 128.26 ?  63  ASN A HD22 1 
ATOM   842   N N    . MET A 1 55  ? 58.223  -13.566 90.281  1.00 121.00 ?  64  MET A N    1 
ATOM   843   C CA   . MET A 1 55  ? 57.039  -13.394 89.474  1.00 115.30 ?  64  MET A CA   1 
ATOM   844   C C    . MET A 1 55  ? 57.316  -13.956 88.106  1.00 130.40 ?  64  MET A C    1 
ATOM   845   O O    . MET A 1 55  ? 57.931  -13.304 87.266  1.00 117.13 ?  64  MET A O    1 
ATOM   846   C CB   . MET A 1 55  ? 56.646  -11.938 89.355  1.00 113.72 ?  64  MET A CB   1 
ATOM   847   C CG   . MET A 1 55  ? 55.326  -11.845 88.653  1.00 96.16  ?  64  MET A CG   1 
ATOM   848   S SD   . MET A 1 55  ? 54.722  -10.168 88.574  1.00 88.42  ?  64  MET A SD   1 
ATOM   849   C CE   . MET A 1 55  ? 54.451  -9.881  90.336  1.00 87.98  ?  64  MET A CE   1 
ATOM   850   H H    . MET A 1 55  ? 58.671  -12.845 90.420  1.00 145.20 ?  64  MET A H    1 
ATOM   851   H HA   . MET A 1 55  ? 56.301  -13.877 89.878  1.00 138.36 ?  64  MET A HA   1 
ATOM   852   H HB2  . MET A 1 55  ? 56.558  -11.548 90.239  1.00 136.46 ?  64  MET A HB2  1 
ATOM   853   H HB3  . MET A 1 55  ? 57.310  -11.460 88.834  1.00 136.46 ?  64  MET A HB3  1 
ATOM   854   H HG2  . MET A 1 55  ? 55.424  -12.174 87.746  1.00 115.40 ?  64  MET A HG2  1 
ATOM   855   H HG3  . MET A 1 55  ? 54.673  -12.378 89.133  1.00 115.40 ?  64  MET A HG3  1 
ATOM   856   H HE1  . MET A 1 55  ? 54.111  -8.982  90.460  1.00 105.58 ?  64  MET A HE1  1 
ATOM   857   H HE2  . MET A 1 55  ? 53.806  -10.527 90.665  1.00 105.58 ?  64  MET A HE2  1 
ATOM   858   H HE3  . MET A 1 55  ? 55.293  -9.985  90.806  1.00 105.58 ?  64  MET A HE3  1 
ATOM   859   N N    . LEU A 1 56  ? 56.823  -15.156 87.872  1.00 110.24 ?  65  LEU A N    1 
ATOM   860   C CA   . LEU A 1 56  ? 56.981  -15.739 86.568  1.00 96.16  ?  65  LEU A CA   1 
ATOM   861   C C    . LEU A 1 56  ? 55.911  -15.211 85.645  1.00 104.41 ?  65  LEU A C    1 
ATOM   862   O O    . LEU A 1 56  ? 54.872  -14.701 86.070  1.00 103.14 ?  65  LEU A O    1 
ATOM   863   C CB   . LEU A 1 56  ? 56.875  -17.252 86.609  1.00 110.19 ?  65  LEU A CB   1 
ATOM   864   C CG   . LEU A 1 56  ? 57.860  -17.984 87.501  1.00 123.53 ?  65  LEU A CG   1 
ATOM   865   C CD1  . LEU A 1 56  ? 57.769  -19.478 87.184  1.00 114.01 ?  65  LEU A CD1  1 
ATOM   866   C CD2  . LEU A 1 56  ? 59.285  -17.448 87.362  1.00 62.84  ?  65  LEU A CD2  1 
ATOM   867   H H    . LEU A 1 56  ? 56.400  -15.643 88.441  1.00 132.28 ?  65  LEU A H    1 
ATOM   868   H HA   . LEU A 1 56  ? 57.849  -15.499 86.207  1.00 115.39 ?  65  LEU A HA   1 
ATOM   869   H HB2  . LEU A 1 56  ? 55.985  -17.484 86.914  1.00 132.23 ?  65  LEU A HB2  1 
ATOM   870   H HB3  . LEU A 1 56  ? 57.002  -17.588 85.707  1.00 132.23 ?  65  LEU A HB3  1 
ATOM   871   H HG   . LEU A 1 56  ? 57.590  -17.863 88.425  1.00 148.23 ?  65  LEU A HG   1 
ATOM   872   H HD11 . LEU A 1 56  ? 58.394  -19.959 87.749  1.00 136.81 ?  65  LEU A HD11 1 
ATOM   873   H HD12 . LEU A 1 56  ? 56.864  -19.783 87.357  1.00 136.81 ?  65  LEU A HD12 1 
ATOM   874   H HD13 . LEU A 1 56  ? 57.992  -19.617 86.250  1.00 136.81 ?  65  LEU A HD13 1 
ATOM   875   H HD21 . LEU A 1 56  ? 59.869  -17.949 87.951  1.00 75.41  ?  65  LEU A HD21 1 
ATOM   876   H HD22 . LEU A 1 56  ? 59.573  -17.553 86.441  1.00 75.41  ?  65  LEU A HD22 1 
ATOM   877   H HD23 . LEU A 1 56  ? 59.293  -16.509 87.606  1.00 75.41  ?  65  LEU A HD23 1 
ATOM   878   N N    . SER A 1 57  ? 56.197  -15.337 84.364  1.00 111.63 ?  66  SER A N    1 
ATOM   879   C CA   . SER A 1 57  ? 55.302  -14.950 83.297  1.00 75.63  ?  66  SER A CA   1 
ATOM   880   C C    . SER A 1 57  ? 54.361  -16.088 82.910  1.00 88.85  ?  66  SER A C    1 
ATOM   881   O O    . SER A 1 57  ? 54.711  -17.268 83.005  1.00 91.41  ?  66  SER A O    1 
ATOM   882   C CB   . SER A 1 57  ? 56.136  -14.531 82.094  1.00 76.56  ?  66  SER A CB   1 
ATOM   883   O OG   . SER A 1 57  ? 55.305  -14.203 81.017  1.00 87.18  ?  66  SER A OG   1 
ATOM   884   H H    . SER A 1 57  ? 56.940  -15.659 84.076  1.00 133.95 ?  66  SER A H    1 
ATOM   885   H HA   . SER A 1 57  ? 54.768  -14.192 83.581  1.00 90.76  ?  66  SER A HA   1 
ATOM   886   H HB2  . SER A 1 57  ? 56.669  -13.756 82.332  1.00 91.88  ?  66  SER A HB2  1 
ATOM   887   H HB3  . SER A 1 57  ? 56.714  -15.267 81.837  1.00 91.88  ?  66  SER A HB3  1 
ATOM   888   H HG   . SER A 1 57  ? 55.768  -13.972 80.356  1.00 104.61 ?  66  SER A HG   1 
ATOM   889   N N    . ILE A 1 58  ? 53.166  -15.714 82.430  1.00 76.90  ?  67  ILE A N    1 
ATOM   890   C CA   . ILE A 1 58  ? 52.210  -16.687 81.890  1.00 92.75  ?  67  ILE A CA   1 
ATOM   891   C C    . ILE A 1 58  ? 52.391  -16.853 80.394  1.00 113.76 ?  67  ILE A C    1 
ATOM   892   O O    . ILE A 1 58  ? 51.686  -17.652 79.763  1.00 116.36 ?  67  ILE A O    1 
ATOM   893   C CB   . ILE A 1 58  ? 50.724  -16.321 82.119  1.00 98.62  ?  67  ILE A CB   1 
ATOM   894   C CG1  . ILE A 1 58  ? 50.356  -15.050 81.376  1.00 59.75  ?  67  ILE A CG1  1 
ATOM   895   C CG2  . ILE A 1 58  ? 50.463  -16.098 83.537  1.00 53.40  ?  67  ILE A CG2  1 
ATOM   896   C CD1  . ILE A 1 58  ? 49.538  -15.222 80.159  1.00 118.64 ?  67  ILE A CD1  1 
ATOM   897   H H    . ILE A 1 58  ? 52.887  -14.901 82.406  1.00 92.28  ?  67  ILE A H    1 
ATOM   898   H HA   . ILE A 1 58  ? 52.372  -17.548 82.307  1.00 111.30 ?  67  ILE A HA   1 
ATOM   899   H HB   . ILE A 1 58  ? 50.165  -17.048 81.803  1.00 118.34 ?  67  ILE A HB   1 
ATOM   900   H HG12 . ILE A 1 58  ? 49.857  -14.478 81.980  1.00 71.70  ?  67  ILE A HG12 1 
ATOM   901   H HG13 . ILE A 1 58  ? 51.175  -14.602 81.113  1.00 71.70  ?  67  ILE A HG13 1 
ATOM   902   H HG21 . ILE A 1 58  ? 49.527  -15.870 83.653  1.00 64.09  ?  67  ILE A HG21 1 
ATOM   903   H HG22 . ILE A 1 58  ? 50.671  -16.909 84.028  1.00 64.09  ?  67  ILE A HG22 1 
ATOM   904   H HG23 . ILE A 1 58  ? 51.022  -15.369 83.850  1.00 64.09  ?  67  ILE A HG23 1 
ATOM   905   H HD11 . ILE A 1 58  ? 49.364  -14.350 79.770  1.00 142.37 ?  67  ILE A HD11 1 
ATOM   906   H HD12 . ILE A 1 58  ? 50.025  -15.775 79.528  1.00 142.37 ?  67  ILE A HD12 1 
ATOM   907   H HD13 . ILE A 1 58  ? 48.702  -15.650 80.399  1.00 142.37 ?  67  ILE A HD13 1 
ATOM   908   N N    . ASP A 1 59  ? 53.321  -16.132 79.806  1.00 137.79 ?  68  ASP A N    1 
ATOM   909   C CA   . ASP A 1 59  ? 53.393  -16.081 78.369  1.00 122.67 ?  68  ASP A CA   1 
ATOM   910   C C    . ASP A 1 59  ? 54.003  -17.340 77.783  1.00 156.32 ?  68  ASP A C    1 
ATOM   911   O O    . ASP A 1 59  ? 54.023  -17.497 76.567  1.00 89.34  ?  68  ASP A O    1 
ATOM   912   C CB   . ASP A 1 59  ? 54.147  -14.825 77.977  1.00 121.61 ?  68  ASP A CB   1 
ATOM   913   C CG   . ASP A 1 59  ? 53.523  -13.562 78.577  1.00 112.07 ?  68  ASP A CG   1 
ATOM   914   O OD1  . ASP A 1 59  ? 52.460  -13.661 79.246  1.00 115.06 ?  68  ASP A OD1  1 
ATOM   915   O OD2  . ASP A 1 59  ? 54.097  -12.468 78.364  1.00 118.49 -1 68  ASP A OD2  1 
ATOM   916   H H    . ASP A 1 59  ? 53.919  -15.667 80.214  1.00 165.35 ?  68  ASP A H    1 
ATOM   917   H HA   . ASP A 1 59  ? 52.492  -16.003 78.018  1.00 147.20 ?  68  ASP A HA   1 
ATOM   918   H HB2  . ASP A 1 59  ? 55.061  -14.890 78.296  1.00 145.93 ?  68  ASP A HB2  1 
ATOM   919   H HB3  . ASP A 1 59  ? 54.137  -14.736 77.011  1.00 145.93 ?  68  ASP A HB3  1 
ATOM   920   N N    . HIS A 1 60  ? 54.558  -18.216 78.600  1.00 126.19 ?  69  HIS A N    1 
ATOM   921   C CA   . HIS A 1 60  ? 55.009  -19.503 78.097  1.00 115.58 ?  69  HIS A CA   1 
ATOM   922   C C    . HIS A 1 60  ? 53.958  -20.592 78.289  1.00 154.25 ?  69  HIS A C    1 
ATOM   923   O O    . HIS A 1 60  ? 54.282  -21.783 78.223  1.00 90.50  ?  69  HIS A O    1 
ATOM   924   C CB   . HIS A 1 60  ? 56.308  -19.928 78.759  1.00 117.57 ?  69  HIS A CB   1 
ATOM   925   C CG   . HIS A 1 60  ? 57.439  -18.965 78.562  1.00 107.70 ?  69  HIS A CG   1 
ATOM   926   N ND1  . HIS A 1 60  ? 57.793  -18.024 79.508  1.00 102.23 ?  69  HIS A ND1  1 
ATOM   927   C CD2  . HIS A 1 60  ? 58.268  -18.766 77.512  1.00 113.72 ?  69  HIS A CD2  1 
ATOM   928   C CE1  . HIS A 1 60  ? 58.805  -17.306 79.062  1.00 121.89 ?  69  HIS A CE1  1 
ATOM   929   N NE2  . HIS A 1 60  ? 59.112  -17.735 77.852  1.00 138.95 ?  69  HIS A NE2  1 
ATOM   930   H H    . HIS A 1 60  ? 54.684  -18.095 79.442  1.00 151.42 ?  69  HIS A H    1 
ATOM   931   H HA   . HIS A 1 60  ? 55.177  -19.421 77.145  1.00 138.69 ?  69  HIS A HA   1 
ATOM   932   H HB2  . HIS A 1 60  ? 56.157  -20.015 79.713  1.00 141.08 ?  69  HIS A HB2  1 
ATOM   933   H HB3  . HIS A 1 60  ? 56.580  -20.783 78.391  1.00 141.08 ?  69  HIS A HB3  1 
ATOM   934   H HD2  . HIS A 1 60  ? 58.275  -19.245 76.715  1.00 136.47 ?  69  HIS A HD2  1 
ATOM   935   H HE1  . HIS A 1 60  ? 59.227  -16.614 79.519  1.00 146.26 ?  69  HIS A HE1  1 
ATOM   936   H HE2  . HIS A 1 60  ? 59.740  -17.420 77.356  1.00 166.74 ?  69  HIS A HE2  1 
ATOM   937   N N    . LEU A 1 61  ? 52.721  -20.215 78.583  1.00 119.05 ?  70  LEU A N    1 
ATOM   938   C CA   . LEU A 1 61  ? 51.622  -21.154 78.650  1.00 108.81 ?  70  LEU A CA   1 
ATOM   939   C C    . LEU A 1 61  ? 50.854  -21.020 77.355  1.00 114.71 ?  70  LEU A C    1 
ATOM   940   O O    . LEU A 1 61  ? 50.020  -20.128 77.196  1.00 130.48 ?  70  LEU A O    1 
ATOM   941   C CB   . LEU A 1 61  ? 50.755  -20.873 79.859  1.00 86.91  ?  70  LEU A CB   1 
ATOM   942   C CG   . LEU A 1 61  ? 51.558  -20.941 81.144  1.00 70.80  ?  70  LEU A CG   1 
ATOM   943   C CD1  . LEU A 1 61  ? 50.766  -20.441 82.290  1.00 109.86 ?  70  LEU A CD1  1 
ATOM   944   C CD2  . LEU A 1 61  ? 52.021  -22.341 81.381  1.00 53.80  ?  70  LEU A CD2  1 
ATOM   945   H H    . LEU A 1 61  ? 52.492  -19.403 78.750  1.00 142.86 ?  70  LEU A H    1 
ATOM   946   H HA   . LEU A 1 61  ? 51.966  -22.059 78.716  1.00 130.58 ?  70  LEU A HA   1 
ATOM   947   H HB2  . LEU A 1 61  ? 50.377  -19.983 79.782  1.00 104.30 ?  70  LEU A HB2  1 
ATOM   948   H HB3  . LEU A 1 61  ? 50.048  -21.536 79.907  1.00 104.30 ?  70  LEU A HB3  1 
ATOM   949   H HG   . LEU A 1 61  ? 52.342  -20.378 81.055  1.00 84.96  ?  70  LEU A HG   1 
ATOM   950   H HD11 . LEU A 1 61  ? 51.306  -20.498 83.094  1.00 131.84 ?  70  LEU A HD11 1 
ATOM   951   H HD12 . LEU A 1 61  ? 50.516  -19.519 82.123  1.00 131.84 ?  70  LEU A HD12 1 
ATOM   952   H HD13 . LEU A 1 61  ? 49.971  -20.988 82.386  1.00 131.84 ?  70  LEU A HD13 1 
ATOM   953   H HD21 . LEU A 1 61  ? 52.532  -22.370 82.205  1.00 64.56  ?  70  LEU A HD21 1 
ATOM   954   H HD22 . LEU A 1 61  ? 51.247  -22.922 81.451  1.00 64.56  ?  70  LEU A HD22 1 
ATOM   955   H HD23 . LEU A 1 61  ? 52.577  -22.620 80.636  1.00 64.56  ?  70  LEU A HD23 1 
ATOM   956   N N    . THR A 1 62  ? 51.143  -21.919 76.433  1.00 120.48 ?  71  THR A N    1 
ATOM   957   C CA   . THR A 1 62  ? 50.707  -21.765 75.058  1.00 108.34 ?  71  THR A CA   1 
ATOM   958   C C    . THR A 1 62  ? 49.395  -22.481 74.780  1.00 98.63  ?  71  THR A C    1 
ATOM   959   O O    . THR A 1 62  ? 48.391  -21.855 74.425  1.00 156.32 ?  71  THR A O    1 
ATOM   960   C CB   . THR A 1 62  ? 51.808  -22.299 74.152  1.00 106.19 ?  71  THR A CB   1 
ATOM   961   O OG1  . THR A 1 62  ? 52.094  -23.659 74.510  1.00 100.37 ?  71  THR A OG1  1 
ATOM   962   C CG2  . THR A 1 62  ? 53.034  -21.470 74.345  1.00 92.75  ?  71  THR A CG2  1 
ATOM   963   H H    . THR A 1 62  ? 51.596  -22.636 76.579  1.00 144.58 ?  71  THR A H    1 
ATOM   964   H HA   . THR A 1 62  ? 50.585  -20.822 74.865  1.00 130.01 ?  71  THR A HA   1 
ATOM   965   H HB   . THR A 1 62  ? 51.531  -22.249 73.223  1.00 127.43 ?  71  THR A HB   1 
ATOM   966   H HG1  . THR A 1 62  ? 52.700  -23.965 74.016  1.00 120.44 ?  71  THR A HG1  1 
ATOM   967   H HG21 . THR A 1 62  ? 53.748  -21.796 73.775  1.00 111.30 ?  71  THR A HG21 1 
ATOM   968   H HG22 . THR A 1 62  ? 52.847  -20.545 74.119  1.00 111.30 ?  71  THR A HG22 1 
ATOM   969   H HG23 . THR A 1 62  ? 53.323  -21.517 75.270  1.00 111.30 ?  71  THR A HG23 1 
ATOM   970   N N    . ASP A 1 63  ? 49.398  -23.792 74.937  1.00 78.15  ?  72  ASP A N    1 
ATOM   971   C CA   . ASP A 1 63  ? 48.245  -24.552 74.554  1.00 81.04  ?  72  ASP A CA   1 
ATOM   972   C C    . ASP A 1 63  ? 47.198  -24.409 75.625  1.00 107.34 ?  72  ASP A C    1 
ATOM   973   O O    . ASP A 1 63  ? 47.483  -24.073 76.781  1.00 75.34  ?  72  ASP A O    1 
ATOM   974   C CB   . ASP A 1 63  ? 48.603  -26.034 74.334  1.00 96.25  ?  72  ASP A CB   1 
ATOM   975   C CG   . ASP A 1 63  ? 49.227  -26.696 75.559  1.00 98.68  ?  72  ASP A CG   1 
ATOM   976   H H    . ASP A 1 63  ? 50.048  -24.253 75.260  1.00 93.78  ?  72  ASP A H    1 
ATOM   977   H HA   . ASP A 1 63  ? 47.886  -24.197 73.725  1.00 97.25  ?  72  ASP A HA   1 
ATOM   978   H HB2  . ASP A 1 63  ? 47.795  -26.523 74.111  1.00 115.50 ?  72  ASP A HB2  1 
ATOM   979   H HB3  . ASP A 1 63  ? 49.239  -26.099 73.604  1.00 115.50 ?  72  ASP A HB3  1 
ATOM   980   N N    . HIS A 1 64  ? 45.963  -24.656 75.230  1.00 85.83  ?  73  HIS A N    1 
ATOM   981   C CA   . HIS A 1 64  ? 44.912  -24.537 76.218  1.00 63.83  ?  73  HIS A CA   1 
ATOM   982   C C    . HIS A 1 64  ? 45.204  -25.429 77.405  1.00 70.77  ?  73  HIS A C    1 
ATOM   983   O O    . HIS A 1 64  ? 45.097  -24.997 78.548  1.00 48.22  ?  73  HIS A O    1 
ATOM   984   C CB   . HIS A 1 64  ? 43.581  -24.877 75.580  1.00 79.47  ?  73  HIS A CB   1 
ATOM   985   C CG   . HIS A 1 64  ? 42.455  -24.897 76.552  1.00 86.40  ?  73  HIS A CG   1 
ATOM   986   N ND1  . HIS A 1 64  ? 41.989  -23.758 77.180  1.00 105.04 ?  73  HIS A ND1  1 
ATOM   987   C CD2  . HIS A 1 64  ? 41.736  -25.930 77.059  1.00 80.10  ?  73  HIS A CD2  1 
ATOM   988   C CE1  . HIS A 1 64  ? 41.016  -24.087 78.019  1.00 64.81  ?  73  HIS A CE1  1 
ATOM   989   N NE2  . HIS A 1 64  ? 40.848  -25.399 77.974  1.00 63.92  ?  73  HIS A NE2  1 
ATOM   990   H H    . HIS A 1 64  ? 45.715  -24.882 74.438  1.00 103.00 ?  73  HIS A H    1 
ATOM   991   H HA   . HIS A 1 64  ? 44.872  -23.620 76.532  1.00 76.60  ?  73  HIS A HA   1 
ATOM   992   H HB2  . HIS A 1 64  ? 43.378  -24.214 74.902  1.00 95.37  ?  73  HIS A HB2  1 
ATOM   993   H HB3  . HIS A 1 64  ? 43.641  -25.756 75.175  1.00 95.37  ?  73  HIS A HB3  1 
ATOM   994   H HD1  . HIS A 1 64  ? 42.282  -22.960 77.045  1.00 126.05 ?  73  HIS A HD1  1 
ATOM   995   H HD2  . HIS A 1 64  ? 41.829  -26.829 76.837  1.00 96.12  ?  73  HIS A HD2  1 
ATOM   996   H HE1  . HIS A 1 64  ? 40.534  -23.495 78.551  1.00 77.77  ?  73  HIS A HE1  1 
ATOM   997   N N    . LYS A 1 65  ? 45.641  -26.662 77.157  1.00 81.75  ?  74  LYS A N    1 
ATOM   998   C CA   . LYS A 1 65  ? 45.828  -27.589 78.264  1.00 74.75  ?  74  LYS A CA   1 
ATOM   999   C C    . LYS A 1 65  ? 46.957  -27.131 79.182  1.00 81.99  ?  74  LYS A C    1 
ATOM   1000  O O    . LYS A 1 65  ? 46.803  -27.173 80.406  1.00 82.15  ?  74  LYS A O    1 
ATOM   1001  C CB   . LYS A 1 65  ? 46.097  -28.998 77.752  1.00 110.97 ?  74  LYS A CB   1 
ATOM   1002  C CG   . LYS A 1 65  ? 44.925  -29.641 77.040  1.00 113.68 ?  74  LYS A CG   1 
ATOM   1003  C CD   . LYS A 1 65  ? 45.224  -31.110 76.689  1.00 85.31  ?  74  LYS A CD   1 
ATOM   1004  C CE   . LYS A 1 65  ? 44.105  -31.781 75.894  1.00 95.14  ?  74  LYS A CE   1 
ATOM   1005  N NZ   . LYS A 1 65  ? 44.443  -33.171 75.469  1.00 97.19  1  74  LYS A NZ   1 
ATOM   1006  H H    . LYS A 1 65  ? 45.830  -26.977 76.379  1.00 98.10  ?  74  LYS A H    1 
ATOM   1007  H HA   . LYS A 1 65  ? 45.013  -27.616 78.789  1.00 89.70  ?  74  LYS A HA   1 
ATOM   1008  H HB2  . LYS A 1 65  ? 46.839  -28.965 77.127  1.00 133.16 ?  74  LYS A HB2  1 
ATOM   1009  H HB3  . LYS A 1 65  ? 46.330  -29.563 78.505  1.00 133.16 ?  74  LYS A HB3  1 
ATOM   1010  H HG2  . LYS A 1 65  ? 44.146  -29.618 77.618  1.00 136.41 ?  74  LYS A HG2  1 
ATOM   1011  H HG3  . LYS A 1 65  ? 44.747  -29.161 76.216  1.00 136.41 ?  74  LYS A HG3  1 
ATOM   1012  H HD2  . LYS A 1 65  ? 46.033  -31.147 76.155  1.00 102.37 ?  74  LYS A HD2  1 
ATOM   1013  H HD3  . LYS A 1 65  ? 45.347  -31.610 77.511  1.00 102.37 ?  74  LYS A HD3  1 
ATOM   1014  H HE2  . LYS A 1 65  ? 43.308  -31.822 76.445  1.00 114.16 ?  74  LYS A HE2  1 
ATOM   1015  H HE3  . LYS A 1 65  ? 43.929  -31.258 75.096  1.00 114.16 ?  74  LYS A HE3  1 
ATOM   1016  H HZ1  . LYS A 1 65  ? 43.765  -33.522 75.010  1.00 116.63 ?  74  LYS A HZ1  1 
ATOM   1017  H HZ2  . LYS A 1 65  ? 45.168  -33.164 74.953  1.00 116.63 ?  74  LYS A HZ2  1 
ATOM   1018  H HZ3  . LYS A 1 65  ? 44.601  -33.678 76.183  1.00 116.63 ?  74  LYS A HZ3  1 
ATOM   1019  N N    . SER A 1 66  ? 48.072  -26.619 78.635  1.00 85.18  ?  75  SER A N    1 
ATOM   1020  C CA   . SER A 1 66  ? 49.125  -26.179 79.548  1.00 123.21 ?  75  SER A CA   1 
ATOM   1021  C C    . SER A 1 66  ? 48.653  -24.999 80.381  1.00 110.22 ?  75  SER A C    1 
ATOM   1022  O O    . SER A 1 66  ? 49.019  -24.880 81.564  1.00 52.32  ?  75  SER A O    1 
ATOM   1023  C CB   . SER A 1 66  ? 50.374  -25.798 78.781  1.00 93.03  ?  75  SER A CB   1 
ATOM   1024  O OG   . SER A 1 66  ? 50.090  -24.716 77.940  1.00 106.98 ?  75  SER A OG   1 
ATOM   1025  H H    . SER A 1 66  ? 48.232  -26.522 77.796  1.00 102.22 ?  75  SER A H    1 
ATOM   1026  H HA   . SER A 1 66  ? 49.348  -26.906 80.151  1.00 147.85 ?  75  SER A HA   1 
ATOM   1027  H HB2  . SER A 1 66  ? 51.069  -25.543 79.407  1.00 111.64 ?  75  SER A HB2  1 
ATOM   1028  H HB3  . SER A 1 66  ? 50.664  -26.553 78.245  1.00 111.64 ?  75  SER A HB3  1 
ATOM   1029  H HG   . SER A 1 66  ? 49.484  -24.926 77.397  1.00 128.38 ?  75  SER A HG   1 
ATOM   1030  N N    . GLN A 1 67  ? 47.775  -24.175 79.801  1.00 67.96  ?  76  GLN A N    1 
ATOM   1031  C CA   . GLN A 1 67  ? 47.094  -23.140 80.554  1.00 56.22  ?  76  GLN A CA   1 
ATOM   1032  C C    . GLN A 1 67  ? 46.147  -23.742 81.591  1.00 61.44  ?  76  GLN A C    1 
ATOM   1033  O O    . GLN A 1 67  ? 46.051  -23.265 82.724  1.00 67.05  ?  76  GLN A O    1 
ATOM   1034  C CB   . GLN A 1 67  ? 46.323  -22.285 79.575  1.00 78.79  ?  76  GLN A CB   1 
ATOM   1035  C CG   . GLN A 1 67  ? 47.195  -21.650 78.563  1.00 99.20  ?  76  GLN A CG   1 
ATOM   1036  C CD   . GLN A 1 67  ? 46.398  -20.979 77.504  1.00 82.82  ?  76  GLN A CD   1 
ATOM   1037  O OE1  . GLN A 1 67  ? 45.560  -20.164 77.821  1.00 82.30  ?  76  GLN A OE1  1 
ATOM   1038  N NE2  . GLN A 1 67  ? 46.690  -21.251 76.242  1.00 104.29 ?  76  GLN A NE2  1 
ATOM   1039  H H    . GLN A 1 67  ? 47.561  -24.202 78.969  1.00 81.55  ?  76  GLN A H    1 
ATOM   1040  H HA   . GLN A 1 67  ? 47.744  -22.583 81.010  1.00 67.46  ?  76  GLN A HA   1 
ATOM   1041  H HB2  . GLN A 1 67  ? 45.679  -22.841 79.109  1.00 94.55  ?  76  GLN A HB2  1 
ATOM   1042  H HB3  . GLN A 1 67  ? 45.865  -21.582 80.061  1.00 94.55  ?  76  GLN A HB3  1 
ATOM   1043  H HG2  . GLN A 1 67  ? 47.752  -20.982 78.994  1.00 119.04 ?  76  GLN A HG2  1 
ATOM   1044  H HG3  . GLN A 1 67  ? 47.747  -22.328 78.144  1.00 119.04 ?  76  GLN A HG3  1 
ATOM   1045  H HE21 . GLN A 1 67  ? 47.325  -21.801 76.056  1.00 125.15 ?  76  GLN A HE21 1 
ATOM   1046  H HE22 . GLN A 1 67  ? 46.246  -20.877 75.607  1.00 125.15 ?  76  GLN A HE22 1 
ATOM   1047  N N    . ARG A 1 68  ? 45.457  -24.810 81.257  1.00 85.35  ?  77  ARG A N    1 
ATOM   1048  C CA   . ARG A 1 68  ? 44.594  -25.373 82.288  1.00 76.16  ?  77  ARG A CA   1 
ATOM   1049  C C    . ARG A 1 68  ? 45.396  -26.062 83.369  1.00 75.10  ?  77  ARG A C    1 
ATOM   1050  O O    . ARG A 1 68  ? 44.990  -26.061 84.546  1.00 60.03  ?  77  ARG A O    1 
ATOM   1051  C CB   . ARG A 1 68  ? 43.583  -26.320 81.666  1.00 73.97  ?  77  ARG A CB   1 
ATOM   1052  C CG   . ARG A 1 68  ? 42.497  -25.577 80.912  1.00 73.95  ?  77  ARG A CG   1 
ATOM   1053  C CD   . ARG A 1 68  ? 41.488  -24.940 81.925  1.00 72.65  ?  77  ARG A CD   1 
ATOM   1054  N NE   . ARG A 1 68  ? 40.827  -25.995 82.674  1.00 85.71  ?  77  ARG A NE   1 
ATOM   1055  C CZ   . ARG A 1 68  ? 39.782  -26.657 82.208  1.00 71.48  ?  77  ARG A CZ   1 
ATOM   1056  N NH1  . ARG A 1 68  ? 39.301  -26.331 81.005  1.00 57.40  1  77  ARG A NH1  1 
ATOM   1057  N NH2  . ARG A 1 68  ? 39.233  -27.638 82.942  1.00 58.67  1  77  ARG A NH2  1 
ATOM   1058  H H    . ARG A 1 68  ? 45.461  -25.211 80.497  1.00 102.42 ?  77  ARG A H    1 
ATOM   1059  H HA   . ARG A 1 68  ? 44.099  -24.650 82.706  1.00 91.39  ?  77  ARG A HA   1 
ATOM   1060  H HB2  . ARG A 1 68  ? 44.038  -26.907 81.041  1.00 88.76  ?  77  ARG A HB2  1 
ATOM   1061  H HB3  . ARG A 1 68  ? 43.161  -26.841 82.367  1.00 88.76  ?  77  ARG A HB3  1 
ATOM   1062  H HG2  . ARG A 1 68  ? 42.896  -24.866 80.384  1.00 88.74  ?  77  ARG A HG2  1 
ATOM   1063  H HG3  . ARG A 1 68  ? 42.014  -26.195 80.342  1.00 88.74  ?  77  ARG A HG3  1 
ATOM   1064  H HD2  . ARG A 1 68  ? 41.966  -24.370 82.547  1.00 87.18  ?  77  ARG A HD2  1 
ATOM   1065  H HD3  . ARG A 1 68  ? 40.816  -24.434 81.442  1.00 87.18  ?  77  ARG A HD3  1 
ATOM   1066  H HE   . ARG A 1 68  ? 41.011  -26.070 83.511  1.00 102.86 ?  77  ARG A HE   1 
ATOM   1067  H HH11 . ARG A 1 68  ? 39.672  -25.704 80.548  1.00 68.88  ?  77  ARG A HH11 1 
ATOM   1068  H HH12 . ARG A 1 68  ? 38.620  -26.749 80.686  1.00 68.88  ?  77  ARG A HH12 1 
ATOM   1069  H HH21 . ARG A 1 68  ? 39.557  -27.828 83.716  1.00 70.40  ?  77  ARG A HH21 1 
ATOM   1070  H HH22 . ARG A 1 68  ? 38.547  -28.064 82.646  1.00 70.40  ?  77  ARG A HH22 1 
ATOM   1071  N N    . LEU A 1 69  ? 46.552  -26.624 82.995  1.00 68.43  ?  78  LEU A N    1 
ATOM   1072  C CA   . LEU A 1 69  ? 47.396  -27.228 84.010  1.00 53.08  ?  78  LEU A CA   1 
ATOM   1073  C C    . LEU A 1 69  ? 47.948  -26.181 84.936  1.00 64.41  ?  78  LEU A C    1 
ATOM   1074  O O    . LEU A 1 69  ? 47.987  -26.416 86.147  1.00 48.18  ?  78  LEU A O    1 
ATOM   1075  C CB   . LEU A 1 69  ? 48.547  -28.004 83.408  1.00 55.25  ?  78  LEU A CB   1 
ATOM   1076  C CG   . LEU A 1 69  ? 49.534  -28.595 84.464  1.00 66.29  ?  78  LEU A CG   1 
ATOM   1077  C CD1  . LEU A 1 69  ? 48.849  -29.577 85.454  1.00 48.51  ?  78  LEU A CD1  1 
ATOM   1078  C CD2  . LEU A 1 69  ? 50.680  -29.306 83.746  1.00 77.95  ?  78  LEU A CD2  1 
ATOM   1079  H H    . LEU A 1 69  ? 46.854  -26.665 82.191  1.00 82.11  ?  78  LEU A H    1 
ATOM   1080  H HA   . LEU A 1 69  ? 46.863  -27.844 84.537  1.00 63.70  ?  78  LEU A HA   1 
ATOM   1081  H HB2  . LEU A 1 69  ? 48.189  -28.743 82.891  1.00 66.30  ?  78  LEU A HB2  1 
ATOM   1082  H HB3  . LEU A 1 69  ? 49.053  -27.412 82.829  1.00 66.30  ?  78  LEU A HB3  1 
ATOM   1083  H HG   . LEU A 1 69  ? 49.914  -27.867 84.982  1.00 79.55  ?  78  LEU A HG   1 
ATOM   1084  H HD11 . LEU A 1 69  ? 49.512  -29.907 86.081  1.00 58.21  ?  78  LEU A HD11 1 
ATOM   1085  H HD12 . LEU A 1 69  ? 48.148  -29.106 85.931  1.00 58.21  ?  78  LEU A HD12 1 
ATOM   1086  H HD13 . LEU A 1 69  ? 48.470  -30.316 84.953  1.00 58.21  ?  78  LEU A HD13 1 
ATOM   1087  H HD21 . LEU A 1 69  ? 51.289  -29.671 84.407  1.00 93.54  ?  78  LEU A HD21 1 
ATOM   1088  H HD22 . LEU A 1 69  ? 50.315  -30.022 83.202  1.00 93.54  ?  78  LEU A HD22 1 
ATOM   1089  H HD23 . LEU A 1 69  ? 51.145  -28.667 83.184  1.00 93.54  ?  78  LEU A HD23 1 
ATOM   1090  N N    . ALA A 1 70  ? 48.304  -24.992 84.406  1.00 53.09  ?  79  ALA A N    1 
ATOM   1091  C CA   . ALA A 1 70  ? 48.831  -23.954 85.292  1.00 53.66  ?  79  ALA A CA   1 
ATOM   1092  C C    . ALA A 1 70  ? 47.767  -23.498 86.292  1.00 41.37  ?  79  ALA A C    1 
ATOM   1093  O O    . ALA A 1 70  ? 48.009  -23.391 87.500  1.00 69.63  ?  79  ALA A O    1 
ATOM   1094  C CB   . ALA A 1 70  ? 49.356  -22.795 84.458  1.00 80.90  ?  79  ALA A CB   1 
ATOM   1095  H H    . ALA A 1 70  ? 48.250  -24.776 83.575  1.00 63.70  ?  79  ALA A H    1 
ATOM   1096  H HA   . ALA A 1 70  ? 49.575  -24.319 85.796  1.00 64.39  ?  79  ALA A HA   1 
ATOM   1097  H HB1  . ALA A 1 70  ? 49.703  -22.111 85.052  1.00 97.08  ?  79  ALA A HB1  1 
ATOM   1098  H HB2  . ALA A 1 70  ? 50.061  -23.119 83.877  1.00 97.08  ?  79  ALA A HB2  1 
ATOM   1099  H HB3  . ALA A 1 70  ? 48.628  -22.434 83.927  1.00 97.08  ?  79  ALA A HB3  1 
ATOM   1100  N N    . ARG A 1 71  ? 46.537  -23.365 85.824  1.00 59.06  ?  80  ARG A N    1 
ATOM   1101  C CA   . ARG A 1 71  ? 45.509  -22.788 86.670  1.00 53.66  ?  80  ARG A CA   1 
ATOM   1102  C C    . ARG A 1 71  ? 45.185  -23.721 87.828  1.00 59.03  ?  80  ARG A C    1 
ATOM   1103  O O    . ARG A 1 71  ? 44.913  -23.297 88.956  1.00 99.29  ?  80  ARG A O    1 
ATOM   1104  C CB   . ARG A 1 71  ? 44.316  -22.494 85.773  1.00 77.29  ?  80  ARG A CB   1 
ATOM   1105  C CG   . ARG A 1 71  ? 43.554  -21.252 86.184  1.00 87.12  ?  80  ARG A CG   1 
ATOM   1106  C CD   . ARG A 1 71  ? 42.113  -21.341 85.774  1.00 63.98  ?  80  ARG A CD   1 
ATOM   1107  N NE   . ARG A 1 71  ? 41.247  -21.789 86.872  1.00 61.74  ?  80  ARG A NE   1 
ATOM   1108  C CZ   . ARG A 1 71  ? 40.649  -20.951 87.736  1.00 60.73  ?  80  ARG A CZ   1 
ATOM   1109  N NH1  . ARG A 1 71  ? 40.813  -19.634 87.588  1.00 57.30  1  80  ARG A NH1  1 
ATOM   1110  N NH2  . ARG A 1 71  ? 39.873  -21.397 88.734  1.00 71.69  1  80  ARG A NH2  1 
ATOM   1111  H H    . ARG A 1 71  ? 46.276  -23.597 85.038  1.00 70.87  ?  80  ARG A H    1 
ATOM   1112  H HA   . ARG A 1 71  ? 45.829  -21.949 87.036  1.00 64.39  ?  80  ARG A HA   1 
ATOM   1113  H HB2  . ARG A 1 71  ? 44.629  -22.365 84.864  1.00 92.75  ?  80  ARG A HB2  1 
ATOM   1114  H HB3  . ARG A 1 71  ? 43.703  -23.245 85.808  1.00 92.75  ?  80  ARG A HB3  1 
ATOM   1115  H HG2  . ARG A 1 71  ? 43.591  -21.157 87.149  1.00 104.54 ?  80  ARG A HG2  1 
ATOM   1116  H HG3  . ARG A 1 71  ? 43.947  -20.477 85.754  1.00 104.54 ?  80  ARG A HG3  1 
ATOM   1117  H HD2  . ARG A 1 71  ? 41.809  -20.465 85.489  1.00 76.77  ?  80  ARG A HD2  1 
ATOM   1118  H HD3  . ARG A 1 71  ? 42.029  -21.976 85.046  1.00 76.77  ?  80  ARG A HD3  1 
ATOM   1119  H HE   . ARG A 1 71  ? 41.217  -22.631 87.043  1.00 74.09  ?  80  ARG A HE   1 
ATOM   1120  H HH11 . ARG A 1 71  ? 41.309  -19.331 86.954  1.00 68.76  ?  80  ARG A HH11 1 
ATOM   1121  H HH12 . ARG A 1 71  ? 40.431  -19.089 88.133  1.00 68.76  ?  80  ARG A HH12 1 
ATOM   1122  H HH21 . ARG A 1 71  ? 39.752  -22.241 88.839  1.00 86.03  ?  80  ARG A HH21 1 
ATOM   1123  H HH22 . ARG A 1 71  ? 39.494  -20.838 89.266  1.00 86.03  ?  80  ARG A HH22 1 
ATOM   1124  N N    . LEU A 1 72  ? 45.392  -24.986 87.587  1.00 71.14  ?  81  LEU A N    1 
ATOM   1125  C CA   . LEU A 1 72  ? 45.184  -25.984 88.612  1.00 67.79  ?  81  LEU A CA   1 
ATOM   1126  C C    . LEU A 1 72  ? 46.344  -25.907 89.593  1.00 67.14  ?  81  LEU A C    1 
ATOM   1127  O O    . LEU A 1 72  ? 46.143  -25.815 90.807  1.00 47.58  ?  81  LEU A O    1 
ATOM   1128  C CB   . LEU A 1 72  ? 45.010  -27.343 87.906  1.00 73.78  ?  81  LEU A CB   1 
ATOM   1129  C CG   . LEU A 1 72  ? 45.147  -28.605 88.743  1.00 73.32  ?  81  LEU A CG   1 
ATOM   1130  C CD1  . LEU A 1 72  ? 44.227  -28.655 89.868  1.00 70.71  ?  81  LEU A CD1  1 
ATOM   1131  C CD2  . LEU A 1 72  ? 44.948  -29.816 87.926  1.00 59.69  ?  81  LEU A CD2  1 
ATOM   1132  H H    . LEU A 1 72  ? 45.656  -25.303 86.832  1.00 85.37  ?  81  LEU A H    1 
ATOM   1133  H HA   . LEU A 1 72  ? 44.366  -25.784 89.092  1.00 81.35  ?  81  LEU A HA   1 
ATOM   1134  H HB2  . LEU A 1 72  ? 44.124  -27.362 87.511  1.00 88.53  ?  81  LEU A HB2  1 
ATOM   1135  H HB3  . LEU A 1 72  ? 45.673  -27.399 87.200  1.00 88.53  ?  81  LEU A HB3  1 
ATOM   1136  H HG   . LEU A 1 72  ? 46.048  -28.639 89.101  1.00 87.98  ?  81  LEU A HG   1 
ATOM   1137  H HD11 . LEU A 1 72  ? 44.369  -29.482 90.355  1.00 84.85  ?  81  LEU A HD11 1 
ATOM   1138  H HD12 . LEU A 1 72  ? 44.396  -27.896 90.448  1.00 84.85  ?  81  LEU A HD12 1 
ATOM   1139  H HD13 . LEU A 1 72  ? 43.317  -28.620 89.534  1.00 84.85  ?  81  LEU A HD13 1 
ATOM   1140  H HD21 . LEU A 1 72  ? 45.043  -30.598 88.492  1.00 71.62  ?  81  LEU A HD21 1 
ATOM   1141  H HD22 . LEU A 1 72  ? 44.059  -29.793 87.539  1.00 71.62  ?  81  LEU A HD22 1 
ATOM   1142  H HD23 . LEU A 1 72  ? 45.615  -29.835 87.222  1.00 71.62  ?  81  LEU A HD23 1 
ATOM   1143  N N    . VAL A 1 73  ? 47.560  -25.754 89.075  1.00 69.99  ?  82  VAL A N    1 
ATOM   1144  C CA   . VAL A 1 73  ? 48.714  -25.598 89.954  1.00 54.61  ?  82  VAL A CA   1 
ATOM   1145  C C    . VAL A 1 73  ? 48.576  -24.355 90.838  1.00 55.40  ?  82  VAL A C    1 
ATOM   1146  O O    . VAL A 1 73  ? 48.642  -24.440 92.062  1.00 55.12  ?  82  VAL A O    1 
ATOM   1147  C CB   . VAL A 1 73  ? 49.986  -25.548 89.101  1.00 68.90  ?  82  VAL A CB   1 
ATOM   1148  C CG1  . VAL A 1 73  ? 51.158  -25.001 89.887  1.00 80.19  ?  82  VAL A CG1  1 
ATOM   1149  C CG2  . VAL A 1 73  ? 50.253  -26.905 88.558  1.00 77.66  ?  82  VAL A CG2  1 
ATOM   1150  H H    . VAL A 1 73  ? 47.741  -25.737 88.235  1.00 83.98  ?  82  VAL A H    1 
ATOM   1151  H HA   . VAL A 1 73  ? 48.774  -26.373 90.535  1.00 65.54  ?  82  VAL A HA   1 
ATOM   1152  H HB   . VAL A 1 73  ? 49.833  -24.955 88.349  1.00 82.68  ?  82  VAL A HB   1 
ATOM   1153  H HG11 . VAL A 1 73  ? 51.941  -24.985 89.316  1.00 96.23  ?  82  VAL A HG11 1 
ATOM   1154  H HG12 . VAL A 1 73  ? 50.945  -24.102 90.184  1.00 96.23  ?  82  VAL A HG12 1 
ATOM   1155  H HG13 . VAL A 1 73  ? 51.318  -25.574 90.653  1.00 96.23  ?  82  VAL A HG13 1 
ATOM   1156  H HG21 . VAL A 1 73  ? 51.058  -26.876 88.017  1.00 93.20  ?  82  VAL A HG21 1 
ATOM   1157  H HG22 . VAL A 1 73  ? 50.372  -27.522 89.296  1.00 93.20  ?  82  VAL A HG22 1 
ATOM   1158  H HG23 . VAL A 1 73  ? 49.499  -27.181 88.014  1.00 93.20  ?  82  VAL A HG23 1 
ATOM   1159  N N    . LEU A 1 74  ? 48.331  -23.191 90.245  1.00 49.24  ?  83  LEU A N    1 
ATOM   1160  C CA   . LEU A 1 74  ? 48.289  -21.982 91.075  1.00 66.95  ?  83  LEU A CA   1 
ATOM   1161  C C    . LEU A 1 74  ? 47.142  -22.031 92.071  1.00 54.12  ?  83  LEU A C    1 
ATOM   1162  O O    . LEU A 1 74  ? 47.265  -21.558 93.208  1.00 101.55 ?  83  LEU A O    1 
ATOM   1163  C CB   . LEU A 1 74  ? 48.201  -20.758 90.172  1.00 82.14  ?  83  LEU A CB   1 
ATOM   1164  C CG   . LEU A 1 74  ? 49.430  -20.551 89.259  1.00 68.15  ?  83  LEU A CG   1 
ATOM   1165  C CD1  . LEU A 1 74  ? 49.208  -19.539 88.203  1.00 89.83  ?  83  LEU A CD1  1 
ATOM   1166  C CD2  . LEU A 1 74  ? 50.639  -20.190 90.034  1.00 77.32  ?  83  LEU A CD2  1 
ATOM   1167  H H    . LEU A 1 74  ? 48.192  -23.071 89.405  1.00 59.08  ?  83  LEU A H    1 
ATOM   1168  H HA   . LEU A 1 74  ? 49.116  -21.920 91.579  1.00 80.35  ?  83  LEU A HA   1 
ATOM   1169  H HB2  . LEU A 1 74  ? 47.422  -20.848 89.601  1.00 98.57  ?  83  LEU A HB2  1 
ATOM   1170  H HB3  . LEU A 1 74  ? 48.110  -19.968 90.727  1.00 98.57  ?  83  LEU A HB3  1 
ATOM   1171  H HG   . LEU A 1 74  ? 49.618  -21.391 88.813  1.00 81.78  ?  83  LEU A HG   1 
ATOM   1172  H HD11 . LEU A 1 74  ? 50.014  -19.459 87.669  1.00 107.80 ?  83  LEU A HD11 1 
ATOM   1173  H HD12 . LEU A 1 74  ? 48.468  -19.824 87.645  1.00 107.80 ?  83  LEU A HD12 1 
ATOM   1174  H HD13 . LEU A 1 74  ? 49.001  -18.688 88.620  1.00 107.80 ?  83  LEU A HD13 1 
ATOM   1175  H HD21 . LEU A 1 74  ? 51.382  -20.070 89.421  1.00 92.78  ?  83  LEU A HD21 1 
ATOM   1176  H HD22 . LEU A 1 74  ? 50.471  -19.365 90.515  1.00 92.78  ?  83  LEU A HD22 1 
ATOM   1177  H HD23 . LEU A 1 74  ? 50.838  -20.904 90.660  1.00 92.78  ?  83  LEU A HD23 1 
ATOM   1178  N N    . GLY A 1 75  ? 46.034  -22.671 91.668  1.00 68.79  ?  84  GLY A N    1 
ATOM   1179  C CA   . GLY A 1 75  ? 44.878  -22.757 92.534  1.00 59.17  ?  84  GLY A CA   1 
ATOM   1180  C C    . GLY A 1 75  ? 45.121  -23.697 93.694  1.00 42.99  ?  84  GLY A C    1 
ATOM   1181  O O    . GLY A 1 75  ? 44.773  -23.373 94.834  1.00 57.06  ?  84  GLY A O    1 
ATOM   1182  H H    . GLY A 1 75  ? 45.939  -23.056 90.904  1.00 82.54  ?  84  GLY A H    1 
ATOM   1183  H HA2  . GLY A 1 75  ? 44.668  -21.878 92.886  1.00 71.01  ?  84  GLY A HA2  1 
ATOM   1184  H HA3  . GLY A 1 75  ? 44.115  -23.079 92.029  1.00 71.01  ?  84  GLY A HA3  1 
ATOM   1185  N N    . CYS A 1 76  ? 45.860  -24.761 93.474  1.00 99.56  ?  85  CYS A N    1 
ATOM   1186  C CA   . CYS A 1 76  ? 46.154  -25.539 94.650  1.00 95.75  ?  85  CYS A CA   1 
ATOM   1187  C C    . CYS A 1 76  ? 47.081  -24.772 95.564  1.00 95.25  ?  85  CYS A C    1 
ATOM   1188  O O    . CYS A 1 76  ? 46.788  -24.604 96.753  1.00 46.04  ?  85  CYS A O    1 
ATOM   1189  C CB   . CYS A 1 76  ? 46.760  -26.863 94.250  1.00 93.52  ?  85  CYS A CB   1 
ATOM   1190  S SG   . CYS A 1 76  ? 45.643  -27.947 93.387  1.00 81.44  ?  85  CYS A SG   1 
ATOM   1191  H H    . CYS A 1 76  ? 46.180  -25.036 92.725  1.00 119.47 ?  85  CYS A H    1 
ATOM   1192  H HA   . CYS A 1 76  ? 45.331  -25.715 95.131  1.00 114.90 ?  85  CYS A HA   1 
ATOM   1193  H HB2  . CYS A 1 76  ? 47.517  -26.696 93.667  1.00 112.23 ?  85  CYS A HB2  1 
ATOM   1194  H HB3  . CYS A 1 76  ? 47.058  -27.323 95.050  1.00 112.23 ?  85  CYS A HB3  1 
ATOM   1195  H HG   . CYS A 1 76  ? 46.218  -28.965 93.116  1.00 97.72  ?  85  CYS A HG   1 
ATOM   1196  N N    . ILE A 1 77  ? 48.098  -24.147 94.991  1.00 86.64  ?  86  ILE A N    1 
ATOM   1197  C CA   . ILE A 1 77  ? 49.036  -23.374 95.790  1.00 118.61 ?  86  ILE A CA   1 
ATOM   1198  C C    . ILE A 1 77  ? 48.317  -22.307 96.585  1.00 72.79  ?  86  ILE A C    1 
ATOM   1199  O O    . ILE A 1 77  ? 48.563  -22.156 97.791  1.00 58.27  ?  86  ILE A O    1 
ATOM   1200  C CB   . ILE A 1 77  ? 50.086  -22.761 94.861  1.00 79.27  ?  86  ILE A CB   1 
ATOM   1201  C CG1  . ILE A 1 77  ? 50.922  -23.881 94.268  1.00 56.92  ?  86  ILE A CG1  1 
ATOM   1202  C CG2  . ILE A 1 77  ? 50.860  -21.709 95.564  1.00 60.92  ?  86  ILE A CG2  1 
ATOM   1203  C CD1  . ILE A 1 77  ? 51.713  -23.480 93.079  1.00 63.88  ?  86  ILE A CD1  1 
ATOM   1204  H H    . ILE A 1 77  ? 48.267  -24.153 94.148  1.00 103.97 ?  86  ILE A H    1 
ATOM   1205  H HA   . ILE A 1 77  ? 49.488  -23.964 96.412  1.00 142.34 ?  86  ILE A HA   1 
ATOM   1206  H HB   . ILE A 1 77  ? 49.614  -22.333 94.129  1.00 95.12  ?  86  ILE A HB   1 
ATOM   1207  H HG12 . ILE A 1 77  ? 51.543  -24.197 94.943  1.00 68.31  ?  86  ILE A HG12 1 
ATOM   1208  H HG13 . ILE A 1 77  ? 50.332  -24.603 94.002  1.00 68.31  ?  86  ILE A HG13 1 
ATOM   1209  H HG21 . ILE A 1 77  ? 51.516  -21.339 94.953  1.00 73.11  ?  86  ILE A HG21 1 
ATOM   1210  H HG22 . ILE A 1 77  ? 50.251  -21.013 95.857  1.00 73.11  ?  86  ILE A HG22 1 
ATOM   1211  H HG23 . ILE A 1 77  ? 51.305  -22.104 96.329  1.00 73.11  ?  86  ILE A HG23 1 
ATOM   1212  H HD11 . ILE A 1 77  ? 52.216  -24.247 92.762  1.00 76.66  ?  86  ILE A HD11 1 
ATOM   1213  H HD12 . ILE A 1 77  ? 51.107  -23.173 92.386  1.00 76.66  ?  86  ILE A HD12 1 
ATOM   1214  H HD13 . ILE A 1 77  ? 52.319  -22.766 93.329  1.00 76.66  ?  86  ILE A HD13 1 
ATOM   1215  N N    . THR A 1 78  ? 47.358  -21.613 95.950  1.00 63.82  ?  87  THR A N    1 
ATOM   1216  C CA   . THR A 1 78  ? 46.688  -20.500 96.619  1.00 47.13  ?  87  THR A CA   1 
ATOM   1217  C C    . THR A 1 78  ? 45.903  -20.937 97.837  1.00 79.63  ?  87  THR A C    1 
ATOM   1218  O O    . THR A 1 78  ? 45.913  -20.254 98.862  1.00 52.87  ?  87  THR A O    1 
ATOM   1219  C CB   . THR A 1 78  ? 45.795  -19.813 95.586  1.00 75.68  ?  87  THR A CB   1 
ATOM   1220  O OG1  . THR A 1 78  ? 46.628  -19.222 94.580  1.00 55.08  ?  87  THR A OG1  1 
ATOM   1221  C CG2  . THR A 1 78  ? 44.943  -18.699 96.156  1.00 39.64  ?  87  THR A CG2  1 
ATOM   1222  H H    . THR A 1 78  ? 47.087  -21.766 95.148  1.00 76.58  ?  87  THR A H    1 
ATOM   1223  H HA   . THR A 1 78  ? 47.356  -19.859 96.909  1.00 56.55  ?  87  THR A HA   1 
ATOM   1224  H HB   . THR A 1 78  ? 45.210  -20.470 95.176  1.00 90.82  ?  87  THR A HB   1 
ATOM   1225  H HG1  . THR A 1 78  ? 47.090  -19.814 94.204  1.00 66.09  ?  87  THR A HG1  1 
ATOM   1226  H HG21 . THR A 1 78  ? 44.401  -18.305 95.455  1.00 47.57  ?  87  THR A HG21 1 
ATOM   1227  H HG22 . THR A 1 78  ? 44.359  -19.050 96.847  1.00 47.57  ?  87  THR A HG22 1 
ATOM   1228  H HG23 . THR A 1 78  ? 45.510  -18.013 96.541  1.00 47.57  ?  87  THR A HG23 1 
ATOM   1229  N N    . MET A 1 79  ? 45.246  -22.081 97.751  1.00 39.00  ?  88  MET A N    1 
ATOM   1230  C CA   . MET A 1 79  ? 44.434  -22.568 98.869  1.00 46.57  ?  88  MET A CA   1 
ATOM   1231  C C    . MET A 1 79  ? 45.333  -22.985 100.026 1.00 68.92  ?  88  MET A C    1 
ATOM   1232  O O    . MET A 1 79  ? 45.043  -22.738 101.203 1.00 134.47 ?  88  MET A O    1 
ATOM   1233  C CB   . MET A 1 79  ? 43.499  -23.705 98.343  1.00 37.24  ?  88  MET A CB   1 
ATOM   1234  C CG   . MET A 1 79  ? 42.540  -23.329 97.302  1.00 212.59 ?  88  MET A CG   1 
ATOM   1235  S SD   . MET A 1 79  ? 41.492  -22.205 98.047  1.00 95.88  ?  88  MET A SD   1 
ATOM   1236  C CE   . MET A 1 79  ? 40.078  -22.322 97.043  1.00 79.60  ?  88  MET A CE   1 
ATOM   1237  H H    . MET A 1 79  ? 45.250  -22.597 97.063  1.00 46.80  ?  88  MET A H    1 
ATOM   1238  H HA   . MET A 1 79  ? 43.865  -21.843 99.172  1.00 55.88  ?  88  MET A HA   1 
ATOM   1239  H HB2  . MET A 1 79  ? 44.056  -24.411 97.980  1.00 44.69  ?  88  MET A HB2  1 
ATOM   1240  H HB3  . MET A 1 79  ? 42.990  -24.050 99.093  1.00 44.69  ?  88  MET A HB3  1 
ATOM   1241  H HG2  . MET A 1 79  ? 42.994  -22.904 96.558  1.00 255.10 ?  88  MET A HG2  1 
ATOM   1242  H HG3  . MET A 1 79  ? 42.031  -24.103 97.014  1.00 255.10 ?  88  MET A HG3  1 
ATOM   1243  H HE1  . MET A 1 79  ? 39.401  -21.714 97.380  1.00 95.52  ?  88  MET A HE1  1 
ATOM   1244  H HE2  . MET A 1 79  ? 40.316  -22.082 96.134  1.00 95.52  ?  88  MET A HE2  1 
ATOM   1245  H HE3  . MET A 1 79  ? 39.747  -23.233 97.070  1.00 95.52  ?  88  MET A HE3  1 
ATOM   1246  N N    . ALA A 1 80  ? 46.457  -23.580 99.675  1.00 57.83  ?  89  ALA A N    1 
ATOM   1247  C CA   . ALA A 1 80  ? 47.469  -23.961 100.645 1.00 85.18  ?  89  ALA A CA   1 
ATOM   1248  C C    . ALA A 1 80  ? 48.066  -22.756 101.367 1.00 59.46  ?  89  ALA A C    1 
ATOM   1249  O O    . ALA A 1 80  ? 48.244  -22.795 102.599 1.00 56.99  ?  89  ALA A O    1 
ATOM   1250  C CB   . ALA A 1 80  ? 48.552  -24.767 99.941  1.00 140.51 ?  89  ALA A CB   1 
ATOM   1251  H H    . ALA A 1 80  ? 46.663  -23.779 98.864  1.00 69.40  ?  89  ALA A H    1 
ATOM   1252  H HA   . ALA A 1 80  ? 47.061  -24.534 101.314 1.00 102.22 ?  89  ALA A HA   1 
ATOM   1253  H HB1  . ALA A 1 80  ? 49.228  -25.022 100.589 1.00 168.61 ?  89  ALA A HB1  1 
ATOM   1254  H HB2  . ALA A 1 80  ? 48.152  -25.560 99.551  1.00 168.61 ?  89  ALA A HB2  1 
ATOM   1255  H HB3  . ALA A 1 80  ? 48.950  -24.220 99.245  1.00 168.61 ?  89  ALA A HB3  1 
ATOM   1256  N N    . TYR A 1 81  ? 48.382  -21.674 100.624 1.00 48.16  ?  90  TYR A N    1 
ATOM   1257  C CA   . TYR A 1 81  ? 48.936  -20.483 101.244 1.00 65.00  ?  90  TYR A CA   1 
ATOM   1258  C C    . TYR A 1 81  ? 47.903  -19.821 102.138 1.00 78.30  ?  90  TYR A C    1 
ATOM   1259  O O    . TYR A 1 81  ? 48.171  -19.602 103.332 1.00 55.06  ?  90  TYR A O    1 
ATOM   1260  C CB   . TYR A 1 81  ? 49.455  -19.531 100.160 1.00 85.95  ?  90  TYR A CB   1 
ATOM   1261  C CG   . TYR A 1 81  ? 50.161  -18.286 100.671 1.00 78.66  ?  90  TYR A CG   1 
ATOM   1262  C CD1  . TYR A 1 81  ? 51.541  -18.266 100.865 1.00 79.87  ?  90  TYR A CD1  1 
ATOM   1263  C CD2  . TYR A 1 81  ? 49.444  -17.128 100.969 1.00 84.51  ?  90  TYR A CD2  1 
ATOM   1264  C CE1  . TYR A 1 81  ? 52.179  -17.139 101.333 1.00 72.17  ?  90  TYR A CE1  1 
ATOM   1265  C CE2  . TYR A 1 81  ? 50.086  -15.986 101.435 1.00 93.75  ?  90  TYR A CE2  1 
ATOM   1266  C CZ   . TYR A 1 81  ? 51.453  -15.987 101.613 1.00 93.91  ?  90  TYR A CZ   1 
ATOM   1267  O OH   . TYR A 1 81  ? 52.068  -14.836 102.088 1.00 98.83  ?  90  TYR A OH   1 
ATOM   1268  H H    . TYR A 1 81  ? 48.281  -21.618 99.772  1.00 57.79  ?  90  TYR A H    1 
ATOM   1269  H HA   . TYR A 1 81  ? 49.689  -20.740 101.799 1.00 78.00  ?  90  TYR A HA   1 
ATOM   1270  H HB2  . TYR A 1 81  ? 50.084  -20.015 99.602  1.00 103.14 ?  90  TYR A HB2  1 
ATOM   1271  H HB3  . TYR A 1 81  ? 48.702  -19.239 99.622  1.00 103.14 ?  90  TYR A HB3  1 
ATOM   1272  H HD1  . TYR A 1 81  ? 52.040  -19.028 100.676 1.00 95.85  ?  90  TYR A HD1  1 
ATOM   1273  H HD2  . TYR A 1 81  ? 48.522  -17.117 100.846 1.00 101.41 ?  90  TYR A HD2  1 
ATOM   1274  H HE1  . TYR A 1 81  ? 53.102  -17.145 101.451 1.00 86.60  ?  90  TYR A HE1  1 
ATOM   1275  H HE2  . TYR A 1 81  ? 49.593  -15.221 101.626 1.00 112.50 ?  90  TYR A HE2  1 
ATOM   1276  H HH   . TYR A 1 81  ? 52.895  -14.964 102.166 1.00 118.60 ?  90  TYR A HH   1 
ATOM   1277  N N    . VAL A 1 82  ? 46.674  -19.631 101.625 1.00 58.19  ?  91  VAL A N    1 
ATOM   1278  C CA   . VAL A 1 82  ? 45.609  -19.007 102.411 1.00 71.18  ?  91  VAL A CA   1 
ATOM   1279  C C    . VAL A 1 82  ? 45.317  -19.803 103.679 1.00 77.23  ?  91  VAL A C    1 
ATOM   1280  O O    . VAL A 1 82  ? 45.333  -19.253 104.789 1.00 59.84  ?  91  VAL A O    1 
ATOM   1281  C CB   . VAL A 1 82  ? 44.348  -18.898 101.554 1.00 79.82  ?  91  VAL A CB   1 
ATOM   1282  C CG1  . VAL A 1 82  ? 43.139  -18.472 102.386 1.00 49.65  ?  91  VAL A CG1  1 
ATOM   1283  C CG2  . VAL A 1 82  ? 44.599  -17.988 100.431 1.00 48.84  ?  91  VAL A CG2  1 
ATOM   1284  H H    . VAL A 1 82  ? 46.439  -19.856 100.829 1.00 69.83  ?  91  VAL A H    1 
ATOM   1285  H HA   . VAL A 1 82  ? 45.882  -18.113 102.669 1.00 85.41  ?  91  VAL A HA   1 
ATOM   1286  H HB   . VAL A 1 82  ? 44.152  -19.772 101.183 1.00 95.78  ?  91  VAL A HB   1 
ATOM   1287  H HG11 . VAL A 1 82  ? 42.363  -18.415 101.807 1.00 59.58  ?  91  VAL A HG11 1 
ATOM   1288  H HG12 . VAL A 1 82  ? 42.986  -19.131 103.081 1.00 59.58  ?  91  VAL A HG12 1 
ATOM   1289  H HG13 . VAL A 1 82  ? 43.320  -17.606 102.784 1.00 59.58  ?  91  VAL A HG13 1 
ATOM   1290  H HG21 . VAL A 1 82  ? 43.795  -17.924 99.892  1.00 58.61  ?  91  VAL A HG21 1 
ATOM   1291  H HG22 . VAL A 1 82  ? 44.835  -17.114 100.779 1.00 58.61  ?  91  VAL A HG22 1 
ATOM   1292  H HG23 . VAL A 1 82  ? 45.328  -18.340 99.897  1.00 58.61  ?  91  VAL A HG23 1 
ATOM   1293  N N    . TRP A 1 83  ? 45.025  -21.118 103.543 1.00 62.91  ?  92  TRP A N    1 
ATOM   1294  C CA   . TRP A 1 83  ? 44.450  -21.843 104.682 1.00 61.72  ?  92  TRP A CA   1 
ATOM   1295  C C    . TRP A 1 83  ? 45.481  -22.458 105.585 1.00 69.04  ?  92  TRP A C    1 
ATOM   1296  O O    . TRP A 1 83  ? 45.136  -22.701 106.743 1.00 69.67  ?  92  TRP A O    1 
ATOM   1297  C CB   . TRP A 1 83  ? 43.462  -22.926 104.238 1.00 80.65  ?  92  TRP A CB   1 
ATOM   1298  C CG   . TRP A 1 83  ? 42.281  -22.364 103.580 1.00 79.60  ?  92  TRP A CG   1 
ATOM   1299  C CD1  . TRP A 1 83  ? 41.830  -22.659 102.330 1.00 59.96  ?  92  TRP A CD1  1 
ATOM   1300  C CD2  . TRP A 1 83  ? 41.396  -21.346 104.106 1.00 48.29  ?  92  TRP A CD2  1 
ATOM   1301  N NE1  . TRP A 1 83  ? 40.730  -21.871 102.028 1.00 51.37  ?  92  TRP A NE1  1 
ATOM   1302  C CE2  . TRP A 1 83  ? 40.433  -21.079 103.110 1.00 47.70  ?  92  TRP A CE2  1 
ATOM   1303  C CE3  . TRP A 1 83  ? 41.319  -20.659 105.324 1.00 64.43  ?  92  TRP A CE3  1 
ATOM   1304  C CZ2  . TRP A 1 83  ? 39.412  -20.146 103.285 1.00 60.65  ?  92  TRP A CZ2  1 
ATOM   1305  C CZ3  . TRP A 1 83  ? 40.314  -19.738 105.511 1.00 70.41  ?  92  TRP A CZ3  1 
ATOM   1306  C CH2  . TRP A 1 83  ? 39.360  -19.478 104.492 1.00 73.93  ?  92  TRP A CH2  1 
ATOM   1307  H H    . TRP A 1 83  ? 45.147  -21.588 102.832 1.00 75.49  ?  92  TRP A H    1 
ATOM   1308  H HA   . TRP A 1 83  ? 43.951  -21.206 105.217 1.00 74.06  ?  92  TRP A HA   1 
ATOM   1309  H HB2  . TRP A 1 83  ? 43.902  -23.520 103.610 1.00 96.78  ?  92  TRP A HB2  1 
ATOM   1310  H HB3  . TRP A 1 83  ? 43.165  -23.424 105.016 1.00 96.78  ?  92  TRP A HB3  1 
ATOM   1311  H HD1  . TRP A 1 83  ? 42.233  -23.260 101.745 1.00 71.95  ?  92  TRP A HD1  1 
ATOM   1312  H HE1  . TRP A 1 83  ? 40.281  -21.901 101.294 1.00 61.64  ?  92  TRP A HE1  1 
ATOM   1313  H HE3  . TRP A 1 83  ? 41.946  -20.814 105.993 1.00 77.31  ?  92  TRP A HE3  1 
ATOM   1314  H HZ2  . TRP A 1 83  ? 38.782  -19.989 102.619 1.00 72.78  ?  92  TRP A HZ2  1 
ATOM   1315  H HZ3  . TRP A 1 83  ? 40.264  -19.273 106.315 1.00 84.49  ?  92  TRP A HZ3  1 
ATOM   1316  H HH2  . TRP A 1 83  ? 38.686  -18.855 104.643 1.00 88.72  ?  92  TRP A HH2  1 
ATOM   1317  N N    . GLY A 1 84  ? 46.721  -22.662 105.099 1.00 75.10  ?  93  GLY A N    1 
ATOM   1318  C CA   . GLY A 1 84  ? 47.815  -23.138 105.953 1.00 66.10  ?  93  GLY A CA   1 
ATOM   1319  C C    . GLY A 1 84  ? 47.675  -24.591 106.357 1.00 64.55  ?  93  GLY A C    1 
ATOM   1320  O O    . GLY A 1 84  ? 47.497  -25.486 105.513 1.00 57.05  ?  93  GLY A O    1 
ATOM   1321  H H    . GLY A 1 84  ? 46.948  -22.530 104.280 1.00 90.11  ?  93  GLY A H    1 
ATOM   1322  H HA2  . GLY A 1 84  ? 48.657  -23.033 105.482 1.00 79.31  ?  93  GLY A HA2  1 
ATOM   1323  H HA3  . GLY A 1 84  ? 47.849  -22.600 106.759 1.00 79.31  ?  93  GLY A HA3  1 
ATOM   1324  N N    . LYS A 1 85  ? 47.801  -24.838 107.672 1.00 73.23  ?  94  LYS A N    1 
ATOM   1325  C CA   . LYS A 1 85  ? 47.604  -26.180 108.225 1.00 68.99  ?  94  LYS A CA   1 
ATOM   1326  C C    . LYS A 1 85  ? 46.111  -26.564 108.373 1.00 78.63  ?  94  LYS A C    1 
ATOM   1327  O O    . LYS A 1 85  ? 45.806  -27.724 108.674 1.00 93.45  ?  94  LYS A O    1 
ATOM   1328  C CB   . LYS A 1 85  ? 48.341  -26.276 109.589 1.00 68.30  ?  94  LYS A CB   1 
ATOM   1329  C CG   . LYS A 1 85  ? 49.885  -26.337 109.504 1.00 110.60 ?  94  LYS A CG   1 
ATOM   1330  C CD   . LYS A 1 85  ? 50.606  -26.405 110.873 1.00 73.39  ?  94  LYS A CD   1 
ATOM   1331  C CE   . LYS A 1 85  ? 52.113  -26.600 110.681 1.00 101.95 ?  94  LYS A CE   1 
ATOM   1332  N NZ   . LYS A 1 85  ? 52.892  -26.480 111.923 1.00 164.48 1  94  LYS A NZ   1 
ATOM   1333  H H    . LYS A 1 85  ? 48.000  -24.243 108.261 1.00 87.87  ?  94  LYS A H    1 
ATOM   1334  H HA   . LYS A 1 85  ? 48.013  -26.824 107.625 1.00 82.79  ?  94  LYS A HA   1 
ATOM   1335  H HB2  . LYS A 1 85  ? 48.109  -25.498 110.120 1.00 81.96  ?  94  LYS A HB2  1 
ATOM   1336  H HB3  . LYS A 1 85  ? 48.042  -27.079 110.044 1.00 81.96  ?  94  LYS A HB3  1 
ATOM   1337  H HG2  . LYS A 1 85  ? 50.136  -27.127 109.000 1.00 132.72 ?  94  LYS A HG2  1 
ATOM   1338  H HG3  . LYS A 1 85  ? 50.201  -25.543 109.045 1.00 132.72 ?  94  LYS A HG3  1 
ATOM   1339  H HD2  . LYS A 1 85  ? 50.464  -25.575 111.354 1.00 88.07  ?  94  LYS A HD2  1 
ATOM   1340  H HD3  . LYS A 1 85  ? 50.262  -27.155 111.382 1.00 88.07  ?  94  LYS A HD3  1 
ATOM   1341  H HE2  . LYS A 1 85  ? 52.269  -27.486 110.318 1.00 122.34 ?  94  LYS A HE2  1 
ATOM   1342  H HE3  . LYS A 1 85  ? 52.439  -25.929 110.061 1.00 122.34 ?  94  LYS A HE3  1 
ATOM   1343  H HZ1  . LYS A 1 85  ? 53.757  -26.602 111.752 1.00 197.38 ?  94  LYS A HZ1  1 
ATOM   1344  H HZ2  . LYS A 1 85  ? 52.778  -25.671 112.275 1.00 197.38 ?  94  LYS A HZ2  1 
ATOM   1345  H HZ3  . LYS A 1 85  ? 52.623  -27.093 112.510 1.00 197.38 ?  94  LYS A HZ3  1 
ATOM   1346  N N    . GLY A 1 86  ? 45.183  -25.639 108.112 1.00 85.20  ?  95  GLY A N    1 
ATOM   1347  C CA   . GLY A 1 86  ? 43.755  -25.888 108.235 1.00 65.84  ?  95  GLY A CA   1 
ATOM   1348  C C    . GLY A 1 86  ? 43.161  -25.816 109.635 1.00 69.69  ?  95  GLY A C    1 
ATOM   1349  O O    . GLY A 1 86  ? 42.126  -26.445 109.902 1.00 77.35  ?  95  GLY A O    1 
ATOM   1350  H H    . GLY A 1 86  ? 45.367  -24.839 107.856 1.00 102.24 ?  95  GLY A H    1 
ATOM   1351  H HA2  . GLY A 1 86  ? 43.282  -25.244 107.685 1.00 79.01  ?  95  GLY A HA2  1 
ATOM   1352  H HA3  . GLY A 1 86  ? 43.565  -26.772 107.883 1.00 79.01  ?  95  GLY A HA3  1 
ATOM   1353  N N    . HIS A 1 87  ? 43.722  -24.997 110.509 1.00 67.12  ?  96  HIS A N    1 
ATOM   1354  C CA   . HIS A 1 87  ? 43.265  -24.944 111.884 1.00 91.00  ?  96  HIS A CA   1 
ATOM   1355  C C    . HIS A 1 87  ? 43.001  -23.511 112.332 1.00 88.15  ?  96  HIS A C    1 
ATOM   1356  O O    . HIS A 1 87  ? 42.730  -23.294 113.518 1.00 86.19  ?  96  HIS A O    1 
ATOM   1357  C CB   . HIS A 1 87  ? 44.312  -25.620 112.791 1.00 111.38 ?  96  HIS A CB   1 
ATOM   1358  C CG   . HIS A 1 87  ? 44.623  -27.050 112.408 1.00 104.88 ?  96  HIS A CG   1 
ATOM   1359  N ND1  . HIS A 1 87  ? 43.648  -27.962 112.053 1.00 117.70 ?  96  HIS A ND1  1 
ATOM   1360  C CD2  . HIS A 1 87  ? 45.805  -27.709 112.296 1.00 96.34  ?  96  HIS A CD2  1 
ATOM   1361  C CE1  . HIS A 1 87  ? 44.213  -29.114 111.746 1.00 115.89 ?  96  HIS A CE1  1 
ATOM   1362  N NE2  . HIS A 1 87  ? 45.520  -28.986 111.881 1.00 125.67 ?  96  HIS A NE2  1 
ATOM   1363  H H    . HIS A 1 87  ? 44.370  -24.462 110.330 1.00 80.54  ?  96  HIS A H    1 
ATOM   1364  H HA   . HIS A 1 87  ? 42.435  -25.440 111.961 1.00 109.20 ?  96  HIS A HA   1 
ATOM   1365  H HB2  . HIS A 1 87  ? 45.139  -25.115 112.745 1.00 133.65 ?  96  HIS A HB2  1 
ATOM   1366  H HB3  . HIS A 1 87  ? 43.980  -25.624 113.703 1.00 133.65 ?  96  HIS A HB3  1 
ATOM   1367  H HD2  . HIS A 1 87  ? 46.650  -27.358 112.463 1.00 115.61 ?  96  HIS A HD2  1 
ATOM   1368  H HE1  . HIS A 1 87  ? 43.766  -29.886 111.482 1.00 139.06 ?  96  HIS A HE1  1 
ATOM   1369  N N    . GLY A 1 88  ? 43.001  -22.546 111.404 1.00 127.27 ?  97  GLY A N    1 
ATOM   1370  C CA   . GLY A 1 88  ? 42.626  -21.174 111.698 1.00 87.36  ?  97  GLY A CA   1 
ATOM   1371  C C    . GLY A 1 88  ? 43.737  -20.126 111.650 1.00 110.76 ?  97  GLY A C    1 
ATOM   1372  O O    . GLY A 1 88  ? 43.458  -18.952 111.924 1.00 115.99 ?  97  GLY A O    1 
ATOM   1373  H H    . GLY A 1 88  ? 43.220  -22.672 110.582 1.00 152.72 ?  97  GLY A H    1 
ATOM   1374  H HA2  . GLY A 1 88  ? 41.940  -20.901 111.069 1.00 104.83 ?  97  GLY A HA2  1 
ATOM   1375  H HA3  . GLY A 1 88  ? 42.237  -21.146 112.587 1.00 104.83 ?  97  GLY A HA3  1 
ATOM   1376  N N    . ASP A 1 89  ? 44.987  -20.499 111.378 1.00 121.58 ?  98  ASP A N    1 
ATOM   1377  C CA   . ASP A 1 89  ? 46.069  -19.529 111.158 1.00 116.53 ?  98  ASP A CA   1 
ATOM   1378  C C    . ASP A 1 89  ? 46.084  -19.154 109.677 1.00 63.88  ?  98  ASP A C    1 
ATOM   1379  O O    . ASP A 1 89  ? 46.660  -19.847 108.844 1.00 71.14  ?  98  ASP A O    1 
ATOM   1380  C CB   . ASP A 1 89  ? 47.398  -20.103 111.629 1.00 136.89 ?  98  ASP A CB   1 
ATOM   1381  C CG   . ASP A 1 89  ? 48.590  -19.346 111.082 1.00 150.95 ?  98  ASP A CG   1 
ATOM   1382  O OD1  . ASP A 1 89  ? 48.432  -18.163 110.720 1.00 141.01 ?  98  ASP A OD1  1 
ATOM   1383  O OD2  . ASP A 1 89  ? 49.688  -19.941 111.015 1.00 166.19 -1 98  ASP A OD2  1 
ATOM   1384  H H    . ASP A 1 89  ? 45.241  -21.318 111.313 1.00 145.89 ?  98  ASP A H    1 
ATOM   1385  H HA   . ASP A 1 89  ? 45.887  -18.727 111.672 1.00 139.84 ?  98  ASP A HA   1 
ATOM   1386  H HB2  . ASP A 1 89  ? 47.435  -20.062 112.597 1.00 164.27 ?  98  ASP A HB2  1 
ATOM   1387  H HB3  . ASP A 1 89  ? 47.467  -21.024 111.333 1.00 164.27 ?  98  ASP A HB3  1 
ATOM   1388  N N    . VAL A 1 90  ? 45.426  -18.038 109.344 1.00 80.83  ?  99  VAL A N    1 
ATOM   1389  C CA   . VAL A 1 90  ? 45.023  -17.669 107.975 1.00 72.29  ?  99  VAL A CA   1 
ATOM   1390  C C    . VAL A 1 90  ? 45.826  -16.476 107.440 1.00 70.89  ?  99  VAL A C    1 
ATOM   1391  O O    . VAL A 1 90  ? 46.188  -15.572 108.201 1.00 101.78 ?  99  VAL A O    1 
ATOM   1392  C CB   . VAL A 1 90  ? 43.517  -17.369 107.947 1.00 67.83  ?  99  VAL A CB   1 
ATOM   1393  C CG1  . VAL A 1 90  ? 43.120  -16.709 106.655 1.00 91.57  ?  99  VAL A CG1  1 
ATOM   1394  C CG2  . VAL A 1 90  ? 42.743  -18.683 108.130 1.00 90.89  ?  99  VAL A CG2  1 
ATOM   1395  H H    . VAL A 1 90  ? 45.190  -17.448 109.924 1.00 97.00  ?  99  VAL A H    1 
ATOM   1396  H HA   . VAL A 1 90  ? 45.187  -18.423 107.388 1.00 86.75  ?  99  VAL A HA   1 
ATOM   1397  H HB   . VAL A 1 90  ? 43.291  -16.775 108.680 1.00 81.39  ?  99  VAL A HB   1 
ATOM   1398  H HG11 . VAL A 1 90  ? 42.166  -16.534 106.670 1.00 109.89 ?  99  VAL A HG11 1 
ATOM   1399  H HG12 . VAL A 1 90  ? 43.609  -15.875 106.565 1.00 109.89 ?  99  VAL A HG12 1 
ATOM   1400  H HG13 . VAL A 1 90  ? 43.337  -17.301 105.919 1.00 109.89 ?  99  VAL A HG13 1 
ATOM   1401  H HG21 . VAL A 1 90  ? 41.792  -18.493 108.113 1.00 109.07 ?  99  VAL A HG21 1 
ATOM   1402  H HG22 . VAL A 1 90  ? 42.974  -19.288 107.408 1.00 109.07 ?  99  VAL A HG22 1 
ATOM   1403  H HG23 . VAL A 1 90  ? 42.987  -19.076 108.983 1.00 109.07 ?  99  VAL A HG23 1 
ATOM   1404  N N    . ARG A 1 91  ? 46.126  -16.508 106.122 1.00 57.82  ?  100 ARG A N    1 
ATOM   1405  C CA   . ARG A 1 91  ? 46.692  -15.400 105.339 1.00 92.17  ?  100 ARG A CA   1 
ATOM   1406  C C    . ARG A 1 91  ? 45.583  -14.664 104.597 1.00 68.18  ?  100 ARG A C    1 
ATOM   1407  O O    . ARG A 1 91  ? 44.823  -15.288 103.856 1.00 66.47  ?  100 ARG A O    1 
ATOM   1408  C CB   . ARG A 1 91  ? 47.689  -15.868 104.259 1.00 81.33  ?  100 ARG A CB   1 
ATOM   1409  C CG   . ARG A 1 91  ? 48.994  -16.419 104.690 1.00 90.67  ?  100 ARG A CG   1 
ATOM   1410  C CD   . ARG A 1 91  ? 49.838  -15.384 105.360 1.00 83.44  ?  100 ARG A CD   1 
ATOM   1411  N NE   . ARG A 1 91  ? 50.066  -15.805 106.725 1.00 79.01  ?  100 ARG A NE   1 
ATOM   1412  C CZ   . ARG A 1 91  ? 51.247  -15.983 107.291 1.00 92.03  ?  100 ARG A CZ   1 
ATOM   1413  N NH1  . ARG A 1 91  ? 52.403  -15.755 106.645 1.00 115.05 1  100 ARG A NH1  1 
ATOM   1414  N NH2  . ARG A 1 91  ? 51.237  -16.382 108.548 1.00 111.51 1  100 ARG A NH2  1 
ATOM   1415  H H    . ARG A 1 91  ? 45.998  -17.209 105.640 1.00 69.38  ?  100 ARG A H    1 
ATOM   1416  H HA   . ARG A 1 91  ? 47.141  -14.776 105.930 1.00 110.61 ?  100 ARG A HA   1 
ATOM   1417  H HB2  . ARG A 1 91  ? 47.254  -16.558 103.734 1.00 97.59  ?  100 ARG A HB2  1 
ATOM   1418  H HB3  . ARG A 1 91  ? 47.881  -15.110 103.685 1.00 97.59  ?  100 ARG A HB3  1 
ATOM   1419  H HG2  . ARG A 1 91  ? 48.844  -17.141 105.319 1.00 108.80 ?  100 ARG A HG2  1 
ATOM   1420  H HG3  . ARG A 1 91  ? 49.475  -16.746 103.914 1.00 108.80 ?  100 ARG A HG3  1 
ATOM   1421  H HD2  . ARG A 1 91  ? 50.692  -15.310 104.907 1.00 100.13 ?  100 ARG A HD2  1 
ATOM   1422  H HD3  . ARG A 1 91  ? 49.373  -14.532 105.367 1.00 100.13 ?  100 ARG A HD3  1 
ATOM   1423  H HE   . ARG A 1 91  ? 49.372  -15.952 107.211 1.00 94.81  ?  100 ARG A HE   1 
ATOM   1424  H HH11 . ARG A 1 91  ? 52.393  -15.496 105.825 1.00 138.06 ?  100 ARG A HH11 1 
ATOM   1425  H HH12 . ARG A 1 91  ? 53.152  -15.877 107.049 1.00 138.06 ?  100 ARG A HH12 1 
ATOM   1426  H HH21 . ARG A 1 91  ? 50.489  -16.518 108.950 1.00 133.82 ?  100 ARG A HH21 1 
ATOM   1427  H HH22 . ARG A 1 91  ? 51.979  -16.504 108.966 1.00 133.82 ?  100 ARG A HH22 1 
ATOM   1428  N N    . LYS A 1 92  ? 45.550  -13.338 104.721 1.00 77.79  ?  101 LYS A N    1 
ATOM   1429  C CA   . LYS A 1 92  ? 44.554  -12.526 104.034 1.00 69.58  ?  101 LYS A CA   1 
ATOM   1430  C C    . LYS A 1 92  ? 45.108  -11.820 102.786 1.00 60.53  ?  101 LYS A C    1 
ATOM   1431  O O    . LYS A 1 92  ? 44.346  -11.104 102.127 1.00 76.94  ?  101 LYS A O    1 
ATOM   1432  C CB   . LYS A 1 92  ? 43.906  -11.492 105.012 1.00 74.19  ?  101 LYS A CB   1 
ATOM   1433  C CG   . LYS A 1 92  ? 43.267  -12.117 106.327 1.00 105.13 ?  101 LYS A CG   1 
ATOM   1434  C CD   . LYS A 1 92  ? 42.066  -11.337 106.918 1.00 79.88  ?  101 LYS A CD   1 
ATOM   1435  C CE   . LYS A 1 92  ? 41.472  -11.928 108.219 1.00 113.09 ?  101 LYS A CE   1 
ATOM   1436  H H    . LYS A 1 92  ? 46.100  -12.884 105.201 1.00 93.34  ?  101 LYS A H    1 
ATOM   1437  H HA   . LYS A 1 92  ? 43.844  -13.116 103.734 1.00 83.50  ?  101 LYS A HA   1 
ATOM   1438  H HB2  . LYS A 1 92  ? 44.588  -10.861 105.290 1.00 89.02  ?  101 LYS A HB2  1 
ATOM   1439  H HB3  . LYS A 1 92  ? 43.201  -11.022 104.540 1.00 89.02  ?  101 LYS A HB3  1 
ATOM   1440  H HG2  . LYS A 1 92  ? 42.960  -13.014 106.123 1.00 126.16 ?  101 LYS A HG2  1 
ATOM   1441  H HG3  . LYS A 1 92  ? 43.953  -12.157 107.012 1.00 126.16 ?  101 LYS A HG3  1 
ATOM   1442  H HD2  . LYS A 1 92  ? 42.353  -10.432 107.114 1.00 95.86  ?  101 LYS A HD2  1 
ATOM   1443  H HD3  . LYS A 1 92  ? 41.357  -11.317 106.257 1.00 95.86  ?  101 LYS A HD3  1 
ATOM   1444  H HE2  . LYS A 1 92  ? 41.240  -12.858 108.067 1.00 135.71 ?  101 LYS A HE2  1 
ATOM   1445  H HE3  . LYS A 1 92  ? 42.133  -11.862 108.926 1.00 135.71 ?  101 LYS A HE3  1 
ATOM   1446  N N    . VAL A 1 93  ? 46.392  -11.988 102.438 1.00 78.32  ?  102 VAL A N    1 
ATOM   1447  C CA   . VAL A 1 93  ? 47.006  -11.313 101.281 1.00 54.38  ?  102 VAL A CA   1 
ATOM   1448  C C    . VAL A 1 93  ? 47.793  -12.327 100.449 1.00 63.30  ?  102 VAL A C    1 
ATOM   1449  O O    . VAL A 1 93  ? 48.719  -12.963 100.956 1.00 71.73  ?  102 VAL A O    1 
ATOM   1450  C CB   . VAL A 1 93  ? 47.951  -10.147 101.704 1.00 60.14  ?  102 VAL A CB   1 
ATOM   1451  C CG1  . VAL A 1 93  ? 48.639  -9.439  100.445 1.00 60.26  ?  102 VAL A CG1  1 
ATOM   1452  C CG2  . VAL A 1 93  ? 47.224  -9.096  102.576 1.00 59.94  ?  102 VAL A CG2  1 
ATOM   1453  H H    . VAL A 1 93  ? 46.938  -12.497 102.864 1.00 93.98  ?  102 VAL A H    1 
ATOM   1454  H HA   . VAL A 1 93  ? 46.306  -10.944 100.721 1.00 65.25  ?  102 VAL A HA   1 
ATOM   1455  H HB   . VAL A 1 93  ? 48.664  -10.521 102.245 1.00 72.17  ?  102 VAL A HB   1 
ATOM   1456  H HG11 . VAL A 1 93  ? 49.213  -8.724  100.761 1.00 72.31  ?  102 VAL A HG11 1 
ATOM   1457  H HG12 . VAL A 1 93  ? 49.163  -10.096 99.961  1.00 72.31  ?  102 VAL A HG12 1 
ATOM   1458  H HG13 . VAL A 1 93  ? 47.946  -9.077  99.870  1.00 72.31  ?  102 VAL A HG13 1 
ATOM   1459  H HG21 . VAL A 1 93  ? 47.851  -8.394  102.812 1.00 71.93  ?  102 VAL A HG21 1 
ATOM   1460  H HG22 . VAL A 1 93  ? 46.486  -8.722  102.070 1.00 71.93  ?  102 VAL A HG22 1 
ATOM   1461  H HG23 . VAL A 1 93  ? 46.891  -9.527  103.378 1.00 71.93  ?  102 VAL A HG23 1 
ATOM   1462  N N    . LEU A 1 94  ? 47.500  -12.403 99.165  1.00 73.09  ?  103 LEU A N    1 
ATOM   1463  C CA   . LEU A 1 94  ? 48.221  -13.298 98.268  1.00 67.37  ?  103 LEU A CA   1 
ATOM   1464  C C    . LEU A 1 94  ? 49.376  -12.596 97.578  1.00 60.75  ?  103 LEU A C    1 
ATOM   1465  O O    . LEU A 1 94  ? 49.145  -11.592 96.893  1.00 80.57  ?  103 LEU A O    1 
ATOM   1466  C CB   . LEU A 1 94  ? 47.311  -13.815 97.217  1.00 57.93  ?  103 LEU A CB   1 
ATOM   1467  C CG   . LEU A 1 94  ? 47.840  -14.937 96.316  1.00 64.37  ?  103 LEU A CG   1 
ATOM   1468  C CD1  . LEU A 1 94  ? 48.077  -16.200 97.115  1.00 88.73  ?  103 LEU A CD1  1 
ATOM   1469  C CD2  . LEU A 1 94  ? 46.899  -15.221 95.148  1.00 56.72  ?  103 LEU A CD2  1 
ATOM   1470  H H    . LEU A 1 94  ? 46.882  -11.944 98.780  1.00 87.71  ?  103 LEU A H    1 
ATOM   1471  H HA   . LEU A 1 94  ? 48.572  -14.049 98.771  1.00 80.84  ?  103 LEU A HA   1 
ATOM   1472  H HB2  . LEU A 1 94  ? 46.512  -14.152 97.651  1.00 69.52  ?  103 LEU A HB2  1 
ATOM   1473  H HB3  . LEU A 1 94  ? 47.070  -13.075 96.638  1.00 69.52  ?  103 LEU A HB3  1 
ATOM   1474  H HG   . LEU A 1 94  ? 48.692  -14.660 95.945  1.00 77.24  ?  103 LEU A HG   1 
ATOM   1475  H HD11 . LEU A 1 94  ? 48.410  -16.891 96.520  1.00 106.48 ?  103 LEU A HD11 1 
ATOM   1476  H HD12 . LEU A 1 94  ? 48.730  -16.017 97.808  1.00 106.48 ?  103 LEU A HD12 1 
ATOM   1477  H HD13 . LEU A 1 94  ? 47.239  -16.483 97.514  1.00 106.48 ?  103 LEU A HD13 1 
ATOM   1478  H HD21 . LEU A 1 94  ? 47.274  -15.934 94.608  1.00 68.07  ?  103 LEU A HD21 1 
ATOM   1479  H HD22 . LEU A 1 94  ? 46.035  -15.488 95.496  1.00 68.07  ?  103 LEU A HD22 1 
ATOM   1480  H HD23 . LEU A 1 94  ? 46.807  -14.416 94.614  1.00 68.07  ?  103 LEU A HD23 1 
ATOM   1481  N N    . PRO A 1 95  ? 50.616  -13.100 97.682  1.00 54.90  ?  104 PRO A N    1 
ATOM   1482  C CA   . PRO A 1 95  ? 51.758  -12.353 97.133  1.00 82.97  ?  104 PRO A CA   1 
ATOM   1483  C C    . PRO A 1 95  ? 51.707  -12.142 95.633  1.00 59.10  ?  104 PRO A C    1 
ATOM   1484  O O    . PRO A 1 95  ? 51.292  -13.027 94.880  1.00 57.42  ?  104 PRO A O    1 
ATOM   1485  C CB   . PRO A 1 95  ? 52.959  -13.212 97.526  1.00 88.54  ?  104 PRO A CB   1 
ATOM   1486  C CG   . PRO A 1 95  ? 52.549  -13.873 98.697  1.00 87.10  ?  104 PRO A CG   1 
ATOM   1487  C CD   . PRO A 1 95  ? 51.078  -14.081 98.676  1.00 110.26 ?  104 PRO A CD   1 
ATOM   1488  H HA   . PRO A 1 95  ? 51.830  -11.491 97.570  1.00 99.56  ?  104 PRO A HA   1 
ATOM   1489  H HB2  . PRO A 1 95  ? 53.154  -13.849 96.820  1.00 106.25 ?  104 PRO A HB2  1 
ATOM   1490  H HB3  . PRO A 1 95  ? 53.726  -12.644 97.700  1.00 106.25 ?  104 PRO A HB3  1 
ATOM   1491  H HG2  . PRO A 1 95  ? 53.000  -14.730 98.746  1.00 104.52 ?  104 PRO A HG2  1 
ATOM   1492  H HG3  . PRO A 1 95  ? 52.792  -13.330 99.463  1.00 104.52 ?  104 PRO A HG3  1 
ATOM   1493  H HD2  . PRO A 1 95  ? 50.867  -14.982 98.387  1.00 132.31 ?  104 PRO A HD2  1 
ATOM   1494  H HD3  . PRO A 1 95  ? 50.696  -13.887 99.546  1.00 132.31 ?  104 PRO A HD3  1 
ATOM   1495  N N    . ARG A 1 96  ? 52.153  -10.955 95.222  1.00 56.17  ?  105 ARG A N    1 
ATOM   1496  C CA   . ARG A 1 96  ? 52.295  -10.638 93.809  1.00 85.63  ?  105 ARG A CA   1 
ATOM   1497  C C    . ARG A 1 96  ? 53.015  -11.755 93.066  1.00 72.19  ?  105 ARG A C    1 
ATOM   1498  O O    . ARG A 1 96  ? 52.576  -12.162 91.991  1.00 63.98  ?  105 ARG A O    1 
ATOM   1499  C CB   . ARG A 1 96  ? 53.047  -9.309  93.626  1.00 87.10  ?  105 ARG A CB   1 
ATOM   1500  C CG   . ARG A 1 96  ? 54.487  -9.341  94.020  1.00 99.94  ?  105 ARG A CG   1 
ATOM   1501  C CD   . ARG A 1 96  ? 55.142  -7.981  93.950  1.00 102.79 ?  105 ARG A CD   1 
ATOM   1502  N NE   . ARG A 1 96  ? 54.555  -7.052  94.898  1.00 94.31  ?  105 ARG A NE   1 
ATOM   1503  C CZ   . ARG A 1 96  ? 53.745  -6.055  94.558  1.00 67.30  ?  105 ARG A CZ   1 
ATOM   1504  N NH1  . ARG A 1 96  ? 53.414  -5.818  93.271  1.00 67.69  1  105 ARG A NH1  1 
ATOM   1505  N NH2  . ARG A 1 96  ? 53.257  -5.314  95.534  1.00 68.46  1  105 ARG A NH2  1 
ATOM   1506  H H    . ARG A 1 96  ? 52.380  -10.314 95.749  1.00 67.40  ?  105 ARG A H    1 
ATOM   1507  H HA   . ARG A 1 96  ? 51.413  -10.539 93.418  1.00 102.75 ?  105 ARG A HA   1 
ATOM   1508  H HB2  . ARG A 1 96  ? 53.005  -9.056  92.691  1.00 104.52 ?  105 ARG A HB2  1 
ATOM   1509  H HB3  . ARG A 1 96  ? 52.611  -8.631  94.166  1.00 104.52 ?  105 ARG A HB3  1 
ATOM   1510  H HG2  . ARG A 1 96  ? 54.559  -9.662  94.932  1.00 119.93 ?  105 ARG A HG2  1 
ATOM   1511  H HG3  . ARG A 1 96  ? 54.965  -9.935  93.421  1.00 119.93 ?  105 ARG A HG3  1 
ATOM   1512  H HD2  . ARG A 1 96  ? 56.085  -8.070  94.157  1.00 123.34 ?  105 ARG A HD2  1 
ATOM   1513  H HD3  . ARG A 1 96  ? 55.027  -7.617  93.058  1.00 123.34 ?  105 ARG A HD3  1 
ATOM   1514  H HE   . ARG A 1 96  ? 54.792  -7.115  95.722  1.00 113.17 ?  105 ARG A HE   1 
ATOM   1515  H HH11 . ARG A 1 96  ? 53.731  -6.317  92.647  1.00 81.23  ?  105 ARG A HH11 1 
ATOM   1516  H HH12 . ARG A 1 96  ? 52.890  -5.165  93.075  1.00 81.23  ?  105 ARG A HH12 1 
ATOM   1517  H HH21 . ARG A 1 96  ? 53.480  -5.475  96.349  1.00 82.15  ?  105 ARG A HH21 1 
ATOM   1518  H HH22 . ARG A 1 96  ? 52.739  -4.652  95.353  1.00 82.15  ?  105 ARG A HH22 1 
ATOM   1519  N N    . ASN A 1 97  ? 54.080  -12.309 93.663  1.00 67.47  ?  106 ASN A N    1 
ATOM   1520  C CA   . ASN A 1 97  ? 54.867  -13.370 93.021  1.00 66.71  ?  106 ASN A CA   1 
ATOM   1521  C C    . ASN A 1 97  ? 53.969  -14.407 92.388  1.00 74.44  ?  106 ASN A C    1 
ATOM   1522  O O    . ASN A 1 97  ? 54.246  -14.929 91.299  1.00 91.72  ?  106 ASN A O    1 
ATOM   1523  C CB   . ASN A 1 97  ? 55.771  -14.060 94.057  1.00 97.09  ?  106 ASN A CB   1 
ATOM   1524  H H    . ASN A 1 97  ? 54.367  -12.087 94.443  1.00 80.96  ?  106 ASN A H    1 
ATOM   1525  H HA   . ASN A 1 97  ? 55.429  -12.984 92.330  1.00 80.05  ?  106 ASN A HA   1 
ATOM   1526  N N    . ILE A 1 98  ? 52.849  -14.642 93.044  1.00 77.09  ?  107 ILE A N    1 
ATOM   1527  C CA   . ILE A 1 98  ? 51.878  -15.630 92.635  1.00 68.16  ?  107 ILE A CA   1 
ATOM   1528  C C    . ILE A 1 98  ? 50.535  -15.012 92.252  1.00 63.40  ?  107 ILE A C    1 
ATOM   1529  O O    . ILE A 1 98  ? 49.972  -15.386 91.227  1.00 51.02  ?  107 ILE A O    1 
ATOM   1530  C CB   . ILE A 1 98  ? 51.720  -16.660 93.749  1.00 61.84  ?  107 ILE A CB   1 
ATOM   1531  C CG1  . ILE A 1 98  ? 50.750  -17.709 93.328  1.00 58.18  ?  107 ILE A CG1  1 
ATOM   1532  C CG2  . ILE A 1 98  ? 51.253  -15.971 95.038  1.00 88.32  ?  107 ILE A CG2  1 
ATOM   1533  C CD1  . ILE A 1 98  ? 50.816  -18.885 94.179  1.00 161.37 ?  107 ILE A CD1  1 
ATOM   1534  H H    . ILE A 1 98  ? 52.622  -14.222 93.759  1.00 92.51  ?  107 ILE A H    1 
ATOM   1535  H HA   . ILE A 1 98  ? 52.219  -16.093 91.854  1.00 81.80  ?  107 ILE A HA   1 
ATOM   1536  H HB   . ILE A 1 98  ? 52.580  -17.078 93.913  1.00 74.21  ?  107 ILE A HB   1 
ATOM   1537  H HG12 . ILE A 1 98  ? 49.851  -17.349 93.379  1.00 69.82  ?  107 ILE A HG12 1 
ATOM   1538  H HG13 . ILE A 1 98  ? 50.951  -17.981 92.419  1.00 69.82  ?  107 ILE A HG13 1 
ATOM   1539  H HG21 . ILE A 1 98  ? 51.158  -16.638 95.735  1.00 105.98 ?  107 ILE A HG21 1 
ATOM   1540  H HG22 . ILE A 1 98  ? 51.914  -15.311 95.299  1.00 105.98 ?  107 ILE A HG22 1 
ATOM   1541  H HG23 . ILE A 1 98  ? 50.400  -15.539 94.873  1.00 105.98 ?  107 ILE A HG23 1 
ATOM   1542  H HD11 . ILE A 1 98  ? 50.169  -19.537 93.867  1.00 193.64 ?  107 ILE A HD11 1 
ATOM   1543  H HD12 . ILE A 1 98  ? 51.710  -19.258 94.133  1.00 193.64 ?  107 ILE A HD12 1 
ATOM   1544  H HD13 . ILE A 1 98  ? 50.612  -18.626 95.091  1.00 193.64 ?  107 ILE A HD13 1 
ATOM   1545  N N    . ALA A 1 99  ? 50.052  -13.986 92.979  1.00 72.81  ?  108 ALA A N    1 
ATOM   1546  C CA   . ALA A 1 99  ? 48.720  -13.440 92.663  1.00 64.31  ?  108 ALA A CA   1 
ATOM   1547  C C    . ALA A 1 99  ? 48.668  -12.905 91.243  1.00 73.41  ?  108 ALA A C    1 
ATOM   1548  O O    . ALA A 1 99  ? 47.679  -13.131 90.520  1.00 62.30  ?  108 ALA A O    1 
ATOM   1549  C CB   . ALA A 1 99  ? 48.287  -12.303 93.625  1.00 51.75  ?  108 ALA A CB   1 
ATOM   1550  H H    . ALA A 1 99  ? 50.458  -13.604 93.634  1.00 87.37  ?  108 ALA A H    1 
ATOM   1551  H HA   . ALA A 1 99  ? 48.066  -14.153 92.735  1.00 77.17  ?  108 ALA A HA   1 
ATOM   1552  H HB1  . ALA A 1 99  ? 47.407  -11.988 93.365  1.00 62.11  ?  108 ALA A HB1  1 
ATOM   1553  H HB2  . ALA A 1 99  ? 48.261  -12.649 94.531  1.00 62.11  ?  108 ALA A HB2  1 
ATOM   1554  H HB3  . ALA A 1 99  ? 48.929  -11.578 93.566  1.00 62.11  ?  108 ALA A HB3  1 
ATOM   1555  N N    . VAL A 1 100 ? 49.709  -12.179 90.838  1.00 59.70  ?  109 VAL A N    1 
ATOM   1556  C CA   . VAL A 1 100 ? 49.727  -11.550 89.528  1.00 77.80  ?  109 VAL A CA   1 
ATOM   1557  C C    . VAL A 1 100 ? 49.622  -12.611 88.445  1.00 75.00  ?  109 VAL A C    1 
ATOM   1558  O O    . VAL A 1 100 ? 48.608  -12.648 87.758  1.00 57.61  ?  109 VAL A O    1 
ATOM   1559  C CB   . VAL A 1 100 ? 50.963  -10.663 89.360  1.00 106.40 ?  109 VAL A CB   1 
ATOM   1560  C CG1  . VAL A 1 100 ? 51.111  -10.198 87.923  1.00 58.61  ?  109 VAL A CG1  1 
ATOM   1561  C CG2  . VAL A 1 100 ? 50.799  -9.442  90.266  1.00 58.10  ?  109 VAL A CG2  1 
ATOM   1562  H H    . VAL A 1 100 ? 50.416  -12.037 91.307  1.00 71.64  ?  109 VAL A H    1 
ATOM   1563  H HA   . VAL A 1 100 ? 48.947  -10.979 89.451  1.00 93.36  ?  109 VAL A HA   1 
ATOM   1564  H HB   . VAL A 1 100 ? 51.761  -11.148 89.622  1.00 127.68 ?  109 VAL A HB   1 
ATOM   1565  H HG11 . VAL A 1 100 ? 51.901  -9.640  87.852  1.00 70.33  ?  109 VAL A HG11 1 
ATOM   1566  H HG12 . VAL A 1 100 ? 51.201  -10.975 87.348  1.00 70.33  ?  109 VAL A HG12 1 
ATOM   1567  H HG13 . VAL A 1 100 ? 50.323  -9.691  87.673  1.00 70.33  ?  109 VAL A HG13 1 
ATOM   1568  H HG21 . VAL A 1 100 ? 51.577  -8.870  90.168  1.00 69.72  ?  109 VAL A HG21 1 
ATOM   1569  H HG22 . VAL A 1 100 ? 49.999  -8.960  90.004  1.00 69.72  ?  109 VAL A HG22 1 
ATOM   1570  H HG23 . VAL A 1 100 ? 50.720  -9.740  91.185  1.00 69.72  ?  109 VAL A HG23 1 
ATOM   1571  N N    . PRO A 1 101 ? 50.546  -13.549 88.315  1.00 60.19  ?  110 PRO A N    1 
ATOM   1572  C CA   . PRO A 1 101 ? 50.408  -14.507 87.208  1.00 97.30  ?  110 PRO A CA   1 
ATOM   1573  C C    . PRO A 1 101 ? 49.107  -15.263 87.297  1.00 104.33 ?  110 PRO A C    1 
ATOM   1574  O O    . PRO A 1 101 ? 48.434  -15.488 86.293  1.00 48.63  ?  110 PRO A O    1 
ATOM   1575  C CB   . PRO A 1 101 ? 51.630  -15.436 87.363  1.00 59.81  ?  110 PRO A CB   1 
ATOM   1576  C CG   . PRO A 1 101 ? 52.040  -15.332 88.853  1.00 52.14  ?  110 PRO A CG   1 
ATOM   1577  C CD   . PRO A 1 101 ? 51.615  -13.911 89.266  1.00 80.41  ?  110 PRO A CD   1 
ATOM   1578  H HA   . PRO A 1 101 ? 50.457  -14.049 86.355  1.00 116.76 ?  110 PRO A HA   1 
ATOM   1579  H HB2  . PRO A 1 101 ? 51.379  -16.346 87.140  1.00 71.77  ?  110 PRO A HB2  1 
ATOM   1580  H HB3  . PRO A 1 101 ? 52.348  -15.128 86.788  1.00 71.77  ?  110 PRO A HB3  1 
ATOM   1581  H HG2  . PRO A 1 101 ? 51.566  -15.999 89.372  1.00 62.57  ?  110 PRO A HG2  1 
ATOM   1582  H HG3  . PRO A 1 101 ? 53.000  -15.444 88.939  1.00 62.57  ?  110 PRO A HG3  1 
ATOM   1583  H HD2  . PRO A 1 101 ? 51.269  -13.916 90.172  1.00 96.49  ?  110 PRO A HD2  1 
ATOM   1584  H HD3  . PRO A 1 101 ? 52.362  -13.299 89.178  1.00 96.49  ?  110 PRO A HD3  1 
ATOM   1585  N N    . TYR A 1 102 ? 48.655  -15.562 88.492  1.00 69.08  ?  111 TYR A N    1 
ATOM   1586  C CA   . TYR A 1 102 ? 47.397  -16.266 88.604  1.00 80.31  ?  111 TYR A CA   1 
ATOM   1587  C C    . TYR A 1 102 ? 46.234  -15.433 88.080  1.00 80.13  ?  111 TYR A C    1 
ATOM   1588  O O    . TYR A 1 102 ? 45.412  -15.933 87.295  1.00 59.77  ?  111 TYR A O    1 
ATOM   1589  C CB   . TYR A 1 102 ? 47.186  -16.650 90.054  1.00 55.02  ?  111 TYR A CB   1 
ATOM   1590  C CG   . TYR A 1 102 ? 45.992  -17.540 90.379  1.00 68.05  ?  111 TYR A CG   1 
ATOM   1591  C CD1  . TYR A 1 102 ? 45.594  -18.542 89.504  1.00 113.93 ?  111 TYR A CD1  1 
ATOM   1592  C CD2  . TYR A 1 102 ? 45.340  -17.462 91.614  1.00 78.35  ?  111 TYR A CD2  1 
ATOM   1593  C CE1  . TYR A 1 102 ? 44.572  -19.417 89.811  1.00 68.68  ?  111 TYR A CE1  1 
ATOM   1594  C CE2  . TYR A 1 102 ? 44.329  -18.326 91.942  1.00 68.73  ?  111 TYR A CE2  1 
ATOM   1595  C CZ   . TYR A 1 102 ? 43.941  -19.324 91.020  1.00 74.73  ?  111 TYR A CZ   1 
ATOM   1596  O OH   . TYR A 1 102 ? 42.934  -20.252 91.245  1.00 75.58  ?  111 TYR A OH   1 
ATOM   1597  H H    . TYR A 1 102 ? 49.042  -15.376 89.237  1.00 82.89  ?  111 TYR A H    1 
ATOM   1598  H HA   . TYR A 1 102 ? 47.442  -17.082 88.080  1.00 96.37  ?  111 TYR A HA   1 
ATOM   1599  H HB2  . TYR A 1 102 ? 47.980  -17.117 90.360  1.00 66.02  ?  111 TYR A HB2  1 
ATOM   1600  H HB3  . TYR A 1 102 ? 47.080  -15.834 90.568  1.00 66.02  ?  111 TYR A HB3  1 
ATOM   1601  H HD1  . TYR A 1 102 ? 46.031  -18.628 88.688  1.00 136.71 ?  111 TYR A HD1  1 
ATOM   1602  H HD2  . TYR A 1 102 ? 45.607  -16.819 92.230  1.00 94.02  ?  111 TYR A HD2  1 
ATOM   1603  H HE1  . TYR A 1 102 ? 44.322  -20.075 89.203  1.00 82.41  ?  111 TYR A HE1  1 
ATOM   1604  H HE2  . TYR A 1 102 ? 43.898  -18.254 92.763  1.00 82.48  ?  111 TYR A HE2  1 
ATOM   1605  H HH   . TYR A 1 102 ? 42.596  -20.131 92.004  1.00 90.70  ?  111 TYR A HH   1 
ATOM   1606  N N    . CYS A 1 103 ? 46.161  -14.152 88.465  1.00 73.38  ?  112 CYS A N    1 
ATOM   1607  C CA   . CYS A 1 103 ? 45.009  -13.376 88.031  1.00 65.97  ?  112 CYS A CA   1 
ATOM   1608  C C    . CYS A 1 103 ? 45.040  -13.164 86.527  1.00 74.33  ?  112 CYS A C    1 
ATOM   1609  O O    . CYS A 1 103 ? 43.992  -13.116 85.885  1.00 160.30 ?  112 CYS A O    1 
ATOM   1610  C CB   . CYS A 1 103 ? 44.935  -12.073 88.815  1.00 53.43  ?  112 CYS A CB   1 
ATOM   1611  S SG   . CYS A 1 103 ? 44.386  -12.376 90.482  1.00 72.16  ?  112 CYS A SG   1 
ATOM   1612  H H    . CYS A 1 103 ? 46.735  -13.733 88.950  1.00 88.06  ?  112 CYS A H    1 
ATOM   1613  H HA   . CYS A 1 103 ? 44.206  -13.881 88.235  1.00 79.17  ?  112 CYS A HA   1 
ATOM   1614  H HB2  . CYS A 1 103 ? 45.816  -11.667 88.851  1.00 64.12  ?  112 CYS A HB2  1 
ATOM   1615  H HB3  . CYS A 1 103 ? 44.303  -11.474 88.388  1.00 64.12  ?  112 CYS A HB3  1 
ATOM   1616  H HG   . CYS A 1 103 ? 43.297  -12.878 90.449  1.00 86.59  ?  112 CYS A HG   1 
ATOM   1617  N N    . GLN A 1 104 ? 46.235  -13.125 85.956  1.00 80.47  ?  113 GLN A N    1 
ATOM   1618  C CA   . GLN A 1 104 ? 46.383  -13.013 84.514  1.00 76.13  ?  113 GLN A CA   1 
ATOM   1619  C C    . GLN A 1 104 ? 45.941  -14.301 83.852  1.00 91.36  ?  113 GLN A C    1 
ATOM   1620  O O    . GLN A 1 104 ? 45.174  -14.304 82.887  1.00 67.37  ?  113 GLN A O    1 
ATOM   1621  C CB   . GLN A 1 104 ? 47.850  -12.745 84.153  1.00 90.58  ?  113 GLN A CB   1 
ATOM   1622  C CG   . GLN A 1 104 ? 48.401  -11.363 84.412  1.00 113.70 ?  113 GLN A CG   1 
ATOM   1623  C CD   . GLN A 1 104 ? 49.871  -11.327 84.088  1.00 135.89 ?  113 GLN A CD   1 
ATOM   1624  O OE1  . GLN A 1 104 ? 50.699  -11.450 84.973  1.00 116.60 ?  113 GLN A OE1  1 
ATOM   1625  N NE2  . GLN A 1 104 ? 50.203  -11.207 82.804  1.00 157.21 ?  113 GLN A NE2  1 
ATOM   1626  H H    . GLN A 1 104 ? 46.980  -13.161 86.384  1.00 96.57  ?  113 GLN A H    1 
ATOM   1627  H HA   . GLN A 1 104 ? 45.838  -12.284 84.181  1.00 91.36  ?  113 GLN A HA   1 
ATOM   1628  H HB2  . GLN A 1 104 ? 48.399  -13.367 84.655  1.00 108.70 ?  113 GLN A HB2  1 
ATOM   1629  H HB3  . GLN A 1 104 ? 47.960  -12.919 83.205  1.00 108.70 ?  113 GLN A HB3  1 
ATOM   1630  H HG2  . GLN A 1 104 ? 47.944  -10.720 83.847  1.00 136.45 ?  113 GLN A HG2  1 
ATOM   1631  H HG3  . GLN A 1 104 ? 48.285  -11.137 85.348  1.00 136.45 ?  113 GLN A HG3  1 
ATOM   1632  H HE21 . GLN A 1 104 ? 49.588  -11.154 82.204  1.00 188.65 ?  113 GLN A HE21 1 
ATOM   1633  H HE22 . GLN A 1 104 ? 51.031  -11.182 82.574  1.00 188.65 ?  113 GLN A HE22 1 
ATOM   1634  N N    . LEU A 1 105 ? 46.389  -15.425 84.388  1.00 88.13  ?  114 LEU A N    1 
ATOM   1635  C CA   . LEU A 1 105 ? 46.095  -16.660 83.699  1.00 75.38  ?  114 LEU A CA   1 
ATOM   1636  C C    . LEU A 1 105 ? 44.608  -16.896 83.755  1.00 62.04  ?  114 LEU A C    1 
ATOM   1637  O O    . LEU A 1 105 ? 44.049  -17.437 82.807  1.00 69.36  ?  114 LEU A O    1 
ATOM   1638  C CB   . LEU A 1 105 ? 46.886  -17.835 84.282  1.00 63.87  ?  114 LEU A CB   1 
ATOM   1639  C CG   . LEU A 1 105 ? 46.552  -19.196 83.628  1.00 111.05 ?  114 LEU A CG   1 
ATOM   1640  C CD1  . LEU A 1 105 ? 46.862  -19.226 82.125  1.00 128.22 ?  114 LEU A CD1  1 
ATOM   1641  C CD2  . LEU A 1 105 ? 47.199  -20.359 84.343  1.00 120.54 ?  114 LEU A CD2  1 
ATOM   1642  H H    . LEU A 1 105 ? 46.844  -15.497 85.114  1.00 105.76 ?  114 LEU A H    1 
ATOM   1643  H HA   . LEU A 1 105 ? 46.347  -16.566 82.767  1.00 90.45  ?  114 LEU A HA   1 
ATOM   1644  H HB2  . LEU A 1 105 ? 47.833  -17.669 84.154  1.00 76.65  ?  114 LEU A HB2  1 
ATOM   1645  H HB3  . LEU A 1 105 ? 46.690  -17.906 85.230  1.00 76.65  ?  114 LEU A HB3  1 
ATOM   1646  H HG   . LEU A 1 105 ? 45.595  -19.326 83.710  1.00 133.26 ?  114 LEU A HG   1 
ATOM   1647  H HD11 . LEU A 1 105 ? 46.633  -20.100 81.773  1.00 153.87 ?  114 LEU A HD11 1 
ATOM   1648  H HD12 . LEU A 1 105 ? 46.337  -18.542 81.681  1.00 153.87 ?  114 LEU A HD12 1 
ATOM   1649  H HD13 . LEU A 1 105 ? 47.808  -19.054 81.995  1.00 153.87 ?  114 LEU A HD13 1 
ATOM   1650  H HD21 . LEU A 1 105 ? 46.956  -21.182 83.891  1.00 144.64 ?  114 LEU A HD21 1 
ATOM   1651  H HD22 . LEU A 1 105 ? 48.162  -20.244 84.326  1.00 144.64 ?  114 LEU A HD22 1 
ATOM   1652  H HD23 . LEU A 1 105 ? 46.885  -20.380 85.261  1.00 144.64 ?  114 LEU A HD23 1 
ATOM   1653  N N    . SER A 1 106 ? 43.953  -16.401 84.804  1.00 107.24 ?  115 SER A N    1 
ATOM   1654  C CA   . SER A 1 106 ? 42.516  -16.580 84.940  1.00 62.96  ?  115 SER A CA   1 
ATOM   1655  C C    . SER A 1 106 ? 41.736  -15.743 83.927  1.00 73.88  ?  115 SER A C    1 
ATOM   1656  O O    . SER A 1 106 ? 40.933  -16.276 83.160  1.00 85.96  ?  115 SER A O    1 
ATOM   1657  C CB   . SER A 1 106 ? 42.134  -16.183 86.332  1.00 52.87  ?  115 SER A CB   1 
ATOM   1658  O OG   . SER A 1 106 ? 42.861  -16.891 87.318  1.00 56.76  ?  115 SER A OG   1 
ATOM   1659  H H    . SER A 1 106 ? 44.318  -15.961 85.446  1.00 128.69 ?  115 SER A H    1 
ATOM   1660  H HA   . SER A 1 106 ? 42.290  -17.515 84.810  1.00 75.55  ?  115 SER A HA   1 
ATOM   1661  H HB2  . SER A 1 106 ? 42.305  -15.234 86.442  1.00 63.44  ?  115 SER A HB2  1 
ATOM   1662  H HB3  . SER A 1 106 ? 41.188  -16.360 86.457  1.00 63.44  ?  115 SER A HB3  1 
ATOM   1663  H HG   . SER A 1 106 ? 43.684  -16.745 87.229  1.00 68.12  ?  115 SER A HG   1 
ATOM   1664  N N    . LYS A 1 107 ? 42.009  -14.435 83.871  1.00 77.62  ?  116 LYS A N    1 
ATOM   1665  C CA   . LYS A 1 107 ? 41.322  -13.554 82.936  1.00 72.66  ?  116 LYS A CA   1 
ATOM   1666  C C    . LYS A 1 107 ? 41.412  -14.112 81.531  1.00 64.16  ?  116 LYS A C    1 
ATOM   1667  O O    . LYS A 1 107 ? 40.460  -13.998 80.737  1.00 63.58  ?  116 LYS A O    1 
ATOM   1668  C CB   . LYS A 1 107 ? 41.932  -12.152 83.018  1.00 92.01  ?  116 LYS A CB   1 
ATOM   1669  C CG   . LYS A 1 107 ? 41.397  -11.068 82.107  1.00 116.97 ?  116 LYS A CG   1 
ATOM   1670  C CD   . LYS A 1 107 ? 42.198  -9.767  82.328  1.00 109.71 ?  116 LYS A CD   1 
ATOM   1671  C CE   . LYS A 1 107 ? 41.703  -8.558  81.492  1.00 106.89 ?  116 LYS A CE   1 
ATOM   1672  H H    . LYS A 1 107 ? 42.590  -14.038 84.366  1.00 93.14  ?  116 LYS A H    1 
ATOM   1673  H HA   . LYS A 1 107 ? 40.386  -13.494 83.181  1.00 87.19  ?  116 LYS A HA   1 
ATOM   1674  H HB2  . LYS A 1 107 ? 41.818  -11.833 83.927  1.00 110.42 ?  116 LYS A HB2  1 
ATOM   1675  H HB3  . LYS A 1 107 ? 42.880  -12.231 82.830  1.00 110.42 ?  116 LYS A HB3  1 
ATOM   1676  H HG2  . LYS A 1 107 ? 41.497  -11.341 81.181  1.00 140.36 ?  116 LYS A HG2  1 
ATOM   1677  H HG3  . LYS A 1 107 ? 40.465  -10.898 82.315  1.00 140.36 ?  116 LYS A HG3  1 
ATOM   1678  H HD2  . LYS A 1 107 ? 42.138  -9.522  83.264  1.00 131.65 ?  116 LYS A HD2  1 
ATOM   1679  H HD3  . LYS A 1 107 ? 43.124  -9.930  82.091  1.00 131.65 ?  116 LYS A HD3  1 
ATOM   1680  H HE2  . LYS A 1 107 ? 41.789  -8.769  80.549  1.00 128.26 ?  116 LYS A HE2  1 
ATOM   1681  H HE3  . LYS A 1 107 ? 40.774  -8.383  81.709  1.00 128.26 ?  116 LYS A HE3  1 
ATOM   1682  N N    . LYS A 1 108 ? 42.572  -14.696 81.193  1.00 85.30  ?  117 LYS A N    1 
ATOM   1683  C CA   . LYS A 1 108 ? 42.741  -15.331 79.891  1.00 96.14  ?  117 LYS A CA   1 
ATOM   1684  C C    . LYS A 1 108 ? 41.751  -16.490 79.729  1.00 92.57  ?  117 LYS A C    1 
ATOM   1685  O O    . LYS A 1 108 ? 41.163  -16.692 78.656  1.00 84.78  ?  117 LYS A O    1 
ATOM   1686  C CB   . LYS A 1 108 ? 44.187  -15.807 79.732  1.00 84.31  ?  117 LYS A CB   1 
ATOM   1687  C CG   . LYS A 1 108 ? 44.516  -16.264 78.323  1.00 90.46  ?  117 LYS A CG   1 
ATOM   1688  C CD   . LYS A 1 108 ? 45.976  -16.602 78.105  1.00 94.84  ?  117 LYS A CD   1 
ATOM   1689  C CE   . LYS A 1 108 ? 46.246  -16.799 76.614  1.00 96.48  ?  117 LYS A CE   1 
ATOM   1690  N NZ   . LYS A 1 108 ? 46.098  -15.525 75.825  1.00 93.10  1  117 LYS A NZ   1 
ATOM   1691  H H    . LYS A 1 108 ? 43.266  -14.735 81.700  1.00 102.36 ?  117 LYS A H    1 
ATOM   1692  H HA   . LYS A 1 108 ? 42.560  -14.680 79.195  1.00 115.37 ?  117 LYS A HA   1 
ATOM   1693  H HB2  . LYS A 1 108 ? 44.785  -15.077 79.955  1.00 101.17 ?  117 LYS A HB2  1 
ATOM   1694  H HB3  . LYS A 1 108 ? 44.340  -16.554 80.331  1.00 101.17 ?  117 LYS A HB3  1 
ATOM   1695  H HG2  . LYS A 1 108 ? 43.996  -17.058 78.125  1.00 108.55 ?  117 LYS A HG2  1 
ATOM   1696  H HG3  . LYS A 1 108 ? 44.281  -15.556 77.704  1.00 108.55 ?  117 LYS A HG3  1 
ATOM   1697  H HD2  . LYS A 1 108 ? 46.530  -15.874 78.427  1.00 113.81 ?  117 LYS A HD2  1 
ATOM   1698  H HD3  . LYS A 1 108 ? 46.192  -17.426 78.569  1.00 113.81 ?  117 LYS A HD3  1 
ATOM   1699  H HE2  . LYS A 1 108 ? 47.153  -17.120 76.497  1.00 115.78 ?  117 LYS A HE2  1 
ATOM   1700  H HE3  . LYS A 1 108 ? 45.616  -17.446 76.261  1.00 115.78 ?  117 LYS A HE3  1 
ATOM   1701  H HZ1  . LYS A 1 108 ? 46.263  -15.680 74.965  1.00 111.73 ?  117 LYS A HZ1  1 
ATOM   1702  H HZ2  . LYS A 1 108 ? 45.270  -15.211 75.909  1.00 111.73 ?  117 LYS A HZ2  1 
ATOM   1703  H HZ3  . LYS A 1 108 ? 46.671  -14.914 76.124  1.00 111.73 ?  117 LYS A HZ3  1 
ATOM   1704  N N    . LEU A 1 109 ? 41.520  -17.230 80.792  1.00 82.20  ?  118 LEU A N    1 
ATOM   1705  C CA   . LEU A 1 109 ? 40.636  -18.379 80.720  1.00 81.32  ?  118 LEU A CA   1 
ATOM   1706  C C    . LEU A 1 109 ? 39.186  -18.052 81.103  1.00 89.20  ?  118 LEU A C    1 
ATOM   1707  O O    . LEU A 1 109 ? 38.312  -18.910 80.951  1.00 120.84 ?  118 LEU A O    1 
ATOM   1708  C CB   . LEU A 1 109 ? 41.189  -19.495 81.618  1.00 43.83  ?  118 LEU A CB   1 
ATOM   1709  C CG   . LEU A 1 109 ? 42.505  -20.178 81.140  1.00 59.90  ?  118 LEU A CG   1 
ATOM   1710  C CD1  . LEU A 1 109 ? 43.293  -20.923 82.285  1.00 66.03  ?  118 LEU A CD1  1 
ATOM   1711  C CD2  . LEU A 1 109 ? 42.300  -21.147 79.950  1.00 70.36  ?  118 LEU A CD2  1 
ATOM   1712  H H    . LEU A 1 109 ? 41.861  -17.092 81.570  1.00 98.63  ?  118 LEU A H    1 
ATOM   1713  H HA   . LEU A 1 109 ? 40.632  -18.709 79.808  1.00 97.58  ?  118 LEU A HA   1 
ATOM   1714  H HB2  . LEU A 1 109 ? 41.361  -19.122 82.497  1.00 52.59  ?  118 LEU A HB2  1 
ATOM   1715  H HB3  . LEU A 1 109 ? 40.514  -20.189 81.691  1.00 52.59  ?  118 LEU A HB3  1 
ATOM   1716  H HG   . LEU A 1 109 ? 43.092  -19.476 80.820  1.00 71.89  ?  118 LEU A HG   1 
ATOM   1717  H HD11 . LEU A 1 109 ? 44.095  -21.319 81.909  1.00 79.24  ?  118 LEU A HD11 1 
ATOM   1718  H HD12 . LEU A 1 109 ? 43.532  -20.282 82.973  1.00 79.24  ?  118 LEU A HD12 1 
ATOM   1719  H HD13 . LEU A 1 109 ? 42.726  -21.615 82.659  1.00 79.24  ?  118 LEU A HD13 1 
ATOM   1720  H HD21 . LEU A 1 109 ? 43.155  -21.534 79.707  1.00 84.44  ?  118 LEU A HD21 1 
ATOM   1721  H HD22 . LEU A 1 109 ? 41.684  -21.848 80.217  1.00 84.44  ?  118 LEU A HD22 1 
ATOM   1722  H HD23 . LEU A 1 109 ? 41.934  -20.653 79.200  1.00 84.44  ?  118 LEU A HD23 1 
ATOM   1723  N N    . GLU A 1 110 ? 38.898  -16.811 81.499  1.00 91.32  ?  119 GLU A N    1 
ATOM   1724  C CA   . GLU A 1 110 ? 37.566  -16.367 81.918  1.00 91.50  ?  119 GLU A CA   1 
ATOM   1725  C C    . GLU A 1 110 ? 37.113  -17.027 83.208  1.00 76.06  ?  119 GLU A C    1 
ATOM   1726  O O    . GLU A 1 110 ? 35.915  -17.152 83.489  1.00 65.55  ?  119 GLU A O    1 
ATOM   1727  C CB   . GLU A 1 110 ? 36.529  -16.587 80.832  1.00 105.29 ?  119 GLU A CB   1 
ATOM   1728  C CG   . GLU A 1 110 ? 36.848  -15.839 79.648  1.00 101.76 ?  119 GLU A CG   1 
ATOM   1729  C CD   . GLU A 1 110 ? 35.671  -15.670 78.795  1.00 101.15 ?  119 GLU A CD   1 
ATOM   1730  O OE1  . GLU A 1 110 ? 34.643  -15.197 79.320  1.00 111.36 ?  119 GLU A OE1  1 
ATOM   1731  O OE2  . GLU A 1 110 ? 35.791  -15.990 77.600  1.00 106.00 -1 119 GLU A OE2  1 
ATOM   1732  H H    . GLU A 1 110 ? 39.484  -16.183 81.536  1.00 109.58 ?  119 GLU A H    1 
ATOM   1733  H HA   . GLU A 1 110 ? 37.606  -15.412 82.085  1.00 109.80 ?  119 GLU A HA   1 
ATOM   1734  H HB2  . GLU A 1 110 ? 36.502  -17.528 80.600  1.00 126.35 ?  119 GLU A HB2  1 
ATOM   1735  H HB3  . GLU A 1 110 ? 35.662  -16.294 81.153  1.00 126.35 ?  119 GLU A HB3  1 
ATOM   1736  H HG2  . GLU A 1 110 ? 37.171  -14.960 79.901  1.00 122.11 ?  119 GLU A HG2  1 
ATOM   1737  H HG3  . GLU A 1 110 ? 37.526  -16.314 79.142  1.00 122.11 ?  119 GLU A HG3  1 
ATOM   1738  N N    . LEU A 1 111 ? 38.040  -17.355 84.035  1.00 73.70  ?  120 LEU A N    1 
ATOM   1739  C CA   . LEU A 1 111 ? 37.690  -17.914 85.317  1.00 80.10  ?  120 LEU A CA   1 
ATOM   1740  C C    . LEU A 1 111 ? 38.123  -17.004 86.445  1.00 87.91  ?  120 LEU A C    1 
ATOM   1741  O O    . LEU A 1 111 ? 38.973  -16.125 86.262  1.00 112.37 ?  120 LEU A O    1 
ATOM   1742  C CB   . LEU A 1 111 ? 38.373  -19.266 85.505  1.00 74.38  ?  120 LEU A CB   1 
ATOM   1743  C CG   . LEU A 1 111 ? 37.809  -20.380 84.638  1.00 91.19  ?  120 LEU A CG   1 
ATOM   1744  C CD1  . LEU A 1 111 ? 38.868  -21.460 84.507  1.00 117.60 ?  120 LEU A CD1  1 
ATOM   1745  C CD2  . LEU A 1 111 ? 36.557  -20.892 85.237  1.00 120.69 ?  120 LEU A CD2  1 
ATOM   1746  H H    . LEU A 1 111 ? 38.885  -17.270 83.894  1.00 88.44  ?  120 LEU A H    1 
ATOM   1747  H HA   . LEU A 1 111 ? 36.729  -18.040 85.368  1.00 96.12  ?  120 LEU A HA   1 
ATOM   1748  H HB2  . LEU A 1 111 ? 39.314  -19.171 85.289  1.00 89.26  ?  120 LEU A HB2  1 
ATOM   1749  H HB3  . LEU A 1 111 ? 38.277  -19.536 86.432  1.00 89.26  ?  120 LEU A HB3  1 
ATOM   1750  H HG   . LEU A 1 111 ? 37.609  -20.034 83.754  1.00 109.42 ?  120 LEU A HG   1 
ATOM   1751  H HD11 . LEU A 1 111 ? 38.520  -22.178 83.955  1.00 141.12 ?  120 LEU A HD11 1 
ATOM   1752  H HD12 . LEU A 1 111 ? 39.658  -21.078 84.094  1.00 141.12 ?  120 LEU A HD12 1 
ATOM   1753  H HD13 . LEU A 1 111 ? 39.085  -21.796 85.390  1.00 141.12 ?  120 LEU A HD13 1 
ATOM   1754  H HD21 . LEU A 1 111 ? 36.207  -21.601 84.676  1.00 144.83 ?  120 LEU A HD21 1 
ATOM   1755  H HD22 . LEU A 1 111 ? 36.749  -21.235 86.124  1.00 144.83 ?  120 LEU A HD22 1 
ATOM   1756  H HD23 . LEU A 1 111 ? 35.916  -20.167 85.294  1.00 144.83 ?  120 LEU A HD23 1 
ATOM   1757  N N    . PRO A 1 112 ? 37.563  -17.191 87.632  1.00 64.15  ?  121 PRO A N    1 
ATOM   1758  C CA   . PRO A 1 112 ? 38.014  -16.438 88.793  1.00 81.54  ?  121 PRO A CA   1 
ATOM   1759  C C    . PRO A 1 112 ? 39.264  -17.036 89.431  1.00 88.41  ?  121 PRO A C    1 
ATOM   1760  O O    . PRO A 1 112 ? 39.589  -18.216 89.236  1.00 79.88  ?  121 PRO A O    1 
ATOM   1761  C CB   . PRO A 1 112 ? 36.780  -16.479 89.721  1.00 89.10  ?  121 PRO A CB   1 
ATOM   1762  C CG   . PRO A 1 112 ? 36.034  -17.607 89.327  1.00 65.58  ?  121 PRO A CG   1 
ATOM   1763  C CD   . PRO A 1 112 ? 36.292  -17.858 87.893  1.00 49.13  ?  121 PRO A CD   1 
ATOM   1764  H HA   . PRO A 1 112 ? 38.193  -15.518 88.544  1.00 97.85  ?  121 PRO A HA   1 
ATOM   1765  H HB2  . PRO A 1 112 ? 37.070  -16.567 90.642  1.00 106.92 ?  121 PRO A HB2  1 
ATOM   1766  H HB3  . PRO A 1 112 ? 36.259  -15.669 89.604  1.00 106.92 ?  121 PRO A HB3  1 
ATOM   1767  H HG2  . PRO A 1 112 ? 36.313  -18.372 89.855  1.00 78.70  ?  121 PRO A HG2  1 
ATOM   1768  H HG3  . PRO A 1 112 ? 35.091  -17.430 89.470  1.00 78.70  ?  121 PRO A HG3  1 
ATOM   1769  H HD2  . PRO A 1 112 ? 36.373  -18.811 87.728  1.00 58.96  ?  121 PRO A HD2  1 
ATOM   1770  H HD3  . PRO A 1 112 ? 35.589  -17.465 87.352  1.00 58.96  ?  121 PRO A HD3  1 
ATOM   1771  N N    . PRO A 1 113 ? 40.006  -16.264 90.127  1.00 74.49  ?  122 PRO A N    1 
ATOM   1772  C CA   . PRO A 1 113 ? 41.226  -16.713 90.832  1.00 65.35  ?  122 PRO A CA   1 
ATOM   1773  C C    . PRO A 1 113 ? 40.925  -17.458 92.118  1.00 58.77  ?  122 PRO A C    1 
ATOM   1774  O O    . PRO A 1 113 ? 41.180  -17.040 93.271  1.00 56.75  ?  122 PRO A O    1 
ATOM   1775  C CB   . PRO A 1 113 ? 41.943  -15.401 91.103  1.00 80.53  ?  122 PRO A CB   1 
ATOM   1776  C CG   . PRO A 1 113 ? 40.793  -14.468 91.372  1.00 69.94  ?  122 PRO A CG   1 
ATOM   1777  C CD   . PRO A 1 113 ? 39.724  -14.858 90.410  1.00 54.52  ?  122 PRO A CD   1 
ATOM   1778  H HA   . PRO A 1 113 ? 41.771  -17.268 90.253  1.00 78.42  ?  122 PRO A HA   1 
ATOM   1779  H HB2  . PRO A 1 113 ? 42.517  -15.486 91.880  1.00 96.64  ?  122 PRO A HB2  1 
ATOM   1780  H HB3  . PRO A 1 113 ? 42.445  -15.125 90.320  1.00 96.64  ?  122 PRO A HB3  1 
ATOM   1781  H HG2  . PRO A 1 113 ? 40.488  -14.582 92.286  1.00 83.92  ?  122 PRO A HG2  1 
ATOM   1782  H HG3  . PRO A 1 113 ? 41.074  -13.552 91.217  1.00 83.92  ?  122 PRO A HG3  1 
ATOM   1783  H HD2  . PRO A 1 113 ? 38.851  -14.765 90.821  1.00 65.42  ?  122 PRO A HD2  1 
ATOM   1784  H HD3  . PRO A 1 113 ? 39.792  -14.331 89.598  1.00 65.42  ?  122 PRO A HD3  1 
ATOM   1785  N N    . ILE A 1 114 ? 40.291  -18.589 91.936  1.00 54.23  ?  123 ILE A N    1 
ATOM   1786  C CA   . ILE A 1 114 ? 40.115  -19.490 93.039  1.00 55.84  ?  123 ILE A CA   1 
ATOM   1787  C C    . ILE A 1 114 ? 39.935  -20.830 92.411  1.00 70.36  ?  123 ILE A C    1 
ATOM   1788  O O    . ILE A 1 114 ? 39.538  -20.955 91.245  1.00 77.21  ?  123 ILE A O    1 
ATOM   1789  C CB   . ILE A 1 114 ? 38.940  -19.112 93.957  1.00 41.94  ?  123 ILE A CB   1 
ATOM   1790  C CG1  . ILE A 1 114 ? 38.977  -19.969 95.195  1.00 41.42  ?  123 ILE A CG1  1 
ATOM   1791  C CG2  . ILE A 1 114 ? 37.624  -19.304 93.217  1.00 46.26  ?  123 ILE A CG2  1 
ATOM   1792  C CD1  . ILE A 1 114 ? 38.235  -19.392 96.392  1.00 42.71  ?  123 ILE A CD1  1 
ATOM   1793  H H    . ILE A 1 114 ? 39.955  -18.856 91.190  1.00 65.08  ?  123 ILE A H    1 
ATOM   1794  H HA   . ILE A 1 114 ? 40.925  -19.509 93.573  1.00 67.01  ?  123 ILE A HA   1 
ATOM   1795  H HB   . ILE A 1 114 ? 39.026  -18.181 94.214  1.00 50.33  ?  123 ILE A HB   1 
ATOM   1796  H HG12 . ILE A 1 114 ? 38.578  -20.829 94.989  1.00 49.70  ?  123 ILE A HG12 1 
ATOM   1797  H HG13 . ILE A 1 114 ? 39.903  -20.095 95.457  1.00 49.70  ?  123 ILE A HG13 1 
ATOM   1798  H HG21 . ILE A 1 114 ? 36.892  -19.063 93.807  1.00 55.51  ?  123 ILE A HG21 1 
ATOM   1799  H HG22 . ILE A 1 114 ? 37.618  -18.735 92.431  1.00 55.51  ?  123 ILE A HG22 1 
ATOM   1800  H HG23 . ILE A 1 114 ? 37.543  -20.234 92.953  1.00 55.51  ?  123 ILE A HG23 1 
ATOM   1801  H HD11 . ILE A 1 114 ? 38.313  -20.008 97.138  1.00 51.26  ?  123 ILE A HD11 1 
ATOM   1802  H HD12 . ILE A 1 114 ? 38.630  -18.537 96.626  1.00 51.26  ?  123 ILE A HD12 1 
ATOM   1803  H HD13 . ILE A 1 114 ? 37.302  -19.273 96.157  1.00 51.26  ?  123 ILE A HD13 1 
ATOM   1804  N N    . LEU A 1 115 ? 40.285  -21.815 93.187  1.00 57.42  ?  124 LEU A N    1 
ATOM   1805  C CA   . LEU A 1 115 ? 40.204  -23.181 92.738  1.00 58.59  ?  124 LEU A CA   1 
ATOM   1806  C C    . LEU A 1 115 ? 38.739  -23.542 92.554  1.00 73.82  ?  124 LEU A C    1 
ATOM   1807  O O    . LEU A 1 115 ? 37.942  -23.469 93.497  1.00 77.99  ?  124 LEU A O    1 
ATOM   1808  C CB   . LEU A 1 115 ? 40.860  -24.073 93.771  1.00 66.72  ?  124 LEU A CB   1 
ATOM   1809  C CG   . LEU A 1 115 ? 41.058  -25.519 93.356  1.00 68.09  ?  124 LEU A CG   1 
ATOM   1810  C CD1  . LEU A 1 115 ? 42.192  -25.581 92.369  1.00 45.68  ?  124 LEU A CD1  1 
ATOM   1811  C CD2  . LEU A 1 115 ? 41.326  -26.362 94.554  1.00 49.23  ?  124 LEU A CD2  1 
ATOM   1812  H H    . LEU A 1 115 ? 40.577  -21.724 93.990  1.00 68.91  ?  124 LEU A H    1 
ATOM   1813  H HA   . LEU A 1 115 ? 40.666  -23.282 91.891  1.00 70.31  ?  124 LEU A HA   1 
ATOM   1814  H HB2  . LEU A 1 115 ? 41.735  -23.709 93.980  1.00 80.07  ?  124 LEU A HB2  1 
ATOM   1815  H HB3  . LEU A 1 115 ? 40.310  -24.073 94.570  1.00 80.07  ?  124 LEU A HB3  1 
ATOM   1816  H HG   . LEU A 1 115 ? 40.253  -25.845 92.923  1.00 81.71  ?  124 LEU A HG   1 
ATOM   1817  H HD11 . LEU A 1 115 ? 42.325  -26.503 92.099  1.00 54.81  ?  124 LEU A HD11 1 
ATOM   1818  H HD12 . LEU A 1 115 ? 41.969  -25.038 91.597  1.00 54.81  ?  124 LEU A HD12 1 
ATOM   1819  H HD13 . LEU A 1 115 ? 42.996  -25.240 92.792  1.00 54.81  ?  124 LEU A HD13 1 
ATOM   1820  H HD21 . LEU A 1 115 ? 41.450  -27.282 94.270  1.00 59.08  ?  124 LEU A HD21 1 
ATOM   1821  H HD22 . LEU A 1 115 ? 42.129  -26.040 94.992  1.00 59.08  ?  124 LEU A HD22 1 
ATOM   1822  H HD23 . LEU A 1 115 ? 40.571  -26.301 95.159  1.00 59.08  ?  124 LEU A HD23 1 
ATOM   1823  N N    . VAL A 1 116 ? 38.381  -23.941 91.352  1.00 55.57  ?  125 VAL A N    1 
ATOM   1824  C CA   . VAL A 1 116 ? 37.037  -24.418 91.107  1.00 54.47  ?  125 VAL A CA   1 
ATOM   1825  C C    . VAL A 1 116 ? 37.080  -25.888 90.643  1.00 54.28  ?  125 VAL A C    1 
ATOM   1826  O O    . VAL A 1 116 ? 38.124  -26.430 90.264  1.00 68.85  ?  125 VAL A O    1 
ATOM   1827  C CB   . VAL A 1 116 ? 36.322  -23.543 90.088  1.00 45.08  ?  125 VAL A CB   1 
ATOM   1828  C CG1  . VAL A 1 116 ? 36.231  -22.104 90.624  1.00 46.54  ?  125 VAL A CG1  1 
ATOM   1829  C CG2  . VAL A 1 116 ? 37.014  -23.681 88.746  1.00 54.88  ?  125 VAL A CG2  1 
ATOM   1830  H H    . VAL A 1 116 ? 38.894  -23.947 90.662  1.00 66.68  ?  125 VAL A H    1 
ATOM   1831  H HA   . VAL A 1 116 ? 36.535  -24.381 91.935  1.00 65.37  ?  125 VAL A HA   1 
ATOM   1832  H HB   . VAL A 1 116 ? 35.416  -23.871 89.983  1.00 54.09  ?  125 VAL A HB   1 
ATOM   1833  H HG11 . VAL A 1 116 ? 35.775  -21.552 89.969  1.00 55.85  ?  125 VAL A HG11 1 
ATOM   1834  H HG12 . VAL A 1 116 ? 35.735  -22.109 91.457  1.00 55.85  ?  125 VAL A HG12 1 
ATOM   1835  H HG13 . VAL A 1 116 ? 37.128  -21.766 90.774  1.00 55.85  ?  125 VAL A HG13 1 
ATOM   1836  H HG21 . VAL A 1 116 ? 36.558  -23.122 88.098  1.00 65.85  ?  125 VAL A HG21 1 
ATOM   1837  H HG22 . VAL A 1 116 ? 37.937  -23.397 88.837  1.00 65.85  ?  125 VAL A HG22 1 
ATOM   1838  H HG23 . VAL A 1 116 ? 36.979  -24.609 88.467  1.00 65.85  ?  125 VAL A HG23 1 
ATOM   1839  N N    . TYR A 1 117 ? 35.897  -26.492 90.625  1.00 55.77  ?  126 TYR A N    1 
ATOM   1840  C CA   . TYR A 1 117 ? 35.722  -27.919 90.340  1.00 47.73  ?  126 TYR A CA   1 
ATOM   1841  C C    . TYR A 1 117 ? 36.311  -28.321 88.991  1.00 35.41  ?  126 TYR A C    1 
ATOM   1842  O O    . TYR A 1 117 ? 36.911  -29.395 88.855  1.00 93.61  ?  126 TYR A O    1 
ATOM   1843  C CB   . TYR A 1 117 ? 34.208  -28.178 90.451  1.00 47.67  ?  126 TYR A CB   1 
ATOM   1844  C CG   . TYR A 1 117 ? 33.647  -29.477 90.046  1.00 72.62  ?  126 TYR A CG   1 
ATOM   1845  C CD1  . TYR A 1 117 ? 33.498  -29.771 88.730  1.00 67.83  ?  126 TYR A CD1  1 
ATOM   1846  C CD2  . TYR A 1 117 ? 33.130  -30.334 90.975  1.00 61.80  ?  126 TYR A CD2  1 
ATOM   1847  C CE1  . TYR A 1 117 ? 32.961  -30.915 88.355  1.00 63.85  ?  126 TYR A CE1  1 
ATOM   1848  C CE2  . TYR A 1 117 ? 32.555  -31.504 90.602  1.00 52.48  ?  126 TYR A CE2  1 
ATOM   1849  C CZ   . TYR A 1 117 ? 32.470  -31.784 89.289  1.00 53.41  ?  126 TYR A CZ   1 
ATOM   1850  O OH   . TYR A 1 117 ? 31.854  -32.930 88.857  1.00 65.17  ?  126 TYR A OH   1 
ATOM   1851  H H    . TYR A 1 117 ? 35.156  -26.085 90.779  1.00 66.92  ?  126 TYR A H    1 
ATOM   1852  H HA   . TYR A 1 117 ? 36.167  -28.437 91.028  1.00 57.27  ?  126 TYR A HA   1 
ATOM   1853  H HB2  . TYR A 1 117 ? 33.959  -28.050 91.380  1.00 57.20  ?  126 TYR A HB2  1 
ATOM   1854  H HB3  . TYR A 1 117 ? 33.758  -27.506 89.915  1.00 57.20  ?  126 TYR A HB3  1 
ATOM   1855  H HD1  . TYR A 1 117 ? 33.833  -29.188 88.087  1.00 81.39  ?  126 TYR A HD1  1 
ATOM   1856  H HD2  . TYR A 1 117 ? 33.200  -30.127 91.879  1.00 74.16  ?  126 TYR A HD2  1 
ATOM   1857  H HE1  . TYR A 1 117 ? 32.875  -31.111 87.450  1.00 76.61  ?  126 TYR A HE1  1 
ATOM   1858  H HE2  . TYR A 1 117 ? 32.218  -32.094 91.237  1.00 62.98  ?  126 TYR A HE2  1 
ATOM   1859  H HH   . TYR A 1 117 ? 31.856  -32.958 88.018  1.00 78.20  ?  126 TYR A HH   1 
ATOM   1860  N N    . ALA A 1 118 ? 36.232  -27.407 88.022  1.00 38.22  ?  127 ALA A N    1 
ATOM   1861  C CA   . ALA A 1 118 ? 36.762  -27.664 86.696  1.00 72.89  ?  127 ALA A CA   1 
ATOM   1862  C C    . ALA A 1 118 ? 38.270  -27.687 86.709  1.00 56.07  ?  127 ALA A C    1 
ATOM   1863  O O    . ALA A 1 118 ? 38.875  -28.059 85.683  1.00 39.52  ?  127 ALA A O    1 
ATOM   1864  C CB   . ALA A 1 118 ? 36.295  -26.603 85.707  1.00 65.52  ?  127 ALA A CB   1 
ATOM   1865  H H    . ALA A 1 118 ? 35.874  -26.630 88.113  1.00 45.87  ?  127 ALA A H    1 
ATOM   1866  H HA   . ALA A 1 118 ? 36.447  -28.528 86.388  1.00 87.46  ?  127 ALA A HA   1 
ATOM   1867  H HB1  . ALA A 1 118 ? 36.665  -26.802 84.833  1.00 78.62  ?  127 ALA A HB1  1 
ATOM   1868  H HB2  . ALA A 1 118 ? 35.326  -26.615 85.667  1.00 78.62  ?  127 ALA A HB2  1 
ATOM   1869  H HB3  . ALA A 1 118 ? 36.603  -25.734 86.008  1.00 78.62  ?  127 ALA A HB3  1 
ATOM   1870  N N    . ASP A 1 119 ? 38.855  -27.189 87.814  1.00 45.70  ?  128 ASP A N    1 
ATOM   1871  C CA   . ASP A 1 119 ? 40.286  -27.349 88.125  1.00 48.74  ?  128 ASP A CA   1 
ATOM   1872  C C    . ASP A 1 119 ? 40.614  -28.722 88.718  1.00 67.65  ?  128 ASP A C    1 
ATOM   1873  O O    . ASP A 1 119 ? 41.074  -29.630 88.025  1.00 115.61 ?  128 ASP A O    1 
ATOM   1874  C CB   . ASP A 1 119 ? 40.722  -26.229 89.085  1.00 42.75  ?  128 ASP A CB   1 
ATOM   1875  C CG   . ASP A 1 119 ? 40.807  -24.890 88.386  1.00 52.33  ?  128 ASP A CG   1 
ATOM   1876  O OD1  . ASP A 1 119 ? 41.301  -24.890 87.210  1.00 50.73  ?  128 ASP A OD1  1 
ATOM   1877  O OD2  . ASP A 1 119 ? 40.455  -23.866 89.018  1.00 71.56  -1 128 ASP A OD2  1 
ATOM   1878  H H    . ASP A 1 119 ? 38.429  -26.743 88.413  1.00 54.84  ?  128 ASP A H    1 
ATOM   1879  H HA   . ASP A 1 119 ? 40.795  -27.252 87.306  1.00 58.49  ?  128 ASP A HA   1 
ATOM   1880  H HB2  . ASP A 1 119 ? 40.074  -26.155 89.804  1.00 51.30  ?  128 ASP A HB2  1 
ATOM   1881  H HB3  . ASP A 1 119 ? 41.598  -26.439 89.444  1.00 51.30  ?  128 ASP A HB3  1 
ATOM   1882  N N    . CYS A 1 120 ? 40.243  -28.896 89.975  1.00 50.90  ?  129 CYS A N    1 
ATOM   1883  C CA   . CYS A 1 120 ? 40.564  -29.982 90.823  1.00 190.47 ?  129 CYS A CA   1 
ATOM   1884  C C    . CYS A 1 120 ? 39.739  -31.199 90.499  1.00 88.86  ?  129 CYS A C    1 
ATOM   1885  O O    . CYS A 1 120 ? 39.958  -32.226 91.132  1.00 58.78  ?  129 CYS A O    1 
ATOM   1886  C CB   . CYS A 1 120 ? 40.332  -29.514 92.252  1.00 742.75 ?  129 CYS A CB   1 
ATOM   1887  S SG   . CYS A 1 120 ? 38.584  -29.144 92.620  1.00 503.70 ?  129 CYS A SG   1 
ATOM   1888  H H    . CYS A 1 120 ? 39.751  -28.320 90.381  1.00 61.08  ?  129 CYS A H    1 
ATOM   1889  H HA   . CYS A 1 120 ? 41.501  -30.209 90.720  1.00 228.56 ?  129 CYS A HA   1 
ATOM   1890  H HB2  . CYS A 1 120 ? 40.624  -30.209 92.862  1.00 891.30 ?  129 CYS A HB2  1 
ATOM   1891  H HB3  . CYS A 1 120 ? 40.846  -28.705 92.405  1.00 891.30 ?  129 CYS A HB3  1 
ATOM   1892  H HG   . CYS A 1 120 ? 38.492  -28.783 93.761  1.00 604.44 ?  129 CYS A HG   1 
ATOM   1893  N N    . VAL A 1 121 ? 38.818  -31.172 89.514  1.00 60.63  ?  130 VAL A N    1 
ATOM   1894  C CA   . VAL A 1 121 ? 38.164  -32.392 89.055  1.00 43.58  ?  130 VAL A CA   1 
ATOM   1895  C C    . VAL A 1 121 ? 38.318  -32.594 87.570  1.00 68.04  ?  130 VAL A C    1 
ATOM   1896  O O    . VAL A 1 121 ? 38.712  -33.666 87.135  1.00 64.12  ?  130 VAL A O    1 
ATOM   1897  C CB   . VAL A 1 121 ? 36.665  -32.444 89.440  1.00 48.02  ?  130 VAL A CB   1 
ATOM   1898  C CG1  . VAL A 1 121 ? 36.031  -33.756 88.826  1.00 46.58  ?  130 VAL A CG1  1 
ATOM   1899  C CG2  . VAL A 1 121 ? 36.433  -32.378 90.959  1.00 46.03  ?  130 VAL A CG2  1 
ATOM   1900  H H    . VAL A 1 121 ? 38.563  -30.460 89.105  1.00 72.76  ?  130 VAL A H    1 
ATOM   1901  H HA   . VAL A 1 121 ? 38.595  -33.144 89.490  1.00 52.30  ?  130 VAL A HA   1 
ATOM   1902  H HB   . VAL A 1 121 ? 36.214  -31.684 89.040  1.00 57.63  ?  130 VAL A HB   1 
ATOM   1903  H HG11 . VAL A 1 121 ? 35.092  -33.794 89.064  1.00 55.90  ?  130 VAL A HG11 1 
ATOM   1904  H HG12 . VAL A 1 121 ? 36.128  -33.731 87.861  1.00 55.90  ?  130 VAL A HG12 1 
ATOM   1905  H HG13 . VAL A 1 121 ? 36.496  -34.529 89.185  1.00 55.90  ?  130 VAL A HG13 1 
ATOM   1906  H HG21 . VAL A 1 121 ? 35.480  -32.415 91.134  1.00 55.23  ?  130 VAL A HG21 1 
ATOM   1907  H HG22 . VAL A 1 121 ? 36.876  -33.132 91.379  1.00 55.23  ?  130 VAL A HG22 1 
ATOM   1908  H HG23 . VAL A 1 121 ? 36.800  -31.547 91.298  1.00 55.23  ?  130 VAL A HG23 1 
ATOM   1909  N N    . LEU A 1 122 ? 38.016  -31.581 86.768  1.00 46.62  ?  131 LEU A N    1 
ATOM   1910  C CA   . LEU A 1 122 ? 38.039  -31.867 85.333  1.00 60.72  ?  131 LEU A CA   1 
ATOM   1911  C C    . LEU A 1 122 ? 39.442  -31.854 84.711  1.00 73.84  ?  131 LEU A C    1 
ATOM   1912  O O    . LEU A 1 122 ? 39.600  -32.335 83.584  1.00 82.57  ?  131 LEU A O    1 
ATOM   1913  C CB   . LEU A 1 122 ? 37.167  -30.870 84.595  1.00 61.63  ?  131 LEU A CB   1 
ATOM   1914  C CG   . LEU A 1 122 ? 35.737  -30.804 85.102  1.00 57.53  ?  131 LEU A CG   1 
ATOM   1915  C CD1  . LEU A 1 122 ? 34.965  -29.665 84.485  1.00 48.82  ?  131 LEU A CD1  1 
ATOM   1916  C CD2  . LEU A 1 122 ? 35.042  -32.103 84.796  1.00 57.98  ?  131 LEU A CD2  1 
ATOM   1917  H H    . LEU A 1 122 ? 37.809  -30.779 87.001  1.00 55.94  ?  131 LEU A H    1 
ATOM   1918  H HA   . LEU A 1 122 ? 37.663  -32.749 85.188  1.00 72.87  ?  131 LEU A HA   1 
ATOM   1919  H HB2  . LEU A 1 122 ? 37.556  -29.986 84.689  1.00 73.95  ?  131 LEU A HB2  1 
ATOM   1920  H HB3  . LEU A 1 122 ? 37.137  -31.116 83.657  1.00 73.95  ?  131 LEU A HB3  1 
ATOM   1921  H HG   . LEU A 1 122 ? 35.744  -30.681 86.064  1.00 69.03  ?  131 LEU A HG   1 
ATOM   1922  H HD11 . LEU A 1 122 ? 34.062  -29.667 84.841  1.00 58.59  ?  131 LEU A HD11 1 
ATOM   1923  H HD12 . LEU A 1 122 ? 35.405  -28.830 84.705  1.00 58.59  ?  131 LEU A HD12 1 
ATOM   1924  H HD13 . LEU A 1 122 ? 34.942  -29.785 83.523  1.00 58.59  ?  131 LEU A HD13 1 
ATOM   1925  H HD21 . LEU A 1 122 ? 34.130  -32.057 85.122  1.00 69.58  ?  131 LEU A HD21 1 
ATOM   1926  H HD22 . LEU A 1 122 ? 35.045  -32.244 83.837  1.00 69.58  ?  131 LEU A HD22 1 
ATOM   1927  H HD23 . LEU A 1 122 ? 35.515  -32.826 85.238  1.00 69.58  ?  131 LEU A HD23 1 
ATOM   1928  N N    . ALA A 1 123 ? 40.446  -31.257 85.366  1.00 57.56  ?  132 ALA A N    1 
ATOM   1929  C CA   . ALA A 1 123 ? 41.759  -31.098 84.750  1.00 71.80  ?  132 ALA A CA   1 
ATOM   1930  C C    . ALA A 1 123 ? 42.857  -31.726 85.587  1.00 73.59  ?  132 ALA A C    1 
ATOM   1931  O O    . ALA A 1 123 ? 44.039  -31.633 85.216  1.00 57.78  ?  132 ALA A O    1 
ATOM   1932  C CB   . ALA A 1 123 ? 42.035  -29.610 84.491  1.00 60.91  ?  132 ALA A CB   1 
ATOM   1933  H H    . ALA A 1 123 ? 40.389  -30.940 86.164  1.00 69.07  ?  132 ALA A H    1 
ATOM   1934  H HA   . ALA A 1 123 ? 41.753  -31.548 83.891  1.00 86.16  ?  132 ALA A HA   1 
ATOM   1935  H HB1  . ALA A 1 123 ? 42.909  -29.518 84.082  1.00 73.09  ?  132 ALA A HB1  1 
ATOM   1936  H HB2  . ALA A 1 123 ? 41.352  -29.261 83.897  1.00 73.09  ?  132 ALA A HB2  1 
ATOM   1937  H HB3  . ALA A 1 123 ? 42.013  -29.134 85.336  1.00 73.09  ?  132 ALA A HB3  1 
ATOM   1938  N N    . ASN A 1 124 ? 42.477  -32.405 86.676  1.00 60.83  ?  133 ASN A N    1 
ATOM   1939  C CA   . ASN A 1 124 ? 43.367  -32.934 87.697  1.00 47.57  ?  133 ASN A CA   1 
ATOM   1940  C C    . ASN A 1 124 ? 43.452  -34.447 87.625  1.00 51.45  ?  133 ASN A C    1 
ATOM   1941  O O    . ASN A 1 124 ? 43.243  -35.090 88.669  1.00 44.70  ?  133 ASN A O    1 
ATOM   1942  C CB   . ASN A 1 124 ? 42.804  -32.568 89.051  1.00 42.80  ?  133 ASN A CB   1 
ATOM   1943  C CG   . ASN A 1 124 ? 43.698  -32.878 90.222  1.00 48.63  ?  133 ASN A CG   1 
ATOM   1944  O OD1  . ASN A 1 124 ? 44.931  -32.992 90.117  1.00 61.79  ?  133 ASN A OD1  1 
ATOM   1945  N ND2  . ASN A 1 124 ? 43.083  -32.838 91.422  1.00 53.57  ?  133 ASN A ND2  1 
ATOM   1946  H H    . ASN A 1 124 ? 41.652  -32.577 86.846  1.00 73.00  ?  133 ASN A H    1 
ATOM   1947  H HA   . ASN A 1 124 ? 44.255  -32.555 87.603  1.00 57.08  ?  133 ASN A HA   1 
ATOM   1948  H HB2  . ASN A 1 124 ? 42.626  -31.615 89.064  1.00 51.36  ?  133 ASN A HB2  1 
ATOM   1949  H HB3  . ASN A 1 124 ? 41.974  -33.054 89.181  1.00 51.36  ?  133 ASN A HB3  1 
ATOM   1950  H HD21 . ASN A 1 124 ? 43.528  -33.004 92.139  1.00 64.29  ?  133 ASN A HD21 1 
ATOM   1951  H HD22 . ASN A 1 124 ? 42.246  -32.648 91.470  1.00 64.29  ?  133 ASN A HD22 1 
ATOM   1952  N N    . TRP A 1 125 ? 43.734  -35.029 86.441  1.00 72.76  ?  134 TRP A N    1 
ATOM   1953  C CA   . TRP A 1 125 ? 43.655  -36.490 86.340  1.00 75.11  ?  134 TRP A CA   1 
ATOM   1954  C C    . TRP A 1 125 ? 44.472  -37.050 85.164  1.00 69.77  ?  134 TRP A C    1 
ATOM   1955  O O    . TRP A 1 125 ? 44.643  -36.412 84.126  1.00 52.55  ?  134 TRP A O    1 
ATOM   1956  C CB   . TRP A 1 125 ? 42.172  -36.978 86.222  1.00 68.70  ?  134 TRP A CB   1 
ATOM   1957  C CG   . TRP A 1 125 ? 41.550  -36.614 84.961  1.00 56.30  ?  134 TRP A CG   1 
ATOM   1958  C CD1  . TRP A 1 125 ? 40.892  -35.469 84.683  1.00 55.64  ?  134 TRP A CD1  1 
ATOM   1959  C CD2  . TRP A 1 125 ? 41.577  -37.373 83.729  1.00 67.85  ?  134 TRP A CD2  1 
ATOM   1960  N NE1  . TRP A 1 125 ? 40.484  -35.462 83.330  1.00 57.61  ?  134 TRP A NE1  1 
ATOM   1961  C CE2  . TRP A 1 125 ? 40.887  -36.623 82.745  1.00 63.70  ?  134 TRP A CE2  1 
ATOM   1962  C CE3  . TRP A 1 125 ? 42.106  -38.604 83.371  1.00 78.08  ?  134 TRP A CE3  1 
ATOM   1963  C CZ2  . TRP A 1 125 ? 40.687  -37.079 81.452  1.00 75.44  ?  134 TRP A CZ2  1 
ATOM   1964  C CZ3  . TRP A 1 125 ? 41.910  -39.048 82.065  1.00 92.65  ?  134 TRP A CZ3  1 
ATOM   1965  C CH2  . TRP A 1 125 ? 41.205  -38.285 81.126  1.00 85.90  ?  134 TRP A CH2  1 
ATOM   1966  H H    . TRP A 1 125 ? 43.963  -34.619 85.721  1.00 87.31  ?  134 TRP A H    1 
ATOM   1967  H HA   . TRP A 1 125 ? 44.021  -36.871 87.153  1.00 90.13  ?  134 TRP A HA   1 
ATOM   1968  H HB2  . TRP A 1 125 ? 42.152  -37.945 86.298  1.00 82.44  ?  134 TRP A HB2  1 
ATOM   1969  H HB3  . TRP A 1 125 ? 41.652  -36.579 86.938  1.00 82.44  ?  134 TRP A HB3  1 
ATOM   1970  H HD1  . TRP A 1 125 ? 40.742  -34.780 85.289  1.00 66.77  ?  134 TRP A HD1  1 
ATOM   1971  H HE1  . TRP A 1 125 ? 40.028  -34.840 82.948  1.00 69.13  ?  134 TRP A HE1  1 
ATOM   1972  H HE3  . TRP A 1 125 ? 42.560  -39.128 83.991  1.00 93.70  ?  134 TRP A HE3  1 
ATOM   1973  H HZ2  . TRP A 1 125 ? 40.234  -36.564 80.824  1.00 90.53  ?  134 TRP A HZ2  1 
ATOM   1974  H HZ3  . TRP A 1 125 ? 42.251  -39.875 81.812  1.00 111.18 ?  134 TRP A HZ3  1 
ATOM   1975  H HH2  . TRP A 1 125 ? 41.103  -38.607 80.260  1.00 103.08 ?  134 TRP A HH2  1 
ATOM   1976  N N    . LYS A 1 126 ? 44.886  -38.310 85.305  1.00 65.29  ?  135 LYS A N    1 
ATOM   1977  C CA   . LYS A 1 126 ? 45.682  -38.998 84.295  1.00 84.46  ?  135 LYS A CA   1 
ATOM   1978  C C    . LYS A 1 126 ? 45.243  -40.444 84.326  1.00 101.48 ?  135 LYS A C    1 
ATOM   1979  O O    . LYS A 1 126 ? 44.752  -40.930 85.352  1.00 49.16  ?  135 LYS A O    1 
ATOM   1980  C CB   . LYS A 1 126 ? 47.204  -38.878 84.521  1.00 72.00  ?  135 LYS A CB   1 
ATOM   1981  C CG   . LYS A 1 126 ? 47.733  -39.359 85.890  1.00 109.23 ?  135 LYS A CG   1 
ATOM   1982  C CD   . LYS A 1 126 ? 49.253  -39.512 85.903  1.00 112.17 ?  135 LYS A CD   1 
ATOM   1983  H H    . LYS A 1 126 ? 44.715  -38.794 85.995  1.00 78.34  ?  135 LYS A H    1 
ATOM   1984  H HA   . LYS A 1 126 ? 45.474  -38.635 83.420  1.00 101.36 ?  135 LYS A HA   1 
ATOM   1985  H HB2  . LYS A 1 126 ? 47.655  -39.399 83.838  1.00 86.40  ?  135 LYS A HB2  1 
ATOM   1986  H HB3  . LYS A 1 126 ? 47.452  -37.945 84.428  1.00 86.40  ?  135 LYS A HB3  1 
ATOM   1987  H HG2  . LYS A 1 126 ? 47.489  -38.712 86.570  1.00 131.07 ?  135 LYS A HG2  1 
ATOM   1988  H HG3  . LYS A 1 126 ? 47.341  -40.223 86.096  1.00 131.07 ?  135 LYS A HG3  1 
ATOM   1989  H HD2  . LYS A 1 126 ? 49.543  -39.860 85.045  1.00 134.60 ?  135 LYS A HD2  1 
ATOM   1990  H HD3  . LYS A 1 126 ? 49.656  -38.644 86.062  1.00 134.60 ?  135 LYS A HD3  1 
ATOM   1991  N N    . LYS A 1 127 ? 45.306  -41.098 83.178  1.00 178.83 ?  136 LYS A N    1 
ATOM   1992  C CA   . LYS A 1 127 ? 45.197  -42.546 83.166  1.00 133.09 ?  136 LYS A CA   1 
ATOM   1993  C C    . LYS A 1 127 ? 46.598  -43.144 83.191  1.00 238.11 ?  136 LYS A C    1 
ATOM   1994  O O    . LYS A 1 127 ? 47.483  -42.719 82.444  1.00 188.96 ?  136 LYS A O    1 
ATOM   1995  C CB   . LYS A 1 127 ? 44.356  -43.051 81.991  1.00 111.71 ?  136 LYS A CB   1 
ATOM   1996  C CG   . LYS A 1 127 ? 44.791  -42.656 80.622  1.00 97.21  ?  136 LYS A CG   1 
ATOM   1997  C CD   . LYS A 1 127 ? 43.663  -42.803 79.585  1.00 119.24 ?  136 LYS A CD   1 
ATOM   1998  C CE   . LYS A 1 127 ? 43.052  -44.208 79.559  1.00 127.87 ?  136 LYS A CE   1 
ATOM   1999  N NZ   . LYS A 1 127 ? 42.104  -44.403 78.423  1.00 98.02  1  136 LYS A NZ   1 
ATOM   2000  H H    . LYS A 1 127 ? 45.409  -40.735 82.405  1.00 214.60 ?  136 LYS A H    1 
ATOM   2001  H HA   . LYS A 1 127 ? 44.750  -42.824 83.981  1.00 159.71 ?  136 LYS A HA   1 
ATOM   2002  H HB2  . LYS A 1 127 ? 44.350  -44.021 82.020  1.00 134.05 ?  136 LYS A HB2  1 
ATOM   2003  H HB3  . LYS A 1 127 ? 43.450  -42.724 82.107  1.00 134.05 ?  136 LYS A HB3  1 
ATOM   2004  H HG2  . LYS A 1 127 ? 45.071  -41.728 80.633  1.00 116.65 ?  136 LYS A HG2  1 
ATOM   2005  H HG3  . LYS A 1 127 ? 45.528  -43.224 80.347  1.00 116.65 ?  136 LYS A HG3  1 
ATOM   2006  H HD2  . LYS A 1 127 ? 42.956  -42.173 79.797  1.00 143.09 ?  136 LYS A HD2  1 
ATOM   2007  H HD3  . LYS A 1 127 ? 44.020  -42.616 78.703  1.00 143.09 ?  136 LYS A HD3  1 
ATOM   2008  H HE2  . LYS A 1 127 ? 43.764  -44.861 79.471  1.00 153.45 ?  136 LYS A HE2  1 
ATOM   2009  H HE3  . LYS A 1 127 ? 42.565  -44.356 80.385  1.00 153.45 ?  136 LYS A HE3  1 
ATOM   2010  H HZ1  . LYS A 1 127 ? 41.772  -45.228 78.442  1.00 117.62 ?  136 LYS A HZ1  1 
ATOM   2011  H HZ2  . LYS A 1 127 ? 41.435  -43.820 78.482  1.00 117.62 ?  136 LYS A HZ2  1 
ATOM   2012  H HZ3  . LYS A 1 127 ? 42.527  -44.280 77.650  1.00 117.62 ?  136 LYS A HZ3  1 
ATOM   2013  N N    . LYS A 1 128 ? 46.801  -44.085 84.110  1.00 205.96 ?  137 LYS A N    1 
ATOM   2014  C CA   . LYS A 1 128 ? 48.107  -44.698 84.300  1.00 176.74 ?  137 LYS A CA   1 
ATOM   2015  C C    . LYS A 1 128 ? 48.561  -45.395 83.036  1.00 214.74 ?  137 LYS A C    1 
ATOM   2016  O O    . LYS A 1 128 ? 49.637  -45.114 82.501  1.00 211.68 ?  137 LYS A O    1 
ATOM   2017  C CB   . LYS A 1 128 ? 48.007  -45.717 85.421  1.00 135.38 ?  137 LYS A CB   1 
ATOM   2018  C CG   . LYS A 1 128 ? 47.798  -45.096 86.751  1.00 61.70  ?  137 LYS A CG   1 
ATOM   2019  C CD   . LYS A 1 128 ? 47.399  -46.103 87.901  1.00 61.57  ?  137 LYS A CD   1 
ATOM   2020  C CE   . LYS A 1 128 ? 47.294  -45.413 89.288  1.00 73.89  ?  137 LYS A CE   1 
ATOM   2021  N NZ   . LYS A 1 128 ? 46.797  -46.265 90.383  1.00 105.76 1  137 LYS A NZ   1 
ATOM   2022  H H    . LYS A 1 128 ? 46.193  -44.387 84.638  1.00 247.15 ?  137 LYS A H    1 
ATOM   2023  H HA   . LYS A 1 128 ? 48.760  -44.022 84.542  1.00 212.09 ?  137 LYS A HA   1 
ATOM   2024  H HB2  . LYS A 1 128 ? 47.256  -46.306 85.245  1.00 162.45 ?  137 LYS A HB2  1 
ATOM   2025  H HB3  . LYS A 1 128 ? 48.829  -46.229 85.456  1.00 162.45 ?  137 LYS A HB3  1 
ATOM   2026  H HG2  . LYS A 1 128 ? 48.620  -44.657 87.019  1.00 74.04  ?  137 LYS A HG2  1 
ATOM   2027  H HG3  . LYS A 1 128 ? 47.088  -44.440 86.677  1.00 74.04  ?  137 LYS A HG3  1 
ATOM   2028  H HD2  . LYS A 1 128 ? 46.536  -46.495 87.694  1.00 73.89  ?  137 LYS A HD2  1 
ATOM   2029  H HD3  . LYS A 1 128 ? 48.073  -46.798 87.962  1.00 73.89  ?  137 LYS A HD3  1 
ATOM   2030  H HE2  . LYS A 1 128 ? 48.176  -45.098 89.541  1.00 88.67  ?  137 LYS A HE2  1 
ATOM   2031  H HE3  . LYS A 1 128 ? 46.690  -44.658 89.209  1.00 88.67  ?  137 LYS A HE3  1 
ATOM   2032  H HZ1  . LYS A 1 128 ? 46.766  -45.799 91.140  1.00 126.91 ?  137 LYS A HZ1  1 
ATOM   2033  H HZ2  . LYS A 1 128 ? 45.980  -46.560 90.191  1.00 126.91 ?  137 LYS A HZ2  1 
ATOM   2034  H HZ3  . LYS A 1 128 ? 47.338  -46.963 90.495  1.00 126.91 ?  137 LYS A HZ3  1 
ATOM   2035  N N    . ASP A 1 129 ? 47.741  -46.306 82.540  1.00 114.38 ?  138 ASP A N    1 
ATOM   2036  C CA   . ASP A 1 129 ? 48.008  -47.013 81.302  1.00 80.24  ?  138 ASP A CA   1 
ATOM   2037  C C    . ASP A 1 129 ? 47.046  -46.536 80.219  1.00 203.94 ?  138 ASP A C    1 
ATOM   2038  O O    . ASP A 1 129 ? 45.853  -46.875 80.259  1.00 87.68  ?  138 ASP A O    1 
ATOM   2039  C CB   . ASP A 1 129 ? 47.867  -48.519 81.523  1.00 87.49  ?  138 ASP A CB   1 
ATOM   2040  C CG   . ASP A 1 129 ? 48.322  -49.361 80.312  1.00 95.31  ?  138 ASP A CG   1 
ATOM   2041  O OD1  . ASP A 1 129 ? 48.539  -48.798 79.220  1.00 109.91 ?  138 ASP A OD1  1 
ATOM   2042  O OD2  . ASP A 1 129 ? 48.429  -50.602 80.447  1.00 172.64 -1 138 ASP A OD2  1 
ATOM   2043  H H    . ASP A 1 129 ? 47.002  -46.537 82.915  1.00 137.25 ?  138 ASP A H    1 
ATOM   2044  H HA   . ASP A 1 129 ? 48.914  -46.827 81.012  1.00 96.29  ?  138 ASP A HA   1 
ATOM   2045  H HB2  . ASP A 1 129 ? 48.408  -48.776 82.286  1.00 104.99 ?  138 ASP A HB2  1 
ATOM   2046  H HB3  . ASP A 1 129 ? 46.935  -48.725 81.696  1.00 104.99 ?  138 ASP A HB3  1 
ATOM   2047  N N    . PRO A 1 130 ? 47.516  -45.774 79.236  1.00 123.98 ?  139 PRO A N    1 
ATOM   2048  C CA   . PRO A 1 130 ? 46.623  -45.283 78.167  1.00 108.12 ?  139 PRO A CA   1 
ATOM   2049  C C    . PRO A 1 130 ? 45.721  -46.318 77.518  1.00 119.22 ?  139 PRO A C    1 
ATOM   2050  O O    . PRO A 1 130 ? 44.561  -46.021 77.207  1.00 122.20 ?  139 PRO A O    1 
ATOM   2051  C CB   . PRO A 1 130 ? 47.618  -44.740 77.141  1.00 107.21 ?  139 PRO A CB   1 
ATOM   2052  C CG   . PRO A 1 130 ? 48.822  -44.321 77.978  1.00 97.75  ?  139 PRO A CG   1 
ATOM   2053  C CD   . PRO A 1 130 ? 48.879  -45.221 79.140  1.00 91.22  ?  139 PRO A CD   1 
ATOM   2054  H HA   . PRO A 1 130 ? 46.078  -44.551 78.498  1.00 129.74 ?  139 PRO A HA   1 
ATOM   2055  H HB2  . PRO A 1 130 ? 47.860  -45.440 76.514  1.00 128.65 ?  139 PRO A HB2  1 
ATOM   2056  H HB3  . PRO A 1 130 ? 47.234  -43.978 76.680  1.00 128.65 ?  139 PRO A HB3  1 
ATOM   2057  H HG2  . PRO A 1 130 ? 49.628  -44.406 77.446  1.00 117.30 ?  139 PRO A HG2  1 
ATOM   2058  H HG3  . PRO A 1 130 ? 48.705  -43.403 78.269  1.00 117.30 ?  139 PRO A HG3  1 
ATOM   2059  H HD2  . PRO A 1 130 ? 49.520  -45.932 78.982  1.00 109.46 ?  139 PRO A HD2  1 
ATOM   2060  H HD3  . PRO A 1 130 ? 49.096  -44.721 79.942  1.00 109.46 ?  139 PRO A HD3  1 
ATOM   2061  N N    . ASN A 1 131 ? 46.208  -47.531 77.299  1.00 116.45 ?  140 ASN A N    1 
ATOM   2062  C CA   . ASN A 1 131 ? 45.402  -48.478 76.552  1.00 106.31 ?  140 ASN A CA   1 
ATOM   2063  C C    . ASN A 1 131 ? 44.198  -48.948 77.359  1.00 125.26 ?  140 ASN A C    1 
ATOM   2064  O O    . ASN A 1 131 ? 43.136  -49.231 76.788  1.00 128.73 ?  140 ASN A O    1 
ATOM   2065  C CB   . ASN A 1 131 ? 46.280  -49.638 76.110  1.00 87.60  ?  140 ASN A CB   1 
ATOM   2066  C CG   . ASN A 1 131 ? 47.154  -49.286 74.916  1.00 107.95 ?  140 ASN A CG   1 
ATOM   2067  O OD1  . ASN A 1 131 ? 47.825  -48.261 74.909  1.00 127.76 ?  140 ASN A OD1  1 
ATOM   2068  N ND2  . ASN A 1 131 ? 47.130  -50.130 73.893  1.00 151.68 ?  140 ASN A ND2  1 
ATOM   2069  H H    . ASN A 1 131 ? 46.974  -47.821 77.561  1.00 139.74 ?  140 ASN A H    1 
ATOM   2070  H HA   . ASN A 1 131 ? 45.068  -48.041 75.754  1.00 127.57 ?  140 ASN A HA   1 
ATOM   2071  H HB2  . ASN A 1 131 ? 46.862  -49.893 76.844  1.00 105.12 ?  140 ASN A HB2  1 
ATOM   2072  H HB3  . ASN A 1 131 ? 45.715  -50.386 75.860  1.00 105.12 ?  140 ASN A HB3  1 
ATOM   2073  H HD21 . ASN A 1 131 ? 47.607  -49.973 73.195  1.00 182.02 ?  140 ASN A HD21 1 
ATOM   2074  H HD22 . ASN A 1 131 ? 46.637  -50.834 73.927  1.00 182.02 ?  140 ASN A HD22 1 
ATOM   2075  N N    . LYS A 1 132 ? 44.294  -48.924 78.667  1.00 128.57 ?  141 LYS A N    1 
ATOM   2076  C CA   . LYS A 1 132 ? 43.213  -49.440 79.473  1.00 126.88 ?  141 LYS A CA   1 
ATOM   2077  C C    . LYS A 1 132 ? 42.120  -48.389 79.656  1.00 97.29  ?  141 LYS A C    1 
ATOM   2078  O O    . LYS A 1 132 ? 42.351  -47.196 79.469  1.00 103.84 ?  141 LYS A O    1 
ATOM   2079  C CB   . LYS A 1 132 ? 43.780  -49.899 80.807  1.00 128.30 ?  141 LYS A CB   1 
ATOM   2080  C CG   . LYS A 1 132 ? 44.779  -51.059 80.652  1.00 107.96 ?  141 LYS A CG   1 
ATOM   2081  C CD   . LYS A 1 132 ? 45.413  -51.458 81.984  1.00 92.15  ?  141 LYS A CD   1 
ATOM   2082  C CE   . LYS A 1 132 ? 46.147  -52.744 81.930  1.00 113.64 ?  141 LYS A CE   1 
ATOM   2083  N NZ   . LYS A 1 132 ? 46.975  -52.893 83.138  1.00 126.66 1  141 LYS A NZ   1 
ATOM   2084  H H    . LYS A 1 132 ? 44.965  -48.619 79.111  1.00 154.29 ?  141 LYS A H    1 
ATOM   2085  H HA   . LYS A 1 132 ? 42.822  -50.209 79.029  1.00 152.26 ?  141 LYS A HA   1 
ATOM   2086  H HB2  . LYS A 1 132 ? 44.243  -49.157 81.226  1.00 153.96 ?  141 LYS A HB2  1 
ATOM   2087  H HB3  . LYS A 1 132 ? 43.053  -50.201 81.373  1.00 153.96 ?  141 LYS A HB3  1 
ATOM   2088  H HG2  . LYS A 1 132 ? 44.315  -51.832 80.296  1.00 129.55 ?  141 LYS A HG2  1 
ATOM   2089  H HG3  . LYS A 1 132 ? 45.489  -50.788 80.050  1.00 129.55 ?  141 LYS A HG3  1 
ATOM   2090  H HD2  . LYS A 1 132 ? 46.040  -50.768 82.252  1.00 110.58 ?  141 LYS A HD2  1 
ATOM   2091  H HD3  . LYS A 1 132 ? 44.714  -51.543 82.651  1.00 110.58 ?  141 LYS A HD3  1 
ATOM   2092  H HE2  . LYS A 1 132 ? 45.516  -53.479 81.894  1.00 136.37 ?  141 LYS A HE2  1 
ATOM   2093  H HE3  . LYS A 1 132 ? 46.728  -52.754 81.153  1.00 136.37 ?  141 LYS A HE3  1 
ATOM   2094  H HZ1  . LYS A 1 132 ? 47.418  -53.664 83.110  1.00 152.00 ?  141 LYS A HZ1  1 
ATOM   2095  H HZ2  . LYS A 1 132 ? 47.560  -52.224 83.190  1.00 152.00 ?  141 LYS A HZ2  1 
ATOM   2096  H HZ3  . LYS A 1 132 ? 46.458  -52.882 83.863  1.00 152.00 ?  141 LYS A HZ3  1 
ATOM   2097  N N    . PRO A 1 133 ? 40.919  -48.809 80.014  1.00 89.95  ?  142 PRO A N    1 
ATOM   2098  C CA   . PRO A 1 133 ? 39.780  -47.889 80.088  1.00 92.27  ?  142 PRO A CA   1 
ATOM   2099  C C    . PRO A 1 133 ? 39.809  -47.047 81.350  1.00 102.81 ?  142 PRO A C    1 
ATOM   2100  O O    . PRO A 1 133 ? 40.624  -47.273 82.226  1.00 76.06  ?  142 PRO A O    1 
ATOM   2101  C CB   . PRO A 1 133 ? 38.575  -48.818 80.101  1.00 98.64  ?  142 PRO A CB   1 
ATOM   2102  C CG   . PRO A 1 133 ? 39.085  -50.084 80.665  1.00 95.25  ?  142 PRO A CG   1 
ATOM   2103  C CD   . PRO A 1 133 ? 40.509  -50.210 80.198  1.00 84.78  ?  142 PRO A CD   1 
ATOM   2104  H HA   . PRO A 1 133 ? 39.746  -47.315 79.307  1.00 110.72 ?  142 PRO A HA   1 
ATOM   2105  H HB2  . PRO A 1 133 ? 37.879  -48.446 80.665  1.00 118.37 ?  142 PRO A HB2  1 
ATOM   2106  H HB3  . PRO A 1 133 ? 38.253  -48.950 79.196  1.00 118.37 ?  142 PRO A HB3  1 
ATOM   2107  H HG2  . PRO A 1 133 ? 39.048  -50.045 81.633  1.00 114.30 ?  142 PRO A HG2  1 
ATOM   2108  H HG3  . PRO A 1 133 ? 38.553  -50.824 80.333  1.00 114.30 ?  142 PRO A HG3  1 
ATOM   2109  H HD2  . PRO A 1 133 ? 41.053  -50.636 80.879  1.00 101.74 ?  142 PRO A HD2  1 
ATOM   2110  H HD3  . PRO A 1 133 ? 40.549  -50.689 79.356  1.00 101.74 ?  142 PRO A HD3  1 
ATOM   2111  N N    . LEU A 1 134 ? 38.847  -46.116 81.441  1.00 93.76  ?  143 LEU A N    1 
ATOM   2112  C CA   . LEU A 1 134 ? 38.744  -45.170 82.557  1.00 76.80  ?  143 LEU A CA   1 
ATOM   2113  C C    . LEU A 1 134 ? 38.032  -45.795 83.750  1.00 75.78  ?  143 LEU A C    1 
ATOM   2114  O O    . LEU A 1 134 ? 36.912  -45.439 84.121  1.00 76.13  ?  143 LEU A O    1 
ATOM   2115  C CB   . LEU A 1 134 ? 37.998  -43.917 82.135  1.00 82.56  ?  143 LEU A CB   1 
ATOM   2116  C CG   . LEU A 1 134 ? 38.698  -43.017 81.131  1.00 95.11  ?  143 LEU A CG   1 
ATOM   2117  C CD1  . LEU A 1 134 ? 37.788  -42.108 80.351  1.00 61.44  ?  143 LEU A CD1  1 
ATOM   2118  C CD2  . LEU A 1 134 ? 39.642  -42.171 81.926  1.00 132.69 ?  143 LEU A CD2  1 
ATOM   2119  H H    . LEU A 1 134 ? 38.229  -46.013 80.851  1.00 112.51 ?  143 LEU A H    1 
ATOM   2120  H HA   . LEU A 1 134 ? 39.635  -44.911 82.838  1.00 92.16  ?  143 LEU A HA   1 
ATOM   2121  H HB2  . LEU A 1 134 ? 37.154  -44.185 81.740  1.00 99.07  ?  143 LEU A HB2  1 
ATOM   2122  H HB3  . LEU A 1 134 ? 37.827  -43.385 82.928  1.00 99.07  ?  143 LEU A HB3  1 
ATOM   2123  H HG   . LEU A 1 134 ? 39.212  -43.555 80.509  1.00 114.14 ?  143 LEU A HG   1 
ATOM   2124  H HD11 . LEU A 1 134 ? 38.321  -41.575 79.741  1.00 73.73  ?  143 LEU A HD11 1 
ATOM   2125  H HD12 . LEU A 1 134 ? 37.154  -42.647 79.853  1.00 73.73  ?  143 LEU A HD12 1 
ATOM   2126  H HD13 . LEU A 1 134 ? 37.315  -41.528 80.970  1.00 73.73  ?  143 LEU A HD13 1 
ATOM   2127  H HD21 . LEU A 1 134 ? 40.115  -41.575 81.323  1.00 159.23 ?  143 LEU A HD21 1 
ATOM   2128  H HD22 . LEU A 1 134 ? 39.135  -41.654 82.571  1.00 159.23 ?  143 LEU A HD22 1 
ATOM   2129  H HD23 . LEU A 1 134 ? 40.272  -42.747 82.384  1.00 159.23 ?  143 LEU A HD23 1 
ATOM   2130  N N    . THR A 1 135 ? 38.739  -46.690 84.407  1.00 56.86  ?  144 THR A N    1 
ATOM   2131  C CA   . THR A 1 135 ? 38.267  -47.210 85.669  1.00 66.65  ?  144 THR A CA   1 
ATOM   2132  C C    . THR A 1 135 ? 39.144  -46.596 86.734  1.00 60.25  ?  144 THR A C    1 
ATOM   2133  O O    . THR A 1 135 ? 40.288  -46.223 86.474  1.00 68.79  ?  144 THR A O    1 
ATOM   2134  C CB   . THR A 1 135 ? 38.357  -48.744 85.741  1.00 81.30  ?  144 THR A CB   1 
ATOM   2135  O OG1  . THR A 1 135 ? 39.720  -49.132 85.862  1.00 97.49  ?  144 THR A OG1  1 
ATOM   2136  C CG2  . THR A 1 135 ? 37.862  -49.367 84.458  1.00 85.10  ?  144 THR A CG2  1 
ATOM   2137  H H    . THR A 1 135 ? 39.493  -47.011 84.146  1.00 68.23  ?  144 THR A H    1 
ATOM   2138  H HA   . THR A 1 135 ? 37.348  -46.938 85.819  1.00 79.97  ?  144 THR A HA   1 
ATOM   2139  H HB   . THR A 1 135 ? 37.839  -49.082 86.488  1.00 97.56  ?  144 THR A HB   1 
ATOM   2140  H HG1  . THR A 1 135 ? 39.778  -49.969 85.902  1.00 116.99 ?  144 THR A HG1  1 
ATOM   2141  H HG21 . THR A 1 135 ? 37.923  -50.333 84.514  1.00 102.12 ?  144 THR A HG21 1 
ATOM   2142  H HG22 . THR A 1 135 ? 36.937  -49.118 84.304  1.00 102.12 ?  144 THR A HG22 1 
ATOM   2143  H HG23 . THR A 1 135 ? 38.399  -49.060 83.711  1.00 102.12 ?  144 THR A HG23 1 
ATOM   2144  N N    . TYR A 1 136 ? 38.624  -46.590 87.959  1.00 69.34  ?  145 TYR A N    1 
ATOM   2145  C CA   . TYR A 1 136 ? 39.328  -45.971 89.078  1.00 77.20  ?  145 TYR A CA   1 
ATOM   2146  C C    . TYR A 1 136 ? 40.718  -46.559 89.264  1.00 73.41  ?  145 TYR A C    1 
ATOM   2147  O O    . TYR A 1 136 ? 41.678  -45.834 89.515  1.00 62.67  ?  145 TYR A O    1 
ATOM   2148  C CB   . TYR A 1 136 ? 38.505  -46.113 90.356  1.00 74.69  ?  145 TYR A CB   1 
ATOM   2149  C CG   . TYR A 1 136 ? 39.070  -45.399 91.590  1.00 79.27  ?  145 TYR A CG   1 
ATOM   2150  C CD1  . TYR A 1 136 ? 40.032  -46.026 92.396  1.00 72.87  ?  145 TYR A CD1  1 
ATOM   2151  C CD2  . TYR A 1 136 ? 38.612  -44.104 91.969  1.00 74.83  ?  145 TYR A CD2  1 
ATOM   2152  C CE1  . TYR A 1 136 ? 40.540  -45.401 93.546  1.00 74.91  ?  145 TYR A CE1  1 
ATOM   2153  C CE2  . TYR A 1 136 ? 39.102  -43.455 93.121  1.00 53.71  ?  145 TYR A CE2  1 
ATOM   2154  C CZ   . TYR A 1 136 ? 40.053  -44.124 93.912  1.00 73.36  ?  145 TYR A CZ   1 
ATOM   2155  O OH   . TYR A 1 136 ? 40.552  -43.544 95.048  1.00 79.93  ?  145 TYR A OH   1 
ATOM   2156  H H    . TYR A 1 136 ? 37.866  -46.938 88.168  1.00 83.21  ?  145 TYR A H    1 
ATOM   2157  H HA   . TYR A 1 136 ? 39.429  -45.024 88.896  1.00 92.64  ?  145 TYR A HA   1 
ATOM   2158  H HB2  . TYR A 1 136 ? 37.619  -45.753 90.192  1.00 89.63  ?  145 TYR A HB2  1 
ATOM   2159  H HB3  . TYR A 1 136 ? 38.435  -47.056 90.572  1.00 89.63  ?  145 TYR A HB3  1 
ATOM   2160  H HD1  . TYR A 1 136 ? 40.336  -46.875 92.167  1.00 87.45  ?  145 TYR A HD1  1 
ATOM   2161  H HD2  . TYR A 1 136 ? 37.967  -43.681 91.450  1.00 89.79  ?  145 TYR A HD2  1 
ATOM   2162  H HE1  . TYR A 1 136 ? 41.169  -45.833 94.077  1.00 89.90  ?  145 TYR A HE1  1 
ATOM   2163  H HE2  . TYR A 1 136 ? 38.788  -42.614 93.363  1.00 64.46  ?  145 TYR A HE2  1 
ATOM   2164  H HH   . TYR A 1 136 ? 40.195  -42.793 95.168  1.00 95.92  ?  145 TYR A HH   1 
ATOM   2165  N N    . GLU A 1 137 ? 40.845  -47.870 89.169  1.00 90.27  ?  146 GLU A N    1 
ATOM   2166  C CA   . GLU A 1 137 ? 42.151  -48.465 89.400  1.00 115.00 ?  146 GLU A CA   1 
ATOM   2167  C C    . GLU A 1 137 ? 43.162  -48.033 88.354  1.00 98.35  ?  146 GLU A C    1 
ATOM   2168  O O    . GLU A 1 137 ? 44.364  -48.236 88.559  1.00 102.83 ?  146 GLU A O    1 
ATOM   2169  C CB   . GLU A 1 137 ? 42.054  -49.977 89.426  1.00 124.67 ?  146 GLU A CB   1 
ATOM   2170  C CG   . GLU A 1 137 ? 41.498  -50.548 90.721  1.00 133.30 ?  146 GLU A CG   1 
ATOM   2171  C CD   . GLU A 1 137 ? 40.044  -50.220 90.920  1.00 143.92 ?  146 GLU A CD   1 
ATOM   2172  O OE1  . GLU A 1 137 ? 39.617  -50.073 92.091  1.00 160.67 ?  146 GLU A OE1  1 
ATOM   2173  O OE2  . GLU A 1 137 ? 39.329  -50.135 89.894  1.00 128.76 -1 146 GLU A OE2  1 
ATOM   2174  H H    . GLU A 1 137 ? 40.215  -48.423 88.978  1.00 108.33 ?  146 GLU A H    1 
ATOM   2175  H HA   . GLU A 1 137 ? 42.478  -48.174 90.266  1.00 138.00 ?  146 GLU A HA   1 
ATOM   2176  H HB2  . GLU A 1 137 ? 41.472  -50.263 88.704  1.00 149.60 ?  146 GLU A HB2  1 
ATOM   2177  H HB3  . GLU A 1 137 ? 42.941  -50.348 89.297  1.00 149.60 ?  146 GLU A HB3  1 
ATOM   2178  H HG2  . GLU A 1 137 ? 41.589  -51.513 90.705  1.00 159.96 ?  146 GLU A HG2  1 
ATOM   2179  H HG3  . GLU A 1 137 ? 41.995  -50.179 91.468  1.00 159.96 ?  146 GLU A HG3  1 
ATOM   2180  N N    . ASN A 1 138 ? 42.699  -47.486 87.222  1.00 67.29  ?  147 ASN A N    1 
ATOM   2181  C CA   . ASN A 1 138 ? 43.586  -47.021 86.164  1.00 96.40  ?  147 ASN A CA   1 
ATOM   2182  C C    . ASN A 1 138 ? 43.823  -45.509 86.247  1.00 97.47  ?  147 ASN A C    1 
ATOM   2183  O O    . ASN A 1 138 ? 44.409  -44.915 85.331  1.00 83.39  ?  147 ASN A O    1 
ATOM   2184  C CB   . ASN A 1 138 ? 43.027  -47.428 84.785  1.00 94.30  ?  147 ASN A CB   1 
ATOM   2185  C CG   . ASN A 1 138 ? 44.071  -47.303 83.644  1.00 105.40 ?  147 ASN A CG   1 
ATOM   2186  O OD1  . ASN A 1 138 ? 45.245  -47.650 83.823  1.00 121.28 ?  147 ASN A OD1  1 
ATOM   2187  N ND2  . ASN A 1 138 ? 43.630  -46.878 82.465  1.00 113.71 ?  147 ASN A ND2  1 
ATOM   2188  H H    . ASN A 1 138 ? 41.864  -47.374 87.048  1.00 80.75  ?  147 ASN A H    1 
ATOM   2189  H HA   . ASN A 1 138 ? 44.446  -47.456 86.271  1.00 115.68 ?  147 ASN A HA   1 
ATOM   2190  H HB2  . ASN A 1 138 ? 42.737  -48.353 84.824  1.00 113.16 ?  147 ASN A HB2  1 
ATOM   2191  H HB3  . ASN A 1 138 ? 42.276  -46.855 84.568  1.00 113.16 ?  147 ASN A HB3  1 
ATOM   2192  H HD21 . ASN A 1 138 ? 44.176  -46.795 81.806  1.00 136.45 ?  147 ASN A HD21 1 
ATOM   2193  H HD22 . ASN A 1 138 ? 42.798  -46.687 82.361  1.00 136.45 ?  147 ASN A HD22 1 
ATOM   2194  N N    . MET A 1 139 ? 43.370  -44.869 87.314  1.00 90.99  ?  148 MET A N    1 
ATOM   2195  C CA   . MET A 1 139 ? 43.353  -43.420 87.361  1.00 83.36  ?  148 MET A CA   1 
ATOM   2196  C C    . MET A 1 139 ? 44.097  -42.930 88.605  1.00 67.56  ?  148 MET A C    1 
ATOM   2197  O O    . MET A 1 139 ? 44.200  -43.622 89.614  1.00 71.84  ?  148 MET A O    1 
ATOM   2198  C CB   . MET A 1 139 ? 41.848  -42.935 87.305  1.00 86.97  ?  148 MET A CB   1 
ATOM   2199  C CG   . MET A 1 139 ? 41.168  -43.155 85.943  1.00 48.68  ?  148 MET A CG   1 
ATOM   2200  S SD   . MET A 1 139 ? 39.438  -42.926 85.869  1.00 93.00  ?  148 MET A SD   1 
ATOM   2201  C CE   . MET A 1 139 ? 39.424  -41.133 85.859  1.00 81.01  ?  148 MET A CE   1 
ATOM   2202  H H    . MET A 1 139 ? 43.068  -45.251 88.022  1.00 109.18 ?  148 MET A H    1 
ATOM   2203  H HA   . MET A 1 139 ? 43.804  -43.077 86.574  1.00 100.03 ?  148 MET A HA   1 
ATOM   2204  H HB2  . MET A 1 139 ? 41.339  -43.422 87.971  1.00 104.37 ?  148 MET A HB2  1 
ATOM   2205  H HB3  . MET A 1 139 ? 41.820  -41.985 87.499  1.00 104.37 ?  148 MET A HB3  1 
ATOM   2206  H HG2  . MET A 1 139 ? 41.564  -42.540 85.306  1.00 58.42  ?  148 MET A HG2  1 
ATOM   2207  H HG3  . MET A 1 139 ? 41.347  -44.065 85.660  1.00 58.42  ?  148 MET A HG3  1 
ATOM   2208  H HE1  . MET A 1 139 ? 38.504  -40.825 85.819  1.00 97.22  ?  148 MET A HE1  1 
ATOM   2209  H HE2  . MET A 1 139 ? 39.846  -40.809 86.670  1.00 97.22  ?  148 MET A HE2  1 
ATOM   2210  H HE3  . MET A 1 139 ? 39.913  -40.817 85.083  1.00 97.22  ?  148 MET A HE3  1 
ATOM   2211  N N    . ASP A 1 140 ? 44.612  -41.713 88.511  1.00 49.40  ?  149 ASP A N    1 
ATOM   2212  C CA   . ASP A 1 140 ? 45.187  -40.974 89.616  1.00 86.01  ?  149 ASP A CA   1 
ATOM   2213  C C    . ASP A 1 140 ? 44.856  -39.502 89.408  1.00 77.26  ?  149 ASP A C    1 
ATOM   2214  O O    . ASP A 1 140 ? 44.483  -39.093 88.306  1.00 63.70  ?  149 ASP A O    1 
ATOM   2215  C CB   . ASP A 1 140 ? 46.684  -41.178 89.671  1.00 107.92 ?  149 ASP A CB   1 
ATOM   2216  C CG   . ASP A 1 140 ? 47.151  -41.483 91.040  1.00 125.51 ?  149 ASP A CG   1 
ATOM   2217  O OD1  . ASP A 1 140 ? 46.615  -40.855 91.980  1.00 143.95 ?  149 ASP A OD1  1 
ATOM   2218  O OD2  . ASP A 1 140 ? 48.012  -42.383 91.171  1.00 129.92 -1 149 ASP A OD2  1 
ATOM   2219  H H    . ASP A 1 140 ? 44.639  -41.274 87.772  1.00 59.28  ?  149 ASP A H    1 
ATOM   2220  H HA   . ASP A 1 140 ? 44.797  -41.271 90.453  1.00 103.21 ?  149 ASP A HA   1 
ATOM   2221  H HB2  . ASP A 1 140 ? 46.926  -41.921 89.096  1.00 129.50 ?  149 ASP A HB2  1 
ATOM   2222  H HB3  . ASP A 1 140 ? 47.127  -40.367 89.374  1.00 129.50 ?  149 ASP A HB3  1 
ATOM   2223  N N    . VAL A 1 141 ? 44.909  -38.722 90.496  1.00 82.97  ?  150 VAL A N    1 
ATOM   2224  C CA   . VAL A 1 141 ? 44.838  -37.252 90.413  1.00 65.34  ?  150 VAL A CA   1 
ATOM   2225  C C    . VAL A 1 141 ? 46.236  -36.711 90.315  1.00 64.93  ?  150 VAL A C    1 
ATOM   2226  O O    . VAL A 1 141 ? 47.203  -37.396 90.651  1.00 105.79 ?  150 VAL A O    1 
ATOM   2227  C CB   . VAL A 1 141 ? 44.191  -36.548 91.617  1.00 58.72  ?  150 VAL A CB   1 
ATOM   2228  C CG1  . VAL A 1 141 ? 42.799  -37.063 91.829  1.00 69.15  ?  150 VAL A CG1  1 
ATOM   2229  C CG2  . VAL A 1 141 ? 45.031  -36.747 92.882  1.00 47.05  ?  150 VAL A CG2  1 
ATOM   2230  H H    . VAL A 1 141 ? 44.985  -39.020 91.299  1.00 99.57  ?  150 VAL A H    1 
ATOM   2231  H HA   . VAL A 1 141 ? 44.353  -36.997 89.612  1.00 78.41  ?  150 VAL A HA   1 
ATOM   2232  H HB   . VAL A 1 141 ? 44.137  -35.597 91.438  1.00 70.47  ?  150 VAL A HB   1 
ATOM   2233  H HG11 . VAL A 1 141 ? 42.408  -36.609 92.592  1.00 82.98  ?  150 VAL A HG11 1 
ATOM   2234  H HG12 . VAL A 1 141 ? 42.273  -36.887 91.033  1.00 82.98  ?  150 VAL A HG12 1 
ATOM   2235  H HG13 . VAL A 1 141 ? 42.837  -38.017 91.996  1.00 82.98  ?  150 VAL A HG13 1 
ATOM   2236  H HG21 . VAL A 1 141 ? 44.599  -36.294 93.622  1.00 56.46  ?  150 VAL A HG21 1 
ATOM   2237  H HG22 . VAL A 1 141 ? 45.099  -37.697 93.069  1.00 56.46  ?  150 VAL A HG22 1 
ATOM   2238  H HG23 . VAL A 1 141 ? 45.915  -36.375 92.735  1.00 56.46  ?  150 VAL A HG23 1 
ATOM   2239  N N    . LEU A 1 142 ? 46.345  -35.448 89.966  1.00 84.73  ?  151 LEU A N    1 
ATOM   2240  C CA   . LEU A 1 142 ? 47.657  -34.841 89.937  1.00 75.27  ?  151 LEU A CA   1 
ATOM   2241  C C    . LEU A 1 142 ? 48.053  -34.150 91.255  1.00 79.91  ?  151 LEU A C    1 
ATOM   2242  O O    . LEU A 1 142 ? 49.252  -34.067 91.546  1.00 128.14 ?  151 LEU A O    1 
ATOM   2243  C CB   . LEU A 1 142 ? 47.700  -33.865 88.787  1.00 75.72  ?  151 LEU A CB   1 
ATOM   2244  C CG   . LEU A 1 142 ? 47.327  -34.357 87.407  1.00 55.64  ?  151 LEU A CG   1 
ATOM   2245  C CD1  . LEU A 1 142 ? 47.325  -33.090 86.452  1.00 47.64  ?  151 LEU A CD1  1 
ATOM   2246  C CD2  . LEU A 1 142 ? 48.251  -35.371 86.877  1.00 58.66  ?  151 LEU A CD2  1 
ATOM   2247  H H    . LEU A 1 142 ? 45.695  -34.930 89.746  1.00 101.67 ?  151 LEU A H    1 
ATOM   2248  H HA   . LEU A 1 142 ? 48.314  -35.533 89.761  1.00 90.32  ?  151 LEU A HA   1 
ATOM   2249  H HB2  . LEU A 1 142 ? 47.098  -33.134 88.996  1.00 90.86  ?  151 LEU A HB2  1 
ATOM   2250  H HB3  . LEU A 1 142 ? 48.605  -33.520 88.726  1.00 90.86  ?  151 LEU A HB3  1 
ATOM   2251  H HG   . LEU A 1 142 ? 46.433  -34.731 87.426  1.00 66.76  ?  151 LEU A HG   1 
ATOM   2252  H HD11 . LEU A 1 142 ? 47.089  -33.372 85.555  1.00 57.17  ?  151 LEU A HD11 1 
ATOM   2253  H HD12 . LEU A 1 142 ? 46.676  -32.449 86.780  1.00 57.17  ?  151 LEU A HD12 1 
ATOM   2254  H HD13 . LEU A 1 142 ? 48.211  -32.694 86.452  1.00 57.17  ?  151 LEU A HD13 1 
ATOM   2255  H HD21 . LEU A 1 142 ? 47.952  -35.639 85.994  1.00 70.39  ?  151 LEU A HD21 1 
ATOM   2256  H HD22 . LEU A 1 142 ? 49.141  -34.989 86.823  1.00 70.39  ?  151 LEU A HD22 1 
ATOM   2257  H HD23 . LEU A 1 142 ? 48.254  -36.137 87.472  1.00 70.39  ?  151 LEU A HD23 1 
ATOM   2258  N N    . PHE A 1 143 ? 47.102  -33.646 92.069  1.00 65.63  ?  152 PHE A N    1 
ATOM   2259  C CA   . PHE A 1 143 ? 47.493  -32.813 93.201  1.00 66.48  ?  152 PHE A CA   1 
ATOM   2260  C C    . PHE A 1 143 ? 46.632  -33.062 94.428  1.00 60.10  ?  152 PHE A C    1 
ATOM   2261  O O    . PHE A 1 143 ? 45.462  -33.417 94.312  1.00 73.61  ?  152 PHE A O    1 
ATOM   2262  C CB   . PHE A 1 143 ? 47.432  -31.335 92.828  1.00 51.98  ?  152 PHE A CB   1 
ATOM   2263  C CG   . PHE A 1 143 ? 48.309  -30.991 91.654  1.00 54.70  ?  152 PHE A CG   1 
ATOM   2264  C CD1  . PHE A 1 143 ? 49.693  -30.925 91.788  1.00 73.64  ?  152 PHE A CD1  1 
ATOM   2265  C CD2  . PHE A 1 143 ? 47.731  -30.749 90.397  1.00 48.91  ?  152 PHE A CD2  1 
ATOM   2266  C CE1  . PHE A 1 143 ? 50.460  -30.619 90.703  1.00 53.26  ?  152 PHE A CE1  1 
ATOM   2267  C CE2  . PHE A 1 143 ? 48.445  -30.428 89.318  1.00 51.44  ?  152 PHE A CE2  1 
ATOM   2268  C CZ   . PHE A 1 143 ? 49.848  -30.362 89.448  1.00 42.97  ?  152 PHE A CZ   1 
ATOM   2269  H H    . PHE A 1 143 ? 46.256  -33.771 91.983  1.00 78.76  ?  152 PHE A H    1 
ATOM   2270  H HA   . PHE A 1 143 ? 48.411  -33.021 93.438  1.00 79.77  ?  152 PHE A HA   1 
ATOM   2271  H HB2  . PHE A 1 143 ? 46.519  -31.105 92.597  1.00 62.38  ?  152 PHE A HB2  1 
ATOM   2272  H HB3  . PHE A 1 143 ? 47.726  -30.805 93.586  1.00 62.38  ?  152 PHE A HB3  1 
ATOM   2273  H HD1  . PHE A 1 143 ? 50.092  -31.090 92.612  1.00 88.36  ?  152 PHE A HD1  1 
ATOM   2274  H HD2  . PHE A 1 143 ? 46.805  -30.790 90.319  1.00 58.70  ?  152 PHE A HD2  1 
ATOM   2275  H HE1  . PHE A 1 143 ? 51.384  -30.568 90.787  1.00 63.91  ?  152 PHE A HE1  1 
ATOM   2276  H HE2  . PHE A 1 143 ? 48.032  -30.272 88.500  1.00 61.73  ?  152 PHE A HE2  1 
ATOM   2277  H HZ   . PHE A 1 143 ? 50.373  -30.151 88.710  1.00 51.56  ?  152 PHE A HZ   1 
ATOM   2278  N N    . SER A 1 144 ? 47.203  -32.774 95.603  1.00 78.41  ?  153 SER A N    1 
ATOM   2279  C CA   . SER A 1 144 ? 46.548  -33.020 96.880  1.00 61.02  ?  153 SER A CA   1 
ATOM   2280  C C    . SER A 1 144 ? 46.971  -31.973 97.912  1.00 58.50  ?  153 SER A C    1 
ATOM   2281  O O    . SER A 1 144 ? 47.893  -31.175 97.675  1.00 59.09  ?  153 SER A O    1 
ATOM   2282  C CB   . SER A 1 144 ? 46.883  -34.413 97.381  1.00 73.16  ?  153 SER A CB   1 
ATOM   2283  O OG   . SER A 1 144 ? 46.452  -35.349 96.431  1.00 70.98  ?  153 SER A OG   1 
ATOM   2284  H H    . SER A 1 144 ? 47.987  -32.429 95.681  1.00 94.10  ?  153 SER A H    1 
ATOM   2285  H HA   . SER A 1 144 ? 45.586  -32.961 96.763  1.00 73.23  ?  153 SER A HA   1 
ATOM   2286  H HB2  . SER A 1 144 ? 47.843  -34.492 97.497  1.00 87.80  ?  153 SER A HB2  1 
ATOM   2287  H HB3  . SER A 1 144 ? 46.426  -34.573 98.221  1.00 87.80  ?  153 SER A HB3  1 
ATOM   2288  H HG   . SER A 1 144 ? 45.622  -35.282 96.318  1.00 85.18  ?  153 SER A HG   1 
ATOM   2289  N N    . PHE A 1 145 ? 46.270  -31.962 99.069  1.00 46.00  ?  154 PHE A N    1 
ATOM   2290  C CA   . PHE A 1 145 ? 46.540  -30.992 100.133 1.00 57.74  ?  154 PHE A CA   1 
ATOM   2291  C C    . PHE A 1 145 ? 47.210  -31.555 101.376 1.00 68.50  ?  154 PHE A C    1 
ATOM   2292  O O    . PHE A 1 145 ? 48.148  -30.939 101.901 1.00 89.95  ?  154 PHE A O    1 
ATOM   2293  C CB   . PHE A 1 145 ? 45.243  -30.298 100.550 1.00 71.28  ?  154 PHE A CB   1 
ATOM   2294  C CG   . PHE A 1 145 ? 44.615  -29.526 99.451  1.00 73.48  ?  154 PHE A CG   1 
ATOM   2295  C CD1  . PHE A 1 145 ? 45.144  -28.315 99.014  1.00 80.06  ?  154 PHE A CD1  1 
ATOM   2296  C CD2  . PHE A 1 145 ? 43.484  -29.986 98.858  1.00 61.27  ?  154 PHE A CD2  1 
ATOM   2297  C CE1  . PHE A 1 145 ? 44.529  -27.582 97.959  1.00 56.05  ?  154 PHE A CE1  1 
ATOM   2298  C CE2  . PHE A 1 145 ? 42.869  -29.268 97.827  1.00 69.62  ?  154 PHE A CE2  1 
ATOM   2299  C CZ   . PHE A 1 145 ? 43.408  -28.075 97.379  1.00 64.66  ?  154 PHE A CZ   1 
ATOM   2300  H H    . PHE A 1 145 ? 45.634  -32.511 99.253  1.00 55.20  ?  154 PHE A H    1 
ATOM   2301  H HA   . PHE A 1 145 ? 47.129  -30.309 99.776  1.00 69.28  ?  154 PHE A HA   1 
ATOM   2302  H HB2  . PHE A 1 145 ? 44.608  -30.969 100.845 1.00 85.53  ?  154 PHE A HB2  1 
ATOM   2303  H HB3  . PHE A 1 145 ? 45.435  -29.682 101.275 1.00 85.53  ?  154 PHE A HB3  1 
ATOM   2304  H HD1  . PHE A 1 145 ? 45.918  -27.985 99.410  1.00 96.07  ?  154 PHE A HD1  1 
ATOM   2305  H HD2  . PHE A 1 145 ? 43.113  -30.791 99.140  1.00 73.52  ?  154 PHE A HD2  1 
ATOM   2306  H HE1  . PHE A 1 145 ? 44.894  -26.777 97.670  1.00 67.26  ?  154 PHE A HE1  1 
ATOM   2307  H HE2  . PHE A 1 145 ? 42.100  -29.604 97.427  1.00 83.54  ?  154 PHE A HE2  1 
ATOM   2308  H HZ   . PHE A 1 145 ? 42.992  -27.603 96.694  1.00 77.60  ?  154 PHE A HZ   1 
ATOM   2309  N N    . ARG A 1 146 ? 46.687  -32.636 101.940 1.00 63.31  ?  155 ARG A N    1 
ATOM   2310  C CA   . ARG A 1 146 ? 47.344  -33.276 103.078 1.00 68.70  ?  155 ARG A CA   1 
ATOM   2311  C C    . ARG A 1 146 ? 47.280  -34.786 102.866 1.00 58.98  ?  155 ARG A C    1 
ATOM   2312  O O    . ARG A 1 146 ? 46.504  -35.284 102.054 1.00 113.84 ?  155 ARG A O    1 
ATOM   2313  C CB   . ARG A 1 146 ? 46.726  -32.890 104.433 1.00 62.13  ?  155 ARG A CB   1 
ATOM   2314  C CG   . ARG A 1 146 ? 46.687  -31.386 104.736 1.00 51.63  ?  155 ARG A CG   1 
ATOM   2315  C CD   . ARG A 1 146 ? 48.021  -30.741 105.023 1.00 65.12  ?  155 ARG A CD   1 
ATOM   2316  N NE   . ARG A 1 146 ? 48.601  -31.038 106.358 1.00 53.03  ?  155 ARG A NE   1 
ATOM   2317  C CZ   . ARG A 1 146 ? 48.104  -30.606 107.511 1.00 66.94  ?  155 ARG A CZ   1 
ATOM   2318  N NH1  . ARG A 1 146 ? 46.967  -29.930 107.523 1.00 66.43  1  155 ARG A NH1  1 
ATOM   2319  N NH2  . ARG A 1 146 ? 48.716  -30.883 108.651 1.00 84.70  1  155 ARG A NH2  1 
ATOM   2320  H H    . ARG A 1 146 ? 45.959  -33.017 101.687 1.00 75.97  ?  155 ARG A H    1 
ATOM   2321  H HA   . ARG A 1 146 ? 48.278  -33.015 103.090 1.00 82.44  ?  155 ARG A HA   1 
ATOM   2322  H HB2  . ARG A 1 146 ? 45.813  -33.215 104.457 1.00 74.56  ?  155 ARG A HB2  1 
ATOM   2323  H HB3  . ARG A 1 146 ? 47.240  -33.315 105.137 1.00 74.56  ?  155 ARG A HB3  1 
ATOM   2324  H HG2  . ARG A 1 146 ? 46.302  -30.930 103.972 1.00 61.96  ?  155 ARG A HG2  1 
ATOM   2325  H HG3  . ARG A 1 146 ? 46.124  -31.245 105.513 1.00 61.96  ?  155 ARG A HG3  1 
ATOM   2326  H HD2  . ARG A 1 146 ? 48.657  -31.043 104.356 1.00 78.14  ?  155 ARG A HD2  1 
ATOM   2327  H HD3  . ARG A 1 146 ? 47.916  -29.779 104.959 1.00 78.14  ?  155 ARG A HD3  1 
ATOM   2328  H HE   . ARG A 1 146 ? 49.310  -31.524 106.385 1.00 63.64  ?  155 ARG A HE   1 
ATOM   2329  H HH11 . ARG A 1 146 ? 46.572  -29.739 106.784 1.00 79.71  ?  155 ARG A HH11 1 
ATOM   2330  H HH12 . ARG A 1 146 ? 46.636  -29.660 108.270 1.00 79.71  ?  155 ARG A HH12 1 
ATOM   2331  H HH21 . ARG A 1 146 ? 49.445  -31.339 108.648 1.00 101.64 ?  155 ARG A HH21 1 
ATOM   2332  H HH22 . ARG A 1 146 ? 48.372  -30.626 109.396 1.00 101.64 ?  155 ARG A HH22 1 
ATOM   2333  N N    . ASP A 1 147 ? 48.111  -35.508 103.600 1.00 64.58  ?  156 ASP A N    1 
ATOM   2334  C CA   . ASP A 1 147 ? 48.117  -36.960 103.520 1.00 69.53  ?  156 ASP A CA   1 
ATOM   2335  C C    . ASP A 1 147 ? 46.810  -37.503 104.070 1.00 108.36 ?  156 ASP A C    1 
ATOM   2336  O O    . ASP A 1 147 ? 46.432  -37.216 105.205 1.00 89.01  ?  156 ASP A O    1 
ATOM   2337  C CB   . ASP A 1 147 ? 49.309  -37.550 104.298 1.00 98.75  ?  156 ASP A CB   1 
ATOM   2338  C CG   . ASP A 1 147 ? 50.651  -37.159 103.689 1.00 114.08 ?  156 ASP A CG   1 
ATOM   2339  O OD1  . ASP A 1 147 ? 50.753  -37.187 102.437 1.00 95.37  ?  156 ASP A OD1  1 
ATOM   2340  O OD2  . ASP A 1 147 ? 51.602  -36.825 104.446 1.00 140.88 -1 156 ASP A OD2  1 
ATOM   2341  H H    . ASP A 1 147 ? 48.682  -35.182 104.154 1.00 77.49  ?  156 ASP A H    1 
ATOM   2342  H HA   . ASP A 1 147 ? 48.194  -37.230 102.591 1.00 83.43  ?  156 ASP A HA   1 
ATOM   2343  H HB2  . ASP A 1 147 ? 49.286  -37.222 105.211 1.00 118.50 ?  156 ASP A HB2  1 
ATOM   2344  H HB3  . ASP A 1 147 ? 49.245  -38.518 104.290 1.00 118.50 ?  156 ASP A HB3  1 
ATOM   2345  N N    . GLY A 1 148 ? 46.124  -38.314 103.284 1.00 144.76 ?  157 GLY A N    1 
ATOM   2346  C CA   . GLY A 1 148 ? 44.881  -38.847 103.793 1.00 107.29 ?  157 GLY A CA   1 
ATOM   2347  C C    . GLY A 1 148 ? 43.802  -37.802 103.898 1.00 72.89  ?  157 GLY A C    1 
ATOM   2348  O O    . GLY A 1 148 ? 42.998  -37.819 104.819 1.00 75.37  ?  157 GLY A O    1 
ATOM   2349  H H    . GLY A 1 148 ? 46.344  -38.560 102.490 1.00 173.71 ?  157 GLY A H    1 
ATOM   2350  H HA2  . GLY A 1 148 ? 44.568  -39.553 103.205 1.00 128.75 ?  157 GLY A HA2  1 
ATOM   2351  H HA3  . GLY A 1 148 ? 45.028  -39.225 104.674 1.00 128.75 ?  157 GLY A HA3  1 
ATOM   2352  N N    . ASP A 1 149 ? 43.828  -36.832 103.025 1.00 84.05  ?  158 ASP A N    1 
ATOM   2353  C CA   . ASP A 1 149 ? 42.681  -35.974 102.853 1.00 84.29  ?  158 ASP A CA   1 
ATOM   2354  C C    . ASP A 1 149 ? 41.634  -36.634 101.972 1.00 95.13  ?  158 ASP A C    1 
ATOM   2355  O O    . ASP A 1 149 ? 40.655  -35.980 101.612 1.00 69.21  ?  158 ASP A O    1 
ATOM   2356  C CB   . ASP A 1 149 ? 43.137  -34.644 102.240 1.00 82.18  ?  158 ASP A CB   1 
ATOM   2357  C CG   . ASP A 1 149 ? 43.982  -34.848 100.968 1.00 78.69  ?  158 ASP A CG   1 
ATOM   2358  O OD1  . ASP A 1 149 ? 44.476  -35.964 100.741 1.00 106.54 ?  158 ASP A OD1  1 
ATOM   2359  O OD2  . ASP A 1 149 ? 44.115  -33.925 100.162 1.00 67.72  -1 158 ASP A OD2  1 
ATOM   2360  H H    . ASP A 1 149 ? 44.496  -36.643 102.518 1.00 100.86 ?  158 ASP A H    1 
ATOM   2361  H HA   . ASP A 1 149 ? 42.282  -35.792 103.718 1.00 101.14 ?  158 ASP A HA   1 
ATOM   2362  H HB2  . ASP A 1 149 ? 42.356  -34.120 102.003 1.00 98.61  ?  158 ASP A HB2  1 
ATOM   2363  H HB3  . ASP A 1 149 ? 43.677  -34.165 102.888 1.00 98.61  ?  158 ASP A HB3  1 
ATOM   2364  N N    . CYS A 1 150 ? 41.883  -37.861 101.517 1.00 131.91 ?  159 CYS A N    1 
ATOM   2365  C CA   . CYS A 1 150 ? 40.943  -38.592 100.693 1.00 193.53 ?  159 CYS A CA   1 
ATOM   2366  C C    . CYS A 1 150 ? 40.654  -37.830 99.429  1.00 127.11 ?  159 CYS A C    1 
ATOM   2367  O O    . CYS A 1 150 ? 39.632  -38.042 98.778  1.00 60.80  ?  159 CYS A O    1 
ATOM   2368  C CB   . CYS A 1 150 ? 39.662  -38.901 101.450 1.00 333.44 ?  159 CYS A CB   1 
ATOM   2369  S SG   . CYS A 1 150 ? 39.932  -40.204 102.660 1.00 359.38 ?  159 CYS A SG   1 
ATOM   2370  H H    . CYS A 1 150 ? 42.608  -38.295 101.679 1.00 158.29 ?  159 CYS A H    1 
ATOM   2371  H HA   . CYS A 1 150 ? 41.345  -39.437 100.440 1.00 232.24 ?  159 CYS A HA   1 
ATOM   2372  H HB2  . CYS A 1 150 ? 39.365  -38.106 101.918 1.00 400.13 ?  159 CYS A HB2  1 
ATOM   2373  H HB3  . CYS A 1 150 ? 38.983  -39.200 100.825 1.00 400.13 ?  159 CYS A HB3  1 
ATOM   2374  H HG   . CYS A 1 150 ? 38.903  -40.420 103.237 1.00 431.25 ?  159 CYS A HG   1 
ATOM   2375  N N    . SER A 1 151 ? 41.532  -36.896 99.086  1.00 72.90  ?  160 SER A N    1 
ATOM   2376  C CA   . SER A 1 151 ? 41.304  -36.117 97.885  1.00 48.75  ?  160 SER A CA   1 
ATOM   2377  C C    . SER A 1 151 ? 41.322  -36.968 96.617  1.00 49.50  ?  160 SER A C    1 
ATOM   2378  O O    . SER A 1 151 ? 40.611  -36.662 95.649  1.00 57.36  ?  160 SER A O    1 
ATOM   2379  C CB   . SER A 1 151 ? 42.312  -34.947 97.799  1.00 51.32  ?  160 SER A CB   1 
ATOM   2380  O OG   . SER A 1 151 ? 43.660  -35.283 97.759  1.00 62.97  ?  160 SER A OG   1 
ATOM   2381  H H    . SER A 1 151 ? 42.248  -36.699 99.520  1.00 87.48  ?  160 SER A H    1 
ATOM   2382  H HA   . SER A 1 151 ? 40.420  -35.724 97.948  1.00 58.51  ?  160 SER A HA   1 
ATOM   2383  H HB2  . SER A 1 151 ? 42.110  -34.441 96.997  1.00 61.59  ?  160 SER A HB2  1 
ATOM   2384  H HB3  . SER A 1 151 ? 42.172  -34.379 98.573  1.00 61.59  ?  160 SER A HB3  1 
ATOM   2385  H HG   . SER A 1 151 ? 43.871  -35.708 98.452  1.00 75.57  ?  160 SER A HG   1 
ATOM   2386  N N    . LYS A 1 152 ? 42.076  -38.036 96.587  1.00 47.84  ?  161 LYS A N    1 
ATOM   2387  C CA   . LYS A 1 152 ? 41.991  -38.902 95.432  1.00 63.21  ?  161 LYS A CA   1 
ATOM   2388  C C    . LYS A 1 152 ? 40.573  -39.409 95.263  1.00 70.80  ?  161 LYS A C    1 
ATOM   2389  O O    . LYS A 1 152 ? 40.035  -39.381 94.158  1.00 59.08  ?  161 LYS A O    1 
ATOM   2390  C CB   . LYS A 1 152 ? 42.986  -40.067 95.570  1.00 65.38  ?  161 LYS A CB   1 
ATOM   2391  C CG   . LYS A 1 152 ? 43.108  -40.881 94.286  1.00 77.56  ?  161 LYS A CG   1 
ATOM   2392  C CD   . LYS A 1 152 ? 44.069  -42.028 94.407  1.00 90.24  ?  161 LYS A CD   1 
ATOM   2393  C CE   . LYS A 1 152 ? 44.055  -42.935 93.198  1.00 84.18  ?  161 LYS A CE   1 
ATOM   2394  N NZ   . LYS A 1 152 ? 44.753  -44.207 93.454  1.00 81.75  1  161 LYS A NZ   1 
ATOM   2395  H H    . LYS A 1 152 ? 42.630  -38.282 97.197  1.00 57.41  ?  161 LYS A H    1 
ATOM   2396  H HA   . LYS A 1 152 ? 42.226  -38.397 94.639  1.00 75.86  ?  161 LYS A HA   1 
ATOM   2397  H HB2  . LYS A 1 152 ? 43.863  -39.711 95.786  1.00 78.45  ?  161 LYS A HB2  1 
ATOM   2398  H HB3  . LYS A 1 152 ? 42.685  -40.660 96.276  1.00 78.45  ?  161 LYS A HB3  1 
ATOM   2399  H HG2  . LYS A 1 152 ? 42.237  -41.242 94.059  1.00 93.07  ?  161 LYS A HG2  1 
ATOM   2400  H HG3  . LYS A 1 152 ? 43.422  -40.301 93.575  1.00 93.07  ?  161 LYS A HG3  1 
ATOM   2401  H HD2  . LYS A 1 152 ? 44.967  -41.678 94.509  1.00 108.29 ?  161 LYS A HD2  1 
ATOM   2402  H HD3  . LYS A 1 152 ? 43.830  -42.560 95.183  1.00 108.29 ?  161 LYS A HD3  1 
ATOM   2403  H HE2  . LYS A 1 152 ? 43.136  -43.137 92.962  1.00 101.02 ?  161 LYS A HE2  1 
ATOM   2404  H HE3  . LYS A 1 152 ? 44.500  -42.489 92.460  1.00 101.02 ?  161 LYS A HE3  1 
ATOM   2405  H HZ1  . LYS A 1 152 ? 44.729  -44.719 92.727  1.00 98.10  ?  161 LYS A HZ1  1 
ATOM   2406  H HZ2  . LYS A 1 152 ? 45.603  -44.049 93.669  1.00 98.10  ?  161 LYS A HZ2  1 
ATOM   2407  H HZ3  . LYS A 1 152 ? 44.361  -44.639 94.126  1.00 98.10  ?  161 LYS A HZ3  1 
ATOM   2408  N N    . GLY A 1 153 ? 39.928  -39.816 96.357  1.00 60.42  ?  162 GLY A N    1 
ATOM   2409  C CA   . GLY A 1 153 ? 38.606  -40.401 96.241  1.00 65.51  ?  162 GLY A CA   1 
ATOM   2410  C C    . GLY A 1 153 ? 37.571  -39.404 95.772  1.00 108.39 ?  162 GLY A C    1 
ATOM   2411  O O    . GLY A 1 153 ? 36.883  -39.613 94.767  1.00 78.21  ?  162 GLY A O    1 
ATOM   2412  H H    . GLY A 1 153 ? 40.232  -39.763 97.160  1.00 72.50  ?  162 GLY A H    1 
ATOM   2413  H HA2  . GLY A 1 153 ? 38.633  -41.136 95.609  1.00 78.61  ?  162 GLY A HA2  1 
ATOM   2414  H HA3  . GLY A 1 153 ? 38.329  -40.747 97.104  1.00 78.61  ?  162 GLY A HA3  1 
ATOM   2415  N N    . PHE A 1 154 ? 37.512  -38.265 96.442  1.00 86.12  ?  163 PHE A N    1 
ATOM   2416  C CA   . PHE A 1 154 ? 36.458  -37.297 96.181  1.00 80.67  ?  163 PHE A CA   1 
ATOM   2417  C C    . PHE A 1 154 ? 36.546  -36.748 94.769  1.00 74.95  ?  163 PHE A C    1 
ATOM   2418  O O    . PHE A 1 154 ? 35.514  -36.421 94.157  1.00 57.29  ?  163 PHE A O    1 
ATOM   2419  C CB   . PHE A 1 154 ? 36.575  -36.171 97.192  1.00 80.83  ?  163 PHE A CB   1 
ATOM   2420  C CG   . PHE A 1 154 ? 35.423  -35.230 97.226  1.00 77.17  ?  163 PHE A CG   1 
ATOM   2421  C CD1  . PHE A 1 154 ? 34.184  -35.647 97.623  1.00 106.07 ?  163 PHE A CD1  1 
ATOM   2422  C CD2  . PHE A 1 154 ? 35.602  -33.908 96.924  1.00 84.34  ?  163 PHE A CD2  1 
ATOM   2423  C CE1  . PHE A 1 154 ? 33.152  -34.778 97.683  1.00 110.88 ?  163 PHE A CE1  1 
ATOM   2424  C CE2  . PHE A 1 154 ? 34.582  -33.038 96.976  1.00 91.06  ?  163 PHE A CE2  1 
ATOM   2425  C CZ   . PHE A 1 154 ? 33.354  -33.470 97.364  1.00 99.32  ?  163 PHE A CZ   1 
ATOM   2426  H H    . PHE A 1 154 ? 38.069  -38.027 97.053  1.00 103.34 ?  163 PHE A H    1 
ATOM   2427  H HA   . PHE A 1 154 ? 35.593  -37.723 96.293  1.00 96.80  ?  163 PHE A HA   1 
ATOM   2428  H HB2  . PHE A 1 154 ? 36.661  -36.559 98.077  1.00 97.00  ?  163 PHE A HB2  1 
ATOM   2429  H HB3  . PHE A 1 154 ? 37.369  -35.653 96.986  1.00 97.00  ?  163 PHE A HB3  1 
ATOM   2430  H HD1  . PHE A 1 154 ? 34.047  -36.539 97.846  1.00 127.29 ?  163 PHE A HD1  1 
ATOM   2431  H HD2  . PHE A 1 154 ? 36.443  -33.609 96.663  1.00 101.21 ?  163 PHE A HD2  1 
ATOM   2432  H HE1  . PHE A 1 154 ? 32.309  -35.071 97.943  1.00 133.05 ?  163 PHE A HE1  1 
ATOM   2433  H HE2  . PHE A 1 154 ? 34.717  -32.144 96.757  1.00 109.28 ?  163 PHE A HE2  1 
ATOM   2434  H HZ   . PHE A 1 154 ? 32.643  -32.872 97.397  1.00 119.18 ?  163 PHE A HZ   1 
ATOM   2435  N N    . PHE A 1 155 ? 37.766  -36.574 94.251  1.00 72.70  ?  164 PHE A N    1 
ATOM   2436  C CA   . PHE A 1 155 ? 37.863  -36.031 92.902  1.00 63.43  ?  164 PHE A CA   1 
ATOM   2437  C C    . PHE A 1 155 ? 37.642  -37.097 91.847  1.00 72.32  ?  164 PHE A C    1 
ATOM   2438  O O    . PHE A 1 155 ? 36.984  -36.831 90.842  1.00 89.20  ?  164 PHE A O    1 
ATOM   2439  C CB   . PHE A 1 155 ? 39.204  -35.343 92.651  1.00 53.33  ?  164 PHE A CB   1 
ATOM   2440  C CG   . PHE A 1 155 ? 39.439  -34.130 93.472  1.00 71.06  ?  164 PHE A CG   1 
ATOM   2441  C CD1  . PHE A 1 155 ? 38.420  -33.457 94.055  1.00 50.04  ?  164 PHE A CD1  1 
ATOM   2442  C CD2  . PHE A 1 155 ? 40.728  -33.661 93.633  1.00 95.36  ?  164 PHE A CD2  1 
ATOM   2443  C CE1  . PHE A 1 155 ? 38.672  -32.388 94.830  1.00 55.13  ?  164 PHE A CE1  1 
ATOM   2444  C CE2  . PHE A 1 155 ? 41.003  -32.560 94.393  1.00 54.15  ?  164 PHE A CE2  1 
ATOM   2445  C CZ   . PHE A 1 155 ? 39.969  -31.917 94.995  1.00 50.95  ?  164 PHE A CZ   1 
ATOM   2446  H H    . PHE A 1 155 ? 38.513  -36.752 94.639  1.00 87.24  ?  164 PHE A H    1 
ATOM   2447  H HA   . PHE A 1 155 ? 37.169  -35.363 92.791  1.00 76.12  ?  164 PHE A HA   1 
ATOM   2448  H HB2  . PHE A 1 155 ? 39.916  -35.972 92.846  1.00 64.00  ?  164 PHE A HB2  1 
ATOM   2449  H HB3  . PHE A 1 155 ? 39.248  -35.080 91.719  1.00 64.00  ?  164 PHE A HB3  1 
ATOM   2450  H HD1  . PHE A 1 155 ? 37.549  -33.770 93.967  1.00 60.05  ?  164 PHE A HD1  1 
ATOM   2451  H HD2  . PHE A 1 155 ? 41.429  -34.119 93.229  1.00 114.43 ?  164 PHE A HD2  1 
ATOM   2452  H HE1  . PHE A 1 155 ? 37.966  -31.934 95.229  1.00 66.16  ?  164 PHE A HE1  1 
ATOM   2453  H HE2  . PHE A 1 155 ? 41.877  -32.261 94.499  1.00 64.99  ?  164 PHE A HE2  1 
ATOM   2454  H HZ   . PHE A 1 155 ? 40.128  -31.160 95.512  1.00 61.15  ?  164 PHE A HZ   1 
ATOM   2455  N N    . LEU A 1 156 ? 38.209  -38.287 92.001  1.00 56.25  ?  165 LEU A N    1 
ATOM   2456  C CA   . LEU A 1 156 ? 38.055  -39.204 90.892  1.00 59.78  ?  165 LEU A CA   1 
ATOM   2457  C C    . LEU A 1 156 ? 36.619  -39.694 90.763  1.00 60.05  ?  165 LEU A C    1 
ATOM   2458  O O    . LEU A 1 156 ? 36.097  -39.860 89.646  1.00 69.46  ?  165 LEU A O    1 
ATOM   2459  C CB   . LEU A 1 156 ? 38.983  -40.368 91.057  1.00 60.77  ?  165 LEU A CB   1 
ATOM   2460  C CG   . LEU A 1 156 ? 40.435  -40.131 90.784  1.00 64.13  ?  165 LEU A CG   1 
ATOM   2461  C CD1  . LEU A 1 156 ? 41.131  -41.453 91.048  1.00 72.04  ?  165 LEU A CD1  1 
ATOM   2462  C CD2  . LEU A 1 156 ? 40.642  -39.659 89.365  1.00 65.81  ?  165 LEU A CD2  1 
ATOM   2463  H H    . LEU A 1 156 ? 38.653  -38.569 92.682  1.00 67.49  ?  165 LEU A H    1 
ATOM   2464  H HA   . LEU A 1 156 ? 38.291  -38.747 90.070  1.00 71.74  ?  165 LEU A HA   1 
ATOM   2465  H HB2  . LEU A 1 156 ? 38.913  -40.681 91.973  1.00 72.93  ?  165 LEU A HB2  1 
ATOM   2466  H HB3  . LEU A 1 156 ? 38.691  -41.072 90.457  1.00 72.93  ?  165 LEU A HB3  1 
ATOM   2467  H HG   . LEU A 1 156 ? 40.783  -39.463 91.395  1.00 76.95  ?  165 LEU A HG   1 
ATOM   2468  H HD11 . LEU A 1 156 ? 42.081  -41.347 90.883  1.00 86.44  ?  165 LEU A HD11 1 
ATOM   2469  H HD12 . LEU A 1 156 ? 40.982  -41.709 91.971  1.00 86.44  ?  165 LEU A HD12 1 
ATOM   2470  H HD13 . LEU A 1 156 ? 40.764  -42.127 90.454  1.00 86.44  ?  165 LEU A HD13 1 
ATOM   2471  H HD21 . LEU A 1 156 ? 41.589  -39.514 89.216  1.00 78.97  ?  165 LEU A HD21 1 
ATOM   2472  H HD22 . LEU A 1 156 ? 40.311  -40.337 88.756  1.00 78.97  ?  165 LEU A HD22 1 
ATOM   2473  H HD23 . LEU A 1 156 ? 40.155  -38.830 89.235  1.00 78.97  ?  165 LEU A HD23 1 
ATOM   2474  N N    . VAL A 1 157 ? 35.970  -39.898 91.904  1.00 54.73  ?  166 VAL A N    1 
ATOM   2475  C CA   . VAL A 1 157 ? 34.603  -40.377 91.886  1.00 66.56  ?  166 VAL A CA   1 
ATOM   2476  C C    . VAL A 1 157 ? 33.716  -39.352 91.219  1.00 76.47  ?  166 VAL A C    1 
ATOM   2477  O O    . VAL A 1 157 ? 32.915  -39.699 90.333  1.00 78.13  ?  166 VAL A O    1 
ATOM   2478  C CB   . VAL A 1 157 ? 34.150  -40.674 93.313  1.00 62.38  ?  166 VAL A CB   1 
ATOM   2479  C CG1  . VAL A 1 157 ? 32.671  -40.928 93.319  1.00 67.84  ?  166 VAL A CG1  1 
ATOM   2480  C CG2  . VAL A 1 157 ? 34.905  -41.853 93.802  1.00 50.57  ?  166 VAL A CG2  1 
ATOM   2481  H H    . VAL A 1 157 ? 36.296  -39.769 92.689  1.00 65.68  ?  166 VAL A H    1 
ATOM   2482  H HA   . VAL A 1 157 ? 34.558  -41.199 91.374  1.00 79.87  ?  166 VAL A HA   1 
ATOM   2483  H HB   . VAL A 1 157 ? 34.343  -39.916 93.886  1.00 74.85  ?  166 VAL A HB   1 
ATOM   2484  H HG11 . VAL A 1 157 ? 32.387  -41.117 94.227  1.00 81.41  ?  166 VAL A HG11 1 
ATOM   2485  H HG12 . VAL A 1 157 ? 32.214  -40.140 92.987  1.00 81.41  ?  166 VAL A HG12 1 
ATOM   2486  H HG13 . VAL A 1 157 ? 32.479  -41.688 92.748  1.00 81.41  ?  166 VAL A HG13 1 
ATOM   2487  H HG21 . VAL A 1 157 ? 34.625  -42.052 94.709  1.00 60.68  ?  166 VAL A HG21 1 
ATOM   2488  H HG22 . VAL A 1 157 ? 34.718  -42.609 93.224  1.00 60.68  ?  166 VAL A HG22 1 
ATOM   2489  H HG23 . VAL A 1 157 ? 35.853  -41.649 93.785  1.00 60.68  ?  166 VAL A HG23 1 
ATOM   2490  N N    . SER A 1 158 ? 33.902  -38.066 91.592  1.00 64.91  ?  167 SER A N    1 
ATOM   2491  C CA   . SER A 1 158 ? 33.217  -36.948 90.946  1.00 54.62  ?  167 SER A CA   1 
ATOM   2492  C C    . SER A 1 158 ? 33.388  -37.069 89.456  1.00 41.25  ?  167 SER A C    1 
ATOM   2493  O O    . SER A 1 158 ? 32.440  -37.017 88.658  1.00 53.03  ?  167 SER A O    1 
ATOM   2494  C CB   . SER A 1 158 ? 33.864  -35.613 91.364  1.00 82.53  ?  167 SER A CB   1 
ATOM   2495  O OG   . SER A 1 158 ? 33.942  -35.414 92.773  1.00 52.00  ?  167 SER A OG   1 
ATOM   2496  H H    . SER A 1 158 ? 34.429  -37.825 92.227  1.00 77.89  ?  167 SER A H    1 
ATOM   2497  H HA   . SER A 1 158 ? 32.274  -36.943 91.170  1.00 65.54  ?  167 SER A HA   1 
ATOM   2498  H HB2  . SER A 1 158 ? 34.763  -35.584 91.002  1.00 99.03  ?  167 SER A HB2  1 
ATOM   2499  H HB3  . SER A 1 158 ? 33.342  -34.890 90.983  1.00 99.03  ?  167 SER A HB3  1 
ATOM   2500  H HG   . SER A 1 158 ? 34.400  -36.025 93.125  1.00 62.41  ?  167 SER A HG   1 
ATOM   2501  N N    . LEU A 1 159 ? 34.648  -37.184 89.079  1.00 43.96  ?  168 LEU A N    1 
ATOM   2502  C CA   . LEU A 1 159 ? 35.014  -37.211 87.689  1.00 41.40  ?  168 LEU A CA   1 
ATOM   2503  C C    . LEU A 1 159 ? 34.385  -38.404 87.039  1.00 44.45  ?  168 LEU A C    1 
ATOM   2504  O O    . LEU A 1 159 ? 33.914  -38.314 85.902  1.00 48.01  ?  168 LEU A O    1 
ATOM   2505  C CB   . LEU A 1 159 ? 36.542  -37.217 87.587  1.00 51.28  ?  168 LEU A CB   1 
ATOM   2506  C CG   . LEU A 1 159 ? 37.187  -37.585 86.268  1.00 54.30  ?  168 LEU A CG   1 
ATOM   2507  C CD1  . LEU A 1 159 ? 37.034  -36.555 85.199  1.00 56.08  ?  168 LEU A CD1  1 
ATOM   2508  C CD2  . LEU A 1 159 ? 38.644  -37.908 86.543  1.00 55.07  ?  168 LEU A CD2  1 
ATOM   2509  H H    . LEU A 1 159 ? 35.314  -37.248 89.619  1.00 52.75  ?  168 LEU A H    1 
ATOM   2510  H HA   . LEU A 1 159 ? 34.681  -36.412 87.251  1.00 49.68  ?  168 LEU A HA   1 
ATOM   2511  H HB2  . LEU A 1 159 ? 36.856  -36.327 87.813  1.00 61.53  ?  168 LEU A HB2  1 
ATOM   2512  H HB3  . LEU A 1 159 ? 36.879  -37.844 88.246  1.00 61.53  ?  168 LEU A HB3  1 
ATOM   2513  H HG   . LEU A 1 159 ? 36.770  -38.398 85.943  1.00 65.16  ?  168 LEU A HG   1 
ATOM   2514  H HD11 . LEU A 1 159 ? 37.473  -36.869 84.393  1.00 67.30  ?  168 LEU A HD11 1 
ATOM   2515  H HD12 . LEU A 1 159 ? 36.089  -36.417 85.028  1.00 67.30  ?  168 LEU A HD12 1 
ATOM   2516  H HD13 . LEU A 1 159 ? 37.441  -35.727 85.497  1.00 67.30  ?  168 LEU A HD13 1 
ATOM   2517  H HD21 . LEU A 1 159 ? 39.077  -38.147 85.708  1.00 66.08  ?  168 LEU A HD21 1 
ATOM   2518  H HD22 . LEU A 1 159 ? 39.074  -37.128 86.927  1.00 66.08  ?  168 LEU A HD22 1 
ATOM   2519  H HD23 . LEU A 1 159 ? 38.690  -38.652 87.164  1.00 66.08  ?  168 LEU A HD23 1 
ATOM   2520  N N    . LEU A 1 160 ? 34.326  -39.541 87.748  1.00 44.05  ?  169 LEU A N    1 
ATOM   2521  C CA   . LEU A 1 160 ? 33.804  -40.686 87.023  1.00 54.93  ?  169 LEU A CA   1 
ATOM   2522  C C    . LEU A 1 160 ? 32.347  -40.450 86.722  1.00 68.30  ?  169 LEU A C    1 
ATOM   2523  O O    . LEU A 1 160 ? 31.935  -40.573 85.567  1.00 66.23  ?  169 LEU A O    1 
ATOM   2524  C CB   . LEU A 1 160 ? 34.055  -41.967 87.794  1.00 60.20  ?  169 LEU A CB   1 
ATOM   2525  C CG   . LEU A 1 160 ? 35.538  -42.309 87.666  1.00 66.23  ?  169 LEU A CG   1 
ATOM   2526  C CD1  . LEU A 1 160 ? 35.990  -43.282 88.754  1.00 64.99  ?  169 LEU A CD1  1 
ATOM   2527  C CD2  . LEU A 1 160 ? 35.850  -42.947 86.315  1.00 94.53  ?  169 LEU A CD2  1 
ATOM   2528  H H    . LEU A 1 160 ? 34.558  -39.663 88.567  1.00 52.85  ?  169 LEU A H    1 
ATOM   2529  H HA   . LEU A 1 160 ? 34.271  -40.757 86.176  1.00 65.92  ?  169 LEU A HA   1 
ATOM   2530  H HB2  . LEU A 1 160 ? 33.841  -41.837 88.731  1.00 72.24  ?  169 LEU A HB2  1 
ATOM   2531  H HB3  . LEU A 1 160 ? 33.531  -42.690 87.415  1.00 72.24  ?  169 LEU A HB3  1 
ATOM   2532  H HG   . LEU A 1 160 ? 36.063  -41.497 87.747  1.00 79.47  ?  169 LEU A HG   1 
ATOM   2533  H HD11 . LEU A 1 160 ? 36.934  -43.471 88.636  1.00 77.99  ?  169 LEU A HD11 1 
ATOM   2534  H HD12 . LEU A 1 160 ? 35.840  -42.876 89.622  1.00 77.99  ?  169 LEU A HD12 1 
ATOM   2535  H HD13 . LEU A 1 160 ? 35.476  -44.101 88.678  1.00 77.99  ?  169 LEU A HD13 1 
ATOM   2536  H HD21 . LEU A 1 160 ? 36.798  -43.149 86.273  1.00 113.44 ?  169 LEU A HD21 1 
ATOM   2537  H HD22 . LEU A 1 160 ? 35.334  -43.763 86.225  1.00 113.44 ?  169 LEU A HD22 1 
ATOM   2538  H HD23 . LEU A 1 160 ? 35.613  -42.324 85.610  1.00 113.44 ?  169 LEU A HD23 1 
ATOM   2539  N N    . VAL A 1 161 ? 31.636  -39.854 87.673  1.00 51.38  ?  170 VAL A N    1 
ATOM   2540  C CA   . VAL A 1 161 ? 30.234  -39.540 87.436  1.00 40.20  ?  170 VAL A CA   1 
ATOM   2541  C C    . VAL A 1 161 ? 30.091  -38.554 86.286  1.00 47.74  ?  170 VAL A C    1 
ATOM   2542  O O    . VAL A 1 161 ? 29.081  -38.545 85.570  1.00 40.16  ?  170 VAL A O    1 
ATOM   2543  C CB   . VAL A 1 161 ? 29.575  -38.939 88.662  1.00 37.57  ?  170 VAL A CB   1 
ATOM   2544  C CG1  . VAL A 1 161 ? 28.086  -38.455 88.214  1.00 37.12  ?  170 VAL A CG1  1 
ATOM   2545  C CG2  . VAL A 1 161 ? 29.612  -39.840 89.823  1.00 45.95  ?  170 VAL A CG2  1 
ATOM   2546  H H    . VAL A 1 161 ? 31.933  -39.625 88.447  1.00 61.66  ?  170 VAL A H    1 
ATOM   2547  H HA   . VAL A 1 161 ? 29.759  -40.352 87.202  1.00 48.24  ?  170 VAL A HA   1 
ATOM   2548  H HB   . VAL A 1 161 ? 30.070  -38.142 88.908  1.00 45.08  ?  170 VAL A HB   1 
ATOM   2549  H HG11 . VAL A 1 161 ? 27.637  -38.065 88.980  1.00 44.55  ?  170 VAL A HG11 1 
ATOM   2550  H HG12 . VAL A 1 161 ? 28.168  -37.796 87.507  1.00 44.55  ?  170 VAL A HG12 1 
ATOM   2551  H HG13 . VAL A 1 161 ? 27.588  -39.223 87.894  1.00 44.55  ?  170 VAL A HG13 1 
ATOM   2552  H HG21 . VAL A 1 161 ? 29.178  -39.405 90.573  1.00 55.14  ?  170 VAL A HG21 1 
ATOM   2553  H HG22 . VAL A 1 161 ? 29.144  -40.660 89.600  1.00 55.14  ?  170 VAL A HG22 1 
ATOM   2554  H HG23 . VAL A 1 161 ? 30.536  -40.034 90.042  1.00 55.14  ?  170 VAL A HG23 1 
ATOM   2555  N N    . GLU A 1 162 ? 31.028  -37.614 86.180  1.00 55.72  ?  171 GLU A N    1 
ATOM   2556  C CA   . GLU A 1 162 ? 30.997  -36.721 85.039  1.00 42.75  ?  171 GLU A CA   1 
ATOM   2557  C C    . GLU A 1 162 ? 31.117  -37.499 83.735  1.00 37.84  ?  171 GLU A C    1 
ATOM   2558  O O    . GLU A 1 162 ? 30.328  -37.326 82.803  1.00 73.95  ?  171 GLU A O    1 
ATOM   2559  C CB   . GLU A 1 162 ? 32.115  -35.702 85.213  1.00 58.67  ?  171 GLU A CB   1 
ATOM   2560  C CG   . GLU A 1 162 ? 31.756  -34.400 84.508  1.00 63.72  ?  171 GLU A CG   1 
ATOM   2561  C CD   . GLU A 1 162 ? 31.153  -33.247 85.421  1.00 77.18  ?  171 GLU A CD   1 
ATOM   2562  O OE1  . GLU A 1 162 ? 30.650  -32.265 84.827  1.00 111.39 ?  171 GLU A OE1  1 
ATOM   2563  O OE2  . GLU A 1 162 ? 31.153  -33.280 86.683  1.00 62.80  -1 171 GLU A OE2  1 
ATOM   2564  H H    . GLU A 1 162 ? 31.670  -37.480 86.737  1.00 66.86  ?  171 GLU A H    1 
ATOM   2565  H HA   . GLU A 1 162 ? 30.152  -36.245 85.031  1.00 51.30  ?  171 GLU A HA   1 
ATOM   2566  H HB2  . GLU A 1 162 ? 32.241  -35.517 86.156  1.00 70.40  ?  171 GLU A HB2  1 
ATOM   2567  H HB3  . GLU A 1 162 ? 32.932  -36.049 84.822  1.00 70.40  ?  171 GLU A HB3  1 
ATOM   2568  H HG2  . GLU A 1 162 ? 32.559  -34.048 84.093  1.00 76.47  ?  171 GLU A HG2  1 
ATOM   2569  H HG3  . GLU A 1 162 ? 31.100  -34.597 83.821  1.00 76.47  ?  171 GLU A HG3  1 
ATOM   2570  N N    . ILE A 1 163 ? 32.020  -38.463 83.726  1.00 52.24  ?  172 ILE A N    1 
ATOM   2571  C CA   . ILE A 1 163 ? 32.197  -39.341 82.575  1.00 76.41  ?  172 ILE A CA   1 
ATOM   2572  C C    . ILE A 1 163 ? 30.941  -40.175 82.337  1.00 73.43  ?  172 ILE A C    1 
ATOM   2573  O O    . ILE A 1 163 ? 30.515  -40.366 81.192  1.00 69.44  ?  172 ILE A O    1 
ATOM   2574  C CB   . ILE A 1 163 ? 33.429  -40.229 82.792  1.00 76.83  ?  172 ILE A CB   1 
ATOM   2575  C CG1  . ILE A 1 163 ? 34.671  -39.339 82.784  1.00 74.63  ?  172 ILE A CG1  1 
ATOM   2576  C CG2  . ILE A 1 163 ? 33.518  -41.289 81.720  1.00 93.43  ?  172 ILE A CG2  1 
ATOM   2577  C CD1  . ILE A 1 163 ? 35.848  -39.925 83.425  1.00 78.53  ?  172 ILE A CD1  1 
ATOM   2578  H H    . ILE A 1 163 ? 32.551  -38.634 84.380  1.00 62.69  ?  172 ILE A H    1 
ATOM   2579  H HA   . ILE A 1 163 ? 32.352  -38.799 81.785  1.00 91.69  ?  172 ILE A HA   1 
ATOM   2580  H HB   . ILE A 1 163 ? 33.357  -40.661 83.657  1.00 92.19  ?  172 ILE A HB   1 
ATOM   2581  H HG12 . ILE A 1 163 ? 34.905  -39.143 81.863  1.00 89.56  ?  172 ILE A HG12 1 
ATOM   2582  H HG13 . ILE A 1 163 ? 34.464  -38.514 83.250  1.00 89.56  ?  172 ILE A HG13 1 
ATOM   2583  H HG21 . ILE A 1 163 ? 34.303  -41.835 81.881  1.00 112.12 ?  172 ILE A HG21 1 
ATOM   2584  H HG22 . ILE A 1 163 ? 32.719  -41.839 81.753  1.00 112.12 ?  172 ILE A HG22 1 
ATOM   2585  H HG23 . ILE A 1 163 ? 33.586  -40.857 80.854  1.00 112.12 ?  172 ILE A HG23 1 
ATOM   2586  H HD11 . ILE A 1 163 ? 36.583  -39.294 83.373  1.00 94.24  ?  172 ILE A HD11 1 
ATOM   2587  H HD12 . ILE A 1 163 ? 35.640  -40.115 84.353  1.00 94.24  ?  172 ILE A HD12 1 
ATOM   2588  H HD13 . ILE A 1 163 ? 36.083  -40.746 82.964  1.00 94.24  ?  172 ILE A HD13 1 
ATOM   2589  N N    . ALA A 1 164 ? 30.316  -40.656 83.417  1.00 62.69  ?  173 ALA A N    1 
ATOM   2590  C CA   . ALA A 1 164 ? 29.137  -41.487 83.260  1.00 81.65  ?  173 ALA A CA   1 
ATOM   2591  C C    . ALA A 1 164 ? 28.018  -40.707 82.628  1.00 72.71  ?  173 ALA A C    1 
ATOM   2592  O O    . ALA A 1 164 ? 27.273  -41.251 81.812  1.00 90.98  ?  173 ALA A O    1 
ATOM   2593  C CB   . ALA A 1 164 ? 28.672  -42.002 84.611  1.00 88.84  ?  173 ALA A CB   1 
ATOM   2594  H H    . ALA A 1 164 ? 30.555  -40.516 84.231  1.00 75.23  ?  173 ALA A H    1 
ATOM   2595  H HA   . ALA A 1 164 ? 29.345  -42.246 82.693  1.00 97.97  ?  173 ALA A HA   1 
ATOM   2596  H HB1  . ALA A 1 164 ? 27.884  -42.554 84.485  1.00 106.60 ?  173 ALA A HB1  1 
ATOM   2597  H HB2  . ALA A 1 164 ? 29.383  -42.527 85.011  1.00 106.60 ?  173 ALA A HB2  1 
ATOM   2598  H HB3  . ALA A 1 164 ? 28.459  -41.246 85.181  1.00 106.60 ?  173 ALA A HB3  1 
ATOM   2599  N N    . ALA A 1 165 ? 27.964  -39.409 82.905  1.00 62.79  ?  174 ALA A N    1 
ATOM   2600  C CA   . ALA A 1 165 ? 26.986  -38.551 82.278  1.00 78.93  ?  174 ALA A CA   1 
ATOM   2601  C C    . ALA A 1 165 ? 27.378  -38.181 80.851  1.00 68.57  ?  174 ALA A C    1 
ATOM   2602  O O    . ALA A 1 165 ? 26.529  -37.751 80.074  1.00 64.38  ?  174 ALA A O    1 
ATOM   2603  C CB   . ALA A 1 165 ? 26.806  -37.309 83.126  1.00 110.90 ?  174 ALA A CB   1 
ATOM   2604  H H    . ALA A 1 165 ? 28.487  -39.005 83.456  1.00 75.35  ?  174 ALA A H    1 
ATOM   2605  H HA   . ALA A 1 165 ? 26.135  -39.015 82.243  1.00 94.72  ?  174 ALA A HA   1 
ATOM   2606  H HB1  . ALA A 1 165 ? 26.149  -36.732 82.706  1.00 133.09 ?  174 ALA A HB1  1 
ATOM   2607  H HB2  . ALA A 1 165 ? 26.500  -37.571 84.009  1.00 133.09 ?  174 ALA A HB2  1 
ATOM   2608  H HB3  . ALA A 1 165 ? 27.657  -36.847 83.194  1.00 133.09 ?  174 ALA A HB3  1 
ATOM   2609  N N    . ALA A 1 166 ? 28.642  -38.281 80.471  1.00 84.79  ?  175 ALA A N    1 
ATOM   2610  C CA   . ALA A 1 166 ? 28.917  -37.901 79.103  1.00 86.29  ?  175 ALA A CA   1 
ATOM   2611  C C    . ALA A 1 166 ? 28.027  -38.663 78.158  1.00 82.52  ?  175 ALA A C    1 
ATOM   2612  O O    . ALA A 1 166 ? 27.536  -38.089 77.184  1.00 80.77  ?  175 ALA A O    1 
ATOM   2613  C CB   . ALA A 1 166 ? 30.378  -38.157 78.774  1.00 127.32 ?  175 ALA A CB   1 
ATOM   2614  H H    . ALA A 1 166 ? 29.309  -38.544 80.945  1.00 101.75 ?  175 ALA A H    1 
ATOM   2615  H HA   . ALA A 1 166 ? 28.740  -36.954 78.991  1.00 103.54 ?  175 ALA A HA   1 
ATOM   2616  H HB1  . ALA A 1 166 ? 30.545  -37.897 77.854  1.00 152.79 ?  175 ALA A HB1  1 
ATOM   2617  H HB2  . ALA A 1 166 ? 30.933  -37.631 79.372  1.00 152.79 ?  175 ALA A HB2  1 
ATOM   2618  H HB3  . ALA A 1 166 ? 30.568  -39.101 78.891  1.00 152.79 ?  175 ALA A HB3  1 
ATOM   2619  N N    . SER A 1 167 ? 27.719  -39.918 78.483  1.00 110.71 ?  176 SER A N    1 
ATOM   2620  C CA   . SER A 1 167 ? 26.919  -40.730 77.583  1.00 85.21  ?  176 SER A CA   1 
ATOM   2621  C C    . SER A 1 167 ? 25.569  -40.090 77.368  1.00 93.81  ?  176 SER A C    1 
ATOM   2622  O O    . SER A 1 167 ? 25.057  -40.037 76.248  1.00 69.98  ?  176 SER A O    1 
ATOM   2623  C CB   . SER A 1 167 ? 26.728  -42.122 78.176  1.00 89.39  ?  176 SER A CB   1 
ATOM   2624  O OG   . SER A 1 167 ? 27.938  -42.694 78.575  1.00 109.75 ?  176 SER A OG   1 
ATOM   2625  H H    . SER A 1 167 ? 27.958  -40.313 79.209  1.00 132.86 ?  176 SER A H    1 
ATOM   2626  H HA   . SER A 1 167 ? 27.367  -40.813 76.726  1.00 102.25 ?  176 SER A HA   1 
ATOM   2627  H HB2  . SER A 1 167 ? 26.146  -42.054 78.949  1.00 107.27 ?  176 SER A HB2  1 
ATOM   2628  H HB3  . SER A 1 167 ? 26.319  -42.692 77.507  1.00 107.27 ?  176 SER A HB3  1 
ATOM   2629  H HG   . SER A 1 167 ? 27.803  -43.457 78.897  1.00 131.70 ?  176 SER A HG   1 
ATOM   2630  N N    . ALA A 1 168 ? 25.049  -39.468 78.399  1.00 84.88  ?  177 ALA A N    1 
ATOM   2631  C CA   . ALA A 1 168 ? 23.746  -38.854 78.279  1.00 64.54  ?  177 ALA A CA   1 
ATOM   2632  C C    . ALA A 1 168 ? 23.840  -37.526 77.538  1.00 69.39  ?  177 ALA A C    1 
ATOM   2633  O O    . ALA A 1 168 ? 23.020  -37.229 76.664  1.00 57.34  ?  177 ALA A O    1 
ATOM   2634  C CB   . ALA A 1 168 ? 23.164  -38.668 79.674  1.00 63.51  ?  177 ALA A CB   1 
ATOM   2635  H H    . ALA A 1 168 ? 25.421  -39.386 79.170  1.00 101.86 ?  177 ALA A H    1 
ATOM   2636  H HA   . ALA A 1 168 ? 23.158  -39.442 77.779  1.00 77.45  ?  177 ALA A HA   1 
ATOM   2637  H HB1  . ALA A 1 168 ? 22.289  -38.256 79.598  1.00 76.21  ?  177 ALA A HB1  1 
ATOM   2638  H HB2  . ALA A 1 168 ? 23.086  -39.535 80.101  1.00 76.21  ?  177 ALA A HB2  1 
ATOM   2639  H HB3  . ALA A 1 168 ? 23.755  -38.097 80.189  1.00 76.21  ?  177 ALA A HB3  1 
ATOM   2640  N N    . ILE A 1 169 ? 24.886  -36.761 77.813  1.00 74.32  ?  178 ILE A N    1 
ATOM   2641  C CA   . ILE A 1 169 ? 25.091  -35.517 77.103  1.00 91.07  ?  178 ILE A CA   1 
ATOM   2642  C C    . ILE A 1 169 ? 25.068  -35.748 75.609  1.00 76.10  ?  178 ILE A C    1 
ATOM   2643  O O    . ILE A 1 169 ? 24.610  -34.884 74.860  1.00 56.56  ?  178 ILE A O    1 
ATOM   2644  C CB   . ILE A 1 169 ? 26.421  -34.887 77.522  1.00 120.15 ?  178 ILE A CB   1 
ATOM   2645  C CG1  . ILE A 1 169 ? 26.423  -34.607 79.024  1.00 106.84 ?  178 ILE A CG1  1 
ATOM   2646  C CG2  . ILE A 1 169 ? 26.682  -33.643 76.678  1.00 70.40  ?  178 ILE A CG2  1 
ATOM   2647  C CD1  . ILE A 1 169 ? 27.804  -34.284 79.575  1.00 116.34 ?  178 ILE A CD1  1 
ATOM   2648  H H    . ILE A 1 169 ? 25.486  -36.941 78.402  1.00 89.18  ?  178 ILE A H    1 
ATOM   2649  H HA   . ILE A 1 169 ? 24.378  -34.899 77.327  1.00 109.29 ?  178 ILE A HA   1 
ATOM   2650  H HB   . ILE A 1 169 ? 27.126  -35.526 77.338  1.00 144.18 ?  178 ILE A HB   1 
ATOM   2651  H HG12 . ILE A 1 169 ? 25.846  -33.847 79.202  1.00 128.21 ?  178 ILE A HG12 1 
ATOM   2652  H HG13 . ILE A 1 169 ? 26.091  -35.390 79.490  1.00 128.21 ?  178 ILE A HG13 1 
ATOM   2653  H HG21 . ILE A 1 169 ? 27.526  -33.249 76.949  1.00 84.48  ?  178 ILE A HG21 1 
ATOM   2654  H HG22 . ILE A 1 169 ? 26.722  -33.898 75.743  1.00 84.48  ?  178 ILE A HG22 1 
ATOM   2655  H HG23 . ILE A 1 169 ? 25.961  -33.009 76.818  1.00 84.48  ?  178 ILE A HG23 1 
ATOM   2656  H HD11 . ILE A 1 169 ? 27.732  -34.118 80.528  1.00 139.60 ?  178 ILE A HD11 1 
ATOM   2657  H HD12 . ILE A 1 169 ? 28.392  -35.039 79.414  1.00 139.60 ?  178 ILE A HD12 1 
ATOM   2658  H HD13 . ILE A 1 169 ? 28.147  -33.496 79.127  1.00 139.60 ?  178 ILE A HD13 1 
ATOM   2659  N N    . LYS A 1 170 ? 25.674  -36.857 75.138  1.00 81.46  ?  179 LYS A N    1 
ATOM   2660  C CA   . LYS A 1 170 ? 25.738  -37.132 73.693  1.00 65.02  ?  179 LYS A CA   1 
ATOM   2661  C C    . LYS A 1 170 ? 24.376  -37.007 72.996  1.00 68.16  ?  179 LYS A C    1 
ATOM   2662  O O    . LYS A 1 170 ? 24.302  -36.643 71.809  1.00 75.43  ?  179 LYS A O    1 
ATOM   2663  C CB   . LYS A 1 170 ? 26.263  -38.551 73.425  1.00 79.54  ?  179 LYS A CB   1 
ATOM   2664  C CG   . LYS A 1 170 ? 27.581  -38.992 74.057  1.00 108.78 ?  179 LYS A CG   1 
ATOM   2665  C CD   . LYS A 1 170 ? 28.200  -40.235 73.305  1.00 113.27 ?  179 LYS A CD   1 
ATOM   2666  C CE   . LYS A 1 170 ? 27.224  -41.445 73.198  1.00 115.22 ?  179 LYS A CE   1 
ATOM   2667  N NZ   . LYS A 1 170 ? 27.759  -42.676 72.509  1.00 109.21 1  179 LYS A NZ   1 
ATOM   2668  H H    . LYS A 1 170 ? 26.050  -37.454 75.629  1.00 97.76  ?  179 LYS A H    1 
ATOM   2669  H HA   . LYS A 1 170 ? 26.348  -36.502 73.278  1.00 78.02  ?  179 LYS A HA   1 
ATOM   2670  H HB2  . LYS A 1 170 ? 25.586  -39.176 73.728  1.00 95.44  ?  179 LYS A HB2  1 
ATOM   2671  H HB3  . LYS A 1 170 ? 26.370  -38.647 72.465  1.00 95.44  ?  179 LYS A HB3  1 
ATOM   2672  H HG2  . LYS A 1 170 ? 28.217  -38.262 74.012  1.00 130.54 ?  179 LYS A HG2  1 
ATOM   2673  H HG3  . LYS A 1 170 ? 27.423  -39.244 74.981  1.00 130.54 ?  179 LYS A HG3  1 
ATOM   2674  H HD2  . LYS A 1 170 ? 28.442  -39.967 72.405  1.00 135.92 ?  179 LYS A HD2  1 
ATOM   2675  H HD3  . LYS A 1 170 ? 28.989  -40.530 73.785  1.00 135.92 ?  179 LYS A HD3  1 
ATOM   2676  H HE2  . LYS A 1 170 ? 26.964  -41.707 74.095  1.00 138.26 ?  179 LYS A HE2  1 
ATOM   2677  H HE3  . LYS A 1 170 ? 26.438  -41.159 72.706  1.00 138.26 ?  179 LYS A HE3  1 
ATOM   2678  H HZ1  . LYS A 1 170 ? 27.136  -43.312 72.495  1.00 131.05 ?  179 LYS A HZ1  1 
ATOM   2679  H HZ2  . LYS A 1 170 ? 27.992  -42.480 71.673  1.00 131.05 ?  179 LYS A HZ2  1 
ATOM   2680  H HZ3  . LYS A 1 170 ? 28.474  -42.981 72.944  1.00 131.05 ?  179 LYS A HZ3  1 
ATOM   2681  N N    . VAL A 1 171 ? 23.292  -37.281 73.720  1.00 50.72  ?  180 VAL A N    1 
ATOM   2682  C CA   . VAL A 1 171 ? 21.997  -37.482 73.100  1.00 108.69 ?  180 VAL A CA   1 
ATOM   2683  C C    . VAL A 1 171 ? 21.258  -36.162 72.940  1.00 99.33  ?  180 VAL A C    1 
ATOM   2684  O O    . VAL A 1 171 ? 20.426  -36.028 72.038  1.00 85.07  ?  180 VAL A O    1 
ATOM   2685  C CB   . VAL A 1 171 ? 21.233  -38.512 73.956  1.00 102.35 ?  180 VAL A CB   1 
ATOM   2686  C CG1  . VAL A 1 171 ? 19.901  -38.817 73.360  1.00 104.32 ?  180 VAL A CG1  1 
ATOM   2687  C CG2  . VAL A 1 171 ? 22.038  -39.785 74.112  1.00 74.74  ?  180 VAL A CG2  1 
ATOM   2688  H H    . VAL A 1 171 ? 23.286  -37.355 74.577  1.00 60.86  ?  180 VAL A H    1 
ATOM   2689  H HA   . VAL A 1 171 ? 22.125  -37.862 72.217  1.00 130.43 ?  180 VAL A HA   1 
ATOM   2690  H HB   . VAL A 1 171 ? 21.087  -38.141 74.840  1.00 122.83 ?  180 VAL A HB   1 
ATOM   2691  H HG11 . VAL A 1 171 ? 19.446  -39.466 73.919  1.00 125.19 ?  180 VAL A HG11 1 
ATOM   2692  H HG12 . VAL A 1 171 ? 19.382  -37.999 73.313  1.00 125.19 ?  180 VAL A HG12 1 
ATOM   2693  H HG13 . VAL A 1 171 ? 20.029  -39.179 72.469  1.00 125.19 ?  180 VAL A HG13 1 
ATOM   2694  H HG21 . VAL A 1 171 ? 21.534  -40.413 74.654  1.00 89.69  ?  180 VAL A HG21 1 
ATOM   2695  H HG22 . VAL A 1 171 ? 22.204  -40.163 73.235  1.00 89.69  ?  180 VAL A HG22 1 
ATOM   2696  H HG23 . VAL A 1 171 ? 22.880  -39.575 74.547  1.00 89.69  ?  180 VAL A HG23 1 
ATOM   2697  N N    . ILE A 1 172 ? 21.608  -35.166 73.746  1.00 84.30  ?  181 ILE A N    1 
ATOM   2698  C CA   . ILE A 1 172 ? 20.881  -33.898 73.772  1.00 73.70  ?  181 ILE A CA   1 
ATOM   2699  C C    . ILE A 1 172 ? 20.566  -33.398 72.367  1.00 82.13  ?  181 ILE A C    1 
ATOM   2700  O O    . ILE A 1 172 ? 19.412  -33.041 72.098  1.00 70.25  ?  181 ILE A O    1 
ATOM   2701  C CB   . ILE A 1 172 ? 21.661  -32.877 74.616  1.00 71.79  ?  181 ILE A CB   1 
ATOM   2702  C CG1  . ILE A 1 172 ? 21.506  -33.201 76.094  1.00 93.48  ?  181 ILE A CG1  1 
ATOM   2703  C CG2  . ILE A 1 172 ? 21.172  -31.512 74.450  1.00 47.97  ?  181 ILE A CG2  1 
ATOM   2704  C CD1  . ILE A 1 172 ? 22.418  -32.386 76.971  1.00 76.02  ?  181 ILE A CD1  1 
ATOM   2705  H H    . ILE A 1 172 ? 22.269  -35.198 74.294  1.00 101.16 ?  181 ILE A H    1 
ATOM   2706  H HA   . ILE A 1 172 ? 20.032  -34.047 74.217  1.00 88.44  ?  181 ILE A HA   1 
ATOM   2707  H HB   . ILE A 1 172 ? 22.601  -32.913 74.376  1.00 86.15  ?  181 ILE A HB   1 
ATOM   2708  H HG12 . ILE A 1 172 ? 20.592  -33.019 76.362  1.00 112.17 ?  181 ILE A HG12 1 
ATOM   2709  H HG13 . ILE A 1 172 ? 21.713  -34.138 76.235  1.00 112.17 ?  181 ILE A HG13 1 
ATOM   2710  H HG21 . ILE A 1 172 ? 21.701  -30.917 75.004  1.00 57.57  ?  181 ILE A HG21 1 
ATOM   2711  H HG22 . ILE A 1 172 ? 21.256  -31.258 73.517  1.00 57.57  ?  181 ILE A HG22 1 
ATOM   2712  H HG23 . ILE A 1 172 ? 20.241  -31.476 74.720  1.00 57.57  ?  181 ILE A HG23 1 
ATOM   2713  H HD11 . ILE A 1 172 ? 22.273  -32.637 77.896  1.00 91.22  ?  181 ILE A HD11 1 
ATOM   2714  H HD12 . ILE A 1 172 ? 23.338  -32.564 76.720  1.00 91.22  ?  181 ILE A HD12 1 
ATOM   2715  H HD13 . ILE A 1 172 ? 22.217  -31.445 76.847  1.00 91.22  ?  181 ILE A HD13 1 
ATOM   2716  N N    . PRO A 1 173 ? 21.501  -33.331 71.446  1.00 77.63  ?  182 PRO A N    1 
ATOM   2717  C CA   . PRO A 1 173 ? 21.126  -32.907 70.088  1.00 98.43  ?  182 PRO A CA   1 
ATOM   2718  C C    . PRO A 1 173 ? 20.071  -33.779 69.441  1.00 79.84  ?  182 PRO A C    1 
ATOM   2719  O O    . PRO A 1 173 ? 19.364  -33.315 68.536  1.00 66.10  ?  182 PRO A O    1 
ATOM   2720  C CB   . PRO A 1 173 ? 22.448  -32.978 69.324  1.00 104.22 ?  182 PRO A CB   1 
ATOM   2721  C CG   . PRO A 1 173 ? 23.252  -33.979 70.088  1.00 110.94 ?  182 PRO A CG   1 
ATOM   2722  C CD   . PRO A 1 173 ? 22.876  -33.804 71.521  1.00 95.21  ?  182 PRO A CD   1 
ATOM   2723  H HA   . PRO A 1 173 ? 20.815  -31.988 70.100  1.00 118.12 ?  182 PRO A HA   1 
ATOM   2724  H HB2  . PRO A 1 173 ? 22.289  -33.282 68.416  1.00 125.07 ?  182 PRO A HB2  1 
ATOM   2725  H HB3  . PRO A 1 173 ? 22.880  -32.110 69.329  1.00 125.07 ?  182 PRO A HB3  1 
ATOM   2726  H HG2  . PRO A 1 173 ? 23.030  -34.873 69.785  1.00 133.13 ?  182 PRO A HG2  1 
ATOM   2727  H HG3  . PRO A 1 173 ? 24.197  -33.801 69.961  1.00 133.13 ?  182 PRO A HG3  1 
ATOM   2728  H HD2  . PRO A 1 173 ? 22.918  -34.653 71.988  1.00 114.26 ?  182 PRO A HD2  1 
ATOM   2729  H HD3  . PRO A 1 173 ? 23.442  -33.137 71.941  1.00 114.26 ?  182 PRO A HD3  1 
ATOM   2730  N N    . THR A 1 174 ? 19.999  -35.055 69.808  1.00 92.24  ?  183 THR A N    1 
ATOM   2731  C CA   . THR A 1 174 ? 18.999  -35.918 69.198  1.00 95.02  ?  183 THR A CA   1 
ATOM   2732  C C    . THR A 1 174 ? 17.610  -35.479 69.641  1.00 72.58  ?  183 THR A C    1 
ATOM   2733  O O    . THR A 1 174 ? 16.649  -35.490 68.843  1.00 64.28  ?  183 THR A O    1 
ATOM   2734  C CB   . THR A 1 174 ? 19.278  -37.387 69.542  1.00 95.13  ?  183 THR A CB   1 
ATOM   2735  O OG1  . THR A 1 174 ? 20.577  -37.762 69.064  1.00 136.33 ?  183 THR A OG1  1 
ATOM   2736  C CG2  . THR A 1 174 ? 18.321  -38.254 68.866  1.00 100.09 ?  183 THR A CG2  1 
ATOM   2737  H H    . THR A 1 174 ? 20.503  -35.435 70.392  1.00 110.69 ?  183 THR A H    1 
ATOM   2738  H HA   . THR A 1 174 ? 19.049  -35.823 68.234  1.00 114.02 ?  183 THR A HA   1 
ATOM   2739  H HB   . THR A 1 174 ? 19.217  -37.528 70.500  1.00 114.15 ?  183 THR A HB   1 
ATOM   2740  H HG1  . THR A 1 174 ? 20.731  -38.566 69.251  1.00 163.60 ?  183 THR A HG1  1 
ATOM   2741  H HG21 . THR A 1 174 ? 18.501  -39.181 69.086  1.00 120.11 ?  183 THR A HG21 1 
ATOM   2742  H HG22 . THR A 1 174 ? 17.418  -38.033 69.145  1.00 120.11 ?  183 THR A HG22 1 
ATOM   2743  H HG23 . THR A 1 174 ? 18.391  -38.138 67.905  1.00 120.11 ?  183 THR A HG23 1 
ATOM   2744  N N    . VAL A 1 175 ? 17.512  -34.995 70.873  1.00 53.71  ?  184 VAL A N    1 
ATOM   2745  C CA   . VAL A 1 175 ? 16.241  -34.491 71.372  1.00 52.12  ?  184 VAL A CA   1 
ATOM   2746  C C    . VAL A 1 175 ? 15.768  -33.295 70.584  1.00 73.02  ?  184 VAL A C    1 
ATOM   2747  O O    . VAL A 1 175 ? 14.683  -33.296 69.995  1.00 115.95 ?  184 VAL A O    1 
ATOM   2748  C CB   . VAL A 1 175 ? 16.381  -34.133 72.849  1.00 53.72  ?  184 VAL A CB   1 
ATOM   2749  C CG1  . VAL A 1 175 ? 15.160  -33.348 73.315  1.00 71.21  ?  184 VAL A CG1  1 
ATOM   2750  C CG2  . VAL A 1 175 ? 16.542  -35.466 73.617  1.00 48.33  ?  184 VAL A CG2  1 
ATOM   2751  H H    . VAL A 1 175 ? 18.161  -34.947 71.436  1.00 64.45  ?  184 VAL A H    1 
ATOM   2752  H HA   . VAL A 1 175 ? 15.570  -35.188 71.293  1.00 62.55  ?  184 VAL A HA   1 
ATOM   2753  H HB   . VAL A 1 175 ? 17.175  -33.592 72.984  1.00 64.47  ?  184 VAL A HB   1 
ATOM   2754  H HG11 . VAL A 1 175 ? 15.266  -33.129 74.254  1.00 85.45  ?  184 VAL A HG11 1 
ATOM   2755  H HG12 . VAL A 1 175 ? 15.088  -32.535 72.791  1.00 85.45  ?  184 VAL A HG12 1 
ATOM   2756  H HG13 . VAL A 1 175 ? 14.368  -33.894 73.190  1.00 85.45  ?  184 VAL A HG13 1 
ATOM   2757  H HG21 . VAL A 1 175 ? 16.635  -35.276 74.563  1.00 58.00  ?  184 VAL A HG21 1 
ATOM   2758  H HG22 . VAL A 1 175 ? 15.756  -36.014 73.465  1.00 58.00  ?  184 VAL A HG22 1 
ATOM   2759  H HG23 . VAL A 1 175 ? 17.333  -35.924 73.292  1.00 58.00  ?  184 VAL A HG23 1 
ATOM   2760  N N    . PHE A 1 176 ? 16.583  -32.272 70.540  1.00 73.41  ?  185 PHE A N    1 
ATOM   2761  C CA   . PHE A 1 176 ? 16.055  -31.029 70.059  1.00 129.35 ?  185 PHE A CA   1 
ATOM   2762  C C    . PHE A 1 176 ? 15.703  -31.183 68.617  1.00 115.90 ?  185 PHE A C    1 
ATOM   2763  O O    . PHE A 1 176 ? 14.753  -30.559 68.168  1.00 53.61  ?  185 PHE A O    1 
ATOM   2764  C CB   . PHE A 1 176 ? 17.046  -29.891 70.295  1.00 158.29 ?  185 PHE A CB   1 
ATOM   2765  C CG   . PHE A 1 176 ? 17.110  -29.454 71.733  1.00 132.62 ?  185 PHE A CG   1 
ATOM   2766  C CD1  . PHE A 1 176 ? 15.952  -29.126 72.420  1.00 95.34  ?  185 PHE A CD1  1 
ATOM   2767  C CD2  . PHE A 1 176 ? 18.303  -29.420 72.407  1.00 134.08 ?  185 PHE A CD2  1 
ATOM   2768  C CE1  . PHE A 1 176 ? 15.988  -28.754 73.734  1.00 81.15  ?  185 PHE A CE1  1 
ATOM   2769  C CE2  . PHE A 1 176 ? 18.352  -29.051 73.718  1.00 142.89 ?  185 PHE A CE2  1 
ATOM   2770  C CZ   . PHE A 1 176 ? 17.198  -28.727 74.386  1.00 103.65 ?  185 PHE A CZ   1 
ATOM   2771  H H    . PHE A 1 176 ? 17.411  -32.267 70.773  1.00 88.09  ?  185 PHE A H    1 
ATOM   2772  H HA   . PHE A 1 176 ? 15.242  -30.823 70.545  1.00 155.22 ?  185 PHE A HA   1 
ATOM   2773  H HB2  . PHE A 1 176 ? 17.932  -30.186 70.033  1.00 189.95 ?  185 PHE A HB2  1 
ATOM   2774  H HB3  . PHE A 1 176 ? 16.780  -29.126 69.761  1.00 189.95 ?  185 PHE A HB3  1 
ATOM   2775  H HD1  . PHE A 1 176 ? 15.135  -29.155 71.977  1.00 114.40 ?  185 PHE A HD1  1 
ATOM   2776  H HD2  . PHE A 1 176 ? 19.088  -29.647 71.964  1.00 160.90 ?  185 PHE A HD2  1 
ATOM   2777  H HE1  . PHE A 1 176 ? 15.205  -28.530 74.183  1.00 97.37  ?  185 PHE A HE1  1 
ATOM   2778  H HE2  . PHE A 1 176 ? 19.169  -29.025 74.163  1.00 171.47 ?  185 PHE A HE2  1 
ATOM   2779  H HZ   . PHE A 1 176 ? 17.237  -28.466 75.277  1.00 124.38 ?  185 PHE A HZ   1 
ATOM   2780  N N    . LYS A 1 177 ? 16.384  -32.081 67.911  1.00 87.81  ?  186 LYS A N    1 
ATOM   2781  C CA   . LYS A 1 177 ? 16.041  -32.271 66.509  1.00 104.50 ?  186 LYS A CA   1 
ATOM   2782  C C    . LYS A 1 177 ? 14.710  -32.973 66.376  1.00 67.05  ?  186 LYS A C    1 
ATOM   2783  O O    . LYS A 1 177 ? 13.876  -32.582 65.549  1.00 58.32  ?  186 LYS A O    1 
ATOM   2784  C CB   . LYS A 1 177 ? 17.108  -33.094 65.787  1.00 59.45  ?  186 LYS A CB   1 
ATOM   2785  H H    . LYS A 1 177 ? 17.023  -32.574 68.207  1.00 105.37 ?  186 LYS A H    1 
ATOM   2786  H HA   . LYS A 1 177 ? 15.976  -31.407 66.075  1.00 125.40 ?  186 LYS A HA   1 
ATOM   2787  N N    . ALA A 1 178 ? 14.464  -33.950 67.243  1.00 73.68  ?  187 ALA A N    1 
ATOM   2788  C CA   . ALA A 1 178 ? 13.244  -34.715 67.140  1.00 100.86 ?  187 ALA A CA   1 
ATOM   2789  C C    . ALA A 1 178 ? 12.072  -33.830 67.411  1.00 86.54  ?  187 ALA A C    1 
ATOM   2790  O O    . ALA A 1 178 ? 11.027  -33.983 66.777  1.00 116.95 ?  187 ALA A O    1 
ATOM   2791  C CB   . ALA A 1 178 ? 13.236  -35.831 68.145  1.00 52.50  ?  187 ALA A CB   1 
ATOM   2792  H H    . ALA A 1 178 ? 14.983  -34.182 67.889  1.00 88.42  ?  187 ALA A H    1 
ATOM   2793  H HA   . ALA A 1 178 ? 13.160  -35.090 66.249  1.00 121.03 ?  187 ALA A HA   1 
ATOM   2794  H HB1  . ALA A 1 178 ? 12.408  -36.329 68.056  1.00 63.00  ?  187 ALA A HB1  1 
ATOM   2795  H HB2  . ALA A 1 178 ? 13.993  -36.413 67.976  1.00 63.00  ?  187 ALA A HB2  1 
ATOM   2796  H HB3  . ALA A 1 178 ? 13.301  -35.453 69.036  1.00 63.00  ?  187 ALA A HB3  1 
ATOM   2797  N N    . MET A 1 179 ? 12.246  -32.850 68.296  1.00 91.59  ?  188 MET A N    1 
ATOM   2798  C CA   . MET A 1 179 ? 11.214  -31.840 68.462  1.00 90.07  ?  188 MET A CA   1 
ATOM   2799  C C    . MET A 1 179 ? 11.072  -31.002 67.202  1.00 111.73 ?  188 MET A C    1 
ATOM   2800  O O    . MET A 1 179 ? 9.960   -30.834 66.676  1.00 121.37 ?  188 MET A O    1 
ATOM   2801  C CB   . MET A 1 179 ? 11.518  -30.946 69.650  1.00 69.63  ?  188 MET A CB   1 
ATOM   2802  C CG   . MET A 1 179 ? 11.230  -31.560 71.004  1.00 70.24  ?  188 MET A CG   1 
ATOM   2803  S SD   . MET A 1 179 ? 11.689  -30.472 72.401  1.00 83.13  ?  188 MET A SD   1 
ATOM   2804  C CE   . MET A 1 179 ? 10.736  -29.001 72.034  1.00 100.28 ?  188 MET A CE   1 
ATOM   2805  H H    . MET A 1 179 ? 12.936  -32.752 68.800  1.00 109.91 ?  188 MET A H    1 
ATOM   2806  H HA   . MET A 1 179 ? 10.370  -32.285 68.636  1.00 108.08 ?  188 MET A HA   1 
ATOM   2807  H HB2  . MET A 1 179 ? 12.460  -30.714 69.628  1.00 83.55  ?  188 MET A HB2  1 
ATOM   2808  H HB3  . MET A 1 179 ? 10.983  -30.141 69.575  1.00 83.55  ?  188 MET A HB3  1 
ATOM   2809  H HG2  . MET A 1 179 ? 10.281  -31.745 71.070  1.00 84.29  ?  188 MET A HG2  1 
ATOM   2810  H HG3  . MET A 1 179 ? 11.735  -32.384 71.089  1.00 84.29  ?  188 MET A HG3  1 
ATOM   2811  H HE1  . MET A 1 179 ? 10.901  -28.338 72.722  1.00 120.34 ?  188 MET A HE1  1 
ATOM   2812  H HE2  . MET A 1 179 ? 11.008  -28.656 71.169  1.00 120.34 ?  188 MET A HE2  1 
ATOM   2813  H HE3  . MET A 1 179 ? 9.794   -29.232 72.016  1.00 120.34 ?  188 MET A HE3  1 
ATOM   2814  N N    . GLN A 1 180 ? 12.192  -30.489 66.685  1.00 82.92  ?  189 GLN A N    1 
ATOM   2815  C CA   . GLN A 1 180 ? 12.121  -29.643 65.505  1.00 110.28 ?  189 GLN A CA   1 
ATOM   2816  C C    . GLN A 1 180 ? 11.508  -30.395 64.335  1.00 80.93  ?  189 GLN A C    1 
ATOM   2817  O O    . GLN A 1 180 ? 10.795  -29.801 63.526  1.00 89.93  ?  189 GLN A O    1 
ATOM   2818  C CB   . GLN A 1 180 ? 13.512  -29.128 65.153  1.00 120.88 ?  189 GLN A CB   1 
ATOM   2819  H H    . GLN A 1 180 ? 12.984  -30.615 66.994  1.00 99.50  ?  189 GLN A H    1 
ATOM   2820  H HA   . GLN A 1 180 ? 11.557  -28.878 65.698  1.00 132.34 ?  189 GLN A HA   1 
ATOM   2821  N N    . MET A 1 181 ? 11.769  -31.703 64.233  1.00 113.04 ?  190 MET A N    1 
ATOM   2822  C CA   . MET A 1 181 ? 11.240  -32.552 63.167  1.00 137.27 ?  190 MET A CA   1 
ATOM   2823  C C    . MET A 1 181 ? 10.008  -33.365 63.571  1.00 105.79 ?  190 MET A C    1 
ATOM   2824  O O    . MET A 1 181 ? 9.498   -34.129 62.751  1.00 120.55 ?  190 MET A O    1 
ATOM   2825  C CB   . MET A 1 181 ? 12.335  -33.511 62.661  1.00 91.31  ?  190 MET A CB   1 
ATOM   2826  C CG   . MET A 1 181 ? 13.480  -32.857 61.896  1.00 87.83  ?  190 MET A CG   1 
ATOM   2827  H H    . MET A 1 181 ? 12.266  -32.131 64.790  1.00 135.65 ?  190 MET A H    1 
ATOM   2828  H HA   . MET A 1 181 ? 10.993  -31.981 62.423  1.00 164.73 ?  190 MET A HA   1 
ATOM   2829  H HB2  . MET A 1 181 ? 12.720  -33.968 63.426  1.00 109.57 ?  190 MET A HB2  1 
ATOM   2830  H HB3  . MET A 1 181 ? 11.924  -34.161 62.070  1.00 109.57 ?  190 MET A HB3  1 
ATOM   2831  H HG2  . MET A 1 181 ? 13.113  -32.337 61.164  1.00 105.40 ?  190 MET A HG2  1 
ATOM   2832  H HG3  . MET A 1 181 ? 13.972  -32.278 62.499  1.00 105.40 ?  190 MET A HG3  1 
ATOM   2833  N N    . GLN A 1 182 ? 9.527   -33.241 64.804  1.00 95.28  ?  191 GLN A N    1 
ATOM   2834  C CA   . GLN A 1 182 ? 8.265   -33.867 65.228  1.00 92.91  ?  191 GLN A CA   1 
ATOM   2835  C C    . GLN A 1 182 ? 8.292   -35.394 65.074  1.00 105.85 ?  191 GLN A C    1 
ATOM   2836  O O    . GLN A 1 182 ? 7.285   -36.017 64.745  1.00 125.15 ?  191 GLN A O    1 
ATOM   2837  C CB   . GLN A 1 182 ? 7.081   -33.259 64.467  1.00 123.86 ?  191 GLN A CB   1 
ATOM   2838  C CG   . GLN A 1 182 ? 6.537   -31.920 65.007  1.00 118.68 ?  191 GLN A CG   1 
ATOM   2839  C CD   . GLN A 1 182 ? 5.557   -32.040 66.197  1.00 118.65 ?  191 GLN A CD   1 
ATOM   2840  O OE1  . GLN A 1 182 ? 5.105   -31.035 66.736  1.00 130.53 ?  191 GLN A OE1  1 
ATOM   2841  N NE2  . GLN A 1 182 ? 5.238   -33.255 66.607  1.00 178.88 ?  191 GLN A NE2  1 
ATOM   2842  H H    . GLN A 1 182 ? 9.915   -32.794 65.427  1.00 114.34 ?  191 GLN A H    1 
ATOM   2843  H HA   . GLN A 1 182 ? 8.132   -33.675 66.170  1.00 111.49 ?  191 GLN A HA   1 
ATOM   2844  H HB2  . GLN A 1 182 ? 7.355   -33.109 63.549  1.00 148.63 ?  191 GLN A HB2  1 
ATOM   2845  H HB3  . GLN A 1 182 ? 6.349   -33.895 64.485  1.00 148.63 ?  191 GLN A HB3  1 
ATOM   2846  H HG2  . GLN A 1 182 ? 7.287   -31.378 65.300  1.00 142.41 ?  191 GLN A HG2  1 
ATOM   2847  H HG3  . GLN A 1 182 ? 6.070   -31.466 64.288  1.00 142.41 ?  191 GLN A HG3  1 
ATOM   2848  H HE21 . GLN A 1 182 ? 5.573   -33.943 66.214  1.00 214.66 ?  191 GLN A HE21 1 
ATOM   2849  H HE22 . GLN A 1 182 ? 4.695   -33.358 67.266  1.00 214.66 ?  191 GLN A HE22 1 
ATOM   2850  N N    . GLU A 1 183 ? 9.447   -36.004 65.334  1.00 110.91 ?  192 GLU A N    1 
ATOM   2851  C CA   . GLU A 1 183 ? 9.625   -37.462 65.317  1.00 80.90  ?  192 GLU A CA   1 
ATOM   2852  C C    . GLU A 1 183 ? 9.416   -38.028 66.711  1.00 93.40  ?  192 GLU A C    1 
ATOM   2853  O O    . GLU A 1 183 ? 10.346  -38.161 67.495  1.00 108.31 ?  192 GLU A O    1 
ATOM   2854  C CB   . GLU A 1 183 ? 11.008  -37.834 64.818  1.00 83.09  ?  192 GLU A CB   1 
ATOM   2855  C CG   . GLU A 1 183 ? 11.256  -37.758 63.318  1.00 108.33 ?  192 GLU A CG   1 
ATOM   2856  C CD   . GLU A 1 183 ? 10.628  -38.918 62.569  1.00 128.48 ?  192 GLU A CD   1 
ATOM   2857  O OE1  . GLU A 1 183 ? 10.216  -38.729 61.404  1.00 131.02 ?  192 GLU A OE1  1 
ATOM   2858  O OE2  . GLU A 1 183 ? 10.580  -40.035 63.147  1.00 129.42 -1 192 GLU A OE2  1 
ATOM   2859  H H    . GLU A 1 183 ? 10.169  -35.580 65.530  1.00 133.09 ?  192 GLU A H    1 
ATOM   2860  H HA   . GLU A 1 183 ? 8.969   -37.860 64.724  1.00 97.08  ?  192 GLU A HA   1 
ATOM   2861  H HB2  . GLU A 1 183 ? 11.650  -37.243 65.242  1.00 99.71  ?  192 GLU A HB2  1 
ATOM   2862  H HB3  . GLU A 1 183 ? 11.190  -38.748 65.090  1.00 99.71  ?  192 GLU A HB3  1 
ATOM   2863  H HG2  . GLU A 1 183 ? 10.873  -36.936 62.974  1.00 129.99 ?  192 GLU A HG2  1 
ATOM   2864  H HG3  . GLU A 1 183 ? 12.211  -37.774 63.153  1.00 129.99 ?  192 GLU A HG3  1 
ATOM   2865  N N    . ARG A 1 184 ? 8.189   -38.422 67.004  1.00 86.56  ?  193 ARG A N    1 
ATOM   2866  C CA   . ARG A 1 184 ? 7.838   -38.799 68.371  1.00 56.11  ?  193 ARG A CA   1 
ATOM   2867  C C    . ARG A 1 184 ? 8.483   -40.108 68.822  1.00 70.78  ?  193 ARG A C    1 
ATOM   2868  O O    . ARG A 1 184 ? 8.860   -40.250 69.999  1.00 77.57  ?  193 ARG A O    1 
ATOM   2869  C CB   . ARG A 1 184 ? 6.298   -38.899 68.488  1.00 61.83  ?  193 ARG A CB   1 
ATOM   2870  C CG   . ARG A 1 184 ? 5.801   -39.459 69.831  1.00 65.39  ?  193 ARG A CG   1 
ATOM   2871  C CD   . ARG A 1 184 ? 5.663   -40.994 69.780  1.00 76.80  ?  193 ARG A CD   1 
ATOM   2872  N NE   . ARG A 1 184 ? 4.908   -41.480 70.920  1.00 79.41  ?  193 ARG A NE   1 
ATOM   2873  C CZ   . ARG A 1 184 ? 4.788   -42.760 71.257  1.00 65.11  ?  193 ARG A CZ   1 
ATOM   2874  N NH1  . ARG A 1 184 ? 5.392   -43.712 70.536  1.00 85.06  1  193 ARG A NH1  1 
ATOM   2875  N NH2  . ARG A 1 184 ? 4.047   -43.064 72.316  1.00 62.75  1  193 ARG A NH2  1 
ATOM   2876  H H    . ARG A 1 184 ? 7.543   -38.481 66.439  1.00 103.88 ?  193 ARG A H    1 
ATOM   2877  H HA   . ARG A 1 184 ? 8.137   -38.099 68.973  1.00 67.33  ?  193 ARG A HA   1 
ATOM   2878  H HB2  . ARG A 1 184 ? 5.920   -38.012 68.380  1.00 74.19  ?  193 ARG A HB2  1 
ATOM   2879  H HB3  . ARG A 1 184 ? 5.970   -39.482 67.786  1.00 74.19  ?  193 ARG A HB3  1 
ATOM   2880  H HG2  . ARG A 1 184 ? 6.437   -39.233 70.528  1.00 78.47  ?  193 ARG A HG2  1 
ATOM   2881  H HG3  . ARG A 1 184 ? 4.931   -39.081 70.034  1.00 78.47  ?  193 ARG A HG3  1 
ATOM   2882  H HD2  . ARG A 1 184 ? 5.193   -41.249 68.970  1.00 92.16  ?  193 ARG A HD2  1 
ATOM   2883  H HD3  . ARG A 1 184 ? 6.544   -41.399 69.801  1.00 92.16  ?  193 ARG A HD3  1 
ATOM   2884  H HE   . ARG A 1 184 ? 4.510   -40.899 71.413  1.00 95.30  ?  193 ARG A HE   1 
ATOM   2885  H HH11 . ARG A 1 184 ? 5.863   -43.498 69.849  1.00 102.07 ?  193 ARG A HH11 1 
ATOM   2886  H HH12 . ARG A 1 184 ? 5.311   -44.538 70.761  1.00 102.07 ?  193 ARG A HH12 1 
ATOM   2887  H HH21 . ARG A 1 184 ? 3.668   -42.439 72.769  1.00 75.30  ?  193 ARG A HH21 1 
ATOM   2888  H HH22 . ARG A 1 184 ? 3.960   -43.884 72.558  1.00 75.30  ?  193 ARG A HH22 1 
ATOM   2889  N N    . ASP A 1 185 ? 8.561   -41.107 67.941  1.00 93.55  ?  194 ASP A N    1 
ATOM   2890  C CA   . ASP A 1 185 ? 9.100   -42.367 68.419  1.00 98.86  ?  194 ASP A CA   1 
ATOM   2891  C C    . ASP A 1 185 ? 10.531  -42.136 68.845  1.00 88.32  ?  194 ASP A C    1 
ATOM   2892  O O    . ASP A 1 185 ? 10.904  -42.427 69.993  1.00 60.80  ?  194 ASP A O    1 
ATOM   2893  C CB   . ASP A 1 185 ? 8.983   -43.444 67.350  1.00 109.74 ?  194 ASP A CB   1 
ATOM   2894  C CG   . ASP A 1 185 ? 7.517   -43.910 67.133  1.00 106.29 ?  194 ASP A CG   1 
ATOM   2895  O OD1  . ASP A 1 185 ? 6.688   -43.768 68.077  1.00 106.06 ?  194 ASP A OD1  1 
ATOM   2896  O OD2  . ASP A 1 185 ? 7.197   -44.406 66.020  1.00 105.95 -1 194 ASP A OD2  1 
ATOM   2897  H H    . ASP A 1 185 ? 8.323   -41.082 67.114  1.00 112.25 ?  194 ASP A H    1 
ATOM   2898  H HA   . ASP A 1 185 ? 8.596   -42.656 69.196  1.00 118.64 ?  194 ASP A HA   1 
ATOM   2899  H HB2  . ASP A 1 185 ? 9.315   -43.093 66.509  1.00 131.69 ?  194 ASP A HB2  1 
ATOM   2900  H HB3  . ASP A 1 185 ? 9.507   -44.216 67.618  1.00 131.69 ?  194 ASP A HB3  1 
ATOM   2901  N N    . THR A 1 186 ? 11.262  -41.397 67.997  1.00 99.49  ?  195 THR A N    1 
ATOM   2902  C CA   . THR A 1 186 ? 12.674  -41.108 68.191  1.00 98.18  ?  195 THR A CA   1 
ATOM   2903  C C    . THR A 1 186 ? 12.896  -40.303 69.465  1.00 104.38 ?  195 THR A C    1 
ATOM   2904  O O    . THR A 1 186 ? 13.882  -40.504 70.176  1.00 78.63  ?  195 THR A O    1 
ATOM   2905  C CB   . THR A 1 186 ? 13.190  -40.327 66.974  1.00 93.14  ?  195 THR A CB   1 
ATOM   2906  O OG1  . THR A 1 186 ? 13.011  -41.084 65.772  1.00 93.22  ?  195 THR A OG1  1 
ATOM   2907  C CG2  . THR A 1 186 ? 14.644  -40.006 67.080  1.00 86.61  ?  195 THR A CG2  1 
ATOM   2908  H H    . THR A 1 186 ? 10.942  -41.044 67.281  1.00 119.38 ?  195 THR A H    1 
ATOM   2909  H HA   . THR A 1 186 ? 13.170  -41.939 68.260  1.00 117.81 ?  195 THR A HA   1 
ATOM   2910  H HB   . THR A 1 186 ? 12.701  -39.492 66.900  1.00 111.77 ?  195 THR A HB   1 
ATOM   2911  H HG1  . THR A 1 186 ? 13.296  -40.649 65.113  1.00 111.86 ?  195 THR A HG1  1 
ATOM   2912  H HG21 . THR A 1 186 ? 14.933  -39.514 66.296  1.00 103.93 ?  195 THR A HG21 1 
ATOM   2913  H HG22 . THR A 1 186 ? 14.807  -39.466 67.869  1.00 103.93 ?  195 THR A HG22 1 
ATOM   2914  H HG23 . THR A 1 186 ? 15.160  -40.825 67.147  1.00 103.93 ?  195 THR A HG23 1 
ATOM   2915  N N    . LEU A 1 187 ? 11.991  -39.387 69.795  1.00 87.95  ?  196 LEU A N    1 
ATOM   2916  C CA   . LEU A 1 187 ? 12.199  -38.644 71.031  1.00 64.15  ?  196 LEU A CA   1 
ATOM   2917  C C    . LEU A 1 187 ? 12.077  -39.574 72.235  1.00 85.08  ?  196 LEU A C    1 
ATOM   2918  O O    . LEU A 1 187 ? 12.924  -39.572 73.134  1.00 82.96  ?  196 LEU A O    1 
ATOM   2919  C CB   . LEU A 1 187 ? 11.209  -37.481 71.093  1.00 49.76  ?  196 LEU A CB   1 
ATOM   2920  C CG   . LEU A 1 187 ? 10.966  -36.643 72.364  1.00 80.74  ?  196 LEU A CG   1 
ATOM   2921  C CD1  . LEU A 1 187 ? 12.120  -35.852 72.795  1.00 119.93 ?  196 LEU A CD1  1 
ATOM   2922  C CD2  . LEU A 1 187 ? 9.827   -35.685 72.149  1.00 118.79 ?  196 LEU A CD2  1 
ATOM   2923  H H    . LEU A 1 187 ? 11.285  -39.184 69.347  1.00 105.54 ?  196 LEU A H    1 
ATOM   2924  H HA   . LEU A 1 187 ? 13.096  -38.274 71.030  1.00 76.98  ?  196 LEU A HA   1 
ATOM   2925  H HB2  . LEU A 1 187 ? 11.480  -36.849 70.409  1.00 59.72  ?  196 LEU A HB2  1 
ATOM   2926  H HB3  . LEU A 1 187 ? 10.342  -37.840 70.846  1.00 59.72  ?  196 LEU A HB3  1 
ATOM   2927  H HG   . LEU A 1 187 ? 10.723  -37.237 73.091  1.00 96.89  ?  196 LEU A HG   1 
ATOM   2928  H HD11 . LEU A 1 187 ? 11.882  -35.358 73.596  1.00 143.92 ?  196 LEU A HD11 1 
ATOM   2929  H HD12 . LEU A 1 187 ? 12.860  -36.450 72.982  1.00 143.92 ?  196 LEU A HD12 1 
ATOM   2930  H HD13 . LEU A 1 187 ? 12.363  -35.236 72.086  1.00 143.92 ?  196 LEU A HD13 1 
ATOM   2931  H HD21 . LEU A 1 187 ? 9.692   -35.169 72.960  1.00 142.55 ?  196 LEU A HD21 1 
ATOM   2932  H HD22 . LEU A 1 187 ? 10.047  -35.093 71.413  1.00 142.55 ?  196 LEU A HD22 1 
ATOM   2933  H HD23 . LEU A 1 187 ? 9.025   -36.190 71.941  1.00 142.55 ?  196 LEU A HD23 1 
ATOM   2934  N N    . LEU A 1 188 ? 11.117  -40.478 72.199  1.00 95.29  ?  197 LEU A N    1 
ATOM   2935  C CA   . LEU A 1 188 ? 10.916  -41.346 73.339  1.00 112.43 ?  197 LEU A CA   1 
ATOM   2936  C C    . LEU A 1 188 ? 12.134  -42.225 73.568  1.00 77.65  ?  197 LEU A C    1 
ATOM   2937  O O    . LEU A 1 188 ? 12.657  -42.331 74.696  1.00 55.59  ?  197 LEU A O    1 
ATOM   2938  C CB   . LEU A 1 188 ? 9.674   -42.161 73.072  1.00 96.49  ?  197 LEU A CB   1 
ATOM   2939  C CG   . LEU A 1 188 ? 9.151   -42.959 74.240  1.00 75.48  ?  197 LEU A CG   1 
ATOM   2940  C CD1  . LEU A 1 188 ? 7.663   -43.118 74.106  1.00 115.14 ?  197 LEU A CD1  1 
ATOM   2941  C CD2  . LEU A 1 188 ? 9.866   -44.309 74.225  1.00 73.71  ?  197 LEU A CD2  1 
ATOM   2942  H H    . LEU A 1 188 ? 10.579  -40.608 71.541  1.00 114.35 ?  197 LEU A H    1 
ATOM   2943  H HA   . LEU A 1 188 ? 10.769  -40.809 74.134  1.00 134.92 ?  197 LEU A HA   1 
ATOM   2944  H HB2  . LEU A 1 188 ? 8.967   -41.559 72.793  1.00 115.79 ?  197 LEU A HB2  1 
ATOM   2945  H HB3  . LEU A 1 188 ? 9.867   -42.787 72.357  1.00 115.79 ?  197 LEU A HB3  1 
ATOM   2946  H HG   . LEU A 1 188 ? 9.349   -42.503 75.073  1.00 90.58  ?  197 LEU A HG   1 
ATOM   2947  H HD11 . LEU A 1 188 ? 7.331   -43.632 74.859  1.00 138.17 ?  197 LEU A HD11 1 
ATOM   2948  H HD12 . LEU A 1 188 ? 7.252   -42.239 74.098  1.00 138.17 ?  197 LEU A HD12 1 
ATOM   2949  H HD13 . LEU A 1 188 ? 7.469   -43.582 73.277  1.00 138.17 ?  197 LEU A HD13 1 
ATOM   2950  H HD21 . LEU A 1 188 ? 9.547   -44.843 74.968  1.00 88.46  ?  197 LEU A HD21 1 
ATOM   2951  H HD22 . LEU A 1 188 ? 9.674   -44.758 73.387  1.00 88.46  ?  197 LEU A HD22 1 
ATOM   2952  H HD23 . LEU A 1 188 ? 10.821  -44.160 74.309  1.00 88.46  ?  197 LEU A HD23 1 
ATOM   2953  N N    . LYS A 1 189 ? 12.631  -42.823 72.490  1.00 58.80  ?  198 LYS A N    1 
ATOM   2954  C CA   . LYS A 1 189 ? 13.826  -43.648 72.585  1.00 80.18  ?  198 LYS A CA   1 
ATOM   2955  C C    . LYS A 1 189 ? 14.932  -42.873 73.275  1.00 93.09  ?  198 LYS A C    1 
ATOM   2956  O O    . LYS A 1 189 ? 15.597  -43.386 74.183  1.00 122.51 ?  198 LYS A O    1 
ATOM   2957  C CB   . LYS A 1 189 ? 14.263  -44.094 71.180  1.00 102.36 ?  198 LYS A CB   1 
ATOM   2958  C CG   . LYS A 1 189 ? 15.513  -44.916 71.129  1.00 111.11 ?  198 LYS A CG   1 
ATOM   2959  C CD   . LYS A 1 189 ? 15.990  -45.085 69.693  1.00 108.75 ?  198 LYS A CD   1 
ATOM   2960  C CE   . LYS A 1 189 ? 17.250  -45.937 69.627  1.00 105.32 ?  198 LYS A CE   1 
ATOM   2961  N NZ   . LYS A 1 189 ? 16.910  -47.296 70.071  1.00 152.01 1  198 LYS A NZ   1 
ATOM   2962  H H    . LYS A 1 189 ? 12.297  -42.767 71.699  1.00 70.55  ?  198 LYS A H    1 
ATOM   2963  H HA   . LYS A 1 189 ? 13.632  -44.439 73.112  1.00 96.21  ?  198 LYS A HA   1 
ATOM   2964  H HB2  . LYS A 1 189 ? 13.550  -44.624 70.791  1.00 122.83 ?  198 LYS A HB2  1 
ATOM   2965  H HB3  . LYS A 1 189 ? 14.411  -43.303 70.639  1.00 122.83 ?  198 LYS A HB3  1 
ATOM   2966  H HG2  . LYS A 1 189 ? 16.212  -44.471 71.633  1.00 133.33 ?  198 LYS A HG2  1 
ATOM   2967  H HG3  . LYS A 1 189 ? 15.337  -45.795 71.499  1.00 133.33 ?  198 LYS A HG3  1 
ATOM   2968  H HD2  . LYS A 1 189 ? 15.298  -45.524 69.175  1.00 130.50 ?  198 LYS A HD2  1 
ATOM   2969  H HD3  . LYS A 1 189 ? 16.191  -44.214 69.317  1.00 130.50 ?  198 LYS A HD3  1 
ATOM   2970  H HE2  . LYS A 1 189 ? 17.574  -45.977 68.714  1.00 126.38 ?  198 LYS A HE2  1 
ATOM   2971  H HE3  . LYS A 1 189 ? 17.926  -45.573 70.219  1.00 126.38 ?  198 LYS A HE3  1 
ATOM   2972  H HZ1  . LYS A 1 189 ? 17.632  -47.815 70.041  1.00 182.42 ?  198 LYS A HZ1  1 
ATOM   2973  H HZ2  . LYS A 1 189 ? 16.603  -47.275 70.906  1.00 182.42 ?  198 LYS A HZ2  1 
ATOM   2974  H HZ3  . LYS A 1 189 ? 16.283  -47.641 69.541  1.00 182.42 ?  198 LYS A HZ3  1 
ATOM   2975  N N    . ALA A 1 190 ? 15.090  -41.608 72.897  1.00 74.21  ?  199 ALA A N    1 
ATOM   2976  C CA   . ALA A 1 190 ? 16.169  -40.799 73.432  1.00 63.51  ?  199 ALA A CA   1 
ATOM   2977  C C    . ALA A 1 190 ? 15.995  -40.557 74.925  1.00 56.98  ?  199 ALA A C    1 
ATOM   2978  O O    . ALA A 1 190 ? 16.903  -40.792 75.731  1.00 71.63  ?  199 ALA A O    1 
ATOM   2979  C CB   . ALA A 1 190 ? 16.236  -39.487 72.664  1.00 59.47  ?  199 ALA A CB   1 
ATOM   2980  H H    . ALA A 1 190 ? 14.585  -41.199 72.334  1.00 89.05  ?  199 ALA A H    1 
ATOM   2981  H HA   . ALA A 1 190 ? 17.009  -41.266 73.301  1.00 76.21  ?  199 ALA A HA   1 
ATOM   2982  H HB1  . ALA A 1 190 ? 16.958  -38.947 73.023  1.00 71.36  ?  199 ALA A HB1  1 
ATOM   2983  H HB2  . ALA A 1 190 ? 16.400  -39.678 71.727  1.00 71.36  ?  199 ALA A HB2  1 
ATOM   2984  H HB3  . ALA A 1 190 ? 15.392  -39.019 72.764  1.00 71.36  ?  199 ALA A HB3  1 
ATOM   2985  N N    . LEU A 1 191 ? 14.822  -40.099 75.318  1.00 57.11  ?  200 LEU A N    1 
ATOM   2986  C CA   . LEU A 1 191 ? 14.637  -39.838 76.735  1.00 47.17  ?  200 LEU A CA   1 
ATOM   2987  C C    . LEU A 1 191 ? 14.916  -41.089 77.546  1.00 60.94  ?  200 LEU A C    1 
ATOM   2988  O O    . LEU A 1 191 ? 15.380  -41.007 78.683  1.00 83.81  ?  200 LEU A O    1 
ATOM   2989  C CB   . LEU A 1 191 ? 13.228  -39.338 76.981  1.00 82.97  ?  200 LEU A CB   1 
ATOM   2990  C CG   . LEU A 1 191 ? 13.015  -38.012 76.277  1.00 90.27  ?  200 LEU A CG   1 
ATOM   2991  C CD1  . LEU A 1 191 ? 11.549  -37.722 76.207  1.00 77.30  ?  200 LEU A CD1  1 
ATOM   2992  C CD2  . LEU A 1 191 ? 13.775  -36.882 76.902  1.00 97.40  ?  200 LEU A CD2  1 
ATOM   2993  H H    . LEU A 1 191 ? 14.144  -39.936 74.814  1.00 68.54  ?  200 LEU A H    1 
ATOM   2994  H HA   . LEU A 1 191 ? 15.258  -39.148 77.017  1.00 56.60  ?  200 LEU A HA   1 
ATOM   2995  H HB2  . LEU A 1 191 ? 12.590  -39.979 76.631  1.00 99.57  ?  200 LEU A HB2  1 
ATOM   2996  H HB3  . LEU A 1 191 ? 13.092  -39.207 77.933  1.00 99.57  ?  200 LEU A HB3  1 
ATOM   2997  H HG   . LEU A 1 191 ? 13.334  -38.100 75.365  1.00 108.32 ?  200 LEU A HG   1 
ATOM   2998  H HD11 . LEU A 1 191 ? 11.417  -36.874 75.755  1.00 92.76  ?  200 LEU A HD11 1 
ATOM   2999  H HD12 . LEU A 1 191 ? 11.110  -38.432 75.712  1.00 92.76  ?  200 LEU A HD12 1 
ATOM   3000  H HD13 . LEU A 1 191 ? 11.193  -37.677 77.108  1.00 92.76  ?  200 LEU A HD13 1 
ATOM   3001  H HD21 . LEU A 1 191 ? 13.595  -36.068 76.406  1.00 116.88 ?  200 LEU A HD21 1 
ATOM   3002  H HD22 . LEU A 1 191 ? 13.486  -36.779 77.822  1.00 116.88 ?  200 LEU A HD22 1 
ATOM   3003  H HD23 . LEU A 1 191 ? 14.723  -37.085 76.873  1.00 116.88 ?  200 LEU A HD23 1 
ATOM   3004  N N    . LEU A 1 192 ? 14.666  -42.255 76.967  1.00 57.71  ?  201 LEU A N    1 
ATOM   3005  C CA   . LEU A 1 192 ? 14.932  -43.469 77.707  1.00 75.17  ?  201 LEU A CA   1 
ATOM   3006  C C    . LEU A 1 192 ? 16.421  -43.741 77.791  1.00 84.08  ?  201 LEU A C    1 
ATOM   3007  O O    . LEU A 1 192 ? 16.904  -44.161 78.843  1.00 81.69  ?  201 LEU A O    1 
ATOM   3008  C CB   . LEU A 1 192 ? 14.201  -44.645 77.045  1.00 81.90  ?  201 LEU A CB   1 
ATOM   3009  C CG   . LEU A 1 192 ? 12.706  -44.581 77.192  1.00 91.16  ?  201 LEU A CG   1 
ATOM   3010  C CD1  . LEU A 1 192 ? 12.135  -45.763 76.473  1.00 106.51 ?  201 LEU A CD1  1 
ATOM   3011  C CD2  . LEU A 1 192 ? 12.329  -44.622 78.651  1.00 75.86  ?  201 LEU A CD2  1 
ATOM   3012  H H    . LEU A 1 192 ? 14.354  -42.366 76.174  1.00 69.25  ?  201 LEU A H    1 
ATOM   3013  H HA   . LEU A 1 192 ? 14.591  -43.372 78.610  1.00 90.21  ?  201 LEU A HA   1 
ATOM   3014  H HB2  . LEU A 1 192 ? 14.407  -44.649 76.098  1.00 98.28  ?  201 LEU A HB2  1 
ATOM   3015  H HB3  . LEU A 1 192 ? 14.505  -45.471 77.452  1.00 98.28  ?  201 LEU A HB3  1 
ATOM   3016  H HG   . LEU A 1 192 ? 12.362  -43.766 76.794  1.00 109.39 ?  201 LEU A HG   1 
ATOM   3017  H HD11 . LEU A 1 192 ? 11.168  -45.744 76.553  1.00 127.82 ?  201 LEU A HD11 1 
ATOM   3018  H HD12 . LEU A 1 192 ? 12.390  -45.717 75.538  1.00 127.82 ?  201 LEU A HD12 1 
ATOM   3019  H HD13 . LEU A 1 192 ? 12.485  -46.575 76.872  1.00 127.82 ?  201 LEU A HD13 1 
ATOM   3020  H HD21 . LEU A 1 192 ? 11.363  -44.581 78.728  1.00 91.03  ?  201 LEU A HD21 1 
ATOM   3021  H HD22 . LEU A 1 192 ? 12.657  -45.449 79.038  1.00 91.03  ?  201 LEU A HD22 1 
ATOM   3022  H HD23 . LEU A 1 192 ? 12.731  -43.863 79.102  1.00 91.03  ?  201 LEU A HD23 1 
ATOM   3023  N N    . GLU A 1 193 ? 17.160  -43.484 76.702  1.00 102.94 ?  202 GLU A N    1 
ATOM   3024  C CA   . GLU A 1 193 ? 18.609  -43.643 76.721  1.00 62.44  ?  202 GLU A CA   1 
ATOM   3025  C C    . GLU A 1 193 ? 19.203  -42.699 77.748  1.00 82.14  ?  202 GLU A C    1 
ATOM   3026  O O    . GLU A 1 193 ? 20.008  -43.093 78.601  1.00 84.75  ?  202 GLU A O    1 
ATOM   3027  C CB   . GLU A 1 193 ? 19.173  -43.361 75.320  1.00 92.36  ?  202 GLU A CB   1 
ATOM   3028  C CG   . GLU A 1 193 ? 20.686  -43.217 75.141  1.00 123.43 ?  202 GLU A CG   1 
ATOM   3029  C CD   . GLU A 1 193 ? 21.464  -44.522 75.302  1.00 138.58 ?  202 GLU A CD   1 
ATOM   3030  O OE1  . GLU A 1 193 ? 20.861  -45.605 75.149  1.00 132.41 ?  202 GLU A OE1  1 
ATOM   3031  O OE2  . GLU A 1 193 ? 22.696  -44.466 75.528  1.00 134.16 -1 202 GLU A OE2  1 
ATOM   3032  H H    . GLU A 1 193 ? 16.842  -43.218 75.949  1.00 123.53 ?  202 GLU A H    1 
ATOM   3033  H HA   . GLU A 1 193 ? 18.834  -44.554 76.969  1.00 74.93  ?  202 GLU A HA   1 
ATOM   3034  H HB2  . GLU A 1 193 ? 18.892  -44.085 74.738  1.00 110.84 ?  202 GLU A HB2  1 
ATOM   3035  H HB3  . GLU A 1 193 ? 18.776  -42.534 75.004  1.00 110.84 ?  202 GLU A HB3  1 
ATOM   3036  H HG2  . GLU A 1 193 ? 20.863  -42.875 74.251  1.00 148.12 ?  202 GLU A HG2  1 
ATOM   3037  H HG3  . GLU A 1 193 ? 21.019  -42.591 75.804  1.00 148.12 ?  202 GLU A HG3  1 
ATOM   3038  N N    . ILE A 1 194 ? 18.712  -41.475 77.774  1.00 55.95  ?  203 ILE A N    1 
ATOM   3039  C CA   . ILE A 1 194 ? 19.222  -40.528 78.738  1.00 41.71  ?  203 ILE A CA   1 
ATOM   3040  C C    . ILE A 1 194 ? 18.956  -40.999 80.146  1.00 54.24  ?  203 ILE A C    1 
ATOM   3041  O O    . ILE A 1 194 ? 19.801  -40.840 81.036  1.00 75.46  ?  203 ILE A O    1 
ATOM   3042  C CB   . ILE A 1 194 ? 18.621  -39.158 78.465  1.00 41.20  ?  203 ILE A CB   1 
ATOM   3043  C CG1  . ILE A 1 194 ? 19.345  -38.548 77.274  1.00 113.71 ?  203 ILE A CG1  1 
ATOM   3044  C CG2  . ILE A 1 194 ? 18.628  -38.362 79.754  1.00 40.18  ?  203 ILE A CG2  1 
ATOM   3045  C CD1  . ILE A 1 194 ? 18.708  -37.345 76.760  1.00 114.05 ?  203 ILE A CD1  1 
ATOM   3046  H H    . ILE A 1 194 ? 18.096  -41.174 77.256  1.00 67.14  ?  203 ILE A H    1 
ATOM   3047  H HA   . ILE A 1 194 ? 20.183  -40.456 78.627  1.00 50.06  ?  203 ILE A HA   1 
ATOM   3048  H HB   . ILE A 1 194 ? 17.695  -39.289 78.208  1.00 49.44  ?  203 ILE A HB   1 
ATOM   3049  H HG12 . ILE A 1 194 ? 20.247  -38.315 77.541  1.00 136.45 ?  203 ILE A HG12 1 
ATOM   3050  H HG13 . ILE A 1 194 ? 19.371  -39.200 76.556  1.00 136.45 ?  203 ILE A HG13 1 
ATOM   3051  H HG21 . ILE A 1 194 ? 18.246  -37.487 79.586  1.00 48.21  ?  203 ILE A HG21 1 
ATOM   3052  H HG22 . ILE A 1 194 ? 18.100  -38.833 80.418  1.00 48.21  ?  203 ILE A HG22 1 
ATOM   3053  H HG23 . ILE A 1 194 ? 19.543  -38.270 80.063  1.00 48.21  ?  203 ILE A HG23 1 
ATOM   3054  H HD11 . ILE A 1 194 ? 19.222  -37.014 76.006  1.00 136.86 ?  203 ILE A HD11 1 
ATOM   3055  H HD12 . ILE A 1 194 ? 17.806  -37.562 76.476  1.00 136.86 ?  203 ILE A HD12 1 
ATOM   3056  H HD13 . ILE A 1 194 ? 18.683  -36.677 77.462  1.00 136.86 ?  203 ILE A HD13 1 
ATOM   3057  N N    . ALA A 1 195 ? 17.751  -41.510 80.390  1.00 42.05  ?  204 ALA A N    1 
ATOM   3058  C CA   . ALA A 1 195 ? 17.406  -41.979 81.730  1.00 57.10  ?  204 ALA A CA   1 
ATOM   3059  C C    . ALA A 1 195 ? 18.305  -43.142 82.124  1.00 57.90  ?  204 ALA A C    1 
ATOM   3060  O O    . ALA A 1 195 ? 18.813  -43.207 83.249  1.00 51.96  ?  204 ALA A O    1 
ATOM   3061  C CB   . ALA A 1 195 ? 15.933  -42.381 81.793  1.00 87.21  ?  204 ALA A CB   1 
ATOM   3062  H H    . ALA A 1 195 ? 17.124  -41.596 79.807  1.00 50.46  ?  204 ALA A H    1 
ATOM   3063  H HA   . ALA A 1 195 ? 17.549  -41.259 82.364  1.00 68.52  ?  204 ALA A HA   1 
ATOM   3064  H HB1  . ALA A 1 195 ? 15.728  -42.688 82.690  1.00 104.65 ?  204 ALA A HB1  1 
ATOM   3065  H HB2  . ALA A 1 195 ? 15.386  -41.610 81.574  1.00 104.65 ?  204 ALA A HB2  1 
ATOM   3066  H HB3  . ALA A 1 195 ? 15.772  -43.093 81.154  1.00 104.65 ?  204 ALA A HB3  1 
ATOM   3067  N N    . SER A 1 196 ? 18.597  -44.013 81.188  1.00 66.75  ?  205 SER A N    1 
ATOM   3068  C CA   . SER A 1 196 ? 19.442  -45.123 81.535  1.00 79.21  ?  205 SER A CA   1 
ATOM   3069  C C    . SER A 1 196 ? 20.809  -44.609 81.919  1.00 102.25 ?  205 SER A C    1 
ATOM   3070  O O    . SER A 1 196 ? 21.418  -45.049 82.903  1.00 54.07  ?  205 SER A O    1 
ATOM   3071  C CB   . SER A 1 196 ? 19.562  -46.063 80.361  1.00 104.36 ?  205 SER A CB   1 
ATOM   3072  O OG   . SER A 1 196 ? 20.443  -47.097 80.713  1.00 118.32 ?  205 SER A OG   1 
ATOM   3073  H H    . SER A 1 196 ? 18.329  -43.987 80.371  1.00 80.10  ?  205 SER A H    1 
ATOM   3074  H HA   . SER A 1 196 ? 19.064  -45.605 82.287  1.00 95.05  ?  205 SER A HA   1 
ATOM   3075  H HB2  . SER A 1 196 ? 18.691  -46.436 80.155  1.00 125.23 ?  205 SER A HB2  1 
ATOM   3076  H HB3  . SER A 1 196 ? 19.916  -45.583 79.596  1.00 125.23 ?  205 SER A HB3  1 
ATOM   3077  H HG   . SER A 1 196 ? 20.526  -47.634 80.073  1.00 141.98 ?  205 SER A HG   1 
ATOM   3078  N N    . CYS A 1 197 ? 21.287  -43.629 81.174  1.00 77.32  ?  206 CYS A N    1 
ATOM   3079  C CA   . CYS A 1 197 ? 22.635  -43.171 81.424  1.00 60.24  ?  206 CYS A CA   1 
ATOM   3080  C C    . CYS A 1 197 ? 22.754  -42.521 82.811  1.00 62.36  ?  206 CYS A C    1 
ATOM   3081  O O    . CYS A 1 197 ? 23.790  -42.671 83.478  1.00 63.14  ?  206 CYS A O    1 
ATOM   3082  C CB   . CYS A 1 197 ? 23.055  -42.249 80.292  1.00 44.06  ?  206 CYS A CB   1 
ATOM   3083  S SG   . CYS A 1 197 ? 23.324  -43.001 78.633  1.00 109.51 ?  206 CYS A SG   1 
ATOM   3084  H H    . CYS A 1 197 ? 20.868  -43.227 80.540  1.00 92.79  ?  206 CYS A H    1 
ATOM   3085  H HA   . CYS A 1 197 ? 23.228  -43.938 81.410  1.00 72.29  ?  206 CYS A HA   1 
ATOM   3086  H HB2  . CYS A 1 197 ? 22.370  -41.570 80.188  1.00 52.88  ?  206 CYS A HB2  1 
ATOM   3087  H HB3  . CYS A 1 197 ? 23.888  -41.822 80.548  1.00 52.88  ?  206 CYS A HB3  1 
ATOM   3088  H HG   . CYS A 1 197 ? 22.303  -43.514 78.267  1.00 131.42 ?  206 CYS A HG   1 
ATOM   3089  N N    . LEU A 1 198 ? 21.697  -41.853 83.297  1.00 54.92  ?  207 LEU A N    1 
ATOM   3090  C CA   . LEU A 1 198 ? 21.747  -41.334 84.660  1.00 46.29  ?  207 LEU A CA   1 
ATOM   3091  C C    . LEU A 1 198 ? 21.512  -42.381 85.708  1.00 55.26  ?  207 LEU A C    1 
ATOM   3092  O O    . LEU A 1 198 ? 21.805  -42.125 86.875  1.00 55.87  ?  207 LEU A O    1 
ATOM   3093  C CB   . LEU A 1 198 ? 20.733  -40.234 84.886  1.00 76.19  ?  207 LEU A CB   1 
ATOM   3094  C CG   . LEU A 1 198 ? 20.810  -38.981 84.031  1.00 95.24  ?  207 LEU A CG   1 
ATOM   3095  C CD1  . LEU A 1 198 ? 19.638  -38.113 84.436  1.00 41.94  ?  207 LEU A CD1  1 
ATOM   3096  C CD2  . LEU A 1 198 ? 22.086  -38.238 84.125  1.00 117.90 ?  207 LEU A CD2  1 
ATOM   3097  H H    . LEU A 1 198 ? 20.967  -41.694 82.871  1.00 65.91  ?  207 LEU A H    1 
ATOM   3098  H HA   . LEU A 1 198 ? 22.628  -40.957 84.815  1.00 55.55  ?  207 LEU A HA   1 
ATOM   3099  H HB2  . LEU A 1 198 ? 19.851  -40.614 84.748  1.00 91.43  ?  207 LEU A HB2  1 
ATOM   3100  H HB3  . LEU A 1 198 ? 20.810  -39.947 85.810  1.00 91.43  ?  207 LEU A HB3  1 
ATOM   3101  H HG   . LEU A 1 198 ? 20.683  -39.231 83.102  1.00 114.28 ?  207 LEU A HG   1 
ATOM   3102  H HD11 . LEU A 1 198 ? 19.651  -37.299 83.909  1.00 50.32  ?  207 LEU A HD11 1 
ATOM   3103  H HD12 . LEU A 1 198 ? 18.814  -38.600 84.272  1.00 50.32  ?  207 LEU A HD12 1 
ATOM   3104  H HD13 . LEU A 1 198 ? 19.714  -37.900 85.379  1.00 50.32  ?  207 LEU A HD13 1 
ATOM   3105  H HD21 . LEU A 1 198 ? 22.041  -37.460 83.548  1.00 141.48 ?  207 LEU A HD21 1 
ATOM   3106  H HD22 . LEU A 1 198 ? 22.223  -37.962 85.045  1.00 141.48 ?  207 LEU A HD22 1 
ATOM   3107  H HD23 . LEU A 1 198 ? 22.810  -38.819 83.842  1.00 141.48 ?  207 LEU A HD23 1 
ATOM   3108  N N    . GLU A 1 199 ? 20.871  -43.497 85.372  1.00 53.34  ?  208 GLU A N    1 
ATOM   3109  C CA   . GLU A 1 199 ? 20.800  -44.566 86.360  1.00 76.50  ?  208 GLU A CA   1 
ATOM   3110  C C    . GLU A 1 199 ? 22.205  -45.120 86.558  1.00 70.51  ?  208 GLU A C    1 
ATOM   3111  O O    . GLU A 1 199 ? 22.700  -45.242 87.687  1.00 60.56  ?  208 GLU A O    1 
ATOM   3112  C CB   . GLU A 1 199 ? 19.804  -45.626 85.891  1.00 97.67  ?  208 GLU A CB   1 
ATOM   3113  H H    . GLU A 1 199 ? 20.488  -43.656 84.618  1.00 64.00  ?  208 GLU A H    1 
ATOM   3114  H HA   . GLU A 1 199 ? 20.489  -44.205 87.205  1.00 91.80  ?  208 GLU A HA   1 
ATOM   3115  N N    . LYS A 1 200 ? 22.929  -45.220 85.449  1.00 60.21  ?  209 LYS A N    1 
ATOM   3116  C CA   . LYS A 1 200 ? 24.325  -45.593 85.491  1.00 53.47  ?  209 LYS A CA   1 
ATOM   3117  C C    . LYS A 1 200 ? 25.114  -44.589 86.302  1.00 90.35  ?  209 LYS A C    1 
ATOM   3118  O O    . LYS A 1 200 ? 25.863  -44.937 87.218  1.00 68.16  ?  209 LYS A O    1 
ATOM   3119  C CB   . LYS A 1 200 ? 24.895  -45.643 84.061  1.00 66.71  ?  209 LYS A CB   1 
ATOM   3120  C CG   . LYS A 1 200 ? 24.286  -46.772 83.144  1.00 87.01  ?  209 LYS A CG   1 
ATOM   3121  H H    . LYS A 1 200 ? 22.628  -45.074 84.656  1.00 72.25  ?  209 LYS A H    1 
ATOM   3122  H HA   . LYS A 1 200 ? 24.420  -46.468 85.897  1.00 64.16  ?  209 LYS A HA   1 
ATOM   3123  H HB2  . LYS A 1 200 ? 24.724  -44.791 83.630  1.00 80.05  ?  209 LYS A HB2  1 
ATOM   3124  H HB3  . LYS A 1 200 ? 25.852  -45.794 84.115  1.00 80.05  ?  209 LYS A HB3  1 
ATOM   3125  H HG2  . LYS A 1 200 ? 24.674  -47.625 83.393  1.00 104.41 ?  209 LYS A HG2  1 
ATOM   3126  H HG3  . LYS A 1 200 ? 23.324  -46.796 83.269  1.00 104.41 ?  209 LYS A HG3  1 
ATOM   3127  N N    . ALA A 1 201 ? 24.888  -43.321 86.052  1.00 88.25  ?  210 ALA A N    1 
ATOM   3128  C CA   . ALA A 1 201 ? 25.700  -42.376 86.784  1.00 80.31  ?  210 ALA A CA   1 
ATOM   3129  C C    . ALA A 1 201 ? 25.496  -42.517 88.277  1.00 78.02  ?  210 ALA A C    1 
ATOM   3130  O O    . ALA A 1 201 ? 26.438  -42.292 89.043  1.00 55.36  ?  210 ALA A O    1 
ATOM   3131  C CB   . ALA A 1 201 ? 25.386  -40.974 86.323  1.00 81.82  ?  210 ALA A CB   1 
ATOM   3132  H H    . ALA A 1 201 ? 24.312  -42.994 85.503  1.00 105.90 ?  210 ALA A H    1 
ATOM   3133  H HA   . ALA A 1 201 ? 26.634  -42.551 86.593  1.00 96.38  ?  210 ALA A HA   1 
ATOM   3134  H HB1  . ALA A 1 201 ? 25.935  -40.348 86.820  1.00 98.19  ?  210 ALA A HB1  1 
ATOM   3135  H HB2  . ALA A 1 201 ? 25.578  -40.903 85.374  1.00 98.19  ?  210 ALA A HB2  1 
ATOM   3136  H HB3  . ALA A 1 201 ? 24.447  -40.791 86.484  1.00 98.19  ?  210 ALA A HB3  1 
ATOM   3137  N N    . LEU A 1 202 ? 24.315  -42.966 88.701  1.00 68.80  ?  211 LEU A N    1 
ATOM   3138  C CA   . LEU A 1 202 ? 24.065  -43.137 90.118  1.00 57.14  ?  211 LEU A CA   1 
ATOM   3139  C C    . LEU A 1 202 ? 24.898  -44.283 90.701  1.00 67.71  ?  211 LEU A C    1 
ATOM   3140  O O    . LEU A 1 202 ? 25.376  -44.200 91.831  1.00 83.67  ?  211 LEU A O    1 
ATOM   3141  C CB   . LEU A 1 202 ? 22.565  -43.359 90.314  1.00 68.81  ?  211 LEU A CB   1 
ATOM   3142  C CG   . LEU A 1 202 ? 22.144  -43.683 91.748  1.00 44.34  ?  211 LEU A CG   1 
ATOM   3143  C CD1  . LEU A 1 202 ? 22.623  -42.538 92.656  1.00 53.66  ?  211 LEU A CD1  1 
ATOM   3144  C CD2  . LEU A 1 202 ? 20.705  -43.827 91.866  1.00 107.47 ?  211 LEU A CD2  1 
ATOM   3145  H H    . LEU A 1 202 ? 23.654  -43.173 88.192  1.00 82.56  ?  211 LEU A H    1 
ATOM   3146  H HA   . LEU A 1 202 ? 24.311  -42.322 90.583  1.00 68.56  ?  211 LEU A HA   1 
ATOM   3147  H HB2  . LEU A 1 202 ? 22.096  -42.553 90.046  1.00 82.57  ?  211 LEU A HB2  1 
ATOM   3148  H HB3  . LEU A 1 202 ? 22.287  -44.100 89.752  1.00 82.57  ?  211 LEU A HB3  1 
ATOM   3149  H HG   . LEU A 1 202 ? 22.566  -44.508 92.037  1.00 53.21  ?  211 LEU A HG   1 
ATOM   3150  H HD11 . LEU A 1 202 ? 22.362  -42.730 93.570  1.00 64.39  ?  211 LEU A HD11 1 
ATOM   3151  H HD12 . LEU A 1 202 ? 23.588  -42.469 92.594  1.00 64.39  ?  211 LEU A HD12 1 
ATOM   3152  H HD13 . LEU A 1 202 ? 22.212  -41.710 92.361  1.00 64.39  ?  211 LEU A HD13 1 
ATOM   3153  H HD21 . LEU A 1 202 ? 20.483  -44.031 92.788  1.00 128.97 ?  211 LEU A HD21 1 
ATOM   3154  H HD22 . LEU A 1 202 ? 20.282  -42.996 91.600  1.00 128.97 ?  211 LEU A HD22 1 
ATOM   3155  H HD23 . LEU A 1 202 ? 20.412  -44.548 91.287  1.00 128.97 ?  211 LEU A HD23 1 
ATOM   3156  N N    . GLN A 1 203 ? 25.063  -45.367 89.952  1.00 74.95  ?  212 GLN A N    1 
ATOM   3157  C CA   . GLN A 1 203 ? 25.796  -46.512 90.479  1.00 83.30  ?  212 GLN A CA   1 
ATOM   3158  C C    . GLN A 1 203 ? 27.255  -46.155 90.608  1.00 73.77  ?  212 GLN A C    1 
ATOM   3159  O O    . GLN A 1 203 ? 27.958  -46.635 91.511  1.00 70.41  ?  212 GLN A O    1 
ATOM   3160  C CB   . GLN A 1 203 ? 25.634  -47.755 89.579  1.00 89.07  ?  212 GLN A CB   1 
ATOM   3161  C CG   . GLN A 1 203 ? 24.136  -48.170 89.288  1.00 79.81  ?  212 GLN A CG   1 
ATOM   3162  C CD   . GLN A 1 203 ? 23.226  -48.192 90.540  1.00 88.66  ?  212 GLN A CD   1 
ATOM   3163  O OE1  . GLN A 1 203 ? 23.547  -48.800 91.582  1.00 89.53  ?  212 GLN A OE1  1 
ATOM   3164  N NE2  . GLN A 1 203 ? 22.091  -47.513 90.433  1.00 112.22 ?  212 GLN A NE2  1 
ATOM   3165  H H    . GLN A 1 203 ? 24.767  -45.465 89.151  1.00 89.94  ?  212 GLN A H    1 
ATOM   3166  H HA   . GLN A 1 203 ? 25.457  -46.730 91.361  1.00 99.96  ?  212 GLN A HA   1 
ATOM   3167  H HB2  . GLN A 1 203 ? 26.060  -47.577 88.726  1.00 106.89 ?  212 GLN A HB2  1 
ATOM   3168  H HB3  . GLN A 1 203 ? 26.068  -48.508 90.010  1.00 106.89 ?  212 GLN A HB3  1 
ATOM   3169  H HG2  . GLN A 1 203 ? 23.756  -47.538 88.658  1.00 95.77  ?  212 GLN A HG2  1 
ATOM   3170  H HG3  . GLN A 1 203 ? 24.130  -49.060 88.902  1.00 95.77  ?  212 GLN A HG3  1 
ATOM   3171  H HE21 . GLN A 1 203 ? 21.905  -47.099 89.703  1.00 134.66 ?  212 GLN A HE21 1 
ATOM   3172  H HE22 . GLN A 1 203 ? 21.542  -47.487 91.095  1.00 134.66 ?  212 GLN A HE22 1 
ATOM   3173  N N    . VAL A 1 204 ? 27.717  -45.272 89.740  1.00 75.99  ?  213 VAL A N    1 
ATOM   3174  C CA   . VAL A 1 204 ? 29.076  -44.809 89.880  1.00 47.65  ?  213 VAL A CA   1 
ATOM   3175  C C    . VAL A 1 204 ? 29.232  -43.971 91.152  1.00 47.83  ?  213 VAL A C    1 
ATOM   3176  O O    . VAL A 1 204 ? 30.169  -44.156 91.932  1.00 62.29  ?  213 VAL A O    1 
ATOM   3177  C CB   . VAL A 1 204 ? 29.451  -43.998 88.623  1.00 60.14  ?  213 VAL A CB   1 
ATOM   3178  C CG1  . VAL A 1 204 ? 30.782  -43.179 88.850  1.00 45.12  ?  213 VAL A CG1  1 
ATOM   3179  C CG2  . VAL A 1 204 ? 29.473  -44.924 87.387  1.00 53.11  ?  213 VAL A CG2  1 
ATOM   3180  H H    . VAL A 1 204 ? 27.277  -44.937 89.081  1.00 91.19  ?  213 VAL A H    1 
ATOM   3181  H HA   . VAL A 1 204 ? 29.672  -45.572 89.941  1.00 57.18  ?  213 VAL A HA   1 
ATOM   3182  H HB   . VAL A 1 204 ? 28.747  -43.348 88.471  1.00 72.17  ?  213 VAL A HB   1 
ATOM   3183  H HG11 . VAL A 1 204 ? 30.988  -42.682 88.043  1.00 54.14  ?  213 VAL A HG11 1 
ATOM   3184  H HG12 . VAL A 1 204 ? 30.653  -42.567 89.592  1.00 54.14  ?  213 VAL A HG12 1 
ATOM   3185  H HG13 . VAL A 1 204 ? 31.502  -43.796 89.051  1.00 54.14  ?  213 VAL A HG13 1 
ATOM   3186  H HG21 . VAL A 1 204 ? 29.710  -44.401 86.605  1.00 63.73  ?  213 VAL A HG21 1 
ATOM   3187  H HG22 . VAL A 1 204 ? 30.130  -45.624 87.529  1.00 63.73  ?  213 VAL A HG22 1 
ATOM   3188  H HG23 . VAL A 1 204 ? 28.593  -45.314 87.269  1.00 63.73  ?  213 VAL A HG23 1 
ATOM   3189  N N    . PHE A 1 205 ? 28.282  -43.107 91.424  1.00 62.87  ?  214 PHE A N    1 
ATOM   3190  C CA   . PHE A 1 205 ? 28.369  -42.310 92.615  1.00 59.13  ?  214 PHE A CA   1 
ATOM   3191  C C    . PHE A 1 205 ? 28.435  -43.202 93.861  1.00 50.38  ?  214 PHE A C    1 
ATOM   3192  O O    . PHE A 1 205 ? 29.139  -42.874 94.821  1.00 52.71  ?  214 PHE A O    1 
ATOM   3193  C CB   . PHE A 1 205 ? 27.158  -41.382 92.503  1.00 119.73 ?  214 PHE A CB   1 
ATOM   3194  C CG   . PHE A 1 205 ? 27.112  -40.231 93.466  1.00 69.40  ?  214 PHE A CG   1 
ATOM   3195  C CD1  . PHE A 1 205 ? 28.150  -39.926 94.318  1.00 56.17  ?  214 PHE A CD1  1 
ATOM   3196  C CD2  . PHE A 1 205 ? 25.970  -39.426 93.490  1.00 56.68  ?  214 PHE A CD2  1 
ATOM   3197  C CE1  . PHE A 1 205 ? 28.019  -38.864 95.205  1.00 75.75  ?  214 PHE A CE1  1 
ATOM   3198  C CE2  . PHE A 1 205 ? 25.861  -38.300 94.400  1.00 44.25  ?  214 PHE A CE2  1 
ATOM   3199  C CZ   . PHE A 1 205 ? 26.833  -38.056 95.228  1.00 41.10  ?  214 PHE A CZ   1 
ATOM   3200  H H    . PHE A 1 205 ? 27.585  -42.965 90.940  1.00 75.44  ?  214 PHE A H    1 
ATOM   3201  H HA   . PHE A 1 205 ? 29.173  -41.769 92.583  1.00 70.95  ?  214 PHE A HA   1 
ATOM   3202  H HB2  . PHE A 1 205 ? 27.142  -41.009 91.608  1.00 143.68 ?  214 PHE A HB2  1 
ATOM   3203  H HB3  . PHE A 1 205 ? 26.356  -41.909 92.646  1.00 143.68 ?  214 PHE A HB3  1 
ATOM   3204  H HD1  . PHE A 1 205 ? 28.915  -40.455 94.332  1.00 67.40  ?  214 PHE A HD1  1 
ATOM   3205  H HD2  . PHE A 1 205 ? 25.265  -39.617 92.914  1.00 68.02  ?  214 PHE A HD2  1 
ATOM   3206  H HE1  . PHE A 1 205 ? 28.718  -38.664 95.784  1.00 90.90  ?  214 PHE A HE1  1 
ATOM   3207  H HE2  . PHE A 1 205 ? 25.089  -37.781 94.415  1.00 53.10  ?  214 PHE A HE2  1 
ATOM   3208  H HZ   . PHE A 1 205 ? 26.776  -37.332 95.809  1.00 49.32  ?  214 PHE A HZ   1 
ATOM   3209  N N    . HIS A 1 206 ? 27.916  -44.414 93.796  1.00 62.81  ?  215 HIS A N    1 
ATOM   3210  C CA   . HIS A 1 206 ? 27.979  -45.281 94.962  1.00 85.73  ?  215 HIS A CA   1 
ATOM   3211  C C    . HIS A 1 206 ? 29.415  -45.558 95.343  1.00 66.40  ?  215 HIS A C    1 
ATOM   3212  O O    . HIS A 1 206 ? 29.709  -45.757 96.523  1.00 66.93  ?  215 HIS A O    1 
ATOM   3213  C CB   . HIS A 1 206 ? 27.251  -46.623 94.690  1.00 88.09  ?  215 HIS A CB   1 
ATOM   3214  C CG   . HIS A 1 206 ? 25.761  -46.526 94.758  1.00 106.38 ?  215 HIS A CG   1 
ATOM   3215  N ND1  . HIS A 1 206 ? 25.034  -45.631 93.999  1.00 106.31 ?  215 HIS A ND1  1 
ATOM   3216  C CD2  . HIS A 1 206 ? 24.857  -47.225 95.481  1.00 104.99 ?  215 HIS A CD2  1 
ATOM   3217  C CE1  . HIS A 1 206 ? 23.750  -45.772 94.270  1.00 110.45 ?  215 HIS A CE1  1 
ATOM   3218  N NE2  . HIS A 1 206 ? 23.617  -46.735 95.162  1.00 113.17 ?  215 HIS A NE2  1 
ATOM   3219  H H    . HIS A 1 206 ? 27.530  -44.755 93.107  1.00 75.37  ?  215 HIS A H    1 
ATOM   3220  H HA   . HIS A 1 206 ? 27.544  -44.844 95.711  1.00 102.87 ?  215 HIS A HA   1 
ATOM   3221  H HB2  . HIS A 1 206 ? 27.488  -46.932 93.801  1.00 105.71 ?  215 HIS A HB2  1 
ATOM   3222  H HB3  . HIS A 1 206 ? 27.537  -47.273 95.350  1.00 105.71 ?  215 HIS A HB3  1 
ATOM   3223  H HD1  . HIS A 1 206 ? 25.367  -45.061 93.449  1.00 127.58 ?  215 HIS A HD1  1 
ATOM   3224  H HD2  . HIS A 1 206 ? 25.043  -47.905 96.089  1.00 125.99 ?  215 HIS A HD2  1 
ATOM   3225  H HE1  . HIS A 1 206 ? 23.057  -45.283 93.888  1.00 132.54 ?  215 HIS A HE1  1 
ATOM   3226  N N    . GLN A 1 207 ? 30.327  -45.452 94.386  1.00 73.70  ?  216 GLN A N    1 
ATOM   3227  C CA   . GLN A 1 207 ? 31.729  -45.772 94.643  1.00 58.45  ?  216 GLN A CA   1 
ATOM   3228  C C    . GLN A 1 207 ? 32.359  -44.864 95.701  1.00 60.11  ?  216 GLN A C    1 
ATOM   3229  O O    . GLN A 1 207 ? 33.388  -45.209 96.300  1.00 57.66  ?  216 GLN A O    1 
ATOM   3230  C CB   . GLN A 1 207 ? 32.528  -45.676 93.335  1.00 66.50  ?  216 GLN A CB   1 
ATOM   3231  C CG   . GLN A 1 207 ? 31.999  -46.640 92.264  1.00 83.32  ?  216 GLN A CG   1 
ATOM   3232  C CD   . GLN A 1 207 ? 32.824  -46.705 90.955  1.00 95.07  ?  216 GLN A CD   1 
ATOM   3233  O OE1  . GLN A 1 207 ? 34.059  -46.587 90.965  1.00 78.01  ?  216 GLN A OE1  1 
ATOM   3234  N NE2  . GLN A 1 207 ? 32.136  -46.930 89.832  1.00 121.54 ?  216 GLN A NE2  1 
ATOM   3235  H H    . GLN A 1 207 ? 30.164  -45.199 93.581  1.00 88.44  ?  216 GLN A H    1 
ATOM   3236  H HA   . GLN A 1 207 ? 31.788  -46.686 94.962  1.00 70.14  ?  216 GLN A HA   1 
ATOM   3237  H HB2  . GLN A 1 207 ? 32.462  -44.772 92.988  1.00 79.80  ?  216 GLN A HB2  1 
ATOM   3238  H HB3  . GLN A 1 207 ? 33.455  -45.899 93.512  1.00 79.80  ?  216 GLN A HB3  1 
ATOM   3239  H HG2  . GLN A 1 207 ? 31.980  -47.534 92.639  1.00 99.99  ?  216 GLN A HG2  1 
ATOM   3240  H HG3  . GLN A 1 207 ? 31.099  -46.370 92.026  1.00 99.99  ?  216 GLN A HG3  1 
ATOM   3241  H HE21 . GLN A 1 207 ? 31.282  -47.030 89.863  1.00 145.85 ?  216 GLN A HE21 1 
ATOM   3242  H HE22 . GLN A 1 207 ? 32.546  -46.975 89.078  1.00 145.85 ?  216 GLN A HE22 1 
ATOM   3243  N N    . ILE A 1 208 ? 31.687  -43.774 96.031  1.00 75.68  ?  217 ILE A N    1 
ATOM   3244  C CA   . ILE A 1 208 ? 32.202  -42.777 96.950  1.00 69.47  ?  217 ILE A CA   1 
ATOM   3245  C C    . ILE A 1 208 ? 32.655  -43.397 98.247  1.00 66.18  ?  217 ILE A C    1 
ATOM   3246  O O    . ILE A 1 208 ? 33.670  -42.973 98.817  1.00 72.07  ?  217 ILE A O    1 
ATOM   3247  C CB   . ILE A 1 208 ? 31.075  -41.742 97.171  1.00 78.26  ?  217 ILE A CB   1 
ATOM   3248  C CG1  . ILE A 1 208 ? 31.532  -40.628 98.044  1.00 69.63  ?  217 ILE A CG1  1 
ATOM   3249  C CG2  . ILE A 1 208 ? 29.840  -42.349 97.796  1.00 95.92  ?  217 ILE A CG2  1 
ATOM   3250  C CD1  . ILE A 1 208 ? 32.329  -39.722 97.213  1.00 71.15  ?  217 ILE A CD1  1 
ATOM   3251  H H    . ILE A 1 208 ? 30.906  -43.585 95.726  1.00 90.81  ?  217 ILE A H    1 
ATOM   3252  H HA   . ILE A 1 208 ? 32.959  -42.325 96.545  1.00 83.36  ?  217 ILE A HA   1 
ATOM   3253  H HB   . ILE A 1 208 ? 30.830  -41.372 96.308  1.00 93.92  ?  217 ILE A HB   1 
ATOM   3254  H HG12 . ILE A 1 208 ? 30.767  -40.145 98.395  1.00 83.55  ?  217 ILE A HG12 1 
ATOM   3255  H HG13 . ILE A 1 208 ? 32.087  -40.972 98.760  1.00 83.55  ?  217 ILE A HG13 1 
ATOM   3256  H HG21 . ILE A 1 208 ? 29.171  -41.655 97.909  1.00 115.10 ?  217 ILE A HG21 1 
ATOM   3257  H HG22 . ILE A 1 208 ? 29.499  -43.044 97.211  1.00 115.10 ?  217 ILE A HG22 1 
ATOM   3258  H HG23 . ILE A 1 208 ? 30.075  -42.726 98.658  1.00 115.10 ?  217 ILE A HG23 1 
ATOM   3259  H HD11 . ILE A 1 208 ? 32.640  -38.984 97.760  1.00 85.38  ?  217 ILE A HD11 1 
ATOM   3260  H HD12 . ILE A 1 208 ? 33.087  -40.209 96.853  1.00 85.38  ?  217 ILE A HD12 1 
ATOM   3261  H HD13 . ILE A 1 208 ? 31.776  -39.388 96.490  1.00 85.38  ?  217 ILE A HD13 1 
ATOM   3262  N N    . HIS A 1 209 ? 31.955  -44.442 98.698  1.00 56.08  ?  218 HIS A N    1 
ATOM   3263  C CA   . HIS A 1 209 ? 32.097  -44.940 100.061 1.00 53.65  ?  218 HIS A CA   1 
ATOM   3264  C C    . HIS A 1 209 ? 33.393  -45.681 100.268 1.00 80.48  ?  218 HIS A C    1 
ATOM   3265  O O    . HIS A 1 209 ? 33.859  -45.776 101.408 1.00 57.16  ?  218 HIS A O    1 
ATOM   3266  C CB   . HIS A 1 209 ? 30.917  -45.838 100.396 1.00 98.88  ?  218 HIS A CB   1 
ATOM   3267  C CG   . HIS A 1 209 ? 29.658  -45.073 100.576 1.00 78.16  ?  218 HIS A CG   1 
ATOM   3268  N ND1  . HIS A 1 209 ? 29.456  -44.212 101.639 1.00 64.66  ?  218 HIS A ND1  1 
ATOM   3269  C CD2  . HIS A 1 209 ? 28.583  -44.937 99.765  1.00 77.18  ?  218 HIS A CD2  1 
ATOM   3270  C CE1  . HIS A 1 209 ? 28.278  -43.622 101.498 1.00 69.35  ?  218 HIS A CE1  1 
ATOM   3271  N NE2  . HIS A 1 209 ? 27.726  -44.051 100.373 1.00 62.31  ?  218 HIS A NE2  1 
ATOM   3272  H H    . HIS A 1 209 ? 31.388  -44.882 98.225  1.00 67.30  ?  218 HIS A H    1 
ATOM   3273  H HA   . HIS A 1 209 ? 32.083  -44.187 100.673 1.00 64.37  ?  218 HIS A HA   1 
ATOM   3274  H HB2  . HIS A 1 209 ? 30.785  -46.471 99.673  1.00 118.65 ?  218 HIS A HB2  1 
ATOM   3275  H HB3  . HIS A 1 209 ? 31.103  -46.310 101.223 1.00 118.65 ?  218 HIS A HB3  1 
ATOM   3276  H HD2  . HIS A 1 209 ? 28.436  -45.386 98.965  1.00 92.61  ?  218 HIS A HD2  1 
ATOM   3277  H HE1  . HIS A 1 209 ? 27.898  -43.017 102.094 1.00 83.22  ?  218 HIS A HE1  1 
ATOM   3278  H HE2  . HIS A 1 209 ? 26.959  -43.810 100.069 1.00 74.77  ?  218 HIS A HE2  1 
ATOM   3279  N N    . ASP A 1 210 ? 33.956  -46.256 99.204  1.00 54.10  ?  219 ASP A N    1 
ATOM   3280  C CA   . ASP A 1 210 ? 35.214  -46.978 99.342  1.00 68.16  ?  219 ASP A CA   1 
ATOM   3281  C C    . ASP A 1 210 ? 36.435  -46.082 99.402  1.00 71.08  ?  219 ASP A C    1 
ATOM   3282  O O    . ASP A 1 210 ? 37.508  -46.566 99.773  1.00 84.56  ?  219 ASP A O    1 
ATOM   3283  C CB   . ASP A 1 210 ? 35.369  -47.930 98.183  1.00 93.05  ?  219 ASP A CB   1 
ATOM   3284  C CG   . ASP A 1 210 ? 34.260  -48.909 98.115  1.00 85.82  ?  219 ASP A CG   1 
ATOM   3285  O OD1  . ASP A 1 210 ? 33.780  -49.316 99.198  1.00 59.74  ?  219 ASP A OD1  1 
ATOM   3286  O OD2  . ASP A 1 210 ? 33.870  -49.263 96.985  1.00 67.64  -1 219 ASP A OD2  1 
ATOM   3287  H H    . ASP A 1 210 ? 33.633  -46.243 98.407  1.00 64.92  ?  219 ASP A H    1 
ATOM   3288  H HA   . ASP A 1 210 ? 35.188  -47.502 100.158 1.00 81.80  ?  219 ASP A HA   1 
ATOM   3289  H HB2  . ASP A 1 210 ? 35.378  -47.425 97.355  1.00 111.66 ?  219 ASP A HB2  1 
ATOM   3290  H HB3  . ASP A 1 210 ? 36.200  -48.421 98.284  1.00 111.66 ?  219 ASP A HB3  1 
ATOM   3291  N N    . HIS A 1 211 ? 36.294  -44.788 99.073  1.00 51.68  ?  220 HIS A N    1 
ATOM   3292  C CA   . HIS A 1 211 ? 37.440  -43.964 98.790  1.00 82.03  ?  220 HIS A CA   1 
ATOM   3293  C C    . HIS A 1 211 ? 37.396  -42.687 99.576  1.00 94.14  ?  220 HIS A C    1 
ATOM   3294  O O    . HIS A 1 211 ? 38.221  -41.816 99.331  1.00 63.89  ?  220 HIS A O    1 
ATOM   3295  C CB   . HIS A 1 211 ? 37.517  -43.599 97.308  1.00 48.67  ?  220 HIS A CB   1 
ATOM   3296  C CG   . HIS A 1 211 ? 37.549  -44.761 96.379  1.00 90.45  ?  220 HIS A CG   1 
ATOM   3297  N ND1  . HIS A 1 211 ? 36.569  -45.002 95.439  1.00 136.28 ?  220 HIS A ND1  1 
ATOM   3298  C CD2  . HIS A 1 211 ? 38.454  -45.741 96.236  1.00 52.06  ?  220 HIS A CD2  1 
ATOM   3299  C CE1  . HIS A 1 211 ? 36.891  -46.069 94.739  1.00 51.00  ?  220 HIS A CE1  1 
ATOM   3300  N NE2  . HIS A 1 211 ? 38.022  -46.547 95.216  1.00 141.99 ?  220 HIS A NE2  1 
ATOM   3301  H H    . HIS A 1 211 ? 35.540  -44.379 99.012  1.00 62.02  ?  220 HIS A H    1 
ATOM   3302  H HA   . HIS A 1 211 ? 38.248  -44.444 99.029  1.00 98.43  ?  220 HIS A HA   1 
ATOM   3303  H HB2  . HIS A 1 211 ? 36.741  -43.063 97.081  1.00 58.41  ?  220 HIS A HB2  1 
ATOM   3304  H HB3  . HIS A 1 211 ? 38.324  -43.082 97.159  1.00 58.41  ?  220 HIS A HB3  1 
ATOM   3305  H HD2  . HIS A 1 211 ? 39.234  -45.848 96.731  1.00 62.47  ?  220 HIS A HD2  1 
ATOM   3306  H HE1  . HIS A 1 211 ? 36.386  -46.445 94.055  1.00 61.20  ?  220 HIS A HE1  1 
ATOM   3307  N N    . VAL A 1 212 ? 36.417  -42.513 100.447 1.00 82.06  ?  221 VAL A N    1 
ATOM   3308  C CA   . VAL A 1 212 ? 36.395  -41.370 101.340 1.00 48.92  ?  221 VAL A CA   1 
ATOM   3309  C C    . VAL A 1 212 ? 35.881  -41.855 102.678 1.00 51.14  ?  221 VAL A C    1 
ATOM   3310  O O    . VAL A 1 212 ? 34.987  -42.706 102.724 1.00 106.35 ?  221 VAL A O    1 
ATOM   3311  C CB   . VAL A 1 212 ? 35.509  -40.222 100.806 1.00 59.48  ?  221 VAL A CB   1 
ATOM   3312  C CG1  . VAL A 1 212 ? 35.671  -39.040 101.673 1.00 60.23  ?  221 VAL A CG1  1 
ATOM   3313  C CG2  . VAL A 1 212 ? 35.843  -39.827 99.372  1.00 44.87  ?  221 VAL A CG2  1 
ATOM   3314  H H    . VAL A 1 212 ? 35.748  -43.046 100.540 1.00 98.47  ?  221 VAL A H    1 
ATOM   3315  H HA   . VAL A 1 212 ? 37.297  -41.033 101.459 1.00 58.71  ?  221 VAL A HA   1 
ATOM   3316  H HB   . VAL A 1 212 ? 34.578  -40.495 100.837 1.00 71.38  ?  221 VAL A HB   1 
ATOM   3317  H HG11 . VAL A 1 212 ? 35.113  -38.322 101.335 1.00 72.27  ?  221 VAL A HG11 1 
ATOM   3318  H HG12 . VAL A 1 212 ? 35.401  -39.271 102.576 1.00 72.27  ?  221 VAL A HG12 1 
ATOM   3319  H HG13 . VAL A 1 212 ? 36.602  -38.768 101.665 1.00 72.27  ?  221 VAL A HG13 1 
ATOM   3320  H HG21 . VAL A 1 212 ? 35.256  -39.106 99.098  1.00 53.84  ?  221 VAL A HG21 1 
ATOM   3321  H HG22 . VAL A 1 212 ? 36.767  -39.535 99.333  1.00 53.84  ?  221 VAL A HG22 1 
ATOM   3322  H HG23 . VAL A 1 212 ? 35.715  -40.597 98.795  1.00 53.84  ?  221 VAL A HG23 1 
ATOM   3323  N N    . ASN A 1 213 ? 36.449  -41.336 103.765 1.00 76.59  ?  222 ASN A N    1 
ATOM   3324  C CA   . ASN A 1 213 ? 35.952  -41.594 105.105 1.00 90.29  ?  222 ASN A CA   1 
ATOM   3325  C C    . ASN A 1 213 ? 35.473  -40.281 105.723 1.00 80.15  ?  222 ASN A C    1 
ATOM   3326  O O    . ASN A 1 213 ? 35.855  -39.214 105.250 1.00 66.95  ?  222 ASN A O    1 
ATOM   3327  C CB   . ASN A 1 213 ? 37.026  -42.308 105.948 1.00 108.43 ?  222 ASN A CB   1 
ATOM   3328  C CG   . ASN A 1 213 ? 37.670  -41.432 107.017 1.00 114.11 ?  222 ASN A CG   1 
ATOM   3329  O OD1  . ASN A 1 213 ? 38.635  -40.716 106.761 1.00 156.52 ?  222 ASN A OD1  1 
ATOM   3330  N ND2  . ASN A 1 213 ? 37.182  -41.566 108.250 1.00 137.63 ?  222 ASN A ND2  1 
ATOM   3331  H H    . ASN A 1 213 ? 37.137  -40.822 103.747 1.00 91.91  ?  222 ASN A H    1 
ATOM   3332  H HA   . ASN A 1 213 ? 35.186  -42.186 105.043 1.00 108.35 ?  222 ASN A HA   1 
ATOM   3333  H HB2  . ASN A 1 213 ? 36.617  -43.065 106.396 1.00 130.12 ?  222 ASN A HB2  1 
ATOM   3334  H HB3  . ASN A 1 213 ? 37.730  -42.618 105.358 1.00 130.12 ?  222 ASN A HB3  1 
ATOM   3335  H HD21 . ASN A 1 213 ? 37.507  -41.097 108.894 1.00 165.16 ?  222 ASN A HD21 1 
ATOM   3336  H HD22 . ASN A 1 213 ? 36.543  -42.121 108.402 1.00 165.16 ?  222 ASN A HD22 1 
ATOM   3337  N N    . PRO A 1 214 ? 34.502  -40.315 106.624 1.00 80.50  ?  223 PRO A N    1 
ATOM   3338  C CA   . PRO A 1 214 ? 33.970  -39.046 107.175 1.00 84.20  ?  223 PRO A CA   1 
ATOM   3339  C C    . PRO A 1 214 ? 34.941  -38.115 107.918 1.00 68.35  ?  223 PRO A C    1 
ATOM   3340  O O    . PRO A 1 214 ? 34.947  -36.904 107.657 1.00 114.10 ?  223 PRO A O    1 
ATOM   3341  C CB   . PRO A 1 214 ? 32.862  -39.551 108.107 1.00 119.48 ?  223 PRO A CB   1 
ATOM   3342  C CG   . PRO A 1 214 ? 32.438  -40.841 107.536 1.00 129.80 ?  223 PRO A CG   1 
ATOM   3343  C CD   . PRO A 1 214 ? 33.640  -41.462 106.932 1.00 116.72 ?  223 PRO A CD   1 
ATOM   3344  H HA   . PRO A 1 214 ? 33.556  -38.539 106.460 1.00 101.05 ?  223 PRO A HA   1 
ATOM   3345  H HB2  . PRO A 1 214 ? 33.217  -39.671 109.002 1.00 143.38 ?  223 PRO A HB2  1 
ATOM   3346  H HB3  . PRO A 1 214 ? 32.126  -38.919 108.112 1.00 143.38 ?  223 PRO A HB3  1 
ATOM   3347  H HG2  . PRO A 1 214 ? 32.085  -41.405 108.243 1.00 155.76 ?  223 PRO A HG2  1 
ATOM   3348  H HG3  . PRO A 1 214 ? 31.761  -40.686 106.859 1.00 155.76 ?  223 PRO A HG3  1 
ATOM   3349  H HD2  . PRO A 1 214 ? 34.075  -42.049 107.570 1.00 140.06 ?  223 PRO A HD2  1 
ATOM   3350  H HD3  . PRO A 1 214 ? 33.404  -41.935 106.118 1.00 140.06 ?  223 PRO A HD3  1 
ATOM   3351  N N    . LYS A 1 215 ? 35.738  -38.629 108.860 1.00 101.54 ?  224 LYS A N    1 
ATOM   3352  C CA   . LYS A 1 215 ? 36.547  -37.750 109.708 1.00 84.50  ?  224 LYS A CA   1 
ATOM   3353  C C    . LYS A 1 215 ? 37.424  -36.864 108.846 1.00 123.45 ?  224 LYS A C    1 
ATOM   3354  O O    . LYS A 1 215 ? 37.434  -35.639 108.980 1.00 94.25  ?  224 LYS A O    1 
ATOM   3355  C CB   . LYS A 1 215 ? 37.413  -38.563 110.676 1.00 108.43 ?  224 LYS A CB   1 
ATOM   3356  H H    . LYS A 1 215 ? 35.827  -39.468 109.025 1.00 121.85 ?  224 LYS A H    1 
ATOM   3357  H HA   . LYS A 1 215 ? 35.960  -37.180 110.230 1.00 101.40 ?  224 LYS A HA   1 
ATOM   3358  N N    . ALA A 1 216 ? 38.104  -37.475 107.895 1.00 96.26  ?  225 ALA A N    1 
ATOM   3359  C CA   . ALA A 1 216 ? 39.080  -36.771 107.091 1.00 64.81  ?  225 ALA A CA   1 
ATOM   3360  C C    . ALA A 1 216 ? 38.443  -35.691 106.243 1.00 91.16  ?  225 ALA A C    1 
ATOM   3361  O O    . ALA A 1 216 ? 39.055  -34.650 105.984 1.00 118.68 ?  225 ALA A O    1 
ATOM   3362  C CB   . ALA A 1 216 ? 39.779  -37.772 106.203 1.00 85.86  ?  225 ALA A CB   1 
ATOM   3363  H H    . ALA A 1 216 ? 38.018  -38.307 107.693 1.00 115.52 ?  225 ALA A H    1 
ATOM   3364  H HA   . ALA A 1 216 ? 39.740  -36.359 107.671 1.00 77.77  ?  225 ALA A HA   1 
ATOM   3365  H HB1  . ALA A 1 216 ? 40.436  -37.308 105.660 1.00 103.03 ?  225 ALA A HB1  1 
ATOM   3366  H HB2  . ALA A 1 216 ? 40.218  -38.435 106.759 1.00 103.03 ?  225 ALA A HB2  1 
ATOM   3367  H HB3  . ALA A 1 216 ? 39.122  -38.201 105.632 1.00 103.03 ?  225 ALA A HB3  1 
ATOM   3368  N N    . PHE A 1 217 ? 37.259  -35.960 105.715 1.00 99.15  ?  226 PHE A N    1 
ATOM   3369  C CA   . PHE A 1 217 ? 36.618  -34.987 104.851 1.00 80.47  ?  226 PHE A CA   1 
ATOM   3370  C C    . PHE A 1 217 ? 36.103  -33.805 105.654 1.00 84.83  ?  226 PHE A C    1 
ATOM   3371  O O    . PHE A 1 217 ? 36.215  -32.652 105.229 1.00 75.88  ?  226 PHE A O    1 
ATOM   3372  C CB   . PHE A 1 217 ? 35.486  -35.661 104.092 1.00 61.55  ?  226 PHE A CB   1 
ATOM   3373  C CG   . PHE A 1 217 ? 34.758  -34.746 103.169 1.00 70.11  ?  226 PHE A CG   1 
ATOM   3374  C CD1  . PHE A 1 217 ? 35.236  -34.528 101.903 1.00 69.51  ?  226 PHE A CD1  1 
ATOM   3375  C CD2  . PHE A 1 217 ? 33.607  -34.081 103.564 1.00 96.42  ?  226 PHE A CD2  1 
ATOM   3376  C CE1  . PHE A 1 217 ? 34.581  -33.650 100.997 1.00 72.10  ?  226 PHE A CE1  1 
ATOM   3377  C CE2  . PHE A 1 217 ? 32.938  -33.214 102.670 1.00 86.38  ?  226 PHE A CE2  1 
ATOM   3378  C CZ   . PHE A 1 217 ? 33.438  -33.003 101.379 1.00 77.19  ?  226 PHE A CZ   1 
ATOM   3379  H H    . PHE A 1 217 ? 36.814  -36.686 105.838 1.00 118.98 ?  226 PHE A H    1 
ATOM   3380  H HA   . PHE A 1 217 ? 37.263  -34.658 104.206 1.00 96.56  ?  226 PHE A HA   1 
ATOM   3381  H HB2  . PHE A 1 217 ? 35.852  -36.387 103.563 1.00 73.86  ?  226 PHE A HB2  1 
ATOM   3382  H HB3  . PHE A 1 217 ? 34.845  -36.010 104.731 1.00 73.86  ?  226 PHE A HB3  1 
ATOM   3383  H HD1  . PHE A 1 217 ? 36.011  -34.963 101.630 1.00 83.41  ?  226 PHE A HD1  1 
ATOM   3384  H HD2  . PHE A 1 217 ? 33.267  -34.215 104.419 1.00 115.70 ?  226 PHE A HD2  1 
ATOM   3385  H HE1  . PHE A 1 217 ? 34.923  -33.525 100.141 1.00 86.52  ?  226 PHE A HE1  1 
ATOM   3386  H HE2  . PHE A 1 217 ? 32.165  -32.775 102.944 1.00 103.66 ?  226 PHE A HE2  1 
ATOM   3387  H HZ   . PHE A 1 217 ? 33.001  -32.430 100.791 1.00 92.63  ?  226 PHE A HZ   1 
ATOM   3388  N N    . PHE A 1 218 ? 35.537  -34.059 106.822 1.00 124.61 ?  227 PHE A N    1 
ATOM   3389  C CA   . PHE A 1 218 ? 34.931  -32.945 107.514 1.00 83.91  ?  227 PHE A CA   1 
ATOM   3390  C C    . PHE A 1 218 ? 35.974  -31.982 108.012 1.00 74.92  ?  227 PHE A C    1 
ATOM   3391  O O    . PHE A 1 218 ? 35.827  -30.768 107.832 1.00 85.04  ?  227 PHE A O    1 
ATOM   3392  C CB   . PHE A 1 218 ? 34.105  -33.428 108.685 1.00 64.74  ?  227 PHE A CB   1 
ATOM   3393  C CG   . PHE A 1 218 ? 33.651  -32.315 109.599 1.00 74.35  ?  227 PHE A CG   1 
ATOM   3394  C CD1  . PHE A 1 218 ? 32.612  -31.484 109.230 1.00 78.71  ?  227 PHE A CD1  1 
ATOM   3395  C CD2  . PHE A 1 218 ? 34.288  -32.089 110.820 1.00 92.39  ?  227 PHE A CD2  1 
ATOM   3396  C CE1  . PHE A 1 218 ? 32.204  -30.449 110.061 1.00 95.50  ?  227 PHE A CE1  1 
ATOM   3397  C CE2  . PHE A 1 218 ? 33.874  -31.068 111.660 1.00 110.88 ?  227 PHE A CE2  1 
ATOM   3398  C CZ   . PHE A 1 218 ? 32.825  -30.243 111.277 1.00 109.58 ?  227 PHE A CZ   1 
ATOM   3399  H H    . PHE A 1 218 ? 35.492  -34.823 107.215 1.00 149.53 ?  227 PHE A H    1 
ATOM   3400  H HA   . PHE A 1 218 ? 34.345  -32.470 106.904 1.00 100.70 ?  227 PHE A HA   1 
ATOM   3401  H HB2  . PHE A 1 218 ? 33.314  -33.877 108.348 1.00 77.69  ?  227 PHE A HB2  1 
ATOM   3402  H HB3  . PHE A 1 218 ? 34.637  -34.046 109.211 1.00 77.69  ?  227 PHE A HB3  1 
ATOM   3403  H HD1  . PHE A 1 218 ? 32.184  -31.616 108.415 1.00 94.46  ?  227 PHE A HD1  1 
ATOM   3404  H HD2  . PHE A 1 218 ? 34.988  -32.642 111.082 1.00 110.86 ?  227 PHE A HD2  1 
ATOM   3405  H HE1  . PHE A 1 218 ? 31.498  -29.902 109.804 1.00 114.60 ?  227 PHE A HE1  1 
ATOM   3406  H HE2  . PHE A 1 218 ? 34.303  -30.930 112.473 1.00 133.05 ?  227 PHE A HE2  1 
ATOM   3407  H HZ   . PHE A 1 218 ? 32.547  -29.550 111.832 1.00 131.50 ?  227 PHE A HZ   1 
ATOM   3408  N N    . SER A 1 219 ? 37.045  -32.509 108.610 1.00 86.41  ?  228 SER A N    1 
ATOM   3409  C CA   . SER A 1 219 ? 38.022  -31.717 109.346 1.00 110.40 ?  228 SER A CA   1 
ATOM   3410  C C    . SER A 1 219 ? 39.170  -31.211 108.473 1.00 121.58 ?  228 SER A C    1 
ATOM   3411  O O    . SER A 1 219 ? 39.863  -30.249 108.857 1.00 95.00  ?  228 SER A O    1 
ATOM   3412  C CB   . SER A 1 219 ? 38.581  -32.545 110.511 1.00 97.69  ?  228 SER A CB   1 
ATOM   3413  O OG   . SER A 1 219 ? 39.472  -33.514 110.010 1.00 90.66  ?  228 SER A OG   1 
ATOM   3414  H H    . SER A 1 219 ? 37.228  -33.349 108.601 1.00 103.69 ?  228 SER A H    1 
ATOM   3415  H HA   . SER A 1 219 ? 37.575  -30.943 109.722 1.00 132.48 ?  228 SER A HA   1 
ATOM   3416  H HB2  . SER A 1 219 ? 39.054  -31.959 111.122 1.00 117.23 ?  228 SER A HB2  1 
ATOM   3417  H HB3  . SER A 1 219 ? 37.849  -32.988 110.968 1.00 117.23 ?  228 SER A HB3  1 
ATOM   3418  H HG   . SER A 1 219 ? 39.073  -34.023 109.475 1.00 108.79 ?  228 SER A HG   1 
ATOM   3419  N N    . VAL A 1 220 ? 39.383  -31.824 107.316 1.00 67.23  ?  229 VAL A N    1 
ATOM   3420  C CA   . VAL A 1 220 ? 40.564  -31.517 106.526 1.00 50.95  ?  229 VAL A CA   1 
ATOM   3421  C C    . VAL A 1 220 ? 40.208  -31.046 105.136 1.00 52.53  ?  229 VAL A C    1 
ATOM   3422  O O    . VAL A 1 220 ? 40.483  -29.897 104.769 1.00 86.03  ?  229 VAL A O    1 
ATOM   3423  C CB   . VAL A 1 220 ? 41.483  -32.733 106.452 1.00 56.22  ?  229 VAL A CB   1 
ATOM   3424  C CG1  . VAL A 1 220 ? 42.719  -32.415 105.528 1.00 55.30  ?  229 VAL A CG1  1 
ATOM   3425  C CG2  . VAL A 1 220 ? 41.856  -33.166 107.921 1.00 50.89  ?  229 VAL A CG2  1 
ATOM   3426  H H    . VAL A 1 220 ? 38.864  -32.416 106.970 1.00 80.68  ?  229 VAL A H    1 
ATOM   3427  H HA   . VAL A 1 220 ? 41.053  -30.802 106.964 1.00 61.15  ?  229 VAL A HA   1 
ATOM   3428  H HB   . VAL A 1 220 ? 40.995  -33.465 106.046 1.00 67.46  ?  229 VAL A HB   1 
ATOM   3429  H HG11 . VAL A 1 220 ? 43.294  -33.195 105.490 1.00 66.36  ?  229 VAL A HG11 1 
ATOM   3430  H HG12 . VAL A 1 220 ? 42.400  -32.196 104.638 1.00 66.36  ?  229 VAL A HG12 1 
ATOM   3431  H HG13 . VAL A 1 220 ? 43.206  -31.663 105.900 1.00 66.36  ?  229 VAL A HG13 1 
ATOM   3432  H HG21 . VAL A 1 220 ? 42.441  -33.939 107.883 1.00 61.07  ?  229 VAL A HG21 1 
ATOM   3433  H HG22 . VAL A 1 220 ? 42.308  -32.430 108.362 1.00 61.07  ?  229 VAL A HG22 1 
ATOM   3434  H HG23 . VAL A 1 220 ? 41.043  -33.389 108.400 1.00 61.07  ?  229 VAL A HG23 1 
ATOM   3435  N N    . LEU A 1 221 ? 39.672  -31.945 104.318 1.00 66.12  ?  230 LEU A N    1 
ATOM   3436  C CA   . LEU A 1 221 ? 39.499  -31.585 102.914 1.00 58.11  ?  230 LEU A CA   1 
ATOM   3437  C C    . LEU A 1 221 ? 38.503  -30.462 102.732 1.00 56.38  ?  230 LEU A C    1 
ATOM   3438  O O    . LEU A 1 221 ? 38.551  -29.768 101.714 1.00 45.35  ?  230 LEU A O    1 
ATOM   3439  C CB   . LEU A 1 221 ? 38.953  -32.733 102.095 1.00 48.10  ?  230 LEU A CB   1 
ATOM   3440  C CG   . LEU A 1 221 ? 38.895  -32.522 100.580 1.00 44.82  ?  230 LEU A CG   1 
ATOM   3441  C CD1  . LEU A 1 221 ? 40.331  -32.289 100.020 1.00 44.41  ?  230 LEU A CD1  1 
ATOM   3442  C CD2  . LEU A 1 221 ? 38.250  -33.683 99.849  1.00 58.53  ?  230 LEU A CD2  1 
ATOM   3443  H H    . LEU A 1 221 ? 39.411  -32.735 104.536 1.00 79.34  ?  230 LEU A H    1 
ATOM   3444  H HA   . LEU A 1 221 ? 40.351  -31.311 102.539 1.00 69.73  ?  230 LEU A HA   1 
ATOM   3445  H HB2  . LEU A 1 221 ? 39.508  -33.512 102.256 1.00 57.72  ?  230 LEU A HB2  1 
ATOM   3446  H HB3  . LEU A 1 221 ? 38.049  -32.916 102.395 1.00 57.72  ?  230 LEU A HB3  1 
ATOM   3447  H HG   . LEU A 1 221 ? 38.371  -31.727 100.394 1.00 53.78  ?  230 LEU A HG   1 
ATOM   3448  H HD11 . LEU A 1 221 ? 40.278  -32.157 99.061  1.00 53.29  ?  230 LEU A HD11 1 
ATOM   3449  H HD12 . LEU A 1 221 ? 40.709  -31.502 100.442 1.00 53.29  ?  230 LEU A HD12 1 
ATOM   3450  H HD13 . LEU A 1 221 ? 40.876  -33.066 100.218 1.00 53.29  ?  230 LEU A HD13 1 
ATOM   3451  H HD21 . LEU A 1 221 ? 38.242  -33.492 98.898  1.00 70.23  ?  230 LEU A HD21 1 
ATOM   3452  H HD22 . LEU A 1 221 ? 38.763  -34.488 100.020 1.00 70.23  ?  230 LEU A HD22 1 
ATOM   3453  H HD23 . LEU A 1 221 ? 37.342  -33.794 100.172 1.00 70.23  ?  230 LEU A HD23 1 
ATOM   3454  N N    . ARG A 1 222 ? 37.506  -30.367 103.613 1.00 72.91  ?  231 ARG A N    1 
ATOM   3455  C CA   . ARG A 1 222 ? 36.529  -29.290 103.509 1.00 84.73  ?  231 ARG A CA   1 
ATOM   3456  C C    . ARG A 1 222 ? 37.198  -27.937 103.716 1.00 81.72  ?  231 ARG A C    1 
ATOM   3457  O O    . ARG A 1 222 ? 36.867  -26.965 103.032 1.00 122.42 ?  231 ARG A O    1 
ATOM   3458  C CB   . ARG A 1 222 ? 35.389  -29.585 104.509 1.00 83.45  ?  231 ARG A CB   1 
ATOM   3459  C CG   . ARG A 1 222 ? 34.163  -28.669 104.440 1.00 91.54  ?  231 ARG A CG   1 
ATOM   3460  C CD   . ARG A 1 222 ? 33.130  -28.989 105.515 1.00 82.05  ?  231 ARG A CD   1 
ATOM   3461  N NE   . ARG A 1 222 ? 33.669  -28.805 106.858 1.00 100.34 ?  231 ARG A NE   1 
ATOM   3462  C CZ   . ARG A 1 222 ? 33.325  -27.828 107.683 1.00 120.30 ?  231 ARG A CZ   1 
ATOM   3463  N NH1  . ARG A 1 222 ? 32.411  -26.937 107.314 1.00 146.28 1  231 ARG A NH1  1 
ATOM   3464  N NH2  . ARG A 1 222 ? 33.884  -27.768 108.890 1.00 124.83 1  231 ARG A NH2  1 
ATOM   3465  H H    . ARG A 1 222 ? 37.376  -30.907 104.270 1.00 87.49  ?  231 ARG A H    1 
ATOM   3466  H HA   . ARG A 1 222 ? 36.148  -29.298 102.616 1.00 101.68 ?  231 ARG A HA   1 
ATOM   3467  H HB2  . ARG A 1 222 ? 35.079  -30.492 104.357 1.00 100.14 ?  231 ARG A HB2  1 
ATOM   3468  H HB3  . ARG A 1 222 ? 35.749  -29.516 105.407 1.00 100.14 ?  231 ARG A HB3  1 
ATOM   3469  H HG2  . ARG A 1 222 ? 34.448  -27.750 104.561 1.00 109.85 ?  231 ARG A HG2  1 
ATOM   3470  H HG3  . ARG A 1 222 ? 33.738  -28.775 103.574 1.00 109.85 ?  231 ARG A HG3  1 
ATOM   3471  H HD2  . ARG A 1 222 ? 32.368  -28.399 105.411 1.00 98.45  ?  231 ARG A HD2  1 
ATOM   3472  H HD3  . ARG A 1 222 ? 32.852  -29.914 105.425 1.00 98.45  ?  231 ARG A HD3  1 
ATOM   3473  H HE   . ARG A 1 222 ? 34.253  -29.372 107.135 1.00 120.41 ?  231 ARG A HE   1 
ATOM   3474  H HH11 . ARG A 1 222 ? 32.053  -26.986 106.534 1.00 175.53 ?  231 ARG A HH11 1 
ATOM   3475  H HH12 . ARG A 1 222 ? 32.185  -26.305 107.852 1.00 175.53 ?  231 ARG A HH12 1 
ATOM   3476  H HH21 . ARG A 1 222 ? 34.472  -28.352 109.121 1.00 149.79 ?  231 ARG A HH21 1 
ATOM   3477  H HH22 . ARG A 1 222 ? 33.664  -27.140 109.434 1.00 149.79 ?  231 ARG A HH22 1 
ATOM   3478  N N    . ILE A 1 223 ? 38.206  -27.896 104.584 1.00 77.11  ?  232 ILE A N    1 
ATOM   3479  C CA   . ILE A 1 223 ? 38.908  -26.660 104.919 1.00 95.32  ?  232 ILE A CA   1 
ATOM   3480  C C    . ILE A 1 223 ? 39.580  -26.074 103.673 1.00 78.07  ?  232 ILE A C    1 
ATOM   3481  O O    . ILE A 1 223 ? 39.479  -24.860 103.389 1.00 63.11  ?  232 ILE A O    1 
ATOM   3482  C CB   . ILE A 1 223 ? 39.918  -26.935 106.052 1.00 79.31  ?  232 ILE A CB   1 
ATOM   3483  C CG1  . ILE A 1 223 ? 39.277  -27.718 107.244 1.00 82.38  ?  232 ILE A CG1  1 
ATOM   3484  C CG2  . ILE A 1 223 ? 40.507  -25.651 106.568 1.00 88.41  ?  232 ILE A CG2  1 
ATOM   3485  C CD1  . ILE A 1 223 ? 38.144  -27.045 108.009 1.00 79.76  ?  232 ILE A CD1  1 
ATOM   3486  H H    . ILE A 1 223 ? 38.508  -28.585 105.000 1.00 92.54  ?  232 ILE A H    1 
ATOM   3487  H HA   . ILE A 1 223 ? 38.265  -26.011 105.243 1.00 114.38 ?  232 ILE A HA   1 
ATOM   3488  H HB   . ILE A 1 223 ? 40.638  -27.474 105.690 1.00 95.17  ?  232 ILE A HB   1 
ATOM   3489  H HG12 . ILE A 1 223 ? 38.927  -28.554 106.898 1.00 98.85  ?  232 ILE A HG12 1 
ATOM   3490  H HG13 . ILE A 1 223 ? 39.978  -27.909 107.886 1.00 98.85  ?  232 ILE A HG13 1 
ATOM   3491  H HG21 . ILE A 1 223 ? 41.136  -25.855 107.277 1.00 106.09 ?  232 ILE A HG21 1 
ATOM   3492  H HG22 . ILE A 1 223 ? 40.963  -25.199 105.841 1.00 106.09 ?  232 ILE A HG22 1 
ATOM   3493  H HG23 . ILE A 1 223 ? 39.792  -25.091 106.909 1.00 106.09 ?  232 ILE A HG23 1 
ATOM   3494  H HD11 . ILE A 1 223 ? 37.844  -27.639 108.715 1.00 95.71  ?  232 ILE A HD11 1 
ATOM   3495  H HD12 . ILE A 1 223 ? 38.470  -26.215 108.390 1.00 95.71  ?  232 ILE A HD12 1 
ATOM   3496  H HD13 . ILE A 1 223 ? 37.414  -26.864 107.396 1.00 95.71  ?  232 ILE A HD13 1 
ATOM   3497  N N    . TYR A 1 224 ? 40.210  -26.945 102.874 1.00 74.19  ?  233 TYR A N    1 
ATOM   3498  C CA   . TYR A 1 224 ? 40.965  -26.522 101.697 1.00 59.81  ?  233 TYR A CA   1 
ATOM   3499  C C    . TYR A 1 224 ? 40.073  -26.313 100.482 1.00 67.27  ?  233 TYR A C    1 
ATOM   3500  O O    . TYR A 1 224 ? 40.548  -25.781 99.469  1.00 63.99  ?  233 TYR A O    1 
ATOM   3501  C CB   . TYR A 1 224 ? 42.107  -27.556 101.374 1.00 49.58  ?  233 TYR A CB   1 
ATOM   3502  C CG   . TYR A 1 224 ? 43.132  -27.625 102.465 1.00 62.72  ?  233 TYR A CG   1 
ATOM   3503  C CD1  . TYR A 1 224 ? 44.147  -26.705 102.530 1.00 102.18 ?  233 TYR A CD1  1 
ATOM   3504  C CD2  . TYR A 1 224 ? 43.028  -28.553 103.468 1.00 77.65  ?  233 TYR A CD2  1 
ATOM   3505  C CE1  . TYR A 1 224 ? 45.071  -26.724 103.534 1.00 82.15  ?  233 TYR A CE1  1 
ATOM   3506  C CE2  . TYR A 1 224 ? 43.942  -28.581 104.503 1.00 63.19  ?  233 TYR A CE2  1 
ATOM   3507  C CZ   . TYR A 1 224 ? 44.976  -27.657 104.530 1.00 71.38  ?  233 TYR A CZ   1 
ATOM   3508  O OH   . TYR A 1 224 ? 45.907  -27.656 105.569 1.00 58.80  ?  233 TYR A OH   1 
ATOM   3509  H H    . TYR A 1 224 ? 40.213  -27.796 102.998 1.00 89.03  ?  233 TYR A H    1 
ATOM   3510  H HA   . TYR A 1 224 ? 41.390  -25.673 101.895 1.00 71.78  ?  233 TYR A HA   1 
ATOM   3511  H HB2  . TYR A 1 224 ? 41.717  -28.438 101.270 1.00 59.50  ?  233 TYR A HB2  1 
ATOM   3512  H HB3  . TYR A 1 224 ? 42.554  -27.290 100.556 1.00 59.50  ?  233 TYR A HB3  1 
ATOM   3513  H HD1  . TYR A 1 224 ? 44.221  -26.064 101.860 1.00 122.62 ?  233 TYR A HD1  1 
ATOM   3514  H HD2  . TYR A 1 224 ? 42.334  -29.171 103.452 1.00 93.18  ?  233 TYR A HD2  1 
ATOM   3515  H HE1  . TYR A 1 224 ? 45.754  -26.094 103.551 1.00 98.58  ?  233 TYR A HE1  1 
ATOM   3516  H HE2  . TYR A 1 224 ? 43.870  -29.221 105.173 1.00 75.83  ?  233 TYR A HE2  1 
ATOM   3517  H HH   . TYR A 1 224 ? 46.462  -27.036 105.457 1.00 70.56  ?  233 TYR A HH   1 
ATOM   3518  N N    . LEU A 1 225 ? 38.785  -26.599 100.559 1.00 86.40  ?  234 LEU A N    1 
ATOM   3519  C CA   . LEU A 1 225 ? 37.925  -26.274 99.429  1.00 74.08  ?  234 LEU A CA   1 
ATOM   3520  C C    . LEU A 1 225 ? 37.044  -25.072 99.707  1.00 60.30  ?  234 LEU A C    1 
ATOM   3521  O O    . LEU A 1 225 ? 36.246  -24.692 98.850  1.00 53.19  ?  234 LEU A O    1 
ATOM   3522  C CB   . LEU A 1 225 ? 37.111  -27.479 99.052  1.00 66.21  ?  234 LEU A CB   1 
ATOM   3523  C CG   . LEU A 1 225 ? 37.921  -28.712 98.610  1.00 61.22  ?  234 LEU A CG   1 
ATOM   3524  C CD1  . LEU A 1 225 ? 36.903  -29.800 98.247  1.00 54.96  ?  234 LEU A CD1  1 
ATOM   3525  C CD2  . LEU A 1 225 ? 39.029  -28.482 97.448  1.00 45.50  ?  234 LEU A CD2  1 
ATOM   3526  H H    . LEU A 1 225 ? 38.392  -26.969 101.228 1.00 103.68 ?  234 LEU A H    1 
ATOM   3527  H HA   . LEU A 1 225 ? 38.487  -26.053 98.670  1.00 88.90  ?  234 LEU A HA   1 
ATOM   3528  H HB2  . LEU A 1 225 ? 36.577  -27.740 99.818  1.00 79.45  ?  234 LEU A HB2  1 
ATOM   3529  H HB3  . LEU A 1 225 ? 36.526  -27.236 98.317  1.00 79.45  ?  234 LEU A HB3  1 
ATOM   3530  H HG   . LEU A 1 225 ? 38.404  -29.035 99.387  1.00 73.46  ?  234 LEU A HG   1 
ATOM   3531  H HD11 . LEU A 1 225 ? 37.379  -30.596 97.962  1.00 65.95  ?  234 LEU A HD11 1 
ATOM   3532  H HD12 . LEU A 1 225 ? 36.362  -29.999 99.027  1.00 65.95  ?  234 LEU A HD12 1 
ATOM   3533  H HD13 . LEU A 1 225 ? 36.339  -29.477 97.527  1.00 65.95  ?  234 LEU A HD13 1 
ATOM   3534  H HD21 . LEU A 1 225 ? 39.468  -29.326 97.260  1.00 54.60  ?  234 LEU A HD21 1 
ATOM   3535  H HD22 . LEU A 1 225 ? 38.586  -28.154 96.650  1.00 54.60  ?  234 LEU A HD22 1 
ATOM   3536  H HD23 . LEU A 1 225 ? 39.680  -27.832 97.757  1.00 54.60  ?  234 LEU A HD23 1 
ATOM   3537  N N    . SER A 1 226 ? 37.251  -24.430 100.855 1.00 49.61  ?  235 SER A N    1 
ATOM   3538  C CA   . SER A 1 226 ? 36.592  -23.208 101.248 1.00 43.58  ?  235 SER A CA   1 
ATOM   3539  C C    . SER A 1 226 ? 37.134  -21.981 100.526 1.00 70.69  ?  235 SER A C    1 
ATOM   3540  O O    . SER A 1 226 ? 38.327  -21.868 100.245 1.00 66.32  ?  235 SER A O    1 
ATOM   3541  C CB   . SER A 1 226 ? 36.796  -23.049 102.730 1.00 49.39  ?  235 SER A CB   1 
ATOM   3542  O OG   . SER A 1 226 ? 36.517  -24.332 103.275 1.00 76.17  ?  235 SER A OG   1 
ATOM   3543  H H    . SER A 1 226 ? 37.804  -24.710 101.450 1.00 59.54  ?  235 SER A H    1 
ATOM   3544  H HA   . SER A 1 226 ? 35.641  -23.278 101.070 1.00 52.29  ?  235 SER A HA   1 
ATOM   3545  H HB2  . SER A 1 226 ? 37.715  -22.799 102.916 1.00 59.27  ?  235 SER A HB2  1 
ATOM   3546  H HB3  . SER A 1 226 ? 36.176  -22.393 103.085 1.00 59.27  ?  235 SER A HB3  1 
ATOM   3547  H HG   . SER A 1 226 ? 37.042  -24.902 102.951 1.00 91.40  ?  235 SER A HG   1 
ATOM   3548  N N    . GLY A 1 227 ? 36.241  -21.043 100.255 1.00 75.73  ?  236 GLY A N    1 
ATOM   3549  C CA   . GLY A 1 227 ? 36.603  -19.786 99.615  1.00 55.88  ?  236 GLY A CA   1 
ATOM   3550  C C    . GLY A 1 227 ? 36.363  -18.610 100.517 1.00 61.35  ?  236 GLY A C    1 
ATOM   3551  O O    . GLY A 1 227 ? 36.384  -18.752 101.738 1.00 48.43  ?  236 GLY A O    1 
ATOM   3552  H H    . GLY A 1 227 ? 35.403  -21.111 100.435 1.00 90.88  ?  236 GLY A H    1 
ATOM   3553  H HA2  . GLY A 1 227 ? 37.543  -19.803 99.373  1.00 67.06  ?  236 GLY A HA2  1 
ATOM   3554  H HA3  . GLY A 1 227 ? 36.078  -19.669 98.808  1.00 67.06  ?  236 GLY A HA3  1 
ATOM   3555  N N    . TRP A 1 228 ? 36.164  -17.437 99.943  1.00 97.38  ?  237 TRP A N    1 
ATOM   3556  C CA   . TRP A 1 228 ? 36.117  -16.226 100.729 1.00 85.39  ?  237 TRP A CA   1 
ATOM   3557  C C    . TRP A 1 228 ? 34.939  -15.368 100.268 1.00 93.55  ?  237 TRP A C    1 
ATOM   3558  O O    . TRP A 1 228 ? 35.073  -14.218 99.883  1.00 108.91 ?  237 TRP A O    1 
ATOM   3559  C CB   . TRP A 1 228 ? 37.458  -15.513 100.667 1.00 51.41  ?  237 TRP A CB   1 
ATOM   3560  C CG   . TRP A 1 228 ? 38.232  -15.736 99.403  1.00 63.26  ?  237 TRP A CG   1 
ATOM   3561  C CD1  . TRP A 1 228 ? 38.176  -14.991 98.261  1.00 71.42  ?  237 TRP A CD1  1 
ATOM   3562  C CD2  . TRP A 1 228 ? 39.217  -16.775 99.149  1.00 47.60  ?  237 TRP A CD2  1 
ATOM   3563  N NE1  . TRP A 1 228 ? 39.034  -15.501 97.312  1.00 60.94  ?  237 TRP A NE1  1 
ATOM   3564  C CE2  . TRP A 1 228 ? 39.699  -16.580 97.846  1.00 50.06  ?  237 TRP A CE2  1 
ATOM   3565  C CE3  . TRP A 1 228 ? 39.716  -17.848 99.898  1.00 46.65  ?  237 TRP A CE3  1 
ATOM   3566  C CZ2  . TRP A 1 228 ? 40.635  -17.440 97.279  1.00 47.70  ?  237 TRP A CZ2  1 
ATOM   3567  C CZ3  . TRP A 1 228 ? 40.616  -18.666 99.343  1.00 59.36  ?  237 TRP A CZ3  1 
ATOM   3568  C CH2  . TRP A 1 228 ? 41.063  -18.485 98.045  1.00 50.38  ?  237 TRP A CH2  1 
ATOM   3569  H H    . TRP A 1 228 ? 36.054  -17.318 99.098  1.00 116.86 ?  237 TRP A H    1 
ATOM   3570  H HA   . TRP A 1 228 ? 35.957  -16.466 101.655 1.00 102.47 ?  237 TRP A HA   1 
ATOM   3571  H HB2  . TRP A 1 228 ? 37.306  -14.559 100.753 1.00 61.70  ?  237 TRP A HB2  1 
ATOM   3572  H HB3  . TRP A 1 228 ? 38.007  -15.823 101.405 1.00 61.70  ?  237 TRP A HB3  1 
ATOM   3573  H HD1  . TRP A 1 228 ? 37.641  -14.240 98.143  1.00 85.71  ?  237 TRP A HD1  1 
ATOM   3574  H HE1  . TRP A 1 228 ? 39.160  -15.175 96.526  1.00 73.12  ?  237 TRP A HE1  1 
ATOM   3575  H HE3  . TRP A 1 228 ? 39.411  -18.000 100.764 1.00 55.98  ?  237 TRP A HE3  1 
ATOM   3576  H HZ2  . TRP A 1 228 ? 40.940  -17.319 96.409  1.00 57.24  ?  237 TRP A HZ2  1 
ATOM   3577  H HZ3  . TRP A 1 228 ? 40.953  -19.374 99.843  1.00 71.24  ?  237 TRP A HZ3  1 
ATOM   3578  H HH2  . TRP A 1 228 ? 41.713  -19.058 97.706  1.00 60.46  ?  237 TRP A HH2  1 
ATOM   3579  N N    . LYS A 1 229 ? 33.749  -15.966 100.284 1.00 84.11  ?  238 LYS A N    1 
ATOM   3580  C CA   . LYS A 1 229 ? 32.510  -15.239 100.085 1.00 71.23  ?  238 LYS A CA   1 
ATOM   3581  C C    . LYS A 1 229 ? 31.598  -15.578 101.249 1.00 68.32  ?  238 LYS A C    1 
ATOM   3582  O O    . LYS A 1 229 ? 31.241  -16.739 101.448 1.00 123.10 ?  238 LYS A O    1 
ATOM   3583  C CB   . LYS A 1 229 ? 31.896  -15.584 98.733  1.00 74.09  ?  238 LYS A CB   1 
ATOM   3584  C CG   . LYS A 1 229 ? 30.739  -14.662 98.248  1.00 76.02  ?  238 LYS A CG   1 
ATOM   3585  C CD   . LYS A 1 229 ? 30.417  -15.045 96.806  1.00 71.37  ?  238 LYS A CD   1 
ATOM   3586  C CE   . LYS A 1 229 ? 29.253  -14.317 96.156  1.00 66.88  ?  238 LYS A CE   1 
ATOM   3587  N NZ   . LYS A 1 229 ? 28.948  -15.007 94.814  1.00 108.80 1  238 LYS A NZ   1 
ATOM   3588  H H    . LYS A 1 229 ? 33.638  -16.809 100.410 1.00 100.93 ?  238 LYS A H    1 
ATOM   3589  H HA   . LYS A 1 229 ? 32.690  -14.286 100.105 1.00 85.47  ?  238 LYS A HA   1 
ATOM   3590  H HB2  . LYS A 1 229 ? 32.596  -15.545 98.062  1.00 88.91  ?  238 LYS A HB2  1 
ATOM   3591  H HB3  . LYS A 1 229 ? 31.546  -16.487 98.779  1.00 88.91  ?  238 LYS A HB3  1 
ATOM   3592  H HG2  . LYS A 1 229 ? 29.951  -14.803 98.796  1.00 91.22  ?  238 LYS A HG2  1 
ATOM   3593  H HG3  . LYS A 1 229 ? 31.020  -13.734 98.274  1.00 91.22  ?  238 LYS A HG3  1 
ATOM   3594  H HD2  . LYS A 1 229 ? 31.203  -14.873 96.264  1.00 85.64  ?  238 LYS A HD2  1 
ATOM   3595  H HD3  . LYS A 1 229 ? 30.213  -15.993 96.783  1.00 85.64  ?  238 LYS A HD3  1 
ATOM   3596  H HE2  . LYS A 1 229 ? 28.468  -14.374 96.723  1.00 80.26  ?  238 LYS A HE2  1 
ATOM   3597  H HE3  . LYS A 1 229 ? 29.493  -13.393 95.987  1.00 80.26  ?  238 LYS A HE3  1 
ATOM   3598  H HZ1  . LYS A 1 229 ? 28.267  -14.599 94.410  1.00 130.56 ?  238 LYS A HZ1  1 
ATOM   3599  H HZ2  . LYS A 1 229 ? 29.662  -14.970 94.284  1.00 130.56 ?  238 LYS A HZ2  1 
ATOM   3600  H HZ3  . LYS A 1 229 ? 28.733  -15.859 94.952  1.00 130.56 ?  238 LYS A HZ3  1 
ATOM   3601  N N    . GLY A 1 230 ? 31.268  -14.580 102.044 1.00 87.88  ?  239 GLY A N    1 
ATOM   3602  C CA   . GLY A 1 230 ? 30.438  -14.841 103.194 1.00 91.11  ?  239 GLY A CA   1 
ATOM   3603  C C    . GLY A 1 230 ? 31.128  -15.655 104.248 1.00 90.16  ?  239 GLY A C    1 
ATOM   3604  O O    . GLY A 1 230 ? 30.468  -16.332 105.035 1.00 103.40 ?  239 GLY A O    1 
ATOM   3605  H H    . GLY A 1 230 ? 31.507  -13.760 101.943 1.00 105.45 ?  239 GLY A H    1 
ATOM   3606  H HA2  . GLY A 1 230 ? 30.165  -13.999 103.590 1.00 109.33 ?  239 GLY A HA2  1 
ATOM   3607  H HA3  . GLY A 1 230 ? 29.642  -15.319 102.913 1.00 109.33 ?  239 GLY A HA3  1 
ATOM   3608  N N    . ASN A 1 231 ? 32.448  -15.624 104.270 1.00 100.81 ?  240 ASN A N    1 
ATOM   3609  C CA   . ASN A 1 231 ? 33.177  -16.375 105.253 1.00 89.90  ?  240 ASN A CA   1 
ATOM   3610  C C    . ASN A 1 231 ? 33.679  -15.461 106.367 1.00 102.57 ?  240 ASN A C    1 
ATOM   3611  O O    . ASN A 1 231 ? 34.423  -14.514 106.087 1.00 108.90 ?  240 ASN A O    1 
ATOM   3612  C CB   . ASN A 1 231 ? 34.342  -17.061 104.582 1.00 89.12  ?  240 ASN A CB   1 
ATOM   3613  C CG   . ASN A 1 231 ? 34.970  -18.137 105.447 1.00 76.58  ?  240 ASN A CG   1 
ATOM   3614  O OD1  . ASN A 1 231 ? 34.817  -18.180 106.713 1.00 59.18  ?  240 ASN A OD1  1 
ATOM   3615  N ND2  . ASN A 1 231 ? 35.782  -18.959 104.796 1.00 60.76  ?  240 ASN A ND2  1 
ATOM   3616  H H    . ASN A 1 231 ? 32.939  -15.175 103.725 1.00 120.97 ?  240 ASN A H    1 
ATOM   3617  H HA   . ASN A 1 231 ? 32.600  -17.051 105.642 1.00 107.88 ?  240 ASN A HA   1 
ATOM   3618  H HB2  . ASN A 1 231 ? 34.033  -17.478 103.762 1.00 106.94 ?  240 ASN A HB2  1 
ATOM   3619  H HB3  . ASN A 1 231 ? 35.025  -16.402 104.381 1.00 106.94 ?  240 ASN A HB3  1 
ATOM   3620  H HD21 . ASN A 1 231 ? 36.177  -19.597 105.218 1.00 72.91  ?  240 ASN A HD21 1 
ATOM   3621  H HD22 . ASN A 1 231 ? 35.914  -18.855 103.953 1.00 72.91  ?  240 ASN A HD22 1 
ATOM   3622  N N    . PRO A 1 232 ? 33.345  -15.731 107.628 1.00 124.38 ?  241 PRO A N    1 
ATOM   3623  C CA   . PRO A 1 232 ? 33.838  -14.892 108.724 1.00 137.25 ?  241 PRO A CA   1 
ATOM   3624  C C    . PRO A 1 232 ? 35.339  -14.786 108.848 1.00 136.94 ?  241 PRO A C    1 
ATOM   3625  O O    . PRO A 1 232 ? 35.836  -13.717 109.214 1.00 103.03 ?  241 PRO A O    1 
ATOM   3626  C CB   . PRO A 1 232 ? 33.260  -15.577 109.960 1.00 81.38  ?  241 PRO A CB   1 
ATOM   3627  C CG   . PRO A 1 232 ? 32.082  -16.249 109.496 1.00 89.46  ?  241 PRO A CG   1 
ATOM   3628  C CD   . PRO A 1 232 ? 32.296  -16.642 108.082 1.00 77.15  ?  241 PRO A CD   1 
ATOM   3629  H HA   . PRO A 1 232 ? 33.463  -14.000 108.654 1.00 164.70 ?  241 PRO A HA   1 
ATOM   3630  H HB2  . PRO A 1 232 ? 33.902  -16.213 110.312 1.00 97.65  ?  241 PRO A HB2  1 
ATOM   3631  H HB3  . PRO A 1 232 ? 33.034  -14.911 110.628 1.00 97.65  ?  241 PRO A HB3  1 
ATOM   3632  H HG2  . PRO A 1 232 ? 31.930  -17.037 110.041 1.00 107.36 ?  241 PRO A HG2  1 
ATOM   3633  H HG3  . PRO A 1 232 ? 31.325  -15.647 109.563 1.00 107.36 ?  241 PRO A HG3  1 
ATOM   3634  H HD2  . PRO A 1 232 ? 32.601  -17.561 108.029 1.00 92.58  ?  241 PRO A HD2  1 
ATOM   3635  H HD3  . PRO A 1 232 ? 31.485  -16.506 107.567 1.00 92.58  ?  241 PRO A HD3  1 
ATOM   3636  N N    . GLN A 1 233 ? 36.090  -15.844 108.616 1.00 117.40 ?  242 GLN A N    1 
ATOM   3637  C CA   . GLN A 1 233 ? 37.509  -15.683 108.897 1.00 123.00 ?  242 GLN A CA   1 
ATOM   3638  C C    . GLN A 1 233 ? 38.231  -14.875 107.826 1.00 126.32 ?  242 GLN A C    1 
ATOM   3639  O O    . GLN A 1 233 ? 39.403  -14.533 108.017 1.00 140.13 ?  242 GLN A O    1 
ATOM   3640  C CB   . GLN A 1 233 ? 38.191  -17.036 109.123 1.00 110.55 ?  242 GLN A CB   1 
ATOM   3641  C CG   . GLN A 1 233 ? 37.958  -18.110 108.091 1.00 108.41 ?  242 GLN A CG   1 
ATOM   3642  C CD   . GLN A 1 233 ? 38.308  -19.503 108.622 1.00 91.48  ?  242 GLN A CD   1 
ATOM   3643  O OE1  . GLN A 1 233 ? 39.166  -19.668 109.481 1.00 70.13  ?  242 GLN A OE1  1 
ATOM   3644  N NE2  . GLN A 1 233 ? 37.603  -20.502 108.136 1.00 116.09 ?  242 GLN A NE2  1 
ATOM   3645  H H    . GLN A 1 233 ? 35.835  -16.610 108.319 1.00 140.88 ?  242 GLN A H    1 
ATOM   3646  H HA   . GLN A 1 233 ? 37.592  -15.186 109.725 1.00 147.60 ?  242 GLN A HA   1 
ATOM   3647  H HB2  . GLN A 1 233 ? 39.149  -16.886 109.166 1.00 132.66 ?  242 GLN A HB2  1 
ATOM   3648  H HB3  . GLN A 1 233 ? 37.886  -17.387 109.974 1.00 132.66 ?  242 GLN A HB3  1 
ATOM   3649  H HG2  . GLN A 1 233 ? 37.022  -18.110 107.838 1.00 130.09 ?  242 GLN A HG2  1 
ATOM   3650  H HG3  . GLN A 1 233 ? 38.514  -17.933 107.317 1.00 130.09 ?  242 GLN A HG3  1 
ATOM   3651  H HE21 . GLN A 1 233 ? 36.988  -20.351 107.554 1.00 139.30 ?  242 GLN A HE21 1 
ATOM   3652  H HE22 . GLN A 1 233 ? 37.758  -21.306 108.399 1.00 139.30 ?  242 GLN A HE22 1 
ATOM   3653  N N    . LEU A 1 234 ? 37.546  -14.545 106.719 1.00 105.01 ?  243 LEU A N    1 
ATOM   3654  C CA   . LEU A 1 234 ? 38.052  -13.634 105.695 1.00 115.70 ?  243 LEU A CA   1 
ATOM   3655  C C    . LEU A 1 234 ? 36.906  -12.689 105.287 1.00 121.87 ?  243 LEU A C    1 
ATOM   3656  O O    . LEU A 1 234 ? 36.388  -12.696 104.173 1.00 118.39 ?  243 LEU A O    1 
ATOM   3657  C CB   . LEU A 1 234 ? 38.622  -14.394 104.506 1.00 98.45  ?  243 LEU A CB   1 
ATOM   3658  C CG   . LEU A 1 234 ? 39.947  -15.123 104.754 1.00 91.89  ?  243 LEU A CG   1 
ATOM   3659  C CD1  . LEU A 1 234 ? 40.269  -15.943 103.579 1.00 52.71  ?  243 LEU A CD1  1 
ATOM   3660  C CD2  . LEU A 1 234 ? 41.113  -14.225 104.984 1.00 107.09 ?  243 LEU A CD2  1 
ATOM   3661  H H    . LEU A 1 234 ? 36.762  -14.849 106.540 1.00 126.01 ?  243 LEU A H    1 
ATOM   3662  H HA   . LEU A 1 234 ? 38.764  -13.096 106.075 1.00 138.84 ?  243 LEU A HA   1 
ATOM   3663  H HB2  . LEU A 1 234 ? 37.972  -15.058 104.227 1.00 118.14 ?  243 LEU A HB2  1 
ATOM   3664  H HB3  . LEU A 1 234 ? 38.769  -13.764 103.783 1.00 118.14 ?  243 LEU A HB3  1 
ATOM   3665  H HG   . LEU A 1 234 ? 39.854  -15.710 105.521 1.00 110.27 ?  243 LEU A HG   1 
ATOM   3666  H HD11 . LEU A 1 234 ? 41.108  -16.404 103.738 1.00 63.25  ?  243 LEU A HD11 1 
ATOM   3667  H HD12 . LEU A 1 234 ? 39.558  -16.588 103.440 1.00 63.25  ?  243 LEU A HD12 1 
ATOM   3668  H HD13 . LEU A 1 234 ? 40.350  -15.366 102.804 1.00 63.25  ?  243 LEU A HD13 1 
ATOM   3669  H HD21 . LEU A 1 234 ? 41.904  -14.767 105.131 1.00 128.51 ?  243 LEU A HD21 1 
ATOM   3670  H HD22 . LEU A 1 234 ? 41.238  -13.663 104.203 1.00 128.51 ?  243 LEU A HD22 1 
ATOM   3671  H HD23 . LEU A 1 234 ? 40.939  -13.675 105.763 1.00 128.51 ?  243 LEU A HD23 1 
ATOM   3672  N N    . SER A 1 235 ? 36.506  -11.856 106.248 1.00 137.17 ?  244 SER A N    1 
ATOM   3673  C CA   . SER A 1 235 ? 35.296  -11.045 106.142 1.00 112.90 ?  244 SER A CA   1 
ATOM   3674  C C    . SER A 1 235 ? 35.172  -10.330 104.800 1.00 106.92 ?  244 SER A C    1 
ATOM   3675  O O    . SER A 1 235 ? 34.074  -10.216 104.249 1.00 92.62  ?  244 SER A O    1 
ATOM   3676  C CB   . SER A 1 235 ? 35.281  -10.016 107.275 1.00 95.98  ?  244 SER A CB   1 
ATOM   3677  O OG   . SER A 1 235 ? 35.487  -10.622 108.534 1.00 117.20 ?  244 SER A OG   1 
ATOM   3678  H H    . SER A 1 235 ? 36.929  -11.743 106.988 1.00 164.61 ?  244 SER A H    1 
ATOM   3679  H HA   . SER A 1 235 ? 34.521  -11.618 106.247 1.00 135.48 ?  244 SER A HA   1 
ATOM   3680  H HB2  . SER A 1 235 ? 35.987  -9.370  107.120 1.00 115.17 ?  244 SER A HB2  1 
ATOM   3681  H HB3  . SER A 1 235 ? 34.421  -9.569  107.280 1.00 115.17 ?  244 SER A HB3  1 
ATOM   3682  H HG   . SER A 1 235 ? 35.475  -10.039 109.138 1.00 140.64 ?  244 SER A HG   1 
ATOM   3683  N N    . ASP A 1 236 ? 36.264  -9.761  104.304 1.00 132.39 ?  245 ASP A N    1 
ATOM   3684  C CA   . ASP A 1 236 ? 36.209  -8.904  103.130 1.00 109.39 ?  245 ASP A CA   1 
ATOM   3685  C C    . ASP A 1 236 ? 36.757  -9.534  101.867 1.00 81.68  ?  245 ASP A C    1 
ATOM   3686  O O    . ASP A 1 236 ? 36.792  -8.863  100.830 1.00 97.49  ?  245 ASP A O    1 
ATOM   3687  C CB   . ASP A 1 236 ? 36.974  -7.622  103.419 1.00 129.98 ?  245 ASP A CB   1 
ATOM   3688  C CG   . ASP A 1 236 ? 36.439  -6.920  104.612 1.00 130.34 ?  245 ASP A CG   1 
ATOM   3689  O OD1  . ASP A 1 236 ? 35.352  -6.336  104.486 1.00 132.90 ?  245 ASP A OD1  1 
ATOM   3690  O OD2  . ASP A 1 236 ? 37.067  -7.010  105.684 1.00 118.26 -1 245 ASP A OD2  1 
ATOM   3691  H H    . ASP A 1 236 ? 37.053  -9.857  104.632 1.00 158.87 ?  245 ASP A H    1 
ATOM   3692  H HA   . ASP A 1 236 ? 35.283  -8.666  102.963 1.00 131.27 ?  245 ASP A HA   1 
ATOM   3693  H HB2  . ASP A 1 236 ? 37.905  -7.837  103.587 1.00 155.97 ?  245 ASP A HB2  1 
ATOM   3694  H HB3  . ASP A 1 236 ? 36.900  -7.027  102.658 1.00 155.97 ?  245 ASP A HB3  1 
ATOM   3695  N N    . GLY A 1 237 ? 37.187  -10.785 101.919 1.00 76.67  ?  246 GLY A N    1 
ATOM   3696  C CA   . GLY A 1 237 ? 37.787  -11.439 100.767 1.00 59.83  ?  246 GLY A CA   1 
ATOM   3697  C C    . GLY A 1 237 ? 39.310  -11.411 100.755 1.00 75.25  ?  246 GLY A C    1 
ATOM   3698  O O    . GLY A 1 237 ? 40.002  -11.134 101.751 1.00 68.59  ?  246 GLY A O    1 
ATOM   3699  H H    . GLY A 1 237 ? 37.142  -11.283 102.619 1.00 92.00  ?  246 GLY A H    1 
ATOM   3700  H HA2  . GLY A 1 237 ? 37.503  -12.367 100.746 1.00 71.80  ?  246 GLY A HA2  1 
ATOM   3701  H HA3  . GLY A 1 237 ? 37.472  -11.008 99.958  1.00 71.80  ?  246 GLY A HA3  1 
ATOM   3702  N N    . LEU A 1 238 ? 39.840  -11.684 99.571  1.00 74.77  ?  247 LEU A N    1 
ATOM   3703  C CA   . LEU A 1 238 ? 41.274  -11.785 99.374  1.00 76.83  ?  247 LEU A CA   1 
ATOM   3704  C C    . LEU A 1 238 ? 41.837  -10.605 98.577  1.00 85.98  ?  247 LEU A C    1 
ATOM   3705  O O    . LEU A 1 238 ? 41.222  -10.169 97.605  1.00 99.21  ?  247 LEU A O    1 
ATOM   3706  C CB   . LEU A 1 238 ? 41.568  -13.126 98.685  1.00 110.99 ?  247 LEU A CB   1 
ATOM   3707  C CG   . LEU A 1 238 ? 43.013  -13.618 98.610  1.00 103.41 ?  247 LEU A CG   1 
ATOM   3708  C CD1  . LEU A 1 238 ? 43.529  -13.967 99.973  1.00 69.52  ?  247 LEU A CD1  1 
ATOM   3709  C CD2  . LEU A 1 238 ? 43.123  -14.824 97.685  1.00 112.03 ?  247 LEU A CD2  1 
ATOM   3710  H H    . LEU A 1 238 ? 39.381  -11.818 98.856  1.00 89.73  ?  247 LEU A H    1 
ATOM   3711  H HA   . LEU A 1 238 ? 41.710  -11.794 100.240 1.00 92.20  ?  247 LEU A HA   1 
ATOM   3712  H HB2  . LEU A 1 238 ? 41.064  -13.813 99.150  1.00 133.19 ?  247 LEU A HB2  1 
ATOM   3713  H HB3  . LEU A 1 238 ? 41.246  -13.065 97.772  1.00 133.19 ?  247 LEU A HB3  1 
ATOM   3714  H HG   . LEU A 1 238 ? 43.570  -12.910 98.250  1.00 124.10 ?  247 LEU A HG   1 
ATOM   3715  H HD11 . LEU A 1 238 ? 44.445  -14.275 99.894  1.00 83.43  ?  247 LEU A HD11 1 
ATOM   3716  H HD12 . LEU A 1 238 ? 43.492  -13.178 100.536 1.00 83.43  ?  247 LEU A HD12 1 
ATOM   3717  H HD13 . LEU A 1 238 ? 42.975  -14.669 100.349 1.00 83.43  ?  247 LEU A HD13 1 
ATOM   3718  H HD21 . LEU A 1 238 ? 44.048  -15.115 97.655  1.00 134.43 ?  247 LEU A HD21 1 
ATOM   3719  H HD22 . LEU A 1 238 ? 42.562  -15.537 98.028  1.00 134.43 ?  247 LEU A HD22 1 
ATOM   3720  H HD23 . LEU A 1 238 ? 42.828  -14.568 96.797  1.00 134.43 ?  247 LEU A HD23 1 
ATOM   3721  N N    . VAL A 1 239 ? 42.974  -10.057 99.036  1.00 65.67  ?  248 VAL A N    1 
ATOM   3722  C CA   . VAL A 1 239 ? 43.803  -9.149  98.237  1.00 105.39 ?  248 VAL A CA   1 
ATOM   3723  C C    . VAL A 1 239 ? 44.622  -9.951  97.240  1.00 63.41  ?  248 VAL A C    1 
ATOM   3724  O O    . VAL A 1 239 ? 45.444  -10.767 97.629  1.00 55.68  ?  248 VAL A O    1 
ATOM   3725  C CB   . VAL A 1 239 ? 44.777  -8.359  99.114  1.00 161.94 ?  248 VAL A CB   1 
ATOM   3726  C CG1  . VAL A 1 239 ? 45.639  -7.503  98.245  1.00 62.78  ?  248 VAL A CG1  1 
ATOM   3727  C CG2  . VAL A 1 239 ? 44.094  -7.528  100.117 1.00 64.12  ?  248 VAL A CG2  1 
ATOM   3728  H H    . VAL A 1 239 ? 43.289  -10.201 99.824  1.00 78.80  ?  248 VAL A H    1 
ATOM   3729  H HA   . VAL A 1 239 ? 43.239  -8.526  97.753  1.00 126.47 ?  248 VAL A HA   1 
ATOM   3730  H HB   . VAL A 1 239 ? 45.352  -8.982  99.584  1.00 194.32 ?  248 VAL A HB   1 
ATOM   3731  H HG11 . VAL A 1 239 ? 46.254  -7.005  98.804  1.00 75.34  ?  248 VAL A HG11 1 
ATOM   3732  H HG12 . VAL A 1 239 ? 46.133  -8.072  97.634  1.00 75.34  ?  248 VAL A HG12 1 
ATOM   3733  H HG13 . VAL A 1 239 ? 45.075  -6.892  97.745  1.00 75.34  ?  248 VAL A HG13 1 
ATOM   3734  H HG21 . VAL A 1 239 ? 44.760  -7.054  100.640 1.00 76.94  ?  248 VAL A HG21 1 
ATOM   3735  H HG22 . VAL A 1 239 ? 43.517  -6.894  99.663  1.00 76.94  ?  248 VAL A HG22 1 
ATOM   3736  H HG23 . VAL A 1 239 ? 43.567  -8.101  100.695 1.00 76.94  ?  248 VAL A HG23 1 
ATOM   3737  N N    . TYR A 1 240 ? 44.493  -9.647  95.970  1.00 86.97  ?  249 TYR A N    1 
ATOM   3738  C CA   . TYR A 1 240 ? 45.395  -10.226 94.975  1.00 74.47  ?  249 TYR A CA   1 
ATOM   3739  C C    . TYR A 1 240 ? 46.476  -9.175  94.682  1.00 80.39  ?  249 TYR A C    1 
ATOM   3740  O O    . TYR A 1 240 ? 46.361  -8.356  93.763  1.00 87.97  ?  249 TYR A O    1 
ATOM   3741  C CB   . TYR A 1 240 ? 44.605  -10.658 93.740  1.00 83.06  ?  249 TYR A CB   1 
ATOM   3742  C CG   . TYR A 1 240 ? 43.641  -11.786 94.018  1.00 71.10  ?  249 TYR A CG   1 
ATOM   3743  C CD1  . TYR A 1 240 ? 42.453  -11.560 94.666  1.00 110.30 ?  249 TYR A CD1  1 
ATOM   3744  C CD2  . TYR A 1 240 ? 43.917  -13.057 93.632  1.00 105.19 ?  249 TYR A CD2  1 
ATOM   3745  C CE1  . TYR A 1 240 ? 41.619  -12.546 94.931  1.00 119.50 ?  249 TYR A CE1  1 
ATOM   3746  C CE2  . TYR A 1 240 ? 43.080  -14.051 93.912  1.00 91.18  ?  249 TYR A CE2  1 
ATOM   3747  C CZ   . TYR A 1 240 ? 41.925  -13.780 94.545  1.00 80.36  ?  249 TYR A CZ   1 
ATOM   3748  O OH   . TYR A 1 240 ? 41.024  -14.756 94.827  1.00 50.48  ?  249 TYR A OH   1 
ATOM   3749  H H    . TYR A 1 240 ? 43.900  -9.112  95.649  1.00 104.37 ?  249 TYR A H    1 
ATOM   3750  H HA   . TYR A 1 240 ? 45.826  -11.010 95.349  1.00 89.36  ?  249 TYR A HA   1 
ATOM   3751  H HB2  . TYR A 1 240 ? 44.093  -9.901  93.414  1.00 99.68  ?  249 TYR A HB2  1 
ATOM   3752  H HB3  . TYR A 1 240 ? 45.225  -10.956 93.058  1.00 99.68  ?  249 TYR A HB3  1 
ATOM   3753  H HD1  . TYR A 1 240 ? 42.241  -10.697 94.941  1.00 132.36 ?  249 TYR A HD1  1 
ATOM   3754  H HD2  . TYR A 1 240 ? 44.720  -13.241 93.199  1.00 126.22 ?  249 TYR A HD2  1 
ATOM   3755  H HE1  . TYR A 1 240 ? 40.817  -12.377 95.370  1.00 143.40 ?  249 TYR A HE1  1 
ATOM   3756  H HE2  . TYR A 1 240 ? 43.274  -14.919 93.640  1.00 109.42 ?  249 TYR A HE2  1 
ATOM   3757  H HH   . TYR A 1 240 ? 41.305  -15.496 94.546  1.00 60.58  ?  249 TYR A HH   1 
ATOM   3758  N N    . GLU A 1 241 ? 47.531  -9.202  95.495  1.00 58.22  ?  250 GLU A N    1 
ATOM   3759  C CA   . GLU A 1 241 ? 48.570  -8.174  95.484  1.00 72.49  ?  250 GLU A CA   1 
ATOM   3760  C C    . GLU A 1 241 ? 49.056  -7.894  94.068  1.00 116.99 ?  250 GLU A C    1 
ATOM   3761  O O    . GLU A 1 241 ? 49.509  -8.789  93.338  1.00 59.36  ?  250 GLU A O    1 
ATOM   3762  C CB   . GLU A 1 241 ? 49.751  -8.622  96.377  1.00 89.84  ?  250 GLU A CB   1 
ATOM   3763  C CG   . GLU A 1 241 ? 50.874  -7.629  96.608  1.00 77.90  ?  250 GLU A CG   1 
ATOM   3764  C CD   . GLU A 1 241 ? 51.978  -8.216  97.457  1.00 93.54  ?  250 GLU A CD   1 
ATOM   3765  O OE1  . GLU A 1 241 ? 52.798  -8.960  96.883  1.00 117.11 ?  250 GLU A OE1  1 
ATOM   3766  O OE2  . GLU A 1 241 ? 52.012  -7.971  98.699  1.00 65.09  -1 250 GLU A OE2  1 
ATOM   3767  H H    . GLU A 1 241 ? 47.670  -9.821  96.076  1.00 69.87  ?  250 GLU A H    1 
ATOM   3768  H HA   . GLU A 1 241 ? 48.209  -7.351  95.849  1.00 86.99  ?  250 GLU A HA   1 
ATOM   3769  H HB2  . GLU A 1 241 ? 49.395  -8.856  97.249  1.00 107.81 ?  250 GLU A HB2  1 
ATOM   3770  H HB3  . GLU A 1 241 ? 50.148  -9.411  95.975  1.00 107.81 ?  250 GLU A HB3  1 
ATOM   3771  H HG2  . GLU A 1 241 ? 51.254  -7.372  95.753  1.00 93.48  ?  250 GLU A HG2  1 
ATOM   3772  H HG3  . GLU A 1 241 ? 50.522  -6.850  97.067  1.00 93.48  ?  250 GLU A HG3  1 
ATOM   3773  N N    . GLY A 1 242 ? 48.978  -6.630  93.691  1.00 81.68  ?  251 GLY A N    1 
ATOM   3774  C CA   . GLY A 1 242 ? 49.554  -6.213  92.440  1.00 66.66  ?  251 GLY A CA   1 
ATOM   3775  C C    . GLY A 1 242 ? 48.676  -6.397  91.236  1.00 81.72  ?  251 GLY A C    1 
ATOM   3776  O O    . GLY A 1 242 ? 48.969  -5.798  90.182  1.00 86.42  ?  251 GLY A O    1 
ATOM   3777  H H    . GLY A 1 242 ? 48.598  -6.002  94.140  1.00 98.01  ?  251 GLY A H    1 
ATOM   3778  H HA2  . GLY A 1 242 ? 49.784  -5.272  92.499  1.00 79.99  ?  251 GLY A HA2  1 
ATOM   3779  H HA3  . GLY A 1 242 ? 50.372  -6.712  92.290  1.00 79.99  ?  251 GLY A HA3  1 
ATOM   3780  N N    . PHE A 1 243 ? 47.599  -7.182  91.352  1.00 62.80  ?  252 PHE A N    1 
ATOM   3781  C CA   . PHE A 1 243 ? 46.598  -7.244  90.284  1.00 122.35 ?  252 PHE A CA   1 
ATOM   3782  C C    . PHE A 1 243 ? 45.355  -6.400  90.553  1.00 64.65  ?  252 PHE A C    1 
ATOM   3783  O O    . PHE A 1 243 ? 45.003  -5.544  89.739  1.00 67.03  ?  252 PHE A O    1 
ATOM   3784  C CB   . PHE A 1 243 ? 46.178  -8.679  90.061  1.00 99.06  ?  252 PHE A CB   1 
ATOM   3785  C CG   . PHE A 1 243 ? 45.618  -8.910  88.742  1.00 115.08 ?  252 PHE A CG   1 
ATOM   3786  C CD1  . PHE A 1 243 ? 46.449  -9.109  87.655  1.00 140.50 ?  252 PHE A CD1  1 
ATOM   3787  C CD2  . PHE A 1 243 ? 44.272  -8.927  88.573  1.00 96.71  ?  252 PHE A CD2  1 
ATOM   3788  C CE1  . PHE A 1 243 ? 45.934  -9.310  86.406  1.00 97.08  ?  252 PHE A CE1  1 
ATOM   3789  C CE2  . PHE A 1 243 ? 43.734  -9.130  87.328  1.00 110.22 ?  252 PHE A CE2  1 
ATOM   3790  C CZ   . PHE A 1 243 ? 44.567  -9.328  86.241  1.00 108.36 ?  252 PHE A CZ   1 
ATOM   3791  H H    . PHE A 1 243 ? 47.427  -7.681  92.031  1.00 75.37  ?  252 PHE A H    1 
ATOM   3792  H HA   . PHE A 1 243 ? 47.000  -6.922  89.462  1.00 146.82 ?  252 PHE A HA   1 
ATOM   3793  H HB2  . PHE A 1 243 ? 46.953  -9.253  90.161  1.00 118.87 ?  252 PHE A HB2  1 
ATOM   3794  H HB3  . PHE A 1 243 ? 45.504  -8.915  90.717  1.00 118.87 ?  252 PHE A HB3  1 
ATOM   3795  H HD1  . PHE A 1 243 ? 47.372  -9.092  87.774  1.00 168.59 ?  252 PHE A HD1  1 
ATOM   3796  H HD2  . PHE A 1 243 ? 43.712  -8.791  89.302  1.00 116.05 ?  252 PHE A HD2  1 
ATOM   3797  H HE1  . PHE A 1 243 ? 46.498  -9.445  85.680  1.00 116.50 ?  252 PHE A HE1  1 
ATOM   3798  H HE2  . PHE A 1 243 ? 42.811  -9.142  87.216  1.00 132.26 ?  252 PHE A HE2  1 
ATOM   3799  H HZ   . PHE A 1 243 ? 44.202  -9.470  85.397  1.00 130.03 ?  252 PHE A HZ   1 
ATOM   3800  N N    . TRP A 1 244 ? 44.737  -6.559  91.719  1.00 64.02  ?  253 TRP A N    1 
ATOM   3801  C CA   . TRP A 1 244 ? 43.612  -5.738  92.164  1.00 79.28  ?  253 TRP A CA   1 
ATOM   3802  C C    . TRP A 1 244 ? 43.937  -5.031  93.450  1.00 87.42  ?  253 TRP A C    1 
ATOM   3803  O O    . TRP A 1 244 ? 44.524  -5.608  94.374  1.00 94.85  ?  253 TRP A O    1 
ATOM   3804  C CB   . TRP A 1 244 ? 42.334  -6.530  92.422  1.00 93.83  ?  253 TRP A CB   1 
ATOM   3805  C CG   . TRP A 1 244 ? 41.696  -6.997  91.201  1.00 77.45  ?  253 TRP A CG   1 
ATOM   3806  C CD1  . TRP A 1 244 ? 41.387  -6.254  90.103  1.00 69.40  ?  253 TRP A CD1  1 
ATOM   3807  C CD2  . TRP A 1 244 ? 41.300  -8.325  90.925  1.00 82.47  ?  253 TRP A CD2  1 
ATOM   3808  N NE1  . TRP A 1 244 ? 40.800  -7.042  89.153  1.00 150.29 ?  253 TRP A NE1  1 
ATOM   3809  C CE2  . TRP A 1 244 ? 40.731  -8.326  89.633  1.00 91.90  ?  253 TRP A CE2  1 
ATOM   3810  C CE3  . TRP A 1 244 ? 41.369  -9.520  91.642  1.00 63.66  ?  253 TRP A CE3  1 
ATOM   3811  C CZ2  . TRP A 1 244 ? 40.231  -9.480  89.036  1.00 75.46  ?  253 TRP A CZ2  1 
ATOM   3812  C CZ3  . TRP A 1 244 ? 40.866  -10.674 91.045  1.00 82.52  ?  253 TRP A CZ3  1 
ATOM   3813  C CH2  . TRP A 1 244 ? 40.307  -10.644 89.751  1.00 86.43  ?  253 TRP A CH2  1 
ATOM   3814  H H    . TRP A 1 244 ? 44.961  -7.159  92.292  1.00 76.83  ?  253 TRP A H    1 
ATOM   3815  H HA   . TRP A 1 244 ? 43.421  -5.068  91.490  1.00 95.14  ?  253 TRP A HA   1 
ATOM   3816  H HB2  . TRP A 1 244 ? 42.548  -7.307  92.963  1.00 112.60 ?  253 TRP A HB2  1 
ATOM   3817  H HB3  . TRP A 1 244 ? 41.702  -5.964  92.892  1.00 112.60 ?  253 TRP A HB3  1 
ATOM   3818  H HD1  . TRP A 1 244 ? 41.536  -5.340  90.019  1.00 83.28  ?  253 TRP A HD1  1 
ATOM   3819  H HE1  . TRP A 1 244 ? 40.518  -6.778  88.384  1.00 180.35 ?  253 TRP A HE1  1 
ATOM   3820  H HE3  . TRP A 1 244 ? 41.735  -9.544  92.496  1.00 76.40  ?  253 TRP A HE3  1 
ATOM   3821  H HZ2  . TRP A 1 244 ? 39.865  -9.462  88.182  1.00 90.55  ?  253 TRP A HZ2  1 
ATOM   3822  H HZ3  . TRP A 1 244 ? 40.898  -11.479 91.510  1.00 99.02  ?  253 TRP A HZ3  1 
ATOM   3823  H HH2  . TRP A 1 244 ? 39.976  -11.429 89.379  1.00 103.71 ?  253 TRP A HH2  1 
ATOM   3824  N N    . GLU A 1 245 ? 43.457  -3.804  93.516  1.00 84.69  ?  254 GLU A N    1 
ATOM   3825  C CA   . GLU A 1 245 ? 43.740  -2.950  94.661  1.00 88.08  ?  254 GLU A CA   1 
ATOM   3826  C C    . GLU A 1 245 ? 43.002  -3.419  95.904  1.00 94.50  ?  254 GLU A C    1 
ATOM   3827  O O    . GLU A 1 245 ? 43.602  -3.564  96.973  1.00 72.67  ?  254 GLU A O    1 
ATOM   3828  C CB   . GLU A 1 245 ? 43.371  -1.510  94.293  1.00 88.36  ?  254 GLU A CB   1 
ATOM   3829  C CG   . GLU A 1 245 ? 43.789  -0.490  95.294  1.00 107.05 ?  254 GLU A CG   1 
ATOM   3830  C CD   . GLU A 1 245 ? 43.999  0.901   94.699  1.00 116.46 ?  254 GLU A CD   1 
ATOM   3831  O OE1  . GLU A 1 245 ? 44.286  1.031   93.474  1.00 104.42 ?  254 GLU A OE1  1 
ATOM   3832  O OE2  . GLU A 1 245 ? 43.890  1.871   95.486  1.00 100.30 -1 254 GLU A OE2  1 
ATOM   3833  H H    . GLU A 1 245 ? 42.964  -3.438  92.914  1.00 101.62 ?  254 GLU A H    1 
ATOM   3834  H HA   . GLU A 1 245 ? 44.692  -2.978  94.848  1.00 105.70 ?  254 GLU A HA   1 
ATOM   3835  H HB2  . GLU A 1 245 ? 43.795  -1.286  93.450  1.00 106.03 ?  254 GLU A HB2  1 
ATOM   3836  H HB3  . GLU A 1 245 ? 42.407  -1.451  94.199  1.00 106.03 ?  254 GLU A HB3  1 
ATOM   3837  H HG2  . GLU A 1 245 ? 43.103  -0.421  95.977  1.00 128.45 ?  254 GLU A HG2  1 
ATOM   3838  H HG3  . GLU A 1 245 ? 44.626  -0.770  95.696  1.00 128.45 ?  254 GLU A HG3  1 
ATOM   3839  N N    . ASP A 1 246 ? 41.730  -3.689  95.780  1.00 98.58  ?  255 ASP A N    1 
ATOM   3840  C CA   . ASP A 1 246 ? 40.913  -4.072  96.915  1.00 95.95  ?  255 ASP A CA   1 
ATOM   3841  C C    . ASP A 1 246 ? 40.776  -5.583  97.032  1.00 92.96  ?  255 ASP A C    1 
ATOM   3842  O O    . ASP A 1 246 ? 41.013  -6.332  96.078  1.00 83.06  ?  255 ASP A O    1 
ATOM   3843  C CB   . ASP A 1 246 ? 39.543  -3.419  96.834  1.00 114.51 ?  255 ASP A CB   1 
ATOM   3844  C CG   . ASP A 1 246 ? 39.625  -1.935  96.600  1.00 155.28 ?  255 ASP A CG   1 
ATOM   3845  O OD1  . ASP A 1 246 ? 39.889  -1.213  97.585  1.00 259.07 ?  255 ASP A OD1  1 
ATOM   3846  O OD2  . ASP A 1 246 ? 39.451  -1.492  95.444  1.00 130.85 -1 255 ASP A OD2  1 
ATOM   3847  H H    . ASP A 1 246 ? 41.300  -3.660  95.036  1.00 118.29 ?  255 ASP A H    1 
ATOM   3848  H HA   . ASP A 1 246 ? 41.342  -3.753  97.725  1.00 115.14 ?  255 ASP A HA   1 
ATOM   3849  H HB2  . ASP A 1 246 ? 39.047  -3.812  96.098  1.00 137.41 ?  255 ASP A HB2  1 
ATOM   3850  H HB3  . ASP A 1 246 ? 39.071  -3.566  97.669  1.00 137.41 ?  255 ASP A HB3  1 
ATOM   3851  N N    . PRO A 1 247 ? 40.417  -6.062  98.212  1.00 91.48  ?  256 PRO A N    1 
ATOM   3852  C CA   . PRO A 1 247 ? 40.096  -7.480  98.345  1.00 96.05  ?  256 PRO A CA   1 
ATOM   3853  C C    . PRO A 1 247 ? 38.768  -7.818  97.686  1.00 87.79  ?  256 PRO A C    1 
ATOM   3854  O O    . PRO A 1 247 ? 37.812  -7.037  97.696  1.00 106.18 ?  256 PRO A O    1 
ATOM   3855  C CB   . PRO A 1 247 ? 40.063  -7.705  99.861  1.00 81.08  ?  256 PRO A CB   1 
ATOM   3856  C CG   . PRO A 1 247 ? 39.800  -6.376  100.438 1.00 68.92  ?  256 PRO A CG   1 
ATOM   3857  C CD   . PRO A 1 247 ? 40.326  -5.346  99.490  1.00 85.73  ?  256 PRO A CD   1 
ATOM   3858  H HA   . PRO A 1 247 ? 40.798  -8.023  97.954  1.00 115.25 ?  256 PRO A HA   1 
ATOM   3859  H HB2  . PRO A 1 247 ? 39.351  -8.324  100.084 1.00 97.29  ?  256 PRO A HB2  1 
ATOM   3860  H HB3  . PRO A 1 247 ? 40.921  -8.045  100.159 1.00 97.29  ?  256 PRO A HB3  1 
ATOM   3861  H HG2  . PRO A 1 247 ? 38.844  -6.264  100.555 1.00 82.71  ?  256 PRO A HG2  1 
ATOM   3862  H HG3  . PRO A 1 247 ? 40.252  -6.305  101.293 1.00 82.71  ?  256 PRO A HG3  1 
ATOM   3863  H HD2  . PRO A 1 247 ? 39.704  -4.605  99.417  1.00 102.87 ?  256 PRO A HD2  1 
ATOM   3864  H HD3  . PRO A 1 247 ? 41.204  -5.046  99.771  1.00 102.87 ?  256 PRO A HD3  1 
ATOM   3865  N N    . LYS A 1 248 ? 38.767  -8.983  97.053  1.00 97.10  ?  257 LYS A N    1 
ATOM   3866  C CA   . LYS A 1 248 ? 37.658  -9.515  96.282  1.00 87.27  ?  257 LYS A CA   1 
ATOM   3867  C C    . LYS A 1 248 ? 37.160  -10.814 96.937  1.00 77.78  ?  257 LYS A C    1 
ATOM   3868  O O    . LYS A 1 248 ? 37.959  -11.627 97.404  1.00 92.53  ?  257 LYS A O    1 
ATOM   3869  C CB   . LYS A 1 248 ? 38.105  -9.741  94.812  1.00 72.00  ?  257 LYS A CB   1 
ATOM   3870  C CG   . LYS A 1 248 ? 38.783  -8.543  94.143  1.00 77.04  ?  257 LYS A CG   1 
ATOM   3871  C CD   . LYS A 1 248 ? 37.884  -7.335  94.096  1.00 112.28 ?  257 LYS A CD   1 
ATOM   3872  C CE   . LYS A 1 248 ? 38.377  -6.230  93.171  1.00 75.77  ?  257 LYS A CE   1 
ATOM   3873  H H    . LYS A 1 248 ? 39.444  -9.513  97.058  1.00 116.52 ?  257 LYS A H    1 
ATOM   3874  H HA   . LYS A 1 248 ? 36.930  -8.874  96.284  1.00 104.72 ?  257 LYS A HA   1 
ATOM   3875  H HB2  . LYS A 1 248 ? 38.733  -10.480 94.792  1.00 86.39  ?  257 LYS A HB2  1 
ATOM   3876  H HB3  . LYS A 1 248 ? 37.323  -9.966  94.284  1.00 86.39  ?  257 LYS A HB3  1 
ATOM   3877  H HG2  . LYS A 1 248 ? 39.579  -8.307  94.644  1.00 92.45  ?  257 LYS A HG2  1 
ATOM   3878  H HG3  . LYS A 1 248 ? 39.019  -8.779  93.232  1.00 92.45  ?  257 LYS A HG3  1 
ATOM   3879  H HD2  . LYS A 1 248 ? 37.007  -7.611  93.786  1.00 134.73 ?  257 LYS A HD2  1 
ATOM   3880  H HD3  . LYS A 1 248 ? 37.814  -6.964  94.989  1.00 134.73 ?  257 LYS A HD3  1 
ATOM   3881  H HE2  . LYS A 1 248 ? 39.107  -5.759  93.603  1.00 90.92  ?  257 LYS A HE2  1 
ATOM   3882  H HE3  . LYS A 1 248 ? 38.684  -6.627  92.341  1.00 90.92  ?  257 LYS A HE3  1 
ATOM   3883  N N    . GLU A 1 249 ? 35.831  -10.989 97.016  1.00 93.97  ?  258 GLU A N    1 
ATOM   3884  C CA   . GLU A 1 249 ? 35.207  -12.187 97.593  1.00 81.21  ?  258 GLU A CA   1 
ATOM   3885  C C    . GLU A 1 249 ? 34.950  -13.174 96.472  1.00 76.65  ?  258 GLU A C    1 
ATOM   3886  O O    . GLU A 1 249 ? 34.483  -12.770 95.405  1.00 55.43  ?  258 GLU A O    1 
ATOM   3887  C CB   . GLU A 1 249 ? 33.884  -11.880 98.323  1.00 90.66  ?  258 GLU A CB   1 
ATOM   3888  C CG   . GLU A 1 249 ? 34.033  -11.091 99.624  1.00 103.12 ?  258 GLU A CG   1 
ATOM   3889  C CD   . GLU A 1 249 ? 32.732  -10.910 100.421 1.00 110.43 ?  258 GLU A CD   1 
ATOM   3890  O OE1  . GLU A 1 249 ? 32.164  -9.792  100.390 1.00 190.48 ?  258 GLU A OE1  1 
ATOM   3891  O OE2  . GLU A 1 249 ? 32.297  -11.865 101.094 1.00 99.50  -1 258 GLU A OE2  1 
ATOM   3892  H H    . GLU A 1 249 ? 35.259  -10.412 96.733  1.00 112.77 ?  258 GLU A H    1 
ATOM   3893  H HA   . GLU A 1 249 ? 35.818  -12.594 98.227  1.00 97.45  ?  258 GLU A HA   1 
ATOM   3894  H HB2  . GLU A 1 249 ? 33.318  -11.362 97.729  1.00 108.80 ?  258 GLU A HB2  1 
ATOM   3895  H HB3  . GLU A 1 249 ? 33.448  -12.720 98.537  1.00 108.80 ?  258 GLU A HB3  1 
ATOM   3896  H HG2  . GLU A 1 249 ? 34.664  -11.555 100.196 1.00 123.75 ?  258 GLU A HG2  1 
ATOM   3897  H HG3  . GLU A 1 249 ? 34.372  -10.208 99.413  1.00 123.75 ?  258 GLU A HG3  1 
ATOM   3898  N N    . PHE A 1 250 ? 35.317  -14.452 96.694  1.00 92.66  ?  259 PHE A N    1 
ATOM   3899  C CA   . PHE A 1 250 ? 35.109  -15.544 95.742  1.00 87.36  ?  259 PHE A CA   1 
ATOM   3900  C C    . PHE A 1 250 ? 34.751  -16.827 96.465  1.00 90.83  ?  259 PHE A C    1 
ATOM   3901  O O    . PHE A 1 250 ? 35.345  -17.193 97.489  1.00 83.01  ?  259 PHE A O    1 
ATOM   3902  C CB   . PHE A 1 250 ? 36.327  -15.857 94.874  1.00 95.22  ?  259 PHE A CB   1 
ATOM   3903  C CG   . PHE A 1 250 ? 36.625  -14.831 93.847  1.00 68.42  ?  259 PHE A CG   1 
ATOM   3904  C CD1  . PHE A 1 250 ? 35.903  -14.764 92.676  1.00 80.47  ?  259 PHE A CD1  1 
ATOM   3905  C CD2  . PHE A 1 250 ? 37.647  -13.909 94.050  1.00 65.53  ?  259 PHE A CD2  1 
ATOM   3906  C CE1  . PHE A 1 250 ? 36.202  -13.795 91.714  1.00 77.28  ?  259 PHE A CE1  1 
ATOM   3907  C CE2  . PHE A 1 250 ? 37.932  -12.915 93.090  1.00 59.72  ?  259 PHE A CE2  1 
ATOM   3908  C CZ   . PHE A 1 250 ? 37.190  -12.868 91.923  1.00 75.03  ?  259 PHE A CZ   1 
ATOM   3909  H H    . PHE A 1 250 ? 35.703  -14.710 97.418  1.00 111.20 ?  259 PHE A H    1 
ATOM   3910  H HA   . PHE A 1 250 ? 34.372  -15.314 95.155  1.00 104.83 ?  259 PHE A HA   1 
ATOM   3911  H HB2  . PHE A 1 250 ? 37.105  -15.934 95.448  1.00 114.26 ?  259 PHE A HB2  1 
ATOM   3912  H HB3  . PHE A 1 250 ? 36.174  -16.698 94.415  1.00 114.26 ?  259 PHE A HB3  1 
ATOM   3913  H HD1  . PHE A 1 250 ? 35.221  -15.375 92.518  1.00 96.56  ?  259 PHE A HD1  1 
ATOM   3914  H HD2  . PHE A 1 250 ? 38.136  -13.936 94.841  1.00 78.63  ?  259 PHE A HD2  1 
ATOM   3915  H HE1  . PHE A 1 250 ? 35.700  -13.759 90.932  1.00 92.74  ?  259 PHE A HE1  1 
ATOM   3916  H HE2  . PHE A 1 250 ? 38.617  -12.302 93.236  1.00 71.66  ?  259 PHE A HE2  1 
ATOM   3917  H HZ   . PHE A 1 250 ? 37.378  -12.230 91.274  1.00 90.04  ?  259 PHE A HZ   1 
ATOM   3918  N N    . ALA A 1 251 ? 33.856  -17.558 95.833  1.00 82.55  ?  260 ALA A N    1 
ATOM   3919  C CA   . ALA A 1 251 ? 33.196  -18.698 96.435  1.00 58.88  ?  260 ALA A CA   1 
ATOM   3920  C C    . ALA A 1 251 ? 34.047  -19.945 96.465  1.00 54.49  ?  260 ALA A C    1 
ATOM   3921  O O    . ALA A 1 251 ? 34.744  -20.286 95.503  1.00 70.02  ?  260 ALA A O    1 
ATOM   3922  C CB   . ALA A 1 251 ? 31.949  -18.984 95.632  1.00 48.93  ?  260 ALA A CB   1 
ATOM   3923  H H    . ALA A 1 251 ? 33.606  -17.409 95.024  1.00 99.06  ?  260 ALA A H    1 
ATOM   3924  H HA   . ALA A 1 251 ? 32.936  -18.479 97.344  1.00 70.66  ?  260 ALA A HA   1 
ATOM   3925  H HB1  . ALA A 1 251 ? 31.492  -19.746 96.021  1.00 58.71  ?  260 ALA A HB1  1 
ATOM   3926  H HB2  . ALA A 1 251 ? 31.373  -18.204 95.655  1.00 58.71  ?  260 ALA A HB2  1 
ATOM   3927  H HB3  . ALA A 1 251 ? 32.203  -19.181 94.716  1.00 58.71  ?  260 ALA A HB3  1 
ATOM   3928  N N    . GLY A 1 252 ? 33.877  -20.712 97.521  1.00 52.56  ?  261 GLY A N    1 
ATOM   3929  C CA   . GLY A 1 252 ? 34.457  -22.037 97.519  1.00 86.79  ?  261 GLY A CA   1 
ATOM   3930  C C    . GLY A 1 252 ? 33.827  -22.927 96.460  1.00 101.95 ?  261 GLY A C    1 
ATOM   3931  O O    . GLY A 1 252 ? 32.710  -22.695 95.988  1.00 87.36  ?  261 GLY A O    1 
ATOM   3932  H H    . GLY A 1 252 ? 33.444  -20.499 98.233  1.00 63.07  ?  261 GLY A H    1 
ATOM   3933  H HA2  . GLY A 1 252 ? 35.409  -21.975 97.344  1.00 104.15 ?  261 GLY A HA2  1 
ATOM   3934  H HA3  . GLY A 1 252 ? 34.329  -22.450 98.387  1.00 104.15 ?  261 GLY A HA3  1 
ATOM   3935  N N    . GLY A 1 253 ? 34.593  -23.944 96.064  1.00 69.28  ?  262 GLY A N    1 
ATOM   3936  C CA   . GLY A 1 253 ? 34.094  -24.953 95.128  1.00 68.50  ?  262 GLY A CA   1 
ATOM   3937  C C    . GLY A 1 253 ? 32.915  -25.762 95.683  1.00 48.34  ?  262 GLY A C    1 
ATOM   3938  O O    . GLY A 1 253 ? 32.831  -26.057 96.888  1.00 63.26  ?  262 GLY A O    1 
ATOM   3939  H H    . GLY A 1 253 ? 35.404  -24.072 96.321  1.00 83.13  ?  262 GLY A H    1 
ATOM   3940  H HA2  . GLY A 1 253 ? 33.806  -24.518 94.310  1.00 82.20  ?  262 GLY A HA2  1 
ATOM   3941  H HA3  . GLY A 1 253 ? 34.810  -25.570 94.910  1.00 82.20  ?  262 GLY A HA3  1 
ATOM   3942  N N    . SER A 1 254 ? 31.995  -26.129 94.795  1.00 43.74  ?  263 SER A N    1 
ATOM   3943  C CA   . SER A 1 254 ? 30.829  -26.862 95.236  1.00 68.93  ?  263 SER A CA   1 
ATOM   3944  C C    . SER A 1 254 ? 30.319  -27.754 94.117  1.00 43.17  ?  263 SER A C    1 
ATOM   3945  O O    . SER A 1 254 ? 30.642  -27.557 92.953  1.00 53.88  ?  263 SER A O    1 
ATOM   3946  C CB   . SER A 1 254 ? 29.727  -25.910 95.585  1.00 49.69  ?  263 SER A CB   1 
ATOM   3947  O OG   . SER A 1 254 ? 28.919  -25.734 94.426  1.00 68.62  ?  263 SER A OG   1 
ATOM   3948  H H    . SER A 1 254 ? 32.025  -25.967 93.951  1.00 52.49  ?  263 SER A H    1 
ATOM   3949  H HA   . SER A 1 254 ? 31.044  -27.405 96.010  1.00 82.72  ?  263 SER A HA   1 
ATOM   3950  H HB2  . SER A 1 254 ? 29.191  -26.283 96.302  1.00 59.63  ?  263 SER A HB2  1 
ATOM   3951  H HB3  . SER A 1 254 ? 30.106  -25.057 95.850  1.00 59.63  ?  263 SER A HB3  1 
ATOM   3952  H HG   . SER A 1 254 ? 28.290  -25.203 94.592  1.00 82.35  ?  263 SER A HG   1 
ATOM   3953  N N    . ALA A 1 255 ? 29.455  -28.696 94.437  1.00 58.43  ?  264 ALA A N    1 
ATOM   3954  C CA   . ALA A 1 255 ? 28.905  -29.453 93.314  1.00 71.93  ?  264 ALA A CA   1 
ATOM   3955  C C    . ALA A 1 255 ? 28.183  -28.560 92.292  1.00 65.70  ?  264 ALA A C    1 
ATOM   3956  O O    . ALA A 1 255 ? 28.150  -28.891 91.093  1.00 64.46  ?  264 ALA A O    1 
ATOM   3957  C CB   . ALA A 1 255 ? 27.941  -30.502 93.809  1.00 46.35  ?  264 ALA A CB   1 
ATOM   3958  H H    . ALA A 1 255 ? 29.183  -28.910 95.224  1.00 70.12  ?  264 ALA A H    1 
ATOM   3959  H HA   . ALA A 1 255 ? 29.630  -29.905 92.855  1.00 86.32  ?  264 ALA A HA   1 
ATOM   3960  H HB1  . ALA A 1 255 ? 27.589  -30.991 93.048  1.00 55.62  ?  264 ALA A HB1  1 
ATOM   3961  H HB2  . ALA A 1 255 ? 28.411  -31.108 94.403  1.00 55.62  ?  264 ALA A HB2  1 
ATOM   3962  H HB3  . ALA A 1 255 ? 27.217  -30.066 94.285  1.00 55.62  ?  264 ALA A HB3  1 
ATOM   3963  N N    . GLY A 1 256 ? 27.639  -27.412 92.731  1.00 79.24  ?  265 GLY A N    1 
ATOM   3964  C CA   . GLY A 1 256 ? 26.887  -26.535 91.851  1.00 56.80  ?  265 GLY A CA   1 
ATOM   3965  C C    . GLY A 1 256 ? 27.674  -26.005 90.659  1.00 55.89  ?  265 GLY A C    1 
ATOM   3966  O O    . GLY A 1 256 ? 27.073  -25.672 89.617  1.00 58.42  ?  265 GLY A O    1 
ATOM   3967  H H    . GLY A 1 256 ? 27.699  -27.127 93.540  1.00 95.09  ?  265 GLY A H    1 
ATOM   3968  H HA2  . GLY A 1 256 ? 26.115  -27.014 91.512  1.00 68.16  ?  265 GLY A HA2  1 
ATOM   3969  H HA3  . GLY A 1 256 ? 26.568  -25.774 92.362  1.00 68.16  ?  265 GLY A HA3  1 
ATOM   3970  N N    . GLN A 1 257 ? 29.003  -26.082 90.720  1.00 65.74  ?  266 GLN A N    1 
ATOM   3971  C CA   . GLN A 1 257 ? 29.840  -25.726 89.588  1.00 58.12  ?  266 GLN A CA   1 
ATOM   3972  C C    . GLN A 1 257 ? 29.910  -26.833 88.538  1.00 62.28  ?  266 GLN A C    1 
ATOM   3973  O O    . GLN A 1 257 ? 30.385  -26.558 87.426  1.00 59.77  ?  266 GLN A O    1 
ATOM   3974  C CB   . GLN A 1 257 ? 31.234  -25.416 90.096  1.00 62.85  ?  266 GLN A CB   1 
ATOM   3975  C CG   . GLN A 1 257 ? 31.245  -24.273 91.006  1.00 82.25  ?  266 GLN A CG   1 
ATOM   3976  C CD   . GLN A 1 257 ? 32.521  -24.133 91.736  1.00 72.21  ?  266 GLN A CD   1 
ATOM   3977  O OE1  . GLN A 1 257 ? 33.315  -25.093 91.857  1.00 55.81  ?  266 GLN A OE1  1 
ATOM   3978  N NE2  . GLN A 1 257 ? 32.781  -22.904 92.194  1.00 78.68  ?  266 GLN A NE2  1 
ATOM   3979  H H    . GLN A 1 257 ? 29.442  -26.341 91.413  1.00 78.88  ?  266 GLN A H    1 
ATOM   3980  H HA   . GLN A 1 257 ? 29.485  -24.928 89.165  1.00 69.74  ?  266 GLN A HA   1 
ATOM   3981  H HB2  . GLN A 1 257 ? 31.576  -26.187 90.575  1.00 75.42  ?  266 GLN A HB2  1 
ATOM   3982  H HB3  . GLN A 1 257 ? 31.808  -25.209 89.343  1.00 75.42  ?  266 GLN A HB3  1 
ATOM   3983  H HG2  . GLN A 1 257 ? 31.102  -23.461 90.494  1.00 98.70  ?  266 GLN A HG2  1 
ATOM   3984  H HG3  . GLN A 1 257 ? 30.536  -24.382 91.659  1.00 98.70  ?  266 GLN A HG3  1 
ATOM   3985  H HE21 . GLN A 1 257 ? 32.221  -22.266 92.054  1.00 94.42  ?  266 GLN A HE21 1 
ATOM   3986  H HE22 . GLN A 1 257 ? 33.507  -22.752 92.629  1.00 94.42  ?  266 GLN A HE22 1 
ATOM   3987  N N    . SER A 1 258 ? 29.430  -28.052 88.831  1.00 69.40  ?  267 SER A N    1 
ATOM   3988  C CA   . SER A 1 258 ? 29.358  -29.097 87.810  1.00 65.53  ?  267 SER A CA   1 
ATOM   3989  C C    . SER A 1 258 ? 28.327  -28.748 86.743  1.00 68.56  ?  267 SER A C    1 
ATOM   3990  O O    . SER A 1 258 ? 27.176  -28.470 87.063  1.00 85.46  ?  267 SER A O    1 
ATOM   3991  C CB   . SER A 1 258 ? 28.988  -30.428 88.458  1.00 75.02  ?  267 SER A CB   1 
ATOM   3992  O OG   . SER A 1 258 ? 28.571  -31.409 87.469  1.00 52.20  ?  267 SER A OG   1 
ATOM   3993  H H    . SER A 1 258 ? 29.144  -28.292 89.606  1.00 83.28  ?  267 SER A H    1 
ATOM   3994  H HA   . SER A 1 258 ? 30.224  -29.193 87.382  1.00 78.63  ?  267 SER A HA   1 
ATOM   3995  H HB2  . SER A 1 258 ? 29.761  -30.771 88.933  1.00 90.02  ?  267 SER A HB2  1 
ATOM   3996  H HB3  . SER A 1 258 ? 28.258  -30.281 89.080  1.00 90.02  ?  267 SER A HB3  1 
ATOM   3997  H HG   . SER A 1 258 ? 28.373  -32.132 87.847  1.00 62.64  ?  267 SER A HG   1 
ATOM   3998  N N    . SER A 1 259 ? 28.716  -28.750 85.470  1.00 53.49  ?  268 SER A N    1 
ATOM   3999  C CA   . SER A 1 259 ? 27.696  -28.514 84.446  1.00 56.71  ?  268 SER A CA   1 
ATOM   4000  C C    . SER A 1 259 ? 26.610  -29.553 84.558  1.00 59.15  ?  268 SER A C    1 
ATOM   4001  O O    . SER A 1 259 ? 25.424  -29.230 84.651  1.00 83.65  ?  268 SER A O    1 
ATOM   4002  C CB   . SER A 1 259 ? 28.274  -28.618 83.041  1.00 121.06 ?  268 SER A CB   1 
ATOM   4003  O OG   . SER A 1 259 ? 29.289  -27.709 82.863  1.00 65.79  ?  268 SER A OG   1 
ATOM   4004  H H    . SER A 1 259 ? 29.516  -28.876 85.183  1.00 64.19  ?  268 SER A H    1 
ATOM   4005  H HA   . SER A 1 259 ? 27.305  -27.635 84.563  1.00 68.05  ?  268 SER A HA   1 
ATOM   4006  H HB2  . SER A 1 259 ? 28.624  -29.513 82.909  1.00 145.27 ?  268 SER A HB2  1 
ATOM   4007  H HB3  . SER A 1 259 ? 27.572  -28.437 82.397  1.00 145.27 ?  268 SER A HB3  1 
ATOM   4008  H HG   . SER A 1 259 ? 29.600  -27.775 82.086  1.00 78.95  ?  268 SER A HG   1 
ATOM   4009  N N    . VAL A 1 260 ? 27.039  -30.804 84.703  1.00 64.19  ?  269 VAL A N    1 
ATOM   4010  C CA   . VAL A 1 260 ? 26.188  -31.964 84.741  1.00 77.37  ?  269 VAL A CA   1 
ATOM   4011  C C    . VAL A 1 260 ? 25.184  -31.823 85.863  1.00 67.00  ?  269 VAL A C    1 
ATOM   4012  O O    . VAL A 1 260 ? 24.075  -32.349 85.789  1.00 72.37  ?  269 VAL A O    1 
ATOM   4013  C CB   . VAL A 1 260 ? 27.111  -33.201 84.867  1.00 62.26  ?  269 VAL A CB   1 
ATOM   4014  C CG1  . VAL A 1 260 ? 26.554  -34.254 85.796  1.00 75.53  ?  269 VAL A CG1  1 
ATOM   4015  C CG2  . VAL A 1 260 ? 27.261  -33.835 83.487  1.00 65.77  ?  269 VAL A CG2  1 
ATOM   4016  H H    . VAL A 1 260 ? 27.871  -31.004 84.786  1.00 77.03  ?  269 VAL A H    1 
ATOM   4017  H HA   . VAL A 1 260 ? 25.701  -32.032 83.905  1.00 92.85  ?  269 VAL A HA   1 
ATOM   4018  H HB   . VAL A 1 260 ? 27.986  -32.931 85.185  1.00 74.71  ?  269 VAL A HB   1 
ATOM   4019  H HG11 . VAL A 1 260 ? 27.173  -35.000 85.834  1.00 90.63  ?  269 VAL A HG11 1 
ATOM   4020  H HG12 . VAL A 1 260 ? 26.445  -33.868 86.680  1.00 90.63  ?  269 VAL A HG12 1 
ATOM   4021  H HG13 . VAL A 1 260 ? 25.696  -34.552 85.457  1.00 90.63  ?  269 VAL A HG13 1 
ATOM   4022  H HG21 . VAL A 1 260 ? 27.838  -34.612 83.557  1.00 78.93  ?  269 VAL A HG21 1 
ATOM   4023  H HG22 . VAL A 1 260 ? 26.385  -34.102 83.166  1.00 78.93  ?  269 VAL A HG22 1 
ATOM   4024  H HG23 . VAL A 1 260 ? 27.652  -33.186 82.882  1.00 78.93  ?  269 VAL A HG23 1 
ATOM   4025  N N    . PHE A 1 261 ? 25.552  -31.131 86.921  1.00 51.77  ?  270 PHE A N    1 
ATOM   4026  C CA   . PHE A 1 261 ? 24.615  -30.912 88.003  1.00 55.70  ?  270 PHE A CA   1 
ATOM   4027  C C    . PHE A 1 261 ? 23.502  -29.920 87.603  1.00 74.45  ?  270 PHE A C    1 
ATOM   4028  O O    . PHE A 1 261 ? 22.546  -29.724 88.356  1.00 93.17  ?  270 PHE A O    1 
ATOM   4029  C CB   . PHE A 1 261 ? 25.417  -30.438 89.210  1.00 60.62  ?  270 PHE A CB   1 
ATOM   4030  C CG   . PHE A 1 261 ? 24.611  -30.272 90.459  1.00 65.95  ?  270 PHE A CG   1 
ATOM   4031  C CD1  . PHE A 1 261 ? 23.896  -29.121 90.688  1.00 78.83  ?  270 PHE A CD1  1 
ATOM   4032  C CD2  . PHE A 1 261 ? 24.611  -31.262 91.431  1.00 89.59  ?  270 PHE A CD2  1 
ATOM   4033  C CE1  . PHE A 1 261 ? 23.167  -28.979 91.863  1.00 89.11  ?  270 PHE A CE1  1 
ATOM   4034  C CE2  . PHE A 1 261 ? 23.891  -31.116 92.607  1.00 102.10 ?  270 PHE A CE2  1 
ATOM   4035  C CZ   . PHE A 1 261 ? 23.180  -29.972 92.824  1.00 88.37  ?  270 PHE A CZ   1 
ATOM   4036  H H    . PHE A 1 261 ? 26.328  -30.780 87.038  1.00 62.12  ?  270 PHE A H    1 
ATOM   4037  H HA   . PHE A 1 261 ? 24.196  -31.756 88.234  1.00 66.84  ?  270 PHE A HA   1 
ATOM   4038  H HB2  . PHE A 1 261 ? 26.114  -31.087 89.394  1.00 72.74  ?  270 PHE A HB2  1 
ATOM   4039  H HB3  . PHE A 1 261 ? 25.815  -29.579 89.001  1.00 72.74  ?  270 PHE A HB3  1 
ATOM   4040  H HD1  . PHE A 1 261 ? 23.888  -28.444 90.051  1.00 94.60  ?  270 PHE A HD1  1 
ATOM   4041  H HD2  . PHE A 1 261 ? 25.102  -32.039 91.290  1.00 107.51 ?  270 PHE A HD2  1 
ATOM   4042  H HE1  . PHE A 1 261 ? 22.681  -28.200 92.012  1.00 106.93 ?  270 PHE A HE1  1 
ATOM   4043  H HE2  . PHE A 1 261 ? 23.896  -31.791 93.246  1.00 122.52 ?  270 PHE A HE2  1 
ATOM   4044  H HZ   . PHE A 1 261 ? 22.686  -29.871 93.605  1.00 106.04 ?  270 PHE A HZ   1 
ATOM   4045  N N    . GLN A 1 262 ? 23.662  -29.239 86.478  1.00 60.37  ?  271 GLN A N    1 
ATOM   4046  C CA   . GLN A 1 262 ? 22.758  -28.232 85.951  1.00 61.20  ?  271 GLN A CA   1 
ATOM   4047  C C    . GLN A 1 262 ? 22.197  -28.607 84.587  1.00 70.96  ?  271 GLN A C    1 
ATOM   4048  O O    . GLN A 1 262 ? 21.033  -28.372 84.327  1.00 85.03  ?  271 GLN A O    1 
ATOM   4049  C CB   . GLN A 1 262 ? 23.527  -26.879 85.846  1.00 82.12  ?  271 GLN A CB   1 
ATOM   4050  C CG   . GLN A 1 262 ? 24.007  -26.268 87.190  1.00 85.47  ?  271 GLN A CG   1 
ATOM   4051  C CD   . GLN A 1 262 ? 24.133  -24.691 87.221  1.00 68.72  ?  271 GLN A CD   1 
ATOM   4052  O OE1  . GLN A 1 262 ? 23.524  -23.965 86.410  1.00 69.98  ?  271 GLN A OE1  1 
ATOM   4053  N NE2  . GLN A 1 262 ? 24.856  -24.181 88.227  1.00 69.18  ?  271 GLN A NE2  1 
ATOM   4054  H H    . GLN A 1 262 ? 24.343  -29.355 85.966  1.00 72.45  ?  271 GLN A H    1 
ATOM   4055  H HA   . GLN A 1 262 ? 22.016  -28.114 86.565  1.00 73.45  ?  271 GLN A HA   1 
ATOM   4056  H HB2  . GLN A 1 262 ? 24.312  -27.016 85.293  1.00 98.54  ?  271 GLN A HB2  1 
ATOM   4057  H HB3  . GLN A 1 262 ? 22.944  -26.229 85.424  1.00 98.54  ?  271 GLN A HB3  1 
ATOM   4058  H HG2  . GLN A 1 262 ? 23.378  -26.522 87.884  1.00 102.57 ?  271 GLN A HG2  1 
ATOM   4059  H HG3  . GLN A 1 262 ? 24.881  -26.633 87.398  1.00 102.57 ?  271 GLN A HG3  1 
ATOM   4060  H HE21 . GLN A 1 262 ? 25.217  -24.705 88.806  1.00 83.02  ?  271 GLN A HE21 1 
ATOM   4061  H HE22 . GLN A 1 262 ? 24.959  -23.330 88.295  1.00 83.02  ?  271 GLN A HE22 1 
ATOM   4062  N N    . CYS A 1 263 ? 22.966  -29.259 83.726  1.00 58.85  ?  272 CYS A N    1 
ATOM   4063  C CA   . CYS A 1 263 ? 22.565  -29.296 82.331  1.00 162.50 ?  272 CYS A CA   1 
ATOM   4064  C C    . CYS A 1 263 ? 21.300  -30.081 82.127  1.00 72.26  ?  272 CYS A C    1 
ATOM   4065  O O    . CYS A 1 263 ? 20.557  -29.812 81.183  1.00 142.73 ?  272 CYS A O    1 
ATOM   4066  C CB   . CYS A 1 263 ? 23.662  -29.923 81.503  1.00 202.92 ?  272 CYS A CB   1 
ATOM   4067  S SG   . CYS A 1 263 ? 23.839  -31.597 81.937  1.00 236.25 ?  272 CYS A SG   1 
ATOM   4068  H H    . CYS A 1 263 ? 23.697  -29.671 83.914  1.00 70.62  ?  272 CYS A H    1 
ATOM   4069  H HA   . CYS A 1 263 ? 22.419  -28.392 82.013  1.00 195.00 ?  272 CYS A HA   1 
ATOM   4070  H HB2  . CYS A 1 263 ? 23.431  -29.870 80.562  1.00 243.50 ?  272 CYS A HB2  1 
ATOM   4071  H HB3  . CYS A 1 263 ? 24.501  -29.468 81.675  1.00 243.50 ?  272 CYS A HB3  1 
ATOM   4072  H HG   . CYS A 1 263 ? 22.803  -32.166 81.730  1.00 283.49 ?  272 CYS A HG   1 
ATOM   4073  N N    . PHE A 1 264 ? 21.012  -31.012 83.004  1.00 97.61  ?  273 PHE A N    1 
ATOM   4074  C CA   . PHE A 1 264 ? 19.865  -31.845 82.743  1.00 67.10  ?  273 PHE A CA   1 
ATOM   4075  C C    . PHE A 1 264 ? 18.602  -31.227 83.276  1.00 50.75  ?  273 PHE A C    1 
ATOM   4076  O O    . PHE A 1 264 ? 17.541  -31.361 82.643  1.00 56.13  ?  273 PHE A O    1 
ATOM   4077  C CB   . PHE A 1 264 ? 20.081  -33.259 83.320  1.00 126.23 ?  273 PHE A CB   1 
ATOM   4078  C CG   . PHE A 1 264 ? 21.121  -34.011 82.575  1.00 75.48  ?  273 PHE A CG   1 
ATOM   4079  C CD1  . PHE A 1 264 ? 20.894  -34.412 81.252  1.00 60.50  ?  273 PHE A CD1  1 
ATOM   4080  C CD2  . PHE A 1 264 ? 22.373  -34.214 83.127  1.00 66.96  ?  273 PHE A CD2  1 
ATOM   4081  C CE1  . PHE A 1 264 ? 21.906  -35.054 80.510  1.00 73.51  ?  273 PHE A CE1  1 
ATOM   4082  C CE2  . PHE A 1 264 ? 23.387  -34.842 82.392  1.00 73.63  ?  273 PHE A CE2  1 
ATOM   4083  C CZ   . PHE A 1 264 ? 23.168  -35.254 81.083  1.00 65.03  ?  273 PHE A CZ   1 
ATOM   4084  H H    . PHE A 1 264 ? 21.444  -31.180 83.729  1.00 117.14 ?  273 PHE A H    1 
ATOM   4085  H HA   . PHE A 1 264 ? 19.762  -31.934 81.783  1.00 80.52  ?  273 PHE A HA   1 
ATOM   4086  H HB2  . PHE A 1 264 ? 20.365  -33.185 84.245  1.00 151.47 ?  273 PHE A HB2  1 
ATOM   4087  H HB3  . PHE A 1 264 ? 19.250  -33.756 83.264  1.00 151.47 ?  273 PHE A HB3  1 
ATOM   4088  H HD1  . PHE A 1 264 ? 20.063  -34.260 80.861  1.00 72.60  ?  273 PHE A HD1  1 
ATOM   4089  H HD2  . PHE A 1 264 ? 22.546  -33.924 83.993  1.00 80.36  ?  273 PHE A HD2  1 
ATOM   4090  H HE1  . PHE A 1 264 ? 21.740  -35.331 79.639  1.00 88.22  ?  273 PHE A HE1  1 
ATOM   4091  H HE2  . PHE A 1 264 ? 24.217  -34.986 82.787  1.00 88.35  ?  273 PHE A HE2  1 
ATOM   4092  H HZ   . PHE A 1 264 ? 23.834  -35.698 80.610  1.00 78.04  ?  273 PHE A HZ   1 
ATOM   4093  N N    . ASP A 1 265 ? 18.699  -30.539 84.415  1.00 50.54  ?  274 ASP A N    1 
ATOM   4094  C CA   . ASP A 1 265 ? 17.574  -29.768 84.903  1.00 64.98  ?  274 ASP A CA   1 
ATOM   4095  C C    . ASP A 1 265 ? 17.129  -28.773 83.857  1.00 73.82  ?  274 ASP A C    1 
ATOM   4096  O O    . ASP A 1 265 ? 15.937  -28.593 83.600  1.00 82.88  ?  274 ASP A O    1 
ATOM   4097  C CB   . ASP A 1 265 ? 17.985  -29.058 86.172  1.00 52.53  ?  274 ASP A CB   1 
ATOM   4098  C CG   . ASP A 1 265 ? 18.447  -29.987 87.238  1.00 78.54  ?  274 ASP A CG   1 
ATOM   4099  O OD1  . ASP A 1 265 ? 17.570  -30.581 87.919  1.00 80.45  ?  274 ASP A OD1  1 
ATOM   4100  O OD2  . ASP A 1 265 ? 19.680  -30.146 87.383  1.00 131.91 -1 274 ASP A OD2  1 
ATOM   4101  H H    . ASP A 1 265 ? 19.400  -30.507 84.913  1.00 60.65  ?  274 ASP A H    1 
ATOM   4102  H HA   . ASP A 1 265 ? 16.834  -30.361 85.104  1.00 77.97  ?  274 ASP A HA   1 
ATOM   4103  H HB2  . ASP A 1 265 ? 18.712  -28.449 85.971  1.00 63.04  ?  274 ASP A HB2  1 
ATOM   4104  H HB3  . ASP A 1 265 ? 17.224  -28.564 86.517  1.00 63.04  ?  274 ASP A HB3  1 
ATOM   4105  N N    . VAL A 1 266 ? 18.097  -28.144 83.232  1.00 58.10  ?  275 VAL A N    1 
ATOM   4106  C CA   . VAL A 1 266 ? 17.826  -27.128 82.236  1.00 81.98  ?  275 VAL A CA   1 
ATOM   4107  C C    . VAL A 1 266 ? 17.198  -27.746 80.996  1.00 75.51  ?  275 VAL A C    1 
ATOM   4108  O O    . VAL A 1 266 ? 16.217  -27.225 80.441  1.00 71.76  ?  275 VAL A O    1 
ATOM   4109  C CB   . VAL A 1 266 ? 19.158  -26.392 81.971  1.00 63.51  ?  275 VAL A CB   1 
ATOM   4110  C CG1  . VAL A 1 266 ? 19.162  -25.654 80.675  1.00 71.73  ?  275 VAL A CG1  1 
ATOM   4111  C CG2  . VAL A 1 266 ? 19.399  -25.466 83.115  1.00 103.23 ?  275 VAL A CG2  1 
ATOM   4112  H H    . VAL A 1 266 ? 18.934  -28.287 83.366  1.00 69.72  ?  275 VAL A H    1 
ATOM   4113  H HA   . VAL A 1 266 ? 17.196  -26.486 82.602  1.00 98.37  ?  275 VAL A HA   1 
ATOM   4114  H HB   . VAL A 1 266 ? 19.880  -27.040 81.951  1.00 76.21  ?  275 VAL A HB   1 
ATOM   4115  H HG11 . VAL A 1 266 ? 20.020  -25.215 80.565  1.00 86.08  ?  275 VAL A HG11 1 
ATOM   4116  H HG12 . VAL A 1 266 ? 19.017  -26.285 79.952  1.00 86.08  ?  275 VAL A HG12 1 
ATOM   4117  H HG13 . VAL A 1 266 ? 18.451  -24.994 80.686  1.00 86.08  ?  275 VAL A HG13 1 
ATOM   4118  H HG21 . VAL A 1 266 ? 20.233  -24.994 82.969  1.00 123.87 ?  275 VAL A HG21 1 
ATOM   4119  H HG22 . VAL A 1 266 ? 18.665  -24.834 83.169  1.00 123.87 ?  275 VAL A HG22 1 
ATOM   4120  H HG23 . VAL A 1 266 ? 19.451  -25.984 83.934  1.00 123.87 ?  275 VAL A HG23 1 
ATOM   4121  N N    . LEU A 1 267 ? 17.749  -28.874 80.566  1.00 79.37  ?  276 LEU A N    1 
ATOM   4122  C CA   . LEU A 1 267 ? 17.216  -29.608 79.433  1.00 56.51  ?  276 LEU A CA   1 
ATOM   4123  C C    . LEU A 1 267 ? 15.751  -29.952 79.644  1.00 76.32  ?  276 LEU A C    1 
ATOM   4124  O O    . LEU A 1 267 ? 14.945  -29.882 78.721  1.00 58.24  ?  276 LEU A O    1 
ATOM   4125  C CB   . LEU A 1 267 ? 18.012  -30.884 79.280  1.00 71.89  ?  276 LEU A CB   1 
ATOM   4126  C CG   . LEU A 1 267 ? 17.416  -31.838 78.270  1.00 69.08  ?  276 LEU A CG   1 
ATOM   4127  C CD1  . LEU A 1 267 ? 17.526  -31.251 76.875  1.00 64.76  ?  276 LEU A CD1  1 
ATOM   4128  C CD2  . LEU A 1 267 ? 18.071  -33.180 78.367  1.00 45.15  ?  276 LEU A CD2  1 
ATOM   4129  H H    . LEU A 1 267 ? 18.443  -29.239 80.921  1.00 95.24  ?  276 LEU A H    1 
ATOM   4130  H HA   . LEU A 1 267 ? 17.303  -29.080 78.624  1.00 67.81  ?  276 LEU A HA   1 
ATOM   4131  H HB2  . LEU A 1 267 ? 18.910  -30.661 78.987  1.00 86.27  ?  276 LEU A HB2  1 
ATOM   4132  H HB3  . LEU A 1 267 ? 18.046  -31.338 80.136  1.00 86.27  ?  276 LEU A HB3  1 
ATOM   4133  H HG   . LEU A 1 267 ? 16.473  -31.954 78.469  1.00 82.89  ?  276 LEU A HG   1 
ATOM   4134  H HD11 . LEU A 1 267 ? 17.140  -31.874 76.240  1.00 77.71  ?  276 LEU A HD11 1 
ATOM   4135  H HD12 . LEU A 1 267 ? 17.045  -30.409 76.848  1.00 77.71  ?  276 LEU A HD12 1 
ATOM   4136  H HD13 . LEU A 1 267 ? 18.463  -31.104 76.668  1.00 77.71  ?  276 LEU A HD13 1 
ATOM   4137  H HD21 . LEU A 1 267 ? 17.672  -33.773 77.711  1.00 54.19  ?  276 LEU A HD21 1 
ATOM   4138  H HD22 . LEU A 1 267 ? 19.020  -33.081 78.191  1.00 54.19  ?  276 LEU A HD22 1 
ATOM   4139  H HD23 . LEU A 1 267 ? 17.934  -33.534 79.259  1.00 54.19  ?  276 LEU A HD23 1 
ATOM   4140  N N    . LEU A 1 268 ? 15.417  -30.437 80.826  1.00 46.07  ?  277 LEU A N    1 
ATOM   4141  C CA   . LEU A 1 268 ? 14.068  -30.894 81.092  1.00 73.94  ?  277 LEU A CA   1 
ATOM   4142  C C    . LEU A 1 268 ? 13.100  -29.763 81.424  1.00 72.71  ?  277 LEU A C    1 
ATOM   4143  O O    . LEU A 1 268 ? 11.955  -30.038 81.758  1.00 96.79  ?  277 LEU A O    1 
ATOM   4144  C CB   . LEU A 1 268 ? 14.124  -31.921 82.224  1.00 74.23  ?  277 LEU A CB   1 
ATOM   4145  C CG   . LEU A 1 268 ? 14.936  -33.159 81.813  1.00 60.12  ?  277 LEU A CG   1 
ATOM   4146  C CD1  . LEU A 1 268 ? 15.219  -34.076 82.990  1.00 90.99  ?  277 LEU A CD1  1 
ATOM   4147  C CD2  . LEU A 1 268 ? 14.215  -33.955 80.698  1.00 45.98  ?  277 LEU A CD2  1 
ATOM   4148  H H    . LEU A 1 268 ? 15.954  -30.513 81.493  1.00 55.29  ?  277 LEU A H    1 
ATOM   4149  H HA   . LEU A 1 268 ? 13.731  -31.344 80.302  1.00 88.73  ?  277 LEU A HA   1 
ATOM   4150  H HB2  . LEU A 1 268 ? 14.549  -31.521 82.999  1.00 89.08  ?  277 LEU A HB2  1 
ATOM   4151  H HB3  . LEU A 1 268 ? 13.223  -32.207 82.443  1.00 89.08  ?  277 LEU A HB3  1 
ATOM   4152  H HG   . LEU A 1 268 ? 15.790  -32.865 81.458  1.00 72.15  ?  277 LEU A HG   1 
ATOM   4153  H HD11 . LEU A 1 268 ? 15.732  -34.838 82.680  1.00 109.19 ?  277 LEU A HD11 1 
ATOM   4154  H HD12 . LEU A 1 268 ? 15.726  -33.585 83.657  1.00 109.19 ?  277 LEU A HD12 1 
ATOM   4155  H HD13 . LEU A 1 268 ? 14.377  -34.374 83.367  1.00 109.19 ?  277 LEU A HD13 1 
ATOM   4156  H HD21 . LEU A 1 268 ? 14.753  -34.728 80.464  1.00 55.17  ?  277 LEU A HD21 1 
ATOM   4157  H HD22 . LEU A 1 268 ? 13.349  -34.243 81.027  1.00 55.17  ?  277 LEU A HD22 1 
ATOM   4158  H HD23 . LEU A 1 268 ? 14.102  -33.383 79.924  1.00 55.17  ?  277 LEU A HD23 1 
ATOM   4159  N N    . GLY A 1 269 ? 13.542  -28.509 81.342  1.00 65.55  ?  278 GLY A N    1 
ATOM   4160  C CA   . GLY A 1 269 ? 12.696  -27.352 81.554  1.00 60.62  ?  278 GLY A CA   1 
ATOM   4161  C C    . GLY A 1 269 ? 12.307  -27.137 82.995  1.00 74.80  ?  278 GLY A C    1 
ATOM   4162  O O    . GLY A 1 269 ? 11.210  -26.647 83.284  1.00 147.90 ?  278 GLY A O    1 
ATOM   4163  H H    . GLY A 1 269 ? 14.356  -28.304 81.157  1.00 78.66  ?  278 GLY A H    1 
ATOM   4164  H HA2  . GLY A 1 269 ? 13.158  -26.558 81.244  1.00 72.74  ?  278 GLY A HA2  1 
ATOM   4165  H HA3  . GLY A 1 269 ? 11.883  -27.453 81.034  1.00 72.74  ?  278 GLY A HA3  1 
ATOM   4166  N N    . ILE A 1 270 ? 13.195  -27.489 83.906  1.00 53.34  ?  279 ILE A N    1 
ATOM   4167  C CA   . ILE A 1 270 ? 13.015  -27.267 85.339  1.00 66.28  ?  279 ILE A CA   1 
ATOM   4168  C C    . ILE A 1 270 ? 13.606  -25.906 85.698  1.00 141.89 ?  279 ILE A C    1 
ATOM   4169  O O    . ILE A 1 270 ? 14.825  -25.721 85.662  1.00 131.07 ?  279 ILE A O    1 
ATOM   4170  C CB   . ILE A 1 270 ? 13.679  -28.395 86.138  1.00 56.01  ?  279 ILE A CB   1 
ATOM   4171  C CG1  . ILE A 1 270 ? 13.111  -29.764 85.680  1.00 91.35  ?  279 ILE A CG1  1 
ATOM   4172  C CG2  . ILE A 1 270 ? 13.597  -28.162 87.650  1.00 67.01  ?  279 ILE A CG2  1 
ATOM   4173  C CD1  . ILE A 1 270 ? 13.822  -30.990 86.224  1.00 65.17  ?  279 ILE A CD1  1 
ATOM   4174  H H    . ILE A 1 270 ? 13.941  -27.873 83.717  1.00 64.01  ?  279 ILE A H    1 
ATOM   4175  H HA   . ILE A 1 270 ? 12.068  -27.258 85.549  1.00 79.53  ?  279 ILE A HA   1 
ATOM   4176  H HB   . ILE A 1 270 ? 14.621  -28.389 85.905  1.00 67.21  ?  279 ILE A HB   1 
ATOM   4177  H HG12 . ILE A 1 270 ? 12.184  -29.819 85.959  1.00 109.62 ?  279 ILE A HG12 1 
ATOM   4178  H HG13 . ILE A 1 270 ? 13.160  -29.806 84.712  1.00 109.62 ?  279 ILE A HG13 1 
ATOM   4179  H HG21 . ILE A 1 270 ? 14.029  -28.900 88.106  1.00 80.42  ?  279 ILE A HG21 1 
ATOM   4180  H HG22 . ILE A 1 270 ? 14.045  -27.330 87.865  1.00 80.42  ?  279 ILE A HG22 1 
ATOM   4181  H HG23 . ILE A 1 270 ? 12.664  -28.113 87.910  1.00 80.42  ?  279 ILE A HG23 1 
ATOM   4182  H HD11 . ILE A 1 270 ? 13.389  -31.785 85.877  1.00 78.20  ?  279 ILE A HD11 1 
ATOM   4183  H HD12 . ILE A 1 270 ? 14.750  -30.968 85.941  1.00 78.20  ?  279 ILE A HD12 1 
ATOM   4184  H HD13 . ILE A 1 270 ? 13.771  -30.981 87.193  1.00 78.20  ?  279 ILE A HD13 1 
ATOM   4185  N N    . GLN A 1 271 ? 12.754  -24.965 86.105  1.00 159.72 ?  280 GLN A N    1 
ATOM   4186  C CA   . GLN A 1 271 ? 13.177  -23.579 86.311  1.00 127.85 ?  280 GLN A CA   1 
ATOM   4187  C C    . GLN A 1 271 ? 13.931  -23.415 87.635  1.00 94.42  ?  280 GLN A C    1 
ATOM   4188  O O    . GLN A 1 271 ? 13.478  -22.765 88.579  1.00 94.57  ?  280 GLN A O    1 
ATOM   4189  C CB   . GLN A 1 271 ? 11.961  -22.673 86.259  1.00 127.68 ?  280 GLN A CB   1 
ATOM   4190  C CG   . GLN A 1 271 ? 11.233  -22.756 84.967  1.00 132.70 ?  280 GLN A CG   1 
ATOM   4191  C CD   . GLN A 1 271 ? 12.105  -22.346 83.818  1.00 136.25 ?  280 GLN A CD   1 
ATOM   4192  O OE1  . GLN A 1 271 ? 13.069  -21.595 83.990  1.00 200.40 ?  280 GLN A OE1  1 
ATOM   4193  N NE2  . GLN A 1 271 ? 11.791  -22.849 82.639  1.00 141.78 ?  280 GLN A NE2  1 
ATOM   4194  H H    . GLN A 1 271 ? 11.921  -25.104 86.269  1.00 191.66 ?  280 GLN A H    1 
ATOM   4195  H HA   . GLN A 1 271 ? 13.775  -23.320 85.592  1.00 153.43 ?  280 GLN A HA   1 
ATOM   4196  H HB2  . GLN A 1 271 ? 11.347  -22.927 86.966  1.00 153.21 ?  280 GLN A HB2  1 
ATOM   4197  H HB3  . GLN A 1 271 ? 12.247  -21.754 86.383  1.00 153.21 ?  280 GLN A HB3  1 
ATOM   4198  H HG2  . GLN A 1 271 ? 10.946  -23.671 84.819  1.00 159.24 ?  280 GLN A HG2  1 
ATOM   4199  H HG3  . GLN A 1 271 ? 10.466  -22.163 84.992  1.00 159.24 ?  280 GLN A HG3  1 
ATOM   4200  H HE21 . GLN A 1 271 ? 11.118  -23.380 82.563  1.00 170.14 ?  280 GLN A HE21 1 
ATOM   4201  H HE22 . GLN A 1 271 ? 12.259  -22.647 81.946  1.00 170.14 ?  280 GLN A HE22 1 
ATOM   4202  N N    . GLN A 1 272 ? 15.143  -23.974 87.664  1.00 72.13  ?  281 GLN A N    1 
ATOM   4203  C CA   . GLN A 1 272 ? 15.998  -23.906 88.857  1.00 100.34 ?  281 GLN A CA   1 
ATOM   4204  C C    . GLN A 1 272 ? 16.529  -22.505 89.125  1.00 122.81 ?  281 GLN A C    1 
ATOM   4205  O O    . GLN A 1 272 ? 16.802  -22.155 90.280  1.00 123.32 ?  281 GLN A O    1 
ATOM   4206  C CB   . GLN A 1 272 ? 17.209  -24.823 88.701  1.00 94.06  ?  281 GLN A CB   1 
ATOM   4207  C CG   . GLN A 1 272 ? 16.906  -26.329 88.576  1.00 108.74 ?  281 GLN A CG   1 
ATOM   4208  C CD   . GLN A 1 272 ? 16.523  -26.992 89.895  1.00 136.51 ?  281 GLN A CD   1 
ATOM   4209  O OE1  . GLN A 1 272 ? 16.160  -26.328 90.866  1.00 130.78 ?  281 GLN A OE1  1 
ATOM   4210  N NE2  . GLN A 1 272 ? 16.626  -28.305 89.936  1.00 141.67 ?  281 GLN A NE2  1 
ATOM   4211  H H    . GLN A 1 272 ? 15.495  -24.400 87.006  1.00 86.56  ?  281 GLN A H    1 
ATOM   4212  H HA   . GLN A 1 272 ? 15.492  -24.195 89.633  1.00 120.41 ?  281 GLN A HA   1 
ATOM   4213  H HB2  . GLN A 1 272 ? 17.691  -24.558 87.901  1.00 112.87 ?  281 GLN A HB2  1 
ATOM   4214  H HB3  . GLN A 1 272 ? 17.782  -24.707 89.475  1.00 112.87 ?  281 GLN A HB3  1 
ATOM   4215  H HG2  . GLN A 1 272 ? 16.167  -26.448 87.958  1.00 130.48 ?  281 GLN A HG2  1 
ATOM   4216  H HG3  . GLN A 1 272 ? 17.695  -26.779 88.235  1.00 130.48 ?  281 GLN A HG3  1 
ATOM   4217  H HE21 . GLN A 1 272 ? 16.897  -28.737 89.244  1.00 170.00 ?  281 GLN A HE21 1 
ATOM   4218  H HE22 . GLN A 1 272 ? 16.423  -28.730 90.656  1.00 170.00 ?  281 GLN A HE22 1 
ATOM   4219  N N    . THR A 1 273 ? 16.721  -21.715 88.072  1.00 122.58 ?  282 THR A N    1 
ATOM   4220  C CA   . THR A 1 273 ? 17.284  -20.385 88.189  1.00 141.55 ?  282 THR A CA   1 
ATOM   4221  C C    . THR A 1 273 ? 16.244  -19.273 88.156  1.00 115.91 ?  282 THR A C    1 
ATOM   4222  O O    . THR A 1 273 ? 16.609  -18.106 88.375  1.00 102.99 ?  282 THR A O    1 
ATOM   4223  C CB   . THR A 1 273 ? 18.296  -20.194 87.066  1.00 148.14 ?  282 THR A CB   1 
ATOM   4224  O OG1  . THR A 1 273 ? 17.830  -20.863 85.889  1.00 117.05 ?  282 THR A OG1  1 
ATOM   4225  C CG2  . THR A 1 273 ? 19.557  -20.825 87.453  1.00 122.32 ?  282 THR A CG2  1 
ATOM   4226  H H    . THR A 1 273 ? 16.527  -21.936 87.265  1.00 147.10 ?  282 THR A H    1 
ATOM   4227  H HA   . THR A 1 273 ? 17.760  -20.320 89.031  1.00 169.86 ?  282 THR A HA   1 
ATOM   4228  H HB   . THR A 1 273 ? 18.441  -19.251 86.891  1.00 177.77 ?  282 THR A HB   1 
ATOM   4229  H HG1  . THR A 1 273 ? 18.383  -20.762 85.264  1.00 140.46 ?  282 THR A HG1  1 
ATOM   4230  H HG21 . THR A 1 273 ? 20.214  -20.713 86.749  1.00 146.78 ?  282 THR A HG21 1 
ATOM   4231  H HG22 . THR A 1 273 ? 19.894  -20.418 88.267  1.00 146.78 ?  282 THR A HG22 1 
ATOM   4232  H HG23 . THR A 1 273 ? 19.419  -21.773 87.608  1.00 146.78 ?  282 THR A HG23 1 
ATOM   4233  N N    . ALA A 1 274 ? 14.972  -19.606 87.913  1.00 156.60 ?  283 ALA A N    1 
ATOM   4234  C CA   . ALA A 1 274 ? 13.878  -18.641 87.904  1.00 185.60 ?  283 ALA A CA   1 
ATOM   4235  C C    . ALA A 1 274 ? 13.185  -18.617 89.262  1.00 152.75 ?  283 ALA A C    1 
ATOM   4236  O O    . ALA A 1 274 ? 13.316  -19.528 90.084  1.00 139.65 ?  283 ALA A O    1 
ATOM   4237  C CB   . ALA A 1 274 ? 12.859  -18.968 86.802  1.00 162.31 ?  283 ALA A CB   1 
ATOM   4238  H H    . ALA A 1 274 ? 14.715  -20.410 87.746  1.00 187.92 ?  283 ALA A H    1 
ATOM   4239  H HA   . ALA A 1 274 ? 14.235  -17.757 87.731  1.00 222.72 ?  283 ALA A HA   1 
ATOM   4240  H HB1  . ALA A 1 274 ? 12.148  -18.309 86.825  1.00 194.77 ?  283 ALA A HB1  1 
ATOM   4241  H HB2  . ALA A 1 274 ? 13.306  -18.943 85.942  1.00 194.77 ?  283 ALA A HB2  1 
ATOM   4242  H HB3  . ALA A 1 274 ? 12.496  -19.853 86.961  1.00 194.77 ?  283 ALA A HB3  1 
ATOM   4243  N N    . GLY A 1 275 ? 12.395  -17.575 89.476  1.00 123.87 ?  284 GLY A N    1 
ATOM   4244  C CA   . GLY A 1 275 ? 11.685  -17.428 90.709  1.00 163.07 ?  284 GLY A CA   1 
ATOM   4245  C C    . GLY A 1 275 ? 12.508  -16.710 91.751  1.00 150.17 ?  284 GLY A C    1 
ATOM   4246  O O    . GLY A 1 275 ? 11.949  -15.973 92.566  1.00 152.16 ?  284 GLY A O    1 
ATOM   4247  H H    . GLY A 1 275 ? 12.259  -16.940 88.911  1.00 148.64 ?  284 GLY A H    1 
ATOM   4248  H HA2  . GLY A 1 275 ? 10.870  -16.923 90.558  1.00 195.68 ?  284 GLY A HA2  1 
ATOM   4249  H HA3  . GLY A 1 275 ? 11.447  -18.303 91.053  1.00 195.68 ?  284 GLY A HA3  1 
ATOM   4250  N N    . GLY A 1 276 ? 13.831  -16.918 91.734  1.00 150.00 ?  285 GLY A N    1 
ATOM   4251  C CA   . GLY A 1 276 ? 14.803  -16.162 92.524  1.00 144.71 ?  285 GLY A CA   1 
ATOM   4252  C C    . GLY A 1 276 ? 15.129  -16.632 93.935  1.00 130.69 ?  285 GLY A C    1 
ATOM   4253  O O    . GLY A 1 276 ? 15.780  -15.876 94.672  1.00 113.52 ?  285 GLY A O    1 
ATOM   4254  H H    . GLY A 1 276 ? 14.202  -17.523 91.248  1.00 180.00 ?  285 GLY A H    1 
ATOM   4255  H HA2  . GLY A 1 276 ? 15.638  -16.141 92.031  1.00 173.66 ?  285 GLY A HA2  1 
ATOM   4256  H HA3  . GLY A 1 276 ? 14.486  -15.248 92.594  1.00 173.66 ?  285 GLY A HA3  1 
ATOM   4257  N N    . GLY A 1 277 ? 14.759  -17.851 94.327  1.00 137.00 ?  286 GLY A N    1 
ATOM   4258  C CA   . GLY A 1 277 ? 14.992  -18.274 95.695  1.00 123.31 ?  286 GLY A CA   1 
ATOM   4259  C C    . GLY A 1 277 ? 16.466  -18.282 96.003  1.00 112.30 ?  286 GLY A C    1 
ATOM   4260  O O    . GLY A 1 277 ? 17.314  -18.263 95.115  1.00 103.94 ?  286 GLY A O    1 
ATOM   4261  H H    . GLY A 1 277 ? 14.379  -18.438 93.827  1.00 164.40 ?  286 GLY A H    1 
ATOM   4262  H HA2  . GLY A 1 277 ? 14.547  -17.668 96.308  1.00 147.97 ?  286 GLY A HA2  1 
ATOM   4263  H HA3  . GLY A 1 277 ? 14.639  -19.168 95.828  1.00 147.97 ?  286 GLY A HA3  1 
ATOM   4264  N N    . HIS A 1 278 ? 16.789  -18.340 97.292  1.00 103.47 ?  287 HIS A N    1 
ATOM   4265  C CA   . HIS A 1 278 ? 18.204  -18.331 97.629  1.00 88.29  ?  287 HIS A CA   1 
ATOM   4266  C C    . HIS A 1 278 ? 18.920  -19.399 96.819  1.00 86.49  ?  287 HIS A C    1 
ATOM   4267  O O    . HIS A 1 278 ? 19.969  -19.157 96.214  1.00 78.24  ?  287 HIS A O    1 
ATOM   4268  C CB   . HIS A 1 278 ? 18.426  -18.566 99.127  1.00 85.19  ?  287 HIS A CB   1 
ATOM   4269  C CG   . HIS A 1 278 ? 19.878  -18.602 99.519  1.00 64.62  ?  287 HIS A CG   1 
ATOM   4270  H H    . HIS A 1 278 ? 16.242  -18.382 97.954  1.00 124.16 ?  287 HIS A H    1 
ATOM   4271  H HA   . HIS A 1 278 ? 18.583  -17.469 97.398  1.00 105.95 ?  287 HIS A HA   1 
ATOM   4272  H HB2  . HIS A 1 278 ? 18.002  -17.849 99.623  1.00 102.23 ?  287 HIS A HB2  1 
ATOM   4273  H HB3  . HIS A 1 278 ? 18.030  -19.416 99.373  1.00 102.23 ?  287 HIS A HB3  1 
ATOM   4274  N N    . ALA A 1 279 ? 18.308  -20.556 96.708  1.00 82.02  ?  288 ALA A N    1 
ATOM   4275  C CA   . ALA A 1 279 ? 18.917  -21.593 95.924  1.00 77.28  ?  288 ALA A CA   1 
ATOM   4276  C C    . ALA A 1 279 ? 18.916  -21.231 94.460  1.00 93.11  ?  288 ALA A C    1 
ATOM   4277  O O    . ALA A 1 279 ? 19.799  -21.643 93.706  1.00 61.09  ?  288 ALA A O    1 
ATOM   4278  C CB   . ALA A 1 279 ? 18.149  -22.875 96.139  1.00 83.68  ?  288 ALA A CB   1 
ATOM   4279  H H    . ALA A 1 279 ? 17.555  -20.762 97.069  1.00 98.42  ?  288 ALA A H    1 
ATOM   4280  H HA   . ALA A 1 279 ? 19.834  -21.726 96.211  1.00 92.73  ?  288 ALA A HA   1 
ATOM   4281  H HB1  . ALA A 1 279 ? 18.557  -23.579 95.612  1.00 100.42 ?  288 ALA A HB1  1 
ATOM   4282  H HB2  . ALA A 1 279 ? 18.180  -23.106 97.081  1.00 100.42 ?  288 ALA A HB2  1 
ATOM   4283  H HB3  . ALA A 1 279 ? 17.230  -22.742 95.861  1.00 100.42 ?  288 ALA A HB3  1 
ATOM   4284  N N    . ALA A 1 280 ? 17.922  -20.492 94.013  1.00 134.21 ?  289 ALA A N    1 
ATOM   4285  C CA   . ALA A 1 280 ? 17.894  -20.252 92.589  1.00 106.62 ?  289 ALA A CA   1 
ATOM   4286  C C    . ALA A 1 280 ? 19.044  -19.355 92.189  1.00 89.45  ?  289 ALA A C    1 
ATOM   4287  O O    . ALA A 1 280 ? 19.703  -19.606 91.178  1.00 78.74  ?  289 ALA A O    1 
ATOM   4288  C CB   . ALA A 1 280 ? 16.562  -19.656 92.188  1.00 106.49 ?  289 ALA A CB   1 
ATOM   4289  H H    . ALA A 1 280 ? 17.290  -20.139 94.477  1.00 161.05 ?  289 ALA A H    1 
ATOM   4290  H HA   . ALA A 1 280 ? 17.996  -21.096 92.123  1.00 127.94 ?  289 ALA A HA   1 
ATOM   4291  H HB1  . ALA A 1 280 ? 16.561  -19.501 91.231  1.00 127.79 ?  289 ALA A HB1  1 
ATOM   4292  H HB2  . ALA A 1 280 ? 15.855  -20.276 92.424  1.00 127.79 ?  289 ALA A HB2  1 
ATOM   4293  H HB3  . ALA A 1 280 ? 16.438  -18.817 92.660  1.00 127.79 ?  289 ALA A HB3  1 
ATOM   4294  N N    . GLN A 1 281 ? 19.349  -18.347 93.007  1.00 69.57  ?  290 GLN A N    1 
ATOM   4295  C CA   . GLN A 1 281 ? 20.406  -17.429 92.629  1.00 69.97  ?  290 GLN A CA   1 
ATOM   4296  C C    . GLN A 1 281 ? 21.740  -18.148 92.683  1.00 111.88 ?  290 GLN A C    1 
ATOM   4297  O O    . GLN A 1 281 ? 22.540  -18.081 91.749  1.00 75.07  ?  290 GLN A O    1 
ATOM   4298  C CB   . GLN A 1 281 ? 20.398  -16.201 93.546  1.00 58.74  ?  290 GLN A CB   1 
ATOM   4299  C CG   . GLN A 1 281 ? 21.224  -15.000 93.023  1.00 76.25  ?  290 GLN A CG   1 
ATOM   4300  C CD   . GLN A 1 281 ? 20.702  -14.442 91.707  1.00 77.74  ?  290 GLN A CD   1 
ATOM   4301  H H    . GLN A 1 281 ? 18.969  -18.181 93.760  1.00 83.49  ?  290 GLN A H    1 
ATOM   4302  H HA   . GLN A 1 281 ? 20.259  -17.129 91.719  1.00 83.96  ?  290 GLN A HA   1 
ATOM   4303  H HB2  . GLN A 1 281 ? 19.482  -15.902 93.655  1.00 70.49  ?  290 GLN A HB2  1 
ATOM   4304  H HB3  . GLN A 1 281 ? 20.763  -16.456 94.407  1.00 70.49  ?  290 GLN A HB3  1 
ATOM   4305  H HG2  . GLN A 1 281 ? 21.195  -14.289 93.682  1.00 91.50  ?  290 GLN A HG2  1 
ATOM   4306  H HG3  . GLN A 1 281 ? 22.141  -15.286 92.884  1.00 91.50  ?  290 GLN A HG3  1 
ATOM   4307  N N    . PHE A 1 282 ? 21.927  -18.972 93.699  1.00 137.50 ?  291 PHE A N    1 
ATOM   4308  C CA   . PHE A 1 282 ? 23.217  -19.618 93.880  1.00 66.83  ?  291 PHE A CA   1 
ATOM   4309  C C    . PHE A 1 282 ? 23.619  -20.480 92.672  1.00 69.31  ?  291 PHE A C    1 
ATOM   4310  O O    . PHE A 1 282 ? 24.808  -20.652 92.391  1.00 75.11  ?  291 PHE A O    1 
ATOM   4311  C CB   . PHE A 1 282 ? 23.168  -20.461 95.129  1.00 63.23  ?  291 PHE A CB   1 
ATOM   4312  C CG   . PHE A 1 282 ? 24.395  -21.189 95.364  1.00 70.32  ?  291 PHE A CG   1 
ATOM   4313  C CD1  . PHE A 1 282 ? 25.454  -20.581 96.014  1.00 68.68  ?  291 PHE A CD1  1 
ATOM   4314  C CD2  . PHE A 1 282 ? 24.543  -22.473 94.866  1.00 77.25  ?  291 PHE A CD2  1 
ATOM   4315  C CE1  . PHE A 1 282 ? 26.663  -21.249 96.214  1.00 61.17  ?  291 PHE A CE1  1 
ATOM   4316  C CE2  . PHE A 1 282 ? 25.734  -23.155 95.058  1.00 57.99  ?  291 PHE A CE2  1 
ATOM   4317  C CZ   . PHE A 1 282 ? 26.812  -22.527 95.715  1.00 63.33  ?  291 PHE A CZ   1 
ATOM   4318  H H    . PHE A 1 282 ? 21.335  -19.173 94.290  1.00 164.99 ?  291 PHE A H    1 
ATOM   4319  H HA   . PHE A 1 282 ? 23.897  -18.938 94.003  1.00 80.20  ?  291 PHE A HA   1 
ATOM   4320  H HB2  . PHE A 1 282 ? 23.011  -19.885 95.893  1.00 75.88  ?  291 PHE A HB2  1 
ATOM   4321  H HB3  . PHE A 1 282 ? 22.448  -21.106 95.047  1.00 75.88  ?  291 PHE A HB3  1 
ATOM   4322  H HD1  . PHE A 1 282 ? 25.356  -19.712 96.331  1.00 82.42  ?  291 PHE A HD1  1 
ATOM   4323  H HD2  . PHE A 1 282 ? 23.839  -22.882 94.416  1.00 92.70  ?  291 PHE A HD2  1 
ATOM   4324  H HE1  . PHE A 1 282 ? 27.365  -20.831 96.658  1.00 73.40  ?  291 PHE A HE1  1 
ATOM   4325  H HE2  . PHE A 1 282 ? 25.832  -24.020 94.729  1.00 69.59  ?  291 PHE A HE2  1 
ATOM   4326  H HZ   . PHE A 1 282 ? 27.606  -22.992 95.856  1.00 75.99  ?  291 PHE A HZ   1 
ATOM   4327  N N    . LEU A 1 283 ? 22.663  -21.142 92.033  1.00 68.67  ?  292 LEU A N    1 
ATOM   4328  C CA   . LEU A 1 283 ? 22.989  -21.887 90.827  1.00 63.57  ?  292 LEU A CA   1 
ATOM   4329  C C    . LEU A 1 283 ? 23.279  -20.989 89.648  1.00 67.48  ?  292 LEU A C    1 
ATOM   4330  O O    . LEU A 1 283 ? 24.042  -21.371 88.756  1.00 69.22  ?  292 LEU A O    1 
ATOM   4331  C CB   . LEU A 1 283 ? 21.843  -22.817 90.446  1.00 65.40  ?  292 LEU A CB   1 
ATOM   4332  C CG   . LEU A 1 283 ? 21.699  -24.007 91.403  1.00 89.28  ?  292 LEU A CG   1 
ATOM   4333  C CD1  . LEU A 1 283 ? 20.394  -24.667 91.259  1.00 108.33 ?  292 LEU A CD1  1 
ATOM   4334  C CD2  . LEU A 1 283 ? 22.817  -24.992 91.181  1.00 89.30  ?  292 LEU A CD2  1 
ATOM   4335  H H    . LEU A 1 283 ? 21.837  -21.175 92.269  1.00 82.40  ?  292 LEU A H    1 
ATOM   4336  H HA   . LEU A 1 283 ? 23.775  -22.430 90.992  1.00 76.28  ?  292 LEU A HA   1 
ATOM   4337  H HB2  . LEU A 1 283 ? 21.012  -22.317 90.463  1.00 78.48  ?  292 LEU A HB2  1 
ATOM   4338  H HB3  . LEU A 1 283 ? 22.002  -23.166 89.555  1.00 78.48  ?  292 LEU A HB3  1 
ATOM   4339  H HG   . LEU A 1 283 ? 21.768  -23.683 92.314  1.00 107.13 ?  292 LEU A HG   1 
ATOM   4340  H HD11 . LEU A 1 283 ? 20.347  -25.411 91.881  1.00 130.00 ?  292 LEU A HD11 1 
ATOM   4341  H HD12 . LEU A 1 283 ? 19.693  -24.026 91.456  1.00 130.00 ?  292 LEU A HD12 1 
ATOM   4342  H HD13 . LEU A 1 283 ? 20.302  -24.990 90.349  1.00 130.00 ?  292 LEU A HD13 1 
ATOM   4343  H HD21 . LEU A 1 283 ? 22.708  -25.736 91.795  1.00 107.16 ?  292 LEU A HD21 1 
ATOM   4344  H HD22 . LEU A 1 283 ? 22.780  -25.310 90.265  1.00 107.16 ?  292 LEU A HD22 1 
ATOM   4345  H HD23 . LEU A 1 283 ? 23.664  -24.550 91.344  1.00 107.16 ?  292 LEU A HD23 1 
ATOM   4346  N N    . GLN A 1 284 ? 22.613  -19.840 89.568  1.00 85.28  ?  293 GLN A N    1 
ATOM   4347  C CA   . GLN A 1 284 ? 22.910  -18.929 88.481  1.00 78.52  ?  293 GLN A CA   1 
ATOM   4348  C C    . GLN A 1 284 ? 24.297  -18.345 88.681  1.00 129.74 ?  293 GLN A C    1 
ATOM   4349  O O    . GLN A 1 284 ? 25.088  -18.222 87.735  1.00 47.82  ?  293 GLN A O    1 
ATOM   4350  C CB   . GLN A 1 284 ? 21.858  -17.829 88.423  1.00 92.84  ?  293 GLN A CB   1 
ATOM   4351  C CG   . GLN A 1 284 ? 21.928  -16.913 87.193  1.00 114.03 ?  293 GLN A CG   1 
ATOM   4352  C CD   . GLN A 1 284 ? 21.597  -17.643 85.886  1.00 118.06 ?  293 GLN A CD   1 
ATOM   4353  O OE1  . GLN A 1 284 ? 20.519  -18.245 85.748  1.00 148.77 ?  293 GLN A OE1  1 
ATOM   4354  N NE2  . GLN A 1 284 ? 22.499  -17.540 84.900  1.00 77.45  ?  293 GLN A NE2  1 
ATOM   4355  H H    . GLN A 1 284 ? 22.003  -19.576 90.115  1.00 102.34 ?  293 GLN A H    1 
ATOM   4356  H HA   . GLN A 1 284 ? 22.897  -19.412 87.640  1.00 94.23  ?  293 GLN A HA   1 
ATOM   4357  H HB2  . GLN A 1 284 ? 20.981  -18.243 88.428  1.00 111.41 ?  293 GLN A HB2  1 
ATOM   4358  H HB3  . GLN A 1 284 ? 21.956  -17.269 89.208  1.00 111.41 ?  293 GLN A HB3  1 
ATOM   4359  H HG2  . GLN A 1 284 ? 21.291  -16.190 87.302  1.00 136.84 ?  293 GLN A HG2  1 
ATOM   4360  H HG3  . GLN A 1 284 ? 22.826  -16.555 87.117  1.00 136.84 ?  293 GLN A HG3  1 
ATOM   4361  H HE21 . GLN A 1 284 ? 23.218  -17.083 85.020  1.00 92.94  ?  293 GLN A HE21 1 
ATOM   4362  H HE22 . GLN A 1 284 ? 22.360  -17.931 84.147  1.00 92.94  ?  293 GLN A HE22 1 
ATOM   4363  N N    . ASP A 1 285 ? 24.628  -18.011 89.923  1.00 68.55  ?  294 ASP A N    1 
ATOM   4364  C CA   . ASP A 1 285 ? 25.921  -17.410 90.160  1.00 72.04  ?  294 ASP A CA   1 
ATOM   4365  C C    . ASP A 1 285 ? 27.028  -18.403 89.814  1.00 67.97  ?  294 ASP A C    1 
ATOM   4366  O O    . ASP A 1 285 ? 27.920  -18.092 89.020  1.00 85.25  ?  294 ASP A O    1 
ATOM   4367  C CB   . ASP A 1 285 ? 26.002  -16.913 91.617  1.00 62.84  ?  294 ASP A CB   1 
ATOM   4368  C CG   . ASP A 1 285 ? 25.031  -15.795 91.910  1.00 79.63  ?  294 ASP A CG   1 
ATOM   4369  O OD1  . ASP A 1 285 ? 24.506  -15.204 90.930  1.00 90.76  ?  294 ASP A OD1  1 
ATOM   4370  O OD2  . ASP A 1 285 ? 24.793  -15.492 93.095  1.00 172.74 -1 294 ASP A OD2  1 
ATOM   4371  H H    . ASP A 1 285 ? 24.138  -18.120 90.621  1.00 82.26  ?  294 ASP A H    1 
ATOM   4372  H HA   . ASP A 1 285 ? 26.020  -16.641 89.579  1.00 86.45  ?  294 ASP A HA   1 
ATOM   4373  H HB2  . ASP A 1 285 ? 25.800  -17.651 92.214  1.00 75.41  ?  294 ASP A HB2  1 
ATOM   4374  H HB3  . ASP A 1 285 ? 26.899  -16.585 91.788  1.00 75.41  ?  294 ASP A HB3  1 
ATOM   4375  N N    . MET A 1 286 ? 26.900  -19.647 90.243  1.00 76.91  ?  295 MET A N    1 
ATOM   4376  C CA   . MET A 1 286 ? 28.003  -20.553 89.961  1.00 83.12  ?  295 MET A CA   1 
ATOM   4377  C C    . MET A 1 286 ? 28.171  -20.826 88.469  1.00 45.97  ?  295 MET A C    1 
ATOM   4378  O O    . MET A 1 286 ? 29.211  -21.363 88.068  1.00 45.59  ?  295 MET A O    1 
ATOM   4379  C CB   . MET A 1 286 ? 27.807  -21.886 90.656  1.00 44.41  ?  295 MET A CB   1 
ATOM   4380  C CG   . MET A 1 286 ? 27.913  -21.876 92.172  1.00 73.28  ?  295 MET A CG   1 
ATOM   4381  S SD   . MET A 1 286 ? 29.483  -21.255 92.737  1.00 80.71  ?  295 MET A SD   1 
ATOM   4382  C CE   . MET A 1 286 ? 29.105  -19.533 93.074  1.00 114.65 ?  295 MET A CE   1 
ATOM   4383  H H    . MET A 1 286 ? 26.232  -19.978 90.671  1.00 92.30  ?  295 MET A H    1 
ATOM   4384  H HA   . MET A 1 286 ? 28.823  -20.160 90.300  1.00 99.74  ?  295 MET A HA   1 
ATOM   4385  H HB2  . MET A 1 286 ? 26.925  -22.220 90.431  1.00 53.29  ?  295 MET A HB2  1 
ATOM   4386  H HB3  . MET A 1 286 ? 28.478  -22.504 90.325  1.00 53.29  ?  295 MET A HB3  1 
ATOM   4387  H HG2  . MET A 1 286 ? 27.215  -21.308 92.534  1.00 87.94  ?  295 MET A HG2  1 
ATOM   4388  H HG3  . MET A 1 286 ? 27.810  -22.782 92.503  1.00 87.94  ?  295 MET A HG3  1 
ATOM   4389  H HE1  . MET A 1 286 ? 29.906  -19.091 93.395  1.00 137.58 ?  295 MET A HE1  1 
ATOM   4390  H HE2  . MET A 1 286 ? 28.798  -19.112 92.256  1.00 137.58 ?  295 MET A HE2  1 
ATOM   4391  H HE3  . MET A 1 286 ? 28.410  -19.490 93.750  1.00 137.58 ?  295 MET A HE3  1 
ATOM   4392  N N    . ARG A 1 287 ? 27.232  -20.463 87.619  1.00 51.73  ?  296 ARG A N    1 
ATOM   4393  C CA   . ARG A 1 287 ? 27.521  -20.632 86.206  1.00 46.95  ?  296 ARG A CA   1 
ATOM   4394  C C    . ARG A 1 287 ? 28.722  -19.784 85.818  1.00 82.51  ?  296 ARG A C    1 
ATOM   4395  O O    . ARG A 1 287 ? 29.459  -20.138 84.896  1.00 66.75  ?  296 ARG A O    1 
ATOM   4396  C CB   . ARG A 1 287 ? 26.271  -20.237 85.325  1.00 48.18  ?  296 ARG A CB   1 
ATOM   4397  C CG   . ARG A 1 287 ? 25.065  -21.109 85.463  1.00 54.18  ?  296 ARG A CG   1 
ATOM   4398  C CD   . ARG A 1 287 ? 24.187  -21.059 84.207  1.00 65.10  ?  296 ARG A CD   1 
ATOM   4399  N NE   . ARG A 1 287 ? 22.970  -21.792 84.516  1.00 71.77  ?  296 ARG A NE   1 
ATOM   4400  C CZ   . ARG A 1 287 ? 21.844  -21.692 83.848  1.00 73.83  ?  296 ARG A CZ   1 
ATOM   4401  N NH1  . ARG A 1 287 ? 21.755  -20.879 82.809  1.00 86.47  1  296 ARG A NH1  1 
ATOM   4402  N NH2  . ARG A 1 287 ? 20.788  -22.354 84.290  1.00 86.66  1  296 ARG A NH2  1 
ATOM   4403  H H    . ARG A 1 287 ? 26.461  -20.135 87.815  1.00 62.08  ?  296 ARG A H    1 
ATOM   4404  H HA   . ARG A 1 287 ? 27.735  -21.562 86.032  1.00 56.33  ?  296 ARG A HA   1 
ATOM   4405  H HB2  . ARG A 1 287 ? 26.003  -19.335 85.564  1.00 57.82  ?  296 ARG A HB2  1 
ATOM   4406  H HB3  . ARG A 1 287 ? 26.537  -20.257 84.393  1.00 57.82  ?  296 ARG A HB3  1 
ATOM   4407  H HG2  . ARG A 1 287 ? 25.348  -22.026 85.599  1.00 65.01  ?  296 ARG A HG2  1 
ATOM   4408  H HG3  . ARG A 1 287 ? 24.535  -20.805 86.216  1.00 65.01  ?  296 ARG A HG3  1 
ATOM   4409  H HD2  . ARG A 1 287 ? 23.960  -20.141 83.994  1.00 78.12  ?  296 ARG A HD2  1 
ATOM   4410  H HD3  . ARG A 1 287 ? 24.639  -21.490 83.465  1.00 78.12  ?  296 ARG A HD3  1 
ATOM   4411  H HE   . ARG A 1 287 ? 22.990  -22.331 85.186  1.00 86.13  ?  296 ARG A HE   1 
ATOM   4412  H HH11 . ARG A 1 287 ? 22.445  -20.433 82.553  1.00 103.77 ?  296 ARG A HH11 1 
ATOM   4413  H HH12 . ARG A 1 287 ? 21.016  -20.815 82.375  1.00 103.77 ?  296 ARG A HH12 1 
ATOM   4414  H HH21 . ARG A 1 287 ? 20.864  -22.881 84.965  1.00 103.99 ?  296 ARG A HH21 1 
ATOM   4415  H HH22 . ARG A 1 287 ? 20.046  -22.317 83.856  1.00 103.99 ?  296 ARG A HH22 1 
ATOM   4416  N N    . ARG A 1 288 ? 28.932  -18.653 86.502  1.00 70.40  ?  297 ARG A N    1 
ATOM   4417  C CA   . ARG A 1 288 ? 30.033  -17.755 86.125  1.00 77.95  ?  297 ARG A CA   1 
ATOM   4418  C C    . ARG A 1 288 ? 31.378  -18.322 86.515  1.00 115.60 ?  297 ARG A C    1 
ATOM   4419  O O    . ARG A 1 288 ? 32.410  -17.831 86.047  1.00 139.81 ?  297 ARG A O    1 
ATOM   4420  C CB   . ARG A 1 288 ? 29.859  -16.374 86.755  1.00 95.79  ?  297 ARG A CB   1 
ATOM   4421  C CG   . ARG A 1 288 ? 29.903  -15.254 85.725  1.00 111.04 ?  297 ARG A CG   1 
ATOM   4422  C CD   . ARG A 1 288 ? 28.514  -14.766 85.294  1.00 115.66 ?  297 ARG A CD   1 
ATOM   4423  N NE   . ARG A 1 288 ? 28.246  -14.776 83.844  1.00 117.65 ?  297 ARG A NE   1 
ATOM   4424  C CZ   . ARG A 1 288 ? 29.047  -14.257 82.902  1.00 126.10 ?  297 ARG A CZ   1 
ATOM   4425  N NH1  . ARG A 1 288 ? 30.216  -13.717 83.214  1.00 165.65 1  297 ARG A NH1  1 
ATOM   4426  N NH2  . ARG A 1 288 ? 28.695  -14.277 81.621  1.00 76.26  1  297 ARG A NH2  1 
ATOM   4427  H H    . ARG A 1 288 ? 28.464  -18.386 87.172  1.00 84.48  ?  297 ARG A H    1 
ATOM   4428  H HA   . ARG A 1 288 ? 30.028  -17.643 85.162  1.00 93.54  ?  297 ARG A HA   1 
ATOM   4429  H HB2  . ARG A 1 288 ? 28.999  -16.337 87.204  1.00 114.95 ?  297 ARG A HB2  1 
ATOM   4430  H HB3  . ARG A 1 288 ? 30.574  -16.224 87.393  1.00 114.95 ?  297 ARG A HB3  1 
ATOM   4431  H HG2  . ARG A 1 288 ? 30.379  -14.498 86.104  1.00 133.25 ?  297 ARG A HG2  1 
ATOM   4432  H HG3  . ARG A 1 288 ? 30.365  -15.573 84.934  1.00 133.25 ?  297 ARG A HG3  1 
ATOM   4433  H HD2  . ARG A 1 288 ? 27.848  -15.332 85.715  1.00 138.80 ?  297 ARG A HD2  1 
ATOM   4434  H HD3  . ARG A 1 288 ? 28.402  -13.853 85.602  1.00 138.80 ?  297 ARG A HD3  1 
ATOM   4435  H HE   . ARG A 1 288 ? 27.515  -15.145 83.581  1.00 141.18 ?  297 ARG A HE   1 
ATOM   4436  H HH11 . ARG A 1 288 ? 30.466  -13.679 84.036  1.00 198.78 ?  297 ARG A HH11 1 
ATOM   4437  H HH12 . ARG A 1 288 ? 30.720  -13.396 82.596  1.00 198.78 ?  297 ARG A HH12 1 
ATOM   4438  H HH21 . ARG A 1 288 ? 27.948  -14.632 81.387  1.00 91.51  ?  297 ARG A HH21 1 
ATOM   4439  H HH22 . ARG A 1 288 ? 29.227  -13.961 81.024  1.00 91.51  ?  297 ARG A HH22 1 
ATOM   4440  N N    . TYR A 1 289 ? 31.359  -19.377 87.317  1.00 70.72  ?  298 TYR A N    1 
ATOM   4441  C CA   . TYR A 1 289 ? 32.522  -20.100 87.778  1.00 71.27  ?  298 TYR A CA   1 
ATOM   4442  C C    . TYR A 1 289 ? 32.788  -21.320 86.941  1.00 83.56  ?  298 TYR A C    1 
ATOM   4443  O O    . TYR A 1 289 ? 33.513  -22.193 87.394  1.00 45.28  ?  298 TYR A O    1 
ATOM   4444  C CB   . TYR A 1 289 ? 32.336  -20.550 89.216  1.00 45.99  ?  298 TYR A CB   1 
ATOM   4445  C CG   . TYR A 1 289 ? 32.438  -19.477 90.301  1.00 65.76  ?  298 TYR A CG   1 
ATOM   4446  C CD1  . TYR A 1 289 ? 31.580  -18.389 90.315  1.00 62.49  ?  298 TYR A CD1  1 
ATOM   4447  C CD2  . TYR A 1 289 ? 33.285  -19.649 91.393  1.00 72.98  ?  298 TYR A CD2  1 
ATOM   4448  C CE1  . TYR A 1 289 ? 31.621  -17.479 91.319  1.00 80.00  ?  298 TYR A CE1  1 
ATOM   4449  C CE2  . TYR A 1 289 ? 33.318  -18.738 92.394  1.00 79.73  ?  298 TYR A CE2  1 
ATOM   4450  C CZ   . TYR A 1 289 ? 32.489  -17.657 92.365  1.00 58.56  ?  298 TYR A CZ   1 
ATOM   4451  O OH   . TYR A 1 289 ? 32.538  -16.739 93.388  1.00 62.17  ?  298 TYR A OH   1 
ATOM   4452  H H    . TYR A 1 289 ? 30.628  -19.709 87.624  1.00 84.87  ?  298 TYR A H    1 
ATOM   4453  H HA   . TYR A 1 289 ? 33.300  -19.522 87.735  1.00 85.52  ?  298 TYR A HA   1 
ATOM   4454  H HB2  . TYR A 1 289 ? 31.457  -20.952 89.294  1.00 55.19  ?  298 TYR A HB2  1 
ATOM   4455  H HB3  . TYR A 1 289 ? 33.011  -21.219 89.412  1.00 55.19  ?  298 TYR A HB3  1 
ATOM   4456  H HD1  . TYR A 1 289 ? 30.985  -18.266 89.611  1.00 74.99  ?  298 TYR A HD1  1 
ATOM   4457  H HD2  . TYR A 1 289 ? 33.850  -20.387 91.424  1.00 87.57  ?  298 TYR A HD2  1 
ATOM   4458  H HE1  . TYR A 1 289 ? 31.057  -16.740 91.301  1.00 96.00  ?  298 TYR A HE1  1 
ATOM   4459  H HE2  . TYR A 1 289 ? 33.908  -18.851 93.104  1.00 95.68  ?  298 TYR A HE2  1 
ATOM   4460  H HH   . TYR A 1 289 ? 31.986  -16.122 93.247  1.00 74.60  ?  298 TYR A HH   1 
ATOM   4461  N N    . MET A 1 290 ? 32.115  -21.477 85.848  1.00 76.17  ?  299 MET A N    1 
ATOM   4462  C CA   . MET A 1 290 ? 32.401  -22.546 84.914  1.00 73.99  ?  299 MET A CA   1 
ATOM   4463  C C    . MET A 1 290 ? 33.188  -22.035 83.733  1.00 92.84  ?  299 MET A C    1 
ATOM   4464  O O    . MET A 1 290 ? 33.117  -20.849 83.377  1.00 115.89 ?  299 MET A O    1 
ATOM   4465  C CB   . MET A 1 290 ? 31.117  -23.157 84.395  1.00 65.06  ?  299 MET A CB   1 
ATOM   4466  C CG   . MET A 1 290 ? 30.294  -23.878 85.432  1.00 78.20  ?  299 MET A CG   1 
ATOM   4467  S SD   . MET A 1 290 ? 28.728  -24.329 84.659  1.00 65.28  ?  299 MET A SD   1 
ATOM   4468  C CE   . MET A 1 290 ? 27.865  -24.888 86.202  1.00 60.10  ?  299 MET A CE   1 
ATOM   4469  H H    . MET A 1 290 ? 31.465  -20.969 85.605  1.00 91.40  ?  299 MET A H    1 
ATOM   4470  H HA   . MET A 1 290 ? 32.909  -23.239 85.364  1.00 88.79  ?  299 MET A HA   1 
ATOM   4471  H HB2  . MET A 1 290 ? 30.566  -22.450 84.024  1.00 78.07  ?  299 MET A HB2  1 
ATOM   4472  H HB3  . MET A 1 290 ? 31.338  -23.797 83.700  1.00 78.07  ?  299 MET A HB3  1 
ATOM   4473  H HG2  . MET A 1 290 ? 30.751  -24.685 85.717  1.00 93.84  ?  299 MET A HG2  1 
ATOM   4474  H HG3  . MET A 1 290 ? 30.119  -23.292 86.184  1.00 93.84  ?  299 MET A HG3  1 
ATOM   4475  H HE1  . MET A 1 290 ? 26.968  -25.180 85.974  1.00 72.12  ?  299 MET A HE1  1 
ATOM   4476  H HE2  . MET A 1 290 ? 28.363  -25.623 86.593  1.00 72.12  ?  299 MET A HE2  1 
ATOM   4477  H HE3  . MET A 1 290 ? 27.823  -24.146 86.826  1.00 72.12  ?  299 MET A HE3  1 
ATOM   4478  N N    . PRO A 1 291 ? 33.867  -22.933 83.031  1.00 72.10  ?  300 PRO A N    1 
ATOM   4479  C CA   . PRO A 1 291 ? 34.542  -22.534 81.814  1.00 67.74  ?  300 PRO A CA   1 
ATOM   4480  C C    . PRO A 1 291 ? 33.594  -21.752 80.936  1.00 65.25  ?  300 PRO A C    1 
ATOM   4481  O O    . PRO A 1 291 ? 32.397  -22.061 80.855  1.00 69.42  ?  300 PRO A O    1 
ATOM   4482  C CB   . PRO A 1 291 ? 34.941  -23.870 81.159  1.00 91.05  ?  300 PRO A CB   1 
ATOM   4483  C CG   . PRO A 1 291 ? 35.005  -24.822 82.250  1.00 46.95  ?  300 PRO A CG   1 
ATOM   4484  C CD   . PRO A 1 291 ? 34.028  -24.383 83.303  1.00 65.92  ?  300 PRO A CD   1 
ATOM   4485  H HA   . PRO A 1 291 ? 35.333  -22.007 82.009  1.00 81.28  ?  300 PRO A HA   1 
ATOM   4486  H HB2  . PRO A 1 291 ? 34.265  -24.132 80.514  1.00 109.25 ?  300 PRO A HB2  1 
ATOM   4487  H HB3  . PRO A 1 291 ? 35.807  -23.779 80.732  1.00 109.25 ?  300 PRO A HB3  1 
ATOM   4488  H HG2  . PRO A 1 291 ? 34.767  -25.702 81.919  1.00 56.34  ?  300 PRO A HG2  1 
ATOM   4489  H HG3  . PRO A 1 291 ? 35.905  -24.832 82.611  1.00 56.34  ?  300 PRO A HG3  1 
ATOM   4490  H HD2  . PRO A 1 291 ? 33.182  -24.844 83.193  1.00 79.11  ?  300 PRO A HD2  1 
ATOM   4491  H HD3  . PRO A 1 291 ? 34.399  -24.523 84.188  1.00 79.11  ?  300 PRO A HD3  1 
ATOM   4492  N N    . PRO A 1 292 ? 34.093  -20.769 80.223  1.00 76.86  ?  301 PRO A N    1 
ATOM   4493  C CA   . PRO A 1 292 ? 33.178  -19.994 79.401  1.00 83.94  ?  301 PRO A CA   1 
ATOM   4494  C C    . PRO A 1 292 ? 32.382  -20.885 78.461  1.00 52.55  ?  301 PRO A C    1 
ATOM   4495  O O    . PRO A 1 292 ? 31.163  -20.887 78.552  1.00 77.80  ?  301 PRO A O    1 
ATOM   4496  C CB   . PRO A 1 292 ? 34.122  -19.044 78.674  1.00 70.23  ?  301 PRO A CB   1 
ATOM   4497  C CG   . PRO A 1 292 ? 35.399  -19.771 78.630  1.00 71.47  ?  301 PRO A CG   1 
ATOM   4498  C CD   . PRO A 1 292 ? 35.481  -20.616 79.799  1.00 61.78  ?  301 PRO A CD   1 
ATOM   4499  H HA   . PRO A 1 292 ? 32.569  -19.483 79.958  1.00 100.73 ?  301 PRO A HA   1 
ATOM   4500  H HB2  . PRO A 1 292 ? 33.791  -18.872 77.778  1.00 84.28  ?  301 PRO A HB2  1 
ATOM   4501  H HB3  . PRO A 1 292 ? 34.211  -18.219 79.176  1.00 84.28  ?  301 PRO A HB3  1 
ATOM   4502  H HG2  . PRO A 1 292 ? 35.429  -20.312 77.825  1.00 85.76  ?  301 PRO A HG2  1 
ATOM   4503  H HG3  . PRO A 1 292 ? 36.128  -19.132 78.629  1.00 85.76  ?  301 PRO A HG3  1 
ATOM   4504  H HD2  . PRO A 1 292 ? 35.858  -21.479 79.565  1.00 74.14  ?  301 PRO A HD2  1 
ATOM   4505  H HD3  . PRO A 1 292 ? 35.999  -20.180 80.494  1.00 74.14  ?  301 PRO A HD3  1 
ATOM   4506  N N    . ALA A 1 293 ? 33.040  -21.773 77.705  1.00 60.89  ?  302 ALA A N    1 
ATOM   4507  C CA   . ALA A 1 293 ? 32.323  -22.664 76.782  1.00 70.24  ?  302 ALA A CA   1 
ATOM   4508  C C    . ALA A 1 293 ? 31.258  -23.467 77.504  1.00 73.04  ?  302 ALA A C    1 
ATOM   4509  O O    . ALA A 1 293 ? 30.176  -23.723 76.944  1.00 68.08  ?  302 ALA A O    1 
ATOM   4510  C CB   . ALA A 1 293 ? 33.242  -23.663 76.084  1.00 74.44  ?  302 ALA A CB   1 
ATOM   4511  H H    . ALA A 1 293 ? 33.894  -21.879 77.708  1.00 73.07  ?  302 ALA A H    1 
ATOM   4512  H HA   . ALA A 1 293 ? 31.887  -22.129 76.100  1.00 84.29  ?  302 ALA A HA   1 
ATOM   4513  H HB1  . ALA A 1 293 ? 32.711  -24.219 75.492  1.00 89.33  ?  302 ALA A HB1  1 
ATOM   4514  H HB2  . ALA A 1 293 ? 33.907  -23.176 75.573  1.00 89.33  ?  302 ALA A HB2  1 
ATOM   4515  H HB3  . ALA A 1 293 ? 33.676  -24.213 76.754  1.00 89.33  ?  302 ALA A HB3  1 
ATOM   4516  N N    . HIS A 1 294 ? 31.504  -23.851 78.752  1.00 67.05  ?  303 HIS A N    1 
ATOM   4517  C CA   . HIS A 1 294 ? 30.471  -24.676 79.360  1.00 59.64  ?  303 HIS A CA   1 
ATOM   4518  C C    . HIS A 1 294 ? 29.327  -23.825 79.853  1.00 62.97  ?  303 HIS A C    1 
ATOM   4519  O O    . HIS A 1 294 ? 28.196  -24.291 79.853  1.00 64.81  ?  303 HIS A O    1 
ATOM   4520  C CB   . HIS A 1 294 ? 31.069  -25.531 80.470  1.00 61.89  ?  303 HIS A CB   1 
ATOM   4521  C CG   . HIS A 1 294 ? 32.063  -26.528 79.940  1.00 72.65  ?  303 HIS A CG   1 
ATOM   4522  N ND1  . HIS A 1 294 ? 32.825  -27.352 80.748  1.00 53.15  ?  303 HIS A ND1  1 
ATOM   4523  C CD2  . HIS A 1 294 ? 32.443  -26.795 78.657  1.00 60.66  ?  303 HIS A CD2  1 
ATOM   4524  C CE1  . HIS A 1 294 ? 33.599  -28.103 79.979  1.00 51.84  ?  303 HIS A CE1  1 
ATOM   4525  N NE2  . HIS A 1 294 ? 33.402  -27.769 78.715  1.00 49.06  ?  303 HIS A NE2  1 
ATOM   4526  H H    . HIS A 1 294 ? 32.195  -23.669 79.231  1.00 80.46  ?  303 HIS A H    1 
ATOM   4527  H HA   . HIS A 1 294 ? 30.118  -25.277 78.685  1.00 71.56  ?  303 HIS A HA   1 
ATOM   4528  H HB2  . HIS A 1 294 ? 31.527  -24.955 81.103  1.00 74.27  ?  303 HIS A HB2  1 
ATOM   4529  H HB3  . HIS A 1 294 ? 30.358  -26.019 80.914  1.00 74.27  ?  303 HIS A HB3  1 
ATOM   4530  H HD2  . HIS A 1 294 ? 32.113  -26.390 77.888  1.00 72.79  ?  303 HIS A HD2  1 
ATOM   4531  H HE1  . HIS A 1 294 ? 34.206  -28.740 80.281  1.00 62.21  ?  303 HIS A HE1  1 
ATOM   4532  H HE2  . HIS A 1 294 ? 33.795  -28.124 78.037  1.00 58.88  ?  303 HIS A HE2  1 
ATOM   4533  N N    . ARG A 1 295 ? 29.590  -22.564 80.248  1.00 57.81  ?  304 ARG A N    1 
ATOM   4534  C CA   . ARG A 1 295 ? 28.493  -21.701 80.638  1.00 56.92  ?  304 ARG A CA   1 
ATOM   4535  C C    . ARG A 1 295 ? 27.644  -21.382 79.411  1.00 54.31  ?  304 ARG A C    1 
ATOM   4536  O O    . ARG A 1 295 ? 26.411  -21.377 79.481  1.00 87.92  ?  304 ARG A O    1 
ATOM   4537  C CB   . ARG A 1 295 ? 29.067  -20.470 81.366  1.00 79.17  ?  304 ARG A CB   1 
ATOM   4538  C CG   . ARG A 1 295 ? 28.965  -19.085 80.637  1.00 87.01  ?  304 ARG A CG   1 
ATOM   4539  C CD   . ARG A 1 295 ? 29.508  -17.953 81.494  1.00 78.63  ?  304 ARG A CD   1 
ATOM   4540  H H    . ARG A 1 295 ? 30.372  -22.207 80.293  1.00 69.38  ?  304 ARG A H    1 
ATOM   4541  H HA   . ARG A 1 295 ? 27.931  -22.179 81.268  1.00 68.31  ?  304 ARG A HA   1 
ATOM   4542  H HB2  . ARG A 1 295 ? 28.604  -20.380 82.213  1.00 95.00  ?  304 ARG A HB2  1 
ATOM   4543  H HB3  . ARG A 1 295 ? 30.008  -20.633 81.534  1.00 95.00  ?  304 ARG A HB3  1 
ATOM   4544  H HG2  . ARG A 1 295 ? 29.480  -19.118 79.816  1.00 104.41 ?  304 ARG A HG2  1 
ATOM   4545  H HG3  . ARG A 1 295 ? 28.034  -18.896 80.440  1.00 104.41 ?  304 ARG A HG3  1 
ATOM   4546  H HD2  . ARG A 1 295 ? 29.725  -17.200 80.922  1.00 94.36  ?  304 ARG A HD2  1 
ATOM   4547  H HD3  . ARG A 1 295 ? 28.834  -17.694 82.141  1.00 94.36  ?  304 ARG A HD3  1 
ATOM   4548  N N    . ASN A 1 296 ? 28.285  -21.340 78.253  1.00 49.22  ?  305 ASN A N    1 
ATOM   4549  C CA   . ASN A 1 296 ? 27.624  -21.014 77.005  1.00 62.92  ?  305 ASN A CA   1 
ATOM   4550  C C    . ASN A 1 296 ? 26.719  -22.129 76.579  1.00 72.23  ?  305 ASN A C    1 
ATOM   4551  O O    . ASN A 1 296 ? 25.729  -21.898 75.870  1.00 82.13  ?  305 ASN A O    1 
ATOM   4552  C CB   . ASN A 1 296 ? 28.645  -20.796 75.875  1.00 86.68  ?  305 ASN A CB   1 
ATOM   4553  C CG   . ASN A 1 296 ? 29.545  -19.592 76.076  1.00 102.75 ?  305 ASN A CG   1 
ATOM   4554  O OD1  . ASN A 1 296 ? 30.685  -19.606 75.638  1.00 132.67 ?  305 ASN A OD1  1 
ATOM   4555  N ND2  . ASN A 1 296 ? 29.039  -18.551 76.722  1.00 192.93 ?  305 ASN A ND2  1 
ATOM   4556  H H    . ASN A 1 296 ? 29.126  -21.502 78.165  1.00 59.06  ?  305 ASN A H    1 
ATOM   4557  H HA   . ASN A 1 296 ? 27.098  -20.206 77.113  1.00 75.51  ?  305 ASN A HA   1 
ATOM   4558  H HB2  . ASN A 1 296 ? 29.212  -21.581 75.812  1.00 104.01 ?  305 ASN A HB2  1 
ATOM   4559  H HB3  . ASN A 1 296 ? 28.165  -20.671 75.042  1.00 104.01 ?  305 ASN A HB3  1 
ATOM   4560  H HD21 . ASN A 1 296 ? 29.521  -17.851 76.854  1.00 231.52 ?  305 ASN A HD21 1 
ATOM   4561  H HD22 . ASN A 1 296 ? 28.229  -18.576 77.010  1.00 231.52 ?  305 ASN A HD22 1 
ATOM   4562  N N    . PHE A 1 297 ? 27.109  -23.352 76.905  1.00 68.66  ?  306 PHE A N    1 
ATOM   4563  C CA   . PHE A 1 297 ? 26.310  -24.494 76.515  1.00 68.99  ?  306 PHE A CA   1 
ATOM   4564  C C    . PHE A 1 297 ? 25.000  -24.507 77.286  1.00 74.53  ?  306 PHE A C    1 
ATOM   4565  O O    . PHE A 1 297 ? 23.915  -24.563 76.676  1.00 88.26  ?  306 PHE A O    1 
ATOM   4566  C CB   . PHE A 1 297 ? 27.135  -25.760 76.694  1.00 55.89  ?  306 PHE A CB   1 
ATOM   4567  C CG   . PHE A 1 297 ? 26.422  -26.954 76.323  1.00 53.08  ?  306 PHE A CG   1 
ATOM   4568  C CD1  . PHE A 1 297 ? 26.122  -27.196 74.987  1.00 76.74  ?  306 PHE A CD1  1 
ATOM   4569  C CD2  . PHE A 1 297 ? 26.020  -27.834 77.288  1.00 45.12  ?  306 PHE A CD2  1 
ATOM   4570  C CE1  . PHE A 1 297 ? 25.380  -28.337 74.602  1.00 53.71  ?  306 PHE A CE1  1 
ATOM   4571  C CE2  . PHE A 1 297 ? 25.276  -28.965 76.921  1.00 59.48  ?  306 PHE A CE2  1 
ATOM   4572  C CZ   . PHE A 1 297 ? 24.972  -29.211 75.562  1.00 55.12  ?  306 PHE A CZ   1 
ATOM   4573  H H    . PHE A 1 297 ? 27.822  -23.543 77.346  1.00 82.39  ?  306 PHE A H    1 
ATOM   4574  H HA   . PHE A 1 297 ? 26.095  -24.415 75.572  1.00 82.78  ?  306 PHE A HA   1 
ATOM   4575  H HB2  . PHE A 1 297 ? 27.928  -25.700 76.139  1.00 67.06  ?  306 PHE A HB2  1 
ATOM   4576  H HB3  . PHE A 1 297 ? 27.390  -25.841 77.627  1.00 67.06  ?  306 PHE A HB3  1 
ATOM   4577  H HD1  . PHE A 1 297 ? 26.392  -26.587 74.339  1.00 92.09  ?  306 PHE A HD1  1 
ATOM   4578  H HD2  . PHE A 1 297 ? 26.207  -27.666 78.183  1.00 54.14  ?  306 PHE A HD2  1 
ATOM   4579  H HE1  . PHE A 1 297 ? 25.185  -28.494 73.707  1.00 64.46  ?  306 PHE A HE1  1 
ATOM   4580  H HE2  . PHE A 1 297 ? 25.004  -29.570 77.573  1.00 71.37  ?  306 PHE A HE2  1 
ATOM   4581  H HZ   . PHE A 1 297 ? 24.497  -29.975 75.324  1.00 66.15  ?  306 PHE A HZ   1 
ATOM   4582  N N    . LEU A 1 298 ? 25.069  -24.334 78.617  1.00 52.74  ?  307 LEU A N    1 
ATOM   4583  C CA   . LEU A 1 298 ? 23.844  -24.238 79.402  1.00 67.06  ?  307 LEU A CA   1 
ATOM   4584  C C    . LEU A 1 298 ? 22.953  -23.103 78.912  1.00 83.73  ?  307 LEU A C    1 
ATOM   4585  O O    . LEU A 1 298 ? 21.737  -23.268 78.763  1.00 78.84  ?  307 LEU A O    1 
ATOM   4586  C CB   . LEU A 1 298 ? 24.157  -24.020 80.873  1.00 58.36  ?  307 LEU A CB   1 
ATOM   4587  C CG   . LEU A 1 298 ? 24.785  -25.208 81.592  1.00 62.94  ?  307 LEU A CG   1 
ATOM   4588  C CD1  . LEU A 1 298 ? 25.041  -24.895 83.065  1.00 60.72  ?  307 LEU A CD1  1 
ATOM   4589  C CD2  . LEU A 1 298 ? 23.890  -26.368 81.522  1.00 81.26  ?  307 LEU A CD2  1 
ATOM   4590  H H    . LEU A 1 298 ? 25.796  -24.271 79.071  1.00 63.29  ?  307 LEU A H    1 
ATOM   4591  H HA   . LEU A 1 298 ? 23.348  -25.067 79.319  1.00 80.48  ?  307 LEU A HA   1 
ATOM   4592  H HB2  . LEU A 1 298 ? 24.774  -23.275 80.949  1.00 70.03  ?  307 LEU A HB2  1 
ATOM   4593  H HB3  . LEU A 1 298 ? 23.331  -23.805 81.334  1.00 70.03  ?  307 LEU A HB3  1 
ATOM   4594  H HG   . LEU A 1 298 ? 25.628  -25.438 81.171  1.00 75.53  ?  307 LEU A HG   1 
ATOM   4595  H HD11 . LEU A 1 298 ? 25.440  -25.672 83.487  1.00 72.86  ?  307 LEU A HD11 1 
ATOM   4596  H HD12 . LEU A 1 298 ? 25.645  -24.138 83.126  1.00 72.86  ?  307 LEU A HD12 1 
ATOM   4597  H HD13 . LEU A 1 298 ? 24.197  -24.682 83.493  1.00 72.86  ?  307 LEU A HD13 1 
ATOM   4598  H HD21 . LEU A 1 298 ? 24.305  -27.114 81.983  1.00 97.51  ?  307 LEU A HD21 1 
ATOM   4599  H HD22 . LEU A 1 298 ? 23.048  -26.142 81.946  1.00 97.51  ?  307 LEU A HD22 1 
ATOM   4600  H HD23 . LEU A 1 298 ? 23.742  -26.595 80.590  1.00 97.51  ?  307 LEU A HD23 1 
ATOM   4601  N N    . CYS A 1 299 ? 23.533  -21.957 78.630  1.00 83.50  ?  308 CYS A N    1 
ATOM   4602  C CA   . CYS A 1 299 ? 22.705  -20.819 78.290  1.00 95.32  ?  308 CYS A CA   1 
ATOM   4603  C C    . CYS A 1 299 ? 21.971  -21.076 76.969  1.00 72.07  ?  308 CYS A C    1 
ATOM   4604  O O    . CYS A 1 299 ? 20.797  -20.729 76.806  1.00 74.40  ?  308 CYS A O    1 
ATOM   4605  C CB   . CYS A 1 299 ? 23.605  -19.588 78.287  1.00 104.98 ?  308 CYS A CB   1 
ATOM   4606  S SG   . CYS A 1 299 ? 22.772  -18.162 77.895  1.00 170.92 ?  308 CYS A SG   1 
ATOM   4607  H H    . CYS A 1 299 ? 24.380  -21.811 78.628  1.00 100.20 ?  308 CYS A H    1 
ATOM   4608  H HA   . CYS A 1 299 ? 22.037  -20.698 78.983  1.00 114.38 ?  308 CYS A HA   1 
ATOM   4609  N N    . SER A 1 300 ? 22.643  -21.710 76.021  1.00 89.48  ?  309 SER A N    1 
ATOM   4610  C CA   . SER A 1 300 ? 22.037  -21.996 74.731  1.00 68.54  ?  309 SER A CA   1 
ATOM   4611  C C    . SER A 1 300 ? 21.009  -23.118 74.803  1.00 80.59  ?  309 SER A C    1 
ATOM   4612  O O    . SER A 1 300 ? 20.267  -23.321 73.827  1.00 85.41  ?  309 SER A O    1 
ATOM   4613  C CB   . SER A 1 300 ? 23.135  -22.342 73.718  1.00 70.72  ?  309 SER A CB   1 
ATOM   4614  H H    . SER A 1 300 ? 23.453  -21.986 76.100  1.00 107.38 ?  309 SER A H    1 
ATOM   4615  H HA   . SER A 1 300 ? 21.583  -21.199 74.416  1.00 82.25  ?  309 SER A HA   1 
ATOM   4616  N N    . LEU A 1 301 ? 21.028  -23.921 75.875  1.00 85.31  ?  310 LEU A N    1 
ATOM   4617  C CA   . LEU A 1 301 ? 19.898  -24.816 76.153  1.00 77.30  ?  310 LEU A CA   1 
ATOM   4618  C C    . LEU A 1 301 ? 18.634  -24.042 76.534  1.00 87.20  ?  310 LEU A C    1 
ATOM   4619  O O    . LEU A 1 301 ? 17.544  -24.390 76.069  1.00 99.33  ?  310 LEU A O    1 
ATOM   4620  C CB   . LEU A 1 301 ? 20.241  -25.808 77.265  1.00 57.43  ?  310 LEU A CB   1 
ATOM   4621  C CG   . LEU A 1 301 ? 21.240  -26.977 77.109  1.00 63.90  ?  310 LEU A CG   1 
ATOM   4622  C CD1  . LEU A 1 301 ? 21.334  -27.760 78.402  1.00 61.06  ?  310 LEU A CD1  1 
ATOM   4623  C CD2  . LEU A 1 301 ? 20.927  -27.956 75.992  1.00 78.12  ?  310 LEU A CD2  1 
ATOM   4624  H H    . LEU A 1 301 ? 21.669  -23.965 76.446  1.00 102.37 ?  310 LEU A H    1 
ATOM   4625  H HA   . LEU A 1 301 ? 19.701  -25.326 75.352  1.00 92.76  ?  310 LEU A HA   1 
ATOM   4626  H HB2  . LEU A 1 301 ? 20.571  -25.282 78.010  1.00 68.92  ?  310 LEU A HB2  1 
ATOM   4627  H HB3  . LEU A 1 301 ? 19.404  -26.217 77.535  1.00 68.92  ?  310 LEU A HB3  1 
ATOM   4628  H HG   . LEU A 1 301 ? 22.118  -26.606 76.930  1.00 76.68  ?  310 LEU A HG   1 
ATOM   4629  H HD11 . LEU A 1 301 ? 21.965  -28.488 78.285  1.00 73.27  ?  310 LEU A HD11 1 
ATOM   4630  H HD12 . LEU A 1 301 ? 21.639  -27.169 79.108  1.00 73.27  ?  310 LEU A HD12 1 
ATOM   4631  H HD13 . LEU A 1 301 ? 20.458  -28.114 78.621  1.00 73.27  ?  310 LEU A HD13 1 
ATOM   4632  H HD21 . LEU A 1 301 ? 21.608  -28.646 75.977  1.00 93.74  ?  310 LEU A HD21 1 
ATOM   4633  H HD22 . LEU A 1 301 ? 20.056  -28.352 76.155  1.00 93.74  ?  310 LEU A HD22 1 
ATOM   4634  H HD23 . LEU A 1 301 ? 20.921  -27.479 75.147  1.00 93.74  ?  310 LEU A HD23 1 
ATOM   4635  N N    . GLU A 1 302 ? 18.740  -23.011 77.399  1.00 70.71  ?  311 GLU A N    1 
ATOM   4636  C CA   . GLU A 1 302 ? 17.564  -22.207 77.740  1.00 65.68  ?  311 GLU A CA   1 
ATOM   4637  C C    . GLU A 1 302 ? 16.958  -21.593 76.498  1.00 68.66  ?  311 GLU A C    1 
ATOM   4638  O O    . GLU A 1 302 ? 15.767  -21.276 76.499  1.00 92.62  ?  311 GLU A O    1 
ATOM   4639  C CB   . GLU A 1 302 ? 17.879  -21.112 78.769  1.00 89.77  ?  311 GLU A CB   1 
ATOM   4640  C CG   . GLU A 1 302 ? 18.420  -21.591 80.095  1.00 139.18 ?  311 GLU A CG   1 
ATOM   4641  H H    . GLU A 1 302 ? 19.467  -22.767 77.788  1.00 84.85  ?  311 GLU A H    1 
ATOM   4642  H HA   . GLU A 1 302 ? 16.896  -22.791 78.133  1.00 78.82  ?  311 GLU A HA   1 
ATOM   4643  H HB2  . GLU A 1 302 ? 18.540  -20.514 78.385  1.00 107.72 ?  311 GLU A HB2  1 
ATOM   4644  H HB3  . GLU A 1 302 ? 17.064  -20.618 78.950  1.00 107.72 ?  311 GLU A HB3  1 
ATOM   4645  H HG2  . GLU A 1 302 ? 17.720  -22.068 80.567  1.00 167.02 ?  311 GLU A HG2  1 
ATOM   4646  H HG3  . GLU A 1 302 ? 19.173  -22.180 79.934  1.00 167.02 ?  311 GLU A HG3  1 
ATOM   4647  N N    . SER A 1 303 ? 17.752  -21.464 75.430  1.00 58.33  ?  312 SER A N    1 
ATOM   4648  C CA   . SER A 1 303 ? 17.360  -20.857 74.161  1.00 80.03  ?  312 SER A CA   1 
ATOM   4649  C C    . SER A 1 303 ? 16.536  -21.778 73.275  1.00 88.37  ?  312 SER A C    1 
ATOM   4650  O O    . SER A 1 303 ? 15.793  -21.293 72.396  1.00 85.00  ?  312 SER A O    1 
ATOM   4651  C CB   . SER A 1 303 ? 18.600  -20.449 73.386  1.00 81.32  ?  312 SER A CB   1 
ATOM   4652  O OG   . SER A 1 303 ? 19.197  -19.341 73.980  1.00 108.85 ?  312 SER A OG   1 
ATOM   4653  H H    . SER A 1 303 ? 18.567  -21.739 75.423  1.00 70.00  ?  312 SER A H    1 
ATOM   4654  H HA   . SER A 1 303 ? 16.837  -20.059 74.338  1.00 96.04  ?  312 SER A HA   1 
ATOM   4655  H HB2  . SER A 1 303 ? 19.231  -21.187 73.384  1.00 97.59  ?  312 SER A HB2  1 
ATOM   4656  H HB3  . SER A 1 303 ? 18.347  -20.225 72.477  1.00 97.59  ?  312 SER A HB3  1 
ATOM   4657  H HG   . SER A 1 303 ? 19.882  -19.119 73.549  1.00 130.62 ?  312 SER A HG   1 
ATOM   4658  N N    . ASN A 1 304 ? 16.769  -23.083 73.371  1.00 73.78  ?  313 ASN A N    1 
ATOM   4659  C CA   . ASN A 1 304 ? 15.981  -24.017 72.598  1.00 83.07  ?  313 ASN A CA   1 
ATOM   4660  C C    . ASN A 1 304 ? 14.609  -24.148 73.244  1.00 72.54  ?  313 ASN A C    1 
ATOM   4661  O O    . ASN A 1 304 ? 14.458  -23.960 74.454  1.00 140.60 ?  313 ASN A O    1 
ATOM   4662  C CB   . ASN A 1 304 ? 16.673  -25.386 72.504  1.00 86.06  ?  313 ASN A CB   1 
ATOM   4663  C CG   . ASN A 1 304 ? 17.862  -25.397 71.507  1.00 93.78  ?  313 ASN A CG   1 
ATOM   4664  O OD1  . ASN A 1 304 ? 17.711  -25.069 70.321  1.00 118.25 ?  313 ASN A OD1  1 
ATOM   4665  N ND2  . ASN A 1 304 ? 19.056  -25.759 72.008  1.00 72.83  ?  313 ASN A ND2  1 
ATOM   4666  H H    . ASN A 1 304 ? 17.369  -23.443 73.871  1.00 88.53  ?  313 ASN A H    1 
ATOM   4667  H HA   . ASN A 1 304 ? 15.864  -23.672 71.700  1.00 99.68  ?  313 ASN A HA   1 
ATOM   4668  H HB2  . ASN A 1 304 ? 17.015  -25.627 73.379  1.00 103.28 ?  313 ASN A HB2  1 
ATOM   4669  H HB3  . ASN A 1 304 ? 16.028  -26.046 72.207  1.00 103.28 ?  313 ASN A HB3  1 
ATOM   4670  H HD21 . ASN A 1 304 ? 19.748  -25.782 71.497  1.00 87.40  ?  313 ASN A HD21 1 
ATOM   4671  H HD22 . ASN A 1 304 ? 19.129  -25.967 72.839  1.00 87.40  ?  313 ASN A HD22 1 
ATOM   4672  N N    . PRO A 1 305 ? 13.596  -24.480 72.459  1.00 82.63  ?  314 PRO A N    1 
ATOM   4673  C CA   . PRO A 1 305 ? 12.243  -24.592 73.029  1.00 100.82 ?  314 PRO A CA   1 
ATOM   4674  C C    . PRO A 1 305 ? 12.141  -25.727 74.041  1.00 61.38  ?  314 PRO A C    1 
ATOM   4675  O O    . PRO A 1 305 ? 12.830  -26.739 73.945  1.00 93.11  ?  314 PRO A O    1 
ATOM   4676  C CB   . PRO A 1 305 ? 11.352  -24.832 71.805  1.00 96.65  ?  314 PRO A CB   1 
ATOM   4677  C CG   . PRO A 1 305 ? 12.292  -25.311 70.687  1.00 92.89  ?  314 PRO A CG   1 
ATOM   4678  C CD   . PRO A 1 305 ? 13.650  -24.736 71.001  1.00 85.24  ?  314 PRO A CD   1 
ATOM   4679  H HA   . PRO A 1 305 ? 11.986  -23.758 73.454  1.00 120.99 ?  314 PRO A HA   1 
ATOM   4680  H HB2  . PRO A 1 305 ? 10.693  -25.514 72.012  1.00 115.99 ?  314 PRO A HB2  1 
ATOM   4681  H HB3  . PRO A 1 305 ? 10.916  -24.003 71.553  1.00 115.99 ?  314 PRO A HB3  1 
ATOM   4682  H HG2  . PRO A 1 305 ? 12.325  -26.280 70.685  1.00 111.47 ?  314 PRO A HG2  1 
ATOM   4683  H HG3  . PRO A 1 305 ? 11.973  -24.980 69.832  1.00 111.47 ?  314 PRO A HG3  1 
ATOM   4684  H HD2  . PRO A 1 305 ? 14.344  -25.383 70.798  1.00 102.28 ?  314 PRO A HD2  1 
ATOM   4685  H HD3  . PRO A 1 305 ? 13.785  -23.906 70.518  1.00 102.28 ?  314 PRO A HD3  1 
ATOM   4686  N N    . SER A 1 306 ? 11.240  -25.539 75.002  1.00 101.94 ?  315 SER A N    1 
ATOM   4687  C CA   . SER A 1 306 ? 11.202  -26.349 76.216  1.00 74.36  ?  315 SER A CA   1 
ATOM   4688  C C    . SER A 1 306 ? 10.828  -27.795 75.932  1.00 95.48  ?  315 SER A C    1 
ATOM   4689  O O    . SER A 1 306 ? 9.835   -28.068 75.248  1.00 115.24 ?  315 SER A O    1 
ATOM   4690  C CB   . SER A 1 306 ? 10.219  -25.745 77.220  1.00 103.45 ?  315 SER A CB   1 
ATOM   4691  O OG   . SER A 1 306 ? 10.123  -26.525 78.396  1.00 119.32 ?  315 SER A OG   1 
ATOM   4692  H H    . SER A 1 306 ? 10.627  -24.935 74.973  1.00 122.33 ?  315 SER A H    1 
ATOM   4693  H HA   . SER A 1 306 ? 12.083  -26.345 76.623  1.00 89.23  ?  315 SER A HA   1 
ATOM   4694  H HB2  . SER A 1 306 ? 10.522  -24.855 77.459  1.00 124.14 ?  315 SER A HB2  1 
ATOM   4695  H HB3  . SER A 1 306 ? 9.342   -25.693 76.807  1.00 124.14 ?  315 SER A HB3  1 
ATOM   4696  H HG   . SER A 1 306 ? 9.578   -26.173 78.930  1.00 143.18 ?  315 SER A HG   1 
ATOM   4697  N N    . VAL A 1 307 ? 11.604  -28.733 76.494  1.00 99.16  ?  316 VAL A N    1 
ATOM   4698  C CA   . VAL A 1 307 ? 11.216  -30.138 76.402  1.00 82.91  ?  316 VAL A CA   1 
ATOM   4699  C C    . VAL A 1 307 ? 9.954   -30.395 77.229  1.00 77.39  ?  316 VAL A C    1 
ATOM   4700  O O    . VAL A 1 307 ? 9.041   -31.088 76.774  1.00 70.68  ?  316 VAL A O    1 
ATOM   4701  C CB   . VAL A 1 307 ? 12.396  -31.057 76.805  1.00 64.56  ?  316 VAL A CB   1 
ATOM   4702  C CG1  . VAL A 1 307 ? 12.008  -32.521 76.880  1.00 53.71  ?  316 VAL A CG1  1 
ATOM   4703  C CG2  . VAL A 1 307 ? 13.499  -30.982 75.792  1.00 126.50 ?  316 VAL A CG2  1 
ATOM   4704  H H    . VAL A 1 307 ? 12.337  -28.583 76.919  1.00 119.00 ?  316 VAL A H    1 
ATOM   4705  H HA   . VAL A 1 307 ? 11.000  -30.335 75.477  1.00 99.50  ?  316 VAL A HA   1 
ATOM   4706  H HB   . VAL A 1 307 ? 12.746  -30.783 77.667  1.00 77.48  ?  316 VAL A HB   1 
ATOM   4707  H HG11 . VAL A 1 307 ? 12.787  -33.040 77.136  1.00 64.45  ?  316 VAL A HG11 1 
ATOM   4708  H HG12 . VAL A 1 307 ? 11.307  -32.628 77.542  1.00 64.45  ?  316 VAL A HG12 1 
ATOM   4709  H HG13 . VAL A 1 307 ? 11.689  -32.808 76.010  1.00 64.45  ?  316 VAL A HG13 1 
ATOM   4710  H HG21 . VAL A 1 307 ? 14.222  -31.566 76.070  1.00 151.80 ?  316 VAL A HG21 1 
ATOM   4711  H HG22 . VAL A 1 307 ? 13.155  -31.267 74.930  1.00 151.80 ?  316 VAL A HG22 1 
ATOM   4712  H HG23 . VAL A 1 307 ? 13.814  -30.067 75.737  1.00 151.80 ?  316 VAL A HG23 1 
ATOM   4713  N N    . ARG A 1 308 ? 9.834   -29.771 78.399  1.00 77.29  ?  317 ARG A N    1 
ATOM   4714  C CA   . ARG A 1 308 ? 8.645   -29.978 79.225  1.00 68.12  ?  317 ARG A CA   1 
ATOM   4715  C C    . ARG A 1 308 ? 7.373   -29.521 78.475  1.00 97.52  ?  317 ARG A C    1 
ATOM   4716  O O    . ARG A 1 308 ? 6.401   -30.292 78.344  1.00 66.08  ?  317 ARG A O    1 
ATOM   4717  C CB   . ARG A 1 308 ? 8.818   -29.254 80.578  1.00 67.10  ?  317 ARG A CB   1 
ATOM   4718  C CG   . ARG A 1 308 ? 7.790   -29.571 81.641  1.00 88.86  ?  317 ARG A CG   1 
ATOM   4719  C CD   . ARG A 1 308 ? 8.085   -28.988 83.074  1.00 80.99  ?  317 ARG A CD   1 
ATOM   4720  N NE   . ARG A 1 308 ? 7.491   -29.825 84.149  1.00 58.71  ?  317 ARG A NE   1 
ATOM   4721  C CZ   . ARG A 1 308 ? 6.293   -29.626 84.704  1.00 118.29 ?  317 ARG A CZ   1 
ATOM   4722  N NH1  . ARG A 1 308 ? 5.549   -28.595 84.319  1.00 177.17 1  317 ARG A NH1  1 
ATOM   4723  N NH2  . ARG A 1 308 ? 5.832   -30.463 85.651  1.00 94.71  1  317 ARG A NH2  1 
ATOM   4724  H H    . ARG A 1 308 ? 10.414  -29.231 78.733  1.00 92.74  ?  317 ARG A H    1 
ATOM   4725  H HA   . ARG A 1 308 ? 8.554   -30.926 79.408  1.00 81.75  ?  317 ARG A HA   1 
ATOM   4726  H HB2  . ARG A 1 308 ? 9.688   -29.488 80.939  1.00 80.52  ?  317 ARG A HB2  1 
ATOM   4727  H HB3  . ARG A 1 308 ? 8.782   -28.298 80.418  1.00 80.52  ?  317 ARG A HB3  1 
ATOM   4728  H HG2  . ARG A 1 308 ? 6.934   -29.217 81.355  1.00 106.63 ?  317 ARG A HG2  1 
ATOM   4729  H HG3  . ARG A 1 308 ? 7.728   -30.536 81.728  1.00 106.63 ?  317 ARG A HG3  1 
ATOM   4730  H HD2  . ARG A 1 308 ? 9.044   -28.954 83.213  1.00 97.19  ?  317 ARG A HD2  1 
ATOM   4731  H HD3  . ARG A 1 308 ? 7.706   -28.098 83.140  1.00 97.19  ?  317 ARG A HD3  1 
ATOM   4732  H HE   . ARG A 1 308 ? 7.955   -30.490 84.435  1.00 70.45  ?  317 ARG A HE   1 
ATOM   4733  H HH11 . ARG A 1 308 ? 5.836   -28.062 83.708  1.00 212.60 ?  317 ARG A HH11 1 
ATOM   4734  H HH12 . ARG A 1 308 ? 4.779   -28.462 84.678  1.00 212.60 ?  317 ARG A HH12 1 
ATOM   4735  H HH21 . ARG A 1 308 ? 6.313   -31.128 85.909  1.00 113.65 ?  317 ARG A HH21 1 
ATOM   4736  H HH22 . ARG A 1 308 ? 5.065   -30.321 86.014  1.00 113.65 ?  317 ARG A HH22 1 
ATOM   4737  N N    . GLU A 1 309 ? 7.385   -28.301 77.904  1.00 72.39  ?  318 GLU A N    1 
ATOM   4738  C CA   . GLU A 1 309 ? 6.176   -27.801 77.239  1.00 69.98  ?  318 GLU A CA   1 
ATOM   4739  C C    . GLU A 1 309 ? 5.789   -28.691 76.077  1.00 95.72  ?  318 GLU A C    1 
ATOM   4740  O O    . GLU A 1 309 ? 4.606   -28.883 75.796  1.00 86.59  ?  318 GLU A O    1 
ATOM   4741  C CB   . GLU A 1 309 ? 6.330   -26.379 76.702  1.00 61.57  ?  318 GLU A CB   1 
ATOM   4742  C CG   . GLU A 1 309 ? 6.013   -25.252 77.736  1.00 92.56  ?  318 GLU A CG   1 
ATOM   4743  H H    . GLU A 1 309 ? 8.057   -27.764 77.890  1.00 86.87  ?  318 GLU A H    1 
ATOM   4744  H HA   . GLU A 1 309 ? 5.443   -27.804 77.875  1.00 83.98  ?  318 GLU A HA   1 
ATOM   4745  H HB2  . GLU A 1 309 ? 7.246   -26.257 76.407  1.00 73.89  ?  318 GLU A HB2  1 
ATOM   4746  H HB3  . GLU A 1 309 ? 5.727   -26.265 75.951  1.00 73.89  ?  318 GLU A HB3  1 
ATOM   4747  H HG2  . GLU A 1 309 ? 6.450   -25.463 78.576  1.00 111.07 ?  318 GLU A HG2  1 
ATOM   4748  H HG3  . GLU A 1 309 ? 6.343   -24.407 77.393  1.00 111.07 ?  318 GLU A HG3  1 
ATOM   4749  N N    . PHE A 1 310 ? 6.763   -29.247 75.390  1.00 60.77  ?  319 PHE A N    1 
ATOM   4750  C CA   . PHE A 1 310 ? 6.433   -30.102 74.271  1.00 62.56  ?  319 PHE A CA   1 
ATOM   4751  C C    . PHE A 1 310 ? 5.745   -31.368 74.736  1.00 76.50  ?  319 PHE A C    1 
ATOM   4752  O O    . PHE A 1 310 ? 4.764   -31.821 74.113  1.00 63.04  ?  319 PHE A O    1 
ATOM   4753  C CB   . PHE A 1 310 ? 7.699   -30.451 73.523  1.00 61.72  ?  319 PHE A CB   1 
ATOM   4754  C CG   . PHE A 1 310 ? 7.485   -31.290 72.303  1.00 82.93  ?  319 PHE A CG   1 
ATOM   4755  C CD1  . PHE A 1 310 ? 7.439   -32.674 72.377  1.00 84.07  ?  319 PHE A CD1  1 
ATOM   4756  C CD2  . PHE A 1 310 ? 7.383   -30.705 71.065  1.00 101.04 ?  319 PHE A CD2  1 
ATOM   4757  C CE1  . PHE A 1 310 ? 7.278   -33.438 71.239  1.00 99.97  ?  319 PHE A CE1  1 
ATOM   4758  C CE2  . PHE A 1 310 ? 7.223   -31.474 69.927  1.00 99.46  ?  319 PHE A CE2  1 
ATOM   4759  C CZ   . PHE A 1 310 ? 7.168   -32.839 70.022  1.00 108.16 ?  319 PHE A CZ   1 
ATOM   4760  H H    . PHE A 1 310 ? 7.604   -29.151 75.545  1.00 72.93  ?  319 PHE A H    1 
ATOM   4761  H HA   . PHE A 1 310 ? 5.838   -29.631 73.667  1.00 75.07  ?  319 PHE A HA   1 
ATOM   4762  H HB2  . PHE A 1 310 ? 8.131   -29.628 73.243  1.00 74.06  ?  319 PHE A HB2  1 
ATOM   4763  H HB3  . PHE A 1 310 ? 8.286   -30.941 74.119  1.00 74.06  ?  319 PHE A HB3  1 
ATOM   4764  H HD1  . PHE A 1 310 ? 7.517   -33.093 73.204  1.00 100.88 ?  319 PHE A HD1  1 
ATOM   4765  H HD2  . PHE A 1 310 ? 7.423   -29.778 70.990  1.00 121.25 ?  319 PHE A HD2  1 
ATOM   4766  H HE1  . PHE A 1 310 ? 7.239   -34.365 71.305  1.00 119.96 ?  319 PHE A HE1  1 
ATOM   4767  H HE2  . PHE A 1 310 ? 7.145   -31.063 69.096  1.00 119.36 ?  319 PHE A HE2  1 
ATOM   4768  H HZ   . PHE A 1 310 ? 7.052   -33.356 69.257  1.00 129.79 ?  319 PHE A HZ   1 
ATOM   4769  N N    . VAL A 1 311 ? 6.286   -31.993 75.791  1.00 61.22  ?  320 VAL A N    1 
ATOM   4770  C CA   . VAL A 1 311 ? 5.749   -33.282 76.218  1.00 78.91  ?  320 VAL A CA   1 
ATOM   4771  C C    . VAL A 1 311 ? 4.375   -33.099 76.821  1.00 68.28  ?  320 VAL A C    1 
ATOM   4772  O O    . VAL A 1 311 ? 3.479   -33.911 76.603  1.00 76.51  ?  320 VAL A O    1 
ATOM   4773  C CB   . VAL A 1 311 ? 6.716   -33.976 77.197  1.00 72.45  ?  320 VAL A CB   1 
ATOM   4774  C CG1  . VAL A 1 311 ? 6.059   -35.176 77.884  1.00 59.60  ?  320 VAL A CG1  1 
ATOM   4775  C CG2  . VAL A 1 311 ? 7.869   -34.502 76.451  1.00 81.38  ?  320 VAL A CG2  1 
ATOM   4776  H H    . VAL A 1 311 ? 6.945   -31.699 76.260  1.00 73.47  ?  320 VAL A H    1 
ATOM   4777  H HA   . VAL A 1 311 ? 5.656   -33.854 75.440  1.00 94.69  ?  320 VAL A HA   1 
ATOM   4778  H HB   . VAL A 1 311 ? 7.027   -33.349 77.869  1.00 86.94  ?  320 VAL A HB   1 
ATOM   4779  H HG11 . VAL A 1 311 ? 6.699   -35.582 78.489  1.00 71.52  ?  320 VAL A HG11 1 
ATOM   4780  H HG12 . VAL A 1 311 ? 5.283   -34.869 78.380  1.00 71.52  ?  320 VAL A HG12 1 
ATOM   4781  H HG13 . VAL A 1 311 ? 5.788   -35.817 77.209  1.00 71.52  ?  320 VAL A HG13 1 
ATOM   4782  H HG21 . VAL A 1 311 ? 8.475   -34.938 77.071  1.00 97.66  ?  320 VAL A HG21 1 
ATOM   4783  H HG22 . VAL A 1 311 ? 7.554   -35.141 75.792  1.00 97.66  ?  320 VAL A HG22 1 
ATOM   4784  H HG23 . VAL A 1 311 ? 8.321   -33.767 76.008  1.00 97.66  ?  320 VAL A HG23 1 
ATOM   4785  N N    . LEU A 1 312 ? 4.187   -32.007 77.548  1.00 66.39  ?  321 LEU A N    1 
ATOM   4786  C CA   . LEU A 1 312 ? 2.915   -31.678 78.154  1.00 71.37  ?  321 LEU A CA   1 
ATOM   4787  C C    . LEU A 1 312 ? 1.870   -31.431 77.105  1.00 74.40  ?  321 LEU A C    1 
ATOM   4788  O O    . LEU A 1 312 ? 0.679   -31.413 77.418  1.00 78.00  ?  321 LEU A O    1 
ATOM   4789  C CB   . LEU A 1 312 ? 3.056   -30.434 79.002  1.00 82.82  ?  321 LEU A CB   1 
ATOM   4790  C CG   . LEU A 1 312 ? 3.669   -30.581 80.375  1.00 91.19  ?  321 LEU A CG   1 
ATOM   4791  C CD1  . LEU A 1 312 ? 3.958   -29.183 80.879  1.00 101.91 ?  321 LEU A CD1  1 
ATOM   4792  C CD2  . LEU A 1 312 ? 2.745   -31.328 81.306  1.00 131.96 ?  321 LEU A CD2  1 
ATOM   4793  H H    . LEU A 1 312 ? 4.802   -31.427 77.707  1.00 79.67  ?  321 LEU A H    1 
ATOM   4794  H HA   . LEU A 1 312 ? 2.623   -32.409 78.720  1.00 85.64  ?  321 LEU A HA   1 
ATOM   4795  H HB2  . LEU A 1 312 ? 3.605   -29.800 78.514  1.00 99.38  ?  321 LEU A HB2  1 
ATOM   4796  H HB3  . LEU A 1 312 ? 2.171   -30.056 79.127  1.00 99.38  ?  321 LEU A HB3  1 
ATOM   4797  H HG   . LEU A 1 312 ? 4.505   -31.067 80.309  1.00 109.42 ?  321 LEU A HG   1 
ATOM   4798  H HD11 . LEU A 1 312 ? 4.354   -29.242 81.762  1.00 122.29 ?  321 LEU A HD11 1 
ATOM   4799  H HD12 . LEU A 1 312 ? 4.574   -28.748 80.268  1.00 122.29 ?  321 LEU A HD12 1 
ATOM   4800  H HD13 . LEU A 1 312 ? 3.127   -28.684 80.921  1.00 122.29 ?  321 LEU A HD13 1 
ATOM   4801  H HD21 . LEU A 1 312 ? 3.168   -31.404 82.176  1.00 158.36 ?  321 LEU A HD21 1 
ATOM   4802  H HD22 . LEU A 1 312 ? 1.912   -30.837 81.385  1.00 158.36 ?  321 LEU A HD22 1 
ATOM   4803  H HD23 . LEU A 1 312 ? 2.576   -32.210 80.941  1.00 158.36 ?  321 LEU A HD23 1 
ATOM   4804  N N    . SER A 1 313 ? 2.299   -31.056 75.910  1.00 60.80  ?  322 SER A N    1 
ATOM   4805  C CA   . SER A 1 313 ? 1.336   -30.659 74.912  1.00 70.56  ?  322 SER A CA   1 
ATOM   4806  C C    . SER A 1 313 ? 0.716   -31.856 74.218  1.00 84.56  ?  322 SER A C    1 
ATOM   4807  O O    . SER A 1 313 ? -0.389  -31.747 73.674  1.00 106.11 ?  322 SER A O    1 
ATOM   4808  C CB   . SER A 1 313 ? 2.014   -29.774 73.884  1.00 78.54  ?  322 SER A CB   1 
ATOM   4809  O OG   . SER A 1 313 ? 2.795   -30.568 73.012  1.00 92.85  ?  322 SER A OG   1 
ATOM   4810  H H    . SER A 1 313 ? 3.122   -31.025 75.660  1.00 72.96  ?  322 SER A H    1 
ATOM   4811  H HA   . SER A 1 313 ? 0.626   -30.149 75.335  1.00 84.67  ?  322 SER A HA   1 
ATOM   4812  H HB2  . SER A 1 313 ? 1.338   -29.305 73.370  1.00 94.25  ?  322 SER A HB2  1 
ATOM   4813  H HB3  . SER A 1 313 ? 2.589   -29.139 74.339  1.00 94.25  ?  322 SER A HB3  1 
ATOM   4814  H HG   . SER A 1 313 ? 3.382   -30.981 73.448  1.00 111.41 ?  322 SER A HG   1 
ATOM   4815  N N    . LYS A 1 314 ? 1.396   -32.994 74.227  1.00 63.14  ?  323 LYS A N    1 
ATOM   4816  C CA   . LYS A 1 314 ? 1.062   -34.005 73.245  1.00 85.07  ?  323 LYS A CA   1 
ATOM   4817  C C    . LYS A 1 314 ? 0.015   -35.033 73.721  1.00 110.12 ?  323 LYS A C    1 
ATOM   4818  O O    . LYS A 1 314 ? -0.656  -35.672 72.872  1.00 65.92  ?  323 LYS A O    1 
ATOM   4819  C CB   . LYS A 1 314 ? 2.373   -34.642 72.772  1.00 73.54  ?  323 LYS A CB   1 
ATOM   4820  C CG   . LYS A 1 314 ? 3.144   -33.764 71.796  1.00 94.47  ?  323 LYS A CG   1 
ATOM   4821  C CD   . LYS A 1 314 ? 2.563   -33.729 70.386  1.00 212.03 ?  323 LYS A CD   1 
ATOM   4822  H H    . LYS A 1 314 ? 2.032   -33.197 74.770  1.00 75.77  ?  323 LYS A H    1 
ATOM   4823  H HA   . LYS A 1 314 ? 0.677   -33.554 72.477  1.00 102.08 ?  323 LYS A HA   1 
ATOM   4824  H HB2  . LYS A 1 314 ? 2.941   -34.803 73.542  1.00 88.25  ?  323 LYS A HB2  1 
ATOM   4825  H HB3  . LYS A 1 314 ? 2.173   -35.480 72.326  1.00 88.25  ?  323 LYS A HB3  1 
ATOM   4826  H HG2  . LYS A 1 314 ? 3.150   -32.855 72.135  1.00 113.36 ?  323 LYS A HG2  1 
ATOM   4827  H HG3  . LYS A 1 314 ? 4.053   -34.095 71.732  1.00 113.36 ?  323 LYS A HG3  1 
ATOM   4828  H HD2  . LYS A 1 314 ? 2.411   -34.638 70.084  1.00 254.43 ?  323 LYS A HD2  1 
ATOM   4829  H HD3  . LYS A 1 314 ? 1.725   -33.240 70.402  1.00 254.43 ?  323 LYS A HD3  1 
ATOM   4830  N N    . GLY A 1 315 ? -0.231  -35.132 75.028  1.00 110.88 ?  324 GLY A N    1 
ATOM   4831  C CA   . GLY A 1 315 ? -1.197  -36.115 75.501  1.00 104.00 ?  324 GLY A CA   1 
ATOM   4832  C C    . GLY A 1 315 ? -0.762  -37.549 75.277  1.00 103.40 ?  324 GLY A C    1 
ATOM   4833  O O    . GLY A 1 315 ? -1.590  -38.436 75.066  1.00 88.86  ?  324 GLY A O    1 
ATOM   4834  H H    . GLY A 1 315 ? 0.137   -34.657 75.643  1.00 133.06 ?  324 GLY A H    1 
ATOM   4835  H HA2  . GLY A 1 315 ? -1.343  -35.988 76.452  1.00 124.80 ?  324 GLY A HA2  1 
ATOM   4836  H HA3  . GLY A 1 315 ? -2.041  -35.979 75.043  1.00 124.80 ?  324 GLY A HA3  1 
ATOM   4837  N N    . ASP A 1 316 ? 0.530   -37.784 75.316  1.00 98.46  ?  325 ASP A N    1 
ATOM   4838  C CA   . ASP A 1 316 ? 1.148   -39.027 74.891  1.00 77.62  ?  325 ASP A CA   1 
ATOM   4839  C C    . ASP A 1 316 ? 1.757   -39.662 76.136  1.00 95.31  ?  325 ASP A C    1 
ATOM   4840  O O    . ASP A 1 316 ? 2.855   -39.294 76.565  1.00 111.89 ?  325 ASP A O    1 
ATOM   4841  C CB   . ASP A 1 316 ? 2.188   -38.695 73.812  1.00 78.26  ?  325 ASP A CB   1 
ATOM   4842  C CG   . ASP A 1 316 ? 2.891   -39.917 73.230  1.00 97.25  ?  325 ASP A CG   1 
ATOM   4843  O OD1  . ASP A 1 316 ? 3.178   -40.876 73.983  1.00 83.74  ?  325 ASP A OD1  1 
ATOM   4844  O OD2  . ASP A 1 316 ? 3.186   -39.900 72.011  1.00 109.41 -1 325 ASP A OD2  1 
ATOM   4845  H H    . ASP A 1 316 ? 1.102   -37.209 75.601  1.00 118.16 ?  325 ASP A H    1 
ATOM   4846  H HA   . ASP A 1 316 ? 0.481   -39.625 74.520  1.00 93.14  ?  325 ASP A HA   1 
ATOM   4847  H HB2  . ASP A 1 316 ? 1.744   -38.233 73.083  1.00 93.91  ?  325 ASP A HB2  1 
ATOM   4848  H HB3  . ASP A 1 316 ? 2.866   -38.120 74.199  1.00 93.91  ?  325 ASP A HB3  1 
ATOM   4849  N N    . ALA A 1 317 ? 1.077   -40.660 76.681  1.00 60.22  ?  326 ALA A N    1 
ATOM   4850  C CA   . ALA A 1 317 ? 1.537   -41.260 77.930  1.00 78.47  ?  326 ALA A CA   1 
ATOM   4851  C C    . ALA A 1 317 ? 2.934   -41.871 77.820  1.00 69.22  ?  326 ALA A C    1 
ATOM   4852  O O    . ALA A 1 317 ? 3.693   -41.860 78.794  1.00 61.38  ?  326 ALA A O    1 
ATOM   4853  C CB   . ALA A 1 317 ? 0.575   -42.339 78.375  1.00 59.74  ?  326 ALA A CB   1 
ATOM   4854  H H    . ALA A 1 317 ? 0.359   -41.005 76.358  1.00 72.27  ?  326 ALA A H    1 
ATOM   4855  H HA   . ALA A 1 317 ? 1.562   -40.577 78.619  1.00 94.16  ?  326 ALA A HA   1 
ATOM   4856  H HB1  . ALA A 1 317 ? 0.896   -42.726 79.204  1.00 71.69  ?  326 ALA A HB1  1 
ATOM   4857  H HB2  . ALA A 1 317 ? -0.301  -41.944 78.510  1.00 71.69  ?  326 ALA A HB2  1 
ATOM   4858  H HB3  . ALA A 1 317 ? 0.528   -43.022 77.687  1.00 71.69  ?  326 ALA A HB3  1 
ATOM   4859  N N    . GLY A 1 318 ? 3.311   -42.367 76.651  1.00 72.24  ?  327 GLY A N    1 
ATOM   4860  C CA   . GLY A 1 318 ? 4.632   -42.921 76.515  1.00 60.56  ?  327 GLY A CA   1 
ATOM   4861  C C    . GLY A 1 318 ? 5.689   -41.848 76.698  1.00 68.11  ?  327 GLY A C    1 
ATOM   4862  O O    . GLY A 1 318 ? 6.646   -42.031 77.458  1.00 80.44  ?  327 GLY A O    1 
ATOM   4863  H H    . GLY A 1 318 ? 2.828   -42.393 75.939  1.00 86.69  ?  327 GLY A H    1 
ATOM   4864  H HA2  . GLY A 1 318 ? 4.769   -43.611 77.183  1.00 72.67  ?  327 GLY A HA2  1 
ATOM   4865  H HA3  . GLY A 1 318 ? 4.735   -43.314 75.635  1.00 72.67  ?  327 GLY A HA3  1 
ATOM   4866  N N    . LEU A 1 319 ? 5.488   -40.684 76.067  1.00 52.14  ?  328 LEU A N    1 
ATOM   4867  C CA   . LEU A 1 319 ? 6.424   -39.585 76.247  1.00 49.35  ?  328 LEU A CA   1 
ATOM   4868  C C    . LEU A 1 319 ? 6.443   -39.114 77.672  1.00 56.09  ?  328 LEU A C    1 
ATOM   4869  O O    . LEU A 1 319 ? 7.460   -38.655 78.155  1.00 66.31  ?  328 LEU A O    1 
ATOM   4870  C CB   . LEU A 1 319 ? 6.064   -38.426 75.360  1.00 88.94  ?  328 LEU A CB   1 
ATOM   4871  C CG   . LEU A 1 319 ? 6.586   -38.499 73.949  1.00 113.36 ?  328 LEU A CG   1 
ATOM   4872  C CD1  . LEU A 1 319 ? 5.941   -37.381 73.169  1.00 148.26 ?  328 LEU A CD1  1 
ATOM   4873  C CD2  . LEU A 1 319 ? 8.072   -38.368 73.950  1.00 112.98 ?  328 LEU A CD2  1 
ATOM   4874  H H    . LEU A 1 319 ? 4.829   -40.513 75.540  1.00 62.57  ?  328 LEU A H    1 
ATOM   4875  H HA   . LEU A 1 319 ? 7.317   -39.883 76.012  1.00 59.22  ?  328 LEU A HA   1 
ATOM   4876  H HB2  . LEU A 1 319 ? 5.097   -38.368 75.309  1.00 106.72 ?  328 LEU A HB2  1 
ATOM   4877  H HB3  . LEU A 1 319 ? 6.416   -37.614 75.758  1.00 106.72 ?  328 LEU A HB3  1 
ATOM   4878  H HG   . LEU A 1 319 ? 6.342   -39.348 73.547  1.00 136.04 ?  328 LEU A HG   1 
ATOM   4879  H HD11 . LEU A 1 319 ? 6.262   -37.408 72.254  1.00 177.91 ?  328 LEU A HD11 1 
ATOM   4880  H HD12 . LEU A 1 319 ? 4.978   -37.500 73.185  1.00 177.91 ?  328 LEU A HD12 1 
ATOM   4881  H HD13 . LEU A 1 319 ? 6.177   -36.534 73.578  1.00 177.91 ?  328 LEU A HD13 1 
ATOM   4882  H HD21 . LEU A 1 319 ? 8.394   -38.417 73.036  1.00 135.58 ?  328 LEU A HD21 1 
ATOM   4883  H HD22 . LEU A 1 319 ? 8.313   -37.513 74.340  1.00 135.58 ?  328 LEU A HD22 1 
ATOM   4884  H HD23 . LEU A 1 319 ? 8.452   -39.090 74.474  1.00 135.58 ?  328 LEU A HD23 1 
ATOM   4885  N N    . ARG A 1 320 ? 5.324   -39.178 78.355  1.00 76.30  ?  329 ARG A N    1 
ATOM   4886  C CA   . ARG A 1 320 ? 5.325   -38.722 79.729  1.00 76.98  ?  329 ARG A CA   1 
ATOM   4887  C C    . ARG A 1 320 ? 6.128   -39.670 80.615  1.00 80.29  ?  329 ARG A C    1 
ATOM   4888  O O    . ARG A 1 320 ? 7.027   -39.222 81.336  1.00 77.51  ?  329 ARG A O    1 
ATOM   4889  C CB   . ARG A 1 320 ? 3.869   -38.547 80.218  1.00 88.41  ?  329 ARG A CB   1 
ATOM   4890  C CG   . ARG A 1 320 ? 3.201   -37.239 79.723  1.00 112.82 ?  329 ARG A CG   1 
ATOM   4891  C CD   . ARG A 1 320 ? 1.986   -36.773 80.547  1.00 144.64 ?  329 ARG A CD   1 
ATOM   4892  N NE   . ARG A 1 320 ? 0.905   -37.731 80.469  1.00 114.09 ?  329 ARG A NE   1 
ATOM   4893  C CZ   . ARG A 1 320 ? 0.112   -37.828 79.414  1.00 119.43 ?  329 ARG A CZ   1 
ATOM   4894  N NH1  . ARG A 1 320 ? 0.291   -37.002 78.383  1.00 138.52 1  329 ARG A NH1  1 
ATOM   4895  N NH2  . ARG A 1 320 ? -0.849  -38.745 79.379  1.00 169.37 1  329 ARG A NH2  1 
ATOM   4896  H H    . ARG A 1 320 ? 4.570   -39.471 78.061  1.00 91.56  ?  329 ARG A H    1 
ATOM   4897  H HA   . ARG A 1 320 ? 5.753   -37.852 79.767  1.00 92.38  ?  329 ARG A HA   1 
ATOM   4898  H HB2  . ARG A 1 320 ? 3.339   -39.292 79.896  1.00 106.09 ?  329 ARG A HB2  1 
ATOM   4899  H HB3  . ARG A 1 320 ? 3.864   -38.534 81.188  1.00 106.09 ?  329 ARG A HB3  1 
ATOM   4900  H HG2  . ARG A 1 320 ? 3.860   -36.528 79.746  1.00 135.39 ?  329 ARG A HG2  1 
ATOM   4901  H HG3  . ARG A 1 320 ? 2.900   -37.374 78.811  1.00 135.39 ?  329 ARG A HG3  1 
ATOM   4902  H HD2  . ARG A 1 320 ? 2.245   -36.680 81.477  1.00 173.57 ?  329 ARG A HD2  1 
ATOM   4903  H HD3  . ARG A 1 320 ? 1.668   -35.925 80.199  1.00 173.57 ?  329 ARG A HD3  1 
ATOM   4904  H HE   . ARG A 1 320 ? 0.896   -38.375 81.040  1.00 136.91 ?  329 ARG A HE   1 
ATOM   4905  H HH11 . ARG A 1 320 ? 0.920   -36.416 78.405  1.00 166.23 ?  329 ARG A HH11 1 
ATOM   4906  H HH12 . ARG A 1 320 ? -0.222  -37.057 77.694  1.00 166.23 ?  329 ARG A HH12 1 
ATOM   4907  H HH21 . ARG A 1 320 ? -0.965  -39.272 80.048  1.00 203.24 ?  329 ARG A HH21 1 
ATOM   4908  H HH22 . ARG A 1 320 ? -1.369  -38.797 78.696  1.00 203.24 ?  329 ARG A HH22 1 
ATOM   4909  N N    . GLU A 1 321 ? 5.879   -40.992 80.514  1.00 61.31  ?  330 GLU A N    1 
ATOM   4910  C CA   . GLU A 1 321 ? 6.622   -41.945 81.347  1.00 65.35  ?  330 GLU A CA   1 
ATOM   4911  C C    . GLU A 1 321 ? 8.108   -41.825 81.036  1.00 88.03  ?  330 GLU A C    1 
ATOM   4912  O O    . GLU A 1 321 ? 8.959   -41.961 81.920  1.00 72.66  ?  330 GLU A O    1 
ATOM   4913  C CB   . GLU A 1 321 ? 6.145   -43.404 81.115  1.00 55.74  ?  330 GLU A CB   1 
ATOM   4914  C CG   . GLU A 1 321 ? 4.749   -43.704 81.730  1.00 81.71  ?  330 GLU A CG   1 
ATOM   4915  H H    . GLU A 1 321 ? 5.302   -41.348 79.986  1.00 73.57  ?  330 GLU A H    1 
ATOM   4916  H HA   . GLU A 1 321 ? 6.488   -41.726 82.282  1.00 78.42  ?  330 GLU A HA   1 
ATOM   4917  H HB2  . GLU A 1 321 ? 6.091   -43.568 80.160  1.00 66.89  ?  330 GLU A HB2  1 
ATOM   4918  H HB3  . GLU A 1 321 ? 6.785   -44.011 81.519  1.00 66.89  ?  330 GLU A HB3  1 
ATOM   4919  H HG2  . GLU A 1 321 ? 4.817   -43.673 82.697  1.00 98.05  ?  330 GLU A HG2  1 
ATOM   4920  H HG3  . GLU A 1 321 ? 4.117   -43.036 81.420  1.00 98.05  ?  330 GLU A HG3  1 
ATOM   4921  N N    . ALA A 1 322 ? 8.428   -41.538 79.779  1.00 73.49  ?  331 ALA A N    1 
ATOM   4922  C CA   . ALA A 1 322 ? 9.818   -41.431 79.377  1.00 47.62  ?  331 ALA A CA   1 
ATOM   4923  C C    . ALA A 1 322 ? 10.454  -40.181 79.939  1.00 98.41  ?  331 ALA A C    1 
ATOM   4924  O O    . ALA A 1 322 ? 11.583  -40.199 80.439  1.00 77.17  ?  331 ALA A O    1 
ATOM   4925  C CB   . ALA A 1 322 ? 9.941   -41.376 77.852  1.00 56.48  ?  331 ALA A CB   1 
ATOM   4926  H H    . ALA A 1 322 ? 7.861   -41.401 79.147  1.00 88.18  ?  331 ALA A H    1 
ATOM   4927  H HA   . ALA A 1 322 ? 10.311  -42.201 79.699  1.00 57.14  ?  331 ALA A HA   1 
ATOM   4928  H HB1  . ALA A 1 322 ? 10.879  -41.305 77.613  1.00 67.78  ?  331 ALA A HB1  1 
ATOM   4929  H HB2  . ALA A 1 322 ? 9.564   -42.187 77.476  1.00 67.78  ?  331 ALA A HB2  1 
ATOM   4930  H HB3  . ALA A 1 322 ? 9.456   -40.602 77.524  1.00 67.78  ?  331 ALA A HB3  1 
ATOM   4931  N N    . TYR A 1 323 ? 9.739   -39.084 79.854  1.00 74.69  ?  332 TYR A N    1 
ATOM   4932  C CA   . TYR A 1 323 ? 10.205  -37.878 80.490  1.00 55.08  ?  332 TYR A CA   1 
ATOM   4933  C C    . TYR A 1 323 ? 10.307  -38.097 81.974  1.00 58.48  ?  332 TYR A C    1 
ATOM   4934  O O    . TYR A 1 323 ? 11.268  -37.636 82.579  1.00 50.35  ?  332 TYR A O    1 
ATOM   4935  C CB   . TYR A 1 323 ? 9.244   -36.726 80.158  1.00 54.89  ?  332 TYR A CB   1 
ATOM   4936  C CG   . TYR A 1 323 ? 9.453   -35.415 80.906  1.00 54.62  ?  332 TYR A CG   1 
ATOM   4937  C CD1  . TYR A 1 323 ? 10.246  -34.406 80.339  1.00 72.77  ?  332 TYR A CD1  1 
ATOM   4938  C CD2  . TYR A 1 323 ? 8.853   -35.171 82.151  1.00 45.61  ?  332 TYR A CD2  1 
ATOM   4939  C CE1  . TYR A 1 323 ? 10.452  -33.215 80.966  1.00 60.92  ?  332 TYR A CE1  1 
ATOM   4940  C CE2  . TYR A 1 323 ? 9.071   -33.962 82.802  1.00 86.49  ?  332 TYR A CE2  1 
ATOM   4941  C CZ   . TYR A 1 323 ? 9.858   -32.993 82.196  1.00 64.36  ?  332 TYR A CZ   1 
ATOM   4942  O OH   . TYR A 1 323 ? 10.062  -31.790 82.803  1.00 84.32  ?  332 TYR A OH   1 
ATOM   4943  H H    . TYR A 1 323 ? 8.990   -39.010 79.440  1.00 89.63  ?  332 TYR A H    1 
ATOM   4944  H HA   . TYR A 1 323 ? 11.085  -37.652 80.151  1.00 66.10  ?  332 TYR A HA   1 
ATOM   4945  H HB2  . TYR A 1 323 ? 9.323   -36.530 79.211  1.00 65.87  ?  332 TYR A HB2  1 
ATOM   4946  H HB3  . TYR A 1 323 ? 8.340   -37.022 80.348  1.00 65.87  ?  332 TYR A HB3  1 
ATOM   4947  H HD1  . TYR A 1 323 ? 10.641  -34.555 79.510  1.00 87.32  ?  332 TYR A HD1  1 
ATOM   4948  H HD2  . TYR A 1 323 ? 8.326   -35.825 82.549  1.00 54.73  ?  332 TYR A HD2  1 
ATOM   4949  H HE1  . TYR A 1 323 ? 10.979  -32.559 80.571  1.00 73.10  ?  332 TYR A HE1  1 
ATOM   4950  H HE2  . TYR A 1 323 ? 8.672   -33.795 83.625  1.00 103.79 ?  332 TYR A HE2  1 
ATOM   4951  H HH   . TYR A 1 323 ? 10.553  -31.305 82.323  1.00 101.19 ?  332 TYR A HH   1 
ATOM   4952  N N    . ASP A 1 324 ? 9.300   -38.752 82.594  1.00 62.76  ?  333 ASP A N    1 
ATOM   4953  C CA   . ASP A 1 324 ? 9.367   -38.978 84.032  1.00 59.42  ?  333 ASP A CA   1 
ATOM   4954  C C    . ASP A 1 324 ? 10.598  -39.797 84.397  1.00 63.21  ?  333 ASP A C    1 
ATOM   4955  O O    . ASP A 1 324 ? 11.208  -39.580 85.453  1.00 52.50  ?  333 ASP A O    1 
ATOM   4956  C CB   . ASP A 1 324 ? 8.112   -39.675 84.557  1.00 92.99  ?  333 ASP A CB   1 
ATOM   4957  C CG   . ASP A 1 324 ? 6.920   -38.744 84.769  1.00 123.78 ?  333 ASP A CG   1 
ATOM   4958  O OD1  . ASP A 1 324 ? 7.128   -37.542 84.969  1.00 104.79 ?  333 ASP A OD1  1 
ATOM   4959  O OD2  . ASP A 1 324 ? 5.767   -39.240 84.768  1.00 153.54 -1 333 ASP A OD2  1 
ATOM   4960  H H    . ASP A 1 324 ? 8.595   -39.061 82.209  1.00 75.31  ?  333 ASP A H    1 
ATOM   4961  H HA   . ASP A 1 324 ? 9.439   -38.121 84.480  1.00 71.30  ?  333 ASP A HA   1 
ATOM   4962  H HB2  . ASP A 1 324 ? 7.845   -40.356 83.920  1.00 111.59 ?  333 ASP A HB2  1 
ATOM   4963  H HB3  . ASP A 1 324 ? 8.319   -40.088 85.410  1.00 111.59 ?  333 ASP A HB3  1 
ATOM   4964  N N    . ALA A 1 325 ? 11.016  -40.706 83.535  1.00 72.58  ?  334 ALA A N    1 
ATOM   4965  C CA   . ALA A 1 325 ? 12.140  -41.538 83.909  1.00 69.02  ?  334 ALA A CA   1 
ATOM   4966  C C    . ALA A 1 325 ? 13.389  -40.676 84.087  1.00 97.68  ?  334 ALA A C    1 
ATOM   4967  O O    . ALA A 1 325 ? 14.131  -40.834 85.069  1.00 95.38  ?  334 ALA A O    1 
ATOM   4968  C CB   . ALA A 1 325 ? 12.334  -42.627 82.858  1.00 44.86  ?  334 ALA A CB   1 
ATOM   4969  H H    . ALA A 1 325 ? 10.681  -40.858 82.758  1.00 87.10  ?  334 ALA A H    1 
ATOM   4970  H HA   . ALA A 1 325 ? 11.948  -41.968 84.756  1.00 82.83  ?  334 ALA A HA   1 
ATOM   4971  H HB1  . ALA A 1 325 ? 13.089  -43.181 83.114  1.00 53.83  ?  334 ALA A HB1  1 
ATOM   4972  H HB2  . ALA A 1 325 ? 11.529  -43.166 82.810  1.00 53.83  ?  334 ALA A HB2  1 
ATOM   4973  H HB3  . ALA A 1 325 ? 12.506  -42.210 81.999  1.00 53.83  ?  334 ALA A HB3  1 
ATOM   4974  N N    . CYS A 1 326 ? 13.591  -39.701 83.194  1.00 64.34  ?  335 CYS A N    1 
ATOM   4975  C CA   . CYS A 1 326 ? 14.745  -38.834 83.331  1.00 97.58  ?  335 CYS A CA   1 
ATOM   4976  C C    . CYS A 1 326 ? 14.645  -37.997 84.580  1.00 79.61  ?  335 CYS A C    1 
ATOM   4977  O O    . CYS A 1 326 ? 15.625  -37.849 85.314  1.00 55.08  ?  335 CYS A O    1 
ATOM   4978  C CB   . CYS A 1 326 ? 14.868  -37.936 82.115  1.00 70.49  ?  335 CYS A CB   1 
ATOM   4979  S SG   . CYS A 1 326 ? 15.005  -38.821 80.625  1.00 95.02  ?  335 CYS A SG   1 
ATOM   4980  H H    . CYS A 1 326 ? 13.086  -39.531 82.520  1.00 77.21  ?  335 CYS A H    1 
ATOM   4981  H HA   . CYS A 1 326 ? 15.548  -39.376 83.392  1.00 117.09 ?  335 CYS A HA   1 
ATOM   4982  H HB2  . CYS A 1 326 ? 14.079  -37.374 82.057  1.00 84.59  ?  335 CYS A HB2  1 
ATOM   4983  H HB3  . CYS A 1 326 ? 15.661  -37.385 82.209  1.00 84.59  ?  335 CYS A HB3  1 
ATOM   4984  H HG   . CYS A 1 326 ? 15.097  -38.043 79.716  1.00 114.02 ?  335 CYS A HG   1 
ATOM   4985  N N    . VAL A 1 327 ? 13.450  -37.510 84.880  1.00 83.64  ?  336 VAL A N    1 
ATOM   4986  C CA   . VAL A 1 327 ? 13.253  -36.719 86.083  1.00 61.53  ?  336 VAL A CA   1 
ATOM   4987  C C    . VAL A 1 327 ? 13.421  -37.573 87.332  1.00 70.99  ?  336 VAL A C    1 
ATOM   4988  O O    . VAL A 1 327 ? 14.061  -37.138 88.303  1.00 63.26  ?  336 VAL A O    1 
ATOM   4989  C CB   . VAL A 1 327 ? 11.883  -36.020 85.995  1.00 62.15  ?  336 VAL A CB   1 
ATOM   4990  C CG1  . VAL A 1 327 ? 11.561  -35.215 87.255  1.00 44.92  ?  336 VAL A CG1  1 
ATOM   4991  C CG2  . VAL A 1 327 ? 11.844  -35.108 84.800  1.00 106.42 ?  336 VAL A CG2  1 
ATOM   4992  H H    . VAL A 1 327 ? 12.741  -37.623 84.406  1.00 100.36 ?  336 VAL A H    1 
ATOM   4993  H HA   . VAL A 1 327 ? 13.932  -36.026 86.110  1.00 73.83  ?  336 VAL A HA   1 
ATOM   4994  H HB   . VAL A 1 327 ? 11.192  -36.692 85.883  1.00 74.58  ?  336 VAL A HB   1 
ATOM   4995  H HG11 . VAL A 1 327 ? 10.692  -34.798 87.149  1.00 53.90  ?  336 VAL A HG11 1 
ATOM   4996  H HG12 . VAL A 1 327 ? 11.549  -35.815 88.018  1.00 53.90  ?  336 VAL A HG12 1 
ATOM   4997  H HG13 . VAL A 1 327 ? 12.242  -34.536 87.378  1.00 53.90  ?  336 VAL A HG13 1 
ATOM   4998  H HG21 . VAL A 1 327 ? 10.976  -34.677 84.761  1.00 127.70 ?  336 VAL A HG21 1 
ATOM   4999  H HG22 . VAL A 1 327 ? 12.541  -34.440 84.891  1.00 127.70 ?  336 VAL A HG22 1 
ATOM   5000  H HG23 . VAL A 1 327 ? 11.991  -35.633 83.998  1.00 127.70 ?  336 VAL A HG23 1 
ATOM   5001  N N    . LYS A 1 328 ? 12.867  -38.802 87.333  1.00 60.77  ?  337 LYS A N    1 
ATOM   5002  C CA   . LYS A 1 328 ? 12.999  -39.661 88.510  1.00 54.93  ?  337 LYS A CA   1 
ATOM   5003  C C    . LYS A 1 328 ? 14.459  -40.030 88.742  1.00 64.37  ?  337 LYS A C    1 
ATOM   5004  O O    . LYS A 1 328 ? 14.936  -39.991 89.881  1.00 61.89  ?  337 LYS A O    1 
ATOM   5005  C CB   . LYS A 1 328 ? 12.099  -40.912 88.386  1.00 63.48  ?  337 LYS A CB   1 
ATOM   5006  H H    . LYS A 1 328 ? 12.424  -39.146 86.681  1.00 72.93  ?  337 LYS A H    1 
ATOM   5007  H HA   . LYS A 1 328 ? 12.698  -39.164 89.287  1.00 65.92  ?  337 LYS A HA   1 
ATOM   5008  N N    . ALA A 1 329 ? 15.212  -40.261 87.666  1.00 85.70  ?  338 ALA A N    1 
ATOM   5009  C CA   . ALA A 1 329 ? 16.626  -40.571 87.837  1.00 65.75  ?  338 ALA A CA   1 
ATOM   5010  C C    . ALA A 1 329 ? 17.330  -39.430 88.530  1.00 81.83  ?  338 ALA A C    1 
ATOM   5011  O O    . ALA A 1 329 ? 18.071  -39.651 89.501  1.00 59.59  ?  338 ALA A O    1 
ATOM   5012  C CB   . ALA A 1 329 ? 17.290  -40.847 86.495  1.00 72.61  ?  338 ALA A CB   1 
ATOM   5013  H H    . ALA A 1 329 ? 14.937  -40.245 86.851  1.00 102.84 ?  338 ALA A H    1 
ATOM   5014  H HA   . ALA A 1 329 ? 16.715  -41.363 88.389  1.00 78.90  ?  338 ALA A HA   1 
ATOM   5015  H HB1  . ALA A 1 329 ? 18.227  -41.049 86.642  1.00 87.13  ?  338 ALA A HB1  1 
ATOM   5016  H HB2  . ALA A 1 329 ? 16.850  -41.603 86.075  1.00 87.13  ?  338 ALA A HB2  1 
ATOM   5017  H HB3  . ALA A 1 329 ? 17.205  -40.060 85.933  1.00 87.13  ?  338 ALA A HB3  1 
ATOM   5018  N N    . LEU A 1 330 ? 17.025  -38.195 88.121  1.00 71.96  ?  339 LEU A N    1 
ATOM   5019  C CA   . LEU A 1 330 ? 17.656  -37.062 88.773  1.00 55.62  ?  339 LEU A CA   1 
ATOM   5020  C C    . LEU A 1 330 ? 17.248  -36.989 90.218  1.00 61.08  ?  339 LEU A C    1 
ATOM   5021  O O    . LEU A 1 330 ? 17.957  -36.396 91.037  1.00 44.62  ?  339 LEU A O    1 
ATOM   5022  C CB   . LEU A 1 330 ? 17.288  -35.735 88.140  1.00 64.84  ?  339 LEU A CB   1 
ATOM   5023  C CG   . LEU A 1 330 ? 17.830  -35.393 86.755  1.00 67.86  ?  339 LEU A CG   1 
ATOM   5024  C CD1  . LEU A 1 330 ? 17.406  -33.944 86.429  1.00 73.30  ?  339 LEU A CD1  1 
ATOM   5025  C CD2  . LEU A 1 330 ? 19.286  -35.580 86.604  1.00 62.24  ?  339 LEU A CD2  1 
ATOM   5026  H H    . LEU A 1 330 ? 16.475  -37.997 87.490  1.00 86.35  ?  339 LEU A H    1 
ATOM   5027  H HA   . LEU A 1 330 ? 18.620  -37.164 88.732  1.00 66.75  ?  339 LEU A HA   1 
ATOM   5028  H HB2  . LEU A 1 330 ? 16.321  -35.698 88.077  1.00 77.81  ?  339 LEU A HB2  1 
ATOM   5029  H HB3  . LEU A 1 330 ? 17.588  -35.032 88.738  1.00 77.81  ?  339 LEU A HB3  1 
ATOM   5030  H HG   . LEU A 1 330 ? 17.398  -35.972 86.108  1.00 81.43  ?  339 LEU A HG   1 
ATOM   5031  H HD11 . LEU A 1 330 ? 17.742  -33.707 85.551  1.00 87.96  ?  339 LEU A HD11 1 
ATOM   5032  H HD12 . LEU A 1 330 ? 16.438  -33.889 86.440  1.00 87.96  ?  339 LEU A HD12 1 
ATOM   5033  H HD13 . LEU A 1 330 ? 17.779  -33.349 87.098  1.00 87.96  ?  339 LEU A HD13 1 
ATOM   5034  H HD21 . LEU A 1 330 ? 19.542  -35.341 85.700  1.00 74.68  ?  339 LEU A HD21 1 
ATOM   5035  H HD22 . LEU A 1 330 ? 19.745  -35.009 87.240  1.00 74.68  ?  339 LEU A HD22 1 
ATOM   5036  H HD23 . LEU A 1 330 ? 19.504  -36.509 86.776  1.00 74.68  ?  339 LEU A HD23 1 
ATOM   5037  N N    . VAL A 1 331 ? 16.013  -37.377 90.513  1.00 66.35  ?  340 VAL A N    1 
ATOM   5038  C CA   . VAL A 1 331 ? 15.629  -37.342 91.917  1.00 77.74  ?  340 VAL A CA   1 
ATOM   5039  C C    . VAL A 1 331 ? 16.478  -38.304 92.701  1.00 68.40  ?  340 VAL A C    1 
ATOM   5040  O O    . VAL A 1 331 ? 16.752  -38.081 93.887  1.00 68.23  ?  340 VAL A O    1 
ATOM   5041  C CB   . VAL A 1 331 ? 14.142  -37.648 92.051  1.00 74.51  ?  340 VAL A CB   1 
ATOM   5042  C CG1  . VAL A 1 331 ? 13.743  -37.719 93.532  1.00 92.49  ?  340 VAL A CG1  1 
ATOM   5043  C CG2  . VAL A 1 331 ? 13.399  -36.582 91.303  1.00 54.35  ?  340 VAL A CG2  1 
ATOM   5044  H H    . VAL A 1 331 ? 15.414  -37.648 89.960  1.00 79.62  ?  340 VAL A H    1 
ATOM   5045  H HA   . VAL A 1 331 ? 15.785  -36.450 92.266  1.00 93.29  ?  340 VAL A HA   1 
ATOM   5046  H HB   . VAL A 1 331 ? 13.949  -38.505 91.639  1.00 89.41  ?  340 VAL A HB   1 
ATOM   5047  H HG11 . VAL A 1 331 ? 12.795  -37.914 93.595  1.00 110.99 ?  340 VAL A HG11 1 
ATOM   5048  H HG12 . VAL A 1 331 ? 14.256  -38.421 93.963  1.00 110.99 ?  340 VAL A HG12 1 
ATOM   5049  H HG13 . VAL A 1 331 ? 13.934  -36.865 93.952  1.00 110.99 ?  340 VAL A HG13 1 
ATOM   5050  H HG21 . VAL A 1 331 ? 12.447  -36.754 91.372  1.00 65.22  ?  340 VAL A HG21 1 
ATOM   5051  H HG22 . VAL A 1 331 ? 13.609  -35.719 91.691  1.00 65.22  ?  340 VAL A HG22 1 
ATOM   5052  H HG23 . VAL A 1 331 ? 13.672  -36.602 90.372  1.00 65.22  ?  340 VAL A HG23 1 
ATOM   5053  N N    . SER A 1 332 ? 16.873  -39.408 92.066  1.00 65.39  ?  341 SER A N    1 
ATOM   5054  C CA   . SER A 1 332 ? 17.721  -40.380 92.733  1.00 70.27  ?  341 SER A CA   1 
ATOM   5055  C C    . SER A 1 332 ? 19.090  -39.782 93.000  1.00 68.96  ?  341 SER A C    1 
ATOM   5056  O O    . SER A 1 332 ? 19.624  -39.865 94.117  1.00 58.22  ?  341 SER A O    1 
ATOM   5057  C CB   . SER A 1 332 ? 17.812  -41.628 91.878  1.00 62.78  ?  341 SER A CB   1 
ATOM   5058  O OG   . SER A 1 332 ? 16.487  -42.092 91.671  1.00 79.73  ?  341 SER A OG   1 
ATOM   5059  H H    . SER A 1 332 ? 16.663  -39.612 91.257  1.00 78.47  ?  341 SER A H    1 
ATOM   5060  H HA   . SER A 1 332 ? 17.323  -40.623 93.583  1.00 84.33  ?  341 SER A HA   1 
ATOM   5061  H HB2  . SER A 1 332 ? 18.220  -41.411 91.025  1.00 75.34  ?  341 SER A HB2  1 
ATOM   5062  H HB3  . SER A 1 332 ? 18.328  -42.306 92.342  1.00 75.34  ?  341 SER A HB3  1 
ATOM   5063  H HG   . SER A 1 332 ? 16.497  -42.787 91.199  1.00 95.67  ?  341 SER A HG   1 
ATOM   5064  N N    . LEU A 1 333 ? 19.616  -39.066 92.019  1.00 45.80  ?  342 LEU A N    1 
ATOM   5065  C CA   . LEU A 1 333 ? 20.929  -38.426 92.229  1.00 50.19  ?  342 LEU A CA   1 
ATOM   5066  C C    . LEU A 1 333 ? 20.856  -37.351 93.334  1.00 45.80  ?  342 LEU A C    1 
ATOM   5067  O O    . LEU A 1 333 ? 21.734  -37.256 94.203  1.00 58.25  ?  342 LEU A O    1 
ATOM   5068  C CB   . LEU A 1 333 ? 21.430  -37.844 90.918  1.00 53.16  ?  342 LEU A CB   1 
ATOM   5069  C CG   . LEU A 1 333 ? 21.962  -38.912 89.929  1.00 68.43  ?  342 LEU A CG   1 
ATOM   5070  C CD1  . LEU A 1 333 ? 21.825  -38.499 88.463  1.00 70.58  ?  342 LEU A CD1  1 
ATOM   5071  C CD2  . LEU A 1 333 ? 23.390  -39.272 90.237  1.00 112.92 ?  342 LEU A CD2  1 
ATOM   5072  H H    . LEU A 1 333 ? 19.260  -38.932 91.248  1.00 54.96  ?  342 LEU A H    1 
ATOM   5073  H HA   . LEU A 1 333 ? 21.563  -39.102 92.515  1.00 60.22  ?  342 LEU A HA   1 
ATOM   5074  H HB2  . LEU A 1 333 ? 20.700  -37.374 90.484  1.00 63.79  ?  342 LEU A HB2  1 
ATOM   5075  H HB3  . LEU A 1 333 ? 22.154  -37.226 91.106  1.00 63.79  ?  342 LEU A HB3  1 
ATOM   5076  H HG   . LEU A 1 333 ? 21.435  -39.718 90.047  1.00 82.12  ?  342 LEU A HG   1 
ATOM   5077  H HD11 . LEU A 1 333 ? 22.175  -39.209 87.901  1.00 84.69  ?  342 LEU A HD11 1 
ATOM   5078  H HD12 . LEU A 1 333 ? 20.888  -38.351 88.263  1.00 84.69  ?  342 LEU A HD12 1 
ATOM   5079  H HD13 . LEU A 1 333 ? 22.328  -37.683 88.317  1.00 84.69  ?  342 LEU A HD13 1 
ATOM   5080  H HD21 . LEU A 1 333 ? 23.691  -39.940 89.602  1.00 135.50 ?  342 LEU A HD21 1 
ATOM   5081  H HD22 . LEU A 1 333 ? 23.939  -38.475 90.164  1.00 135.50 ?  342 LEU A HD22 1 
ATOM   5082  H HD23 . LEU A 1 333 ? 23.438  -39.626 91.139  1.00 135.50 ?  342 LEU A HD23 1 
ATOM   5083  N N    . ARG A 1 334 ? 19.771  -36.603 93.395  1.00 64.76  ?  343 ARG A N    1 
ATOM   5084  C CA   . ARG A 1 334 ? 19.706  -35.682 94.502  1.00 62.54  ?  343 ARG A CA   1 
ATOM   5085  C C    . ARG A 1 334 ? 19.515  -36.425 95.813  1.00 61.77  ?  343 ARG A C    1 
ATOM   5086  O O    . ARG A 1 334 ? 20.158  -36.061 96.815  1.00 61.47  ?  343 ARG A O    1 
ATOM   5087  C CB   . ARG A 1 334 ? 18.616  -34.616 94.271  1.00 90.72  ?  343 ARG A CB   1 
ATOM   5088  C CG   . ARG A 1 334 ? 19.045  -33.468 93.376  1.00 77.55  ?  343 ARG A CG   1 
ATOM   5089  C CD   . ARG A 1 334 ? 19.501  -33.928 92.029  1.00 62.14  ?  343 ARG A CD   1 
ATOM   5090  N NE   . ARG A 1 334 ? 20.428  -33.026 91.324  1.00 51.55  ?  343 ARG A NE   1 
ATOM   5091  C CZ   . ARG A 1 334 ? 20.042  -32.084 90.475  1.00 90.45  ?  343 ARG A CZ   1 
ATOM   5092  N NH1  . ARG A 1 334 ? 18.735  -31.880 90.224  1.00 95.38  1  343 ARG A NH1  1 
ATOM   5093  N NH2  . ARG A 1 334 ? 20.967  -31.375 89.843  1.00 82.75  1  343 ARG A NH2  1 
ATOM   5094  H H    . ARG A 1 334 ? 19.105  -36.606 92.851  1.00 77.71  ?  343 ARG A H    1 
ATOM   5095  H HA   . ARG A 1 334 ? 20.555  -35.216 94.558  1.00 75.05  ?  343 ARG A HA   1 
ATOM   5096  H HB2  . ARG A 1 334 ? 17.849  -35.041 93.858  1.00 108.86 ?  343 ARG A HB2  1 
ATOM   5097  H HB3  . ARG A 1 334 ? 18.361  -34.242 95.129  1.00 108.86 ?  343 ARG A HB3  1 
ATOM   5098  H HG2  . ARG A 1 334 ? 18.294  -32.867 93.250  1.00 93.06  ?  343 ARG A HG2  1 
ATOM   5099  H HG3  . ARG A 1 334 ? 19.781  -32.996 93.798  1.00 93.06  ?  343 ARG A HG3  1 
ATOM   5100  H HD2  . ARG A 1 334 ? 19.950  -34.781 92.134  1.00 74.57  ?  343 ARG A HD2  1 
ATOM   5101  H HD3  . ARG A 1 334 ? 18.721  -34.041 91.465  1.00 74.57  ?  343 ARG A HD3  1 
ATOM   5102  H HE   . ARG A 1 334 ? 21.262  -33.063 91.532  1.00 61.86  ?  343 ARG A HE   1 
ATOM   5103  H HH11 . ARG A 1 334 ? 18.141  -32.359 90.621  1.00 114.45 ?  343 ARG A HH11 1 
ATOM   5104  H HH12 . ARG A 1 334 ? 18.493  -31.265 89.674  1.00 114.45 ?  343 ARG A HH12 1 
ATOM   5105  H HH21 . ARG A 1 334 ? 21.800  -31.506 90.014  1.00 99.30  ?  343 ARG A HH21 1 
ATOM   5106  H HH22 . ARG A 1 334 ? 20.733  -30.746 89.305  1.00 99.30  ?  343 ARG A HH22 1 
ATOM   5107  N N    . SER A 1 335 ? 18.748  -37.525 95.826  1.00 52.40  ?  344 SER A N    1 
ATOM   5108  C CA   . SER A 1 335 ? 18.525  -38.117 97.141  1.00 75.09  ?  344 SER A CA   1 
ATOM   5109  C C    . SER A 1 335 ? 19.812  -38.751 97.634  1.00 67.42  ?  344 SER A C    1 
ATOM   5110  O O    . SER A 1 335 ? 20.221  -38.504 98.777  1.00 44.24  ?  344 SER A O    1 
ATOM   5111  C CB   . SER A 1 335 ? 17.376  -39.105 97.110  1.00 93.31  ?  344 SER A CB   1 
ATOM   5112  O OG   . SER A 1 335 ? 16.163  -38.407 96.978  1.00 112.57 ?  344 SER A OG   1 
ATOM   5113  H H    . SER A 1 335 ? 18.379  -37.913 95.153  1.00 62.88  ?  344 SER A H    1 
ATOM   5114  H HA   . SER A 1 335 ? 18.288  -37.411 97.762  1.00 90.11  ?  344 SER A HA   1 
ATOM   5115  H HB2  . SER A 1 335 ? 17.487  -39.702 96.352  1.00 111.97 ?  344 SER A HB2  1 
ATOM   5116  H HB3  . SER A 1 335 ? 17.367  -39.611 97.937  1.00 111.97 ?  344 SER A HB3  1 
ATOM   5117  H HG   . SER A 1 335 ? 16.164  -37.961 96.266  1.00 135.08 ?  344 SER A HG   1 
ATOM   5118  N N    . TYR A 1 336 ? 20.577  -39.357 96.724  1.00 45.96  ?  345 TYR A N    1 
ATOM   5119  C CA   . TYR A 1 336 ? 21.810  -39.999 97.148  1.00 42.46  ?  345 TYR A CA   1 
ATOM   5120  C C    . TYR A 1 336 ? 22.804  -38.986 97.674  1.00 82.87  ?  345 TYR A C    1 
ATOM   5121  O O    . TYR A 1 336 ? 23.455  -39.223 98.710  1.00 40.34  ?  345 TYR A O    1 
ATOM   5122  C CB   . TYR A 1 336 ? 22.356  -40.813 95.996  1.00 39.81  ?  345 TYR A CB   1 
ATOM   5123  C CG   . TYR A 1 336 ? 23.446  -41.753 96.476  1.00 69.63  ?  345 TYR A CG   1 
ATOM   5124  C CD1  . TYR A 1 336 ? 23.148  -42.888 97.247  1.00 59.51  ?  345 TYR A CD1  1 
ATOM   5125  C CD2  . TYR A 1 336 ? 24.798  -41.499 96.163  1.00 59.69  ?  345 TYR A CD2  1 
ATOM   5126  C CE1  . TYR A 1 336 ? 24.141  -43.689 97.707  1.00 81.53  ?  345 TYR A CE1  1 
ATOM   5127  C CE2  . TYR A 1 336 ? 25.780  -42.309 96.636  1.00 77.05  ?  345 TYR A CE2  1 
ATOM   5128  C CZ   . TYR A 1 336 ? 25.452  -43.396 97.388  1.00 93.25  ?  345 TYR A CZ   1 
ATOM   5129  O OH   . TYR A 1 336 ? 26.468  -44.187 97.806  1.00 71.23  ?  345 TYR A OH   1 
ATOM   5130  H H    . TYR A 1 336 ? 20.407  -39.409 95.883  1.00 55.16  ?  345 TYR A H    1 
ATOM   5131  H HA   . TYR A 1 336 ? 21.608  -40.613 97.871  1.00 50.95  ?  345 TYR A HA   1 
ATOM   5132  H HB2  . TYR A 1 336 ? 21.642  -41.344 95.609  1.00 47.77  ?  345 TYR A HB2  1 
ATOM   5133  H HB3  . TYR A 1 336 ? 22.735  -40.218 95.331  1.00 47.77  ?  345 TYR A HB3  1 
ATOM   5134  H HD1  . TYR A 1 336 ? 22.265  -43.072 97.474  1.00 71.41  ?  345 TYR A HD1  1 
ATOM   5135  H HD2  . TYR A 1 336 ? 25.021  -40.746 95.664  1.00 71.63  ?  345 TYR A HD2  1 
ATOM   5136  H HE1  . TYR A 1 336 ? 23.940  -44.439 98.218  1.00 97.84  ?  345 TYR A HE1  1 
ATOM   5137  H HE2  . TYR A 1 336 ? 26.670  -42.138 96.426  1.00 92.46  ?  345 TYR A HE2  1 
ATOM   5138  H HH   . TYR A 1 336 ? 26.166  -44.829 98.256  1.00 85.48  ?  345 TYR A HH   1 
ATOM   5139  N N    . HIS A 1 337 ? 22.863  -37.824 97.018  1.00 57.77  ?  346 HIS A N    1 
ATOM   5140  C CA   . HIS A 1 337 ? 23.676  -36.704 97.508  1.00 60.07  ?  346 HIS A CA   1 
ATOM   5141  C C    . HIS A 1 337 ? 23.242  -36.291 98.906  1.00 53.38  ?  346 HIS A C    1 
ATOM   5142  O O    . HIS A 1 337 ? 24.062  -36.027 99.785  1.00 58.84  ?  346 HIS A O    1 
ATOM   5143  C CB   . HIS A 1 337 ? 23.564  -35.536 96.568  1.00 71.53  ?  346 HIS A CB   1 
ATOM   5144  C CG   . HIS A 1 337 ? 24.727  -34.572 96.625  1.00 82.10  ?  346 HIS A CG   1 
ATOM   5145  N ND1  . HIS A 1 337 ? 24.933  -33.572 95.684  1.00 70.93  ?  346 HIS A ND1  1 
ATOM   5146  C CD2  . HIS A 1 337 ? 25.776  -34.485 97.481  1.00 71.88  ?  346 HIS A CD2  1 
ATOM   5147  C CE1  . HIS A 1 337 ? 26.048  -32.915 95.962  1.00 64.04  ?  346 HIS A CE1  1 
ATOM   5148  N NE2  . HIS A 1 337 ? 26.566  -33.437 97.058  1.00 56.84  ?  346 HIS A NE2  1 
ATOM   5149  H H    . HIS A 1 337 ? 22.443  -37.658 96.286  1.00 69.32  ?  346 HIS A H    1 
ATOM   5150  H HA   . HIS A 1 337 ? 24.607  -36.976 97.546  1.00 72.08  ?  346 HIS A HA   1 
ATOM   5151  H HB2  . HIS A 1 337 ? 23.506  -35.872 95.660  1.00 85.84  ?  346 HIS A HB2  1 
ATOM   5152  H HB3  . HIS A 1 337 ? 22.760  -35.039 96.784  1.00 85.84  ?  346 HIS A HB3  1 
ATOM   5153  H HD2  . HIS A 1 337 ? 25.925  -35.022 98.226  1.00 86.26  ?  346 HIS A HD2  1 
ATOM   5154  H HE1  . HIS A 1 337 ? 26.389  -32.192 95.487  1.00 76.84  ?  346 HIS A HE1  1 
ATOM   5155  H HE2  . HIS A 1 337 ? 27.292  -33.176 97.439  1.00 68.21  ?  346 HIS A HE2  1 
ATOM   5156  N N    . LEU A 1 338 ? 21.951  -36.182 99.134  1.00 71.32  ?  347 LEU A N    1 
ATOM   5157  C CA   . LEU A 1 338 ? 21.547  -35.887 100.490 1.00 82.15  ?  347 LEU A CA   1 
ATOM   5158  C C    . LEU A 1 338 ? 22.099  -36.933 101.445 1.00 68.39  ?  347 LEU A C    1 
ATOM   5159  O O    . LEU A 1 338 ? 22.546  -36.593 102.552 1.00 47.37  ?  347 LEU A O    1 
ATOM   5160  C CB   . LEU A 1 338 ? 20.025  -35.798 100.600 1.00 92.17  ?  347 LEU A CB   1 
ATOM   5161  C CG   . LEU A 1 338 ? 19.428  -34.453 100.176 1.00 79.19  ?  347 LEU A CG   1 
ATOM   5162  C CD1  . LEU A 1 338 ? 17.949  -34.574 99.822  1.00 79.74  ?  347 LEU A CD1  1 
ATOM   5163  C CD2  . LEU A 1 338 ? 19.601  -33.413 101.309 1.00 70.99  ?  347 LEU A CD2  1 
ATOM   5164  H H    . LEU A 1 338 ? 21.319  -36.269 98.558  1.00 85.58  ?  347 LEU A H    1 
ATOM   5165  H HA   . LEU A 1 338 ? 21.915  -35.027 100.747 1.00 98.58  ?  347 LEU A HA   1 
ATOM   5166  H HB2  . LEU A 1 338 ? 19.634  -36.483 100.035 1.00 110.61 ?  347 LEU A HB2  1 
ATOM   5167  H HB3  . LEU A 1 338 ? 19.771  -35.953 101.523 1.00 110.61 ?  347 LEU A HB3  1 
ATOM   5168  H HG   . LEU A 1 338 ? 19.900  -34.128 99.393  1.00 95.02  ?  347 LEU A HG   1 
ATOM   5169  H HD11 . LEU A 1 338 ? 17.615  -33.701 99.561  1.00 95.68  ?  347 LEU A HD11 1 
ATOM   5170  H HD12 . LEU A 1 338 ? 17.850  -35.200 99.088  1.00 95.68  ?  347 LEU A HD12 1 
ATOM   5171  H HD13 . LEU A 1 338 ? 17.464  -34.895 100.599 1.00 95.68  ?  347 LEU A HD13 1 
ATOM   5172  H HD21 . LEU A 1 338 ? 19.219  -32.569 101.023 1.00 85.19  ?  347 LEU A HD21 1 
ATOM   5173  H HD22 . LEU A 1 338 ? 19.144  -33.732 102.102 1.00 85.19  ?  347 LEU A HD22 1 
ATOM   5174  H HD23 . LEU A 1 338 ? 20.547  -33.302 101.493 1.00 85.19  ?  347 LEU A HD23 1 
ATOM   5175  N N    . GLN A 1 339 ? 22.127  -38.201 101.029 1.00 100.43 ?  348 GLN A N    1 
ATOM   5176  C CA   . GLN A 1 339 ? 22.655  -39.217 101.933 1.00 82.82  ?  348 GLN A CA   1 
ATOM   5177  C C    . GLN A 1 339 ? 24.141  -38.993 102.150 1.00 79.56  ?  348 GLN A C    1 
ATOM   5178  O O    . GLN A 1 339 ? 24.645  -39.086 103.280 1.00 62.94  ?  348 GLN A O    1 
ATOM   5179  C CB   . GLN A 1 339 ? 22.398  -40.613 101.393 1.00 94.33  ?  348 GLN A CB   1 
ATOM   5180  C CG   . GLN A 1 339 ? 20.966  -41.057 101.450 1.00 105.74 ?  348 GLN A CG   1 
ATOM   5181  C CD   . GLN A 1 339 ? 20.758  -42.349 100.677 1.00 116.35 ?  348 GLN A CD   1 
ATOM   5182  O OE1  . GLN A 1 339 ? 21.479  -43.319 100.888 1.00 111.58 ?  348 GLN A OE1  1 
ATOM   5183  N NE2  . GLN A 1 339 ? 19.819  -42.340 99.720  1.00 121.05 ?  348 GLN A NE2  1 
ATOM   5184  H H    . GLN A 1 339 ? 21.859  -38.487 100.263 1.00 120.51 ?  348 GLN A H    1 
ATOM   5185  H HA   . GLN A 1 339 ? 22.211  -39.139 102.792 1.00 99.39  ?  348 GLN A HA   1 
ATOM   5186  H HB2  . GLN A 1 339 ? 22.676  -40.642 100.464 1.00 113.20 ?  348 GLN A HB2  1 
ATOM   5187  H HB3  . GLN A 1 339 ? 22.921  -41.246 101.909 1.00 113.20 ?  348 GLN A HB3  1 
ATOM   5188  H HG2  . GLN A 1 339 ? 20.714  -41.211 102.374 1.00 126.89 ?  348 GLN A HG2  1 
ATOM   5189  H HG3  . GLN A 1 339 ? 20.402  -40.373 101.057 1.00 126.89 ?  348 GLN A HG3  1 
ATOM   5190  H HE21 . GLN A 1 339 ? 19.367  -41.625 99.567  1.00 145.25 ?  348 GLN A HE21 1 
ATOM   5191  H HE22 . GLN A 1 339 ? 19.669  -43.050 99.258  1.00 145.25 ?  348 GLN A HE22 1 
ATOM   5192  N N    . ILE A 1 340 ? 24.849  -38.634 101.089 1.00 75.63  ?  349 ILE A N    1 
ATOM   5193  C CA   . ILE A 1 340 ? 26.284  -38.399 101.228 1.00 70.32  ?  349 ILE A CA   1 
ATOM   5194  C C    . ILE A 1 340 ? 26.548  -37.250 102.186 1.00 61.89  ?  349 ILE A C    1 
ATOM   5195  O O    . ILE A 1 340 ? 27.348  -37.375 103.117 1.00 68.96  ?  349 ILE A O    1 
ATOM   5196  C CB   . ILE A 1 340 ? 26.911  -38.136 99.854  1.00 78.64  ?  349 ILE A CB   1 
ATOM   5197  C CG1  . ILE A 1 340 ? 26.802  -39.392 98.979  1.00 56.25  ?  349 ILE A CG1  1 
ATOM   5198  C CG2  . ILE A 1 340 ? 28.386  -37.772 100.049 1.00 85.81  ?  349 ILE A CG2  1 
ATOM   5199  C CD1  . ILE A 1 340 ? 27.226  -40.672 99.758  1.00 57.15  ?  349 ILE A CD1  1 
ATOM   5200  H H    . ILE A 1 340 ? 24.536  -38.520 100.296 1.00 90.76  ?  349 ILE A H    1 
ATOM   5201  H HA   . ILE A 1 340 ? 26.697  -39.195 101.597 1.00 84.38  ?  349 ILE A HA   1 
ATOM   5202  H HB   . ILE A 1 340 ? 26.450  -37.399 99.423  1.00 94.37  ?  349 ILE A HB   1 
ATOM   5203  H HG12 . ILE A 1 340 ? 25.883  -39.503 98.691  1.00 67.50  ?  349 ILE A HG12 1 
ATOM   5204  H HG13 . ILE A 1 340 ? 27.386  -39.298 98.210  1.00 67.50  ?  349 ILE A HG13 1 
ATOM   5205  H HG21 . ILE A 1 340 ? 28.787  -37.604 99.182  1.00 102.97 ?  349 ILE A HG21 1 
ATOM   5206  H HG22 . ILE A 1 340 ? 28.444  -36.976 100.600 1.00 102.97 ?  349 ILE A HG22 1 
ATOM   5207  H HG23 . ILE A 1 340 ? 28.838  -38.511 100.486 1.00 102.97 ?  349 ILE A HG23 1 
ATOM   5208  H HD11 . ILE A 1 340 ? 27.143  -41.440 99.172  1.00 68.58  ?  349 ILE A HD11 1 
ATOM   5209  H HD12 . ILE A 1 340 ? 28.147  -40.575 100.048 1.00 68.58  ?  349 ILE A HD12 1 
ATOM   5210  H HD13 . ILE A 1 340 ? 26.646  -40.779 100.528 1.00 68.58  ?  349 ILE A HD13 1 
ATOM   5211  N N    . VAL A 1 341 ? 25.849  -36.135 102.011 1.00 63.57  ?  350 VAL A N    1 
ATOM   5212  C CA   . VAL A 1 341 ? 26.107  -35.011 102.910 1.00 54.52  ?  350 VAL A CA   1 
ATOM   5213  C C    . VAL A 1 341 ? 25.794  -35.368 104.354 1.00 74.40  ?  350 VAL A C    1 
ATOM   5214  O O    . VAL A 1 341 ? 26.375  -34.812 105.295 1.00 95.45  ?  350 VAL A O    1 
ATOM   5215  C CB   . VAL A 1 341 ? 25.300  -33.773 102.493 1.00 82.61  ?  350 VAL A CB   1 
ATOM   5216  C CG1  . VAL A 1 341 ? 25.351  -32.727 103.582 1.00 70.60  ?  350 VAL A CG1  1 
ATOM   5217  C CG2  . VAL A 1 341 ? 25.829  -33.205 101.219 1.00 97.73  ?  350 VAL A CG2  1 
ATOM   5218  H H    . VAL A 1 341 ? 25.248  -36.003 101.411 1.00 76.28  ?  350 VAL A H    1 
ATOM   5219  H HA   . VAL A 1 341 ? 27.048  -34.781 102.860 1.00 65.43  ?  350 VAL A HA   1 
ATOM   5220  H HB   . VAL A 1 341 ? 24.373  -34.025 102.354 1.00 99.13  ?  350 VAL A HB   1 
ATOM   5221  H HG11 . VAL A 1 341 ? 24.837  -31.954 103.301 1.00 84.72  ?  350 VAL A HG11 1 
ATOM   5222  H HG12 . VAL A 1 341 ? 24.974  -33.099 104.394 1.00 84.72  ?  350 VAL A HG12 1 
ATOM   5223  H HG13 . VAL A 1 341 ? 26.275  -32.474 103.732 1.00 84.72  ?  350 VAL A HG13 1 
ATOM   5224  H HG21 . VAL A 1 341 ? 25.302  -32.426 100.979 1.00 117.27 ?  350 VAL A HG21 1 
ATOM   5225  H HG22 . VAL A 1 341 ? 26.756  -32.951 101.348 1.00 117.27 ?  350 VAL A HG22 1 
ATOM   5226  H HG23 . VAL A 1 341 ? 25.763  -33.877 100.523 1.00 117.27 ?  350 VAL A HG23 1 
ATOM   5227  N N    . THR A 1 342 ? 24.887  -36.290 104.570 1.00 76.28  ?  351 THR A N    1 
ATOM   5228  C CA   . THR A 1 342 ? 24.664  -36.695 105.940 1.00 97.73  ?  351 THR A CA   1 
ATOM   5229  C C    . THR A 1 342 ? 25.863  -37.440 106.471 1.00 93.57  ?  351 THR A C    1 
ATOM   5230  O O    . THR A 1 342 ? 26.399  -37.093 107.531 1.00 92.32  ?  351 THR A O    1 
ATOM   5231  C CB   . THR A 1 342 ? 23.432  -37.551 105.997 1.00 102.03 ?  351 THR A CB   1 
ATOM   5232  O OG1  . THR A 1 342 ? 22.377  -36.757 105.445 1.00 86.65  ?  351 THR A OG1  1 
ATOM   5233  C CG2  . THR A 1 342 ? 23.168  -38.003 107.432 1.00 100.51 ?  351 THR A CG2  1 
ATOM   5234  H H    . THR A 1 342 ? 24.406  -36.683 103.975 1.00 91.54  ?  351 THR A H    1 
ATOM   5235  H HA   . THR A 1 342 ? 24.520  -35.910 106.491 1.00 117.28 ?  351 THR A HA   1 
ATOM   5236  H HB   . THR A 1 342 ? 23.563  -38.339 105.447 1.00 122.44 ?  351 THR A HB   1 
ATOM   5237  H HG1  . THR A 1 342 ? 22.560  -36.546 104.653 1.00 103.98 ?  351 THR A HG1  1 
ATOM   5238  H HG21 . THR A 1 342 ? 22.372  -38.556 107.464 1.00 120.61 ?  351 THR A HG21 1 
ATOM   5239  H HG22 . THR A 1 342 ? 23.922  -38.517 107.761 1.00 120.61 ?  351 THR A HG22 1 
ATOM   5240  H HG23 . THR A 1 342 ? 23.040  -37.231 108.004 1.00 120.61 ?  351 THR A HG23 1 
ATOM   5241  N N    . LYS A 1 343 ? 26.334  -38.433 105.707 1.00 91.79  ?  352 LYS A N    1 
ATOM   5242  C CA   . LYS A 1 343 ? 27.414  -39.266 106.184 1.00 59.29  ?  352 LYS A CA   1 
ATOM   5243  C C    . LYS A 1 343 ? 28.686  -38.441 106.324 1.00 61.34  ?  352 LYS A C    1 
ATOM   5244  O O    . LYS A 1 343 ? 29.427  -38.576 107.316 1.00 73.88  ?  352 LYS A O    1 
ATOM   5245  C CB   . LYS A 1 343 ? 27.616  -40.453 105.231 1.00 55.27  ?  352 LYS A CB   1 
ATOM   5246  C CG   . LYS A 1 343 ? 28.612  -41.586 105.747 1.00 64.81  ?  352 LYS A CG   1 
ATOM   5247  C CD   . LYS A 1 343 ? 29.149  -42.466 104.634 1.00 97.35  ?  352 LYS A CD   1 
ATOM   5248  C CE   . LYS A 1 343 ? 30.201  -43.412 105.168 1.00 114.77 ?  352 LYS A CE   1 
ATOM   5249  N NZ   . LYS A 1 343 ? 30.730  -44.307 104.142 1.00 75.89  1  352 LYS A NZ   1 
ATOM   5250  H H    . LYS A 1 343 ? 26.044  -38.633 104.922 1.00 110.14 ?  352 LYS A H    1 
ATOM   5251  H HA   . LYS A 1 343 ? 27.184  -39.616 107.059 1.00 71.14  ?  352 LYS A HA   1 
ATOM   5252  H HB2  . LYS A 1 343 ? 26.754  -40.872 105.076 1.00 66.32  ?  352 LYS A HB2  1 
ATOM   5253  H HB3  . LYS A 1 343 ? 27.968  -40.117 104.392 1.00 66.32  ?  352 LYS A HB3  1 
ATOM   5254  H HG2  . LYS A 1 343 ? 29.367  -41.165 106.185 1.00 77.78  ?  352 LYS A HG2  1 
ATOM   5255  H HG3  . LYS A 1 343 ? 28.141  -42.155 106.376 1.00 77.78  ?  352 LYS A HG3  1 
ATOM   5256  H HD2  . LYS A 1 343 ? 28.424  -42.991 104.260 1.00 116.82 ?  352 LYS A HD2  1 
ATOM   5257  H HD3  . LYS A 1 343 ? 29.553  -41.910 103.950 1.00 116.82 ?  352 LYS A HD3  1 
ATOM   5258  H HE2  . LYS A 1 343 ? 30.940  -42.895 105.523 1.00 137.73 ?  352 LYS A HE2  1 
ATOM   5259  H HE3  . LYS A 1 343 ? 29.810  -43.957 105.868 1.00 137.73 ?  352 LYS A HE3  1 
ATOM   5260  H HZ1  . LYS A 1 343 ? 31.344  -44.846 104.496 1.00 91.06  ?  352 LYS A HZ1  1 
ATOM   5261  H HZ2  . LYS A 1 343 ? 30.072  -44.802 103.803 1.00 91.06  ?  352 LYS A HZ2  1 
ATOM   5262  H HZ3  . LYS A 1 343 ? 31.103  -43.833 103.488 1.00 91.06  ?  352 LYS A HZ3  1 
ATOM   5263  N N    . TYR A 1 344 ? 28.913  -37.525 105.393 1.00 64.43  ?  353 TYR A N    1 
ATOM   5264  C CA   . TYR A 1 344 ? 30.217  -36.866 105.298 1.00 83.28  ?  353 TYR A CA   1 
ATOM   5265  C C    . TYR A 1 344 ? 30.268  -35.472 105.929 1.00 79.73  ?  353 TYR A C    1 
ATOM   5266  O O    . TYR A 1 344 ? 31.348  -34.882 105.965 1.00 81.79  ?  353 TYR A O    1 
ATOM   5267  C CB   . TYR A 1 344 ? 30.699  -36.795 103.817 1.00 78.32  ?  353 TYR A CB   1 
ATOM   5268  C CG   . TYR A 1 344 ? 31.197  -38.135 103.267 1.00 64.68  ?  353 TYR A CG   1 
ATOM   5269  C CD1  . TYR A 1 344 ? 32.483  -38.605 103.537 1.00 68.31  ?  353 TYR A CD1  1 
ATOM   5270  C CD2  . TYR A 1 344 ? 30.361  -38.968 102.551 1.00 74.24  ?  353 TYR A CD2  1 
ATOM   5271  C CE1  . TYR A 1 344 ? 32.909  -39.865 103.055 1.00 104.59 ?  353 TYR A CE1  1 
ATOM   5272  C CE2  . TYR A 1 344 ? 30.795  -40.240 102.083 1.00 64.37  ?  353 TYR A CE2  1 
ATOM   5273  C CZ   . TYR A 1 344 ? 32.051  -40.656 102.334 1.00 76.06  ?  353 TYR A CZ   1 
ATOM   5274  O OH   . TYR A 1 344 ? 32.451  -41.873 101.859 1.00 102.09 ?  353 TYR A OH   1 
ATOM   5275  H H    . TYR A 1 344 ? 28.339  -37.267 104.807 1.00 77.31  ?  353 TYR A H    1 
ATOM   5276  H HA   . TYR A 1 344 ? 30.860  -37.413 105.776 1.00 99.93  ?  353 TYR A HA   1 
ATOM   5277  H HB2  . TYR A 1 344 ? 29.960  -36.502 103.261 1.00 93.98  ?  353 TYR A HB2  1 
ATOM   5278  H HB3  . TYR A 1 344 ? 31.429  -36.159 103.755 1.00 93.98  ?  353 TYR A HB3  1 
ATOM   5279  H HD1  . TYR A 1 344 ? 33.072  -38.077 104.026 1.00 81.97  ?  353 TYR A HD1  1 
ATOM   5280  H HD2  . TYR A 1 344 ? 29.491  -38.693 102.373 1.00 89.09  ?  353 TYR A HD2  1 
ATOM   5281  H HE1  . TYR A 1 344 ? 33.775  -40.159 103.229 1.00 125.51 ?  353 TYR A HE1  1 
ATOM   5282  H HE2  . TYR A 1 344 ? 30.219  -40.775 101.587 1.00 77.24  ?  353 TYR A HE2  1 
ATOM   5283  H HH   . TYR A 1 344 ? 33.248  -42.019 102.078 1.00 122.51 ?  353 TYR A HH   1 
ATOM   5284  N N    . ILE A 1 345 ? 29.169  -34.906 106.409 1.00 114.22 ?  354 ILE A N    1 
ATOM   5285  C CA   . ILE A 1 345 ? 29.341  -33.623 107.077 1.00 76.86  ?  354 ILE A CA   1 
ATOM   5286  C C    . ILE A 1 345 ? 28.567  -33.505 108.366 1.00 91.42  ?  354 ILE A C    1 
ATOM   5287  O O    . ILE A 1 345 ? 29.130  -33.129 109.404 1.00 96.81  ?  354 ILE A O    1 
ATOM   5288  C CB   . ILE A 1 345 ? 28.947  -32.477 106.158 1.00 76.55  ?  354 ILE A CB   1 
ATOM   5289  C CG1  . ILE A 1 345 ? 29.866  -32.510 104.977 1.00 54.56  ?  354 ILE A CG1  1 
ATOM   5290  C CG2  . ILE A 1 345 ? 29.102  -31.136 106.885 1.00 94.16  ?  354 ILE A CG2  1 
ATOM   5291  C CD1  . ILE A 1 345 ? 29.555  -31.475 103.900 1.00 53.20  ?  354 ILE A CD1  1 
ATOM   5292  H H    . ILE A 1 345 ? 28.367  -35.215 106.368 1.00 137.07 ?  354 ILE A H    1 
ATOM   5293  H HA   . ILE A 1 345 ? 30.281  -33.514 107.292 1.00 92.23  ?  354 ILE A HA   1 
ATOM   5294  H HB   . ILE A 1 345 ? 28.029  -32.589 105.865 1.00 91.86  ?  354 ILE A HB   1 
ATOM   5295  H HG12 . ILE A 1 345 ? 30.772  -32.350 105.285 1.00 65.48  ?  354 ILE A HG12 1 
ATOM   5296  H HG13 . ILE A 1 345 ? 29.811  -33.387 104.566 1.00 65.48  ?  354 ILE A HG13 1 
ATOM   5297  H HG21 . ILE A 1 345 ? 28.846  -30.420 106.283 1.00 113.00 ?  354 ILE A HG21 1 
ATOM   5298  H HG22 . ILE A 1 345 ? 28.528  -31.132 107.667 1.00 113.00 ?  354 ILE A HG22 1 
ATOM   5299  H HG23 . ILE A 1 345 ? 30.028  -31.028 107.153 1.00 113.00 ?  354 ILE A HG23 1 
ATOM   5300  H HD11 . ILE A 1 345 ? 30.196  -31.568 103.178 1.00 63.84  ?  354 ILE A HD11 1 
ATOM   5301  H HD12 . ILE A 1 345 ? 28.656  -31.626 103.567 1.00 63.84  ?  354 ILE A HD12 1 
ATOM   5302  H HD13 . ILE A 1 345 ? 29.619  -30.588 104.287 1.00 63.84  ?  354 ILE A HD13 1 
ATOM   5303  N N    . LEU A 1 346 ? 27.256  -33.711 108.277 1.00 69.77  ?  355 LEU A N    1 
ATOM   5304  C CA   . LEU A 1 346 ? 26.410  -33.319 109.393 1.00 91.64  ?  355 LEU A CA   1 
ATOM   5305  C C    . LEU A 1 346 ? 26.710  -34.146 110.640 1.00 100.14 ?  355 LEU A C    1 
ATOM   5306  O O    . LEU A 1 346 ? 26.642  -33.620 111.760 1.00 97.74  ?  355 LEU A O    1 
ATOM   5307  C CB   . LEU A 1 346 ? 24.941  -33.406 108.990 1.00 108.50 ?  355 LEU A CB   1 
ATOM   5308  C CG   . LEU A 1 346 ? 24.464  -32.375 107.972 1.00 155.75 ?  355 LEU A CG   1 
ATOM   5309  H H    . LEU A 1 346 ? 26.847  -34.063 107.608 1.00 83.72  ?  355 LEU A H    1 
ATOM   5310  H HA   . LEU A 1 346 ? 26.598  -32.392 109.609 1.00 109.96 ?  355 LEU A HA   1 
ATOM   5311  H HB2  . LEU A 1 346 ? 24.781  -34.284 108.609 1.00 130.20 ?  355 LEU A HB2  1 
ATOM   5312  H HB3  . LEU A 1 346 ? 24.399  -33.298 109.787 1.00 130.20 ?  355 LEU A HB3  1 
ATOM   5313  H HG   . LEU A 1 346 ? 25.079  -32.364 107.222 1.00 186.90 ?  355 LEU A HG   1 
ATOM   5314  N N    . ILE A 1 347 ? 27.056  -35.418 110.473 1.00 108.32 ?  356 ILE A N    1 
ATOM   5315  C CA   . ILE A 1 347 ? 27.339  -36.301 111.597 1.00 123.61 ?  356 ILE A CA   1 
ATOM   5316  C C    . ILE A 1 347 ? 28.675  -35.897 112.216 1.00 151.17 ?  356 ILE A C    1 
ATOM   5317  O O    . ILE A 1 347 ? 28.733  -35.604 113.420 1.00 203.16 ?  356 ILE A O    1 
ATOM   5318  C CB   . ILE A 1 347 ? 27.322  -37.766 111.135 1.00 213.69 ?  356 ILE A CB   1 
ATOM   5319  C CG1  . ILE A 1 347 ? 25.887  -38.217 110.923 1.00 153.91 ?  356 ILE A CG1  1 
ATOM   5320  C CG2  . ILE A 1 347 ? 28.006  -38.656 112.138 1.00 127.95 ?  356 ILE A CG2  1 
ATOM   5321  C CD1  . ILE A 1 347 ? 25.762  -39.535 110.174 1.00 121.97 ?  356 ILE A CD1  1 
ATOM   5322  H H    . ILE A 1 347 ? 27.134  -35.799 109.706 1.00 129.98 ?  356 ILE A H    1 
ATOM   5323  H HA   . ILE A 1 347 ? 26.649  -36.189 112.270 1.00 148.33 ?  356 ILE A HA   1 
ATOM   5324  H HB   . ILE A 1 347 ? 27.795  -37.830 110.290 1.00 256.43 ?  356 ILE A HB   1 
ATOM   5325  H HG12 . ILE A 1 347 ? 25.463  -38.326 111.788 1.00 184.70 ?  356 ILE A HG12 1 
ATOM   5326  H HG13 . ILE A 1 347 ? 25.419  -37.539 110.410 1.00 184.70 ?  356 ILE A HG13 1 
ATOM   5327  H HG21 . ILE A 1 347 ? 27.979  -39.572 111.818 1.00 153.54 ?  356 ILE A HG21 1 
ATOM   5328  H HG22 . ILE A 1 347 ? 28.927  -38.368 112.240 1.00 153.54 ?  356 ILE A HG22 1 
ATOM   5329  H HG23 . ILE A 1 347 ? 27.542  -38.589 112.988 1.00 153.54 ?  356 ILE A HG23 1 
ATOM   5330  H HD11 . ILE A 1 347 ? 24.822  -39.755 110.078 1.00 146.36 ?  356 ILE A HD11 1 
ATOM   5331  H HD12 . ILE A 1 347 ? 26.171  -39.441 109.300 1.00 146.36 ?  356 ILE A HD12 1 
ATOM   5332  H HD13 . ILE A 1 347 ? 26.215  -40.228 110.679 1.00 146.36 ?  356 ILE A HD13 1 
ATOM   5333  N N    . PRO A 1 348 ? 29.764  -35.869 111.446 1.00 120.25 ?  357 PRO A N    1 
ATOM   5334  C CA   . PRO A 1 348 ? 31.037  -35.368 111.987 1.00 186.75 ?  357 PRO A CA   1 
ATOM   5335  C C    . PRO A 1 348 ? 30.924  -34.028 112.656 1.00 126.33 ?  357 PRO A C    1 
ATOM   5336  O O    . PRO A 1 348 ? 31.496  -33.809 113.726 1.00 115.48 ?  357 PRO A O    1 
ATOM   5337  C CB   . PRO A 1 348 ? 31.902  -35.227 110.739 1.00 98.33  ?  357 PRO A CB   1 
ATOM   5338  C CG   . PRO A 1 348 ? 31.368  -36.212 109.811 1.00 115.56 ?  357 PRO A CG   1 
ATOM   5339  C CD   . PRO A 1 348 ? 29.920  -36.373 110.075 1.00 122.63 ?  357 PRO A CD   1 
ATOM   5340  H HA   . PRO A 1 348 ? 31.434  -36.011 112.594 1.00 224.10 ?  357 PRO A HA   1 
ATOM   5341  H HB2  . PRO A 1 348 ? 31.815  -34.331 110.378 1.00 118.00 ?  357 PRO A HB2  1 
ATOM   5342  H HB3  . PRO A 1 348 ? 32.827  -35.424 110.956 1.00 118.00 ?  357 PRO A HB3  1 
ATOM   5343  H HG2  . PRO A 1 348 ? 31.507  -35.901 108.903 1.00 138.67 ?  357 PRO A HG2  1 
ATOM   5344  H HG3  . PRO A 1 348 ? 31.826  -37.056 109.947 1.00 138.67 ?  357 PRO A HG3  1 
ATOM   5345  H HD2  . PRO A 1 348 ? 29.402  -35.835 109.456 1.00 147.16 ?  357 PRO A HD2  1 
ATOM   5346  H HD3  . PRO A 1 348 ? 29.670  -37.309 110.028 1.00 147.16 ?  357 PRO A HD3  1 
ATOM   5347  N N    . ALA A 1 349 ? 30.190  -33.113 112.026 1.00 73.60  ?  358 ALA A N    1 
ATOM   5348  C CA   . ALA A 1 349 ? 30.038  -31.756 112.537 1.00 94.68  ?  358 ALA A CA   1 
ATOM   5349  C C    . ALA A 1 349 ? 29.357  -31.760 113.905 1.00 113.60 ?  358 ALA A C    1 
ATOM   5350  O O    . ALA A 1 349 ? 29.575  -30.857 114.723 1.00 149.18 ?  358 ALA A O    1 
ATOM   5351  C CB   . ALA A 1 349 ? 29.253  -30.925 111.505 1.00 75.23  ?  358 ALA A CB   1 
ATOM   5352  H H    . ALA A 1 349 ? 29.766  -33.257 111.291 1.00 88.32  ?  358 ALA A H    1 
ATOM   5353  H HA   . ALA A 1 349 ? 30.916  -31.356 112.640 1.00 113.62 ?  358 ALA A HA   1 
ATOM   5354  H HB1  . ALA A 1 349 ? 29.149  -30.021 111.841 1.00 90.27  ?  358 ALA A HB1  1 
ATOM   5355  H HB2  . ALA A 1 349 ? 29.745  -30.914 110.669 1.00 90.27  ?  358 ALA A HB2  1 
ATOM   5356  H HB3  . ALA A 1 349 ? 28.382  -31.331 111.370 1.00 90.27  ?  358 ALA A HB3  1 
ATOM   5357  N N    . SER A 1 350 ? 28.542  -32.776 114.165 1.00 91.62  ?  359 SER A N    1 
ATOM   5358  C CA   . SER A 1 350 ? 27.915  -33.005 115.452 1.00 101.97 ?  359 SER A CA   1 
ATOM   5359  C C    . SER A 1 350 ? 28.868  -33.618 116.463 1.00 96.74  ?  359 SER A C    1 
ATOM   5360  O O    . SER A 1 350 ? 28.439  -33.877 117.580 1.00 100.45 ?  359 SER A O    1 
ATOM   5361  C CB   . SER A 1 350 ? 26.712  -33.914 115.277 1.00 135.36 ?  359 SER A CB   1 
ATOM   5362  O OG   . SER A 1 350 ? 27.140  -35.243 115.099 1.00 164.50 ?  359 SER A OG   1 
ATOM   5363  H H    . SER A 1 350 ? 28.331  -33.371 113.581 1.00 109.95 ?  359 SER A H    1 
ATOM   5364  H HA   . SER A 1 350 ? 27.603  -32.158 115.807 1.00 122.37 ?  359 SER A HA   1 
ATOM   5365  H HB2  . SER A 1 350 ? 26.155  -33.861 116.069 1.00 162.43 ?  359 SER A HB2  1 
ATOM   5366  H HB3  . SER A 1 350 ? 26.211  -33.633 114.495 1.00 162.43 ?  359 SER A HB3  1 
ATOM   5367  H HG   . SER A 1 350 ? 27.627  -35.299 114.417 1.00 197.40 ?  359 SER A HG   1 
ATOM   5368  N N    . GLN A 1 351 ? 30.096  -33.973 116.069 1.00 175.24 ?  360 GLN A N    1 
ATOM   5369  C CA   . GLN A 1 351 ? 31.074  -34.534 116.992 1.00 235.13 ?  360 GLN A CA   1 
ATOM   5370  C C    . GLN A 1 351 ? 32.225  -33.591 117.341 1.00 200.39 ?  360 GLN A C    1 
ATOM   5371  O O    . GLN A 1 351 ? 33.012  -33.910 118.239 1.00 119.66 ?  360 GLN A O    1 
ATOM   5372  C CB   . GLN A 1 351 ? 31.648  -35.814 116.388 1.00 168.73 ?  360 GLN A CB   1 
ATOM   5373  C CG   . GLN A 1 351 ? 30.625  -36.908 116.206 1.00 194.29 ?  360 GLN A CG   1 
ATOM   5374  C CD   . GLN A 1 351 ? 31.209  -38.102 115.503 1.00 237.03 ?  360 GLN A CD   1 
ATOM   5375  O OE1  . GLN A 1 351 ? 32.368  -38.437 115.701 1.00 145.42 ?  360 GLN A OE1  1 
ATOM   5376  N NE2  . GLN A 1 351 ? 30.418  -38.745 114.674 1.00 125.70 ?  360 GLN A NE2  1 
ATOM   5377  H H    . GLN A 1 351 ? 30.384  -33.897 115.262 1.00 210.29 ?  360 GLN A H    1 
ATOM   5378  H HA   . GLN A 1 351 ? 30.624  -34.770 117.818 1.00 282.16 ?  360 GLN A HA   1 
ATOM   5379  H HB2  . GLN A 1 351 ? 32.021  -35.609 115.516 1.00 202.47 ?  360 GLN A HB2  1 
ATOM   5380  H HB3  . GLN A 1 351 ? 32.344  -36.152 116.973 1.00 202.47 ?  360 GLN A HB3  1 
ATOM   5381  H HG2  . GLN A 1 351 ? 30.306  -37.195 117.077 1.00 233.14 ?  360 GLN A HG2  1 
ATOM   5382  H HG3  . GLN A 1 351 ? 29.888  -36.572 115.673 1.00 233.14 ?  360 GLN A HG3  1 
ATOM   5383  H HE21 . GLN A 1 351 ? 29.609  -38.477 114.556 1.00 150.84 ?  360 GLN A HE21 1 
ATOM   5384  H HE22 . GLN A 1 351 ? 30.709  -39.434 114.249 1.00 150.84 ?  360 GLN A HE22 1 
ATOM   5385  N N    . GLN A 1 352 ? 32.345  -32.443 116.668 1.00 177.18 ?  361 GLN A N    1 
ATOM   5386  C CA   . GLN A 1 352 ? 33.377  -31.460 116.983 1.00 157.97 ?  361 GLN A CA   1 
ATOM   5387  C C    . GLN A 1 352 ? 32.795  -30.451 117.973 1.00 164.18 ?  361 GLN A C    1 
ATOM   5388  O O    . GLN A 1 352 ? 31.844  -29.737 117.618 1.00 150.89 ?  361 GLN A O    1 
ATOM   5389  C CB   . GLN A 1 352 ? 33.860  -30.761 115.710 1.00 139.38 ?  361 GLN A CB   1 
ATOM   5390  H H    . GLN A 1 352 ? 31.832  -32.211 116.018 1.00 212.61 ?  361 GLN A H    1 
ATOM   5391  H HA   . GLN A 1 352 ? 34.133  -31.903 117.400 1.00 189.57 ?  361 GLN A HA   1 
ATOM   5392  N N    . PRO A 1 353 ? 33.293  -30.372 119.226 1.00 186.80 ?  362 PRO A N    1 
ATOM   5393  C CA   . PRO A 1 353 ? 32.694  -29.452 120.215 1.00 137.18 ?  362 PRO A CA   1 
ATOM   5394  C C    . PRO A 1 353 ? 33.184  -28.004 120.087 1.00 137.37 ?  362 PRO A C    1 
ATOM   5395  O O    . PRO A 1 353 ? 33.100  -27.239 121.059 1.00 160.47 ?  362 PRO A O    1 
ATOM   5396  C CB   . PRO A 1 353 ? 33.129  -30.045 121.563 1.00 133.67 ?  362 PRO A CB   1 
ATOM   5397  C CG   . PRO A 1 353 ? 34.444  -30.670 121.255 1.00 131.17 ?  362 PRO A CG   1 
ATOM   5398  C CD   . PRO A 1 353 ? 34.349  -31.207 119.823 1.00 134.99 ?  362 PRO A CD   1 
ATOM   5399  H HA   . PRO A 1 353 ? 31.726  -29.472 120.152 1.00 164.62 ?  362 PRO A HA   1 
ATOM   5400  H HB2  . PRO A 1 353 ? 33.224  -29.339 122.221 1.00 160.40 ?  362 PRO A HB2  1 
ATOM   5401  H HB3  . PRO A 1 353 ? 32.487  -30.711 121.855 1.00 160.40 ?  362 PRO A HB3  1 
ATOM   5402  H HG2  . PRO A 1 353 ? 35.142  -30.000 121.321 1.00 157.41 ?  362 PRO A HG2  1 
ATOM   5403  H HG3  . PRO A 1 353 ? 34.610  -31.394 121.878 1.00 157.41 ?  362 PRO A HG3  1 
ATOM   5404  H HD2  . PRO A 1 353 ? 35.190  -31.077 119.356 1.00 161.99 ?  362 PRO A HD2  1 
ATOM   5405  H HD3  . PRO A 1 353 ? 34.084  -32.140 119.827 1.00 161.99 ?  362 PRO A HD3  1 
ATOM   5406  N N    . GLY A 1 371 ? 27.064  -22.868 105.465 1.00 159.33 ?  380 GLY A N    1 
ATOM   5407  C CA   . GLY A 1 371 ? 27.985  -23.595 106.326 1.00 147.70 ?  380 GLY A CA   1 
ATOM   5408  C C    . GLY A 1 371 ? 27.762  -25.090 106.276 1.00 150.45 ?  380 GLY A C    1 
ATOM   5409  O O    . GLY A 1 371 ? 27.863  -25.700 105.211 1.00 133.88 ?  380 GLY A O    1 
ATOM   5410  H HA2  . GLY A 1 371 ? 28.897  -23.411 106.052 1.00 177.24 ?  380 GLY A HA2  1 
ATOM   5411  H HA3  . GLY A 1 371 ? 27.873  -23.298 107.243 1.00 177.24 ?  380 GLY A HA3  1 
ATOM   5412  N N    . GLY A 1 372 ? 27.455  -25.679 107.431 1.00 161.89 ?  381 GLY A N    1 
ATOM   5413  C CA   . GLY A 1 372 ? 27.150  -27.092 107.498 1.00 149.69 ?  381 GLY A CA   1 
ATOM   5414  C C    . GLY A 1 372 ? 25.776  -27.389 106.939 1.00 125.67 ?  381 GLY A C    1 
ATOM   5415  O O    . GLY A 1 372 ? 25.631  -28.213 106.037 1.00 175.27 ?  381 GLY A O    1 
ATOM   5416  H H    . GLY A 1 372 ? 27.419  -25.275 108.189 1.00 194.26 ?  381 GLY A H    1 
ATOM   5417  H HA2  . GLY A 1 372 ? 27.807  -27.592 106.990 1.00 179.62 ?  381 GLY A HA2  1 
ATOM   5418  H HA3  . GLY A 1 372 ? 27.180  -27.388 108.421 1.00 179.62 ?  381 GLY A HA3  1 
ATOM   5419  N N    . THR A 1 373 ? 24.760  -26.700 107.453 1.00 157.73 ?  382 THR A N    1 
ATOM   5420  C CA   . THR A 1 373 ? 23.372  -26.973 107.092 1.00 114.15 ?  382 THR A CA   1 
ATOM   5421  C C    . THR A 1 373 ? 22.850  -26.130 105.931 1.00 111.37 ?  382 THR A C    1 
ATOM   5422  O O    . THR A 1 373 ? 21.906  -26.558 105.263 1.00 183.77 ?  382 THR A O    1 
ATOM   5423  C CB   . THR A 1 373 ? 22.460  -26.769 108.301 1.00 104.75 ?  382 THR A CB   1 
ATOM   5424  O OG1  . THR A 1 373 ? 22.619  -25.436 108.794 1.00 130.22 ?  382 THR A OG1  1 
ATOM   5425  C CG2  . THR A 1 373 ? 22.808  -27.764 109.396 1.00 127.02 ?  382 THR A CG2  1 
ATOM   5426  H H    . THR A 1 373 ? 24.850  -26.061 108.022 1.00 189.27 ?  382 THR A H    1 
ATOM   5427  H HA   . THR A 1 373 ? 23.302  -27.904 106.828 1.00 136.98 ?  382 THR A HA   1 
ATOM   5428  H HB   . THR A 1 373 ? 21.537  -26.909 108.039 1.00 125.71 ?  382 THR A HB   1 
ATOM   5429  H HG1  . THR A 1 373 ? 22.122  -25.314 109.459 1.00 156.26 ?  382 THR A HG1  1 
ATOM   5430  H HG21 . THR A 1 373 ? 22.227  -27.631 110.161 1.00 152.43 ?  382 THR A HG21 1 
ATOM   5431  H HG22 . THR A 1 373 ? 22.695  -28.670 109.068 1.00 152.43 ?  382 THR A HG22 1 
ATOM   5432  H HG23 . THR A 1 373 ? 23.729  -27.642 109.674 1.00 152.43 ?  382 THR A HG23 1 
ATOM   5433  N N    . ASP A 1 374 ? 23.412  -24.947 105.668 1.00 142.36 ?  383 ASP A N    1 
ATOM   5434  C CA   . ASP A 1 374 ? 22.923  -24.173 104.533 1.00 135.44 ?  383 ASP A CA   1 
ATOM   5435  C C    . ASP A 1 374 ? 22.995  -25.002 103.277 1.00 116.47 ?  383 ASP A C    1 
ATOM   5436  O O    . ASP A 1 374 ? 22.236  -24.773 102.331 1.00 115.07 ?  383 ASP A O    1 
ATOM   5437  C CB   . ASP A 1 374 ? 23.762  -22.910 104.309 1.00 135.64 ?  383 ASP A CB   1 
ATOM   5438  C CG   . ASP A 1 374 ? 23.543  -21.870 105.365 1.00 134.20 ?  383 ASP A CG   1 
ATOM   5439  O OD1  . ASP A 1 374 ? 22.571  -21.093 105.222 1.00 132.19 ?  383 ASP A OD1  1 
ATOM   5440  O OD2  . ASP A 1 374 ? 24.352  -21.821 106.320 1.00 168.70 -1 383 ASP A OD2  1 
ATOM   5441  H H    . ASP A 1 374 ? 24.052  -24.584 106.114 1.00 170.83 ?  383 ASP A H    1 
ATOM   5442  H HA   . ASP A 1 374 ? 22.001  -23.914 104.685 1.00 162.53 ?  383 ASP A HA   1 
ATOM   5443  H HB2  . ASP A 1 374 ? 24.701  -23.150 104.315 1.00 162.77 ?  383 ASP A HB2  1 
ATOM   5444  H HB3  . ASP A 1 374 ? 23.524  -22.521 103.453 1.00 162.77 ?  383 ASP A HB3  1 
ATOM   5445  N N    . LEU A 1 375 ? 23.910  -25.963 103.270 1.00 118.41 ?  384 LEU A N    1 
ATOM   5446  C CA   . LEU A 1 375 ? 24.081  -26.873 102.151 1.00 98.40  ?  384 LEU A CA   1 
ATOM   5447  C C    . LEU A 1 375 ? 22.925  -27.858 102.037 1.00 87.79  ?  384 LEU A C    1 
ATOM   5448  O O    . LEU A 1 375 ? 22.477  -28.179 100.933 1.00 91.33  ?  384 LEU A O    1 
ATOM   5449  C CB   . LEU A 1 375 ? 25.403  -27.598 102.344 1.00 110.33 ?  384 LEU A CB   1 
ATOM   5450  C CG   . LEU A 1 375 ? 25.715  -28.711 101.361 1.00 90.88  ?  384 LEU A CG   1 
ATOM   5451  C CD1  . LEU A 1 375 ? 25.737  -28.202 99.933  1.00 90.10  ?  384 LEU A CD1  1 
ATOM   5452  C CD2  . LEU A 1 375 ? 27.042  -29.295 101.743 1.00 106.87 ?  384 LEU A CD2  1 
ATOM   5453  H H    . LEU A 1 375 ? 24.455  -26.110 103.919 1.00 142.09 ?  384 LEU A H    1 
ATOM   5454  H HA   . LEU A 1 375 ? 24.130  -26.363 101.327 1.00 118.09 ?  384 LEU A HA   1 
ATOM   5455  H HB2  . LEU A 1 375 ? 26.119  -26.946 102.278 1.00 132.40 ?  384 LEU A HB2  1 
ATOM   5456  H HB3  . LEU A 1 375 ? 25.407  -27.989 103.232 1.00 132.40 ?  384 LEU A HB3  1 
ATOM   5457  H HG   . LEU A 1 375 ? 25.041  -29.405 101.431 1.00 109.05 ?  384 LEU A HG   1 
ATOM   5458  H HD11 . LEU A 1 375 ? 25.939  -28.941 99.338  1.00 108.12 ?  384 LEU A HD11 1 
ATOM   5459  H HD12 . LEU A 1 375 ? 24.867  -27.831 99.717  1.00 108.12 ?  384 LEU A HD12 1 
ATOM   5460  H HD13 . LEU A 1 375 ? 26.418  -27.517 99.853  1.00 108.12 ?  384 LEU A HD13 1 
ATOM   5461  H HD21 . LEU A 1 375 ? 27.261  -30.010 101.126 1.00 128.24 ?  384 LEU A HD21 1 
ATOM   5462  H HD22 . LEU A 1 375 ? 27.717  -28.600 101.698 1.00 128.24 ?  384 LEU A HD22 1 
ATOM   5463  H HD23 . LEU A 1 375 ? 26.985  -29.643 102.647 1.00 128.24 ?  384 LEU A HD23 1 
ATOM   5464  N N    . MET A 1 376 ? 22.451  -28.366 103.172 1.00 103.38 ?  385 MET A N    1 
ATOM   5465  C CA   . MET A 1 376 ? 21.343  -29.300 103.158 1.00 101.55 ?  385 MET A CA   1 
ATOM   5466  C C    . MET A 1 376 ? 20.076  -28.628 102.635 1.00 110.13 ?  385 MET A C    1 
ATOM   5467  O O    . MET A 1 376 ? 19.382  -29.185 101.776 1.00 141.83 ?  385 MET A O    1 
ATOM   5468  C CB   . MET A 1 376 ? 21.139  -29.869 104.561 1.00 113.15 ?  385 MET A CB   1 
ATOM   5469  C CG   . MET A 1 376 ? 22.139  -30.962 104.942 1.00 115.15 ?  385 MET A CG   1 
ATOM   5470  S SD   . MET A 1 376 ? 21.605  -32.655 104.586 1.00 113.18 ?  385 MET A SD   1 
ATOM   5471  H H    . MET A 1 376 ? 22.755  -28.184 103.956 1.00 124.06 ?  385 MET A H    1 
ATOM   5472  H HA   . MET A 1 376 ? 21.567  -30.039 102.570 1.00 121.86 ?  385 MET A HA   1 
ATOM   5473  H HB2  . MET A 1 376 ? 21.228  -29.150 105.205 1.00 135.78 ?  385 MET A HB2  1 
ATOM   5474  H HB3  . MET A 1 376 ? 20.249  -30.251 104.616 1.00 135.78 ?  385 MET A HB3  1 
ATOM   5475  H HG2  . MET A 1 376 ? 22.963  -30.808 104.454 1.00 138.18 ?  385 MET A HG2  1 
ATOM   5476  H HG3  . MET A 1 376 ? 22.310  -30.904 105.895 1.00 138.18 ?  385 MET A HG3  1 
ATOM   5477  N N    . ASN A 1 377 ? 19.786  -27.407 103.100 1.00 104.43 ?  386 ASN A N    1 
ATOM   5478  C CA   . ASN A 1 377 ? 18.605  -26.713 102.610 1.00 118.36 ?  386 ASN A CA   1 
ATOM   5479  C C    . ASN A 1 377 ? 18.671  -26.633 101.106 1.00 171.37 ?  386 ASN A C    1 
ATOM   5480  O O    . ASN A 1 377 ? 17.752  -27.063 100.407 1.00 93.80  ?  386 ASN A O    1 
ATOM   5481  C CB   . ASN A 1 377 ? 18.516  -25.301 103.203 1.00 112.85 ?  386 ASN A CB   1 
ATOM   5482  C CG   . ASN A 1 377 ? 18.443  -25.303 104.719 1.00 117.64 ?  386 ASN A CG   1 
ATOM   5483  O OD1  . ASN A 1 377 ? 19.055  -24.457 105.398 1.00 127.81 ?  386 ASN A OD1  1 
ATOM   5484  N ND2  . ASN A 1 377 ? 17.662  -26.247 105.264 1.00 107.62 ?  386 ASN A ND2  1 
ATOM   5485  H H    . ASN A 1 377 ? 20.246  -26.975 103.683 1.00 125.31 ?  386 ASN A H    1 
ATOM   5486  H HA   . ASN A 1 377 ? 17.808  -27.206 102.860 1.00 142.03 ?  386 ASN A HA   1 
ATOM   5487  H HB2  . ASN A 1 377 ? 19.304  -24.799 102.942 1.00 135.42 ?  386 ASN A HB2  1 
ATOM   5488  H HB3  . ASN A 1 377 ? 17.718  -24.866 102.865 1.00 135.42 ?  386 ASN A HB3  1 
ATOM   5489  H HD21 . ASN A 1 377 ? 17.581  -26.297 106.119 1.00 129.15 ?  386 ASN A HD21 1 
ATOM   5490  H HD22 . ASN A 1 377 ? 17.242  -26.802 104.759 1.00 129.15 ?  386 ASN A HD22 1 
ATOM   5491  N N    . PHE A 1 378 ? 19.821  -26.206 100.599 1.00 114.20 ?  387 PHE A N    1 
ATOM   5492  C CA   . PHE A 1 378 ? 19.994  -26.034 99.169  1.00 90.78  ?  387 PHE A CA   1 
ATOM   5493  C C    . PHE A 1 378 ? 19.586  -27.315 98.432  1.00 85.42  ?  387 PHE A C    1 
ATOM   5494  O O    . PHE A 1 378 ? 18.812  -27.279 97.467  1.00 93.87  ?  387 PHE A O    1 
ATOM   5495  C CB   . PHE A 1 378 ? 21.459  -25.630 98.911  1.00 70.29  ?  387 PHE A CB   1 
ATOM   5496  C CG   . PHE A 1 378 ? 21.833  -25.585 97.463  1.00 68.62  ?  387 PHE A CG   1 
ATOM   5497  C CD1  . PHE A 1 378 ? 21.328  -24.588 96.643  1.00 74.59  ?  387 PHE A CD1  1 
ATOM   5498  C CD2  . PHE A 1 378 ? 22.681  -26.555 96.914  1.00 57.63  ?  387 PHE A CD2  1 
ATOM   5499  C CE1  . PHE A 1 378 ? 21.650  -24.535 95.308  1.00 72.92  ?  387 PHE A CE1  1 
ATOM   5500  C CE2  . PHE A 1 378 ? 23.031  -26.515 95.543  1.00 56.11  ?  387 PHE A CE2  1 
ATOM   5501  C CZ   . PHE A 1 378 ? 22.494  -25.508 94.741  1.00 79.40  ?  387 PHE A CZ   1 
ATOM   5502  H H    . PHE A 1 378 ? 20.516  -26.009 101.065 1.00 137.04 ?  387 PHE A H    1 
ATOM   5503  H HA   . PHE A 1 378 ? 19.423  -25.313 98.862  1.00 108.94 ?  387 PHE A HA   1 
ATOM   5504  H HB2  . PHE A 1 378 ? 21.608  -24.746 99.282  1.00 84.34  ?  387 PHE A HB2  1 
ATOM   5505  H HB3  . PHE A 1 378 ? 22.041  -26.272 99.347  1.00 84.34  ?  387 PHE A HB3  1 
ATOM   5506  H HD1  . PHE A 1 378 ? 20.759  -23.945 97.002  1.00 89.51  ?  387 PHE A HD1  1 
ATOM   5507  H HD2  . PHE A 1 378 ? 23.024  -27.228 97.456  1.00 69.16  ?  387 PHE A HD2  1 
ATOM   5508  H HE1  . PHE A 1 378 ? 21.299  -23.859 94.774  1.00 87.50  ?  387 PHE A HE1  1 
ATOM   5509  H HE2  . PHE A 1 378 ? 23.592  -27.161 95.178  1.00 67.33  ?  387 PHE A HE2  1 
ATOM   5510  H HZ   . PHE A 1 378 ? 22.718  -25.462 93.840  1.00 95.28  ?  387 PHE A HZ   1 
ATOM   5511  N N    . LEU A 1 379 ? 20.056  -28.469 98.910  1.00 79.08  ?  388 LEU A N    1 
ATOM   5512  C CA   . LEU A 1 379 ? 19.731  -29.721 98.236  1.00 84.68  ?  388 LEU A CA   1 
ATOM   5513  C C    . LEU A 1 379 ? 18.275  -30.180 98.487  1.00 82.40  ?  388 LEU A C    1 
ATOM   5514  O O    . LEU A 1 379 ? 17.606  -30.670 97.566  1.00 74.35  ?  388 LEU A O    1 
ATOM   5515  C CB   . LEU A 1 379 ? 20.762  -30.783 98.647  1.00 73.00  ?  388 LEU A CB   1 
ATOM   5516  C CG   . LEU A 1 379 ? 22.163  -30.592 98.036  1.00 107.26 ?  388 LEU A CG   1 
ATOM   5517  C CD1  . LEU A 1 379 ? 23.262  -31.231 98.851  1.00 126.12 ?  388 LEU A CD1  1 
ATOM   5518  C CD2  . LEU A 1 379 ? 22.211  -31.161 96.631  1.00 152.03 ?  388 LEU A CD2  1 
ATOM   5519  H H    . LEU A 1 379 ? 20.553  -28.551 99.607  1.00 94.89  ?  388 LEU A H    1 
ATOM   5520  H HA   . LEU A 1 379 ? 19.827  -29.583 97.281  1.00 101.62 ?  388 LEU A HA   1 
ATOM   5521  H HB2  . LEU A 1 379 ? 20.858  -30.765 99.612  1.00 87.59  ?  388 LEU A HB2  1 
ATOM   5522  H HB3  . LEU A 1 379 ? 20.437  -31.654 98.368  1.00 87.59  ?  388 LEU A HB3  1 
ATOM   5523  H HG   . LEU A 1 379 ? 22.351  -29.642 97.978  1.00 128.71 ?  388 LEU A HG   1 
ATOM   5524  H HD11 . LEU A 1 379 ? 24.112  -31.073 98.412  1.00 151.34 ?  388 LEU A HD11 1 
ATOM   5525  H HD12 . LEU A 1 379 ? 23.268  -30.836 99.737  1.00 151.34 ?  388 LEU A HD12 1 
ATOM   5526  H HD13 . LEU A 1 379 ? 23.094  -32.184 98.914  1.00 151.34 ?  388 LEU A HD13 1 
ATOM   5527  H HD21 . LEU A 1 379 ? 23.100  -31.029 96.268  1.00 182.43 ?  388 LEU A HD21 1 
ATOM   5528  H HD22 . LEU A 1 379 ? 22.005  -32.108 96.667  1.00 182.43 ?  388 LEU A HD22 1 
ATOM   5529  H HD23 . LEU A 1 379 ? 21.557  -30.701 96.082  1.00 182.43 ?  388 LEU A HD23 1 
ATOM   5530  N N    . LYS A 1 380 ? 17.726  -29.965 99.680  1.00 64.14  ?  389 LYS A N    1 
ATOM   5531  C CA   . LYS A 1 380 ? 16.323  -30.310 99.878  1.00 81.67  ?  389 LYS A CA   1 
ATOM   5532  C C    . LYS A 1 380 ? 15.469  -29.512 98.900  1.00 85.45  ?  389 LYS A C    1 
ATOM   5533  O O    . LYS A 1 380 ? 14.476  -30.022 98.373  1.00 112.33 ?  389 LYS A O    1 
ATOM   5534  C CB   . LYS A 1 380 ? 15.898  -30.035 101.331 1.00 101.26 ?  389 LYS A CB   1 
ATOM   5535  C CG   . LYS A 1 380 ? 16.216  -31.111 102.363 1.00 73.02  ?  389 LYS A CG   1 
ATOM   5536  H H    . LYS A 1 380 ? 18.126  -29.635 100.366 1.00 76.96  ?  389 LYS A H    1 
ATOM   5537  H HA   . LYS A 1 380 ? 16.194  -31.254 99.695  1.00 98.00  ?  389 LYS A HA   1 
ATOM   5538  H HB2  . LYS A 1 380 ? 16.336  -29.221 101.624 1.00 121.51 ?  389 LYS A HB2  1 
ATOM   5539  H HB3  . LYS A 1 380 ? 14.937  -29.903 101.344 1.00 121.51 ?  389 LYS A HB3  1 
ATOM   5540  H HG2  . LYS A 1 380 ? 15.833  -31.953 102.070 1.00 87.62  ?  389 LYS A HG2  1 
ATOM   5541  H HG3  . LYS A 1 380 ? 17.179  -31.196 102.444 1.00 87.62  ?  389 LYS A HG3  1 
ATOM   5542  N N    . THR A 1 381 ? 15.862  -28.255 98.654  1.00 106.55 ?  390 THR A N    1 
ATOM   5543  C CA   . THR A 1 381 ? 15.191  -27.388 97.693  1.00 89.13  ?  390 THR A CA   1 
ATOM   5544  C C    . THR A 1 381 ? 15.400  -27.898 96.278  1.00 96.71  ?  390 THR A C    1 
ATOM   5545  O O    . THR A 1 381 ? 14.449  -28.031 95.499  1.00 112.27 ?  390 THR A O    1 
ATOM   5546  C CB   . THR A 1 381 ? 15.753  -25.969 97.779  1.00 74.86  ?  390 THR A CB   1 
ATOM   5547  O OG1  . THR A 1 381 ? 15.733  -25.489 99.120  1.00 75.13  ?  390 THR A OG1  1 
ATOM   5548  C CG2  . THR A 1 381 ? 14.924  -25.000 96.916  1.00 110.29 ?  390 THR A CG2  1 
ATOM   5549  H H    . THR A 1 381 ? 16.531  -27.880 99.043  1.00 127.87 ?  390 THR A H    1 
ATOM   5550  H HA   . THR A 1 381 ? 14.239  -27.361 97.880  1.00 106.96 ?  390 THR A HA   1 
ATOM   5551  H HB   . THR A 1 381 ? 16.665  -25.965 97.450  1.00 89.84  ?  390 THR A HB   1 
ATOM   5552  H HG1  . THR A 1 381 ? 16.199  -25.988 99.610  1.00 90.15  ?  390 THR A HG1  1 
ATOM   5553  H HG21 . THR A 1 381 ? 15.291  -24.104 96.979  1.00 132.35 ?  390 THR A HG21 1 
ATOM   5554  H HG22 . THR A 1 381 ? 14.943  -25.284 95.988  1.00 132.35 ?  390 THR A HG22 1 
ATOM   5555  H HG23 . THR A 1 381 ? 14.004  -24.987 97.223  1.00 132.35 ?  390 THR A HG23 1 
ATOM   5556  N N    . VAL A 1 382 ? 16.656  -28.176 95.925  1.00 71.56  ?  391 VAL A N    1 
ATOM   5557  C CA   . VAL A 1 382 ? 16.949  -28.655 94.579  1.00 79.29  ?  391 VAL A CA   1 
ATOM   5558  C C    . VAL A 1 382 ? 16.238  -29.967 94.320  1.00 89.03  ?  391 VAL A C    1 
ATOM   5559  O O    . VAL A 1 382 ? 15.761  -30.229 93.210  1.00 100.54 ?  391 VAL A O    1 
ATOM   5560  C CB   . VAL A 1 382 ? 18.478  -28.763 94.380  1.00 71.97  ?  391 VAL A CB   1 
ATOM   5561  C CG1  . VAL A 1 382 ? 18.848  -29.563 93.181  1.00 118.37 ?  391 VAL A CG1  1 
ATOM   5562  C CG2  . VAL A 1 382 ? 19.000  -27.424 94.122  1.00 65.46  ?  391 VAL A CG2  1 
ATOM   5563  H H    . VAL A 1 382 ? 17.342  -28.097 96.437  1.00 85.88  ?  391 VAL A H    1 
ATOM   5564  H HA   . VAL A 1 382 ? 16.614  -28.008 93.939  1.00 95.14  ?  391 VAL A HA   1 
ATOM   5565  H HB   . VAL A 1 382 ? 18.904  -29.134 95.168  1.00 86.37  ?  391 VAL A HB   1 
ATOM   5566  H HG11 . VAL A 1 382 ? 19.814  -29.595 93.109  1.00 142.04 ?  391 VAL A HG11 1 
ATOM   5567  H HG12 . VAL A 1 382 ? 18.493  -30.460 93.279  1.00 142.04 ?  391 VAL A HG12 1 
ATOM   5568  H HG13 . VAL A 1 382 ? 18.470  -29.142 92.393  1.00 142.04 ?  391 VAL A HG13 1 
ATOM   5569  H HG21 . VAL A 1 382 ? 19.960  -27.479 93.996  1.00 78.56  ?  391 VAL A HG21 1 
ATOM   5570  H HG22 . VAL A 1 382 ? 18.580  -27.070 93.323  1.00 78.56  ?  391 VAL A HG22 1 
ATOM   5571  H HG23 . VAL A 1 382 ? 18.798  -26.855 94.882  1.00 78.56  ?  391 VAL A HG23 1 
ATOM   5572  N N    . ARG A 1 383 ? 16.161  -30.812 95.333  1.00 77.10  ?  392 ARG A N    1 
ATOM   5573  C CA   . ARG A 1 383 ? 15.459  -32.074 95.179  1.00 75.53  ?  392 ARG A CA   1 
ATOM   5574  C C    . ARG A 1 383 ? 13.941  -31.845 95.115  1.00 87.27  ?  392 ARG A C    1 
ATOM   5575  O O    . ARG A 1 383 ? 13.255  -32.360 94.222  1.00 94.54  ?  392 ARG A O    1 
ATOM   5576  C CB   . ARG A 1 383 ? 15.828  -32.984 96.346  1.00 80.77  ?  392 ARG A CB   1 
ATOM   5577  C CG   . ARG A 1 383 ? 15.206  -34.343 96.292  1.00 74.89  ?  392 ARG A CG   1 
ATOM   5578  C CD   . ARG A 1 383 ? 15.191  -35.048 97.666  1.00 83.58  ?  392 ARG A CD   1 
ATOM   5579  N NE   . ARG A 1 383 ? 13.915  -35.711 97.923  1.00 117.10 ?  392 ARG A NE   1 
ATOM   5580  C CZ   . ARG A 1 383 ? 12.721  -35.187 97.633  1.00 106.93 ?  392 ARG A CZ   1 
ATOM   5581  H H    . ARG A 1 383 ? 16.502  -30.683 96.112  1.00 92.52  ?  392 ARG A H    1 
ATOM   5582  H HA   . ARG A 1 383 ? 15.740  -32.501 94.355  1.00 90.63  ?  392 ARG A HA   1 
ATOM   5583  H HB2  . ARG A 1 383 ? 16.791  -33.102 96.355  1.00 96.93  ?  392 ARG A HB2  1 
ATOM   5584  H HB3  . ARG A 1 383 ? 15.543  -32.562 97.171  1.00 96.93  ?  392 ARG A HB3  1 
ATOM   5585  H HG2  . ARG A 1 383 ? 14.288  -34.258 95.988  1.00 89.87  ?  392 ARG A HG2  1 
ATOM   5586  H HG3  . ARG A 1 383 ? 15.709  -34.897 95.675  1.00 89.87  ?  392 ARG A HG3  1 
ATOM   5587  H HD2  . ARG A 1 383 ? 15.891  -35.719 97.688  1.00 100.29 ?  392 ARG A HD2  1 
ATOM   5588  H HD3  . ARG A 1 383 ? 15.336  -34.390 98.363  1.00 100.29 ?  392 ARG A HD3  1 
ATOM   5589  H HE   . ARG A 1 383 ? 13.933  -36.491 98.285  1.00 140.52 ?  392 ARG A HE   1 
ATOM   5590  N N    . SER A 1 384 ? 13.405  -31.038 96.035  1.00 72.16  ?  393 SER A N    1 
ATOM   5591  C CA   . SER A 1 384 ? 11.971  -30.810 96.062  1.00 96.01  ?  393 SER A CA   1 
ATOM   5592  C C    . SER A 1 384 ? 11.506  -30.150 94.775  1.00 97.06  ?  393 SER A C    1 
ATOM   5593  O O    . SER A 1 384 ? 10.381  -30.391 94.315  1.00 93.01  ?  393 SER A O    1 
ATOM   5594  C CB   . SER A 1 384 ? 11.590  -29.925 97.266  1.00 76.32  ?  393 SER A CB   1 
ATOM   5595  H H    . SER A 1 384 ? 13.847  -30.621 96.643  1.00 86.59  ?  393 SER A H    1 
ATOM   5596  H HA   . SER A 1 384 ? 11.512  -31.660 96.152  1.00 115.21 ?  393 SER A HA   1 
ATOM   5597  N N    . THR A 1 385 ? 12.359  -29.331 94.169  1.00 82.81  ?  394 THR A N    1 
ATOM   5598  C CA   . THR A 1 385 ? 11.989  -28.686 92.921  1.00 67.06  ?  394 THR A CA   1 
ATOM   5599  C C    . THR A 1 385 ? 12.067  -29.662 91.761  1.00 72.29  ?  394 THR A C    1 
ATOM   5600  O O    . THR A 1 385 ? 11.269  -29.573 90.817  1.00 87.12  ?  394 THR A O    1 
ATOM   5601  C CB   . THR A 1 385 ? 12.861  -27.451 92.747  1.00 70.78  ?  394 THR A CB   1 
ATOM   5602  O OG1  . THR A 1 385 ? 12.568  -26.564 93.831  1.00 91.15  ?  394 THR A OG1  1 
ATOM   5603  C CG2  . THR A 1 385 ? 12.623  -26.734 91.431  1.00 67.68  ?  394 THR A CG2  1 
ATOM   5604  H H    . THR A 1 385 ? 13.146  -29.137 94.456  1.00 99.38  ?  394 THR A H    1 
ATOM   5605  H HA   . THR A 1 385 ? 11.068  -28.387 92.989  1.00 80.47  ?  394 THR A HA   1 
ATOM   5606  H HB   . THR A 1 385 ? 13.794  -27.710 92.788  1.00 84.94  ?  394 THR A HB   1 
ATOM   5607  H HG1  . THR A 1 385 ? 12.738  -26.939 94.564  1.00 109.38 ?  394 THR A HG1  1 
ATOM   5608  H HG21 . THR A 1 385 ? 13.200  -25.958 91.368  1.00 81.22  ?  394 THR A HG21 1 
ATOM   5609  H HG22 . THR A 1 385 ? 12.814  -27.330 90.690  1.00 81.22  ?  394 THR A HG22 1 
ATOM   5610  H HG23 . THR A 1 385 ? 11.698  -26.446 91.373  1.00 81.22  ?  394 THR A HG23 1 
ATOM   5611  N N    . THR A 1 386 ? 12.996  -30.611 91.824  1.00 80.51  ?  395 THR A N    1 
ATOM   5612  C CA   . THR A 1 386 ? 13.022  -31.674 90.834  1.00 82.05  ?  395 THR A CA   1 
ATOM   5613  C C    . THR A 1 386 ? 11.855  -32.640 91.005  1.00 85.35  ?  395 THR A C    1 
ATOM   5614  O O    . THR A 1 386 ? 11.127  -32.904 90.042  1.00 86.48  ?  395 THR A O    1 
ATOM   5615  C CB   . THR A 1 386 ? 14.367  -32.370 90.907  1.00 75.99  ?  395 THR A CB   1 
ATOM   5616  O OG1  . THR A 1 386 ? 15.379  -31.388 90.635  1.00 70.34  ?  395 THR A OG1  1 
ATOM   5617  C CG2  . THR A 1 386 ? 14.448  -33.505 89.912  1.00 78.23  ?  395 THR A CG2  1 
ATOM   5618  H H    . THR A 1 386 ? 13.613  -30.660 92.422  1.00 96.61  ?  395 THR A H    1 
ATOM   5619  H HA   . THR A 1 386 ? 12.945  -31.276 89.952  1.00 98.46  ?  395 THR A HA   1 
ATOM   5620  H HB   . THR A 1 386 ? 14.497  -32.731 91.798  1.00 91.19  ?  395 THR A HB   1 
ATOM   5621  H HG1  . THR A 1 386 ? 15.341  -30.771 91.204  1.00 84.41  ?  395 THR A HG1  1 
ATOM   5622  H HG21 . THR A 1 386 ? 15.314  -33.938 89.973  1.00 93.88  ?  395 THR A HG21 1 
ATOM   5623  H HG22 . THR A 1 386 ? 13.755  -34.158 90.098  1.00 93.88  ?  395 THR A HG22 1 
ATOM   5624  H HG23 . THR A 1 386 ? 14.328  -33.166 89.011  1.00 93.88  ?  395 THR A HG23 1 
ATOM   5625  N N    . GLU A 1 387 ? 11.600  -33.122 92.225  1.00 97.86  ?  396 GLU A N    1 
ATOM   5626  C CA   . GLU A 1 387 ? 10.452  -34.021 92.412  1.00 89.79  ?  396 GLU A CA   1 
ATOM   5627  C C    . GLU A 1 387 ? 9.148   -33.332 91.995  1.00 90.45  ?  396 GLU A C    1 
ATOM   5628  O O    . GLU A 1 387 ? 8.289   -33.967 91.376  1.00 88.89  ?  396 GLU A O    1 
ATOM   5629  C CB   . GLU A 1 387 ? 10.342  -34.529 93.859  1.00 91.61  ?  396 GLU A CB   1 
ATOM   5630  H H    . GLU A 1 387 ? 12.055  -32.954 92.935  1.00 117.43 ?  396 GLU A H    1 
ATOM   5631  H HA   . GLU A 1 387 ? 10.570  -34.794 91.839  1.00 107.75 ?  396 GLU A HA   1 
ATOM   5632  N N    . LYS A 1 388 ? 8.979   -32.026 92.283  1.00 83.27  ?  397 LYS A N    1 
ATOM   5633  C CA   . LYS A 1 388 ? 7.733   -31.387 91.840  1.00 83.73  ?  397 LYS A CA   1 
ATOM   5634  C C    . LYS A 1 388 ? 7.697   -31.144 90.329  1.00 77.76  ?  397 LYS A C    1 
ATOM   5635  O O    . LYS A 1 388 ? 6.648   -30.771 89.811  1.00 94.09  ?  397 LYS A O    1 
ATOM   5636  C CB   . LYS A 1 388 ? 7.440   -30.068 92.589  1.00 76.25  ?  397 LYS A CB   1 
ATOM   5637  H H    . LYS A 1 388 ? 9.533   -31.521 92.704  1.00 99.92  ?  397 LYS A H    1 
ATOM   5638  H HA   . LYS A 1 388 ? 7.003   -31.993 92.044  1.00 100.48 ?  397 LYS A HA   1 
ATOM   5639  N N    . SER A 1 389 ? 8.769   -31.414 89.593  1.00 93.38  ?  398 SER A N    1 
ATOM   5640  C CA   . SER A 1 389 ? 8.767   -31.210 88.152  1.00 86.64  ?  398 SER A CA   1 
ATOM   5641  C C    . SER A 1 389 ? 8.243   -32.438 87.401  1.00 97.34  ?  398 SER A C    1 
ATOM   5642  O O    . SER A 1 389 ? 8.286   -32.463 86.160  1.00 66.45  ?  398 SER A O    1 
ATOM   5643  C CB   . SER A 1 389 ? 10.181  -30.864 87.690  1.00 93.03  ?  398 SER A CB   1 
ATOM   5644  H H    . SER A 1 389 ? 9.511   -31.716 89.906  1.00 112.06 ?  398 SER A H    1 
ATOM   5645  H HA   . SER A 1 389 ? 8.189   -30.460 87.939  1.00 103.97 ?  398 SER A HA   1 
ATOM   5646  N N    . LEU A 1 390 ? 7.765   -33.454 88.138  1.00 82.50  ?  399 LEU A N    1 
ATOM   5647  C CA   . LEU A 1 390 ? 7.168   -34.702 87.636  1.00 75.21  ?  399 LEU A CA   1 
ATOM   5648  C C    . LEU A 1 390 ? 5.701   -34.553 87.247  1.00 96.74  ?  399 LEU A C    1 
ATOM   5649  O O    . LEU A 1 390 ? 4.979   -33.649 87.699  1.00 91.34  ?  399 LEU A O    1 
ATOM   5650  C CB   . LEU A 1 390 ? 7.256   -35.824 88.694  1.00 83.36  ?  399 LEU A CB   1 
ATOM   5651  C CG   . LEU A 1 390 ? 8.625   -36.475 88.993  1.00 93.44  ?  399 LEU A CG   1 
ATOM   5652  C CD1  . LEU A 1 390 ? 8.655   -37.238 90.288  1.00 107.05 ?  399 LEU A CD1  1 
ATOM   5653  C CD2  . LEU A 1 390 ? 9.017   -37.416 87.895  1.00 82.49  ?  399 LEU A CD2  1 
ATOM   5654  H H    . LEU A 1 390 ? 7.781   -33.436 88.998  1.00 99.00  ?  399 LEU A H    1 
ATOM   5655  H HA   . LEU A 1 390 ? 7.657   -34.992 86.850  1.00 90.25  ?  399 LEU A HA   1 
ATOM   5656  H HB2  . LEU A 1 390 ? 6.933   -35.461 89.534  1.00 100.03 ?  399 LEU A HB2  1 
ATOM   5657  H HB3  . LEU A 1 390 ? 6.664   -36.539 88.414  1.00 100.03 ?  399 LEU A HB3  1 
ATOM   5658  H HG   . LEU A 1 390 ? 9.299   -35.779 89.042  1.00 112.12 ?  399 LEU A HG   1 
ATOM   5659  H HD11 . LEU A 1 390 ? 9.539   -37.618 90.411  1.00 128.46 ?  399 LEU A HD11 1 
ATOM   5660  H HD12 . LEU A 1 390 ? 8.451   -36.630 91.016  1.00 128.46 ?  399 LEU A HD12 1 
ATOM   5661  H HD13 . LEU A 1 390 ? 7.992   -37.945 90.253  1.00 128.46 ?  399 LEU A HD13 1 
ATOM   5662  H HD21 . LEU A 1 390 ? 9.878   -37.809 88.109  1.00 98.98  ?  399 LEU A HD21 1 
ATOM   5663  H HD22 . LEU A 1 390 ? 8.345   -38.112 87.821  1.00 98.98  ?  399 LEU A HD22 1 
ATOM   5664  H HD23 . LEU A 1 390 ? 9.076   -36.922 87.062  1.00 98.98  ?  399 LEU A HD23 1 
ATOM   5665  N N    . LEU A 1 391 ? 5.250   -35.539 86.473  1.00 99.40  ?  400 LEU A N    1 
ATOM   5666  C CA   . LEU A 1 391 ? 3.909   -35.584 85.905  1.00 119.31 ?  400 LEU A CA   1 
ATOM   5667  C C    . LEU A 1 391 ? 3.012   -36.619 86.582  1.00 109.74 ?  400 LEU A C    1 
ATOM   5668  O O    . LEU A 1 391 ? 2.001   -36.237 87.169  1.00 122.03 ?  400 LEU A O    1 
ATOM   5669  C CB   . LEU A 1 391 ? 4.030   -35.813 84.398  1.00 130.43 ?  400 LEU A CB   1 
ATOM   5670  C CG   . LEU A 1 391 ? 4.996   -34.862 83.661  1.00 72.95  ?  400 LEU A CG   1 
ATOM   5671  C CD1  . LEU A 1 391 ? 5.007   -35.164 82.221  1.00 72.12  ?  400 LEU A CD1  1 
ATOM   5672  C CD2  . LEU A 1 391 ? 4.686   -33.388 83.772  1.00 119.73 ?  400 LEU A CD2  1 
ATOM   5673  H H    . LEU A 1 391 ? 5.727   -36.221 86.256  1.00 119.28 ?  400 LEU A H    1 
ATOM   5674  H HA   . LEU A 1 391 ? 3.495   -34.717 86.033  1.00 143.17 ?  400 LEU A HA   1 
ATOM   5675  H HB2  . LEU A 1 391 ? 4.342   -36.719 84.248  1.00 156.52 ?  400 LEU A HB2  1 
ATOM   5676  H HB3  . LEU A 1 391 ? 3.152   -35.702 83.999  1.00 156.52 ?  400 LEU A HB3  1 
ATOM   5677  H HG   . LEU A 1 391 ? 5.894   -35.003 84.001  1.00 87.54  ?  400 LEU A HG   1 
ATOM   5678  H HD11 . LEU A 1 391 ? 5.619   -34.557 81.776  1.00 86.54  ?  400 LEU A HD11 1 
ATOM   5679  H HD12 . LEU A 1 391 ? 5.298   -36.080 82.093  1.00 86.54  ?  400 LEU A HD12 1 
ATOM   5680  H HD13 . LEU A 1 391 ? 4.111   -35.048 81.868  1.00 86.54  ?  400 LEU A HD13 1 
ATOM   5681  H HD21 . LEU A 1 391 ? 5.352   -32.888 83.275  1.00 143.67 ?  400 LEU A HD21 1 
ATOM   5682  H HD22 . LEU A 1 391 ? 3.804   -33.223 83.403  1.00 143.67 ?  400 LEU A HD22 1 
ATOM   5683  H HD23 . LEU A 1 391 ? 4.708   -33.131 84.707  1.00 143.67 ?  400 LEU A HD23 1 
ATOM   5684  N N    . LYS A 1 392 ? 3.320   -37.912 86.526  1.00 106.41 ?  401 LYS A N    1 
ATOM   5685  C CA   . LYS A 1 392 ? 2.417   -38.894 87.150  1.00 112.05 ?  401 LYS A CA   1 
ATOM   5686  C C    . LYS A 1 392 ? 2.913   -39.173 88.598  1.00 126.89 ?  401 LYS A C    1 
ATOM   5687  O O    . LYS A 1 392 ? 3.463   -40.233 88.944  1.00 143.89 ?  401 LYS A O    1 
ATOM   5688  C CB   . LYS A 1 392 ? 2.291   -40.195 86.316  1.00 94.06  ?  401 LYS A CB   1 
ATOM   5689  H H    . LYS A 1 392 ? 4.018   -38.244 86.149  1.00 127.69 ?  401 LYS A H    1 
ATOM   5690  H HA   . LYS A 1 392 ? 1.532   -38.502 87.215  1.00 134.46 ?  401 LYS A HA   1 
ATOM   5691  N N    . MET B 1 1   ? 21.531  -10.755 57.679  1.00 139.98 1  10  MET B N    1 
ATOM   5692  C CA   . MET B 1 1   ? 20.477  -10.452 58.641  1.00 115.29 ?  10  MET B CA   1 
ATOM   5693  C C    . MET B 1 1   ? 20.517  -11.405 59.850  1.00 96.07  ?  10  MET B C    1 
ATOM   5694  O O    . MET B 1 1   ? 21.017  -12.521 59.756  1.00 102.27 ?  10  MET B O    1 
ATOM   5695  C CB   . MET B 1 1   ? 19.098  -10.518 57.962  1.00 132.46 ?  10  MET B CB   1 
ATOM   5696  H HA   . MET B 1 1   ? 20.602  -9.545  58.960  1.00 138.35 ?  10  MET B HA   1 
ATOM   5697  N N    . ILE B 1 2   ? 20.034  -10.892 60.995  1.00 84.98  ?  11  ILE B N    1 
ATOM   5698  C CA   . ILE B 1 2   ? 19.889  -11.610 62.267  1.00 120.76 ?  11  ILE B CA   1 
ATOM   5699  C C    . ILE B 1 2   ? 18.654  -12.505 62.261  1.00 106.34 ?  11  ILE B C    1 
ATOM   5700  O O    . ILE B 1 2   ? 17.642  -12.206 61.620  1.00 123.31 ?  11  ILE B O    1 
ATOM   5701  C CB   . ILE B 1 2   ? 19.817  -10.605 63.432  1.00 192.41 ?  11  ILE B CB   1 
ATOM   5702  C CG1  . ILE B 1 2   ? 21.138  -9.851  63.546  1.00 113.83 ?  11  ILE B CG1  1 
ATOM   5703  C CG2  . ILE B 1 2   ? 19.424  -11.290 64.726  1.00 80.66  ?  11  ILE B CG2  1 
ATOM   5704  C CD1  . ILE B 1 2   ? 21.118  -8.741  64.534  1.00 141.21 ?  11  ILE B CD1  1 
ATOM   5705  H H    . ILE B 1 2   ? 19.768  -10.076 61.055  1.00 101.97 ?  11  ILE B H    1 
ATOM   5706  H HA   . ILE B 1 2   ? 20.667  -12.173 62.403  1.00 144.92 ?  11  ILE B HA   1 
ATOM   5707  H HB   . ILE B 1 2   ? 19.127  -9.957  63.220  1.00 230.89 ?  11  ILE B HB   1 
ATOM   5708  H HG12 . ILE B 1 2   ? 21.830  -10.475 63.816  1.00 136.59 ?  11  ILE B HG12 1 
ATOM   5709  H HG13 . ILE B 1 2   ? 21.357  -9.473  62.680  1.00 136.59 ?  11  ILE B HG13 1 
ATOM   5710  H HG21 . ILE B 1 2   ? 19.389  -10.629 65.435  1.00 96.80  ?  11  ILE B HG21 1 
ATOM   5711  H HG22 . ILE B 1 2   ? 18.552  -11.701 64.613  1.00 96.80  ?  11  ILE B HG22 1 
ATOM   5712  H HG23 . ILE B 1 2   ? 20.084  -11.968 64.938  1.00 96.80  ?  11  ILE B HG23 1 
ATOM   5713  H HD11 . ILE B 1 2   ? 21.989  -8.315  64.548  1.00 169.45 ?  11  ILE B HD11 1 
ATOM   5714  H HD12 . ILE B 1 2   ? 20.439  -8.099  64.273  1.00 169.45 ?  11  ILE B HD12 1 
ATOM   5715  H HD13 . ILE B 1 2   ? 20.912  -9.103  65.411  1.00 169.45 ?  11  ILE B HD13 1 
ATOM   5716  N N    . SER B 1 3   ? 18.712  -13.574 63.057  1.00 100.10 ?  12  SER B N    1 
ATOM   5717  C CA   . SER B 1 3   ? 17.640  -14.563 63.096  1.00 127.33 ?  12  SER B CA   1 
ATOM   5718  C C    . SER B 1 3   ? 16.357  -14.021 63.716  1.00 146.87 ?  12  SER B C    1 
ATOM   5719  O O    . SER B 1 3   ? 16.376  -13.295 64.713  1.00 100.49 ?  12  SER B O    1 
ATOM   5720  C CB   . SER B 1 3   ? 18.083  -15.808 63.853  1.00 103.15 ?  12  SER B CB   1 
ATOM   5721  O OG   . SER B 1 3   ? 17.042  -16.774 63.896  1.00 116.30 ?  12  SER B OG   1 
ATOM   5722  H H    . SER B 1 3   ? 19.367  -13.748 63.587  1.00 120.12 ?  12  SER B H    1 
ATOM   5723  H HA   . SER B 1 3   ? 17.434  -14.831 62.186  1.00 152.80 ?  12  SER B HA   1 
ATOM   5724  H HB2  . SER B 1 3   ? 18.853  -16.193 63.405  1.00 123.78 ?  12  SER B HB2  1 
ATOM   5725  H HB3  . SER B 1 3   ? 18.319  -15.558 64.760  1.00 123.78 ?  12  SER B HB3  1 
ATOM   5726  H HG   . SER B 1 3   ? 17.299  -17.454 64.316  1.00 139.56 ?  12  SER B HG   1 
ATOM   5727  N N    . LYS B 1 4   ? 15.228  -14.416 63.124  1.00 92.84  ?  13  LYS B N    1 
ATOM   5728  C CA   . LYS B 1 4   ? 13.945  -13.921 63.574  1.00 80.85  ?  13  LYS B CA   1 
ATOM   5729  C C    . LYS B 1 4   ? 13.569  -14.484 64.930  1.00 90.70  ?  13  LYS B C    1 
ATOM   5730  O O    . LYS B 1 4   ? 12.786  -13.855 65.647  1.00 83.06  ?  13  LYS B O    1 
ATOM   5731  C CB   . LYS B 1 4   ? 12.869  -14.245 62.533  1.00 156.63 ?  13  LYS B CB   1 
ATOM   5732  H H    . LYS B 1 4   ? 15.186  -14.967 62.465  1.00 111.41 ?  13  LYS B H    1 
ATOM   5733  H HA   . LYS B 1 4   ? 13.996  -12.956 63.658  1.00 97.02  ?  13  LYS B HA   1 
ATOM   5734  N N    . GLU B 1 5   ? 14.165  -15.596 65.344  1.00 111.13 ?  14  GLU B N    1 
ATOM   5735  C CA   . GLU B 1 5   ? 13.840  -16.095 66.675  1.00 97.41  ?  14  GLU B CA   1 
ATOM   5736  C C    . GLU B 1 5   ? 14.392  -15.202 67.793  1.00 90.26  ?  14  GLU B C    1 
ATOM   5737  O O    . GLU B 1 5   ? 14.086  -15.446 68.964  1.00 101.30 ?  14  GLU B O    1 
ATOM   5738  C CB   . GLU B 1 5   ? 14.309  -17.551 66.838  1.00 81.86  ?  14  GLU B CB   1 
ATOM   5739  C CG   . GLU B 1 5   ? 15.784  -17.784 66.696  1.00 167.24 ?  14  GLU B CG   1 
ATOM   5740  H H    . GLU B 1 5   ? 14.735  -16.061 64.899  1.00 133.35 ?  14  GLU B H    1 
ATOM   5741  H HA   . GLU B 1 5   ? 12.874  -16.096 66.766  1.00 116.89 ?  14  GLU B HA   1 
ATOM   5742  H HB2  . GLU B 1 5   ? 14.051  -17.858 67.721  1.00 98.23  ?  14  GLU B HB2  1 
ATOM   5743  H HB3  . GLU B 1 5   ? 13.865  -18.092 66.166  1.00 98.23  ?  14  GLU B HB3  1 
ATOM   5744  H HG2  . GLU B 1 5   ? 16.139  -17.167 66.037  1.00 200.69 ?  14  GLU B HG2  1 
ATOM   5745  H HG3  . GLU B 1 5   ? 16.211  -17.634 67.554  1.00 200.69 ?  14  GLU B HG3  1 
ATOM   5746  N N    . TYR B 1 6   ? 15.177  -14.176 67.478  1.00 110.50 ?  15  TYR B N    1 
ATOM   5747  C CA   . TYR B 1 6   ? 15.616  -13.248 68.506  1.00 124.99 ?  15  TYR B CA   1 
ATOM   5748  C C    . TYR B 1 6   ? 14.789  -11.983 68.599  1.00 92.71  ?  15  TYR B C    1 
ATOM   5749  O O    . TYR B 1 6   ? 15.059  -11.173 69.486  1.00 91.48  ?  15  TYR B O    1 
ATOM   5750  C CB   . TYR B 1 6   ? 17.076  -12.852 68.309  1.00 148.75 ?  15  TYR B CB   1 
ATOM   5751  C CG   . TYR B 1 6   ? 17.982  -13.975 68.564  1.00 133.72 ?  15  TYR B CG   1 
ATOM   5752  C CD1  . TYR B 1 6   ? 18.080  -14.540 69.820  1.00 110.37 ?  15  TYR B CD1  1 
ATOM   5753  C CD2  . TYR B 1 6   ? 18.737  -14.471 67.550  1.00 63.55  ?  15  TYR B CD2  1 
ATOM   5754  C CE1  . TYR B 1 6   ? 18.895  -15.581 70.035  1.00 80.73  ?  15  TYR B CE1  1 
ATOM   5755  C CE2  . TYR B 1 6   ? 19.560  -15.514 67.741  1.00 71.63  ?  15  TYR B CE2  1 
ATOM   5756  C CZ   . TYR B 1 6   ? 19.654  -16.088 68.978  1.00 74.85  ?  15  TYR B CZ   1 
ATOM   5757  O OH   . TYR B 1 6   ? 20.526  -17.166 69.127  1.00 87.72  ?  15  TYR B OH   1 
ATOM   5758  H H    . TYR B 1 6   ? 15.465  -13.999 66.687  1.00 132.60 ?  15  TYR B H    1 
ATOM   5759  H HA   . TYR B 1 6   ? 15.553  -13.695 69.364  1.00 149.99 ?  15  TYR B HA   1 
ATOM   5760  H HB2  . TYR B 1 6   ? 17.206  -12.559 67.393  1.00 178.50 ?  15  TYR B HB2  1 
ATOM   5761  H HB3  . TYR B 1 6   ? 17.299  -12.136 68.924  1.00 178.50 ?  15  TYR B HB3  1 
ATOM   5762  H HD1  . TYR B 1 6   ? 17.563  -14.208 70.518  1.00 132.45 ?  15  TYR B HD1  1 
ATOM   5763  H HD2  . TYR B 1 6   ? 18.668  -14.094 66.703  1.00 76.26  ?  15  TYR B HD2  1 
ATOM   5764  H HE1  . TYR B 1 6   ? 18.954  -15.964 70.880  1.00 96.87  ?  15  TYR B HE1  1 
ATOM   5765  H HE2  . TYR B 1 6   ? 20.065  -15.845 67.033  1.00 85.95  ?  15  TYR B HE2  1 
ATOM   5766  H HH   . TYR B 1 6   ? 20.899  -17.337 68.395  1.00 105.26 ?  15  TYR B HH   1 
ATOM   5767  N N    . HIS B 1 7   ? 13.820  -11.766 67.712  1.00 99.92  ?  16  HIS B N    1 
ATOM   5768  C CA   . HIS B 1 7   ? 12.895  -10.630 67.840  1.00 85.90  ?  16  HIS B CA   1 
ATOM   5769  C C    . HIS B 1 7   ? 13.632  -9.300  67.881  1.00 103.75 ?  16  HIS B C    1 
ATOM   5770  O O    . HIS B 1 7   ? 13.354  -8.434  68.713  1.00 83.83  ?  16  HIS B O    1 
ATOM   5771  C CB   . HIS B 1 7   ? 12.022  -10.746 69.082  1.00 89.11  ?  16  HIS B CB   1 
ATOM   5772  C CG   . HIS B 1 7   ? 11.196  -11.983 69.136  1.00 86.15  ?  16  HIS B CG   1 
ATOM   5773  N ND1  . HIS B 1 7   ? 10.766  -12.650 68.009  1.00 88.79  ?  16  HIS B ND1  1 
ATOM   5774  C CD2  . HIS B 1 7   ? 10.670  -12.646 70.192  1.00 90.14  ?  16  HIS B CD2  1 
ATOM   5775  C CE1  . HIS B 1 7   ? 10.047  -13.697 68.372  1.00 92.35  ?  16  HIS B CE1  1 
ATOM   5776  N NE2  . HIS B 1 7   ? 9.972   -13.716 69.692  1.00 95.97  ?  16  HIS B NE2  1 
ATOM   5777  H H    . HIS B 1 7   ? 13.674  -12.260 67.024  1.00 119.90 ?  16  HIS B H    1 
ATOM   5778  H HA   . HIS B 1 7   ? 12.309  -10.619 67.067  1.00 103.08 ?  16  HIS B HA   1 
ATOM   5779  H HB2  . HIS B 1 7   ? 12.594  -10.739 69.866  1.00 106.93 ?  16  HIS B HB2  1 
ATOM   5780  H HB3  . HIS B 1 7   ? 11.419  -9.987  69.111  1.00 106.93 ?  16  HIS B HB3  1 
ATOM   5781  H HD2  . HIS B 1 7   ? 10.784  -12.432 71.090  1.00 108.17 ?  16  HIS B HD2  1 
ATOM   5782  H HE1  . HIS B 1 7   ? 9.650   -14.310 67.797  1.00 110.83 ?  16  HIS B HE1  1 
ATOM   5783  N N    . ILE B 1 8   ? 14.572  -9.129  66.970  1.00 103.61 ?  17  ILE B N    1 
ATOM   5784  C CA   . ILE B 1 8   ? 15.169  -7.825  66.741  1.00 68.54  ?  17  ILE B CA   1 
ATOM   5785  C C    . ILE B 1 8   ? 14.705  -7.334  65.389  1.00 70.77  ?  17  ILE B C    1 
ATOM   5786  O O    . ILE B 1 8   ? 14.707  -8.093  64.415  1.00 76.06  ?  17  ILE B O    1 
ATOM   5787  C CB   . ILE B 1 8   ? 16.698  -7.849  66.822  1.00 70.72  ?  17  ILE B CB   1 
ATOM   5788  C CG1  . ILE B 1 8   ? 17.149  -8.155  68.256  1.00 87.14  ?  17  ILE B CG1  1 
ATOM   5789  C CG2  . ILE B 1 8   ? 17.202  -6.509  66.363  1.00 58.00  ?  17  ILE B CG2  1 
ATOM   5790  C CD1  . ILE B 1 8   ? 18.541  -8.556  68.379  1.00 144.95 ?  17  ILE B CD1  1 
ATOM   5791  H H    . ILE B 1 8   ? 14.883  -9.753  66.467  1.00 124.33 ?  17  ILE B H    1 
ATOM   5792  H HA   . ILE B 1 8   ? 14.844  -7.206  67.413  1.00 82.25  ?  17  ILE B HA   1 
ATOM   5793  H HB   . ILE B 1 8   ? 17.037  -8.537  66.228  1.00 84.86  ?  17  ILE B HB   1 
ATOM   5794  H HG12 . ILE B 1 8   ? 17.023  -7.360  68.797  1.00 104.56 ?  17  ILE B HG12 1 
ATOM   5795  H HG13 . ILE B 1 8   ? 16.603  -8.877  68.605  1.00 104.56 ?  17  ILE B HG13 1 
ATOM   5796  H HG21 . ILE B 1 8   ? 18.171  -6.504  66.407  1.00 69.59  ?  17  ILE B HG21 1 
ATOM   5797  H HG22 . ILE B 1 8   ? 16.911  -6.358  65.450  1.00 69.59  ?  17  ILE B HG22 1 
ATOM   5798  H HG23 . ILE B 1 8   ? 16.841  -5.820  66.944  1.00 69.59  ?  17  ILE B HG23 1 
ATOM   5799  H HD11 . ILE B 1 8   ? 18.738  -8.729  69.313  1.00 173.94 ?  17  ILE B HD11 1 
ATOM   5800  H HD12 . ILE B 1 8   ? 18.686  -9.360  67.856  1.00 173.94 ?  17  ILE B HD12 1 
ATOM   5801  H HD13 . ILE B 1 8   ? 19.106  -7.840  68.048  1.00 173.94 ?  17  ILE B HD13 1 
ATOM   5802  N N    . ASP B 1 9   ? 14.258  -6.091  65.356  1.00 79.78  ?  18  ASP B N    1 
ATOM   5803  C CA   . ASP B 1 9   ? 13.631  -5.522  64.188  1.00 122.83 ?  18  ASP B CA   1 
ATOM   5804  C C    . ASP B 1 9   ? 14.656  -4.807  63.334  1.00 87.64  ?  18  ASP B C    1 
ATOM   5805  O O    . ASP B 1 9   ? 15.525  -4.118  63.863  1.00 81.65  ?  18  ASP B O    1 
ATOM   5806  C CB   . ASP B 1 9   ? 12.547  -4.545  64.615  1.00 110.24 ?  18  ASP B CB   1 
ATOM   5807  C CG   . ASP B 1 9   ? 11.795  -4.035  63.461  1.00 72.02  ?  18  ASP B CG   1 
ATOM   5808  O OD1  . ASP B 1 9   ? 11.027  -4.838  62.893  1.00 120.16 ?  18  ASP B OD1  1 
ATOM   5809  O OD2  . ASP B 1 9   ? 12.012  -2.868  63.072  1.00 85.11  -1 18  ASP B OD2  1 
ATOM   5810  H H    . ASP B 1 9   ? 14.310  -5.545  66.018  1.00 95.73  ?  18  ASP B H    1 
ATOM   5811  H HA   . ASP B 1 9   ? 13.224  -6.227  63.659  1.00 147.40 ?  18  ASP B HA   1 
ATOM   5812  H HB2  . ASP B 1 9   ? 11.925  -4.996  65.207  1.00 132.29 ?  18  ASP B HB2  1 
ATOM   5813  H HB3  . ASP B 1 9   ? 12.956  -3.792  65.068  1.00 132.29 ?  18  ASP B HB3  1 
ATOM   5814  N N    . GLU B 1 10  ? 14.551  -4.969  62.012  1.00 103.71 ?  19  GLU B N    1 
ATOM   5815  C CA   . GLU B 1 10  ? 15.466  -4.271  61.123  1.00 112.13 ?  19  GLU B CA   1 
ATOM   5816  C C    . GLU B 1 10  ? 15.399  -2.754  61.337  1.00 122.33 ?  19  GLU B C    1 
ATOM   5817  O O    . GLU B 1 10  ? 16.428  -2.071  61.292  1.00 110.33 ?  19  GLU B O    1 
ATOM   5818  C CB   . GLU B 1 10  ? 15.154  -4.637  59.672  1.00 124.72 ?  19  GLU B CB   1 
ATOM   5819  H H    . GLU B 1 10  ? 13.971  -5.467  61.617  1.00 124.45 ?  19  GLU B H    1 
ATOM   5820  H HA   . GLU B 1 10  ? 16.372  -4.560  61.315  1.00 134.56 ?  19  GLU B HA   1 
ATOM   5821  N N    . GLU B 1 11  ? 14.222  -2.215  61.654  1.00 134.52 ?  20  GLU B N    1 
ATOM   5822  C CA   . GLU B 1 11  ? 14.071  -0.773  61.851  1.00 121.12 ?  20  GLU B CA   1 
ATOM   5823  C C    . GLU B 1 11  ? 14.343  -0.312  63.296  1.00 106.55 ?  20  GLU B C    1 
ATOM   5824  O O    . GLU B 1 11  ? 15.170  0.576   63.514  1.00 135.49 ?  20  GLU B O    1 
ATOM   5825  C CB   . GLU B 1 11  ? 12.673  -0.354  61.382  1.00 129.36 ?  20  GLU B CB   1 
ATOM   5826  C CG   . GLU B 1 11  ? 12.430  1.140   61.388  1.00 142.76 ?  20  GLU B CG   1 
ATOM   5827  H H    . GLU B 1 11  ? 13.495  -2.662  61.760  1.00 161.43 ?  20  GLU B H    1 
ATOM   5828  H HA   . GLU B 1 11  ? 14.713  -0.321  61.282  1.00 145.34 ?  20  GLU B HA   1 
ATOM   5829  H HB2  . GLU B 1 11  ? 12.543  -0.670  60.474  1.00 155.23 ?  20  GLU B HB2  1 
ATOM   5830  H HB3  . GLU B 1 11  ? 12.015  -0.762  61.966  1.00 155.23 ?  20  GLU B HB3  1 
ATOM   5831  H HG2  . GLU B 1 11  ? 12.494  1.466   62.299  1.00 171.32 ?  20  GLU B HG2  1 
ATOM   5832  H HG3  . GLU B 1 11  ? 13.099  1.571   60.833  1.00 171.32 ?  20  GLU B HG3  1 
ATOM   5833  N N    . VAL B 1 12  ? 13.637  -0.873  64.284  1.00 105.38 ?  21  VAL B N    1 
ATOM   5834  C CA   . VAL B 1 12  ? 13.614  -0.359  65.659  1.00 85.87  ?  21  VAL B CA   1 
ATOM   5835  C C    . VAL B 1 12  ? 14.411  -1.220  66.652  1.00 60.16  ?  21  VAL B C    1 
ATOM   5836  O O    . VAL B 1 12  ? 14.302  -1.016  67.875  1.00 66.29  ?  21  VAL B O    1 
ATOM   5837  C CB   . VAL B 1 12  ? 12.161  -0.222  66.170  1.00 90.99  ?  21  VAL B CB   1 
ATOM   5838  C CG1  . VAL B 1 12  ? 11.313  0.690   65.251  1.00 72.43  ?  21  VAL B CG1  1 
ATOM   5839  C CG2  . VAL B 1 12  ? 11.505  -1.624  66.370  1.00 70.39  ?  21  VAL B CG2  1 
ATOM   5840  H H    . VAL B 1 12  ? 13.149  -1.573  64.177  1.00 126.46 ?  21  VAL B H    1 
ATOM   5841  H HA   . VAL B 1 12  ? 14.008  0.527   65.662  1.00 103.04 ?  21  VAL B HA   1 
ATOM   5842  H HB   . VAL B 1 12  ? 12.189  0.203   67.041  1.00 109.19 ?  21  VAL B HB   1 
ATOM   5843  H HG11 . VAL B 1 12  ? 10.413  0.748   65.607  1.00 86.92  ?  21  VAL B HG11 1 
ATOM   5844  H HG12 . VAL B 1 12  ? 11.716  1.572   65.224  1.00 86.92  ?  21  VAL B HG12 1 
ATOM   5845  H HG13 . VAL B 1 12  ? 11.293  0.308   64.360  1.00 86.92  ?  21  VAL B HG13 1 
ATOM   5846  H HG21 . VAL B 1 12  ? 10.597  -1.505  66.690  1.00 84.46  ?  21  VAL B HG21 1 
ATOM   5847  H HG22 . VAL B 1 12  ? 11.498  -2.093  65.521  1.00 84.46  ?  21  VAL B HG22 1 
ATOM   5848  H HG23 . VAL B 1 12  ? 12.022  -2.125  67.021  1.00 84.46  ?  21  VAL B HG23 1 
ATOM   5849  N N    . GLY B 1 13  ? 15.123  -2.242  66.200  1.00 58.30  ?  22  GLY B N    1 
ATOM   5850  C CA   . GLY B 1 13  ? 15.915  -3.018  67.129  1.00 54.04  ?  22  GLY B CA   1 
ATOM   5851  C C    . GLY B 1 13  ? 15.187  -3.867  68.151  1.00 94.21  ?  22  GLY B C    1 
ATOM   5852  O O    . GLY B 1 13  ? 14.438  -4.814  67.844  1.00 55.31  ?  22  GLY B O    1 
ATOM   5853  H H    . GLY B 1 13  ? 15.163  -2.499  65.380  1.00 69.96  ?  22  GLY B H    1 
ATOM   5854  H HA2  . GLY B 1 13  ? 16.487  -3.611  66.617  1.00 64.85  ?  22  GLY B HA2  1 
ATOM   5855  H HA3  . GLY B 1 13  ? 16.490  -2.409  67.618  1.00 64.85  ?  22  GLY B HA3  1 
ATOM   5856  N N    . PHE B 1 14  ? 15.491  -3.572  69.408  1.00 60.19  ?  23  PHE B N    1 
ATOM   5857  C CA   . PHE B 1 14  ? 14.909  -4.330  70.513  1.00 68.70  ?  23  PHE B CA   1 
ATOM   5858  C C    . PHE B 1 14  ? 13.536  -3.834  70.874  1.00 89.62  ?  23  PHE B C    1 
ATOM   5859  O O    . PHE B 1 14  ? 12.806  -4.505  71.619  1.00 79.67  ?  23  PHE B O    1 
ATOM   5860  C CB   . PHE B 1 14  ? 15.763  -4.222  71.752  1.00 76.50  ?  23  PHE B CB   1 
ATOM   5861  C CG   . PHE B 1 14  ? 17.006  -4.959  71.672  1.00 102.88 ?  23  PHE B CG   1 
ATOM   5862  C CD1  . PHE B 1 14  ? 16.994  -6.321  71.716  1.00 100.30 ?  23  PHE B CD1  1 
ATOM   5863  C CD2  . PHE B 1 14  ? 18.196  -4.300  71.563  1.00 105.49 ?  23  PHE B CD2  1 
ATOM   5864  C CE1  . PHE B 1 14  ? 18.126  -7.020  71.650  1.00 68.80  ?  23  PHE B CE1  1 
ATOM   5865  C CE2  . PHE B 1 14  ? 19.360  -4.995  71.510  1.00 77.18  ?  23  PHE B CE2  1 
ATOM   5866  C CZ   . PHE B 1 14  ? 19.349  -6.340  71.538  1.00 63.89  ?  23  PHE B CZ   1 
ATOM   5867  H H    . PHE B 1 14  ? 16.026  -2.944  69.649  1.00 72.22  ?  23  PHE B H    1 
ATOM   5868  H HA   . PHE B 1 14  ? 14.844  -5.265  70.265  1.00 82.44  ?  23  PHE B HA   1 
ATOM   5869  H HB2  . PHE B 1 14  ? 15.981  -3.288  71.901  1.00 91.80  ?  23  PHE B HB2  1 
ATOM   5870  H HB3  . PHE B 1 14  ? 15.262  -4.567  72.508  1.00 91.80  ?  23  PHE B HB3  1 
ATOM   5871  H HD1  . PHE B 1 14  ? 16.183  -6.770  71.788  1.00 120.36 ?  23  PHE B HD1  1 
ATOM   5872  H HD2  . PHE B 1 14  ? 18.210  -3.371  71.541  1.00 126.59 ?  23  PHE B HD2  1 
ATOM   5873  H HE1  . PHE B 1 14  ? 18.107  -7.949  71.678  1.00 82.56  ?  23  PHE B HE1  1 
ATOM   5874  H HE2  . PHE B 1 14  ? 20.167  -4.541  71.430  1.00 92.62  ?  23  PHE B HE2  1 
ATOM   5875  H HZ   . PHE B 1 14  ? 20.147  -6.815  71.494  1.00 76.67  ?  23  PHE B HZ   1 
ATOM   5876  N N    . ALA B 1 15  ? 13.183  -2.668  70.368  1.00 83.76  ?  24  ALA B N    1 
ATOM   5877  C CA   . ALA B 1 15  ? 11.856  -2.190  70.580  1.00 95.99  ?  24  ALA B CA   1 
ATOM   5878  C C    . ALA B 1 15  ? 10.861  -3.139  69.916  1.00 100.48 ?  24  ALA B C    1 
ATOM   5879  O O    . ALA B 1 15  ? 11.197  -3.934  69.020  1.00 84.46  ?  24  ALA B O    1 
ATOM   5880  C CB   . ALA B 1 15  ? 11.741  -0.780  70.035  1.00 102.19 ?  24  ALA B CB   1 
ATOM   5881  H H    . ALA B 1 15  ? 13.690  -2.149  69.907  1.00 100.51 ?  24  ALA B H    1 
ATOM   5882  H HA   . ALA B 1 15  ? 11.669  -2.166  71.532  1.00 115.19 ?  24  ALA B HA   1 
ATOM   5883  H HB1  . ALA B 1 15  ? 10.838  -0.458  70.181  1.00 122.63 ?  24  ALA B HB1  1 
ATOM   5884  H HB2  . ALA B 1 15  ? 12.375  -0.210  70.498  1.00 122.63 ?  24  ALA B HB2  1 
ATOM   5885  H HB3  . ALA B 1 15  ? 11.939  -0.792  69.085  1.00 122.63 ?  24  ALA B HB3  1 
ATOM   5886  N N    . LEU B 1 16  ? 9.631   -3.070  70.412  1.00 93.56  ?  25  LEU B N    1 
ATOM   5887  C CA   . LEU B 1 16  ? 8.528   -3.815  69.845  1.00 88.08  ?  25  LEU B CA   1 
ATOM   5888  C C    . LEU B 1 16  ? 7.961   -3.048  68.655  1.00 95.00  ?  25  LEU B C    1 
ATOM   5889  O O    . LEU B 1 16  ? 7.601   -1.885  68.807  1.00 113.39 ?  25  LEU B O    1 
ATOM   5890  C CB   . LEU B 1 16  ? 7.487   -4.018  70.930  1.00 71.83  ?  25  LEU B CB   1 
ATOM   5891  C CG   . LEU B 1 16  ? 6.372   -4.988  70.641  1.00 78.90  ?  25  LEU B CG   1 
ATOM   5892  C CD1  . LEU B 1 16  ? 6.917   -6.356  70.397  1.00 74.12  ?  25  LEU B CD1  1 
ATOM   5893  C CD2  . LEU B 1 16  ? 5.443   -4.988  71.866  1.00 108.64 ?  25  LEU B CD2  1 
ATOM   5894  H H    . LEU B 1 16  ? 9.412   -2.588  71.090  1.00 112.28 ?  25  LEU B H    1 
ATOM   5895  H HA   . LEU B 1 16  ? 8.838   -4.682  69.541  1.00 105.70 ?  25  LEU B HA   1 
ATOM   5896  H HB2  . LEU B 1 16  ? 7.940   -4.334  71.727  1.00 86.20  ?  25  LEU B HB2  1 
ATOM   5897  H HB3  . LEU B 1 16  ? 7.076   -3.159  71.117  1.00 86.20  ?  25  LEU B HB3  1 
ATOM   5898  H HG   . LEU B 1 16  ? 5.872   -4.700  69.861  1.00 94.68  ?  25  LEU B HG   1 
ATOM   5899  H HD11 . LEU B 1 16  ? 6.181   -6.960  70.213  1.00 88.94  ?  25  LEU B HD11 1 
ATOM   5900  H HD12 . LEU B 1 16  ? 7.518   -6.325  69.636  1.00 88.94  ?  25  LEU B HD12 1 
ATOM   5901  H HD13 . LEU B 1 16  ? 7.397   -6.649  71.187  1.00 88.94  ?  25  LEU B HD13 1 
ATOM   5902  H HD21 . LEU B 1 16  ? 4.713   -5.606  71.707  1.00 130.36 ?  25  LEU B HD21 1 
ATOM   5903  H HD22 . LEU B 1 16  ? 5.949   -5.265  72.645  1.00 130.36 ?  25  LEU B HD22 1 
ATOM   5904  H HD23 . LEU B 1 16  ? 5.096   -4.092  71.998  1.00 130.36 ?  25  LEU B HD23 1 
ATOM   5905  N N    . PRO B 1 17  ? 7.900   -3.625  67.462  1.00 122.96 ?  26  PRO B N    1 
ATOM   5906  C CA   . PRO B 1 17  ? 7.525   -2.813  66.300  1.00 119.93 ?  26  PRO B CA   1 
ATOM   5907  C C    . PRO B 1 17  ? 6.016   -2.621  66.220  1.00 146.43 ?  26  PRO B C    1 
ATOM   5908  O O    . PRO B 1 17  ? 5.250   -3.582  66.327  1.00 180.40 ?  26  PRO B O    1 
ATOM   5909  C CB   . PRO B 1 17  ? 8.063   -3.620  65.119  1.00 108.83 ?  26  PRO B CB   1 
ATOM   5910  C CG   . PRO B 1 17  ? 8.081   -5.026  65.616  1.00 82.52  ?  26  PRO B CG   1 
ATOM   5911  C CD   . PRO B 1 17  ? 8.320   -4.979  67.080  1.00 80.99  ?  26  PRO B CD   1 
ATOM   5912  H HA   . PRO B 1 17  ? 7.963   -1.948  66.331  1.00 143.92 ?  26  PRO B HA   1 
ATOM   5913  H HB2  . PRO B 1 17  ? 7.467   -3.529  64.358  1.00 130.60 ?  26  PRO B HB2  1 
ATOM   5914  H HB3  . PRO B 1 17  ? 8.958   -3.321  64.895  1.00 130.60 ?  26  PRO B HB3  1 
ATOM   5915  H HG2  . PRO B 1 17  ? 7.225   -5.442  65.429  1.00 99.02  ?  26  PRO B HG2  1 
ATOM   5916  H HG3  . PRO B 1 17  ? 8.794   -5.513  65.175  1.00 99.02  ?  26  PRO B HG3  1 
ATOM   5917  H HD2  . PRO B 1 17  ? 7.774   -5.641  67.532  1.00 97.19  ?  26  PRO B HD2  1 
ATOM   5918  H HD3  . PRO B 1 17  ? 9.262   -5.106  67.272  1.00 97.19  ?  26  PRO B HD3  1 
ATOM   5919  N N    . ASN B 1 18  ? 5.594   -1.361  66.023  1.00 173.40 ?  27  ASN B N    1 
ATOM   5920  C CA   . ASN B 1 18  ? 4.184   -0.979  65.980  1.00 145.08 ?  27  ASN B CA   1 
ATOM   5921  C C    . ASN B 1 18  ? 3.410   -1.721  67.068  1.00 127.25 ?  27  ASN B C    1 
ATOM   5922  O O    . ASN B 1 18  ? 2.646   -2.643  66.767  1.00 145.02 ?  27  ASN B O    1 
ATOM   5923  C CB   . ASN B 1 18  ? 3.597   -1.253  64.589  1.00 152.67 ?  27  ASN B CB   1 
ATOM   5924  C CG   . ASN B 1 18  ? 4.221   -0.377  63.503  1.00 129.04 ?  27  ASN B CG   1 
ATOM   5925  H H    . ASN B 1 18  ? 6.127   -0.696  65.909  1.00 208.08 ?  27  ASN B H    1 
ATOM   5926  H HA   . ASN B 1 18  ? 4.109   -0.027  66.155  1.00 174.09 ?  27  ASN B HA   1 
ATOM   5927  H HB2  . ASN B 1 18  ? 3.757   -2.181  64.355  1.00 183.20 ?  27  ASN B HB2  1 
ATOM   5928  H HB3  . ASN B 1 18  ? 2.643   -1.076  64.607  1.00 183.20 ?  27  ASN B HB3  1 
ATOM   5929  N N    . PRO B 1 19  ? 3.591   -1.362  68.337  1.00 93.88  ?  28  PRO B N    1 
ATOM   5930  C CA   . PRO B 1 19  ? 2.883   -2.048  69.418  1.00 97.41  ?  28  PRO B CA   1 
ATOM   5931  C C    . PRO B 1 19  ? 1.412   -1.677  69.491  1.00 92.98  ?  28  PRO B C    1 
ATOM   5932  O O    . PRO B 1 19  ? 1.001   -0.540  69.242  1.00 102.48 ?  28  PRO B O    1 
ATOM   5933  C CB   . PRO B 1 19  ? 3.632   -1.582  70.670  1.00 165.61 ?  28  PRO B CB   1 
ATOM   5934  C CG   . PRO B 1 19  ? 4.084   -0.224  70.327  1.00 115.54 ?  28  PRO B CG   1 
ATOM   5935  C CD   . PRO B 1 19  ? 4.361   -0.224  68.849  1.00 78.19  ?  28  PRO B CD   1 
ATOM   5936  H HA   . PRO B 1 19  ? 2.972   -3.009  69.327  1.00 116.89 ?  28  PRO B HA   1 
ATOM   5937  H HB2  . PRO B 1 19  ? 3.028   -1.564  71.429  1.00 198.74 ?  28  PRO B HB2  1 
ATOM   5938  H HB3  . PRO B 1 19  ? 4.387   -2.166  70.840  1.00 198.74 ?  28  PRO B HB3  1 
ATOM   5939  H HG2  . PRO B 1 19  ? 3.384   0.412   70.540  1.00 138.64 ?  28  PRO B HG2  1 
ATOM   5940  H HG3  . PRO B 1 19  ? 4.892   -0.018  70.823  1.00 138.64 ?  28  PRO B HG3  1 
ATOM   5941  H HD2  . PRO B 1 19  ? 4.047   0.602   68.448  1.00 93.83  ?  28  PRO B HD2  1 
ATOM   5942  H HD3  . PRO B 1 19  ? 5.308   -0.359  68.684  1.00 93.83  ?  28  PRO B HD3  1 
ATOM   5943  N N    . GLN B 1 20  ? 0.629   -2.653  69.914  1.00 102.22 ?  29  GLN B N    1 
ATOM   5944  C CA   . GLN B 1 20  ? -0.810  -2.501  69.876  1.00 134.44 ?  29  GLN B CA   1 
ATOM   5945  C C    . GLN B 1 20  ? -1.241  -1.415  70.849  1.00 134.25 ?  29  GLN B C    1 
ATOM   5946  O O    . GLN B 1 20  ? -0.614  -1.194  71.885  1.00 101.19 ?  29  GLN B O    1 
ATOM   5947  C CB   . GLN B 1 20  ? -1.495  -3.836  70.174  1.00 162.31 ?  29  GLN B CB   1 
ATOM   5948  C CG   . GLN B 1 20  ? -2.973  -3.875  69.765  1.00 171.80 ?  29  GLN B CG   1 
ATOM   5949  C CD   . GLN B 1 20  ? -3.459  -5.290  69.488  1.00 163.53 ?  29  GLN B CD   1 
ATOM   5950  O OE1  . GLN B 1 20  ? -2.685  -6.142  69.050  1.00 165.87 ?  29  GLN B OE1  1 
ATOM   5951  N NE2  . GLN B 1 20  ? -4.749  -5.544  69.724  1.00 184.93 ?  29  GLN B NE2  1 
ATOM   5952  H H    . GLN B 1 20  ? 0.903   -3.407  70.225  1.00 122.66 ?  29  GLN B H    1 
ATOM   5953  H HA   . GLN B 1 20  ? -1.073  -2.224  68.984  1.00 161.33 ?  29  GLN B HA   1 
ATOM   5954  H HB2  . GLN B 1 20  ? -1.034  -4.540  69.691  1.00 194.77 ?  29  GLN B HB2  1 
ATOM   5955  H HB3  . GLN B 1 20  ? -1.447  -4.007  71.128  1.00 194.77 ?  29  GLN B HB3  1 
ATOM   5956  H HG2  . GLN B 1 20  ? -3.511  -3.507  70.483  1.00 206.16 ?  29  GLN B HG2  1 
ATOM   5957  H HG3  . GLN B 1 20  ? -3.092  -3.352  68.957  1.00 206.16 ?  29  GLN B HG3  1 
ATOM   5958  H HE21 . GLN B 1 20  ? -5.263  -4.921  70.019  1.00 221.92 ?  29  GLN B HE21 1 
ATOM   5959  H HE22 . GLN B 1 20  ? -5.065  -6.331  69.581  1.00 221.92 ?  29  GLN B HE22 1 
ATOM   5960  N N    . GLU B 1 21  ? -2.248  -0.653  70.442  1.00 141.98 ?  30  GLU B N    1 
ATOM   5961  C CA   . GLU B 1 21  ? -2.785  0.400   71.285  1.00 145.20 ?  30  GLU B CA   1 
ATOM   5962  C C    . GLU B 1 21  ? -3.979  -0.044  72.126  1.00 126.36 ?  30  GLU B C    1 
ATOM   5963  O O    . GLU B 1 21  ? -4.297  0.638   73.109  1.00 100.01 ?  30  GLU B O    1 
ATOM   5964  C CB   . GLU B 1 21  ? -3.212  1.591   70.422  1.00 160.63 ?  30  GLU B CB   1 
ATOM   5965  C CG   . GLU B 1 21  ? -2.103  2.221   69.589  1.00 124.05 ?  30  GLU B CG   1 
ATOM   5966  H H    . GLU B 1 21  ? -2.638  -0.728  69.679  1.00 170.38 ?  30  GLU B H    1 
ATOM   5967  H HA   . GLU B 1 21  ? -2.090  0.703   71.890  1.00 174.24 ?  30  GLU B HA   1 
ATOM   5968  H HB2  . GLU B 1 21  ? -3.904  1.295   69.810  1.00 192.75 ?  30  GLU B HB2  1 
ATOM   5969  H HB3  . GLU B 1 21  ? -3.568  2.281   71.004  1.00 192.75 ?  30  GLU B HB3  1 
ATOM   5970  H HG2  . GLU B 1 21  ? -1.429  2.585   70.184  1.00 148.86 ?  30  GLU B HG2  1 
ATOM   5971  H HG3  . GLU B 1 21  ? -1.710  1.541   69.020  1.00 148.86 ?  30  GLU B HG3  1 
ATOM   5972  N N    . ASN B 1 22  ? -4.671  -1.135  71.748  1.00 128.16 ?  31  ASN B N    1 
ATOM   5973  C CA   . ASN B 1 22  ? -5.923  -1.543  72.393  1.00 124.56 ?  31  ASN B CA   1 
ATOM   5974  C C    . ASN B 1 22  ? -6.045  -3.058  72.530  1.00 114.04 ?  31  ASN B C    1 
ATOM   5975  O O    . ASN B 1 22  ? -5.718  -3.801  71.603  1.00 106.49 ?  31  ASN B O    1 
ATOM   5976  C CB   . ASN B 1 22  ? -7.158  -1.030  71.621  1.00 124.58 ?  31  ASN B CB   1 
ATOM   5977  C CG   . ASN B 1 22  ? -7.270  0.470   71.625  1.00 118.93 ?  31  ASN B CG   1 
ATOM   5978  O OD1  . ASN B 1 22  ? -7.603  1.078   72.647  1.00 118.17 ?  31  ASN B OD1  1 
ATOM   5979  N ND2  . ASN B 1 22  ? -6.933  1.087   70.481  1.00 134.22 ?  31  ASN B ND2  1 
ATOM   5980  H H    . ASN B 1 22  ? -4.426  -1.659  71.112  1.00 153.79 ?  31  ASN B H    1 
ATOM   5981  H HA   . ASN B 1 22  ? -5.953  -1.162  73.284  1.00 149.48 ?  31  ASN B HA   1 
ATOM   5982  H HB2  . ASN B 1 22  ? -7.097  -1.324  70.699  1.00 149.49 ?  31  ASN B HB2  1 
ATOM   5983  H HB3  . ASN B 1 22  ? -7.959  -1.391  72.032  1.00 149.49 ?  31  ASN B HB3  1 
ATOM   5984  H HD21 . ASN B 1 22  ? -6.978  1.944   70.425  1.00 161.06 ?  31  ASN B HD21 1 
ATOM   5985  H HD22 . ASN B 1 22  ? -6.673  0.625   69.804  1.00 161.06 ?  31  ASN B HD22 1 
ATOM   5986  N N    . LEU B 1 23  ? -6.504  -3.509  73.715  1.00 117.73 ?  32  LEU B N    1 
ATOM   5987  C CA   . LEU B 1 23  ? -6.905  -4.886  73.983  1.00 120.52 ?  32  LEU B CA   1 
ATOM   5988  C C    . LEU B 1 23  ? -8.375  -5.139  73.626  1.00 151.85 ?  32  LEU B C    1 
ATOM   5989  O O    . LEU B 1 23  ? -9.204  -4.220  73.566  1.00 134.33 ?  32  LEU B O    1 
ATOM   5990  C CB   . LEU B 1 23  ? -6.642  -5.230  75.452  1.00 112.37 ?  32  LEU B CB   1 
ATOM   5991  H H    . LEU B 1 23  ? -6.590  -3.002  74.404  1.00 141.27 ?  32  LEU B H    1 
ATOM   5992  H HA   . LEU B 1 23  ? -6.363  -5.479  73.439  1.00 144.63 ?  32  LEU B HA   1 
ATOM   5993  N N    . PRO B 1 24  ? -8.723  -6.388  73.416  1.00 126.08 ?  33  PRO B N    1 
ATOM   5994  C CA   . PRO B 1 24  ? -10.118 -6.750  73.176  1.00 128.72 ?  33  PRO B CA   1 
ATOM   5995  C C    . PRO B 1 24  ? -11.112 -6.114  74.128  1.00 156.15 ?  33  PRO B C    1 
ATOM   5996  O O    . PRO B 1 24  ? -10.765 -5.715  75.242  1.00 167.28 ?  33  PRO B O    1 
ATOM   5997  C CB   . PRO B 1 24  ? -10.100 -8.268  73.361  1.00 107.97 ?  33  PRO B CB   1 
ATOM   5998  C CG   . PRO B 1 24  ? -8.773  -8.686  73.068  1.00 163.37 ?  33  PRO B CG   1 
ATOM   5999  C CD   . PRO B 1 24  ? -7.859  -7.574  73.450  1.00 174.97 ?  33  PRO B CD   1 
ATOM   6000  H HA   . PRO B 1 24  ? -10.368 -6.541  72.262  1.00 154.46 ?  33  PRO B HA   1 
ATOM   6001  H HB2  . PRO B 1 24  ? -10.330 -8.485  74.278  1.00 129.56 ?  33  PRO B HB2  1 
ATOM   6002  H HB3  . PRO B 1 24  ? -10.729 -8.677  72.747  1.00 129.56 ?  33  PRO B HB3  1 
ATOM   6003  H HG2  . PRO B 1 24  ? -8.567  -9.482  73.584  1.00 196.05 ?  33  PRO B HG2  1 
ATOM   6004  H HG3  . PRO B 1 24  ? -8.698  -8.872  72.119  1.00 196.05 ?  33  PRO B HG3  1 
ATOM   6005  H HD2  . PRO B 1 24  ? -7.513  -7.714  74.345  1.00 209.96 ?  33  PRO B HD2  1 
ATOM   6006  H HD3  . PRO B 1 24  ? -7.143  -7.489  72.801  1.00 209.96 ?  33  PRO B HD3  1 
ATOM   6007  N N    . ASP B 1 25  ? -12.365 -6.010  73.692  1.00 159.45 ?  34  ASP B N    1 
ATOM   6008  C CA   . ASP B 1 25  ? -13.359 -5.424  74.563  1.00 142.94 ?  34  ASP B CA   1 
ATOM   6009  C C    . ASP B 1 25  ? -13.456 -6.204  75.856  1.00 128.49 ?  34  ASP B C    1 
ATOM   6010  O O    . ASP B 1 25  ? -13.821 -5.632  76.880  1.00 122.12 ?  34  ASP B O    1 
ATOM   6011  C CB   . ASP B 1 25  ? -14.713 -5.419  73.852  1.00 175.78 ?  34  ASP B CB   1 
ATOM   6012  C CG   . ASP B 1 25  ? -14.784 -4.408  72.740  1.00 156.77 ?  34  ASP B CG   1 
ATOM   6013  O OD1  . ASP B 1 25  ? -14.046 -3.406  72.813  1.00 134.82 ?  34  ASP B OD1  1 
ATOM   6014  O OD2  . ASP B 1 25  ? -15.565 -4.628  71.789  1.00 160.71 -1 34  ASP B OD2  1 
ATOM   6015  H H    . ASP B 1 25  ? -12.652 -6.263  72.922  1.00 191.35 ?  34  ASP B H    1 
ATOM   6016  H HA   . ASP B 1 25  ? -13.113 -4.509  74.770  1.00 171.52 ?  34  ASP B HA   1 
ATOM   6017  H HB2  . ASP B 1 25  ? -14.872 -6.296  73.470  1.00 210.94 ?  34  ASP B HB2  1 
ATOM   6018  H HB3  . ASP B 1 25  ? -15.406 -5.206  74.495  1.00 210.94 ?  34  ASP B HB3  1 
ATOM   6019  N N    . PHE B 1 26  ? -13.011 -7.457  75.859  1.00 122.16 ?  35  PHE B N    1 
ATOM   6020  C CA   . PHE B 1 26  ? -13.102 -8.273  77.063  1.00 213.61 ?  35  PHE B CA   1 
ATOM   6021  C C    . PHE B 1 26  ? -12.444 -7.592  78.255  1.00 145.37 ?  35  PHE B C    1 
ATOM   6022  O O    . PHE B 1 26  ? -12.864 -7.786  79.401  1.00 111.57 ?  35  PHE B O    1 
ATOM   6023  C CB   . PHE B 1 26  ? -12.466 -9.633  76.799  1.00 116.22 ?  35  PHE B CB   1 
ATOM   6024  C CG   . PHE B 1 26  ? -12.699 -10.640 77.890  1.00 144.76 ?  35  PHE B CG   1 
ATOM   6025  C CD1  . PHE B 1 26  ? -13.842 -11.437 77.876  1.00 119.98 ?  35  PHE B CD1  1 
ATOM   6026  C CD2  . PHE B 1 26  ? -11.802 -10.794 78.930  1.00 113.52 ?  35  PHE B CD2  1 
ATOM   6027  C CE1  . PHE B 1 26  ? -14.084 -12.380 78.882  1.00 120.43 ?  35  PHE B CE1  1 
ATOM   6028  C CE2  . PHE B 1 26  ? -12.032 -11.739 79.942  1.00 144.73 ?  35  PHE B CE2  1 
ATOM   6029  C CZ   . PHE B 1 26  ? -13.176 -12.539 79.912  1.00 117.28 ?  35  PHE B CZ   1 
ATOM   6030  H H    . PHE B 1 26  ? -12.657 -7.855  75.184  1.00 146.59 ?  35  PHE B H    1 
ATOM   6031  H HA   . PHE B 1 26  ? -14.037 -8.416  77.278  1.00 256.33 ?  35  PHE B HA   1 
ATOM   6032  H HB2  . PHE B 1 26  ? -12.834 -9.995  75.978  1.00 139.46 ?  35  PHE B HB2  1 
ATOM   6033  H HB3  . PHE B 1 26  ? -11.508 -9.516  76.705  1.00 139.46 ?  35  PHE B HB3  1 
ATOM   6034  H HD1  . PHE B 1 26  ? -14.456 -11.342 77.183  1.00 143.97 ?  35  PHE B HD1  1 
ATOM   6035  H HD2  . PHE B 1 26  ? -11.034 -10.271 78.955  1.00 136.23 ?  35  PHE B HD2  1 
ATOM   6036  H HE1  . PHE B 1 26  ? -14.850 -12.906 78.852  1.00 144.52 ?  35  PHE B HE1  1 
ATOM   6037  H HE2  . PHE B 1 26  ? -11.417 -11.836 80.634  1.00 173.68 ?  35  PHE B HE2  1 
ATOM   6038  H HZ   . PHE B 1 26  ? -13.332 -13.161 80.585  1.00 140.73 ?  35  PHE B HZ   1 
ATOM   6039  N N    . TYR B 1 27  ? -11.370 -6.851  78.018  1.00 167.43 ?  36  TYR B N    1 
ATOM   6040  C CA   . TYR B 1 27  ? -10.584 -6.260  79.091  1.00 149.38 ?  36  TYR B CA   1 
ATOM   6041  C C    . TYR B 1 27  ? -10.923 -4.808  79.318  1.00 229.43 ?  36  TYR B C    1 
ATOM   6042  O O    . TYR B 1 27  ? -10.121 -4.071  79.897  1.00 213.88 ?  36  TYR B O    1 
ATOM   6043  C CB   . TYR B 1 27  ? -9.103  -6.421  78.782  1.00 116.04 ?  36  TYR B CB   1 
ATOM   6044  C CG   . TYR B 1 27  ? -8.759  -7.856  78.707  1.00 115.67 ?  36  TYR B CG   1 
ATOM   6045  C CD1  . TYR B 1 27  ? -8.641  -8.597  79.865  1.00 104.33 ?  36  TYR B CD1  1 
ATOM   6046  C CD2  . TYR B 1 27  ? -8.631  -8.497  77.480  1.00 126.93 ?  36  TYR B CD2  1 
ATOM   6047  C CE1  . TYR B 1 27  ? -8.345  -9.934  79.821  1.00 105.34 ?  36  TYR B CE1  1 
ATOM   6048  C CE2  . TYR B 1 27  ? -8.350  -9.847  77.410  1.00 127.80 ?  36  TYR B CE2  1 
ATOM   6049  C CZ   . TYR B 1 27  ? -8.211  -10.574 78.589  1.00 107.55 ?  36  TYR B CZ   1 
ATOM   6050  O OH   . TYR B 1 27  ? -7.939  -11.936 78.548  1.00 119.00 ?  36  TYR B OH   1 
ATOM   6051  H H    . TYR B 1 27  ? -11.071 -6.674  77.232  1.00 200.91 ?  36  TYR B H    1 
ATOM   6052  H HA   . TYR B 1 27  ? -10.769 -6.740  79.913  1.00 179.26 ?  36  TYR B HA   1 
ATOM   6053  H HB2  . TYR B 1 27  ? -8.902  -6.010  77.927  1.00 139.24 ?  36  TYR B HB2  1 
ATOM   6054  H HB3  . TYR B 1 27  ? -8.577  -6.014  79.489  1.00 139.24 ?  36  TYR B HB3  1 
ATOM   6055  H HD1  . TYR B 1 27  ? -8.732  -8.176  80.689  1.00 125.19 ?  36  TYR B HD1  1 
ATOM   6056  H HD2  . TYR B 1 27  ? -8.728  -8.008  76.695  1.00 152.32 ?  36  TYR B HD2  1 
ATOM   6057  H HE1  . TYR B 1 27  ? -8.263  -10.420 80.609  1.00 126.40 ?  36  TYR B HE1  1 
ATOM   6058  H HE2  . TYR B 1 27  ? -8.257  -10.266 76.585  1.00 153.36 ?  36  TYR B HE2  1 
ATOM   6059  H HH   . TYR B 1 27  ? -7.883  -12.241 79.329  1.00 142.80 ?  36  TYR B HH   1 
ATOM   6060  N N    . ASN B 1 28  ? -12.109 -4.387  78.918  1.00 214.38 ?  37  ASN B N    1 
ATOM   6061  C CA   . ASN B 1 28  ? -12.413 -2.977  79.025  1.00 162.55 ?  37  ASN B CA   1 
ATOM   6062  C C    . ASN B 1 28  ? -12.327 -2.480  80.461  1.00 136.16 ?  37  ASN B C    1 
ATOM   6063  O O    . ASN B 1 28  ? -12.262 -1.264  80.663  1.00 113.99 ?  37  ASN B O    1 
ATOM   6064  C CB   . ASN B 1 28  ? -13.765 -2.716  78.398  1.00 144.26 ?  37  ASN B CB   1 
ATOM   6065  C CG   . ASN B 1 28  ? -13.723 -2.822  76.887  1.00 170.90 ?  37  ASN B CG   1 
ATOM   6066  O OD1  . ASN B 1 28  ? -12.660 -2.745  76.278  1.00 182.93 ?  37  ASN B OD1  1 
ATOM   6067  N ND2  . ASN B 1 28  ? -14.881 -3.008  76.277  1.00 185.10 ?  37  ASN B ND2  1 
ATOM   6068  H H    . ASN B 1 28  ? -12.735 -4.878  78.593  1.00 257.26 ?  37  ASN B H    1 
ATOM   6069  H HA   . ASN B 1 28  ? -11.756 -2.483  78.510  1.00 195.06 ?  37  ASN B HA   1 
ATOM   6070  H HB2  . ASN B 1 28  ? -14.401 -3.370  78.729  1.00 173.11 ?  37  ASN B HB2  1 
ATOM   6071  H HB3  . ASN B 1 28  ? -14.056 -1.820  78.630  1.00 173.11 ?  37  ASN B HB3  1 
ATOM   6072  H HD21 . ASN B 1 28  ? -14.910 -3.074  75.420  1.00 222.12 ?  37  ASN B HD21 1 
ATOM   6073  H HD22 . ASN B 1 28  ? -15.606 -3.062  76.737  1.00 222.12 ?  37  ASN B HD22 1 
ATOM   6074  N N    . ASP B 1 29  ? -12.350 -3.373  81.463  1.00 125.66 ?  38  ASP B N    1 
ATOM   6075  C CA   . ASP B 1 29  ? -12.183 -2.911  82.844  1.00 168.59 ?  38  ASP B CA   1 
ATOM   6076  C C    . ASP B 1 29  ? -10.731 -2.647  83.179  1.00 120.99 ?  38  ASP B C    1 
ATOM   6077  O O    . ASP B 1 29  ? -10.438 -1.700  83.912  1.00 118.62 ?  38  ASP B O    1 
ATOM   6078  C CB   . ASP B 1 29  ? -12.731 -3.909  83.867  1.00 136.82 ?  38  ASP B CB   1 
ATOM   6079  C CG   . ASP B 1 29  ? -14.205 -3.699  84.189  1.00 123.70 ?  38  ASP B CG   1 
ATOM   6080  O OD1  . ASP B 1 29  ? -14.693 -2.570  83.989  1.00 115.27 ?  38  ASP B OD1  1 
ATOM   6081  O OD2  . ASP B 1 29  ? -14.855 -4.630  84.706  1.00 184.60 -1 38  ASP B OD2  1 
ATOM   6082  H H    . ASP B 1 29  ? -12.457 -4.221  81.372  1.00 150.79 ?  38  ASP B H    1 
ATOM   6083  H HA   . ASP B 1 29  ? -12.668 -2.079  82.954  1.00 202.31 ?  38  ASP B HA   1 
ATOM   6084  H HB2  . ASP B 1 29  ? -12.628 -4.807  83.515  1.00 164.18 ?  38  ASP B HB2  1 
ATOM   6085  H HB3  . ASP B 1 29  ? -12.230 -3.819  84.692  1.00 164.18 ?  38  ASP B HB3  1 
ATOM   6086  N N    . TRP B 1 30  ? -9.814  -3.474  82.671  1.00 139.18 ?  39  TRP B N    1 
ATOM   6087  C CA   . TRP B 1 30  ? -8.392  -3.176  82.830  1.00 133.37 ?  39  TRP B CA   1 
ATOM   6088  C C    . TRP B 1 30  ? -8.047  -1.933  82.035  1.00 166.37 ?  39  TRP B C    1 
ATOM   6089  O O    . TRP B 1 30  ? -7.466  -0.982  82.557  1.00 139.06 ?  39  TRP B O    1 
ATOM   6090  C CB   . TRP B 1 30  ? -7.515  -4.339  82.352  1.00 110.71 ?  39  TRP B CB   1 
ATOM   6091  C CG   . TRP B 1 30  ? -7.530  -5.638  83.165  1.00 96.78  ?  39  TRP B CG   1 
ATOM   6092  C CD1  . TRP B 1 30  ? -8.197  -5.872  84.313  1.00 99.39  ?  39  TRP B CD1  1 
ATOM   6093  C CD2  . TRP B 1 30  ? -6.823  -6.861  82.861  1.00 96.86  ?  39  TRP B CD2  1 
ATOM   6094  N NE1  . TRP B 1 30  ? -7.981  -7.158  84.751  1.00 101.07 ?  39  TRP B NE1  1 
ATOM   6095  C CE2  . TRP B 1 30  ? -7.134  -7.784  83.880  1.00 100.68 ?  39  TRP B CE2  1 
ATOM   6096  C CE3  . TRP B 1 30  ? -5.946  -7.261  81.829  1.00 97.07  ?  39  TRP B CE3  1 
ATOM   6097  C CZ2  . TRP B 1 30  ? -6.602  -9.083  83.906  1.00 128.48 ?  39  TRP B CZ2  1 
ATOM   6098  C CZ3  . TRP B 1 30  ? -5.426  -8.556  81.859  1.00 97.44  ?  39  TRP B CZ3  1 
ATOM   6099  C CH2  . TRP B 1 30  ? -5.747  -9.444  82.890  1.00 101.16 ?  39  TRP B CH2  1 
ATOM   6100  H H    . TRP B 1 30  ? -9.985  -4.199  82.240  1.00 167.02 ?  39  TRP B H    1 
ATOM   6101  H HA   . TRP B 1 30  ? -8.198  -3.008  83.765  1.00 160.05 ?  39  TRP B HA   1 
ATOM   6102  H HB2  . TRP B 1 30  ? -7.791  -4.569  81.450  1.00 132.85 ?  39  TRP B HB2  1 
ATOM   6103  H HB3  . TRP B 1 30  ? -6.596  -4.030  82.332  1.00 132.85 ?  39  TRP B HB3  1 
ATOM   6104  H HD1  . TRP B 1 30  ? -8.752  -5.257  84.735  1.00 119.27 ?  39  TRP B HD1  1 
ATOM   6105  H HE1  . TRP B 1 30  ? -8.314  -7.507  85.463  1.00 121.28 ?  39  TRP B HE1  1 
ATOM   6106  H HE3  . TRP B 1 30  ? -5.721  -6.675  81.143  1.00 116.48 ?  39  TRP B HE3  1 
ATOM   6107  H HZ2  . TRP B 1 30  ? -6.817  -9.678  84.588  1.00 154.18 ?  39  TRP B HZ2  1 
ATOM   6108  H HZ3  . TRP B 1 30  ? -4.851  -8.832  81.182  1.00 116.92 ?  39  TRP B HZ3  1 
ATOM   6109  H HH2  . TRP B 1 30  ? -5.392  -10.303 82.878  1.00 121.39 ?  39  TRP B HH2  1 
ATOM   6110  N N    . MET B 1 31  ? -8.466  -1.907  80.776  1.00 269.30 ?  40  MET B N    1 
ATOM   6111  C CA   . MET B 1 31  ? -8.121  -0.812  79.888  1.00 107.98 ?  40  MET B CA   1 
ATOM   6112  C C    . MET B 1 31  ? -8.523  0.525   80.494  1.00 172.01 ?  40  MET B C    1 
ATOM   6113  O O    . MET B 1 31  ? -7.909  1.560   80.219  1.00 96.45  ?  40  MET B O    1 
ATOM   6114  C CB   . MET B 1 31  ? -8.837  -1.034  78.558  1.00 186.17 ?  40  MET B CB   1 
ATOM   6115  C CG   . MET B 1 31  ? -8.285  -0.314  77.344  1.00 246.80 ?  40  MET B CG   1 
ATOM   6116  S SD   . MET B 1 31  ? -6.797  -1.111  76.702  1.00 177.61 ?  40  MET B SD   1 
ATOM   6117  C CE   . MET B 1 31  ? -5.578  0.116   77.044  1.00 96.92  ?  40  MET B CE   1 
ATOM   6118  H H    . MET B 1 31  ? -8.953  -2.515  80.412  1.00 323.16 ?  40  MET B H    1 
ATOM   6119  H HA   . MET B 1 31  ? -7.164  -0.818  79.727  1.00 129.58 ?  40  MET B HA   1 
ATOM   6120  H HB2  . MET B 1 31  ? -8.815  -1.983  78.359  1.00 223.40 ?  40  MET B HB2  1 
ATOM   6121  H HB3  . MET B 1 31  ? -9.759  -0.752  78.662  1.00 223.40 ?  40  MET B HB3  1 
ATOM   6122  H HG2  . MET B 1 31  ? -8.955  -0.314  76.642  1.00 296.16 ?  40  MET B HG2  1 
ATOM   6123  H HG3  . MET B 1 31  ? -8.058  0.597   77.590  1.00 296.16 ?  40  MET B HG3  1 
ATOM   6124  H HE1  . MET B 1 31  ? -4.715  -0.203  76.738  1.00 116.30 ?  40  MET B HE1  1 
ATOM   6125  H HE2  . MET B 1 31  ? -5.814  0.933   76.577  1.00 116.30 ?  40  MET B HE2  1 
ATOM   6126  H HE3  . MET B 1 31  ? -5.552  0.277   78.000  1.00 116.30 ?  40  MET B HE3  1 
ATOM   6127  N N    . PHE B 1 32  ? -9.596  0.543   81.273  1.00 142.43 ?  41  PHE B N    1 
ATOM   6128  C CA   . PHE B 1 32  ? -10.087 1.822   81.765  1.00 127.04 ?  41  PHE B CA   1 
ATOM   6129  C C    . PHE B 1 32  ? -9.175  2.384   82.841  1.00 145.97 ?  41  PHE B C    1 
ATOM   6130  O O    . PHE B 1 32  ? -8.733  3.534   82.757  1.00 95.96  ?  41  PHE B O    1 
ATOM   6131  C CB   . PHE B 1 32  ? -11.514 1.671   82.285  1.00 103.18 ?  41  PHE B CB   1 
ATOM   6132  H H    . PHE B 1 32  ? -10.045 -0.146  81.525  1.00 170.92 ?  41  PHE B H    1 
ATOM   6133  H HA   . PHE B 1 32  ? -10.104 2.455   81.030  1.00 152.45 ?  41  PHE B HA   1 
ATOM   6134  N N    . ILE B 1 33  ? -8.821  1.561   83.819  1.00 198.75 ?  42  ILE B N    1 
ATOM   6135  C CA   . ILE B 1 33  ? -8.063  2.058   84.961  1.00 216.26 ?  42  ILE B CA   1 
ATOM   6136  C C    . ILE B 1 33  ? -6.709  2.575   84.508  1.00 128.67 ?  42  ILE B C    1 
ATOM   6137  O O    . ILE B 1 33  ? -6.296  3.692   84.843  1.00 170.68 ?  42  ILE B O    1 
ATOM   6138  C CB   . ILE B 1 33  ? -7.912  0.944   86.010  1.00 167.73 ?  42  ILE B CB   1 
ATOM   6139  C CG1  . ILE B 1 33  ? -9.281  0.550   86.571  1.00 164.47 ?  42  ILE B CG1  1 
ATOM   6140  C CG2  . ILE B 1 33  ? -6.956  1.367   87.128  1.00 179.13 ?  42  ILE B CG2  1 
ATOM   6141  C CD1  . ILE B 1 33  ? -9.251  -0.719  87.423  1.00 95.19  ?  42  ILE B CD1  1 
ATOM   6142  H H    . ILE B 1 33  ? -9.005  0.722   83.848  1.00 238.50 ?  42  ILE B H    1 
ATOM   6143  H HA   . ILE B 1 33  ? -8.546  2.794   85.368  1.00 259.51 ?  42  ILE B HA   1 
ATOM   6144  H HB   . ILE B 1 33  ? -7.533  0.167   85.569  1.00 201.27 ?  42  ILE B HB   1 
ATOM   6145  H HG12 . ILE B 1 33  ? -9.611  1.274   87.126  1.00 197.36 ?  42  ILE B HG12 1 
ATOM   6146  H HG13 . ILE B 1 33  ? -9.890  0.398   85.831  1.00 197.36 ?  42  ILE B HG13 1 
ATOM   6147  H HG21 . ILE B 1 33  ? -6.884  0.644   87.771  1.00 214.96 ?  42  ILE B HG21 1 
ATOM   6148  H HG22 . ILE B 1 33  ? -6.086  1.557   86.744  1.00 214.96 ?  42  ILE B HG22 1 
ATOM   6149  H HG23 . ILE B 1 33  ? -7.308  2.160   87.561  1.00 214.96 ?  42  ILE B HG23 1 
ATOM   6150  H HD11 . ILE B 1 33  ? -10.148 -0.906  87.742  1.00 114.23 ?  42  ILE B HD11 1 
ATOM   6151  H HD12 . ILE B 1 33  ? -8.933  -1.457  86.879  1.00 114.23 ?  42  ILE B HD12 1 
ATOM   6152  H HD13 . ILE B 1 33  ? -8.654  -0.580  88.175  1.00 114.23 ?  42  ILE B HD13 1 
ATOM   6153  N N    . ALA B 1 34  ? -6.011  1.782   83.709  1.00 118.03 ?  43  ALA B N    1 
ATOM   6154  C CA   . ALA B 1 34  ? -4.665  2.157   83.320  1.00 94.22  ?  43  ALA B CA   1 
ATOM   6155  C C    . ALA B 1 34  ? -4.660  3.470   82.590  1.00 105.71 ?  43  ALA B C    1 
ATOM   6156  O O    . ALA B 1 34  ? -3.671  4.207   82.653  1.00 90.28  ?  43  ALA B O    1 
ATOM   6157  C CB   . ALA B 1 34  ? -4.058  1.079   82.439  1.00 100.82 ?  43  ALA B CB   1 
ATOM   6158  H H    . ALA B 1 34  ? -6.288  1.035   83.385  1.00 141.64 ?  43  ALA B H    1 
ATOM   6159  H HA   . ALA B 1 34  ? -4.115  2.247   84.114  1.00 113.06 ?  43  ALA B HA   1 
ATOM   6160  H HB1  . ALA B 1 34  ? -3.159  1.345   82.188  1.00 120.98 ?  43  ALA B HB1  1 
ATOM   6161  H HB2  . ALA B 1 34  ? -4.030  0.245   82.934  1.00 120.98 ?  43  ALA B HB2  1 
ATOM   6162  H HB3  . ALA B 1 34  ? -4.606  0.975   81.645  1.00 120.98 ?  43  ALA B HB3  1 
ATOM   6163  N N    . LYS B 1 35  ? -5.751  3.769   81.896  1.00 116.35 ?  44  LYS B N    1 
ATOM   6164  C CA   . LYS B 1 35  ? -5.889  4.984   81.120  1.00 93.86  ?  44  LYS B CA   1 
ATOM   6165  C C    . LYS B 1 35  ? -6.162  6.213   81.981  1.00 96.69  ?  44  LYS B C    1 
ATOM   6166  O O    . LYS B 1 35  ? -6.190  7.323   81.441  1.00 111.97 ?  44  LYS B O    1 
ATOM   6167  C CB   . LYS B 1 35  ? -7.002  4.783   80.081  1.00 94.92  ?  44  LYS B CB   1 
ATOM   6168  H H    . LYS B 1 35  ? -6.446  3.263   81.861  1.00 139.62 ?  44  LYS B H    1 
ATOM   6169  H HA   . LYS B 1 35  ? -5.061  5.140   80.639  1.00 112.63 ?  44  LYS B HA   1 
ATOM   6170  N N    . HIS B 1 36  ? -6.352  6.060   83.299  1.00 132.08 ?  45  HIS B N    1 
ATOM   6171  C CA   . HIS B 1 36  ? -6.745  7.197   84.132  1.00 129.88 ?  45  HIS B CA   1 
ATOM   6172  C C    . HIS B 1 36  ? -5.997  7.214   85.468  1.00 113.30 ?  45  HIS B C    1 
ATOM   6173  O O    . HIS B 1 36  ? -6.476  7.799   86.446  1.00 126.04 ?  45  HIS B O    1 
ATOM   6174  C CB   . HIS B 1 36  ? -8.271  7.189   84.361  1.00 123.22 ?  45  HIS B CB   1 
ATOM   6175  C CG   . HIS B 1 36  ? -9.086  7.483   83.132  1.00 150.99 ?  45  HIS B CG   1 
ATOM   6176  N ND1  . HIS B 1 36  ? -9.443  6.515   82.211  1.00 97.40  ?  45  HIS B ND1  1 
ATOM   6177  C CD2  . HIS B 1 36  ? -9.689  8.626   82.722  1.00 121.29 ?  45  HIS B CD2  1 
ATOM   6178  C CE1  . HIS B 1 36  ? -10.178 7.064   81.260  1.00 98.82  ?  45  HIS B CE1  1 
ATOM   6179  N NE2  . HIS B 1 36  ? -10.351 8.341   81.552  1.00 112.02 ?  45  HIS B NE2  1 
ATOM   6180  H H    . HIS B 1 36  ? -6.261  5.319   83.726  1.00 158.49 ?  45  HIS B H    1 
ATOM   6181  H HA   . HIS B 1 36  ? -6.524  8.016   83.662  1.00 155.85 ?  45  HIS B HA   1 
ATOM   6182  H HB2  . HIS B 1 36  ? -8.531  6.312   84.684  1.00 147.87 ?  45  HIS B HB2  1 
ATOM   6183  H HB3  . HIS B 1 36  ? -8.489  7.860   85.026  1.00 147.87 ?  45  HIS B HB3  1 
ATOM   6184  H HD1  . HIS B 1 36  ? -9.196  5.691   82.235  1.00 116.88 ?  45  HIS B HD1  1 
ATOM   6185  H HD2  . HIS B 1 36  ? -9.642  9.455   83.142  1.00 145.55 ?  45  HIS B HD2  1 
ATOM   6186  H HE1  . HIS B 1 36  ? -10.531 6.621   80.522  1.00 118.58 ?  45  HIS B HE1  1 
ATOM   6187  N N    . LEU B 1 37  ? -4.799  6.630   85.502  1.00 116.06 ?  46  LEU B N    1 
ATOM   6188  C CA   . LEU B 1 37  ? -3.990  6.593   86.721  1.00 109.82 ?  46  LEU B CA   1 
ATOM   6189  C C    . LEU B 1 37  ? -3.773  7.971   87.345  1.00 109.81 ?  46  LEU B C    1 
ATOM   6190  O O    . LEU B 1 37  ? -3.831  8.081   88.586  1.00 123.62 ?  46  LEU B O    1 
ATOM   6191  C CB   . LEU B 1 37  ? -2.648  5.904   86.409  1.00 105.36 ?  46  LEU B CB   1 
ATOM   6192  H H    . LEU B 1 37  ? -4.430  6.245   84.828  1.00 139.27 ?  46  LEU B H    1 
ATOM   6193  H HA   . LEU B 1 37  ? -4.451  6.048   87.378  1.00 131.78 ?  46  LEU B HA   1 
ATOM   6194  N N    . PRO B 1 38  ? -3.541  9.031   86.581  1.00 91.20  ?  47  PRO B N    1 
ATOM   6195  C CA   . PRO B 1 38  ? -3.439  10.365  87.193  1.00 92.14  ?  47  PRO B CA   1 
ATOM   6196  C C    . PRO B 1 38  ? -4.640  10.771  88.031  1.00 102.61 ?  47  PRO B C    1 
ATOM   6197  O O    . PRO B 1 38  ? -4.463  11.056  89.225  1.00 119.29 ?  47  PRO B O    1 
ATOM   6198  C CB   . PRO B 1 38  ? -3.273  11.270  85.977  1.00 92.58  ?  47  PRO B CB   1 
ATOM   6199  C CG   . PRO B 1 38  ? -2.719  10.399  84.922  1.00 91.49  ?  47  PRO B CG   1 
ATOM   6200  C CD   . PRO B 1 38  ? -3.232  9.034   85.149  1.00 90.98  ?  47  PRO B CD   1 
ATOM   6201  H HA   . PRO B 1 38  ? -2.639  10.420  87.739  1.00 110.56 ?  47  PRO B HA   1 
ATOM   6202  H HB2  . PRO B 1 38  ? -4.137  11.623  85.712  1.00 111.10 ?  47  PRO B HB2  1 
ATOM   6203  H HB3  . PRO B 1 38  ? -2.658  11.990  86.186  1.00 111.10 ?  47  PRO B HB3  1 
ATOM   6204  H HG2  . PRO B 1 38  ? -3.007  10.726  84.055  1.00 109.79 ?  47  PRO B HG2  1 
ATOM   6205  H HG3  . PRO B 1 38  ? -1.750  10.407  84.978  1.00 109.79 ?  47  PRO B HG3  1 
ATOM   6206  H HD2  . PRO B 1 38  ? -4.036  8.884   84.628  1.00 109.18 ?  47  PRO B HD2  1 
ATOM   6207  H HD3  . PRO B 1 38  ? -2.548  8.377   84.948  1.00 109.18 ?  47  PRO B HD3  1 
ATOM   6208  N N    . ASP B 1 39  ? -5.864  10.764  87.464  1.00 94.80  ?  48  ASP B N    1 
ATOM   6209  C CA   . ASP B 1 39  ? -7.044  11.208  88.217  1.00 96.74  ?  48  ASP B CA   1 
ATOM   6210  C C    . ASP B 1 39  ? -7.328  10.280  89.406  1.00 102.91 ?  48  ASP B C    1 
ATOM   6211  O O    . ASP B 1 39  ? -7.584  10.745  90.526  1.00 97.88  ?  48  ASP B O    1 
ATOM   6212  C CB   . ASP B 1 39  ? -8.250  11.292  87.278  1.00 128.26 ?  48  ASP B CB   1 
ATOM   6213  C CG   . ASP B 1 39  ? -8.176  12.479  86.339  1.00 98.67  ?  48  ASP B CG   1 
ATOM   6214  H H    . ASP B 1 39  ? -6.030  10.511  86.660  1.00 113.76 ?  48  ASP B H    1 
ATOM   6215  H HA   . ASP B 1 39  ? -6.877  12.097  88.567  1.00 116.08 ?  48  ASP B HA   1 
ATOM   6216  H HB2  . ASP B 1 39  ? -8.289  10.486  86.740  1.00 153.91 ?  48  ASP B HB2  1 
ATOM   6217  H HB3  . ASP B 1 39  ? -9.058  11.378  87.808  1.00 153.91 ?  48  ASP B HB3  1 
ATOM   6218  N N    . LEU B 1 40  ? -7.272  8.957   89.175  1.00 95.50  ?  49  LEU B N    1 
ATOM   6219  C CA   . LEU B 1 40  ? -7.625  7.964   90.190  1.00 117.63 ?  49  LEU B CA   1 
ATOM   6220  C C    . LEU B 1 40  ? -6.619  7.907   91.310  1.00 116.63 ?  49  LEU B C    1 
ATOM   6221  O O    . LEU B 1 40  ? -6.973  7.565   92.440  1.00 99.94  ?  49  LEU B O    1 
ATOM   6222  C CB   . LEU B 1 40  ? -7.720  6.585   89.559  1.00 121.77 ?  49  LEU B CB   1 
ATOM   6223  C CG   . LEU B 1 40  ? -8.845  6.360   88.559  1.00 146.01 ?  49  LEU B CG   1 
ATOM   6224  C CD1  . LEU B 1 40  ? -8.621  5.047   87.856  1.00 131.84 ?  49  LEU B CD1  1 
ATOM   6225  C CD2  . LEU B 1 40  ? -10.207 6.355   89.258  1.00 137.26 ?  49  LEU B CD2  1 
ATOM   6226  H H    . LEU B 1 40  ? -7.028  8.611   88.427  1.00 114.60 ?  49  LEU B H    1 
ATOM   6227  H HA   . LEU B 1 40  ? -8.490  8.186   90.569  1.00 141.16 ?  49  LEU B HA   1 
ATOM   6228  H HB2  . LEU B 1 40  ? -6.886  6.408   89.095  1.00 146.12 ?  49  LEU B HB2  1 
ATOM   6229  H HB3  . LEU B 1 40  ? -7.834  5.935   90.269  1.00 146.12 ?  49  LEU B HB3  1 
ATOM   6230  H HG   . LEU B 1 40  ? -8.840  7.070   87.898  1.00 175.21 ?  49  LEU B HG   1 
ATOM   6231  H HD11 . LEU B 1 40  ? -9.338  4.904   87.219  1.00 158.20 ?  49  LEU B HD11 1 
ATOM   6232  H HD12 . LEU B 1 40  ? -7.769  5.078   87.393  1.00 158.20 ?  49  LEU B HD12 1 
ATOM   6233  H HD13 . LEU B 1 40  ? -8.615  4.334   88.513  1.00 158.20 ?  49  LEU B HD13 1 
ATOM   6234  H HD21 . LEU B 1 40  ? -10.901 6.209   88.595  1.00 164.71 ?  49  LEU B HD21 1 
ATOM   6235  H HD22 . LEU B 1 40  ? -10.221 5.641   89.915  1.00 164.71 ?  49  LEU B HD22 1 
ATOM   6236  H HD23 . LEU B 1 40  ? -10.340 7.210   89.695  1.00 164.71 ?  49  LEU B HD23 1 
ATOM   6237  N N    . ILE B 1 41  ? -5.355  8.143   91.001  1.00 149.44 ?  50  ILE B N    1 
ATOM   6238  C CA   . ILE B 1 41  ? -4.369  8.268   92.052  1.00 148.16 ?  50  ILE B CA   1 
ATOM   6239  C C    . ILE B 1 41  ? -4.610  9.570   92.794  1.00 181.67 ?  50  ILE B C    1 
ATOM   6240  O O    . ILE B 1 41  ? -4.708  9.605   94.023  1.00 199.48 ?  50  ILE B O    1 
ATOM   6241  C CB   . ILE B 1 41  ? -2.956  8.185   91.458  1.00 132.67 ?  50  ILE B CB   1 
ATOM   6242  C CG1  . ILE B 1 41  ? -2.712  6.789   90.890  1.00 216.88 ?  50  ILE B CG1  1 
ATOM   6243  C CG2  . ILE B 1 41  ? -1.921  8.453   92.526  1.00 160.14 ?  50  ILE B CG2  1 
ATOM   6244  C CD1  . ILE B 1 41  ? -1.470  6.687   90.040  1.00 88.14  ?  50  ILE B CD1  1 
ATOM   6245  H H    . ILE B 1 41  ? -5.047  8.234   90.203  1.00 179.32 ?  50  ILE B H    1 
ATOM   6246  H HA   . ILE B 1 41  ? -4.478  7.537   92.680  1.00 177.80 ?  50  ILE B HA   1 
ATOM   6247  H HB   . ILE B 1 41  ? -2.866  8.841   90.749  1.00 159.20 ?  50  ILE B HB   1 
ATOM   6248  H HG12 . ILE B 1 41  ? -2.620  6.164   91.626  1.00 260.25 ?  50  ILE B HG12 1 
ATOM   6249  H HG13 . ILE B 1 41  ? -3.470  6.539   90.339  1.00 260.25 ?  50  ILE B HG13 1 
ATOM   6250  H HG21 . ILE B 1 41  ? -1.037  8.396   92.130  1.00 192.17 ?  50  ILE B HG21 1 
ATOM   6251  H HG22 . ILE B 1 41  ? -2.064  9.342   92.888  1.00 192.17 ?  50  ILE B HG22 1 
ATOM   6252  H HG23 . ILE B 1 41  ? -2.012  7.790   93.228  1.00 192.17 ?  50  ILE B HG23 1 
ATOM   6253  H HD11 . ILE B 1 41  ? -1.383  5.776   89.717  1.00 105.77 ?  50  ILE B HD11 1 
ATOM   6254  H HD12 . ILE B 1 41  ? -1.549  7.298   89.291  1.00 105.77 ?  50  ILE B HD12 1 
ATOM   6255  H HD13 . ILE B 1 41  ? -0.699  6.922   90.579  1.00 105.77 ?  50  ILE B HD13 1 
ATOM   6256  N N    . GLU B 1 42  ? -4.757  10.657  92.045  1.00 159.10 ?  51  GLU B N    1 
ATOM   6257  C CA   . GLU B 1 42  ? -4.890  11.959  92.673  1.00 161.64 ?  51  GLU B CA   1 
ATOM   6258  C C    . GLU B 1 42  ? -6.133  12.022  93.536  1.00 147.20 ?  51  GLU B C    1 
ATOM   6259  O O    . GLU B 1 42  ? -6.088  12.501  94.671  1.00 126.28 ?  51  GLU B O    1 
ATOM   6260  C CB   . GLU B 1 42  ? -4.950  13.028  91.596  1.00 97.72  ?  51  GLU B CB   1 
ATOM   6261  C CG   . GLU B 1 42  ? -5.384  14.392  92.084  1.00 113.20 ?  51  GLU B CG   1 
ATOM   6262  C CD   . GLU B 1 42  ? -6.902  14.579  92.095  1.00 120.68 ?  51  GLU B CD   1 
ATOM   6263  H H    . GLU B 1 42  ? -4.784  10.666  91.186  1.00 190.92 ?  51  GLU B H    1 
ATOM   6264  H HA   . GLU B 1 42  ? -4.117  12.129  93.234  1.00 193.97 ?  51  GLU B HA   1 
ATOM   6265  H HB2  . GLU B 1 42  ? -4.067  13.123  91.205  1.00 117.27 ?  51  GLU B HB2  1 
ATOM   6266  H HB3  . GLU B 1 42  ? -5.580  12.746  90.914  1.00 117.27 ?  51  GLU B HB3  1 
ATOM   6267  H HG2  . GLU B 1 42  ? -5.061  14.519  92.990  1.00 135.84 ?  51  GLU B HG2  1 
ATOM   6268  H HG3  . GLU B 1 42  ? -5.005  15.069  91.501  1.00 135.84 ?  51  GLU B HG3  1 
ATOM   6269  N N    . SER B 1 43  ? -7.248  11.505  93.035  1.00 153.25 ?  52  SER B N    1 
ATOM   6270  C CA   . SER B 1 43  ? -8.457  11.522  93.836  1.00 112.00 ?  52  SER B CA   1 
ATOM   6271  C C    . SER B 1 43  ? -8.362  10.568  95.004  1.00 101.36 ?  52  SER B C    1 
ATOM   6272  O O    . SER B 1 43  ? -8.939  10.835  96.065  1.00 131.37 ?  52  SER B O    1 
ATOM   6273  C CB   . SER B 1 43  ? -9.671  11.197  92.979  1.00 110.66 ?  52  SER B CB   1 
ATOM   6274  O OG   . SER B 1 43  ? -9.852  9.811   92.852  1.00 108.29 ?  52  SER B OG   1 
ATOM   6275  H H    . SER B 1 43  ? -7.328  11.149  92.256  1.00 183.90 ?  52  SER B H    1 
ATOM   6276  H HA   . SER B 1 43  ? -8.580  12.415  94.194  1.00 134.40 ?  52  SER B HA   1 
ATOM   6277  H HB2  . SER B 1 43  ? -10.459 11.580  93.395  1.00 132.79 ?  52  SER B HB2  1 
ATOM   6278  H HB3  . SER B 1 43  ? -9.544  11.580  92.097  1.00 132.79 ?  52  SER B HB3  1 
ATOM   6279  H HG   . SER B 1 43  ? -10.526 9.652   92.376  1.00 129.94 ?  52  SER B HG   1 
ATOM   6280  N N    . GLY B 1 44  ? -7.659  9.456   94.828  1.00 103.71 ?  53  GLY B N    1 
ATOM   6281  C CA   . GLY B 1 44  ? -7.553  8.413   95.835  1.00 76.74  ?  53  GLY B CA   1 
ATOM   6282  C C    . GLY B 1 44  ? -8.502  7.236   95.700  1.00 82.76  ?  53  GLY B C    1 
ATOM   6283  O O    . GLY B 1 44  ? -8.831  6.610   96.716  1.00 97.62  ?  53  GLY B O    1 
ATOM   6284  H H    . GLY B 1 44  ? -7.220  9.279   94.109  1.00 124.45 ?  53  GLY B H    1 
ATOM   6285  H HA2  . GLY B 1 44  ? -6.649  8.062   95.822  1.00 92.09  ?  53  GLY B HA2  1 
ATOM   6286  H HA3  . GLY B 1 44  ? -7.703  8.810   96.707  1.00 92.09  ?  53  GLY B HA3  1 
ATOM   6287  N N    . GLN B 1 45  ? -8.952  6.917   94.494  1.00 98.29  ?  54  GLN B N    1 
ATOM   6288  C CA   . GLN B 1 45  ? -9.900  5.837   94.300  1.00 83.84  ?  54  GLN B CA   1 
ATOM   6289  C C    . GLN B 1 45  ? -9.297  4.721   93.482  1.00 109.97 ?  54  GLN B C    1 
ATOM   6290  O O    . GLN B 1 45  ? -10.025 3.820   93.047  1.00 125.93 ?  54  GLN B O    1 
ATOM   6291  C CB   . GLN B 1 45  ? -11.167 6.366   93.611  1.00 117.23 ?  54  GLN B CB   1 
ATOM   6292  H H    . GLN B 1 45  ? -8.720  7.315   93.768  1.00 117.95 ?  54  GLN B H    1 
ATOM   6293  H HA   . GLN B 1 45  ? -10.153 5.477   95.164  1.00 100.60 ?  54  GLN B HA   1 
ATOM   6294  N N    . LEU B 1 46  ? -7.979  4.745   93.285  1.00 134.23 ?  55  LEU B N    1 
ATOM   6295  C CA   . LEU B 1 46  ? -7.326  3.661   92.567  1.00 112.23 ?  55  LEU B CA   1 
ATOM   6296  C C    . LEU B 1 46  ? -7.383  2.368   93.356  1.00 102.10 ?  55  LEU B C    1 
ATOM   6297  O O    . LEU B 1 46  ? -7.730  1.317   92.815  1.00 108.05 ?  55  LEU B O    1 
ATOM   6298  C CB   . LEU B 1 46  ? -5.881  4.017   92.251  1.00 155.08 ?  55  LEU B CB   1 
ATOM   6299  C CG   . LEU B 1 46  ? -5.161  2.935   91.426  1.00 116.97 ?  55  LEU B CG   1 
ATOM   6300  C CD1  . LEU B 1 46  ? -4.968  3.308   89.967  1.00 123.21 ?  55  LEU B CD1  1 
ATOM   6301  C CD2  . LEU B 1 46  ? -3.838  2.610   92.062  1.00 85.99  ?  55  LEU B CD2  1 
ATOM   6302  H H    . LEU B 1 46  ? -7.451  5.368   93.553  1.00 161.07 ?  55  LEU B H    1 
ATOM   6303  H HA   . LEU B 1 46  ? -7.788  3.518   91.727  1.00 134.67 ?  55  LEU B HA   1 
ATOM   6304  H HB2  . LEU B 1 46  ? -5.863  4.843   91.742  1.00 186.10 ?  55  LEU B HB2  1 
ATOM   6305  H HB3  . LEU B 1 46  ? -5.395  4.131   93.083  1.00 186.10 ?  55  LEU B HB3  1 
ATOM   6306  H HG   . LEU B 1 46  ? -5.698  2.128   91.448  1.00 140.36 ?  55  LEU B HG   1 
ATOM   6307  H HD11 . LEU B 1 46  ? -4.511  2.582   89.514  1.00 147.86 ?  55  LEU B HD11 1 
ATOM   6308  H HD12 . LEU B 1 46  ? -5.836  3.456   89.561  1.00 147.86 ?  55  LEU B HD12 1 
ATOM   6309  H HD13 . LEU B 1 46  ? -4.436  4.117   89.916  1.00 147.86 ?  55  LEU B HD13 1 
ATOM   6310  H HD21 . LEU B 1 46  ? -3.393  1.928   91.534  1.00 103.18 ?  55  LEU B HD21 1 
ATOM   6311  H HD22 . LEU B 1 46  ? -3.295  3.414   92.089  1.00 103.18 ?  55  LEU B HD22 1 
ATOM   6312  H HD23 . LEU B 1 46  ? -3.992  2.284   92.962  1.00 103.18 ?  55  LEU B HD23 1 
ATOM   6313  N N    . ARG B 1 47  ? -7.038  2.411   94.630  1.00 75.76  ?  56  ARG B N    1 
ATOM   6314  C CA   . ARG B 1 47  ? -7.061  1.163   95.375  1.00 91.19  ?  56  ARG B CA   1 
ATOM   6315  C C    . ARG B 1 47  ? -8.487  0.630   95.576  1.00 116.49 ?  56  ARG B C    1 
ATOM   6316  O O    . ARG B 1 47  ? -8.707  -0.577  95.448  1.00 116.03 ?  56  ARG B O    1 
ATOM   6317  C CB   . ARG B 1 47  ? -6.335  1.349   96.699  1.00 100.37 ?  56  ARG B CB   1 
ATOM   6318  C CG   . ARG B 1 47  ? -4.868  1.686   96.475  1.00 113.41 ?  56  ARG B CG   1 
ATOM   6319  C CD   . ARG B 1 47  ? -4.222  2.083   97.761  1.00 116.97 ?  56  ARG B CD   1 
ATOM   6320  N NE   . ARG B 1 47  ? -2.806  2.269   97.575  1.00 104.37 ?  56  ARG B NE   1 
ATOM   6321  C CZ   . ARG B 1 47  ? -2.029  2.827   98.480  1.00 78.16  ?  56  ARG B CZ   1 
ATOM   6322  N NH1  . ARG B 1 47  ? -2.526  3.242   99.654  1.00 99.47  1  56  ARG B NH1  1 
ATOM   6323  N NH2  . ARG B 1 47  ? -0.748  2.964   98.203  1.00 66.64  1  56  ARG B NH2  1 
ATOM   6324  H H    . ARG B 1 47  ? -6.799  3.109   95.071  1.00 90.91  ?  56  ARG B H    1 
ATOM   6325  H HA   . ARG B 1 47  ? -6.572  0.495   94.868  1.00 109.43 ?  56  ARG B HA   1 
ATOM   6326  H HB2  . ARG B 1 47  ? -6.744  2.078   97.191  1.00 120.44 ?  56  ARG B HB2  1 
ATOM   6327  H HB3  . ARG B 1 47  ? -6.385  0.526   97.212  1.00 120.44 ?  56  ARG B HB3  1 
ATOM   6328  H HG2  . ARG B 1 47  ? -4.406  0.907   96.128  1.00 136.10 ?  56  ARG B HG2  1 
ATOM   6329  H HG3  . ARG B 1 47  ? -4.797  2.427   95.854  1.00 136.10 ?  56  ARG B HG3  1 
ATOM   6330  H HD2  . ARG B 1 47  ? -4.604  2.920   98.070  1.00 140.37 ?  56  ARG B HD2  1 
ATOM   6331  H HD3  . ARG B 1 47  ? -4.356  1.385   98.421  1.00 140.37 ?  56  ARG B HD3  1 
ATOM   6332  H HE   . ARG B 1 47  ? -2.431  1.862   96.917  1.00 125.24 ?  56  ARG B HE   1 
ATOM   6333  H HH11 . ARG B 1 47  ? -3.365  3.151   99.822  1.00 119.37 ?  56  ARG B HH11 1 
ATOM   6334  H HH12 . ARG B 1 47  ? -2.008  3.603   100.238 1.00 119.37 ?  56  ARG B HH12 1 
ATOM   6335  H HH21 . ARG B 1 47  ? -0.439  2.691   97.449  1.00 79.97  ?  56  ARG B HH21 1 
ATOM   6336  H HH22 . ARG B 1 47  ? -0.219  3.319   98.781  1.00 79.97  ?  56  ARG B HH22 1 
ATOM   6337  N N    . GLU B 1 48  ? -9.482  1.490   95.855  1.00 111.73 ?  57  GLU B N    1 
ATOM   6338  C CA   . GLU B 1 48  ? -10.859 0.987   95.973  1.00 115.79 ?  57  GLU B CA   1 
ATOM   6339  C C    . GLU B 1 48  ? -11.324 0.382   94.656  1.00 138.74 ?  57  GLU B C    1 
ATOM   6340  O O    . GLU B 1 48  ? -11.926 -0.698  94.628  1.00 133.32 ?  57  GLU B O    1 
ATOM   6341  C CB   . GLU B 1 48  ? -11.826 2.090   96.421  1.00 98.74  ?  57  GLU B CB   1 
ATOM   6342  H H    . GLU B 1 48  ? -9.391  2.336   95.976  1.00 134.07 ?  57  GLU B H    1 
ATOM   6343  H HA   . GLU B 1 48  ? -10.879 0.286   96.643  1.00 138.95 ?  57  GLU B HA   1 
ATOM   6344  N N    . ARG B 1 49  ? -11.022 1.058   93.553  1.00 145.93 ?  58  ARG B N    1 
ATOM   6345  C CA   . ARG B 1 49  ? -11.462 0.614   92.241  1.00 122.62 ?  58  ARG B CA   1 
ATOM   6346  C C    . ARG B 1 49  ? -10.796 -0.702  91.860  1.00 114.70 ?  58  ARG B C    1 
ATOM   6347  O O    . ARG B 1 49  ? -11.457 -1.645  91.406  1.00 165.18 ?  58  ARG B O    1 
ATOM   6348  C CB   . ARG B 1 49  ? -11.140 1.706   91.234  1.00 121.34 ?  58  ARG B CB   1 
ATOM   6349  C CG   . ARG B 1 49  ? -11.355 1.325   89.812  1.00 114.39 ?  58  ARG B CG   1 
ATOM   6350  C CD   . ARG B 1 49  ? -12.826 1.231   89.440  1.00 126.93 ?  58  ARG B CD   1 
ATOM   6351  N NE   . ARG B 1 49  ? -12.976 1.336   87.992  1.00 138.51 ?  58  ARG B NE   1 
ATOM   6352  C CZ   . ARG B 1 49  ? -13.088 2.487   87.333  1.00 156.81 ?  58  ARG B CZ   1 
ATOM   6353  N NH1  . ARG B 1 49  ? -13.091 3.638   87.983  1.00 141.16 1  58  ARG B NH1  1 
ATOM   6354  N NH2  . ARG B 1 49  ? -13.182 2.493   86.013  1.00 92.98  1  58  ARG B NH2  1 
ATOM   6355  H H    . ARG B 1 49  ? -10.559 1.783   93.540  1.00 175.12 ?  58  ARG B H    1 
ATOM   6356  H HA   . ARG B 1 49  ? -12.422 0.479   92.252  1.00 147.14 ?  58  ARG B HA   1 
ATOM   6357  H HB2  . ARG B 1 49  ? -11.703 2.474   91.420  1.00 145.60 ?  58  ARG B HB2  1 
ATOM   6358  H HB3  . ARG B 1 49  ? -10.208 1.954   91.333  1.00 145.60 ?  58  ARG B HB3  1 
ATOM   6359  H HG2  . ARG B 1 49  ? -10.944 1.993   89.241  1.00 137.27 ?  58  ARG B HG2  1 
ATOM   6360  H HG3  . ARG B 1 49  ? -10.950 0.458   89.653  1.00 137.27 ?  58  ARG B HG3  1 
ATOM   6361  H HD2  . ARG B 1 49  ? -13.181 0.375   89.726  1.00 152.32 ?  58  ARG B HD2  1 
ATOM   6362  H HD3  . ARG B 1 49  ? -13.315 1.959   89.855  1.00 152.32 ?  58  ARG B HD3  1 
ATOM   6363  H HE   . ARG B 1 49  ? -12.993 0.608   87.536  1.00 166.22 ?  58  ARG B HE   1 
ATOM   6364  H HH11 . ARG B 1 49  ? -13.019 3.648   88.840  1.00 169.39 ?  58  ARG B HH11 1 
ATOM   6365  H HH12 . ARG B 1 49  ? -13.166 4.377   87.549  1.00 169.39 ?  58  ARG B HH12 1 
ATOM   6366  H HH21 . ARG B 1 49  ? -13.188 1.750   85.579  1.00 111.58 ?  58  ARG B HH21 1 
ATOM   6367  H HH22 . ARG B 1 49  ? -13.267 3.238   85.592  1.00 111.58 ?  58  ARG B HH22 1 
ATOM   6368  N N    . VAL B 1 50  ? -9.478  -0.762  92.023  1.00 108.46 ?  59  VAL B N    1 
ATOM   6369  C CA   . VAL B 1 50  ? -8.726  -2.006  91.864  1.00 110.02 ?  59  VAL B CA   1 
ATOM   6370  C C    . VAL B 1 50  ? -9.322  -3.110  92.726  1.00 106.54 ?  59  VAL B C    1 
ATOM   6371  O O    . VAL B 1 50  ? -9.535  -4.248  92.279  1.00 94.77  ?  59  VAL B O    1 
ATOM   6372  C CB   . VAL B 1 50  ? -7.249  -1.761  92.233  1.00 98.29  ?  59  VAL B CB   1 
ATOM   6373  C CG1  . VAL B 1 50  ? -6.482  -3.050  92.452  1.00 92.26  ?  59  VAL B CG1  1 
ATOM   6374  C CG2  . VAL B 1 50  ? -6.554  -0.939  91.136  1.00 130.61 ?  59  VAL B CG2  1 
ATOM   6375  H H    . VAL B 1 50  ? -8.987  -0.086  92.229  1.00 130.15 ?  59  VAL B H    1 
ATOM   6376  H HA   . VAL B 1 50  ? -8.765  -2.288  90.937  1.00 132.02 ?  59  VAL B HA   1 
ATOM   6377  H HB   . VAL B 1 50  ? -7.213  -1.250  93.056  1.00 117.95 ?  59  VAL B HB   1 
ATOM   6378  H HG11 . VAL B 1 50  ? -5.564  -2.835  92.680  1.00 110.72 ?  59  VAL B HG11 1 
ATOM   6379  H HG12 . VAL B 1 50  ? -6.896  -3.545  93.176  1.00 110.72 ?  59  VAL B HG12 1 
ATOM   6380  H HG13 . VAL B 1 50  ? -6.506  -3.574  91.636  1.00 110.72 ?  59  VAL B HG13 1 
ATOM   6381  H HG21 . VAL B 1 50  ? -5.628  -0.797  91.387  1.00 156.73 ?  59  VAL B HG21 1 
ATOM   6382  H HG22 . VAL B 1 50  ? -6.599  -1.429  90.299  1.00 156.73 ?  59  VAL B HG22 1 
ATOM   6383  H HG23 . VAL B 1 50  ? -7.007  -0.087  91.045  1.00 156.73 ?  59  VAL B HG23 1 
ATOM   6384  N N    . GLU B 1 51  ? -9.577  -2.800  93.987  1.00 154.56 ?  60  GLU B N    1 
ATOM   6385  C CA   . GLU B 1 51  ? -10.045 -3.842  94.878  1.00 107.74 ?  60  GLU B CA   1 
ATOM   6386  C C    . GLU B 1 51  ? -11.448 -4.292  94.487  1.00 102.62 ?  60  GLU B C    1 
ATOM   6387  O O    . GLU B 1 51  ? -11.819 -5.435  94.766  1.00 118.14 ?  60  GLU B O    1 
ATOM   6388  C CB   . GLU B 1 51  ? -9.926  -3.332  96.324  1.00 92.18  ?  60  GLU B CB   1 
ATOM   6389  C CG   . GLU B 1 51  ? -8.429  -3.254  96.821  1.00 135.71 ?  60  GLU B CG   1 
ATOM   6390  C CD   . GLU B 1 51  ? -8.131  -2.188  97.908  1.00 162.83 ?  60  GLU B CD   1 
ATOM   6391  O OE1  . GLU B 1 51  ? -9.082  -1.576  98.421  1.00 143.82 ?  60  GLU B OE1  1 
ATOM   6392  O OE2  . GLU B 1 51  ? -6.941  -1.952  98.245  1.00 150.57 -1 60  GLU B OE2  1 
ATOM   6393  H H    . GLU B 1 51  ? -9.492  -2.020  94.340  1.00 185.48 ?  60  GLU B H    1 
ATOM   6394  H HA   . GLU B 1 51  ? -9.458  -4.609  94.790  1.00 129.29 ?  60  GLU B HA   1 
ATOM   6395  H HB2  . GLU B 1 51  ? -10.307 -2.442  96.378  1.00 110.62 ?  60  GLU B HB2  1 
ATOM   6396  H HB3  . GLU B 1 51  ? -10.406 -3.935  96.912  1.00 110.62 ?  60  GLU B HB3  1 
ATOM   6397  H HG2  . GLU B 1 51  ? -8.184  -4.118  97.188  1.00 162.85 ?  60  GLU B HG2  1 
ATOM   6398  H HG3  . GLU B 1 51  ? -7.864  -3.056  96.058  1.00 162.85 ?  60  GLU B HG3  1 
ATOM   6399  N N    . LYS B 1 52  ? -12.204 -3.463  93.762  1.00 108.97 ?  61  LYS B N    1 
ATOM   6400  C CA   . LYS B 1 52  ? -13.535 -3.858  93.310  1.00 130.29 ?  61  LYS B CA   1 
ATOM   6401  C C    . LYS B 1 52  ? -13.518 -4.451  91.907  1.00 123.49 ?  61  LYS B C    1 
ATOM   6402  O O    . LYS B 1 52  ? -14.435 -4.198  91.120  1.00 125.09 ?  61  LYS B O    1 
ATOM   6403  C CB   . LYS B 1 52  ? -14.522 -2.684  93.401  1.00 107.52 ?  61  LYS B CB   1 
ATOM   6404  H H    . LYS B 1 52  ? -11.968 -2.672  93.522  1.00 130.77 ?  61  LYS B H    1 
ATOM   6405  H HA   . LYS B 1 52  ? -13.861 -4.550  93.906  1.00 156.35 ?  61  LYS B HA   1 
ATOM   6406  N N    . LEU B 1 53  ? -12.458 -5.159  91.541  1.00 110.85 ?  62  LEU B N    1 
ATOM   6407  C CA   . LEU B 1 53  ? -12.430 -5.878  90.276  1.00 123.98 ?  62  LEU B CA   1 
ATOM   6408  C C    . LEU B 1 53  ? -12.593 -7.382  90.475  1.00 122.78 ?  62  LEU B C    1 
ATOM   6409  O O    . LEU B 1 53  ? -12.408 -7.913  91.570  1.00 159.30 ?  62  LEU B O    1 
ATOM   6410  C CB   . LEU B 1 53  ? -11.144 -5.604  89.519  1.00 120.13 ?  62  LEU B CB   1 
ATOM   6411  C CG   . LEU B 1 53  ? -10.942 -4.129  89.186  1.00 119.80 ?  62  LEU B CG   1 
ATOM   6412  C CD1  . LEU B 1 53  ? -9.680  -4.071  88.371  1.00 108.72 ?  62  LEU B CD1  1 
ATOM   6413  C CD2  . LEU B 1 53  ? -12.124 -3.451  88.489  1.00 133.75 ?  62  LEU B CD2  1 
ATOM   6414  H H    . LEU B 1 53  ? -11.741 -5.239  92.009  1.00 133.02 ?  62  LEU B H    1 
ATOM   6415  H HA   . LEU B 1 53  ? -13.168 -5.571  89.727  1.00 148.77 ?  62  LEU B HA   1 
ATOM   6416  H HB2  . LEU B 1 53  ? -10.392 -5.892  90.060  1.00 144.15 ?  62  LEU B HB2  1 
ATOM   6417  H HB3  . LEU B 1 53  ? -11.159 -6.098  88.684  1.00 144.15 ?  62  LEU B HB3  1 
ATOM   6418  H HG   . LEU B 1 53  ? -10.778 -3.648  90.012  1.00 143.76 ?  62  LEU B HG   1 
ATOM   6419  H HD11 . LEU B 1 53  ? -9.502  -3.148  88.130  1.00 130.46 ?  62  LEU B HD11 1 
ATOM   6420  H HD12 . LEU B 1 53  ? -8.947  -4.422  88.901  1.00 130.46 ?  62  LEU B HD12 1 
ATOM   6421  H HD13 . LEU B 1 53  ? -9.796  -4.606  87.571  1.00 130.46 ?  62  LEU B HD13 1 
ATOM   6422  H HD21 . LEU B 1 53  ? -11.899 -2.522  88.321  1.00 160.50 ?  62  LEU B HD21 1 
ATOM   6423  H HD22 . LEU B 1 53  ? -12.299 -3.906  87.651  1.00 160.50 ?  62  LEU B HD22 1 
ATOM   6424  H HD23 . LEU B 1 53  ? -12.902 -3.505  89.065  1.00 160.50 ?  62  LEU B HD23 1 
ATOM   6425  N N    . ASN B 1 54  ? -12.992 -8.060  89.403  1.00 113.46 ?  63  ASN B N    1 
ATOM   6426  C CA   . ASN B 1 54  ? -13.047 -9.516  89.395  1.00 111.19 ?  63  ASN B CA   1 
ATOM   6427  C C    . ASN B 1 54  ? -11.734 -10.128 88.953  1.00 161.86 ?  63  ASN B C    1 
ATOM   6428  O O    . ASN B 1 54  ? -10.934 -9.520  88.252  1.00 142.60 ?  63  ASN B O    1 
ATOM   6429  C CB   . ASN B 1 54  ? -14.165 -10.014 88.479  1.00 115.04 ?  63  ASN B CB   1 
ATOM   6430  C CG   . ASN B 1 54  ? -15.534 -9.546  88.928  1.00 117.37 ?  63  ASN B CG   1 
ATOM   6431  O OD1  . ASN B 1 54  ? -16.307 -9.085  88.111  1.00 118.98 ?  63  ASN B OD1  1 
ATOM   6432  N ND2  . ASN B 1 54  ? -15.847 -9.683  90.219  1.00 119.24 ?  63  ASN B ND2  1 
ATOM   6433  H H    . ASN B 1 54  ? -13.236 -7.696  88.664  1.00 136.15 ?  63  ASN B H    1 
ATOM   6434  H HA   . ASN B 1 54  ? -13.235 -9.829  90.293  1.00 133.43 ?  63  ASN B HA   1 
ATOM   6435  H HB2  . ASN B 1 54  ? -14.012 -9.680  87.581  1.00 138.04 ?  63  ASN B HB2  1 
ATOM   6436  H HB3  . ASN B 1 54  ? -14.165 -10.984 88.477  1.00 138.04 ?  63  ASN B HB3  1 
ATOM   6437  H HD21 . ASN B 1 54  ? -16.616 -9.427  90.505  1.00 143.09 ?  63  ASN B HD21 1 
ATOM   6438  H HD22 . ASN B 1 54  ? -15.279 -10.029 90.765  1.00 143.09 ?  63  ASN B HD22 1 
ATOM   6439  N N    . MET B 1 55  ? -11.520 -11.357 89.373  1.00 230.46 ?  64  MET B N    1 
ATOM   6440  C CA   . MET B 1 55  ? -10.357 -12.104 88.925  1.00 114.86 ?  64  MET B CA   1 
ATOM   6441  C C    . MET B 1 55  ? -10.640 -12.612 87.520  1.00 111.69 ?  64  MET B C    1 
ATOM   6442  O O    . MET B 1 55  ? -11.378 -13.577 87.342  1.00 112.69 ?  64  MET B O    1 
ATOM   6443  C CB   . MET B 1 55  ? -10.084 -13.233 89.895  1.00 168.79 ?  64  MET B CB   1 
ATOM   6444  C CG   . MET B 1 55  ? -8.812  -13.924 89.685  1.00 156.04 ?  64  MET B CG   1 
ATOM   6445  S SD   . MET B 1 55  ? -8.548  -14.954 91.127  1.00 265.78 ?  64  MET B SD   1 
ATOM   6446  H H    . MET B 1 55  ? -12.030 -11.785 89.918  1.00 276.55 ?  64  MET B H    1 
ATOM   6447  H HA   . MET B 1 55  ? -9.583  -11.519 88.908  1.00 137.83 ?  64  MET B HA   1 
ATOM   6448  H HB2  . MET B 1 55  ? -10.076 -12.872 90.796  1.00 202.55 ?  64  MET B HB2  1 
ATOM   6449  H HB3  . MET B 1 55  ? -10.792 -13.890 89.813  1.00 202.55 ?  64  MET B HB3  1 
ATOM   6450  H HG2  . MET B 1 55  ? -8.862  -14.486 88.896  1.00 187.25 ?  64  MET B HG2  1 
ATOM   6451  H HG3  . MET B 1 55  ? -8.089  -13.282 89.614  1.00 187.25 ?  64  MET B HG3  1 
ATOM   6452  N N    . LEU B 1 56  ? -10.086 -11.939 86.510  1.00 160.88 ?  65  LEU B N    1 
ATOM   6453  C CA   . LEU B 1 56  ? -10.250 -12.308 85.105  1.00 145.08 ?  65  LEU B CA   1 
ATOM   6454  C C    . LEU B 1 56  ? -9.223  -13.339 84.625  1.00 123.07 ?  65  LEU B C    1 
ATOM   6455  O O    . LEU B 1 56  ? -8.205  -13.588 85.267  1.00 110.26 ?  65  LEU B O    1 
ATOM   6456  C CB   . LEU B 1 56  ? -10.160 -11.081 84.203  1.00 153.49 ?  65  LEU B CB   1 
ATOM   6457  C CG   . LEU B 1 56  ? -11.162 -9.965  84.432  1.00 138.89 ?  65  LEU B CG   1 
ATOM   6458  C CD1  . LEU B 1 56  ? -11.057 -8.958  83.289  1.00 142.70 ?  65  LEU B CD1  1 
ATOM   6459  C CD2  . LEU B 1 56  ? -12.582 -10.500 84.558  1.00 152.72 ?  65  LEU B CD2  1 
ATOM   6460  H H    . LEU B 1 56  ? -9.595  -11.241 86.621  1.00 193.05 ?  65  LEU B H    1 
ATOM   6461  H HA   . LEU B 1 56  ? -11.131 -12.695 84.988  1.00 174.09 ?  65  LEU B HA   1 
ATOM   6462  H HB2  . LEU B 1 56  ? -9.276  -10.694 84.311  1.00 184.19 ?  65  LEU B HB2  1 
ATOM   6463  H HB3  . LEU B 1 56  ? -10.268 -11.375 83.285  1.00 184.19 ?  65  LEU B HB3  1 
ATOM   6464  H HG   . LEU B 1 56  ? -10.941 -9.506  85.258  1.00 166.66 ?  65  LEU B HG   1 
ATOM   6465  H HD11 . LEU B 1 56  ? -11.699 -8.245  83.436  1.00 171.24 ?  65  LEU B HD11 1 
ATOM   6466  H HD12 . LEU B 1 56  ? -10.158 -8.595  83.270  1.00 171.24 ?  65  LEU B HD12 1 
ATOM   6467  H HD13 . LEU B 1 56  ? -11.250 -9.409  82.452  1.00 171.24 ?  65  LEU B HD13 1 
ATOM   6468  H HD21 . LEU B 1 56  ? -13.188 -9.756  84.703  1.00 183.27 ?  65  LEU B HD21 1 
ATOM   6469  H HD22 . LEU B 1 56  ? -12.818 -10.964 83.740  1.00 183.27 ?  65  LEU B HD22 1 
ATOM   6470  H HD23 . LEU B 1 56  ? -12.623 -11.112 85.310  1.00 183.27 ?  65  LEU B HD23 1 
ATOM   6471  N N    . SER B 1 57  ? -9.544  -13.962 83.481  1.00 164.32 ?  66  SER B N    1 
ATOM   6472  C CA   . SER B 1 57  ? -8.697  -14.921 82.772  1.00 215.06 ?  66  SER B CA   1 
ATOM   6473  C C    . SER B 1 57  ? -7.777  -14.227 81.763  1.00 144.06 ?  66  SER B C    1 
ATOM   6474  O O    . SER B 1 57  ? -8.107  -13.166 81.230  1.00 152.02 ?  66  SER B O    1 
ATOM   6475  C CB   . SER B 1 57  ? -9.575  -15.945 82.051  1.00 298.85 ?  66  SER B CB   1 
ATOM   6476  O OG   . SER B 1 57  ? -8.803  -16.878 81.322  1.00 232.38 ?  66  SER B OG   1 
ATOM   6477  H H    . SER B 1 57  ? -10.293 -13.832 83.079  1.00 197.19 ?  66  SER B H    1 
ATOM   6478  H HA   . SER B 1 57  ? -8.143  -15.394 83.413  1.00 258.07 ?  66  SER B HA   1 
ATOM   6479  H HB2  . SER B 1 57  ? -10.103 -16.423 82.710  1.00 358.62 ?  66  SER B HB2  1 
ATOM   6480  H HB3  . SER B 1 57  ? -10.162 -15.477 81.437  1.00 358.62 ?  66  SER B HB3  1 
ATOM   6481  H HG   . SER B 1 57  ? -9.307  -17.428 80.936  1.00 278.85 ?  66  SER B HG   1 
ATOM   6482  N N    . ILE B 1 58  ? -6.619  -14.842 81.489  1.00 125.72 ?  67  ILE B N    1 
ATOM   6483  C CA   . ILE B 1 58  ? -5.673  -14.293 80.515  1.00 104.90 ?  67  ILE B CA   1 
ATOM   6484  C C    . ILE B 1 58  ? -5.805  -14.899 79.106  1.00 108.21 ?  67  ILE B C    1 
ATOM   6485  O O    . ILE B 1 58  ? -5.062  -14.491 78.201  1.00 115.94 ?  67  ILE B O    1 
ATOM   6486  C CB   . ILE B 1 58  ? -4.216  -14.429 81.029  1.00 139.36 ?  67  ILE B CB   1 
ATOM   6487  C CG1  . ILE B 1 58  ? -3.826  -15.889 81.190  1.00 170.95 ?  67  ILE B CG1  1 
ATOM   6488  C CG2  . ILE B 1 58  ? -4.001  -13.713 82.367  1.00 115.78 ?  67  ILE B CG2  1 
ATOM   6489  C CD1  . ILE B 1 58  ? -2.886  -16.351 80.127  1.00 178.53 ?  67  ILE B CD1  1 
ATOM   6490  H H    . ILE B 1 58  ? -6.361  -15.576 81.854  1.00 150.86 ?  67  ILE B H    1 
ATOM   6491  H HA   . ILE B 1 58  ? -5.853  -13.343 80.429  1.00 125.88 ?  67  ILE B HA   1 
ATOM   6492  H HB   . ILE B 1 58  ? -3.625  -14.029 80.373  1.00 167.23 ?  67  ILE B HB   1 
ATOM   6493  H HG12 . ILE B 1 58  ? -3.391  -16.008 82.049  1.00 205.14 ?  67  ILE B HG12 1 
ATOM   6494  H HG13 . ILE B 1 58  ? -4.625  -16.437 81.144  1.00 205.14 ?  67  ILE B HG13 1 
ATOM   6495  H HG21 . ILE B 1 58  ? -3.078  -13.829 82.642  1.00 138.94 ?  67  ILE B HG21 1 
ATOM   6496  H HG22 . ILE B 1 58  ? -4.196  -12.769 82.255  1.00 138.94 ?  67  ILE B HG22 1 
ATOM   6497  H HG23 . ILE B 1 58  ? -4.595  -14.097 83.030  1.00 138.94 ?  67  ILE B HG23 1 
ATOM   6498  H HD11 . ILE B 1 58  ? -2.672  -17.285 80.279  1.00 214.23 ?  67  ILE B HD11 1 
ATOM   6499  H HD12 . ILE B 1 58  ? -3.312  -16.245 79.262  1.00 214.23 ?  67  ILE B HD12 1 
ATOM   6500  H HD13 . ILE B 1 58  ? -2.078  -15.815 80.166  1.00 214.23 ?  67  ILE B HD13 1 
ATOM   6501  N N    . ASP B 1 59  ? -6.756  -15.810 78.875  1.00 199.23 ?  68  ASP B N    1 
ATOM   6502  C CA   . ASP B 1 59  ? -6.759  -16.638 77.666  1.00 142.06 ?  68  ASP B CA   1 
ATOM   6503  C C    . ASP B 1 59  ? -7.196  -15.931 76.396  1.00 126.07 ?  68  ASP B C    1 
ATOM   6504  O O    . ASP B 1 59  ? -6.975  -16.471 75.310  1.00 119.41 ?  68  ASP B O    1 
ATOM   6505  C CB   . ASP B 1 59  ? -7.685  -17.820 77.852  1.00 179.38 ?  68  ASP B CB   1 
ATOM   6506  C CG   . ASP B 1 59  ? -7.359  -18.605 79.067  1.00 210.95 ?  68  ASP B CG   1 
ATOM   6507  O OD1  . ASP B 1 59  ? -6.348  -18.271 79.711  1.00 211.51 ?  68  ASP B OD1  1 
ATOM   6508  O OD2  . ASP B 1 59  ? -8.120  -19.534 79.394  1.00 228.76 -1 68  ASP B OD2  1 
ATOM   6509  H H    . ASP B 1 59  ? -7.414  -15.968 79.406  1.00 239.08 ?  68  ASP B H    1 
ATOM   6510  H HA   . ASP B 1 59  ? -5.864  -16.981 77.521  1.00 170.47 ?  68  ASP B HA   1 
ATOM   6511  H HB2  . ASP B 1 59  ? -8.597  -17.499 77.937  1.00 215.25 ?  68  ASP B HB2  1 
ATOM   6512  H HB3  . ASP B 1 59  ? -7.609  -18.407 77.084  1.00 215.25 ?  68  ASP B HB3  1 
ATOM   6513  N N    . HIS B 1 60  ? -7.771  -14.747 76.481  1.00 155.18 ?  69  HIS B N    1 
ATOM   6514  C CA   . HIS B 1 60  ? -8.234  -14.046 75.294  1.00 163.91 ?  69  HIS B CA   1 
ATOM   6515  C C    . HIS B 1 60  ? -7.194  -13.098 74.750  1.00 156.20 ?  69  HIS B C    1 
ATOM   6516  O O    . HIS B 1 60  ? -7.499  -12.262 73.894  1.00 167.48 ?  69  HIS B O    1 
ATOM   6517  C CB   . HIS B 1 60  ? -9.528  -13.329 75.629  1.00 160.90 ?  69  HIS B CB   1 
ATOM   6518  C CG   . HIS B 1 60  ? -10.601 -14.274 76.060  1.00 178.11 ?  69  HIS B CG   1 
ATOM   6519  N ND1  . HIS B 1 60  ? -10.797 -14.617 77.379  1.00 261.54 ?  69  HIS B ND1  1 
ATOM   6520  C CD2  . HIS B 1 60  ? -11.525 -14.962 75.349  1.00 141.31 ?  69  HIS B CD2  1 
ATOM   6521  C CE1  . HIS B 1 60  ? -11.786 -15.487 77.464  1.00 123.87 ?  69  HIS B CE1  1 
ATOM   6522  N NE2  . HIS B 1 60  ? -12.255 -15.701 76.247  1.00 161.97 ?  69  HIS B NE2  1 
ATOM   6523  H H    . HIS B 1 60  ? -7.908  -14.323 77.216  1.00 186.22 ?  69  HIS B H    1 
ATOM   6524  H HA   . HIS B 1 60  ? -8.428  -14.698 74.603  1.00 196.70 ?  69  HIS B HA   1 
ATOM   6525  H HB2  . HIS B 1 60  ? -9.367  -12.704 76.354  1.00 193.08 ?  69  HIS B HB2  1 
ATOM   6526  H HB3  . HIS B 1 60  ? -9.842  -12.854 74.844  1.00 193.08 ?  69  HIS B HB3  1 
ATOM   6527  H HD2  . HIS B 1 60  ? -11.644 -14.937 74.427  1.00 169.58 ?  69  HIS B HD2  1 
ATOM   6528  H HE1  . HIS B 1 60  ? -12.116 -15.862 78.248  1.00 148.64 ?  69  HIS B HE1  1 
ATOM   6529  H HE2  . HIS B 1 60  ? -12.907 -16.225 76.049  1.00 194.36 ?  69  HIS B HE2  1 
ATOM   6530  N N    . LEU B 1 61  ? -5.975  -13.237 75.218  1.00 211.79 ?  70  LEU B N    1 
ATOM   6531  C CA   . LEU B 1 61  ? -4.825  -12.507 74.727  1.00 158.40 ?  70  LEU B CA   1 
ATOM   6532  C C    . LEU B 1 61  ? -4.110  -13.465 73.784  1.00 115.40 ?  70  LEU B C    1 
ATOM   6533  O O    . LEU B 1 61  ? -3.445  -14.399 74.233  1.00 112.10 ?  70  LEU B O    1 
ATOM   6534  C CB   . LEU B 1 61  ? -3.983  -12.081 75.918  1.00 162.11 ?  70  LEU B CB   1 
ATOM   6535  C CG   . LEU B 1 61  ? -4.747  -11.179 76.887  1.00 228.67 ?  70  LEU B CG   1 
ATOM   6536  C CD1  . LEU B 1 61  ? -4.074  -11.126 78.224  1.00 175.57 ?  70  LEU B CD1  1 
ATOM   6537  C CD2  . LEU B 1 61  ? -4.833  -9.771  76.329  1.00 156.74 ?  70  LEU B CD2  1 
ATOM   6538  H H    . LEU B 1 61  ? -5.777  -13.778 75.857  1.00 254.15 ?  70  LEU B H    1 
ATOM   6539  H HA   . LEU B 1 61  ? -5.109  -11.721 74.234  1.00 190.08 ?  70  LEU B HA   1 
ATOM   6540  H HB2  . LEU B 1 61  ? -3.700  -12.872 76.404  1.00 194.53 ?  70  LEU B HB2  1 
ATOM   6541  H HB3  . LEU B 1 61  ? -3.208  -11.592 75.599  1.00 194.53 ?  70  LEU B HB3  1 
ATOM   6542  H HG   . LEU B 1 61  ? -5.648  -11.519 77.007  1.00 274.41 ?  70  LEU B HG   1 
ATOM   6543  H HD11 . LEU B 1 61  ? -4.585  -10.546 78.811  1.00 210.69 ?  70  LEU B HD11 1 
ATOM   6544  H HD12 . LEU B 1 61  ? -4.037  -12.022 78.594  1.00 210.69 ?  70  LEU B HD12 1 
ATOM   6545  H HD13 . LEU B 1 61  ? -3.177  -10.776 78.112  1.00 210.69 ?  70  LEU B HD13 1 
ATOM   6546  H HD21 . LEU B 1 61  ? -5.320  -9.213  76.955  1.00 188.09 ?  70  LEU B HD21 1 
ATOM   6547  H HD22 . LEU B 1 61  ? -3.935  -9.425  76.206  1.00 188.09 ?  70  LEU B HD22 1 
ATOM   6548  H HD23 . LEU B 1 61  ? -5.297  -9.797  75.477  1.00 188.09 ?  70  LEU B HD23 1 
ATOM   6549  N N    . THR B 1 62  ? -4.294  -13.273 72.474  1.00 176.95 ?  71  THR B N    1 
ATOM   6550  C CA   . THR B 1 62  ? -3.894  -14.285 71.499  1.00 205.13 ?  71  THR B CA   1 
ATOM   6551  C C    . THR B 1 62  ? -2.482  -14.039 70.959  1.00 129.40 ?  71  THR B C    1 
ATOM   6552  O O    . THR B 1 62  ? -1.606  -14.887 71.135  1.00 137.25 ?  71  THR B O    1 
ATOM   6553  C CB   . THR B 1 62  ? -4.925  -14.360 70.365  1.00 145.70 ?  71  THR B CB   1 
ATOM   6554  O OG1  . THR B 1 62  ? -4.573  -13.463 69.311  1.00 171.20 ?  71  THR B OG1  1 
ATOM   6555  C CG2  . THR B 1 62  ? -6.303  -14.000 70.881  1.00 150.99 ?  71  THR B CG2  1 
ATOM   6556  H H    . THR B 1 62  ? -4.647  -12.569 72.129  1.00 212.34 ?  71  THR B H    1 
ATOM   6557  H HA   . THR B 1 62  ? -3.887  -15.148 71.941  1.00 246.15 ?  71  THR B HA   1 
ATOM   6558  H HB   . THR B 1 62  ? -4.956  -15.266 70.019  1.00 174.83 ?  71  THR B HB   1 
ATOM   6559  H HG1  . THR B 1 62  ? -5.140  -13.508 68.693  1.00 205.44 ?  71  THR B HG1  1 
ATOM   6560  H HG21 . THR B 1 62  ? -6.950  -14.049 70.160  1.00 181.19 ?  71  THR B HG21 1 
ATOM   6561  H HG22 . THR B 1 62  ? -6.566  -14.616 71.583  1.00 181.19 ?  71  THR B HG22 1 
ATOM   6562  H HG23 . THR B 1 62  ? -6.298  -13.098 71.238  1.00 181.19 ?  71  THR B HG23 1 
ATOM   6563  N N    . ASP B 1 63  ? -2.246  -12.910 70.285  1.00 150.72 ?  72  ASP B N    1 
ATOM   6564  C CA   . ASP B 1 63  ? -0.929  -12.641 69.703  1.00 212.55 ?  72  ASP B CA   1 
ATOM   6565  C C    . ASP B 1 63  ? 0.031   -12.045 70.737  1.00 274.94 ?  72  ASP B C    1 
ATOM   6566  O O    . ASP B 1 63  ? -0.375  -11.549 71.788  1.00 173.26 ?  72  ASP B O    1 
ATOM   6567  C CB   . ASP B 1 63  ? -1.032  -11.717 68.486  1.00 175.19 ?  72  ASP B CB   1 
ATOM   6568  C CG   . ASP B 1 63  ? -1.778  -10.446 68.773  1.00 152.28 ?  72  ASP B CG   1 
ATOM   6569  O OD1  . ASP B 1 63  ? -2.825  -10.505 69.442  1.00 159.77 ?  72  ASP B OD1  1 
ATOM   6570  O OD2  . ASP B 1 63  ? -1.322  -9.386  68.310  1.00 150.93 -1 72  ASP B OD2  1 
ATOM   6571  H H    . ASP B 1 63  ? -2.826  -12.289 70.152  1.00 180.87 ?  72  ASP B H    1 
ATOM   6572  H HA   . ASP B 1 63  ? -0.549  -13.481 69.401  1.00 255.06 ?  72  ASP B HA   1 
ATOM   6573  H HB2  . ASP B 1 63  ? -0.138  -11.480 68.195  1.00 210.22 ?  72  ASP B HB2  1 
ATOM   6574  H HB3  . ASP B 1 63  ? -1.499  -12.184 67.775  1.00 210.22 ?  72  ASP B HB3  1 
ATOM   6575  N N    . HIS B 1 64  ? 1.331   -12.105 70.422  1.00 136.15 ?  73  HIS B N    1 
ATOM   6576  C CA   . HIS B 1 64  ? 2.345   -11.600 71.352  1.00 141.56 ?  73  HIS B CA   1 
ATOM   6577  C C    . HIS B 1 64  ? 2.101   -10.134 71.691  1.00 112.72 ?  73  HIS B C    1 
ATOM   6578  O O    . HIS B 1 64  ? 2.140   -9.758  72.864  1.00 98.80  ?  73  HIS B O    1 
ATOM   6579  C CB   . HIS B 1 64  ? 3.763   -11.804 70.760  1.00 156.59 ?  73  HIS B CB   1 
ATOM   6580  C CG   . HIS B 1 64  ? 4.926   -11.353 71.637  1.00 117.79 ?  73  HIS B CG   1 
ATOM   6581  N ND1  . HIS B 1 64  ? 5.276   -11.988 72.811  1.00 97.40  ?  73  HIS B ND1  1 
ATOM   6582  C CD2  . HIS B 1 64  ? 5.858   -10.380 71.466  1.00 104.47 ?  73  HIS B CD2  1 
ATOM   6583  C CE1  . HIS B 1 64  ? 6.342   -11.410 73.340  1.00 75.70  ?  73  HIS B CE1  1 
ATOM   6584  N NE2  . HIS B 1 64  ? 6.712   -10.426 72.544  1.00 152.88 ?  73  HIS B NE2  1 
ATOM   6585  H H    . HIS B 1 64  ? 1.645   -12.427 69.689  1.00 163.38 ?  73  HIS B H    1 
ATOM   6586  H HA   . HIS B 1 64  ? 2.292   -12.108 72.176  1.00 169.88 ?  73  HIS B HA   1 
ATOM   6587  H HB2  . HIS B 1 64  ? 3.886   -12.749 70.580  1.00 187.90 ?  73  HIS B HB2  1 
ATOM   6588  H HB3  . HIS B 1 64  ? 3.821   -11.308 69.928  1.00 187.90 ?  73  HIS B HB3  1 
ATOM   6589  H HD2  . HIS B 1 64  ? 5.897   -9.776  70.760  1.00 125.37 ?  73  HIS B HD2  1 
ATOM   6590  H HE1  . HIS B 1 64  ? 6.755   -11.651 74.138  1.00 90.84  ?  73  HIS B HE1  1 
ATOM   6591  N N    . LYS B 1 65  ? 1.781   -9.300  70.697  1.00 130.15 ?  74  LYS B N    1 
ATOM   6592  C CA   . LYS B 1 65  ? 1.760   -7.854  70.939  1.00 109.45 ?  74  LYS B CA   1 
ATOM   6593  C C    . LYS B 1 65  ? 0.721   -7.487  71.984  1.00 91.31  ?  74  LYS B C    1 
ATOM   6594  O O    . LYS B 1 65  ? 0.930   -6.569  72.798  1.00 75.91  ?  74  LYS B O    1 
ATOM   6595  C CB   . LYS B 1 65  ? 1.485   -7.087  69.635  1.00 103.74 ?  74  LYS B CB   1 
ATOM   6596  C CG   . LYS B 1 65  ? 2.616   -7.108  68.563  1.00 91.15  ?  74  LYS B CG   1 
ATOM   6597  C CD   . LYS B 1 65  ? 2.332   -6.204  67.335  1.00 88.07  ?  74  LYS B CD   1 
ATOM   6598  C CE   . LYS B 1 65  ? 3.459   -6.271  66.275  1.00 122.87 ?  74  LYS B CE   1 
ATOM   6599  N NZ   . LYS B 1 65  ? 3.250   -5.470  65.019  1.00 176.40 1  74  LYS B NZ   1 
ATOM   6600  H H    . LYS B 1 65  ? 1.578   -9.537  69.895  1.00 156.18 ?  74  LYS B H    1 
ATOM   6601  H HA   . LYS B 1 65  ? 2.628   -7.578  71.271  1.00 131.34 ?  74  LYS B HA   1 
ATOM   6602  H HB2  . LYS B 1 65  ? 0.692   -7.463  69.224  1.00 124.48 ?  74  LYS B HB2  1 
ATOM   6603  H HB3  . LYS B 1 65  ? 1.320   -6.158  69.860  1.00 124.48 ?  74  LYS B HB3  1 
ATOM   6604  H HG2  . LYS B 1 65  ? 3.440   -6.802  68.972  1.00 109.38 ?  74  LYS B HG2  1 
ATOM   6605  H HG3  . LYS B 1 65  ? 2.726   -8.017  68.242  1.00 109.38 ?  74  LYS B HG3  1 
ATOM   6606  H HD2  . LYS B 1 65  ? 1.506   -6.491  66.915  1.00 105.69 ?  74  LYS B HD2  1 
ATOM   6607  H HD3  . LYS B 1 65  ? 2.252   -5.284  67.632  1.00 105.69 ?  74  LYS B HD3  1 
ATOM   6608  H HE2  . LYS B 1 65  ? 4.279   -5.953  66.684  1.00 147.44 ?  74  LYS B HE2  1 
ATOM   6609  H HE3  . LYS B 1 65  ? 3.570   -7.197  66.009  1.00 147.44 ?  74  LYS B HE3  1 
ATOM   6610  H HZ1  . LYS B 1 65  ? 3.947   -5.572  64.474  1.00 211.68 ?  74  LYS B HZ1  1 
ATOM   6611  H HZ2  . LYS B 1 65  ? 2.514   -5.746  64.601  1.00 211.68 ?  74  LYS B HZ2  1 
ATOM   6612  H HZ3  . LYS B 1 65  ? 3.163   -4.607  65.219  1.00 211.68 ?  74  LYS B HZ3  1 
ATOM   6613  N N    . SER B 1 66  ? -0.426  -8.162  71.931  1.00 110.65 ?  75  SER B N    1 
ATOM   6614  C CA   . SER B 1 66  ? -1.515  -7.941  72.872  1.00 116.45 ?  75  SER B CA   1 
ATOM   6615  C C    . SER B 1 66  ? -1.185  -8.496  74.248  1.00 90.94  ?  75  SER B C    1 
ATOM   6616  O O    . SER B 1 66  ? -1.638  -7.963  75.274  1.00 77.90  ?  75  SER B O    1 
ATOM   6617  C CB   . SER B 1 66  ? -2.799  -8.589  72.341  1.00 165.84 ?  75  SER B CB   1 
ATOM   6618  O OG   . SER B 1 66  ? -3.263  -7.945  71.161  1.00 177.10 ?  75  SER B OG   1 
ATOM   6619  H H    . SER B 1 66  ? -0.597  -8.768  71.345  1.00 132.78 ?  75  SER B H    1 
ATOM   6620  H HA   . SER B 1 66  ? -1.671  -6.987  72.961  1.00 139.74 ?  75  SER B HA   1 
ATOM   6621  H HB2  . SER B 1 66  ? -2.619  -9.520  72.139  1.00 199.01 ?  75  SER B HB2  1 
ATOM   6622  H HB3  . SER B 1 66  ? -3.486  -8.526  73.022  1.00 199.01 ?  75  SER B HB3  1 
ATOM   6623  H HG   . SER B 1 66  ? -2.679  -7.993  70.559  1.00 212.51 ?  75  SER B HG   1 
ATOM   6624  N N    . GLN B 1 67  ? -0.391  -9.556  74.301  1.00 90.84  ?  76  GLN B N    1 
ATOM   6625  C CA   . GLN B 1 67  ? 0.065   -10.045 75.597  1.00 88.68  ?  76  GLN B CA   1 
ATOM   6626  C C    . GLN B 1 67  ? 1.066   -9.058  76.231  1.00 90.36  ?  76  GLN B C    1 
ATOM   6627  O O    . GLN B 1 67  ? 1.078   -8.884  77.452  1.00 93.13  ?  76  GLN B O    1 
ATOM   6628  C CB   . GLN B 1 67  ? 0.649   -11.447 75.418  1.00 86.00  ?  76  GLN B CB   1 
ATOM   6629  C CG   . GLN B 1 67  ? -0.281  -12.419 74.810  1.00 148.83 ?  76  GLN B CG   1 
ATOM   6630  C CD   . GLN B 1 67  ? 0.382   -13.716 74.507  1.00 151.12 ?  76  GLN B CD   1 
ATOM   6631  O OE1  . GLN B 1 67  ? 0.890   -14.386 75.397  1.00 183.40 ?  76  GLN B OE1  1 
ATOM   6632  N NE2  . GLN B 1 67  ? 0.418   -14.071 73.240  1.00 121.75 ?  76  GLN B NE2  1 
ATOM   6633  H H    . GLN B 1 67  ? -0.107  -10.001 73.623  1.00 109.01 ?  76  GLN B H    1 
ATOM   6634  H HA   . GLN B 1 67  ? -0.698  -10.115 76.191  1.00 106.42 ?  76  GLN B HA   1 
ATOM   6635  H HB2  . GLN B 1 67  ? 1.430   -11.389 74.846  1.00 103.20 ?  76  GLN B HB2  1 
ATOM   6636  H HB3  . GLN B 1 67  ? 0.906   -11.790 76.288  1.00 103.20 ?  76  GLN B HB3  1 
ATOM   6637  H HG2  . GLN B 1 67  ? -1.011  -12.589 75.426  1.00 178.60 ?  76  GLN B HG2  1 
ATOM   6638  H HG3  . GLN B 1 67  ? -0.624  -12.053 73.979  1.00 178.60 ?  76  GLN B HG3  1 
ATOM   6639  H HE21 . GLN B 1 67  ? 0.070   -13.561 72.641  1.00 146.09 ?  76  GLN B HE21 1 
ATOM   6640  H HE22 . GLN B 1 67  ? 0.790   -14.812 73.012  1.00 146.09 ?  76  GLN B HE22 1 
ATOM   6641  N N    . ARG B 1 68  ? 1.915   -8.405  75.427  1.00 86.35  ?  77  ARG B N    1 
ATOM   6642  C CA   . ARG B 1 68  ? 2.839   -7.426  75.985  1.00 100.68 ?  77  ARG B CA   1 
ATOM   6643  C C    . ARG B 1 68  ? 2.096   -6.166  76.404  1.00 112.74 ?  77  ARG B C    1 
ATOM   6644  O O    . ARG B 1 68  ? 2.401   -5.579  77.451  1.00 113.52 ?  77  ARG B O    1 
ATOM   6645  C CB   . ARG B 1 68  ? 3.928   -7.089  74.952  1.00 110.88 ?  77  ARG B CB   1 
ATOM   6646  C CG   . ARG B 1 68  ? 4.966   -8.194  74.681  1.00 107.40 ?  77  ARG B CG   1 
ATOM   6647  C CD   . ARG B 1 68  ? 6.026   -8.319  75.783  1.00 82.17  ?  77  ARG B CD   1 
ATOM   6648  N NE   . ARG B 1 68  ? 6.851   -7.113  75.842  1.00 65.47  ?  77  ARG B NE   1 
ATOM   6649  C CZ   . ARG B 1 68  ? 7.917   -6.893  75.072  1.00 72.39  ?  77  ARG B CZ   1 
ATOM   6650  N NH1  . ARG B 1 68  ? 8.325   -7.816  74.202  1.00 74.11  1  77  ARG B NH1  1 
ATOM   6651  N NH2  . ARG B 1 68  ? 8.572   -5.739  75.173  1.00 78.40  1  77  ARG B NH2  1 
ATOM   6652  H H    . ARG B 1 68  ? 1.972   -8.512  74.575  1.00 103.63 ?  77  ARG B H    1 
ATOM   6653  H HA   . ARG B 1 68  ? 3.269   -7.801  76.769  1.00 120.81 ?  77  ARG B HA   1 
ATOM   6654  H HB2  . ARG B 1 68  ? 3.495   -6.885  74.108  1.00 133.06 ?  77  ARG B HB2  1 
ATOM   6655  H HB3  . ARG B 1 68  ? 4.412   -6.308  75.263  1.00 133.06 ?  77  ARG B HB3  1 
ATOM   6656  H HG2  . ARG B 1 68  ? 4.507   -9.045  74.612  1.00 128.88 ?  77  ARG B HG2  1 
ATOM   6657  H HG3  . ARG B 1 68  ? 5.423   -7.997  73.849  1.00 128.88 ?  77  ARG B HG3  1 
ATOM   6658  H HD2  . ARG B 1 68  ? 5.588   -8.433  76.641  1.00 98.61  ?  77  ARG B HD2  1 
ATOM   6659  H HD3  . ARG B 1 68  ? 6.602   -9.076  75.592  1.00 98.61  ?  77  ARG B HD3  1 
ATOM   6660  H HE   . ARG B 1 68  ? 6.635   -6.506  76.411  1.00 78.57  ?  77  ARG B HE   1 
ATOM   6661  H HH11 . ARG B 1 68  ? 7.894   -8.557  74.127  1.00 88.93  ?  77  ARG B HH11 1 
ATOM   6662  H HH12 . ARG B 1 68  ? 9.017   -7.670  73.713  1.00 88.93  ?  77  ARG B HH12 1 
ATOM   6663  H HH21 . ARG B 1 68  ? 8.315   -5.147  75.741  1.00 94.08  ?  77  ARG B HH21 1 
ATOM   6664  H HH22 . ARG B 1 68  ? 9.272   -5.599  74.693  1.00 94.08  ?  77  ARG B HH22 1 
ATOM   6665  N N    . LEU B 1 69  ? 1.070   -5.780  75.635  1.00 108.77 ?  78  LEU B N    1 
ATOM   6666  C CA   . LEU B 1 69  ? 0.270   -4.610  75.979  1.00 99.44  ?  78  LEU B CA   1 
ATOM   6667  C C    . LEU B 1 69  ? -0.489  -4.850  77.261  1.00 103.00 ?  78  LEU B C    1 
ATOM   6668  O O    . LEU B 1 69  ? -0.699  -3.921  78.041  1.00 149.26 ?  78  LEU B O    1 
ATOM   6669  C CB   . LEU B 1 69  ? -0.702  -4.274  74.855  1.00 113.46 ?  78  LEU B CB   1 
ATOM   6670  C CG   . LEU B 1 69  ? -1.725  -3.191  75.193  1.00 111.21 ?  78  LEU B CG   1 
ATOM   6671  C CD1  . LEU B 1 69  ? -1.056  -1.892  75.503  1.00 132.59 ?  78  LEU B CD1  1 
ATOM   6672  C CD2  . LEU B 1 69  ? -2.736  -3.010  74.079  1.00 158.88 ?  78  LEU B CD2  1 
ATOM   6673  H H    . LEU B 1 69  ? 0.822   -6.179  74.915  1.00 130.53 ?  78  LEU B H    1 
ATOM   6674  H HA   . LEU B 1 69  ? 0.857   -3.849  76.111  1.00 119.33 ?  78  LEU B HA   1 
ATOM   6675  H HB2  . LEU B 1 69  ? -0.194  -3.967  74.088  1.00 136.15 ?  78  LEU B HB2  1 
ATOM   6676  H HB3  . LEU B 1 69  ? -1.192  -5.077  74.620  1.00 136.15 ?  78  LEU B HB3  1 
ATOM   6677  H HG   . LEU B 1 69  ? -2.212  -3.465  75.986  1.00 133.45 ?  78  LEU B HG   1 
ATOM   6678  H HD11 . LEU B 1 69  ? -1.734  -1.230  75.712  1.00 159.11 ?  78  LEU B HD11 1 
ATOM   6679  H HD12 . LEU B 1 69  ? -0.467  -2.014  76.264  1.00 159.11 ?  78  LEU B HD12 1 
ATOM   6680  H HD13 . LEU B 1 69  ? -0.544  -1.609  74.730  1.00 159.11 ?  78  LEU B HD13 1 
ATOM   6681  H HD21 . LEU B 1 69  ? -3.364  -2.316  74.334  1.00 190.66 ?  78  LEU B HD21 1 
ATOM   6682  H HD22 . LEU B 1 69  ? -2.269  -2.753  73.269  1.00 190.66 ?  78  LEU B HD22 1 
ATOM   6683  H HD23 . LEU B 1 69  ? -3.206  -3.847  73.940  1.00 190.66 ?  78  LEU B HD23 1 
ATOM   6684  N N    . ALA B 1 70  ? -0.925  -6.081  77.479  1.00 130.73 ?  79  ALA B N    1 
ATOM   6685  C CA   . ALA B 1 70  ? -1.557  -6.410  78.738  1.00 121.97 ?  79  ALA B CA   1 
ATOM   6686  C C    . ALA B 1 70  ? -0.536  -6.369  79.865  1.00 105.80 ?  79  ALA B C    1 
ATOM   6687  O O    . ALA B 1 70  ? -0.789  -5.810  80.934  1.00 80.04  ?  79  ALA B O    1 
ATOM   6688  C CB   . ALA B 1 70  ? -2.199  -7.785  78.629  1.00 71.42  ?  79  ALA B CB   1 
ATOM   6689  H H    . ALA B 1 70  ? -0.868  -6.733  76.922  1.00 156.87 ?  79  ALA B H    1 
ATOM   6690  H HA   . ALA B 1 70  ? -2.252  -5.761  78.931  1.00 146.36 ?  79  ALA B HA   1 
ATOM   6691  H HB1  . ALA B 1 70  ? -2.622  -8.003  79.474  1.00 85.70  ?  79  ALA B HB1  1 
ATOM   6692  H HB2  . ALA B 1 70  ? -2.862  -7.767  77.921  1.00 85.70  ?  79  ALA B HB2  1 
ATOM   6693  H HB3  . ALA B 1 70  ? -1.512  -8.438  78.423  1.00 85.70  ?  79  ALA B HB3  1 
ATOM   6694  N N    . ARG B 1 71  ? 0.656   -6.894  79.621  1.00 99.51  ?  80  ARG B N    1 
ATOM   6695  C CA   . ARG B 1 71  ? 1.658   -6.922  80.677  1.00 85.43  ?  80  ARG B CA   1 
ATOM   6696  C C    . ARG B 1 71  ? 2.143   -5.534  81.000  1.00 72.06  ?  80  ARG B C    1 
ATOM   6697  O O    . ARG B 1 71  ? 2.727   -5.313  82.066  1.00 88.42  ?  80  ARG B O    1 
ATOM   6698  C CB   . ARG B 1 71  ? 2.834   -7.774  80.268  1.00 114.63 ?  80  ARG B CB   1 
ATOM   6699  C CG   . ARG B 1 71  ? 3.451   -8.473  81.425  1.00 112.01 ?  80  ARG B CG   1 
ATOM   6700  C CD   . ARG B 1 71  ? 4.874   -8.774  81.152  1.00 108.52 ?  80  ARG B CD   1 
ATOM   6701  N NE   . ARG B 1 71  ? 5.772   -7.875  81.856  1.00 110.77 ?  80  ARG B NE   1 
ATOM   6702  C CZ   . ARG B 1 71  ? 6.162   -8.082  83.102  1.00 88.17  ?  80  ARG B CZ   1 
ATOM   6703  N NH1  . ARG B 1 71  ? 5.722   -9.139  83.744  1.00 107.13 1  80  ARG B NH1  1 
ATOM   6704  N NH2  . ARG B 1 71  ? 6.978   -7.249  83.708  1.00 116.80 1  80  ARG B NH2  1 
ATOM   6705  H H    . ARG B 1 71  ? 0.907   -7.232  78.871  1.00 119.42 ?  80  ARG B H    1 
ATOM   6706  H HA   . ARG B 1 71  ? 1.269   -7.304  81.479  1.00 102.52 ?  80  ARG B HA   1 
ATOM   6707  H HB2  . ARG B 1 71  ? 2.536   -8.445  79.635  1.00 137.56 ?  80  ARG B HB2  1 
ATOM   6708  H HB3  . ARG B 1 71  ? 3.510   -7.208  79.862  1.00 137.56 ?  80  ARG B HB3  1 
ATOM   6709  H HG2  . ARG B 1 71  ? 3.403   -7.904  82.210  1.00 134.42 ?  80  ARG B HG2  1 
ATOM   6710  H HG3  . ARG B 1 71  ? 2.985   -9.309  81.584  1.00 134.42 ?  80  ARG B HG3  1 
ATOM   6711  H HD2  . ARG B 1 71  ? 5.067   -9.680  81.440  1.00 130.22 ?  80  ARG B HD2  1 
ATOM   6712  H HD3  . ARG B 1 71  ? 5.041   -8.683  80.201  1.00 130.22 ?  80  ARG B HD3  1 
ATOM   6713  H HE   . ARG B 1 71  ? 6.198   -7.288  81.394  1.00 132.92 ?  80  ARG B HE   1 
ATOM   6714  H HH11 . ARG B 1 71  ? 5.188   -9.688  83.353  1.00 128.56 ?  80  ARG B HH11 1 
ATOM   6715  H HH12 . ARG B 1 71  ? 5.969   -9.282  84.555  1.00 128.56 ?  80  ARG B HH12 1 
ATOM   6716  H HH21 . ARG B 1 71  ? 7.269   -6.554  83.294  1.00 140.16 ?  80  ARG B HH21 1 
ATOM   6717  H HH22 . ARG B 1 71  ? 7.220   -7.398  84.520  1.00 140.16 ?  80  ARG B HH22 1 
ATOM   6718  N N    . LEU B 1 72  ? 1.960   -4.612  80.064  1.00 64.30  ?  81  LEU B N    1 
ATOM   6719  C CA   . LEU B 1 72  ? 2.239   -3.219  80.327  1.00 54.45  ?  81  LEU B CA   1 
ATOM   6720  C C    . LEU B 1 72  ? 1.125   -2.594  81.155  1.00 97.05  ?  81  LEU B C    1 
ATOM   6721  O O    . LEU B 1 72  ? 1.394   -1.852  82.097  1.00 100.42 ?  81  LEU B O    1 
ATOM   6722  C CB   . LEU B 1 72  ? 2.423   -2.492  78.990  1.00 83.67  ?  81  LEU B CB   1 
ATOM   6723  C CG   . LEU B 1 72  ? 2.372   -0.959  78.928  1.00 49.84  ?  81  LEU B CG   1 
ATOM   6724  C CD1  . LEU B 1 72  ? 3.311   -0.409  79.888  1.00 46.54  ?  81  LEU B CD1  1 
ATOM   6725  C CD2  . LEU B 1 72  ? 2.672   -0.503  77.508  1.00 50.24  ?  81  LEU B CD2  1 
ATOM   6726  H H    . LEU B 1 72  ? 1.675   -4.773  79.269  1.00 77.16  ?  81  LEU B H    1 
ATOM   6727  H HA   . LEU B 1 72  ? 3.067   -3.147  80.827  1.00 65.34  ?  81  LEU B HA   1 
ATOM   6728  H HB2  . LEU B 1 72  ? 3.287   -2.752  78.635  1.00 100.40 ?  81  LEU B HB2  1 
ATOM   6729  H HB3  . LEU B 1 72  ? 1.732   -2.813  78.389  1.00 100.40 ?  81  LEU B HB3  1 
ATOM   6730  H HG   . LEU B 1 72  ? 1.481   -0.657  79.164  1.00 59.81  ?  81  LEU B HG   1 
ATOM   6731  H HD11 . LEU B 1 72  ? 3.275   0.559   79.845  1.00 55.85  ?  81  LEU B HD11 1 
ATOM   6732  H HD12 . LEU B 1 72  ? 3.065   -0.711  80.777  1.00 55.85  ?  81  LEU B HD12 1 
ATOM   6733  H HD13 . LEU B 1 72  ? 4.204   -0.718  79.668  1.00 55.85  ?  81  LEU B HD13 1 
ATOM   6734  H HD21 . LEU B 1 72  ? 2.639   0.466   77.474  1.00 60.29  ?  81  LEU B HD21 1 
ATOM   6735  H HD22 . LEU B 1 72  ? 3.556   -0.813  77.257  1.00 60.29  ?  81  LEU B HD22 1 
ATOM   6736  H HD23 . LEU B 1 72  ? 2.007   -0.878  76.909  1.00 60.29  ?  81  LEU B HD23 1 
ATOM   6737  N N    . VAL B 1 73  ? -0.125  -2.911  80.840  1.00 91.46  ?  82  VAL B N    1 
ATOM   6738  C CA   . VAL B 1 73  ? -1.254  -2.342  81.565  1.00 76.03  ?  82  VAL B CA   1 
ATOM   6739  C C    . VAL B 1 73  ? -1.227  -2.771  83.032  1.00 63.87  ?  82  VAL B C    1 
ATOM   6740  O O    . VAL B 1 73  ? -1.324  -1.941  83.941  1.00 142.96 ?  82  VAL B O    1 
ATOM   6741  C CB   . VAL B 1 73  ? -2.563  -2.707  80.831  1.00 77.17  ?  82  VAL B CB   1 
ATOM   6742  C CG1  . VAL B 1 73  ? -3.775  -2.520  81.684  1.00 86.90  ?  82  VAL B CG1  1 
ATOM   6743  C CG2  . VAL B 1 73  ? -2.709  -1.846  79.535  1.00 65.08  ?  82  VAL B CG2  1 
ATOM   6744  H H    . VAL B 1 73  ? -0.347  -3.453  80.210  1.00 109.75 ?  82  VAL B H    1 
ATOM   6745  H HA   . VAL B 1 73  ? -1.172  -1.376  81.547  1.00 91.24  ?  82  VAL B HA   1 
ATOM   6746  H HB   . VAL B 1 73  ? -2.526  -3.640  80.567  1.00 92.61  ?  82  VAL B HB   1 
ATOM   6747  H HG11 . VAL B 1 73  ? -4.562  -2.763  81.172  1.00 104.28 ?  82  VAL B HG11 1 
ATOM   6748  H HG12 . VAL B 1 73  ? -3.700  -3.088  82.467  1.00 104.28 ?  82  VAL B HG12 1 
ATOM   6749  H HG13 . VAL B 1 73  ? -3.830  -1.590  81.954  1.00 104.28 ?  82  VAL B HG13 1 
ATOM   6750  H HG21 . VAL B 1 73  ? -3.535  -2.088  79.088  1.00 78.10  ?  82  VAL B HG21 1 
ATOM   6751  H HG22 . VAL B 1 73  ? -2.728  -0.908  79.781  1.00 78.10  ?  82  VAL B HG22 1 
ATOM   6752  H HG23 . VAL B 1 73  ? -1.953  -2.021  78.953  1.00 78.10  ?  82  VAL B HG23 1 
ATOM   6753  N N    . LEU B 1 74  ? -1.051  -4.062  83.285  1.00 78.14  ?  83  LEU B N    1 
ATOM   6754  C CA   . LEU B 1 74  ? -1.093  -4.551  84.661  1.00 75.91  ?  83  LEU B CA   1 
ATOM   6755  C C    . LEU B 1 74  ? 0.069   -4.036  85.500  1.00 69.94  ?  83  LEU B C    1 
ATOM   6756  O O    . LEU B 1 74  ? -0.081  -3.766  86.708  1.00 74.87  ?  83  LEU B O    1 
ATOM   6757  C CB   . LEU B 1 74  ? -1.062  -6.081  84.704  1.00 94.17  ?  83  LEU B CB   1 
ATOM   6758  C CG   . LEU B 1 74  ? -2.250  -6.875  84.130  1.00 86.69  ?  83  LEU B CG   1 
ATOM   6759  C CD1  . LEU B 1 74  ? -1.846  -8.327  84.018  1.00 108.70 ?  83  LEU B CD1  1 
ATOM   6760  C CD2  . LEU B 1 74  ? -3.451  -6.700  84.977  1.00 119.22 ?  83  LEU B CD2  1 
ATOM   6761  H H    . LEU B 1 74  ? -0.908  -4.667  82.691  1.00 93.76  ?  83  LEU B H    1 
ATOM   6762  H HA   . LEU B 1 74  ? -1.918  -4.255  85.076  1.00 91.09  ?  83  LEU B HA   1 
ATOM   6763  H HB2  . LEU B 1 74  ? -0.274  -6.372  84.219  1.00 113.00 ?  83  LEU B HB2  1 
ATOM   6764  H HB3  . LEU B 1 74  ? -0.974  -6.346  85.632  1.00 113.00 ?  83  LEU B HB3  1 
ATOM   6765  H HG   . LEU B 1 74  ? -2.454  -6.547  83.240  1.00 104.02 ?  83  LEU B HG   1 
ATOM   6766  H HD11 . LEU B 1 74  ? -2.590  -8.834  83.657  1.00 130.44 ?  83  LEU B HD11 1 
ATOM   6767  H HD12 . LEU B 1 74  ? -1.080  -8.397  83.427  1.00 130.44 ?  83  LEU B HD12 1 
ATOM   6768  H HD13 . LEU B 1 74  ? -1.616  -8.660  84.899  1.00 130.44 ?  83  LEU B HD13 1 
ATOM   6769  H HD21 . LEU B 1 74  ? -4.183  -7.209  84.595  1.00 143.07 ?  83  LEU B HD21 1 
ATOM   6770  H HD22 . LEU B 1 74  ? -3.256  -7.021  85.871  1.00 143.07 ?  83  LEU B HD22 1 
ATOM   6771  H HD23 . LEU B 1 74  ? -3.682  -5.759  85.005  1.00 143.07 ?  83  LEU B HD23 1 
ATOM   6772  N N    . GLY B 1 75  ? 1.232   -3.876  84.903  1.00 73.69  ?  84  GLY B N    1 
ATOM   6773  C CA   . GLY B 1 75  ? 2.369   -3.485  85.716  1.00 72.59  ?  84  GLY B CA   1 
ATOM   6774  C C    . GLY B 1 75  ? 2.274   -2.062  86.209  1.00 81.07  ?  84  GLY B C    1 
ATOM   6775  O O    . GLY B 1 75  ? 2.675   -1.761  87.352  1.00 72.61  ?  84  GLY B O    1 
ATOM   6776  H H    . GLY B 1 75  ? 1.390   -3.982  84.064  1.00 88.43  ?  84  GLY B H    1 
ATOM   6777  H HA2  . GLY B 1 75  ? 2.430   -4.072  86.486  1.00 87.11  ?  84  GLY B HA2  1 
ATOM   6778  H HA3  . GLY B 1 75  ? 3.183   -3.575  85.196  1.00 87.11  ?  84  GLY B HA3  1 
ATOM   6779  N N    . CYS B 1 76  ? 1.707   -1.176  85.379  1.00 74.52  ?  85  CYS B N    1 
ATOM   6780  C CA   . CYS B 1 76  ? 1.495   0.216   85.789  1.00 74.24  ?  85  CYS B CA   1 
ATOM   6781  C C    . CYS B 1 76  ? 0.444   0.289   86.901  1.00 81.04  ?  85  CYS B C    1 
ATOM   6782  O O    . CYS B 1 76  ? 0.574   1.070   87.860  1.00 82.48  ?  85  CYS B O    1 
ATOM   6783  C CB   . CYS B 1 76  ? 1.027   1.035   84.590  1.00 76.16  ?  85  CYS B CB   1 
ATOM   6784  S SG   . CYS B 1 76  ? 2.109   1.193   83.145  1.00 86.16  ?  85  CYS B SG   1 
ATOM   6785  H H    . CYS B 1 76  ? 1.439   -1.356  84.582  1.00 89.43  ?  85  CYS B H    1 
ATOM   6786  H HA   . CYS B 1 76  ? 2.326   0.591   86.119  1.00 89.09  ?  85  CYS B HA   1 
ATOM   6787  H HB2  . CYS B 1 76  ? 0.197   0.644   84.274  1.00 91.40  ?  85  CYS B HB2  1 
ATOM   6788  H HB3  . CYS B 1 76  ? 0.848   1.936   84.903  1.00 91.40  ?  85  CYS B HB3  1 
ATOM   6789  H HG   . CYS B 1 76  ? 2.327   0.101   82.699  1.00 103.39 ?  85  CYS B HG   1 
ATOM   6790  N N    . ILE B 1 77  ? -0.626  -0.509  86.760  1.00 54.56  ?  86  ILE B N    1 
ATOM   6791  C CA   . ILE B 1 77  ? -1.649  -0.595  87.794  1.00 67.50  ?  86  ILE B CA   1 
ATOM   6792  C C    . ILE B 1 77  ? -1.033  -1.082  89.096  1.00 75.27  ?  86  ILE B C    1 
ATOM   6793  O O    . ILE B 1 77  ? -1.418  -0.655  90.199  1.00 71.75  ?  86  ILE B O    1 
ATOM   6794  C CB   . ILE B 1 77  ? -2.779  -1.506  87.305  1.00 97.92  ?  86  ILE B CB   1 
ATOM   6795  C CG1  . ILE B 1 77  ? -3.440  -0.861  86.092  1.00 122.68 ?  86  ILE B CG1  1 
ATOM   6796  C CG2  . ILE B 1 77  ? -3.791  -1.755  88.398  1.00 86.28  ?  86  ILE B CG2  1 
ATOM   6797  C CD1  . ILE B 1 77  ? -4.354  -1.760  85.382  1.00 98.10  ?  86  ILE B CD1  1 
ATOM   6798  H H    . ILE B 1 77  ? -0.775  -1.005  86.074  1.00 65.47  ?  86  ILE B H    1 
ATOM   6799  H HA   . ILE B 1 77  ? -2.020  0.288   87.949  1.00 81.00  ?  86  ILE B HA   1 
ATOM   6800  H HB   . ILE B 1 77  ? -2.397  -2.356  87.035  1.00 117.50 ?  86  ILE B HB   1 
ATOM   6801  H HG12 . ILE B 1 77  ? -3.949  -0.089  86.386  1.00 147.22 ?  86  ILE B HG12 1 
ATOM   6802  H HG13 . ILE B 1 77  ? -2.750  -0.583  85.469  1.00 147.22 ?  86  ILE B HG13 1 
ATOM   6803  H HG21 . ILE B 1 77  ? -4.490  -2.334  88.055  1.00 103.54 ?  86  ILE B HG21 1 
ATOM   6804  H HG22 . ILE B 1 77  ? -3.347  -2.181  89.148  1.00 103.54 ?  86  ILE B HG22 1 
ATOM   6805  H HG23 . ILE B 1 77  ? -4.170  -0.907  88.676  1.00 103.54 ?  86  ILE B HG23 1 
ATOM   6806  H HD11 . ILE B 1 77  ? -4.737  -1.287  84.626  1.00 117.72 ?  86  ILE B HD11 1 
ATOM   6807  H HD12 . ILE B 1 77  ? -3.857  -2.533  85.071  1.00 117.72 ?  86  ILE B HD12 1 
ATOM   6808  H HD13 . ILE B 1 77  ? -5.057  -2.039  85.989  1.00 117.72 ?  86  ILE B HD13 1 
ATOM   6809  N N    . THR B 1 78  ? -0.089  -2.032  88.991  1.00 65.84  ?  87  THR B N    1 
ATOM   6810  C CA   . THR B 1 78  ? 0.516   -2.566  90.201  1.00 74.46  ?  87  THR B CA   1 
ATOM   6811  C C    . THR B 1 78  ? 1.341   -1.493  90.898  1.00 70.28  ?  87  THR B C    1 
ATOM   6812  O O    . THR B 1 78  ? 1.289   -1.370  92.129  1.00 87.23  ?  87  THR B O    1 
ATOM   6813  C CB   . THR B 1 78  ? 1.370   -3.777  89.858  1.00 93.51  ?  87  THR B CB   1 
ATOM   6814  O OG1  . THR B 1 78  ? 0.532   -4.811  89.327  1.00 103.63 ?  87  THR B OG1  1 
ATOM   6815  C CG2  . THR B 1 78  ? 2.095   -4.274  91.097  1.00 79.36  ?  87  THR B CG2  1 
ATOM   6816  H H    . THR B 1 78  ? 0.203   -2.367  88.255  1.00 79.00  ?  87  THR B H    1 
ATOM   6817  H HA   . THR B 1 78  ? -0.184  -2.852  90.809  1.00 89.35  ?  87  THR B HA   1 
ATOM   6818  H HB   . THR B 1 78  ? 2.032   -3.527  89.195  1.00 112.21 ?  87  THR B HB   1 
ATOM   6819  H HG1  . THR B 1 78  ? 0.144   -4.538  88.633  1.00 124.35 ?  87  THR B HG1  1 
ATOM   6820  H HG21 . THR B 1 78  ? 2.639   -5.047  90.876  1.00 95.23  ?  87  THR B HG21 1 
ATOM   6821  H HG22 . THR B 1 78  ? 2.669   -3.575  91.448  1.00 95.23  ?  87  THR B HG22 1 
ATOM   6822  H HG23 . THR B 1 78  ? 1.453   -4.527  91.779  1.00 95.23  ?  87  THR B HG23 1 
ATOM   6823  N N    . MET B 1 79  ? 2.061   -0.670  90.114  1.00 54.46  ?  88  MET B N    1 
ATOM   6824  C CA   . MET B 1 79  ? 2.922   0.352   90.705  1.00 56.02  ?  88  MET B CA   1 
ATOM   6825  C C    . MET B 1 79  ? 2.084   1.443   91.331  1.00 63.40  ?  88  MET B C    1 
ATOM   6826  O O    . MET B 1 79  ? 2.352   1.882   92.453  1.00 80.64  ?  88  MET B O    1 
ATOM   6827  C CB   . MET B 1 79  ? 3.855   0.899   89.629  1.00 63.57  ?  88  MET B CB   1 
ATOM   6828  C CG   . MET B 1 79  ? 4.832   -0.171  89.052  1.00 85.01  ?  88  MET B CG   1 
ATOM   6829  S SD   . MET B 1 79  ? 5.957   -0.738  90.314  1.00 109.01 ?  88  MET B SD   1 
ATOM   6830  C CE   . MET B 1 79  ? 7.351   -1.286  89.344  1.00 177.59 ?  88  MET B CE   1 
ATOM   6831  H H    . MET B 1 79  ? 2.065   -0.687  89.254  1.00 65.35  ?  88  MET B H    1 
ATOM   6832  H HA   . MET B 1 79  ? 3.469   -0.058  91.393  1.00 67.23  ?  88  MET B HA   1 
ATOM   6833  H HB2  . MET B 1 79  ? 3.321   1.240   88.894  1.00 76.29  ?  88  MET B HB2  1 
ATOM   6834  H HB3  . MET B 1 79  ? 4.388   1.614   90.009  1.00 76.29  ?  88  MET B HB3  1 
ATOM   6835  H HG2  . MET B 1 79  ? 4.324   -0.932  88.730  1.00 102.02 ?  88  MET B HG2  1 
ATOM   6836  H HG3  . MET B 1 79  ? 5.351   0.220   88.332  1.00 102.02 ?  88  MET B HG3  1 
ATOM   6837  H HE1  . MET B 1 79  ? 8.038   -1.622  89.942  1.00 213.10 ?  88  MET B HE1  1 
ATOM   6838  H HE2  . MET B 1 79  ? 7.061   -1.991  88.744  1.00 213.10 ?  88  MET B HE2  1 
ATOM   6839  H HE3  . MET B 1 79  ? 7.694   -0.536  88.834  1.00 213.10 ?  88  MET B HE3  1 
ATOM   6840  N N    . ALA B 1 80  ? 1.009   1.827   90.636  1.00 79.06  ?  89  ALA B N    1 
ATOM   6841  C CA   . ALA B 1 80  ? 0.013   2.732   91.185  1.00 70.49  ?  89  ALA B CA   1 
ATOM   6842  C C    . ALA B 1 80  ? -0.667  2.141   92.412  1.00 67.67  ?  89  ALA B C    1 
ATOM   6843  O O    . ALA B 1 80  ? -0.919  2.865   93.368  1.00 71.93  ?  89  ALA B O    1 
ATOM   6844  C CB   . ALA B 1 80  ? -1.007  3.080   90.111  1.00 128.74 ?  89  ALA B CB   1 
ATOM   6845  H H    . ALA B 1 80  ? 0.838   1.569   89.833  1.00 94.87  ?  89  ALA B H    1 
ATOM   6846  H HA   . ALA B 1 80  ? 0.452   3.554   91.455  1.00 84.58  ?  89  ALA B HA   1 
ATOM   6847  H HB1  . ALA B 1 80  ? -1.666  3.684   90.487  1.00 154.49 ?  89  ALA B HB1  1 
ATOM   6848  H HB2  . ALA B 1 80  ? -0.550  3.508   89.370  1.00 154.49 ?  89  ALA B HB2  1 
ATOM   6849  H HB3  . ALA B 1 80  ? -1.437  2.265   89.809  1.00 154.49 ?  89  ALA B HB3  1 
ATOM   6850  N N    . TYR B 1 81  ? -0.982  0.838   92.416  1.00 57.71  ?  90  TYR B N    1 
ATOM   6851  C CA   . TYR B 1 81  ? -1.616  0.231   93.596  1.00 80.29  ?  90  TYR B CA   1 
ATOM   6852  C C    . TYR B 1 81  ? -0.651  0.173   94.776  1.00 81.69  ?  90  TYR B C    1 
ATOM   6853  O O    . TYR B 1 81  ? -1.021  0.520   95.899  1.00 100.10 ?  90  TYR B O    1 
ATOM   6854  C CB   . TYR B 1 81  ? -2.179  -1.187  93.293  1.00 74.69  ?  90  TYR B CB   1 
ATOM   6855  C CG   . TYR B 1 81  ? -2.883  -1.800  94.499  1.00 83.54  ?  90  TYR B CG   1 
ATOM   6856  C CD1  . TYR B 1 81  ? -4.235  -1.571  94.732  1.00 70.76  ?  90  TYR B CD1  1 
ATOM   6857  C CD2  . TYR B 1 81  ? -2.175  -2.549  95.435  1.00 116.56 ?  90  TYR B CD2  1 
ATOM   6858  C CE1  . TYR B 1 81  ? -4.885  -2.104  95.853  1.00 94.86  ?  90  TYR B CE1  1 
ATOM   6859  C CE2  . TYR B 1 81  ? -2.795  -3.074  96.554  1.00 97.50  ?  90  TYR B CE2  1 
ATOM   6860  C CZ   . TYR B 1 81  ? -4.157  -2.843  96.766  1.00 95.33  ?  90  TYR B CZ   1 
ATOM   6861  O OH   . TYR B 1 81  ? -4.763  -3.372  97.890  1.00 78.33  ?  90  TYR B OH   1 
ATOM   6862  H H    . TYR B 1 81  ? -0.844  0.295   91.763  1.00 69.25  ?  90  TYR B H    1 
ATOM   6863  H HA   . TYR B 1 81  ? -2.364  0.788   93.861  1.00 96.35  ?  90  TYR B HA   1 
ATOM   6864  H HB2  . TYR B 1 81  ? -2.821  -1.125  92.568  1.00 89.63  ?  90  TYR B HB2  1 
ATOM   6865  H HB3  . TYR B 1 81  ? -1.447  -1.772  93.042  1.00 89.63  ?  90  TYR B HB3  1 
ATOM   6866  H HD1  . TYR B 1 81  ? -4.721  -1.066  94.122  1.00 84.91  ?  90  TYR B HD1  1 
ATOM   6867  H HD2  . TYR B 1 81  ? -1.266  -2.698  95.305  1.00 139.87 ?  90  TYR B HD2  1 
ATOM   6868  H HE1  . TYR B 1 81  ? -5.791  -1.944  95.992  1.00 113.83 ?  90  TYR B HE1  1 
ATOM   6869  H HE2  . TYR B 1 81  ? -2.306  -3.577  97.165  1.00 117.00 ?  90  TYR B HE2  1 
ATOM   6870  H HH   . TYR B 1 81  ? -5.578  -3.170  97.899  1.00 93.99  ?  90  TYR B HH   1 
ATOM   6871  N N    . VAL B 1 82  ? 0.583   -0.269  94.547  1.00 82.31  ?  91  VAL B N    1 
ATOM   6872  C CA   . VAL B 1 82  ? 1.539   -0.412  95.649  1.00 87.43  ?  91  VAL B CA   1 
ATOM   6873  C C    . VAL B 1 82  ? 1.921   0.939   96.233  1.00 75.32  ?  91  VAL B C    1 
ATOM   6874  O O    . VAL B 1 82  ? 1.797   1.153   97.452  1.00 68.37  ?  91  VAL B O    1 
ATOM   6875  C CB   . VAL B 1 82  ? 2.779   -1.185  95.201  1.00 58.38  ?  91  VAL B CB   1 
ATOM   6876  C CG1  . VAL B 1 82  ? 3.880   -1.014  96.183  1.00 100.09 ?  91  VAL B CG1  1 
ATOM   6877  C CG2  . VAL B 1 82  ? 2.458   -2.664  95.061  1.00 85.84  ?  91  VAL B CG2  1 
ATOM   6878  H H    . VAL B 1 82  ? 0.891   -0.492  93.775  1.00 98.77  ?  91  VAL B H    1 
ATOM   6879  H HA   . VAL B 1 82  ? 1.116   -0.924  96.357  1.00 104.91 ?  91  VAL B HA   1 
ATOM   6880  H HB   . VAL B 1 82  ? 3.077   -0.850  94.341  1.00 70.06  ?  91  VAL B HB   1 
ATOM   6881  H HG11 . VAL B 1 82  ? 4.655   -1.512  95.878  1.00 120.11 ?  91  VAL B HG11 1 
ATOM   6882  H HG12 . VAL B 1 82  ? 4.099   -0.071  96.251  1.00 120.11 ?  91  VAL B HG12 1 
ATOM   6883  H HG13 . VAL B 1 82  ? 3.589   -1.349  97.045  1.00 120.11 ?  91  VAL B HG13 1 
ATOM   6884  H HG21 . VAL B 1 82  ? 3.257   -3.134  94.777  1.00 103.01 ?  91  VAL B HG21 1 
ATOM   6885  H HG22 . VAL B 1 82  ? 2.161   -3.005  95.919  1.00 103.01 ?  91  VAL B HG22 1 
ATOM   6886  H HG23 . VAL B 1 82  ? 1.756   -2.773  94.400  1.00 103.01 ?  91  VAL B HG23 1 
ATOM   6887  N N    . TRP B 1 83  ? 2.377   1.876   95.373  1.00 87.60  ?  92  TRP B N    1 
ATOM   6888  C CA   . TRP B 1 83  ? 2.999   3.130   95.818  1.00 84.37  ?  92  TRP B CA   1 
ATOM   6889  C C    . TRP B 1 83  ? 1.985   4.254   96.056  1.00 116.53 ?  92  TRP B C    1 
ATOM   6890  O O    . TRP B 1 83  ? 2.325   5.245   96.721  1.00 134.45 ?  92  TRP B O    1 
ATOM   6891  C CB   . TRP B 1 83  ? 4.066   3.639   94.803  1.00 74.94  ?  92  TRP B CB   1 
ATOM   6892  C CG   . TRP B 1 83  ? 5.247   2.684   94.525  1.00 69.73  ?  92  TRP B CG   1 
ATOM   6893  C CD1  . TRP B 1 83  ? 5.669   2.208   93.284  1.00 66.09  ?  92  TRP B CD1  1 
ATOM   6894  C CD2  . TRP B 1 83  ? 6.081   2.038   95.494  1.00 71.15  ?  92  TRP B CD2  1 
ATOM   6895  N NE1  . TRP B 1 83  ? 6.680   1.321   93.454  1.00 61.63  ?  92  TRP B NE1  1 
ATOM   6896  C CE2  . TRP B 1 83  ? 6.966   1.202   94.791  1.00 61.94  ?  92  TRP B CE2  1 
ATOM   6897  C CE3  . TRP B 1 83  ? 6.158   2.075   96.887  1.00 78.31  ?  92  TRP B CE3  1 
ATOM   6898  C CZ2  . TRP B 1 83  ? 7.933   0.424   95.443  1.00 86.59  ?  92  TRP B CZ2  1 
ATOM   6899  C CZ3  . TRP B 1 83  ? 7.110   1.302   97.530  1.00 96.11  ?  92  TRP B CZ3  1 
ATOM   6900  C CH2  . TRP B 1 83  ? 7.987   0.492   96.810  1.00 98.48  ?  92  TRP B CH2  1 
ATOM   6901  H H    . TRP B 1 83  ? 2.333   1.800   94.518  1.00 105.12 ?  92  TRP B H    1 
ATOM   6902  H HA   . TRP B 1 83  ? 3.453   2.965   96.659  1.00 101.25 ?  92  TRP B HA   1 
ATOM   6903  H HB2  . TRP B 1 83  ? 3.625   3.807   93.955  1.00 89.93  ?  92  TRP B HB2  1 
ATOM   6904  H HB3  . TRP B 1 83  ? 4.438   4.468   95.141  1.00 89.93  ?  92  TRP B HB3  1 
ATOM   6905  H HD1  . TRP B 1 83  ? 5.292   2.439   92.466  1.00 79.31  ?  92  TRP B HD1  1 
ATOM   6906  H HE1  . TRP B 1 83  ? 7.102   0.923   92.820  1.00 73.96  ?  92  TRP B HE1  1 
ATOM   6907  H HE3  . TRP B 1 83  ? 5.573   2.606   97.377  1.00 93.97  ?  92  TRP B HE3  1 
ATOM   6908  H HZ2  . TRP B 1 83  ? 8.522   -0.113  94.964  1.00 103.91 ?  92  TRP B HZ2  1 
ATOM   6909  H HZ3  . TRP B 1 83  ? 7.170   1.329   98.457  1.00 115.33 ?  92  TRP B HZ3  1 
ATOM   6910  H HH2  . TRP B 1 83  ? 8.623   -0.009  97.267  1.00 118.17 ?  92  TRP B HH2  1 
ATOM   6911  N N    . GLY B 1 84  ? 0.773   4.134   95.513  1.00 136.65 ?  93  GLY B N    1 
ATOM   6912  C CA   . GLY B 1 84  ? -0.305  5.057   95.859  1.00 132.73 ?  93  GLY B CA   1 
ATOM   6913  C C    . GLY B 1 84  ? -0.113  6.452   95.284  1.00 98.39  ?  93  GLY B C    1 
ATOM   6914  O O    . GLY B 1 84  ? 0.079   6.641   94.084  1.00 71.28  ?  93  GLY B O    1 
ATOM   6915  H H    . GLY B 1 84  ? 0.551   3.529   94.944  1.00 163.99 ?  93  GLY B H    1 
ATOM   6916  H HA2  . GLY B 1 84  ? -1.146  4.704   95.528  1.00 159.28 ?  93  GLY B HA2  1 
ATOM   6917  H HA3  . GLY B 1 84  ? -0.365  5.131   96.825  1.00 159.28 ?  93  GLY B HA3  1 
ATOM   6918  N N    . LYS B 1 85  ? -0.217  7.459   96.145  1.00 93.46  ?  94  LYS B N    1 
ATOM   6919  C CA   . LYS B 1 85  ? 0.068   8.819   95.710  1.00 94.95  ?  94  LYS B CA   1 
ATOM   6920  C C    . LYS B 1 85  ? 1.576   9.058   95.548  1.00 97.64  ?  94  LYS B C    1 
ATOM   6921  O O    . LYS B 1 85  ? 1.998   10.158  95.190  1.00 77.49  ?  94  LYS B O    1 
ATOM   6922  C CB   . LYS B 1 85  ? -0.536  9.830   96.706  1.00 93.07  ?  94  LYS B CB   1 
ATOM   6923  C CG   . LYS B 1 85  ? -2.013  10.058  96.549  1.00 98.45  ?  94  LYS B CG   1 
ATOM   6924  H H    . LYS B 1 85  ? -0.447  7.383   96.970  1.00 112.16 ?  94  LYS B H    1 
ATOM   6925  H HA   . LYS B 1 85  ? -0.350  8.966   94.847  1.00 113.94 ?  94  LYS B HA   1 
ATOM   6926  H HB2  . LYS B 1 85  ? -0.382  9.506   97.608  1.00 111.68 ?  94  LYS B HB2  1 
ATOM   6927  H HB3  . LYS B 1 85  ? -0.093  10.685  96.587  1.00 111.68 ?  94  LYS B HB3  1 
ATOM   6928  H HG2  . LYS B 1 85  ? -2.190  10.375  95.650  1.00 118.14 ?  94  LYS B HG2  1 
ATOM   6929  H HG3  . LYS B 1 85  ? -2.480  9.222   96.704  1.00 118.14 ?  94  LYS B HG3  1 
ATOM   6930  N N    . GLY B 1 86  ? 2.398   8.058   95.827  1.00 72.41  ?  95  GLY B N    1 
ATOM   6931  C CA   . GLY B 1 86  ? 3.821   8.248   95.766  1.00 102.32 ?  95  GLY B CA   1 
ATOM   6932  C C    . GLY B 1 86  ? 4.434   9.009   96.936  1.00 95.21  ?  95  GLY B C    1 
ATOM   6933  O O    . GLY B 1 86  ? 5.488   9.650   96.768  1.00 98.57  ?  95  GLY B O    1 
ATOM   6934  H H    . GLY B 1 86  ? 2.151   7.266   96.053  1.00 86.89  ?  95  GLY B H    1 
ATOM   6935  H HA2  . GLY B 1 86  ? 4.250   7.379   95.720  1.00 122.79 ?  95  GLY B HA2  1 
ATOM   6936  H HA3  . GLY B 1 86  ? 4.037   8.730   94.952  1.00 122.79 ?  95  GLY B HA3  1 
ATOM   6937  N N    . HIS B 1 87  ? 3.839   8.918   98.135  1.00 54.70  ?  96  HIS B N    1 
ATOM   6938  C CA   . HIS B 1 87  ? 4.309   9.638   99.311  1.00 56.45  ?  96  HIS B CA   1 
ATOM   6939  C C    . HIS B 1 87  ? 4.441   8.735   100.518 1.00 70.87  ?  96  HIS B C    1 
ATOM   6940  O O    . HIS B 1 87  ? 4.425   9.250   101.644 1.00 82.63  ?  96  HIS B O    1 
ATOM   6941  C CB   . HIS B 1 87  ? 3.397   10.806  99.665  1.00 75.27  ?  96  HIS B CB   1 
ATOM   6942  C CG   . HIS B 1 87  ? 3.283   11.823  98.573  1.00 85.78  ?  96  HIS B CG   1 
ATOM   6943  N ND1  . HIS B 1 87  ? 2.146   11.969  97.811  1.00 107.15 ?  96  HIS B ND1  1 
ATOM   6944  C CD2  . HIS B 1 87  ? 4.179   12.718  98.097  1.00 95.84  ?  96  HIS B CD2  1 
ATOM   6945  C CE1  . HIS B 1 87  ? 2.338   12.927  96.925  1.00 127.51 ?  96  HIS B CE1  1 
ATOM   6946  N NE2  . HIS B 1 87  ? 3.565   13.393  97.074  1.00 197.29 ?  96  HIS B NE2  1 
ATOM   6947  H H    . HIS B 1 87  ? 3.146   8.432   98.288  1.00 65.64  ?  96  HIS B H    1 
ATOM   6948  H HA   . HIS B 1 87  ? 5.188   10.000  99.119  1.00 67.74  ?  96  HIS B HA   1 
ATOM   6949  H HB2  . HIS B 1 87  ? 2.508   10.466  99.849  1.00 90.32  ?  96  HIS B HB2  1 
ATOM   6950  H HB3  . HIS B 1 87  ? 3.749   11.252  100.451 1.00 90.32  ?  96  HIS B HB3  1 
ATOM   6951  H HD2  . HIS B 1 87  ? 5.044   12.854  98.408  1.00 115.01 ?  96  HIS B HD2  1 
ATOM   6952  H HE1  . HIS B 1 87  ? 1.718   13.219  96.296  1.00 153.02 ?  96  HIS B HE1  1 
ATOM   6953  N N    . GLY B 1 88  ? 4.468   7.402   100.321 1.00 92.35  ?  97  GLY B N    1 
ATOM   6954  C CA   . GLY B 1 88  ? 4.830   6.467   101.377 1.00 78.23  ?  97  GLY B CA   1 
ATOM   6955  C C    . GLY B 1 88  ? 3.699   5.646   101.992 1.00 104.81 ?  97  GLY B C    1 
ATOM   6956  O O    . GLY B 1 88  ? 3.986   4.862   102.902 1.00 128.31 ?  97  GLY B O    1 
ATOM   6957  H H    . GLY B 1 88  ? 4.277   7.022   99.573  1.00 110.82 ?  97  GLY B H    1 
ATOM   6958  H HA2  . GLY B 1 88  ? 5.484   5.843   101.025 1.00 93.88  ?  97  GLY B HA2  1 
ATOM   6959  H HA3  . GLY B 1 88  ? 5.253   6.963   102.095 1.00 93.88  ?  97  GLY B HA3  1 
ATOM   6960  N N    . ASP B 1 89  ? 2.428   5.809   101.570 1.00 142.22 ?  98  ASP B N    1 
ATOM   6961  C CA   . ASP B 1 89  ? 1.327   4.945   102.040 1.00 126.91 ?  98  ASP B CA   1 
ATOM   6962  C C    . ASP B 1 89  ? 1.311   3.661   101.192 1.00 108.69 ?  98  ASP B C    1 
ATOM   6963  O O    . ASP B 1 89  ? 0.681   3.576   100.138 1.00 77.15  ?  98  ASP B O    1 
ATOM   6964  C CB   . ASP B 1 89  ? -0.000  5.703   101.992 1.00 89.88  ?  98  ASP B CB   1 
ATOM   6965  H H    . ASP B 1 89  ? 2.180   6.414   101.012 1.00 170.67 ?  98  ASP B H    1 
ATOM   6966  H HA   . ASP B 1 89  ? 1.494   4.694   102.961 1.00 152.29 ?  98  ASP B HA   1 
ATOM   6967  N N    . VAL B 1 90  ? 1.978   2.615   101.669 1.00 113.11 ?  99  VAL B N    1 
ATOM   6968  C CA   . VAL B 1 90  ? 2.377   1.506   100.805 1.00 95.52  ?  99  VAL B CA   1 
ATOM   6969  C C    . VAL B 1 90  ? 1.457   0.332   101.077 1.00 90.52  ?  99  VAL B C    1 
ATOM   6970  O O    . VAL B 1 90  ? 1.252   -0.054  102.233 1.00 108.60 ?  99  VAL B O    1 
ATOM   6971  C CB   . VAL B 1 90  ? 3.845   1.076   101.042 1.00 95.47  ?  99  VAL B CB   1 
ATOM   6972  C CG1  . VAL B 1 90  ? 4.194   -0.203  100.226 1.00 91.16  ?  99  VAL B CG1  1 
ATOM   6973  C CG2  . VAL B 1 90  ? 4.833   2.178   100.748 1.00 98.07  ?  99  VAL B CG2  1 
ATOM   6974  H H    . VAL B 1 90  ? 2.212   2.521   102.492 1.00 135.73 ?  99  VAL B H    1 
ATOM   6975  H HA   . VAL B 1 90  ? 2.278   1.767   99.876  1.00 114.62 ?  99  VAL B HA   1 
ATOM   6976  H HB   . VAL B 1 90  ? 3.943   0.850   101.980 1.00 114.57 ?  99  VAL B HB   1 
ATOM   6977  H HG11 . VAL B 1 90  ? 5.118   -0.444  100.398 1.00 109.40 ?  99  VAL B HG11 1 
ATOM   6978  H HG12 . VAL B 1 90  ? 3.607   -0.924  100.504 1.00 109.40 ?  99  VAL B HG12 1 
ATOM   6979  H HG13 . VAL B 1 90  ? 4.070   -0.019  99.282  1.00 109.40 ?  99  VAL B HG13 1 
ATOM   6980  H HG21 . VAL B 1 90  ? 5.731   1.850   100.915 1.00 117.68 ?  99  VAL B HG21 1 
ATOM   6981  H HG22 . VAL B 1 90  ? 4.744   2.442   99.819  1.00 117.68 ?  99  VAL B HG22 1 
ATOM   6982  H HG23 . VAL B 1 90  ? 4.645   2.933   101.327 1.00 117.68 ?  99  VAL B HG23 1 
ATOM   6983  N N    . ARG B 1 91  ? 0.984   -0.295  100.015 1.00 85.15  ?  100 ARG B N    1 
ATOM   6984  C CA   . ARG B 1 91  ? 0.242   -1.530  100.155 1.00 91.02  ?  100 ARG B CA   1 
ATOM   6985  C C    . ARG B 1 91  ? 1.217   -2.686  99.930  1.00 82.68  ?  100 ARG B C    1 
ATOM   6986  O O    . ARG B 1 91  ? 1.947   -2.711  98.932  1.00 68.07  ?  100 ARG B O    1 
ATOM   6987  C CB   . ARG B 1 91  ? -0.961  -1.536  99.193  1.00 88.98  ?  100 ARG B CB   1 
ATOM   6988  C CG   . ARG B 1 91  ? -2.203  -0.801  99.742  1.00 136.67 ?  100 ARG B CG   1 
ATOM   6989  H H    . ARG B 1 91  ? 1.080   -0.027  99.204  1.00 102.18 ?  100 ARG B H    1 
ATOM   6990  H HA   . ARG B 1 91  ? -0.098  -1.595  101.061 1.00 109.22 ?  100 ARG B HA   1 
ATOM   6991  H HB2  . ARG B 1 91  ? -0.702  -1.101  98.365  1.00 106.77 ?  100 ARG B HB2  1 
ATOM   6992  H HB3  . ARG B 1 91  ? -1.215  -2.455  99.016  1.00 106.77 ?  100 ARG B HB3  1 
ATOM   6993  H HG2  . ARG B 1 91  ? -1.989  0.138   99.857  1.00 164.00 ?  100 ARG B HG2  1 
ATOM   6994  H HG3  . ARG B 1 91  ? -2.934  -0.900  99.112  1.00 164.00 ?  100 ARG B HG3  1 
ATOM   6995  N N    . LYS B 1 92  ? 1.229   -3.633  100.866 1.00 97.63  ?  101 LYS B N    1 
ATOM   6996  C CA   . LYS B 1 92  ? 2.121   -4.781  100.833 1.00 96.25  ?  101 LYS B CA   1 
ATOM   6997  C C    . LYS B 1 92  ? 1.455   -6.041  100.300 1.00 104.00 ?  101 LYS B C    1 
ATOM   6998  O O    . LYS B 1 92  ? 2.122   -7.071  100.198 1.00 96.58  ?  101 LYS B O    1 
ATOM   6999  C CB   . LYS B 1 92  ? 2.660   -5.075  102.242 1.00 96.88  ?  101 LYS B CB   1 
ATOM   7000  C CG   . LYS B 1 92  ? 3.292   -3.895  102.937 1.00 137.25 ?  101 LYS B CG   1 
ATOM   7001  H H    . LYS B 1 92  ? 0.710   -3.628  101.552 1.00 117.15 ?  101 LYS B H    1 
ATOM   7002  H HA   . LYS B 1 92  ? 2.877   -4.577  100.260 1.00 115.50 ?  101 LYS B HA   1 
ATOM   7003  H HB2  . LYS B 1 92  ? 1.925   -5.382  102.796 1.00 116.25 ?  101 LYS B HB2  1 
ATOM   7004  H HB3  . LYS B 1 92  ? 3.332   -5.772  102.177 1.00 116.25 ?  101 LYS B HB3  1 
ATOM   7005  H HG2  . LYS B 1 92  ? 3.989   -3.531  102.370 1.00 164.70 ?  101 LYS B HG2  1 
ATOM   7006  H HG3  . LYS B 1 92  ? 2.612   -3.223  103.101 1.00 164.70 ?  101 LYS B HG3  1 
ATOM   7007  N N    . VAL B 1 93  ? 0.176   -5.990  99.944  1.00 133.02 ?  102 VAL B N    1 
ATOM   7008  C CA   . VAL B 1 93  ? -0.537  -7.168  99.486  1.00 103.15 ?  102 VAL B CA   1 
ATOM   7009  C C    . VAL B 1 93  ? -1.190  -6.815  98.177  1.00 86.80  ?  102 VAL B C    1 
ATOM   7010  O O    . VAL B 1 93  ? -1.997  -5.882  98.111  1.00 125.02 ?  102 VAL B O    1 
ATOM   7011  C CB   . VAL B 1 93  ? -1.598  -7.637  100.484 1.00 115.24 ?  102 VAL B CB   1 
ATOM   7012  C CG1  . VAL B 1 93  ? -2.241  -8.906  99.969  1.00 116.16 ?  102 VAL B CG1  1 
ATOM   7013  C CG2  . VAL B 1 93  ? -0.976  -7.840  101.841 1.00 134.72 ?  102 VAL B CG2  1 
ATOM   7014  H H    . VAL B 1 93  ? -0.303  -5.276  99.961  1.00 159.63 ?  102 VAL B H    1 
ATOM   7015  H HA   . VAL B 1 93  ? 0.090   -7.893  99.336  1.00 123.78 ?  102 VAL B HA   1 
ATOM   7016  H HB   . VAL B 1 93  ? -2.286  -6.957  100.563 1.00 138.29 ?  102 VAL B HB   1 
ATOM   7017  H HG11 . VAL B 1 93  ? -2.912  -9.199  100.604 1.00 139.39 ?  102 VAL B HG11 1 
ATOM   7018  H HG12 . VAL B 1 93  ? -2.654  -8.724  99.110  1.00 139.39 ?  102 VAL B HG12 1 
ATOM   7019  H HG13 . VAL B 1 93  ? -1.558  -9.588  99.870  1.00 139.39 ?  102 VAL B HG13 1 
ATOM   7020  H HG21 . VAL B 1 93  ? -1.661  -8.137  102.460 1.00 161.67 ?  102 VAL B HG21 1 
ATOM   7021  H HG22 . VAL B 1 93  ? -0.280  -8.512  101.771 1.00 161.67 ?  102 VAL B HG22 1 
ATOM   7022  H HG23 . VAL B 1 93  ? -0.597  -7.000  102.143 1.00 161.67 ?  102 VAL B HG23 1 
ATOM   7023  N N    . LEU B 1 94  ? -0.899  -7.552  97.207  1.00 82.92  ?  103 LEU B N    1 
ATOM   7024  C CA   . LEU B 1 94  ? -1.502  -7.279  95.927  1.00 71.61  ?  103 LEU B CA   1 
ATOM   7025  C C    . LEU B 1 94  ? -2.783  -8.105  95.803  1.00 119.35 ?  103 LEU B C    1 
ATOM   7026  O O    . LEU B 1 94  ? -2.751  -9.322  96.016  1.00 111.36 ?  103 LEU B O    1 
ATOM   7027  C CB   . LEU B 1 94  ? -0.546  -7.627  94.819  1.00 76.99  ?  103 LEU B CB   1 
ATOM   7028  C CG   . LEU B 1 94  ? -0.884  -6.968  93.492  1.00 72.44  ?  103 LEU B CG   1 
ATOM   7029  C CD1  . LEU B 1 94  ? -0.672  -5.460  93.544  1.00 66.54  ?  103 LEU B CD1  1 
ATOM   7030  C CD2  . LEU B 1 94  ? -0.063  -7.547  92.437  1.00 64.21  ?  103 LEU B CD2  1 
ATOM   7031  H H    . LEU B 1 94  ? -0.360  -8.222  97.227  1.00 99.50  ?  103 LEU B H    1 
ATOM   7032  H HA   . LEU B 1 94  ? -1.728  -6.338  95.863  1.00 85.93  ?  103 LEU B HA   1 
ATOM   7033  H HB2  . LEU B 1 94  ? 0.345   -7.341  95.074  1.00 92.38  ?  103 LEU B HB2  1 
ATOM   7034  H HB3  . LEU B 1 94  ? -0.558  -8.587  94.686  1.00 92.38  ?  103 LEU B HB3  1 
ATOM   7035  H HG   . LEU B 1 94  ? -1.815  -7.137  93.278  1.00 86.93  ?  103 LEU B HG   1 
ATOM   7036  H HD11 . LEU B 1 94  ? -0.897  -5.080  92.681  1.00 79.85  ?  103 LEU B HD11 1 
ATOM   7037  H HD12 . LEU B 1 94  ? -1.244  -5.085  94.231  1.00 79.85  ?  103 LEU B HD12 1 
ATOM   7038  H HD13 . LEU B 1 94  ? 0.258   -5.280  93.753  1.00 79.85  ?  103 LEU B HD13 1 
ATOM   7039  H HD21 . LEU B 1 94  ? -0.285  -7.121  91.595  1.00 77.05  ?  103 LEU B HD21 1 
ATOM   7040  H HD22 . LEU B 1 94  ? 0.872   -7.397  92.648  1.00 77.05  ?  103 LEU B HD22 1 
ATOM   7041  H HD23 . LEU B 1 94  ? -0.242  -8.499  92.385  1.00 77.05  ?  103 LEU B HD23 1 
ATOM   7042  N N    . PRO B 1 95  ? -3.914  -7.491  95.478  1.00 126.76 ?  104 PRO B N    1 
ATOM   7043  C CA   . PRO B 1 95  ? -5.195  -8.211  95.523  1.00 118.22 ?  104 PRO B CA   1 
ATOM   7044  C C    . PRO B 1 95  ? -5.267  -9.428  94.611  1.00 104.55 ?  104 PRO B C    1 
ATOM   7045  O O    . PRO B 1 95  ? -4.988  -9.348  93.418  1.00 106.47 ?  104 PRO B O    1 
ATOM   7046  C CB   . PRO B 1 95  ? -6.191  -7.153  95.062  1.00 105.16 ?  104 PRO B CB   1 
ATOM   7047  C CG   . PRO B 1 95  ? -5.565  -5.882  95.391  1.00 83.31  ?  104 PRO B CG   1 
ATOM   7048  C CD   . PRO B 1 95  ? -4.103  -6.042  95.363  1.00 125.40 ?  104 PRO B CD   1 
ATOM   7049  H HA   . PRO B 1 95  ? -5.403  -8.475  96.433  1.00 141.86 ?  104 PRO B HA   1 
ATOM   7050  H HB2  . PRO B 1 95  ? -6.331  -7.230  94.105  1.00 126.19 ?  104 PRO B HB2  1 
ATOM   7051  H HB3  . PRO B 1 95  ? -7.027  -7.258  95.543  1.00 126.19 ?  104 PRO B HB3  1 
ATOM   7052  H HG2  . PRO B 1 95  ? -5.837  -5.219  94.737  1.00 99.97  ?  104 PRO B HG2  1 
ATOM   7053  H HG3  . PRO B 1 95  ? -5.851  -5.610  96.277  1.00 99.97  ?  104 PRO B HG3  1 
ATOM   7054  H HD2  . PRO B 1 95  ? -3.743  -5.721  94.522  1.00 150.48 ?  104 PRO B HD2  1 
ATOM   7055  H HD3  . PRO B 1 95  ? -3.699  -5.588  96.119  1.00 150.48 ?  104 PRO B HD3  1 
ATOM   7056  N N    . ARG B 1 96  ? -5.822  -10.515 95.147  1.00 123.21 ?  105 ARG B N    1 
ATOM   7057  C CA   . ARG B 1 96  ? -5.935  -11.730 94.359  1.00 100.97 ?  105 ARG B CA   1 
ATOM   7058  C C    . ARG B 1 96  ? -6.520  -11.424 92.998  1.00 95.45  ?  105 ARG B C    1 
ATOM   7059  O O    . ARG B 1 96  ? -5.979  -11.839 91.971  1.00 92.61  ?  105 ARG B O    1 
ATOM   7060  C CB   . ARG B 1 96  ? -6.819  -12.741 95.091  1.00 154.87 ?  105 ARG B CB   1 
ATOM   7061  H H    . ARG B 1 96  ? -6.134  -10.570 95.947  1.00 147.85 ?  105 ARG B H    1 
ATOM   7062  H HA   . ARG B 1 96  ? -5.056  -12.121 94.236  1.00 121.16 ?  105 ARG B HA   1 
ATOM   7063  N N    . ASN B 1 97  ? -7.580  -10.616 92.979  1.00 133.65 ?  106 ASN B N    1 
ATOM   7064  C CA   . ASN B 1 97  ? -8.276  -10.303 91.741  1.00 118.39 ?  106 ASN B CA   1 
ATOM   7065  C C    . ASN B 1 97  ? -7.294  -9.903  90.669  1.00 159.69 ?  106 ASN B C    1 
ATOM   7066  O O    . ASN B 1 97  ? -7.423  -10.268 89.502  1.00 77.29  ?  106 ASN B O    1 
ATOM   7067  C CB   . ASN B 1 97  ? -9.251  -9.161  91.986  1.00 109.95 ?  106 ASN B CB   1 
ATOM   7068  H H    . ASN B 1 97  ? -7.914  -10.236 93.674  1.00 160.38 ?  106 ASN B H    1 
ATOM   7069  H HA   . ASN B 1 97  ? -8.772  -11.079 91.437  1.00 142.07 ?  106 ASN B HA   1 
ATOM   7070  N N    . ILE B 1 98  ? -6.262  -9.190  91.053  1.00 151.26 ?  107 ILE B N    1 
ATOM   7071  C CA   . ILE B 1 98  ? -5.335  -8.683  90.077  1.00 98.12  ?  107 ILE B CA   1 
ATOM   7072  C C    . ILE B 1 98  ? -4.004  -9.386  90.152  1.00 103.70 ?  107 ILE B C    1 
ATOM   7073  O O    . ILE B 1 98  ? -3.341  -9.523  89.128  1.00 66.98  ?  107 ILE B O    1 
ATOM   7074  C CB   . ILE B 1 98  ? -5.154  -7.175  90.255  1.00 102.52 ?  107 ILE B CB   1 
ATOM   7075  C CG1  . ILE B 1 98  ? -4.140  -6.642  89.263  1.00 96.48  ?  107 ILE B CG1  1 
ATOM   7076  C CG2  . ILE B 1 98  ? -4.736  -6.861  91.697  1.00 126.86 ?  107 ILE B CG2  1 
ATOM   7077  C CD1  . ILE B 1 98  ? -4.118  -5.139  89.256  1.00 63.91  ?  107 ILE B CD1  1 
ATOM   7078  H H    . ILE B 1 98  ? -6.077  -8.985  91.868  1.00 181.51 ?  107 ILE B H    1 
ATOM   7079  H HA   . ILE B 1 98  ? -5.700  -8.835  89.191  1.00 117.74 ?  107 ILE B HA   1 
ATOM   7080  H HB   . ILE B 1 98  ? -6.005  -6.743  90.083  1.00 123.02 ?  107 ILE B HB   1 
ATOM   7081  H HG12 . ILE B 1 98  ? -3.256  -6.959  89.506  1.00 115.78 ?  107 ILE B HG12 1 
ATOM   7082  H HG13 . ILE B 1 98  ? -4.372  -6.947  88.372  1.00 115.78 ?  107 ILE B HG13 1 
ATOM   7083  H HG21 . ILE B 1 98  ? -4.626  -5.902  91.792  1.00 152.24 ?  107 ILE B HG21 1 
ATOM   7084  H HG22 . ILE B 1 98  ? -5.426  -7.176  92.301  1.00 152.24 ?  107 ILE B HG22 1 
ATOM   7085  H HG23 . ILE B 1 98  ? -3.898  -7.311  91.887  1.00 152.24 ?  107 ILE B HG23 1 
ATOM   7086  H HD11 . ILE B 1 98  ? -3.460  -4.836  88.611  1.00 76.69  ?  107 ILE B HD11 1 
ATOM   7087  H HD12 . ILE B 1 98  ? -4.997  -4.812  89.010  1.00 76.69  ?  107 ILE B HD12 1 
ATOM   7088  H HD13 . ILE B 1 98  ? -3.883  -4.823  90.143  1.00 76.69  ?  107 ILE B HD13 1 
ATOM   7089  N N    . ALA B 1 99  ? -3.584  -9.798  91.337  1.00 116.77 ?  108 ALA B N    1 
ATOM   7090  C CA   . ALA B 1 99  ? -2.270  -10.399 91.495  1.00 106.07 ?  108 ALA B CA   1 
ATOM   7091  C C    . ALA B 1 99  ? -2.179  -11.715 90.743  1.00 127.00 ?  108 ALA B C    1 
ATOM   7092  O O    . ALA B 1 99  ? -1.217  -11.960 90.006  1.00 186.51 ?  108 ALA B O    1 
ATOM   7093  C CB   . ALA B 1 99  ? -1.964  -10.604 92.983  1.00 97.28  ?  108 ALA B CB   1 
ATOM   7094  H H    . ALA B 1 99  ? -4.039  -9.741  92.065  1.00 140.13 ?  108 ALA B H    1 
ATOM   7095  H HA   . ALA B 1 99  ? -1.602  -9.798  91.130  1.00 127.28 ?  108 ALA B HA   1 
ATOM   7096  H HB1  . ALA B 1 99  ? -1.085  -11.005 93.072  1.00 116.73 ?  108 ALA B HB1  1 
ATOM   7097  H HB2  . ALA B 1 99  ? -1.981  -9.743  93.430  1.00 116.73 ?  108 ALA B HB2  1 
ATOM   7098  H HB3  . ALA B 1 99  ? -2.636  -11.190 93.366  1.00 116.73 ?  108 ALA B HB3  1 
ATOM   7099  N N    . VAL B 1 100 ? -3.186  -12.563 90.884  1.00 97.06  ?  109 VAL B N    1 
ATOM   7100  C CA   . VAL B 1 100 ? -3.105  -13.883 90.276  1.00 88.08  ?  109 VAL B CA   1 
ATOM   7101  C C    . VAL B 1 100 ? -2.938  -13.732 88.768  1.00 125.63 ?  109 VAL B C    1 
ATOM   7102  O O    . VAL B 1 100 ? -1.971  -14.261 88.209  1.00 135.09 ?  109 VAL B O    1 
ATOM   7103  C CB   . VAL B 1 100 ? -4.316  -14.731 90.681  1.00 105.33 ?  109 VAL B CB   1 
ATOM   7104  C CG1  . VAL B 1 100 ? -4.322  -16.039 89.934  1.00 81.82  ?  109 VAL B CG1  1 
ATOM   7105  C CG2  . VAL B 1 100 ? -4.271  -14.998 92.190  1.00 80.30  ?  109 VAL B CG2  1 
ATOM   7106  H H    . VAL B 1 100 ? -3.913  -12.406 91.317  1.00 116.47 ?  109 VAL B H    1 
ATOM   7107  H HA   . VAL B 1 100 ? -2.312  -14.329 90.613  1.00 105.70 ?  109 VAL B HA   1 
ATOM   7108  H HB   . VAL B 1 100 ? -5.134  -14.252 90.475  1.00 126.39 ?  109 VAL B HB   1 
ATOM   7109  H HG11 . VAL B 1 100 ? -5.096  -16.555 90.208  1.00 98.18  ?  109 VAL B HG11 1 
ATOM   7110  H HG12 . VAL B 1 100 ? -4.364  -15.858 88.982  1.00 98.18  ?  109 VAL B HG12 1 
ATOM   7111  H HG13 . VAL B 1 100 ? -3.508  -16.525 90.142  1.00 98.18  ?  109 VAL B HG13 1 
ATOM   7112  H HG21 . VAL B 1 100 ? -5.040  -15.534 92.439  1.00 96.36  ?  109 VAL B HG21 1 
ATOM   7113  H HG22 . VAL B 1 100 ? -3.453  -15.473 92.402  1.00 96.36  ?  109 VAL B HG22 1 
ATOM   7114  H HG23 . VAL B 1 100 ? -4.293  -14.150 92.661  1.00 96.36  ?  109 VAL B HG23 1 
ATOM   7115  N N    . PRO B 1 101 ? -3.833  -13.036 88.070  1.00 102.67 ?  110 PRO B N    1 
ATOM   7116  C CA   . PRO B 1 101 ? -3.689  -12.956 86.615  1.00 89.87  ?  110 PRO B CA   1 
ATOM   7117  C C    . PRO B 1 101 ? -2.417  -12.294 86.144  1.00 123.25 ?  110 PRO B C    1 
ATOM   7118  O O    . PRO B 1 101 ? -1.876  -12.678 85.100  1.00 77.77  ?  110 PRO B O    1 
ATOM   7119  C CB   . PRO B 1 101 ? -4.897  -12.133 86.194  1.00 74.30  ?  110 PRO B CB   1 
ATOM   7120  C CG   . PRO B 1 101 ? -5.301  -11.391 87.352  1.00 173.93 ?  110 PRO B CG   1 
ATOM   7121  C CD   . PRO B 1 101 ? -4.959  -12.219 88.542  1.00 144.78 ?  110 PRO B CD   1 
ATOM   7122  H HA   . PRO B 1 101 ? -3.753  -13.841 86.223  1.00 107.84 ?  110 PRO B HA   1 
ATOM   7123  H HB2  . PRO B 1 101 ? -4.645  -11.532 85.476  1.00 89.15  ?  110 PRO B HB2  1 
ATOM   7124  H HB3  . PRO B 1 101 ? -5.608  -12.727 85.906  1.00 89.15  ?  110 PRO B HB3  1 
ATOM   7125  H HG2  . PRO B 1 101 ? -4.821  -10.549 87.378  1.00 208.72 ?  110 PRO B HG2  1 
ATOM   7126  H HG3  . PRO B 1 101 ? -6.258  -11.233 87.315  1.00 208.72 ?  110 PRO B HG3  1 
ATOM   7127  H HD2  . PRO B 1 101 ? -4.681  -11.654 89.280  1.00 173.74 ?  110 PRO B HD2  1 
ATOM   7128  H HD3  . PRO B 1 101 ? -5.707  -12.785 88.788  1.00 173.74 ?  110 PRO B HD3  1 
ATOM   7129  N N    . TYR B 1 102 ? -1.930  -11.280 86.854  1.00 105.63 ?  111 TYR B N    1 
ATOM   7130  C CA   . TYR B 1 102 ? -0.672  -10.682 86.440  1.00 95.72  ?  111 TYR B CA   1 
ATOM   7131  C C    . TYR B 1 102 ? 0.408   -11.723 86.511  1.00 77.06  ?  111 TYR B C    1 
ATOM   7132  O O    . TYR B 1 102 ? 1.219   -11.810 85.588  1.00 68.09  ?  111 TYR B O    1 
ATOM   7133  C CB   . TYR B 1 102 ? -0.316  -9.458  87.294  1.00 112.88 ?  111 TYR B CB   1 
ATOM   7134  C CG   . TYR B 1 102 ? 0.950   -8.635  86.886  1.00 80.60  ?  111 TYR B CG   1 
ATOM   7135  C CD1  . TYR B 1 102 ? 1.338   -8.478  85.549  1.00 82.29  ?  111 TYR B CD1  1 
ATOM   7136  C CD2  . TYR B 1 102 ? 1.710   -7.961  87.846  1.00 75.34  ?  111 TYR B CD2  1 
ATOM   7137  C CE1  . TYR B 1 102 ? 2.453   -7.719  85.192  1.00 79.45  ?  111 TYR B CE1  1 
ATOM   7138  C CE2  . TYR B 1 102 ? 2.823   -7.194  87.496  1.00 100.26 ?  111 TYR B CE2  1 
ATOM   7139  C CZ   . TYR B 1 102 ? 3.188   -7.078  86.170  1.00 122.50 ?  111 TYR B CZ   1 
ATOM   7140  O OH   . TYR B 1 102 ? 4.294   -6.312  85.832  1.00 129.95 ?  111 TYR B OH   1 
ATOM   7141  H H    . TYR B 1 102 ? -2.294  -10.933 87.552  1.00 126.76 ?  111 TYR B H    1 
ATOM   7142  H HA   . TYR B 1 102 ? -0.749  -10.392 85.518  1.00 114.87 ?  111 TYR B HA   1 
ATOM   7143  H HB2  . TYR B 1 102 ? -1.070  -8.849  87.272  1.00 135.45 ?  111 TYR B HB2  1 
ATOM   7144  H HB3  . TYR B 1 102 ? -0.177  -9.759  88.205  1.00 135.45 ?  111 TYR B HB3  1 
ATOM   7145  H HD1  . TYR B 1 102 ? 0.849   -8.906  84.883  1.00 98.74  ?  111 TYR B HD1  1 
ATOM   7146  H HD2  . TYR B 1 102 ? 1.472   -8.032  88.742  1.00 90.41  ?  111 TYR B HD2  1 
ATOM   7147  H HE1  . TYR B 1 102 ? 2.696   -7.638  84.298  1.00 95.34  ?  111 TYR B HE1  1 
ATOM   7148  H HE2  . TYR B 1 102 ? 3.319   -6.765  88.155  1.00 120.31 ?  111 TYR B HE2  1 
ATOM   7149  H HH   . TYR B 1 102 ? 4.640   -5.985  86.524  1.00 155.95 ?  111 TYR B HH   1 
ATOM   7150  N N    . CYS B 1 103 ? 0.406   -12.543 87.581  1.00 77.91  ?  112 CYS B N    1 
ATOM   7151  C CA   . CYS B 1 103 ? 1.417   -13.585 87.761  1.00 93.05  ?  112 CYS B CA   1 
ATOM   7152  C C    . CYS B 1 103 ? 1.264   -14.688 86.717  1.00 112.58 ?  112 CYS B C    1 
ATOM   7153  O O    . CYS B 1 103 ? 2.235   -15.371 86.393  1.00 129.81 ?  112 CYS B O    1 
ATOM   7154  C CB   . CYS B 1 103 ? 1.332   -14.196 89.161  1.00 88.72  ?  112 CYS B CB   1 
ATOM   7155  S SG   . CYS B 1 103 ? 1.890   -13.235 90.562  1.00 76.98  ?  112 CYS B SG   1 
ATOM   7156  H H    . CYS B 1 103 ? -0.176  -12.510 88.214  1.00 93.49  ?  112 CYS B H    1 
ATOM   7157  H HA   . CYS B 1 103 ? 2.298   -13.193 87.657  1.00 111.66 ?  112 CYS B HA   1 
ATOM   7158  H HB2  . CYS B 1 103 ? 0.403   -14.419 89.329  1.00 106.47 ?  112 CYS B HB2  1 
ATOM   7159  H HB3  . CYS B 1 103 ? 1.855   -15.013 89.158  1.00 106.47 ?  112 CYS B HB3  1 
ATOM   7160  H HG   . CYS B 1 103 ? 3.050   -12.966 90.415  1.00 92.37  ?  112 CYS B HG   1 
ATOM   7161  N N    . GLN B 1 104 ? 0.055   -14.893 86.203  1.00 93.23  ?  113 GLN B N    1 
ATOM   7162  C CA   . GLN B 1 104 ? -0.169  -15.923 85.197  1.00 103.68 ?  113 GLN B CA   1 
ATOM   7163  C C    . GLN B 1 104 ? 0.459   -15.523 83.865  1.00 118.85 ?  113 GLN B C    1 
ATOM   7164  O O    . GLN B 1 104 ? 0.923   -16.381 83.096  1.00 72.64  ?  113 GLN B O    1 
ATOM   7165  C CB   . GLN B 1 104 ? -1.684  -16.214 85.064  1.00 76.35  ?  113 GLN B CB   1 
ATOM   7166  C CG   . GLN B 1 104 ? -2.202  -17.255 86.072  1.00 79.85  ?  113 GLN B CG   1 
ATOM   7167  C CD   . GLN B 1 104 ? -3.695  -17.613 85.910  1.00 83.88  ?  113 GLN B CD   1 
ATOM   7168  H H    . GLN B 1 104 ? -0.650  -14.449 86.420  1.00 111.87 ?  113 GLN B H    1 
ATOM   7169  H HA   . GLN B 1 104 ? 0.262   -16.741 85.491  1.00 124.42 ?  113 GLN B HA   1 
ATOM   7170  H HB2  . GLN B 1 104 ? -2.175  -15.390 85.209  1.00 91.62  ?  113 GLN B HB2  1 
ATOM   7171  H HB3  . GLN B 1 104 ? -1.861  -16.550 84.172  1.00 91.62  ?  113 GLN B HB3  1 
ATOM   7172  H HG2  . GLN B 1 104 ? -1.690  -18.072 85.965  1.00 95.83  ?  113 GLN B HG2  1 
ATOM   7173  H HG3  . GLN B 1 104 ? -2.078  -16.907 86.969  1.00 95.83  ?  113 GLN B HG3  1 
ATOM   7174  N N    . LEU B 1 105 ? 0.360   -14.242 83.523  1.00 100.75 ?  114 LEU B N    1 
ATOM   7175  C CA   . LEU B 1 105 ? 0.868   -13.756 82.247  1.00 91.02  ?  114 LEU B CA   1 
ATOM   7176  C C    . LEU B 1 105 ? 2.394   -13.650 82.258  1.00 97.83  ?  114 LEU B C    1 
ATOM   7177  O O    . LEU B 1 105 ? 3.062   -13.915 81.240  1.00 74.67  ?  114 LEU B O    1 
ATOM   7178  C CB   . LEU B 1 105 ? 0.221   -12.418 81.951  1.00 96.26  ?  114 LEU B CB   1 
ATOM   7179  C CG   . LEU B 1 105 ? 0.486   -11.664 80.657  1.00 128.32 ?  114 LEU B CG   1 
ATOM   7180  C CD1  . LEU B 1 105 ? 0.044   -12.510 79.502  1.00 125.37 ?  114 LEU B CD1  1 
ATOM   7181  C CD2  . LEU B 1 105 ? -0.266  -10.348 80.638  1.00 169.43 ?  114 LEU B CD2  1 
ATOM   7182  H H    . LEU B 1 105 ? 0.002   -13.633 84.014  1.00 120.90 ?  114 LEU B H    1 
ATOM   7183  H HA   . LEU B 1 105 ? 0.614   -14.377 81.547  1.00 109.22 ?  114 LEU B HA   1 
ATOM   7184  H HB2  . LEU B 1 105 ? -0.739  -12.553 81.990  1.00 115.51 ?  114 LEU B HB2  1 
ATOM   7185  H HB3  . LEU B 1 105 ? 0.474   -11.816 82.668  1.00 115.51 ?  114 LEU B HB3  1 
ATOM   7186  H HG   . LEU B 1 105 ? 1.435   -11.485 80.569  1.00 153.98 ?  114 LEU B HG   1 
ATOM   7187  H HD11 . LEU B 1 105 ? 0.213   -12.030 78.677  1.00 150.45 ?  114 LEU B HD11 1 
ATOM   7188  H HD12 . LEU B 1 105 ? 0.544   -13.341 79.511  1.00 150.45 ?  114 LEU B HD12 1 
ATOM   7189  H HD13 . LEU B 1 105 ? -0.904  -12.694 79.591  1.00 150.45 ?  114 LEU B HD13 1 
ATOM   7190  H HD21 . LEU B 1 105 ? -0.078  -9.890  79.803  1.00 203.31 ?  114 LEU B HD21 1 
ATOM   7191  H HD22 . LEU B 1 105 ? -1.216  -10.527 80.711  1.00 203.31 ?  114 LEU B HD22 1 
ATOM   7192  H HD23 . LEU B 1 105 ? 0.028   -9.806  81.386  1.00 203.31 ?  114 LEU B HD23 1 
ATOM   7193  N N    . SER B 1 106 ? 2.962   -13.338 83.417  1.00 112.70 ?  115 SER B N    1 
ATOM   7194  C CA   . SER B 1 106 ? 4.408   -13.245 83.526  1.00 142.00 ?  115 SER B CA   1 
ATOM   7195  C C    . SER B 1 106 ? 5.056   -14.606 83.308  1.00 92.23  ?  115 SER B C    1 
ATOM   7196  O O    . SER B 1 106 ? 5.997   -14.732 82.524  1.00 105.64 ?  115 SER B O    1 
ATOM   7197  C CB   . SER B 1 106 ? 4.771   -12.662 84.888  1.00 145.17 ?  115 SER B CB   1 
ATOM   7198  O OG   . SER B 1 106 ? 4.282   -11.342 85.027  1.00 73.62  ?  115 SER B OG   1 
ATOM   7199  H H    . SER B 1 106 ? 2.537   -13.177 84.146  1.00 135.24 ?  115 SER B H    1 
ATOM   7200  H HA   . SER B 1 106 ? 4.740   -12.641 82.842  1.00 170.40 ?  115 SER B HA   1 
ATOM   7201  H HB2  . SER B 1 106 ? 4.380   -13.217 85.582  1.00 174.21 ?  115 SER B HB2  1 
ATOM   7202  H HB3  . SER B 1 106 ? 5.737   -12.652 84.979  1.00 174.21 ?  115 SER B HB3  1 
ATOM   7203  H HG   . SER B 1 106 ? 3.446   -11.336 84.952  1.00 88.34  ?  115 SER B HG   1 
ATOM   7204  N N    . LYS B 1 107 ? 4.554   -15.643 83.976  1.00 90.24  ?  116 LYS B N    1 
ATOM   7205  C CA   . LYS B 1 107 ? 5.109   -16.984 83.784  1.00 86.31  ?  116 LYS B CA   1 
ATOM   7206  C C    . LYS B 1 107 ? 5.110   -17.365 82.313  1.00 103.84 ?  116 LYS B C    1 
ATOM   7207  O O    . LYS B 1 107 ? 6.132   -17.827 81.788  1.00 102.27 ?  116 LYS B O    1 
ATOM   7208  C CB   . LYS B 1 107 ? 4.317   -18.020 84.602  1.00 81.47  ?  116 LYS B CB   1 
ATOM   7209  C CG   . LYS B 1 107 ? 4.823   -19.502 84.578  1.00 93.39  ?  116 LYS B CG   1 
ATOM   7210  H H    . LYS B 1 107 ? 3.904   -15.600 84.537  1.00 108.29 ?  116 LYS B H    1 
ATOM   7211  H HA   . LYS B 1 107 ? 6.028   -16.994 84.097  1.00 103.57 ?  116 LYS B HA   1 
ATOM   7212  H HB2  . LYS B 1 107 ? 4.319   -17.734 85.530  1.00 97.76  ?  116 LYS B HB2  1 
ATOM   7213  H HB3  . LYS B 1 107 ? 3.404   -18.026 84.274  1.00 97.76  ?  116 LYS B HB3  1 
ATOM   7214  H HG2  . LYS B 1 107 ? 4.822   -19.821 83.662  1.00 112.07 ?  116 LYS B HG2  1 
ATOM   7215  H HG3  . LYS B 1 107 ? 5.723   -19.535 84.940  1.00 112.07 ?  116 LYS B HG3  1 
ATOM   7216  N N    . LYS B 1 108 ? 4.018   -17.073 81.601  1.00 76.90  ?  117 LYS B N    1 
ATOM   7217  C CA   . LYS B 1 108 ? 3.956   -17.422 80.188  1.00 76.12  ?  117 LYS B CA   1 
ATOM   7218  C C    . LYS B 1 108 ? 5.054   -16.738 79.401  1.00 138.91 ?  117 LYS B C    1 
ATOM   7219  O O    . LYS B 1 108 ? 5.681   -17.354 78.531  1.00 124.40 ?  117 LYS B O    1 
ATOM   7220  C CB   . LYS B 1 108 ? 2.611   -17.035 79.607  1.00 73.42  ?  117 LYS B CB   1 
ATOM   7221  H H    . LYS B 1 108 ? 3.317   -16.681 81.908  1.00 92.27  ?  117 LYS B H    1 
ATOM   7222  H HA   . LYS B 1 108 ? 4.065   -18.381 80.091  1.00 91.34  ?  117 LYS B HA   1 
ATOM   7223  N N    . LEU B 1 109 ? 5.325   -15.476 79.715  1.00 123.55 ?  118 LEU B N    1 
ATOM   7224  C CA   . LEU B 1 109 ? 6.300   -14.686 78.972  1.00 97.64  ?  118 LEU B CA   1 
ATOM   7225  C C    . LEU B 1 109 ? 7.708   -14.790 79.555  1.00 88.83  ?  118 LEU B C    1 
ATOM   7226  O O    . LEU B 1 109 ? 8.611   -14.105 79.073  1.00 81.03  ?  118 LEU B O    1 
ATOM   7227  C CB   . LEU B 1 109 ? 5.867   -13.200 78.908  1.00 75.51  ?  118 LEU B CB   1 
ATOM   7228  C CG   . LEU B 1 109 ? 4.593   -12.795 78.092  1.00 65.10  ?  118 LEU B CG   1 
ATOM   7229  C CD1  . LEU B 1 109 ? 4.091   -11.435 78.481  1.00 61.42  ?  118 LEU B CD1  1 
ATOM   7230  C CD2  . LEU B 1 109 ? 4.732   -12.750 76.566  1.00 69.63  ?  118 LEU B CD2  1 
ATOM   7231  H H    . LEU B 1 109 ? 4.953   -15.049 80.362  1.00 148.26 ?  118 LEU B H    1 
ATOM   7232  H HA   . LEU B 1 109 ? 6.337   -15.019 78.062  1.00 117.17 ?  118 LEU B HA   1 
ATOM   7233  H HB2  . LEU B 1 109 ? 5.718   -12.901 79.819  1.00 90.61  ?  118 LEU B HB2  1 
ATOM   7234  H HB3  . LEU B 1 109 ? 6.607   -12.697 78.533  1.00 90.61  ?  118 LEU B HB3  1 
ATOM   7235  H HG   . LEU B 1 109 ? 3.889   -13.430 78.297  1.00 78.13  ?  118 LEU B HG   1 
ATOM   7236  H HD11 . LEU B 1 109 ? 3.305   -11.227 77.952  1.00 73.70  ?  118 LEU B HD11 1 
ATOM   7237  H HD12 . LEU B 1 109 ? 3.865   -11.440 79.424  1.00 73.70  ?  118 LEU B HD12 1 
ATOM   7238  H HD13 . LEU B 1 109 ? 4.788   -10.782 78.311  1.00 73.70  ?  118 LEU B HD13 1 
ATOM   7239  H HD21 . LEU B 1 109 ? 3.882   -12.487 76.180  1.00 83.55  ?  118 LEU B HD21 1 
ATOM   7240  H HD22 . LEU B 1 109 ? 5.416   -12.103 76.331  1.00 83.55  ?  118 LEU B HD22 1 
ATOM   7241  H HD23 . LEU B 1 109 ? 4.984   -13.630 76.246  1.00 83.55  ?  118 LEU B HD23 1 
ATOM   7242  N N    . GLU B 1 110 ? 7.921   -15.590 80.597  1.00 85.11  ?  119 GLU B N    1 
ATOM   7243  C CA   . GLU B 1 110 ? 9.257   -15.751 81.158  1.00 119.34 ?  119 GLU B CA   1 
ATOM   7244  C C    . GLU B 1 110 ? 9.801   -14.418 81.708  1.00 88.93  ?  119 GLU B C    1 
ATOM   7245  O O    . GLU B 1 110 ? 11.020  -14.187 81.765  1.00 82.46  ?  119 GLU B O    1 
ATOM   7246  C CB   . GLU B 1 110 ? 10.204  -16.368 80.120  1.00 64.13  ?  119 GLU B CB   1 
ATOM   7247  C CG   . GLU B 1 110 ? 9.864   -17.788 79.661  1.00 84.44  ?  119 GLU B CG   1 
ATOM   7248  C CD   . GLU B 1 110 ? 11.012  -18.491 78.920  1.00 114.54 ?  119 GLU B CD   1 
ATOM   7249  O OE1  . GLU B 1 110 ? 12.146  -18.566 79.460  1.00 140.62 ?  119 GLU B OE1  1 
ATOM   7250  O OE2  . GLU B 1 110 ? 10.770  -18.973 77.782  1.00 91.22  -1 119 GLU B OE2  1 
ATOM   7251  H H    . GLU B 1 110 ? 7.311   -16.047 80.995  1.00 102.14 ?  119 GLU B H    1 
ATOM   7252  H HA   . GLU B 1 110 ? 9.202   -16.370 81.903  1.00 143.20 ?  119 GLU B HA   1 
ATOM   7253  H HB2  . GLU B 1 110 ? 10.204  -15.801 79.332  1.00 76.96  ?  119 GLU B HB2  1 
ATOM   7254  H HB3  . GLU B 1 110 ? 11.097  -16.392 80.499  1.00 76.96  ?  119 GLU B HB3  1 
ATOM   7255  H HG2  . GLU B 1 110 ? 9.642   -18.323 80.438  1.00 101.33 ?  119 GLU B HG2  1 
ATOM   7256  H HG3  . GLU B 1 110 ? 9.104   -17.749 79.060  1.00 101.33 ?  119 GLU B HG3  1 
ATOM   7257  N N    . LEU B 1 111 ? 8.899   -13.538 82.135  1.00 99.83  ?  120 LEU B N    1 
ATOM   7258  C CA   . LEU B 1 111 ? 9.225   -12.279 82.791  1.00 78.70  ?  120 LEU B CA   1 
ATOM   7259  C C    . LEU B 1 111 ? 8.676   -12.228 84.221  1.00 61.85  ?  120 LEU B C    1 
ATOM   7260  O O    . LEU B 1 111 ? 7.782   -13.004 84.592  1.00 88.75  ?  120 LEU B O    1 
ATOM   7261  C CB   . LEU B 1 111 ? 8.702   -11.084 81.972  1.00 75.04  ?  120 LEU B CB   1 
ATOM   7262  C CG   . LEU B 1 111 ? 9.526   -10.802 80.701  1.00 143.29 ?  120 LEU B CG   1 
ATOM   7263  C CD1  . LEU B 1 111 ? 8.828   -10.007 79.632  1.00 54.29  ?  120 LEU B CD1  1 
ATOM   7264  C CD2  . LEU B 1 111 ? 10.774  -10.087 81.082  1.00 188.91 ?  120 LEU B CD2  1 
ATOM   7265  H H    . LEU B 1 111 ? 8.051   -13.657 82.049  1.00 119.80 ?  120 LEU B H    1 
ATOM   7266  H HA   . LEU B 1 111 ? 10.190  -12.199 82.845  1.00 94.44  ?  120 LEU B HA   1 
ATOM   7267  H HB2  . LEU B 1 111 ? 7.789   -11.265 81.700  1.00 90.05  ?  120 LEU B HB2  1 
ATOM   7268  H HB3  . LEU B 1 111 ? 8.729   -10.288 82.526  1.00 90.05  ?  120 LEU B HB3  1 
ATOM   7269  H HG   . LEU B 1 111 ? 9.785   -11.651 80.310  1.00 171.95 ?  120 LEU B HG   1 
ATOM   7270  H HD11 . LEU B 1 111 ? 9.432   -9.888  78.883  1.00 65.15  ?  120 LEU B HD11 1 
ATOM   7271  H HD12 . LEU B 1 111 ? 8.037   -10.490 79.347  1.00 65.15  ?  120 LEU B HD12 1 
ATOM   7272  H HD13 . LEU B 1 111 ? 8.577   -9.143  79.995  1.00 65.15  ?  120 LEU B HD13 1 
ATOM   7273  H HD21 . LEU B 1 111 ? 11.293  -9.910  80.282  1.00 226.70 ?  120 LEU B HD21 1 
ATOM   7274  H HD22 . LEU B 1 111 ? 10.539  -9.252  81.517  1.00 226.70 ?  120 LEU B HD22 1 
ATOM   7275  H HD23 . LEU B 1 111 ? 11.284  -10.645 81.690  1.00 226.70 ?  120 LEU B HD23 1 
ATOM   7276  N N    . PRO B 1 112 ? 9.202   -11.333 85.056  1.00 61.91  ?  121 PRO B N    1 
ATOM   7277  C CA   . PRO B 1 112 ? 8.672   -11.187 86.436  1.00 67.24  ?  121 PRO B CA   1 
ATOM   7278  C C    . PRO B 1 112 ? 7.410   -10.336 86.544  1.00 84.16  ?  121 PRO B C    1 
ATOM   7279  O O    . PRO B 1 112 ? 7.160   -9.403  85.752  1.00 61.21  ?  121 PRO B O    1 
ATOM   7280  C CB   . PRO B 1 112 ? 9.847   -10.529 87.191  1.00 55.61  ?  121 PRO B CB   1 
ATOM   7281  C CG   . PRO B 1 112 ? 10.678  -9.845  86.132  1.00 88.88  ?  121 PRO B CG   1 
ATOM   7282  C CD   . PRO B 1 112 ? 10.502  -10.633 84.872  1.00 81.46  ?  121 PRO B CD   1 
ATOM   7283  H HA   . PRO B 1 112 ? 8.499   -12.061 86.820  1.00 80.69  ?  121 PRO B HA   1 
ATOM   7284  H HB2  . PRO B 1 112 ? 9.504   -9.881  87.826  1.00 66.73  ?  121 PRO B HB2  1 
ATOM   7285  H HB3  . PRO B 1 112 ? 10.366  -11.211 87.644  1.00 66.73  ?  121 PRO B HB3  1 
ATOM   7286  H HG2  . PRO B 1 112 ? 10.361  -8.937  86.010  1.00 106.65 ?  121 PRO B HG2  1 
ATOM   7287  H HG3  . PRO B 1 112 ? 11.610  -9.845  86.403  1.00 106.65 ?  121 PRO B HG3  1 
ATOM   7288  H HD2  . PRO B 1 112 ? 10.458  -10.038 84.107  1.00 97.76  ?  121 PRO B HD2  1 
ATOM   7289  H HD3  . PRO B 1 112 ? 11.220  -11.278 84.776  1.00 97.76  ?  121 PRO B HD3  1 
ATOM   7290  N N    . PRO B 1 113 ? 6.538   -10.601 87.708  1.00 94.00  ?  122 PRO B N    1 
ATOM   7291  C CA   . PRO B 1 113 ? 5.380   -9.765  88.022  1.00 86.45  ?  122 PRO B CA   1 
ATOM   7292  C C    . PRO B 1 113 ? 5.795   -8.430  88.635  1.00 104.58 ?  122 PRO B C    1 
ATOM   7293  O O    . PRO B 1 113 ? 5.440   -8.069  89.785  1.00 66.16  ?  122 PRO B O    1 
ATOM   7294  C CB   . PRO B 1 113 ? 4.616   -10.649 89.007  1.00 121.99 ?  122 PRO B CB   1 
ATOM   7295  C CG   . PRO B 1 113 ? 5.695   -11.359 89.734  1.00 96.83  ?  122 PRO B CG   1 
ATOM   7296  C CD   . PRO B 1 113 ? 6.745   -11.634 88.730  1.00 78.96  ?  122 PRO B CD   1 
ATOM   7297  H HA   . PRO B 1 113 ? 4.840   -9.612  87.231  1.00 103.74 ?  122 PRO B HA   1 
ATOM   7298  H HB2  . PRO B 1 113 ? 4.093   -10.098 89.611  1.00 146.39 ?  122 PRO B HB2  1 
ATOM   7299  H HB3  . PRO B 1 113 ? 4.051   -11.273 88.525  1.00 146.39 ?  122 PRO B HB3  1 
ATOM   7300  H HG2  . PRO B 1 113 ? 6.039   -10.791 90.441  1.00 116.20 ?  122 PRO B HG2  1 
ATOM   7301  H HG3  . PRO B 1 113 ? 5.349   -12.188 90.101  1.00 116.20 ?  122 PRO B HG3  1 
ATOM   7302  H HD2  . PRO B 1 113 ? 7.624   -11.541 89.129  1.00 94.75  ?  122 PRO B HD2  1 
ATOM   7303  H HD3  . PRO B 1 113 ? 6.621   -12.517 88.347  1.00 94.75  ?  122 PRO B HD3  1 
ATOM   7304  N N    . ILE B 1 114 ? 6.559   -7.674  87.856  1.00 99.92  ?  123 ILE B N    1 
ATOM   7305  C CA   . ILE B 1 114 ? 6.862   -6.289  88.164  1.00 81.69  ?  123 ILE B CA   1 
ATOM   7306  C C    . ILE B 1 114 ? 7.076   -5.618  86.835  1.00 67.76  ?  123 ILE B C    1 
ATOM   7307  O O    . ILE B 1 114 ? 7.395   -6.269  85.840  1.00 67.69  ?  123 ILE B O    1 
ATOM   7308  C CB   . ILE B 1 114 ? 8.098   -6.047  89.059  1.00 95.69  ?  123 ILE B CB   1 
ATOM   7309  C CG1  . ILE B 1 114 ? 8.143   -4.565  89.429  1.00 77.41  ?  123 ILE B CG1  1 
ATOM   7310  C CG2  . ILE B 1 114 ? 9.398   -6.420  88.345  1.00 127.49 ?  123 ILE B CG2  1 
ATOM   7311  C CD1  . ILE B 1 114 ? 9.008   -4.275  90.627  1.00 60.08  ?  123 ILE B CD1  1 
ATOM   7312  H H    . ILE B 1 114 ? 6.921   -7.951  87.127  1.00 119.90 ?  123 ILE B H    1 
ATOM   7313  H HA   . ILE B 1 114 ? 6.093   -5.881  88.592  1.00 98.03  ?  123 ILE B HA   1 
ATOM   7314  H HB   . ILE B 1 114 ? 8.015   -6.575  89.868  1.00 114.83 ?  123 ILE B HB   1 
ATOM   7315  H HG12 . ILE B 1 114 ? 8.498   -4.064  88.677  1.00 92.89  ?  123 ILE B HG12 1 
ATOM   7316  H HG13 . ILE B 1 114 ? 7.244   -4.263  89.630  1.00 92.89  ?  123 ILE B HG13 1 
ATOM   7317  H HG21 . ILE B 1 114 ? 10.144  -6.253  88.941  1.00 152.99 ?  123 ILE B HG21 1 
ATOM   7318  H HG22 . ILE B 1 114 ? 9.368   -7.360  88.107  1.00 152.99 ?  123 ILE B HG22 1 
ATOM   7319  H HG23 . ILE B 1 114 ? 9.485   -5.879  87.545  1.00 152.99 ?  123 ILE B HG23 1 
ATOM   7320  H HD11 . ILE B 1 114 ? 8.991   -3.321  90.805  1.00 72.09  ?  123 ILE B HD11 1 
ATOM   7321  H HD12 . ILE B 1 114 ? 8.660   -4.760  91.392  1.00 72.09  ?  123 ILE B HD12 1 
ATOM   7322  H HD13 . ILE B 1 114 ? 9.915   -4.561  90.438  1.00 72.09  ?  123 ILE B HD13 1 
ATOM   7323  N N    . LEU B 1 115 ? 6.829   -4.319  86.820  1.00 74.62  ?  124 LEU B N    1 
ATOM   7324  C CA   . LEU B 1 115 ? 7.056   -3.507  85.643  1.00 75.90  ?  124 LEU B CA   1 
ATOM   7325  C C    . LEU B 1 115 ? 8.561   -3.393  85.362  1.00 81.62  ?  124 LEU B C    1 
ATOM   7326  O O    . LEU B 1 115 ? 9.348   -2.975  86.222  1.00 115.60 ?  124 LEU B O    1 
ATOM   7327  C CB   . LEU B 1 115 ? 6.428   -2.141  85.873  1.00 52.77  ?  124 LEU B CB   1 
ATOM   7328  C CG   . LEU B 1 115 ? 6.381   -1.167  84.683  1.00 51.52  ?  124 LEU B CG   1 
ATOM   7329  C CD1  . LEU B 1 115 ? 5.270   -1.511  83.633  1.00 58.29  ?  124 LEU B CD1  1 
ATOM   7330  C CD2  . LEU B 1 115 ? 6.236   0.225   85.111  1.00 62.08  ?  124 LEU B CD2  1 
ATOM   7331  H H    . LEU B 1 115 ? 6.525   -3.878  87.493  1.00 89.55  ?  124 LEU B H    1 
ATOM   7332  H HA   . LEU B 1 115 ? 6.628   -3.919  84.876  1.00 91.09  ?  124 LEU B HA   1 
ATOM   7333  H HB2  . LEU B 1 115 ? 5.512   -2.277  86.164  1.00 63.32  ?  124 LEU B HB2  1 
ATOM   7334  H HB3  . LEU B 1 115 ? 6.923   -1.700  86.581  1.00 63.32  ?  124 LEU B HB3  1 
ATOM   7335  H HG   . LEU B 1 115 ? 7.231   -1.229  84.220  1.00 61.82  ?  124 LEU B HG   1 
ATOM   7336  H HD11 . LEU B 1 115 ? 5.301   -0.858  82.916  1.00 69.95  ?  124 LEU B HD11 1 
ATOM   7337  H HD12 . LEU B 1 115 ? 5.434   -2.399  83.279  1.00 69.95  ?  124 LEU B HD12 1 
ATOM   7338  H HD13 . LEU B 1 115 ? 4.404   -1.483  84.069  1.00 69.95  ?  124 LEU B HD13 1 
ATOM   7339  H HD21 . LEU B 1 115 ? 6.212   0.795   84.326  1.00 74.50  ?  124 LEU B HD21 1 
ATOM   7340  H HD22 . LEU B 1 115 ? 5.410   0.316   85.612  1.00 74.50  ?  124 LEU B HD22 1 
ATOM   7341  H HD23 . LEU B 1 115 ? 6.991   0.463   85.670  1.00 74.50  ?  124 LEU B HD23 1 
ATOM   7342  N N    . VAL B 1 116 ? 8.968   -3.779  84.168  1.00 65.41  ?  125 VAL B N    1 
ATOM   7343  C CA   . VAL B 1 116 ? 10.354  -3.657  83.767  1.00 69.24  ?  125 VAL B CA   1 
ATOM   7344  C C    . VAL B 1 116 ? 10.452  -2.745  82.543  1.00 73.84  ?  125 VAL B C    1 
ATOM   7345  O O    . VAL B 1 116 ? 9.461   -2.331  81.955  1.00 91.17  ?  125 VAL B O    1 
ATOM   7346  C CB   . VAL B 1 116 ? 10.999  -5.031  83.459  1.00 61.32  ?  125 VAL B CB   1 
ATOM   7347  C CG1  . VAL B 1 116 ? 10.900  -6.037  84.645  1.00 56.40  ?  125 VAL B CG1  1 
ATOM   7348  C CG2  . VAL B 1 116 ? 10.444  -5.617  82.211  1.00 53.79  ?  125 VAL B CG2  1 
ATOM   7349  H H    . VAL B 1 116 ? 8.456   -4.118  83.566  1.00 78.49  ?  125 VAL B H    1 
ATOM   7350  H HA   . VAL B 1 116 ? 10.856  -3.246  84.488  1.00 83.09  ?  125 VAL B HA   1 
ATOM   7351  H HB   . VAL B 1 116 ? 11.945  -4.882  83.300  1.00 73.58  ?  125 VAL B HB   1 
ATOM   7352  H HG11 . VAL B 1 116 ? 11.321  -6.872  84.387  1.00 67.68  ?  125 VAL B HG11 1 
ATOM   7353  H HG12 . VAL B 1 116 ? 11.353  -5.662  85.416  1.00 67.68  ?  125 VAL B HG12 1 
ATOM   7354  H HG13 . VAL B 1 116 ? 9.964   -6.188  84.853  1.00 67.68  ?  125 VAL B HG13 1 
ATOM   7355  H HG21 . VAL B 1 116 ? 10.869  -6.474  82.048  1.00 64.55  ?  125 VAL B HG21 1 
ATOM   7356  H HG22 . VAL B 1 116 ? 9.487   -5.736  82.317  1.00 64.55  ?  125 VAL B HG22 1 
ATOM   7357  H HG23 . VAL B 1 116 ? 10.622  -5.014  81.472  1.00 64.55  ?  125 VAL B HG23 1 
ATOM   7358  N N    . TYR B 1 117 ? 11.684  -2.457  82.162  1.00 70.24  ?  126 TYR B N    1 
ATOM   7359  C CA   . TYR B 1 117 ? 11.944  -1.575  81.034  1.00 65.59  ?  126 TYR B CA   1 
ATOM   7360  C C    . TYR B 1 117 ? 11.372  -2.070  79.720  1.00 66.72  ?  126 TYR B C    1 
ATOM   7361  O O    . TYR B 1 117 ? 11.041  -1.260  78.856  1.00 66.34  ?  126 TYR B O    1 
ATOM   7362  C CB   . TYR B 1 117 ? 13.444  -1.423  80.903  1.00 47.79  ?  126 TYR B CB   1 
ATOM   7363  C CG   . TYR B 1 117 ? 13.997  -0.667  79.711  1.00 48.87  ?  126 TYR B CG   1 
ATOM   7364  C CD1  . TYR B 1 117 ? 14.407  -1.349  78.577  1.00 49.67  ?  126 TYR B CD1  1 
ATOM   7365  C CD2  . TYR B 1 117 ? 14.262  0.700   79.774  1.00 49.45  ?  126 TYR B CD2  1 
ATOM   7366  C CE1  . TYR B 1 117 ? 15.019  -0.679  77.514  1.00 85.11  ?  126 TYR B CE1  1 
ATOM   7367  C CE2  . TYR B 1 117 ? 14.870  1.374   78.726  1.00 50.87  ?  126 TYR B CE2  1 
ATOM   7368  C CZ   . TYR B 1 117 ? 15.224  0.679   77.604  1.00 51.58  ?  126 TYR B CZ   1 
ATOM   7369  O OH   . TYR B 1 117 ? 15.831  1.286   76.551  1.00 79.58  ?  126 TYR B OH   1 
ATOM   7370  H H    . TYR B 1 117 ? 12.393  -2.761  82.541  1.00 84.29  ?  126 TYR B H    1 
ATOM   7371  H HA   . TYR B 1 117 ? 11.566  -0.701  81.218  1.00 78.71  ?  126 TYR B HA   1 
ATOM   7372  H HB2  . TYR B 1 117 ? 13.766  -0.967  81.696  1.00 57.34  ?  126 TYR B HB2  1 
ATOM   7373  H HB3  . TYR B 1 117 ? 13.830  -2.312  80.873  1.00 57.34  ?  126 TYR B HB3  1 
ATOM   7374  H HD1  . TYR B 1 117 ? 14.272  -2.267  78.522  1.00 59.60  ?  126 TYR B HD1  1 
ATOM   7375  H HD2  . TYR B 1 117 ? 14.026  1.172   80.540  1.00 59.34  ?  126 TYR B HD2  1 
ATOM   7376  H HE1  . TYR B 1 117 ? 15.269  -1.143  76.747  1.00 102.13 ?  126 TYR B HE1  1 
ATOM   7377  H HE2  . TYR B 1 117 ? 15.016  2.291   78.777  1.00 61.04  ?  126 TYR B HE2  1 
ATOM   7378  H HH   . TYR B 1 117 ? 16.008  0.720   75.956  1.00 95.50  ?  126 TYR B HH   1 
ATOM   7379  N N    . ALA B 1 118 ? 11.298  -3.370  79.507  1.00 87.83  ?  127 ALA B N    1 
ATOM   7380  C CA   . ALA B 1 118 ? 10.850  -3.798  78.195  1.00 85.33  ?  127 ALA B CA   1 
ATOM   7381  C C    . ALA B 1 118 ? 9.352   -3.559  78.012  1.00 108.01 ?  127 ALA B C    1 
ATOM   7382  O O    . ALA B 1 118 ? 8.904   -3.516  76.865  1.00 54.89  ?  127 ALA B O    1 
ATOM   7383  C CB   . ALA B 1 118 ? 11.261  -5.278  77.924  1.00 69.18  ?  127 ALA B CB   1 
ATOM   7384  H H    . ALA B 1 118 ? 11.488  -3.994  80.068  1.00 105.40 ?  127 ALA B H    1 
ATOM   7385  H HA   . ALA B 1 118 ? 11.304  -3.254  77.533  1.00 102.40 ?  127 ALA B HA   1 
ATOM   7386  H HB1  . ALA B 1 118 ? 10.949  -5.536  77.043  1.00 83.02  ?  127 ALA B HB1  1 
ATOM   7387  H HB2  . ALA B 1 118 ? 12.227  -5.350  77.968  1.00 83.02  ?  127 ALA B HB2  1 
ATOM   7388  H HB3  . ALA B 1 118 ? 10.855  -5.846  78.598  1.00 83.02  ?  127 ALA B HB3  1 
ATOM   7389  N N    . ASP B 1 119 ? 8.595   -3.345  79.101  1.00 77.39  ?  128 ASP B N    1 
ATOM   7390  C CA   . ASP B 1 119 ? 7.177   -2.944  79.023  1.00 77.10  ?  128 ASP B CA   1 
ATOM   7391  C C    . ASP B 1 119 ? 7.006   -1.449  78.734  1.00 77.76  ?  128 ASP B C    1 
ATOM   7392  O O    . ASP B 1 119 ? 6.562   -1.046  77.658  1.00 83.55  ?  128 ASP B O    1 
ATOM   7393  C CB   . ASP B 1 119 ? 6.457   -3.239  80.346  1.00 75.83  ?  128 ASP B CB   1 
ATOM   7394  C CG   . ASP B 1 119 ? 6.277   -4.700  80.644  1.00 86.55  ?  128 ASP B CG   1 
ATOM   7395  O OD1  . ASP B 1 119 ? 5.940   -5.465  79.701  1.00 98.36  ?  128 ASP B OD1  1 
ATOM   7396  O OD2  . ASP B 1 119 ? 6.383   -5.050  81.848  1.00 91.62  -1 128 ASP B OD2  1 
ATOM   7397  H H    . ASP B 1 119 ? 8.884   -3.427  79.907  1.00 92.87  ?  128 ASP B H    1 
ATOM   7398  H HA   . ASP B 1 119 ? 6.739   -3.445  78.317  1.00 92.52  ?  128 ASP B HA   1 
ATOM   7399  H HB2  . ASP B 1 119 ? 6.970   -2.852  81.072  1.00 90.99  ?  128 ASP B HB2  1 
ATOM   7400  H HB3  . ASP B 1 119 ? 5.576   -2.834  80.317  1.00 90.99  ?  128 ASP B HB3  1 
ATOM   7401  N N    . CYS B 1 120 ? 7.342   -0.614  79.716  1.00 67.79  ?  129 CYS B N    1 
ATOM   7402  C CA   . CYS B 1 120 ? 7.084   0.812   79.737  1.00 73.25  ?  129 CYS B CA   1 
ATOM   7403  C C    . CYS B 1 120 ? 8.018   1.612   78.856  1.00 85.18  ?  129 CYS B C    1 
ATOM   7404  O O    . CYS B 1 120 ? 7.882   2.842   78.841  1.00 98.58  ?  129 CYS B O    1 
ATOM   7405  C CB   . CYS B 1 120 ? 7.233   1.339   81.162  1.00 78.48  ?  129 CYS B CB   1 
ATOM   7406  S SG   . CYS B 1 120 ? 8.868   1.294   81.993  1.00 83.42  ?  129 CYS B SG   1 
ATOM   7407  H H    . CYS B 1 120 ? 7.748   -0.879  80.427  1.00 81.34  ?  129 CYS B H    1 
ATOM   7408  H HA   . CYS B 1 120 ? 6.174   0.977   79.444  1.00 87.90  ?  129 CYS B HA   1 
ATOM   7409  H HB2  . CYS B 1 120 ? 6.952   2.268   81.159  1.00 94.17  ?  129 CYS B HB2  1 
ATOM   7410  H HB3  . CYS B 1 120 ? 6.625   0.833   81.724  1.00 94.17  ?  129 CYS B HB3  1 
ATOM   7411  H HG   . CYS B 1 120 ? 9.648   1.945   81.355  1.00 100.11 ?  129 CYS B HG   1 
ATOM   7412  N N    . VAL B 1 121 ? 8.966   0.968   78.152  1.00 80.25  ?  130 VAL B N    1 
ATOM   7413  C CA   . VAL B 1 121 ? 9.763   1.623   77.132  1.00 64.84  ?  130 VAL B CA   1 
ATOM   7414  C C    . VAL B 1 121 ? 9.648   0.921   75.784  1.00 59.79  ?  130 VAL B C    1 
ATOM   7415  O O    . VAL B 1 121 ? 9.595   1.578   74.747  1.00 74.95  ?  130 VAL B O    1 
ATOM   7416  C CB   . VAL B 1 121 ? 11.264  1.770   77.527  1.00 53.39  ?  130 VAL B CB   1 
ATOM   7417  C CG1  . VAL B 1 121 ? 11.987  2.505   76.435  1.00 57.44  ?  130 VAL B CG1  1 
ATOM   7418  C CG2  . VAL B 1 121 ? 11.488  2.584   78.803  1.00 74.54  ?  130 VAL B CG2  1 
ATOM   7419  H H    . VAL B 1 121 ? 9.160   0.137   78.259  1.00 96.30  ?  130 VAL B H    1 
ATOM   7420  H HA   . VAL B 1 121 ? 9.414   2.521   77.013  1.00 77.81  ?  130 VAL B HA   1 
ATOM   7421  H HB   . VAL B 1 121 ? 11.666  0.894   77.637  1.00 64.07  ?  130 VAL B HB   1 
ATOM   7422  H HG11 . VAL B 1 121 ? 12.921  2.596   76.682  1.00 68.93  ?  130 VAL B HG11 1 
ATOM   7423  H HG12 . VAL B 1 121 ? 11.910  2.000   75.611  1.00 68.93  ?  130 VAL B HG12 1 
ATOM   7424  H HG13 . VAL B 1 121 ? 11.587  3.381   76.326  1.00 68.93  ?  130 VAL B HG13 1 
ATOM   7425  H HG21 . VAL B 1 121 ? 12.439  2.632   78.984  1.00 89.45  ?  130 VAL B HG21 1 
ATOM   7426  H HG22 . VAL B 1 121 ? 11.130  3.477   78.674  1.00 89.45  ?  130 VAL B HG22 1 
ATOM   7427  H HG23 . VAL B 1 121 ? 11.031  2.148   79.540  1.00 89.45  ?  130 VAL B HG23 1 
ATOM   7428  N N    . LEU B 1 122 ? 9.696   -0.397  75.741  1.00 57.89  ?  131 LEU B N    1 
ATOM   7429  C CA   . LEU B 1 122 ? 9.800   -0.997  74.415  1.00 80.43  ?  131 LEU B CA   1 
ATOM   7430  C C    . LEU B 1 122 ? 8.419   -1.243  73.807  1.00 74.61  ?  131 LEU B C    1 
ATOM   7431  O O    . LEU B 1 122 ? 8.265   -1.315  72.578  1.00 77.19  ?  131 LEU B O    1 
ATOM   7432  C CB   . LEU B 1 122 ? 10.650  -2.272  74.496  1.00 73.35  ?  131 LEU B CB   1 
ATOM   7433  C CG   . LEU B 1 122 ? 12.063  -2.207  75.146  1.00 62.44  ?  131 LEU B CG   1 
ATOM   7434  C CD1  . LEU B 1 122 ? 12.726  -3.607  75.189  1.00 90.02  ?  131 LEU B CD1  1 
ATOM   7435  C CD2  . LEU B 1 122 ? 12.967  -1.292  74.379  1.00 61.00  ?  131 LEU B CD2  1 
ATOM   7436  H H    . LEU B 1 122 ? 9.672   -0.938  76.409  1.00 69.47  ?  131 LEU B H    1 
ATOM   7437  H HA   . LEU B 1 122 ? 10.265  -0.375  73.833  1.00 96.52  ?  131 LEU B HA   1 
ATOM   7438  H HB2  . LEU B 1 122 ? 10.144  -2.930  74.998  1.00 88.02  ?  131 LEU B HB2  1 
ATOM   7439  H HB3  . LEU B 1 122 ? 10.776  -2.598  73.591  1.00 88.02  ?  131 LEU B HB3  1 
ATOM   7440  H HG   . LEU B 1 122 ? 11.987  -1.875  76.054  1.00 74.93  ?  131 LEU B HG   1 
ATOM   7441  H HD11 . LEU B 1 122 ? 13.602  -3.528  75.598  1.00 108.02 ?  131 LEU B HD11 1 
ATOM   7442  H HD12 . LEU B 1 122 ? 12.168  -4.204  75.711  1.00 108.02 ?  131 LEU B HD12 1 
ATOM   7443  H HD13 . LEU B 1 122 ? 12.813  -3.942  74.283  1.00 108.02 ?  131 LEU B HD13 1 
ATOM   7444  H HD21 . LEU B 1 122 ? 13.836  -1.274  74.809  1.00 73.19  ?  131 LEU B HD21 1 
ATOM   7445  H HD22 . LEU B 1 122 ? 13.053  -1.621  73.471  1.00 73.19  ?  131 LEU B HD22 1 
ATOM   7446  H HD23 . LEU B 1 122 ? 12.582  -0.401  74.374  1.00 73.19  ?  131 LEU B HD23 1 
ATOM   7447  N N    . ALA B 1 123 ? 7.406   -1.289  74.655  1.00 67.61  ?  132 ALA B N    1 
ATOM   7448  C CA   . ALA B 1 123 ? 6.049   -1.634  74.265  1.00 73.34  ?  132 ALA B CA   1 
ATOM   7449  C C    . ALA B 1 123 ? 5.109   -0.457  74.504  1.00 80.16  ?  132 ALA B C    1 
ATOM   7450  O O    . ALA B 1 123 ? 3.899   -0.589  74.324  1.00 73.79  ?  132 ALA B O    1 
ATOM   7451  C CB   . ALA B 1 123 ? 5.572   -2.884  75.035  1.00 71.62  ?  132 ALA B CB   1 
ATOM   7452  H H    . ALA B 1 123 ? 7.482   -1.119  75.494  1.00 81.14  ?  132 ALA B H    1 
ATOM   7453  H HA   . ALA B 1 123 ? 6.036   -1.842  73.317  1.00 88.00  ?  132 ALA B HA   1 
ATOM   7454  H HB1  . ALA B 1 123 ? 4.666   -3.097  74.761  1.00 85.95  ?  132 ALA B HB1  1 
ATOM   7455  H HB2  . ALA B 1 123 ? 6.163   -3.625  74.831  1.00 85.95  ?  132 ALA B HB2  1 
ATOM   7456  H HB3  . ALA B 1 123 ? 5.594   -2.695  75.987  1.00 85.95  ?  132 ALA B HB3  1 
ATOM   7457  N N    . ASN B 1 124 ? 5.637   0.686   74.904  1.00 97.55  ?  133 ASN B N    1 
ATOM   7458  C CA   . ASN B 1 124 ? 4.784   1.770   75.345  1.00 100.95 ?  133 ASN B CA   1 
ATOM   7459  C C    . ASN B 1 124 ? 4.798   2.998   74.443  1.00 81.22  ?  133 ASN B C    1 
ATOM   7460  O O    . ASN B 1 124 ? 5.029   4.090   74.958  1.00 70.82  ?  133 ASN B O    1 
ATOM   7461  C CB   . ASN B 1 124 ? 5.228   2.144   76.758  1.00 106.47 ?  133 ASN B CB   1 
ATOM   7462  C CG   . ASN B 1 124 ? 4.390   3.187   77.340  1.00 86.25  ?  133 ASN B CG   1 
ATOM   7463  O OD1  . ASN B 1 124 ? 3.264   3.332   76.932  1.00 92.51  ?  133 ASN B OD1  1 
ATOM   7464  N ND2  . ASN B 1 124 ? 4.929   3.956   78.257  1.00 109.92 ?  133 ASN B ND2  1 
ATOM   7465  H H    . ASN B 1 124 ? 6.479   0.858   74.930  1.00 117.06 ?  133 ASN B H    1 
ATOM   7466  H HA   . ASN B 1 124 ? 3.870   1.449   75.394  1.00 121.14 ?  133 ASN B HA   1 
ATOM   7467  H HB2  . ASN B 1 124 ? 5.173   1.359   77.327  1.00 127.77 ?  133 ASN B HB2  1 
ATOM   7468  H HB3  . ASN B 1 124 ? 6.141   2.471   76.729  1.00 127.77 ?  133 ASN B HB3  1 
ATOM   7469  H HD21 . ASN B 1 124 ? 4.465   4.581   78.621  1.00 131.90 ?  133 ASN B HD21 1 
ATOM   7470  H HD22 . ASN B 1 124 ? 5.747   3.835   78.493  1.00 131.90 ?  133 ASN B HD22 1 
ATOM   7471  N N    . TRP B 1 125 ? 4.498   2.875   73.144  1.00 81.97  ?  134 TRP B N    1 
ATOM   7472  C CA   . TRP B 1 125 ? 4.681   4.005   72.245  1.00 84.54  ?  134 TRP B CA   1 
ATOM   7473  C C    . TRP B 1 125 ? 3.753   3.886   71.043  1.00 86.14  ?  134 TRP B C    1 
ATOM   7474  O O    . TRP B 1 125 ? 3.223   2.815   70.722  1.00 114.06 ?  134 TRP B O    1 
ATOM   7475  C CB   . TRP B 1 125 ? 6.153   4.130   71.810  1.00 87.21  ?  134 TRP B CB   1 
ATOM   7476  C CG   . TRP B 1 125 ? 6.660   3.012   70.985  1.00 96.29  ?  134 TRP B CG   1 
ATOM   7477  C CD1  . TRP B 1 125 ? 7.181   1.832   71.443  1.00 95.27  ?  134 TRP B CD1  1 
ATOM   7478  C CD2  . TRP B 1 125 ? 6.724   2.950   69.540  1.00 130.61 ?  134 TRP B CD2  1 
ATOM   7479  N NE1  . TRP B 1 125 ? 7.559   1.036   70.376  1.00 74.30  ?  134 TRP B NE1  1 
ATOM   7480  C CE2  . TRP B 1 125 ? 7.291   1.697   69.202  1.00 118.24 ?  134 TRP B CE2  1 
ATOM   7481  C CE3  . TRP B 1 125 ? 6.354   3.829   68.502  1.00 152.46 ?  134 TRP B CE3  1 
ATOM   7482  C CZ2  . TRP B 1 125 ? 7.494   1.299   67.874  1.00 115.26 ?  134 TRP B CZ2  1 
ATOM   7483  C CZ3  . TRP B 1 125 ? 6.558   3.429   67.181  1.00 149.89 ?  134 TRP B CZ3  1 
ATOM   7484  C CH2  . TRP B 1 125 ? 7.124   2.174   66.883  1.00 138.17 ?  134 TRP B CH2  1 
ATOM   7485  H H    . TRP B 1 125 ? 4.195   2.162   72.771  1.00 98.36  ?  134 TRP B H    1 
ATOM   7486  H HA   . TRP B 1 125 ? 4.445   4.818   72.718  1.00 101.44 ?  134 TRP B HA   1 
ATOM   7487  H HB2  . TRP B 1 125 ? 6.254   4.944   71.292  1.00 104.66 ?  134 TRP B HB2  1 
ATOM   7488  H HB3  . TRP B 1 125 ? 6.706   4.180   72.605  1.00 104.66 ?  134 TRP B HB3  1 
ATOM   7489  H HD1  . TRP B 1 125 ? 7.268   1.599   72.339  1.00 114.33 ?  134 TRP B HD1  1 
ATOM   7490  H HE1  . TRP B 1 125 ? 7.908   0.252   70.439  1.00 89.17  ?  134 TRP B HE1  1 
ATOM   7491  H HE3  . TRP B 1 125 ? 5.979   4.658   68.694  1.00 182.96 ?  134 TRP B HE3  1 
ATOM   7492  H HZ2  . TRP B 1 125 ? 7.867   0.472   67.671  1.00 138.32 ?  134 TRP B HZ2  1 
ATOM   7493  H HZ3  . TRP B 1 125 ? 6.318   4.000   66.487  1.00 179.86 ?  134 TRP B HZ3  1 
ATOM   7494  H HH2  . TRP B 1 125 ? 7.250   1.932   65.994  1.00 165.81 ?  134 TRP B HH2  1 
ATOM   7495  N N    . LYS B 1 126 ? 3.579   5.030   70.387  1.00 77.15  ?  135 LYS B N    1 
ATOM   7496  C CA   . LYS B 1 126 ? 2.704   5.215   69.244  1.00 81.83  ?  135 LYS B CA   1 
ATOM   7497  C C    . LYS B 1 126 ? 3.387   6.161   68.264  1.00 89.95  ?  135 LYS B C    1 
ATOM   7498  O O    . LYS B 1 126 ? 3.980   7.167   68.672  1.00 101.74 ?  135 LYS B O    1 
ATOM   7499  C CB   . LYS B 1 126 ? 1.343   5.830   69.711  1.00 88.99  ?  135 LYS B CB   1 
ATOM   7500  H H    . LYS B 1 126 ? 3.988   5.754   70.605  1.00 92.58  ?  135 LYS B H    1 
ATOM   7501  H HA   . LYS B 1 126 ? 2.539   4.366   68.806  1.00 98.19  ?  135 LYS B HA   1 
ATOM   7502  N N    . LYS B 1 127 ? 3.233   5.904   66.972  1.00 84.30  ?  136 LYS B N    1 
ATOM   7503  C CA   . LYS B 1 127 ? 3.661   6.883   65.991  1.00 96.86  ?  136 LYS B CA   1 
ATOM   7504  C C    . LYS B 1 127 ? 2.461   7.787   65.813  1.00 113.29 ?  136 LYS B C    1 
ATOM   7505  O O    . LYS B 1 127 ? 1.366   7.292   65.549  1.00 130.43 ?  136 LYS B O    1 
ATOM   7506  C CB   . LYS B 1 127 ? 4.071   6.215   64.678  1.00 106.93 ?  136 LYS B CB   1 
ATOM   7507  H H    . LYS B 1 127 ? 2.891   5.186   66.644  1.00 101.16 ?  136 LYS B H    1 
ATOM   7508  H HA   . LYS B 1 127 ? 4.405   7.401   66.334  1.00 116.23 ?  136 LYS B HA   1 
ATOM   7509  N N    . LYS B 1 128 ? 2.631   9.092   66.018  1.00 127.35 ?  137 LYS B N    1 
ATOM   7510  C CA   . LYS B 1 128 ? 1.472   9.964   65.872  1.00 131.56 ?  137 LYS B CA   1 
ATOM   7511  C C    . LYS B 1 128 ? 0.929   9.901   64.451  1.00 135.11 ?  137 LYS B C    1 
ATOM   7512  O O    . LYS B 1 128 ? -0.258  9.637   64.240  1.00 109.39 ?  137 LYS B O    1 
ATOM   7513  C CB   . LYS B 1 128 ? 1.797   11.405  66.246  1.00 129.46 ?  137 LYS B CB   1 
ATOM   7514  C CG   . LYS B 1 128 ? 1.930   11.675  67.739  1.00 116.93 ?  137 LYS B CG   1 
ATOM   7515  C CD   . LYS B 1 128 ? 2.363   13.132  67.954  1.00 99.93  ?  137 LYS B CD   1 
ATOM   7516  C CE   . LYS B 1 128 ? 2.342   13.559  69.402  1.00 175.72 ?  137 LYS B CE   1 
ATOM   7517  N NZ   . LYS B 1 128 ? 2.832   14.949  69.500  1.00 209.07 1  137 LYS B NZ   1 
ATOM   7518  H H    . LYS B 1 128 ? 3.368   9.480   66.231  1.00 152.82 ?  137 LYS B H    1 
ATOM   7519  H HA   . LYS B 1 128 ? 0.773   9.655   66.469  1.00 157.88 ?  137 LYS B HA   1 
ATOM   7520  H HB2  . LYS B 1 128 ? 2.639   11.648  65.829  1.00 155.35 ?  137 LYS B HB2  1 
ATOM   7521  H HB3  . LYS B 1 128 ? 1.091   11.977  65.908  1.00 155.35 ?  137 LYS B HB3  1 
ATOM   7522  H HG2  . LYS B 1 128 ? 1.074   11.538  68.174  1.00 140.32 ?  137 LYS B HG2  1 
ATOM   7523  H HG3  . LYS B 1 128 ? 2.605   11.091  68.119  1.00 140.32 ?  137 LYS B HG3  1 
ATOM   7524  H HD2  . LYS B 1 128 ? 3.268   13.242  67.624  1.00 119.92 ?  137 LYS B HD2  1 
ATOM   7525  H HD3  . LYS B 1 128 ? 1.760   13.713  67.464  1.00 119.92 ?  137 LYS B HD3  1 
ATOM   7526  H HE2  . LYS B 1 128 ? 1.435   13.523  69.742  1.00 210.86 ?  137 LYS B HE2  1 
ATOM   7527  H HE3  . LYS B 1 128 ? 2.927   12.985  69.921  1.00 210.86 ?  137 LYS B HE3  1 
ATOM   7528  H HZ1  . LYS B 1 128 ? 2.825   15.214  70.349  1.00 250.88 ?  137 LYS B HZ1  1 
ATOM   7529  H HZ2  . LYS B 1 128 ? 3.663   15.001  69.186  1.00 250.88 ?  137 LYS B HZ2  1 
ATOM   7530  H HZ3  . LYS B 1 128 ? 2.309   15.489  69.023  1.00 250.88 ?  137 LYS B HZ3  1 
ATOM   7531  N N    . ASP B 1 129 ? 1.783   10.143  63.466  1.00 132.28 ?  138 ASP B N    1 
ATOM   7532  C CA   . ASP B 1 129 ? 1.415   9.963   62.070  1.00 132.14 ?  138 ASP B CA   1 
ATOM   7533  C C    . ASP B 1 129 ? 2.173   8.747   61.550  1.00 166.98 ?  138 ASP B C    1 
ATOM   7534  O O    . ASP B 1 129 ? 3.404   8.812   61.392  1.00 159.79 ?  138 ASP B O    1 
ATOM   7535  C CB   . ASP B 1 129 ? 1.758   11.207  61.250  1.00 161.25 ?  138 ASP B CB   1 
ATOM   7536  C CG   . ASP B 1 129 ? 1.222   11.140  59.831  1.00 137.99 ?  138 ASP B CG   1 
ATOM   7537  O OD1  . ASP B 1 129 ? 0.781   10.054  59.409  1.00 159.45 ?  138 ASP B OD1  1 
ATOM   7538  O OD2  . ASP B 1 129 ? 1.275   12.163  59.122  1.00 168.50 -1 138 ASP B OD2  1 
ATOM   7539  N N    . PRO B 1 130 ? 1.506   7.612   61.323  1.00 153.29 ?  139 PRO B N    1 
ATOM   7540  C CA   . PRO B 1 130 ? 2.210   6.441   60.770  1.00 154.86 ?  139 PRO B CA   1 
ATOM   7541  C C    . PRO B 1 130 ? 3.013   6.783   59.532  1.00 171.40 ?  139 PRO B C    1 
ATOM   7542  O O    . PRO B 1 130 ? 4.085   6.211   59.286  1.00 183.49 ?  139 PRO B O    1 
ATOM   7543  C CB   . PRO B 1 130 ? 1.064   5.471   60.455  1.00 172.80 ?  139 PRO B CB   1 
ATOM   7544  C CG   . PRO B 1 130 ? -0.028  5.845   61.417  1.00 150.51 ?  139 PRO B CG   1 
ATOM   7545  C CD   . PRO B 1 130 ? 0.097   7.328   61.655  1.00 126.46 ?  139 PRO B CD   1 
ATOM   7546  N N    . ASN B 1 131 ? 2.491   7.706   58.729  1.00 154.77 ?  140 ASN B N    1 
ATOM   7547  C CA   . ASN B 1 131 ? 3.127   8.112   57.489  1.00 132.98 ?  140 ASN B CA   1 
ATOM   7548  C C    . ASN B 1 131 ? 4.409   8.894   57.743  1.00 133.49 ?  140 ASN B C    1 
ATOM   7549  O O    . ASN B 1 131 ? 5.276   8.939   56.866  1.00 134.87 ?  140 ASN B O    1 
ATOM   7550  C CB   . ASN B 1 131 ? 2.116   8.931   56.676  1.00 128.83 ?  140 ASN B CB   1 
ATOM   7551  C CG   . ASN B 1 131 ? 2.736   9.621   55.507  1.00 120.97 ?  140 ASN B CG   1 
ATOM   7552  O OD1  . ASN B 1 131 ? 2.375   10.749  55.178  1.00 148.59 ?  140 ASN B OD1  1 
ATOM   7553  N ND2  . ASN B 1 131 ? 3.692   8.954   54.869  1.00 131.72 ?  140 ASN B ND2  1 
ATOM   7554  N N    . LYS B 1 132 ? 4.528   9.527   58.919  1.00 143.51 ?  141 LYS B N    1 
ATOM   7555  C CA   . LYS B 1 132 ? 5.629   10.357  59.387  1.00 147.23 ?  141 LYS B CA   1 
ATOM   7556  C C    . LYS B 1 132 ? 6.718   9.542   60.091  1.00 151.38 ?  141 LYS B C    1 
ATOM   7557  O O    . LYS B 1 132 ? 6.521   8.386   60.485  1.00 149.87 ?  141 LYS B O    1 
ATOM   7558  C CB   . LYS B 1 132 ? 5.103   11.443  60.324  1.00 160.30 ?  141 LYS B CB   1 
ATOM   7559  N N    . PRO B 1 133 ? 7.891   10.132  60.255  1.00 129.79 ?  142 PRO B N    1 
ATOM   7560  C CA   . PRO B 1 133 ? 9.037   9.411   60.816  1.00 106.07 ?  142 PRO B CA   1 
ATOM   7561  C C    . PRO B 1 133 ? 9.018   9.307   62.338  1.00 110.30 ?  142 PRO B C    1 
ATOM   7562  O O    . PRO B 1 133 ? 8.171   9.869   63.029  1.00 105.29 ?  142 PRO B O    1 
ATOM   7563  C CB   . PRO B 1 133 ? 10.222  10.258  60.356  1.00 103.24 ?  142 PRO B CB   1 
ATOM   7564  C CG   . PRO B 1 133 ? 9.661   11.624  60.222  1.00 149.13 ?  142 PRO B CG   1 
ATOM   7565  C CD   . PRO B 1 133 ? 8.253   11.464  59.755  1.00 130.34 ?  142 PRO B CD   1 
ATOM   7566  N N    . LEU B 1 134 ? 10.013  8.573   62.851  1.00 115.85 ?  143 LEU B N    1 
ATOM   7567  C CA   . LEU B 1 134 ? 10.166  8.316   64.287  1.00 102.77 ?  143 LEU B CA   1 
ATOM   7568  C C    . LEU B 1 134 ? 11.006  9.402   64.971  1.00 115.60 ?  143 LEU B C    1 
ATOM   7569  O O    . LEU B 1 134 ? 12.160  9.200   65.335  1.00 118.86 ?  143 LEU B O    1 
ATOM   7570  C CB   . LEU B 1 134 ? 10.772  6.939   64.508  1.00 133.16 ?  143 LEU B CB   1 
ATOM   7571  C CG   . LEU B 1 134 ? 9.954   5.732   64.049  1.00 107.98 ?  143 LEU B CG   1 
ATOM   7572  C CD1  . LEU B 1 134 ? 10.853  4.535   63.904  1.00 123.33 ?  143 LEU B CD1  1 
ATOM   7573  C CD2  . LEU B 1 134 ? 8.837   5.384   64.991  1.00 81.16  ?  143 LEU B CD2  1 
ATOM   7574  N N    . THR B 1 135 ? 10.413  10.583  65.130  1.00 126.28 ?  144 THR B N    1 
ATOM   7575  C CA   . THR B 1 135 ? 10.992  11.633  65.959  1.00 119.19 ?  144 THR B CA   1 
ATOM   7576  C C    . THR B 1 135 ? 10.168  11.862  67.213  1.00 148.87 ?  144 THR B C    1 
ATOM   7577  O O    . THR B 1 135 ? 9.003   11.475  67.307  1.00 84.62  ?  144 THR B O    1 
ATOM   7578  C CB   . THR B 1 135 ? 11.107  12.946  65.186  1.00 105.99 ?  144 THR B CB   1 
ATOM   7579  O OG1  . THR B 1 135 ? 9.811   13.345  64.738  1.00 129.76 ?  144 THR B OG1  1 
ATOM   7580  C CG2  . THR B 1 135 ? 12.032  12.849  64.032  1.00 101.26 ?  144 THR B CG2  1 
ATOM   7581  H H    . THR B 1 135 ? 9.666   10.801  64.763  1.00 151.53 ?  144 THR B H    1 
ATOM   7582  H HA   . THR B 1 135 ? 11.884  11.366  66.230  1.00 143.03 ?  144 THR B HA   1 
ATOM   7583  H HB   . THR B 1 135 ? 11.452  13.628  65.783  1.00 127.19 ?  144 THR B HB   1 
ATOM   7584  H HG1  . THR B 1 135 ? 9.864   14.066  64.311  1.00 155.72 ?  144 THR B HG1  1 
ATOM   7585  H HG21 . THR B 1 135 ? 12.076  13.701  63.570  1.00 121.51 ?  144 THR B HG21 1 
ATOM   7586  H HG22 . THR B 1 135 ? 12.921  12.611  64.340  1.00 121.51 ?  144 THR B HG22 1 
ATOM   7587  H HG23 . THR B 1 135 ? 11.720  12.171  63.413  1.00 121.51 ?  144 THR B HG23 1 
ATOM   7588  N N    . TYR B 1 136 ? 10.775  12.558  68.171  1.00 115.25 ?  145 TYR B N    1 
ATOM   7589  C CA   . TYR B 1 136 ? 10.035  12.893  69.383  1.00 119.44 ?  145 TYR B CA   1 
ATOM   7590  C C    . TYR B 1 136 ? 8.739   13.602  69.021  1.00 132.39 ?  145 TYR B C    1 
ATOM   7591  O O    . TYR B 1 136 ? 7.672   13.228  69.507  1.00 120.30 ?  145 TYR B O    1 
ATOM   7592  C CB   . TYR B 1 136 ? 10.898  13.772  70.288  1.00 129.12 ?  145 TYR B CB   1 
ATOM   7593  C CG   . TYR B 1 136 ? 10.307  14.107  71.637  1.00 122.65 ?  145 TYR B CG   1 
ATOM   7594  C CD1  . TYR B 1 136 ? 10.396  13.219  72.695  1.00 158.73 ?  145 TYR B CD1  1 
ATOM   7595  C CD2  . TYR B 1 136 ? 9.709   15.326  71.868  1.00 122.23 ?  145 TYR B CD2  1 
ATOM   7596  C CE1  . TYR B 1 136 ? 9.878   13.524  73.934  1.00 128.45 ?  145 TYR B CE1  1 
ATOM   7597  C CE2  . TYR B 1 136 ? 9.184   15.636  73.106  1.00 107.40 ?  145 TYR B CE2  1 
ATOM   7598  C CZ   . TYR B 1 136 ? 9.273   14.728  74.136  1.00 87.83  ?  145 TYR B CZ   1 
ATOM   7599  O OH   . TYR B 1 136 ? 8.767   15.023  75.370  1.00 92.48  ?  145 TYR B OH   1 
ATOM   7600  H H    . TYR B 1 136 ? 11.587  12.839  68.146  1.00 138.30 ?  145 TYR B H    1 
ATOM   7601  H HA   . TYR B 1 136 ? 9.817   12.079  69.863  1.00 143.33 ?  145 TYR B HA   1 
ATOM   7602  H HB2  . TYR B 1 136 ? 11.739  13.316  70.445  1.00 154.94 ?  145 TYR B HB2  1 
ATOM   7603  H HB3  . TYR B 1 136 ? 11.066  14.610  69.829  1.00 154.94 ?  145 TYR B HB3  1 
ATOM   7604  H HD1  . TYR B 1 136 ? 10.804  12.394  72.563  1.00 190.48 ?  145 TYR B HD1  1 
ATOM   7605  H HD2  . TYR B 1 136 ? 9.642   15.943  71.175  1.00 146.68 ?  145 TYR B HD2  1 
ATOM   7606  H HE1  . TYR B 1 136 ? 9.939   12.909  74.630  1.00 154.14 ?  145 TYR B HE1  1 
ATOM   7607  H HE2  . TYR B 1 136 ? 8.775   16.460  73.246  1.00 128.88 ?  145 TYR B HE2  1 
ATOM   7608  H HH   . TYR B 1 136 ? 8.423   15.790  75.363  1.00 110.97 ?  145 TYR B HH   1 
ATOM   7609  N N    . GLU B 1 137 ? 8.801   14.562  68.085  1.00 122.92 ?  146 GLU B N    1 
ATOM   7610  C CA   . GLU B 1 137 ? 7.636   15.357  67.712  1.00 123.12 ?  146 GLU B CA   1 
ATOM   7611  C C    . GLU B 1 137 ? 6.543   14.521  67.066  1.00 120.94 ?  146 GLU B C    1 
ATOM   7612  O O    . GLU B 1 137 ? 5.364   14.887  67.158  1.00 110.79 ?  146 GLU B O    1 
ATOM   7613  C CB   . GLU B 1 137 ? 8.055   16.481  66.749  1.00 128.06 ?  146 GLU B CB   1 
ATOM   7614  C CG   . GLU B 1 137 ? 8.681   17.681  67.444  1.00 134.63 ?  146 GLU B CG   1 
ATOM   7615  C CD   . GLU B 1 137 ? 9.967   17.306  68.162  1.00 156.13 ?  146 GLU B CD   1 
ATOM   7616  O OE1  . GLU B 1 137 ? 10.668  16.403  67.666  1.00 141.16 ?  146 GLU B OE1  1 
ATOM   7617  O OE2  . GLU B 1 137 ? 10.268  17.883  69.231  1.00 179.99 -1 146 GLU B OE2  1 
ATOM   7618  H H    . GLU B 1 137 ? 9.516   14.769  67.652  1.00 147.50 ?  146 GLU B H    1 
ATOM   7619  H HA   . GLU B 1 137 ? 7.266   15.767  68.509  1.00 147.75 ?  146 GLU B HA   1 
ATOM   7620  H HB2  . GLU B 1 137 ? 8.705   16.129  66.121  1.00 153.67 ?  146 GLU B HB2  1 
ATOM   7621  H HB3  . GLU B 1 137 ? 7.270   16.792  66.271  1.00 153.67 ?  146 GLU B HB3  1 
ATOM   7622  H HG2  . GLU B 1 137 ? 8.890   18.360  66.784  1.00 161.55 ?  146 GLU B HG2  1 
ATOM   7623  H HG3  . GLU B 1 137 ? 8.059   18.032  68.100  1.00 161.55 ?  146 GLU B HG3  1 
ATOM   7624  N N    . ASN B 1 138 ? 6.888   13.378  66.479  1.00 119.18 ?  147 ASN B N    1 
ATOM   7625  C CA   . ASN B 1 138 ? 5.888   12.519  65.863  1.00 105.16 ?  147 ASN B CA   1 
ATOM   7626  C C    . ASN B 1 138 ? 5.409   11.420  66.794  1.00 92.68  ?  147 ASN B C    1 
ATOM   7627  O O    . ASN B 1 138 ? 4.521   10.654  66.411  1.00 92.82  ?  147 ASN B O    1 
ATOM   7628  C CB   . ASN B 1 138 ? 6.441   11.897  64.569  1.00 104.08 ?  147 ASN B CB   1 
ATOM   7629  C CG   . ASN B 1 138 ? 5.362   11.184  63.741  1.00 114.66 ?  147 ASN B CG   1 
ATOM   7630  O OD1  . ASN B 1 138 ? 4.254   11.685  63.563  1.00 173.49 ?  147 ASN B OD1  1 
ATOM   7631  N ND2  . ASN B 1 138 ? 5.690   10.001  63.254  1.00 120.77 ?  147 ASN B ND2  1 
ATOM   7632  H H    . ASN B 1 138 ? 7.693   13.080  66.425  1.00 143.01 ?  147 ASN B H    1 
ATOM   7633  H HA   . ASN B 1 138 ? 5.119   13.060  65.625  1.00 126.19 ?  147 ASN B HA   1 
ATOM   7634  H HB2  . ASN B 1 138 ? 6.825   12.598  64.021  1.00 124.89 ?  147 ASN B HB2  1 
ATOM   7635  H HB3  . ASN B 1 138 ? 7.122   11.245  64.798  1.00 124.89 ?  147 ASN B HB3  1 
ATOM   7636  H HD21 . ASN B 1 138 ? 5.123   9.558   62.782  1.00 144.92 ?  147 ASN B HD21 1 
ATOM   7637  H HD22 . ASN B 1 138 ? 6.470   9.674   63.408  1.00 144.92 ?  147 ASN B HD22 1 
ATOM   7638  N N    . MET B 1 139 ? 5.862   11.396  68.034  1.00 84.73  ?  148 MET B N    1 
ATOM   7639  C CA   . MET B 1 139 ? 5.604   10.257  68.891  1.00 88.13  ?  148 MET B CA   1 
ATOM   7640  C C    . MET B 1 139 ? 4.919   10.640  70.196  1.00 88.13  ?  148 MET B C    1 
ATOM   7641  O O    . MET B 1 139 ? 4.996   11.773  70.682  1.00 102.73 ?  148 MET B O    1 
ATOM   7642  C CB   . MET B 1 139 ? 6.915   9.543   69.215  1.00 96.55  ?  148 MET B CB   1 
ATOM   7643  C CG   . MET B 1 139 ? 7.486   8.812   68.019  1.00 127.51 ?  148 MET B CG   1 
ATOM   7644  S SD   . MET B 1 139 ? 9.153   8.191   68.278  1.00 107.32 ?  148 MET B SD   1 
ATOM   7645  C CE   . MET B 1 139 ? 8.740   6.720   69.182  1.00 82.69  ?  148 MET B CE   1 
ATOM   7646  H H    . MET B 1 139 ? 6.320   12.024  68.402  1.00 101.67 ?  148 MET B H    1 
ATOM   7647  H HA   . MET B 1 139 ? 5.036   9.631   68.414  1.00 105.75 ?  148 MET B HA   1 
ATOM   7648  H HB2  . MET B 1 139 ? 7.568   10.197  69.509  1.00 115.86 ?  148 MET B HB2  1 
ATOM   7649  H HB3  . MET B 1 139 ? 6.756   8.892   69.917  1.00 115.86 ?  148 MET B HB3  1 
ATOM   7650  H HG2  . MET B 1 139 ? 6.916   8.055   67.813  1.00 153.02 ?  148 MET B HG2  1 
ATOM   7651  H HG3  . MET B 1 139 ? 7.511   9.421   67.263  1.00 153.02 ?  148 MET B HG3  1 
ATOM   7652  H HE1  . MET B 1 139 ? 9.557   6.249   69.408  1.00 99.22  ?  148 MET B HE1  1 
ATOM   7653  H HE2  . MET B 1 139 ? 8.266   6.969   69.991  1.00 99.22  ?  148 MET B HE2  1 
ATOM   7654  H HE3  . MET B 1 139 ? 8.176   6.157   68.628  1.00 99.22  ?  148 MET B HE3  1 
ATOM   7655  N N    . ASP B 1 140 ? 4.253   9.656   70.777  1.00 80.03  ?  149 ASP B N    1 
ATOM   7656  C CA   . ASP B 1 140 ? 3.779   9.817   72.128  1.00 80.62  ?  149 ASP B CA   1 
ATOM   7657  C C    . ASP B 1 140 ? 3.865   8.456   72.779  1.00 99.20  ?  149 ASP B C    1 
ATOM   7658  O O    . ASP B 1 140 ? 3.898   7.425   72.108  1.00 130.44 ?  149 ASP B O    1 
ATOM   7659  C CB   . ASP B 1 140 ? 2.362   10.389  72.198  1.00 122.49 ?  149 ASP B CB   1 
ATOM   7660  C CG   . ASP B 1 140 ? 2.325   11.740  72.873  1.00 84.30  ?  149 ASP B CG   1 
ATOM   7661  H H    . ASP B 1 140 ? 4.066   8.899   70.413  1.00 96.03  ?  149 ASP B H    1 
ATOM   7662  H HA   . ASP B 1 140 ? 4.372   10.419  72.605  1.00 96.74  ?  149 ASP B HA   1 
ATOM   7663  H HB2  . ASP B 1 140 ? 2.017   10.492  71.297  1.00 146.99 ?  149 ASP B HB2  1 
ATOM   7664  H HB3  . ASP B 1 140 ? 1.799   9.783   72.704  1.00 146.99 ?  149 ASP B HB3  1 
ATOM   7665  N N    . VAL B 1 141 ? 3.890   8.463   74.101  1.00 113.55 ?  150 VAL B N    1 
ATOM   7666  C CA   . VAL B 1 141 ? 3.791   7.210   74.831  1.00 100.70 ?  150 VAL B CA   1 
ATOM   7667  C C    . VAL B 1 141 ? 2.312   6.911   75.016  1.00 109.93 ?  150 VAL B C    1 
ATOM   7668  O O    . VAL B 1 141 ? 1.466   7.789   74.794  1.00 124.20 ?  150 VAL B O    1 
ATOM   7669  C CB   . VAL B 1 141 ? 4.548   7.259   76.175  1.00 100.33 ?  150 VAL B CB   1 
ATOM   7670  C CG1  . VAL B 1 141 ? 5.999   7.559   75.914  1.00 114.29 ?  150 VAL B CG1  1 
ATOM   7671  C CG2  . VAL B 1 141 ? 4.002   8.270   77.101  1.00 74.34  ?  150 VAL B CG2  1 
ATOM   7672  H H    . VAL B 1 141 ? 3.963   9.164   74.593  1.00 136.25 ?  150 VAL B H    1 
ATOM   7673  H HA   . VAL B 1 141 ? 4.177   6.499   74.295  1.00 120.84 ?  150 VAL B HA   1 
ATOM   7674  H HB   . VAL B 1 141 ? 4.491   6.391   76.605  1.00 120.40 ?  150 VAL B HB   1 
ATOM   7675  H HG11 . VAL B 1 141 ? 6.472   7.589   76.760  1.00 137.15 ?  150 VAL B HG11 1 
ATOM   7676  H HG12 . VAL B 1 141 ? 6.369   6.860   75.352  1.00 137.15 ?  150 VAL B HG12 1 
ATOM   7677  H HG13 . VAL B 1 141 ? 6.067   8.416   75.465  1.00 137.15 ?  150 VAL B HG13 1 
ATOM   7678  H HG21 . VAL B 1 141 ? 4.515   8.255   77.924  1.00 89.21  ?  150 VAL B HG21 1 
ATOM   7679  H HG22 . VAL B 1 141 ? 4.066   9.145   76.687  1.00 89.21  ?  150 VAL B HG22 1 
ATOM   7680  H HG23 . VAL B 1 141 ? 3.073   8.059   77.286  1.00 89.21  ?  150 VAL B HG23 1 
ATOM   7681  N N    . LEU B 1 142 ? 1.992   5.678   75.412  1.00 77.67  ?  151 LEU B N    1 
ATOM   7682  C CA   . LEU B 1 142 ? 0.611   5.269   75.613  1.00 71.31  ?  151 LEU B CA   1 
ATOM   7683  C C    . LEU B 1 142 ? 0.121   5.543   77.032  1.00 95.96  ?  151 LEU B C    1 
ATOM   7684  O O    . LEU B 1 142 ? -1.080  5.784   77.220  1.00 132.95 ?  151 LEU B O    1 
ATOM   7685  C CB   . LEU B 1 142 ? 0.428   3.784   75.279  1.00 65.59  ?  151 LEU B CB   1 
ATOM   7686  C CG   . LEU B 1 142 ? 0.891   3.291   73.892  1.00 107.30 ?  151 LEU B CG   1 
ATOM   7687  C CD1  . LEU B 1 142 ? 0.809   1.755   73.723  1.00 106.34 ?  151 LEU B CD1  1 
ATOM   7688  C CD2  . LEU B 1 142 ? 0.156   3.959   72.786  1.00 70.05  ?  151 LEU B CD2  1 
ATOM   7689  H H    . LEU B 1 142 ? 2.565   5.058   75.571  1.00 93.20  ?  151 LEU B H    1 
ATOM   7690  H HA   . LEU B 1 142 ? 0.048   5.777   75.007  1.00 85.57  ?  151 LEU B HA   1 
ATOM   7691  H HB2  . LEU B 1 142 ? 0.916   3.268   75.940  1.00 78.70  ?  151 LEU B HB2  1 
ATOM   7692  H HB3  . LEU B 1 142 ? -0.517  3.577   75.351  1.00 78.70  ?  151 LEU B HB3  1 
ATOM   7693  H HG   . LEU B 1 142 ? 1.826   3.532   73.791  1.00 128.76 ?  151 LEU B HG   1 
ATOM   7694  H HD11 . LEU B 1 142 ? 1.114   1.520   72.833  1.00 127.60 ?  151 LEU B HD11 1 
ATOM   7695  H HD12 . LEU B 1 142 ? 1.374   1.334   74.389  1.00 127.60 ?  151 LEU B HD12 1 
ATOM   7696  H HD13 . LEU B 1 142 ? -0.111  1.474   73.843  1.00 127.60 ?  151 LEU B HD13 1 
ATOM   7697  H HD21 . LEU B 1 142 ? 0.481   3.616   71.939  1.00 84.06  ?  151 LEU B HD21 1 
ATOM   7698  H HD22 . LEU B 1 142 ? -0.791  3.770   72.878  1.00 84.06  ?  151 LEU B HD22 1 
ATOM   7699  H HD23 . LEU B 1 142 ? 0.309   4.915   72.838  1.00 84.06  ?  151 LEU B HD23 1 
ATOM   7700  N N    . PHE B 1 143 ? 1.022   5.569   78.024  1.00 106.84 ?  152 PHE B N    1 
ATOM   7701  C CA   . PHE B 1 143 ? 0.636   5.654   79.435  1.00 103.81 ?  152 PHE B CA   1 
ATOM   7702  C C    . PHE B 1 143 ? 1.569   6.545   80.281  1.00 123.31 ?  152 PHE B C    1 
ATOM   7703  O O    . PHE B 1 143 ? 2.726   6.801   79.932  1.00 131.85 ?  152 PHE B O    1 
ATOM   7704  C CB   . PHE B 1 143 ? 0.576   4.247   80.030  1.00 91.96  ?  152 PHE B CB   1 
ATOM   7705  C CG   . PHE B 1 143 ? -0.425  3.329   79.356  1.00 97.43  ?  152 PHE B CG   1 
ATOM   7706  C CD1  . PHE B 1 143 ? -1.786  3.452   79.599  1.00 108.47 ?  152 PHE B CD1  1 
ATOM   7707  C CD2  . PHE B 1 143 ? 0.005   2.342   78.475  1.00 105.73 ?  152 PHE B CD2  1 
ATOM   7708  C CE1  . PHE B 1 143 ? -2.690  2.609   78.995  1.00 120.56 ?  152 PHE B CE1  1 
ATOM   7709  C CE2  . PHE B 1 143 ? -0.892  1.493   77.871  1.00 121.03 ?  152 PHE B CE2  1 
ATOM   7710  C CZ   . PHE B 1 143 ? -2.247  1.627   78.134  1.00 122.72 ?  152 PHE B CZ   1 
ATOM   7711  H H    . PHE B 1 143 ? 1.872   5.539   77.901  1.00 128.21 ?  152 PHE B H    1 
ATOM   7712  H HA   . PHE B 1 143 ? -0.256  6.032   79.488  1.00 124.57 ?  152 PHE B HA   1 
ATOM   7713  H HB2  . PHE B 1 143 ? 1.452   3.837   79.951  1.00 110.36 ?  152 PHE B HB2  1 
ATOM   7714  H HB3  . PHE B 1 143 ? 0.330   4.315   80.966  1.00 110.36 ?  152 PHE B HB3  1 
ATOM   7715  H HD1  . PHE B 1 143 ? -2.089  4.106   80.187  1.00 130.16 ?  152 PHE B HD1  1 
ATOM   7716  H HD2  . PHE B 1 143 ? 0.914   2.244   78.305  1.00 126.87 ?  152 PHE B HD2  1 
ATOM   7717  H HE1  . PHE B 1 143 ? -3.599  2.700   79.169  1.00 144.68 ?  152 PHE B HE1  1 
ATOM   7718  H HE2  . PHE B 1 143 ? -0.593  0.835   77.286  1.00 145.23 ?  152 PHE B HE2  1 
ATOM   7719  H HZ   . PHE B 1 143 ? -2.859  1.062   77.719  1.00 147.27 ?  152 PHE B HZ   1 
ATOM   7720  N N    . SER B 1 144 ? 1.024   7.026   81.411  1.00 96.19  ?  153 SER B N    1 
ATOM   7721  C CA   . SER B 1 144 ? 1.702   7.893   82.379  1.00 97.23  ?  153 SER B CA   1 
ATOM   7722  C C    . SER B 1 144 ? 1.160   7.582   83.779  1.00 91.09  ?  153 SER B C    1 
ATOM   7723  O O    . SER B 1 144 ? 0.128   6.924   83.935  1.00 92.41  ?  153 SER B O    1 
ATOM   7724  C CB   . SER B 1 144 ? 1.481   9.403   82.072  1.00 101.21 ?  153 SER B CB   1 
ATOM   7725  O OG   . SER B 1 144 ? 2.007   9.806   80.807  1.00 99.00  ?  153 SER B OG   1 
ATOM   7726  H H    . SER B 1 144 ? 0.216   6.849   81.645  1.00 115.43 ?  153 SER B H    1 
ATOM   7727  H HA   . SER B 1 144 ? 2.655   7.710   82.369  1.00 116.68 ?  153 SER B HA   1 
ATOM   7728  H HB2  . SER B 1 144 ? 0.528   9.582   82.080  1.00 121.46 ?  153 SER B HB2  1 
ATOM   7729  H HB3  . SER B 1 144 ? 1.914   9.925   82.765  1.00 121.46 ?  153 SER B HB3  1 
ATOM   7730  H HG   . SER B 1 144 ? 1.865   10.625  80.684  1.00 118.80 ?  153 SER B HG   1 
ATOM   7731  N N    . PHE B 1 145 ? 1.827   8.111   84.804  1.00 101.69 ?  154 PHE B N    1 
ATOM   7732  C CA   . PHE B 1 145 ? 1.393   7.939   86.189  1.00 95.35  ?  154 PHE B CA   1 
ATOM   7733  C C    . PHE B 1 145 ? 0.649   9.138   86.751  1.00 84.91  ?  154 PHE B C    1 
ATOM   7734  O O    . PHE B 1 145 ? -0.398  8.987   87.391  1.00 82.50  ?  154 PHE B O    1 
ATOM   7735  C CB   . PHE B 1 145 ? 2.602   7.694   87.097  1.00 93.60  ?  154 PHE B CB   1 
ATOM   7736  C CG   . PHE B 1 145 ? 3.249   6.434   86.867  1.00 107.09 ?  154 PHE B CG   1 
ATOM   7737  C CD1  . PHE B 1 145 ? 2.692   5.302   87.373  1.00 74.37  ?  154 PHE B CD1  1 
ATOM   7738  C CD2  . PHE B 1 145 ? 4.402   6.349   86.128  1.00 85.70  ?  154 PHE B CD2  1 
ATOM   7739  C CE1  . PHE B 1 145 ? 3.266   4.088   87.153  1.00 59.61  ?  154 PHE B CE1  1 
ATOM   7740  C CE2  . PHE B 1 145 ? 4.972   5.153   85.920  1.00 62.77  ?  154 PHE B CE2  1 
ATOM   7741  C CZ   . PHE B 1 145 ? 4.397   4.008   86.434  1.00 76.42  ?  154 PHE B CZ   1 
ATOM   7742  H H    . PHE B 1 145 ? 2.544   8.579   84.721  1.00 122.03 ?  154 PHE B H    1 
ATOM   7743  H HA   . PHE B 1 145 ? 0.809   7.166   86.246  1.00 114.43 ?  154 PHE B HA   1 
ATOM   7744  H HB2  . PHE B 1 145 ? 3.255   8.395   86.945  1.00 112.32 ?  154 PHE B HB2  1 
ATOM   7745  H HB3  . PHE B 1 145 ? 2.308   7.713   88.021  1.00 112.32 ?  154 PHE B HB3  1 
ATOM   7746  H HD1  . PHE B 1 145 ? 1.905   5.357   87.866  1.00 89.24  ?  154 PHE B HD1  1 
ATOM   7747  H HD2  . PHE B 1 145 ? 4.788   7.119   85.776  1.00 102.84 ?  154 PHE B HD2  1 
ATOM   7748  H HE1  . PHE B 1 145 ? 2.881   3.319   87.506  1.00 71.54  ?  154 PHE B HE1  1 
ATOM   7749  H HE2  . PHE B 1 145 ? 5.755   5.094   85.421  1.00 75.32  ?  154 PHE B HE2  1 
ATOM   7750  H HZ   . PHE B 1 145 ? 4.798   3.181   86.290  1.00 91.70  ?  154 PHE B HZ   1 
ATOM   7751  N N    . ARG B 1 146 ? 1.241   10.313  86.598  1.00 71.40  ?  155 ARG B N    1 
ATOM   7752  C CA   . ARG B 1 146 ? 0.684   11.547  87.099  1.00 109.38 ?  155 ARG B CA   1 
ATOM   7753  C C    . ARG B 1 146 ? 0.889   12.604  86.029  1.00 86.50  ?  155 ARG B C    1 
ATOM   7754  O O    . ARG B 1 146 ? 1.692   12.449  85.106  1.00 84.81  ?  155 ARG B O    1 
ATOM   7755  C CB   . ARG B 1 146 ? 1.329   11.960  88.439  1.00 92.84  ?  155 ARG B CB   1 
ATOM   7756  C CG   . ARG B 1 146 ? 1.217   10.934  89.589  1.00 101.93 ?  155 ARG B CG   1 
ATOM   7757  C CD   . ARG B 1 146 ? -0.194  10.800  90.099  1.00 111.44 ?  155 ARG B CD   1 
ATOM   7758  N NE   . ARG B 1 146 ? -0.660  11.933  90.922  1.00 93.51  ?  155 ARG B NE   1 
ATOM   7759  C CZ   . ARG B 1 146 ? -0.360  12.142  92.203  1.00 109.51 ?  155 ARG B CZ   1 
ATOM   7760  N NH1  . ARG B 1 146 ? 0.435   11.310  92.852  1.00 111.64 1  155 ARG B NH1  1 
ATOM   7761  N NH2  . ARG B 1 146 ? -0.841  13.209  92.832  1.00 133.58 1  155 ARG B NH2  1 
ATOM   7762  H H    . ARG B 1 146 ? 1.992   10.419  86.192  1.00 85.68  ?  155 ARG B H    1 
ATOM   7763  H HA   . ARG B 1 146 ? -0.270  11.435  87.241  1.00 131.25 ?  155 ARG B HA   1 
ATOM   7764  H HB2  . ARG B 1 146 ? 2.273   12.121  88.286  1.00 111.40 ?  155 ARG B HB2  1 
ATOM   7765  H HB3  . ARG B 1 146 ? 0.907   12.779  88.741  1.00 111.40 ?  155 ARG B HB3  1 
ATOM   7766  H HG2  . ARG B 1 146 ? 1.506   10.065  89.268  1.00 122.32 ?  155 ARG B HG2  1 
ATOM   7767  H HG3  . ARG B 1 146 ? 1.779   11.220  90.326  1.00 122.32 ?  155 ARG B HG3  1 
ATOM   7768  H HD2  . ARG B 1 146 ? -0.792  10.724  89.339  1.00 133.72 ?  155 ARG B HD2  1 
ATOM   7769  H HD3  . ARG B 1 146 ? -0.253  9.999   90.642  1.00 133.72 ?  155 ARG B HD3  1 
ATOM   7770  H HE   . ARG B 1 146 ? -1.172  12.509  90.541  1.00 112.22 ?  155 ARG B HE   1 
ATOM   7771  H HH11 . ARG B 1 146 ? 0.753   10.619  92.451  1.00 133.97 ?  155 ARG B HH11 1 
ATOM   7772  H HH12 . ARG B 1 146 ? 0.626   11.455  93.678  1.00 133.97 ?  155 ARG B HH12 1 
ATOM   7773  H HH21 . ARG B 1 146 ? -1.356  13.758  92.416  1.00 160.30 ?  155 ARG B HH21 1 
ATOM   7774  H HH22 . ARG B 1 146 ? -0.645  13.346  93.658  1.00 160.30 ?  155 ARG B HH22 1 
ATOM   7775  N N    . ASP B 1 147 ? 0.104   13.655  86.122  1.00 120.63 ?  156 ASP B N    1 
ATOM   7776  C CA   . ASP B 1 147 ? 0.252   14.725  85.157  1.00 111.29 ?  156 ASP B CA   1 
ATOM   7777  C C    . ASP B 1 147 ? 1.579   15.409  85.402  1.00 92.13  ?  156 ASP B C    1 
ATOM   7778  O O    . ASP B 1 147 ? 1.892   15.769  86.544  1.00 78.72  ?  156 ASP B O    1 
ATOM   7779  C CB   . ASP B 1 147 ? -0.921  15.683  85.281  1.00 123.30 ?  156 ASP B CB   1 
ATOM   7780  C CG   . ASP B 1 147 ? -2.243  14.997  84.929  1.00 124.45 ?  156 ASP B CG   1 
ATOM   7781  O OD1  . ASP B 1 147 ? -2.253  14.234  83.931  1.00 96.39  ?  156 ASP B OD1  1 
ATOM   7782  O OD2  . ASP B 1 147 ? -3.248  15.178  85.652  1.00 137.94 -1 156 ASP B OD2  1 
ATOM   7783  H H    . ASP B 1 147 ? -0.507  13.776  86.716  1.00 144.75 ?  156 ASP B H    1 
ATOM   7784  H HA   . ASP B 1 147 ? 0.255   14.355  84.260  1.00 133.54 ?  156 ASP B HA   1 
ATOM   7785  H HB2  . ASP B 1 147 ? -0.978  16.002  86.195  1.00 147.96 ?  156 ASP B HB2  1 
ATOM   7786  H HB3  . ASP B 1 147 ? -0.792  16.427  84.673  1.00 147.96 ?  156 ASP B HB3  1 
ATOM   7787  N N    . GLY B 1 148 ? 2.373   15.567  84.343  1.00 87.83  ?  157 GLY B N    1 
ATOM   7788  C CA   . GLY B 1 148 ? 3.668   16.214  84.510  1.00 93.24  ?  157 GLY B CA   1 
ATOM   7789  C C    . GLY B 1 148 ? 4.713   15.376  85.232  1.00 78.88  ?  157 GLY B C    1 
ATOM   7790  O O    . GLY B 1 148 ? 5.508   15.892  86.008  1.00 81.83  ?  157 GLY B O    1 
ATOM   7791  H H    . GLY B 1 148 ? 2.190   15.316  83.541  1.00 105.40 ?  157 GLY B H    1 
ATOM   7792  H HA2  . GLY B 1 148 ? 4.020   16.443  83.635  1.00 111.88 ?  157 GLY B HA2  1 
ATOM   7793  H HA3  . GLY B 1 148 ? 3.547   17.036  85.009  1.00 111.88 ?  157 GLY B HA3  1 
ATOM   7794  N N    . ASP B 1 149 ? 4.677   14.097  85.072  1.00 98.40  ?  158 ASP B N    1 
ATOM   7795  C CA   . ASP B 1 149 ? 5.857   13.346  85.451  1.00 106.20 ?  158 ASP B CA   1 
ATOM   7796  C C    . ASP B 1 149 ? 6.923   13.339  84.340  1.00 106.16 ?  158 ASP B C    1 
ATOM   7797  O O    . ASP B 1 149 ? 7.935   12.668  84.463  1.00 79.79  ?  158 ASP B O    1 
ATOM   7798  C CB   . ASP B 1 149 ? 5.404   11.948  85.841  1.00 98.77  ?  158 ASP B CB   1 
ATOM   7799  C CG   . ASP B 1 149 ? 4.540   11.330  84.768  1.00 94.05  ?  158 ASP B CG   1 
ATOM   7800  O OD1  . ASP B 1 149 ? 4.134   12.071  83.837  1.00 120.56 ?  158 ASP B OD1  1 
ATOM   7801  O OD2  . ASP B 1 149 ? 4.184   10.158  84.880  1.00 76.17  -1 158 ASP B OD2  1 
ATOM   7802  H H    . ASP B 1 149 ? 4.019   13.639  84.761  1.00 118.08 ?  158 ASP B H    1 
ATOM   7803  H HA   . ASP B 1 149 ? 6.251   13.759  86.235  1.00 127.43 ?  158 ASP B HA   1 
ATOM   7804  H HB2  . ASP B 1 149 ? 6.182   11.383  85.968  1.00 118.53 ?  158 ASP B HB2  1 
ATOM   7805  H HB3  . ASP B 1 149 ? 4.886   11.996  86.660  1.00 118.53 ?  158 ASP B HB3  1 
ATOM   7806  N N    . CYS B 1 150 ? 6.717   14.008  83.220  1.00 157.84 ?  159 CYS B N    1 
ATOM   7807  C CA   . CYS B 1 150 ? 7.744   14.001  82.192  1.00 154.50 ?  159 CYS B CA   1 
ATOM   7808  C C    . CYS B 1 150 ? 8.001   12.602  81.658  1.00 146.15 ?  159 CYS B C    1 
ATOM   7809  O O    . CYS B 1 150 ? 9.017   12.355  81.011  1.00 153.26 ?  159 CYS B O    1 
ATOM   7810  C CB   . CYS B 1 150 ? 9.058   14.558  82.740  1.00 138.30 ?  159 CYS B CB   1 
ATOM   7811  S SG   . CYS B 1 150 ? 9.043   16.286  83.061  1.00 101.13 ?  159 CYS B SG   1 
ATOM   7812  H H    . CYS B 1 150 ? 6.012   14.463  83.031  1.00 189.41 ?  159 CYS B H    1 
ATOM   7813  H HA   . CYS B 1 150 ? 7.460   14.562  81.453  1.00 185.40 ?  159 CYS B HA   1 
ATOM   7814  H HB2  . CYS B 1 150 ? 9.262   14.105  83.574  1.00 165.96 ?  159 CYS B HB2  1 
ATOM   7815  H HB3  . CYS B 1 150 ? 9.761   14.385  82.095  1.00 165.96 ?  159 CYS B HB3  1 
ATOM   7816  H HG   . CYS B 1 150 ? 10.116  16.614  83.486  1.00 121.36 ?  159 CYS B HG   1 
ATOM   7817  N N    . SER B 1 151 ? 7.121   11.651  81.922  1.00 121.32 ?  160 SER B N    1 
ATOM   7818  C CA   . SER B 1 151 ? 7.376   10.303  81.436  1.00 115.93 ?  160 SER B CA   1 
ATOM   7819  C C    . SER B 1 151 ? 7.308   10.207  79.915  1.00 56.87  ?  160 SER B C    1 
ATOM   7820  O O    . SER B 1 151 ? 7.925   9.306   79.353  1.00 76.36  ?  160 SER B O    1 
ATOM   7821  C CB   . SER B 1 151 ? 6.431   9.301   82.082  1.00 144.60 ?  160 SER B CB   1 
ATOM   7822  O OG   . SER B 1 151 ? 5.152   9.641   81.746  1.00 55.89  ?  160 SER B OG   1 
ATOM   7823  H H    . SER B 1 151 ? 6.391   11.751  82.366  1.00 145.58 ?  160 SER B H    1 
ATOM   7824  H HA   . SER B 1 151 ? 8.276   10.055  81.697  1.00 139.12 ?  160 SER B HA   1 
ATOM   7825  H HB2  . SER B 1 151 ? 6.628   8.411   81.751  1.00 173.51 ?  160 SER B HB2  1 
ATOM   7826  H HB3  . SER B 1 151 ? 6.533   9.336   83.046  1.00 173.51 ?  160 SER B HB3  1 
ATOM   7827  H HG   . SER B 1 151 ? 4.611   9.100   82.092  1.00 67.06  ?  160 SER B HG   1 
ATOM   7828  N N    . LYS B 1 152 ? 6.561   11.044  79.207  1.00 81.23  ?  161 LYS B N    1 
ATOM   7829  C CA   . LYS B 1 152 ? 6.742   10.974  77.769  1.00 77.60  ?  161 LYS B CA   1 
ATOM   7830  C C    . LYS B 1 152 ? 8.212   11.212  77.465  1.00 87.31  ?  161 LYS B C    1 
ATOM   7831  O O    . LYS B 1 152 ? 8.870   10.401  76.811  1.00 89.73  ?  161 LYS B O    1 
ATOM   7832  C CB   . LYS B 1 152 ? 5.851   11.987  77.039  1.00 64.45  ?  161 LYS B CB   1 
ATOM   7833  H H    . LYS B 1 152 ? 5.991   11.616  79.504  1.00 97.48  ?  161 LYS B H    1 
ATOM   7834  H HA   . LYS B 1 152 ? 6.507   10.085  77.459  1.00 93.12  ?  161 LYS B HA   1 
ATOM   7835  N N    . GLY B 1 153 ? 8.785   12.238  78.085  1.00 133.58 ?  162 GLY B N    1 
ATOM   7836  C CA   . GLY B 1 153 ? 10.163  12.582  77.791  1.00 112.63 ?  162 GLY B CA   1 
ATOM   7837  C C    . GLY B 1 153 ? 11.124  11.493  78.214  1.00 93.39  ?  162 GLY B C    1 
ATOM   7838  O O    . GLY B 1 153 ? 12.036  11.125  77.465  1.00 59.13  ?  162 GLY B O    1 
ATOM   7839  H H    . GLY B 1 153 ? 8.403   12.739  78.670  1.00 160.30 ?  162 GLY B H    1 
ATOM   7840  H HA2  . GLY B 1 153 ? 10.264  12.730  76.838  1.00 135.16 ?  162 GLY B HA2  1 
ATOM   7841  H HA3  . GLY B 1 153 ? 10.400  13.400  78.257  1.00 135.16 ?  162 GLY B HA3  1 
ATOM   7842  N N    . PHE B 1 154 ? 10.978  11.003  79.436  1.00 70.22  ?  163 PHE B N    1 
ATOM   7843  C CA   . PHE B 1 154 ? 11.929  10.002  79.921  1.00 74.48  ?  163 PHE B CA   1 
ATOM   7844  C C    . PHE B 1 154 ? 11.810  8.678   79.187  1.00 67.36  ?  163 PHE B C    1 
ATOM   7845  O O    . PHE B 1 154 ? 12.807  7.982   78.983  1.00 90.47  ?  163 PHE B O    1 
ATOM   7846  C CB   . PHE B 1 154 ? 11.764  9.751   81.409  1.00 65.29  ?  163 PHE B CB   1 
ATOM   7847  C CG   . PHE B 1 154 ? 12.811  8.840   81.977  1.00 79.74  ?  163 PHE B CG   1 
ATOM   7848  C CD1  . PHE B 1 154 ? 14.116  9.214   81.993  1.00 129.83 ?  163 PHE B CD1  1 
ATOM   7849  C CD2  . PHE B 1 154 ? 12.478  7.615   82.504  1.00 60.88  ?  163 PHE B CD2  1 
ATOM   7850  C CE1  . PHE B 1 154 ? 15.062  8.385   82.525  1.00 78.72  ?  163 PHE B CE1  1 
ATOM   7851  C CE2  . PHE B 1 154 ? 13.416  6.776   83.045  1.00 70.62  ?  163 PHE B CE2  1 
ATOM   7852  C CZ   . PHE B 1 154 ? 14.715  7.150   83.056  1.00 76.95  ?  163 PHE B CZ   1 
ATOM   7853  H H    . PHE B 1 154 ? 10.359  11.221  79.992  1.00 84.26  ?  163 PHE B H    1 
ATOM   7854  H HA   . PHE B 1 154 ? 12.828  10.336  79.778  1.00 89.37  ?  163 PHE B HA   1 
ATOM   7855  H HB2  . PHE B 1 154 ? 11.819  10.598  81.879  1.00 78.35  ?  163 PHE B HB2  1 
ATOM   7856  H HB3  . PHE B 1 154 ? 10.898  9.342   81.564  1.00 78.35  ?  163 PHE B HB3  1 
ATOM   7857  H HD1  . PHE B 1 154 ? 14.366  10.039  81.645  1.00 155.80 ?  163 PHE B HD1  1 
ATOM   7858  H HD2  . PHE B 1 154 ? 11.586  7.352   82.503  1.00 73.05  ?  163 PHE B HD2  1 
ATOM   7859  H HE1  . PHE B 1 154 ? 15.953  8.650   82.529  1.00 94.46  ?  163 PHE B HE1  1 
ATOM   7860  H HE2  . PHE B 1 154 ? 13.163  5.951   83.393  1.00 84.75  ?  163 PHE B HE2  1 
ATOM   7861  H HZ   . PHE B 1 154 ? 15.365  6.589   83.413  1.00 92.34  ?  163 PHE B HZ   1 
ATOM   7862  N N    . PHE B 1 155 ? 10.606  8.277   78.843  1.00 60.45  ?  164 PHE B N    1 
ATOM   7863  C CA   . PHE B 1 155 ? 10.484  7.020   78.138  1.00 60.00  ?  164 PHE B CA   1 
ATOM   7864  C C    . PHE B 1 155 ? 10.881  7.221   76.690  1.00 76.67  ?  164 PHE B C    1 
ATOM   7865  O O    . PHE B 1 155 ? 11.738  6.499   76.168  1.00 93.16  ?  164 PHE B O    1 
ATOM   7866  C CB   . PHE B 1 155 ? 9.047   6.485   78.244  1.00 68.14  ?  164 PHE B CB   1 
ATOM   7867  C CG   . PHE B 1 155 ? 8.670   5.992   79.625  1.00 75.14  ?  164 PHE B CG   1 
ATOM   7868  C CD1  . PHE B 1 155 ? 9.643   5.521   80.516  1.00 75.56  ?  164 PHE B CD1  1 
ATOM   7869  C CD2  . PHE B 1 155 ? 7.331   5.978   80.046  1.00 64.06  ?  164 PHE B CD2  1 
ATOM   7870  C CE1  . PHE B 1 155 ? 9.288   5.067   81.791  1.00 67.11  ?  164 PHE B CE1  1 
ATOM   7871  C CE2  . PHE B 1 155 ? 6.993   5.511   81.334  1.00 47.32  ?  164 PHE B CE2  1 
ATOM   7872  C CZ   . PHE B 1 155 ? 7.967   5.079   82.196  1.00 88.78  ?  164 PHE B CZ   1 
ATOM   7873  H H    . PHE B 1 155 ? 9.870   8.693   78.998  1.00 72.54  ?  164 PHE B H    1 
ATOM   7874  H HA   . PHE B 1 155 ? 11.084  6.369   78.533  1.00 72.00  ?  164 PHE B HA   1 
ATOM   7875  H HB2  . PHE B 1 155 ? 8.431   7.195   78.006  1.00 81.77  ?  164 PHE B HB2  1 
ATOM   7876  H HB3  . PHE B 1 155 ? 8.945   5.743   77.628  1.00 81.77  ?  164 PHE B HB3  1 
ATOM   7877  H HD1  . PHE B 1 155 ? 10.537  5.521   80.261  1.00 90.67  ?  164 PHE B HD1  1 
ATOM   7878  H HD2  . PHE B 1 155 ? 6.663   6.282   79.474  1.00 76.88  ?  164 PHE B HD2  1 
ATOM   7879  H HE1  . PHE B 1 155 ? 9.947   4.766   82.373  1.00 80.53  ?  164 PHE B HE1  1 
ATOM   7880  H HE2  . PHE B 1 155 ? 6.104   5.514   81.608  1.00 56.78  ?  164 PHE B HE2  1 
ATOM   7881  H HZ   . PHE B 1 155 ? 7.737   4.766   83.041  1.00 106.54 ?  164 PHE B HZ   1 
ATOM   7882  N N    . LEU B 1 156 ? 10.361  8.276   76.066  1.00 84.94  ?  165 LEU B N    1 
ATOM   7883  C CA   . LEU B 1 156 ? 10.552  8.394   74.632  1.00 75.27  ?  165 LEU B CA   1 
ATOM   7884  C C    . LEU B 1 156 ? 12.004  8.617   74.311  1.00 77.10  ?  165 LEU B C    1 
ATOM   7885  O O    . LEU B 1 156 ? 12.499  8.109   73.305  1.00 75.34  ?  165 LEU B O    1 
ATOM   7886  C CB   . LEU B 1 156 ? 9.719   9.540   74.044  1.00 83.68  ?  165 LEU B CB   1 
ATOM   7887  C CG   . LEU B 1 156 ? 8.208   9.379   73.912  1.00 92.65  ?  165 LEU B CG   1 
ATOM   7888  C CD1  . LEU B 1 156 ? 7.612   10.654  73.361  1.00 125.61 ?  165 LEU B CD1  1 
ATOM   7889  C CD2  . LEU B 1 156 ? 7.799   8.236   73.026  1.00 81.15  ?  165 LEU B CD2  1 
ATOM   7890  H H    . LEU B 1 156 ? 9.912   8.910   76.435  1.00 101.93 ?  165 LEU B H    1 
ATOM   7891  H HA   . LEU B 1 156 ? 10.272  7.569   74.206  1.00 90.33  ?  165 LEU B HA   1 
ATOM   7892  H HB2  . LEU B 1 156 ? 9.867   10.322  74.598  1.00 100.42 ?  165 LEU B HB2  1 
ATOM   7893  H HB3  . LEU B 1 156 ? 10.058  9.720   73.153  1.00 100.42 ?  165 LEU B HB3  1 
ATOM   7894  H HG   . LEU B 1 156 ? 7.829   9.227   74.791  1.00 111.18 ?  165 LEU B HG   1 
ATOM   7895  H HD11 . LEU B 1 156 ? 6.652   10.544  73.280  1.00 150.73 ?  165 LEU B HD11 1 
ATOM   7896  H HD12 . LEU B 1 156 ? 7.812   11.384  73.968  1.00 150.73 ?  165 LEU B HD12 1 
ATOM   7897  H HD13 . LEU B 1 156 ? 8.000   10.833  72.490  1.00 150.73 ?  165 LEU B HD13 1 
ATOM   7898  H HD21 . LEU B 1 156 ? 6.831   8.196   72.989  1.00 97.38  ?  165 LEU B HD21 1 
ATOM   7899  H HD22 . LEU B 1 156 ? 8.159   8.382   72.137  1.00 97.38  ?  165 LEU B HD22 1 
ATOM   7900  H HD23 . LEU B 1 156 ? 8.151   7.411   73.394  1.00 97.38  ?  165 LEU B HD23 1 
ATOM   7901  N N    . VAL B 1 157 ? 12.705  9.385   75.137  1.00 87.45  ?  166 VAL B N    1 
ATOM   7902  C CA   . VAL B 1 157 ? 14.103  9.629   74.828  1.00 64.12  ?  166 VAL B CA   1 
ATOM   7903  C C    . VAL B 1 157 ? 14.878  8.321   74.918  1.00 52.99  ?  166 VAL B C    1 
ATOM   7904  O O    . VAL B 1 157 ? 15.516  7.925   73.934  1.00 70.49  ?  166 VAL B O    1 
ATOM   7905  C CB   . VAL B 1 157 ? 14.667  10.736  75.731  1.00 68.85  ?  166 VAL B CB   1 
ATOM   7906  C CG1  . VAL B 1 157 ? 16.220  10.849  75.575  1.00 89.77  ?  166 VAL B CG1  1 
ATOM   7907  C CG2  . VAL B 1 157 ? 14.003  12.071  75.406  1.00 99.46  ?  166 VAL B CG2  1 
ATOM   7908  H H    . VAL B 1 157 ? 12.410  9.762   75.851  1.00 104.94 ?  166 VAL B H    1 
ATOM   7909  H HA   . VAL B 1 157 ? 14.166  9.941   73.912  1.00 76.94  ?  166 VAL B HA   1 
ATOM   7910  H HB   . VAL B 1 157 ? 14.473  10.520  76.656  1.00 82.62  ?  166 VAL B HB   1 
ATOM   7911  H HG11 . VAL B 1 157 ? 16.545  11.555  76.156  1.00 107.73 ?  166 VAL B HG11 1 
ATOM   7912  H HG12 . VAL B 1 157 ? 16.624  10.003  75.823  1.00 107.73 ?  166 VAL B HG12 1 
ATOM   7913  H HG13 . VAL B 1 157 ? 16.430  11.058  74.651  1.00 107.73 ?  166 VAL B HG13 1 
ATOM   7914  H HG21 . VAL B 1 157 ? 14.371  12.756  75.985  1.00 119.35 ?  166 VAL B HG21 1 
ATOM   7915  H HG22 . VAL B 1 157 ? 14.177  12.293  74.478  1.00 119.35 ?  166 VAL B HG22 1 
ATOM   7916  H HG23 . VAL B 1 157 ? 13.047  11.992  75.553  1.00 119.35 ?  166 VAL B HG23 1 
ATOM   7917  N N    . SER B 1 158 ? 14.675  7.535   76.000  1.00 55.12  ?  167 SER B N    1 
ATOM   7918  C CA   . SER B 1 158 ? 15.248  6.165   76.039  1.00 51.27  ?  167 SER B CA   1 
ATOM   7919  C C    . SER B 1 158 ? 14.933  5.425   74.749  1.00 63.51  ?  167 SER B C    1 
ATOM   7920  O O    . SER B 1 158 ? 15.826  4.888   74.081  1.00 73.21  ?  167 SER B O    1 
ATOM   7921  C CB   . SER B 1 158 ? 14.672  5.300   77.129  1.00 46.13  ?  167 SER B CB   1 
ATOM   7922  O OG   . SER B 1 158 ? 14.779  5.822   78.417  1.00 41.53  ?  167 SER B OG   1 
ATOM   7923  H H    . SER B 1 158 ? 14.228  7.761   76.699  1.00 66.15  ?  167 SER B H    1 
ATOM   7924  H HA   . SER B 1 158 ? 16.211  6.212   76.149  1.00 61.53  ?  167 SER B HA   1 
ATOM   7925  H HB2  . SER B 1 158 ? 13.731  5.160   76.937  1.00 55.35  ?  167 SER B HB2  1 
ATOM   7926  H HB3  . SER B 1 158 ? 15.131  4.446   77.110  1.00 55.35  ?  167 SER B HB3  1 
ATOM   7927  H HG   . SER B 1 158 ? 14.377  6.558   78.464  1.00 49.83  ?  167 SER B HG   1 
ATOM   7928  N N    . LEU B 1 159 ? 13.647  5.367   74.388  1.00 57.43  ?  168 LEU B N    1 
ATOM   7929  C CA   . LEU B 1 159 ? 13.270  4.622   73.193  1.00 62.47  ?  168 LEU B CA   1 
ATOM   7930  C C    . LEU B 1 159 ? 13.995  5.167   71.975  1.00 55.97  ?  168 LEU B C    1 
ATOM   7931  O O    . LEU B 1 159 ? 14.309  4.420   71.044  1.00 54.15  ?  168 LEU B O    1 
ATOM   7932  C CB   . LEU B 1 159 ? 11.756  4.658   72.986  1.00 66.05  ?  168 LEU B CB   1 
ATOM   7933  C CG   . LEU B 1 159 ? 11.180  4.161   71.669  1.00 77.23  ?  168 LEU B CG   1 
ATOM   7934  C CD1  . LEU B 1 159 ? 11.311  2.704   71.594  1.00 92.21  ?  168 LEU B CD1  1 
ATOM   7935  C CD2  . LEU B 1 159 ? 9.767   4.574   71.559  1.00 98.36  ?  168 LEU B CD2  1 
ATOM   7936  H H    . LEU B 1 159 ? 12.994  5.739   74.807  1.00 68.91  ?  168 LEU B H    1 
ATOM   7937  H HA   . LEU B 1 159 ? 13.533  3.695   73.305  1.00 74.97  ?  168 LEU B HA   1 
ATOM   7938  H HB2  . LEU B 1 159 ? 11.350  4.124   73.687  1.00 79.27  ?  168 LEU B HB2  1 
ATOM   7939  H HB3  . LEU B 1 159 ? 11.467  5.579   73.086  1.00 79.27  ?  168 LEU B HB3  1 
ATOM   7940  H HG   . LEU B 1 159 ? 11.673  4.553   70.931  1.00 92.68  ?  168 LEU B HG   1 
ATOM   7941  H HD11 . LEU B 1 159 ? 10.941  2.397   70.752  1.00 110.65 ?  168 LEU B HD11 1 
ATOM   7942  H HD12 . LEU B 1 159 ? 12.250  2.469   71.649  1.00 110.65 ?  168 LEU B HD12 1 
ATOM   7943  H HD13 . LEU B 1 159 ? 10.826  2.305   72.334  1.00 110.65 ?  168 LEU B HD13 1 
ATOM   7944  H HD21 . LEU B 1 159 ? 9.409   4.252   70.716  1.00 118.04 ?  168 LEU B HD21 1 
ATOM   7945  H HD22 . LEU B 1 159 ? 9.268   4.192   72.298  1.00 118.04 ?  168 LEU B HD22 1 
ATOM   7946  H HD23 . LEU B 1 159 ? 9.718   5.542   71.591  1.00 118.04 ?  168 LEU B HD23 1 
ATOM   7947  N N    . LEU B 1 160 ? 14.214  6.469   71.920  1.00 68.61  ?  169 LEU B N    1 
ATOM   7948  C CA   . LEU B 1 160 ? 14.885  6.972   70.741  1.00 89.17  ?  169 LEU B CA   1 
ATOM   7949  C C    . LEU B 1 160 ? 16.339  6.532   70.757  1.00 66.81  ?  169 LEU B C    1 
ATOM   7950  O O    . LEU B 1 160 ? 16.988  6.405   69.708  1.00 79.53  ?  169 LEU B O    1 
ATOM   7951  C CB   . LEU B 1 160 ? 14.764  8.473   70.687  1.00 105.85 ?  169 LEU B CB   1 
ATOM   7952  C CG   . LEU B 1 160 ? 13.366  8.932   70.367  1.00 89.42  ?  169 LEU B CG   1 
ATOM   7953  C CD1  . LEU B 1 160 ? 13.314  10.382  70.684  1.00 80.27  ?  169 LEU B CD1  1 
ATOM   7954  C CD2  . LEU B 1 160 ? 13.000  8.681   68.951  1.00 89.10  ?  169 LEU B CD2  1 
ATOM   7955  H H    . LEU B 1 160 ? 13.998  7.051   72.515  1.00 82.34  ?  169 LEU B H    1 
ATOM   7956  H HA   . LEU B 1 160 ? 14.463  6.603   69.949  1.00 107.00 ?  169 LEU B HA   1 
ATOM   7957  H HB2  . LEU B 1 160 ? 15.011  8.841   71.549  1.00 127.02 ?  169 LEU B HB2  1 
ATOM   7958  H HB3  . LEU B 1 160 ? 15.357  8.813   69.998  1.00 127.02 ?  169 LEU B HB3  1 
ATOM   7959  H HG   . LEU B 1 160 ? 12.734  8.468   70.937  1.00 107.30 ?  169 LEU B HG   1 
ATOM   7960  H HD11 . LEU B 1 160 ? 12.424  10.715  70.490  1.00 96.33  ?  169 LEU B HD11 1 
ATOM   7961  H HD12 . LEU B 1 160 ? 13.517  10.506  71.625  1.00 96.33  ?  169 LEU B HD12 1 
ATOM   7962  H HD13 . LEU B 1 160 ? 13.969  10.847  70.140  1.00 96.33  ?  169 LEU B HD13 1 
ATOM   7963  H HD21 . LEU B 1 160 ? 12.094  8.994   68.800  1.00 106.92 ?  169 LEU B HD21 1 
ATOM   7964  H HD22 . LEU B 1 160 ? 13.616  9.160   68.376  1.00 106.92 ?  169 LEU B HD22 1 
ATOM   7965  H HD23 . LEU B 1 160 ? 13.055  7.729   68.775  1.00 106.92 ?  169 LEU B HD23 1 
ATOM   7966  N N    . VAL B 1 161 ? 16.882  6.392   71.953  1.00 62.44  ?  170 VAL B N    1 
ATOM   7967  C CA   . VAL B 1 161 ? 18.223  5.893   72.076  1.00 70.72  ?  170 VAL B CA   1 
ATOM   7968  C C    . VAL B 1 161 ? 18.311  4.439   71.659  1.00 91.52  ?  170 VAL B C    1 
ATOM   7969  O O    . VAL B 1 161 ? 19.253  4.051   70.967  1.00 50.35  ?  170 VAL B O    1 
ATOM   7970  C CB   . VAL B 1 161 ? 18.703  6.060   73.511  1.00 86.85  ?  170 VAL B CB   1 
ATOM   7971  C CG1  . VAL B 1 161 ? 19.966  5.176   73.706  1.00 65.25  ?  170 VAL B CG1  1 
ATOM   7972  C CG2  . VAL B 1 161 ? 18.944  7.534   73.793  1.00 111.56 ?  170 VAL B CG2  1 
ATOM   7973  H H    . VAL B 1 161 ? 16.496  6.578   72.699  1.00 74.93  ?  170 VAL B H    1 
ATOM   7974  H HA   . VAL B 1 161 ? 18.808  6.409   71.499  1.00 84.86  ?  170 VAL B HA   1 
ATOM   7975  H HB   . VAL B 1 161 ? 18.015  5.743   74.117  1.00 104.22 ?  170 VAL B HB   1 
ATOM   7976  H HG11 . VAL B 1 161 ? 20.282  5.274   74.618  1.00 78.30  ?  170 VAL B HG11 1 
ATOM   7977  H HG12 . VAL B 1 161 ? 19.733  4.250   73.534  1.00 78.30  ?  170 VAL B HG12 1 
ATOM   7978  H HG13 . VAL B 1 161 ? 20.653  5.466   73.086  1.00 78.30  ?  170 VAL B HG13 1 
ATOM   7979  H HG21 . VAL B 1 161 ? 19.250  7.635   74.708  1.00 133.87 ?  170 VAL B HG21 1 
ATOM   7980  H HG22 . VAL B 1 161 ? 19.619  7.867   73.180  1.00 133.87 ?  170 VAL B HG22 1 
ATOM   7981  H HG23 . VAL B 1 161 ? 18.114  8.019   73.667  1.00 133.87 ?  170 VAL B HG23 1 
ATOM   7982  N N    . GLU B 1 162 ? 17.362  3.595   72.099  1.00 89.41  ?  171 GLU B N    1 
ATOM   7983  C CA   . GLU B 1 162 ? 17.399  2.194   71.693  1.00 74.92  ?  171 GLU B CA   1 
ATOM   7984  C C    . GLU B 1 162 ? 17.310  2.082   70.175  1.00 71.27  ?  171 GLU B C    1 
ATOM   7985  O O    . GLU B 1 162 ? 18.018  1.280   69.545  1.00 76.04  ?  171 GLU B O    1 
ATOM   7986  C CB   . GLU B 1 162 ? 16.277  1.426   72.376  1.00 122.99 ?  171 GLU B CB   1 
ATOM   7987  C CG   . GLU B 1 162 ? 16.535  -0.091  72.582  1.00 101.51 ?  171 GLU B CG   1 
ATOM   7988  C CD   . GLU B 1 162 ? 16.990  -0.454  74.020  1.00 87.86  ?  171 GLU B CD   1 
ATOM   7989  O OE1  . GLU B 1 162 ? 16.956  0.443   74.887  1.00 87.12  ?  171 GLU B OE1  1 
ATOM   7990  O OE2  . GLU B 1 162 ? 17.330  -1.639  74.299  1.00 116.63 -1 171 GLU B OE2  1 
ATOM   7991  H H    . GLU B 1 162 ? 16.708  3.807   72.616  1.00 107.29 ?  171 GLU B H    1 
ATOM   7992  H HA   . GLU B 1 162 ? 18.243  1.806   71.974  1.00 89.90  ?  171 GLU B HA   1 
ATOM   7993  H HB2  . GLU B 1 162 ? 16.125  1.816   73.251  1.00 147.59 ?  171 GLU B HB2  1 
ATOM   7994  H HB3  . GLU B 1 162 ? 15.474  1.514   71.839  1.00 147.59 ?  171 GLU B HB3  1 
ATOM   7995  H HG2  . GLU B 1 162 ? 15.715  -0.576  72.398  1.00 121.82 ?  171 GLU B HG2  1 
ATOM   7996  H HG3  . GLU B 1 162 ? 17.231  -0.376  71.969  1.00 121.82 ?  171 GLU B HG3  1 
ATOM   7997  N N    . ILE B 1 163 ? 16.484  2.926   69.572  1.00 56.01  ?  172 ILE B N    1 
ATOM   7998  C CA   . ILE B 1 163 ? 16.328  2.961   68.130  1.00 51.47  ?  172 ILE B CA   1 
ATOM   7999  C C    . ILE B 1 163 ? 17.608  3.396   67.440  1.00 105.28 ?  172 ILE B C    1 
ATOM   8000  O O    . ILE B 1 163 ? 17.944  2.857   66.384  1.00 60.25  ?  172 ILE B O    1 
ATOM   8001  C CB   . ILE B 1 163 ? 15.173  3.912   67.785  1.00 75.48  ?  172 ILE B CB   1 
ATOM   8002  C CG1  . ILE B 1 163 ? 13.843  3.353   68.286  1.00 82.80  ?  172 ILE B CG1  1 
ATOM   8003  C CG2  . ILE B 1 163 ? 15.077  4.141   66.278  1.00 88.25  ?  172 ILE B CG2  1 
ATOM   8004  C CD1  . ILE B 1 163 ? 12.786  4.393   68.450  1.00 120.82 ?  172 ILE B CD1  1 
ATOM   8005  H H    . ILE B 1 163 ? 15.995  3.498   69.987  1.00 67.22  ?  172 ILE B H    1 
ATOM   8006  H HA   . ILE B 1 163 ? 16.098  2.075   67.812  1.00 61.77  ?  172 ILE B HA   1 
ATOM   8007  H HB   . ILE B 1 163 ? 15.334  4.765   68.219  1.00 90.58  ?  172 ILE B HB   1 
ATOM   8008  H HG12 . ILE B 1 163 ? 13.519  2.697   67.649  1.00 99.36  ?  172 ILE B HG12 1 
ATOM   8009  H HG13 . ILE B 1 163 ? 13.985  2.933   69.149  1.00 99.36  ?  172 ILE B HG13 1 
ATOM   8010  H HG21 . ILE B 1 163 ? 14.339  4.744   66.097  1.00 105.90 ?  172 ILE B HG21 1 
ATOM   8011  H HG22 . ILE B 1 163 ? 15.908  4.530   65.965  1.00 105.90 ?  172 ILE B HG22 1 
ATOM   8012  H HG23 . ILE B 1 163 ? 14.924  3.289   65.839  1.00 105.90 ?  172 ILE B HG23 1 
ATOM   8013  H HD11 . ILE B 1 163 ? 11.974  3.969   68.769  1.00 144.98 ?  172 ILE B HD11 1 
ATOM   8014  H HD12 . ILE B 1 163 ? 13.090  5.052   69.093  1.00 144.98 ?  172 ILE B HD12 1 
ATOM   8015  H HD13 . ILE B 1 163 ? 12.624  4.816   67.593  1.00 144.98 ?  172 ILE B HD13 1 
ATOM   8016  N N    . ALA B 1 164 ? 18.303  4.428   67.962  1.00 71.75  ?  173 ALA B N    1 
ATOM   8017  C CA   . ALA B 1 164 ? 19.574  4.852   67.332  1.00 83.24  ?  173 ALA B CA   1 
ATOM   8018  C C    . ALA B 1 164 ? 20.654  3.778   67.481  1.00 74.78  ?  173 ALA B C    1 
ATOM   8019  O O    . ALA B 1 164 ? 21.592  3.726   66.684  1.00 63.04  ?  173 ALA B O    1 
ATOM   8020  C CB   . ALA B 1 164 ? 20.092  6.179   67.902  1.00 74.58  ?  173 ALA B CB   1 
ATOM   8021  H H    . ALA B 1 164 ? 18.072  4.884   68.654  1.00 86.10  ?  173 ALA B H    1 
ATOM   8022  H HA   . ALA B 1 164 ? 19.419  4.982   66.383  1.00 99.88  ?  173 ALA B HA   1 
ATOM   8023  H HB1  . ALA B 1 164 ? 20.922  6.411   67.457  1.00 89.49  ?  173 ALA B HB1  1 
ATOM   8024  H HB2  . ALA B 1 164 ? 19.428  6.870   67.745  1.00 89.49  ?  173 ALA B HB2  1 
ATOM   8025  H HB3  . ALA B 1 164 ? 20.244  6.076   68.854  1.00 89.49  ?  173 ALA B HB3  1 
ATOM   8026  N N    . ALA B 1 165 ? 20.515  2.925   68.486  1.00 76.29  ?  174 ALA B N    1 
ATOM   8027  C CA   . ALA B 1 165 ? 21.385  1.796   68.662  1.00 60.40  ?  174 ALA B CA   1 
ATOM   8028  C C    . ALA B 1 165 ? 21.070  0.650   67.710  1.00 76.26  ?  174 ALA B C    1 
ATOM   8029  O O    . ALA B 1 165 ? 21.958  -0.140  67.383  1.00 102.05 ?  174 ALA B O    1 
ATOM   8030  C CB   . ALA B 1 165 ? 21.242  1.315   70.093  1.00 45.54  ?  174 ALA B CB   1 
ATOM   8031  H H    . ALA B 1 165 ? 19.906  2.989   69.090  1.00 91.55  ?  174 ALA B H    1 
ATOM   8032  H HA   . ALA B 1 165 ? 22.304  2.070   68.519  1.00 72.48  ?  174 ALA B HA   1 
ATOM   8033  H HB1  . ALA B 1 165 ? 21.824  0.551   70.228  1.00 54.65  ?  174 ALA B HB1  1 
ATOM   8034  H HB2  . ALA B 1 165 ? 21.493  2.033   70.694  1.00 54.65  ?  174 ALA B HB2  1 
ATOM   8035  H HB3  . ALA B 1 165 ? 20.319  1.060   70.249  1.00 54.65  ?  174 ALA B HB3  1 
ATOM   8036  N N    . ALA B 1 166 ? 19.836  0.532   67.252  1.00 63.79  ?  175 ALA B N    1 
ATOM   8037  C CA   . ALA B 1 166 ? 19.525  -0.552  66.333  1.00 76.63  ?  175 ALA B CA   1 
ATOM   8038  C C    . ALA B 1 166 ? 20.394  -0.481  65.105  1.00 72.84  ?  175 ALA B C    1 
ATOM   8039  O O    . ALA B 1 166 ? 20.726  -1.523  64.527  1.00 79.19  ?  175 ALA B O    1 
ATOM   8040  C CB   . ALA B 1 166 ? 18.048  -0.521  65.944  1.00 108.01 ?  175 ALA B CB   1 
ATOM   8041  H H    . ALA B 1 166 ? 19.176  1.049   67.448  1.00 76.55  ?  175 ALA B H    1 
ATOM   8042  H HA   . ALA B 1 166 ? 19.701  -1.398  66.774  1.00 91.95  ?  175 ALA B HA   1 
ATOM   8043  H HB1  . ALA B 1 166 ? 17.867  -1.252  65.333  1.00 129.61 ?  175 ALA B HB1  1 
ATOM   8044  H HB2  . ALA B 1 166 ? 17.509  -0.618  66.745  1.00 129.61 ?  175 ALA B HB2  1 
ATOM   8045  H HB3  . ALA B 1 166 ? 17.853  0.327   65.514  1.00 129.61 ?  175 ALA B HB3  1 
ATOM   8046  N N    . SER B 1 167 ? 20.777  0.740   64.699  1.00 64.98  ?  176 SER B N    1 
ATOM   8047  C CA   . SER B 1 167 ? 21.599  0.938   63.497  1.00 88.27  ?  176 SER B CA   1 
ATOM   8048  C C    . SER B 1 167 ? 22.931  0.202   63.580  1.00 92.57  ?  176 SER B C    1 
ATOM   8049  O O    . SER B 1 167 ? 23.562  -0.037  62.547  1.00 101.61 ?  176 SER B O    1 
ATOM   8050  C CB   . SER B 1 167 ? 21.888  2.412   63.285  1.00 96.69  ?  176 SER B CB   1 
ATOM   8051  O OG   . SER B 1 167 ? 20.689  3.129   63.315  1.00 115.87 ?  176 SER B OG   1 
ATOM   8052  H H    . SER B 1 167 ? 20.572  1.470   65.105  1.00 77.97  ?  176 SER B H    1 
ATOM   8053  H HA   . SER B 1 167 ? 21.117  0.608   62.723  1.00 105.92 ?  176 SER B HA   1 
ATOM   8054  H HB2  . SER B 1 167 ? 22.469  2.729   63.994  1.00 116.02 ?  176 SER B HB2  1 
ATOM   8055  H HB3  . SER B 1 167 ? 22.313  2.534   62.422  1.00 116.02 ?  176 SER B HB3  1 
ATOM   8056  H HG   . SER B 1 167 ? 20.841  3.947   63.199  1.00 139.04 ?  176 SER B HG   1 
ATOM   8057  N N    . ALA B 1 168 ? 23.445  -0.009  64.796  1.00 89.05  ?  177 ALA B N    1 
ATOM   8058  C CA   . ALA B 1 168 ? 24.653  -0.797  64.996  1.00 65.41  ?  177 ALA B CA   1 
ATOM   8059  C C    . ALA B 1 168 ? 24.334  -2.289  65.061  1.00 85.70  ?  177 ALA B C    1 
ATOM   8060  O O    . ALA B 1 168 ? 25.101  -3.109  64.530  1.00 90.23  ?  177 ALA B O    1 
ATOM   8061  C CB   . ALA B 1 168 ? 25.379  -0.351  66.283  1.00 42.53  ?  177 ALA B CB   1 
ATOM   8062  H H    . ALA B 1 168 ? 23.106  0.298   65.524  1.00 106.86 ?  177 ALA B H    1 
ATOM   8063  H HA   . ALA B 1 168 ? 25.253  -0.651  64.248  1.00 78.49  ?  177 ALA B HA   1 
ATOM   8064  H HB1  . ALA B 1 168 ? 26.179  -0.888  66.396  1.00 51.04  ?  177 ALA B HB1  1 
ATOM   8065  H HB2  . ALA B 1 168 ? 25.617  0.586   66.202  1.00 51.04  ?  177 ALA B HB2  1 
ATOM   8066  H HB3  . ALA B 1 168 ? 24.785  -0.477  67.040  1.00 51.04  ?  177 ALA B HB3  1 
ATOM   8067  N N    . ILE B 1 169 ? 23.197  -2.649  65.679  1.00 71.30  ?  178 ILE B N    1 
ATOM   8068  C CA   . ILE B 1 169 ? 22.823  -4.060  65.833  1.00 63.65  ?  178 ILE B CA   1 
ATOM   8069  C C    . ILE B 1 169 ? 22.881  -4.791  64.490  1.00 73.83  ?  178 ILE B C    1 
ATOM   8070  O O    . ILE B 1 169 ? 23.450  -5.880  64.377  1.00 104.64 ?  178 ILE B O    1 
ATOM   8071  C CB   . ILE B 1 169 ? 21.411  -4.180  66.445  1.00 74.89  ?  178 ILE B CB   1 
ATOM   8072  C CG1  . ILE B 1 169 ? 21.300  -3.479  67.797  1.00 74.42  ?  178 ILE B CG1  1 
ATOM   8073  C CG2  . ILE B 1 169 ? 21.054  -5.611  66.616  1.00 80.63  ?  178 ILE B CG2  1 
ATOM   8074  C CD1  . ILE B 1 169 ? 22.341  -3.975  68.859  1.00 76.15  ?  178 ILE B CD1  1 
ATOM   8075  H H    . ILE B 1 169 ? 22.629  -2.097  66.015  1.00 85.57  ?  178 ILE B H    1 
ATOM   8076  H HA   . ILE B 1 169 ? 23.450  -4.489  66.437  1.00 76.38  ?  178 ILE B HA   1 
ATOM   8077  H HB   . ILE B 1 169 ? 20.776  -3.774  65.834  1.00 89.87  ?  178 ILE B HB   1 
ATOM   8078  H HG12 . ILE B 1 169 ? 21.439  -2.528  67.668  1.00 89.31  ?  178 ILE B HG12 1 
ATOM   8079  H HG13 . ILE B 1 169 ? 20.413  -3.635  68.157  1.00 89.31  ?  178 ILE B HG13 1 
ATOM   8080  H HG21 . ILE B 1 169 ? 20.166  -5.670  67.001  1.00 96.76  ?  178 ILE B HG21 1 
ATOM   8081  H HG22 . ILE B 1 169 ? 21.070  -6.046  65.749  1.00 96.76  ?  178 ILE B HG22 1 
ATOM   8082  H HG23 . ILE B 1 169 ? 21.700  -6.028  67.208  1.00 96.76  ?  178 ILE B HG23 1 
ATOM   8083  H HD11 . ILE B 1 169 ? 22.206  -3.486  69.686  1.00 91.38  ?  178 ILE B HD11 1 
ATOM   8084  H HD12 . ILE B 1 169 ? 22.209  -4.924  69.011  1.00 91.38  ?  178 ILE B HD12 1 
ATOM   8085  H HD13 . ILE B 1 169 ? 23.236  -3.815  68.522  1.00 91.38  ?  178 ILE B HD13 1 
ATOM   8086  N N    . LYS B 1 170 ? 22.301  -4.199  63.444  1.00 71.54  ?  179 LYS B N    1 
ATOM   8087  C CA   . LYS B 1 170 ? 22.309  -4.866  62.144  1.00 66.66  ?  179 LYS B CA   1 
ATOM   8088  C C    . LYS B 1 170 ? 23.703  -5.267  61.734  1.00 69.76  ?  179 LYS B C    1 
ATOM   8089  O O    . LYS B 1 170 ? 23.871  -6.187  60.930  1.00 115.89 ?  179 LYS B O    1 
ATOM   8090  C CB   . LYS B 1 170 ? 21.647  -4.001  61.023  1.00 63.51  ?  179 LYS B CB   1 
ATOM   8091  C CG   . LYS B 1 170 ? 21.922  -2.517  61.010  1.00 74.52  ?  179 LYS B CG   1 
ATOM   8092  C CD   . LYS B 1 170 ? 20.917  -1.683  60.151  1.00 83.34  ?  179 LYS B CD   1 
ATOM   8093  C CE   . LYS B 1 170 ? 21.037  -1.959  58.640  1.00 87.51  ?  179 LYS B CE   1 
ATOM   8094  H H    . LYS B 1 170 ? 21.907  -3.435  63.459  1.00 85.84  ?  179 LYS B H    1 
ATOM   8095  H HA   . LYS B 1 170 ? 21.789  -5.681  62.221  1.00 79.99  ?  179 LYS B HA   1 
ATOM   8096  H HB2  . LYS B 1 170 ? 21.941  -4.349  60.167  1.00 76.21  ?  179 LYS B HB2  1 
ATOM   8097  H HB3  . LYS B 1 170 ? 20.685  -4.108  61.095  1.00 76.21  ?  179 LYS B HB3  1 
ATOM   8098  H HG2  . LYS B 1 170 ? 21.878  -2.185  61.921  1.00 89.43  ?  179 LYS B HG2  1 
ATOM   8099  H HG3  . LYS B 1 170 ? 22.811  -2.369  60.651  1.00 89.43  ?  179 LYS B HG3  1 
ATOM   8100  H HD2  . LYS B 1 170 ? 20.012  -1.902  60.423  1.00 100.01 ?  179 LYS B HD2  1 
ATOM   8101  H HD3  . LYS B 1 170 ? 21.086  -0.739  60.296  1.00 100.01 ?  179 LYS B HD3  1 
ATOM   8102  H HE2  . LYS B 1 170 ? 21.966  -1.872  58.375  1.00 105.01 ?  179 LYS B HE2  1 
ATOM   8103  H HE3  . LYS B 1 170 ? 20.724  -2.859  58.457  1.00 105.01 ?  179 LYS B HE3  1 
ATOM   8104  N N    . VAL B 1 171 ? 24.708  -4.587  62.266  1.00 98.87  ?  180 VAL B N    1 
ATOM   8105  C CA   . VAL B 1 171 ? 26.048  -4.732  61.740  1.00 97.80  ?  180 VAL B CA   1 
ATOM   8106  C C    . VAL B 1 171 ? 26.745  -5.934  62.333  1.00 67.83  ?  180 VAL B C    1 
ATOM   8107  O O    . VAL B 1 171 ? 27.562  -6.557  61.651  1.00 78.77  ?  180 VAL B O    1 
ATOM   8108  C CB   . VAL B 1 171 ? 26.817  -3.447  62.037  1.00 76.39  ?  180 VAL B CB   1 
ATOM   8109  C CG1  . VAL B 1 171 ? 28.193  -3.537  61.491  1.00 83.26  ?  180 VAL B CG1  1 
ATOM   8110  C CG2  . VAL B 1 171 ? 26.084  -2.264  61.435  1.00 57.39  ?  180 VAL B CG2  1 
ATOM   8111  H H    . VAL B 1 171 ? 24.638  -4.040  62.926  1.00 118.65 ?  180 VAL B H    1 
ATOM   8112  H HA   . VAL B 1 171 ? 26.005  -4.847  60.778  1.00 117.36 ?  180 VAL B HA   1 
ATOM   8113  H HB   . VAL B 1 171 ? 26.875  -3.318  62.997  1.00 91.67  ?  180 VAL B HB   1 
ATOM   8114  H HG11 . VAL B 1 171 ? 28.666  -2.713  61.689  1.00 99.91  ?  180 VAL B HG11 1 
ATOM   8115  H HG12 . VAL B 1 171 ? 28.648  -4.287  61.904  1.00 99.91  ?  180 VAL B HG12 1 
ATOM   8116  H HG13 . VAL B 1 171 ? 28.143  -3.667  60.531  1.00 99.91  ?  180 VAL B HG13 1 
ATOM   8117  H HG21 . VAL B 1 171 ? 26.580  -1.453  61.629  1.00 68.87  ?  180 VAL B HG21 1 
ATOM   8118  H HG22 . VAL B 1 171 ? 26.017  -2.389  60.476  1.00 68.87  ?  180 VAL B HG22 1 
ATOM   8119  H HG23 . VAL B 1 171 ? 25.197  -2.211  61.825  1.00 68.87  ?  180 VAL B HG23 1 
ATOM   8120  N N    . ILE B 1 172 ? 26.332  -6.339  63.539  1.00 70.34  ?  181 ILE B N    1 
ATOM   8121  C CA   . ILE B 1 172 ? 26.986  -7.447  64.233  1.00 77.23  ?  181 ILE B CA   1 
ATOM   8122  C C    . ILE B 1 172 ? 27.199  -8.654  63.344  1.00 101.44 ?  181 ILE B C    1 
ATOM   8123  O O    . ILE B 1 172 ? 28.348  -9.127  63.243  1.00 72.26  ?  181 ILE B O    1 
ATOM   8124  C CB   . ILE B 1 172 ? 26.148  -7.809  65.505  1.00 78.77  ?  181 ILE B CB   1 
ATOM   8125  C CG1  . ILE B 1 172 ? 26.430  -6.767  66.584  1.00 89.06  ?  181 ILE B CG1  1 
ATOM   8126  C CG2  . ILE B 1 172 ? 26.427  -9.200  65.971  1.00 88.15  ?  181 ILE B CG2  1 
ATOM   8127  C CD1  . ILE B 1 172 ? 25.543  -6.864  67.822  1.00 112.70 ?  181 ILE B CD1  1 
ATOM   8128  H H    . ILE B 1 172 ? 25.678  -5.988  63.973  1.00 84.41  ?  181 ILE B H    1 
ATOM   8129  H HA   . ILE B 1 172 ? 27.859  -7.150  64.534  1.00 92.68  ?  181 ILE B HA   1 
ATOM   8130  H HB   . ILE B 1 172 ? 25.208  -7.754  65.271  1.00 94.52  ?  181 ILE B HB   1 
ATOM   8131  H HG12 . ILE B 1 172 ? 27.350  -6.865  66.875  1.00 106.87 ?  181 ILE B HG12 1 
ATOM   8132  H HG13 . ILE B 1 172 ? 26.302  -5.884  66.201  1.00 106.87 ?  181 ILE B HG13 1 
ATOM   8133  H HG21 . ILE B 1 172 ? 25.890  -9.383  66.757  1.00 105.77 ?  181 ILE B HG21 1 
ATOM   8134  H HG22 . ILE B 1 172 ? 26.199  -9.821  65.262  1.00 105.77 ?  181 ILE B HG22 1 
ATOM   8135  H HG23 . ILE B 1 172 ? 27.370  -9.276  66.188  1.00 105.77 ?  181 ILE B HG23 1 
ATOM   8136  H HD11 . ILE B 1 172 ? 25.796  -6.165  68.446  1.00 135.24 ?  181 ILE B HD11 1 
ATOM   8137  H HD12 . ILE B 1 172 ? 24.617  -6.752  67.556  1.00 135.24 ?  181 ILE B HD12 1 
ATOM   8138  H HD13 . ILE B 1 172 ? 25.668  -7.734  68.231  1.00 135.24 ?  181 ILE B HD13 1 
ATOM   8139  N N    . PRO B 1 173 ? 26.201  -9.166  62.639  1.00 92.11  ?  182 PRO B N    1 
ATOM   8140  C CA   . PRO B 1 173 ? 26.433  -10.289 61.742  1.00 111.90 ?  182 PRO B CA   1 
ATOM   8141  C C    . PRO B 1 173 ? 27.573  -10.033 60.794  1.00 70.35  ?  182 PRO B C    1 
ATOM   8142  O O    . PRO B 1 173 ? 28.268  -10.978 60.413  1.00 62.91  ?  182 PRO B O    1 
ATOM   8143  C CB   . PRO B 1 173 ? 25.094  -10.401 60.985  1.00 60.16  ?  182 PRO B CB   1 
ATOM   8144  C CG   . PRO B 1 173 ? 24.129  -9.855  61.854  1.00 91.33  ?  182 PRO B CG   1 
ATOM   8145  C CD   . PRO B 1 173 ? 24.782  -8.845  62.749  1.00 79.81  ?  182 PRO B CD   1 
ATOM   8146  H HA   . PRO B 1 173 ? 26.597  -11.103 62.243  1.00 134.28 ?  182 PRO B HA   1 
ATOM   8147  H HB2  . PRO B 1 173 ? 25.141  -9.891  60.161  1.00 72.19  ?  182 PRO B HB2  1 
ATOM   8148  H HB3  . PRO B 1 173 ? 24.900  -11.334 60.801  1.00 72.19  ?  182 PRO B HB3  1 
ATOM   8149  H HG2  . PRO B 1 173 ? 23.436  -9.429  61.326  1.00 109.59 ?  182 PRO B HG2  1 
ATOM   8150  H HG3  . PRO B 1 173 ? 23.746  -10.569 62.387  1.00 109.59 ?  182 PRO B HG3  1 
ATOM   8151  H HD2  . PRO B 1 173 ? 24.612  -7.947  62.426  1.00 95.77  ?  182 PRO B HD2  1 
ATOM   8152  H HD3  . PRO B 1 173 ? 24.479  -8.958  63.664  1.00 95.77  ?  182 PRO B HD3  1 
ATOM   8153  N N    . THR B 1 174 ? 27.789  -8.782  60.387  1.00 132.96 ?  183 THR B N    1 
ATOM   8154  C CA   . THR B 1 174 ? 28.905  -8.487  59.497  1.00 137.44 ?  183 THR B CA   1 
ATOM   8155  C C    . THR B 1 174 ? 30.226  -8.644  60.239  1.00 78.46  ?  183 THR B C    1 
ATOM   8156  O O    . THR B 1 174 ? 31.202  -9.174  59.693  1.00 70.31  ?  183 THR B O    1 
ATOM   8157  C CB   . THR B 1 174 ? 28.711  -7.088  58.920  1.00 92.76  ?  183 THR B CB   1 
ATOM   8158  O OG1  . THR B 1 174 ? 27.480  -7.085  58.199  1.00 77.79  ?  183 THR B OG1  1 
ATOM   8159  C CG2  . THR B 1 174 ? 29.801  -6.702  57.972  1.00 130.11 ?  183 THR B CG2  1 
ATOM   8160  H H    . THR B 1 174 ? 27.313  -8.101  60.608  1.00 159.55 ?  183 THR B H    1 
ATOM   8161  H HA   . THR B 1 174 ? 28.898  -9.119  58.761  1.00 164.93 ?  183 THR B HA   1 
ATOM   8162  H HB   . THR B 1 174 ? 28.673  -6.437  59.638  1.00 111.31 ?  183 THR B HB   1 
ATOM   8163  H HG1  . THR B 1 174 ? 27.344  -6.325  57.867  1.00 93.35  ?  183 THR B HG1  1 
ATOM   8164  H HG21 . THR B 1 174 ? 29.641  -5.809  57.628  1.00 156.13 ?  183 THR B HG21 1 
ATOM   8165  H HG22 . THR B 1 174 ? 30.657  -6.715  58.428  1.00 156.13 ?  183 THR B HG22 1 
ATOM   8166  H HG23 . THR B 1 174 ? 29.830  -7.325  57.228  1.00 156.13 ?  183 THR B HG23 1 
ATOM   8167  N N    . VAL B 1 175 ? 30.229  -8.294  61.518  1.00 72.41  ?  184 VAL B N    1 
ATOM   8168  C CA   . VAL B 1 175 ? 31.425  -8.436  62.319  1.00 58.79  ?  184 VAL B CA   1 
ATOM   8169  C C    . VAL B 1 175 ? 31.821  -9.888  62.434  1.00 72.37  ?  184 VAL B C    1 
ATOM   8170  O O    . VAL B 1 175 ? 33.001  -10.232 62.327  1.00 91.92  ?  184 VAL B O    1 
ATOM   8171  C CB   . VAL B 1 175 ? 31.215  -7.824  63.702  1.00 84.71  ?  184 VAL B CB   1 
ATOM   8172  C CG1  . VAL B 1 175 ? 32.403  -8.167  64.562  1.00 58.67  ?  184 VAL B CG1  1 
ATOM   8173  C CG2  . VAL B 1 175 ? 31.008  -6.338  63.552  1.00 128.13 ?  184 VAL B CG2  1 
ATOM   8174  H H    . VAL B 1 175 ? 29.552  -7.974  61.942  1.00 86.89  ?  184 VAL B H    1 
ATOM   8175  H HA   . VAL B 1 175 ? 32.152  -7.960  61.888  1.00 70.55  ?  184 VAL B HA   1 
ATOM   8176  H HB   . VAL B 1 175 ? 30.421  -8.205  64.107  1.00 101.65 ?  184 VAL B HB   1 
ATOM   8177  H HG11 . VAL B 1 175 ? 32.277  -7.781  65.443  1.00 70.41  ?  184 VAL B HG11 1 
ATOM   8178  H HG12 . VAL B 1 175 ? 32.475  -9.132  64.631  1.00 70.41  ?  184 VAL B HG12 1 
ATOM   8179  H HG13 . VAL B 1 175 ? 33.204  -7.804  64.153  1.00 70.41  ?  184 VAL B HG13 1 
ATOM   8180  H HG21 . VAL B 1 175 ? 30.875  -5.948  64.430  1.00 153.76 ?  184 VAL B HG21 1 
ATOM   8181  H HG22 . VAL B 1 175 ? 31.793  -5.951  63.134  1.00 153.76 ?  184 VAL B HG22 1 
ATOM   8182  H HG23 . VAL B 1 175 ? 30.227  -6.183  62.998  1.00 153.76 ?  184 VAL B HG23 1 
ATOM   8183  N N    . PHE B 1 176 ? 30.873  -10.743 62.782  1.00 80.74  ?  185 PHE B N    1 
ATOM   8184  C CA   . PHE B 1 176 ? 31.249  -12.104 63.117  1.00 74.82  ?  185 PHE B CA   1 
ATOM   8185  C C    . PHE B 1 176 ? 31.646  -12.916 61.905  1.00 77.88  ?  185 PHE B C    1 
ATOM   8186  O O    . PHE B 1 176 ? 32.525  -13.772 62.020  1.00 63.25  ?  185 PHE B O    1 
ATOM   8187  C CB   . PHE B 1 176 ? 30.101  -12.775 63.835  1.00 63.87  ?  185 PHE B CB   1 
ATOM   8188  C CG   . PHE B 1 176 ? 29.994  -12.391 65.275  1.00 54.86  ?  185 PHE B CG   1 
ATOM   8189  C CD1  . PHE B 1 176 ? 31.111  -12.443 66.117  1.00 54.85  ?  185 PHE B CD1  1 
ATOM   8190  C CD2  . PHE B 1 176 ? 28.788  -12.016 65.816  1.00 75.05  ?  185 PHE B CD2  1 
ATOM   8191  C CE1  . PHE B 1 176 ? 31.020  -12.134 67.444  1.00 90.67  ?  185 PHE B CE1  1 
ATOM   8192  C CE2  . PHE B 1 176 ? 28.693  -11.710 67.140  1.00 83.68  ?  185 PHE B CE2  1 
ATOM   8193  C CZ   . PHE B 1 176 ? 29.813  -11.768 67.953  1.00 121.51 ?  185 PHE B CZ   1 
ATOM   8194  H H    . PHE B 1 176 ? 30.032  -10.569 62.832  1.00 96.89  ?  185 PHE B H    1 
ATOM   8195  H HA   . PHE B 1 176 ? 32.007  -12.081 63.722  1.00 89.78  ?  185 PHE B HA   1 
ATOM   8196  H HB2  . PHE B 1 176 ? 29.271  -12.528 63.399  1.00 76.65  ?  185 PHE B HB2  1 
ATOM   8197  H HB3  . PHE B 1 176 ? 30.223  -13.736 63.792  1.00 76.65  ?  185 PHE B HB3  1 
ATOM   8198  H HD1  . PHE B 1 176 ? 31.932  -12.706 65.767  1.00 65.83  ?  185 PHE B HD1  1 
ATOM   8199  H HD2  . PHE B 1 176 ? 28.029  -11.986 65.279  1.00 90.06  ?  185 PHE B HD2  1 
ATOM   8200  H HE1  . PHE B 1 176 ? 31.773  -12.168 67.990  1.00 108.80 ?  185 PHE B HE1  1 
ATOM   8201  H HE2  . PHE B 1 176 ? 27.875  -11.451 67.497  1.00 100.42 ?  185 PHE B HE2  1 
ATOM   8202  H HZ   . PHE B 1 176 ? 29.742  -11.541 68.852  1.00 145.81 ?  185 PHE B HZ   1 
ATOM   8203  N N    . LYS B 1 177 ? 31.031  -12.649 60.752  1.00 74.92  ?  186 LYS B N    1 
ATOM   8204  C CA   . LYS B 1 177 ? 31.334  -13.379 59.524  1.00 68.27  ?  186 LYS B CA   1 
ATOM   8205  C C    . LYS B 1 177 ? 32.707  -12.977 58.979  1.00 76.11  ?  186 LYS B C    1 
ATOM   8206  O O    . LYS B 1 177 ? 33.411  -13.791 58.371  1.00 80.90  ?  186 LYS B O    1 
ATOM   8207  C CB   . LYS B 1 177 ? 30.219  -13.125 58.482  1.00 69.81  ?  186 LYS B CB   1 
ATOM   8208  C CG   . LYS B 1 177 ? 30.192  -14.032 57.239  1.00 72.81  ?  186 LYS B CG   1 
ATOM   8209  C CD   . LYS B 1 177 ? 29.050  -13.630 56.285  1.00 103.57 ?  186 LYS B CD   1 
ATOM   8210  C CE   . LYS B 1 177 ? 28.886  -14.597 55.094  1.00 86.07  ?  186 LYS B CE   1 
ATOM   8211  H H    . LYS B 1 177 ? 30.429  -12.042 60.656  1.00 89.90  ?  186 LYS B H    1 
ATOM   8212  H HA   . LYS B 1 177 ? 31.354  -14.330 59.717  1.00 81.93  ?  186 LYS B HA   1 
ATOM   8213  H HB2  . LYS B 1 177 ? 29.364  -13.227 58.927  1.00 83.77  ?  186 LYS B HB2  1 
ATOM   8214  H HB3  . LYS B 1 177 ? 30.307  -12.212 58.166  1.00 83.77  ?  186 LYS B HB3  1 
ATOM   8215  H HG2  . LYS B 1 177 ? 31.032  -13.948 56.762  1.00 87.37  ?  186 LYS B HG2  1 
ATOM   8216  H HG3  . LYS B 1 177 ? 30.051  -14.951 57.515  1.00 87.37  ?  186 LYS B HG3  1 
ATOM   8217  H HD2  . LYS B 1 177 ? 28.215  -13.622 56.780  1.00 124.28 ?  186 LYS B HD2  1 
ATOM   8218  H HD3  . LYS B 1 177 ? 29.232  -12.746 55.930  1.00 124.28 ?  186 LYS B HD3  1 
ATOM   8219  H HE2  . LYS B 1 177 ? 29.681  -14.553 54.541  1.00 103.29 ?  186 LYS B HE2  1 
ATOM   8220  H HE3  . LYS B 1 177 ? 28.767  -15.498 55.433  1.00 103.29 ?  186 LYS B HE3  1 
ATOM   8221  N N    . ALA B 1 178 ? 33.088  -11.722 59.170  1.00 74.72  ?  187 ALA B N    1 
ATOM   8222  C CA   . ALA B 1 178 ? 34.368  -11.253 58.680  1.00 107.13 ?  187 ALA B CA   1 
ATOM   8223  C C    . ALA B 1 178 ? 35.529  -11.875 59.458  1.00 93.64  ?  187 ALA B C    1 
ATOM   8224  O O    . ALA B 1 178 ? 36.613  -12.084 58.896  1.00 116.39 ?  187 ALA B O    1 
ATOM   8225  C CB   . ALA B 1 178 ? 34.376  -9.736  58.749  1.00 129.09 ?  187 ALA B CB   1 
ATOM   8226  H H    . ALA B 1 178 ? 32.624  -11.125 59.580  1.00 89.67  ?  187 ALA B H    1 
ATOM   8227  H HA   . ALA B 1 178 ? 34.462  -11.510 57.749  1.00 128.56 ?  187 ALA B HA   1 
ATOM   8228  H HB1  . ALA B 1 178 ? 35.229  -9.409  58.423  1.00 154.90 ?  187 ALA B HB1  1 
ATOM   8229  H HB2  . ALA B 1 178 ? 33.656  -9.391  58.197  1.00 154.90 ?  187 ALA B HB2  1 
ATOM   8230  H HB3  . ALA B 1 178 ? 34.246  -9.461  59.671  1.00 154.90 ?  187 ALA B HB3  1 
ATOM   8231  N N    . MET B 1 179 ? 35.322  -12.173 60.746  1.00 72.07  ?  188 MET B N    1 
ATOM   8232  C CA   . MET B 1 179 ? 36.279  -12.977 61.502  1.00 70.12  ?  188 MET B CA   1 
ATOM   8233  C C    . MET B 1 179 ? 36.309  -14.383 60.913  1.00 94.22  ?  188 MET B C    1 
ATOM   8234  O O    . MET B 1 179 ? 37.372  -14.911 60.558  1.00 97.02  ?  188 MET B O    1 
ATOM   8235  C CB   . MET B 1 179 ? 35.862  -13.039 62.988  1.00 70.26  ?  188 MET B CB   1 
ATOM   8236  C CG   . MET B 1 179 ? 36.003  -11.744 63.838  1.00 86.50  ?  188 MET B CG   1 
ATOM   8237  S SD   . MET B 1 179 ? 35.286  -11.733 65.536  1.00 94.24  ?  188 MET B SD   1 
ATOM   8238  C CE   . MET B 1 179 ? 36.170  -13.085 66.292  1.00 134.00 ?  188 MET B CE   1 
ATOM   8239  H H    . MET B 1 179 ? 34.636  -11.921 61.200  1.00 86.48  ?  188 MET B H    1 
ATOM   8240  H HA   . MET B 1 179 ? 37.161  -12.578 61.442  1.00 84.14  ?  188 MET B HA   1 
ATOM   8241  H HB2  . MET B 1 179 ? 34.929  -13.301 63.026  1.00 84.31  ?  188 MET B HB2  1 
ATOM   8242  H HB3  . MET B 1 179 ? 36.400  -13.720 63.421  1.00 84.31  ?  188 MET B HB3  1 
ATOM   8243  H HG2  . MET B 1 179 ? 36.949  -11.551 63.931  1.00 103.80 ?  188 MET B HG2  1 
ATOM   8244  H HG3  . MET B 1 179 ? 35.580  -11.020 63.350  1.00 103.80 ?  188 MET B HG3  1 
ATOM   8245  H HE1  . MET B 1 179 ? 35.873  -13.182 67.211  1.00 160.79 ?  188 MET B HE1  1 
ATOM   8246  H HE2  . MET B 1 179 ? 35.985  -13.899 65.797  1.00 160.79 ?  188 MET B HE2  1 
ATOM   8247  H HE3  . MET B 1 179 ? 37.120  -12.892 66.270  1.00 160.79 ?  188 MET B HE3  1 
ATOM   8248  N N    . GLN B 1 180 ? 35.117  -14.961 60.734  1.00 110.86 ?  189 GLN B N    1 
ATOM   8249  C CA   . GLN B 1 180 ? 34.935  -16.323 60.249  1.00 145.66 ?  189 GLN B CA   1 
ATOM   8250  C C    . GLN B 1 180 ? 35.552  -16.520 58.859  1.00 70.48  ?  189 GLN B C    1 
ATOM   8251  O O    . GLN B 1 180 ? 36.067  -17.604 58.554  1.00 81.75  ?  189 GLN B O    1 
ATOM   8252  C CB   . GLN B 1 180 ? 33.422  -16.609 60.317  1.00 114.17 ?  189 GLN B CB   1 
ATOM   8253  C CG   . GLN B 1 180 ? 32.894  -17.884 59.713  1.00 141.03 ?  189 GLN B CG   1 
ATOM   8254  H H    . GLN B 1 180 ? 34.373  -14.561 60.894  1.00 133.04 ?  189 GLN B H    1 
ATOM   8255  H HA   . GLN B 1 180 ? 35.379  -16.934 60.858  1.00 174.79 ?  189 GLN B HA   1 
ATOM   8256  H HB2  . GLN B 1 180 ? 33.165  -16.617 61.252  1.00 137.01 ?  189 GLN B HB2  1 
ATOM   8257  H HB3  . GLN B 1 180 ? 32.964  -15.879 59.872  1.00 137.01 ?  189 GLN B HB3  1 
ATOM   8258  H HG2  . GLN B 1 180 ? 32.848  -17.782 58.750  1.00 169.24 ?  189 GLN B HG2  1 
ATOM   8259  H HG3  . GLN B 1 180 ? 33.491  -18.613 59.942  1.00 169.24 ?  189 GLN B HG3  1 
ATOM   8260  N N    . MET B 1 181 ? 35.515  -15.497 58.014  1.00 59.24  ?  190 MET B N    1 
ATOM   8261  C CA   . MET B 1 181 ? 36.123  -15.514 56.691  1.00 101.15 ?  190 MET B CA   1 
ATOM   8262  C C    . MET B 1 181 ? 37.484  -14.795 56.642  1.00 110.47 ?  190 MET B C    1 
ATOM   8263  O O    . MET B 1 181 ? 38.106  -14.731 55.571  1.00 89.82  ?  190 MET B O    1 
ATOM   8264  C CB   . MET B 1 181 ? 35.138  -14.893 55.685  1.00 105.32 ?  190 MET B CB   1 
ATOM   8265  C CG   . MET B 1 181 ? 33.862  -15.697 55.490  1.00 122.62 ?  190 MET B CG   1 
ATOM   8266  H H    . MET B 1 181 ? 35.126  -14.751 58.194  1.00 71.08  ?  190 MET B H    1 
ATOM   8267  H HA   . MET B 1 181 ? 36.259  -16.438 56.430  1.00 121.38 ?  190 MET B HA   1 
ATOM   8268  H HB2  . MET B 1 181 ? 34.886  -14.011 55.999  1.00 126.39 ?  190 MET B HB2  1 
ATOM   8269  H HB3  . MET B 1 181 ? 35.576  -14.821 54.823  1.00 126.39 ?  190 MET B HB3  1 
ATOM   8270  H HG2  . MET B 1 181 ? 34.089  -16.568 55.128  1.00 147.14 ?  190 MET B HG2  1 
ATOM   8271  H HG3  . MET B 1 181 ? 33.419  -15.799 56.347  1.00 147.14 ?  190 MET B HG3  1 
ATOM   8272  N N    . GLN B 1 182 ? 37.960  -14.258 57.771  1.00 102.02 ?  191 GLN B N    1 
ATOM   8273  C CA   . GLN B 1 182 ? 39.279  -13.623 57.864  1.00 89.70  ?  191 GLN B CA   1 
ATOM   8274  C C    . GLN B 1 182 ? 39.392  -12.424 56.920  1.00 64.85  ?  191 GLN B C    1 
ATOM   8275  O O    . GLN B 1 182 ? 40.412  -12.229 56.275  1.00 100.83 ?  191 GLN B O    1 
ATOM   8276  C CB   . GLN B 1 182 ? 40.398  -14.636 57.608  1.00 107.81 ?  191 GLN B CB   1 
ATOM   8277  C CG   . GLN B 1 182 ? 40.767  -15.472 58.841  1.00 99.00  ?  191 GLN B CG   1 
ATOM   8278  C CD   . GLN B 1 182 ? 41.715  -14.769 59.835  1.00 104.55 ?  191 GLN B CD   1 
ATOM   8279  O OE1  . GLN B 1 182 ? 41.997  -15.303 60.904  1.00 130.15 ?  191 GLN B OE1  1 
ATOM   8280  N NE2  . GLN B 1 182 ? 42.221  -13.592 59.481  1.00 115.69 ?  191 GLN B NE2  1 
ATOM   8281  H H    . GLN B 1 182 ? 37.526  -14.249 58.513  1.00 122.42 ?  191 GLN B H    1 
ATOM   8282  H HA   . GLN B 1 182 ? 39.393  -13.290 58.768  1.00 107.64 ?  191 GLN B HA   1 
ATOM   8283  H HB2  . GLN B 1 182 ? 40.114  -15.246 56.910  1.00 129.37 ?  191 GLN B HB2  1 
ATOM   8284  H HB3  . GLN B 1 182 ? 41.194  -14.158 57.325  1.00 129.37 ?  191 GLN B HB3  1 
ATOM   8285  H HG2  . GLN B 1 182 ? 39.953  -15.694 59.319  1.00 118.80 ?  191 GLN B HG2  1 
ATOM   8286  H HG3  . GLN B 1 182 ? 41.204  -16.285 58.544  1.00 118.80 ?  191 GLN B HG3  1 
ATOM   8287  H HE21 . GLN B 1 182 ? 42.017  -13.247 58.720  1.00 138.83 ?  191 GLN B HE21 1 
ATOM   8288  H HE22 . GLN B 1 182 ? 42.753  -13.175 60.012  1.00 138.83 ?  191 GLN B HE22 1 
ATOM   8289  N N    . GLU B 1 183 ? 38.301  -11.649 56.806  1.00 103.06 ?  192 GLU B N    1 
ATOM   8290  C CA   . GLU B 1 183 ? 38.236  -10.413 56.012  1.00 94.97  ?  192 GLU B CA   1 
ATOM   8291  C C    . GLU B 1 183 ? 38.522  -9.193  56.888  1.00 91.94  ?  192 GLU B C    1 
ATOM   8292  O O    . GLU B 1 183 ? 37.618  -8.608  57.488  1.00 92.60  ?  192 GLU B O    1 
ATOM   8293  C CB   . GLU B 1 183 ? 36.869  -10.272 55.368  1.00 106.19 ?  192 GLU B CB   1 
ATOM   8294  C CG   . GLU B 1 183 ? 36.599  -11.252 54.292  1.00 123.03 ?  192 GLU B CG   1 
ATOM   8295  C CD   . GLU B 1 183 ? 37.414  -10.982 53.061  1.00 125.88 ?  192 GLU B CD   1 
ATOM   8296  O OE1  . GLU B 1 183 ? 37.701  -9.789  52.807  1.00 142.98 ?  192 GLU B OE1  1 
ATOM   8297  O OE2  . GLU B 1 183 ? 37.725  -11.951 52.332  1.00 128.22 -1 192 GLU B OE2  1 
ATOM   8298  H H    . GLU B 1 183 ? 37.557  -11.829 57.197  1.00 123.67 ?  192 GLU B H    1 
ATOM   8299  H HA   . GLU B 1 183 ? 38.903  -10.447 55.308  1.00 113.97 ?  192 GLU B HA   1 
ATOM   8300  H HB2  . GLU B 1 183 ? 36.190  -10.389 56.051  1.00 127.42 ?  192 GLU B HB2  1 
ATOM   8301  H HB3  . GLU B 1 183 ? 36.796  -9.384  54.984  1.00 127.42 ?  192 GLU B HB3  1 
ATOM   8302  H HG2  . GLU B 1 183 ? 36.818  -12.141 54.610  1.00 147.64 ?  192 GLU B HG2  1 
ATOM   8303  H HG3  . GLU B 1 183 ? 35.661  -11.206 54.049  1.00 147.64 ?  192 GLU B HG3  1 
ATOM   8304  N N    . ARG B 1 184 ? 39.797  -8.799  56.962  1.00 98.28  ?  193 ARG B N    1 
ATOM   8305  C CA   . ARG B 1 184 ? 40.193  -7.687  57.817  1.00 76.77  ?  193 ARG B CA   1 
ATOM   8306  C C    . ARG B 1 184 ? 39.622  -6.380  57.288  1.00 106.39 ?  193 ARG B C    1 
ATOM   8307  O O    . ARG B 1 184 ? 39.254  -5.505  58.060  1.00 54.80  ?  193 ARG B O    1 
ATOM   8308  C CB   . ARG B 1 184 ? 41.734  -7.657  57.930  1.00 83.47  ?  193 ARG B CB   1 
ATOM   8309  C CG   . ARG B 1 184 ? 42.356  -6.482  58.710  1.00 79.81  ?  193 ARG B CG   1 
ATOM   8310  C CD   . ARG B 1 184 ? 42.634  -5.294  57.800  1.00 65.10  ?  193 ARG B CD   1 
ATOM   8311  N NE   . ARG B 1 184 ? 43.388  -4.259  58.490  1.00 79.86  ?  193 ARG B NE   1 
ATOM   8312  C CZ   . ARG B 1 184 ? 43.559  -3.036  57.991  1.00 77.11  ?  193 ARG B CZ   1 
ATOM   8313  N NH1  . ARG B 1 184 ? 43.027  -2.740  56.800  1.00 71.84  1  193 ARG B NH1  1 
ATOM   8314  N NH2  . ARG B 1 184 ? 44.227  -2.104  58.686  1.00 57.09  1  193 ARG B NH2  1 
ATOM   8315  H H    . ARG B 1 184 ? 40.445  -9.160  56.527  1.00 117.93 ?  193 ARG B H    1 
ATOM   8316  H HA   . ARG B 1 184 ? 39.833  -7.831  58.706  1.00 92.12  ?  193 ARG B HA   1 
ATOM   8317  H HB2  . ARG B 1 184 ? 42.021  -8.474  58.367  1.00 100.17 ?  193 ARG B HB2  1 
ATOM   8318  H HB3  . ARG B 1 184 ? 42.102  -7.630  57.032  1.00 100.17 ?  193 ARG B HB3  1 
ATOM   8319  H HG2  . ARG B 1 184 ? 41.740  -6.197  59.403  1.00 95.77  ?  193 ARG B HG2  1 
ATOM   8320  H HG3  . ARG B 1 184 ? 43.195  -6.767  59.103  1.00 95.77  ?  193 ARG B HG3  1 
ATOM   8321  H HD2  . ARG B 1 184 ? 43.152  -5.590  57.036  1.00 78.12  ?  193 ARG B HD2  1 
ATOM   8322  H HD3  . ARG B 1 184 ? 41.792  -4.912  57.507  1.00 78.12  ?  193 ARG B HD3  1 
ATOM   8323  H HE   . ARG B 1 184 ? 43.883  -4.495  59.153  1.00 95.83  ?  193 ARG B HE   1 
ATOM   8324  H HH11 . ARG B 1 184 ? 42.588  -3.337  56.365  1.00 86.20  ?  193 ARG B HH11 1 
ATOM   8325  H HH12 . ARG B 1 184 ? 43.131  -1.954  56.466  1.00 86.20  ?  193 ARG B HH12 1 
ATOM   8326  H HH21 . ARG B 1 184 ? 44.570  -2.301  59.449  1.00 68.51  ?  193 ARG B HH21 1 
ATOM   8327  H HH22 . ARG B 1 184 ? 44.343  -1.320  58.352  1.00 68.51  ?  193 ARG B HH22 1 
ATOM   8328  N N    . ASP B 1 185 ? 39.530  -6.205  55.986  1.00 79.40  ?  194 ASP B N    1 
ATOM   8329  C CA   . ASP B 1 185 ? 38.974  -4.953  55.529  1.00 97.43  ?  194 ASP B CA   1 
ATOM   8330  C C    . ASP B 1 185 ? 37.504  -4.842  55.913  1.00 98.76  ?  194 ASP B C    1 
ATOM   8331  O O    . ASP B 1 185 ? 37.058  -3.813  56.430  1.00 85.53  ?  194 ASP B O    1 
ATOM   8332  C CB   . ASP B 1 185 ? 39.148  -4.820  54.030  1.00 104.94 ?  194 ASP B CB   1 
ATOM   8333  C CG   . ASP B 1 185 ? 40.586  -4.575  53.630  1.00 77.00  ?  194 ASP B CG   1 
ATOM   8334  O OD1  . ASP B 1 185 ? 41.382  -4.124  54.485  1.00 82.12  ?  194 ASP B OD1  1 
ATOM   8335  O OD2  . ASP B 1 185 ? 40.900  -4.779  52.447  1.00 72.45  -1 194 ASP B OD2  1 
ATOM   8336  H H    . ASP B 1 185 ? 39.768  -6.762  55.376  1.00 95.27  ?  194 ASP B H    1 
ATOM   8337  H HA   . ASP B 1 185 ? 39.451  -4.222  55.953  1.00 116.92 ?  194 ASP B HA   1 
ATOM   8338  H HB2  . ASP B 1 185 ? 38.852  -5.639  53.603  1.00 125.93 ?  194 ASP B HB2  1 
ATOM   8339  H HB3  . ASP B 1 185 ? 38.617  -4.071  53.716  1.00 125.93 ?  194 ASP B HB3  1 
ATOM   8340  N N    . THR B 1 186 ? 36.722  -5.886  55.675  1.00 137.34 ?  195 THR B N    1 
ATOM   8341  C CA   . THR B 1 186 ? 35.313  -5.765  56.019  1.00 63.78  ?  195 THR B CA   1 
ATOM   8342  C C    . THR B 1 186 ? 35.135  -5.575  57.525  1.00 67.19  ?  195 THR B C    1 
ATOM   8343  O O    . THR B 1 186 ? 34.199  -4.881  58.004  1.00 68.57  ?  195 THR B O    1 
ATOM   8344  C CB   . THR B 1 186 ? 34.547  -7.008  55.586  1.00 74.45  ?  195 THR B CB   1 
ATOM   8345  O OG1  . THR B 1 186 ? 34.649  -7.186  54.163  1.00 81.37  ?  195 THR B OG1  1 
ATOM   8346  C CG2  . THR B 1 186 ? 33.057  -6.935  56.007  1.00 82.64  ?  195 THR B CG2  1 
ATOM   8347  H H    . THR B 1 186 ? 36.964  -6.637  55.335  1.00 164.81 ?  195 THR B H    1 
ATOM   8348  H HA   . THR B 1 186 ? 34.934  -4.996  55.565  1.00 76.53  ?  195 THR B HA   1 
ATOM   8349  H HB   . THR B 1 186 ? 34.938  -7.781  56.023  1.00 89.34  ?  195 THR B HB   1 
ATOM   8350  H HG1  . THR B 1 186 ? 34.225  -7.873  53.928  1.00 97.64  ?  195 THR B HG1  1 
ATOM   8351  H HG21 . THR B 1 186 ? 32.592  -7.737  55.721  1.00 99.16  ?  195 THR B HG21 1 
ATOM   8352  H HG22 . THR B 1 186 ? 32.989  -6.859  56.972  1.00 99.16  ?  195 THR B HG22 1 
ATOM   8353  H HG23 . THR B 1 186 ? 32.635  -6.163  55.599  1.00 99.16  ?  195 THR B HG23 1 
ATOM   8354  N N    . LEU B 1 187 ? 36.017  -6.197  58.295  1.00 53.97  ?  196 LEU B N    1 
ATOM   8355  C CA   . LEU B 1 187 ? 35.870  -6.118  59.735  1.00 64.27  ?  196 LEU B CA   1 
ATOM   8356  C C    . LEU B 1 187 ? 36.100  -4.702  60.223  1.00 53.79  ?  196 LEU B C    1 
ATOM   8357  O O    . LEU B 1 187 ? 35.520  -4.286  61.230  1.00 48.75  ?  196 LEU B O    1 
ATOM   8358  C CB   . LEU B 1 187 ? 36.834  -7.101  60.393  1.00 52.82  ?  196 LEU B CB   1 
ATOM   8359  C CG   . LEU B 1 187 ? 36.944  -6.932  61.915  1.00 53.48  ?  196 LEU B CG   1 
ATOM   8360  C CD1  . LEU B 1 187 ? 35.659  -7.183  62.533  1.00 50.10  ?  196 LEU B CD1  1 
ATOM   8361  C CD2  . LEU B 1 187 ? 38.016  -7.824  62.569  1.00 70.71  ?  196 LEU B CD2  1 
ATOM   8362  H H    . LEU B 1 187 ? 36.689  -6.657  58.018  1.00 64.76  ?  196 LEU B H    1 
ATOM   8363  H HA   . LEU B 1 187 ? 34.967  -6.376  59.975  1.00 77.12  ?  196 LEU B HA   1 
ATOM   8364  H HB2  . LEU B 1 187 ? 36.528  -8.005  60.216  1.00 63.39  ?  196 LEU B HB2  1 
ATOM   8365  H HB3  . LEU B 1 187 ? 37.718  -6.973  60.016  1.00 63.39  ?  196 LEU B HB3  1 
ATOM   8366  H HG   . LEU B 1 187 ? 37.181  -6.011  62.103  1.00 64.18  ?  196 LEU B HG   1 
ATOM   8367  H HD11 . LEU B 1 187 ? 35.744  -7.072  63.493  1.00 60.12  ?  196 LEU B HD11 1 
ATOM   8368  H HD12 . LEU B 1 187 ? 35.012  -6.550  62.183  1.00 60.12  ?  196 LEU B HD12 1 
ATOM   8369  H HD13 . LEU B 1 187 ? 35.381  -8.089  62.327  1.00 60.12  ?  196 LEU B HD13 1 
ATOM   8370  H HD21 . LEU B 1 187 ? 38.022  -7.660  63.525  1.00 84.85  ?  196 LEU B HD21 1 
ATOM   8371  H HD22 . LEU B 1 187 ? 37.802  -8.754  62.395  1.00 84.85  ?  196 LEU B HD22 1 
ATOM   8372  H HD23 . LEU B 1 187 ? 38.881  -7.607  62.190  1.00 84.85  ?  196 LEU B HD23 1 
ATOM   8373  N N    . LEU B 1 188 ? 37.027  -3.992  59.601  1.00 80.56  ?  197 LEU B N    1 
ATOM   8374  C CA   . LEU B 1 188 ? 37.368  -2.667  60.089  1.00 82.47  ?  197 LEU B CA   1 
ATOM   8375  C C    . LEU B 1 188 ? 36.200  -1.720  59.856  1.00 92.80  ?  197 LEU B C    1 
ATOM   8376  O O    . LEU B 1 188 ? 35.696  -1.102  60.798  1.00 47.43  ?  197 LEU B O    1 
ATOM   8377  C CB   . LEU B 1 188 ? 38.676  -2.226  59.417  1.00 147.76 ?  197 LEU B CB   1 
ATOM   8378  C CG   . LEU B 1 188 ? 39.509  -1.054  59.914  1.00 112.57 ?  197 LEU B CG   1 
ATOM   8379  C CD1  . LEU B 1 188 ? 40.945  -1.285  59.567  1.00 95.34  ?  197 LEU B CD1  1 
ATOM   8380  C CD2  . LEU B 1 188 ? 39.049  0.192   59.264  1.00 95.88  ?  197 LEU B CD2  1 
ATOM   8381  H H    . LEU B 1 188 ? 37.466  -4.248  58.907  1.00 96.67  ?  197 LEU B H    1 
ATOM   8382  H HA   . LEU B 1 188 ? 37.526  -2.715  61.045  1.00 98.96  ?  197 LEU B HA   1 
ATOM   8383  H HB2  . LEU B 1 188 ? 39.268  -2.994  59.428  1.00 177.31 ?  197 LEU B HB2  1 
ATOM   8384  H HB3  . LEU B 1 188 ? 38.460  -2.022  58.493  1.00 177.31 ?  197 LEU B HB3  1 
ATOM   8385  H HG   . LEU B 1 188 ? 39.423  -0.964  60.876  1.00 135.09 ?  197 LEU B HG   1 
ATOM   8386  H HD11 . LEU B 1 188 ? 41.471  -0.535  59.886  1.00 114.41 ?  197 LEU B HD11 1 
ATOM   8387  H HD12 . LEU B 1 188 ? 41.244  -2.104  59.992  1.00 114.41 ?  197 LEU B HD12 1 
ATOM   8388  H HD13 . LEU B 1 188 ? 41.028  -1.362  58.604  1.00 114.41 ?  197 LEU B HD13 1 
ATOM   8389  H HD21 . LEU B 1 188 ? 39.586  0.933   59.586  1.00 115.05 ?  197 LEU B HD21 1 
ATOM   8390  H HD22 . LEU B 1 188 ? 39.152  0.102   58.303  1.00 115.05 ?  197 LEU B HD22 1 
ATOM   8391  H HD23 . LEU B 1 188 ? 38.116  0.337   59.485  1.00 115.05 ?  197 LEU B HD23 1 
ATOM   8392  N N    . LYS B 1 189 ? 35.676  -1.721  58.630  1.00 59.06  ?  198 LYS B N    1 
ATOM   8393  C CA   . LYS B 1 189 ? 34.501  -0.937  58.268  1.00 60.18  ?  198 LYS B CA   1 
ATOM   8394  C C    . LYS B 1 189 ? 33.329  -1.226  59.203  1.00 67.20  ?  198 LYS B C    1 
ATOM   8395  O O    . LYS B 1 189 ? 32.603  -0.307  59.622  1.00 79.51  ?  198 LYS B O    1 
ATOM   8396  C CB   . LYS B 1 189 ? 34.090  -1.242  56.823  1.00 80.27  ?  198 LYS B CB   1 
ATOM   8397  C CG   . LYS B 1 189 ? 32.912  -0.428  56.275  1.00 94.32  ?  198 LYS B CG   1 
ATOM   8398  H H    . LYS B 1 189 ? 35.993  -2.181  57.976  1.00 70.87  ?  198 LYS B H    1 
ATOM   8399  H HA   . LYS B 1 189 ? 34.714  0.008   58.332  1.00 72.21  ?  198 LYS B HA   1 
ATOM   8400  H HB2  . LYS B 1 189 ? 34.851  -1.072  56.247  1.00 96.32  ?  198 LYS B HB2  1 
ATOM   8401  H HB3  . LYS B 1 189 ? 33.845  -2.179  56.766  1.00 96.32  ?  198 LYS B HB3  1 
ATOM   8402  H HG2  . LYS B 1 189 ? 32.101  -0.702  56.730  1.00 113.19 ?  198 LYS B HG2  1 
ATOM   8403  H HG3  . LYS B 1 189 ? 33.079  0.514   56.432  1.00 113.19 ?  198 LYS B HG3  1 
ATOM   8404  N N    . ALA B 1 190 ? 33.121  -2.506  59.533  1.00 62.24  ?  199 ALA B N    1 
ATOM   8405  C CA   . ALA B 1 190 ? 32.008  -2.847  60.394  1.00 54.71  ?  199 ALA B CA   1 
ATOM   8406  C C    . ALA B 1 190 ? 32.146  -2.152  61.727  1.00 54.37  ?  199 ALA B C    1 
ATOM   8407  O O    . ALA B 1 190 ? 31.258  -1.417  62.142  1.00 71.98  ?  199 ALA B O    1 
ATOM   8408  C CB   . ALA B 1 190 ? 31.950  -4.350  60.587  1.00 58.07  ?  199 ALA B CB   1 
ATOM   8409  H H    . ALA B 1 190 ? 33.601  -3.172  59.275  1.00 74.69  ?  199 ALA B H    1 
ATOM   8410  H HA   . ALA B 1 190 ? 31.179  -2.558  59.981  1.00 65.65  ?  199 ALA B HA   1 
ATOM   8411  H HB1  . ALA B 1 190 ? 31.201  -4.565  61.165  1.00 69.68  ?  199 ALA B HB1  1 
ATOM   8412  H HB2  . ALA B 1 190 ? 31.834  -4.775  59.723  1.00 69.68  ?  199 ALA B HB2  1 
ATOM   8413  H HB3  . ALA B 1 190 ? 32.779  -4.648  60.994  1.00 69.68  ?  199 ALA B HB3  1 
ATOM   8414  N N    . LEU B 1 191 ? 33.289  -2.301  62.378  1.00 85.95  ?  200 LEU B N    1 
ATOM   8415  C CA   . LEU B 1 191 ? 33.467  -1.628  63.655  1.00 84.37  ?  200 LEU B CA   1 
ATOM   8416  C C    . LEU B 1 191 ? 33.306  -0.109  63.562  1.00 105.84 ?  200 LEU B C    1 
ATOM   8417  O O    . LEU B 1 191 ? 32.850  0.497   64.530  1.00 100.26 ?  200 LEU B O    1 
ATOM   8418  C CB   . LEU B 1 191 ? 34.830  -1.950  64.186  1.00 88.36  ?  200 LEU B CB   1 
ATOM   8419  C CG   . LEU B 1 191 ? 35.029  -3.392  64.586  1.00 81.62  ?  200 LEU B CG   1 
ATOM   8420  C CD1  . LEU B 1 191 ? 36.505  -3.710  64.684  1.00 82.21  ?  200 LEU B CD1  1 
ATOM   8421  C CD2  . LEU B 1 191 ? 34.447  -3.601  65.946  1.00 59.79  ?  200 LEU B CD2  1 
ATOM   8422  H H    . LEU B 1 191 ? 33.959  -2.770  62.113  1.00 103.14 ?  200 LEU B H    1 
ATOM   8423  H HA   . LEU B 1 191 ? 32.810  -1.963  64.285  1.00 101.24 ?  200 LEU B HA   1 
ATOM   8424  H HB2  . LEU B 1 191 ? 35.485  -1.742  63.502  1.00 106.03 ?  200 LEU B HB2  1 
ATOM   8425  H HB3  . LEU B 1 191 ? 34.993  -1.402  64.970  1.00 106.03 ?  200 LEU B HB3  1 
ATOM   8426  H HG   . LEU B 1 191 ? 34.605  -3.990  63.951  1.00 97.94  ?  200 LEU B HG   1 
ATOM   8427  H HD11 . LEU B 1 191 ? 36.611  -4.639  64.942  1.00 98.65  ?  200 LEU B HD11 1 
ATOM   8428  H HD12 . LEU B 1 191 ? 36.918  -3.556  63.820  1.00 98.65  ?  200 LEU B HD12 1 
ATOM   8429  H HD13 . LEU B 1 191 ? 36.908  -3.133  65.352  1.00 98.65  ?  200 LEU B HD13 1 
ATOM   8430  H HD21 . LEU B 1 191 ? 34.574  -4.527  66.205  1.00 71.74  ?  200 LEU B HD21 1 
ATOM   8431  H HD22 . LEU B 1 191 ? 34.897  -3.016  66.575  1.00 71.74  ?  200 LEU B HD22 1 
ATOM   8432  H HD23 . LEU B 1 191 ? 33.500  -3.391  65.919  1.00 71.74  ?  200 LEU B HD23 1 
ATOM   8433  N N    . LEU B 1 192 ? 33.663  0.526   62.425  1.00 74.26  ?  201 LEU B N    1 
ATOM   8434  C CA   . LEU B 1 192 ? 33.526  1.975   62.309  1.00 68.20  ?  201 LEU B CA   1 
ATOM   8435  C C    . LEU B 1 192 ? 32.086  2.387   62.131  1.00 130.64 ?  201 LEU B C    1 
ATOM   8436  O O    . LEU B 1 192 ? 31.684  3.447   62.607  1.00 86.29  ?  201 LEU B O    1 
ATOM   8437  C CB   . LEU B 1 192 ? 34.313  2.546   61.129  1.00 74.03  ?  201 LEU B CB   1 
ATOM   8438  C CG   . LEU B 1 192 ? 35.831  2.587   61.160  1.00 72.46  ?  201 LEU B CG   1 
ATOM   8439  C CD1  . LEU B 1 192 ? 36.332  3.261   59.932  1.00 104.12 ?  201 LEU B CD1  1 
ATOM   8440  C CD2  . LEU B 1 192 ? 36.299  3.287   62.377  1.00 57.93  ?  201 LEU B CD2  1 
ATOM   8441  H H    . LEU B 1 192 ? 33.981  0.140   61.725  1.00 89.11  ?  201 LEU B H    1 
ATOM   8442  H HA   . LEU B 1 192 ? 33.859  2.390   63.120  1.00 81.84  ?  201 LEU B HA   1 
ATOM   8443  H HB2  . LEU B 1 192 ? 34.070  2.031   60.344  1.00 88.84  ?  201 LEU B HB2  1 
ATOM   8444  H HB3  . LEU B 1 192 ? 34.018  3.462   61.001  1.00 88.84  ?  201 LEU B HB3  1 
ATOM   8445  H HG   . LEU B 1 192 ? 36.177  1.681   61.176  1.00 86.96  ?  201 LEU B HG   1 
ATOM   8446  H HD11 . LEU B 1 192 ? 37.302  3.284   59.958  1.00 124.95 ?  201 LEU B HD11 1 
ATOM   8447  H HD12 . LEU B 1 192 ? 36.034  2.762   59.155  1.00 124.95 ?  201 LEU B HD12 1 
ATOM   8448  H HD13 . LEU B 1 192 ? 35.980  4.164   59.901  1.00 124.95 ?  201 LEU B HD13 1 
ATOM   8449  H HD21 . LEU B 1 192 ? 37.269  3.302   62.378  1.00 69.52  ?  201 LEU B HD21 1 
ATOM   8450  H HD22 . LEU B 1 192 ? 35.953  4.193   62.372  1.00 69.52  ?  201 LEU B HD22 1 
ATOM   8451  H HD23 . LEU B 1 192 ? 35.974  2.812   63.158  1.00 69.52  ?  201 LEU B HD23 1 
ATOM   8452  N N    . GLU B 1 193 ? 31.318  1.605   61.384  1.00 193.39 ?  202 GLU B N    1 
ATOM   8453  C CA   . GLU B 1 193 ? 29.897  1.890   61.257  1.00 103.64 ?  202 GLU B CA   1 
ATOM   8454  C C    . GLU B 1 193 ? 29.214  1.810   62.617  1.00 72.19  ?  202 GLU B C    1 
ATOM   8455  O O    . GLU B 1 193 ? 28.360  2.636   62.959  1.00 98.06  ?  202 GLU B O    1 
ATOM   8456  C CB   . GLU B 1 193 ? 29.281  0.899   60.274  1.00 128.56 ?  202 GLU B CB   1 
ATOM   8457  C CG   . GLU B 1 193 ? 27.762  0.868   60.225  1.00 147.95 ?  202 GLU B CG   1 
ATOM   8458  C CD   . GLU B 1 193 ? 27.146  2.127   59.639  1.00 154.27 ?  202 GLU B CD   1 
ATOM   8459  O OE1  . GLU B 1 193 ? 27.837  2.837   58.879  1.00 168.51 ?  202 GLU B OE1  1 
ATOM   8460  O OE2  . GLU B 1 193 ? 25.964  2.396   59.939  1.00 132.91 -1 202 GLU B OE2  1 
ATOM   8461  H H    . GLU B 1 193 ? 31.590  0.916   60.948  1.00 232.07 ?  202 GLU B H    1 
ATOM   8462  H HA   . GLU B 1 193 ? 29.777  2.786   60.905  1.00 124.37 ?  202 GLU B HA   1 
ATOM   8463  H HB2  . GLU B 1 193 ? 29.595  1.119   59.383  1.00 154.27 ?  202 GLU B HB2  1 
ATOM   8464  H HB3  . GLU B 1 193 ? 29.581  0.008   60.511  1.00 154.27 ?  202 GLU B HB3  1 
ATOM   8465  H HG2  . GLU B 1 193 ? 27.482  0.118   59.678  1.00 177.54 ?  202 GLU B HG2  1 
ATOM   8466  H HG3  . GLU B 1 193 ? 27.422  0.763   61.127  1.00 177.54 ?  202 GLU B HG3  1 
ATOM   8467  N N    . ILE B 1 194 ? 29.589  0.821   63.408  1.00 72.16  ?  203 ILE B N    1 
ATOM   8468  C CA   . ILE B 1 194 ? 29.050  0.675   64.750  1.00 53.57  ?  203 ILE B CA   1 
ATOM   8469  C C    . ILE B 1 194 ? 29.467  1.848   65.607  1.00 69.12  ?  203 ILE B C    1 
ATOM   8470  O O    . ILE B 1 194 ? 28.669  2.364   66.389  1.00 96.65  ?  203 ILE B O    1 
ATOM   8471  C CB   . ILE B 1 194 ? 29.497  -0.675  65.362  1.00 40.21  ?  203 ILE B CB   1 
ATOM   8472  C CG1  . ILE B 1 194 ? 28.669  -1.827  64.772  1.00 93.98  ?  203 ILE B CG1  1 
ATOM   8473  C CG2  . ILE B 1 194 ? 29.437  -0.696  66.872  1.00 38.13  ?  203 ILE B CG2  1 
ATOM   8474  C CD1  . ILE B 1 194 ? 29.135  -3.174  65.183  1.00 101.66 ?  203 ILE B CD1  1 
ATOM   8475  H H    . ILE B 1 194 ? 30.159  0.214   63.191  1.00 86.60  ?  203 ILE B H    1 
ATOM   8476  H HA   . ILE B 1 194 ? 28.082  0.673   64.700  1.00 64.29  ?  203 ILE B HA   1 
ATOM   8477  H HB   . ILE B 1 194 ? 30.422  -0.819  65.106  1.00 48.25  ?  203 ILE B HB   1 
ATOM   8478  H HG12 . ILE B 1 194 ? 27.749  -1.731  65.063  1.00 112.78 ?  203 ILE B HG12 1 
ATOM   8479  H HG13 . ILE B 1 194 ? 28.714  -1.781  63.804  1.00 112.78 ?  203 ILE B HG13 1 
ATOM   8480  H HG21 . ILE B 1 194 ? 29.728  -1.565  67.188  1.00 45.76  ?  203 ILE B HG21 1 
ATOM   8481  H HG22 . ILE B 1 194 ? 30.021  -0.004  67.221  1.00 45.76  ?  203 ILE B HG22 1 
ATOM   8482  H HG23 . ILE B 1 194 ? 28.523  -0.530  67.154  1.00 45.76  ?  203 ILE B HG23 1 
ATOM   8483  H HD11 . ILE B 1 194 ? 28.565  -3.843  64.772  1.00 121.99 ?  203 ILE B HD11 1 
ATOM   8484  H HD12 . ILE B 1 194 ? 30.051  -3.294  64.889  1.00 121.99 ?  203 ILE B HD12 1 
ATOM   8485  H HD13 . ILE B 1 194 ? 29.085  -3.244  66.149  1.00 121.99 ?  203 ILE B HD13 1 
ATOM   8486  N N    . ALA B 1 195 ? 30.721  2.279   65.503  1.00 84.76  ?  204 ALA B N    1 
ATOM   8487  C CA   . ALA B 1 195 ? 31.155  3.356   66.377  1.00 97.07  ?  204 ALA B CA   1 
ATOM   8488  C C    . ALA B 1 195 ? 30.345  4.610   66.105  1.00 102.45 ?  204 ALA B C    1 
ATOM   8489  O O    . ALA B 1 195 ? 29.892  5.282   67.034  1.00 57.87  ?  204 ALA B O    1 
ATOM   8490  C CB   . ALA B 1 195 ? 32.655  3.621   66.193  1.00 76.71  ?  204 ALA B CB   1 
ATOM   8491  H H    . ALA B 1 195 ? 31.315  1.978   64.959  1.00 101.72 ?  204 ALA B H    1 
ATOM   8492  H HA   . ALA B 1 195 ? 31.006  3.096   67.300  1.00 116.48 ?  204 ALA B HA   1 
ATOM   8493  H HB1  . ALA B 1 195 ? 32.923  4.341   66.784  1.00 92.05  ?  204 ALA B HB1  1 
ATOM   8494  H HB2  . ALA B 1 195 ? 33.146  2.813   66.411  1.00 92.05  ?  204 ALA B HB2  1 
ATOM   8495  H HB3  . ALA B 1 195 ? 32.820  3.870   65.270  1.00 92.05  ?  204 ALA B HB3  1 
ATOM   8496  N N    . SER B 1 196 ? 30.058  4.883   64.842  1.00 63.13  ?  205 SER B N    1 
ATOM   8497  C CA   . SER B 1 196 ? 29.316  6.077   64.530  1.00 56.99  ?  205 SER B CA   1 
ATOM   8498  C C    . SER B 1 196 ? 27.914  6.000   65.092  1.00 104.11 ?  205 SER B C    1 
ATOM   8499  O O    . SER B 1 196 ? 27.388  6.985   65.629  1.00 78.20  ?  205 SER B O    1 
ATOM   8500  C CB   . SER B 1 196 ? 29.276  6.272   63.028  1.00 69.09  ?  205 SER B CB   1 
ATOM   8501  O OG   . SER B 1 196 ? 28.536  7.441   62.733  1.00 111.75 ?  205 SER B OG   1 
ATOM   8502  H H    . SER B 1 196 ? 30.278  4.401   64.165  1.00 75.76  ?  205 SER B H    1 
ATOM   8503  H HA   . SER B 1 196 ? 29.761  6.843   64.926  1.00 68.39  ?  205 SER B HA   1 
ATOM   8504  H HB2  . SER B 1 196 ? 30.181  6.372   62.693  1.00 82.90  ?  205 SER B HB2  1 
ATOM   8505  H HB3  . SER B 1 196 ? 28.846  5.507   62.616  1.00 82.90  ?  205 SER B HB3  1 
ATOM   8506  H HG   . SER B 1 196 ? 28.507  7.561   61.903  1.00 134.10 ?  205 SER B HG   1 
ATOM   8507  N N    . CYS B 1 197 ? 27.308  4.821   64.986  1.00 83.62  ?  206 CYS B N    1 
ATOM   8508  C CA   . CYS B 1 197 ? 25.927  4.629   65.408  1.00 81.62  ?  206 CYS B CA   1 
ATOM   8509  C C    . CYS B 1 197 ? 25.812  4.843   66.895  1.00 70.05  ?  206 CYS B C    1 
ATOM   8510  O O    . CYS B 1 197 ? 24.843  5.426   67.370  1.00 70.42  ?  206 CYS B O    1 
ATOM   8511  C CB   . CYS B 1 197 ? 25.467  3.235   64.983  1.00 68.35  ?  206 CYS B CB   1 
ATOM   8512  S SG   . CYS B 1 197 ? 25.293  3.109   63.126  1.00 85.65  ?  206 CYS B SG   1 
ATOM   8513  H H    . CYS B 1 197 ? 27.679  4.112   64.671  1.00 100.34 ?  206 CYS B H    1 
ATOM   8514  H HA   . CYS B 1 197 ? 25.364  5.283   64.964  1.00 97.94  ?  206 CYS B HA   1 
ATOM   8515  H HB2  . CYS B 1 197 ? 26.121  2.579   65.272  1.00 82.02  ?  206 CYS B HB2  1 
ATOM   8516  H HB3  . CYS B 1 197 ? 24.603  3.047   65.382  1.00 82.02  ?  206 CYS B HB3  1 
ATOM   8517  H HG   . CYS B 1 197 ? 26.356  3.335   62.618  1.00 102.78 ?  206 CYS B HG   1 
ATOM   8518  N N    . LEU B 1 198 ? 26.851  4.494   67.614  1.00 77.86  ?  207 LEU B N    1 
ATOM   8519  C CA   . LEU B 1 198 ? 26.952  4.795   69.024  1.00 69.58  ?  207 LEU B CA   1 
ATOM   8520  C C    . LEU B 1 198 ? 27.307  6.234   69.238  1.00 65.24  ?  207 LEU B C    1 
ATOM   8521  O O    . LEU B 1 198 ? 27.038  6.765   70.313  1.00 65.35  ?  207 LEU B O    1 
ATOM   8522  C CB   . LEU B 1 198 ? 28.054  3.955   69.657  1.00 82.79  ?  207 LEU B CB   1 
ATOM   8523  C CG   . LEU B 1 198 ? 27.825  2.450   69.675  1.00 93.16  ?  207 LEU B CG   1 
ATOM   8524  C CD1  . LEU B 1 198 ? 29.080  1.713   69.976  1.00 120.85 ?  207 LEU B CD1  1 
ATOM   8525  C CD2  . LEU B 1 198 ? 26.811  2.157   70.744  1.00 52.45  ?  207 LEU B CD2  1 
ATOM   8526  H H    . LEU B 1 198 ? 27.531  4.070   67.302  1.00 93.43  ?  207 LEU B H    1 
ATOM   8527  H HA   . LEU B 1 198 ? 26.111  4.605   69.469  1.00 83.50  ?  207 LEU B HA   1 
ATOM   8528  H HB2  . LEU B 1 198 ? 28.877  4.116   69.170  1.00 99.34  ?  207 LEU B HB2  1 
ATOM   8529  H HB3  . LEU B 1 198 ? 28.164  4.241   70.577  1.00 99.34  ?  207 LEU B HB3  1 
ATOM   8530  H HG   . LEU B 1 198 ? 27.478  2.154   68.819  1.00 111.80 ?  207 LEU B HG   1 
ATOM   8531  H HD11 . LEU B 1 198 ? 28.895  0.761   69.979  1.00 145.02 ?  207 LEU B HD11 1 
ATOM   8532  H HD12 . LEU B 1 198 ? 29.739  1.920   69.294  1.00 145.02 ?  207 LEU B HD12 1 
ATOM   8533  H HD13 . LEU B 1 198 ? 29.407  1.989   70.847  1.00 145.02 ?  207 LEU B HD13 1 
ATOM   8534  H HD21 . LEU B 1 198 ? 26.650  1.201   70.772  1.00 62.93  ?  207 LEU B HD21 1 
ATOM   8535  H HD22 . LEU B 1 198 ? 27.156  2.460   71.598  1.00 62.93  ?  207 LEU B HD22 1 
ATOM   8536  H HD23 . LEU B 1 198 ? 25.988  2.626   70.534  1.00 62.93  ?  207 LEU B HD23 1 
ATOM   8537  N N    . GLU B 1 199 ? 27.984  6.868   68.282  1.00 73.45  ?  208 GLU B N    1 
ATOM   8538  C CA   . GLU B 1 199 ? 28.155  8.296   68.442  1.00 70.80  ?  208 GLU B CA   1 
ATOM   8539  C C    . GLU B 1 199 ? 26.831  8.998   68.155  1.00 69.86  ?  208 GLU B C    1 
ATOM   8540  O O    . GLU B 1 199 ? 26.397  9.835   68.947  1.00 67.85  ?  208 GLU B O    1 
ATOM   8541  C CB   . GLU B 1 199 ? 29.309  8.796   67.566  1.00 71.20  ?  208 GLU B CB   1 
ATOM   8542  C CG   . GLU B 1 199 ? 30.653  8.651   68.253  1.00 113.01 ?  208 GLU B CG   1 
ATOM   8543  H H    . GLU B 1 199 ? 28.331  6.516   67.578  1.00 88.14  ?  208 GLU B H    1 
ATOM   8544  H HA   . GLU B 1 199 ? 28.388  8.478   69.365  1.00 84.96  ?  208 GLU B HA   1 
ATOM   8545  H HB2  . GLU B 1 199 ? 29.332  8.280   66.745  1.00 85.44  ?  208 GLU B HB2  1 
ATOM   8546  H HB3  . GLU B 1 199 ? 29.172  9.736   67.366  1.00 85.44  ?  208 GLU B HB3  1 
ATOM   8547  H HG2  . GLU B 1 199 ? 30.626  9.120   69.102  1.00 135.61 ?  208 GLU B HG2  1 
ATOM   8548  H HG3  . GLU B 1 199 ? 30.832  7.709   68.401  1.00 135.61 ?  208 GLU B HG3  1 
ATOM   8549  N N    . LYS B 1 200 ? 26.116  8.555   67.113  1.00 77.67  ?  209 LYS B N    1 
ATOM   8550  C CA   . LYS B 1 200 ? 24.812  9.120   66.797  1.00 84.49  ?  209 LYS B CA   1 
ATOM   8551  C C    . LYS B 1 200 ? 23.857  8.926   67.961  1.00 91.32  ?  209 LYS B C    1 
ATOM   8552  O O    . LYS B 1 200 ? 23.068  9.817   68.294  1.00 115.11 ?  209 LYS B O    1 
ATOM   8553  C CB   . LYS B 1 200 ? 24.254  8.480   65.519  1.00 61.64  ?  209 LYS B CB   1 
ATOM   8554  C CG   . LYS B 1 200 ? 24.763  9.145   64.207  1.00 74.38  ?  209 LYS B CG   1 
ATOM   8555  H H    . LYS B 1 200 ? 26.369  7.930   66.579  1.00 93.20  ?  209 LYS B H    1 
ATOM   8556  H HA   . LYS B 1 200 ? 24.907  10.072  66.640  1.00 101.38 ?  209 LYS B HA   1 
ATOM   8557  H HB2  . LYS B 1 200 ? 24.514  7.546   65.498  1.00 73.96  ?  209 LYS B HB2  1 
ATOM   8558  H HB3  . LYS B 1 200 ? 23.286  8.551   65.531  1.00 73.96  ?  209 LYS B HB3  1 
ATOM   8559  H HG2  . LYS B 1 200 ? 24.431  8.640   63.448  1.00 89.26  ?  209 LYS B HG2  1 
ATOM   8560  H HG3  . LYS B 1 200 ? 24.436  10.057  64.167  1.00 89.26  ?  209 LYS B HG3  1 
ATOM   8561  N N    . ALA B 1 201 ? 23.883  7.752   68.573  1.00 77.43  ?  210 ALA B N    1 
ATOM   8562  C CA   . ALA B 1 201 ? 22.998  7.513   69.709  1.00 70.49  ?  210 ALA B CA   1 
ATOM   8563  C C    . ALA B 1 201 ? 23.363  8.376   70.897  1.00 67.04  ?  210 ALA B C    1 
ATOM   8564  O O    . ALA B 1 201 ? 22.540  8.579   71.785  1.00 82.10  ?  210 ALA B O    1 
ATOM   8565  C CB   . ALA B 1 201 ? 23.029  6.058   70.133  1.00 72.68  ?  210 ALA B CB   1 
ATOM   8566  H H    . ALA B 1 201 ? 24.389  7.091   68.360  1.00 92.91  ?  210 ALA B H    1 
ATOM   8567  H HA   . ALA B 1 201 ? 22.089  7.730   69.451  1.00 84.59  ?  210 ALA B HA   1 
ATOM   8568  H HB1  . ALA B 1 201 ? 22.432  5.936   70.887  1.00 87.22  ?  210 ALA B HB1  1 
ATOM   8569  H HB2  . ALA B 1 201 ? 22.740  5.507   69.389  1.00 87.22  ?  210 ALA B HB2  1 
ATOM   8570  H HB3  . ALA B 1 201 ? 23.936  5.823   70.387  1.00 87.22  ?  210 ALA B HB3  1 
ATOM   8571  N N    . LEU B 1 202 ? 24.603  8.818   70.990  1.00 78.66  ?  211 LEU B N    1 
ATOM   8572  C CA   . LEU B 1 202 ? 24.924  9.706   72.088  1.00 99.15  ?  211 LEU B CA   1 
ATOM   8573  C C    . LEU B 1 202 ? 24.218  11.041  71.932  1.00 94.75  ?  211 LEU B C    1 
ATOM   8574  O O    . LEU B 1 202 ? 23.699  11.581  72.907  1.00 66.55  ?  211 LEU B O    1 
ATOM   8575  C CB   . LEU B 1 202 ? 26.425  9.895   72.173  1.00 75.42  ?  211 LEU B CB   1 
ATOM   8576  C CG   . LEU B 1 202 ? 26.827  10.998  73.146  1.00 83.75  ?  211 LEU B CG   1 
ATOM   8577  C CD1  . LEU B 1 202 ? 26.351  10.755  74.569  1.00 102.44 ?  211 LEU B CD1  1 
ATOM   8578  C CD2  . LEU B 1 202 ? 28.291  11.170  73.067  1.00 52.54  ?  211 LEU B CD2  1 
ATOM   8579  H H    . LEU B 1 202 ? 25.251  8.630   70.456  1.00 94.39  ?  211 LEU B H    1 
ATOM   8580  H HA   . LEU B 1 202 ? 24.625  9.303   72.918  1.00 118.98 ?  211 LEU B HA   1 
ATOM   8581  H HB2  . LEU B 1 202 ? 26.831  9.067   72.474  1.00 90.51  ?  211 LEU B HB2  1 
ATOM   8582  H HB3  . LEU B 1 202 ? 26.764  10.132  71.295  1.00 90.51  ?  211 LEU B HB3  1 
ATOM   8583  H HG   . LEU B 1 202 ? 26.424  11.828  72.847  1.00 100.50 ?  211 LEU B HG   1 
ATOM   8584  H HD11 . LEU B 1 202 ? 26.641  11.492  75.129  1.00 122.93 ?  211 LEU B HD11 1 
ATOM   8585  H HD12 . LEU B 1 202 ? 25.383  10.698  74.573  1.00 122.93 ?  211 LEU B HD12 1 
ATOM   8586  H HD13 . LEU B 1 202 ? 26.733  9.924   74.892  1.00 122.93 ?  211 LEU B HD13 1 
ATOM   8587  H HD21 . LEU B 1 202 ? 28.560  11.870  73.682  1.00 63.04  ?  211 LEU B HD21 1 
ATOM   8588  H HD22 . LEU B 1 202 ? 28.720  10.334  73.308  1.00 63.04  ?  211 LEU B HD22 1 
ATOM   8589  H HD23 . LEU B 1 202 ? 28.531  11.416  72.160  1.00 63.04  ?  211 LEU B HD23 1 
ATOM   8590  N N    . GLN B 1 203 ? 24.141  11.564  70.710  1.00 87.15  ?  212 GLN B N    1 
ATOM   8591  C CA   . GLN B 1 203 ? 23.579  12.896  70.510  1.00 109.45 ?  212 GLN B CA   1 
ATOM   8592  C C    . GLN B 1 203 ? 22.093  12.884  70.816  1.00 129.66 ?  212 GLN B C    1 
ATOM   8593  O O    . GLN B 1 203 ? 21.527  13.896  71.246  1.00 162.07 ?  212 GLN B O    1 
ATOM   8594  C CB   . GLN B 1 203 ? 23.803  13.370  69.061  1.00 112.51 ?  212 GLN B CB   1 
ATOM   8595  C CG   . GLN B 1 203 ? 25.239  13.307  68.515  1.00 116.22 ?  212 GLN B CG   1 
ATOM   8596  C CD   . GLN B 1 203 ? 26.256  13.857  69.483  1.00 112.66 ?  212 GLN B CD   1 
ATOM   8597  O OE1  . GLN B 1 203 ? 26.071  14.946  70.034  1.00 96.43  ?  212 GLN B OE1  1 
ATOM   8598  N NE2  . GLN B 1 203 ? 27.360  13.112  69.681  1.00 119.17 ?  212 GLN B NE2  1 
ATOM   8599  H H    . GLN B 1 203 ? 24.404  11.174  69.990  1.00 104.58 ?  212 GLN B H    1 
ATOM   8600  H HA   . GLN B 1 203 ? 24.012  13.523  71.109  1.00 131.34 ?  212 GLN B HA   1 
ATOM   8601  H HB2  . GLN B 1 203 ? 23.252  12.824  68.478  1.00 135.01 ?  212 GLN B HB2  1 
ATOM   8602  H HB3  . GLN B 1 203 ? 23.514  14.294  69.000  1.00 135.01 ?  212 GLN B HB3  1 
ATOM   8603  H HG2  . GLN B 1 203 ? 25.468  12.382  68.332  1.00 139.47 ?  212 GLN B HG2  1 
ATOM   8604  H HG3  . GLN B 1 203 ? 25.289  13.829  67.698  1.00 139.47 ?  212 GLN B HG3  1 
ATOM   8605  H HE21 . GLN B 1 203 ? 27.455  12.365  69.265  1.00 143.00 ?  212 GLN B HE21 1 
ATOM   8606  H HE22 . GLN B 1 203 ? 27.970  13.382  70.224  1.00 143.00 ?  212 GLN B HE22 1 
ATOM   8607  N N    . VAL B 1 204 ? 21.458  11.732  70.592  1.00 115.53 ?  213 VAL B N    1 
ATOM   8608  C CA   . VAL B 1 204 ? 20.045  11.538  70.874  1.00 84.47  ?  213 VAL B CA   1 
ATOM   8609  C C    . VAL B 1 204 ? 19.777  11.510  72.363  1.00 81.44  ?  213 VAL B C    1 
ATOM   8610  O O    . VAL B 1 204 ? 18.664  11.781  72.812  1.00 82.86  ?  213 VAL B O    1 
ATOM   8611  C CB   . VAL B 1 204 ? 19.559  10.245  70.222  1.00 87.90  ?  213 VAL B CB   1 
ATOM   8612  C CG1  . VAL B 1 204 ? 18.136  9.956   70.723  1.00 98.32  ?  213 VAL B CG1  1 
ATOM   8613  C CG2  . VAL B 1 204 ? 19.693  10.332  68.705  1.00 84.07  ?  213 VAL B CG2  1 
ATOM   8614  H H    . VAL B 1 204 ? 21.840  11.033  70.269  1.00 138.63 ?  213 VAL B H    1 
ATOM   8615  H HA   . VAL B 1 204 ? 19.542  12.275  70.492  1.00 101.36 ?  213 VAL B HA   1 
ATOM   8616  H HB   . VAL B 1 204 ? 20.126  9.517   70.522  1.00 105.48 ?  213 VAL B HB   1 
ATOM   8617  H HG11 . VAL B 1 204 ? 17.818  9.136   70.314  1.00 117.99 ?  213 VAL B HG11 1 
ATOM   8618  H HG12 . VAL B 1 204 ? 18.155  9.860   71.688  1.00 117.99 ?  213 VAL B HG12 1 
ATOM   8619  H HG13 . VAL B 1 204 ? 17.559  10.696  70.475  1.00 117.99 ?  213 VAL B HG13 1 
ATOM   8620  H HG21 . VAL B 1 204 ? 19.379  9.502   68.312  1.00 100.89 ?  213 VAL B HG21 1 
ATOM   8621  H HG22 . VAL B 1 204 ? 19.157  11.074  68.383  1.00 100.89 ?  213 VAL B HG22 1 
ATOM   8622  H HG23 . VAL B 1 204 ? 20.625  10.474  68.478  1.00 100.89 ?  213 VAL B HG23 1 
ATOM   8623  N N    . PHE B 1 205 ? 20.703  10.989  73.126  1.00 84.93  ?  214 PHE B N    1 
ATOM   8624  C CA   . PHE B 1 205 ? 20.566  11.026  74.563  1.00 63.30  ?  214 PHE B CA   1 
ATOM   8625  C C    . PHE B 1 205 ? 20.599  12.446  75.081  1.00 86.29  ?  214 PHE B C    1 
ATOM   8626  O O    . PHE B 1 205 ? 20.129  12.680  76.196  1.00 64.21  ?  214 PHE B O    1 
ATOM   8627  C CB   . PHE B 1 205 ? 21.694  10.187  75.131  1.00 53.29  ?  214 PHE B CB   1 
ATOM   8628  C CG   . PHE B 1 205 ? 21.584  9.801   76.591  1.00 45.52  ?  214 PHE B CG   1 
ATOM   8629  C CD1  . PHE B 1 205 ? 20.465  10.011  77.344  1.00 52.87  ?  214 PHE B CD1  1 
ATOM   8630  C CD2  . PHE B 1 205 ? 22.651  9.169   77.200  1.00 85.38  ?  214 PHE B CD2  1 
ATOM   8631  C CE1  . PHE B 1 205 ? 20.398  9.595   78.696  1.00 89.16  ?  214 PHE B CE1  1 
ATOM   8632  C CE2  . PHE B 1 205 ? 22.587  8.753   78.563  1.00 39.14  ?  214 PHE B CE2  1 
ATOM   8633  C CZ   . PHE B 1 205 ? 21.481  8.968   79.286  1.00 60.38  ?  214 PHE B CZ   1 
ATOM   8634  H H    . PHE B 1 205 ? 21.421  10.609  72.842  1.00 101.92 ?  214 PHE B H    1 
ATOM   8635  H HA   . PHE B 1 205 ? 19.721  10.623  74.820  1.00 75.96  ?  214 PHE B HA   1 
ATOM   8636  H HB2  . PHE B 1 205 ? 21.746  9.364   74.620  1.00 63.95  ?  214 PHE B HB2  1 
ATOM   8637  H HB3  . PHE B 1 205 ? 22.522  10.681  75.026  1.00 63.95  ?  214 PHE B HB3  1 
ATOM   8638  H HD1  . PHE B 1 205 ? 19.727  10.424  76.957  1.00 63.44  ?  214 PHE B HD1  1 
ATOM   8639  H HD2  . PHE B 1 205 ? 23.424  9.005   76.710  1.00 102.46 ?  214 PHE B HD2  1 
ATOM   8640  H HE1  . PHE B 1 205 ? 19.628  9.755   79.193  1.00 106.99 ?  214 PHE B HE1  1 
ATOM   8641  H HE2  . PHE B 1 205 ? 23.320  8.334   78.953  1.00 46.96  ?  214 PHE B HE2  1 
ATOM   8642  H HZ   . PHE B 1 205 ? 21.444  8.706   80.177  1.00 72.46  ?  214 PHE B HZ   1 
ATOM   8643  N N    . HIS B 1 206 ? 21.175  13.390  74.305  1.00 84.78  ?  215 HIS B N    1 
ATOM   8644  C CA   . HIS B 1 206 ? 21.227  14.786  74.715  1.00 90.17  ?  215 HIS B CA   1 
ATOM   8645  C C    . HIS B 1 206 ? 19.841  15.380  74.841  1.00 94.95  ?  215 HIS B C    1 
ATOM   8646  O O    . HIS B 1 206 ? 19.662  16.337  75.601  1.00 145.62 ?  215 HIS B O    1 
ATOM   8647  C CB   . HIS B 1 206 ? 22.067  15.619  73.726  1.00 99.17  ?  215 HIS B CB   1 
ATOM   8648  C CG   . HIS B 1 206 ? 23.552  15.573  73.978  1.00 103.83 ?  215 HIS B CG   1 
ATOM   8649  N ND1  . HIS B 1 206 ? 24.268  14.401  74.031  1.00 100.84 ?  215 HIS B ND1  1 
ATOM   8650  C CD2  . HIS B 1 206 ? 24.447  16.561  74.222  1.00 123.99 ?  215 HIS B CD2  1 
ATOM   8651  C CE1  . HIS B 1 206 ? 25.534  14.660  74.294  1.00 105.54 ?  215 HIS B CE1  1 
ATOM   8652  N NE2  . HIS B 1 206 ? 25.669  15.965  74.416  1.00 141.27 ?  215 HIS B NE2  1 
ATOM   8653  H H    . HIS B 1 206 ? 21.539  13.235  73.541  1.00 101.73 ?  215 HIS B H    1 
ATOM   8654  H HA   . HIS B 1 206 ? 21.653  14.841  75.585  1.00 108.21 ?  215 HIS B HA   1 
ATOM   8655  H HB2  . HIS B 1 206 ? 21.910  15.287  72.828  1.00 119.01 ?  215 HIS B HB2  1 
ATOM   8656  H HB3  . HIS B 1 206 ? 21.787  16.546  73.785  1.00 119.01 ?  215 HIS B HB3  1 
ATOM   8657  H HD1  . HIS B 1 206 ? 23.937  13.615  73.917  1.00 121.00 ?  215 HIS B HD1  1 
ATOM   8658  H HD2  . HIS B 1 206 ? 24.266  17.472  74.258  1.00 148.79 ?  215 HIS B HD2  1 
ATOM   8659  H HE1  . HIS B 1 206 ? 26.215  14.031  74.371  1.00 126.65 ?  215 HIS B HE1  1 
ATOM   8660  N N    . GLN B 1 207 ? 18.852  14.808  74.145  1.00 78.39  ?  216 GLN B N    1 
ATOM   8661  C CA   . GLN B 1 207 ? 17.483  15.316  74.137  1.00 90.78  ?  216 GLN B CA   1 
ATOM   8662  C C    . GLN B 1 207 ? 16.829  15.235  75.485  1.00 90.21  ?  216 GLN B C    1 
ATOM   8663  O O    . GLN B 1 207 ? 15.802  15.860  75.716  1.00 86.73  ?  216 GLN B O    1 
ATOM   8664  C CB   . GLN B 1 207 ? 16.628  14.526  73.151  1.00 103.82 ?  216 GLN B CB   1 
ATOM   8665  C CG   . GLN B 1 207 ? 17.108  14.653  71.753  1.00 85.63  ?  216 GLN B CG   1 
ATOM   8666  C CD   . GLN B 1 207 ? 16.246  13.924  70.822  1.00 96.56  ?  216 GLN B CD   1 
ATOM   8667  O OE1  . GLN B 1 207 ? 15.053  13.762  71.065  1.00 109.56 ?  216 GLN B OE1  1 
ATOM   8668  N NE2  . GLN B 1 207 ? 16.818  13.523  69.698  1.00 85.87  ?  216 GLN B NE2  1 
ATOM   8669  H H    . GLN B 1 207 ? 18.957  14.107  73.657  1.00 94.06  ?  216 GLN B H    1 
ATOM   8670  H HA   . GLN B 1 207 ? 17.488  16.245  73.858  1.00 108.94 ?  216 GLN B HA   1 
ATOM   8671  H HB2  . GLN B 1 207 ? 16.652  13.587  73.393  1.00 124.59 ?  216 GLN B HB2  1 
ATOM   8672  H HB3  . GLN B 1 207 ? 15.717  14.856  73.187  1.00 124.59 ?  216 GLN B HB3  1 
ATOM   8673  H HG2  . GLN B 1 207 ? 17.108  15.589  71.499  1.00 102.75 ?  216 GLN B HG2  1 
ATOM   8674  H HG3  . GLN B 1 207 ? 18.004  14.287  71.688  1.00 102.75 ?  216 GLN B HG3  1 
ATOM   8675  H HE21 . GLN B 1 207 ? 17.648  13.695  69.553  1.00 103.05 ?  216 GLN B HE21 1 
ATOM   8676  H HE22 . GLN B 1 207 ? 16.360  13.090  69.113  1.00 103.05 ?  216 GLN B HE22 1 
ATOM   8677  N N    . ILE B 1 208 ? 17.412  14.487  76.388  1.00 83.52  ?  217 ILE B N    1 
ATOM   8678  C CA   . ILE B 1 208 ? 16.790  14.301  77.678  1.00 86.95  ?  217 ILE B CA   1 
ATOM   8679  C C    . ILE B 1 208 ? 16.537  15.623  78.359  1.00 100.94 ?  217 ILE B C    1 
ATOM   8680  O O    . ILE B 1 208 ? 15.596  15.740  79.146  1.00 74.28  ?  217 ILE B O    1 
ATOM   8681  C CB   . ILE B 1 208 ? 17.676  13.401  78.531  1.00 67.26  ?  217 ILE B CB   1 
ATOM   8682  C CG1  . ILE B 1 208 ? 16.975  13.098  79.811  1.00 58.26  ?  217 ILE B CG1  1 
ATOM   8683  C CG2  . ILE B 1 208 ? 18.987  14.103  78.841  1.00 122.49 ?  217 ILE B CG2  1 
ATOM   8684  C CD1  . ILE B 1 208 ? 17.548  11.936  80.528  1.00 64.46  ?  217 ILE B CD1  1 
ATOM   8685  H H    . ILE B 1 208 ? 18.161  14.077  76.284  1.00 100.22 ?  217 ILE B H    1 
ATOM   8686  H HA   . ILE B 1 208 ? 15.936  13.857  77.558  1.00 104.34 ?  217 ILE B HA   1 
ATOM   8687  H HB   . ILE B 1 208 ? 17.854  12.574  78.055  1.00 80.71  ?  217 ILE B HB   1 
ATOM   8688  H HG12 . ILE B 1 208 ? 17.039  13.870  80.395  1.00 69.92  ?  217 ILE B HG12 1 
ATOM   8689  H HG13 . ILE B 1 208 ? 16.044  12.903  79.621  1.00 69.92  ?  217 ILE B HG13 1 
ATOM   8690  H HG21 . ILE B 1 208 ? 19.538  13.517  79.383  1.00 146.99 ?  217 ILE B HG21 1 
ATOM   8691  H HG22 . ILE B 1 208 ? 19.440  14.307  78.008  1.00 146.99 ?  217 ILE B HG22 1 
ATOM   8692  H HG23 . ILE B 1 208 ? 18.799  14.922  79.325  1.00 146.99 ?  217 ILE B HG23 1 
ATOM   8693  H HD11 . ILE B 1 208 ? 17.049  11.794  81.347  1.00 77.35  ?  217 ILE B HD11 1 
ATOM   8694  H HD12 . ILE B 1 208 ? 17.483  11.152  79.960  1.00 77.35  ?  217 ILE B HD12 1 
ATOM   8695  H HD13 . ILE B 1 208 ? 18.478  12.120  80.733  1.00 77.35  ?  217 ILE B HD13 1 
ATOM   8696  N N    . HIS B 1 209 ? 17.406  16.606  78.134  1.00 76.73  ?  218 HIS B N    1 
ATOM   8697  C CA   . HIS B 1 209 ? 17.365  17.822  78.925  1.00 85.55  ?  218 HIS B CA   1 
ATOM   8698  C C    . HIS B 1 209 ? 16.180  18.679  78.538  1.00 92.32  ?  218 HIS B C    1 
ATOM   8699  O O    . HIS B 1 209 ? 15.672  19.468  79.350  1.00 85.74  ?  218 HIS B O    1 
ATOM   8700  C CB   . HIS B 1 209 ? 18.647  18.583  78.719  1.00 75.56  ?  218 HIS B CB   1 
ATOM   8701  C CG   . HIS B 1 209 ? 19.821  17.959  79.373  1.00 95.63  ?  218 HIS B CG   1 
ATOM   8702  N ND1  . HIS B 1 209 ? 19.955  17.875  80.739  1.00 127.95 ?  218 HIS B ND1  1 
ATOM   8703  C CD2  . HIS B 1 209 ? 20.931  17.412  78.846  1.00 68.50  ?  218 HIS B CD2  1 
ATOM   8704  C CE1  . HIS B 1 209 ? 21.106  17.302  81.025  1.00 52.15  ?  218 HIS B CE1  1 
ATOM   8705  N NE2  . HIS B 1 209 ? 21.720  17.012  79.893  1.00 106.26 ?  218 HIS B NE2  1 
ATOM   8706  H H    . HIS B 1 209 ? 18.022  16.590  77.535  1.00 92.07  ?  218 HIS B H    1 
ATOM   8707  H HA   . HIS B 1 209 ? 17.288  17.595  79.865  1.00 102.66 ?  218 HIS B HA   1 
ATOM   8708  H HB2  . HIS B 1 209 ? 18.830  18.636  77.768  1.00 90.67  ?  218 HIS B HB2  1 
ATOM   8709  H HB3  . HIS B 1 209 ? 18.543  19.475  79.085  1.00 90.67  ?  218 HIS B HB3  1 
ATOM   8710  H HD2  . HIS B 1 209 ? 21.131  17.330  77.941  1.00 82.20  ?  218 HIS B HD2  1 
ATOM   8711  H HE1  . HIS B 1 209 ? 21.428  17.123  81.879  1.00 62.58  ?  218 HIS B HE1  1 
ATOM   8712  N N    . ASP B 1 210 ? 15.744  18.518  77.298  1.00 156.59 ?  219 ASP B N    1 
ATOM   8713  C CA   . ASP B 1 210 ? 14.664  19.293  76.731  1.00 99.58  ?  219 ASP B CA   1 
ATOM   8714  C C    . ASP B 1 210 ? 13.303  18.797  77.159  1.00 85.54  ?  219 ASP B C    1 
ATOM   8715  O O    . ASP B 1 210 ? 12.305  19.483  76.935  1.00 136.42 ?  219 ASP B O    1 
ATOM   8716  C CB   . ASP B 1 210 ? 14.722  19.202  75.219  1.00 115.93 ?  219 ASP B CB   1 
ATOM   8717  C CG   . ASP B 1 210 ? 16.063  19.555  74.672  1.00 123.43 ?  219 ASP B CG   1 
ATOM   8718  O OD1  . ASP B 1 210 ? 16.722  20.438  75.263  1.00 133.45 ?  219 ASP B OD1  1 
ATOM   8719  O OD2  . ASP B 1 210 ? 16.463  18.921  73.669  1.00 113.33 -1 219 ASP B OD2  1 
ATOM   8720  H H    . ASP B 1 210 ? 16.073  17.943  76.750  1.00 187.91 ?  219 ASP B H    1 
ATOM   8721  H HA   . ASP B 1 210 ? 14.755  20.223  76.993  1.00 119.49 ?  219 ASP B HA   1 
ATOM   8722  H HB2  . ASP B 1 210 ? 14.518  18.293  74.949  1.00 139.12 ?  219 ASP B HB2  1 
ATOM   8723  H HB3  . ASP B 1 210 ? 14.073  19.815  74.840  1.00 139.12 ?  219 ASP B HB3  1 
ATOM   8724  N N    . HIS B 1 211 ? 13.231  17.612  77.725  1.00 81.73  ?  220 HIS B N    1 
ATOM   8725  C CA   . HIS B 1 211 ? 11.954  16.939  77.900  1.00 72.87  ?  220 HIS B CA   1 
ATOM   8726  C C    . HIS B 1 211 ? 11.786  16.345  79.297  1.00 56.93  ?  220 HIS B C    1 
ATOM   8727  O O    . HIS B 1 211 ? 10.757  15.714  79.574  1.00 77.65  ?  220 HIS B O    1 
ATOM   8728  C CB   . HIS B 1 211 ? 11.782  15.868  76.804  1.00 85.15  ?  220 HIS B CB   1 
ATOM   8729  C CG   . HIS B 1 211 ? 11.872  16.414  75.404  1.00 90.35  ?  220 HIS B CG   1 
ATOM   8730  N ND1  . HIS B 1 211 ? 12.876  16.066  74.526  1.00 112.22 ?  220 HIS B ND1  1 
ATOM   8731  C CD2  . HIS B 1 211 ? 11.093  17.303  74.744  1.00 100.38 ?  220 HIS B CD2  1 
ATOM   8732  C CE1  . HIS B 1 211 ? 12.700  16.699  73.380  1.00 93.65  ?  220 HIS B CE1  1 
ATOM   8733  N NE2  . HIS B 1 211 ? 11.623  17.454  73.486  1.00 101.98 ?  220 HIS B NE2  1 
ATOM   8734  H H    . HIS B 1 211 ? 13.907  17.170  78.020  1.00 98.08  ?  220 HIS B H    1 
ATOM   8735  H HA   . HIS B 1 211 ? 11.247  17.592  77.779  1.00 87.44  ?  220 HIS B HA   1 
ATOM   8736  H HB2  . HIS B 1 211 ? 12.478  15.200  76.907  1.00 102.18 ?  220 HIS B HB2  1 
ATOM   8737  H HB3  . HIS B 1 211 ? 10.911  15.454  76.905  1.00 102.18 ?  220 HIS B HB3  1 
ATOM   8738  H HD2  . HIS B 1 211 ? 10.330  17.720  75.074  1.00 120.46 ?  220 HIS B HD2  1 
ATOM   8739  H HE1  . HIS B 1 211 ? 13.244  16.627  72.629  1.00 112.38 ?  220 HIS B HE1  1 
ATOM   8740  N N    . VAL B 1 212 ? 12.728  16.606  80.210  1.00 69.96  ?  221 VAL B N    1 
ATOM   8741  C CA   . VAL B 1 212 ? 12.614  16.203  81.612  1.00 73.90  ?  221 VAL B CA   1 
ATOM   8742  C C    . VAL B 1 212 ? 13.050  17.357  82.515  1.00 88.73  ?  221 VAL B C    1 
ATOM   8743  O O    . VAL B 1 212 ? 13.980  18.107  82.195  1.00 101.69 ?  221 VAL B O    1 
ATOM   8744  C CB   . VAL B 1 212 ? 13.461  14.950  81.946  1.00 72.44  ?  221 VAL B CB   1 
ATOM   8745  C CG1  . VAL B 1 212 ? 13.167  14.496  83.375  1.00 79.08  ?  221 VAL B CG1  1 
ATOM   8746  C CG2  . VAL B 1 212 ? 13.214  13.804  80.948  1.00 61.91  ?  221 VAL B CG2  1 
ATOM   8747  H H    . VAL B 1 212 ? 13.459  17.024  80.035  1.00 83.95  ?  221 VAL B H    1 
ATOM   8748  H HA   . VAL B 1 212 ? 11.686  16.000  81.809  1.00 88.68  ?  221 VAL B HA   1 
ATOM   8749  H HB   . VAL B 1 212 ? 14.400  15.187  81.898  1.00 86.93  ?  221 VAL B HB   1 
ATOM   8750  H HG11 . VAL B 1 212 ? 13.702  13.712  83.573  1.00 94.90  ?  221 VAL B HG11 1 
ATOM   8751  H HG12 . VAL B 1 212 ? 13.393  15.215  83.986  1.00 94.90  ?  221 VAL B HG12 1 
ATOM   8752  H HG13 . VAL B 1 212 ? 12.224  14.282  83.450  1.00 94.90  ?  221 VAL B HG13 1 
ATOM   8753  H HG21 . VAL B 1 212 ? 13.764  13.045  81.197  1.00 74.29  ?  221 VAL B HG21 1 
ATOM   8754  H HG22 . VAL B 1 212 ? 12.277  13.557  80.976  1.00 74.29  ?  221 VAL B HG22 1 
ATOM   8755  H HG23 . VAL B 1 212 ? 13.451  14.106  80.057  1.00 74.29  ?  221 VAL B HG23 1 
ATOM   8756  N N    . ASN B 1 213 ? 12.375  17.493  83.635  1.00 73.73  ?  222 ASN B N    1 
ATOM   8757  C CA   . ASN B 1 213 ? 12.791  18.465  84.590  1.00 78.60  ?  222 ASN B CA   1 
ATOM   8758  C C    . ASN B 1 213 ? 13.326  17.739  85.802  1.00 75.76  ?  222 ASN B C    1 
ATOM   8759  O O    . ASN B 1 213 ? 12.772  16.707  86.200  1.00 64.16  ?  222 ASN B O    1 
ATOM   8760  C CB   . ASN B 1 213 ? 11.628  19.370  85.017  1.00 105.36 ?  222 ASN B CB   1 
ATOM   8761  C CG   . ASN B 1 213 ? 11.944  20.168  86.262  1.00 141.04 ?  222 ASN B CG   1 
ATOM   8762  H H    . ASN B 1 213 ? 11.681  17.037  83.858  1.00 88.48  ?  222 ASN B H    1 
ATOM   8763  H HA   . ASN B 1 213 ? 13.497  19.015  84.216  1.00 94.33  ?  222 ASN B HA   1 
ATOM   8764  H HB2  . ASN B 1 213 ? 11.434  19.995  84.300  1.00 126.43 ?  222 ASN B HB2  1 
ATOM   8765  H HB3  . ASN B 1 213 ? 10.850  18.821  85.200  1.00 126.43 ?  222 ASN B HB3  1 
ATOM   8766  N N    . PRO B 1 214 ? 14.397  18.229  86.409  1.00 72.62  ?  223 PRO B N    1 
ATOM   8767  C CA   . PRO B 1 214 ? 14.925  17.506  87.566  1.00 74.53  ?  223 PRO B CA   1 
ATOM   8768  C C    . PRO B 1 214 ? 13.886  17.340  88.636  1.00 85.93  ?  223 PRO B C    1 
ATOM   8769  O O    . PRO B 1 214 ? 13.745  16.247  89.185  1.00 70.10  ?  223 PRO B O    1 
ATOM   8770  C CB   . PRO B 1 214 ? 16.107  18.371  88.006  1.00 71.44  ?  223 PRO B CB   1 
ATOM   8771  C CG   . PRO B 1 214 ? 16.529  19.064  86.791  1.00 117.12 ?  223 PRO B CG   1 
ATOM   8772  C CD   . PRO B 1 214 ? 15.290  19.308  85.979  1.00 128.20 ?  223 PRO B CD   1 
ATOM   8773  H HA   . PRO B 1 214 ? 15.250  16.632  87.297  1.00 89.44  ?  223 PRO B HA   1 
ATOM   8774  H HB2  . PRO B 1 214 ? 15.817  19.005  88.681  1.00 85.72  ?  223 PRO B HB2  1 
ATOM   8775  H HB3  . PRO B 1 214 ? 16.819  17.807  88.345  1.00 85.72  ?  223 PRO B HB3  1 
ATOM   8776  H HG2  . PRO B 1 214 ? 16.948  19.906  87.030  1.00 140.54 ?  223 PRO B HG2  1 
ATOM   8777  H HG3  . PRO B 1 214 ? 17.151  18.504  86.301  1.00 140.54 ?  223 PRO B HG3  1 
ATOM   8778  H HD2  . PRO B 1 214 ? 14.907  20.172  86.195  1.00 153.83 ?  223 PRO B HD2  1 
ATOM   8779  H HD3  . PRO B 1 214 ? 15.484  19.230  85.032  1.00 153.83 ?  223 PRO B HD3  1 
ATOM   8780  N N    . LYS B 1 215 ? 13.143  18.405  88.931  1.00 112.24 ?  224 LYS B N    1 
ATOM   8781  C CA   . LYS B 1 215 ? 12.198  18.369  90.035  1.00 102.50 ?  224 LYS B CA   1 
ATOM   8782  C C    . LYS B 1 215 ? 11.192  17.242  89.850  1.00 90.72  ?  224 LYS B C    1 
ATOM   8783  O O    . LYS B 1 215 ? 10.960  16.444  90.767  1.00 75.88  ?  224 LYS B O    1 
ATOM   8784  C CB   . LYS B 1 215 ? 11.480  19.717  90.139  1.00 141.68 ?  224 LYS B CB   1 
ATOM   8785  H H    . LYS B 1 215 ? 13.169  19.153  88.508  1.00 134.68 ?  224 LYS B H    1 
ATOM   8786  H HA   . LYS B 1 215 ? 12.679  18.216  90.863  1.00 123.00 ?  224 LYS B HA   1 
ATOM   8787  N N    . ALA B 1 216 ? 10.590  17.159  88.658  1.00 106.48 ?  225 ALA B N    1 
ATOM   8788  C CA   . ALA B 1 216 ? 9.497   16.210  88.432  1.00 100.19 ?  225 ALA B CA   1 
ATOM   8789  C C    . ALA B 1 216 ? 9.967   14.764  88.485  1.00 87.31  ?  225 ALA B C    1 
ATOM   8790  O O    . ALA B 1 216 ? 9.300   13.920  89.085  1.00 77.82  ?  225 ALA B O    1 
ATOM   8791  C CB   . ALA B 1 216 ? 8.829   16.483  87.074  1.00 106.03 ?  225 ALA B CB   1 
ATOM   8792  H H    . ALA B 1 216 ? 10.794  17.635  87.972  1.00 127.78 ?  225 ALA B H    1 
ATOM   8793  H HA   . ALA B 1 216 ? 8.828   16.332  89.123  1.00 120.23 ?  225 ALA B HA   1 
ATOM   8794  H HB1  . ALA B 1 216 ? 8.110   15.845  86.943  1.00 127.24 ?  225 ALA B HB1  1 
ATOM   8795  H HB2  . ALA B 1 216 ? 8.476   17.386  87.071  1.00 127.24 ?  225 ALA B HB2  1 
ATOM   8796  H HB3  . ALA B 1 216 ? 9.491   16.384  86.371  1.00 127.24 ?  225 ALA B HB3  1 
ATOM   8797  N N    . PHE B 1 217 ? 11.118  14.465  87.872  1.00 95.24  ?  226 PHE B N    1 
ATOM   8798  C CA   . PHE B 1 217 ? 11.613  13.088  87.794  1.00 80.39  ?  226 PHE B CA   1 
ATOM   8799  C C    . PHE B 1 217 ? 11.969  12.553  89.172  1.00 67.05  ?  226 PHE B C    1 
ATOM   8800  O O    . PHE B 1 217 ? 11.693  11.393  89.477  1.00 56.97  ?  226 PHE B O    1 
ATOM   8801  C CB   . PHE B 1 217 ? 12.844  13.022  86.869  1.00 82.39  ?  226 PHE B CB   1 
ATOM   8802  C CG   . PHE B 1 217 ? 13.516  11.666  86.822  1.00 63.28  ?  226 PHE B CG   1 
ATOM   8803  C CD1  . PHE B 1 217 ? 13.137  10.697  85.880  1.00 58.58  ?  226 PHE B CD1  1 
ATOM   8804  C CD2  . PHE B 1 217 ? 14.528  11.333  87.765  1.00 71.86  ?  226 PHE B CD2  1 
ATOM   8805  C CE1  . PHE B 1 217 ? 13.764  9.413   85.868  1.00 66.40  ?  226 PHE B CE1  1 
ATOM   8806  C CE2  . PHE B 1 217 ? 15.162  10.044  87.761  1.00 74.06  ?  226 PHE B CE2  1 
ATOM   8807  C CZ   . PHE B 1 217 ? 14.795  9.105   86.823  1.00 72.54  ?  226 PHE B CZ   1 
ATOM   8808  H H    . PHE B 1 217 ? 11.630  15.043  87.493  1.00 114.29 ?  226 PHE B H    1 
ATOM   8809  H HA   . PHE B 1 217 ? 10.921  12.522  87.418  1.00 96.47  ?  226 PHE B HA   1 
ATOM   8810  H HB2  . PHE B 1 217 ? 12.567  13.245  85.966  1.00 98.87  ?  226 PHE B HB2  1 
ATOM   8811  H HB3  . PHE B 1 217 ? 13.500  13.666  87.178  1.00 98.87  ?  226 PHE B HB3  1 
ATOM   8812  H HD1  . PHE B 1 217 ? 12.473  10.892  85.259  1.00 70.30  ?  226 PHE B HD1  1 
ATOM   8813  H HD2  . PHE B 1 217 ? 14.782  11.963  88.400  1.00 86.23  ?  226 PHE B HD2  1 
ATOM   8814  H HE1  . PHE B 1 217 ? 13.514  8.780   85.234  1.00 79.68  ?  226 PHE B HE1  1 
ATOM   8815  H HE2  . PHE B 1 217 ? 15.828  9.849   88.380  1.00 88.87  ?  226 PHE B HE2  1 
ATOM   8816  H HZ   . PHE B 1 217 ? 15.204  8.270   86.813  1.00 87.05  ?  226 PHE B HZ   1 
ATOM   8817  N N    . PHE B 1 218 ? 12.568  13.376  90.018  1.00 56.16  ?  227 PHE B N    1 
ATOM   8818  C CA   . PHE B 1 218 ? 13.043  12.874  91.284  1.00 96.32  ?  227 PHE B CA   1 
ATOM   8819  C C    . PHE B 1 218 ? 11.899  12.597  92.244  1.00 104.20 ?  227 PHE B C    1 
ATOM   8820  O O    . PHE B 1 218 ? 11.981  11.673  93.063  1.00 89.40  ?  227 PHE B O    1 
ATOM   8821  C CB   . PHE B 1 218 ? 13.993  13.860  91.919  1.00 82.61  ?  227 PHE B CB   1 
ATOM   8822  C CG   . PHE B 1 218 ? 14.485  13.388  93.202  1.00 61.24  ?  227 PHE B CG   1 
ATOM   8823  C CD1  . PHE B 1 218 ? 15.495  12.438  93.245  1.00 59.55  ?  227 PHE B CD1  1 
ATOM   8824  C CD2  . PHE B 1 218 ? 13.885  13.787  94.367  1.00 64.11  ?  227 PHE B CD2  1 
ATOM   8825  C CE1  . PHE B 1 218 ? 15.952  11.937  94.486  1.00 60.95  ?  227 PHE B CE1  1 
ATOM   8826  C CE2  . PHE B 1 218 ? 14.333  13.284  95.625  1.00 65.52  ?  227 PHE B CE2  1 
ATOM   8827  C CZ   . PHE B 1 218 ? 15.356  12.359  95.676  1.00 68.78  ?  227 PHE B CZ   1 
ATOM   8828  H H    . PHE B 1 218 ? 12.708  14.214  89.882  1.00 67.39  ?  227 PHE B H    1 
ATOM   8829  H HA   . PHE B 1 218 ? 13.522  12.044  91.137  1.00 115.58 ?  227 PHE B HA   1 
ATOM   8830  H HB2  . PHE B 1 218 ? 14.755  13.992  91.333  1.00 99.13  ?  227 PHE B HB2  1 
ATOM   8831  H HB3  . PHE B 1 218 ? 13.532  14.701  92.063  1.00 99.13  ?  227 PHE B HB3  1 
ATOM   8832  H HD1  . PHE B 1 218 ? 15.894  12.151  92.455  1.00 71.46  ?  227 PHE B HD1  1 
ATOM   8833  H HD2  . PHE B 1 218 ? 13.193  14.408  94.340  1.00 76.93  ?  227 PHE B HD2  1 
ATOM   8834  H HE1  . PHE B 1 218 ? 16.642  11.314  94.509  1.00 73.14  ?  227 PHE B HE1  1 
ATOM   8835  H HE2  . PHE B 1 218 ? 13.932  13.577  96.412  1.00 78.62  ?  227 PHE B HE2  1 
ATOM   8836  H HZ   . PHE B 1 218 ? 15.657  12.034  96.493  1.00 82.54  ?  227 PHE B HZ   1 
ATOM   8837  N N    . SER B 1 219 ? 10.873  13.449  92.236  1.00 100.16 ?  228 SER B N    1 
ATOM   8838  C CA   . SER B 1 219 ? 9.846   13.421  93.271  1.00 93.12  ?  228 SER B CA   1 
ATOM   8839  C C    . SER B 1 219 ? 8.690   12.507  92.946  1.00 94.38  ?  228 SER B C    1 
ATOM   8840  O O    . SER B 1 219 ? 7.995   12.031  93.863  1.00 71.18  ?  228 SER B O    1 
ATOM   8841  C CB   . SER B 1 219 ? 9.290   14.816  93.459  1.00 82.01  ?  228 SER B CB   1 
ATOM   8842  O OG   . SER B 1 219 ? 10.314  15.701  93.848  1.00 97.49  ?  228 SER B OG   1 
ATOM   8843  H H    . SER B 1 219 ? 10.751  14.054  91.638  1.00 120.20 ?  228 SER B H    1 
ATOM   8844  H HA   . SER B 1 219 ? 10.240  13.131  94.109  1.00 111.74 ?  228 SER B HA   1 
ATOM   8845  H HB2  . SER B 1 219 ? 8.908   15.121  92.621  1.00 98.41  ?  228 SER B HB2  1 
ATOM   8846  H HB3  . SER B 1 219 ? 8.608   14.796  94.148  1.00 98.41  ?  228 SER B HB3  1 
ATOM   8847  H HG   . SER B 1 219 ? 10.002  16.474  93.951  1.00 116.99 ?  228 SER B HG   1 
ATOM   8848  N N    . VAL B 1 220 ? 8.508   12.232  91.668  1.00 71.26  ?  229 VAL B N    1 
ATOM   8849  C CA   . VAL B 1 220 ? 7.320   11.581  91.183  1.00 87.68  ?  229 VAL B CA   1 
ATOM   8850  C C    . VAL B 1 220 ? 7.745   10.313  90.464  1.00 85.60  ?  229 VAL B C    1 
ATOM   8851  O O    . VAL B 1 220 ? 7.651   9.201   90.997  1.00 109.94 ?  229 VAL B O    1 
ATOM   8852  C CB   . VAL B 1 220 ? 6.570   12.554  90.242  1.00 107.13 ?  229 VAL B CB   1 
ATOM   8853  C CG1  . VAL B 1 220 ? 5.256   11.978  89.717  1.00 68.90  ?  229 VAL B CG1  1 
ATOM   8854  C CG2  . VAL B 1 220 ? 6.341   13.864  90.937  1.00 61.13  ?  229 VAL B CG2  1 
ATOM   8855  H H    . VAL B 1 220 ? 9.076   12.419  91.050  1.00 85.52  ?  229 VAL B H    1 
ATOM   8856  H HA   . VAL B 1 220 ? 6.741   11.347  91.926  1.00 105.21 ?  229 VAL B HA   1 
ATOM   8857  H HB   . VAL B 1 220 ? 7.135   12.730  89.474  1.00 128.56 ?  229 VAL B HB   1 
ATOM   8858  H HG11 . VAL B 1 220 ? 4.836   12.631  89.136  1.00 82.68  ?  229 VAL B HG11 1 
ATOM   8859  H HG12 . VAL B 1 220 ? 5.444   11.166  89.221  1.00 82.68  ?  229 VAL B HG12 1 
ATOM   8860  H HG13 . VAL B 1 220 ? 4.676   11.780  90.469  1.00 82.68  ?  229 VAL B HG13 1 
ATOM   8861  H HG21 . VAL B 1 220 ? 5.871   14.462  90.336  1.00 73.36  ?  229 VAL B HG21 1 
ATOM   8862  H HG22 . VAL B 1 220 ? 5.809   13.710  91.734  1.00 73.36  ?  229 VAL B HG22 1 
ATOM   8863  H HG23 . VAL B 1 220 ? 7.199   14.246  91.181  1.00 73.36  ?  229 VAL B HG23 1 
ATOM   8864  N N    . LEU B 1 221 ? 8.307   10.492  89.281  1.00 60.16  ?  230 LEU B N    1 
ATOM   8865  C CA   . LEU B 1 221 ? 8.452   9.364   88.370  1.00 62.95  ?  230 LEU B CA   1 
ATOM   8866  C C    . LEU B 1 221 ? 9.418   8.285   88.839  1.00 81.40  ?  230 LEU B C    1 
ATOM   8867  O O    . LEU B 1 221 ? 9.231   7.108   88.488  1.00 80.98  ?  230 LEU B O    1 
ATOM   8868  C CB   . LEU B 1 221 ? 8.890   9.891   87.024  1.00 65.86  ?  230 LEU B CB   1 
ATOM   8869  C CG   . LEU B 1 221 ? 8.919   8.824   85.959  1.00 76.98  ?  230 LEU B CG   1 
ATOM   8870  C CD1  . LEU B 1 221 ? 7.568   8.095   85.870  1.00 63.81  ?  230 LEU B CD1  1 
ATOM   8871  C CD2  . LEU B 1 221 ? 9.262   9.570   84.660  1.00 87.42  ?  230 LEU B CD2  1 
ATOM   8872  H H    . LEU B 1 221 ? 8.609   11.240  88.982  1.00 72.19  ?  230 LEU B H    1 
ATOM   8873  H HA   . LEU B 1 221 ? 7.584   8.948   88.254  1.00 75.54  ?  230 LEU B HA   1 
ATOM   8874  H HB2  . LEU B 1 221 ? 8.271   10.582  86.738  1.00 79.03  ?  230 LEU B HB2  1 
ATOM   8875  H HB3  . LEU B 1 221 ? 9.784   10.259  87.104  1.00 79.03  ?  230 LEU B HB3  1 
ATOM   8876  H HG   . LEU B 1 221 ? 9.619   8.180   86.151  1.00 92.38  ?  230 LEU B HG   1 
ATOM   8877  H HD11 . LEU B 1 221 ? 7.621   7.417   85.178  1.00 76.57  ?  230 LEU B HD11 1 
ATOM   8878  H HD12 . LEU B 1 221 ? 7.376   7.681   86.725  1.00 76.57  ?  230 LEU B HD12 1 
ATOM   8879  H HD13 . LEU B 1 221 ? 6.877   8.739   85.650  1.00 76.57  ?  230 LEU B HD13 1 
ATOM   8880  H HD21 . LEU B 1 221 ? 9.296   8.933   83.930  1.00 104.91 ?  230 LEU B HD21 1 
ATOM   8881  H HD22 . LEU B 1 221 ? 8.576   10.234  84.488  1.00 104.91 ?  230 LEU B HD22 1 
ATOM   8882  H HD23 . LEU B 1 221 ? 10.124  10.003  84.763  1.00 104.91 ?  230 LEU B HD23 1 
ATOM   8883  N N    . ARG B 1 222 ? 10.474  8.650   89.574  1.00 58.67  ?  231 ARG B N    1 
ATOM   8884  C CA   . ARG B 1 222 ? 11.362  7.630   90.115  1.00 71.43  ?  231 ARG B CA   1 
ATOM   8885  C C    . ARG B 1 222 ? 10.612  6.746   91.093  1.00 46.25  ?  231 ARG B C    1 
ATOM   8886  O O    . ARG B 1 222 ? 10.767  5.519   91.057  1.00 59.37  ?  231 ARG B O    1 
ATOM   8887  C CB   . ARG B 1 222 ? 12.544  8.312   90.810  1.00 78.19  ?  231 ARG B CB   1 
ATOM   8888  C CG   . ARG B 1 222 ? 13.658  7.415   91.313  1.00 75.40  ?  231 ARG B CG   1 
ATOM   8889  C CD   . ARG B 1 222 ? 14.655  8.270   92.079  1.00 137.31 ?  231 ARG B CD   1 
ATOM   8890  N NE   . ARG B 1 222 ? 14.059  8.828   93.291  1.00 154.90 ?  231 ARG B NE   1 
ATOM   8891  C CZ   . ARG B 1 222 ? 14.444  8.556   94.530  1.00 112.09 ?  231 ARG B CZ   1 
ATOM   8892  N NH1  . ARG B 1 222 ? 15.496  7.759   94.773  1.00 135.40 1  231 ARG B NH1  1 
ATOM   8893  N NH2  . ARG B 1 222 ? 13.795  9.134   95.525  1.00 92.27  1  231 ARG B NH2  1 
ATOM   8894  H H    . ARG B 1 222 ? 10.691  9.460   89.766  1.00 70.41  ?  231 ARG B H    1 
ATOM   8895  H HA   . ARG B 1 222 ? 11.702  7.077   89.394  1.00 85.72  ?  231 ARG B HA   1 
ATOM   8896  H HB2  . ARG B 1 222 ? 12.941  8.937   90.185  1.00 93.82  ?  231 ARG B HB2  1 
ATOM   8897  H HB3  . ARG B 1 222 ? 12.202  8.799   91.576  1.00 93.82  ?  231 ARG B HB3  1 
ATOM   8898  H HG2  . ARG B 1 222 ? 13.296  6.744   91.912  1.00 90.48  ?  231 ARG B HG2  1 
ATOM   8899  H HG3  . ARG B 1 222 ? 14.111  7.001   90.562  1.00 90.48  ?  231 ARG B HG3  1 
ATOM   8900  H HD2  . ARG B 1 222 ? 15.414  7.723   92.336  1.00 164.77 ?  231 ARG B HD2  1 
ATOM   8901  H HD3  . ARG B 1 222 ? 14.946  9.005   91.516  1.00 164.77 ?  231 ARG B HD3  1 
ATOM   8902  H HE   . ARG B 1 222 ? 13.406  9.378   93.193  1.00 185.88 ?  231 ARG B HE   1 
ATOM   8903  H HH11 . ARG B 1 222 ? 15.914  7.388   94.119  1.00 162.49 ?  231 ARG B HH11 1 
ATOM   8904  H HH12 . ARG B 1 222 ? 15.738  7.601   95.583  1.00 162.49 ?  231 ARG B HH12 1 
ATOM   8905  H HH21 . ARG B 1 222 ? 13.129  9.653   95.359  1.00 110.72 ?  231 ARG B HH21 1 
ATOM   8906  H HH22 . ARG B 1 222 ? 14.034  8.987   96.337  1.00 110.72 ?  231 ARG B HH22 1 
ATOM   8907  N N    . ILE B 1 223 ? 9.693   7.353   91.865  1.00 63.09  ?  232 ILE B N    1 
ATOM   8908  C CA   . ILE B 1 223 ? 8.937   6.657   92.907  1.00 64.08  ?  232 ILE B CA   1 
ATOM   8909  C C    . ILE B 1 223 ? 8.166   5.485   92.317  1.00 84.52  ?  232 ILE B C    1 
ATOM   8910  O O    . ILE B 1 223 ? 8.141   4.402   92.904  1.00 68.86  ?  232 ILE B O    1 
ATOM   8911  C CB   . ILE B 1 223 ? 7.966   7.625   93.615  1.00 66.58  ?  232 ILE B CB   1 
ATOM   8912  C CG1  . ILE B 1 223 ? 8.605   8.958   94.086  1.00 90.33  ?  232 ILE B CG1  1 
ATOM   8913  C CG2  . ILE B 1 223 ? 7.412   6.947   94.810  1.00 86.06  ?  232 ILE B CG2  1 
ATOM   8914  C CD1  . ILE B 1 223 ? 9.678   8.853   95.193  1.00 90.98  ?  232 ILE B CD1  1 
ATOM   8915  H H    . ILE B 1 223 ? 9.491   8.186   91.798  1.00 75.71  ?  232 ILE B H    1 
ATOM   8916  H HA   . ILE B 1 223 ? 9.554   6.309   93.569  1.00 76.90  ?  232 ILE B HA   1 
ATOM   8917  H HB   . ILE B 1 223 ? 7.237   7.829   93.009  1.00 79.90  ?  232 ILE B HB   1 
ATOM   8918  H HG12 . ILE B 1 223 ? 9.023   9.382   93.320  1.00 108.39 ?  232 ILE B HG12 1 
ATOM   8919  H HG13 . ILE B 1 223 ? 7.899   9.531   94.423  1.00 108.39 ?  232 ILE B HG13 1 
ATOM   8920  H HG21 . ILE B 1 223 ? 6.801   7.551   95.260  1.00 103.28 ?  232 ILE B HG21 1 
ATOM   8921  H HG22 . ILE B 1 223 ? 6.941   6.148   94.529  1.00 103.28 ?  232 ILE B HG22 1 
ATOM   8922  H HG23 . ILE B 1 223 ? 8.141   6.710   95.405  1.00 103.28 ?  232 ILE B HG23 1 
ATOM   8923  H HD11 . ILE B 1 223 ? 10.002  9.743   95.404  1.00 109.18 ?  232 ILE B HD11 1 
ATOM   8924  H HD12 . ILE B 1 223 ? 9.280   8.451   95.981  1.00 109.18 ?  232 ILE B HD12 1 
ATOM   8925  H HD13 . ILE B 1 223 ? 10.409  8.302   94.873  1.00 109.18 ?  232 ILE B HD13 1 
ATOM   8926  N N    . TYR B 1 224 ? 7.522   5.681   91.151  1.00 47.76  ?  233 TYR B N    1 
ATOM   8927  C CA   . TYR B 1 224 ? 6.688   4.654   90.525  1.00 49.70  ?  233 TYR B CA   1 
ATOM   8928  C C    . TYR B 1 224 ? 7.511   3.711   89.719  1.00 85.93  ?  233 TYR B C    1 
ATOM   8929  O O    . TYR B 1 224 ? 6.952   2.852   89.026  1.00 72.06  ?  233 TYR B O    1 
ATOM   8930  C CB   . TYR B 1 224 ? 5.596   5.260   89.629  1.00 103.09 ?  233 TYR B CB   1 
ATOM   8931  C CG   . TYR B 1 224 ? 4.590   6.072   90.396  1.00 98.47  ?  233 TYR B CG   1 
ATOM   8932  C CD1  . TYR B 1 224 ? 3.589   5.469   91.083  1.00 51.63  ?  233 TYR B CD1  1 
ATOM   8933  C CD2  . TYR B 1 224 ? 4.701   7.423   90.479  1.00 121.50 ?  233 TYR B CD2  1 
ATOM   8934  C CE1  . TYR B 1 224 ? 2.701   6.178   91.807  1.00 156.21 ?  233 TYR B CE1  1 
ATOM   8935  C CE2  . TYR B 1 224 ? 3.815   8.130   91.204  1.00 121.07 ?  233 TYR B CE2  1 
ATOM   8936  C CZ   . TYR B 1 224 ? 2.825   7.511   91.848  1.00 105.10 ?  233 TYR B CZ   1 
ATOM   8937  O OH   . TYR B 1 224 ? 2.005   8.294   92.570  1.00 59.76  ?  233 TYR B OH   1 
ATOM   8938  H H    . TYR B 1 224 ? 7.558   6.414   90.703  1.00 57.31  ?  233 TYR B H    1 
ATOM   8939  H HA   . TYR B 1 224 ? 6.248   4.142   91.222  1.00 59.64  ?  233 TYR B HA   1 
ATOM   8940  H HB2  . TYR B 1 224 ? 6.013   5.842   88.974  1.00 123.71 ?  233 TYR B HB2  1 
ATOM   8941  H HB3  . TYR B 1 224 ? 5.122   4.543   89.180  1.00 123.71 ?  233 TYR B HB3  1 
ATOM   8942  H HD1  . TYR B 1 224 ? 3.508   4.543   91.046  1.00 61.95  ?  233 TYR B HD1  1 
ATOM   8943  H HD2  . TYR B 1 224 ? 5.387   7.861   90.028  1.00 145.80 ?  233 TYR B HD2  1 
ATOM   8944  H HE1  . TYR B 1 224 ? 2.015   5.750   92.266  1.00 187.45 ?  233 TYR B HE1  1 
ATOM   8945  H HE2  . TYR B 1 224 ? 3.890   9.056   91.251  1.00 145.29 ?  233 TYR B HE2  1 
ATOM   8946  H HH   . TYR B 1 224 ? 1.434   7.823   92.968  1.00 71.71  ?  233 TYR B HH   1 
ATOM   8947  N N    . LEU B 1 225 ? 8.812   3.931   89.691  1.00 79.82  ?  234 LEU B N    1 
ATOM   8948  C CA   . LEU B 1 225 ? 9.672   2.941   89.119  1.00 59.82  ?  234 LEU B CA   1 
ATOM   8949  C C    . LEU B 1 225 ? 10.440  2.227   90.203  1.00 59.78  ?  234 LEU B C    1 
ATOM   8950  O O    . LEU B 1 225 ? 11.276  1.372   89.891  1.00 72.19  ?  234 LEU B O    1 
ATOM   8951  C CB   . LEU B 1 225 ? 10.588  3.572   88.129  1.00 38.68  ?  234 LEU B CB   1 
ATOM   8952  C CG   . LEU B 1 225 ? 10.006  4.374   86.967  1.00 45.63  ?  234 LEU B CG   1 
ATOM   8953  C CD1  . LEU B 1 225 ? 11.152  4.869   86.066  1.00 63.16  ?  234 LEU B CD1  1 
ATOM   8954  C CD2  . LEU B 1 225 ? 9.028   3.572   86.186  1.00 56.71  ?  234 LEU B CD2  1 
ATOM   8955  H H    . LEU B 1 225 ? 9.207   4.632   89.992  1.00 95.78  ?  234 LEU B H    1 
ATOM   8956  H HA   . LEU B 1 225 ? 9.132   2.284   88.652  1.00 71.79  ?  234 LEU B HA   1 
ATOM   8957  H HB2  . LEU B 1 225 ? 11.173  4.174   88.614  1.00 46.41  ?  234 LEU B HB2  1 
ATOM   8958  H HB3  . LEU B 1 225 ? 11.124  2.866   87.736  1.00 46.41  ?  234 LEU B HB3  1 
ATOM   8959  H HG   . LEU B 1 225 ? 9.544   5.151   87.320  1.00 54.76  ?  234 LEU B HG   1 
ATOM   8960  H HD11 . LEU B 1 225 ? 10.777  5.377   85.330  1.00 75.79  ?  234 LEU B HD11 1 
ATOM   8961  H HD12 . LEU B 1 225 ? 11.745  5.431   86.589  1.00 75.79  ?  234 LEU B HD12 1 
ATOM   8962  H HD13 . LEU B 1 225 ? 11.639  4.102   85.725  1.00 75.79  ?  234 LEU B HD13 1 
ATOM   8963  H HD21 . LEU B 1 225 ? 8.683   4.116   85.460  1.00 68.05  ?  234 LEU B HD21 1 
ATOM   8964  H HD22 . LEU B 1 225 ? 9.476   2.789   85.829  1.00 68.05  ?  234 LEU B HD22 1 
ATOM   8965  H HD23 . LEU B 1 225 ? 8.303   3.302   86.771  1.00 68.05  ?  234 LEU B HD23 1 
ATOM   8966  N N    . SER B 1 226 ? 10.156  2.533   91.470  1.00 42.69  ?  235 SER B N    1 
ATOM   8967  C CA   . SER B 1 226 ? 10.764  1.759   92.535  1.00 61.18  ?  235 SER B CA   1 
ATOM   8968  C C    . SER B 1 226 ? 10.151  0.376   92.617  1.00 70.85  ?  235 SER B C    1 
ATOM   8969  O O    . SER B 1 226 ? 8.991   0.171   92.267  1.00 83.55  ?  235 SER B O    1 
ATOM   8970  C CB   . SER B 1 226 ? 10.625  2.499   93.834  1.00 74.31  ?  235 SER B CB   1 
ATOM   8971  O OG   . SER B 1 226 ? 11.213  3.759   93.626  1.00 90.96  ?  235 SER B OG   1 
ATOM   8972  H H    . SER B 1 226 ? 9.631   3.163   91.728  1.00 51.22  ?  235 SER B H    1 
ATOM   8973  H HA   . SER B 1 226 ? 11.710  1.656   92.349  1.00 73.41  ?  235 SER B HA   1 
ATOM   8974  H HB2  . SER B 1 226 ? 9.686   2.605   94.055  1.00 89.17  ?  235 SER B HB2  1 
ATOM   8975  H HB3  . SER B 1 226 ? 11.096  2.026   94.537  1.00 89.17  ?  235 SER B HB3  1 
ATOM   8976  H HG   . SER B 1 226 ? 11.162  4.219   94.327  1.00 109.15 ?  235 SER B HG   1 
ATOM   8977  N N    . GLY B 1 227 ? 10.980  -0.588  92.989  1.00 94.75  ?  236 GLY B N    1 
ATOM   8978  C CA   . GLY B 1 227 ? 10.520  -1.939  93.226  1.00 51.28  ?  236 GLY B CA   1 
ATOM   8979  C C    . GLY B 1 227 ? 10.715  -2.389  94.656  1.00 70.87  ?  236 GLY B C    1 
ATOM   8980  O O    . GLY B 1 227 ? 10.963  -1.563  95.534  1.00 73.18  ?  236 GLY B O    1 
ATOM   8981  H H    . GLY B 1 227 ? 11.824  -0.480  93.111  1.00 113.70 ?  236 GLY B H    1 
ATOM   8982  H HA2  . GLY B 1 227 ? 9.576   -1.999  93.014  1.00 61.54  ?  236 GLY B HA2  1 
ATOM   8983  H HA3  . GLY B 1 227 ? 11.003  -2.549  92.646  1.00 61.54  ?  236 GLY B HA3  1 
ATOM   8984  N N    . TRP B 1 228 ? 10.678  -3.699  94.902  1.00 105.94 ?  237 TRP B N    1 
ATOM   8985  C CA   . TRP B 1 228 ? 10.630  -4.240  96.267  1.00 105.02 ?  237 TRP B CA   1 
ATOM   8986  C C    . TRP B 1 228 ? 11.668  -5.356  96.389  1.00 119.73 ?  237 TRP B C    1 
ATOM   8987  O O    . TRP B 1 228 ? 11.385  -6.466  96.839  1.00 134.37 ?  237 TRP B O    1 
ATOM   8988  C CB   . TRP B 1 228 ? 9.197   -4.714  96.643  1.00 83.86  ?  237 TRP B CB   1 
ATOM   8989  C CG   . TRP B 1 228 ? 8.413   -5.252  95.457  1.00 68.37  ?  237 TRP B CG   1 
ATOM   8990  C CD1  . TRP B 1 228 ? 8.394   -6.555  95.036  1.00 96.16  ?  237 TRP B CD1  1 
ATOM   8991  C CD2  . TRP B 1 228 ? 7.576   -4.518  94.518  1.00 66.79  ?  237 TRP B CD2  1 
ATOM   8992  N NE1  . TRP B 1 228 ? 7.633   -6.682  93.907  1.00 55.81  ?  237 TRP B NE1  1 
ATOM   8993  C CE2  . TRP B 1 228 ? 7.116   -5.456  93.560  1.00 67.58  ?  237 TRP B CE2  1 
ATOM   8994  C CE3  . TRP B 1 228 ? 7.171   -3.160  94.392  1.00 53.98  ?  237 TRP B CE3  1 
ATOM   8995  C CZ2  . TRP B 1 228 ? 6.275   -5.090  92.476  1.00 59.63  ?  237 TRP B CZ2  1 
ATOM   8996  C CZ3  . TRP B 1 228 ? 6.351   -2.805  93.326  1.00 52.69  ?  237 TRP B CZ3  1 
ATOM   8997  C CH2  . TRP B 1 228 ? 5.920   -3.775  92.374  1.00 51.50  ?  237 TRP B CH2  1 
ATOM   8998  H H    . TRP B 1 228 ? 10.679  -4.303  94.290  1.00 127.13 ?  237 TRP B H    1 
ATOM   8999  H HA   . TRP B 1 228 ? 10.878  -3.537  96.888  1.00 126.03 ?  237 TRP B HA   1 
ATOM   9000  H HB2  . TRP B 1 228 ? 9.263   -5.422  97.302  1.00 100.63 ?  237 TRP B HB2  1 
ATOM   9001  H HB3  . TRP B 1 228 ? 8.703   -3.965  97.011  1.00 100.63 ?  237 TRP B HB3  1 
ATOM   9002  H HD1  . TRP B 1 228 ? 8.859   -7.251  95.442  1.00 115.39 ?  237 TRP B HD1  1 
ATOM   9003  H HE1  . TRP B 1 228 ? 7.496   -7.417  93.481  1.00 66.97  ?  237 TRP B HE1  1 
ATOM   9004  H HE3  . TRP B 1 228 ? 7.478   -2.517  94.989  1.00 64.78  ?  237 TRP B HE3  1 
ATOM   9005  H HZ2  . TRP B 1 228 ? 5.969   -5.723  91.866  1.00 71.56  ?  237 TRP B HZ2  1 
ATOM   9006  H HZ3  . TRP B 1 228 ? 6.089   -1.918  93.226  1.00 63.23  ?  237 TRP B HZ3  1 
ATOM   9007  H HH2  . TRP B 1 228 ? 5.350   -3.513  91.688  1.00 61.80  ?  237 TRP B HH2  1 
ATOM   9008  N N    . LYS B 1 229 ? 12.910  -5.049  95.986  1.00 94.73  ?  238 LYS B N    1 
ATOM   9009  C CA   . LYS B 1 229 ? 14.066  -5.925  96.170  1.00 75.82  ?  238 LYS B CA   1 
ATOM   9010  C C    . LYS B 1 229 ? 15.085  -5.100  96.921  1.00 62.23  ?  238 LYS B C    1 
ATOM   9011  O O    . LYS B 1 229 ? 15.581  -4.089  96.409  1.00 77.87  ?  238 LYS B O    1 
ATOM   9012  C CB   . LYS B 1 229 ? 14.638  -6.414  94.828  1.00 65.30  ?  238 LYS B CB   1 
ATOM   9013  C CG   . LYS B 1 229 ? 15.744  -7.473  94.942  1.00 60.09  ?  238 LYS B CG   1 
ATOM   9014  H H    . LYS B 1 229 ? 13.108  -4.312  95.591  1.00 113.68 ?  238 LYS B H    1 
ATOM   9015  H HA   . LYS B 1 229 ? 13.820  -6.693  96.709  1.00 90.99  ?  238 LYS B HA   1 
ATOM   9016  H HB2  . LYS B 1 229 ? 13.916  -6.800  94.308  1.00 78.36  ?  238 LYS B HB2  1 
ATOM   9017  H HB3  . LYS B 1 229 ? 15.010  -5.653  94.355  1.00 78.36  ?  238 LYS B HB3  1 
ATOM   9018  H HG2  . LYS B 1 229 ? 16.544  -7.057  95.302  1.00 72.10  ?  238 LYS B HG2  1 
ATOM   9019  H HG3  . LYS B 1 229 ? 15.444  -8.181  95.533  1.00 72.10  ?  238 LYS B HG3  1 
ATOM   9020  N N    . GLY B 1 230 ? 15.360  -5.485  98.151  1.00 67.91  ?  239 GLY B N    1 
ATOM   9021  C CA   . GLY B 1 230 ? 16.259  -4.645  98.901  1.00 88.12  ?  239 GLY B CA   1 
ATOM   9022  C C    . GLY B 1 230 ? 15.675  -3.294  99.180  1.00 94.94  ?  239 GLY B C    1 
ATOM   9023  O O    . GLY B 1 230 ? 16.411  -2.318  99.298  1.00 118.18 ?  239 GLY B O    1 
ATOM   9024  H H    . GLY B 1 230 ? 15.059  -6.183  98.553  1.00 81.50  ?  239 GLY B H    1 
ATOM   9025  H HA2  . GLY B 1 230 ? 16.469  -5.070  99.747  1.00 105.74 ?  239 GLY B HA2  1 
ATOM   9026  H HA3  . GLY B 1 230 ? 17.082  -4.527  98.402  1.00 105.74 ?  239 GLY B HA3  1 
ATOM   9027  N N    . ASN B 1 231 ? 14.408  -3.196  99.191  1.00 107.10 ?  240 ASN B N    1 
ATOM   9028  C CA   . ASN B 1 231 ? 13.779  -1.931  99.485  1.00 89.50  ?  240 ASN B CA   1 
ATOM   9029  C C    . ASN B 1 231 ? 13.233  -1.932  100.902 1.00 93.18  ?  240 ASN B C    1 
ATOM   9030  O O    . ASN B 1 231 ? 12.484  -2.851  101.280 1.00 118.46 ?  240 ASN B O    1 
ATOM   9031  C CB   . ASN B 1 231 ? 12.673  -1.643  98.483  1.00 80.53  ?  240 ASN B CB   1 
ATOM   9032  C CG   . ASN B 1 231 ? 12.170  -0.254  98.594  1.00 67.75  ?  240 ASN B CG   1 
ATOM   9033  O OD1  . ASN B 1 231 ? 12.244  0.347   99.677  1.00 67.43  ?  240 ASN B OD1  1 
ATOM   9034  N ND2  . ASN B 1 231 ? 11.646  0.279   97.491  1.00 69.34  ?  240 ASN B ND2  1 
ATOM   9035  H H    . ASN B 1 231 ? 13.862  -3.841  99.032  1.00 128.52 ?  240 ASN B H    1 
ATOM   9036  H HA   . ASN B 1 231 ? 14.440  -1.224  99.417  1.00 107.40 ?  240 ASN B HA   1 
ATOM   9037  H HB2  . ASN B 1 231 ? 13.016  -1.769  97.584  1.00 96.64  ?  240 ASN B HB2  1 
ATOM   9038  H HB3  . ASN B 1 231 ? 11.931  -2.246  98.645  1.00 96.64  ?  240 ASN B HB3  1 
ATOM   9039  H HD21 . ASN B 1 231 ? 11.341  1.083   97.506  1.00 83.21  ?  240 ASN B HD21 1 
ATOM   9040  H HD22 . ASN B 1 231 ? 11.613  -0.180  96.765  1.00 83.21  ?  240 ASN B HD22 1 
ATOM   9041  N N    . PRO B 1 232 ? 13.605  -0.936  101.709 1.00 87.63  ?  241 PRO B N    1 
ATOM   9042  C CA   . PRO B 1 232 ? 13.082  -0.859  103.082 1.00 120.89 ?  241 PRO B CA   1 
ATOM   9043  C C    . PRO B 1 232 ? 11.571  -0.806  103.171 1.00 120.73 ?  241 PRO B C    1 
ATOM   9044  O O    . PRO B 1 232 ? 11.011  -1.329  104.142 1.00 103.59 ?  241 PRO B O    1 
ATOM   9045  C CB   . PRO B 1 232 ? 13.719  0.425   103.627 1.00 128.44 ?  241 PRO B CB   1 
ATOM   9046  C CG   . PRO B 1 232 ? 14.932  0.619   102.839 1.00 108.72 ?  241 PRO B CG   1 
ATOM   9047  C CD   . PRO B 1 232 ? 14.670  0.049   101.477 1.00 78.98  ?  241 PRO B CD   1 
ATOM   9048  H HA   . PRO B 1 232 ? 13.402  -1.613  103.601 1.00 145.07 ?  241 PRO B HA   1 
ATOM   9049  H HB2  . PRO B 1 232 ? 13.109  1.169   103.505 1.00 154.13 ?  241 PRO B HB2  1 
ATOM   9050  H HB3  . PRO B 1 232 ? 13.935  0.309   104.565 1.00 154.13 ?  241 PRO B HB3  1 
ATOM   9051  H HG2  . PRO B 1 232 ? 15.125  1.568   102.776 1.00 130.46 ?  241 PRO B HG2  1 
ATOM   9052  H HG3  . PRO B 1 232 ? 15.668  0.153   103.264 1.00 130.46 ?  241 PRO B HG3  1 
ATOM   9053  H HD2  . PRO B 1 232 ? 14.362  0.744   100.874 1.00 94.77  ?  241 PRO B HD2  1 
ATOM   9054  H HD3  . PRO B 1 232 ? 15.466  -0.389  101.137 1.00 94.77  ?  241 PRO B HD3  1 
ATOM   9055  N N    . GLN B 1 233 ? 10.894  -0.164  102.225 1.00 147.57 ?  242 GLN B N    1 
ATOM   9056  C CA   . GLN B 1 233 ? 9.453   -0.012  102.343 1.00 111.90 ?  242 GLN B CA   1 
ATOM   9057  C C    . GLN B 1 233 ? 8.695   -1.283  102.027 1.00 132.20 ?  242 GLN B C    1 
ATOM   9058  O O    . GLN B 1 233 ? 7.496   -1.356  102.318 1.00 119.43 ?  242 GLN B O    1 
ATOM   9059  C CB   . GLN B 1 233 ? 8.952   1.067   101.397 1.00 126.07 ?  242 GLN B CB   1 
ATOM   9060  C CG   . GLN B 1 233 ? 9.735   2.335   101.421 1.00 154.63 ?  242 GLN B CG   1 
ATOM   9061  C CD   . GLN B 1 233 ? 9.206   3.346   100.421 1.00 175.92 ?  242 GLN B CD   1 
ATOM   9062  O OE1  . GLN B 1 233 ? 8.147   3.945   100.622 1.00 182.84 ?  242 GLN B OE1  1 
ATOM   9063  N NE2  . GLN B 1 233 ? 9.939   3.530   99.324  1.00 182.94 ?  242 GLN B NE2  1 
ATOM   9064  H H    . GLN B 1 233 ? 11.238  0.186   101.519 1.00 177.08 ?  242 GLN B H    1 
ATOM   9065  H HA   . GLN B 1 233 ? 9.234   0.254   103.250 1.00 134.28 ?  242 GLN B HA   1 
ATOM   9066  H HB2  . GLN B 1 233 ? 8.981   0.721   100.491 1.00 151.29 ?  242 GLN B HB2  1 
ATOM   9067  H HB3  . GLN B 1 233 ? 8.037   1.283   101.633 1.00 151.29 ?  242 GLN B HB3  1 
ATOM   9068  H HG2  . GLN B 1 233 ? 9.680   2.728   102.306 1.00 185.56 ?  242 GLN B HG2  1 
ATOM   9069  H HG3  . GLN B 1 233 ? 10.659  2.143   101.197 1.00 185.56 ?  242 GLN B HG3  1 
ATOM   9070  H HE21 . GLN B 1 233 ? 10.668  3.087   99.215  1.00 219.53 ?  242 GLN B HE21 1 
ATOM   9071  H HE22 . GLN B 1 233 ? 9.683   4.092   98.725  1.00 219.53 ?  242 GLN B HE22 1 
ATOM   9072  N N    . LEU B 1 234 ? 9.355   -2.282  101.453 1.00 119.11 ?  243 LEU B N    1 
ATOM   9073  C CA   . LEU B 1 234 ? 8.740   -3.573  101.228 1.00 100.50 ?  243 LEU B CA   1 
ATOM   9074  C C    . LEU B 1 234 ? 9.772   -4.646  101.554 1.00 103.82 ?  243 LEU B C    1 
ATOM   9075  O O    . LEU B 1 234 ? 10.125  -5.487  100.737 1.00 159.91 ?  243 LEU B O    1 
ATOM   9076  C CB   . LEU B 1 234 ? 8.205   -3.666  99.800  1.00 85.91  ?  243 LEU B CB   1 
ATOM   9077  C CG   . LEU B 1 234 ? 6.947   -2.832  99.550  1.00 91.34  ?  243 LEU B CG   1 
ATOM   9078  C CD1  . LEU B 1 234 ? 6.590   -2.812  98.096  1.00 81.21  ?  243 LEU B CD1  1 
ATOM   9079  C CD2  . LEU B 1 234 ? 5.773   -3.399  100.330 1.00 95.26  ?  243 LEU B CD2  1 
ATOM   9080  H H    . LEU B 1 234 ? 10.170  -2.232  101.184 1.00 142.93 ?  243 LEU B H    1 
ATOM   9081  H HA   . LEU B 1 234 ? 7.992   -3.679  101.836 1.00 120.59 ?  243 LEU B HA   1 
ATOM   9082  H HB2  . LEU B 1 234 ? 8.891   -3.356  99.189  1.00 103.09 ?  243 LEU B HB2  1 
ATOM   9083  H HB3  . LEU B 1 234 ? 7.989   -4.592  99.607  1.00 103.09 ?  243 LEU B HB3  1 
ATOM   9084  H HG   . LEU B 1 234 ? 7.099   -1.920  99.842  1.00 109.60 ?  243 LEU B HG   1 
ATOM   9085  H HD11 . LEU B 1 234 ? 5.790   -2.276  97.975  1.00 97.46  ?  243 LEU B HD11 1 
ATOM   9086  H HD12 . LEU B 1 234 ? 7.326   -2.426  97.595  1.00 97.46  ?  243 LEU B HD12 1 
ATOM   9087  H HD13 . LEU B 1 234 ? 6.427   -3.721  97.798  1.00 97.46  ?  243 LEU B HD13 1 
ATOM   9088  H HD21 . LEU B 1 234 ? 4.988   -2.857  100.157 1.00 114.32 ?  243 LEU B HD21 1 
ATOM   9089  H HD22 . LEU B 1 234 ? 5.615   -4.312  100.042 1.00 114.32 ?  243 LEU B HD22 1 
ATOM   9090  H HD23 . LEU B 1 234 ? 5.986   -3.382  101.276 1.00 114.32 ?  243 LEU B HD23 1 
ATOM   9091  N N    . SER B 1 235 ? 10.205  -4.634  102.813 1.00 105.47 ?  244 SER B N    1 
ATOM   9092  C CA   . SER B 1 235 ? 11.384  -5.390  103.216 1.00 113.21 ?  244 SER B CA   1 
ATOM   9093  C C    . SER B 1 235 ? 11.357  -6.809  102.669 1.00 126.28 ?  244 SER B C    1 
ATOM   9094  O O    . SER B 1 235 ? 12.340  -7.268  102.077 1.00 147.81 ?  244 SER B O    1 
ATOM   9095  C CB   . SER B 1 235 ? 11.492  -5.396  104.736 1.00 117.25 ?  244 SER B CB   1 
ATOM   9096  O OG   . SER B 1 235 ? 10.236  -5.708  105.304 1.00 161.41 ?  244 SER B OG   1 
ATOM   9097  H H    . SER B 1 235 ? 9.833   -4.196  103.452 1.00 126.57 ?  244 SER B H    1 
ATOM   9098  H HA   . SER B 1 235 ? 12.174  -4.950  102.863 1.00 135.85 ?  244 SER B HA   1 
ATOM   9099  H HB2  . SER B 1 235 ? 12.140  -6.066  105.006 1.00 140.71 ?  244 SER B HB2  1 
ATOM   9100  H HB3  . SER B 1 235 ? 11.770  -4.518  105.039 1.00 140.71 ?  244 SER B HB3  1 
ATOM   9101  H HG   . SER B 1 235 ? 10.293  -5.713  106.142 1.00 193.70 ?  244 SER B HG   1 
ATOM   9102  N N    . ASP B 1 236 ? 10.225  -7.499  102.784 1.00 117.20 ?  245 ASP B N    1 
ATOM   9103  C CA   . ASP B 1 236 ? 10.172  -8.894  102.368 1.00 110.44 ?  245 ASP B CA   1 
ATOM   9104  C C    . ASP B 1 236 ? 9.593   -9.059  100.993 1.00 112.85 ?  245 ASP B C    1 
ATOM   9105  O O    . ASP B 1 236 ? 9.366   -10.190 100.560 1.00 100.56 ?  245 ASP B O    1 
ATOM   9106  C CB   . ASP B 1 236 ? 9.365   -9.735  103.336 1.00 103.57 ?  245 ASP B CB   1 
ATOM   9107  C CG   . ASP B 1 236 ? 9.966   -9.748  104.696 1.00 103.12 ?  245 ASP B CG   1 
ATOM   9108  O OD1  . ASP B 1 236 ? 11.065  -10.343 104.756 1.00 102.01 ?  245 ASP B OD1  1 
ATOM   9109  O OD2  . ASP B 1 236 ? 9.352   -9.251  105.684 1.00 106.93 -1 245 ASP B OD2  1 
ATOM   9110  H H    . ASP B 1 236 ? 9.486   -7.188  103.094 1.00 140.64 ?  245 ASP B H    1 
ATOM   9111  H HA   . ASP B 1 236 ? 11.075  -9.247  102.353 1.00 132.53 ?  245 ASP B HA   1 
ATOM   9112  H HB2  . ASP B 1 236 ? 8.469   -9.370  103.405 1.00 124.28 ?  245 ASP B HB2  1 
ATOM   9113  H HB3  . ASP B 1 236 ? 9.331   -10.649 103.012 1.00 124.28 ?  245 ASP B HB3  1 
ATOM   9114  N N    . GLY B 1 237 ? 9.331   -7.962  100.315 1.00 114.39 ?  246 GLY B N    1 
ATOM   9115  C CA   . GLY B 1 237 ? 8.746   -7.998  99.008  1.00 97.71  ?  246 GLY B CA   1 
ATOM   9116  C C    . GLY B 1 237 ? 7.249   -7.810  99.064  1.00 102.50 ?  246 GLY B C    1 
ATOM   9117  O O    . GLY B 1 237 ? 6.657   -7.374  100.053 1.00 104.70 ?  246 GLY B O    1 
ATOM   9118  H H    . GLY B 1 237 ? 9.489   -7.167  100.604 1.00 137.27 ?  246 GLY B H    1 
ATOM   9119  H HA2  . GLY B 1 237 ? 9.127   -7.293  98.462  1.00 117.25 ?  246 GLY B HA2  1 
ATOM   9120  H HA3  . GLY B 1 237 ? 8.936   -8.852  98.590  1.00 117.25 ?  246 GLY B HA3  1 
ATOM   9121  N N    . LEU B 1 238 ? 6.630   -8.156  97.962  1.00 91.67  ?  247 LEU B N    1 
ATOM   9122  C CA   . LEU B 1 238 ? 5.201   -8.028  97.820  1.00 89.99  ?  247 LEU B CA   1 
ATOM   9123  C C    . LEU B 1 238 ? 4.627   -9.424  97.839  1.00 124.80 ?  247 LEU B C    1 
ATOM   9124  O O    . LEU B 1 238 ? 5.083   -10.292 97.094  1.00 149.59 ?  247 LEU B O    1 
ATOM   9125  C CB   . LEU B 1 238 ? 4.892   -7.333  96.508  1.00 104.24 ?  247 LEU B CB   1 
ATOM   9126  C CG   . LEU B 1 238 ? 3.504   -6.821  96.263  1.00 100.72 ?  247 LEU B CG   1 
ATOM   9127  C CD1  . LEU B 1 238 ? 3.293   -5.638  97.154  1.00 72.40  ?  247 LEU B CD1  1 
ATOM   9128  C CD2  . LEU B 1 238 ? 3.436   -6.489  94.806  1.00 152.17 ?  247 LEU B CD2  1 
ATOM   9129  H H    . LEU B 1 238 ? 7.022   -8.476  97.267  1.00 110.00 ?  247 LEU B H    1 
ATOM   9130  H HA   . LEU B 1 238 ? 4.831   -7.514  98.554  1.00 107.99 ?  247 LEU B HA   1 
ATOM   9131  H HB2  . LEU B 1 238 ? 5.487   -6.570  96.432  1.00 125.09 ?  247 LEU B HB2  1 
ATOM   9132  H HB3  . LEU B 1 238 ? 5.089   -7.956  95.791  1.00 125.09 ?  247 LEU B HB3  1 
ATOM   9133  H HG   . LEU B 1 238 ? 2.848   -7.506  96.471  1.00 120.87 ?  247 LEU B HG   1 
ATOM   9134  H HD11 . LEU B 1 238 ? 2.399   -5.291  97.012  1.00 86.88  ?  247 LEU B HD11 1 
ATOM   9135  H HD12 . LEU B 1 238 ? 3.398   -5.916  98.078  1.00 86.88  ?  247 LEU B HD12 1 
ATOM   9136  H HD13 . LEU B 1 238 ? 3.951   -4.959  96.937  1.00 86.88  ?  247 LEU B HD13 1 
ATOM   9137  H HD21 . LEU B 1 238 ? 2.550   -6.152  94.600  1.00 182.61 ?  247 LEU B HD21 1 
ATOM   9138  H HD22 . LEU B 1 238 ? 4.103   -5.813  94.606  1.00 182.61 ?  247 LEU B HD22 1 
ATOM   9139  H HD23 . LEU B 1 238 ? 3.614   -7.291  94.291  1.00 182.61 ?  247 LEU B HD23 1 
ATOM   9140  N N    . VAL B 1 239 ? 3.633   -9.647  98.679  1.00 157.76 ?  248 VAL B N    1 
ATOM   9141  C CA   . VAL B 1 239 ? 2.899   -10.901 98.594  1.00 142.21 ?  248 VAL B CA   1 
ATOM   9142  C C    . VAL B 1 239 ? 1.882   -10.762 97.473  1.00 118.36 ?  248 VAL B C    1 
ATOM   9143  O O    . VAL B 1 239 ? 1.031   -9.862  97.491  1.00 84.87  ?  248 VAL B O    1 
ATOM   9144  C CB   . VAL B 1 239 ? 2.240   -11.290 99.929  1.00 138.43 ?  248 VAL B CB   1 
ATOM   9145  C CG1  . VAL B 1 239 ? 1.923   -10.094 100.774 1.00 133.82 ?  248 VAL B CG1  1 
ATOM   9146  C CG2  . VAL B 1 239 ? 0.979   -12.154 99.694  1.00 128.81 ?  248 VAL B CG2  1 
ATOM   9147  H H    . VAL B 1 239 ? 3.366   -9.106  99.292  1.00 189.31 ?  248 VAL B H    1 
ATOM   9148  H HA   . VAL B 1 239 ? 3.515   -11.610 98.350  1.00 170.65 ?  248 VAL B HA   1 
ATOM   9149  H HB   . VAL B 1 239 ? 2.869   -11.833 100.428 1.00 166.12 ?  248 VAL B HB   1 
ATOM   9150  H HG11 . VAL B 1 239 ? 1.511   -10.392 101.600 1.00 160.58 ?  248 VAL B HG11 1 
ATOM   9151  H HG12 . VAL B 1 239 ? 2.746   -9.618  100.967 1.00 160.58 ?  248 VAL B HG12 1 
ATOM   9152  H HG13 . VAL B 1 239 ? 1.313   -9.517  100.289 1.00 160.58 ?  248 VAL B HG13 1 
ATOM   9153  H HG21 . VAL B 1 239 ? 0.589   -12.381 100.552 1.00 154.57 ?  248 VAL B HG21 1 
ATOM   9154  H HG22 . VAL B 1 239 ? 0.344   -11.648 99.165  1.00 154.57 ?  248 VAL B HG22 1 
ATOM   9155  H HG23 . VAL B 1 239 ? 1.235   -12.962 99.222  1.00 154.57 ?  248 VAL B HG23 1 
ATOM   9156  N N    . TYR B 1 240 ? 1.956   -11.677 96.511  1.00 86.26  ?  249 TYR B N    1 
ATOM   9157  C CA   . TYR B 1 240 ? 1.005   -11.724 95.403  1.00 90.71  ?  249 TYR B CA   1 
ATOM   9158  C C    . TYR B 1 240 ? -0.161  -12.598 95.847  1.00 117.03 ?  249 TYR B C    1 
ATOM   9159  O O    . TYR B 1 240 ? -0.170  -13.814 95.678  1.00 111.35 ?  249 TYR B O    1 
ATOM   9160  C CB   . TYR B 1 240 ? 1.700   -12.238 94.152  1.00 89.55  ?  249 TYR B CB   1 
ATOM   9161  C CG   . TYR B 1 240 ? 2.804   -11.268 93.658  1.00 87.66  ?  249 TYR B CG   1 
ATOM   9162  C CD1  . TYR B 1 240 ? 4.044   -11.195 94.290  1.00 86.60  ?  249 TYR B CD1  1 
ATOM   9163  C CD2  . TYR B 1 240 ? 2.594   -10.419 92.565  1.00 62.15  ?  249 TYR B CD2  1 
ATOM   9164  C CE1  . TYR B 1 240 ? 5.008   -10.321 93.837  1.00 73.60  ?  249 TYR B CE1  1 
ATOM   9165  C CE2  . TYR B 1 240 ? 3.537   -9.554  92.143  1.00 145.51 ?  249 TYR B CE2  1 
ATOM   9166  C CZ   . TYR B 1 240 ? 4.732   -9.511  92.770  1.00 100.16 ?  249 TYR B CZ   1 
ATOM   9167  O OH   . TYR B 1 240 ? 5.654   -8.636  92.297  1.00 72.45  ?  249 TYR B OH   1 
ATOM   9168  H H    . TYR B 1 240 ? 2.557   -12.292 96.477  1.00 103.52 ?  249 TYR B H    1 
ATOM   9169  H HA   . TYR B 1 240 ? 0.670   -10.831 95.224  1.00 108.85 ?  249 TYR B HA   1 
ATOM   9170  H HB2  . TYR B 1 240 ? 2.115   -13.093 94.347  1.00 107.46 ?  249 TYR B HB2  1 
ATOM   9171  H HB3  . TYR B 1 240 ? 1.046   -12.338 93.443  1.00 107.46 ?  249 TYR B HB3  1 
ATOM   9172  H HD1  . TYR B 1 240 ? 4.224   -11.744 95.018  1.00 103.92 ?  249 TYR B HD1  1 
ATOM   9173  H HD2  . TYR B 1 240 ? 1.772   -10.437 92.130  1.00 74.58  ?  249 TYR B HD2  1 
ATOM   9174  H HE1  . TYR B 1 240 ? 5.834   -10.273 94.261  1.00 88.32  ?  249 TYR B HE1  1 
ATOM   9175  H HE2  . TYR B 1 240 ? 3.373   -9.003  91.412  1.00 174.62 ?  249 TYR B HE2  1 
ATOM   9176  H HH   . TYR B 1 240 ? 5.339   -8.213  91.643  1.00 86.93  ?  249 TYR B HH   1 
ATOM   9177  N N    . GLU B 1 241 ? -1.156  -11.947 96.438  1.00 106.88 ?  250 GLU B N    1 
ATOM   9178  C CA   . GLU B 1 241 ? -2.215  -12.639 97.149  1.00 118.27 ?  250 GLU B CA   1 
ATOM   9179  C C    . GLU B 1 241 ? -2.775  -13.799 96.350  1.00 151.98 ?  250 GLU B C    1 
ATOM   9180  O O    . GLU B 1 241 ? -3.195  -13.645 95.202  1.00 127.07 ?  250 GLU B O    1 
ATOM   9181  C CB   . GLU B 1 241 ? -3.331  -11.657 97.480  1.00 155.54 ?  250 GLU B CB   1 
ATOM   9182  C CG   . GLU B 1 241 ? -4.433  -12.234 98.345  1.00 157.98 ?  250 GLU B CG   1 
ATOM   9183  C CD   . GLU B 1 241 ? -5.570  -11.249 98.596  1.00 128.36 ?  250 GLU B CD   1 
ATOM   9184  O OE1  . GLU B 1 241 ? -6.443  -11.077 97.711  1.00 118.10 ?  250 GLU B OE1  1 
ATOM   9185  O OE2  . GLU B 1 241 ? -5.577  -10.631 99.680  1.00 198.52 -1 250 GLU B OE2  1 
ATOM   9186  H H    . GLU B 1 241 ? -1.239  -11.091 96.440  1.00 128.26 ?  250 GLU B H    1 
ATOM   9187  H HA   . GLU B 1 241 ? -1.863  -12.989 97.983  1.00 141.93 ?  250 GLU B HA   1 
ATOM   9188  H HB2  . GLU B 1 241 ? -2.950  -10.901 97.953  1.00 186.65 ?  250 GLU B HB2  1 
ATOM   9189  H HB3  . GLU B 1 241 ? -3.735  -11.355 96.651  1.00 186.65 ?  250 GLU B HB3  1 
ATOM   9190  H HG2  . GLU B 1 241 ? -4.805  -13.014 97.904  1.00 189.58 ?  250 GLU B HG2  1 
ATOM   9191  H HG3  . GLU B 1 241 ? -4.060  -12.486 99.205  1.00 189.58 ?  250 GLU B HG3  1 
ATOM   9192  N N    . GLY B 1 242 ? -2.773  -14.966 96.979  1.00 105.33 ?  251 GLY B N    1 
ATOM   9193  C CA   . GLY B 1 242 ? -3.394  -16.136 96.427  1.00 122.76 ?  251 GLY B CA   1 
ATOM   9194  C C    . GLY B 1 242 ? -2.540  -16.900 95.458  1.00 124.02 ?  251 GLY B C    1 
ATOM   9195  O O    . GLY B 1 242 ? -2.844  -18.068 95.174  1.00 185.33 ?  251 GLY B O    1 
ATOM   9196  H H    . GLY B 1 242 ? -2.407  -15.098 97.746  1.00 126.39 ?  251 GLY B H    1 
ATOM   9197  H HA2  . GLY B 1 242 ? -3.636  -16.735 97.150  1.00 147.31 ?  251 GLY B HA2  1 
ATOM   9198  H HA3  . GLY B 1 242 ? -4.207  -15.874 95.968  1.00 147.31 ?  251 GLY B HA3  1 
ATOM   9199  N N    . PHE B 1 243 ? -1.458  -16.305 94.974  1.00 115.94 ?  252 PHE B N    1 
ATOM   9200  C CA   . PHE B 1 243 ? -0.520  -16.982 94.103  1.00 147.45 ?  252 PHE B CA   1 
ATOM   9201  C C    . PHE B 1 243 ? 0.700   -17.493 94.848  1.00 146.28 ?  252 PHE B C    1 
ATOM   9202  O O    . PHE B 1 243 ? 1.197   -18.578 94.546  1.00 107.22 ?  252 PHE B O    1 
ATOM   9203  C CB   . PHE B 1 243 ? -0.115  -16.032 92.998  1.00 97.94  ?  252 PHE B CB   1 
ATOM   9204  C CG   . PHE B 1 243 ? 0.469   -16.707 91.815  1.00 84.20  ?  252 PHE B CG   1 
ATOM   9205  C CD1  . PHE B 1 243 ? -0.310  -17.063 90.738  1.00 72.09  ?  252 PHE B CD1  1 
ATOM   9206  C CD2  . PHE B 1 243 ? 1.840   -16.972 91.765  1.00 99.48  ?  252 PHE B CD2  1 
ATOM   9207  C CE1  . PHE B 1 243 ? 0.276   -17.708 89.618  1.00 95.00  ?  252 PHE B CE1  1 
ATOM   9208  C CE2  . PHE B 1 243 ? 2.420   -17.603 90.658  1.00 78.62  ?  252 PHE B CE2  1 
ATOM   9209  C CZ   . PHE B 1 243 ? 1.643   -17.968 89.594  1.00 83.36  ?  252 PHE B CZ   1 
ATOM   9210  H H    . PHE B 1 243 ? -1.244  -15.489 95.143  1.00 139.13 ?  252 PHE B H    1 
ATOM   9211  H HA   . PHE B 1 243 ? -0.961  -17.744 93.696  1.00 176.94 ?  252 PHE B HA   1 
ATOM   9212  H HB2  . PHE B 1 243 ? -0.899  -15.543 92.704  1.00 117.53 ?  252 PHE B HB2  1 
ATOM   9213  H HB3  . PHE B 1 243 ? 0.547   -15.414 93.344  1.00 117.53 ?  252 PHE B HB3  1 
ATOM   9214  H HD1  . PHE B 1 243 ? -1.225  -16.895 90.751  1.00 86.51  ?  252 PHE B HD1  1 
ATOM   9215  H HD2  . PHE B 1 243 ? 2.377   -16.732 92.485  1.00 119.38 ?  252 PHE B HD2  1 
ATOM   9216  H HE1  . PHE B 1 243 ? -0.255  -17.951 88.894  1.00 114.00 ?  252 PHE B HE1  1 
ATOM   9217  H HE2  . PHE B 1 243 ? 3.334   -17.776 90.648  1.00 94.35  ?  252 PHE B HE2  1 
ATOM   9218  H HZ   . PHE B 1 243 ? 2.027   -18.386 88.857  1.00 100.03 ?  252 PHE B HZ   1 
ATOM   9219  N N    . TRP B 1 244 ? 1.276   -16.687 95.721  1.00 141.79 ?  253 TRP B N    1 
ATOM   9220  C CA   . TRP B 1 244 ? 2.291   -17.182 96.626  1.00 146.07 ?  253 TRP B CA   1 
ATOM   9221  C C    . TRP B 1 244 ? 1.850   -16.915 98.044  1.00 170.58 ?  253 TRP B C    1 
ATOM   9222  O O    . TRP B 1 244 ? 1.339   -15.838 98.358  1.00 201.03 ?  253 TRP B O    1 
ATOM   9223  C CB   . TRP B 1 244 ? 3.636   -16.528 96.385  1.00 161.32 ?  253 TRP B CB   1 
ATOM   9224  C CG   . TRP B 1 244 ? 4.215   -16.975 95.131  1.00 145.62 ?  253 TRP B CG   1 
ATOM   9225  C CD1  . TRP B 1 244 ? 4.462   -18.255 94.766  1.00 131.35 ?  253 TRP B CD1  1 
ATOM   9226  C CD2  . TRP B 1 244 ? 4.621   -16.153 94.029  1.00 116.21 ?  253 TRP B CD2  1 
ATOM   9227  N NE1  . TRP B 1 244 ? 4.998   -18.287 93.497  1.00 123.16 ?  253 TRP B NE1  1 
ATOM   9228  C CE2  . TRP B 1 244 ? 5.110   -17.005 93.028  1.00 118.90 ?  253 TRP B CE2  1 
ATOM   9229  C CE3  . TRP B 1 244 ? 4.618   -14.782 93.792  1.00 97.17  ?  253 TRP B CE3  1 
ATOM   9230  C CZ2  . TRP B 1 244 ? 5.587   -16.527 91.810  1.00 113.36 ?  253 TRP B CZ2  1 
ATOM   9231  C CZ3  . TRP B 1 244 ? 5.101   -14.312 92.576  1.00 69.67  ?  253 TRP B CZ3  1 
ATOM   9232  C CH2  . TRP B 1 244 ? 5.563   -15.182 91.606  1.00 113.66 ?  253 TRP B CH2  1 
ATOM   9233  H H    . TRP B 1 244 ? 1.097   -15.851 95.809  1.00 170.15 ?  253 TRP B H    1 
ATOM   9234  H HA   . TRP B 1 244 ? 2.389   -18.140 96.510  1.00 175.29 ?  253 TRP B HA   1 
ATOM   9235  H HB2  . TRP B 1 244 ? 3.523   -15.566 96.344  1.00 193.58 ?  253 TRP B HB2  1 
ATOM   9236  H HB3  . TRP B 1 244 ? 4.243   -16.766 97.103  1.00 193.58 ?  253 TRP B HB3  1 
ATOM   9237  H HD1  . TRP B 1 244 ? 4.291   -19.003 95.293  1.00 157.62 ?  253 TRP B HD1  1 
ATOM   9238  H HE1  . TRP B 1 244 ? 5.233   -18.997 93.072  1.00 147.79 ?  253 TRP B HE1  1 
ATOM   9239  H HE3  . TRP B 1 244 ? 4.299   -14.190 94.435  1.00 116.61 ?  253 TRP B HE3  1 
ATOM   9240  H HZ2  . TRP B 1 244 ? 5.907   -17.107 91.157  1.00 136.03 ?  253 TRP B HZ2  1 
ATOM   9241  H HZ3  . TRP B 1 244 ? 5.101   -13.398 92.407  1.00 83.60  ?  253 TRP B HZ3  1 
ATOM   9242  H HH2  . TRP B 1 244 ? 5.887   -14.838 90.805  1.00 136.39 ?  253 TRP B HH2  1 
ATOM   9243  N N    . GLU B 1 245 ? 2.056   -17.902 98.893  1.00 126.84 ?  254 GLU B N    1 
ATOM   9244  C CA   . GLU B 1 245 ? 1.871   -17.648 100.302 1.00 111.67 ?  254 GLU B CA   1 
ATOM   9245  C C    . GLU B 1 245 ? 2.933   -16.677 100.757 1.00 84.75  ?  254 GLU B C    1 
ATOM   9246  O O    . GLU B 1 245 ? 2.695   -15.832 101.625 1.00 150.58 ?  254 GLU B O    1 
ATOM   9247  C CB   . GLU B 1 245 ? 1.946   -18.953 101.092 1.00 164.67 ?  254 GLU B CB   1 
ATOM   9248  H H    . GLU B 1 245 ? 2.296   -18.702 98.688  1.00 152.21 ?  254 GLU B H    1 
ATOM   9249  H HA   . GLU B 1 245 ? 1.000   -17.246 100.449 1.00 134.01 ?  254 GLU B HA   1 
ATOM   9250  N N    . ASP B 1 246 ? 3.992   -16.752 100.176 1.00 125.23 ?  255 ASP B N    1 
ATOM   9251  C CA   . ASP B 1 246 ? 5.281   -16.141 100.443 1.00 139.81 ?  255 ASP B CA   1 
ATOM   9252  C C    . ASP B 1 246 ? 5.369   -14.767 99.769  1.00 126.90 ?  255 ASP B C    1 
ATOM   9253  O O    . ASP B 1 246 ? 4.984   -14.618 98.603  1.00 147.92 ?  255 ASP B O    1 
ATOM   9254  C CB   . ASP B 1 246 ? 6.392   -17.029 99.865  1.00 143.67 ?  255 ASP B CB   1 
ATOM   9255  C CG   . ASP B 1 246 ? 6.085   -18.550 99.969  1.00 130.56 ?  255 ASP B CG   1 
ATOM   9256  O OD1  . ASP B 1 246 ? 6.224   -19.117 101.076 1.00 176.64 ?  255 ASP B OD1  1 
ATOM   9257  O OD2  . ASP B 1 246 ? 5.706   -19.184 98.931  1.00 102.31 -1 255 ASP B OD2  1 
ATOM   9258  H H    . ASP B 1 246 ? 4.052   -17.241 99.471  1.00 150.28 ?  255 ASP B H    1 
ATOM   9259  H HA   . ASP B 1 246 ? 5.415   -16.040 101.398 1.00 167.77 ?  255 ASP B HA   1 
ATOM   9260  H HB2  . ASP B 1 246 ? 6.510   -16.812 98.927  1.00 172.41 ?  255 ASP B HB2  1 
ATOM   9261  H HB3  . ASP B 1 246 ? 7.214   -16.857 100.349 1.00 172.41 ?  255 ASP B HB3  1 
ATOM   9262  N N    . PRO B 1 247 ? 5.907   -13.742 100.422 1.00 105.13 ?  256 PRO B N    1 
ATOM   9263  C CA   . PRO B 1 247 ? 6.167   -12.497 99.704  1.00 74.90  ?  256 PRO B CA   1 
ATOM   9264  C C    . PRO B 1 247 ? 7.429   -12.624 98.870  1.00 79.24  ?  256 PRO B C    1 
ATOM   9265  O O    . PRO B 1 247 ? 8.449   -13.146 99.323  1.00 110.96 ?  256 PRO B O    1 
ATOM   9266  C CB   . PRO B 1 247 ? 6.303   -11.464 100.831 1.00 71.25  ?  256 PRO B CB   1 
ATOM   9267  C CG   . PRO B 1 247 ? 6.682   -12.219 102.013 1.00 98.69  ?  256 PRO B CG   1 
ATOM   9268  C CD   . PRO B 1 247 ? 6.133   -13.601 101.871 1.00 77.67  ?  256 PRO B CD   1 
ATOM   9269  H HA   . PRO B 1 247 ? 5.417   -12.265 99.135  1.00 89.89  ?  256 PRO B HA   1 
ATOM   9270  H HB2  . PRO B 1 247 ? 6.991   -10.821 100.601 1.00 85.49  ?  256 PRO B HB2  1 
ATOM   9271  H HB3  . PRO B 1 247 ? 5.452   -11.019 100.968 1.00 85.49  ?  256 PRO B HB3  1 
ATOM   9272  H HG2  . PRO B 1 247 ? 7.650   -12.248 102.075 1.00 118.42 ?  256 PRO B HG2  1 
ATOM   9273  H HG3  . PRO B 1 247 ? 6.309   -11.789 102.798 1.00 118.42 ?  256 PRO B HG3  1 
ATOM   9274  H HD2  . PRO B 1 247 ? 6.782   -14.254 102.176 1.00 93.21  ?  256 PRO B HD2  1 
ATOM   9275  H HD3  . PRO B 1 247 ? 5.295   -13.682 102.353 1.00 93.21  ?  256 PRO B HD3  1 
ATOM   9276  N N    . LYS B 1 248 ? 7.364   -12.136 97.641  1.00 72.63  ?  257 LYS B N    1 
ATOM   9277  C CA   . LYS B 1 248 ? 8.460   -12.315 96.701  1.00 68.08  ?  257 LYS B CA   1 
ATOM   9278  C C    . LYS B 1 248 ? 9.062   -10.964 96.332  1.00 86.04  ?  257 LYS B C    1 
ATOM   9279  O O    . LYS B 1 248 ? 8.335   -9.994  96.096  1.00 137.99 ?  257 LYS B O    1 
ATOM   9280  C CB   . LYS B 1 248 ? 7.989   -13.065 95.457  1.00 79.84  ?  257 LYS B CB   1 
ATOM   9281  C CG   . LYS B 1 248 ? 7.392   -14.457 95.733  1.00 117.28 ?  257 LYS B CG   1 
ATOM   9282  C CD   . LYS B 1 248 ? 8.345   -15.392 96.449  1.00 90.74  ?  257 LYS B CD   1 
ATOM   9283  H H    . LYS B 1 248 ? 6.696   -11.696 97.325  1.00 87.16  ?  257 LYS B H    1 
ATOM   9284  H HA   . LYS B 1 248 ? 9.154   -12.845 97.124  1.00 81.70  ?  257 LYS B HA   1 
ATOM   9285  H HB2  . LYS B 1 248 ? 7.307   -12.535 95.016  1.00 95.80  ?  257 LYS B HB2  1 
ATOM   9286  H HB3  . LYS B 1 248 ? 8.746   -13.183 94.862  1.00 95.80  ?  257 LYS B HB3  1 
ATOM   9287  H HG2  . LYS B 1 248 ? 6.602   -14.355 96.288  1.00 140.74 ?  257 LYS B HG2  1 
ATOM   9288  H HG3  . LYS B 1 248 ? 7.150   -14.867 94.888  1.00 140.74 ?  257 LYS B HG3  1 
ATOM   9289  H HD2  . LYS B 1 248 ? 9.178   -15.433 95.955  1.00 108.88 ?  257 LYS B HD2  1 
ATOM   9290  H HD3  . LYS B 1 248 ? 8.505   -15.055 97.344  1.00 108.88 ?  257 LYS B HD3  1 
ATOM   9291  N N    . GLU B 1 249 ? 10.406  -10.921 96.309  1.00 95.30  ?  258 GLU B N    1 
ATOM   9292  C CA   . GLU B 1 249 ? 11.187  -9.712  96.035  1.00 82.68  ?  258 GLU B CA   1 
ATOM   9293  C C    . GLU B 1 249 ? 11.586  -9.582  94.564  1.00 82.28  ?  258 GLU B C    1 
ATOM   9294  O O    . GLU B 1 249 ? 12.213  -10.479 93.995  1.00 76.84  ?  258 GLU B O    1 
ATOM   9295  C CB   . GLU B 1 249 ? 12.439  -9.709  96.914  1.00 95.25  ?  258 GLU B CB   1 
ATOM   9296  C CG   . GLU B 1 249 ? 12.165  -9.482  98.371  1.00 103.37 ?  258 GLU B CG   1 
ATOM   9297  C CD   . GLU B 1 249 ? 13.417  -9.403  99.206  1.00 129.32 ?  258 GLU B CD   1 
ATOM   9298  O OE1  . GLU B 1 249 ? 14.112  -8.371  99.172  1.00 160.79 ?  258 GLU B OE1  1 
ATOM   9299  O OE2  . GLU B 1 249 ? 13.690  -10.391 99.910  1.00 125.04 -1 258 GLU B OE2  1 
ATOM   9300  H H    . GLU B 1 249 ? 10.900  -11.610 96.455  1.00 114.35 ?  258 GLU B H    1 
ATOM   9301  H HA   . GLU B 1 249 ? 10.656  -8.935  96.269  1.00 99.22  ?  258 GLU B HA   1 
ATOM   9302  H HB2  . GLU B 1 249 ? 12.883  -10.567 96.827  1.00 114.30 ?  258 GLU B HB2  1 
ATOM   9303  H HB3  . GLU B 1 249 ? 13.031  -9.002  96.611  1.00 114.30 ?  258 GLU B HB3  1 
ATOM   9304  H HG2  . GLU B 1 249 ? 11.684  -8.646  98.474  1.00 124.04 ?  258 GLU B HG2  1 
ATOM   9305  H HG3  . GLU B 1 249 ? 11.627  -10.216 98.708  1.00 124.04 ?  258 GLU B HG3  1 
ATOM   9306  N N    . PHE B 1 250 ? 11.303  -8.422  93.977  1.00 110.15 ?  259 PHE B N    1 
ATOM   9307  C CA   . PHE B 1 250 ? 11.642  -8.162  92.583  1.00 100.32 ?  259 PHE B CA   1 
ATOM   9308  C C    . PHE B 1 250 ? 12.109  -6.719  92.426  1.00 91.19  ?  259 PHE B C    1 
ATOM   9309  O O    . PHE B 1 250 ? 11.590  -5.809  93.080  1.00 133.68 ?  259 PHE B O    1 
ATOM   9310  C CB   . PHE B 1 250 ? 10.456  -8.413  91.628  1.00 97.20  ?  259 PHE B CB   1 
ATOM   9311  C CG   . PHE B 1 250 ? 10.050  -9.857  91.514  1.00 88.45  ?  259 PHE B CG   1 
ATOM   9312  C CD1  . PHE B 1 250 ? 10.846  -10.772 90.836  1.00 98.02  ?  259 PHE B CD1  1 
ATOM   9313  C CD2  . PHE B 1 250 ? 8.843   -10.290 92.036  1.00 88.75  ?  259 PHE B CD2  1 
ATOM   9314  C CE1  . PHE B 1 250 ? 10.473  -12.099 90.736  1.00 87.61  ?  259 PHE B CE1  1 
ATOM   9315  C CE2  . PHE B 1 250 ? 8.463   -11.609 91.935  1.00 139.26 ?  259 PHE B CE2  1 
ATOM   9316  C CZ   . PHE B 1 250 ? 9.276   -12.515 91.276  1.00 125.22 ?  259 PHE B CZ   1 
ATOM   9317  H H    . PHE B 1 250 ? 10.912  -7.764  94.369  1.00 132.18 ?  259 PHE B H    1 
ATOM   9318  H HA   . PHE B 1 250 ? 12.371  -8.745  92.319  1.00 120.39 ?  259 PHE B HA   1 
ATOM   9319  H HB2  . PHE B 1 250 ? 9.687   -7.915  91.949  1.00 116.64 ?  259 PHE B HB2  1 
ATOM   9320  H HB3  . PHE B 1 250 ? 10.699  -8.104  90.742  1.00 116.64 ?  259 PHE B HB3  1 
ATOM   9321  H HD1  . PHE B 1 250 ? 11.659  -10.496 90.478  1.00 117.62 ?  259 PHE B HD1  1 
ATOM   9322  H HD2  . PHE B 1 250 ? 8.296   -9.688  92.487  1.00 106.50 ?  259 PHE B HD2  1 
ATOM   9323  H HE1  . PHE B 1 250 ? 11.019  -12.704 90.289  1.00 105.13 ?  259 PHE B HE1  1 
ATOM   9324  H HE2  . PHE B 1 250 ? 7.654   -11.889 92.300  1.00 167.11 ?  259 PHE B HE2  1 
ATOM   9325  H HZ   . PHE B 1 250 ? 9.016   -13.405 91.202  1.00 150.26 ?  259 PHE B HZ   1 
ATOM   9326  N N    . ALA B 1 251 ? 13.085  -6.521  91.549  1.00 98.65  ?  260 ALA B N    1 
ATOM   9327  C CA   . ALA B 1 251 ? 13.758  -5.246  91.428  1.00 77.64  ?  260 ALA B CA   1 
ATOM   9328  C C    . ALA B 1 251 ? 12.972  -4.203  90.634  1.00 78.63  ?  260 ALA B C    1 
ATOM   9329  O O    . ALA B 1 251 ? 12.313  -4.504  89.632  1.00 85.16  ?  260 ALA B O    1 
ATOM   9330  C CB   . ALA B 1 251 ? 15.084  -5.436  90.745  1.00 99.23  ?  260 ALA B CB   1 
ATOM   9331  H H    . ALA B 1 251 ? 13.377  -7.122  91.006  1.00 118.37 ?  260 ALA B H    1 
ATOM   9332  H HA   . ALA B 1 251 ? 13.923  -4.889  92.314  1.00 93.16  ?  260 ALA B HA   1 
ATOM   9333  H HB1  . ALA B 1 251 ? 15.525  -4.575  90.669  1.00 119.08 ?  260 ALA B HB1  1 
ATOM   9334  H HB2  . ALA B 1 251 ? 15.627  -6.042  91.273  1.00 119.08 ?  260 ALA B HB2  1 
ATOM   9335  H HB3  . ALA B 1 251 ? 14.933  -5.809  89.863  1.00 119.08 ?  260 ALA B HB3  1 
ATOM   9336  N N    . GLY B 1 252 ? 13.123  -2.941  91.041  1.00 78.83  ?  261 GLY B N    1 
ATOM   9337  C CA   . GLY B 1 252 ? 12.657  -1.859  90.208  1.00 71.64  ?  261 GLY B CA   1 
ATOM   9338  C C    . GLY B 1 252 ? 13.420  -1.763  88.898  1.00 68.42  ?  261 GLY B C    1 
ATOM   9339  O O    . GLY B 1 252 ? 14.562  -2.205  88.755  1.00 109.55 ?  261 GLY B O    1 
ATOM   9340  H H    . GLY B 1 252 ? 13.485  -2.699  91.783  1.00 94.60  ?  261 GLY B H    1 
ATOM   9341  H HA2  . GLY B 1 252 ? 11.717  -1.989  90.006  1.00 85.96  ?  261 GLY B HA2  1 
ATOM   9342  H HA3  . GLY B 1 252 ? 12.756  -1.020  90.683  1.00 85.96  ?  261 GLY B HA3  1 
ATOM   9343  N N    . GLY B 1 253 ? 12.755  -1.181  87.910  1.00 60.05  ?  262 GLY B N    1 
ATOM   9344  C CA   . GLY B 1 253 ? 13.392  -0.950  86.627  1.00 55.55  ?  262 GLY B CA   1 
ATOM   9345  C C    . GLY B 1 253 ? 14.610  -0.055  86.753  1.00 94.98  ?  262 GLY B C    1 
ATOM   9346  O O    . GLY B 1 253 ? 14.730  0.799   87.668  1.00 60.16  ?  262 GLY B O    1 
ATOM   9347  H H    . GLY B 1 253 ? 11.939  -0.913  87.957  1.00 72.06  ?  262 GLY B H    1 
ATOM   9348  H HA2  . GLY B 1 253 ? 13.670  -1.797  86.245  1.00 66.66  ?  262 GLY B HA2  1 
ATOM   9349  H HA3  . GLY B 1 253 ? 12.762  -0.529  86.022  1.00 66.66  ?  262 GLY B HA3  1 
ATOM   9350  N N    . SER B 1 254 ? 15.554  -0.336  85.868  1.00 40.97  ?  263 SER B N    1 
ATOM   9351  C CA   . SER B 1 254 ? 16.807  0.383   85.799  1.00 58.54  ?  263 SER B CA   1 
ATOM   9352  C C    . SER B 1 254 ? 17.385  0.230   84.402  1.00 58.68  ?  263 SER B C    1 
ATOM   9353  O O    . SER B 1 254 ? 16.982  -0.624  83.605  1.00 52.08  ?  263 SER B O    1 
ATOM   9354  C CB   . SER B 1 254 ? 17.840  -0.120  86.807  1.00 83.75  ?  263 SER B CB   1 
ATOM   9355  O OG   . SER B 1 254 ? 18.609  -1.194  86.251  1.00 85.30  ?  263 SER B OG   1 
ATOM   9356  H H    . SER B 1 254 ? 15.486  -0.960  85.280  1.00 49.16  ?  263 SER B H    1 
ATOM   9357  H HA   . SER B 1 254 ? 16.649  1.326   85.965  1.00 70.25  ?  263 SER B HA   1 
ATOM   9358  H HB2  . SER B 1 254 ? 18.437  0.608   87.040  1.00 100.50 ?  263 SER B HB2  1 
ATOM   9359  H HB3  . SER B 1 254 ? 17.380  -0.438  87.600  1.00 100.50 ?  263 SER B HB3  1 
ATOM   9360  H HG   . SER B 1 254 ? 19.173  -1.464  86.812  1.00 102.36 ?  263 SER B HG   1 
ATOM   9361  N N    . ALA B 1 255 ? 18.385  1.040   84.129  1.00 71.74  ?  264 ALA B N    1 
ATOM   9362  C CA   . ALA B 1 255 ? 18.982  0.964   82.815  1.00 58.01  ?  264 ALA B CA   1 
ATOM   9363  C C    . ALA B 1 255 ? 19.495  -0.431  82.504  1.00 80.11  ?  264 ALA B C    1 
ATOM   9364  O O    . ALA B 1 255 ? 19.589  -0.804  81.334  1.00 70.26  ?  264 ALA B O    1 
ATOM   9365  C CB   . ALA B 1 255 ? 20.085  2.003   82.756  1.00 75.19  ?  264 ALA B CB   1 
ATOM   9366  H H    . ALA B 1 255 ? 18.726  1.622   84.662  1.00 86.08  ?  264 ALA B H    1 
ATOM   9367  H HA   . ALA B 1 255 ? 18.315  1.194   82.150  1.00 69.61  ?  264 ALA B HA   1 
ATOM   9368  H HB1  . ALA B 1 255 ? 20.502  1.970   81.880  1.00 90.23  ?  264 ALA B HB1  1 
ATOM   9369  H HB2  . ALA B 1 255 ? 19.701  2.880   82.907  1.00 90.23  ?  264 ALA B HB2  1 
ATOM   9370  H HB3  . ALA B 1 255 ? 20.742  1.806   83.442  1.00 90.23  ?  264 ALA B HB3  1 
ATOM   9371  N N    . GLY B 1 256 ? 19.836  -1.218  83.523  1.00 74.79  ?  265 GLY B N    1 
ATOM   9372  C CA   . GLY B 1 256 ? 20.411  -2.529  83.272  1.00 73.55  ?  265 GLY B CA   1 
ATOM   9373  C C    . GLY B 1 256 ? 19.500  -3.502  82.550  1.00 90.00  ?  265 GLY B C    1 
ATOM   9374  O O    . GLY B 1 256 ? 19.993  -4.472  81.965  1.00 63.21  ?  265 GLY B O    1 
ATOM   9375  H H    . GLY B 1 256 ? 19.745  -1.017  84.354  1.00 89.75  ?  265 GLY B H    1 
ATOM   9376  H HA2  . GLY B 1 256 ? 21.216  -2.423  82.741  1.00 88.26  ?  265 GLY B HA2  1 
ATOM   9377  H HA3  . GLY B 1 256 ? 20.662  -2.929  84.120  1.00 88.26  ?  265 GLY B HA3  1 
ATOM   9378  N N    . GLN B 1 257 ? 18.210  -3.234  82.499  1.00 99.68  ?  266 GLN B N    1 
ATOM   9379  C CA   . GLN B 1 257 ? 17.341  -4.129  81.759  1.00 54.73  ?  266 GLN B CA   1 
ATOM   9380  C C    . GLN B 1 257 ? 17.372  -3.834  80.242  1.00 53.62  ?  266 GLN B C    1 
ATOM   9381  O O    . GLN B 1 257 ? 16.829  -4.640  79.434  1.00 45.98  ?  266 GLN B O    1 
ATOM   9382  C CB   . GLN B 1 257 ? 15.932  -4.012  82.353  1.00 66.76  ?  266 GLN B CB   1 
ATOM   9383  C CG   . GLN B 1 257 ? 15.820  -4.404  83.840  1.00 74.24  ?  266 GLN B CG   1 
ATOM   9384  C CD   . GLN B 1 257 ? 14.553  -3.871  84.538  1.00 65.84  ?  266 GLN B CD   1 
ATOM   9385  O OE1  . GLN B 1 257 ? 13.877  -2.925  84.045  1.00 55.73  ?  266 GLN B OE1  1 
ATOM   9386  N NE2  . GLN B 1 257 ? 14.264  -4.417  85.727  1.00 55.22  ?  266 GLN B NE2  1 
ATOM   9387  H H    . GLN B 1 257 ? 17.820  -2.563  82.870  1.00 119.61 ?  266 GLN B H    1 
ATOM   9388  H HA   . GLN B 1 257 ? 17.645  -5.041  81.891  1.00 65.68  ?  266 GLN B HA   1 
ATOM   9389  H HB2  . GLN B 1 257 ? 15.637  -3.091  82.269  1.00 80.11  ?  266 GLN B HB2  1 
ATOM   9390  H HB3  . GLN B 1 257 ? 15.336  -4.590  81.851  1.00 80.11  ?  266 GLN B HB3  1 
ATOM   9391  H HG2  . GLN B 1 257 ? 15.809  -5.371  83.907  1.00 89.09  ?  266 GLN B HG2  1 
ATOM   9392  H HG3  . GLN B 1 257 ? 16.589  -4.050  84.314  1.00 89.09  ?  266 GLN B HG3  1 
ATOM   9393  H HE21 . GLN B 1 257 ? 14.774  -5.027  86.056  1.00 66.27  ?  266 GLN B HE21 1 
ATOM   9394  H HE22 . GLN B 1 257 ? 13.569  -4.158  86.162  1.00 66.27  ?  266 GLN B HE22 1 
ATOM   9395  N N    . SER B 1 258 ? 18.005  -2.709  79.810  1.00 59.35  ?  267 SER B N    1 
ATOM   9396  C CA   . SER B 1 258 ? 18.113  -2.440  78.378  1.00 65.17  ?  267 SER B CA   1 
ATOM   9397  C C    . SER B 1 258 ? 19.007  -3.486  77.720  1.00 73.34  ?  267 SER B C    1 
ATOM   9398  O O    . SER B 1 258 ? 20.186  -3.622  78.069  1.00 78.07  ?  267 SER B O    1 
ATOM   9399  C CB   . SER B 1 258 ? 18.673  -1.039  78.097  1.00 65.97  ?  267 SER B CB   1 
ATOM   9400  O OG   . SER B 1 258 ? 19.052  -0.876  76.654  1.00 57.94  ?  267 SER B OG   1 
ATOM   9401  H H    . SER B 1 258 ? 18.364  -2.116  80.319  1.00 71.23  ?  267 SER B H    1 
ATOM   9402  H HA   . SER B 1 258 ? 17.232  -2.499  77.977  1.00 78.20  ?  267 SER B HA   1 
ATOM   9403  H HB2  . SER B 1 258 ? 17.996  -0.380  78.320  1.00 79.17  ?  267 SER B HB2  1 
ATOM   9404  H HB3  . SER B 1 258 ? 19.461  -0.900  78.646  1.00 79.17  ?  267 SER B HB3  1 
ATOM   9405  H HG   . SER B 1 258 ? 18.379  -0.992  76.166  1.00 69.53  ?  267 SER B HG   1 
ATOM   9406  N N    . SER B 1 259 ? 18.477  -4.187  76.725  1.00 56.64  ?  268 SER B N    1 
ATOM   9407  C CA   . SER B 1 259 ? 19.337  -5.104  75.988  1.00 69.40  ?  268 SER B CA   1 
ATOM   9408  C C    . SER B 1 259 ? 20.532  -4.348  75.405  1.00 65.37  ?  268 SER B C    1 
ATOM   9409  O O    . SER B 1 259 ? 21.641  -4.889  75.298  1.00 62.41  ?  268 SER B O    1 
ATOM   9410  C CB   . SER B 1 259 ? 18.539  -5.788  74.879  1.00 64.71  ?  268 SER B CB   1 
ATOM   9411  O OG   . SER B 1 259 ? 17.484  -6.522  75.458  1.00 108.50 ?  268 SER B OG   1 
ATOM   9412  H H    . SER B 1 259 ? 17.658  -4.154  76.464  1.00 67.97  ?  268 SER B H    1 
ATOM   9413  H HA   . SER B 1 259 ? 19.671  -5.787  76.590  1.00 83.28  ?  268 SER B HA   1 
ATOM   9414  H HB2  . SER B 1 259 ? 18.173  -5.115  74.284  1.00 77.65  ?  268 SER B HB2  1 
ATOM   9415  H HB3  . SER B 1 259 ? 19.120  -6.391  74.389  1.00 77.65  ?  268 SER B HB3  1 
ATOM   9416  H HG   . SER B 1 259 ? 17.792  -7.104  75.980  1.00 130.20 ?  268 SER B HG   1 
ATOM   9417  N N    . VAL B 1 260 ? 20.288  -3.107  74.961  1.00 74.31  ?  269 VAL B N    1 
ATOM   9418  C CA   . VAL B 1 260 ? 21.290  -2.265  74.306  1.00 67.02  ?  269 VAL B CA   1 
ATOM   9419  C C    . VAL B 1 260 ? 22.437  -1.927  75.258  1.00 64.68  ?  269 VAL B C    1 
ATOM   9420  O O    . VAL B 1 260 ? 23.596  -1.842  74.845  1.00 95.70  ?  269 VAL B O    1 
ATOM   9421  C CB   . VAL B 1 260 ? 20.537  -1.024  73.749  1.00 67.70  ?  269 VAL B CB   1 
ATOM   9422  C CG1  . VAL B 1 260 ? 21.245  0.274   73.959  1.00 75.48  ?  269 VAL B CG1  1 
ATOM   9423  C CG2  . VAL B 1 260 ? 20.266  -1.230  72.263  1.00 88.68  ?  269 VAL B CG2  1 
ATOM   9424  H H    . VAL B 1 260 ? 19.522  -2.723  75.033  1.00 89.17  ?  269 VAL B H    1 
ATOM   9425  H HA   . VAL B 1 260 ? 21.663  -2.749  73.552  1.00 80.42  ?  269 VAL B HA   1 
ATOM   9426  H HB   . VAL B 1 260 ? 19.678  -0.962  74.195  1.00 81.24  ?  269 VAL B HB   1 
ATOM   9427  H HG11 . VAL B 1 260 ? 20.708  0.990   73.584  1.00 90.57  ?  269 VAL B HG11 1 
ATOM   9428  H HG12 . VAL B 1 260 ? 21.368  0.416   74.911  1.00 90.57  ?  269 VAL B HG12 1 
ATOM   9429  H HG13 . VAL B 1 260 ? 22.107  0.239   73.516  1.00 90.57  ?  269 VAL B HG13 1 
ATOM   9430  H HG21 . VAL B 1 260 ? 19.796  -0.454  71.918  1.00 106.42 ?  269 VAL B HG21 1 
ATOM   9431  H HG22 . VAL B 1 260 ? 21.112  -1.337  71.800  1.00 106.42 ?  269 VAL B HG22 1 
ATOM   9432  H HG23 . VAL B 1 260 ? 19.723  -2.025  72.148  1.00 106.42 ?  269 VAL B HG23 1 
ATOM   9433  N N    . PHE B 1 261 ? 22.152  -1.794  76.537  1.00 77.52  ?  270 PHE B N    1 
ATOM   9434  C CA   . PHE B 1 261 ? 23.163  -1.386  77.486  1.00 68.88  ?  270 PHE B CA   1 
ATOM   9435  C C    . PHE B 1 261 ? 24.178  -2.466  77.733  1.00 67.78  ?  270 PHE B C    1 
ATOM   9436  O O    . PHE B 1 261 ? 25.289  -2.194  78.214  1.00 74.60  ?  270 PHE B O    1 
ATOM   9437  C CB   . PHE B 1 261 ? 22.415  -1.037  78.722  1.00 51.60  ?  270 PHE B CB   1 
ATOM   9438  C CG   . PHE B 1 261 ? 23.231  -0.519  79.873  1.00 50.44  ?  270 PHE B CG   1 
ATOM   9439  C CD1  . PHE B 1 261 ? 23.852  -1.384  80.741  1.00 60.17  ?  270 PHE B CD1  1 
ATOM   9440  C CD2  . PHE B 1 261 ? 23.233  0.846   80.191  1.00 56.01  ?  270 PHE B CD2  1 
ATOM   9441  C CE1  . PHE B 1 261 ? 24.528  -0.893  81.873  1.00 57.86  ?  270 PHE B CE1  1 
ATOM   9442  C CE2  . PHE B 1 261 ? 23.893  1.342   81.318  1.00 60.87  ?  270 PHE B CE2  1 
ATOM   9443  C CZ   . PHE B 1 261 ? 24.539  0.449   82.157  1.00 62.87  ?  270 PHE B CZ   1 
ATOM   9444  H H    . PHE B 1 261 ? 21.377  -1.934  76.883  1.00 93.02  ?  270 PHE B H    1 
ATOM   9445  H HA   . PHE B 1 261 ? 23.620  -0.594  77.161  1.00 82.65  ?  270 PHE B HA   1 
ATOM   9446  H HB2  . PHE B 1 261 ? 21.764  -0.353  78.500  1.00 61.92  ?  270 PHE B HB2  1 
ATOM   9447  H HB3  . PHE B 1 261 ? 21.953  -1.832  79.032  1.00 61.92  ?  270 PHE B HB3  1 
ATOM   9448  H HD1  . PHE B 1 261 ? 23.840  -2.298  80.570  1.00 72.21  ?  270 PHE B HD1  1 
ATOM   9449  H HD2  . PHE B 1 261 ? 22.783  1.440   79.634  1.00 67.22  ?  270 PHE B HD2  1 
ATOM   9450  H HE1  . PHE B 1 261 ? 24.970  -1.486  82.438  1.00 69.43  ?  270 PHE B HE1  1 
ATOM   9451  H HE2  . PHE B 1 261 ? 23.907  2.254   81.495  1.00 73.05  ?  270 PHE B HE2  1 
ATOM   9452  H HZ   . PHE B 1 261 ? 25.008  0.763   82.897  1.00 75.44  ?  270 PHE B HZ   1 
ATOM   9453  N N    . GLN B 1 262 ? 23.847  -3.680  77.339  1.00 68.70  ?  271 GLN B N    1 
ATOM   9454  C CA   . GLN B 1 262 ? 24.680  -4.816  77.596  1.00 74.49  ?  271 GLN B CA   1 
ATOM   9455  C C    . GLN B 1 262 ? 25.292  -5.389  76.333  1.00 76.07  ?  271 GLN B C    1 
ATOM   9456  O O    . GLN B 1 262 ? 26.364  -6.002  76.389  1.00 83.98  ?  271 GLN B O    1 
ATOM   9457  C CB   . GLN B 1 262 ? 23.846  -5.872  78.297  1.00 59.08  ?  271 GLN B CB   1 
ATOM   9458  C CG   . GLN B 1 262 ? 23.361  -5.486  79.682  1.00 78.63  ?  271 GLN B CG   1 
ATOM   9459  C CD   . GLN B 1 262 ? 23.251  -6.691  80.672  1.00 58.51  ?  271 GLN B CD   1 
ATOM   9460  O OE1  . GLN B 1 262 ? 23.937  -7.708  80.517  1.00 110.19 ?  271 GLN B OE1  1 
ATOM   9461  N NE2  . GLN B 1 262 ? 22.430  -6.533  81.713  1.00 71.13  ?  271 GLN B NE2  1 
ATOM   9462  H H    . GLN B 1 262 ? 23.126  -3.868  76.911  1.00 82.44  ?  271 GLN B H    1 
ATOM   9463  H HA   . GLN B 1 262 ? 25.401  -4.555  78.190  1.00 89.39  ?  271 GLN B HA   1 
ATOM   9464  H HB2  . GLN B 1 262 ? 23.064  -6.059  77.754  1.00 70.90  ?  271 GLN B HB2  1 
ATOM   9465  H HB3  . GLN B 1 262 ? 24.380  -6.677  78.387  1.00 70.90  ?  271 GLN B HB3  1 
ATOM   9466  H HG2  . GLN B 1 262 ? 23.982  -4.845  80.064  1.00 94.36  ?  271 GLN B HG2  1 
ATOM   9467  H HG3  . GLN B 1 262 ? 22.481  -5.085  79.605  1.00 94.36  ?  271 GLN B HG3  1 
ATOM   9468  H HE21 . GLN B 1 262 ? 21.996  -5.797  81.811  1.00 85.35  ?  271 GLN B HE21 1 
ATOM   9469  H HE22 . GLN B 1 262 ? 22.334  -7.167  82.286  1.00 85.35  ?  271 GLN B HE22 1 
ATOM   9470  N N    . CYS B 1 263 ? 24.616  -5.249  75.204  1.00 61.82  ?  272 CYS B N    1 
ATOM   9471  C CA   . CYS B 1 263 ? 25.022  -6.046  74.060  1.00 69.53  ?  272 CYS B CA   1 
ATOM   9472  C C    . CYS B 1 263 ? 26.329  -5.571  73.436  1.00 56.19  ?  272 CYS B C    1 
ATOM   9473  O O    . CYS B 1 263 ? 26.962  -6.322  72.705  1.00 60.03  ?  272 CYS B O    1 
ATOM   9474  C CB   . CYS B 1 263 ? 23.890  -6.098  73.045  1.00 81.73  ?  272 CYS B CB   1 
ATOM   9475  S SG   . CYS B 1 263 ? 23.586  -4.584  72.232  1.00 80.16  ?  272 CYS B SG   1 
ATOM   9476  H H    . CYS B 1 263 ? 23.948  -4.723  75.075  1.00 74.18  ?  272 CYS B H    1 
ATOM   9477  H HA   . CYS B 1 263 ? 25.169  -6.954  74.366  1.00 83.44  ?  272 CYS B HA   1 
ATOM   9478  H HB2  . CYS B 1 263 ? 24.109  -6.758  72.369  1.00 98.08  ?  272 CYS B HB2  1 
ATOM   9479  H HB3  . CYS B 1 263 ? 23.075  -6.357  73.502  1.00 98.08  ?  272 CYS B HB3  1 
ATOM   9480  H HG   . CYS B 1 263 ? 24.577  -4.251  71.644  1.00 96.19  ?  272 CYS B HG   1 
ATOM   9481  N N    . PHE B 1 264 ? 26.724  -4.344  73.652  1.00 68.11  ?  273 PHE B N    1 
ATOM   9482  C CA   . PHE B 1 264 ? 27.974  -3.939  73.020  1.00 53.04  ?  273 PHE B CA   1 
ATOM   9483  C C    . PHE B 1 264 ? 29.160  -4.306  73.877  1.00 57.70  ?  273 PHE B C    1 
ATOM   9484  O O    . PHE B 1 264 ? 30.102  -4.893  73.352  1.00 73.21  ?  273 PHE B O    1 
ATOM   9485  C CB   . PHE B 1 264 ? 27.904  -2.445  72.718  1.00 52.61  ?  273 PHE B CB   1 
ATOM   9486  C CG   . PHE B 1 264 ? 26.908  -2.168  71.649  1.00 62.69  ?  273 PHE B CG   1 
ATOM   9487  C CD1  . PHE B 1 264 ? 27.119  -2.639  70.372  1.00 70.62  ?  273 PHE B CD1  1 
ATOM   9488  C CD2  . PHE B 1 264 ? 25.702  -1.591  71.937  1.00 59.04  ?  273 PHE B CD2  1 
ATOM   9489  C CE1  . PHE B 1 264 ? 26.198  -2.459  69.402  1.00 62.04  ?  273 PHE B CE1  1 
ATOM   9490  C CE2  . PHE B 1 264 ? 24.781  -1.431  70.969  1.00 54.19  ?  273 PHE B CE2  1 
ATOM   9491  C CZ   . PHE B 1 264 ? 25.023  -1.870  69.696  1.00 78.31  ?  273 PHE B CZ   1 
ATOM   9492  H H    . PHE B 1 264 ? 26.325  -3.749  74.129  1.00 81.73  ?  273 PHE B H    1 
ATOM   9493  H HA   . PHE B 1 264 ? 28.063  -4.408  72.176  1.00 63.65  ?  273 PHE B HA   1 
ATOM   9494  H HB2  . PHE B 1 264 ? 27.636  -1.967  73.518  1.00 63.13  ?  273 PHE B HB2  1 
ATOM   9495  H HB3  . PHE B 1 264 ? 28.772  -2.137  72.414  1.00 63.13  ?  273 PHE B HB3  1 
ATOM   9496  H HD1  . PHE B 1 264 ? 27.925  -3.055  70.166  1.00 84.74  ?  273 PHE B HD1  1 
ATOM   9497  H HD2  . PHE B 1 264 ? 25.522  -1.297  72.801  1.00 70.85  ?  273 PHE B HD2  1 
ATOM   9498  H HE1  . PHE B 1 264 ? 26.366  -2.759  68.538  1.00 74.45  ?  273 PHE B HE1  1 
ATOM   9499  H HE2  . PHE B 1 264 ? 23.975  -1.010  71.165  1.00 65.03  ?  273 PHE B HE2  1 
ATOM   9500  H HZ   . PHE B 1 264 ? 24.390  -1.735  69.028  1.00 93.97  ?  273 PHE B HZ   1 
ATOM   9501  N N    . ASP B 1 265 ? 29.027  -4.168  75.206  1.00 49.07  ?  274 ASP B N    1 
ATOM   9502  C CA   . ASP B 1 265 ? 30.013  -4.729  76.110  1.00 41.11  ?  274 ASP B CA   1 
ATOM   9503  C C    . ASP B 1 265 ? 30.283  -6.186  75.727  1.00 77.72  ?  274 ASP B C    1 
ATOM   9504  O O    . ASP B 1 265 ? 31.431  -6.633  75.671  1.00 83.16  ?  274 ASP B O    1 
ATOM   9505  C CB   . ASP B 1 265 ? 29.510  -4.719  77.549  1.00 77.95  ?  274 ASP B CB   1 
ATOM   9506  C CG   . ASP B 1 265 ? 29.019  -3.379  78.012  1.00 97.67  ?  274 ASP B CG   1 
ATOM   9507  O OD1  . ASP B 1 265 ? 29.886  -2.538  78.335  1.00 93.79  ?  274 ASP B OD1  1 
ATOM   9508  O OD2  . ASP B 1 265 ? 27.774  -3.189  78.098  1.00 110.55 -1 274 ASP B OD2  1 
ATOM   9509  H H    . ASP B 1 265 ? 28.379  -3.757  75.595  1.00 58.89  ?  274 ASP B H    1 
ATOM   9510  H HA   . ASP B 1 265 ? 30.841  -4.226  76.058  1.00 49.33  ?  274 ASP B HA   1 
ATOM   9511  H HB2  . ASP B 1 265 ? 28.774  -5.346  77.627  1.00 93.54  ?  274 ASP B HB2  1 
ATOM   9512  H HB3  . ASP B 1 265 ? 30.234  -4.988  78.135  1.00 93.54  ?  274 ASP B HB3  1 
ATOM   9513  N N    . VAL B 1 266 ? 29.224  -6.942  75.450  1.00 59.68  ?  275 VAL B N    1 
ATOM   9514  C CA   . VAL B 1 266 ? 29.403  -8.338  75.123  1.00 50.09  ?  275 VAL B CA   1 
ATOM   9515  C C    . VAL B 1 266 ? 29.993  -8.498  73.745  1.00 68.28  ?  275 VAL B C    1 
ATOM   9516  O O    . VAL B 1 266 ? 30.906  -9.319  73.514  1.00 53.37  ?  275 VAL B O    1 
ATOM   9517  C CB   . VAL B 1 266 ? 28.069  -9.053  75.244  1.00 51.39  ?  275 VAL B CB   1 
ATOM   9518  C CG1  . VAL B 1 266 ? 28.098  -10.398 74.499  1.00 75.42  ?  275 VAL B CG1  1 
ATOM   9519  C CG2  . VAL B 1 266 ? 27.789  -9.243  76.763  1.00 51.71  ?  275 VAL B CG2  1 
ATOM   9520  H H    . VAL B 1 266 ? 28.409  -6.670  75.446  1.00 71.62  ?  275 VAL B H    1 
ATOM   9521  H HA   . VAL B 1 266 ? 30.016  -8.737  75.760  1.00 60.11  ?  275 VAL B HA   1 
ATOM   9522  H HB   . VAL B 1 266 ? 27.366  -8.502  74.865  1.00 61.67  ?  275 VAL B HB   1 
ATOM   9523  H HG11 . VAL B 1 266 ? 27.235  -10.830 74.593  1.00 90.51  ?  275 VAL B HG11 1 
ATOM   9524  H HG12 . VAL B 1 266 ? 28.286  -10.235 73.561  1.00 90.51  ?  275 VAL B HG12 1 
ATOM   9525  H HG13 . VAL B 1 266 ? 28.792  -10.956 74.883  1.00 90.51  ?  275 VAL B HG13 1 
ATOM   9526  H HG21 . VAL B 1 266 ? 26.940  -9.699  76.874  1.00 62.05  ?  275 VAL B HG21 1 
ATOM   9527  H HG22 . VAL B 1 266 ? 28.503  -9.773  77.151  1.00 62.05  ?  275 VAL B HG22 1 
ATOM   9528  H HG23 . VAL B 1 266 ? 27.755  -8.372  77.189  1.00 62.05  ?  275 VAL B HG23 1 
ATOM   9529  N N    . LEU B 1 267 ? 29.472  -7.746  72.793  1.00 68.37  ?  276 LEU B N    1 
ATOM   9530  C CA   . LEU B 1 267 ? 30.062  -7.856  71.476  1.00 64.96  ?  276 LEU B CA   1 
ATOM   9531  C C    . LEU B 1 267 ? 31.560  -7.606  71.561  1.00 56.91  ?  276 LEU B C    1 
ATOM   9532  O O    . LEU B 1 267 ? 32.350  -8.403  71.057  1.00 52.78  ?  276 LEU B O    1 
ATOM   9533  C CB   . LEU B 1 267 ? 29.415  -6.888  70.508  1.00 57.88  ?  276 LEU B CB   1 
ATOM   9534  C CG   . LEU B 1 267 ? 30.161  -6.932  69.165  1.00 52.28  ?  276 LEU B CG   1 
ATOM   9535  C CD1  . LEU B 1 267 ? 30.097  -8.256  68.396  1.00 57.18  ?  276 LEU B CD1  1 
ATOM   9536  C CD2  . LEU B 1 267 ? 29.637  -5.919  68.253  1.00 45.18  ?  276 LEU B CD2  1 
ATOM   9537  H H    . LEU B 1 267 ? 28.816  -7.196  72.873  1.00 82.05  ?  276 LEU B H    1 
ATOM   9538  H HA   . LEU B 1 267 ? 29.925  -8.756  71.141  1.00 77.95  ?  276 LEU B HA   1 
ATOM   9539  H HB2  . LEU B 1 267 ? 28.491  -7.144  70.358  1.00 69.45  ?  276 LEU B HB2  1 
ATOM   9540  H HB3  . LEU B 1 267 ? 29.468  -5.987  70.862  1.00 69.45  ?  276 LEU B HB3  1 
ATOM   9541  H HG   . LEU B 1 267 ? 31.096  -6.730  69.324  1.00 62.73  ?  276 LEU B HG   1 
ATOM   9542  H HD11 . LEU B 1 267 ? 30.600  -8.166  67.571  1.00 68.61  ?  276 LEU B HD11 1 
ATOM   9543  H HD12 . LEU B 1 267 ? 30.483  -8.957  68.944  1.00 68.61  ?  276 LEU B HD12 1 
ATOM   9544  H HD13 . LEU B 1 267 ? 29.170  -8.462  68.199  1.00 68.61  ?  276 LEU B HD13 1 
ATOM   9545  H HD21 . LEU B 1 267 ? 30.122  -5.967  67.415  1.00 54.21  ?  276 LEU B HD21 1 
ATOM   9546  H HD22 . LEU B 1 267 ? 28.694  -6.089  68.100  1.00 54.21  ?  276 LEU B HD22 1 
ATOM   9547  H HD23 . LEU B 1 267 ? 29.754  -5.043  68.654  1.00 54.21  ?  276 LEU B HD23 1 
ATOM   9548  N N    . LEU B 1 268 ? 31.961  -6.537  72.262  1.00 59.17  ?  277 LEU B N    1 
ATOM   9549  C CA   . LEU B 1 268 ? 33.354  -6.100  72.289  1.00 65.67  ?  277 LEU B CA   1 
ATOM   9550  C C    . LEU B 1 268 ? 34.193  -6.864  73.287  1.00 79.88  ?  277 LEU B C    1 
ATOM   9551  O O    . LEU B 1 268 ? 35.392  -6.568  73.468  1.00 68.59  ?  277 LEU B O    1 
ATOM   9552  C CB   . LEU B 1 268 ? 33.467  -4.616  72.627  1.00 60.37  ?  277 LEU B CB   1 
ATOM   9553  C CG   . LEU B 1 268 ? 32.766  -3.764  71.589  1.00 57.80  ?  277 LEU B CG   1 
ATOM   9554  C CD1  . LEU B 1 268 ? 32.704  -2.305  72.064  1.00 94.03  ?  277 LEU B CD1  1 
ATOM   9555  C CD2  . LEU B 1 268 ? 33.355  -3.914  70.200  1.00 48.11  ?  277 LEU B CD2  1 
ATOM   9556  H H    . LEU B 1 268 ? 31.436  -6.046  72.734  1.00 71.01  ?  277 LEU B H    1 
ATOM   9557  H HA   . LEU B 1 268 ? 33.741  -6.236  71.410  1.00 78.80  ?  277 LEU B HA   1 
ATOM   9558  H HB2  . LEU B 1 268 ? 33.053  -4.450  73.488  1.00 72.44  ?  277 LEU B HB2  1 
ATOM   9559  H HB3  . LEU B 1 268 ? 34.403  -4.362  72.648  1.00 72.44  ?  277 LEU B HB3  1 
ATOM   9560  H HG   . LEU B 1 268 ? 31.848  -4.073  71.532  1.00 69.36  ?  277 LEU B HG   1 
ATOM   9561  H HD11 . LEU B 1 268 ? 32.253  -1.773  71.390  1.00 112.84 ?  277 LEU B HD11 1 
ATOM   9562  H HD12 . LEU B 1 268 ? 32.214  -2.266  72.900  1.00 112.84 ?  277 LEU B HD12 1 
ATOM   9563  H HD13 . LEU B 1 268 ? 33.608  -1.978  72.194  1.00 112.84 ?  277 LEU B HD13 1 
ATOM   9564  H HD21 . LEU B 1 268 ? 32.864  -3.346  69.587  1.00 57.73  ?  277 LEU B HD21 1 
ATOM   9565  H HD22 . LEU B 1 268 ? 34.288  -3.649  70.223  1.00 57.73  ?  277 LEU B HD22 1 
ATOM   9566  H HD23 . LEU B 1 268 ? 33.281  -4.841  69.925  1.00 57.73  ?  277 LEU B HD23 1 
ATOM   9567  N N    . GLY B 1 269 ? 33.617  -7.852  73.930  1.00 65.09  ?  278 GLY B N    1 
ATOM   9568  C CA   . GLY B 1 269 ? 34.459  -8.604  74.818  1.00 54.51  ?  278 GLY B CA   1 
ATOM   9569  C C    . GLY B 1 269 ? 34.824  -7.884  76.097  1.00 55.00  ?  278 GLY B C    1 
ATOM   9570  O O    . GLY B 1 269 ? 35.864  -8.177  76.732  1.00 50.41  ?  278 GLY B O    1 
ATOM   9571  H H    . GLY B 1 269 ? 32.794  -8.095  73.877  1.00 78.11  ?  278 GLY B H    1 
ATOM   9572  H HA2  . GLY B 1 269 ? 34.009  -9.430  75.056  1.00 65.41  ?  278 GLY B HA2  1 
ATOM   9573  H HA3  . GLY B 1 269 ? 35.281  -8.832  74.356  1.00 65.41  ?  278 GLY B HA3  1 
ATOM   9574  N N    . ILE B 1 270 ? 33.941  -7.035  76.561  1.00 61.68  ?  279 ILE B N    1 
ATOM   9575  C CA   . ILE B 1 270 ? 34.110  -6.409  77.856  1.00 55.47  ?  279 ILE B CA   1 
ATOM   9576  C C    . ILE B 1 270 ? 33.367  -7.292  78.854  1.00 78.28  ?  279 ILE B C    1 
ATOM   9577  O O    . ILE B 1 270 ? 32.138  -7.460  78.801  1.00 115.46 ?  279 ILE B O    1 
ATOM   9578  C CB   . ILE B 1 270 ? 33.577  -4.979  77.829  1.00 65.92  ?  279 ILE B CB   1 
ATOM   9579  C CG1  . ILE B 1 270 ? 34.219  -4.263  76.640  1.00 87.13  ?  279 ILE B CG1  1 
ATOM   9580  C CG2  . ILE B 1 270 ? 33.887  -4.284  79.101  1.00 65.20  ?  279 ILE B CG2  1 
ATOM   9581  C CD1  . ILE B 1 270 ? 33.560  -3.017  76.325  1.00 39.74  ?  279 ILE B CD1  1 
ATOM   9582  H H    . ILE B 1 270 ? 33.226  -6.800  76.146  1.00 74.01  ?  279 ILE B H    1 
ATOM   9583  H HA   . ILE B 1 270 ? 35.050  -6.389  78.093  1.00 66.57  ?  279 ILE B HA   1 
ATOM   9584  H HB   . ILE B 1 270 ? 32.615  -5.001  77.705  1.00 79.10  ?  279 ILE B HB   1 
ATOM   9585  H HG12 . ILE B 1 270 ? 35.146  -4.068  76.850  1.00 104.56 ?  279 ILE B HG12 1 
ATOM   9586  H HG13 . ILE B 1 270 ? 34.168  -4.836  75.859  1.00 104.56 ?  279 ILE B HG13 1 
ATOM   9587  H HG21 . ILE B 1 270 ? 33.538  -3.380  79.059  1.00 78.24  ?  279 ILE B HG21 1 
ATOM   9588  H HG22 . ILE B 1 270 ? 33.470  -4.766  79.833  1.00 78.24  ?  279 ILE B HG22 1 
ATOM   9589  H HG23 . ILE B 1 270 ? 34.849  -4.264  79.223  1.00 78.24  ?  279 ILE B HG23 1 
ATOM   9590  H HD11 . ILE B 1 270 ? 34.006  -2.607  75.567  1.00 47.68  ?  279 ILE B HD11 1 
ATOM   9591  H HD12 . ILE B 1 270 ? 32.633  -3.198  76.106  1.00 47.68  ?  279 ILE B HD12 1 
ATOM   9592  H HD13 . ILE B 1 270 ? 33.610  -2.430  77.096  1.00 47.68  ?  279 ILE B HD13 1 
ATOM   9593  N N    . GLN B 1 271 ? 34.131  -7.901  79.735  1.00 73.72  ?  280 GLN B N    1 
ATOM   9594  C CA   . GLN B 1 271 ? 33.578  -8.841  80.673  1.00 79.53  ?  280 GLN B CA   1 
ATOM   9595  C C    . GLN B 1 271 ? 32.952  -8.011  81.782  1.00 73.87  ?  280 GLN B C    1 
ATOM   9596  O O    . GLN B 1 271 ? 33.483  -7.880  82.888  1.00 70.94  ?  280 GLN B O    1 
ATOM   9597  C CB   . GLN B 1 271 ? 34.660  -9.793  81.179  1.00 92.82  ?  280 GLN B CB   1 
ATOM   9598  C CG   . GLN B 1 271 ? 35.359  -10.606 80.063  1.00 105.91 ?  280 GLN B CG   1 
ATOM   9599  C CD   . GLN B 1 271 ? 36.479  -11.536 80.574  1.00 116.43 ?  280 GLN B CD   1 
ATOM   9600  O OE1  . GLN B 1 271 ? 36.311  -12.223 81.575  1.00 141.30 ?  280 GLN B OE1  1 
ATOM   9601  N NE2  . GLN B 1 271 ? 37.613  -11.559 79.879  1.00 139.42 ?  280 GLN B NE2  1 
ATOM   9602  H H    . GLN B 1 271 ? 34.980  -7.786  79.808  1.00 88.47  ?  280 GLN B H    1 
ATOM   9603  H HA   . GLN B 1 271 ? 32.882  -9.362  80.243  1.00 95.43  ?  280 GLN B HA   1 
ATOM   9604  H HB2  . GLN B 1 271 ? 35.340  -9.275  81.638  1.00 111.39 ?  280 GLN B HB2  1 
ATOM   9605  H HB3  . GLN B 1 271 ? 34.256  -10.423 81.796  1.00 111.39 ?  280 GLN B HB3  1 
ATOM   9606  H HG2  . GLN B 1 271 ? 34.697  -11.157 79.617  1.00 127.09 ?  280 GLN B HG2  1 
ATOM   9607  H HG3  . GLN B 1 271 ? 35.754  -9.988  79.428  1.00 127.09 ?  280 GLN B HG3  1 
ATOM   9608  H HE21 . GLN B 1 271 ? 37.698  -11.069 79.178  1.00 167.31 ?  280 GLN B HE21 1 
ATOM   9609  H HE22 . GLN B 1 271 ? 38.262  -12.064 80.131  1.00 167.31 ?  280 GLN B HE22 1 
ATOM   9610  N N    . GLN B 1 272 ? 31.829  -7.385  81.445  1.00 75.69  ?  281 GLN B N    1 
ATOM   9611  C CA   . GLN B 1 272 ? 31.109  -6.649  82.478  1.00 74.85  ?  281 GLN B CA   1 
ATOM   9612  C C    . GLN B 1 272 ? 30.545  -7.609  83.514  1.00 72.32  ?  281 GLN B C    1 
ATOM   9613  O O    . GLN B 1 272 ? 30.209  -7.205  84.637  1.00 72.21  ?  281 GLN B O    1 
ATOM   9614  C CB   . GLN B 1 272 ? 29.990  -5.796  81.878  1.00 88.01  ?  281 GLN B CB   1 
ATOM   9615  C CG   . GLN B 1 272 ? 30.474  -4.626  81.044  1.00 81.85  ?  281 GLN B CG   1 
ATOM   9616  C CD   . GLN B 1 272 ? 30.937  -3.411  81.867  1.00 78.65  ?  281 GLN B CD   1 
ATOM   9617  O OE1  . GLN B 1 272 ? 31.155  -3.500  83.105  1.00 59.90  ?  281 GLN B OE1  1 
ATOM   9618  N NE2  . GLN B 1 272 ? 31.095  -2.255  81.168  1.00 48.88  ?  281 GLN B NE2  1 
ATOM   9619  H H    . GLN B 1 272 ? 31.476  -7.370  80.661  1.00 90.82  ?  281 GLN B H    1 
ATOM   9620  H HA   . GLN B 1 272 ? 31.729  -6.054  82.928  1.00 89.82  ?  281 GLN B HA   1 
ATOM   9621  H HB2  . GLN B 1 272 ? 29.443  -6.358  81.307  1.00 105.61 ?  281 GLN B HB2  1 
ATOM   9622  H HB3  . GLN B 1 272 ? 29.450  -5.440  82.600  1.00 105.61 ?  281 GLN B HB3  1 
ATOM   9623  H HG2  . GLN B 1 272 ? 31.224  -4.918  80.503  1.00 98.21  ?  281 GLN B HG2  1 
ATOM   9624  H HG3  . GLN B 1 272 ? 29.750  -4.333  80.469  1.00 98.21  ?  281 GLN B HG3  1 
ATOM   9625  H HE21 . GLN B 1 272 ? 30.938  -2.239  80.322  1.00 58.66  ?  281 GLN B HE21 1 
ATOM   9626  H HE22 . GLN B 1 272 ? 31.352  -1.540  81.571  1.00 58.66  ?  281 GLN B HE22 1 
ATOM   9627  N N    . THR B 1 273 ? 30.385  -8.862  83.155  1.00 110.60 ?  282 THR B N    1 
ATOM   9628  C CA   . THR B 1 273 ? 29.818  -9.830  84.068  1.00 112.63 ?  282 THR B CA   1 
ATOM   9629  C C    . THR B 1 273 ? 30.877  -10.590 84.853  1.00 83.96  ?  282 THR B C    1 
ATOM   9630  O O    . THR B 1 273 ? 30.541  -11.386 85.742  1.00 82.25  ?  282 THR B O    1 
ATOM   9631  C CB   . THR B 1 273 ? 28.930  -10.742 83.262  1.00 72.29  ?  282 THR B CB   1 
ATOM   9632  O OG1  . THR B 1 273 ? 29.442  -10.819 81.923  1.00 83.64  ?  282 THR B OG1  1 
ATOM   9633  C CG2  . THR B 1 273 ? 27.567  -10.233 83.239  1.00 53.44  ?  282 THR B CG2  1 
ATOM   9634  H H    . THR B 1 273 ? 30.598  -9.181  82.385  1.00 132.72 ?  282 THR B H    1 
ATOM   9635  H HA   . THR B 1 273 ? 29.258  -9.363  84.708  1.00 135.15 ?  282 THR B HA   1 
ATOM   9636  H HB   . THR B 1 273 ? 28.924  -11.626 83.661  1.00 86.75  ?  282 THR B HB   1 
ATOM   9637  H HG1  . THR B 1 273 ? 28.957  -11.325 81.459  1.00 100.37 ?  282 THR B HG1  1 
ATOM   9638  H HG21 . THR B 1 273 ? 27.001  -10.824 82.718  1.00 64.13  ?  282 THR B HG21 1 
ATOM   9639  H HG22 . THR B 1 273 ? 27.218  -10.177 84.142  1.00 64.13  ?  282 THR B HG22 1 
ATOM   9640  H HG23 . THR B 1 273 ? 27.550  -9.349  82.839  1.00 64.13  ?  282 THR B HG23 1 
ATOM   9641  N N    . ALA B 1 274 ? 32.140  -10.276 84.634  1.00 145.39 ?  283 ALA B N    1 
ATOM   9642  C CA   . ALA B 1 274 ? 33.211  -10.953 85.333  1.00 94.54  ?  283 ALA B CA   1 
ATOM   9643  C C    . ALA B 1 274 ? 33.597  -10.239 86.627  1.00 127.34 ?  283 ALA B C    1 
ATOM   9644  O O    . ALA B 1 274 ? 33.163  -9.126  86.917  1.00 151.86 ?  283 ALA B O    1 
ATOM   9645  C CB   . ALA B 1 274 ? 34.420  -11.056 84.422  1.00 80.34  ?  283 ALA B CB   1 
ATOM   9646  H H    . ALA B 1 274 ? 32.405  -9.671  84.083  1.00 174.47 ?  283 ALA B H    1 
ATOM   9647  H HA   . ALA B 1 274 ? 32.925  -11.852 85.558  1.00 113.45 ?  283 ALA B HA   1 
ATOM   9648  H HB1  . ALA B 1 274 ? 35.134  -11.510 84.895  1.00 96.41  ?  283 ALA B HB1  1 
ATOM   9649  H HB2  . ALA B 1 274 ? 34.176  -11.559 83.629  1.00 96.41  ?  283 ALA B HB2  1 
ATOM   9650  H HB3  . ALA B 1 274 ? 34.704  -10.162 84.173  1.00 96.41  ?  283 ALA B HB3  1 
ATOM   9651  N N    . GLY B 1 275 ? 34.426  -10.925 87.417  1.00 102.12 ?  284 GLY B N    1 
ATOM   9652  C CA   . GLY B 1 275 ? 35.003  -10.410 88.628  1.00 80.72  ?  284 GLY B CA   1 
ATOM   9653  C C    . GLY B 1 275 ? 34.267  -10.702 89.909  1.00 100.93 ?  284 GLY B C    1 
ATOM   9654  O O    . GLY B 1 275 ? 34.909  -10.858 90.940  1.00 114.58 ?  284 GLY B O    1 
ATOM   9655  H H    . GLY B 1 275 ? 34.673  -11.732 87.249  1.00 122.54 ?  284 GLY B H    1 
ATOM   9656  H HA2  . GLY B 1 275 ? 35.900  -10.769 88.719  1.00 96.86  ?  284 GLY B HA2  1 
ATOM   9657  H HA3  . GLY B 1 275 ? 35.078  -9.446  88.548  1.00 96.86  ?  284 GLY B HA3  1 
ATOM   9658  N N    . GLY B 1 276 ? 32.949  -10.794 89.877  1.00 149.66 ?  285 GLY B N    1 
ATOM   9659  C CA   . GLY B 1 276 ? 32.194  -11.140 91.066  1.00 101.86 ?  285 GLY B CA   1 
ATOM   9660  C C    . GLY B 1 276 ? 31.781  -9.962  91.926  1.00 101.25 ?  285 GLY B C    1 
ATOM   9661  O O    . GLY B 1 276 ? 31.458  -10.156 93.111  1.00 83.34  ?  285 GLY B O    1 
ATOM   9662  H H    . GLY B 1 276 ? 32.467  -10.661 89.177  1.00 179.59 ?  285 GLY B H    1 
ATOM   9663  H HA2  . GLY B 1 276 ? 31.389  -11.613 90.801  1.00 122.23 ?  285 GLY B HA2  1 
ATOM   9664  H HA3  . GLY B 1 276 ? 32.726  -11.738 91.614  1.00 122.23 ?  285 GLY B HA3  1 
ATOM   9665  N N    . GLY B 1 277 ? 31.870  -8.745  91.394  1.00 120.14 ?  286 GLY B N    1 
ATOM   9666  C CA   . GLY B 1 277 ? 31.466  -7.546  92.108  1.00 113.67 ?  286 GLY B CA   1 
ATOM   9667  C C    . GLY B 1 277 ? 29.957  -7.347  92.221  1.00 109.00 ?  286 GLY B C    1 
ATOM   9668  O O    . GLY B 1 277 ? 29.149  -7.982  91.553  1.00 63.52  ?  286 GLY B O    1 
ATOM   9669  H H    . GLY B 1 277 ? 32.169  -8.590  90.602  1.00 144.17 ?  286 GLY B H    1 
ATOM   9670  H HA2  . GLY B 1 277 ? 31.832  -7.575  93.006  1.00 136.41 ?  286 GLY B HA2  1 
ATOM   9671  H HA3  . GLY B 1 277 ? 31.837  -6.771  91.657  1.00 136.41 ?  286 GLY B HA3  1 
ATOM   9672  N N    . HIS B 1 278 ? 29.556  -6.403  93.068  1.00 102.05 ?  287 HIS B N    1 
ATOM   9673  C CA   . HIS B 1 278 ? 28.133  -6.109  93.154  1.00 88.61  ?  287 HIS B CA   1 
ATOM   9674  C C    . HIS B 1 278 ? 27.601  -5.770  91.776  1.00 69.04  ?  287 HIS B C    1 
ATOM   9675  O O    . HIS B 1 278 ? 26.590  -6.314  91.304  1.00 55.68  ?  287 HIS B O    1 
ATOM   9676  C CB   . HIS B 1 278 ? 27.890  -4.942  94.102  1.00 113.62 ?  287 HIS B CB   1 
ATOM   9677  C CG   . HIS B 1 278 ? 26.455  -4.515  94.180  1.00 103.36 ?  287 HIS B CG   1 
ATOM   9678  H H    . HIS B 1 278 ? 30.063  -5.937  93.582  1.00 122.46 ?  287 HIS B H    1 
ATOM   9679  H HA   . HIS B 1 278 ? 27.658  -6.886  93.489  1.00 106.33 ?  287 HIS B HA   1 
ATOM   9680  H HB2  . HIS B 1 278 ? 28.172  -5.201  94.993  1.00 136.34 ?  287 HIS B HB2  1 
ATOM   9681  H HB3  . HIS B 1 278 ? 28.410  -4.181  93.800  1.00 136.34 ?  287 HIS B HB3  1 
ATOM   9682  N N    . ALA B 1 279 ? 28.344  -4.981  91.048  1.00 81.53  ?  288 ALA B N    1 
ATOM   9683  C CA   . ALA B 1 279 ? 27.832  -4.618  89.746  1.00 62.19  ?  288 ALA B CA   1 
ATOM   9684  C C    . ALA B 1 279 ? 27.783  -5.787  88.827  1.00 75.10  ?  288 ALA B C    1 
ATOM   9685  O O    . ALA B 1 279 ? 27.008  -5.766  87.872  1.00 62.29  ?  288 ALA B O    1 
ATOM   9686  C CB   . ALA B 1 279 ? 28.709  -3.572  89.113  1.00 63.92  ?  288 ALA B CB   1 
ATOM   9687  H H    . ALA B 1 279 ? 29.110  -4.653  91.263  1.00 97.84  ?  288 ALA B H    1 
ATOM   9688  H HA   . ALA B 1 279 ? 26.936  -4.258  89.837  1.00 74.62  ?  288 ALA B HA   1 
ATOM   9689  H HB1  . ALA B 1 279 ? 28.348  -3.343  88.242  1.00 76.70  ?  288 ALA B HB1  1 
ATOM   9690  H HB2  . ALA B 1 279 ? 28.723  -2.787  89.683  1.00 76.70  ?  288 ALA B HB2  1 
ATOM   9691  H HB3  . ALA B 1 279 ? 29.606  -3.928  89.017  1.00 76.70  ?  288 ALA B HB3  1 
ATOM   9692  N N    . ALA B 1 280 ? 28.694  -6.746  89.013  1.00 119.34 ?  289 ALA B N    1 
ATOM   9693  C CA   . ALA B 1 280 ? 28.736  -7.891  88.121  1.00 110.21 ?  289 ALA B CA   1 
ATOM   9694  C C    . ALA B 1 280 ? 27.512  -8.783  88.320  1.00 76.21  ?  289 ALA B C    1 
ATOM   9695  O O    . ALA B 1 280 ? 26.925  -9.205  87.344  1.00 59.36  ?  289 ALA B O    1 
ATOM   9696  C CB   . ALA B 1 280 ? 30.042  -8.653  88.310  1.00 134.82 ?  289 ALA B CB   1 
ATOM   9697  H H    . ALA B 1 280 ? 29.285  -6.753  89.638  1.00 143.20 ?  289 ALA B H    1 
ATOM   9698  H HA   . ALA B 1 280 ? 28.716  -7.569  87.206  1.00 132.26 ?  289 ALA B HA   1 
ATOM   9699  H HB1  . ALA B 1 280 ? 30.053  -9.413  87.707  1.00 161.79 ?  289 ALA B HB1  1 
ATOM   9700  H HB2  . ALA B 1 280 ? 30.784  -8.061  88.111  1.00 161.79 ?  289 ALA B HB2  1 
ATOM   9701  H HB3  . ALA B 1 280 ? 30.098  -8.958  89.229  1.00 161.79 ?  289 ALA B HB3  1 
ATOM   9702  N N    . GLN B 1 281 ? 27.054  -9.007  89.555  1.00 71.33  ?  290 GLN B N    1 
ATOM   9703  C CA   . GLN B 1 281 ? 25.856  -9.813  89.770  1.00 95.60  ?  290 GLN B CA   1 
ATOM   9704  C C    . GLN B 1 281 ? 24.642  -9.132  89.168  1.00 103.34 ?  290 GLN B C    1 
ATOM   9705  O O    . GLN B 1 281 ? 23.751  -9.796  88.625  1.00 118.96 ?  290 GLN B O    1 
ATOM   9706  C CB   . GLN B 1 281 ? 25.596  -10.026 91.275  1.00 63.92  ?  290 GLN B CB   1 
ATOM   9707  H H    . GLN B 1 281 ? 27.415  -8.705  90.275  1.00 85.60  ?  290 GLN B H    1 
ATOM   9708  H HA   . GLN B 1 281 ? 25.967  -10.680 89.348  1.00 114.72 ?  290 GLN B HA   1 
ATOM   9709  N N    . PHE B 1 282 ? 24.592  -7.805  89.267  1.00 92.28  ?  291 PHE B N    1 
ATOM   9710  C CA   . PHE B 1 282 ? 23.371  -7.076  88.930  1.00 70.84  ?  291 PHE B CA   1 
ATOM   9711  C C    . PHE B 1 282 ? 23.011  -7.211  87.475  1.00 64.98  ?  291 PHE B C    1 
ATOM   9712  O O    . PHE B 1 282 ? 21.833  -7.325  87.115  1.00 83.57  ?  291 PHE B O    1 
ATOM   9713  C CB   . PHE B 1 282 ? 23.510  -5.583  89.238  1.00 63.66  ?  291 PHE B CB   1 
ATOM   9714  C CG   . PHE B 1 282 ? 22.243  -4.796  88.982  1.00 75.96  ?  291 PHE B CG   1 
ATOM   9715  C CD1  . PHE B 1 282 ? 21.236  -4.768  89.931  1.00 67.65  ?  291 PHE B CD1  1 
ATOM   9716  C CD2  . PHE B 1 282 ? 22.065  -4.065  87.819  1.00 88.87  ?  291 PHE B CD2  1 
ATOM   9717  C CE1  . PHE B 1 282 ? 20.105  -4.052  89.737  1.00 64.98  ?  291 PHE B CE1  1 
ATOM   9718  C CE2  . PHE B 1 282 ? 20.898  -3.330  87.611  1.00 55.11  ?  291 PHE B CE2  1 
ATOM   9719  C CZ   . PHE B 1 282 ? 19.924  -3.327  88.561  1.00 52.85  ?  291 PHE B CZ   1 
ATOM   9720  H H    . PHE B 1 282 ? 25.244  -7.308  89.525  1.00 110.74 ?  291 PHE B H    1 
ATOM   9721  H HA   . PHE B 1 282 ? 22.636  -7.427  89.457  1.00 85.00  ?  291 PHE B HA   1 
ATOM   9722  H HB2  . PHE B 1 282 ? 23.744  -5.476  90.173  1.00 76.40  ?  291 PHE B HB2  1 
ATOM   9723  H HB3  . PHE B 1 282 ? 24.210  -5.211  88.678  1.00 76.40  ?  291 PHE B HB3  1 
ATOM   9724  H HD1  . PHE B 1 282 ? 21.342  -5.246  90.722  1.00 81.18  ?  291 PHE B HD1  1 
ATOM   9725  H HD2  . PHE B 1 282 ? 22.730  -4.065  87.169  1.00 106.64 ?  291 PHE B HD2  1 
ATOM   9726  H HE1  . PHE B 1 282 ? 19.439  -4.054  90.387  1.00 77.97  ?  291 PHE B HE1  1 
ATOM   9727  H HE2  . PHE B 1 282 ? 20.784  -2.847  86.824  1.00 66.14  ?  291 PHE B HE2  1 
ATOM   9728  H HZ   . PHE B 1 282 ? 19.143  -2.841  88.428  1.00 63.43  ?  291 PHE B HZ   1 
ATOM   9729  N N    . LEU B 1 283 ? 24.010  -7.131  86.626  1.00 45.70  ?  292 LEU B N    1 
ATOM   9730  C CA   . LEU B 1 283 ? 23.792  -7.232  85.202  1.00 47.01  ?  292 LEU B CA   1 
ATOM   9731  C C    . LEU B 1 283 ? 23.364  -8.628  84.802  1.00 92.99  ?  292 LEU B C    1 
ATOM   9732  O O    . LEU B 1 283 ? 22.653  -8.780  83.813  1.00 67.52  ?  292 LEU B O    1 
ATOM   9733  C CB   . LEU B 1 283 ? 25.081  -6.835  84.492  1.00 87.40  ?  292 LEU B CB   1 
ATOM   9734  C CG   . LEU B 1 283 ? 25.514  -5.363  84.461  1.00 74.13  ?  292 LEU B CG   1 
ATOM   9735  C CD1  . LEU B 1 283 ? 27.089  -5.263  84.221  1.00 75.69  ?  292 LEU B CD1  1 
ATOM   9736  C CD2  . LEU B 1 283 ? 24.798  -4.635  83.361  1.00 122.23 ?  292 LEU B CD2  1 
ATOM   9737  H H    . LEU B 1 283 ? 24.832  -7.017  86.851  1.00 54.84  ?  292 LEU B H    1 
ATOM   9738  H HA   . LEU B 1 283 ? 23.094  -6.612  84.939  1.00 56.41  ?  292 LEU B HA   1 
ATOM   9739  H HB2  . LEU B 1 283 ? 25.806  -7.326  84.909  1.00 104.88 ?  292 LEU B HB2  1 
ATOM   9740  H HB3  . LEU B 1 283 ? 25.004  -7.119  83.568  1.00 104.88 ?  292 LEU B HB3  1 
ATOM   9741  H HG   . LEU B 1 283 ? 25.299  -4.939  85.306  1.00 88.96  ?  292 LEU B HG   1 
ATOM   9742  H HD11 . LEU B 1 283 ? 27.347  -4.328  84.204  1.00 90.82  ?  292 LEU B HD11 1 
ATOM   9743  H HD12 . LEU B 1 283 ? 27.547  -5.719  84.944  1.00 90.82  ?  292 LEU B HD12 1 
ATOM   9744  H HD13 . LEU B 1 283 ? 27.307  -5.682  83.374  1.00 90.82  ?  292 LEU B HD13 1 
ATOM   9745  H HD21 . LEU B 1 283 ? 25.085  -3.708  83.357  1.00 146.68 ?  292 LEU B HD21 1 
ATOM   9746  H HD22 . LEU B 1 283 ? 25.016  -5.053  82.513  1.00 146.68 ?  292 LEU B HD22 1 
ATOM   9747  H HD23 . LEU B 1 283 ? 23.843  -4.686  83.519  1.00 146.68 ?  292 LEU B HD23 1 
ATOM   9748  N N    . GLN B 1 284 ? 23.843  -9.656  85.497  1.00 84.64  ?  293 GLN B N    1 
ATOM   9749  C CA   . GLN B 1 284 ? 23.403  -11.002 85.179  1.00 87.43  ?  293 GLN B CA   1 
ATOM   9750  C C    . GLN B 1 284 ? 21.969  -11.185 85.661  1.00 92.57  ?  293 GLN B C    1 
ATOM   9751  O O    . GLN B 1 284 ? 21.118  -11.724 84.951  1.00 107.53 ?  293 GLN B O    1 
ATOM   9752  C CB   . GLN B 1 284 ? 24.371  -12.011 85.817  1.00 91.98  ?  293 GLN B CB   1 
ATOM   9753  C CG   . GLN B 1 284 ? 24.252  -13.442 85.322  1.00 76.07  ?  293 GLN B CG   1 
ATOM   9754  C CD   . GLN B 1 284 ? 24.732  -13.618 83.873  1.00 60.03  ?  293 GLN B CD   1 
ATOM   9755  O OE1  . GLN B 1 284 ? 25.891  -13.416 83.562  1.00 108.78 ?  293 GLN B OE1  1 
ATOM   9756  N NE2  . GLN B 1 284 ? 23.798  -13.929 82.977  1.00 58.22  ?  293 GLN B NE2  1 
ATOM   9757  H H    . GLN B 1 284 ? 24.410  -9.600  86.142  1.00 101.57 ?  293 GLN B H    1 
ATOM   9758  H HA   . GLN B 1 284 ? 23.421  -11.128 84.217  1.00 104.92 ?  293 GLN B HA   1 
ATOM   9759  H HB2  . GLN B 1 284 ? 25.279  -11.718 85.641  1.00 110.38 ?  293 GLN B HB2  1 
ATOM   9760  H HB3  . GLN B 1 284 ? 24.215  -12.022 86.774  1.00 110.38 ?  293 GLN B HB3  1 
ATOM   9761  H HG2  . GLN B 1 284 ? 24.790  -14.017 85.887  1.00 91.29  ?  293 GLN B HG2  1 
ATOM   9762  H HG3  . GLN B 1 284 ? 23.321  -13.713 85.363  1.00 91.29  ?  293 GLN B HG3  1 
ATOM   9763  H HE21 . GLN B 1 284 ? 22.979  -14.020 83.223  1.00 69.86  ?  293 GLN B HE21 1 
ATOM   9764  H HE22 . GLN B 1 284 ? 24.013  -14.039 82.152  1.00 69.86  ?  293 GLN B HE22 1 
ATOM   9765  N N    . ASP B 1 285 ? 21.688  -10.690 86.860  1.00 92.27  ?  294 ASP B N    1 
ATOM   9766  C CA   . ASP B 1 285 ? 20.362  -10.803 87.445  1.00 82.83  ?  294 ASP B CA   1 
ATOM   9767  C C    . ASP B 1 285 ? 19.335  -10.007 86.651  1.00 79.65  ?  294 ASP B C    1 
ATOM   9768  O O    . ASP B 1 285 ? 18.208  -10.462 86.460  1.00 75.11  ?  294 ASP B O    1 
ATOM   9769  C CB   . ASP B 1 285 ? 20.408  -10.357 88.903  1.00 81.37  ?  294 ASP B CB   1 
ATOM   9770  H H    . ASP B 1 285 ? 22.255  -10.279 87.359  1.00 110.73 ?  294 ASP B H    1 
ATOM   9771  H HA   . ASP B 1 285 ? 20.092  -11.735 87.429  1.00 99.40  ?  294 ASP B HA   1 
ATOM   9772  H HB2  . ASP B 1 285 ? 20.700  -9.432  88.941  1.00 97.65  ?  294 ASP B HB2  1 
ATOM   9773  H HB3  . ASP B 1 285 ? 19.522  -10.441 89.288  1.00 97.65  ?  294 ASP B HB3  1 
ATOM   9774  N N    . MET B 1 286 ? 19.678  -8.805  86.223  1.00 144.61 ?  295 MET B N    1 
ATOM   9775  C CA   . MET B 1 286 ? 18.721  -8.103  85.403  1.00 214.07 ?  295 MET B CA   1 
ATOM   9776  C C    . MET B 1 286 ? 18.571  -8.757  84.056  1.00 95.52  ?  295 MET B C    1 
ATOM   9777  O O    . MET B 1 286 ? 17.758  -8.316  83.268  1.00 42.76  ?  295 MET B O    1 
ATOM   9778  C CB   . MET B 1 286 ? 19.116  -6.660  85.148  1.00 433.07 ?  295 MET B CB   1 
ATOM   9779  C CG   . MET B 1 286 ? 18.866  -5.671  86.247  1.00 651.59 ?  295 MET B CG   1 
ATOM   9780  S SD   . MET B 1 286 ? 17.157  -5.599  86.810  1.00 1031.7 ?  295 MET B SD   1 
ATOM   9781  C CE   . MET B 1 286 ? 17.313  -6.528  88.319  1.00 737.35 ?  295 MET B CE   1 
ATOM   9782  H H    . MET B 1 286 ? 20.417  -8.395  86.382  1.00 173.53 ?  295 MET B H    1 
ATOM   9783  H HA   . MET B 1 286 ? 17.861  -8.104  85.852  1.00 256.88 ?  295 MET B HA   1 
ATOM   9784  H HB2  . MET B 1 286 ? 20.066  -6.639  84.956  1.00 519.68 ?  295 MET B HB2  1 
ATOM   9785  H HB3  . MET B 1 286 ? 18.628  -6.349  84.369  1.00 519.68 ?  295 MET B HB3  1 
ATOM   9786  H HG2  . MET B 1 286 ? 19.417  -5.908  87.009  1.00 781.90 ?  295 MET B HG2  1 
ATOM   9787  H HG3  . MET B 1 286 ? 19.109  -4.787  85.931  1.00 781.90 ?  295 MET B HG3  1 
ATOM   9788  H HE1  . MET B 1 286 ? 16.446  -6.578  88.750  1.00 884.82 ?  295 MET B HE1  1 
ATOM   9789  H HE2  . MET B 1 286 ? 17.631  -7.420  88.108  1.00 884.82 ?  295 MET B HE2  1 
ATOM   9790  H HE3  . MET B 1 286 ? 17.947  -6.080  88.900  1.00 884.82 ?  295 MET B HE3  1 
ATOM   9791  N N    . ARG B 1 287 ? 19.409  -9.705  83.693  1.00 81.66  ?  296 ARG B N    1 
ATOM   9792  C CA   . ARG B 1 287 ? 19.187  -10.380 82.408  1.00 79.13  ?  296 ARG B CA   1 
ATOM   9793  C C    . ARG B 1 287 ? 17.929  -11.224 82.395  1.00 74.15  ?  296 ARG B C    1 
ATOM   9794  O O    . ARG B 1 287 ? 17.399  -11.524 81.310  1.00 47.44  ?  296 ARG B O    1 
ATOM   9795  C CB   . ARG B 1 287 ? 20.350  -11.265 82.026  1.00 64.01  ?  296 ARG B CB   1 
ATOM   9796  C CG   . ARG B 1 287 ? 21.528  -10.486 81.591  1.00 65.23  ?  296 ARG B CG   1 
ATOM   9797  C CD   . ARG B 1 287 ? 22.414  -11.291 80.720  1.00 69.47  ?  296 ARG B CD   1 
ATOM   9798  N NE   . ARG B 1 287 ? 23.616  -10.591 80.314  1.00 69.62  ?  296 ARG B NE   1 
ATOM   9799  C CZ   . ARG B 1 287 ? 24.691  -11.179 79.804  1.00 65.70  ?  296 ARG B CZ   1 
ATOM   9800  N NH1  . ARG B 1 287 ? 24.738  -12.495 79.662  1.00 65.21  1  296 ARG B NH1  1 
ATOM   9801  N NH2  . ARG B 1 287 ? 25.745  -10.439 79.493  1.00 98.01  1  296 ARG B NH2  1 
ATOM   9802  H H    . ARG B 1 287 ? 20.090  -9.976  84.143  1.00 97.99  ?  296 ARG B H    1 
ATOM   9803  H HA   . ARG B 1 287 ? 19.094  -9.705  81.718  1.00 94.96  ?  296 ARG B HA   1 
ATOM   9804  H HB2  . ARG B 1 287 ? 20.608  -11.800 82.793  1.00 76.81  ?  296 ARG B HB2  1 
ATOM   9805  H HB3  . ARG B 1 287 ? 20.082  -11.842 81.293  1.00 76.81  ?  296 ARG B HB3  1 
ATOM   9806  H HG2  . ARG B 1 287 ? 21.232  -9.710  81.090  1.00 78.28  ?  296 ARG B HG2  1 
ATOM   9807  H HG3  . ARG B 1 287 ? 22.036  -10.211 82.370  1.00 78.28  ?  296 ARG B HG3  1 
ATOM   9808  H HD2  . ARG B 1 287 ? 22.682  -12.090 81.199  1.00 83.36  ?  296 ARG B HD2  1 
ATOM   9809  H HD3  . ARG B 1 287 ? 21.927  -11.535 79.917  1.00 83.36  ?  296 ARG B HD3  1 
ATOM   9810  H HE   . ARG B 1 287 ? 23.634  -9.736  80.409  1.00 83.54  ?  296 ARG B HE   1 
ATOM   9811  H HH11 . ARG B 1 287 ? 24.058  -12.975 79.875  1.00 78.25  ?  296 ARG B HH11 1 
ATOM   9812  H HH12 . ARG B 1 287 ? 25.442  -12.867 79.337  1.00 78.25  ?  296 ARG B HH12 1 
ATOM   9813  H HH21 . ARG B 1 287 ? 25.714  -9.586  79.591  1.00 117.61 ?  296 ARG B HH21 1 
ATOM   9814  H HH22 . ARG B 1 287 ? 26.448  -10.810 79.164  1.00 117.61 ?  296 ARG B HH22 1 
ATOM   9815  N N    . ARG B 1 288 ? 17.518  -11.695 83.569  1.00 77.29  ?  297 ARG B N    1 
ATOM   9816  C CA   . ARG B 1 288 ? 16.312  -12.466 83.761  1.00 58.38  ?  297 ARG B CA   1 
ATOM   9817  C C    . ARG B 1 288 ? 15.092  -11.566 83.647  1.00 73.14  ?  297 ARG B C    1 
ATOM   9818  O O    . ARG B 1 288 ? 13.970  -12.087 83.581  1.00 100.24 ?  297 ARG B O    1 
ATOM   9819  C CB   . ARG B 1 288 ? 16.370  -13.155 85.144  1.00 52.02  ?  297 ARG B CB   1 
ATOM   9820  H H    . ARG B 1 288 ? 17.951  -11.568 84.301  1.00 92.75  ?  297 ARG B H    1 
ATOM   9821  H HA   . ARG B 1 288 ? 16.253  -13.152 83.078  1.00 70.06  ?  297 ARG B HA   1 
ATOM   9822  N N    . TYR B 1 289 ? 15.304  -10.232 83.615  1.00 76.73  ?  298 TYR B N    1 
ATOM   9823  C CA   . TYR B 1 289 ? 14.241  -9.228  83.536  1.00 60.56  ?  298 TYR B CA   1 
ATOM   9824  C C    . TYR B 1 289 ? 14.021  -8.721  82.138  1.00 53.59  ?  298 TYR B C    1 
ATOM   9825  O O    . TYR B 1 289 ? 13.270  -7.764  81.964  1.00 48.04  ?  298 TYR B O    1 
ATOM   9826  C CB   . TYR B 1 289 ? 14.516  -8.010  84.417  1.00 45.06  ?  298 TYR B CB   1 
ATOM   9827  C CG   . TYR B 1 289 ? 14.463  -8.257  85.895  1.00 52.16  ?  298 TYR B CG   1 
ATOM   9828  C CD1  . TYR B 1 289 ? 15.414  -9.051  86.521  1.00 68.37  ?  298 TYR B CD1  1 
ATOM   9829  C CD2  . TYR B 1 289 ? 13.445  -7.706  86.669  1.00 62.31  ?  298 TYR B CD2  1 
ATOM   9830  C CE1  . TYR B 1 289 ? 15.357  -9.280  87.859  1.00 64.33  ?  298 TYR B CE1  1 
ATOM   9831  C CE2  . TYR B 1 289 ? 13.380  -7.938  88.006  1.00 52.87  ?  298 TYR B CE2  1 
ATOM   9832  C CZ   . TYR B 1 289 ? 14.310  -8.713  88.595  1.00 50.74  ?  298 TYR B CZ   1 
ATOM   9833  O OH   . TYR B 1 289 ? 14.205  -8.895  89.940  1.00 59.86  ?  298 TYR B OH   1 
ATOM   9834  H H    . TYR B 1 289 ? 16.089  -9.882  83.639  1.00 92.07  ?  298 TYR B H    1 
ATOM   9835  H HA   . TYR B 1 289 ? 13.411  -9.630  83.838  1.00 72.67  ?  298 TYR B HA   1 
ATOM   9836  H HB2  . TYR B 1 289 ? 15.403  -7.676  84.209  1.00 54.08  ?  298 TYR B HB2  1 
ATOM   9837  H HB3  . TYR B 1 289 ? 13.858  -7.327  84.212  1.00 54.08  ?  298 TYR B HB3  1 
ATOM   9838  H HD1  . TYR B 1 289 ? 16.100  -9.429  86.019  1.00 82.05  ?  298 TYR B HD1  1 
ATOM   9839  H HD2  . TYR B 1 289 ? 12.796  -7.177  86.263  1.00 74.77  ?  298 TYR B HD2  1 
ATOM   9840  H HE1  . TYR B 1 289 ? 15.996  -9.811  88.276  1.00 77.20  ?  298 TYR B HE1  1 
ATOM   9841  H HE2  . TYR B 1 289 ? 12.696  -7.562  88.513  1.00 63.44  ?  298 TYR B HE2  1 
ATOM   9842  H HH   . TYR B 1 289 ? 14.838  -9.373  90.216  1.00 71.83  ?  298 TYR B HH   1 
ATOM   9843  N N    . MET B 1 290 ? 14.668  -9.288  81.173  1.00 56.55  ?  299 MET B N    1 
ATOM   9844  C CA   . MET B 1 290 ? 14.450  -8.966  79.775  1.00 59.73  ?  299 MET B CA   1 
ATOM   9845  C C    . MET B 1 290 ? 13.530  -9.992  79.116  1.00 69.05  ?  299 MET B C    1 
ATOM   9846  O O    . MET B 1 290 ? 13.289  -11.068 79.666  1.00 88.99  ?  299 MET B O    1 
ATOM   9847  C CB   . MET B 1 290 ? 15.776  -8.967  79.044  1.00 69.70  ?  299 MET B CB   1 
ATOM   9848  C CG   . MET B 1 290 ? 16.826  -7.952  79.461  1.00 93.04  ?  299 MET B CG   1 
ATOM   9849  S SD   . MET B 1 290 ? 18.307  -8.176  78.535  1.00 340.16 ?  299 MET B SD   1 
ATOM   9850  C CE   . MET B 1 290 ? 19.276  -7.077  79.470  1.00 54.84  ?  299 MET B CE   1 
ATOM   9851  H H    . MET B 1 290 ? 15.268  -9.892  81.293  1.00 67.86  ?  299 MET B H    1 
ATOM   9852  H HA   . MET B 1 290 ? 14.057  -8.082  79.702  1.00 71.68  ?  299 MET B HA   1 
ATOM   9853  H HB2  . MET B 1 290 ? 16.174  -9.845  79.153  1.00 83.63  ?  299 MET B HB2  1 
ATOM   9854  H HB3  . MET B 1 290 ? 15.596  -8.816  78.103  1.00 83.63  ?  299 MET B HB3  1 
ATOM   9855  H HG2  . MET B 1 290 ? 16.492  -7.056  79.295  1.00 111.65 ?  299 MET B HG2  1 
ATOM   9856  H HG3  . MET B 1 290 ? 17.031  -8.068  80.402  1.00 111.65 ?  299 MET B HG3  1 
ATOM   9857  H HE1  . MET B 1 290 ? 20.173  -7.057  79.102  1.00 65.81  ?  299 MET B HE1  1 
ATOM   9858  H HE2  . MET B 1 290 ? 18.880  -6.193  79.426  1.00 65.81  ?  299 MET B HE2  1 
ATOM   9859  H HE3  . MET B 1 290 ? 19.302  -7.384  80.390  1.00 65.81  ?  299 MET B HE3  1 
ATOM   9860  N N    . PRO B 1 291 ? 12.952  -9.689  77.960  1.00 81.86  ?  300 PRO B N    1 
ATOM   9861  C CA   . PRO B 1 291 ? 12.240  -10.708 77.232  1.00 85.88  ?  300 PRO B CA   1 
ATOM   9862  C C    . PRO B 1 291 ? 13.131  -11.916 77.109  1.00 63.74  ?  300 PRO B C    1 
ATOM   9863  O O    . PRO B 1 291 ? 14.335  -11.757 76.935  1.00 64.34  ?  300 PRO B O    1 
ATOM   9864  C CB   . PRO B 1 291 ? 11.986  -10.074 75.858  1.00 72.66  ?  300 PRO B CB   1 
ATOM   9865  C CG   . PRO B 1 291 ? 11.966  -8.656  76.108  1.00 61.76  ?  300 PRO B CG   1 
ATOM   9866  C CD   . PRO B 1 291 ? 12.893  -8.399  77.268  1.00 58.73  ?  300 PRO B CD   1 
ATOM   9867  H HA   . PRO B 1 291 ? 11.403  -10.939 77.664  1.00 103.06 ?  300 PRO B HA   1 
ATOM   9868  H HB2  . PRO B 1 291 ? 12.707  -10.307 75.251  1.00 87.19  ?  300 PRO B HB2  1 
ATOM   9869  H HB3  . PRO B 1 291 ? 11.132  -10.375 75.510  1.00 87.19  ?  300 PRO B HB3  1 
ATOM   9870  H HG2  . PRO B 1 291 ? 12.276  -8.186  75.318  1.00 74.11  ?  300 PRO B HG2  1 
ATOM   9871  H HG3  . PRO B 1 291 ? 11.063  -8.383  76.331  1.00 74.11  ?  300 PRO B HG3  1 
ATOM   9872  H HD2  . PRO B 1 291 ? 13.773  -8.148  76.947  1.00 70.47  ?  300 PRO B HD2  1 
ATOM   9873  H HD3  . PRO B 1 291 ? 12.521  -7.720  77.852  1.00 70.47  ?  300 PRO B HD3  1 
ATOM   9874  N N    . PRO B 1 292 ? 12.580  -13.117 77.159  1.00 77.59  ?  301 PRO B N    1 
ATOM   9875  C CA   . PRO B 1 292 ? 13.434  -14.291 77.046  1.00 79.90  ?  301 PRO B CA   1 
ATOM   9876  C C    . PRO B 1 292 ? 14.183  -14.282 75.729  1.00 85.89  ?  301 PRO B C    1 
ATOM   9877  O O    . PRO B 1 292 ? 15.368  -14.617 75.708  1.00 93.04  ?  301 PRO B O    1 
ATOM   9878  C CB   . PRO B 1 292 ? 12.439  -15.430 77.132  1.00 88.81  ?  301 PRO B CB   1 
ATOM   9879  C CG   . PRO B 1 292 ? 11.235  -14.873 76.501  1.00 92.50  ?  301 PRO B CG   1 
ATOM   9880  C CD   . PRO B 1 292 ? 11.200  -13.418 76.746  1.00 85.66  ?  301 PRO B CD   1 
ATOM   9881  H HA   . PRO B 1 292 ? 14.059  -14.340 77.786  1.00 95.88  ?  301 PRO B HA   1 
ATOM   9882  H HB2  . PRO B 1 292 ? 12.768  -16.197 76.638  1.00 106.57 ?  301 PRO B HB2  1 
ATOM   9883  H HB3  . PRO B 1 292 ? 12.273  -15.656 78.061  1.00 106.57 ?  301 PRO B HB3  1 
ATOM   9884  H HG2  . PRO B 1 292 ? 11.268  -15.048 75.548  1.00 111.00 ?  301 PRO B HG2  1 
ATOM   9885  H HG3  . PRO B 1 292 ? 10.452  -15.293 76.889  1.00 111.00 ?  301 PRO B HG3  1 
ATOM   9886  H HD2  . PRO B 1 292 ? 10.978  -12.942 75.931  1.00 102.79 ?  301 PRO B HD2  1 
ATOM   9887  H HD3  . PRO B 1 292 ? 10.578  -13.209 77.461  1.00 102.79 ?  301 PRO B HD3  1 
ATOM   9888  N N    . ALA B 1 293 ? 13.529  -13.902 74.621  1.00 95.87  ?  302 ALA B N    1 
ATOM   9889  C CA   . ALA B 1 293 ? 14.219  -13.884 73.332  1.00 70.93  ?  302 ALA B CA   1 
ATOM   9890  C C    . ALA B 1 293 ? 15.473  -13.024 73.400  1.00 107.71 ?  302 ALA B C    1 
ATOM   9891  O O    . ALA B 1 293 ? 16.528  -13.362 72.843  1.00 70.90  ?  302 ALA B O    1 
ATOM   9892  C CB   . ALA B 1 293 ? 13.309  -13.309 72.252  1.00 58.51  ?  302 ALA B CB   1 
ATOM   9893  H H    . ALA B 1 293 ? 12.705  -13.657 74.592  1.00 115.05 ?  302 ALA B H    1 
ATOM   9894  H HA   . ALA B 1 293 ? 14.472  -14.786 73.081  1.00 85.12  ?  302 ALA B HA   1 
ATOM   9895  H HB1  . ALA B 1 293 ? 13.785  -13.306 71.407  1.00 70.21  ?  302 ALA B HB1  1 
ATOM   9896  H HB2  . ALA B 1 293 ? 12.515  -13.862 72.183  1.00 70.21  ?  302 ALA B HB2  1 
ATOM   9897  H HB3  . ALA B 1 293 ? 13.063  -12.404 72.497  1.00 70.21  ?  302 ALA B HB3  1 
ATOM   9898  N N    . HIS B 1 294 ? 15.382  -11.910 74.102  1.00 107.04 ?  303 HIS B N    1 
ATOM   9899  C CA   . HIS B 1 294 ? 16.498  -10.994 74.136  1.00 102.45 ?  303 HIS B CA   1 
ATOM   9900  C C    . HIS B 1 294 ? 17.528  -11.481 75.126  1.00 61.90  ?  303 HIS B C    1 
ATOM   9901  O O    . HIS B 1 294 ? 18.723  -11.310 74.908  1.00 48.97  ?  303 HIS B O    1 
ATOM   9902  C CB   . HIS B 1 294 ? 16.004  -9.602  74.520  1.00 68.88  ?  303 HIS B CB   1 
ATOM   9903  C CG   . HIS B 1 294 ? 15.058  -8.978  73.522  1.00 75.64  ?  303 HIS B CG   1 
ATOM   9904  N ND1  . HIS B 1 294 ? 14.279  -7.868  73.814  1.00 73.55  ?  303 HIS B ND1  1 
ATOM   9905  C CD2  . HIS B 1 294 ? 14.816  -9.267  72.219  1.00 70.70  ?  303 HIS B CD2  1 
ATOM   9906  C CE1  . HIS B 1 294 ? 13.570  -7.529  72.749  1.00 64.61  ?  303 HIS B CE1  1 
ATOM   9907  N NE2  . HIS B 1 294 ? 13.869  -8.363  71.765  1.00 59.60  ?  303 HIS B NE2  1 
ATOM   9908  H H    . HIS B 1 294 ? 14.697  -11.666 74.561  1.00 128.45 ?  303 HIS B H    1 
ATOM   9909  H HA   . HIS B 1 294 ? 16.909  -10.947 73.258  1.00 122.94 ?  303 HIS B HA   1 
ATOM   9910  H HB2  . HIS B 1 294 ? 15.539  -9.661  75.369  1.00 82.66  ?  303 HIS B HB2  1 
ATOM   9911  H HB3  . HIS B 1 294 ? 16.770  -9.013  74.607  1.00 82.66  ?  303 HIS B HB3  1 
ATOM   9912  H HD2  . HIS B 1 294 ? 15.192  -9.963  71.730  1.00 84.84  ?  303 HIS B HD2  1 
ATOM   9913  H HE1  . HIS B 1 294 ? 12.965  -6.825  72.701  1.00 77.53  ?  303 HIS B HE1  1 
ATOM   9914  H HE2  . HIS B 1 294 ? 13.540  -8.339  70.970  1.00 71.52  ?  303 HIS B HE2  1 
ATOM   9915  N N    . ARG B 1 295 ? 17.111  -12.187 76.165  1.00 62.94  ?  304 ARG B N    1 
ATOM   9916  C CA   . ARG B 1 295 ? 18.132  -12.771 77.026  1.00 62.54  ?  304 ARG B CA   1 
ATOM   9917  C C    . ARG B 1 295 ? 18.899  -13.820 76.246  1.00 66.64  ?  304 ARG B C    1 
ATOM   9918  O O    . ARG B 1 295 ? 20.100  -13.952 76.448  1.00 75.25  ?  304 ARG B O    1 
ATOM   9919  C CB   . ARG B 1 295 ? 17.506  -13.350 78.326  1.00 55.70  ?  304 ARG B CB   1 
ATOM   9920  C CG   . ARG B 1 295 ? 17.285  -14.931 78.385  1.00 70.73  ?  304 ARG B CG   1 
ATOM   9921  C CD   . ARG B 1 295 ? 16.565  -15.432 79.646  1.00 94.90  ?  304 ARG B CD   1 
ATOM   9922  N NE   . ARG B 1 295 ? 15.350  -14.642 79.887  1.00 144.38 ?  304 ARG B NE   1 
ATOM   9923  C CZ   . ARG B 1 295 ? 14.295  -15.052 80.576  1.00 121.97 ?  304 ARG B CZ   1 
ATOM   9924  N NH1  . ARG B 1 295 ? 14.266  -16.267 81.100  1.00 150.72 1  304 ARG B NH1  1 
ATOM   9925  N NH2  . ARG B 1 295 ? 13.266  -14.238 80.731  1.00 133.47 1  304 ARG B NH2  1 
ATOM   9926  H H    . ARG B 1 295 ? 16.294  -12.339 76.387  1.00 75.53  ?  304 ARG B H    1 
ATOM   9927  H HA   . ARG B 1 295 ? 18.758  -12.076 77.283  1.00 75.05  ?  304 ARG B HA   1 
ATOM   9928  H HB2  . ARG B 1 295 ? 18.083  -13.115 79.069  1.00 66.84  ?  304 ARG B HB2  1 
ATOM   9929  H HB3  . ARG B 1 295 ? 16.638  -12.936 78.452  1.00 66.84  ?  304 ARG B HB3  1 
ATOM   9930  H HG2  . ARG B 1 295 ? 16.754  -15.198 77.618  1.00 84.88  ?  304 ARG B HG2  1 
ATOM   9931  H HG3  . ARG B 1 295 ? 18.151  -15.366 78.349  1.00 84.88  ?  304 ARG B HG3  1 
ATOM   9932  H HD2  . ARG B 1 295 ? 16.310  -16.360 79.526  1.00 113.89 ?  304 ARG B HD2  1 
ATOM   9933  H HD3  . ARG B 1 295 ? 17.151  -15.337 80.413  1.00 113.89 ?  304 ARG B HD3  1 
ATOM   9934  H HE   . ARG B 1 295 ? 15.321  -13.849 79.555  1.00 173.26 ?  304 ARG B HE   1 
ATOM   9935  H HH11 . ARG B 1 295 ? 14.938  -16.794 81.001  1.00 180.86 ?  304 ARG B HH11 1 
ATOM   9936  H HH12 . ARG B 1 295 ? 13.577  -16.527 81.544  1.00 180.86 ?  304 ARG B HH12 1 
ATOM   9937  H HH21 . ARG B 1 295 ? 13.285  -13.450 80.386  1.00 160.16 ?  304 ARG B HH21 1 
ATOM   9938  H HH22 . ARG B 1 295 ? 12.574  -14.498 81.171  1.00 160.16 ?  304 ARG B HH22 1 
ATOM   9939  N N    . ASN B 1 296 ? 18.229  -14.496 75.294  1.00 89.50  ?  305 ASN B N    1 
ATOM   9940  C CA   . ASN B 1 296 ? 18.847  -15.508 74.439  1.00 80.93  ?  305 ASN B CA   1 
ATOM   9941  C C    . ASN B 1 296 ? 19.747  -14.893 73.396  1.00 67.69  ?  305 ASN B C    1 
ATOM   9942  O O    . ASN B 1 296 ? 20.739  -15.503 72.988  1.00 103.53 ?  305 ASN B O    1 
ATOM   9943  C CB   . ASN B 1 296 ? 17.784  -16.341 73.748  1.00 77.99  ?  305 ASN B CB   1 
ATOM   9944  C CG   . ASN B 1 296 ? 16.996  -17.209 74.725  1.00 96.79  ?  305 ASN B CG   1 
ATOM   9945  O OD1  . ASN B 1 296 ? 17.379  -17.386 75.882  1.00 150.90 ?  305 ASN B OD1  1 
ATOM   9946  N ND2  . ASN B 1 296 ? 15.900  -17.768 74.245  1.00 86.03  ?  305 ASN B ND2  1 
ATOM   9947  H H    . ASN B 1 296 ? 17.394  -14.377 75.128  1.00 107.40 ?  305 ASN B H    1 
ATOM   9948  H HA   . ASN B 1 296 ? 19.384  -16.100 74.987  1.00 97.11  ?  305 ASN B HA   1 
ATOM   9949  H HB2  . ASN B 1 296 ? 17.159  -15.750 73.300  1.00 93.59  ?  305 ASN B HB2  1 
ATOM   9950  H HB3  . ASN B 1 296 ? 18.210  -16.926 73.102  1.00 93.59  ?  305 ASN B HB3  1 
ATOM   9951  H HD21 . ASN B 1 296 ? 15.416  -18.268 74.751  1.00 103.24 ?  305 ASN B HD21 1 
ATOM   9952  H HD22 . ASN B 1 296 ? 15.671  -17.632 73.428  1.00 103.24 ?  305 ASN B HD22 1 
ATOM   9953  N N    . PHE B 1 297 ? 19.428  -13.691 72.952  1.00 72.33  ?  306 PHE B N    1 
ATOM   9954  C CA   . PHE B 1 297 ? 20.326  -13.051 72.020  1.00 56.61  ?  306 PHE B CA   1 
ATOM   9955  C C    . PHE B 1 297 ? 21.661  -12.775 72.664  1.00 61.89  ?  306 PHE B C    1 
ATOM   9956  O O    . PHE B 1 297 ? 22.708  -13.106 72.097  1.00 69.09  ?  306 PHE B O    1 
ATOM   9957  C CB   . PHE B 1 297 ? 19.747  -11.753 71.520  1.00 51.06  ?  306 PHE B CB   1 
ATOM   9958  C CG   . PHE B 1 297 ? 20.674  -11.038 70.575  1.00 60.86  ?  306 PHE B CG   1 
ATOM   9959  C CD1  . PHE B 1 297 ? 20.912  -11.548 69.296  1.00 75.44  ?  306 PHE B CD1  1 
ATOM   9960  C CD2  . PHE B 1 297 ? 21.306  -9.856  70.961  1.00 56.54  ?  306 PHE B CD2  1 
ATOM   9961  C CE1  . PHE B 1 297 ? 21.750  -10.894 68.393  1.00 64.99  ?  306 PHE B CE1  1 
ATOM   9962  C CE2  . PHE B 1 297 ? 22.136  -9.167  70.053  1.00 55.36  ?  306 PHE B CE2  1 
ATOM   9963  C CZ   . PHE B 1 297 ? 22.369  -9.699  68.755  1.00 50.53  ?  306 PHE B CZ   1 
ATOM   9964  H H    . PHE B 1 297 ? 18.726  -13.241 73.165  1.00 86.80  ?  306 PHE B H    1 
ATOM   9965  H HA   . PHE B 1 297 ? 20.468  -13.635 71.258  1.00 67.93  ?  306 PHE B HA   1 
ATOM   9966  H HB2  . PHE B 1 297 ? 18.919  -11.935 71.050  1.00 61.28  ?  306 PHE B HB2  1 
ATOM   9967  H HB3  . PHE B 1 297 ? 19.580  -11.169 72.276  1.00 61.28  ?  306 PHE B HB3  1 
ATOM   9968  H HD1  . PHE B 1 297 ? 20.494  -12.337 69.037  1.00 90.53  ?  306 PHE B HD1  1 
ATOM   9969  H HD2  . PHE B 1 297 ? 21.144  -9.497  71.803  1.00 67.85  ?  306 PHE B HD2  1 
ATOM   9970  H HE1  . PHE B 1 297 ? 21.889  -11.251 67.546  1.00 77.98  ?  306 PHE B HE1  1 
ATOM   9971  H HE2  . PHE B 1 297 ? 22.557  -8.380  70.314  1.00 66.43  ?  306 PHE B HE2  1 
ATOM   9972  H HZ   . PHE B 1 297 ? 22.936  -9.262  68.161  1.00 60.63  ?  306 PHE B HZ   1 
ATOM   9973  N N    . LEU B 1 298 ? 21.641  -12.193 73.869  1.00 47.44  ?  307 LEU B N    1 
ATOM   9974  C CA   . LEU B 1 298 ? 22.894  -11.901 74.544  1.00 45.55  ?  307 LEU B CA   1 
ATOM   9975  C C    . LEU B 1 298 ? 23.677  -13.180 74.686  1.00 87.68  ?  307 LEU B C    1 
ATOM   9976  O O    . LEU B 1 298 ? 24.908  -13.206 74.576  1.00 85.86  ?  307 LEU B O    1 
ATOM   9977  C CB   . LEU B 1 298 ? 22.635  -11.323 75.904  1.00 44.58  ?  307 LEU B CB   1 
ATOM   9978  C CG   . LEU B 1 298 ? 21.969  -9.973  75.875  1.00 60.71  ?  307 LEU B CG   1 
ATOM   9979  C CD1  . LEU B 1 298 ? 21.781  -9.569  77.341  1.00 43.92  ?  307 LEU B CD1  1 
ATOM   9980  C CD2  . LEU B 1 298 ? 22.731  -8.950  75.121  1.00 77.20  ?  307 LEU B CD2  1 
ATOM   9981  H H    . LEU B 1 298 ? 20.932  -11.965 74.300  1.00 56.93  ?  307 LEU B H    1 
ATOM   9982  H HA   . LEU B 1 298 ? 23.412  -11.268 74.024  1.00 54.66  ?  307 LEU B HA   1 
ATOM   9983  H HB2  . LEU B 1 298 ? 22.057  -11.927 76.396  1.00 53.49  ?  307 LEU B HB2  1 
ATOM   9984  H HB3  . LEU B 1 298 ? 23.480  -11.226 76.369  1.00 53.49  ?  307 LEU B HB3  1 
ATOM   9985  H HG   . LEU B 1 298 ? 21.092  -10.058 75.469  1.00 72.85  ?  307 LEU B HG   1 
ATOM   9986  H HD11 . LEU B 1 298 ? 21.352  -8.700  77.376  1.00 52.70  ?  307 LEU B HD11 1 
ATOM   9987  H HD12 . LEU B 1 298 ? 21.224  -10.231 77.781  1.00 52.70  ?  307 LEU B HD12 1 
ATOM   9988  H HD13 . LEU B 1 298 ? 22.649  -9.528  77.771  1.00 52.70  ?  307 LEU B HD13 1 
ATOM   9989  H HD21 . LEU B 1 298 ? 22.243  -8.112  75.145  1.00 92.64  ?  307 LEU B HD21 1 
ATOM   9990  H HD22 . LEU B 1 298 ? 23.602  -8.838  75.532  1.00 92.64  ?  307 LEU B HD22 1 
ATOM   9991  H HD23 . LEU B 1 298 ? 22.834  -9.246  74.203  1.00 92.64  ?  307 LEU B HD23 1 
ATOM   9992  N N    . CYS B 1 299 ? 22.965  -14.257 74.936  1.00 63.17  ?  308 CYS B N    1 
ATOM   9993  C CA   . CYS B 1 299 ? 23.626  -15.512 75.169  1.00 57.31  ?  308 CYS B CA   1 
ATOM   9994  C C    . CYS B 1 299 ? 24.402  -15.963 73.918  1.00 62.65  ?  308 CYS B C    1 
ATOM   9995  O O    . CYS B 1 299 ? 25.564  -16.395 74.001  1.00 48.78  ?  308 CYS B O    1 
ATOM   9996  C CB   . CYS B 1 299 ? 22.567  -16.519 75.540  1.00 75.45  ?  308 CYS B CB   1 
ATOM   9997  S SG   . CYS B 1 299 ? 23.192  -18.093 75.928  1.00 102.45 ?  308 CYS B SG   1 
ATOM   9998  H H    . CYS B 1 299 ? 22.106  -14.286 74.976  1.00 75.80  ?  308 CYS B H    1 
ATOM   9999  H HA   . CYS B 1 299 ? 24.248  -15.425 75.908  1.00 68.77  ?  308 CYS B HA   1 
ATOM   10000 H HB2  . CYS B 1 299 ? 22.085  -16.192 76.316  1.00 90.54  ?  308 CYS B HB2  1 
ATOM   10001 H HB3  . CYS B 1 299 ? 21.957  -16.619 74.793  1.00 90.54  ?  308 CYS B HB3  1 
ATOM   10002 N N    . SER B 1 300 ? 23.782  -15.820 72.741  1.00 55.06  ?  309 SER B N    1 
ATOM   10003 C CA   . SER B 1 300 ? 24.437  -16.204 71.507  1.00 61.38  ?  309 SER B CA   1 
ATOM   10004 C C    . SER B 1 300 ? 25.573  -15.263 71.178  1.00 68.57  ?  309 SER B C    1 
ATOM   10005 O O    . SER B 1 300 ? 26.491  -15.648 70.445  1.00 104.43 ?  309 SER B O    1 
ATOM   10006 C CB   . SER B 1 300 ? 23.417  -16.211 70.353  1.00 72.97  ?  309 SER B CB   1 
ATOM   10007 O OG   . SER B 1 300 ? 23.205  -14.901 69.847  1.00 84.94  ?  309 SER B OG   1 
ATOM   10008 H H    . SER B 1 300 ? 22.988  -15.504 72.640  1.00 66.08  ?  309 SER B H    1 
ATOM   10009 H HA   . SER B 1 300 ? 24.799  -17.100 71.600  1.00 73.66  ?  309 SER B HA   1 
ATOM   10010 H HB2  . SER B 1 300 ? 23.754  -16.773 69.638  1.00 87.56  ?  309 SER B HB2  1 
ATOM   10011 H HB3  . SER B 1 300 ? 22.574  -16.562 70.680  1.00 87.56  ?  309 SER B HB3  1 
ATOM   10012 H HG   . SER B 1 300 ? 22.911  -14.402 70.456  1.00 101.92 ?  309 SER B HG   1 
ATOM   10013 N N    . LEU B 1 301 ? 25.558  -14.056 71.721  1.00 81.36  ?  310 LEU B N    1 
ATOM   10014 C CA   . LEU B 1 301 ? 26.705  -13.192 71.526  1.00 79.55  ?  310 LEU B CA   1 
ATOM   10015 C C    . LEU B 1 301 ? 27.908  -13.661 72.313  1.00 54.16  ?  310 LEU B C    1 
ATOM   10016 O O    . LEU B 1 301 ? 28.987  -13.871 71.745  1.00 70.02  ?  310 LEU B O    1 
ATOM   10017 C CB   . LEU B 1 301 ? 26.393  -11.764 71.913  1.00 80.97  ?  310 LEU B CB   1 
ATOM   10018 C CG   . LEU B 1 301 ? 25.381  -11.042 71.067  1.00 50.23  ?  310 LEU B CG   1 
ATOM   10019 C CD1  . LEU B 1 301 ? 25.506  -9.609  71.555  1.00 56.98  ?  310 LEU B CD1  1 
ATOM   10020 C CD2  . LEU B 1 301 ? 25.637  -11.192 69.577  1.00 61.01  ?  310 LEU B CD2  1 
ATOM   10021 H H    . LEU B 1 301 ? 24.919  -13.723 72.191  1.00 97.63  ?  310 LEU B H    1 
ATOM   10022 H HA   . LEU B 1 301 ? 26.945  -13.200 70.586  1.00 95.46  ?  310 LEU B HA   1 
ATOM   10023 H HB2  . LEU B 1 301 ? 26.059  -11.763 72.824  1.00 97.16  ?  310 LEU B HB2  1 
ATOM   10024 H HB3  . LEU B 1 301 ? 27.217  -11.253 71.874  1.00 97.16  ?  310 LEU B HB3  1 
ATOM   10025 H HG   . LEU B 1 301 ? 24.490  -11.367 71.269  1.00 60.27  ?  310 LEU B HG   1 
ATOM   10026 H HD11 . LEU B 1 301 ? 24.883  -9.053  71.062  1.00 68.38  ?  310 LEU B HD11 1 
ATOM   10027 H HD12 . LEU B 1 301 ? 25.299  -9.579  72.502  1.00 68.38  ?  310 LEU B HD12 1 
ATOM   10028 H HD13 . LEU B 1 301 ? 26.414  -9.303  71.404  1.00 68.38  ?  310 LEU B HD13 1 
ATOM   10029 H HD21 . LEU B 1 301 ? 24.954  -10.706 69.090  1.00 73.22  ?  310 LEU B HD21 1 
ATOM   10030 H HD22 . LEU B 1 301 ? 26.513  -10.829 69.370  1.00 73.22  ?  310 LEU B HD22 1 
ATOM   10031 H HD23 . LEU B 1 301 ? 25.605  -12.133 69.345  1.00 73.22  ?  310 LEU B HD23 1 
ATOM   10032 N N    . GLU B 1 302 ? 27.749  -13.891 73.602  1.00 45.21  ?  311 GLU B N    1 
ATOM   10033 C CA   . GLU B 1 302 ? 28.919  -14.367 74.324  1.00 48.93  ?  311 GLU B CA   1 
ATOM   10034 C C    . GLU B 1 302 ? 29.434  -15.681 73.710  1.00 71.64  ?  311 GLU B C    1 
ATOM   10035 O O    . GLU B 1 302 ? 30.634  -15.961 73.756  1.00 130.17 ?  311 GLU B O    1 
ATOM   10036 C CB   . GLU B 1 302 ? 28.585  -14.542 75.810  1.00 59.56  ?  311 GLU B CB   1 
ATOM   10037 C CG   . GLU B 1 302 ? 28.403  -13.256 76.563  1.00 85.69  ?  311 GLU B CG   1 
ATOM   10038 C CD   . GLU B 1 302 ? 28.373  -13.409 78.089  1.00 89.49  ?  311 GLU B CD   1 
ATOM   10039 O OE1  . GLU B 1 302 ? 27.294  -13.253 78.685  1.00 69.27  ?  311 GLU B OE1  1 
ATOM   10040 O OE2  . GLU B 1 302 ? 29.437  -13.643 78.699  1.00 132.64 -1 311 GLU B OE2  1 
ATOM   10041 H H    . GLU B 1 302 ? 27.028  -13.791 74.060  1.00 54.26  ?  311 GLU B H    1 
ATOM   10042 H HA   . GLU B 1 302 ? 29.625  -13.706 74.251  1.00 58.71  ?  311 GLU B HA   1 
ATOM   10043 H HB2  . GLU B 1 302 ? 27.760  -15.046 75.886  1.00 71.47  ?  311 GLU B HB2  1 
ATOM   10044 H HB3  . GLU B 1 302 ? 29.307  -15.031 76.235  1.00 71.47  ?  311 GLU B HB3  1 
ATOM   10045 H HG2  . GLU B 1 302 ? 29.135  -12.661 76.341  1.00 102.83 ?  311 GLU B HG2  1 
ATOM   10046 H HG3  . GLU B 1 302 ? 27.562  -12.855 76.292  1.00 102.83 ?  311 GLU B HG3  1 
ATOM   10047 N N    . SER B 1 303 ? 28.560  -16.441 73.051  1.00 71.65  ?  312 SER B N    1 
ATOM   10048 C CA   . SER B 1 303 ? 28.952  -17.721 72.530  1.00 79.20  ?  312 SER B CA   1 
ATOM   10049 C C    . SER B 1 303 ? 29.815  -17.531 71.313  1.00 82.92  ?  312 SER B C    1 
ATOM   10050 O O    . SER B 1 303 ? 30.716  -18.334 71.050  1.00 88.25  ?  312 SER B O    1 
ATOM   10051 C CB   . SER B 1 303 ? 27.725  -18.606 72.207  1.00 85.37  ?  312 SER B CB   1 
ATOM   10052 O OG   . SER B 1 303 ? 27.109  -19.146 73.390  1.00 59.07  ?  312 SER B OG   1 
ATOM   10053 H H    . SER B 1 303 ? 27.740  -16.229 72.898  1.00 85.98  ?  312 SER B H    1 
ATOM   10054 H HA   . SER B 1 303 ? 29.481  -18.182 73.199  1.00 95.04  ?  312 SER B HA   1 
ATOM   10055 H HB2  . SER B 1 303 ? 27.071  -18.069 71.734  1.00 102.44 ?  312 SER B HB2  1 
ATOM   10056 H HB3  . SER B 1 303 ? 28.013  -19.341 71.643  1.00 102.44 ?  312 SER B HB3  1 
ATOM   10057 H HG   . SER B 1 303 ? 26.849  -18.523 73.889  1.00 70.89  ?  312 SER B HG   1 
ATOM   10058 N N    . ASN B 1 304 ? 29.607  -16.473 70.582  1.00 137.44 ?  313 ASN B N    1 
ATOM   10059 C CA   . ASN B 1 304 ? 30.490  -16.290 69.462  1.00 86.52  ?  313 ASN B CA   1 
ATOM   10060 C C    . ASN B 1 304 ? 31.891  -15.940 69.957  1.00 80.17  ?  313 ASN B C    1 
ATOM   10061 O O    . ASN B 1 304 ? 32.068  -15.462 71.078  1.00 91.39  ?  313 ASN B O    1 
ATOM   10062 C CB   . ASN B 1 304 ? 29.974  -15.207 68.546  1.00 100.53 ?  313 ASN B CB   1 
ATOM   10063 C CG   . ASN B 1 304 ? 28.820  -15.677 67.699  1.00 118.04 ?  313 ASN B CG   1 
ATOM   10064 O OD1  . ASN B 1 304 ? 27.882  -16.298 68.204  1.00 127.72 ?  313 ASN B OD1  1 
ATOM   10065 N ND2  . ASN B 1 304 ? 28.876  -15.376 66.405  1.00 136.69 ?  313 ASN B ND2  1 
ATOM   10066 H H    . ASN B 1 304 ? 29.001  -15.874 70.698  1.00 164.93 ?  313 ASN B H    1 
ATOM   10067 H HA   . ASN B 1 304 ? 30.543  -17.116 68.957  1.00 103.83 ?  313 ASN B HA   1 
ATOM   10068 H HB2  . ASN B 1 304 ? 29.670  -14.457 69.081  1.00 120.64 ?  313 ASN B HB2  1 
ATOM   10069 H HB3  . ASN B 1 304 ? 30.688  -14.925 67.953  1.00 120.64 ?  313 ASN B HB3  1 
ATOM   10070 H HD21 . ASN B 1 304 ? 28.242  -15.622 65.878  1.00 164.03 ?  313 ASN B HD21 1 
ATOM   10071 H HD22 . ASN B 1 304 ? 29.547  -14.937 66.094  1.00 164.03 ?  313 ASN B HD22 1 
ATOM   10072 N N    . PRO B 1 305 ? 32.906  -16.235 69.171  1.00 91.50  ?  314 PRO B N    1 
ATOM   10073 C CA   . PRO B 1 305 ? 34.282  -15.970 69.607  1.00 93.13  ?  314 PRO B CA   1 
ATOM   10074 C C    . PRO B 1 305 ? 34.615  -14.487 69.678  1.00 101.39 ?  314 PRO B C    1 
ATOM   10075 O O    . PRO B 1 305 ? 34.112  -13.670 68.894  1.00 85.91  ?  314 PRO B O    1 
ATOM   10076 C CB   . PRO B 1 305 ? 35.129  -16.657 68.542  1.00 84.06  ?  314 PRO B CB   1 
ATOM   10077 C CG   . PRO B 1 305 ? 34.203  -16.773 67.341  1.00 77.22  ?  314 PRO B CG   1 
ATOM   10078 C CD   . PRO B 1 305 ? 32.828  -16.838 67.835  1.00 78.60  ?  314 PRO B CD   1 
ATOM   10079 H HA   . PRO B 1 305 ? 34.451  -16.382 70.469  1.00 111.76 ?  314 PRO B HA   1 
ATOM   10080 H HB2  . PRO B 1 305 ? 35.901  -16.109 68.331  1.00 100.87 ?  314 PRO B HB2  1 
ATOM   10081 H HB3  . PRO B 1 305 ? 35.402  -17.534 68.853  1.00 100.87 ?  314 PRO B HB3  1 
ATOM   10082 H HG2  . PRO B 1 305 ? 34.318  -15.995 66.774  1.00 92.66  ?  314 PRO B HG2  1 
ATOM   10083 H HG3  . PRO B 1 305 ? 34.420  -17.580 66.849  1.00 92.66  ?  314 PRO B HG3  1 
ATOM   10084 H HD2  . PRO B 1 305 ? 32.241  -16.318 67.264  1.00 94.32  ?  314 PRO B HD2  1 
ATOM   10085 H HD3  . PRO B 1 305 ? 32.536  -17.760 67.897  1.00 94.32  ?  314 PRO B HD3  1 
ATOM   10086 N N    . SER B 1 306 ? 35.566  -14.179 70.569  1.00 85.57  ?  315 SER B N    1 
ATOM   10087 C CA   . SER B 1 306 ? 35.832  -12.809 70.998  1.00 72.49  ?  315 SER B CA   1 
ATOM   10088 C C    . SER B 1 306 ? 36.367  -11.951 69.874  1.00 70.29  ?  315 SER B C    1 
ATOM   10089 O O    . SER B 1 306 ? 37.285  -12.338 69.148  1.00 80.20  ?  315 SER B O    1 
ATOM   10090 C CB   . SER B 1 306 ? 36.815  -12.809 72.153  1.00 62.65  ?  315 SER B CB   1 
ATOM   10091 O OG   . SER B 1 306 ? 37.150  -11.514 72.576  1.00 118.42 ?  315 SER B OG   1 
ATOM   10092 H H    . SER B 1 306 ? 36.077  -14.760 70.944  1.00 102.69 ?  315 SER B H    1 
ATOM   10093 H HA   . SER B 1 306 ? 35.005  -12.411 71.310  1.00 86.99  ?  315 SER B HA   1 
ATOM   10094 H HB2  . SER B 1 306 ? 36.418  -13.286 72.898  1.00 75.18  ?  315 SER B HB2  1 
ATOM   10095 H HB3  . SER B 1 306 ? 37.625  -13.261 71.870  1.00 75.18  ?  315 SER B HB3  1 
ATOM   10096 H HG   . SER B 1 306 ? 37.694  -11.553 73.215  1.00 142.10 ?  315 SER B HG   1 
ATOM   10097 N N    . VAL B 1 307 ? 35.756  -10.778 69.726  1.00 68.07  ?  316 VAL B N    1 
ATOM   10098 C CA   . VAL B 1 307 ? 36.280  -9.763  68.825  1.00 69.51  ?  316 VAL B CA   1 
ATOM   10099 C C    . VAL B 1 307 ? 37.558  -9.154  69.420  1.00 84.46  ?  316 VAL B C    1 
ATOM   10100 O O    . VAL B 1 307 ? 38.544  -8.929  68.715  1.00 99.44  ?  316 VAL B O    1 
ATOM   10101 C CB   . VAL B 1 307 ? 35.159  -8.734  68.567  1.00 79.18  ?  316 VAL B CB   1 
ATOM   10102 C CG1  . VAL B 1 307 ? 35.562  -7.595  67.612  1.00 66.27  ?  316 VAL B CG1  1 
ATOM   10103 C CG2  . VAL B 1 307 ? 33.933  -9.428  68.080  1.00 121.70 ?  316 VAL B CG2  1 
ATOM   10104 H H    . VAL B 1 307 ? 35.036  -10.548 70.137  1.00 81.68  ?  316 VAL B H    1 
ATOM   10105 H HA   . VAL B 1 307 ? 36.510  -10.177 67.979  1.00 83.41  ?  316 VAL B HA   1 
ATOM   10106 H HB   . VAL B 1 307 ? 34.932  -8.322  69.415  1.00 95.01  ?  316 VAL B HB   1 
ATOM   10107 H HG11 . VAL B 1 307 ? 34.809  -6.995  67.502  1.00 79.52  ?  316 VAL B HG11 1 
ATOM   10108 H HG12 . VAL B 1 307 ? 36.315  -7.116  67.993  1.00 79.52  ?  316 VAL B HG12 1 
ATOM   10109 H HG13 . VAL B 1 307 ? 35.811  -7.976  66.755  1.00 79.52  ?  316 VAL B HG13 1 
ATOM   10110 H HG21 . VAL B 1 307 ? 33.239  -8.769  67.923  1.00 146.05 ?  316 VAL B HG21 1 
ATOM   10111 H HG22 . VAL B 1 307 ? 34.141  -9.894  67.255  1.00 146.05 ?  316 VAL B HG22 1 
ATOM   10112 H HG23 . VAL B 1 307 ? 33.641  -10.062 68.754  1.00 146.05 ?  316 VAL B HG23 1 
ATOM   10113 N N    . ARG B 1 308 ? 37.583  -8.941  70.741  1.00 93.24  ?  317 ARG B N    1 
ATOM   10114 C CA   . ARG B 1 308 ? 38.775  -8.411  71.412  1.00 78.83  ?  317 ARG B CA   1 
ATOM   10115 C C    . ARG B 1 308 ? 39.960  -9.355  71.186  1.00 81.60  ?  317 ARG B C    1 
ATOM   10116 O O    . ARG B 1 308 ? 41.032  -8.939  70.721  1.00 98.52  ?  317 ARG B O    1 
ATOM   10117 C CB   . ARG B 1 308 ? 38.439  -8.190  72.915  1.00 63.83  ?  317 ARG B CB   1 
ATOM   10118 C CG   . ARG B 1 308 ? 39.458  -7.677  74.041  1.00 63.38  ?  317 ARG B CG   1 
ATOM   10119 C CD   . ARG B 1 308 ? 39.932  -6.194  74.060  1.00 78.73  ?  317 ARG B CD   1 
ATOM   10120 N NE   . ARG B 1 308 ? 40.208  -5.606  75.404  1.00 67.99  ?  317 ARG B NE   1 
ATOM   10121 C CZ   . ARG B 1 308 ? 41.417  -5.533  76.001  1.00 78.30  ?  317 ARG B CZ   1 
ATOM   10122 N NH1  . ARG B 1 308 ? 42.499  -6.019  75.437  1.00 100.47 1  317 ARG B NH1  1 
ATOM   10123 N NH2  . ARG B 1 308 ? 41.576  -4.972  77.191  1.00 76.27  1  317 ARG B NH2  1 
ATOM   10124 H H    . ARG B 1 308 ? 36.923  -9.095  71.270  1.00 111.89 ?  317 ARG B H    1 
ATOM   10125 H HA   . ARG B 1 308 ? 39.000  -7.550  71.025  1.00 94.60  ?  317 ARG B HA   1 
ATOM   10126 H HB2  . ARG B 1 308 ? 37.702  -7.560  72.935  1.00 76.59  ?  317 ARG B HB2  1 
ATOM   10127 H HB3  . ARG B 1 308 ? 38.108  -9.041  73.243  1.00 76.59  ?  317 ARG B HB3  1 
ATOM   10128 H HG2  . ARG B 1 308 ? 39.044  -7.843  74.902  1.00 76.06  ?  317 ARG B HG2  1 
ATOM   10129 H HG3  . ARG B 1 308 ? 40.259  -8.219  73.973  1.00 76.06  ?  317 ARG B HG3  1 
ATOM   10130 H HD2  . ARG B 1 308 ? 40.751  -6.130  73.544  1.00 94.47  ?  317 ARG B HD2  1 
ATOM   10131 H HD3  . ARG B 1 308 ? 39.246  -5.650  73.643  1.00 94.47  ?  317 ARG B HD3  1 
ATOM   10132 H HE   . ARG B 1 308 ? 39.538  -5.284  75.836  1.00 81.59  ?  317 ARG B HE   1 
ATOM   10133 H HH11 . ARG B 1 308 ? 42.452  -6.388  74.662  1.00 120.57 ?  317 ARG B HH11 1 
ATOM   10134 H HH12 . ARG B 1 308 ? 43.257  -5.963  75.841  1.00 120.57 ?  317 ARG B HH12 1 
ATOM   10135 H HH21 . ARG B 1 308 ? 40.898  -4.644  77.606  1.00 91.52  ?  317 ARG B HH21 1 
ATOM   10136 H HH22 . ARG B 1 308 ? 42.355  -4.948  77.554  1.00 91.52  ?  317 ARG B HH22 1 
ATOM   10137 N N    . GLU B 1 309 ? 39.758  -10.651 71.419  1.00 76.75  ?  318 GLU B N    1 
ATOM   10138 C CA   . GLU B 1 309 ? 40.862  -11.591 71.289  1.00 92.32  ?  318 GLU B CA   1 
ATOM   10139 C C    . GLU B 1 309 ? 41.383  -11.656 69.850  1.00 73.78  ?  318 GLU B C    1 
ATOM   10140 O O    . GLU B 1 309 ? 42.596  -11.734 69.619  1.00 111.16 ?  318 GLU B O    1 
ATOM   10141 C CB   . GLU B 1 309 ? 40.403  -12.952 71.788  1.00 48.80  ?  318 GLU B CB   1 
ATOM   10142 H H    . GLU B 1 309 ? 39.008  -11.003 71.650  1.00 92.11  ?  318 GLU B H    1 
ATOM   10143 H HA   . GLU B 1 309 ? 41.593  -11.297 71.855  1.00 110.78 ?  318 GLU B HA   1 
ATOM   10144 N N    . PHE B 1 310 ? 40.492  -11.587 68.876  1.00 62.64  ?  319 PHE B N    1 
ATOM   10145 C CA   . PHE B 1 310 ? 40.899  -11.605 67.484  1.00 123.71 ?  319 PHE B CA   1 
ATOM   10146 C C    . PHE B 1 310 ? 41.653  -10.336 67.116  1.00 99.76  ?  319 PHE B C    1 
ATOM   10147 O O    . PHE B 1 310 ? 42.696  -10.393 66.448  1.00 116.22 ?  319 PHE B O    1 
ATOM   10148 C CB   . PHE B 1 310 ? 39.655  -11.813 66.651  1.00 48.63  ?  319 PHE B CB   1 
ATOM   10149 C CG   . PHE B 1 310 ? 39.862  -11.847 65.183  1.00 56.48  ?  319 PHE B CG   1 
ATOM   10150 C CD1  . PHE B 1 310 ? 39.802  -10.687 64.434  1.00 52.83  ?  319 PHE B CD1  1 
ATOM   10151 C CD2  . PHE B 1 310 ? 40.011  -13.046 64.514  1.00 78.31  ?  319 PHE B CD2  1 
ATOM   10152 C CE1  . PHE B 1 310 ? 39.954  -10.739 63.021  1.00 52.93  ?  319 PHE B CE1  1 
ATOM   10153 C CE2  . PHE B 1 310 ? 40.172  -13.111 63.118  1.00 114.57 ?  319 PHE B CE2  1 
ATOM   10154 C CZ   . PHE B 1 310 ? 40.150  -11.960 62.380  1.00 51.45  ?  319 PHE B CZ   1 
ATOM   10155 H H    . PHE B 1 310 ? 39.642  -11.528 68.995  1.00 75.17  ?  319 PHE B H    1 
ATOM   10156 H HA   . PHE B 1 310 ? 41.490  -12.360 67.336  1.00 148.46 ?  319 PHE B HA   1 
ATOM   10157 H HB2  . PHE B 1 310 ? 39.253  -12.659 66.907  1.00 58.36  ?  319 PHE B HB2  1 
ATOM   10158 H HB3  . PHE B 1 310 ? 39.036  -11.091 66.841  1.00 58.36  ?  319 PHE B HB3  1 
ATOM   10159 H HD1  . PHE B 1 310 ? 39.682  -9.868  64.857  1.00 63.39  ?  319 PHE B HD1  1 
ATOM   10160 H HD2  . PHE B 1 310 ? 40.040  -13.835 65.007  1.00 93.97  ?  319 PHE B HD2  1 
ATOM   10161 H HE1  . PHE B 1 310 ? 39.938  -9.953  62.524  1.00 63.51  ?  319 PHE B HE1  1 
ATOM   10162 H HE2  . PHE B 1 310 ? 40.295  -13.933 62.700  1.00 137.49 ?  319 PHE B HE2  1 
ATOM   10163 H HZ   . PHE B 1 310 ? 40.248  -11.994 61.456  1.00 61.74  ?  319 PHE B HZ   1 
ATOM   10164 N N    . VAL B 1 311 ? 41.159  -9.174  67.553  1.00 68.78  ?  320 VAL B N    1 
ATOM   10165 C CA   . VAL B 1 311 ? 41.771  -7.929  67.090  1.00 77.08  ?  320 VAL B CA   1 
ATOM   10166 C C    . VAL B 1 311 ? 43.165  -7.809  67.651  1.00 79.56  ?  320 VAL B C    1 
ATOM   10167 O O    . VAL B 1 311 ? 44.121  -7.497  66.927  1.00 76.72  ?  320 VAL B O    1 
ATOM   10168 C CB   . VAL B 1 311 ? 40.923  -6.696  67.453  1.00 61.23  ?  320 VAL B CB   1 
ATOM   10169 C CG1  . VAL B 1 311 ? 41.678  -5.449  67.225  1.00 87.65  ?  320 VAL B CG1  1 
ATOM   10170 C CG2  . VAL B 1 311 ? 39.707  -6.666  66.604  1.00 86.41  ?  320 VAL B CG2  1 
ATOM   10171 H H    . VAL B 1 311 ? 40.497  -9.082  68.095  1.00 82.54  ?  320 VAL B H    1 
ATOM   10172 H HA   . VAL B 1 311 ? 41.845  -7.960  66.123  1.00 92.50  ?  320 VAL B HA   1 
ATOM   10173 H HB   . VAL B 1 311 ? 40.656  -6.739  68.385  1.00 73.48  ?  320 VAL B HB   1 
ATOM   10174 H HG11 . VAL B 1 311 ? 41.118  -4.693  67.463  1.00 105.18 ?  320 VAL B HG11 1 
ATOM   10175 H HG12 . VAL B 1 311 ? 42.475  -5.457  67.779  1.00 105.18 ?  320 VAL B HG12 1 
ATOM   10176 H HG13 . VAL B 1 311 ? 41.925  -5.397  66.289  1.00 105.18 ?  320 VAL B HG13 1 
ATOM   10177 H HG21 . VAL B 1 311 ? 39.178  -5.888  66.838  1.00 103.69 ?  320 VAL B HG21 1 
ATOM   10178 H HG22 . VAL B 1 311 ? 39.975  -6.617  65.672  1.00 103.69 ?  320 VAL B HG22 1 
ATOM   10179 H HG23 . VAL B 1 311 ? 39.194  -7.474  66.759  1.00 103.69 ?  320 VAL B HG23 1 
ATOM   10180 N N    . LEU B 1 312 ? 43.326  -8.180  68.904  1.00 82.17  ?  321 LEU B N    1 
ATOM   10181 C CA   . LEU B 1 312 ? 44.647  -8.120  69.471  1.00 94.27  ?  321 LEU B CA   1 
ATOM   10182 C C    . LEU B 1 312 ? 45.598  -9.064  68.749  1.00 120.02 ?  321 LEU B C    1 
ATOM   10183 O O    . LEU B 1 312 ? 46.778  -8.739  68.544  1.00 141.37 ?  321 LEU B O    1 
ATOM   10184 C CB   . LEU B 1 312 ? 44.576  -8.502  70.930  1.00 86.45  ?  321 LEU B CB   1 
ATOM   10185 C CG   . LEU B 1 312 ? 44.119  -7.505  71.960  1.00 112.97 ?  321 LEU B CG   1 
ATOM   10186 C CD1  . LEU B 1 312 ? 43.976  -8.267  73.250  1.00 116.24 ?  321 LEU B CD1  1 
ATOM   10187 C CD2  . LEU B 1 312 ? 45.134  -6.395  72.104  1.00 151.14 ?  321 LEU B CD2  1 
ATOM   10188 H H    . LEU B 1 312 ? 42.708  -8.462  69.431  1.00 98.60  ?  321 LEU B H    1 
ATOM   10189 H HA   . LEU B 1 312 ? 44.993  -7.216  69.401  1.00 113.13 ?  321 LEU B HA   1 
ATOM   10190 H HB2  . LEU B 1 312 ? 43.976  -9.261  71.000  1.00 103.73 ?  321 LEU B HB2  1 
ATOM   10191 H HB3  . LEU B 1 312 ? 45.464  -8.784  71.198  1.00 103.73 ?  321 LEU B HB3  1 
ATOM   10192 H HG   . LEU B 1 312 ? 43.261  -7.129  71.711  1.00 135.56 ?  321 LEU B HG   1 
ATOM   10193 H HD11 . LEU B 1 312 ? 43.682  -7.657  73.945  1.00 139.48 ?  321 LEU B HD11 1 
ATOM   10194 H HD12 . LEU B 1 312 ? 43.321  -8.972  73.128  1.00 139.48 ?  321 LEU B HD12 1 
ATOM   10195 H HD13 . LEU B 1 312 ? 44.835  -8.650  73.487  1.00 139.48 ?  321 LEU B HD13 1 
ATOM   10196 H HD21 . LEU B 1 312 ? 44.820  -5.765  72.772  1.00 181.37 ?  321 LEU B HD21 1 
ATOM   10197 H HD22 . LEU B 1 312 ? 45.981  -6.776  72.381  1.00 181.37 ?  321 LEU B HD22 1 
ATOM   10198 H HD23 . LEU B 1 312 ? 45.235  -5.948  71.249  1.00 181.37 ?  321 LEU B HD23 1 
ATOM   10199 N N    . SER B 1 313 ? 45.076  -10.184 68.262  1.00 86.80  ?  322 SER B N    1 
ATOM   10200 C CA   . SER B 1 313 ? 45.937  -11.215 67.738  1.00 76.28  ?  322 SER B CA   1 
ATOM   10201 C C    . SER B 1 313 ? 46.509  -10.861 66.381  1.00 72.02  ?  322 SER B C    1 
ATOM   10202 O O    . SER B 1 313 ? 47.482  -11.487 65.964  1.00 75.72  ?  322 SER B O    1 
ATOM   10203 C CB   . SER B 1 313 ? 45.174  -12.526 67.650  1.00 77.91  ?  322 SER B CB   1 
ATOM   10204 O OG   . SER B 1 313 ? 44.321  -12.560 66.536  1.00 78.34  ?  322 SER B OG   1 
ATOM   10205 H H    . SER B 1 313 ? 44.236  -10.364 68.227  1.00 104.16 ?  322 SER B H    1 
ATOM   10206 H HA   . SER B 1 313 ? 46.680  -11.343 68.349  1.00 91.54  ?  322 SER B HA   1 
ATOM   10207 H HB2  . SER B 1 313 ? 45.810  -13.254 67.579  1.00 93.50  ?  322 SER B HB2  1 
ATOM   10208 H HB3  . SER B 1 313 ? 44.641  -12.632 68.454  1.00 93.50  ?  322 SER B HB3  1 
ATOM   10209 H HG   . SER B 1 313 ? 43.760  -11.936 66.584  1.00 94.01  ?  322 SER B HG   1 
ATOM   10210 N N    . LYS B 1 314 ? 45.914  -9.915  65.670  1.00 90.52  ?  323 LYS B N    1 
ATOM   10211 C CA   . LYS B 1 314 ? 46.281  -9.654  64.289  1.00 73.44  ?  323 LYS B CA   1 
ATOM   10212 C C    . LYS B 1 314 ? 47.458  -8.682  64.170  1.00 90.73  ?  323 LYS B C    1 
ATOM   10213 O O    . LYS B 1 314 ? 48.010  -8.539  63.071  1.00 104.34 ?  323 LYS B O    1 
ATOM   10214 C CB   . LYS B 1 314 ? 45.051  -9.113  63.528  1.00 56.03  ?  323 LYS B CB   1 
ATOM   10215 C CG   . LYS B 1 314 ? 43.998  -10.137 63.169  1.00 72.28  ?  323 LYS B CG   1 
ATOM   10216 C CD   . LYS B 1 314 ? 44.261  -10.780 61.835  1.00 103.99 ?  323 LYS B CD   1 
ATOM   10217 H H    . LYS B 1 314 ? 45.289  -9.405  65.968  1.00 108.63 ?  323 LYS B H    1 
ATOM   10218 H HA   . LYS B 1 314 ? 46.544  -10.490 63.873  1.00 88.13  ?  323 LYS B HA   1 
ATOM   10219 H HB2  . LYS B 1 314 ? 44.623  -8.439  64.079  1.00 67.24  ?  323 LYS B HB2  1 
ATOM   10220 H HB3  . LYS B 1 314 ? 45.356  -8.709  62.701  1.00 67.24  ?  323 LYS B HB3  1 
ATOM   10221 H HG2  . LYS B 1 314 ? 43.990  -10.835 63.844  1.00 86.74  ?  323 LYS B HG2  1 
ATOM   10222 H HG3  . LYS B 1 314 ? 43.132  -9.702  63.129  1.00 86.74  ?  323 LYS B HG3  1 
ATOM   10223 H HD2  . LYS B 1 314 ? 43.546  -11.406 61.640  1.00 124.79 ?  323 LYS B HD2  1 
ATOM   10224 H HD3  . LYS B 1 314 ? 44.293  -10.090 61.154  1.00 124.79 ?  323 LYS B HD3  1 
ATOM   10225 N N    . GLY B 1 315 ? 47.828  -7.999  65.262  1.00 113.36 ?  324 GLY B N    1 
ATOM   10226 C CA   . GLY B 1 315 ? 48.934  -7.052  65.237  1.00 99.96  ?  324 GLY B CA   1 
ATOM   10227 C C    . GLY B 1 315 ? 48.680  -5.874  64.328  1.00 97.42  ?  324 GLY B C    1 
ATOM   10228 O O    . GLY B 1 315 ? 49.608  -5.424  63.652  1.00 125.85 ?  324 GLY B O    1 
ATOM   10229 H H    . GLY B 1 315 ? 47.448  -8.072  66.030  1.00 136.04 ?  324 GLY B H    1 
ATOM   10230 H HA2  . GLY B 1 315 ? 49.091  -6.717  66.133  1.00 119.95 ?  324 GLY B HA2  1 
ATOM   10231 H HA3  . GLY B 1 315 ? 49.737  -7.504  64.934  1.00 119.95 ?  324 GLY B HA3  1 
ATOM   10232 N N    . ASP B 1 316 ? 47.416  -5.413  64.235  1.00 93.33  ?  325 ASP B N    1 
ATOM   10233 C CA   . ASP B 1 316 ? 46.956  -4.442  63.239  1.00 79.09  ?  325 ASP B CA   1 
ATOM   10234 C C    . ASP B 1 316 ? 46.540  -3.148  63.957  1.00 78.55  ?  325 ASP B C    1 
ATOM   10235 O O    . ASP B 1 316 ? 45.539  -3.129  64.669  1.00 100.74 ?  325 ASP B O    1 
ATOM   10236 C CB   . ASP B 1 316 ? 45.798  -5.034  62.424  1.00 79.41  ?  325 ASP B CB   1 
ATOM   10237 C CG   . ASP B 1 316 ? 45.354  -4.137  61.275  1.00 82.25  ?  325 ASP B CG   1 
ATOM   10238 O OD1  . ASP B 1 316 ? 45.403  -2.914  61.452  1.00 80.94  ?  325 ASP B OD1  1 
ATOM   10239 O OD2  . ASP B 1 316 ? 44.933  -4.659  60.214  1.00 74.17  -1 325 ASP B OD2  1 
ATOM   10240 H H    . ASP B 1 316 ? 46.787  -5.665  64.765  1.00 112.00 ?  325 ASP B H    1 
ATOM   10241 H HA   . ASP B 1 316 ? 47.684  -4.235  62.631  1.00 94.90  ?  325 ASP B HA   1 
ATOM   10242 H HB2  . ASP B 1 316 ? 46.079  -5.883  62.048  1.00 95.30  ?  325 ASP B HB2  1 
ATOM   10243 H HB3  . ASP B 1 316 ? 45.037  -5.168  63.010  1.00 95.30  ?  325 ASP B HB3  1 
ATOM   10244 N N    . ALA B 1 317 ? 47.330  -2.085  63.825  1.00 82.55  ?  326 ALA B N    1 
ATOM   10245 C CA   . ALA B 1 317 ? 46.987  -0.842  64.487  1.00 100.08 ?  326 ALA B CA   1 
ATOM   10246 C C    . ALA B 1 317 ? 45.694  -0.280  63.954  1.00 93.76  ?  326 ALA B C    1 
ATOM   10247 O O    . ALA B 1 317 ? 44.961  0.395   64.681  1.00 49.51  ?  326 ALA B O    1 
ATOM   10248 C CB   . ALA B 1 317 ? 48.082  0.176   64.284  1.00 53.92  ?  326 ALA B CB   1 
ATOM   10249 H H    . ALA B 1 317 ? 48.057  -2.062  63.365  1.00 99.06  ?  326 ALA B H    1 
ATOM   10250 H HA   . ALA B 1 317 ? 46.886  -0.999  65.439  1.00 120.10 ?  326 ALA B HA   1 
ATOM   10251 H HB1  . ALA B 1 317 ? 47.834  0.999   64.734  1.00 64.70  ?  326 ALA B HB1  1 
ATOM   10252 H HB2  . ALA B 1 317 ? 48.907  -0.170  64.658  1.00 64.70  ?  326 ALA B HB2  1 
ATOM   10253 H HB3  . ALA B 1 317 ? 48.190  0.337   63.334  1.00 64.70  ?  326 ALA B HB3  1 
ATOM   10254 N N    . GLY B 1 318 ? 45.396  -0.532  62.686  1.00 71.69  ?  327 GLY B N    1 
ATOM   10255 C CA   . GLY B 1 318 ? 44.121  -0.086  62.148  1.00 58.92  ?  327 GLY B CA   1 
ATOM   10256 C C    . GLY B 1 318 ? 42.954  -0.811  62.789  1.00 85.15  ?  327 GLY B C    1 
ATOM   10257 O O    . GLY B 1 318 ? 41.997  -0.177  63.242  1.00 59.09  ?  327 GLY B O    1 
ATOM   10258 H H    . GLY B 1 318 ? 45.901  -0.948  62.128  1.00 86.03  ?  327 GLY B H    1 
ATOM   10259 H HA2  . GLY B 1 318 ? 44.017  0.866   62.304  1.00 70.71  ?  327 GLY B HA2  1 
ATOM   10260 H HA3  . GLY B 1 318 ? 44.097  -0.247  61.192  1.00 70.71  ?  327 GLY B HA3  1 
ATOM   10261 N N    . LEU B 1 319 ? 43.036  -2.143  62.901  1.00 88.86  ?  328 LEU B N    1 
ATOM   10262 C CA   . LEU B 1 319 ? 41.964  -2.835  63.597  1.00 70.85  ?  328 LEU B CA   1 
ATOM   10263 C C    . LEU B 1 319 ? 41.905  -2.388  65.035  1.00 65.54  ?  328 LEU B C    1 
ATOM   10264 O O    . LEU B 1 319 ? 40.824  -2.200  65.588  1.00 72.31  ?  328 LEU B O    1 
ATOM   10265 C CB   . LEU B 1 319 ? 42.125  -4.342  63.554  1.00 89.88  ?  328 LEU B CB   1 
ATOM   10266 C CG   . LEU B 1 319 ? 41.587  -5.055  62.330  1.00 94.24  ?  328 LEU B CG   1 
ATOM   10267 C CD1  . LEU B 1 319 ? 41.969  -6.554  62.418  1.00 91.71  ?  328 LEU B CD1  1 
ATOM   10268 C CD2  . LEU B 1 319 ? 40.097  -4.828  62.195  1.00 66.22  ?  328 LEU B CD2  1 
ATOM   10269 H H    . LEU B 1 319 ? 43.669  -2.640  62.598  1.00 106.63 ?  328 LEU B H    1 
ATOM   10270 H HA   . LEU B 1 319 ? 41.119  -2.611  63.177  1.00 85.02  ?  328 LEU B HA   1 
ATOM   10271 H HB2  . LEU B 1 319 ? 43.072  -4.546  63.610  1.00 107.86 ?  328 LEU B HB2  1 
ATOM   10272 H HB3  . LEU B 1 319 ? 41.672  -4.716  64.325  1.00 107.86 ?  328 LEU B HB3  1 
ATOM   10273 H HG   . LEU B 1 319 ? 42.015  -4.687  61.542  1.00 113.09 ?  328 LEU B HG   1 
ATOM   10274 H HD11 . LEU B 1 319 ? 41.625  -7.013  61.636  1.00 110.05 ?  328 LEU B HD11 1 
ATOM   10275 H HD12 . LEU B 1 319 ? 42.935  -6.632  62.450  1.00 110.05 ?  328 LEU B HD12 1 
ATOM   10276 H HD13 . LEU B 1 319 ? 41.579  -6.932  63.222  1.00 110.05 ?  328 LEU B HD13 1 
ATOM   10277 H HD21 . LEU B 1 319 ? 39.778  -5.294  61.406  1.00 79.47  ?  328 LEU B HD21 1 
ATOM   10278 H HD22 . LEU B 1 319 ? 39.653  -5.172  62.985  1.00 79.47  ?  328 LEU B HD22 1 
ATOM   10279 H HD23 . LEU B 1 319 ? 39.930  -3.877  62.108  1.00 79.47  ?  328 LEU B HD23 1 
ATOM   10280 N N    . ARG B 1 320 ? 43.046  -2.132  65.641  1.00 80.87  ?  329 ARG B N    1 
ATOM   10281 C CA   . ARG B 1 320 ? 42.974  -1.712  67.020  1.00 72.92  ?  329 ARG B CA   1 
ATOM   10282 C C    . ARG B 1 320 ? 42.288  -0.360  67.123  1.00 76.87  ?  329 ARG B C    1 
ATOM   10283 O O    . ARG B 1 320 ? 41.451  -0.168  67.996  1.00 77.13  ?  329 ARG B O    1 
ATOM   10284 C CB   . ARG B 1 320 ? 44.364  -1.675  67.651  1.00 58.32  ?  329 ARG B CB   1 
ATOM   10285 C CG   . ARG B 1 320 ? 44.975  -3.021  67.994  1.00 77.89  ?  329 ARG B CG   1 
ATOM   10286 C CD   . ARG B 1 320 ? 46.081  -2.940  69.109  1.00 97.22  ?  329 ARG B CD   1 
ATOM   10287 N NE   . ARG B 1 320 ? 47.145  -2.009  68.782  1.00 82.29  ?  329 ARG B NE   1 
ATOM   10288 C CZ   . ARG B 1 320 ? 48.069  -2.236  67.867  1.00 92.62  ?  329 ARG B CZ   1 
ATOM   10289 N NH1  . ARG B 1 320 ? 48.062  -3.358  67.164  1.00 106.66 1  329 ARG B NH1  1 
ATOM   10290 N NH2  . ARG B 1 320 ? 48.990  -1.318  67.646  1.00 112.91 1  329 ARG B NH2  1 
ATOM   10291 H H    . ARG B 1 320 ? 43.834  -2.190  65.299  1.00 97.05  ?  329 ARG B H    1 
ATOM   10292 H HA   . ARG B 1 320 ? 42.441  -2.354  67.515  1.00 87.50  ?  329 ARG B HA   1 
ATOM   10293 H HB2  . ARG B 1 320 ? 44.967  -1.233  67.034  1.00 69.99  ?  329 ARG B HB2  1 
ATOM   10294 H HB3  . ARG B 1 320 ? 44.312  -1.163  68.473  1.00 69.99  ?  329 ARG B HB3  1 
ATOM   10295 H HG2  . ARG B 1 320 ? 44.274  -3.611  68.313  1.00 93.47  ?  329 ARG B HG2  1 
ATOM   10296 H HG3  . ARG B 1 320 ? 45.382  -3.393  67.197  1.00 93.47  ?  329 ARG B HG3  1 
ATOM   10297 H HD2  . ARG B 1 320 ? 45.673  -2.649  69.939  1.00 116.66 ?  329 ARG B HD2  1 
ATOM   10298 H HD3  . ARG B 1 320 ? 46.477  -3.818  69.225  1.00 116.66 ?  329 ARG B HD3  1 
ATOM   10299 H HE   . ARG B 1 320 ? 47.214  -1.295  69.256  1.00 98.75  ?  329 ARG B HE   1 
ATOM   10300 H HH11 . ARG B 1 320 ? 47.458  -3.952  67.309  1.00 127.99 ?  329 ARG B HH11 1 
ATOM   10301 H HH12 . ARG B 1 320 ? 48.666  -3.495  66.567  1.00 127.99 ?  329 ARG B HH12 1 
ATOM   10302 H HH21 . ARG B 1 320 ? 48.989  -0.590  68.103  1.00 135.49 ?  329 ARG B HH21 1 
ATOM   10303 H HH22 . ARG B 1 320 ? 49.596  -1.451  67.051  1.00 135.49 ?  329 ARG B HH22 1 
ATOM   10304 N N    . GLU B 1 321 ? 42.620  0.587   66.243  1.00 98.25  ?  330 GLU B N    1 
ATOM   10305 C CA   . GLU B 1 321 ? 42.024  1.919   66.342  1.00 75.58  ?  330 GLU B CA   1 
ATOM   10306 C C    . GLU B 1 321 ? 40.502  1.888   66.142  1.00 65.61  ?  330 GLU B C    1 
ATOM   10307 O O    . GLU B 1 321 ? 39.764  2.584   66.851  1.00 70.17  ?  330 GLU B O    1 
ATOM   10308 C CB   . GLU B 1 321 ? 42.688  2.880   65.346  1.00 77.10  ?  330 GLU B CB   1 
ATOM   10309 C CG   . GLU B 1 321 ? 44.016  3.493   65.812  1.00 97.62  ?  330 GLU B CG   1 
ATOM   10310 H H    . GLU B 1 321 ? 43.175  0.487   65.594  1.00 117.90 ?  330 GLU B H    1 
ATOM   10311 H HA   . GLU B 1 321 ? 42.191  2.264   67.233  1.00 90.69  ?  330 GLU B HA   1 
ATOM   10312 H HB2  . GLU B 1 321 ? 42.863  2.398   64.523  1.00 92.52  ?  330 GLU B HB2  1 
ATOM   10313 H HB3  . GLU B 1 321 ? 42.076  3.612   65.170  1.00 92.52  ?  330 GLU B HB3  1 
ATOM   10314 H HG2  . GLU B 1 321 ? 43.846  4.083   66.563  1.00 117.15 ?  330 GLU B HG2  1 
ATOM   10315 H HG3  . GLU B 1 321 ? 44.616  2.780   66.079  1.00 117.15 ?  330 GLU B HG3  1 
ATOM   10316 N N    . ALA B 1 322 ? 40.001  1.038   65.239  1.00 83.15  ?  331 ALA B N    1 
ATOM   10317 C CA   . ALA B 1 322 ? 38.551  0.975   65.008  1.00 80.70  ?  331 ALA B CA   1 
ATOM   10318 C C    . ALA B 1 322 ? 37.843  0.321   66.175  1.00 83.86  ?  331 ALA B C    1 
ATOM   10319 O O    . ALA B 1 322 ? 36.762  0.751   66.570  1.00 112.17 ?  331 ALA B O    1 
ATOM   10320 C CB   . ALA B 1 322 ? 38.229  0.201   63.734  1.00 76.29  ?  331 ALA B CB   1 
ATOM   10321 H H    . ALA B 1 322 ? 40.466  0.499   64.757  1.00 99.78  ?  331 ALA B H    1 
ATOM   10322 H HA   . ALA B 1 322 ? 38.205  1.876   64.911  1.00 96.83  ?  331 ALA B HA   1 
ATOM   10323 H HB1  . ALA B 1 322 ? 37.267  0.179   63.614  1.00 91.55  ?  331 ALA B HB1  1 
ATOM   10324 H HB2  . ALA B 1 322 ? 38.647  0.646   62.981  1.00 91.55  ?  331 ALA B HB2  1 
ATOM   10325 H HB3  . ALA B 1 322 ? 38.573  -0.702  63.819  1.00 91.55  ?  331 ALA B HB3  1 
ATOM   10326 N N    . TYR B 1 323 ? 38.436  -0.723  66.732  1.00 105.68 ?  332 TYR B N    1 
ATOM   10327 C CA   . TYR B 1 323 ? 37.903  -1.304  67.949  1.00 88.38  ?  332 TYR B CA   1 
ATOM   10328 C C    . TYR B 1 323 ? 37.865  -0.270  69.065  1.00 81.29  ?  332 TYR B C    1 
ATOM   10329 O O    . TYR B 1 323 ? 36.870  -0.154  69.785  1.00 90.47  ?  332 TYR B O    1 
ATOM   10330 C CB   . TYR B 1 323 ? 38.763  -2.517  68.343  1.00 47.84  ?  332 TYR B CB   1 
ATOM   10331 C CG   . TYR B 1 323 ? 38.427  -3.087  69.702  1.00 62.96  ?  332 TYR B CG   1 
ATOM   10332 C CD1  . TYR B 1 323 ? 37.473  -4.123  69.843  1.00 67.27  ?  332 TYR B CD1  1 
ATOM   10333 C CD2  . TYR B 1 323 ? 39.013  -2.578  70.853  1.00 77.06  ?  332 TYR B CD2  1 
ATOM   10334 C CE1  . TYR B 1 323 ? 37.107  -4.626  71.099  1.00 48.05  ?  332 TYR B CE1  1 
ATOM   10335 C CE2  . TYR B 1 323 ? 38.660  -3.083  72.117  1.00 75.29  ?  332 TYR B CE2  1 
ATOM   10336 C CZ   . TYR B 1 323 ? 37.708  -4.101  72.210  1.00 56.83  ?  332 TYR B CZ   1 
ATOM   10337 O OH   . TYR B 1 323 ? 37.343  -4.572  73.416  1.00 40.83  ?  332 TYR B OH   1 
ATOM   10338 H H    . TYR B 1 323 ? 39.142  -1.110  66.429  1.00 126.81 ?  332 TYR B H    1 
ATOM   10339 H HA   . TYR B 1 323 ? 36.997  -1.612  67.787  1.00 106.06 ?  332 TYR B HA   1 
ATOM   10340 H HB2  . TYR B 1 323 ? 38.632  -3.219  67.687  1.00 57.40  ?  332 TYR B HB2  1 
ATOM   10341 H HB3  . TYR B 1 323 ? 39.695  -2.248  68.356  1.00 57.40  ?  332 TYR B HB3  1 
ATOM   10342 H HD1  . TYR B 1 323 ? 37.060  -4.463  69.082  1.00 80.72  ?  332 TYR B HD1  1 
ATOM   10343 H HD2  . TYR B 1 323 ? 39.636  -1.891  70.789  1.00 92.47  ?  332 TYR B HD2  1 
ATOM   10344 H HE1  . TYR B 1 323 ? 36.475  -5.304  71.174  1.00 57.66  ?  332 TYR B HE1  1 
ATOM   10345 H HE2  . TYR B 1 323 ? 39.050  -2.735  72.886  1.00 90.35  ?  332 TYR B HE2  1 
ATOM   10346 H HH   . TYR B 1 323 ? 36.756  -5.166  73.326  1.00 49.00  ?  332 TYR B HH   1 
ATOM   10347 N N    . ASP B 1 324 ? 38.948  0.493   69.217  1.00 61.29  ?  333 ASP B N    1 
ATOM   10348 C CA   . ASP B 1 324 ? 39.039  1.517   70.257  1.00 65.82  ?  333 ASP B CA   1 
ATOM   10349 C C    . ASP B 1 324 ? 37.955  2.556   70.107  1.00 71.59  ?  333 ASP B C    1 
ATOM   10350 O O    . ASP B 1 324 ? 37.476  3.090   71.101  1.00 72.32  ?  333 ASP B O    1 
ATOM   10351 C CB   . ASP B 1 324 ? 40.410  2.202   70.238  1.00 103.23 ?  333 ASP B CB   1 
ATOM   10352 C CG   . ASP B 1 324 ? 41.517  1.404   70.966  1.00 122.80 ?  333 ASP B CG   1 
ATOM   10353 O OD1  . ASP B 1 324 ? 41.195  0.612   71.881  1.00 97.23  ?  333 ASP B OD1  1 
ATOM   10354 O OD2  . ASP B 1 324 ? 42.719  1.578   70.629  1.00 146.19 -1 333 ASP B OD2  1 
ATOM   10355 H H    . ASP B 1 324 ? 39.650  0.437   68.724  1.00 73.55  ?  333 ASP B H    1 
ATOM   10356 H HA   . ASP B 1 324 ? 38.929  1.095   71.124  1.00 78.98  ?  333 ASP B HA   1 
ATOM   10357 H HB2  . ASP B 1 324 ? 40.687  2.320   69.316  1.00 123.87 ?  333 ASP B HB2  1 
ATOM   10358 H HB3  . ASP B 1 324 ? 40.334  3.067   70.671  1.00 123.87 ?  333 ASP B HB3  1 
ATOM   10359 N N    . ALA B 1 325 ? 37.553  2.837   68.877  1.00 63.19  ?  334 ALA B N    1 
ATOM   10360 C CA   . ALA B 1 325 ? 36.566  3.865   68.627  1.00 84.02  ?  334 ALA B CA   1 
ATOM   10361 C C    . ALA B 1 325 ? 35.234  3.457   69.216  1.00 126.59 ?  334 ALA B C    1 
ATOM   10362 O O    . ALA B 1 325 ? 34.598  4.248   69.922  1.00 79.77  ?  334 ALA B O    1 
ATOM   10363 C CB   . ALA B 1 325 ? 36.437  4.091   67.127  1.00 77.15  ?  334 ALA B CB   1 
ATOM   10364 H H    . ALA B 1 325 ? 37.840  2.442   68.169  1.00 75.83  ?  334 ALA B H    1 
ATOM   10365 H HA   . ALA B 1 325 ? 36.847  4.695   69.042  1.00 100.82 ?  334 ALA B HA   1 
ATOM   10366 H HB1  . ALA B 1 325 ? 35.774  4.781   66.968  1.00 92.59  ?  334 ALA B HB1  1 
ATOM   10367 H HB2  . ALA B 1 325 ? 37.296  4.371   66.775  1.00 92.59  ?  334 ALA B HB2  1 
ATOM   10368 H HB3  . ALA B 1 325 ? 36.160  3.263   66.705  1.00 92.59  ?  334 ALA B HB3  1 
ATOM   10369 N N    . CYS B 1 326 ? 34.846  2.191   69.019  1.00 121.48 ?  335 CYS B N    1 
ATOM   10370 C CA   . CYS B 1 326 ? 33.619  1.700   69.626  1.00 73.07  ?  335 CYS B CA   1 
ATOM   10371 C C    . CYS B 1 326 ? 33.733  1.719   71.144  1.00 77.75  ?  335 CYS B C    1 
ATOM   10372 O O    . CYS B 1 326 ? 32.758  1.976   71.845  1.00 64.56  ?  335 CYS B O    1 
ATOM   10373 C CB   . CYS B 1 326 ? 33.301  0.289   69.176  1.00 57.79  ?  335 CYS B CB   1 
ATOM   10374 S SG   . CYS B 1 326 ? 33.160  -0.065  67.397  1.00 59.40  ?  335 CYS B SG   1 
ATOM   10375 H H    . CYS B 1 326 ? 35.272  1.612   68.547  1.00 145.78 ?  335 CYS B H    1 
ATOM   10376 H HA   . CYS B 1 326 ? 32.882  2.275   69.368  1.00 87.68  ?  335 CYS B HA   1 
ATOM   10377 H HB2  . CYS B 1 326 ? 33.996  -0.293  69.521  1.00 69.35  ?  335 CYS B HB2  1 
ATOM   10378 H HB3  . CYS B 1 326 ? 32.454  0.037   69.577  1.00 69.35  ?  335 CYS B HB3  1 
ATOM   10379 H HG   . CYS B 1 326 ? 32.906  -1.229  67.249  1.00 71.28  ?  335 CYS B HG   1 
ATOM   10380 N N    . VAL B 1 327 ? 34.912  1.441   71.685  1.00 72.31  ?  336 VAL B N    1 
ATOM   10381 C CA   . VAL B 1 327 ? 35.074  1.578   73.129  1.00 73.06  ?  336 VAL B CA   1 
ATOM   10382 C C    . VAL B 1 327 ? 34.920  3.037   73.521  1.00 78.80  ?  336 VAL B C    1 
ATOM   10383 O O    . VAL B 1 327 ? 34.273  3.353   74.526  1.00 73.40  ?  336 VAL B O    1 
ATOM   10384 C CB   . VAL B 1 327 ? 36.438  0.996   73.556  1.00 70.05  ?  336 VAL B CB   1 
ATOM   10385 C CG1  . VAL B 1 327 ? 36.730  1.138   75.138  1.00 48.71  ?  336 VAL B CG1  1 
ATOM   10386 C CG2  . VAL B 1 327 ? 36.548  -0.447  73.124  1.00 60.89  ?  336 VAL B CG2  1 
ATOM   10387 H H    . VAL B 1 327 ? 35.611  1.180   71.258  1.00 86.77  ?  336 VAL B H    1 
ATOM   10388 H HA   . VAL B 1 327 ? 34.378  1.071   73.576  1.00 87.67  ?  336 VAL B HA   1 
ATOM   10389 H HB   . VAL B 1 327 ? 37.134  1.487   73.092  1.00 84.06  ?  336 VAL B HB   1 
ATOM   10390 H HG11 . VAL B 1 327 ? 37.599  0.754   75.333  1.00 58.45  ?  336 VAL B HG11 1 
ATOM   10391 H HG12 . VAL B 1 327 ? 36.723  2.078   75.376  1.00 58.45  ?  336 VAL B HG12 1 
ATOM   10392 H HG13 . VAL B 1 327 ? 36.041  0.666   75.629  1.00 58.45  ?  336 VAL B HG13 1 
ATOM   10393 H HG21 . VAL B 1 327 ? 37.410  -0.795  73.401  1.00 73.07  ?  336 VAL B HG21 1 
ATOM   10394 H HG22 . VAL B 1 327 ? 35.836  -0.957  73.542  1.00 73.07  ?  336 VAL B HG22 1 
ATOM   10395 H HG23 . VAL B 1 327 ? 36.466  -0.495  72.159  1.00 73.07  ?  336 VAL B HG23 1 
ATOM   10396 N N    . LYS B 1 328 ? 35.481  3.945   72.702  1.00 83.48  ?  337 LYS B N    1 
ATOM   10397 C CA   . LYS B 1 328 ? 35.425  5.373   72.972  1.00 71.18  ?  337 LYS B CA   1 
ATOM   10398 C C    . LYS B 1 328 ? 33.987  5.842   73.009  1.00 70.18  ?  337 LYS B C    1 
ATOM   10399 O O    . LYS B 1 328 ? 33.600  6.587   73.919  1.00 82.40  ?  337 LYS B O    1 
ATOM   10400 C CB   . LYS B 1 328 ? 36.189  6.146   71.902  1.00 117.24 ?  337 LYS B CB   1 
ATOM   10401 H H    . LYS B 1 328 ? 35.901  3.745   71.979  1.00 100.17 ?  337 LYS B H    1 
ATOM   10402 H HA   . LYS B 1 328 ? 35.831  5.556   73.834  1.00 85.41  ?  337 LYS B HA   1 
ATOM   10403 N N    . ALA B 1 329 ? 33.158  5.329   72.085  1.00 71.74  ?  338 ALA B N    1 
ATOM   10404 C CA   . ALA B 1 329 ? 31.742  5.704   72.061  1.00 70.57  ?  338 ALA B CA   1 
ATOM   10405 C C    . ALA B 1 329 ? 31.015  5.223   73.305  1.00 58.04  ?  338 ALA B C    1 
ATOM   10406 O O    . ALA B 1 329 ? 30.232  5.974   73.893  1.00 51.89  ?  338 ALA B O    1 
ATOM   10407 C CB   . ALA B 1 329 ? 31.031  5.182   70.821  1.00 80.98  ?  338 ALA B CB   1 
ATOM   10408 H H    . ALA B 1 329 ? 33.390  4.771   71.473  1.00 86.09  ?  338 ALA B H    1 
ATOM   10409 H HA   . ALA B 1 329 ? 31.682  6.672   72.045  1.00 84.68  ?  338 ALA B HA   1 
ATOM   10410 H HB1  . ALA B 1 329 ? 30.101  5.456   70.852  1.00 97.18  ?  338 ALA B HB1  1 
ATOM   10411 H HB2  . ALA B 1 329 ? 31.459  5.552   70.033  1.00 97.18  ?  338 ALA B HB2  1 
ATOM   10412 H HB3  . ALA B 1 329 ? 31.091  4.214   70.807  1.00 97.18  ?  338 ALA B HB3  1 
ATOM   10413 N N    . LEU B 1 330 ? 31.289  4.019   73.766  1.00 79.50  ?  339 LEU B N    1 
ATOM   10414 C CA   . LEU B 1 330 ? 30.606  3.561   74.965  1.00 65.42  ?  339 LEU B CA   1 
ATOM   10415 C C    . LEU B 1 330 ? 30.960  4.392   76.178  1.00 75.79  ?  339 LEU B C    1 
ATOM   10416 O O    . LEU B 1 330 ? 30.072  4.828   76.911  1.00 88.53  ?  339 LEU B O    1 
ATOM   10417 C CB   . LEU B 1 330 ? 30.964  2.091   75.220  1.00 50.90  ?  339 LEU B CB   1 
ATOM   10418 C CG   . LEU B 1 330 ? 30.256  1.087   74.299  1.00 52.29  ?  339 LEU B CG   1 
ATOM   10419 C CD1  . LEU B 1 330 ? 30.662  -0.345  74.501  1.00 49.02  ?  339 LEU B CD1  1 
ATOM   10420 C CD2  . LEU B 1 330 ? 28.810  1.119   74.656  1.00 74.75  ?  339 LEU B CD2  1 
ATOM   10421 H H    . LEU B 1 330 ? 31.845  3.461   73.420  1.00 95.41  ?  339 LEU B H    1 
ATOM   10422 H HA   . LEU B 1 330 ? 29.648  3.621   74.828  1.00 78.50  ?  339 LEU B HA   1 
ATOM   10423 H HB2  . LEU B 1 330 ? 31.919  1.979   75.096  1.00 61.08  ?  339 LEU B HB2  1 
ATOM   10424 H HB3  . LEU B 1 330 ? 30.725  1.868   76.133  1.00 61.08  ?  339 LEU B HB3  1 
ATOM   10425 H HG   . LEU B 1 330 ? 30.368  1.333   73.367  1.00 62.75  ?  339 LEU B HG   1 
ATOM   10426 H HD11 . LEU B 1 330 ? 30.168  -0.904  73.881  1.00 58.82  ?  339 LEU B HD11 1 
ATOM   10427 H HD12 . LEU B 1 330 ? 31.614  -0.430  74.337  1.00 58.82  ?  339 LEU B HD12 1 
ATOM   10428 H HD13 . LEU B 1 330 ? 30.459  -0.604  75.414  1.00 58.82  ?  339 LEU B HD13 1 
ATOM   10429 H HD21 . LEU B 1 330 ? 28.332  0.493   74.090  1.00 89.69  ?  339 LEU B HD21 1 
ATOM   10430 H HD22 . LEU B 1 330 ? 28.710  0.866   75.587  1.00 89.69  ?  339 LEU B HD22 1 
ATOM   10431 H HD23 . LEU B 1 330 ? 28.471  2.017   74.518  1.00 89.69  ?  339 LEU B HD23 1 
ATOM   10432 N N    . VAL B 1 331 ? 32.236  4.701   76.364  1.00 86.06  ?  340 VAL B N    1 
ATOM   10433 C CA   . VAL B 1 331 ? 32.594  5.476   77.539  1.00 97.48  ?  340 VAL B CA   1 
ATOM   10434 C C    . VAL B 1 331 ? 31.872  6.821   77.530  1.00 73.26  ?  340 VAL B C    1 
ATOM   10435 O O    . VAL B 1 331 ? 31.367  7.263   78.570  1.00 63.66  ?  340 VAL B O    1 
ATOM   10436 C CB   . VAL B 1 331 ? 34.119  5.612   77.598  1.00 101.20 ?  340 VAL B CB   1 
ATOM   10437 C CG1  . VAL B 1 331 ? 34.537  6.534   78.754  1.00 73.78  ?  340 VAL B CG1  1 
ATOM   10438 C CG2  . VAL B 1 331 ? 34.729  4.233   77.728  1.00 116.77 ?  340 VAL B CG2  1 
ATOM   10439 H H    . VAL B 1 331 ? 32.889  4.484   75.848  1.00 103.27 ?  340 VAL B H    1 
ATOM   10440 H HA   . VAL B 1 331 ? 32.309  4.993   78.331  1.00 116.98 ?  340 VAL B HA   1 
ATOM   10441 H HB   . VAL B 1 331 ? 34.435  6.005   76.769  1.00 121.44 ?  340 VAL B HB   1 
ATOM   10442 H HG11 . VAL B 1 331 ? 35.505  6.603   78.768  1.00 88.54  ?  340 VAL B HG11 1 
ATOM   10443 H HG12 . VAL B 1 331 ? 34.145  7.411   78.616  1.00 88.54  ?  340 VAL B HG12 1 
ATOM   10444 H HG13 . VAL B 1 331 ? 34.220  6.157   79.589  1.00 88.54  ?  340 VAL B HG13 1 
ATOM   10445 H HG21 . VAL B 1 331 ? 35.695  4.317   77.765  1.00 140.13 ?  340 VAL B HG21 1 
ATOM   10446 H HG22 . VAL B 1 331 ? 34.402  3.819   78.541  1.00 140.13 ?  340 VAL B HG22 1 
ATOM   10447 H HG23 . VAL B 1 331 ? 34.473  3.701   76.958  1.00 140.13 ?  340 VAL B HG23 1 
ATOM   10448 N N    . SER B 1 332 ? 31.677  7.410   76.340  1.00 57.72  ?  341 SER B N    1 
ATOM   10449 C CA   . SER B 1 332 ? 30.984  8.686   76.237  1.00 74.08  ?  341 SER B CA   1 
ATOM   10450 C C    . SER B 1 332 ? 29.569  8.551   76.788  1.00 75.68  ?  341 SER B C    1 
ATOM   10451 O O    . SER B 1 332 ? 29.060  9.427   77.502  1.00 92.37  ?  341 SER B O    1 
ATOM   10452 C CB   . SER B 1 332 ? 30.955  9.118   74.775  1.00 131.96 ?  341 SER B CB   1 
ATOM   10453 O OG   . SER B 1 332 ? 32.258  9.219   74.255  1.00 144.21 ?  341 SER B OG   1 
ATOM   10454 H H    . SER B 1 332 ? 31.938  7.088   75.586  1.00 69.26  ?  341 SER B H    1 
ATOM   10455 H HA   . SER B 1 332 ? 31.456  9.358   76.752  1.00 88.90  ?  341 SER B HA   1 
ATOM   10456 H HB2  . SER B 1 332 ? 30.460  8.460   74.262  1.00 158.35 ?  341 SER B HB2  1 
ATOM   10457 H HB3  . SER B 1 332 ? 30.521  9.983   74.711  1.00 158.35 ?  341 SER B HB3  1 
ATOM   10458 H HG   . SER B 1 332 ? 32.645  8.475   74.305  1.00 173.05 ?  341 SER B HG   1 
ATOM   10459 N N    . LEU B 1 333 ? 28.934  7.433   76.469  1.00 74.08  ?  342 LEU B N    1 
ATOM   10460 C CA   . LEU B 1 333 ? 27.572  7.147   76.906  1.00 61.99  ?  342 LEU B CA   1 
ATOM   10461 C C    . LEU B 1 333 ? 27.517  6.829   78.384  1.00 37.05  ?  342 LEU B C    1 
ATOM   10462 O O    . LEU B 1 333 ? 26.595  7.228   79.085  1.00 47.20  ?  342 LEU B O    1 
ATOM   10463 C CB   . LEU B 1 333 ? 27.031  6.012   76.086  1.00 63.73  ?  342 LEU B CB   1 
ATOM   10464 C CG   . LEU B 1 333 ? 26.649  6.402   74.654  1.00 56.01  ?  342 LEU B CG   1 
ATOM   10465 C CD1  . LEU B 1 333 ? 26.824  5.257   73.650  1.00 67.52  ?  342 LEU B CD1  1 
ATOM   10466 C CD2  . LEU B 1 333 ? 25.261  6.716   74.761  1.00 64.77  ?  342 LEU B CD2  1 
ATOM   10467 H H    . LEU B 1 333 ? 29.278  6.809   75.988  1.00 88.89  ?  342 LEU B H    1 
ATOM   10468 H HA   . LEU B 1 333 ? 27.017  7.926   76.745  1.00 74.38  ?  342 LEU B HA   1 
ATOM   10469 H HB2  . LEU B 1 333 ? 27.705  5.316   76.033  1.00 76.48  ?  342 LEU B HB2  1 
ATOM   10470 H HB3  . LEU B 1 333 ? 26.236  5.665   76.520  1.00 76.48  ?  342 LEU B HB3  1 
ATOM   10471 H HG   . LEU B 1 333 ? 27.144  7.183   74.362  1.00 67.21  ?  342 LEU B HG   1 
ATOM   10472 H HD11 . LEU B 1 333 ? 26.567  5.570   72.768  1.00 81.02  ?  342 LEU B HD11 1 
ATOM   10473 H HD12 . LEU B 1 333 ? 27.754  4.982   73.645  1.00 81.02  ?  342 LEU B HD12 1 
ATOM   10474 H HD13 . LEU B 1 333 ? 26.260  4.515   73.916  1.00 81.02  ?  342 LEU B HD13 1 
ATOM   10475 H HD21 . LEU B 1 333 ? 24.929  6.978   73.888  1.00 77.72  ?  342 LEU B HD21 1 
ATOM   10476 H HD22 . LEU B 1 333 ? 24.783  5.932   75.075  1.00 77.72  ?  342 LEU B HD22 1 
ATOM   10477 H HD23 . LEU B 1 333 ? 25.150  7.446   75.390  1.00 77.72  ?  342 LEU B HD23 1 
ATOM   10478 N N    . ARG B 1 334 ? 28.503  6.189   78.908  1.00 41.91  ?  343 ARG B N    1 
ATOM   10479 C CA   . ARG B 1 334 ? 28.422  5.979   80.338  1.00 40.87  ?  343 ARG B CA   1 
ATOM   10480 C C    . ARG B 1 334 ? 28.645  7.271   81.100  1.00 57.70  ?  343 ARG B C    1 
ATOM   10481 O O    . ARG B 1 334 ? 28.137  7.433   82.207  1.00 89.26  ?  343 ARG B O    1 
ATOM   10482 C CB   . ARG B 1 334 ? 29.426  4.895   80.668  1.00 75.63  ?  343 ARG B CB   1 
ATOM   10483 C CG   . ARG B 1 334 ? 29.084  3.588   79.894  1.00 108.62 ?  343 ARG B CG   1 
ATOM   10484 C CD   . ARG B 1 334 ? 28.358  2.578   80.744  1.00 101.78 ?  343 ARG B CD   1 
ATOM   10485 N NE   . ARG B 1 334 ? 27.580  1.581   79.997  1.00 124.65 ?  343 ARG B NE   1 
ATOM   10486 C CZ   . ARG B 1 334 ? 28.085  0.628   79.215  1.00 80.82  ?  343 ARG B CZ   1 
ATOM   10487 N NH1  . ARG B 1 334 ? 29.384  0.517   79.028  1.00 74.99  1  343 ARG B NH1  1 
ATOM   10488 N NH2  . ARG B 1 334 ? 27.280  -0.240  78.624  1.00 92.98  1  343 ARG B NH2  1 
ATOM   10489 H H    . ARG B 1 334 ? 29.195  5.877   78.505  1.00 50.29  ?  343 ARG B H    1 
ATOM   10490 H HA   . ARG B 1 334 ? 27.538  5.649   80.560  1.00 49.05  ?  343 ARG B HA   1 
ATOM   10491 H HB2  . ARG B 1 334 ? 30.314  5.184   80.405  1.00 90.76  ?  343 ARG B HB2  1 
ATOM   10492 H HB3  . ARG B 1 334 ? 29.398  4.706   81.619  1.00 90.76  ?  343 ARG B HB3  1 
ATOM   10493 H HG2  . ARG B 1 334 ? 28.515  3.808   79.139  1.00 130.35 ?  343 ARG B HG2  1 
ATOM   10494 H HG3  . ARG B 1 334 ? 29.907  3.181   79.582  1.00 130.35 ?  343 ARG B HG3  1 
ATOM   10495 H HD2  . ARG B 1 334 ? 29.011  2.098   81.278  1.00 122.14 ?  343 ARG B HD2  1 
ATOM   10496 H HD3  . ARG B 1 334 ? 27.744  3.050   81.328  1.00 122.14 ?  343 ARG B HD3  1 
ATOM   10497 H HE   . ARG B 1 334 ? 26.724  1.616   80.071  1.00 149.59 ?  343 ARG B HE   1 
ATOM   10498 H HH11 . ARG B 1 334 ? 29.923  1.065   79.414  1.00 89.99  ?  343 ARG B HH11 1 
ATOM   10499 H HH12 . ARG B 1 334 ? 29.694  -0.103  78.518  1.00 89.99  ?  343 ARG B HH12 1 
ATOM   10500 H HH21 . ARG B 1 334 ? 26.429  -0.178  78.730  1.00 111.58 ?  343 ARG B HH21 1 
ATOM   10501 H HH22 . ARG B 1 334 ? 27.606  -0.846  78.108  1.00 111.58 ?  343 ARG B HH22 1 
ATOM   10502 N N    . SER B 1 335 ? 29.444  8.182   80.554  1.00 71.26  ?  344 SER B N    1 
ATOM   10503 C CA   . SER B 1 335 ? 29.702  9.443   81.240  1.00 71.24  ?  344 SER B CA   1 
ATOM   10504 C C    . SER B 1 335 ? 28.518  10.401  81.102  1.00 68.77  ?  344 SER B C    1 
ATOM   10505 O O    . SER B 1 335 ? 28.152  11.067  82.072  1.00 80.59  ?  344 SER B O    1 
ATOM   10506 C CB   . SER B 1 335 ? 31.008  10.057  80.715  1.00 61.58  ?  344 SER B CB   1 
ATOM   10507 O OG   . SER B 1 335 ? 32.137  9.339   81.159  1.00 85.38  ?  344 SER B OG   1 
ATOM   10508 H H    . SER B 1 335 ? 29.844  8.097   79.797  1.00 85.51  ?  344 SER B H    1 
ATOM   10509 H HA   . SER B 1 335 ? 29.823  9.262   82.185  1.00 85.48  ?  344 SER B HA   1 
ATOM   10510 H HB2  . SER B 1 335 ? 30.992  10.047  79.746  1.00 73.90  ?  344 SER B HB2  1 
ATOM   10511 H HB3  . SER B 1 335 ? 31.074  10.971  81.034  1.00 73.90  ?  344 SER B HB3  1 
ATOM   10512 H HG   . SER B 1 335 ? 32.838  9.692   80.860  1.00 102.46 ?  344 SER B HG   1 
ATOM   10513 N N    . TYR B 1 336 ? 27.853  10.434  79.934  1.00 54.76  ?  345 TYR B N    1 
ATOM   10514 C CA   . TYR B 1 336 ? 26.709  11.323  79.833  1.00 81.77  ?  345 TYR B CA   1 
ATOM   10515 C C    . TYR B 1 336 ? 25.623  10.865  80.787  1.00 122.64 ?  345 TYR B C    1 
ATOM   10516 O O    . TYR B 1 336 ? 25.031  11.676  81.508  1.00 88.19  ?  345 TYR B O    1 
ATOM   10517 C CB   . TYR B 1 336 ? 26.161  11.388  78.409  1.00 85.40  ?  345 TYR B CB   1 
ATOM   10518 C CG   . TYR B 1 336 ? 25.409  12.686  78.220  1.00 94.54  ?  345 TYR B CG   1 
ATOM   10519 C CD1  . TYR B 1 336 ? 26.122  13.853  78.023  1.00 117.72 ?  345 TYR B CD1  1 
ATOM   10520 C CD2  . TYR B 1 336 ? 24.026  12.769  78.321  1.00 104.34 ?  345 TYR B CD2  1 
ATOM   10521 C CE1  . TYR B 1 336 ? 25.506  15.049  77.887  1.00 113.41 ?  345 TYR B CE1  1 
ATOM   10522 C CE2  . TYR B 1 336 ? 23.384  13.986  78.187  1.00 58.71  ?  345 TYR B CE2  1 
ATOM   10523 C CZ   . TYR B 1 336 ? 24.143  15.127  77.978  1.00 95.35  ?  345 TYR B CZ   1 
ATOM   10524 O OH   . TYR B 1 336 ? 23.598  16.377  77.849  1.00 106.80 ?  345 TYR B OH   1 
ATOM   10525 H H    . TYR B 1 336 ? 28.038  9.977   79.230  1.00 65.71  ?  345 TYR B H    1 
ATOM   10526 H HA   . TYR B 1 336 ? 26.980  12.218  80.091  1.00 98.13  ?  345 TYR B HA   1 
ATOM   10527 H HB2  . TYR B 1 336 ? 26.895  11.358  77.775  1.00 102.48 ?  345 TYR B HB2  1 
ATOM   10528 H HB3  . TYR B 1 336 ? 25.550  10.650  78.260  1.00 102.48 ?  345 TYR B HB3  1 
ATOM   10529 H HD1  . TYR B 1 336 ? 27.050  13.814  77.969  1.00 141.27 ?  345 TYR B HD1  1 
ATOM   10530 H HD2  . TYR B 1 336 ? 23.527  11.998  78.469  1.00 125.20 ?  345 TYR B HD2  1 
ATOM   10531 H HE1  . TYR B 1 336 ? 26.008  15.820  77.751  1.00 136.09 ?  345 TYR B HE1  1 
ATOM   10532 H HE2  . TYR B 1 336 ? 22.458  14.041  78.247  1.00 70.46  ?  345 TYR B HE2  1 
ATOM   10533 H HH   . TYR B 1 336 ? 22.761  16.335  77.917  1.00 128.16 ?  345 TYR B HH   1 
ATOM   10534 N N    . HIS B 1 337 ? 25.435  9.553   80.890  1.00 66.32  ?  346 HIS B N    1 
ATOM   10535 C CA   . HIS B 1 337 ? 24.484  9.024   81.843  1.00 77.14  ?  346 HIS B CA   1 
ATOM   10536 C C    . HIS B 1 337 ? 24.796  9.530   83.238  1.00 68.60  ?  346 HIS B C    1 
ATOM   10537 O O    . HIS B 1 337 ? 23.922  10.042  83.956  1.00 70.58  ?  346 HIS B O    1 
ATOM   10538 C CB   . HIS B 1 337 ? 24.537  7.507   81.799  1.00 92.60  ?  346 HIS B CB   1 
ATOM   10539 C CG   . HIS B 1 337 ? 23.379  6.838   82.461  1.00 77.66  ?  346 HIS B CG   1 
ATOM   10540 N ND1  . HIS B 1 337 ? 22.528  5.981   81.801  1.00 89.53  ?  346 HIS B ND1  1 
ATOM   10541 C CD2  . HIS B 1 337 ? 22.929  6.904   83.731  1.00 97.42  ?  346 HIS B CD2  1 
ATOM   10542 C CE1  . HIS B 1 337 ? 21.606  5.548   82.637  1.00 106.81 ?  346 HIS B CE1  1 
ATOM   10543 N NE2  . HIS B 1 337 ? 21.827  6.094   83.815  1.00 116.07 ?  346 HIS B NE2  1 
ATOM   10544 H H    . HIS B 1 337 ? 25.843  8.958   80.422  1.00 79.59  ?  346 HIS B H    1 
ATOM   10545 H HA   . HIS B 1 337 ? 23.589  9.310   81.603  1.00 92.57  ?  346 HIS B HA   1 
ATOM   10546 H HB2  . HIS B 1 337 ? 24.552  7.222   80.871  1.00 111.12 ?  346 HIS B HB2  1 
ATOM   10547 H HB3  . HIS B 1 337 ? 25.345  7.210   82.246  1.00 111.12 ?  346 HIS B HB3  1 
ATOM   10548 H HD2  . HIS B 1 337 ? 23.299  7.406   84.422  1.00 116.90 ?  346 HIS B HD2  1 
ATOM   10549 H HE1  . HIS B 1 337 ? 20.917  4.959   82.430  1.00 128.17 ?  346 HIS B HE1  1 
ATOM   10550 H HE2  . HIS B 1 337 ? 21.356  5.963   84.523  1.00 139.29 ?  346 HIS B HE2  1 
ATOM   10551 N N    . LEU B 1 338 ? 26.039  9.387   83.644  1.00 53.79  ?  347 LEU B N    1 
ATOM   10552 C CA   . LEU B 1 338 ? 26.440  9.892   84.938  1.00 69.82  ?  347 LEU B CA   1 
ATOM   10553 C C    . LEU B 1 338 ? 26.187  11.381  85.043  1.00 87.81  ?  347 LEU B C    1 
ATOM   10554 O O    . LEU B 1 338 ? 25.830  11.873  86.113  1.00 77.18  ?  347 LEU B O    1 
ATOM   10555 C CB   . LEU B 1 338 ? 27.905  9.558   85.158  1.00 75.60  ?  347 LEU B CB   1 
ATOM   10556 C CG   . LEU B 1 338 ? 28.164  8.095   85.558  1.00 56.44  ?  347 LEU B CG   1 
ATOM   10557 C CD1  . LEU B 1 338 ? 29.542  7.646   85.222  1.00 67.80  ?  347 LEU B CD1  1 
ATOM   10558 C CD2  . LEU B 1 338 ? 27.939  7.934   87.067  1.00 47.98  ?  347 LEU B CD2  1 
ATOM   10559 H H    . LEU B 1 338 ? 26.666  9.005   83.195  1.00 64.55  ?  347 LEU B H    1 
ATOM   10560 H HA   . LEU B 1 338 ? 25.922  9.448   85.627  1.00 83.78  ?  347 LEU B HA   1 
ATOM   10561 H HB2  . LEU B 1 338 ? 28.391  9.729   84.335  1.00 90.72  ?  347 LEU B HB2  1 
ATOM   10562 H HB3  . LEU B 1 338 ? 28.251  10.123  85.866  1.00 90.72  ?  347 LEU B HB3  1 
ATOM   10563 H HG   . LEU B 1 338 ? 27.535  7.521   85.094  1.00 67.73  ?  347 LEU B HG   1 
ATOM   10564 H HD11 . LEU B 1 338 ? 29.648  6.721   85.495  1.00 81.36  ?  347 LEU B HD11 1 
ATOM   10565 H HD12 . LEU B 1 338 ? 29.675  7.725   84.264  1.00 81.36  ?  347 LEU B HD12 1 
ATOM   10566 H HD13 . LEU B 1 338 ? 30.180  8.205   85.692  1.00 81.36  ?  347 LEU B HD13 1 
ATOM   10567 H HD21 . LEU B 1 338 ? 28.104  7.011   87.313  1.00 57.58  ?  347 LEU B HD21 1 
ATOM   10568 H HD22 . LEU B 1 338 ? 28.553  8.518   87.541  1.00 57.58  ?  347 LEU B HD22 1 
ATOM   10569 H HD23 . LEU B 1 338 ? 27.024  8.175   87.277  1.00 57.58  ?  347 LEU B HD23 1 
ATOM   10570 N N    . GLN B 1 339 ? 26.354  12.127  83.964  1.00 86.38  ?  348 GLN B N    1 
ATOM   10571 C CA   . GLN B 1 339 ? 26.038  13.531  84.112  1.00 66.81  ?  348 GLN B CA   1 
ATOM   10572 C C    . GLN B 1 339 ? 24.559  13.680  84.405  1.00 73.87  ?  348 GLN B C    1 
ATOM   10573 O O    . GLN B 1 339 ? 24.172  14.412  85.334  1.00 68.42  ?  348 GLN B O    1 
ATOM   10574 C CB   . GLN B 1 339 ? 26.417  14.322  82.860  1.00 85.42  ?  348 GLN B CB   1 
ATOM   10575 C CG   . GLN B 1 339 ? 27.935  14.561  82.706  1.00 77.18  ?  348 GLN B CG   1 
ATOM   10576 C CD   . GLN B 1 339 ? 28.308  15.151  81.359  1.00 80.68  ?  348 GLN B CD   1 
ATOM   10577 O OE1  . GLN B 1 339 ? 27.724  16.126  80.885  1.00 116.45 ?  348 GLN B OE1  1 
ATOM   10578 N NE2  . GLN B 1 339 ? 29.288  14.556  80.741  1.00 64.98  ?  348 GLN B NE2  1 
ATOM   10579 H H    . GLN B 1 339 ? 26.627  11.869  83.190  1.00 103.66 ?  348 GLN B H    1 
ATOM   10580 H HA   . GLN B 1 339 ? 26.535  13.893  84.862  1.00 80.17  ?  348 GLN B HA   1 
ATOM   10581 H HB2  . GLN B 1 339 ? 26.114  13.834  82.079  1.00 102.50 ?  348 GLN B HB2  1 
ATOM   10582 H HB3  . GLN B 1 339 ? 25.983  15.189  82.896  1.00 102.50 ?  348 GLN B HB3  1 
ATOM   10583 H HG2  . GLN B 1 339 ? 28.228  15.179  83.395  1.00 92.61  ?  348 GLN B HG2  1 
ATOM   10584 H HG3  . GLN B 1 339 ? 28.398  13.715  82.801  1.00 92.61  ?  348 GLN B HG3  1 
ATOM   10585 H HE21 . GLN B 1 339 ? 29.674  13.877  81.101  1.00 77.98  ?  348 GLN B HE21 1 
ATOM   10586 H HE22 . GLN B 1 339 ? 29.549  14.841  79.973  1.00 77.98  ?  348 GLN B HE22 1 
ATOM   10587 N N    . ILE B 1 340 ? 23.738  12.890  83.703  1.00 50.25  ?  349 ILE B N    1 
ATOM   10588 C CA   . ILE B 1 340 ? 22.275  12.969  83.828  1.00 50.55  ?  349 ILE B CA   1 
ATOM   10589 C C    . ILE B 1 340 ? 21.827  12.644  85.250  1.00 60.62  ?  349 ILE B C    1 
ATOM   10590 O O    . ILE B 1 340 ? 21.019  13.369  85.848  1.00 62.95  ?  349 ILE B O    1 
ATOM   10591 C CB   . ILE B 1 340 ? 21.629  12.018  82.814  1.00 47.63  ?  349 ILE B CB   1 
ATOM   10592 C CG1  . ILE B 1 340 ? 21.880  12.478  81.389  1.00 105.33 ?  349 ILE B CG1  1 
ATOM   10593 C CG2  . ILE B 1 340 ? 20.184  11.712  83.228  1.00 47.48  ?  349 ILE B CG2  1 
ATOM   10594 C CD1  . ILE B 1 340 ? 21.756  13.934  81.175  1.00 91.47  ?  349 ILE B CD1  1 
ATOM   10595 H H    . ILE B 1 340 ? 24.006  12.296  83.142  1.00 60.30  ?  349 ILE B H    1 
ATOM   10596 H HA   . ILE B 1 340 ? 21.987  13.872  83.620  1.00 60.66  ?  349 ILE B HA   1 
ATOM   10597 H HB   . ILE B 1 340 ? 22.106  11.177  82.901  1.00 57.16  ?  349 ILE B HB   1 
ATOM   10598 H HG12 . ILE B 1 340 ? 22.781  12.221  81.136  1.00 126.40 ?  349 ILE B HG12 1 
ATOM   10599 H HG13 . ILE B 1 340 ? 21.241  12.040  80.806  1.00 126.40 ?  349 ILE B HG13 1 
ATOM   10600 H HG21 . ILE B 1 340 ? 19.790  11.110  82.577  1.00 56.97  ?  349 ILE B HG21 1 
ATOM   10601 H HG22 . ILE B 1 340 ? 20.188  11.295  84.104  1.00 56.97  ?  349 ILE B HG22 1 
ATOM   10602 H HG23 . ILE B 1 340 ? 19.682  12.541  83.257  1.00 56.97  ?  349 ILE B HG23 1 
ATOM   10603 H HD11 . ILE B 1 340 ? 21.933  14.131  80.242  1.00 109.76 ?  349 ILE B HD11 1 
ATOM   10604 H HD12 . ILE B 1 340 ? 20.856  14.211  81.407  1.00 109.76 ?  349 ILE B HD12 1 
ATOM   10605 H HD13 . ILE B 1 340 ? 22.399  14.392  81.738  1.00 109.76 ?  349 ILE B HD13 1 
ATOM   10606 N N    . VAL B 1 341 ? 22.339  11.539  85.801  1.00 48.68  ?  350 VAL B N    1 
ATOM   10607 C CA   . VAL B 1 341 ? 22.045  11.147  87.175  1.00 44.00  ?  350 VAL B CA   1 
ATOM   10608 C C    . VAL B 1 341 ? 22.519  12.187  88.184  1.00 73.57  ?  350 VAL B C    1 
ATOM   10609 O O    . VAL B 1 341 ? 22.004  12.253  89.291  1.00 75.82  ?  350 VAL B O    1 
ATOM   10610 C CB   . VAL B 1 341 ? 22.654  9.739   87.424  1.00 53.76  ?  350 VAL B CB   1 
ATOM   10611 C CG1  . VAL B 1 341 ? 22.588  9.303   88.874  1.00 106.91 ?  350 VAL B CG1  1 
ATOM   10612 C CG2  . VAL B 1 341 ? 21.944  8.763   86.582  1.00 70.10  ?  350 VAL B CG2  1 
ATOM   10613 H H    . VAL B 1 341 ? 22.865  10.996  85.391  1.00 58.42  ?  350 VAL B H    1 
ATOM   10614 H HA   . VAL B 1 341 ? 21.083  11.068  87.272  1.00 52.80  ?  350 VAL B HA   1 
ATOM   10615 H HB   . VAL B 1 341 ? 23.586  9.745   87.155  1.00 64.51  ?  350 VAL B HB   1 
ATOM   10616 H HG11 . VAL B 1 341 ? 22.983  8.421   88.957  1.00 128.29 ?  350 VAL B HG11 1 
ATOM   10617 H HG12 . VAL B 1 341 ? 23.080  9.938   89.418  1.00 128.29 ?  350 VAL B HG12 1 
ATOM   10618 H HG13 . VAL B 1 341 ? 21.659  9.277   89.154  1.00 128.29 ?  350 VAL B HG13 1 
ATOM   10619 H HG21 . VAL B 1 341 ? 22.321  7.882   86.734  1.00 84.12  ?  350 VAL B HG21 1 
ATOM   10620 H HG22 . VAL B 1 341 ? 21.004  8.766   86.820  1.00 84.12  ?  350 VAL B HG22 1 
ATOM   10621 H HG23 . VAL B 1 341 ? 22.051  9.013   85.651  1.00 84.12  ?  350 VAL B HG23 1 
ATOM   10622 N N    . THR B 1 342 ? 23.508  12.998  87.839  1.00 103.71 ?  351 THR B N    1 
ATOM   10623 C CA   . THR B 1 342 ? 23.885  14.101  88.712  1.00 87.80  ?  351 THR B CA   1 
ATOM   10624 C C    . THR B 1 342 ? 22.800  15.167  88.678  1.00 76.61  ?  351 THR B C    1 
ATOM   10625 O O    . THR B 1 342 ? 22.371  15.666  89.725  1.00 58.74  ?  351 THR B O    1 
ATOM   10626 C CB   . THR B 1 342 ? 25.238  14.652  88.276  1.00 77.98  ?  351 THR B CB   1 
ATOM   10627 O OG1  . THR B 1 342 ? 26.170  13.575  88.244  1.00 94.34  ?  351 THR B OG1  1 
ATOM   10628 C CG2  . THR B 1 342 ? 25.755  15.654  89.225  1.00 86.70  ?  351 THR B CG2  1 
ATOM   10629 H H    . THR B 1 342 ? 23.971  12.934  87.117  1.00 124.46 ?  351 THR B H    1 
ATOM   10630 H HA   . THR B 1 342 ? 23.966  13.777  89.623  1.00 105.36 ?  351 THR B HA   1 
ATOM   10631 H HB   . THR B 1 342 ? 25.167  15.056  87.397  1.00 93.57  ?  351 THR B HB   1 
ATOM   10632 H HG1  . THR B 1 342 ? 25.913  12.989  87.700  1.00 113.21 ?  351 THR B HG1  1 
ATOM   10633 H HG21 . THR B 1 342 ? 26.615  15.985  88.922  1.00 104.04 ?  351 THR B HG21 1 
ATOM   10634 H HG22 . THR B 1 342 ? 25.136  16.398  89.291  1.00 104.04 ?  351 THR B HG22 1 
ATOM   10635 H HG23 . THR B 1 342 ? 25.863  15.254  90.103  1.00 104.04 ?  351 THR B HG23 1 
ATOM   10636 N N    . LYS B 1 343 ? 22.338  15.520  87.469  1.00 59.73  ?  352 LYS B N    1 
ATOM   10637 C CA   . LYS B 1 343 ? 21.326  16.566  87.334  1.00 56.05  ?  352 LYS B CA   1 
ATOM   10638 C C    . LYS B 1 343 ? 20.004  16.077  87.887  1.00 77.26  ?  352 LYS B C    1 
ATOM   10639 O O    . LYS B 1 343 ? 19.342  16.795  88.631  1.00 65.15  ?  352 LYS B O    1 
ATOM   10640 C CB   . LYS B 1 343 ? 21.190  16.985  85.863  1.00 78.73  ?  352 LYS B CB   1 
ATOM   10641 C CG   . LYS B 1 343 ? 20.274  18.151  85.555  1.00 118.95 ?  352 LYS B CG   1 
ATOM   10642 H H    . LYS B 1 343 ? 22.592  15.172  86.725  1.00 71.68  ?  352 LYS B H    1 
ATOM   10643 H HA   . LYS B 1 343 ? 21.600  17.343  87.846  1.00 67.26  ?  352 LYS B HA   1 
ATOM   10644 H HB2  . LYS B 1 343 ? 22.072  17.221  85.535  1.00 94.48  ?  352 LYS B HB2  1 
ATOM   10645 H HB3  . LYS B 1 343 ? 20.858  16.223  85.363  1.00 94.48  ?  352 LYS B HB3  1 
ATOM   10646 H HG2  . LYS B 1 343 ? 19.355  17.878  85.701  1.00 142.73 ?  352 LYS B HG2  1 
ATOM   10647 H HG3  . LYS B 1 343 ? 20.497  18.891  86.141  1.00 142.73 ?  352 LYS B HG3  1 
ATOM   10648 N N    . TYR B 1 344 ? 19.656  14.814  87.645  1.00 108.54 ?  353 TYR B N    1 
ATOM   10649 C CA   . TYR B 1 344 ? 18.293  14.381  87.897  1.00 56.55  ?  353 TYR B CA   1 
ATOM   10650 C C    . TYR B 1 344 ? 18.110  13.564  89.173  1.00 52.79  ?  353 TYR B C    1 
ATOM   10651 O O    . TYR B 1 344 ? 16.954  13.348  89.576  1.00 64.91  ?  353 TYR B O    1 
ATOM   10652 C CB   . TYR B 1 344 ? 17.756  13.599  86.685  1.00 47.38  ?  353 TYR B CB   1 
ATOM   10653 C CG   . TYR B 1 344 ? 17.572  14.506  85.498  1.00 68.41  ?  353 TYR B CG   1 
ATOM   10654 C CD1  . TYR B 1 344 ? 16.494  15.364  85.423  1.00 96.86  ?  353 TYR B CD1  1 
ATOM   10655 C CD2  . TYR B 1 344 ? 18.486  14.531  84.464  1.00 59.65  ?  353 TYR B CD2  1 
ATOM   10656 C CE1  . TYR B 1 344 ? 16.336  16.227  84.345  1.00 102.22 ?  353 TYR B CE1  1 
ATOM   10657 C CE2  . TYR B 1 344 ? 18.334  15.392  83.384  1.00 104.41 ?  353 TYR B CE2  1 
ATOM   10658 C CZ   . TYR B 1 344 ? 17.253  16.228  83.332  1.00 87.32  ?  353 TYR B CZ   1 
ATOM   10659 O OH   . TYR B 1 344 ? 17.079  17.070  82.268  1.00 102.41 ?  353 TYR B OH   1 
ATOM   10660 H H    . TYR B 1 344 ? 20.181  14.203  87.341  1.00 130.25 ?  353 TYR B H    1 
ATOM   10661 H HA   . TYR B 1 344 ? 17.742  15.174  87.989  1.00 67.86  ?  353 TYR B HA   1 
ATOM   10662 H HB2  . TYR B 1 344 ? 18.388  12.904  86.444  1.00 56.86  ?  353 TYR B HB2  1 
ATOM   10663 H HB3  . TYR B 1 344 ? 16.895  13.210  86.908  1.00 56.86  ?  353 TYR B HB3  1 
ATOM   10664 H HD1  . TYR B 1 344 ? 15.868  15.373  86.110  1.00 116.24 ?  353 TYR B HD1  1 
ATOM   10665 H HD2  . TYR B 1 344 ? 19.225  13.968  84.496  1.00 71.58  ?  353 TYR B HD2  1 
ATOM   10666 H HE1  . TYR B 1 344 ? 15.600  16.794  84.307  1.00 122.66 ?  353 TYR B HE1  1 
ATOM   10667 H HE2  . TYR B 1 344 ? 18.956  15.390  82.693  1.00 125.29 ?  353 TYR B HE2  1 
ATOM   10668 H HH   . TYR B 1 344 ? 16.376  17.520  82.369  1.00 122.89 ?  353 TYR B HH   1 
ATOM   10669 N N    . ILE B 1 345 ? 19.178  13.163  89.872  1.00 61.35  ?  354 ILE B N    1 
ATOM   10670 C CA   . ILE B 1 345 ? 18.972  12.460  91.153  1.00 70.08  ?  354 ILE B CA   1 
ATOM   10671 C C    . ILE B 1 345 ? 19.844  13.135  92.204  1.00 62.12  ?  354 ILE B C    1 
ATOM   10672 O O    . ILE B 1 345 ? 19.342  13.587  93.237  1.00 71.59  ?  354 ILE B O    1 
ATOM   10673 C CB   . ILE B 1 345 ? 19.219  10.918  91.099  1.00 89.71  ?  354 ILE B CB   1 
ATOM   10674 C CG1  . ILE B 1 345 ? 18.171  10.191  90.257  1.00 81.58  ?  354 ILE B CG1  1 
ATOM   10675 C CG2  . ILE B 1 345 ? 19.141  10.238  92.470  1.00 94.37  ?  354 ILE B CG2  1 
ATOM   10676 C CD1  . ILE B 1 345 ? 18.433  8.637   90.048  1.00 98.69  ?  354 ILE B CD1  1 
ATOM   10677 H H    . ILE B 1 345 ? 19.998  13.277  89.643  1.00 73.61  ?  354 ILE B H    1 
ATOM   10678 H HA   . ILE B 1 345 ? 18.049  12.590  91.422  1.00 84.10  ?  354 ILE B HA   1 
ATOM   10679 H HB   . ILE B 1 345 ? 20.096  10.755  90.718  1.00 107.66 ?  354 ILE B HB   1 
ATOM   10680 H HG12 . ILE B 1 345 ? 17.308  10.287  90.689  1.00 97.90  ?  354 ILE B HG12 1 
ATOM   10681 H HG13 . ILE B 1 345 ? 18.142  10.603  89.379  1.00 97.90  ?  354 ILE B HG13 1 
ATOM   10682 H HG21 . ILE B 1 345 ? 19.303  9.288   92.361  1.00 113.25 ?  354 ILE B HG21 1 
ATOM   10683 H HG22 . ILE B 1 345 ? 19.814  10.624  93.052  1.00 113.25 ?  354 ILE B HG22 1 
ATOM   10684 H HG23 . ILE B 1 345 ? 18.258  10.383  92.844  1.00 113.25 ?  354 ILE B HG23 1 
ATOM   10685 H HD11 . ILE B 1 345 ? 17.719  8.268   89.505  1.00 118.42 ?  354 ILE B HD11 1 
ATOM   10686 H HD12 . ILE B 1 345 ? 19.285  8.518   89.601  1.00 118.42 ?  354 ILE B HD12 1 
ATOM   10687 H HD13 . ILE B 1 345 ? 18.449  8.201   90.914  1.00 118.42 ?  354 ILE B HD13 1 
ATOM   10688 N N    . LEU B 1 346 ? 21.148  13.228  91.971  1.00 99.48  ?  355 LEU B N    1 
ATOM   10689 C CA   . LEU B 1 346 ? 22.016  13.561  93.091  1.00 82.16  ?  355 LEU B CA   1 
ATOM   10690 C C    . LEU B 1 346 ? 21.808  14.994  93.563  1.00 77.55  ?  355 LEU B C    1 
ATOM   10691 O O    . LEU B 1 346 ? 21.746  15.244  94.771  1.00 68.60  ?  355 LEU B O    1 
ATOM   10692 C CB   . LEU B 1 346 ? 23.472  13.306  92.716  1.00 102.53 ?  355 LEU B CB   1 
ATOM   10693 C CG   . LEU B 1 346 ? 24.353  13.222  93.949  1.00 132.45 ?  355 LEU B CG   1 
ATOM   10694 C CD1  . LEU B 1 346 ? 25.097  11.908  93.991  1.00 162.44 ?  355 LEU B CD1  1 
ATOM   10695 C CD2  . LEU B 1 346 ? 25.299  14.388  93.952  1.00 136.36 ?  355 LEU B CD2  1 
ATOM   10696 H H    . LEU B 1 346 ? 21.538  13.110  91.215  1.00 119.38 ?  355 LEU B H    1 
ATOM   10697 H HA   . LEU B 1 346 ? 21.800  12.976  93.833  1.00 98.60  ?  355 LEU B HA   1 
ATOM   10698 H HB2  . LEU B 1 346 ? 23.537  12.465  92.238  1.00 123.03 ?  355 LEU B HB2  1 
ATOM   10699 H HB3  . LEU B 1 346 ? 23.792  14.035  92.162  1.00 123.03 ?  355 LEU B HB3  1 
ATOM   10700 H HG   . LEU B 1 346 ? 23.798  13.282  94.742  1.00 158.95 ?  355 LEU B HG   1 
ATOM   10701 H HD11 . LEU B 1 346 ? 25.650  11.884  94.788  1.00 194.93 ?  355 LEU B HD11 1 
ATOM   10702 H HD12 . LEU B 1 346 ? 24.453  11.183  94.013  1.00 194.93 ?  355 LEU B HD12 1 
ATOM   10703 H HD13 . LEU B 1 346 ? 25.652  11.835  93.200  1.00 194.93 ?  355 LEU B HD13 1 
ATOM   10704 H HD21 . LEU B 1 346 ? 25.863  14.335  94.740  1.00 163.63 ?  355 LEU B HD21 1 
ATOM   10705 H HD22 . LEU B 1 346 ? 25.845  14.353  93.151  1.00 163.63 ?  355 LEU B HD22 1 
ATOM   10706 H HD23 . LEU B 1 346 ? 24.785  15.211  93.967  1.00 163.63 ?  355 LEU B HD23 1 
ATOM   10707 N N    . ILE B 1 347 ? 21.633  15.940  92.650  1.00 67.87  ?  356 ILE B N    1 
ATOM   10708 C CA   . ILE B 1 347 ? 21.504  17.324  93.079  1.00 86.92  ?  356 ILE B CA   1 
ATOM   10709 C C    . ILE B 1 347 ? 20.130  17.462  93.710  1.00 84.62  ?  356 ILE B C    1 
ATOM   10710 O O    . ILE B 1 347 ? 20.038  17.825  94.891  1.00 86.24  ?  356 ILE B O    1 
ATOM   10711 C CB   . ILE B 1 347 ? 21.789  18.283  91.916  1.00 73.02  ?  356 ILE B CB   1 
ATOM   10712 C CG1  . ILE B 1 347 ? 23.321  18.306  91.731  1.00 73.59  ?  356 ILE B CG1  1 
ATOM   10713 C CG2  . ILE B 1 347 ? 21.227  19.714  92.172  1.00 76.90  ?  356 ILE B CG2  1 
ATOM   10714 C CD1  . ILE B 1 347 ? 23.886  18.988  90.391  1.00 81.72  ?  356 ILE B CD1  1 
ATOM   10715 H H    . ILE B 1 347 ? 21.586  15.813  91.801  1.00 81.44  ?  356 ILE B H    1 
ATOM   10716 H HA   . ILE B 1 347 ? 22.163  17.498  93.770  1.00 104.30 ?  356 ILE B HA   1 
ATOM   10717 H HB   . ILE B 1 347 ? 21.382  17.927  91.111  1.00 87.62  ?  356 ILE B HB   1 
ATOM   10718 H HG12 . ILE B 1 347 ? 23.707  18.786  92.480  1.00 88.31  ?  356 ILE B HG12 1 
ATOM   10719 H HG13 . ILE B 1 347 ? 23.639  17.390  91.741  1.00 88.31  ?  356 ILE B HG13 1 
ATOM   10720 H HG21 . ILE B 1 347 ? 21.434  20.275  91.408  1.00 92.28  ?  356 ILE B HG21 1 
ATOM   10721 H HG22 . ILE B 1 347 ? 20.265  19.658  92.291  1.00 92.28  ?  356 ILE B HG22 1 
ATOM   10722 H HG23 . ILE B 1 347 ? 21.639  20.076  92.971  1.00 92.28  ?  356 ILE B HG23 1 
ATOM   10723 H HD11 . ILE B 1 347 ? 24.855  18.938  90.396  1.00 98.07  ?  356 ILE B HD11 1 
ATOM   10724 H HD12 . ILE B 1 347 ? 23.534  18.512  89.622  1.00 98.07  ?  356 ILE B HD12 1 
ATOM   10725 H HD13 . ILE B 1 347 ? 23.603  19.915  90.365  1.00 98.07  ?  356 ILE B HD13 1 
ATOM   10726 N N    . PRO B 1 348 ? 19.052  17.111  93.004  1.00 101.33 ?  357 PRO B N    1 
ATOM   10727 C CA   . PRO B 1 348 ? 17.735  17.142  93.648  1.00 136.98 ?  357 PRO B CA   1 
ATOM   10728 C C    . PRO B 1 348 ? 17.688  16.454  94.997  1.00 108.13 ?  357 PRO B C    1 
ATOM   10729 O O    . PRO B 1 348 ? 17.024  16.950  95.912  1.00 137.21 ?  357 PRO B O    1 
ATOM   10730 C CB   . PRO B 1 348 ? 16.847  16.425  92.632  1.00 69.68  ?  357 PRO B CB   1 
ATOM   10731 C CG   . PRO B 1 348 ? 17.445  16.650  91.326  1.00 84.71  ?  357 PRO B CG   1 
ATOM   10732 C CD   . PRO B 1 348 ? 18.935  16.766  91.568  1.00 103.45 ?  357 PRO B CD   1 
ATOM   10733 H HA   . PRO B 1 348 ? 17.431  18.058  93.746  1.00 164.38 ?  357 PRO B HA   1 
ATOM   10734 H HB2  . PRO B 1 348 ? 16.824  15.477  92.835  1.00 83.61  ?  357 PRO B HB2  1 
ATOM   10735 H HB3  . PRO B 1 348 ? 15.952  16.800  92.664  1.00 83.61  ?  357 PRO B HB3  1 
ATOM   10736 H HG2  . PRO B 1 348 ? 17.251  15.898  90.746  1.00 101.65 ?  357 PRO B HG2  1 
ATOM   10737 H HG3  . PRO B 1 348 ? 17.096  17.472  90.947  1.00 101.65 ?  357 PRO B HG3  1 
ATOM   10738 H HD2  . PRO B 1 348 ? 19.370  15.917  91.392  1.00 124.14 ?  357 PRO B HD2  1 
ATOM   10739 H HD3  . PRO B 1 348 ? 19.310  17.474  91.022  1.00 124.14 ?  357 PRO B HD3  1 
ATOM   10740 N N    . ALA B 1 349 ? 18.361  15.318  95.157  1.00 134.43 ?  358 ALA B N    1 
ATOM   10741 C CA   . ALA B 1 349 ? 18.304  14.632  96.439  1.00 81.88  ?  358 ALA B CA   1 
ATOM   10742 C C    . ALA B 1 349 ? 18.920  15.469  97.547  1.00 99.62  ?  358 ALA B C    1 
ATOM   10743 O O    . ALA B 1 349 ? 18.521  15.361  98.711  1.00 74.21  ?  358 ALA B O    1 
ATOM   10744 C CB   . ALA B 1 349 ? 19.010  13.294  96.346  1.00 88.84  ?  358 ALA B CB   1 
ATOM   10745 H H    . ALA B 1 349 ? 18.845  14.935  94.558  1.00 161.32 ?  358 ALA B H    1 
ATOM   10746 H HA   . ALA B 1 349 ? 17.375  14.467  96.668  1.00 98.25  ?  358 ALA B HA   1 
ATOM   10747 H HB1  . ALA B 1 349 ? 18.961  12.852  97.208  1.00 106.60 ?  358 ALA B HB1  1 
ATOM   10748 H HB2  . ALA B 1 349 ? 18.572  12.753  95.670  1.00 106.60 ?  358 ALA B HB2  1 
ATOM   10749 H HB3  . ALA B 1 349 ? 19.937  13.443  96.102  1.00 106.60 ?  358 ALA B HB3  1 
ATOM   10750 N N    . SER B 1 350 ? 19.871  16.327  97.218  1.00 134.55 ?  359 SER B N    1 
ATOM   10751 C CA   . SER B 1 350 ? 20.428  17.159  98.271  1.00 122.21 ?  359 SER B CA   1 
ATOM   10752 C C    . SER B 1 350 ? 19.512  18.302  98.663  1.00 101.95 ?  359 SER B C    1 
ATOM   10753 O O    . SER B 1 350 ? 19.698  18.857  99.750  1.00 83.43  ?  359 SER B O    1 
ATOM   10754 C CB   . SER B 1 350 ? 21.766  17.715  97.816  1.00 117.67 ?  359 SER B CB   1 
ATOM   10755 O OG   . SER B 1 350 ? 21.554  18.766  96.891  1.00 108.73 ?  359 SER B OG   1 
ATOM   10756 H H    . SER B 1 350 ? 20.199  16.446  96.432  1.00 161.46 ?  359 SER B H    1 
ATOM   10757 H HA   . SER B 1 350 ? 20.581  16.613  99.058  1.00 146.65 ?  359 SER B HA   1 
ATOM   10758 H HB2  . SER B 1 350 ? 22.248  18.058  98.584  1.00 141.20 ?  359 SER B HB2  1 
ATOM   10759 H HB3  . SER B 1 350 ? 22.277  17.010  97.387  1.00 141.20 ?  359 SER B HB3  1 
ATOM   10760 H HG   . SER B 1 350 ? 21.132  18.480  96.223  1.00 130.48 ?  359 SER B HG   1 
ATOM   10761 N N    . GLN B 1 351 ? 18.478  18.580  97.858  1.00 129.56 ?  360 GLN B N    1 
ATOM   10762 C CA   . GLN B 1 351 ? 17.531  19.677  98.052  1.00 116.85 ?  360 GLN B CA   1 
ATOM   10763 C C    . GLN B 1 351 ? 16.180  19.201  98.609  1.00 116.95 ?  360 GLN B C    1 
ATOM   10764 O O    . GLN B 1 351 ? 15.148  19.805  98.316  1.00 128.17 ?  360 GLN B O    1 
ATOM   10765 C CB   . GLN B 1 351 ? 17.345  20.435  96.727  1.00 123.65 ?  360 GLN B CB   1 
ATOM   10766 C CG   . GLN B 1 351 ? 18.602  21.163  96.256  1.00 115.45 ?  360 GLN B CG   1 
ATOM   10767 C CD   . GLN B 1 351 ? 18.484  21.823  94.882  1.00 122.88 ?  360 GLN B CD   1 
ATOM   10768 O OE1  . GLN B 1 351 ? 19.102  22.856  94.634  1.00 134.40 ?  360 GLN B OE1  1 
ATOM   10769 N NE2  . GLN B 1 351 ? 17.714  21.231  93.988  1.00 175.77 ?  360 GLN B NE2  1 
ATOM   10770 H H    . GLN B 1 351 ? 18.302  18.118  97.155  1.00 155.47 ?  360 GLN B H    1 
ATOM   10771 H HA   . GLN B 1 351 ? 17.907  20.299  98.694  1.00 140.22 ?  360 GLN B HA   1 
ATOM   10772 H HB2  . GLN B 1 351 ? 17.092  19.802  96.037  1.00 148.38 ?  360 GLN B HB2  1 
ATOM   10773 H HB3  . GLN B 1 351 ? 16.644  21.096  96.841  1.00 148.38 ?  360 GLN B HB3  1 
ATOM   10774 H HG2  . GLN B 1 351 ? 18.816  21.858  96.898  1.00 138.54 ?  360 GLN B HG2  1 
ATOM   10775 H HG3  . GLN B 1 351 ? 19.331  20.524  96.213  1.00 138.54 ?  360 GLN B HG3  1 
ATOM   10776 H HE21 . GLN B 1 351 ? 17.303  20.503  94.189  1.00 210.93 ?  360 GLN B HE21 1 
ATOM   10777 H HE22 . GLN B 1 351 ? 17.623  21.574  93.204  1.00 210.93 ?  360 GLN B HE22 1 
ATOM   10778 N N    . GLN B 1 352 ? 16.156  18.097  99.359  1.00 123.54 ?  361 GLN B N    1 
ATOM   10779 C CA   . GLN B 1 352 ? 14.924  17.579  99.971  1.00 110.10 ?  361 GLN B CA   1 
ATOM   10780 C C    . GLN B 1 352 ? 14.743  18.140  101.388 1.00 116.43 ?  361 GLN B C    1 
ATOM   10781 O O    . GLN B 1 352 ? 13.667  18.052  101.994 1.00 118.54 ?  361 GLN B O    1 
ATOM   10782 C CB   . GLN B 1 352 ? 14.941  16.049  99.999  1.00 119.83 ?  361 GLN B CB   1 
ATOM   10783 H H    . GLN B 1 352 ? 16.851  17.621  99.533  1.00 148.25 ?  361 GLN B H    1 
ATOM   10784 H HA   . GLN B 1 352 ? 14.164  17.861  99.437  1.00 132.12 ?  361 GLN B HA   1 
ATOM   10785 N N    . GLY B 1 372 ? 19.011  7.749   96.089  1.00 162.22 ?  381 GLY B N    1 
ATOM   10786 C CA   . GLY B 1 372 ? 19.456  6.997   94.928  1.00 182.10 ?  381 GLY B CA   1 
ATOM   10787 C C    . GLY B 1 372 ? 20.966  7.058   94.735  1.00 143.20 ?  381 GLY B C    1 
ATOM   10788 O O    . GLY B 1 372 ? 21.496  7.445   93.684  1.00 128.11 ?  381 GLY B O    1 
ATOM   10789 H H    . GLY B 1 372 ? 19.194  8.588   96.053  1.00 194.67 ?  381 GLY B H    1 
ATOM   10790 H HA2  . GLY B 1 372 ? 19.196  6.068   95.027  1.00 218.52 ?  381 GLY B HA2  1 
ATOM   10791 H HA3  . GLY B 1 372 ? 19.030  7.352   94.132  1.00 218.52 ?  381 GLY B HA3  1 
ATOM   10792 N N    . THR B 1 373 ? 21.684  6.661   95.766  1.00 133.67 ?  382 THR B N    1 
ATOM   10793 C CA   . THR B 1 373 ? 23.127  6.800   95.705  1.00 124.48 ?  382 THR B CA   1 
ATOM   10794 C C    . THR B 1 373 ? 23.831  5.551   95.191  1.00 133.68 ?  382 THR B C    1 
ATOM   10795 O O    . THR B 1 373 ? 24.864  5.657   94.509  1.00 113.15 ?  382 THR B O    1 
ATOM   10796 C CB   . THR B 1 373 ? 23.643  7.136   97.103  1.00 111.01 ?  382 THR B CB   1 
ATOM   10797 O OG1  . THR B 1 373 ? 22.691  7.987   97.770  1.00 137.53 ?  382 THR B OG1  1 
ATOM   10798 C CG2  . THR B 1 373 ? 24.972  7.800   96.988  1.00 80.11  ?  382 THR B CG2  1 
ATOM   10799 H H    . THR B 1 373 ? 21.375  6.318   96.492  1.00 160.40 ?  382 THR B H    1 
ATOM   10800 H HA   . THR B 1 373 ? 23.350  7.536   95.114  1.00 149.38 ?  382 THR B HA   1 
ATOM   10801 H HB   . THR B 1 373 ? 23.754  6.317   97.610  1.00 133.21 ?  382 THR B HB   1 
ATOM   10802 H HG1  . THR B 1 373 ? 22.966  8.178   98.540  1.00 165.03 ?  382 THR B HG1  1 
ATOM   10803 H HG21 . THR B 1 373 ? 25.310  8.018   97.871  1.00 96.14  ?  382 THR B HG21 1 
ATOM   10804 H HG22 . THR B 1 373 ? 25.601  7.207   96.548  1.00 96.14  ?  382 THR B HG22 1 
ATOM   10805 H HG23 . THR B 1 373 ? 24.891  8.616   96.470  1.00 96.14  ?  382 THR B HG23 1 
ATOM   10806 N N    . ASP B 1 374 ? 23.268  4.377   95.486  1.00 122.37 ?  383 ASP B N    1 
ATOM   10807 C CA   . ASP B 1 374 ? 23.861  3.119   95.064  1.00 91.93  ?  383 ASP B CA   1 
ATOM   10808 C C    . ASP B 1 374 ? 23.928  3.028   93.557  1.00 77.55  ?  383 ASP B C    1 
ATOM   10809 O O    . ASP B 1 374 ? 24.820  2.366   93.022  1.00 79.32  ?  383 ASP B O    1 
ATOM   10810 C CB   . ASP B 1 374 ? 23.054  1.962   95.649  1.00 84.43  ?  383 ASP B CB   1 
ATOM   10811 C CG   . ASP B 1 374 ? 22.978  2.006   97.164  1.00 106.59 ?  383 ASP B CG   1 
ATOM   10812 H H    . ASP B 1 374 ? 22.537  4.287   95.931  1.00 146.84 ?  383 ASP B H    1 
ATOM   10813 H HA   . ASP B 1 374 ? 24.766  3.062   95.410  1.00 110.31 ?  383 ASP B HA   1 
ATOM   10814 H HB2  . ASP B 1 374 ? 22.149  2.000   95.302  1.00 101.32 ?  383 ASP B HB2  1 
ATOM   10815 H HB3  . ASP B 1 374 ? 23.472  1.124   95.395  1.00 101.32 ?  383 ASP B HB3  1 
ATOM   10816 N N    . LEU B 1 375 ? 23.027  3.737   92.868  1.00 94.80  ?  384 LEU B N    1 
ATOM   10817 C CA   . LEU B 1 375 ? 23.003  3.771   91.407  1.00 83.25  ?  384 LEU B CA   1 
ATOM   10818 C C    . LEU B 1 375 ? 24.250  4.435   90.868  1.00 100.40 ?  384 LEU B C    1 
ATOM   10819 O O    . LEU B 1 375 ? 24.786  4.037   89.829  1.00 93.13  ?  384 LEU B O    1 
ATOM   10820 C CB   . LEU B 1 375 ? 21.774  4.554   90.948  1.00 67.69  ?  384 LEU B CB   1 
ATOM   10821 C CG   . LEU B 1 375 ? 21.653  4.927   89.468  1.00 60.33  ?  384 LEU B CG   1 
ATOM   10822 C CD1  . LEU B 1 375 ? 21.688  3.674   88.613  1.00 58.54  ?  384 LEU B CD1  1 
ATOM   10823 C CD2  . LEU B 1 375 ? 20.375  5.751   89.198  1.00 70.01  ?  384 LEU B CD2  1 
ATOM   10824 H H    . LEU B 1 375 ? 22.411  4.214   93.233  1.00 113.76 ?  384 LEU B H    1 
ATOM   10825 H HA   . LEU B 1 375 ? 22.951  2.868   91.056  1.00 99.90  ?  384 LEU B HA   1 
ATOM   10826 H HB2  . LEU B 1 375 ? 20.990  4.028   91.170  1.00 81.22  ?  384 LEU B HB2  1 
ATOM   10827 H HB3  . LEU B 1 375 ? 21.749  5.384   91.449  1.00 81.22  ?  384 LEU B HB3  1 
ATOM   10828 H HG   . LEU B 1 375 ? 22.415  5.475   89.221  1.00 72.39  ?  384 LEU B HG   1 
ATOM   10829 H HD11 . LEU B 1 375 ? 21.611  3.927   87.680  1.00 70.25  ?  384 LEU B HD11 1 
ATOM   10830 H HD12 . LEU B 1 375 ? 22.529  3.214   88.763  1.00 70.25  ?  384 LEU B HD12 1 
ATOM   10831 H HD13 . LEU B 1 375 ? 20.947  3.101   88.864  1.00 70.25  ?  384 LEU B HD13 1 
ATOM   10832 H HD21 . LEU B 1 375 ? 20.333  5.968   88.254  1.00 84.01  ?  384 LEU B HD21 1 
ATOM   10833 H HD22 . LEU B 1 375 ? 19.601  5.225   89.452  1.00 84.01  ?  384 LEU B HD22 1 
ATOM   10834 H HD23 . LEU B 1 375 ? 20.409  6.566   89.724  1.00 84.01  ?  384 LEU B HD23 1 
ATOM   10835 N N    . MET B 1 376 ? 24.702  5.479   91.551  1.00 83.68  ?  385 MET B N    1 
ATOM   10836 C CA   . MET B 1 376 ? 25.863  6.187   91.076  1.00 100.17 ?  385 MET B CA   1 
ATOM   10837 C C    . MET B 1 376 ? 27.057  5.277   91.089  1.00 126.00 ?  385 MET B C    1 
ATOM   10838 O O    . MET B 1 376 ? 27.815  5.216   90.117  1.00 124.71 ?  385 MET B O    1 
ATOM   10839 C CB   . MET B 1 376 ? 26.108  7.404   91.947  1.00 135.71 ?  385 MET B CB   1 
ATOM   10840 C CG   . MET B 1 376 ? 25.312  8.601   91.522  1.00 151.67 ?  385 MET B CG   1 
ATOM   10841 S SD   . MET B 1 376 ? 25.987  9.364   90.033  1.00 124.11 ?  385 MET B SD   1 
ATOM   10842 C CE   . MET B 1 376 ? 25.615  11.086  90.308  1.00 130.12 ?  385 MET B CE   1 
ATOM   10843 H H    . MET B 1 376 ? 24.358  5.787   92.277  1.00 100.41 ?  385 MET B H    1 
ATOM   10844 H HA   . MET B 1 376 ? 25.702  6.491   90.169  1.00 120.21 ?  385 MET B HA   1 
ATOM   10845 H HB2  . MET B 1 376 ? 25.864  7.192   92.861  1.00 162.86 ?  385 MET B HB2  1 
ATOM   10846 H HB3  . MET B 1 376 ? 27.048  7.639   91.902  1.00 162.86 ?  385 MET B HB3  1 
ATOM   10847 H HG2  . MET B 1 376 ? 24.400  8.327   91.336  1.00 182.01 ?  385 MET B HG2  1 
ATOM   10848 H HG3  . MET B 1 376 ? 25.325  9.261   92.233  1.00 182.01 ?  385 MET B HG3  1 
ATOM   10849 H HE1  . MET B 1 376 ? 25.939  11.603  89.554  1.00 156.14 ?  385 MET B HE1  1 
ATOM   10850 H HE2  . MET B 1 376 ? 24.654  11.191  90.393  1.00 156.14 ?  385 MET B HE2  1 
ATOM   10851 H HE3  . MET B 1 376 ? 26.053  11.377  91.122  1.00 156.14 ?  385 MET B HE3  1 
ATOM   10852 N N    . ASN B 1 377 ? 27.229  4.535   92.172  1.00 112.04 ?  386 ASN B N    1 
ATOM   10853 C CA   . ASN B 1 377 ? 28.351  3.621   92.212  1.00 75.73  ?  386 ASN B CA   1 
ATOM   10854 C C    . ASN B 1 377 ? 28.227  2.627   91.082  1.00 77.92  ?  386 ASN B C    1 
ATOM   10855 O O    . ASN B 1 377 ? 29.134  2.462   90.271  1.00 72.65  ?  386 ASN B O    1 
ATOM   10856 C CB   . ASN B 1 377 ? 28.428  2.905   93.558  1.00 69.05  ?  386 ASN B CB   1 
ATOM   10857 C CG   . ASN B 1 377 ? 28.532  3.852   94.711  1.00 69.70  ?  386 ASN B CG   1 
ATOM   10858 O OD1  . ASN B 1 377 ? 27.998  3.597   95.784  1.00 84.58  ?  386 ASN B OD1  1 
ATOM   10859 N ND2  . ASN B 1 377 ? 29.170  4.988   94.477  1.00 108.62 ?  386 ASN B ND2  1 
ATOM   10860 H H    . ASN B 1 377 ? 26.730  4.541   92.872  1.00 134.45 ?  386 ASN B H    1 
ATOM   10861 H HA   . ASN B 1 377 ? 29.174  4.120   92.087  1.00 90.87  ?  386 ASN B HA   1 
ATOM   10862 H HB2  . ASN B 1 377 ? 27.626  2.373   93.679  1.00 82.86  ?  386 ASN B HB2  1 
ATOM   10863 H HB3  . ASN B 1 377 ? 29.211  2.333   93.568  1.00 82.86  ?  386 ASN B HB3  1 
ATOM   10864 H HD21 . ASN B 1 377 ? 29.259  5.568   95.106  1.00 130.35 ?  386 ASN B HD21 1 
ATOM   10865 H HD22 . ASN B 1 377 ? 29.496  5.146   93.697  1.00 130.35 ?  386 ASN B HD22 1 
ATOM   10866 N N    . PHE B 1 378 ? 27.062  2.034   90.945  1.00 119.87 ?  387 PHE B N    1 
ATOM   10867 C CA   . PHE B 1 378 ? 26.918  1.024   89.924  1.00 101.83 ?  387 PHE B CA   1 
ATOM   10868 C C    . PHE B 1 378 ? 27.422  1.516   88.568  1.00 80.03  ?  387 PHE B C    1 
ATOM   10869 O O    . PHE B 1 378 ? 28.155  0.811   87.870  1.00 85.35  ?  387 PHE B O    1 
ATOM   10870 C CB   . PHE B 1 378 ? 25.467  0.603   89.842  1.00 91.11  ?  387 PHE B CB   1 
ATOM   10871 C CG   . PHE B 1 378 ? 25.192  -0.195  88.662  1.00 68.05  ?  387 PHE B CG   1 
ATOM   10872 C CD1  . PHE B 1 378 ? 25.716  -1.457  88.543  1.00 65.75  ?  387 PHE B CD1  1 
ATOM   10873 C CD2  . PHE B 1 378 ? 24.504  0.332   87.622  1.00 58.75  ?  387 PHE B CD2  1 
ATOM   10874 C CE1  . PHE B 1 378 ? 25.497  -2.202  87.408  1.00 94.81  ?  387 PHE B CE1  1 
ATOM   10875 C CE2  . PHE B 1 378 ? 24.263  -0.415  86.485  1.00 48.94  ?  387 PHE B CE2  1 
ATOM   10876 C CZ   . PHE B 1 378 ? 24.765  -1.674  86.375  1.00 65.51  ?  387 PHE B CZ   1 
ATOM   10877 H H    . PHE B 1 378 ? 26.359  2.191   91.415  1.00 143.84 ?  387 PHE B H    1 
ATOM   10878 H HA   . PHE B 1 378 ? 27.442  0.246   90.174  1.00 122.20 ?  387 PHE B HA   1 
ATOM   10879 H HB2  . PHE B 1 378 ? 25.246  0.072   90.623  1.00 109.34 ?  387 PHE B HB2  1 
ATOM   10880 H HB3  . PHE B 1 378 ? 24.908  1.395   89.808  1.00 109.34 ?  387 PHE B HB3  1 
ATOM   10881 H HD1  . PHE B 1 378 ? 26.210  -1.819  89.243  1.00 78.90  ?  387 PHE B HD1  1 
ATOM   10882 H HD2  . PHE B 1 378 ? 24.153  1.191   87.691  1.00 70.50  ?  387 PHE B HD2  1 
ATOM   10883 H HE1  . PHE B 1 378 ? 25.838  -3.065  87.345  1.00 113.77 ?  387 PHE B HE1  1 
ATOM   10884 H HE2  . PHE B 1 378 ? 23.773  -0.049  85.785  1.00 58.73  ?  387 PHE B HE2  1 
ATOM   10885 H HZ   . PHE B 1 378 ? 24.610  -2.176  85.607  1.00 78.61  ?  387 PHE B HZ   1 
ATOM   10886 N N    . LEU B 1 379 ? 27.065  2.731   88.178  1.00 100.97 ?  388 LEU B N    1 
ATOM   10887 C CA   . LEU B 1 379 ? 27.415  3.150   86.826  1.00 72.83  ?  388 LEU B CA   1 
ATOM   10888 C C    . LEU B 1 379 ? 28.912  3.399   86.693  1.00 76.68  ?  388 LEU B C    1 
ATOM   10889 O O    . LEU B 1 379 ? 29.494  3.121   85.638  1.00 90.18  ?  388 LEU B O    1 
ATOM   10890 C CB   . LEU B 1 379 ? 26.605  4.382   86.463  1.00 66.02  ?  388 LEU B CB   1 
ATOM   10891 C CG   . LEU B 1 379 ? 25.119  4.056   86.324  1.00 73.62  ?  388 LEU B CG   1 
ATOM   10892 C CD1  . LEU B 1 379 ? 24.311  5.295   86.671  1.00 114.29 ?  388 LEU B CD1  1 
ATOM   10893 C CD2  . LEU B 1 379 ? 24.777  3.620   84.945  1.00 53.92  ?  388 LEU B CD2  1 
ATOM   10894 H H    . LEU B 1 379 ? 26.639  3.310   88.650  1.00 121.16 ?  388 LEU B H    1 
ATOM   10895 H HA   . LEU B 1 379 ? 27.175  2.444   86.207  1.00 87.39  ?  388 LEU B HA   1 
ATOM   10896 H HB2  . LEU B 1 379 ? 26.706  5.048   87.161  1.00 79.22  ?  388 LEU B HB2  1 
ATOM   10897 H HB3  . LEU B 1 379 ? 26.920  4.733   85.616  1.00 79.22  ?  388 LEU B HB3  1 
ATOM   10898 H HG   . LEU B 1 379 ? 24.880  3.347   86.942  1.00 88.35  ?  388 LEU B HG   1 
ATOM   10899 H HD11 . LEU B 1 379 ? 23.367  5.091   86.583  1.00 137.15 ?  388 LEU B HD11 1 
ATOM   10900 H HD12 . LEU B 1 379 ? 24.510  5.555   87.584  1.00 137.15 ?  388 LEU B HD12 1 
ATOM   10901 H HD13 . LEU B 1 379 ? 24.554  6.010   86.062  1.00 137.15 ?  388 LEU B HD13 1 
ATOM   10902 H HD21 . LEU B 1 379 ? 23.828  3.425   84.902  1.00 64.70  ?  388 LEU B HD21 1 
ATOM   10903 H HD22 . LEU B 1 379 ? 24.997  4.333   84.325  1.00 64.70  ?  388 LEU B HD22 1 
ATOM   10904 H HD23 . LEU B 1 379 ? 25.289  2.825   84.730  1.00 64.70  ?  388 LEU B HD23 1 
ATOM   10905 N N    . LYS B 1 380 ? 29.560  3.868   87.764  1.00 98.96  ?  389 LYS B N    1 
ATOM   10906 C CA   . LYS B 1 380 ? 30.997  4.141   87.717  1.00 72.49  ?  389 LYS B CA   1 
ATOM   10907 C C    . LYS B 1 380 ? 31.838  2.880   87.488  1.00 65.19  ?  389 LYS B C    1 
ATOM   10908 O O    . LYS B 1 380 ? 32.765  2.870   86.643  1.00 52.00  ?  389 LYS B O    1 
ATOM   10909 C CB   . LYS B 1 380 ? 31.414  4.826   89.009  1.00 70.86  ?  389 LYS B CB   1 
ATOM   10910 C CG   . LYS B 1 380 ? 31.045  6.317   89.040  1.00 91.11  ?  389 LYS B CG   1 
ATOM   10911 C CD   . LYS B 1 380 ? 31.204  6.889   90.443  1.00 97.37  ?  389 LYS B CD   1 
ATOM   10912 C CE   . LYS B 1 380 ? 31.059  8.413   90.536  1.00 72.70  ?  389 LYS B CE   1 
ATOM   10913 N NZ   . LYS B 1 380 ? 30.866  8.680   91.987  1.00 65.66  1  389 LYS B NZ   1 
ATOM   10914 H H    . LYS B 1 380 ? 29.192  4.036   88.523  1.00 118.75 ?  389 LYS B H    1 
ATOM   10915 H HA   . LYS B 1 380 ? 31.175  4.752   86.986  1.00 86.99  ?  389 LYS B HA   1 
ATOM   10916 H HB2  . LYS B 1 380 ? 30.970  4.392   89.755  1.00 85.03  ?  389 LYS B HB2  1 
ATOM   10917 H HB3  . LYS B 1 380 ? 32.376  4.754   89.109  1.00 85.03  ?  389 LYS B HB3  1 
ATOM   10918 H HG2  . LYS B 1 380 ? 31.632  6.806   88.443  1.00 109.33 ?  389 LYS B HG2  1 
ATOM   10919 H HG3  . LYS B 1 380 ? 30.120  6.425   88.769  1.00 109.33 ?  389 LYS B HG3  1 
ATOM   10920 H HD2  . LYS B 1 380 ? 30.528  6.495   91.016  1.00 116.84 ?  389 LYS B HD2  1 
ATOM   10921 H HD3  . LYS B 1 380 ? 32.086  6.658   90.773  1.00 116.84 ?  389 LYS B HD3  1 
ATOM   10922 H HE2  . LYS B 1 380 ? 31.867  8.853   90.229  1.00 87.24  ?  389 LYS B HE2  1 
ATOM   10923 H HE3  . LYS B 1 380 ? 30.278  8.713   90.044  1.00 87.24  ?  389 LYS B HE3  1 
ATOM   10924 H HZ1  . LYS B 1 380 ? 30.773  9.554   92.126  1.00 78.79  ?  389 LYS B HZ1  1 
ATOM   10925 H HZ2  . LYS B 1 380 ? 30.137  8.262   92.279  1.00 78.79  ?  389 LYS B HZ2  1 
ATOM   10926 H HZ3  . LYS B 1 380 ? 31.571  8.388   92.446  1.00 78.79  ?  389 LYS B HZ3  1 
ATOM   10927 N N    . THR B 1 381 ? 31.495  1.795   88.180  1.00 62.33  ?  390 THR B N    1 
ATOM   10928 C CA   . THR B 1 381 ? 32.220  0.552   87.992  1.00 77.55  ?  390 THR B CA   1 
ATOM   10929 C C    . THR B 1 381 ? 32.107  0.141   86.544  1.00 47.39  ?  390 THR B C    1 
ATOM   10930 O O    . THR B 1 381 ? 33.092  -0.135  85.863  1.00 73.43  ?  390 THR B O    1 
ATOM   10931 C CB   . THR B 1 381 ? 31.642  -0.524  88.920  1.00 98.25  ?  390 THR B CB   1 
ATOM   10932 O OG1  . THR B 1 381 ? 31.739  -0.098  90.284  1.00 146.84 ?  390 THR B OG1  1 
ATOM   10933 C CG2  . THR B 1 381 ? 32.338  -1.833  88.722  1.00 94.32  ?  390 THR B CG2  1 
ATOM   10934 H H    . THR B 1 381 ? 30.856  1.756   88.755  1.00 74.79  ?  390 THR B H    1 
ATOM   10935 H HA   . THR B 1 381 ? 33.156  0.682   88.209  1.00 93.06  ?  390 THR B HA   1 
ATOM   10936 H HB   . THR B 1 381 ? 30.705  -0.653  88.701  1.00 117.90 ?  390 THR B HB   1 
ATOM   10937 H HG1  . THR B 1 381 ? 31.423  -0.687  90.792  1.00 176.21 ?  390 THR B HG1  1 
ATOM   10938 H HG21 . THR B 1 381 ? 31.961  -2.502  89.315  1.00 113.18 ?  390 THR B HG21 1 
ATOM   10939 H HG22 . THR B 1 381 ? 32.232  -2.130  87.804  1.00 113.18 ?  390 THR B HG22 1 
ATOM   10940 H HG23 . THR B 1 381 ? 33.284  -1.738  88.914  1.00 113.18 ?  390 THR B HG23 1 
ATOM   10941 N N    . VAL B 1 382 ? 30.902  0.184   86.028  1.00 49.50  ?  391 VAL B N    1 
ATOM   10942 C CA   . VAL B 1 382 ? 30.714  -0.232  84.654  1.00 70.05  ?  391 VAL B CA   1 
ATOM   10943 C C    . VAL B 1 382 ? 31.467  0.703   83.723  1.00 64.38  ?  391 VAL B C    1 
ATOM   10944 O O    . VAL B 1 382 ? 31.854  0.314   82.612  1.00 63.13  ?  391 VAL B O    1 
ATOM   10945 C CB   . VAL B 1 382 ? 29.216  -0.259  84.328  1.00 69.57  ?  391 VAL B CB   1 
ATOM   10946 C CG1  . VAL B 1 382 ? 29.059  -0.694  82.919  1.00 62.19  ?  391 VAL B CG1  1 
ATOM   10947 C CG2  . VAL B 1 382 ? 28.463  -1.109  85.322  1.00 76.71  ?  391 VAL B CG2  1 
ATOM   10948 H H    . VAL B 1 382 ? 30.190  0.442   86.436  1.00 59.40  ?  391 VAL B H    1 
ATOM   10949 H HA   . VAL B 1 382 ? 31.067  -1.128  84.538  1.00 84.06  ?  391 VAL B HA   1 
ATOM   10950 H HB   . VAL B 1 382 ? 28.869  0.644   84.394  1.00 83.48  ?  391 VAL B HB   1 
ATOM   10951 H HG11 . VAL B 1 382 ? 28.114  -0.716  82.699  1.00 74.63  ?  391 VAL B HG11 1 
ATOM   10952 H HG12 . VAL B 1 382 ? 29.519  -0.066  82.341  1.00 74.63  ?  391 VAL B HG12 1 
ATOM   10953 H HG13 . VAL B 1 382 ? 29.443  -1.579  82.818  1.00 74.63  ?  391 VAL B HG13 1 
ATOM   10954 H HG21 . VAL B 1 382 ? 27.521  -1.106  85.090  1.00 92.05  ?  391 VAL B HG21 1 
ATOM   10955 H HG22 . VAL B 1 382 ? 28.810  -2.014  85.290  1.00 92.05  ?  391 VAL B HG22 1 
ATOM   10956 H HG23 . VAL B 1 382 ? 28.586  -0.738  86.210  1.00 92.05  ?  391 VAL B HG23 1 
ATOM   10957 N N    . ARG B 1 383 ? 31.570  1.984   84.097  1.00 58.49  ?  392 ARG B N    1 
ATOM   10958 C CA   . ARG B 1 383 ? 32.257  2.873   83.194  1.00 58.72  ?  392 ARG B CA   1 
ATOM   10959 C C    . ARG B 1 383 ? 33.730  2.545   83.213  1.00 62.78  ?  392 ARG B C    1 
ATOM   10960 O O    . ARG B 1 383 ? 34.374  2.429   82.162  1.00 65.83  ?  392 ARG B O    1 
ATOM   10961 C CB   . ARG B 1 383 ? 32.021  4.351   83.531  1.00 88.07  ?  392 ARG B CB   1 
ATOM   10962 C CG   . ARG B 1 383 ? 32.731  5.203   82.512  1.00 112.43 ?  392 ARG B CG   1 
ATOM   10963 C CD   . ARG B 1 383 ? 32.723  6.610   82.805  1.00 112.07 ?  392 ARG B CD   1 
ATOM   10964 N NE   . ARG B 1 383 ? 33.169  6.881   84.152  1.00 110.75 ?  392 ARG B NE   1 
ATOM   10965 C CZ   . ARG B 1 383 ? 33.122  8.104   84.660  1.00 78.68  ?  392 ARG B CZ   1 
ATOM   10966 N NH1  . ARG B 1 383 ? 32.666  9.103   83.920  1.00 76.25  1  392 ARG B NH1  1 
ATOM   10967 N NH2  . ARG B 1 383 ? 33.496  8.327   85.896  1.00 84.67  1  392 ARG B NH2  1 
ATOM   10968 H H    . ARG B 1 383 ? 31.268  2.334   84.822  1.00 70.18  ?  392 ARG B H    1 
ATOM   10969 H HA   . ARG B 1 383 ? 31.930  2.719   82.293  1.00 70.47  ?  392 ARG B HA   1 
ATOM   10970 H HB2  . ARG B 1 383 ? 31.072  4.549   83.496  1.00 105.69 ?  392 ARG B HB2  1 
ATOM   10971 H HB3  . ARG B 1 383 ? 32.382  4.549   84.409  1.00 105.69 ?  392 ARG B HB3  1 
ATOM   10972 H HG2  . ARG B 1 383 ? 33.657  4.918   82.460  1.00 134.92 ?  392 ARG B HG2  1 
ATOM   10973 H HG3  . ARG B 1 383 ? 32.302  5.079   81.651  1.00 134.92 ?  392 ARG B HG3  1 
ATOM   10974 H HD2  . ARG B 1 383 ? 33.318  7.068   82.191  1.00 134.48 ?  392 ARG B HD2  1 
ATOM   10975 H HD3  . ARG B 1 383 ? 31.819  6.950   82.712  1.00 134.48 ?  392 ARG B HD3  1 
ATOM   10976 H HE   . ARG B 1 383 ? 33.692  6.310   84.525  1.00 132.90 ?  392 ARG B HE   1 
ATOM   10977 H HH11 . ARG B 1 383 ? 32.408  8.957   83.113  1.00 91.50  ?  392 ARG B HH11 1 
ATOM   10978 H HH12 . ARG B 1 383 ? 32.634  9.898   84.245  1.00 91.50  ?  392 ARG B HH12 1 
ATOM   10979 H HH21 . ARG B 1 383 ? 33.796  7.680   86.378  1.00 101.60 ?  392 ARG B HH21 1 
ATOM   10980 H HH22 . ARG B 1 383 ? 33.472  9.125   86.215  1.00 101.60 ?  392 ARG B HH22 1 
ATOM   10981 N N    . SER B 1 384 ? 34.264  2.346   84.401  1.00 54.00  ?  393 SER B N    1 
ATOM   10982 C CA   . SER B 1 384 ? 35.684  2.088   84.512  1.00 69.76  ?  393 SER B CA   1 
ATOM   10983 C C    . SER B 1 384 ? 36.075  0.779   83.816  1.00 80.84  ?  393 SER B C    1 
ATOM   10984 O O    . SER B 1 384 ? 37.183  0.655   83.263  1.00 69.78  ?  393 SER B O    1 
ATOM   10985 C CB   . SER B 1 384 ? 36.055  2.083   85.987  1.00 92.32  ?  393 SER B CB   1 
ATOM   10986 O OG   . SER B 1 384 ? 35.491  0.971   86.643  1.00 116.60 ?  393 SER B OG   1 
ATOM   10987 H H    . SER B 1 384 ? 33.836  2.356   85.147  1.00 64.79  ?  393 SER B H    1 
ATOM   10988 H HA   . SER B 1 384 ? 36.170  2.810   84.085  1.00 83.71  ?  393 SER B HA   1 
ATOM   10989 H HB2  . SER B 1 384 ? 37.020  2.042   86.070  1.00 110.78 ?  393 SER B HB2  1 
ATOM   10990 H HB3  . SER B 1 384 ? 35.721  2.895   86.400  1.00 110.78 ?  393 SER B HB3  1 
ATOM   10991 H HG   . SER B 1 384 ? 34.653  0.994   86.579  1.00 139.92 ?  393 SER B HG   1 
ATOM   10992 N N    . THR B 1 385 ? 35.157  -0.188  83.772  1.00 81.64  ?  394 THR B N    1 
ATOM   10993 C CA   . THR B 1 385 ? 35.474  -1.439  83.096  1.00 69.07  ?  394 THR B CA   1 
ATOM   10994 C C    . THR B 1 385 ? 35.464  -1.261  81.592  1.00 86.79  ?  394 THR B C    1 
ATOM   10995 O O    . THR B 1 385 ? 36.288  -1.859  80.882  1.00 78.39  ?  394 THR B O    1 
ATOM   10996 C CB   . THR B 1 385 ? 34.524  -2.543  83.555  1.00 55.66  ?  394 THR B CB   1 
ATOM   10997 O OG1  . THR B 1 385 ? 34.744  -2.773  84.948  1.00 70.73  ?  394 THR B OG1  1 
ATOM   10998 C CG2  . THR B 1 385 ? 34.735  -3.861  82.851  1.00 60.77  ?  394 THR B CG2  1 
ATOM   10999 H H    . THR B 1 385 ? 34.369  -0.146  84.114  1.00 97.97  ?  394 THR B H    1 
ATOM   11000 H HA   . THR B 1 385 ? 36.372  -1.705  83.349  1.00 82.88  ?  394 THR B HA   1 
ATOM   11001 H HB   . THR B 1 385 ? 33.606  -2.261  83.414  1.00 66.80  ?  394 THR B HB   1 
ATOM   11002 H HG1  . THR B 1 385 ? 34.230  -3.378  85.224  1.00 84.88  ?  394 THR B HG1  1 
ATOM   11003 H HG21 . THR B 1 385 ? 34.105  -4.519  83.184  1.00 72.92  ?  394 THR B HG21 1 
ATOM   11004 H HG22 . THR B 1 385 ? 34.601  -3.752  81.896  1.00 72.92  ?  394 THR B HG22 1 
ATOM   11005 H HG23 . THR B 1 385 ? 35.637  -4.180  83.009  1.00 72.92  ?  394 THR B HG23 1 
ATOM   11006 N N    . THR B 1 386 ? 34.606  -0.388  81.098  1.00 73.92  ?  395 THR B N    1 
ATOM   11007 C CA   . THR B 1 386 ? 34.666  -0.069  79.686  1.00 110.60 ?  395 THR B CA   1 
ATOM   11008 C C    . THR B 1 386 ? 35.982  0.633   79.377  1.00 111.96 ?  395 THR B C    1 
ATOM   11009 O O    . THR B 1 386 ? 36.662  0.319   78.389  1.00 68.24  ?  395 THR B O    1 
ATOM   11010 C CB   . THR B 1 386 ? 33.486  0.822   79.328  1.00 66.72  ?  395 THR B CB   1 
ATOM   11011 O OG1  . THR B 1 386 ? 32.284  0.239   79.831  1.00 55.75  ?  395 THR B OG1  1 
ATOM   11012 C CG2  . THR B 1 386 ? 33.343  0.960   77.819  1.00 49.72  ?  395 THR B CG2  1 
ATOM   11013 H H    . THR B 1 386 ? 33.996  0.024   81.543  1.00 88.70  ?  395 THR B H    1 
ATOM   11014 H HA   . THR B 1 386 ? 34.615  -0.884  79.162  1.00 132.72 ?  395 THR B HA   1 
ATOM   11015 H HB   . THR B 1 386 ? 33.610  1.704   79.713  1.00 80.06  ?  395 THR B HB   1 
ATOM   11016 H HG1  . THR B 1 386 ? 32.330  0.161   80.666  1.00 66.89  ?  395 THR B HG1  1 
ATOM   11017 H HG21 . THR B 1 386 ? 32.587  1.531   77.608  1.00 59.66  ?  395 THR B HG21 1 
ATOM   11018 H HG22 . THR B 1 386 ? 34.148  1.352   77.444  1.00 59.66  ?  395 THR B HG22 1 
ATOM   11019 H HG23 . THR B 1 386 ? 33.201  0.088   77.418  1.00 59.66  ?  395 THR B HG23 1 
ATOM   11020 N N    . GLU B 1 387 ? 36.367  1.579   80.232  1.00 128.16 ?  396 GLU B N    1 
ATOM   11021 C CA   . GLU B 1 387 ? 37.596  2.300   79.978  1.00 122.22 ?  396 GLU B CA   1 
ATOM   11022 C C    . GLU B 1 387 ? 38.773  1.345   79.952  1.00 75.47  ?  396 GLU B C    1 
ATOM   11023 O O    . GLU B 1 387 ? 39.604  1.408   79.042  1.00 81.33  ?  396 GLU B O    1 
ATOM   11024 C CB   . GLU B 1 387 ? 37.803  3.374   81.043  1.00 118.01 ?  396 GLU B CB   1 
ATOM   11025 C CG   . GLU B 1 387 ? 36.777  4.497   81.048  1.00 140.58 ?  396 GLU B CG   1 
ATOM   11026 C CD   . GLU B 1 387 ? 36.919  5.454   82.245  1.00 168.91 ?  396 GLU B CD   1 
ATOM   11027 O OE1  . GLU B 1 387 ? 37.128  4.985   83.381  1.00 183.78 ?  396 GLU B OE1  1 
ATOM   11028 O OE2  . GLU B 1 387 ? 36.814  6.683   82.050  1.00 170.41 -1 396 GLU B OE2  1 
ATOM   11029 H H    . GLU B 1 387 ? 35.945  1.813   80.943  1.00 153.79 ?  396 GLU B H    1 
ATOM   11030 H HA   . GLU B 1 387 ? 37.539  2.736   79.114  1.00 146.67 ?  396 GLU B HA   1 
ATOM   11031 H HB2  . GLU B 1 387 ? 37.774  2.950   81.915  1.00 141.61 ?  396 GLU B HB2  1 
ATOM   11032 H HB3  . GLU B 1 387 ? 38.674  3.776   80.907  1.00 141.61 ?  396 GLU B HB3  1 
ATOM   11033 H HG2  . GLU B 1 387 ? 36.879  5.019   80.236  1.00 168.69 ?  396 GLU B HG2  1 
ATOM   11034 H HG3  . GLU B 1 387 ? 35.888  4.110   81.081  1.00 168.69 ?  396 GLU B HG3  1 
ATOM   11035 N N    . LYS B 1 388 ? 38.814  0.375   80.870  1.00 91.39  ?  397 LYS B N    1 
ATOM   11036 C CA   . LYS B 1 388 ? 40.021  -0.472  80.935  1.00 55.75  ?  397 LYS B CA   1 
ATOM   11037 C C    . LYS B 1 388 ? 40.161  -1.416  79.750  1.00 71.20  ?  397 LYS B C    1 
ATOM   11038 O O    . LYS B 1 388 ? 41.128  -2.181  79.715  1.00 91.52  ?  397 LYS B O    1 
ATOM   11039 C CB   . LYS B 1 388 ? 40.065  -1.301  82.249  1.00 55.71  ?  397 LYS B CB   1 
ATOM   11040 C CG   . LYS B 1 388 ? 40.658  -0.533  83.518  1.00 76.57  ?  397 LYS B CG   1 
ATOM   11041 C CD   . LYS B 1 388 ? 40.421  -1.184  84.907  1.00 61.49  ?  397 LYS B CD   1 
ATOM   11042 H H    . LYS B 1 388 ? 38.196  0.189   81.439  1.00 109.67 ?  397 LYS B H    1 
ATOM   11043 H HA   . LYS B 1 388 ? 40.799  0.108   80.934  1.00 66.90  ?  397 LYS B HA   1 
ATOM   11044 H HB2  . LYS B 1 388 ? 39.161  -1.575  82.470  1.00 66.85  ?  397 LYS B HB2  1 
ATOM   11045 H HB3  . LYS B 1 388 ? 40.615  -2.085  82.100  1.00 66.85  ?  397 LYS B HB3  1 
ATOM   11046 H HG2  . LYS B 1 388 ? 41.617  -0.450  83.401  1.00 91.88  ?  397 LYS B HG2  1 
ATOM   11047 H HG3  . LYS B 1 388 ? 40.262  0.353   83.547  1.00 91.88  ?  397 LYS B HG3  1 
ATOM   11048 H HD2  . LYS B 1 388 ? 39.468  -1.295  85.045  1.00 73.78  ?  397 LYS B HD2  1 
ATOM   11049 H HD3  . LYS B 1 388 ? 40.863  -2.047  84.930  1.00 73.78  ?  397 LYS B HD3  1 
ATOM   11050 N N    . SER B 1 389 ? 39.206  -1.440  78.830  1.00 66.89  ?  398 SER B N    1 
ATOM   11051 C CA   . SER B 1 389 ? 39.201  -2.373  77.709  1.00 76.18  ?  398 SER B CA   1 
ATOM   11052 C C    . SER B 1 389 ? 39.779  -1.793  76.434  1.00 73.27  ?  398 SER B C    1 
ATOM   11053 O O    . SER B 1 389 ? 39.599  -2.387  75.364  1.00 77.93  ?  398 SER B O    1 
ATOM   11054 C CB   . SER B 1 389 ? 37.801  -2.898  77.485  1.00 90.55  ?  398 SER B CB   1 
ATOM   11055 O OG   . SER B 1 389 ? 37.422  -3.668  78.623  1.00 83.67  ?  398 SER B OG   1 
ATOM   11056 H H    . SER B 1 389 ? 38.529  -0.909  78.833  1.00 80.27  ?  398 SER B H    1 
ATOM   11057 H HA   . SER B 1 389 ? 39.754  -3.133  77.951  1.00 91.41  ?  398 SER B HA   1 
ATOM   11058 H HB2  . SER B 1 389 ? 37.189  -2.153  77.380  1.00 108.66 ?  398 SER B HB2  1 
ATOM   11059 H HB3  . SER B 1 389 ? 37.789  -3.461  76.695  1.00 108.66 ?  398 SER B HB3  1 
ATOM   11060 H HG   . SER B 1 389 ? 37.438  -3.188  79.313  1.00 100.40 ?  398 SER B HG   1 
ATOM   11061 N N    . LEU B 1 390 ? 40.399  -0.628  76.526  1.00 56.35  ?  399 LEU B N    1 
ATOM   11062 C CA   . LEU B 1 390 ? 41.165  -0.041  75.432  1.00 84.52  ?  399 LEU B CA   1 
ATOM   11063 C C    . LEU B 1 390 ? 42.513  -0.763  75.273  1.00 121.18 ?  399 LEU B C    1 
ATOM   11064 O O    . LEU B 1 390 ? 42.966  -1.506  76.157  1.00 107.24 ?  399 LEU B O    1 
ATOM   11065 C CB   . LEU B 1 390 ? 41.400  1.454   75.684  1.00 61.27  ?  399 LEU B CB   1 
ATOM   11066 C CG   . LEU B 1 390 ? 40.206  2.437   75.583  1.00 72.97  ?  399 LEU B CG   1 
ATOM   11067 C CD1  . LEU B 1 390 ? 40.574  3.797   76.055  1.00 63.00  ?  399 LEU B CD1  1 
ATOM   11068 C CD2  . LEU B 1 390 ? 39.604  2.584   74.196  1.00 60.28  ?  399 LEU B CD2  1 
ATOM   11069 H H    . LEU B 1 390 ? 40.391  -0.141  77.235  1.00 67.62  ?  399 LEU B H    1 
ATOM   11070 H HA   . LEU B 1 390 ? 40.668  -0.137  74.604  1.00 101.42 ?  399 LEU B HA   1 
ATOM   11071 H HB2  . LEU B 1 390 ? 41.761  1.547   76.579  1.00 73.53  ?  399 LEU B HB2  1 
ATOM   11072 H HB3  . LEU B 1 390 ? 42.064  1.758   75.045  1.00 73.53  ?  399 LEU B HB3  1 
ATOM   11073 H HG   . LEU B 1 390 ? 39.501  2.113   76.166  1.00 87.56  ?  399 LEU B HG   1 
ATOM   11074 H HD11 . LEU B 1 390 ? 39.801  4.378   75.975  1.00 75.59  ?  399 LEU B HD11 1 
ATOM   11075 H HD12 . LEU B 1 390 ? 40.854  3.743   76.982  1.00 75.59  ?  399 LEU B HD12 1 
ATOM   11076 H HD13 . LEU B 1 390 ? 41.300  4.134   75.508  1.00 75.59  ?  399 LEU B HD13 1 
ATOM   11077 H HD21 . LEU B 1 390 ? 38.869  3.216   74.237  1.00 72.34  ?  399 LEU B HD21 1 
ATOM   11078 H HD22 . LEU B 1 390 ? 40.287  2.910   73.589  1.00 72.34  ?  399 LEU B HD22 1 
ATOM   11079 H HD23 . LEU B 1 390 ? 39.282  1.719   73.898  1.00 72.34  ?  399 LEU B HD23 1 
ATOM   11080 N N    . LEU B 1 391 ? 43.156  -0.550  74.120  1.00 108.92 ?  400 LEU B N    1 
ATOM   11081 C CA   . LEU B 1 391 ? 44.358  -1.297  73.762  1.00 123.57 ?  400 LEU B CA   1 
ATOM   11082 C C    . LEU B 1 391 ? 45.625  -0.454  73.800  1.00 139.76 ?  400 LEU B C    1 
ATOM   11083 O O    . LEU B 1 391 ? 46.422  -0.600  74.730  1.00 137.42 ?  400 LEU B O    1 
ATOM   11084 C CB   . LEU B 1 391 ? 44.154  -1.912  72.373  1.00 114.34 ?  400 LEU B CB   1 
ATOM   11085 C CG   . LEU B 1 391 ? 42.822  -2.660  72.205  1.00 82.19  ?  400 LEU B CG   1 
ATOM   11086 C CD1  . LEU B 1 391 ? 42.624  -3.250  70.818  1.00 79.17  ?  400 LEU B CD1  1 
ATOM   11087 C CD2  . LEU B 1 391 ? 42.702  -3.737  73.241  1.00 100.49 ?  400 LEU B CD2  1 
ATOM   11088 H H    . LEU B 1 391 ? 42.912  0.025   73.529  1.00 130.70 ?  400 LEU B H    1 
ATOM   11089 H HA   . LEU B 1 391 ? 44.470  -2.025  74.393  1.00 148.29 ?  400 LEU B HA   1 
ATOM   11090 H HB2  . LEU B 1 391 ? 44.180  -1.203  71.712  1.00 137.21 ?  400 LEU B HB2  1 
ATOM   11091 H HB3  . LEU B 1 391 ? 44.871  -2.543  72.204  1.00 137.21 ?  400 LEU B HB3  1 
ATOM   11092 H HG   . LEU B 1 391 ? 42.099  -2.031  72.357  1.00 98.63  ?  400 LEU B HG   1 
ATOM   11093 H HD11 . LEU B 1 391 ? 41.767  -3.704  70.788  1.00 95.00  ?  400 LEU B HD11 1 
ATOM   11094 H HD12 . LEU B 1 391 ? 42.643  -2.534  70.164  1.00 95.00  ?  400 LEU B HD12 1 
ATOM   11095 H HD13 . LEU B 1 391 ? 43.339  -3.881  70.638  1.00 95.00  ?  400 LEU B HD13 1 
ATOM   11096 H HD21 . LEU B 1 391 ? 41.857  -4.198  73.120  1.00 120.59 ?  400 LEU B HD21 1 
ATOM   11097 H HD22 . LEU B 1 391 ? 43.437  -4.361  73.134  1.00 120.59 ?  400 LEU B HD22 1 
ATOM   11098 H HD23 . LEU B 1 391 ? 42.736  -3.333  74.122  1.00 120.59 ?  400 LEU B HD23 1 
ATOM   11099 N N    . LYS B 1 392 ? 45.831  0.435   72.828  1.00 187.45 ?  401 LYS B N    1 
ATOM   11100 C CA   . LYS B 1 392 ? 47.071  1.211   72.744  1.00 166.98 ?  401 LYS B CA   1 
ATOM   11101 C C    . LYS B 1 392 ? 46.885  2.585   73.351  1.00 190.58 ?  401 LYS B C    1 
ATOM   11102 O O    . LYS B 1 392 ? 45.967  2.784   74.136  1.00 75.70  ?  401 LYS B O    1 
ATOM   11103 C CB   . LYS B 1 392 ? 47.552  1.333   71.285  1.00 161.00 ?  401 LYS B CB   1 
ATOM   11104 H H    . LYS B 1 392 ? 45.266  0.609   72.203  1.00 224.95 ?  401 LYS B H    1 
ATOM   11105 H HA   . LYS B 1 392 ? 47.763  0.754   73.248  1.00 200.38 ?  401 LYS B HA   1 
HETATM 11106 C C13  . C51 C 2 .   ? 32.613  -32.243 93.898  1.00 100.91 ?  501 C51 A C13  1 
HETATM 11107 C C18  . C51 C 2 .   ? 32.078  -30.991 94.188  1.00 107.99 ?  501 C51 A C18  1 
HETATM 11108 C C17  . C51 C 2 .   ? 32.910  -29.914 94.382  1.00 110.79 ?  501 C51 A C17  1 
HETATM 11109 C C16  . C51 C 2 .   ? 34.298  -30.076 94.295  1.00 115.27 ?  501 C51 A C16  1 
HETATM 11110 C C15  . C51 C 2 .   ? 34.823  -31.330 94.011  1.00 114.64 ?  501 C51 A C15  1 
HETATM 11111 C C19  . C51 C 2 .   ? 35.179  -28.953 94.504  1.00 125.42 ?  501 C51 A C19  1 
HETATM 11112 C C21  . C51 C 2 .   ? 24.973  -34.938 92.644  1.00 68.41  ?  501 C51 A C21  1 
HETATM 11113 C C22  . C51 C 2 .   ? 23.639  -34.599 92.721  1.00 63.72  ?  501 C51 A C22  1 
HETATM 11114 C C24  . C51 C 2 .   ? 23.388  -34.650 90.454  1.00 59.20  ?  501 C51 A C24  1 
HETATM 11115 C C27  . C51 C 2 .   ? 23.098  -34.639 88.067  1.00 60.66  ?  501 C51 A C27  1 
HETATM 11116 C C1   . C51 C 2 .   ? 29.881  -34.931 92.268  1.00 71.60  ?  501 C51 A C1   1 
HETATM 11117 C C2   . C51 C 2 .   ? 29.175  -33.742 91.698  1.00 61.55  ?  501 C51 A C2   1 
HETATM 11118 C C3   . C51 C 2 .   ? 27.656  -33.829 91.954  1.00 65.25  ?  501 C51 A C3   1 
HETATM 11119 C C4   . C51 C 2 .   ? 27.073  -35.085 91.322  1.00 67.84  ?  501 C51 A C4   1 
HETATM 11120 C C5   . C51 C 2 .   ? 27.710  -36.222 92.024  1.00 78.53  ?  501 C51 A C5   1 
HETATM 11121 C C6   . C51 C 2 .   ? 29.207  -36.195 91.750  1.00 92.55  ?  501 C51 A C6   1 
HETATM 11122 C C7   . C51 C 2 .   ? 25.564  -35.105 91.427  1.00 60.45  ?  501 C51 A C7   1 
HETATM 11123 C C8   . C51 C 2 .   ? 29.861  -34.801 93.809  1.00 95.28  ?  501 C51 A C8   1 
HETATM 11124 C C9   . C51 C 2 .   ? 30.476  -35.999 94.522  1.00 101.70 ?  501 C51 A C9   1 
HETATM 11125 C C10  . C51 C 2 .   ? 30.588  -33.552 94.285  1.00 85.34  ?  501 C51 A C10  1 
HETATM 11126 N N11  . C51 C 2 .   ? 31.763  -33.339 93.683  1.00 85.81  ?  501 C51 A N11  1 
HETATM 11127 O O12  . C51 C 2 .   ? 30.133  -32.819 95.170  1.00 64.44  ?  501 C51 A O12  1 
HETATM 11128 C C14  . C51 C 2 .   ? 33.987  -32.402 93.817  1.00 110.67 ?  501 C51 A C14  1 
HETATM 11129 N N20  . C51 C 2 .   ? 35.900  -28.088 94.665  1.00 132.68 ?  501 C51 A N20  1 
HETATM 11130 N N23  . C51 C 2 .   ? 22.847  -34.434 91.682  1.00 59.55  ?  501 C51 A N23  1 
HETATM 11131 C C25  . C51 C 2 .   ? 24.744  -35.021 90.268  1.00 57.63  ?  501 C51 A C25  1 
HETATM 11132 C C26  . C51 C 2 .   ? 22.572  -34.448 89.323  1.00 53.44  ?  501 C51 A C26  1 
HETATM 11133 C C28  . C51 C 2 .   ? 24.402  -35.012 87.897  1.00 47.93  ?  501 C51 A C28  1 
HETATM 11134 C C29  . C51 C 2 .   ? 25.213  -35.209 88.955  1.00 83.17  ?  501 C51 A C29  1 
HETATM 11135 H H48  . C51 C 2 .   ? 31.002  -30.842 94.268  1.00 129.59 ?  501 C51 A H48  1 
HETATM 11136 H H47  . C51 C 2 .   ? 32.484  -28.936 94.602  1.00 132.95 ?  501 C51 A H47  1 
HETATM 11137 H H46  . C51 C 2 .   ? 35.901  -31.461 93.943  1.00 137.57 ?  501 C51 A H46  1 
HETATM 11138 H H49  . C51 C 2 .   ? 25.538  -35.068 93.566  1.00 82.09  ?  501 C51 A H49  1 
HETATM 11139 H H50  . C51 C 2 .   ? 23.154  -34.445 93.683  1.00 76.47  ?  501 C51 A H50  1 
HETATM 11140 H H52  . C51 C 2 .   ? 22.471  -34.493 87.189  1.00 72.79  ?  501 C51 A H52  1 
HETATM 11141 H H30  . C51 C 2 .   ? 30.919  -34.922 91.939  1.00 85.92  ?  501 C51 A H30  1 
HETATM 11142 H H32  . C51 C 2 .   ? 29.578  -32.826 92.127  1.00 73.86  ?  501 C51 A H32  1 
HETATM 11143 H H31  . C51 C 2 .   ? 29.367  -33.652 90.630  1.00 73.86  ?  501 C51 A H31  1 
HETATM 11144 H H34  . C51 C 2 .   ? 27.457  -33.824 93.025  1.00 78.30  ?  501 C51 A H34  1 
HETATM 11145 H H33  . C51 C 2 .   ? 27.153  -32.935 91.590  1.00 78.30  ?  501 C51 A H33  1 
HETATM 11146 H H35  . C51 C 2 .   ? 27.362  -35.107 90.273  1.00 81.41  ?  501 C51 A H35  1 
HETATM 11147 H H36  . C51 C 2 .   ? 27.268  -37.173 91.728  1.00 94.24  ?  501 C51 A H36  1 
HETATM 11148 H H37  . C51 C 2 .   ? 27.524  -36.152 93.094  1.00 94.24  ?  501 C51 A H37  1 
HETATM 11149 H H38  . C51 C 2 .   ? 29.395  -36.341 90.687  1.00 111.06 ?  501 C51 A H38  1 
HETATM 11150 H H39  . C51 C 2 .   ? 29.677  -37.061 92.214  1.00 111.06 ?  501 C51 A H39  1 
HETATM 11151 H H40  . C51 C 2 .   ? 28.814  -34.775 94.108  1.00 114.34 ?  501 C51 A H40  1 
HETATM 11152 H H43  . C51 C 2 .   ? 31.521  -36.147 94.257  1.00 122.04 ?  501 C51 A H43  1 
HETATM 11153 H H42  . C51 C 2 .   ? 29.949  -36.927 94.304  1.00 122.04 ?  501 C51 A H42  1 
HETATM 11154 H H41  . C51 C 2 .   ? 30.445  -35.875 95.604  1.00 122.04 ?  501 C51 A H41  1 
HETATM 11155 H H44  . C51 C 2 .   ? 32.098  -34.015 93.003  1.00 102.97 ?  501 C51 A H44  1 
HETATM 11156 H H45  . C51 C 2 .   ? 34.457  -33.360 93.601  1.00 132.81 ?  501 C51 A H45  1 
HETATM 11157 H H51  . C51 C 2 .   ? 21.536  -34.143 89.460  1.00 64.13  ?  501 C51 A H51  1 
HETATM 11158 H H53  . C51 C 2 .   ? 24.789  -35.150 86.889  1.00 57.52  ?  501 C51 A H53  1 
HETATM 11159 H H54  . C51 C 2 .   ? 26.247  -35.518 88.813  1.00 99.80  ?  501 C51 A H54  1 
HETATM 11160 C C13  . C51 D 2 .   ? 15.433  3.773   81.760  1.00 108.12 ?  501 C51 B C13  1 
HETATM 11161 C C18  . C51 D 2 .   ? 14.132  3.668   81.302  1.00 106.61 ?  501 C51 B C18  1 
HETATM 11162 C C17  . C51 D 2 .   ? 13.176  3.058   82.073  1.00 106.49 ?  501 C51 B C17  1 
HETATM 11163 C C16  . C51 D 2 .   ? 13.504  2.545   83.307  1.00 115.98 ?  501 C51 B C16  1 
HETATM 11164 C C15  . C51 D 2 .   ? 14.795  2.668   83.774  1.00 107.46 ?  501 C51 B C15  1 
HETATM 11165 C C19  . C51 D 2 .   ? 12.532  1.803   84.061  1.00 148.41 ?  501 C51 B C19  1 
HETATM 11166 C C21  . C51 D 2 .   ? 22.793  4.594   79.239  1.00 130.67 ?  501 C51 B C21  1 
HETATM 11167 C C22  . C51 D 2 .   ? 24.132  4.445   79.518  1.00 136.65 ?  501 C51 B C22  1 
HETATM 11168 C C24  . C51 D 2 .   ? 24.501  3.245   77.623  1.00 114.33 ?  501 C51 B C24  1 
HETATM 11169 C C27  . C51 D 2 .   ? 24.924  1.844   75.716  1.00 102.58 ?  501 C51 B C27  1 
HETATM 11170 C C1   . C51 D 2 .   ? 18.084  4.915   78.748  1.00 125.15 ?  501 C51 B C1   1 
HETATM 11171 C C2   . C51 D 2 .   ? 18.525  3.471   78.721  1.00 122.34 ?  501 C51 B C2   1 
HETATM 11172 C C3   . C51 D 2 .   ? 20.027  3.349   78.895  1.00 126.07 ?  501 C51 B C3   1 
HETATM 11173 C C4   . C51 D 2 .   ? 20.782  4.125   77.829  1.00 124.86 ?  501 C51 B C4   1 
HETATM 11174 C C5   . C51 D 2 .   ? 20.280  5.568   77.764  1.00 127.31 ?  501 C51 B C5   1 
HETATM 11175 C C6   . C51 D 2 .   ? 18.775  5.646   77.622  1.00 126.36 ?  501 C51 B C6   1 
HETATM 11176 C C7   . C51 D 2 .   ? 22.270  4.058   78.104  1.00 121.60 ?  501 C51 B C7   1 
HETATM 11177 C C8   . C51 D 2 .   ? 18.317  5.565   80.135  1.00 135.66 ?  501 C51 B C8   1 
HETATM 11178 C C9   . C51 D 2 .   ? 17.850  6.996   80.195  1.00 146.95 ?  501 C51 B C9   1 
HETATM 11179 C C10  . C51 D 2 .   ? 17.620  4.833   81.259  1.00 135.23 ?  501 C51 B C10  1 
HETATM 11180 N N11  . C51 D 2 .   ? 16.403  4.362   80.935  1.00 117.53 ?  501 C51 B N11  1 
HETATM 11181 O O12  . C51 D 2 .   ? 18.139  4.742   82.369  1.00 151.15 ?  501 C51 B O12  1 
HETATM 11182 C C14  . C51 D 2 .   ? 15.756  3.274   83.001  1.00 105.65 ?  501 C51 B C14  1 
HETATM 11183 N N20  . C51 D 2 .   ? 11.790  1.199   84.677  1.00 170.42 ?  501 C51 B N20  1 
HETATM 11184 N N23  . C51 D 2 .   ? 24.987  3.796   78.767  1.00 130.91 ?  501 C51 B N23  1 
HETATM 11185 C C25  . C51 D 2 .   ? 23.149  3.366   77.230  1.00 112.41 ?  501 C51 B C25  1 
HETATM 11186 C C26  . C51 D 2 .   ? 25.372  2.464   76.837  1.00 106.57 ?  501 C51 B C26  1 
HETATM 11187 C C28  . C51 D 2 .   ? 23.626  1.981   75.315  1.00 107.07 ?  501 C51 B C28  1 
HETATM 11188 C C29  . C51 D 2 .   ? 22.741  2.728   76.041  1.00 109.47 ?  501 C51 B C29  1 
HETATM 11189 H H48  . C51 D 2 .   ? 13.842  4.063   80.329  1.00 127.93 ?  501 C51 B H48  1 
HETATM 11190 H H47  . C51 D 2 .   ? 12.154  2.981   81.704  1.00 127.79 ?  501 C51 B H47  1 
HETATM 11191 H H46  . C51 D 2 .   ? 15.052  2.283   84.760  1.00 128.95 ?  501 C51 B H46  1 
HETATM 11192 H H49  . C51 D 2 .   ? 22.167  5.145   79.940  1.00 156.81 ?  501 C51 B H49  1 
HETATM 11193 H H50  . C51 D 2 .   ? 24.568  4.878   80.417  1.00 163.98 ?  501 C51 B H50  1 
HETATM 11194 H H52  . C51 D 2 .   ? 25.602  1.229   75.126  1.00 123.10 ?  501 C51 B H52  1 
HETATM 11195 H H30  . C51 D 2 .   ? 17.012  4.946   78.558  1.00 150.18 ?  501 C51 B H30  1 
HETATM 11196 H H32  . C51 D 2 .   ? 18.011  2.912   79.501  1.00 146.81 ?  501 C51 B H32  1 
HETATM 11197 H H31  . C51 D 2 .   ? 18.218  2.991   77.793  1.00 146.81 ?  501 C51 B H31  1 
HETATM 11198 H H34  . C51 D 2 .   ? 20.313  3.710   79.882  1.00 151.29 ?  501 C51 B H34  1 
HETATM 11199 H H33  . C51 D 2 .   ? 20.327  2.302   78.903  1.00 151.29 ?  501 C51 B H33  1 
HETATM 11200 H H35  . C51 D 2 .   ? 20.584  3.650   76.870  1.00 149.83 ?  501 C51 B H35  1 
HETATM 11201 H H36  . C51 D 2 .   ? 20.614  6.134   78.633  1.00 152.77 ?  501 C51 B H36  1 
HETATM 11202 H H37  . C51 D 2 .   ? 20.749  6.075   76.922  1.00 152.77 ?  501 C51 B H37  1 
HETATM 11203 H H38  . C51 D 2 .   ? 18.452  6.683   77.552  1.00 151.63 ?  501 C51 B H38  1 
HETATM 11204 H H39  . C51 D 2 .   ? 18.470  5.211   76.671  1.00 151.63 ?  501 C51 B H39  1 
HETATM 11205 H H40  . C51 D 2 .   ? 19.394  5.588   80.296  1.00 162.79 ?  501 C51 B H40  1 
HETATM 11206 H H43  . C51 D 2 .   ? 18.356  7.628   79.466  1.00 176.34 ?  501 C51 B H43  1 
HETATM 11207 H H42  . C51 D 2 .   ? 18.007  7.442   81.176  1.00 176.34 ?  501 C51 B H42  1 
HETATM 11208 H H41  . C51 D 2 .   ? 16.784  7.076   79.987  1.00 176.34 ?  501 C51 B H41  1 
HETATM 11209 H H44  . C51 D 2 .   ? 16.120  4.429   79.963  1.00 141.04 ?  501 C51 B H44  1 
HETATM 11210 H H45  . C51 D 2 .   ? 16.760  3.333   83.418  1.00 126.78 ?  501 C51 B H45  1 
HETATM 11211 H H51  . C51 D 2 .   ? 26.412  2.367   77.146  1.00 127.89 ?  501 C51 B H51  1 
HETATM 11212 H H53  . C51 D 2 .   ? 23.295  1.486   74.403  1.00 128.49 ?  501 C51 B H53  1 
HETATM 11213 H H54  . C51 D 2 .   ? 21.708  2.843   75.715  1.00 131.37 ?  501 C51 B H54  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   . MET A 1   ? 1.5059  1.8364  1.1590  -0.2452 -0.0984 -0.0806 10  MET A N   
2     C CA  . MET A 1   ? 1.6708  1.9726  1.3484  -0.2261 -0.0715 -0.0817 10  MET A CA  
3     C C   . MET A 1   ? 1.8298  2.1223  1.5282  -0.2148 -0.0776 -0.0337 10  MET A C   
4     O O   . MET A 1   ? 1.1573  1.4722  0.8336  -0.2247 -0.0967 0.0000  10  MET A O   
5     C CB  . MET A 1   ? 1.5650  1.8855  1.2043  -0.2321 -0.0460 -0.1078 10  MET A CB  
7     N N   . ILE A 2   ? 2.2522  2.5102  1.9907  -0.1949 -0.0621 -0.0314 11  ILE A N   
8     C CA  . ILE A 2   ? 2.8754  3.1194  2.6379  -0.1829 -0.0675 0.0086  11  ILE A CA  
9     C C   . ILE A 2   ? 1.6302  1.8898  1.3618  -0.1892 -0.0582 0.0280  11  ILE A C   
10    O O   . ILE A 2   ? 1.7260  2.0007  1.4311  -0.1958 -0.0373 0.0048  11  ILE A O   
11    C CB  . ILE A 2   ? 3.9502  4.1546  3.7600  -0.1622 -0.0536 0.0031  11  ILE A CB  
12    C CG1 . ILE A 2   ? 2.7673  2.9577  2.6080  -0.1595 -0.0614 -0.0126 11  ILE A CG1 
13    C CG2 . ILE A 2   ? 2.3793  2.5700  2.2118  -0.1505 -0.0594 0.0405  11  ILE A CG2 
14    C CD1 . ILE A 2   ? 3.0917  3.2445  2.9702  -0.1436 -0.0465 -0.0202 11  ILE A CD1 
26    N N   . SER A 3   ? 1.3675  1.6236  1.1066  -0.1871 -0.0736 0.0700  12  SER A N   
27    C CA  . SER A 3   ? 2.0575  2.3256  1.7705  -0.1960 -0.0676 0.0950  12  SER A CA  
28    C C   . SER A 3   ? 2.9365  3.1850  2.6704  -0.1833 -0.0403 0.0854  12  SER A C   
29    O O   . SER A 3   ? 1.0074  1.2224  0.7842  -0.1641 -0.0377 0.0864  12  SER A O   
30    C CB  . SER A 3   ? 1.3827  1.6441  1.1045  -0.1963 -0.0955 0.1431  12  SER A CB  
31    O OG  . SER A 3   ? 1.6433  1.9122  1.3409  -0.2077 -0.0910 0.1706  12  SER A OG  
37    N N   . LYS A 4   ? 2.0985  2.3723  1.8015  -0.1954 -0.0206 0.0773  13  LYS A N   
38    C CA  . LYS A 4   ? 1.8287  2.0916  1.5529  -0.1847 0.0040  0.0681  13  LYS A CA  
39    C C   . LYS A 4   ? 2.0515  2.2962  1.7933  -0.1818 -0.0038 0.1092  13  LYS A C   
40    O O   . LYS A 4   ? 2.5274  2.7543  2.2975  -0.1696 0.0108  0.1057  13  LYS A O   
41    C CB  . LYS A 4   ? 1.8888  2.1922  1.5793  -0.1989 0.0287  0.0439  13  LYS A CB  
44    N N   . GLU A 5   ? 1.7280  1.9751  1.4552  -0.1927 -0.0288 0.1479  14  GLU A N   
45    C CA  . GLU A 5   ? 1.2956  1.5195  1.0420  -0.1900 -0.0409 0.1875  14  GLU A CA  
46    C C   . GLU A 5   ? 1.0639  1.2447  0.8623  -0.1645 -0.0477 0.1867  14  GLU A C   
47    O O   . GLU A 5   ? 1.3018  1.4584  1.1220  -0.1589 -0.0553 0.2122  14  GLU A O   
48    C CB  . GLU A 5   ? 1.2767  1.5099  0.9977  -0.2066 -0.0707 0.2285  14  GLU A CB  
49    C CG  . GLU A 5   ? 2.4583  2.6736  2.2041  -0.1935 -0.0991 0.2360  14  GLU A CG  
56    N N   . TYR A 6   ? 1.4184  1.5899  1.2360  -0.1508 -0.0455 0.1581  15  TYR A N   
57    C CA  . TYR A 6   ? 1.1572  1.2937  1.0200  -0.1289 -0.0453 0.1512  15  TYR A CA  
58    C C   . TYR A 6   ? 1.0856  1.2100  0.9619  -0.1190 -0.0196 0.1222  15  TYR A C   
59    O O   . TYR A 6   ? 0.7820  0.8776  0.6906  -0.1030 -0.0169 0.1169  15  TYR A O   
60    C CB  . TYR A 6   ? 1.0663  1.2016  0.9444  -0.1227 -0.0602 0.1418  15  TYR A CB  
61    C CG  . TYR A 6   ? 1.5325  1.6745  1.4142  -0.1255 -0.0902 0.1712  15  TYR A CG  
62    C CD1 . TYR A 6   ? 1.0328  1.1521  0.9452  -0.1138 -0.1047 0.1967  15  TYR A CD1 
63    C CD2 . TYR A 6   ? 1.8631  2.0338  1.7196  -0.1393 -0.1060 0.1719  15  TYR A CD2 
64    C CE1 . TYR A 6   ? 0.7477  0.8713  0.6700  -0.1136 -0.1351 0.2235  15  TYR A CE1 
65    C CE2 . TYR A 6   ? 1.2078  1.3853  1.0712  -0.1407 -0.1370 0.2004  15  TYR A CE2 
66    C CZ  . TYR A 6   ? 1.0950  1.2483  0.9933  -0.1269 -0.1517 0.2265  15  TYR A CZ  
67    O OH  . TYR A 6   ? 0.9115  1.0696  0.8235  -0.1255 -0.1853 0.2546  15  TYR A OH  
77    N N   . HIS A 7   ? 1.0639  1.2111  0.9172  -0.1280 -0.0012 0.1030  16  HIS A N   
78    C CA  . HIS A 7   ? 1.0911  1.2285  0.9617  -0.1174 0.0203  0.0782  16  HIS A CA  
79    C C   . HIS A 7   ? 0.8622  0.9734  0.7568  -0.1031 0.0213  0.0542  16  HIS A C   
80    O O   . HIS A 7   ? 1.1668  1.2505  1.0886  -0.0895 0.0262  0.0511  16  HIS A O   
81    C CB  . HIS A 7   ? 1.3463  1.4682  1.2364  -0.1121 0.0236  0.0979  16  HIS A CB  
82    C CG  . HIS A 7   ? 1.4356  1.5826  1.3034  -0.1297 0.0239  0.1225  16  HIS A CG  
83    N ND1 . HIS A 7   ? 1.5864  1.7747  1.4187  -0.1477 0.0336  0.1153  16  HIS A ND1 
84    C CD2 . HIS A 7   ? 1.1718  1.3084  1.0460  -0.1346 0.0147  0.1551  16  HIS A CD2 
85    C CE1 . HIS A 7   ? 1.5525  1.7568  1.3689  -0.1646 0.0315  0.1450  16  HIS A CE1 
86    N NE2 . HIS A 7   ? 1.2507  1.4216  1.0934  -0.1569 0.0188  0.1704  16  HIS A NE2 
93    N N   . ILE A 8   ? 0.6821  0.8032  0.5639  -0.1089 0.0155  0.0385  17  ILE A N   
94    C CA  . ILE A 8   ? 0.7913  0.8928  0.6897  -0.1016 0.0175  0.0127  17  ILE A CA  
95    C C   . ILE A 8   ? 1.1354  1.2532  1.0160  -0.1071 0.0303  -0.0218 17  ILE A C   
96    O O   . ILE A 8   ? 1.2896  1.4398  1.1381  -0.1215 0.0292  -0.0275 17  ILE A O   
97    C CB  . ILE A 8   ? 0.9551  1.0550  0.8594  -0.1048 -0.0009 0.0201  17  ILE A CB  
98    C CG1 . ILE A 8   ? 1.3126  1.3955  1.2423  -0.0951 -0.0106 0.0473  17  ILE A CG1 
99    C CG2 . ILE A 8   ? 1.1648  1.2477  1.0828  -0.1029 0.0018  -0.0070 17  ILE A CG2 
100   C CD1 . ILE A 8   ? 1.4847  1.5774  1.4226  -0.0978 -0.0298 0.0597  17  ILE A CD1 
112   N N   . ASP A 9   ? 1.2161  1.3116  1.1174  -0.0958 0.0417  -0.0448 18  ASP A N   
113   C CA  . ASP A 9   ? 1.3891  1.4956  1.2832  -0.0962 0.0549  -0.0810 18  ASP A CA  
114   C C   . ASP A 9   ? 1.0294  1.1211  0.9244  -0.1000 0.0468  -0.1041 18  ASP A C   
115   O O   . ASP A 9   ? 0.8260  0.8850  0.7437  -0.0948 0.0387  -0.0986 18  ASP A O   
116   C CB  . ASP A 9   ? 1.1514  1.2389  1.0743  -0.0800 0.0678  -0.0915 18  ASP A CB  
117   C CG  . ASP A 9   ? 1.3148  1.4157  1.2393  -0.0761 0.0827  -0.1314 18  ASP A CG  
118   O OD1 . ASP A 9   ? 1.0662  1.2088  0.9704  -0.0837 0.0952  -0.1402 18  ASP A OD1 
119   O OD2 . ASP A 9   ? 1.5114  1.5804  1.4595  -0.0652 0.0819  -0.1540 18  ASP A OD2 
124   N N   . GLU A 10  ? 0.9360  1.0529  0.8057  -0.1107 0.0500  -0.1315 19  GLU A N   
125   C CA  . GLU A 10  ? 1.6566  1.7602  1.5260  -0.1168 0.0416  -0.1575 19  GLU A CA  
126   C C   . GLU A 10  ? 1.2866  1.3436  1.1924  -0.1030 0.0443  -0.1742 19  GLU A C   
127   O O   . GLU A 10  ? 0.8907  0.9211  0.8097  -0.1070 0.0328  -0.1760 19  GLU A O   
128   C CB  . GLU A 10  ? 0.7661  0.9050  0.6016  -0.1288 0.0483  -0.1907 19  GLU A CB  
131   N N   . GLU A 11  ? 1.3349  1.3819  1.2593  -0.0877 0.0576  -0.1815 20  GLU A N   
132   C CA  . GLU A 11  ? 1.0588  1.0600  1.0183  -0.0732 0.0576  -0.1924 20  GLU A CA  
133   C C   . GLU A 11  ? 0.8698  0.8444  0.8490  -0.0659 0.0519  -0.1564 20  GLU A C   
134   O O   . GLU A 11  ? 0.8033  0.7437  0.7965  -0.0675 0.0422  -0.1486 20  GLU A O   
135   C CB  . GLU A 11  ? 1.2236  1.2321  1.1970  -0.0592 0.0728  -0.2223 20  GLU A CB  
136   C CG  . GLU A 11  ? 1.4693  1.4322  1.4839  -0.0402 0.0711  -0.2300 20  GLU A CG  
137   C CD  . GLU A 11  ? 1.6524  1.6349  1.6880  -0.0230 0.0864  -0.2470 20  GLU A CD  
138   O OE1 . GLU A 11  ? 1.9666  1.9997  1.9842  -0.0275 0.1010  -0.2510 20  GLU A OE1 
139   O OE2 . GLU A 11  ? 1.5878  1.5366  1.6599  -0.0059 0.0828  -0.2548 20  GLU A OE2 
146   N N   . VAL A 12  ? 1.2115  1.2017  1.1913  -0.0598 0.0580  -0.1342 21  VAL A N   
147   C CA  . VAL A 12  ? 1.0254  0.9866  1.0242  -0.0522 0.0528  -0.1072 21  VAL A CA  
148   C C   . VAL A 12  ? 1.0423  1.0137  1.0306  -0.0599 0.0452  -0.0757 21  VAL A C   
149   O O   . VAL A 12  ? 0.9088  0.8601  0.9098  -0.0548 0.0417  -0.0550 21  VAL A O   
150   C CB  . VAL A 12  ? 1.1784  1.1386  1.1951  -0.0379 0.0610  -0.1036 21  VAL A CB  
151   C CG1 . VAL A 12  ? 1.0267  0.9735  1.0637  -0.0267 0.0656  -0.1350 21  VAL A CG1 
152   C CG2 . VAL A 12  ? 1.5502  1.5529  1.5523  -0.0416 0.0701  -0.0938 21  VAL A CG2 
162   N N   . GLY A 13  ? 1.1329  1.1335  1.0995  -0.0717 0.0410  -0.0726 22  GLY A N   
163   C CA  . GLY A 13  ? 0.9229  0.9285  0.8888  -0.0757 0.0309  -0.0439 22  GLY A CA  
164   C C   . GLY A 13  ? 0.8479  0.8572  0.8174  -0.0692 0.0324  -0.0177 22  GLY A C   
165   O O   . GLY A 13  ? 0.8474  0.8804  0.8029  -0.0720 0.0371  -0.0125 22  GLY A O   
169   N N   . PHE A 14  ? 0.7030  0.6903  0.6900  -0.0627 0.0286  -0.0014 23  PHE A N   
170   C CA  . PHE A 14  ? 0.7387  0.7254  0.7309  -0.0571 0.0277  0.0218  23  PHE A CA  
171   C C   . PHE A 14  ? 0.9711  0.9452  0.9722  -0.0486 0.0367  0.0193  23  PHE A C   
172   O O   . PHE A 14  ? 1.3410  1.3155  1.3461  -0.0458 0.0360  0.0363  23  PHE A O   
173   C CB  . PHE A 14  ? 0.8591  0.8301  0.8668  -0.0530 0.0210  0.0360  23  PHE A CB  
174   C CG  . PHE A 14  ? 1.1926  1.1797  1.2017  -0.0582 0.0101  0.0432  23  PHE A CG  
175   C CD1 . PHE A 14  ? 0.7606  0.7672  0.7633  -0.0606 0.0003  0.0604  23  PHE A CD1 
176   C CD2 . PHE A 14  ? 0.7494  0.7324  0.7695  -0.0614 0.0080  0.0347  23  PHE A CD2 
177   C CE1 . PHE A 14  ? 1.0739  1.0961  1.0832  -0.0636 -0.0133 0.0675  23  PHE A CE1 
178   C CE2 . PHE A 14  ? 0.6550  0.6589  0.6837  -0.0656 -0.0034 0.0405  23  PHE A CE2 
179   C CZ  . PHE A 14  ? 0.8211  0.8442  0.8455  -0.0652 -0.0148 0.0563  23  PHE A CZ  
189   N N   . ALA A 15  ? 0.9284  0.8881  0.9369  -0.0440 0.0424  -0.0006 24  ALA A N   
190   C CA  . ALA A 15  ? 0.9302  0.8842  0.9513  -0.0350 0.0490  -0.0043 24  ALA A CA  
191   C C   . ALA A 15  ? 0.7855  0.7746  0.7985  -0.0385 0.0579  -0.0086 24  ALA A C   
192   O O   . ALA A 15  ? 0.8497  0.8649  0.8436  -0.0480 0.0603  -0.0155 24  ALA A O   
193   C CB  . ALA A 15  ? 1.1078  1.0373  1.1430  -0.0278 0.0500  -0.0245 24  ALA A CB  
199   N N   . LEU A 16  ? 0.8331  0.8257  0.8595  -0.0329 0.0624  -0.0034 25  LEU A N   
200   C CA  . LEU A 16  ? 0.6559  0.6857  0.6787  -0.0376 0.0736  -0.0081 25  LEU A CA  
201   C C   . LEU A 16  ? 0.6637  0.7020  0.6994  -0.0296 0.0839  -0.0412 25  LEU A C   
202   O O   . LEU A 16  ? 0.9335  0.9445  0.9933  -0.0164 0.0806  -0.0509 25  LEU A O   
203   C CB  . LEU A 16  ? 0.8430  0.8754  0.8801  -0.0362 0.0738  0.0105  25  LEU A CB  
204   C CG  . LEU A 16  ? 0.7950  0.8703  0.8268  -0.0468 0.0852  0.0137  25  LEU A CG  
205   C CD1 . LEU A 16  ? 0.8080  0.9019  0.8081  -0.0638 0.0820  0.0312  25  LEU A CD1 
206   C CD2 . LEU A 16  ? 0.8154  0.8845  0.8691  -0.0440 0.0825  0.0298  25  LEU A CD2 
218   N N   . PRO A 17  ? 0.7152  0.7877  0.7347  -0.0372 0.0946  -0.0604 26  PRO A N   
219   C CA  . PRO A 17  ? 1.0081  1.0873  1.0432  -0.0274 0.1047  -0.0989 26  PRO A CA  
220   C C   . PRO A 17  ? 1.0874  1.1933  1.1504  -0.0186 0.1178  -0.1100 26  PRO A C   
221   O O   . PRO A 17  ? 1.3285  1.4742  1.3828  -0.0293 0.1280  -0.0991 26  PRO A O   
222   C CB  . PRO A 17  ? 1.0005  1.1107  1.0028  -0.0412 0.1115  -0.1167 26  PRO A CB  
223   C CG  . PRO A 17  ? 0.7544  0.8902  0.7257  -0.0595 0.1090  -0.0837 26  PRO A CG  
224   C CD  . PRO A 17  ? 0.5708  0.6713  0.5548  -0.0551 0.0943  -0.0490 26  PRO A CD  
232   N N   . ASN A 18  ? 1.1272  1.2123  1.2261  0.0003  0.1165  -0.1321 27  ASN A N   
233   C CA  . ASN A 18  ? 0.8334  0.9404  0.9721  0.0142  0.1256  -0.1475 27  ASN A CA  
234   C C   . ASN A 18  ? 0.8355  0.9637  0.9780  0.0068  0.1271  -0.1170 27  ASN A C   
235   O O   . ASN A 18  ? 1.1106  1.2898  1.2510  -0.0031 0.1432  -0.1190 27  ASN A O   
236   C CB  . ASN A 18  ? 0.7543  0.9069  0.8981  0.0160  0.1460  -0.1887 27  ASN A CB  
237   C CG  . ASN A 18  ? 1.5609  1.6832  1.7181  0.0298  0.1416  -0.2251 27  ASN A CG  
242   N N   . PRO A 19  ? 0.9607  1.0501  1.1093  0.0102  0.1103  -0.0896 28  PRO A N   
243   C CA  . PRO A 19  ? 0.7794  0.8797  0.9313  0.0025  0.1078  -0.0605 28  PRO A CA  
244   C C   . PRO A 19  ? 0.7434  0.8762  0.9361  0.0103  0.1153  -0.0695 28  PRO A C   
245   O O   . PRO A 19  ? 0.5605  0.6921  0.7886  0.0285  0.1154  -0.0939 28  PRO A O   
246   C CB  . PRO A 19  ? 0.6483  0.6956  0.7979  0.0071  0.0878  -0.0385 28  PRO A CB  
247   C CG  . PRO A 19  ? 0.9553  0.9734  1.0848  0.0075  0.0827  -0.0467 28  PRO A CG  
248   C CD  . PRO A 19  ? 0.8117  0.8467  0.9527  0.0149  0.0932  -0.0818 28  PRO A CD  
256   N N   . GLN A 20  ? 0.7274  0.8909  0.9179  -0.0043 0.1208  -0.0494 29  GLN A N   
257   C CA  . GLN A 20  ? 0.6675  0.8719  0.8983  -0.0007 0.1299  -0.0578 29  GLN A CA  
258   C C   . GLN A 20  ? 0.6699  0.8393  0.9343  0.0161  0.1107  -0.0518 29  GLN A C   
259   O O   . GLN A 20  ? 0.5743  0.7014  0.8221  0.0133  0.0935  -0.0274 29  GLN A O   
260   C CB  . GLN A 20  ? 1.4145  1.6563  1.6333  -0.0246 0.1384  -0.0339 29  GLN A CB  
261   C CG  . GLN A 20  ? 1.1208  1.4212  1.3775  -0.0273 0.1543  -0.0455 29  GLN A CG  
262   C CD  . GLN A 20  ? 1.0254  1.3699  1.2583  -0.0566 0.1685  -0.0264 29  GLN A CD  
263   O OE1 . GLN A 20  ? 0.7922  1.1385  0.9798  -0.0713 0.1734  -0.0194 29  GLN A OE1 
264   N NE2 . GLN A 20  ? 1.0928  1.4712  1.3553  -0.0678 0.1723  -0.0139 29  GLN A NE2 
273   N N   . GLU A 21  ? 0.8718  1.0596  1.1838  0.0341  0.1127  -0.0753 30  GLU A N   
274   C CA  . GLU A 21  ? 0.8751  1.0324  1.2203  0.0499  0.0913  -0.0681 30  GLU A CA  
275   C C   . GLU A 21  ? 0.8375  1.0281  1.2134  0.0437  0.0895  -0.0546 30  GLU A C   
276   O O   . GLU A 21  ? 0.7356  0.8984  1.1253  0.0490  0.0683  -0.0386 30  GLU A O   
277   C CB  . GLU A 21  ? 1.0697  1.2204  1.4557  0.0755  0.0877  -0.0988 30  GLU A CB  
278   C CG  . GLU A 21  ? 1.1093  1.2206  1.4740  0.0828  0.0851  -0.1138 30  GLU A CG  
279   C CD  . GLU A 21  ? 1.2266  1.3228  1.6396  0.1095  0.0757  -0.1408 30  GLU A CD  
280   O OE1 . GLU A 21  ? 1.1278  1.2213  1.5826  0.1229  0.0600  -0.1350 30  GLU A OE1 
281   O OE2 . GLU A 21  ? 1.3616  1.4474  1.7721  0.1168  0.0819  -0.1678 30  GLU A OE2 
288   N N   . ASN A 22  ? 0.9724  1.2224  1.3555  0.0292  0.1106  -0.0586 31  ASN A N   
289   C CA  . ASN A 22  ? 0.8455  1.1359  1.2674  0.0229  0.1110  -0.0508 31  ASN A CA  
290   C C   . ASN A 22  ? 0.8431  1.1632  1.2371  -0.0076 0.1239  -0.0288 31  ASN A C   
291   O O   . ASN A 22  ? 0.9455  1.2941  1.3117  -0.0210 0.1442  -0.0345 31  ASN A O   
292   C CB  . ASN A 22  ? 0.9450  1.2912  1.4252  0.0390  0.1253  -0.0847 31  ASN A CB  
293   C CG  . ASN A 22  ? 1.6109  1.9230  2.1254  0.0700  0.1076  -0.1033 31  ASN A CG  
294   O OD1 . ASN A 22  ? 1.5865  1.8695  2.1229  0.0796  0.0825  -0.0890 31  ASN A OD1 
295   N ND2 . ASN A 22  ? 0.9259  1.2376  1.4429  0.0848  0.1184  -0.1345 31  ASN A ND2 
302   N N   . LEU A 23  ? 1.0287  1.3413  1.4300  -0.0195 0.1104  -0.0036 32  LEU A N   
303   C CA  . LEU A 23  ? 0.9248  1.2638  1.3089  -0.0494 0.1193  0.0195  32  LEU A CA  
304   C C   . LEU A 23  ? 1.0601  1.4770  1.4880  -0.0586 0.1399  0.0069  32  LEU A C   
305   O O   . LEU A 23  ? 0.8620  1.3070  1.3436  -0.0396 0.1405  -0.0160 32  LEU A O   
306   C CB  . LEU A 23  ? 0.6592  0.9574  1.0373  -0.0593 0.0957  0.0488  32  LEU A CB  
307   C CG  . LEU A 23  ? 0.8054  1.0321  1.1413  -0.0532 0.0769  0.0619  32  LEU A CG  
308   C CD1 . LEU A 23  ? 0.8383  1.0298  1.1774  -0.0595 0.0536  0.0823  32  LEU A CD1 
309   C CD2 . LEU A 23  ? 0.4995  0.7167  0.7857  -0.0673 0.0867  0.0727  32  LEU A CD2 
321   N N   . PRO A 24  ? 0.8537  1.3091  1.2617  -0.0883 0.1569  0.0219  33  PRO A N   
322   C CA  . PRO A 24  ? 0.6988  1.2314  1.1493  -0.1030 0.1762  0.0152  33  PRO A CA  
323   C C   . PRO A 24  ? 0.5727  1.1052  1.0778  -0.0955 0.1574  0.0190  33  PRO A C   
324   O O   . PRO A 24  ? 0.6301  1.1031  1.1248  -0.0923 0.1300  0.0385  33  PRO A O   
325   C CB  . PRO A 24  ? 0.5201  1.0679  0.9303  -0.1421 0.1854  0.0471  33  PRO A CB  
326   C CG  . PRO A 24  ? 1.4123  1.9125  1.7597  -0.1417 0.1815  0.0553  33  PRO A CG  
327   C CD  . PRO A 24  ? 0.7515  1.1853  1.0987  -0.1104 0.1592  0.0458  33  PRO A CD  
335   N N   . ASP A 25  ? 0.8958  1.4997  1.4607  -0.0927 0.1724  -0.0018 34  ASP A N   
336   C CA  . ASP A 25  ? 0.8206  1.4323  1.4453  -0.0826 0.1530  -0.0022 34  ASP A CA  
337   C C   . ASP A 25  ? 0.5119  1.1054  1.1297  -0.1110 0.1356  0.0338  34  ASP A C   
338   O O   . ASP A 25  ? 0.6041  1.1774  1.2530  -0.1026 0.1100  0.0389  34  ASP A O   
339   C CB  . ASP A 25  ? 1.1675  1.8678  1.8634  -0.0749 0.1741  -0.0328 34  ASP A CB  
340   C CG  . ASP A 25  ? 1.5129  2.2177  2.2352  -0.0364 0.1801  -0.0735 34  ASP A CG  
341   O OD1 . ASP A 25  ? 1.5899  2.2223  2.2878  -0.0134 0.1586  -0.0740 34  ASP A OD1 
342   O OD2 . ASP A 25  ? 1.6375  2.4184  2.4084  -0.0294 0.2056  -0.1058 34  ASP A OD2 
347   N N   . PHE A 26  ? 0.6543  1.2467  1.2289  -0.1441 0.1450  0.0597  35  PHE A N   
348   C CA  . PHE A 26  ? 0.8127  1.3733  1.3785  -0.1692 0.1245  0.0931  35  PHE A CA  
349   C C   . PHE A 26  ? 0.9144  1.3928  1.4630  -0.1493 0.0912  0.0993  35  PHE A C   
350   O O   . PHE A 26  ? 0.4761  0.9397  1.0501  -0.1524 0.0686  0.1078  35  PHE A O   
351   C CB  . PHE A 26  ? 1.0117  1.5644  1.5238  -0.2016 0.1355  0.1205  35  PHE A CB  
352   C CG  . PHE A 26  ? 1.2169  1.7364  1.7188  -0.2305 0.1165  0.1551  35  PHE A CG  
353   C CD1 . PHE A 26  ? 0.9010  1.4720  1.4361  -0.2624 0.1233  0.1692  35  PHE A CD1 
354   C CD2 . PHE A 26  ? 0.7561  1.1932  1.2147  -0.2272 0.0928  0.1731  35  PHE A CD2 
355   C CE1 . PHE A 26  ? 0.9169  1.4526  1.4428  -0.2909 0.1045  0.2012  35  PHE A CE1 
356   C CE2 . PHE A 26  ? 0.7405  1.1433  1.1915  -0.2529 0.0746  0.2023  35  PHE A CE2 
357   C CZ  . PHE A 26  ? 0.6846  1.1346  1.1685  -0.2860 0.0798  0.2175  35  PHE A CZ  
367   N N   . TYR A 27  ? 0.7744  1.2049  1.2844  -0.1271 0.0882  0.0907  36  TYR A N   
368   C CA  . TYR A 27  ? 0.6854  1.0395  1.1686  -0.1145 0.0603  0.0997  36  TYR A CA  
369   C C   . TYR A 27  ? 0.6202  0.9610  1.1336  -0.0845 0.0435  0.0813  36  TYR A C   
370   O O   . TYR A 27  ? 0.7552  1.0364  1.2383  -0.0695 0.0267  0.0827  36  TYR A O   
371   C CB  . TYR A 27  ? 0.7383  1.0453  1.1630  -0.1105 0.0634  0.1048  36  TYR A CB  
372   C CG  . TYR A 27  ? 0.5754  0.8859  0.9662  -0.1397 0.0735  0.1281  36  TYR A CG  
373   C CD1 . TYR A 27  ? 0.5578  0.8349  0.9369  -0.1597 0.0570  0.1538  36  TYR A CD1 
374   C CD2 . TYR A 27  ? 0.9623  1.3084  1.3325  -0.1476 0.0976  0.1241  36  TYR A CD2 
375   C CE1 . TYR A 27  ? 0.7517  1.0275  1.1027  -0.1870 0.0622  0.1790  36  TYR A CE1 
376   C CE2 . TYR A 27  ? 0.7993  1.1480  1.1366  -0.1763 0.1034  0.1499  36  TYR A CE2 
377   C CZ  . TYR A 27  ? 0.9746  1.2859  1.3038  -0.1957 0.0844  0.1791  36  TYR A CZ  
378   O OH  . TYR A 27  ? 1.3496  1.6569  1.6487  -0.2246 0.0855  0.2087  36  TYR A OH  
388   N N   . ASN A 28  ? 0.4494  0.8453  1.0235  -0.0759 0.0464  0.0649  37  ASN A N   
389   C CA  . ASN A 28  ? 0.5963  0.9786  1.2024  -0.0462 0.0268  0.0496  37  ASN A CA  
390   C C   . ASN A 28  ? 0.5457  0.8718  1.1364  -0.0459 -0.0067 0.0658  37  ASN A C   
391   O O   . ASN A 28  ? 1.0284  1.3197  1.6186  -0.0231 -0.0259 0.0599  37  ASN A O   
392   C CB  . ASN A 28  ? 0.7271  1.1819  1.4092  -0.0386 0.0321  0.0316  37  ASN A CB  
393   C CG  . ASN A 28  ? 1.0106  1.5193  1.7138  -0.0285 0.0634  0.0049  37  ASN A CG  
394   O OD1 . ASN A 28  ? 1.2015  1.6853  1.8646  -0.0202 0.0758  -0.0036 37  ASN A OD1 
395   N ND2 . ASN A 28  ? 1.1937  1.7804  1.9614  -0.0298 0.0771  -0.0108 37  ASN A ND2 
402   N N   . ASP A 29  ? 0.8450  1.1584  1.4196  -0.0719 -0.0147 0.0861  38  ASP A N   
403   C CA  . ASP A 29  ? 0.8535  1.1198  1.4157  -0.0728 -0.0460 0.0968  38  ASP A CA  
404   C C   . ASP A 29  ? 0.7766  0.9723  1.2770  -0.0650 -0.0539 0.1019  38  ASP A C   
405   O O   . ASP A 29  ? 0.7842  0.9424  1.2720  -0.0529 -0.0765 0.1016  38  ASP A O   
406   C CB  . ASP A 29  ? 0.9731  1.2477  1.5429  -0.1034 -0.0533 0.1131  38  ASP A CB  
407   C CG  . ASP A 29  ? 0.9974  1.3386  1.6366  -0.1109 -0.0567 0.1086  38  ASP A CG  
408   O OD1 . ASP A 29  ? 0.8737  1.2444  1.5560  -0.0875 -0.0622 0.0927  38  ASP A OD1 
409   O OD2 . ASP A 29  ? 0.8799  1.2406  1.5328  -0.1402 -0.0572 0.1217  38  ASP A OD2 
414   N N   . TRP A 30  ? 0.8768  1.0574  1.3387  -0.0725 -0.0357 0.1069  39  TRP A N   
415   C CA  . TRP A 30  ? 0.5045  0.6265  0.9139  -0.0636 -0.0400 0.1091  39  TRP A CA  
416   C C   . TRP A 30  ? 0.5516  0.6648  0.9617  -0.0374 -0.0403 0.0944  39  TRP A C   
417   O O   . TRP A 30  ? 0.6340  0.7060  1.0243  -0.0265 -0.0584 0.0950  39  TRP A O   
418   C CB  . TRP A 30  ? 0.4893  0.6056  0.8658  -0.0756 -0.0211 0.1170  39  TRP A CB  
419   C CG  . TRP A 30  ? 0.4941  0.5996  0.8582  -0.1016 -0.0237 0.1360  39  TRP A CG  
420   C CD1 . TRP A 30  ? 0.5062  0.5963  0.8793  -0.1154 -0.0420 0.1447  39  TRP A CD1 
421   C CD2 . TRP A 30  ? 1.1072  1.2154  1.4492  -0.1170 -0.0093 0.1487  39  TRP A CD2 
422   N NE1 . TRP A 30  ? 0.7068  0.7854  1.0672  -0.1379 -0.0404 0.1619  39  TRP A NE1 
423   C CE2 . TRP A 30  ? 0.7776  0.8672  1.1184  -0.1392 -0.0211 0.1666  39  TRP A CE2 
424   C CE3 . TRP A 30  ? 0.4990  0.6216  0.8208  -0.1148 0.0101  0.1472  39  TRP A CE3 
425   C CZ2 . TRP A 30  ? 1.7852  1.8671  2.1065  -0.1586 -0.0156 0.1860  39  TRP A CZ2 
426   C CZ3 . TRP A 30  ? 0.6577  0.7761  0.9561  -0.1355 0.0157  0.1671  39  TRP A CZ3 
427   C CH2 . TRP A 30  ? 1.2573  1.3551  1.5571  -0.1564 0.0023  0.1873  39  TRP A CH2 
438   N N   . MET A 31  ? 0.5905  0.7448  1.0266  -0.0282 -0.0213 0.0804  40  MET A N   
439   C CA  . MET A 31  ? 0.8351  0.9783  1.2747  -0.0037 -0.0209 0.0647  40  MET A CA  
440   C C   . MET A 31  ? 0.8795  1.0036  1.3405  0.0121  -0.0482 0.0640  40  MET A C   
441   O O   . MET A 31  ? 1.1305  1.2159  1.5727  0.0271  -0.0576 0.0616  40  MET A O   
442   C CB  . MET A 31  ? 0.8018  0.9999  1.2767  0.0035  0.0026  0.0447  40  MET A CB  
443   C CG  . MET A 31  ? 0.9554  1.1337  1.4248  0.0261  0.0061  0.0270  40  MET A CG  
444   S SD  . MET A 31  ? 0.8228  0.9600  1.2241  0.0181  0.0183  0.0326  40  MET A SD  
445   C CE  . MET A 31  ? 1.3357  1.5344  1.7426  0.0066  0.0514  0.0194  40  MET A CE  
455   N N   . PHE A 32  ? 0.7090  0.8586  1.2076  0.0069  -0.0630 0.0683  41  PHE A N   
456   C CA  . PHE A 32  ? 0.6188  0.7570  1.1427  0.0222  -0.0919 0.0687  41  PHE A CA  
457   C C   . PHE A 32  ? 0.9066  0.9832  1.3779  0.0184  -0.1143 0.0834  41  PHE A C   
458   O O   . PHE A 32  ? 0.8100  0.8600  1.2801  0.0326  -0.1359 0.0859  41  PHE A O   
459   C CB  . PHE A 32  ? 0.4699  0.6566  1.0507  0.0165  -0.1034 0.0689  41  PHE A CB  
460   C CG  . PHE A 32  ? 0.4875  0.6540  1.0811  0.0259  -0.1400 0.0762  41  PHE A CG  
461   C CD1 . PHE A 32  ? 0.4985  0.6652  1.1272  0.0520  -0.1549 0.0684  41  PHE A CD1 
462   C CD2 . PHE A 32  ? 0.4990  0.6408  1.0653  0.0086  -0.1616 0.0910  41  PHE A CD2 
463   C CE1 . PHE A 32  ? 1.2472  1.3927  1.8836  0.0594  -0.1923 0.0794  41  PHE A CE1 
464   C CE2 . PHE A 32  ? 0.5212  0.6442  1.0914  0.0152  -0.1972 0.0989  41  PHE A CE2 
465   C CZ  . PHE A 32  ? 1.0077  1.1334  1.6127  0.0400  -0.2132 0.0951  41  PHE A CZ  
475   N N   . ILE A 33  ? 0.7490  0.8058  1.1812  -0.0017 -0.1119 0.0936  42  ILE A N   
476   C CA  . ILE A 33  ? 1.4025  1.4062  1.7820  -0.0069 -0.1279 0.1030  42  ILE A CA  
477   C C   . ILE A 33  ? 1.1740  1.1404  1.5121  0.0027  -0.1183 0.1014  42  ILE A C   
478   O O   . ILE A 33  ? 0.6287  0.5609  0.9414  0.0086  -0.1342 0.1062  42  ILE A O   
479   C CB  . ILE A 33  ? 1.0668  1.0628  1.4246  -0.0290 -0.1253 0.1093  42  ILE A CB  
480   C CG1 . ILE A 33  ? 0.5032  0.5325  0.9035  -0.0396 -0.1406 0.1116  42  ILE A CG1 
481   C CG2 . ILE A 33  ? 0.9683  0.9130  1.2693  -0.0336 -0.1336 0.1129  42  ILE A CG2 
482   C CD1 . ILE A 33  ? 0.5066  0.5364  0.9018  -0.0626 -0.1384 0.1170  42  ILE A CD1 
494   N N   . ALA A 34  ? 0.7825  0.7563  1.1115  0.0016  -0.0929 0.0961  43  ALA A N   
495   C CA  . ALA A 34  ? 0.7880  0.7309  1.0808  0.0080  -0.0833 0.0938  43  ALA A CA  
496   C C   . ALA A 34  ? 1.1875  1.1233  1.4970  0.0265  -0.0909 0.0879  43  ALA A C   
497   O O   . ALA A 34  ? 0.5829  0.4821  0.8613  0.0307  -0.0944 0.0904  43  ALA A O   
498   C CB  . ALA A 34  ? 0.9602  0.9216  1.2487  0.0035  -0.0574 0.0886  43  ALA A CB  
504   N N   . LYS A 35  ? 1.0341  1.0055  1.3963  0.0374  -0.0934 0.0794  44  LYS A N   
505   C CA  . LYS A 35  ? 0.5042  0.4641  0.8878  0.0572  -0.1036 0.0727  44  LYS A CA  
506   C C   . LYS A 35  ? 0.5301  0.4578  0.9067  0.0606  -0.1361 0.0873  44  LYS A C   
507   O O   . LYS A 35  ? 0.6267  0.5299  1.0110  0.0749  -0.1498 0.0879  44  LYS A O   
508   C CB  . LYS A 35  ? 0.7738  0.7820  1.2195  0.0715  -0.0949 0.0545  44  LYS A CB  
509   C CG  . LYS A 35  ? 0.6576  0.6921  1.1027  0.0706  -0.0628 0.0375  44  LYS A CG  
510   C CD  . LYS A 35  ? 1.2023  1.2051  1.6305  0.0825  -0.0579 0.0273  44  LYS A CD  
511   C CE  . LYS A 35  ? 1.1375  1.1675  1.5584  0.0791  -0.0271 0.0095  44  LYS A CE  
512   N NZ  . LYS A 35  ? 0.7663  0.7612  1.1642  0.0867  -0.0234 -0.0001 44  LYS A NZ  
526   N N   . HIS A 36  ? 0.6626  0.5846  1.0189  0.0462  -0.1498 0.0998  45  HIS A N   
527   C CA  . HIS A 36  ? 0.6628  0.5626  1.0145  0.0479  -0.1829 0.1135  45  HIS A CA  
528   C C   . HIS A 36  ? 1.1057  0.9753  1.3979  0.0289  -0.1906 0.1254  45  HIS A C   
529   O O   . HIS A 36  ? 1.2525  1.1171  1.5384  0.0226  -0.2165 0.1353  45  HIS A O   
530   C CB  . HIS A 36  ? 0.8124  0.7512  1.2208  0.0527  -0.2010 0.1125  45  HIS A CB  
531   C CG  . HIS A 36  ? 0.7524  0.7272  1.2279  0.0738  -0.1951 0.0973  45  HIS A CG  
532   N ND1 . HIS A 36  ? 0.8512  0.8753  1.3626  0.0735  -0.1679 0.0807  45  HIS A ND1 
533   C CD2 . HIS A 36  ? 0.5776  0.5453  1.0900  0.0961  -0.2118 0.0944  45  HIS A CD2 
534   C CE1 . HIS A 36  ? 1.3116  1.3628  1.8807  0.0953  -0.1664 0.0650  45  HIS A CE1 
535   N NE2 . HIS A 36  ? 1.1024  1.1181  1.6762  0.1108  -0.1939 0.0723  45  HIS A NE2 
543   N N   . LEU A 37  ? 0.8419  0.6944  1.0916  0.0196  -0.1693 0.1228  46  LEU A N   
544   C CA  . LEU A 37  ? 0.7007  0.5266  0.8965  0.0035  -0.1747 0.1294  46  LEU A CA  
545   C C   . LEU A 37  ? 0.8997  0.6961  1.0657  0.0016  -0.2004 0.1433  46  LEU A C   
546   O O   . LEU A 37  ? 1.1380  0.9284  1.2791  -0.0107 -0.2177 0.1486  46  LEU A O   
547   C CB  . LEU A 37  ? 0.9894  0.8010  1.1507  -0.0015 -0.1486 0.1238  46  LEU A CB  
548   C CG  . LEU A 37  ? 0.7797  0.6177  0.9628  -0.0032 -0.1266 0.1145  46  LEU A CG  
549   C CD1 . LEU A 37  ? 0.6533  0.4768  0.8067  -0.0046 -0.1045 0.1104  46  LEU A CD1 
550   C CD2 . LEU A 37  ? 0.5401  0.3866  0.7237  -0.0169 -0.1325 0.1145  46  LEU A CD2 
562   N N   . PRO A 38  ? 0.9585  0.7358  1.1257  0.0117  -0.2064 0.1501  47  PRO A N   
563   C CA  . PRO A 38  ? 1.5037  1.2513  1.6395  0.0065  -0.2337 0.1684  47  PRO A CA  
564   C C   . PRO A 38  ? 1.0609  0.8205  1.2155  0.0059  -0.2654 0.1771  47  PRO A C   
565   O O   . PRO A 38  ? 1.3573  1.1050  1.4687  -0.0098 -0.2818 0.1862  47  PRO A O   
566   C CB  . PRO A 38  ? 0.6934  0.4225  0.8488  0.0209  -0.2369 0.1733  47  PRO A CB  
567   C CG  . PRO A 38  ? 0.6535  0.3942  0.8213  0.0269  -0.2014 0.1546  47  PRO A CG  
568   C CD  . PRO A 38  ? 0.6241  0.4019  0.8133  0.0249  -0.1874 0.1415  47  PRO A CD  
576   N N   . ASP A 39  ? 0.9244  0.7120  1.1442  0.0222  -0.2740 0.1722  48  ASP A N   
577   C CA  . ASP A 39  ? 0.9705  0.7738  1.2181  0.0235  -0.3076 0.1808  48  ASP A CA  
578   C C   . ASP A 39  ? 0.9886  0.8099  1.2193  0.0052  -0.3083 0.1755  48  ASP A C   
579   O O   . ASP A 39  ? 1.1334  0.9450  1.3336  -0.0075 -0.3348 0.1863  48  ASP A O   
580   C CB  . ASP A 39  ? 1.0309  0.8680  1.3604  0.0464  -0.3111 0.1718  48  ASP A CB  
581   C CG  . ASP A 39  ? 1.2395  1.0563  1.5879  0.0655  -0.3061 0.1704  48  ASP A CG  
582   O OD1 . ASP A 39  ? 1.2950  1.0675  1.6011  0.0615  -0.3189 0.1868  48  ASP A OD1 
583   O OD2 . ASP A 39  ? 1.8037  1.6485  2.2067  0.0824  -0.2889 0.1521  48  ASP A OD2 
588   N N   . LEU A 40  ? 0.9795  0.8227  1.2229  0.0013  -0.2795 0.1594  49  LEU A N   
589   C CA  . LEU A 40  ? 0.7752  0.6329  1.0109  -0.0158 -0.2809 0.1533  49  LEU A CA  
590   C C   . LEU A 40  ? 1.0572  0.8823  1.2209  -0.0338 -0.2826 0.1545  49  LEU A C   
591   O O   . LEU A 40  ? 0.7129  0.5406  0.8614  -0.0486 -0.2974 0.1518  49  LEU A O   
592   C CB  . LEU A 40  ? 0.6263  0.5093  0.8897  -0.0172 -0.2506 0.1396  49  LEU A CB  
593   C CG  . LEU A 40  ? 0.7350  0.6608  1.0707  -0.0025 -0.2458 0.1346  49  LEU A CG  
594   C CD1 . LEU A 40  ? 0.5694  0.5200  0.9226  -0.0080 -0.2152 0.1243  49  LEU A CD1 
595   C CD2 . LEU A 40  ? 0.6160  0.5703  0.9961  -0.0019 -0.2746 0.1385  49  LEU A CD2 
607   N N   . ILE A 41  ? 0.6977  0.4948  0.8178  -0.0338 -0.2663 0.1559  50  ILE A N   
608   C CA  . ILE A 41  ? 0.7288  0.5006  0.7817  -0.0506 -0.2673 0.1552  50  ILE A CA  
609   C C   . ILE A 41  ? 0.7796  0.5392  0.8035  -0.0582 -0.3018 0.1714  50  ILE A C   
610   O O   . ILE A 41  ? 0.8903  0.6497  0.8847  -0.0735 -0.3177 0.1683  50  ILE A O   
611   C CB  . ILE A 41  ? 0.7751  0.5264  0.7944  -0.0493 -0.2404 0.1531  50  ILE A CB  
612   C CG1 . ILE A 41  ? 0.6774  0.4410  0.7180  -0.0456 -0.2106 0.1374  50  ILE A CG1 
613   C CG2 . ILE A 41  ? 0.9097  0.6387  0.8588  -0.0661 -0.2398 0.1529  50  ILE A CG2 
614   C CD1 . ILE A 41  ? 0.6637  0.4137  0.6838  -0.0420 -0.1852 0.1348  50  ILE A CD1 
626   N N   . GLU A 42  ? 1.1706  0.9189  1.2033  -0.0479 -0.3160 0.1890  51  GLU A N   
627   C CA  . GLU A 42  ? 0.9127  0.6436  0.9087  -0.0574 -0.3497 0.2095  51  GLU A CA  
628   C C   . GLU A 42  ? 0.9705  0.7224  0.9896  -0.0611 -0.3819 0.2116  51  GLU A C   
629   O O   . GLU A 42  ? 0.9183  0.6612  0.8915  -0.0774 -0.4082 0.2219  51  GLU A O   
630   C CB  . GLU A 42  ? 1.2385  0.9502  1.2501  -0.0442 -0.3616 0.2293  51  GLU A CB  
631   C CG  . GLU A 42  ? 1.5412  1.2236  1.5025  -0.0520 -0.3415 0.2349  51  GLU A CG  
632   C CD  . GLU A 42  ? 1.8457  1.4977  1.7924  -0.0523 -0.3695 0.2642  51  GLU A CD  
633   O OE1 . GLU A 42  ? 1.8946  1.5445  1.8989  -0.0317 -0.3852 0.2713  51  GLU A OE1 
634   O OE2 . GLU A 42  ? 1.9444  1.5756  1.8234  -0.0738 -0.3769 0.2800  51  GLU A OE2 
641   N N   . SER A 43  ? 0.8934  0.6766  0.9827  -0.0480 -0.3805 0.2020  52  SER A N   
642   C CA  . SER A 43  ? 1.0983  0.9072  1.2159  -0.0535 -0.4093 0.2018  52  SER A CA  
643   C C   . SER A 43  ? 1.2078  1.0163  1.2824  -0.0761 -0.4042 0.1863  52  SER A C   
644   O O   . SER A 43  ? 1.2749  1.0854  1.3264  -0.0906 -0.4345 0.1902  52  SER A O   
645   C CB  . SER A 43  ? 1.0169  0.8656  1.2216  -0.0368 -0.4030 0.1927  52  SER A CB  
646   O OG  . SER A 43  ? 1.0592  0.9348  1.2828  -0.0500 -0.4134 0.1834  52  SER A OG  
652   N N   . GLY A 44  ? 0.9095  0.7125  0.9703  -0.0794 -0.3679 0.1684  53  GLY A N   
653   C CA  . GLY A 44  ? 1.1017  0.9033  1.1360  -0.0971 -0.3617 0.1498  53  GLY A CA  
654   C C   . GLY A 44  ? 1.1288  0.9590  1.2247  -0.0965 -0.3570 0.1395  53  GLY A C   
655   O O   . GLY A 44  ? 1.2471  1.0813  1.3386  -0.1123 -0.3676 0.1281  53  GLY A O   
659   N N   . GLN A 45  ? 1.6227  1.4750  1.7770  -0.0802 -0.3436 0.1433  54  GLN A N   
660   C CA  . GLN A 45  ? 0.8133  0.6991  1.0281  -0.0817 -0.3362 0.1360  54  GLN A CA  
661   C C   . GLN A 45  ? 0.8404  0.7281  1.0690  -0.0747 -0.2983 0.1295  54  GLN A C   
662   O O   . GLN A 45  ? 1.0487  0.9697  1.3322  -0.0716 -0.2874 0.1279  54  GLN A O   
663   C CB  . GLN A 45  ? 1.4789  1.4031  1.7596  -0.0713 -0.3587 0.1451  54  GLN A CB  
664   C CG  . GLN A 45  ? 1.8867  1.8146  2.1590  -0.0831 -0.4005 0.1510  54  GLN A CG  
665   C CD  . GLN A 45  ? 2.1709  2.1450  2.5198  -0.0754 -0.4246 0.1569  54  GLN A CD  
666   O OE1 . GLN A 45  ? 2.1020  2.0986  2.5030  -0.0545 -0.4177 0.1605  54  GLN A OE1 
667   N NE2 . GLN A 45  ? 2.4499  2.4403  2.8084  -0.0920 -0.4533 0.1556  54  GLN A NE2 
676   N N   . LEU A 46  ? 1.2191  1.0756  1.3996  -0.0721 -0.2781 0.1266  55  LEU A N   
677   C CA  . LEU A 46  ? 0.9978  0.8554  1.1877  -0.0673 -0.2449 0.1208  55  LEU A CA  
678   C C   . LEU A 46  ? 0.9468  0.8047  1.1417  -0.0827 -0.2369 0.1114  55  LEU A C   
679   O O   . LEU A 46  ? 0.9208  0.8008  1.1541  -0.0839 -0.2218 0.1119  55  LEU A O   
680   C CB  . LEU A 46  ? 0.7499  0.5765  0.8904  -0.0617 -0.2280 0.1199  55  LEU A CB  
681   C CG  . LEU A 46  ? 0.8862  0.7136  1.0338  -0.0542 -0.1959 0.1159  55  LEU A CG  
682   C CD1 . LEU A 46  ? 0.8076  0.6208  0.9363  -0.0644 -0.1818 0.1059  55  LEU A CD1 
683   C CD2 . LEU A 46  ? 1.1919  1.0550  1.3969  -0.0463 -0.1864 0.1180  55  LEU A CD2 
695   N N   . ARG A 47  ? 0.9290  0.7622  1.0853  -0.0958 -0.2474 0.1025  56  ARG A N   
696   C CA  . ARG A 47  ? 0.9724  0.7986  1.1362  -0.1098 -0.2426 0.0928  56  ARG A CA  
697   C C   . ARG A 47  ? 1.1627  1.0205  1.3798  -0.1211 -0.2571 0.0972  56  ARG A C   
698   O O   . ARG A 47  ? 1.1231  0.9894  1.3693  -0.1297 -0.2456 0.0982  56  ARG A O   
699   C CB  . ARG A 47  ? 0.8744  0.6670  0.9860  -0.1195 -0.2510 0.0773  56  ARG A CB  
700   C CG  . ARG A 47  ? 1.0250  0.7954  1.0945  -0.1094 -0.2304 0.0726  56  ARG A CG  
701   C CD  . ARG A 47  ? 1.1307  0.8767  1.1453  -0.1174 -0.2374 0.0562  56  ARG A CD  
702   N NE  . ARG A 47  ? 1.0740  0.8029  1.0561  -0.1095 -0.2132 0.0479  56  ARG A NE  
703   C CZ  . ARG A 47  ? 1.1056  0.8203  1.0359  -0.1136 -0.2112 0.0346  56  ARG A CZ  
704   N NH1 . ARG A 47  ? 1.3319  1.0448  1.2294  -0.1263 -0.2326 0.0286  56  ARG A NH1 
705   N NH2 . ARG A 47  ? 0.7848  0.4908  0.6961  -0.1062 -0.1876 0.0267  56  ARG A NH2 
719   N N   . GLU A 48  ? 0.9932  0.8721  1.2273  -0.1214 -0.2823 0.1023  57  GLU A N   
720   C CA  . GLU A 48  ? 0.8908  0.8079  1.1828  -0.1315 -0.2958 0.1063  57  GLU A CA  
721   C C   . GLU A 48  ? 0.8853  0.8376  1.2282  -0.1258 -0.2713 0.1132  57  GLU A C   
722   O O   . GLU A 48  ? 1.1306  1.1047  1.5102  -0.1414 -0.2675 0.1146  57  GLU A O   
723   C CB  . GLU A 48  ? 1.4057  1.3449  1.7144  -0.1269 -0.3267 0.1127  57  GLU A CB  
724   C CG  . GLU A 48  ? 1.7571  1.6746  2.0244  -0.1408 -0.3577 0.1068  57  GLU A CG  
725   C CD  . GLU A 48  ? 1.0943  1.0255  1.3644  -0.1325 -0.3884 0.1180  57  GLU A CD  
732   N N   . ARG A 49  ? 0.8398  0.7986  1.1839  -0.1056 -0.2542 0.1171  58  ARG A N   
733   C CA  . ARG A 49  ? 0.8277  0.8264  1.2193  -0.1004 -0.2314 0.1204  58  ARG A CA  
734   C C   . ARG A 49  ? 0.8667  0.8532  1.2456  -0.1120 -0.2073 0.1210  58  ARG A C   
735   O O   . ARG A 49  ? 1.2741  1.2917  1.6900  -0.1256 -0.1976 0.1254  58  ARG A O   
736   C CB  . ARG A 49  ? 0.9319  0.9374  1.3273  -0.0758 -0.2203 0.1209  58  ARG A CB  
737   C CG  . ARG A 49  ? 0.8127  0.8400  1.2416  -0.0612 -0.2442 0.1231  58  ARG A CG  
738   C CD  . ARG A 49  ? 0.8560  0.9414  1.3572  -0.0645 -0.2516 0.1221  58  ARG A CD  
739   N NE  . ARG A 49  ? 1.3149  1.4028  1.8229  -0.0780 -0.2853 0.1252  58  ARG A NE  
740   C CZ  . ARG A 49  ? 1.4368  1.5723  2.0026  -0.0893 -0.2959 0.1248  58  ARG A CZ  
741   N NH1 . ARG A 49  ? 1.4544  1.6415  2.0759  -0.0892 -0.2731 0.1214  58  ARG A NH1 
742   N NH2 . ARG A 49  ? 1.3577  1.4923  1.9250  -0.1027 -0.3290 0.1269  58  ARG A NH2 
756   N N   . VAL A 50  ? 0.8274  0.7696  1.1550  -0.1084 -0.1991 0.1176  59  VAL A N   
757   C CA  . VAL A 50  ? 1.2519  1.1787  1.5677  -0.1164 -0.1792 0.1196  59  VAL A CA  
758   C C   . VAL A 50  ? 0.8375  0.7598  1.1686  -0.1401 -0.1896 0.1214  59  VAL A C   
759   O O   . VAL A 50  ? 1.0864  1.0222  1.4387  -0.1527 -0.1770 0.1305  59  VAL A O   
760   C CB  . VAL A 50  ? 0.9633  0.8448  1.2255  -0.1068 -0.1722 0.1131  59  VAL A CB  
761   C CG1 . VAL A 50  ? 0.8059  0.6649  1.0574  -0.1152 -0.1598 0.1144  59  VAL A CG1 
762   C CG2 . VAL A 50  ? 1.1428  1.0310  1.3961  -0.0874 -0.1589 0.1141  59  VAL A CG2 
772   N N   . GLU A 51  ? 0.8334  0.7352  1.1515  -0.1485 -0.2136 0.1133  60  GLU A N   
773   C CA  . GLU A 51  ? 1.4337  1.3229  1.7641  -0.1718 -0.2257 0.1122  60  GLU A CA  
774   C C   . GLU A 51  ? 1.2069  1.1449  1.5949  -0.1883 -0.2280 0.1234  60  GLU A C   
775   O O   . GLU A 51  ? 1.3923  1.3255  1.7980  -0.2103 -0.2292 0.1295  60  GLU A O   
776   C CB  . GLU A 51  ? 0.6840  0.5441  0.9853  -0.1765 -0.2513 0.0972  60  GLU A CB  
777   C CG  . GLU A 51  ? 0.6978  0.5119  0.9460  -0.1666 -0.2450 0.0841  60  GLU A CG  
778   C CD  . GLU A 51  ? 1.1925  0.9885  1.4017  -0.1661 -0.2647 0.0689  60  GLU A CD  
779   O OE1 . GLU A 51  ? 1.8427  1.6588  2.0672  -0.1754 -0.2882 0.0696  60  GLU A OE1 
780   O OE2 . GLU A 51  ? 1.1478  0.9115  1.3113  -0.1582 -0.2573 0.0556  60  GLU A OE2 
787   N N   . LYS A 52  ? 1.1809  1.1665  1.6010  -0.1777 -0.2267 0.1266  61  LYS A N   
788   C CA  . LYS A 52  ? 1.0007  1.0444  1.4817  -0.1905 -0.2257 0.1344  61  LYS A CA  
789   C C   . LYS A 52  ? 1.5026  1.5833  2.0052  -0.1872 -0.1941 0.1429  61  LYS A C   
790   O O   . LYS A 52  ? 0.5684  0.7086  1.1222  -0.1893 -0.1878 0.1449  61  LYS A O   
791   C CB  . LYS A 52  ? 1.2104  1.2879  1.7204  -0.1792 -0.2462 0.1296  61  LYS A CB  
792   C CG  . LYS A 52  ? 1.5224  1.5768  2.0186  -0.1903 -0.2806 0.1230  61  LYS A CG  
793   C CD  . LYS A 52  ? 1.6385  1.7323  2.1712  -0.1814 -0.3051 0.1224  61  LYS A CD  
794   C CE  . LYS A 52  ? 1.8213  1.9038  2.3495  -0.2003 -0.3405 0.1172  61  LYS A CE  
795   N NZ  . LYS A 52  ? 1.9996  2.1215  2.5650  -0.1922 -0.3687 0.1189  61  LYS A NZ  
809   N N   . LEU A 53  ? 0.6571  0.7084  1.1242  -0.1834 -0.1744 0.1468  62  LEU A N   
810   C CA  . LEU A 53  ? 0.5566  0.6445  1.0395  -0.1848 -0.1459 0.1552  62  LEU A CA  
811   C C   . LEU A 53  ? 0.9307  1.0171  1.4192  -0.2142 -0.1391 0.1713  62  LEU A C   
812   O O   . LEU A 53  ? 1.7252  1.7615  2.1909  -0.2266 -0.1525 0.1750  62  LEU A O   
813   C CB  . LEU A 53  ? 0.7460  0.8082  1.1878  -0.1635 -0.1289 0.1519  62  LEU A CB  
814   C CG  . LEU A 53  ? 0.7766  0.8335  1.2033  -0.1341 -0.1279 0.1400  62  LEU A CG  
815   C CD1 . LEU A 53  ? 0.6363  0.6579  1.0178  -0.1254 -0.1116 0.1411  62  LEU A CD1 
816   C CD2 . LEU A 53  ? 0.9188  1.0338  1.3888  -0.1220 -0.1159 0.1344  62  LEU A CD2 
828   N N   . ASN A 54  ? 1.0303  1.1703  1.5468  -0.2248 -0.1170 0.1804  63  ASN A N   
829   C CA  . ASN A 54  ? 1.2234  1.3633  1.7395  -0.2545 -0.1082 0.2009  63  ASN A CA  
830   C C   . ASN A 54  ? 1.1938  1.2997  1.6642  -0.2473 -0.0934 0.2088  63  ASN A C   
831   O O   . ASN A 54  ? 1.6842  1.7915  2.1338  -0.2224 -0.0803 0.1986  63  ASN A O   
832   C CB  . ASN A 54  ? 1.1989  1.4167  1.7612  -0.2750 -0.0891 0.2096  63  ASN A CB  
833   C CG  . ASN A 54  ? 0.9065  1.1690  1.5246  -0.2849 -0.1034 0.2031  63  ASN A CG  
834   O OD1 . ASN A 54  ? 0.6192  0.9535  1.2819  -0.2825 -0.0887 0.1961  63  ASN A OD1 
835   N ND2 . ASN A 54  ? 1.0733  1.2962  1.6915  -0.2948 -0.1324 0.2026  63  ASN A ND2 
842   N N   . MET A 55  ? 1.3543  1.4308  1.8125  -0.2711 -0.0971 0.2287  64  MET A N   
843   C CA  . MET A 55  ? 1.3047  1.3516  1.7245  -0.2673 -0.0866 0.2401  64  MET A CA  
844   C C   . MET A 55  ? 1.4743  1.5816  1.8989  -0.2745 -0.0586 0.2492  64  MET A C   
845   O O   . MET A 55  ? 1.2910  1.4291  1.7303  -0.3053 -0.0511 0.2701  64  MET A O   
846   C CB  . MET A 55  ? 1.3051  1.3010  1.7147  -0.2904 -0.1021 0.2608  64  MET A CB  
847   C CG  . MET A 55  ? 1.1065  1.0691  1.4781  -0.2809 -0.0958 0.2708  64  MET A CG  
848   S SD  . MET A 55  ? 1.0361  0.9313  1.3921  -0.2951 -0.1170 0.2883  64  MET A SD  
849   C CE  . MET A 55  ? 1.0486  0.8871  1.4072  -0.2781 -0.1420 0.2599  64  MET A CE  
859   N N   . LEU A 56  ? 1.2186  1.3417  1.6281  -0.2478 -0.0432 0.2333  65  LEU A N   
860   C CA  . LEU A 56  ? 1.0220  1.2005  1.4309  -0.2526 -0.0158 0.2367  65  LEU A CA  
861   C C   . LEU A 56  ? 1.1498  1.3004  1.5170  -0.2619 -0.0112 0.2569  65  LEU A C   
862   O O   . LEU A 56  ? 1.1636  1.2514  1.5039  -0.2538 -0.0274 0.2619  65  LEU A O   
863   C CB  . LEU A 56  ? 1.1904  1.3949  1.6015  -0.2210 -0.0022 0.2100  65  LEU A CB  
864   C CG  . LEU A 56  ? 1.3362  1.5678  1.7895  -0.2060 -0.0091 0.1896  65  LEU A CG  
865   C CD1 . LEU A 56  ? 1.2041  1.4655  1.6622  -0.1778 0.0076  0.1664  65  LEU A CD1 
866   C CD2 . LEU A 56  ? 0.5329  0.8191  1.0357  -0.2316 -0.0077 0.1964  65  LEU A CD2 
878   N N   . SER A 57  ? 1.2252  1.4273  1.5888  -0.2793 0.0111  0.2677  66  SER A N   
879   C CA  . SER A 57  ? 0.7871  0.9761  1.1104  -0.2910 0.0167  0.2891  66  SER A CA  
880   C C   . SER A 57  ? 0.9636  1.1547  1.2575  -0.2634 0.0299  0.2705  66  SER A C   
881   O O   . SER A 57  ? 0.9791  1.2062  1.2877  -0.2433 0.0444  0.2431  66  SER A O   
882   C CB  . SER A 57  ? 0.7769  1.0260  1.1062  -0.3282 0.0349  0.3108  66  SER A CB  
883   O OG  . SER A 57  ? 0.9286  1.1686  1.2150  -0.3414 0.0390  0.3339  66  SER A OG  
889   N N   . ILE A 58  ? 0.8381  0.9906  1.0931  -0.2633 0.0231  0.2861  67  ILE A N   
890   C CA  . ILE A 58  ? 1.0476  1.2042  1.2722  -0.2430 0.0347  0.2721  67  ILE A CA  
891   C C   . ILE A 58  ? 1.3022  1.5138  1.5063  -0.2644 0.0564  0.2830  67  ILE A C   
892   O O   . ILE A 58  ? 1.3403  1.5634  1.5174  -0.2524 0.0675  0.2712  67  ILE A O   
893   C CB  . ILE A 58  ? 1.1532  1.2459  1.3478  -0.2294 0.0162  0.2801  67  ILE A CB  
894   C CG1 . ILE A 58  ? 0.6741  0.7454  0.8507  -0.2558 0.0035  0.3176  67  ILE A CG1 
895   C CG2 . ILE A 58  ? 0.5929  0.6344  0.8018  -0.2108 -0.0029 0.2684  67  ILE A CG2 
896   C CD1 . ILE A 58  ? 1.4281  1.5123  1.5674  -0.2617 0.0097  0.3309  67  ILE A CD1 
908   N N   . ASP A 59  ? 1.5908  1.8391  1.8054  -0.2979 0.0632  0.3044  68  ASP A N   
909   C CA  . ASP A 59  ? 1.3927  1.6894  1.5787  -0.3244 0.0817  0.3208  68  ASP A CA  
910   C C   . ASP A 59  ? 1.7917  2.1622  1.9856  -0.3163 0.1138  0.2881  68  ASP A C   
911   O O   . ASP A 59  ? 0.9370  1.3547  1.1026  -0.3355 0.1332  0.2936  68  ASP A O   
912   C CB  . ASP A 59  ? 1.3761  1.6788  1.5657  -0.3600 0.0759  0.3515  68  ASP A CB  
913   C CG  . ASP A 59  ? 1.2855  1.5049  1.4677  -0.3581 0.0410  0.3729  68  ASP A CG  
914   O OD1 . ASP A 59  ? 1.3436  1.5086  1.5195  -0.3353 0.0241  0.3694  68  ASP A OD1 
915   O OD2 . ASP A 59  ? 1.3692  1.5794  1.5536  -0.3790 0.0312  0.3911  68  ASP A OD2 
920   N N   . HIS A 60  ? 1.3926  1.7763  1.6255  -0.2897 0.1192  0.2541  69  HIS A N   
921   C CA  . HIS A 60  ? 1.2339  1.6789  1.4787  -0.2752 0.1467  0.2182  69  HIS A CA  
922   C C   . HIS A 60  ? 1.7413  2.1535  1.9658  -0.2404 0.1441  0.1922  69  HIS A C   
923   O O   . HIS A 60  ? 0.9167  1.3619  1.1602  -0.2192 0.1602  0.1567  69  HIS A O   
924   C CB  . HIS A 60  ? 1.2253  1.7108  1.5309  -0.2661 0.1540  0.1954  69  HIS A CB  
925   C CG  . HIS A 60  ? 1.0771  1.6050  1.4099  -0.3016 0.1590  0.2172  69  HIS A CG  
926   N ND1 . HIS A 60  ? 1.0120  1.5035  1.3687  -0.3113 0.1351  0.2370  69  HIS A ND1 
927   C CD2 . HIS A 60  ? 1.1262  1.7306  1.4643  -0.3328 0.1853  0.2228  69  HIS A CD2 
928   C CE1 . HIS A 60  ? 1.2368  1.7786  1.6157  -0.3469 0.1452  0.2547  69  HIS A CE1 
929   N NE2 . HIS A 60  ? 1.4329  2.0456  1.8008  -0.3612 0.1766  0.2475  69  HIS A NE2 
937   N N   . LEU A 61  ? 1.3282  1.6753  1.5199  -0.2333 0.1229  0.2080  70  LEU A N   
938   C CA  . LEU A 61  ? 1.2157  1.5340  1.3847  -0.2063 0.1205  0.1878  70  LEU A CA  
939   C C   . LEU A 61  ? 1.3019  1.6340  1.4224  -0.2233 0.1275  0.2011  70  LEU A C   
940   O O   . LEU A 61  ? 1.5238  1.8177  1.6161  -0.2348 0.1096  0.2312  70  LEU A O   
941   C CB  . LEU A 61  ? 0.9630  1.2080  1.1314  -0.1873 0.0939  0.1936  70  LEU A CB  
942   C CG  . LEU A 61  ? 0.7489  0.9819  0.9595  -0.1744 0.0848  0.1828  70  LEU A CG  
943   C CD1 . LEU A 61  ? 1.2679  1.4336  1.4728  -0.1624 0.0600  0.1909  70  LEU A CD1 
944   C CD2 . LEU A 61  ? 0.5166  0.7758  0.7519  -0.1503 0.0971  0.1478  70  LEU A CD2 
956   N N   . THR A 62  ? 1.3594  1.7469  1.4716  -0.2241 0.1523  0.1769  71  THR A N   
957   C CA  . THR A 62  ? 1.2113  1.6293  1.2757  -0.2475 0.1628  0.1890  71  THR A CA  
958   C C   . THR A 62  ? 1.1091  1.4995  1.1391  -0.2304 0.1563  0.1758  71  THR A C   
959   O O   . THR A 62  ? 1.8619  2.2217  1.8559  -0.2404 0.1391  0.2031  71  THR A O   
960   C CB  . THR A 62  ? 1.1534  1.6552  1.2263  -0.2614 0.1962  0.1667  71  THR A CB  
961   O OG1 . THR A 62  ? 1.0641  1.5807  1.1686  -0.2293 0.2092  0.1190  71  THR A OG1 
962   C CG2 . THR A 62  ? 0.9617  1.4947  1.0678  -0.2838 0.2016  0.1848  71  THR A CG2 
970   N N   . ASP A 63  ? 0.8414  1.2420  0.8858  -0.2048 0.1682  0.1344  72  ASP A N   
971   C CA  . ASP A 63  ? 0.8945  1.2771  0.9075  -0.1925 0.1647  0.1190  72  ASP A CA  
972   C C   . ASP A 63  ? 1.2501  1.5613  1.2672  -0.1726 0.1380  0.1292  72  ASP A C   
973   O O   . ASP A 63  ? 0.8452  1.1236  0.8938  -0.1614 0.1262  0.1355  72  ASP A O   
974   C CB  . ASP A 63  ? 1.0712  1.4856  1.1003  -0.1727 0.1856  0.0695  72  ASP A CB  
975   C CG  . ASP A 63  ? 1.0903  1.4853  1.1737  -0.1441 0.1831  0.0470  72  ASP A CG  
980   N N   . HIS A 64  ? 0.9954  1.2860  0.9799  -0.1695 0.1285  0.1300  73  HIS A N   
981   C CA  . HIS A 64  ? 0.7352  0.9650  0.7252  -0.1515 0.1058  0.1375  73  HIS A CA  
982   C C   . HIS A 64  ? 0.8184  1.0257  0.8447  -0.1248 0.1069  0.1106  73  HIS A C   
983   O O   . HIS A 64  ? 0.5398  0.7072  0.5852  -0.1149 0.0923  0.1209  73  HIS A O   
984   C CB  . HIS A 64  ? 0.9480  1.1680  0.9037  -0.1510 0.0976  0.1363  73  HIS A CB  
985   C CG  . HIS A 64  ? 1.0506  1.2171  1.0152  -0.1323 0.0780  0.1388  73  HIS A CG  
986   N ND1 . HIS A 64  ? 1.2968  1.4261  1.2682  -0.1327 0.0580  0.1675  73  HIS A ND1 
987   C CD2 . HIS A 64  ? 0.9758  1.1210  0.9466  -0.1129 0.0763  0.1145  73  HIS A CD2 
988   C CE1 . HIS A 64  ? 0.7963  0.8890  0.7770  -0.1141 0.0471  0.1590  73  HIS A CE1 
989   N NE2 . HIS A 64  ? 0.7826  0.8839  0.7622  -0.1033 0.0577  0.1291  73  HIS A NE2 
997   N N   . LYS A 65  ? 0.9454  1.1784  0.9823  -0.1136 0.1234  0.0758  74  LYS A N   
998   C CA  . LYS A 65  ? 0.8546  1.0609  0.9245  -0.0882 0.1202  0.0531  74  LYS A CA  
999   C C   . LYS A 65  ? 0.9339  1.1401  1.0411  -0.0849 0.1178  0.0603  74  LYS A C   
1000  O O   . LYS A 65  ? 0.9442  1.1092  1.0678  -0.0708 0.1031  0.0633  74  LYS A O   
1001  C CB  . LYS A 65  ? 1.3024  1.5334  1.3806  -0.0761 0.1361  0.0137  74  LYS A CB  
1002  C CG  . LYS A 65  ? 1.3503  1.5738  1.3951  -0.0767 0.1353  0.0013  74  LYS A CG  
1003  C CD  . LYS A 65  ? 0.9811  1.2199  1.0404  -0.0621 0.1487  -0.0423 74  LYS A CD  
1004  C CE  . LYS A 65  ? 1.1182  1.3528  1.1438  -0.0655 0.1479  -0.0581 74  LYS A CE  
1005  N NZ  . LYS A 65  ? 1.1346  1.3833  1.1750  -0.0524 0.1610  -0.1038 74  LYS A NZ  
1019  N N   . SER A 66  ? 0.9548  1.2078  1.0741  -0.1006 0.1311  0.0651  75  SER A N   
1020  C CA  . SER A 66  ? 1.4234  1.6767  1.5814  -0.0984 0.1262  0.0718  75  SER A CA  
1021  C C   . SER A 66  ? 1.2770  1.4836  1.4273  -0.1049 0.1044  0.1033  75  SER A C   
1022  O O   . SER A 66  ? 0.5439  0.7247  0.7195  -0.0946 0.0918  0.1045  75  SER A O   
1023  C CB  . SER A 66  ? 1.0144  1.3312  1.1891  -0.1172 0.1451  0.0721  75  SER A CB  
1024  O OG  . SER A 66  ? 1.1986  1.5270  1.3392  -0.1458 0.1462  0.1017  75  SER A OG  
1030  N N   . GLN A 67  ? 0.7578  0.9509  0.8735  -0.1203 0.0978  0.1269  76  GLN A N   
1031  C CA  . GLN A 67  ? 0.6279  0.7710  0.7371  -0.1220 0.0761  0.1516  76  GLN A CA  
1032  C C   . GLN A 67  ? 0.7096  0.8063  0.8184  -0.0984 0.0643  0.1389  76  GLN A C   
1033  O O   . GLN A 67  ? 0.7890  0.8495  0.9091  -0.0918 0.0499  0.1450  76  GLN A O   
1034  C CB  . GLN A 67  ? 0.9253  1.0672  1.0011  -0.1409 0.0708  0.1775  76  GLN A CB  
1035  C CG  . GLN A 67  ? 1.1709  1.3573  1.2409  -0.1687 0.0817  0.1948  76  GLN A CG  
1036  C CD  . GLN A 67  ? 0.9762  1.1628  1.0080  -0.1878 0.0749  0.2212  76  GLN A CD  
1037  O OE1 . GLN A 67  ? 0.9865  1.1289  1.0117  -0.1870 0.0534  0.2428  76  GLN A OE1 
1038  N NE2 . GLN A 67  ? 1.2391  1.4769  1.2465  -0.2062 0.0921  0.2205  76  GLN A NE2 
1047  N N   . ARG A 68  ? 1.0164  1.1145  1.1121  -0.0872 0.0704  0.1200  77  ARG A N   
1048  C CA  . ARG A 68  ? 0.9138  0.9699  1.0100  -0.0686 0.0598  0.1104  77  ARG A CA  
1049  C C   . ARG A 68  ? 0.8938  0.9415  1.0181  -0.0541 0.0585  0.0954  77  ARG A C   
1050  O O   . ARG A 68  ? 0.7146  0.7251  0.8411  -0.0445 0.0462  0.0968  77  ARG A O   
1051  C CB  . ARG A 68  ? 0.8926  0.9495  0.9684  -0.0630 0.0644  0.0959  77  ARG A CB  
1052  C CG  . ARG A 68  ? 0.9026  0.9562  0.9511  -0.0744 0.0575  0.1142  77  ARG A CG  
1053  C CD  . ARG A 68  ? 0.9002  0.9100  0.9502  -0.0668 0.0404  0.1262  77  ARG A CD  
1054  N NE  . ARG A 68  ? 1.0716  1.0608  1.1243  -0.0518 0.0400  0.1075  77  ARG A NE  
1055  C CZ  . ARG A 68  ? 0.8959  0.8857  0.9345  -0.0499 0.0404  0.0989  77  ARG A CZ  
1056  N NH1 . ARG A 68  ? 0.7169  0.7275  0.7366  -0.0610 0.0397  0.1073  77  ARG A NH1 
1057  N NH2 . ARG A 68  ? 0.7388  0.7089  0.7815  -0.0392 0.0401  0.0836  77  ARG A NH2 
1071  N N   . LEU A 69  ? 0.7897  0.8740  0.9363  -0.0529 0.0706  0.0810  78  LEU A N   
1072  C CA  . LEU A 69  ? 0.5870  0.6647  0.7653  -0.0385 0.0655  0.0694  78  LEU A CA  
1073  C C   . LEU A 69  ? 0.7307  0.7950  0.9217  -0.0448 0.0526  0.0871  78  LEU A C   
1074  O O   . LEU A 69  ? 0.5322  0.5669  0.7316  -0.0341 0.0391  0.0855  78  LEU A O   
1075  C CB  . LEU A 69  ? 0.5892  0.7128  0.7972  -0.0337 0.0803  0.0483  78  LEU A CB  
1076  C CG  . LEU A 69  ? 0.7169  0.8363  0.9657  -0.0175 0.0709  0.0382  78  LEU A CG  
1077  C CD1 . LEU A 69  ? 0.5094  0.5801  0.7535  0.0006  0.0564  0.0313  78  LEU A CD1 
1078  C CD2 . LEU A 69  ? 0.8345  1.0066  1.1205  -0.0111 0.0870  0.0143  78  LEU A CD2 
1090  N N   . ALA A 70  ? 0.5819  0.6642  0.7709  -0.0642 0.0546  0.1054  79  ALA A N   
1091  C CA  . ALA A 70  ? 0.5901  0.6562  0.7926  -0.0718 0.0406  0.1206  79  ALA A CA  
1092  C C   . ALA A 70  ? 0.4590  0.4715  0.6415  -0.0659 0.0240  0.1278  79  ALA A C   
1093  O O   . ALA A 70  ? 0.8217  0.8107  1.0132  -0.0600 0.0110  0.1261  79  ALA A O   
1094  C CB  . ALA A 70  ? 0.9259  1.0182  1.1296  -0.0963 0.0452  0.1404  79  ALA A CB  
1100  N N   . ARG A 71  ? 0.6975  0.6934  0.8530  -0.0661 0.0248  0.1326  80  ARG A N   
1101  C CA  . ARG A 71  ? 0.6484  0.6009  0.7896  -0.0615 0.0114  0.1380  80  ARG A CA  
1102  C C   . ARG A 71  ? 0.7246  0.6544  0.8640  -0.0453 0.0070  0.1228  80  ARG A C   
1103  O O   . ARG A 71  ? 1.2454  1.1459  1.3811  -0.0422 -0.0041 0.1230  80  ARG A O   
1104  C CB  . ARG A 71  ? 0.9563  0.9047  1.0756  -0.0649 0.0130  0.1464  80  ARG A CB  
1105  C CG  . ARG A 71  ? 1.0934  1.0084  1.2082  -0.0674 -0.0013 0.1598  80  ARG A CG  
1106  C CD  . ARG A 71  ? 0.8093  0.7140  0.9076  -0.0614 -0.0028 0.1604  80  ARG A CD  
1107  N NE  . ARG A 71  ? 0.7900  0.6702  0.8856  -0.0467 -0.0055 0.1455  80  ARG A NE  
1108  C CZ  . ARG A 71  ? 0.7857  0.6369  0.8850  -0.0418 -0.0158 0.1454  80  ARG A CZ  
1109  N NH1 . ARG A 71  ? 0.7436  0.5813  0.8521  -0.0491 -0.0269 0.1597  80  ARG A NH1 
1110  N NH2 . ARG A 71  ? 0.9312  0.7671  1.0257  -0.0309 -0.0150 0.1307  80  ARG A NH2 
1124  N N   . LEU A 72  ? 0.8713  0.8164  1.0152  -0.0365 0.0153  0.1091  81  LEU A N   
1125  C CA  . LEU A 72  ? 0.8367  0.7600  0.9792  -0.0236 0.0097  0.0982  81  LEU A CA  
1126  C C   . LEU A 72  ? 0.8220  0.7443  0.9849  -0.0220 -0.0009 0.0986  81  LEU A C   
1127  O O   . LEU A 72  ? 0.5864  0.4812  0.7402  -0.0194 -0.0129 0.0999  81  LEU A O   
1128  C CB  . LEU A 72  ? 0.9078  0.8441  1.0513  -0.0153 0.0199  0.0836  81  LEU A CB  
1129  C CG  . LEU A 72  ? 0.9055  0.8239  1.0563  -0.0027 0.0137  0.0731  81  LEU A CG  
1130  C CD1 . LEU A 72  ? 0.8915  0.7739  1.0212  -0.0017 0.0042  0.0781  81  LEU A CD1 
1131  C CD2 . LEU A 72  ? 0.7285  0.6565  0.8828  0.0043  0.0229  0.0574  81  LEU A CD2 
1143  N N   . VAL A 73  ? 0.8381  0.7935  1.0276  -0.0263 0.0029  0.0986  82  VAL A N   
1144  C CA  . VAL A 73  ? 0.6338  0.5935  0.8477  -0.0261 -0.0093 0.0997  82  VAL A CA  
1145  C C   . VAL A 73  ? 0.6561  0.5901  0.8587  -0.0360 -0.0228 0.1107  82  VAL A C   
1146  O O   . VAL A 73  ? 0.6620  0.5732  0.8593  -0.0322 -0.0371 0.1092  82  VAL A O   
1147  C CB  . VAL A 73  ? 0.7869  0.7952  1.0357  -0.0314 0.0000  0.0972  82  VAL A CB  
1148  C CG1 . VAL A 73  ? 0.9176  0.9352  1.1941  -0.0368 -0.0136 0.1021  82  VAL A CG1 
1149  C CG2 . VAL A 73  ? 0.8850  0.9150  1.1508  -0.0169 0.0101  0.0796  82  VAL A CG2 
1159  N N   . LEU A 74  ? 0.5797  0.5145  0.7765  -0.0493 -0.0197 0.1214  83  LEU A N   
1160  C CA  . LEU A 74  ? 0.8147  0.7228  1.0065  -0.0581 -0.0339 0.1283  83  LEU A CA  
1161  C C   . LEU A 74  ? 0.6744  0.5438  0.8383  -0.0495 -0.0404 0.1219  83  LEU A C   
1162  O O   . LEU A 74  ? 1.2838  1.1320  1.4425  -0.0512 -0.0535 0.1188  83  LEU A O   
1163  C CB  . LEU A 74  ? 1.0053  0.9170  1.1986  -0.0738 -0.0313 0.1429  83  LEU A CB  
1164  C CG  . LEU A 74  ? 0.8049  0.7597  1.0249  -0.0883 -0.0239 0.1513  83  LEU A CG  
1165  C CD1 . LEU A 74  ? 1.0799  1.0390  1.2943  -0.1058 -0.0201 0.1697  83  LEU A CD1 
1166  C CD2 . LEU A 74  ? 0.9094  0.8723  1.1560  -0.0955 -0.0356 0.1510  83  LEU A CD2 
1178  N N   . GLY A 75  ? 0.8679  0.7318  1.0138  -0.0413 -0.0307 0.1181  84  GLY A N   
1179  C CA  . GLY A 75  ? 0.7639  0.5987  0.8856  -0.0348 -0.0334 0.1115  84  GLY A CA  
1180  C C   . GLY A 75  ? 0.5649  0.3903  0.6783  -0.0288 -0.0402 0.1045  84  GLY A C   
1181  O O   . GLY A 75  ? 0.7559  0.5599  0.8520  -0.0299 -0.0480 0.1001  84  GLY A O   
1185  N N   . CYS A 76  ? 1.2713  1.1130  1.3987  -0.0237 -0.0395 0.1036  85  CYS A N   
1186  C CA  . CYS A 76  ? 1.2299  1.0582  1.3500  -0.0194 -0.0513 0.1016  85  CYS A CA  
1187  C C   . CYS A 76  ? 1.2224  1.0479  1.3487  -0.0262 -0.0672 0.1038  85  CYS A C   
1188  O O   . CYS A 76  ? 0.6142  0.4185  0.7165  -0.0292 -0.0772 0.1019  85  CYS A O   
1189  C CB  . CYS A 76  ? 1.1906  1.0328  1.3302  -0.0099 -0.0506 0.0994  85  CYS A CB  
1190  S SG  . CYS A 76  ? 1.0422  0.8812  1.1709  -0.0031 -0.0355 0.0935  85  CYS A SG  
1196  N N   . ILE A 77  ? 1.0961  0.9442  1.2516  -0.0316 -0.0685 0.1071  86  ILE A N   
1197  C CA  . ILE A 77  ? 1.4978  1.3456  1.6635  -0.0403 -0.0850 0.1088  86  ILE A CA  
1198  C C   . ILE A 77  ? 0.9363  0.7546  1.0748  -0.0477 -0.0906 0.1049  86  ILE A C   
1199  O O   . ILE A 77  ? 0.7617  0.5661  0.8860  -0.0513 -0.1058 0.1009  86  ILE A O   
1200  C CB  . ILE A 77  ? 0.9764  0.8562  1.1791  -0.0487 -0.0817 0.1140  86  ILE A CB  
1201  C CG1 . ILE A 77  ? 0.6717  0.5855  0.9056  -0.0394 -0.0767 0.1121  86  ILE A CG1 
1202  C CG2 . ILE A 77  ? 0.7420  0.6182  0.9546  -0.0618 -0.0980 0.1159  86  ILE A CG2 
1203  C CD1 . ILE A 77  ? 0.7355  0.6896  1.0021  -0.0476 -0.0647 0.1150  86  ILE A CD1 
1215  N N   . THR A 78  ? 0.8287  0.6372  0.9588  -0.0490 -0.0792 0.1045  87  THR A N   
1216  C CA  . THR A 78  ? 0.6322  0.4134  0.7450  -0.0536 -0.0843 0.0971  87  THR A CA  
1217  C C   . THR A 78  ? 1.0613  0.8239  1.1402  -0.0492 -0.0862 0.0858  87  THR A C   
1218  O O   . THR A 78  ? 0.7328  0.4790  0.7972  -0.0546 -0.0961 0.0757  87  THR A O   
1219  C CB  . THR A 78  ? 0.9942  0.7706  1.1108  -0.0528 -0.0735 0.1007  87  THR A CB  
1220  O OG1 . THR A 78  ? 0.7189  0.5116  0.8622  -0.0626 -0.0740 0.1136  87  THR A OG1 
1221  C CG2 . THR A 78  ? 0.5509  0.2984  0.6567  -0.0531 -0.0778 0.0903  87  THR A CG2 
1229  N N   . MET A 79  ? 0.5503  0.3163  0.6152  -0.0414 -0.0766 0.0869  88  MET A N   
1230  C CA  . MET A 79  ? 0.6624  0.4143  0.6926  -0.0408 -0.0761 0.0790  88  MET A CA  
1231  C C   . MET A 79  ? 0.9507  0.6997  0.9680  -0.0462 -0.0936 0.0810  88  MET A C   
1232  O O   . MET A 79  ? 1.7953  1.5319  1.7820  -0.0525 -0.0995 0.0724  88  MET A O   
1233  C CB  . MET A 79  ? 0.5455  0.3018  0.5678  -0.0339 -0.0620 0.0823  88  MET A CB  
1234  C CG  . MET A 79  ? 2.7617  2.5223  2.7933  -0.0294 -0.0478 0.0804  88  MET A CG  
1235  S SD  . MET A 79  ? 1.2934  1.0398  1.3098  -0.0305 -0.0448 0.0651  88  MET A SD  
1236  C CE  . MET A 79  ? 1.0822  0.8365  1.1058  -0.0232 -0.0292 0.0641  88  MET A CE  
1246  N N   . ALA A 80  ? 0.7973  0.5606  0.8395  -0.0441 -0.1026 0.0914  89  ALA A N   
1247  C CA  . ALA A 80  ? 1.1445  0.9083  1.1837  -0.0481 -0.1238 0.0961  89  ALA A CA  
1248  C C   . ALA A 80  ? 0.8209  0.5804  0.8580  -0.0591 -0.1380 0.0887  89  ALA A C   
1249  O O   . ALA A 80  ? 0.8021  0.5521  0.8110  -0.0663 -0.1534 0.0860  89  ALA A O   
1250  C CB  . ALA A 80  ? 1.8249  1.6101  1.9038  -0.0405 -0.1293 0.1059  89  ALA A CB  
1256  N N   . TYR A 81  ? 0.6667  0.4320  0.7313  -0.0626 -0.1345 0.0859  90  TYR A N   
1257  C CA  . TYR A 81  ? 0.8820  0.6394  0.9482  -0.0744 -0.1489 0.0777  90  TYR A CA  
1258  C C   . TYR A 81  ? 1.0718  0.8038  1.0994  -0.0776 -0.1462 0.0601  90  TYR A C   
1259  O O   . TYR A 81  ? 0.7886  0.5122  0.7911  -0.0861 -0.1610 0.0507  90  TYR A O   
1260  C CB  . TYR A 81  ? 1.1311  0.8980  1.2365  -0.0796 -0.1454 0.0822  90  TYR A CB  
1261  C CG  . TYR A 81  ? 1.0386  0.7962  1.1538  -0.0943 -0.1623 0.0755  90  TYR A CG  
1262  C CD1 . TYR A 81  ? 1.0381  0.8163  1.1804  -0.1035 -0.1797 0.0816  90  TYR A CD1 
1263  C CD2 . TYR A 81  ? 1.1271  0.8556  1.2283  -0.0986 -0.1620 0.0612  90  TYR A CD2 
1264  C CE1 . TYR A 81  ? 0.9402  0.7095  1.0924  -0.1192 -0.1964 0.0749  90  TYR A CE1 
1265  C CE2 . TYR A 81  ? 1.2451  0.9604  1.3565  -0.1128 -0.1789 0.0529  90  TYR A CE2 
1266  C CZ  . TYR A 81  ? 1.2323  0.9677  1.3679  -0.1245 -0.1962 0.0604  90  TYR A CZ  
1267  O OH  . TYR A 81  ? 1.2960  1.0171  1.4421  -0.1410 -0.2144 0.0513  90  TYR A OH  
1277  N N   . VAL A 82  ? 0.8224  0.5456  0.8430  -0.0703 -0.1271 0.0542  91  VAL A N   
1278  C CA  . VAL A 82  ? 1.0030  0.7076  0.9938  -0.0707 -0.1212 0.0335  91  VAL A CA  
1279  C C   . VAL A 82  ? 1.0945  0.7991  1.0406  -0.0748 -0.1238 0.0282  91  VAL A C   
1280  O O   . VAL A 82  ? 0.8864  0.5819  0.8053  -0.0833 -0.1321 0.0113  91  VAL A O   
1281  C CB  . VAL A 82  ? 1.1107  0.8133  1.1088  -0.0601 -0.1010 0.0311  91  VAL A CB  
1282  C CG1 . VAL A 82  ? 0.7413  0.4328  0.7125  -0.0577 -0.0916 0.0075  91  VAL A CG1 
1283  C CG2 . VAL A 82  ? 0.7072  0.4064  0.7421  -0.0593 -0.1018 0.0378  91  VAL A CG2 
1293  N N   . TRP A 83  ? 0.9137  0.6276  0.8489  -0.0705 -0.1171 0.0425  92  TRP A N   
1294  C CA  . TRP A 83  ? 0.9150  0.6267  0.8032  -0.0768 -0.1160 0.0398  92  TRP A CA  
1295  C C   . TRP A 83  ? 1.0136  0.7262  0.8835  -0.0860 -0.1394 0.0517  92  TRP A C   
1296  O O   . TRP A 83  ? 1.0382  0.7473  0.8617  -0.0966 -0.1429 0.0473  92  TRP A O   
1297  C CB  . TRP A 83  ? 1.1556  0.8721  1.0366  -0.0711 -0.0986 0.0491  92  TRP A CB  
1298  C CG  . TRP A 83  ? 1.1380  0.8563  1.0303  -0.0636 -0.0774 0.0359  92  TRP A CG  
1299  C CD1 . TRP A 83  ? 0.8778  0.6022  0.7981  -0.0536 -0.0654 0.0437  92  TRP A CD1 
1300  C CD2 . TRP A 83  ? 0.7466  0.4617  0.6263  -0.0642 -0.0672 0.0108  92  TRP A CD2 
1301  N NE1 . TRP A 83  ? 0.7664  0.4914  0.6938  -0.0480 -0.0508 0.0281  92  TRP A NE1 
1302  C CE2 . TRP A 83  ? 0.7292  0.4485  0.6347  -0.0530 -0.0510 0.0069  92  TRP A CE2 
1303  C CE3 . TRP A 83  ? 0.9626  0.6731  0.8122  -0.0726 -0.0706 -0.0107 92  TRP A CE3 
1304  C CZ2 . TRP A 83  ? 0.8923  0.6110  0.8011  -0.0477 -0.0393 -0.0169 92  TRP A CZ2 
1305  C CZ3 . TRP A 83  ? 1.0381  0.7483  0.8888  -0.0677 -0.0565 -0.0378 92  TRP A CZ3 
1306  C CH2 . TRP A 83  ? 1.0706  0.7846  0.9540  -0.0541 -0.0412 -0.0407 92  TRP A CH2 
1317  N N   . GLY A 84  ? 1.0759  0.7961  0.9814  -0.0831 -0.1556 0.0660  93  GLY A N   
1318  C CA  . GLY A 84  ? 0.9639  0.6870  0.8605  -0.0904 -0.1828 0.0773  93  GLY A CA  
1319  C C   . GLY A 84  ? 0.9527  0.6727  0.8273  -0.0898 -0.1891 0.0966  93  GLY A C   
1320  O O   . GLY A 84  ? 0.8494  0.5715  0.7469  -0.0787 -0.1802 0.1084  93  GLY A O   
1324  N N   . LYS A 85  ? 1.0799  0.7936  0.9087  -0.1032 -0.2069 0.1006  94  LYS A N   
1325  C CA  . LYS A 85  ? 1.0387  0.7442  0.8384  -0.1070 -0.2162 0.1224  94  LYS A CA  
1326  C C   . LYS A 85  ? 1.1762  0.8747  0.9366  -0.1124 -0.1906 0.1191  94  LYS A C   
1327  O O   . LYS A 85  ? 1.3742  1.0634  1.1132  -0.1169 -0.1950 0.1392  94  LYS A O   
1328  C CB  . LYS A 85  ? 1.0435  0.7464  0.8052  -0.1226 -0.2479 0.1315  94  LYS A CB  
1329  C CG  . LYS A 85  ? 1.5616  1.2740  1.3669  -0.1168 -0.2795 0.1429  94  LYS A CG  
1330  C CD  . LYS A 85  ? 1.1035  0.8148  0.8703  -0.1332 -0.3149 0.1528  94  LYS A CD  
1331  C CE  . LYS A 85  ? 1.4423  1.1675  1.2637  -0.1247 -0.3469 0.1657  94  LYS A CE  
1332  N NZ  . LYS A 85  ? 2.2437  1.9716  2.0342  -0.1406 -0.3839 0.1732  94  LYS A NZ  
1346  N N   . GLY A 86  ? 1.2592  0.9623  1.0157  -0.1116 -0.1649 0.0952  95  GLY A N   
1347  C CA  . GLY A 86  ? 1.0236  0.7277  0.7504  -0.1164 -0.1393 0.0884  95  GLY A CA  
1348  C C   . GLY A 86  ? 1.0931  0.7998  0.7551  -0.1368 -0.1372 0.0808  95  GLY A C   
1349  O O   . GLY A 86  ? 1.1986  0.9089  0.8313  -0.1455 -0.1206 0.0849  95  GLY A O   
1353  N N   . HIS A 87  ? 1.0678  0.7761  0.7063  -0.1461 -0.1511 0.0669  96  HIS A N   
1354  C CA  . HIS A 87  ? 1.3907  1.1050  0.9619  -0.1677 -0.1502 0.0584  96  HIS A CA  
1355  C C   . HIS A 87  ? 1.3558  1.0774  0.9160  -0.1699 -0.1397 0.0185  96  HIS A C   
1356  O O   . HIS A 87  ? 1.3473  1.0773  0.8503  -0.1882 -0.1390 0.0043  96  HIS A O   
1357  C CB  . HIS A 87  ? 1.6619  1.3691  1.2008  -0.1821 -0.1856 0.0846  96  HIS A CB  
1358  C CG  . HIS A 87  ? 1.5787  1.2737  1.1326  -0.1783 -0.2000 0.1232  96  HIS A CG  
1359  N ND1 . HIS A 87  ? 1.7438  1.4354  1.2929  -0.1791 -0.1811 0.1362  96  HIS A ND1 
1360  C CD2 . HIS A 87  ? 1.4655  1.1504  1.0446  -0.1724 -0.2325 0.1494  96  HIS A CD2 
1361  C CE1 . HIS A 87  ? 1.7195  1.3951  1.2885  -0.1741 -0.2016 0.1680  96  HIS A CE1 
1362  N NE2 . HIS A 87  ? 1.8378  1.5100  1.4270  -0.1685 -0.2326 0.1760  96  HIS A NE2 
1369  N N   . GLY A 88  ? 1.8351  1.5533  1.4471  -0.1523 -0.1306 -0.0006 97  GLY A N   
1370  C CA  . GLY A 88  ? 1.3296  1.0490  0.9406  -0.1510 -0.1199 -0.0401 97  GLY A CA  
1371  C C   . GLY A 88  ? 1.6215  1.3285  1.2584  -0.1492 -0.1421 -0.0519 97  GLY A C   
1372  O O   . GLY A 88  ? 1.6890  1.3914  1.3266  -0.1483 -0.1359 -0.0864 97  GLY A O   
1376  N N   . ASP A 89  ? 1.7526  1.4550  1.4117  -0.1495 -0.1685 -0.0263 98  ASP A N   
1377  C CA  . ASP A 89  ? 1.6799  1.3740  1.3738  -0.1487 -0.1886 -0.0344 98  ASP A CA  
1378  C C   . ASP A 89  ? 0.9928  0.6822  0.7520  -0.1313 -0.1781 -0.0288 98  ASP A C   
1379  O O   . ASP A 89  ? 1.0715  0.7667  0.8649  -0.1239 -0.1835 -0.0022 98  ASP A O   
1380  C CB  . ASP A 89  ? 1.9380  1.6364  1.6270  -0.1587 -0.2221 -0.0108 98  ASP A CB  
1381  C CG  . ASP A 89  ? 2.0992  1.7957  1.8405  -0.1566 -0.2414 -0.0105 98  ASP A CG  
1382  O OD1 . ASP A 89  ? 1.9689  1.6551  1.7337  -0.1540 -0.2336 -0.0338 98  ASP A OD1 
1383  O OD2 . ASP A 89  ? 2.2823  1.9882  2.0441  -0.1578 -0.2652 0.0134  98  ASP A OD2 
1388  N N   . VAL A 90  ? 1.2052  0.8844  0.9817  -0.1246 -0.1633 -0.0551 99  VAL A N   
1389  C CA  . VAL A 90  ? 1.0816  0.7559  0.9092  -0.1088 -0.1485 -0.0508 99  VAL A CA  
1390  C C   . VAL A 90  ? 1.0545  0.7143  0.9248  -0.1096 -0.1623 -0.0563 99  VAL A C   
1391  O O   . VAL A 90  ? 1.4534  1.1008  1.3131  -0.1193 -0.1756 -0.0786 99  VAL A O   
1392  C CB  . VAL A 90  ? 1.0283  0.7017  0.8470  -0.0996 -0.1220 -0.0730 99  VAL A CB  
1393  C CG1 . VAL A 90  ? 1.3151  0.9795  1.1848  -0.0849 -0.1126 -0.0719 99  VAL A CG1 
1394  C CG2 . VAL A 90  ? 1.3248  1.0155  1.1131  -0.1000 -0.1064 -0.0591 99  VAL A CG2 
1404  N N   . ARG A 91  ? 0.8724  0.5348  0.7895  -0.1016 -0.1595 -0.0352 100 ARG A N   
1405  C CA  . ARG A 91  ? 1.2970  0.9465  1.2587  -0.1032 -0.1678 -0.0346 100 ARG A CA  
1406  C C   . ARG A 91  ? 0.9919  0.6257  0.9729  -0.0911 -0.1513 -0.0447 100 ARG A C   
1407  O O   . ARG A 91  ? 0.9651  0.6092  0.9513  -0.0798 -0.1341 -0.0331 100 ARG A O   
1408  C CB  . ARG A 91  ? 1.1406  0.8079  1.1415  -0.1040 -0.1730 -0.0039 100 ARG A CB  
1409  C CG  . ARG A 91  ? 1.2520  0.9371  1.2559  -0.1138 -0.1929 0.0089  100 ARG A CG  
1410  C CD  . ARG A 91  ? 1.1624  0.8366  1.1714  -0.1293 -0.2151 -0.0046 100 ARG A CD  
1411  N NE  . ARG A 91  ? 1.1196  0.7965  1.0859  -0.1370 -0.2300 -0.0143 100 ARG A NE  
1412  C CZ  . ARG A 91  ? 1.2789  0.9692  1.2487  -0.1487 -0.2550 -0.0074 100 ARG A CZ  
1413  N NH1 . ARG A 91  ? 1.5487  1.2547  1.5680  -0.1547 -0.2675 0.0073  100 ARG A NH1 
1414  N NH2 . ARG A 91  ? 1.5415  1.2321  1.4633  -0.1558 -0.2677 -0.0156 100 ARG A NH2 
1428  N N   . LYS A 92  ? 1.1171  0.7249  1.1136  -0.0937 -0.1593 -0.0646 101 LYS A N   
1429  C CA  . LYS A 92  ? 1.0113  0.5999  1.0326  -0.0811 -0.1492 -0.0736 101 LYS A CA  
1430  C C   . LYS A 92  ? 0.8854  0.4614  0.9528  -0.0846 -0.1583 -0.0508 101 LYS A C   
1431  O O   . LYS A 92  ? 1.0919  0.6488  1.1828  -0.0750 -0.1544 -0.0530 101 LYS A O   
1432  C CB  . LYS A 92  ? 1.0817  0.6455  1.0916  -0.0781 -0.1507 -0.1153 101 LYS A CB  
1433  C CG  . LYS A 92  ? 1.4854  1.0663  1.4430  -0.0779 -0.1385 -0.1415 101 LYS A CG  
1434  C CD  . LYS A 92  ? 1.1709  0.7402  1.1241  -0.0662 -0.1260 -0.1838 101 LYS A CD  
1435  C CE  . LYS A 92  ? 1.6020  1.1948  1.5002  -0.0703 -0.1114 -0.2097 101 LYS A CE  
1446  N N   . VAL A 93  ? 1.1018  0.6898  1.1841  -0.0988 -0.1706 -0.0283 102 VAL A N   
1447  C CA  . VAL A 93  ? 0.7871  0.3686  0.9104  -0.1075 -0.1782 -0.0048 102 VAL A CA  
1448  C C   . VAL A 93  ? 0.8838  0.5033  1.0180  -0.1118 -0.1725 0.0258  102 VAL A C   
1449  O O   . VAL A 93  ? 0.9852  0.6268  1.1134  -0.1191 -0.1797 0.0291  102 VAL A O   
1450  C CB  . VAL A 93  ? 0.8623  0.4195  1.0034  -0.1259 -0.2014 -0.0131 102 VAL A CB  
1451  C CG1 . VAL A 93  ? 0.8511  0.4034  1.0350  -0.1402 -0.2090 0.0165  102 VAL A CG1 
1452  C CG2 . VAL A 93  ? 0.8761  0.3927  1.0088  -0.1210 -0.2083 -0.0497 102 VAL A CG2 
1462  N N   . LEU A 94  ? 0.9988  0.6264  1.1519  -0.1081 -0.1618 0.0473  103 LEU A N   
1463  C CA  . LEU A 94  ? 0.9094  0.5750  1.0754  -0.1119 -0.1540 0.0722  103 LEU A CA  
1464  C C   . LEU A 94  ? 0.8116  0.4852  1.0114  -0.1320 -0.1640 0.0910  103 LEU A C   
1465  O O   . LEU A 94  ? 1.0644  0.7162  1.2807  -0.1393 -0.1677 0.1007  103 LEU A O   
1466  C CB  . LEU A 94  ? 0.7871  0.4628  0.9512  -0.0998 -0.1361 0.0841  103 LEU A CB  
1467  C CG  . LEU A 94  ? 0.8525  0.5691  1.0241  -0.0995 -0.1239 0.1028  103 LEU A CG  
1468  C CD1 . LEU A 94  ? 1.1608  0.8956  1.3150  -0.0914 -0.1217 0.0943  103 LEU A CD1 
1469  C CD2 . LEU A 94  ? 0.7542  0.4772  0.9238  -0.0909 -0.1086 0.1140  103 LEU A CD2 
1481  N N   . PRO A 95  ? 0.7219  0.4281  0.9359  -0.1422 -0.1689 0.0984  104 PRO A N   
1482  C CA  . PRO A 95  ? 1.0618  0.7798  1.3109  -0.1650 -0.1784 0.1145  104 PRO A CA  
1483  C C   . PRO A 95  ? 0.7487  0.4811  1.0158  -0.1724 -0.1657 0.1398  104 PRO A C   
1484  O O   . PRO A 95  ? 0.7219  0.4786  0.9811  -0.1608 -0.1476 0.1474  104 PRO A O   
1485  C CB  . PRO A 95  ? 1.1138  0.8740  1.3765  -0.1688 -0.1829 0.1154  104 PRO A CB  
1486  C CG  . PRO A 95  ? 1.1094  0.8593  1.3407  -0.1543 -0.1876 0.0964  104 PRO A CG  
1487  C CD  . PRO A 95  ? 1.4217  1.1466  1.6210  -0.1365 -0.1737 0.0879  104 PRO A CD  
1495  N N   . ARG A 96  ? 0.7094  0.4259  0.9988  -0.1942 -0.1767 0.1529  105 ARG A N   
1496  C CA  . ARG A 96  ? 1.0718  0.8047  1.3769  -0.2087 -0.1675 0.1815  105 ARG A CA  
1497  C C   . ARG A 96  ? 0.8772  0.6733  1.1924  -0.2096 -0.1487 0.1919  105 ARG A C   
1498  O O   . ARG A 96  ? 0.7695  0.5845  1.0769  -0.2060 -0.1317 0.2052  105 ARG A O   
1499  C CB  . ARG A 96  ? 1.0875  0.8042  1.4176  -0.2371 -0.1837 0.1954  105 ARG A CB  
1500  C CG  . ARG A 96  ? 1.2295  0.9784  1.5893  -0.2584 -0.1923 0.1964  105 ARG A CG  
1501  C CD  . ARG A 96  ? 1.2656  1.0011  1.6387  -0.2789 -0.2052 0.2027  105 ARG A CD  
1502  N NE  . ARG A 96  ? 1.1823  0.8603  1.5408  -0.2701 -0.2228 0.1809  105 ARG A NE  
1503  C CZ  . ARG A 96  ? 0.8574  0.4951  1.2048  -0.2641 -0.2260 0.1830  105 ARG A CZ  
1504  N NH1 . ARG A 96  ? 0.8604  0.5064  1.2052  -0.2672 -0.2155 0.2088  105 ARG A NH1 
1505  N NH2 . ARG A 96  ? 0.8904  0.4810  1.2298  -0.2548 -0.2409 0.1578  105 ARG A NH2 
1519  N N   . ASN A 97  ? 0.8002  0.6301  1.1331  -0.2121 -0.1522 0.1831  106 ASN A N   
1520  C CA  . ASN A 97  ? 0.7635  0.6559  1.1152  -0.2107 -0.1355 0.1883  106 ASN A CA  
1521  C C   . ASN A 97  ? 0.8659  0.7684  1.1940  -0.1888 -0.1151 0.1862  106 ASN A C   
1522  O O   . ASN A 97  ? 1.0673  1.0127  1.4051  -0.1917 -0.0965 0.1957  106 ASN A O   
1523  C CB  . ASN A 97  ? 1.1350  1.0510  1.5031  -0.2042 -0.1462 0.1726  106 ASN A CB  
1526  N N   . ILE A 98  ? 0.9229  0.7865  1.2196  -0.1688 -0.1182 0.1726  107 ILE A N   
1527  C CA  . ILE A 98  ? 0.8167  0.6836  1.0896  -0.1481 -0.1020 0.1681  107 ILE A CA  
1528  C C   . ILE A 98  ? 0.7770  0.6056  1.0264  -0.1437 -0.1005 0.1727  107 ILE A C   
1529  O O   . ILE A 98  ? 0.6187  0.4609  0.8589  -0.1398 -0.0862 0.1816  107 ILE A O   
1530  C CB  . ILE A 98  ? 0.7429  0.6053  1.0016  -0.1283 -0.1059 0.1491  107 ILE A CB  
1531  C CG1 . ILE A 98  ? 0.7029  0.5681  0.9398  -0.1096 -0.0900 0.1449  107 ILE A CG1 
1532  C CG2 . ILE A 98  ? 1.0997  0.9169  1.3392  -0.1271 -0.1233 0.1358  107 ILE A CG2 
1533  C CD1 . ILE A 98  ? 2.0111  1.8803  2.2399  -0.0941 -0.0926 0.1323  107 ILE A CD1 
1545  N N   . ALA A 99  ? 0.9136  0.6960  1.1567  -0.1454 -0.1162 0.1666  108 ALA A N   
1546  C CA  . ALA A 99  ? 0.8229  0.5702  1.0504  -0.1369 -0.1161 0.1683  108 ALA A CA  
1547  C C   . ALA A 99  ? 0.9327  0.6881  1.1684  -0.1510 -0.1122 0.1953  108 ALA A C   
1548  O O   . ALA A 99  ? 0.7974  0.5510  1.0189  -0.1415 -0.1043 0.2015  108 ALA A O   
1549  C CB  . ALA A 99  ? 0.6809  0.3775  0.9081  -0.1363 -0.1343 0.1545  108 ALA A CB  
1555  N N   . VAL A 100 ? 0.7487  0.5138  1.0060  -0.1758 -0.1187 0.2129  109 VAL A N   
1556  C CA  . VAL A 100 ? 0.9744  0.7456  1.2360  -0.1950 -0.1171 0.2428  109 VAL A CA  
1557  C C   . VAL A 100 ? 0.9272  0.7465  1.1758  -0.1914 -0.0948 0.2501  109 VAL A C   
1558  O O   . VAL A 100 ? 0.7163  0.5261  0.9466  -0.1840 -0.0916 0.2583  109 VAL A O   
1559  C CB  . VAL A 100 ? 1.3255  1.1067  1.6107  -0.2239 -0.1256 0.2579  109 VAL A CB  
1560  C CG1 . VAL A 100 ? 0.7145  0.5191  0.9934  -0.2419 -0.1182 0.2855  109 VAL A CG1 
1561  C CG2 . VAL A 100 ? 0.7297  0.4603  1.0175  -0.2211 -0.1472 0.2447  109 VAL A CG2 
1571  N N   . PRO A 101 ? 0.7196  0.5898  0.9774  -0.1931 -0.0798 0.2435  110 PRO A N   
1572  C CA  . PRO A 101 ? 1.1791  1.0934  1.4246  -0.1899 -0.0582 0.2470  110 PRO A CA  
1573  C C   . PRO A 101 ? 1.2824  1.1793  1.5022  -0.1641 -0.0535 0.2332  110 PRO A C   
1574  O O   . PRO A 101 ? 0.5796  0.4869  0.7811  -0.1639 -0.0449 0.2425  110 PRO A O   
1575  C CB  . PRO A 101 ? 0.6792  0.6458  0.9473  -0.1896 -0.0456 0.2335  110 PRO A CB  
1576  C CG  . PRO A 101 ? 0.5853  0.5276  0.8683  -0.1815 -0.0625 0.2171  110 PRO A CG  
1577  C CD  . PRO A 101 ? 0.9625  0.8507  1.2420  -0.1927 -0.0830 0.2276  110 PRO A CD  
1585  N N   . TYR A 102 ? 0.8468  0.7152  1.0626  -0.1445 -0.0609 0.2124  111 TYR A N   
1586  C CA  . TYR A 102 ? 1.0012  0.8556  1.1946  -0.1228 -0.0558 0.2000  111 TYR A CA  
1587  C C   . TYR A 102 ? 1.0128  0.8370  1.1949  -0.1227 -0.0636 0.2129  111 TYR A C   
1588  O O   . TYR A 102 ? 0.7566  0.5916  0.9230  -0.1162 -0.0553 0.2161  111 TYR A O   
1589  C CB  . TYR A 102 ? 0.6897  0.5212  0.8794  -0.1064 -0.0623 0.1773  111 TYR A CB  
1590  C CG  . TYR A 102 ? 0.8652  0.6870  1.0335  -0.0858 -0.0555 0.1624  111 TYR A CG  
1591  C CD1 . TYR A 102 ? 1.4410  1.2881  1.5996  -0.0798 -0.0409 0.1627  111 TYR A CD1 
1592  C CD2 . TYR A 102 ? 1.0092  0.8006  1.1670  -0.0743 -0.0627 0.1459  111 TYR A CD2 
1593  C CE1 . TYR A 102 ? 0.8760  0.7158  1.0177  -0.0640 -0.0352 0.1497  111 TYR A CE1 
1594  C CE2 . TYR A 102 ? 0.8946  0.6827  1.0342  -0.0593 -0.0550 0.1335  111 TYR A CE2 
1595  C CZ  . TYR A 102 ? 0.9649  0.7765  1.0978  -0.0545 -0.0418 0.1366  111 TYR A CZ  
1596  O OH  . TYR A 102 ? 0.9817  0.7915  1.0986  -0.0423 -0.0341 0.1258  111 TYR A OH  
1606  N N   . CYS A 103 ? 0.9365  0.7226  1.1291  -0.1300 -0.0813 0.2204  112 CYS A N   
1607  C CA  . CYS A 103 ? 0.8547  0.6092  1.0428  -0.1259 -0.0919 0.2313  112 CYS A CA  
1608  C C   . CYS A 103 ? 0.9558  0.7311  1.1371  -0.1430 -0.0895 0.2613  112 CYS A C   
1609  O O   . CYS A 103 ? 2.0507  1.8189  2.2210  -0.1361 -0.0926 0.2699  112 CYS A O   
1610  C CB  . CYS A 103 ? 0.7067  0.4121  0.9113  -0.1277 -0.1128 0.2289  112 CYS A CB  
1611  S SG  . CYS A 103 ? 0.9529  0.6349  1.1540  -0.1041 -0.1137 0.1904  112 CYS A SG  
1617  N N   . GLN A 104 ? 1.0212  0.8283  1.2080  -0.1659 -0.0829 0.2763  113 GLN A N   
1618  C CA  . GLN A 104 ? 0.9607  0.7967  1.1352  -0.1864 -0.0770 0.3043  113 GLN A CA  
1619  C C   . GLN A 104 ? 1.1478  1.0231  1.3005  -0.1751 -0.0574 0.2934  113 GLN A C   
1620  O O   . GLN A 104 ? 0.8488  0.7292  0.9818  -0.1777 -0.0581 0.3079  113 GLN A O   
1621  C CB  . GLN A 104 ? 1.1279  0.9978  1.3161  -0.2150 -0.0704 0.3186  113 GLN A CB  
1622  C CG  . GLN A 104 ? 1.4250  1.2687  1.6265  -0.2281 -0.0879 0.3267  113 GLN A CG  
1623  C CD  . GLN A 104 ? 1.6863  1.5738  1.9032  -0.2553 -0.0775 0.3367  113 GLN A CD  
1624  O OE1 . GLN A 104 ? 1.4320  1.3242  1.6740  -0.2576 -0.0782 0.3245  113 GLN A OE1 
1625  N NE2 . GLN A 104 ? 1.9488  1.8734  2.1509  -0.2764 -0.0671 0.3579  113 GLN A NE2 
1634  N N   . LEU A 105 ? 1.0970  0.9979  1.2538  -0.1622 -0.0420 0.2671  114 LEU A N   
1635  C CA  . LEU A 105 ? 0.9291  0.8666  1.0683  -0.1537 -0.0237 0.2555  114 LEU A CA  
1636  C C   . LEU A 105 ? 0.7744  0.6858  0.8972  -0.1350 -0.0298 0.2493  114 LEU A C   
1637  O O   . LEU A 105 ? 0.8665  0.7993  0.9695  -0.1353 -0.0222 0.2517  114 LEU A O   
1638  C CB  . LEU A 105 ? 0.7699  0.7352  0.9219  -0.1421 -0.0092 0.2291  114 LEU A CB  
1639  C CG  . LEU A 105 ? 1.3617  1.3589  1.4987  -0.1310 0.0086  0.2123  114 LEU A CG  
1640  C CD1 . LEU A 105 ? 1.5690  1.6111  1.6918  -0.1506 0.0225  0.2249  114 LEU A CD1 
1641  C CD2 . LEU A 105 ? 1.4711  1.4837  1.6250  -0.1153 0.0176  0.1862  114 LEU A CD2 
1653  N N   . SER A 106 ? 1.3584  1.2263  1.4900  -0.1209 -0.0440 0.2416  115 SER A N   
1654  C CA  . SER A 106 ? 0.8074  0.6548  0.9299  -0.1029 -0.0491 0.2338  115 SER A CA  
1655  C C   . SER A 106 ? 0.9513  0.7886  1.0672  -0.1107 -0.0625 0.2594  115 SER A C   
1656  O O   . SER A 106 ? 1.1043  0.9579  1.2041  -0.1070 -0.0592 0.2611  115 SER A O   
1657  C CB  . SER A 106 ? 0.6878  0.4974  0.8235  -0.0879 -0.0588 0.2170  115 SER A CB  
1658  O OG  . SER A 106 ? 0.7338  0.5503  0.8727  -0.0826 -0.0506 0.1972  115 SER A OG  
1664  N N   . LYS A 107 ? 1.0035  0.8137  1.1319  -0.1233 -0.0797 0.2810  116 LYS A N   
1665  C CA  . LYS A 107 ? 0.9471  0.7420  1.0716  -0.1317 -0.0976 0.3101  116 LYS A CA  
1666  C C   . LYS A 107 ? 0.8343  0.6725  0.9309  -0.1479 -0.0875 0.3273  116 LYS A C   
1667  O O   . LYS A 107 ? 0.8314  0.6691  0.9152  -0.1469 -0.0979 0.3420  116 LYS A O   
1668  C CB  . LYS A 107 ? 1.1955  0.9671  1.3335  -0.1434 -0.1130 0.3213  116 LYS A CB  
1669  C CG  . LYS A 107 ? 1.5170  1.2758  1.6516  -0.1498 -0.1324 0.3437  116 LYS A CG  
1670  C CD  . LYS A 107 ? 1.4275  1.1635  1.5775  -0.1628 -0.1454 0.3516  116 LYS A CD  
1671  C CE  . LYS A 107 ? 1.3977  1.1144  1.5490  -0.1697 -0.1684 0.3757  116 LYS A CE  
1682  N N   . LYS A 108 ? 1.0916  0.9703  1.1793  -0.1633 -0.0677 0.3247  117 LYS A N   
1683  C CA  . LYS A 108 ? 1.2223  1.1490  1.2815  -0.1789 -0.0536 0.3337  117 LYS A CA  
1684  C C   . LYS A 108 ? 1.1774  1.1185  1.2214  -0.1593 -0.0451 0.3109  117 LYS A C   
1685  O O   . LYS A 108 ? 1.0806  1.0414  1.0993  -0.1668 -0.0465 0.3222  117 LYS A O   
1686  C CB  . LYS A 108 ? 1.0570  1.0277  1.1187  -0.1945 -0.0313 0.3266  117 LYS A CB  
1687  C CG  . LYS A 108 ? 1.1268  1.1513  1.1589  -0.2155 -0.0151 0.3363  117 LYS A CG  
1688  C CD  . LYS A 108 ? 1.1629  1.2368  1.2037  -0.2322 0.0077  0.3292  117 LYS A CD  
1689  C CE  . LYS A 108 ? 1.1767  1.3049  1.1842  -0.2582 0.0230  0.3426  117 LYS A CE  
1690  N NZ  . LYS A 108 ? 1.1448  1.2603  1.1325  -0.2878 0.0050  0.3884  117 LYS A NZ  
1704  N N   . LEU A 109 ? 1.0450  0.9752  1.1028  -0.1362 -0.0383 0.2802  118 LEU A N   
1705  C CA  . LEU A 109 ? 1.0338  0.9760  1.0800  -0.1200 -0.0300 0.2582  118 LEU A CA  
1706  C C   . LEU A 109 ? 1.1418  1.0525  1.1950  -0.1032 -0.0469 0.2577  118 LEU A C   
1707  O O   . LEU A 109 ? 1.5419  1.4632  1.5864  -0.0927 -0.0426 0.2430  118 LEU A O   
1708  C CB  . LEU A 109 ? 0.5528  0.5032  0.6092  -0.1064 -0.0131 0.2269  118 LEU A CB  
1709  C CG  . LEU A 109 ? 0.7431  0.7353  0.7977  -0.1173 0.0065  0.2188  118 LEU A CG  
1710  C CD1 . LEU A 109 ? 0.8142  0.8042  0.8905  -0.1038 0.0150  0.1945  118 LEU A CD1 
1711  C CD2 . LEU A 109 ? 0.8705  0.9019  0.9011  -0.1221 0.0205  0.2097  118 LEU A CD2 
1723  N N   . GLU A 110 ? 1.0837  1.0882  1.2978  -0.1181 -0.2193 0.2549  119 GLU A N   
1724  C CA  . GLU A 110 ? 1.0920  1.0509  1.3338  -0.1046 -0.2272 0.2429  119 GLU A CA  
1725  C C   . GLU A 110 ? 0.9091  0.8370  1.1440  -0.0792 -0.2047 0.2038  119 GLU A C   
1726  O O   . GLU A 110 ? 0.7787  0.6842  1.0277  -0.0648 -0.2004 0.1860  119 GLU A O   
1727  C CB  . GLU A 110 ? 1.2580  1.2350  1.5075  -0.1079 -0.2311 0.2531  119 GLU A CB  
1728  C CG  . GLU A 110 ? 1.2005  1.2066  1.4591  -0.1353 -0.2564 0.2933  119 GLU A CG  
1729  C CD  . GLU A 110 ? 1.1854  1.1948  1.4633  -0.1389 -0.2692 0.3061  119 GLU A CD  
1730  O OE1 . GLU A 110 ? 1.3189  1.2841  1.6281  -0.1240 -0.2782 0.2946  119 GLU A OE1 
1731  O OE2 . GLU A 110 ? 1.2349  1.2947  1.4979  -0.1575 -0.2707 0.3270  119 GLU A OE2 
1738  N N   . LEU A 111 ? 0.8858  0.8129  1.1017  -0.0755 -0.1926 0.1921  120 LEU A N   
1739  C CA  . LEU A 111 ? 0.9781  0.8790  1.1862  -0.0559 -0.1740 0.1590  120 LEU A CA  
1740  C C   . LEU A 111 ? 1.0840  0.9525  1.3038  -0.0561 -0.1840 0.1512  120 LEU A C   
1741  O O   . LEU A 111 ? 1.3909  1.2598  1.6189  -0.0715 -0.2027 0.1718  120 LEU A O   
1742  C CB  . LEU A 111 ? 0.9083  0.8350  1.0828  -0.0496 -0.1497 0.1479  120 LEU A CB  
1743  C CG  . LEU A 111 ? 1.1164  1.0694  1.2789  -0.0446 -0.1355 0.1441  120 LEU A CG  
1744  C CD1 . LEU A 111 ? 1.4485  1.4341  1.5856  -0.0433 -0.1199 0.1408  120 LEU A CD1 
1745  C CD2 . LEU A 111 ? 1.4973  1.4255  1.6629  -0.0288 -0.1237 0.1202  120 LEU A CD2 
1757  N N   . PRO A 112 ? 0.7915  0.6343  1.0118  -0.0413 -0.1722 0.1210  121 PRO A N   
1758  C CA  . PRO A 112 ? 1.0180  0.8350  1.2453  -0.0418 -0.1786 0.1081  121 PRO A CA  
1759  C C   . PRO A 112 ? 1.1103  0.9425  1.3062  -0.0452 -0.1665 0.1073  121 PRO A C   
1760  O O   . PRO A 112 ? 1.0024  0.8600  1.1725  -0.0413 -0.1489 0.1080  121 PRO A O   
1761  C CB  . PRO A 112 ? 1.1173  0.9109  1.3573  -0.0257 -0.1690 0.0741  121 PRO A CB  
1762  C CG  . PRO A 112 ? 0.8185  0.6291  1.0442  -0.0170 -0.1509 0.0688  121 PRO A CG  
1763  C CD  . PRO A 112 ? 0.6031  0.4389  0.8248  -0.0259 -0.1569 0.0979  121 PRO A CD  
1771  N N   . PRO A 113 ? 0.9373  0.7558  1.1373  -0.0526 -0.1771 0.1069  122 PRO A N   
1772  C CA  . PRO A 113 ? 0.8257  0.6580  0.9992  -0.0568 -0.1684 0.1068  122 PRO A CA  
1773  C C   . PRO A 113 ? 0.7510  0.5759  0.9063  -0.0454 -0.1489 0.0781  122 PRO A C   
1774  O O   . PRO A 113 ? 0.7310  0.5414  0.8839  -0.0474 -0.1500 0.0621  122 PRO A O   
1775  C CB  . PRO A 113 ? 1.0181  0.8336  1.2082  -0.0709 -0.1910 0.1163  122 PRO A CB  
1776  C CG  . PRO A 113 ? 0.8848  0.6640  1.1085  -0.0648 -0.2032 0.0989  122 PRO A CG  
1777  C CD  . PRO A 113 ? 0.6840  0.4696  0.9178  -0.0570 -0.2000 0.1037  122 PRO A CD  
1785  N N   . ILE A 114 ? 0.6940  0.5302  0.8363  -0.0348 -0.1315 0.0709  123 ILE A N   
1786  C CA  . ILE A 114 ? 0.7216  0.5576  0.8427  -0.0276 -0.1138 0.0509  123 ILE A CA  
1787  C C   . ILE A 114 ? 0.9041  0.7592  1.0102  -0.0202 -0.0997 0.0562  123 ILE A C   
1788  O O   . ILE A 114 ? 0.9848  0.8493  1.0996  -0.0186 -0.1014 0.0665  123 ILE A O   
1789  C CB  . ILE A 114 ? 0.5487  0.3642  0.6808  -0.0217 -0.1097 0.0222  123 ILE A CB  
1790  C CG1 . ILE A 114 ? 0.5486  0.3704  0.6547  -0.0207 -0.0938 0.0062  123 ILE A CG1 
1791  C CG2 . ILE A 114 ? 0.5989  0.4120  0.7468  -0.0127 -0.1063 0.0173  123 ILE A CG2 
1792  C CD1 . ILE A 114 ? 0.5664  0.3773  0.6793  -0.0208 -0.0908 -0.0244 123 ILE A CD1 
1804  N N   . LEU A 115 ? 0.7454  0.6068  0.8297  -0.0173 -0.0876 0.0501  124 LEU A N   
1805  C CA  . LEU A 115 ? 0.7595  0.6353  0.8314  -0.0098 -0.0757 0.0529  124 LEU A CA  
1806  C C   . LEU A 115 ? 0.9537  0.8203  1.0309  -0.0028 -0.0675 0.0397  124 LEU A C   
1807  O O   . LEU A 115 ? 1.0113  0.8652  1.0869  -0.0020 -0.0622 0.0225  124 LEU A O   
1808  C CB  . LEU A 115 ? 0.8680  0.7473  0.9199  -0.0095 -0.0688 0.0506  124 LEU A CB  
1809  C CG  . LEU A 115 ? 0.8839  0.7758  0.9273  -0.0014 -0.0605 0.0550  124 LEU A CG  
1810  C CD1 . LEU A 115 ? 0.5900  0.5064  0.6390  -0.0009 -0.0654 0.0695  124 LEU A CD1 
1811  C CD2 . LEU A 115 ? 0.6519  0.5394  0.6793  -0.0020 -0.0562 0.0522  124 LEU A CD2 
1823  N N   . VAL A 116 ? 0.7169  0.5945  0.7999  0.0010  -0.0662 0.0468  125 VAL A N   
1824  C CA  . VAL A 116 ? 0.7036  0.5756  0.7906  0.0072  -0.0584 0.0359  125 VAL A CA  
1825  C C   . VAL A 116 ? 0.7014  0.5857  0.7752  0.0129  -0.0480 0.0369  125 VAL A C   
1826  O O   . VAL A 116 ? 0.8830  0.7828  0.9502  0.0137  -0.0482 0.0457  125 VAL A O   
1827  C CB  . VAL A 116 ? 0.5772  0.4490  0.6866  0.0059  -0.0680 0.0412  125 VAL A CB  
1828  C CG1 . VAL A 116 ? 0.5952  0.4491  0.7240  0.0019  -0.0809 0.0375  125 VAL A CG1 
1829  C CG2 . VAL A 116 ? 0.6932  0.5892  0.8026  0.0017  -0.0732 0.0604  125 VAL A CG2 
1839  N N   . TYR A 117 ? 0.7224  0.6006  0.7960  0.0170  -0.0400 0.0264  126 TYR A N   
1840  C CA  . TYR A 117 ? 0.6224  0.5053  0.6858  0.0220  -0.0313 0.0239  126 TYR A CA  
1841  C C   . TYR A 117 ? 0.4581  0.3624  0.5247  0.0244  -0.0329 0.0319  126 TYR A C   
1842  O O   . TYR A 117 ? 1.1950  1.1066  1.2553  0.0294  -0.0292 0.0307  126 TYR A O   
1843  C CB  . TYR A 117 ? 0.6234  0.4977  0.6900  0.0231  -0.0247 0.0122  126 TYR A CB  
1844  C CG  . TYR A 117 ? 0.9411  0.8165  1.0016  0.0263  -0.0175 0.0083  126 TYR A CG  
1845  C CD1 . TYR A 117 ? 0.8739  0.7625  0.9407  0.0290  -0.0181 0.0108  126 TYR A CD1 
1846  C CD2 . TYR A 117 ? 0.8112  0.6762  0.8608  0.0243  -0.0112 0.0018  126 TYR A CD2 
1847  C CE1 . TYR A 117 ? 0.8249  0.7132  0.8878  0.0315  -0.0125 0.0050  126 TYR A CE1 
1848  C CE2 . TYR A 117 ? 0.6950  0.5578  0.7413  0.0258  -0.0068 -0.0010 126 TYR A CE2 
1849  C CZ  . TYR A 117 ? 0.7009  0.5738  0.7546  0.0303  -0.0074 -0.0008 126 TYR A CZ  
1850  O OH  . TYR A 117 ? 0.8514  0.7214  0.9034  0.0314  -0.0038 -0.0061 126 TYR A OH  
1860  N N   . ALA A 118 ? 0.4857  0.4027  0.5641  0.0200  -0.0402 0.0402  127 ALA A N   
1861  C CA  . ALA A 118 ? 0.9142  0.8608  0.9944  0.0185  -0.0417 0.0476  127 ALA A CA  
1862  C C   . ALA A 118 ? 0.6962  0.6615  0.7724  0.0173  -0.0443 0.0549  127 ALA A C   
1863  O O   . ALA A 118 ? 0.4756  0.4733  0.5525  0.0164  -0.0434 0.0573  127 ALA A O   
1864  C CB  . ALA A 118 ? 0.8126  0.7709  0.9060  0.0099  -0.0517 0.0593  127 ALA A CB  
1870  N N   . ASP A 119 ? 0.5711  0.5210  0.6443  0.0156  -0.0480 0.0579  128 ASP A N   
1871  C CA  . ASP A 119 ? 0.6063  0.5705  0.6752  0.0155  -0.0500 0.0636  128 ASP A CA  
1872  C C   . ASP A 119 ? 0.8497  0.8087  0.9119  0.0260  -0.0426 0.0541  128 ASP A C   
1873  O O   . ASP A 119 ? 1.4490  1.4288  1.5149  0.0329  -0.0389 0.0494  128 ASP A O   
1874  C CB  . ASP A 119 ? 0.5355  0.4846  0.6042  0.0078  -0.0585 0.0706  128 ASP A CB  
1875  C CG  . ASP A 119 ? 0.6502  0.6077  0.7304  -0.0036 -0.0707 0.0843  128 ASP A CG  
1876  O OD1 . ASP A 119 ? 0.6178  0.6083  0.7015  -0.0086 -0.0734 0.0948  128 ASP A OD1 
1877  O OD2 . ASP A 119 ? 0.8994  0.8335  0.9862  -0.0086 -0.0787 0.0844  128 ASP A OD2 
1882  N N   . CYS A 120 ? 0.6494  0.5809  0.7037  0.0264  -0.0411 0.0501  129 CYS A N   
1883  C CA  . CYS A 120 ? 2.4226  2.3438  2.4706  0.0318  -0.0389 0.0471  129 CYS A CA  
1884  C C   . CYS A 120 ? 1.1382  1.0508  1.1871  0.0389  -0.0329 0.0376  129 CYS A C   
1885  O O   . CYS A 120 ? 0.7617  0.6632  0.8085  0.0430  -0.0337 0.0369  129 CYS A O   
1886  C CB  . CYS A 120 ? 9.4279  9.3283  9.4650  0.0241  -0.0405 0.0478  129 CYS A CB  
1887  S SG  . CYS A 120 ? 6.4079  6.2888  6.4418  0.0197  -0.0345 0.0361  129 CYS A SG  
1893  N N   . VAL A 121 ? 0.7777  0.6951  0.8310  0.0397  -0.0287 0.0314  130 VAL A N   
1894  C CA  . VAL A 121 ? 0.5626  0.4750  0.6183  0.0462  -0.0239 0.0214  130 VAL A CA  
1895  C C   . VAL A 121 ? 0.8601  0.8004  0.9248  0.0502  -0.0219 0.0156  130 VAL A C   
1896  O O   . VAL A 121 ? 0.8054  0.7538  0.8772  0.0589  -0.0206 0.0061  130 VAL A O   
1897  C CB  . VAL A 121 ? 0.6277  0.5193  0.6777  0.0416  -0.0196 0.0165  130 VAL A CB  
1898  C CG1 . VAL A 121 ? 0.6097  0.4970  0.6631  0.0470  -0.0160 0.0066  130 VAL A CG1 
1899  C CG2 . VAL A 121 ? 0.6129  0.4841  0.6519  0.0352  -0.0200 0.0193  130 VAL A CG2 
1909  N N   . LEU A 122 ? 0.5825  0.5398  0.6490  0.0432  -0.0229 0.0205  131 LEU A N   
1910  C CA  . LEU A 122 ? 0.7485  0.7379  0.8208  0.0438  -0.0205 0.0147  131 LEU A CA  
1911  C C   . LEU A 122 ? 0.9000  0.9279  0.9778  0.0450  -0.0219 0.0157  131 LEU A C   
1912  O O   . LEU A 122 ? 0.9978  1.0589  1.0805  0.0464  -0.0182 0.0057  131 LEU A O   
1913  C CB  . LEU A 122 ? 0.7567  0.7547  0.8302  0.0336  -0.0232 0.0225  131 LEU A CB  
1914  C CG  . LEU A 122 ? 0.7152  0.6829  0.7877  0.0329  -0.0216 0.0195  131 LEU A CG  
1915  C CD1 . LEU A 122 ? 0.6003  0.5746  0.6801  0.0241  -0.0278 0.0293  131 LEU A CD1 
1916  C CD2 . LEU A 122 ? 0.7233  0.6858  0.7939  0.0386  -0.0146 0.0050  131 LEU A CD2 
1928  N N   . ALA A 123 ? 0.6932  0.7231  0.7708  0.0429  -0.0269 0.0266  132 ALA A N   
1929  C CA  . ALA A 123 ? 0.8571  0.9301  0.9408  0.0416  -0.0285 0.0292  132 ALA A CA  
1930  C C   . ALA A 123 ? 0.8791  0.9485  0.9684  0.0518  -0.0297 0.0261  132 ALA A C   
1931  O O   . ALA A 123 ? 0.6638  0.7708  0.7608  0.0521  -0.0309 0.0272  132 ALA A O   
1932  C CB  . ALA A 123 ? 0.7148  0.8034  0.7959  0.0254  -0.0365 0.0494  132 ALA A CB  
1938  N N   . ASN A 124 ? 0.7319  0.7608  0.8187  0.0592  -0.0301 0.0229  133 ASN A N   
1939  C CA  . ASN A 124 ? 0.5661  0.5837  0.6576  0.0664  -0.0348 0.0253  133 ASN A CA  
1940  C C   . ASN A 124 ? 0.6126  0.6236  0.7186  0.0818  -0.0342 0.0098  133 ASN A C   
1941  O O   . ASN A 124 ? 0.5391  0.5154  0.6437  0.0847  -0.0390 0.0133  133 ASN A O   
1942  C CB  . ASN A 124 ? 0.5238  0.5014  0.6011  0.0595  -0.0380 0.0356  133 ASN A CB  
1943  C CG  . ASN A 124 ? 0.6009  0.5682  0.6787  0.0615  -0.0449 0.0435  133 ASN A CG  
1944  O OD1 . ASN A 124 ? 0.7556  0.7472  0.8448  0.0666  -0.0489 0.0457  133 ASN A OD1 
1945  N ND2 . ASN A 124 ? 0.6786  0.6141  0.7428  0.0546  -0.0468 0.0494  133 ASN A ND2 
1952  N N   . TRP A 125 ? 0.8666  0.9106  0.9873  0.0902  -0.0298 -0.0075 134 TRP A N   
1953  C CA  . TRP A 125 ? 0.8946  0.9261  1.0331  0.1056  -0.0309 -0.0261 134 TRP A CA  
1954  C C   . TRP A 125 ? 0.8033  0.8832  0.9645  0.1173  -0.0270 -0.0491 134 TRP A C   
1955  O O   . TRP A 125 ? 0.5713  0.6968  0.7287  0.1100  -0.0203 -0.0532 134 TRP A O   
1956  C CB  . TRP A 125 ? 0.8272  0.8263  0.9569  0.1029  -0.0278 -0.0322 134 TRP A CB  
1957  C CG  . TRP A 125 ? 0.6626  0.6895  0.7871  0.0970  -0.0195 -0.0417 134 TRP A CG  
1958  C CD1 . TRP A 125 ? 0.6578  0.6908  0.7654  0.0825  -0.0166 -0.0291 134 TRP A CD1 
1959  C CD2 . TRP A 125 ? 0.7940  0.8514  0.9324  0.1046  -0.0145 -0.0665 134 TRP A CD2 
1960  N NE1 . TRP A 125 ? 0.6714  0.7377  0.7797  0.0789  -0.0108 -0.0408 134 TRP A NE1 
1961  C CE2 . TRP A 125 ? 0.7374  0.8205  0.8623  0.0916  -0.0083 -0.0649 134 TRP A CE2 
1962  C CE3 . TRP A 125 ? 0.9126  0.9786  1.0756  0.1210  -0.0156 -0.0912 134 TRP A CE3 
1963  C CZ2 . TRP A 125 ? 0.8721  0.9915  1.0028  0.0922  -0.0022 -0.0863 134 TRP A CZ2 
1964  C CZ3 . TRP A 125 ? 1.0826  1.1843  1.2535  0.1235  -0.0086 -0.1168 134 TRP A CZ3 
1965  C CH2 . TRP A 125 ? 0.9939  1.1236  1.1463  0.1080  -0.0013 -0.1137 134 TRP A CH2 
1976  N N   . LYS A 126 ? 0.7412  0.8115  0.9279  0.1348  -0.0322 -0.0657 135 LYS A N   
1977  C CA  . LYS A 126 ? 0.9594  1.0753  1.1745  0.1496  -0.0289 -0.0944 135 LYS A CA  
1978  C C   . LYS A 126 ? 1.1786  1.2608  1.4163  0.1652  -0.0347 -0.1153 135 LYS A C   
1979  O O   . LYS A 126 ? 0.5349  0.5621  0.7707  0.1654  -0.0447 -0.1014 135 LYS A O   
1980  C CB  . LYS A 126 ? 0.7831  0.9342  1.0185  0.1581  -0.0330 -0.0937 135 LYS A CB  
1981  C CG  . LYS A 126 ? 1.2637  1.3742  1.5122  0.1668  -0.0475 -0.0786 135 LYS A CG  
1982  C CD  . LYS A 126 ? 1.2773  1.4288  1.5558  0.1800  -0.0522 -0.0855 135 LYS A CD  
1991  N N   . LYS A 127 ? 2.1407  2.2563  2.3979  0.1752  -0.0287 -0.1482 136 LYS A N   
1992  C CA  . LYS A 127 ? 1.5598  1.6477  1.8493  0.1939  -0.0371 -0.1731 136 LYS A CA  
1993  C C   . LYS A 127 ? 2.8669  2.9817  3.1985  0.2154  -0.0440 -0.1914 136 LYS A C   
1994  O O   . LYS A 127 ? 2.2199  2.3997  2.5600  0.2180  -0.0349 -0.2061 136 LYS A O   
1995  C CB  . LYS A 127 ? 1.2842  1.3859  1.5744  0.1936  -0.0286 -0.2026 136 LYS A CB  
1996  C CG  . LYS A 127 ? 1.0748  1.2529  1.3658  0.1913  -0.0142 -0.2274 136 LYS A CG  
1997  C CD  . LYS A 127 ? 1.3555  1.5439  1.6313  0.1813  -0.0052 -0.2445 136 LYS A CD  
1998  C CE  . LYS A 127 ? 1.4711  1.6166  1.7709  0.1951  -0.0128 -0.2709 136 LYS A CE  
1999  N NZ  . LYS A 127 ? 1.0900  1.2562  1.3781  0.1860  -0.0035 -0.2932 136 LYS A NZ  
2013  N N   . LYS A 128 ? 2.4670  2.5332  2.8253  0.2289  -0.0615 -0.1872 137 LYS A N   
2014  C CA  . LYS A 128 ? 2.0759  2.1597  2.4798  0.2511  -0.0721 -0.2012 137 LYS A CA  
2015  C C   . LYS A 128 ? 2.5278  2.6618  2.9694  0.2702  -0.0653 -0.2510 137 LYS A C   
2016  O O   . LYS A 128 ? 2.4614  2.6601  2.9214  0.2784  -0.0581 -0.2684 137 LYS A O   
2017  C CB  . LYS A 128 ? 1.5667  1.5823  1.9946  0.2603  -0.0955 -0.1872 137 LYS A CB  
2018  C CG  . LYS A 128 ? 0.6570  0.6344  1.0529  0.2423  -0.1032 -0.1409 137 LYS A CG  
2019  C CD  . LYS A 128 ? 0.6743  0.5810  1.0843  0.2430  -0.1274 -0.1202 137 LYS A CD  
2020  C CE  . LYS A 128 ? 0.8507  0.7308  1.2261  0.2221  -0.1341 -0.0745 137 LYS A CE  
2021  N NZ  . LYS A 128 ? 1.2728  1.0925  1.6531  0.2155  -0.1561 -0.0500 137 LYS A NZ  
2035  N N   . ASP A 129 ? 1.2613  1.3696  1.7149  0.2762  -0.0672 -0.2759 138 ASP A N   
2036  C CA  . ASP A 129 ? 0.8022  0.9568  1.2899  0.2929  -0.0600 -0.3286 138 ASP A CA  
2037  C C   . ASP A 129 ? 2.3710  2.5559  2.8218  0.2743  -0.0410 -0.3402 138 ASP A C   
2038  O O   . ASP A 129 ? 0.9202  1.0573  1.3540  0.2655  -0.0437 -0.3354 138 ASP A O   
2039  C CB  . ASP A 129 ? 0.8952  0.9969  1.4323  0.3152  -0.0798 -0.3526 138 ASP A CB  
2040  C CG  . ASP A 129 ? 0.9695  1.1168  1.5351  0.3252  -0.0739 -0.4026 138 ASP A CG  
2041  O OD1 . ASP A 129 ? 1.1328  1.3557  1.6875  0.3209  -0.0533 -0.4281 138 ASP A OD1 
2042  O OD2 . ASP A 129 ? 1.9512  2.0598  2.5484  0.3344  -0.0908 -0.4146 138 ASP A OD2 
2047  N N   . PRO A 130 ? 1.3357  1.6012  1.7738  0.2663  -0.0230 -0.3542 139 PRO A N   
2048  C CA  . PRO A 130 ? 1.1353  1.4346  1.5381  0.2460  -0.0069 -0.3619 139 PRO A CA  
2049  C C   . PRO A 130 ? 1.2785  1.5576  1.6936  0.2518  -0.0075 -0.3967 139 PRO A C   
2050  O O   . PRO A 130 ? 1.3330  1.5967  1.7135  0.2329  -0.0021 -0.3852 139 PRO A O   
2051  C CB  . PRO A 130 ? 1.0887  1.4884  1.4963  0.2434  0.0082  -0.3843 139 PRO A CB  
2052  C CG  . PRO A 130 ? 0.9615  1.3693  1.3833  0.2510  0.0017  -0.3632 139 PRO A CG  
2053  C CD  . PRO A 130 ? 0.8944  1.2250  1.3465  0.2713  -0.0181 -0.3562 139 PRO A CD  
2061  N N   . ASN A 131 ? 1.2266  1.5050  1.6929  0.2776  -0.0151 -0.4399 140 ASN A N   
2062  C CA  . ASN A 131 ? 1.0999  1.3647  1.5746  0.2785  -0.0156 -0.4736 140 ASN A CA  
2063  C C   . ASN A 131 ? 1.3736  1.5463  1.8392  0.2749  -0.0297 -0.4509 140 ASN A C   
2064  O O   . ASN A 131 ? 1.4268  1.5879  1.8764  0.2640  -0.0260 -0.4622 140 ASN A O   
2065  C CB  . ASN A 131 ? 0.8437  1.1237  1.3609  0.2932  -0.0240 -0.5091 140 ASN A CB  
2066  C CG  . ASN A 131 ? 1.0670  1.4484  1.5864  0.2899  -0.0070 -0.5415 140 ASN A CG  
2067  O OD1 . ASN A 131 ? 1.3040  1.7399  1.8103  0.2851  0.0041  -0.5286 140 ASN A OD1 
2068  N ND2 . ASN A 131 ? 1.6058  2.0159  2.1415  0.2902  -0.0056 -0.5828 140 ASN A ND2 
2075  N N   . LYS A 132 ? 1.4353  1.5474  1.9026  0.2773  -0.0451 -0.4125 141 LYS A N   
2076  C CA  . LYS A 132 ? 1.4446  1.4738  1.9025  0.2698  -0.0599 -0.3878 141 LYS A CA  
2077  C C   . LYS A 132 ? 1.0927  1.1122  1.4915  0.2408  -0.0492 -0.3487 141 LYS A C   
2078  O O   . LYS A 132 ? 1.1712  1.2351  1.5393  0.2279  -0.0353 -0.3309 141 LYS A O   
2079  C CB  . LYS A 132 ? 1.4724  1.4459  1.9565  0.2814  -0.0823 -0.3619 141 LYS A CB  
2080  C CG  . LYS A 132 ? 1.1979  1.1760  1.7281  0.2978  -0.0955 -0.3854 141 LYS A CG  
2081  C CD  . LYS A 132 ? 1.0067  0.9363  1.5584  0.3044  -0.1184 -0.3530 141 LYS A CD  
2082  C CE  . LYS A 132 ? 1.2663  1.1859  1.8655  0.3189  -0.1358 -0.3732 141 LYS A CE  
2083  N NZ  . LYS A 132 ? 1.4343  1.3250  2.0533  0.3251  -0.1553 -0.3419 141 LYS A NZ  
2097  N N   . PRO A 133 ? 1.0233  0.9862  1.4082  0.2299  -0.0566 -0.3352 142 PRO A N   
2098  C CA  . PRO A 133 ? 1.0713  1.0285  1.4061  0.2042  -0.0464 -0.3045 142 PRO A CA  
2099  C C   . PRO A 133 ? 1.2221  1.1522  1.5319  0.1933  -0.0500 -0.2568 142 PRO A C   
2100  O O   . PRO A 133 ? 0.8837  0.7936  1.2126  0.2036  -0.0620 -0.2445 142 PRO A O   
2101  C CB  . PRO A 133 ? 1.1682  1.0746  1.5051  0.1986  -0.0553 -0.3104 142 PRO A CB  
2102  C CG  . PRO A 133 ? 1.1254  0.9857  1.5081  0.2175  -0.0769 -0.3223 142 PRO A CG  
2103  C CD  . PRO A 133 ? 0.9651  0.8720  1.3842  0.2405  -0.0751 -0.3530 142 PRO A CD  
2111  N N   . LEU A 134 ? 1.1214  1.0506  1.3904  0.1722  -0.0406 -0.2314 143 LEU A N   
2112  C CA  . LEU A 134 ? 0.9219  0.8319  1.1641  0.1597  -0.0414 -0.1903 143 LEU A CA  
2113  C C   . LEU A 134 ? 0.9311  0.7770  1.1712  0.1534  -0.0554 -0.1680 143 LEU A C   
2114  O O   . LEU A 134 ? 0.9510  0.7771  1.1644  0.1364  -0.0524 -0.1491 143 LEU A O   
2115  C CB  . LEU A 134 ? 0.9980  0.9348  1.2041  0.1412  -0.0272 -0.1758 143 LEU A CB  
2116  C CG  . LEU A 134 ? 1.1370  1.1391  1.3378  0.1400  -0.0152 -0.1849 143 LEU A CG  
2117  C CD1 . LEU A 134 ? 0.7106  0.7395  0.8844  0.1222  -0.0049 -0.1779 143 LEU A CD1 
2118  C CD2 . LEU A 134 ? 1.6123  1.6208  1.8085  0.1401  -0.0170 -0.1613 143 LEU A CD2 
2130  N N   . THR A 135 ? 0.6913  0.5081  0.9610  0.1662  -0.0720 -0.1681 144 THR A N   
2131  C CA  . THR A 135 ? 0.8345  0.5960  1.1017  0.1571  -0.0880 -0.1402 144 THR A CA  
2132  C C   . THR A 135 ? 0.7551  0.5175  1.0164  0.1561  -0.0927 -0.1128 144 THR A C   
2133  O O   . THR A 135 ? 0.8477  0.6438  1.1223  0.1689  -0.0896 -0.1214 144 THR A O   
2134  C CB  . THR A 135 ? 1.0204  0.7408  1.3279  0.1690  -0.1091 -0.1545 144 THR A CB  
2135  O OG1 . THR A 135 ? 1.2106  0.9382  1.5555  0.1900  -0.1201 -0.1642 144 THR A OG1 
2136  C CG2 . THR A 135 ? 1.0601  0.7912  1.3821  0.1758  -0.1038 -0.1930 144 THR A CG2 
2144  N N   . TYR A 136 ? 0.8881  0.6151  1.1315  0.1400  -0.1016 -0.0807 145 TYR A N   
2145  C CA  . TYR A 136 ? 0.9910  0.7188  1.2235  0.1346  -0.1062 -0.0529 145 TYR A CA  
2146  C C   . TYR A 136 ? 0.9302  0.6586  1.2005  0.1539  -0.1214 -0.0571 145 TYR A C   
2147  O O   . TYR A 136 ? 0.7859  0.5411  1.0541  0.1578  -0.1182 -0.0499 145 TYR A O   
2148  C CB  . TYR A 136 ? 0.9785  0.6705  1.1889  0.1126  -0.1154 -0.0211 145 TYR A CB  
2149  C CG  . TYR A 136 ? 1.0411  0.7372  1.2335  0.1021  -0.1188 0.0079  145 TYR A CG  
2150  C CD1 . TYR A 136 ? 0.9582  0.6377  1.1730  0.1071  -0.1395 0.0237  145 TYR A CD1 
2151  C CD2 . TYR A 136 ? 0.9905  0.7069  1.1457  0.0867  -0.1028 0.0188  145 TYR A CD2 
2152  C CE1 . TYR A 136 ? 0.9881  0.6735  1.1847  0.0951  -0.1434 0.0505  145 TYR A CE1 
2153  C CE2 . TYR A 136 ? 0.7271  0.4483  0.8654  0.0757  -0.1059 0.0420  145 TYR A CE2 
2154  C CZ  . TYR A 136 ? 0.9746  0.6811  1.1315  0.0788  -0.1258 0.0584  145 TYR A CZ  
2155  O OH  . TYR A 136 ? 1.0613  0.7748  1.2011  0.0664  -0.1301 0.0814  145 TYR A OH  
2165  N N   . GLU A 137 ? 1.1412  0.8396  1.4493  0.1659  -0.1398 -0.0684 146 GLU A N   
2166  C CA  . GLU A 137 ? 1.4405  1.1378  1.7912  0.1859  -0.1571 -0.0723 146 GLU A CA  
2167  C C   . GLU A 137 ? 1.2053  0.9572  1.5743  0.2063  -0.1431 -0.1041 146 GLU A C   
2168  O O   . GLU A 137 ? 1.2472  1.0116  1.6482  0.2226  -0.1534 -0.1067 146 GLU A O   
2169  C CB  . GLU A 137 ? 1.5636  1.2153  1.9580  0.1964  -0.1820 -0.0812 146 GLU A CB  
2170  C CG  . GLU A 137 ? 1.6928  1.2920  2.0799  0.1762  -0.2048 -0.0412 146 GLU A CG  
2171  C CD  . GLU A 137 ? 1.8466  1.4335  2.1882  0.1493  -0.1936 -0.0263 146 GLU A CD  
2172  O OE1 . GLU A 137 ? 2.0737  1.6420  2.3891  0.1258  -0.2015 0.0110  146 GLU A OE1 
2173  O OE2 . GLU A 137 ? 1.6530  1.2526  1.9866  0.1512  -0.1773 -0.0529 146 GLU A OE2 
2180  N N   . ASN A 138 ? 0.8059  0.5936  1.1572  0.2048  -0.1212 -0.1279 147 ASN A N   
2181  C CA  . ASN A 138 ? 1.1502  0.9986  1.5140  0.2191  -0.1067 -0.1568 147 ASN A CA  
2182  C C   . ASN A 138 ? 1.1635  1.0509  1.4890  0.2050  -0.0901 -0.1376 147 ASN A C   
2183  O O   . ASN A 138 ? 0.9663  0.9094  1.2927  0.2097  -0.0762 -0.1558 147 ASN A O   
2184  C CB  . ASN A 138 ? 1.1138  0.9836  1.4855  0.2248  -0.0953 -0.1962 147 ASN A CB  
2185  C CG  . ASN A 138 ? 1.2236  1.1611  1.6200  0.2420  -0.0838 -0.2336 147 ASN A CG  
2186  O OD1 . ASN A 138 ? 1.4076  1.3597  1.8408  0.2606  -0.0927 -0.2433 147 ASN A OD1 
2187  N ND2 . ASN A 138 ? 1.3202  1.3015  1.6988  0.2353  -0.0653 -0.2553 147 ASN A ND2 
2194  N N   . MET A 139 ? 1.1010  0.9623  1.3938  0.1865  -0.0920 -0.1019 148 MET A N   
2195  C CA  . MET A 139 ? 1.0067  0.8972  1.2633  0.1715  -0.0774 -0.0857 148 MET A CA  
2196  C C   . MET A 139 ? 0.8116  0.6940  1.0613  0.1661  -0.0863 -0.0564 148 MET A C   
2197  O O   . MET A 139 ? 0.8746  0.7203  1.1347  0.1662  -0.1031 -0.0401 148 MET A O   
2198  C CB  . MET A 139 ? 1.0703  0.9434  1.2910  0.1523  -0.0675 -0.0768 148 MET A CB  
2199  C CG  . MET A 139 ? 0.5780  0.4711  0.8006  0.1546  -0.0565 -0.1045 148 MET A CG  
2200  S SD  . MET A 139 ? 1.1572  1.0268  1.3494  0.1361  -0.0494 -0.0970 148 MET A SD  
2201  C CE  . MET A 139 ? 1.0052  0.9073  1.1657  0.1216  -0.0365 -0.0782 148 MET A CE  
2211  N N   . ASP A 140 ? 0.5757  0.4938  0.8074  0.1593  -0.0762 -0.0486 149 ASP A N   
2212  C CA  . ASP A 140 ? 1.0452  0.9605  1.2622  0.1497  -0.0814 -0.0216 149 ASP A CA  
2213  C C   . ASP A 140 ? 0.9380  0.8754  1.1220  0.1335  -0.0674 -0.0130 149 ASP A C   
2214  O O   . ASP A 140 ? 0.7595  0.7227  0.9383  0.1324  -0.0555 -0.0273 149 ASP A O   
2215  C CB  . ASP A 140 ? 1.3037  1.2460  1.5507  0.1644  -0.0896 -0.0248 149 ASP A CB  
2216  C CG  . ASP A 140 ? 1.5347  1.4486  1.7858  0.1614  -0.1069 0.0003  149 ASP A CG  
2217  O OD1 . ASP A 140 ? 1.7859  1.6795  2.0041  0.1420  -0.1068 0.0239  149 ASP A OD1 
2218  O OD2 . ASP A 140 ? 1.5781  1.4911  1.8672  0.1783  -0.1214 -0.0046 149 ASP A OD2 
2223  N N   . VAL A 141 ? 1.0218  0.9470  1.1838  0.1195  -0.0704 0.0105  150 VAL A N   
2224  C CA  . VAL A 141 ? 0.8000  0.7449  0.9377  0.1056  -0.0612 0.0191  150 VAL A CA  
2225  C C   . VAL A 141 ? 0.7793  0.7606  0.9272  0.1090  -0.0635 0.0228  150 VAL A C   
2226  O O   . VAL A 141 ? 1.2878  1.2740  1.4579  0.1201  -0.0730 0.0231  150 VAL A O   
2227  C CB  . VAL A 141 ? 0.7345  0.6524  0.8443  0.0881  -0.0624 0.0378  150 VAL A CB  
2228  C CG1 . VAL A 141 ? 0.8806  0.7670  0.9797  0.0826  -0.0600 0.0356  150 VAL A CG1 
2229  C CG2 . VAL A 141 ? 0.5896  0.4977  0.7005  0.0854  -0.0747 0.0548  150 VAL A CG2 
2239  N N   . LEU A 142 ? 1.0272  1.0320  1.1601  0.0978  -0.0572 0.0284  151 LEU A N   
2240  C CA  . LEU A 142 ? 0.8930  0.9334  1.0333  0.0970  -0.0602 0.0350  151 LEU A CA  
2241  C C   . LEU A 142 ? 0.9623  0.9863  1.0875  0.0851  -0.0680 0.0561  151 LEU A C   
2242  O O   . LEU A 142 ? 1.5621  1.6081  1.6984  0.0874  -0.0744 0.0627  151 LEU A O   
2243  C CB  . LEU A 142 ? 0.8876  0.9667  1.0225  0.0889  -0.0520 0.0320  151 LEU A CB  
2244  C CG  . LEU A 142 ? 0.6210  0.7267  0.7662  0.0958  -0.0434 0.0116  151 LEU A CG  
2245  C CD1 . LEU A 142 ? 0.5111  0.6545  0.6444  0.0795  -0.0386 0.0188  151 LEU A CD1 
2246  C CD2 . LEU A 142 ? 0.6386  0.7768  0.8133  0.1135  -0.0435 -0.0078 151 LEU A CD2 
2258  N N   . PHE A 143 ? 0.8007  0.7911  0.9020  0.0719  -0.0674 0.0649  152 PHE A N   
2259  C CA  . PHE A 143 ? 0.8190  0.8020  0.9048  0.0584  -0.0734 0.0805  152 PHE A CA  
2260  C C   . PHE A 143 ? 0.7565  0.7027  0.8244  0.0496  -0.0758 0.0864  152 PHE A C   
2261  O O   . PHE A 143 ? 0.9364  0.8624  0.9980  0.0493  -0.0702 0.0793  152 PHE A O   
2262  C CB  . PHE A 143 ? 0.6349  0.6310  0.7091  0.0456  -0.0698 0.0838  152 PHE A CB  
2263  C CG  . PHE A 143 ? 0.6502  0.6893  0.7387  0.0486  -0.0685 0.0822  152 PHE A CG  
2264  C CD1 . PHE A 143 ? 0.8765  0.9452  0.9761  0.0497  -0.0746 0.0893  152 PHE A CD1 
2265  C CD2 . PHE A 143 ? 0.5710  0.6257  0.6618  0.0484  -0.0613 0.0741  152 PHE A CD2 
2266  C CE1 . PHE A 143 ? 0.5987  0.7139  0.7109  0.0501  -0.0724 0.0872  152 PHE A CE1 
2267  C CE2 . PHE A 143 ? 0.5847  0.6843  0.6856  0.0471  -0.0598 0.0735  152 PHE A CE2 
2268  C CZ  . PHE A 143 ? 0.4626  0.5954  0.5745  0.0477  -0.0648 0.0795  152 PHE A CZ  
2278  N N   . SER A 144 ? 0.9928  0.9357  1.0509  0.0397  -0.0837 0.0996  153 SER A N   
2279  C CA  . SER A 144 ? 0.7871  0.7049  0.8265  0.0276  -0.0870 0.1067  153 SER A CA  
2280  C C   . SER A 144 ? 0.7597  0.6826  0.7807  0.0109  -0.0905 0.1149  153 SER A C   
2281  O O   . SER A 144 ? 0.7590  0.7016  0.7845  0.0097  -0.0929 0.1177  153 SER A O   
2282  C CB  . SER A 144 ? 0.9403  0.8476  0.9920  0.0338  -0.0983 0.1162  153 SER A CB  
2283  O OG  . SER A 144 ? 0.9089  0.8090  0.9791  0.0490  -0.0956 0.1051  153 SER A OG  
2289  N N   . PHE A 145 ? 0.6133  0.5214  0.6131  -0.0041 -0.0908 0.1176  154 PHE A N   
2290  C CA  . PHE A 145 ? 0.7663  0.6804  0.7469  -0.0217 -0.0933 0.1207  154 PHE A CA  
2291  C C   . PHE A 145 ? 0.9042  0.8226  0.8758  -0.0329 -0.1056 0.1382  154 PHE A C   
2292  O O   . PHE A 145 ? 1.1726  1.1053  1.1396  -0.0411 -0.1122 0.1452  154 PHE A O   
2293  C CB  . PHE A 145 ? 0.9472  0.8512  0.9098  -0.0331 -0.0833 0.1058  154 PHE A CB  
2294  C CG  . PHE A 145 ? 0.9731  0.8734  0.9455  -0.0249 -0.0744 0.0909  154 PHE A CG  
2295  C CD1 . PHE A 145 ? 1.0518  0.9599  1.0304  -0.0258 -0.0761 0.0880  154 PHE A CD1 
2296  C CD2 . PHE A 145 ? 0.8208  0.7102  0.7969  -0.0181 -0.0663 0.0820  154 PHE A CD2 
2297  C CE1 . PHE A 145 ? 0.7452  0.6496  0.7350  -0.0202 -0.0710 0.0781  154 PHE A CE1 
2298  C CE2 . PHE A 145 ? 0.9238  0.8112  0.9101  -0.0116 -0.0599 0.0705  154 PHE A CE2 
2299  C CZ  . PHE A 145 ? 0.8561  0.7511  0.8497  -0.0129 -0.0631 0.0698  154 PHE A CZ  
2309  N N   . ARG A 146 ? 0.8440  0.7508  0.8108  -0.0371 -0.1099 0.1468  155 ARG A N   
2310  C CA  . ARG A 146 ? 0.9127  0.8242  0.8733  -0.0493 -0.1251 0.1686  155 ARG A CA  
2311  C C   . ARG A 146 ? 0.7883  0.6842  0.7684  -0.0390 -0.1356 0.1813  155 ARG A C   
2312  O O   . ARG A 146 ? 1.4847  1.3656  1.4750  -0.0273 -0.1288 0.1708  155 ARG A O   
2313  C CB  . ARG A 146 ? 0.8385  0.7561  0.7662  -0.0764 -0.1237 0.1701  155 ARG A CB  
2314  C CG  . ARG A 146 ? 0.7068  0.6372  0.6177  -0.0869 -0.1143 0.1525  155 ARG A CG  
2315  C CD  . ARG A 146 ? 0.8717  0.8180  0.7844  -0.0905 -0.1234 0.1605  155 ARG A CD  
2316  N NE  . ARG A 146 ? 0.7194  0.6808  0.6148  -0.1113 -0.1364 0.1794  155 ARG A NE  
2317  C CZ  . ARG A 146 ? 0.9011  0.8751  0.7672  -0.1359 -0.1337 0.1739  155 ARG A CZ  
2318  N NH1 . ARG A 146 ? 0.8994  0.8711  0.7534  -0.1406 -0.1182 0.1482  155 ARG A NH1 
2319  N NH2 . ARG A 146 ? 1.1253  1.1173  0.9757  -0.1562 -0.1468 0.1932  155 ARG A NH2 
2333  N N   . ASP A 147 ? 0.8559  0.7545  0.8433  -0.0437 -0.1542 0.2043  156 ASP A N   
2334  C CA  . ASP A 147 ? 0.9170  0.7970  0.9277  -0.0350 -0.1693 0.2187  156 ASP A CA  
2335  C C   . ASP A 147 ? 1.4210  1.2846  1.4115  -0.0523 -0.1680 0.2237  156 ASP A C   
2336  O O   . ASP A 147 ? 1.1828  1.0565  1.1427  -0.0788 -0.1689 0.2337  156 ASP A O   
2337  C CB  . ASP A 147 ? 1.2799  1.1670  1.3053  -0.0384 -0.1931 0.2458  156 ASP A CB  
2338  C CG  . ASP A 147 ? 1.4587  1.3659  1.5099  -0.0195 -0.1953 0.2410  156 ASP A CG  
2339  O OD1 . ASP A 147 ? 1.2134  1.1217  1.2885  0.0040  -0.1860 0.2212  156 ASP A OD1 
2340  O OD2 . ASP A 147 ? 1.7932  1.7192  1.8406  -0.0296 -0.2063 0.2568  156 ASP A OD2 
2345  N N   . GLY A 148 ? 1.8835  1.7255  1.8910  -0.0392 -0.1663 0.2162  157 GLY A N   
2346  C CA  . GLY A 148 ? 1.4196  1.2484  1.4086  -0.0574 -0.1658 0.2224  157 GLY A CA  
2347  C C   . GLY A 148 ? 0.9902  0.8315  0.9480  -0.0702 -0.1434 0.2026  157 GLY A C   
2348  O O   . GLY A 148 ? 1.0280  0.8765  0.9594  -0.0949 -0.1418 0.2092  157 GLY A O   
2352  N N   . ASP A 149 ? 1.1279  0.9762  1.0894  -0.0553 -0.1273 0.1789  158 ASP A N   
2353  C CA  . ASP A 149 ? 1.1352  0.9888  1.0785  -0.0611 -0.1078 0.1573  158 ASP A CA  
2354  C C   . ASP A 149 ? 1.2749  1.1107  1.2289  -0.0513 -0.1013 0.1475  158 ASP A C   
2355  O O   . ASP A 149 ? 0.9482  0.7876  0.8939  -0.0519 -0.0856 0.1285  158 ASP A O   
2356  C CB  . ASP A 149 ? 1.1034  0.9692  1.0498  -0.0505 -0.0970 0.1392  158 ASP A CB  
2357  C CG  . ASP A 149 ? 1.0504  0.9130  1.0264  -0.0254 -0.0995 0.1361  158 ASP A CG  
2358  O OD1 . ASP A 149 ? 1.3996  1.2529  1.3955  -0.0151 -0.1113 0.1470  158 ASP A OD1 
2359  O OD2 . ASP A 149 ? 0.9069  0.7778  0.8882  -0.0164 -0.0903 0.1220  158 ASP A OD2 
2364  N N   . CYS A 150 ? 1.7395  1.5562  1.7163  -0.0398 -0.1137 0.1576  159 CYS A N   
2365  C CA  . CYS A 150 ? 2.5222  2.3208  2.5103  -0.0315 -0.1097 0.1484  159 CYS A CA  
2366  C C   . CYS A 150 ? 1.6764  1.4809  1.6722  -0.0143 -0.0929 0.1232  159 CYS A C   
2367  O O   . CYS A 150 ? 0.8387  0.6353  0.8361  -0.0113 -0.0844 0.1112  159 CYS A O   
2368  C CB  . CYS A 150 ? 4.3024  4.0988  4.2680  -0.0548 -0.1071 0.1542  159 CYS A CB  
2369  S SG  . CYS A 150 ? 4.6355  4.4201  4.5991  -0.0757 -0.1328 0.1901  159 CYS A SG  
2375  N N   . SER A 151 ? 0.9831  0.8037  0.9830  -0.0053 -0.0890 0.1167  160 SER A N   
2376  C CA  . SER A 151 ? 0.6721  0.5012  0.6791  0.0076  -0.0756 0.0970  160 SER A CA  
2377  C C   . SER A 151 ? 0.6756  0.4981  0.7072  0.0266  -0.0761 0.0877  160 SER A C   
2378  O O   . SER A 151 ? 0.7733  0.5989  0.8070  0.0323  -0.0652 0.0726  160 SER A O   
2379  C CB  . SER A 151 ? 0.6981  0.5470  0.7049  0.0100  -0.0741 0.0956  160 SER A CB  
2380  O OG  . SER A 151 ? 0.8375  0.6949  0.8602  0.0189  -0.0848 0.1049  160 SER A OG  
2386  N N   . LYS A 152 ? 0.6504  0.4649  0.7026  0.0364  -0.0893 0.0947  161 LYS A N   
2387  C CA  . LYS A 152 ? 0.8388  0.6473  0.9157  0.0539  -0.0896 0.0807  161 LYS A CA  
2388  C C   . LYS A 152 ? 0.9438  0.7332  1.0129  0.0472  -0.0848 0.0753  161 LYS A C   
2389  O O   . LYS A 152 ? 0.7919  0.5858  0.8670  0.0556  -0.0751 0.0579  161 LYS A O   
2390  C CB  . LYS A 152 ? 0.8595  0.6586  0.9658  0.0662  -0.1076 0.0877  161 LYS A CB  
2391  C CG  . LYS A 152 ? 1.0033  0.8029  1.1408  0.0876  -0.1075 0.0662  161 LYS A CG  
2392  C CD  . LYS A 152 ? 1.1551  0.9446  1.3291  0.1025  -0.1267 0.0689  161 LYS A CD  
2393  C CE  . LYS A 152 ? 1.0678  0.8559  1.2749  0.1233  -0.1270 0.0424  161 LYS A CE  
2394  N NZ  . LYS A 152 ? 1.0303  0.7980  1.2779  0.1375  -0.1496 0.0448  161 LYS A NZ  
2408  N N   . GLY A 153 ? 0.8231  0.5957  0.8767  0.0294  -0.0911 0.0909  162 GLY A N   
2409  C CA  . GLY A 153 ? 0.8950  0.6514  0.9427  0.0212  -0.0881 0.0877  162 GLY A CA  
2410  C C   . GLY A 153 ? 1.4389  1.2092  1.4702  0.0170  -0.0693 0.0727  162 GLY A C   
2411  O O   . GLY A 153 ? 1.0548  0.8229  1.0938  0.0243  -0.0625 0.0582  162 GLY A O   
2415  N N   . PHE A 154 ? 1.1579  0.9443  1.1698  0.0063  -0.0618 0.0746  163 PHE A N   
2416  C CA  . PHE A 154 ? 1.0889  0.8867  1.0894  0.0015  -0.0468 0.0612  163 PHE A CA  
2417  C C   . PHE A 154 ? 1.0087  0.8160  1.0230  0.0175  -0.0393 0.0460  163 PHE A C   
2418  O O   . PHE A 154 ? 0.7841  0.5948  0.7979  0.0173  -0.0303 0.0350  163 PHE A O   
2419  C CB  . PHE A 154 ? 1.0919  0.9046  1.0747  -0.0108 -0.0427 0.0631  163 PHE A CB  
2420  C CG  . PHE A 154 ? 1.0447  0.8683  1.0192  -0.0173 -0.0298 0.0486  163 PHE A CG  
2421  C CD1 . PHE A 154 ? 1.4135  1.2374  1.3793  -0.0294 -0.0249 0.0461  163 PHE A CD1 
2422  C CD2 . PHE A 154 ? 1.1307  0.9655  1.1085  -0.0122 -0.0241 0.0380  163 PHE A CD2 
2423  C CE1 . PHE A 154 ? 1.4708  1.3084  1.4337  -0.0337 -0.0134 0.0305  163 PHE A CE1 
2424  C CE2 . PHE A 154 ? 1.2134  1.0566  1.1900  -0.0161 -0.0149 0.0237  163 PHE A CE2 
2425  C CZ  . PHE A 154 ? 1.3192  1.1652  1.2893  -0.0259 -0.0089 0.0185  163 PHE A CZ  
2435  N N   . PHE A 155 ? 0.9731  0.7896  0.9997  0.0297  -0.0433 0.0462  164 PHE A N   
2436  C CA  . PHE A 155 ? 0.8467  0.6793  0.8842  0.0408  -0.0368 0.0340  164 PHE A CA  
2437  C C   . PHE A 155 ? 0.9552  0.7843  1.0081  0.0516  -0.0372 0.0235  164 PHE A C   
2438  O O   . PHE A 155 ? 1.1650  1.0039  1.2203  0.0539  -0.0298 0.0127  164 PHE A O   
2439  C CB  . PHE A 155 ? 0.7100  0.5623  0.7541  0.0470  -0.0396 0.0371  164 PHE A CB  
2440  C CG  . PHE A 155 ? 0.9372  0.7946  0.9682  0.0367  -0.0392 0.0440  164 PHE A CG  
2441  C CD1 . PHE A 155 ? 0.6775  0.5284  0.6956  0.0258  -0.0339 0.0412  164 PHE A CD1 
2442  C CD2 . PHE A 155 ? 1.2392  1.1104  1.2736  0.0384  -0.0447 0.0512  164 PHE A CD2 
2443  C CE1 . PHE A 155 ? 0.7434  0.5987  0.7526  0.0172  -0.0344 0.0434  164 PHE A CE1 
2444  C CE2 . PHE A 155 ? 0.7198  0.5945  0.7433  0.0283  -0.0458 0.0564  164 PHE A CE2 
2445  C CZ  . PHE A 155 ? 0.6865  0.5520  0.6976  0.0180  -0.0408 0.0513  164 PHE A CZ  
2455  N N   . LEU A 156 ? 0.7514  0.5678  0.8178  0.0586  -0.0470 0.0255  165 LEU A N   
2456  C CA  . LEU A 156 ? 0.7905  0.6061  0.8749  0.0703  -0.0472 0.0098  165 LEU A CA  
2457  C C   . LEU A 156 ? 0.8018  0.6002  0.8794  0.0624  -0.0438 0.0055  165 LEU A C   
2458  O O   . LEU A 156 ? 0.9162  0.7232  1.0000  0.0673  -0.0378 -0.0098 165 LEU A O   
2459  C CB  . LEU A 156 ? 0.7993  0.6032  0.9066  0.0818  -0.0606 0.0098  165 LEU A CB  
2460  C CG  . LEU A 156 ? 0.8282  0.6565  0.9517  0.0946  -0.0635 0.0069  165 LEU A CG  
2461  C CD1 . LEU A 156 ? 0.9250  0.7351  1.0770  0.1067  -0.0795 0.0061  165 LEU A CD1 
2462  C CD2 . LEU A 156 ? 0.8354  0.6994  0.9658  0.1031  -0.0524 -0.0125 165 LEU A CD2 
2474  N N   . VAL A 157 ? 0.7456  0.5245  0.8094  0.0480  -0.0474 0.0194  166 VAL A N   
2475  C CA  . VAL A 157 ? 0.9020  0.6678  0.9590  0.0380  -0.0446 0.0172  166 VAL A CA  
2476  C C   . VAL A 157 ? 1.0241  0.8092  1.0724  0.0355  -0.0306 0.0071  166 VAL A C   
2477  O O   . VAL A 157 ? 1.0432  0.8289  1.0963  0.0371  -0.0267 -0.0041 166 VAL A O   
2478  C CB  . VAL A 157 ? 0.8592  0.6100  0.9009  0.0195  -0.0507 0.0356  166 VAL A CB  
2479  C CG1 . VAL A 157 ? 0.9329  0.6794  0.9653  0.0065  -0.0453 0.0333  166 VAL A CG1 
2480  C CG2 . VAL A 157 ? 0.7126  0.4408  0.7680  0.0214  -0.0687 0.0478  166 VAL A CG2 
2490  N N   . SER A 158 ? 0.8757  0.6766  0.9139  0.0322  -0.0247 0.0108  167 SER A N   
2491  C CA  . SER A 158 ? 0.7403  0.5586  0.7764  0.0315  -0.0151 0.0030  167 SER A CA  
2492  C C   . SER A 158 ? 0.5622  0.3943  0.6108  0.0421  -0.0133 -0.0077 167 SER A C   
2493  O O   . SER A 158 ? 0.7086  0.5473  0.7592  0.0406  -0.0085 -0.0154 167 SER A O   
2494  C CB  . SER A 158 ? 1.0909  0.9220  1.1227  0.0306  -0.0139 0.0077  167 SER A CB  
2495  O OG  . SER A 158 ? 0.7108  0.5353  0.7299  0.0204  -0.0155 0.0157  167 SER A OG  
2501  N N   . LEU A 159 ? 0.5903  0.4321  0.6477  0.0517  -0.0173 -0.0086 168 LEU A N   
2502  C CA  . LEU A 159 ? 0.5465  0.4118  0.6148  0.0601  -0.0150 -0.0200 168 LEU A CA  
2503  C C   . LEU A 159 ? 0.5854  0.4423  0.6613  0.0633  -0.0151 -0.0335 168 LEU A C   
2504  O O   . LEU A 159 ? 0.6233  0.4991  0.7018  0.0634  -0.0104 -0.0440 168 LEU A O   
2505  C CB  . LEU A 159 ? 0.6632  0.5441  0.7410  0.0694  -0.0192 -0.0197 168 LEU A CB  
2506  C CG  . LEU A 159 ? 0.6866  0.5978  0.7788  0.0790  -0.0174 -0.0353 168 LEU A CG  
2507  C CD1 . LEU A 159 ? 0.6992  0.6448  0.7869  0.0731  -0.0117 -0.0357 168 LEU A CD1 
2508  C CD2 . LEU A 159 ? 0.6888  0.6092  0.7943  0.0894  -0.0231 -0.0358 168 LEU A CD2 
2520  N N   . LEU A 160 ? 0.5884  0.4167  0.6684  0.0640  -0.0222 -0.0322 169 LEU A N   
2521  C CA  . LEU A 160 ? 0.7257  0.5449  0.8166  0.0675  -0.0242 -0.0472 169 LEU A CA  
2522  C C   . LEU A 160 ? 0.8985  0.7178  0.9786  0.0565  -0.0176 -0.0483 169 LEU A C   
2523  O O   . LEU A 160 ? 0.8654  0.7011  0.9498  0.0582  -0.0134 -0.0625 169 LEU A O   
2524  C CB  . LEU A 160 ? 0.7999  0.5854  0.9020  0.0697  -0.0370 -0.0436 169 LEU A CB  
2525  C CG  . LEU A 160 ? 0.8671  0.6599  0.9894  0.0855  -0.0440 -0.0497 169 LEU A CG  
2526  C CD1 . LEU A 160 ? 0.8589  0.6175  0.9930  0.0864  -0.0604 -0.0369 169 LEU A CD1 
2527  C CD2 . LEU A 160 ? 1.2126  1.0233  1.3560  0.0994  -0.0424 -0.0775 169 LEU A CD2 
2539  N N   . VAL A 161 ? 0.6918  0.5027  0.7577  0.0449  -0.0152 -0.0345 170 VAL A N   
2540  C CA  . VAL A 161 ? 0.5509  0.3664  0.6100  0.0352  -0.0087 -0.0361 170 VAL A CA  
2541  C C   . VAL A 161 ? 0.6357  0.4809  0.6971  0.0380  -0.0026 -0.0421 170 VAL A C   
2542  O O   . VAL A 161 ? 0.5366  0.3907  0.5988  0.0335  0.0008  -0.0479 170 VAL A O   
2543  C CB  . VAL A 161 ? 0.5235  0.3336  0.5703  0.0235  -0.0060 -0.0243 170 VAL A CB  
2544  C CG1 . VAL A 161 ? 0.5139  0.3369  0.5597  0.0162  0.0015  -0.0293 170 VAL A CG1 
2545  C CG2 . VAL A 161 ? 0.6393  0.4262  0.6805  0.0154  -0.0130 -0.0142 170 VAL A CG2 
2555  N N   . GLU A 162 ? 0.7311  0.5928  0.7932  0.0427  -0.0023 -0.0374 171 GLU A N   
2556  C CA  . GLU A 162 ? 0.5559  0.4473  0.6212  0.0426  0.0002  -0.0391 171 GLU A CA  
2557  C C   . GLU A 162 ? 0.4855  0.3952  0.5570  0.0463  0.0010  -0.0540 171 GLU A C   
2558  O O   . GLU A 162 ? 0.9369  0.8641  1.0087  0.0410  0.0031  -0.0580 171 GLU A O   
2559  C CB  . GLU A 162 ? 0.7530  0.6576  0.8185  0.0450  -0.0020 -0.0297 171 GLU A CB  
2560  C CG  . GLU A 162 ? 0.8088  0.7356  0.8768  0.0392  -0.0026 -0.0223 171 GLU A CG  
2561  C CD  . GLU A 162 ? 0.9835  0.8971  1.0520  0.0344  -0.0040 -0.0129 171 GLU A CD  
2562  O OE1 . GLU A 162 ? 1.4099  1.3363  1.4862  0.0302  -0.0074 -0.0072 171 GLU A OE1 
2563  O OE2 . GLU A 162 ? 0.8099  0.7031  0.8731  0.0341  -0.0030 -0.0119 171 GLU A OE2 
2570  N N   . ILE A 163 ? 0.6672  0.5721  0.7457  0.0553  -0.0016 -0.0640 172 ILE A N   
2571  C CA  . ILE A 163 ? 0.9643  0.8867  1.0520  0.0605  -0.0008 -0.0848 172 ILE A CA  
2572  C C   . ILE A 163 ? 0.9323  0.8380  1.0196  0.0550  -0.0007 -0.0937 172 ILE A C   
2573  O O   . ILE A 163 ? 0.8736  0.8025  0.9623  0.0522  0.0022  -0.1072 172 ILE A O   
2574  C CB  . ILE A 163 ? 0.9669  0.8833  1.0689  0.0738  -0.0054 -0.0958 172 ILE A CB  
2575  C CG1 . ILE A 163 ? 0.9297  0.8737  1.0323  0.0776  -0.0045 -0.0884 172 ILE A CG1 
2576  C CG2 . ILE A 163 ? 1.1678  1.0983  1.2839  0.0808  -0.0051 -0.1235 172 ILE A CG2 
2577  C CD1 . ILE A 163 ? 0.9781  0.9115  1.0942  0.0897  -0.0104 -0.0909 172 ILE A CD1 
2589  N N   . ALA A 164 ? 0.8096  0.6784  0.8939  0.0510  -0.0042 -0.0852 173 ALA A N   
2590  C CA  . ALA A 164 ? 1.0551  0.9077  1.1393  0.0438  -0.0053 -0.0917 173 ALA A CA  
2591  C C   . ALA A 164 ? 0.9372  0.8115  1.0139  0.0340  0.0007  -0.0888 173 ALA A C   
2592  O O   . ALA A 164 ? 1.1659  1.0468  1.2444  0.0295  0.0013  -0.1006 173 ALA A O   
2593  C CB  . ALA A 164 ? 1.1598  0.9756  1.2400  0.0369  -0.0106 -0.0783 173 ALA A CB  
2599  N N   . ALA A 165 ? 0.8090  0.6967  0.8802  0.0313  0.0038  -0.0744 174 ALA A N   
2600  C CA  . ALA A 165 ? 1.0066  0.9158  1.0766  0.0236  0.0066  -0.0699 174 ALA A CA  
2601  C C   . ALA A 165 ? 0.8621  0.8090  0.9344  0.0235  0.0068  -0.0757 174 ALA A C   
2602  O O   . ALA A 165 ? 0.8020  0.7693  0.8749  0.0157  0.0068  -0.0734 174 ALA A O   
2603  C CB  . ALA A 165 ? 1.4126  1.3197  1.4816  0.0218  0.0072  -0.0544 174 ALA A CB  
2609  N N   . ALA A 166 ? 1.0618  1.0240  1.1359  0.0305  0.0066  -0.0819 175 ALA A N   
2610  C CA  . ALA A 166 ? 1.0660  1.0726  1.1400  0.0260  0.0073  -0.0866 175 ALA A CA  
2611  C C   . ALA A 166 ? 1.0143  1.0330  1.0879  0.0198  0.0086  -0.1020 175 ALA A C   
2612  O O   . ALA A 166 ? 0.9821  1.0340  1.0529  0.0094  0.0078  -0.0973 175 ALA A O   
2613  C CB  . ALA A 166 ? 1.5775  1.6052  1.6551  0.0342  0.0083  -0.0974 175 ALA A CB  
2619  N N   . SER A 167 ? 1.3799  1.3700  1.4568  0.0239  0.0087  -0.1176 176 SER A N   
2620  C CA  . SER A 167 ? 1.0534  1.0533  1.1307  0.0176  0.0092  -0.1351 176 SER A CA  
2621  C C   . SER A 167 ? 1.1617  1.1689  1.2339  0.0048  0.0087  -0.1208 176 SER A C   
2622  O O   . SER A 167 ? 0.8498  0.8895  0.9196  -0.0046 0.0088  -0.1264 176 SER A O   
2623  C CB  . SER A 167 ? 1.1180  1.0763  1.2022  0.0227  0.0061  -0.1495 176 SER A CB  
2624  O OG  . SER A 167 ? 1.3770  1.3218  1.4712  0.0362  0.0036  -0.1596 176 SER A OG  
2630  N N   . ALA A 168 ? 1.0563  1.0403  1.1285  0.0041  0.0079  -0.1019 177 ALA A N   
2631  C CA  . ALA A 168 ? 0.7958  0.7872  0.8693  -0.0056 0.0069  -0.0902 177 ALA A CA  
2632  C C   . ALA A 168 ? 0.8446  0.8713  0.9207  -0.0103 0.0034  -0.0751 177 ALA A C   
2633  O O   . ALA A 168 ? 0.6828  0.7347  0.7610  -0.0202 0.0002  -0.0711 177 ALA A O   
2634  C CB  . ALA A 168 ? 0.7927  0.7523  0.8681  -0.0045 0.0078  -0.0795 177 ALA A CB  
2640  N N   . ILE A 169 ? 0.9056  0.9359  0.9821  -0.0048 0.0021  -0.0657 178 ILE A N   
2641  C CA  . ILE A 169 ? 1.1060  1.1682  1.1862  -0.0113 -0.0042 -0.0486 178 ILE A CA  
2642  C C   . ILE A 169 ? 0.9033  1.0098  0.9782  -0.0225 -0.0058 -0.0544 178 ILE A C   
2643  O O   . ILE A 169 ? 0.6452  0.7795  0.7242  -0.0338 -0.0137 -0.0378 178 ILE A O   
2644  C CB  . ILE A 169 ? 1.4746  1.5366  1.5541  -0.0054 -0.0054 -0.0406 178 ILE A CB  
2645  C CG1 . ILE A 169 ? 1.3182  1.3399  1.4014  0.0035  -0.0042 -0.0354 178 ILE A CG1 
2646  C CG2 . ILE A 169 ? 0.8314  0.9285  0.9149  -0.0157 -0.0147 -0.0205 178 ILE A CG2 
2647  C CD1 . ILE A 169 ? 1.4409  1.4578  1.5215  0.0102  -0.0043 -0.0316 178 ILE A CD1 
2659  N N   . LYS A 170 ? 0.9701  1.0874  1.0377  -0.0199 0.0004  -0.0780 179 LYS A N   
2660  C CA  . LYS A 170 ? 0.7473  0.9147  0.8085  -0.0316 0.0005  -0.0889 179 LYS A CA  
2661  C C   . LYS A 170 ? 0.7820  0.9646  0.8432  -0.0456 -0.0042 -0.0822 179 LYS A C   
2662  O O   . LYS A 170 ? 0.8595  1.0908  0.9157  -0.0608 -0.0085 -0.0769 179 LYS A O   
2663  C CB  . LYS A 170 ? 0.9316  1.0998  0.9906  -0.0244 0.0079  -0.1233 179 LYS A CB  
2664  C CG  . LYS A 170 ? 1.3055  1.4586  1.3691  -0.0086 0.0119  -0.1360 179 LYS A CG  
2665  C CD  . LYS A 170 ? 1.3538  1.5290  1.4210  -0.0034 0.0171  -0.1739 179 LYS A CD  
2666  C CE  . LYS A 170 ? 1.3859  1.5355  1.4563  -0.0037 0.0169  -0.1956 179 LYS A CE  
2667  N NZ  . LYS A 170 ? 1.3016  1.4671  1.3807  0.0029  0.0201  -0.2365 179 LYS A NZ  
2681  N N   . VAL A 171 ? 0.5714  0.7173  0.6384  -0.0424 -0.0042 -0.0809 180 VAL A N   
2682  C CA  . VAL A 171 ? 1.3011  1.4597  1.3691  -0.0541 -0.0073 -0.0807 180 VAL A CA  
2683  C C   . VAL A 171 ? 1.1741  1.3467  1.2534  -0.0620 -0.0177 -0.0515 180 VAL A C   
2684  O O   . VAL A 171 ? 0.9832  1.1851  1.0639  -0.0756 -0.0239 -0.0453 180 VAL A O   
2685  C CB  . VAL A 171 ? 1.2343  1.3502  1.3045  -0.0483 -0.0026 -0.0944 180 VAL A CB  
2686  C CG1 . VAL A 171 ? 1.2545  1.3832  1.3260  -0.0607 -0.0054 -0.0959 180 VAL A CG1 
2687  C CG2 . VAL A 171 ? 0.8923  0.9902  0.9572  -0.0399 0.0033  -0.1211 180 VAL A CG2 
2697  N N   . ILE A 172 ? 0.9865  1.1405  1.0758  -0.0541 -0.0214 -0.0338 181 ILE A N   
2698  C CA  . ILE A 172 ? 0.8448  1.0029  0.9527  -0.0579 -0.0335 -0.0084 181 ILE A CA  
2699  C C   . ILE A 172 ? 0.9352  1.1412  1.0442  -0.0760 -0.0454 0.0074  181 ILE A C   
2700  O O   . ILE A 172 ? 0.7775  0.9906  0.9010  -0.0821 -0.0540 0.0188  181 ILE A O   
2701  C CB  . ILE A 172 ? 0.8241  0.9621  0.9414  -0.0484 -0.0372 0.0054  181 ILE A CB  
2702  C CG1 . ILE A 172 ? 1.1126  1.2061  1.2331  -0.0337 -0.0280 -0.0061 181 ILE A CG1 
2703  C CG2 . ILE A 172 ? 0.5125  0.6578  0.6525  -0.0527 -0.0531 0.0308  181 ILE A CG2 
2704  C CD1 . ILE A 172 ? 0.8963  0.9704  1.0215  -0.0247 -0.0297 0.0019  181 ILE A CD1 
2716  N N   . PRO A 173 ? 0.8700  1.1139  0.9655  -0.0866 -0.0472 0.0098  182 PRO A N   
2717  C CA  . PRO A 173 ? 1.1168  1.4123  1.2108  -0.1083 -0.0594 0.0266  182 PRO A CA  
2718  C C   . PRO A 173 ? 0.8778  1.1897  0.9660  -0.1173 -0.0567 0.0125  182 PRO A C   
2719  O O   . PRO A 173 ? 0.6907  1.0370  0.7838  -0.1344 -0.0696 0.0310  182 PRO A O   
2720  C CB  . PRO A 173 ? 1.1823  1.5201  1.2576  -0.1181 -0.0566 0.0230  182 PRO A CB  
2721  C CG  . PRO A 173 ? 1.2801  1.5893  1.3458  -0.1000 -0.0393 -0.0082 182 PRO A CG  
2722  C CD  . PRO A 173 ? 1.0963  1.3449  1.1765  -0.0812 -0.0374 -0.0057 182 PRO A CD  
2730  N N   . THR A 174 ? 1.0455  1.3359  1.1232  -0.1083 -0.0420 -0.0189 183 THR A N   
2731  C CA  . THR A 174 ? 1.0779  1.3821  1.1503  -0.1181 -0.0402 -0.0335 183 THR A CA  
2732  C C   . THR A 174 ? 0.7934  1.0783  0.8860  -0.1172 -0.0479 -0.0173 183 THR A C   
2733  O O   . THR A 174 ? 0.6779  0.9911  0.7733  -0.1318 -0.0556 -0.0106 183 THR A O   
2734  C CB  . THR A 174 ? 1.0913  1.3712  1.1519  -0.1087 -0.0256 -0.0703 183 THR A CB  
2735  O OG1 . THR A 174 ? 1.6096  1.9134  1.6569  -0.1081 -0.0192 -0.0883 183 THR A OG1 
2736  C CG2 . THR A 174 ? 1.1511  1.4456  1.2062  -0.1205 -0.0251 -0.0860 183 THR A CG2 
2744  N N   . VAL A 175 ? 0.5630  0.8060  0.6716  -0.1010 -0.0469 -0.0101 184 VAL A N   
2745  C CA  . VAL A 175 ? 0.5395  0.7689  0.6721  -0.0981 -0.0534 0.0023  184 VAL A CA  
2746  C C   . VAL A 175 ? 0.7871  1.0483  0.9391  -0.1090 -0.0726 0.0321  184 VAL A C   
2747  O O   . VAL A 175 ? 1.3202  1.6030  1.4823  -0.1194 -0.0806 0.0393  184 VAL A O   
2748  C CB  . VAL A 175 ? 0.5701  0.7555  0.7156  -0.0794 -0.0479 0.0011  184 VAL A CB  
2749  C CG1 . VAL A 175 ? 0.7828  0.9634  0.9594  -0.0753 -0.0559 0.0134  184 VAL A CG1 
2750  C CG2 . VAL A 175 ? 0.5177  0.6726  0.6460  -0.0726 -0.0319 -0.0252 184 VAL A CG2 
2760  N N   . PHE A 176 ? 0.7885  1.0535  0.9473  -0.1081 -0.0821 0.0515  185 PHE A N   
2761  C CA  . PHE A 176 ? 1.4818  1.7649  1.6680  -0.1157 -0.1041 0.0831  185 PHE A CA  
2762  C C   . PHE A 176 ? 1.2977  1.6325  1.4736  -0.1397 -0.1143 0.0948  185 PHE A C   
2763  O O   . PHE A 176 ? 0.4953  0.8464  0.6951  -0.1476 -0.1318 0.1165  185 PHE A O   
2764  C CB  . PHE A 176 ? 1.8478  2.1224  2.0441  -0.1124 -0.1148 0.1035  185 PHE A CB  
2765  C CG  . PHE A 176 ? 1.5323  1.7584  1.7480  -0.0898 -0.1098 0.0960  185 PHE A CG  
2766  C CD1 . PHE A 176 ? 1.0563  1.2629  1.3032  -0.0783 -0.1130 0.0937  185 PHE A CD1 
2767  C CD2 . PHE A 176 ? 1.5625  1.7671  1.7650  -0.0808 -0.1010 0.0886  185 PHE A CD2 
2768  C CE1 . PHE A 176 ? 0.8835  1.0529  1.1468  -0.0593 -0.1070 0.0829  185 PHE A CE1 
2769  C CE2 . PHE A 176 ? 1.6823  1.8469  1.9000  -0.0625 -0.0961 0.0803  185 PHE A CE2 
2770  C CZ  . PHE A 176 ? 1.1811  1.3290  1.4281  -0.0522 -0.0985 0.0764  185 PHE A CZ  
2780  N N   . LYS A 177 ? 0.9439  1.3061  1.0863  -0.1510 -0.1033 0.0777  186 LYS A N   
2781  C CA  . LYS A 177 ? 1.1408  1.5592  1.2704  -0.1766 -0.1120 0.0857  186 LYS A CA  
2782  C C   . LYS A 177 ? 0.6646  1.0840  0.7988  -0.1795 -0.1099 0.0742  186 LYS A C   
2783  O O   . LYS A 177 ? 0.5392  0.9927  0.6839  -0.1964 -0.1262 0.0952  186 LYS A O   
2784  C CB  . LYS A 177 ? 0.5704  1.0237  0.6647  -0.1875 -0.0992 0.0634  186 LYS A CB  
2787  N N   . ALA A 178 ? 0.7631  1.1441  0.8924  -0.1639 -0.0922 0.0444  187 ALA A N   
2788  C CA  . ALA A 178 ? 1.1061  1.4882  1.2377  -0.1685 -0.0895 0.0321  187 ALA A CA  
2789  C C   . ALA A 178 ? 0.9142  1.2926  1.0814  -0.1656 -0.1042 0.0564  187 ALA A C   
2790  O O   . ALA A 178 ? 1.2882  1.6929  1.4623  -0.1787 -0.1123 0.0623  187 ALA A O   
2791  C CB  . ALA A 178 ? 0.5113  0.8493  0.6342  -0.1535 -0.0707 0.0009  187 ALA A CB  
2797  N N   . MET A 179 ? 0.9794  1.3287  1.1721  -0.1488 -0.1093 0.0702  188 MET A N   
2798  C CA  . MET A 179 ? 0.9458  1.2962  1.1801  -0.1447 -0.1267 0.0931  188 MET A CA  
2799  C C   . MET A 179 ? 1.2020  1.5966  1.4468  -0.1649 -0.1516 0.1268  188 MET A C   
2800  O O   . MET A 179 ? 1.3093  1.7279  1.5744  -0.1741 -0.1652 0.1403  188 MET A O   
2801  C CB  . MET A 179 ? 0.6911  1.0024  0.9520  -0.1225 -0.1275 0.0967  188 MET A CB  
2802  C CG  . MET A 179 ? 0.7112  0.9847  0.9729  -0.1043 -0.1076 0.0694  188 MET A CG  
2803  S SD  . MET A 179 ? 0.8783  1.1119  1.1685  -0.0801 -0.1079 0.0701  188 MET A SD  
2804  C CE  . MET A 179 ? 1.0712  1.3209  1.4182  -0.0778 -0.1364 0.0978  188 MET A CE  
2814  N N   . GLN A 180 ? 0.8366  1.2462  1.0678  -0.1742 -0.1589 0.1425  189 GLN A N   
2815  C CA  . GLN A 180 ? 1.1652  1.6194  1.4056  -0.1972 -0.1852 0.1796  189 GLN A CA  
2816  C C   . GLN A 180 ? 0.7838  1.2881  1.0029  -0.2219 -0.1866 0.1775  189 GLN A C   
2817  O O   . GLN A 180 ? 0.8803  1.4183  1.1182  -0.2389 -0.2101 0.2078  189 GLN A O   
2818  C CB  . GLN A 180 ? 1.3010  1.7683  1.5236  -0.2066 -0.1897 0.1941  189 GLN A CB  
2821  N N   . MET A 181 ? 1.2013  1.7104  1.3833  -0.2245 -0.1632 0.1418  190 MET A N   
2822  C CA  . MET A 181 ? 1.5006  2.0557  1.6595  -0.2476 -0.1618 0.1319  190 MET A CA  
2823  C C   . MET A 181 ? 1.1050  1.6421  1.2724  -0.2406 -0.1534 0.1116  190 MET A C   
2824  O O   . MET A 181 ? 1.2866  1.8579  1.4358  -0.2593 -0.1520 0.1007  190 MET A O   
2825  C CB  . MET A 181 ? 0.9256  1.5033  1.0405  -0.2570 -0.1434 0.1018  190 MET A CB  
2826  C CG  . MET A 181 ? 0.8727  1.4925  0.9721  -0.2741 -0.1520 0.1212  190 MET A CG  
2833  N N   . GLN A 182 ? 0.9795  1.4678  1.1730  -0.2161 -0.1474 0.1052  191 GLN A N   
2834  C CA  . GLN A 182 ? 0.9489  1.4255  1.1556  -0.2114 -0.1418 0.0912  191 GLN A CA  
2835  C C   . GLN A 182 ? 1.1252  1.6004  1.2962  -0.2189 -0.1225 0.0552  191 GLN A C   
2836  O O   . GLN A 182 ? 1.3646  1.8550  1.5355  -0.2299 -0.1231 0.0480  191 GLN A O   
2837  C CB  . GLN A 182 ? 1.3189  1.8337  1.5535  -0.2259 -0.1647 0.1195  191 GLN A CB  
2838  C CG  . GLN A 182 ? 1.2401  1.7415  1.5275  -0.2104 -0.1837 0.1475  191 GLN A CG  
2839  C CD  . GLN A 182 ? 1.2397  1.7101  1.5582  -0.1886 -0.1745 0.1316  191 GLN A CD  
2840  O OE1 . GLN A 182 ? 1.3787  1.8379  1.7431  -0.1729 -0.1871 0.1458  191 GLN A OE1 
2841  N NE2 . GLN A 182 ? 2.0141  2.4728  2.3098  -0.1885 -0.1535 0.1015  191 GLN A NE2 
2850  N N   . GLU A 183 ? 1.2049  1.6604  1.3487  -0.2124 -0.1066 0.0318  192 GLU A N   
2851  C CA  . GLU A 183 ? 0.8380  1.2823  0.9535  -0.2153 -0.0896 -0.0054 192 GLU A CA  
2852  C C   . GLU A 183 ? 1.0125  1.4005  1.1357  -0.1953 -0.0761 -0.0224 192 GLU A C   
2853  O O   . GLU A 183 ? 1.2150  1.5684  1.3319  -0.1796 -0.0657 -0.0333 192 GLU A O   
2854  C CB  . GLU A 183 ? 0.8710  1.3279  0.9580  -0.2183 -0.0815 -0.0229 192 GLU A CB  
2855  C CG  . GLU A 183 ? 1.1752  1.6976  1.2430  -0.2444 -0.0898 -0.0187 192 GLU A CG  
2856  C CD  . GLU A 183 ? 1.4285  1.9742  1.4788  -0.2616 -0.0858 -0.0456 192 GLU A CD  
2857  O OE1 . GLU A 183 ? 1.4444  2.0470  1.4868  -0.2866 -0.0970 -0.0344 192 GLU A OE1 
2858  O OE2 . GLU A 183 ? 1.4552  1.9622  1.4998  -0.2515 -0.0725 -0.0778 192 GLU A OE2 
2865  N N   . ARG A 184 ? 0.9235  1.3062  1.0593  -0.1984 -0.0765 -0.0246 193 ARG A N   
2866  C CA  . ARG A 184 ? 0.5494  0.8869  0.6956  -0.1831 -0.0659 -0.0345 193 ARG A CA  
2867  C C   . ARG A 184 ? 0.7552  1.0570  0.8770  -0.1801 -0.0518 -0.0644 193 ARG A C   
2868  O O   . ARG A 184 ? 0.8539  1.1152  0.9780  -0.1651 -0.0430 -0.0697 193 ARG A O   
2869  C CB  . ARG A 184 ? 0.6108  0.9609  0.7775  -0.1906 -0.0706 -0.0285 193 ARG A CB  
2870  C CG  . ARG A 184 ? 0.6657  0.9793  0.8396  -0.1813 -0.0591 -0.0401 193 ARG A CG  
2871  C CD  . ARG A 184 ? 0.8238  1.1207  0.9735  -0.1939 -0.0515 -0.0644 193 ARG A CD  
2872  N NE  . ARG A 184 ? 0.8616  1.1355  1.0204  -0.1923 -0.0447 -0.0685 193 ARG A NE  
2873  C CZ  . ARG A 184 ? 0.6944  0.9424  0.8373  -0.2014 -0.0392 -0.0856 193 ARG A CZ  
2874  N NH1 . ARG A 184 ? 0.9580  1.1961  1.0779  -0.2097 -0.0397 -0.1046 193 ARG A NH1 
2875  N NH2 . ARG A 184 ? 0.6656  0.9003  0.8182  -0.2030 -0.0344 -0.0841 193 ARG A NH2 
2889  N N   . ASP A 185 ? 1.0459  1.3617  1.1467  -0.1948 -0.0507 -0.0848 194 ASP A N   
2890  C CA  . ASP A 185 ? 1.1314  1.4081  1.2168  -0.1905 -0.0407 -0.1134 194 ASP A CA  
2891  C C   . ASP A 185 ? 1.0072  1.2627  1.0860  -0.1736 -0.0344 -0.1181 194 ASP A C   
2892  O O   . ASP A 185 ? 0.6724  0.8838  0.7538  -0.1598 -0.0278 -0.1222 194 ASP A O   
2893  C CB  . ASP A 185 ? 1.2686  1.5644  1.3366  -0.2079 -0.0419 -0.1389 194 ASP A CB  
2894  C CG  . ASP A 185 ? 1.2191  1.5265  1.2931  -0.2253 -0.0474 -0.1371 194 ASP A CG  
2895  O OD1 . ASP A 185 ? 1.2174  1.5050  1.3075  -0.2214 -0.0470 -0.1234 194 ASP A OD1 
2896  O OD2 . ASP A 185 ? 1.2076  1.5477  1.2701  -0.2437 -0.0520 -0.1503 194 ASP A OD2 
2901  N N   . THR A 186 ? 1.1385  1.4300  1.2116  -0.1758 -0.0380 -0.1105 195 THR A N   
2902  C CA  . THR A 186 ? 1.1270  1.4100  1.1932  -0.1628 -0.0330 -0.1142 195 THR A CA  
2903  C C   . THR A 186 ? 1.2122  1.4604  1.2935  -0.1447 -0.0312 -0.0955 195 THR A C   
2904  O O   . THR A 186 ? 0.8975  1.1154  0.9745  -0.1306 -0.0242 -0.1042 195 THR A O   
2905  C CB  . THR A 186 ? 1.0472  1.3860  1.1058  -0.1746 -0.0397 -0.1030 195 THR A CB  
2906  O OG1 . THR A 186 ? 1.0405  1.4185  1.0830  -0.1933 -0.0404 -0.1237 195 THR A OG1 
2907  C CG2 . THR A 186 ? 0.9670  1.3053  1.0183  -0.1639 -0.0348 -0.1063 195 THR A CG2 
2915  N N   . LEU A 187 ? 0.9958  1.2490  1.0970  -0.1443 -0.0379 -0.0712 196 LEU A N   
2916  C CA  . LEU A 187 ? 0.6995  0.9219  0.8160  -0.1270 -0.0355 -0.0588 196 LEU A CA  
2917  C C   . LEU A 187 ? 0.9804  1.1586  1.0936  -0.1193 -0.0251 -0.0743 196 LEU A C   
2918  O O   . LEU A 187 ? 0.9649  1.1126  1.0748  -0.1063 -0.0190 -0.0775 196 LEU A O   
2919  C CB  . LEU A 187 ? 0.5022  0.7420  0.6466  -0.1271 -0.0460 -0.0342 196 LEU A CB  
2920  C CG  . LEU A 187 ? 0.8945  1.1101  1.0633  -0.1108 -0.0448 -0.0244 196 LEU A CG  
2921  C CD1 . LEU A 187 ? 1.3956  1.5960  1.5653  -0.0981 -0.0449 -0.0173 196 LEU A CD1 
2922  C CD2 . LEU A 187 ? 1.3572  1.5976  1.5586  -0.1125 -0.0573 -0.0058 196 LEU A CD2 
2934  N N   . LEU A 188 ? 1.1111  1.2868  1.2226  -0.1300 -0.0242 -0.0842 197 LEU A N   
2935  C CA  . LEU A 188 ? 1.3420  1.4787  1.4511  -0.1271 -0.0172 -0.0939 197 LEU A CA  
2936  C C   . LEU A 188 ? 0.9175  1.0224  1.0104  -0.1204 -0.0125 -0.1117 197 LEU A C   
2937  O O   . LEU A 188 ? 0.6494  0.7208  0.7419  -0.1101 -0.0079 -0.1107 197 LEU A O   
2938  C CB  . LEU A 188 ? 1.1372  1.2817  1.2473  -0.1434 -0.0194 -0.0998 197 LEU A CB  
2939  C CG  . LEU A 188 ? 0.8815  0.9942  0.9922  -0.1464 -0.0149 -0.1033 197 LEU A CG  
2940  C CD1 . LEU A 188 ? 1.3728  1.5080  1.4941  -0.1614 -0.0179 -0.0984 197 LEU A CD1 
2941  C CD2 . LEU A 188 ? 0.8762  0.9544  0.9702  -0.1491 -0.0146 -0.1232 197 LEU A CD2 
2953  N N   . LYS A 189 ? 0.6781  0.7968  0.7591  -0.1260 -0.0142 -0.1288 198 LYS A N   
2954  C CA  . LYS A 189 ? 0.9605  1.0537  1.0320  -0.1175 -0.0110 -0.1494 198 LYS A CA  
2955  C C   . LYS A 189 ? 1.1276  1.2088  1.2007  -0.1010 -0.0074 -0.1391 198 LYS A C   
2956  O O   . LYS A 189 ? 1.5130  1.5566  1.5854  -0.0911 -0.0048 -0.1447 198 LYS A O   
2957  C CB  . LYS A 189 ? 1.2339  1.3595  1.2957  -0.1248 -0.0125 -0.1712 198 LYS A CB  
2958  C CG  . LYS A 189 ? 1.3521  1.4597  1.4097  -0.1144 -0.0095 -0.1975 198 LYS A CG  
2959  C CD  . LYS A 189 ? 1.3095  1.4642  1.3583  -0.1217 -0.0090 -0.2198 198 LYS A CD  
2960  C CE  . LYS A 189 ? 1.2701  1.4111  1.3205  -0.1090 -0.0058 -0.2516 198 LYS A CE  
2961  N NZ  . LYS A 189 ? 1.8747  1.9682  1.9330  -0.1082 -0.0099 -0.2724 198 LYS A NZ  
2975  N N   . ALA A 190 ? 0.8768  0.9888  0.9538  -0.0992 -0.0092 -0.1215 199 ALA A N   
2976  C CA  . ALA A 190 ? 0.7434  0.8476  0.8219  -0.0855 -0.0071 -0.1116 199 ALA A CA  
2977  C C   . ALA A 190 ? 0.6702  0.7383  0.7565  -0.0761 -0.0040 -0.1010 199 ALA A C   
2978  O O   . ALA A 190 ? 0.8665  0.9062  0.9491  -0.0656 -0.0004 -0.1047 199 ALA A O   
2979  C CB  . ALA A 190 ? 0.6772  0.8217  0.7607  -0.0892 -0.0133 -0.0921 199 ALA A CB  
2985  N N   . LEU A 191 ? 0.6665  0.7389  0.7646  -0.0805 -0.0054 -0.0887 200 LEU A N   
2986  C CA  . LEU A 191 ? 0.5467  0.5936  0.6518  -0.0734 -0.0012 -0.0817 200 LEU A CA  
2987  C C   . LEU A 191 ? 0.7370  0.7475  0.8310  -0.0742 0.0027  -0.0930 200 LEU A C   
2988  O O   . LEU A 191 ? 1.0349  1.0219  1.1277  -0.0674 0.0060  -0.0889 200 LEU A O   
2989  C CB  . LEU A 191 ? 0.9890  1.0525  1.1111  -0.0791 -0.0024 -0.0726 200 LEU A CB  
2990  C CG  . LEU A 191 ? 1.0652  1.1599  1.2046  -0.0765 -0.0100 -0.0583 200 LEU A CG  
2991  C CD1 . LEU A 191 ? 0.8870  1.0036  1.0465  -0.0831 -0.0134 -0.0527 200 LEU A CD1 
2992  C CD2 . LEU A 191 ? 1.1551  1.2416  1.3041  -0.0629 -0.0107 -0.0488 200 LEU A CD2 
3004  N N   . LEU A 192 ? 0.7003  0.7053  0.7873  -0.0835 0.0004  -0.1069 201 LEU A N   
3005  C CA  . LEU A 192 ? 0.9363  0.9028  1.0171  -0.0853 -0.0002 -0.1154 201 LEU A CA  
3006  C C   . LEU A 192 ? 1.0572  1.0038  1.1335  -0.0721 -0.0004 -0.1240 201 LEU A C   
3007  O O   . LEU A 192 ? 1.0382  0.9524  1.1131  -0.0681 -0.0011 -0.1206 201 LEU A O   
3008  C CB  . LEU A 192 ? 1.0233  0.9866  1.1020  -0.0994 -0.0050 -0.1291 201 LEU A CB  
3009  C CG  . LEU A 192 ? 1.1336  1.1124  1.2175  -0.1140 -0.0051 -0.1199 201 LEU A CG  
3010  C CD1 . LEU A 192 ? 1.3307  1.3048  1.4116  -0.1284 -0.0111 -0.1345 201 LEU A CD1 
3011  C CD2 . LEU A 192 ? 0.9457  0.9054  1.0313  -0.1172 -0.0025 -0.1070 201 LEU A CD2 
3023  N N   . GLU A 193 ? 1.2889  1.2590  1.3633  -0.0667 -0.0004 -0.1341 202 GLU A N   
3024  C CA  . GLU A 193 ? 0.7799  0.7399  0.8528  -0.0533 0.0002  -0.1436 202 GLU A CA  
3025  C C   . GLU A 193 ? 1.0323  0.9828  1.1058  -0.0435 0.0030  -0.1255 202 GLU A C   
3026  O O   . GLU A 193 ? 1.0751  0.9964  1.1486  -0.0353 0.0023  -0.1258 202 GLU A O   
3027  C CB  . GLU A 193 ? 1.1462  1.1471  1.2161  -0.0528 0.0011  -0.1562 202 GLU A CB  
3028  C CG  . GLU A 193 ? 1.5373  1.5456  1.6069  -0.0399 0.0032  -0.1650 202 GLU A CG  
3029  C CD  . GLU A 193 ? 1.7366  1.7163  1.8124  -0.0308 0.0010  -0.1899 202 GLU A CD  
3030  O OE1 . GLU A 193 ? 1.6635  1.6246  1.7429  -0.0368 -0.0032 -0.2053 202 GLU A OE1 
3031  O OE2 . GLU A 193 ? 1.6803  1.6572  1.7600  -0.0177 0.0022  -0.1948 202 GLU A OE2 
3038  N N   . ILE A 194 ? 0.6921  0.6649  0.7688  -0.0450 0.0047  -0.1090 203 ILE A N   
3039  C CA  . ILE A 194 ? 0.5138  0.4782  0.5928  -0.0362 0.0068  -0.0945 203 ILE A CA  
3040  C C   . ILE A 194 ? 0.6837  0.6159  0.7612  -0.0374 0.0085  -0.0902 203 ILE A C   
3041  O O   . ILE A 194 ? 0.9593  0.8736  1.0342  -0.0299 0.0094  -0.0854 203 ILE A O   
3042  C CB  . ILE A 194 ? 0.4949  0.4870  0.5835  -0.0377 0.0056  -0.0799 203 ILE A CB  
3043  C CG1 . ILE A 194 ? 1.4034  1.4260  1.4911  -0.0369 0.0020  -0.0780 203 ILE A CG1 
3044  C CG2 . ILE A 194 ? 0.4847  0.4624  0.5794  -0.0314 0.0080  -0.0690 203 ILE A CG2 
3045  C CD1 . ILE A 194 ? 1.3945  1.4446  1.4943  -0.0412 -0.0039 -0.0620 203 ILE A CD1 
3057  N N   . ALA A 195 ? 0.5299  0.4591  0.6088  -0.0489 0.0085  -0.0898 204 ALA A N   
3058  C CA  . ALA A 195 ? 0.7293  0.6351  0.8050  -0.0550 0.0096  -0.0835 204 ALA A CA  
3059  C C   . ALA A 195 ? 0.7532  0.6238  0.8228  -0.0534 0.0042  -0.0882 204 ALA A C   
3060  O O   . ALA A 195 ? 0.6859  0.5371  0.7515  -0.0522 0.0036  -0.0795 204 ALA A O   
3061  C CB  . ALA A 195 ? 1.1066  1.0216  1.1852  -0.0704 0.0099  -0.0823 204 ALA A CB  
3067  N N   . SER A 196 ? 0.8670  0.7309  0.9381  -0.0524 -0.0008 -0.1029 205 SER A N   
3068  C CA  . SER A 196 ? 1.0361  0.8649  1.1087  -0.0487 -0.0085 -0.1092 205 SER A CA  
3069  C C   . SER A 196 ? 1.3292  1.1539  1.4020  -0.0334 -0.0073 -0.1063 205 SER A C   
3070  O O   . SER A 196 ? 0.7283  0.5249  0.8013  -0.0315 -0.0126 -0.0987 205 SER A O   
3071  C CB  . SER A 196 ? 1.3533  1.1800  1.4320  -0.0478 -0.0137 -0.1318 205 SER A CB  
3072  O OG  . SER A 196 ? 1.5392  1.3301  1.6262  -0.0411 -0.0231 -0.1397 205 SER A OG  
3078  N N   . CYS A 197 ? 1.0035  0.8582  1.0763  -0.0245 -0.0016 -0.1095 206 CYS A N   
3079  C CA  . CYS A 197 ? 0.7871  0.6411  0.8606  -0.0110 -0.0010 -0.1078 206 CYS A CA  
3080  C C   . CYS A 197 ? 0.8197  0.6616  0.8882  -0.0114 0.0007  -0.0887 206 CYS A C   
3081  O O   . CYS A 197 ? 0.8352  0.6601  0.9039  -0.0040 -0.0024 -0.0851 206 CYS A O   
3082  C CB  . CYS A 197 ? 0.5693  0.4619  0.6430  -0.0056 0.0034  -0.1126 206 CYS A CB  
3083  S SG  . CYS A 197 ? 1.3885  1.3064  1.4661  -0.0048 0.0025  -0.1396 206 CYS A SG  
3089  N N   . LEU A 198 ? 0.7230  0.5752  0.7885  -0.0204 0.0053  -0.0783 207 LEU A N   
3090  C CA  . LEU A 198 ? 0.6179  0.4624  0.6786  -0.0226 0.0075  -0.0650 207 LEU A CA  
3091  C C   . LEU A 198 ? 0.7421  0.5602  0.7972  -0.0337 0.0026  -0.0582 207 LEU A C   
3092  O O   . LEU A 198 ? 0.7541  0.5661  0.8028  -0.0367 0.0031  -0.0475 207 LEU A O   
3093  C CB  . LEU A 198 ? 0.9875  0.8560  1.0513  -0.0270 0.0141  -0.0603 207 LEU A CB  
3094  C CG  . LEU A 198 ? 1.2172  1.1113  1.2900  -0.0187 0.0158  -0.0608 207 LEU A CG  
3095  C CD1 . LEU A 198 ? 0.5329  0.4452  0.6153  -0.0232 0.0199  -0.0580 207 LEU A CD1 
3096  C CD2 . LEU A 198 ? 1.5047  1.3982  1.5769  -0.0079 0.0148  -0.0570 207 LEU A CD2 
3108  N N   . GLU A 199 ? 0.7215  0.5267  0.7784  -0.0431 -0.0029 -0.0627 208 GLU A N   
3109  C CA  . GLU A 199 ? 1.0256  0.8020  1.0789  -0.0556 -0.0118 -0.0523 208 GLU A CA  
3110  C C   . GLU A 199 ? 0.9573  0.7065  1.0155  -0.0442 -0.0214 -0.0521 208 GLU A C   
3111  O O   . GLU A 199 ? 0.8377  0.5724  0.8909  -0.0484 -0.0265 -0.0373 208 GLU A O   
3112  C CB  . GLU A 199 ? 1.2959  1.0625  1.3526  -0.0691 -0.0178 -0.0568 208 GLU A CB  
3115  N N   . LYS A 200 ? 0.8227  0.5740  0.8908  -0.0286 -0.0222 -0.0692 209 LYS A N   
3116  C CA  . LYS A 200 ? 0.7398  0.4743  0.8174  -0.0141 -0.0295 -0.0733 209 LYS A CA  
3117  C C   . LYS A 200 ? 1.2063  0.9504  1.2763  -0.0085 -0.0248 -0.0604 209 LYS A C   
3118  O O   . LYS A 200 ? 0.9316  0.6553  1.0028  -0.0077 -0.0332 -0.0490 209 LYS A O   
3119  C CB  . LYS A 200 ? 0.8983  0.6494  0.9869  0.0008  -0.0271 -0.0976 209 LYS A CB  
3120  C CG  . LYS A 200 ? 1.1554  0.8964  1.2542  -0.0031 -0.0331 -0.1170 209 LYS A CG  
3127  N N   . ALA A 201 ? 1.1720  0.9462  1.2349  -0.0064 -0.0132 -0.0600 210 ALA A N   
3128  C CA  . ALA A 201 ? 1.0709  0.8521  1.1285  -0.0009 -0.0102 -0.0500 210 ALA A CA  
3129  C C   . ALA A 201 ? 1.0499  0.8170  1.0976  -0.0136 -0.0132 -0.0329 210 ALA A C   
3130  O O   . ALA A 201 ? 0.7659  0.5270  0.8106  -0.0102 -0.0164 -0.0240 210 ALA A O   
3131  C CB  . ALA A 201 ? 1.0805  0.8926  1.1358  0.0017  -0.0002 -0.0513 210 ALA A CB  
3137  N N   . LEU A 202 ? 0.9359  0.7001  0.9781  -0.0301 -0.0133 -0.0278 211 LEU A N   
3138  C CA  . LEU A 202 ? 0.7939  0.5526  0.8244  -0.0466 -0.0160 -0.0110 211 LEU A CA  
3139  C C   . LEU A 202 ? 0.9378  0.6636  0.9714  -0.0495 -0.0324 0.0013  211 LEU A C   
3140  O O   . LEU A 202 ? 1.1438  0.8667  1.1685  -0.0571 -0.0366 0.0168  211 LEU A O   
3141  C CB  . LEU A 202 ? 0.9395  0.7102  0.9648  -0.0651 -0.0118 -0.0092 211 LEU A CB  
3142  C CG  . LEU A 202 ? 0.6335  0.4062  0.6450  -0.0879 -0.0147 0.0084  211 LEU A CG  
3143  C CD1 . LEU A 202 ? 0.7476  0.5414  0.7497  -0.0859 -0.0064 0.0106  211 LEU A CD1 
3144  C CD2 . LEU A 202 ? 1.4277  1.2200  1.4357  -0.1059 -0.0092 0.0083  211 LEU A CD2 
3156  N N   . GLN A 203 ? 1.0327  0.7341  1.0810  -0.0441 -0.0431 -0.0059 212 GLN A N   
3157  C CA  . GLN A 203 ? 1.1468  0.8130  1.2053  -0.0459 -0.0624 0.0057  212 GLN A CA  
3158  C C   . GLN A 203 ? 1.0242  0.6888  1.0898  -0.0281 -0.0652 0.0054  212 GLN A C   
3159  O O   . GLN A 203 ? 0.9870  0.6324  1.0557  -0.0319 -0.0791 0.0227  212 GLN A O   
3160  C CB  . GLN A 203 ? 1.2223  0.8611  1.3011  -0.0419 -0.0746 -0.0073 212 GLN A CB  
3161  C CG  . GLN A 203 ? 1.1061  0.7470  1.1792  -0.0602 -0.0726 -0.0087 212 GLN A CG  
3162  C CD  . GLN A 203 ? 1.2224  0.8692  1.2769  -0.0884 -0.0737 0.0166  212 GLN A CD  
3163  O OE1 . GLN A 203 ? 1.2408  0.8675  1.2936  -0.1019 -0.0888 0.0393  212 GLN A OE1 
3164  N NE2 . GLN A 203 ? 1.5143  1.1933  1.5562  -0.0982 -0.0582 0.0128  212 GLN A NE2 
3173  N N   . VAL A 204 ? 1.0437  0.7316  1.1119  -0.0106 -0.0529 -0.0116 213 VAL A N   
3174  C CA  . VAL A 204 ? 0.6814  0.3742  0.7548  0.0043  -0.0540 -0.0111 213 VAL A CA  
3175  C C   . VAL A 204 ? 0.6864  0.3896  0.7411  -0.0063 -0.0506 0.0080  213 VAL A C   
3176  O O   . VAL A 204 ? 0.8724  0.5651  0.9291  -0.0054 -0.0605 0.0211  213 VAL A O   
3177  C CB  . VAL A 204 ? 0.8286  0.5496  0.9069  0.0210  -0.0418 -0.0315 213 VAL A CB  
3178  C CG1 . VAL A 204 ? 0.6332  0.3688  0.7123  0.0328  -0.0401 -0.0282 213 VAL A CG1 
3179  C CG2 . VAL A 204 ? 0.7351  0.4503  0.8326  0.0313  -0.0459 -0.0538 213 VAL A CG2 
3189  N N   . PHE A 205 ? 0.8752  0.5999  0.9135  -0.0174 -0.0379 0.0090  214 PHE A N   
3190  C CA  . PHE A 205 ? 0.8288  0.5670  0.8507  -0.0278 -0.0338 0.0215  214 PHE A CA  
3191  C C   . PHE A 205 ? 0.7263  0.4472  0.7408  -0.0461 -0.0475 0.0435  214 PHE A C   
3192  O O   . PHE A 205 ? 0.7574  0.4825  0.7629  -0.0509 -0.0509 0.0561  214 PHE A O   
3193  C CB  . PHE A 205 ? 1.5906  1.3549  1.6039  -0.0346 -0.0186 0.0127  214 PHE A CB  
3194  C CG  . PHE A 205 ? 0.9498  0.7365  0.9504  -0.0412 -0.0100 0.0149  214 PHE A CG  
3195  C CD1 . PHE A 205 ? 0.7849  0.5707  0.7785  -0.0415 -0.0143 0.0243  214 PHE A CD1 
3196  C CD2 . PHE A 205 ? 0.7814  0.5925  0.7798  -0.0467 0.0022  0.0049  214 PHE A CD2 
3197  C CE1 . PHE A 205 ? 1.0292  0.8374  1.0115  -0.0488 -0.0061 0.0223  214 PHE A CE1 
3198  C CE2 . PHE A 205 ? 0.6187  0.4529  0.6096  -0.0517 0.0105  0.0010  214 PHE A CE2 
3199  C CZ  . PHE A 205 ? 0.5825  0.4148  0.5644  -0.0535 0.0067  0.0087  214 PHE A CZ  
3209  N N   . HIS A 206 ? 0.8891  0.5875  0.9100  -0.0556 -0.0590 0.0500  215 HIS A N   
3210  C CA  . HIS A 206 ? 1.1867  0.8686  1.2019  -0.0762 -0.0756 0.0756  215 HIS A CA  
3211  C C   . HIS A 206 ? 0.9442  0.6087  0.9702  -0.0661 -0.0904 0.0867  215 HIS A C   
3212  O O   . HIS A 206 ? 0.9547  0.6180  0.9702  -0.0831 -0.1011 0.1104  215 HIS A O   
3213  C CB  . HIS A 206 ? 1.2223  0.8766  1.2483  -0.0874 -0.0897 0.0815  215 HIS A CB  
3214  C CG  . HIS A 206 ? 1.4522  1.1260  1.4638  -0.1072 -0.0792 0.0804  215 HIS A CG  
3215  N ND1 . HIS A 206 ? 1.4435  1.1441  1.4518  -0.0988 -0.0590 0.0587  215 HIS A ND1 
3216  C CD2 . HIS A 206 ? 1.4382  1.1111  1.4398  -0.1360 -0.0872 0.0993  215 HIS A CD2 
3217  C CE1 . HIS A 206 ? 1.4940  1.2104  1.4923  -0.1196 -0.0541 0.0624  215 HIS A CE1 
3218  N NE2 . HIS A 206 ? 1.5352  1.2368  1.5281  -0.1432 -0.0702 0.0865  215 HIS A NE2 
3226  N N   . GLN A 207 ? 1.0319  0.6905  1.0776  -0.0397 -0.0898 0.0697  216 GLN A N   
3227  C CA  . GLN A 207 ? 0.8382  0.4826  0.9001  -0.0272 -0.1044 0.0775  216 GLN A CA  
3228  C C   . GLN A 207 ? 0.8585  0.5234  0.9018  -0.0345 -0.1010 0.0919  216 GLN A C   
3229  O O   . GLN A 207 ? 0.8283  0.4824  0.8803  -0.0326 -0.1165 0.1074  216 GLN A O   
3230  C CB  . GLN A 207 ? 0.9315  0.5784  1.0169  0.0019  -0.1001 0.0517  216 GLN A CB  
3231  C CG  . GLN A 207 ? 1.1439  0.7723  1.2496  0.0095  -0.1044 0.0335  216 GLN A CG  
3232  C CD  . GLN A 207 ? 1.2816  0.9182  1.4124  0.0367  -0.1011 0.0049  216 GLN A CD  
3233  O OE1 . GLN A 207 ? 1.0588  0.7012  1.2043  0.0521  -0.1056 0.0026  216 GLN A OE1 
3234  N NE2 . GLN A 207 ? 1.6136  1.2546  1.7498  0.0412  -0.0937 -0.0176 216 GLN A NE2 
3243  N N   . ILE A 208 ? 1.0543  0.7480  1.0732  -0.0448 -0.0831 0.0879  217 ILE A N   
3244  C CA  . ILE A 208 ? 0.9741  0.6903  0.9752  -0.0513 -0.0776 0.0951  217 ILE A CA  
3245  C C   . ILE A 208 ? 0.9377  0.6460  0.9311  -0.0704 -0.0952 0.1235  217 ILE A C   
3246  O O   . ILE A 208 ? 1.0108  0.7265  1.0011  -0.0684 -0.0996 0.1318  217 ILE A O   
3247  C CB  . ILE A 208 ? 1.0825  0.8281  1.0631  -0.0629 -0.0579 0.0841  217 ILE A CB  
3248  C CG1 . ILE A 208 ? 0.9705  0.7401  0.9349  -0.0685 -0.0510 0.0851  217 ILE A CG1 
3249  C CG2 . ILE A 208 ? 1.3093  1.0584  1.2769  -0.0880 -0.0589 0.0939  217 ILE A CG2 
3250  C CD1 . ILE A 208 ? 0.9846  0.7586  0.9602  -0.0457 -0.0444 0.0701  217 ILE A CD1 
3262  N N   . HIS A 209 ? 0.8154  0.5085  0.8069  -0.0902 -0.1079 0.1407  218 HIS A N   
3263  C CA  . HIS A 209 ? 0.7889  0.4829  0.7665  -0.1173 -0.1243 0.1722  218 HIS A CA  
3264  C C   . HIS A 209 ? 1.1303  0.7976  1.1299  -0.1085 -0.1489 0.1908  218 HIS A C   
3265  O O   . HIS A 209 ? 0.8366  0.5111  0.8243  -0.1275 -0.1619 0.2169  218 HIS A O   
3266  C CB  . HIS A 209 ? 1.3664  1.0538  1.3367  -0.1435 -0.1319 0.1871  218 HIS A CB  
3267  C CG  . HIS A 209 ? 1.0999  0.8240  1.0459  -0.1586 -0.1091 0.1736  218 HIS A CG  
3268  N ND1 . HIS A 209 ? 0.9245  0.6895  0.8427  -0.1781 -0.0976 0.1759  218 HIS A ND1 
3269  C CD2 . HIS A 209 ? 1.0848  0.8143  1.0333  -0.1539 -0.0945 0.1533  218 HIS A CD2 
3270  C CE1 . HIS A 209 ? 0.9779  0.7717  0.8854  -0.1842 -0.0773 0.1569  218 HIS A CE1 
3271  N NE2 . HIS A 209 ? 0.8899  0.6623  0.8152  -0.1702 -0.0756 0.1448  218 HIS A NE2 
3279  N N   . ASP A 210 ? 0.7943  0.4337  0.8275  -0.0813 -0.1567 0.1776  219 ASP A N   
3280  C CA  . ASP A 210 ? 0.9709  0.5863  1.0327  -0.0690 -0.1809 0.1915  219 ASP A CA  
3281  C C   . ASP A 210 ? 1.0007  0.6365  1.0635  -0.0528 -0.1747 0.1854  219 ASP A C   
3282  O O   . ASP A 210 ? 1.1687  0.7921  1.2521  -0.0467 -0.1951 0.2012  219 ASP A O   
3283  C CB  . ASP A 210 ? 1.2839  0.8666  1.3850  -0.0449 -0.1910 0.1742  219 ASP A CB  
3284  C CG  . ASP A 210 ? 1.1997  0.7573  1.3038  -0.0611 -0.2011 0.1814  219 ASP A CG  
3285  O OD1 . ASP A 210 ? 0.8761  0.4302  0.9636  -0.0921 -0.2146 0.2131  219 ASP A OD1 
3286  O OD2 . ASP A 210 ? 0.9678  0.5124  1.0898  -0.0450 -0.1958 0.1560  219 ASP A OD2 
3291  N N   . HIS A 211 ? 0.7513  0.4178  0.7945  -0.0468 -0.1489 0.1645  220 HIS A N   
3292  C CA  . HIS A 211 ? 1.1278  0.8112  1.1776  -0.0277 -0.1426 0.1539  220 HIS A CA  
3293  C C   . HIS A 211 ? 1.2817  0.9964  1.2990  -0.0422 -0.1282 0.1559  220 HIS A C   
3294  O O   . HIS A 211 ? 0.8924  0.6236  0.9114  -0.0292 -0.1207 0.1461  220 HIS A O   
3295  C CB  . HIS A 211 ? 0.6980  0.3869  0.7644  -0.0011 -0.1275 0.1224  220 HIS A CB  
3296  C CG  . HIS A 211 ? 1.2245  0.8880  1.3242  0.0157  -0.1382 0.1113  220 HIS A CG  
3297  N ND1 . HIS A 211 ? 1.8060  1.4638  1.9081  0.0193  -0.1286 0.0922  220 HIS A ND1 
3298  C CD2 . HIS A 211 ? 0.7334  0.3765  0.8682  0.0305  -0.1586 0.1141  220 HIS A CD2 
3299  C CE1 . HIS A 211 ? 0.7222  0.3577  0.8580  0.0354  -0.1416 0.0817  220 HIS A CE1 
3300  N NE2 . HIS A 211 ? 1.8705  1.4958  2.0285  0.0433  -0.1603 0.0940  220 HIS A NE2 
3307  N N   . VAL A 212 ? 1.1341  0.8605  1.1233  -0.0687 -0.1232 0.1650  221 VAL A N   
3308  C CA  . VAL A 212 ? 0.7135  0.4715  0.6740  -0.0842 -0.1115 0.1646  221 VAL A CA  
3309  C C   . VAL A 212 ? 0.7461  0.5133  0.6836  -0.1179 -0.1212 0.1896  221 VAL A C   
3310  O O   . VAL A 212 ? 1.4492  1.2054  1.3860  -0.1312 -0.1268 0.1987  221 VAL A O   
3311  C CB  . VAL A 212 ? 0.8443  0.6222  0.7936  -0.0797 -0.0864 0.1366  221 VAL A CB  
3312  C CG1 . VAL A 212 ? 0.8514  0.6584  0.7786  -0.0913 -0.0769 0.1321  221 VAL A CG1 
3313  C CG2 . VAL A 212 ? 0.6542  0.4253  0.6252  -0.0506 -0.0781 0.1150  221 VAL A CG2 
3323  N N   . ASN A 213 ? 1.0674  0.8572  0.9855  -0.1340 -0.1242 0.2017  222 ASN A N   
3324  C CA  . ASN A 213 ? 1.2429  1.0545  1.1332  -0.1705 -0.1305 0.2234  222 ASN A CA  
3325  C C   . ASN A 213 ? 1.1099  0.9640  0.9714  -0.1836 -0.1083 0.2026  222 ASN A C   
3326  O O   . ASN A 213 ? 0.9393  0.7992  0.8053  -0.1642 -0.0947 0.1786  222 ASN A O   
3327  C CB  . ASN A 213 ? 1.4741  1.2780  1.3679  -0.1826 -0.1579 0.2590  222 ASN A CB  
3328  C CG  . ASN A 213 ? 1.5428  1.3815  1.4115  -0.1990 -0.1556 0.2637  222 ASN A CG  
3329  O OD1 . ASN A 213 ? 2.0765  1.9171  1.9533  -0.1803 -0.1522 0.2528  222 ASN A OD1 
3330  N ND2 . ASN A 213 ? 1.8407  1.7095  1.6791  -0.2366 -0.1598 0.2823  222 ASN A ND2 
3337  N N   . PRO A 214 ? 1.1129  0.9974  0.9484  -0.2145 -0.1028 0.2066  223 PRO A N   
3338  C CA  . PRO A 214 ? 1.1527  1.0807  0.9660  -0.2246 -0.0804 0.1792  223 PRO A CA  
3339  C C   . PRO A 214 ? 0.9490  0.8988  0.7490  -0.2286 -0.0796 0.1751  223 PRO A C   
3340  O O   . PRO A 214 ? 1.5241  1.4852  1.3259  -0.2144 -0.0630 0.1442  223 PRO A O   
3341  C CB  . PRO A 214 ? 1.5966  1.5577  1.3854  -0.2615 -0.0791 0.1901  223 PRO A CB  
3342  C CG  . PRO A 214 ? 1.7334  1.6608  1.5376  -0.2612 -0.0932 0.2113  223 PRO A CG  
3343  C CD  . PRO A 214 ? 1.5745  1.4553  1.4049  -0.2382 -0.1137 0.2290  223 PRO A CD  
3351  N N   . LYS A 215 ? 1.3713  1.3280  1.1588  -0.2492 -0.0987 0.2061  224 LYS A N   
3352  C CA  . LYS A 215 ? 1.1519  1.1365  0.9220  -0.2591 -0.0977 0.2020  224 LYS A CA  
3353  C C   . LYS A 215 ? 1.6452  1.6092  1.4362  -0.2254 -0.0920 0.1819  224 LYS A C   
3354  O O   . LYS A 215 ? 1.2710  1.2549  1.0550  -0.2221 -0.0770 0.1538  224 LYS A O   
3355  C CB  . LYS A 215 ? 1.4572  1.4461  1.2166  -0.2831 -0.1236 0.2439  224 LYS A CB  
3358  N N   . ALA A 216 ? 1.3044  1.2294  1.1238  -0.2001 -0.1040 0.1940  225 ALA A N   
3359  C CA  . ALA A 216 ? 0.9044  0.8145  0.7436  -0.1715 -0.1017 0.1810  225 ALA A CA  
3360  C C   . ALA A 216 ? 1.2355  1.1466  1.0815  -0.1534 -0.0799 0.1449  225 ALA A C   
3361  O O   . ALA A 216 ? 1.5812  1.4958  1.4321  -0.1414 -0.0744 0.1296  225 ALA A O   
3362  C CB  . ALA A 216 ? 1.1724  1.0470  1.0427  -0.1490 -0.1176 0.1978  225 ALA A CB  
3368  N N   . PHE A 217 ? 1.3371  1.2428  1.1872  -0.1505 -0.0698 0.1334  226 PHE A N   
3369  C CA  . PHE A 217 ? 1.0971  1.0025  0.9579  -0.1329 -0.0520 0.1021  226 PHE A CA  
3370  C C   . PHE A 217 ? 1.1471  1.0850  0.9912  -0.1467 -0.0382 0.0779  226 PHE A C   
3371  O O   . PHE A 217 ? 1.0301  0.9683  0.8845  -0.1328 -0.0300 0.0552  226 PHE A O   
3372  C CB  . PHE A 217 ? 0.8585  0.7511  0.7292  -0.1272 -0.0465 0.0979  226 PHE A CB  
3373  C CG  . PHE A 217 ? 0.9623  0.8551  0.8464  -0.1101 -0.0307 0.0692  226 PHE A CG  
3374  C CD1 . PHE A 217 ? 0.9542  0.8261  0.8606  -0.0848 -0.0313 0.0643  226 PHE A CD1 
3375  C CD2 . PHE A 217 ? 1.2898  1.2073  1.1663  -0.1199 -0.0161 0.0471  226 PHE A CD2 
3376  C CE1 . PHE A 217 ? 0.9823  0.8545  0.9026  -0.0705 -0.0196 0.0416  226 PHE A CE1 
3377  C CE2 . PHE A 217 ? 1.1574  1.0729  1.0519  -0.1027 -0.0045 0.0221  226 PHE A CE2 
3378  C CZ  . PHE A 217 ? 1.0419  0.9332  0.9578  -0.0787 -0.0075 0.0218  226 PHE A CZ  
3388  N N   . PHE A 218 ? 1.6490  1.6166  1.4690  -0.1750 -0.0365 0.0814  227 PHE A N   
3389  C CA  . PHE A 218 ? 1.1258  1.1286  0.9340  -0.1861 -0.0213 0.0509  227 PHE A CA  
3390  C C   . PHE A 218 ? 1.0109  1.0220  0.8139  -0.1868 -0.0243 0.0435  227 PHE A C   
3391  O O   . PHE A 218 ? 1.1340  1.1499  0.9471  -0.1763 -0.0143 0.0130  227 PHE A O   
3392  C CB  . PHE A 218 ? 0.8784  0.9213  0.6602  -0.2193 -0.0177 0.0544  227 PHE A CB  
3393  C CG  . PHE A 218 ? 0.9894  1.0777  0.7577  -0.2338 -0.0029 0.0205  227 PHE A CG  
3394  C CD1 . PHE A 218 ? 1.0355  1.1358  0.8195  -0.2220 0.0146  -0.0175 227 PHE A CD1 
3395  C CD2 . PHE A 218 ? 1.2158  1.3360  0.9585  -0.2587 -0.0074 0.0249  227 PHE A CD2 
3396  C CE1 . PHE A 218 ? 1.2362  1.3786  1.0138  -0.2328 0.0276  -0.0540 227 PHE A CE1 
3397  C CE2 . PHE A 218 ? 1.4387  1.6037  1.1705  -0.2719 0.0066  -0.0115 227 PHE A CE2 
3398  C CZ  . PHE A 218 ? 1.4123  1.5880  1.1633  -0.2579 0.0244  -0.0529 227 PHE A CZ  
3408  N N   . SER A 219 ? 1.1606  1.1715  0.9510  -0.1987 -0.0399 0.0720  228 SER A N   
3409  C CA  . SER A 219 ? 1.4630  1.4897  1.2421  -0.2073 -0.0442 0.0685  228 SER A CA  
3410  C C   . SER A 219 ? 1.6072  1.6043  1.4081  -0.1819 -0.0512 0.0712  228 SER A C   
3411  O O   . SER A 219 ? 1.2686  1.2755  1.0656  -0.1846 -0.0520 0.0600  228 SER A O   
3412  C CB  . SER A 219 ? 1.3036  1.3509  1.0572  -0.2366 -0.0591 0.1007  228 SER A CB  
3413  O OG  . SER A 219 ? 1.2203  1.2359  0.9885  -0.2252 -0.0777 0.1351  228 SER A OG  
3419  N N   . VAL A 220 ? 0.9220  0.8869  0.7457  -0.1592 -0.0563 0.0843  229 VAL A N   
3420  C CA  . VAL A 220 ? 0.7160  0.6611  0.5590  -0.1387 -0.0643 0.0910  229 VAL A CA  
3421  C C   . VAL A 220 ? 0.7345  0.6593  0.6022  -0.1131 -0.0558 0.0743  229 VAL A C   
3422  O O   . VAL A 220 ? 1.1561  1.0799  1.0329  -0.1047 -0.0522 0.0579  229 VAL A O   
3423  C CB  . VAL A 220 ? 0.7846  0.7166  0.6347  -0.1357 -0.0819 0.1245  229 VAL A CB  
3424  C CG1 . VAL A 220 ? 0.7696  0.6882  0.6433  -0.1128 -0.0883 0.1282  229 VAL A CG1 
3425  C CG2 . VAL A 220 ? 0.7180  0.6729  0.5427  -0.1652 -0.0936 0.1459  229 VAL A CG2 
3435  N N   . LEU A 221 ? 0.9081  0.8160  0.7881  -0.1016 -0.0550 0.0805  230 LEU A N   
3436  C CA  . LEU A 221 ? 0.8043  0.6961  0.7076  -0.0783 -0.0494 0.0689  230 LEU A CA  
3437  C C   . LEU A 221 ? 0.7795  0.6769  0.6859  -0.0769 -0.0363 0.0413  230 LEU A C   
3438  O O   . LEU A 221 ? 0.6368  0.5248  0.5616  -0.0613 -0.0343 0.0322  230 LEU A O   
3439  C CB  . LEU A 221 ? 0.6792  0.5546  0.5939  -0.0681 -0.0497 0.0761  230 LEU A CB  
3440  C CG  . LEU A 221 ? 0.6340  0.4972  0.5716  -0.0457 -0.0455 0.0670  230 LEU A CG  
3441  C CD1 . LEU A 221 ? 0.6243  0.4876  0.5752  -0.0334 -0.0539 0.0755  230 LEU A CD1 
3442  C CD2 . LEU A 221 ? 0.8092  0.6583  0.7564  -0.0380 -0.0454 0.0705  230 LEU A CD2 
3454  N N   . ARG A 222 ? 0.9880  0.9024  0.8798  -0.0927 -0.0281 0.0282  231 ARG A N   
3455  C CA  . ARG A 222 ? 1.1323  1.0544  1.0328  -0.0899 -0.0166 -0.0016 231 ARG A CA  
3456  C C   . ARG A 222 ? 1.0915  1.0158  0.9977  -0.0884 -0.0191 -0.0158 231 ARG A C   
3457  O O   . ARG A 222 ? 1.6029  1.5182  1.5302  -0.0759 -0.0168 -0.0329 231 ARG A O   
3458  C CB  . ARG A 222 ? 1.1129  1.0612  0.9966  -0.1089 -0.0069 -0.0136 231 ARG A CB  
3459  C CG  . ARG A 222 ? 1.2065  1.1679  1.1037  -0.1051 0.0061  -0.0475 231 ARG A CG  
3460  C CD  . ARG A 222 ? 1.0802  1.0777  0.9595  -0.1265 0.0165  -0.0603 231 ARG A CD  
3461  N NE  . ARG A 222 ? 1.3109  1.3363  1.1652  -0.1491 0.0151  -0.0621 231 ARG A NE  
3462  C CZ  . ARG A 222 ? 1.5543  1.6101  1.4066  -0.1581 0.0236  -0.0947 231 ARG A CZ  
3463  N NH1 . ARG A 222 ? 1.8734  1.9333  1.7512  -0.1447 0.0333  -0.1289 231 ARG A NH1 
3464  N NH2 . ARG A 222 ? 1.6109  1.6948  1.4372  -0.1812 0.0215  -0.0939 231 ARG A NH2 
3478  N N   . ILE A 223 ? 1.0354  0.9693  0.9253  -0.1010 -0.0265 -0.0057 232 ILE A N   
3479  C CA  . ILE A 223 ? 1.2639  1.2008  1.1569  -0.1032 -0.0304 -0.0185 232 ILE A CA  
3480  C C   . ILE A 223 ? 1.0451  0.9591  0.9621  -0.0845 -0.0375 -0.0122 232 ILE A C   
3481  O O   . ILE A 223 ? 0.8523  0.7594  0.7860  -0.0793 -0.0384 -0.0302 232 ILE A O   
3482  C CB  . ILE A 223 ? 1.0637  1.0172  0.9324  -0.1221 -0.0385 -0.0035 232 ILE A CB  
3483  C CG1 . ILE A 223 ? 1.1024  1.0834  0.9442  -0.1452 -0.0337 -0.0018 232 ILE A CG1 
3484  C CG2 . ILE A 223 ? 1.1767  1.1368  1.0457  -0.1283 -0.0417 -0.0209 232 ILE A CG2 
3485  C CD1 . ILE A 223 ? 1.0624  1.0706  0.8975  -0.1573 -0.0201 -0.0368 232 ILE A CD1 
3497  N N   . TYR A 224 ? 0.9979  0.9014  0.9195  -0.0745 -0.0432 0.0126  233 TYR A N   
3498  C CA  . TYR A 224 ? 0.8133  0.7048  0.7546  -0.0601 -0.0497 0.0214  233 TYR A CA  
3499  C C   . TYR A 224 ? 0.9048  0.7849  0.8662  -0.0459 -0.0446 0.0131  233 TYR A C   
3500  O O   . TYR A 224 ? 0.8598  0.7341  0.8376  -0.0370 -0.0500 0.0188  233 TYR A O   
3501  C CB  . TYR A 224 ? 0.6836  0.5763  0.6240  -0.0551 -0.0578 0.0479  233 TYR A CB  
3502  C CG  . TYR A 224 ? 0.8511  0.7559  0.7762  -0.0685 -0.0661 0.0594  233 TYR A CG  
3503  C CD1 . TYR A 224 ? 1.3481  1.2579  1.2764  -0.0716 -0.0735 0.0613  233 TYR A CD1 
3504  C CD2 . TYR A 224 ? 1.0437  0.9560  0.9506  -0.0808 -0.0678 0.0691  233 TYR A CD2 
3505  C CE1 . TYR A 224 ? 1.0949  1.0176  1.0090  -0.0851 -0.0816 0.0715  233 TYR A CE1 
3506  C CE2 . TYR A 224 ? 0.8609  0.7869  0.7531  -0.0955 -0.0769 0.0812  233 TYR A CE2 
3507  C CZ  . TYR A 224 ? 0.9616  0.8932  0.8574  -0.0970 -0.0834 0.0815  233 TYR A CZ  
3508  O OH  . TYR A 224 ? 0.8019  0.7493  0.6828  -0.1127 -0.0932 0.0938  233 TYR A OH  
3518  N N   . LEU A 225 ? 1.1473  1.0272  1.1084  -0.0456 -0.0352 -0.0001 234 LEU A N   
3519  C CA  . LEU A 225 ? 0.9874  0.8581  0.9692  -0.0333 -0.0319 -0.0081 234 LEU A CA  
3520  C C   . LEU A 225 ? 0.8085  0.6788  0.8040  -0.0342 -0.0292 -0.0336 234 LEU A C   
3521  O O   . LEU A 225 ? 0.7139  0.5771  0.7299  -0.0246 -0.0283 -0.0407 234 LEU A O   
3522  C CB  . LEU A 225 ? 0.8891  0.7590  0.8676  -0.0294 -0.0249 -0.0039 234 LEU A CB  
3523  C CG  . LEU A 225 ? 0.8286  0.6952  0.8022  -0.0247 -0.0295 0.0179  234 LEU A CG  
3524  C CD1 . LEU A 225 ? 0.7509  0.6132  0.7241  -0.0219 -0.0233 0.0177  234 LEU A CD1 
3525  C CD2 . LEU A 225 ? 0.6250  0.4907  0.6130  -0.0133 -0.0370 0.0299  234 LEU A CD2 
3537  N N   . SER A 226 ? 0.6731  0.5517  0.6603  -0.0452 -0.0296 -0.0479 235 SER A N   
3538  C CA  . SER A 226 ? 0.5908  0.4700  0.5949  -0.0456 -0.0289 -0.0769 235 SER A CA  
3539  C C   . SER A 226 ? 0.9319  0.7925  0.9615  -0.0388 -0.0423 -0.0759 235 SER A C   
3540  O O   . SER A 226 ? 0.8798  0.7351  0.9051  -0.0411 -0.0520 -0.0559 235 SER A O   
3541  C CB  . SER A 226 ? 0.6648  0.5633  0.6486  -0.0618 -0.0253 -0.0923 235 SER A CB  
3542  O OG  . SER A 226 ? 1.0069  0.9223  0.9648  -0.0713 -0.0168 -0.0819 235 SER A OG  
3548  N N   . GLY A 227 ? 0.9889  0.8411  1.0474  -0.0315 -0.0444 -0.0972 236 GLY A N   
3549  C CA  . GLY A 227 ? 0.7346  0.5664  0.8223  -0.0269 -0.0606 -0.0963 236 GLY A CA  
3550  C C   . GLY A 227 ? 0.7991  0.6276  0.9042  -0.0300 -0.0650 -0.1290 236 GLY A C   
3551  O O   . GLY A 227 ? 0.6359  0.4825  0.7216  -0.0397 -0.0561 -0.1482 236 GLY A O   
3555  N N   . TRP A 228 ? 1.2502  1.0570  1.3928  -0.0231 -0.0801 -0.1358 237 TRP A N   
3556  C CA  . TRP A 228 ? 1.0937  0.8921  1.2587  -0.0253 -0.0885 -0.1674 237 TRP A CA  
3557  C C   . TRP A 228 ? 1.1859  0.9694  1.3993  -0.0111 -0.0962 -0.1899 237 TRP A C   
3558  O O   . TRP A 228 ? 1.3769  1.1341  1.6269  -0.0077 -0.1167 -0.1924 237 TRP A O   
3559  C CB  . TRP A 228 ? 0.6690  0.4510  0.8334  -0.0348 -0.1062 -0.1503 237 TRP A CB  
3560  C CG  . TRP A 228 ? 0.8229  0.5953  0.9852  -0.0352 -0.1170 -0.1071 237 TRP A CG  
3561  C CD1 . TRP A 228 ? 0.9226  0.6740  1.1172  -0.0312 -0.1355 -0.0902 237 TRP A CD1 
3562  C CD2 . TRP A 228 ? 0.6309  0.4193  0.7584  -0.0414 -0.1109 -0.0754 237 TRP A CD2 
3563  N NE1 . TRP A 228 ? 0.7927  0.5511  0.9716  -0.0359 -0.1391 -0.0517 237 TRP A NE1 
3564  C CE2 . TRP A 228 ? 0.6606  0.4411  0.8005  -0.0406 -0.1240 -0.0444 237 TRP A CE2 
3565  C CE3 . TRP A 228 ? 0.6241  0.4342  0.7140  -0.0477 -0.0971 -0.0707 237 TRP A CE3 
3566  C CZ2 . TRP A 228 ? 0.6328  0.4298  0.7498  -0.0440 -0.1209 -0.0143 237 TRP A CZ2 
3567  C CZ3 . TRP A 228 ? 0.7881  0.6080  0.8595  -0.0494 -0.0967 -0.0398 237 TRP A CZ3 
3568  C CH2 . TRP A 228 ? 0.6714  0.4865  0.7565  -0.0465 -0.1071 -0.0142 237 TRP A CH2 
3579  N N   . LYS A 229 ? 1.0596  0.8604  1.2756  -0.0030 -0.0810 -0.2046 238 LYS A N   
3580  C CA  . LYS A 229 ? 0.8828  0.6778  1.1457  0.0112  -0.0852 -0.2330 238 LYS A CA  
3581  C C   . LYS A 229 ? 0.8370  0.6667  1.0923  0.0105  -0.0640 -0.2741 238 LYS A C   
3582  O O   . LYS A 229 ? 1.5329  1.3888  1.7556  0.0055  -0.0454 -0.2671 238 LYS A O   
3583  C CB  . LYS A 229 ? 0.9167  0.7029  1.1955  0.0211  -0.0897 -0.2070 238 LYS A CB  
3584  C CG  . LYS A 229 ? 0.9260  0.6991  1.2633  0.0369  -0.1022 -0.2272 238 LYS A CG  
3585  C CD  . LYS A 229 ? 0.8671  0.6323  1.2122  0.0418  -0.1095 -0.1913 238 LYS A CD  
3586  C CE  . LYS A 229 ? 0.7952  0.5496  1.1964  0.0565  -0.1233 -0.2019 238 LYS A CE  
3587  N NZ  . LYS A 229 ? 1.3274  1.0847  1.7219  0.0570  -0.1250 -0.1648 238 LYS A NZ  
3601  N N   . GLY A 230 ? 1.0740  0.9063  1.3588  0.0138  -0.0674 -0.3174 239 GLY A N   
3602  C CA  . GLY A 230 ? 1.1034  0.9777  1.3807  0.0108  -0.0464 -0.3599 239 GLY A CA  
3603  C C   . GLY A 230 ? 1.1002  1.0048  1.3208  -0.0103 -0.0308 -0.3559 239 GLY A C   
3604  O O   . GLY A 230 ? 1.2610  1.2078  1.4600  -0.0184 -0.0107 -0.3747 239 GLY A O   
3608  N N   . ASN A 231 ? 1.2491  1.1358  1.4453  -0.0209 -0.0408 -0.3293 240 ASN A N   
3609  C CA  . ASN A 231 ? 1.1190  1.0329  1.2638  -0.0414 -0.0295 -0.3216 240 ASN A CA  
3610  C C   . ASN A 231 ? 1.2760  1.1992  1.4221  -0.0517 -0.0332 -0.3563 240 ASN A C   
3611  O O   . ASN A 231 ? 1.3601  1.2505  1.5272  -0.0489 -0.0522 -0.3538 240 ASN A O   
3612  C CB  . ASN A 231 ? 1.1254  1.0192  1.2415  -0.0466 -0.0373 -0.2694 240 ASN A CB  
3613  C CG  . ASN A 231 ? 0.9745  0.8965  1.0388  -0.0660 -0.0263 -0.2529 240 ASN A CG  
3614  O OD1 . ASN A 231 ? 0.7492  0.7060  0.7935  -0.0811 -0.0158 -0.2792 240 ASN A OD1 
3615  N ND2 . ASN A 231 ? 0.7853  0.6943  0.8289  -0.0672 -0.0308 -0.2092 240 ASN A ND2 
3622  N N   . PRO A 232 ? 1.5447  1.5142  1.6670  -0.0664 -0.0165 -0.3870 241 PRO A N   
3623  C CA  . PRO A 232 ? 1.7035  1.6872  1.8241  -0.0784 -0.0191 -0.4228 241 PRO A CA  
3624  C C   . PRO A 232 ? 1.7146  1.6788  1.8097  -0.0918 -0.0327 -0.3934 241 PRO A C   
3625  O O   . PRO A 232 ? 1.2835  1.2343  1.3968  -0.0939 -0.0449 -0.4174 241 PRO A O   
3626  C CB  . PRO A 232 ? 0.9863  1.0332  1.0724  -0.0973 0.0037  -0.4478 241 PRO A CB  
3627  C CG  . PRO A 232 ? 1.0811  1.1424  1.1757  -0.0875 0.0163  -0.4461 241 PRO A CG  
3628  C CD  . PRO A 232 ? 0.9376  0.9518  1.0420  -0.0720 0.0050  -0.3984 241 PRO A CD  
3636  N N   . GLN A 233 ? 1.4803  1.4445  1.5359  -0.1013 -0.0316 -0.3449 242 GLN A N   
3637  C CA  . GLN A 233 ? 1.5620  1.5160  1.5954  -0.1151 -0.0438 -0.3229 242 GLN A CA  
3638  C C   . GLN A 233 ? 1.6104  1.5148  1.6745  -0.1031 -0.0658 -0.3020 242 GLN A C   
3639  O O   . GLN A 233 ? 1.7922  1.6869  1.8451  -0.1140 -0.0780 -0.2875 242 GLN A O   
3640  C CB  . GLN A 233 ? 1.4142  1.3874  1.3988  -0.1301 -0.0380 -0.2801 242 GLN A CB  
3641  C CG  . GLN A 233 ? 1.3927  1.3529  1.3735  -0.1187 -0.0349 -0.2412 242 GLN A CG  
3642  C CD  . GLN A 233 ? 1.1841  1.1710  1.1207  -0.1348 -0.0273 -0.2111 242 GLN A CD  
3643  O OE1 . GLN A 233 ? 0.9171  0.9219  0.8255  -0.1534 -0.0306 -0.2027 242 GLN A OE1 
3644  N NE2 . GLN A 233 ? 1.4963  1.4858  1.4287  -0.1286 -0.0188 -0.1950 242 GLN A NE2 
3653  N N   . LEU A 234 ? 1.3370  1.2130  1.4398  -0.0830 -0.0719 -0.2992 243 LEU A N   
3654  C CA  . LEU A 234 ? 1.4755  1.3073  1.6131  -0.0737 -0.0948 -0.2822 243 LEU A CA  
3655  C C   . LEU A 234 ? 1.5418  1.3542  1.7345  -0.0555 -0.1018 -0.3152 243 LEU A C   
3656  O O   . LEU A 234 ? 1.4960  1.2880  1.7144  -0.0413 -0.1081 -0.2974 243 LEU A O   
3657  C CB  . LEU A 234 ? 1.2659  1.0839  1.3910  -0.0701 -0.0993 -0.2286 243 LEU A CB  
3658  C CG  . LEU A 234 ? 1.1926  1.0231  1.2758  -0.0850 -0.0990 -0.1945 243 LEU A CG  
3659  C CD1 . LEU A 234 ? 0.7008  0.5245  0.7774  -0.0781 -0.0999 -0.1515 243 LEU A CD1 
3660  C CD2 . LEU A 234 ? 1.3886  1.2051  1.4752  -0.0963 -0.1166 -0.1903 243 LEU A CD2 
3672  N N   . SER A 235 ? 1.7259  1.5476  1.9385  -0.0566 -0.1012 -0.3665 244 SER A N   
3673  C CA  . SER A 235 ? 1.4031  1.2164  1.6701  -0.0385 -0.1045 -0.4089 244 SER A CA  
3674  C C   . SER A 235 ? 1.3273  1.0917  1.6433  -0.0228 -0.1292 -0.3863 244 SER A C   
3675  O O   . SER A 235 ? 1.1356  0.8952  1.4884  -0.0055 -0.1295 -0.3974 244 SER A O   
3676  C CB  . SER A 235 ? 1.1793  1.0008  1.4666  -0.0429 -0.1079 -0.4656 244 SER A CB  
3677  O OG  . SER A 235 ? 1.4477  1.3187  1.6868  -0.0619 -0.0869 -0.4842 244 SER A OG  
3683  N N   . ASP A 236 ? 1.6598  1.3901  1.9802  -0.0301 -0.1520 -0.3561 245 ASP A N   
3684  C CA  . ASP A 236 ? 1.3672  1.0524  1.7368  -0.0201 -0.1799 -0.3353 245 ASP A CA  
3685  C C   . ASP A 236 ? 1.0259  0.7017  1.3759  -0.0235 -0.1856 -0.2738 245 ASP A C   
3686  O O   . ASP A 236 ? 1.2250  0.8682  1.6111  -0.0197 -0.2100 -0.2498 245 ASP A O   
3687  C CB  . ASP A 236 ? 1.6296  1.2817  2.0273  -0.0277 -0.2063 -0.3475 245 ASP A CB  
3688  C CG  . ASP A 236 ? 1.6224  1.2934  2.0364  -0.0223 -0.1979 -0.4031 245 ASP A CG  
3689  O OD1 . ASP A 236 ? 1.6397  1.3144  2.0955  -0.0031 -0.1982 -0.4224 245 ASP A OD1 
3690  O OD2 . ASP A 236 ? 1.4735  1.1630  1.8569  -0.0378 -0.1895 -0.4259 245 ASP A OD2 
3695  N N   . GLY A 237 ? 0.9705  0.6756  1.2670  -0.0314 -0.1652 -0.2484 246 GLY A N   
3696  C CA  . GLY A 237 ? 0.7646  0.4671  1.0417  -0.0347 -0.1687 -0.1951 246 GLY A CA  
3697  C C   . GLY A 237 ? 0.9694  0.6702  1.2197  -0.0518 -0.1782 -0.1640 246 GLY A C   
3698  O O   . GLY A 237 ? 0.8884  0.5947  1.1231  -0.0633 -0.1783 -0.1795 246 GLY A O   
3702  N N   . LEU A 238 ? 0.9660  0.6629  1.2122  -0.0543 -0.1867 -0.1196 247 LEU A N   
3703  C CA  . LEU A 238 ? 0.9981  0.7012  1.2200  -0.0697 -0.1943 -0.0860 247 LEU A CA  
3704  C C   . LEU A 238 ? 1.1124  0.7876  1.3669  -0.0785 -0.2250 -0.0634 247 LEU A C   
3705  O O   . LEU A 238 ? 1.2747  0.9327  1.5619  -0.0725 -0.2387 -0.0516 247 LEU A O   
3706  C CB  . LEU A 238 ? 1.4328  1.1628  1.6216  -0.0681 -0.1787 -0.0538 247 LEU A CB  
3707  C CG  . LEU A 238 ? 1.3405  1.0901  1.4986  -0.0808 -0.1789 -0.0232 247 LEU A CG  
3708  C CD1 . LEU A 238 ? 0.9161  0.6805  1.0449  -0.0881 -0.1680 -0.0405 247 LEU A CD1 
3709  C CD2 . LEU A 238 ? 1.4482  1.2209  1.5874  -0.0751 -0.1667 0.0043  247 LEU A CD2 
3721  N N   . VAL A 239 ? 0.8589  0.5301  1.1059  -0.0945 -0.2372 -0.0572 248 VAL A N   
3722  C CA  . VAL A 239 ? 1.3612  1.0146  1.6286  -0.1089 -0.2658 -0.0247 248 VAL A CA  
3723  C C   . VAL A 239 ? 0.8285  0.5116  1.0694  -0.1163 -0.2613 0.0210  248 VAL A C   
3724  O O   . VAL A 239 ? 0.7331  0.4452  0.9374  -0.1211 -0.2464 0.0290  248 VAL A O   
3725  C CB  . VAL A 239 ? 2.0813  1.7243  2.3472  -0.1251 -0.2794 -0.0342 248 VAL A CB  
3726  C CG1 . VAL A 239 ? 0.8241  0.4523  1.1091  -0.1427 -0.3090 0.0037  248 VAL A CG1 
3727  C CG2 . VAL A 239 ? 0.8420  0.4594  1.1348  -0.1193 -0.2844 -0.0833 248 VAL A CG2 
3737  N N   . TYR A 240 ? 1.1215  0.7998  1.3833  -0.1193 -0.2768 0.0514  249 TYR A N   
3738  C CA  . TYR A 240 ? 0.9591  0.6708  1.1995  -0.1300 -0.2756 0.0933  249 TYR A CA  
3739  C C   . TYR A 240 ? 1.0321  0.7365  1.2859  -0.1536 -0.3039 0.1203  249 TYR A C   
3740  O O   . TYR A 240 ? 1.1233  0.8129  1.4063  -0.1639 -0.3290 0.1447  249 TYR A O   
3741  C CB  . TYR A 240 ? 1.0617  0.7833  1.3110  -0.1221 -0.2728 0.1107  249 TYR A CB  
3742  C CG  . TYR A 240 ? 0.9122  0.6443  1.1451  -0.1013 -0.2447 0.0868  249 TYR A CG  
3743  C CD1 . TYR A 240 ? 1.4105  1.1181  1.6621  -0.0868 -0.2403 0.0516  249 TYR A CD1 
3744  C CD2 . TYR A 240 ? 1.3424  1.1100  1.5442  -0.0969 -0.2238 0.0984  249 TYR A CD2 
3745  C CE1 . TYR A 240 ? 1.5281  1.2479  1.7646  -0.0715 -0.2163 0.0325  249 TYR A CE1 
3746  C CE2 . TYR A 240 ? 1.1674  0.9416  1.3556  -0.0807 -0.2013 0.0787  249 TYR A CE2 
3747  C CZ  . TYR A 240 ? 1.0327  0.7834  1.2373  -0.0693 -0.1979 0.0476  249 TYR A CZ  
3748  O OH  . TYR A 240 ? 0.6556  0.4151  0.8473  -0.0553 -0.1760 0.0289  249 TYR A OH  
3758  N N   . GLU A 241 ? 0.7547  0.4704  0.9870  -0.1639 -0.3013 0.1176  250 GLU A N   
3759  C CA  . GLU A 241 ? 0.9347  0.6414  1.1783  -0.1874 -0.3276 0.1373  250 GLU A CA  
3760  C C   . GLU A 241 ? 1.4890  1.2139  1.7424  -0.2045 -0.3456 0.1844  250 GLU A C   
3761  O O   . GLU A 241 ? 0.7517  0.5219  0.9817  -0.2056 -0.3313 0.2072  250 GLU A O   
3762  C CB  . GLU A 241 ? 1.1567  0.8901  1.3667  -0.1958 -0.3163 0.1348  250 GLU A CB  
3763  C CG  . GLU A 241 ? 1.0054  0.7317  1.2227  -0.2206 -0.3410 0.1500  250 GLU A CG  
3764  C CD  . GLU A 241 ? 1.2042  0.9626  1.3874  -0.2271 -0.3277 0.1483  250 GLU A CD  
3765  O OE1 . GLU A 241 ? 1.4944  1.2972  1.6579  -0.2314 -0.3188 0.1763  250 GLU A OE1 
3766  O OE2 . GLU A 241 ? 0.8511  0.5938  1.0281  -0.2275 -0.3257 0.1177  250 GLU A OE2 
3773  N N   . GLY A 242 ? 1.0408  0.7321  1.3305  -0.2192 -0.3786 0.1983  251 GLY A N   
3774  C CA  . GLY A 242 ? 0.8412  0.5519  1.1397  -0.2426 -0.4003 0.2466  251 GLY A CA  
3775  C C   . GLY A 242 ? 1.0250  0.7424  1.3374  -0.2378 -0.4030 0.2654  251 GLY A C   
3776  O O   . GLY A 242 ? 1.0753  0.8087  1.3995  -0.2561 -0.4252 0.3032  251 GLY A O   
3780  N N   . PHE A 243 ? 0.7880  0.5028  1.0955  -0.2115 -0.3796 0.2386  252 PHE A N   
3781  C CA  . PHE A 243 ? 1.5361  1.2506  1.8621  -0.2060 -0.3848 0.2526  252 PHE A CA  
3782  C C   . PHE A 243 ? 0.8081  0.4707  1.1776  -0.1911 -0.4012 0.2289  252 PHE A C   
3783  O O   . PHE A 243 ? 0.8292  0.4918  1.2257  -0.1944 -0.4245 0.2480  252 PHE A O   
3784  C CB  . PHE A 243 ? 1.2394  0.9907  1.5338  -0.1868 -0.3494 0.2410  252 PHE A CB  
3785  C CG  . PHE A 243 ? 1.4330  1.2055  1.7338  -0.1898 -0.3530 0.2664  252 PHE A CG  
3786  C CD1 . PHE A 243 ? 1.7436  1.5657  2.0289  -0.2113 -0.3570 0.3051  252 PHE A CD1 
3787  C CD2 . PHE A 243 ? 1.2012  0.9496  1.5236  -0.1727 -0.3524 0.2512  252 PHE A CD2 
3788  C CE1 . PHE A 243 ? 1.1840  1.0313  1.4733  -0.2171 -0.3608 0.3286  252 PHE A CE1 
3789  C CE2 . PHE A 243 ? 1.3634  1.1332  1.6913  -0.1773 -0.3571 0.2760  252 PHE A CE2 
3790  C CZ  . PHE A 243 ? 1.3291  1.1488  1.6391  -0.2001 -0.3612 0.3147  252 PHE A CZ  
3800  N N   . TRP A 244 ? 0.8083  0.4424  1.1818  -0.1709 -0.3867 0.1828  253 TRP A N   
3801  C CA  . TRP A 244 ? 1.0002  0.5992  1.4131  -0.1510 -0.3960 0.1494  253 TRP A CA  
3802  C C   . TRP A 244 ? 1.1090  0.6824  1.5300  -0.1489 -0.4000 0.1152  253 TRP A C   
3803  O O   . TRP A 244 ? 1.2117  0.7875  1.6046  -0.1535 -0.3842 0.0972  253 TRP A O   
3804  C CB  . TRP A 244 ? 1.1855  0.7785  1.6011  -0.1268 -0.3733 0.1173  253 TRP A CB  
3805  C CG  . TRP A 244 ? 0.9709  0.5827  1.3892  -0.1244 -0.3722 0.1432  253 TRP A CG  
3806  C CD1 . TRP A 244 ? 0.8576  0.4767  1.3025  -0.1301 -0.3959 0.1720  253 TRP A CD1 
3807  C CD2 . TRP A 244 ? 1.0346  0.6780  1.4210  -0.1134 -0.3420 0.1407  253 TRP A CD2 
3808  N NE1 . TRP A 244 ? 1.8775  1.5187  2.3140  -0.1278 -0.3863 0.1894  253 TRP A NE1 
3809  C CE2 . TRP A 244 ? 1.1458  0.7985  1.5476  -0.1170 -0.3536 0.1704  253 TRP A CE2 
3810  C CE3 . TRP A 244 ? 0.8017  0.4706  1.1467  -0.1009 -0.3064 0.1165  253 TRP A CE3 
3811  C CZ2 . TRP A 244 ? 0.9346  0.6213  1.3113  -0.1078 -0.3294 0.1734  253 TRP A CZ2 
3812  C CZ3 . TRP A 244 ? 1.0379  0.7369  1.3605  -0.0913 -0.2840 0.1210  253 TRP A CZ3 
3813  C CH2 . TRP A 244 ? 1.0793  0.7870  1.4176  -0.0945 -0.2949 0.1477  253 TRP A CH2 
3824  N N   . GLU A 245 ? 1.0685  0.6189  1.5303  -0.1411 -0.4216 0.1040  254 GLU A N   
3825  C CA  . GLU A 245 ? 1.1152  0.6414  1.5902  -0.1393 -0.4286 0.0713  254 GLU A CA  
3826  C C   . GLU A 245 ? 1.2004  0.7187  1.6714  -0.1200 -0.4029 0.0145  254 GLU A C   
3827  O O   . GLU A 245 ? 0.9316  0.4486  1.3811  -0.1262 -0.3928 -0.0098 254 GLU A O   
3828  C CB  . GLU A 245 ? 1.1091  0.6140  1.6341  -0.1356 -0.4608 0.0765  254 GLU A CB  
3829  C CG  . GLU A 245 ? 1.3484  0.8285  1.8904  -0.1368 -0.4731 0.0497  254 GLU A CG  
3830  C CD  . GLU A 245 ? 1.4597  0.9227  2.0423  -0.1448 -0.5123 0.0752  254 GLU A CD  
3831  O OE1 . GLU A 245 ? 1.3017  0.7795  1.8863  -0.1595 -0.5319 0.1250  254 GLU A OE1 
3832  O OE2 . GLU A 245 ? 1.2537  0.6907  1.8665  -0.1375 -0.5242 0.0443  254 GLU A OE2 
3839  N N   . ASP A 246 ? 1.2458  0.7645  1.7352  -0.0988 -0.3921 -0.0063 255 ASP A N   
3840  C CA  . ASP A 246 ? 1.2128  0.7315  1.7013  -0.0805 -0.3679 -0.0613 255 ASP A CA  
3841  C C   . ASP A 246 ? 1.1817  0.7205  1.6301  -0.0792 -0.3392 -0.0651 255 ASP A C   
3842  O O   . ASP A 246 ? 1.0583  0.6093  1.4882  -0.0867 -0.3373 -0.0267 255 ASP A O   
3843  C CB  . ASP A 246 ? 1.4343  0.9458  1.9707  -0.0574 -0.3729 -0.0868 255 ASP A CB  
3844  C CG  . ASP A 246 ? 1.9424  1.4327  2.5246  -0.0583 -0.4057 -0.0795 255 ASP A CG  
3845  O OD1 . ASP A 246 ? 3.2576  2.7351  3.8508  -0.0576 -0.4093 -0.1114 255 ASP A OD1 
3846  O OD2 . ASP A 246 ? 1.6257  1.1135  2.2325  -0.0613 -0.4288 -0.0420 255 ASP A OD2 
3851  N N   . PRO A 247 ? 1.1653  0.7111  1.5993  -0.0712 -0.3170 -0.1114 256 PRO A N   
3852  C CA  . PRO A 247 ? 1.2252  0.8085  1.6156  -0.0639 -0.2830 -0.1134 256 PRO A CA  
3853  C C   . PRO A 247 ? 1.1128  0.6975  1.5254  -0.0455 -0.2765 -0.1176 256 PRO A C   
3854  O O   . PRO A 247 ? 1.3363  0.9019  1.7963  -0.0320 -0.2879 -0.1421 256 PRO A O   
3855  C CB  . PRO A 247 ? 1.0375  0.6375  1.4056  -0.0624 -0.2620 -0.1604 256 PRO A CB  
3856  C CG  . PRO A 247 ? 0.8786  0.4452  1.2950  -0.0601 -0.2834 -0.1983 256 PRO A CG  
3857  C CD  . PRO A 247 ? 1.0903  0.6316  1.5354  -0.0670 -0.3145 -0.1594 256 PRO A CD  
3865  N N   . LYS A 248 ? 1.2328  0.8466  1.6099  -0.0447 -0.2577 -0.0902 257 LYS A N   
3866  C CA  . LYS A 248 ? 1.1020  0.7236  1.4901  -0.0308 -0.2496 -0.0854 257 LYS A CA  
3867  C C   . LYS A 248 ? 0.9837  0.6391  1.3324  -0.0223 -0.2141 -0.1062 257 LYS A C   
3868  O O   . LYS A 248 ? 1.1783  0.8564  1.4813  -0.0308 -0.1976 -0.0986 257 LYS A O   
3869  C CB  . LYS A 248 ? 0.9086  0.5361  1.2909  -0.0403 -0.2615 -0.0320 257 LYS A CB  
3870  C CG  . LYS A 248 ? 0.9711  0.5716  1.3846  -0.0556 -0.2978 -0.0022 257 LYS A CG  
3871  C CD  . LYS A 248 ? 1.4079  0.9785  1.8796  -0.0454 -0.3212 -0.0195 257 LYS A CD  
3872  C CE  . LYS A 248 ? 0.9394  0.5036  1.4358  -0.0586 -0.3539 0.0193  257 LYS A CE  
3883  N N   . GLU A 249 ? 1.1806  0.8401  1.5498  -0.0064 -0.2041 -0.1326 258 GLU A N   
3884  C CA  . GLU A 249 ? 1.0193  0.7110  1.3554  -0.0001 -0.1727 -0.1511 258 GLU A CA  
3885  C C   . GLU A 249 ? 0.9626  0.6681  1.2818  0.0024  -0.1648 -0.1178 258 GLU A C   
3886  O O   . GLU A 249 ? 0.6879  0.3802  1.0381  0.0070  -0.1806 -0.1003 258 GLU A O   
3887  C CB  . GLU A 249 ? 1.1273  0.8235  1.4941  0.0142  -0.1643 -0.2001 258 GLU A CB  
3888  C CG  . GLU A 249 ? 1.2821  0.9757  1.6604  0.0121  -0.1655 -0.2441 258 GLU A CG  
3889  C CD  . GLU A 249 ? 1.3598  1.0706  1.7654  0.0256  -0.1527 -0.2979 258 GLU A CD  
3890  O OE1 . GLU A 249 ? 2.3619  2.0503  2.8252  0.0375  -0.1709 -0.3251 258 GLU A OE1 
3891  O OE2 . GLU A 249 ? 1.2202  0.9684  1.5919  0.0237  -0.1256 -0.3135 258 GLU A OE2 
3898  N N   . PHE A 250 ? 0.9983  0.9621  1.5604  0.0592  -0.3255 -0.2710 259 PHE A N   
3899  C CA  . PHE A 250 ? 0.9380  0.8969  1.4842  0.0492  -0.3128 -0.2393 259 PHE A CA  
3900  C C   . PHE A 250 ? 0.9714  0.9884  1.4913  0.0465  -0.2807 -0.2433 259 PHE A C   
3901  O O   . PHE A 250 ? 0.8659  0.9199  1.3683  0.0389  -0.2682 -0.2467 259 PHE A O   
3902  C CB  . PHE A 250 ? 1.0544  0.9821  1.5813  0.0286  -0.3119 -0.1905 259 PHE A CB  
3903  C CG  . PHE A 250 ? 0.7314  0.6048  1.2636  0.0256  -0.3342 -0.1671 259 PHE A CG  
3904  C CD1 . PHE A 250 ? 0.8930  0.7391  1.4254  0.0272  -0.3411 -0.1492 259 PHE A CD1 
3905  C CD2 . PHE A 250 ? 0.7004  0.5556  1.2337  0.0183  -0.3497 -0.1591 259 PHE A CD2 
3906  C CE1 . PHE A 250 ? 0.8659  0.6724  1.3980  0.0200  -0.3647 -0.1218 259 PHE A CE1 
3907  C CE2 . PHE A 250 ? 0.6412  0.4526  1.1752  0.0116  -0.3732 -0.1329 259 PHE A CE2 
3908  C CZ  . PHE A 250 ? 0.8428  0.6324  1.3757  0.0121  -0.3813 -0.1139 259 PHE A CZ  
3918  N N   . ALA A 251 ? 0.8685  0.8885  1.3794  0.0494  -0.2675 -0.2337 260 ALA A N   
3919  C CA  . ALA A 251 ? 0.5600  0.6314  1.0460  0.0468  -0.2400 -0.2387 260 ALA A CA  
3920  C C   . ALA A 251 ? 0.5158  0.5925  0.9620  0.0314  -0.2174 -0.1983 260 ALA A C   
3921  O O   . ALA A 251 ? 0.7285  0.7673  1.1645  0.0255  -0.2147 -0.1620 260 ALA A O   
3922  C CB  . ALA A 251 ? 0.4332  0.5002  0.9256  0.0537  -0.2377 -0.2406 260 ALA A CB  
3928  N N   . GLY A 252 ? 0.4821  0.6086  0.9063  0.0238  -0.2013 -0.2051 261 GLY A N   
3929  C CA  . GLY A 252 ? 0.9266  1.0546  1.3166  0.0112  -0.1835 -0.1665 261 GLY A CA  
3930  C C   . GLY A 252 ? 1.1313  1.2358  1.5064  0.0107  -0.1711 -0.1445 261 GLY A C   
3931  O O   . GLY A 252 ? 0.9432  1.0476  1.3283  0.0168  -0.1729 -0.1610 261 GLY A O   
3935  N N   . GLY A 253 ? 0.7312  0.8154  1.0856  0.0039  -0.1598 -0.1082 262 GLY A N   
3936  C CA  . GLY A 253 ? 0.7353  0.7968  1.0707  0.0010  -0.1464 -0.0875 262 GLY A CA  
3937  C C   . GLY A 253 ? 0.4762  0.5711  0.7893  -0.0074 -0.1368 -0.0952 262 GLY A C   
3938  O O   . GLY A 253 ? 0.6553  0.7927  0.9556  -0.0171 -0.1355 -0.1024 262 GLY A O   
3942  N N   . SER A 254 ? 0.4256  0.5049  0.7314  -0.0081 -0.1307 -0.0923 263 SER A N   
3943  C CA  . SER A 254 ? 0.7402  0.8537  1.0252  -0.0191 -0.1223 -0.0989 263 SER A CA  
3944  C C   . SER A 254 ? 0.4318  0.5114  0.6971  -0.0247 -0.1129 -0.0780 263 SER A C   
3945  O O   . SER A 254 ? 0.5795  0.6159  0.8519  -0.0187 -0.1137 -0.0670 263 SER A O   
3946  C CB  . SER A 254 ? 0.4746  0.6292  0.7842  -0.0125 -0.1291 -0.1384 263 SER A CB  
3947  O OG  . SER A 254 ? 0.7189  0.8492  1.0394  -0.0064 -0.1317 -0.1390 263 SER A OG  
3953  N N   . ALA A 255 ? 0.6266  0.7283  0.8653  -0.0398 -0.1047 -0.0737 264 ALA A N   
3954  C CA  . ALA A 255 ? 0.8150  0.8824  1.0356  -0.0459 -0.0973 -0.0571 264 ALA A CA  
3955  C C   . ALA A 255 ? 0.7316  0.7889  0.9757  -0.0363 -0.1035 -0.0719 264 ALA A C   
3956  O O   . ALA A 255 ? 0.7330  0.7491  0.9670  -0.0392 -0.1001 -0.0557 264 ALA A O   
3957  C CB  . ALA A 255 ? 0.4924  0.5876  0.6812  -0.0669 -0.0905 -0.0515 264 ALA A CB  
3963  N N   . GLY A 256 ? 0.8800  0.9733  1.1575  -0.0251 -0.1149 -0.1031 265 GLY A N   
3964  C CA  . GLY A 256 ? 0.5893  0.6732  0.8957  -0.0151 -0.1277 -0.1165 265 GLY A CA  
3965  C C   . GLY A 256 ? 0.5946  0.6198  0.9093  -0.0104 -0.1374 -0.0982 265 GLY A C   
3966  O O   . GLY A 256 ? 0.6307  0.6350  0.9541  -0.0112 -0.1473 -0.0943 265 GLY A O   
3970  N N   . GLN A 257 ? 0.7299  0.7307  1.0371  -0.0103 -0.1336 -0.0827 266 GLN A N   
3971  C CA  . GLN A 257 ? 0.6485  0.6024  0.9573  -0.0125 -0.1387 -0.0636 266 GLN A CA  
3972  C C   . GLN A 257 ? 0.7224  0.6466  0.9974  -0.0266 -0.1220 -0.0392 266 GLN A C   
3973  O O   . GLN A 257 ? 0.7020  0.5944  0.9746  -0.0337 -0.1246 -0.0256 266 GLN A O   
3974  C CB  . GLN A 257 ? 0.7072  0.6568  1.0239  -0.0081 -0.1394 -0.0592 266 GLN A CB  
3975  C CG  . GLN A 257 ? 0.9350  0.9071  1.2830  0.0035  -0.1569 -0.0842 266 GLN A CG  
3976  C CD  . GLN A 257 ? 0.8050  0.7823  1.1563  0.0052  -0.1562 -0.0805 266 GLN A CD  
3977  O OE1 . GLN A 257 ? 0.6048  0.5797  0.9360  -0.0001 -0.1408 -0.0609 266 GLN A OE1 
3978  N NE2 . GLN A 257 ? 0.8760  0.8574  1.2562  0.0129  -0.1757 -0.0994 266 GLN A NE2 
3987  N N   . SER A 258 ? 0.8185  0.7523  1.0661  -0.0338 -0.1064 -0.0341 267 SER A N   
3988  C CA  . SER A 258 ? 0.7902  0.6928  1.0067  -0.0470 -0.0923 -0.0161 267 SER A CA  
3989  C C   . SER A 258 ? 0.8325  0.7256  1.0470  -0.0560 -0.1000 -0.0161 267 SER A C   
3990  O O   . SER A 258 ? 1.0339  0.9544  1.2589  -0.0546 -0.1089 -0.0288 267 SER A O   
3991  C CB  . SER A 258 ? 0.9168  0.8280  1.1055  -0.0545 -0.0799 -0.0105 267 SER A CB  
3992  O OG  . SER A 258 ? 0.6479  0.5291  0.8064  -0.0686 -0.0691 0.0016  267 SER A OG  
3998  N N   . SER A 259 ? 0.6568  0.5164  0.8592  -0.0670 -0.0975 -0.0026 268 SER A N   
3999  C CA  . SER A 259 ? 0.7027  0.5535  0.8985  -0.0801 -0.1071 0.0016  268 SER A CA  
4000  C C   . SER A 259 ? 0.7381  0.5997  0.9097  -0.0888 -0.0970 0.0010  268 SER A C   
4001  O O   . SER A 259 ? 1.0364  0.9219  1.2201  -0.0891 -0.1090 -0.0070 268 SER A O   
4002  C CB  . SER A 259 ? 1.5360  1.3535  1.7102  -0.0988 -0.1015 0.0177  268 SER A CB  
4003  O OG  . SER A 259 ? 0.8324  0.6427  1.0246  -0.0970 -0.1106 0.0213  268 SER A OG  
4009  N N   . VAL A 260 ? 0.8164  0.6641  0.9585  -0.0943 -0.0769 0.0079  269 VAL A N   
4010  C CA  . VAL A 260 ? 0.9936  0.8411  1.1052  -0.1077 -0.0673 0.0118  269 VAL A CA  
4011  C C   . VAL A 260 ? 0.8424  0.7372  0.9663  -0.1043 -0.0750 0.0003  269 VAL A C   
4012  O O   . VAL A 260 ? 0.9109  0.8204  1.0183  -0.1184 -0.0742 0.0011  269 VAL A O   
4013  C CB  . VAL A 260 ? 0.8199  0.6377  0.9080  -0.1091 -0.0502 0.0199  269 VAL A CB  
4014  C CG1 . VAL A 260 ? 0.9914  0.8186  1.0596  -0.1160 -0.0476 0.0237  269 VAL A CG1 
4015  C CG2 . VAL A 260 ? 0.8866  0.6652  0.9472  -0.1242 -0.0383 0.0258  269 VAL A CG2 
4025  N N   . PHE A 261 ? 0.6302  0.5545  0.7822  -0.0882 -0.0815 -0.0122 270 PHE A N   
4026  C CA  . PHE A 261 ? 0.6568  0.6370  0.8226  -0.0865 -0.0868 -0.0294 270 PHE A CA  
4027  C C   . PHE A 261 ? 0.8744  0.8820  1.0722  -0.0811 -0.1024 -0.0461 270 PHE A C   
4028  O O   . PHE A 261 ? 1.0875  1.1503  1.3022  -0.0797 -0.1057 -0.0660 270 PHE A O   
4029  C CB  . PHE A 261 ? 0.7048  0.7085  0.8900  -0.0726 -0.0890 -0.0406 270 PHE A CB  
4030  C CG  . PHE A 261 ? 0.7469  0.8164  0.9425  -0.0741 -0.0908 -0.0622 270 PHE A CG  
4031  C CD1 . PHE A 261 ? 0.8825  0.9936  1.1193  -0.0604 -0.1028 -0.0918 270 PHE A CD1 
4032  C CD2 . PHE A 261 ? 1.0490  1.1406  1.2146  -0.0904 -0.0822 -0.0539 270 PHE A CD2 
4033  C CE1 . PHE A 261 ? 0.9850  1.1674  1.2332  -0.0627 -0.1012 -0.1185 270 PHE A CE1 
4034  C CE2 . PHE A 261 ? 1.1821  1.3443  1.3528  -0.0981 -0.0821 -0.0748 270 PHE A CE2 
4035  C CZ  . PHE A 261 ? 0.9780  1.1893  1.1903  -0.0837 -0.0892 -0.1098 270 PHE A CZ  
4045  N N   . GLN A 262 ? 0.7033  0.6770  0.9135  -0.0783 -0.1140 -0.0392 271 GLN A N   
4046  C CA  . GLN A 262 ? 0.6977  0.6845  0.9433  -0.0721 -0.1362 -0.0495 271 GLN A CA  
4047  C C   . GLN A 262 ? 0.8385  0.7968  1.0609  -0.0919 -0.1391 -0.0295 271 GLN A C   
4048  O O   . GLN A 262 ? 1.0027  0.9859  1.2423  -0.0942 -0.1520 -0.0355 271 GLN A O   
4049  C CB  . GLN A 262 ? 0.9564  0.9237  1.2400  -0.0547 -0.1568 -0.0553 271 GLN A CB  
4050  C CG  . GLN A 262 ? 0.9789  0.9768  1.2920  -0.0343 -0.1588 -0.0801 271 GLN A CG  
4051  C CD  . GLN A 262 ? 0.7506  0.7430  1.1175  -0.0142 -0.1892 -0.0977 271 GLN A CD  
4052  O OE1 . GLN A 262 ? 0.7628  0.7402  1.1560  -0.0120 -0.2142 -0.0960 271 GLN A OE1 
4053  N NE2 . GLN A 262 ? 0.7461  0.7518  1.1306  -0.0003 -0.1898 -0.1153 271 GLN A NE2 
4062  N N   . CYS A 263 ? 0.7137  0.6253  0.8970  -0.1078 -0.1263 -0.0078 272 CYS A N   
4063  C CA  . CYS A 263 ? 2.0417  1.9260  2.2066  -0.1281 -0.1335 0.0093  272 CYS A CA  
4064  C C   . CYS A 263 ? 0.8990  0.8023  1.0444  -0.1442 -0.1297 0.0112  272 CYS A C   
4065  O O   . CYS A 263 ? 1.7927  1.6917  1.9386  -0.1575 -0.1449 0.0204  272 CYS A O   
4066  C CB  . CYS A 263 ? 2.5815  2.4213  2.7071  -0.1435 -0.1157 0.0253  272 CYS A CB  
4067  S SG  . CYS A 263 ? 3.0207  2.8515  3.1040  -0.1511 -0.0859 0.0259  272 CYS A SG  
4073  N N   . PHE A 264 ? 1.2182  1.1442  1.3465  -0.1461 -0.1130 0.0047  273 PHE A N   
4074  C CA  . PHE A 264 ? 0.8349  0.7763  0.9383  -0.1671 -0.1091 0.0096  273 PHE A CA  
4075  C C   . PHE A 264 ? 0.5932  0.5973  0.7376  -0.1589 -0.1247 -0.0079 273 PHE A C   
4076  O O   . PHE A 264 ? 0.6575  0.6760  0.7994  -0.1739 -0.1332 -0.0028 273 PHE A O   
4077  C CB  . PHE A 264 ? 1.6015  1.5331  1.6615  -0.1804 -0.0871 0.0154  273 PHE A CB  
4078  C CG  . PHE A 264 ? 0.9917  0.8617  1.0147  -0.1893 -0.0727 0.0290  273 PHE A CG  
4079  C CD1 . PHE A 264 ? 0.8234  0.6596  0.8156  -0.2112 -0.0703 0.0400  273 PHE A CD1 
4080  C CD2 . PHE A 264 ? 0.8904  0.7398  0.9142  -0.1751 -0.0627 0.0281  273 PHE A CD2 
4081  C CE1 . PHE A 264 ? 1.0152  0.8005  0.9775  -0.2183 -0.0548 0.0451  273 PHE A CE1 
4082  C CE2 . PHE A 264 ? 0.9997  0.7985  0.9993  -0.1794 -0.0492 0.0348  273 PHE A CE2 
4083  C CZ  . PHE A 264 ? 0.9111  0.6793  0.8806  -0.2004 -0.0439 0.0408  273 PHE A CZ  
4093  N N   . ASP A 265 ? 0.5636  0.6089  0.7479  -0.1356 -0.1287 -0.0308 274 ASP A N   
4094  C CA  . ASP A 265 ? 0.7075  0.8180  0.9434  -0.1221 -0.1444 -0.0562 274 ASP A CA  
4095  C C   . ASP A 265 ? 0.8122  0.9078  1.0850  -0.1148 -0.1731 -0.0528 274 ASP A C   
4096  O O   . ASP A 265 ? 0.9056  1.0392  1.2043  -0.1169 -0.1871 -0.0597 274 ASP A O   
4097  C CB  . ASP A 265 ? 0.5250  0.6728  0.7982  -0.0971 -0.1447 -0.0848 274 ASP A CB  
4098  C CG  . ASP A 265 ? 0.8613  1.0250  1.0980  -0.1078 -0.1213 -0.0842 274 ASP A CG  
4099  O OD1 . ASP A 265 ? 0.8692  1.0909  1.0966  -0.1223 -0.1120 -0.0938 274 ASP A OD1 
4100  O OD2 . ASP A 265 ? 1.5581  1.6787  1.7752  -0.1042 -0.1138 -0.0724 274 ASP A OD2 
4105  N N   . VAL A 266 ? 0.6306  0.6716  0.9054  -0.1090 -0.1841 -0.0397 275 VAL A N   
4106  C CA  . VAL A 266 ? 0.9297  0.9481  1.2368  -0.1060 -0.2171 -0.0305 275 VAL A CA  
4107  C C   . VAL A 266 ? 0.8664  0.8654  1.1371  -0.1366 -0.2198 -0.0040 275 VAL A C   
4108  O O   . VAL A 266 ? 0.8031  0.8179  1.1057  -0.1376 -0.2472 -0.0017 275 VAL A O   
4109  C CB  . VAL A 266 ? 0.7124  0.6793  1.0212  -0.0993 -0.2257 -0.0204 275 VAL A CB  
4110  C CG1 . VAL A 266 ? 0.8283  0.7540  1.1432  -0.1123 -0.2564 0.0040  275 VAL A CG1 
4111  C CG2 . VAL A 266 ? 1.1891  1.1824  1.5506  -0.0672 -0.2355 -0.0507 275 VAL A CG2 
4121  N N   . LEU A 267 ? 0.9479  0.9135  1.1541  -0.1615 -0.1930 0.0144  276 LEU A N   
4122  C CA  . LEU A 267 ? 0.6793  0.6256  0.8421  -0.1942 -0.1908 0.0364  276 LEU A CA  
4123  C C   . LEU A 267 ? 0.9084  0.9071  1.0844  -0.2001 -0.1960 0.0288  276 LEU A C   
4124  O O   . LEU A 267 ? 0.6795  0.6790  0.8543  -0.2180 -0.2138 0.0430  276 LEU A O   
4125  C CB  . LEU A 267 ? 0.9076  0.8177  1.0063  -0.2133 -0.1573 0.0457  276 LEU A CB  
4126  C CG  . LEU A 267 ? 0.8944  0.7872  0.9431  -0.2482 -0.1503 0.0621  276 LEU A CG  
4127  C CD1 . LEU A 267 ? 0.8530  0.7153  0.8921  -0.2681 -0.1690 0.0818  276 LEU A CD1 
4128  C CD2 . LEU A 267 ? 0.6200  0.4809  0.6148  -0.2612 -0.1187 0.0633  276 LEU A CD2 
4140  N N   . LEU A 268 ? 0.5078  0.5528  0.6900  -0.1909 -0.1792 0.0088  277 LEU A N   
4141  C CA  . LEU A 268 ? 0.8389  0.9424  1.0282  -0.2018 -0.1795 0.0010  277 LEU A CA  
4142  C C   . LEU A 268 ? 0.7763  0.9422  1.0440  -0.1766 -0.2069 -0.0228 277 LEU A C   
4143  O O   . LEU A 268 ? 1.0544  1.2842  1.3390  -0.1824 -0.2069 -0.0352 277 LEU A O   
4144  C CB  . LEU A 268 ? 0.8436  0.9745  1.0024  -0.2092 -0.1513 -0.0083 277 LEU A CB  
4145  C CG  . LEU A 268 ? 0.7109  0.7764  0.7970  -0.2340 -0.1290 0.0148  277 LEU A CG  
4146  C CD1 . LEU A 268 ? 1.1061  1.1857  1.1655  -0.2392 -0.1081 0.0102  277 LEU A CD1 
4147  C CD2 . LEU A 268 ? 0.5530  0.5976  0.5964  -0.2686 -0.1296 0.0350  277 LEU A CD2 
4159  N N   . GLY A 269 ? 0.6745  0.8237  0.9924  -0.1494 -0.2312 -0.0307 278 GLY A N   
4160  C CA  . GLY A 269 ? 0.5685  0.7655  0.9693  -0.1211 -0.2632 -0.0552 278 GLY A CA  
4161  C C   . GLY A 269 ? 0.7070  0.9819  1.1532  -0.0958 -0.2522 -0.0993 278 GLY A C   
4162  O O   . GLY A 269 ? 1.5893  1.9322  2.0980  -0.0796 -0.2682 -0.1266 278 GLY A O   
4166  N N   . ILE A 270 ? 0.4461  0.7168  0.8638  -0.0930 -0.2257 -0.1081 279 ILE A N   
4167  C CA  . ILE A 270 ? 0.5742  0.9178  1.0262  -0.0735 -0.2132 -0.1499 279 ILE A CA  
4168  C C   . ILE A 270 ? 1.5162  1.8467  2.0284  -0.0361 -0.2348 -0.1751 279 ILE A C   
4169  O O   . ILE A 270 ? 1.4072  1.6770  1.8960  -0.0332 -0.2323 -0.1609 279 ILE A O   
4170  C CB  . ILE A 270 ? 0.4665  0.8095  0.8523  -0.0949 -0.1775 -0.1415 279 ILE A CB  
4171  C CG1 . ILE A 270 ? 0.9349  1.2769  1.2590  -0.1343 -0.1612 -0.1134 279 ILE A CG1 
4172  C CG2 . ILE A 270 ? 0.5712  0.9909  0.9842  -0.0813 -0.1645 -0.1822 279 ILE A CG2 
4173  C CD1 . ILE A 270 ? 0.6346  0.9529  0.8886  -0.1589 -0.1334 -0.0951 279 ILE A CD1 
4185  N N   . GLN A 271 ? 1.6951  2.0858  2.2877  -0.0072 -0.2558 -0.2157 280 GLN A N   
4186  C CA  . GLN A 271 ? 1.2837  1.6454  1.9289  0.0297  -0.2787 -0.2371 280 GLN A CA  
4187  C C   . GLN A 271 ? 0.8528  1.2385  1.4964  0.0426  -0.2577 -0.2686 280 GLN A C   
4188  O O   . GLN A 271 ? 0.8270  1.2604  1.5058  0.0670  -0.2515 -0.3123 280 GLN A O   
4189  C CB  . GLN A 271 ? 1.2520  1.6438  1.9555  0.0568  -0.2964 -0.2629 280 GLN A CB  
4190  C CG  . GLN A 271 ? 1.3224  1.6908  2.0288  0.0439  -0.3203 -0.2299 280 GLN A CG  
4191  C CD  . GLN A 271 ? 1.4062  1.6763  2.0942  0.0352  -0.3479 -0.1871 280 GLN A CD  
4192  O OE1 . GLN A 271 ? 2.2339  2.4524  2.9279  0.0499  -0.3572 -0.1892 280 GLN A OE1 
4193  N NE2 . GLN A 271 ? 1.4941  1.7387  2.1544  0.0069  -0.3603 -0.1471 280 GLN A NE2 
4202  N N   . GLN A 272 ? 0.6030  0.9432  1.1944  0.0250  -0.2438 -0.2429 281 GLN A N   
4203  C CA  . GLN A 272 ? 0.9585  1.3144  1.5396  0.0320  -0.2249 -0.2644 281 GLN A CA  
4204  C C   . GLN A 272 ? 1.2350  1.5632  1.8681  0.0652  -0.2488 -0.2896 281 GLN A C   
4205  O O   . GLN A 272 ? 1.2269  1.5893  1.8693  0.0782  -0.2361 -0.3241 281 GLN A O   
4206  C CB  . GLN A 272 ? 0.9251  1.2206  1.4280  0.0071  -0.2025 -0.2221 281 GLN A CB  
4207  C CG  . GLN A 272 ? 1.1299  1.4353  1.5664  -0.0276 -0.1752 -0.1943 281 GLN A CG  
4208  C CD  . GLN A 272 ? 1.4606  1.8452  1.8810  -0.0399 -0.1505 -0.2168 281 GLN A CD  
4209  O OE1 . GLN A 272 ? 1.3504  1.8031  1.8154  -0.0230 -0.1516 -0.2607 281 GLN A OE1 
4210  N NE2 . GLN A 272 ? 1.5506  1.9261  1.9060  -0.0716 -0.1294 -0.1874 281 GLN A NE2 
4219  N N   . THR A 273 ? 1.2504  1.5060  1.9013  0.0744  -0.2799 -0.2674 282 THR A N   
4220  C CA  . THR A 273 ? 1.4965  1.7022  2.1796  0.0997  -0.3026 -0.2813 282 THR A CA  
4221  C C   . THR A 273 ? 1.1520  1.3607  1.8912  0.1270  -0.3257 -0.3131 282 THR A C   
4222  O O   . THR A 273 ? 0.9921  1.1596  1.7617  0.1467  -0.3471 -0.3332 282 THR A O   
4223  C CB  . THR A 273 ? 1.6166  1.7349  2.2773  0.0851  -0.3242 -0.2334 282 THR A CB  
4224  O OG1 . THR A 273 ? 1.2356  1.3387  1.8732  0.0612  -0.3304 -0.1956 282 THR A OG1 
4225  C CG2 . THR A 273 ? 1.3056  1.4151  1.9269  0.0693  -0.3048 -0.2195 282 THR A CG2 
4233  N N   . ALA A 274 ? 1.6465  1.9025  2.4009  0.1266  -0.3235 -0.3199 283 ALA A N   
4234  C CA  . ALA A 274 ? 1.9910  2.2581  2.8027  0.1522  -0.3449 -0.3531 283 ALA A CA  
4235  C C   . ALA A 274 ? 1.5372  1.8943  2.3722  0.1679  -0.3200 -0.4139 283 ALA A C   
4236  O O   . ALA A 274 ? 1.3614  1.7817  2.1629  0.1529  -0.2849 -0.4228 283 ALA A O   
4237  C CB  . ALA A 274 ? 1.6930  1.9627  2.5112  0.1419  -0.3595 -0.3246 283 ALA A CB  
4243  N N   . GLY A 275 ? 1.1499  1.5144  2.0421  0.1947  -0.3401 -0.4565 284 GLY A N   
4244  C CA  . GLY A 275 ? 1.6093  2.0597  2.5269  0.2090  -0.3197 -0.5198 284 GLY A CA  
4245  C C   . GLY A 275 ? 1.4466  1.8887  2.3705  0.2212  -0.3181 -0.5607 284 GLY A C   
4246  O O   . GLY A 275 ? 1.4441  1.9274  2.4098  0.2405  -0.3216 -0.6219 284 GLY A O   
4250  N N   . GLY A 276 ? 1.4741  1.8668  2.3584  0.2085  -0.3141 -0.5292 285 GLY A N   
4251  C CA  . GLY A 276 ? 1.4139  1.7814  2.3031  0.2172  -0.3199 -0.5570 285 GLY A CA  
4252  C C   . GLY A 276 ? 1.2189  1.6634  2.0834  0.2104  -0.2835 -0.5931 285 GLY A C   
4253  O O   . GLY A 276 ? 1.0010  1.4343  1.8781  0.2192  -0.2915 -0.6260 285 GLY A O   
4257  N N   . GLY A 277 ? 1.2859  1.8068  2.1127  0.1899  -0.2467 -0.5849 286 GLY A N   
4258  C CA  . GLY A 277 ? 1.0950  1.6945  1.8957  0.1779  -0.2141 -0.6185 286 GLY A CA  
4259  C C   . GLY A 277 ? 0.9793  1.5362  1.7515  0.1704  -0.2127 -0.5979 286 GLY A C   
4260  O O   . GLY A 277 ? 0.9044  1.3791  1.6658  0.1684  -0.2303 -0.5497 286 GLY A O   
4264  N N   . HIS A 278 ? 1.2781  1.1663  1.4869  0.0573  -0.1490 -0.2792 287 HIS A N   
4265  C CA  . HIS A 278 ? 1.1086  0.9610  1.2852  0.0331  -0.1562 -0.2531 287 HIS A CA  
4266  C C   . HIS A 278 ? 1.0820  0.9470  1.2574  0.0119  -0.1486 -0.2143 287 HIS A C   
4267  O O   . HIS A 278 ? 0.9909  0.8236  1.1583  0.0002  -0.1643 -0.1847 287 HIS A O   
4268  C CB  . HIS A 278 ? 1.0758  0.9373  1.2239  0.0204  -0.1404 -0.2702 287 HIS A CB  
4269  C CG  . HIS A 278 ? 0.8364  0.6647  0.9541  -0.0048 -0.1497 -0.2434 287 HIS A CG  
4274  N N   . ALA A 279 ? 1.0060  0.9186  1.1916  0.0078  -0.1252 -0.2149 288 ALA A N   
4275  C CA  . ALA A 279 ? 0.9429  0.8659  1.1274  -0.0091 -0.1182 -0.1820 288 ALA A CA  
4276  C C   . ALA A 279 ? 1.1432  1.0499  1.3445  -0.0001 -0.1350 -0.1644 288 ALA A C   
4277  O O   . ALA A 279 ? 0.7428  0.6401  0.9381  -0.0138 -0.1374 -0.1340 288 ALA A O   
4278  C CB  . ALA A 279 ? 1.0056  0.9784  1.1957  -0.0154 -0.0919 -0.1891 288 ALA A CB  
4284  N N   . ALA A 280 ? 1.6575  1.5621  1.8796  0.0229  -0.1469 -0.1833 289 ALA A N   
4285  C CA  . ALA A 280 ? 1.3097  1.1985  1.5428  0.0288  -0.1635 -0.1641 289 ALA A CA  
4286  C C   . ALA A 280 ? 1.1156  0.9517  1.3315  0.0202  -0.1868 -0.1402 289 ALA A C   
4287  O O   . ALA A 280 ? 0.9850  0.8117  1.1950  0.0081  -0.1908 -0.1105 289 ALA A O   
4288  C CB  . ALA A 280 ? 1.2961  1.1932  1.5569  0.0563  -0.1750 -0.1887 289 ALA A CB  
4294  N N   . GLN A 281 ? 0.8786  0.6809  1.0840  0.0238  -0.2009 -0.1528 290 GLN A N   
4295  C CA  . GLN A 281 ? 0.9062  0.6566  1.0956  0.0131  -0.2254 -0.1299 290 GLN A CA  
4296  C C   . GLN A 281 ? 1.4398  1.1972  1.6140  -0.0154 -0.2139 -0.1001 290 GLN A C   
4297  O O   . GLN A 281 ? 0.9799  0.7227  1.1495  -0.0292 -0.2220 -0.0701 290 GLN A O   
4298  C CB  . GLN A 281 ? 0.7807  0.4904  0.9610  0.0231  -0.2448 -0.1525 290 GLN A CB  
4299  C CG  . GLN A 281 ? 1.0282  0.6748  1.1943  0.0154  -0.2778 -0.1319 290 GLN A CG  
4300  C CD  . GLN A 281 ? 1.0517  0.6745  1.2276  0.0280  -0.2997 -0.1216 290 GLN A CD  
4307  N N   . PHE A 282 ? 1.7567  1.5427  1.9247  -0.0244 -0.1930 -0.1079 291 PHE A N   
4308  C CA  . PHE A 282 ? 0.8637  0.6554  1.0202  -0.0487 -0.1853 -0.0820 291 PHE A CA  
4309  C C   . PHE A 282 ? 0.8857  0.6977  1.0501  -0.0575 -0.1757 -0.0543 291 PHE A C   
4310  O O   . PHE A 282 ? 0.9617  0.7703  1.1220  -0.0752 -0.1769 -0.0286 291 PHE A O   
4311  C CB  . PHE A 282 ? 0.8122  0.6310  0.9593  -0.0550 -0.1657 -0.0957 291 PHE A CB  
4312  C CG  . PHE A 282 ? 0.9024  0.7285  1.0409  -0.0764 -0.1599 -0.0716 291 PHE A CG  
4313  C CD1 . PHE A 282 ? 0.8948  0.6946  1.0203  -0.0902 -0.1747 -0.0632 291 PHE A CD1 
4314  C CD2 . PHE A 282 ? 0.9772  0.8353  1.1226  -0.0825 -0.1421 -0.0563 291 PHE A CD2 
4315  C CE1 . PHE A 282 ? 0.7970  0.6070  0.9200  -0.1094 -0.1718 -0.0400 291 PHE A CE1 
4316  C CE2 . PHE A 282 ? 0.7321  0.5974  0.8738  -0.0995 -0.1388 -0.0345 291 PHE A CE2 
4317  C CZ  . PHE A 282 ? 0.8100  0.6533  0.9428  -0.1126 -0.1539 -0.0257 291 PHE A CZ  
4327  N N   . LEU A 283 ? 0.8648  0.7033  1.0411  -0.0462 -0.1640 -0.0609 292 LEU A N   
4328  C CA  . LEU A 283 ? 0.7941  0.6472  0.9741  -0.0530 -0.1564 -0.0374 292 LEU A CA  
4329  C C   . LEU A 283 ? 0.8544  0.6775  1.0321  -0.0539 -0.1762 -0.0193 292 LEU A C   
4330  O O   . LEU A 283 ? 0.8759  0.7040  1.0500  -0.0665 -0.1719 0.0054  292 LEU A O   
4331  C CB  . LEU A 283 ? 0.8026  0.6889  0.9934  -0.0422 -0.1411 -0.0499 292 LEU A CB  
4332  C CG  . LEU A 283 ? 1.0950  1.0134  1.2837  -0.0484 -0.1187 -0.0596 292 LEU A CG  
4333  C CD1 . LEU A 283 ? 1.3225  1.2709  1.5227  -0.0385 -0.1068 -0.0773 292 LEU A CD1 
4334  C CD2 . LEU A 283 ? 1.0947  1.0219  1.2764  -0.0645 -0.1080 -0.0357 292 LEU A CD2 
4346  N N   . GLN A 284 ? 1.0895  0.8821  1.2687  -0.0400 -0.1977 -0.0319 293 GLN A N   
4347  C CA  . GLN A 284 ? 1.0185  0.7750  1.1901  -0.0436 -0.2202 -0.0122 293 GLN A CA  
4348  C C   . GLN A 284 ? 1.6800  1.4109  1.8386  -0.0657 -0.2297 0.0095  293 GLN A C   
4349  O O   . GLN A 284 ? 0.6480  0.3707  0.7984  -0.0824 -0.2337 0.0374  293 GLN A O   
4350  C CB  . GLN A 284 ? 1.2085  0.9335  1.3855  -0.0214 -0.2448 -0.0319 293 GLN A CB  
4351  C CG  . GLN A 284 ? 1.4945  1.1774  1.6607  -0.0233 -0.2720 -0.0115 293 GLN A CG  
4352  C CD  . GLN A 284 ? 1.5385  1.2429  1.7041  -0.0246 -0.2644 0.0036  293 GLN A CD  
4353  O OE1 . GLN A 284 ? 1.9126  1.6461  2.0939  -0.0076 -0.2560 -0.0140 293 GLN A OE1 
4354  N NE2 . GLN A 284 ? 1.0356  0.7253  1.1820  -0.0459 -0.2683 0.0356  293 GLN A NE2 
4363  N N   . ASP A 285 ? 0.9091  0.6304  1.0651  -0.0682 -0.2325 -0.0031 294 ASP A N   
4364  C CA  . ASP A 285 ? 0.9648  0.6620  1.1105  -0.0903 -0.2445 0.0166  294 ASP A CA  
4365  C C   . ASP A 285 ? 0.8999  0.6330  1.0498  -0.1106 -0.2249 0.0418  294 ASP A C   
4366  O O   . ASP A 285 ? 1.1223  0.8479  1.2688  -0.1289 -0.2309 0.0684  294 ASP A O   
4367  C CB  . ASP A 285 ? 0.8562  0.5359  0.9957  -0.0885 -0.2520 -0.0044 294 ASP A CB  
4368  C CG  . ASP A 285 ? 1.0832  0.7232  1.2191  -0.0673 -0.2737 -0.0303 294 ASP A CG  
4369  O OD1 . ASP A 285 ? 1.2315  0.8477  1.3691  -0.0577 -0.2899 -0.0258 294 ASP A OD1 
4370  O OD2 . ASP A 285 ? 2.2673  1.8983  2.3977  -0.0597 -0.2757 -0.0556 294 ASP A OD2 
4375  N N   . MET A 286 ? 0.9968  0.7709  1.1547  -0.1067 -0.2008 0.0339  295 MET A N   
4376  C CA  . MET A 286 ? 1.0629  0.8682  1.2271  -0.1229 -0.1850 0.0557  295 MET A CA  
4377  C C   . MET A 286 ? 0.5881  0.4048  0.7536  -0.1272 -0.1785 0.0757  295 MET A C   
4378  O O   . MET A 286 ? 0.5733  0.4139  0.7452  -0.1413 -0.1672 0.0950  295 MET A O   
4379  C CB  . MET A 286 ? 0.5589  0.3998  0.7287  -0.1173 -0.1632 0.0444  295 MET A CB  
4380  C CG  . MET A 286 ? 0.9278  0.7647  1.0918  -0.1191 -0.1654 0.0294  295 MET A CG  
4381  S SD  . MET A 286 ? 1.0267  0.8497  1.1903  -0.1415 -0.1809 0.0482  295 MET A SD  
4382  C CE  . MET A 286 ? 1.4790  1.2486  1.6285  -0.1395 -0.2090 0.0359  295 MET A CE  
4392  N N   . ARG A 287 ? 0.6682  0.4697  0.8277  -0.1160 -0.1857 0.0717  296 ARG A N   
4393  C CA  . ARG A 287 ? 0.6072  0.4155  0.7610  -0.1242 -0.1813 0.0929  296 ARG A CA  
4394  C C   . ARG A 287 ? 1.0655  0.8567  1.2128  -0.1482 -0.1930 0.1189  296 ARG A C   
4395  O O   . ARG A 287 ? 0.8598  0.6713  1.0053  -0.1624 -0.1815 0.1393  296 ARG A O   
4396  C CB  . ARG A 287 ? 0.6325  0.4206  0.7776  -0.1090 -0.1934 0.0858  296 ARG A CB  
4397  C CG  . ARG A 287 ? 0.6976  0.5090  0.8518  -0.0885 -0.1813 0.0630  296 ARG A CG  
4398  C CD  . ARG A 287 ? 0.8408  0.6453  0.9874  -0.0798 -0.1887 0.0653  296 ARG A CD  
4399  N NE  . ARG A 287 ? 0.9131  0.7410  1.0730  -0.0609 -0.1797 0.0408  296 ARG A NE  
4400  C CZ  . ARG A 287 ? 0.9396  0.7641  1.1016  -0.0468 -0.1898 0.0320  296 ARG A CZ  
4401  N NH1 . ARG A 287 ? 1.1147  0.9083  1.2626  -0.0482 -0.2112 0.0464  296 ARG A NH1 
4402  N NH2 . ARG A 287 ? 1.0875  0.9390  1.2661  -0.0322 -0.1804 0.0087  296 ARG A NH2 
4416  N N   . ARG A 288 ? 0.9259  0.6803  1.0687  -0.1542 -0.2157 0.1177  297 ARG A N   
4417  C CA  . ARG A 288 ? 1.0307  0.7650  1.1661  -0.1807 -0.2299 0.1437  297 ARG A CA  
4418  C C   . ARG A 288 ? 1.4895  1.2617  1.6410  -0.1994 -0.2147 0.1570  297 ARG A C   
4419  O O   . ARG A 288 ? 1.7961  1.5688  1.9471  -0.2246 -0.2193 0.1812  297 ARG A O   
4420  C CB  . ARG A 288 ? 1.2790  0.9571  1.4034  -0.1820 -0.2615 0.1376  297 ARG A CB  
4421  C CG  . ARG A 288 ? 1.4941  1.1271  1.5978  -0.1958 -0.2857 0.1585  297 ARG A CG  
4422  C CD  . ARG A 288 ? 1.5685  1.1650  1.6612  -0.1712 -0.3036 0.1434  297 ARG A CD  
4423  N NE  . ARG A 288 ? 1.6004  1.1924  1.6774  -0.1759 -0.3053 0.1622  297 ARG A NE  
4424  C CZ  . ARG A 288 ? 1.7192  1.2954  1.7767  -0.2048 -0.3133 0.1942  297 ARG A CZ  
4425  N NH1 . ARG A 288 ? 2.2222  1.7940  2.2778  -0.2314 -0.3178 0.2110  297 ARG A NH1 
4426  N NH2 . ARG A 288 ? 1.0967  0.6663  1.1346  -0.2081 -0.3156 0.2091  297 ARG A NH2 
4440  N N   . TYR A 289 ? 0.9051  0.7107  1.0714  -0.1880 -0.1970 0.1423  298 TYR A N   
4441  C CA  . TYR A 289 ? 0.8926  0.7371  1.0781  -0.1996 -0.1834 0.1512  298 TYR A CA  
4442  C C   . TYR A 289 ? 1.0294  0.9197  1.2259  -0.1963 -0.1569 0.1580  298 TYR A C   
4443  O O   . TYR A 289 ? 0.5266  0.4518  0.7419  -0.1971 -0.1439 0.1590  298 TYR A O   
4444  C CB  . TYR A 289 ? 0.5697  0.4174  0.7604  -0.1892 -0.1831 0.1313  298 TYR A CB  
4445  C CG  . TYR A 289 ? 0.8358  0.6453  1.0174  -0.1957 -0.2072 0.1239  298 TYR A CG  
4446  C CD1 . TYR A 289 ? 0.8161  0.5784  0.9800  -0.1882 -0.2269 0.1123  298 TYR A CD1 
4447  C CD2 . TYR A 289 ? 0.9212  0.7407  1.1109  -0.2059 -0.2110 0.1245  298 TYR A CD2 
4448  C CE1 . TYR A 289 ? 1.0535  0.7792  1.2071  -0.1915 -0.2481 0.1015  298 TYR A CE1 
4449  C CE2 . TYR A 289 ? 1.0230  0.8063  1.2003  -0.2112 -0.2326 0.1151  298 TYR A CE2 
4450  C CZ  . TYR A 289 ? 0.7768  0.5127  0.9353  -0.2038 -0.2504 0.1027  298 TYR A CZ  
4451  O OH  . TYR A 289 ? 0.8406  0.5370  0.9845  -0.2080 -0.2726 0.0905  298 TYR A OH  
4461  N N   . MET A 290 ? 0.9404  0.8290  1.1247  -0.1891 -0.1502 0.1590  299 MET A N   
4462  C CA  . MET A 290 ? 0.8979  0.8257  1.0878  -0.1872 -0.1260 0.1652  299 MET A CA  
4463  C C   . MET A 290 ? 1.1362  1.0712  1.3199  -0.2085 -0.1237 0.1894  299 MET A C   
4464  O O   . MET A 290 ? 1.4456  1.3454  1.6123  -0.2222 -0.1431 0.2012  299 MET A O   
4465  C CB  . MET A 290 ? 0.7905  0.7140  0.9675  -0.1670 -0.1188 0.1500  299 MET A CB  
4466  C CG  . MET A 290 ? 0.9543  0.8799  1.1371  -0.1481 -0.1153 0.1265  299 MET A CG  
4467  S SD  . MET A 290 ? 0.7975  0.7166  0.9663  -0.1292 -0.1115 0.1113  299 MET A SD  
4468  C CE  . MET A 290 ? 0.7282  0.6497  0.9056  -0.1139 -0.1098 0.0844  299 MET A CE  
4478  N N   . PRO A 291 ? 0.8556  0.8341  1.0495  -0.2112 -0.1001 0.1963  300 PRO A N   
4479  C CA  . PRO A 291 ? 0.7994  0.7906  0.9837  -0.2322 -0.0932 0.2178  300 PRO A CA  
4480  C C   . PRO A 291 ? 0.7940  0.7424  0.9428  -0.2343 -0.1079 0.2227  300 PRO A C   
4481  O O   . PRO A 291 ? 0.8574  0.7866  0.9935  -0.2136 -0.1113 0.2067  300 PRO A O   
4482  C CB  . PRO A 291 ? 1.0743  1.1153  1.2697  -0.2233 -0.0629 0.2137  300 PRO A CB  
4483  C CG  . PRO A 291 ? 0.5015  0.5600  0.7224  -0.2052 -0.0573 0.1971  300 PRO A CG  
4484  C CD  . PRO A 291 ? 0.7584  0.7753  0.9712  -0.1948 -0.0784 0.1837  300 PRO A CD  
4492  N N   . PRO A 292 ? 0.9515  0.8852  1.0836  -0.2601 -0.1174 0.2455  301 PRO A N   
4493  C CA  . PRO A 292 ? 1.0690  0.9556  1.1648  -0.2619 -0.1361 0.2517  301 PRO A CA  
4494  C C   . PRO A 292 ? 0.6733  0.5714  0.7521  -0.2455 -0.1209 0.2425  301 PRO A C   
4495  O O   . PRO A 292 ? 1.0058  0.8753  1.0752  -0.2250 -0.1340 0.2274  301 PRO A O   
4496  C CB  . PRO A 292 ? 0.9026  0.7833  0.9827  -0.2980 -0.1421 0.2818  301 PRO A CB  
4497  C CG  . PRO A 292 ? 0.8877  0.8326  0.9951  -0.3102 -0.1131 0.2881  301 PRO A CG  
4498  C CD  . PRO A 292 ? 0.7446  0.7151  0.8879  -0.2882 -0.1046 0.2671  301 PRO A CD  
4506  N N   . ALA A 293 ? 0.7629  0.7074  0.8433  -0.2509 -0.0921 0.2469  302 ALA A N   
4507  C CA  . ALA A 293 ? 0.8849  0.8384  0.9456  -0.2364 -0.0778 0.2371  302 ALA A CA  
4508  C C   . ALA A 293 ? 0.9175  0.8663  0.9915  -0.2056 -0.0791 0.2102  302 ALA A C   
4509  O O   . ALA A 293 ? 0.8671  0.7987  0.9211  -0.1927 -0.0842 0.2012  302 ALA A O   
4510  C CB  . ALA A 293 ? 0.9180  0.9260  0.9843  -0.2415 -0.0440 0.2389  302 ALA A CB  
4516  N N   . HIS A 294 ? 0.8262  0.7892  0.9322  -0.1953 -0.0761 0.1978  303 HIS A N   
4517  C CA  . HIS A 294 ? 0.7304  0.6910  0.8444  -0.1700 -0.0751 0.1737  303 HIS A CA  
4518  C C   . HIS A 294 ? 0.7888  0.7075  0.8964  -0.1607 -0.1014 0.1649  303 HIS A C   
4519  O O   . HIS A 294 ? 0.8151  0.7279  0.9197  -0.1430 -0.1033 0.1482  303 HIS A O   
4520  C CB  . HIS A 294 ? 0.7389  0.7287  0.8839  -0.1622 -0.0620 0.1633  303 HIS A CB  
4521  C CG  . HIS A 294 ? 0.8573  0.8903  1.0127  -0.1644 -0.0362 0.1670  303 HIS A CG  
4522  N ND1 . HIS A 294 ? 0.5908  0.6533  0.7753  -0.1582 -0.0248 0.1611  303 HIS A ND1 
4523  C CD2 . HIS A 294 ? 0.7045  0.7560  0.8443  -0.1717 -0.0203 0.1753  303 HIS A CD2 
4524  C CE1 . HIS A 294 ? 0.5605  0.6586  0.7507  -0.1586 -0.0030 0.1638  303 HIS A CE1 
4525  N NE2 . HIS A 294 ? 0.5359  0.6296  0.6987  -0.1675 0.0016  0.1719  303 HIS A NE2 
4533  N N   . ARG A 295 ? 0.7337  0.6230  0.8400  -0.1724 -0.1228 0.1751  304 ARG A N   
4534  C CA  . ARG A 295 ? 0.7384  0.5857  0.8387  -0.1607 -0.1491 0.1646  304 ARG A CA  
4535  C C   . ARG A 295 ? 0.7220  0.5458  0.7957  -0.1582 -0.1612 0.1699  304 ARG A C   
4536  O O   . ARG A 295 ? 1.1524  0.9615  1.2266  -0.1386 -0.1730 0.1532  304 ARG A O   
4537  C CB  . ARG A 295 ? 1.0289  0.8467  1.1325  -0.1738 -0.1699 0.1732  304 ARG A CB  
4538  C CG  . ARG A 295 ? 1.1532  0.9216  1.2311  -0.1875 -0.1983 0.1914  304 ARG A CG  
4539  C CD  . ARG A 295 ? 1.0567  0.7925  1.1384  -0.1996 -0.2200 0.1967  304 ARG A CD  
4548  N N   . ASN A 296 ? 0.6631  0.4923  0.7147  -0.1772 -0.1542 0.1915  305 ASN A N   
4549  C CA  . ASN A 296 ? 0.8557  0.6602  0.8748  -0.1796 -0.1670 0.2009  305 ASN A CA  
4550  C C   . ASN A 296 ? 0.9675  0.7919  0.9850  -0.1608 -0.1546 0.1836  305 ASN A C   
4551  O O   . ASN A 296 ? 1.1072  0.9078  1.1058  -0.1533 -0.1719 0.1822  305 ASN A O   
4552  C CB  . ASN A 296 ? 1.1635  0.9749  1.1550  -0.2087 -0.1576 0.2286  305 ASN A CB  
4553  C CG  . ASN A 296 ? 1.3763  1.1644  1.3634  -0.2343 -0.1727 0.2508  305 ASN A CG  
4554  O OD1 . ASN A 296 ? 1.7486  1.5618  1.7305  -0.2592 -0.1562 0.2695  305 ASN A OD1 
4555  N ND2 . ASN A 296 ? 2.5332  2.2746  2.5228  -0.2286 -0.2040 0.2481  305 ASN A ND2 
4562  N N   . PHE A 297 ? 0.9025  0.7689  0.9375  -0.1551 -0.1264 0.1726  306 PHE A N   
4563  C CA  . PHE A 297 ? 0.9018  0.7855  0.9339  -0.1396 -0.1144 0.1563  306 PHE A CA  
4564  C C   . PHE A 297 ? 0.9698  0.8423  1.0198  -0.1180 -0.1291 0.1342  306 PHE A C   
4565  O O   . PHE A 297 ? 1.1511  1.0122  1.1902  -0.1084 -0.1412 0.1274  306 PHE A O   
4566  C CB  . PHE A 297 ? 0.7175  0.6430  0.7629  -0.1391 -0.0831 0.1508  306 PHE A CB  
4567  C CG  . PHE A 297 ? 0.6791  0.6181  0.7197  -0.1255 -0.0716 0.1348  306 PHE A CG  
4568  C CD1 . PHE A 297 ? 0.9910  0.9257  0.9991  -0.1295 -0.0697 0.1395  306 PHE A CD1 
4569  C CD2 . PHE A 297 ? 0.5655  0.5188  0.6299  -0.1109 -0.0640 0.1155  306 PHE A CD2 
4570  C CE1 . PHE A 297 ? 0.6988  0.6424  0.6998  -0.1175 -0.0614 0.1233  306 PHE A CE1 
4571  C CE2 . PHE A 297 ? 0.7467  0.7086  0.8046  -0.1003 -0.0556 0.1008  306 PHE A CE2 
4572  C CZ  . PHE A 297 ? 0.7035  0.6604  0.7305  -0.1035 -0.0546 0.1044  306 PHE A CZ  
4582  N N   . LEU A 298 ? 0.6840  0.5591  0.7609  -0.1114 -0.1305 0.1232  307 LEU A N   
4583  C CA  . LEU A 298 ? 0.8617  0.7301  0.9563  -0.0923 -0.1428 0.1010  307 LEU A CA  
4584  C C   . LEU A 298 ? 1.0881  0.9203  1.1731  -0.0858 -0.1733 0.1022  307 LEU A C   
4585  O O   . LEU A 298 ? 1.0237  0.8566  1.1153  -0.0700 -0.1826 0.0868  307 LEU A O   
4586  C CB  . LEU A 298 ? 0.7428  0.6145  0.8602  -0.0895 -0.1414 0.0910  307 LEU A CB  
4587  C CG  . LEU A 298 ? 0.7853  0.6904  0.9158  -0.0912 -0.1162 0.0854  307 LEU A CG  
4588  C CD1 . LEU A 298 ? 0.7519  0.6557  0.8995  -0.0900 -0.1186 0.0762  307 LEU A CD1 
4589  C CD2 . LEU A 298 ? 1.0094  0.9346  1.1435  -0.0799 -0.1044 0.0693  307 LEU A CD2 
4601  N N   . CYS A 299 ? 1.1008  0.9008  1.1712  -0.0983 -0.1909 0.1209  308 CYS A N   
4602  C CA  . CYS A 299 ? 1.2669  1.0253  1.3293  -0.0902 -0.2244 0.1215  308 CYS A CA  
4603  C C   . CYS A 299 ? 0.9816  0.7348  1.0221  -0.0880 -0.2327 0.1270  308 CYS A C   
4604  O O   . CYS A 299 ? 1.0140  0.7520  1.0610  -0.0704 -0.2553 0.1153  308 CYS A O   
4605  C CB  . CYS A 299 ? 1.4069  1.1276  1.4544  -0.1083 -0.2418 0.1430  308 CYS A CB  
4606  S SG  . CYS A 299 ? 2.2662  1.9271  2.3008  -0.0996 -0.2860 0.1464  308 CYS A SG  
4609  N N   . SER A 300 ? 1.2056  0.9735  1.2208  -0.1050 -0.2148 0.1434  309 SER A N   
4610  C CA  . SER A 300 ? 0.9516  0.7134  0.9392  -0.1058 -0.2219 0.1494  309 SER A CA  
4611  C C   . SER A 300 ? 1.0887  0.8801  1.0933  -0.0875 -0.2121 0.1257  309 SER A C   
4612  O O   . SER A 300 ? 1.1583  0.9429  1.1440  -0.0848 -0.2235 0.1265  309 SER A O   
4613  C CB  . SER A 300 ? 0.9878  0.7588  0.9403  -0.1307 -0.2025 0.1720  309 SER A CB  
4616  N N   . LEU A 301 ? 1.1272  0.9513  1.1628  -0.0786 -0.1907 0.1068  310 LEU A N   
4617  C CA  . LEU A 301 ? 1.0107  0.8594  1.0670  -0.0621 -0.1861 0.0831  310 LEU A CA  
4618  C C   . LEU A 301 ? 1.1325  0.9687  1.2121  -0.0429 -0.2137 0.0675  310 LEU A C   
4619  O O   . LEU A 301 ? 1.2815  1.1262  1.3664  -0.0327 -0.2235 0.0567  310 LEU A O   
4620  C CB  . LEU A 301 ? 0.7400  0.6221  0.8200  -0.0600 -0.1586 0.0688  310 LEU A CB  
4621  C CG  . LEU A 301 ? 0.8177  0.7227  0.8873  -0.0709 -0.1288 0.0742  310 LEU A CG  
4622  C CD1 . LEU A 301 ? 0.7650  0.6941  0.8609  -0.0658 -0.1113 0.0589  310 LEU A CD1 
4623  C CD2 . LEU A 301 ? 1.0026  0.9158  1.0497  -0.0728 -0.1208 0.0735  310 LEU A CD2 
4635  N N   . GLU A 302 ? 0.9242  0.7422  1.0202  -0.0368 -0.2269 0.0642  311 GLU A N   
4636  C CA  . GLU A 302 ? 0.8566  0.6624  0.9767  -0.0154 -0.2538 0.0468  311 GLU A CA  
4637  C C   . GLU A 302 ? 0.9111  0.6862  1.0116  -0.0123 -0.2851 0.0585  311 GLU A C   
4638  O O   . GLU A 302 ? 1.2067  0.9823  1.3300  0.0080  -0.3068 0.0421  311 GLU A O   
4639  C CB  . GLU A 302 ? 1.1648  0.9473  1.2986  -0.0096 -0.2652 0.0418  311 GLU A CB  
4640  C CG  . GLU A 302 ? 1.7761  1.5849  1.9275  -0.0122 -0.2391 0.0295  311 GLU A CG  
4647  N N   . SER A 303 ? 0.8020  0.5535  0.8608  -0.0326 -0.2873 0.0862  312 SER A N   
4648  C CA  . SER A 303 ? 1.0990  0.8145  1.1272  -0.0357 -0.3178 0.1032  312 SER A CA  
4649  C C   . SER A 303 ? 1.2004  0.9367  1.2207  -0.0324 -0.3170 0.0977  312 SER A C   
4650  O O   . SER A 303 ? 1.1710  0.8816  1.1769  -0.0272 -0.3488 0.1040  312 SER A O   
4651  C CB  . SER A 303 ? 1.1402  0.8275  1.1222  -0.0637 -0.3155 0.1355  312 SER A CB  
4652  O OG  . SER A 303 ? 1.4987  1.1540  1.4830  -0.0682 -0.3287 0.1443  312 SER A OG  
4658  N N   . ASN A 304 ? 1.0015  0.7778  1.0238  -0.0384 -0.2835 0.0897  313 ASN A N   
4659  C CA  . ASN A 304 ? 1.1156  0.9104  1.1303  -0.0364 -0.2827 0.0824  313 ASN A CA  
4660  C C   . ASN A 304 ? 0.9582  0.7776  1.0204  -0.0133 -0.2945 0.0551  313 ASN A C   
4661  O O   . ASN A 304 ? 1.8020  1.6380  1.9023  -0.0015 -0.2875 0.0382  313 ASN A O   
4662  C CB  . ASN A 304 ? 1.1481  0.9730  1.1489  -0.0495 -0.2450 0.0812  313 ASN A CB  
4663  C CG  . ASN A 304 ? 1.2683  1.0763  1.2188  -0.0720 -0.2335 0.1063  313 ASN A CG  
4664  O OD1 . ASN A 304 ? 1.5995  1.3825  1.5111  -0.0807 -0.2514 0.1214  313 ASN A OD1 
4665  N ND2 . ASN A 304 ? 0.9973  0.8210  0.9489  -0.0820 -0.2038 0.1106  313 ASN A ND2 
4672  N N   . PRO A 305 ? 1.0847  0.9097  1.1453  -0.0077 -0.3118 0.0499  314 PRO A N   
4673  C CA  . PRO A 305 ? 1.2880  1.1438  1.3991  0.0133  -0.3233 0.0233  314 PRO A CA  
4674  C C   . PRO A 305 ? 0.7625  0.6663  0.9033  0.0126  -0.2890 0.0027  314 PRO A C   
4675  O O   . PRO A 305 ? 1.1685  1.0822  1.2871  -0.0030 -0.2613 0.0078  314 PRO A O   
4676  C CB  . PRO A 305 ? 1.2418  1.0931  1.3376  0.0138  -0.3484 0.0265  314 PRO A CB  
4677  C CG  . PRO A 305 ? 1.2228  1.0509  1.2558  -0.0102 -0.3372 0.0505  314 PRO A CG  
4678  C CD  . PRO A 305 ? 1.1408  0.9455  1.1524  -0.0217 -0.3223 0.0679  314 PRO A CD  
4686  N N   . SER A 306 ? 1.2499  1.1828  1.4408  0.0301  -0.2924 -0.0214 315 SER A N   
4687  C CA  . SER A 306 ? 0.8775  0.8514  1.0966  0.0286  -0.2613 -0.0401 315 SER A CA  
4688  C C   . SER A 306 ? 1.1360  1.1403  1.3514  0.0164  -0.2438 -0.0458 315 SER A C   
4689  O O   . SER A 306 ? 1.3790  1.3964  1.6032  0.0196  -0.2605 -0.0519 315 SER A O   
4690  C CB  . SER A 306 ? 1.2193  1.2201  1.4912  0.0498  -0.2698 -0.0661 315 SER A CB  
4691  O OG  . SER A 306 ? 1.3991  1.4404  1.6941  0.0454  -0.2397 -0.0837 315 SER A OG  
4697  N N   . VAL A 307 ? 1.1834  1.1977  1.3867  0.0025  -0.2121 -0.0444 316 VAL A N   
4698  C CA  . VAL A 307 ? 0.9695  1.0095  1.1713  -0.0089 -0.1960 -0.0521 316 VAL A CA  
4699  C C   . VAL A 307 ? 0.8685  0.9538  1.1181  -0.0025 -0.1953 -0.0766 316 VAL A C   
4700  O O   . VAL A 307 ? 0.7732  0.8801  1.0322  -0.0066 -0.2012 -0.0846 316 VAL A O   
4701  C CB  . VAL A 307 ? 0.7471  0.7817  0.9243  -0.0235 -0.1656 -0.0442 316 VAL A CB  
4702  C CG1 . VAL A 307 ? 0.6031  0.6587  0.7789  -0.0351 -0.1501 -0.0532 316 VAL A CG1 
4703  C CG2 . VAL A 307 ? 1.5578  1.5584  1.6904  -0.0310 -0.1648 -0.0228 316 VAL A CG2 
4713  N N   . ARG A 308 ? 0.8514  0.9528  1.1323  0.0075  -0.1899 -0.0895 317 ARG A N   
4714  C CA  . ARG A 308 ? 0.7034  0.8543  1.0307  0.0127  -0.1857 -0.1144 317 ARG A CA  
4715  C C   . ARG A 308 ? 1.0600  1.2282  1.4171  0.0270  -0.2152 -0.1245 317 ARG A C   
4716  O O   . ARG A 308 ? 0.6420  0.8479  1.0209  0.0207  -0.2149 -0.1361 317 ARG A O   
4717  C CB  . ARG A 308 ? 0.6793  0.8406  1.0294  0.0224  -0.1751 -0.1275 317 ARG A CB  
4718  C CG  . ARG A 308 ? 0.9223  1.1390  1.3148  0.0235  -0.1613 -0.1538 317 ARG A CG  
4719  C CD  . ARG A 308 ? 0.8156  1.0410  1.2207  0.0295  -0.1458 -0.1675 317 ARG A CD  
4720  N NE  . ARG A 308 ? 0.5104  0.7856  0.9347  0.0164  -0.1201 -0.1853 317 ARG A NE  
4721  C CZ  . ARG A 308 ? 1.2323  1.5602  1.7021  0.0252  -0.1179 -0.2120 317 ARG A CZ  
4722  N NH1 . ARG A 308 ? 1.9631  2.3003  2.4682  0.0513  -0.1417 -0.2260 317 ARG A NH1 
4723  N NH2 . ARG A 308 ? 0.9152  1.2877  1.3956  0.0074  -0.0922 -0.2248 317 ARG A NH2 
4737  N N   . GLU A 309 ? 0.7518  0.8902  1.1085  0.0447  -0.2438 -0.1183 318 GLU A N   
4738  C CA  . GLU A 309 ? 0.7058  0.8591  1.0940  0.0612  -0.2760 -0.1282 318 GLU A CA  
4739  C C   . GLU A 309 ? 1.0382  1.1925  1.4064  0.0474  -0.2856 -0.1191 318 GLU A C   
4740  O O   . GLU A 309 ? 0.8992  1.0889  1.3021  0.0527  -0.3014 -0.1328 318 GLU A O   
4741  C CB  . GLU A 309 ? 0.6160  0.7253  0.9982  0.0807  -0.3097 -0.1189 318 GLU A CB  
4742  C CG  . GLU A 309 ? 0.9913  1.1098  1.4157  0.1056  -0.3161 -0.1395 318 GLU A CG  
4749  N N   . PHE A 310 ? 0.6260  0.7437  0.9394  0.0297  -0.2765 -0.0975 319 PHE A N   
4750  C CA  . PHE A 310 ? 0.6581  0.7723  0.9465  0.0164  -0.2854 -0.0905 319 PHE A CA  
4751  C C   . PHE A 310 ? 0.8120  0.9719  1.1229  0.0028  -0.2669 -0.1063 319 PHE A C   
4752  O O   . PHE A 310 ? 0.6302  0.8109  0.9543  -0.0008 -0.2836 -0.1129 319 PHE A O   
4753  C CB  . PHE A 310 ? 0.6842  0.7523  0.9086  0.0012  -0.2748 -0.0672 319 PHE A CB  
4754  C CG  . PHE A 310 ? 0.9685  1.0254  1.1572  -0.0124 -0.2836 -0.0602 319 PHE A CG  
4755  C CD1 . PHE A 310 ? 0.9807  1.0534  1.1600  -0.0289 -0.2628 -0.0668 319 PHE A CD1 
4756  C CD2 . PHE A 310 ? 1.2187  1.2434  1.3771  -0.0100 -0.3136 -0.0462 319 PHE A CD2 
4757  C CE1 . PHE A 310 ? 1.1996  1.2570  1.3417  -0.0412 -0.2717 -0.0618 319 PHE A CE1 
4758  C CE2 . PHE A 310 ? 1.2161  1.2277  1.3354  -0.0235 -0.3216 -0.0405 319 PHE A CE2 
4759  C CZ  . PHE A 310 ? 1.3231  1.3515  1.4350  -0.0384 -0.3002 -0.0495 319 PHE A CZ  
4769  N N   . VAL A 311 ? 0.6141  0.7865  0.9255  -0.0076 -0.2340 -0.1107 320 VAL A N   
4770  C CA  . VAL A 311 ? 0.8224  1.0299  1.1458  -0.0256 -0.2160 -0.1219 320 VAL A CA  
4771  C C   . VAL A 311 ? 0.6475  0.9139  1.0330  -0.0187 -0.2226 -0.1449 320 VAL A C   
4772  O O   . VAL A 311 ? 0.7356  1.0336  1.1377  -0.0312 -0.2257 -0.1534 320 VAL A O   
4773  C CB  . VAL A 311 ? 0.7493  0.9498  1.0536  -0.0389 -0.1822 -0.1185 320 VAL A CB  
4774  C CG1 . VAL A 311 ? 0.5683  0.8063  0.8899  -0.0581 -0.1649 -0.1310 320 VAL A CG1 
4775  C CG2 . VAL A 311 ? 0.8964  1.0504  1.1453  -0.0482 -0.1756 -0.0996 320 VAL A CG2 
4785  N N   . LEU A 312 ? 0.6064  0.8886  1.0275  0.0016  -0.2257 -0.1561 321 LEU A N   
4786  C CA  . LEU A 312 ? 0.6280  0.9706  1.1131  0.0130  -0.2308 -0.1812 321 LEU A CA  
4787  C C   . LEU A 312 ? 0.6532  1.0104  1.1631  0.0230  -0.2656 -0.1852 321 LEU A C   
4788  O O   . LEU A 312 ? 0.6601  1.0765  1.2272  0.0289  -0.2713 -0.2065 321 LEU A O   
4789  C CB  . LEU A 312 ? 0.7636  1.1086  1.2746  0.0370  -0.2307 -0.1926 321 LEU A CB  
4790  C CG  . LEU A 312 ? 0.8681  1.2215  1.3751  0.0296  -0.1969 -0.1988 321 LEU A CG  
4791  C CD1 . LEU A 312 ? 1.0051  1.3416  1.5255  0.0557  -0.2057 -0.2061 321 LEU A CD1 
4792  C CD2 . LEU A 312 ? 1.3492  1.7699  1.8949  0.0165  -0.1748 -0.2204 321 LEU A CD2 
4804  N N   . SER A 313 ? 0.5110  0.8167  0.9824  0.0278  -0.2910 -0.1658 322 SER A N   
4805  C CA  . SER A 313 ? 0.6248  0.9384  1.1176  0.0399  -0.3296 -0.1682 322 SER A CA  
4806  C C   . SER A 313 ? 0.7982  1.1308  1.2840  0.0176  -0.3337 -0.1676 322 SER A C   
4807  O O   . SER A 313 ? 1.0490  1.4119  1.5710  0.0243  -0.3621 -0.1766 322 SER A O   
4808  C CB  . SER A 313 ? 0.7628  1.0105  1.2108  0.0507  -0.3572 -0.1460 322 SER A CB  
4809  O OG  . SER A 313 ? 0.9796  1.1858  1.3622  0.0284  -0.3509 -0.1249 322 SER A OG  
4815  N N   . LYS A 314 ? 0.5478  0.8621  0.9892  -0.0082 -0.3082 -0.1578 323 LYS A N   
4816  C CA  . LYS A 314 ? 0.8368  1.1439  1.2514  -0.0283 -0.3191 -0.1519 323 LYS A CA  
4817  C C   . LYS A 314 ? 1.1208  1.4874  1.5759  -0.0472 -0.3098 -0.1690 323 LYS A C   
4818  O O   . LYS A 314 ? 0.5605  0.9331  1.0112  -0.0604 -0.3292 -0.1689 323 LYS A O   
4819  C CB  . LYS A 314 ? 0.7356  0.9831  1.0756  -0.0435 -0.3022 -0.1321 323 LYS A CB  
4820  C CG  . LYS A 314 ? 1.0344  1.2260  1.3289  -0.0316 -0.3211 -0.1129 323 LYS A CG  
4821  C CD  . LYS A 314 ? 2.5364  2.7103  2.8093  -0.0330 -0.3575 -0.1060 323 LYS A CD  
4830  N N   . GLY A 315 ? 1.1011  1.5144  1.5974  -0.0496 -0.2836 -0.1842 324 GLY A N   
4831  C CA  . GLY A 315 ? 0.9829  1.4536  1.5149  -0.0723 -0.2731 -0.1985 324 GLY A CA  
4832  C C   . GLY A 315 ? 1.0020  1.4435  1.4833  -0.1045 -0.2584 -0.1877 324 GLY A C   
4833  O O   . GLY A 315 ? 0.8037  1.2738  1.2987  -0.1265 -0.2640 -0.1936 324 GLY A O   
4837  N N   . ASP A 316 ? 0.9774  1.3619  1.4018  -0.1073 -0.2410 -0.1726 325 ASP A N   
4838  C CA  . ASP A 316 ? 0.7469  1.0879  1.1143  -0.1306 -0.2317 -0.1614 325 ASP A CA  
4839  C C   . ASP A 316 ? 0.9736  1.3150  1.3328  -0.1448 -0.1972 -0.1612 325 ASP A C   
4840  O O   . ASP A 316 ? 1.2018  1.5123  1.5372  -0.1344 -0.1813 -0.1528 325 ASP A O   
4841  C CB  . ASP A 316 ? 0.7962  1.0719  1.1055  -0.1187 -0.2423 -0.1445 325 ASP A CB  
4842  C CG  . ASP A 316 ? 1.0732  1.3006  1.3212  -0.1376 -0.2340 -0.1354 325 ASP A CG  
4843  O OD1 . ASP A 316 ? 0.9056  1.1311  1.1449  -0.1549 -0.2112 -0.1369 325 ASP A OD1 
4844  O OD2 . ASP A 316 ? 1.2543  1.4427  1.4600  -0.1347 -0.2509 -0.1270 325 ASP A OD2 
4849  N N   . ALA A 317 ? 0.5134  0.8864  0.8885  -0.1712 -0.1874 -0.1688 326 ALA A N   
4850  C CA  . ALA A 317 ? 0.7463  1.1213  1.1138  -0.1873 -0.1572 -0.1680 326 ALA A CA  
4851  C C   . ALA A 317 ? 0.6729  0.9795  0.9776  -0.1901 -0.1450 -0.1522 326 ALA A C   
4852  O O   . ALA A 317 ? 0.5800  0.8769  0.8754  -0.1899 -0.1235 -0.1482 326 ALA A O   
4853  C CB  . ALA A 317 ? 0.4903  0.9032  0.8765  -0.2204 -0.1519 -0.1756 326 ALA A CB  
4859  N N   . GLY A 318 ? 0.7409  1.0010  1.0029  -0.1911 -0.1588 -0.1443 327 GLY A N   
4860  C CA  . GLY A 318 ? 0.6308  0.8316  0.8387  -0.1904 -0.1467 -0.1323 327 GLY A CA  
4861  C C   . GLY A 318 ? 0.7338  0.9184  0.9358  -0.1653 -0.1383 -0.1246 327 GLY A C   
4862  O O   . GLY A 318 ? 0.9016  1.0669  1.0878  -0.1650 -0.1190 -0.1184 327 GLY A O   
4866  N N   . LEU A 319 ? 0.5237  0.7168  0.7405  -0.1452 -0.1548 -0.1245 328 LEU A N   
4867  C CA  . LEU A 319 ? 0.4949  0.6726  0.7075  -0.1239 -0.1493 -0.1165 328 LEU A CA  
4868  C C   . LEU A 319 ? 0.5590  0.7668  0.8054  -0.1208 -0.1323 -0.1224 328 LEU A C   
4869  O O   . LEU A 319 ? 0.6990  0.8873  0.9333  -0.1116 -0.1200 -0.1149 328 LEU A O   
4870  C CB  . LEU A 319 ? 0.9923  1.1717  1.2152  -0.1055 -0.1739 -0.1151 328 LEU A CB  
4871  C CG  . LEU A 319 ? 1.3326  1.4680  1.5066  -0.1033 -0.1874 -0.1036 328 LEU A CG  
4872  C CD1 . LEU A 319 ? 1.7673  1.9093  1.9565  -0.0885 -0.2167 -0.1027 328 LEU A CD1 
4873  C CD2 . LEU A 319 ? 1.3532  1.4501  1.4894  -0.0977 -0.1702 -0.0903 328 LEU A CD2 
4885  N N   . ARG A 320 ? 0.7841  1.0418  1.0732  -0.1289 -0.1313 -0.1365 329 ARG A N   
4886  C CA  . ARG A 320 ? 0.7734  1.0610  1.0907  -0.1266 -0.1133 -0.1441 329 ARG A CA  
4887  C C   . ARG A 320 ? 0.8319  1.0986  1.1200  -0.1446 -0.0900 -0.1369 329 ARG A C   
4888  O O   . ARG A 320 ? 0.8047  1.0567  1.0838  -0.1365 -0.0774 -0.1317 329 ARG A O   
4889  C CB  . ARG A 320 ? 0.8772  1.2314  1.2504  -0.1310 -0.1162 -0.1635 329 ARG A CB  
4890  C CG  . ARG A 320 ? 1.1651  1.5436  1.5782  -0.1041 -0.1385 -0.1733 329 ARG A CG  
4891  C CD  . ARG A 320 ? 1.5228  1.9732  1.9996  -0.1000 -0.1353 -0.1964 329 ARG A CD  
4892  N NE  . ARG A 320 ? 1.1139  1.6077  1.6133  -0.1240 -0.1359 -0.2048 329 ARG A NE  
4893  C CZ  . ARG A 320 ? 1.1723  1.6780  1.6876  -0.1233 -0.1616 -0.2069 329 ARG A CZ  
4894  N NH1 . ARG A 320 ? 1.4266  1.9021  1.9346  -0.0992 -0.1883 -0.2006 329 ARG A NH1 
4895  N NH2 . ARG A 320 ? 1.7846  2.3302  2.3204  -0.1486 -0.1622 -0.2138 329 ARG A NH2 
4909  N N   . GLU A 321 ? 0.6004  0.8592  0.8699  -0.1690 -0.0870 -0.1350 330 GLU A N   
4910  C CA  . GLU A 321 ? 0.6699  0.9031  0.9098  -0.1861 -0.0690 -0.1270 330 GLU A CA  
4911  C C   . GLU A 321 ? 0.9872  1.1679  1.1897  -0.1710 -0.0658 -0.1131 330 GLU A C   
4912  O O   . GLU A 321 ? 0.8022  0.9672  0.9914  -0.1726 -0.0516 -0.1066 330 GLU A O   
4913  C CB  . GLU A 321 ? 0.5584  0.7804  0.7791  -0.2144 -0.0716 -0.1260 330 GLU A CB  
4914  C CG  . GLU A 321 ? 0.8558  1.1352  1.1136  -0.2379 -0.0691 -0.1382 330 GLU A CG  
4921  N N   . ALA A 322 ? 0.8167  0.9728  1.0027  -0.1568 -0.0792 -0.1085 331 ALA A N   
4922  C CA  . ALA A 322 ? 0.5145  0.6275  0.6672  -0.1437 -0.0748 -0.0962 331 ALA A CA  
4923  C C   . ALA A 322 ? 1.1507  1.2703  1.3181  -0.1265 -0.0696 -0.0924 331 ALA A C   
4924  O O   . ALA A 322 ? 0.8938  0.9923  1.0460  -0.1230 -0.0579 -0.0837 331 ALA A O   
4925  C CB  . ALA A 322 ? 0.6430  0.7318  0.7714  -0.1353 -0.0894 -0.0928 331 ALA A CB  
4931  N N   . TYR A 323 ? 0.8308  0.9783  1.0288  -0.1153 -0.0802 -0.0993 332 TYR A N   
4932  C CA  . TYR A 323 ? 0.5754  0.7283  0.7891  -0.1003 -0.0772 -0.0982 332 TYR A CA  
4933  C C   . TYR A 323 ? 0.6094  0.7787  0.8339  -0.1094 -0.0595 -0.1028 332 TYR A C   
4934  O O   . TYR A 323 ? 0.5140  0.6683  0.7307  -0.1032 -0.0516 -0.0961 332 TYR A O   
4935  C CB  . TYR A 323 ? 0.5529  0.7322  0.8005  -0.0856 -0.0950 -0.1079 332 TYR A CB  
4936  C CG  . TYR A 323 ? 0.5394  0.7269  0.8091  -0.0693 -0.0951 -0.1117 332 TYR A CG  
4937  C CD1 . TYR A 323 ? 0.7842  0.9407  1.0399  -0.0543 -0.1059 -0.1000 332 TYR A CD1 
4938  C CD2 . TYR A 323 ? 0.4021  0.6269  0.7038  -0.0701 -0.0848 -0.1274 332 TYR A CD2 
4939  C CE1 . TYR A 323 ? 0.6284  0.7853  0.9009  -0.0403 -0.1090 -0.1032 332 TYR A CE1 
4940  C CE2 . TYR A 323 ? 0.9137  1.1408  1.2319  -0.0538 -0.0861 -0.1329 332 TYR A CE2 
4941  C CZ  . TYR A 323 ? 0.6502  0.8412  0.9540  -0.0388 -0.0997 -0.1208 332 TYR A CZ  
4942  O OH  . TYR A 323 ? 0.8995  1.0869  1.2175  -0.0236 -0.1041 -0.1262 332 TYR A OH  
4952  N N   . ASP A 324 ? 0.6469  0.8488  0.8889  -0.1260 -0.0537 -0.1141 333 ASP A N   
4953  C CA  . ASP A 324 ? 0.5979  0.8154  0.8442  -0.1382 -0.0361 -0.1179 333 ASP A CA  
4954  C C   . ASP A 324 ? 0.6722  0.8485  0.8808  -0.1468 -0.0264 -0.1029 333 ASP A C   
4955  O O   . ASP A 324 ? 0.5393  0.7122  0.7433  -0.1480 -0.0159 -0.1002 333 ASP A O   
4956  C CB  . ASP A 324 ? 1.0025  1.2619  1.2689  -0.1599 -0.0302 -0.1303 333 ASP A CB  
4957  C CG  . ASP A 324 ? 1.3578  1.6729  1.6725  -0.1505 -0.0335 -0.1498 333 ASP A CG  
4958  O OD1 . ASP A 324 ? 1.1103  1.4299  1.4412  -0.1285 -0.0365 -0.1553 333 ASP A OD1 
4959  O OD2 . ASP A 324 ? 1.7134  2.0688  2.0516  -0.1657 -0.0336 -0.1606 333 ASP A OD2 
4964  N N   . ALA A 325 ? 0.8110  0.9544  0.9923  -0.1511 -0.0310 -0.0939 334 ALA A N   
4965  C CA  . ALA A 325 ? 0.7887  0.8949  0.9391  -0.1569 -0.0233 -0.0819 334 ALA A CA  
4966  C C   . ALA A 325 ? 1.1583  1.2482  1.3048  -0.1391 -0.0205 -0.0731 334 ALA A C   
4967  O O   . ALA A 325 ? 1.1356  1.2150  1.2735  -0.1430 -0.0124 -0.0670 334 ALA A O   
4968  C CB  . ALA A 325 ? 0.5026  0.5761  0.6258  -0.1610 -0.0297 -0.0775 334 ALA A CB  
4974  N N   . CYS A 326 ? 0.7343  0.8231  0.8873  -0.1214 -0.0286 -0.0717 335 CYS A N   
4975  C CA  . CYS A 326 ? 1.1606  1.2358  1.3111  -0.1078 -0.0269 -0.0624 335 CYS A CA  
4976  C C   . CYS A 326 ? 0.9203  1.0147  1.0898  -0.1070 -0.0225 -0.0676 335 CYS A C   
4977  O O   . CYS A 326 ? 0.6162  0.6980  0.7784  -0.1063 -0.0168 -0.0600 335 CYS A O   
4978  C CB  . CYS A 326 ? 0.8196  0.8887  0.9701  -0.0932 -0.0379 -0.0587 335 CYS A CB  
4979  S SG  . CYS A 326 ? 1.1469  1.1937  1.2695  -0.0941 -0.0422 -0.0545 335 CYS A SG  
4985  N N   . VAL A 327 ? 0.9524  1.0789  1.1466  -0.1074 -0.0251 -0.0820 336 VAL A N   
4986  C CA  . VAL A 327 ? 0.6598  0.8068  0.8712  -0.1057 -0.0197 -0.0913 336 VAL A CA  
4987  C C   . VAL A 327 ? 0.7835  0.9323  0.9815  -0.1246 -0.0057 -0.0905 336 VAL A C   
4988  O O   . VAL A 327 ? 0.6892  0.8324  0.8820  -0.1242 -0.0005 -0.0886 336 VAL A O   
4989  C CB  . VAL A 327 ? 0.6436  0.8288  0.8889  -0.0988 -0.0259 -0.1098 336 VAL A CB  
4990  C CG1 . VAL A 327 ? 0.4108  0.6212  0.6748  -0.0955 -0.0185 -0.1246 336 VAL A CG1 
4991  C CG2 . VAL A 327 ? 1.2051  1.3797  1.4586  -0.0798 -0.0439 -0.1073 336 VAL A CG2 
5001  N N   . LYS A 328 ? 0.6557  0.8087  0.8445  -0.1432 -0.0012 -0.0909 337 LYS A N   
5002  C CA  . LYS A 328 ? 0.5889  0.7386  0.7596  -0.1644 0.0097  -0.0877 337 LYS A CA  
5003  C C   . LYS A 328 ? 0.7313  0.8395  0.8752  -0.1623 0.0091  -0.0707 337 LYS A C   
5004  O O   . LYS A 328 ? 0.7050  0.8085  0.8382  -0.1696 0.0145  -0.0673 337 LYS A O   
5005  C CB  . LYS A 328 ? 0.6966  0.8544  0.8609  -0.1873 0.0118  -0.0898 337 LYS A CB  
5008  N N   . ALA A 329 ? 1.0134  1.0944  1.1485  -0.1504 0.0020  -0.0610 338 ALA A N   
5009  C CA  . ALA A 329 ? 0.7775  0.8260  0.8947  -0.1455 0.0014  -0.0466 338 ALA A CA  
5010  C C   . ALA A 329 ? 0.9769  1.0296  1.1026  -0.1363 0.0020  -0.0443 338 ALA A C   
5011  O O   . ALA A 329 ? 0.7036  0.7434  0.8173  -0.1424 0.0037  -0.0370 338 ALA A O   
5012  C CB  . ALA A 329 ? 0.8738  0.9009  0.9840  -0.1322 -0.0036 -0.0400 338 ALA A CB  
5018  N N   . LEU A 330 ? 0.8399  0.9091  0.9851  -0.1232 -0.0015 -0.0511 339 LEU A N   
5019  C CA  . LEU A 330 ? 0.6309  0.6999  0.7827  -0.1154 -0.0032 -0.0499 339 LEU A CA  
5020  C C   . LEU A 330 ? 0.6961  0.7790  0.8456  -0.1274 0.0035  -0.0586 339 LEU A C   
5021  O O   . LEU A 330 ? 0.4916  0.5669  0.6368  -0.1263 0.0026  -0.0557 339 LEU A O   
5022  C CB  . LEU A 330 ? 0.7377  0.8169  0.9090  -0.1001 -0.0110 -0.0566 339 LEU A CB  
5023  C CG  . LEU A 330 ? 0.7813  0.8454  0.9516  -0.0883 -0.0191 -0.0463 339 LEU A CG  
5024  C CD1 . LEU A 330 ? 0.8428  0.9124  1.0299  -0.0753 -0.0302 -0.0526 339 LEU A CD1 
5025  C CD2 . LEU A 330 ? 0.7213  0.7642  0.8793  -0.0871 -0.0178 -0.0299 339 LEU A CD2 
5037  N N   . VAL A 331 ? 0.7528  0.8608  0.9075  -0.1385 0.0100  -0.0716 340 VAL A N   
5038  C CA  . VAL A 331 ? 0.8938  1.0180  1.0421  -0.1526 0.0193  -0.0805 340 VAL A CA  
5039  C C   . VAL A 331 ? 0.7944  0.8919  0.9124  -0.1686 0.0209  -0.0655 340 VAL A C   
5040  O O   . VAL A 331 ? 0.7973  0.8938  0.9014  -0.1773 0.0244  -0.0663 340 VAL A O   
5041  C CB  . VAL A 331 ? 0.8355  0.9981  0.9974  -0.1642 0.0280  -0.0971 340 VAL A CB  
5042  C CG1 . VAL A 331 ? 1.0606  1.2430  1.2107  -0.1828 0.0411  -0.1063 340 VAL A CG1 
5043  C CG2 . VAL A 331 ? 0.5609  0.7480  0.7563  -0.1441 0.0223  -0.1120 340 VAL A CG2 
5053  N N   . SER A 332 ? 0.7685  0.8422  0.8738  -0.1726 0.0169  -0.0525 341 SER A N   
5054  C CA  . SER A 332 ? 0.8497  0.8928  0.9275  -0.1848 0.0142  -0.0375 341 SER A CA  
5055  C C   . SER A 332 ? 0.8396  0.8641  0.9165  -0.1721 0.0072  -0.0271 341 SER A C   
5056  O O   . SER A 332 ? 0.7132  0.7261  0.7726  -0.1818 0.0053  -0.0209 341 SER A O   
5057  C CB  . SER A 332 ? 0.7659  0.7859  0.8337  -0.1874 0.0096  -0.0292 341 SER A CB  
5058  O OG  . SER A 332 ? 0.9729  1.0130  1.0433  -0.2019 0.0149  -0.0392 341 SER A OG  
5064  N N   . LEU A 333 ? 0.5403  0.5643  0.6357  -0.1521 0.0028  -0.0254 342 LEU A N   
5065  C CA  . LEU A 333 ? 0.5991  0.6101  0.6976  -0.1420 -0.0039 -0.0151 342 LEU A CA  
5066  C C   . LEU A 333 ? 0.5402  0.5613  0.6388  -0.1453 -0.0038 -0.0224 342 LEU A C   
5067  O O   . LEU A 333 ? 0.7059  0.7137  0.7937  -0.1497 -0.0092 -0.0142 342 LEU A O   
5068  C CB  . LEU A 333 ? 0.6307  0.6420  0.7470  -0.1240 -0.0071 -0.0114 342 LEU A CB  
5069  C CG  . LEU A 333 ? 0.8306  0.8268  0.9427  -0.1186 -0.0074 -0.0028 342 LEU A CG  
5070  C CD1 . LEU A 333 ? 0.8520  0.8548  0.9748  -0.1059 -0.0067 -0.0048 342 LEU A CD1 
5071  C CD2 . LEU A 333 ? 1.3998  1.3802  1.5104  -0.1146 -0.0122 0.0107  342 LEU A CD2 
5083  N N   . ARG A 334 ? 0.7689  0.8133  0.8782  -0.1439 0.0014  -0.0393 343 ARG A N   
5084  C CA  . ARG A 334 ? 0.7398  0.7910  0.8454  -0.1465 0.0020  -0.0490 343 ARG A CA  
5085  C C   . ARG A 334 ? 0.7394  0.7897  0.8177  -0.1681 0.0083  -0.0495 343 ARG A C   
5086  O O   . ARG A 334 ? 0.7448  0.7837  0.8072  -0.1735 0.0042  -0.0468 343 ARG A O   
5087  C CB  . ARG A 334 ? 1.0811  1.1577  1.2081  -0.1358 0.0050  -0.0700 343 ARG A CB  
5088  C CG  . ARG A 334 ? 0.9109  0.9786  1.0570  -0.1161 -0.0063 -0.0681 343 ARG A CG  
5089  C CD  . ARG A 334 ? 0.7173  0.7744  0.8693  -0.1096 -0.0107 -0.0532 343 ARG A CD  
5090  N NE  . ARG A 334 ? 0.5859  0.6269  0.7457  -0.0980 -0.0214 -0.0423 343 ARG A NE  
5091  C CZ  . ARG A 334 ? 1.0736  1.1155  1.2476  -0.0855 -0.0290 -0.0467 343 ARG A CZ  
5092  N NH1 . ARG A 334 ? 1.1255  1.1860  1.3123  -0.0796 -0.0284 -0.0633 343 ARG A NH1 
5093  N NH2 . ARG A 334 ? 0.9809  1.0060  1.1570  -0.0800 -0.0383 -0.0333 343 ARG A NH2 
5107  N N   . SER A 335 ? 0.6217  0.6794  0.6899  -0.1831 0.0160  -0.0501 344 SER A N   
5108  C CA  . SER A 335 ? 0.9197  0.9761  0.9572  -0.2072 0.0218  -0.0499 344 SER A CA  
5109  C C   . SER A 335 ? 0.8431  0.8621  0.8564  -0.2132 0.0096  -0.0286 344 SER A C   
5110  O O   . SER A 335 ? 0.5598  0.5703  0.5508  -0.2233 0.0069  -0.0267 344 SER A O   
5111  C CB  . SER A 335 ? 1.1471  1.2204  1.1779  -0.2262 0.0324  -0.0545 344 SER A CB  
5112  O OG  . SER A 335 ? 1.3690  1.4845  1.4236  -0.2224 0.0440  -0.0770 344 SER A OG  
5118  N N   . TYR A 336 ? 0.5757  0.5734  0.5972  -0.2024 0.0003  -0.0141 345 TYR A N   
5119  C CA  . TYR A 336 ? 0.5477  0.5127  0.5528  -0.2047 -0.0131 0.0049  345 TYR A CA  
5120  C C   . TYR A 336 ? 1.0592  1.0204  1.0690  -0.1965 -0.0217 0.0081  345 TYR A C   
5121  O O   . TYR A 336 ? 0.5345  0.4771  0.5213  -0.2076 -0.0312 0.0179  345 TYR A O   
5122  C CB  . TYR A 336 ? 0.5156  0.4640  0.5330  -0.1916 -0.0191 0.0150  345 TYR A CB  
5123  C CG  . TYR A 336 ? 0.9100  0.8246  0.9108  -0.1945 -0.0337 0.0328  345 TYR A CG  
5124  C CD1 . TYR A 336 ? 0.8010  0.6916  0.7683  -0.2157 -0.0385 0.0404  345 TYR A CD1 
5125  C CD2 . TYR A 336 ? 0.7805  0.6874  0.8001  -0.1764 -0.0443 0.0426  345 TYR A CD2 
5126  C CE1 . TYR A 336 ? 1.0962  0.9527  1.0490  -0.2164 -0.0557 0.0567  345 TYR A CE1 
5127  C CE2 . TYR A 336 ? 1.0128  0.8923  1.0225  -0.1765 -0.0597 0.0573  345 TYR A CE2 
5128  C CZ  . TYR A 336 ? 1.2382  1.0904  1.2146  -0.1949 -0.0666 0.0642  345 TYR A CZ  
5129  O OH  . TYR A 336 ? 0.9722  0.7937  0.9406  -0.1921 -0.0856 0.0793  345 TYR A OH  
5139  N N   . HIS A 337 ? 0.7270  0.7042  0.7637  -0.1795 -0.0200 0.0000  346 HIS A N   
5140  C CA  . HIS A 337 ? 0.7555  0.7297  0.7971  -0.1740 -0.0286 0.0009  346 HIS A CA  
5141  C C   . HIS A 337 ? 0.6789  0.6552  0.6941  -0.1895 -0.0261 -0.0095 346 HIS A C   
5142  O O   . HIS A 337 ? 0.7582  0.7193  0.7583  -0.1955 -0.0370 -0.0026 346 HIS A O   
5143  C CB  . HIS A 337 ? 0.8867  0.8745  0.9567  -0.1567 -0.0273 -0.0072 346 HIS A CB  
5144  C CG  . HIS A 337 ? 1.0198  0.9986  1.1008  -0.1495 -0.0397 0.0009  346 HIS A CG  
5145  N ND1 . HIS A 337 ? 0.8690  0.8525  0.9735  -0.1360 -0.0426 0.0002  346 HIS A ND1 
5146  C CD2 . HIS A 337 ? 0.8984  0.8630  0.9697  -0.1561 -0.0517 0.0115  346 HIS A CD2 
5147  C CE1 . HIS A 337 ? 0.7832  0.7572  0.8927  -0.1361 -0.0545 0.0100  346 HIS A CE1 
5148  N NE2 . HIS A 337 ? 0.7016  0.6655  0.7928  -0.1475 -0.0604 0.0161  346 HIS A NE2 
5156  N N   . LEU A 338 ? 0.9007  0.8983  0.9107  -0.1962 -0.0117 -0.0275 347 LEU A N   
5157  C CA  . LEU A 338 ? 1.0460  1.0481  1.0271  -0.2124 -0.0066 -0.0387 347 LEU A CA  
5158  C C   . LEU A 338 ? 0.8926  0.8702  0.8358  -0.2338 -0.0138 -0.0216 347 LEU A C   
5159  O O   . LEU A 338 ? 0.6393  0.6048  0.5557  -0.2443 -0.0203 -0.0210 347 LEU A O   
5160  C CB  . LEU A 338 ? 1.1609  1.1970  1.1443  -0.2182 0.0128  -0.0614 347 LEU A CB  
5161  C CG  . LEU A 338 ? 0.9788  1.0376  0.9923  -0.1978 0.0170  -0.0840 347 LEU A CG  
5162  C CD1 . LEU A 338 ? 0.9669  1.0644  0.9983  -0.1978 0.0337  -0.1035 347 LEU A CD1 
5163  C CD2 . LEU A 338 ? 0.8819  0.9374  0.8779  -0.1990 0.0157  -0.0985 347 LEU A CD2 
5175  N N   . GLN A 339 ? 1.3040  1.2693  1.2424  -0.2403 -0.0158 -0.0071 348 GLN A N   
5176  C CA  . GLN A 339 ? 1.1035  1.0392  1.0042  -0.2603 -0.0268 0.0106  348 GLN A CA  
5177  C C   . GLN A 339 ? 1.0694  0.9803  0.9731  -0.2508 -0.0481 0.0264  348 GLN A C   
5178  O O   . GLN A 339 ? 0.8763  0.7678  0.7475  -0.2656 -0.0595 0.0346  348 GLN A O   
5179  C CB  . GLN A 339 ? 1.2558  1.1772  1.1511  -0.2674 -0.0276 0.0223  348 GLN A CB  
5180  C CG  . GLN A 339 ? 1.3969  1.3399  1.2809  -0.2861 -0.0094 0.0107  348 GLN A CG  
5181  C CD  . GLN A 339 ? 1.5370  1.4628  1.4212  -0.2900 -0.0128 0.0215  348 GLN A CD  
5182  O OE1 . GLN A 339 ? 1.4963  1.3834  1.3598  -0.2959 -0.0290 0.0404  348 GLN A OE1 
5183  N NE2 . GLN A 339 ? 1.5793  1.5312  1.4888  -0.2842 -0.0002 0.0090  348 GLN A NE2 
5192  N N   . ILE A 340 ? 1.0058  0.9197  0.9481  -0.2273 -0.0537 0.0304  349 ILE A N   
5193  C CA  . ILE A 340 ? 0.9403  0.8385  0.8930  -0.2184 -0.0731 0.0451  349 ILE A CA  
5194  C C   . ILE A 340 ? 0.8373  0.7367  0.7776  -0.2243 -0.0785 0.0383  349 ILE A C   
5195  O O   . ILE A 340 ? 0.9404  0.8202  0.8597  -0.2341 -0.0953 0.0497  349 ILE A O   
5196  C CB  . ILE A 340 ? 1.0273  0.9361  1.0245  -0.1944 -0.0739 0.0486  349 ILE A CB  
5197  C CG1 . ILE A 340 ? 0.7438  0.6453  0.7481  -0.1883 -0.0713 0.0552  349 ILE A CG1 
5198  C CG2 . ILE A 340 ? 1.1152  1.0168  1.1283  -0.1873 -0.0925 0.0623  349 ILE A CG2 
5199  C CD1 . ILE A 340 ? 0.7751  0.6452  0.7512  -0.2004 -0.0860 0.0704  349 ILE A CD1 
5211  N N   . VAL A 341 ? 0.8483  0.7680  0.7990  -0.2186 -0.0663 0.0189  350 VAL A N   
5212  C CA  . VAL A 341 ? 0.7395  0.6556  0.6765  -0.2230 -0.0727 0.0101  350 VAL A CA  
5213  C C   . VAL A 341 ? 1.0118  0.9165  0.8986  -0.2469 -0.0729 0.0075  350 VAL A C   
5214  O O   . VAL A 341 ? 1.2904  1.1809  1.1554  -0.2549 -0.0855 0.0078  350 VAL A O   
5215  C CB  . VAL A 341 ? 1.0825  1.0185  1.0378  -0.2109 -0.0607 -0.0130 350 VAL A CB  
5216  C CG1 . VAL A 341 ? 0.9405  0.8691  0.8728  -0.2174 -0.0657 -0.0268 350 VAL A CG1 
5217  C CG2 . VAL A 341 ? 1.2586  1.1989  1.2557  -0.1909 -0.0657 -0.0072 350 VAL A CG2 
5227  N N   . THR A 342 ? 1.0414  0.9510  0.9060  -0.2612 -0.0598 0.0054  351 THR A N   
5228  C CA  . THR A 342 ? 1.3350  1.2319  1.1465  -0.2878 -0.0603 0.0062  351 THR A CA  
5229  C C   . THR A 342 ? 1.3007  1.1625  1.0920  -0.2965 -0.0860 0.0324  351 THR A C   
5230  O O   . THR A 342 ? 1.3011  1.1461  1.0607  -0.3086 -0.0995 0.0353  351 THR A O   
5231  C CB  . THR A 342 ? 1.3906  1.3021  1.1840  -0.3044 -0.0406 0.0003  351 THR A CB  
5232  O OG1 . THR A 342 ? 1.1741  1.1227  0.9954  -0.2922 -0.0193 -0.0254 351 THR A OG1 
5233  C CG2 . THR A 342 ? 1.3958  1.2948  1.1282  -0.3365 -0.0395 0.0025  351 THR A CG2 
5241  N N   . LYS A 343 ? 1.2754  1.1253  1.0868  -0.2882 -0.0951 0.0507  352 LYS A N   
5242  C CA  . LYS A 343 ? 0.8803  0.6966  0.6757  -0.2940 -0.1212 0.0750  352 LYS A CA  
5243  C C   . LYS A 343 ? 0.9007  0.7130  0.7169  -0.2819 -0.1415 0.0811  352 LYS A C   
5244  O O   . LYS A 343 ? 1.0769  0.8654  0.8648  -0.2942 -0.1636 0.0937  352 LYS A O   
5245  C CB  . LYS A 343 ? 0.8255  0.6312  0.6433  -0.2829 -0.1257 0.0888  352 LYS A CB  
5246  C CG  . LYS A 343 ? 0.9662  0.7315  0.7650  -0.2883 -0.1551 0.1142  352 LYS A CG  
5247  C CD  . LYS A 343 ? 1.3684  1.1260  1.2045  -0.2661 -0.1625 0.1240  352 LYS A CD  
5248  C CE  . LYS A 343 ? 1.6057  1.3252  1.4299  -0.2664 -0.1945 0.1462  352 LYS A CE  
5249  N NZ  . LYS A 343 ? 1.1043  0.8151  0.9639  -0.2428 -0.2019 0.1527  352 LYS A NZ  
5263  N N   . TYR A 344 ? 0.9168  0.7520  0.7792  -0.2607 -0.1354 0.0724  353 TYR A N   
5264  C CA  . TYR A 344 ? 1.1462  0.9806  1.0373  -0.2494 -0.1552 0.0816  353 TYR A CA  
5265  C C   . TYR A 344 ? 1.1036  0.9412  0.9847  -0.2545 -0.1575 0.0683  353 TYR A C   
5266  O O   . TYR A 344 ? 1.1235  0.9592  1.0249  -0.2497 -0.1759 0.0765  353 TYR A O   
5267  C CB  . TYR A 344 ? 1.0575  0.9119  1.0063  -0.2246 -0.1509 0.0851  353 TYR A CB  
5268  C CG  . TYR A 344 ? 0.8826  0.7285  0.8466  -0.2155 -0.1582 0.1010  353 TYR A CG  
5269  C CD1 . TYR A 344 ? 0.9278  0.7625  0.9051  -0.2110 -0.1831 0.1190  353 TYR A CD1 
5270  C CD2 . TYR A 344 ? 1.0035  0.8504  0.9671  -0.2117 -0.1424 0.0970  353 TYR A CD2 
5271  C CE1 . TYR A 344 ? 1.3861  1.2103  1.3776  -0.1995 -0.1910 0.1307  353 TYR A CE1 
5272  C CE2 . TYR A 344 ? 0.8799  0.7125  0.8533  -0.2026 -0.1508 0.1095  353 TYR A CE2 
5273  C CZ  . TYR A 344 ? 1.0271  0.8482  1.0146  -0.1954 -0.1745 0.1252  353 TYR A CZ  
5274  O OH  . TYR A 344 ? 1.3580  1.1640  1.3570  -0.1832 -0.1832 0.1343  353 TYR A OH  
5284  N N   . ILE A 345 ? 1.4955  1.6829  1.1616  -0.2774 0.1120  0.1755  354 ILE A N   
5285  C CA  . ILE A 345 ? 1.0276  1.2475  0.6453  -0.2877 0.1068  0.1570  354 ILE A CA  
5286  C C   . ILE A 345 ? 1.1995  1.4998  0.7741  -0.2857 0.1235  0.1342  354 ILE A C   
5287  O O   . ILE A 345 ? 1.2774  1.5991  0.8019  -0.2831 0.1143  0.1237  354 ILE A O   
5288  C CB  . ILE A 345 ? 1.0225  1.2426  0.6436  -0.2959 0.1023  0.1419  354 ILE A CB  
5289  C CG1 . ILE A 345 ? 0.7543  0.8999  0.4189  -0.2940 0.0827  0.1671  354 ILE A CG1 
5290  C CG2 . ILE A 345 ? 1.2442  1.4707  0.8629  -0.2670 0.0699  0.0914  354 ILE A CG2 
5291  C CD1 . ILE A 345 ? 0.7345  0.8567  0.4300  -0.2917 0.0668  0.1576  354 ILE A CD1 
5303  N N   . LEU A 346 ? 0.9017  1.2540  0.4953  -0.2828 0.1456  0.1206  355 LEU A N   
5304  C CA  . LEU A 346 ? 1.1572  1.6068  0.7178  -0.2734 0.1621  0.0859  355 LEU A CA  
5305  C C   . LEU A 346 ? 1.2689  1.7332  0.8027  -0.2742 0.1662  0.1084  355 LEU A C   
5306  O O   . LEU A 346 ? 1.2316  1.7622  0.7200  -0.2608 0.1681  0.0797  355 LEU A O   
5307  C CB  . LEU A 346 ? 1.3397  1.8459  0.9370  -0.2714 0.1848  0.0683  355 LEU A CB  
5308  C CG  . LEU A 346 ? 1.9287  2.4469  1.5423  -0.2669 0.1827  0.0302  355 LEU A CG  
5314  N N   . ILE A 347 ? 1.3835  1.7900  0.9420  -0.2851 0.1638  0.1529  356 ILE A N   
5315  C CA  . ILE A 347 ? 1.5828  1.9988  1.1149  -0.2911 0.1656  0.1785  356 ILE A CA  
5316  C C   . ILE A 347 ? 1.9557  2.3436  1.4444  -0.2864 0.1447  0.1779  356 ILE A C   
5317  O O   . ILE A 347 ? 2.6141  3.0541  2.0511  -0.2800 0.1468  0.1661  356 ILE A O   
5318  C CB  . ILE A 347 ? 2.7281  3.0917  2.2996  -0.3026 0.1632  0.2173  356 ILE A CB  
5319  C CG1 . ILE A 347 ? 1.9461  2.3557  1.5462  -0.3107 0.1842  0.2199  356 ILE A CG1 
5320  C CG2 . ILE A 347 ? 1.6555  2.0072  1.1987  -0.3120 0.1553  0.2469  356 ILE A CG2 
5321  C CD1 . ILE A 347 ? 1.5447  1.9012  1.1882  -0.3197 0.1775  0.2492  356 ILE A CD1 
5333  N N   . PRO A 348 ? 1.5833  1.8946  1.0911  -0.2874 0.1231  0.1887  357 PRO A N   
5334  C CA  . PRO A 348 ? 2.4472  2.7334  1.9151  -0.2854 0.0999  0.1868  357 PRO A CA  
5335  C C   . PRO A 348 ? 1.6823  2.0244  1.0932  -0.2732 0.0934  0.1445  357 PRO A C   
5336  O O   . PRO A 348 ? 1.5571  1.9160  0.9148  -0.2639 0.0794  0.1346  357 PRO A O   
5337  C CB  . PRO A 348 ? 1.3373  1.5505  0.8484  -0.2884 0.0818  0.1961  357 PRO A CB  
5338  C CG  . PRO A 348 ? 1.5438  1.7344  1.1124  -0.2863 0.0927  0.2098  357 PRO A CG  
5339  C CD  . PRO A 348 ? 1.6145  1.8633  1.1816  -0.2877 0.1171  0.2021  357 PRO A CD  
5347  N N   . ALA A 349 ? 1.0014  1.3741  0.4209  -0.2676 0.0976  0.1106  358 ALA A N   
5348  C CA  . ALA A 349 ? 1.2644  1.6879  0.6451  -0.2409 0.0769  0.0464  358 ALA A CA  
5349  C C   . ALA A 349 ? 1.4854  2.0075  0.8234  -0.2183 0.0925  0.0148  358 ALA A C   
5350  O O   . ALA A 349 ? 1.9362  2.4981  1.2337  -0.1853 0.0652  -0.0421 358 ALA A O   
5351  C CB  . ALA A 349 ? 0.9991  1.4116  0.4476  -0.2235 0.0699  0.0098  358 ALA A CB  
5357  N N   . SER A 350 ? 1.1892  1.7428  0.5494  -0.2303 0.1277  0.0478  359 SER A N   
5358  C CA  . SER A 350 ? 1.3021  1.9406  0.6319  -0.2172 0.1453  0.0366  359 SER A CA  
5359  C C   . SER A 350 ? 1.2603  1.8720  0.5432  -0.2221 0.1345  0.0688  359 SER A C   
5360  O O   . SER A 350 ? 1.2957  1.9752  0.5458  -0.2152 0.1484  0.0674  359 SER A O   
5361  C CB  . SER A 350 ? 1.6986  2.3746  1.0697  -0.2365 0.1794  0.0661  359 SER A CB  
5362  O OG  . SER A 350 ? 2.0853  2.6908  1.4741  -0.2653 0.1805  0.1302  359 SER A OG  
5368  N N   . GLN A 351 ? 2.2855  2.8033  1.5697  -0.2369 0.1119  0.1026  360 GLN A N   
5369  C CA  . GLN A 351 ? 3.0680  3.5564  2.3095  -0.2397 0.0968  0.1296  360 GLN A CA  
5370  C C   . GLN A 351 ? 2.6523  3.1132  1.8484  -0.2193 0.0559  0.0969  360 GLN A C   
5371  O O   . GLN A 351 ? 1.6497  2.0946  0.8020  -0.2155 0.0395  0.1100  360 GLN A O   
5372  C CB  . GLN A 351 ? 2.2400  2.6460  1.5248  -0.2680 0.0953  0.1883  360 GLN A CB  
5373  C CG  . GLN A 351 ? 2.5444  2.9693  1.8684  -0.2859 0.1220  0.2190  360 GLN A CG  
5374  C CD  . GLN A 351 ? 3.0966  3.4412  2.4682  -0.3034 0.1105  0.2594  360 GLN A CD  
5375  O OE1 . GLN A 351 ? 1.9572  2.2505  1.3176  -0.3055 0.0878  0.2748  360 GLN A OE1 
5376  N NE2 . GLN A 351 ? 1.6714  2.0083  1.0963  -0.3128 0.1229  0.2710  360 GLN A NE2 
5385  N N   . GLN A 352 ? 2.3577  2.8109  1.5633  -0.2061 0.0319  0.0525  361 GLN A N   
5386  C CA  . GLN A 352 ? 2.1342  2.5616  1.3064  -0.1850 -0.0222 0.0112  361 GLN A CA  
5387  C C   . GLN A 352 ? 2.1947  2.7067  1.3368  -0.1334 -0.0385 -0.0704 361 GLN A C   
5388  O O   . GLN A 352 ? 1.9998  2.5608  1.1728  -0.1119 -0.0340 -0.1208 361 GLN A O   
5389  C CB  . GLN A 352 ? 1.9001  2.2362  1.1593  -0.1854 -0.0515 0.0047  361 GLN A CB  
5392  N N   . PRO A 353 ? 2.4927  3.0215  1.5835  -0.1073 -0.0587 -0.0897 362 PRO A N   
5393  C CA  . PRO A 353 ? 1.8437  2.4527  0.9158  -0.0524 -0.0731 -0.1701 362 PRO A CA  
5394  C C   . PRO A 353 ? 1.8446  2.4251  0.9497  -0.0048 -0.1458 -0.2561 362 PRO A C   
5395  O O   . PRO A 353 ? 2.1281  2.7456  1.2233  0.0460  -0.1750 -0.3229 362 PRO A O   
5396  C CB  . PRO A 353 ? 1.8161  2.4416  0.8210  -0.0481 -0.0684 -0.1479 362 PRO A CB  
5397  C CG  . PRO A 353 ? 1.8209  2.3476  0.8155  -0.0798 -0.0909 -0.0912 362 PRO A CG  
5398  C CD  . PRO A 353 ? 1.8670  2.3437  0.9184  -0.1253 -0.0671 -0.0378 362 PRO A CD  
5406  N N   . GLY A 371 ? 2.0219  2.0897  1.9421  -0.0825 -0.2420 -0.2070 380 GLY A N   
5407  C CA  . GLY A 371 ? 1.8855  1.9740  1.7525  -0.0975 -0.2135 -0.1819 380 GLY A CA  
5408  C C   . GLY A 371 ? 1.9212  2.0622  1.7331  -0.1281 -0.1359 -0.1359 380 GLY A C   
5409  O O   . GLY A 371 ? 1.7195  1.8300  1.5373  -0.1585 -0.1106 -0.0794 380 GLY A O   
5412  N N   . GLY A 372 ? 2.0565  2.2788  1.8156  -0.1195 -0.1019 -0.1599 381 GLY A N   
5413  C CA  . GLY A 372 ? 1.9002  2.1745  1.6126  -0.1500 -0.0354 -0.1162 381 GLY A CA  
5414  C C   . GLY A 372 ? 1.5731  1.8972  1.3045  -0.1497 -0.0044 -0.1290 381 GLY A C   
5415  O O   . GLY A 372 ? 2.2059  2.5109  1.9427  -0.1788 0.0253  -0.0797 381 GLY A O   
5419  N N   . THR A 373 ? 1.9519  2.3425  1.6985  -0.1132 -0.0151 -0.2005 382 THR A N   
5420  C CA  . THR A 373 ? 1.3709  1.8270  1.1392  -0.1098 0.0154  -0.2214 382 THR A CA  
5421  C C   . THR A 373 ? 1.3331  1.7318  1.1667  -0.0935 -0.0233 -0.2437 382 THR A C   
5422  O O   . THR A 373 ? 2.2343  2.6583  2.0896  -0.1016 0.0023  -0.2390 382 THR A O   
5423  C CB  . THR A 373 ? 1.2156  1.7982  0.9664  -0.0780 0.0307  -0.2898 382 THR A CB  
5424  O OG1 . THR A 373 ? 1.5341  2.1068  1.3068  -0.0290 -0.0296 -0.3642 382 THR A OG1 
5425  C CG2 . THR A 373 ? 1.4982  2.1505  1.1776  -0.1009 0.0765  -0.2559 382 THR A CG2 
5433  N N   . ASP A 374 ? 1.7396  2.0607  1.6086  -0.0722 -0.0884 -0.2659 383 ASP A N   
5434  C CA  . ASP A 374 ? 1.6520  1.9135  1.5806  -0.0612 -0.1293 -0.2776 383 ASP A CA  
5435  C C   . ASP A 374 ? 1.4268  1.6449  1.3536  -0.0998 -0.0980 -0.2052 383 ASP A C   
5436  O O   . ASP A 374 ? 1.4033  1.6025  1.3662  -0.0945 -0.1096 -0.2114 383 ASP A O   
5437  C CB  . ASP A 374 ? 1.6732  1.8393  1.6413  -0.0472 -0.2072 -0.2853 383 ASP A CB  
5438  C CG  . ASP A 374 ? 1.6380  1.8343  1.6267  0.0022  -0.2585 -0.3729 383 ASP A CG  
5439  O OD1 . ASP A 374 ? 1.5920  1.8025  1.6283  0.0385  -0.2956 -0.4378 383 ASP A OD1 
5440  O OD2 . ASP A 374 ? 2.0818  2.2867  2.0414  0.0078  -0.2663 -0.3805 383 ASP A OD2 
5445  N N   . LEU A 375 ? 1.4700  1.6737  1.3553  -0.1349 -0.0626 -0.1410 384 LEU A N   
5446  C CA  . LEU A 375 ? 1.2293  1.4010  1.1086  -0.1676 -0.0327 -0.0766 384 LEU A CA  
5447  C C   . LEU A 375 ? 1.0739  1.3127  0.9490  -0.1747 0.0157  -0.0804 384 LEU A C   
5448  O O   . LEU A 375 ? 1.1195  1.3361  1.0143  -0.1828 0.0217  -0.0601 384 LEU A O   
5449  C CB  . LEU A 375 ? 1.4015  1.5476  1.2429  -0.1963 -0.0149 -0.0194 384 LEU A CB  
5450  C CG  . LEU A 375 ? 1.1658  1.2916  0.9955  -0.2262 0.0173  0.0416  384 LEU A CG  
5451  C CD1 . LEU A 375 ? 1.1639  1.2337  1.0258  -0.2266 -0.0080 0.0622  384 LEU A CD1 
5452  C CD2 . LEU A 375 ? 1.3851  1.4921  1.1834  -0.2471 0.0266  0.0841  384 LEU A CD2 
5464  N N   . MET A 376 ? 1.2510  1.5758  1.1012  -0.1733 0.0494  -0.1029 385 MET A N   
5465  C CA  . MET A 376 ? 1.2020  1.5994  1.0569  -0.1853 0.0942  -0.1019 385 MET A CA  
5466  C C   . MET A 376 ? 1.2853  1.7063  1.1927  -0.1580 0.0777  -0.1555 385 MET A C   
5467  O O   . MET A 376 ? 1.6787  2.0993  1.6108  -0.1689 0.0930  -0.1403 385 MET A O   
5468  C CB  . MET A 376 ? 1.3293  1.8243  1.1457  -0.1921 0.1313  -0.1099 385 MET A CB  
5469  C CG  . MET A 376 ? 1.3769  1.8541  1.1441  -0.2283 0.1558  -0.0445 385 MET A CG  
5470  S SD  . MET A 376 ? 1.3419  1.8483  1.1103  -0.2722 0.2029  0.0154  385 MET A SD  
5477  N N   . ASN A 377 ? 1.2008  1.6365  1.1304  -0.1193 0.0392  -0.2220 386 ASN A N   
5478  C CA  . ASN A 377 ? 1.3526  1.8068  1.3376  -0.0892 0.0153  -0.2788 386 ASN A CA  
5479  C C   . ASN A 377 ? 2.0472  2.4065  2.0577  -0.0990 -0.0088 -0.2428 386 ASN A C   
5480  O O   . ASN A 377 ? 1.0499  1.4270  1.0871  -0.1020 0.0061  -0.2440 386 ASN A O   
5481  C CB  . ASN A 377 ? 1.2731  1.7308  1.2840  -0.0422 -0.0407 -0.3556 386 ASN A CB  
5482  C CG  . ASN A 377 ? 1.3086  1.8722  1.2891  -0.0242 -0.0200 -0.4008 386 ASN A CG  
5483  O OD1 . ASN A 377 ? 1.4452  1.9921  1.4188  0.0025  -0.0613 -0.4370 386 ASN A OD1 
5484  N ND2 . ASN A 377 ? 1.1488  1.8276  1.1128  -0.0386 0.0418  -0.3989 386 ASN A ND2 
5491  N N   . PHE A 378 ? 1.3587  1.6230  1.3574  -0.1083 -0.0420 -0.2031 387 PHE A N   
5492  C CA  . PHE A 378 ? 1.0843  1.2652  1.0998  -0.1175 -0.0672 -0.1643 387 PHE A CA  
5493  C C   . PHE A 378 ? 1.0139  1.2129  1.0186  -0.1414 -0.0206 -0.1250 387 PHE A C   
5494  O O   . PHE A 378 ? 1.1167  1.3005  1.1495  -0.1337 -0.0316 -0.1316 387 PHE A O   
5495  C CB  . PHE A 378 ? 0.8575  0.9585  0.8546  -0.1339 -0.0947 -0.1139 387 PHE A CB  
5496  C CG  . PHE A 378 ? 0.8582  0.8890  0.8600  -0.1497 -0.1115 -0.0600 387 PHE A CG  
5497  C CD1 . PHE A 378 ? 0.9371  0.9196  0.9775  -0.1327 -0.1638 -0.0752 387 PHE A CD1 
5498  C CD2 . PHE A 378 ? 0.7350  0.7532  0.7016  -0.1797 -0.0772 0.0047  387 PHE A CD2 
5499  C CE1 . PHE A 378 ? 0.9353  0.8625  0.9727  -0.1478 -0.1786 -0.0218 387 PHE A CE1 
5500  C CE2 . PHE A 378 ? 0.7322  0.7017  0.6980  -0.1910 -0.0904 0.0525  387 PHE A CE2 
5501  C CZ  . PHE A 378 ? 1.0308  0.9577  1.0285  -0.1763 -0.1389 0.0418  387 PHE A CZ  
5511  N N   . LEU A 379 ? 0.9352  1.1664  0.9030  -0.1684 0.0263  -0.0875 388 LEU A N   
5512  C CA  . LEU A 379 ? 1.0037  1.2454  0.9684  -0.1900 0.0612  -0.0516 388 LEU A CA  
5513  C C   . LEU A 379 ? 0.9371  1.2584  0.9352  -0.1849 0.0862  -0.0882 388 LEU A C   
5514  O O   . LEU A 379 ? 0.8291  1.1434  0.8525  -0.1871 0.0895  -0.0820 388 LEU A O   
5515  C CB  . LEU A 379 ? 0.8703  1.1108  0.7923  -0.2201 0.0921  0.0009  388 LEU A CB  
5516  C CG  . LEU A 379 ? 1.3366  1.5033  1.2354  -0.2288 0.0725  0.0453  388 LEU A CG  
5517  C CD1 . LEU A 379 ? 1.5868  1.7575  1.4477  -0.2491 0.0914  0.0778  388 LEU A CD1 
5518  C CD2 . LEU A 379 ? 1.9139  2.0451  1.8173  -0.2346 0.0725  0.0781  388 LEU A CD2 
5530  N N   . LYS A 380 ? 0.6768  1.0804  0.6798  -0.1755 0.1013  -0.1301 389 LYS A N   
5531  C CA  . LYS A 380 ? 0.8558  1.3479  0.8993  -0.1712 0.1250  -0.1652 389 LYS A CA  
5532  C C   . LYS A 380 ? 0.8965  1.3593  0.9910  -0.1414 0.0873  -0.2077 389 LYS A C   
5533  O O   . LYS A 380 ? 1.2140  1.7067  1.3473  -0.1439 0.0992  -0.2154 389 LYS A O   
5534  C CB  . LYS A 380 ? 1.0694  1.6705  1.1076  -0.1600 0.1456  -0.2098 389 LYS A CB  
5535  C CG  . LYS A 380 ? 0.7034  1.3709  0.7001  -0.1949 0.1942  -0.1676 389 LYS A CG  
5542  N N   . THR A 381 ? 1.1834  1.5835  1.2817  -0.1142 0.0363  -0.2335 390 THR A N   
5543  C CA  . THR A 381 ? 0.9631  1.3176  1.1060  -0.0861 -0.0115 -0.2681 390 THR A CA  
5544  C C   . THR A 381 ? 1.0864  1.3659  1.2222  -0.1023 -0.0175 -0.2154 390 THR A C   
5545  O O   . THR A 381 ? 1.2709  1.5527  1.4424  -0.0923 -0.0255 -0.2325 390 THR A O   
5546  C CB  . THR A 381 ? 0.8016  1.0934  0.9494  -0.0602 -0.0724 -0.2940 390 THR A CB  
5547  O OG1 . THR A 381 ? 0.7828  1.1410  0.9306  -0.0405 -0.0720 -0.3457 390 THR A OG1 
5548  C CG2 . THR A 381 ? 1.2470  1.4961  1.4473  -0.0287 -0.1301 -0.3361 390 THR A CG2 
5556  N N   . VAL A 382 ? 0.8036  1.0216  0.8939  -0.1244 -0.0154 -0.1543 391 VAL A N   
5557  C CA  . VAL A 382 ? 0.9256  1.0845  1.0025  -0.1355 -0.0206 -0.1069 391 VAL A CA  
5558  C C   . VAL A 382 ? 1.0302  1.2331  1.1192  -0.1482 0.0173  -0.0993 391 VAL A C   
5559  O O   . VAL A 382 ? 1.1800  1.3570  1.2833  -0.1415 0.0048  -0.0945 391 VAL A O   
5560  C CB  . VAL A 382 ? 0.8663  0.9731  0.8952  -0.1563 -0.0198 -0.0467 391 VAL A CB  
5561  C CG1 . VAL A 382 ? 1.4712  1.5471  1.4791  -0.1680 -0.0112 0.0003  391 VAL A CG1 
5562  C CG2 . VAL A 382 ? 0.8025  0.8494  0.8355  -0.1450 -0.0707 -0.0459 391 VAL A CG2 
5572  N N   . ARG A 383 ? 0.8586  1.1274  0.9435  -0.1674 0.0596  -0.0958 392 ARG A N   
5573  C CA  . ARG A 383 ? 0.8170  1.1280  0.9247  -0.1843 0.0900  -0.0848 392 ARG A CA  
5574  C C   . ARG A 383 ? 0.9268  1.2928  1.0963  -0.1665 0.0858  -0.1383 392 ARG A C   
5575  O O   . ARG A 383 ? 1.0113  1.3680  1.2129  -0.1641 0.0794  -0.1392 392 ARG A O   
5576  C CB  . ARG A 383 ? 0.8720  1.2379  0.9592  -0.2146 0.1315  -0.0581 392 ARG A CB  
5577  C CG  . ARG A 383 ? 0.7748  1.1801  0.8907  -0.2394 0.1576  -0.0365 392 ARG A CG  
5578  C CD  . ARG A 383 ? 0.8616  1.3451  0.9689  -0.2703 0.1967  -0.0172 392 ARG A CD  
5579  N NE  . ARG A 383 ? 1.2397  1.8057  1.4039  -0.2860 0.2187  -0.0261 392 ARG A NE  
5580  C CZ  . ARG A 383 ? 1.0784  1.6875  1.2970  -0.2650 0.2121  -0.0759 392 ARG A CZ  
5590  N N   . SER A 384 ? 0.7084  1.1349  0.8983  -0.1498 0.0854  -0.1887 393 SER A N   
5591  C CA  . SER A 384 ? 0.9664  1.4606  1.2208  -0.1309 0.0831  -0.2455 393 SER A CA  
5592  C C   . SER A 384 ? 0.9938  1.4182  1.2759  -0.1025 0.0340  -0.2685 393 SER A C   
5593  O O   . SER A 384 ? 0.9139  1.3695  1.2504  -0.0934 0.0307  -0.2970 393 SER A O   
5594  C CB  . SER A 384 ? 0.6853  1.2610  0.9534  -0.1091 0.0850  -0.3049 393 SER A CB  
5597  N N   . THR A 385 ? 0.8561  1.1872  1.1032  -0.0903 -0.0062 -0.2528 394 THR A N   
5598  C CA  . THR A 385 ? 0.6741  0.9350  0.9388  -0.0665 -0.0564 -0.2647 394 THR A CA  
5599  C C   . THR A 385 ? 0.7582  0.9800  1.0085  -0.0795 -0.0500 -0.2208 394 THR A C   
5600  O O   . THR A 385 ? 0.9432  1.1436  1.2235  -0.0610 -0.0776 -0.2405 394 THR A O   
5601  C CB  . THR A 385 ? 0.7565  0.9395  0.9933  -0.0541 -0.1038 -0.2563 394 THR A CB  
5602  O OG1 . THR A 385 ? 0.9909  1.2172  1.2552  -0.0333 -0.1179 -0.3139 394 THR A OG1 
5603  C CG2 . THR A 385 ? 0.7412  0.8437  0.9867  -0.0348 -0.1608 -0.2542 394 THR A CG2 
5611  N N   . THR A 386 ? 0.8791  1.0935  1.0863  -0.1075 -0.0177 -0.1669 395 THR A N   
5612  C CA  . THR A 386 ? 0.9088  1.0999  1.1088  -0.1155 -0.0120 -0.1353 395 THR A CA  
5613  C C   . THR A 386 ? 0.9098  1.1644  1.1687  -0.1223 0.0096  -0.1579 395 THR A C   
5614  O O   . THR A 386 ? 0.9195  1.1578  1.2084  -0.1076 -0.0114 -0.1721 395 THR A O   
5615  C CB  . THR A 386 ? 0.8581  1.0265  1.0027  -0.1391 0.0101  -0.0789 395 THR A CB  
5616  O OG1 . THR A 386 ? 0.8194  0.9331  0.9202  -0.1335 -0.0137 -0.0572 395 THR A OG1 
5617  C CG2 . THR A 386 ? 0.8948  1.0438  1.0339  -0.1415 0.0112  -0.0541 395 THR A CG2 
5625  N N   . GLU A 387 ? 1.0355  1.3674  1.3155  -0.1444 0.0483  -0.1618 396 GLU A N   
5626  C CA  . GLU A 387 ? 0.8882  1.2895  1.2341  -0.1572 0.0682  -0.1764 396 GLU A CA  
5627  C C   . GLU A 387 ? 0.8678  1.2926  1.2763  -0.1273 0.0423  -0.2366 396 GLU A C   
5628  O O   . GLU A 387 ? 0.8270  1.2626  1.2879  -0.1262 0.0349  -0.2467 396 GLU A O   
5629  C CB  . GLU A 387 ? 0.8761  1.3714  1.2333  -0.1887 0.1148  -0.1665 396 GLU A CB  
5632  N N   . LYS A 388 ? 0.7754  1.2036  1.1849  -0.0999 0.0211  -0.2806 397 LYS A N   
5633  C CA  . LYS A 388 ? 0.7535  1.2002  1.2277  -0.0681 -0.0104 -0.3420 397 LYS A CA  
5634  C C   . LYS A 388 ? 0.7137  1.0628  1.1780  -0.0449 -0.0603 -0.3380 397 LYS A C   
5635  O O   . LYS A 388 ? 0.9007  1.2551  1.4193  -0.0191 -0.0909 -0.3846 397 LYS A O   
5636  C CB  . LYS A 388 ? 0.6413  1.1237  1.1321  -0.0397 -0.0281 -0.4012 397 LYS A CB  
5639  N N   . SER A 389 ? 0.9600  1.2298  1.3584  -0.0529 -0.0685 -0.2844 398 SER A N   
5640  C CA  . SER A 389 ? 0.9075  1.0976  1.2868  -0.0308 -0.1131 -0.2766 398 SER A CA  
5641  C C   . SER A 389 ? 1.0321  1.2277  1.4387  -0.0339 -0.1090 -0.2702 398 SER A C   
5642  O O   . SER A 389 ? 0.6684  0.8047  1.0517  -0.0143 -0.1433 -0.2620 398 SER A O   
5643  C CB  . SER A 389 ? 1.0403  1.1582  1.3364  -0.0362 -0.1236 -0.2230 398 SER A CB  
5646  N N   . LEU A 390 ? 0.8036  1.0711  1.2598  -0.0587 -0.0709 -0.2718 399 LEU A N   
5647  C CA  . LEU A 390 ? 0.6909  0.9723  1.1944  -0.0666 -0.0697 -0.2683 399 LEU A CA  
5648  C C   . LEU A 390 ? 0.9256  1.2370  1.5133  -0.0457 -0.0945 -0.3228 399 LEU A C   
5649  O O   . LEU A 390 ? 0.8308  1.1827  1.4570  -0.0312 -0.1000 -0.3685 399 LEU A O   
5650  C CB  . LEU A 390 ? 0.7627  1.1107  1.2937  -0.1094 -0.0228 -0.2392 399 LEU A CB  
5651  C CG  . LEU A 390 ? 0.9224  1.2413  1.3865  -0.1342 -0.0009 -0.1818 399 LEU A CG  
5652  C CD1 . LEU A 390 ? 1.0632  1.4533  1.5509  -0.1769 0.0428  -0.1554 399 LEU A CD1 
5653  C CD2 . LEU A 390 ? 0.8078  1.0685  1.2578  -0.1265 -0.0251 -0.1605 399 LEU A CD2 
5665  N N   . LEU A 391 ? 0.9513  1.2497  1.5758  -0.0441 -0.1103 -0.3211 400 LEU A N   
5666  C CA  . LEU A 391 ? 1.1698  1.4861  1.8771  -0.0234 -0.1404 -0.3693 400 LEU A CA  
5667  C C   . LEU A 391 ? 0.9861  1.3901  1.7934  -0.0556 -0.1133 -0.3732 400 LEU A C   
5668  O O   . LEU A 391 ? 1.0909  1.5741  1.9717  -0.0567 -0.1025 -0.4127 400 LEU A O   
5669  C CB  . LEU A 391 ? 1.3495  1.5815  2.0247  0.0086  -0.1893 -0.3690 400 LEU A CB  
5670  C CG  . LEU A 391 ? 0.6825  0.8352  1.2540  0.0338  -0.2146 -0.3507 400 LEU A CG  
5671  C CD1 . LEU A 391 ? 0.7025  0.7940  1.2437  0.0653  -0.2588 -0.3516 400 LEU A CD1 
5672  C CD2 . LEU A 391 ? 1.2806  1.4213  1.8471  0.0545  -0.2372 -0.3809 400 LEU A CD2 
5684  N N   . LYS A 392 ? 0.9419  1.3397  1.7614  -0.0823 -0.1050 -0.3339 401 LYS A N   
5685  C CA  . LYS A 392 ? 0.9505  1.4310  1.8758  -0.1191 -0.0853 -0.3295 401 LYS A CA  
5686  C C   . LYS A 392 ? 1.1189  1.6714  2.0310  -0.1675 -0.0278 -0.2859 401 LYS A C   
5687  O O   . LYS A 392 ? 1.3367  1.8850  2.2454  -0.2035 -0.0141 -0.2343 401 LYS A O   
5688  C CB  . LYS A 392 ? 0.7231  1.1589  1.6918  -0.1227 -0.1196 -0.3143 401 LYS A CB  
5691  N N   . MET B 1   ? 1.9044  2.0387  1.3754  0.0602  0.1729  -0.0309 10  MET B N   
5692  C CA  . MET B 1   ? 1.5753  1.7180  1.0874  0.0401  0.1526  -0.0493 10  MET B CA  
5693  C C   . MET B 1   ? 1.3474  1.4186  0.8840  -0.0155 0.1515  -0.0984 10  MET B C   
5694  O O   . MET B 1   ? 1.4437  1.4840  0.9580  -0.0415 0.1605  -0.1340 10  MET B O   
5695  C CB  . MET B 1   ? 1.7630  2.0210  1.2486  0.0504  0.1265  -0.0784 10  MET B CB  
5697  N N   . ILE B 2   ? 1.2000  1.2438  0.7849  -0.0295 0.1437  -0.0949 11  ILE B N   
5698  C CA  . ILE B 2   ? 1.6622  1.6504  1.2759  -0.0773 0.1414  -0.1338 11  ILE B CA  
5699  C C   . ILE B 2   ? 1.4616  1.5124  1.0664  -0.1048 0.1220  -0.1944 11  ILE B C   
5700  O O   . ILE B 2   ? 1.6509  1.7908  1.2433  -0.0863 0.1041  -0.2009 11  ILE B O   
5701  C CB  . ILE B 2   ? 2.5681  2.5110  2.2317  -0.0755 0.1408  -0.1051 11  ILE B CB  
5702  C CG1 . ILE B 2   ? 1.5910  1.4617  1.2722  -0.0579 0.1590  -0.0514 11  ILE B CG1 
5703  C CG2 . ILE B 2   ? 1.1563  1.0632  0.8453  -0.1198 0.1362  -0.1451 11  ILE B CG2 
5704  C CD1 . ILE B 2   ? 1.9366  1.7645  1.6642  -0.0516 0.1579  -0.0238 11  ILE B CD1 
5716  N N   . SER B 3   ? 1.3930  1.3985  1.0120  -0.1498 0.1256  -0.2353 12  SER B N   
5717  C CA  . SER B 3   ? 1.7170  1.7715  1.3494  -0.1770 0.1069  -0.2852 12  SER B CA  
5718  C C   . SER B 3   ? 1.9389  2.0441  1.5975  -0.1804 0.0905  -0.2937 12  SER B C   
5719  O O   . SER B 3   ? 1.3549  1.4220  1.0414  -0.1788 0.0960  -0.2710 12  SER B O   
5720  C CB  . SER B 3   ? 1.4138  1.4080  1.0975  -0.2061 0.1119  -0.2901 12  SER B CB  
5721  O OG  . SER B 3   ? 1.5541  1.5922  1.2724  -0.2219 0.0960  -0.3160 12  SER B OG  
5727  N N   . LYS B 4   ? 1.2249  1.4134  0.8892  -0.1801 0.0680  -0.3176 13  LYS B N   
5728  C CA  . LYS B 4   ? 1.0437  1.2956  0.7326  -0.1809 0.0524  -0.3255 13  LYS B CA  
5729  C C   . LYS B 4   ? 1.1632  1.3704  0.9127  -0.2107 0.0557  -0.3313 13  LYS B C   
5730  O O   . LYS B 4   ? 1.0513  1.2837  0.8209  -0.2106 0.0516  -0.3311 13  LYS B O   
5731  C CB  . LYS B 4   ? 1.9709  2.3267  1.6536  -0.1740 0.0274  -0.3467 13  LYS B CB  
5734  N N   . GLU B 5   ? 1.4332  1.5789  1.2103  -0.2301 0.0664  -0.3298 14  GLU B N   
5735  C CA  . GLU B 5   ? 1.2519  1.3679  1.0813  -0.2472 0.0736  -0.3220 14  GLU B CA  
5736  C C   . GLU B 5   ? 1.1781  1.2374  1.0141  -0.2412 0.0854  -0.2946 14  GLU B C   
5737  O O   . GLU B 5   ? 1.3115  1.3549  1.1827  -0.2473 0.0909  -0.2839 14  GLU B O   
5738  C CB  . GLU B 5   ? 1.0586  1.1400  0.9117  -0.2607 0.0843  -0.3209 14  GLU B CB  
5739  C CG  . GLU B 5   ? 2.1659  2.1853  2.0031  -0.2558 0.0992  -0.3015 14  GLU B CG  
5746  N N   . TYR B 6   ? 1.4569  1.4857  1.2560  -0.2269 0.0910  -0.2828 15  TYR B N   
5747  C CA  . TYR B 6   ? 1.6569  1.6289  1.4633  -0.2221 0.1010  -0.2609 15  TYR B CA  
5748  C C   . TYR B 6   ? 1.2384  1.2450  1.0390  -0.2024 0.0957  -0.2600 15  TYR B C   
5749  O O   . TYR B 6   ? 1.2337  1.1913  1.0508  -0.1923 0.1027  -0.2373 15  TYR B O   
5750  C CB  . TYR B 6   ? 1.9902  1.8897  1.7720  -0.2155 0.1159  -0.2376 15  TYR B CB  
5751  C CG  . TYR B 6   ? 1.8016  1.6715  1.6075  -0.2229 0.1224  -0.2195 15  TYR B CG  
5752  C CD1 . TYR B 6   ? 1.4958  1.3568  1.3412  -0.2218 0.1234  -0.1993 15  TYR B CD1 
5753  C CD2 . TYR B 6   ? 0.9250  0.7854  0.7042  -0.2236 0.1296  -0.2230 15  TYR B CD2 
5754  C CE1 . TYR B 6   ? 1.1207  0.9694  0.9772  -0.2200 0.1302  -0.1845 15  TYR B CE1 
5755  C CE2 . TYR B 6   ? 1.0280  0.8671  0.8263  -0.2283 0.1387  -0.2089 15  TYR B CE2 
5756  C CZ  . TYR B 6   ? 1.0571  0.8935  0.8935  -0.2250 0.1390  -0.1892 15  TYR B CZ  
5757  O OH  . TYR B 6   ? 1.2210  1.0451  1.0667  -0.2227 0.1485  -0.1772 15  TYR B OH  
5767  N N   . HIS B 7   ? 1.3020  1.3975  1.0969  -0.1834 0.0808  -0.2646 16  HIS B N   
5768  C CA  . HIS B 7   ? 1.1020  1.2449  0.9170  -0.1508 0.0741  -0.2420 16  HIS B CA  
5769  C C   . HIS B 7   ? 1.3443  1.4366  1.1612  -0.1134 0.0848  -0.1936 16  HIS B C   
5770  O O   . HIS B 7   ? 1.0914  1.1600  0.9338  -0.0994 0.0898  -0.1781 16  HIS B O   
5771  C CB  . HIS B 7   ? 1.1301  1.2757  0.9799  -0.1690 0.0747  -0.2599 16  HIS B CB  
5772  C CG  . HIS B 7   ? 1.0712  1.2687  0.9334  -0.2060 0.0655  -0.3035 16  HIS B CG  
5773  N ND1 . HIS B 7   ? 1.0854  1.3549  0.9334  -0.2136 0.0499  -0.3273 16  HIS B ND1 
5774  C CD2 . HIS B 7   ? 1.1134  1.3044  1.0070  -0.2351 0.0698  -0.3238 16  HIS B CD2 
5775  C CE1 . HIS B 7   ? 1.1108  1.4033  0.9950  -0.2409 0.0459  -0.3483 16  HIS B CE1 
5776  N NE2 . HIS B 7   ? 1.1616  1.4086  1.0763  -0.2495 0.0594  -0.3386 16  HIS B NE2 
5783  N N   . ILE B 8   ? 1.3563  1.4319  1.1484  -0.0966 0.0895  -0.1698 17  ILE B N   
5784  C CA  . ILE B 8   ? 0.9199  0.9642  0.7203  -0.0570 0.0989  -0.1189 17  ILE B CA  
5785  C C   . ILE B 8   ? 0.9242  1.0551  0.7094  -0.0176 0.0917  -0.0937 17  ILE B C   
5786  O O   . ILE B 8   ? 0.9858  1.1675  0.7365  -0.0222 0.0842  -0.1100 17  ILE B O   
5787  C CB  . ILE B 8   ? 0.9794  0.9350  0.7725  -0.0638 0.1132  -0.0992 17  ILE B CB  
5788  C CG1 . ILE B 8   ? 1.2082  1.0828  1.0197  -0.0984 0.1190  -0.1174 17  ILE B CG1 
5789  C CG2 . ILE B 8   ? 0.8190  0.7578  0.6267  -0.0208 0.1220  -0.0443 17  ILE B CG2 
5790  C CD1 . ILE B 8   ? 1.9673  1.7684  1.7718  -0.1157 0.1298  -0.1079 17  ILE B CD1 
5802  N N   . ASP B 9   ? 1.0231  1.1740  0.8342  0.0214  0.0943  -0.0559 18  ASP B N   
5803  C CA  . ASP B 9   ? 1.5392  1.7844  1.3435  0.0631  0.0875  -0.0262 18  ASP B CA  
5804  C C   . ASP B 9   ? 1.1035  1.3268  0.8995  0.0984  0.1013  0.0266  18  ASP B C   
5805  O O   . ASP B 9   ? 1.0481  1.1847  0.8695  0.1042  0.1173  0.0546  18  ASP B O   
5806  C CB  . ASP B 9   ? 1.3542  1.6359  1.1986  0.0900  0.0867  -0.0081 18  ASP B CB  
5807  C CG  . ASP B 9   ? 0.8351  1.2255  0.6760  0.1319  0.0784  0.0233  18  ASP B CG  
5808  O OD1 . ASP B 9   ? 1.4222  1.9032  1.2402  0.1194  0.0585  -0.0069 18  ASP B OD1 
5809  O OD2 . ASP B 9   ? 0.9948  1.3826  0.8565  0.1768  0.0914  0.0788  18  ASP B OD2 
5814  N N   . GLU B 10  ? 1.2912  1.5966  1.0528  0.1218  0.0950  0.0404  19  GLU B N   
5815  C CA  . GLU B 10  ? 1.4031  1.6998  1.1577  0.1606  0.1105  0.0971  19  GLU B CA  
5816  C C   . GLU B 10  ? 1.5213  1.7980  1.3289  0.2025  0.1248  0.1563  19  GLU B C   
5817  O O   . GLU B 10  ? 1.3843  1.5951  1.2128  0.2195  0.1438  0.2000  19  GLU B O   
5818  C CB  . GLU B 10  ? 1.5423  1.9486  1.2479  0.1842  0.1000  0.1019  19  GLU B CB  
5821  N N   . GLU B 11  ? 1.6497  1.9753  1.4863  0.2173  0.1176  0.1575  20  GLU B N   
5822  C CA  . GLU B 11  ? 1.4681  1.7746  1.3592  0.2591  0.1336  0.2116  20  GLU B CA  
5823  C C   . GLU B 11  ? 1.3066  1.5011  1.2407  0.2383  0.1441  0.1973  20  GLU B C   
5824  O O   . GLU B 11  ? 1.6870  1.8044  1.6564  0.2538  0.1622  0.2343  20  GLU B O   
5825  C CB  . GLU B 11  ? 1.5301  1.9516  1.4332  0.2923  0.1236  0.2267  20  GLU B CB  
5826  C CG  . GLU B 11  ? 1.6822  2.0986  1.6436  0.3431  0.1429  0.2890  20  GLU B CG  
5833  N N   . VAL B 12  ? 1.2941  1.4820  1.2279  0.2047  0.1333  0.1448  21  VAL B N   
5834  C CA  . VAL B 12  ? 1.0631  1.1658  1.0336  0.1919  0.1420  0.1294  21  VAL B CA  
5835  C C   . VAL B 12  ? 0.7722  0.7884  0.7251  0.1397  0.1394  0.0840  21  VAL B C   
5836  O O   . VAL B 12  ? 0.8633  0.8198  0.8356  0.1231  0.1428  0.0604  21  VAL B O   
5837  C CB  . VAL B 12  ? 1.1024  1.2634  1.0914  0.1987  0.1361  0.1101  21  VAL B CB  
5838  C CG1 . VAL B 12  ? 0.8289  1.0805  0.8425  0.2534  0.1397  0.1599  21  VAL B CG1 
5839  C CG2 . VAL B 12  ? 0.8347  1.0495  0.7903  0.1564  0.1162  0.0534  21  VAL B CG2 
5849  N N   . GLY B 13  ? 0.7619  0.7764  0.6767  0.1134  0.1335  0.0685  22  GLY B N   
5850  C CA  . GLY B 13  ? 0.7382  0.6730  0.6422  0.0675  0.1333  0.0333  22  GLY B CA  
5851  C C   . GLY B 13  ? 1.2475  1.1870  1.1450  0.0301  0.1241  -0.0200 22  GLY B C   
5852  O O   . GLY B 13  ? 0.7388  0.7472  0.6155  0.0136  0.1123  -0.0504 22  GLY B O   
5856  N N   . PHE B 14  ? 0.8360  0.6985  0.7523  0.0141  0.1298  -0.0324 23  PHE B N   
5857  C CA  . PHE B 14  ? 0.9462  0.8060  0.8582  -0.0198 0.1249  -0.0778 23  PHE B CA  
5858  C C   . PHE B 14  ? 1.1869  1.0995  1.1190  -0.0004 0.1241  -0.0846 23  PHE B C   
5859  O O   . PHE B 14  ? 1.0539  0.9887  0.9847  -0.0236 0.1204  -0.1188 23  PHE B O   
5860  C CB  . PHE B 14  ? 1.0744  0.8389  0.9933  -0.0430 0.1307  -0.0888 23  PHE B CB  
5861  C CG  . PHE B 14  ? 1.4301  1.1467  1.3323  -0.0709 0.1311  -0.0893 23  PHE B CG  
5862  C CD1 . PHE B 14  ? 1.3983  1.1344  1.2783  -0.1054 0.1271  -0.1187 23  PHE B CD1 
5863  C CD2 . PHE B 14  ? 1.4807  1.1321  1.3953  -0.0628 0.1370  -0.0588 23  PHE B CD2 
5864  C CE1 . PHE B 14  ? 1.0182  0.7103  0.8857  -0.1290 0.1303  -0.1172 23  PHE B CE1 
5865  C CE2 . PHE B 14  ? 1.1400  0.7498  1.0428  -0.0879 0.1387  -0.0562 23  PHE B CE2 
5866  C CZ  . PHE B 14  ? 0.9734  0.6026  0.8515  -0.1193 0.1362  -0.0840 23  PHE B CZ  
5876  N N   . ALA B 15  ? 1.0979  1.0316  1.0530  0.0434  0.1298  -0.0489 24  ALA B N   
5877  C CA  . ALA B 15  ? 1.2260  1.2182  1.2030  0.0666  0.1308  -0.0499 24  ALA B CA  
5878  C C   . ALA B 15  ? 1.2515  1.3515  1.2147  0.0568  0.1156  -0.0674 24  ALA B C   
5879  O O   . ALA B 15  ? 1.0462  1.1805  0.9823  0.0429  0.1050  -0.0718 24  ALA B O   
5880  C CB  . ALA B 15  ? 1.2927  1.2888  1.3013  0.1180  0.1421  -0.0019 24  ALA B CB  
5886  N N   . LEU B 16  ? 1.1399  1.2918  1.1233  0.0628  0.1149  -0.0802 25  LEU B N   
5887  C CA  . LEU B 16  ? 1.0340  1.2959  1.0169  0.0558  0.0993  -0.0949 25  LEU B CA  
5888  C C   . LEU B 16  ? 1.0894  1.4360  1.0842  0.1016  0.0947  -0.0540 25  LEU B C   
5889  O O   . LEU B 16  ? 1.3132  1.6564  1.3386  0.1417  0.1080  -0.0218 25  LEU B O   
5890  C CB  . LEU B 16  ? 0.8136  1.0957  0.8199  0.0444  0.1028  -0.1201 25  LEU B CB  
5891  C CG  . LEU B 16  ? 0.8659  1.2515  0.8804  0.0240  0.0864  -0.1440 25  LEU B CG  
5892  C CD1 . LEU B 16  ? 0.8167  1.1955  0.8040  -0.0233 0.0743  -0.1781 25  LEU B CD1 
5893  C CD2 . LEU B 16  ? 1.2305  1.6228  1.2744  0.0191  0.0968  -0.1600 25  LEU B CD2 
5905  N N   . PRO B 17  ? 1.4261  1.8483  1.3975  0.0995  0.0777  -0.0526 26  PRO B N   
5906  C CA  . PRO B 17  ? 1.3590  1.8603  1.3375  0.1477  0.0747  -0.0062 26  PRO B CA  
5907  C C   . PRO B 17  ? 1.6477  2.2583  1.6576  0.1662  0.0657  -0.0013 26  PRO B C   
5908  O O   . PRO B 17  ? 2.0574  2.7304  2.0666  0.1348  0.0485  -0.0392 26  PRO B O   
5909  C CB  . PRO B 17  ? 1.2198  1.7621  1.1532  0.1350  0.0588  -0.0138 26  PRO B CB  
5910  C CG  . PRO B 17  ? 0.8978  1.4251  0.8124  0.0779  0.0475  -0.0736 26  PRO B CG  
5911  C CD  . PRO B 17  ? 0.9038  1.3347  0.8389  0.0564  0.0631  -0.0907 26  PRO B CD  
5919  N N   . ASN B 18  ? 1.9702  2.6044  2.0139  0.2183  0.0787  0.0483  27  ASN B N   
5920  C CA  . ASN B 18  ? 1.5650  2.3003  1.6470  0.2445  0.0749  0.0638  27  ASN B CA  
5921  C C   . ASN B 18  ? 1.3328  2.0720  1.4302  0.2075  0.0713  0.0168  27  ASN B C   
5922  O O   . ASN B 18  ? 1.5280  2.3582  1.6238  0.1821  0.0488  -0.0100 27  ASN B O   
5923  C CB  . ASN B 18  ? 1.6191  2.4932  1.6883  0.2598  0.0502  0.0809  27  ASN B CB  
5924  C CG  . ASN B 18  ? 1.3192  2.2049  1.3788  0.3070  0.0578  0.1390  27  ASN B CG  
5929  N N   . PRO B 19  ? 0.9366  1.5808  1.0497  0.2029  0.0930  0.0053  28  PRO B N   
5930  C CA  . PRO B 19  ? 0.9753  1.6234  1.1024  0.1711  0.0934  -0.0346 28  PRO B CA  
5931  C C   . PRO B 19  ? 0.8703  1.6188  1.0435  0.1981  0.0946  -0.0180 28  PRO B C   
5932  O O   . PRO B 19  ? 0.9729  1.7451  1.1757  0.2488  0.1081  0.0258  28  PRO B O   
5933  C CB  . PRO B 19  ? 1.8843  2.4003  2.0080  0.1673  0.1178  -0.0455 28  PRO B CB  
5934  C CG  . PRO B 19  ? 1.2599  1.7328  1.3972  0.2153  0.1345  -0.0007 28  PRO B CG  
5935  C CD  . PRO B 19  ? 0.7705  1.3063  0.8940  0.2307  0.1191  0.0304  28  PRO B CD  
5943  N N   . GLN B 20  ? 0.9652  1.7683  1.1504  0.1635  0.0833  -0.0518 29  GLN B N   
5944  C CA  . GLN B 20  ? 1.3199  2.2360  1.5523  0.1828  0.0799  -0.0372 29  GLN B CA  
5945  C C   . GLN B 20  ? 1.3204  2.1942  1.5861  0.2223  0.1122  -0.0153 29  GLN B C   
5946  O O   . GLN B 20  ? 0.9439  1.7056  1.1954  0.2161  0.1335  -0.0320 29  GLN B O   
5947  C CB  . GLN B 20  ? 1.6482  2.6256  1.8931  0.1325  0.0620  -0.0792 29  GLN B CB  
5948  C CG  . GLN B 20  ? 1.7030  2.8262  1.9985  0.1456  0.0477  -0.0637 29  GLN B CG  
5949  C CD  . GLN B 20  ? 1.5695  2.7702  1.8737  0.0914  0.0183  -0.1046 29  GLN B CD  
5950  O OE1 . GLN B 20  ? 1.6220  2.7930  1.8875  0.0535  0.0018  -0.1366 29  GLN B OE1 
5951  N NE2 . GLN B 20  ? 1.7886  3.0896  2.1483  0.0876  0.0125  -0.1032 29  GLN B NE2 
5960  N N   . GLU B 21  ? 1.3744  2.3373  1.6829  0.2672  0.1164  0.0247  30  GLU B N   
5961  C CA  . GLU B 21  ? 1.4131  2.3457  1.7583  0.3099  0.1495  0.0470  30  GLU B CA  
5962  C C   . GLU B 21  ? 1.1420  2.1348  1.5244  0.3003  0.1558  0.0315  30  GLU B C   
5963  O O   . GLU B 21  ? 0.8176  1.7627  1.2196  0.3269  0.1871  0.0360  30  GLU B O   
5964  C CB  . GLU B 21  ? 1.5775  2.5687  1.9568  0.3717  0.1576  0.1074  30  GLU B CB  
5965  C CG  . GLU B 21  ? 1.1413  2.0772  1.4950  0.3916  0.1579  0.1349  30  GLU B CG  
5972  N N   . ASN B 22  ? 1.1251  2.2235  1.5209  0.2647  0.1280  0.0143  31  ASN B N   
5973  C CA  . ASN B 22  ? 1.0371  2.2143  1.4814  0.2580  0.1326  0.0086  31  ASN B CA  
5974  C C   . ASN B 22  ? 0.8933  2.1053  1.3345  0.1934  0.1087  -0.0361 31  ASN B C   
5975  O O   . ASN B 22  ? 0.7918  2.0419  1.2126  0.1618  0.0768  -0.0524 31  ASN B O   
5976  C CB  . ASN B 22  ? 0.9712  2.2909  1.4713  0.2977  0.1246  0.0539  31  ASN B CB  
5977  C CG  . ASN B 22  ? 0.9014  2.1955  1.4218  0.3657  0.1552  0.1031  31  ASN B CG  
5978  O OD1 . ASN B 22  ? 0.9013  2.1459  1.4427  0.3922  0.1902  0.1079  31  ASN B OD1 
5979  N ND2 . ASN B 22  ? 1.0883  2.4103  1.6010  0.3958  0.1444  0.1398  31  ASN B ND2 
5986  N N   . LEU B 23  ? 0.9383  2.1341  1.4007  0.1753  0.1269  -0.0560 32  LEU B N   
5987  C CA  . LEU B 23  ? 0.9513  2.1945  1.4334  0.1194  0.1109  -0.0900 32  LEU B CA  
5988  C C   . LEU B 23  ? 1.2738  2.6693  1.8264  0.1219  0.0967  -0.0727 32  LEU B C   
5989  O O   . LEU B 23  ? 1.0190  2.4753  1.6098  0.1709  0.1095  -0.0328 32  LEU B O   
5990  C CB  . LEU B 23  ? 0.8813  2.0350  1.3534  0.1013  0.1400  -0.1137 32  LEU B CB  
5993  N N   . PRO B 24  ? 0.9185  2.3773  1.4947  0.0690  0.0714  -0.1017 33  PRO B N   
5994  C CA  . PRO B 24  ? 0.8785  2.4827  1.5296  0.0630  0.0561  -0.0895 33  PRO B CA  
5995  C C   . PRO B 24  ? 1.1981  2.8329  1.9019  0.1015  0.0903  -0.0571 33  PRO B C   
5996  O O   . PRO B 24  ? 1.3787  2.9156  2.0616  0.1190  0.1276  -0.0574 33  PRO B O   
5997  C CB  . PRO B 24  ? 0.6072  2.2205  1.2746  -0.0069 0.0386  -0.1351 33  PRO B CB  
5998  C CG  . PRO B 24  ? 1.3654  2.8779  1.9641  -0.0343 0.0296  -0.1672 33  PRO B CG  
5999  C CD  . PRO B 24  ? 1.5695  2.9669  2.1117  0.0098  0.0574  -0.1482 33  PRO B CD  
6007  N N   . ASP B 25  ? 1.1416  2.6260  2.2910  -0.0576 -0.0167 -0.3999 34  ASP B N   
6008  C CA  . ASP B 25  ? 0.9231  2.4048  2.1031  -0.0524 -0.0075 -0.3662 34  ASP B CA  
6009  C C   . ASP B 25  ? 0.7400  2.1924  1.9498  -0.0546 0.0146  -0.3543 34  ASP B C   
6010  O O   . ASP B 25  ? 0.6610  2.0993  1.8797  -0.0435 0.0311  -0.3234 34  ASP B O   
6011  C CB  . ASP B 25  ? 1.3097  2.8345  2.5348  -0.0605 -0.0261 -0.3658 34  ASP B CB  
6012  C CG  . ASP B 25  ? 1.0699  2.6213  2.2652  -0.0552 -0.0458 -0.3691 34  ASP B CG  
6013  O OD1 . ASP B 25  ? 0.8133  2.3498  1.9593  -0.0419 -0.0413 -0.3592 34  ASP B OD1 
6014  O OD2 . ASP B 25  ? 1.0993  2.6864  2.3206  -0.0658 -0.0675 -0.3810 34  ASP B OD2 
6019  N N   . PHE B 26  ? 0.6603  2.1012  1.8800  -0.0663 0.0169  -0.3794 35  PHE B N   
6020  C CA  . PHE B 26  ? 1.8191  3.2309  3.0661  -0.0696 0.0371  -0.3694 35  PHE B CA  
6021  C C   . PHE B 26  ? 0.9789  2.3503  2.1942  -0.0544 0.0597  -0.3412 35  PHE B C   
6022  O O   . PHE B 26  ? 0.5492  1.9021  1.7877  -0.0508 0.0781  -0.3194 35  PHE B O   
6023  C CB  . PHE B 26  ? 0.5877  1.9894  1.8387  -0.0824 0.0356  -0.4056 35  PHE B CB  
6024  C CG  . PHE B 26  ? 0.9462  2.3222  2.2317  -0.0896 0.0524  -0.4002 35  PHE B CG  
6025  C CD1 . PHE B 26  ? 0.6048  2.0034  1.9504  -0.1052 0.0439  -0.4029 35  PHE B CD1 
6026  C CD2 . PHE B 26  ? 0.5744  1.9049  1.8341  -0.0824 0.0748  -0.3900 35  PHE B CD2 
6027  C CE1 . PHE B 26  ? 0.6070  1.9836  1.9854  -0.1127 0.0586  -0.3964 35  PHE B CE1 
6028  C CE2 . PHE B 26  ? 0.9681  2.2736  2.2575  -0.0888 0.0902  -0.3853 35  PHE B CE2 
6029  C CZ  . PHE B 26  ? 0.5929  1.9217  1.9413  -0.1036 0.0826  -0.3892 35  PHE B CZ  
6039  N N   . TYR B 27  ? 1.2800  2.6386  2.4428  -0.0463 0.0580  -0.3412 36  TYR B N   
6040  C CA  . TYR B 27  ? 1.0746  2.3950  2.2063  -0.0355 0.0750  -0.3177 36  TYR B CA  
6041  C C   . TYR B 27  ? 2.0910  3.4183  3.2078  -0.0212 0.0740  -0.2926 36  TYR B C   
6042  O O   . TYR B 27  ? 1.9134  3.2175  2.9956  -0.0131 0.0800  -0.2779 36  TYR B O   
6043  C CB  . TYR B 27  ? 0.6718  1.9763  1.7608  -0.0373 0.0732  -0.3293 36  TYR B CB  
6044  C CG  . TYR B 27  ? 0.6647  1.9607  1.7695  -0.0477 0.0782  -0.3545 36  TYR B CG  
6045  C CD1 . TYR B 27  ? 0.5283  1.7882  1.6475  -0.0500 0.0972  -0.3468 36  TYR B CD1 
6046  C CD2 . TYR B 27  ? 0.7964  2.1226  1.9038  -0.0545 0.0637  -0.3886 36  TYR B CD2 
6047  C CE1 . TYR B 27  ? 0.5387  1.7900  1.6736  -0.0594 0.1018  -0.3719 36  TYR B CE1 
6048  C CE2 . TYR B 27  ? 0.8031  2.1243  1.9285  -0.0629 0.0683  -0.4170 36  TYR B CE2 
6049  C CZ  . TYR B 27  ? 0.5546  1.8371  1.6946  -0.0660 0.0875  -0.4085 36  TYR B CZ  
6050  O OH  . TYR B 27  ? 0.6955  1.9713  1.8548  -0.0745 0.0923  -0.4384 36  TYR B OH  
6060  N N   . ASN B 28  ? 1.8799  3.2406  3.0252  -0.0179 0.0664  -0.2869 37  ASN B N   
6061  C CA  . ASN B 28  ? 1.2254  2.5962  2.3545  -0.0022 0.0646  -0.2671 37  ASN B CA  
6062  C C   . ASN B 28  ? 0.9028  2.2436  2.0271  0.0134  0.0878  -0.2424 37  ASN B C   
6063  O O   . ASN B 28  ? 0.6296  1.9728  1.7288  0.0283  0.0868  -0.2300 37  ASN B O   
6064  C CB  . ASN B 28  ? 0.9667  2.3803  2.1341  -0.0005 0.0546  -0.2628 37  ASN B CB  
6065  C CG  . ASN B 28  ? 1.2972  2.7414  2.4548  -0.0126 0.0282  -0.2875 37  ASN B CG  
6066  O OD1 . ASN B 28  ? 1.4669  2.9032  2.5803  -0.0164 0.0182  -0.3040 37  ASN B OD1 
6067  N ND2 . ASN B 28  ? 1.4501  2.9320  2.6509  -0.0182 0.0168  -0.2880 37  ASN B ND2 
6074  N N   . ASP B 29  ? 0.7714  2.0857  1.9174  0.0117  0.1080  -0.2364 38  ASP B N   
6075  C CA  . ASP B 29  ? 1.3287  2.6120  2.4649  0.0281  0.1312  -0.2150 38  ASP B CA  
6076  C C   . ASP B 29  ? 0.7528  2.0028  1.8413  0.0249  0.1298  -0.2185 38  ASP B C   
6077  O O   . ASP B 29  ? 0.7347  1.9718  1.8003  0.0393  0.1373  -0.2052 38  ASP B O   
6078  C CB  . ASP B 29  ? 0.9196  2.1866  2.0921  0.0291  0.1543  -0.2042 38  ASP B CB  
6079  C CG  . ASP B 29  ? 0.7278  2.0256  1.9466  0.0449  0.1672  -0.1813 38  ASP B CG  
6080  O OD1 . ASP B 29  ? 0.6148  1.9340  1.8310  0.0623  0.1659  -0.1702 38  ASP B OD1 
6081  O OD2 . ASP B 29  ? 1.4849  2.7870  2.7420  0.0417  0.1798  -0.1722 38  ASP B OD2 
6086  N N   . TRP B 30  ? 0.9913  2.2306  2.0665  0.0074  0.1208  -0.2354 39  TRP B N   
6087  C CA  . TRP B 30  ? 0.9387  2.1562  1.9726  0.0032  0.1166  -0.2335 39  TRP B CA  
6088  C C   . TRP B 30  ? 1.3589  2.6025  2.3601  0.0066  0.0954  -0.2316 39  TRP B C   
6089  O O   . TRP B 30  ? 1.0243  2.2613  1.9981  0.0127  0.0932  -0.2178 39  TRP B O   
6090  C CB  . TRP B 30  ? 0.6566  1.8641  1.6857  -0.0122 0.1134  -0.2502 39  TRP B CB  
6091  C CG  . TRP B 30  ? 0.4828  1.6601  1.5342  -0.0179 0.1318  -0.2540 39  TRP B CG  
6092  C CD1 . TRP B 30  ? 0.5156  1.6721  1.5887  -0.0115 0.1511  -0.2416 39  TRP B CD1 
6093  C CD2 . TRP B 30  ? 0.4872  1.6542  1.5389  -0.0293 0.1326  -0.2721 39  TRP B CD2 
6094  N NE1 . TRP B 30  ? 0.5406  1.6730  1.6265  -0.0206 0.1616  -0.2506 39  TRP B NE1 
6095  C CE2 . TRP B 30  ? 0.5380  1.6758  1.6117  -0.0314 0.1506  -0.2704 39  TRP B CE2 
6096  C CE3 . TRP B 30  ? 0.4903  1.6725  1.5254  -0.0356 0.1212  -0.2897 39  TRP B CE3 
6097  C CZ2 . TRP B 30  ? 0.8937  2.0146  1.9734  -0.0411 0.1561  -0.2877 39  TRP B CZ2 
6098  C CZ3 . TRP B 30  ? 0.4970  1.6652  1.5399  -0.0426 0.1291  -0.3068 39  TRP B CZ3 
6099  C CH2 . TRP B 30  ? 0.5474  1.6840  1.6122  -0.0460 0.1456  -0.3064 39  TRP B CH2 
6110  N N   . MET B 31  ? 2.6506  3.9273  3.6542  0.0027  0.0781  -0.2457 40  MET B N   
6111  C CA  . MET B 31  ? 0.6106  1.9131  1.5793  0.0048  0.0561  -0.2447 40  MET B CA  
6112  C C   . MET B 31  ? 1.4237  2.7325  2.3795  0.0207  0.0555  -0.2272 40  MET B C   
6113  O O   . MET B 31  ? 0.4756  1.7967  1.3924  0.0228  0.0382  -0.2193 40  MET B O   
6114  C CB  . MET B 31  ? 1.5850  2.9223  2.5661  0.0007  0.0412  -0.2632 40  MET B CB  
6115  C CG  . MET B 31  ? 2.3572  3.7203  3.2997  -0.0010 0.0182  -0.2683 40  MET B CG  
6116  S SD  . MET B 31  ? 1.4906  2.8497  2.4080  -0.0114 0.0147  -0.2795 40  MET B SD  
6117  C CE  . MET B 31  ? 0.4866  1.8388  1.3569  -0.0093 0.0052  -0.2514 40  MET B CE  
6127  N N   . PHE B 32  ? 1.0394  2.3454  2.0270  0.0342  0.0734  -0.2200 41  PHE B N   
6128  C CA  . PHE B 32  ? 0.8444  2.1637  1.8187  0.0561  0.0746  -0.2060 41  PHE B CA  
6129  C C   . PHE B 32  ? 1.1018  2.3998  2.0445  0.0633  0.0798  -0.1941 41  PHE B C   
6130  O O   . PHE B 32  ? 0.4758  1.7925  1.3778  0.0710  0.0614  -0.1858 41  PHE B O   
6131  C CB  . PHE B 32  ? 0.5250  1.8511  1.5443  0.0735  0.0962  -0.1977 41  PHE B CB  
6134  N N   . ILE B 33  ? 1.7771  3.0391  2.7355  0.0592  0.1013  -0.1921 42  ILE B N   
6135  C CA  . ILE B 33  ? 2.0134  3.2565  2.9470  0.0672  0.1086  -0.1809 42  ILE B CA  
6136  C C   . ILE B 33  ? 0.9137  2.1692  1.8060  0.0498  0.0796  -0.1753 42  ILE B C   
6137  O O   . ILE B 33  ? 1.4614  2.7178  2.3058  0.0585  0.0629  -0.1572 42  ILE B O   
6138  C CB  . ILE B 33  ? 1.4051  2.6032  2.3645  0.0624  0.1370  -0.1806 42  ILE B CB  
6139  C CG1 . ILE B 33  ? 1.3541  2.5435  2.3516  0.0819  0.1651  -0.1766 42  ILE B CG1 
6140  C CG2 . ILE B 33  ? 1.5647  2.7428  2.4986  0.0655  0.1427  -0.1716 42  ILE B CG2 
6141  C CD1 . ILE B 33  ? 0.4819  1.6307  1.5043  0.0745  0.1892  -0.1744 42  ILE B CD1 
6153  N N   . ALA B 34  ? 0.7804  2.0293  1.6750  0.0268  0.0705  -0.1823 43  ALA B N   
6154  C CA  . ALA B 34  ? 0.4876  1.7453  1.3468  0.0106  0.0466  -0.1701 43  ALA B CA  
6155  C C   . ALA B 34  ? 0.6333  1.9286  1.4546  0.0152  0.0163  -0.1601 43  ALA B C   
6156  O O   . ALA B 34  ? 0.4468  1.7529  1.2307  0.0058  -0.0081 -0.1372 43  ALA B O   
6157  C CB  . ALA B 34  ? 0.5712  1.8209  1.4385  -0.0053 0.0462  -0.1801 43  ALA B CB  
6163  N N   . LYS B 35  ? 0.7588  2.0741  1.5880  0.0277  0.0145  -0.1723 44  LYS B N   
6164  C CA  . LYS B 35  ? 0.4749  1.8235  1.2679  0.0339  -0.0135 -0.1644 44  LYS B CA  
6165  C C   . LYS B 35  ? 0.5156  1.8787  1.2797  0.0560  -0.0232 -0.1447 44  LYS B C   
6166  O O   . LYS B 35  ? 0.7271  2.0891  1.4380  0.0613  -0.0511 -0.1297 44  LYS B O   
6167  C CB  . LYS B 35  ? 0.4755  1.8406  1.2903  0.0393  -0.0111 -0.1838 44  LYS B CB  
6170  N N   . HIS B 36  ? 0.9991  2.2794  1.7398  0.0682  -0.0007 -0.1319 45  HIS B N   
6171  C CA  . HIS B 36  ? 1.0342  2.2175  1.6830  0.0934  -0.0060 -0.1019 45  HIS B CA  
6172  C C   . HIS B 36  ? 0.8849  1.9534  1.4667  0.0903  -0.0027 -0.0751 45  HIS B C   
6173  O O   . HIS B 36  ? 1.1001  2.0751  1.6140  0.1166  0.0060  -0.0556 45  HIS B O   
6174  C CB  . HIS B 36  ? 0.9334  2.1319  1.6166  0.1271  0.0233  -0.1125 45  HIS B CB  
6175  C CG  . HIS B 36  ? 1.2383  2.5321  1.9663  0.1332  0.0135  -0.1299 45  HIS B CG  
6176  N ND1 . HIS B 36  ? 0.4954  1.8851  1.3202  0.1172  0.0208  -0.1622 45  HIS B ND1 
6177  C CD2 . HIS B 36  ? 0.8788  2.1701  1.5596  0.1545  -0.0027 -0.1174 45  HIS B CD2 
6178  C CE1 . HIS B 36  ? 0.5050  1.9230  1.3267  0.1234  0.0073  -0.1651 45  HIS B CE1 
6179  N NE2 . HIS B 36  ? 0.6983  2.1002  1.4578  0.1500  -0.0055 -0.1430 45  HIS B NE2 
6187  N N   . LEU B 37  ? 0.9151  1.9861  1.5085  0.0599  -0.0113 -0.0711 46  LEU B N   
6188  C CA  . LEU B 37  ? 0.8908  1.8570  1.4248  0.0516  -0.0122 -0.0441 46  LEU B CA  
6189  C C   . LEU B 37  ? 0.9734  1.8211  1.3778  0.0615  -0.0430 -0.0044 46  LEU B C   
6190  O O   . LEU B 37  ? 1.2049  1.9437  1.5485  0.0749  -0.0323 0.0127  46  LEU B O   
6191  C CB  . LEU B 37  ? 0.8107  1.8146  1.3777  0.0157  -0.0237 -0.0403 46  LEU B CB  
6194  N N   . PRO B 38  ? 0.7524  1.6078  1.1049  0.0565  -0.0815 0.0116  47  PRO B N   
6195  C CA  . PRO B 38  ? 0.8497  1.5811  1.0700  0.0680  -0.1129 0.0486  47  PRO B CA  
6196  C C   . PRO B 38  ? 1.0254  1.6781  1.1952  0.1131  -0.0872 0.0477  47  PRO B C   
6197  O O   . PRO B 38  ? 1.3085  1.8334  1.3908  0.1237  -0.0877 0.0710  47  PRO B O   
6198  C CB  . PRO B 38  ? 0.8430  1.6295  1.0451  0.0586  -0.1514 0.0556  47  PRO B CB  
6199  C CG  . PRO B 38  ? 0.7511  1.6679  1.0571  0.0312  -0.1488 0.0351  47  PRO B CG  
6200  C CD  . PRO B 38  ? 0.6938  1.6638  1.0992  0.0380  -0.1009 -0.0007 47  PRO B CD  
6208  N N   . ASP B 39  ? 0.8846  1.6097  1.1077  0.1414  -0.0634 0.0234  48  ASP B N   
6209  C CA  . ASP B 39  ? 0.9470  1.6053  1.1233  0.1896  -0.0366 0.0283  48  ASP B CA  
6210  C C   . ASP B 39  ? 1.0308  1.6454  1.2337  0.2037  0.0070  0.0238  48  ASP B C   
6211  O O   . ASP B 39  ? 1.0388  1.5311  1.1490  0.2339  0.0169  0.0454  48  ASP B O   
6212  C CB  . ASP B 39  ? 1.2878  2.0518  1.5336  0.2124  -0.0206 0.0064  48  ASP B CB  
6213  C CG  . ASP B 39  ? 0.9281  1.7033  1.1175  0.2113  -0.0616 0.0168  48  ASP B CG  
6218  N N   . LEU B 40  ? 0.8650  1.5740  1.1894  0.1829  0.0327  -0.0038 49  LEU B N   
6219  C CA  . LEU B 40  ? 1.1384  1.8249  1.5063  0.1945  0.0762  -0.0113 49  LEU B CA  
6220  C C   . LEU B 40  ? 1.1902  1.7589  1.4824  0.1812  0.0677  0.0112  49  LEU B C   
6221  O O   . LEU B 40  ? 1.0083  1.5067  1.2821  0.2033  0.0988  0.0173  49  LEU B O   
6222  C CB  . LEU B 40  ? 1.1006  1.9147  1.6114  0.1708  0.0982  -0.0465 49  LEU B CB  
6223  C CG  . LEU B 40  ? 1.3368  2.2707  1.9401  0.1821  0.1116  -0.0713 49  LEU B CG  
6224  C CD1 . LEU B 40  ? 1.0818  2.1233  1.8040  0.1501  0.1200  -0.1048 49  LEU B CD1 
6225  C CD2 . LEU B 40  ? 1.2259  2.1453  1.8439  0.2255  0.1510  -0.0654 49  LEU B CD2 
6237  N N   . ILE B 41  ? 1.6222  2.1761  1.8797  0.1435  0.0273  0.0246  50  ILE B N   
6238  C CA  . ILE B 41  ? 1.6747  2.1075  1.8473  0.1288  0.0106  0.0531  50  ILE B CA  
6239  C C   . ILE B 41  ? 2.1969  2.4850  2.2205  0.1585  -0.0092 0.0847  50  ILE B C   
6240  O O   . ILE B 41  ? 2.4856  2.6560  2.4379  0.1789  0.0052  0.0998  50  ILE B O   
6241  C CB  . ILE B 41  ? 1.4636  1.9308  1.6465  0.0797  -0.0289 0.0651  50  ILE B CB  
6242  C CG1 . ILE B 41  ? 2.4429  3.0353  2.7622  0.0569  -0.0033 0.0337  50  ILE B CG1 
6243  C CG2 . ILE B 41  ? 1.8865  2.2240  1.9743  0.0614  -0.0541 0.1017  50  ILE B CG2 
6244  C CD1 . ILE B 41  ? 0.7828  1.4386  1.1276  0.0164  -0.0360 0.0434  50  ILE B CD1 
6256  N N   . GLU B 42  ? 1.9277  2.2193  1.8981  0.1643  -0.0416 0.0944  51  GLU B N   
6257  C CA  . GLU B 42  ? 2.0602  2.2055  1.8758  0.1908  -0.0672 0.1257  51  GLU B CA  
6258  C C   . GLU B 42  ? 1.9092  1.9926  1.6914  0.2487  -0.0220 0.1226  51  GLU B C   
6259  O O   . GLU B 42  ? 1.7348  1.6672  1.3961  0.2718  -0.0242 0.1465  51  GLU B O   
6260  C CB  . GLU B 42  ? 1.2512  1.4299  1.0319  0.1886  -0.1058 0.1322  51  GLU B CB  
6261  C CG  . GLU B 42  ? 1.5449  1.5849  1.1713  0.2258  -0.1268 0.1585  51  GLU B CG  
6262  C CD  . GLU B 42  ? 1.6290  1.6895  1.2669  0.2847  -0.0831 0.1437  51  GLU B CD  
6269  N N   . SER B 43  ? 1.9122  2.1099  1.8007  0.2731  0.0199  0.0958  52  SER B N   
6270  C CA  . SER B 43  ? 1.4112  1.5643  1.2799  0.3300  0.0666  0.0982  52  SER B CA  
6271  C C   . SER B 43  ? 1.2864  1.3908  1.1741  0.3338  0.1023  0.0978  52  SER B C   
6272  O O   . SER B 43  ? 1.7276  1.7266  1.5371  0.3797  0.1288  0.1144  52  SER B O   
6273  C CB  . SER B 43  ? 1.3074  1.6034  1.2936  0.3512  0.0990  0.0751  52  SER B CB  
6274  O OG  . SER B 43  ? 1.1924  1.5988  1.3232  0.3322  0.1328  0.0486  52  SER B OG  
6280  N N   . GLY B 44  ? 1.1237  1.9116  0.9053  0.1534  -0.1327 -0.1098 53  GLY B N   
6281  C CA  . GLY B 44  ? 0.7635  1.5676  0.5847  0.1276  -0.0585 -0.0829 53  GLY B CA  
6282  C C   . GLY B 44  ? 0.7776  1.6559  0.7111  0.0963  -0.0096 -0.1121 53  GLY B C   
6283  O O   . GLY B 44  ? 0.9409  1.8538  0.9144  0.0822  0.0470  -0.1010 53  GLY B O   
6287  N N   . GLN B 45  ? 0.9504  1.8516  0.9327  0.0828  -0.0308 -0.1477 54  GLN B N   
6288  C CA  . GLN B 45  ? 0.7074  1.6786  0.7994  0.0534  0.0088  -0.1777 54  GLN B CA  
6289  C C   . GLN B 45  ? 1.0434  1.9800  1.1551  0.0123  0.0264  -0.1653 54  GLN B C   
6290  O O   . GLN B 45  ? 1.2004  2.1847  1.3997  -0.0140 0.0476  -0.1929 54  GLN B O   
6291  C CB  . GLN B 45  ? 1.0887  2.1273  1.2382  0.0742  -0.0325 -0.2392 54  GLN B CB  
6294  N N   . LEU B 46  ? 1.4027  2.2589  1.4384  0.0062  0.0185  -0.1254 55  LEU B N   
6295  C CA  . LEU B 46  ? 1.1288  1.9517  1.1836  -0.0306 0.0385  -0.1148 55  LEU B CA  
6296  C C   . LEU B 46  ? 0.9734  1.8119  1.0938  -0.0643 0.1039  -0.0947 55  LEU B C   
6297  O O   . LEU B 46  ? 1.0180  1.8777  1.2097  -0.0950 0.1245  -0.1132 55  LEU B O   
6298  C CB  . LEU B 46  ? 1.7299  2.4695  1.6932  -0.0281 0.0178  -0.0774 55  LEU B CB  
6299  C CG  . LEU B 46  ? 1.2512  1.9585  1.2346  -0.0629 0.0369  -0.0725 55  LEU B CG  
6300  C CD1 . LEU B 46  ? 1.3483  2.0368  1.2965  -0.0629 -0.0091 -0.0995 55  LEU B CD1 
6301  C CD2 . LEU B 46  ? 0.8930  1.5382  0.8360  -0.0721 0.0630  -0.0195 55  LEU B CD2 
6313  N N   . ARG B 47  ? 0.6536  1.4769  0.7479  -0.0610 0.1344  -0.0558 56  ARG B N   
6314  C CA  . ARG B 47  ? 0.8284  1.6582  0.9782  -0.0973 0.1930  -0.0331 56  ARG B CA  
6315  C C   . ARG B 47  ? 1.0865  2.0054  1.3341  -0.1130 0.2214  -0.0684 56  ARG B C   
6316  O O   . ARG B 47  ? 1.0531  1.9849  1.3706  -0.1511 0.2540  -0.0697 56  ARG B O   
6317  C CB  . ARG B 47  ? 0.9793  1.7649  1.0693  -0.0921 0.2158  0.0188  56  ARG B CB  
6318  C CG  . ARG B 47  ? 1.2009  1.8989  1.2094  -0.0832 0.1910  0.0560  56  ARG B CG  
6319  C CD  . ARG B 47  ? 1.2828  1.9362  1.2254  -0.0717 0.2024  0.1039  56  ARG B CD  
6320  N NE  . ARG B 47  ? 1.1716  1.7440  1.0499  -0.0679 0.1820  0.1411  56  ARG B NE  
6321  C CZ  . ARG B 47  ? 0.8816  1.4006  0.6874  -0.0524 0.1757  0.1837  56  ARG B CZ  
6322  N NH1 . ARG B 47  ? 1.1543  1.6891  0.9361  -0.0388 0.1898  0.1942  56  ARG B NH1 
6323  N NH2 . ARG B 47  ? 0.7743  1.2251  0.5325  -0.0509 0.1557  0.2147  56  ARG B NH2 
6337  N N   . GLU B 48  ? 1.0008  1.9837  1.2605  -0.0849 0.2080  -0.0995 57  GLU B N   
6338  C CA  . GLU B 48  ? 0.9868  2.0631  1.3497  -0.1008 0.2348  -0.1367 57  GLU B CA  
6339  C C   . GLU B 48  ? 1.2475  2.3449  1.6791  -0.1195 0.2153  -0.1756 57  GLU B C   
6340  O O   . GLU B 48  ? 1.1367  2.2738  1.6549  -0.1559 0.2489  -0.1856 57  GLU B O   
6341  C CB  . GLU B 48  ? 0.7461  1.8909  1.1147  -0.0622 0.2192  -0.1698 57  GLU B CB  
6344  N N   . ARG B 49  ? 1.3634  2.4294  1.7520  -0.0974 0.1592  -0.1960 58  ARG B N   
6345  C CA  . ARG B 49  ? 1.0462  2.1264  1.4864  -0.1119 0.1335  -0.2358 58  ARG B CA  
6346  C C   . ARG B 49  ? 0.9534  1.9895  1.4152  -0.1531 0.1619  -0.2163 58  ARG B C   
6347  O O   . ARG B 49  ? 1.5530  2.6238  2.0992  -0.1821 0.1756  -0.2408 58  ARG B O   
6348  C CB  . ARG B 49  ? 1.0663  2.1099  1.4341  -0.0805 0.0663  -0.2544 58  ARG B CB  
6349  C CG  . ARG B 49  ? 0.9718  2.0095  1.3651  -0.0953 0.0345  -0.2899 58  ARG B CG  
6350  C CD  . ARG B 49  ? 1.0710  2.1905  1.5613  -0.0958 0.0207  -0.3430 58  ARG B CD  
6351  N NE  . ARG B 49  ? 1.2270  2.3271  1.7088  -0.0973 -0.0320 -0.3789 58  ARG B NE  
6352  C CZ  . ARG B 49  ? 1.4826  2.5674  1.9081  -0.0667 -0.0964 -0.4009 58  ARG B CZ  
6353  N NH1 . ARG B 49  ? 1.2987  2.3873  1.6772  -0.0297 -0.1178 -0.3930 58  ARG B NH1 
6354  N NH2 . ARG B 49  ? 0.6873  1.7474  1.0981  -0.0738 -0.1424 -0.4304 58  ARG B NH2 
6368  N N   . VAL B 50  ? 0.9246  1.8833  1.3132  -0.1549 0.1678  -0.1739 59  VAL B N   
6369  C CA  . VAL B 50  ? 0.9532  1.8657  1.3613  -0.1906 0.1978  -0.1514 59  VAL B CA  
6370  C C   . VAL B 50  ? 0.8694  1.8185  1.3600  -0.2250 0.2500  -0.1402 59  VAL B C   
6371  O O   . VAL B 50  ? 0.6968  1.6495  1.2546  -0.2584 0.2656  -0.1518 59  VAL B O   
6372  C CB  . VAL B 50  ? 0.8608  1.6926  1.1812  -0.1822 0.1993  -0.1030 59  VAL B CB  
6373  C CG1 . VAL B 50  ? 0.7907  1.5769  1.1381  -0.2164 0.2362  -0.0737 59  VAL B CG1 
6374  C CG2 . VAL B 50  ? 1.3084  2.0991  1.5549  -0.1606 0.1502  -0.1143 59  VAL B CG2 
6384  N N   . GLU B 51  ? 1.4724  2.4457  1.9546  -0.2191 0.2772  -0.1163 60  GLU B N   
6385  C CA  . GLU B 51  ? 0.8482  1.8494  1.3961  -0.2568 0.3288  -0.0985 60  GLU B CA  
6386  C C   . GLU B 51  ? 0.7196  1.8073  1.3721  -0.2749 0.3352  -0.1437 60  GLU B C   
6387  O O   . GLU B 51  ? 0.9033  1.9769  1.6087  -0.3067 0.3605  -0.1301 60  GLU B O   
6388  C CB  . GLU B 51  ? 0.6669  1.6690  1.1666  -0.2463 0.3562  -0.0613 60  GLU B CB  
6389  C CG  . GLU B 51  ? 1.2809  2.1854  1.6900  -0.2409 0.3562  -0.0071 60  GLU B CG  
6390  C CD  . GLU B 51  ? 1.6567  2.5474  1.9829  -0.2099 0.3563  0.0210  60  GLU B CD  
6391  O OE1 . GLU B 51  ? 1.3894  2.3473  1.7280  -0.1940 0.3636  0.0005  60  GLU B OE1 
6392  O OE2 . GLU B 51  ? 1.5527  2.3656  1.8028  -0.2003 0.3477  0.0618  60  GLU B OE2 
6399  N N   . LYS B 52  ? 0.7786  1.9162  1.4456  -0.2467 0.2970  -0.1906 61  LYS B N   
6400  C CA  . LYS B 52  ? 0.9861  2.2062  1.7582  -0.2622 0.2969  -0.2365 61  LYS B CA  
6401  C C   . LYS B 52  ? 0.8971  2.0942  1.7008  -0.2765 0.2657  -0.2667 61  LYS B C   
6402  O O   . LYS B 52  ? 0.8837  2.1313  1.7379  -0.2682 0.2343  -0.3144 61  LYS B O   
6403  C CB  . LYS B 52  ? 0.6678  1.9636  1.4537  -0.2245 0.2731  -0.2747 61  LYS B CB  
6406  N N   . LEU B 53  ? 0.7742  1.8932  1.5443  -0.2942 0.2694  -0.2424 62  LEU B N   
6407  C CA  . LEU B 53  ? 0.9375  2.0334  1.7396  -0.3118 0.2467  -0.2713 62  LEU B CA  
6408  C C   . LEU B 53  ? 0.9018  1.9869  1.7764  -0.3567 0.2811  -0.2584 62  LEU B C   
6409  O O   . LEU B 53  ? 1.3765  2.4322  2.2440  -0.3693 0.3157  -0.2125 62  LEU B O   
6410  C CB  . LEU B 53  ? 0.9467  1.9592  1.6584  -0.2963 0.2199  -0.2614 62  LEU B CB  
6411  C CG  . LEU B 53  ? 0.9727  1.9785  1.6007  -0.2531 0.1763  -0.2711 62  LEU B CG  
6412  C CD1 . LEU B 53  ? 0.8847  1.8118  1.4343  -0.2483 0.1561  -0.2611 62  LEU B CD1 
6413  C CD2 . LEU B 53  ? 1.1181  2.1842  1.7795  -0.2355 0.1346  -0.3226 62  LEU B CD2 
6425  N N   . ASN B 54  ? 0.7663  1.8522  1.6926  -0.3736 0.2609  -0.2939 63  ASN B N   
6426  C CA  . ASN B 54  ? 0.7353  1.7807  1.7087  -0.4076 0.2784  -0.2792 63  ASN B CA  
6427  C C   . ASN B 54  ? 1.4145  2.3829  2.3525  -0.4185 0.2801  -0.2660 63  ASN B C   
6428  O O   . ASN B 54  ? 1.1969  2.1421  2.0790  -0.4009 0.2594  -0.2800 63  ASN B O   
6429  C CB  . ASN B 54  ? 0.7469  1.8282  1.7958  -0.4207 0.2549  -0.3241 63  ASN B CB  
6430  C CG  . ASN B 54  ? 0.7346  1.8929  1.8321  -0.4119 0.2548  -0.3376 63  ASN B CG  
6431  O OD1 . ASN B 54  ? 0.7300  1.9318  1.8589  -0.4002 0.2209  -0.3837 63  ASN B OD1 
6432  N ND2 . ASN B 54  ? 0.7510  1.9246  1.8550  -0.4180 0.2912  -0.2985 63  ASN B ND2 
6439  N N   . MET B 55  ? 2.2905  3.2118  3.2540  -0.4443 0.3007  -0.2362 64  MET B N   
6440  C CA  . MET B 55  ? 0.8570  1.7049  1.8020  -0.4549 0.3010  -0.2287 64  MET B CA  
6441  C C   . MET B 55  ? 0.8032  1.6520  1.7886  -0.4653 0.2743  -0.2816 64  MET B C   
6442  O O   . MET B 55  ? 0.7942  1.6460  1.8415  -0.4873 0.2717  -0.2912 64  MET B O   
6443  C CB  . MET B 55  ? 1.5515  2.3503  2.5115  -0.4776 0.3250  -0.1800 64  MET B CB  
6444  C CG  . MET B 55  ? 1.4227  2.1443  2.3619  -0.4834 0.3262  -0.1661 64  MET B CG  
6445  S SD  . MET B 55  ? 2.8277  3.5001  3.7706  -0.5059 0.3482  -0.1011 64  MET B SD  
6452  N N   . LEU B 56  ? 1.4412  2.2862  2.3852  -0.4492 0.2509  -0.3152 65  LEU B N   
6453  C CA  . LEU B 56  ? 1.2418  2.0732  2.1973  -0.4524 0.2194  -0.3647 65  LEU B CA  
6454  C C   . LEU B 56  ? 0.9883  1.7478  1.9400  -0.4652 0.2258  -0.3655 65  LEU B C   
6455  O O   . LEU B 56  ? 0.8496  1.5636  1.7761  -0.4646 0.2489  -0.3282 65  LEU B O   
6456  C CB  . LEU B 56  ? 1.3733  2.2085  2.2503  -0.4188 0.1812  -0.3919 65  LEU B CB  
6457  C CG  . LEU B 56  ? 1.1661  2.0676  2.0433  -0.3995 0.1622  -0.4024 65  LEU B CG  
6458  C CD1 . LEU B 56  ? 1.2439  2.1332  2.0449  -0.3727 0.1144  -0.4349 65  LEU B CD1 
6459  C CD2 . LEU B 56  ? 1.2833  2.2513  2.2682  -0.4226 0.1636  -0.4256 65  LEU B CD2 
6471  N N   . SER B 57  ? 1.5041  2.2538  2.4856  -0.4765 0.2029  -0.4113 66  SER B N   
6472  C CA  . SER B 57  ? 2.1682  2.8545  3.1485  -0.4852 0.2024  -0.4276 66  SER B CA  
6473  C C   . SER B 57  ? 1.3120  1.9645  2.1971  -0.4578 0.1837  -0.4489 66  SER B C   
6474  O O   . SER B 57  ? 1.4223  2.1001  2.2536  -0.4388 0.1578  -0.4666 66  SER B O   
6475  C CB  . SER B 57  ? 3.2008  3.8941  4.2600  -0.5120 0.1857  -0.4686 66  SER B CB  
6476  O OG  . SER B 57  ? 2.3794  3.0116  3.4382  -0.5182 0.1827  -0.4904 66  SER B OG  
6482  N N   . ILE B 58  ? 1.1052  1.7003  1.9712  -0.4572 0.1957  -0.4483 67  ILE B N   
6483  C CA  . ILE B 58  ? 0.8806  1.4455  1.6596  -0.4360 0.1838  -0.4692 67  ILE B CA  
6484  C C   . ILE B 58  ? 0.9286  1.4737  1.7091  -0.4439 0.1622  -0.5277 67  ILE B C   
6485  O O   . ILE B 58  ? 1.0594  1.5813  1.7646  -0.4301 0.1537  -0.5497 67  ILE B O   
6486  C CB  . ILE B 58  ? 1.3419  1.8616  2.0916  -0.4259 0.2108  -0.4355 67  ILE B CB  
6487  C CG1 . ILE B 58  ? 1.7311  2.2103  2.5539  -0.4448 0.2276  -0.4386 67  ILE B CG1 
6488  C CG2 . ILE B 58  ? 1.0453  1.5772  1.7766  -0.4158 0.2280  -0.3777 67  ILE B CG2 
6489  C CD1 . ILE B 58  ? 1.8488  2.2876  2.6469  -0.4378 0.2260  -0.4765 67  ILE B CD1 
6501  N N   . ASP B 59  ? 2.0520  2.6067  2.9114  -0.4666 0.1518  -0.5540 68  ASP B N   
6502  C CA  . ASP B 59  ? 1.3349  1.8585  2.2043  -0.4762 0.1347  -0.6071 68  ASP B CA  
6503  C C   . ASP B 59  ? 1.1507  1.6839  1.9553  -0.4679 0.0982  -0.6522 68  ASP B C   
6504  O O   . ASP B 59  ? 1.0832  1.5836  1.8701  -0.4719 0.0855  -0.6970 68  ASP B O   
6505  C CB  . ASP B 59  ? 1.7705  2.2989  2.7460  -0.5051 0.1304  -0.6185 68  ASP B CB  
6506  C CG  . ASP B 59  ? 2.1540  2.6672  3.1937  -0.5195 0.1610  -0.5746 68  ASP B CG  
6507  O OD1 . ASP B 59  ? 2.1801  2.6747  3.1814  -0.5048 0.1846  -0.5384 68  ASP B OD1 
6508  O OD2 . ASP B 59  ? 2.3486  2.8673  3.4758  -0.5472 0.1594  -0.5743 68  ASP B OD2 
6513  N N   . HIS B 60  ? 1.5198  2.0921  2.2844  -0.4560 0.0790  -0.6431 69  HIS B N   
6514  C CA  . HIS B 60  ? 1.6505  2.2263  2.3512  -0.4498 0.0376  -0.6839 69  HIS B CA  
6515  C C   . HIS B 60  ? 1.6008  2.1519  2.1822  -0.4306 0.0350  -0.6813 69  HIS B C   
6516  O O   . HIS B 60  ? 1.7672  2.3195  2.2768  -0.4245 -0.0012 -0.7047 69  HIS B O   
6517  C CB  . HIS B 60  ? 1.5832  2.2146  2.3156  -0.4482 0.0109  -0.6805 69  HIS B CB  
6518  C CG  . HIS B 60  ? 1.7512  2.4126  2.6035  -0.4714 0.0130  -0.6865 69  HIS B CG  
6519  N ND1 . HIS B 60  ? 2.7735  3.4640  3.7000  -0.4805 0.0464  -0.6451 69  HIS B ND1 
6520  C CD2 . HIS B 60  ? 1.2649  1.9302  2.1742  -0.4902 -0.0145 -0.7277 69  HIS B CD2 
6521  C CE1 . HIS B 60  ? 0.9890  1.7027  2.0147  -0.5058 0.0413  -0.6595 69  HIS B CE1 
6522  N NE2 . HIS B 60  ? 1.4806  2.1773  2.4962  -0.5084 0.0036  -0.7066 69  HIS B NE2 
6530  N N   . LEU B 61  ? 2.3198  2.8467  2.8805  -0.4232 0.0707  -0.6532 70  LEU B N   
6531  C CA  . LEU B 61  ? 1.6863  2.1890  2.1431  -0.4090 0.0756  -0.6494 70  LEU B CA  
6532  C C   . LEU B 61  ? 1.1573  1.6204  1.6069  -0.4173 0.0877  -0.6900 70  LEU B C   
6533  O O   . LEU B 61  ? 1.1038  1.5474  1.6081  -0.4197 0.1194  -0.6819 70  LEU B O   
6534  C CB  . LEU B 61  ? 1.7343  2.2398  2.1854  -0.3955 0.1066  -0.5926 70  LEU B CB  
6535  C CG  . LEU B 61  ? 2.5609  3.1063  3.0213  -0.3862 0.0955  -0.5563 70  LEU B CG  
6536  C CD1 . LEU B 61  ? 1.8823  2.4263  2.3624  -0.3781 0.1293  -0.5014 70  LEU B CD1 
6537  C CD2 . LEU B 61  ? 1.6805  2.2336  2.0412  -0.3716 0.0606  -0.5594 70  LEU B CD2 
6549  N N   . THR B 62  ? 1.9633  2.4124  2.3475  -0.4220 0.0599  -0.7363 71  THR B N   
6550  C CA  . THR B 62  ? 2.3313  2.7459  2.7168  -0.4315 0.0667  -0.7855 71  THR B CA  
6551  C C   . THR B 62  ? 1.4073  1.7996  1.7096  -0.4233 0.0918  -0.7916 71  THR B C   
6552  O O   . THR B 62  ? 1.4995  1.8738  1.8415  -0.4208 0.1257  -0.7957 71  THR B O   
6553  C CB  . THR B 62  ? 1.5874  1.9959  1.9525  -0.4440 0.0229  -0.8363 71  THR B CB  
6554  O OG1 . THR B 62  ? 1.9574  2.3501  2.1972  -0.4387 0.0039  -0.8504 71  THR B OG1 
6555  C CG2 . THR B 62  ? 1.6242  2.0691  2.0437  -0.4476 -0.0084 -0.8226 71  THR B CG2 
6563  N N   . ASP B 63  ? 1.7147  2.1078  1.9044  -0.4205 0.0743  -0.7935 72  ASP B N   
6564  C CA  . ASP B 63  ? 2.5302  2.9078  2.6378  -0.4172 0.0993  -0.8005 72  ASP B CA  
6565  C C   . ASP B 63  ? 3.3173  3.7078  3.4213  -0.4029 0.1283  -0.7436 72  ASP B C   
6566  O O   . ASP B 63  ? 2.0127  2.4221  2.1482  -0.3949 0.1219  -0.6982 72  ASP B O   
6567  C CB  . ASP B 63  ? 2.1026  2.4686  2.0850  -0.4208 0.0680  -0.8157 72  ASP B CB  
6568  C CG  . ASP B 63  ? 1.8226  2.2019  1.7615  -0.4129 0.0283  -0.7760 72  ASP B CG  
6569  O OD1 . ASP B 63  ? 1.8871  2.2877  1.8959  -0.4142 0.0080  -0.7727 72  ASP B OD1 
6570  O OD2 . ASP B 63  ? 1.8431  2.2101  1.6816  -0.4048 0.0164  -0.7469 72  ASP B OD2 
6575  N N   . HIS B 64  ? 1.4758  2.0336  1.6636  -0.3233 -0.0062 -0.4677 73  HIS B N   
6576  C CA  . HIS B 64  ? 1.5771  2.0486  1.7531  -0.2899 0.0108  -0.4113 73  HIS B CA  
6577  C C   . HIS B 64  ? 1.1841  1.7254  1.3732  -0.2387 -0.0063 -0.3784 73  HIS B C   
6578  O O   . HIS B 64  ? 1.0075  1.5309  1.2155  -0.2351 0.0060  -0.3474 73  HIS B O   
6579  C CB  . HIS B 64  ? 1.8193  2.1857  1.9446  -0.2612 0.0194  -0.3939 73  HIS B CB  
6580  C CG  . HIS B 64  ? 1.3597  1.6410  1.4748  -0.2287 0.0351  -0.3398 73  HIS B CG  
6581  N ND1 . HIS B 64  ? 1.1243  1.3274  1.2489  -0.2531 0.0597  -0.3209 73  HIS B ND1 
6582  C CD2 . HIS B 64  ? 1.2049  1.4659  1.2988  -0.1757 0.0299  -0.3027 73  HIS B CD2 
6583  C CE1 . HIS B 64  ? 0.8716  1.0202  0.9846  -0.2152 0.0651  -0.2766 73  HIS B CE1 
6584  N NE2 . HIS B 64  ? 1.8429  2.0257  1.9402  -0.1708 0.0482  -0.2658 73  HIS B NE2 
6591  N N   . LYS B 65  ? 1.3829  2.0035  1.5586  -0.1985 -0.0343 -0.3861 74  LYS B N   
6592  C CA  . LYS B 65  ? 1.1086  1.7678  1.2823  -0.1411 -0.0475 -0.3495 74  LYS B CA  
6593  C C   . LYS B 65  ? 0.8377  1.5708  1.0611  -0.1517 -0.0470 -0.3482 74  LYS B C   
6594  O O   . LYS B 65  ? 0.6472  1.3646  0.8722  -0.1193 -0.0427 -0.3108 74  LYS B O   
6595  C CB  . LYS B 65  ? 1.0222  1.7532  1.1661  -0.0950 -0.0771 -0.3591 74  LYS B CB  
6596  C CG  . LYS B 65  ? 0.9065  1.5658  0.9910  -0.0688 -0.0762 -0.3502 74  LYS B CG  
6597  C CD  . LYS B 65  ? 0.8582  1.5848  0.9033  -0.0162 -0.1041 -0.3519 74  LYS B CD  
6598  C CE  . LYS B 65  ? 1.3436  1.9981  1.3267  0.0066  -0.0978 -0.3431 74  LYS B CE  
6599  N NZ  . LYS B 65  ? 2.0209  2.7289  1.9527  0.0577  -0.1217 -0.3428 74  LYS B NZ  
6613  N N   . SER B 66  ? 1.0402  1.8595  1.3044  -0.1967 -0.0513 -0.3913 75  SER B N   
6614  C CA  . SER B 66  ? 1.0675  1.9716  1.3855  -0.2131 -0.0476 -0.3964 75  SER B CA  
6615  C C   . SER B 66  ? 0.7681  1.5882  1.0991  -0.2505 -0.0131 -0.3752 75  SER B C   
6616  O O   . SER B 66  ? 0.5837  1.4353  0.9409  -0.2433 -0.0044 -0.3572 75  SER B O   
6617  C CB  . SER B 66  ? 1.6464  2.6553  1.9994  -0.2515 -0.0569 -0.4458 75  SER B CB  
6618  O OG  . SER B 66  ? 1.7677  2.8576  2.1035  -0.2055 -0.0884 -0.4579 75  SER B OG  
6624  N N   . GLN B 67  ? 0.8111  1.5213  1.1192  -0.2865 0.0075  -0.3760 76  GLN B N   
6625  C CA  . GLN B 67  ? 0.8148  1.4321  1.1226  -0.3122 0.0391  -0.3491 76  GLN B CA  
6626  C C   . GLN B 67  ? 0.8669  1.4193  1.1469  -0.2578 0.0398  -0.2968 76  GLN B C   
6627  O O   . GLN B 67  ? 0.9080  1.4348  1.1959  -0.2609 0.0561  -0.2716 76  GLN B O   
6628  C CB  . GLN B 67  ? 0.8229  1.3364  1.1083  -0.3588 0.0600  -0.3639 76  GLN B CB  
6629  C CG  . GLN B 67  ? 1.5934  2.1592  1.9024  -0.4175 0.0607  -0.4180 76  GLN B CG  
6630  C CD  . GLN B 67  ? 1.6726  2.1213  1.9480  -0.4540 0.0806  -0.4321 76  GLN B CD  
6631  O OE1 . GLN B 67  ? 2.1226  2.4643  2.3816  -0.4729 0.1100  -0.4085 76  GLN B OE1 
6632  N NE2 . GLN B 67  ? 1.3036  1.7630  1.5591  -0.4543 0.0651  -0.4655 76  GLN B NE2 
6641  N N   . ARG B 68  ? 0.8367  1.3619  1.0825  -0.2101 0.0235  -0.2811 77  ARG B N   
6642  C CA  . ARG B 68  ? 1.0439  1.5140  1.2673  -0.1640 0.0239  -0.2357 77  ARG B CA  
6643  C C   . ARG B 68  ? 1.1651  1.7137  1.4049  -0.1293 0.0116  -0.2243 77  ARG B C   
6644  O O   . ARG B 68  ? 1.1874  1.7018  1.4242  -0.1135 0.0201  -0.1942 77  ARG B O   
6645  C CB  . ARG B 68  ? 1.2022  1.6245  1.3863  -0.1276 0.0140  -0.2237 77  ARG B CB  
6646  C CG  . ARG B 68  ? 1.1975  1.5237  1.3596  -0.1487 0.0298  -0.2255 77  ARG B CG  
6647  C CD  . ARG B 68  ? 0.9119  1.1440  1.0662  -0.1457 0.0479  -0.1890 77  ARG B CD  
6648  N NE  . ARG B 68  ? 0.7106  0.9272  0.8499  -0.0988 0.0397  -0.1546 77  ARG B NE  
6649  C CZ  . ARG B 68  ? 0.8193  0.9967  0.9343  -0.0728 0.0384  -0.1429 77  ARG B CZ  
6650  N NH1 . ARG B 68  ? 0.8563  1.0031  0.9564  -0.0844 0.0445  -0.1622 77  ARG B NH1 
6651  N NH2 . ARG B 68  ? 0.9024  1.0695  1.0069  -0.0365 0.0331  -0.1130 77  ARG B NH2 
6665  N N   . LEU B 69  ? 1.0732  1.7296  1.3300  -0.1168 -0.0087 -0.2504 78  LEU B N   
6666  C CA  . LEU B 69  ? 0.9231  1.6596  1.1956  -0.0784 -0.0203 -0.2422 78  LEU B CA  
6667  C C   . LEU B 69  ? 0.9445  1.7129  1.2559  -0.1088 -0.0019 -0.2449 78  LEU B C   
6668  O O   . LEU B 69  ? 1.5250  2.3075  1.8387  -0.0778 0.0001  -0.2243 78  LEU B O   
6669  C CB  . LEU B 69  ? 1.0579  1.9114  1.3416  -0.0571 -0.0475 -0.2718 78  LEU B CB  
6670  C CG  . LEU B 69  ? 0.9888  1.9414  1.2953  -0.0165 -0.0594 -0.2692 78  LEU B CG  
6671  C CD1 . LEU B 69  ? 1.2935  2.1837  1.5606  0.0423  -0.0604 -0.2269 78  LEU B CD1 
6672  C CD2 . LEU B 69  ? 1.5452  2.6251  1.8665  0.0034  -0.0887 -0.3018 78  LEU B CD2 
6684  N N   . ALA B 70  ? 1.2835  2.0610  1.6226  -0.1701 0.0140  -0.2711 79  ALA B N   
6685  C CA  . ALA B 70  ? 1.1564  1.9511  1.5268  -0.2047 0.0381  -0.2705 79  ALA B CA  
6686  C C   . ALA B 70  ? 1.0019  1.6781  1.3399  -0.2001 0.0582  -0.2301 79  ALA B C   
6687  O O   . ALA B 70  ? 0.6713  1.3558  1.0142  -0.1879 0.0687  -0.2119 79  ALA B O   
6688  C CB  . ALA B 70  ? 0.4975  1.3168  0.8993  -0.2764 0.0536  -0.3078 79  ALA B CB  
6694  N N   . ARG B 71  ? 0.9698  1.5388  1.2725  -0.2043 0.0618  -0.2157 80  ARG B N   
6695  C CA  . ARG B 71  ? 0.8361  1.3002  1.1098  -0.1994 0.0776  -0.1791 80  ARG B CA  
6696  C C   . ARG B 71  ? 0.6760  1.1316  0.9305  -0.1439 0.0647  -0.1497 80  ARG B C   
6697  O O   . ARG B 71  ? 0.9095  1.3043  1.1457  -0.1369 0.0748  -0.1222 80  ARG B O   
6698  C CB  . ARG B 71  ? 1.2497  1.6118  1.4940  -0.2103 0.0827  -0.1720 80  ARG B CB  
6699  C CG  . ARG B 71  ? 1.2536  1.5228  1.4796  -0.2310 0.1060  -0.1482 80  ARG B CG  
6700  C CD  . ARG B 71  ? 1.2520  1.4252  1.4458  -0.2137 0.1044  -0.1287 80  ARG B CD  
6701  N NE  . ARG B 71  ? 1.2991  1.4352  1.4745  -0.1750 0.0976  -0.0933 80  ARG B NE  
6702  C CZ  . ARG B 71  ? 1.0362  1.1178  1.1963  -0.1793 0.1103  -0.0687 80  ARG B CZ  
6703  N NH1 . ARG B 71  ? 1.2868  1.3394  1.4444  -0.2184 0.1329  -0.0725 80  ARG B NH1 
6704  N NH2 . ARG B 71  ? 1.4131  1.4675  1.5574  -0.1463 0.1011  -0.0413 80  ARG B NH2 
6718  N N   . LEU B 72  ? 0.5606  1.0690  0.8134  -0.1043 0.0423  -0.1551 81  LEU B N   
6719  C CA  . LEU B 72  ? 0.4443  0.9467  0.6777  -0.0528 0.0319  -0.1306 81  LEU B CA  
6720  C C   . LEU B 72  ? 0.9520  1.5275  1.2078  -0.0423 0.0360  -0.1347 81  LEU B C   
6721  O O   . LEU B 72  ? 1.0118  1.5527  1.2509  -0.0209 0.0413  -0.1125 81  LEU B O   
6722  C CB  . LEU B 72  ? 0.8132  1.3369  1.0289  -0.0129 0.0099  -0.1326 81  LEU B CB  
6723  C CG  . LEU B 72  ? 0.3878  0.9233  0.5825  0.0444  -0.0027 -0.1142 81  LEU B CG  
6724  C CD1 . LEU B 72  ? 0.3823  0.8324  0.5538  0.0544  0.0065  -0.0840 81  LEU B CD1 
6725  C CD2 . LEU B 72  ? 0.4001  0.9403  0.5685  0.0767  -0.0201 -0.1142 81  LEU B CD2 
6737  N N   . VAL B 73  ? 0.8333  1.5134  1.1281  -0.0586 0.0342  -0.1651 82  VAL B N   
6738  C CA  . VAL B 73  ? 0.6004  1.3655  0.9230  -0.0464 0.0397  -0.1720 82  VAL B CA  
6739  C C   . VAL B 73  ? 0.4599  1.1833  0.7835  -0.0778 0.0680  -0.1594 82  VAL B C   
6740  O O   . VAL B 73  ? 1.4673  2.1855  1.7789  -0.0500 0.0741  -0.1434 82  VAL B O   
6741  C CB  . VAL B 73  ? 0.5539  1.4523  0.9260  -0.0620 0.0309  -0.2111 82  VAL B CB  
6742  C CG1 . VAL B 73  ? 0.6308  1.6259  1.0452  -0.0673 0.0447  -0.2235 82  VAL B CG1 
6743  C CG2 . VAL B 73  ? 0.3872  1.3380  0.7476  -0.0080 -0.0010 -0.2170 82  VAL B CG2 
6753  N N   . LEU B 74  ? 0.6518  1.3354  0.9816  -0.1339 0.0864  -0.1654 83  LEU B N   
6754  C CA  . LEU B 74  ? 0.6387  1.2823  0.9633  -0.1646 0.1154  -0.1521 83  LEU B CA  
6755  C C   . LEU B 74  ? 0.6146  1.1529  0.8901  -0.1376 0.1161  -0.1156 83  LEU B C   
6756  O O   . LEU B 74  ? 0.6853  1.2112  0.9482  -0.1351 0.1320  -0.1015 83  LEU B O   
6757  C CB  . LEU B 74  ? 0.8809  1.4848  1.2124  -0.2288 0.1366  -0.1629 83  LEU B CB  
6758  C CG  . LEU B 74  ? 0.7370  1.4369  1.1197  -0.2768 0.1440  -0.2032 83  LEU B CG  
6759  C CD1 . LEU B 74  ? 1.0466  1.6657  1.4180  -0.3340 0.1625  -0.2096 83  LEU B CD1 
6760  C CD2 . LEU B 74  ? 1.1061  1.8979  1.5259  -0.2919 0.1641  -0.2131 83  LEU B CD2 
6772  N N   . GLY B 75  ? 0.6953  1.1620  0.9426  -0.1176 0.0996  -0.1012 84  GLY B N   
6773  C CA  . GLY B 75  ? 0.7256  1.1000  0.9325  -0.0987 0.0996  -0.0700 84  GLY B CA  
6774  C C   . GLY B 75  ? 0.8331  1.2221  1.0253  -0.0535 0.0908  -0.0594 84  GLY B C   
6775  O O   . GLY B 75  ? 0.7506  1.0921  0.9160  -0.0475 0.0983  -0.0412 84  GLY B O   
6779  N N   . CYS B 76  ? 0.7244  1.1776  0.9296  -0.0198 0.0753  -0.0715 85  CYS B N   
6780  C CA  . CYS B 76  ? 0.7229  1.1870  0.9110  0.0269  0.0690  -0.0636 85  CYS B CA  
6781  C C   . CYS B 76  ? 0.7863  1.3048  0.9880  0.0218  0.0881  -0.0713 85  CYS B C   
6782  O O   . CYS B 76  ? 0.8241  1.3119  0.9981  0.0446  0.0931  -0.0593 85  CYS B O   
6783  C CB  . CYS B 76  ? 0.7257  1.2467  0.9215  0.0668  0.0499  -0.0740 85  CYS B CB  
6784  S SG  . CYS B 76  ? 0.8770  1.3459  1.0507  0.0823  0.0297  -0.0651 85  CYS B SG  
6790  N N   . ILE B 77  ? 0.4083  1.0115  0.6532  -0.0095 0.1001  -0.0936 86  ILE B N   
6791  C CA  . ILE B 77  ? 0.5459  1.2089  0.8098  -0.0221 0.1239  -0.1019 86  ILE B CA  
6792  C C   . ILE B 77  ? 0.6842  1.2626  0.9131  -0.0478 0.1446  -0.0811 86  ILE B C   
6793  O O   . ILE B 77  ? 0.6419  1.2281  0.8564  -0.0377 0.1609  -0.0761 86  ILE B O   
6794  C CB  . ILE B 77  ? 0.8776  1.6442  1.1987  -0.0621 0.1338  -0.1312 86  ILE B CB  
6795  C CG1 . ILE B 77  ? 1.1494  2.0113  1.5006  -0.0260 0.1088  -0.1518 86  ILE B CG1 
6796  C CG2 . ILE B 77  ? 0.7018  1.5300  1.0464  -0.0853 0.1647  -0.1392 86  ILE B CG2 
6797  C CD1 . ILE B 77  ? 0.7864  1.7479  1.1929  -0.0662 0.1099  -0.1840 86  ILE B CD1 
6809  N N   . THR B 78  ? 0.5971  1.0952  0.8092  -0.0798 0.1452  -0.0692 87  THR B N   
6810  C CA  . THR B 78  ? 0.7457  1.1634  0.9201  -0.1005 0.1628  -0.0474 87  THR B CA  
6811  C C   . THR B 78  ? 0.7280  1.0856  0.8567  -0.0600 0.1502  -0.0276 87  THR B C   
6812  O O   . THR B 78  ? 0.9601  1.2952  1.0591  -0.0598 0.1651  -0.0171 87  THR B O   
6813  C CB  . THR B 78  ? 1.0145  1.3588  1.1796  -0.1347 0.1641  -0.0387 87  THR B CB  
6814  O OG1 . THR B 78  ? 1.1134  1.5071  1.3169  -0.1791 0.1795  -0.0606 87  THR B OG1 
6815  C CG2 . THR B 78  ? 0.8800  1.1364  0.9987  -0.1465 0.1783  -0.0122 87  THR B CG2 
6823  N N   . MET B 79  ? 0.5383  0.8716  0.6592  -0.0265 0.1240  -0.0243 88  MET B N   
6824  C CA  . MET B 79  ? 0.5928  0.8640  0.6719  0.0056  0.1116  -0.0086 88  MET B CA  
6825  C C   . MET B 79  ? 0.6757  0.9877  0.7456  0.0374  0.1177  -0.0167 88  MET B C   
6826  O O   . MET B 79  ? 0.9200  1.1920  0.9520  0.0467  0.1228  -0.0081 88  MET B O   
6827  C CB  . MET B 79  ? 0.7010  0.9373  0.7772  0.0268  0.0873  -0.0038 88  MET B CB  
6828  C CG  . MET B 79  ? 0.9862  1.1760  1.0679  -0.0002 0.0825  0.0047  88  MET B CG  
6829  S SD  . MET B 79  ? 1.3299  1.4364  1.3754  -0.0159 0.0861  0.0276  88  MET B SD  
6830  C CE  . MET B 79  ? 2.2138  2.2684  2.2653  -0.0205 0.0711  0.0375  88  MET B CE  
6840  N N   . ALA B 80  ? 0.8343  1.2313  0.9384  0.0551  0.1178  -0.0349 89  ALA B N   
6841  C CA  . ALA B 80  ? 0.7077  1.1596  0.8108  0.0876  0.1276  -0.0456 89  ALA B CA  
6842  C C   . ALA B 80  ? 0.6626  1.1427  0.7660  0.0614  0.1571  -0.0480 89  ALA B C   
6843  O O   . ALA B 80  ? 0.7280  1.2023  0.8025  0.0852  0.1673  -0.0476 89  ALA B O   
6844  C CB  . ALA B 80  ? 1.3989  1.9481  1.5446  0.1117  0.1202  -0.0647 89  ALA B CB  
6850  N N   . TYR B 81  ? 0.5185  1.0244  0.6499  0.0119  0.1739  -0.0508 90  TYR B N   
6851  C CA  . TYR B 81  ? 0.7994  1.3252  0.9262  -0.0171 0.2071  -0.0499 90  TYR B CA  
6852  C C   . TYR B 81  ? 0.8723  1.2966  0.9349  -0.0202 0.2113  -0.0262 90  TYR B C   
6853  O O   . TYR B 81  ? 1.1143  1.5414  1.1476  -0.0108 0.2300  -0.0241 90  TYR B O   
6854  C CB  . TYR B 81  ? 0.7006  1.2679  0.8694  -0.0750 0.2274  -0.0585 90  TYR B CB  
6855  C CG  . TYR B 81  ? 0.8084  1.3951  0.9706  -0.1079 0.2674  -0.0558 90  TYR B CG  
6856  C CD1 . TYR B 81  ? 0.5950  1.2951  0.7985  -0.1079 0.2902  -0.0762 90  TYR B CD1 
6857  C CD2 . TYR B 81  ? 1.2752  1.7674  1.3861  -0.1344 0.2828  -0.0313 90  TYR B CD2 
6858  C CE1 . TYR B 81  ? 0.8963  1.6157  1.0923  -0.1393 0.3316  -0.0728 90  TYR B CE1 
6859  C CE2 . TYR B 81  ? 1.0360  1.5378  1.1309  -0.1625 0.3219  -0.0252 90  TYR B CE2 
6860  C CZ  . TYR B 81  ? 0.9564  1.5717  1.0942  -0.1669 0.3481  -0.0462 90  TYR B CZ  
6861  O OH  . TYR B 81  ? 0.7438  1.3684  0.8639  -0.1973 0.3916  -0.0390 90  TYR B OH  
6871  N N   . VAL B 82  ? 0.9162  1.2553  0.9557  -0.0313 0.1940  -0.0093 91  VAL B N   
6872  C CA  . VAL B 82  ? 1.0302  1.2810  1.0107  -0.0337 0.1941  0.0129  91  VAL B CA  
6873  C C   . VAL B 82  ? 0.8996  1.1224  0.8398  0.0088  0.1794  0.0130  91  VAL B C   
6874  O O   . VAL B 82  ? 0.8317  1.0373  0.7289  0.0142  0.1931  0.0175  91  VAL B O   
6875  C CB  . VAL B 82  ? 0.6897  0.8670  0.6615  -0.0504 0.1772  0.0293  91  VAL B CB  
6876  C CG1 . VAL B 82  ? 1.2633  1.3615  1.1781  -0.0392 0.1663  0.0494  91  VAL B CG1 
6877  C CG2 . VAL B 82  ? 1.0317  1.2087  1.0212  -0.0963 0.1996  0.0327  91  VAL B CG2 
6887  N N   . TRP B 83  ? 1.0553  1.2688  1.0042  0.0385  0.1531  0.0072  92  TRP B N   
6888  C CA  . TRP B 83  ? 1.0451  1.2090  0.9517  0.0729  0.1365  0.0076  92  TRP B CA  
6889  C C   . TRP B 83  ? 1.4389  1.6478  1.3409  0.1099  0.1462  -0.0097 92  TRP B C   
6890  O O   . TRP B 83  ? 1.6962  1.8594  1.5529  0.1356  0.1401  -0.0122 92  TRP B O   
6891  C CB  . TRP B 83  ? 0.9386  1.0580  0.8510  0.0848  0.1074  0.0117  92  TRP B CB  
6892  C CG  . TRP B 83  ? 0.8873  0.9589  0.8033  0.0569  0.0951  0.0281  92  TRP B CG  
6893  C CD1 . TRP B 83  ? 0.8287  0.9030  0.7796  0.0471  0.0847  0.0305  92  TRP B CD1 
6894  C CD2 . TRP B 83  ? 0.9335  0.9535  0.8164  0.0394  0.0935  0.0438  92  TRP B CD2 
6895  N NE1 . TRP B 83  ? 0.7901  0.8180  0.7337  0.0259  0.0789  0.0457  92  TRP B NE1 
6896  C CE2 . TRP B 83  ? 0.8187  0.8134  0.7213  0.0222  0.0827  0.0551  92  TRP B CE2 
6897  C CE3 . TRP B 83  ? 1.0490  1.0428  0.8836  0.0397  0.1000  0.0494  92  TRP B CE3 
6898  C CZ2 . TRP B 83  ? 1.1555  1.1009  1.0337  0.0089  0.0770  0.0729  92  TRP B CZ2 
6899  C CZ3 . TRP B 83  ? 1.2998  1.2451  1.1067  0.0251  0.0928  0.0676  92  TRP B CZ3 
6900  C CH2 . TRP B 83  ? 1.3298  1.2521  1.1599  0.0115  0.0810  0.0797  92  TRP B CH2 
6911  N N   . GLY B 84  ? 1.6489  1.9468  1.5966  0.1145  0.1603  -0.0234 93  GLY B N   
6912  C CA  . GLY B 84  ? 1.5812  1.9343  1.5278  0.1520  0.1741  -0.0396 93  GLY B CA  
6913  C C   . GLY B 84  ? 1.1609  1.4864  1.0908  0.2021  0.1545  -0.0456 93  GLY B C   
6914  O O   . GLY B 84  ? 0.8081  1.1384  0.7619  0.2127  0.1364  -0.0448 93  GLY B O   
6918  N N   . LYS B 85  ? 1.1249  1.4180  1.0083  0.2348  0.1606  -0.0521 94  LYS B N   
6919  C CA  . LYS B 85  ? 1.1701  1.4126  1.0251  0.2805  0.1448  -0.0564 94  LYS B CA  
6920  C C   . LYS B 85  ? 1.2500  1.3877  1.0723  0.2651  0.1210  -0.0438 94  LYS B C   
6921  O O   . LYS B 85  ? 1.0240  1.1022  0.8180  0.2939  0.1090  -0.0454 94  LYS B O   
6922  C CB  . LYS B 85  ? 1.1637  1.3974  0.9751  0.3208  0.1611  -0.0707 94  LYS B CB  
6923  C CG  . LYS B 85  ? 1.1852  1.5238  1.0316  0.3566  0.1805  -0.0856 94  LYS B CG  
6930  N N   . GLY B 86  ? 0.9377  1.0509  0.7626  0.2208  0.1154  -0.0313 95  GLY B N   
6931  C CA  . GLY B 86  ? 1.3529  1.3817  1.1532  0.2061  0.0935  -0.0212 95  GLY B CA  
6932  C C   . GLY B 86  ? 1.3069  1.2647  1.0460  0.2120  0.0892  -0.0268 95  GLY B C   
6933  O O   . GLY B 86  ? 1.3793  1.2684  1.0974  0.2104  0.0704  -0.0256 95  GLY B O   
6937  N N   . HIS B 87  ? 0.7985  0.7720  0.5078  0.2152  0.1067  -0.0342 96  HIS B N   
6938  C CA  . HIS B 87  ? 0.8631  0.7740  0.5077  0.2225  0.1031  -0.0438 96  HIS B CA  
6939  C C   . HIS B 87  ? 1.0535  0.9688  0.6703  0.1972  0.1110  -0.0368 96  HIS B C   
6940  O O   . HIS B 87  ? 1.2318  1.1168  0.7910  0.2082  0.1157  -0.0482 96  HIS B O   
6941  C CB  . HIS B 87  ? 1.1122  1.0223  0.7254  0.2667  0.1188  -0.0640 96  HIS B CB  
6942  C CG  . HIS B 87  ? 1.2481  1.1381  0.8730  0.2994  0.1118  -0.0690 96  HIS B CG  
6943  N ND1 . HIS B 87  ? 1.4841  1.4416  1.1456  0.3315  0.1248  -0.0719 96  HIS B ND1 
6944  C CD2 . HIS B 87  ? 1.4094  1.2193  1.0128  0.3042  0.0937  -0.0701 96  HIS B CD2 
6945  C CE1 . HIS B 87  ? 1.7587  1.6727  1.4136  0.3598  0.1146  -0.0724 96  HIS B CE1 
6946  N NE2 . HIS B 87  ? 2.6853  2.5059  2.3047  0.3415  0.0978  -0.0708 96  HIS B NE2 
6953  N N   . GLY B 88  ? 1.3023  1.2531  0.9534  0.1662  0.1157  -0.0190 97  GLY B N   
6954  C CA  . GLY B 88  ? 1.1391  1.0761  0.7572  0.1414  0.1201  -0.0057 97  GLY B CA  
6955  C C   . GLY B 88  ? 1.4572  1.4492  1.0759  0.1319  0.1555  -0.0014 97  GLY B C   
6956  O O   . GLY B 88  ? 1.7737  1.7459  1.3556  0.1130  0.1620  0.0129  97  GLY B O   
6960  N N   . ASP B 89  ? 1.8950  1.9571  1.5518  0.1450  0.1794  -0.0130 98  ASP B N   
6961  C CA  . ASP B 89  ? 1.6751  1.8013  1.3457  0.1279  0.2163  -0.0098 98  ASP B CA  
6962  C C   . ASP B 89  ? 1.4161  1.5707  1.1430  0.0897  0.2195  0.0044  98  ASP B C   
6963  O O   . ASP B 89  ? 0.9758  1.1909  0.7646  0.0888  0.2218  -0.0044 98  ASP B O   
6964  C CB  . ASP B 89  ? 1.1747  1.3739  0.8662  0.1593  0.2396  -0.0314 98  ASP B CB  
6967  N N   . VAL B 90  ? 1.4953  1.6052  1.1972  0.0590  0.2202  0.0259  99  VAL B N   
6968  C CA  . VAL B 90  ? 1.2609  1.3648  1.0036  0.0272  0.2140  0.0396  99  VAL B CA  
6969  C C   . VAL B 90  ? 1.1791  1.3223  0.9379  -0.0085 0.2524  0.0464  99  VAL B C   
6970  O O   . VAL B 90  ? 1.4303  1.5557  1.1401  -0.0182 0.2765  0.0578  99  VAL B O   
6971  C CB  . VAL B 90  ? 1.3000  1.3214  1.0062  0.0198  0.1876  0.0602  99  VAL B CB  
6972  C CG1 . VAL B 90  ? 1.2368  1.2472  0.9798  -0.0114 0.1873  0.0748  99  VAL B CG1 
6973  C CG2 . VAL B 90  ? 1.3485  1.3329  1.0447  0.0462  0.1509  0.0524  99  VAL B CG2 
6983  N N   . ARG B 91  ? 1.0745  1.2638  0.8969  -0.0316 0.2581  0.0403  100 ARG B N   
6984  C CA  . ARG B 91  ? 1.1337  1.3498  0.9749  -0.0755 0.2936  0.0459  100 ARG B CA  
6985  C C   . ARG B 91  ? 1.0587  1.1973  0.8855  -0.1031 0.2854  0.0684  100 ARG B C   
6986  O O   . ARG B 91  ? 0.8719  0.9899  0.7244  -0.0985 0.2567  0.0671  100 ARG B O   
6987  C CB  . ARG B 91  ? 1.0466  1.3680  0.9662  -0.0867 0.3062  0.0207  100 ARG B CB  
6988  C CG  . ARG B 91  ? 1.6172  2.0264  1.5492  -0.0682 0.3316  0.0024  100 ARG B CG  
6995  N N   . LYS B 92  ? 1.2784  1.3712  1.0598  -0.1287 0.3124  0.0899  101 LYS B N   
6996  C CA  . LYS B 92  ? 1.2975  1.3067  1.0529  -0.1494 0.3091  0.1148  101 LYS B CA  
6997  C C   . LYS B 92  ? 1.3802  1.3991  1.1720  -0.1992 0.3403  0.1136  101 LYS B C   
6998  O O   . LYS B 92  ? 1.3187  1.2621  1.0889  -0.2168 0.3416  0.1331  101 LYS B O   
6999  C CB  . LYS B 92  ? 1.3588  1.2949  1.0272  -0.1420 0.3180  0.1437  101 LYS B CB  
7000  C CG  . LYS B 92  ? 1.8892  1.8128  1.5129  -0.0986 0.2892  0.1421  101 LYS B CG  
7007  N N   . VAL B 93  ? 1.6992  1.8090  1.5461  -0.2220 0.3650  0.0896  102 VAL B N   
7008  C CA  . VAL B 93  ? 1.3033  1.4288  1.1873  -0.2768 0.3968  0.0834  102 VAL B CA  
7009  C C   . VAL B 93  ? 1.0358  1.2583  1.0041  -0.2813 0.3826  0.0484  102 VAL B C   
7010  O O   . VAL B 93  ? 1.4760  1.7943  1.4799  -0.2612 0.3817  0.0271  102 VAL B O   
7011  C CB  . VAL B 93  ? 1.4527  1.6047  1.3212  -0.3116 0.4494  0.0881  102 VAL B CB  
7012  C CG1 . VAL B 93  ? 1.4489  1.6037  1.3609  -0.3615 0.4660  0.0805  102 VAL B CG1 
7013  C CG2 . VAL B 93  ? 1.7618  1.8211  1.5360  -0.2987 0.4616  0.1238  102 VAL B CG2 
7023  N N   . LEU B 94  ? 0.9851  1.1849  0.9804  -0.3046 0.3735  0.0424  103 LEU B N   
7024  C CA  . LEU B 94  ? 0.7862  1.0783  0.8561  -0.3089 0.3580  0.0088  103 LEU B CA  
7025  C C   . LEU B 94  ? 1.3517  1.7133  1.4699  -0.3656 0.3943  -0.0123 103 LEU B C   
7026  O O   . LEU B 94  ? 1.2812  1.5706  1.3792  -0.4002 0.4092  -0.0007 103 LEU B O   
7027  C CB  . LEU B 94  ? 0.8701  1.1086  0.9464  -0.3044 0.3273  0.0081  103 LEU B CB  
7028  C CG  . LEU B 94  ? 0.7636  1.0889  0.9000  -0.2871 0.2987  -0.0222 103 LEU B CG  
7029  C CD1 . LEU B 94  ? 0.6802  1.0376  0.8105  -0.2270 0.2708  -0.0216 103 LEU B CD1 
7030  C CD2 . LEU B 94  ? 0.6760  0.9478  0.8159  -0.2932 0.2784  -0.0240 103 LEU B CD2 
7042  N N   . PRO B 95  ? 1.3850  1.8691  1.5621  -0.3573 0.3915  -0.0404 104 PRO B N   
7043  C CA  . PRO B 95  ? 1.2446  1.7844  1.4627  -0.3939 0.4101  -0.0572 104 PRO B CA  
7044  C C   . PRO B 95  ? 1.0738  1.5839  1.3147  -0.4380 0.4052  -0.0714 104 PRO B C   
7045  O O   . PRO B 95  ? 1.0822  1.6118  1.3514  -0.4331 0.3774  -0.0903 104 PRO B O   
7046  C CB  . PRO B 95  ? 1.0131  1.6907  1.2917  -0.3638 0.3957  -0.0863 104 PRO B CB  
7047  C CG  . PRO B 95  ? 0.7455  1.4248  0.9951  -0.3098 0.3842  -0.0760 104 PRO B CG  
7048  C CD  . PRO B 95  ? 1.3343  1.9008  1.5294  -0.3053 0.3732  -0.0525 104 PRO B CD  
7056  N N   . ARG B 96  ? 1.4052  1.7896  1.4865  -0.4284 0.2825  -0.3292 105 ARG B N   
7057  C CA  . ARG B 96  ? 1.1371  1.4856  1.2136  -0.4654 0.2955  -0.3352 105 ARG B CA  
7058  C C   . ARG B 96  ? 1.0286  1.4480  1.1499  -0.4577 0.2823  -0.3671 105 ARG B C   
7059  O O   . ARG B 96  ? 1.0060  1.3858  1.1272  -0.4516 0.2734  -0.3663 105 ARG B O   
7060  C CB  . ARG B 96  ? 1.8243  2.1765  1.8837  -0.5252 0.3295  -0.3414 105 ARG B CB  
7063  N N   . ASN B 97  ? 1.4636  1.9917  1.6227  -0.4513 0.2791  -0.3946 106 ASN B N   
7064  C CA  . ASN B 97  ? 1.2288  1.8391  1.4305  -0.4429 0.2664  -0.4260 106 ASN B CA  
7065  C C   . ASN B 97  ? 1.7642  2.3355  1.9678  -0.3995 0.2408  -0.4133 106 ASN B C   
7066  O O   . ASN B 97  ? 0.7105  1.2985  0.9276  -0.4037 0.2346  -0.4296 106 ASN B O   
7067  C CB  . ASN B 97  ? 1.0718  1.7952  1.3105  -0.4198 0.2596  -0.4481 106 ASN B CB  
7070  N N   . ILE B 98  ? 1.6800  2.1985  1.8687  -0.3593 0.2263  -0.3841 107 ILE B N   
7071  C CA  . ILE B 98  ? 1.0150  1.5043  1.2087  -0.3173 0.2032  -0.3701 107 ILE B CA  
7072  C C   . ILE B 98  ? 1.1344  1.5137  1.2922  -0.3176 0.2045  -0.3393 107 ILE B C   
7073  O O   . ILE B 98  ? 0.6783  1.0300  0.8367  -0.3005 0.1938  -0.3334 107 ILE B O   
7074  C CB  . ILE B 98  ? 1.0538  1.5747  1.2666  -0.2669 0.1829  -0.3625 107 ILE B CB  
7075  C CG1 . ILE B 98  ? 0.9873  1.4740  1.2044  -0.2263 0.1615  -0.3438 107 ILE B CG1 
7076  C CG2 . ILE B 98  ? 1.3826  1.8645  1.5732  -0.2644 0.1877  -0.3444 107 ILE B CG2 
7077  C CD1 . ILE B 98  ? 0.5557  1.0767  0.7958  -0.1792 0.1425  -0.3397 107 ILE B CD1 
7089  N N   . ALA B 99  ? 1.3302  1.6507  1.4560  -0.3328 0.2169  -0.3190 108 ALA B N   
7090  C CA  . ALA B 99  ? 1.2396  1.4592  1.3313  -0.3263 0.2162  -0.2875 108 ALA B CA  
7091  C C   . ALA B 99  ? 1.5257  1.6974  1.6024  -0.3548 0.2288  -0.2929 108 ALA B C   
7092  O O   . ALA B 99  ? 2.2987  2.4199  2.3679  -0.3346 0.2196  -0.2800 108 ALA B O   
7093  C CB  . ALA B 99  ? 1.1546  1.3296  1.2119  -0.3370 0.2272  -0.2654 108 ALA B CB  
7099  N N   . VAL B 100 ? 1.1417  1.3307  1.2155  -0.4026 0.2507  -0.3142 109 VAL B N   
7100  C CA  . VAL B 100 ? 1.0532  1.1844  1.1091  -0.4344 0.2650  -0.3214 109 VAL B CA  
7101  C C   . VAL B 100 ? 1.5124  1.6697  1.5912  -0.4131 0.2484  -0.3395 109 VAL B C   
7102  O O   . VAL B 100 ? 1.6619  1.7489  1.7219  -0.3993 0.2450  -0.3267 109 VAL B O   
7103  C CB  . VAL B 100 ? 1.2647  1.4181  1.3191  -0.4944 0.2922  -0.3444 109 VAL B CB  
7104  C CG1 . VAL B 100 ? 0.9907  1.0868  1.0313  -0.5294 0.3061  -0.3588 109 VAL B CG1 
7105  C CG2 . VAL B 100 ? 0.9732  1.0838  0.9939  -0.5129 0.3108  -0.3182 109 VAL B CG2 
7115  N N   . PRO B 101 ? 1.1752  1.4335  1.2922  -0.4071 0.2379  -0.3686 110 PRO B N   
7116  C CA  . PRO B 101 ? 0.9989  1.2837  1.1319  -0.3872 0.2229  -0.3849 110 PRO B CA  
7117  C C   . PRO B 101 ? 1.4353  1.6842  1.5637  -0.3345 0.2031  -0.3562 110 PRO B C   
7118  O O   . PRO B 101 ? 0.8688  1.0945  0.9915  -0.3229 0.1978  -0.3593 110 PRO B O   
7119  C CB  . PRO B 101 ? 0.7471  1.1549  0.9209  -0.3832 0.2135  -0.4151 110 PRO B CB  
7120  C CG  . PRO B 101 ? 1.9958  2.4352  2.1776  -0.3792 0.2161  -0.4061 110 PRO B CG  
7121  C CD  . PRO B 101 ? 1.6659  2.0228  1.8125  -0.4111 0.2375  -0.3865 110 PRO B CD  
7129  N N   . TYR B 102 ? 1.2112  1.4591  1.3433  -0.3027 0.1923  -0.3303 111 TYR B N   
7130  C CA  . TYR B 102 ? 1.0984  1.3103  1.2283  -0.2579 0.1754  -0.3023 111 TYR B CA  
7131  C C   . TYR B 102 ? 0.9053  1.0203  1.0021  -0.2632 0.1839  -0.2829 111 TYR B C   
7132  O O   . TYR B 102 ? 0.7999  0.8926  0.8948  -0.2397 0.1761  -0.2755 111 TYR B O   
7133  C CB  . TYR B 102 ? 1.3095  1.5304  1.4489  -0.2284 0.1632  -0.2803 111 TYR B CB  
7134  C CG  . TYR B 102 ? 0.9077  1.1020  1.0528  -0.1836 0.1449  -0.2518 111 TYR B CG  
7135  C CD1 . TYR B 102 ? 0.9212  1.1287  1.0766  -0.1606 0.1354  -0.2513 111 TYR B CD1 
7136  C CD2 . TYR B 102 ? 0.8525  1.0160  0.9940  -0.1658 0.1374  -0.2270 111 TYR B CD2 
7137  C CE1 . TYR B 102 ? 0.8895  1.0773  1.0521  -0.1239 0.1217  -0.2243 111 TYR B CE1 
7138  C CE2 . TYR B 102 ? 1.1712  1.3156  1.3226  -0.1306 0.1220  -0.2030 111 TYR B CE2 
7139  C CZ  . TYR B 102 ? 1.4453  1.6014  1.6079  -0.1107 0.1153  -0.2005 111 TYR B CZ  
7140  O OH  . TYR B 102 ? 1.5414  1.6809  1.7153  -0.0791 0.1026  -0.1750 111 TYR B OH  
7150  N N   . CYS B 103 ? 0.9444  1.0024  1.0134  -0.2929 0.2012  -0.2743 112 CYS B N   
7151  C CA  . CYS B 103 ? 1.1808  1.1402  1.2146  -0.2953 0.2102  -0.2534 112 CYS B CA  
7152  C C   . CYS B 103 ? 1.4399  1.3730  1.4648  -0.3151 0.2205  -0.2764 112 CYS B C   
7153  O O   . CYS B 103 ? 1.6891  1.5509  1.6922  -0.3021 0.2225  -0.2630 112 CYS B O   
7154  C CB  . CYS B 103 ? 1.1539  1.0607  1.1564  -0.3221 0.2273  -0.2374 112 CYS B CB  
7155  S SG  . CYS B 103 ? 1.0074  0.9140  1.0033  -0.2977 0.2169  -0.2058 112 CYS B SG  
7161  N N   . GLN B 104 ? 1.1695  1.1613  1.2114  -0.3464 0.2269  -0.3131 113 GLN B N   
7162  C CA  . GLN B 104 ? 1.3108  1.2832  1.3455  -0.3689 0.2357  -0.3416 113 GLN B CA  
7163  C C   . GLN B 104 ? 1.4911  1.4874  1.5372  -0.3291 0.2181  -0.3457 113 GLN B C   
7164  O O   . GLN B 104 ? 0.9277  0.8760  0.9565  -0.3297 0.2230  -0.3558 113 GLN B O   
7165  C CB  . GLN B 104 ? 0.9356  0.9761  0.9893  -0.4169 0.2466  -0.3828 113 GLN B CB  
7166  C CG  . GLN B 104 ? 1.0062  0.9909  1.0370  -0.4708 0.2738  -0.3842 113 GLN B CG  
7167  C CD  . GLN B 104 ? 1.0257  1.0820  1.0793  -0.5244 0.2867  -0.4273 113 GLN B CD  
7174  N N   . LEU B 105 ? 1.2261  1.3009  1.3010  -0.2964 0.1989  -0.3414 114 LEU B N   
7175  C CA  . LEU B 105 ? 1.0886  1.1957  1.1741  -0.2587 0.1832  -0.3424 114 LEU B CA  
7176  C C   . LEU B 105 ? 1.2016  1.2430  1.2724  -0.2214 0.1781  -0.3055 114 LEU B C   
7177  O O   . LEU B 105 ? 0.9148  0.9437  0.9788  -0.2006 0.1751  -0.3069 114 LEU B O   
7178  C CB  . LEU B 105 ? 1.1109  1.3170  1.2295  -0.2364 0.1663  -0.3462 114 LEU B CB  
7179  C CG  . LEU B 105 ? 1.4945  1.7542  1.6268  -0.1966 0.1493  -0.3453 114 LEU B CG  
7180  C CD1 . LEU B 105 ? 1.4516  1.7351  1.5769  -0.2126 0.1526  -0.3816 114 LEU B CD1 
7181  C CD2 . LEU B 105 ? 1.9760  2.3231  2.1383  -0.1762 0.1348  -0.3456 114 LEU B CD2 
7193  N N   . SER B 106 ? 1.4053  1.4066  1.4702  -0.2139 0.1780  -0.2743 115 SER B N   
7194  C CA  . SER B 106 ? 1.7980  1.7445  1.8527  -0.1805 0.1726  -0.2402 115 SER B CA  
7195  C C   . SER B 106 ? 1.2053  1.0700  1.2288  -0.1873 0.1861  -0.2412 115 SER B C   
7196  O O   . SER B 106 ? 1.3822  1.2293  1.4024  -0.1587 0.1823  -0.2330 115 SER B O   
7197  C CB  . SER B 106 ? 1.8446  1.7724  1.8989  -0.1749 0.1686  -0.2118 115 SER B CB  
7198  O OG  . SER B 106 ? 0.9055  0.9027  0.9889  -0.1628 0.1554  -0.2116 115 SER B OG  
7204  N N   . LYS B 107 ? 1.2055  1.0182  1.2051  -0.2247 0.2035  -0.2512 116 LYS B N   
7205  C CA  . LYS B 107 ? 1.1961  0.9201  1.1631  -0.2312 0.2179  -0.2532 116 LYS B CA  
7206  C C   . LYS B 107 ? 1.4115  1.1526  1.3813  -0.2243 0.2172  -0.2826 116 LYS B C   
7207  O O   . LYS B 107 ? 1.4118  1.1066  1.3673  -0.1971 0.2180  -0.2742 116 LYS B O   
7208  C CB  . LYS B 107 ? 1.1609  0.8312  1.1032  -0.2799 0.2392  -0.2642 116 LYS B CB  
7209  C CG  . LYS B 107 ? 1.3622  0.9212  1.2652  -0.2902 0.2574  -0.2642 116 LYS B CG  
7216  N N   . LYS B 108 ? 1.0380  0.8559  1.0278  -0.2432 0.2138  -0.3169 117 LYS B N   
7217  C CA  . LYS B 108 ? 1.0199  0.8625  1.0097  -0.2371 0.2119  -0.3480 117 LYS B CA  
7218  C C   . LYS B 108 ? 1.8056  1.6697  1.8027  -0.1851 0.1983  -0.3267 117 LYS B C   
7219  O O   . LYS B 108 ? 1.6364  1.4722  1.6179  -0.1689 0.2019  -0.3366 117 LYS B O   
7220  C CB  . LYS B 108 ? 0.9458  0.8845  0.9593  -0.2605 0.2062  -0.3851 117 LYS B CB  
7223  N N   . LEU B 109 ? 1.5876  1.4988  1.6079  -0.1590 0.1841  -0.2976 118 LEU B N   
7224  C CA  . LEU B 109 ? 1.2461  1.1860  1.2779  -0.1135 0.1721  -0.2751 118 LEU B CA  
7225  C C   . LEU B 109 ? 1.1587  1.0343  1.1820  -0.0877 0.1734  -0.2377 118 LEU B C   
7226  O O   . LEU B 109 ? 1.0479  0.9465  1.0842  -0.0523 0.1650  -0.2152 118 LEU B O   
7227  C CB  . LEU B 109 ? 0.9275  0.9508  0.9906  -0.0982 0.1561  -0.2634 118 LEU B CB  
7228  C CG  . LEU B 109 ? 0.7617  0.8729  0.8391  -0.1080 0.1494  -0.2953 118 LEU B CG  
7229  C CD1 . LEU B 109 ? 0.6857  0.8573  0.7907  -0.0963 0.1363  -0.2807 118 LEU B CD1 
7230  C CD2 . LEU B 109 ? 0.8045  0.9622  0.8788  -0.0848 0.1443  -0.3090 118 LEU B CD2 
7242  N N   . GLU B 110 ? 1.1438  0.9438  1.1464  -0.1038 0.1836  -0.2288 119 GLU B N   
7243  C CA  . GLU B 110 ? 1.5988  1.3430  1.5925  -0.0766 0.1833  -0.1945 119 GLU B CA  
7244  C C   . GLU B 110 ? 1.1908  0.9760  1.2120  -0.0543 0.1676  -0.1615 119 GLU B C   
7245  O O   . GLU B 110 ? 1.1109  0.8840  1.1383  -0.0237 0.1623  -0.1344 119 GLU B O   
7246  C CB  . GLU B 110 ? 0.9110  0.6320  0.8937  -0.0480 0.1879  -0.1978 119 GLU B CB  
7247  C CG  . GLU B 110 ? 1.1984  0.8601  1.1498  -0.0671 0.2043  -0.2306 119 GLU B CG  
7248  C CD  . GLU B 110 ? 1.5983  1.2196  1.5341  -0.0326 0.2103  -0.2292 119 GLU B CD  
7249  O OE1 . GLU B 110 ? 1.9422  1.5257  1.8751  -0.0041 0.2093  -0.1972 119 GLU B OE1 
7250  O OE2 . GLU B 110 ? 1.3024  0.9347  1.2290  -0.0330 0.2156  -0.2623 119 GLU B OE2 
7257  N N   . LEU B 111 ? 1.3063  1.1410  1.3457  -0.0700 0.1603  -0.1655 120 LEU B N   
7258  C CA  . LEU B 111 ? 1.0200  0.8865  1.0838  -0.0553 0.1463  -0.1401 120 LEU B CA  
7259  C C   . LEU B 111 ? 0.8151  0.6639  0.8712  -0.0790 0.1475  -0.1364 120 LEU B C   
7260  O O   . LEU B 111 ? 1.1688  0.9974  1.2060  -0.1109 0.1598  -0.1555 120 LEU B O   
7261  C CB  . LEU B 111 ? 0.9379  0.8826  1.0308  -0.0444 0.1354  -0.1463 120 LEU B CB  
7262  C CG  . LEU B 111 ? 1.7912  1.7593  1.8938  -0.0133 0.1320  -0.1370 120 LEU B CG  
7263  C CD1 . LEU B 111 ? 0.6351  0.6740  0.7537  -0.0048 0.1256  -0.1485 120 LEU B CD1 
7264  C CD2 . LEU B 111 ? 2.3661  2.3260  2.4858  0.0113  0.1240  -0.1019 120 LEU B CD2 
7276  N N   . PRO B 112 ? 0.8085  0.6654  0.8785  -0.0658 0.1359  -0.1128 121 PRO B N   
7277  C CA  . PRO B 112 ? 0.8820  0.7299  0.9429  -0.0859 0.1364  -0.1104 121 PRO B CA  
7278  C C   . PRO B 112 ? 1.0698  0.9784  1.1496  -0.1007 0.1332  -0.1301 121 PRO B C   
7279  O O   . PRO B 112 ? 0.7521  0.7145  0.8591  -0.0861 0.1237  -0.1360 121 PRO B O   
7280  C CB  . PRO B 112 ? 0.7352  0.5727  0.8049  -0.0623 0.1230  -0.0806 121 PRO B CB  
7281  C CG  . PRO B 112 ? 1.1376  1.0038  1.2355  -0.0335 0.1134  -0.0704 121 PRO B CG  
7282  C CD  . PRO B 112 ? 1.0475  0.9108  1.1370  -0.0329 0.1239  -0.0859 121 PRO B CD  
7290  N N   . PRO B 113 ? 1.2019  1.1041  1.2656  -0.1300 0.1418  -0.1387 122 PRO B N   
7291  C CA  . PRO B 113 ? 1.0800  1.0427  1.1619  -0.1414 0.1392  -0.1567 122 PRO B CA  
7292  C C   . PRO B 113 ? 1.2955  1.2808  1.3974  -0.1185 0.1226  -0.1422 122 PRO B C   
7293  O O   . PRO B 113 ? 0.8085  0.8002  0.9049  -0.1274 0.1223  -0.1428 122 PRO B O   
7294  C CB  . PRO B 113 ? 1.5471  1.4864  1.6016  -0.1779 0.1566  -0.1656 122 PRO B CB  
7295  C CG  . PRO B 113 ? 1.2634  1.1287  1.2870  -0.1728 0.1598  -0.1383 122 PRO B CG  
7296  C CD  . PRO B 113 ? 1.0447  0.8833  1.0721  -0.1477 0.1542  -0.1277 122 PRO B CD  
7304  N N   . ILE B 114 ? 1.2248  1.2222  1.3495  -0.0897 0.1095  -0.1299 123 ILE B N   
7305  C CA  . ILE B 114 ? 0.9775  0.9991  1.1274  -0.0691 0.0939  -0.1202 123 ILE B CA  
7306  C C   . ILE B 114 ? 0.7829  0.8338  0.9581  -0.0462 0.0865  -0.1164 123 ILE B C   
7307  O O   . ILE B 114 ? 0.7860  0.8299  0.9559  -0.0421 0.0917  -0.1149 123 ILE B O   
7308  C CB  . ILE B 114 ? 1.1681  1.1533  1.3146  -0.0582 0.0846  -0.0962 123 ILE B CB  
7309  C CG1 . ILE B 114 ? 0.9184  0.9306  1.0921  -0.0439 0.0696  -0.0949 123 ILE B CG1 
7310  C CG2 . ILE B 114 ? 1.5789  1.5369  1.7282  -0.0407 0.0822  -0.0751 123 ILE B CG2 
7311  C CD1 . ILE B 114 ? 0.7087  0.6967  0.8772  -0.0413 0.0600  -0.0818 123 ILE B CD1 
7323  N N   . LEU B 115 ? 0.8506  0.9339  1.0508  -0.0308 0.0754  -0.1160 124 LEU B N   
7324  C CA  . LEU B 115 ? 0.8509  0.9593  1.0738  -0.0066 0.0683  -0.1066 124 LEU B CA  
7325  C C   . LEU B 115 ? 0.9314  1.0085  1.1615  0.0082  0.0639  -0.0783 124 LEU B C   
7326  O O   . LEU B 115 ? 1.3675  1.4206  1.6042  0.0097  0.0566  -0.0649 124 LEU B O   
7327  C CB  . LEU B 115 ? 0.5403  0.6795  0.7853  0.0065  0.0585  -0.1115 124 LEU B CB  
7328  C CG  . LEU B 115 ? 0.5079  0.6756  0.7739  0.0333  0.0518  -0.1013 124 LEU B CG  
7329  C CD1 . LEU B 115 ? 0.5778  0.7972  0.8399  0.0359  0.0561  -0.1201 124 LEU B CD1 
7330  C CD2 . LEU B 115 ? 0.6337  0.8047  0.9204  0.0491  0.0414  -0.0973 124 LEU B CD2 
7342  N N   . VAL B 116 ? 0.7243  0.8071  0.9538  0.0188  0.0683  -0.0709 125 VAL B N   
7343  C CA  . VAL B 116 ? 0.7755  0.8402  1.0153  0.0340  0.0662  -0.0447 125 VAL B CA  
7344  C C   . VAL B 116 ? 0.8166  0.9132  1.0759  0.0552  0.0635  -0.0316 125 VAL B C   
7345  O O   . VAL B 116 ? 1.0241  1.1551  1.2850  0.0608  0.0626  -0.0429 125 VAL B O   
7346  C CB  . VAL B 116 ? 0.6914  0.7289  0.9094  0.0311  0.0764  -0.0434 125 VAL B CB  
7347  C CG1 . VAL B 116 ? 0.6511  0.6485  0.8434  0.0112  0.0811  -0.0521 125 VAL B CG1 
7348  C CG2 . VAL B 116 ? 0.5926  0.6524  0.7988  0.0336  0.0850  -0.0581 125 VAL B CG2 
7358  N N   . TYR B 117 ? 0.7691  0.8568  1.0429  0.0677  0.0629  -0.0062 126 TYR B N   
7359  C CA  . TYR B 117 ? 0.6961  0.8092  0.9869  0.0871  0.0627  0.0129  126 TYR B CA  
7360  C C   . TYR B 117 ? 0.7051  0.8509  0.9790  0.0971  0.0703  0.0040  126 TYR B C   
7361  O O   . TYR B 117 ? 0.6881  0.8635  0.9691  0.1133  0.0687  0.0138  126 TYR B O   
7362  C CB  . TYR B 117 ? 0.4689  0.5695  0.7773  0.0938  0.0640  0.0403  126 TYR B CB  
7363  C CG  . TYR B 117 ? 0.4694  0.5931  0.7942  0.1114  0.0682  0.0662  126 TYR B CG  
7364  C CD1 . TYR B 117 ? 0.4771  0.6203  0.7897  0.1234  0.0792  0.0719  126 TYR B CD1 
7365  C CD2 . TYR B 117 ? 0.4686  0.5898  0.8206  0.1151  0.0626  0.0868  126 TYR B CD2 
7366  C CE1 . TYR B 117 ? 0.9138  1.0803  1.2395  0.1392  0.0854  0.0993  126 TYR B CE1 
7367  C CE2 . TYR B 117 ? 0.4764  0.6138  0.8425  0.1287  0.0691  0.1156  126 TYR B CE2 
7368  C CZ  . TYR B 117 ? 0.4817  0.6446  0.8337  0.1407  0.0808  0.1225  126 TYR B CZ  
7369  O OH  . TYR B 117 ? 0.8261  1.0093  1.1883  0.1541  0.0896  0.1523  126 TYR B OH  
7379  N N   . ALA B 118 ? 0.9823  1.1221  1.2327  0.0892  0.0785  -0.0134 127 ALA B N   
7380  C CA  . ALA B 118 ? 0.9445  1.1186  1.1792  0.0991  0.0847  -0.0240 127 ALA B CA  
7381  C C   . ALA B 118 ? 1.2209  1.4327  1.4504  0.0951  0.0800  -0.0481 127 ALA B C   
7382  O O   . ALA B 118 ? 0.5368  0.7904  0.7582  0.1085  0.0809  -0.0535 127 ALA B O   
7383  C CB  . ALA B 118 ? 0.7550  0.9078  0.9657  0.0928  0.0955  -0.0386 127 ALA B CB  
7389  N N   . ASP B 119 ? 0.8339  1.0382  1.0685  0.0794  0.0748  -0.0621 128 ASP B N   
7390  C CA  . ASP B 119 ? 0.8148  1.0634  1.0514  0.0784  0.0695  -0.0837 128 ASP B CA  
7391  C C   . ASP B 119 ? 0.8088  1.0804  1.0655  0.1038  0.0600  -0.0639 128 ASP B C   
7392  O O   . ASP B 119 ? 0.8684  1.1829  1.1233  0.1241  0.0574  -0.0610 128 ASP B O   
7393  C CB  . ASP B 119 ? 0.8036  1.0385  1.0388  0.0532  0.0696  -0.1051 128 ASP B CB  
7394  C CG  . ASP B 119 ? 0.9541  1.1676  1.1667  0.0254  0.0803  -0.1276 128 ASP B CG  
7395  O OD1 . ASP B 119 ? 1.1011  1.3358  1.3002  0.0219  0.0858  -0.1450 128 ASP B OD1 
7396  O OD2 . ASP B 119 ? 1.0326  1.2089  1.2396  0.0064  0.0833  -0.1293 128 ASP B OD2 
7401  N N   . CYS B 120 ? 0.6868  0.9280  0.9608  0.1034  0.0544  -0.0506 129 CYS B N   
7402  C CA  . CYS B 120 ? 0.7472  0.9956  1.0403  0.1237  0.0457  -0.0363 129 CYS B CA  
7403  C C   . CYS B 120 ? 0.8980  1.1375  1.2010  0.1452  0.0461  0.0001  129 CYS B C   
7404  O O   . CYS B 120 ? 1.0642  1.2989  1.3823  0.1624  0.0401  0.0158  129 CYS B O   
7405  C CB  . CYS B 120 ? 0.8211  1.0333  1.1274  0.1123  0.0404  -0.0386 129 CYS B CB  
7406  S SG  . CYS B 120 ? 0.8998  1.0542  1.2157  0.0989  0.0404  -0.0169 129 CYS B SG  
7412  N N   . VAL B 121 ? 0.8397  1.0746  1.1348  0.1449  0.0542  0.0142  130 VAL B N   
7413  C CA  . VAL B 121 ? 0.6411  0.8800  0.9427  0.1648  0.0580  0.0486  130 VAL B CA  
7414  C C   . VAL B 121 ? 0.5709  0.8510  0.8498  0.1770  0.0652  0.0464  130 VAL B C   
7415  O O   . VAL B 121 ? 0.7554  1.0618  1.0307  0.2003  0.0662  0.0675  130 VAL B O   
7416  C CB  . VAL B 121 ? 0.5030  0.7028  0.8229  0.1561  0.0620  0.0739  130 VAL B CB  
7417  C CG1 . VAL B 121 ? 0.5484  0.7578  0.8762  0.1744  0.0685  0.1105  130 VAL B CG1 
7418  C CG2 . VAL B 121 ? 0.7759  0.9373  1.1190  0.1444  0.0534  0.0763  130 VAL B CG2 
7428  N N   . LEU B 122 ? 0.5518  0.8348  0.8131  0.1629  0.0710  0.0230  131 LEU B N   
7429  C CA  . LEU B 122 ? 0.8325  1.1510  1.0726  0.1760  0.0784  0.0217  131 LEU B CA  
7430  C C   . LEU B 122 ? 0.7473  1.1180  0.9697  0.1811  0.0732  -0.0073 131 LEU B C   
7431  O O   . LEU B 122 ? 0.7710  1.1855  0.9762  0.1996  0.0751  -0.0056 131 LEU B O   
7432  C CB  . LEU B 122 ? 0.7547  1.0484  0.9837  0.1628  0.0884  0.0117  131 LEU B CB  
7433  C CG  . LEU B 122 ? 0.6247  0.8755  0.8723  0.1580  0.0926  0.0365  131 LEU B CG  
7434  C CD1 . LEU B 122 ? 0.9863  1.2158  1.2183  0.1504  0.1019  0.0220  131 LEU B CD1 
7435  C CD2 . LEU B 122 ? 0.5970  0.8612  0.8594  0.1769  0.0974  0.0752  131 LEU B CD2 
7447  N N   . ALA B 123 ? 0.6560  1.0294  0.8837  0.1662  0.0661  -0.0332 132 ALA B N   
7448  C CA  . ALA B 123 ? 0.7138  1.1422  0.9304  0.1648  0.0608  -0.0668 132 ALA B CA  
7449  C C   . ALA B 123 ? 0.7857  1.2423  1.0178  0.1814  0.0494  -0.0629 132 ALA B C   
7450  O O   . ALA B 123 ? 0.6881  1.1982  0.9175  0.1819  0.0432  -0.0908 132 ALA B O   
7451  C CB  . ALA B 123 ? 0.6994  1.1134  0.9086  0.1294  0.0653  -0.1056 132 ALA B CB  
7457  N N   . ASN B 124 ? 1.0115  1.4341  1.2609  0.1953  0.0466  -0.0305 133 ASN B N   
7458  C CA  . ASN B 124 ? 1.0452  1.4804  1.3099  0.2106  0.0366  -0.0296 133 ASN B CA  
7459  C C   . ASN B 124 ? 0.7903  1.2400  1.0559  0.2491  0.0320  0.0046  133 ASN B C   
7460  O O   . ASN B 124 ? 0.6656  1.0770  0.9481  0.2597  0.0289  0.0266  133 ASN B O   
7461  C CB  . ASN B 124 ? 1.1286  1.5048  1.4121  0.1935  0.0363  -0.0260 133 ASN B CB  
7462  C CG  . ASN B 124 ? 0.8653  1.2480  1.1640  0.2079  0.0272  -0.0302 133 ASN B CG  
7463  O OD1 . ASN B 124 ? 0.9271  1.3648  1.2231  0.2237  0.0214  -0.0465 133 ASN B OD1 
7464  N ND2 . ASN B 124 ? 1.1770  1.5072  1.4922  0.2051  0.0254  -0.0168 133 ASN B ND2 
7471  N N   . TRP B 125 ? 0.7883  1.2913  1.0347  0.2708  0.0312  0.0089  134 TRP B N   
7472  C CA  . TRP B 125 ? 0.8203  1.3295  1.0622  0.3082  0.0294  0.0495  134 TRP B CA  
7473  C C   . TRP B 125 ? 0.8213  1.4112  1.0407  0.3353  0.0225  0.0403  134 TRP B C   
7474  O O   . TRP B 125 ? 1.1625  1.8023  1.3690  0.3216  0.0212  0.0035  134 TRP B O   
7475  C CB  . TRP B 125 ? 0.8693  1.3354  1.1090  0.3066  0.0419  0.0886  134 TRP B CB  
7476  C CG  . TRP B 125 ? 0.9826  1.4753  1.2008  0.2985  0.0509  0.0803  134 TRP B CG  
7477  C CD1 . TRP B 125 ? 0.9765  1.4496  1.1939  0.2681  0.0578  0.0565  134 TRP B CD1 
7478  C CD2 . TRP B 125 ? 1.4099  1.9518  1.6009  0.3238  0.0545  0.0955  134 TRP B CD2 
7479  N NE1 . TRP B 125 ? 0.7085  1.2129  0.9018  0.2729  0.0657  0.0532  134 TRP B NE1 
7480  C CE2 . TRP B 125 ? 1.2554  1.8054  1.4318  0.3060  0.0639  0.0758  134 TRP B CE2 
7481  C CE3 . TRP B 125 ? 1.6795  2.2591  1.8543  0.3618  0.0510  0.1245  134 TRP B CE3 
7482  C CZ2 . TRP B 125 ? 1.2117  1.8091  1.3587  0.3237  0.0698  0.0803  134 TRP B CZ2 
7483  C CZ3 . TRP B 125 ? 1.6406  2.2701  1.7842  0.3792  0.0566  0.1321  134 TRP B CZ3 
7484  C CH2 . TRP B 125 ? 1.4934  2.1328  1.6238  0.3594  0.0659  0.1083  134 TRP B CH2 
7495  N N   . LYS B 126 ? 0.7058  1.3056  0.9200  0.3744  0.0180  0.0750  135 LYS B N   
7496  C CA  . LYS B 126 ? 0.7466  1.4237  0.9387  0.4103  0.0088  0.0755  135 LYS B CA  
7497  C C   . LYS B 126 ? 0.8606  1.5212  1.0358  0.4445  0.0146  0.1321  135 LYS B C   
7498  O O   . LYS B 126 ? 1.0277  1.6207  1.2174  0.4507  0.0195  0.1691  135 LYS B O   
7499  C CB  . LYS B 126 ? 0.8205  1.5342  1.0265  0.4309  -0.0066 0.0560  135 LYS B CB  
7502  N N   . LYS B 127 ? 0.7786  1.5024  0.9221  0.4677  0.0137  0.1390  136 LYS B N   
7503  C CA  . LYS B 127 ? 0.9465  1.6646  1.0692  0.5057  0.0186  0.1951  136 LYS B CA  
7504  C C   . LYS B 127 ? 1.1434  1.8988  1.2624  0.5486  0.0022  0.2009  136 LYS B C   
7505  O O   . LYS B 127 ? 1.3358  2.1729  1.4471  0.5583  -0.0121 0.1627  136 LYS B O   
7506  C CB  . LYS B 127 ? 1.0683  1.8403  1.1544  0.5141  0.0258  0.2014  136 LYS B CB  
7509  N N   . LYS B 128 ? 1.3387  2.0346  1.4656  0.5731  0.0039  0.2450  137 LYS B N   
7510  C CA  . LYS B 128 ? 1.3885  2.1046  1.5058  0.6085  -0.0104 0.2464  137 LYS B CA  
7511  C C   . LYS B 128 ? 1.4236  2.2152  1.4948  0.6385  -0.0156 0.2540  137 LYS B C   
7512  O O   . LYS B 128 ? 1.0769  1.9411  1.1383  0.6496  -0.0308 0.2180  137 LYS B O   
7513  C CB  . LYS B 128 ? 1.3910  2.0114  1.5164  0.6218  -0.0050 0.2899  137 LYS B CB  
7514  C CG  . LYS B 128 ? 1.2401  1.7939  1.4090  0.5998  -0.0056 0.2731  137 LYS B CG  
7515  C CD  . LYS B 128 ? 1.0561  1.5112  1.2296  0.6123  0.0007  0.3175  137 LYS B CD  
7516  C CE  . LYS B 128 ? 2.0243  2.4154  2.2368  0.5970  -0.0024 0.2979  137 LYS B CE  
7517  N NZ  . LYS B 128 ? 2.4786  2.7717  2.6934  0.6066  0.0042  0.3394  137 LYS B NZ  
7531  N N   . ASP B 129 ? 1.4014  2.1809  1.4437  0.6512  -0.0021 0.3002  138 ASP B N   
7532  C CA  . ASP B 129 ? 1.3898  2.2462  1.3847  0.6787  -0.0046 0.3073  138 ASP B CA  
7533  C C   . ASP B 129 ? 1.8185  2.7223  1.8035  0.6619  0.0032  0.2949  138 ASP B C   
7534  O O   . ASP B 129 ? 1.7424  2.6009  1.7278  0.6536  0.0215  0.3329  138 ASP B O   
7535  C CB  . ASP B 129 ? 1.7833  2.5955  1.7479  0.7096  0.0070  0.3704  138 ASP B CB  
7536  C CG  . ASP B 129 ? 1.4780  2.3733  1.3916  0.7431  0.0039  0.3770  138 ASP B CG  
7537  O OD1 . ASP B 129 ? 1.7239  2.7103  1.6242  0.7396  -0.0059 0.3341  138 ASP B OD1 
7538  O OD2 . ASP B 129 ? 1.8820  2.7514  1.7689  0.7721  0.0120  0.4242  138 ASP B OD2 
7539  N N   . PRO B 130 ? 1.6174  2.6103  1.5968  0.6540  -0.0093 0.2402  139 PRO B N   
7540  C CA  . PRO B 130 ? 1.6282  2.6612  1.5945  0.6367  -0.0011 0.2227  139 PRO B CA  
7541  C C   . PRO B 130 ? 1.8483  2.8913  1.7727  0.6643  0.0128  0.2749  139 PRO B C   
7542  O O   . PRO B 130 ? 2.0114  3.0320  1.9285  0.6409  0.0314  0.2804  139 PRO B O   
7543  C CB  . PRO B 130 ? 1.8239  2.9604  1.7813  0.6340  -0.0200 0.1585  139 PRO B CB  
7544  C CG  . PRO B 130 ? 1.5329  2.6648  1.5209  0.6293  -0.0348 0.1321  139 PRO B CG  
7545  C CD  . PRO B 130 ? 1.2549  2.3072  1.2428  0.6526  -0.0296 0.1870  139 PRO B CD  
7546  N N   . ASN B 131 ? 1.6443  2.7025  1.5337  0.7000  0.0105  0.3063  140 ASN B N   
7547  C CA  . ASN B 131 ? 1.3798  2.4486  1.2244  0.7252  0.0266  0.3558  140 ASN B CA  
7548  C C   . ASN B 131 ? 1.4140  2.3856  1.2725  0.7161  0.0505  0.4172  140 ASN B C   
7549  O O   . ASN B 131 ? 1.4386  2.4166  1.2694  0.7240  0.0695  0.4551  140 ASN B O   
7550  C CB  . ASN B 131 ? 1.3265  2.4320  1.1365  0.7635  0.0189  0.3684  140 ASN B CB  
7551  C CG  . ASN B 131 ? 1.2421  2.3424  1.0117  0.7903  0.0386  0.4270  140 ASN B CG  
7552  O OD1 . ASN B 131 ? 1.6058  2.6782  1.3619  0.8170  0.0413  0.4635  140 ASN B OD1 
7553  N ND2 . ASN B 131 ? 1.3758  2.5024  1.1265  0.7835  0.0537  0.4364  140 ASN B ND2 
7554  N N   . LYS B 132 ? 1.5554  2.4403  1.4569  0.6982  0.0507  0.4259  141 LYS B N   
7555  C CA  . LYS B 132 ? 1.6280  2.4130  1.5529  0.6830  0.0706  0.4766  141 LYS B CA  
7556  C C   . LYS B 132 ? 1.6776  2.4365  1.6375  0.6464  0.0808  0.4665  141 LYS B C   
7557  O O   . LYS B 132 ? 1.6442  2.4350  1.6153  0.6187  0.0737  0.4076  141 LYS B O   
7558  C CB  . LYS B 132 ? 1.8096  2.5185  1.7624  0.6829  0.0627  0.4821  141 LYS B CB  
7559  N N   . PRO B 133 ? 1.4232  2.1092  1.3989  0.6295  0.1024  0.5129  142 PRO B N   
7560  C CA  . PRO B 133 ? 1.1240  1.7770  1.1293  0.5820  0.1178  0.4969  142 PRO B CA  
7561  C C   . PRO B 133 ? 1.1815  1.7725  1.2369  0.5454  0.1094  0.4618  142 PRO B C   
7562  O O   . PRO B 133 ? 1.1211  1.6875  1.1918  0.5543  0.0937  0.4509  142 PRO B O   
7563  C CB  . PRO B 133 ? 1.1038  1.7106  1.1083  0.5812  0.1434  0.5648  142 PRO B CB  
7564  C CG  . PRO B 133 ? 1.7016  2.2678  1.6968  0.6105  0.1397  0.6065  142 PRO B CG  
7565  C CD  . PRO B 133 ? 1.4530  2.0843  1.4150  0.6433  0.1180  0.5744  142 PRO B CD  
7566  N N   . LEU B 134 ? 1.2512  1.8196  1.3311  0.5058  0.1209  0.4450  143 LEU B N   
7567  C CA  . LEU B 134 ? 1.0888  1.6034  1.2126  0.4685  0.1146  0.4114  143 LEU B CA  
7568  C C   . LEU B 134 ? 1.2676  1.6981  1.4265  0.4520  0.1245  0.4512  143 LEU B C   
7569  O O   . LEU B 134 ? 1.3104  1.7114  1.4944  0.4215  0.1380  0.4589  143 LEU B O   
7570  C CB  . LEU B 134 ? 1.4653  1.9992  1.5950  0.4381  0.1201  0.3723  143 LEU B CB  
7571  C CG  . LEU B 134 ? 1.1323  1.7370  1.2333  0.4441  0.1099  0.3216  143 LEU B CG  
7572  C CD1 . LEU B 134 ? 1.3237  1.9402  1.4223  0.4224  0.1226  0.3005  143 LEU B CD1 
7573  C CD2 . LEU B 134 ? 0.7879  1.3929  0.9029  0.4330  0.0902  0.2725  143 LEU B CD2 
7574  N N   . THR B 135 ? 1.4146  1.8074  1.5759  0.4734  0.1175  0.4757  144 THR B N   
7575  C CA  . THR B 135 ? 1.3420  1.6474  1.5393  0.4555  0.1227  0.5019  144 THR B CA  
7576  C C   . THR B 135 ? 1.7216  1.9919  1.9431  0.4497  0.1035  0.4638  144 THR B C   
7577  O O   . THR B 135 ? 0.8979  1.2113  1.1061  0.4677  0.0867  0.4278  144 THR B O   
7578  C CB  . THR B 135 ? 1.1915  1.4625  1.3730  0.4836  0.1338  0.5659  144 THR B CB  
7579  O OG1 . THR B 135 ? 1.4936  1.7923  1.6445  0.5296  0.1186  0.5664  144 THR B OG1 
7580  C CG2 . THR B 135 ? 1.1292  1.4288  1.2893  0.4857  0.1565  0.6093  144 THR B CG2 
7588  N N   . TYR B 136 ? 1.3091  1.5029  1.5671  0.4244  0.1065  0.4722  145 TYR B N   
7589  C CA  . TYR B 136 ? 1.3673  1.5242  1.6468  0.4207  0.0896  0.4379  145 TYR B CA  
7590  C C   . TYR B 136 ? 1.5349  1.7029  1.7922  0.4675  0.0775  0.4432  145 TYR B C   
7591  O O   . TYR B 136 ? 1.3709  1.5728  1.6270  0.4775  0.0610  0.4004  145 TYR B O   
7592  C CB  . TYR B 136 ? 1.5062  1.5759  1.8237  0.3921  0.0953  0.4530  145 TYR B CB  
7593  C CG  . TYR B 136 ? 1.4304  1.4586  1.7712  0.3840  0.0796  0.4150  145 TYR B CG  
7594  C CD1 . TYR B 136 ? 1.8774  1.9176  2.2362  0.3526  0.0715  0.3676  145 TYR B CD1 
7595  C CD2 . TYR B 136 ? 1.4423  1.4161  1.7857  0.4086  0.0740  0.4278  145 TYR B CD2 
7596  C CE1 . TYR B 136 ? 1.4989  1.5054  1.8760  0.3453  0.0585  0.3334  145 TYR B CE1 
7597  C CE2 . TYR B 136 ? 1.2595  1.1981  1.6231  0.4026  0.0606  0.3905  145 TYR B CE2 
7598  C CZ  . TYR B 136 ? 0.9997  0.9579  1.3797  0.3701  0.0531  0.3432  145 TYR B CZ  
7599  O OH  . TYR B 136 ? 1.0630  0.9909  1.4598  0.3642  0.0411  0.3063  145 TYR B OH  
7609  N N   . GLU B 137 ? 1.4284  1.5764  1.6655  0.4988  0.0862  0.4970  146 GLU B N   
7610  C CA  . GLU B 137 ? 1.4391  1.5897  1.6493  0.5378  0.0744  0.4987  146 GLU B CA  
7611  C C   . GLU B 137 ? 1.3881  1.6394  1.5679  0.5658  0.0609  0.4698  146 GLU B C   
7612  O O   . GLU B 137 ? 1.2571  1.5258  1.4266  0.5918  0.0451  0.4489  146 GLU B O   
7613  C CB  . GLU B 137 ? 1.5247  1.6308  1.7101  0.5503  0.0889  0.5543  146 GLU B CB  
7614  C CG  . GLU B 137 ? 1.6352  1.6326  1.8474  0.5295  0.0963  0.5748  146 GLU B CG  
7615  C CD  . GLU B 137 ? 1.9046  1.8693  2.1584  0.4821  0.1084  0.5755  146 GLU B CD  
7616  O OE1 . GLU B 137 ? 1.6984  1.7139  1.9510  0.4693  0.1196  0.5851  146 GLU B OE1 
7617  O OE2 . GLU B 137 ? 2.2196  2.1119  2.5073  0.4584  0.1058  0.5639  146 GLU B OE2 
7624  N N   . ASN B 138 ? 1.3465  1.6670  1.5147  0.5596  0.0659  0.4633  147 ASN B N   
7625  C CA  . ASN B 138 ? 1.1453  1.5644  1.2859  0.5808  0.0527  0.4300  147 ASN B CA  
7626  C C   . ASN B 138 ? 0.9681  1.4224  1.1310  0.5535  0.0410  0.3658  147 ASN B C   
7627  O O   . ASN B 138 ? 0.9481  1.4844  1.0942  0.5645  0.0293  0.3306  147 ASN B O   
7628  C CB  . ASN B 138 ? 1.1234  1.6010  1.2301  0.5882  0.0646  0.4522  147 ASN B CB  
7629  C CG  . ASN B 138 ? 1.2349  1.8153  1.3064  0.6131  0.0502  0.4202  147 ASN B CG  
7630  O OD1 . ASN B 138 ? 1.9782  2.5798  2.0339  0.6382  0.0365  0.4098  147 ASN B OD1 
7631  N ND2 . ASN B 138 ? 1.2964  1.9369  1.3553  0.5998  0.0541  0.3982  147 ASN B ND2 
7638  N N   . MET B 139 ? 0.8758  1.2693  1.0740  0.5168  0.0428  0.3469  148 MET B N   
7639  C CA  . MET B 139 ? 0.9053  1.3240  1.1191  0.4825  0.0363  0.2897  148 MET B CA  
7640  C C   . MET B 139 ? 0.9067  1.2940  1.1478  0.4762  0.0248  0.2593  148 MET B C   
7641  O O   . MET B 139 ? 1.1078  1.4314  1.3642  0.4872  0.0243  0.2808  148 MET B O   
7642  C CB  . MET B 139 ? 1.0182  1.4049  1.2453  0.4393  0.0503  0.2892  148 MET B CB  
7643  C CG  . MET B 139 ? 1.4037  1.8378  1.6035  0.4418  0.0614  0.3028  148 MET B CG  
7644  S SD  . MET B 139 ? 1.1548  1.5507  1.3722  0.4007  0.0800  0.3126  148 MET B SD  
7645  C CE  . MET B 139 ? 0.8331  1.2510  1.0576  0.3689  0.0712  0.2467  148 MET B CE  
7655  N N   . ASP B 140 ? 0.7875  1.2190  1.0342  0.4566  0.0168  0.2074  149 ASP B N   
7656  C CA  . ASP B 140 ? 0.7957  1.1991  1.0682  0.4416  0.0095  0.1754  149 ASP B CA  
7657  C C   . ASP B 140 ? 1.0224  1.4464  1.3004  0.3988  0.0112  0.1320  149 ASP B C   
7658  O O   . ASP B 140 ? 1.4076  1.8803  1.6682  0.3893  0.0143  0.1190  149 ASP B O   
7659  C CB  . ASP B 140 ? 1.3122  1.7569  1.5849  0.4783  -0.0048 0.1588  149 ASP B CB  
7660  C CG  . ASP B 140 ? 0.8463  1.2205  1.1362  0.4975  -0.0073 0.1769  149 ASP B CG  
7665  N N   . VAL B 141 ? 1.2100  1.5941  1.5101  0.3740  0.0096  0.1093  150 VAL B N   
7666  C CA  . VAL B 141 ? 1.0405  1.4424  1.3433  0.3362  0.0110  0.0681  150 VAL B CA  
7667  C C   . VAL B 141 ? 1.1352  1.6044  1.4371  0.3444  0.0014  0.0283  150 VAL B C   
7668  O O   . VAL B 141 ? 1.3070  1.8007  1.6114  0.3802  -0.0073 0.0324  150 VAL B O   
7669  C CB  . VAL B 141 ? 1.0517  1.3859  1.3746  0.3045  0.0141  0.0627  150 VAL B CB  
7670  C CG1 . VAL B 141 ? 1.2446  1.5251  1.5727  0.2961  0.0230  0.1009  150 VAL B CG1 
7671  C CG2 . VAL B 141 ? 0.7260  1.0325  1.0660  0.3160  0.0066  0.0550  150 VAL B CG2 
7681  N N   . LEU B 142 ? 0.7173  1.2173  1.0164  0.3120  0.0037  -0.0098 151 LEU B N   
7682  C CA  . LEU B 142 ? 0.6124  1.1828  0.9143  0.3116  -0.0031 -0.0507 151 LEU B CA  
7683  C C   . LEU B 142 ? 0.9242  1.4759  1.2458  0.2985  -0.0046 -0.0739 151 LEU B C   
7684  O O   . LEU B 142 ? 1.3711  1.9788  1.7016  0.3133  -0.0115 -0.0983 151 LEU B O   
7685  C CB  . LEU B 142 ? 0.5300  1.1436  0.8184  0.2802  0.0019  -0.0817 151 LEU B CB  
7686  C CG  . LEU B 142 ? 1.0575  1.6965  1.3228  0.2891  0.0045  -0.0681 151 LEU B CG  
7687  C CD1 . LEU B 142 ? 1.0412  1.7057  1.2934  0.2529  0.0109  -0.1037 151 LEU B CD1 
7688  C CD2 . LEU B 142 ? 0.5670  1.2716  0.8232  0.3323  -0.0061 -0.0578 151 LEU B CD2 
7700  N N   . PHE B 143 ? 1.0839  1.5632  1.4125  0.2742  0.0012  -0.0669 152 PHE B N   
7701  C CA  . PHE B 143 ? 1.0465  1.5095  1.3883  0.2570  0.0012  -0.0920 152 PHE B CA  
7702  C C   . PHE B 143 ? 1.3169  1.6985  1.6698  0.2564  0.0009  -0.0715 152 PHE B C   
7703  O O   . PHE B 143 ? 1.4419  1.7734  1.7942  0.2554  0.0036  -0.0397 152 PHE B O   
7704  C CB  . PHE B 143 ? 0.8954  1.3696  1.2293  0.2127  0.0096  -0.1213 152 PHE B CB  
7705  C CG  . PHE B 143 ? 0.9408  1.4940  1.2672  0.2053  0.0104  -0.1495 152 PHE B CG  
7706  C CD1 . PHE B 143 ? 1.0539  1.6758  1.3916  0.2121  0.0062  -0.1800 152 PHE B CD1 
7707  C CD2 . PHE B 143 ? 1.0487  1.6103  1.3582  0.1910  0.0155  -0.1481 152 PHE B CD2 
7708  C CE1 . PHE B 143 ? 1.1823  1.8816  1.5170  0.2010  0.0065  -0.2087 152 PHE B CE1 
7709  C CE2 . PHE B 143 ? 1.2210  1.8531  1.5243  0.1806  0.0157  -0.1781 152 PHE B CE2 
7710  C CZ  . PHE B 143 ? 1.2144  1.9170  1.5316  0.1838  0.0108  -0.2087 152 PHE B CZ  
7720  N N   . SER B 144 ? 0.9721  1.3464  1.3364  0.2563  -0.0021 -0.0929 153 SER B N   
7721  C CA  . SER B 144 ? 1.0047  1.3093  1.3802  0.2545  -0.0042 -0.0846 153 SER B CA  
7722  C C   . SER B 144 ? 0.9234  1.2366  1.3009  0.2334  -0.0028 -0.1207 153 SER B C   
7723  O O   . SER B 144 ? 0.9208  1.2957  1.2948  0.2262  0.0001  -0.1493 153 SER B O   
7724  C CB  . SER B 144 ? 1.0596  1.3398  1.4463  0.2969  -0.0114 -0.0667 153 SER B CB  
7725  O OG  . SER B 144 ? 1.0374  1.3045  1.4196  0.3178  -0.0111 -0.0278 153 SER B OG  
7731  N N   . PHE B 145 ? 1.0750  1.3301  1.4586  0.2237  -0.0047 -0.1203 154 PHE B N   
7732  C CA  . PHE B 145 ? 0.9936  1.2538  1.3756  0.2065  -0.0034 -0.1525 154 PHE B CA  
7733  C C   . PHE B 145 ? 0.8577  1.1166  1.2518  0.2361  -0.0093 -0.1695 154 PHE B C   
7734  O O   . PHE B 145 ? 0.8113  1.1184  1.2050  0.2375  -0.0068 -0.2011 154 PHE B O   
7735  C CB  . PHE B 145 ? 0.9920  1.1946  1.3697  0.1766  -0.0030 -0.1465 154 PHE B CB  
7736  C CG  . PHE B 145 ? 1.1672  1.3706  1.5311  0.1478  0.0037  -0.1367 154 PHE B CG  
7737  C CD1 . PHE B 145 ? 0.7468  0.9840  1.0948  0.1235  0.0116  -0.1585 154 PHE B CD1 
7738  C CD2 . PHE B 145 ? 0.9064  1.0770  1.2729  0.1451  0.0035  -0.1057 154 PHE B CD2 
7739  C CE1 . PHE B 145 ? 0.5671  0.7980  0.9000  0.0985  0.0186  -0.1501 154 PHE B CE1 
7740  C CE2 . PHE B 145 ? 0.6201  0.7918  0.9730  0.1224  0.0101  -0.0991 154 PHE B CE2 
7741  C CZ  . PHE B 145 ? 0.7900  0.9884  1.1251  0.0998  0.0174  -0.1217 154 PHE B CZ  
7751  N N   . ARG B 146 ? 0.7026  0.9026  1.1076  0.2572  -0.0158 -0.1497 155 ARG B N   
7752  C CA  . ARG B 146 ? 1.1862  1.3677  1.6019  0.2882  -0.0216 -0.1641 155 ARG B CA  
7753  C C   . ARG B 146 ? 0.9058  1.0509  1.3300  0.3241  -0.0261 -0.1313 155 ARG B C   
7754  O O   . ARG B 146 ? 0.8918  1.0163  1.3141  0.3184  -0.0242 -0.0969 155 ARG B O   
7755  C CB  . ARG B 146 ? 0.9946  1.1206  1.4122  0.2693  -0.0243 -0.1801 155 ARG B CB  
7756  C CG  . ARG B 146 ? 1.1044  1.2607  1.5079  0.2341  -0.0193 -0.2082 155 ARG B CG  
7757  C CD  . ARG B 146 ? 1.2034  1.4267  1.6040  0.2463  -0.0149 -0.2435 155 ARG B CD  
7758  N NE  . ARG B 146 ? 0.9797  1.1858  1.3876  0.2721  -0.0196 -0.2688 155 ARG B NE  
7759  C CZ  . ARG B 146 ? 1.1935  1.3728  1.5945  0.2575  -0.0208 -0.2915 155 ARG B CZ  
7760  N NH1 . ARG B 146 ? 1.2297  1.3962  1.6159  0.2179  -0.0187 -0.2895 155 ARG B NH1 
7761  N NH2 . ARG B 146 ? 1.5013  1.6656  1.9087  0.2853  -0.0249 -0.3168 155 ARG B NH2 
7775  N N   . ASP B 147 ? 1.3369  1.4776  1.7687  0.3636  -0.0308 -0.1413 156 ASP B N   
7776  C CA  . ASP B 147 ? 1.2313  1.3293  1.6678  0.4010  -0.0342 -0.1076 156 ASP B CA  
7777  C C   . ASP B 147 ? 1.0183  1.0195  1.4625  0.3831  -0.0343 -0.0856 156 ASP B C   
7778  O O   . ASP B 147 ? 0.8602  0.8199  1.3108  0.3673  -0.0368 -0.1091 156 ASP B O   
7779  C CB  . ASP B 147 ? 1.3768  1.4892  1.8190  0.4510  -0.0393 -0.1253 156 ASP B CB  
7780  C CG  . ASP B 147 ? 1.3557  1.5777  1.7951  0.4684  -0.0396 -0.1463 156 ASP B CG  
7781  O OD1 . ASP B 147 ? 0.9869  1.2570  1.4185  0.4623  -0.0382 -0.1285 156 ASP B OD1 
7782  O OD2 . ASP B 147 ? 1.5103  1.7747  1.9561  0.4857  -0.0408 -0.1827 156 ASP B OD2 
7787  N N   . GLY B 148 ? 0.9744  0.9446  1.4182  0.3834  -0.0313 -0.0421 157 GLY B N   
7788  C CA  . GLY B 148 ? 1.0677  0.9516  1.5232  0.3624  -0.0299 -0.0198 157 GLY B CA  
7789  C C   . GLY B 148 ? 0.8863  0.7652  1.3456  0.3112  -0.0285 -0.0288 157 GLY B C   
7790  O O   . GLY B 148 ? 0.9387  0.7597  1.4109  0.2902  -0.0314 -0.0350 157 GLY B O   
7794  N N   . ASP B 149 ? 1.1172  1.0564  1.5652  0.2919  -0.0251 -0.0335 158 ASP B N   
7795  C CA  . ASP B 149 ? 1.2189  1.1464  1.6696  0.2497  -0.0230 -0.0288 158 ASP B CA  
7796  C C   . ASP B 149 ? 1.2233  1.1308  1.6796  0.2429  -0.0166 0.0158  158 ASP B C   
7797  O O   . ASP B 149 ? 0.8886  0.7946  1.3486  0.2123  -0.0140 0.0236  158 ASP B O   
7798  C CB  . ASP B 149 ? 1.1091  1.1004  1.5434  0.2309  -0.0207 -0.0534 158 ASP B CB  
7799  C CG  . ASP B 149 ? 1.0328  1.0867  1.4542  0.2496  -0.0163 -0.0477 158 ASP B CG  
7800  O OD1 . ASP B 149 ? 1.3678  1.4218  1.7910  0.2833  -0.0170 -0.0281 158 ASP B OD1 
7801  O OD2 . ASP B 149 ? 0.7941  0.8973  1.2026  0.2326  -0.0126 -0.0643 158 ASP B OD2 
7806  N N   . CYS B 150 ? 1.8813  1.7793  2.3366  0.2725  -0.0131 0.0466  159 CYS B N   
7807  C CA  . CYS B 150 ? 1.8429  1.7256  2.3019  0.2648  -0.0047 0.0897  159 CYS B CA  
7808  C C   . CYS B 150 ? 1.7220  1.6638  2.1673  0.2490  0.0009  0.0927  159 CYS B C   
7809  O O   . CYS B 150 ? 1.8124  1.7490  2.2617  0.2355  0.0086  0.1218  159 CYS B O   
7810  C CB  . CYS B 150 ? 1.6507  1.4702  2.1338  0.2343  -0.0040 0.1004  159 CYS B CB  
7811  S SG  . CYS B 150 ? 1.2029  0.9360  1.7036  0.2489  -0.0071 0.1064  159 CYS B SG  
7817  N N   . SER B 151 ? 1.2937  1.6933  1.6225  0.2279  0.1479  0.0754  160 SER B N   
7818  C CA  . SER B 151 ? 1.2161  1.6564  1.5323  0.2015  0.1129  0.0630  160 SER B CA  
7819  C C   . SER B 151 ? 0.4586  0.9404  0.7618  0.2331  0.0974  0.0868  160 SER B C   
7820  O O   . SER B 151 ? 0.7092  1.1987  0.9933  0.2131  0.0761  0.0802  160 SER B O   
7821  C CB  . SER B 151 ? 1.5529  2.0544  1.8866  0.1758  0.0927  0.0374  160 SER B CB  
7822  O OG  . SER B 151 ? 0.3998  0.9676  0.7560  0.2097  0.0920  0.0483  160 SER B OG  
7828  N N   . LYS B 152 ? 0.7539  1.2670  1.0656  0.2823  0.1067  0.1143  161 LYS B N   
7829  C CA  . LYS B 152 ? 0.7045  1.2473  0.9966  0.3089  0.0932  0.1377  161 LYS B CA  
7830  C C   . LYS B 152 ? 0.8635  1.3265  1.1274  0.2983  0.1051  0.1450  161 LYS B C   
7831  O O   . LYS B 152 ? 0.8986  1.3691  1.1418  0.2807  0.0854  0.1399  161 LYS B O   
7832  C CB  . LYS B 152 ? 0.5223  1.1024  0.8240  0.3690  0.1051  0.1725  161 LYS B CB  
7835  N N   . GLY B 153 ? 1.4759  1.8597  1.7400  0.3012  0.1386  0.1511  162 GLY B N   
7836  C CA  . GLY B 153 ? 1.2428  1.5538  1.4828  0.2917  0.1534  0.1586  162 GLY B CA  
7837  C C   . GLY B 153 ? 1.0075  1.3033  1.2375  0.2408  0.1349  0.1305  162 GLY B C   
7838  O O   . GLY B 153 ? 0.5850  0.8680  0.7936  0.2340  0.1267  0.1354  162 GLY B O   
7842  N N   . PHE B 154 ? 0.7098  1.0038  0.9543  0.2058  0.1306  0.1022  163 PHE B N   
7843  C CA  . PHE B 154 ? 0.7731  1.0491  1.0076  0.1600  0.1154  0.0783  163 PHE B CA  
7844  C C   . PHE B 154 ? 0.6679  0.9988  0.8925  0.1499  0.0817  0.0709  163 PHE B C   
7845  O O   . PHE B 154 ? 0.9723  1.2844  1.1806  0.1274  0.0716  0.0636  163 PHE B O   
7846  C CB  . PHE B 154 ? 0.6558  0.9199  0.9051  0.1260  0.1183  0.0516  163 PHE B CB  
7847  C CG  . PHE B 154 ? 0.8500  1.0914  1.0883  0.0831  0.1061  0.0313  163 PHE B CG  
7848  C CD1 . PHE B 154 ? 1.5066  1.6942  1.7322  0.0716  0.1191  0.0341  163 PHE B CD1 
7849  C CD2 . PHE B 154 ? 0.5990  0.8741  0.8399  0.0549  0.0829  0.0102  163 PHE B CD2 
7850  C CE1 . PHE B 154 ? 0.8664  1.0404  1.0842  0.0359  0.1074  0.0176  163 PHE B CE1 
7851  C CE2 . PHE B 154 ? 0.7330  0.9872  0.9633  0.0199  0.0729  -0.0052 163 PHE B CE2 
7852  C CZ  . PHE B 154 ? 0.8326  1.0392  1.0521  0.0116  0.0840  -0.0009 163 PHE B CZ  
7862  N N   . PHE B 155 ? 0.5541  0.9538  0.7891  0.1635  0.0651  0.0703  164 PHE B N   
7863  C CA  . PHE B 155 ? 0.5354  0.9852  0.7590  0.1502  0.0356  0.0599  164 PHE B CA  
7864  C C   . PHE B 155 ? 0.7507  1.2095  0.9528  0.1777  0.0322  0.0829  164 PHE B C   
7865  O O   . PHE B 155 ? 0.9706  1.4171  1.1521  0.1613  0.0214  0.0776  164 PHE B O   
7866  C CB  . PHE B 155 ? 0.6065  1.1340  0.8487  0.1507  0.0189  0.0482  164 PHE B CB  
7867  C CG  . PHE B 155 ? 0.6907  1.2144  0.9499  0.1166  0.0187  0.0218  164 PHE B CG  
7868  C CD1 . PHE B 155 ? 0.7177  1.1851  0.9682  0.0801  0.0217  0.0054  164 PHE B CD1 
7869  C CD2 . PHE B 155 ? 0.5230  1.1040  0.8071  0.1212  0.0155  0.0139  164 PHE B CD2 
7870  C CE1 . PHE B 155 ? 0.6075  1.0722  0.8702  0.0496  0.0219  -0.0169 164 PHE B CE1 
7871  C CE2 . PHE B 155 ? 0.3082  0.8840  0.6057  0.0883  0.0169  -0.0105 164 PHE B CE2 
7872  C CZ  . PHE B 155 ? 0.8573  1.3735  1.1426  0.0534  0.0204  -0.0248 164 PHE B CZ  
7882  N N   . LEU B 156 ? 0.8499  1.3227  1.0549  0.2212  0.0448  0.1106  165 LEU B N   
7883  C CA  . LEU B 156 ? 0.7276  1.2222  0.9102  0.2493  0.0387  0.1336  165 LEU B CA  
7884  C C   . LEU B 156 ? 0.7814  1.2068  0.9413  0.2419  0.0520  0.1416  165 LEU B C   
7885  O O   . LEU B 156 ? 0.7626  1.2007  0.8994  0.2425  0.0399  0.1458  165 LEU B O   
7886  C CB  . LEU B 156 ? 0.8232  1.3445  1.0119  0.3020  0.0518  0.1665  165 LEU B CB  
7887  C CG  . LEU B 156 ? 0.8992  1.5124  1.1086  0.3219  0.0356  0.1669  165 LEU B CG  
7888  C CD1 . LEU B 156 ? 1.3121  1.9357  1.5246  0.3782  0.0539  0.2048  165 LEU B CD1 
7889  C CD2 . LEU B 156 ? 0.7306  1.4242  0.9285  0.3112  0.0022  0.1550  165 LEU B CD2 
7901  N N   . VAL B 157 ? 0.9343  1.2883  1.1002  0.2338  0.0780  0.1424  166 VAL B N   
7902  C CA  . VAL B 157 ? 0.6654  0.9587  0.8121  0.2251  0.0918  0.1491  166 VAL B CA  
7903  C C   . VAL B 157 ? 0.5265  0.8226  0.6641  0.1864  0.0706  0.1247  166 VAL B C   
7904  O O   . VAL B 157 ? 0.7543  1.0536  0.8704  0.1890  0.0633  0.1311  166 VAL B O   
7905  C CB  . VAL B 157 ? 0.7466  0.9670  0.9024  0.2204  0.1252  0.1517  166 VAL B CB  
7906  C CG1 . VAL B 157 ? 1.0364  1.1985  1.1761  0.2010  0.1381  0.1518  166 VAL B CG1 
7907  C CG2 . VAL B 157 ? 1.1372  1.3454  1.2963  0.2649  0.1510  0.1810  166 VAL B CG2 
7917  N N   . SER B 158 ? 0.5462  0.8498  0.6984  0.1534  0.0589  0.0973  167 SER B N   
7918  C CA  . SER B 158 ? 0.4980  0.8094  0.6407  0.1207  0.0380  0.0757  167 SER B CA  
7919  C C   . SER B 158 ? 0.6425  1.0035  0.7670  0.1319  0.0180  0.0788  167 SER B C   
7920  O O   . SER B 158 ? 0.7760  1.1244  0.8811  0.1248  0.0133  0.0782  167 SER B O   
7921  C CB  . SER B 158 ? 0.4216  0.7519  0.5791  0.0911  0.0246  0.0496  167 SER B CB  
7922  O OG  . SER B 158 ? 0.3696  0.6651  0.5432  0.0768  0.0395  0.0420  167 SER B OG  
7928  N N   . LEU B 159 ? 0.5430  0.9652  0.6738  0.1487  0.0061  0.0808  168 LEU B N   
7929  C CA  . LEU B 159 ? 0.5943  1.0723  0.7071  0.1553  -0.0142 0.0798  168 LEU B CA  
7930  C C   . LEU B 159 ? 0.5251  0.9882  0.6134  0.1813  -0.0060 0.1048  168 LEU B C   
7931  O O   . LEU B 159 ? 0.5029  0.9859  0.5686  0.1765  -0.0187 0.1002  168 LEU B O   
7932  C CB  . LEU B 159 ? 0.6097  1.1642  0.7359  0.1722  -0.0269 0.0805  168 LEU B CB  
7933  C CG  . LEU B 159 ? 0.7333  1.3594  0.8418  0.1853  -0.0466 0.0831  168 LEU B CG  
7934  C CD1 . LEU B 159 ? 0.9218  1.5631  1.0188  0.1471  -0.0648 0.0521  168 LEU B CD1 
7935  C CD2 . LEU B 159 ? 0.9702  1.6700  1.0972  0.2098  -0.0537 0.0910  168 LEU B CD2 
7947  N N   . LEU B 160 ? 0.6960  1.1247  0.7864  0.2095  0.0169  0.1313  169 LEU B N   
7948  C CA  . LEU B 160 ? 0.9698  1.3836  1.0346  0.2337  0.0263  0.1562  169 LEU B CA  
7949  C C   . LEU B 160 ? 0.7086  1.0694  0.7605  0.2077  0.0321  0.1465  169 LEU B C   
7950  O O   . LEU B 160 ? 0.8788  1.2372  0.9059  0.2157  0.0324  0.1566  169 LEU B O   
7951  C CB  . LEU B 160 ? 1.1900  1.5733  1.2585  0.2699  0.0532  0.1878  169 LEU B CB  
7952  C CG  . LEU B 160 ? 0.9587  1.4029  1.0360  0.3056  0.0475  0.2044  169 LEU B CG  
7953  C CD1 . LEU B 160 ? 0.8559  1.2521  0.9421  0.3358  0.0796  0.2310  169 LEU B CD1 
7954  C CD2 . LEU B 160 ? 0.9424  1.4479  0.9952  0.3305  0.0311  0.2202  169 LEU B CD2 
7966  N N   . VAL B 161 ? 0.6615  0.9803  0.7305  0.1788  0.0388  0.1291  170 VAL B N   
7967  C CA  . VAL B 161 ? 0.7825  1.0606  0.8438  0.1539  0.0422  0.1186  170 VAL B CA  
7968  C C   . VAL B 161 ? 1.0401  1.3486  1.0886  0.1345  0.0189  0.0983  170 VAL B C   
7969  O O   . VAL B 161 ? 0.5295  0.8236  0.5599  0.1310  0.0200  0.0993  170 VAL B O   
7970  C CB  . VAL B 161 ? 0.9936  1.2297  1.0765  0.1278  0.0526  0.1045  170 VAL B CB  
7971  C CG1 . VAL B 161 ? 0.7297  0.9422  0.8073  0.0993  0.0482  0.0894  170 VAL B CG1 
7972  C CG2 . VAL B 161 ? 1.3189  1.5109  1.4090  0.1431  0.0819  0.1231  170 VAL B CG2 
7982  N N   . GLU B 162 ? 0.9973  1.3450  1.0547  0.1198  0.0001  0.0782  171 GLU B N   
7983  C CA  . GLU B 162 ? 0.8108  1.1820  0.8538  0.0996  -0.0185 0.0571  171 GLU B CA  
7984  C C   . GLU B 162 ? 0.7621  1.1675  0.7781  0.1191  -0.0248 0.0671  171 GLU B C   
7985  O O   . GLU B 162 ? 0.8317  1.2298  0.8277  0.1085  -0.0285 0.0582  171 GLU B O   
7986  C CB  . GLU B 162 ? 1.4027  1.8111  1.4592  0.0809  -0.0343 0.0348  171 GLU B CB  
7987  C CG  . GLU B 162 ? 1.1349  1.5395  1.1826  0.0479  -0.0463 0.0074  171 GLU B CG  
7988  C CD  . GLU B 162 ? 0.9705  1.3333  1.0345  0.0219  -0.0418 -0.0052 171 GLU B CD  
7989  O OE1 . GLU B 162 ? 0.9608  1.3056  1.0438  0.0261  -0.0316 0.0032  171 GLU B OE1 
7990  O OE2 . GLU B 162 ? 1.3420  1.6909  1.3986  -0.0024 -0.0477 -0.0236 171 GLU B OE2 
7997  N N   . ILE B 163 ? 0.5574  0.9993  0.5715  0.1497  -0.0244 0.0873  172 ILE B N   
7998  C CA  . ILE B 163 ? 0.4962  0.9768  0.4828  0.1719  -0.0303 0.1007  172 ILE B CA  
7999  C C   . ILE B 163 ? 1.1997  1.6344  1.1660  0.1824  -0.0135 0.1183  172 ILE B C   
8000  O O   . ILE B 163 ? 0.6330  1.0843  0.5721  0.1832  -0.0194 0.1164  172 ILE B O   
8001  C CB  . ILE B 163 ? 0.7822  1.3111  0.7747  0.2072  -0.0313 0.1236  172 ILE B CB  
8002  C CG1 . ILE B 163 ? 0.8481  1.4381  0.8599  0.1959  -0.0503 0.1037  172 ILE B CG1 
8003  C CG2 . ILE B 163 ? 0.9411  1.5097  0.9023  0.2356  -0.0354 0.1441  172 ILE B CG2 
8004  C CD1 . ILE B 163 ? 1.3118  1.9363  1.3425  0.2285  -0.0464 0.1251  172 ILE B CD1 
8016  N N   . ALA B 164 ? 0.7898  1.1687  0.7675  0.1906  0.0094  0.1358  173 ALA B N   
8017  C CA  . ALA B 164 ? 0.9559  1.2907  0.9159  0.1972  0.0278  0.1513  173 ALA B CA  
8018  C C   . ALA B 164 ? 0.8581  1.1690  0.8143  0.1667  0.0243  0.1286  173 ALA B C   
8019  O O   . ALA B 164 ? 0.7216  1.0154  0.6583  0.1699  0.0329  0.1354  173 ALA B O   
8020  C CB  . ALA B 164 ? 0.8602  1.1395  0.8339  0.2076  0.0555  0.1714  173 ALA B CB  
8026  N N   . ALA B 165 ? 0.8715  1.1815  0.8458  0.1390  0.0129  0.1030  174 ALA B N   
8027  C CA  . ALA B 165 ? 0.6774  0.9692  0.6484  0.1133  0.0084  0.0822  174 ALA B CA  
8028  C C   . ALA B 165 ? 0.8745  1.2024  0.8207  0.1082  -0.0074 0.0667  174 ALA B C   
8029  O O   . ALA B 165 ? 1.2113  1.5211  1.1452  0.0964  -0.0054 0.0562  174 ALA B O   
8030  C CB  . ALA B 165 ? 0.4853  0.7635  0.4815  0.0880  0.0029  0.0631  174 ALA B CB  
8036  N N   . ALA B 166 ? 0.7015  1.0822  0.6401  0.1161  -0.0219 0.0640  175 ALA B N   
8037  C CA  . ALA B 166 ? 0.8603  1.2777  0.7735  0.1070  -0.0358 0.0457  175 ALA B CA  
8038  C C   . ALA B 166 ? 0.8250  1.2341  0.7087  0.1200  -0.0270 0.0568  175 ALA B C   
8039  O O   . ALA B 166 ? 0.9112  1.3234  0.7743  0.1055  -0.0310 0.0376  175 ALA B O   
8040  C CB  . ALA B 166 ? 1.2356  1.7223  1.1458  0.1154  -0.0527 0.0433  175 ALA B CB  
8046  N N   . SER B 167 ? 0.7312  1.1263  0.6113  0.1468  -0.0124 0.0873  176 SER B N   
8047  C CA  . SER B 167 ? 1.0387  1.4258  0.8893  0.1611  -0.0015 0.1014  176 SER B CA  
8048  C C   . SER B 167 ? 1.1084  1.4517  0.9570  0.1418  0.0084  0.0873  176 SER B C   
8049  O O   . SER B 167 ? 1.2320  1.5748  1.0537  0.1469  0.0148  0.0894  176 SER B O   
8050  C CB  . SER B 167 ? 1.1525  1.5177  1.0035  0.1896  0.0176  0.1369  176 SER B CB  
8051  O OG  . SER B 167 ? 1.3816  1.7829  1.2379  0.2111  0.0110  0.1523  176 SER B OG  
8057  N N   . ALA B 168 ? 1.0667  1.3728  0.9440  0.1233  0.0125  0.0772  177 ALA B N   
8058  C CA  . ALA B 168 ? 0.7781  1.0492  0.6579  0.1065  0.0201  0.0638  177 ALA B CA  
8059  C C   . ALA B 168 ? 1.0341  1.3164  0.9058  0.0851  0.0065  0.0335  177 ALA B C   
8060  O O   . ALA B 168 ? 1.1012  1.3698  0.9572  0.0788  0.0120  0.0223  177 ALA B O   
8061  C CB  . ALA B 168 ? 0.4904  0.7221  0.4035  0.0969  0.0302  0.0677  177 ALA B CB  
8067  N N   . ILE B 169 ? 0.8406  1.1465  0.7221  0.0738  -0.0088 0.0198  178 ILE B N   
8068  C CA  . ILE B 169 ? 0.7443  1.0556  0.6184  0.0500  -0.0189 -0.0102 178 ILE B CA  
8069  C C   . ILE B 169 ? 0.8791  1.2090  0.7169  0.0494  -0.0195 -0.0228 178 ILE B C   
8070  O O   . ILE B 169 ? 1.2811  1.5868  1.1080  0.0347  -0.0143 -0.0420 178 ILE B O   
8071  C CB  . ILE B 169 ? 0.8712  1.2171  0.7572  0.0397  -0.0347 -0.0215 178 ILE B CB  
8072  C CG1 . ILE B 169 ? 0.8601  1.1877  0.7799  0.0389  -0.0330 -0.0113 178 ILE B CG1 
8073  C CG2 . ILE B 169 ? 0.9469  1.2926  0.8241  0.0124  -0.0414 -0.0527 178 ILE B CG2 
8074  C CD1 . ILE B 169 ? 0.8935  1.1698  0.8300  0.0234  -0.0247 -0.0169 178 ILE B CD1 
8086  N N   . LYS B 170 ? 0.8425  1.2159  0.6597  0.0665  -0.0245 -0.0117 179 LYS B N   
8087  C CA  . LYS B 170 ? 0.7855  1.1823  0.5648  0.0643  -0.0255 -0.0251 179 LYS B CA  
8088  C C   . LYS B 170 ? 0.8436  1.1960  0.6111  0.0644  -0.0079 -0.0262 179 LYS B C   
8089  O O   . LYS B 170 ? 1.4361  1.7918  1.1753  0.0543  -0.0054 -0.0465 179 LYS B O   
8090  C CB  . LYS B 170 ? 0.7349  1.1868  0.4914  0.0882  -0.0322 -0.0059 179 LYS B CB  
8091  C CG  . LYS B 170 ? 0.8739  1.3174  0.6403  0.1186  -0.0229 0.0324  179 LYS B CG  
8092  C CD  . LYS B 170 ? 0.9710  1.4759  0.7197  0.1445  -0.0326 0.0533  179 LYS B CD  
8093  C CE  . LYS B 170 ? 1.0277  1.5660  0.7311  0.1518  -0.0334 0.0524  179 LYS B CE  
8104  N N   . VAL B 171 ? 1.2182  1.5314  1.0071  0.0748  0.0056  -0.0060 180 VAL B N   
8105  C CA  . VAL B 171 ? 1.2185  1.4998  0.9977  0.0800  0.0235  -0.0017 180 VAL B CA  
8106  C C   . VAL B 171 ? 0.8482  1.0923  0.6368  0.0618  0.0293  -0.0233 180 VAL B C   
8107  O O   . VAL B 171 ? 0.9980  1.2259  0.7689  0.0618  0.0416  -0.0316 180 VAL B O   
8108  C CB  . VAL B 171 ? 0.9478  1.2079  0.7469  0.0969  0.0367  0.0284  180 VAL B CB  
8109  C CG1 . VAL B 171 ? 1.0460  1.2796  0.8380  0.1017  0.0559  0.0332  180 VAL B CG1 
8110  C CG2 . VAL B 171 ? 0.7008  0.9918  0.4879  0.1181  0.0339  0.0523  180 VAL B CG2 
8120  N N   . ILE B 172 ? 0.8757  1.1083  0.6887  0.0470  0.0210  -0.0333 181 ILE B N   
8121  C CA  . ILE B 172 ? 0.9723  1.1667  0.7955  0.0329  0.0274  -0.0493 181 ILE B CA  
8122  C C   . ILE B 172 ? 1.2924  1.4774  1.0845  0.0249  0.0351  -0.0725 181 ILE B C   
8123  O O   . ILE B 172 ? 0.9332  1.0863  0.7261  0.0294  0.0506  -0.0728 181 ILE B O   
8124  C CB  . ILE B 172 ? 0.9858  1.1774  0.8297  0.0158  0.0151  -0.0595 181 ILE B CB  
8125  C CG1 . ILE B 172 ? 1.1072  1.2913  0.9854  0.0226  0.0145  -0.0378 181 ILE B CG1 
8126  C CG2 . ILE B 172 ? 1.1168  1.2742  0.9581  -0.0004 0.0204  -0.0804 181 ILE B CG2 
8127  C CD1 . ILE B 172 ? 1.3990  1.5858  1.2973  0.0081  0.0027  -0.0443 181 ILE B CD1 
8139  N N   . PRO B 173 ? 1.1742  1.3872  0.9384  0.0136  0.0267  -0.0926 182 PRO B N   
8140  C CA  . PRO B 173 ? 1.4396  1.6410  1.1710  0.0038  0.0370  -0.1175 182 PRO B CA  
8141  C C   . PRO B 173 ? 0.9216  1.1129  0.6384  0.0213  0.0534  -0.1065 182 PRO B C   
8142  O O   . PRO B 173 ? 0.8425  1.0034  0.5444  0.0173  0.0692  -0.1224 182 PRO B O   
8143  C CB  . PRO B 173 ? 0.7762  1.0293  0.4802  -0.0084 0.0223  -0.1350 182 PRO B CB  
8144  C CG  . PRO B 173 ? 1.1545  1.4325  0.8830  -0.0117 0.0054  -0.1276 182 PRO B CG  
8145  C CD  . PRO B 173 ? 1.0038  1.2611  0.7675  0.0062  0.0079  -0.0970 182 PRO B CD  
8153  N N   . THR B 174 ? 1.7062  1.9198  1.4258  0.0411  0.0525  -0.0795 183 THR B N   
8154  C CA  . THR B 174 ? 1.7707  1.9745  1.4768  0.0569  0.0701  -0.0677 183 THR B CA  
8155  C C   . THR B 174 ? 1.0278  1.1891  0.7641  0.0619  0.0855  -0.0596 183 THR B C   
8156  O O   . THR B 174 ? 0.9347  1.0757  0.6610  0.0665  0.1032  -0.0651 183 THR B O   
8157  C CB  . THR B 174 ? 1.1962  1.4319  0.8963  0.0758  0.0668  -0.0395 183 THR B CB  
8158  O OG1 . THR B 174 ? 1.0008  1.2832  0.6717  0.0727  0.0515  -0.0480 183 THR B OG1 
8159  C CG2 . THR B 174 ? 1.6774  1.9047  1.3614  0.0911  0.0861  -0.0259 183 THR B CG2 
8167  N N   . VAL B 175 ? 0.9425  1.0929  0.7158  0.0598  0.0788  -0.0489 184 VAL B N   
8168  C CA  . VAL B 175 ? 0.7700  0.8899  0.5740  0.0638  0.0904  -0.0409 184 VAL B CA  
8169  C C   . VAL B 175 ? 0.9542  1.0434  0.7521  0.0566  0.0996  -0.0625 184 VAL B C   
8170  O O   . VAL B 175 ? 1.2058  1.2754  1.0115  0.0660  0.1163  -0.0594 184 VAL B O   
8171  C CB  . VAL B 175 ? 1.0863  1.2051  0.9271  0.0599  0.0796  -0.0283 184 VAL B CB  
8172  C CG1 . VAL B 175 ? 0.7548  0.8492  0.6253  0.0619  0.0894  -0.0233 184 VAL B CG1 
8173  C CG2 . VAL B 175 ? 1.6271  1.7672  1.4742  0.0696  0.0771  -0.0056 184 VAL B CG2 
8183  N N   . PHE B 176 ? 1.0658  1.1484  0.8536  0.0400  0.0903  -0.0831 185 PHE B N   
8184  C CA  . PHE B 176 ? 1.0048  1.0480  0.7899  0.0335  0.1016  -0.1009 185 PHE B CA  
8185  C C   . PHE B 176 ? 1.0595  1.0889  0.8105  0.0349  0.1195  -0.1194 185 PHE B C   
8186  O O   . PHE B 176 ? 0.8851  0.8785  0.6394  0.0410  0.1373  -0.1244 185 PHE B O   
8187  C CB  . PHE B 176 ? 0.8695  0.9056  0.6518  0.0127  0.0897  -0.1184 185 PHE B CB  
8188  C CG  . PHE B 176 ? 0.7445  0.7776  0.5623  0.0110  0.0785  -0.1035 185 PHE B CG  
8189  C CD1 . PHE B 176 ? 0.7422  0.7534  0.5886  0.0227  0.0864  -0.0875 185 PHE B CD1 
8190  C CD2 . PHE B 176 ? 0.9911  1.0465  0.8140  -0.0025 0.0605  -0.1061 185 PHE B CD2 
8191  C CE1 . PHE B 176 ? 1.1861  1.1970  1.0617  0.0194  0.0762  -0.0754 185 PHE B CE1 
8192  C CE2 . PHE B 176 ? 1.0919  1.1429  0.9447  -0.0053 0.0520  -0.0944 185 PHE B CE2 
8193  C CZ  . PHE B 176 ? 1.5703  1.5985  1.4479  0.0049  0.0596  -0.0793 185 PHE B CZ  
8203  N N   . LYS B 177 ? 1.0232  1.0822  0.7411  0.0308  0.1159  -0.1286 186 LYS B N   
8204  C CA  . LYS B 177 ? 0.9546  1.0045  0.6349  0.0294  0.1330  -0.1490 186 LYS B CA  
8205  C C   . LYS B 177 ? 1.0540  1.0977  0.7401  0.0513  0.1514  -0.1318 186 LYS B C   
8206  O O   . LYS B 177 ? 1.1289  1.1469  0.7980  0.0548  0.1727  -0.1458 186 LYS B O   
8207  C CB  . LYS B 177 ? 0.9719  1.0660  0.6145  0.0180  0.1207  -0.1625 186 LYS B CB  
8208  C CG  . LYS B 177 ? 1.0268  1.1166  0.6229  0.0074  0.1354  -0.1927 186 LYS B CG  
8209  C CD  . LYS B 177 ? 1.4086  1.5565  0.9700  -0.0031 0.1188  -0.2024 186 LYS B CD  
8210  C CE  . LYS B 177 ? 1.2034  1.3520  0.7151  -0.0200 0.1319  -0.2381 186 LYS B CE  
8221  N N   . ALA B 178 ? 1.0212  1.0874  0.7305  0.0652  0.1457  -0.1028 187 ALA B N   
8222  C CA  . ALA B 178 ? 1.4296  1.4941  1.1467  0.0832  0.1638  -0.0863 187 ALA B CA  
8223  C C   . ALA B 178 ? 1.2585  1.2913  1.0081  0.0918  0.1784  -0.0830 187 ALA B C   
8224  O O   . ALA B 178 ? 1.5498  1.5739  1.2987  0.1044  0.1993  -0.0814 187 ALA B O   
8225  C CB  . ALA B 178 ? 1.6928  1.7862  1.4257  0.0921  0.1554  -0.0574 187 ALA B CB  
8231  N N   . MET B 179 ? 0.9806  0.9992  0.7585  0.0864  0.1681  -0.0811 188 MET B N   
8232  C CA  . MET B 179 ? 0.9570  0.9465  0.7607  0.0955  0.1807  -0.0794 188 MET B CA  
8233  C C   . MET B 179 ? 1.2844  1.2375  1.0582  0.0936  0.1988  -0.1053 188 MET B C   
8234  O O   . MET B 179 ? 1.3248  1.2604  1.1013  0.1087  0.2210  -0.1059 188 MET B O   
8235  C CB  . MET B 179 ? 0.9513  0.9342  0.7841  0.0883  0.1644  -0.0726 188 MET B CB  
8236  C CG  . MET B 179 ? 1.1352  1.1475  1.0038  0.0896  0.1500  -0.0481 188 MET B CG  
8237  S SD  . MET B 179 ? 1.2255  1.2344  1.1209  0.0771  0.1291  -0.0431 188 MET B SD  
8238  C CE  . MET B 179 ? 1.7354  1.7103  1.6455  0.0874  0.1421  -0.0444 188 MET B CE  
8248  N N   . GLN B 180 ? 1.5084  1.4518  1.2520  0.0738  0.1910  -0.1285 189 GLN B N   
8249  C CA  . GLN B 180 ? 1.9730  1.8769  1.6844  0.0651  0.2086  -0.1581 189 GLN B CA  
8250  C C   . GLN B 180 ? 1.0312  0.9342  0.7126  0.0727  0.2302  -0.1696 189 GLN B C   
8251  O O   . GLN B 180 ? 1.1922  1.0543  0.8596  0.0768  0.2549  -0.1864 189 GLN B O   
8252  C CB  . GLN B 180 ? 1.5806  1.4895  1.2680  0.0374  0.1922  -0.1800 189 GLN B CB  
8253  C CG  . GLN B 180 ? 1.9454  1.8209  1.5924  0.0182  0.2075  -0.2168 189 GLN B CG  
8260  N N   . MET B 181 ? 0.8788  0.8234  0.5485  0.0755  0.2235  -0.1603 190 MET B N   
8261  C CA  . MET B 181 ? 1.4174  1.3674  1.0583  0.0833  0.2432  -0.1675 190 MET B CA  
8262  C C   . MET B 181 ? 1.5219  1.4830  1.1924  0.1074  0.2556  -0.1405 190 MET B C   
8263  O O   . MET B 181 ? 1.2654  1.2322  0.9152  0.1155  0.2739  -0.1435 190 MET B O   
8264  C CB  . MET B 181 ? 1.4694  1.4609  1.0714  0.0704  0.2290  -0.1749 190 MET B CB  
8265  C CG  . MET B 181 ? 1.7007  1.6896  1.2687  0.0439  0.2203  -0.2075 190 MET B CG  
8272  N N   . GLN B 182 ? 1.3970  1.3641  1.1150  0.1169  0.2469  -0.1157 191 GLN B N   
8273  C CA  . GLN B 182 ? 1.2251  1.2063  0.9767  0.1362  0.2589  -0.0921 191 GLN B CA  
8274  C C   . GLN B 182 ? 0.9036  0.9193  0.6412  0.1383  0.2594  -0.0788 191 GLN B C   
8275  O O   . GLN B 182 ? 1.3564  1.3785  1.0961  0.1508  0.2796  -0.0723 191 GLN B O   
8276  C CB  . GLN B 182 ? 1.4621  1.4159  1.2182  0.1523  0.2875  -0.1004 191 GLN B CB  
8277  C CG  . GLN B 182 ? 1.3484  1.2752  1.1379  0.1608  0.2891  -0.0970 191 GLN B CG  
8278  C CD  . GLN B 182 ? 1.3912  1.3458  1.2356  0.1746  0.2837  -0.0680 191 GLN B CD  
8279  O OE1 . GLN B 182 ? 1.7100  1.6524  1.5826  0.1824  0.2813  -0.0609 191 GLN B OE1 
8280  N NE2 . GLN B 182 ? 1.5151  1.5076  1.3729  0.1767  0.2830  -0.0517 191 GLN B NE2 
8289  N N   . GLU B 183 ? 1.3857  1.4234  1.1067  0.1270  0.2385  -0.0746 192 GLU B N   
8290  C CA  . GLU B 183 ? 1.2781  1.3464  0.9841  0.1305  0.2372  -0.0573 192 GLU B CA  
8291  C C   . GLU B 183 ? 1.2210  1.3042  0.9681  0.1341  0.2287  -0.0289 192 GLU B C   
8292  O O   . GLU B 183 ? 1.2239  1.3169  0.9777  0.1268  0.2082  -0.0214 192 GLU B O   
8293  C CB  . GLU B 183 ? 1.4281  1.5146  1.0919  0.1193  0.2205  -0.0672 192 GLU B CB  
8294  C CG  . GLU B 183 ? 1.6592  1.7395  1.2759  0.1125  0.2305  -0.0957 192 GLU B CG  
8295  C CD  . GLU B 183 ? 1.7010  1.7896  1.2924  0.1234  0.2524  -0.0915 192 GLU B CD  
8296  O OE1 . GLU B 183 ? 1.9086  2.0186  1.5054  0.1333  0.2530  -0.0647 192 GLU B OE1 
8297  O OE2 . GLU B 183 ? 1.7454  1.8173  1.3092  0.1212  0.2707  -0.1155 192 GLU B OE2 
8304  N N   . ARG B 184 ? 1.2909  1.3770  1.0661  0.1442  0.2461  -0.0145 193 ARG B N   
8305  C CA  . ARG B 184 ? 1.0007  1.1001  0.8162  0.1439  0.2417  0.0088  193 ARG B CA  
8306  C C   . ARG B 184 ? 1.3772  1.4916  1.1737  0.1427  0.2376  0.0260  193 ARG B C   
8307  O O   . ARG B 184 ? 0.7151  0.8345  0.5326  0.1377  0.2260  0.0400  193 ARG B O   
8308  C CB  . ARG B 184 ? 1.0723  1.1775  0.9218  0.1530  0.2633  0.0169  193 ARG B CB  
8309  C CG  . ARG B 184 ? 1.0059  1.1291  0.8974  0.1492  0.2640  0.0381  193 ARG B CG  
8310  C CD  . ARG B 184 ? 0.8214  0.9546  0.6975  0.1499  0.2792  0.0538  193 ARG B CD  
8311  N NE  . ARG B 184 ? 0.9902  1.1373  0.9067  0.1433  0.2860  0.0702  193 ARG B NE  
8312  C CZ  . ARG B 184 ? 0.9570  1.1068  0.8660  0.1402  0.2993  0.0867  193 ARG B CZ  
8313  N NH1 . ARG B 184 ? 0.9084  1.0506  0.7704  0.1467  0.3054  0.0916  193 ARG B NH1 
8314  N NH2 . ARG B 184 ? 0.6876  0.8476  0.6339  0.1299  0.3072  0.0984  193 ARG B NH2 
8328  N N   . ASP B 185 ? 1.0469  1.1675  0.8023  0.1481  0.2480  0.0264  194 ASP B N   
8329  C CA  . ASP B 185 ? 1.2774  1.4105  1.0142  0.1506  0.2449  0.0469  194 ASP B CA  
8330  C C   . ASP B 185 ? 1.2955  1.4360  1.0208  0.1452  0.2184  0.0447  194 ASP B C   
8331  O O   . ASP B 185 ? 1.1221  1.2664  0.8612  0.1455  0.2103  0.0630  194 ASP B O   
8332  C CB  . ASP B 185 ? 1.3850  1.5263  1.0759  0.1589  0.2611  0.0493  194 ASP B CB  
8333  C CG  . ASP B 185 ? 1.0278  1.1658  0.7322  0.1645  0.2897  0.0577  194 ASP B CG  
8334  O OD1 . ASP B 185 ? 1.0783  1.2136  0.8284  0.1618  0.2963  0.0679  194 ASP B OD1 
8335  O OD2 . ASP B 185 ? 0.9808  1.1227  0.6494  0.1704  0.3059  0.0539  194 ASP B OD2 
8340  N N   . THR B 186 ? 1.7917  1.9343  1.4922  0.1393  0.2062  0.0212  195 THR B N   
8341  C CA  . THR B 186 ? 0.8583  1.0150  0.5499  0.1331  0.1814  0.0185  195 THR B CA  
8342  C C   . THR B 186 ? 0.8899  1.0364  0.6266  0.1260  0.1686  0.0227  195 THR B C   
8343  O O   . THR B 186 ? 0.9016  1.0597  0.6442  0.1247  0.1526  0.0327  195 THR B O   
8344  C CB  . THR B 186 ? 1.0024  1.1637  0.6626  0.1228  0.1722  -0.0118 195 THR B CB  
8345  O OG1 . THR B 186 ? 1.1010  1.2755  0.7150  0.1273  0.1835  -0.0182 195 THR B OG1 
8346  C CG2 . THR B 186 ? 1.1006  1.2832  0.7560  0.1140  0.1459  -0.0169 195 THR B CG2 
8354  N N   . LEU B 187 ? 0.7184  0.8454  0.4868  0.1224  0.1757  0.0157  196 LEU B N   
8355  C CA  . LEU B 187 ? 0.8381  0.9579  0.6460  0.1147  0.1632  0.0183  196 LEU B CA  
8356  C C   . LEU B 187 ? 0.6951  0.8207  0.5278  0.1170  0.1654  0.0428  196 LEU B C   
8357  O O   . LEU B 187 ? 0.6240  0.7501  0.4781  0.1103  0.1517  0.0472  196 LEU B O   
8358  C CB  . LEU B 187 ? 0.6903  0.7923  0.5245  0.1138  0.1714  0.0082  196 LEU B CB  
8359  C CG  . LEU B 187 ? 0.6854  0.7842  0.5625  0.1072  0.1609  0.0146  196 LEU B CG  
8360  C CD1 . LEU B 187 ? 0.6449  0.7419  0.5166  0.0965  0.1401  0.0056  196 LEU B CD1 
8361  C CD2 . LEU B 187 ? 0.8980  0.9857  0.8028  0.1109  0.1697  0.0102  196 LEU B CD2 
8373  N N   . LEU B 188 ? 1.0337  1.1607  0.8663  0.1247  0.1851  0.0575  197 LEU B N   
8374  C CA  . LEU B 188 ? 1.0500  1.1764  0.9070  0.1237  0.1923  0.0787  197 LEU B CA  
8375  C C   . LEU B 188 ? 1.1861  1.3171  1.0227  0.1282  0.1833  0.0923  197 LEU B C   
8376  O O   . LEU B 188 ? 0.6055  0.7332  0.4634  0.1227  0.1742  0.0986  197 LEU B O   
8377  C CB  . LEU B 188 ? 1.8760  2.0020  1.7362  0.1287  0.2187  0.0892  197 LEU B CB  
8378  C CG  . LEU B 188 ? 1.4207  1.5443  1.3122  0.1229  0.2345  0.1060  197 LEU B CG  
8379  C CD1 . LEU B 188 ? 1.1952  1.3254  1.1020  0.1235  0.2563  0.1048  197 LEU B CD1 
8380  C CD2 . LEU B 188 ? 1.2198  1.3359  1.0872  0.1289  0.2440  0.1266  197 LEU B CD2 
8392  N N   . LYS B 189 ? 0.7696  0.9110  0.5635  0.1387  0.1841  0.0949  198 LYS B N   
8393  C CA  . LYS B 189 ? 0.7875  0.9410  0.5580  0.1479  0.1744  0.1091  198 LYS B CA  
8394  C C   . LYS B 189 ? 0.8693  1.0312  0.6530  0.1404  0.1496  0.0986  198 LYS B C   
8395  O O   . LYS B 189 ? 1.0219  1.1861  0.8129  0.1451  0.1440  0.1135  198 LYS B O   
8396  C CB  . LYS B 189 ? 1.0520  1.2255  0.7724  0.1588  0.1745  0.1077  198 LYS B CB  
8397  C CG  . LYS B 189 ? 1.2321  1.4275  0.9243  0.1732  0.1649  0.1260  198 LYS B CG  
8404  N N   . ALA B 190 ? 0.8048  0.9693  0.5908  0.1291  0.1368  0.0731  199 ALA B N   
8405  C CA  . ALA B 190 ? 0.7029  0.8757  0.4999  0.1198  0.1149  0.0618  199 ALA B CA  
8406  C C   . ALA B 190 ? 0.6899  0.8483  0.5275  0.1139  0.1139  0.0714  199 ALA B C   
8407  O O   . ALA B 190 ? 0.9085  1.0745  0.7518  0.1164  0.1051  0.0809  199 ALA B O   
8408  C CB  . ALA B 190 ? 0.7482  0.9163  0.5419  0.1067  0.1073  0.0333  199 ALA B CB  
8414  N N   . LEU B 191 ? 1.0864  1.2269  0.9524  0.1071  0.1245  0.0701  200 LEU B N   
8415  C CA  . LEU B 191 ? 1.0573  1.1882  0.9602  0.0987  0.1239  0.0772  200 LEU B CA  
8416  C C   . LEU B 191 ? 1.3301  1.4566  1.2346  0.1058  0.1345  0.0998  200 LEU B C   
8417  O O   . LEU B 191 ? 1.2543  1.3757  1.1795  0.0997  0.1296  0.1034  200 LEU B O   
8418  C CB  . LEU B 191 ? 1.1015  1.2235  1.0322  0.0918  0.1351  0.0742  200 LEU B CB  
8419  C CG  . LEU B 191 ? 1.0152  1.1348  0.9512  0.0864  0.1267  0.0551  200 LEU B CG  
8420  C CD1 . LEU B 191 ? 1.0162  1.1341  0.9732  0.0877  0.1417  0.0559  200 LEU B CD1 
8421  C CD2 . LEU B 191 ? 0.7319  0.8495  0.6902  0.0744  0.1104  0.0488  200 LEU B CD2 
8433  N N   . LEU B 192 ? 0.9383  1.0634  0.8197  0.1189  0.1512  0.1154  201 LEU B N   
8434  C CA  . LEU B 192 ? 0.8661  0.9792  0.7460  0.1273  0.1655  0.1390  201 LEU B CA  
8435  C C   . LEU B 192 ? 1.6589  1.7843  1.5206  0.1401  0.1522  0.1476  201 LEU B C   
8436  O O   . LEU B 192 ? 1.0979  1.2105  0.9702  0.1442  0.1583  0.1623  201 LEU B O   
8437  C CB  . LEU B 192 ? 0.9499  1.0555  0.8075  0.1384  0.1894  0.1557  201 LEU B CB  
8438  C CG  . LEU B 192 ? 0.9273  1.0218  0.8041  0.1283  0.2106  0.1546  201 LEU B CG  
8439  C CD1 . LEU B 192 ? 1.3401  1.4270  1.1890  0.1406  0.2344  0.1734  201 LEU B CD1 
8440  C CD2 . LEU B 192 ? 0.7350  0.8151  0.6510  0.1122  0.2181  0.1555  201 LEU B CD2 
8452  N N   . GLU B 193 ? 2.4543  2.6061  2.2877  0.1473  0.1361  0.1389  202 GLU B N   
8453  C CA  . GLU B 193 ? 1.3143  1.4897  1.1338  0.1590  0.1204  0.1450  202 GLU B CA  
8454  C C   . GLU B 193 ? 0.9058  1.0803  0.7568  0.1466  0.1058  0.1341  202 GLU B C   
8455  O O   . GLU B 193 ? 1.2302  1.4085  1.0872  0.1561  0.1034  0.1469  202 GLU B O   
8456  C CB  . GLU B 193 ? 1.6296  1.8400  1.4151  0.1623  0.1048  0.1311  202 GLU B CB  
8457  C CG  . GLU B 193 ? 1.8659  2.1145  1.6411  0.1692  0.0832  0.1295  202 GLU B CG  
8458  C CD  . GLU B 193 ? 1.9470  2.2087  1.7060  0.1962  0.0888  0.1610  202 GLU B CD  
8459  O OE1 . GLU B 193 ? 2.1388  2.3839  1.8800  0.2105  0.1089  0.1828  202 GLU B OE1 
8460  O OE2 . GLU B 193 ? 1.6656  1.9545  1.4297  0.2042  0.0742  0.1648  202 GLU B OE2 
8467  N N   . ILE B 194 ? 0.9007  1.0695  0.7716  0.1267  0.0976  0.1116  203 ILE B N   
8468  C CA  . ILE B 194 ? 0.6566  0.8229  0.5561  0.1128  0.0851  0.1008  203 ILE B CA  
8469  C C   . ILE B 194 ? 0.8530  0.9942  0.7791  0.1104  0.0997  0.1146  203 ILE B C   
8470  O O   . ILE B 194 ? 1.1968  1.3382  1.1372  0.1092  0.0944  0.1167  203 ILE B O   
8471  C CB  . ILE B 194 ? 0.4849  0.6465  0.3962  0.0939  0.0762  0.0766  203 ILE B CB  
8472  C CG1 . ILE B 194 ? 1.1667  1.3510  1.0531  0.0913  0.0602  0.0580  203 ILE B CG1 
8473  C CG2 . ILE B 194 ? 0.4513  0.6019  0.3956  0.0781  0.0700  0.0695  203 ILE B CG2 
8474  C CD1 . ILE B 194 ? 1.2664  1.4383  1.1577  0.0760  0.0567  0.0362  203 ILE B CD1 
8486  N N   . ALA B 195 ? 1.0555  1.1758  0.9894  0.1075  0.1196  0.1223  204 ALA B N   
8487  C CA  . ALA B 195 ? 1.2107  1.3073  1.1702  0.0995  0.1350  0.1309  204 ALA B CA  
8488  C C   . ALA B 195 ? 1.2856  1.3726  1.2346  0.1165  0.1450  0.1517  204 ALA B C   
8489  O O   . ALA B 195 ? 0.7189  0.7936  0.6864  0.1115  0.1474  0.1530  204 ALA B O   
8490  C CB  . ALA B 195 ? 0.9547  1.0362  0.9236  0.0920  0.1564  0.1347  204 ALA B CB  
8496  N N   . SER B 196 ? 0.7955  0.8900  0.7131  0.1384  0.1501  0.1682  205 SER B N   
8497  C CA  . SER B 196 ? 0.7248  0.8098  0.6308  0.1596  0.1615  0.1922  205 SER B CA  
8498  C C   . SER B 196 ? 1.3120  1.4189  1.2247  0.1655  0.1417  0.1880  205 SER B C   
8499  O O   . SER B 196 ? 0.9859  1.0759  0.9096  0.1730  0.1516  0.1999  205 SER B O   
8500  C CB  . SER B 196 ? 0.8873  0.9827  0.7549  0.1837  0.1685  0.2120  205 SER B CB  
8501  O OG  . SER B 196 ? 1.4349  1.5208  1.2903  0.2085  0.1804  0.2392  205 SER B OG  
8507  N N   . CYS B 197 ? 1.0423  1.1859  0.9488  0.1609  0.1157  0.1697  206 CYS B N   
8508  C CA  . CYS B 197 ? 1.0053  1.1786  0.9171  0.1652  0.0957  0.1636  206 CYS B CA  
8509  C C   . CYS B 197 ? 0.8537  1.0081  0.7996  0.1475  0.0958  0.1528  206 CYS B C   
8510  O O   . CYS B 197 ? 0.8532  1.0137  0.8087  0.1563  0.0939  0.1587  206 CYS B O   
8511  C CB  . CYS B 197 ? 0.8289  1.0416  0.7265  0.1572  0.0713  0.1419  206 CYS B CB  
8512  S SG  . CYS B 197 ? 1.0523  1.2987  0.9031  0.1807  0.0696  0.1550  206 CYS B SG  
8518  N N   . LEU B 198 ? 0.9543  1.0858  0.9182  0.1244  0.1007  0.1394  207 LEU B N   
8519  C CA  . LEU B 198 ? 0.8459  0.9581  0.8399  0.1057  0.1039  0.1302  207 LEU B CA  
8520  C C   . LEU B 198 ? 0.8001  0.8771  0.8018  0.1107  0.1308  0.1473  207 LEU B C   
8521  O O   . LEU B 198 ? 0.7995  0.8617  0.8217  0.1004  0.1358  0.1426  207 LEU B O   
8522  C CB  . LEU B 198 ? 1.0104  1.1155  1.0196  0.0812  0.1007  0.1125  207 LEU B CB  
8523  C CG  . LEU B 198 ? 1.1358  1.2641  1.1399  0.0724  0.0781  0.0931  207 LEU B CG  
8524  C CD1 . LEU B 198 ? 1.4860  1.6056  1.5002  0.0574  0.0801  0.0831  207 LEU B CD1 
8525  C CD2 . LEU B 198 ? 0.6118  0.7507  0.6302  0.0617  0.0628  0.0806  207 LEU B CD2 
8537  N N   . GLU B 199 ? 0.9154  0.9748  0.9006  0.1232  0.1510  0.1655  208 GLU B N   
8538  C CA  . GLU B 199 ? 0.8935  0.9140  0.8826  0.1291  0.1799  0.1829  208 GLU B CA  
8539  C C   . GLU B 199 ? 0.8838  0.9089  0.8618  0.1579  0.1809  0.2014  208 GLU B C   
8540  O O   . GLU B 199 ? 0.8611  0.8631  0.8539  0.1578  0.1935  0.2042  208 GLU B O   
8541  C CB  . GLU B 199 ? 0.9112  0.9076  0.8864  0.1317  0.2047  0.1971  208 GLU B CB  
8542  C CG  . GLU B 199 ? 1.4375  1.4206  1.4357  0.1007  0.2141  0.1809  208 GLU B CG  
8549  N N   . LYS B 200 ? 0.9786  1.0400  0.9324  0.1813  0.1651  0.2111  209 LYS B N   
8550  C CA  . LYS B 200 ? 1.0620  1.1415  1.0066  0.2116  0.1623  0.2295  209 LYS B CA  
8551  C C   . LYS B 200 ? 1.1349  1.2298  1.1052  0.2024  0.1476  0.2132  209 LYS B C   
8552  O O   . LYS B 200 ? 1.4368  1.5225  1.4144  0.2199  0.1583  0.2264  209 LYS B O   
8553  C CB  . LYS B 200 ? 0.7659  0.8951  0.6808  0.2327  0.1430  0.2373  209 LYS B CB  
8554  C CG  . LYS B 200 ? 0.9430  1.0579  0.8252  0.2571  0.1630  0.2665  209 LYS B CG  
8561  N N   . ALA B 201 ? 0.9469  1.0648  0.9301  0.1765  0.1244  0.1852  210 ALA B N   
8562  C CA  . ALA B 201 ? 0.8465  0.9789  0.8529  0.1652  0.1112  0.1688  210 ALA B CA  
8563  C C   . ALA B 201 ? 0.8100  0.8979  0.8394  0.1506  0.1321  0.1657  210 ALA B C   
8564  O O   . ALA B 201 ? 0.9934  1.0859  1.0400  0.1481  0.1292  0.1587  210 ALA B O   
8565  C CB  . ALA B 201 ? 0.8633  1.0225  0.8757  0.1393  0.0854  0.1408  210 ALA B CB  
8571  N N   . LEU B 202 ? 0.9697  1.0180  1.0009  0.1371  0.1527  0.1673  211 LEU B N   
8572  C CA  . LEU B 202 ? 1.2361  1.2440  1.2871  0.1208  0.1744  0.1623  211 LEU B CA  
8573  C C   . LEU B 202 ? 1.1908  1.1715  1.2378  0.1473  0.1990  0.1845  211 LEU B C   
8574  O O   . LEU B 202 ? 0.8334  0.7983  0.8971  0.1419  0.2079  0.1780  211 LEU B O   
8575  C CB  . LEU B 202 ? 0.9444  0.9224  0.9988  0.0983  0.1917  0.1578  211 LEU B CB  
8576  C CG  . LEU B 202 ? 1.0592  0.9930  1.1298  0.0804  0.2199  0.1533  211 LEU B CG  
8577  C CD1 . LEU B 202 ? 1.2859  1.2279  1.3785  0.0587  0.2087  0.1310  211 LEU B CD1 
8578  C CD2 . LEU B 202 ? 0.6695  0.5836  0.7430  0.0587  0.2364  0.1494  211 LEU B CD2 
8590  N N   . GLN B 203 ? 1.1041  1.0796  1.1278  0.1781  0.2107  0.2117  212 GLN B N   
8591  C CA  . GLN B 203 ? 1.3997  1.3417  1.4173  0.2072  0.2390  0.2375  212 GLN B CA  
8592  C C   . GLN B 203 ? 1.6413  1.6175  1.6678  0.2287  0.2246  0.2400  212 GLN B C   
8593  O O   . GLN B 203 ? 2.0589  2.0058  2.0930  0.2443  0.2471  0.2511  212 GLN B O   
8594  C CB  . GLN B 203 ? 1.4514  1.3853  1.4381  0.2385  0.2530  0.2694  212 GLN B CB  
8595  C CG  . GLN B 203 ? 1.5109  1.4196  1.4855  0.2209  0.2665  0.2694  212 GLN B CG  
8596  C CD  . GLN B 203 ? 1.4761  1.3345  1.4701  0.1862  0.2918  0.2534  212 GLN B CD  
8597  O OE1 . GLN B 203 ? 1.2836  1.0960  1.2844  0.1880  0.3206  0.2594  212 GLN B OE1 
8598  N NE2 . GLN B 203 ? 1.5522  1.4206  1.5549  0.1543  0.2827  0.2325  212 GLN B NE2 
8607  N N   . VAL B 204 ? 1.4417  1.4799  1.4678  0.2289  0.1890  0.2288  213 VAL B N   
8608  C CA  . VAL B 204 ? 1.0296  1.1131  1.0667  0.2448  0.1712  0.2271  213 VAL B CA  
8609  C C   . VAL B 204 ? 0.9857  1.0573  1.0513  0.2189  0.1716  0.2029  213 VAL B C   
8610  O O   . VAL B 204 ? 0.9927  1.0836  1.0719  0.2331  0.1698  0.2040  213 VAL B O   
8611  C CB  . VAL B 204 ? 1.0535  1.2053  1.0809  0.2443  0.1348  0.2170  213 VAL B CB  
8612  C CG1 . VAL B 204 ? 1.1629  1.3652  1.2078  0.2516  0.1161  0.2086  213 VAL B CG1 
8613  C CG2 . VAL B 204 ? 1.0095  1.1793  1.0056  0.2725  0.1345  0.2418  213 VAL B CG2 
8623  N N   . PHE B 205 ? 1.0332  1.0857  1.1081  0.1806  0.1686  0.1789  214 PHE B N   
8624  C CA  . PHE B 205 ? 0.7561  0.7946  0.8544  0.1544  0.1712  0.1567  214 PHE B CA  
8625  C C   . PHE B 205 ? 1.0633  1.0468  1.1684  0.1608  0.2079  0.1660  214 PHE B C   
8626  O O   . PHE B 205 ? 0.7804  0.7559  0.9035  0.1482  0.2131  0.1513  214 PHE B O   
8627  C CB  . PHE B 205 ? 0.6298  0.6624  0.7328  0.1153  0.1609  0.1335  214 PHE B CB  
8628  C CG  . PHE B 205 ? 0.5241  0.5581  0.6474  0.0840  0.1533  0.1075  214 PHE B CG  
8629  C CD1 . PHE B 205 ? 0.6089  0.6542  0.7456  0.0877  0.1522  0.1014  214 PHE B CD1 
8630  C CD2 . PHE B 205 ? 1.0292  1.0573  1.1575  0.0511  0.1467  0.0896  214 PHE B CD2 
8631  C CE1 . PHE B 205 ? 1.0625  1.1102  1.2148  0.0570  0.1450  0.0771  214 PHE B CE1 
8632  C CE2 . PHE B 205 ? 0.4368  0.4697  0.5805  0.0223  0.1384  0.0670  214 PHE B CE2 
8633  C CZ  . PHE B 205 ? 0.6998  0.7406  0.8538  0.0245  0.1379  0.0608  214 PHE B CZ  
8643  N N   . HIS B 206 ? 1.0631  1.0052  1.1528  0.1784  0.2358  0.1891  215 HIS B N   
8644  C CA  . HIS B 206 ? 1.1509  1.0316  1.2436  0.1849  0.2761  0.1987  215 HIS B CA  
8645  C C   . HIS B 206 ? 1.2064  1.0954  1.3060  0.2190  0.2831  0.2126  215 HIS B C   
8646  O O   . HIS B 206 ? 1.8602  1.7032  1.9695  0.2178  0.3129  0.2104  215 HIS B O   
8647  C CB  . HIS B 206 ? 1.2875  1.1219  1.3587  0.1991  0.3057  0.2235  215 HIS B CB  
8648  C CG  . HIS B 206 ? 1.3566  1.1602  1.4284  0.1601  0.3169  0.2074  215 HIS B CG  
8649  N ND1 . HIS B 206 ? 1.3050  1.1456  1.3807  0.1332  0.2883  0.1883  215 HIS B ND1 
8650  C CD2 . HIS B 206 ? 1.6329  1.3748  1.7034  0.1427  0.3549  0.2068  215 HIS B CD2 
8651  C CE1 . HIS B 206 ? 1.3740  1.1834  1.4528  0.1031  0.3060  0.1777  215 HIS B CE1 
8652  N NE2 . HIS B 206 ? 1.8471  1.5977  1.9229  0.1059  0.3462  0.1872  215 HIS B NE2 
8660  N N   . GLN B 207 ? 0.9774  0.9276  1.0733  0.2481  0.2565  0.2247  216 GLN B N   
8661  C CA  . GLN B 207 ? 1.1242  1.0967  1.2285  0.2857  0.2602  0.2408  216 GLN B CA  
8662  C C   . GLN B 207 ? 1.1063  1.0845  1.2369  0.2669  0.2582  0.2159  216 GLN B C   
8663  O O   . GLN B 207 ? 1.0568  1.0398  1.1987  0.2947  0.2702  0.2266  216 GLN B O   
8664  C CB  . GLN B 207 ? 1.2655  1.3174  1.3619  0.3124  0.2263  0.2528  216 GLN B CB  
8665  C CG  . GLN B 207 ? 1.0445  1.0971  1.1118  0.3363  0.2283  0.2801  216 GLN B CG  
8666  C CD  . GLN B 207 ? 1.1588  1.2928  1.2171  0.3603  0.1960  0.2895  216 GLN B CD  
8667  O OE1 . GLN B 207 ? 1.3007  1.4871  1.3751  0.3754  0.1813  0.2878  216 GLN B OE1 
8668  N NE2 . GLN B 207 ? 1.0275  1.1760  1.0594  0.3648  0.1862  0.3000  216 GLN B NE2 
8677  N N   . ILE B 208 ? 1.0182  0.9966  1.1585  0.2215  0.2443  0.1840  217 ILE B N   
8678  C CA  . ILE B 208 ? 1.0508  1.0394  1.2134  0.2013  0.2401  0.1594  217 ILE B CA  
8679  C C   . ILE B 208 ? 1.2440  1.1763  1.4150  0.2107  0.2801  0.1634  217 ILE B C   
8680  O O   . ILE B 208 ? 0.8957  0.8422  1.0844  0.2138  0.2818  0.1538  217 ILE B O   
8681  C CB  . ILE B 208 ? 0.8003  0.7882  0.9670  0.1512  0.2237  0.1281  217 ILE B CB  
8682  C CG1 . ILE B 208 ? 0.6743  0.6790  0.8605  0.1310  0.2166  0.1041  217 ILE B CG1 
8683  C CG2 . ILE B 208 ? 1.5230  1.4471  1.6839  0.1276  0.2518  0.1235  217 ILE B CG2 
8684  C CD1 . ILE B 208 ? 0.7456  0.7692  0.9342  0.0894  0.1916  0.0776  217 ILE B CD1 
8696  N N   . HIS B 209 ? 0.9638  0.8289  1.1225  0.2113  0.3148  0.1746  218 HIS B N   
8697  C CA  . HIS B 209 ? 1.0953  0.8951  1.2601  0.2093  0.3571  0.1712  218 HIS B CA  
8698  C C   . HIS B 209 ? 1.1812  0.9773  1.3491  0.2617  0.3771  0.1992  218 HIS B C   
8699  O O   . HIS B 209 ? 1.1058  0.8667  1.2853  0.2656  0.4056  0.1931  218 HIS B O   
8700  C CB  . HIS B 209 ? 0.9970  0.7272  1.1466  0.1926  0.3896  0.1743  218 HIS B CB  
8701  C CG  . HIS B 209 ? 1.2507  0.9802  1.4027  0.1390  0.3774  0.1438  218 HIS B CG  
8702  N ND1 . HIS B 209 ? 1.6576  1.3804  1.8237  0.0995  0.3793  0.1111  218 HIS B ND1 
8703  C CD2 . HIS B 209 ? 0.9078  0.6452  1.0498  0.1200  0.3643  0.1423  218 HIS B CD2 
8704  C CE1 . HIS B 209 ? 0.6957  0.4251  0.8607  0.0594  0.3666  0.0920  218 HIS B CE1 
8705  N NE2 . HIS B 209 ? 1.3825  1.1204  1.5344  0.0715  0.3579  0.1103  218 HIS B NE2 
8712  N N   . ASP B 210 ? 1.9860  1.8208  2.1429  0.3028  0.3627  0.2299  219 ASP B N   
8713  C CA  . ASP B 210 ? 1.2615  1.1028  1.4191  0.3596  0.3788  0.2632  219 ASP B CA  
8714  C C   . ASP B 210 ? 1.0518  0.9649  1.2335  0.3743  0.3548  0.2560  219 ASP B C   
8715  O O   . ASP B 210 ? 1.6925  1.6159  1.8751  0.4112  0.3647  0.2772  219 ASP B O   
8716  C CB  . ASP B 210 ? 1.4671  1.3358  1.6019  0.3963  0.3675  0.2983  219 ASP B CB  
8717  C CG  . ASP B 210 ? 1.5905  1.3984  1.7008  0.3815  0.3876  0.3060  219 ASP B CG  
8718  O OD1 . ASP B 210 ? 1.7446  1.4731  1.8527  0.3617  0.4263  0.2983  219 ASP B OD1 
8719  O OD2 . ASP B 210 ? 1.4568  1.2998  1.5495  0.3853  0.3641  0.3166  219 ASP B OD2 
8724  N N   . HIS B 211 ? 1.1468  1.0083  0.9503  -0.0165 -0.0776 0.1071  220 HIS B N   
8725  C CA  . HIS B 211 ? 1.0178  0.9174  0.8335  0.0248  -0.0733 0.0827  220 HIS B CA  
8726  C C   . HIS B 211 ? 0.8107  0.7215  0.6309  0.0173  -0.0707 0.0477  220 HIS B C   
8727  O O   . HIS B 211 ? 1.0567  1.0028  0.8908  0.0464  -0.0640 0.0263  220 HIS B O   
8728  C CB  . HIS B 211 ? 1.1342  1.1232  0.9779  0.0415  -0.0706 0.0947  220 HIS B CB  
8729  C CG  . HIS B 211 ? 1.2067  1.1878  1.0383  0.0535  -0.0724 0.1293  220 HIS B CG  
8730  N ND1 . HIS B 211 ? 1.4678  1.4903  1.3058  0.0315  -0.0703 0.1566  220 HIS B ND1 
8731  C CD2 . HIS B 211 ? 1.3564  1.2915  1.1661  0.0868  -0.0756 0.1422  220 HIS B CD2 
8732  C CE1 . HIS B 211 ? 1.2462  1.2488  1.0633  0.0496  -0.0707 0.1858  220 HIS B CE1 
8733  N NE2 . HIS B 211 ? 1.3759  1.3239  1.1749  0.0838  -0.0753 0.1784  220 HIS B NE2 
8740  N N   . VAL B 212 ? 0.9913  0.8691  0.7978  -0.0203 -0.0760 0.0411  221 VAL B N   
8741  C CA  . VAL B 212 ? 1.0448  0.9203  0.8427  -0.0272 -0.0749 0.0091  221 VAL B CA  
8742  C C   . VAL B 212 ? 1.2745  1.0607  1.0363  -0.0487 -0.0834 -0.0027 221 VAL B C   
8743  O O   . VAL B 212 ? 1.4537  1.2008  1.2092  -0.0786 -0.0926 0.0158  221 VAL B O   
8744  C CB  . VAL B 212 ? 0.9954  0.9419  0.8151  -0.0532 -0.0770 0.0082  221 VAL B CB  
8745  C CG1 . VAL B 212 ? 1.0862  1.0286  0.8898  -0.0536 -0.0743 -0.0227 221 VAL B CG1 
8746  C CG2 . VAL B 212 ? 0.8218  0.8528  0.6778  -0.0365 -0.0708 0.0205  221 VAL B CG2 
8756  N N   . ASN B 213 ? 1.1027  0.8574  0.8414  -0.0343 -0.0794 -0.0344 222 ASN B N   
8757  C CA  . ASN B 213 ? 1.2038  0.8774  0.9054  -0.0541 -0.0888 -0.0519 222 ASN B CA  
8758  C C   . ASN B 213 ? 1.1628  0.8620  0.8537  -0.0769 -0.0932 -0.0734 222 ASN B C   
8759  O O   . ASN B 213 ? 0.9945  0.7494  0.6937  -0.0602 -0.0820 -0.0850 222 ASN B O   
8760  C CB  . ASN B 213 ? 1.5756  1.1795  1.2480  -0.0173 -0.0817 -0.0750 222 ASN B CB  
8761  C CG  . ASN B 213 ? 2.0683  1.5937  1.6970  -0.0341 -0.0903 -0.1040 222 ASN B CG  
8766  N N   . PRO B 214 ? 1.1420  0.8027  0.8147  -0.1153 -0.1101 -0.0786 223 PRO B N   
8767  C CA  . PRO B 214 ? 1.1618  0.8496  0.8205  -0.1342 -0.1176 -0.0983 223 PRO B CA  
8768  C C   . PRO B 214 ? 1.3233  0.9945  0.9471  -0.1047 -0.1048 -0.1304 223 PRO B C   
8769  O O   . PRO B 214 ? 1.1043  0.8301  0.7290  -0.0999 -0.0977 -0.1371 223 PRO B O   
8770  C CB  . PRO B 214 ? 1.1459  0.7800  0.7884  -0.1771 -0.1408 -0.1027 223 PRO B CB  
8771  C CG  . PRO B 214 ? 1.7217  1.3381  1.3903  -0.1910 -0.1428 -0.0720 223 PRO B CG  
8772  C CD  . PRO B 214 ? 1.8657  1.4689  1.5363  -0.1472 -0.1244 -0.0628 223 PRO B CD  
8780  N N   . LYS B 215 ? 1.6921  1.2877  1.2847  -0.0838 -0.1001 -0.1496 224 LYS B N   
8781  C CA  . LYS B 215 ? 1.5878  1.1637  1.1430  -0.0562 -0.0860 -0.1833 224 LYS B CA  
8782  C C   . LYS B 215 ? 1.4042  1.0562  0.9865  -0.0252 -0.0619 -0.1802 224 LYS B C   
8783  O O   . LYS B 215 ? 1.2116  0.8944  0.7770  -0.0220 -0.0516 -0.1953 224 LYS B O   
8784  C CB  . LYS B 215 ? 2.1237  1.6097  1.6498  -0.0318 -0.0829 -0.2022 224 LYS B CB  
8787  N N   . ALA B 216 ? 1.5799  1.2623  1.2037  -0.0030 -0.0532 -0.1600 225 ALA B N   
8788  C CA  . ALA B 216 ? 1.4672  1.2178  1.1219  0.0280  -0.0311 -0.1610 225 ALA B CA  
8789  C C   . ALA B 216 ? 1.2702  1.0991  0.9483  0.0094  -0.0295 -0.1492 225 ALA B C   
8790  O O   . ALA B 216 ? 1.1366  1.0037  0.8164  0.0220  -0.0116 -0.1613 225 ALA B O   
8791  C CB  . ALA B 216 ? 1.5231  1.2892  1.2163  0.0551  -0.0281 -0.1425 225 ALA B CB  
8797  N N   . PHE B 217 ? 1.3564  1.2089  1.0533  -0.0204 -0.0469 -0.1254 226 PHE B N   
8798  C CA  . PHE B 217 ? 1.1354  1.0610  0.8581  -0.0348 -0.0472 -0.1129 226 PHE B CA  
8799  C C   . PHE B 217 ? 0.9792  0.9021  0.6662  -0.0493 -0.0481 -0.1291 226 PHE B C   
8800  O O   . PHE B 217 ? 0.8319  0.8037  0.5289  -0.0445 -0.0366 -0.1287 226 PHE B O   
8801  C CB  . PHE B 217 ? 1.1444  1.0930  0.8932  -0.0622 -0.0655 -0.0858 226 PHE B CB  
8802  C CG  . PHE B 217 ? 0.8709  0.8891  0.6445  -0.0768 -0.0690 -0.0745 226 PHE B CG  
8803  C CD1 . PHE B 217 ? 0.7757  0.8584  0.5916  -0.0619 -0.0598 -0.0613 226 PHE B CD1 
8804  C CD2 . PHE B 217 ? 0.9863  1.0045  0.7394  -0.1037 -0.0834 -0.0791 226 PHE B CD2 
8805  C CE1 . PHE B 217 ? 0.8479  0.9892  0.6856  -0.0734 -0.0633 -0.0527 226 PHE B CE1 
8806  C CE2 . PHE B 217 ? 0.9861  1.0663  0.7614  -0.1134 -0.0879 -0.0683 226 PHE B CE2 
8807  C CZ  . PHE B 217 ? 0.9337  1.0719  0.7507  -0.0984 -0.0773 -0.0552 226 PHE B CZ  
8817  N N   . PHE B 218 ? 0.8758  0.7395  0.5186  -0.0667 -0.0623 -0.1436 227 PHE B N   
8818  C CA  . PHE B 218 ? 1.3979  1.2603  1.0015  -0.0813 -0.0682 -0.1572 227 PHE B CA  
8819  C C   . PHE B 218 ? 1.5109  1.3662  1.0819  -0.0552 -0.0430 -0.1792 227 PHE B C   
8820  O O   . PHE B 218 ? 1.3219  1.2025  0.8724  -0.0590 -0.0377 -0.1816 227 PHE B O   
8821  C CB  . PHE B 218 ? 1.2572  1.0592  0.8222  -0.1076 -0.0933 -0.1700 227 PHE B CB  
8822  C CG  . PHE B 218 ? 1.0020  0.8028  0.5222  -0.1202 -0.1029 -0.1848 227 PHE B CG  
8823  C CD1 . PHE B 218 ? 0.9579  0.8103  0.4945  -0.1416 -0.1194 -0.1686 227 PHE B CD1 
8824  C CD2 . PHE B 218 ? 1.0741  0.8273  0.5344  -0.1063 -0.0941 -0.2142 227 PHE B CD2 
8825  C CE1 . PHE B 218 ? 0.9915  0.8434  0.4811  -0.1500 -0.1307 -0.1807 227 PHE B CE1 
8826  C CE2 . PHE B 218 ? 1.1093  0.8620  0.5180  -0.1158 -0.1034 -0.2272 227 PHE B CE2 
8827  C CZ  . PHE B 218 ? 1.1297  0.9310  0.5527  -0.1372 -0.1227 -0.2093 227 PHE B CZ  
8837  N N   . SER B 219 ? 1.4760  1.2926  1.0372  -0.0288 -0.0274 -0.1960 228 SER B N   
8838  C CA  . SER B 219 ? 1.4039  1.2062  0.9281  -0.0048 -0.0024 -0.2215 228 SER B CA  
8839  C C   . SER B 219 ? 1.3860  1.2496  0.9504  0.0199  0.0277  -0.2162 228 SER B C   
8840  O O   . SER B 219 ? 1.0967  0.9710  0.6370  0.0319  0.0519  -0.2303 228 SER B O   
8841  C CB  . SER B 219 ? 1.2964  1.0272  0.7925  0.0149  0.0003  -0.2455 228 SER B CB  
8842  O OG  . SER B 219 ? 1.5266  1.1938  0.9839  -0.0102 -0.0275 -0.2544 228 SER B OG  
8848  N N   . VAL B 220 ? 1.0593  0.9647  0.6837  0.0256  0.0264  -0.1961 229 VAL B N   
8849  C CA  . VAL B 220 ? 1.2334  1.1936  0.9044  0.0507  0.0511  -0.1948 229 VAL B CA  
8850  C C   . VAL B 220 ? 1.1701  1.1961  0.8862  0.0355  0.0460  -0.1705 229 VAL B C   
8851  O O   . VAL B 220 ? 1.4663  1.5274  1.1834  0.0287  0.0587  -0.1681 229 VAL B O   
8852  C CB  . VAL B 220 ? 1.4755  1.4203  1.1746  0.0788  0.0516  -0.1975 229 VAL B CB  
8853  C CG1 . VAL B 220 ? 0.9531  0.9589  0.7059  0.1075  0.0745  -0.2001 229 VAL B CG1 
8854  C CG2 . VAL B 220 ? 0.9345  0.8029  0.5854  0.0924  0.0522  -0.2214 229 VAL B CG2 
8864  N N   . LEU B 221 ? 0.8334  0.8708  0.5816  0.0291  0.0267  -0.1517 230 LEU B N   
8865  C CA  . LEU B 221 ? 0.8301  0.9334  0.6283  0.0242  0.0247  -0.1327 230 LEU B CA  
8866  C C   . LEU B 221 ? 1.0587  1.1854  0.8488  -0.0018 0.0169  -0.1219 230 LEU B C   
8867  O O   . LEU B 221 ? 1.0243  1.2032  0.8494  -0.0014 0.0240  -0.1135 230 LEU B O   
8868  C CB  . LEU B 221 ? 0.8570  0.9634  0.6820  0.0244  0.0068  -0.1152 230 LEU B CB  
8869  C CG  . LEU B 221 ? 0.9586  1.1325  0.8339  0.0252  0.0051  -0.0994 230 LEU B CG  
8870  C CD1 . LEU B 221 ? 0.7649  0.9836  0.6759  0.0487  0.0263  -0.1112 230 LEU B CD1 
8871  C CD2 . LEU B 221 ? 1.0876  1.2563  0.9778  0.0295  -0.0101 -0.0826 230 LEU B CD2 
8883  N N   . ARG B 222 ? 0.7975  0.8870  0.5448  -0.0238 -0.0001 -0.1222 231 ARG B N   
8884  C CA  . ARG B 222 ? 0.9552  1.0667  0.6922  -0.0441 -0.0092 -0.1128 231 ARG B CA  
8885  C C   . ARG B 222 ? 0.6389  0.7608  0.3574  -0.0360 0.0141  -0.1210 231 ARG B C   
8886  O O   . ARG B 222 ? 0.7860  0.9463  0.5234  -0.0411 0.0172  -0.1089 231 ARG B O   
8887  C CB  . ARG B 222 ? 1.0694  1.1386  0.7627  -0.0672 -0.0337 -0.1159 231 ARG B CB  
8888  C CG  . ARG B 222 ? 1.0300  1.1217  0.7133  -0.0876 -0.0510 -0.1054 231 ARG B CG  
8889  C CD  . ARG B 222 ? 1.8432  1.8910  1.4829  -0.1087 -0.0762 -0.1147 231 ARG B CD  
8890  N NE  . ARG B 222 ? 2.1037  2.0996  1.6821  -0.1005 -0.0666 -0.1388 231 ARG B NE  
8891  C CZ  . ARG B 222 ? 1.5854  1.5641  1.1094  -0.1076 -0.0746 -0.1481 231 ARG B CZ  
8892  N NH1 . ARG B 222 ? 1.8710  1.8786  1.3952  -0.1236 -0.0960 -0.1348 231 ARG B NH1 
8893  N NH2 . ARG B 222 ? 1.3690  1.3007  0.8361  -0.0965 -0.0623 -0.1716 231 ARG B NH2 
8907  N N   . ILE B 223 ? 0.8739  0.9631  0.5601  -0.0209 0.0338  -0.1412 232 ILE B N   
8908  C CA  . ILE B 223 ? 0.8932  0.9876  0.5541  -0.0138 0.0609  -0.1493 232 ILE B CA  
8909  C C   . ILE B 223 ? 1.1139  1.2660  0.8315  -0.0068 0.0810  -0.1392 232 ILE B C   
8910  O O   . ILE B 223 ? 0.9131  1.0813  0.6219  -0.0142 0.0929  -0.1313 232 ILE B O   
8911  C CB  . ILE B 223 ? 0.9488  1.0054  0.5755  0.0060  0.0820  -0.1746 232 ILE B CB  
8912  C CG1 . ILE B 223 ? 1.2891  1.2799  0.8630  0.0014  0.0613  -0.1900 232 ILE B CG1 
8913  C CG2 . ILE B 223 ? 1.2074  1.2662  0.7964  0.0088  0.1097  -0.1809 232 ILE B CG2 
8914  C CD1 . ILE B 223 ? 1.3293  1.2890  0.8385  -0.0202 0.0424  -0.1920 232 ILE B CD1 
8926  N N   . TYR B 224 ? 0.6193  0.8010  0.3942  0.0077  0.0838  -0.1395 233 TYR B N   
8927  C CA  . TYR B 224 ? 0.6056  0.8433  0.4395  0.0149  0.1008  -0.1351 233 TYR B CA  
8928  C C   . TYR B 224 ? 1.0429  1.3132  0.9089  0.0009  0.0819  -0.1161 233 TYR B C   
8929  O O   . TYR B 224 ? 0.8348  1.1503  0.7529  0.0052  0.0900  -0.1133 233 TYR B O   
8930  C CB  . TYR B 224 ? 1.2588  1.5183  1.1398  0.0395  0.1091  -0.1463 233 TYR B CB  
8931  C CG  . TYR B 224 ? 1.2151  1.4517  1.0747  0.0591  0.1326  -0.1677 233 TYR B CG  
8932  C CD1 . TYR B 224 ? 0.6102  0.8716  0.4797  0.0645  0.1655  -0.1772 233 TYR B CD1 
8933  C CD2 . TYR B 224 ? 1.5337  1.7214  1.3613  0.0708  0.1229  -0.1783 233 TYR B CD2 
8934  C CE1 . TYR B 224 ? 1.9465  2.1920  1.7968  0.0837  0.1895  -0.1977 233 TYR B CE1 
8935  C CE2 . TYR B 224 ? 1.5427  1.7084  1.3491  0.0912  0.1446  -0.2000 233 TYR B CE2 
8936  C CZ  . TYR B 224 ? 1.3257  1.5233  1.1441  0.0987  0.1780  -0.2100 233 TYR B CZ  
8937  O OH  . TYR B 224 ? 0.7665  0.9425  0.5615  0.1210  0.2002  -0.2330 233 TYR B OH  
8947  N N   . LEU B 225 ? 0.9802  1.2310  0.8215  -0.0144 0.0556  -0.1053 234 LEU B N   
8948  C CA  . LEU B 225 ? 0.7081  0.9903  0.5746  -0.0266 0.0397  -0.0883 234 LEU B CA  
8949  C C   . LEU B 225 ? 0.7264  0.9929  0.5519  -0.0419 0.0351  -0.0805 234 LEU B C   
8950  O O   . LEU B 225 ? 0.8713  1.1595  0.7121  -0.0508 0.0202  -0.0664 234 LEU B O   
8951  C CB  . LEU B 225 ? 0.4344  0.7201  0.3151  -0.0314 0.0144  -0.0795 234 LEU B CB  
8952  C CG  . LEU B 225 ? 0.5086  0.8039  0.4213  -0.0154 0.0140  -0.0824 234 LEU B CG  
8953  C CD1 . LEU B 225 ? 0.7275  1.0252  0.6470  -0.0257 -0.0100 -0.0676 234 LEU B CD1 
8954  C CD2 . LEU B 225 ? 0.6160  0.9589  0.5799  -0.0002 0.0269  -0.0855 234 LEU B CD2 
8966  N N   . SER B 226 ? 0.5402  0.7700  0.3117  -0.0424 0.0476  -0.0895 235 SER B N   
8967  C CA  . SER B 226 ? 0.7939  1.0093  0.5212  -0.0536 0.0444  -0.0805 235 SER B CA  
8968  C C   . SER B 226 ? 0.9003  1.1408  0.6507  -0.0523 0.0662  -0.0708 235 SER B C   
8969  O O   . SER B 226 ? 1.0417  1.3033  0.8293  -0.0434 0.0914  -0.0776 235 SER B O   
8970  C CB  . SER B 226 ? 0.9992  1.1678  0.6563  -0.0531 0.0514  -0.0938 235 SER B CB  
8971  O OG  . SER B 226 ? 1.2230  1.3662  0.8668  -0.0565 0.0290  -0.1035 235 SER B OG  
8977  N N   . GLY B 227 ? 1.2085  1.4485  0.9429  -0.0615 0.0537  -0.0545 236 GLY B N   
8978  C CA  . GLY B 227 ? 0.6506  0.9010  0.3969  -0.0628 0.0729  -0.0426 236 GLY B CA  
8979  C C   . GLY B 227 ? 0.9342  1.1486  0.6100  -0.0675 0.0805  -0.0328 236 GLY B C   
8980  O O   . GLY B 227 ? 0.9941  1.1769  0.6095  -0.0676 0.0755  -0.0408 236 GLY B O   
8984  N N   . TRP B 228 ? 1.3773  1.5923  1.0557  -0.0712 0.0899  -0.0152 237 TRP B N   
8985  C CA  . TRP B 228 ? 1.4009  1.5797  1.0098  -0.0741 0.1045  -0.0021 237 TRP B CA  
8986  C C   . TRP B 228 ? 1.5933  1.7645  1.1914  -0.0765 0.0810  0.0211  237 TRP B C   
8987  O O   . TRP B 228 ? 1.7877  1.9437  1.3740  -0.0789 0.0982  0.0393  237 TRP B O   
8988  C CB  . TRP B 228 ? 1.1298  1.3092  0.7471  -0.0754 0.1521  -0.0020 237 TRP B CB  
8989  C CG  . TRP B 228 ? 0.8899  1.1104  0.5976  -0.0768 0.1654  -0.0064 237 TRP B CG  
8990  C CD1 . TRP B 228 ? 1.2256  1.4551  0.9730  -0.0834 0.1681  0.0084  237 TRP B CD1 
8991  C CD2 . TRP B 228 ? 0.8374  1.0940  0.6062  -0.0702 0.1738  -0.0282 237 TRP B CD2 
8992  N NE1 . TRP B 228 ? 0.6741  0.9444  0.5020  -0.0829 0.1761  -0.0048 237 TRP B NE1 
8993  C CE2 . TRP B 228 ? 0.8117  1.1016  0.6543  -0.0740 0.1792  -0.0263 237 TRP B CE2 
8994  C CE3 . TRP B 228 ? 0.6745  0.9355  0.4411  -0.0597 0.1757  -0.0496 237 TRP B CE3 
8995  C CZ2 . TRP B 228 ? 0.6732  1.0060  0.5867  -0.0674 0.1844  -0.0451 237 TRP B CZ2 
8996  C CZ3 . TRP B 228 ? 0.6220  0.9220  0.4581  -0.0516 0.1818  -0.0652 237 TRP B CZ3 
8997  C CH2 . TRP B 228 ? 0.5701  0.9082  0.4785  -0.0553 0.1850  -0.0627 237 TRP B CH2 
9008  N N   . LYS B 229 ? 1.2715  1.4531  0.8749  -0.0756 0.0412  0.0212  238 LYS B N   
9009  C CA  . LYS B 229 ? 1.0379  1.2153  0.6277  -0.0739 0.0127  0.0405  238 LYS B CA  
9010  C C   . LYS B 229 ? 0.8901  1.0522  0.4223  -0.0749 -0.0184 0.0363  238 LYS B C   
9011  O O   . LYS B 229 ? 1.0756  1.2553  0.6279  -0.0787 -0.0386 0.0213  238 LYS B O   
9012  C CB  . LYS B 229 ? 0.8660  1.0835  0.5315  -0.0711 -0.0066 0.0421  238 LYS B CB  
9013  C CG  . LYS B 229 ? 0.8019  1.0183  0.4629  -0.0648 -0.0329 0.0614  238 LYS B CG  
9020  N N   . GLY B 230 ? 0.9981  1.1257  0.4566  -0.0724 -0.0220 0.0491  239 GLY B N   
9021  C CA  . GLY B 230 ? 1.2772  1.3914  0.6794  -0.0740 -0.0534 0.0406  239 GLY B CA  
9022  C C   . GLY B 230 ? 1.3771  1.4765  0.7536  -0.0787 -0.0412 0.0154  239 GLY B C   
9023  O O   . GLY B 230 ? 1.6747  1.7682  1.0475  -0.0800 -0.0687 0.0001  239 GLY B O   
9027  N N   . ASN B 231 ? 1.5324  1.6239  0.9129  -0.0769 -0.0009 0.0092  240 ASN B N   
9028  C CA  . ASN B 231 ? 1.3234  1.3984  0.6786  -0.0769 0.0130  -0.0160 240 ASN B CA  
9029  C C   . ASN B 231 ? 1.4113  1.4449  0.6842  -0.0691 0.0359  -0.0165 240 ASN B C   
9030  O O   . ASN B 231 ? 1.7376  1.7658  0.9974  -0.0670 0.0692  -0.0001 240 ASN B O   
9031  C CB  . ASN B 231 ? 1.1786  1.2779  0.6033  -0.0746 0.0425  -0.0270 240 ASN B CB  
9032  C CG  . ASN B 231 ? 1.0272  1.1109  0.4362  -0.0713 0.0501  -0.0537 240 ASN B CG  
9033  O OD1 . ASN B 231 ? 1.0602  1.1077  0.3943  -0.0695 0.0489  -0.0654 240 ASN B OD1 
9034  N ND2 . ASN B 231 ? 1.0172  1.1248  0.4925  -0.0684 0.0571  -0.0645 240 ASN B ND2 
9041  N N   . PRO B 232 ? 1.3665  1.3717  0.5912  -0.0627 0.0188  -0.0344 241 PRO B N   
9042  C CA  . PRO B 232 ? 1.8215  1.7964  0.9755  -0.0494 0.0398  -0.0371 241 PRO B CA  
9043  C C   . PRO B 232 ? 1.8179  1.7939  0.9753  -0.0446 0.0924  -0.0431 241 PRO B C   
9044  O O   . PRO B 232 ? 1.6173  1.5841  0.7344  -0.0367 0.1193  -0.0318 241 PRO B O   
9045  C CB  . PRO B 232 ? 1.9340  1.8911  1.0551  -0.0463 0.0096  -0.0636 241 PRO B CB  
9046  C CG  . PRO B 232 ? 1.6649  1.6373  0.8285  -0.0575 -0.0342 -0.0636 241 PRO B CG  
9047  C CD  . PRO B 232 ? 1.2538  1.2587  0.4883  -0.0678 -0.0239 -0.0507 241 PRO B CD  
9055  N N   . GLN B 233 ? 2.1354  2.1282  1.3433  -0.0482 0.1078  -0.0608 242 GLN B N   
9056  C CA  . GLN B 233 ? 1.6771  1.6771  0.8973  -0.0395 0.1564  -0.0702 242 GLN B CA  
9057  C C   . GLN B 233 ? 1.9119  1.9375  1.1737  -0.0453 0.1909  -0.0472 242 GLN B C   
9058  O O   . GLN B 233 ? 1.7423  1.7784  1.0169  -0.0382 0.2328  -0.0502 242 GLN B O   
9059  C CB  . GLN B 233 ? 1.8366  1.8501  1.1036  -0.0380 0.1606  -0.0969 242 GLN B CB  
9060  C CG  . GLN B 233 ? 2.2163  2.2029  1.4560  -0.0379 0.1247  -0.1194 242 GLN B CG  
9061  C CD  . GLN B 233 ? 2.4660  2.4627  1.7554  -0.0345 0.1297  -0.1419 242 GLN B CD  
9062  O OE1 . GLN B 233 ? 2.5567  2.5478  1.8424  -0.0196 0.1609  -0.1612 242 GLN B OE1 
9063  N NE2 . GLN B 233 ? 2.5301  2.5439  1.8770  -0.0431 0.0975  -0.1363 242 GLN B NE2 
9072  N N   . LEU B 234 ? 1.7331  1.7718  1.0206  -0.0580 0.1738  -0.0253 243 LEU B N   
9073  C CA  . LEU B 234 ? 1.4802  1.5358  0.8024  -0.0661 0.2037  -0.0026 243 LEU B CA  
9074  C C   . LEU B 234 ? 1.5400  1.5765  0.8284  -0.0715 0.1788  0.0266  243 LEU B C   
9075  O O   . LEU B 234 ? 2.2248  2.2797  1.5712  -0.0762 0.1650  0.0411  243 LEU B O   
9076  C CB  . LEU B 234 ? 1.2446  1.3463  0.6733  -0.0691 0.2086  -0.0103 243 LEU B CB  
9077  C CG  . LEU B 234 ? 1.2942  1.4180  0.7581  -0.0615 0.2412  -0.0353 243 LEU B CG  
9078  C CD1 . LEU B 234 ? 1.1176  1.2862  0.6820  -0.0607 0.2347  -0.0439 243 LEU B CD1 
9079  C CD2 . LEU B 234 ? 1.3468  1.4703  0.8025  -0.0610 0.2905  -0.0273 243 LEU B CD2 
9091  N N   . SER B 235 ? 1.5982  1.5991  0.8102  -0.0608 0.1695  0.0353  244 SER B N   
9092  C CA  . SER B 235 ? 1.7151  1.6970  0.8894  -0.0590 0.1348  0.0586  244 SER B CA  
9093  C C   . SER B 235 ? 1.8689  1.8544  1.0746  -0.0700 0.1443  0.0875  244 SER B C   
9094  O O   . SER B 235 ? 2.1300  2.1249  1.3611  -0.0708 0.1079  0.0970  244 SER B O   
9095  C CB  . SER B 235 ? 1.8013  1.7570  0.8968  -0.0461 0.1364  0.0669  244 SER B CB  
9096  O OG  . SER B 235 ? 2.3635  2.3187  1.4508  -0.0472 0.1867  0.0739  244 SER B OG  
9102  N N   . ASP B 236 ? 1.7495  1.7329  0.9706  -0.0767 0.1917  0.0997  245 ASP B N   
9103  C CA  . ASP B 236 ? 1.6536  1.6324  0.9102  -0.0856 0.2005  0.1272  245 ASP B CA  
9104  C C   . ASP B 236 ? 1.6318  1.6544  1.0015  -0.0927 0.2088  0.1138  245 ASP B C   
9105  O O   . ASP B 236 ? 1.4616  1.4831  0.8763  -0.1001 0.2190  0.1308  245 ASP B O   
9106  C CB  . ASP B 236 ? 1.5898  1.5388  0.8067  -0.0899 0.2438  0.1528  245 ASP B CB  
9107  C CG  . ASP B 236 ? 1.6225  1.5414  0.7541  -0.0752 0.2270  0.1680  245 ASP B CG  
9108  O OD1 . ASP B 236 ? 1.6248  1.5222  0.7291  -0.0692 0.1905  0.1870  245 ASP B OD1 
9109  O OD2 . ASP B 236 ? 1.6824  1.6027  0.7776  -0.0701 0.2491  0.1618  245 ASP B OD2 
9114  N N   . GLY B 237 ? 1.6253  1.6828  1.0384  -0.0900 0.2041  0.0835  246 GLY B N   
9115  C CA  . GLY B 237 ? 1.3656  1.4671  0.8798  -0.0938 0.2098  0.0686  246 GLY B CA  
9116  C C   . GLY B 237 ? 1.4096  1.5305  0.9545  -0.0995 0.2586  0.0567  246 GLY B C   
9117  O O   . GLY B 237 ? 1.4610  1.5664  0.9506  -0.0983 0.2888  0.0543  246 GLY B O   
9121  N N   . LEU B 238 ? 1.2291  1.3884  0.8655  -0.1046 0.2660  0.0477  247 LEU B N   
9122  C CA  . LEU B 238 ? 1.1809  1.3716  0.8668  -0.1098 0.3082  0.0339  247 LEU B CA  
9123  C C   . LEU B 238 ? 1.6114  1.7985  1.3319  -0.1276 0.3353  0.0538  247 LEU B C   
9124  O O   . LEU B 238 ? 1.9112  2.0985  1.6739  -0.1324 0.3139  0.0620  247 LEU B O   
9125  C CB  . LEU B 238 ? 1.3180  1.5579  1.0850  -0.1019 0.2928  0.0066  247 LEU B CB  
9126  C CG  . LEU B 238 ? 1.2419  1.5231  1.0621  -0.0997 0.3266  -0.0152 247 LEU B CG  
9127  C CD1 . LEU B 238 ? 0.9090  1.1745  0.6673  -0.0866 0.3396  -0.0274 247 LEU B CD1 
9128  C CD2 . LEU B 238 ? 1.8522  2.1770  1.7526  -0.0919 0.3013  -0.0345 247 LEU B CD2 
9140  N N   . VAL B 239 ? 2.0360  2.2187  1.7395  -0.1377 0.3834  0.0609  248 VAL B N   
9141  C CA  . VAL B 239 ? 1.8216  2.0062  1.5753  -0.1579 0.4120  0.0771  248 VAL B CA  
9142  C C   . VAL B 239 ? 1.4615  1.7077  1.3278  -0.1591 0.4161  0.0506  248 VAL B C   
9143  O O   . VAL B 239 ? 1.0175  1.2976  0.9094  -0.1449 0.4246  0.0310  248 VAL B O   
9144  C CB  . VAL B 239 ? 1.7973  1.9572  1.5053  -0.1613 0.4457  0.1000  248 VAL B CB  
9145  C CG1 . VAL B 239 ? 1.7527  1.9201  1.4117  -0.1414 0.4527  0.0869  248 VAL B CG1 
9146  C CG2 . VAL B 239 ? 1.6380  1.8266  1.4294  -0.1803 0.4766  0.1036  248 VAL B CG2 
9156  N N   . TYR B 240 ? 1.0290  1.2874  0.9612  -0.1739 0.4075  0.0502  249 TYR B N   
9157  C CA  . TYR B 240 ? 1.0308  1.3453  1.0704  -0.1744 0.4041  0.0261  249 TYR B CA  
9158  C C   . TYR B 240 ? 1.3505  1.6682  1.4279  -0.1923 0.4366  0.0380  249 TYR B C   
9159  O O   . TYR B 240 ? 1.2757  1.5746  1.3806  -0.2141 0.4431  0.0517  249 TYR B O   
9160  C CB  . TYR B 240 ? 0.9964  1.3215  1.0848  -0.1760 0.3689  0.0173  249 TYR B CB  
9161  C CG  . TYR B 240 ? 0.9826  1.3088  1.0391  -0.1510 0.3237  0.0075  249 TYR B CG  
9162  C CD1 . TYR B 240 ? 1.0124  1.2910  0.9871  -0.1426 0.3012  0.0272  249 TYR B CD1 
9163  C CD2 . TYR B 240 ? 0.6253  1.0014  0.7347  -0.1365 0.3037  -0.0205 249 TYR B CD2 
9164  C CE1 . TYR B 240 ? 0.8526  1.1368  0.8071  -0.1245 0.2628  0.0180  249 TYR B CE1 
9165  C CE2 . TYR B 240 ? 1.6906  2.0656  1.7727  -0.1178 0.2680  -0.0264 249 TYR B CE2 
9166  C CZ  . TYR B 240 ? 1.1554  1.4863  1.1640  -0.1137 0.2486  -0.0078 249 TYR B CZ  
9167  O OH  . TYR B 240 ? 0.8089  1.1440  0.7997  -0.0987 0.2138  -0.0147 249 TYR B OH  
9177  N N   . GLU B 241 ? 1.2138  1.5554  1.2919  -0.1834 0.4577  0.0322  250 GLU B N   
9178  C CA  . GLU B 241 ? 1.3509  1.6966  1.4463  -0.2008 0.4929  0.0468  250 GLU B CA  
9179  C C   . GLU B 241 ? 1.7439  2.1055  1.9250  -0.2246 0.4928  0.0451  250 GLU B C   
9180  O O   . GLU B 241 ? 1.3884  1.7937  1.6458  -0.2194 0.4714  0.0194  250 GLU B O   
9181  C CB  . GLU B 241 ? 1.8022  2.1927  1.9149  -0.1845 0.5096  0.0306  250 GLU B CB  
9182  C CG  . GLU B 241 ? 1.8255  2.2276  1.9494  -0.2015 0.5496  0.0457  250 GLU B CG  
9183  C CD  . GLU B 241 ? 1.4251  1.8786  1.5732  -0.1834 0.5665  0.0276  250 GLU B CD  
9184  O OE1 . GLU B 241 ? 1.2500  1.7549  1.4824  -0.1797 0.5586  0.0065  250 GLU B OE1 
9185  O OE2 . GLU B 241 ? 2.3404  2.7821  2.4203  -0.1708 0.5861  0.0339  250 GLU B OE2 
9192  N N   . GLY B 242 ? 1.1726  1.4936  1.3357  -0.2500 0.5149  0.0732  251 GLY B N   
9193  C CA  . GLY B 242 ? 1.3662  1.6934  1.6047  -0.2766 0.5201  0.0737  251 GLY B CA  
9194  C C   . GLY B 242 ? 1.3815  1.6837  1.6469  -0.2846 0.4926  0.0701  251 GLY B C   
9195  O O   . GLY B 242 ? 2.1483  2.4337  2.4598  -0.3098 0.4981  0.0761  251 GLY B O   
9199  N N   . PHE B 243 ? 1.2905  1.5873  1.5273  -0.2651 0.4642  0.0607  252 PHE B N   
9200  C CA  . PHE B 243 ? 1.6905  1.9649  1.9471  -0.2702 0.4392  0.0577  252 PHE B CA  
9201  C C   . PHE B 243 ? 1.7308  1.9287  1.8986  -0.2718 0.4400  0.0924  252 PHE B C   
9202  O O   . PHE B 243 ? 1.2475  1.4023  1.4242  -0.2787 0.4233  0.1046  252 PHE B O   
9203  C CB  . PHE B 243 ? 1.0374  1.3606  1.3233  -0.2458 0.4026  0.0254  252 PHE B CB  
9204  C CG  . PHE B 243 ? 0.8463  1.1711  1.1818  -0.2469 0.3705  0.0112  252 PHE B CG  
9205  C CD1 . PHE B 243 ? 0.6494  1.0164  1.0735  -0.2515 0.3566  -0.0161 252 PHE B CD1 
9206  C CD2 . PHE B 243 ? 1.0747  1.3518  1.3534  -0.2299 0.3351  0.0266  252 PHE B CD2 
9207  C CE1 . PHE B 243 ? 0.9243  1.2930  1.3923  -0.2508 0.3260  -0.0327 252 PHE B CE1 
9208  C CE2 . PHE B 243 ? 0.7977  1.0741  1.1155  -0.2226 0.2984  0.0131  252 PHE B CE2 
9209  C CZ  . PHE B 243 ? 0.8129  1.1326  1.2216  -0.2328 0.2945  -0.0166 252 PHE B CZ  
9219  N N   . TRP B 244 ? 1.7104  1.8890  1.7880  -0.2535 0.4390  0.1060  253 TRP B N   
9220  C CA  . TRP B 244 ? 1.8211  1.9258  1.8032  -0.2475 0.4302  0.1425  253 TRP B CA  
9221  C C   . TRP B 244 ? 2.1647  2.2459  2.0707  -0.2547 0.4743  0.1662  253 TRP B C   
9222  O O   . TRP B 244 ? 2.5390  2.6618  2.4375  -0.2416 0.4807  0.1489  253 TRP B O   
9223  C CB  . TRP B 244 ? 2.0325  2.1309  1.9660  -0.2168 0.3794  0.1377  253 TRP B CB  
9224  C CG  . TRP B 244 ? 1.8099  1.9206  1.8026  -0.2089 0.3391  0.1219  253 TRP B CG  
9225  C CD1 . TRP B 244 ? 1.6323  1.7064  1.6518  -0.2176 0.3301  0.1332  253 TRP B CD1 
9226  C CD2 . TRP B 244 ? 1.4074  1.5691  1.4391  -0.1896 0.3029  0.0909  253 TRP B CD2 
9227  N NE1 . TRP B 244 ? 1.5013  1.6041  1.5740  -0.2034 0.2905  0.1085  253 TRP B NE1 
9228  C CE2 . TRP B 244 ? 1.4268  1.5846  1.5064  -0.1867 0.2741  0.0840  253 TRP B CE2 
9229  C CE3 . TRP B 244 ? 1.1524  1.3590  1.1807  -0.1742 0.2929  0.0691  253 TRP B CE3 
9230  C CZ2 . TRP B 244 ? 1.3280  1.5298  1.4493  -0.1690 0.2380  0.0572  253 TRP B CZ2 
9231  C CZ3 . TRP B 244 ? 0.7768  1.0226  0.8476  -0.1581 0.2562  0.0451  253 TRP B CZ3 
9232  C CH2 . TRP B 244 ? 1.3190  1.5646  1.4348  -0.1559 0.2306  0.0398  253 TRP B CH2 
9243  N N   . GLU B 245 ? 1.6509  1.6663  1.5022  -0.2661 0.4895  0.2048  254 GLU B N   
9244  C CA  . GLU B 245 ? 1.4940  1.4879  1.2612  -0.2595 0.5077  0.2275  254 GLU B CA  
9245  C C   . GLU B 245 ? 1.1884  1.1679  0.8638  -0.2322 0.4817  0.2270  254 GLU B C   
9246  O O   . GLU B 245 ? 2.0341  2.0280  1.6594  -0.2190 0.4892  0.2231  254 GLU B O   
9247  C CB  . GLU B 245 ? 2.2025  2.1268  1.9275  -0.2750 0.5231  0.2709  254 GLU B CB  
9250  N N   . ASP B 246 ? 1.7099  1.6720  1.3764  -0.2204 0.4435  0.2255  255 ASP B N   
9251  C CA  . ASP B 246 ? 1.9247  1.8696  1.5179  -0.1930 0.3984  0.2268  255 ASP B CA  
9252  C C   . ASP B 246 ? 1.7304  1.7357  1.3556  -0.1776 0.3753  0.1869  255 ASP B C   
9253  O O   . ASP B 246 ? 1.9497  2.0034  1.6671  -0.1803 0.3673  0.1598  255 ASP B O   
9254  C CB  . ASP B 246 ? 1.9803  1.8940  1.5846  -0.1830 0.3534  0.2390  255 ASP B CB  
9255  C CG  . ASP B 246 ? 1.8264  1.6877  1.4465  -0.2020 0.3742  0.2693  255 ASP B CG  
9256  O OD1 . ASP B 246 ? 2.4577  2.2579  1.9959  -0.2046 0.3915  0.3075  255 ASP B OD1 
9257  O OD2 . ASP B 246 ? 1.4321  1.3103  1.1449  -0.2143 0.3724  0.2548  255 ASP B OD2 
9262  N N   . PRO B 247 ? 1.4807  1.4822  1.0316  -0.1606 0.3612  0.1817  256 PRO B N   
9263  C CA  . PRO B 247 ? 1.0723  1.1204  0.6533  -0.1462 0.3330  0.1468  256 PRO B CA  
9264  C C   . PRO B 247 ? 1.1195  1.1701  0.7211  -0.1333 0.2783  0.1437  256 PRO B C   
9265  O O   . PRO B 247 ? 1.5523  1.5637  1.1000  -0.1254 0.2526  0.1662  256 PRO B O   
9266  C CB  . PRO B 247 ? 1.0624  1.0949  0.5498  -0.1354 0.3392  0.1440  256 PRO B CB  
9267  C CG  . PRO B 247 ? 1.4596  1.4340  0.8560  -0.1369 0.3481  0.1798  256 PRO B CG  
9268  C CD  . PRO B 247 ? 1.1864  1.1422  0.6226  -0.1557 0.3755  0.2049  256 PRO B CD  
9276  N N   . LYS B 248 ? 0.9937  1.0930  0.6730  -0.1295 0.2604  0.1160  257 LYS B N   
9277  C CA  . LYS B 248 ? 0.9219  1.0323  0.6326  -0.1185 0.2142  0.1117  257 LYS B CA  
9278  C C   . LYS B 248 ? 1.1414  1.2812  0.8466  -0.1054 0.1850  0.0896  257 LYS B C   
9279  O O   . LYS B 248 ? 1.7823  1.9514  1.5091  -0.1053 0.1993  0.0675  257 LYS B O   
9280  C CB  . LYS B 248 ? 1.0296  1.1684  0.8355  -0.1255 0.2154  0.1006  257 LYS B CB  
9281  C CG  . LYS B 248 ? 1.5100  1.6156  1.3307  -0.1424 0.2431  0.1212  257 LYS B CG  
9282  C CD  . LYS B 248 ? 1.2144  1.2601  0.9730  -0.1372 0.2281  0.1542  257 LYS B CD  
9291  N N   . GLU B 249 ? 1.2710  1.4016  0.9481  -0.0944 0.1439  0.0965  258 GLU B N   
9292  C CA  . GLU B 249 ? 1.1071  1.2595  0.7749  -0.0853 0.1127  0.0798  258 GLU B CA  
9293  C C   . GLU B 249 ? 1.0617  1.2585  0.8059  -0.0804 0.0884  0.0644  258 GLU B C   
9294  O O   . GLU B 249 ? 0.9815  1.1827  0.7554  -0.0760 0.0699  0.0727  258 GLU B O   
9295  C CB  . GLU B 249 ? 1.3005  1.4234  0.8954  -0.0779 0.0820  0.0957  258 GLU B CB  
9296  C CG  . GLU B 249 ? 1.4467  1.5288  0.9519  -0.0795 0.1002  0.1060  258 GLU B CG  
9297  C CD  . GLU B 249 ? 1.8077  1.8653  1.2407  -0.0707 0.0642  0.1182  258 GLU B CD  
9298  O OE1 . GLU B 249 ? 2.2053  2.2778  1.6263  -0.0678 0.0358  0.1017  258 GLU B OE1 
9299  O OE2 . GLU B 249 ? 1.7802  1.8023  1.1684  -0.0668 0.0639  0.1450  258 GLU B OE2 
9306  N N   . PHE B 250 ? 1.3965  1.4586  1.3300  0.0440  0.1875  0.0934  259 PHE B N   
9307  C CA  . PHE B 250 ? 1.2671  1.3276  1.2171  0.0364  0.1736  0.0757  259 PHE B CA  
9308  C C   . PHE B 250 ? 1.1547  1.2213  1.0889  0.0513  0.1654  0.0609  259 PHE B C   
9309  O O   . PHE B 250 ? 1.6914  1.7741  1.6136  0.0630  0.1725  0.0628  259 PHE B O   
9310  C CB  . PHE B 250 ? 1.2080  1.2916  1.1934  0.0192  0.1763  0.0751  259 PHE B CB  
9311  C CG  . PHE B 250 ? 1.0940  1.1677  1.0992  -0.0002 0.1816  0.0858  259 PHE B CG  
9312  C CD1 . PHE B 250 ? 1.2242  1.2678  1.2322  -0.0095 0.1724  0.0798  259 PHE B CD1 
9313  C CD2 . PHE B 250 ? 1.0852  1.1795  1.1073  -0.0096 0.1964  0.1018  259 PHE B CD2 
9314  C CE1 . PHE B 250 ? 1.0918  1.1209  1.1160  -0.0277 0.1777  0.0888  259 PHE B CE1 
9315  C CE2 . PHE B 250 ? 1.7225  1.8051  1.7636  -0.0296 0.2017  0.1117  259 PHE B CE2 
9316  C CZ  . PHE B 250 ? 1.5561  1.6040  1.5975  -0.0389 0.1921  0.1046  259 PHE B CZ  
9326  N N   . ALA B 251 ? 1.2538  1.3063  1.1880  0.0507  0.1514  0.0465  260 ALA B N   
9327  C CA  . ALA B 251 ? 0.9934  1.0450  0.9115  0.0633  0.1431  0.0329  260 ALA B CA  
9328  C C   . ALA B 251 ? 0.9945  1.0679  0.9254  0.0643  0.1434  0.0244  260 ALA B C   
9329  O O   . ALA B 251 ? 1.0643  1.1507  1.0206  0.0531  0.1427  0.0225  260 ALA B O   
9330  C CB  . ALA B 251 ? 1.2744  1.3056  1.1905  0.0620  0.1293  0.0224  260 ALA B CB  
9336  N N   . GLY B 252 ? 1.0029  1.0782  0.9142  0.0784  0.1432  0.0179  261 GLY B N   
9337  C CA  . GLY B 252 ? 0.9045  0.9936  0.8238  0.0822  0.1419  0.0085  261 GLY B CA  
9338  C C   . GLY B 252 ? 0.8631  0.9431  0.7935  0.0762  0.1294  -0.0039 261 GLY B C   
9339  O O   . GLY B 252 ? 1.3922  1.4526  1.3177  0.0732  0.1205  -0.0080 261 GLY B O   
9343  N N   . GLY B 253 ? 0.7464  0.8432  0.6920  0.0758  0.1292  -0.0089 262 GLY B N   
9344  C CA  . GLY B 253 ? 0.6887  0.7791  0.6428  0.0726  0.1188  -0.0201 262 GLY B CA  
9345  C C   . GLY B 253 ? 1.2017  1.2714  1.1356  0.0812  0.1122  -0.0293 262 GLY B C   
9346  O O   . GLY B 253 ? 0.7699  0.8333  0.6826  0.0917  0.1156  -0.0302 262 GLY B O   
9350  N N   . SER B 254 ? 0.5194  0.5776  0.4596  0.0759  0.1028  -0.0362 263 SER B N   
9351  C CA  . SER B 254 ? 0.7520  0.7931  0.6793  0.0807  0.0955  -0.0446 263 SER B CA  
9352  C C   . SER B 254 ? 0.7498  0.7886  0.6912  0.0758  0.0883  -0.0512 263 SER B C   
9353  O O   . SER B 254 ? 0.6583  0.7044  0.6160  0.0683  0.0873  -0.0501 263 SER B O   
9354  C CB  . SER B 254 ? 1.0812  1.1067  0.9942  0.0810  0.0914  -0.0426 263 SER B CB  
9355  O OG  . SER B 254 ? 1.0998  1.1178  1.0235  0.0738  0.0850  -0.0423 263 SER B OG  
9361  N N   . ALA B 255 ? 0.9212  0.9490  0.8555  0.0797  0.0832  -0.0583 264 ALA B N   
9362  C CA  . ALA B 255 ? 0.7440  0.7703  0.6899  0.0768  0.0778  -0.0636 264 ALA B CA  
9363  C C   . ALA B 255 ? 1.0224  1.0439  0.9775  0.0697  0.0733  -0.0618 264 ALA B C   
9364  O O   . ALA B 255 ? 0.8933  0.9169  0.8595  0.0668  0.0704  -0.0652 264 ALA B O   
9365  C CB  . ALA B 255 ? 0.9683  0.9830  0.9057  0.0808  0.0740  -0.0697 264 ALA B CB  
9371  N N   . GLY B 256 ? 0.9598  0.9736  0.9083  0.0681  0.0728  -0.0565 265 GLY B N   
9372  C CA  . GLY B 256 ? 0.9451  0.9498  0.8997  0.0633  0.0693  -0.0543 265 GLY B CA  
9373  C C   . GLY B 256 ? 1.1476  1.1561  1.1158  0.0552  0.0715  -0.0529 265 GLY B C   
9374  O O   . GLY B 256 ? 0.8101  0.8082  0.7836  0.0516  0.0681  -0.0542 265 GLY B O   
9378  N N   . GLN B 257 ? 1.2629  1.2868  1.2375  0.0524  0.0766  -0.0512 266 GLN B N   
9379  C CA  . GLN B 257 ? 0.6864  0.7169  0.6762  0.0425  0.0770  -0.0513 266 GLN B CA  
9380  C C   . GLN B 257 ? 0.6675  0.7043  0.6656  0.0425  0.0717  -0.0609 266 GLN B C   
9381  O O   . GLN B 257 ? 0.5659  0.6060  0.5753  0.0338  0.0692  -0.0640 266 GLN B O   
9382  C CB  . GLN B 257 ? 0.8303  0.8799  0.8263  0.0391  0.0846  -0.0443 266 GLN B CB  
9383  C CG  . GLN B 257 ? 0.9301  0.9740  0.9168  0.0395  0.0914  -0.0334 266 GLN B CG  
9384  C CD  . GLN B 257 ? 0.8157  0.8815  0.8045  0.0414  0.1007  -0.0262 266 GLN B CD  
9385  O OE1 . GLN B 257 ? 0.6796  0.7645  0.6735  0.0461  0.1020  -0.0298 266 GLN B OE1 
9386  N NE2 . GLN B 257 ? 0.6840  0.7472  0.6670  0.0403  0.1082  -0.0151 266 GLN B NE2 
9395  N N   . SER B 258 ? 0.7418  0.7796  0.7337  0.0517  0.0697  -0.0657 267 SER B N   
9396  C CA  . SER B 258 ? 0.8119  0.8549  0.8092  0.0536  0.0657  -0.0733 267 SER B CA  
9397  C C   . SER B 258 ? 0.9205  0.9475  0.9187  0.0505  0.0605  -0.0774 267 SER B C   
9398  O O   . SER B 258 ? 0.9874  0.9998  0.9790  0.0543  0.0591  -0.0765 267 SER B O   
9399  C CB  . SER B 258 ? 0.8242  0.8682  0.8143  0.0637  0.0663  -0.0757 267 SER B CB  
9400  O OG  . SER B 258 ? 0.7208  0.7667  0.7141  0.0669  0.0629  -0.0818 267 SER B OG  
9406  N N   . SER B 259 ? 0.7052  0.7358  0.7110  0.0447  0.0573  -0.0826 268 SER B N   
9407  C CA  . SER B 259 ? 0.8734  0.8866  0.8769  0.0443  0.0530  -0.0880 268 SER B CA  
9408  C C   . SER B 259 ? 0.8254  0.8355  0.8227  0.0554  0.0520  -0.0906 268 SER B C   
9409  O O   . SER B 259 ? 0.7943  0.7893  0.7876  0.0589  0.0506  -0.0913 268 SER B O   
9410  C CB  . SER B 259 ? 0.8101  0.8284  0.8201  0.0369  0.0488  -0.0958 268 SER B CB  
9411  O OG  . SER B 259 ? 1.3607  1.3824  1.3795  0.0243  0.0500  -0.0926 268 SER B OG  
9417  N N   . VAL B 260 ? 0.9337  0.9587  0.9310  0.0613  0.0534  -0.0915 269 VAL B N   
9418  C CA  . VAL B 260 ? 0.8430  0.8670  0.8363  0.0706  0.0538  -0.0930 269 VAL B CA  
9419  C C   . VAL B 260 ? 0.8178  0.8320  0.8076  0.0732  0.0549  -0.0886 269 VAL B C   
9420  O O   . VAL B 260 ? 1.2125  1.2216  1.2019  0.0781  0.0542  -0.0892 269 VAL B O   
9421  C CB  . VAL B 260 ? 0.8461  0.8867  0.8395  0.0758  0.0564  -0.0932 269 VAL B CB  
9422  C CG1 . VAL B 260 ? 0.9468  0.9850  0.9359  0.0828  0.0602  -0.0902 269 VAL B CG1 
9423  C CG2 . VAL B 260 ? 1.1090  1.1576  1.1029  0.0789  0.0536  -0.0992 269 VAL B CG2 
9433  N N   . PHE B 261 ? 0.9816  0.9947  0.9690  0.0702  0.0564  -0.0840 270 PHE B N   
9434  C CA  . PHE B 261 ? 0.8759  0.8824  0.8586  0.0725  0.0559  -0.0809 270 PHE B CA  
9435  C C   . PHE B 261 ? 0.8655  0.8614  0.8484  0.0726  0.0527  -0.0792 270 PHE B C   
9436  O O   . PHE B 261 ? 0.9529  0.9469  0.9346  0.0756  0.0506  -0.0774 270 PHE B O   
9437  C CB  . PHE B 261 ? 0.6583  0.6670  0.6354  0.0704  0.0584  -0.0772 270 PHE B CB  
9438  C CG  . PHE B 261 ? 0.6481  0.6512  0.6171  0.0723  0.0570  -0.0752 270 PHE B CG  
9439  C CD1 . PHE B 261 ? 0.7749  0.7711  0.7404  0.0715  0.0541  -0.0713 270 PHE B CD1 
9440  C CD2 . PHE B 261 ? 0.7204  0.7246  0.6832  0.0750  0.0586  -0.0771 270 PHE B CD2 
9441  C CE1 . PHE B 261 ? 0.7492  0.7433  0.7057  0.0733  0.0514  -0.0700 270 PHE B CE1 
9442  C CE2 . PHE B 261 ? 0.7869  0.7856  0.7403  0.0754  0.0561  -0.0771 270 PHE B CE2 
9443  C CZ  . PHE B 261 ? 0.8142  0.8097  0.7647  0.0745  0.0518  -0.0738 270 PHE B CZ  
9453  N N   . GLN B 262 ? 0.8788  0.8678  0.8636  0.0698  0.0521  -0.0800 271 GLN B N   
9454  C CA  . GLN B 262 ? 0.9573  0.9328  0.9404  0.0714  0.0503  -0.0775 271 GLN B CA  
9455  C C   . GLN B 262 ? 0.9786  0.9481  0.9635  0.0760  0.0492  -0.0826 271 GLN B C   
9456  O O   . GLN B 262 ? 1.0820  1.0431  1.0657  0.0819  0.0482  -0.0804 271 GLN B O   
9457  C CB  . GLN B 262 ? 0.7660  0.7317  0.7471  0.0647  0.0518  -0.0736 271 GLN B CB  
9458  C CG  . GLN B 262 ? 1.0135  0.9838  0.9902  0.0624  0.0542  -0.0669 271 GLN B CG  
9459  C CD  . GLN B 262 ? 0.7650  0.7211  0.7369  0.0598  0.0562  -0.0588 271 GLN B CD  
9460  O OE1 . GLN B 262 ? 1.4253  1.3658  1.3955  0.0624  0.0551  -0.0573 271 GLN B OE1 
9461  N NE2 . GLN B 262 ? 0.9244  0.8853  0.8928  0.0563  0.0601  -0.0527 271 GLN B NE2 
9470  N N   . CYS B 263 ? 0.7959  0.7703  0.7825  0.0746  0.0493  -0.0890 272 CYS B N   
9471  C CA  . CYS B 263 ? 0.8974  0.8626  0.8819  0.0787  0.0482  -0.0947 272 CYS B CA  
9472  C C   . CYS B 263 ? 0.7268  0.6963  0.7118  0.0894  0.0493  -0.0944 272 CYS B C   
9473  O O   . CYS B 263 ? 0.7797  0.7398  0.7612  0.0958  0.0495  -0.0973 272 CYS B O   
9474  C CB  . CYS B 263 ? 1.0501  1.0207  1.0346  0.0741  0.0467  -0.1025 272 CYS B CB  
9475  S SG  . CYS B 263 ? 1.0223  1.0148  1.0086  0.0791  0.0480  -0.1041 272 CYS B SG  
9481  N N   . PHE B 264 ? 0.8719  0.8548  0.8611  0.0913  0.0506  -0.0911 273 PHE B N   
9482  C CA  . PHE B 264 ? 0.6780  0.6666  0.6706  0.0998  0.0525  -0.0897 273 PHE B CA  
9483  C C   . PHE B 264 ? 0.7364  0.7235  0.7327  0.1030  0.0512  -0.0839 273 PHE B C   
9484  O O   . PHE B 264 ? 0.9330  0.9182  0.9304  0.1114  0.0523  -0.0832 273 PHE B O   
9485  C CB  . PHE B 264 ? 0.6668  0.6689  0.6631  0.0997  0.0551  -0.0887 273 PHE B CB  
9486  C CG  . PHE B 264 ? 0.7947  0.8007  0.7866  0.1007  0.0566  -0.0935 273 PHE B CG  
9487  C CD1 . PHE B 264 ? 0.8968  0.9019  0.8845  0.1078  0.0577  -0.0976 273 PHE B CD1 
9488  C CD2 . PHE B 264 ? 0.7472  0.7583  0.7377  0.0956  0.0564  -0.0943 273 PHE B CD2 
9489  C CE1 . PHE B 264 ? 0.7882  0.7987  0.7705  0.1093  0.0575  -0.1026 273 PHE B CE1 
9490  C CE2 . PHE B 264 ? 0.6847  0.7026  0.6718  0.0974  0.0566  -0.0983 273 PHE B CE2 
9491  C CZ  . PHE B 264 ? 0.9915  1.0095  0.9743  0.1039  0.0565  -0.1028 273 PHE B CZ  
9501  N N   . ASP B 265 ? 0.6271  0.6141  0.6232  0.0977  0.0486  -0.0799 274 ASP B N   
9502  C CA  . ASP B 265 ? 0.5263  0.5119  0.5236  0.1014  0.0460  -0.0742 274 ASP B CA  
9503  C C   . ASP B 265 ? 0.9966  0.9670  0.9895  0.1082  0.0470  -0.0740 274 ASP B C   
9504  O O   . ASP B 265 ? 1.0638  1.0361  1.0597  0.1174  0.0469  -0.0703 274 ASP B O   
9505  C CB  . ASP B 265 ? 0.9956  0.9785  0.9877  0.0956  0.0434  -0.0706 274 ASP B CB  
9506  C CG  . ASP B 265 ? 1.2423  1.2345  1.2342  0.0893  0.0430  -0.0721 274 ASP B CG  
9507  O OD1 . ASP B 265 ? 1.1882  1.1906  1.1848  0.0895  0.0406  -0.0713 274 ASP B OD1 
9508  O OD2 . ASP B 265 ? 1.4081  1.3972  1.3953  0.0842  0.0452  -0.0741 274 ASP B OD2 
9513  N N   . VAL B 266 ? 0.7757  0.7305  0.7615  0.1037  0.0480  -0.0780 275 VAL B N   
9514  C CA  . VAL B 266 ? 0.6632  0.5975  0.6425  0.1089  0.0491  -0.0790 275 VAL B CA  
9515  C C   . VAL B 266 ? 0.8942  0.8278  0.8725  0.1182  0.0512  -0.0845 275 VAL B C   
9516  O O   . VAL B 266 ? 0.7096  0.6336  0.6847  0.1293  0.0530  -0.0827 275 VAL B O   
9517  C CB  . VAL B 266 ? 0.6871  0.6049  0.6607  0.0985  0.0492  -0.0824 275 VAL B CB  
9518  C CG1 . VAL B 266 ? 1.0027  0.8950  0.9680  0.1020  0.0504  -0.0875 275 VAL B CG1 
9519  C CG2 . VAL B 266 ? 0.6926  0.6072  0.6648  0.0935  0.0490  -0.0735 275 VAL B CG2 
9529  N N   . LEU B 267 ? 0.8917  0.8352  0.8710  0.1155  0.0518  -0.0907 276 LEU B N   
9530  C CA  . LEU B 267 ? 0.8493  0.7934  0.8255  0.1260  0.0546  -0.0952 276 LEU B CA  
9531  C C   . LEU B 267 ? 0.7405  0.6972  0.7246  0.1372  0.0573  -0.0879 276 LEU B C   
9532  O O   . LEU B 267 ? 0.6922  0.6410  0.6721  0.1492  0.0601  -0.0878 276 LEU B O   
9533  C CB  . LEU B 267 ? 0.7552  0.7125  0.7314  0.1235  0.0553  -0.1005 276 LEU B CB  
9534  C CG  . LEU B 267 ? 0.6849  0.6449  0.6564  0.1366  0.0594  -0.1035 276 LEU B CG  
9535  C CD1 . LEU B 267 ? 0.7593  0.6970  0.7163  0.1430  0.0592  -0.1120 276 LEU B CD1 
9536  C CD2 . LEU B 267 ? 0.5906  0.5648  0.5612  0.1363  0.0609  -0.1063 276 LEU B CD2 
9548  N N   . LEU B 268 ? 0.7589  0.7349  0.7545  0.1331  0.0563  -0.0816 277 LEU B N   
9549  C CA  . LEU B 268 ? 0.8310  0.8255  0.8387  0.1407  0.0581  -0.0748 277 LEU B CA  
9550  C C   . LEU B 268 ? 1.0104  1.0040  1.0208  0.1462  0.0555  -0.0680 277 LEU B C   
9551  O O   . LEU B 268 ? 0.8567  0.8697  0.8796  0.1521  0.0556  -0.0615 277 LEU B O   
9552  C CB  . LEU B 268 ? 0.7536  0.7676  0.7726  0.1324  0.0573  -0.0720 277 LEU B CB  
9553  C CG  . LEU B 268 ? 0.7211  0.7375  0.7375  0.1298  0.0611  -0.0764 277 LEU B CG  
9554  C CD1 . LEU B 268 ? 1.1732  1.2016  1.1980  0.1206  0.0608  -0.0739 277 LEU B CD1 
9555  C CD2 . LEU B 268 ? 0.5973  0.6179  0.6129  0.1414  0.0675  -0.0769 277 LEU B CD2 
9567  N N   . GLY B 269 ? 0.8334  0.8064  0.8334  0.1448  0.0534  -0.0684 278 GLY B N   
9568  C CA  . GLY B 269 ? 0.6995  0.6713  0.7003  0.1529  0.0516  -0.0605 278 GLY B CA  
9569  C C   . GLY B 269 ? 0.6966  0.6872  0.7058  0.1472  0.0459  -0.0542 278 GLY B C   
9570  O O   . GLY B 269 ? 0.6328  0.6350  0.6476  0.1556  0.0434  -0.0467 278 GLY B O   
9574  N N   . ILE B 270 ? 0.7809  0.7736  0.7891  0.1341  0.0434  -0.0573 279 ILE B N   
9575  C CA  . ILE B 270 ? 0.6973  0.7024  0.7081  0.1283  0.0375  -0.0533 279 ILE B CA  
9576  C C   . ILE B 270 ? 0.9970  0.9833  0.9942  0.1270  0.0365  -0.0501 279 ILE B C   
9577  O O   . ILE B 270 ? 1.4757  1.4464  1.4648  0.1195  0.0391  -0.0537 279 ILE B O   
9578  C CB  . ILE B 270 ? 0.8250  0.8399  0.8396  0.1166  0.0367  -0.0583 279 ILE B CB  
9579  C CG1 . ILE B 270 ? 1.0851  1.1136  1.1120  0.1186  0.0403  -0.0602 279 ILE B CG1 
9580  C CG2 . ILE B 270 ? 0.8116  0.8384  0.8273  0.1113  0.0301  -0.0561 279 ILE B CG2 
9581  C CD1 . ILE B 270 ? 0.4837  0.5147  0.5115  0.1093  0.0420  -0.0647 279 ILE B CD1 
9593  N N   . GLN B 271 ? 0.9389  0.9280  0.9343  0.1351  0.0334  -0.0423 280 GLN B N   
9594  C CA  . GLN B 271 ? 1.0232  0.9935  1.0050  0.1363  0.0339  -0.0367 280 GLN B CA  
9595  C C   . GLN B 271 ? 0.9507  0.9285  0.9275  0.1265  0.0300  -0.0366 280 GLN B C   
9596  O O   . GLN B 271 ? 0.9109  0.8999  0.8844  0.1298  0.0245  -0.0312 280 GLN B O   
9597  C CB  . GLN B 271 ? 1.1921  1.1628  1.1720  0.1515  0.0324  -0.0270 280 GLN B CB  
9598  C CG  . GLN B 271 ? 1.3593  1.3221  1.3426  0.1642  0.0373  -0.0271 280 GLN B CG  
9599  C CD  . GLN B 271 ? 1.4924  1.4574  1.4740  0.1822  0.0366  -0.0162 280 GLN B CD  
9600  O OE1 . GLN B 271 ? 1.8156  1.7679  1.7855  0.1862  0.0361  -0.0082 280 GLN B OE1 
9601  N NE2 . GLN B 271 ? 1.7742  1.7561  1.7672  0.1943  0.0375  -0.0148 280 GLN B NE2 
9610  N N   . GLN B 272 ? 0.9756  0.9489  0.9513  0.1155  0.0328  -0.0433 281 GLN B N   
9611  C CA  . GLN B 272 ? 0.9661  0.9435  0.9345  0.1078  0.0309  -0.0434 281 GLN B CA  
9612  C C   . GLN B 272 ? 0.9434  0.9060  0.8984  0.1095  0.0331  -0.0352 281 GLN B C   
9613  O O   . GLN B 272 ? 0.9437  0.9106  0.8892  0.1074  0.0314  -0.0324 281 GLN B O   
9614  C CB  . GLN B 272 ? 1.1323  1.1093  1.1024  0.0979  0.0344  -0.0510 281 GLN B CB  
9615  C CG  . GLN B 272 ? 1.0459  1.0371  1.0268  0.0959  0.0331  -0.0575 281 GLN B CG  
9616  C CD  . GLN B 272 ? 1.0009  1.0058  0.9815  0.0926  0.0277  -0.0591 281 GLN B CD  
9617  O OE1 . GLN B 272 ? 0.7656  0.7728  0.7375  0.0939  0.0231  -0.0556 281 GLN B OE1 
9618  N NE2 . GLN B 272 ? 0.6186  0.6313  0.6073  0.0883  0.0283  -0.0647 281 GLN B NE2 
9627  N N   . THR B 273 ? 1.4355  1.3785  1.3881  0.1131  0.0378  -0.0313 282 THR B N   
9628  C CA  . THR B 273 ? 1.4711  1.3966  1.4116  0.1138  0.0417  -0.0221 282 THR B CA  
9629  C C   . THR B 273 ? 1.1110  1.0347  1.0444  0.1276  0.0393  -0.0116 282 THR B C   
9630  O O   . THR B 273 ? 1.0982  1.0075  1.0195  0.1305  0.0429  -0.0015 282 THR B O   
9631  C CB  . THR B 273 ? 0.9678  0.8699  0.9092  0.1078  0.0484  -0.0243 282 THR B CB  
9632  O OG1 . THR B 273 ? 1.1092  1.0099  1.0589  0.1108  0.0477  -0.0323 282 THR B OG1 
9633  C CG2 . THR B 273 ? 0.7276  0.6322  0.6709  0.0945  0.0515  -0.0283 282 THR B CG2 
9641  N N   . ALA B 274 ? 1.8806  1.8220  1.8215  0.1363  0.0332  -0.0125 283 ALA B N   
9642  C CA  . ALA B 274 ? 1.2369  1.1822  1.1729  0.1511  0.0300  -0.0021 283 ALA B CA  
9643  C C   . ALA B 274 ? 1.6470  1.6147  1.5767  0.1527  0.0218  0.0013  283 ALA B C   
9644  O O   . ALA B 274 ? 1.9535  1.9333  1.8832  0.1425  0.0184  -0.0057 283 ALA B O   
9645  C CB  . ALA B 274 ? 1.0489  1.0057  0.9980  0.1610  0.0279  -0.0040 283 ALA B CB  
9651  N N   . GLY B 275 ? 1.3285  1.3005  1.2510  0.1670  0.0185  0.0123  284 GLY B N   
9652  C CA  . GLY B 275 ? 1.0521  1.0474  0.9673  0.1715  0.0088  0.0159  284 GLY B CA  
9653  C C   . GLY B 275 ? 1.3191  1.3036  1.2122  0.1730  0.0110  0.0243  284 GLY B C   
9654  O O   . GLY B 275 ? 1.4911  1.4889  1.3733  0.1840  0.0044  0.0323  284 GLY B O   
9658  N N   . GLY B 276 ? 1.9457  1.9087  1.8319  0.1629  0.0202  0.0235  285 GLY B N   
9659  C CA  . GLY B 276 ? 1.3507  1.3032  1.2164  0.1647  0.0248  0.0334  285 GLY B CA  
9660  C C   . GLY B 276 ? 1.3408  1.3099  1.1963  0.1585  0.0197  0.0273  285 GLY B C   
9661  O O   . GLY B 276 ? 1.1214  1.0886  0.9564  0.1642  0.0212  0.0362  285 GLY B O   
9665  N N   . GLY B 277 ? 1.5711  1.5556  1.4381  0.1486  0.0138  0.0128  286 GLY B N   
9666  C CA  . GLY B 277 ? 1.4890  1.4848  1.3453  0.1425  0.0094  0.0048  286 GLY B CA  
9667  C C   . GLY B 277 ? 1.4370  1.4187  1.2858  0.1342  0.0204  0.0044  286 GLY B C   
9668  O O   . GLY B 277 ? 0.8638  0.8294  0.7205  0.1291  0.0306  0.0077  286 GLY B O   
9672  N N   . HIS B 278 ? 1.3517  1.3407  1.1850  0.1326  0.0181  -0.0006 287 HIS B N   
9673  C CA  . HIS B 278 ? 1.1864  1.1662  1.0141  0.1261  0.0291  -0.0009 287 HIS B CA  
9674  C C   . HIS B 278 ? 0.9326  0.9087  0.7820  0.1150  0.0336  -0.0094 287 HIS B C   
9675  O O   . HIS B 278 ? 0.7644  0.7301  0.6209  0.1097  0.0439  -0.0051 287 HIS B O   
9676  C CB  . HIS B 278 ? 1.5068  1.4951  1.3149  0.1270  0.0253  -0.0083 287 HIS B CB  
9677  C CG  . HIS B 278 ? 1.3807  1.3629  1.1835  0.1223  0.0370  -0.0088 287 HIS B CG  
9682  N N   . ALA B 279 ? 1.0835  1.0688  0.9455  0.1115  0.0256  -0.0206 288 ALA B N   
9683  C CA  . ALA B 279 ? 0.8335  0.8159  0.7135  0.1027  0.0301  -0.0279 288 ALA B CA  
9684  C C   . ALA B 279 ? 0.9960  0.9680  0.8895  0.1021  0.0350  -0.0226 288 ALA B C   
9685  O O   . ALA B 279 ? 0.8316  0.7989  0.7363  0.0951  0.0408  -0.0264 288 ALA B O   
9686  C CB  . ALA B 279 ? 0.8482  0.8414  0.7391  0.0994  0.0219  -0.0393 288 ALA B CB  
9692  N N   . ALA B 280 ? 1.5574  1.5265  1.4503  0.1100  0.0319  -0.0152 289 ALA B N   
9693  C CA  . ALA B 280 ? 1.4432  1.3980  1.3464  0.1107  0.0366  -0.0112 289 ALA B CA  
9694  C C   . ALA B 280 ? 1.0202  0.9568  0.9186  0.1063  0.0472  -0.0033 289 ALA B C   
9695  O O   . ALA B 280 ? 0.8066  0.7328  0.7159  0.0992  0.0520  -0.0064 289 ALA B O   
9696  C CB  . ALA B 280 ? 1.7548  1.7106  1.6573  0.1227  0.0313  -0.0046 289 ALA B CB  
9702  N N   . GLN B 281 ? 0.9645  0.8988  0.8471  0.1092  0.0509  0.0064  290 GLN B N   
9703  C CA  . GLN B 281 ? 1.2776  1.1967  1.1581  0.1033  0.0622  0.0152  290 GLN B CA  
9704  C C   . GLN B 281 ? 1.3698  1.2956  1.2610  0.0910  0.0668  0.0074  290 GLN B C   
9705  O O   . GLN B 281 ? 1.5678  1.4834  1.4688  0.0818  0.0739  0.0093  290 GLN B O   
9706  C CB  . GLN B 281 ? 0.8833  0.8020  0.7433  0.1100  0.0665  0.0282  290 GLN B CB  
9709  N N   . PHE B 282 ? 1.2248  1.1676  1.1139  0.0909  0.0627  -0.0015 291 PHE B N   
9710  C CA  . PHE B 282 ? 0.9482  0.8995  0.8438  0.0827  0.0681  -0.0066 291 PHE B CA  
9711  C C   . PHE B 282 ? 0.8680  0.8178  0.7830  0.0741  0.0685  -0.0143 291 PHE B C   
9712  O O   . PHE B 282 ? 1.0995  1.0521  1.0235  0.0657  0.0748  -0.0139 291 PHE B O   
9713  C CB  . PHE B 282 ? 0.8553  0.8205  0.7431  0.0858  0.0636  -0.0156 291 PHE B CB  
9714  C CG  . PHE B 282 ? 1.0067  0.9808  0.8988  0.0808  0.0702  -0.0194 291 PHE B CG  
9715  C CD1 . PHE B 282 ? 0.9035  0.8816  0.7853  0.0821  0.0790  -0.0118 291 PHE B CD1 
9716  C CD2 . PHE B 282 ? 1.1637  1.1437  1.0692  0.0765  0.0685  -0.0296 291 PHE B CD2 
9717  C CE1 . PHE B 282 ? 0.8646  0.8535  0.7507  0.0797  0.0855  -0.0142 291 PHE B CE1 
9718  C CE2 . PHE B 282 ? 0.7318  0.7218  0.6406  0.0743  0.0747  -0.0319 291 PHE B CE2 
9719  C CZ  . PHE B 282 ? 0.7044  0.6996  0.6043  0.0760  0.0830  -0.0244 291 PHE B CZ  
9729  N N   . LEU B 283 ? 0.6220  0.5704  0.5438  0.0765  0.0614  -0.0215 292 LEU B N   
9730  C CA  . LEU B 283 ? 0.6341  0.5811  0.5710  0.0706  0.0610  -0.0294 292 LEU B CA  
9731  C C   . LEU B 283 ? 1.2204  1.1501  1.1627  0.0650  0.0654  -0.0251 292 LEU B C   
9732  O O   . LEU B 283 ? 0.8942  0.8238  0.8475  0.0568  0.0666  -0.0311 292 LEU B O   
9733  C CB  . LEU B 283 ? 1.1432  1.0934  1.0842  0.0764  0.0536  -0.0364 292 LEU B CB  
9734  C CG  . LEU B 283 ? 0.9702  0.9355  0.9110  0.0783  0.0491  -0.0437 292 LEU B CG  
9735  C CD1 . LEU B 283 ? 0.9875  0.9566  0.9317  0.0848  0.0417  -0.0457 292 LEU B CD1 
9736  C CD2 . LEU B 283 ? 1.5740  1.5459  1.5243  0.0732  0.0512  -0.0516 292 LEU B CD2 
9748  N N   . GLN B 284 ? 1.1227  1.0365  1.0567  0.0696  0.0671  -0.0154 293 GLN B N   
9749  C CA  . GLN B 284 ? 1.1643  1.0561  1.1018  0.0634  0.0722  -0.0110 293 GLN B CA  
9750  C C   . GLN B 284 ? 1.2274  1.1216  1.1684  0.0520  0.0803  -0.0049 293 GLN B C   
9751  O O   . GLN B 284 ? 1.4149  1.3032  1.3675  0.0399  0.0830  -0.0080 293 GLN B O   
9752  C CB  . GLN B 284 ? 1.2322  1.1046  1.1582  0.0739  0.0727  -0.0008 293 GLN B CB  
9753  C CG  . GLN B 284 ? 1.0403  0.8824  0.9678  0.0701  0.0773  0.0021  293 GLN B CG  
9754  C CD  . GLN B 284 ? 0.8370  0.6717  0.7720  0.0704  0.0726  -0.0107 293 GLN B CD  
9755  O OE1 . GLN B 284 ? 1.4538  1.2926  1.3869  0.0824  0.0676  -0.0136 293 GLN B OE1 
9756  N NE2 . GLN B 284 ? 0.8134  0.6408  0.7577  0.0569  0.0742  -0.0187 293 GLN B NE2 
9765  N N   . ASP B 285 ? 1.2231  1.1284  1.1544  0.0557  0.0839  0.0033  294 ASP B N   
9766  C CA  . ASP B 285 ? 1.1004  1.0120  1.0349  0.0469  0.0932  0.0113  294 ASP B CA  
9767  C C   . ASP B 285 ? 1.0482  0.9804  0.9979  0.0378  0.0932  0.0020  294 ASP B C   
9768  O O   . ASP B 285 ? 0.9852  0.9208  0.9476  0.0255  0.0991  0.0050  294 ASP B O   
9769  C CB  . ASP B 285 ? 1.0851  1.0048  1.0019  0.0564  0.0969  0.0214  294 ASP B CB  
9774  N N   . MET B 286 ? 1.8660  1.8134  1.8152  0.0435  0.0870  -0.0084 295 MET B N   
9775  C CA  . MET B 286 ? 2.7349  2.7010  2.6977  0.0369  0.0873  -0.0161 295 MET B CA  
9776  C C   . MET B 286 ? 1.2307  1.1905  1.2081  0.0277  0.0835  -0.0241 295 MET B C   
9777  O O   . MET B 286 ? 0.5531  0.5292  0.5425  0.0219  0.0827  -0.0306 295 MET B O   
9778  C CB  . MET B 286 ? 5.5054  5.4854  5.4637  0.0453  0.0824  -0.0251 295 MET B CB  
9779  C CG  . MET B 286 ? 8.2738  8.2647  8.2189  0.0528  0.0861  -0.0215 295 MET B CG  
9780  S SD  . MET B 286 ? 13.0798 13.0890 13.0309 0.0479  0.0977  -0.0130 295 MET B SD  
9781  C CE  . MET B 286 ? 9.3611  9.3576  9.2972  0.0504  0.1043  0.0022  295 MET B CE  
9791  N N   . ARG B 287 ? 1.0636  1.0007  1.0384  0.0283  0.0803  -0.0252 296 ARG B N   
9792  C CA  . ARG B 287 ? 1.0309  0.9593  1.0166  0.0195  0.0769  -0.0342 296 ARG B CA  
9793  C C   . ARG B 287 ? 0.9642  0.8910  0.9622  0.0032  0.0818  -0.0306 296 ARG B C   
9794  O O   . ARG B 287 ? 0.6215  0.5500  0.6308  -0.0067 0.0780  -0.0402 296 ARG B O   
9795  C CB  . ARG B 287 ? 0.8508  0.7523  0.8291  0.0251  0.0735  -0.0362 296 ARG B CB  
9796  C CG  . ARG B 287 ? 0.8661  0.7734  0.8390  0.0380  0.0675  -0.0426 296 ARG B CG  
9797  C CD  . ARG B 287 ? 0.9274  0.8143  0.8978  0.0425  0.0642  -0.0482 296 ARG B CD  
9798  N NE  . ARG B 287 ? 0.9276  0.8224  0.8950  0.0550  0.0595  -0.0525 296 ARG B NE  
9799  C CZ  . ARG B 287 ? 0.8842  0.7645  0.8475  0.0640  0.0576  -0.0544 296 ARG B CZ  
9800  N NH1 . ARG B 287 ? 0.8886  0.7415  0.8474  0.0631  0.0600  -0.0530 296 ARG B NH1 
9801  N NH2 . ARG B 287 ? 1.2890  1.1821  1.2528  0.0743  0.0541  -0.0570 296 ARG B NH2 
9815  N N   . ARG B 288 ? 1.0064  0.9286  1.0017  0.0002  0.0901  -0.0170 297 ARG B N   
9816  C CA  . ARG B 288 ? 0.7623  0.6850  0.7710  -0.0163 0.0968  -0.0104 297 ARG B CA  
9817  C C   . ARG B 288 ? 0.9322  0.8914  0.9555  -0.0220 0.0986  -0.0118 297 ARG B C   
9818  O O   . ARG B 288 ? 1.2667  1.2351  1.3071  -0.0377 0.1028  -0.0083 297 ARG B O   
9819  C CB  . ARG B 288 ? 0.6903  0.5973  0.6890  -0.0145 0.1068  0.0072  297 ARG B CB  
9822  N N   . TYR B 289 ? 0.9725  0.9526  0.9901  -0.0095 0.0957  -0.0164 298 TYR B N   
9823  C CA  . TYR B 289 ? 0.7528  0.7672  0.7809  -0.0100 0.0980  -0.0172 298 TYR B CA  
9824  C C   . TYR B 289 ? 0.6562  0.6853  0.6947  -0.0118 0.0896  -0.0311 298 TYR B C   
9825  O O   . TYR B 289 ? 0.5742  0.6318  0.6195  -0.0086 0.0906  -0.0323 298 TYR B O   
9826  C CB  . TYR B 289 ? 0.5580  0.5834  0.5708  0.0058  0.1013  -0.0135 298 TYR B CB  
9827  C CG  . TYR B 289 ? 0.6536  0.6736  0.6545  0.0097  0.1106  0.0008  298 TYR B CG  
9828  C CD1 . TYR B 289 ? 0.8726  0.8657  0.8595  0.0131  0.1106  0.0067  298 TYR B CD1 
9829  C CD2 . TYR B 289 ? 0.7739  0.8171  0.7765  0.0118  0.1200  0.0092  298 TYR B CD2 
9830  C CE1 . TYR B 289 ? 0.8271  0.8162  0.8010  0.0180  0.1191  0.0204  298 TYR B CE1 
9831  C CE2 . TYR B 289 ? 0.6601  0.6990  0.6496  0.0166  0.1293  0.0226  298 TYR B CE2 
9832  C CZ  . TYR B 289 ? 0.6469  0.6591  0.6218  0.0194  0.1286  0.0282  298 TYR B CZ  
9833  O OH  . TYR B 289 ? 0.7682  0.7781  0.7280  0.0259  0.1381  0.0424  298 TYR B OH  
9843  N N   . MET B 290 ? 0.7000  0.7109  0.7377  -0.0145 0.0819  -0.0408 299 MET B N   
9844  C CA  . MET B 290 ? 0.7334  0.7568  0.7793  -0.0164 0.0737  -0.0539 299 MET B CA  
9845  C C   . MET B 290 ? 0.8452  0.8704  0.9079  -0.0352 0.0709  -0.0583 299 MET B C   
9846  O O   . MET B 290 ? 1.1018  1.1104  1.1688  -0.0471 0.0753  -0.0517 299 MET B O   
9847  C CB  . MET B 290 ? 0.8710  0.8732  0.9039  -0.0068 0.0671  -0.0628 299 MET B CB  
9848  C CG  . MET B 290 ? 1.1719  1.1726  1.1905  0.0097  0.0675  -0.0612 299 MET B CG  
9849  S SD  . MET B 290 ? 4.3122  4.2914  4.3209  0.0184  0.0609  -0.0701 299 MET B SD  
9850  C CE  . MET B 290 ? 0.7017  0.6835  0.6987  0.0322  0.0628  -0.0645 299 MET B CE  
9860  N N   . PRO B 291 ? 0.9973  1.0430  1.0701  -0.0389 0.0636  -0.0689 300 PRO B N   
9861  C CA  . PRO B 291 ? 1.0439  1.0885  1.1308  -0.0576 0.0582  -0.0762 300 PRO B CA  
9862  C C   . PRO B 291 ? 0.7818  0.7825  0.8573  -0.0617 0.0566  -0.0801 300 PRO B C   
9863  O O   . PRO B 291 ? 0.8022  0.7823  0.8602  -0.0474 0.0551  -0.0832 300 PRO B O   
9864  C CB  . PRO B 291 ? 0.8680  0.9351  0.9578  -0.0538 0.0483  -0.0897 300 PRO B CB  
9865  C CG  . PRO B 291 ? 0.7228  0.8147  0.8091  -0.0374 0.0519  -0.0845 300 PRO B CG  
9866  C CD  . PRO B 291 ? 0.6964  0.7674  0.7676  -0.0264 0.0599  -0.0746 300 PRO B CD  
9874  N N   . PRO B 292 ? 0.9591  0.9445  1.0445  -0.0808 0.0571  -0.0801 301 PRO B N   
9875  C CA  . PRO B 292 ? 1.0084  0.9471  1.0804  -0.0830 0.0566  -0.0836 301 PRO B CA  
9876  C C   . PRO B 292 ? 1.0927  1.0189  1.1520  -0.0747 0.0467  -0.1005 301 PRO B C   
9877  O O   . PRO B 292 ? 1.1994  1.0947  1.2409  -0.0624 0.0476  -0.1014 301 PRO B O   
9878  C CB  . PRO B 292 ? 1.1186  1.0486  1.2071  -0.1082 0.0579  -0.0828 301 PRO B CB  
9879  C CG  . PRO B 292 ? 1.1436  1.1178  1.2531  -0.1188 0.0515  -0.0893 301 PRO B CG  
9880  C CD  . PRO B 292 ? 1.0448  1.0560  1.1538  -0.1012 0.0536  -0.0838 301 PRO B CD  
9888  N N   . ALA B 293 ? 1.2079  1.1594  1.2754  -0.0795 0.0374  -0.1133 302 ALA B N   
9889  C CA  . ALA B 293 ? 0.9004  0.8411  0.9535  -0.0702 0.0286  -0.1291 302 ALA B CA  
9890  C C   . ALA B 293 ? 1.3727  1.3105  1.4094  -0.0463 0.0317  -0.1254 302 ALA B C   
9891  O O   . ALA B 293 ? 0.9205  0.8325  0.9409  -0.0356 0.0299  -0.1320 302 ALA B O   
9892  C CB  . ALA B 293 ? 0.7275  0.7048  0.7906  -0.0748 0.0189  -0.1405 302 ALA B CB  
9898  N N   . HIS B 294 ? 1.3541  1.3179  1.3953  -0.0376 0.0366  -0.1147 303 HIS B N   
9899  C CA  . HIS B 294 ? 1.3000  1.2641  1.3284  -0.0176 0.0386  -0.1120 303 HIS B CA  
9900  C C   . HIS B 294 ? 0.7993  0.7351  0.8176  -0.0112 0.0448  -0.1026 303 HIS B C   
9901  O O   . HIS B 294 ? 0.6437  0.5670  0.6499  0.0028  0.0445  -0.1038 303 HIS B O   
9902  C CB  . HIS B 294 ? 0.8611  0.8600  0.8962  -0.0111 0.0415  -0.1053 303 HIS B CB  
9903  C CG  . HIS B 294 ? 0.9332  0.9636  0.9770  -0.0130 0.0357  -0.1130 303 HIS B CG  
9904  N ND1 . HIS B 294 ? 0.8930  0.9563  0.9453  -0.0091 0.0386  -0.1070 303 HIS B ND1 
9905  C CD2 . HIS B 294 ? 0.8696  0.9039  0.9128  -0.0160 0.0271  -0.1261 303 HIS B CD2 
9906  C CE1 . HIS B 294 ? 0.7696  0.8574  0.8278  -0.0096 0.0320  -0.1149 303 HIS B CE1 
9907  N NE2 . HIS B 294 ? 0.7133  0.7851  0.7660  -0.0143 0.0244  -0.1269 303 HIS B NE2 
9915  N N   . ARG B 295 ? 0.8146  0.7394  0.8375  -0.0212 0.0504  -0.0929 304 ARG B N   
9916  C CA  . ARG B 295 ? 0.8230  0.7191  0.8340  -0.0135 0.0555  -0.0840 304 ARG B CA  
9917  C C   . ARG B 295 ? 0.8899  0.7519  0.8902  -0.0112 0.0524  -0.0926 304 ARG B C   
9918  O O   . ARG B 295 ? 1.0086  0.8539  0.9968  0.0030  0.0540  -0.0894 304 ARG B O   
9919  C CB  . ARG B 295 ? 0.7367  0.6267  0.7529  -0.0235 0.0635  -0.0700 304 ARG B CB  
9920  C CG  . ARG B 295 ? 0.9391  0.7930  0.9554  -0.0372 0.0661  -0.0689 304 ARG B CG  
9921  C CD  . ARG B 295 ? 1.2441  1.0949  1.2670  -0.0478 0.0757  -0.0530 304 ARG B CD  
9922  N NE  . ARG B 295 ? 1.8518  1.7422  1.8918  -0.0567 0.0773  -0.0498 304 ARG B NE  
9923  C CZ  . ARG B 295 ? 1.5609  1.4588  1.6145  -0.0717 0.0845  -0.0396 304 ARG B CZ  
9924  N NH1 . ARG B 295 ? 1.9361  1.8020  1.9884  -0.0815 0.0910  -0.0312 304 ARG B NH1 
9925  N NH2 . ARG B 295 ? 1.6881  1.6259  1.7571  -0.0763 0.0861  -0.0369 304 ARG B NH2 
9939  N N   . ASN B 296 ? 1.1807  1.0347  1.1851  -0.0241 0.0474  -0.1047 305 ASN B N   
9940  C CA  . ASN B 296 ? 1.0880  0.9071  1.0797  -0.0221 0.0442  -0.1156 305 ASN B CA  
9941  C C   . ASN B 296 ? 0.9217  0.7474  0.9027  -0.0051 0.0396  -0.1251 305 ASN B C   
9942  O O   . ASN B 296 ? 1.3896  1.1877  1.3562  0.0060  0.0402  -0.1291 305 ASN B O   
9943  C CB  . ASN B 296 ? 1.0516  0.8615  1.0502  -0.0427 0.0390  -0.1273 305 ASN B CB  
9944  C CG  . ASN B 296 ? 1.2910  1.0862  1.3002  -0.0613 0.0450  -0.1174 305 ASN B CG  
9945  O OD1 . ASN B 296 ? 1.9812  1.7648  1.9875  -0.0563 0.0537  -0.1018 305 ASN B OD1 
9946  N ND2 . ASN B 296 ? 1.1505  0.9466  1.1717  -0.0830 0.0402  -0.1262 305 ASN B ND2 
9953  N N   . PHE B 297 ? 0.9665  0.8279  0.9539  -0.0015 0.0363  -0.1278 306 PHE B N   
9954  C CA  . PHE B 297 ? 0.7683  0.6365  0.7460  0.0151  0.0338  -0.1342 306 PHE B CA  
9955  C C   . PHE B 297 ? 0.8398  0.7010  0.8108  0.0314  0.0393  -0.1241 306 PHE B C   
9956  O O   . PHE B 297 ? 0.9401  0.7852  0.8998  0.0442  0.0397  -0.1278 306 PHE B O   
9957  C CB  . PHE B 297 ? 0.6829  0.5892  0.6681  0.0169  0.0307  -0.1364 306 PHE B CB  
9958  C CG  . PHE B 297 ? 0.8078  0.7212  0.7833  0.0340  0.0299  -0.1408 306 PHE B CG  
9959  C CD1 . PHE B 297 ? 1.0004  0.9020  0.9641  0.0384  0.0254  -0.1540 306 PHE B CD1 
9960  C CD2 . PHE B 297 ? 0.7466  0.6775  0.7240  0.0455  0.0340  -0.1319 306 PHE B CD2 
9961  C CE1 . PHE B 297 ? 0.8684  0.7779  0.8228  0.0549  0.0261  -0.1567 306 PHE B CE1 
9962  C CE2 . PHE B 297 ? 0.7315  0.6700  0.7020  0.0599  0.0344  -0.1347 306 PHE B CE2 
9963  C CZ  . PHE B 297 ? 0.6774  0.6060  0.6364  0.0654  0.0311  -0.1464 306 PHE B CZ  
9973  N N   . LEU B 298 ? 0.6503  0.5245  0.6279  0.0315  0.0434  -0.1113 307 LEU B N   
9974  C CA  . LEU B 298 ? 0.6290  0.5004  0.6014  0.0456  0.0469  -0.1022 307 LEU B CA  
9975  C C   . LEU B 298 ? 1.1773  1.0146  1.1396  0.0510  0.0492  -0.1005 307 LEU B C   
9976  O O   . LEU B 298 ? 1.1582  0.9900  1.1140  0.0660  0.0503  -0.0984 307 LEU B O   
9977  C CB  . LEU B 298 ? 0.6103  0.4953  0.5881  0.0431  0.0502  -0.0901 307 LEU B CB  
9978  C CG  . LEU B 298 ? 0.8016  0.7179  0.7871  0.0411  0.0493  -0.0907 307 LEU B CG  
9979  C CD1 . LEU B 298 ? 0.5861  0.5099  0.5727  0.0399  0.0534  -0.0790 307 LEU B CD1 
9980  C CD2 . LEU B 298 ? 1.0063  0.9367  0.9902  0.0524  0.0475  -0.0948 307 LEU B CD2 
9992  N N   . CYS B 299 ? 0.8747  0.6890  0.8364  0.0389  0.0504  -0.1007 308 CYS B N   
9993  C CA  . CYS B 299 ? 0.8166  0.5938  0.7672  0.0441  0.0539  -0.0976 308 CYS B CA  
9994  C C   . CYS B 299 ? 0.8939  0.6537  0.8328  0.0555  0.0518  -0.1095 308 CYS B C   
9995  O O   . CYS B 299 ? 0.7268  0.4705  0.6561  0.0717  0.0550  -0.1052 308 CYS B O   
9996  C CB  . CYS B 299 ? 1.0529  0.8076  1.0061  0.0260  0.0560  -0.0967 308 CYS B CB  
9997  S SG  . CYS B 299 ? 1.4169  1.1204  1.3556  0.0308  0.0620  -0.0913 308 CYS B SG  
10002 N N   . SER B 300 ? 0.7959  0.5615  0.7347  0.0489  0.0465  -0.1241 309 SER B N   
10003 C CA  . SER B 300 ? 0.8856  0.6358  0.8107  0.0603  0.0448  -0.1363 309 SER B CA  
10004 C C   . SER B 300 ? 0.9692  0.7425  0.8936  0.0796  0.0463  -0.1328 309 SER B C   
10005 O O   . SER B 300 ? 1.4320  1.1915  1.3443  0.0948  0.0481  -0.1375 309 SER B O   
10006 C CB  . SER B 300 ? 1.0311  0.7860  0.9554  0.0482  0.0375  -0.1530 309 SER B CB  
10007 O OG  . SER B 300 ? 1.1669  0.9615  1.0987  0.0510  0.0343  -0.1546 309 SER B OG  
10013 N N   . LEU B 301 ? 1.1159  0.9227  1.0526  0.0794  0.0463  -0.1245 310 LEU B N   
10014 C CA  . LEU B 301 ? 1.0858  0.9127  1.0240  0.0956  0.0483  -0.1198 310 LEU B CA  
10015 C C   . LEU B 301 ? 0.7687  0.5846  0.7045  0.1084  0.0525  -0.1089 310 LEU B C   
10016 O O   . LEU B 301 ? 0.9728  0.7848  0.9027  0.1244  0.0551  -0.1095 310 LEU B O   
10017 C CB  . LEU B 301 ? 1.0880  0.9495  1.0388  0.0914  0.0472  -0.1146 310 LEU B CB  
10018 C CG  . LEU B 301 ? 0.6915  0.5715  0.6454  0.0838  0.0436  -0.1232 310 LEU B CG  
10019 C CD1 . LEU B 301 ? 0.7642  0.6729  0.7279  0.0854  0.0449  -0.1154 310 LEU B CD1 
10020 C CD2 . LEU B 301 ? 0.8327  0.7092  0.7763  0.0923  0.0423  -0.1345 310 LEU B CD2 
10032 N N   . GLU B 302 ? 0.6557  0.4671  0.5951  0.1031  0.0537  -0.0985 311 GLU B N   
10033 C CA  . GLU B 302 ? 0.7066  0.5097  0.6427  0.1173  0.0570  -0.0877 311 GLU B CA  
10034 C C   . GLU B 302 ? 1.0109  0.7786  0.9326  0.1281  0.0603  -0.0920 311 GLU B C   
10035 O O   . GLU B 302 ? 1.7539  1.5197  1.6722  0.1459  0.0633  -0.0861 311 GLU B O   
10036 C CB  . GLU B 302 ? 0.8414  0.6418  0.7797  0.1107  0.0579  -0.0756 311 GLU B CB  
10037 C CG  . GLU B 302 ? 1.1579  0.9912  1.1066  0.1055  0.0554  -0.0703 311 GLU B CG  
10038 C CD  . GLU B 302 ? 1.2068  1.0394  1.1541  0.1044  0.0566  -0.0573 311 GLU B CD  
10039 O OE1 . GLU B 302 ? 0.9494  0.7839  0.8986  0.0914  0.0574  -0.0553 311 GLU B OE1 
10040 O OE2 . GLU B 302 ? 1.7541  1.5873  1.6983  0.1174  0.0568  -0.0486 311 GLU B OE2 
10047 N N   . SER B 303 ? 1.0226  0.7638  0.9360  0.1180  0.0596  -0.1032 312 SER B N   
10048 C CA  . SER B 303 ? 1.1370  0.8384  1.0339  0.1271  0.0629  -0.1085 312 SER B CA  
10049 C C   . SER B 303 ? 1.1845  0.8919  1.0743  0.1441  0.0637  -0.1166 312 SER B C   
10050 O O   . SER B 303 ? 1.2638  0.9483  1.1410  0.1616  0.0685  -0.1159 312 SER B O   
10051 C CB  . SER B 303 ? 1.2281  0.8973  1.1182  0.1086  0.0610  -0.1195 312 SER B CB  
10052 O OG  . SER B 303 ? 0.8990  0.5525  0.7930  0.0960  0.0635  -0.1092 312 SER B OG  
10058 N N   . ASN B 304 ? 1.8625  1.6005  1.7591  0.1414  0.0603  -0.1228 313 ASN B N   
10059 C CA  . ASN B 304 ? 1.2178  0.9626  1.1072  0.1590  0.0628  -0.1283 313 ASN B CA  
10060 C C   . ASN B 304 ? 1.1279  0.8926  1.0256  0.1770  0.0675  -0.1143 313 ASN B C   
10061 O O   . ASN B 304 ? 1.2595  1.0424  1.1706  0.1733  0.0666  -0.1021 313 ASN B O   
10062 C CB  . ASN B 304 ? 1.3841  1.1575  1.2782  0.1533  0.0590  -0.1364 313 ASN B CB  
10063 C CG  . ASN B 304 ? 1.6157  1.3711  1.4983  0.1410  0.0537  -0.1529 313 ASN B CG  
10064 O OD1 . ASN B 304 ? 1.7444  1.4808  1.6274  0.1245  0.0504  -0.1557 313 ASN B OD1 
10065 N ND2 . ASN B 304 ? 1.8526  1.6157  1.7253  0.1486  0.0527  -0.1636 313 ASN B ND2 
10072 N N   . PRO B 305 ? 1.2753  1.0368  1.1646  0.1971  0.0726  -0.1157 314 PRO B N   
10073 C CA  . PRO B 305 ? 1.2850  1.0689  1.1847  0.2146  0.0771  -0.1019 314 PRO B CA  
10074 C C   . PRO B 305 ? 1.3672  1.1978  1.2876  0.2109  0.0755  -0.0956 314 PRO B C   
10075 O O   . PRO B 305 ? 1.1655  1.0109  1.0878  0.2038  0.0740  -0.1027 314 PRO B O   
10076 C CB  . PRO B 305 ? 1.1801  0.9490  1.0646  0.2369  0.0840  -0.1068 314 PRO B CB  
10077 C CG  . PRO B 305 ? 1.1048  0.8561  0.9730  0.2296  0.0817  -0.1247 314 PRO B CG  
10078 C CD  . PRO B 305 ? 1.1263  0.8647  0.9956  0.2052  0.0744  -0.1304 314 PRO B CD  
10086 N N   . SER B 306 ? 1.1544  1.0076  1.0894  0.2177  0.0760  -0.0819 315 SER B N   
10087 C CA  . SER B 306 ? 0.9684  0.8617  0.9242  0.2099  0.0730  -0.0752 315 SER B CA  
10088 C C   . SER B 306 ? 0.9298  0.8481  0.8927  0.2163  0.0771  -0.0770 315 SER B C   
10089 O O   . SER B 306 ? 1.0556  0.9762  1.0156  0.2343  0.0836  -0.0755 315 SER B O   
10090 C CB  . SER B 306 ? 0.8337  0.7448  0.8020  0.2167  0.0716  -0.0615 315 SER B CB  
10091 O OG  . SER B 306 ? 1.5213  1.4690  1.5090  0.2085  0.0680  -0.0563 315 SER B OG  
10097 N N   . VAL B 307 ? 0.8930  0.8292  0.8641  0.2022  0.0744  -0.0795 316 VAL B N   
10098 C CA  . VAL B 307 ? 0.8992  0.8621  0.8797  0.2063  0.0790  -0.0781 316 VAL B CA  
10099 C C   . VAL B 307 ? 1.0706  1.0655  1.0732  0.2107  0.0801  -0.0655 316 VAL B C   
10100 O O   . VAL B 307 ? 1.2511  1.2651  1.2619  0.2229  0.0868  -0.0606 316 VAL B O   
10101 C CB  . VAL B 307 ? 1.0198  0.9881  1.0006  0.1904  0.0759  -0.0839 316 VAL B CB  
10102 C CG1 . VAL B 307 ? 0.8455  0.8381  0.8343  0.1937  0.0815  -0.0816 316 VAL B CG1 
10103 C CG2 . VAL B 307 ? 1.5738  1.5148  1.5356  0.1854  0.0731  -0.0960 316 VAL B CG2 
10113 N N   . ARG B 308 ? 1.1760  1.1782  1.1885  0.2013  0.0736  -0.0598 317 ARG B N   
10114 C CA  . ARG B 308 ? 0.9758  1.0098  1.0096  0.2037  0.0722  -0.0490 317 ARG B CA  
10115 C C   . ARG B 308 ? 1.0087  1.0476  1.0443  0.2249  0.0772  -0.0423 317 ARG B C   
10116 O O   . ARG B 308 ? 1.2079  1.2757  1.2599  0.2334  0.0820  -0.0356 317 ARG B O   
10117 C CB  . ARG B 308 ? 0.7842  0.8195  0.8215  0.1909  0.0630  -0.0463 317 ARG B CB  
10118 C CG  . ARG B 308 ? 0.7618  0.8281  0.8184  0.1890  0.0567  -0.0369 317 ARG B CG  
10119 C CD  . ARG B 308 ? 0.9387  1.0362  1.0163  0.1771  0.0547  -0.0352 317 ARG B CD  
10120 N NE  . ARG B 308 ? 0.7940  0.9083  0.8811  0.1665  0.0447  -0.0323 317 ARG B NE  
10121 C CZ  . ARG B 308 ? 0.9085  1.0529  1.0134  0.1703  0.0397  -0.0247 317 ARG B CZ  
10122 N NH1 . ARG B 308 ? 1.1789  1.3423  1.2963  0.1852  0.0445  -0.0176 317 ARG B NH1 
10123 N NH2 . ARG B 308 ? 0.8764  1.0346  0.9869  0.1598  0.0294  -0.0242 317 ARG B NH2 
10137 N N   . GLU B 309 ? 0.9628  0.9724  0.9812  0.2346  0.0774  -0.0437 318 GLU B N   
10138 C CA  . GLU B 309 ? 1.1593  1.1709  1.1774  0.2571  0.0827  -0.0367 318 GLU B CA  
10139 C C   . GLU B 309 ? 0.9240  0.9399  0.9392  0.2722  0.0929  -0.0390 318 GLU B C   
10140 O O   . GLU B 309 ? 1.3847  1.4259  1.4128  0.2887  0.0985  -0.0300 318 GLU B O   
10141 C CB  . GLU B 309 ? 0.6286  0.6003  0.6254  0.2636  0.0820  -0.0383 318 GLU B CB  
10144 N N   . PHE B 310 ? 0.7953  0.7903  0.7943  0.2674  0.0955  -0.0506 319 PHE B N   
10145 C CA  . PHE B 310 ? 1.5700  1.5682  1.5623  0.2821  0.1052  -0.0536 319 PHE B CA  
10146 C C   . PHE B 310 ? 1.2438  1.2858  1.2608  0.2800  0.1093  -0.0451 319 PHE B C   
10147 O O   . PHE B 310 ? 1.4432  1.5053  1.4675  0.2974  0.1186  -0.0382 319 PHE B O   
10148 C CB  . PHE B 310 ? 0.6378  0.6041  0.6058  0.2755  0.1044  -0.0687 319 PHE B CB  
10149 C CG  . PHE B 310 ? 0.7421  0.7072  0.6967  0.2899  0.1132  -0.0743 319 PHE B CG  
10150 C CD1 . PHE B 310 ? 0.6849  0.6747  0.6476  0.2850  0.1165  -0.0732 319 PHE B CD1 
10151 C CD2 . PHE B 310 ? 1.0367  0.9718  0.9669  0.3085  0.1184  -0.0815 319 PHE B CD2 
10152 C CE1 . PHE B 310 ? 0.6921  0.6802  0.6387  0.3002  0.1253  -0.0781 319 PHE B CE1 
10153 C CE2 . PHE B 310 ? 1.5026  1.4348  1.4158  0.3236  0.1266  -0.0880 319 PHE B CE2 
10154 C CZ  . PHE B 310 ? 0.6910  0.6512  0.6125  0.3197  0.1301  -0.0858 319 PHE B CZ  
10164 N N   . VAL B 311 ? 0.8421  0.8988  0.8725  0.2590  0.1035  -0.0447 320 VAL B N   
10165 C CA  . VAL B 311 ? 0.9283  1.0204  0.9802  0.2550  0.1085  -0.0375 320 VAL B CA  
10166 C C   . VAL B 311 ? 0.9386  1.0667  1.0175  0.2614  0.1097  -0.0241 320 VAL B C   
10167 O O   . VAL B 311 ? 0.8888  1.0441  0.9820  0.2718  0.1191  -0.0161 320 VAL B O   
10168 C CB  . VAL B 311 ? 0.7241  0.8197  0.7826  0.2317  0.1025  -0.0403 320 VAL B CB  
10169 C CG1 . VAL B 311 ? 1.0391  1.1689  1.1223  0.2259  0.1072  -0.0312 320 VAL B CG1 
10170 C CG2 . VAL B 311 ? 1.0589  1.1296  1.0947  0.2287  0.1036  -0.0515 320 VAL B CG2 
10180 N N   . LEU B 312 ? 0.9692  1.0986  1.0542  0.2577  0.1007  -0.0210 321 LEU B N   
10181 C CA  . LEU B 312 ? 1.1014  1.2683  1.2123  0.2644  0.1000  -0.0086 321 LEU B CA  
10182 C C   . LEU B 312 ? 1.4261  1.5993  1.5349  0.2917  0.1105  -0.0025 321 LEU B C   
10183 O O   . LEU B 312 ? 1.6748  1.8881  1.8087  0.2998  0.1159  0.0087  321 LEU B O   
10184 C CB  . LEU B 312 ? 1.0029  1.1668  1.1148  0.2588  0.0881  -0.0068 321 LEU B CB  
10185 C CG  . LEU B 312 ? 1.3328  1.5050  1.4545  0.2348  0.0768  -0.0088 321 LEU B CG  
10186 C CD1 . LEU B 312 ? 1.3809  1.5418  1.4938  0.2364  0.0674  -0.0073 321 LEU B CD1 
10187 C CD2 . LEU B 312 ? 1.7902  2.0079  1.9445  0.2260  0.0753  -0.0010 321 LEU B CD2 
10199 N N   . SER B 313 ? 1.0283  1.1623  1.1075  0.3059  0.1146  -0.0102 322 SER B N   
10200 C CA  . SER B 313 ? 0.8976  1.0308  0.9701  0.3341  0.1241  -0.0052 322 SER B CA  
10201 C C   . SER B 313 ? 0.8361  0.9879  0.9123  0.3468  0.1377  -0.0027 322 SER B C   
10202 O O   . SER B 313 ? 0.8781  1.0426  0.9564  0.3713  0.1472  0.0048  322 SER B O   
10203 C CB  . SER B 313 ? 0.9478  1.0275  0.9850  0.3441  0.1242  -0.0156 322 SER B CB  
10204 O OG  . SER B 313 ? 0.9707  1.0217  0.9842  0.3426  0.1287  -0.0286 322 SER B OG  
10210 N N   . LYS B 314 ? 1.0706  1.2232  1.1456  0.3329  0.1398  -0.0079 323 LYS B N   
10211 C CA  . LYS B 314 ? 0.8520  1.0153  0.9233  0.3463  0.1537  -0.0063 323 LYS B CA  
10212 C C   . LYS B 314 ? 1.0405  1.2579  1.1491  0.3454  0.1607  0.0096  323 LYS B C   
10213 O O   . LYS B 314 ? 1.2073  1.4404  1.3167  0.3602  0.1747  0.0149  323 LYS B O   
10214 C CB  . LYS B 314 ? 0.6468  0.7851  0.6970  0.3335  0.1530  -0.0187 323 LYS B CB  
10215 C CG  . LYS B 314 ? 0.8820  0.9703  0.8939  0.3388  0.1497  -0.0350 323 LYS B CG  
10216 C CD  . LYS B 314 ? 1.2960  1.3717  1.2836  0.3635  0.1618  -0.0396 323 LYS B CD  
10225 N N   . GLY B 315 ? 1.3074  1.5535  1.4464  0.3274  0.1514  0.0170  324 GLY B N   
10226 C CA  . GLY B 315 ? 1.1072  1.4055  1.2851  0.3223  0.1564  0.0314  324 GLY B CA  
10227 C C   . GLY B 315 ? 1.0710  1.3767  1.2540  0.3105  0.1647  0.0326  324 GLY B C   
10228 O O   . GLY B 315 ? 1.4122  1.7531  1.6166  0.3175  0.1772  0.0448  324 GLY B O   
10232 N N   . ASP B 316 ? 1.0370  1.3098  1.1993  0.2948  0.1594  0.0210  325 ASP B N   
10233 C CA  . ASP B 316 ? 0.8592  1.1293  1.0164  0.2880  0.1680  0.0208  325 ASP B CA  
10234 C C   . ASP B 316 ? 0.8447  1.1202  1.0196  0.2587  0.1595  0.0209  325 ASP B C   
10235 O O   . ASP B 316 ? 1.1392  1.3882  1.3003  0.2453  0.1475  0.0103  325 ASP B O   
10236 C CB  . ASP B 316 ? 0.8915  1.1189  1.0070  0.2974  0.1692  0.0067  325 ASP B CB  
10237 C CG  . ASP B 316 ? 0.9309  1.1569  1.0373  0.2957  0.1790  0.0073  325 ASP B CG  
10238 O OD1 . ASP B 316 ? 0.9018  1.1445  1.0290  0.2779  0.1797  0.0144  325 ASP B OD1 
10239 O OD2 . ASP B 316 ? 0.8451  1.0514  0.9215  0.3123  0.1855  0.0005  325 ASP B OD2 
10244 N N   . ALA B 317 ? 0.8738  1.1831  1.0797  0.2486  0.1661  0.0331  326 ALA B N   
10245 C CA  . ALA B 317 ? 1.0903  1.4010  1.3114  0.2213  0.1588  0.0326  326 ALA B CA  
10246 C C   . ALA B 317 ? 1.0303  1.3072  1.2250  0.2147  0.1600  0.0241  326 ALA B C   
10247 O O   . ALA B 317 ? 0.4754  0.7372  0.6686  0.1955  0.1504  0.0179  326 ALA B O   
10248 C CB  . ALA B 317 ? 0.4799  0.8302  0.7384  0.2116  0.1675  0.0474  326 ALA B CB  
10254 N N   . GLY B 318 ? 0.7616  1.0276  0.9346  0.2316  0.1717  0.0238  327 GLY B N   
10255 C CA  . GLY B 318 ? 0.6188  0.8550  0.7650  0.2279  0.1718  0.0156  327 GLY B CA  
10256 C C   . GLY B 318 ? 0.9700  1.1737  1.0914  0.2248  0.1575  -0.0002 327 GLY B C   
10257 O O   . GLY B 318 ? 0.6476  0.8347  0.7628  0.2093  0.1502  -0.0062 327 GLY B O   
10261 N N   . LEU B 319 ? 1.0247  1.2187  1.1329  0.2391  0.1538  -0.0062 328 LEU B N   
10262 C CA  . LEU B 319 ? 0.8135  0.9771  0.9014  0.2337  0.1408  -0.0197 328 LEU B CA  
10263 C C   . LEU B 319 ? 0.7390  0.9068  0.8444  0.2139  0.1291  -0.0193 328 LEU B C   
10264 O O   . LEU B 319 ? 0.8353  0.9827  0.9293  0.2016  0.1203  -0.0277 328 LEU B O   
10265 C CB  . LEU B 319 ? 1.0649  1.2140  1.1364  0.2513  0.1395  -0.0253 328 LEU B CB  
10266 C CG  . LEU B 319 ? 1.1380  1.2647  1.1781  0.2681  0.1452  -0.0343 328 LEU B CG  
10267 C CD1 . LEU B 319 ? 1.1156  1.2267  1.1422  0.2857  0.1447  -0.0388 328 LEU B CD1 
10268 C CD2 . LEU B 319 ? 0.7986  0.8998  0.8178  0.2566  0.1378  -0.0465 328 LEU B CD2 
10280 N N   . ARG B 320 ? 0.9142  1.1108  1.0478  0.2104  0.1288  -0.0096 329 ARG B N   
10281 C CA  . ARG B 320 ? 0.8079  1.0079  0.9547  0.1920  0.1163  -0.0108 329 ARG B CA  
10282 C C   . ARG B 320 ? 0.8595  1.0529  1.0084  0.1729  0.1152  -0.0127 329 ARG B C   
10283 O O   . ARG B 320 ? 0.8714  1.0476  1.0117  0.1606  0.1053  -0.0201 329 ARG B O   
10284 C CB  . ARG B 320 ? 0.6007  0.8368  0.7785  0.1913  0.1146  -0.0006 329 ARG B CB  
10285 C CG  . ARG B 320 ? 0.8475  1.0887  1.0234  0.2089  0.1121  0.0013  329 ARG B CG  
10286 C CD  . ARG B 320 ? 1.0708  1.3469  1.2761  0.2035  0.1037  0.0092  329 ARG B CD  
10287 N NE  . ARG B 320 ? 0.8576  1.1731  1.0960  0.1968  0.1098  0.0200  329 ARG B NE  
10288 C CZ  . ARG B 320 ? 0.9757  1.3161  1.2274  0.2126  0.1227  0.0302  329 ARG B CZ  
10289 N NH1 . ARG B 320 ? 1.1644  1.4919  1.3961  0.2373  0.1305  0.0297  329 ARG B NH1 
10290 N NH2 . ARG B 320 ? 1.2093  1.5867  1.4940  0.2032  0.1282  0.0407  329 ARG B NH2 
10304 N N   . GLU B 321 ? 1.1228  1.3283  1.2818  0.1712  0.1263  -0.0053 330 GLU B N   
10305 C CA  . GLU B 321 ? 0.8381  1.0346  0.9988  0.1541  0.1265  -0.0059 330 GLU B CA  
10306 C C   . GLU B 321 ? 0.7325  0.8971  0.8633  0.1546  0.1236  -0.0164 330 GLU B C   
10307 O O   . GLU B 321 ? 0.7959  0.9470  0.9232  0.1405  0.1171  -0.0212 330 GLU B O   
10308 C CB  . GLU B 321 ? 0.8467  1.0602  1.0228  0.1540  0.1411  0.0059  330 GLU B CB  
10309 C CG  . GLU B 321 ? 1.0836  1.3293  1.2964  0.1421  0.1422  0.0163  330 GLU B CG  
10316 N N   . ALA B 322 ? 0.9660  1.1188  1.0747  0.1709  0.1274  -0.0208 331 ALA B N   
10317 C CA  . ALA B 322 ? 0.9519  1.0793  1.0348  0.1707  0.1236  -0.0308 331 ALA B CA  
10318 C C   . ALA B 322 ? 0.9997  1.1117  1.0751  0.1632  0.1105  -0.0401 331 ALA B C   
10319 O O   . ALA B 322 ? 1.3661  1.4638  1.4319  0.1540  0.1054  -0.0458 331 ALA B O   
10320 C CB  . ALA B 322 ? 0.9060  1.0258  0.9669  0.1889  0.1296  -0.0346 331 ALA B CB  
10326 N N   . TYR B 323 ? 1.2736  1.3887  1.3529  0.1682  0.1058  -0.0406 332 TYR B N   
10327 C CA  . TYR B 323 ? 1.0606  1.1628  1.1348  0.1609  0.0944  -0.0467 332 TYR B CA  
10328 C C   . TYR B 323 ? 0.9648  1.0723  1.0516  0.1436  0.0883  -0.0453 332 TYR B C   
10329 O O   . TYR B 323 ? 1.0895  1.1819  1.1661  0.1349  0.0817  -0.0513 332 TYR B O   
10330 C CB  . TYR B 323 ? 0.5442  0.6512  0.6222  0.1713  0.0921  -0.0445 332 TYR B CB  
10331 C CG  . TYR B 323 ? 0.7403  0.8369  0.8151  0.1646  0.0814  -0.0476 332 TYR B CG  
10332 C CD1 . TYR B 323 ? 0.8104  0.8807  0.8647  0.1674  0.0777  -0.0553 332 TYR B CD1 
10333 C CD2 . TYR B 323 ? 0.9079  1.0205  0.9994  0.1547  0.0748  -0.0431 332 TYR B CD2 
10334 C CE1 . TYR B 323 ? 0.5718  0.6317  0.6222  0.1612  0.0694  -0.0565 332 TYR B CE1 
10335 C CE2 . TYR B 323 ? 0.8907  0.9938  0.9762  0.1499  0.0653  -0.0454 332 TYR B CE2 
10336 C CZ  . TYR B 323 ? 0.6726  0.7493  0.7376  0.1538  0.0637  -0.0512 332 TYR B CZ  
10337 O OH  . TYR B 323 ? 0.4753  0.5423  0.5339  0.1494  0.0562  -0.0517 332 TYR B OH  
10347 N N   . ASP B 324 ? 0.6967  0.8262  0.8059  0.1383  0.0907  -0.0374 333 ASP B N   
10348 C CA  . ASP B 324 ? 0.7486  0.8825  0.8696  0.1211  0.0844  -0.0373 333 ASP B CA  
10349 C C   . ASP B 324 ? 0.8314  0.9475  0.9411  0.1125  0.0865  -0.0413 333 ASP B C   
10350 O O   . ASP B 324 ? 0.8447  0.9518  0.9514  0.1008  0.0795  -0.0458 333 ASP B O   
10351 C CB  . ASP B 324 ? 1.2038  1.3655  1.3529  0.1155  0.0874  -0.0284 333 ASP B CB  
10352 C CG  . ASP B 324 ? 1.4388  1.6235  1.6037  0.1193  0.0806  -0.0246 333 ASP B CG  
10353 O OD1 . ASP B 324 ? 1.1212  1.2973  1.2756  0.1212  0.0712  -0.0293 333 ASP B OD1 
10354 O OD2 . ASP B 324 ? 1.7176  1.9307  1.9064  0.1209  0.0853  -0.0158 333 ASP B OD2 
10359 N N   . ALA B 325 ? 0.7295  0.8404  0.8310  0.1198  0.0962  -0.0396 334 ALA B N   
10360 C CA  . ALA B 325 ? 1.0018  1.0978  1.0926  0.1145  0.0995  -0.0416 334 ALA B CA  
10361 C C   . ALA B 325 ? 1.5534  1.6313  1.6252  0.1132  0.0919  -0.0507 334 ALA B C   
10362 O O   . ALA B 325 ? 0.9650  1.0327  1.0330  0.1037  0.0889  -0.0535 334 ALA B O   
10363 C CB  . ALA B 325 ? 0.9169  1.0138  1.0008  0.1260  0.1113  -0.0369 334 ALA B CB  
10369 N N   . CYS B 326 ? 1.4938  1.5674  1.5545  0.1221  0.0888  -0.0553 335 CYS B N   
10370 C CA  . CYS B 326 ? 0.8906  0.9493  0.9365  0.1193  0.0818  -0.0630 335 CYS B CA  
10371 C C   . CYS B 326 ? 0.9488  1.0060  0.9995  0.1091  0.0734  -0.0642 335 CYS B C   
10372 O O   . CYS B 326 ? 0.7881  0.8350  0.8298  0.1030  0.0697  -0.0683 335 CYS B O   
10373 C CB  . CYS B 326 ? 0.7029  0.7552  0.7376  0.1286  0.0799  -0.0677 335 CYS B CB  
10374 S SG  . CYS B 326 ? 0.7270  0.7796  0.7502  0.1431  0.0875  -0.0693 335 CYS B SG  
10380 N N   . VAL B 327 ? 0.8713  0.9406  0.9355  0.1081  0.0704  -0.0604 336 VAL B N   
10381 C CA  . VAL B 327 ? 0.8795  0.9495  0.9469  0.0988  0.0617  -0.0616 336 VAL B CA  
10382 C C   . VAL B 327 ? 0.9522  1.0195  1.0223  0.0873  0.0620  -0.0626 336 VAL B C   
10383 O O   . VAL B 327 ? 0.8902  0.9475  0.9512  0.0806  0.0567  -0.0670 336 VAL B O   
10384 C CB  . VAL B 327 ? 0.8304  0.9184  0.9128  0.1015  0.0578  -0.0567 336 VAL B CB  
10385 C CG1 . VAL B 327 ? 0.5578  0.6503  0.6427  0.0925  0.0469  -0.0580 336 VAL B CG1 
10386 C CG2 . VAL B 327 ? 0.7172  0.8026  0.7937  0.1151  0.0590  -0.0558 336 VAL B CG2 
10396 N N   . LYS B 328 ? 1.0056  1.0796  1.0867  0.0856  0.0693  -0.0582 337 LYS B N   
10397 C CA  . LYS B 328 ? 0.8511  0.9184  0.9349  0.0744  0.0710  -0.0587 337 LYS B CA  
10398 C C   . LYS B 328 ? 0.8517  0.8988  0.9161  0.0752  0.0730  -0.0634 337 LYS B C   
10399 O O   . LYS B 328 ? 1.0123  1.0481  1.0704  0.0670  0.0695  -0.0676 337 LYS B O   
10400 C CB  . LYS B 328 ? 1.4268  1.5027  1.5250  0.0740  0.0811  -0.0512 337 LYS B CB  
10403 N N   . ALA B 329 ? 0.8762  0.9197  0.9299  0.0857  0.0778  -0.0633 338 ALA B N   
10404 C CA  . ALA B 329 ? 0.8714  0.9012  0.9087  0.0878  0.0795  -0.0669 338 ALA B CA  
10405 C C   . ALA B 329 ? 0.7180  0.7414  0.7460  0.0840  0.0715  -0.0726 338 ALA B C   
10406 O O   . ALA B 329 ? 0.6466  0.6594  0.6653  0.0809  0.0717  -0.0752 338 ALA B O   
10407 C CB  . ALA B 329 ? 1.0055  1.0371  1.0344  0.0991  0.0842  -0.0665 338 ALA B CB  
10413 N N   . LEU B 330 ? 0.9875  1.0162  1.0171  0.0851  0.0654  -0.0736 339 LEU B N   
10414 C CA  . LEU B 330 ? 0.8143  0.8368  0.8346  0.0819  0.0592  -0.0772 339 LEU B CA  
10415 C C   . LEU B 330 ? 0.9469  0.9661  0.9665  0.0735  0.0547  -0.0790 339 LEU B C   
10416 O O   . LEU B 330 ? 1.1156  1.1251  1.1231  0.0714  0.0542  -0.0822 339 LEU B O   
10417 C CB  . LEU B 330 ? 0.6285  0.6550  0.6503  0.0854  0.0544  -0.0764 339 LEU B CB  
10418 C CG  . LEU B 330 ? 0.6490  0.6723  0.6655  0.0922  0.0570  -0.0777 339 LEU B CG  
10419 C CD1 . LEU B 330 ? 0.6081  0.6297  0.6247  0.0961  0.0535  -0.0769 339 LEU B CD1 
10420 C CD2 . LEU B 330 ? 0.9393  0.9555  0.9452  0.0896  0.0569  -0.0807 339 LEU B CD2 
10432 N N   . VAL B 331 ? 1.0699  1.0977  1.1022  0.0686  0.0518  -0.0775 340 VAL B N   
10433 C CA  . VAL B 331 ? 1.2162  1.2408  1.2468  0.0593  0.0457  -0.0812 340 VAL B CA  
10434 C C   . VAL B 331 ? 0.9184  0.9261  0.9392  0.0556  0.0508  -0.0846 340 VAL B C   
10435 O O   . VAL B 331 ? 0.8050  0.8015  0.8121  0.0523  0.0474  -0.0897 340 VAL B O   
10436 C CB  . VAL B 331 ? 1.2515  1.2924  1.3012  0.0534  0.0412  -0.0788 340 VAL B CB  
10437 C CG1 . VAL B 331 ? 0.9059  0.9434  0.9540  0.0415  0.0335  -0.0846 340 VAL B CG1 
10438 C CG2 . VAL B 331 ? 1.4415  1.4978  1.4977  0.0602  0.0364  -0.0749 340 VAL B CG2 
10448 N N   . SER B 332 ? 0.7216  0.7257  0.7457  0.0587  0.0601  -0.0812 341 SER B N   
10449 C CA  . SER B 332 ? 0.9383  0.9243  0.9521  0.0578  0.0665  -0.0829 341 SER B CA  
10450 C C   . SER B 332 ? 0.9678  0.9447  0.9630  0.0637  0.0669  -0.0862 341 SER B C   
10451 O O   . SER B 332 ? 1.1887  1.1499  1.1709  0.0619  0.0677  -0.0904 341 SER B O   
10452 C CB  . SER B 332 ? 1.6695  1.6558  1.6887  0.0635  0.0770  -0.0765 341 SER B CB  
10453 O OG  . SER B 332 ? 1.8148  1.8120  1.8525  0.0585  0.0783  -0.0719 341 SER B OG  
10459 N N   . LEU B 333 ? 0.9447  0.9312  0.9386  0.0707  0.0664  -0.0845 342 LEU B N   
10460 C CA  . LEU B 333 ? 0.7970  0.7805  0.7777  0.0757  0.0672  -0.0862 342 LEU B CA  
10461 C C   . LEU B 333 ? 0.4850  0.4656  0.4573  0.0717  0.0606  -0.0897 342 LEU B C   
10462 O O   . LEU B 333 ? 0.6206  0.5934  0.5793  0.0738  0.0624  -0.0918 342 LEU B O   
10463 C CB  . LEU B 333 ? 0.8141  0.8089  0.7984  0.0815  0.0679  -0.0838 342 LEU B CB  
10464 C CG  . LEU B 333 ? 0.7148  0.7125  0.7007  0.0886  0.0748  -0.0811 342 LEU B CG  
10465 C CD1 . LEU B 333 ? 0.8547  0.8635  0.8471  0.0925  0.0737  -0.0801 342 LEU B CD1 
10466 C CD2 . LEU B 333 ? 0.8294  0.8261  0.8054  0.0934  0.0779  -0.0816 342 LEU B CD2 
10478 N N   . ARG B 334 ? 0.5421  0.5293  0.5209  0.0672  0.0533  -0.0898 343 ARG B N   
10479 C CA  . ARG B 334 ? 0.5336  0.5180  0.5013  0.0648  0.0472  -0.0926 343 ARG B CA  
10480 C C   . ARG B 334 ? 0.7543  0.7257  0.7122  0.0596  0.0456  -0.0986 343 ARG B C   
10481 O O   . ARG B 334 ? 1.1620  1.1261  1.1034  0.0604  0.0436  -0.1022 343 ARG B O   
10482 C CB  . ARG B 334 ? 0.9669  0.9632  0.9435  0.0634  0.0396  -0.0901 343 ARG B CB  
10483 C CG  . ARG B 334 ? 1.3805  1.3833  1.3633  0.0692  0.0422  -0.0853 343 ARG B CG  
10484 C CD  . ARG B 334 ? 1.2978  1.2989  1.2707  0.0715  0.0407  -0.0832 343 ARG B CD  
10485 N NE  . ARG B 334 ? 1.5864  1.5879  1.5620  0.0748  0.0448  -0.0806 343 ARG B NE  
10486 C CZ  . ARG B 334 ? 1.0273  1.0317  1.0117  0.0774  0.0443  -0.0786 343 ARG B CZ  
10487 N NH1 . ARG B 334 ? 0.9486  0.9588  0.9418  0.0786  0.0410  -0.0773 343 ARG B NH1 
10488 N NH2 . ARG B 334 ? 1.1823  1.1840  1.1666  0.0788  0.0471  -0.0781 343 ARG B NH2 
10502 N N   . SER B 335 ? 0.9244  0.8918  0.8914  0.0538  0.0466  -0.1000 344 SER B N   
10503 C CA  . SER B 335 ? 0.9328  0.8837  0.8903  0.0469  0.0448  -0.1071 344 SER B CA  
10504 C C   . SER B 335 ? 0.9135  0.8445  0.8547  0.0531  0.0544  -0.1088 344 SER B C   
10505 O O   . SER B 335 ? 1.0749  0.9899  0.9975  0.0528  0.0533  -0.1154 344 SER B O   
10506 C CB  . SER B 335 ? 0.8036  0.7572  0.7792  0.0366  0.0430  -0.1071 344 SER B CB  
10507 O OG  . SER B 335 ? 1.0941  1.0672  1.0828  0.0309  0.0327  -0.1068 344 SER B OG  
10513 N N   . TYR B 336 ? 0.7341  0.6668  0.6798  0.0607  0.0637  -0.1028 345 TYR B N   
10514 C CA  . TYR B 336 ? 1.0867  1.0034  1.0170  0.0689  0.0727  -0.1032 345 TYR B CA  
10515 C C   . TYR B 336 ? 1.6087  1.5275  1.5235  0.0757  0.0723  -0.1048 345 TYR B C   
10516 O O   . TYR B 336 ? 1.1842  1.0862  1.0804  0.0796  0.0756  -0.1091 345 TYR B O   
10517 C CB  . TYR B 336 ? 1.1284  1.0507  1.0657  0.0774  0.0817  -0.0959 345 TYR B CB  
10518 C CG  . TYR B 336 ? 1.2558  1.1574  1.1790  0.0848  0.0914  -0.0957 345 TYR B CG  
10519 C CD1 . TYR B 336 ? 1.5568  1.4369  1.4793  0.0791  0.0951  -0.0970 345 TYR B CD1 
10520 C CD2 . TYR B 336 ? 1.3836  1.2863  1.2944  0.0971  0.0972  -0.0941 345 TYR B CD2 
10521 C CE1 . TYR B 336 ? 1.5149  1.3713  1.4227  0.0864  0.1046  -0.0966 345 TYR B CE1 
10522 C CE2 . TYR B 336 ? 0.8172  0.6998  0.7138  0.1061  0.1067  -0.0933 345 TYR B CE2 
10523 C CZ  . TYR B 336 ? 1.2907  1.1478  1.1845  0.1010  0.1105  -0.0948 345 TYR B CZ  
10524 O OH  . TYR B 336 ? 1.4494  1.2808  1.3276  0.1101  0.1207  -0.0938 345 TYR B OH  
10534 N N   . HIS B 337 ? 0.8869  0.8247  0.8084  0.0767  0.0683  -0.1013 346 HIS B N   
10535 C CA  . HIS B 337 ? 1.0267  0.9684  0.9358  0.0817  0.0685  -0.1011 346 HIS B CA  
10536 C C   . HIS B 337 ? 0.9290  0.8572  0.8204  0.0789  0.0638  -0.1080 346 HIS B C   
10537 O O   . HIS B 337 ? 0.9634  0.8821  0.8362  0.0856  0.0686  -0.1103 346 HIS B O   
10538 C CB  . HIS B 337 ? 1.2127  1.1727  1.1329  0.0801  0.0640  -0.0963 346 HIS B CB  
10539 C CG  . HIS B 337 ? 1.0237  0.9908  0.9363  0.0850  0.0669  -0.0931 346 HIS B CG  
10540 N ND1 . HIS B 337 ? 1.1661  1.1472  1.0885  0.0873  0.0702  -0.0878 346 HIS B ND1 
10541 C CD2 . HIS B 337 ? 1.2808  1.2437  1.1768  0.0875  0.0673  -0.0941 346 HIS B CD2 
10542 C CE1 . HIS B 337 ? 1.3857  1.3719  1.3007  0.0898  0.0730  -0.0848 346 HIS B CE1 
10543 N NE2 . HIS B 337 ? 1.5122  1.4876  1.4104  0.0910  0.0720  -0.0880 346 HIS B NE2 
10551 N N   . LEU B 338 ? 0.7396  0.6685  0.6357  0.0698  0.0543  -0.1116 347 LEU B N   
10552 C CA  . LEU B 338 ? 0.9524  0.8696  0.8309  0.0663  0.0477  -0.1198 347 LEU B CA  
10553 C C   . LEU B 338 ? 1.1940  1.0854  1.0569  0.0669  0.0527  -0.1273 347 LEU B C   
10554 O O   . LEU B 338 ? 1.0719  0.9492  0.9114  0.0700  0.0521  -0.1340 347 LEU B O   
10555 C CB  . LEU B 338 ? 1.0184  0.9450  0.9091  0.0557  0.0358  -0.1222 347 LEU B CB  
10556 C CG  . LEU B 338 ? 0.7669  0.7139  0.6637  0.0577  0.0298  -0.1161 347 LEU B CG  
10557 C CD1 . LEU B 338 ? 0.8990  0.8609  0.8161  0.0505  0.0213  -0.1145 347 LEU B CD1 
10558 C CD2 . LEU B 338 ? 0.6685  0.6125  0.5421  0.0608  0.0245  -0.1196 347 LEU B CD2 
10570 N N   . GLN B 339 ? 1.1754  1.0581  1.0487  0.0649  0.0585  -0.1260 348 GLN B N   
10571 C CA  . GLN B 339 ? 0.9430  0.7966  0.7989  0.0668  0.0646  -0.1324 348 GLN B CA  
10572 C C   . GLN B 339 ? 1.0404  0.8890  0.8775  0.0824  0.0744  -0.1302 348 GLN B C   
10573 O O   . GLN B 339 ? 0.9865  0.8143  0.7988  0.0869  0.0762  -0.1378 348 GLN B O   
10574 C CB  . GLN B 339 ? 1.1775  1.0211  1.0470  0.0635  0.0712  -0.1290 348 GLN B CB  
10575 C CG  . GLN B 339 ? 1.0676  0.9110  0.9539  0.0466  0.0631  -0.1325 348 GLN B CG  
10576 C CD  . GLN B 339 ? 1.1081  0.9465  1.0108  0.0440  0.0713  -0.1258 348 GLN B CD  
10577 O OE1 . GLN B 339 ? 1.5720  1.3878  1.4647  0.0503  0.0821  -0.1242 348 GLN B OE1 
10578 N NE2 . GLN B 339 ? 0.8941  0.7537  0.8211  0.0362  0.0672  -0.1208 348 GLN B NE2 
10587 N N   . ILE B 340 ? 0.7303  0.6003  0.5789  0.0905  0.0800  -0.1204 349 ILE B N   
10588 C CA  . ILE B 340 ? 0.7370  0.6099  0.5737  0.1052  0.0898  -0.1163 349 ILE B CA  
10589 C C   . ILE B 340 ? 0.8708  0.7442  0.6883  0.1091  0.0880  -0.1196 349 ILE B C   
10590 O O   . ILE B 340 ? 0.9121  0.7717  0.7080  0.1199  0.0953  -0.1222 349 ILE B O   
10591 C CB  . ILE B 340 ? 0.6842  0.5848  0.5409  0.1092  0.0929  -0.1062 349 ILE B CB  
10592 C CG1 . ILE B 340 ? 1.4110  1.3101  1.2810  0.1095  0.0968  -0.1024 349 ILE B CG1 
10593 C CG2 . ILE B 340 ? 0.6803  0.5942  0.5294  0.1211  0.1000  -0.1013 349 ILE B CG2 
10594 C CD1 . ILE B 340 ? 1.2487  1.1212  1.1054  0.1155  0.1049  -0.1046 349 ILE B CD1 
10606 N N   . VAL B 341 ? 0.7122  0.6015  0.5360  0.1021  0.0791  -0.1186 350 VAL B N   
10607 C CA  . VAL B 341 ? 0.6588  0.5495  0.4636  0.1057  0.0770  -0.1204 350 VAL B CA  
10608 C C   . VAL B 341 ? 1.0508  0.9151  0.8293  0.1049  0.0731  -0.1328 350 VAL B C   
10609 O O   . VAL B 341 ? 1.0890  0.9482  0.8437  0.1127  0.0750  -0.1355 350 VAL B O   
10610 C CB  . VAL B 341 ? 0.7711  0.6823  0.5892  0.0984  0.0681  -0.1154 350 VAL B CB  
10611 C CG1 . VAL B 341 ? 1.4506  1.3630  1.2484  0.1016  0.0646  -0.1165 350 VAL B CG1 
10612 C CG2 . VAL B 341 ? 0.9643  0.8966  0.8025  0.1004  0.0732  -0.1049 350 VAL B CG2 
10622 N N   . THR B 342 ? 1.4374  1.2843  1.2189  0.0951  0.0677  -0.1407 351 THR B N   
10623 C CA  . THR B 342 ? 1.2542  1.0719  1.0099  0.0931  0.0641  -0.1543 351 THR B CA  
10624 C C   . THR B 342 ? 1.1273  0.9213  0.8623  0.1070  0.0777  -0.1562 351 THR B C   
10625 O O   . THR B 342 ? 0.9168  0.6934  0.6217  0.1152  0.0797  -0.1638 351 THR B O   
10626 C CB  . THR B 342 ? 1.1289  0.9359  0.8979  0.0764  0.0550  -0.1614 351 THR B CB  
10627 O OG1 . THR B 342 ? 1.3202  1.1541  1.1103  0.0666  0.0437  -0.1575 351 THR B OG1 
10628 C CG2 . THR B 342 ? 1.2571  1.0356  1.0016  0.0704  0.0483  -0.1770 351 THR B CG2 
10636 N N   . LYS B 343 ? 0.9089  0.7024  0.6583  0.1115  0.0875  -0.1488 352 LYS B N   
10637 C CA  . LYS B 343 ? 0.8756  0.6474  0.6066  0.1268  0.1011  -0.1490 352 LYS B CA  
10638 C C   . LYS B 343 ? 1.1420  0.9313  0.8622  0.1435  0.1096  -0.1423 352 LYS B C   
10639 O O   . LYS B 343 ? 1.0043  0.7744  0.6966  0.1565  0.1170  -0.1472 352 LYS B O   
10640 C CB  . LYS B 343 ? 1.1568  0.9280  0.9068  0.1287  0.1090  -0.1409 352 LYS B CB  
10641 C CG  . LYS B 343 ? 1.6800  1.4268  1.4126  0.1453  0.1233  -0.1396 352 LYS B CG  
10648 N N   . TYR B 344 ? 1.5193  1.3446  1.2603  0.1427  0.1083  -0.1317 353 TYR B N   
10649 C CA  . TYR B 344 ? 0.8548  0.7009  0.5929  0.1575  0.1184  -0.1226 353 TYR B CA  
10650 C C   . TYR B 344 ? 0.8073  0.6656  0.5331  0.1586  0.1157  -0.1220 353 TYR B C   
10651 O O   . TYR B 344 ? 0.9578  0.8309  0.6775  0.1716  0.1258  -0.1148 353 TYR B O   
10652 C CB  . TYR B 344 ? 0.7179  0.5955  0.4869  0.1571  0.1213  -0.1102 353 TYR B CB  
10653 C CG  . TYR B 344 ? 0.9855  0.8532  0.7606  0.1628  0.1277  -0.1084 353 TYR B CG  
10654 C CD1 . TYR B 344 ? 1.3523  1.2138  1.1142  0.1809  0.1404  -0.1054 353 TYR B CD1 
10655 C CD2 . TYR B 344 ? 0.8698  0.7341  0.6624  0.1518  0.1221  -0.1087 353 TYR B CD2 
10656 C CE1 . TYR B 344 ? 1.4225  1.2734  1.1878  0.1880  0.1468  -0.1025 353 TYR B CE1 
10657 C CE2 . TYR B 344 ? 1.4391  1.2930  1.2350  0.1581  0.1290  -0.1057 353 TYR B CE2 
10658 C CZ  . TYR B 344 ? 1.2298  1.0765  1.0116  0.1764  0.1412  -0.1024 353 TYR B CZ  
10659 O OH  . TYR B 344 ? 1.4237  1.2601  1.2074  0.1847  0.1486  -0.0979 353 TYR B OH  
10669 N N   . ILE B 345 ? 0.7108  0.7177  0.9024  0.1327  0.0092  -0.1107 354 ILE B N   
10670 C CA  . ILE B 345 ? 0.8173  0.8584  0.9872  0.1291  -0.0057 -0.1286 354 ILE B CA  
10671 C C   . ILE B 345 ? 0.7207  0.7373  0.9022  0.1305  -0.0065 -0.1717 354 ILE B C   
10672 O O   . ILE B 345 ? 0.8404  0.8667  1.0129  0.1463  -0.0036 -0.1900 354 ILE B O   
10673 C CB  . ILE B 345 ? 1.0663  1.1323  1.2102  0.1083  -0.0247 -0.1181 354 ILE B CB  
10674 C CG1 . ILE B 345 ? 0.9553  1.0551  1.0893  0.1052  -0.0254 -0.0833 354 ILE B CG1 
10675 C CG2 . ILE B 345 ? 1.1284  1.2160  1.2413  0.1086  -0.0350 -0.1350 354 ILE B CG2 
10676 C CD1 . ILE B 345 ? 1.1752  1.2893  1.2851  0.0816  -0.0405 -0.0727 354 ILE B CD1 
10688 N N   . LEU B 346 ? 1.1958  1.1841  1.3999  0.1148  -0.0103 -0.1918 355 LEU B N   
10689 C CA  . LEU B 346 ? 0.9750  0.9575  1.1893  0.1136  -0.0202 -0.2398 355 LEU B CA  
10690 C C   . LEU B 346 ? 0.9176  0.8726  1.1564  0.1282  -0.0020 -0.2660 355 LEU B C   
10691 O O   . LEU B 346 ? 0.8045  0.7709  1.0311  0.1397  -0.0102 -0.2993 355 LEU B O   
10692 C CB  . LEU B 346 ? 1.2280  1.1966  1.4710  0.0926  -0.0291 -0.2595 355 LEU B CB  
10693 C CG  . LEU B 346 ? 1.6011  1.5855  1.8461  0.0933  -0.0513 -0.3101 355 LEU B CG  
10694 C CD1 . LEU B 346 ? 1.9798  1.9886  2.2034  0.0849  -0.0763 -0.3085 355 LEU B CD1 
10695 C CD2 . LEU B 346 ? 1.6401  1.5952  1.9457  0.0836  -0.0402 -0.3531 355 LEU B CD2 
10707 N N   . ILE B 347 ? 0.7989  0.7145  1.0654  0.1316  0.0244  -0.2503 356 ILE B N   
10708 C CA  . ILE B 347 ? 1.0445  0.9229  1.3350  0.1451  0.0454  -0.2764 356 ILE B CA  
10709 C C   . ILE B 347 ? 1.0174  0.9221  1.2755  0.1730  0.0475  -0.2645 356 ILE B C   
10710 O O   . ILE B 347 ? 1.0383  0.9498  1.2886  0.1836  0.0428  -0.3001 356 ILE B O   
10711 C CB  . ILE B 347 ? 0.8773  0.6950  1.2020  0.1427  0.0782  -0.2607 356 ILE B CB  
10712 C CG1 . ILE B 347 ? 0.8776  0.6723  1.2463  0.1121  0.0786  -0.2924 356 ILE B CG1 
10713 C CG2 . ILE B 347 ? 0.9375  0.7091  1.2751  0.1655  0.1073  -0.2714 356 ILE B CG2 
10714 C CD1 . ILE B 347 ? 0.9903  0.7216  1.3932  0.1016  0.1157  -0.2718 356 ILE B CD1 
10726 N N   . PRO B 348 ? 1.2281  1.1552  1.4667  0.1857  0.0525  -0.2184 357 PRO B N   
10727 C CA  . PRO B 348 ? 1.6752  1.6395  1.8901  0.2106  0.0546  -0.2093 357 PRO B CA  
10728 C C   . PRO B 348 ? 1.3070  1.3094  1.4922  0.2091  0.0368  -0.2338 357 PRO B C   
10729 O O   . PRO B 348 ? 1.6762  1.6881  1.8491  0.2305  0.0443  -0.2494 357 PRO B O   
10730 C CB  . PRO B 348 ? 0.8143  0.8149  1.0182  0.2136  0.0526  -0.1612 357 PRO B CB  
10731 C CG  . PRO B 348 ? 1.0121  0.9739  1.2326  0.2059  0.0606  -0.1418 357 PRO B CG  
10732 C CD  . PRO B 348 ? 1.2560  1.1784  1.4962  0.1812  0.0579  -0.1753 357 PRO B CD  
10740 N N   . ALA B 349 ? 1.6393  1.6610  1.8074  0.1883  0.0152  -0.2362 358 ALA B N   
10741 C CA  . ALA B 349 ? 0.9769  1.0286  1.1054  0.1929  0.0009  -0.2547 358 ALA B CA  
10742 C C   . ALA B 349 ? 1.2079  1.2395  1.3378  0.2041  -0.0029 -0.3071 358 ALA B C   
10743 O O   . ALA B 349 ? 0.8918  0.9432  0.9846  0.2217  -0.0062 -0.3238 358 ALA B O   
10744 C CB  . ALA B 349 ? 1.0674  1.1336  1.1743  0.1725  -0.0203 -0.2468 358 ALA B CB  
10750 N N   . SER B 350 ? 1.6492  1.6414  1.8215  0.1946  -0.0004 -0.3355 359 SER B N   
10751 C CA  . SER B 350 ? 1.4957  1.4720  1.6757  0.2034  -0.0050 -0.3924 359 SER B CA  
10752 C C   . SER B 350 ? 1.2446  1.2023  1.4267  0.2281  0.0185  -0.4008 359 SER B C   
10753 O O   . SER B 350 ? 1.0146  0.9678  1.1876  0.2413  0.0137  -0.4477 359 SER B O   
10754 C CB  . SER B 350 ? 1.4312  1.3732  1.6665  0.1805  -0.0067 -0.4259 359 SER B CB  
10755 O OG  . SER B 350 ? 1.3206  1.2139  1.5968  0.1782  0.0249  -0.4118 359 SER B OG  
10761 N N   . GLN B 351 ? 1.5940  1.5467  1.7820  0.2387  0.0413  -0.3573 360 GLN B N   
10762 C CA  . GLN B 351 ? 1.4378  1.3718  1.6301  0.2667  0.0665  -0.3581 360 GLN B CA  
10763 C C   . GLN B 351 ? 1.4349  1.4205  1.5883  0.2903  0.0700  -0.3341 360 GLN B C   
10764 O O   . GLN B 351 ? 1.5743  1.5606  1.7350  0.3137  0.0912  -0.3131 360 GLN B O   
10765 C CB  . GLN B 351 ? 1.5266  1.4173  1.7541  0.2689  0.0913  -0.3274 360 GLN B CB  
10766 C CG  . GLN B 351 ? 1.4292  1.2572  1.7003  0.2474  0.1004  -0.3542 360 GLN B CG  
10767 C CD  . GLN B 351 ? 1.5323  1.3091  1.8275  0.2513  0.1294  -0.3171 360 GLN B CD  
10768 O OE1 . GLN B 351 ? 1.6892  1.3990  2.0184  0.2459  0.1534  -0.3378 360 GLN B OE1 
10769 N NE2 . GLN B 351 ? 2.1986  2.0046  2.4754  0.2611  0.1284  -0.2641 360 GLN B NE2 
10778 N N   . GLN B 352 ? 1.5173  1.5463  1.6305  0.2856  0.0523  -0.3345 361 GLN B N   
10779 C CA  . GLN B 352 ? 1.3427  1.4199  1.4207  0.3040  0.0612  -0.3136 361 GLN B CA  
10780 C C   . GLN B 352 ? 1.4342  1.5093  1.4802  0.3301  0.0661  -0.3539 361 GLN B C   
10781 O O   . GLN B 352 ? 1.4586  1.5659  1.4796  0.3516  0.0819  -0.3430 361 GLN B O   
10782 C CB  . GLN B 352 ? 1.4634  1.5793  1.5102  0.2853  0.0470  -0.2881 361 GLN B CB  
10785 N N   . GLY B 372 ? 2.0213  2.1450  1.9974  0.1221  -0.0538 -0.1584 381 GLY B N   
10786 C CA  . GLY B 372 ? 2.2715  2.3871  2.2604  0.0997  -0.0612 -0.1387 381 GLY B CA  
10787 C C   . GLY B 372 ? 1.7828  1.8748  1.7836  0.0965  -0.0800 -0.1617 381 GLY B C   
10788 O O   . GLY B 372 ? 1.5828  1.6622  1.6226  0.0850  -0.0808 -0.1603 381 GLY B O   
10792 N N   . THR B 373 ? 1.6748  1.7629  1.6410  0.1090  -0.0945 -0.1836 382 THR B N   
10793 C CA  . THR B 373 ? 1.5555  1.6328  1.5415  0.1089  -0.1143 -0.2132 382 THR B CA  
10794 C C   . THR B 373 ? 1.6808  1.7498  1.6487  0.0983  -0.1259 -0.1982 382 THR B C   
10795 O O   . THR B 373 ? 1.4110  1.4733  1.4150  0.0887  -0.1350 -0.2105 382 THR B O   
10796 C CB  . THR B 373 ? 1.3906  1.4750  1.3522  0.1339  -0.1297 -0.2534 382 THR B CB  
10797 O OG1 . THR B 373 ? 1.7260  1.8171  1.6823  0.1475  -0.1153 -0.2601 382 THR B OG1 
10798 C CG2 . THR B 373 ? 0.9834  1.0670  0.9936  0.1315  -0.1467 -0.2954 382 THR B CG2 
10806 N N   . ASP B 374 ? 1.5563  1.6227  1.4706  0.0993  -0.1217 -0.1714 383 ASP B N   
10807 C CA  . ASP B 374 ? 1.1840  1.2352  1.0736  0.0917  -0.1300 -0.1559 383 ASP B CA  
10808 C C   . ASP B 374 ? 0.9902  1.0356  0.9206  0.0662  -0.1249 -0.1379 383 ASP B C   
10809 O O   . ASP B 374 ? 1.0168  1.0497  0.9471  0.0606  -0.1350 -0.1373 383 ASP B O   
10810 C CB  . ASP B 374 ? 1.1138  1.1546  0.9397  0.0948  -0.1176 -0.1283 383 ASP B CB  
10811 C CG  . ASP B 374 ? 1.4119  1.4536  1.1843  0.1253  -0.1193 -0.1425 383 ASP B CG  
10816 N N   . LEU B 375 ? 1.1945  1.2498  1.1578  0.0551  -0.1097 -0.1248 384 LEU B N   
10817 C CA  . LEU B 375 ? 1.0389  1.0897  1.0345  0.0367  -0.1045 -0.1073 384 LEU B CA  
10818 C C   . LEU B 375 ? 1.2469  1.2851  1.2828  0.0357  -0.1104 -0.1275 384 LEU B C   
10819 O O   . LEU B 375 ? 1.1550  1.1816  1.2019  0.0238  -0.1108 -0.1174 384 LEU B O   
10820 C CB  . LEU B 375 ? 0.8285  0.8964  0.8469  0.0353  -0.0890 -0.0927 384 LEU B CB  
10821 C CG  . LEU B 375 ? 0.7262  0.7910  0.7751  0.0262  -0.0831 -0.0763 384 LEU B CG  
10822 C CD1 . LEU B 375 ? 0.7110  0.7724  0.7409  0.0090  -0.0882 -0.0573 384 LEU B CD1 
10823 C CD2 . LEU B 375 ? 0.8357  0.9227  0.9017  0.0346  -0.0704 -0.0638 384 LEU B CD2 
10835 N N   . MET B 376 ? 1.0259  1.0664  1.0870  0.0472  -0.1125 -0.1581 385 MET B N   
10836 C CA  . MET B 376 ? 1.2221  1.2518  1.3322  0.0421  -0.1129 -0.1814 385 MET B CA  
10837 C C   . MET B 376 ? 1.5510  1.5815  1.6550  0.0406  -0.1302 -0.1934 385 MET B C   
10838 O O   . MET B 376 ? 1.5281  1.5486  1.6616  0.0287  -0.1258 -0.1912 385 MET B O   
10839 C CB  . MET B 376 ? 1.6612  1.6944  1.8010  0.0526  -0.1126 -0.2189 385 MET B CB  
10840 C CG  . MET B 376 ? 1.8587  1.8789  2.0253  0.0527  -0.0896 -0.2101 385 MET B CG  
10841 S SD  . MET B 376 ? 1.5020  1.4903  1.7233  0.0372  -0.0673 -0.2027 385 MET B SD  
10842 C CE  . MET B 376 ? 1.5734  1.5385  1.8320  0.0458  -0.0442 -0.2211 385 MET B CE  
10852 N N   . ASN B 377 ? 1.3848  1.4259  1.4464  0.0561  -0.1483 -0.2043 386 ASN B N   
10853 C CA  . ASN B 377 ? 0.9279  0.9705  0.9789  0.0613  -0.1662 -0.2146 386 ASN B CA  
10854 C C   . ASN B 377 ? 0.9671  0.9915  1.0020  0.0461  -0.1584 -0.1795 386 ASN B C   
10855 O O   . ASN B 377 ? 0.8923  0.9123  0.9557  0.0381  -0.1592 -0.1835 386 ASN B O   
10856 C CB  . ASN B 377 ? 0.8604  0.9109  0.8525  0.0875  -0.1851 -0.2251 386 ASN B CB  
10857 C CG  . ASN B 377 ? 0.8590  0.9298  0.8596  0.1058  -0.1955 -0.2634 386 ASN B CG  
10858 O OD1 . ASN B 377 ? 1.0652  1.1381  1.0105  0.1267  -0.2000 -0.2626 386 ASN B OD1 
10859 N ND2 . ASN B 377 ? 1.3251  1.4073  1.3946  0.0969  -0.1956 -0.2972 386 ASN B ND2 
10866 N N   . PHE B 378 ? 1.5146  1.5299  1.5099  0.0400  -0.1483 -0.1470 387 PHE B N   
10867 C CA  . PHE B 378 ? 1.2976  1.2960  1.2755  0.0251  -0.1430 -0.1191 387 PHE B CA  
10868 C C   . PHE B 378 ? 1.0079  1.0011  1.0316  0.0112  -0.1347 -0.1167 387 PHE B C   
10869 O O   . PHE B 378 ? 1.0801  1.0612  1.1016  0.0064  -0.1375 -0.1127 387 PHE B O   
10870 C CB  . PHE B 378 ? 1.1717  1.1697  1.1206  0.0148  -0.1302 -0.0907 387 PHE B CB  
10871 C CG  . PHE B 378 ? 0.8858  0.8717  0.8281  -0.0037 -0.1246 -0.0680 387 PHE B CG  
10872 C CD1 . PHE B 378 ? 0.8757  0.8383  0.7842  -0.0057 -0.1299 -0.0617 387 PHE B CD1 
10873 C CD2 . PHE B 378 ? 0.7561  0.7521  0.7241  -0.0155 -0.1153 -0.0551 387 PHE B CD2 
10874 C CE1 . PHE B 378 ? 1.2501  1.1996  1.1524  -0.0234 -0.1252 -0.0449 387 PHE B CE1 
10875 C CE2 . PHE B 378 ? 0.6373  0.6255  0.5965  -0.0307 -0.1132 -0.0382 387 PHE B CE2 
10876 C CZ  . PHE B 378 ? 0.8654  0.8302  0.7934  -0.0364 -0.1180 -0.0347 387 PHE B CZ  
10886 N N   . LEU B 379 ? 1.2589  1.2568  1.3207  0.0074  -0.1218 -0.1183 388 LEU B N   
10887 C CA  . LEU B 379 ? 0.8964  0.8813  0.9894  -0.0030 -0.1080 -0.1086 388 LEU B CA  
10888 C C   . LEU B 379 ? 0.9330  0.9144  1.0661  -0.0035 -0.1091 -0.1343 388 LEU B C   
10889 O O   . LEU B 379 ? 1.1050  1.0735  1.2480  -0.0111 -0.1006 -0.1251 388 LEU B O   
10890 C CB  . LEU B 379 ? 0.8029  0.7868  0.9188  -0.0017 -0.0908 -0.1000 388 LEU B CB  
10891 C CG  . LEU B 379 ? 0.9054  0.9022  0.9897  -0.0017 -0.0897 -0.0738 388 LEU B CG  
10892 C CD1 . LEU B 379 ? 1.4115  1.4161  1.5148  0.0091  -0.0787 -0.0755 388 LEU B CD1 
10893 C CD2 . LEU B 379 ? 0.6617  0.6527  0.7343  -0.0090 -0.0847 -0.0484 388 LEU B CD2 
10905 N N   . LYS B 380 ? 1.2021  1.1990  1.3590  0.0053  -0.1199 -0.1692 389 LYS B N   
10906 C CA  . LYS B 380 ? 0.8472  0.8523  1.0548  0.0035  -0.1223 -0.2014 389 LYS B CA  
10907 C C   . LYS B 380 ? 0.7598  0.7685  0.9485  0.0075  -0.1362 -0.2003 389 LYS B C   
10908 O O   . LYS B 380 ? 0.5816  0.5875  0.8067  -0.0007 -0.1262 -0.2052 389 LYS B O   
10909 C CB  . LYS B 380 ? 0.8097  0.8390  1.0437  0.0142  -0.1369 -0.2447 389 LYS B CB  
10910 C CG  . LYS B 380 ? 1.0548  1.0748  1.3322  0.0071  -0.1169 -0.2571 389 LYS B CG  
10911 C CD  . LYS B 380 ? 1.1223  1.1660  1.4112  0.0199  -0.1347 -0.3004 389 LYS B CD  
10912 C CE  . LYS B 380 ? 0.7969  0.8276  1.1378  0.0121  -0.1142 -0.3225 389 LYS B CE  
10913 N NZ  . LYS B 380 ? 0.7054  0.7594  1.0300  0.0300  -0.1362 -0.3571 389 LYS B NZ  
10927 N N   . THR B 381 ? 0.7428  0.7529  0.8723  0.0208  -0.1550 -0.1910 390 THR B N   
10928 C CA  . THR B 381 ? 0.9459  0.9514  1.0494  0.0286  -0.1666 -0.1872 390 THR B CA  
10929 C C   . THR B 381 ? 0.5729  0.5543  0.6734  0.0120  -0.1487 -0.1587 390 THR B C   
10930 O O   . THR B 381 ? 0.8951  0.8758  1.0192  0.0106  -0.1453 -0.1651 390 THR B O   
10931 C CB  . THR B 381 ? 1.2356  1.2316  1.2657  0.0452  -0.1813 -0.1738 390 THR B CB  
10932 O OG1 . THR B 381 ? 1.8455  1.8638  1.8701  0.0656  -0.1978 -0.2005 390 THR B OG1 
10933 C CG2 . THR B 381 ? 1.2019  1.1833  1.1985  0.0563  -0.1905 -0.1670 390 THR B CG2 
10941 N N   . VAL B 382 ? 0.6133  0.5789  0.6886  0.0005  -0.1365 -0.1295 391 VAL B N   
10942 C CA  . VAL B 382 ? 0.8839  0.8293  0.9484  -0.0119 -0.1229 -0.1046 391 VAL B CA  
10943 C C   . VAL B 382 ? 0.7952  0.7384  0.9126  -0.0181 -0.1036 -0.1112 391 VAL B C   
10944 O O   . VAL B 382 ? 0.7858  0.7136  0.8995  -0.0229 -0.0926 -0.0990 391 VAL B O   
10945 C CB  . VAL B 382 ? 0.8898  0.8300  0.9235  -0.0207 -0.1168 -0.0778 391 VAL B CB  
10946 C CG1 . VAL B 382 ? 0.8064  0.7304  0.8261  -0.0301 -0.1072 -0.0575 391 VAL B CG1 
10947 C CG2 . VAL B 382 ? 0.9950  0.9360  0.9837  -0.0178 -0.1284 -0.0724 391 VAL B CG2 
10957 N N   . ARG B 383 ? 0.7018  0.6548  0.8656  -0.0188 -0.0946 -0.1282 392 ARG B N   
10958 C CA  . ARG B 383 ? 0.6920  0.6339  0.9053  -0.0267 -0.0686 -0.1318 392 ARG B CA  
10959 C C   . ARG B 383 ? 0.7257  0.6814  0.9782  -0.0267 -0.0711 -0.1587 392 ARG B C   
10960 O O   . ARG B 383 ? 0.7637  0.7065  1.0310  -0.0322 -0.0519 -0.1510 392 ARG B O   
10961 C CB  . ARG B 383 ? 1.0502  0.9899  1.3062  -0.0293 -0.0527 -0.1440 392 ARG B CB  
10962 C CG  . ARG B 383 ? 1.3508  1.2676  1.6535  -0.0385 -0.0179 -0.1430 392 ARG B CG  
10963 C CD  . ARG B 383 ? 1.3340  1.2397  1.6844  -0.0429 0.0028  -0.1586 392 ARG B CD  
10964 N NE  . ARG B 383 ? 1.2948  1.2312  1.6821  -0.0431 -0.0175 -0.2025 392 ARG B NE  
10965 C CZ  . ARG B 383 ? 0.8767  0.8060  1.3067  -0.0472 -0.0042 -0.2250 392 ARG B CZ  
10966 N NH1 . ARG B 383 ? 0.8570  0.7449  1.2953  -0.0501 0.0312  -0.2035 392 ARG B NH1 
10967 N NH2 . ARG B 383 ? 0.9325  0.8930  1.3915  -0.0454 -0.0261 -0.2687 392 ARG B NH2 
10981 N N   . SER B 384 ? 0.6001  0.5851  0.8664  -0.0172 -0.0955 -0.1906 393 SER B N   
10982 C CA  . SER B 384 ? 0.7762  0.7865  1.0880  -0.0134 -0.1018 -0.2222 393 SER B CA  
10983 C C   . SER B 384 ? 0.9324  0.9321  1.2071  -0.0070 -0.1056 -0.2041 393 SER B C   
10984 O O   . SER B 384 ? 0.7751  0.7854  1.0909  -0.0084 -0.0957 -0.2179 393 SER B O   
10985 C CB  . SER B 384 ? 1.0458  1.0939  1.3680  0.0027  -0.1333 -0.2604 393 SER B CB  
10986 O OG  . SER B 384 ? 1.3803  1.4232  1.6267  0.0213  -0.1579 -0.2443 393 SER B OG  
10992 N N   . THR B 385 ? 0.9750  0.9519  1.1752  -0.0018 -0.1161 -0.1740 394 THR B N   
10993 C CA  . THR B 385 ? 0.8344  0.7936  0.9964  0.0034  -0.1179 -0.1583 394 THR B CA  
10994 C C   . THR B 385 ? 1.0651  1.0004  1.2321  -0.0101 -0.0894 -0.1368 394 THR B C   
10995 O O   . THR B 385 ? 0.9593  0.8892  1.1298  -0.0068 -0.0821 -0.1375 394 THR B O   
10996 C CB  . THR B 385 ? 0.6972  0.6353  0.7824  0.0102  -0.1344 -0.1368 394 THR B CB  
10997 O OG1 . THR B 385 ? 0.8855  0.8423  0.9597  0.0296  -0.1582 -0.1564 394 THR B OG1 
10998 C CG2 . THR B 385 ? 0.7858  0.6961  0.8269  0.0138  -0.1342 -0.1210 394 THR B CG2 
11006 N N   . THR B 386 ? 0.9064  0.8282  1.0740  -0.0214 -0.0721 -0.1191 395 THR B N   
11007 C CA  . THR B 386 ? 1.3781  1.2766  1.5475  -0.0282 -0.0431 -0.0992 395 THR B CA  
11008 C C   . THR B 386 ? 1.3688  1.2765  1.6086  -0.0322 -0.0191 -0.1204 395 THR B C   
11009 O O   . THR B 386 ? 0.8181  0.7138  1.0609  -0.0322 0.0003  -0.1140 395 THR B O   
11010 C CB  . THR B 386 ? 0.8320  0.7161  0.9869  -0.0325 -0.0306 -0.0769 395 THR B CB  
11011 O OG1 . THR B 386 ? 0.7082  0.5961  0.8138  -0.0312 -0.0535 -0.0648 395 THR B OG1 
11012 C CG2 . THR B 386 ? 0.6336  0.4897  0.7658  -0.0319 -0.0048 -0.0502 395 THR B CG2 
11020 N N   . GLU B 387 ? 1.5463  1.4768  1.8463  -0.0365 -0.0186 -0.1489 396 GLU B N   
11021 C CA  . GLU B 387 ? 1.4406  1.3834  1.8199  -0.0455 0.0072  -0.1743 396 GLU B CA  
11022 C C   . GLU B 387 ? 0.8334  0.8026  1.2314  -0.0377 -0.0031 -0.1941 396 GLU B C   
11023 O O   . GLU B 387 ? 0.8983  0.8626  1.3291  -0.0430 0.0263  -0.1942 396 GLU B O   
11024 C CB  . GLU B 387 ? 1.3575  1.3254  1.8008  -0.0525 0.0035  -0.2102 396 GLU B CB  
11025 C CG  . GLU B 387 ? 1.6552  1.5944  2.0917  -0.0589 0.0202  -0.1942 396 GLU B CG  
11026 C CD  . GLU B 387 ? 1.9874  1.9505  2.4799  -0.0641 0.0115  -0.2344 396 GLU B CD  
11027 O OE1 . GLU B 387 ? 2.1626  2.1649  2.6555  -0.0542 -0.0257 -0.2636 396 GLU B OE1 
11028 O OE2 . GLU B 387 ? 2.0013  1.9404  2.5332  -0.0760 0.0427  -0.2372 396 GLU B OE2 
11035 N N   . LYS B 388 ? 1.0373  1.0295  1.4056  -0.0215 -0.0421 -0.2065 397 LYS B N   
11036 C CA  . LYS B 388 ? 0.5687  0.5899  0.9596  -0.0080 -0.0533 -0.2290 397 LYS B CA  
11037 C C   . LYS B 388 ? 0.7890  0.7799  1.1363  -0.0038 -0.0386 -0.2017 397 LYS B C   
11038 O O   . LYS B 388 ? 1.0351  1.0460  1.3960  0.0102  -0.0456 -0.2172 397 LYS B O   
11039 C CB  . LYS B 388 ? 0.5695  0.6172  0.9299  0.0161  -0.0981 -0.2472 397 LYS B CB  
11040 C CG  . LYS B 388 ? 0.7932  0.8960  1.2201  0.0214  -0.1191 -0.2961 397 LYS B CG  
11041 C CD  . LYS B 388 ? 0.6126  0.7336  0.9900  0.0500  -0.1626 -0.3082 397 LYS B CD  
11050 N N   . SER B 389 ? 0.7678  0.7141  1.0596  -0.0118 -0.0219 -0.1640 398 SER B N   
11051 C CA  . SER B 389 ? 0.9133  0.8284  1.1528  -0.0067 -0.0112 -0.1398 398 SER B CA  
11052 C C   . SER B 389 ? 0.8713  0.7721  1.1405  -0.0145 0.0322  -0.1312 398 SER B C   
11053 O O   . SER B 389 ? 0.9580  0.8275  1.1753  -0.0102 0.0448  -0.1078 398 SER B O   
11054 C CB  . SER B 389 ? 1.1343  1.0151  1.2912  -0.0081 -0.0238 -0.1088 398 SER B CB  
11055 O OG  . SER B 389 ? 1.0551  0.9433  1.1806  0.0006  -0.0581 -0.1156 398 SER B OG  
11061 N N   . LEU B 390 ? 0.6249  0.5438  0.9725  -0.0264 0.0573  -0.1492 399 LEU B N   
11062 C CA  . LEU B 390 ? 0.9724  0.8785  1.3605  -0.0343 0.1061  -0.1448 399 LEU B CA  
11063 C C   . LEU B 390 ? 1.4125  1.3497  1.8422  -0.0263 0.1103  -0.1688 399 LEU B C   
11064 O O   . LEU B 390 ? 1.2192  1.1942  1.6611  -0.0137 0.0743  -0.1947 399 LEU B O   
11065 C CB  . LEU B 390 ? 0.6500  0.5618  1.1164  -0.0530 0.1356  -0.1599 399 LEU B CB  
11066 C CG  . LEU B 390 ? 0.8215  0.6947  1.2563  -0.0589 0.1471  -0.1334 399 LEU B CG  
11067 C CD1 . LEU B 390 ? 0.6652  0.5446  1.1838  -0.0768 0.1723  -0.1570 399 LEU B CD1 
11068 C CD2 . LEU B 390 ? 0.7008  0.5197  1.0700  -0.0521 0.1800  -0.0881 399 LEU B CD2 
11080 N N   . LEU B 391 ? 1.2568  1.1769  1.7045  -0.0299 0.1562  -0.1587 400 LEU B N   
11081 C CA  . LEU B 391 ? 1.4235  1.3693  1.9024  -0.0198 0.1655  -0.1763 400 LEU B CA  
11082 C C   . LEU B 391 ? 1.5749  1.5622  2.1731  -0.0351 0.2015  -0.2103 400 LEU B C   
11083 O O   . LEU B 391 ? 1.5010  1.5501  2.1702  -0.0323 0.1768  -0.2529 400 LEU B O   
11084 C CB  . LEU B 391 ? 1.3486  1.2455  1.7503  -0.0091 0.1905  -0.1409 400 LEU B CB  
11085 C CG  . LEU B 391 ? 0.9922  0.8484  1.2822  0.0009  0.1588  -0.1105 400 LEU B CG  
11086 C CD1 . LEU B 391 ? 0.9943  0.8060  1.2077  0.0124  0.1804  -0.0819 400 LEU B CD1 
11087 C CD2 . LEU B 391 ? 1.2241  1.1018  1.4922  0.0127  0.1073  -0.1271 400 LEU B CD2 
11099 N N   . LYS B 392 ? 2.1812  2.1370  2.8042  -0.0503 0.2604  -0.1939 401 LYS B N   
11100 C CA  . LYS B 392 ? 1.8703  1.8613  2.6130  -0.0695 0.3047  -0.2262 401 LYS B CA  
11101 C C   . LYS B 392 ? 2.1464  2.1381  2.9567  -0.0958 0.3196  -0.2427 401 LYS B C   
11102 O O   . LYS B 392 ? 0.7051  0.6903  1.4810  -0.0947 0.2823  -0.2404 401 LYS B O   
11103 C CB  . LYS B 392 ? 1.8109  1.7620  2.5443  -0.0704 0.3706  -0.1989 401 LYS B CB  
# 
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   10  10  MET MET A . n 
A 1 2   ILE 2   11  11  ILE ILE A . n 
A 1 3   SER 3   12  12  SER SER A . n 
A 1 4   LYS 4   13  13  LYS LYS A . n 
A 1 5   GLU 5   14  14  GLU GLU A . n 
A 1 6   TYR 6   15  15  TYR TYR A . n 
A 1 7   HIS 7   16  16  HIS HIS A . n 
A 1 8   ILE 8   17  17  ILE ILE A . n 
A 1 9   ASP 9   18  18  ASP ASP A . n 
A 1 10  GLU 10  19  19  GLU GLU A . n 
A 1 11  GLU 11  20  20  GLU GLU A . n 
A 1 12  VAL 12  21  21  VAL VAL A . n 
A 1 13  GLY 13  22  22  GLY GLY A . n 
A 1 14  PHE 14  23  23  PHE PHE A . n 
A 1 15  ALA 15  24  24  ALA ALA A . n 
A 1 16  LEU 16  25  25  LEU LEU A . n 
A 1 17  PRO 17  26  26  PRO PRO A . n 
A 1 18  ASN 18  27  27  ASN ASN A . n 
A 1 19  PRO 19  28  28  PRO PRO A . n 
A 1 20  GLN 20  29  29  GLN GLN A . n 
A 1 21  GLU 21  30  30  GLU GLU A . n 
A 1 22  ASN 22  31  31  ASN ASN A . n 
A 1 23  LEU 23  32  32  LEU LEU A . n 
A 1 24  PRO 24  33  33  PRO PRO A . n 
A 1 25  ASP 25  34  34  ASP ASP A . n 
A 1 26  PHE 26  35  35  PHE PHE A . n 
A 1 27  TYR 27  36  36  TYR TYR A . n 
A 1 28  ASN 28  37  37  ASN ASN A . n 
A 1 29  ASP 29  38  38  ASP ASP A . n 
A 1 30  TRP 30  39  39  TRP TRP A . n 
A 1 31  MET 31  40  40  MET MET A . n 
A 1 32  PHE 32  41  41  PHE PHE A . n 
A 1 33  ILE 33  42  42  ILE ILE A . n 
A 1 34  ALA 34  43  43  ALA ALA A . n 
A 1 35  LYS 35  44  44  LYS LYS A . n 
A 1 36  HIS 36  45  45  HIS HIS A . n 
A 1 37  LEU 37  46  46  LEU LEU A . n 
A 1 38  PRO 38  47  47  PRO PRO A . n 
A 1 39  ASP 39  48  48  ASP ASP A . n 
A 1 40  LEU 40  49  49  LEU LEU A . n 
A 1 41  ILE 41  50  50  ILE ILE A . n 
A 1 42  GLU 42  51  51  GLU GLU A . n 
A 1 43  SER 43  52  52  SER SER A . n 
A 1 44  GLY 44  53  53  GLY GLY A . n 
A 1 45  GLN 45  54  54  GLN GLN A . n 
A 1 46  LEU 46  55  55  LEU LEU A . n 
A 1 47  ARG 47  56  56  ARG ARG A . n 
A 1 48  GLU 48  57  57  GLU GLU A . n 
A 1 49  ARG 49  58  58  ARG ARG A . n 
A 1 50  VAL 50  59  59  VAL VAL A . n 
A 1 51  GLU 51  60  60  GLU GLU A . n 
A 1 52  LYS 52  61  61  LYS LYS A . n 
A 1 53  LEU 53  62  62  LEU LEU A . n 
A 1 54  ASN 54  63  63  ASN ASN A . n 
A 1 55  MET 55  64  64  MET MET A . n 
A 1 56  LEU 56  65  65  LEU LEU A . n 
A 1 57  SER 57  66  66  SER SER A . n 
A 1 58  ILE 58  67  67  ILE ILE A . n 
A 1 59  ASP 59  68  68  ASP ASP A . n 
A 1 60  HIS 60  69  69  HIS HIS A . n 
A 1 61  LEU 61  70  70  LEU LEU A . n 
A 1 62  THR 62  71  71  THR THR A . n 
A 1 63  ASP 63  72  72  ASP ASP A . n 
A 1 64  HIS 64  73  73  HIS HIS A . n 
A 1 65  LYS 65  74  74  LYS LYS A . n 
A 1 66  SER 66  75  75  SER SER A . n 
A 1 67  GLN 67  76  76  GLN GLN A . n 
A 1 68  ARG 68  77  77  ARG ARG A . n 
A 1 69  LEU 69  78  78  LEU LEU A . n 
A 1 70  ALA 70  79  79  ALA ALA A . n 
A 1 71  ARG 71  80  80  ARG ARG A . n 
A 1 72  LEU 72  81  81  LEU LEU A . n 
A 1 73  VAL 73  82  82  VAL VAL A . n 
A 1 74  LEU 74  83  83  LEU LEU A . n 
A 1 75  GLY 75  84  84  GLY GLY A . n 
A 1 76  CYS 76  85  85  CYS CYS A . n 
A 1 77  ILE 77  86  86  ILE ILE A . n 
A 1 78  THR 78  87  87  THR THR A . n 
A 1 79  MET 79  88  88  MET MET A . n 
A 1 80  ALA 80  89  89  ALA ALA A . n 
A 1 81  TYR 81  90  90  TYR TYR A . n 
A 1 82  VAL 82  91  91  VAL VAL A . n 
A 1 83  TRP 83  92  92  TRP TRP A . n 
A 1 84  GLY 84  93  93  GLY GLY A . n 
A 1 85  LYS 85  94  94  LYS LYS A . n 
A 1 86  GLY 86  95  95  GLY GLY A . n 
A 1 87  HIS 87  96  96  HIS HIS A . n 
A 1 88  GLY 88  97  97  GLY GLY A . n 
A 1 89  ASP 89  98  98  ASP ASP A . n 
A 1 90  VAL 90  99  99  VAL VAL A . n 
A 1 91  ARG 91  100 100 ARG ARG A . n 
A 1 92  LYS 92  101 101 LYS LYS A . n 
A 1 93  VAL 93  102 102 VAL VAL A . n 
A 1 94  LEU 94  103 103 LEU LEU A . n 
A 1 95  PRO 95  104 104 PRO PRO A . n 
A 1 96  ARG 96  105 105 ARG ARG A . n 
A 1 97  ASN 97  106 106 ASN ASN A . n 
A 1 98  ILE 98  107 107 ILE ILE A . n 
A 1 99  ALA 99  108 108 ALA ALA A . n 
A 1 100 VAL 100 109 109 VAL VAL A . n 
A 1 101 PRO 101 110 110 PRO PRO A . n 
A 1 102 TYR 102 111 111 TYR TYR A . n 
A 1 103 CYS 103 112 112 CYS CYS A . n 
A 1 104 GLN 104 113 113 GLN GLN A . n 
A 1 105 LEU 105 114 114 LEU LEU A . n 
A 1 106 SER 106 115 115 SER SER A . n 
A 1 107 LYS 107 116 116 LYS LYS A . n 
A 1 108 LYS 108 117 117 LYS LYS A . n 
A 1 109 LEU 109 118 118 LEU LEU A . n 
A 1 110 GLU 110 119 119 GLU GLU A . n 
A 1 111 LEU 111 120 120 LEU LEU A . n 
A 1 112 PRO 112 121 121 PRO PRO A . n 
A 1 113 PRO 113 122 122 PRO PRO A . n 
A 1 114 ILE 114 123 123 ILE ILE A . n 
A 1 115 LEU 115 124 124 LEU LEU A . n 
A 1 116 VAL 116 125 125 VAL VAL A . n 
A 1 117 TYR 117 126 126 TYR TYR A . n 
A 1 118 ALA 118 127 127 ALA ALA A . n 
A 1 119 ASP 119 128 128 ASP ASP A . n 
A 1 120 CYS 120 129 129 CYS CYS A . n 
A 1 121 VAL 121 130 130 VAL VAL A . n 
A 1 122 LEU 122 131 131 LEU LEU A . n 
A 1 123 ALA 123 132 132 ALA ALA A . n 
A 1 124 ASN 124 133 133 ASN ASN A . n 
A 1 125 TRP 125 134 134 TRP TRP A . n 
A 1 126 LYS 126 135 135 LYS LYS A . n 
A 1 127 LYS 127 136 136 LYS LYS A . n 
A 1 128 LYS 128 137 137 LYS LYS A . n 
A 1 129 ASP 129 138 138 ASP ASP A . n 
A 1 130 PRO 130 139 139 PRO PRO A . n 
A 1 131 ASN 131 140 140 ASN ASN A . n 
A 1 132 LYS 132 141 141 LYS LYS A . n 
A 1 133 PRO 133 142 142 PRO PRO A . n 
A 1 134 LEU 134 143 143 LEU LEU A . n 
A 1 135 THR 135 144 144 THR THR A . n 
A 1 136 TYR 136 145 145 TYR TYR A . n 
A 1 137 GLU 137 146 146 GLU GLU A . n 
A 1 138 ASN 138 147 147 ASN ASN A . n 
A 1 139 MET 139 148 148 MET MET A . n 
A 1 140 ASP 140 149 149 ASP ASP A . n 
A 1 141 VAL 141 150 150 VAL VAL A . n 
A 1 142 LEU 142 151 151 LEU LEU A . n 
A 1 143 PHE 143 152 152 PHE PHE A . n 
A 1 144 SER 144 153 153 SER SER A . n 
A 1 145 PHE 145 154 154 PHE PHE A . n 
A 1 146 ARG 146 155 155 ARG ARG A . n 
A 1 147 ASP 147 156 156 ASP ASP A . n 
A 1 148 GLY 148 157 157 GLY GLY A . n 
A 1 149 ASP 149 158 158 ASP ASP A . n 
A 1 150 CYS 150 159 159 CYS CYS A . n 
A 1 151 SER 151 160 160 SER SER A . n 
A 1 152 LYS 152 161 161 LYS LYS A . n 
A 1 153 GLY 153 162 162 GLY GLY A . n 
A 1 154 PHE 154 163 163 PHE PHE A . n 
A 1 155 PHE 155 164 164 PHE PHE A . n 
A 1 156 LEU 156 165 165 LEU LEU A . n 
A 1 157 VAL 157 166 166 VAL VAL A . n 
A 1 158 SER 158 167 167 SER SER A . n 
A 1 159 LEU 159 168 168 LEU LEU A . n 
A 1 160 LEU 160 169 169 LEU LEU A . n 
A 1 161 VAL 161 170 170 VAL VAL A . n 
A 1 162 GLU 162 171 171 GLU GLU A . n 
A 1 163 ILE 163 172 172 ILE ILE A . n 
A 1 164 ALA 164 173 173 ALA ALA A . n 
A 1 165 ALA 165 174 174 ALA ALA A . n 
A 1 166 ALA 166 175 175 ALA ALA A . n 
A 1 167 SER 167 176 176 SER SER A . n 
A 1 168 ALA 168 177 177 ALA ALA A . n 
A 1 169 ILE 169 178 178 ILE ILE A . n 
A 1 170 LYS 170 179 179 LYS LYS A . n 
A 1 171 VAL 171 180 180 VAL VAL A . n 
A 1 172 ILE 172 181 181 ILE ILE A . n 
A 1 173 PRO 173 182 182 PRO PRO A . n 
A 1 174 THR 174 183 183 THR THR A . n 
A 1 175 VAL 175 184 184 VAL VAL A . n 
A 1 176 PHE 176 185 185 PHE PHE A . n 
A 1 177 LYS 177 186 186 LYS LYS A . n 
A 1 178 ALA 178 187 187 ALA ALA A . n 
A 1 179 MET 179 188 188 MET MET A . n 
A 1 180 GLN 180 189 189 GLN GLN A . n 
A 1 181 MET 181 190 190 MET MET A . n 
A 1 182 GLN 182 191 191 GLN GLN A . n 
A 1 183 GLU 183 192 192 GLU GLU A . n 
A 1 184 ARG 184 193 193 ARG ARG A . n 
A 1 185 ASP 185 194 194 ASP ASP A . n 
A 1 186 THR 186 195 195 THR THR A . n 
A 1 187 LEU 187 196 196 LEU LEU A . n 
A 1 188 LEU 188 197 197 LEU LEU A . n 
A 1 189 LYS 189 198 198 LYS LYS A . n 
A 1 190 ALA 190 199 199 ALA ALA A . n 
A 1 191 LEU 191 200 200 LEU LEU A . n 
A 1 192 LEU 192 201 201 LEU LEU A . n 
A 1 193 GLU 193 202 202 GLU GLU A . n 
A 1 194 ILE 194 203 203 ILE ILE A . n 
A 1 195 ALA 195 204 204 ALA ALA A . n 
A 1 196 SER 196 205 205 SER SER A . n 
A 1 197 CYS 197 206 206 CYS CYS A . n 
A 1 198 LEU 198 207 207 LEU LEU A . n 
A 1 199 GLU 199 208 208 GLU GLU A . n 
A 1 200 LYS 200 209 209 LYS LYS A . n 
A 1 201 ALA 201 210 210 ALA ALA A . n 
A 1 202 LEU 202 211 211 LEU LEU A . n 
A 1 203 GLN 203 212 212 GLN GLN A . n 
A 1 204 VAL 204 213 213 VAL VAL A . n 
A 1 205 PHE 205 214 214 PHE PHE A . n 
A 1 206 HIS 206 215 215 HIS HIS A . n 
A 1 207 GLN 207 216 216 GLN GLN A . n 
A 1 208 ILE 208 217 217 ILE ILE A . n 
A 1 209 HIS 209 218 218 HIS HIS A . n 
A 1 210 ASP 210 219 219 ASP ASP A . n 
A 1 211 HIS 211 220 220 HIS HIS A . n 
A 1 212 VAL 212 221 221 VAL VAL A . n 
A 1 213 ASN 213 222 222 ASN ASN A . n 
A 1 214 PRO 214 223 223 PRO PRO A . n 
A 1 215 LYS 215 224 224 LYS LYS A . n 
A 1 216 ALA 216 225 225 ALA ALA A . n 
A 1 217 PHE 217 226 226 PHE PHE A . n 
A 1 218 PHE 218 227 227 PHE PHE A . n 
A 1 219 SER 219 228 228 SER SER A . n 
A 1 220 VAL 220 229 229 VAL VAL A . n 
A 1 221 LEU 221 230 230 LEU LEU A . n 
A 1 222 ARG 222 231 231 ARG ARG A . n 
A 1 223 ILE 223 232 232 ILE ILE A . n 
A 1 224 TYR 224 233 233 TYR TYR A . n 
A 1 225 LEU 225 234 234 LEU LEU A . n 
A 1 226 SER 226 235 235 SER SER A . n 
A 1 227 GLY 227 236 236 GLY GLY A . n 
A 1 228 TRP 228 237 237 TRP TRP A . n 
A 1 229 LYS 229 238 238 LYS LYS A . n 
A 1 230 GLY 230 239 239 GLY GLY A . n 
A 1 231 ASN 231 240 240 ASN ASN A . n 
A 1 232 PRO 232 241 241 PRO PRO A . n 
A 1 233 GLN 233 242 242 GLN GLN A . n 
A 1 234 LEU 234 243 243 LEU LEU A . n 
A 1 235 SER 235 244 244 SER SER A . n 
A 1 236 ASP 236 245 245 ASP ASP A . n 
A 1 237 GLY 237 246 246 GLY GLY A . n 
A 1 238 LEU 238 247 247 LEU LEU A . n 
A 1 239 VAL 239 248 248 VAL VAL A . n 
A 1 240 TYR 240 249 249 TYR TYR A . n 
A 1 241 GLU 241 250 250 GLU GLU A . n 
A 1 242 GLY 242 251 251 GLY GLY A . n 
A 1 243 PHE 243 252 252 PHE PHE A . n 
A 1 244 TRP 244 253 253 TRP TRP A . n 
A 1 245 GLU 245 254 254 GLU GLU A . n 
A 1 246 ASP 246 255 255 ASP ASP A . n 
A 1 247 PRO 247 256 256 PRO PRO A . n 
A 1 248 LYS 248 257 257 LYS LYS A . n 
A 1 249 GLU 249 258 258 GLU GLU A . n 
A 1 250 PHE 250 259 259 PHE PHE A . n 
A 1 251 ALA 251 260 260 ALA ALA A . n 
A 1 252 GLY 252 261 261 GLY GLY A . n 
A 1 253 GLY 253 262 262 GLY GLY A . n 
A 1 254 SER 254 263 263 SER SER A . n 
A 1 255 ALA 255 264 264 ALA ALA A . n 
A 1 256 GLY 256 265 265 GLY GLY A . n 
A 1 257 GLN 257 266 266 GLN GLN A . n 
A 1 258 SER 258 267 267 SER SER A . n 
A 1 259 SER 259 268 268 SER SER A . n 
A 1 260 VAL 260 269 269 VAL VAL A . n 
A 1 261 PHE 261 270 270 PHE PHE A . n 
A 1 262 GLN 262 271 271 GLN GLN A . n 
A 1 263 CYS 263 272 272 CYS CYS A . n 
A 1 264 PHE 264 273 273 PHE PHE A . n 
A 1 265 ASP 265 274 274 ASP ASP A . n 
A 1 266 VAL 266 275 275 VAL VAL A . n 
A 1 267 LEU 267 276 276 LEU LEU A . n 
A 1 268 LEU 268 277 277 LEU LEU A . n 
A 1 269 GLY 269 278 278 GLY GLY A . n 
A 1 270 ILE 270 279 279 ILE ILE A . n 
A 1 271 GLN 271 280 280 GLN GLN A . n 
A 1 272 GLN 272 281 281 GLN GLN A . n 
A 1 273 THR 273 282 282 THR THR A . n 
A 1 274 ALA 274 283 283 ALA ALA A . n 
A 1 275 GLY 275 284 284 GLY GLY A . n 
A 1 276 GLY 276 285 285 GLY GLY A . n 
A 1 277 GLY 277 286 286 GLY GLY A . n 
A 1 278 HIS 278 287 287 HIS HIS A . n 
A 1 279 ALA 279 288 288 ALA ALA A . n 
A 1 280 ALA 280 289 289 ALA ALA A . n 
A 1 281 GLN 281 290 290 GLN GLN A . n 
A 1 282 PHE 282 291 291 PHE PHE A . n 
A 1 283 LEU 283 292 292 LEU LEU A . n 
A 1 284 GLN 284 293 293 GLN GLN A . n 
A 1 285 ASP 285 294 294 ASP ASP A . n 
A 1 286 MET 286 295 295 MET MET A . n 
A 1 287 ARG 287 296 296 ARG ARG A . n 
A 1 288 ARG 288 297 297 ARG ARG A . n 
A 1 289 TYR 289 298 298 TYR TYR A . n 
A 1 290 MET 290 299 299 MET MET A . n 
A 1 291 PRO 291 300 300 PRO PRO A . n 
A 1 292 PRO 292 301 301 PRO PRO A . n 
A 1 293 ALA 293 302 302 ALA ALA A . n 
A 1 294 HIS 294 303 303 HIS HIS A . n 
A 1 295 ARG 295 304 304 ARG ARG A . n 
A 1 296 ASN 296 305 305 ASN ASN A . n 
A 1 297 PHE 297 306 306 PHE PHE A . n 
A 1 298 LEU 298 307 307 LEU LEU A . n 
A 1 299 CYS 299 308 308 CYS CYS A . n 
A 1 300 SER 300 309 309 SER SER A . n 
A 1 301 LEU 301 310 310 LEU LEU A . n 
A 1 302 GLU 302 311 311 GLU GLU A . n 
A 1 303 SER 303 312 312 SER SER A . n 
A 1 304 ASN 304 313 313 ASN ASN A . n 
A 1 305 PRO 305 314 314 PRO PRO A . n 
A 1 306 SER 306 315 315 SER SER A . n 
A 1 307 VAL 307 316 316 VAL VAL A . n 
A 1 308 ARG 308 317 317 ARG ARG A . n 
A 1 309 GLU 309 318 318 GLU GLU A . n 
A 1 310 PHE 310 319 319 PHE PHE A . n 
A 1 311 VAL 311 320 320 VAL VAL A . n 
A 1 312 LEU 312 321 321 LEU LEU A . n 
A 1 313 SER 313 322 322 SER SER A . n 
A 1 314 LYS 314 323 323 LYS LYS A . n 
A 1 315 GLY 315 324 324 GLY GLY A . n 
A 1 316 ASP 316 325 325 ASP ASP A . n 
A 1 317 ALA 317 326 326 ALA ALA A . n 
A 1 318 GLY 318 327 327 GLY GLY A . n 
A 1 319 LEU 319 328 328 LEU LEU A . n 
A 1 320 ARG 320 329 329 ARG ARG A . n 
A 1 321 GLU 321 330 330 GLU GLU A . n 
A 1 322 ALA 322 331 331 ALA ALA A . n 
A 1 323 TYR 323 332 332 TYR TYR A . n 
A 1 324 ASP 324 333 333 ASP ASP A . n 
A 1 325 ALA 325 334 334 ALA ALA A . n 
A 1 326 CYS 326 335 335 CYS CYS A . n 
A 1 327 VAL 327 336 336 VAL VAL A . n 
A 1 328 LYS 328 337 337 LYS LYS A . n 
A 1 329 ALA 329 338 338 ALA ALA A . n 
A 1 330 LEU 330 339 339 LEU LEU A . n 
A 1 331 VAL 331 340 340 VAL VAL A . n 
A 1 332 SER 332 341 341 SER SER A . n 
A 1 333 LEU 333 342 342 LEU LEU A . n 
A 1 334 ARG 334 343 343 ARG ARG A . n 
A 1 335 SER 335 344 344 SER SER A . n 
A 1 336 TYR 336 345 345 TYR TYR A . n 
A 1 337 HIS 337 346 346 HIS HIS A . n 
A 1 338 LEU 338 347 347 LEU LEU A . n 
A 1 339 GLN 339 348 348 GLN GLN A . n 
A 1 340 ILE 340 349 349 ILE ILE A . n 
A 1 341 VAL 341 350 350 VAL VAL A . n 
A 1 342 THR 342 351 351 THR THR A . n 
A 1 343 LYS 343 352 352 LYS LYS A . n 
A 1 344 TYR 344 353 353 TYR TYR A . n 
A 1 345 ILE 345 354 354 ILE ILE A . n 
A 1 346 LEU 346 355 355 LEU LEU A . n 
A 1 347 ILE 347 356 356 ILE ILE A . n 
A 1 348 PRO 348 357 357 PRO PRO A . n 
A 1 349 ALA 349 358 358 ALA ALA A . n 
A 1 350 SER 350 359 359 SER SER A . n 
A 1 351 GLN 351 360 360 GLN GLN A . n 
A 1 352 GLN 352 361 361 GLN GLN A . n 
A 1 353 PRO 353 362 362 PRO PRO A . n 
A 1 354 LYS 354 363 ?   ?   ?   A . n 
A 1 355 GLU 355 364 ?   ?   ?   A . n 
A 1 356 ASN 356 365 ?   ?   ?   A . n 
A 1 357 LYS 357 366 ?   ?   ?   A . n 
A 1 358 THR 358 367 ?   ?   ?   A . n 
A 1 359 SER 359 368 ?   ?   ?   A . n 
A 1 360 GLU 360 369 ?   ?   ?   A . n 
A 1 361 ASP 361 370 ?   ?   ?   A . n 
A 1 362 PRO 362 371 ?   ?   ?   A . n 
A 1 363 SER 363 372 ?   ?   ?   A . n 
A 1 364 LYS 364 373 ?   ?   ?   A . n 
A 1 365 LEU 365 374 ?   ?   ?   A . n 
A 1 366 GLU 366 375 ?   ?   ?   A . n 
A 1 367 ALA 367 376 ?   ?   ?   A . n 
A 1 368 LYS 368 377 ?   ?   ?   A . n 
A 1 369 GLY 369 378 ?   ?   ?   A . n 
A 1 370 THR 370 379 ?   ?   ?   A . n 
A 1 371 GLY 371 380 380 GLY GLY A . n 
A 1 372 GLY 372 381 381 GLY GLY A . n 
A 1 373 THR 373 382 382 THR THR A . n 
A 1 374 ASP 374 383 383 ASP ASP A . n 
A 1 375 LEU 375 384 384 LEU LEU A . n 
A 1 376 MET 376 385 385 MET MET A . n 
A 1 377 ASN 377 386 386 ASN ASN A . n 
A 1 378 PHE 378 387 387 PHE PHE A . n 
A 1 379 LEU 379 388 388 LEU LEU A . n 
A 1 380 LYS 380 389 389 LYS LYS A . n 
A 1 381 THR 381 390 390 THR THR A . n 
A 1 382 VAL 382 391 391 VAL VAL A . n 
A 1 383 ARG 383 392 392 ARG ARG A . n 
A 1 384 SER 384 393 393 SER SER A . n 
A 1 385 THR 385 394 394 THR THR A . n 
A 1 386 THR 386 395 395 THR THR A . n 
A 1 387 GLU 387 396 396 GLU GLU A . n 
A 1 388 LYS 388 397 397 LYS LYS A . n 
A 1 389 SER 389 398 398 SER SER A . n 
A 1 390 LEU 390 399 399 LEU LEU A . n 
A 1 391 LEU 391 400 400 LEU LEU A . n 
A 1 392 LYS 392 401 401 LYS LYS A . n 
A 1 393 GLU 393 402 ?   ?   ?   A . n 
A 1 394 GLY 394 403 ?   ?   ?   A . n 
B 1 1   MET 1   10  10  MET MET B . n 
B 1 2   ILE 2   11  11  ILE ILE B . n 
B 1 3   SER 3   12  12  SER SER B . n 
B 1 4   LYS 4   13  13  LYS LYS B . n 
B 1 5   GLU 5   14  14  GLU GLU B . n 
B 1 6   TYR 6   15  15  TYR TYR B . n 
B 1 7   HIS 7   16  16  HIS HIS B . n 
B 1 8   ILE 8   17  17  ILE ILE B . n 
B 1 9   ASP 9   18  18  ASP ASP B . n 
B 1 10  GLU 10  19  19  GLU GLU B . n 
B 1 11  GLU 11  20  20  GLU GLU B . n 
B 1 12  VAL 12  21  21  VAL VAL B . n 
B 1 13  GLY 13  22  22  GLY GLY B . n 
B 1 14  PHE 14  23  23  PHE PHE B . n 
B 1 15  ALA 15  24  24  ALA ALA B . n 
B 1 16  LEU 16  25  25  LEU LEU B . n 
B 1 17  PRO 17  26  26  PRO PRO B . n 
B 1 18  ASN 18  27  27  ASN ASN B . n 
B 1 19  PRO 19  28  28  PRO PRO B . n 
B 1 20  GLN 20  29  29  GLN GLN B . n 
B 1 21  GLU 21  30  30  GLU GLU B . n 
B 1 22  ASN 22  31  31  ASN ASN B . n 
B 1 23  LEU 23  32  32  LEU LEU B . n 
B 1 24  PRO 24  33  33  PRO PRO B . n 
B 1 25  ASP 25  34  34  ASP ASP B . n 
B 1 26  PHE 26  35  35  PHE PHE B . n 
B 1 27  TYR 27  36  36  TYR TYR B . n 
B 1 28  ASN 28  37  37  ASN ASN B . n 
B 1 29  ASP 29  38  38  ASP ASP B . n 
B 1 30  TRP 30  39  39  TRP TRP B . n 
B 1 31  MET 31  40  40  MET MET B . n 
B 1 32  PHE 32  41  41  PHE PHE B . n 
B 1 33  ILE 33  42  42  ILE ILE B . n 
B 1 34  ALA 34  43  43  ALA ALA B . n 
B 1 35  LYS 35  44  44  LYS LYS B . n 
B 1 36  HIS 36  45  45  HIS HIS B . n 
B 1 37  LEU 37  46  46  LEU LEU B . n 
B 1 38  PRO 38  47  47  PRO PRO B . n 
B 1 39  ASP 39  48  48  ASP ASP B . n 
B 1 40  LEU 40  49  49  LEU LEU B . n 
B 1 41  ILE 41  50  50  ILE ILE B . n 
B 1 42  GLU 42  51  51  GLU GLU B . n 
B 1 43  SER 43  52  52  SER SER B . n 
B 1 44  GLY 44  53  53  GLY GLY B . n 
B 1 45  GLN 45  54  54  GLN GLN B . n 
B 1 46  LEU 46  55  55  LEU LEU B . n 
B 1 47  ARG 47  56  56  ARG ARG B . n 
B 1 48  GLU 48  57  57  GLU GLU B . n 
B 1 49  ARG 49  58  58  ARG ARG B . n 
B 1 50  VAL 50  59  59  VAL VAL B . n 
B 1 51  GLU 51  60  60  GLU GLU B . n 
B 1 52  LYS 52  61  61  LYS LYS B . n 
B 1 53  LEU 53  62  62  LEU LEU B . n 
B 1 54  ASN 54  63  63  ASN ASN B . n 
B 1 55  MET 55  64  64  MET MET B . n 
B 1 56  LEU 56  65  65  LEU LEU B . n 
B 1 57  SER 57  66  66  SER SER B . n 
B 1 58  ILE 58  67  67  ILE ILE B . n 
B 1 59  ASP 59  68  68  ASP ASP B . n 
B 1 60  HIS 60  69  69  HIS HIS B . n 
B 1 61  LEU 61  70  70  LEU LEU B . n 
B 1 62  THR 62  71  71  THR THR B . n 
B 1 63  ASP 63  72  72  ASP ASP B . n 
B 1 64  HIS 64  73  73  HIS HIS B . n 
B 1 65  LYS 65  74  74  LYS LYS B . n 
B 1 66  SER 66  75  75  SER SER B . n 
B 1 67  GLN 67  76  76  GLN GLN B . n 
B 1 68  ARG 68  77  77  ARG ARG B . n 
B 1 69  LEU 69  78  78  LEU LEU B . n 
B 1 70  ALA 70  79  79  ALA ALA B . n 
B 1 71  ARG 71  80  80  ARG ARG B . n 
B 1 72  LEU 72  81  81  LEU LEU B . n 
B 1 73  VAL 73  82  82  VAL VAL B . n 
B 1 74  LEU 74  83  83  LEU LEU B . n 
B 1 75  GLY 75  84  84  GLY GLY B . n 
B 1 76  CYS 76  85  85  CYS CYS B . n 
B 1 77  ILE 77  86  86  ILE ILE B . n 
B 1 78  THR 78  87  87  THR THR B . n 
B 1 79  MET 79  88  88  MET MET B . n 
B 1 80  ALA 80  89  89  ALA ALA B . n 
B 1 81  TYR 81  90  90  TYR TYR B . n 
B 1 82  VAL 82  91  91  VAL VAL B . n 
B 1 83  TRP 83  92  92  TRP TRP B . n 
B 1 84  GLY 84  93  93  GLY GLY B . n 
B 1 85  LYS 85  94  94  LYS LYS B . n 
B 1 86  GLY 86  95  95  GLY GLY B . n 
B 1 87  HIS 87  96  96  HIS HIS B . n 
B 1 88  GLY 88  97  97  GLY GLY B . n 
B 1 89  ASP 89  98  98  ASP ASP B . n 
B 1 90  VAL 90  99  99  VAL VAL B . n 
B 1 91  ARG 91  100 100 ARG ARG B . n 
B 1 92  LYS 92  101 101 LYS LYS B . n 
B 1 93  VAL 93  102 102 VAL VAL B . n 
B 1 94  LEU 94  103 103 LEU LEU B . n 
B 1 95  PRO 95  104 104 PRO PRO B . n 
B 1 96  ARG 96  105 105 ARG ARG B . n 
B 1 97  ASN 97  106 106 ASN ASN B . n 
B 1 98  ILE 98  107 107 ILE ILE B . n 
B 1 99  ALA 99  108 108 ALA ALA B . n 
B 1 100 VAL 100 109 109 VAL VAL B . n 
B 1 101 PRO 101 110 110 PRO PRO B . n 
B 1 102 TYR 102 111 111 TYR TYR B . n 
B 1 103 CYS 103 112 112 CYS CYS B . n 
B 1 104 GLN 104 113 113 GLN GLN B . n 
B 1 105 LEU 105 114 114 LEU LEU B . n 
B 1 106 SER 106 115 115 SER SER B . n 
B 1 107 LYS 107 116 116 LYS LYS B . n 
B 1 108 LYS 108 117 117 LYS LYS B . n 
B 1 109 LEU 109 118 118 LEU LEU B . n 
B 1 110 GLU 110 119 119 GLU GLU B . n 
B 1 111 LEU 111 120 120 LEU LEU B . n 
B 1 112 PRO 112 121 121 PRO PRO B . n 
B 1 113 PRO 113 122 122 PRO PRO B . n 
B 1 114 ILE 114 123 123 ILE ILE B . n 
B 1 115 LEU 115 124 124 LEU LEU B . n 
B 1 116 VAL 116 125 125 VAL VAL B . n 
B 1 117 TYR 117 126 126 TYR TYR B . n 
B 1 118 ALA 118 127 127 ALA ALA B . n 
B 1 119 ASP 119 128 128 ASP ASP B . n 
B 1 120 CYS 120 129 129 CYS CYS B . n 
B 1 121 VAL 121 130 130 VAL VAL B . n 
B 1 122 LEU 122 131 131 LEU LEU B . n 
B 1 123 ALA 123 132 132 ALA ALA B . n 
B 1 124 ASN 124 133 133 ASN ASN B . n 
B 1 125 TRP 125 134 134 TRP TRP B . n 
B 1 126 LYS 126 135 135 LYS LYS B . n 
B 1 127 LYS 127 136 136 LYS LYS B . n 
B 1 128 LYS 128 137 137 LYS LYS B . n 
B 1 129 ASP 129 138 138 ASP ASP B . n 
B 1 130 PRO 130 139 139 PRO PRO B . n 
B 1 131 ASN 131 140 140 ASN ASN B . n 
B 1 132 LYS 132 141 141 LYS LYS B . n 
B 1 133 PRO 133 142 142 PRO PRO B . n 
B 1 134 LEU 134 143 143 LEU LEU B . n 
B 1 135 THR 135 144 144 THR THR B . n 
B 1 136 TYR 136 145 145 TYR TYR B . n 
B 1 137 GLU 137 146 146 GLU GLU B . n 
B 1 138 ASN 138 147 147 ASN ASN B . n 
B 1 139 MET 139 148 148 MET MET B . n 
B 1 140 ASP 140 149 149 ASP ASP B . n 
B 1 141 VAL 141 150 150 VAL VAL B . n 
B 1 142 LEU 142 151 151 LEU LEU B . n 
B 1 143 PHE 143 152 152 PHE PHE B . n 
B 1 144 SER 144 153 153 SER SER B . n 
B 1 145 PHE 145 154 154 PHE PHE B . n 
B 1 146 ARG 146 155 155 ARG ARG B . n 
B 1 147 ASP 147 156 156 ASP ASP B . n 
B 1 148 GLY 148 157 157 GLY GLY B . n 
B 1 149 ASP 149 158 158 ASP ASP B . n 
B 1 150 CYS 150 159 159 CYS CYS B . n 
B 1 151 SER 151 160 160 SER SER B . n 
B 1 152 LYS 152 161 161 LYS LYS B . n 
B 1 153 GLY 153 162 162 GLY GLY B . n 
B 1 154 PHE 154 163 163 PHE PHE B . n 
B 1 155 PHE 155 164 164 PHE PHE B . n 
B 1 156 LEU 156 165 165 LEU LEU B . n 
B 1 157 VAL 157 166 166 VAL VAL B . n 
B 1 158 SER 158 167 167 SER SER B . n 
B 1 159 LEU 159 168 168 LEU LEU B . n 
B 1 160 LEU 160 169 169 LEU LEU B . n 
B 1 161 VAL 161 170 170 VAL VAL B . n 
B 1 162 GLU 162 171 171 GLU GLU B . n 
B 1 163 ILE 163 172 172 ILE ILE B . n 
B 1 164 ALA 164 173 173 ALA ALA B . n 
B 1 165 ALA 165 174 174 ALA ALA B . n 
B 1 166 ALA 166 175 175 ALA ALA B . n 
B 1 167 SER 167 176 176 SER SER B . n 
B 1 168 ALA 168 177 177 ALA ALA B . n 
B 1 169 ILE 169 178 178 ILE ILE B . n 
B 1 170 LYS 170 179 179 LYS LYS B . n 
B 1 171 VAL 171 180 180 VAL VAL B . n 
B 1 172 ILE 172 181 181 ILE ILE B . n 
B 1 173 PRO 173 182 182 PRO PRO B . n 
B 1 174 THR 174 183 183 THR THR B . n 
B 1 175 VAL 175 184 184 VAL VAL B . n 
B 1 176 PHE 176 185 185 PHE PHE B . n 
B 1 177 LYS 177 186 186 LYS LYS B . n 
B 1 178 ALA 178 187 187 ALA ALA B . n 
B 1 179 MET 179 188 188 MET MET B . n 
B 1 180 GLN 180 189 189 GLN GLN B . n 
B 1 181 MET 181 190 190 MET MET B . n 
B 1 182 GLN 182 191 191 GLN GLN B . n 
B 1 183 GLU 183 192 192 GLU GLU B . n 
B 1 184 ARG 184 193 193 ARG ARG B . n 
B 1 185 ASP 185 194 194 ASP ASP B . n 
B 1 186 THR 186 195 195 THR THR B . n 
B 1 187 LEU 187 196 196 LEU LEU B . n 
B 1 188 LEU 188 197 197 LEU LEU B . n 
B 1 189 LYS 189 198 198 LYS LYS B . n 
B 1 190 ALA 190 199 199 ALA ALA B . n 
B 1 191 LEU 191 200 200 LEU LEU B . n 
B 1 192 LEU 192 201 201 LEU LEU B . n 
B 1 193 GLU 193 202 202 GLU GLU B . n 
B 1 194 ILE 194 203 203 ILE ILE B . n 
B 1 195 ALA 195 204 204 ALA ALA B . n 
B 1 196 SER 196 205 205 SER SER B . n 
B 1 197 CYS 197 206 206 CYS CYS B . n 
B 1 198 LEU 198 207 207 LEU LEU B . n 
B 1 199 GLU 199 208 208 GLU GLU B . n 
B 1 200 LYS 200 209 209 LYS LYS B . n 
B 1 201 ALA 201 210 210 ALA ALA B . n 
B 1 202 LEU 202 211 211 LEU LEU B . n 
B 1 203 GLN 203 212 212 GLN GLN B . n 
B 1 204 VAL 204 213 213 VAL VAL B . n 
B 1 205 PHE 205 214 214 PHE PHE B . n 
B 1 206 HIS 206 215 215 HIS HIS B . n 
B 1 207 GLN 207 216 216 GLN GLN B . n 
B 1 208 ILE 208 217 217 ILE ILE B . n 
B 1 209 HIS 209 218 218 HIS HIS B . n 
B 1 210 ASP 210 219 219 ASP ASP B . n 
B 1 211 HIS 211 220 220 HIS HIS B . n 
B 1 212 VAL 212 221 221 VAL VAL B . n 
B 1 213 ASN 213 222 222 ASN ASN B . n 
B 1 214 PRO 214 223 223 PRO PRO B . n 
B 1 215 LYS 215 224 224 LYS LYS B . n 
B 1 216 ALA 216 225 225 ALA ALA B . n 
B 1 217 PHE 217 226 226 PHE PHE B . n 
B 1 218 PHE 218 227 227 PHE PHE B . n 
B 1 219 SER 219 228 228 SER SER B . n 
B 1 220 VAL 220 229 229 VAL VAL B . n 
B 1 221 LEU 221 230 230 LEU LEU B . n 
B 1 222 ARG 222 231 231 ARG ARG B . n 
B 1 223 ILE 223 232 232 ILE ILE B . n 
B 1 224 TYR 224 233 233 TYR TYR B . n 
B 1 225 LEU 225 234 234 LEU LEU B . n 
B 1 226 SER 226 235 235 SER SER B . n 
B 1 227 GLY 227 236 236 GLY GLY B . n 
B 1 228 TRP 228 237 237 TRP TRP B . n 
B 1 229 LYS 229 238 238 LYS LYS B . n 
B 1 230 GLY 230 239 239 GLY GLY B . n 
B 1 231 ASN 231 240 240 ASN ASN B . n 
B 1 232 PRO 232 241 241 PRO PRO B . n 
B 1 233 GLN 233 242 242 GLN GLN B . n 
B 1 234 LEU 234 243 243 LEU LEU B . n 
B 1 235 SER 235 244 244 SER SER B . n 
B 1 236 ASP 236 245 245 ASP ASP B . n 
B 1 237 GLY 237 246 246 GLY GLY B . n 
B 1 238 LEU 238 247 247 LEU LEU B . n 
B 1 239 VAL 239 248 248 VAL VAL B . n 
B 1 240 TYR 240 249 249 TYR TYR B . n 
B 1 241 GLU 241 250 250 GLU GLU B . n 
B 1 242 GLY 242 251 251 GLY GLY B . n 
B 1 243 PHE 243 252 252 PHE PHE B . n 
B 1 244 TRP 244 253 253 TRP TRP B . n 
B 1 245 GLU 245 254 254 GLU GLU B . n 
B 1 246 ASP 246 255 255 ASP ASP B . n 
B 1 247 PRO 247 256 256 PRO PRO B . n 
B 1 248 LYS 248 257 257 LYS LYS B . n 
B 1 249 GLU 249 258 258 GLU GLU B . n 
B 1 250 PHE 250 259 259 PHE PHE B . n 
B 1 251 ALA 251 260 260 ALA ALA B . n 
B 1 252 GLY 252 261 261 GLY GLY B . n 
B 1 253 GLY 253 262 262 GLY GLY B . n 
B 1 254 SER 254 263 263 SER SER B . n 
B 1 255 ALA 255 264 264 ALA ALA B . n 
B 1 256 GLY 256 265 265 GLY GLY B . n 
B 1 257 GLN 257 266 266 GLN GLN B . n 
B 1 258 SER 258 267 267 SER SER B . n 
B 1 259 SER 259 268 268 SER SER B . n 
B 1 260 VAL 260 269 269 VAL VAL B . n 
B 1 261 PHE 261 270 270 PHE PHE B . n 
B 1 262 GLN 262 271 271 GLN GLN B . n 
B 1 263 CYS 263 272 272 CYS CYS B . n 
B 1 264 PHE 264 273 273 PHE PHE B . n 
B 1 265 ASP 265 274 274 ASP ASP B . n 
B 1 266 VAL 266 275 275 VAL VAL B . n 
B 1 267 LEU 267 276 276 LEU LEU B . n 
B 1 268 LEU 268 277 277 LEU LEU B . n 
B 1 269 GLY 269 278 278 GLY GLY B . n 
B 1 270 ILE 270 279 279 ILE ILE B . n 
B 1 271 GLN 271 280 280 GLN GLN B . n 
B 1 272 GLN 272 281 281 GLN GLN B . n 
B 1 273 THR 273 282 282 THR THR B . n 
B 1 274 ALA 274 283 283 ALA ALA B . n 
B 1 275 GLY 275 284 284 GLY GLY B . n 
B 1 276 GLY 276 285 285 GLY GLY B . n 
B 1 277 GLY 277 286 286 GLY GLY B . n 
B 1 278 HIS 278 287 287 HIS HIS B . n 
B 1 279 ALA 279 288 288 ALA ALA B . n 
B 1 280 ALA 280 289 289 ALA ALA B . n 
B 1 281 GLN 281 290 290 GLN GLN B . n 
B 1 282 PHE 282 291 291 PHE PHE B . n 
B 1 283 LEU 283 292 292 LEU LEU B . n 
B 1 284 GLN 284 293 293 GLN GLN B . n 
B 1 285 ASP 285 294 294 ASP ASP B . n 
B 1 286 MET 286 295 295 MET MET B . n 
B 1 287 ARG 287 296 296 ARG ARG B . n 
B 1 288 ARG 288 297 297 ARG ARG B . n 
B 1 289 TYR 289 298 298 TYR TYR B . n 
B 1 290 MET 290 299 299 MET MET B . n 
B 1 291 PRO 291 300 300 PRO PRO B . n 
B 1 292 PRO 292 301 301 PRO PRO B . n 
B 1 293 ALA 293 302 302 ALA ALA B . n 
B 1 294 HIS 294 303 303 HIS HIS B . n 
B 1 295 ARG 295 304 304 ARG ARG B . n 
B 1 296 ASN 296 305 305 ASN ASN B . n 
B 1 297 PHE 297 306 306 PHE PHE B . n 
B 1 298 LEU 298 307 307 LEU LEU B . n 
B 1 299 CYS 299 308 308 CYS CYS B . n 
B 1 300 SER 300 309 309 SER SER B . n 
B 1 301 LEU 301 310 310 LEU LEU B . n 
B 1 302 GLU 302 311 311 GLU GLU B . n 
B 1 303 SER 303 312 312 SER SER B . n 
B 1 304 ASN 304 313 313 ASN ASN B . n 
B 1 305 PRO 305 314 314 PRO PRO B . n 
B 1 306 SER 306 315 315 SER SER B . n 
B 1 307 VAL 307 316 316 VAL VAL B . n 
B 1 308 ARG 308 317 317 ARG ARG B . n 
B 1 309 GLU 309 318 318 GLU GLU B . n 
B 1 310 PHE 310 319 319 PHE PHE B . n 
B 1 311 VAL 311 320 320 VAL VAL B . n 
B 1 312 LEU 312 321 321 LEU LEU B . n 
B 1 313 SER 313 322 322 SER SER B . n 
B 1 314 LYS 314 323 323 LYS LYS B . n 
B 1 315 GLY 315 324 324 GLY GLY B . n 
B 1 316 ASP 316 325 325 ASP ASP B . n 
B 1 317 ALA 317 326 326 ALA ALA B . n 
B 1 318 GLY 318 327 327 GLY GLY B . n 
B 1 319 LEU 319 328 328 LEU LEU B . n 
B 1 320 ARG 320 329 329 ARG ARG B . n 
B 1 321 GLU 321 330 330 GLU GLU B . n 
B 1 322 ALA 322 331 331 ALA ALA B . n 
B 1 323 TYR 323 332 332 TYR TYR B . n 
B 1 324 ASP 324 333 333 ASP ASP B . n 
B 1 325 ALA 325 334 334 ALA ALA B . n 
B 1 326 CYS 326 335 335 CYS CYS B . n 
B 1 327 VAL 327 336 336 VAL VAL B . n 
B 1 328 LYS 328 337 337 LYS LYS B . n 
B 1 329 ALA 329 338 338 ALA ALA B . n 
B 1 330 LEU 330 339 339 LEU LEU B . n 
B 1 331 VAL 331 340 340 VAL VAL B . n 
B 1 332 SER 332 341 341 SER SER B . n 
B 1 333 LEU 333 342 342 LEU LEU B . n 
B 1 334 ARG 334 343 343 ARG ARG B . n 
B 1 335 SER 335 344 344 SER SER B . n 
B 1 336 TYR 336 345 345 TYR TYR B . n 
B 1 337 HIS 337 346 346 HIS HIS B . n 
B 1 338 LEU 338 347 347 LEU LEU B . n 
B 1 339 GLN 339 348 348 GLN GLN B . n 
B 1 340 ILE 340 349 349 ILE ILE B . n 
B 1 341 VAL 341 350 350 VAL VAL B . n 
B 1 342 THR 342 351 351 THR THR B . n 
B 1 343 LYS 343 352 352 LYS LYS B . n 
B 1 344 TYR 344 353 353 TYR TYR B . n 
B 1 345 ILE 345 354 354 ILE ILE B . n 
B 1 346 LEU 346 355 355 LEU LEU B . n 
B 1 347 ILE 347 356 356 ILE ILE B . n 
B 1 348 PRO 348 357 357 PRO PRO B . n 
B 1 349 ALA 349 358 358 ALA ALA B . n 
B 1 350 SER 350 359 359 SER SER B . n 
B 1 351 GLN 351 360 360 GLN GLN B . n 
B 1 352 GLN 352 361 361 GLN GLN B . n 
B 1 353 PRO 353 362 ?   ?   ?   B . n 
B 1 354 LYS 354 363 ?   ?   ?   B . n 
B 1 355 GLU 355 364 ?   ?   ?   B . n 
B 1 356 ASN 356 365 ?   ?   ?   B . n 
B 1 357 LYS 357 366 ?   ?   ?   B . n 
B 1 358 THR 358 367 ?   ?   ?   B . n 
B 1 359 SER 359 368 ?   ?   ?   B . n 
B 1 360 GLU 360 369 ?   ?   ?   B . n 
B 1 361 ASP 361 370 ?   ?   ?   B . n 
B 1 362 PRO 362 371 ?   ?   ?   B . n 
B 1 363 SER 363 372 ?   ?   ?   B . n 
B 1 364 LYS 364 373 ?   ?   ?   B . n 
B 1 365 LEU 365 374 ?   ?   ?   B . n 
B 1 366 GLU 366 375 ?   ?   ?   B . n 
B 1 367 ALA 367 376 ?   ?   ?   B . n 
B 1 368 LYS 368 377 ?   ?   ?   B . n 
B 1 369 GLY 369 378 ?   ?   ?   B . n 
B 1 370 THR 370 379 ?   ?   ?   B . n 
B 1 371 GLY 371 380 ?   ?   ?   B . n 
B 1 372 GLY 372 381 381 GLY GLY B . n 
B 1 373 THR 373 382 382 THR THR B . n 
B 1 374 ASP 374 383 383 ASP ASP B . n 
B 1 375 LEU 375 384 384 LEU LEU B . n 
B 1 376 MET 376 385 385 MET MET B . n 
B 1 377 ASN 377 386 386 ASN ASN B . n 
B 1 378 PHE 378 387 387 PHE PHE B . n 
B 1 379 LEU 379 388 388 LEU LEU B . n 
B 1 380 LYS 380 389 389 LYS LYS B . n 
B 1 381 THR 381 390 390 THR THR B . n 
B 1 382 VAL 382 391 391 VAL VAL B . n 
B 1 383 ARG 383 392 392 ARG ARG B . n 
B 1 384 SER 384 393 393 SER SER B . n 
B 1 385 THR 385 394 394 THR THR B . n 
B 1 386 THR 386 395 395 THR THR B . n 
B 1 387 GLU 387 396 396 GLU GLU B . n 
B 1 388 LYS 388 397 397 LYS LYS B . n 
B 1 389 SER 389 398 398 SER SER B . n 
B 1 390 LEU 390 399 399 LEU LEU B . n 
B 1 391 LEU 391 400 400 LEU LEU B . n 
B 1 392 LYS 392 401 401 LYS LYS B . n 
B 1 393 GLU 393 402 ?   ?   ?   B . n 
B 1 394 GLY 394 403 ?   ?   ?   B . n 
# 
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 
C 2 C51 1 501 1 C51 LG1 A . 
D 2 C51 1 501 1 C51 LG1 B . 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_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_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2018-03-21 
2 'Structure model' 1 1 2018-04-11 
# 
_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_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
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[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 48.4604 -23.4364 89.8756  0.4556 0.4024 0.6568 -0.0487 -0.0148 0.1200  4.7283 3.2062 3.1292 
1.3816  1.3388  0.5509  -0.1580 0.5332  0.1216  0.0700  0.0835  -0.6402 -0.1817 0.6007  -0.3666 
'X-RAY DIFFRACTION' 2  ? refined 33.6529 -32.7396 89.3959  0.4672 0.3384 0.5149 0.0346  -0.0095 0.0027  4.7619 1.2180 2.2984 
1.6637  1.6999  0.2499  0.0395  0.1369  -0.0828 0.1852  -0.1450 0.0080  0.1603  0.1238  -0.0887 
'X-RAY DIFFRACTION' 3  ? refined 22.2770 -26.0038 87.8090  0.4022 0.4701 0.7514 -0.0255 -0.1675 -0.1135 5.4395 2.5743 4.1946 
2.9779  2.5481  0.7245  -0.4954 -0.8033 1.1022  -0.2384 -0.0844 0.3963  -0.0139 -0.8850 -0.0128 
'X-RAY DIFFRACTION' 4  ? refined 18.7346 -30.1219 85.7377  0.3858 0.4112 0.5838 -0.0494 -0.0660 -0.0372 2.4746 3.1240 3.6384 
0.9779  1.5825  0.4629  -0.1672 -0.0462 0.4282  -0.1287 -0.2883 0.2858  -0.2820 -0.3572 -0.2650 
'X-RAY DIFFRACTION' 5  ? refined 20.0363 -30.9039 101.6336 0.6921 1.1029 0.5861 -0.2179 0.1390  -0.0571 8.8589 4.0746 4.2796 
-1.1939 5.5681  0.9628  -0.5498 -2.0150 0.7719  0.5405  -0.5236 0.7558  -0.4452 -1.4007 -0.5536 
'X-RAY DIFFRACTION' 6  ? refined 9.4020  -6.3547  67.5881  0.6918 1.0388 0.5958 -0.0024 0.0634  -0.1368 6.4849 3.1092 2.6510 
-1.2804 -1.4287 -1.7220 0.4197  1.8547  0.6531  -0.4434 -0.3853 0.4787  -0.2722 -1.8810 -0.4733 
'X-RAY DIFFRACTION' 7  ? refined -8.4638 1.4233   83.6649  0.3677 1.8124 1.4407 0.0583  0.1079  -0.2351 0.4930 3.2253 3.8728 
-0.9692 1.2345  -3.3687 -0.4281 1.1061  -0.8658 0.6047  0.0722  0.9339  -0.7567 -0.6469 -0.4316 
'X-RAY DIFFRACTION' 8  ? refined -8.3699 -6.8871  86.1495  0.6809 1.5018 1.2831 -0.3142 0.1691  -0.2926 2.7178 4.6327 2.9222 
1.1234  2.7863  0.8580  -0.3785 0.0597  -1.6937 -0.3518 -0.4088 1.3879  0.2271  -1.3446 0.1501  
'X-RAY DIFFRACTION' 9  ? refined 1.2127  -2.3507  88.0722  0.4423 0.8616 0.6371 -0.0792 0.1246  -0.0586 3.8197 4.0185 7.1548 
-0.9794 -1.4362 0.9891  -0.1251 0.1668  -0.5953 0.4735  -0.3941 0.7530  0.3623  -2.0391 -0.2159 
'X-RAY DIFFRACTION' 10 ? refined 4.6084  0.6855   77.9155  0.4794 0.8556 0.7557 0.1504  0.0407  -0.0734 4.5506 2.2485 5.3184 
-0.7808 -0.5885 0.7136  0.1773  0.9504  0.4060  -0.2037 -0.6754 -0.0024 -0.0732 -1.0872 -0.5845 
'X-RAY DIFFRACTION' 11 ? refined 25.0093 1.6066   67.2133  0.4600 0.6742 0.4014 0.1111  0.0440  0.0953  3.0835 1.6424 4.1263 
0.2911  -2.1875 0.2113  0.4480  0.9737  0.3977  -0.6124 -0.2649 -0.0621 -0.2808 -0.6895 -0.0122 
'X-RAY DIFFRACTION' 12 ? refined 8.4311  -0.7506  94.0518  0.6070 0.8404 0.3312 -0.0490 0.1260  -0.0710 3.9405 4.0266 4.3666 
-0.9514 0.2337  0.6299  -0.0648 -0.7088 -0.0578 1.4575  -0.1901 0.5437  -0.3381 -0.3167 -0.0738 
'X-RAY DIFFRACTION' 13 ? refined 27.8291 -4.1934  77.3747  0.4750 0.4566 0.4631 0.0869  0.0461  -0.0751 1.8251 1.5757 2.6241 
-0.7903 -0.4380 -0.4458 0.0366  -0.0624 -0.2026 0.0815  -0.0663 -0.0794 0.2614  0.0704  -0.0548 
'X-RAY DIFFRACTION' 14 ? refined 28.8239 6.0266   87.7807  0.5736 0.5609 0.7825 0.0034  -0.0927 -0.1781 4.2695 4.8111 5.0295 
-2.5580 -2.1527 1.9357  0.0924  -0.6076 1.1165  0.1749  0.5395  -0.7806 -0.1941 0.0554  -0.1934 
# 
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.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 10 through 118 )
;
'X-RAY DIFFRACTION' 2  2  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 119 through 258 )
;
'X-RAY DIFFRACTION' 3  3  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 259 through 286 )
;
'X-RAY DIFFRACTION' 4  4  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 287 through 353 )
;
'X-RAY DIFFRACTION' 5  5  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 354 through 401 )
;
'X-RAY DIFFRACTION' 6  6  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 10 through 33 )
;
'X-RAY DIFFRACTION' 7  7  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 34 through 52 )
;
'X-RAY DIFFRACTION' 8  8  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 53 through 72 )
;
'X-RAY DIFFRACTION' 9  9  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 73 through 104 )
;
'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 105 through 159 )
;
'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 160 through 219 )
;
'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 220 through 258 )
;
'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 259 through 353 )
;
'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 354 through 401 )
;
# 
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 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.10.1_2155: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .                    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.22                 3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .                    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 HH B TYR 126 ? ? OE1 B GLU 171 ? ? 1.46 
2 1 HE B ARG 193 ? ? OD2 B ASP 325 ? ? 1.50 
3 1 O  A ILE 356 ? ? HG  A SER 359 ? ? 1.52 
4 1 HH A TYR 36  ? ? O   A SER 66  ? ? 1.54 
5 1 HH A TYR 126 ? ? OE2 A GLU 171 ? ? 1.54 
6 1 O  A PHE 163 ? ? HG  A SER 167 ? ? 1.57 
7 1 OH B TYR 126 ? ? OE1 B GLU 171 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A CYS 308 ? ? SG A CYS 308 ? ? 1.697 1.812 -0.115 0.016 N 
2 1 C  B PRO 121 ? ? N  B PRO 122 ? ? 1.478 1.338 0.140  0.019 Y 
3 1 CB B SER 267 ? ? OG B SER 267 ? ? 1.501 1.418 0.083  0.013 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 100 ? ? CZ A ARG 100 ? ? NH2 A ARG 100 ? ? 116.24 120.30 -4.06 0.50 N 
2 1 NE A ARG 105 ? ? CZ A ARG 105 ? ? NH2 A ARG 105 ? ? 117.24 120.30 -3.06 0.50 N 
# 
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 ASN A 27  ? ? 41.15   73.01  
2  1 PRO A 33  ? ? -47.68  151.33 
3  1 HIS A 45  ? ? -140.25 28.13  
4  1 THR A 71  ? ? -94.30  -62.00 
5  1 ASP A 128 ? ? -79.80  -74.52 
6  1 VAL A 130 ? ? -124.80 -50.20 
7  1 ASN A 133 ? ? -108.45 51.53  
8  1 CYS A 159 ? ? 59.41   19.10  
9  1 VAL A 229 ? ? -122.63 -68.38 
10 1 ILE A 354 ? ? -135.97 -56.24 
11 1 LEU A 400 ? ? -107.14 -62.91 
12 1 ASN B 27  ? ? 41.23   72.21  
13 1 PRO B 33  ? ? -45.95  156.74 
14 1 LYS B 61  ? ? -94.04  33.82  
15 1 THR B 71  ? ? -93.41  -62.22 
16 1 ASP B 128 ? ? -79.48  -70.16 
17 1 ASN B 133 ? ? -113.36 56.02  
18 1 VAL B 229 ? ? -122.32 -73.63 
19 1 ILE B 354 ? ? -130.04 -56.07 
20 1 LEU B 400 ? ? -109.34 -73.78 
# 
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 MET 10  ? CG  ? A MET 1   CG  
2   1 Y 1 A MET 10  ? SD  ? A MET 1   SD  
3   1 Y 1 A MET 10  ? CE  ? A MET 1   CE  
4   1 Y 1 A LYS 13  ? CG  ? A LYS 4   CG  
5   1 Y 1 A LYS 13  ? CD  ? A LYS 4   CD  
6   1 Y 1 A LYS 13  ? CE  ? A LYS 4   CE  
7   1 Y 1 A LYS 13  ? NZ  ? A LYS 4   NZ  
8   1 Y 1 A GLU 14  ? CD  ? A GLU 5   CD  
9   1 Y 1 A GLU 14  ? OE1 ? A GLU 5   OE1 
10  1 Y 1 A GLU 14  ? OE2 ? A GLU 5   OE2 
11  1 Y 1 A GLU 19  ? CG  ? A GLU 10  CG  
12  1 Y 1 A GLU 19  ? CD  ? A GLU 10  CD  
13  1 Y 1 A GLU 19  ? OE1 ? A GLU 10  OE1 
14  1 Y 1 A GLU 19  ? OE2 ? A GLU 10  OE2 
15  1 Y 1 A ASN 27  ? OD1 ? A ASN 18  OD1 
16  1 Y 1 A ASN 27  ? ND2 ? A ASN 18  ND2 
17  1 Y 1 A GLU 57  ? OE1 ? A GLU 48  OE1 
18  1 Y 1 A GLU 57  ? OE2 ? A GLU 48  OE2 
19  1 Y 1 A ASP 72  ? OD1 ? A ASP 63  OD1 
20  1 Y 1 A ASP 72  ? OD2 ? A ASP 63  OD2 
21  1 Y 1 A LYS 101 ? NZ  ? A LYS 92  NZ  
22  1 Y 1 A ASN 106 ? CG  ? A ASN 97  CG  
23  1 Y 1 A ASN 106 ? OD1 ? A ASN 97  OD1 
24  1 Y 1 A ASN 106 ? ND2 ? A ASN 97  ND2 
25  1 Y 1 A LYS 116 ? NZ  ? A LYS 107 NZ  
26  1 Y 1 A LYS 135 ? CE  ? A LYS 126 CE  
27  1 Y 1 A LYS 135 ? NZ  ? A LYS 126 NZ  
28  1 Y 1 A LYS 186 ? CG  ? A LYS 177 CG  
29  1 Y 1 A LYS 186 ? CD  ? A LYS 177 CD  
30  1 Y 1 A LYS 186 ? CE  ? A LYS 177 CE  
31  1 Y 1 A LYS 186 ? NZ  ? A LYS 177 NZ  
32  1 Y 1 A GLN 189 ? CG  ? A GLN 180 CG  
33  1 Y 1 A GLN 189 ? CD  ? A GLN 180 CD  
34  1 Y 1 A GLN 189 ? OE1 ? A GLN 180 OE1 
35  1 Y 1 A GLN 189 ? NE2 ? A GLN 180 NE2 
36  1 Y 1 A MET 190 ? SD  ? A MET 181 SD  
37  1 Y 1 A MET 190 ? CE  ? A MET 181 CE  
38  1 Y 1 A GLU 208 ? CG  ? A GLU 199 CG  
39  1 Y 1 A GLU 208 ? CD  ? A GLU 199 CD  
40  1 Y 1 A GLU 208 ? OE1 ? A GLU 199 OE1 
41  1 Y 1 A GLU 208 ? OE2 ? A GLU 199 OE2 
42  1 Y 1 A LYS 209 ? CD  ? A LYS 200 CD  
43  1 Y 1 A LYS 209 ? CE  ? A LYS 200 CE  
44  1 Y 1 A LYS 209 ? NZ  ? A LYS 200 NZ  
45  1 Y 1 A LYS 224 ? CG  ? A LYS 215 CG  
46  1 Y 1 A LYS 224 ? CD  ? A LYS 215 CD  
47  1 Y 1 A LYS 224 ? CE  ? A LYS 215 CE  
48  1 Y 1 A LYS 224 ? NZ  ? A LYS 215 NZ  
49  1 Y 1 A LYS 257 ? NZ  ? A LYS 248 NZ  
50  1 Y 1 A HIS 287 ? ND1 ? A HIS 278 ND1 
51  1 Y 1 A HIS 287 ? CD2 ? A HIS 278 CD2 
52  1 Y 1 A HIS 287 ? CE1 ? A HIS 278 CE1 
53  1 Y 1 A HIS 287 ? NE2 ? A HIS 278 NE2 
54  1 Y 1 A GLN 290 ? OE1 ? A GLN 281 OE1 
55  1 Y 1 A GLN 290 ? NE2 ? A GLN 281 NE2 
56  1 Y 1 A ARG 304 ? NE  ? A ARG 295 NE  
57  1 Y 1 A ARG 304 ? CZ  ? A ARG 295 CZ  
58  1 Y 1 A ARG 304 ? NH1 ? A ARG 295 NH1 
59  1 Y 1 A ARG 304 ? NH2 ? A ARG 295 NH2 
60  1 Y 1 A SER 309 ? OG  ? A SER 300 OG  
61  1 Y 1 A GLU 311 ? CD  ? A GLU 302 CD  
62  1 Y 1 A GLU 311 ? OE1 ? A GLU 302 OE1 
63  1 Y 1 A GLU 311 ? OE2 ? A GLU 302 OE2 
64  1 Y 1 A GLU 318 ? CD  ? A GLU 309 CD  
65  1 Y 1 A GLU 318 ? OE1 ? A GLU 309 OE1 
66  1 Y 1 A GLU 318 ? OE2 ? A GLU 309 OE2 
67  1 Y 1 A LYS 323 ? CE  ? A LYS 314 CE  
68  1 Y 1 A LYS 323 ? NZ  ? A LYS 314 NZ  
69  1 Y 1 A GLU 330 ? CD  ? A GLU 321 CD  
70  1 Y 1 A GLU 330 ? OE1 ? A GLU 321 OE1 
71  1 Y 1 A GLU 330 ? OE2 ? A GLU 321 OE2 
72  1 Y 1 A LYS 337 ? CG  ? A LYS 328 CG  
73  1 Y 1 A LYS 337 ? CD  ? A LYS 328 CD  
74  1 Y 1 A LYS 337 ? CE  ? A LYS 328 CE  
75  1 Y 1 A LYS 337 ? NZ  ? A LYS 328 NZ  
76  1 Y 1 A LEU 355 ? CD1 ? A LEU 346 CD1 
77  1 Y 1 A LEU 355 ? CD2 ? A LEU 346 CD2 
78  1 Y 1 A GLN 361 ? CG  ? A GLN 352 CG  
79  1 Y 1 A GLN 361 ? CD  ? A GLN 352 CD  
80  1 Y 1 A GLN 361 ? OE1 ? A GLN 352 OE1 
81  1 Y 1 A GLN 361 ? NE2 ? A GLN 352 NE2 
82  1 Y 1 A MET 385 ? CE  ? A MET 376 CE  
83  1 Y 1 A LYS 389 ? CD  ? A LYS 380 CD  
84  1 Y 1 A LYS 389 ? CE  ? A LYS 380 CE  
85  1 Y 1 A LYS 389 ? NZ  ? A LYS 380 NZ  
86  1 Y 1 A ARG 392 ? NH1 ? A ARG 383 NH1 
87  1 Y 1 A ARG 392 ? NH2 ? A ARG 383 NH2 
88  1 Y 1 A SER 393 ? OG  ? A SER 384 OG  
89  1 Y 1 A GLU 396 ? CG  ? A GLU 387 CG  
90  1 Y 1 A GLU 396 ? CD  ? A GLU 387 CD  
91  1 Y 1 A GLU 396 ? OE1 ? A GLU 387 OE1 
92  1 Y 1 A GLU 396 ? OE2 ? A GLU 387 OE2 
93  1 Y 1 A LYS 397 ? CG  ? A LYS 388 CG  
94  1 Y 1 A LYS 397 ? CD  ? A LYS 388 CD  
95  1 Y 1 A LYS 397 ? CE  ? A LYS 388 CE  
96  1 Y 1 A LYS 397 ? NZ  ? A LYS 388 NZ  
97  1 Y 1 A SER 398 ? OG  ? A SER 389 OG  
98  1 Y 1 A LYS 401 ? CG  ? A LYS 392 CG  
99  1 Y 1 A LYS 401 ? CD  ? A LYS 392 CD  
100 1 Y 1 A LYS 401 ? CE  ? A LYS 392 CE  
101 1 Y 1 A LYS 401 ? NZ  ? A LYS 392 NZ  
102 1 Y 1 B MET 10  ? CG  ? B MET 1   CG  
103 1 Y 1 B MET 10  ? SD  ? B MET 1   SD  
104 1 Y 1 B MET 10  ? CE  ? B MET 1   CE  
105 1 Y 1 B LYS 13  ? CG  ? B LYS 4   CG  
106 1 Y 1 B LYS 13  ? CD  ? B LYS 4   CD  
107 1 Y 1 B LYS 13  ? CE  ? B LYS 4   CE  
108 1 Y 1 B LYS 13  ? NZ  ? B LYS 4   NZ  
109 1 Y 1 B GLU 14  ? CD  ? B GLU 5   CD  
110 1 Y 1 B GLU 14  ? OE1 ? B GLU 5   OE1 
111 1 Y 1 B GLU 14  ? OE2 ? B GLU 5   OE2 
112 1 Y 1 B GLU 19  ? CG  ? B GLU 10  CG  
113 1 Y 1 B GLU 19  ? CD  ? B GLU 10  CD  
114 1 Y 1 B GLU 19  ? OE1 ? B GLU 10  OE1 
115 1 Y 1 B GLU 19  ? OE2 ? B GLU 10  OE2 
116 1 Y 1 B GLU 20  ? CD  ? B GLU 11  CD  
117 1 Y 1 B GLU 20  ? OE1 ? B GLU 11  OE1 
118 1 Y 1 B GLU 20  ? OE2 ? B GLU 11  OE2 
119 1 Y 1 B ASN 27  ? OD1 ? B ASN 18  OD1 
120 1 Y 1 B ASN 27  ? ND2 ? B ASN 18  ND2 
121 1 Y 1 B GLU 30  ? CD  ? B GLU 21  CD  
122 1 Y 1 B GLU 30  ? OE1 ? B GLU 21  OE1 
123 1 Y 1 B GLU 30  ? OE2 ? B GLU 21  OE2 
124 1 Y 1 B LEU 32  ? CG  ? B LEU 23  CG  
125 1 Y 1 B LEU 32  ? CD1 ? B LEU 23  CD1 
126 1 Y 1 B LEU 32  ? CD2 ? B LEU 23  CD2 
127 1 Y 1 B PHE 41  ? CG  ? B PHE 32  CG  
128 1 Y 1 B PHE 41  ? CD1 ? B PHE 32  CD1 
129 1 Y 1 B PHE 41  ? CD2 ? B PHE 32  CD2 
130 1 Y 1 B PHE 41  ? CE1 ? B PHE 32  CE1 
131 1 Y 1 B PHE 41  ? CE2 ? B PHE 32  CE2 
132 1 Y 1 B PHE 41  ? CZ  ? B PHE 32  CZ  
133 1 Y 1 B LYS 44  ? CG  ? B LYS 35  CG  
134 1 Y 1 B LYS 44  ? CD  ? B LYS 35  CD  
135 1 Y 1 B LYS 44  ? CE  ? B LYS 35  CE  
136 1 Y 1 B LYS 44  ? NZ  ? B LYS 35  NZ  
137 1 Y 1 B LEU 46  ? CG  ? B LEU 37  CG  
138 1 Y 1 B LEU 46  ? CD1 ? B LEU 37  CD1 
139 1 Y 1 B LEU 46  ? CD2 ? B LEU 37  CD2 
140 1 Y 1 B ASP 48  ? OD1 ? B ASP 39  OD1 
141 1 Y 1 B ASP 48  ? OD2 ? B ASP 39  OD2 
142 1 Y 1 B GLU 51  ? OE1 ? B GLU 42  OE1 
143 1 Y 1 B GLU 51  ? OE2 ? B GLU 42  OE2 
144 1 Y 1 B GLN 54  ? CG  ? B GLN 45  CG  
145 1 Y 1 B GLN 54  ? CD  ? B GLN 45  CD  
146 1 Y 1 B GLN 54  ? OE1 ? B GLN 45  OE1 
147 1 Y 1 B GLN 54  ? NE2 ? B GLN 45  NE2 
148 1 Y 1 B GLU 57  ? CG  ? B GLU 48  CG  
149 1 Y 1 B GLU 57  ? CD  ? B GLU 48  CD  
150 1 Y 1 B GLU 57  ? OE1 ? B GLU 48  OE1 
151 1 Y 1 B GLU 57  ? OE2 ? B GLU 48  OE2 
152 1 Y 1 B LYS 61  ? CG  ? B LYS 52  CG  
153 1 Y 1 B LYS 61  ? CD  ? B LYS 52  CD  
154 1 Y 1 B LYS 61  ? CE  ? B LYS 52  CE  
155 1 Y 1 B LYS 61  ? NZ  ? B LYS 52  NZ  
156 1 Y 1 B MET 64  ? CE  ? B MET 55  CE  
157 1 Y 1 B LYS 94  ? CD  ? B LYS 85  CD  
158 1 Y 1 B LYS 94  ? CE  ? B LYS 85  CE  
159 1 Y 1 B LYS 94  ? NZ  ? B LYS 85  NZ  
160 1 Y 1 B ASP 98  ? CG  ? B ASP 89  CG  
161 1 Y 1 B ASP 98  ? OD1 ? B ASP 89  OD1 
162 1 Y 1 B ASP 98  ? OD2 ? B ASP 89  OD2 
163 1 Y 1 B ARG 100 ? CD  ? B ARG 91  CD  
164 1 Y 1 B ARG 100 ? NE  ? B ARG 91  NE  
165 1 Y 1 B ARG 100 ? CZ  ? B ARG 91  CZ  
166 1 Y 1 B ARG 100 ? NH1 ? B ARG 91  NH1 
167 1 Y 1 B ARG 100 ? NH2 ? B ARG 91  NH2 
168 1 Y 1 B LYS 101 ? CD  ? B LYS 92  CD  
169 1 Y 1 B LYS 101 ? CE  ? B LYS 92  CE  
170 1 Y 1 B LYS 101 ? NZ  ? B LYS 92  NZ  
171 1 Y 1 B ARG 105 ? CG  ? B ARG 96  CG  
172 1 Y 1 B ARG 105 ? CD  ? B ARG 96  CD  
173 1 Y 1 B ARG 105 ? NE  ? B ARG 96  NE  
174 1 Y 1 B ARG 105 ? CZ  ? B ARG 96  CZ  
175 1 Y 1 B ARG 105 ? NH1 ? B ARG 96  NH1 
176 1 Y 1 B ARG 105 ? NH2 ? B ARG 96  NH2 
177 1 Y 1 B ASN 106 ? CG  ? B ASN 97  CG  
178 1 Y 1 B ASN 106 ? OD1 ? B ASN 97  OD1 
179 1 Y 1 B ASN 106 ? ND2 ? B ASN 97  ND2 
180 1 Y 1 B GLN 113 ? OE1 ? B GLN 104 OE1 
181 1 Y 1 B GLN 113 ? NE2 ? B GLN 104 NE2 
182 1 Y 1 B LYS 116 ? CD  ? B LYS 107 CD  
183 1 Y 1 B LYS 116 ? CE  ? B LYS 107 CE  
184 1 Y 1 B LYS 116 ? NZ  ? B LYS 107 NZ  
185 1 Y 1 B LYS 117 ? CG  ? B LYS 108 CG  
186 1 Y 1 B LYS 117 ? CD  ? B LYS 108 CD  
187 1 Y 1 B LYS 117 ? CE  ? B LYS 108 CE  
188 1 Y 1 B LYS 117 ? NZ  ? B LYS 108 NZ  
189 1 Y 1 B LYS 135 ? CG  ? B LYS 126 CG  
190 1 Y 1 B LYS 135 ? CD  ? B LYS 126 CD  
191 1 Y 1 B LYS 135 ? CE  ? B LYS 126 CE  
192 1 Y 1 B LYS 135 ? NZ  ? B LYS 126 NZ  
193 1 Y 1 B LYS 136 ? CG  ? B LYS 127 CG  
194 1 Y 1 B LYS 136 ? CD  ? B LYS 127 CD  
195 1 Y 1 B LYS 136 ? CE  ? B LYS 127 CE  
196 1 Y 1 B LYS 136 ? NZ  ? B LYS 127 NZ  
197 1 Y 1 B LYS 141 ? CG  ? B LYS 132 CG  
198 1 Y 1 B LYS 141 ? CD  ? B LYS 132 CD  
199 1 Y 1 B LYS 141 ? CE  ? B LYS 132 CE  
200 1 Y 1 B LYS 141 ? NZ  ? B LYS 132 NZ  
201 1 Y 1 B ASP 149 ? OD1 ? B ASP 140 OD1 
202 1 Y 1 B ASP 149 ? OD2 ? B ASP 140 OD2 
203 1 Y 1 B LYS 161 ? CG  ? B LYS 152 CG  
204 1 Y 1 B LYS 161 ? CD  ? B LYS 152 CD  
205 1 Y 1 B LYS 161 ? CE  ? B LYS 152 CE  
206 1 Y 1 B LYS 161 ? NZ  ? B LYS 152 NZ  
207 1 Y 1 B LYS 179 ? NZ  ? B LYS 170 NZ  
208 1 Y 1 B LYS 186 ? NZ  ? B LYS 177 NZ  
209 1 Y 1 B GLN 189 ? CD  ? B GLN 180 CD  
210 1 Y 1 B GLN 189 ? OE1 ? B GLN 180 OE1 
211 1 Y 1 B GLN 189 ? NE2 ? B GLN 180 NE2 
212 1 Y 1 B MET 190 ? SD  ? B MET 181 SD  
213 1 Y 1 B MET 190 ? CE  ? B MET 181 CE  
214 1 Y 1 B LYS 198 ? CD  ? B LYS 189 CD  
215 1 Y 1 B LYS 198 ? CE  ? B LYS 189 CE  
216 1 Y 1 B LYS 198 ? NZ  ? B LYS 189 NZ  
217 1 Y 1 B GLU 208 ? CD  ? B GLU 199 CD  
218 1 Y 1 B GLU 208 ? OE1 ? B GLU 199 OE1 
219 1 Y 1 B GLU 208 ? OE2 ? B GLU 199 OE2 
220 1 Y 1 B LYS 209 ? CD  ? B LYS 200 CD  
221 1 Y 1 B LYS 209 ? CE  ? B LYS 200 CE  
222 1 Y 1 B LYS 209 ? NZ  ? B LYS 200 NZ  
223 1 Y 1 B ASN 222 ? OD1 ? B ASN 213 OD1 
224 1 Y 1 B ASN 222 ? ND2 ? B ASN 213 ND2 
225 1 Y 1 B LYS 224 ? CG  ? B LYS 215 CG  
226 1 Y 1 B LYS 224 ? CD  ? B LYS 215 CD  
227 1 Y 1 B LYS 224 ? CE  ? B LYS 215 CE  
228 1 Y 1 B LYS 224 ? NZ  ? B LYS 215 NZ  
229 1 Y 1 B LYS 238 ? CD  ? B LYS 229 CD  
230 1 Y 1 B LYS 238 ? CE  ? B LYS 229 CE  
231 1 Y 1 B LYS 238 ? NZ  ? B LYS 229 NZ  
232 1 Y 1 B GLU 254 ? CG  ? B GLU 245 CG  
233 1 Y 1 B GLU 254 ? CD  ? B GLU 245 CD  
234 1 Y 1 B GLU 254 ? OE1 ? B GLU 245 OE1 
235 1 Y 1 B GLU 254 ? OE2 ? B GLU 245 OE2 
236 1 Y 1 B LYS 257 ? CE  ? B LYS 248 CE  
237 1 Y 1 B LYS 257 ? NZ  ? B LYS 248 NZ  
238 1 Y 1 B HIS 287 ? ND1 ? B HIS 278 ND1 
239 1 Y 1 B HIS 287 ? CD2 ? B HIS 278 CD2 
240 1 Y 1 B HIS 287 ? CE1 ? B HIS 278 CE1 
241 1 Y 1 B HIS 287 ? NE2 ? B HIS 278 NE2 
242 1 Y 1 B GLN 290 ? CG  ? B GLN 281 CG  
243 1 Y 1 B GLN 290 ? CD  ? B GLN 281 CD  
244 1 Y 1 B GLN 290 ? OE1 ? B GLN 281 OE1 
245 1 Y 1 B GLN 290 ? NE2 ? B GLN 281 NE2 
246 1 Y 1 B ASP 294 ? CG  ? B ASP 285 CG  
247 1 Y 1 B ASP 294 ? OD1 ? B ASP 285 OD1 
248 1 Y 1 B ASP 294 ? OD2 ? B ASP 285 OD2 
249 1 Y 1 B ARG 297 ? CG  ? B ARG 288 CG  
250 1 Y 1 B ARG 297 ? CD  ? B ARG 288 CD  
251 1 Y 1 B ARG 297 ? NE  ? B ARG 288 NE  
252 1 Y 1 B ARG 297 ? CZ  ? B ARG 288 CZ  
253 1 Y 1 B ARG 297 ? NH1 ? B ARG 288 NH1 
254 1 Y 1 B ARG 297 ? NH2 ? B ARG 288 NH2 
255 1 Y 1 B GLU 318 ? CG  ? B GLU 309 CG  
256 1 Y 1 B GLU 318 ? CD  ? B GLU 309 CD  
257 1 Y 1 B GLU 318 ? OE1 ? B GLU 309 OE1 
258 1 Y 1 B GLU 318 ? OE2 ? B GLU 309 OE2 
259 1 Y 1 B LYS 323 ? CE  ? B LYS 314 CE  
260 1 Y 1 B LYS 323 ? NZ  ? B LYS 314 NZ  
261 1 Y 1 B GLU 330 ? CD  ? B GLU 321 CD  
262 1 Y 1 B GLU 330 ? OE1 ? B GLU 321 OE1 
263 1 Y 1 B GLU 330 ? OE2 ? B GLU 321 OE2 
264 1 Y 1 B LYS 337 ? CG  ? B LYS 328 CG  
265 1 Y 1 B LYS 337 ? CD  ? B LYS 328 CD  
266 1 Y 1 B LYS 337 ? CE  ? B LYS 328 CE  
267 1 Y 1 B LYS 337 ? NZ  ? B LYS 328 NZ  
268 1 Y 1 B LYS 352 ? CD  ? B LYS 343 CD  
269 1 Y 1 B LYS 352 ? CE  ? B LYS 343 CE  
270 1 Y 1 B LYS 352 ? NZ  ? B LYS 343 NZ  
271 1 Y 1 B GLN 361 ? CG  ? B GLN 352 CG  
272 1 Y 1 B GLN 361 ? CD  ? B GLN 352 CD  
273 1 Y 1 B GLN 361 ? OE1 ? B GLN 352 OE1 
274 1 Y 1 B GLN 361 ? NE2 ? B GLN 352 NE2 
275 1 Y 1 B ASP 383 ? OD1 ? B ASP 374 OD1 
276 1 Y 1 B ASP 383 ? OD2 ? B ASP 374 OD2 
277 1 Y 1 B LYS 397 ? CE  ? B LYS 388 CE  
278 1 Y 1 B LYS 397 ? NZ  ? B LYS 388 NZ  
279 1 Y 1 B LYS 401 ? CG  ? B LYS 392 CG  
280 1 Y 1 B LYS 401 ? CD  ? B LYS 392 CD  
281 1 Y 1 B LYS 401 ? CE  ? B LYS 392 CE  
282 1 Y 1 B LYS 401 ? NZ  ? B LYS 392 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 LYS 363 ? A LYS 354 
2  1 Y 1 A GLU 364 ? A GLU 355 
3  1 Y 1 A ASN 365 ? A ASN 356 
4  1 Y 1 A LYS 366 ? A LYS 357 
5  1 Y 1 A THR 367 ? A THR 358 
6  1 Y 1 A SER 368 ? A SER 359 
7  1 Y 1 A GLU 369 ? A GLU 360 
8  1 Y 1 A ASP 370 ? A ASP 361 
9  1 Y 1 A PRO 371 ? A PRO 362 
10 1 Y 1 A SER 372 ? A SER 363 
11 1 Y 1 A LYS 373 ? A LYS 364 
12 1 Y 1 A LEU 374 ? A LEU 365 
13 1 Y 1 A GLU 375 ? A GLU 366 
14 1 Y 1 A ALA 376 ? A ALA 367 
15 1 Y 1 A LYS 377 ? A LYS 368 
16 1 Y 1 A GLY 378 ? A GLY 369 
17 1 Y 1 A THR 379 ? A THR 370 
18 1 Y 1 A GLU 402 ? A GLU 393 
19 1 Y 1 A GLY 403 ? A GLY 394 
20 1 Y 1 B PRO 362 ? B PRO 353 
21 1 Y 1 B LYS 363 ? B LYS 354 
22 1 Y 1 B GLU 364 ? B GLU 355 
23 1 Y 1 B ASN 365 ? B ASN 356 
24 1 Y 1 B LYS 366 ? B LYS 357 
25 1 Y 1 B THR 367 ? B THR 358 
26 1 Y 1 B SER 368 ? B SER 359 
27 1 Y 1 B GLU 369 ? B GLU 360 
28 1 Y 1 B ASP 370 ? B ASP 361 
29 1 Y 1 B PRO 371 ? B PRO 362 
30 1 Y 1 B SER 372 ? B SER 363 
31 1 Y 1 B LYS 373 ? B LYS 364 
32 1 Y 1 B LEU 374 ? B LEU 365 
33 1 Y 1 B GLU 375 ? B GLU 366 
34 1 Y 1 B ALA 376 ? B ALA 367 
35 1 Y 1 B LYS 377 ? B LYS 368 
36 1 Y 1 B GLY 378 ? B GLY 369 
37 1 Y 1 B THR 379 ? B THR 370 
38 1 Y 1 B GLY 380 ? B GLY 371 
39 1 Y 1 B GLU 402 ? B GLU 393 
40 1 Y 1 B GLY 403 ? B GLY 394 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        '(2R)-N-(4-cyanophenyl)-2-[cis-4-(quinolin-4-yl)cyclohexyl]propanamide' 
_pdbx_entity_nonpoly.comp_id     C51 
# 
_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                ? 
# 
