data_1CPJ
# 
_entry.id   1CPJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1CPJ         
WWPDB D_1000172458 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1CPJ 
_pdbx_database_status.recvd_initial_deposition_date   1995-07-17 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Huber, C.P.' 1 
'Jia, Z.'     2 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
;Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
;
J.Biol.Chem. 270 5527 5533 1995 JBCHA3 US 0021-9258 0071 ? 7890671 10.1074/jbc.270.10.5527 
1       'Crystallization of Recombinant Rat Cathepsin B' J.Biol.Chem. 265 5950 ?    1990 JBCHA3 US 0021-9258 0071 ? ?       ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Jia, Z.'     1  
primary 'Hasnain, S.' 2  
primary 'Hirama, T.'  3  
primary 'Lee, X.'     4  
primary 'Mort, J.S.'  5  
primary 'To, R.'      6  
primary 'Huber, C.P.' 7  
1       'Lee, X.'     8  
1       'Ahmed, F.R.' 9  
1       'Hirama, T.'  10 
1       'Huber, C.P.' 11 
1       'Rose, D.R.'  12 
1       'To, R.'      13 
1       'Hasnain, S.' 14 
1       'Tam, A.'     15 
1       'Mort, J.S.'  16 
# 
_cell.entry_id           1CPJ 
_cell.length_a           47.090 
_cell.length_b           90.250 
_cell.length_c           62.100 
_cell.angle_alpha        90.00 
_cell.angle_beta         97.29 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1CPJ 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 'CATHEPSIN B' 28441.562 2   3.4.22.1 S115A ? ? 
2 water   nat water         18.015    190 ?        ?     ? ? 
# 
_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       
;FSEDINLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGG
YPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGARPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVS
DSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNADWGDNGFFKIL
RGENHCGIESEIVAGIPRTQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FSEDINLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGG
YPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGARPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVS
DSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNADWGDNGFFKIL
RGENHCGIESEIVAGIPRTQ
;
_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   PHE n 
1 2   SER n 
1 3   GLU n 
1 4   ASP n 
1 5   ILE n 
1 6   ASN n 
1 7   LEU n 
1 8   PRO n 
1 9   GLU n 
1 10  SER n 
1 11  PHE n 
1 12  ASP n 
1 13  ALA n 
1 14  ARG n 
1 15  GLU n 
1 16  GLN n 
1 17  TRP n 
1 18  SER n 
1 19  ASN n 
1 20  CYS n 
1 21  PRO n 
1 22  THR n 
1 23  ILE n 
1 24  ALA n 
1 25  GLN n 
1 26  ILE n 
1 27  ARG n 
1 28  ASP n 
1 29  GLN n 
1 30  GLY n 
1 31  SER n 
1 32  CYS n 
1 33  GLY n 
1 34  SER n 
1 35  CYS n 
1 36  TRP n 
1 37  ALA n 
1 38  PHE n 
1 39  GLY n 
1 40  ALA n 
1 41  VAL n 
1 42  GLU n 
1 43  ALA n 
1 44  MET n 
1 45  SER n 
1 46  ASP n 
1 47  ARG n 
1 48  ILE n 
1 49  CYS n 
1 50  ILE n 
1 51  HIS n 
1 52  THR n 
1 53  ASN n 
1 54  GLY n 
1 55  ARG n 
1 56  VAL n 
1 57  ASN n 
1 58  VAL n 
1 59  GLU n 
1 60  VAL n 
1 61  SER n 
1 62  ALA n 
1 63  GLU n 
1 64  ASP n 
1 65  LEU n 
1 66  LEU n 
1 67  THR n 
1 68  CYS n 
1 69  CYS n 
1 70  GLY n 
1 71  ILE n 
1 72  GLN n 
1 73  CYS n 
1 74  GLY n 
1 75  ASP n 
1 76  GLY n 
1 77  CYS n 
1 78  ASN n 
1 79  GLY n 
1 80  GLY n 
1 81  TYR n 
1 82  PRO n 
1 83  SER n 
1 84  GLY n 
1 85  ALA n 
1 86  TRP n 
1 87  ASN n 
1 88  PHE n 
1 89  TRP n 
1 90  THR n 
1 91  ARG n 
1 92  LYS n 
1 93  GLY n 
1 94  LEU n 
1 95  VAL n 
1 96  SER n 
1 97  GLY n 
1 98  GLY n 
1 99  VAL n 
1 100 TYR n 
1 101 ASN n 
1 102 SER n 
1 103 HIS n 
1 104 ILE n 
1 105 GLY n 
1 106 CYS n 
1 107 LEU n 
1 108 PRO n 
1 109 TYR n 
1 110 THR n 
1 111 ILE n 
1 112 PRO n 
1 113 PRO n 
1 114 CYS n 
1 115 GLU n 
1 116 HIS n 
1 117 HIS n 
1 118 VAL n 
1 119 ASN n 
1 120 GLY n 
1 121 ALA n 
1 122 ARG n 
1 123 PRO n 
1 124 PRO n 
1 125 CYS n 
1 126 THR n 
1 127 GLY n 
1 128 GLU n 
1 129 GLY n 
1 130 ASP n 
1 131 THR n 
1 132 PRO n 
1 133 LYS n 
1 134 CYS n 
1 135 ASN n 
1 136 LYS n 
1 137 MET n 
1 138 CYS n 
1 139 GLU n 
1 140 ALA n 
1 141 GLY n 
1 142 TYR n 
1 143 SER n 
1 144 THR n 
1 145 SER n 
1 146 TYR n 
1 147 LYS n 
1 148 GLU n 
1 149 ASP n 
1 150 LYS n 
1 151 HIS n 
1 152 TYR n 
1 153 GLY n 
1 154 TYR n 
1 155 THR n 
1 156 SER n 
1 157 TYR n 
1 158 SER n 
1 159 VAL n 
1 160 SER n 
1 161 ASP n 
1 162 SER n 
1 163 GLU n 
1 164 LYS n 
1 165 GLU n 
1 166 ILE n 
1 167 MET n 
1 168 ALA n 
1 169 GLU n 
1 170 ILE n 
1 171 TYR n 
1 172 LYS n 
1 173 ASN n 
1 174 GLY n 
1 175 PRO n 
1 176 VAL n 
1 177 GLU n 
1 178 GLY n 
1 179 ALA n 
1 180 PHE n 
1 181 THR n 
1 182 VAL n 
1 183 PHE n 
1 184 SER n 
1 185 ASP n 
1 186 PHE n 
1 187 LEU n 
1 188 THR n 
1 189 TYR n 
1 190 LYS n 
1 191 SER n 
1 192 GLY n 
1 193 VAL n 
1 194 TYR n 
1 195 LYS n 
1 196 HIS n 
1 197 GLU n 
1 198 ALA n 
1 199 GLY n 
1 200 ASP n 
1 201 VAL n 
1 202 MET n 
1 203 GLY n 
1 204 GLY n 
1 205 HIS n 
1 206 ALA n 
1 207 ILE n 
1 208 ARG n 
1 209 ILE n 
1 210 LEU n 
1 211 GLY n 
1 212 TRP n 
1 213 GLY n 
1 214 ILE n 
1 215 GLU n 
1 216 ASN n 
1 217 GLY n 
1 218 VAL n 
1 219 PRO n 
1 220 TYR n 
1 221 TRP n 
1 222 LEU n 
1 223 VAL n 
1 224 ALA n 
1 225 ASN n 
1 226 SER n 
1 227 TRP n 
1 228 ASN n 
1 229 ALA n 
1 230 ASP n 
1 231 TRP n 
1 232 GLY n 
1 233 ASP n 
1 234 ASN n 
1 235 GLY n 
1 236 PHE n 
1 237 PHE n 
1 238 LYS n 
1 239 ILE n 
1 240 LEU n 
1 241 ARG n 
1 242 GLY n 
1 243 GLU n 
1 244 ASN n 
1 245 HIS n 
1 246 CYS n 
1 247 GLY n 
1 248 ILE n 
1 249 GLU n 
1 250 SER n 
1 251 GLU n 
1 252 ILE n 
1 253 VAL n 
1 254 ALA n 
1 255 GLY n 
1 256 ILE n 
1 257 PRO n 
1 258 ARG n 
1 259 THR n 
1 260 GLN 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     Rattus 
_entity_src_gen.pdbx_gene_src_gene                 CDNA 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_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               
;baker's yeast
;
_entity_src_gen.pdbx_host_org_scientific_name      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     Saccharomyces 
_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          PLASMID 
_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                    CATB_RAT 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00787 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MWWSLIPLSCLLALTSAHDKPSSHPLSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPNLPERVGFSEDINL
PESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWN
FWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEIM
AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCG
IESEIVAGIPRTQQYWGRF
;
_struct_ref.pdbx_db_isoform            ? 
# 
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 1CPJ A 1 ? 260 ? P00787 74 ? 333 ? -5 254 
2 1 1CPJ B 1 ? 260 ? P00787 74 ? 333 ? -5 254 
# 
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 1CPJ ALA A 121 ? UNP P00787 SER 194 ENGINEERED         115 1 
1 1CPJ ALA A 229 ? UNP P00787 VAL 302 'CLONING ARTIFACT' 223 2 
2 1CPJ ALA B 121 ? UNP P00787 SER 194 ENGINEERED         115 3 
2 1CPJ ALA B 229 ? UNP P00787 VAL 302 'CLONING ARTIFACT' 223 4 
# 
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 
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 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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.entry_id          1CPJ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.52 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'AREA DETECTOR' 
_diffrn_detector.type                   'XUONG-HAMLIN MULTIWIRE' 
_diffrn_detector.pdbx_collection_date   1992-12 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      ? 
_diffrn_source.type                        ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1CPJ 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20.0 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   24886 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         90.7 
_reflns.pdbx_Rmerge_I_obs            0.095 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_refine.entry_id                                 1CPJ 
_refine.ls_number_reflns_obs                     23373 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2. 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             8.0 
_refine.ls_d_res_high                            2.2 
_refine.ls_percent_reflns_obs                    93.9 
_refine.ls_R_factor_obs                          0.175 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.175 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               21.5 
_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                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;RESIDUE ASN 222 OF BOTH CHAINS HAS PHI-PSI ANGLES OUTSIDE
THE NORMALLY PERMITTED RANGE BECAUSE ITS SIDE CHAIN OXYGEN
ATOM IS INVOLVED IN A HYDROGEN BOND WITH THE ADJACENT
MAIN-CHAIN N-H 223.
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_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_analyze.entry_id                        1CPJ 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3868 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             190 
_refine_hist.number_atoms_total               4058 
_refine_hist.d_res_high                       2.2 
_refine_hist.d_res_low                        8.0 
# 
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 
x_bond_d                0.012 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             1.3   ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   0.633800 
_struct_ncs_oper.matrix[1][2]   0.738600 
_struct_ncs_oper.matrix[1][3]   0.229700 
_struct_ncs_oper.matrix[2][1]   0.739400 
_struct_ncs_oper.matrix[2][2]   -0.665700 
_struct_ncs_oper.matrix[2][3]   0.100200 
_struct_ncs_oper.matrix[3][1]   0.226900 
_struct_ncs_oper.matrix[3][2]   0.106400 
_struct_ncs_oper.matrix[3][3]   -0.968100 
_struct_ncs_oper.vector[1]      -52.75100 
_struct_ncs_oper.vector[2]      88.13200 
_struct_ncs_oper.vector[3]      93.84400 
# 
_struct.entry_id                  1CPJ 
_struct.title                     
;CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
;
_struct.pdbx_descriptor           'CATHEPSIN B' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1CPJ 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'THIOL PROTEASE, HYDROLASE' 
# 
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 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               
;MTRIX
 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
 VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE
 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
 SECOND.

           APPLIED TO           TRANSFORMED TO
 MTRIX      RESIDUES               RESIDUES         RMSD
   M1   A    1  ..  A  253     B    1  ..  B  253   0.457
;
_struct_biol.pdbx_parent_biol_id   ? 
# 
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 3  CYS A 35  ? THR A 52  ? CYS A 29  THR A 46  1 ? 18 
HELX_P HELX_P2 4  ALA A 62  ? CYS A 68  ? ALA A 56  CYS A 62  1 ? 7  
HELX_P HELX_P3 6  PRO A 82  ? ARG A 91  ? PRO A 76  ARG A 85  1 ? 10 
HELX_P HELX_P4 7  GLU A 163 ? ASN A 173 ? GLU A 157 ASN A 167 1 ? 11 
HELX_P HELX_P5 12 CYS B 35  ? HIS B 51  ? CYS B 29  HIS B 45  1 ? 17 
HELX_P HELX_P6 13 ALA B 62  ? CYS B 68  ? ALA B 56  CYS B 62  1 ? 7  
HELX_P HELX_P7 15 PRO B 82  ? LYS B 92  ? PRO B 76  LYS B 86  1 ? 11 
HELX_P HELX_P8 17 GLU B 163 ? ASN B 173 ? GLU B 157 ASN B 167 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 20  SG ? ? ? 1_555 A CYS 49  SG ? ? A CYS 14  A CYS 43  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf2  disulf ? ? A CYS 32  SG ? ? ? 1_555 A CYS 77  SG ? ? A CYS 26  A CYS 71  1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf3  disulf ? ? A CYS 68  SG ? ? ? 1_555 A CYS 134 SG ? ? A CYS 62  A CYS 128 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf4  disulf ? ? A CYS 69  SG ? ? ? 1_555 A CYS 73  SG ? ? A CYS 63  A CYS 67  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf5  disulf ? ? A CYS 106 SG ? ? ? 1_555 A CYS 138 SG ? ? A CYS 100 A CYS 132 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf6  disulf ? ? A CYS 114 SG ? ? ? 1_555 A CYS 125 SG ? ? A CYS 108 A CYS 119 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf7  disulf ? ? B CYS 20  SG ? ? ? 1_555 B CYS 49  SG ? ? B CYS 14  B CYS 43  1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf8  disulf ? ? B CYS 32  SG ? ? ? 1_555 B CYS 77  SG ? ? B CYS 26  B CYS 71  1_555 ? ? ? ? ? ? ? 2.022 ? 
disulf9  disulf ? ? B CYS 68  SG ? ? ? 1_555 B CYS 134 SG ? ? B CYS 62  B CYS 128 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf10 disulf ? ? B CYS 69  SG ? ? ? 1_555 B CYS 73  SG ? ? B CYS 63  B CYS 67  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf11 disulf ? ? B CYS 106 SG ? ? ? 1_555 B CYS 138 SG ? ? B CYS 100 B CYS 132 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf12 disulf ? ? B CYS 114 SG ? ? ? 1_555 B CYS 125 SG ? ? B CYS 108 B CYS 119 1_555 ? ? ? ? ? ? ? 2.024 ? 
# 
_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 
SA1 ? 6 ? 
SA2 ? 4 ? 
SB1 ? 6 ? 
SB2 ? 4 ? 
# 
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 
SA1 1 2 ? anti-parallel 
SA1 2 3 ? anti-parallel 
SA1 3 4 ? anti-parallel 
SA1 4 5 ? anti-parallel 
SA1 5 6 ? anti-parallel 
SA2 1 2 ? anti-parallel 
SA2 2 3 ? anti-parallel 
SA2 3 4 ? anti-parallel 
SB1 1 2 ? anti-parallel 
SB1 2 3 ? anti-parallel 
SB1 3 4 ? anti-parallel 
SB1 4 5 ? anti-parallel 
SB1 5 6 ? anti-parallel 
SB2 1 2 ? anti-parallel 
SB2 2 3 ? anti-parallel 
SB2 3 4 ? 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 
SA1 1 TYR A 152 ? VAL A 159 ? TYR A 146 VAL A 153 
SA1 2 ILE A 252 ? ARG A 258 ? ILE A 246 ARG A 252 
SA1 3 VAL A 176 ? SER A 184 ? VAL A 170 SER A 178 
SA1 4 ASP A 200 ? GLU A 215 ? ASP A 194 GLU A 209 
SA1 5 VAL A 218 ? ASN A 225 ? VAL A 212 ASN A 219 
SA1 6 GLY A 235 ? ARG A 241 ? GLY A 229 ARG A 235 
SA2 1 PHE A 11  ? ALA A 13  ? PHE A 5   ALA A 7   
SA2 2 ASP A 200 ? GLU A 215 ? ASP A 194 GLU A 209 
SA2 3 VAL A 218 ? ASN A 225 ? VAL A 212 ASN A 219 
SA2 4 GLY A 235 ? ARG A 241 ? GLY A 229 ARG A 235 
SB1 1 TYR B 152 ? VAL B 159 ? TYR B 146 VAL B 153 
SB1 2 ILE B 252 ? ARG B 258 ? ILE B 246 ARG B 252 
SB1 3 VAL B 176 ? SER B 184 ? VAL B 170 SER B 178 
SB1 4 ASP B 200 ? GLU B 215 ? ASP B 194 GLU B 209 
SB1 5 VAL B 218 ? ASN B 225 ? VAL B 212 ASN B 219 
SB1 6 GLY B 235 ? ARG B 241 ? GLY B 229 ARG B 235 
SB2 1 PHE B 11  ? ALA B 13  ? PHE B 5   ALA B 7   
SB2 2 ASP B 200 ? GLU B 215 ? ASP B 194 GLU B 209 
SB2 3 VAL B 218 ? ASN B 225 ? VAL B 212 ASN B 219 
SB2 4 GLY B 235 ? ARG B 241 ? GLY B 229 ARG B 235 
# 
_struct_site.id                   ACT 
_struct_site.pdbx_evidence_code   Author 
_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    3 
_struct_site.details              'ACTIVE SITE RESIDUES FOR RAT CATHEPSIN B' 
# 
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 ACT 3 CYS A 35  ? CYS A 29  . ? 1_555 ? 
2 ACT 3 HIS A 205 ? HIS A 199 . ? 1_555 ? 
3 ACT 3 ASN A 225 ? ASN A 219 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1CPJ 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1CPJ 
_atom_sites.fract_transf_matrix[1][1]   0.021236 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002717 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011080 
_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]   0.016234 
_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 
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   . LEU A 1 7   ? -4.651  33.418 41.858 1.00 16.22 ? 1   LEU A N   1 
ATOM   2    C CA  . LEU A 1 7   ? -3.696  34.359 41.190 1.00 90.97 ? 1   LEU A CA  1 
ATOM   3    C C   . LEU A 1 7   ? -2.396  33.651 40.821 1.00 43.63 ? 1   LEU A C   1 
ATOM   4    O O   . LEU A 1 7   ? -1.849  32.900 41.623 1.00 16.85 ? 1   LEU A O   1 
ATOM   5    C CB  . LEU A 1 7   ? -3.380  35.531 42.120 1.00 38.58 ? 1   LEU A CB  1 
ATOM   6    C CG  . LEU A 1 7   ? -3.455  36.954 41.567 1.00 45.87 ? 1   LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 7   ? -4.680  37.135 40.675 1.00 11.00 ? 1   LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 7   ? -3.493  37.915 42.738 1.00 12.09 ? 1   LEU A CD2 1 
ATOM   9    N N   . PRO A 1 8   ? -1.896  33.865 39.596 1.00 34.33 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 8   ? -0.765  33.066 39.099 1.00 9.61  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 8   ? 0.536   33.317 39.873 1.00 12.77 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 8   ? 0.660   34.320 40.585 1.00 18.80 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 8   ? -0.671  33.468 37.627 1.00 21.03 ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 8   ? -1.335  34.810 37.556 1.00 17.88 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 8   ? -2.408  34.801 38.579 1.00 39.64 ? 2   PRO A CD  1 
ATOM   16   N N   . GLU A 1 9   ? 1.480   32.385 39.765 1.00 25.84 ? 3   GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? 2.710   32.432 40.568 1.00 2.16  ? 3   GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? 3.687   33.506 40.071 1.00 15.05 ? 3   GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? 4.585   33.931 40.796 1.00 20.24 ? 3   GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? 3.406   31.062 40.576 1.00 36.96 ? 3   GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? 2.548   29.916 41.110 1.00 73.28 ? 3   GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? 1.770   29.176 40.019 1.00 93.19 ? 3   GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? 1.662   29.689 38.882 1.00 55.11 ? 3   GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? 1.256   28.071 40.306 1.00 91.37 ? 3   GLU A OE2 1 
ATOM   25   N N   . SER A 1 10  ? 3.513   33.932 38.824 1.00 10.81 ? 4   SER A N   1 
ATOM   26   C CA  . SER A 1 10  ? 4.125   35.168 38.355 1.00 26.75 ? 4   SER A CA  1 
ATOM   27   C C   . SER A 1 10  ? 3.313   35.772 37.217 1.00 7.93  ? 4   SER A C   1 
ATOM   28   O O   . SER A 1 10  ? 2.381   35.151 36.693 1.00 28.87 ? 4   SER A O   1 
ATOM   29   C CB  . SER A 1 10  ? 5.571   34.936 37.903 1.00 19.73 ? 4   SER A CB  1 
ATOM   30   O OG  . SER A 1 10  ? 5.725   33.653 37.330 1.00 29.78 ? 4   SER A OG  1 
ATOM   31   N N   . PHE A 1 11  ? 3.627   37.019 36.888 1.00 20.52 ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 11  ? 2.814   37.797 35.960 1.00 24.58 ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 11  ? 3.628   38.911 35.316 1.00 44.10 ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 11  ? 4.365   39.623 35.993 1.00 15.79 ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 11  ? 1.636   38.411 36.707 1.00 2.00  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 11  ? 0.735   39.223 35.840 1.00 31.25 ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 11  ? -0.183  38.604 35.017 1.00 19.64 ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 11  ? 0.820   40.612 35.834 1.00 5.39  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 11  ? -1.004  39.349 34.202 1.00 30.92 ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 11  ? -0.001  41.362 35.014 1.00 23.10 ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 11  ? -0.912  40.725 34.201 1.00 4.62  ? 5   PHE A CZ  1 
ATOM   42   N N   . ASP A 1 12  ? 3.410   39.132 34.029 1.00 10.38 ? 6   ASP A N   1 
ATOM   43   C CA  . ASP A 1 12  ? 3.994   40.284 33.357 1.00 5.89  ? 6   ASP A CA  1 
ATOM   44   C C   . ASP A 1 12  ? 2.957   41.033 32.529 1.00 24.48 ? 6   ASP A C   1 
ATOM   45   O O   . ASP A 1 12  ? 2.350   40.464 31.636 1.00 16.22 ? 6   ASP A O   1 
ATOM   46   C CB  . ASP A 1 12  ? 5.136   39.834 32.472 1.00 3.18  ? 6   ASP A CB  1 
ATOM   47   C CG  . ASP A 1 12  ? 6.092   40.967 32.118 1.00 3.19  ? 6   ASP A CG  1 
ATOM   48   O OD1 . ASP A 1 12  ? 5.671   42.144 32.034 1.00 44.81 ? 6   ASP A OD1 1 
ATOM   49   O OD2 . ASP A 1 12  ? 7.302   40.668 32.025 1.00 19.12 ? 6   ASP A OD2 1 
ATOM   50   N N   . ALA A 1 13  ? 2.839   42.338 32.758 1.00 2.00  ? 7   ALA A N   1 
ATOM   51   C CA  . ALA A 1 13  ? 1.845   43.153 32.064 1.00 75.64 ? 7   ALA A CA  1 
ATOM   52   C C   . ALA A 1 13  ? 2.105   43.126 30.557 1.00 27.22 ? 7   ALA A C   1 
ATOM   53   O O   . ALA A 1 13  ? 1.165   43.080 29.749 1.00 7.93  ? 7   ALA A O   1 
ATOM   54   C CB  . ALA A 1 13  ? 1.886   44.596 32.595 1.00 12.83 ? 7   ALA A CB  1 
ATOM   55   N N   . ARG A 1 14  ? 3.375   42.924 30.212 1.00 2.00  ? 8   ARG A N   1 
ATOM   56   C CA  . ARG A 1 14  ? 3.844   43.059 28.832 1.00 34.11 ? 8   ARG A CA  1 
ATOM   57   C C   . ARG A 1 14  ? 3.442   41.842 28.013 1.00 84.03 ? 8   ARG A C   1 
ATOM   58   O O   . ARG A 1 14  ? 2.952   41.970 26.900 1.00 11.02 ? 8   ARG A O   1 
ATOM   59   C CB  . ARG A 1 14  ? 5.366   43.234 28.775 1.00 3.14  ? 8   ARG A CB  1 
ATOM   60   C CG  . ARG A 1 14  ? 5.925   44.330 29.653 1.00 2.00  ? 8   ARG A CG  1 
ATOM   61   C CD  . ARG A 1 14  ? 7.435   44.311 29.633 1.00 20.38 ? 8   ARG A CD  1 
ATOM   62   N NE  . ARG A 1 14  ? 8.029   43.220 30.407 1.00 2.00  ? 8   ARG A NE  1 
ATOM   63   C CZ  . ARG A 1 14  ? 9.336   43.109 30.686 1.00 40.77 ? 8   ARG A CZ  1 
ATOM   64   N NH1 . ARG A 1 14  ? 10.238  43.987 30.232 1.00 6.52  ? 8   ARG A NH1 1 
ATOM   65   N NH2 . ARG A 1 14  ? 9.761   42.100 31.428 1.00 5.94  ? 8   ARG A NH2 1 
ATOM   66   N N   . GLU A 1 15  ? 3.641   40.656 28.575 1.00 2.00  ? 9   GLU A N   1 
ATOM   67   C CA  . GLU A 1 15  ? 3.017   39.453 28.034 1.00 8.94  ? 9   GLU A CA  1 
ATOM   68   C C   . GLU A 1 15  ? 1.487   39.473 28.033 1.00 2.00  ? 9   GLU A C   1 
ATOM   69   O O   . GLU A 1 15  ? 0.863   39.209 27.012 1.00 44.25 ? 9   GLU A O   1 
ATOM   70   C CB  . GLU A 1 15  ? 3.482   38.258 28.816 1.00 11.13 ? 9   GLU A CB  1 
ATOM   71   C CG  . GLU A 1 15  ? 4.937   38.054 28.683 1.00 23.03 ? 9   GLU A CG  1 
ATOM   72   C CD  . GLU A 1 15  ? 5.327   36.710 29.177 1.00 2.00  ? 9   GLU A CD  1 
ATOM   73   O OE1 . GLU A 1 15  ? 4.444   35.814 29.179 1.00 44.76 ? 9   GLU A OE1 1 
ATOM   74   O OE2 . GLU A 1 15  ? 6.529   36.516 29.503 1.00 50.85 ? 9   GLU A OE2 1 
ATOM   75   N N   . GLN A 1 16  ? 0.890   39.750 29.189 1.00 2.00  ? 10  GLN A N   1 
ATOM   76   C CA  . GLN A 1 16  ? -0.568  39.727 29.314 1.00 22.59 ? 10  GLN A CA  1 
ATOM   77   C C   . GLN A 1 16  ? -1.248  40.658 28.303 1.00 2.00  ? 10  GLN A C   1 
ATOM   78   O O   . GLN A 1 16  ? -2.156  40.240 27.579 1.00 53.34 ? 10  GLN A O   1 
ATOM   79   C CB  . GLN A 1 16  ? -0.985  40.107 30.732 1.00 29.13 ? 10  GLN A CB  1 
ATOM   80   C CG  . GLN A 1 16  ? -2.478  39.983 30.974 1.00 2.00  ? 10  GLN A CG  1 
ATOM   81   C CD  . GLN A 1 16  ? -2.971  38.561 30.807 1.00 2.00  ? 10  GLN A CD  1 
ATOM   82   O OE1 . GLN A 1 16  ? -2.222  37.609 31.000 1.00 31.53 ? 10  GLN A OE1 1 
ATOM   83   N NE2 . GLN A 1 16  ? -4.237  38.412 30.490 1.00 24.04 ? 10  GLN A NE2 1 
ATOM   84   N N   . TRP A 1 17  ? -0.633  41.814 28.074 1.00 7.65  ? 11  TRP A N   1 
ATOM   85   C CA  . TRP A 1 17  ? -1.194  42.800 27.154 1.00 6.35  ? 11  TRP A CA  1 
ATOM   86   C C   . TRP A 1 17  ? -0.147  43.253 26.133 1.00 11.86 ? 11  TRP A C   1 
ATOM   87   O O   . TRP A 1 17  ? 0.112   44.461 25.972 1.00 11.08 ? 11  TRP A O   1 
ATOM   88   C CB  . TRP A 1 17  ? -1.747  44.009 27.938 1.00 3.52  ? 11  TRP A CB  1 
ATOM   89   C CG  . TRP A 1 17  ? -2.801  43.667 28.986 1.00 22.45 ? 11  TRP A CG  1 
ATOM   90   C CD1 . TRP A 1 17  ? -4.149  43.560 28.783 1.00 43.14 ? 11  TRP A CD1 1 
ATOM   91   C CD2 . TRP A 1 17  ? -2.607  43.576 30.411 1.00 28.00 ? 11  TRP A CD2 1 
ATOM   92   N NE1 . TRP A 1 17  ? -4.804  43.445 29.986 1.00 2.29  ? 11  TRP A NE1 1 
ATOM   93   C CE2 . TRP A 1 17  ? -3.881  43.447 30.998 1.00 64.80 ? 11  TRP A CE2 1 
ATOM   94   C CE3 . TRP A 1 17  ? -1.485  43.585 31.243 1.00 47.38 ? 11  TRP A CE3 1 
ATOM   95   C CZ2 . TRP A 1 17  ? -4.062  43.339 32.375 1.00 8.17  ? 11  TRP A CZ2 1 
ATOM   96   C CZ3 . TRP A 1 17  ? -1.673  43.461 32.621 1.00 2.28  ? 11  TRP A CZ3 1 
ATOM   97   C CH2 . TRP A 1 17  ? -2.948  43.345 33.165 1.00 24.44 ? 11  TRP A CH2 1 
ATOM   98   N N   . SER A 1 18  ? 0.327   42.289 25.340 1.00 13.61 ? 12  SER A N   1 
ATOM   99   C CA  . SER A 1 18  ? 1.445   42.495 24.409 1.00 38.17 ? 12  SER A CA  1 
ATOM   100  C C   . SER A 1 18  ? 1.186   43.502 23.285 1.00 32.01 ? 12  SER A C   1 
ATOM   101  O O   . SER A 1 18  ? 2.125   44.061 22.702 1.00 31.59 ? 12  SER A O   1 
ATOM   102  C CB  . SER A 1 18  ? 1.841   41.167 23.786 1.00 34.01 ? 12  SER A CB  1 
ATOM   103  O OG  . SER A 1 18  ? 1.117   40.960 22.586 1.00 41.02 ? 12  SER A OG  1 
ATOM   104  N N   . ASN A 1 19  ? -0.083  43.645 22.917 1.00 13.63 ? 13  ASN A N   1 
ATOM   105  C CA  . ASN A 1 19  ? -0.497  44.627 21.915 1.00 7.65  ? 13  ASN A CA  1 
ATOM   106  C C   . ASN A 1 19  ? -0.305  46.093 22.344 1.00 35.86 ? 13  ASN A C   1 
ATOM   107  O O   . ASN A 1 19  ? -0.407  47.009 21.529 1.00 56.87 ? 13  ASN A O   1 
ATOM   108  C CB  . ASN A 1 19  ? -1.957  44.400 21.546 1.00 39.45 ? 13  ASN A CB  1 
ATOM   109  C CG  . ASN A 1 19  ? -2.882  44.725 22.680 1.00 16.17 ? 13  ASN A CG  1 
ATOM   110  O OD1 . ASN A 1 19  ? -3.729  45.602 22.563 1.00 39.99 ? 13  ASN A OD1 1 
ATOM   111  N ND2 . ASN A 1 19  ? -2.674  44.080 23.816 1.00 44.51 ? 13  ASN A ND2 1 
ATOM   112  N N   . CYS A 1 20  ? -0.162  46.303 23.647 1.00 35.20 ? 14  CYS A N   1 
ATOM   113  C CA  . CYS A 1 20  ? 0.072   47.625 24.217 1.00 6.95  ? 14  CYS A CA  1 
ATOM   114  C C   . CYS A 1 20  ? 1.571   47.893 24.377 1.00 67.72 ? 14  CYS A C   1 
ATOM   115  O O   . CYS A 1 20  ? 2.247   47.207 25.129 1.00 2.87  ? 14  CYS A O   1 
ATOM   116  C CB  . CYS A 1 20  ? -0.622  47.713 25.580 1.00 47.50 ? 14  CYS A CB  1 
ATOM   117  S SG  . CYS A 1 20  ? -2.436  47.837 25.452 1.00 2.01  ? 14  CYS A SG  1 
ATOM   118  N N   . PRO A 1 21  ? 2.125   48.818 23.582 1.00 18.97 ? 15  PRO A N   1 
ATOM   119  C CA  . PRO A 1 21  ? 3.588   48.947 23.551 1.00 7.02  ? 15  PRO A CA  1 
ATOM   120  C C   . PRO A 1 21  ? 4.180   49.700 24.724 1.00 28.56 ? 15  PRO A C   1 
ATOM   121  O O   . PRO A 1 21  ? 5.232   49.320 25.227 1.00 3.29  ? 15  PRO A O   1 
ATOM   122  C CB  . PRO A 1 21  ? 3.870   49.678 22.232 1.00 2.00  ? 15  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 21  ? 2.554   50.258 21.811 1.00 16.30 ? 15  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 21  ? 1.534   49.269 22.311 1.00 8.84  ? 15  PRO A CD  1 
ATOM   125  N N   . THR A 1 22  ? 3.504   50.770 25.146 1.00 21.22 ? 16  THR A N   1 
ATOM   126  C CA  . THR A 1 22  ? 3.965   51.611 26.255 1.00 9.19  ? 16  THR A CA  1 
ATOM   127  C C   . THR A 1 22  ? 4.362   50.798 27.501 1.00 4.78  ? 16  THR A C   1 
ATOM   128  O O   . THR A 1 22  ? 5.264   51.212 28.257 1.00 6.32  ? 16  THR A O   1 
ATOM   129  C CB  . THR A 1 22  ? 2.891   52.721 26.674 1.00 15.00 ? 16  THR A CB  1 
ATOM   130  O OG1 . THR A 1 22  ? 1.705   52.115 27.230 1.00 14.78 ? 16  THR A OG1 1 
ATOM   131  C CG2 . THR A 1 22  ? 2.490   53.553 25.470 1.00 2.00  ? 16  THR A CG2 1 
ATOM   132  N N   . ILE A 1 23  ? 3.786   49.600 27.653 1.00 8.47  ? 17  ILE A N   1 
ATOM   133  C CA  . ILE A 1 23  ? 4.009   48.770 28.854 1.00 10.58 ? 17  ILE A CA  1 
ATOM   134  C C   . ILE A 1 23  ? 5.440   48.265 28.951 1.00 28.82 ? 17  ILE A C   1 
ATOM   135  O O   . ILE A 1 23  ? 5.962   48.135 30.050 1.00 7.19  ? 17  ILE A O   1 
ATOM   136  C CB  . ILE A 1 23  ? 3.057   47.520 28.931 1.00 2.00  ? 17  ILE A CB  1 
ATOM   137  C CG1 . ILE A 1 23  ? 1.593   47.939 28.837 1.00 4.73  ? 17  ILE A CG1 1 
ATOM   138  C CG2 . ILE A 1 23  ? 3.308   46.779 30.204 1.00 2.00  ? 17  ILE A CG2 1 
ATOM   139  C CD1 . ILE A 1 23  ? 0.620   46.795 28.952 1.00 6.80  ? 17  ILE A CD1 1 
ATOM   140  N N   . ALA A 1 24  ? 6.037   47.917 27.811 1.00 6.82  ? 18  ALA A N   1 
ATOM   141  C CA  . ALA A 1 24  ? 7.457   47.549 27.759 1.00 17.79 ? 18  ALA A CA  1 
ATOM   142  C C   . ALA A 1 24  ? 8.406   48.747 27.708 1.00 23.13 ? 18  ALA A C   1 
ATOM   143  O O   . ALA A 1 24  ? 9.617   48.572 27.748 1.00 13.54 ? 18  ALA A O   1 
ATOM   144  C CB  . ALA A 1 24  ? 7.717   46.653 26.565 1.00 25.32 ? 18  ALA A CB  1 
ATOM   145  N N   . GLN A 1 25  ? 7.866   49.950 27.518 1.00 2.00  ? 19  GLN A N   1 
ATOM   146  C CA  . GLN A 1 25  ? 8.707   51.130 27.333 1.00 13.91 ? 19  GLN A CA  1 
ATOM   147  C C   . GLN A 1 25  ? 9.386   51.546 28.631 1.00 34.35 ? 19  GLN A C   1 
ATOM   148  O O   . GLN A 1 25  ? 8.852   51.308 29.710 1.00 16.51 ? 19  GLN A O   1 
ATOM   149  C CB  . GLN A 1 25  ? 7.885   52.317 26.798 1.00 6.46  ? 19  GLN A CB  1 
ATOM   150  C CG  . GLN A 1 25  ? 8.723   53.558 26.498 1.00 2.00  ? 19  GLN A CG  1 
ATOM   151  C CD  . GLN A 1 25  ? 7.907   54.817 26.251 1.00 5.72  ? 19  GLN A CD  1 
ATOM   152  O OE1 . GLN A 1 25  ? 6.658   54.771 26.252 1.00 4.92  ? 19  GLN A OE1 1 
ATOM   153  N NE2 . GLN A 1 25  ? 8.533   55.888 26.086 1.00 35.63 ? 19  GLN A NE2 1 
ATOM   154  N N   . ILE A 1 26  ? 10.588  52.106 28.503 1.00 28.82 ? 20  ILE A N   1 
ATOM   155  C CA  . ILE A 1 26  ? 11.350  52.737 29.593 1.00 2.00  ? 20  ILE A CA  1 
ATOM   156  C C   . ILE A 1 26  ? 11.700  54.141 29.115 1.00 16.51 ? 20  ILE A C   1 
ATOM   157  O O   . ILE A 1 26  ? 11.910  54.345 27.914 1.00 13.52 ? 20  ILE A O   1 
ATOM   158  C CB  . ILE A 1 26  ? 12.664  51.950 29.883 1.00 24.55 ? 20  ILE A CB  1 
ATOM   159  C CG1 . ILE A 1 26  ? 12.332  50.662 30.645 1.00 2.00  ? 20  ILE A CG1 1 
ATOM   160  C CG2 . ILE A 1 26  ? 13.712  52.829 30.646 1.00 8.07  ? 20  ILE A CG2 1 
ATOM   161  C CD1 . ILE A 1 26  ? 11.838  50.908 32.065 1.00 2.00  ? 20  ILE A CD1 1 
ATOM   162  N N   . ARG A 1 27  ? 11.528  55.114 30.004 1.00 2.00  ? 21  ARG A N   1 
ATOM   163  C CA  . ARG A 1 27  ? 11.755  56.541 29.708 1.00 2.00  ? 21  ARG A CA  1 
ATOM   164  C C   . ARG A 1 27  ? 12.867  57.121 30.588 1.00 2.00  ? 21  ARG A C   1 
ATOM   165  O O   . ARG A 1 27  ? 13.450  56.415 31.413 1.00 6.04  ? 21  ARG A O   1 
ATOM   166  C CB  . ARG A 1 27  ? 10.460  57.360 29.895 1.00 3.14  ? 21  ARG A CB  1 
ATOM   167  C CG  . ARG A 1 27  ? 9.180   56.541 30.058 1.00 3.78  ? 21  ARG A CG  1 
ATOM   168  C CD  . ARG A 1 27  ? 8.033   56.836 29.045 1.00 17.19 ? 21  ARG A CD  1 
ATOM   169  N NE  . ARG A 1 27  ? 7.368   58.128 29.222 1.00 2.92  ? 21  ARG A NE  1 
ATOM   170  C CZ  . ARG A 1 27  ? 6.053   58.359 29.093 1.00 19.25 ? 21  ARG A CZ  1 
ATOM   171  N NH1 . ARG A 1 27  ? 5.204   57.369 28.871 1.00 2.00  ? 21  ARG A NH1 1 
ATOM   172  N NH2 . ARG A 1 27  ? 5.573   59.605 29.199 1.00 3.37  ? 21  ARG A NH2 1 
ATOM   173  N N   . ASP A 1 28  ? 13.168  58.401 30.408 1.00 22.47 ? 22  ASP A N   1 
ATOM   174  C CA  . ASP A 1 28  ? 14.187  59.070 31.214 1.00 6.87  ? 22  ASP A CA  1 
ATOM   175  C C   . ASP A 1 28  ? 13.729  60.437 31.741 1.00 24.56 ? 22  ASP A C   1 
ATOM   176  O O   . ASP A 1 28  ? 13.581  61.386 30.970 1.00 16.80 ? 22  ASP A O   1 
ATOM   177  C CB  . ASP A 1 28  ? 15.472  59.235 30.392 1.00 38.52 ? 22  ASP A CB  1 
ATOM   178  C CG  . ASP A 1 28  ? 16.686  59.573 31.250 1.00 8.83  ? 22  ASP A CG  1 
ATOM   179  O OD1 . ASP A 1 28  ? 16.505  60.134 32.356 1.00 21.77 ? 22  ASP A OD1 1 
ATOM   180  O OD2 . ASP A 1 28  ? 17.825  59.256 30.820 1.00 14.83 ? 22  ASP A OD2 1 
ATOM   181  N N   . GLN A 1 29  ? 13.641  60.570 33.067 1.00 7.22  ? 23  GLN A N   1 
ATOM   182  C CA  . GLN A 1 29  ? 13.180  61.818 33.711 1.00 12.18 ? 23  GLN A CA  1 
ATOM   183  C C   . GLN A 1 29  ? 14.265  62.900 33.644 1.00 19.52 ? 23  GLN A C   1 
ATOM   184  O O   . GLN A 1 29  ? 14.013  64.099 33.849 1.00 9.57  ? 23  GLN A O   1 
ATOM   185  C CB  . GLN A 1 29  ? 12.843  61.556 35.170 1.00 18.57 ? 23  GLN A CB  1 
ATOM   186  C CG  . GLN A 1 29  ? 14.004  60.993 35.933 1.00 2.00  ? 23  GLN A CG  1 
ATOM   187  C CD  . GLN A 1 29  ? 13.706  60.771 37.403 1.00 31.27 ? 23  GLN A CD  1 
ATOM   188  O OE1 . GLN A 1 29  ? 14.181  61.498 38.268 1.00 8.25  ? 23  GLN A OE1 1 
ATOM   189  N NE2 . GLN A 1 29  ? 12.993  59.714 37.694 1.00 2.00  ? 23  GLN A NE2 1 
ATOM   190  N N   . GLY A 1 30  ? 15.464  62.449 33.299 1.00 19.34 ? 24  GLY A N   1 
ATOM   191  C CA  . GLY A 1 30  ? 16.583  63.338 33.115 1.00 3.25  ? 24  GLY A CA  1 
ATOM   192  C C   . GLY A 1 30  ? 17.039  63.875 34.453 1.00 19.32 ? 24  GLY A C   1 
ATOM   193  O O   . GLY A 1 30  ? 17.051  63.154 35.444 1.00 29.96 ? 24  GLY A O   1 
ATOM   194  N N   . SER A 1 31  ? 17.565  65.090 34.440 1.00 14.13 ? 25  SER A N   1 
ATOM   195  C CA  . SER A 1 31  ? 18.057  65.729 35.650 1.00 48.77 ? 25  SER A CA  1 
ATOM   196  C C   . SER A 1 31  ? 16.893  66.573 36.140 1.00 56.81 ? 25  SER A C   1 
ATOM   197  O O   . SER A 1 31  ? 16.734  67.729 35.750 1.00 33.49 ? 25  SER A O   1 
ATOM   198  C CB  . SER A 1 31  ? 19.299  66.585 35.341 1.00 2.00  ? 25  SER A CB  1 
ATOM   199  O OG  . SER A 1 31  ? 20.196  66.619 36.444 1.00 76.59 ? 25  SER A OG  1 
ATOM   200  N N   . CYS A 1 32  ? 15.914  65.857 36.672 1.00 34.68 ? 26  CYS A N   1 
ATOM   201  C CA  . CYS A 1 32  ? 14.695  66.440 37.209 1.00 15.16 ? 26  CYS A CA  1 
ATOM   202  C C   . CYS A 1 32  ? 14.025  65.365 38.026 1.00 61.99 ? 26  CYS A C   1 
ATOM   203  O O   . CYS A 1 32  ? 13.860  64.253 37.543 1.00 17.36 ? 26  CYS A O   1 
ATOM   204  C CB  . CYS A 1 32  ? 13.746  66.846 36.095 1.00 4.94  ? 26  CYS A CB  1 
ATOM   205  S SG  . CYS A 1 32  ? 12.062  67.255 36.670 1.00 16.73 ? 26  CYS A SG  1 
ATOM   206  N N   . GLY A 1 33  ? 13.688  65.683 39.270 1.00 12.70 ? 27  GLY A N   1 
ATOM   207  C CA  . GLY A 1 33  ? 12.973  64.743 40.115 1.00 25.60 ? 27  GLY A CA  1 
ATOM   208  C C   . GLY A 1 33  ? 11.497  64.576 39.775 1.00 18.83 ? 27  GLY A C   1 
ATOM   209  O O   . GLY A 1 33  ? 10.616  64.911 40.574 1.00 26.78 ? 27  GLY A O   1 
ATOM   210  N N   . SER A 1 34  ? 11.227  64.000 38.611 1.00 8.25  ? 28  SER A N   1 
ATOM   211  C CA  . SER A 1 34  ? 9.857   63.855 38.133 1.00 2.00  ? 28  SER A CA  1 
ATOM   212  C C   . SER A 1 34  ? 9.412   62.396 38.192 1.00 10.71 ? 28  SER A C   1 
ATOM   213  O O   . SER A 1 34  ? 8.365   62.049 37.640 1.00 22.34 ? 28  SER A O   1 
ATOM   214  C CB  . SER A 1 34  ? 9.749   64.392 36.704 1.00 27.32 ? 28  SER A CB  1 
ATOM   215  O OG  . SER A 1 34  ? 10.956  64.137 36.002 1.00 2.00  ? 28  SER A OG  1 
ATOM   216  N N   . CYS A 1 35  ? 10.139  61.573 38.961 1.00 2.00  ? 29  CYS A N   1 
ATOM   217  C CA  . CYS A 1 35  ? 9.769   60.178 39.155 1.00 12.98 ? 29  CYS A CA  1 
ATOM   218  C C   . CYS A 1 35  ? 8.351   60.016 39.664 1.00 15.32 ? 29  CYS A C   1 
ATOM   219  O O   . CYS A 1 35  ? 7.668   59.062 39.303 1.00 15.57 ? 29  CYS A O   1 
ATOM   220  C CB  . CYS A 1 35  ? 10.741  59.444 40.094 1.00 2.00  ? 29  CYS A CB  1 
ATOM   221  S SG  . CYS A 1 35  ? 11.394  60.386 41.415 1.00 20.22 ? 29  CYS A SG  1 
ATOM   222  N N   . TRP A 1 36  ? 7.862   61.010 40.389 1.00 2.00  ? 30  TRP A N   1 
ATOM   223  C CA  . TRP A 1 36  ? 6.452   61.015 40.750 1.00 44.54 ? 30  TRP A CA  1 
ATOM   224  C C   . TRP A 1 36  ? 5.577   61.092 39.500 1.00 2.37  ? 30  TRP A C   1 
ATOM   225  O O   . TRP A 1 36  ? 4.649   60.306 39.349 1.00 7.42  ? 30  TRP A O   1 
ATOM   226  C CB  . TRP A 1 36  ? 6.128   62.170 41.712 1.00 15.24 ? 30  TRP A CB  1 
ATOM   227  C CG  . TRP A 1 36  ? 6.317   63.533 41.171 1.00 13.98 ? 30  TRP A CG  1 
ATOM   228  C CD1 . TRP A 1 36  ? 7.437   64.308 41.274 1.00 2.00  ? 30  TRP A CD1 1 
ATOM   229  C CD2 . TRP A 1 36  ? 5.336   64.335 40.508 1.00 10.58 ? 30  TRP A CD2 1 
ATOM   230  N NE1 . TRP A 1 36  ? 7.207   65.539 40.731 1.00 2.00  ? 30  TRP A NE1 1 
ATOM   231  C CE2 . TRP A 1 36  ? 5.929   65.577 40.237 1.00 6.06  ? 30  TRP A CE2 1 
ATOM   232  C CE3 . TRP A 1 36  ? 4.020   64.114 40.100 1.00 12.15 ? 30  TRP A CE3 1 
ATOM   233  C CZ2 . TRP A 1 36  ? 5.257   66.591 39.576 1.00 18.16 ? 30  TRP A CZ2 1 
ATOM   234  C CZ3 . TRP A 1 36  ? 3.354   65.114 39.442 1.00 6.41  ? 30  TRP A CZ3 1 
ATOM   235  C CH2 . TRP A 1 36  ? 3.970   66.340 39.188 1.00 2.82  ? 30  TRP A CH2 1 
ATOM   236  N N   . ALA A 1 37  ? 5.971   61.959 38.563 1.00 58.58 ? 31  ALA A N   1 
ATOM   237  C CA  . ALA A 1 37  ? 5.251   62.187 37.303 1.00 2.50  ? 31  ALA A CA  1 
ATOM   238  C C   . ALA A 1 37  ? 5.370   61.023 36.351 1.00 2.00  ? 31  ALA A C   1 
ATOM   239  O O   . ALA A 1 37  ? 4.389   60.622 35.728 1.00 9.66  ? 31  ALA A O   1 
ATOM   240  C CB  . ALA A 1 37  ? 5.763   63.445 36.625 1.00 2.00  ? 31  ALA A CB  1 
ATOM   241  N N   . PHE A 1 38  ? 6.553   60.420 36.292 1.00 5.47  ? 32  PHE A N   1 
ATOM   242  C CA  . PHE A 1 38  ? 6.798   59.329 35.343 1.00 2.54  ? 32  PHE A CA  1 
ATOM   243  C C   . PHE A 1 38  ? 6.065   58.067 35.704 1.00 8.07  ? 32  PHE A C   1 
ATOM   244  O O   . PHE A 1 38  ? 5.320   57.521 34.880 1.00 2.63  ? 32  PHE A O   1 
ATOM   245  C CB  . PHE A 1 38  ? 8.296   59.044 35.197 1.00 2.05  ? 32  PHE A CB  1 
ATOM   246  C CG  . PHE A 1 38  ? 8.972   59.952 34.223 1.00 26.93 ? 32  PHE A CG  1 
ATOM   247  C CD1 . PHE A 1 38  ? 9.315   61.254 34.584 1.00 3.88  ? 32  PHE A CD1 1 
ATOM   248  C CD2 . PHE A 1 38  ? 9.010   59.606 32.895 1.00 2.00  ? 32  PHE A CD2 1 
ATOM   249  C CE1 . PHE A 1 38  ? 9.655   62.173 33.637 1.00 50.57 ? 32  PHE A CE1 1 
ATOM   250  C CE2 . PHE A 1 38  ? 9.344   60.538 31.945 1.00 19.51 ? 32  PHE A CE2 1 
ATOM   251  C CZ  . PHE A 1 38  ? 9.660   61.815 32.313 1.00 12.89 ? 32  PHE A CZ  1 
ATOM   252  N N   . GLY A 1 39  ? 6.247   57.627 36.949 1.00 12.27 ? 33  GLY A N   1 
ATOM   253  C CA  . GLY A 1 39  ? 5.539   56.455 37.434 1.00 2.00  ? 33  GLY A CA  1 
ATOM   254  C C   . GLY A 1 39  ? 4.071   56.548 37.093 1.00 2.00  ? 33  GLY A C   1 
ATOM   255  O O   . GLY A 1 39  ? 3.470   55.555 36.635 1.00 4.29  ? 33  GLY A O   1 
ATOM   256  N N   . ALA A 1 40  ? 3.500   57.744 37.220 1.00 2.00  ? 34  ALA A N   1 
ATOM   257  C CA  . ALA A 1 40  ? 2.062   57.933 36.926 1.00 3.76  ? 34  ALA A CA  1 
ATOM   258  C C   . ALA A 1 40  ? 1.731   57.832 35.429 1.00 2.00  ? 34  ALA A C   1 
ATOM   259  O O   . ALA A 1 40  ? 0.960   56.976 35.018 1.00 2.11  ? 34  ALA A O   1 
ATOM   260  C CB  . ALA A 1 40  ? 1.587   59.269 37.472 1.00 2.00  ? 34  ALA A CB  1 
ATOM   261  N N   . VAL A 1 41  ? 2.307   58.728 34.637 1.00 5.44  ? 35  VAL A N   1 
ATOM   262  C CA  . VAL A 1 41  ? 2.037   58.799 33.203 1.00 10.54 ? 35  VAL A CA  1 
ATOM   263  C C   . VAL A 1 41  ? 2.347   57.517 32.397 1.00 2.00  ? 35  VAL A C   1 
ATOM   264  O O   . VAL A 1 41  ? 1.500   57.056 31.653 1.00 21.11 ? 35  VAL A O   1 
ATOM   265  C CB  . VAL A 1 41  ? 2.770   59.994 32.575 1.00 2.00  ? 35  VAL A CB  1 
ATOM   266  C CG1 . VAL A 1 41  ? 2.411   61.265 33.307 1.00 2.00  ? 35  VAL A CG1 1 
ATOM   267  C CG2 . VAL A 1 41  ? 4.290   59.774 32.597 1.00 13.44 ? 35  VAL A CG2 1 
ATOM   268  N N   . GLU A 1 42  ? 3.405   56.809 32.774 1.00 2.00  ? 36  GLU A N   1 
ATOM   269  C CA  . GLU A 1 42  ? 3.630   55.430 32.341 1.00 7.16  ? 36  GLU A CA  1 
ATOM   270  C C   . GLU A 1 42  ? 2.461   54.468 32.561 1.00 2.00  ? 36  GLU A C   1 
ATOM   271  O O   . GLU A 1 42  ? 1.919   53.934 31.601 1.00 2.00  ? 36  GLU A O   1 
ATOM   272  C CB  . GLU A 1 42  ? 4.880   54.868 33.011 1.00 2.00  ? 36  GLU A CB  1 
ATOM   273  C CG  . GLU A 1 42  ? 6.140   55.489 32.491 1.00 10.52 ? 36  GLU A CG  1 
ATOM   274  C CD  . GLU A 1 42  ? 7.273   55.381 33.482 1.00 7.70  ? 36  GLU A CD  1 
ATOM   275  O OE1 . GLU A 1 42  ? 7.166   54.556 34.394 1.00 14.22 ? 36  GLU A OE1 1 
ATOM   276  O OE2 . GLU A 1 42  ? 8.302   56.078 33.316 1.00 2.00  ? 36  GLU A OE2 1 
ATOM   277  N N   . ALA A 1 43  ? 1.989   54.333 33.801 1.00 34.39 ? 37  ALA A N   1 
ATOM   278  C CA  . ALA A 1 43  ? 0.895   53.395 34.097 1.00 2.00  ? 37  ALA A CA  1 
ATOM   279  C C   . ALA A 1 43  ? -0.456  53.837 33.525 1.00 14.36 ? 37  ALA A C   1 
ATOM   280  O O   . ALA A 1 43  ? -1.224  52.992 33.031 1.00 2.00  ? 37  ALA A O   1 
ATOM   281  C CB  . ALA A 1 43  ? 0.772   53.171 35.590 1.00 2.93  ? 37  ALA A CB  1 
ATOM   282  N N   . MET A 1 44  ? -0.732  55.147 33.529 1.00 2.00  ? 38  MET A N   1 
ATOM   283  C CA  . MET A 1 44  ? -1.877  55.665 32.762 1.00 9.93  ? 38  MET A CA  1 
ATOM   284  C C   . MET A 1 44  ? -1.862  55.248 31.284 1.00 26.53 ? 38  MET A C   1 
ATOM   285  O O   . MET A 1 44  ? -2.841  54.675 30.786 1.00 14.35 ? 38  MET A O   1 
ATOM   286  C CB  . MET A 1 44  ? -1.945  57.175 32.843 1.00 2.00  ? 38  MET A CB  1 
ATOM   287  C CG  . MET A 1 44  ? -2.371  57.662 34.199 1.00 32.19 ? 38  MET A CG  1 
ATOM   288  S SD  . MET A 1 44  ? -1.843  59.346 34.448 1.00 2.00  ? 38  MET A SD  1 
ATOM   289  C CE  . MET A 1 44  ? -1.722  59.455 36.240 1.00 10.88 ? 38  MET A CE  1 
ATOM   290  N N   . SER A 1 45  ? -0.719  55.434 30.623 1.00 2.00  ? 39  SER A N   1 
ATOM   291  C CA  . SER A 1 45  ? -0.556  55.001 29.244 1.00 2.00  ? 39  SER A CA  1 
ATOM   292  C C   . SER A 1 45  ? -0.909  53.525 29.125 1.00 2.00  ? 39  SER A C   1 
ATOM   293  O O   . SER A 1 45  ? -1.798  53.163 28.350 1.00 18.71 ? 39  SER A O   1 
ATOM   294  C CB  . SER A 1 45  ? 0.894   55.243 28.748 1.00 2.33  ? 39  SER A CB  1 
ATOM   295  O OG  . SER A 1 45  ? 1.348   56.590 28.953 1.00 2.00  ? 39  SER A OG  1 
ATOM   296  N N   . ASP A 1 46  ? -0.297  52.691 29.967 1.00 3.56  ? 40  ASP A N   1 
ATOM   297  C CA  . ASP A 1 46  ? -0.592  51.254 29.981 1.00 2.00  ? 40  ASP A CA  1 
ATOM   298  C C   . ASP A 1 46  ? -2.079  50.984 30.109 1.00 2.62  ? 40  ASP A C   1 
ATOM   299  O O   . ASP A 1 46  ? -2.631  50.238 29.317 1.00 5.41  ? 40  ASP A O   1 
ATOM   300  C CB  . ASP A 1 46  ? 0.130   50.553 31.127 1.00 2.00  ? 40  ASP A CB  1 
ATOM   301  C CG  . ASP A 1 46  ? 1.624   50.748 31.077 1.00 59.04 ? 40  ASP A CG  1 
ATOM   302  O OD1 . ASP A 1 46  ? 2.142   51.150 30.027 1.00 2.55  ? 40  ASP A OD1 1 
ATOM   303  O OD2 . ASP A 1 46  ? 2.297   50.452 32.072 1.00 3.83  ? 40  ASP A OD2 1 
ATOM   304  N N   . ARG A 1 47  ? -2.746  51.759 30.960 1.00 48.02 ? 41  ARG A N   1 
ATOM   305  C CA  . ARG A 1 47  ? -4.138  51.497 31.323 1.00 2.26  ? 41  ARG A CA  1 
ATOM   306  C C   . ARG A 1 47  ? -5.175  51.996 30.335 1.00 15.29 ? 41  ARG A C   1 
ATOM   307  O O   . ARG A 1 47  ? -6.195  51.331 30.140 1.00 10.11 ? 41  ARG A O   1 
ATOM   308  C CB  . ARG A 1 47  ? -4.434  52.055 32.715 1.00 14.16 ? 41  ARG A CB  1 
ATOM   309  C CG  . ARG A 1 47  ? -3.801  51.244 33.839 1.00 20.02 ? 41  ARG A CG  1 
ATOM   310  C CD  . ARG A 1 47  ? -3.900  51.957 35.191 1.00 43.83 ? 41  ARG A CD  1 
ATOM   311  N NE  . ARG A 1 47  ? -3.528  51.074 36.295 1.00 10.72 ? 41  ARG A NE  1 
ATOM   312  C CZ  . ARG A 1 47  ? -4.395  50.393 37.041 1.00 2.00  ? 41  ARG A CZ  1 
ATOM   313  N NH1 . ARG A 1 47  ? -5.682  50.674 36.984 1.00 2.00  ? 41  ARG A NH1 1 
ATOM   314  N NH2 . ARG A 1 47  ? -3.969  49.468 37.890 1.00 2.59  ? 41  ARG A NH2 1 
ATOM   315  N N   . ILE A 1 48  ? -4.971  53.201 29.796 1.00 2.00  ? 42  ILE A N   1 
ATOM   316  C CA  . ILE A 1 48  ? -5.736  53.714 28.649 1.00 4.07  ? 42  ILE A CA  1 
ATOM   317  C C   . ILE A 1 48  ? -5.775  52.695 27.528 1.00 2.00  ? 42  ILE A C   1 
ATOM   318  O O   . ILE A 1 48  ? -6.849  52.267 27.098 1.00 31.40 ? 42  ILE A O   1 
ATOM   319  C CB  . ILE A 1 48  ? -5.120  54.973 28.028 1.00 2.00  ? 42  ILE A CB  1 
ATOM   320  C CG1 . ILE A 1 48  ? -5.055  56.119 29.036 1.00 4.95  ? 42  ILE A CG1 1 
ATOM   321  C CG2 . ILE A 1 48  ? -5.949  55.381 26.806 1.00 11.67 ? 42  ILE A CG2 1 
ATOM   322  C CD1 . ILE A 1 48  ? -4.408  57.394 28.497 1.00 15.29 ? 42  ILE A CD1 1 
ATOM   323  N N   . CYS A 1 49  ? -4.596  52.211 27.167 1.00 5.17  ? 43  CYS A N   1 
ATOM   324  C CA  . CYS A 1 49  ? -4.449  51.116 26.211 1.00 2.62  ? 43  CYS A CA  1 
ATOM   325  C C   . CYS A 1 49  ? -5.163  49.841 26.645 1.00 6.98  ? 43  CYS A C   1 
ATOM   326  O O   . CYS A 1 49  ? -5.986  49.292 25.883 1.00 35.19 ? 43  CYS A O   1 
ATOM   327  C CB  . CYS A 1 49  ? -2.971  50.811 25.983 1.00 10.35 ? 43  CYS A CB  1 
ATOM   328  S SG  . CYS A 1 49  ? -2.651  49.675 24.609 1.00 17.37 ? 43  CYS A SG  1 
ATOM   329  N N   . ILE A 1 50  ? -4.912  49.396 27.878 1.00 49.12 ? 44  ILE A N   1 
ATOM   330  C CA  . ILE A 1 50  ? -5.536  48.168 28.388 1.00 2.00  ? 44  ILE A CA  1 
ATOM   331  C C   . ILE A 1 50  ? -7.078  48.269 28.399 1.00 19.65 ? 44  ILE A C   1 
ATOM   332  O O   . ILE A 1 50  ? -7.792  47.276 28.139 1.00 12.78 ? 44  ILE A O   1 
ATOM   333  C CB  . ILE A 1 50  ? -5.031  47.801 29.830 1.00 14.94 ? 44  ILE A CB  1 
ATOM   334  C CG1 . ILE A 1 50  ? -3.567  47.349 29.789 1.00 51.85 ? 44  ILE A CG1 1 
ATOM   335  C CG2 . ILE A 1 50  ? -5.852  46.635 30.434 1.00 4.96  ? 44  ILE A CG2 1 
ATOM   336  C CD1 . ILE A 1 50  ? -2.961  47.141 31.170 1.00 2.00  ? 44  ILE A CD1 1 
ATOM   337  N N   . HIS A 1 51  ? -7.565  49.461 28.759 1.00 39.18 ? 45  HIS A N   1 
ATOM   338  C CA  . HIS A 1 51  ? -8.984  49.742 28.961 1.00 12.23 ? 45  HIS A CA  1 
ATOM   339  C C   . HIS A 1 51  ? -9.744  49.693 27.648 1.00 92.73 ? 45  HIS A C   1 
ATOM   340  O O   . HIS A 1 51  ? -10.986 49.696 27.640 1.00 6.35  ? 45  HIS A O   1 
ATOM   341  C CB  . HIS A 1 51  ? -9.158  51.145 29.580 1.00 30.99 ? 45  HIS A CB  1 
ATOM   342  C CG  . HIS A 1 51  ? -10.533 51.404 30.129 1.00 43.98 ? 45  HIS A CG  1 
ATOM   343  N ND1 . HIS A 1 51  ? -11.045 50.701 31.201 1.00 97.78 ? 45  HIS A ND1 1 
ATOM   344  C CD2 . HIS A 1 51  ? -11.521 52.234 29.716 1.00 24.49 ? 45  HIS A CD2 1 
ATOM   345  C CE1 . HIS A 1 51  ? -12.296 51.079 31.412 1.00 92.27 ? 45  HIS A CE1 1 
ATOM   346  N NE2 . HIS A 1 51  ? -12.606 52.006 30.523 1.00 24.58 ? 45  HIS A NE2 1 
ATOM   347  N N   . THR A 1 52  ? -8.990  49.760 26.553 1.00 41.26 ? 46  THR A N   1 
ATOM   348  C CA  . THR A 1 52  ? -9.557  49.955 25.214 1.00 6.82  ? 46  THR A CA  1 
ATOM   349  C C   . THR A 1 52  ? -9.219  48.851 24.241 1.00 5.40  ? 46  THR A C   1 
ATOM   350  O O   . THR A 1 52  ? -9.231  49.068 23.047 1.00 35.35 ? 46  THR A O   1 
ATOM   351  C CB  . THR A 1 52  ? -9.093  51.311 24.606 1.00 17.55 ? 46  THR A CB  1 
ATOM   352  O OG1 . THR A 1 52  ? -7.659  51.380 24.558 1.00 21.09 ? 46  THR A OG1 1 
ATOM   353  C CG2 . THR A 1 52  ? -9.590  52.428 25.440 1.00 2.00  ? 46  THR A CG2 1 
ATOM   354  N N   . ASN A 1 53  ? -8.772  47.712 24.755 1.00 51.77 ? 47  ASN A N   1 
ATOM   355  C CA  . ASN A 1 53  ? -8.347  46.584 23.906 1.00 38.21 ? 47  ASN A CA  1 
ATOM   356  C C   . ASN A 1 53  ? -7.349  46.960 22.785 1.00 18.84 ? 47  ASN A C   1 
ATOM   357  O O   . ASN A 1 53  ? -7.211  46.240 21.794 1.00 66.46 ? 47  ASN A O   1 
ATOM   358  C CB  . ASN A 1 53  ? -9.566  45.853 23.311 1.00 44.97 ? 47  ASN A CB  1 
ATOM   359  C CG  . ASN A 1 53  ? -10.439 45.217 24.375 1.00 51.80 ? 47  ASN A CG  1 
ATOM   360  O OD1 . ASN A 1 53  ? -11.379 45.834 24.877 1.00 67.22 ? 47  ASN A OD1 1 
ATOM   361  N ND2 . ASN A 1 53  ? -10.158 43.960 24.696 1.00 49.75 ? 47  ASN A ND2 1 
ATOM   362  N N   . GLY A 1 54  ? -6.578  48.013 23.028 1.00 22.51 ? 48  GLY A N   1 
ATOM   363  C CA  . GLY A 1 54  ? -5.608  48.459 22.052 1.00 2.21  ? 48  GLY A CA  1 
ATOM   364  C C   . GLY A 1 54  ? -6.091  49.632 21.225 1.00 86.84 ? 48  GLY A C   1 
ATOM   365  O O   . GLY A 1 54  ? -5.293  50.481 20.831 1.00 13.77 ? 48  GLY A O   1 
ATOM   366  N N   . ARG A 1 55  ? -7.408  49.750 21.068 1.00 3.01  ? 49  ARG A N   1 
ATOM   367  C CA  . ARG A 1 55  ? -7.984  50.774 20.195 1.00 18.12 ? 49  ARG A CA  1 
ATOM   368  C C   . ARG A 1 55  ? -7.320  52.125 20.432 1.00 2.00  ? 49  ARG A C   1 
ATOM   369  O O   . ARG A 1 55  ? -7.003  52.843 19.481 1.00 77.23 ? 49  ARG A O   1 
ATOM   370  C CB  . ARG A 1 55  ? -9.503  50.897 20.397 1.00 17.21 ? 49  ARG A CB  1 
ATOM   371  C CG  . ARG A 1 55  ? -10.310 49.699 19.903 1.00 44.42 ? 49  ARG A CG  1 
ATOM   372  C CD  . ARG A 1 55  ? -9.692  48.362 20.351 1.00 7.44  ? 49  ARG A CD  1 
ATOM   373  N NE  . ARG A 1 55  ? -9.536  47.407 19.239 1.00 38.30 ? 49  ARG A NE  1 
ATOM   374  C CZ  . ARG A 1 55  ? -8.397  46.899 18.757 1.00 84.97 ? 49  ARG A CZ  1 
ATOM   375  N NH1 . ARG A 1 55  ? -7.217  47.292 19.233 1.00 67.09 ? 49  ARG A NH1 1 
ATOM   376  N NH2 . ARG A 1 55  ? -8.453  46.018 17.748 1.00 15.51 ? 49  ARG A NH2 1 
ATOM   377  N N   . VAL A 1 56  ? -7.074  52.455 21.695 1.00 18.61 ? 50  VAL A N   1 
ATOM   378  C CA  . VAL A 1 56  ? -6.328  53.665 22.026 1.00 37.59 ? 50  VAL A CA  1 
ATOM   379  C C   . VAL A 1 56  ? -4.932  53.407 22.590 1.00 38.66 ? 50  VAL A C   1 
ATOM   380  O O   . VAL A 1 56  ? -4.771  52.806 23.656 1.00 28.95 ? 50  VAL A O   1 
ATOM   381  C CB  . VAL A 1 56  ? -7.061  54.529 23.031 1.00 11.87 ? 50  VAL A CB  1 
ATOM   382  C CG1 . VAL A 1 56  ? -6.463  55.911 23.037 1.00 2.00  ? 50  VAL A CG1 1 
ATOM   383  C CG2 . VAL A 1 56  ? -8.540  54.570 22.706 1.00 33.30 ? 50  VAL A CG2 1 
ATOM   384  N N   . ASN A 1 57  ? -3.970  54.113 22.006 1.00 47.51 ? 51  ASN A N   1 
ATOM   385  C CA  . ASN A 1 57  ? -2.565  53.824 22.206 1.00 23.76 ? 51  ASN A CA  1 
ATOM   386  C C   . ASN A 1 57  ? -1.762  55.118 22.285 1.00 30.91 ? 51  ASN A C   1 
ATOM   387  O O   . ASN A 1 57  ? -1.104  55.534 21.329 1.00 87.81 ? 51  ASN A O   1 
ATOM   388  C CB  . ASN A 1 57  ? -2.059  52.940 21.068 1.00 12.66 ? 51  ASN A CB  1 
ATOM   389  C CG  . ASN A 1 57  ? -0.934  52.031 21.502 1.00 23.60 ? 51  ASN A CG  1 
ATOM   390  O OD1 . ASN A 1 57  ? -0.061  52.428 22.279 1.00 34.32 ? 51  ASN A OD1 1 
ATOM   391  N ND2 . ASN A 1 57  ? -1.008  50.773 21.092 1.00 20.17 ? 51  ASN A ND2 1 
ATOM   392  N N   . VAL A 1 58  ? -1.854  55.761 23.438 1.00 11.21 ? 52  VAL A N   1 
ATOM   393  C CA  . VAL A 1 58  ? -1.211  57.042 23.657 1.00 8.95  ? 52  VAL A CA  1 
ATOM   394  C C   . VAL A 1 58  ? -0.117  56.950 24.718 1.00 32.11 ? 52  VAL A C   1 
ATOM   395  O O   . VAL A 1 58  ? -0.249  56.221 25.702 1.00 25.62 ? 52  VAL A O   1 
ATOM   396  C CB  . VAL A 1 58  ? -2.237  58.112 24.116 1.00 32.54 ? 52  VAL A CB  1 
ATOM   397  C CG1 . VAL A 1 58  ? -2.920  58.716 22.925 1.00 12.55 ? 52  VAL A CG1 1 
ATOM   398  C CG2 . VAL A 1 58  ? -3.278  57.484 25.037 1.00 22.64 ? 52  VAL A CG2 1 
ATOM   399  N N   . GLU A 1 59  ? 1.006   57.590 24.438 1.00 2.00  ? 53  GLU A N   1 
ATOM   400  C CA  . GLU A 1 59  ? 1.995   57.913 25.448 1.00 8.98  ? 53  GLU A CA  1 
ATOM   401  C C   . GLU A 1 59  ? 1.457   59.165 26.136 1.00 56.04 ? 53  GLU A C   1 
ATOM   402  O O   . GLU A 1 59  ? 1.328   60.201 25.493 1.00 18.07 ? 53  GLU A O   1 
ATOM   403  C CB  . GLU A 1 59  ? 3.342   58.232 24.777 1.00 13.97 ? 53  GLU A CB  1 
ATOM   404  C CG  . GLU A 1 59  ? 4.552   57.317 25.115 1.00 2.00  ? 53  GLU A CG  1 
ATOM   405  C CD  . GLU A 1 59  ? 5.760   57.621 24.187 1.00 93.51 ? 53  GLU A CD  1 
ATOM   406  O OE1 . GLU A 1 59  ? 5.736   57.185 23.030 1.00 6.27  ? 53  GLU A OE1 1 
ATOM   407  O OE2 . GLU A 1 59  ? 6.681   58.399 24.529 1.00 7.65  ? 53  GLU A OE2 1 
ATOM   408  N N   . VAL A 1 60  ? 0.971   59.032 27.365 1.00 41.32 ? 54  VAL A N   1 
ATOM   409  C CA  . VAL A 1 60  ? 0.528   60.205 28.109 1.00 12.95 ? 54  VAL A CA  1 
ATOM   410  C C   . VAL A 1 60  ? 1.725   61.055 28.535 1.00 21.10 ? 54  VAL A C   1 
ATOM   411  O O   . VAL A 1 60  ? 2.783   60.550 28.848 1.00 3.70  ? 54  VAL A O   1 
ATOM   412  C CB  . VAL A 1 60  ? -0.305  59.826 29.364 1.00 13.13 ? 54  VAL A CB  1 
ATOM   413  C CG1 . VAL A 1 60  ? -0.848  61.072 30.025 1.00 34.09 ? 54  VAL A CG1 1 
ATOM   414  C CG2 . VAL A 1 60  ? -1.444  58.935 28.979 1.00 2.00  ? 54  VAL A CG2 1 
ATOM   415  N N   . SER A 1 61  ? 1.566   62.365 28.482 1.00 2.21  ? 55  SER A N   1 
ATOM   416  C CA  . SER A 1 61  ? 2.705   63.254 28.599 1.00 5.58  ? 55  SER A CA  1 
ATOM   417  C C   . SER A 1 61  ? 3.244   63.403 30.015 1.00 13.79 ? 55  SER A C   1 
ATOM   418  O O   . SER A 1 61  ? 2.549   63.906 30.902 1.00 52.86 ? 55  SER A O   1 
ATOM   419  C CB  . SER A 1 61  ? 2.335   64.640 28.070 1.00 2.00  ? 55  SER A CB  1 
ATOM   420  O OG  . SER A 1 61  ? 3.332   65.564 28.450 1.00 10.94 ? 55  SER A OG  1 
ATOM   421  N N   . ALA A 1 62  ? 4.526   63.119 30.189 1.00 5.80  ? 56  ALA A N   1 
ATOM   422  C CA  . ALA A 1 62  ? 5.221   63.482 31.437 1.00 5.83  ? 56  ALA A CA  1 
ATOM   423  C C   . ALA A 1 62  ? 5.450   64.978 31.495 1.00 6.80  ? 56  ALA A C   1 
ATOM   424  O O   . ALA A 1 62  ? 5.518   65.553 32.572 1.00 12.29 ? 56  ALA A O   1 
ATOM   425  C CB  . ALA A 1 62  ? 6.553   62.743 31.573 1.00 2.00  ? 56  ALA A CB  1 
ATOM   426  N N   . GLU A 1 63  ? 5.458   65.636 30.343 1.00 57.38 ? 57  GLU A N   1 
ATOM   427  C CA  . GLU A 1 63  ? 5.623   67.081 30.359 1.00 32.28 ? 57  GLU A CA  1 
ATOM   428  C C   . GLU A 1 63  ? 4.431   67.765 30.968 1.00 14.29 ? 57  GLU A C   1 
ATOM   429  O O   . GLU A 1 63  ? 4.595   68.647 31.827 1.00 2.00  ? 57  GLU A O   1 
ATOM   430  C CB  . GLU A 1 63  ? 5.825   67.663 28.972 1.00 12.25 ? 57  GLU A CB  1 
ATOM   431  C CG  . GLU A 1 63  ? 6.247   69.139 29.062 1.00 2.00  ? 57  GLU A CG  1 
ATOM   432  C CD  . GLU A 1 63  ? 7.755   69.326 29.245 1.00 18.56 ? 57  GLU A CD  1 
ATOM   433  O OE1 . GLU A 1 63  ? 8.521   68.317 29.267 1.00 12.76 ? 57  GLU A OE1 1 
ATOM   434  O OE2 . GLU A 1 63  ? 8.177   70.502 29.308 1.00 42.48 ? 57  GLU A OE2 1 
ATOM   435  N N   . ASP A 1 64  ? 3.252   67.421 30.439 1.00 2.00  ? 58  ASP A N   1 
ATOM   436  C CA  . ASP A 1 64  ? 1.997   68.014 30.882 1.00 2.00  ? 58  ASP A CA  1 
ATOM   437  C C   . ASP A 1 64  ? 1.793   67.946 32.385 1.00 9.84  ? 58  ASP A C   1 
ATOM   438  O O   . ASP A 1 64  ? 1.500   68.945 33.023 1.00 14.44 ? 58  ASP A O   1 
ATOM   439  C CB  . ASP A 1 64  ? 0.797   67.352 30.196 1.00 2.00  ? 58  ASP A CB  1 
ATOM   440  C CG  . ASP A 1 64  ? -0.469  68.180 30.317 1.00 2.00  ? 58  ASP A CG  1 
ATOM   441  O OD1 . ASP A 1 64  ? -0.366  69.378 30.652 1.00 14.54 ? 58  ASP A OD1 1 
ATOM   442  O OD2 . ASP A 1 64  ? -1.560  67.664 29.984 1.00 20.80 ? 58  ASP A OD2 1 
ATOM   443  N N   . LEU A 1 65  ? 1.859   66.738 32.926 1.00 17.05 ? 59  LEU A N   1 
ATOM   444  C CA  . LEU A 1 65  ? 1.708   66.534 34.359 1.00 12.88 ? 59  LEU A CA  1 
ATOM   445  C C   . LEU A 1 65  ? 2.744   67.283 35.213 1.00 13.42 ? 59  LEU A C   1 
ATOM   446  O O   . LEU A 1 65  ? 2.402   67.915 36.215 1.00 23.56 ? 59  LEU A O   1 
ATOM   447  C CB  . LEU A 1 65  ? 1.780   65.046 34.670 1.00 19.35 ? 59  LEU A CB  1 
ATOM   448  C CG  . LEU A 1 65  ? 1.653   64.851 36.175 1.00 6.33  ? 59  LEU A CG  1 
ATOM   449  C CD1 . LEU A 1 65  ? 0.194   65.011 36.552 1.00 4.81  ? 59  LEU A CD1 1 
ATOM   450  C CD2 . LEU A 1 65  ? 2.210   63.510 36.583 1.00 14.82 ? 59  LEU A CD2 1 
ATOM   451  N N   . LEU A 1 66  ? 4.001   67.243 34.800 1.00 19.01 ? 60  LEU A N   1 
ATOM   452  C CA  . LEU A 1 66  ? 5.076   67.857 35.580 1.00 2.00  ? 60  LEU A CA  1 
ATOM   453  C C   . LEU A 1 66  ? 5.026   69.381 35.639 1.00 7.36  ? 60  LEU A C   1 
ATOM   454  O O   . LEU A 1 66  ? 5.252   69.980 36.693 1.00 9.19  ? 60  LEU A O   1 
ATOM   455  C CB  . LEU A 1 66  ? 6.422   67.396 35.035 1.00 2.00  ? 60  LEU A CB  1 
ATOM   456  C CG  . LEU A 1 66  ? 7.615   68.321 35.233 1.00 2.00  ? 60  LEU A CG  1 
ATOM   457  C CD1 . LEU A 1 66  ? 8.162   68.125 36.602 1.00 2.00  ? 60  LEU A CD1 1 
ATOM   458  C CD2 . LEU A 1 66  ? 8.631   68.069 34.164 1.00 2.00  ? 60  LEU A CD2 1 
ATOM   459  N N   . THR A 1 67  ? 4.802   70.012 34.491 1.00 45.74 ? 61  THR A N   1 
ATOM   460  C CA  . THR A 1 67  ? 4.745   71.470 34.425 1.00 2.00  ? 61  THR A CA  1 
ATOM   461  C C   . THR A 1 67  ? 3.378   72.018 34.854 1.00 16.06 ? 61  THR A C   1 
ATOM   462  O O   . THR A 1 67  ? 3.322   73.065 35.505 1.00 2.21  ? 61  THR A O   1 
ATOM   463  C CB  . THR A 1 67  ? 5.028   71.970 33.002 1.00 12.44 ? 61  THR A CB  1 
ATOM   464  O OG1 . THR A 1 67  ? 4.031   71.463 32.107 1.00 9.28  ? 61  THR A OG1 1 
ATOM   465  C CG2 . THR A 1 67  ? 6.382   71.522 32.542 1.00 4.81  ? 61  THR A CG2 1 
ATOM   466  N N   . CYS A 1 68  ? 2.287   71.368 34.412 1.00 6.43  ? 62  CYS A N   1 
ATOM   467  C CA  . CYS A 1 68  ? 0.932   71.927 34.523 1.00 12.10 ? 62  CYS A CA  1 
ATOM   468  C C   . CYS A 1 68  ? 0.090   71.612 35.762 1.00 38.45 ? 62  CYS A C   1 
ATOM   469  O O   . CYS A 1 68  ? -0.944  72.250 35.956 1.00 18.21 ? 62  CYS A O   1 
ATOM   470  C CB  . CYS A 1 68  ? 0.096   71.570 33.299 1.00 31.81 ? 62  CYS A CB  1 
ATOM   471  S SG  . CYS A 1 68  ? 0.431   72.556 31.813 1.00 30.39 ? 62  CYS A SG  1 
ATOM   472  N N   . CYS A 1 69  ? 0.510   70.642 36.581 1.00 17.84 ? 63  CYS A N   1 
ATOM   473  C CA  . CYS A 1 69  ? -0.288  70.173 37.717 1.00 8.14  ? 63  CYS A CA  1 
ATOM   474  C C   . CYS A 1 69  ? -0.490  71.189 38.832 1.00 70.84 ? 63  CYS A C   1 
ATOM   475  O O   . CYS A 1 69  ? -1.605  71.386 39.314 1.00 58.00 ? 63  CYS A O   1 
ATOM   476  C CB  . CYS A 1 69  ? 0.303   68.890 38.325 1.00 60.29 ? 63  CYS A CB  1 
ATOM   477  S SG  . CYS A 1 69  ? -0.687  68.237 39.720 1.00 18.34 ? 63  CYS A SG  1 
ATOM   478  N N   . GLY A 1 70  ? 0.615   71.718 39.337 1.00 2.00  ? 64  GLY A N   1 
ATOM   479  C CA  . GLY A 1 70  ? 0.542   72.740 40.362 1.00 17.50 ? 64  GLY A CA  1 
ATOM   480  C C   . GLY A 1 70  ? 1.003   72.278 41.729 1.00 38.84 ? 64  GLY A C   1 
ATOM   481  O O   . GLY A 1 70  ? 1.807   71.349 41.849 1.00 32.98 ? 64  GLY A O   1 
ATOM   482  N N   . ILE A 1 71  ? 0.417   72.872 42.761 1.00 67.35 ? 65  ILE A N   1 
ATOM   483  C CA  . ILE A 1 71  ? 0.778   72.595 44.147 1.00 12.63 ? 65  ILE A CA  1 
ATOM   484  C C   . ILE A 1 71  ? 0.305   71.208 44.649 1.00 2.00  ? 65  ILE A C   1 
ATOM   485  O O   . ILE A 1 71  ? 1.033   70.517 45.349 1.00 16.76 ? 65  ILE A O   1 
ATOM   486  C CB  . ILE A 1 71  ? 0.230   73.732 45.036 1.00 23.24 ? 65  ILE A CB  1 
ATOM   487  C CG1 . ILE A 1 71  ? 0.973   73.765 46.358 1.00 36.84 ? 65  ILE A CG1 1 
ATOM   488  C CG2 . ILE A 1 71  ? -1.269  73.626 45.186 1.00 4.51  ? 65  ILE A CG2 1 
ATOM   489  C CD1 . ILE A 1 71  ? 2.383   74.246 46.190 1.00 23.36 ? 65  ILE A CD1 1 
ATOM   490  N N   . GLN A 1 72  ? -0.900  70.811 44.235 1.00 7.18  ? 66  GLN A N   1 
ATOM   491  C CA  . GLN A 1 72  ? -1.481  69.486 44.493 1.00 2.00  ? 66  GLN A CA  1 
ATOM   492  C C   . GLN A 1 72  ? -0.465  68.333 44.306 1.00 28.50 ? 66  GLN A C   1 
ATOM   493  O O   . GLN A 1 72  ? -0.223  67.597 45.247 1.00 16.46 ? 66  GLN A O   1 
ATOM   494  C CB  . GLN A 1 72  ? -2.688  69.327 43.585 1.00 2.00  ? 66  GLN A CB  1 
ATOM   495  C CG  . GLN A 1 72  ? -3.204  67.928 43.393 1.00 29.80 ? 66  GLN A CG  1 
ATOM   496  C CD  . GLN A 1 72  ? -4.407  67.902 42.442 1.00 23.36 ? 66  GLN A CD  1 
ATOM   497  O OE1 . GLN A 1 72  ? -5.168  68.865 42.362 1.00 35.61 ? 66  GLN A OE1 1 
ATOM   498  N NE2 . GLN A 1 72  ? -4.520  66.847 41.653 1.00 81.51 ? 66  GLN A NE2 1 
ATOM   499  N N   . CYS A 1 73  ? 0.333   68.390 43.234 1.00 18.10 ? 67  CYS A N   1 
ATOM   500  C CA  . CYS A 1 73  ? 1.351   67.371 42.931 1.00 6.42  ? 67  CYS A CA  1 
ATOM   501  C C   . CYS A 1 73  ? 2.672   67.573 43.676 1.00 46.99 ? 67  CYS A C   1 
ATOM   502  O O   . CYS A 1 73  ? 3.662   66.884 43.397 1.00 10.87 ? 67  CYS A O   1 
ATOM   503  C CB  . CYS A 1 73  ? 1.667   67.351 41.418 1.00 2.00  ? 67  CYS A CB  1 
ATOM   504  S SG  . CYS A 1 73  ? 0.349   66.623 40.424 1.00 10.28 ? 67  CYS A SG  1 
ATOM   505  N N   . GLY A 1 74  ? 2.736   68.599 44.514 1.00 8.07  ? 68  GLY A N   1 
ATOM   506  C CA  . GLY A 1 74  ? 4.003   68.959 45.133 1.00 10.63 ? 68  GLY A CA  1 
ATOM   507  C C   . GLY A 1 74  ? 4.797   70.041 44.401 1.00 2.00  ? 68  GLY A C   1 
ATOM   508  O O   . GLY A 1 74  ? 4.220   70.989 43.864 1.00 26.73 ? 68  GLY A O   1 
ATOM   509  N N   . ASP A 1 75  ? 6.120   69.892 44.358 1.00 8.40  ? 69  ASP A N   1 
ATOM   510  C CA  . ASP A 1 75  ? 7.012   70.953 43.875 1.00 2.00  ? 69  ASP A CA  1 
ATOM   511  C C   . ASP A 1 75  ? 7.918   70.501 42.700 1.00 81.58 ? 69  ASP A C   1 
ATOM   512  O O   . ASP A 1 75  ? 9.170   70.609 42.740 1.00 7.65  ? 69  ASP A O   1 
ATOM   513  C CB  . ASP A 1 75  ? 7.862   71.472 45.039 1.00 45.23 ? 69  ASP A CB  1 
ATOM   514  C CG  . ASP A 1 75  ? 8.685   72.712 44.673 1.00 23.51 ? 69  ASP A CG  1 
ATOM   515  O OD1 . ASP A 1 75  ? 8.114   73.708 44.159 1.00 39.30 ? 69  ASP A OD1 1 
ATOM   516  O OD2 . ASP A 1 75  ? 9.917   72.671 44.910 1.00 65.80 ? 69  ASP A OD2 1 
ATOM   517  N N   . GLY A 1 76  ? 7.269   69.958 41.674 1.00 9.04  ? 70  GLY A N   1 
ATOM   518  C CA  . GLY A 1 76  ? 7.922   69.682 40.397 1.00 16.49 ? 70  GLY A CA  1 
ATOM   519  C C   . GLY A 1 76  ? 9.224   68.909 40.454 1.00 17.45 ? 70  GLY A C   1 
ATOM   520  O O   . GLY A 1 76  ? 9.296   67.861 41.094 1.00 36.68 ? 70  GLY A O   1 
ATOM   521  N N   . CYS A 1 77  ? 10.272  69.465 39.843 1.00 10.43 ? 71  CYS A N   1 
ATOM   522  C CA  . CYS A 1 77  ? 11.567  68.770 39.723 1.00 3.93  ? 71  CYS A CA  1 
ATOM   523  C C   . CYS A 1 77  ? 12.298  68.605 41.029 1.00 19.37 ? 71  CYS A C   1 
ATOM   524  O O   . CYS A 1 77  ? 13.324  67.923 41.081 1.00 12.01 ? 71  CYS A O   1 
ATOM   525  C CB  . CYS A 1 77  ? 12.500  69.479 38.728 1.00 47.05 ? 71  CYS A CB  1 
ATOM   526  S SG  . CYS A 1 77  ? 12.123  69.260 36.951 1.00 18.31 ? 71  CYS A SG  1 
ATOM   527  N N   . ASN A 1 78  ? 11.746  69.193 42.089 1.00 3.33  ? 72  ASN A N   1 
ATOM   528  C CA  . ASN A 1 78  ? 12.256  68.979 43.435 1.00 34.50 ? 72  ASN A CA  1 
ATOM   529  C C   . ASN A 1 78  ? 11.527  67.864 44.169 1.00 17.35 ? 72  ASN A C   1 
ATOM   530  O O   . ASN A 1 78  ? 11.777  67.642 45.357 1.00 36.94 ? 72  ASN A O   1 
ATOM   531  C CB  . ASN A 1 78  ? 12.169  70.272 44.245 1.00 3.92  ? 72  ASN A CB  1 
ATOM   532  C CG  . ASN A 1 78  ? 12.823  71.432 43.538 1.00 47.92 ? 72  ASN A CG  1 
ATOM   533  O OD1 . ASN A 1 78  ? 12.163  72.399 43.144 1.00 24.03 ? 72  ASN A OD1 1 
ATOM   534  N ND2 . ASN A 1 78  ? 14.109  71.288 43.262 1.00 55.98 ? 72  ASN A ND2 1 
ATOM   535  N N   . GLY A 1 79  ? 10.600  67.205 43.479 1.00 29.54 ? 73  GLY A N   1 
ATOM   536  C CA  . GLY A 1 79  ? 9.860   66.102 44.068 1.00 2.00  ? 73  GLY A CA  1 
ATOM   537  C C   . GLY A 1 79  ? 8.363   66.351 44.041 1.00 2.00  ? 73  GLY A C   1 
ATOM   538  O O   . GLY A 1 79  ? 7.935   67.499 43.916 1.00 6.87  ? 73  GLY A O   1 
ATOM   539  N N   . GLY A 1 80  ? 7.565   65.300 44.220 1.00 21.95 ? 74  GLY A N   1 
ATOM   540  C CA  . GLY A 1 80  ? 6.113   65.429 44.094 1.00 2.00  ? 74  GLY A CA  1 
ATOM   541  C C   . GLY A 1 80  ? 5.341   64.280 44.709 1.00 30.13 ? 74  GLY A C   1 
ATOM   542  O O   . GLY A 1 80  ? 5.956   63.325 45.195 1.00 19.14 ? 74  GLY A O   1 
ATOM   543  N N   . TYR A 1 81  ? 4.006   64.337 44.642 1.00 2.00  ? 75  TYR A N   1 
ATOM   544  C CA  . TYR A 1 81  ? 3.165   63.321 45.266 1.00 2.00  ? 75  TYR A CA  1 
ATOM   545  C C   . TYR A 1 81  ? 2.274   62.613 44.264 1.00 10.75 ? 75  TYR A C   1 
ATOM   546  O O   . TYR A 1 81  ? 1.267   63.164 43.795 1.00 2.00  ? 75  TYR A O   1 
ATOM   547  C CB  . TYR A 1 81  ? 2.303   63.903 46.419 1.00 3.34  ? 75  TYR A CB  1 
ATOM   548  C CG  . TYR A 1 81  ? 3.068   64.736 47.446 1.00 2.00  ? 75  TYR A CG  1 
ATOM   549  C CD1 . TYR A 1 81  ? 4.015   64.159 48.309 1.00 2.00  ? 75  TYR A CD1 1 
ATOM   550  C CD2 . TYR A 1 81  ? 2.958   66.121 47.437 1.00 27.71 ? 75  TYR A CD2 1 
ATOM   551  C CE1 . TYR A 1 81  ? 4.819   64.954 49.113 1.00 4.62  ? 75  TYR A CE1 1 
ATOM   552  C CE2 . TYR A 1 81  ? 3.769   66.922 48.230 1.00 13.08 ? 75  TYR A CE2 1 
ATOM   553  C CZ  . TYR A 1 81  ? 4.682   66.353 49.048 1.00 2.00  ? 75  TYR A CZ  1 
ATOM   554  O OH  . TYR A 1 81  ? 5.461   67.205 49.789 1.00 34.70 ? 75  TYR A OH  1 
ATOM   555  N N   . PRO A 1 82  ? 2.570   61.337 44.017 1.00 2.00  ? 76  PRO A N   1 
ATOM   556  C CA  . PRO A 1 82  ? 1.855   60.422 43.144 1.00 2.00  ? 76  PRO A CA  1 
ATOM   557  C C   . PRO A 1 82  ? 0.367   60.565 43.144 1.00 2.00  ? 76  PRO A C   1 
ATOM   558  O O   . PRO A 1 82  ? -0.255  60.566 42.095 1.00 23.65 ? 76  PRO A O   1 
ATOM   559  C CB  . PRO A 1 82  ? 2.291   59.040 43.652 1.00 2.20  ? 76  PRO A CB  1 
ATOM   560  C CG  . PRO A 1 82  ? 3.723   59.246 44.009 1.00 2.00  ? 76  PRO A CG  1 
ATOM   561  C CD  . PRO A 1 82  ? 3.803   60.711 44.542 1.00 2.00  ? 76  PRO A CD  1 
ATOM   562  N N   . SER A 1 83  ? -0.222  60.591 44.320 1.00 3.40  ? 77  SER A N   1 
ATOM   563  C CA  . SER A 1 83  ? -1.673  60.648 44.413 1.00 46.49 ? 77  SER A CA  1 
ATOM   564  C C   . SER A 1 83  ? -2.225  61.977 43.899 1.00 2.00  ? 77  SER A C   1 
ATOM   565  O O   . SER A 1 83  ? -3.261  61.996 43.256 1.00 4.93  ? 77  SER A O   1 
ATOM   566  C CB  . SER A 1 83  ? -2.136  60.394 45.849 1.00 15.20 ? 77  SER A CB  1 
ATOM   567  O OG  . SER A 1 83  ? -1.241  60.953 46.785 1.00 41.79 ? 77  SER A OG  1 
ATOM   568  N N   . GLY A 1 84  ? -1.467  63.053 44.056 1.00 2.00  ? 78  GLY A N   1 
ATOM   569  C CA  . GLY A 1 84  ? -1.799  64.304 43.374 1.00 16.54 ? 78  GLY A CA  1 
ATOM   570  C C   . GLY A 1 84  ? -1.808  64.193 41.846 1.00 3.80  ? 78  GLY A C   1 
ATOM   571  O O   . GLY A 1 84  ? -2.695  64.718 41.166 1.00 2.00  ? 78  GLY A O   1 
ATOM   572  N N   . ALA A 1 85  ? -0.888  63.383 41.329 1.00 2.00  ? 79  ALA A N   1 
ATOM   573  C CA  . ALA A 1 85  ? -0.779  63.086 39.899 1.00 7.81  ? 79  ALA A CA  1 
ATOM   574  C C   . ALA A 1 85  ? -2.087  62.521 39.362 1.00 2.00  ? 79  ALA A C   1 
ATOM   575  O O   . ALA A 1 85  ? -2.731  63.133 38.524 1.00 29.94 ? 79  ALA A O   1 
ATOM   576  C CB  . ALA A 1 85  ? 0.386   62.079 39.664 1.00 2.00  ? 79  ALA A CB  1 
ATOM   577  N N   . TRP A 1 86  ? -2.491  61.363 39.878 1.00 2.00  ? 80  TRP A N   1 
ATOM   578  C CA  . TRP A 1 86  ? -3.684  60.659 39.398 1.00 2.00  ? 80  TRP A CA  1 
ATOM   579  C C   . TRP A 1 86  ? -4.935  61.486 39.682 1.00 4.34  ? 80  TRP A C   1 
ATOM   580  O O   . TRP A 1 86  ? -5.977  61.293 39.060 1.00 29.54 ? 80  TRP A O   1 
ATOM   581  C CB  . TRP A 1 86  ? -3.817  59.305 40.091 1.00 2.00  ? 80  TRP A CB  1 
ATOM   582  C CG  . TRP A 1 86  ? -2.714  58.391 39.766 1.00 24.62 ? 80  TRP A CG  1 
ATOM   583  C CD1 . TRP A 1 86  ? -1.447  58.431 40.251 1.00 3.85  ? 80  TRP A CD1 1 
ATOM   584  C CD2 . TRP A 1 86  ? -2.752  57.320 38.818 1.00 8.98  ? 80  TRP A CD2 1 
ATOM   585  N NE1 . TRP A 1 86  ? -0.683  57.453 39.669 1.00 4.57  ? 80  TRP A NE1 1 
ATOM   586  C CE2 . TRP A 1 86  ? -1.457  56.749 38.790 1.00 2.00  ? 80  TRP A CE2 1 
ATOM   587  C CE3 . TRP A 1 86  ? -3.749  56.799 37.987 1.00 2.00  ? 80  TRP A CE3 1 
ATOM   588  C CZ2 . TRP A 1 86  ? -1.132  55.668 37.970 1.00 14.18 ? 80  TRP A CZ2 1 
ATOM   589  C CZ3 . TRP A 1 86  ? -3.432  55.721 37.163 1.00 11.09 ? 80  TRP A CZ3 1 
ATOM   590  C CH2 . TRP A 1 86  ? -2.130  55.163 37.165 1.00 5.29  ? 80  TRP A CH2 1 
ATOM   591  N N   . ASN A 1 87  ? -4.845  62.336 40.700 1.00 2.00  ? 81  ASN A N   1 
ATOM   592  C CA  . ASN A 1 87  ? -5.949  63.229 41.059 1.00 15.22 ? 81  ASN A CA  1 
ATOM   593  C C   . ASN A 1 87  ? -6.135  64.250 39.957 1.00 2.00  ? 81  ASN A C   1 
ATOM   594  O O   . ASN A 1 87  ? -7.217  64.366 39.384 1.00 19.46 ? 81  ASN A O   1 
ATOM   595  C CB  . ASN A 1 87  ? -5.643  63.955 42.376 1.00 15.45 ? 81  ASN A CB  1 
ATOM   596  C CG  . ASN A 1 87  ? -6.580  63.552 43.502 1.00 12.08 ? 81  ASN A CG  1 
ATOM   597  O OD1 . ASN A 1 87  ? -6.720  64.282 44.484 1.00 27.01 ? 81  ASN A OD1 1 
ATOM   598  N ND2 . ASN A 1 87  ? -7.118  62.334 43.433 1.00 14.10 ? 81  ASN A ND2 1 
ATOM   599  N N   . PHE A 1 88  ? -5.031  64.899 39.576 1.00 21.61 ? 82  PHE A N   1 
ATOM   600  C CA  . PHE A 1 88  ? -5.028  65.886 38.502 1.00 15.02 ? 82  PHE A CA  1 
ATOM   601  C C   . PHE A 1 88  ? -5.501  65.258 37.189 1.00 7.00  ? 82  PHE A C   1 
ATOM   602  O O   . PHE A 1 88  ? -6.268  65.866 36.443 1.00 6.77  ? 82  PHE A O   1 
ATOM   603  C CB  . PHE A 1 88  ? -3.622  66.468 38.340 1.00 2.00  ? 82  PHE A CB  1 
ATOM   604  C CG  . PHE A 1 88  ? -3.489  67.463 37.202 1.00 25.05 ? 82  PHE A CG  1 
ATOM   605  C CD1 . PHE A 1 88  ? -3.800  68.803 37.383 1.00 21.51 ? 82  PHE A CD1 1 
ATOM   606  C CD2 . PHE A 1 88  ? -3.000  67.061 35.964 1.00 3.29  ? 82  PHE A CD2 1 
ATOM   607  C CE1 . PHE A 1 88  ? -3.624  69.716 36.358 1.00 43.21 ? 82  PHE A CE1 1 
ATOM   608  C CE2 . PHE A 1 88  ? -2.823  67.974 34.931 1.00 2.61  ? 82  PHE A CE2 1 
ATOM   609  C CZ  . PHE A 1 88  ? -3.134  69.300 35.135 1.00 32.87 ? 82  PHE A CZ  1 
ATOM   610  N N   . TRP A 1 89  ? -5.062  64.035 36.937 1.00 2.00  ? 83  TRP A N   1 
ATOM   611  C CA  . TRP A 1 89  ? -5.534  63.233 35.807 1.00 2.00  ? 83  TRP A CA  1 
ATOM   612  C C   . TRP A 1 89  ? -7.048  63.031 35.759 1.00 2.00  ? 83  TRP A C   1 
ATOM   613  O O   . TRP A 1 89  ? -7.652  63.171 34.702 1.00 22.12 ? 83  TRP A O   1 
ATOM   614  C CB  . TRP A 1 89  ? -4.823  61.880 35.804 1.00 2.00  ? 83  TRP A CB  1 
ATOM   615  C CG  . TRP A 1 89  ? -5.144  60.987 34.648 1.00 11.65 ? 83  TRP A CG  1 
ATOM   616  C CD1 . TRP A 1 89  ? -5.176  61.324 33.328 1.00 44.50 ? 83  TRP A CD1 1 
ATOM   617  C CD2 . TRP A 1 89  ? -5.516  59.597 34.716 1.00 55.58 ? 83  TRP A CD2 1 
ATOM   618  N NE1 . TRP A 1 89  ? -5.556  60.239 32.571 1.00 20.83 ? 83  TRP A NE1 1 
ATOM   619  C CE2 . TRP A 1 89  ? -5.761  59.165 33.397 1.00 2.00  ? 83  TRP A CE2 1 
ATOM   620  C CE3 . TRP A 1 89  ? -5.668  58.686 35.764 1.00 2.14  ? 83  TRP A CE3 1 
ATOM   621  C CZ2 . TRP A 1 89  ? -6.143  57.854 33.092 1.00 27.07 ? 83  TRP A CZ2 1 
ATOM   622  C CZ3 . TRP A 1 89  ? -6.058  57.373 35.458 1.00 22.14 ? 83  TRP A CZ3 1 
ATOM   623  C CH2 . TRP A 1 89  ? -6.285  56.976 34.131 1.00 19.30 ? 83  TRP A CH2 1 
ATOM   624  N N   . THR A 1 90  ? -7.678  62.742 36.897 1.00 29.27 ? 84  THR A N   1 
ATOM   625  C CA  . THR A 1 90  ? -9.128  62.533 36.892 1.00 26.16 ? 84  THR A CA  1 
ATOM   626  C C   . THR A 1 90  ? -9.869  63.831 36.688 1.00 12.10 ? 84  THR A C   1 
ATOM   627  O O   . THR A 1 90  ? -11.020 63.835 36.229 1.00 7.93  ? 84  THR A O   1 
ATOM   628  C CB  . THR A 1 90  ? -9.685  61.885 38.190 1.00 3.53  ? 84  THR A CB  1 
ATOM   629  O OG1 . THR A 1 90  ? -9.323  62.681 39.322 1.00 39.22 ? 84  THR A OG1 1 
ATOM   630  C CG2 . THR A 1 90  ? -9.171  60.440 38.341 1.00 8.01  ? 84  THR A CG2 1 
ATOM   631  N N   . ARG A 1 91  ? -9.175  64.941 36.896 1.00 2.00  ? 85  ARG A N   1 
ATOM   632  C CA  . ARG A 1 91  ? -9.841  66.222 36.783 1.00 2.00  ? 85  ARG A CA  1 
ATOM   633  C C   . ARG A 1 91  ? -9.429  67.140 35.643 1.00 35.18 ? 85  ARG A C   1 
ATOM   634  O O   . ARG A 1 91  ? -10.256 67.462 34.796 1.00 16.16 ? 85  ARG A O   1 
ATOM   635  C CB  . ARG A 1 91  ? -9.792  66.926 38.121 1.00 16.54 ? 85  ARG A CB  1 
ATOM   636  C CG  . ARG A 1 91  ? -10.765 66.268 39.095 1.00 99.11 ? 85  ARG A CG  1 
ATOM   637  C CD  . ARG A 1 91  ? -10.090 65.965 40.392 1.00 67.62 ? 85  ARG A CD  1 
ATOM   638  N NE  . ARG A 1 91  ? -9.507  67.197 40.879 1.00 41.03 ? 85  ARG A NE  1 
ATOM   639  C CZ  . ARG A 1 91  ? -8.388  67.291 41.582 1.00 49.71 ? 85  ARG A CZ  1 
ATOM   640  N NH1 . ARG A 1 91  ? -7.915  66.271 42.285 1.00 42.09 ? 85  ARG A NH1 1 
ATOM   641  N NH2 . ARG A 1 91  ? -7.820  68.478 41.696 1.00 37.73 ? 85  ARG A NH2 1 
ATOM   642  N N   . LYS A 1 92  ? -8.172  67.563 35.601 1.00 6.32  ? 86  LYS A N   1 
ATOM   643  C CA  . LYS A 1 92  ? -7.717  68.348 34.470 1.00 2.00  ? 86  LYS A CA  1 
ATOM   644  C C   . LYS A 1 92  ? -7.304  67.397 33.312 1.00 25.53 ? 86  LYS A C   1 
ATOM   645  O O   . LYS A 1 92  ? -7.525  67.693 32.132 1.00 10.78 ? 86  LYS A O   1 
ATOM   646  C CB  . LYS A 1 92  ? -6.568  69.273 34.912 1.00 16.54 ? 86  LYS A CB  1 
ATOM   647  C CG  . LYS A 1 92  ? -6.729  70.796 34.459 1.00 41.38 ? 86  LYS A CG  1 
ATOM   648  C CD  . LYS A 1 92  ? -6.876  70.842 32.891 1.00 92.93 ? 86  LYS A CD  1 
ATOM   649  C CE  . LYS A 1 92  ? -6.516  72.174 32.171 1.00 25.48 ? 86  LYS A CE  1 
ATOM   650  N NZ  . LYS A 1 92  ? -7.520  73.282 32.390 1.00 51.22 ? 86  LYS A NZ  1 
ATOM   651  N N   . GLY A 1 93  ? -6.944  66.166 33.668 1.00 19.29 ? 87  GLY A N   1 
ATOM   652  C CA  . GLY A 1 93  ? -6.611  65.168 32.667 1.00 6.05  ? 87  GLY A CA  1 
ATOM   653  C C   . GLY A 1 93  ? -5.297  65.423 31.975 1.00 35.69 ? 87  GLY A C   1 
ATOM   654  O O   . GLY A 1 93  ? -4.625  66.392 32.280 1.00 2.00  ? 87  GLY A O   1 
ATOM   655  N N   . LEU A 1 94  ? -4.915  64.561 31.046 1.00 2.00  ? 88  LEU A N   1 
ATOM   656  C CA  . LEU A 1 94  ? -3.528  64.600 30.576 1.00 14.78 ? 88  LEU A CA  1 
ATOM   657  C C   . LEU A 1 94  ? -3.348  64.397 29.067 1.00 6.41  ? 88  LEU A C   1 
ATOM   658  O O   . LEU A 1 94  ? -3.947  63.490 28.484 1.00 4.70  ? 88  LEU A O   1 
ATOM   659  C CB  . LEU A 1 94  ? -2.680  63.583 31.370 1.00 2.00  ? 88  LEU A CB  1 
ATOM   660  C CG  . LEU A 1 94  ? -2.249  64.059 32.764 1.00 7.58  ? 88  LEU A CG  1 
ATOM   661  C CD1 . LEU A 1 94  ? -1.364  62.995 33.450 1.00 17.37 ? 88  LEU A CD1 1 
ATOM   662  C CD2 . LEU A 1 94  ? -1.525  65.384 32.669 1.00 2.00  ? 88  LEU A CD2 1 
ATOM   663  N N   . VAL A 1 95  ? -2.659  65.336 28.409 1.00 30.42 ? 89  VAL A N   1 
ATOM   664  C CA  . VAL A 1 95  ? -2.405  65.214 26.964 1.00 2.33  ? 89  VAL A CA  1 
ATOM   665  C C   . VAL A 1 95  ? -1.310  64.180 26.680 1.00 11.42 ? 89  VAL A C   1 
ATOM   666  O O   . VAL A 1 95  ? -0.653  63.683 27.603 1.00 19.03 ? 89  VAL A O   1 
ATOM   667  C CB  . VAL A 1 95  ? -2.004  66.559 26.299 1.00 18.74 ? 89  VAL A CB  1 
ATOM   668  C CG1 . VAL A 1 95  ? -3.105  67.600 26.501 1.00 18.96 ? 89  VAL A CG1 1 
ATOM   669  C CG2 . VAL A 1 95  ? -0.647  67.044 26.821 1.00 5.78  ? 89  VAL A CG2 1 
ATOM   670  N N   . SER A 1 96  ? -1.173  63.789 25.415 1.00 3.13  ? 90  SER A N   1 
ATOM   671  C CA  . SER A 1 96  ? -0.095  62.891 25.024 1.00 90.12 ? 90  SER A CA  1 
ATOM   672  C C   . SER A 1 96  ? 1.191   63.654 24.746 1.00 10.74 ? 90  SER A C   1 
ATOM   673  O O   . SER A 1 96  ? 1.182   64.879 24.559 1.00 15.81 ? 90  SER A O   1 
ATOM   674  C CB  . SER A 1 96  ? -0.479  62.090 23.788 1.00 10.18 ? 90  SER A CB  1 
ATOM   675  O OG  . SER A 1 96  ? -0.552  62.920 22.632 1.00 7.49  ? 90  SER A OG  1 
ATOM   676  N N   . GLY A 1 97  ? 2.299   62.917 24.705 1.00 32.50 ? 91  GLY A N   1 
ATOM   677  C CA  . GLY A 1 97  ? 3.598   63.540 24.550 1.00 4.85  ? 91  GLY A CA  1 
ATOM   678  C C   . GLY A 1 97  ? 4.708   62.516 24.540 1.00 51.41 ? 91  GLY A C   1 
ATOM   679  O O   . GLY A 1 97  ? 4.937   61.833 25.537 1.00 11.03 ? 91  GLY A O   1 
ATOM   680  N N   . GLY A 1 98  ? 5.353   62.365 23.388 1.00 6.80  ? 92  GLY A N   1 
ATOM   681  C CA  . GLY A 1 98  ? 6.466   61.443 23.275 1.00 2.00  ? 92  GLY A CA  1 
ATOM   682  C C   . GLY A 1 98  ? 7.669   61.799 24.114 1.00 14.05 ? 92  GLY A C   1 
ATOM   683  O O   . GLY A 1 98  ? 7.611   62.687 24.969 1.00 20.37 ? 92  GLY A O   1 
ATOM   684  N N   . VAL A 1 99  ? 8.773   61.103 23.862 1.00 50.72 ? 93  VAL A N   1 
ATOM   685  C CA  . VAL A 1 99  ? 10.024  61.370 24.560 1.00 9.77  ? 93  VAL A CA  1 
ATOM   686  C C   . VAL A 1 99  ? 10.719  62.602 23.975 1.00 9.42  ? 93  VAL A C   1 
ATOM   687  O O   . VAL A 1 99  ? 10.289  63.139 22.943 1.00 29.93 ? 93  VAL A O   1 
ATOM   688  C CB  . VAL A 1 99  ? 10.989  60.156 24.470 1.00 19.95 ? 93  VAL A CB  1 
ATOM   689  C CG1 . VAL A 1 99  ? 10.300  58.882 25.019 1.00 4.94  ? 93  VAL A CG1 1 
ATOM   690  C CG2 . VAL A 1 99  ? 11.436  59.949 23.034 1.00 29.11 ? 93  VAL A CG2 1 
ATOM   691  N N   . TYR A 1 100 ? 11.750  63.074 24.664 1.00 2.00  ? 94  TYR A N   1 
ATOM   692  C CA  . TYR A 1 100 ? 12.658  64.085 24.136 1.00 19.48 ? 94  TYR A CA  1 
ATOM   693  C C   . TYR A 1 100 ? 12.868  63.910 22.633 1.00 34.52 ? 94  TYR A C   1 
ATOM   694  O O   . TYR A 1 100 ? 13.026  62.787 22.147 1.00 23.40 ? 94  TYR A O   1 
ATOM   695  C CB  . TYR A 1 100 ? 13.994  63.972 24.851 1.00 2.80  ? 94  TYR A CB  1 
ATOM   696  C CG  . TYR A 1 100 ? 14.935  65.109 24.589 1.00 28.08 ? 94  TYR A CG  1 
ATOM   697  C CD1 . TYR A 1 100 ? 14.637  66.390 25.015 1.00 40.78 ? 94  TYR A CD1 1 
ATOM   698  C CD2 . TYR A 1 100 ? 16.227  64.854 24.157 1.00 52.10 ? 94  TYR A CD2 1 
ATOM   699  C CE1 . TYR A 1 100 ? 15.612  67.370 25.040 1.00 43.62 ? 94  TYR A CE1 1 
ATOM   700  C CE2 . TYR A 1 100 ? 17.202  65.814 24.193 1.00 38.75 ? 94  TYR A CE2 1 
ATOM   701  C CZ  . TYR A 1 100 ? 16.896  67.066 24.638 1.00 45.37 ? 94  TYR A CZ  1 
ATOM   702  O OH  . TYR A 1 100 ? 17.905  67.988 24.735 1.00 19.60 ? 94  TYR A OH  1 
ATOM   703  N N   . ASN A 1 101 ? 12.695  65.001 21.893 1.00 84.44 ? 95  ASN A N   1 
ATOM   704  C CA  . ASN A 1 101 ? 12.828  65.004 20.435 1.00 2.00  ? 95  ASN A CA  1 
ATOM   705  C C   . ASN A 1 101 ? 12.150  63.825 19.707 1.00 26.85 ? 95  ASN A C   1 
ATOM   706  O O   . ASN A 1 101 ? 12.479  63.511 18.562 1.00 37.74 ? 95  ASN A O   1 
ATOM   707  C CB  . ASN A 1 101 ? 14.317  65.092 20.039 1.00 37.46 ? 95  ASN A CB  1 
ATOM   708  C CG  . ASN A 1 101 ? 14.519  65.364 18.546 1.00 39.97 ? 95  ASN A CG  1 
ATOM   709  O OD1 . ASN A 1 101 ? 14.309  66.483 18.066 1.00 53.79 ? 95  ASN A OD1 1 
ATOM   710  N ND2 . ASN A 1 101 ? 14.930  64.336 17.810 1.00 72.96 ? 95  ASN A ND2 1 
ATOM   711  N N   . SER A 1 102 ? 11.136  63.241 20.335 1.00 23.88 ? 96  SER A N   1 
ATOM   712  C CA  . SER A 1 102 ? 10.320  62.231 19.667 1.00 68.78 ? 96  SER A CA  1 
ATOM   713  C C   . SER A 1 102 ? 9.500   62.879 18.582 1.00 16.24 ? 96  SER A C   1 
ATOM   714  O O   . SER A 1 102 ? 8.987   62.186 17.705 1.00 17.92 ? 96  SER A O   1 
ATOM   715  C CB  . SER A 1 102 ? 9.352   61.559 20.645 1.00 16.78 ? 96  SER A CB  1 
ATOM   716  O OG  . SER A 1 102 ? 8.068   62.190 20.668 1.00 11.05 ? 96  SER A OG  1 
ATOM   717  N N   . HIS A 1 103 ? 9.022   64.068 18.945 1.00 57.95 ? 97  HIS A N   1 
ATOM   718  C CA  . HIS A 1 103 ? 8.034   64.801 18.175 1.00 2.00  ? 97  HIS A CA  1 
ATOM   719  C C   . HIS A 1 103 ? 6.712   64.059 17.993 1.00 31.74 ? 97  HIS A C   1 
ATOM   720  O O   . HIS A 1 103 ? 6.105   64.158 16.932 1.00 17.23 ? 97  HIS A O   1 
ATOM   721  C CB  . HIS A 1 103 ? 8.583   65.145 16.789 1.00 65.95 ? 97  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 103 ? 9.664   66.174 16.813 1.00 50.88 ? 97  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 103 ? 9.428   67.492 17.125 1.00 14.43 ? 97  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 103 ? 11.007  66.059 16.650 1.00 2.00  ? 97  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 103 ? 10.571  68.147 17.173 1.00 37.10 ? 97  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 103 ? 11.547  67.301 16.887 1.00 43.75 ? 97  HIS A NE2 1 
ATOM   727  N N   . ILE A 1 104 ? 6.264   63.322 19.005 1.00 17.74 ? 98  ILE A N   1 
ATOM   728  C CA  . ILE A 1 104 ? 4.965   62.660 18.929 1.00 68.10 ? 98  ILE A CA  1 
ATOM   729  C C   . ILE A 1 104 ? 3.971   63.196 19.967 1.00 33.64 ? 98  ILE A C   1 
ATOM   730  O O   . ILE A 1 104 ? 4.371   63.826 20.962 1.00 7.11  ? 98  ILE A O   1 
ATOM   731  C CB  . ILE A 1 104 ? 5.096   61.104 19.049 1.00 46.51 ? 98  ILE A CB  1 
ATOM   732  C CG1 . ILE A 1 104 ? 5.064   60.659 20.507 1.00 75.17 ? 98  ILE A CG1 1 
ATOM   733  C CG2 . ILE A 1 104 ? 6.382   60.627 18.404 1.00 51.92 ? 98  ILE A CG2 1 
ATOM   734  C CD1 . ILE A 1 104 ? 4.477   59.284 20.701 1.00 29.01 ? 98  ILE A CD1 1 
ATOM   735  N N   . GLY A 1 105 ? 2.679   63.035 19.688 1.00 28.57 ? 99  GLY A N   1 
ATOM   736  C CA  . GLY A 1 105 ? 1.652   63.600 20.559 1.00 30.41 ? 99  GLY A CA  1 
ATOM   737  C C   . GLY A 1 105 ? 1.705   65.118 20.740 1.00 2.00  ? 99  GLY A C   1 
ATOM   738  O O   . GLY A 1 105 ? 2.416   65.802 19.998 1.00 30.83 ? 99  GLY A O   1 
ATOM   739  N N   . CYS A 1 106 ? 1.065   65.624 21.794 1.00 10.54 ? 100 CYS A N   1 
ATOM   740  C CA  . CYS A 1 106 ? 0.974   67.072 22.064 1.00 13.37 ? 100 CYS A CA  1 
ATOM   741  C C   . CYS A 1 106 ? 2.247   67.684 22.667 1.00 2.00  ? 100 CYS A C   1 
ATOM   742  O O   . CYS A 1 106 ? 2.856   68.573 22.082 1.00 35.42 ? 100 CYS A O   1 
ATOM   743  C CB  . CYS A 1 106 ? -0.203  67.333 23.004 1.00 8.09  ? 100 CYS A CB  1 
ATOM   744  S SG  . CYS A 1 106 ? -0.423  69.026 23.627 1.00 27.26 ? 100 CYS A SG  1 
ATOM   745  N N   . LEU A 1 107 ? 2.595   67.254 23.874 1.00 23.75 ? 101 LEU A N   1 
ATOM   746  C CA  . LEU A 1 107 ? 3.793   67.732 24.567 1.00 31.70 ? 101 LEU A CA  1 
ATOM   747  C C   . LEU A 1 107 ? 4.770   66.590 24.835 1.00 79.51 ? 101 LEU A C   1 
ATOM   748  O O   . LEU A 1 107 ? 4.702   65.914 25.876 1.00 3.11  ? 101 LEU A O   1 
ATOM   749  C CB  . LEU A 1 107 ? 3.422   68.383 25.901 1.00 10.14 ? 101 LEU A CB  1 
ATOM   750  C CG  . LEU A 1 107 ? 2.602   69.671 25.867 1.00 54.54 ? 101 LEU A CG  1 
ATOM   751  C CD1 . LEU A 1 107 ? 1.964   69.951 27.234 1.00 2.00  ? 101 LEU A CD1 1 
ATOM   752  C CD2 . LEU A 1 107 ? 3.523   70.796 25.450 1.00 18.92 ? 101 LEU A CD2 1 
ATOM   753  N N   . PRO A 1 108 ? 5.674   66.337 23.882 1.00 13.32 ? 102 PRO A N   1 
ATOM   754  C CA  . PRO A 1 108 ? 6.942   65.671 24.175 1.00 38.65 ? 102 PRO A CA  1 
ATOM   755  C C   . PRO A 1 108 ? 7.685   66.280 25.354 1.00 5.99  ? 102 PRO A C   1 
ATOM   756  O O   . PRO A 1 108 ? 7.764   67.501 25.495 1.00 20.34 ? 102 PRO A O   1 
ATOM   757  C CB  . PRO A 1 108 ? 7.708   65.823 22.863 1.00 13.47 ? 102 PRO A CB  1 
ATOM   758  C CG  . PRO A 1 108 ? 6.633   65.662 21.858 1.00 27.42 ? 102 PRO A CG  1 
ATOM   759  C CD  . PRO A 1 108 ? 5.483   66.480 22.429 1.00 94.84 ? 102 PRO A CD  1 
ATOM   760  N N   . TYR A 1 109 ? 8.367   65.413 26.097 1.00 15.29 ? 103 TYR A N   1 
ATOM   761  C CA  . TYR A 1 109 ? 9.104   65.820 27.273 1.00 24.31 ? 103 TYR A CA  1 
ATOM   762  C C   . TYR A 1 109 ? 10.329  66.601 26.820 1.00 3.12  ? 103 TYR A C   1 
ATOM   763  O O   . TYR A 1 109 ? 11.007  66.209 25.862 1.00 17.34 ? 103 TYR A O   1 
ATOM   764  C CB  . TYR A 1 109 ? 9.522   64.585 28.062 1.00 4.91  ? 103 TYR A CB  1 
ATOM   765  C CG  . TYR A 1 109 ? 10.231  64.891 29.363 1.00 5.41  ? 103 TYR A CG  1 
ATOM   766  C CD1 . TYR A 1 109 ? 9.610   65.657 30.347 1.00 7.33  ? 103 TYR A CD1 1 
ATOM   767  C CD2 . TYR A 1 109 ? 11.444  64.287 29.674 1.00 2.00  ? 103 TYR A CD2 1 
ATOM   768  C CE1 . TYR A 1 109 ? 10.160  65.806 31.594 1.00 30.00 ? 103 TYR A CE1 1 
ATOM   769  C CE2 . TYR A 1 109 ? 11.987  64.408 30.942 1.00 22.08 ? 103 TYR A CE2 1 
ATOM   770  C CZ  . TYR A 1 109 ? 11.333  65.167 31.898 1.00 10.26 ? 103 TYR A CZ  1 
ATOM   771  O OH  . TYR A 1 109 ? 11.783  65.190 33.181 1.00 2.00  ? 103 TYR A OH  1 
ATOM   772  N N   . THR A 1 110 ? 10.630  67.682 27.533 1.00 21.31 ? 104 THR A N   1 
ATOM   773  C CA  . THR A 1 110 ? 11.602  68.686 27.070 1.00 2.00  ? 104 THR A CA  1 
ATOM   774  C C   . THR A 1 110 ? 12.858  68.722 27.910 1.00 27.28 ? 104 THR A C   1 
ATOM   775  O O   . THR A 1 110 ? 13.591  69.717 27.917 1.00 37.44 ? 104 THR A O   1 
ATOM   776  C CB  . THR A 1 110 ? 11.004  70.108 27.117 1.00 6.04  ? 104 THR A CB  1 
ATOM   777  O OG1 . THR A 1 110 ? 10.911  70.539 28.479 1.00 18.91 ? 104 THR A OG1 1 
ATOM   778  C CG2 . THR A 1 110 ? 9.625   70.133 26.463 1.00 84.91 ? 104 THR A CG2 1 
ATOM   779  N N   . ILE A 1 111 ? 13.033  67.709 28.739 1.00 27.48 ? 105 ILE A N   1 
ATOM   780  C CA  . ILE A 1 111 ? 14.282  67.602 29.465 1.00 2.00  ? 105 ILE A CA  1 
ATOM   781  C C   . ILE A 1 111 ? 15.091  66.381 29.037 1.00 21.29 ? 105 ILE A C   1 
ATOM   782  O O   . ILE A 1 111 ? 14.576  65.262 28.991 1.00 22.28 ? 105 ILE A O   1 
ATOM   783  C CB  . ILE A 1 111 ? 14.046  67.599 30.983 1.00 13.57 ? 105 ILE A CB  1 
ATOM   784  C CG1 . ILE A 1 111 ? 13.187  68.819 31.377 1.00 6.22  ? 105 ILE A CG1 1 
ATOM   785  C CG2 . ILE A 1 111 ? 15.384  67.650 31.711 1.00 2.03  ? 105 ILE A CG2 1 
ATOM   786  C CD1 . ILE A 1 111 ? 12.663  68.757 32.790 1.00 67.85 ? 105 ILE A CD1 1 
ATOM   787  N N   . PRO A 1 112 ? 16.290  66.629 28.503 1.00 41.35 ? 106 PRO A N   1 
ATOM   788  C CA  . PRO A 1 112 ? 17.263  65.665 27.988 1.00 18.46 ? 106 PRO A CA  1 
ATOM   789  C C   . PRO A 1 112 ? 17.497  64.444 28.876 1.00 17.22 ? 106 PRO A C   1 
ATOM   790  O O   . PRO A 1 112 ? 17.547  64.551 30.100 1.00 29.56 ? 106 PRO A O   1 
ATOM   791  C CB  . PRO A 1 112 ? 18.555  66.504 27.824 1.00 3.22  ? 106 PRO A CB  1 
ATOM   792  C CG  . PRO A 1 112 ? 18.250  67.836 28.502 1.00 72.15 ? 106 PRO A CG  1 
ATOM   793  C CD  . PRO A 1 112 ? 16.770  68.010 28.341 1.00 21.03 ? 106 PRO A CD  1 
ATOM   794  N N   . PRO A 1 113 ? 17.782  63.294 28.253 1.00 48.25 ? 107 PRO A N   1 
ATOM   795  C CA  . PRO A 1 113 ? 18.336  62.067 28.851 1.00 4.63  ? 107 PRO A CA  1 
ATOM   796  C C   . PRO A 1 113 ? 19.767  62.193 29.360 1.00 31.05 ? 107 PRO A C   1 
ATOM   797  O O   . PRO A 1 113 ? 20.573  62.943 28.817 1.00 27.99 ? 107 PRO A O   1 
ATOM   798  C CB  . PRO A 1 113 ? 18.229  61.030 27.730 1.00 2.00  ? 107 PRO A CB  1 
ATOM   799  C CG  . PRO A 1 113 ? 17.237  61.605 26.756 1.00 22.86 ? 107 PRO A CG  1 
ATOM   800  C CD  . PRO A 1 113 ? 17.411  63.102 26.846 1.00 2.00  ? 107 PRO A CD  1 
ATOM   801  N N   . CYS A 1 114 ? 20.055  61.497 30.450 1.00 6.96  ? 108 CYS A N   1 
ATOM   802  C CA  . CYS A 1 114 ? 21.397  61.464 31.020 1.00 10.71 ? 108 CYS A CA  1 
ATOM   803  C C   . CYS A 1 114 ? 21.721  60.165 31.795 1.00 10.29 ? 108 CYS A C   1 
ATOM   804  O O   . CYS A 1 114 ? 20.847  59.314 32.007 1.00 14.54 ? 108 CYS A O   1 
ATOM   805  C CB  . CYS A 1 114 ? 21.586  62.672 31.926 1.00 22.76 ? 108 CYS A CB  1 
ATOM   806  S SG  . CYS A 1 114 ? 20.292  62.816 33.209 1.00 23.65 ? 108 CYS A SG  1 
ATOM   807  N N   . GLU A 1 115 ? 22.992  59.990 32.147 1.00 13.30 ? 109 GLU A N   1 
ATOM   808  C CA  . GLU A 1 115 ? 23.447  58.805 32.881 1.00 20.29 ? 109 GLU A CA  1 
ATOM   809  C C   . GLU A 1 115 ? 23.084  58.863 34.366 1.00 13.92 ? 109 GLU A C   1 
ATOM   810  O O   . GLU A 1 115 ? 23.519  59.783 35.071 1.00 13.84 ? 109 GLU A O   1 
ATOM   811  C CB  . GLU A 1 115 ? 24.967  58.666 32.754 1.00 2.00  ? 109 GLU A CB  1 
ATOM   812  C CG  . GLU A 1 115 ? 25.463  58.617 31.319 1.00 28.94 ? 109 GLU A CG  1 
ATOM   813  C CD  . GLU A 1 115 ? 24.878  57.450 30.567 1.00 4.74  ? 109 GLU A CD  1 
ATOM   814  O OE1 . GLU A 1 115 ? 24.456  56.482 31.228 1.00 33.44 ? 109 GLU A OE1 1 
ATOM   815  O OE2 . GLU A 1 115 ? 24.826  57.501 29.329 1.00 30.01 ? 109 GLU A OE2 1 
ATOM   816  N N   . HIS A 1 116 ? 22.302  57.896 34.841 1.00 24.52 ? 110 HIS A N   1 
ATOM   817  C CA  . HIS A 1 116 ? 21.907  57.855 36.255 1.00 36.93 ? 110 HIS A CA  1 
ATOM   818  C C   . HIS A 1 116 ? 22.689  56.813 37.029 1.00 2.00  ? 110 HIS A C   1 
ATOM   819  O O   . HIS A 1 116 ? 22.168  55.747 37.315 1.00 21.17 ? 110 HIS A O   1 
ATOM   820  C CB  . HIS A 1 116 ? 20.418  57.541 36.414 1.00 31.22 ? 110 HIS A CB  1 
ATOM   821  C CG  . HIS A 1 116 ? 19.509  58.571 35.819 1.00 10.16 ? 110 HIS A CG  1 
ATOM   822  N ND1 . HIS A 1 116 ? 18.814  59.486 36.574 1.00 17.63 ? 110 HIS A ND1 1 
ATOM   823  C CD2 . HIS A 1 116 ? 19.185  58.823 34.531 1.00 2.00  ? 110 HIS A CD2 1 
ATOM   824  C CE1 . HIS A 1 116 ? 18.121  60.274 35.779 1.00 11.69 ? 110 HIS A CE1 1 
ATOM   825  N NE2 . HIS A 1 116 ? 18.336  59.895 34.528 1.00 5.14  ? 110 HIS A NE2 1 
ATOM   826  N N   . HIS A 1 117 ? 23.879  57.203 37.495 1.00 26.32 ? 111 HIS A N   1 
ATOM   827  C CA  . HIS A 1 117 ? 24.791  56.348 38.281 1.00 5.69  ? 111 HIS A CA  1 
ATOM   828  C C   . HIS A 1 117 ? 25.427  55.186 37.509 1.00 84.36 ? 111 HIS A C   1 
ATOM   829  O O   . HIS A 1 117 ? 25.713  54.121 38.083 1.00 26.50 ? 111 HIS A O   1 
ATOM   830  C CB  . HIS A 1 117 ? 24.103  55.768 39.521 1.00 31.91 ? 111 HIS A CB  1 
ATOM   831  C CG  . HIS A 1 117 ? 23.253  56.747 40.268 1.00 7.67  ? 111 HIS A CG  1 
ATOM   832  N ND1 . HIS A 1 117 ? 23.768  57.855 40.904 1.00 69.09 ? 111 HIS A ND1 1 
ATOM   833  C CD2 . HIS A 1 117 ? 21.917  56.776 40.482 1.00 78.22 ? 111 HIS A CD2 1 
ATOM   834  C CE1 . HIS A 1 117 ? 22.785  58.527 41.479 1.00 10.97 ? 111 HIS A CE1 1 
ATOM   835  N NE2 . HIS A 1 117 ? 21.653  57.890 41.241 1.00 60.54 ? 111 HIS A NE2 1 
ATOM   836  N N   . VAL A 1 118 ? 25.648  55.403 36.215 1.00 9.90  ? 112 VAL A N   1 
ATOM   837  C CA  . VAL A 1 118 ? 26.214  54.395 35.327 1.00 12.34 ? 112 VAL A CA  1 
ATOM   838  C C   . VAL A 1 118 ? 27.198  55.060 34.359 1.00 49.84 ? 112 VAL A C   1 
ATOM   839  O O   . VAL A 1 118 ? 26.983  56.217 33.962 1.00 2.00  ? 112 VAL A O   1 
ATOM   840  C CB  . VAL A 1 118 ? 25.102  53.640 34.535 1.00 4.12  ? 112 VAL A CB  1 
ATOM   841  C CG1 . VAL A 1 118 ? 24.246  52.840 35.500 1.00 28.32 ? 112 VAL A CG1 1 
ATOM   842  C CG2 . VAL A 1 118 ? 24.210  54.613 33.763 1.00 25.39 ? 112 VAL A CG2 1 
ATOM   843  N N   . ASN A 1 119 ? 28.326  54.381 34.104 1.00 10.34 ? 113 ASN A N   1 
ATOM   844  C CA  . ASN A 1 119 ? 29.386  54.909 33.242 1.00 10.85 ? 113 ASN A CA  1 
ATOM   845  C C   . ASN A 1 119 ? 29.030  54.799 31.757 1.00 47.43 ? 113 ASN A C   1 
ATOM   846  O O   . ASN A 1 119 ? 29.615  53.998 31.020 1.00 18.52 ? 113 ASN A O   1 
ATOM   847  C CB  . ASN A 1 119 ? 30.708  54.168 33.514 1.00 39.04 ? 113 ASN A CB  1 
ATOM   848  C CG  . ASN A 1 119 ? 31.893  54.802 32.802 1.00 18.26 ? 113 ASN A CG  1 
ATOM   849  O OD1 . ASN A 1 119 ? 31.744  55.798 32.124 1.00 8.38  ? 113 ASN A OD1 1 
ATOM   850  N ND2 . ASN A 1 119 ? 33.059  54.196 32.927 1.00 17.75 ? 113 ASN A ND2 1 
ATOM   851  N N   . GLY A 1 120 ? 28.082  55.620 31.321 1.00 18.16 ? 114 GLY A N   1 
ATOM   852  C CA  . GLY A 1 120 ? 27.729  55.665 29.915 1.00 43.35 ? 114 GLY A CA  1 
ATOM   853  C C   . GLY A 1 120 ? 28.275  56.846 29.114 1.00 30.66 ? 114 GLY A C   1 
ATOM   854  O O   . GLY A 1 120 ? 29.236  57.518 29.508 1.00 33.26 ? 114 GLY A O   1 
ATOM   855  N N   . ALA A 1 121 ? 27.657  57.069 27.956 1.00 48.76 ? 115 ALA A N   1 
ATOM   856  C CA  . ALA A 1 121 ? 28.143  58.035 26.972 1.00 18.48 ? 115 ALA A CA  1 
ATOM   857  C C   . ALA A 1 121 ? 27.346  59.344 26.907 1.00 49.12 ? 115 ALA A C   1 
ATOM   858  O O   . ALA A 1 121 ? 27.778  60.311 26.274 1.00 38.19 ? 115 ALA A O   1 
ATOM   859  C CB  . ALA A 1 121 ? 28.187  57.385 25.591 1.00 60.77 ? 115 ALA A CB  1 
ATOM   860  N N   . ARG A 1 122 ? 26.144  59.342 27.477 1.00 36.78 ? 116 ARG A N   1 
ATOM   861  C CA  . ARG A 1 122 ? 25.391  60.581 27.653 1.00 8.86  ? 116 ARG A CA  1 
ATOM   862  C C   . ARG A 1 122 ? 25.984  61.425 28.767 1.00 15.32 ? 116 ARG A C   1 
ATOM   863  O O   . ARG A 1 122 ? 26.812  60.964 29.555 1.00 13.48 ? 116 ARG A O   1 
ATOM   864  C CB  . ARG A 1 122 ? 23.917  60.297 27.956 1.00 23.03 ? 116 ARG A CB  1 
ATOM   865  C CG  . ARG A 1 122 ? 23.207  59.484 26.888 1.00 2.00  ? 116 ARG A CG  1 
ATOM   866  C CD  . ARG A 1 122 ? 21.681  59.500 27.071 1.00 18.08 ? 116 ARG A CD  1 
ATOM   867  N NE  . ARG A 1 122 ? 21.273  58.984 28.375 1.00 75.58 ? 116 ARG A NE  1 
ATOM   868  C CZ  . ARG A 1 122 ? 21.349  57.707 28.740 1.00 30.70 ? 116 ARG A CZ  1 
ATOM   869  N NH1 . ARG A 1 122 ? 21.650  56.763 27.849 1.00 13.55 ? 116 ARG A NH1 1 
ATOM   870  N NH2 . ARG A 1 122 ? 21.011  57.362 29.974 1.00 36.36 ? 116 ARG A NH2 1 
ATOM   871  N N   . PRO A 1 123 ? 25.623  62.706 28.803 1.00 11.18 ? 117 PRO A N   1 
ATOM   872  C CA  . PRO A 1 123 ? 26.035  63.517 29.956 1.00 41.09 ? 117 PRO A CA  1 
ATOM   873  C C   . PRO A 1 123 ? 25.655  62.904 31.326 1.00 38.07 ? 117 PRO A C   1 
ATOM   874  O O   . PRO A 1 123 ? 24.672  62.170 31.447 1.00 41.25 ? 117 PRO A O   1 
ATOM   875  C CB  . PRO A 1 123 ? 25.355  64.864 29.702 1.00 36.76 ? 117 PRO A CB  1 
ATOM   876  C CG  . PRO A 1 123 ? 24.372  64.611 28.523 1.00 28.80 ? 117 PRO A CG  1 
ATOM   877  C CD  . PRO A 1 123 ? 24.986  63.509 27.748 1.00 25.25 ? 117 PRO A CD  1 
ATOM   878  N N   . PRO A 1 124 ? 26.518  63.094 32.338 1.00 46.06 ? 118 PRO A N   1 
ATOM   879  C CA  . PRO A 1 124 ? 26.159  63.033 33.765 1.00 84.90 ? 118 PRO A CA  1 
ATOM   880  C C   . PRO A 1 124 ? 24.873  63.808 34.089 1.00 21.46 ? 118 PRO A C   1 
ATOM   881  O O   . PRO A 1 124 ? 24.768  64.995 33.784 1.00 58.59 ? 118 PRO A O   1 
ATOM   882  C CB  . PRO A 1 124 ? 27.393  63.652 34.481 1.00 32.91 ? 118 PRO A CB  1 
ATOM   883  C CG  . PRO A 1 124 ? 28.207  64.317 33.333 1.00 37.90 ? 118 PRO A CG  1 
ATOM   884  C CD  . PRO A 1 124 ? 27.934  63.443 32.151 1.00 88.05 ? 118 PRO A CD  1 
ATOM   885  N N   . CYS A 1 125 ? 23.868  63.123 34.626 1.00 60.76 ? 119 CYS A N   1 
ATOM   886  C CA  . CYS A 1 125 ? 22.780  63.829 35.311 1.00 12.55 ? 119 CYS A CA  1 
ATOM   887  C C   . CYS A 1 125 ? 23.434  64.546 36.493 1.00 34.30 ? 119 CYS A C   1 
ATOM   888  O O   . CYS A 1 125 ? 24.441  64.062 37.032 1.00 39.03 ? 119 CYS A O   1 
ATOM   889  C CB  . CYS A 1 125 ? 21.730  62.861 35.858 1.00 21.24 ? 119 CYS A CB  1 
ATOM   890  S SG  . CYS A 1 125 ? 21.012  61.652 34.700 1.00 19.04 ? 119 CYS A SG  1 
ATOM   891  N N   . THR A 1 126 ? 22.899  65.694 36.893 1.00 57.23 ? 120 THR A N   1 
ATOM   892  C CA  . THR A 1 126 ? 23.482  66.419 38.025 1.00 90.65 ? 120 THR A CA  1 
ATOM   893  C C   . THR A 1 126 ? 22.478  67.273 38.789 1.00 63.18 ? 120 THR A C   1 
ATOM   894  O O   . THR A 1 126 ? 22.296  68.478 38.519 1.00 10.33 ? 120 THR A O   1 
ATOM   895  C CB  . THR A 1 126 ? 24.616  67.356 37.591 1.00 29.06 ? 120 THR A CB  1 
ATOM   896  O OG1 . THR A 1 126 ? 24.137  68.175 36.506 1.00 27.05 ? 120 THR A OG1 1 
ATOM   897  C CG2 . THR A 1 126 ? 25.878  66.577 37.173 1.00 89.66 ? 120 THR A CG2 1 
ATOM   898  N N   . GLY A 1 127 ? 21.915  66.677 39.826 1.00 80.10 ? 121 GLY A N   1 
ATOM   899  C CA  . GLY A 1 127 ? 21.042  67.438 40.685 1.00 93.04 ? 121 GLY A CA  1 
ATOM   900  C C   . GLY A 1 127 ? 19.757  67.750 39.957 1.00 87.08 ? 121 GLY A C   1 
ATOM   901  O O   . GLY A 1 127 ? 19.729  67.866 38.724 1.00 39.04 ? 121 GLY A O   1 
ATOM   902  N N   . GLU A 1 128 ? 18.672  67.747 40.722 1.00 42.04 ? 122 GLU A N   1 
ATOM   903  C CA  . GLU A 1 128 ? 17.341  67.960 40.153 1.00 40.96 ? 122 GLU A CA  1 
ATOM   904  C C   . GLU A 1 128 ? 17.292  69.214 39.304 1.00 80.02 ? 122 GLU A C   1 
ATOM   905  O O   . GLU A 1 128 ? 17.629  70.306 39.753 1.00 32.24 ? 122 GLU A O   1 
ATOM   906  C CB  . GLU A 1 128 ? 16.376  68.004 41.274 0.00 0.00  ? 122 GLU A CB  1 
ATOM   907  C CG  . GLU A 1 128 ? 16.075  66.682 41.899 0.00 0.00  ? 122 GLU A CG  1 
ATOM   908  C CD  . GLU A 1 128 ? 17.242  66.227 42.740 0.00 0.00  ? 122 GLU A CD  1 
ATOM   909  O OE1 . GLU A 1 128 ? 17.320  66.690 43.897 0.00 0.00  ? 122 GLU A OE1 1 
ATOM   910  O OE2 . GLU A 1 128 ? 18.035  65.350 42.269 0.00 0.00  ? 122 GLU A OE2 1 
ATOM   911  N N   . GLY A 1 129 ? 17.002  69.048 38.026 1.00 45.60 ? 123 GLY A N   1 
ATOM   912  C CA  . GLY A 1 129 ? 16.738  70.232 37.206 1.00 74.73 ? 123 GLY A CA  1 
ATOM   913  C C   . GLY A 1 129 ? 15.709  71.189 37.811 1.00 61.79 ? 123 GLY A C   1 
ATOM   914  O O   . GLY A 1 129 ? 15.052  70.876 38.807 1.00 65.98 ? 123 GLY A O   1 
ATOM   915  N N   . ASP A 1 130 ? 15.588  72.376 37.233 1.00 13.42 ? 124 ASP A N   1 
ATOM   916  C CA  . ASP A 1 130 ? 14.494  73.283 37.578 1.00 34.40 ? 124 ASP A CA  1 
ATOM   917  C C   . ASP A 1 130 ? 13.247  72.999 36.731 1.00 86.81 ? 124 ASP A C   1 
ATOM   918  O O   . ASP A 1 130 ? 13.355  72.764 35.521 1.00 33.02 ? 124 ASP A O   1 
ATOM   919  C CB  . ASP A 1 130 ? 14.937  74.750 37.406 1.00 47.58 ? 124 ASP A CB  1 
ATOM   920  C CG  . ASP A 1 130 ? 13.752  75.711 37.180 1.00 93.28 ? 124 ASP A CG  1 
ATOM   921  O OD1 . ASP A 1 130 ? 13.236  75.757 36.028 1.00 37.83 ? 124 ASP A OD1 1 
ATOM   922  O OD2 . ASP A 1 130 ? 13.301  76.377 38.150 1.00 45.37 ? 124 ASP A OD2 1 
ATOM   923  N N   . THR A 1 131 ? 12.074  73.193 37.337 1.00 37.37 ? 125 THR A N   1 
ATOM   924  C CA  . THR A 1 131 ? 10.793  73.018 36.647 1.00 43.87 ? 125 THR A CA  1 
ATOM   925  C C   . THR A 1 131 ? 10.480  74.123 35.622 1.00 17.75 ? 125 THR A C   1 
ATOM   926  O O   . THR A 1 131 ? 10.405  75.306 35.958 1.00 56.27 ? 125 THR A O   1 
ATOM   927  C CB  . THR A 1 131 ? 9.599   72.931 37.652 1.00 4.18  ? 125 THR A CB  1 
ATOM   928  O OG1 . THR A 1 131 ? 9.962   72.125 38.782 1.00 24.34 ? 125 THR A OG1 1 
ATOM   929  C CG2 . THR A 1 131 ? 8.394   72.284 36.958 1.00 26.59 ? 125 THR A CG2 1 
ATOM   930  N N   . PRO A 1 132 ? 10.180  73.722 34.381 1.00 26.68 ? 126 PRO A N   1 
ATOM   931  C CA  . PRO A 1 132 ? 9.561   74.554 33.330 1.00 16.85 ? 126 PRO A CA  1 
ATOM   932  C C   . PRO A 1 132 ? 8.138   75.074 33.580 1.00 25.76 ? 126 PRO A C   1 
ATOM   933  O O   . PRO A 1 132 ? 7.348   74.431 34.279 1.00 40.30 ? 126 PRO A O   1 
ATOM   934  C CB  . PRO A 1 132 ? 9.600   73.645 32.098 1.00 30.08 ? 126 PRO A CB  1 
ATOM   935  C CG  . PRO A 1 132 ? 9.879   72.235 32.657 1.00 18.35 ? 126 PRO A CG  1 
ATOM   936  C CD  . PRO A 1 132 ? 10.761  72.493 33.818 1.00 2.00  ? 126 PRO A CD  1 
ATOM   937  N N   . LYS A 1 133 ? 7.780   76.174 32.912 1.00 61.36 ? 127 LYS A N   1 
ATOM   938  C CA  . LYS A 1 133 ? 6.440   76.766 33.045 1.00 64.14 ? 127 LYS A CA  1 
ATOM   939  C C   . LYS A 1 133 ? 5.378   75.903 32.359 1.00 44.63 ? 127 LYS A C   1 
ATOM   940  O O   . LYS A 1 133 ? 5.716   74.946 31.663 1.00 19.03 ? 127 LYS A O   1 
ATOM   941  C CB  . LYS A 1 133 ? 6.424   78.182 32.464 1.00 40.45 ? 127 LYS A CB  1 
ATOM   942  C CG  . LYS A 1 133 ? 6.699   78.703 31.909 0.00 0.00  ? 127 LYS A CG  1 
ATOM   943  C CD  . LYS A 1 133 ? 6.495   80.224 31.988 0.00 0.00  ? 127 LYS A CD  1 
ATOM   944  C CE  . LYS A 1 133 ? 7.849   81.096 31.695 0.00 0.00  ? 127 LYS A CE  1 
ATOM   945  N NZ  . LYS A 1 133 ? 8.391   80.735 30.286 0.00 0.00  ? 127 LYS A NZ  1 
ATOM   946  N N   . CYS A 1 134 ? 4.102   76.179 32.622 1.00 4.18  ? 128 CYS A N   1 
ATOM   947  C CA  . CYS A 1 134 ? 3.053   75.389 31.997 1.00 15.93 ? 128 CYS A CA  1 
ATOM   948  C C   . CYS A 1 134 ? 2.456   76.165 30.849 1.00 62.50 ? 128 CYS A C   1 
ATOM   949  O O   . CYS A 1 134 ? 2.036   77.311 31.006 1.00 67.95 ? 128 CYS A O   1 
ATOM   950  C CB  . CYS A 1 134 ? 1.968   74.972 33.009 1.00 2.00  ? 128 CYS A CB  1 
ATOM   951  S SG  . CYS A 1 134 ? 0.302   74.497 32.395 1.00 28.41 ? 128 CYS A SG  1 
ATOM   952  N N   . ASN A 1 135 ? 2.642   75.606 29.660 1.00 28.91 ? 129 ASN A N   1 
ATOM   953  C CA  . ASN A 1 135 ? 2.134   76.188 28.429 1.00 54.45 ? 129 ASN A CA  1 
ATOM   954  C C   . ASN A 1 135 ? 0.967   75.347 27.952 1.00 49.46 ? 129 ASN A C   1 
ATOM   955  O O   . ASN A 1 135 ? 1.095   74.131 27.715 1.00 27.12 ? 129 ASN A O   1 
ATOM   956  C CB  . ASN A 1 135 ? 3.235   76.210 27.371 1.00 63.41 ? 129 ASN A CB  1 
ATOM   957  C CG  . ASN A 1 135 ? 4.520   76.824 27.887 1.00 39.88 ? 129 ASN A CG  1 
ATOM   958  O OD1 . ASN A 1 135 ? 4.624   78.040 28.017 1.00 43.38 ? 129 ASN A OD1 1 
ATOM   959  N ND2 . ASN A 1 135 ? 5.484   75.981 28.242 1.00 66.09 ? 129 ASN A ND2 1 
ATOM   960  N N   . LYS A 1 136 ? -0.209  75.951 27.963 1.00 30.55 ? 130 LYS A N   1 
ATOM   961  C CA  . LYS A 1 136 ? -1.395  75.212 27.543 1.00 36.62 ? 130 LYS A CA  1 
ATOM   962  C C   . LYS A 1 136 ? -1.498  75.201 26.025 1.00 27.17 ? 130 LYS A C   1 
ATOM   963  O O   . LYS A 1 136 ? -2.419  75.795 25.424 1.00 19.18 ? 130 LYS A O   1 
ATOM   964  C CB  . LYS A 1 136 ? -2.658  75.796 28.179 1.00 97.95 ? 130 LYS A CB  1 
ATOM   965  C CG  . LYS A 1 136 ? -3.043  75.134 29.487 1.00 30.98 ? 130 LYS A CG  1 
ATOM   966  C CD  . LYS A 1 136 ? -2.803  76.060 30.665 1.00 27.93 ? 130 LYS A CD  1 
ATOM   967  C CE  . LYS A 1 136 ? -3.632  75.627 31.888 1.00 36.37 ? 130 LYS A CE  1 
ATOM   968  N NZ  . LYS A 1 136 ? -3.647  76.645 32.994 1.00 18.10 ? 130 LYS A NZ  1 
ATOM   969  N N   . MET A 1 137 ? -0.472  74.607 25.417 1.00 18.18 ? 131 MET A N   1 
ATOM   970  C CA  . MET A 1 137 ? -0.372  74.484 23.974 1.00 32.55 ? 131 MET A CA  1 
ATOM   971  C C   . MET A 1 137 ? 0.704   73.462 23.512 1.00 28.44 ? 131 MET A C   1 
ATOM   972  O O   . MET A 1 137 ? 1.859   73.450 24.039 1.00 9.33  ? 131 MET A O   1 
ATOM   973  C CB  . MET A 1 137 ? -0.146  75.870 23.344 1.00 3.90  ? 131 MET A CB  1 
ATOM   974  C CG  . MET A 1 137 ? 0.752   76.814 24.143 1.00 64.06 ? 131 MET A CG  1 
ATOM   975  S SD  . MET A 1 137 ? 0.872   78.468 23.400 1.00 66.66 ? 131 MET A SD  1 
ATOM   976  C CE  . MET A 1 137 ? -0.848  78.877 23.157 1.00 32.40 ? 131 MET A CE  1 
ATOM   977  N N   . CYS A 1 138 ? 0.186   72.473 22.758 1.00 16.76 ? 132 CYS A N   1 
ATOM   978  C CA  . CYS A 1 138 ? 0.927   71.380 22.108 1.00 37.61 ? 132 CYS A CA  1 
ATOM   979  C C   . CYS A 1 138 ? 2.056   71.924 21.269 1.00 33.91 ? 132 CYS A C   1 
ATOM   980  O O   . CYS A 1 138 ? 1.904   73.008 20.741 1.00 34.17 ? 132 CYS A O   1 
ATOM   981  C CB  . CYS A 1 138 ? -0.010  70.632 21.172 1.00 8.43  ? 132 CYS A CB  1 
ATOM   982  S SG  . CYS A 1 138 ? -1.393  69.922 22.091 1.00 15.33 ? 132 CYS A SG  1 
ATOM   983  N N   . GLU A 1 139 ? 3.118   71.158 21.025 1.00 55.84 ? 133 GLU A N   1 
ATOM   984  C CA  . GLU A 1 139 ? 4.187   71.663 20.160 1.00 73.99 ? 133 GLU A CA  1 
ATOM   985  C C   . GLU A 1 139 ? 3.678   71.916 18.732 1.00 10.20 ? 133 GLU A C   1 
ATOM   986  O O   . GLU A 1 139 ? 2.767   71.222 18.247 1.00 36.05 ? 133 GLU A O   1 
ATOM   987  C CB  . GLU A 1 139 ? 5.360   70.687 20.125 1.00 2.00  ? 133 GLU A CB  1 
ATOM   988  C CG  . GLU A 1 139 ? 5.097   69.489 19.244 1.00 10.99 ? 133 GLU A CG  1 
ATOM   989  C CD  . GLU A 1 139 ? 6.218   68.449 19.262 1.00 36.23 ? 133 GLU A CD  1 
ATOM   990  O OE1 . GLU A 1 139 ? 7.368   68.743 19.696 1.00 19.21 ? 133 GLU A OE1 1 
ATOM   991  O OE2 . GLU A 1 139 ? 5.934   67.324 18.810 1.00 42.94 ? 133 GLU A OE2 1 
ATOM   992  N N   . ALA A 1 140 ? 4.280   72.896 18.056 1.00 62.15 ? 134 ALA A N   1 
ATOM   993  C CA  . ALA A 1 140 ? 3.869   73.278 16.702 1.00 50.52 ? 134 ALA A CA  1 
ATOM   994  C C   . ALA A 1 140 ? 4.093   72.150 15.712 1.00 42.23 ? 134 ALA A C   1 
ATOM   995  O O   . ALA A 1 140 ? 5.210   71.659 15.568 1.00 15.83 ? 134 ALA A O   1 
ATOM   996  C CB  . ALA A 1 140 ? 4.622   74.513 16.247 1.00 45.52 ? 134 ALA A CB  1 
ATOM   997  N N   . GLY A 1 141 ? 3.034   71.778 15.000 1.00 12.06 ? 135 GLY A N   1 
ATOM   998  C CA  . GLY A 1 141 ? 3.106   70.638 14.104 1.00 4.01  ? 135 GLY A CA  1 
ATOM   999  C C   . GLY A 1 141 ? 2.067   69.608 14.479 1.00 53.39 ? 135 GLY A C   1 
ATOM   1000 O O   . GLY A 1 141 ? 1.481   68.939 13.617 1.00 34.38 ? 135 GLY A O   1 
ATOM   1001 N N   . TYR A 1 142 ? 1.758   69.572 15.772 1.00 24.78 ? 136 TYR A N   1 
ATOM   1002 C CA  . TYR A 1 142 ? 0.743   68.669 16.286 1.00 42.14 ? 136 TYR A CA  1 
ATOM   1003 C C   . TYR A 1 142 ? -0.664  69.055 15.806 1.00 52.70 ? 136 TYR A C   1 
ATOM   1004 O O   . TYR A 1 142 ? -1.015  70.232 15.797 1.00 73.41 ? 136 TYR A O   1 
ATOM   1005 C CB  . TYR A 1 142 ? 0.806   68.652 17.809 1.00 9.66  ? 136 TYR A CB  1 
ATOM   1006 C CG  . TYR A 1 142 ? 0.059   67.491 18.388 1.00 52.77 ? 136 TYR A CG  1 
ATOM   1007 C CD1 . TYR A 1 142 ? 0.367   66.196 17.999 1.00 6.53  ? 136 TYR A CD1 1 
ATOM   1008 C CD2 . TYR A 1 142 ? -1.092  67.695 19.136 1.00 73.78 ? 136 TYR A CD2 1 
ATOM   1009 C CE1 . TYR A 1 142 ? -0.470  65.131 18.327 1.00 23.41 ? 136 TYR A CE1 1 
ATOM   1010 C CE2 . TYR A 1 142 ? -1.930  66.652 19.453 1.00 17.56 ? 136 TYR A CE2 1 
ATOM   1011 C CZ  . TYR A 1 142 ? -1.622  65.370 19.037 1.00 37.92 ? 136 TYR A CZ  1 
ATOM   1012 O OH  . TYR A 1 142 ? -2.545  64.360 19.201 1.00 29.47 ? 136 TYR A OH  1 
ATOM   1013 N N   . SER A 1 143 ? -1.445  68.061 15.384 1.00 20.13 ? 137 SER A N   1 
ATOM   1014 C CA  . SER A 1 143 ? -2.749  68.287 14.744 1.00 23.66 ? 137 SER A CA  1 
ATOM   1015 C C   . SER A 1 143 ? -3.777  69.056 15.582 1.00 83.13 ? 137 SER A C   1 
ATOM   1016 O O   . SER A 1 143 ? -4.160  70.179 15.219 1.00 28.95 ? 137 SER A O   1 
ATOM   1017 C CB  . SER A 1 143 ? -3.364  66.957 14.272 1.00 67.67 ? 137 SER A CB  1 
ATOM   1018 O OG  . SER A 1 143 ? -2.729  65.828 14.858 1.00 27.98 ? 137 SER A OG  1 
ATOM   1019 N N   . THR A 1 144 ? -4.244  68.450 16.675 1.00 92.03 ? 138 THR A N   1 
ATOM   1020 C CA  . THR A 1 144 ? -5.231  69.092 17.555 1.00 21.11 ? 138 THR A CA  1 
ATOM   1021 C C   . THR A 1 144 ? -4.608  69.999 18.610 1.00 2.52  ? 138 THR A C   1 
ATOM   1022 O O   . THR A 1 144 ? -3.389  70.002 18.823 1.00 49.22 ? 138 THR A O   1 
ATOM   1023 C CB  . THR A 1 144 ? -6.112  68.068 18.293 1.00 21.65 ? 138 THR A CB  1 
ATOM   1024 O OG1 . THR A 1 144 ? -5.302  67.300 19.187 1.00 31.22 ? 138 THR A OG1 1 
ATOM   1025 C CG2 . THR A 1 144 ? -6.809  67.144 17.307 1.00 47.52 ? 138 THR A CG2 1 
ATOM   1026 N N   . SER A 1 145 ? -5.460  70.737 19.321 1.00 59.48 ? 139 SER A N   1 
ATOM   1027 C CA  . SER A 1 145 ? -5.007  71.626 20.394 1.00 36.17 ? 139 SER A CA  1 
ATOM   1028 C C   . SER A 1 145 ? -4.959  70.904 21.749 1.00 46.22 ? 139 SER A C   1 
ATOM   1029 O O   . SER A 1 145 ? -5.624  69.876 21.923 1.00 13.60 ? 139 SER A O   1 
ATOM   1030 C CB  . SER A 1 145 ? -5.936  72.845 20.474 1.00 56.17 ? 139 SER A CB  1 
ATOM   1031 O OG  . SER A 1 145 ? -5.325  73.943 21.131 1.00 43.70 ? 139 SER A OG  1 
ATOM   1032 N N   . TYR A 1 146 ? -4.164  71.440 22.686 1.00 28.70 ? 140 TYR A N   1 
ATOM   1033 C CA  . TYR A 1 146 ? -4.054  70.955 24.081 1.00 11.92 ? 140 TYR A CA  1 
ATOM   1034 C C   . TYR A 1 146 ? -5.374  70.410 24.651 1.00 46.76 ? 140 TYR A C   1 
ATOM   1035 O O   . TYR A 1 146 ? -5.500  69.219 24.991 1.00 2.00  ? 140 TYR A O   1 
ATOM   1036 C CB  . TYR A 1 146 ? -3.535  72.091 24.963 1.00 15.14 ? 140 TYR A CB  1 
ATOM   1037 C CG  . TYR A 1 146 ? -3.210  71.735 26.401 1.00 40.38 ? 140 TYR A CG  1 
ATOM   1038 C CD1 . TYR A 1 146 ? -1.982  71.192 26.732 1.00 17.53 ? 140 TYR A CD1 1 
ATOM   1039 C CD2 . TYR A 1 146 ? -4.045  72.125 27.437 1.00 25.77 ? 140 TYR A CD2 1 
ATOM   1040 C CE1 . TYR A 1 146 ? -1.574  71.069 28.054 1.00 60.92 ? 140 TYR A CE1 1 
ATOM   1041 C CE2 . TYR A 1 146 ? -3.658  71.988 28.757 1.00 38.79 ? 140 TYR A CE2 1 
ATOM   1042 C CZ  . TYR A 1 146 ? -2.413  71.466 29.065 1.00 49.31 ? 140 TYR A CZ  1 
ATOM   1043 O OH  . TYR A 1 146 ? -1.998  71.366 30.380 1.00 23.45 ? 140 TYR A OH  1 
ATOM   1044 N N   . LYS A 1 147 ? -6.380  71.276 24.632 1.00 19.83 ? 141 LYS A N   1 
ATOM   1045 C CA  . LYS A 1 147 ? -7.746  70.950 25.053 1.00 27.73 ? 141 LYS A CA  1 
ATOM   1046 C C   . LYS A 1 147 ? -8.298  69.638 24.488 1.00 23.27 ? 141 LYS A C   1 
ATOM   1047 O O   . LYS A 1 147 ? -8.547  68.683 25.243 1.00 25.93 ? 141 LYS A O   1 
ATOM   1048 C CB  . LYS A 1 147 ? -8.683  72.089 24.671 1.00 11.42 ? 141 LYS A CB  1 
ATOM   1049 C CG  . LYS A 1 147 ? -9.719  72.390 25.713 1.00 31.92 ? 141 LYS A CG  1 
ATOM   1050 C CD  . LYS A 1 147 ? -9.404  73.670 26.471 1.00 67.43 ? 141 LYS A CD  1 
ATOM   1051 C CE  . LYS A 1 147 ? -10.654 74.573 26.560 1.00 29.18 ? 141 LYS A CE  1 
ATOM   1052 N NZ  . LYS A 1 147 ? -10.783 75.604 25.380 1.00 47.88 ? 141 LYS A NZ  1 
ATOM   1053 N N   . GLU A 1 148 ? -8.488  69.596 23.167 1.00 27.42 ? 142 GLU A N   1 
ATOM   1054 C CA  . GLU A 1 148 ? -8.970  68.398 22.466 1.00 73.27 ? 142 GLU A CA  1 
ATOM   1055 C C   . GLU A 1 148 ? -8.121  67.146 22.697 1.00 7.34  ? 142 GLU A C   1 
ATOM   1056 O O   . GLU A 1 148 ? -8.616  66.023 22.644 1.00 34.95 ? 142 GLU A O   1 
ATOM   1057 C CB  . GLU A 1 148 ? -9.045  68.674 20.991 1.00 22.77 ? 142 GLU A CB  1 
ATOM   1058 C CG  . GLU A 1 148 ? -10.033 67.905 20.204 0.00 0.00  ? 142 GLU A CG  1 
ATOM   1059 C CD  . GLU A 1 148 ? -11.376 68.581 20.329 0.00 0.00  ? 142 GLU A CD  1 
ATOM   1060 O OE1 . GLU A 1 148 ? -11.943 68.617 21.468 0.00 0.00  ? 142 GLU A OE1 1 
ATOM   1061 O OE2 . GLU A 1 148 ? -12.160 69.150 19.480 0.00 0.00  ? 142 GLU A OE2 1 
ATOM   1062 N N   . ASP A 1 149 ? -6.847  67.353 23.005 1.00 20.03 ? 143 ASP A N   1 
ATOM   1063 C CA  . ASP A 1 149 ? -5.915  66.251 23.235 1.00 56.88 ? 143 ASP A CA  1 
ATOM   1064 C C   . ASP A 1 149 ? -5.915  65.704 24.675 1.00 45.41 ? 143 ASP A C   1 
ATOM   1065 O O   . ASP A 1 149 ? -5.140  64.813 24.990 1.00 13.84 ? 143 ASP A O   1 
ATOM   1066 C CB  . ASP A 1 149 ? -4.490  66.695 22.843 1.00 2.00  ? 143 ASP A CB  1 
ATOM   1067 C CG  . ASP A 1 149 ? -3.574  65.533 22.508 1.00 2.00  ? 143 ASP A CG  1 
ATOM   1068 O OD1 . ASP A 1 149 ? -4.045  64.487 22.008 1.00 20.09 ? 143 ASP A OD1 1 
ATOM   1069 O OD2 . ASP A 1 149 ? -2.364  65.673 22.721 1.00 24.76 ? 143 ASP A OD2 1 
ATOM   1070 N N   . LYS A 1 150 ? -6.788  66.188 25.551 1.00 59.79 ? 144 LYS A N   1 
ATOM   1071 C CA  . LYS A 1 150 ? -6.762  65.689 26.933 1.00 11.89 ? 144 LYS A CA  1 
ATOM   1072 C C   . LYS A 1 150 ? -7.297  64.270 27.080 1.00 52.31 ? 144 LYS A C   1 
ATOM   1073 O O   . LYS A 1 150 ? -8.290  63.895 26.441 1.00 19.12 ? 144 LYS A O   1 
ATOM   1074 C CB  . LYS A 1 150 ? -7.527  66.610 27.880 1.00 18.11 ? 144 LYS A CB  1 
ATOM   1075 C CG  . LYS A 1 150 ? -6.764  67.861 28.310 1.00 3.62  ? 144 LYS A CG  1 
ATOM   1076 C CD  . LYS A 1 150 ? -5.603  67.567 29.237 1.00 6.03  ? 144 LYS A CD  1 
ATOM   1077 C CE  . LYS A 1 150 ? -5.006  68.896 29.709 1.00 16.11 ? 144 LYS A CE  1 
ATOM   1078 N NZ  . LYS A 1 150 ? -4.043  68.802 30.851 1.00 2.04  ? 144 LYS A NZ  1 
ATOM   1079 N N   . HIS A 1 151 ? -6.596  63.458 27.877 1.00 2.00  ? 145 HIS A N   1 
ATOM   1080 C CA  . HIS A 1 151 ? -7.101  62.125 28.189 1.00 31.13 ? 145 HIS A CA  1 
ATOM   1081 C C   . HIS A 1 151 ? -7.411  62.035 29.679 1.00 2.00  ? 145 HIS A C   1 
ATOM   1082 O O   . HIS A 1 151 ? -6.509  62.201 30.524 1.00 10.62 ? 145 HIS A O   1 
ATOM   1083 C CB  . HIS A 1 151 ? -6.082  61.046 27.792 1.00 7.52  ? 145 HIS A CB  1 
ATOM   1084 C CG  . HIS A 1 151 ? -5.730  61.044 26.325 1.00 30.39 ? 145 HIS A CG  1 
ATOM   1085 N ND1 . HIS A 1 151 ? -6.334  60.194 25.420 1.00 9.68  ? 145 HIS A ND1 1 
ATOM   1086 C CD2 . HIS A 1 151 ? -4.755  61.699 25.642 1.00 3.48  ? 145 HIS A CD2 1 
ATOM   1087 C CE1 . HIS A 1 151 ? -5.753  60.332 24.243 1.00 25.90 ? 145 HIS A CE1 1 
ATOM   1088 N NE2 . HIS A 1 151 ? -4.791  61.235 24.348 1.00 65.34 ? 145 HIS A NE2 1 
ATOM   1089 N N   . TYR A 1 152 ? -8.624  61.583 29.985 1.00 27.55 ? 146 TYR A N   1 
ATOM   1090 C CA  . TYR A 1 152 ? -9.170  61.674 31.345 1.00 2.00  ? 146 TYR A CA  1 
ATOM   1091 C C   . TYR A 1 152 ? -9.154  60.402 32.181 1.00 8.74  ? 146 TYR A C   1 
ATOM   1092 O O   . TYR A 1 152 ? -9.536  59.315 31.716 1.00 9.16  ? 146 TYR A O   1 
ATOM   1093 C CB  . TYR A 1 152 ? -10.593 62.207 31.269 1.00 4.99  ? 146 TYR A CB  1 
ATOM   1094 C CG  . TYR A 1 152 ? -10.626 63.695 31.062 1.00 8.72  ? 146 TYR A CG  1 
ATOM   1095 C CD1 . TYR A 1 152 ? -9.933  64.548 31.916 1.00 10.39 ? 146 TYR A CD1 1 
ATOM   1096 C CD2 . TYR A 1 152 ? -11.257 64.239 29.967 1.00 8.12  ? 146 TYR A CD2 1 
ATOM   1097 C CE1 . TYR A 1 152 ? -9.877  65.915 31.671 1.00 26.54 ? 146 TYR A CE1 1 
ATOM   1098 C CE2 . TYR A 1 152 ? -11.206 65.602 29.710 1.00 7.77  ? 146 TYR A CE2 1 
ATOM   1099 C CZ  . TYR A 1 152 ? -10.513 66.433 30.565 1.00 25.31 ? 146 TYR A CZ  1 
ATOM   1100 O OH  . TYR A 1 152 ? -10.421 67.776 30.281 1.00 32.25 ? 146 TYR A OH  1 
ATOM   1101 N N   . GLY A 1 153 ? -8.896  60.582 33.468 1.00 2.00  ? 147 GLY A N   1 
ATOM   1102 C CA  . GLY A 1 153 ? -9.122  59.501 34.398 1.00 4.48  ? 147 GLY A CA  1 
ATOM   1103 C C   . GLY A 1 153 ? -10.557 59.525 34.875 1.00 2.00  ? 147 GLY A C   1 
ATOM   1104 O O   . GLY A 1 153 ? -11.134 60.590 35.111 1.00 5.90  ? 147 GLY A O   1 
ATOM   1105 N N   . TYR A 1 154 ? -11.169 58.354 34.927 1.00 2.00  ? 148 TYR A N   1 
ATOM   1106 C CA  . TYR A 1 154 ? -12.478 58.238 35.544 1.00 24.12 ? 148 TYR A CA  1 
ATOM   1107 C C   . TYR A 1 154 ? -12.408 58.286 37.084 1.00 12.69 ? 148 TYR A C   1 
ATOM   1108 O O   . TYR A 1 154 ? -13.137 59.043 37.710 1.00 21.96 ? 148 TYR A O   1 
ATOM   1109 C CB  . TYR A 1 154 ? -13.156 56.955 35.071 1.00 2.00  ? 148 TYR A CB  1 
ATOM   1110 C CG  . TYR A 1 154 ? -14.468 56.705 35.763 1.00 21.61 ? 148 TYR A CG  1 
ATOM   1111 C CD1 . TYR A 1 154 ? -15.528 57.617 35.668 1.00 2.00  ? 148 TYR A CD1 1 
ATOM   1112 C CD2 . TYR A 1 154 ? -14.687 55.509 36.418 1.00 2.00  ? 148 TYR A CD2 1 
ATOM   1113 C CE1 . TYR A 1 154 ? -16.767 57.311 36.198 1.00 66.92 ? 148 TYR A CE1 1 
ATOM   1114 C CE2 . TYR A 1 154 ? -15.918 55.195 36.949 1.00 12.04 ? 148 TYR A CE2 1 
ATOM   1115 C CZ  . TYR A 1 154 ? -16.957 56.092 36.843 1.00 46.38 ? 148 TYR A CZ  1 
ATOM   1116 O OH  . TYR A 1 154 ? -18.176 55.767 37.402 1.00 29.44 ? 148 TYR A OH  1 
ATOM   1117 N N   . THR A 1 155 ? -11.642 57.373 37.681 1.00 9.68  ? 149 THR A N   1 
ATOM   1118 C CA  . THR A 1 155 ? -11.372 57.363 39.128 1.00 10.85 ? 149 THR A CA  1 
ATOM   1119 C C   . THR A 1 155 ? -9.888  57.192 39.406 1.00 15.11 ? 149 THR A C   1 
ATOM   1120 O O   . THR A 1 155 ? -9.125  56.740 38.546 1.00 3.99  ? 149 THR A O   1 
ATOM   1121 C CB  . THR A 1 155 ? -12.056 56.200 39.861 1.00 9.22  ? 149 THR A CB  1 
ATOM   1122 O OG1 . THR A 1 155 ? -11.497 54.957 39.409 1.00 14.66 ? 149 THR A OG1 1 
ATOM   1123 C CG2 . THR A 1 155 ? -13.562 56.195 39.601 1.00 50.55 ? 149 THR A CG2 1 
ATOM   1124 N N   . SER A 1 156 ? -9.468  57.615 40.593 1.00 15.57 ? 150 SER A N   1 
ATOM   1125 C CA  . SER A 1 156 ? -8.140  57.252 41.102 1.00 2.00  ? 150 SER A CA  1 
ATOM   1126 C C   . SER A 1 156 ? -8.204  56.847 42.582 1.00 2.00  ? 150 SER A C   1 
ATOM   1127 O O   . SER A 1 156 ? -9.177  57.156 43.283 1.00 36.98 ? 150 SER A O   1 
ATOM   1128 C CB  . SER A 1 156 ? -7.156  58.408 40.895 1.00 3.96  ? 150 SER A CB  1 
ATOM   1129 O OG  . SER A 1 156 ? -7.334  59.418 41.850 1.00 9.01  ? 150 SER A OG  1 
ATOM   1130 N N   . TYR A 1 157 ? -7.235  56.057 43.031 1.00 3.50  ? 151 TYR A N   1 
ATOM   1131 C CA  . TYR A 1 157 ? -7.285  55.550 44.396 1.00 7.71  ? 151 TYR A CA  1 
ATOM   1132 C C   . TYR A 1 157 ? -5.934  55.100 44.922 1.00 78.52 ? 151 TYR A C   1 
ATOM   1133 O O   . TYR A 1 157 ? -4.991  54.893 44.164 1.00 20.38 ? 151 TYR A O   1 
ATOM   1134 C CB  . TYR A 1 157 ? -8.277  54.381 44.484 1.00 2.00  ? 151 TYR A CB  1 
ATOM   1135 C CG  . TYR A 1 157 ? -8.314  53.501 43.245 1.00 9.75  ? 151 TYR A CG  1 
ATOM   1136 C CD1 . TYR A 1 157 ? -7.450  52.412 43.115 1.00 10.80 ? 151 TYR A CD1 1 
ATOM   1137 C CD2 . TYR A 1 157 ? -9.211  53.760 42.203 1.00 3.71  ? 151 TYR A CD2 1 
ATOM   1138 C CE1 . TYR A 1 157 ? -7.472  51.610 42.003 1.00 19.42 ? 151 TYR A CE1 1 
ATOM   1139 C CE2 . TYR A 1 157 ? -9.255  52.921 41.074 1.00 2.00  ? 151 TYR A CE2 1 
ATOM   1140 C CZ  . TYR A 1 157 ? -8.372  51.855 40.990 1.00 2.00  ? 151 TYR A CZ  1 
ATOM   1141 O OH  . TYR A 1 157 ? -8.349  51.050 39.880 1.00 29.94 ? 151 TYR A OH  1 
ATOM   1142 N N   . SER A 1 158 ? -5.832  55.048 46.240 1.00 16.93 ? 152 SER A N   1 
ATOM   1143 C CA  . SER A 1 158 ? -4.764  54.327 46.912 1.00 19.10 ? 152 SER A CA  1 
ATOM   1144 C C   . SER A 1 158 ? -5.144  52.852 47.113 1.00 2.30  ? 152 SER A C   1 
ATOM   1145 O O   . SER A 1 158 ? -6.325  52.543 47.275 1.00 17.20 ? 152 SER A O   1 
ATOM   1146 C CB  . SER A 1 158 ? -4.499  54.997 48.244 1.00 2.00  ? 152 SER A CB  1 
ATOM   1147 O OG  . SER A 1 158 ? -4.217  56.382 48.048 1.00 28.25 ? 152 SER A OG  1 
ATOM   1148 N N   . VAL A 1 159 ? -4.192  51.950 46.864 1.00 19.65 ? 153 VAL A N   1 
ATOM   1149 C CA  . VAL A 1 159 ? -4.347  50.520 47.170 1.00 2.00  ? 153 VAL A CA  1 
ATOM   1150 C C   . VAL A 1 159 ? -3.660  50.138 48.504 1.00 36.28 ? 153 VAL A C   1 
ATOM   1151 O O   . VAL A 1 159 ? -2.536  50.558 48.794 1.00 2.00  ? 153 VAL A O   1 
ATOM   1152 C CB  . VAL A 1 159 ? -3.772  49.623 46.037 1.00 18.52 ? 153 VAL A CB  1 
ATOM   1153 C CG1 . VAL A 1 159 ? -3.833  48.130 46.442 1.00 10.72 ? 153 VAL A CG1 1 
ATOM   1154 C CG2 . VAL A 1 159 ? -4.529  49.849 44.770 1.00 2.56  ? 153 VAL A CG2 1 
ATOM   1155 N N   . SER A 1 160 ? -4.332  49.328 49.315 1.00 26.73 ? 154 SER A N   1 
ATOM   1156 C CA  . SER A 1 160 ? -3.842  49.066 50.662 1.00 3.42  ? 154 SER A CA  1 
ATOM   1157 C C   . SER A 1 160 ? -2.604  48.184 50.682 1.00 35.95 ? 154 SER A C   1 
ATOM   1158 O O   . SER A 1 160 ? -2.311  47.495 49.706 1.00 9.24  ? 154 SER A O   1 
ATOM   1159 C CB  . SER A 1 160 ? -4.945  48.478 51.543 1.00 2.00  ? 154 SER A CB  1 
ATOM   1160 O OG  . SER A 1 160 ? -5.922  49.455 51.867 1.00 7.57  ? 154 SER A OG  1 
ATOM   1161 N N   . ASP A 1 161 ? -1.791  48.343 51.721 1.00 2.03  ? 155 ASP A N   1 
ATOM   1162 C CA  . ASP A 1 161 ? -0.643  47.453 51.965 1.00 16.69 ? 155 ASP A CA  1 
ATOM   1163 C C   . ASP A 1 161 ? -1.087  45.983 52.148 1.00 18.75 ? 155 ASP A C   1 
ATOM   1164 O O   . ASP A 1 161 ? -1.123  45.458 53.254 1.00 19.94 ? 155 ASP A O   1 
ATOM   1165 C CB  . ASP A 1 161 ? 0.128   47.946 53.195 1.00 2.00  ? 155 ASP A CB  1 
ATOM   1166 C CG  . ASP A 1 161 ? 1.456   47.234 53.404 1.00 23.56 ? 155 ASP A CG  1 
ATOM   1167 O OD1 . ASP A 1 161 ? 1.619   46.068 52.982 1.00 8.28  ? 155 ASP A OD1 1 
ATOM   1168 O OD2 . ASP A 1 161 ? 2.327   47.834 54.068 1.00 8.34  ? 155 ASP A OD2 1 
ATOM   1169 N N   . SER A 1 162 ? -1.426  45.326 51.048 1.00 21.51 ? 156 SER A N   1 
ATOM   1170 C CA  . SER A 1 162 ? -1.673  43.888 51.055 1.00 2.01  ? 156 SER A CA  1 
ATOM   1171 C C   . SER A 1 162 ? -1.173  43.304 49.729 1.00 2.70  ? 156 SER A C   1 
ATOM   1172 O O   . SER A 1 162 ? -1.450  43.851 48.658 1.00 19.63 ? 156 SER A O   1 
ATOM   1173 C CB  . SER A 1 162 ? -3.163  43.618 51.252 1.00 2.00  ? 156 SER A CB  1 
ATOM   1174 O OG  . SER A 1 162 ? -3.592  42.412 50.652 1.00 29.90 ? 156 SER A OG  1 
ATOM   1175 N N   . GLU A 1 163 ? -0.299  42.304 49.824 1.00 4.04  ? 157 GLU A N   1 
ATOM   1176 C CA  . GLU A 1 163 ? 0.284   41.663 48.648 1.00 2.00  ? 157 GLU A CA  1 
ATOM   1177 C C   . GLU A 1 163 ? -0.807  41.298 47.657 1.00 47.16 ? 157 GLU A C   1 
ATOM   1178 O O   . GLU A 1 163 ? -1.006  42.003 46.664 1.00 17.48 ? 157 GLU A O   1 
ATOM   1179 C CB  . GLU A 1 163 ? 1.064   40.413 49.080 1.00 48.06 ? 157 GLU A CB  1 
ATOM   1180 C CG  . GLU A 1 163 ? 2.106   39.906 48.086 1.00 3.72  ? 157 GLU A CG  1 
ATOM   1181 C CD  . GLU A 1 163 ? 2.873   38.689 48.595 1.00 2.00  ? 157 GLU A CD  1 
ATOM   1182 O OE1 . GLU A 1 163 ? 2.282   37.879 49.346 1.00 65.92 ? 157 GLU A OE1 1 
ATOM   1183 O OE2 . GLU A 1 163 ? 4.078   38.561 48.290 1.00 82.41 ? 157 GLU A OE2 1 
ATOM   1184 N N   . LYS A 1 164 ? -1.685  40.407 48.106 1.00 6.07  ? 158 LYS A N   1 
ATOM   1185 C CA  . LYS A 1 164 ? -2.746  39.848 47.281 1.00 32.97 ? 158 LYS A CA  1 
ATOM   1186 C C   . LYS A 1 164 ? -3.556  40.948 46.602 1.00 3.21  ? 158 LYS A C   1 
ATOM   1187 O O   . LYS A 1 164 ? -4.099  40.746 45.517 1.00 34.48 ? 158 LYS A O   1 
ATOM   1188 C CB  . LYS A 1 164 ? -3.672  38.963 48.143 1.00 17.17 ? 158 LYS A CB  1 
ATOM   1189 C CG  . LYS A 1 164 ? -4.493  38.056 47.305 0.00 0.00  ? 158 LYS A CG  1 
ATOM   1190 C CD  . LYS A 1 164 ? -3.664  36.769 47.171 0.00 0.00  ? 158 LYS A CD  1 
ATOM   1191 C CE  . LYS A 1 164 ? -3.533  36.213 45.637 0.00 0.00  ? 158 LYS A CE  1 
ATOM   1192 N NZ  . LYS A 1 164 ? -2.194  35.443 45.489 0.00 0.00  ? 158 LYS A NZ  1 
ATOM   1193 N N   . GLU A 1 165 ? -3.738  42.053 47.321 1.00 18.46 ? 159 GLU A N   1 
ATOM   1194 C CA  . GLU A 1 165 ? -4.466  43.213 46.812 1.00 34.11 ? 159 GLU A CA  1 
ATOM   1195 C C   . GLU A 1 165 ? -3.732  43.997 45.713 1.00 14.86 ? 159 GLU A C   1 
ATOM   1196 O O   . GLU A 1 165 ? -4.351  44.479 44.780 1.00 15.97 ? 159 GLU A O   1 
ATOM   1197 C CB  . GLU A 1 165 ? -4.745  44.155 47.960 1.00 6.79  ? 159 GLU A CB  1 
ATOM   1198 C CG  . GLU A 1 165 ? -5.799  45.202 47.692 1.00 13.91 ? 159 GLU A CG  1 
ATOM   1199 C CD  . GLU A 1 165 ? -5.944  46.141 48.908 1.00 43.00 ? 159 GLU A CD  1 
ATOM   1200 O OE1 . GLU A 1 165 ? -5.485  45.726 50.040 1.00 32.79 ? 159 GLU A OE1 1 
ATOM   1201 O OE2 . GLU A 1 165 ? -6.441  47.292 48.709 1.00 51.87 ? 159 GLU A OE2 1 
ATOM   1202 N N   . ILE A 1 166 ? -2.457  44.286 45.947 1.00 10.53 ? 160 ILE A N   1 
ATOM   1203 C CA  . ILE A 1 166 ? -1.629  44.938 44.953 1.00 2.00  ? 160 ILE A CA  1 
ATOM   1204 C C   . ILE A 1 166 ? -1.500  44.014 43.730 1.00 59.58 ? 160 ILE A C   1 
ATOM   1205 O O   . ILE A 1 166 ? -1.464  44.473 42.578 1.00 2.00  ? 160 ILE A O   1 
ATOM   1206 C CB  . ILE A 1 166 ? -0.254  45.246 45.552 1.00 8.20  ? 160 ILE A CB  1 
ATOM   1207 C CG1 . ILE A 1 166 ? -0.419  46.272 46.679 1.00 6.78  ? 160 ILE A CG1 1 
ATOM   1208 C CG2 . ILE A 1 166 ? 0.740   45.709 44.457 1.00 2.00  ? 160 ILE A CG2 1 
ATOM   1209 C CD1 . ILE A 1 166 ? 0.596   46.114 47.799 1.00 2.00  ? 160 ILE A CD1 1 
ATOM   1210 N N   . MET A 1 167 ? -1.569  42.710 43.988 1.00 2.00  ? 161 MET A N   1 
ATOM   1211 C CA  . MET A 1 167 ? -1.515  41.707 42.927 1.00 9.50  ? 161 MET A CA  1 
ATOM   1212 C C   . MET A 1 167 ? -2.797  41.636 42.120 1.00 15.13 ? 161 MET A C   1 
ATOM   1213 O O   . MET A 1 167 ? -2.772  41.741 40.902 1.00 9.83  ? 161 MET A O   1 
ATOM   1214 C CB  . MET A 1 167 ? -1.148  40.325 43.492 1.00 2.00  ? 161 MET A CB  1 
ATOM   1215 C CG  . MET A 1 167 ? 0.369   40.072 43.563 1.00 2.00  ? 161 MET A CG  1 
ATOM   1216 S SD  . MET A 1 167 ? 1.045   38.687 44.643 1.00 16.60 ? 161 MET A SD  1 
ATOM   1217 C CE  . MET A 1 167 ? 0.362   37.235 43.877 1.00 50.72 ? 161 MET A CE  1 
ATOM   1218 N N   . ALA A 1 168 ? -3.933  41.559 42.796 1.00 7.10  ? 162 ALA A N   1 
ATOM   1219 C CA  . ALA A 1 168 ? -5.223  41.606 42.114 1.00 21.80 ? 162 ALA A CA  1 
ATOM   1220 C C   . ALA A 1 168 ? -5.407  42.848 41.223 1.00 2.00  ? 162 ALA A C   1 
ATOM   1221 O O   . ALA A 1 168 ? -6.102  42.800 40.201 1.00 34.53 ? 162 ALA A O   1 
ATOM   1222 C CB  . ALA A 1 168 ? -6.346  41.528 43.140 1.00 5.78  ? 162 ALA A CB  1 
ATOM   1223 N N   . GLU A 1 169 ? -4.825  43.966 41.647 1.00 10.14 ? 163 GLU A N   1 
ATOM   1224 C CA  . GLU A 1 169 ? -4.966  45.235 40.933 1.00 2.00  ? 163 GLU A CA  1 
ATOM   1225 C C   . GLU A 1 169 ? -4.202  45.244 39.602 1.00 28.29 ? 163 GLU A C   1 
ATOM   1226 O O   . GLU A 1 169 ? -4.767  45.578 38.551 1.00 4.79  ? 163 GLU A O   1 
ATOM   1227 C CB  . GLU A 1 169 ? -4.498  46.383 41.830 1.00 2.00  ? 163 GLU A CB  1 
ATOM   1228 C CG  . GLU A 1 169 ? -4.537  47.785 41.183 1.00 12.67 ? 163 GLU A CG  1 
ATOM   1229 C CD  . GLU A 1 169 ? -5.916  48.200 40.690 1.00 2.00  ? 163 GLU A CD  1 
ATOM   1230 O OE1 . GLU A 1 169 ? -6.909  47.557 41.078 1.00 8.46  ? 163 GLU A OE1 1 
ATOM   1231 O OE2 . GLU A 1 169 ? -6.003  49.175 39.918 1.00 2.00  ? 163 GLU A OE2 1 
ATOM   1232 N N   . ILE A 1 170 ? -2.966  44.748 39.643 1.00 2.00  ? 164 ILE A N   1 
ATOM   1233 C CA  . ILE A 1 170 ? -2.104  44.663 38.474 1.00 5.26  ? 164 ILE A CA  1 
ATOM   1234 C C   . ILE A 1 170 ? -2.678  43.656 37.471 1.00 21.26 ? 164 ILE A C   1 
ATOM   1235 O O   . ILE A 1 170 ? -2.862  43.991 36.304 1.00 20.61 ? 164 ILE A O   1 
ATOM   1236 C CB  . ILE A 1 170 ? -0.661  44.302 38.901 1.00 4.93  ? 164 ILE A CB  1 
ATOM   1237 C CG1 . ILE A 1 170 ? -0.172  45.363 39.892 1.00 2.00  ? 164 ILE A CG1 1 
ATOM   1238 C CG2 . ILE A 1 170 ? 0.254   44.257 37.708 1.00 28.40 ? 164 ILE A CG2 1 
ATOM   1239 C CD1 . ILE A 1 170 ? 1.195   45.132 40.429 1.00 2.00  ? 164 ILE A CD1 1 
ATOM   1240 N N   . TYR A 1 171 ? -3.244  42.573 37.999 1.00 5.31  ? 165 TYR A N   1 
ATOM   1241 C CA  . TYR A 1 171 ? -3.822  41.493 37.179 1.00 2.00  ? 165 TYR A CA  1 
ATOM   1242 C C   . TYR A 1 171 ? -5.084  41.902 36.434 1.00 15.17 ? 165 TYR A C   1 
ATOM   1243 O O   . TYR A 1 171 ? -5.326  41.442 35.321 1.00 36.79 ? 165 TYR A O   1 
ATOM   1244 C CB  . TYR A 1 171 ? -4.140  40.271 38.046 1.00 2.00  ? 165 TYR A CB  1 
ATOM   1245 C CG  . TYR A 1 171 ? -4.535  39.059 37.252 1.00 22.05 ? 165 TYR A CG  1 
ATOM   1246 C CD1 . TYR A 1 171 ? -3.570  38.196 36.729 1.00 27.88 ? 165 TYR A CD1 1 
ATOM   1247 C CD2 . TYR A 1 171 ? -5.870  38.762 37.025 1.00 15.92 ? 165 TYR A CD2 1 
ATOM   1248 C CE1 . TYR A 1 171 ? -3.942  37.065 36.010 1.00 59.95 ? 165 TYR A CE1 1 
ATOM   1249 C CE2 . TYR A 1 171 ? -6.252  37.648 36.306 1.00 62.35 ? 165 TYR A CE2 1 
ATOM   1250 C CZ  . TYR A 1 171 ? -5.291  36.798 35.806 1.00 37.53 ? 165 TYR A CZ  1 
ATOM   1251 O OH  . TYR A 1 171 ? -5.692  35.655 35.146 1.00 22.42 ? 165 TYR A OH  1 
ATOM   1252 N N   . LYS A 1 172 ? -5.933  42.673 37.108 1.00 9.64  ? 166 LYS A N   1 
ATOM   1253 C CA  . LYS A 1 172 ? -7.224  43.076 36.566 1.00 2.00  ? 166 LYS A CA  1 
ATOM   1254 C C   . LYS A 1 172 ? -7.217  44.414 35.830 1.00 6.35  ? 166 LYS A C   1 
ATOM   1255 O O   . LYS A 1 172 ? -7.908  44.567 34.826 1.00 42.71 ? 166 LYS A O   1 
ATOM   1256 C CB  . LYS A 1 172 ? -8.264  43.118 37.681 1.00 23.09 ? 166 LYS A CB  1 
ATOM   1257 C CG  . LYS A 1 172 ? -9.396  42.099 37.525 1.00 51.30 ? 166 LYS A CG  1 
ATOM   1258 C CD  . LYS A 1 172 ? -8.895  40.642 37.565 1.00 27.82 ? 166 LYS A CD  1 
ATOM   1259 C CE  . LYS A 1 172 ? -9.358  39.831 36.326 1.00 63.06 ? 166 LYS A CE  1 
ATOM   1260 N NZ  . LYS A 1 172 ? -10.862 39.628 36.182 1.00 26.87 ? 166 LYS A NZ  1 
ATOM   1261 N N   . ASN A 1 173 ? -6.410  45.367 36.293 1.00 13.64 ? 167 ASN A N   1 
ATOM   1262 C CA  . ASN A 1 173 ? -6.393  46.709 35.704 1.00 2.00  ? 167 ASN A CA  1 
ATOM   1263 C C   . ASN A 1 173 ? -5.093  47.174 35.040 1.00 11.29 ? 167 ASN A C   1 
ATOM   1264 O O   . ASN A 1 173 ? -5.016  48.311 34.517 1.00 2.00  ? 167 ASN A O   1 
ATOM   1265 C CB  . ASN A 1 173 ? -6.810  47.741 36.755 1.00 23.93 ? 167 ASN A CB  1 
ATOM   1266 C CG  . ASN A 1 173 ? -8.252  47.584 37.169 1.00 48.76 ? 167 ASN A CG  1 
ATOM   1267 O OD1 . ASN A 1 173 ? -9.109  47.319 36.345 1.00 8.89  ? 167 ASN A OD1 1 
ATOM   1268 N ND2 . ASN A 1 173 ? -8.509  47.646 38.456 1.00 21.20 ? 167 ASN A ND2 1 
ATOM   1269 N N   . GLY A 1 174 ? -4.043  46.360 35.158 1.00 8.12  ? 168 GLY A N   1 
ATOM   1270 C CA  . GLY A 1 174 ? -2.760  46.721 34.579 1.00 2.00  ? 168 GLY A CA  1 
ATOM   1271 C C   . GLY A 1 174 ? -1.822  47.293 35.631 1.00 15.61 ? 168 GLY A C   1 
ATOM   1272 O O   . GLY A 1 174 ? -2.225  47.453 36.780 1.00 8.27  ? 168 GLY A O   1 
ATOM   1273 N N   . PRO A 1 175 ? -0.585  47.662 35.251 1.00 4.94  ? 169 PRO A N   1 
ATOM   1274 C CA  . PRO A 1 175 ? 0.459   48.297 36.080 1.00 2.00  ? 169 PRO A CA  1 
ATOM   1275 C C   . PRO A 1 175 ? -0.012  49.402 37.064 1.00 2.00  ? 169 PRO A C   1 
ATOM   1276 O O   . PRO A 1 175 ? -0.884  50.231 36.740 1.00 2.00  ? 169 PRO A O   1 
ATOM   1277 C CB  . PRO A 1 175 ? 1.385   48.882 35.056 1.00 2.00  ? 169 PRO A CB  1 
ATOM   1278 C CG  . PRO A 1 175 ? 1.158   48.073 33.844 1.00 9.65  ? 169 PRO A CG  1 
ATOM   1279 C CD  . PRO A 1 175 ? -0.265  47.746 33.822 1.00 2.00  ? 169 PRO A CD  1 
ATOM   1280 N N   . VAL A 1 176 ? 0.732   49.576 38.150 1.00 4.12  ? 170 VAL A N   1 
ATOM   1281 C CA  . VAL A 1 176 ? 0.411   50.655 39.100 1.00 6.73  ? 170 VAL A CA  1 
ATOM   1282 C C   . VAL A 1 176 ? 1.632   51.514 39.418 1.00 2.00  ? 170 VAL A C   1 
ATOM   1283 O O   . VAL A 1 176 ? 2.761   51.076 39.230 1.00 3.75  ? 170 VAL A O   1 
ATOM   1284 C CB  . VAL A 1 176 ? -0.136  50.083 40.438 1.00 3.12  ? 170 VAL A CB  1 
ATOM   1285 C CG1 . VAL A 1 176 ? -1.287  49.121 40.163 1.00 2.00  ? 170 VAL A CG1 1 
ATOM   1286 C CG2 . VAL A 1 176 ? 0.997   49.383 41.201 1.00 2.00  ? 170 VAL A CG2 1 
ATOM   1287 N N   . GLU A 1 177 ? 1.424   52.612 40.134 1.00 7.99  ? 171 GLU A N   1 
ATOM   1288 C CA  . GLU A 1 177 ? 2.543   53.396 40.594 1.00 2.00  ? 171 GLU A CA  1 
ATOM   1289 C C   . GLU A 1 177 ? 2.874   53.098 42.035 1.00 2.00  ? 171 GLU A C   1 
ATOM   1290 O O   . GLU A 1 177 ? 1.980   52.978 42.849 1.00 6.31  ? 171 GLU A O   1 
ATOM   1291 C CB  . GLU A 1 177 ? 2.244   54.863 40.427 1.00 2.00  ? 171 GLU A CB  1 
ATOM   1292 C CG  . GLU A 1 177 ? 3.484   55.676 40.516 1.00 2.00  ? 171 GLU A CG  1 
ATOM   1293 C CD  . GLU A 1 177 ? 3.229   57.146 40.413 1.00 2.00  ? 171 GLU A CD  1 
ATOM   1294 O OE1 . GLU A 1 177 ? 2.055   57.573 40.249 1.00 10.06 ? 171 GLU A OE1 1 
ATOM   1295 O OE2 . GLU A 1 177 ? 4.215   57.882 40.438 1.00 2.00  ? 171 GLU A OE2 1 
ATOM   1296 N N   . GLY A 1 178 ? 4.154   52.933 42.328 1.00 2.00  ? 172 GLY A N   1 
ATOM   1297 C CA  . GLY A 1 178 ? 4.612   52.733 43.689 1.00 2.00  ? 172 GLY A CA  1 
ATOM   1298 C C   . GLY A 1 178 ? 5.683   53.733 44.098 1.00 11.95 ? 172 GLY A C   1 
ATOM   1299 O O   . GLY A 1 178 ? 6.038   54.608 43.295 1.00 8.42  ? 172 GLY A O   1 
ATOM   1300 N N   . ALA A 1 179 ? 6.142   53.655 45.354 1.00 2.00  ? 173 ALA A N   1 
ATOM   1301 C CA  . ALA A 1 179 ? 7.382   54.328 45.768 1.00 4.32  ? 173 ALA A CA  1 
ATOM   1302 C C   . ALA A 1 179 ? 8.172   53.563 46.834 1.00 13.27 ? 173 ALA A C   1 
ATOM   1303 O O   . ALA A 1 179 ? 7.654   52.660 47.482 1.00 2.30  ? 173 ALA A O   1 
ATOM   1304 C CB  . ALA A 1 179 ? 7.083   55.727 46.262 1.00 2.00  ? 173 ALA A CB  1 
ATOM   1305 N N   . PHE A 1 180 ? 9.447   53.902 46.992 1.00 5.44  ? 174 PHE A N   1 
ATOM   1306 C CA  . PHE A 1 180 ? 10.260  53.249 48.015 1.00 2.42  ? 174 PHE A CA  1 
ATOM   1307 C C   . PHE A 1 180 ? 11.477  54.033 48.462 1.00 2.14  ? 174 PHE A C   1 
ATOM   1308 O O   . PHE A 1 180 ? 12.021  54.829 47.729 1.00 2.00  ? 174 PHE A O   1 
ATOM   1309 C CB  . PHE A 1 180 ? 10.687  51.862 47.551 1.00 2.00  ? 174 PHE A CB  1 
ATOM   1310 C CG  . PHE A 1 180 ? 11.750  51.870 46.484 1.00 2.71  ? 174 PHE A CG  1 
ATOM   1311 C CD1 . PHE A 1 180 ? 11.538  52.540 45.287 1.00 28.90 ? 174 PHE A CD1 1 
ATOM   1312 C CD2 . PHE A 1 180 ? 12.949  51.213 46.672 1.00 2.00  ? 174 PHE A CD2 1 
ATOM   1313 C CE1 . PHE A 1 180 ? 12.497  52.553 44.302 1.00 17.58 ? 174 PHE A CE1 1 
ATOM   1314 C CE2 . PHE A 1 180 ? 13.920  51.226 45.688 1.00 8.30  ? 174 PHE A CE2 1 
ATOM   1315 C CZ  . PHE A 1 180 ? 13.684  51.900 44.498 1.00 2.00  ? 174 PHE A CZ  1 
ATOM   1316 N N   . THR A 1 181 ? 11.874  53.852 49.706 1.00 2.00  ? 175 THR A N   1 
ATOM   1317 C CA  . THR A 1 181 ? 13.116  54.424 50.182 1.00 10.78 ? 175 THR A CA  1 
ATOM   1318 C C   . THR A 1 181 ? 14.276  53.943 49.335 1.00 16.66 ? 175 THR A C   1 
ATOM   1319 O O   . THR A 1 181 ? 14.426  52.758 49.078 1.00 4.20  ? 175 THR A O   1 
ATOM   1320 C CB  . THR A 1 181 ? 13.376  54.011 51.619 1.00 2.00  ? 175 THR A CB  1 
ATOM   1321 O OG1 . THR A 1 181 ? 12.188  54.242 52.388 1.00 23.91 ? 175 THR A OG1 1 
ATOM   1322 C CG2 . THR A 1 181 ? 14.520  54.785 52.194 1.00 2.00  ? 175 THR A CG2 1 
ATOM   1323 N N   . VAL A 1 182 ? 15.202  54.840 49.058 1.00 2.00  ? 176 VAL A N   1 
ATOM   1324 C CA  . VAL A 1 182 ? 16.330  54.486 48.198 1.00 33.31 ? 176 VAL A CA  1 
ATOM   1325 C C   . VAL A 1 182 ? 17.645  54.585 48.958 1.00 20.83 ? 176 VAL A C   1 
ATOM   1326 O O   . VAL A 1 182 ? 17.999  55.626 49.506 1.00 13.67 ? 176 VAL A O   1 
ATOM   1327 C CB  . VAL A 1 182 ? 16.377  55.362 46.891 1.00 2.00  ? 176 VAL A CB  1 
ATOM   1328 C CG1 . VAL A 1 182 ? 17.785  55.453 46.325 1.00 17.93 ? 176 VAL A CG1 1 
ATOM   1329 C CG2 . VAL A 1 182 ? 15.489  54.725 45.822 1.00 12.01 ? 176 VAL A CG2 1 
ATOM   1330 N N   . PHE A 1 183 ? 18.330  53.461 49.080 1.00 15.87 ? 177 PHE A N   1 
ATOM   1331 C CA  . PHE A 1 183 ? 19.645  53.470 49.664 1.00 3.30  ? 177 PHE A CA  1 
ATOM   1332 C C   . PHE A 1 183 ? 20.753  53.384 48.620 1.00 47.04 ? 177 PHE A C   1 
ATOM   1333 O O   . PHE A 1 183 ? 20.590  52.740 47.572 1.00 23.79 ? 177 PHE A O   1 
ATOM   1334 C CB  . PHE A 1 183 ? 19.750  52.333 50.656 1.00 9.07  ? 177 PHE A CB  1 
ATOM   1335 C CG  . PHE A 1 183 ? 19.021  52.600 51.919 1.00 30.88 ? 177 PHE A CG  1 
ATOM   1336 C CD1 . PHE A 1 183 ? 17.655  52.421 52.006 1.00 64.70 ? 177 PHE A CD1 1 
ATOM   1337 C CD2 . PHE A 1 183 ? 19.710  53.036 53.038 1.00 5.12  ? 177 PHE A CD2 1 
ATOM   1338 C CE1 . PHE A 1 183 ? 16.991  52.668 53.178 1.00 12.98 ? 177 PHE A CE1 1 
ATOM   1339 C CE2 . PHE A 1 183 ? 19.056  53.285 54.212 1.00 74.70 ? 177 PHE A CE2 1 
ATOM   1340 C CZ  . PHE A 1 183 ? 17.696  53.099 54.288 1.00 31.70 ? 177 PHE A CZ  1 
ATOM   1341 N N   . SER A 1 184 ? 21.857  54.086 48.884 1.00 8.35  ? 178 SER A N   1 
ATOM   1342 C CA  . SER A 1 184 ? 23.097  53.934 48.108 1.00 32.35 ? 178 SER A CA  1 
ATOM   1343 C C   . SER A 1 184 ? 23.264  52.599 47.392 1.00 2.00  ? 178 SER A C   1 
ATOM   1344 O O   . SER A 1 184 ? 23.583  52.582 46.204 1.00 18.22 ? 178 SER A O   1 
ATOM   1345 C CB  . SER A 1 184 ? 24.327  54.141 48.995 1.00 8.97  ? 178 SER A CB  1 
ATOM   1346 O OG  . SER A 1 184 ? 24.267  55.396 49.640 1.00 90.02 ? 178 SER A OG  1 
ATOM   1347 N N   . ASP A 1 185 ? 23.145  51.478 48.115 1.00 17.28 ? 179 ASP A N   1 
ATOM   1348 C CA  . ASP A 1 185 ? 23.420  50.158 47.509 1.00 2.00  ? 179 ASP A CA  1 
ATOM   1349 C C   . ASP A 1 185 ? 22.471  49.808 46.357 1.00 25.44 ? 179 ASP A C   1 
ATOM   1350 O O   . ASP A 1 185 ? 22.811  49.020 45.468 1.00 19.50 ? 179 ASP A O   1 
ATOM   1351 C CB  . ASP A 1 185 ? 23.411  49.035 48.581 1.00 10.97 ? 179 ASP A CB  1 
ATOM   1352 C CG  . ASP A 1 185 ? 22.019  48.718 49.120 1.00 25.83 ? 179 ASP A CG  1 
ATOM   1353 O OD1 . ASP A 1 185 ? 21.149  49.614 49.129 1.00 13.05 ? 179 ASP A OD1 1 
ATOM   1354 O OD2 . ASP A 1 185 ? 21.791  47.575 49.562 1.00 6.43  ? 179 ASP A OD2 1 
ATOM   1355 N N   . PHE A 1 186 ? 21.320  50.473 46.320 1.00 11.37 ? 180 PHE A N   1 
ATOM   1356 C CA  . PHE A 1 186 ? 20.446  50.414 45.162 1.00 23.99 ? 180 PHE A CA  1 
ATOM   1357 C C   . PHE A 1 186 ? 21.120  50.911 43.878 1.00 14.81 ? 180 PHE A C   1 
ATOM   1358 O O   . PHE A 1 186 ? 20.961  50.308 42.806 1.00 29.19 ? 180 PHE A O   1 
ATOM   1359 C CB  . PHE A 1 186 ? 19.175  51.229 45.414 1.00 15.13 ? 180 PHE A CB  1 
ATOM   1360 C CG  . PHE A 1 186 ? 18.256  51.292 44.229 1.00 26.50 ? 180 PHE A CG  1 
ATOM   1361 C CD1 . PHE A 1 186 ? 17.536  50.177 43.852 1.00 3.21  ? 180 PHE A CD1 1 
ATOM   1362 C CD2 . PHE A 1 186 ? 18.040  52.488 43.553 1.00 6.20  ? 180 PHE A CD2 1 
ATOM   1363 C CE1 . PHE A 1 186 ? 16.591  50.249 42.829 1.00 18.49 ? 180 PHE A CE1 1 
ATOM   1364 C CE2 . PHE A 1 186 ? 17.091  52.573 42.536 1.00 2.00  ? 180 PHE A CE2 1 
ATOM   1365 C CZ  . PHE A 1 186 ? 16.365  51.455 42.181 1.00 27.92 ? 180 PHE A CZ  1 
ATOM   1366 N N   . LEU A 1 187 ? 21.860  52.011 43.976 1.00 22.18 ? 181 LEU A N   1 
ATOM   1367 C CA  . LEU A 1 187 ? 22.211  52.795 42.792 1.00 18.36 ? 181 LEU A CA  1 
ATOM   1368 C C   . LEU A 1 187 ? 22.951  52.010 41.727 1.00 15.07 ? 181 LEU A C   1 
ATOM   1369 O O   . LEU A 1 187 ? 22.843  52.304 40.544 1.00 25.31 ? 181 LEU A O   1 
ATOM   1370 C CB  . LEU A 1 187 ? 23.040  54.011 43.186 1.00 25.13 ? 181 LEU A CB  1 
ATOM   1371 C CG  . LEU A 1 187 ? 22.301  55.058 44.014 1.00 36.21 ? 181 LEU A CG  1 
ATOM   1372 C CD1 . LEU A 1 187 ? 23.189  56.277 44.184 1.00 19.53 ? 181 LEU A CD1 1 
ATOM   1373 C CD2 . LEU A 1 187 ? 20.993  55.437 43.345 1.00 22.63 ? 181 LEU A CD2 1 
ATOM   1374 N N   . THR A 1 188 ? 23.647  50.964 42.146 1.00 42.99 ? 182 THR A N   1 
ATOM   1375 C CA  . THR A 1 188 ? 24.442  50.153 41.227 1.00 2.00  ? 182 THR A CA  1 
ATOM   1376 C C   . THR A 1 188 ? 23.866  48.756 41.049 1.00 93.85 ? 182 THR A C   1 
ATOM   1377 O O   . THR A 1 188 ? 24.603  47.793 40.820 1.00 37.38 ? 182 THR A O   1 
ATOM   1378 C CB  . THR A 1 188 ? 25.872  50.019 41.732 1.00 91.54 ? 182 THR A CB  1 
ATOM   1379 O OG1 . THR A 1 188 ? 25.841  49.394 43.021 1.00 18.40 ? 182 THR A OG1 1 
ATOM   1380 C CG2 . THR A 1 188 ? 26.556  51.409 41.811 1.00 2.00  ? 182 THR A CG2 1 
ATOM   1381 N N   . TYR A 1 189 ? 22.549  48.643 41.176 1.00 8.57  ? 183 TYR A N   1 
ATOM   1382 C CA  . TYR A 1 189 ? 21.852  47.393 40.869 1.00 50.19 ? 183 TYR A CA  1 
ATOM   1383 C C   . TYR A 1 189 ? 22.104  46.936 39.431 1.00 11.27 ? 183 TYR A C   1 
ATOM   1384 O O   . TYR A 1 189 ? 22.103  47.749 38.517 1.00 4.75  ? 183 TYR A O   1 
ATOM   1385 C CB  . TYR A 1 189 ? 20.353  47.571 41.059 1.00 2.00  ? 183 TYR A CB  1 
ATOM   1386 C CG  . TYR A 1 189 ? 19.561  46.416 40.500 1.00 15.72 ? 183 TYR A CG  1 
ATOM   1387 C CD1 . TYR A 1 189 ? 19.269  45.310 41.281 1.00 17.57 ? 183 TYR A CD1 1 
ATOM   1388 C CD2 . TYR A 1 189 ? 19.047  46.459 39.200 1.00 8.95  ? 183 TYR A CD2 1 
ATOM   1389 C CE1 . TYR A 1 189 ? 18.450  44.299 40.795 1.00 15.88 ? 183 TYR A CE1 1 
ATOM   1390 C CE2 . TYR A 1 189 ? 18.261  45.440 38.721 1.00 2.39  ? 183 TYR A CE2 1 
ATOM   1391 C CZ  . TYR A 1 189 ? 17.948  44.375 39.519 1.00 2.00  ? 183 TYR A CZ  1 
ATOM   1392 O OH  . TYR A 1 189 ? 17.097  43.399 39.059 1.00 10.78 ? 183 TYR A OH  1 
ATOM   1393 N N   . LYS A 1 190 ? 22.160  45.628 39.208 1.00 10.16 ? 184 LYS A N   1 
ATOM   1394 C CA  . LYS A 1 190 ? 22.373  45.132 37.849 1.00 7.38  ? 184 LYS A CA  1 
ATOM   1395 C C   . LYS A 1 190 ? 21.342  44.080 37.393 1.00 14.73 ? 184 LYS A C   1 
ATOM   1396 O O   . LYS A 1 190 ? 20.915  44.104 36.241 1.00 12.66 ? 184 LYS A O   1 
ATOM   1397 C CB  . LYS A 1 190 ? 23.795  44.577 37.707 1.00 2.00  ? 184 LYS A CB  1 
ATOM   1398 C CG  . LYS A 1 190 ? 24.888  45.603 37.916 1.00 43.21 ? 184 LYS A CG  1 
ATOM   1399 C CD  . LYS A 1 190 ? 24.902  46.636 36.797 1.00 50.73 ? 184 LYS A CD  1 
ATOM   1400 C CE  . LYS A 1 190 ? 25.876  47.778 37.088 1.00 90.30 ? 184 LYS A CE  1 
ATOM   1401 N NZ  . LYS A 1 190 ? 27.233  47.305 37.493 1.00 44.74 ? 184 LYS A NZ  1 
ATOM   1402 N N   . SER A 1 191 ? 20.960  43.166 38.296 1.00 2.00  ? 185 SER A N   1 
ATOM   1403 C CA  . SER A 1 191 ? 20.068  42.064 37.962 1.00 16.37 ? 185 SER A CA  1 
ATOM   1404 C C   . SER A 1 191 ? 19.817  41.193 39.186 1.00 7.26  ? 185 SER A C   1 
ATOM   1405 O O   . SER A 1 191 ? 20.420  41.404 40.244 1.00 8.49  ? 185 SER A O   1 
ATOM   1406 C CB  . SER A 1 191 ? 20.638  41.208 36.819 1.00 54.21 ? 185 SER A CB  1 
ATOM   1407 O OG  . SER A 1 191 ? 21.927  40.710 37.124 1.00 57.87 ? 185 SER A OG  1 
ATOM   1408 N N   . GLY A 1 192 ? 18.843  40.297 39.071 1.00 46.41 ? 186 GLY A N   1 
ATOM   1409 C CA  . GLY A 1 192 ? 18.408  39.511 40.215 1.00 2.00  ? 186 GLY A CA  1 
ATOM   1410 C C   . GLY A 1 192 ? 17.389  40.267 41.035 1.00 19.88 ? 186 GLY A C   1 
ATOM   1411 O O   . GLY A 1 192 ? 16.831  41.267 40.590 1.00 15.91 ? 186 GLY A O   1 
ATOM   1412 N N   . VAL A 1 193 ? 17.244  39.874 42.288 1.00 28.37 ? 187 VAL A N   1 
ATOM   1413 C CA  . VAL A 1 193 ? 16.267  40.501 43.155 1.00 13.16 ? 187 VAL A CA  1 
ATOM   1414 C C   . VAL A 1 193 ? 16.954  41.401 44.206 1.00 26.56 ? 187 VAL A C   1 
ATOM   1415 O O   . VAL A 1 193 ? 17.690  40.909 45.065 1.00 51.08 ? 187 VAL A O   1 
ATOM   1416 C CB  . VAL A 1 193 ? 15.445  39.434 43.843 1.00 3.83  ? 187 VAL A CB  1 
ATOM   1417 C CG1 . VAL A 1 193 ? 14.474  40.083 44.856 1.00 17.72 ? 187 VAL A CG1 1 
ATOM   1418 C CG2 . VAL A 1 193 ? 14.694  38.606 42.795 1.00 2.00  ? 187 VAL A CG2 1 
ATOM   1419 N N   . TYR A 1 194 ? 16.720  42.713 44.109 1.00 2.00  ? 188 TYR A N   1 
ATOM   1420 C CA  . TYR A 1 194 ? 17.173  43.681 45.123 1.00 31.04 ? 188 TYR A CA  1 
ATOM   1421 C C   . TYR A 1 194 ? 16.533  43.517 46.508 1.00 53.95 ? 188 TYR A C   1 
ATOM   1422 O O   . TYR A 1 194 ? 15.320  43.676 46.702 1.00 14.51 ? 188 TYR A O   1 
ATOM   1423 C CB  . TYR A 1 194 ? 16.971  45.136 44.653 1.00 13.23 ? 188 TYR A CB  1 
ATOM   1424 C CG  . TYR A 1 194 ? 17.380  46.182 45.686 1.00 16.40 ? 188 TYR A CG  1 
ATOM   1425 C CD1 . TYR A 1 194 ? 18.718  46.555 45.834 1.00 2.85  ? 188 TYR A CD1 1 
ATOM   1426 C CD2 . TYR A 1 194 ? 16.444  46.769 46.541 1.00 17.18 ? 188 TYR A CD2 1 
ATOM   1427 C CE1 . TYR A 1 194 ? 19.127  47.467 46.795 1.00 34.39 ? 188 TYR A CE1 1 
ATOM   1428 C CE2 . TYR A 1 194 ? 16.852  47.692 47.512 1.00 4.39  ? 188 TYR A CE2 1 
ATOM   1429 C CZ  . TYR A 1 194 ? 18.204  48.032 47.637 1.00 28.66 ? 188 TYR A CZ  1 
ATOM   1430 O OH  . TYR A 1 194 ? 18.661  48.917 48.615 1.00 2.00  ? 188 TYR A OH  1 
ATOM   1431 N N   . LYS A 1 195 ? 17.367  43.099 47.444 1.00 6.69  ? 189 LYS A N   1 
ATOM   1432 C CA  . LYS A 1 195 ? 17.176  43.363 48.867 1.00 28.48 ? 189 LYS A CA  1 
ATOM   1433 C C   . LYS A 1 195 ? 18.223  44.380 49.338 1.00 2.11  ? 189 LYS A C   1 
ATOM   1434 O O   . LYS A 1 195 ? 19.327  44.411 48.822 1.00 39.65 ? 189 LYS A O   1 
ATOM   1435 C CB  . LYS A 1 195 ? 17.332  42.064 49.650 1.00 10.61 ? 189 LYS A CB  1 
ATOM   1436 C CG  . LYS A 1 195 ? 17.079  42.190 51.137 1.00 17.62 ? 189 LYS A CG  1 
ATOM   1437 C CD  . LYS A 1 195 ? 16.852  40.821 51.777 1.00 73.92 ? 189 LYS A CD  1 
ATOM   1438 C CE  . LYS A 1 195 ? 16.692  40.935 53.289 1.00 58.10 ? 189 LYS A CE  1 
ATOM   1439 N NZ  . LYS A 1 195 ? 15.779  39.905 53.863 1.00 88.51 ? 189 LYS A NZ  1 
ATOM   1440 N N   . HIS A 1 196 ? 17.921  45.116 50.401 1.00 2.00  ? 190 HIS A N   1 
ATOM   1441 C CA  . HIS A 1 196 ? 18.864  46.119 50.918 1.00 38.80 ? 190 HIS A CA  1 
ATOM   1442 C C   . HIS A 1 196 ? 19.833  45.524 51.954 1.00 8.01  ? 190 HIS A C   1 
ATOM   1443 O O   . HIS A 1 196 ? 19.438  44.752 52.823 1.00 35.57 ? 190 HIS A O   1 
ATOM   1444 C CB  . HIS A 1 196 ? 18.110  47.325 51.525 1.00 2.00  ? 190 HIS A CB  1 
ATOM   1445 C CG  . HIS A 1 196 ? 18.972  48.232 52.355 1.00 37.95 ? 190 HIS A CG  1 
ATOM   1446 N ND1 . HIS A 1 196 ? 19.800  49.186 51.807 1.00 19.27 ? 190 HIS A ND1 1 
ATOM   1447 C CD2 . HIS A 1 196 ? 19.075  48.381 53.699 1.00 27.05 ? 190 HIS A CD2 1 
ATOM   1448 C CE1 . HIS A 1 196 ? 20.363  49.891 52.769 1.00 39.19 ? 190 HIS A CE1 1 
ATOM   1449 N NE2 . HIS A 1 196 ? 19.936  49.426 53.927 1.00 13.48 ? 190 HIS A NE2 1 
ATOM   1450 N N   . GLU A 1 197 ? 21.089  45.939 51.888 1.00 39.82 ? 191 GLU A N   1 
ATOM   1451 C CA  . GLU A 1 197 ? 22.091  45.493 52.847 1.00 35.07 ? 191 GLU A CA  1 
ATOM   1452 C C   . GLU A 1 197 ? 22.925  46.632 53.394 1.00 38.08 ? 191 GLU A C   1 
ATOM   1453 O O   . GLU A 1 197 ? 23.116  46.745 54.598 1.00 64.52 ? 191 GLU A O   1 
ATOM   1454 C CB  . GLU A 1 197 ? 23.015  44.464 52.200 1.00 24.01 ? 191 GLU A CB  1 
ATOM   1455 C CG  . GLU A 1 197 ? 22.606  43.042 52.465 1.00 85.95 ? 191 GLU A CG  1 
ATOM   1456 C CD  . GLU A 1 197 ? 21.656  42.490 51.423 1.00 68.37 ? 191 GLU A CD  1 
ATOM   1457 O OE1 . GLU A 1 197 ? 21.344  43.186 50.422 1.00 90.55 ? 191 GLU A OE1 1 
ATOM   1458 O OE2 . GLU A 1 197 ? 21.268  41.312 51.588 1.00 37.00 ? 191 GLU A OE2 1 
ATOM   1459 N N   . ALA A 1 198 ? 23.378  47.505 52.505 1.00 40.60 ? 192 ALA A N   1 
ATOM   1460 C CA  . ALA A 1 198 ? 24.322  48.548 52.883 1.00 22.50 ? 192 ALA A CA  1 
ATOM   1461 C C   . ALA A 1 198 ? 23.929  49.917 52.349 1.00 48.34 ? 192 ALA A C   1 
ATOM   1462 O O   . ALA A 1 198 ? 22.903  50.060 51.683 1.00 29.88 ? 192 ALA A O   1 
ATOM   1463 C CB  . ALA A 1 198 ? 25.722  48.181 52.395 1.00 79.38 ? 192 ALA A CB  1 
ATOM   1464 N N   . GLY A 1 199 ? 24.762  50.915 52.631 1.00 18.04 ? 193 GLY A N   1 
ATOM   1465 C CA  . GLY A 1 199 ? 24.546  52.239 52.080 1.00 53.88 ? 193 GLY A CA  1 
ATOM   1466 C C   . GLY A 1 199 ? 23.649  53.143 52.905 1.00 14.73 ? 193 GLY A C   1 
ATOM   1467 O O   . GLY A 1 199 ? 22.788  52.667 53.652 1.00 27.44 ? 193 GLY A O   1 
ATOM   1468 N N   . ASP A 1 200 ? 23.766  54.442 52.627 1.00 26.02 ? 194 ASP A N   1 
ATOM   1469 C CA  . ASP A 1 200 ? 23.003  55.510 53.271 1.00 9.60  ? 194 ASP A CA  1 
ATOM   1470 C C   . ASP A 1 200 ? 21.597  55.639 52.665 1.00 32.72 ? 194 ASP A C   1 
ATOM   1471 O O   . ASP A 1 200 ? 21.359  55.168 51.548 1.00 30.61 ? 194 ASP A O   1 
ATOM   1472 C CB  . ASP A 1 200 ? 23.726  56.856 53.073 1.00 44.71 ? 194 ASP A CB  1 
ATOM   1473 C CG  . ASP A 1 200 ? 25.050  56.944 53.816 1.00 16.00 ? 194 ASP A CG  1 
ATOM   1474 O OD1 . ASP A 1 200 ? 26.051  56.361 53.349 1.00 46.53 ? 194 ASP A OD1 1 
ATOM   1475 O OD2 . ASP A 1 200 ? 25.099  57.649 54.842 1.00 98.53 ? 194 ASP A OD2 1 
ATOM   1476 N N   . VAL A 1 201 ? 20.739  56.427 53.319 1.00 35.12 ? 195 VAL A N   1 
ATOM   1477 C CA  . VAL A 1 201 ? 19.456  56.854 52.731 1.00 16.42 ? 195 VAL A CA  1 
ATOM   1478 C C   . VAL A 1 201 ? 19.641  57.944 51.674 1.00 25.52 ? 195 VAL A C   1 
ATOM   1479 O O   . VAL A 1 201 ? 20.490  58.823 51.811 1.00 66.43 ? 195 VAL A O   1 
ATOM   1480 C CB  . VAL A 1 201 ? 18.458  57.408 53.785 1.00 15.75 ? 195 VAL A CB  1 
ATOM   1481 C CG1 . VAL A 1 201 ? 17.025  57.272 53.269 1.00 24.94 ? 195 VAL A CG1 1 
ATOM   1482 C CG2 . VAL A 1 201 ? 18.601  56.672 55.095 1.00 44.27 ? 195 VAL A CG2 1 
ATOM   1483 N N   . MET A 1 202 ? 18.840  57.858 50.615 1.00 42.21 ? 196 MET A N   1 
ATOM   1484 C CA  . MET A 1 202 ? 18.774  58.883 49.570 1.00 2.00  ? 196 MET A CA  1 
ATOM   1485 C C   . MET A 1 202 ? 17.348  59.419 49.463 1.00 50.27 ? 196 MET A C   1 
ATOM   1486 O O   . MET A 1 202 ? 17.130  60.536 49.029 1.00 21.09 ? 196 MET A O   1 
ATOM   1487 C CB  . MET A 1 202 ? 19.180  58.299 48.208 1.00 15.80 ? 196 MET A CB  1 
ATOM   1488 C CG  . MET A 1 202 ? 20.076  57.076 48.287 1.00 54.78 ? 196 MET A CG  1 
ATOM   1489 S SD  . MET A 1 202 ? 21.615  57.252 47.434 1.00 28.54 ? 196 MET A SD  1 
ATOM   1490 C CE  . MET A 1 202 ? 22.512  58.309 48.559 1.00 63.77 ? 196 MET A CE  1 
ATOM   1491 N N   . GLY A 1 203 ? 16.383  58.528 49.639 1.00 6.30  ? 197 GLY A N   1 
ATOM   1492 C CA  . GLY A 1 203 ? 15.007  58.946 49.771 1.00 12.63 ? 197 GLY A CA  1 
ATOM   1493 C C   . GLY A 1 203 ? 14.033  58.049 49.040 1.00 2.00  ? 197 GLY A C   1 
ATOM   1494 O O   . GLY A 1 203 ? 14.422  57.082 48.398 1.00 46.91 ? 197 GLY A O   1 
ATOM   1495 N N   . GLY A 1 204 ? 12.748  58.334 49.205 1.00 11.65 ? 198 GLY A N   1 
ATOM   1496 C CA  . GLY A 1 204 ? 11.745  57.784 48.309 1.00 8.71  ? 198 GLY A CA  1 
ATOM   1497 C C   . GLY A 1 204 ? 12.045  58.117 46.861 1.00 11.15 ? 198 GLY A C   1 
ATOM   1498 O O   . GLY A 1 204 ? 12.865  58.985 46.534 1.00 40.04 ? 198 GLY A O   1 
ATOM   1499 N N   . HIS A 1 205 ? 11.419  57.352 45.983 1.00 16.34 ? 199 HIS A N   1 
ATOM   1500 C CA  . HIS A 1 205 ? 11.580  57.505 44.549 1.00 2.00  ? 199 HIS A CA  1 
ATOM   1501 C C   . HIS A 1 205 ? 10.492  56.613 43.979 1.00 65.86 ? 199 HIS A C   1 
ATOM   1502 O O   . HIS A 1 205 ? 10.291  55.503 44.478 1.00 2.71  ? 199 HIS A O   1 
ATOM   1503 C CB  . HIS A 1 205 ? 12.972  57.002 44.144 1.00 29.02 ? 199 HIS A CB  1 
ATOM   1504 C CG  . HIS A 1 205 ? 13.063  56.479 42.739 1.00 33.63 ? 199 HIS A CG  1 
ATOM   1505 N ND1 . HIS A 1 205 ? 13.138  57.312 41.634 1.00 30.64 ? 199 HIS A ND1 1 
ATOM   1506 C CD2 . HIS A 1 205 ? 13.307  55.227 42.279 1.00 92.80 ? 199 HIS A CD2 1 
ATOM   1507 C CE1 . HIS A 1 205 ? 13.449  56.596 40.565 1.00 10.77 ? 199 HIS A CE1 1 
ATOM   1508 N NE2 . HIS A 1 205 ? 13.560  55.328 40.930 1.00 15.61 ? 199 HIS A NE2 1 
ATOM   1509 N N   . ALA A 1 206 ? 9.697   57.191 43.078 1.00 2.00  ? 200 ALA A N   1 
ATOM   1510 C CA  . ALA A 1 206 ? 8.506   56.580 42.528 1.00 2.00  ? 200 ALA A CA  1 
ATOM   1511 C C   . ALA A 1 206 ? 8.838   55.735 41.345 1.00 13.14 ? 200 ALA A C   1 
ATOM   1512 O O   . ALA A 1 206 ? 9.667   56.124 40.530 1.00 2.00  ? 200 ALA A O   1 
ATOM   1513 C CB  . ALA A 1 206 ? 7.493   57.661 42.105 1.00 2.00  ? 200 ALA A CB  1 
ATOM   1514 N N   . ILE A 1 207 ? 8.037   54.701 41.141 1.00 32.78 ? 201 ILE A N   1 
ATOM   1515 C CA  . ILE A 1 207 ? 8.280   53.731 40.083 1.00 16.49 ? 201 ILE A CA  1 
ATOM   1516 C C   . ILE A 1 207 ? 6.941   53.143 39.613 1.00 3.76  ? 201 ILE A C   1 
ATOM   1517 O O   . ILE A 1 207 ? 5.883   53.583 40.074 1.00 15.88 ? 201 ILE A O   1 
ATOM   1518 C CB  . ILE A 1 207 ? 9.239   52.611 40.575 1.00 2.00  ? 201 ILE A CB  1 
ATOM   1519 C CG1 . ILE A 1 207 ? 8.947   52.262 42.038 1.00 14.04 ? 201 ILE A CG1 1 
ATOM   1520 C CG2 . ILE A 1 207 ? 10.690  53.109 40.535 1.00 8.84  ? 201 ILE A CG2 1 
ATOM   1521 C CD1 . ILE A 1 207 ? 7.736   51.385 42.222 1.00 2.00  ? 201 ILE A CD1 1 
ATOM   1522 N N   . ARG A 1 208 ? 7.000   52.296 38.578 1.00 2.00  ? 202 ARG A N   1 
ATOM   1523 C CA  . ARG A 1 208 ? 5.826   51.666 37.979 1.00 6.04  ? 202 ARG A CA  1 
ATOM   1524 C C   . ARG A 1 208 ? 5.915   50.143 38.170 1.00 14.18 ? 202 ARG A C   1 
ATOM   1525 O O   . ARG A 1 208 ? 6.905   49.518 37.796 1.00 5.41  ? 202 ARG A O   1 
ATOM   1526 C CB  . ARG A 1 208 ? 5.740   52.050 36.486 1.00 2.00  ? 202 ARG A CB  1 
ATOM   1527 C CG  . ARG A 1 208 ? 4.951   51.080 35.640 1.00 2.00  ? 202 ARG A CG  1 
ATOM   1528 C CD  . ARG A 1 208 ? 4.601   51.651 34.268 1.00 48.69 ? 202 ARG A CD  1 
ATOM   1529 N NE  . ARG A 1 208 ? 5.677   51.426 33.312 1.00 3.41  ? 202 ARG A NE  1 
ATOM   1530 C CZ  . ARG A 1 208 ? 5.929   50.262 32.737 1.00 2.05  ? 202 ARG A CZ  1 
ATOM   1531 N NH1 . ARG A 1 208 ? 4.943   49.384 32.532 1.00 3.81  ? 202 ARG A NH1 1 
ATOM   1532 N NH2 . ARG A 1 208 ? 7.122   50.057 32.199 1.00 8.18  ? 202 ARG A NH2 1 
ATOM   1533 N N   . ILE A 1 209 ? 4.977   49.559 38.904 1.00 2.00  ? 203 ILE A N   1 
ATOM   1534 C CA  . ILE A 1 209 ? 5.018   48.109 39.082 1.00 4.96  ? 203 ILE A CA  1 
ATOM   1535 C C   . ILE A 1 209 ? 4.103   47.381 38.108 1.00 24.15 ? 203 ILE A C   1 
ATOM   1536 O O   . ILE A 1 209 ? 2.928   47.756 37.920 1.00 2.57  ? 203 ILE A O   1 
ATOM   1537 C CB  . ILE A 1 209 ? 4.674   47.663 40.514 1.00 2.00  ? 203 ILE A CB  1 
ATOM   1538 C CG1 . ILE A 1 209 ? 5.383   48.550 41.551 1.00 25.47 ? 203 ILE A CG1 1 
ATOM   1539 C CG2 . ILE A 1 209 ? 5.098   46.205 40.699 1.00 2.00  ? 203 ILE A CG2 1 
ATOM   1540 C CD1 . ILE A 1 209 ? 4.952   48.294 43.037 1.00 2.00  ? 203 ILE A CD1 1 
ATOM   1541 N N   . LEU A 1 210 ? 4.661   46.364 37.456 1.00 2.00  ? 204 LEU A N   1 
ATOM   1542 C CA  . LEU A 1 210 ? 4.044   45.808 36.244 1.00 6.97  ? 204 LEU A CA  1 
ATOM   1543 C C   . LEU A 1 210 ? 3.977   44.282 36.251 1.00 15.60 ? 204 LEU A C   1 
ATOM   1544 O O   . LEU A 1 210 ? 3.563   43.668 35.273 1.00 19.84 ? 204 LEU A O   1 
ATOM   1545 C CB  . LEU A 1 210 ? 4.798   46.305 34.983 1.00 3.37  ? 204 LEU A CB  1 
ATOM   1546 C CG  . LEU A 1 210 ? 6.301   45.989 34.800 1.00 31.33 ? 204 LEU A CG  1 
ATOM   1547 C CD1 . LEU A 1 210 ? 6.573   45.511 33.389 1.00 2.00  ? 204 LEU A CD1 1 
ATOM   1548 C CD2 . LEU A 1 210 ? 7.145   47.208 35.066 1.00 2.00  ? 204 LEU A CD2 1 
ATOM   1549 N N   . GLY A 1 211 ? 4.360   43.683 37.377 1.00 18.37 ? 205 GLY A N   1 
ATOM   1550 C CA  . GLY A 1 211 ? 4.373   42.242 37.495 1.00 6.34  ? 205 GLY A CA  1 
ATOM   1551 C C   . GLY A 1 211 ? 5.014   41.742 38.774 1.00 2.00  ? 205 GLY A C   1 
ATOM   1552 O O   . GLY A 1 211 ? 5.527   42.523 39.542 1.00 18.43 ? 205 GLY A O   1 
ATOM   1553 N N   . TRP A 1 212 ? 5.003   40.431 38.968 1.00 4.49  ? 206 TRP A N   1 
ATOM   1554 C CA  . TRP A 1 212 ? 5.609   39.785 40.134 1.00 2.13  ? 206 TRP A CA  1 
ATOM   1555 C C   . TRP A 1 212 ? 6.240   38.461 39.704 1.00 2.00  ? 206 TRP A C   1 
ATOM   1556 O O   . TRP A 1 212 ? 6.079   38.047 38.581 1.00 3.08  ? 206 TRP A O   1 
ATOM   1557 C CB  . TRP A 1 212 ? 4.547   39.560 41.230 1.00 2.00  ? 206 TRP A CB  1 
ATOM   1558 C CG  . TRP A 1 212 ? 3.366   38.714 40.824 1.00 2.72  ? 206 TRP A CG  1 
ATOM   1559 C CD1 . TRP A 1 212 ? 3.257   37.347 40.935 1.00 15.77 ? 206 TRP A CD1 1 
ATOM   1560 C CD2 . TRP A 1 212 ? 2.084   39.175 40.382 1.00 2.00  ? 206 TRP A CD2 1 
ATOM   1561 N NE1 . TRP A 1 212 ? 1.990   36.937 40.601 1.00 2.00  ? 206 TRP A NE1 1 
ATOM   1562 C CE2 . TRP A 1 212 ? 1.250   38.033 40.244 1.00 8.43  ? 206 TRP A CE2 1 
ATOM   1563 C CE3 . TRP A 1 212 ? 1.554   40.438 40.094 1.00 2.00  ? 206 TRP A CE3 1 
ATOM   1564 C CZ2 . TRP A 1 212 ? -0.071  38.120 39.819 1.00 2.00  ? 206 TRP A CZ2 1 
ATOM   1565 C CZ3 . TRP A 1 212 ? 0.247   40.518 39.667 1.00 24.04 ? 206 TRP A CZ3 1 
ATOM   1566 C CH2 . TRP A 1 212 ? -0.549  39.367 39.528 1.00 8.23  ? 206 TRP A CH2 1 
ATOM   1567 N N   . GLY A 1 213 ? 6.907   37.765 40.611 1.00 31.14 ? 207 GLY A N   1 
ATOM   1568 C CA  . GLY A 1 213 ? 7.484   36.474 40.255 1.00 2.00  ? 207 GLY A CA  1 
ATOM   1569 C C   . GLY A 1 213 ? 8.375   35.872 41.331 1.00 9.35  ? 207 GLY A C   1 
ATOM   1570 O O   . GLY A 1 213 ? 8.551   36.429 42.416 1.00 12.59 ? 207 GLY A O   1 
ATOM   1571 N N   . ILE A 1 214 ? 8.921   34.702 41.049 1.00 30.80 ? 208 ILE A N   1 
ATOM   1572 C CA  . ILE A 1 214 ? 9.862   34.100 41.970 1.00 6.26  ? 208 ILE A CA  1 
ATOM   1573 C C   . ILE A 1 214 ? 11.175  33.837 41.250 1.00 21.40 ? 208 ILE A C   1 
ATOM   1574 O O   . ILE A 1 214 ? 11.182  33.281 40.179 1.00 2.29  ? 208 ILE A O   1 
ATOM   1575 C CB  . ILE A 1 214 ? 9.325   32.772 42.558 1.00 52.02 ? 208 ILE A CB  1 
ATOM   1576 C CG1 . ILE A 1 214 ? 7.798   32.685 42.425 1.00 50.29 ? 208 ILE A CG1 1 
ATOM   1577 C CG2 . ILE A 1 214 ? 9.735   32.661 44.006 1.00 26.93 ? 208 ILE A CG2 1 
ATOM   1578 C CD1 . ILE A 1 214 ? 7.002   33.426 43.511 1.00 46.32 ? 208 ILE A CD1 1 
ATOM   1579 N N   . GLU A 1 215 ? 12.282  34.325 41.787 1.00 18.32 ? 209 GLU A N   1 
ATOM   1580 C CA  . GLU A 1 215 ? 13.574  34.075 41.172 1.00 9.22  ? 209 GLU A CA  1 
ATOM   1581 C C   . GLU A 1 215 ? 14.528  33.388 42.159 1.00 24.44 ? 209 GLU A C   1 
ATOM   1582 O O   . GLU A 1 215 ? 15.106  34.051 43.020 1.00 36.36 ? 209 GLU A O   1 
ATOM   1583 C CB  . GLU A 1 215 ? 14.179  35.399 40.696 1.00 2.45  ? 209 GLU A CB  1 
ATOM   1584 C CG  . GLU A 1 215 ? 15.594  35.246 40.147 1.00 41.15 ? 209 GLU A CG  1 
ATOM   1585 C CD  . GLU A 1 215 ? 15.867  36.117 38.936 1.00 66.18 ? 209 GLU A CD  1 
ATOM   1586 O OE1 . GLU A 1 215 ? 14.953  36.293 38.102 1.00 50.09 ? 209 GLU A OE1 1 
ATOM   1587 O OE2 . GLU A 1 215 ? 17.015  36.592 38.796 1.00 42.45 ? 209 GLU A OE2 1 
ATOM   1588 N N   . ASN A 1 216 ? 14.681  32.069 42.050 1.00 26.61 ? 210 ASN A N   1 
ATOM   1589 C CA  . ASN A 1 216 ? 15.539  31.311 42.972 1.00 12.35 ? 210 ASN A CA  1 
ATOM   1590 C C   . ASN A 1 216 ? 15.110  31.402 44.443 1.00 29.84 ? 210 ASN A C   1 
ATOM   1591 O O   . ASN A 1 216 ? 15.848  31.925 45.302 1.00 4.51  ? 210 ASN A O   1 
ATOM   1592 C CB  . ASN A 1 216 ? 17.001  31.755 42.852 1.00 22.54 ? 210 ASN A CB  1 
ATOM   1593 C CG  . ASN A 1 216 ? 17.651  31.298 41.557 1.00 31.80 ? 210 ASN A CG  1 
ATOM   1594 O OD1 . ASN A 1 216 ? 17.002  30.701 40.686 1.00 54.82 ? 210 ASN A OD1 1 
ATOM   1595 N ND2 . ASN A 1 216 ? 18.934  31.627 41.397 1.00 40.54 ? 210 ASN A ND2 1 
ATOM   1596 N N   . GLY A 1 217 ? 13.899  30.915 44.721 1.00 9.56  ? 211 GLY A N   1 
ATOM   1597 C CA  . GLY A 1 217 ? 13.376  30.938 46.076 1.00 67.25 ? 211 GLY A CA  1 
ATOM   1598 C C   . GLY A 1 217 ? 12.735  32.250 46.472 1.00 8.74  ? 211 GLY A C   1 
ATOM   1599 O O   . GLY A 1 217 ? 11.759  32.254 47.217 1.00 35.23 ? 211 GLY A O   1 
ATOM   1600 N N   . VAL A 1 218 ? 13.185  33.336 45.846 1.00 35.72 ? 212 VAL A N   1 
ATOM   1601 C CA  . VAL A 1 218 ? 12.850  34.686 46.296 1.00 51.28 ? 212 VAL A CA  1 
ATOM   1602 C C   . VAL A 1 218 ? 11.730  35.341 45.484 1.00 22.11 ? 212 VAL A C   1 
ATOM   1603 O O   . VAL A 1 218 ? 11.836  35.465 44.266 1.00 43.14 ? 212 VAL A O   1 
ATOM   1604 C CB  . VAL A 1 218 ? 14.083  35.601 46.236 1.00 50.78 ? 212 VAL A CB  1 
ATOM   1605 C CG1 . VAL A 1 218 ? 13.726  36.978 46.747 1.00 21.18 ? 212 VAL A CG1 1 
ATOM   1606 C CG2 . VAL A 1 218 ? 15.235  35.005 47.050 1.00 9.63  ? 212 VAL A CG2 1 
ATOM   1607 N N   . PRO A 1 219 ? 10.649  35.788 46.157 1.00 31.13 ? 213 PRO A N   1 
ATOM   1608 C CA  . PRO A 1 219 ? 9.547   36.513 45.518 1.00 13.47 ? 213 PRO A CA  1 
ATOM   1609 C C   . PRO A 1 219 ? 9.903   37.960 45.214 1.00 22.23 ? 213 PRO A C   1 
ATOM   1610 O O   . PRO A 1 219 ? 10.637  38.598 45.965 1.00 10.00 ? 213 PRO A O   1 
ATOM   1611 C CB  . PRO A 1 219 ? 8.412   36.417 46.546 1.00 5.10  ? 213 PRO A CB  1 
ATOM   1612 C CG  . PRO A 1 219 ? 8.831   35.381 47.490 1.00 4.12  ? 213 PRO A CG  1 
ATOM   1613 C CD  . PRO A 1 219 ? 10.313  35.484 47.552 1.00 26.55 ? 213 PRO A CD  1 
ATOM   1614 N N   . TYR A 1 220 ? 9.475   38.443 44.057 1.00 12.25 ? 214 TYR A N   1 
ATOM   1615 C CA  . TYR A 1 220 ? 9.742   39.827 43.695 1.00 2.09  ? 214 TYR A CA  1 
ATOM   1616 C C   . TYR A 1 220 ? 8.651   40.560 42.950 1.00 2.00  ? 214 TYR A C   1 
ATOM   1617 O O   . TYR A 1 220 ? 7.642   39.982 42.554 1.00 6.43  ? 214 TYR A O   1 
ATOM   1618 C CB  . TYR A 1 220 ? 11.077  39.953 42.953 1.00 27.79 ? 214 TYR A CB  1 
ATOM   1619 C CG  . TYR A 1 220 ? 11.091  39.273 41.625 1.00 22.14 ? 214 TYR A CG  1 
ATOM   1620 C CD1 . TYR A 1 220 ? 10.364  39.792 40.576 1.00 17.55 ? 214 TYR A CD1 1 
ATOM   1621 C CD2 . TYR A 1 220 ? 11.631  38.004 41.490 1.00 22.75 ? 214 TYR A CD2 1 
ATOM   1622 C CE1 . TYR A 1 220 ? 10.109  39.061 39.474 1.00 3.85  ? 214 TYR A CE1 1 
ATOM   1623 C CE2 . TYR A 1 220 ? 11.422  37.277 40.370 1.00 2.00  ? 214 TYR A CE2 1 
ATOM   1624 C CZ  . TYR A 1 220 ? 10.631  37.802 39.357 1.00 16.33 ? 214 TYR A CZ  1 
ATOM   1625 O OH  . TYR A 1 220 ? 10.275  37.063 38.257 1.00 18.17 ? 214 TYR A OH  1 
ATOM   1626 N N   . TRP A 1 221 ? 8.725   41.877 43.042 1.00 11.79 ? 215 TRP A N   1 
ATOM   1627 C CA  . TRP A 1 221 ? 8.009   42.740 42.133 1.00 8.87  ? 215 TRP A CA  1 
ATOM   1628 C C   . TRP A 1 221 ? 8.903   43.032 40.954 1.00 5.45  ? 215 TRP A C   1 
ATOM   1629 O O   . TRP A 1 221 ? 10.119  43.198 41.112 1.00 11.63 ? 215 TRP A O   1 
ATOM   1630 C CB  . TRP A 1 221 ? 7.631   44.041 42.823 1.00 3.68  ? 215 TRP A CB  1 
ATOM   1631 C CG  . TRP A 1 221 ? 6.659   43.855 43.975 1.00 19.64 ? 215 TRP A CG  1 
ATOM   1632 C CD1 . TRP A 1 221 ? 6.926   43.997 45.305 1.00 4.62  ? 215 TRP A CD1 1 
ATOM   1633 C CD2 . TRP A 1 221 ? 5.291   43.451 43.884 1.00 2.00  ? 215 TRP A CD2 1 
ATOM   1634 N NE1 . TRP A 1 221 ? 5.811   43.705 46.040 1.00 2.00  ? 215 TRP A NE1 1 
ATOM   1635 C CE2 . TRP A 1 221 ? 4.792   43.365 45.198 1.00 16.19 ? 215 TRP A CE2 1 
ATOM   1636 C CE3 . TRP A 1 221 ? 4.440   43.132 42.817 1.00 6.43  ? 215 TRP A CE3 1 
ATOM   1637 C CZ2 . TRP A 1 221 ? 3.485   42.973 45.484 1.00 6.80  ? 215 TRP A CZ2 1 
ATOM   1638 C CZ3 . TRP A 1 221 ? 3.139   42.747 43.099 1.00 2.00  ? 215 TRP A CZ3 1 
ATOM   1639 C CH2 . TRP A 1 221 ? 2.675   42.668 44.430 1.00 11.57 ? 215 TRP A CH2 1 
ATOM   1640 N N   . LEU A 1 222 ? 8.321   42.951 39.763 1.00 10.37 ? 216 LEU A N   1 
ATOM   1641 C CA  . LEU A 1 222 ? 8.958   43.453 38.547 1.00 2.00  ? 216 LEU A CA  1 
ATOM   1642 C C   . LEU A 1 222 ? 8.640   44.947 38.366 1.00 2.13  ? 216 LEU A C   1 
ATOM   1643 O O   . LEU A 1 222 ? 7.480   45.320 38.150 1.00 9.40  ? 216 LEU A O   1 
ATOM   1644 C CB  . LEU A 1 222 ? 8.458   42.668 37.340 1.00 11.44 ? 216 LEU A CB  1 
ATOM   1645 C CG  . LEU A 1 222 ? 8.995   43.210 36.014 1.00 14.89 ? 216 LEU A CG  1 
ATOM   1646 C CD1 . LEU A 1 222 ? 10.441  42.765 35.869 1.00 5.14  ? 216 LEU A CD1 1 
ATOM   1647 C CD2 . LEU A 1 222 ? 8.140   42.715 34.856 1.00 2.00  ? 216 LEU A CD2 1 
ATOM   1648 N N   . VAL A 1 223 ? 9.695   45.757 38.301 1.00 10.04 ? 217 VAL A N   1 
ATOM   1649 C CA  . VAL A 1 223 ? 9.601   47.212 38.485 1.00 2.00  ? 217 VAL A CA  1 
ATOM   1650 C C   . VAL A 1 223 ? 10.347  47.998 37.408 1.00 2.00  ? 217 VAL A C   1 
ATOM   1651 O O   . VAL A 1 223 ? 11.422  47.612 36.986 1.00 8.68  ? 217 VAL A O   1 
ATOM   1652 C CB  . VAL A 1 223 ? 10.120  47.599 39.871 1.00 11.97 ? 217 VAL A CB  1 
ATOM   1653 C CG1 . VAL A 1 223 ? 10.107  49.113 40.063 1.00 8.94  ? 217 VAL A CG1 1 
ATOM   1654 C CG2 . VAL A 1 223 ? 9.261   46.918 40.906 1.00 2.00  ? 217 VAL A CG2 1 
ATOM   1655 N N   . ALA A 1 224 ? 9.677   48.980 36.829 1.00 2.00  ? 218 ALA A N   1 
ATOM   1656 C CA  . ALA A 1 224 ? 10.300  49.825 35.827 1.00 4.45  ? 218 ALA A CA  1 
ATOM   1657 C C   . ALA A 1 224 ? 10.773  51.078 36.532 1.00 13.13 ? 218 ALA A C   1 
ATOM   1658 O O   . ALA A 1 224 ? 10.032  51.681 37.321 1.00 6.45  ? 218 ALA A O   1 
ATOM   1659 C CB  . ALA A 1 224 ? 9.290   50.200 34.721 1.00 2.00  ? 218 ALA A CB  1 
ATOM   1660 N N   . ASN A 1 225 ? 12.019  51.435 36.262 1.00 3.63  ? 219 ASN A N   1 
ATOM   1661 C CA  . ASN A 1 225 ? 12.649  52.666 36.749 1.00 2.00  ? 219 ASN A CA  1 
ATOM   1662 C C   . ASN A 1 225 ? 12.690  53.638 35.550 1.00 6.87  ? 219 ASN A C   1 
ATOM   1663 O O   . ASN A 1 225 ? 12.482  53.211 34.409 1.00 22.46 ? 219 ASN A O   1 
ATOM   1664 C CB  . ASN A 1 225 ? 14.058  52.327 37.244 1.00 2.00  ? 219 ASN A CB  1 
ATOM   1665 C CG  . ASN A 1 225 ? 14.612  53.351 38.214 1.00 13.99 ? 219 ASN A CG  1 
ATOM   1666 O OD1 . ASN A 1 225 ? 13.961  54.339 38.543 1.00 2.00  ? 219 ASN A OD1 1 
ATOM   1667 N ND2 . ASN A 1 225 ? 15.795  53.091 38.718 1.00 3.74  ? 219 ASN A ND2 1 
ATOM   1668 N N   . SER A 1 226 ? 12.745  54.945 35.823 1.00 7.64  ? 220 SER A N   1 
ATOM   1669 C CA  . SER A 1 226 ? 12.809  55.983 34.784 1.00 7.58  ? 220 SER A CA  1 
ATOM   1670 C C   . SER A 1 226 ? 14.247  56.532 34.658 1.00 2.00  ? 220 SER A C   1 
ATOM   1671 O O   . SER A 1 226 ? 14.484  57.755 34.601 1.00 2.00  ? 220 SER A O   1 
ATOM   1672 C CB  . SER A 1 226 ? 11.838  57.128 35.130 1.00 2.67  ? 220 SER A CB  1 
ATOM   1673 O OG  . SER A 1 226 ? 12.044  57.558 36.470 1.00 7.30  ? 220 SER A OG  1 
ATOM   1674 N N   . TRP A 1 227 ? 15.227  55.644 34.735 1.00 21.13 ? 221 TRP A N   1 
ATOM   1675 C CA  . TRP A 1 227 ? 16.612  56.065 34.544 1.00 12.52 ? 221 TRP A CA  1 
ATOM   1676 C C   . TRP A 1 227 ? 17.169  55.549 33.216 1.00 92.52 ? 221 TRP A C   1 
ATOM   1677 O O   . TRP A 1 227 ? 18.331  55.166 33.125 1.00 15.91 ? 221 TRP A O   1 
ATOM   1678 C CB  . TRP A 1 227 ? 17.464  55.583 35.714 1.00 7.43  ? 221 TRP A CB  1 
ATOM   1679 C CG  . TRP A 1 227 ? 17.191  56.324 36.983 1.00 2.00  ? 221 TRP A CG  1 
ATOM   1680 C CD1 . TRP A 1 227 ? 16.378  57.417 37.135 1.00 30.77 ? 221 TRP A CD1 1 
ATOM   1681 C CD2 . TRP A 1 227 ? 17.680  56.004 38.291 1.00 8.11  ? 221 TRP A CD2 1 
ATOM   1682 N NE1 . TRP A 1 227 ? 16.326  57.787 38.451 1.00 18.58 ? 221 TRP A NE1 1 
ATOM   1683 C CE2 . TRP A 1 227 ? 17.102  56.930 39.186 1.00 29.10 ? 221 TRP A CE2 1 
ATOM   1684 C CE3 . TRP A 1 227 ? 18.524  55.009 38.794 1.00 35.06 ? 221 TRP A CE3 1 
ATOM   1685 C CZ2 . TRP A 1 227 ? 17.334  56.879 40.561 1.00 2.36  ? 221 TRP A CZ2 1 
ATOM   1686 C CZ3 . TRP A 1 227 ? 18.759  54.961 40.159 1.00 12.35 ? 221 TRP A CZ3 1 
ATOM   1687 C CH2 . TRP A 1 227 ? 18.167  55.886 41.034 1.00 2.00  ? 221 TRP A CH2 1 
ATOM   1688 N N   . ASN A 1 228 ? 16.340  55.556 32.176 1.00 50.41 ? 222 ASN A N   1 
ATOM   1689 C CA  . ASN A 1 228 ? 16.746  55.070 30.860 1.00 2.00  ? 222 ASN A CA  1 
ATOM   1690 C C   . ASN A 1 228 ? 17.122  53.583 30.860 1.00 19.89 ? 222 ASN A C   1 
ATOM   1691 O O   . ASN A 1 228 ? 17.057  52.918 31.887 1.00 2.00  ? 222 ASN A O   1 
ATOM   1692 C CB  . ASN A 1 228 ? 17.929  55.875 30.338 1.00 57.20 ? 222 ASN A CB  1 
ATOM   1693 C CG  . ASN A 1 228 ? 17.845  56.128 28.857 1.00 26.66 ? 222 ASN A CG  1 
ATOM   1694 O OD1 . ASN A 1 228 ? 17.481  55.240 28.063 1.00 2.08  ? 222 ASN A OD1 1 
ATOM   1695 N ND2 . ASN A 1 228 ? 18.151  57.351 28.470 1.00 22.94 ? 222 ASN A ND2 1 
ATOM   1696 N N   . ALA A 1 229 ? 17.506  53.052 29.703 1.00 2.00  ? 223 ALA A N   1 
ATOM   1697 C CA  . ALA A 1 229 ? 17.724  51.629 29.627 1.00 6.86  ? 223 ALA A CA  1 
ATOM   1698 C C   . ALA A 1 229 ? 19.122  51.109 29.930 1.00 19.86 ? 223 ALA A C   1 
ATOM   1699 O O   . ALA A 1 229 ? 19.271  49.932 30.218 1.00 10.52 ? 223 ALA A O   1 
ATOM   1700 C CB  . ALA A 1 229 ? 17.241  51.104 28.306 1.00 9.68  ? 223 ALA A CB  1 
ATOM   1701 N N   . ASP A 1 230 ? 20.124  51.982 29.998 1.00 5.41  ? 224 ASP A N   1 
ATOM   1702 C CA  . ASP A 1 230 ? 21.457  51.523 30.399 1.00 32.67 ? 224 ASP A CA  1 
ATOM   1703 C C   . ASP A 1 230 ? 21.711  51.506 31.907 1.00 11.96 ? 224 ASP A C   1 
ATOM   1704 O O   . ASP A 1 230 ? 22.829  51.254 32.363 1.00 60.34 ? 224 ASP A O   1 
ATOM   1705 C CB  . ASP A 1 230 ? 22.546  52.333 29.703 1.00 10.99 ? 224 ASP A CB  1 
ATOM   1706 C CG  . ASP A 1 230 ? 22.552  53.795 30.099 1.00 27.22 ? 224 ASP A CG  1 
ATOM   1707 O OD1 . ASP A 1 230 ? 21.492  54.370 30.421 1.00 43.74 ? 224 ASP A OD1 1 
ATOM   1708 O OD2 . ASP A 1 230 ? 23.638  54.388 30.006 1.00 28.78 ? 224 ASP A OD2 1 
ATOM   1709 N N   . TRP A 1 231 ? 20.664  51.775 32.676 1.00 64.39 ? 225 TRP A N   1 
ATOM   1710 C CA  . TRP A 1 231 ? 20.701  51.548 34.109 1.00 2.00  ? 225 TRP A CA  1 
ATOM   1711 C C   . TRP A 1 231 ? 20.080  50.175 34.392 1.00 7.14  ? 225 TRP A C   1 
ATOM   1712 O O   . TRP A 1 231 ? 19.138  49.765 33.735 1.00 2.00  ? 225 TRP A O   1 
ATOM   1713 C CB  . TRP A 1 231 ? 19.926  52.647 34.850 1.00 3.36  ? 225 TRP A CB  1 
ATOM   1714 C CG  . TRP A 1 231 ? 19.883  52.423 36.348 1.00 56.46 ? 225 TRP A CG  1 
ATOM   1715 C CD1 . TRP A 1 231 ? 20.822  52.811 37.281 1.00 2.00  ? 225 TRP A CD1 1 
ATOM   1716 C CD2 . TRP A 1 231 ? 18.949  51.604 37.049 1.00 2.00  ? 225 TRP A CD2 1 
ATOM   1717 N NE1 . TRP A 1 231 ? 20.547  52.251 38.500 1.00 2.62  ? 225 TRP A NE1 1 
ATOM   1718 C CE2 . TRP A 1 231 ? 19.394  51.511 38.387 1.00 20.80 ? 225 TRP A CE2 1 
ATOM   1719 C CE3 . TRP A 1 231 ? 17.785  50.916 36.672 1.00 15.30 ? 225 TRP A CE3 1 
ATOM   1720 C CZ2 . TRP A 1 231 ? 18.714  50.768 39.345 1.00 8.43  ? 225 TRP A CZ2 1 
ATOM   1721 C CZ3 . TRP A 1 231 ? 17.110  50.160 37.633 1.00 4.63  ? 225 TRP A CZ3 1 
ATOM   1722 C CH2 . TRP A 1 231 ? 17.581  50.100 38.956 1.00 2.00  ? 225 TRP A CH2 1 
ATOM   1723 N N   . GLY A 1 232 ? 20.527  49.554 35.470 1.00 11.46 ? 226 GLY A N   1 
ATOM   1724 C CA  . GLY A 1 232 ? 19.994  48.287 35.916 1.00 2.00  ? 226 GLY A CA  1 
ATOM   1725 C C   . GLY A 1 232 ? 19.856  47.244 34.832 1.00 8.35  ? 226 GLY A C   1 
ATOM   1726 O O   . GLY A 1 232 ? 20.659  47.195 33.899 1.00 25.57 ? 226 GLY A O   1 
ATOM   1727 N N   . ASP A 1 233 ? 18.778  46.472 34.923 1.00 2.00  ? 227 ASP A N   1 
ATOM   1728 C CA  . ASP A 1 233 ? 18.477  45.409 33.984 1.00 2.00  ? 227 ASP A CA  1 
ATOM   1729 C C   . ASP A 1 233 ? 17.661  45.950 32.821 1.00 6.06  ? 227 ASP A C   1 
ATOM   1730 O O   . ASP A 1 233 ? 16.468  45.692 32.720 1.00 2.00  ? 227 ASP A O   1 
ATOM   1731 C CB  . ASP A 1 233 ? 17.696  44.313 34.698 1.00 2.40  ? 227 ASP A CB  1 
ATOM   1732 C CG  . ASP A 1 233 ? 17.537  43.070 33.874 1.00 11.92 ? 227 ASP A CG  1 
ATOM   1733 O OD1 . ASP A 1 233 ? 17.872  43.079 32.675 1.00 16.67 ? 227 ASP A OD1 1 
ATOM   1734 O OD2 . ASP A 1 233 ? 17.071  42.061 34.432 1.00 29.83 ? 227 ASP A OD2 1 
ATOM   1735 N N   . ASN A 1 234 ? 18.325  46.647 31.902 1.00 2.00  ? 228 ASN A N   1 
ATOM   1736 C CA  . ASN A 1 234 ? 17.650  47.336 30.803 1.00 68.05 ? 228 ASN A CA  1 
ATOM   1737 C C   . ASN A 1 234 ? 16.706  48.427 31.291 1.00 4.23  ? 228 ASN A C   1 
ATOM   1738 O O   . ASN A 1 234 ? 15.696  48.689 30.668 1.00 2.75  ? 228 ASN A O   1 
ATOM   1739 C CB  . ASN A 1 234 ? 16.859  46.345 29.943 1.00 10.78 ? 228 ASN A CB  1 
ATOM   1740 C CG  . ASN A 1 234 ? 17.742  45.351 29.241 1.00 70.66 ? 228 ASN A CG  1 
ATOM   1741 O OD1 . ASN A 1 234 ? 18.914  45.612 29.000 1.00 10.12 ? 228 ASN A OD1 1 
ATOM   1742 N ND2 . ASN A 1 234 ? 17.188  44.188 28.926 1.00 15.32 ? 228 ASN A ND2 1 
ATOM   1743 N N   . GLY A 1 235 ? 17.005  49.008 32.444 1.00 11.71 ? 229 GLY A N   1 
ATOM   1744 C CA  . GLY A 1 235 ? 16.147  50.040 32.995 1.00 6.40  ? 229 GLY A CA  1 
ATOM   1745 C C   . GLY A 1 235 ? 15.087  49.512 33.943 1.00 29.02 ? 229 GLY A C   1 
ATOM   1746 O O   . GLY A 1 235 ? 14.426  50.295 34.623 1.00 2.50  ? 229 GLY A O   1 
ATOM   1747 N N   . PHE A 1 236 ? 14.843  48.205 33.888 1.00 4.87  ? 230 PHE A N   1 
ATOM   1748 C CA  . PHE A 1 236 ? 13.993  47.514 34.871 1.00 4.62  ? 230 PHE A CA  1 
ATOM   1749 C C   . PHE A 1 236 ? 14.804  46.962 36.051 1.00 42.67 ? 230 PHE A C   1 
ATOM   1750 O O   . PHE A 1 236 ? 16.036  46.866 36.002 1.00 2.00  ? 230 PHE A O   1 
ATOM   1751 C CB  . PHE A 1 236 ? 13.223  46.326 34.237 1.00 10.46 ? 230 PHE A CB  1 
ATOM   1752 C CG  . PHE A 1 236 ? 12.264  46.710 33.128 1.00 2.00  ? 230 PHE A CG  1 
ATOM   1753 C CD1 . PHE A 1 236 ? 10.981  47.122 33.402 1.00 41.51 ? 230 PHE A CD1 1 
ATOM   1754 C CD2 . PHE A 1 236 ? 12.643  46.575 31.791 1.00 75.77 ? 230 PHE A CD2 1 
ATOM   1755 C CE1 . PHE A 1 236 ? 10.095  47.403 32.371 1.00 4.72  ? 230 PHE A CE1 1 
ATOM   1756 C CE2 . PHE A 1 236 ? 11.746  46.854 30.747 1.00 12.69 ? 230 PHE A CE2 1 
ATOM   1757 C CZ  . PHE A 1 236 ? 10.481  47.273 31.047 1.00 3.64  ? 230 PHE A CZ  1 
ATOM   1758 N N   . PHE A 1 237 ? 14.073  46.449 37.034 1.00 4.91  ? 231 PHE A N   1 
ATOM   1759 C CA  . PHE A 1 237 ? 14.648  45.830 38.226 1.00 11.66 ? 231 PHE A CA  1 
ATOM   1760 C C   . PHE A 1 237 ? 13.598  44.998 38.973 1.00 8.77  ? 231 PHE A C   1 
ATOM   1761 O O   . PHE A 1 237 ? 12.413  45.023 38.641 1.00 2.00  ? 231 PHE A O   1 
ATOM   1762 C CB  . PHE A 1 237 ? 15.293  46.897 39.144 1.00 3.26  ? 231 PHE A CB  1 
ATOM   1763 C CG  . PHE A 1 237 ? 14.316  47.740 39.920 1.00 34.91 ? 231 PHE A CG  1 
ATOM   1764 C CD1 . PHE A 1 237 ? 13.892  47.353 41.182 1.00 6.35  ? 231 PHE A CD1 1 
ATOM   1765 C CD2 . PHE A 1 237 ? 13.991  49.009 39.484 1.00 13.67 ? 231 PHE A CD2 1 
ATOM   1766 C CE1 . PHE A 1 237 ? 13.189  48.218 41.982 1.00 2.12  ? 231 PHE A CE1 1 
ATOM   1767 C CE2 . PHE A 1 237 ? 13.293  49.876 40.286 1.00 27.55 ? 231 PHE A CE2 1 
ATOM   1768 C CZ  . PHE A 1 237 ? 12.898  49.484 41.534 1.00 2.00  ? 231 PHE A CZ  1 
ATOM   1769 N N   . LYS A 1 238 ? 14.085  44.060 39.763 1.00 4.48  ? 232 LYS A N   1 
ATOM   1770 C CA  . LYS A 1 238 ? 13.227  43.294 40.662 1.00 5.48  ? 232 LYS A CA  1 
ATOM   1771 C C   . LYS A 1 238 ? 13.526  43.713 42.121 1.00 34.81 ? 232 LYS A C   1 
ATOM   1772 O O   . LYS A 1 238 ? 14.634  44.180 42.428 1.00 13.24 ? 232 LYS A O   1 
ATOM   1773 C CB  . LYS A 1 238 ? 13.477  41.786 40.481 1.00 33.22 ? 232 LYS A CB  1 
ATOM   1774 C CG  . LYS A 1 238 ? 13.549  41.325 39.026 1.00 16.22 ? 232 LYS A CG  1 
ATOM   1775 C CD  . LYS A 1 238 ? 13.978  39.864 38.899 1.00 78.74 ? 232 LYS A CD  1 
ATOM   1776 C CE  . LYS A 1 238 ? 14.076  39.418 37.435 1.00 2.00  ? 232 LYS A CE  1 
ATOM   1777 N NZ  . LYS A 1 238 ? 15.227  40.075 36.737 1.00 43.79 ? 232 LYS A NZ  1 
ATOM   1778 N N   . ILE A 1 239 ? 12.508  43.648 42.980 1.00 25.86 ? 233 ILE A N   1 
ATOM   1779 C CA  . ILE A 1 239 ? 12.631  43.996 44.406 1.00 3.87  ? 233 ILE A CA  1 
ATOM   1780 C C   . ILE A 1 239 ? 11.819  43.018 45.266 1.00 2.00  ? 233 ILE A C   1 
ATOM   1781 O O   . ILE A 1 239 ? 10.778  42.513 44.829 1.00 8.97  ? 233 ILE A O   1 
ATOM   1782 C CB  . ILE A 1 239 ? 12.164  45.481 44.677 1.00 28.00 ? 233 ILE A CB  1 
ATOM   1783 C CG1 . ILE A 1 239 ? 12.361  45.864 46.149 1.00 6.77  ? 233 ILE A CG1 1 
ATOM   1784 C CG2 . ILE A 1 239 ? 10.700  45.662 44.288 1.00 32.79 ? 233 ILE A CG2 1 
ATOM   1785 C CD1 . ILE A 1 239 ? 12.432  47.355 46.396 1.00 2.00  ? 233 ILE A CD1 1 
ATOM   1786 N N   . LEU A 1 240 ? 12.387  42.603 46.392 1.00 6.84  ? 234 LEU A N   1 
ATOM   1787 C CA  . LEU A 1 240 ? 11.672  41.759 47.362 1.00 2.00  ? 234 LEU A CA  1 
ATOM   1788 C C   . LEU A 1 240 ? 10.171  42.082 47.516 1.00 4.84  ? 234 LEU A C   1 
ATOM   1789 O O   . LEU A 1 240 ? 9.773   43.244 47.753 1.00 13.80 ? 234 LEU A O   1 
ATOM   1790 C CB  . LEU A 1 240 ? 12.333  41.877 48.721 1.00 12.87 ? 234 LEU A CB  1 
ATOM   1791 C CG  . LEU A 1 240 ? 12.790  40.648 49.509 1.00 31.11 ? 234 LEU A CG  1 
ATOM   1792 C CD1 . LEU A 1 240 ? 13.371  41.159 50.793 1.00 9.71  ? 234 LEU A CD1 1 
ATOM   1793 C CD2 . LEU A 1 240 ? 11.667  39.686 49.783 1.00 42.20 ? 234 LEU A CD2 1 
ATOM   1794 N N   . ARG A 1 241 ? 9.357   41.036 47.441 1.00 2.00  ? 235 ARG A N   1 
ATOM   1795 C CA  . ARG A 1 241 ? 7.909   41.150 47.565 1.00 7.55  ? 235 ARG A CA  1 
ATOM   1796 C C   . ARG A 1 241 ? 7.414   40.361 48.769 1.00 27.06 ? 235 ARG A C   1 
ATOM   1797 O O   . ARG A 1 241 ? 7.930   39.275 49.055 1.00 19.44 ? 235 ARG A O   1 
ATOM   1798 C CB  . ARG A 1 241 ? 7.226   40.631 46.301 1.00 2.00  ? 235 ARG A CB  1 
ATOM   1799 C CG  . ARG A 1 241 ? 5.764   40.306 46.453 1.00 2.00  ? 235 ARG A CG  1 
ATOM   1800 C CD  . ARG A 1 241 ? 5.237   39.664 45.190 1.00 26.57 ? 235 ARG A CD  1 
ATOM   1801 N NE  . ARG A 1 241 ? 4.874   38.259 45.389 1.00 30.48 ? 235 ARG A NE  1 
ATOM   1802 C CZ  . ARG A 1 241 ? 5.354   37.262 44.660 1.00 2.00  ? 235 ARG A CZ  1 
ATOM   1803 N NH1 . ARG A 1 241 ? 6.354   37.483 43.829 1.00 39.39 ? 235 ARG A NH1 1 
ATOM   1804 N NH2 . ARG A 1 241 ? 4.940   36.021 44.860 1.00 35.80 ? 235 ARG A NH2 1 
ATOM   1805 N N   . GLY A 1 242 ? 6.385   40.884 49.438 1.00 2.00  ? 236 GLY A N   1 
ATOM   1806 C CA  . GLY A 1 242 ? 5.934   40.238 50.665 1.00 26.84 ? 236 GLY A CA  1 
ATOM   1807 C C   . GLY A 1 242 ? 6.213   40.890 52.016 1.00 2.00  ? 236 GLY A C   1 
ATOM   1808 O O   . GLY A 1 242 ? 5.308   41.043 52.812 1.00 27.08 ? 236 GLY A O   1 
ATOM   1809 N N   . GLU A 1 243 ? 7.438   41.313 52.284 1.00 24.38 ? 237 GLU A N   1 
ATOM   1810 C CA  . GLU A 1 243 ? 7.715   41.930 53.570 1.00 2.00  ? 237 GLU A CA  1 
ATOM   1811 C C   . GLU A 1 243 ? 7.916   43.456 53.534 1.00 6.64  ? 237 GLU A C   1 
ATOM   1812 O O   . GLU A 1 243 ? 8.756   43.981 54.256 1.00 12.79 ? 237 GLU A O   1 
ATOM   1813 C CB  . GLU A 1 243 ? 8.902   41.242 54.259 1.00 18.99 ? 237 GLU A CB  1 
ATOM   1814 C CG  . GLU A 1 243 ? 9.877   40.543 53.347 1.00 10.55 ? 237 GLU A CG  1 
ATOM   1815 C CD  . GLU A 1 243 ? 11.303  41.001 53.578 1.00 50.29 ? 237 GLU A CD  1 
ATOM   1816 O OE1 . GLU A 1 243 ? 11.604  42.163 53.229 1.00 83.95 ? 237 GLU A OE1 1 
ATOM   1817 O OE2 . GLU A 1 243 ? 12.128  40.220 54.109 1.00 14.40 ? 237 GLU A OE2 1 
ATOM   1818 N N   . ASN A 1 244 ? 6.979   44.168 52.901 1.00 2.00  ? 238 ASN A N   1 
ATOM   1819 C CA  . ASN A 1 244 ? 7.058   45.640 52.745 1.00 2.00  ? 238 ASN A CA  1 
ATOM   1820 C C   . ASN A 1 244 ? 8.454   46.216 52.471 1.00 2.00  ? 238 ASN A C   1 
ATOM   1821 O O   . ASN A 1 244 ? 8.746   47.362 52.847 1.00 8.48  ? 238 ASN A O   1 
ATOM   1822 C CB  . ASN A 1 244 ? 6.511   46.364 53.988 1.00 2.00  ? 238 ASN A CB  1 
ATOM   1823 C CG  . ASN A 1 244 ? 6.036   47.802 53.674 1.00 7.36  ? 238 ASN A CG  1 
ATOM   1824 O OD1 . ASN A 1 244 ? 6.000   48.661 54.542 1.00 24.39 ? 238 ASN A OD1 1 
ATOM   1825 N ND2 . ASN A 1 244 ? 5.684   48.053 52.429 1.00 3.78  ? 238 ASN A ND2 1 
ATOM   1826 N N   . HIS A 1 245 ? 9.333   45.433 51.870 1.00 2.00  ? 239 HIS A N   1 
ATOM   1827 C CA  . HIS A 1 245 ? 10.732  45.841 51.721 1.00 26.50 ? 239 HIS A CA  1 
ATOM   1828 C C   . HIS A 1 245 ? 10.960  47.283 51.229 1.00 9.87  ? 239 HIS A C   1 
ATOM   1829 O O   . HIS A 1 245 ? 10.466  47.659 50.168 1.00 17.40 ? 239 HIS A O   1 
ATOM   1830 C CB  . HIS A 1 245 ? 11.454  44.880 50.797 1.00 10.47 ? 239 HIS A CB  1 
ATOM   1831 C CG  . HIS A 1 245 ? 12.916  44.805 51.069 1.00 2.00  ? 239 HIS A CG  1 
ATOM   1832 N ND1 . HIS A 1 245 ? 13.829  45.631 50.444 1.00 16.85 ? 239 HIS A ND1 1 
ATOM   1833 C CD2 . HIS A 1 245 ? 13.612  44.103 51.990 1.00 7.53  ? 239 HIS A CD2 1 
ATOM   1834 C CE1 . HIS A 1 245 ? 15.026  45.428 50.963 1.00 15.88 ? 239 HIS A CE1 1 
ATOM   1835 N NE2 . HIS A 1 245 ? 14.920  44.506 51.903 1.00 2.00  ? 239 HIS A NE2 1 
ATOM   1836 N N   . CYS A 1 246 ? 11.539  48.123 52.083 1.00 18.91 ? 240 CYS A N   1 
ATOM   1837 C CA  . CYS A 1 246 ? 11.752  49.554 51.780 1.00 5.53  ? 240 CYS A CA  1 
ATOM   1838 C C   . CYS A 1 246 ? 10.453  50.341 51.550 1.00 2.00  ? 240 CYS A C   1 
ATOM   1839 O O   . CYS A 1 246 ? 10.422  51.320 50.819 1.00 2.00  ? 240 CYS A O   1 
ATOM   1840 C CB  . CYS A 1 246 ? 12.697  49.698 50.584 1.00 28.19 ? 240 CYS A CB  1 
ATOM   1841 S SG  . CYS A 1 246 ? 14.391  49.150 50.965 1.00 18.60 ? 240 CYS A SG  1 
ATOM   1842 N N   . GLY A 1 247 ? 9.372   49.808 52.105 1.00 33.29 ? 241 GLY A N   1 
ATOM   1843 C CA  . GLY A 1 247 ? 8.052   50.381 51.931 1.00 2.00  ? 241 GLY A CA  1 
ATOM   1844 C C   . GLY A 1 247 ? 7.572   50.314 50.503 1.00 2.00  ? 241 GLY A C   1 
ATOM   1845 O O   . GLY A 1 247 ? 6.634   51.027 50.127 1.00 2.97  ? 241 GLY A O   1 
ATOM   1846 N N   . ILE A 1 248 ? 8.180   49.437 49.706 1.00 2.00  ? 242 ILE A N   1 
ATOM   1847 C CA  . ILE A 1 248 ? 7.670   49.156 48.352 1.00 2.00  ? 242 ILE A CA  1 
ATOM   1848 C C   . ILE A 1 248 ? 6.156   48.874 48.278 1.00 2.00  ? 242 ILE A C   1 
ATOM   1849 O O   . ILE A 1 248 ? 5.529   49.179 47.269 1.00 14.59 ? 242 ILE A O   1 
ATOM   1850 C CB  . ILE A 1 248 ? 8.463   47.975 47.644 1.00 8.07  ? 242 ILE A CB  1 
ATOM   1851 C CG1 . ILE A 1 248 ? 8.064   47.862 46.169 1.00 2.00  ? 242 ILE A CG1 1 
ATOM   1852 C CG2 . ILE A 1 248 ? 8.192   46.634 48.332 1.00 2.00  ? 242 ILE A CG2 1 
ATOM   1853 C CD1 . ILE A 1 248 ? 8.147   49.151 45.359 1.00 2.00  ? 242 ILE A CD1 1 
ATOM   1854 N N   . GLU A 1 249 ? 5.543   48.393 49.362 1.00 3.45  ? 243 GLU A N   1 
ATOM   1855 C CA  . GLU A 1 249 ? 4.094   48.091 49.339 1.00 3.51  ? 243 GLU A CA  1 
ATOM   1856 C C   . GLU A 1 249 ? 3.219   49.129 50.079 1.00 8.29  ? 243 GLU A C   1 
ATOM   1857 O O   . GLU A 1 249 ? 2.021   48.953 50.263 1.00 2.00  ? 243 GLU A O   1 
ATOM   1858 C CB  . GLU A 1 249 ? 3.839   46.708 49.927 1.00 3.94  ? 243 GLU A CB  1 
ATOM   1859 C CG  . GLU A 1 249 ? 4.212   45.580 49.014 1.00 14.51 ? 243 GLU A CG  1 
ATOM   1860 C CD  . GLU A 1 249 ? 5.028   44.510 49.715 1.00 49.34 ? 243 GLU A CD  1 
ATOM   1861 O OE1 . GLU A 1 249 ? 4.742   44.157 50.870 1.00 18.08 ? 243 GLU A OE1 1 
ATOM   1862 O OE2 . GLU A 1 249 ? 5.982   44.020 49.110 1.00 2.00  ? 243 GLU A OE2 1 
ATOM   1863 N N   . SER A 1 250 ? 3.803   50.284 50.342 1.00 8.39  ? 244 SER A N   1 
ATOM   1864 C CA  . SER A 1 250 ? 3.173   51.244 51.204 1.00 13.17 ? 244 SER A CA  1 
ATOM   1865 C C   . SER A 1 250 ? 2.461   52.370 50.484 1.00 5.01  ? 244 SER A C   1 
ATOM   1866 O O   . SER A 1 250 ? 1.533   52.969 51.055 1.00 9.98  ? 244 SER A O   1 
ATOM   1867 C CB  . SER A 1 250 ? 4.215   51.787 52.176 1.00 13.79 ? 244 SER A CB  1 
ATOM   1868 O OG  . SER A 1 250 ? 4.744   50.700 52.931 1.00 16.05 ? 244 SER A OG  1 
ATOM   1869 N N   . GLU A 1 251 ? 2.836   52.612 49.227 1.00 7.16  ? 245 GLU A N   1 
ATOM   1870 C CA  . GLU A 1 251 ? 2.295   53.738 48.451 1.00 9.90  ? 245 GLU A CA  1 
ATOM   1871 C C   . GLU A 1 251 ? 1.769   53.416 47.067 1.00 11.29 ? 245 GLU A C   1 
ATOM   1872 O O   . GLU A 1 251 ? 2.068   54.127 46.107 1.00 11.06 ? 245 GLU A O   1 
ATOM   1873 C CB  . GLU A 1 251 ? 3.326   54.842 48.274 1.00 3.98  ? 245 GLU A CB  1 
ATOM   1874 C CG  . GLU A 1 251 ? 3.222   55.942 49.252 1.00 44.15 ? 245 GLU A CG  1 
ATOM   1875 C CD  . GLU A 1 251 ? 4.472   56.032 50.031 1.00 5.71  ? 245 GLU A CD  1 
ATOM   1876 O OE1 . GLU A 1 251 ? 4.834   54.996 50.614 1.00 16.86 ? 245 GLU A OE1 1 
ATOM   1877 O OE2 . GLU A 1 251 ? 5.163   57.072 49.963 1.00 82.38 ? 245 GLU A OE2 1 
ATOM   1878 N N   . ILE A 1 252 ? 1.004   52.346 46.956 1.00 2.34  ? 246 ILE A N   1 
ATOM   1879 C CA  . ILE A 1 252 ? 0.443   51.966 45.667 1.00 2.00  ? 246 ILE A CA  1 
ATOM   1880 C C   . ILE A 1 252 ? -0.752  52.885 45.367 1.00 21.54 ? 246 ILE A C   1 
ATOM   1881 O O   . ILE A 1 252 ? -1.608  53.091 46.236 1.00 2.00  ? 246 ILE A O   1 
ATOM   1882 C CB  . ILE A 1 252 ? -0.013  50.480 45.677 1.00 2.00  ? 246 ILE A CB  1 
ATOM   1883 C CG1 . ILE A 1 252 ? 1.158   49.558 46.087 1.00 4.53  ? 246 ILE A CG1 1 
ATOM   1884 C CG2 . ILE A 1 252 ? -0.556  50.116 44.330 1.00 10.25 ? 246 ILE A CG2 1 
ATOM   1885 C CD1 . ILE A 1 252 ? 2.370   49.581 45.178 1.00 2.00  ? 246 ILE A CD1 1 
ATOM   1886 N N   . VAL A 1 253 ? -0.692  53.551 44.210 1.00 2.00  ? 247 VAL A N   1 
ATOM   1887 C CA  . VAL A 1 253 ? -1.740  54.452 43.702 1.00 14.69 ? 247 VAL A CA  1 
ATOM   1888 C C   . VAL A 1 253 ? -2.124  54.057 42.266 1.00 4.95  ? 247 VAL A C   1 
ATOM   1889 O O   . VAL A 1 253 ? -1.265  53.664 41.458 1.00 2.00  ? 247 VAL A O   1 
ATOM   1890 C CB  . VAL A 1 253 ? -1.255  55.939 43.650 1.00 4.95  ? 247 VAL A CB  1 
ATOM   1891 C CG1 . VAL A 1 253 ? -2.385  56.839 43.208 1.00 2.00  ? 247 VAL A CG1 1 
ATOM   1892 C CG2 . VAL A 1 253 ? -0.831  56.400 44.997 1.00 5.53  ? 247 VAL A CG2 1 
ATOM   1893 N N   . ALA A 1 254 ? -3.391  54.243 41.901 1.00 3.41  ? 248 ALA A N   1 
ATOM   1894 C CA  . ALA A 1 254 ? -3.846  53.718 40.623 1.00 12.01 ? 248 ALA A CA  1 
ATOM   1895 C C   . ALA A 1 254 ? -5.108  54.412 40.167 1.00 2.00  ? 248 ALA A C   1 
ATOM   1896 O O   . ALA A 1 254 ? -5.500  55.395 40.747 1.00 3.31  ? 248 ALA A O   1 
ATOM   1897 C CB  . ALA A 1 254 ? -4.055  52.214 40.725 1.00 4.19  ? 248 ALA A CB  1 
ATOM   1898 N N   . GLY A 1 255 ? -5.673  53.986 39.051 1.00 10.30 ? 249 GLY A N   1 
ATOM   1899 C CA  . GLY A 1 255 ? -6.815  54.690 38.507 1.00 4.41  ? 249 GLY A CA  1 
ATOM   1900 C C   . GLY A 1 255 ? -7.349  53.990 37.291 1.00 2.00  ? 249 GLY A C   1 
ATOM   1901 O O   . GLY A 1 255 ? -6.665  53.214 36.660 1.00 2.00  ? 249 GLY A O   1 
ATOM   1902 N N   . ILE A 1 256 ? -8.522  54.404 36.878 1.00 2.00  ? 250 ILE A N   1 
ATOM   1903 C CA  . ILE A 1 256 ? -9.212  53.809 35.752 1.00 3.34  ? 250 ILE A CA  1 
ATOM   1904 C C   . ILE A 1 256 ? -9.441  54.905 34.732 1.00 68.83 ? 250 ILE A C   1 
ATOM   1905 O O   . ILE A 1 256 ? -9.803  56.046 35.088 1.00 2.00  ? 250 ILE A O   1 
ATOM   1906 C CB  . ILE A 1 256 ? -10.573 53.222 36.191 1.00 9.33  ? 250 ILE A CB  1 
ATOM   1907 C CG1 . ILE A 1 256 ? -10.358 52.241 37.356 1.00 8.23  ? 250 ILE A CG1 1 
ATOM   1908 C CG2 . ILE A 1 256 ? -11.307 52.588 35.004 1.00 3.64  ? 250 ILE A CG2 1 
ATOM   1909 C CD1 . ILE A 1 256 ? -10.202 50.804 36.929 1.00 12.65 ? 250 ILE A CD1 1 
ATOM   1910 N N   . PRO A 1 257 ? -9.131  54.609 33.463 1.00 2.00  ? 251 PRO A N   1 
ATOM   1911 C CA  . PRO A 1 257 ? -9.335  55.588 32.407 1.00 2.00  ? 251 PRO A CA  1 
ATOM   1912 C C   . PRO A 1 257 ? -10.819 55.761 32.133 1.00 2.00  ? 251 PRO A C   1 
ATOM   1913 O O   . PRO A 1 257 ? -11.604 54.822 32.286 1.00 21.43 ? 251 PRO A O   1 
ATOM   1914 C CB  . PRO A 1 257 ? -8.603  54.972 31.213 1.00 13.15 ? 251 PRO A CB  1 
ATOM   1915 C CG  . PRO A 1 257 ? -7.536  54.102 31.843 1.00 3.90  ? 251 PRO A CG  1 
ATOM   1916 C CD  . PRO A 1 257 ? -8.302  53.483 32.997 1.00 23.04 ? 251 PRO A CD  1 
ATOM   1917 N N   . ARG A 1 258 ? -11.214 56.988 31.847 1.00 3.28  ? 252 ARG A N   1 
ATOM   1918 C CA  . ARG A 1 258 ? -12.543 57.267 31.329 1.00 4.95  ? 252 ARG A CA  1 
ATOM   1919 C C   . ARG A 1 258 ? -12.747 56.712 29.901 1.00 17.49 ? 252 ARG A C   1 
ATOM   1920 O O   . ARG A 1 258 ? -11.791 56.587 29.146 1.00 30.01 ? 252 ARG A O   1 
ATOM   1921 C CB  . ARG A 1 258 ? -12.754 58.771 31.342 1.00 2.00  ? 252 ARG A CB  1 
ATOM   1922 C CG  . ARG A 1 258 ? -14.191 59.190 31.021 1.00 4.46  ? 252 ARG A CG  1 
ATOM   1923 C CD  . ARG A 1 258 ? -14.747 60.237 31.971 1.00 83.56 ? 252 ARG A CD  1 
ATOM   1924 N NE  . ARG A 1 258 ? -14.557 61.593 31.462 1.00 52.23 ? 252 ARG A NE  1 
ATOM   1925 C CZ  . ARG A 1 258 ? -14.267 62.644 32.222 1.00 27.47 ? 252 ARG A CZ  1 
ATOM   1926 N NH1 . ARG A 1 258 ? -14.211 62.517 33.547 1.00 53.05 ? 252 ARG A NH1 1 
ATOM   1927 N NH2 . ARG A 1 258 ? -14.057 63.829 31.653 1.00 38.60 ? 252 ARG A NH2 1 
ATOM   1928 N N   . THR A 1 259 ? -13.972 56.290 29.586 1.00 15.81 ? 253 THR A N   1 
ATOM   1929 C CA  . THR A 1 259 ? -14.334 55.820 28.248 1.00 90.19 ? 253 THR A CA  1 
ATOM   1930 C C   . THR A 1 259 ? -14.755 56.979 27.343 1.00 28.71 ? 253 THR A C   1 
ATOM   1931 O O   . THR A 1 259 ? -13.924 57.772 26.905 1.00 23.50 ? 253 THR A O   1 
ATOM   1932 C CB  . THR A 1 259 ? -15.496 54.800 28.318 1.00 10.85 ? 253 THR A CB  1 
ATOM   1933 O OG1 . THR A 1 259 ? -15.024 53.576 28.894 1.00 25.49 ? 253 THR A OG1 1 
ATOM   1934 C CG2 . THR A 1 259 ? -16.067 54.534 26.946 1.00 37.98 ? 253 THR A CG2 1 
ATOM   1935 N N   . LEU B 1 7   ? -21.447 66.570 55.913 1.00 6.87  ? 1   LEU B N   1 
ATOM   1936 C CA  . LEU B 1 7   ? -20.244 66.676 56.800 1.00 47.90 ? 1   LEU B CA  1 
ATOM   1937 C C   . LEU B 1 7   ? -20.190 68.036 57.488 1.00 23.65 ? 1   LEU B C   1 
ATOM   1938 O O   . LEU B 1 7   ? -20.657 69.028 56.935 1.00 60.63 ? 1   LEU B O   1 
ATOM   1939 C CB  . LEU B 1 7   ? -18.968 66.475 55.979 1.00 41.25 ? 1   LEU B CB  1 
ATOM   1940 C CG  . LEU B 1 7   ? -18.153 65.194 56.183 1.00 63.26 ? 1   LEU B CG  1 
ATOM   1941 C CD1 . LEU B 1 7   ? -18.828 64.270 57.179 1.00 15.02 ? 1   LEU B CD1 1 
ATOM   1942 C CD2 . LEU B 1 7   ? -17.970 64.511 54.837 1.00 44.14 ? 1   LEU B CD2 1 
ATOM   1943 N N   . PRO B 1 8   ? -19.681 68.088 58.732 1.00 25.63 ? 2   PRO B N   1 
ATOM   1944 C CA  . PRO B 1 8   ? -19.592 69.381 59.429 1.00 75.52 ? 2   PRO B CA  1 
ATOM   1945 C C   . PRO B 1 8   ? -18.485 70.286 58.878 1.00 71.37 ? 2   PRO B C   1 
ATOM   1946 O O   . PRO B 1 8   ? -17.436 69.812 58.466 1.00 2.00  ? 2   PRO B O   1 
ATOM   1947 C CB  . PRO B 1 8   ? -19.330 68.992 60.895 1.00 9.43  ? 2   PRO B CB  1 
ATOM   1948 C CG  . PRO B 1 8   ? -19.623 67.528 60.978 1.00 86.09 ? 2   PRO B CG  1 
ATOM   1949 C CD  . PRO B 1 8   ? -19.316 66.976 59.623 1.00 23.17 ? 2   PRO B CD  1 
ATOM   1950 N N   . GLU B 1 9   ? -18.727 71.592 58.886 1.00 12.33 ? 3   GLU B N   1 
ATOM   1951 C CA  . GLU B 1 9   ? -17.717 72.574 58.507 1.00 3.24  ? 3   GLU B CA  1 
ATOM   1952 C C   . GLU B 1 9   ? -16.580 72.627 59.529 1.00 6.69  ? 3   GLU B C   1 
ATOM   1953 O O   . GLU B 1 9   ? -15.480 73.124 59.269 1.00 38.73 ? 3   GLU B O   1 
ATOM   1954 C CB  . GLU B 1 9   ? -18.338 73.964 58.354 1.00 23.76 ? 3   GLU B CB  1 
ATOM   1955 C CG  . GLU B 1 9   ? -19.189 74.407 59.540 1.00 19.33 ? 3   GLU B CG  1 
ATOM   1956 C CD  . GLU B 1 9   ? -18.841 75.834 60.022 1.00 39.74 ? 3   GLU B CD  1 
ATOM   1957 O OE1 . GLU B 1 9   ? -18.405 76.673 59.175 1.00 66.96 ? 3   GLU B OE1 1 
ATOM   1958 O OE2 . GLU B 1 9   ? -19.051 76.129 61.269 1.00 48.65 ? 3   GLU B OE2 1 
ATOM   1959 N N   . SER B 1 10  ? -16.861 72.088 60.701 1.00 34.11 ? 4   SER B N   1 
ATOM   1960 C CA  . SER B 1 10  ? -15.858 71.989 61.728 1.00 24.64 ? 4   SER B CA  1 
ATOM   1961 C C   . SER B 1 10  ? -16.056 70.702 62.484 1.00 19.50 ? 4   SER B C   1 
ATOM   1962 O O   . SER B 1 10  ? -17.063 70.006 62.292 1.00 28.00 ? 4   SER B O   1 
ATOM   1963 C CB  . SER B 1 10  ? -15.932 73.190 62.666 1.00 64.56 ? 4   SER B CB  1 
ATOM   1964 O OG  . SER B 1 10  ? -15.476 74.357 61.995 1.00 78.78 ? 4   SER B OG  1 
ATOM   1965 N N   . PHE B 1 11  ? -14.979 70.275 63.128 1.00 7.20  ? 5   PHE B N   1 
ATOM   1966 C CA  . PHE B 1 11  ? -14.949 68.984 63.819 1.00 16.14 ? 5   PHE B CA  1 
ATOM   1967 C C   . PHE B 1 11  ? -13.727 68.832 64.691 1.00 52.90 ? 5   PHE B C   1 
ATOM   1968 O O   . PHE B 1 11  ? -12.598 69.149 64.283 1.00 9.51  ? 5   PHE B O   1 
ATOM   1969 C CB  . PHE B 1 11  ? -15.002 67.813 62.835 1.00 11.92 ? 5   PHE B CB  1 
ATOM   1970 C CG  . PHE B 1 11  ? -15.226 66.472 63.495 1.00 24.69 ? 5   PHE B CG  1 
ATOM   1971 C CD1 . PHE B 1 11  ? -16.439 66.184 64.120 1.00 19.04 ? 5   PHE B CD1 1 
ATOM   1972 C CD2 . PHE B 1 11  ? -14.228 65.503 63.492 1.00 8.06  ? 5   PHE B CD2 1 
ATOM   1973 C CE1 . PHE B 1 11  ? -16.664 64.963 64.723 1.00 5.79  ? 5   PHE B CE1 1 
ATOM   1974 C CE2 . PHE B 1 11  ? -14.448 64.273 64.090 1.00 17.10 ? 5   PHE B CE2 1 
ATOM   1975 C CZ  . PHE B 1 11  ? -15.692 64.005 64.712 1.00 15.26 ? 5   PHE B CZ  1 
ATOM   1976 N N   . ASP B 1 12  ? -13.959 68.235 65.851 1.00 21.94 ? 6   ASP B N   1 
ATOM   1977 C CA  . ASP B 1 12  ? -12.904 67.924 66.786 1.00 21.99 ? 6   ASP B CA  1 
ATOM   1978 C C   . ASP B 1 12  ? -13.249 66.582 67.430 1.00 13.29 ? 6   ASP B C   1 
ATOM   1979 O O   . ASP B 1 12  ? -14.309 66.414 68.027 1.00 32.26 ? 6   ASP B O   1 
ATOM   1980 C CB  . ASP B 1 12  ? -12.803 69.041 67.837 1.00 4.96  ? 6   ASP B CB  1 
ATOM   1981 C CG  . ASP B 1 12  ? -11.418 69.132 68.483 1.00 26.67 ? 6   ASP B CG  1 
ATOM   1982 O OD1 . ASP B 1 12  ? -10.708 68.109 68.569 1.00 8.01  ? 6   ASP B OD1 1 
ATOM   1983 O OD2 . ASP B 1 12  ? -11.060 70.236 68.946 1.00 34.19 ? 6   ASP B OD2 1 
ATOM   1984 N N   . ALA B 1 13  ? -12.394 65.592 67.209 1.00 23.05 ? 7   ALA B N   1 
ATOM   1985 C CA  . ALA B 1 13  ? -12.594 64.289 67.810 1.00 10.36 ? 7   ALA B CA  1 
ATOM   1986 C C   . ALA B 1 13  ? -12.544 64.429 69.310 1.00 40.70 ? 7   ALA B C   1 
ATOM   1987 O O   . ALA B 1 13  ? -13.305 63.780 70.013 1.00 2.74  ? 7   ALA B O   1 
ATOM   1988 C CB  . ALA B 1 13  ? -11.526 63.311 67.328 1.00 55.80 ? 7   ALA B CB  1 
ATOM   1989 N N   . ARG B 1 14  ? -11.811 65.433 69.777 1.00 5.18  ? 8   ARG B N   1 
ATOM   1990 C CA  . ARG B 1 14  ? -11.675 65.650 71.207 1.00 2.00  ? 8   ARG B CA  1 
ATOM   1991 C C   . ARG B 1 14  ? -12.978 65.994 71.917 1.00 13.28 ? 8   ARG B C   1 
ATOM   1992 O O   . ARG B 1 14  ? -13.206 65.570 73.043 1.00 23.04 ? 8   ARG B O   1 
ATOM   1993 C CB  . ARG B 1 14  ? -10.649 66.717 71.466 1.00 4.35  ? 8   ARG B CB  1 
ATOM   1994 C CG  . ARG B 1 14  ? -9.244  66.185 71.483 1.00 22.01 ? 8   ARG B CG  1 
ATOM   1995 C CD  . ARG B 1 14  ? -8.259  67.303 71.671 1.00 32.49 ? 8   ARG B CD  1 
ATOM   1996 N NE  . ARG B 1 14  ? -8.709  68.505 70.981 1.00 5.02  ? 8   ARG B NE  1 
ATOM   1997 C CZ  . ARG B 1 14  ? -7.987  69.609 70.859 1.00 21.26 ? 8   ARG B CZ  1 
ATOM   1998 N NH1 . ARG B 1 14  ? -6.719  69.636 71.252 1.00 49.04 ? 8   ARG B NH1 1 
ATOM   1999 N NH2 . ARG B 1 14  ? -8.534  70.683 70.312 1.00 21.89 ? 8   ARG B NH2 1 
ATOM   2000 N N   . GLU B 1 15  ? -13.862 66.712 71.241 1.00 29.16 ? 9   GLU B N   1 
ATOM   2001 C CA  . GLU B 1 15  ? -15.210 66.872 71.763 1.00 19.88 ? 9   GLU B CA  1 
ATOM   2002 C C   . GLU B 1 15  ? -16.209 65.875 71.249 1.00 22.99 ? 9   GLU B C   1 
ATOM   2003 O O   . GLU B 1 15  ? -17.281 65.762 71.819 1.00 10.30 ? 9   GLU B O   1 
ATOM   2004 C CB  . GLU B 1 15  ? -15.773 68.252 71.501 1.00 42.34 ? 9   GLU B CB  1 
ATOM   2005 C CG  . GLU B 1 15  ? -14.997 69.347 72.140 1.00 60.87 ? 9   GLU B CG  1 
ATOM   2006 C CD  . GLU B 1 15  ? -14.397 70.223 71.094 1.00 43.53 ? 9   GLU B CD  1 
ATOM   2007 O OE1 . GLU B 1 15  ? -15.068 70.409 70.029 1.00 23.27 ? 9   GLU B OE1 1 
ATOM   2008 O OE2 . GLU B 1 15  ? -13.236 70.644 71.293 1.00 34.34 ? 9   GLU B OE2 1 
ATOM   2009 N N   . GLN B 1 16  ? -15.954 65.261 70.103 1.00 33.05 ? 10  GLN B N   1 
ATOM   2010 C CA  . GLN B 1 16  ? -16.881 64.233 69.656 1.00 2.13  ? 10  GLN B CA  1 
ATOM   2011 C C   . GLN B 1 16  ? -16.897 63.056 70.627 1.00 2.00  ? 10  GLN B C   1 
ATOM   2012 O O   . GLN B 1 16  ? -17.961 62.597 71.046 1.00 25.59 ? 10  GLN B O   1 
ATOM   2013 C CB  . GLN B 1 16  ? -16.552 63.753 68.259 1.00 2.00  ? 10  GLN B CB  1 
ATOM   2014 C CG  . GLN B 1 16  ? -17.536 62.702 67.747 1.00 29.65 ? 10  GLN B CG  1 
ATOM   2015 C CD  . GLN B 1 16  ? -18.830 63.311 67.271 1.00 31.07 ? 10  GLN B CD  1 
ATOM   2016 O OE1 . GLN B 1 16  ? -19.112 64.482 67.525 1.00 47.55 ? 10  GLN B OE1 1 
ATOM   2017 N NE2 . GLN B 1 16  ? -19.611 62.533 66.548 1.00 56.21 ? 10  GLN B NE2 1 
ATOM   2018 N N   . TRP B 1 17  ? -15.723 62.572 71.007 1.00 27.50 ? 11  TRP B N   1 
ATOM   2019 C CA  . TRP B 1 17  ? -15.659 61.485 71.973 1.00 22.52 ? 11  TRP B CA  1 
ATOM   2020 C C   . TRP B 1 17  ? -14.842 61.945 73.172 1.00 13.27 ? 11  TRP B C   1 
ATOM   2021 O O   . TRP B 1 17  ? -13.734 61.470 73.424 1.00 35.96 ? 11  TRP B O   1 
ATOM   2022 C CB  . TRP B 1 17  ? -15.064 60.223 71.332 1.00 2.00  ? 11  TRP B CB  1 
ATOM   2023 C CG  . TRP B 1 17  ? -15.757 59.786 70.046 1.00 49.28 ? 11  TRP B CG  1 
ATOM   2024 C CD1 . TRP B 1 17  ? -16.761 58.861 69.925 1.00 55.85 ? 11  TRP B CD1 1 
ATOM   2025 C CD2 . TRP B 1 17  ? -15.390 60.148 68.704 1.00 27.48 ? 11  TRP B CD2 1 
ATOM   2026 N NE1 . TRP B 1 17  ? -17.015 58.603 68.597 1.00 38.16 ? 11  TRP B NE1 1 
ATOM   2027 C CE2 . TRP B 1 17  ? -16.189 59.380 67.826 1.00 68.30 ? 11  TRP B CE2 1 
ATOM   2028 C CE3 . TRP B 1 17  ? -14.452 61.032 68.161 1.00 21.06 ? 11  TRP B CE3 1 
ATOM   2029 C CZ2 . TRP B 1 17  ? -16.074 59.460 66.440 1.00 81.08 ? 11  TRP B CZ2 1 
ATOM   2030 C CZ3 . TRP B 1 17  ? -14.333 61.108 66.777 1.00 40.46 ? 11  TRP B CZ3 1 
ATOM   2031 C CH2 . TRP B 1 17  ? -15.140 60.321 65.933 1.00 2.00  ? 11  TRP B CH2 1 
ATOM   2032 N N   . SER B 1 18  ? -15.467 62.810 73.964 1.00 65.08 ? 12  SER B N   1 
ATOM   2033 C CA  . SER B 1 18  ? -14.880 63.370 75.182 1.00 69.78 ? 12  SER B CA  1 
ATOM   2034 C C   . SER B 1 18  ? -14.673 62.336 76.293 1.00 2.57  ? 12  SER B C   1 
ATOM   2035 O O   . SER B 1 18  ? -13.783 62.485 77.139 1.00 23.77 ? 12  SER B O   1 
ATOM   2036 C CB  . SER B 1 18  ? -15.757 64.518 75.695 1.00 36.24 ? 12  SER B CB  1 
ATOM   2037 O OG  . SER B 1 18  ? -17.128 64.283 75.407 1.00 95.57 ? 12  SER B OG  1 
ATOM   2038 N N   . ASN B 1 19  ? -15.388 61.216 76.198 1.00 16.48 ? 13  ASN B N   1 
ATOM   2039 C CA  . ASN B 1 19  ? -15.161 60.073 77.087 1.00 35.60 ? 13  ASN B CA  1 
ATOM   2040 C C   . ASN B 1 19  ? -13.812 59.366 76.811 1.00 42.54 ? 13  ASN B C   1 
ATOM   2041 O O   . ASN B 1 19  ? -13.357 58.518 77.592 1.00 26.97 ? 13  ASN B O   1 
ATOM   2042 C CB  . ASN B 1 19  ? -16.326 59.070 76.961 1.00 17.76 ? 13  ASN B CB  1 
ATOM   2043 C CG  . ASN B 1 19  ? -16.444 58.475 75.561 1.00 79.95 ? 13  ASN B CG  1 
ATOM   2044 O OD1 . ASN B 1 19  ? -15.753 57.525 75.219 1.00 90.70 ? 13  ASN B OD1 1 
ATOM   2045 N ND2 . ASN B 1 19  ? -17.286 59.065 74.735 1.00 21.15 ? 13  ASN B ND2 1 
ATOM   2046 N N   . CYS B 1 20  ? -13.139 59.791 75.744 1.00 38.92 ? 14  CYS B N   1 
ATOM   2047 C CA  . CYS B 1 20  ? -11.970 59.091 75.210 1.00 7.73  ? 14  CYS B CA  1 
ATOM   2048 C C   . CYS B 1 20  ? -10.665 59.882 75.345 1.00 13.33 ? 14  CYS B C   1 
ATOM   2049 O O   . CYS B 1 20  ? -10.217 60.541 74.412 1.00 41.36 ? 14  CYS B O   1 
ATOM   2050 C CB  . CYS B 1 20  ? -12.235 58.731 73.755 1.00 31.11 ? 14  CYS B CB  1 
ATOM   2051 S SG  . CYS B 1 20  ? -13.352 57.306 73.634 1.00 19.60 ? 14  CYS B SG  1 
ATOM   2052 N N   . PRO B 1 21  ? -10.072 59.868 76.545 1.00 6.46  ? 15  PRO B N   1 
ATOM   2053 C CA  . PRO B 1 21  ? -8.943  60.715 76.939 1.00 45.14 ? 15  PRO B CA  1 
ATOM   2054 C C   . PRO B 1 21  ? -7.718  60.666 76.020 1.00 52.35 ? 15  PRO B C   1 
ATOM   2055 O O   . PRO B 1 21  ? -6.972  61.638 75.951 1.00 11.22 ? 15  PRO B O   1 
ATOM   2056 C CB  . PRO B 1 21  ? -8.600  60.223 78.346 1.00 2.00  ? 15  PRO B CB  1 
ATOM   2057 C CG  . PRO B 1 21  ? -9.246  58.852 78.430 1.00 5.32  ? 15  PRO B CG  1 
ATOM   2058 C CD  . PRO B 1 21  ? -10.501 58.999 77.655 1.00 17.64 ? 15  PRO B CD  1 
ATOM   2059 N N   . THR B 1 22  ? -7.479  59.546 75.336 1.00 3.09  ? 16  THR B N   1 
ATOM   2060 C CA  . THR B 1 22  ? -6.222  59.420 74.609 1.00 57.05 ? 16  THR B CA  1 
ATOM   2061 C C   . THR B 1 22  ? -6.221  60.378 73.418 1.00 2.00  ? 16  THR B C   1 
ATOM   2062 O O   . THR B 1 22  ? -5.240  61.090 73.182 1.00 6.04  ? 16  THR B O   1 
ATOM   2063 C CB  . THR B 1 22  ? -5.972  57.971 74.160 1.00 39.59 ? 16  THR B CB  1 
ATOM   2064 O OG1 . THR B 1 22  ? -6.986  57.560 73.236 1.00 16.64 ? 16  THR B OG1 1 
ATOM   2065 C CG2 . THR B 1 22  ? -5.981  57.042 75.372 1.00 5.87  ? 16  THR B CG2 1 
ATOM   2066 N N   . ILE B 1 23  ? -7.414  60.642 72.918 1.00 2.00  ? 17  ILE B N   1 
ATOM   2067 C CA  . ILE B 1 23  ? -7.617  61.667 71.912 1.00 2.00  ? 17  ILE B CA  1 
ATOM   2068 C C   . ILE B 1 23  ? -6.970  63.022 72.237 1.00 26.74 ? 17  ILE B C   1 
ATOM   2069 O O   . ILE B 1 23  ? -6.281  63.571 71.380 1.00 3.91  ? 17  ILE B O   1 
ATOM   2070 C CB  . ILE B 1 23  ? -9.093  61.875 71.610 1.00 2.00  ? 17  ILE B CB  1 
ATOM   2071 C CG1 . ILE B 1 23  ? -9.715  60.561 71.159 1.00 2.00  ? 17  ILE B CG1 1 
ATOM   2072 C CG2 . ILE B 1 23  ? -9.269  62.919 70.548 1.00 22.43 ? 17  ILE B CG2 1 
ATOM   2073 C CD1 . ILE B 1 23  ? -11.195 60.623 70.975 1.00 29.63 ? 17  ILE B CD1 1 
ATOM   2074 N N   . ALA B 1 24  ? -7.015  63.479 73.490 1.00 9.21  ? 18  ALA B N   1 
ATOM   2075 C CA  . ALA B 1 24  ? -6.433  64.796 73.791 1.00 15.64 ? 18  ALA B CA  1 
ATOM   2076 C C   . ALA B 1 24  ? -4.937  64.782 74.158 1.00 2.00  ? 18  ALA B C   1 
ATOM   2077 O O   . ALA B 1 24  ? -4.312  65.830 74.236 1.00 11.29 ? 18  ALA B O   1 
ATOM   2078 C CB  . ALA B 1 24  ? -7.249  65.506 74.872 1.00 4.00  ? 18  ALA B CB  1 
ATOM   2079 N N   . GLN B 1 25  ? -4.324  63.603 74.134 1.00 15.11 ? 19  GLN B N   1 
ATOM   2080 C CA  . GLN B 1 25  ? -2.978  63.432 74.697 1.00 4.14  ? 19  GLN B CA  1 
ATOM   2081 C C   . GLN B 1 25  ? -1.858  63.618 73.689 1.00 41.77 ? 19  GLN B C   1 
ATOM   2082 O O   . GLN B 1 25  ? -1.891  63.062 72.592 1.00 65.98 ? 19  GLN B O   1 
ATOM   2083 C CB  . GLN B 1 25  ? -2.850  62.055 75.336 1.00 2.00  ? 19  GLN B CB  1 
ATOM   2084 C CG  . GLN B 1 25  ? -1.486  61.753 75.944 1.00 2.00  ? 19  GLN B CG  1 
ATOM   2085 C CD  . GLN B 1 25  ? -1.237  60.247 76.101 1.00 19.81 ? 19  GLN B CD  1 
ATOM   2086 O OE1 . GLN B 1 25  ? -2.060  59.446 75.612 1.00 9.51  ? 19  GLN B OE1 1 
ATOM   2087 N NE2 . GLN B 1 25  ? -0.208  59.866 76.695 1.00 8.48  ? 19  GLN B NE2 1 
ATOM   2088 N N   . ILE B 1 26  ? -0.835  64.347 74.116 1.00 4.51  ? 20  ILE B N   1 
ATOM   2089 C CA  . ILE B 1 26  ? 0.380   64.538 73.346 1.00 2.00  ? 20  ILE B CA  1 
ATOM   2090 C C   . ILE B 1 26  ? 1.560   63.737 73.928 1.00 18.78 ? 20  ILE B C   1 
ATOM   2091 O O   . ILE B 1 26  ? 2.011   63.997 75.063 1.00 24.26 ? 20  ILE B O   1 
ATOM   2092 C CB  . ILE B 1 26  ? 0.739   66.044 73.277 1.00 2.00  ? 20  ILE B CB  1 
ATOM   2093 C CG1 . ILE B 1 26  ? -0.388  66.807 72.568 1.00 2.00  ? 20  ILE B CG1 1 
ATOM   2094 C CG2 . ILE B 1 26  ? 2.069   66.253 72.554 1.00 2.00  ? 20  ILE B CG2 1 
ATOM   2095 C CD1 . ILE B 1 26  ? -0.470  66.488 71.028 1.00 3.89  ? 20  ILE B CD1 1 
ATOM   2096 N N   . ARG B 1 27  ? 2.069   62.784 73.144 1.00 2.00  ? 21  ARG B N   1 
ATOM   2097 C CA  . ARG B 1 27  ? 3.215   62.004 73.590 1.00 14.33 ? 21  ARG B CA  1 
ATOM   2098 C C   . ARG B 1 27  ? 4.522   62.708 73.203 1.00 11.18 ? 21  ARG B C   1 
ATOM   2099 O O   . ARG B 1 27  ? 4.506   63.842 72.696 1.00 11.57 ? 21  ARG B O   1 
ATOM   2100 C CB  . ARG B 1 27  ? 3.173   60.563 73.047 1.00 2.00  ? 21  ARG B CB  1 
ATOM   2101 C CG  . ARG B 1 27  ? 1.827   60.113 72.477 1.00 43.03 ? 21  ARG B CG  1 
ATOM   2102 C CD  . ARG B 1 27  ? 1.010   59.188 73.383 1.00 19.66 ? 21  ARG B CD  1 
ATOM   2103 N NE  . ARG B 1 27  ? 1.467   57.803 73.295 1.00 14.04 ? 21  ARG B NE  1 
ATOM   2104 C CZ  . ARG B 1 27  ? 0.682   56.722 73.258 1.00 29.25 ? 21  ARG B CZ  1 
ATOM   2105 N NH1 . ARG B 1 27  ? -0.633  56.817 73.098 1.00 2.18  ? 21  ARG B NH1 1 
ATOM   2106 N NH2 . ARG B 1 27  ? 1.241   55.524 73.272 1.00 13.92 ? 21  ARG B NH2 1 
ATOM   2107 N N   . ASP B 1 28  ? 5.623   62.184 73.711 1.00 23.02 ? 22  ASP B N   1 
ATOM   2108 C CA  . ASP B 1 28  ? 6.933   62.636 73.274 1.00 8.49  ? 22  ASP B CA  1 
ATOM   2109 C C   . ASP B 1 28  ? 7.761   61.453 72.762 1.00 14.35 ? 22  ASP B C   1 
ATOM   2110 O O   . ASP B 1 28  ? 8.136   60.568 73.530 1.00 27.56 ? 22  ASP B O   1 
ATOM   2111 C CB  . ASP B 1 28  ? 7.669   63.323 74.428 1.00 24.04 ? 22  ASP B CB  1 
ATOM   2112 C CG  . ASP B 1 28  ? 8.915   64.087 73.968 1.00 2.00  ? 22  ASP B CG  1 
ATOM   2113 O OD1 . ASP B 1 28  ? 9.544   63.696 72.966 1.00 28.82 ? 22  ASP B OD1 1 
ATOM   2114 O OD2 . ASP B 1 28  ? 9.267   65.087 74.617 1.00 24.80 ? 22  ASP B OD2 1 
ATOM   2115 N N   . GLN B 1 29  ? 8.115   61.484 71.481 1.00 7.41  ? 23  GLN B N   1 
ATOM   2116 C CA  . GLN B 1 29  ? 8.870   60.388 70.888 1.00 3.12  ? 23  GLN B CA  1 
ATOM   2117 C C   . GLN B 1 29  ? 10.332  60.359 71.364 1.00 2.00  ? 23  GLN B C   1 
ATOM   2118 O O   . GLN B 1 29  ? 11.003  59.355 71.248 1.00 7.67  ? 23  GLN B O   1 
ATOM   2119 C CB  . GLN B 1 29  ? 8.802   60.455 69.362 1.00 22.21 ? 23  GLN B CB  1 
ATOM   2120 C CG  . GLN B 1 29  ? 9.362   61.763 68.768 1.00 17.51 ? 23  GLN B CG  1 
ATOM   2121 C CD  . GLN B 1 29  ? 9.283   61.796 67.266 1.00 37.36 ? 23  GLN B CD  1 
ATOM   2122 O OE1 . GLN B 1 29  ? 8.280   62.215 66.713 1.00 24.68 ? 23  GLN B OE1 1 
ATOM   2123 N NE2 . GLN B 1 29  ? 10.345  61.349 66.590 1.00 2.00  ? 23  GLN B NE2 1 
ATOM   2124 N N   . GLY B 1 30  ? 10.795  61.443 71.972 1.00 6.07  ? 24  GLY B N   1 
ATOM   2125 C CA  . GLY B 1 30  ? 12.185  61.514 72.411 1.00 7.73  ? 24  GLY B CA  1 
ATOM   2126 C C   . GLY B 1 30  ? 13.218  61.623 71.295 1.00 6.16  ? 24  GLY B C   1 
ATOM   2127 O O   . GLY B 1 30  ? 12.934  62.142 70.220 1.00 27.57 ? 24  GLY B O   1 
ATOM   2128 N N   . SER B 1 31  ? 14.421  61.109 71.552 1.00 54.31 ? 25  SER B N   1 
ATOM   2129 C CA  . SER B 1 31  ? 15.532  61.148 70.586 1.00 17.19 ? 25  SER B CA  1 
ATOM   2130 C C   . SER B 1 31  ? 15.549  59.901 69.691 1.00 41.70 ? 25  SER B C   1 
ATOM   2131 O O   . SER B 1 31  ? 16.523  59.132 69.675 1.00 29.44 ? 25  SER B O   1 
ATOM   2132 C CB  . SER B 1 31  ? 16.877  61.256 71.318 1.00 62.48 ? 25  SER B CB  1 
ATOM   2133 O OG  . SER B 1 31  ? 16.935  62.410 72.140 1.00 63.06 ? 25  SER B OG  1 
ATOM   2134 N N   . CYS B 1 32  ? 14.470  59.718 68.938 1.00 20.12 ? 26  CYS B N   1 
ATOM   2135 C CA  . CYS B 1 32  ? 14.267  58.507 68.133 1.00 5.19  ? 26  CYS B CA  1 
ATOM   2136 C C   . CYS B 1 32  ? 13.293  58.813 67.021 1.00 26.58 ? 26  CYS B C   1 
ATOM   2137 O O   . CYS B 1 32  ? 12.253  59.428 67.262 1.00 16.11 ? 26  CYS B O   1 
ATOM   2138 C CB  . CYS B 1 32  ? 13.686  57.381 69.005 1.00 26.61 ? 26  CYS B CB  1 
ATOM   2139 S SG  . CYS B 1 32  ? 13.133  55.891 68.108 1.00 17.24 ? 26  CYS B SG  1 
ATOM   2140 N N   . GLY B 1 33  ? 13.615  58.369 65.809 1.00 9.84  ? 27  GLY B N   1 
ATOM   2141 C CA  . GLY B 1 33  ? 12.722  58.565 64.670 1.00 8.36  ? 27  GLY B CA  1 
ATOM   2142 C C   . GLY B 1 33  ? 11.590  57.550 64.591 1.00 25.37 ? 27  GLY B C   1 
ATOM   2143 O O   . GLY B 1 33  ? 11.453  56.795 63.630 1.00 42.45 ? 27  GLY B O   1 
ATOM   2144 N N   . SER B 1 34  ? 10.725  57.611 65.589 1.00 3.49  ? 28  SER B N   1 
ATOM   2145 C CA  . SER B 1 34  ? 9.631   56.662 65.764 1.00 20.85 ? 28  SER B CA  1 
ATOM   2146 C C   . SER B 1 34  ? 8.294   57.389 65.637 1.00 26.87 ? 28  SER B C   1 
ATOM   2147 O O   . SER B 1 34  ? 7.292   56.979 66.250 1.00 8.64  ? 28  SER B O   1 
ATOM   2148 C CB  . SER B 1 34  ? 9.729   56.032 67.149 1.00 5.06  ? 28  SER B CB  1 
ATOM   2149 O OG  . SER B 1 34  ? 9.625   57.041 68.134 1.00 2.00  ? 28  SER B OG  1 
ATOM   2150 N N   . CYS B 1 35  ? 8.282   58.498 64.893 1.00 2.00  ? 29  CYS B N   1 
ATOM   2151 C CA  . CYS B 1 35  ? 7.025   59.215 64.656 1.00 8.31  ? 29  CYS B CA  1 
ATOM   2152 C C   . CYS B 1 35  ? 6.026   58.367 63.875 1.00 9.69  ? 29  CYS B C   1 
ATOM   2153 O O   . CYS B 1 35  ? 4.810   58.525 64.009 1.00 6.67  ? 29  CYS B O   1 
ATOM   2154 C CB  . CYS B 1 35  ? 7.275   60.543 63.923 1.00 36.51 ? 29  CYS B CB  1 
ATOM   2155 S SG  . CYS B 1 35  ? 8.455   60.495 62.556 1.00 15.83 ? 29  CYS B SG  1 
ATOM   2156 N N   . TRP B 1 36  ? 6.552   57.460 63.055 1.00 4.40  ? 30  TRP B N   1 
ATOM   2157 C CA  . TRP B 1 36  ? 5.719   56.458 62.375 1.00 6.38  ? 30  TRP B CA  1 
ATOM   2158 C C   . TRP B 1 36  ? 5.003   55.532 63.380 1.00 67.60 ? 30  TRP B C   1 
ATOM   2159 O O   . TRP B 1 36  ? 3.966   54.961 63.074 1.00 11.08 ? 30  TRP B O   1 
ATOM   2160 C CB  . TRP B 1 36  ? 6.583   55.618 61.424 1.00 2.00  ? 30  TRP B CB  1 
ATOM   2161 C CG  . TRP B 1 36  ? 7.580   54.716 62.131 1.00 2.00  ? 30  TRP B CG  1 
ATOM   2162 C CD1 . TRP B 1 36  ? 8.864   55.030 62.459 1.00 9.10  ? 30  TRP B CD1 1 
ATOM   2163 C CD2 . TRP B 1 36  ? 7.372   53.371 62.595 1.00 23.36 ? 30  TRP B CD2 1 
ATOM   2164 N NE1 . TRP B 1 36  ? 9.462   53.984 63.119 1.00 2.00  ? 30  TRP B NE1 1 
ATOM   2165 C CE2 . TRP B 1 36  ? 8.575   52.950 63.219 1.00 3.21  ? 30  TRP B CE2 1 
ATOM   2166 C CE3 . TRP B 1 36  ? 6.292   52.489 62.553 1.00 2.00  ? 30  TRP B CE3 1 
ATOM   2167 C CZ2 . TRP B 1 36  ? 8.723   51.688 63.812 1.00 2.00  ? 30  TRP B CZ2 1 
ATOM   2168 C CZ3 . TRP B 1 36  ? 6.437   51.239 63.140 1.00 6.73  ? 30  TRP B CZ3 1 
ATOM   2169 C CH2 . TRP B 1 36  ? 7.651   50.849 63.770 1.00 2.00  ? 30  TRP B CH2 1 
ATOM   2170 N N   . ALA B 1 37  ? 5.617   55.321 64.542 1.00 2.00  ? 31  ALA B N   1 
ATOM   2171 C CA  . ALA B 1 37  ? 5.078   54.445 65.567 1.00 10.48 ? 31  ALA B CA  1 
ATOM   2172 C C   . ALA B 1 37  ? 4.073   55.204 66.413 1.00 20.17 ? 31  ALA B C   1 
ATOM   2173 O O   . ALA B 1 37  ? 3.032   54.678 66.796 1.00 2.00  ? 31  ALA B O   1 
ATOM   2174 C CB  . ALA B 1 37  ? 6.210   53.916 66.449 1.00 2.00  ? 31  ALA B CB  1 
ATOM   2175 N N   . PHE B 1 38  ? 4.399   56.466 66.665 1.00 4.05  ? 32  PHE B N   1 
ATOM   2176 C CA  . PHE B 1 38  ? 3.651   57.316 67.579 1.00 2.24  ? 32  PHE B CA  1 
ATOM   2177 C C   . PHE B 1 38  ? 2.299   57.770 66.992 1.00 2.00  ? 32  PHE B C   1 
ATOM   2178 O O   . PHE B 1 38  ? 1.284   57.567 67.644 1.00 18.06 ? 32  PHE B O   1 
ATOM   2179 C CB  . PHE B 1 38  ? 4.517   58.508 67.996 1.00 2.00  ? 32  PHE B CB  1 
ATOM   2180 C CG  . PHE B 1 38  ? 5.197   58.318 69.303 1.00 2.00  ? 32  PHE B CG  1 
ATOM   2181 C CD1 . PHE B 1 38  ? 6.274   57.462 69.408 1.00 2.08  ? 32  PHE B CD1 1 
ATOM   2182 C CD2 . PHE B 1 38  ? 4.660   58.833 70.453 1.00 20.77 ? 32  PHE B CD2 1 
ATOM   2183 C CE1 . PHE B 1 38  ? 6.787   57.098 70.629 1.00 26.67 ? 32  PHE B CE1 1 
ATOM   2184 C CE2 . PHE B 1 38  ? 5.183   58.468 71.684 1.00 2.09  ? 32  PHE B CE2 1 
ATOM   2185 C CZ  . PHE B 1 38  ? 6.235   57.599 71.769 1.00 20.23 ? 32  PHE B CZ  1 
ATOM   2186 N N   . GLY B 1 39  ? 2.259   58.044 65.679 1.00 8.09  ? 33  GLY B N   1 
ATOM   2187 C CA  . GLY B 1 39  ? 1.002   58.405 65.019 1.00 2.00  ? 33  GLY B CA  1 
ATOM   2188 C C   . GLY B 1 39  ? -0.006  57.269 64.880 1.00 24.98 ? 33  GLY B C   1 
ATOM   2189 O O   . GLY B 1 39  ? -1.243  57.491 64.738 1.00 5.94  ? 33  GLY B O   1 
ATOM   2190 N N   . ALA B 1 40  ? 0.518   56.045 64.948 1.00 17.54 ? 34  ALA B N   1 
ATOM   2191 C CA  . ALA B 1 40  ? -0.292  54.821 64.819 1.00 7.40  ? 34  ALA B CA  1 
ATOM   2192 C C   . ALA B 1 40  ? -0.879  54.332 66.158 1.00 23.78 ? 34  ALA B C   1 
ATOM   2193 O O   . ALA B 1 40  ? -2.076  54.000 66.233 1.00 3.03  ? 34  ALA B O   1 
ATOM   2194 C CB  . ALA B 1 40  ? 0.545   53.710 64.191 1.00 2.00  ? 34  ALA B CB  1 
ATOM   2195 N N   . VAL B 1 41  ? -0.027  54.144 67.175 1.00 3.65  ? 35  VAL B N   1 
ATOM   2196 C CA  . VAL B 1 41  ? -0.548  53.716 68.476 1.00 2.00  ? 35  VAL B CA  1 
ATOM   2197 C C   . VAL B 1 41  ? -1.461  54.796 69.032 1.00 2.00  ? 35  VAL B C   1 
ATOM   2198 O O   . VAL B 1 41  ? -2.505  54.493 69.603 1.00 2.49  ? 35  VAL B O   1 
ATOM   2199 C CB  . VAL B 1 41  ? 0.554   53.395 69.528 1.00 2.00  ? 35  VAL B CB  1 
ATOM   2200 C CG1 . VAL B 1 41  ? 1.351   52.209 69.089 1.00 3.04  ? 35  VAL B CG1 1 
ATOM   2201 C CG2 . VAL B 1 41  ? 1.473   54.615 69.783 1.00 2.00  ? 35  VAL B CG2 1 
ATOM   2202 N N   . GLU B 1 42  ? -1.135  56.051 68.771 1.00 2.00  ? 36  GLU B N   1 
ATOM   2203 C CA  . GLU B 1 42  ? -2.027  57.125 69.157 1.00 2.00  ? 36  GLU B CA  1 
ATOM   2204 C C   . GLU B 1 42  ? -3.429  56.998 68.576 1.00 2.00  ? 36  GLU B C   1 
ATOM   2205 O O   . GLU B 1 42  ? -4.420  57.138 69.303 1.00 16.10 ? 36  GLU B O   1 
ATOM   2206 C CB  . GLU B 1 42  ? -1.440  58.450 68.761 1.00 6.04  ? 36  GLU B CB  1 
ATOM   2207 C CG  . GLU B 1 42  ? -0.269  58.876 69.599 1.00 2.00  ? 36  GLU B CG  1 
ATOM   2208 C CD  . GLU B 1 42  ? 0.462   60.048 68.982 1.00 12.50 ? 36  GLU B CD  1 
ATOM   2209 O OE1 . GLU B 1 42  ? 0.091   60.482 67.877 1.00 2.00  ? 36  GLU B OE1 1 
ATOM   2210 O OE2 . GLU B 1 42  ? 1.398   60.554 69.602 1.00 2.00  ? 36  GLU B OE2 1 
ATOM   2211 N N   . ALA B 1 43  ? -3.512  56.886 67.253 1.00 2.00  ? 37  ALA B N   1 
ATOM   2212 C CA  . ALA B 1 43  ? -4.786  56.698 66.579 1.00 2.00  ? 37  ALA B CA  1 
ATOM   2213 C C   . ALA B 1 43  ? -5.455  55.375 66.946 1.00 6.95  ? 37  ALA B C   1 
ATOM   2214 O O   . ALA B 1 43  ? -6.692  55.293 66.963 1.00 4.58  ? 37  ALA B O   1 
ATOM   2215 C CB  . ALA B 1 43  ? -4.608  56.797 65.059 1.00 4.39  ? 37  ALA B CB  1 
ATOM   2216 N N   . MET B 1 44  ? -4.650  54.343 67.242 1.00 2.42  ? 38  MET B N   1 
ATOM   2217 C CA  . MET B 1 44  ? -5.172  53.023 67.644 1.00 2.00  ? 38  MET B CA  1 
ATOM   2218 C C   . MET B 1 44  ? -5.903  53.045 68.996 1.00 27.49 ? 38  MET B C   1 
ATOM   2219 O O   . MET B 1 44  ? -7.002  52.504 69.112 1.00 9.38  ? 38  MET B O   1 
ATOM   2220 C CB  . MET B 1 44  ? -4.035  51.995 67.700 1.00 2.00  ? 38  MET B CB  1 
ATOM   2221 C CG  . MET B 1 44  ? -3.730  51.339 66.354 1.00 2.00  ? 38  MET B CG  1 
ATOM   2222 S SD  . MET B 1 44  ? -2.067  50.736 66.368 1.00 11.60 ? 38  MET B SD  1 
ATOM   2223 C CE  . MET B 1 44  ? -1.721  50.535 64.565 1.00 20.33 ? 38  MET B CE  1 
ATOM   2224 N N   . SER B 1 45  ? -5.267  53.637 70.010 1.00 8.45  ? 39  SER B N   1 
ATOM   2225 C CA  . SER B 1 45  ? -5.905  53.961 71.291 1.00 3.59  ? 39  SER B CA  1 
ATOM   2226 C C   . SER B 1 45  ? -7.226  54.722 71.133 1.00 6.18  ? 39  SER B C   1 
ATOM   2227 O O   . SER B 1 45  ? -8.276  54.208 71.495 1.00 13.28 ? 39  SER B O   1 
ATOM   2228 C CB  . SER B 1 45  ? -4.948  54.783 72.160 1.00 2.00  ? 39  SER B CB  1 
ATOM   2229 O OG  . SER B 1 45  ? -3.659  54.192 72.239 1.00 2.00  ? 39  SER B OG  1 
ATOM   2230 N N   . ASP B 1 46  ? -7.187  55.909 70.526 1.00 9.86  ? 40  ASP B N   1 
ATOM   2231 C CA  . ASP B 1 46  ? -8.409  56.630 70.140 1.00 14.20 ? 40  ASP B CA  1 
ATOM   2232 C C   . ASP B 1 46  ? -9.492  55.684 69.608 1.00 11.91 ? 40  ASP B C   1 
ATOM   2233 O O   . ASP B 1 46  ? -10.627 55.685 70.090 1.00 36.91 ? 40  ASP B O   1 
ATOM   2234 C CB  . ASP B 1 46  ? -8.093  57.690 69.063 1.00 2.00  ? 40  ASP B CB  1 
ATOM   2235 C CG  . ASP B 1 46  ? -7.170  58.796 69.574 1.00 46.27 ? 40  ASP B CG  1 
ATOM   2236 O OD1 . ASP B 1 46  ? -6.553  58.643 70.646 1.00 10.89 ? 40  ASP B OD1 1 
ATOM   2237 O OD2 . ASP B 1 46  ? -7.065  59.839 68.911 1.00 26.75 ? 40  ASP B OD2 1 
ATOM   2238 N N   . ARG B 1 47  ? -9.101  54.776 68.723 1.00 27.09 ? 41  ARG B N   1 
ATOM   2239 C CA  . ARG B 1 47  ? -10.063 53.912 68.036 1.00 2.00  ? 41  ARG B CA  1 
ATOM   2240 C C   . ARG B 1 47  ? -10.624 52.774 68.860 1.00 13.83 ? 41  ARG B C   1 
ATOM   2241 O O   . ARG B 1 47  ? -11.808 52.414 68.699 1.00 4.69  ? 41  ARG B O   1 
ATOM   2242 C CB  . ARG B 1 47  ? -9.431  53.356 66.766 1.00 11.52 ? 41  ARG B CB  1 
ATOM   2243 C CG  . ARG B 1 47  ? -9.918  54.018 65.546 1.00 6.08  ? 41  ARG B CG  1 
ATOM   2244 C CD  . ARG B 1 47  ? -9.001  53.732 64.366 1.00 9.24  ? 41  ARG B CD  1 
ATOM   2245 N NE  . ARG B 1 47  ? -9.034  54.868 63.472 1.00 30.17 ? 41  ARG B NE  1 
ATOM   2246 C CZ  . ARG B 1 47  ? -9.854  54.974 62.441 1.00 26.39 ? 41  ARG B CZ  1 
ATOM   2247 N NH1 . ARG B 1 47  ? -10.463 53.899 61.959 1.00 2.00  ? 41  ARG B NH1 1 
ATOM   2248 N NH2 . ARG B 1 47  ? -9.939  56.133 61.813 1.00 2.00  ? 41  ARG B NH2 1 
ATOM   2249 N N   . ILE B 1 48  ? -9.766  52.179 69.696 1.00 14.53 ? 42  ILE B N   1 
ATOM   2250 C CA  . ILE B 1 48  ? -10.173 51.140 70.643 1.00 2.00  ? 42  ILE B CA  1 
ATOM   2251 C C   . ILE B 1 48  ? -11.234 51.684 71.602 1.00 8.16  ? 42  ILE B C   1 
ATOM   2252 O O   . ILE B 1 48  ? -12.316 51.106 71.685 1.00 20.61 ? 42  ILE B O   1 
ATOM   2253 C CB  . ILE B 1 48  ? -8.954  50.563 71.420 1.00 40.96 ? 42  ILE B CB  1 
ATOM   2254 C CG1 . ILE B 1 48  ? -8.019  49.822 70.455 1.00 7.43  ? 42  ILE B CG1 1 
ATOM   2255 C CG2 . ILE B 1 48  ? -9.412  49.554 72.450 1.00 5.86  ? 42  ILE B CG2 1 
ATOM   2256 C CD1 . ILE B 1 48  ? -6.690  49.481 71.033 1.00 6.13  ? 42  ILE B CD1 1 
ATOM   2257 N N   . CYS B 1 49  ? -11.066 52.948 71.999 1.00 9.06  ? 43  CYS B N   1 
ATOM   2258 C CA  . CYS B 1 49  ? -12.013 53.664 72.874 1.00 9.27  ? 43  CYS B CA  1 
ATOM   2259 C C   . CYS B 1 49  ? -13.366 54.037 72.237 1.00 35.91 ? 43  CYS B C   1 
ATOM   2260 O O   . CYS B 1 49  ? -14.402 54.042 72.905 1.00 30.30 ? 43  CYS B O   1 
ATOM   2261 C CB  . CYS B 1 49  ? -11.343 54.941 73.402 1.00 30.74 ? 43  CYS B CB  1 
ATOM   2262 S SG  . CYS B 1 49  ? -12.298 55.858 74.654 1.00 16.61 ? 43  CYS B SG  1 
ATOM   2263 N N   . ILE B 1 50  ? -13.311 54.490 70.990 1.00 5.50  ? 44  ILE B N   1 
ATOM   2264 C CA  . ILE B 1 50  ? -14.483 54.904 70.226 1.00 7.53  ? 44  ILE B CA  1 
ATOM   2265 C C   . ILE B 1 50  ? -15.305 53.697 69.811 1.00 32.06 ? 44  ILE B C   1 
ATOM   2266 O O   . ILE B 1 50  ? -16.550 53.747 69.696 1.00 16.91 ? 44  ILE B O   1 
ATOM   2267 C CB  . ILE B 1 50  ? -14.032 55.684 68.941 1.00 5.01  ? 44  ILE B CB  1 
ATOM   2268 C CG1 . ILE B 1 50  ? -13.438 57.053 69.342 1.00 18.87 ? 44  ILE B CG1 1 
ATOM   2269 C CG2 . ILE B 1 50  ? -15.171 55.813 67.947 1.00 2.00  ? 44  ILE B CG2 1 
ATOM   2270 C CD1 . ILE B 1 50  ? -12.467 57.666 68.335 1.00 12.31 ? 44  ILE B CD1 1 
ATOM   2271 N N   . HIS B 1 51  ? -14.597 52.632 69.470 1.00 7.13  ? 45  HIS B N   1 
ATOM   2272 C CA  . HIS B 1 51  ? -15.270 51.488 68.883 1.00 2.00  ? 45  HIS B CA  1 
ATOM   2273 C C   . HIS B 1 51  ? -15.964 50.592 69.910 1.00 11.77 ? 45  HIS B C   1 
ATOM   2274 O O   . HIS B 1 51  ? -17.129 50.256 69.722 1.00 30.04 ? 45  HIS B O   1 
ATOM   2275 C CB  . HIS B 1 51  ? -14.316 50.709 67.974 1.00 43.75 ? 45  HIS B CB  1 
ATOM   2276 C CG  . HIS B 1 51  ? -14.101 51.370 66.644 1.00 38.66 ? 45  HIS B CG  1 
ATOM   2277 N ND1 . HIS B 1 51  ? -15.033 51.295 65.634 1.00 48.27 ? 45  HIS B ND1 1 
ATOM   2278 C CD2 . HIS B 1 51  ? -13.219 52.329 66.264 1.00 77.86 ? 45  HIS B CD2 1 
ATOM   2279 C CE1 . HIS B 1 51  ? -14.755 52.196 64.705 1.00 78.69 ? 45  HIS B CE1 1 
ATOM   2280 N NE2 . HIS B 1 51  ? -13.662 52.837 65.069 1.00 15.64 ? 45  HIS B NE2 1 
ATOM   2281 N N   . THR B 1 52  ? -15.338 50.364 71.063 1.00 29.44 ? 46  THR B N   1 
ATOM   2282 C CA  . THR B 1 52  ? -16.047 49.729 72.172 1.00 23.19 ? 46  THR B CA  1 
ATOM   2283 C C   . THR B 1 52  ? -16.947 50.710 72.934 1.00 6.96  ? 46  THR B C   1 
ATOM   2284 O O   . THR B 1 52  ? -17.407 50.400 74.031 1.00 59.06 ? 46  THR B O   1 
ATOM   2285 C CB  . THR B 1 52  ? -15.085 49.086 73.187 1.00 2.45  ? 46  THR B CB  1 
ATOM   2286 O OG1 . THR B 1 52  ? -14.194 50.082 73.688 1.00 19.30 ? 46  THR B OG1 1 
ATOM   2287 C CG2 . THR B 1 52  ? -14.302 47.960 72.549 1.00 4.40  ? 46  THR B CG2 1 
ATOM   2288 N N   . ASN B 1 53  ? -17.161 51.904 72.385 1.00 38.92 ? 47  ASN B N   1 
ATOM   2289 C CA  . ASN B 1 53  ? -18.145 52.835 72.932 1.00 48.60 ? 47  ASN B CA  1 
ATOM   2290 C C   . ASN B 1 53  ? -17.802 53.347 74.330 1.00 44.36 ? 47  ASN B C   1 
ATOM   2291 O O   . ASN B 1 53  ? -18.649 53.911 75.023 1.00 69.37 ? 47  ASN B O   1 
ATOM   2292 C CB  . ASN B 1 53  ? -19.529 52.176 72.950 1.00 45.07 ? 47  ASN B CB  1 
ATOM   2293 C CG  . ASN B 1 53  ? -20.368 52.558 71.752 1.00 93.59 ? 47  ASN B CG  1 
ATOM   2294 O OD1 . ASN B 1 53  ? -20.207 53.640 71.186 1.00 28.92 ? 47  ASN B OD1 1 
ATOM   2295 N ND2 . ASN B 1 53  ? -21.277 51.678 71.363 1.00 64.14 ? 47  ASN B ND2 1 
ATOM   2296 N N   . GLY B 1 54  ? -16.542 53.203 74.714 1.00 38.18 ? 48  GLY B N   1 
ATOM   2297 C CA  . GLY B 1 54  ? -16.148 53.541 76.068 1.00 6.02  ? 48  GLY B CA  1 
ATOM   2298 C C   . GLY B 1 54  ? -15.555 52.367 76.822 1.00 21.79 ? 48  GLY B C   1 
ATOM   2299 O O   . GLY B 1 54  ? -14.582 52.511 77.570 1.00 36.35 ? 48  GLY B O   1 
ATOM   2300 N N   . ARG B 1 55  ? -16.039 51.180 76.476 1.00 15.68 ? 49  ARG B N   1 
ATOM   2301 C CA  . ARG B 1 55  ? -15.818 49.980 77.262 1.00 64.48 ? 49  ARG B CA  1 
ATOM   2302 C C   . ARG B 1 55  ? -14.344 49.758 77.530 1.00 3.19  ? 49  ARG B C   1 
ATOM   2303 O O   . ARG B 1 55  ? -13.934 49.716 78.688 1.00 51.90 ? 49  ARG B O   1 
ATOM   2304 C CB  . ARG B 1 55  ? -16.437 48.760 76.557 1.00 26.48 ? 49  ARG B CB  1 
ATOM   2305 C CG  . ARG B 1 55  ? -17.866 48.453 76.998 1.00 69.08 ? 49  ARG B CG  1 
ATOM   2306 C CD  . ARG B 1 55  ? -18.826 48.187 75.815 1.00 65.02 ? 49  ARG B CD  1 
ATOM   2307 N NE  . ARG B 1 55  ? -18.324 47.249 74.795 1.00 38.39 ? 49  ARG B NE  1 
ATOM   2308 C CZ  . ARG B 1 55  ? -17.876 46.010 75.024 1.00 79.15 ? 49  ARG B CZ  1 
ATOM   2309 N NH1 . ARG B 1 55  ? -17.589 45.582 76.258 1.00 33.39 ? 49  ARG B NH1 1 
ATOM   2310 N NH2 . ARG B 1 55  ? -17.603 45.223 73.997 1.00 25.07 ? 49  ARG B NH2 1 
ATOM   2311 N N   . VAL B 1 56  ? -13.542 49.640 76.474 1.00 49.52 ? 50  VAL B N   1 
ATOM   2312 C CA  . VAL B 1 56  ? -12.093 49.437 76.609 1.00 2.00  ? 50  VAL B CA  1 
ATOM   2313 C C   . VAL B 1 56  ? -11.358 50.767 76.488 1.00 47.13 ? 50  VAL B C   1 
ATOM   2314 O O   . VAL B 1 56  ? -11.459 51.450 75.469 1.00 41.47 ? 50  VAL B O   1 
ATOM   2315 C CB  . VAL B 1 56  ? -11.510 48.506 75.501 1.00 74.42 ? 50  VAL B CB  1 
ATOM   2316 C CG1 . VAL B 1 56  ? -9.980  48.338 75.686 1.00 8.72  ? 50  VAL B CG1 1 
ATOM   2317 C CG2 . VAL B 1 56  ? -12.199 47.156 75.523 1.00 53.05 ? 50  VAL B CG2 1 
ATOM   2318 N N   . ASN B 1 57  ? -10.499 51.054 77.454 1.00 11.32 ? 51  ASN B N   1 
ATOM   2319 C CA  . ASN B 1 57  ? -9.683  52.252 77.377 1.00 25.57 ? 51  ASN B CA  1 
ATOM   2320 C C   . ASN B 1 57  ? -8.232  51.978 77.745 1.00 2.00  ? 51  ASN B C   1 
ATOM   2321 O O   . ASN B 1 57  ? -7.893  51.777 78.909 1.00 54.98 ? 51  ASN B O   1 
ATOM   2322 C CB  . ASN B 1 57  ? -10.259 53.362 78.260 1.00 54.90 ? 51  ASN B CB  1 
ATOM   2323 C CG  . ASN B 1 57  ? -9.653  54.719 77.950 1.00 72.46 ? 51  ASN B CG  1 
ATOM   2324 O OD1 . ASN B 1 57  ? -9.918  55.303 76.902 1.00 84.93 ? 51  ASN B OD1 1 
ATOM   2325 N ND2 . ASN B 1 57  ? -8.766  55.184 78.815 1.00 20.02 ? 51  ASN B ND2 1 
ATOM   2326 N N   . VAL B 1 58  ? -7.372  52.007 76.728 1.00 39.90 ? 52  VAL B N   1 
ATOM   2327 C CA  . VAL B 1 58  ? -5.942  51.731 76.901 1.00 2.00  ? 52  VAL B CA  1 
ATOM   2328 C C   . VAL B 1 58  ? -5.072  52.675 76.118 1.00 2.00  ? 52  VAL B C   1 
ATOM   2329 O O   . VAL B 1 58  ? -5.476  53.184 75.086 1.00 8.66  ? 52  VAL B O   1 
ATOM   2330 C CB  . VAL B 1 58  ? -5.565  50.276 76.473 1.00 15.98 ? 52  VAL B CB  1 
ATOM   2331 C CG1 . VAL B 1 58  ? -6.068  49.280 77.517 1.00 57.86 ? 52  VAL B CG1 1 
ATOM   2332 C CG2 . VAL B 1 58  ? -6.144  49.953 75.095 1.00 59.50 ? 52  VAL B CG2 1 
ATOM   2333 N N   . GLU B 1 59  ? -3.950  53.044 76.720 1.00 9.11  ? 53  GLU B N   1 
ATOM   2334 C CA  . GLU B 1 59  ? -2.795  53.541 75.965 1.00 15.27 ? 53  GLU B CA  1 
ATOM   2335 C C   . GLU B 1 59  ? -2.045  52.372 75.313 1.00 56.84 ? 53  GLU B C   1 
ATOM   2336 O O   . GLU B 1 59  ? -1.335  51.623 75.991 1.00 11.29 ? 53  GLU B O   1 
ATOM   2337 C CB  . GLU B 1 59  ? -1.833  54.289 76.896 1.00 13.44 ? 53  GLU B CB  1 
ATOM   2338 C CG  . GLU B 1 59  ? -2.261  55.734 77.262 1.00 13.79 ? 53  GLU B CG  1 
ATOM   2339 C CD  . GLU B 1 59  ? -1.354  56.342 78.309 1.00 95.70 ? 53  GLU B CD  1 
ATOM   2340 O OE1 . GLU B 1 59  ? -0.188  56.636 77.971 1.00 7.91  ? 53  GLU B OE1 1 
ATOM   2341 O OE2 . GLU B 1 59  ? -1.783  56.472 79.478 1.00 94.67 ? 53  GLU B OE2 1 
ATOM   2342 N N   . VAL B 1 60  ? -2.236  52.198 74.009 1.00 19.05 ? 54  VAL B N   1 
ATOM   2343 C CA  . VAL B 1 60  ? -1.487  51.215 73.215 1.00 35.39 ? 54  VAL B CA  1 
ATOM   2344 C C   . VAL B 1 60  ? -0.001  51.597 73.238 1.00 2.00  ? 54  VAL B C   1 
ATOM   2345 O O   . VAL B 1 60  ? 0.326   52.778 73.122 1.00 2.00  ? 54  VAL B O   1 
ATOM   2346 C CB  . VAL B 1 60  ? -1.998  51.210 71.744 1.00 6.23  ? 54  VAL B CB  1 
ATOM   2347 C CG1 . VAL B 1 60  ? -1.238  50.204 70.916 1.00 2.00  ? 54  VAL B CG1 1 
ATOM   2348 C CG2 . VAL B 1 60  ? -3.487  50.975 71.707 1.00 2.00  ? 54  VAL B CG2 1 
ATOM   2349 N N   . SER B 1 61  ? 0.871   50.614 73.448 1.00 2.00  ? 55  SER B N   1 
ATOM   2350 C CA  . SER B 1 61  ? 2.306   50.837 73.612 1.00 2.00  ? 55  SER B CA  1 
ATOM   2351 C C   . SER B 1 61  ? 3.070   51.238 72.363 1.00 18.79 ? 55  SER B C   1 
ATOM   2352 O O   . SER B 1 61  ? 3.329   50.402 71.488 1.00 11.46 ? 55  SER B O   1 
ATOM   2353 C CB  . SER B 1 61  ? 2.951   49.585 74.175 1.00 2.00  ? 55  SER B CB  1 
ATOM   2354 O OG  . SER B 1 61  ? 4.340   49.752 74.366 1.00 8.38  ? 55  SER B OG  1 
ATOM   2355 N N   . ALA B 1 62  ? 3.693   52.408 72.421 1.00 6.82  ? 56  ALA B N   1 
ATOM   2356 C CA  . ALA B 1 62  ? 4.670   52.782 71.397 1.00 2.35  ? 56  ALA B CA  1 
ATOM   2357 C C   . ALA B 1 62  ? 5.900   51.885 71.404 1.00 12.53 ? 56  ALA B C   1 
ATOM   2358 O O   . ALA B 1 62  ? 6.506   51.636 70.368 1.00 30.12 ? 56  ALA B O   1 
ATOM   2359 C CB  . ALA B 1 62  ? 5.088   54.197 71.577 1.00 2.00  ? 56  ALA B CB  1 
ATOM   2360 N N   . GLU B 1 63  ? 6.238   51.366 72.571 1.00 12.92 ? 57  GLU B N   1 
ATOM   2361 C CA  . GLU B 1 63  ? 7.470   50.626 72.755 1.00 28.34 ? 57  GLU B CA  1 
ATOM   2362 C C   . GLU B 1 63  ? 7.406   49.315 71.998 1.00 30.39 ? 57  GLU B C   1 
ATOM   2363 O O   . GLU B 1 63  ? 8.399   48.828 71.451 1.00 2.00  ? 57  GLU B O   1 
ATOM   2364 C CB  . GLU B 1 63  ? 7.651   50.334 74.234 1.00 32.13 ? 57  GLU B CB  1 
ATOM   2365 C CG  . GLU B 1 63  ? 8.943   49.658 74.538 1.00 2.02  ? 57  GLU B CG  1 
ATOM   2366 C CD  . GLU B 1 63  ? 10.108  50.614 74.584 1.00 2.00  ? 57  GLU B CD  1 
ATOM   2367 O OE1 . GLU B 1 63  ? 9.918   51.848 74.541 1.00 11.84 ? 57  GLU B OE1 1 
ATOM   2368 O OE2 . GLU B 1 63  ? 11.230  50.118 74.721 1.00 12.55 ? 57  GLU B OE2 1 
ATOM   2369 N N   . ASP B 1 64  ? 6.242   48.690 72.077 1.00 10.86 ? 58  ASP B N   1 
ATOM   2370 C CA  . ASP B 1 64  ? 6.030   47.390 71.463 1.00 5.13  ? 58  ASP B CA  1 
ATOM   2371 C C   . ASP B 1 64  ? 6.175   47.466 69.946 1.00 17.31 ? 58  ASP B C   1 
ATOM   2372 O O   . ASP B 1 64  ? 6.939   46.691 69.375 1.00 2.53  ? 58  ASP B O   1 
ATOM   2373 C CB  . ASP B 1 64  ? 4.649   46.857 71.837 1.00 2.00  ? 58  ASP B CB  1 
ATOM   2374 C CG  . ASP B 1 64  ? 4.485   45.401 71.535 1.00 4.71  ? 58  ASP B CG  1 
ATOM   2375 O OD1 . ASP B 1 64  ? 5.497   44.664 71.500 1.00 3.42  ? 58  ASP B OD1 1 
ATOM   2376 O OD2 . ASP B 1 64  ? 3.322   44.966 71.451 1.00 2.00  ? 58  ASP B OD2 1 
ATOM   2377 N N   . LEU B 1 65  ? 5.431   48.385 69.316 1.00 2.00  ? 59  LEU B N   1 
ATOM   2378 C CA  . LEU B 1 65  ? 5.539   48.689 67.885 1.00 11.93 ? 59  LEU B CA  1 
ATOM   2379 C C   . LEU B 1 65  ? 6.964   48.985 67.403 1.00 35.36 ? 59  LEU B C   1 
ATOM   2380 O O   . LEU B 1 65  ? 7.446   48.437 66.413 1.00 23.59 ? 59  LEU B O   1 
ATOM   2381 C CB  . LEU B 1 65  ? 4.650   49.893 67.547 1.00 14.44 ? 59  LEU B CB  1 
ATOM   2382 C CG  . LEU B 1 65  ? 4.336   50.118 66.066 1.00 53.70 ? 59  LEU B CG  1 
ATOM   2383 C CD1 . LEU B 1 65  ? 3.991   48.787 65.435 1.00 3.39  ? 59  LEU B CD1 1 
ATOM   2384 C CD2 . LEU B 1 65  ? 3.180   51.104 65.904 1.00 37.36 ? 59  LEU B CD2 1 
ATOM   2385 N N   . LEU B 1 66  ? 7.628   49.863 68.130 1.00 4.05  ? 60  LEU B N   1 
ATOM   2386 C CA  . LEU B 1 66  ? 8.874   50.441 67.705 1.00 2.00  ? 60  LEU B CA  1 
ATOM   2387 C C   . LEU B 1 66  ? 9.940   49.374 67.666 1.00 42.78 ? 60  LEU B C   1 
ATOM   2388 O O   . LEU B 1 66  ? 10.713  49.292 66.693 1.00 4.36  ? 60  LEU B O   1 
ATOM   2389 C CB  . LEU B 1 66  ? 9.280   51.534 68.679 1.00 8.78  ? 60  LEU B CB  1 
ATOM   2390 C CG  . LEU B 1 66  ? 10.744  51.946 68.573 1.00 36.18 ? 60  LEU B CG  1 
ATOM   2391 C CD1 . LEU B 1 66  ? 10.964  52.540 67.182 1.00 5.21  ? 60  LEU B CD1 1 
ATOM   2392 C CD2 . LEU B 1 66  ? 11.087  52.941 69.671 1.00 19.82 ? 60  LEU B CD2 1 
ATOM   2393 N N   . THR B 1 67  ? 9.953   48.561 68.723 1.00 6.25  ? 61  THR B N   1 
ATOM   2394 C CA  . THR B 1 67  ? 11.020  47.606 68.977 1.00 22.39 ? 61  THR B CA  1 
ATOM   2395 C C   . THR B 1 67  ? 10.721  46.194 68.453 1.00 36.53 ? 61  THR B C   1 
ATOM   2396 O O   . THR B 1 67  ? 11.643  45.493 68.045 1.00 2.21  ? 61  THR B O   1 
ATOM   2397 C CB  . THR B 1 67  ? 11.374  47.525 70.501 1.00 2.00  ? 61  THR B CB  1 
ATOM   2398 O OG1 . THR B 1 67  ? 10.438  46.679 71.174 1.00 9.36  ? 61  THR B OG1 1 
ATOM   2399 C CG2 . THR B 1 67  ? 11.350  48.898 71.139 1.00 2.44  ? 61  THR B CG2 1 
ATOM   2400 N N   . CYS B 1 68  ? 9.444   45.805 68.371 1.00 13.14 ? 62  CYS B N   1 
ATOM   2401 C CA  . CYS B 1 68  ? 9.102   44.414 68.020 1.00 14.03 ? 62  CYS B CA  1 
ATOM   2402 C C   . CYS B 1 68  ? 8.546   44.195 66.620 1.00 40.93 ? 62  CYS B C   1 
ATOM   2403 O O   . CYS B 1 68  ? 8.381   43.050 66.190 1.00 14.90 ? 62  CYS B O   1 
ATOM   2404 C CB  . CYS B 1 68  ? 8.130   43.816 69.053 1.00 8.22  ? 62  CYS B CB  1 
ATOM   2405 S SG  . CYS B 1 68  ? 8.837   43.536 70.707 1.00 15.92 ? 62  CYS B SG  1 
ATOM   2406 N N   . CYS B 1 69  ? 8.230   45.273 65.910 1.00 2.00  ? 63  CYS B N   1 
ATOM   2407 C CA  . CYS B 1 69  ? 7.641   45.131 64.582 1.00 23.44 ? 63  CYS B CA  1 
ATOM   2408 C C   . CYS B 1 69  ? 8.606   44.636 63.537 1.00 13.63 ? 63  CYS B C   1 
ATOM   2409 O O   . CYS B 1 69  ? 8.228   43.817 62.683 1.00 28.22 ? 63  CYS B O   1 
ATOM   2410 C CB  . CYS B 1 69  ? 7.020   46.417 64.061 1.00 6.72  ? 63  CYS B CB  1 
ATOM   2411 S SG  . CYS B 1 69  ? 6.437   46.160 62.367 1.00 9.18  ? 63  CYS B SG  1 
ATOM   2412 N N   . GLY B 1 70  ? 9.830   45.150 63.557 1.00 2.00  ? 64  GLY B N   1 
ATOM   2413 C CA  . GLY B 1 70  ? 10.820  44.656 62.613 1.00 29.00 ? 64  GLY B CA  1 
ATOM   2414 C C   . GLY B 1 70  ? 10.804  45.267 61.220 1.00 24.14 ? 64  GLY B C   1 
ATOM   2415 O O   . GLY B 1 70  ? 10.455  46.433 61.043 1.00 13.49 ? 64  GLY B O   1 
ATOM   2416 N N   . ILE B 1 71  ? 11.146  44.464 60.217 1.00 23.63 ? 65  ILE B N   1 
ATOM   2417 C CA  . ILE B 1 71  ? 11.493  44.993 58.886 1.00 22.09 ? 65  ILE B CA  1 
ATOM   2418 C C   . ILE B 1 71  ? 10.291  45.485 58.050 1.00 14.60 ? 65  ILE B C   1 
ATOM   2419 O O   . ILE B 1 71  ? 10.405  46.461 57.292 1.00 21.61 ? 65  ILE B O   1 
ATOM   2420 C CB  . ILE B 1 71  ? 12.353  43.957 58.100 1.00 11.75 ? 65  ILE B CB  1 
ATOM   2421 C CG1 . ILE B 1 71  ? 12.842  44.550 56.772 1.00 71.10 ? 65  ILE B CG1 1 
ATOM   2422 C CG2 . ILE B 1 71  ? 11.587  42.675 57.915 1.00 17.48 ? 65  ILE B CG2 1 
ATOM   2423 C CD1 . ILE B 1 71  ? 11.945  44.268 55.556 1.00 18.86 ? 65  ILE B CD1 1 
ATOM   2424 N N   . GLN B 1 72  ? 9.132   44.860 58.256 1.00 2.00  ? 66  GLN B N   1 
ATOM   2425 C CA  . GLN B 1 72  ? 7.879   45.304 57.647 1.00 3.48  ? 66  GLN B CA  1 
ATOM   2426 C C   . GLN B 1 72  ? 7.519   46.776 58.005 1.00 3.31  ? 66  GLN B C   1 
ATOM   2427 O O   . GLN B 1 72  ? 6.692   47.414 57.344 1.00 8.30  ? 66  GLN B O   1 
ATOM   2428 C CB  . GLN B 1 72  ? 6.767   44.338 58.080 1.00 5.58  ? 66  GLN B CB  1 
ATOM   2429 C CG  . GLN B 1 72  ? 5.347   44.722 57.735 1.00 66.77 ? 66  GLN B CG  1 
ATOM   2430 C CD  . GLN B 1 72  ? 4.315   43.963 58.573 1.00 54.84 ? 66  GLN B CD  1 
ATOM   2431 O OE1 . GLN B 1 72  ? 4.655   43.242 59.516 1.00 36.13 ? 66  GLN B OE1 1 
ATOM   2432 N NE2 . GLN B 1 72  ? 3.045   44.166 58.260 1.00 33.30 ? 66  GLN B NE2 1 
ATOM   2433 N N   . CYS B 1 73  ? 8.050   47.264 59.125 1.00 29.80 ? 67  CYS B N   1 
ATOM   2434 C CA  . CYS B 1 73  ? 7.752   48.627 59.561 1.00 3.35  ? 67  CYS B CA  1 
ATOM   2435 C C   . CYS B 1 73  ? 8.839   49.613 59.184 1.00 2.00  ? 67  CYS B C   1 
ATOM   2436 O O   . CYS B 1 73  ? 8.620   50.805 59.265 1.00 33.18 ? 67  CYS B O   1 
ATOM   2437 C CB  . CYS B 1 73  ? 7.525   48.693 61.081 1.00 2.00  ? 67  CYS B CB  1 
ATOM   2438 S SG  . CYS B 1 73  ? 5.938   47.993 61.645 1.00 12.15 ? 67  CYS B SG  1 
ATOM   2439 N N   . GLY B 1 74  ? 10.060  49.122 59.006 1.00 5.00  ? 68  GLY B N   1 
ATOM   2440 C CA  . GLY B 1 74  ? 11.154  50.007 58.665 1.00 16.53 ? 68  GLY B CA  1 
ATOM   2441 C C   . GLY B 1 74  ? 12.454  49.735 59.378 1.00 10.35 ? 68  GLY B C   1 
ATOM   2442 O O   . GLY B 1 74  ? 12.902  48.593 59.463 1.00 28.82 ? 68  GLY B O   1 
ATOM   2443 N N   . ASP B 1 75  ? 13.120  50.820 59.755 1.00 6.81  ? 69  ASP B N   1 
ATOM   2444 C CA  . ASP B 1 75  ? 14.333  50.778 60.562 1.00 4.39  ? 69  ASP B CA  1 
ATOM   2445 C C   . ASP B 1 75  ? 14.119  51.409 61.942 1.00 23.16 ? 69  ASP B C   1 
ATOM   2446 O O   . ASP B 1 75  ? 14.979  52.137 62.448 1.00 15.03 ? 69  ASP B O   1 
ATOM   2447 C CB  . ASP B 1 75  ? 15.470  51.504 59.835 1.00 17.30 ? 69  ASP B CB  1 
ATOM   2448 C CG  . ASP B 1 75  ? 16.855  51.114 60.356 1.00 24.51 ? 69  ASP B CG  1 
ATOM   2449 O OD1 . ASP B 1 75  ? 16.961  50.475 61.438 1.00 71.80 ? 69  ASP B OD1 1 
ATOM   2450 O OD2 . ASP B 1 75  ? 17.849  51.410 59.642 1.00 29.64 ? 69  ASP B OD2 1 
ATOM   2451 N N   . GLY B 1 76  ? 13.023  51.052 62.594 1.00 20.87 ? 70  GLY B N   1 
ATOM   2452 C CA  . GLY B 1 76  ? 12.796  51.528 63.953 1.00 25.85 ? 70  GLY B CA  1 
ATOM   2453 C C   . GLY B 1 76  ? 13.090  53.009 64.184 1.00 11.68 ? 70  GLY B C   1 
ATOM   2454 O O   . GLY B 1 76  ? 12.397  53.882 63.649 1.00 10.92 ? 70  GLY B O   1 
ATOM   2455 N N   . CYS B 1 77  ? 14.128  53.294 64.970 1.00 3.25  ? 71  CYS B N   1 
ATOM   2456 C CA  . CYS B 1 77  ? 14.409  54.655 65.392 1.00 14.70 ? 71  CYS B CA  1 
ATOM   2457 C C   . CYS B 1 77  ? 14.924  55.517 64.236 1.00 58.37 ? 71  CYS B C   1 
ATOM   2458 O O   . CYS B 1 77  ? 14.935  56.725 64.330 1.00 14.19 ? 71  CYS B O   1 
ATOM   2459 C CB  . CYS B 1 77  ? 15.431  54.664 66.540 1.00 46.43 ? 71  CYS B CB  1 
ATOM   2460 S SG  . CYS B 1 77  ? 14.735  54.663 68.227 1.00 13.05 ? 71  CYS B SG  1 
ATOM   2461 N N   . ASN B 1 78  ? 15.316  54.889 63.134 1.00 3.59  ? 72  ASN B N   1 
ATOM   2462 C CA  . ASN B 1 78  ? 15.766  55.592 61.941 1.00 2.00  ? 72  ASN B CA  1 
ATOM   2463 C C   . ASN B 1 78  ? 14.629  55.949 60.986 1.00 13.08 ? 72  ASN B C   1 
ATOM   2464 O O   . ASN B 1 78  ? 14.845  56.553 59.940 1.00 56.29 ? 72  ASN B O   1 
ATOM   2465 C CB  . ASN B 1 78  ? 16.801  54.731 61.221 1.00 9.44  ? 72  ASN B CB  1 
ATOM   2466 C CG  . ASN B 1 78  ? 17.991  54.409 62.096 1.00 83.80 ? 72  ASN B CG  1 
ATOM   2467 O OD1 . ASN B 1 78  ? 18.838  55.257 62.331 1.00 19.85 ? 72  ASN B OD1 1 
ATOM   2468 N ND2 . ASN B 1 78  ? 18.030  53.200 62.629 1.00 71.54 ? 72  ASN B ND2 1 
ATOM   2469 N N   . GLY B 1 79  ? 13.446  55.440 61.295 1.00 16.89 ? 73  GLY B N   1 
ATOM   2470 C CA  . GLY B 1 79  ? 12.263  55.748 60.524 1.00 17.24 ? 73  GLY B CA  1 
ATOM   2471 C C   . GLY B 1 79  ? 11.569  54.492 60.053 1.00 24.71 ? 73  GLY B C   1 
ATOM   2472 O O   . GLY B 1 79  ? 12.147  53.399 60.058 1.00 29.56 ? 73  GLY B O   1 
ATOM   2473 N N   . GLY B 1 80  ? 10.341  54.654 59.592 1.00 2.22  ? 74  GLY B N   1 
ATOM   2474 C CA  . GLY B 1 80  ? 9.570   53.507 59.160 1.00 2.00  ? 74  GLY B CA  1 
ATOM   2475 C C   . GLY B 1 80  ? 8.320   53.877 58.391 1.00 2.76  ? 74  GLY B C   1 
ATOM   2476 O O   . GLY B 1 80  ? 8.159   55.039 57.994 1.00 27.99 ? 74  GLY B O   1 
ATOM   2477 N N   . TYR B 1 81  ? 7.386   52.930 58.300 1.00 2.36  ? 75  TYR B N   1 
ATOM   2478 C CA  . TYR B 1 81  ? 6.274   52.996 57.366 1.00 2.00  ? 75  TYR B CA  1 
ATOM   2479 C C   . TYR B 1 81  ? 4.958   52.770 58.110 1.00 2.00  ? 75  TYR B C   1 
ATOM   2480 O O   . TYR B 1 81  ? 4.659   51.659 58.552 1.00 2.70  ? 75  TYR B O   1 
ATOM   2481 C CB  . TYR B 1 81  ? 6.428   51.947 56.232 1.00 3.89  ? 75  TYR B CB  1 
ATOM   2482 C CG  . TYR B 1 81  ? 7.764   51.955 55.504 1.00 2.00  ? 75  TYR B CG  1 
ATOM   2483 C CD1 . TYR B 1 81  ? 8.197   53.085 54.788 1.00 16.87 ? 75  TYR B CD1 1 
ATOM   2484 C CD2 . TYR B 1 81  ? 8.692   50.939 55.731 1.00 6.02  ? 75  TYR B CD2 1 
ATOM   2485 C CE1 . TYR B 1 81  ? 9.521   53.204 54.350 1.00 2.00  ? 75  TYR B CE1 1 
ATOM   2486 C CE2 . TYR B 1 81  ? 10.009  51.050 55.312 1.00 2.00  ? 75  TYR B CE2 1 
ATOM   2487 C CZ  . TYR B 1 81  ? 10.418  52.168 54.635 1.00 6.00  ? 75  TYR B CZ  1 
ATOM   2488 O OH  . TYR B 1 81  ? 11.737  52.222 54.258 1.00 23.36 ? 75  TYR B OH  1 
ATOM   2489 N N   . PRO B 1 82  ? 4.122   53.816 58.201 1.00 8.58  ? 76  PRO B N   1 
ATOM   2490 C CA  . PRO B 1 82  ? 2.849   53.714 58.909 1.00 2.00  ? 76  PRO B CA  1 
ATOM   2491 C C   . PRO B 1 82  ? 2.028   52.460 58.593 1.00 11.16 ? 76  PRO B C   1 
ATOM   2492 O O   . PRO B 1 82  ? 1.611   51.743 59.497 1.00 49.16 ? 76  PRO B O   1 
ATOM   2493 C CB  . PRO B 1 82  ? 2.131   54.991 58.489 1.00 5.97  ? 76  PRO B CB  1 
ATOM   2494 C CG  . PRO B 1 82  ? 3.248   56.014 58.239 1.00 2.00  ? 76  PRO B CG  1 
ATOM   2495 C CD  . PRO B 1 82  ? 4.549   55.233 58.082 1.00 2.79  ? 76  PRO B CD  1 
ATOM   2496 N N   . SER B 1 83  ? 1.929   52.121 57.315 1.00 2.00  ? 77  SER B N   1 
ATOM   2497 C CA  . SER B 1 83  ? 1.057   51.036 56.855 1.00 7.44  ? 77  SER B CA  1 
ATOM   2498 C C   . SER B 1 83  ? 1.551   49.673 57.321 1.00 2.00  ? 77  SER B C   1 
ATOM   2499 O O   . SER B 1 83  ? 0.763   48.746 57.472 1.00 2.00  ? 77  SER B O   1 
ATOM   2500 C CB  . SER B 1 83  ? 0.977   51.033 55.334 1.00 21.24 ? 77  SER B CB  1 
ATOM   2501 O OG  . SER B 1 83  ? 2.216   50.600 54.794 1.00 40.95 ? 77  SER B OG  1 
ATOM   2502 N N   . GLY B 1 84  ? 2.838   49.584 57.640 1.00 2.00  ? 78  GLY B N   1 
ATOM   2503 C CA  . GLY B 1 84  ? 3.380   48.360 58.216 1.00 2.00  ? 78  GLY B CA  1 
ATOM   2504 C C   . GLY B 1 84  ? 3.092   48.264 59.710 1.00 20.43 ? 78  GLY B C   1 
ATOM   2505 O O   . GLY B 1 84  ? 2.889   47.176 60.231 1.00 5.75  ? 78  GLY B O   1 
ATOM   2506 N N   . ALA B 1 85  ? 2.972   49.412 60.375 1.00 32.37 ? 79  ALA B N   1 
ATOM   2507 C CA  . ALA B 1 85  ? 2.468   49.484 61.751 1.00 6.15  ? 79  ALA B CA  1 
ATOM   2508 C C   . ALA B 1 85  ? 1.029   48.946 61.887 1.00 10.42 ? 79  ALA B C   1 
ATOM   2509 O O   . ALA B 1 85  ? 0.795   47.985 62.586 1.00 2.00  ? 79  ALA B O   1 
ATOM   2510 C CB  . ALA B 1 85  ? 2.537   50.916 62.253 1.00 2.00  ? 79  ALA B CB  1 
ATOM   2511 N N   . TRP B 1 86  ? 0.084   49.485 61.126 1.00 2.00  ? 80  TRP B N   1 
ATOM   2512 C CA  . TRP B 1 86  ? -1.272  48.962 61.162 1.00 4.63  ? 80  TRP B CA  1 
ATOM   2513 C C   . TRP B 1 86  ? -1.474  47.512 60.687 1.00 3.50  ? 80  TRP B C   1 
ATOM   2514 O O   . TRP B 1 86  ? -2.403  46.821 61.129 1.00 9.06  ? 80  TRP B O   1 
ATOM   2515 C CB  . TRP B 1 86  ? -2.182  49.895 60.392 1.00 2.06  ? 80  TRP B CB  1 
ATOM   2516 C CG  . TRP B 1 86  ? -2.227  51.221 61.031 1.00 2.00  ? 80  TRP B CG  1 
ATOM   2517 C CD1 . TRP B 1 86  ? -1.282  52.219 60.956 1.00 2.00  ? 80  TRP B CD1 1 
ATOM   2518 C CD2 . TRP B 1 86  ? -3.322  51.757 61.765 1.00 10.04 ? 80  TRP B CD2 1 
ATOM   2519 N NE1 . TRP B 1 86  ? -1.766  53.356 61.539 1.00 4.52  ? 80  TRP B NE1 1 
ATOM   2520 C CE2 . TRP B 1 86  ? -3.017  53.104 62.041 1.00 17.66 ? 80  TRP B CE2 1 
ATOM   2521 C CE3 . TRP B 1 86  ? -4.539  51.238 62.202 1.00 2.00  ? 80  TRP B CE3 1 
ATOM   2522 C CZ2 . TRP B 1 86  ? -3.892  53.931 62.728 1.00 5.21  ? 80  TRP B CZ2 1 
ATOM   2523 C CZ3 . TRP B 1 86  ? -5.410  52.069 62.885 1.00 12.26 ? 80  TRP B CZ3 1 
ATOM   2524 C CH2 . TRP B 1 86  ? -5.080  53.392 63.144 1.00 2.00  ? 80  TRP B CH2 1 
ATOM   2525 N N   . ASN B 1 87  ? -0.536  47.015 59.885 1.00 9.13  ? 81  ASN B N   1 
ATOM   2526 C CA  . ASN B 1 87  ? -0.549  45.607 59.487 1.00 2.40  ? 81  ASN B CA  1 
ATOM   2527 C C   . ASN B 1 87  ? -0.134  44.720 60.628 1.00 31.34 ? 81  ASN B C   1 
ATOM   2528 O O   . ASN B 1 87  ? -0.821  43.745 60.948 1.00 12.06 ? 81  ASN B O   1 
ATOM   2529 C CB  . ASN B 1 87  ? 0.360   45.380 58.279 1.00 2.00  ? 81  ASN B CB  1 
ATOM   2530 C CG  . ASN B 1 87  ? -0.366  45.573 56.980 1.00 2.00  ? 81  ASN B CG  1 
ATOM   2531 O OD1 . ASN B 1 87  ? -1.556  45.893 56.951 1.00 86.27 ? 81  ASN B OD1 1 
ATOM   2532 N ND2 . ASN B 1 87  ? 0.368   45.463 55.884 1.00 20.96 ? 81  ASN B ND2 1 
ATOM   2533 N N   . PHE B 1 88  ? 0.961   45.109 61.269 1.00 2.00  ? 82  PHE B N   1 
ATOM   2534 C CA  . PHE B 1 88  ? 1.453   44.465 62.475 1.00 11.14 ? 82  PHE B CA  1 
ATOM   2535 C C   . PHE B 1 88  ? 0.352   44.278 63.533 1.00 29.42 ? 82  PHE B C   1 
ATOM   2536 O O   . PHE B 1 88  ? 0.120   43.192 64.071 1.00 3.03  ? 82  PHE B O   1 
ATOM   2537 C CB  . PHE B 1 88  ? 2.593   45.305 63.060 1.00 2.00  ? 82  PHE B CB  1 
ATOM   2538 C CG  . PHE B 1 88  ? 3.325   44.627 64.172 1.00 22.06 ? 82  PHE B CG  1 
ATOM   2539 C CD1 . PHE B 1 88  ? 4.118   43.542 63.919 1.00 2.00  ? 82  PHE B CD1 1 
ATOM   2540 C CD2 . PHE B 1 88  ? 3.292   45.129 65.446 1.00 10.38 ? 82  PHE B CD2 1 
ATOM   2541 C CE1 . PHE B 1 88  ? 4.875   42.978 64.913 1.00 18.29 ? 82  PHE B CE1 1 
ATOM   2542 C CE2 . PHE B 1 88  ? 4.049   44.568 66.440 1.00 27.17 ? 82  PHE B CE2 1 
ATOM   2543 C CZ  . PHE B 1 88  ? 4.841   43.497 66.173 1.00 13.64 ? 82  PHE B CZ  1 
ATOM   2544 N N   . TRP B 1 89  ? -0.347  45.358 63.799 1.00 2.00  ? 83  TRP B N   1 
ATOM   2545 C CA  . TRP B 1 89  ? -1.411  45.380 64.796 1.00 3.75  ? 83  TRP B CA  1 
ATOM   2546 C C   . TRP B 1 89  ? -2.459  44.313 64.455 1.00 5.35  ? 83  TRP B C   1 
ATOM   2547 O O   . TRP B 1 89  ? -2.726  43.418 65.253 1.00 20.86 ? 83  TRP B O   1 
ATOM   2548 C CB  . TRP B 1 89  ? -2.017  46.781 64.822 1.00 2.00  ? 83  TRP B CB  1 
ATOM   2549 C CG  . TRP B 1 89  ? -3.111  47.070 65.828 1.00 10.84 ? 83  TRP B CG  1 
ATOM   2550 C CD1 . TRP B 1 89  ? -3.066  46.922 67.194 1.00 2.00  ? 83  TRP B CD1 1 
ATOM   2551 C CD2 . TRP B 1 89  ? -4.339  47.739 65.544 1.00 49.93 ? 83  TRP B CD2 1 
ATOM   2552 N NE1 . TRP B 1 89  ? -4.201  47.458 67.767 1.00 14.30 ? 83  TRP B NE1 1 
ATOM   2553 C CE2 . TRP B 1 89  ? -5.001  47.963 66.774 1.00 2.00  ? 83  TRP B CE2 1 
ATOM   2554 C CE3 . TRP B 1 89  ? -4.941  48.181 64.367 1.00 2.00  ? 83  TRP B CE3 1 
ATOM   2555 C CZ2 . TRP B 1 89  ? -6.240  48.597 66.852 1.00 44.88 ? 83  TRP B CZ2 1 
ATOM   2556 C CZ3 . TRP B 1 89  ? -6.175  48.820 64.445 1.00 43.28 ? 83  TRP B CZ3 1 
ATOM   2557 C CH2 . TRP B 1 89  ? -6.812  49.019 65.677 1.00 27.02 ? 83  TRP B CH2 1 
ATOM   2558 N N   . THR B 1 90  ? -2.908  44.309 63.206 1.00 25.34 ? 84  THR B N   1 
ATOM   2559 C CA  . THR B 1 90  ? -3.926  43.366 62.759 1.00 2.00  ? 84  THR B CA  1 
ATOM   2560 C C   . THR B 1 90  ? -3.459  41.896 62.826 1.00 8.55  ? 84  THR B C   1 
ATOM   2561 O O   . THR B 1 90  ? -4.275  41.004 62.937 1.00 9.34  ? 84  THR B O   1 
ATOM   2562 C CB  . THR B 1 90  ? -4.412  43.719 61.325 1.00 34.49 ? 84  THR B CB  1 
ATOM   2563 O OG1 . THR B 1 90  ? -5.843  43.843 61.319 1.00 21.20 ? 84  THR B OG1 1 
ATOM   2564 C CG2 . THR B 1 90  ? -3.972  42.659 60.310 1.00 12.38 ? 84  THR B CG2 1 
ATOM   2565 N N   . ARG B 1 91  ? -2.149  41.663 62.888 1.00 2.00  ? 85  ARG B N   1 
ATOM   2566 C CA  . ARG B 1 91  ? -1.607  40.330 62.783 1.00 2.00  ? 85  ARG B CA  1 
ATOM   2567 C C   . ARG B 1 91  ? -1.003  39.900 64.079 1.00 6.34  ? 85  ARG B C   1 
ATOM   2568 O O   . ARG B 1 91  ? -1.461  38.942 64.670 1.00 19.21 ? 85  ARG B O   1 
ATOM   2569 C CB  . ARG B 1 91  ? -0.531  40.257 61.710 1.00 6.33  ? 85  ARG B CB  1 
ATOM   2570 C CG  . ARG B 1 91  ? -0.423  38.860 61.088 1.00 33.55 ? 85  ARG B CG  1 
ATOM   2571 C CD  . ARG B 1 91  ? -1.529  38.636 59.925 1.00 33.43 ? 85  ARG B CD  1 
ATOM   2572 N NE  . ARG B 1 91  ? -1.838  37.237 59.533 1.00 41.56 ? 85  ARG B NE  1 
ATOM   2573 C CZ  . ARG B 1 91  ? -1.017  36.420 58.866 1.00 90.12 ? 85  ARG B CZ  1 
ATOM   2574 N NH1 . ARG B 1 91  ? 0.290   36.690 58.826 1.00 13.13 ? 85  ARG B NH1 1 
ATOM   2575 N NH2 . ARG B 1 91  ? -1.483  35.269 58.349 1.00 11.79 ? 85  ARG B NH2 1 
ATOM   2576 N N   . LYS B 1 92  ? -0.016  40.655 64.551 1.00 2.57  ? 86  LYS B N   1 
ATOM   2577 C CA  . LYS B 1 92  ? 0.670   40.332 65.795 1.00 2.00  ? 86  LYS B CA  1 
ATOM   2578 C C   . LYS B 1 92  ? 0.182   41.063 67.071 1.00 42.74 ? 86  LYS B C   1 
ATOM   2579 O O   . LYS B 1 92  ? 0.573   40.685 68.187 1.00 8.53  ? 86  LYS B O   1 
ATOM   2580 C CB  . LYS B 1 92  ? 2.168   40.544 65.610 1.00 2.00  ? 86  LYS B CB  1 
ATOM   2581 C CG  . LYS B 1 92  ? 2.885   39.352 65.013 1.00 20.79 ? 86  LYS B CG  1 
ATOM   2582 C CD  . LYS B 1 92  ? 3.947   38.828 65.954 1.00 47.13 ? 86  LYS B CD  1 
ATOM   2583 C CE  . LYS B 1 92  ? 4.265   37.375 65.681 1.00 16.57 ? 86  LYS B CE  1 
ATOM   2584 N NZ  . LYS B 1 92  ? 5.195   36.836 66.720 1.00 75.79 ? 86  LYS B NZ  1 
ATOM   2585 N N   . GLY B 1 93  ? -0.690  42.064 66.916 1.00 2.00  ? 87  GLY B N   1 
ATOM   2586 C CA  . GLY B 1 93  ? -1.266  42.763 68.071 1.00 2.00  ? 87  GLY B CA  1 
ATOM   2587 C C   . GLY B 1 93  ? -0.328  43.759 68.726 1.00 5.47  ? 87  GLY B C   1 
ATOM   2588 O O   . GLY B 1 93  ? 0.878   43.671 68.515 1.00 2.00  ? 87  GLY B O   1 
ATOM   2589 N N   . LEU B 1 94  ? -0.841  44.701 69.522 1.00 6.65  ? 88  LEU B N   1 
ATOM   2590 C CA  . LEU B 1 94  ? 0.049   45.543 70.367 1.00 2.00  ? 88  LEU B CA  1 
ATOM   2591 C C   . LEU B 1 94  ? -0.352  45.586 71.843 1.00 5.56  ? 88  LEU B C   1 
ATOM   2592 O O   . LEU B 1 94  ? -1.551  45.608 72.171 1.00 2.49  ? 88  LEU B O   1 
ATOM   2593 C CB  . LEU B 1 94  ? 0.122   46.968 69.820 1.00 15.62 ? 88  LEU B CB  1 
ATOM   2594 C CG  . LEU B 1 94  ? 0.733   47.051 68.427 1.00 22.24 ? 88  LEU B CG  1 
ATOM   2595 C CD1 . LEU B 1 94  ? 0.288   48.338 67.716 1.00 2.00  ? 88  LEU B CD1 1 
ATOM   2596 C CD2 . LEU B 1 94  ? 2.263   46.927 68.560 1.00 14.86 ? 88  LEU B CD2 1 
ATOM   2597 N N   . VAL B 1 95  ? 0.640   45.469 72.727 1.00 10.03 ? 89  VAL B N   1 
ATOM   2598 C CA  . VAL B 1 95  ? 0.397   45.469 74.175 1.00 13.75 ? 89  VAL B CA  1 
ATOM   2599 C C   . VAL B 1 95  ? 0.251   46.897 74.693 1.00 25.44 ? 89  VAL B C   1 
ATOM   2600 O O   . VAL B 1 95  ? 0.591   47.856 73.998 1.00 17.14 ? 89  VAL B O   1 
ATOM   2601 C CB  . VAL B 1 95  ? 1.535   44.727 75.000 1.00 2.00  ? 89  VAL B CB  1 
ATOM   2602 C CG1 . VAL B 1 95  ? 1.597   43.282 74.632 1.00 2.00  ? 89  VAL B CG1 1 
ATOM   2603 C CG2 . VAL B 1 95  ? 2.895   45.361 74.799 1.00 2.00  ? 89  VAL B CG2 1 
ATOM   2604 N N   . SER B 1 96  ? -0.319  47.039 75.887 1.00 38.78 ? 90  SER B N   1 
ATOM   2605 C CA  . SER B 1 96  ? -0.466  48.350 76.501 1.00 2.00  ? 90  SER B CA  1 
ATOM   2606 C C   . SER B 1 96  ? 0.820   48.914 77.102 1.00 15.35 ? 90  SER B C   1 
ATOM   2607 O O   . SER B 1 96  ? 1.711   48.178 77.519 1.00 26.62 ? 90  SER B O   1 
ATOM   2608 C CB  . SER B 1 96  ? -1.617  48.346 77.534 1.00 15.44 ? 90  SER B CB  1 
ATOM   2609 O OG  . SER B 1 96  ? -1.175  48.119 78.861 1.00 15.73 ? 90  SER B OG  1 
ATOM   2610 N N   . GLY B 1 97  ? 0.994   50.215 76.913 1.00 15.51 ? 91  GLY B N   1 
ATOM   2611 C CA  . GLY B 1 97  ? 2.180   50.929 77.374 1.00 2.00  ? 91  GLY B CA  1 
ATOM   2612 C C   . GLY B 1 97  ? 1.810   52.400 77.430 1.00 2.00  ? 91  GLY B C   1 
ATOM   2613 O O   . GLY B 1 97  ? 1.112   52.871 76.545 1.00 4.07  ? 91  GLY B O   1 
ATOM   2614 N N   . GLY B 1 98  ? 1.935   52.985 78.615 1.00 11.57 ? 92  GLY B N   1 
ATOM   2615 C CA  . GLY B 1 98  ? 1.848   54.431 78.731 1.00 10.53 ? 92  GLY B CA  1 
ATOM   2616 C C   . GLY B 1 98  ? 3.177   55.160 78.532 1.00 2.72  ? 92  GLY B C   1 
ATOM   2617 O O   . GLY B 1 98  ? 4.198   54.523 78.252 1.00 9.50  ? 92  GLY B O   1 
ATOM   2618 N N   . VAL B 1 99  ? 3.208   56.440 78.895 1.00 2.00  ? 93  VAL B N   1 
ATOM   2619 C CA  . VAL B 1 99  ? 4.367   57.296 78.647 1.00 6.67  ? 93  VAL B CA  1 
ATOM   2620 C C   . VAL B 1 99  ? 5.582   57.017 79.555 1.00 24.26 ? 93  VAL B C   1 
ATOM   2621 O O   . VAL B 1 99  ? 5.495   56.296 80.549 1.00 2.00  ? 93  VAL B O   1 
ATOM   2622 C CB  . VAL B 1 99  ? 4.008   58.816 78.752 1.00 44.14 ? 93  VAL B CB  1 
ATOM   2623 C CG1 . VAL B 1 99  ? 2.663   59.106 78.066 1.00 27.21 ? 93  VAL B CG1 1 
ATOM   2624 C CG2 . VAL B 1 99  ? 3.988   59.256 80.209 1.00 12.04 ? 93  VAL B CG2 1 
ATOM   2625 N N   . TYR B 1 100 ? 6.671   57.730 79.307 1.00 26.03 ? 94  TYR B N   1 
ATOM   2626 C CA  . TYR B 1 100 ? 7.909   57.474 80.022 1.00 29.28 ? 94  TYR B CA  1 
ATOM   2627 C C   . TYR B 1 100 ? 7.782   57.671 81.536 1.00 75.23 ? 94  TYR B C   1 
ATOM   2628 O O   . TYR B 1 100 ? 7.308   58.697 81.982 1.00 2.00  ? 94  TYR B O   1 
ATOM   2629 C CB  . TYR B 1 100 ? 8.997   58.372 79.471 1.00 7.39  ? 94  TYR B CB  1 
ATOM   2630 C CG  . TYR B 1 100 ? 10.353  58.017 79.987 1.00 10.87 ? 94  TYR B CG  1 
ATOM   2631 C CD1 . TYR B 1 100 ? 11.088  56.993 79.422 1.00 27.79 ? 94  TYR B CD1 1 
ATOM   2632 C CD2 . TYR B 1 100 ? 10.920  58.748 81.003 1.00 19.09 ? 94  TYR B CD2 1 
ATOM   2633 C CE1 . TYR B 1 100 ? 12.359  56.723 79.853 1.00 19.63 ? 94  TYR B CE1 1 
ATOM   2634 C CE2 . TYR B 1 100 ? 12.177  58.486 81.443 1.00 24.71 ? 94  TYR B CE2 1 
ATOM   2635 C CZ  . TYR B 1 100 ? 12.903  57.486 80.868 1.00 47.79 ? 94  TYR B CZ  1 
ATOM   2636 O OH  . TYR B 1 100 ? 14.198  57.322 81.288 1.00 38.10 ? 94  TYR B OH  1 
ATOM   2637 N N   . ASN B 1 101 ? 8.224   56.677 82.305 1.00 2.00  ? 95  ASN B N   1 
ATOM   2638 C CA  . ASN B 1 101 ? 8.067   56.609 83.765 1.00 14.00 ? 95  ASN B CA  1 
ATOM   2639 C C   . ASN B 1 101 ? 6.621   56.616 84.306 1.00 2.00  ? 95  ASN B C   1 
ATOM   2640 O O   . ASN B 1 101 ? 6.390   56.924 85.470 1.00 51.29 ? 95  ASN B O   1 
ATOM   2641 C CB  . ASN B 1 101 ? 8.875   57.732 84.433 1.00 5.73  ? 95  ASN B CB  1 
ATOM   2642 C CG  . ASN B 1 101 ? 9.841   57.211 85.450 1.00 81.44 ? 95  ASN B CG  1 
ATOM   2643 O OD1 . ASN B 1 101 ? 9.542   57.174 86.643 1.00 39.54 ? 95  ASN B OD1 1 
ATOM   2644 N ND2 . ASN B 1 101 ? 10.999  56.762 84.986 1.00 92.25 ? 95  ASN B ND2 1 
ATOM   2645 N N   . SER B 1 102 ? 5.654   56.280 83.458 1.00 3.93  ? 96  SER B N   1 
ATOM   2646 C CA  . SER B 1 102 ? 4.250   56.155 83.882 1.00 79.15 ? 96  SER B CA  1 
ATOM   2647 C C   . SER B 1 102 ? 3.992   54.923 84.726 1.00 4.77  ? 96  SER B C   1 
ATOM   2648 O O   . SER B 1 102 ? 3.027   54.881 85.498 1.00 51.99 ? 96  SER B O   1 
ATOM   2649 C CB  . SER B 1 102 ? 3.292   56.095 82.684 1.00 5.95  ? 96  SER B CB  1 
ATOM   2650 O OG  . SER B 1 102 ? 3.569   54.979 81.854 1.00 18.70 ? 96  SER B OG  1 
ATOM   2651 N N   . HIS B 1 103 ? 4.843   53.913 84.576 1.00 38.30 ? 97  HIS B N   1 
ATOM   2652 C CA  . HIS B 1 103 ? 4.549   52.572 85.097 1.00 7.63  ? 97  HIS B CA  1 
ATOM   2653 C C   . HIS B 1 103 ? 3.098   52.183 84.891 1.00 2.57  ? 97  HIS B C   1 
ATOM   2654 O O   . HIS B 1 103 ? 2.461   51.625 85.783 1.00 33.22 ? 97  HIS B O   1 
ATOM   2655 C CB  . HIS B 1 103 ? 4.896   52.478 86.584 1.00 3.69  ? 97  HIS B CB  1 
ATOM   2656 C CG  . HIS B 1 103 ? 6.354   52.647 86.867 1.00 7.76  ? 97  HIS B CG  1 
ATOM   2657 N ND1 . HIS B 1 103 ? 7.210   51.578 86.964 1.00 9.74  ? 97  HIS B ND1 1 
ATOM   2658 C CD2 . HIS B 1 103 ? 7.125   53.759 86.933 1.00 59.48 ? 97  HIS B CD2 1 
ATOM   2659 C CE1 . HIS B 1 103 ? 8.453   52.016 87.053 1.00 4.89  ? 97  HIS B CE1 1 
ATOM   2660 N NE2 . HIS B 1 103 ? 8.429   53.334 87.044 1.00 8.60  ? 97  HIS B NE2 1 
ATOM   2661 N N   . ILE B 1 104 ? 2.551   52.573 83.743 1.00 4.65  ? 98  ILE B N   1 
ATOM   2662 C CA  . ILE B 1 104 ? 1.185   52.171 83.397 1.00 10.04 ? 98  ILE B CA  1 
ATOM   2663 C C   . ILE B 1 104 ? 1.264   51.145 82.266 1.00 17.19 ? 98  ILE B C   1 
ATOM   2664 O O   . ILE B 1 104 ? 2.054   51.308 81.344 1.00 3.36  ? 98  ILE B O   1 
ATOM   2665 C CB  . ILE B 1 104 ? 0.334   53.384 82.927 1.00 39.07 ? 98  ILE B CB  1 
ATOM   2666 C CG1 . ILE B 1 104 ? -0.215  54.138 84.138 1.00 42.40 ? 98  ILE B CG1 1 
ATOM   2667 C CG2 . ILE B 1 104 ? -0.835  52.914 82.055 1.00 2.00  ? 98  ILE B CG2 1 
ATOM   2668 C CD1 . ILE B 1 104 ? -1.340  53.407 84.850 1.00 2.00  ? 98  ILE B CD1 1 
ATOM   2669 N N   . GLY B 1 105 ? 0.458   50.092 82.363 1.00 2.00  ? 99  GLY B N   1 
ATOM   2670 C CA  . GLY B 1 105 ? 0.381   49.101 81.310 1.00 22.07 ? 99  GLY B CA  1 
ATOM   2671 C C   . GLY B 1 105 ? 1.560   48.138 81.276 1.00 39.17 ? 99  GLY B C   1 
ATOM   2672 O O   . GLY B 1 105 ? 2.431   48.113 82.169 1.00 18.09 ? 99  GLY B O   1 
ATOM   2673 N N   . CYS B 1 106 ? 1.595   47.352 80.207 1.00 2.00  ? 100 CYS B N   1 
ATOM   2674 C CA  . CYS B 1 106 ? 2.637   46.350 80.021 1.00 5.79  ? 100 CYS B CA  1 
ATOM   2675 C C   . CYS B 1 106 ? 4.020   46.943 79.761 1.00 3.08  ? 100 CYS B C   1 
ATOM   2676 O O   . CYS B 1 106 ? 4.894   46.871 80.613 1.00 30.03 ? 100 CYS B O   1 
ATOM   2677 C CB  . CYS B 1 106 ? 2.258   45.388 78.899 1.00 29.61 ? 100 CYS B CB  1 
ATOM   2678 S SG  . CYS B 1 106 ? 3.512   44.140 78.499 1.00 11.74 ? 100 CYS B SG  1 
ATOM   2679 N N   . LEU B 1 107 ? 4.207   47.511 78.577 1.00 16.71 ? 101 LEU B N   1 
ATOM   2680 C CA  . LEU B 1 107 ? 5.480   48.138 78.175 1.00 2.00  ? 101 LEU B CA  1 
ATOM   2681 C C   . LEU B 1 107 ? 5.291   49.635 77.971 1.00 6.91  ? 101 LEU B C   1 
ATOM   2682 O O   . LEU B 1 107 ? 5.020   50.082 76.859 1.00 15.73 ? 101 LEU B O   1 
ATOM   2683 C CB  . LEU B 1 107 ? 5.960   47.551 76.844 1.00 23.15 ? 101 LEU B CB  1 
ATOM   2684 C CG  . LEU B 1 107 ? 6.561   46.155 76.750 1.00 52.67 ? 101 LEU B CG  1 
ATOM   2685 C CD1 . LEU B 1 107 ? 6.541   45.710 75.292 1.00 66.57 ? 101 LEU B CD1 1 
ATOM   2686 C CD2 . LEU B 1 107 ? 7.984   46.173 77.277 1.00 21.04 ? 101 LEU B CD2 1 
ATOM   2687 N N   . PRO B 1 108 ? 5.519   50.442 79.014 1.00 49.44 ? 102 PRO B N   1 
ATOM   2688 C CA  . PRO B 1 108 ? 5.655   51.893 78.827 1.00 60.82 ? 102 PRO B CA  1 
ATOM   2689 C C   . PRO B 1 108 ? 6.866   52.281 77.965 1.00 19.69 ? 102 PRO B C   1 
ATOM   2690 O O   . PRO B 1 108 ? 7.880   51.561 77.926 1.00 15.10 ? 102 PRO B O   1 
ATOM   2691 C CB  . PRO B 1 108 ? 5.785   52.432 80.260 1.00 17.69 ? 102 PRO B CB  1 
ATOM   2692 C CG  . PRO B 1 108 ? 5.189   51.372 81.119 1.00 5.63  ? 102 PRO B CG  1 
ATOM   2693 C CD  . PRO B 1 108 ? 5.557   50.071 80.431 1.00 8.82  ? 102 PRO B CD  1 
ATOM   2694 N N   . TYR B 1 109 ? 6.822   53.499 77.419 1.00 23.43 ? 103 TYR B N   1 
ATOM   2695 C CA  . TYR B 1 109 ? 7.940   53.997 76.622 1.00 3.56  ? 103 TYR B CA  1 
ATOM   2696 C C   . TYR B 1 109 ? 9.246   54.186 77.406 1.00 4.05  ? 103 TYR B C   1 
ATOM   2697 O O   . TYR B 1 109 ? 9.265   54.686 78.529 1.00 43.28 ? 103 TYR B O   1 
ATOM   2698 C CB  . TYR B 1 109 ? 7.573   55.298 75.918 1.00 18.03 ? 103 TYR B CB  1 
ATOM   2699 C CG  . TYR B 1 109 ? 8.434   55.569 74.704 1.00 72.83 ? 103 TYR B CG  1 
ATOM   2700 C CD1 . TYR B 1 109 ? 8.616   54.597 73.728 1.00 22.30 ? 103 TYR B CD1 1 
ATOM   2701 C CD2 . TYR B 1 109 ? 8.971   56.826 74.483 1.00 10.60 ? 103 TYR B CD2 1 
ATOM   2702 C CE1 . TYR B 1 109 ? 9.290   54.885 72.554 1.00 16.73 ? 103 TYR B CE1 1 
ATOM   2703 C CE2 . TYR B 1 109 ? 9.634   57.127 73.323 1.00 46.60 ? 103 TYR B CE2 1 
ATOM   2704 C CZ  . TYR B 1 109 ? 9.788   56.164 72.351 1.00 38.42 ? 103 TYR B CZ  1 
ATOM   2705 O OH  . TYR B 1 109 ? 10.385  56.515 71.147 1.00 11.38 ? 103 TYR B OH  1 
ATOM   2706 N N   . THR B 1 110 ? 10.329  53.715 76.812 1.00 3.89  ? 104 THR B N   1 
ATOM   2707 C CA  . THR B 1 110 ? 11.616  53.675 77.490 1.00 27.00 ? 104 THR B CA  1 
ATOM   2708 C C   . THR B 1 110 ? 12.559  54.779 77.027 1.00 3.33  ? 104 THR B C   1 
ATOM   2709 O O   . THR B 1 110 ? 13.713  54.803 77.446 1.00 26.33 ? 104 THR B O   1 
ATOM   2710 C CB  . THR B 1 110 ? 12.367  52.328 77.257 1.00 15.16 ? 104 THR B CB  1 
ATOM   2711 O OG1 . THR B 1 110 ? 12.554  52.124 75.852 1.00 15.31 ? 104 THR B OG1 1 
ATOM   2712 C CG2 . THR B 1 110 ? 11.605  51.161 77.850 1.00 8.22  ? 104 THR B CG2 1 
ATOM   2713 N N   . ILE B 1 111 ? 12.075  55.712 76.212 1.00 35.28 ? 105 ILE B N   1 
ATOM   2714 C CA  . ILE B 1 111 ? 12.938  56.791 75.738 1.00 11.68 ? 105 ILE B CA  1 
ATOM   2715 C C   . ILE B 1 111 ? 12.533  58.155 76.304 1.00 22.25 ? 105 ILE B C   1 
ATOM   2716 O O   . ILE B 1 111 ? 11.360  58.570 76.222 1.00 2.00  ? 105 ILE B O   1 
ATOM   2717 C CB  . ILE B 1 111 ? 12.968  56.883 74.189 1.00 19.33 ? 105 ILE B CB  1 
ATOM   2718 C CG1 . ILE B 1 111 ? 12.785  55.499 73.554 1.00 38.95 ? 105 ILE B CG1 1 
ATOM   2719 C CG2 . ILE B 1 111 ? 14.272  57.518 73.733 1.00 26.47 ? 105 ILE B CG2 1 
ATOM   2720 C CD1 . ILE B 1 111 ? 14.059  54.813 73.121 1.00 16.38 ? 105 ILE B CD1 1 
ATOM   2721 N N   . PRO B 1 112 ? 13.496  58.853 76.926 1.00 10.92 ? 106 PRO B N   1 
ATOM   2722 C CA  . PRO B 1 112 ? 13.266  60.128 77.617 1.00 16.25 ? 106 PRO B CA  1 
ATOM   2723 C C   . PRO B 1 112 ? 12.646  61.209 76.747 1.00 3.81  ? 106 PRO B C   1 
ATOM   2724 O O   . PRO B 1 112 ? 13.014  61.373 75.582 1.00 39.99 ? 106 PRO B O   1 
ATOM   2725 C CB  . PRO B 1 112 ? 14.661  60.528 78.092 1.00 56.91 ? 106 PRO B CB  1 
ATOM   2726 C CG  . PRO B 1 112 ? 15.321  59.243 78.328 1.00 12.60 ? 106 PRO B CG  1 
ATOM   2727 C CD  . PRO B 1 112 ? 14.861  58.364 77.179 1.00 44.30 ? 106 PRO B CD  1 
ATOM   2728 N N   . PRO B 1 113 ? 11.631  61.901 77.286 1.00 11.64 ? 107 PRO B N   1 
ATOM   2729 C CA  . PRO B 1 113 ? 11.200  63.217 76.809 1.00 13.85 ? 107 PRO B CA  1 
ATOM   2730 C C   . PRO B 1 113 ? 12.352  64.209 76.766 1.00 69.79 ? 107 PRO B C   1 
ATOM   2731 O O   . PRO B 1 113 ? 13.322  64.111 77.523 1.00 32.84 ? 107 PRO B O   1 
ATOM   2732 C CB  . PRO B 1 113 ? 10.115  63.627 77.809 1.00 63.56 ? 107 PRO B CB  1 
ATOM   2733 C CG  . PRO B 1 113 ? 10.418  62.846 79.038 1.00 43.12 ? 107 PRO B CG  1 
ATOM   2734 C CD  . PRO B 1 113 ? 10.954  61.533 78.542 1.00 66.01 ? 107 PRO B CD  1 
ATOM   2735 N N   . CYS B 1 114 ? 12.305  65.071 75.764 1.00 40.80 ? 108 CYS B N   1 
ATOM   2736 C CA  . CYS B 1 114 ? 13.381  66.018 75.533 1.00 4.53  ? 108 CYS B CA  1 
ATOM   2737 C C   . CYS B 1 114 ? 12.847  67.240 74.798 1.00 59.72 ? 108 CYS B C   1 
ATOM   2738 O O   . CYS B 1 114 ? 11.663  67.305 74.442 1.00 2.00  ? 108 CYS B O   1 
ATOM   2739 C CB  . CYS B 1 114 ? 14.512  65.370 74.719 1.00 29.12 ? 108 CYS B CB  1 
ATOM   2740 S SG  . CYS B 1 114 ? 14.003  64.467 73.218 1.00 30.87 ? 108 CYS B SG  1 
ATOM   2741 N N   . GLU B 1 115 ? 13.696  68.242 74.640 1.00 2.54  ? 109 GLU B N   1 
ATOM   2742 C CA  . GLU B 1 115 ? 13.287  69.434 73.920 1.00 63.49 ? 109 GLU B CA  1 
ATOM   2743 C C   . GLU B 1 115 ? 13.471  69.339 72.408 1.00 32.16 ? 109 GLU B C   1 
ATOM   2744 O O   . GLU B 1 115 ? 14.534  68.931 71.925 1.00 7.06  ? 109 GLU B O   1 
ATOM   2745 C CB  . GLU B 1 115 ? 14.012  70.642 74.490 1.00 15.90 ? 109 GLU B CB  1 
ATOM   2746 C CG  . GLU B 1 115 ? 13.676  70.877 75.965 1.00 23.58 ? 109 GLU B CG  1 
ATOM   2747 C CD  . GLU B 1 115 ? 12.190  71.113 76.213 1.00 15.73 ? 109 GLU B CD  1 
ATOM   2748 O OE1 . GLU B 1 115 ? 11.453  71.367 75.235 1.00 13.96 ? 109 GLU B OE1 1 
ATOM   2749 O OE2 . GLU B 1 115 ? 11.774  71.102 77.394 1.00 54.22 ? 109 GLU B OE2 1 
ATOM   2750 N N   . HIS B 1 116 ? 12.374  69.588 71.692 1.00 35.28 ? 110 HIS B N   1 
ATOM   2751 C CA  . HIS B 1 116 ? 12.259  69.386 70.241 1.00 29.48 ? 110 HIS B CA  1 
ATOM   2752 C C   . HIS B 1 116 ? 12.140  70.734 69.547 1.00 77.13 ? 110 HIS B C   1 
ATOM   2753 O O   . HIS B 1 116 ? 11.045  71.257 69.434 1.00 7.36  ? 110 HIS B O   1 
ATOM   2754 C CB  . HIS B 1 116 ? 10.984  68.598 69.913 1.00 5.30  ? 110 HIS B CB  1 
ATOM   2755 C CG  . HIS B 1 116 ? 11.018  67.178 70.366 1.00 32.45 ? 110 HIS B CG  1 
ATOM   2756 N ND1 . HIS B 1 116 ? 11.426  66.153 69.542 1.00 9.05  ? 110 HIS B ND1 1 
ATOM   2757 C CD2 . HIS B 1 116 ? 10.732  66.611 71.561 1.00 2.00  ? 110 HIS B CD2 1 
ATOM   2758 C CE1 . HIS B 1 116 ? 11.392  65.015 70.209 1.00 14.88 ? 110 HIS B CE1 1 
ATOM   2759 N NE2 . HIS B 1 116 ? 10.983  65.268 71.438 1.00 22.33 ? 110 HIS B NE2 1 
ATOM   2760 N N   . HIS B 1 117 ? 13.253  71.291 69.083 1.00 6.33  ? 111 HIS B N   1 
ATOM   2761 C CA  . HIS B 1 117 ? 13.252  72.569 68.363 1.00 11.84 ? 111 HIS B CA  1 
ATOM   2762 C C   . HIS B 1 117 ? 12.581  73.693 69.162 1.00 9.55  ? 111 HIS B C   1 
ATOM   2763 O O   . HIS B 1 117 ? 11.953  74.603 68.613 1.00 82.81 ? 111 HIS B O   1 
ATOM   2764 C CB  . HIS B 1 117 ? 12.610  72.402 66.977 1.00 16.36 ? 111 HIS B CB  1 
ATOM   2765 C CG  . HIS B 1 117 ? 13.343  71.450 66.091 1.00 64.35 ? 111 HIS B CG  1 
ATOM   2766 N ND1 . HIS B 1 117 ? 14.511  71.792 65.436 1.00 60.51 ? 111 HIS B ND1 1 
ATOM   2767 C CD2 . HIS B 1 117 ? 13.137  70.140 65.827 1.00 14.46 ? 111 HIS B CD2 1 
ATOM   2768 C CE1 . HIS B 1 117 ? 14.992  70.731 64.820 1.00 42.01 ? 111 HIS B CE1 1 
ATOM   2769 N NE2 . HIS B 1 117 ? 14.177  69.713 65.039 1.00 37.85 ? 111 HIS B NE2 1 
ATOM   2770 N N   . VAL B 1 118 ? 12.730  73.585 70.482 1.00 67.26 ? 112 VAL B N   1 
ATOM   2771 C CA  . VAL B 1 118 ? 12.383  74.633 71.444 1.00 19.83 ? 112 VAL B CA  1 
ATOM   2772 C C   . VAL B 1 118 ? 13.392  74.665 72.591 1.00 51.74 ? 112 VAL B C   1 
ATOM   2773 O O   . VAL B 1 118 ? 14.167  73.721 72.794 1.00 21.95 ? 112 VAL B O   1 
ATOM   2774 C CB  . VAL B 1 118 ? 11.008  74.413 72.091 1.00 30.90 ? 112 VAL B CB  1 
ATOM   2775 C CG1 . VAL B 1 118 ? 9.921   75.082 71.266 1.00 7.89  ? 112 VAL B CG1 1 
ATOM   2776 C CG2 . VAL B 1 118 ? 10.765  72.921 72.280 1.00 8.01  ? 112 VAL B CG2 1 
ATOM   2777 N N   . ASN B 1 119 ? 13.351  75.742 73.365 1.00 53.64 ? 113 ASN B N   1 
ATOM   2778 C CA  . ASN B 1 119 ? 14.086  75.781 74.621 1.00 15.61 ? 113 ASN B CA  1 
ATOM   2779 C C   . ASN B 1 119 ? 13.123  75.400 75.727 1.00 16.03 ? 113 ASN B C   1 
ATOM   2780 O O   . ASN B 1 119 ? 11.923  75.658 75.623 1.00 31.99 ? 113 ASN B O   1 
ATOM   2781 C CB  . ASN B 1 119 ? 14.656  77.171 74.879 1.00 25.32 ? 113 ASN B CB  1 
ATOM   2782 C CG  . ASN B 1 119 ? 15.509  77.672 73.727 1.00 41.08 ? 113 ASN B CG  1 
ATOM   2783 O OD1 . ASN B 1 119 ? 16.532  77.079 73.391 1.00 59.31 ? 113 ASN B OD1 1 
ATOM   2784 N ND2 . ASN B 1 119 ? 15.095  78.775 73.121 1.00 47.88 ? 113 ASN B ND2 1 
ATOM   2785 N N   . GLY B 1 120 ? 13.599  74.569 76.639 1.00 27.07 ? 114 GLY B N   1 
ATOM   2786 C CA  . GLY B 1 120 ? 12.755  74.133 77.731 1.00 28.04 ? 114 GLY B CA  1 
ATOM   2787 C C   . GLY B 1 120 ? 13.572  73.526 78.844 1.00 56.90 ? 114 GLY B C   1 
ATOM   2788 O O   . GLY B 1 120 ? 14.809  73.526 78.775 1.00 38.62 ? 114 GLY B O   1 
ATOM   2789 N N   . ALA B 1 121 ? 12.891  72.961 79.838 1.00 40.83 ? 115 ALA B N   1 
ATOM   2790 C CA  . ALA B 1 121 ? 13.576  72.463 81.033 1.00 2.42  ? 115 ALA B CA  1 
ATOM   2791 C C   . ALA B 1 121 ? 14.289  71.124 80.791 1.00 60.54 ? 115 ALA B C   1 
ATOM   2792 O O   . ALA B 1 121 ? 15.276  70.802 81.474 1.00 28.21 ? 115 ALA B O   1 
ATOM   2793 C CB  . ALA B 1 121 ? 12.589  72.340 82.191 1.00 64.25 ? 115 ALA B CB  1 
ATOM   2794 N N   . ARG B 1 122 ? 13.833  70.400 79.762 1.00 10.09 ? 116 ARG B N   1 
ATOM   2795 C CA  . ARG B 1 122 ? 14.342  69.063 79.444 1.00 65.68 ? 116 ARG B CA  1 
ATOM   2796 C C   . ARG B 1 122 ? 15.605  69.110 78.571 1.00 27.26 ? 116 ARG B C   1 
ATOM   2797 O O   . ARG B 1 122 ? 15.855  70.092 77.864 1.00 23.93 ? 116 ARG B O   1 
ATOM   2798 C CB  . ARG B 1 122 ? 13.244  68.241 78.750 1.00 8.04  ? 116 ARG B CB  1 
ATOM   2799 C CG  . ARG B 1 122 ? 11.844  68.490 79.318 1.00 4.21  ? 116 ARG B CG  1 
ATOM   2800 C CD  . ARG B 1 122 ? 10.816  67.521 78.776 1.00 60.79 ? 116 ARG B CD  1 
ATOM   2801 N NE  . ARG B 1 122 ? 10.619  67.682 77.338 1.00 8.94  ? 116 ARG B NE  1 
ATOM   2802 C CZ  . ARG B 1 122 ? 9.711   68.481 76.776 1.00 24.71 ? 116 ARG B CZ  1 
ATOM   2803 N NH1 . ARG B 1 122 ? 8.830   69.129 77.525 1.00 23.36 ? 116 ARG B NH1 1 
ATOM   2804 N NH2 . ARG B 1 122 ? 9.643   68.581 75.453 1.00 10.17 ? 116 ARG B NH2 1 
ATOM   2805 N N   . PRO B 1 123 ? 16.416  68.043 78.608 1.00 15.25 ? 117 PRO B N   1 
ATOM   2806 C CA  . PRO B 1 123 ? 17.634  68.035 77.781 1.00 26.29 ? 117 PRO B CA  1 
ATOM   2807 C C   . PRO B 1 123 ? 17.203  68.162 76.326 1.00 54.79 ? 117 PRO B C   1 
ATOM   2808 O O   . PRO B 1 123 ? 16.082  67.795 75.992 1.00 2.48  ? 117 PRO B O   1 
ATOM   2809 C CB  . PRO B 1 123 ? 18.245  66.658 78.057 1.00 21.62 ? 117 PRO B CB  1 
ATOM   2810 C CG  . PRO B 1 123 ? 17.052  65.785 78.312 1.00 55.58 ? 117 PRO B CG  1 
ATOM   2811 C CD  . PRO B 1 123 ? 16.042  66.680 79.040 1.00 22.42 ? 117 PRO B CD  1 
ATOM   2812 N N   . PRO B 1 124 ? 18.074  68.685 75.448 1.00 72.73 ? 118 PRO B N   1 
ATOM   2813 C CA  . PRO B 1 124 ? 17.765  68.671 74.012 1.00 12.48 ? 118 PRO B CA  1 
ATOM   2814 C C   . PRO B 1 124 ? 17.658  67.258 73.449 1.00 62.68 ? 118 PRO B C   1 
ATOM   2815 O O   . PRO B 1 124 ? 18.336  66.333 73.907 1.00 25.49 ? 118 PRO B O   1 
ATOM   2816 C CB  . PRO B 1 124 ? 18.943  69.427 73.393 1.00 80.50 ? 118 PRO B CB  1 
ATOM   2817 C CG  . PRO B 1 124 ? 20.085  69.157 74.350 1.00 38.08 ? 118 PRO B CG  1 
ATOM   2818 C CD  . PRO B 1 124 ? 19.426  69.211 75.710 1.00 87.18 ? 118 PRO B CD  1 
ATOM   2819 N N   . CYS B 1 125 ? 16.785  67.082 72.469 1.00 33.06 ? 119 CYS B N   1 
ATOM   2820 C CA  . CYS B 1 125 ? 16.706  65.798 71.793 1.00 52.16 ? 119 CYS B CA  1 
ATOM   2821 C C   . CYS B 1 125 ? 17.943  65.603 70.950 1.00 31.93 ? 119 CYS B C   1 
ATOM   2822 O O   . CYS B 1 125 ? 18.614  66.569 70.581 1.00 85.78 ? 119 CYS B O   1 
ATOM   2823 C CB  . CYS B 1 125 ? 15.481  65.732 70.891 1.00 43.09 ? 119 CYS B CB  1 
ATOM   2824 S SG  . CYS B 1 125 ? 13.916  65.899 71.790 1.00 16.96 ? 119 CYS B SG  1 
ATOM   2825 N N   . THR B 1 126 ? 18.180  64.359 70.556 1.00 91.55 ? 120 THR B N   1 
ATOM   2826 C CA  . THR B 1 126 ? 19.156  64.070 69.515 1.00 33.86 ? 120 THR B CA  1 
ATOM   2827 C C   . THR B 1 126 ? 18.603  63.199 68.387 1.00 61.97 ? 120 THR B C   1 
ATOM   2828 O O   . THR B 1 126 ? 17.482  62.681 68.473 1.00 77.68 ? 120 THR B O   1 
ATOM   2829 C CB  . THR B 1 126 ? 20.470  63.435 70.101 1.00 52.63 ? 120 THR B CB  1 
ATOM   2830 O OG1 . THR B 1 126 ? 20.165  62.358 71.009 1.00 18.60 ? 120 THR B OG1 1 
ATOM   2831 C CG2 . THR B 1 126 ? 21.286  64.514 70.825 1.00 4.14  ? 120 THR B CG2 1 
ATOM   2832 N N   . GLY B 1 127 ? 19.248  63.312 67.233 1.00 67.29 ? 121 GLY B N   1 
ATOM   2833 C CA  . GLY B 1 127 ? 19.019  62.358 66.168 1.00 85.07 ? 121 GLY B CA  1 
ATOM   2834 C C   . GLY B 1 127 ? 19.499  60.985 66.596 1.00 50.66 ? 121 GLY B C   1 
ATOM   2835 O O   . GLY B 1 127 ? 18.745  60.018 66.568 1.00 19.68 ? 121 GLY B O   1 
ATOM   2836 N N   . GLU B 1 128 ? 20.736  60.919 67.081 1.00 72.93 ? 122 GLU B N   1 
ATOM   2837 C CA  . GLU B 1 128 ? 21.253  59.668 67.610 1.00 87.72 ? 122 GLU B CA  1 
ATOM   2838 C C   . GLU B 1 128 ? 20.217  58.967 68.482 1.00 39.39 ? 122 GLU B C   1 
ATOM   2839 O O   . GLU B 1 128 ? 19.872  59.480 69.614 1.00 49.95 ? 122 GLU B O   1 
ATOM   2840 C CB  . GLU B 1 128 ? 22.571  59.907 68.343 0.00 0.00  ? 122 GLU B CB  1 
ATOM   2841 C CG  . GLU B 1 128 ? 23.789  59.827 67.401 0.00 0.00  ? 122 GLU B CG  1 
ATOM   2842 C CD  . GLU B 1 128 ? 24.484  58.494 67.468 0.00 0.00  ? 122 GLU B CD  1 
ATOM   2843 O OE1 . GLU B 1 128 ? 23.877  57.503 67.839 0.00 0.00  ? 122 GLU B OE1 1 
ATOM   2844 O OE2 . GLU B 1 128 ? 25.770  58.458 67.109 0.00 0.00  ? 122 GLU B OE2 1 
ATOM   2845 N N   . GLY B 1 129 ? 19.638  57.888 67.947 1.00 45.67 ? 123 GLY B N   1 
ATOM   2846 C CA  . GLY B 1 129 ? 18.581  57.183 68.646 1.00 78.87 ? 123 GLY B CA  1 
ATOM   2847 C C   . GLY B 1 129 ? 18.582  55.715 68.289 1.00 80.09 ? 123 GLY B C   1 
ATOM   2848 O O   . GLY B 1 129 ? 18.183  55.320 67.191 1.00 66.60 ? 123 GLY B O   1 
ATOM   2849 N N   . ASP B 1 130 ? 19.175  54.920 69.167 1.00 40.70 ? 124 ASP B N   1 
ATOM   2850 C CA  . ASP B 1 130 ? 19.199  53.477 68.988 1.00 33.65 ? 124 ASP B CA  1 
ATOM   2851 C C   . ASP B 1 130 ? 17.801  52.929 69.225 1.00 26.91 ? 124 ASP B C   1 
ATOM   2852 O O   . ASP B 1 130 ? 16.978  53.586 69.847 1.00 27.31 ? 124 ASP B O   1 
ATOM   2853 C CB  . ASP B 1 130 ? 20.225  52.830 69.948 1.00 20.86 ? 124 ASP B CB  1 
ATOM   2854 C CG  . ASP B 1 130 ? 19.742  52.746 71.400 1.00 86.24 ? 124 ASP B CG  1 
ATOM   2855 O OD1 . ASP B 1 130 ? 19.148  53.717 71.921 1.00 50.78 ? 124 ASP B OD1 1 
ATOM   2856 O OD2 . ASP B 1 130 ? 20.057  51.727 72.060 1.00 38.59 ? 124 ASP B OD2 1 
ATOM   2857 N N   . THR B 1 131 ? 17.489  51.798 68.618 1.00 10.21 ? 125 THR B N   1 
ATOM   2858 C CA  . THR B 1 131 ? 16.198  51.162 68.875 1.00 14.87 ? 125 THR B CA  1 
ATOM   2859 C C   . THR B 1 131 ? 16.381  50.197 70.050 1.00 18.76 ? 125 THR B C   1 
ATOM   2860 O O   . THR B 1 131 ? 17.309  49.361 70.056 1.00 10.80 ? 125 THR B O   1 
ATOM   2861 C CB  . THR B 1 131 ? 15.675  50.399 67.613 1.00 20.53 ? 125 THR B CB  1 
ATOM   2862 O OG1 . THR B 1 131 ? 15.937  51.169 66.432 1.00 31.41 ? 125 THR B OG1 1 
ATOM   2863 C CG2 . THR B 1 131 ? 14.165  50.161 67.712 1.00 5.50  ? 125 THR B CG2 1 
ATOM   2864 N N   . PRO B 1 132 ? 15.679  50.460 71.157 1.00 29.17 ? 126 PRO B N   1 
ATOM   2865 C CA  . PRO B 1 132 ? 15.594  49.416 72.176 1.00 9.01  ? 126 PRO B CA  1 
ATOM   2866 C C   . PRO B 1 132 ? 15.252  48.053 71.566 1.00 52.34 ? 126 PRO B C   1 
ATOM   2867 O O   . PRO B 1 132 ? 14.632  47.972 70.509 1.00 10.01 ? 126 PRO B O   1 
ATOM   2868 C CB  . PRO B 1 132 ? 14.492  49.922 73.116 1.00 30.14 ? 126 PRO B CB  1 
ATOM   2869 C CG  . PRO B 1 132 ? 13.802  51.058 72.356 1.00 17.42 ? 126 PRO B CG  1 
ATOM   2870 C CD  . PRO B 1 132 ? 14.897  51.650 71.528 1.00 66.41 ? 126 PRO B CD  1 
ATOM   2871 N N   . LYS B 1 133 ? 15.748  46.992 72.188 1.00 10.60 ? 127 LYS B N   1 
ATOM   2872 C CA  . LYS B 1 133 ? 15.523  45.646 71.701 1.00 38.99 ? 127 LYS B CA  1 
ATOM   2873 C C   . LYS B 1 133 ? 14.075  45.237 71.980 1.00 9.26  ? 127 LYS B C   1 
ATOM   2874 O O   . LYS B 1 133 ? 13.383  45.840 72.805 1.00 21.18 ? 127 LYS B O   1 
ATOM   2875 C CB  . LYS B 1 133 ? 16.533  44.650 72.374 1.00 4.82  ? 127 LYS B CB  1 
ATOM   2876 C CG  . LYS B 1 133 ? 16.721  43.321 71.546 0.00 0.00  ? 127 LYS B CG  1 
ATOM   2877 C CD  . LYS B 1 133 ? 17.331  42.210 72.377 0.00 0.00  ? 127 LYS B CD  1 
ATOM   2878 C CE  . LYS B 1 133 ? 16.358  41.651 73.390 0.00 0.00  ? 127 LYS B CE  1 
ATOM   2879 N NZ  . LYS B 1 133 ? 16.670  40.212 73.634 0.00 0.00  ? 127 LYS B NZ  1 
ATOM   2880 N N   . CYS B 1 134 ? 13.622  44.214 71.275 1.00 20.57 ? 128 CYS B N   1 
ATOM   2881 C CA  . CYS B 1 134 ? 12.294  43.685 71.490 1.00 7.68  ? 128 CYS B CA  1 
ATOM   2882 C C   . CYS B 1 134 ? 12.264  42.712 72.691 1.00 81.43 ? 128 CYS B C   1 
ATOM   2883 O O   . CYS B 1 134 ? 12.647  41.547 72.589 1.00 67.65 ? 128 CYS B O   1 
ATOM   2884 C CB  . CYS B 1 134 ? 11.804  43.028 70.195 1.00 2.68  ? 128 CYS B CB  1 
ATOM   2885 S SG  . CYS B 1 134 ? 10.245  42.116 70.317 1.00 21.98 ? 128 CYS B SG  1 
ATOM   2886 N N   . ASN B 1 135 ? 12.048  43.284 73.872 1.00 31.10 ? 129 ASN B N   1 
ATOM   2887 C CA  . ASN B 1 135 ? 11.792  42.530 75.104 1.00 16.60 ? 129 ASN B CA  1 
ATOM   2888 C C   . ASN B 1 135 ? 10.304  42.146 75.098 1.00 17.22 ? 129 ASN B C   1 
ATOM   2889 O O   . ASN B 1 135 ? 9.433   43.024 75.118 1.00 46.93 ? 129 ASN B O   1 
ATOM   2890 C CB  . ASN B 1 135 ? 12.087  43.443 76.301 1.00 90.81 ? 129 ASN B CB  1 
ATOM   2891 C CG  . ASN B 1 135 ? 12.370  42.685 77.603 1.00 27.00 ? 129 ASN B CG  1 
ATOM   2892 O OD1 . ASN B 1 135 ? 12.866  43.266 78.554 1.00 38.36 ? 129 ASN B OD1 1 
ATOM   2893 N ND2 . ASN B 1 135 ? 11.975  41.418 77.684 1.00 31.92 ? 129 ASN B ND2 1 
ATOM   2894 N N   . LYS B 1 136 ? 9.995   40.865 74.938 1.00 2.31  ? 130 LYS B N   1 
ATOM   2895 C CA  . LYS B 1 136 ? 8.598   40.461 75.005 1.00 2.00  ? 130 LYS B CA  1 
ATOM   2896 C C   . LYS B 1 136 ? 8.104   40.189 76.424 1.00 65.29 ? 130 LYS B C   1 
ATOM   2897 O O   . LYS B 1 136 ? 7.215   39.367 76.632 1.00 41.26 ? 130 LYS B O   1 
ATOM   2898 C CB  . LYS B 1 136 ? 8.321   39.269 74.078 1.00 15.65 ? 130 LYS B CB  1 
ATOM   2899 C CG  . LYS B 1 136 ? 8.347   39.650 72.587 1.00 10.38 ? 130 LYS B CG  1 
ATOM   2900 C CD  . LYS B 1 136 ? 7.407   38.796 71.761 1.00 98.74 ? 130 LYS B CD  1 
ATOM   2901 C CE  . LYS B 1 136 ? 8.110   37.618 71.125 1.00 41.67 ? 130 LYS B CE  1 
ATOM   2902 N NZ  . LYS B 1 136 ? 7.110   36.770 70.413 1.00 87.14 ? 130 LYS B NZ  1 
ATOM   2903 N N   . MET B 1 137 ? 8.579   41.002 77.369 1.00 52.48 ? 131 MET B N   1 
ATOM   2904 C CA  . MET B 1 137 ? 8.095   40.964 78.749 1.00 73.13 ? 131 MET B CA  1 
ATOM   2905 C C   . MET B 1 137 ? 7.495   42.296 79.206 1.00 28.65 ? 131 MET B C   1 
ATOM   2906 O O   . MET B 1 137 ? 8.151   43.345 79.154 1.00 15.64 ? 131 MET B O   1 
ATOM   2907 C CB  . MET B 1 137 ? 9.217   40.567 79.718 1.00 8.15  ? 131 MET B CB  1 
ATOM   2908 C CG  . MET B 1 137 ? 9.373   39.065 79.943 1.00 76.98 ? 131 MET B CG  1 
ATOM   2909 S SD  . MET B 1 137 ? 10.624  38.688 81.188 1.00 89.32 ? 131 MET B SD  1 
ATOM   2910 C CE  . MET B 1 137 ? 9.646   37.812 82.402 1.00 66.76 ? 131 MET B CE  1 
ATOM   2911 N N   . CYS B 1 138 ? 6.238   42.232 79.634 1.00 18.51 ? 132 CYS B N   1 
ATOM   2912 C CA  . CYS B 1 138 ? 5.606   43.288 80.426 1.00 9.77  ? 132 CYS B CA  1 
ATOM   2913 C C   . CYS B 1 138 ? 6.511   43.659 81.572 1.00 6.25  ? 132 CYS B C   1 
ATOM   2914 O O   . CYS B 1 138 ? 7.256   42.813 82.062 1.00 39.57 ? 132 CYS B O   1 
ATOM   2915 C CB  . CYS B 1 138 ? 4.276   42.802 80.996 1.00 2.00  ? 132 CYS B CB  1 
ATOM   2916 S SG  . CYS B 1 138 ? 3.043   42.567 79.702 1.00 22.71 ? 132 CYS B SG  1 
ATOM   2917 N N   . GLU B 1 139 ? 6.529   44.938 81.937 1.00 36.29 ? 133 GLU B N   1 
ATOM   2918 C CA  . GLU B 1 139 ? 7.411   45.404 83.012 1.00 31.78 ? 133 GLU B CA  1 
ATOM   2919 C C   . GLU B 1 139 ? 6.955   44.777 84.312 1.00 59.95 ? 133 GLU B C   1 
ATOM   2920 O O   . GLU B 1 139 ? 5.824   44.294 84.392 1.00 14.65 ? 133 GLU B O   1 
ATOM   2921 C CB  . GLU B 1 139 ? 7.371   46.926 83.143 1.00 7.81  ? 133 GLU B CB  1 
ATOM   2922 C CG  . GLU B 1 139 ? 6.060   47.461 83.656 1.00 9.81  ? 133 GLU B CG  1 
ATOM   2923 C CD  . GLU B 1 139 ? 6.138   48.924 84.071 1.00 49.08 ? 133 GLU B CD  1 
ATOM   2924 O OE1 . GLU B 1 139 ? 7.262   49.492 84.111 1.00 15.11 ? 133 GLU B OE1 1 
ATOM   2925 O OE2 . GLU B 1 139 ? 5.060   49.510 84.339 1.00 19.82 ? 133 GLU B OE2 1 
ATOM   2926 N N   . ALA B 1 140 ? 7.845   44.763 85.302 1.00 17.60 ? 134 ALA B N   1 
ATOM   2927 C CA  . ALA B 1 140 ? 7.546   44.218 86.628 1.00 79.13 ? 134 ALA B CA  1 
ATOM   2928 C C   . ALA B 1 140 ? 6.423   44.945 87.358 1.00 2.02  ? 134 ALA B C   1 
ATOM   2929 O O   . ALA B 1 140 ? 6.450   46.169 87.522 1.00 50.10 ? 134 ALA B O   1 
ATOM   2930 C CB  . ALA B 1 140 ? 8.788   44.226 87.490 1.00 2.00  ? 134 ALA B CB  1 
ATOM   2931 N N   . GLY B 1 141 ? 5.500   44.163 87.891 1.00 7.00  ? 135 GLY B N   1 
ATOM   2932 C CA  . GLY B 1 141 ? 4.352   44.729 88.552 1.00 2.00  ? 135 GLY B CA  1 
ATOM   2933 C C   . GLY B 1 141 ? 3.111   44.514 87.725 1.00 43.63 ? 135 GLY B C   1 
ATOM   2934 O O   . GLY B 1 141 ? 2.069   44.113 88.258 1.00 6.54  ? 135 GLY B O   1 
ATOM   2935 N N   . TYR B 1 142 ? 3.257   44.644 86.406 1.00 49.20 ? 136 TYR B N   1 
ATOM   2936 C CA  . TYR B 1 142 ? 2.105   44.535 85.526 1.00 5.49  ? 136 TYR B CA  1 
ATOM   2937 C C   . TYR B 1 142 ? 1.296   43.246 85.703 1.00 8.63  ? 136 TYR B C   1 
ATOM   2938 O O   . TYR B 1 142 ? 1.858   42.128 85.711 1.00 9.03  ? 136 TYR B O   1 
ATOM   2939 C CB  . TYR B 1 142 ? 2.469   44.716 84.044 1.00 4.47  ? 136 TYR B CB  1 
ATOM   2940 C CG  . TYR B 1 142 ? 1.203   44.863 83.220 1.00 53.60 ? 136 TYR B CG  1 
ATOM   2941 C CD1 . TYR B 1 142 ? 0.390   45.962 83.377 1.00 7.26  ? 136 TYR B CD1 1 
ATOM   2942 C CD2 . TYR B 1 142 ? 0.769   43.862 82.372 1.00 2.33  ? 136 TYR B CD2 1 
ATOM   2943 C CE1 . TYR B 1 142 ? -0.781  46.082 82.699 1.00 6.80  ? 136 TYR B CE1 1 
ATOM   2944 C CE2 . TYR B 1 142 ? -0.431  43.961 81.723 1.00 10.97 ? 136 TYR B CE2 1 
ATOM   2945 C CZ  . TYR B 1 142 ? -1.190  45.090 81.872 1.00 10.90 ? 136 TYR B CZ  1 
ATOM   2946 O OH  . TYR B 1 142 ? -2.293  45.319 81.089 1.00 7.45  ? 136 TYR B OH  1 
ATOM   2947 N N   . SER B 1 143 ? -0.028  43.421 85.755 1.00 2.21  ? 137 SER B N   1 
ATOM   2948 C CA  . SER B 1 143 ? -0.946  42.427 86.316 1.00 34.70 ? 137 SER B CA  1 
ATOM   2949 C C   . SER B 1 143 ? -1.113  41.197 85.435 1.00 23.01 ? 137 SER B C   1 
ATOM   2950 O O   . SER B 1 143 ? -1.530  40.135 85.902 1.00 76.72 ? 137 SER B O   1 
ATOM   2951 C CB  . SER B 1 143 ? -2.321  43.075 86.553 1.00 23.43 ? 137 SER B CB  1 
ATOM   2952 O OG  . SER B 1 143 ? -2.617  44.019 85.534 1.00 15.74 ? 137 SER B OG  1 
ATOM   2953 N N   . THR B 1 144 ? -0.666  41.332 84.190 1.00 2.00  ? 138 THR B N   1 
ATOM   2954 C CA  . THR B 1 144 ? -1.041  40.455 83.086 1.00 22.43 ? 138 THR B CA  1 
ATOM   2955 C C   . THR B 1 144 ? 0.195   40.267 82.203 1.00 11.67 ? 138 THR B C   1 
ATOM   2956 O O   . THR B 1 144 ? 1.074   41.136 82.180 1.00 2.00  ? 138 THR B O   1 
ATOM   2957 C CB  . THR B 1 144 ? -2.166  41.115 82.269 1.00 7.08  ? 138 THR B CB  1 
ATOM   2958 O OG1 . THR B 1 144 ? -3.400  41.053 82.991 1.00 82.55 ? 138 THR B OG1 1 
ATOM   2959 C CG2 . THR B 1 144 ? -2.335  40.452 80.948 1.00 14.07 ? 138 THR B CG2 1 
ATOM   2960 N N   . SER B 1 145 ? 0.324   39.110 81.565 1.00 25.29 ? 139 SER B N   1 
ATOM   2961 C CA  . SER B 1 145 ? 1.543   38.828 80.793 1.00 30.01 ? 139 SER B CA  1 
ATOM   2962 C C   . SER B 1 145 ? 1.484   39.423 79.396 1.00 13.03 ? 139 SER B C   1 
ATOM   2963 O O   . SER B 1 145 ? 0.410   39.791 78.918 1.00 27.72 ? 139 SER B O   1 
ATOM   2964 C CB  . SER B 1 145 ? 1.799   37.321 80.699 1.00 36.86 ? 139 SER B CB  1 
ATOM   2965 O OG  . SER B 1 145 ? 0.917   36.700 79.777 1.00 9.71  ? 139 SER B OG  1 
ATOM   2966 N N   . TYR B 1 146 ? 2.642   39.534 78.752 1.00 51.32 ? 140 TYR B N   1 
ATOM   2967 C CA  . TYR B 1 146 ? 2.747   40.141 77.422 1.00 19.92 ? 140 TYR B CA  1 
ATOM   2968 C C   . TYR B 1 146 ? 1.771   39.558 76.388 1.00 20.85 ? 140 TYR B C   1 
ATOM   2969 O O   . TYR B 1 146 ? 0.943   40.288 75.854 1.00 22.95 ? 140 TYR B O   1 
ATOM   2970 C CB  . TYR B 1 146 ? 4.197   40.058 76.935 1.00 5.69  ? 140 TYR B CB  1 
ATOM   2971 C CG  . TYR B 1 146 ? 4.456   40.575 75.530 1.00 32.27 ? 140 TYR B CG  1 
ATOM   2972 C CD1 . TYR B 1 146 ? 4.327   39.734 74.439 1.00 5.06  ? 140 TYR B CD1 1 
ATOM   2973 C CD2 . TYR B 1 146 ? 4.926   41.865 75.308 1.00 4.96  ? 140 TYR B CD2 1 
ATOM   2974 C CE1 . TYR B 1 146 ? 4.639   40.148 73.168 1.00 10.79 ? 140 TYR B CE1 1 
ATOM   2975 C CE2 . TYR B 1 146 ? 5.265   42.291 74.044 1.00 39.89 ? 140 TYR B CE2 1 
ATOM   2976 C CZ  . TYR B 1 146 ? 5.114   41.429 72.969 1.00 17.28 ? 140 TYR B CZ  1 
ATOM   2977 O OH  . TYR B 1 146 ? 5.411   41.852 71.694 1.00 71.13 ? 140 TYR B OH  1 
ATOM   2978 N N   . LYS B 1 147 ? 1.777   38.235 76.197 1.00 8.77  ? 141 LYS B N   1 
ATOM   2979 C CA  . LYS B 1 147 ? 0.815   37.624 75.267 1.00 21.32 ? 141 LYS B CA  1 
ATOM   2980 C C   . LYS B 1 147 ? -0.634  37.940 75.615 1.00 5.82  ? 141 LYS B C   1 
ATOM   2981 O O   . LYS B 1 147 ? -1.461  38.139 74.722 1.00 4.41  ? 141 LYS B O   1 
ATOM   2982 C CB  . LYS B 1 147 ? 0.975   36.107 75.202 1.00 29.44 ? 141 LYS B CB  1 
ATOM   2983 C CG  . LYS B 1 147 ? 1.710   35.601 73.963 1.00 41.18 ? 141 LYS B CG  1 
ATOM   2984 C CD  . LYS B 1 147 ? 1.437   36.448 72.718 1.00 40.91 ? 141 LYS B CD  1 
ATOM   2985 C CE  . LYS B 1 147 ? 2.515   36.197 71.651 1.00 87.34 ? 141 LYS B CE  1 
ATOM   2986 N NZ  . LYS B 1 147 ? 3.896   35.954 72.223 1.00 24.16 ? 141 LYS B NZ  1 
ATOM   2987 N N   . GLU B 1 148 ? -0.894  38.154 76.905 1.00 2.00  ? 142 GLU B N   1 
ATOM   2988 C CA  . GLU B 1 148 ? -2.268  38.336 77.382 1.00 29.62 ? 142 GLU B CA  1 
ATOM   2989 C C   . GLU B 1 148 ? -2.783  39.736 77.104 1.00 25.71 ? 142 GLU B C   1 
ATOM   2990 O O   . GLU B 1 148 ? -3.966  39.959 76.878 1.00 14.66 ? 142 GLU B O   1 
ATOM   2991 C CB  . GLU B 1 148 ? -2.316  38.066 78.884 1.00 28.18 ? 142 GLU B CB  1 
ATOM   2992 C CG  . GLU B 1 148 ? -3.114  36.862 79.269 1.00 57.36 ? 142 GLU B CG  1 
ATOM   2993 C CD  . GLU B 1 148 ? -2.805  35.675 78.385 1.00 10.28 ? 142 GLU B CD  1 
ATOM   2994 O OE1 . GLU B 1 148 ? -1.598  35.405 78.116 1.00 75.98 ? 142 GLU B OE1 1 
ATOM   2995 O OE2 . GLU B 1 148 ? -3.771  34.943 78.051 1.00 23.74 ? 142 GLU B OE2 1 
ATOM   2996 N N   . ASP B 1 149 ? -1.862  40.678 77.198 1.00 2.00  ? 143 ASP B N   1 
ATOM   2997 C CA  . ASP B 1 149 ? -2.131  42.091 77.141 1.00 15.09 ? 143 ASP B CA  1 
ATOM   2998 C C   . ASP B 1 149 ? -2.183  42.647 75.703 1.00 41.60 ? 143 ASP B C   1 
ATOM   2999 O O   . ASP B 1 149 ? -2.416  43.840 75.525 1.00 18.01 ? 143 ASP B O   1 
ATOM   3000 C CB  . ASP B 1 149 ? -1.031  42.803 77.953 1.00 14.38 ? 143 ASP B CB  1 
ATOM   3001 C CG  . ASP B 1 149 ? -1.419  44.207 78.360 1.00 20.89 ? 143 ASP B CG  1 
ATOM   3002 O OD1 . ASP B 1 149 ? -2.610  44.438 78.641 1.00 11.89 ? 143 ASP B OD1 1 
ATOM   3003 O OD2 . ASP B 1 149 ? -0.542  45.088 78.357 1.00 8.33  ? 143 ASP B OD2 1 
ATOM   3004 N N   . LYS B 1 150 ? -1.949  41.802 74.693 1.00 10.71 ? 144 LYS B N   1 
ATOM   3005 C CA  . LYS B 1 150 ? -2.024  42.229 73.288 1.00 90.21 ? 144 LYS B CA  1 
ATOM   3006 C C   . LYS B 1 150 ? -3.451  42.555 72.827 1.00 2.39  ? 144 LYS B C   1 
ATOM   3007 O O   . LYS B 1 150 ? -4.413  41.862 73.161 1.00 44.09 ? 144 LYS B O   1 
ATOM   3008 C CB  . LYS B 1 150 ? -1.413  41.173 72.341 1.00 5.77  ? 144 LYS B CB  1 
ATOM   3009 C CG  . LYS B 1 150 ? 0.084   41.026 72.470 1.00 2.00  ? 144 LYS B CG  1 
ATOM   3010 C CD  . LYS B 1 150 ? 0.791   41.281 71.143 1.00 24.77 ? 144 LYS B CD  1 
ATOM   3011 C CE  . LYS B 1 150 ? 2.210   41.885 71.327 1.00 2.00  ? 144 LYS B CE  1 
ATOM   3012 N NZ  . LYS B 1 150 ? 2.819   42.237 69.976 1.00 10.93 ? 144 LYS B NZ  1 
ATOM   3013 N N   . HIS B 1 151 ? -3.579  43.675 72.128 1.00 30.09 ? 145 HIS B N   1 
ATOM   3014 C CA  . HIS B 1 151 ? -4.836  44.060 71.498 1.00 2.00  ? 145 HIS B CA  1 
ATOM   3015 C C   . HIS B 1 151 ? -4.668  44.004 69.961 1.00 83.27 ? 145 HIS B C   1 
ATOM   3016 O O   . HIS B 1 151 ? -3.590  44.259 69.422 1.00 2.00  ? 145 HIS B O   1 
ATOM   3017 C CB  . HIS B 1 151 ? -5.235  45.472 71.943 1.00 47.19 ? 145 HIS B CB  1 
ATOM   3018 C CG  . HIS B 1 151 ? -5.195  45.670 73.428 1.00 83.12 ? 145 HIS B CG  1 
ATOM   3019 N ND1 . HIS B 1 151 ? -6.316  45.981 74.174 1.00 14.67 ? 145 HIS B ND1 1 
ATOM   3020 C CD2 . HIS B 1 151 ? -4.168  45.597 74.308 1.00 19.75 ? 145 HIS B CD2 1 
ATOM   3021 C CE1 . HIS B 1 151 ? -5.973  46.110 75.444 1.00 4.92  ? 145 HIS B CE1 1 
ATOM   3022 N NE2 . HIS B 1 151 ? -4.679  45.863 75.555 1.00 10.50 ? 145 HIS B NE2 1 
ATOM   3023 N N   . TYR B 1 152 ? -5.696  43.570 69.253 1.00 2.00  ? 146 TYR B N   1 
ATOM   3024 C CA  . TYR B 1 152 ? -5.519  43.295 67.839 1.00 27.11 ? 146 TYR B CA  1 
ATOM   3025 C C   . TYR B 1 152 ? -6.350  44.161 66.930 1.00 61.63 ? 146 TYR B C   1 
ATOM   3026 O O   . TYR B 1 152 ? -7.476  44.571 67.256 1.00 12.77 ? 146 TYR B O   1 
ATOM   3027 C CB  . TYR B 1 152 ? -5.787  41.837 67.511 1.00 2.00  ? 146 TYR B CB  1 
ATOM   3028 C CG  . TYR B 1 152 ? -4.769  40.866 68.067 1.00 2.00  ? 146 TYR B CG  1 
ATOM   3029 C CD1 . TYR B 1 152 ? -3.593  40.597 67.399 1.00 16.50 ? 146 TYR B CD1 1 
ATOM   3030 C CD2 . TYR B 1 152 ? -4.977  40.255 69.286 1.00 2.00  ? 146 TYR B CD2 1 
ATOM   3031 C CE1 . TYR B 1 152 ? -2.638  39.742 67.951 1.00 2.54  ? 146 TYR B CE1 1 
ATOM   3032 C CE2 . TYR B 1 152 ? -4.060  39.411 69.827 1.00 14.94 ? 146 TYR B CE2 1 
ATOM   3033 C CZ  . TYR B 1 152 ? -2.884  39.152 69.168 1.00 6.24  ? 146 TYR B CZ  1 
ATOM   3034 O OH  . TYR B 1 152 ? -1.960  38.317 69.749 1.00 25.57 ? 146 TYR B OH  1 
ATOM   3035 N N   . GLY B 1 153 ? -5.759  44.458 65.784 1.00 11.35 ? 147 GLY B N   1 
ATOM   3036 C CA  . GLY B 1 153 ? -6.489  45.107 64.731 1.00 2.00  ? 147 GLY B CA  1 
ATOM   3037 C C   . GLY B 1 153 ? -7.417  44.123 64.070 1.00 2.02  ? 147 GLY B C   1 
ATOM   3038 O O   . GLY B 1 153 ? -7.126  42.944 63.911 1.00 2.00  ? 147 GLY B O   1 
ATOM   3039 N N   . TYR B 1 154 ? -8.549  44.616 63.620 1.00 2.00  ? 148 TYR B N   1 
ATOM   3040 C CA  . TYR B 1 154 ? -9.328  43.751 62.759 1.00 17.01 ? 148 TYR B CA  1 
ATOM   3041 C C   . TYR B 1 154 ? -8.959  44.015 61.291 1.00 2.00  ? 148 TYR B C   1 
ATOM   3042 O O   . TYR B 1 154 ? -8.646  43.105 60.542 1.00 8.80  ? 148 TYR B O   1 
ATOM   3043 C CB  . TYR B 1 154 ? -10.790 43.981 63.020 1.00 2.00  ? 148 TYR B CB  1 
ATOM   3044 C CG  . TYR B 1 154 ? -11.671 43.090 62.219 1.00 32.29 ? 148 TYR B CG  1 
ATOM   3045 C CD1 . TYR B 1 154 ? -11.278 41.780 61.929 1.00 58.72 ? 148 TYR B CD1 1 
ATOM   3046 C CD2 . TYR B 1 154 ? -12.897 43.548 61.748 1.00 23.32 ? 148 TYR B CD2 1 
ATOM   3047 C CE1 . TYR B 1 154 ? -12.075 40.933 61.181 1.00 17.34 ? 148 TYR B CE1 1 
ATOM   3048 C CE2 . TYR B 1 154 ? -13.747 42.705 60.998 1.00 38.48 ? 148 TYR B CE2 1 
ATOM   3049 C CZ  . TYR B 1 154 ? -13.337 41.395 60.707 1.00 36.56 ? 148 TYR B CZ  1 
ATOM   3050 O OH  . TYR B 1 154 ? -14.146 40.540 59.933 1.00 34.17 ? 148 TYR B OH  1 
ATOM   3051 N N   . THR B 1 155 ? -8.855  45.289 60.947 1.00 41.44 ? 149 THR B N   1 
ATOM   3052 C CA  . THR B 1 155 ? -8.557  45.684 59.579 1.00 81.27 ? 149 THR B CA  1 
ATOM   3053 C C   . THR B 1 155 ? -7.481  46.765 59.585 1.00 2.62  ? 149 THR B C   1 
ATOM   3054 O O   . THR B 1 155 ? -7.184  47.358 60.630 1.00 14.48 ? 149 THR B O   1 
ATOM   3055 C CB  . THR B 1 155 ? -9.815  46.239 58.846 1.00 7.41  ? 149 THR B CB  1 
ATOM   3056 O OG1 . THR B 1 155 ? -10.132 47.538 59.366 1.00 59.91 ? 149 THR B OG1 1 
ATOM   3057 C CG2 . THR B 1 155 ? -11.017 45.318 59.034 1.00 43.24 ? 149 THR B CG2 1 
ATOM   3058 N N   . SER B 1 156 ? -6.795  46.876 58.455 1.00 2.00  ? 150 SER B N   1 
ATOM   3059 C CA  . SER B 1 156 ? -5.928  48.011 58.145 1.00 23.96 ? 150 SER B CA  1 
ATOM   3060 C C   . SER B 1 156 ? -6.191  48.414 56.701 1.00 2.00  ? 150 SER B C   1 
ATOM   3061 O O   . SER B 1 156 ? -6.425  47.562 55.852 1.00 15.40 ? 150 SER B O   1 
ATOM   3062 C CB  . SER B 1 156 ? -4.454  47.632 58.317 1.00 2.00  ? 150 SER B CB  1 
ATOM   3063 O OG  . SER B 1 156 ? -4.153  46.466 57.577 1.00 43.49 ? 150 SER B OG  1 
ATOM   3064 N N   . TYR B 1 157 ? -6.188  49.712 56.415 1.00 13.07 ? 151 TYR B N   1 
ATOM   3065 C CA  . TYR B 1 157 ? -6.422  50.181 55.056 1.00 2.00  ? 151 TYR B CA  1 
ATOM   3066 C C   . TYR B 1 157 ? -5.871  51.569 54.797 1.00 2.00  ? 151 TYR B C   1 
ATOM   3067 O O   . TYR B 1 157 ? -5.730  52.371 55.727 1.00 9.96  ? 151 TYR B O   1 
ATOM   3068 C CB  . TYR B 1 157 ? -7.907  50.201 54.756 1.00 3.03  ? 151 TYR B CB  1 
ATOM   3069 C CG  . TYR B 1 157 ? -8.728  50.738 55.880 1.00 12.33 ? 151 TYR B CG  1 
ATOM   3070 C CD1 . TYR B 1 157 ? -9.078  49.923 56.956 1.00 25.20 ? 151 TYR B CD1 1 
ATOM   3071 C CD2 . TYR B 1 157 ? -9.140  52.072 55.885 1.00 2.00  ? 151 TYR B CD2 1 
ATOM   3072 C CE1 . TYR B 1 157 ? -9.825  50.404 57.982 1.00 2.00  ? 151 TYR B CE1 1 
ATOM   3073 C CE2 . TYR B 1 157 ? -9.846  52.567 56.915 1.00 3.09  ? 151 TYR B CE2 1 
ATOM   3074 C CZ  . TYR B 1 157 ? -10.221 51.731 57.945 1.00 35.44 ? 151 TYR B CZ  1 
ATOM   3075 O OH  . TYR B 1 157 ? -11.189 52.163 58.790 1.00 7.13  ? 151 TYR B OH  1 
ATOM   3076 N N   . SER B 1 158 ? -5.505  51.827 53.539 1.00 31.89 ? 152 SER B N   1 
ATOM   3077 C CA  . SER B 1 158 ? -5.108  53.167 53.078 1.00 4.23  ? 152 SER B CA  1 
ATOM   3078 C C   . SER B 1 158 ? -6.363  53.929 52.683 1.00 2.00  ? 152 SER B C   1 
ATOM   3079 O O   . SER B 1 158 ? -7.377  53.314 52.350 1.00 4.46  ? 152 SER B O   1 
ATOM   3080 C CB  . SER B 1 158 ? -4.170  53.061 51.870 1.00 11.98 ? 152 SER B CB  1 
ATOM   3081 O OG  . SER B 1 158 ? -2.896  52.544 52.228 1.00 2.00  ? 152 SER B OG  1 
ATOM   3082 N N   . VAL B 1 159 ? -6.376  55.221 52.971 1.00 18.26 ? 153 VAL B N   1 
ATOM   3083 C CA  . VAL B 1 159 ? -7.502  56.091 52.632 1.00 2.00  ? 153 VAL B CA  1 
ATOM   3084 C C   . VAL B 1 159 ? -7.079  56.889 51.419 1.00 7.29  ? 153 VAL B C   1 
ATOM   3085 O O   . VAL B 1 159 ? -5.958  57.407 51.378 1.00 14.65 ? 153 VAL B O   1 
ATOM   3086 C CB  . VAL B 1 159 ? -7.854  57.086 53.786 1.00 40.00 ? 153 VAL B CB  1 
ATOM   3087 C CG1 . VAL B 1 159 ? -9.046  57.956 53.389 1.00 3.05  ? 153 VAL B CG1 1 
ATOM   3088 C CG2 . VAL B 1 159 ? -8.160  56.346 55.086 1.00 2.00  ? 153 VAL B CG2 1 
ATOM   3089 N N   . SER B 1 160 ? -7.917  56.904 50.381 1.00 4.73  ? 154 SER B N   1 
ATOM   3090 C CA  . SER B 1 160 ? -7.574  57.630 49.159 1.00 6.04  ? 154 SER B CA  1 
ATOM   3091 C C   . SER B 1 160 ? -7.439  59.147 49.355 1.00 18.83 ? 154 SER B C   1 
ATOM   3092 O O   . SER B 1 160 ? -7.836  59.715 50.378 1.00 13.58 ? 154 SER B O   1 
ATOM   3093 C CB  . SER B 1 160 ? -8.588  57.327 48.055 1.00 2.48  ? 154 SER B CB  1 
ATOM   3094 O OG  . SER B 1 160 ? -8.491  55.967 47.650 1.00 14.10 ? 154 SER B OG  1 
ATOM   3095 N N   . ASP B 1 161 ? -6.605  59.733 48.519 1.00 7.47  ? 155 ASP B N   1 
ATOM   3096 C CA  . ASP B 1 161 ? -6.421  61.168 48.503 1.00 2.00  ? 155 ASP B CA  1 
ATOM   3097 C C   . ASP B 1 161 ? -7.707  61.855 48.112 1.00 23.37 ? 155 ASP B C   1 
ATOM   3098 O O   . ASP B 1 161 ? -7.835  62.330 46.984 1.00 11.07 ? 155 ASP B O   1 
ATOM   3099 C CB  . ASP B 1 161 ? -5.345  61.547 47.494 1.00 3.63  ? 155 ASP B CB  1 
ATOM   3100 C CG  . ASP B 1 161 ? -4.826  62.935 47.695 1.00 2.00  ? 155 ASP B CG  1 
ATOM   3101 O OD1 . ASP B 1 161 ? -5.549  63.914 47.424 1.00 34.20 ? 155 ASP B OD1 1 
ATOM   3102 O OD2 . ASP B 1 161 ? -3.667  63.057 48.109 1.00 35.32 ? 155 ASP B OD2 1 
ATOM   3103 N N   . SER B 1 162 ? -8.694  61.807 48.997 1.00 2.00  ? 156 SER B N   1 
ATOM   3104 C CA  . SER B 1 162 ? -9.851  62.672 48.850 1.00 15.15 ? 156 SER B CA  1 
ATOM   3105 C C   . SER B 1 162 ? -10.213 63.365 50.154 1.00 19.51 ? 156 SER B C   1 
ATOM   3106 O O   . SER B 1 162 ? -10.610 62.714 51.118 1.00 20.93 ? 156 SER B O   1 
ATOM   3107 C CB  . SER B 1 162 ? -11.052 61.887 48.355 1.00 12.28 ? 156 SER B CB  1 
ATOM   3108 O OG  . SER B 1 162 ? -12.073 62.783 47.955 1.00 22.52 ? 156 SER B OG  1 
ATOM   3109 N N   . GLU B 1 163 ? -10.087 64.687 50.165 1.00 14.00 ? 157 GLU B N   1 
ATOM   3110 C CA  . GLU B 1 163 ? -10.568 65.516 51.262 1.00 7.48  ? 157 GLU B CA  1 
ATOM   3111 C C   . GLU B 1 163 ? -11.904 65.028 51.803 1.00 9.09  ? 157 GLU B C   1 
ATOM   3112 O O   . GLU B 1 163 ? -11.953 64.479 52.886 1.00 2.45  ? 157 GLU B O   1 
ATOM   3113 C CB  . GLU B 1 163 ? -10.683 66.975 50.801 1.00 12.41 ? 157 GLU B CB  1 
ATOM   3114 C CG  . GLU B 1 163 ? -10.520 68.004 51.914 1.00 17.35 ? 157 GLU B CG  1 
ATOM   3115 C CD  . GLU B 1 163 ? -11.032 69.378 51.536 1.00 9.42  ? 157 GLU B CD  1 
ATOM   3116 O OE1 . GLU B 1 163 ? -11.936 69.476 50.680 1.00 57.69 ? 157 GLU B OE1 1 
ATOM   3117 O OE2 . GLU B 1 163 ? -10.523 70.367 52.097 1.00 55.42 ? 157 GLU B OE2 1 
ATOM   3118 N N   . LYS B 1 164 ? -12.923 64.965 50.965 1.00 4.98  ? 158 LYS B N   1 
ATOM   3119 C CA  . LYS B 1 164 ? -14.257 64.542 51.445 1.00 2.66  ? 158 LYS B CA  1 
ATOM   3120 C C   . LYS B 1 164 ? -14.295 63.117 52.011 1.00 38.82 ? 158 LYS B C   1 
ATOM   3121 O O   . LYS B 1 164 ? -15.085 62.818 52.894 1.00 18.69 ? 158 LYS B O   1 
ATOM   3122 C CB  . LYS B 1 164 ? -15.279 64.683 50.330 1.00 32.21 ? 158 LYS B CB  1 
ATOM   3123 C CG  . LYS B 1 164 ? -15.731 66.003 50.087 0.00 0.00  ? 158 LYS B CG  1 
ATOM   3124 C CD  . LYS B 1 164 ? -16.215 66.284 48.671 0.00 0.00  ? 158 LYS B CD  1 
ATOM   3125 C CE  . LYS B 1 164 ? -15.935 67.751 48.269 0.00 0.00  ? 158 LYS B CE  1 
ATOM   3126 N NZ  . LYS B 1 164 ? -14.473 68.091 48.025 0.00 0.00  ? 158 LYS B NZ  1 
ATOM   3127 N N   . GLU B 1 165 ? -13.323 62.306 51.613 1.00 2.52  ? 159 GLU B N   1 
ATOM   3128 C CA  . GLU B 1 165 ? -13.244 60.893 52.003 1.00 24.64 ? 159 GLU B CA  1 
ATOM   3129 C C   . GLU B 1 165 ? -12.449 60.718 53.308 1.00 10.00 ? 159 GLU B C   1 
ATOM   3130 O O   . GLU B 1 165 ? -12.810 59.911 54.156 1.00 21.48 ? 159 GLU B O   1 
ATOM   3131 C CB  . GLU B 1 165 ? -12.581 60.098 50.878 1.00 13.68 ? 159 GLU B CB  1 
ATOM   3132 C CG  . GLU B 1 165 ? -12.802 58.595 50.879 1.00 41.33 ? 159 GLU B CG  1 
ATOM   3133 C CD  . GLU B 1 165 ? -12.073 57.893 49.706 1.00 18.52 ? 159 GLU B CD  1 
ATOM   3134 O OE1 . GLU B 1 165 ? -11.976 58.489 48.594 1.00 46.27 ? 159 GLU B OE1 1 
ATOM   3135 O OE2 . GLU B 1 165 ? -11.618 56.738 49.902 1.00 88.88 ? 159 GLU B OE2 1 
ATOM   3136 N N   . ILE B 1 166 ? -11.353 61.457 53.441 1.00 7.84  ? 160 ILE B N   1 
ATOM   3137 C CA  . ILE B 1 166 ? -10.555 61.533 54.681 1.00 15.52 ? 160 ILE B CA  1 
ATOM   3138 C C   . ILE B 1 166 ? -11.377 62.026 55.876 1.00 62.05 ? 160 ILE B C   1 
ATOM   3139 O O   . ILE B 1 166 ? -11.171 61.576 56.998 1.00 7.75  ? 160 ILE B O   1 
ATOM   3140 C CB  . ILE B 1 166 ? -9.379  62.526 54.539 1.00 8.08  ? 160 ILE B CB  1 
ATOM   3141 C CG1 . ILE B 1 166 ? -8.635  62.292 53.222 1.00 9.25  ? 160 ILE B CG1 1 
ATOM   3142 C CG2 . ILE B 1 166 ? -8.462  62.453 55.749 1.00 2.00  ? 160 ILE B CG2 1 
ATOM   3143 C CD1 . ILE B 1 166 ? -7.990  60.968 53.111 1.00 5.94  ? 160 ILE B CD1 1 
ATOM   3144 N N   . MET B 1 167 ? -12.172 63.070 55.642 1.00 9.71  ? 161 MET B N   1 
ATOM   3145 C CA  . MET B 1 167 ? -12.996 63.724 56.669 1.00 38.10 ? 161 MET B CA  1 
ATOM   3146 C C   . MET B 1 167 ? -14.035 62.756 57.220 1.00 2.00  ? 161 MET B C   1 
ATOM   3147 O O   . MET B 1 167 ? -14.239 62.636 58.424 1.00 87.02 ? 161 MET B O   1 
ATOM   3148 C CB  . MET B 1 167 ? -13.731 64.941 56.072 1.00 3.06  ? 161 MET B CB  1 
ATOM   3149 C CG  . MET B 1 167 ? -12.849 65.936 55.358 1.00 26.01 ? 161 MET B CG  1 
ATOM   3150 S SD  . MET B 1 167 ? -13.663 67.514 55.094 1.00 20.32 ? 161 MET B SD  1 
ATOM   3151 C CE  . MET B 1 167 ? -15.414 66.999 54.756 1.00 13.23 ? 161 MET B CE  1 
ATOM   3152 N N   . ALA B 1 168 ? -14.664 62.059 56.301 1.00 2.00  ? 162 ALA B N   1 
ATOM   3153 C CA  . ALA B 1 168 ? -15.737 61.128 56.600 1.00 24.91 ? 162 ALA B CA  1 
ATOM   3154 C C   . ALA B 1 168 ? -15.231 59.868 57.267 1.00 10.19 ? 162 ALA B C   1 
ATOM   3155 O O   . ALA B 1 168 ? -16.004 59.179 57.914 1.00 25.08 ? 162 ALA B O   1 
ATOM   3156 C CB  . ALA B 1 168 ? -16.492 60.773 55.338 1.00 11.24 ? 162 ALA B CB  1 
ATOM   3157 N N   . GLU B 1 169 ? -13.921 59.628 57.216 1.00 14.72 ? 163 GLU B N   1 
ATOM   3158 C CA  . GLU B 1 169 ? -13.355 58.442 57.867 1.00 2.00  ? 163 GLU B CA  1 
ATOM   3159 C C   . GLU B 1 169 ? -13.192 58.774 59.345 1.00 57.53 ? 163 GLU B C   1 
ATOM   3160 O O   . GLU B 1 169 ? -13.956 58.279 60.174 1.00 21.61 ? 163 GLU B O   1 
ATOM   3161 C CB  . GLU B 1 169 ? -12.013 58.051 57.228 1.00 9.55  ? 163 GLU B CB  1 
ATOM   3162 C CG  . GLU B 1 169 ? -11.151 57.069 58.048 1.00 12.39 ? 163 GLU B CG  1 
ATOM   3163 C CD  . GLU B 1 169 ? -11.702 55.652 58.067 1.00 19.71 ? 163 GLU B CD  1 
ATOM   3164 O OE1 . GLU B 1 169 ? -12.594 55.336 57.248 1.00 33.15 ? 163 GLU B OE1 1 
ATOM   3165 O OE2 . GLU B 1 169 ? -11.213 54.838 58.884 1.00 7.24  ? 163 GLU B OE2 1 
ATOM   3166 N N   . ILE B 1 170 ? -12.426 59.829 59.612 1.00 2.00  ? 164 ILE B N   1 
ATOM   3167 C CA  . ILE B 1 170 ? -12.418 60.476 60.918 1.00 22.92 ? 164 ILE B CA  1 
ATOM   3168 C C   . ILE B 1 170 ? -13.807 60.627 61.583 1.00 3.41  ? 164 ILE B C   1 
ATOM   3169 O O   . ILE B 1 170 ? -14.023 60.118 62.687 1.00 33.83 ? 164 ILE B O   1 
ATOM   3170 C CB  . ILE B 1 170 ? -11.735 61.865 60.821 1.00 9.21  ? 164 ILE B CB  1 
ATOM   3171 C CG1 . ILE B 1 170 ? -10.303 61.697 60.302 1.00 7.96  ? 164 ILE B CG1 1 
ATOM   3172 C CG2 . ILE B 1 170 ? -11.764 62.551 62.179 1.00 24.87 ? 164 ILE B CG2 1 
ATOM   3173 C CD1 . ILE B 1 170 ? -9.624  62.996 59.830 1.00 15.85 ? 164 ILE B CD1 1 
ATOM   3174 N N   . TYR B 1 171 ? -14.715 61.349 60.933 1.00 14.35 ? 165 TYR B N   1 
ATOM   3175 C CA  . TYR B 1 171 ? -16.035 61.652 61.494 1.00 12.94 ? 165 TYR B CA  1 
ATOM   3176 C C   . TYR B 1 171 ? -16.826 60.390 61.844 1.00 28.71 ? 165 TYR B C   1 
ATOM   3177 O O   . TYR B 1 171 ? -17.652 60.400 62.753 1.00 63.64 ? 165 TYR B O   1 
ATOM   3178 C CB  . TYR B 1 171 ? -16.844 62.498 60.515 1.00 26.65 ? 165 TYR B CB  1 
ATOM   3179 C CG  . TYR B 1 171 ? -18.245 62.831 60.993 1.00 19.81 ? 165 TYR B CG  1 
ATOM   3180 C CD1 . TYR B 1 171 ? -18.488 63.983 61.732 1.00 26.23 ? 165 TYR B CD1 1 
ATOM   3181 C CD2 . TYR B 1 171 ? -19.330 62.050 60.622 1.00 44.77 ? 165 TYR B CD2 1 
ATOM   3182 C CE1 . TYR B 1 171 ? -19.769 64.360 62.065 1.00 70.30 ? 165 TYR B CE1 1 
ATOM   3183 C CE2 . TYR B 1 171 ? -20.613 62.415 60.956 1.00 41.99 ? 165 TYR B CE2 1 
ATOM   3184 C CZ  . TYR B 1 171 ? -20.829 63.581 61.664 1.00 56.48 ? 165 TYR B CZ  1 
ATOM   3185 O OH  . TYR B 1 171 ? -22.110 64.032 61.872 1.00 62.98 ? 165 TYR B OH  1 
ATOM   3186 N N   . LYS B 1 172 ? -16.569 59.311 61.112 1.00 23.00 ? 166 LYS B N   1 
ATOM   3187 C CA  . LYS B 1 172 ? -17.283 58.057 61.336 1.00 13.03 ? 166 LYS B CA  1 
ATOM   3188 C C   . LYS B 1 172 ? -16.486 57.007 62.117 1.00 29.40 ? 166 LYS B C   1 
ATOM   3189 O O   . LYS B 1 172 ? -17.081 56.140 62.742 1.00 27.18 ? 166 LYS B O   1 
ATOM   3190 C CB  . LYS B 1 172 ? -17.754 57.479 59.989 1.00 16.52 ? 166 LYS B CB  1 
ATOM   3191 C CG  . LYS B 1 172 ? -18.612 58.468 59.193 1.00 78.37 ? 166 LYS B CG  1 
ATOM   3192 C CD  . LYS B 1 172 ? -19.274 57.857 57.965 1.00 66.09 ? 166 LYS B CD  1 
ATOM   3193 C CE  . LYS B 1 172 ? -19.890 58.952 57.063 1.00 64.43 ? 166 LYS B CE  1 
ATOM   3194 N NZ  . LYS B 1 172 ? -20.873 59.886 57.753 1.00 37.34 ? 166 LYS B NZ  1 
ATOM   3195 N N   . ASN B 1 173 ? -15.164 57.172 62.208 1.00 15.65 ? 167 ASN B N   1 
ATOM   3196 C CA  . ASN B 1 173 ? -14.281 56.095 62.692 1.00 2.95  ? 167 ASN B CA  1 
ATOM   3197 C C   . ASN B 1 173 ? -13.110 56.491 63.599 1.00 6.10  ? 167 ASN B C   1 
ATOM   3198 O O   . ASN B 1 173 ? -12.499 55.628 64.224 1.00 12.80 ? 167 ASN B O   1 
ATOM   3199 C CB  . ASN B 1 173 ? -13.719 55.279 61.507 1.00 16.31 ? 167 ASN B CB  1 
ATOM   3200 C CG  . ASN B 1 173 ? -14.626 54.129 61.093 1.00 24.64 ? 167 ASN B CG  1 
ATOM   3201 O OD1 . ASN B 1 173 ? -14.558 53.042 61.655 1.00 67.28 ? 167 ASN B OD1 1 
ATOM   3202 N ND2 . ASN B 1 173 ? -15.453 54.357 60.086 1.00 53.04 ? 167 ASN B ND2 1 
ATOM   3203 N N   . GLY B 1 174 ? -12.793 57.774 63.705 1.00 5.18  ? 168 GLY B N   1 
ATOM   3204 C CA  . GLY B 1 174 ? -11.696 58.137 64.586 1.00 2.00  ? 168 GLY B CA  1 
ATOM   3205 C C   . GLY B 1 174 ? -10.570 58.907 63.922 1.00 46.23 ? 168 GLY B C   1 
ATOM   3206 O O   . GLY B 1 174 ? -10.437 58.897 62.701 1.00 2.78  ? 168 GLY B O   1 
ATOM   3207 N N   . PRO B 1 175 ? -9.724  59.584 64.711 1.00 4.64  ? 169 PRO B N   1 
ATOM   3208 C CA  . PRO B 1 175 ? -8.453  60.106 64.181 1.00 6.60  ? 169 PRO B CA  1 
ATOM   3209 C C   . PRO B 1 175 ? -7.723  59.153 63.214 1.00 72.95 ? 169 PRO B C   1 
ATOM   3210 O O   . PRO B 1 175 ? -7.919  57.943 63.259 1.00 2.00  ? 169 PRO B O   1 
ATOM   3211 C CB  . PRO B 1 175 ? -7.629  60.376 65.446 1.00 2.00  ? 169 PRO B CB  1 
ATOM   3212 C CG  . PRO B 1 175 ? -8.648  60.634 66.514 1.00 2.00  ? 169 PRO B CG  1 
ATOM   3213 C CD  . PRO B 1 175 ? -9.773  59.662 66.185 1.00 2.00  ? 169 PRO B CD  1 
ATOM   3214 N N   . VAL B 1 176 ? -6.912  59.707 62.315 1.00 23.55 ? 170 VAL B N   1 
ATOM   3215 C CA  . VAL B 1 176 ? -6.072  58.885 61.442 1.00 10.08 ? 170 VAL B CA  1 
ATOM   3216 C C   . VAL B 1 176 ? -4.585  59.152 61.584 1.00 13.85 ? 170 VAL B C   1 
ATOM   3217 O O   . VAL B 1 176 ? -4.161  60.137 62.186 1.00 6.58  ? 170 VAL B O   1 
ATOM   3218 C CB  . VAL B 1 176 ? -6.438  59.052 59.950 1.00 14.31 ? 170 VAL B CB  1 
ATOM   3219 C CG1 . VAL B 1 176 ? -7.851  58.572 59.695 1.00 2.00  ? 170 VAL B CG1 1 
ATOM   3220 C CG2 . VAL B 1 176 ? -6.270  60.462 59.539 1.00 8.40  ? 170 VAL B CG2 1 
ATOM   3221 N N   . GLU B 1 177 ? -3.801  58.177 61.161 1.00 2.00  ? 171 GLU B N   1 
ATOM   3222 C CA  . GLU B 1 177 ? -2.418  58.424 60.916 1.00 24.75 ? 171 GLU B CA  1 
ATOM   3223 C C   . GLU B 1 177 ? -2.204  58.928 59.480 1.00 57.80 ? 171 GLU B C   1 
ATOM   3224 O O   . GLU B 1 177 ? -2.978  58.630 58.563 1.00 3.18  ? 171 GLU B O   1 
ATOM   3225 C CB  . GLU B 1 177 ? -1.602  57.167 61.173 1.00 2.00  ? 171 GLU B CB  1 
ATOM   3226 C CG  . GLU B 1 177 ? -0.133  57.499 61.061 1.00 5.04  ? 171 GLU B CG  1 
ATOM   3227 C CD  . GLU B 1 177 ? 0.789   56.434 61.573 1.00 2.00  ? 171 GLU B CD  1 
ATOM   3228 O OE1 . GLU B 1 177 ? 0.465   55.222 61.476 1.00 2.45  ? 171 GLU B OE1 1 
ATOM   3229 O OE2 . GLU B 1 177 ? 1.888   56.828 61.989 1.00 2.00  ? 171 GLU B OE2 1 
ATOM   3230 N N   . GLY B 1 178 ? -1.205  59.787 59.334 1.00 2.00  ? 172 GLY B N   1 
ATOM   3231 C CA  . GLY B 1 178 ? -0.844  60.322 58.043 1.00 2.10  ? 172 GLY B CA  1 
ATOM   3232 C C   . GLY B 1 178 ? 0.577   60.846 58.029 1.00 4.60  ? 172 GLY B C   1 
ATOM   3233 O O   . GLY B 1 178 ? 1.322   60.742 59.023 1.00 2.00  ? 172 GLY B O   1 
ATOM   3234 N N   . ALA B 1 179 ? 0.978   61.397 56.898 1.00 11.70 ? 173 ALA B N   1 
ATOM   3235 C CA  . ALA B 1 179 ? 2.311   61.968 56.797 1.00 10.65 ? 173 ALA B CA  1 
ATOM   3236 C C   . ALA B 1 179 ? 2.415   63.174 55.861 1.00 11.59 ? 173 ALA B C   1 
ATOM   3237 O O   . ALA B 1 179 ? 1.571   63.392 54.980 1.00 15.53 ? 173 ALA B O   1 
ATOM   3238 C CB  . ALA B 1 179 ? 3.318   60.884 56.384 1.00 10.98 ? 173 ALA B CB  1 
ATOM   3239 N N   . PHE B 1 180 ? 3.433   63.989 56.120 1.00 19.07 ? 174 PHE B N   1 
ATOM   3240 C CA  . PHE B 1 180 ? 3.726   65.136 55.295 1.00 4.25  ? 174 PHE B CA  1 
ATOM   3241 C C   . PHE B 1 180 ? 5.226   65.441 55.183 1.00 13.85 ? 174 PHE B C   1 
ATOM   3242 O O   . PHE B 1 180 ? 6.036   65.004 56.002 1.00 2.00  ? 174 PHE B O   1 
ATOM   3243 C CB  . PHE B 1 180 ? 2.948   66.372 55.800 1.00 2.00  ? 174 PHE B CB  1 
ATOM   3244 C CG  . PHE B 1 180 ? 3.399   66.869 57.149 1.00 24.80 ? 174 PHE B CG  1 
ATOM   3245 C CD1 . PHE B 1 180 ? 3.474   66.012 58.225 1.00 65.08 ? 174 PHE B CD1 1 
ATOM   3246 C CD2 . PHE B 1 180 ? 3.833   68.173 57.311 1.00 35.81 ? 174 PHE B CD2 1 
ATOM   3247 C CE1 . PHE B 1 180 ? 3.980   66.438 59.420 1.00 17.51 ? 174 PHE B CE1 1 
ATOM   3248 C CE2 . PHE B 1 180 ? 4.343   68.604 58.511 1.00 2.00  ? 174 PHE B CE2 1 
ATOM   3249 C CZ  . PHE B 1 180 ? 4.418   67.733 59.568 1.00 66.02 ? 174 PHE B CZ  1 
ATOM   3250 N N   . THR B 1 181 ? 5.613   66.063 54.079 1.00 8.05  ? 175 THR B N   1 
ATOM   3251 C CA  . THR B 1 181 ? 6.991   66.477 53.930 1.00 39.76 ? 175 THR B CA  1 
ATOM   3252 C C   . THR B 1 181 ? 7.284   67.690 54.795 1.00 12.46 ? 175 THR B C   1 
ATOM   3253 O O   . THR B 1 181 ? 6.527   68.655 54.829 1.00 6.98  ? 175 THR B O   1 
ATOM   3254 C CB  . THR B 1 181 ? 7.317   66.788 52.485 1.00 11.88 ? 175 THR B CB  1 
ATOM   3255 O OG1 . THR B 1 181 ? 6.929   65.672 51.679 1.00 7.28  ? 175 THR B OG1 1 
ATOM   3256 C CG2 . THR B 1 181 ? 8.819   67.053 52.324 1.00 11.91 ? 175 THR B CG2 1 
ATOM   3257 N N   . VAL B 1 182 ? 8.233   67.515 55.682 1.00 2.00  ? 176 VAL B N   1 
ATOM   3258 C CA  . VAL B 1 182 ? 8.623   68.598 56.558 1.00 2.00  ? 176 VAL B CA  1 
ATOM   3259 C C   . VAL B 1 182 ? 9.733   69.459 55.968 1.00 23.00 ? 176 VAL B C   1 
ATOM   3260 O O   . VAL B 1 182 ? 10.798  68.957 55.622 1.00 11.39 ? 176 VAL B O   1 
ATOM   3261 C CB  . VAL B 1 182 ? 9.066   68.071 57.917 1.00 2.12  ? 176 VAL B CB  1 
ATOM   3262 C CG1 . VAL B 1 182 ? 9.659   69.212 58.775 1.00 8.63  ? 176 VAL B CG1 1 
ATOM   3263 C CG2 . VAL B 1 182 ? 7.864   67.467 58.630 1.00 24.17 ? 176 VAL B CG2 1 
ATOM   3264 N N   . PHE B 1 183 ? 9.468   70.759 55.890 1.00 9.33  ? 177 PHE B N   1 
ATOM   3265 C CA  . PHE B 1 183 ? 10.504  71.770 55.729 1.00 22.04 ? 177 PHE B CA  1 
ATOM   3266 C C   . PHE B 1 183 ? 10.986  72.448 57.024 1.00 44.57 ? 177 PHE B C   1 
ATOM   3267 O O   . PHE B 1 183 ? 10.317  72.416 58.052 1.00 19.96 ? 177 PHE B O   1 
ATOM   3268 C CB  . PHE B 1 183 ? 10.017  72.821 54.756 1.00 22.24 ? 177 PHE B CB  1 
ATOM   3269 C CG  . PHE B 1 183 ? 9.707   72.272 53.418 1.00 16.02 ? 177 PHE B CG  1 
ATOM   3270 C CD1 . PHE B 1 183 ? 8.525   71.584 53.208 1.00 80.87 ? 177 PHE B CD1 1 
ATOM   3271 C CD2 . PHE B 1 183 ? 10.630  72.356 52.391 1.00 31.88 ? 177 PHE B CD2 1 
ATOM   3272 C CE1 . PHE B 1 183 ? 8.271   70.980 52.008 1.00 32.49 ? 177 PHE B CE1 1 
ATOM   3273 C CE2 . PHE B 1 183 ? 10.381  71.756 51.181 1.00 55.49 ? 177 PHE B CE2 1 
ATOM   3274 C CZ  . PHE B 1 183 ? 9.202   71.061 50.986 1.00 63.42 ? 177 PHE B CZ  1 
ATOM   3275 N N   . SER B 1 184 ? 12.124  73.124 56.948 1.00 6.85  ? 178 SER B N   1 
ATOM   3276 C CA  . SER B 1 184 ? 12.696  73.786 58.112 1.00 35.80 ? 178 SER B CA  1 
ATOM   3277 C C   . SER B 1 184 ? 11.889  74.964 58.660 1.00 2.60  ? 178 SER B C   1 
ATOM   3278 O O   . SER B 1 184 ? 12.032  75.318 59.827 1.00 59.48 ? 178 SER B O   1 
ATOM   3279 C CB  . SER B 1 184 ? 14.139  74.233 57.826 1.00 2.00  ? 178 SER B CB  1 
ATOM   3280 O OG  . SER B 1 184 ? 14.233  75.079 56.691 1.00 25.38 ? 178 SER B OG  1 
ATOM   3281 N N   . ASP B 1 185 ? 10.973  75.501 57.862 1.00 31.33 ? 179 ASP B N   1 
ATOM   3282 C CA  . ASP B 1 185 ? 10.088  76.565 58.354 1.00 10.27 ? 179 ASP B CA  1 
ATOM   3283 C C   . ASP B 1 185 ? 9.024   75.996 59.287 1.00 88.21 ? 179 ASP B C   1 
ATOM   3284 O O   . ASP B 1 185 ? 8.558   76.674 60.198 1.00 25.40 ? 179 ASP B O   1 
ATOM   3285 C CB  . ASP B 1 185 ? 9.429   77.315 57.179 1.00 3.32  ? 179 ASP B CB  1 
ATOM   3286 C CG  . ASP B 1 185 ? 8.393   76.485 56.458 1.00 15.97 ? 179 ASP B CG  1 
ATOM   3287 O OD1 . ASP B 1 185 ? 8.587   75.250 56.359 1.00 28.95 ? 179 ASP B OD1 1 
ATOM   3288 O OD2 . ASP B 1 185 ? 7.384   77.062 56.000 1.00 57.41 ? 179 ASP B OD2 1 
ATOM   3289 N N   . PHE B 1 186 ? 8.702   74.721 59.099 1.00 6.93  ? 180 PHE B N   1 
ATOM   3290 C CA  . PHE B 1 186 ? 7.816   74.004 60.033 1.00 16.77 ? 180 PHE B CA  1 
ATOM   3291 C C   . PHE B 1 186 ? 8.340   74.033 61.467 1.00 20.48 ? 180 PHE B C   1 
ATOM   3292 O O   . PHE B 1 186 ? 7.570   74.168 62.410 1.00 15.63 ? 180 PHE B O   1 
ATOM   3293 C CB  . PHE B 1 186 ? 7.668   72.540 59.605 1.00 5.28  ? 180 PHE B CB  1 
ATOM   3294 C CG  . PHE B 1 186 ? 6.739   71.747 60.466 1.00 10.82 ? 180 PHE B CG  1 
ATOM   3295 C CD1 . PHE B 1 186 ? 5.366   72.000 60.423 1.00 34.14 ? 180 PHE B CD1 1 
ATOM   3296 C CD2 . PHE B 1 186 ? 7.229   70.798 61.357 1.00 10.19 ? 180 PHE B CD2 1 
ATOM   3297 C CE1 . PHE B 1 186 ? 4.501   71.342 61.269 1.00 15.46 ? 180 PHE B CE1 1 
ATOM   3298 C CE2 . PHE B 1 186 ? 6.381   70.122 62.210 1.00 2.00  ? 180 PHE B CE2 1 
ATOM   3299 C CZ  . PHE B 1 186 ? 5.004   70.402 62.180 1.00 2.22  ? 180 PHE B CZ  1 
ATOM   3300 N N   . LEU B 1 187 ? 9.639   73.797 61.637 1.00 16.28 ? 181 LEU B N   1 
ATOM   3301 C CA  . LEU B 1 187 ? 10.170  73.429 62.950 1.00 2.00  ? 181 LEU B CA  1 
ATOM   3302 C C   . LEU B 1 187 ? 9.868   74.442 64.047 1.00 20.94 ? 181 LEU B C   1 
ATOM   3303 O O   . LEU B 1 187 ? 9.690   74.088 65.208 1.00 38.27 ? 181 LEU B O   1 
ATOM   3304 C CB  . LEU B 1 187 ? 11.675  73.182 62.846 1.00 6.08  ? 181 LEU B CB  1 
ATOM   3305 C CG  . LEU B 1 187 ? 12.002  72.101 61.824 1.00 36.45 ? 181 LEU B CG  1 
ATOM   3306 C CD1 . LEU B 1 187 ? 13.411  72.271 61.331 1.00 31.39 ? 181 LEU B CD1 1 
ATOM   3307 C CD2 . LEU B 1 187 ? 11.803  70.750 62.454 1.00 33.20 ? 181 LEU B CD2 1 
ATOM   3308 N N   . THR B 1 188 ? 9.702   75.690 63.640 1.00 35.97 ? 182 THR B N   1 
ATOM   3309 C CA  . THR B 1 188 ? 9.506   76.798 64.567 1.00 27.70 ? 182 THR B CA  1 
ATOM   3310 C C   . THR B 1 188 ? 8.082   77.352 64.478 1.00 31.57 ? 182 THR B C   1 
ATOM   3311 O O   . THR B 1 188 ? 7.879   78.566 64.485 1.00 37.44 ? 182 THR B O   1 
ATOM   3312 C CB  . THR B 1 188 ? 10.493  77.941 64.262 1.00 40.03 ? 182 THR B CB  1 
ATOM   3313 O OG1 . THR B 1 188 ? 10.163  78.536 62.999 1.00 36.71 ? 182 THR B OG1 1 
ATOM   3314 C CG2 . THR B 1 188 ? 11.920  77.403 64.203 1.00 36.94 ? 182 THR B CG2 1 
ATOM   3315 N N   . TYR B 1 189 ? 7.114   76.463 64.280 1.00 25.00 ? 183 TYR B N   1 
ATOM   3316 C CA  . TYR B 1 189 ? 5.711   76.857 64.268 1.00 3.58  ? 183 TYR B CA  1 
ATOM   3317 C C   . TYR B 1 189 ? 5.207   77.036 65.702 1.00 24.81 ? 183 TYR B C   1 
ATOM   3318 O O   . TYR B 1 189 ? 5.606   76.293 66.601 1.00 21.81 ? 183 TYR B O   1 
ATOM   3319 C CB  . TYR B 1 189 ? 4.855   75.809 63.532 1.00 13.70 ? 183 TYR B CB  1 
ATOM   3320 C CG  . TYR B 1 189 ? 3.339   75.915 63.781 1.00 30.40 ? 183 TYR B CG  1 
ATOM   3321 C CD1 . TYR B 1 189 ? 2.738   75.217 64.816 1.00 10.30 ? 183 TYR B CD1 1 
ATOM   3322 C CD2 . TYR B 1 189 ? 2.506   76.646 62.923 1.00 67.18 ? 183 TYR B CD2 1 
ATOM   3323 C CE1 . TYR B 1 189 ? 1.355   75.228 64.983 1.00 6.74  ? 183 TYR B CE1 1 
ATOM   3324 C CE2 . TYR B 1 189 ? 1.102   76.657 63.088 1.00 2.00  ? 183 TYR B CE2 1 
ATOM   3325 C CZ  . TYR B 1 189 ? 0.540   75.938 64.106 1.00 17.04 ? 183 TYR B CZ  1 
ATOM   3326 O OH  . TYR B 1 189 ? -0.838  75.817 64.181 1.00 5.87  ? 183 TYR B OH  1 
ATOM   3327 N N   . LYS B 1 190 ? 4.191   77.884 65.856 1.00 25.14 ? 184 LYS B N   1 
ATOM   3328 C CA  . LYS B 1 190 ? 3.709   78.300 67.167 1.00 51.01 ? 184 LYS B CA  1 
ATOM   3329 C C   . LYS B 1 190 ? 2.187   78.413 67.222 1.00 29.72 ? 184 LYS B C   1 
ATOM   3330 O O   . LYS B 1 190 ? 1.577   78.102 68.234 1.00 29.28 ? 184 LYS B O   1 
ATOM   3331 C CB  . LYS B 1 190 ? 4.350   79.647 67.555 1.00 46.06 ? 184 LYS B CB  1 
ATOM   3332 C CG  . LYS B 1 190 ? 5.916   79.837 67.365 0.00 0.00  ? 184 LYS B CG  1 
ATOM   3333 C CD  . LYS B 1 190 ? 6.384   81.376 67.304 0.00 0.00  ? 184 LYS B CD  1 
ATOM   3334 C CE  . LYS B 1 190 ? 7.683   81.645 66.496 0.00 0.00  ? 184 LYS B CE  1 
ATOM   3335 N NZ  . LYS B 1 190 ? 7.686   82.986 65.803 0.00 0.00  ? 184 LYS B NZ  1 
ATOM   3336 N N   . SER B 1 191 ? 1.589   78.940 66.158 1.00 2.00  ? 185 SER B N   1 
ATOM   3337 C CA  . SER B 1 191 ? 0.186   79.347 66.181 1.00 28.03 ? 185 SER B CA  1 
ATOM   3338 C C   . SER B 1 191 ? -0.335  79.552 64.762 1.00 2.00  ? 185 SER B C   1 
ATOM   3339 O O   . SER B 1 191 ? 0.443   79.833 63.847 1.00 42.12 ? 185 SER B O   1 
ATOM   3340 C CB  . SER B 1 191 ? 0.053   80.650 66.980 1.00 16.47 ? 185 SER B CB  1 
ATOM   3341 O OG  . SER B 1 191 ? -0.656  81.652 66.266 1.00 30.47 ? 185 SER B OG  1 
ATOM   3342 N N   . GLY B 1 192 ? -1.645  79.452 64.580 1.00 33.43 ? 186 GLY B N   1 
ATOM   3343 C CA  . GLY B 1 192 ? -2.231  79.763 63.281 1.00 22.69 ? 186 GLY B CA  1 
ATOM   3344 C C   . GLY B 1 192 ? -2.297  78.572 62.342 1.00 19.39 ? 186 GLY B C   1 
ATOM   3345 O O   . GLY B 1 192 ? -2.321  77.421 62.796 1.00 15.24 ? 186 GLY B O   1 
ATOM   3346 N N   . VAL B 1 193 ? -2.458  78.836 61.048 1.00 39.00 ? 187 VAL B N   1 
ATOM   3347 C CA  . VAL B 1 193 ? -2.444  77.761 60.056 1.00 26.69 ? 187 VAL B CA  1 
ATOM   3348 C C   . VAL B 1 193 ? -1.175  77.705 59.199 1.00 19.42 ? 187 VAL B C   1 
ATOM   3349 O O   . VAL B 1 193 ? -0.860  78.633 58.449 1.00 82.64 ? 187 VAL B O   1 
ATOM   3350 C CB  . VAL B 1 193 ? -3.645  77.807 59.105 1.00 13.02 ? 187 VAL B CB  1 
ATOM   3351 C CG1 . VAL B 1 193 ? -3.532  76.655 58.112 1.00 22.03 ? 187 VAL B CG1 1 
ATOM   3352 C CG2 . VAL B 1 193 ? -4.946  77.700 59.879 1.00 3.93  ? 187 VAL B CG2 1 
ATOM   3353 N N   . TYR B 1 194 ? -0.537  76.541 59.240 1.00 7.82  ? 188 TYR B N   1 
ATOM   3354 C CA  . TYR B 1 194 ? 0.627   76.239 58.425 1.00 29.52 ? 188 TYR B CA  1 
ATOM   3355 C C   . TYR B 1 194 ? 0.392   76.201 56.885 1.00 24.86 ? 188 TYR B C   1 
ATOM   3356 O O   . TYR B 1 194 ? -0.516  75.500 56.375 1.00 14.83 ? 188 TYR B O   1 
ATOM   3357 C CB  . TYR B 1 194 ? 1.224   74.921 58.907 1.00 17.48 ? 188 TYR B CB  1 
ATOM   3358 C CG  . TYR B 1 194 ? 2.529   74.601 58.276 1.00 2.00  ? 188 TYR B CG  1 
ATOM   3359 C CD1 . TYR B 1 194 ? 3.685   75.256 58.669 1.00 13.72 ? 188 TYR B CD1 1 
ATOM   3360 C CD2 . TYR B 1 194 ? 2.593   73.744 57.203 1.00 15.40 ? 188 TYR B CD2 1 
ATOM   3361 C CE1 . TYR B 1 194 ? 4.865   75.079 57.995 1.00 6.02  ? 188 TYR B CE1 1 
ATOM   3362 C CE2 . TYR B 1 194 ? 3.765   73.551 56.523 1.00 27.26 ? 188 TYR B CE2 1 
ATOM   3363 C CZ  . TYR B 1 194 ? 4.888   74.226 56.916 1.00 38.23 ? 188 TYR B CZ  1 
ATOM   3364 O OH  . TYR B 1 194 ? 6.008   74.099 56.158 1.00 2.49  ? 188 TYR B OH  1 
ATOM   3365 N N   . LYS B 1 195 ? 1.141   77.077 56.190 1.00 35.23 ? 189 LYS B N   1 
ATOM   3366 C CA  . LYS B 1 195 ? 1.367   77.038 54.737 1.00 3.43  ? 189 LYS B CA  1 
ATOM   3367 C C   . LYS B 1 195 ? 2.886   77.049 54.615 1.00 24.52 ? 189 LYS B C   1 
ATOM   3368 O O   . LYS B 1 195 ? 3.584   77.813 55.298 1.00 17.43 ? 189 LYS B O   1 
ATOM   3369 C CB  . LYS B 1 195 ? 0.782   78.295 54.047 1.00 19.92 ? 189 LYS B CB  1 
ATOM   3370 C CG  . LYS B 1 195 ? 0.216   78.122 52.604 1.00 27.22 ? 189 LYS B CG  1 
ATOM   3371 C CD  . LYS B 1 195 ? 1.320   78.269 51.442 1.00 37.47 ? 189 LYS B CD  1 
ATOM   3372 C CE  . LYS B 1 195 ? 0.778   78.737 50.064 1.00 20.41 ? 189 LYS B CE  1 
ATOM   3373 N NZ  . LYS B 1 195 ? -0.046  77.686 49.360 1.00 32.22 ? 189 LYS B NZ  1 
ATOM   3374 N N   . HIS B 1 196 ? 3.426   76.162 53.793 1.00 21.69 ? 190 HIS B N   1 
ATOM   3375 C CA  . HIS B 1 196 ? 4.874   76.161 53.610 1.00 12.43 ? 190 HIS B CA  1 
ATOM   3376 C C   . HIS B 1 196 ? 5.233   77.327 52.704 1.00 21.36 ? 190 HIS B C   1 
ATOM   3377 O O   . HIS B 1 196 ? 4.702   77.443 51.599 1.00 62.14 ? 190 HIS B O   1 
ATOM   3378 C CB  . HIS B 1 196 ? 5.332   74.837 53.009 1.00 2.00  ? 190 HIS B CB  1 
ATOM   3379 C CG  . HIS B 1 196 ? 6.741   74.844 52.534 1.00 28.93 ? 190 HIS B CG  1 
ATOM   3380 N ND1 . HIS B 1 196 ? 7.800   75.068 53.376 1.00 18.71 ? 190 HIS B ND1 1 
ATOM   3381 C CD2 . HIS B 1 196 ? 7.254   74.799 51.281 1.00 43.94 ? 190 HIS B CD2 1 
ATOM   3382 C CE1 . HIS B 1 196 ? 8.904   75.190 52.670 1.00 60.48 ? 190 HIS B CE1 1 
ATOM   3383 N NE2 . HIS B 1 196 ? 8.604   75.030 51.395 1.00 9.03  ? 190 HIS B NE2 1 
ATOM   3384 N N   . GLU B 1 197 ? 5.828   78.337 53.318 1.00 80.38 ? 191 GLU B N   1 
ATOM   3385 C CA  . GLU B 1 197 ? 6.353   79.470 52.577 1.00 46.15 ? 191 GLU B CA  1 
ATOM   3386 C C   . GLU B 1 197 ? 7.805   79.193 52.247 1.00 62.07 ? 191 GLU B C   1 
ATOM   3387 O O   . GLU B 1 197 ? 8.106   78.423 51.341 1.00 33.59 ? 191 GLU B O   1 
ATOM   3388 C CB  . GLU B 1 197 ? 6.246   80.744 53.410 1.00 6.14  ? 191 GLU B CB  1 
ATOM   3389 C CG  . GLU B 1 197 ? 5.201   81.750 52.893 1.00 27.36 ? 191 GLU B CG  1 
ATOM   3390 C CD  . GLU B 1 197 ? 3.732   81.408 53.274 1.00 89.14 ? 191 GLU B CD  1 
ATOM   3391 O OE1 . GLU B 1 197 ? 3.388   81.423 54.483 1.00 35.31 ? 191 GLU B OE1 1 
ATOM   3392 O OE2 . GLU B 1 197 ? 2.898   81.209 52.351 1.00 72.45 ? 191 GLU B OE2 1 
ATOM   3393 N N   . ALA B 1 198 ? 8.701   79.720 53.066 1.00 22.11 ? 192 ALA B N   1 
ATOM   3394 C CA  . ALA B 1 198 ? 10.108  79.409 52.923 1.00 32.60 ? 192 ALA B CA  1 
ATOM   3395 C C   . ALA B 1 198 ? 10.430  78.089 53.630 1.00 39.56 ? 192 ALA B C   1 
ATOM   3396 O O   . ALA B 1 198 ? 9.535   77.413 54.124 1.00 87.08 ? 192 ALA B O   1 
ATOM   3397 C CB  . ALA B 1 198 ? 10.922  80.517 53.496 1.00 23.34 ? 192 ALA B CB  1 
ATOM   3398 N N   . GLY B 1 199 ? 11.706  77.719 53.649 1.00 24.03 ? 193 GLY B N   1 
ATOM   3399 C CA  . GLY B 1 199 ? 12.122  76.499 54.304 1.00 42.60 ? 193 GLY B CA  1 
ATOM   3400 C C   . GLY B 1 199 ? 12.791  75.529 53.355 1.00 26.10 ? 193 GLY B C   1 
ATOM   3401 O O   . GLY B 1 199 ? 12.377  75.391 52.205 1.00 51.10 ? 193 GLY B O   1 
ATOM   3402 N N   . ASP B 1 200 ? 13.706  74.742 53.909 1.00 66.53 ? 194 ASP B N   1 
ATOM   3403 C CA  . ASP B 1 200 ? 14.421  73.702 53.177 1.00 17.93 ? 194 ASP B CA  1 
ATOM   3404 C C   . ASP B 1 200 ? 13.936  72.298 53.597 1.00 28.91 ? 194 ASP B C   1 
ATOM   3405 O O   . ASP B 1 200 ? 13.406  72.119 54.693 1.00 18.37 ? 194 ASP B O   1 
ATOM   3406 C CB  . ASP B 1 200 ? 15.926  73.848 53.424 1.00 20.10 ? 194 ASP B CB  1 
ATOM   3407 C CG  . ASP B 1 200 ? 16.831  73.734 52.220 0.00 0.00  ? 194 ASP B CG  1 
ATOM   3408 O OD1 . ASP B 1 200 ? 16.499  72.946 51.314 0.00 0.00  ? 194 ASP B OD1 1 
ATOM   3409 O OD2 . ASP B 1 200 ? 17.878  74.414 52.172 0.00 0.00  ? 194 ASP B OD2 1 
ATOM   3410 N N   . VAL B 1 201 ? 14.164  71.301 52.747 1.00 4.27  ? 195 VAL B N   1 
ATOM   3411 C CA  . VAL B 1 201 ? 13.541  69.991 52.921 1.00 55.53 ? 195 VAL B CA  1 
ATOM   3412 C C   . VAL B 1 201 ? 14.264  69.199 53.992 1.00 18.28 ? 195 VAL B C   1 
ATOM   3413 O O   . VAL B 1 201 ? 15.485  69.140 54.005 1.00 29.51 ? 195 VAL B O   1 
ATOM   3414 C CB  . VAL B 1 201 ? 13.515  69.160 51.594 1.00 13.59 ? 195 VAL B CB  1 
ATOM   3415 C CG1 . VAL B 1 201 ? 13.171  70.058 50.415 1.00 94.90 ? 195 VAL B CG1 1 
ATOM   3416 C CG2 . VAL B 1 201 ? 14.847  68.468 51.361 1.00 44.19 ? 195 VAL B CG2 1 
ATOM   3417 N N   . MET B 1 202 ? 13.501  68.614 54.908 1.00 72.45 ? 196 MET B N   1 
ATOM   3418 C CA  . MET B 1 202 ? 14.086  67.842 55.999 1.00 10.70 ? 196 MET B CA  1 
ATOM   3419 C C   . MET B 1 202 ? 13.624  66.381 56.053 1.00 53.05 ? 196 MET B C   1 
ATOM   3420 O O   . MET B 1 202 ? 14.294  65.530 56.648 1.00 64.29 ? 196 MET B O   1 
ATOM   3421 C CB  . MET B 1 202 ? 13.800  68.529 57.337 1.00 70.22 ? 196 MET B CB  1 
ATOM   3422 C CG  . MET B 1 202 ? 14.292  69.970 57.403 1.00 38.42 ? 196 MET B CG  1 
ATOM   3423 S SD  . MET B 1 202 ? 15.196  70.431 58.900 1.00 78.40 ? 196 MET B SD  1 
ATOM   3424 C CE  . MET B 1 202 ? 14.549  69.225 60.088 1.00 16.04 ? 196 MET B CE  1 
ATOM   3425 N N   . GLY B 1 203 ? 12.464  66.101 55.464 1.00 27.56 ? 197 GLY B N   1 
ATOM   3426 C CA  . GLY B 1 203 ? 12.004  64.725 55.339 1.00 16.86 ? 197 GLY B CA  1 
ATOM   3427 C C   . GLY B 1 203 ? 10.547  64.482 55.685 1.00 33.62 ? 197 GLY B C   1 
ATOM   3428 O O   . GLY B 1 203 ? 9.780   65.423 55.851 1.00 19.29 ? 197 GLY B O   1 
ATOM   3429 N N   . GLY B 1 204 ? 10.140  63.218 55.703 1.00 79.69 ? 198 GLY B N   1 
ATOM   3430 C CA  . GLY B 1 204 ? 8.779   62.891 56.090 1.00 18.23 ? 198 GLY B CA  1 
ATOM   3431 C C   . GLY B 1 204 ? 8.533   63.128 57.577 1.00 80.32 ? 198 GLY B C   1 
ATOM   3432 O O   . GLY B 1 204 ? 9.478   63.278 58.351 1.00 35.38 ? 198 GLY B O   1 
ATOM   3433 N N   . HIS B 1 205 ? 7.270   63.267 57.964 1.00 10.12 ? 199 HIS B N   1 
ATOM   3434 C CA  . HIS B 1 205 ? 6.892   63.174 59.375 1.00 2.00  ? 199 HIS B CA  1 
ATOM   3435 C C   . HIS B 1 205 ? 5.490   62.609 59.477 1.00 25.42 ? 199 HIS B C   1 
ATOM   3436 O O   . HIS B 1 205 ? 4.601   63.020 58.711 1.00 3.41  ? 199 HIS B O   1 
ATOM   3437 C CB  . HIS B 1 205 ? 6.979   64.529 60.082 1.00 24.93 ? 199 HIS B CB  1 
ATOM   3438 C CG  . HIS B 1 205 ? 7.011   64.439 61.585 1.00 36.32 ? 199 HIS B CG  1 
ATOM   3439 N ND1 . HIS B 1 205 ? 7.827   63.558 62.266 1.00 27.86 ? 199 HIS B ND1 1 
ATOM   3440 C CD2 . HIS B 1 205 ? 6.383   65.175 62.539 1.00 31.46 ? 199 HIS B CD2 1 
ATOM   3441 C CE1 . HIS B 1 205 ? 7.707   63.753 63.565 1.00 23.50 ? 199 HIS B CE1 1 
ATOM   3442 N NE2 . HIS B 1 205 ? 6.837   64.728 63.761 1.00 20.56 ? 199 HIS B NE2 1 
ATOM   3443 N N   . ALA B 1 206 ? 5.441   61.443 60.129 1.00 2.00  ? 200 ALA B N   1 
ATOM   3444 C CA  . ALA B 1 206 ? 4.211   60.722 60.420 1.00 2.00  ? 200 ALA B CA  1 
ATOM   3445 C C   . ALA B 1 206 ? 3.538   61.262 61.672 1.00 4.14  ? 200 ALA B C   1 
ATOM   3446 O O   . ALA B 1 206 ? 4.188   61.541 62.666 1.00 11.48 ? 200 ALA B O   1 
ATOM   3447 C CB  . ALA B 1 206 ? 4.512   59.219 60.582 1.00 8.88  ? 200 ALA B CB  1 
ATOM   3448 N N   . ILE B 1 207 ? 2.260   61.584 61.539 1.00 7.32  ? 201 ILE B N   1 
ATOM   3449 C CA  . ILE B 1 207 ? 1.534   62.313 62.574 1.00 9.56  ? 201 ILE B CA  1 
ATOM   3450 C C   . ILE B 1 207 ? 0.140   61.713 62.700 1.00 2.00  ? 201 ILE B C   1 
ATOM   3451 O O   . ILE B 1 207 ? -0.143  60.704 62.069 1.00 11.95 ? 201 ILE B O   1 
ATOM   3452 C CB  . ILE B 1 207 ? 1.423   63.832 62.228 1.00 8.88  ? 201 ILE B CB  1 
ATOM   3453 C CG1 . ILE B 1 207 ? 1.036   64.040 60.750 1.00 6.30  ? 201 ILE B CG1 1 
ATOM   3454 C CG2 . ILE B 1 207 ? 2.740   64.535 62.514 1.00 7.28  ? 201 ILE B CG2 1 
ATOM   3455 C CD1 . ILE B 1 207 ? -0.260  63.445 60.318 1.00 9.37  ? 201 ILE B CD1 1 
ATOM   3456 N N   . ARG B 1 208 ? -0.694  62.275 63.572 1.00 5.59  ? 202 ARG B N   1 
ATOM   3457 C CA  . ARG B 1 208 ? -2.068  61.797 63.741 1.00 4.08  ? 202 ARG B CA  1 
ATOM   3458 C C   . ARG B 1 208 ? -3.018  62.965 63.500 1.00 2.00  ? 202 ARG B C   1 
ATOM   3459 O O   . ARG B 1 208 ? -2.758  64.072 63.973 1.00 6.91  ? 202 ARG B O   1 
ATOM   3460 C CB  . ARG B 1 208 ? -2.266  61.201 65.157 1.00 21.35 ? 202 ARG B CB  1 
ATOM   3461 C CG  . ARG B 1 208 ? -3.742  61.114 65.635 1.00 2.00  ? 202 ARG B CG  1 
ATOM   3462 C CD  . ARG B 1 208 ? -3.858  60.644 67.080 1.00 20.33 ? 202 ARG B CD  1 
ATOM   3463 N NE  . ARG B 1 208 ? -3.235  61.542 68.054 1.00 14.05 ? 202 ARG B NE  1 
ATOM   3464 C CZ  . ARG B 1 208 ? -3.871  62.106 69.094 1.00 23.78 ? 202 ARG B CZ  1 
ATOM   3465 N NH1 . ARG B 1 208 ? -5.188  62.011 69.230 1.00 4.74  ? 202 ARG B NH1 1 
ATOM   3466 N NH2 . ARG B 1 208 ? -3.205  62.835 69.978 1.00 8.30  ? 202 ARG B NH2 1 
ATOM   3467 N N   . ILE B 1 209 ? -3.992  62.770 62.621 1.00 3.14  ? 203 ILE B N   1 
ATOM   3468 C CA  . ILE B 1 209 ? -4.982  63.802 62.276 1.00 10.29 ? 203 ILE B CA  1 
ATOM   3469 C C   . ILE B 1 209 ? -6.275  63.523 63.051 1.00 2.00  ? 203 ILE B C   1 
ATOM   3470 O O   . ILE B 1 209 ? -6.794  62.415 62.994 1.00 5.24  ? 203 ILE B O   1 
ATOM   3471 C CB  . ILE B 1 209 ? -5.331  63.773 60.753 1.00 2.00  ? 203 ILE B CB  1 
ATOM   3472 C CG1 . ILE B 1 209 ? -4.075  63.956 59.927 1.00 9.29  ? 203 ILE B CG1 1 
ATOM   3473 C CG2 . ILE B 1 209 ? -6.339  64.845 60.397 1.00 2.00  ? 203 ILE B CG2 1 
ATOM   3474 C CD1 . ILE B 1 209 ? -4.325  63.728 58.489 1.00 14.98 ? 203 ILE B CD1 1 
ATOM   3475 N N   . LEU B 1 210 ? -6.845  64.546 63.684 1.00 25.78 ? 204 LEU B N   1 
ATOM   3476 C CA  . LEU B 1 210 ? -7.993  64.345 64.572 1.00 2.00  ? 204 LEU B CA  1 
ATOM   3477 C C   . LEU B 1 210 ? -9.133  65.345 64.353 1.00 17.90 ? 204 LEU B C   1 
ATOM   3478 O O   . LEU B 1 210 ? -10.106 65.351 65.110 1.00 22.14 ? 204 LEU B O   1 
ATOM   3479 C CB  . LEU B 1 210 ? -7.537  64.367 66.041 1.00 44.14 ? 204 LEU B CB  1 
ATOM   3480 C CG  . LEU B 1 210 ? -6.824  65.637 66.522 1.00 2.00  ? 204 LEU B CG  1 
ATOM   3481 C CD1 . LEU B 1 210 ? -7.631  66.306 67.616 1.00 50.83 ? 204 LEU B CD1 1 
ATOM   3482 C CD2 . LEU B 1 210 ? -5.407  65.307 67.007 1.00 18.34 ? 204 LEU B CD2 1 
ATOM   3483 N N   . GLY B 1 211 ? -9.048  66.134 63.287 1.00 27.15 ? 205 GLY B N   1 
ATOM   3484 C CA  . GLY B 1 211 ? -10.145 67.018 62.944 1.00 3.68  ? 205 GLY B CA  1 
ATOM   3485 C C   . GLY B 1 211 ? -9.837  68.060 61.884 1.00 56.47 ? 205 GLY B C   1 
ATOM   3486 O O   . GLY B 1 211 ? -8.742  68.089 61.326 1.00 29.30 ? 205 GLY B O   1 
ATOM   3487 N N   . TRP B 1 212 ? -10.770 68.987 61.701 1.00 39.27 ? 206 TRP B N   1 
ATOM   3488 C CA  . TRP B 1 212 ? -10.664 70.004 60.669 1.00 29.44 ? 206 TRP B CA  1 
ATOM   3489 C C   . TRP B 1 212 ? -11.407 71.305 61.034 1.00 14.27 ? 206 TRP B C   1 
ATOM   3490 O O   . TRP B 1 212 ? -12.146 71.353 62.021 1.00 47.18 ? 206 TRP B O   1 
ATOM   3491 C CB  . TRP B 1 212 ? -11.190 69.429 59.354 1.00 2.00  ? 206 TRP B CB  1 
ATOM   3492 C CG  . TRP B 1 212 ? -12.645 69.241 59.332 1.00 3.22  ? 206 TRP B CG  1 
ATOM   3493 C CD1 . TRP B 1 212 ? -13.580 70.186 59.012 1.00 31.31 ? 206 TRP B CD1 1 
ATOM   3494 C CD2 . TRP B 1 212 ? -13.365 68.003 59.484 1.00 5.95  ? 206 TRP B CD2 1 
ATOM   3495 N NE1 . TRP B 1 212 ? -14.822 69.612 58.938 1.00 14.66 ? 206 TRP B NE1 1 
ATOM   3496 C CE2 . TRP B 1 212 ? -14.726 68.280 59.240 1.00 3.65  ? 206 TRP B CE2 1 
ATOM   3497 C CE3 . TRP B 1 212 ? -12.992 66.695 59.800 1.00 12.24 ? 206 TRP B CE3 1 
ATOM   3498 C CZ2 . TRP B 1 212 ? -15.710 67.307 59.299 1.00 2.00  ? 206 TRP B CZ2 1 
ATOM   3499 C CZ3 . TRP B 1 212 ? -13.969 65.727 59.844 1.00 2.00  ? 206 TRP B CZ3 1 
ATOM   3500 C CH2 . TRP B 1 212 ? -15.312 66.036 59.590 1.00 15.39 ? 206 TRP B CH2 1 
ATOM   3501 N N   . GLY B 1 213 ? -11.235 72.348 60.227 1.00 33.57 ? 207 GLY B N   1 
ATOM   3502 C CA  . GLY B 1 213 ? -11.886 73.623 60.509 1.00 4.78  ? 207 GLY B CA  1 
ATOM   3503 C C   . GLY B 1 213 ? -11.438 74.746 59.598 1.00 27.87 ? 207 GLY B C   1 
ATOM   3504 O O   . GLY B 1 213 ? -10.851 74.478 58.550 1.00 45.91 ? 207 GLY B O   1 
ATOM   3505 N N   . ILE B 1 214 ? -11.670 75.998 60.003 1.00 31.71 ? 208 ILE B N   1 
ATOM   3506 C CA  . ILE B 1 214 ? -11.401 77.152 59.133 1.00 11.69 ? 208 ILE B CA  1 
ATOM   3507 C C   . ILE B 1 214 ? -10.888 78.402 59.880 1.00 13.51 ? 208 ILE B C   1 
ATOM   3508 O O   . ILE B 1 214 ? -11.669 79.160 60.443 1.00 67.26 ? 208 ILE B O   1 
ATOM   3509 C CB  . ILE B 1 214 ? -12.671 77.562 58.330 1.00 21.83 ? 208 ILE B CB  1 
ATOM   3510 C CG1 . ILE B 1 214 ? -13.293 76.350 57.625 1.00 11.84 ? 208 ILE B CG1 1 
ATOM   3511 C CG2 . ILE B 1 214 ? -12.306 78.599 57.294 1.00 15.90 ? 208 ILE B CG2 1 
ATOM   3512 C CD1 . ILE B 1 214 ? -14.302 76.695 56.562 1.00 39.75 ? 208 ILE B CD1 1 
ATOM   3513 N N   . GLU B 1 215 ? -9.601  78.689 59.738 1.00 17.81 ? 209 GLU B N   1 
ATOM   3514 C CA  . GLU B 1 215 ? -8.986  79.855 60.368 1.00 18.96 ? 209 GLU B CA  1 
ATOM   3515 C C   . GLU B 1 215 ? -8.895  81.079 59.419 1.00 53.04 ? 209 GLU B C   1 
ATOM   3516 O O   . GLU B 1 215 ? -7.949  81.174 58.630 1.00 41.87 ? 209 GLU B O   1 
ATOM   3517 C CB  . GLU B 1 215 ? -7.588  79.469 60.862 1.00 74.08 ? 209 GLU B CB  1 
ATOM   3518 C CG  . GLU B 1 215 ? -6.934  80.466 61.812 1.00 13.26 ? 209 GLU B CG  1 
ATOM   3519 C CD  . GLU B 1 215 ? -6.561  79.856 63.159 1.00 29.57 ? 209 GLU B CD  1 
ATOM   3520 O OE1 . GLU B 1 215 ? -7.250  78.921 63.629 1.00 25.37 ? 209 GLU B OE1 1 
ATOM   3521 O OE2 . GLU B 1 215 ? -5.579  80.323 63.768 1.00 16.18 ? 209 GLU B OE2 1 
ATOM   3522 N N   . ASN B 1 216 ? -9.833  82.031 59.544 1.00 25.23 ? 210 ASN B N   1 
ATOM   3523 C CA  . ASN B 1 216 ? -9.843  83.295 58.752 1.00 8.05  ? 210 ASN B CA  1 
ATOM   3524 C C   . ASN B 1 216 ? -10.028 83.017 57.268 1.00 44.07 ? 210 ASN B C   1 
ATOM   3525 O O   . ASN B 1 216 ? -9.261  83.526 56.459 1.00 12.30 ? 210 ASN B O   1 
ATOM   3526 C CB  . ASN B 1 216 ? -8.516  84.091 58.876 1.00 26.89 ? 210 ASN B CB  1 
ATOM   3527 C CG  . ASN B 1 216 ? -8.127  84.418 60.306 1.00 52.08 ? 210 ASN B CG  1 
ATOM   3528 O OD1 . ASN B 1 216 ? -7.100  83.956 60.798 1.00 21.41 ? 210 ASN B OD1 1 
ATOM   3529 N ND2 . ASN B 1 216 ? -8.830  85.347 60.904 1.00 9.95  ? 210 ASN B ND2 1 
ATOM   3530 N N   . GLY B 1 217 ? -10.953 82.125 56.918 1.00 6.38  ? 211 GLY B N   1 
ATOM   3531 C CA  . GLY B 1 217 ? -11.039 81.650 55.546 1.00 31.82 ? 211 GLY B CA  1 
ATOM   3532 C C   . GLY B 1 217 ? -10.156 80.463 55.183 1.00 25.68 ? 211 GLY B C   1 
ATOM   3533 O O   . GLY B 1 217 ? -10.506 79.672 54.309 1.00 58.37 ? 211 GLY B O   1 
ATOM   3534 N N   . VAL B 1 218 ? -9.008  80.340 55.838 1.00 7.77  ? 212 VAL B N   1 
ATOM   3535 C CA  . VAL B 1 218 ? -8.076  79.267 55.566 1.00 18.31 ? 212 VAL B CA  1 
ATOM   3536 C C   . VAL B 1 218 ? -8.560  77.929 56.143 1.00 36.60 ? 212 VAL B C   1 
ATOM   3537 O O   . VAL B 1 218 ? -8.563  77.744 57.355 1.00 9.20  ? 212 VAL B O   1 
ATOM   3538 C CB  . VAL B 1 218 ? -6.712  79.589 56.173 1.00 20.26 ? 212 VAL B CB  1 
ATOM   3539 C CG1 . VAL B 1 218 ? -5.694  78.603 55.691 1.00 23.19 ? 212 VAL B CG1 1 
ATOM   3540 C CG2 . VAL B 1 218 ? -6.308  81.005 55.831 1.00 74.56 ? 212 VAL B CG2 1 
ATOM   3541 N N   . PRO B 1 219 ? -8.950  76.969 55.282 1.00 39.69 ? 213 PRO B N   1 
ATOM   3542 C CA  . PRO B 1 219 ? -9.273  75.631 55.803 1.00 22.05 ? 213 PRO B CA  1 
ATOM   3543 C C   . PRO B 1 219 ? -8.016  74.862 56.223 1.00 12.71 ? 213 PRO B C   1 
ATOM   3544 O O   . PRO B 1 219 ? -7.003  74.928 55.533 1.00 18.15 ? 213 PRO B O   1 
ATOM   3545 C CB  . PRO B 1 219 ? -10.019 74.958 54.645 1.00 2.00  ? 213 PRO B CB  1 
ATOM   3546 C CG  . PRO B 1 219 ? -9.547  75.659 53.412 1.00 17.15 ? 213 PRO B CG  1 
ATOM   3547 C CD  . PRO B 1 219 ? -8.965  77.009 53.809 1.00 18.24 ? 213 PRO B CD  1 
ATOM   3548 N N   . TYR B 1 220 ? -8.060  74.217 57.397 1.00 13.53 ? 214 TYR B N   1 
ATOM   3549 C CA  . TYR B 1 220 ? -6.914  73.484 57.942 1.00 6.18  ? 214 TYR B CA  1 
ATOM   3550 C C   . TYR B 1 220 ? -7.289  72.103 58.498 1.00 41.36 ? 214 TYR B C   1 
ATOM   3551 O O   . TYR B 1 220 ? -8.457  71.821 58.742 1.00 7.41  ? 214 TYR B O   1 
ATOM   3552 C CB  . TYR B 1 220 ? -6.241  74.313 59.038 1.00 12.37 ? 214 TYR B CB  1 
ATOM   3553 C CG  . TYR B 1 220 ? -7.050  74.409 60.313 1.00 54.56 ? 214 TYR B CG  1 
ATOM   3554 C CD1 . TYR B 1 220 ? -7.071  73.359 61.216 1.00 63.64 ? 214 TYR B CD1 1 
ATOM   3555 C CD2 . TYR B 1 220 ? -7.916  75.477 60.534 1.00 16.20 ? 214 TYR B CD2 1 
ATOM   3556 C CE1 . TYR B 1 220 ? -7.944  73.348 62.264 1.00 49.76 ? 214 TYR B CE1 1 
ATOM   3557 C CE2 . TYR B 1 220 ? -8.777  75.478 61.593 1.00 85.06 ? 214 TYR B CE2 1 
ATOM   3558 C CZ  . TYR B 1 220 ? -8.796  74.404 62.441 1.00 61.66 ? 214 TYR B CZ  1 
ATOM   3559 O OH  . TYR B 1 220 ? -9.731  74.352 63.422 1.00 13.68 ? 214 TYR B OH  1 
ATOM   3560 N N   . TRP B 1 221 ? -6.286  71.280 58.779 1.00 33.08 ? 215 TRP B N   1 
ATOM   3561 C CA  . TRP B 1 221 ? -6.495  70.027 59.490 1.00 2.00  ? 215 TRP B CA  1 
ATOM   3562 C C   . TRP B 1 221 ? -5.914  70.158 60.895 1.00 7.25  ? 215 TRP B C   1 
ATOM   3563 O O   . TRP B 1 221 ? -4.845  70.793 61.085 1.00 5.50  ? 215 TRP B O   1 
ATOM   3564 C CB  . TRP B 1 221 ? -5.775  68.866 58.803 1.00 11.06 ? 215 TRP B CB  1 
ATOM   3565 C CG  . TRP B 1 221 ? -6.313  68.441 57.485 1.00 21.90 ? 215 TRP B CG  1 
ATOM   3566 C CD1 . TRP B 1 221 ? -5.705  68.610 56.290 1.00 9.33  ? 215 TRP B CD1 1 
ATOM   3567 C CD2 . TRP B 1 221 ? -7.463  67.613 57.240 1.00 2.00  ? 215 TRP B CD2 1 
ATOM   3568 N NE1 . TRP B 1 221 ? -6.380  67.926 55.323 1.00 5.05  ? 215 TRP B NE1 1 
ATOM   3569 C CE2 . TRP B 1 221 ? -7.462  67.306 55.880 1.00 2.00  ? 215 TRP B CE2 1 
ATOM   3570 C CE3 . TRP B 1 221 ? -8.468  67.099 58.041 1.00 2.00  ? 215 TRP B CE3 1 
ATOM   3571 C CZ2 . TRP B 1 221 ? -8.433  66.498 55.295 1.00 2.00  ? 215 TRP B CZ2 1 
ATOM   3572 C CZ3 . TRP B 1 221 ? -9.421  66.290 57.466 1.00 20.47 ? 215 TRP B CZ3 1 
ATOM   3573 C CH2 . TRP B 1 221 ? -9.396  65.997 56.100 1.00 15.38 ? 215 TRP B CH2 1 
ATOM   3574 N N   . LEU B 1 222 ? -6.603  69.571 61.875 1.00 10.90 ? 216 LEU B N   1 
ATOM   3575 C CA  . LEU B 1 222 ? -6.099  69.528 63.254 1.00 12.78 ? 216 LEU B CA  1 
ATOM   3576 C C   . LEU B 1 222 ? -5.150  68.338 63.447 1.00 15.44 ? 216 LEU B C   1 
ATOM   3577 O O   . LEU B 1 222 ? -5.527  67.177 63.243 1.00 2.00  ? 216 LEU B O   1 
ATOM   3578 C CB  . LEU B 1 222 ? -7.264  69.458 64.245 1.00 8.91  ? 216 LEU B CB  1 
ATOM   3579 C CG  . LEU B 1 222 ? -7.023  69.490 65.761 1.00 15.13 ? 216 LEU B CG  1 
ATOM   3580 C CD1 . LEU B 1 222 ? -6.152  70.677 66.233 1.00 2.00  ? 216 LEU B CD1 1 
ATOM   3581 C CD2 . LEU B 1 222 ? -8.392  69.571 66.392 1.00 7.19  ? 216 LEU B CD2 1 
ATOM   3582 N N   . VAL B 1 223 ? -3.907  68.635 63.797 1.00 2.00  ? 217 VAL B N   1 
ATOM   3583 C CA  . VAL B 1 223 ? -2.878  67.604 63.882 1.00 20.88 ? 217 VAL B CA  1 
ATOM   3584 C C   . VAL B 1 223 ? -2.172  67.473 65.243 1.00 23.41 ? 217 VAL B C   1 
ATOM   3585 O O   . VAL B 1 223 ? -1.608  68.430 65.783 1.00 6.34  ? 217 VAL B O   1 
ATOM   3586 C CB  . VAL B 1 223 ? -1.799  67.802 62.782 1.00 39.19 ? 217 VAL B CB  1 
ATOM   3587 C CG1 . VAL B 1 223 ? -0.916  66.553 62.688 1.00 24.36 ? 217 VAL B CG1 1 
ATOM   3588 C CG2 . VAL B 1 223 ? -2.459  68.111 61.427 1.00 18.30 ? 217 VAL B CG2 1 
ATOM   3589 N N   . ALA B 1 224 ? -2.054  66.244 65.716 1.00 2.00  ? 218 ALA B N   1 
ATOM   3590 C CA  . ALA B 1 224 ? -1.260  66.003 66.902 1.00 2.10  ? 218 ALA B CA  1 
ATOM   3591 C C   . ALA B 1 224 ? 0.131   65.626 66.436 1.00 3.80  ? 218 ALA B C   1 
ATOM   3592 O O   . ALA B 1 224 ? 0.283   64.684 65.686 1.00 9.67  ? 218 ALA B O   1 
ATOM   3593 C CB  . ALA B 1 224 ? -1.875  64.867 67.750 1.00 4.35  ? 218 ALA B CB  1 
ATOM   3594 N N   . ASN B 1 225 ? 1.107   66.474 66.717 1.00 2.00  ? 219 ASN B N   1 
ATOM   3595 C CA  . ASN B 1 225 ? 2.507   66.053 66.678 1.00 8.71  ? 219 ASN B CA  1 
ATOM   3596 C C   . ASN B 1 225 ? 2.880   65.192 67.902 1.00 12.86 ? 219 ASN B C   1 
ATOM   3597 O O   . ASN B 1 225 ? 2.169   65.186 68.888 1.00 15.08 ? 219 ASN B O   1 
ATOM   3598 C CB  . ASN B 1 225 ? 3.426   67.280 66.624 1.00 2.03  ? 219 ASN B CB  1 
ATOM   3599 C CG  . ASN B 1 225 ? 4.617   67.077 65.716 1.00 9.76  ? 219 ASN B CG  1 
ATOM   3600 O OD1 . ASN B 1 225 ? 5.317   68.027 65.377 1.00 21.14 ? 219 ASN B OD1 1 
ATOM   3601 N ND2 . ASN B 1 225 ? 4.897   65.834 65.365 1.00 7.93  ? 219 ASN B ND2 1 
ATOM   3602 N N   . SER B 1 226 ? 3.974   64.443 67.802 1.00 4.01  ? 220 SER B N   1 
ATOM   3603 C CA  . SER B 1 226 ? 4.519   63.683 68.919 1.00 2.00  ? 220 SER B CA  1 
ATOM   3604 C C   . SER B 1 226 ? 5.809   64.287 69.482 1.00 11.22 ? 220 SER B C   1 
ATOM   3605 O O   . SER B 1 226 ? 6.711   63.536 69.924 1.00 8.47  ? 220 SER B O   1 
ATOM   3606 C CB  . SER B 1 226 ? 4.795   62.239 68.492 1.00 2.26  ? 220 SER B CB  1 
ATOM   3607 O OG  . SER B 1 226 ? 5.711   62.167 67.411 1.00 2.37  ? 220 SER B OG  1 
ATOM   3608 N N   . TRP B 1 227 ? 5.878   65.625 69.523 1.00 27.46 ? 221 TRP B N   1 
ATOM   3609 C CA  . TRP B 1 227 ? 7.081   66.355 69.976 1.00 18.10 ? 221 TRP B CA  1 
ATOM   3610 C C   . TRP B 1 227 ? 7.006   66.973 71.384 1.00 32.58 ? 221 TRP B C   1 
ATOM   3611 O O   . TRP B 1 227 ? 7.893   67.737 71.756 1.00 30.04 ? 221 TRP B O   1 
ATOM   3612 C CB  . TRP B 1 227 ? 7.458   67.453 68.966 1.00 25.89 ? 221 TRP B CB  1 
ATOM   3613 C CG  . TRP B 1 227 ? 8.390   66.974 67.880 1.00 85.15 ? 221 TRP B CG  1 
ATOM   3614 C CD1 . TRP B 1 227 ? 8.982   65.753 67.809 1.00 8.45  ? 221 TRP B CD1 1 
ATOM   3615 C CD2 . TRP B 1 227 ? 8.642   67.609 66.613 1.00 13.11 ? 221 TRP B CD2 1 
ATOM   3616 N NE1 . TRP B 1 227 ? 9.515   65.555 66.560 1.00 28.73 ? 221 TRP B NE1 1 
ATOM   3617 C CE2 . TRP B 1 227 ? 9.330   66.688 65.813 1.00 24.85 ? 221 TRP B CE2 1 
ATOM   3618 C CE3 . TRP B 1 227 ? 8.342   68.860 66.077 1.00 2.00  ? 221 TRP B CE3 1 
ATOM   3619 C CZ2 . TRP B 1 227 ? 9.716   66.982 64.504 1.00 16.93 ? 221 TRP B CZ2 1 
ATOM   3620 C CZ3 . TRP B 1 227 ? 8.714   69.148 64.782 1.00 13.77 ? 221 TRP B CZ3 1 
ATOM   3621 C CH2 . TRP B 1 227 ? 9.387   68.222 64.008 1.00 27.10 ? 221 TRP B CH2 1 
ATOM   3622 N N   . ASN B 1 228 ? 6.149   66.395 72.227 1.00 65.53 ? 222 ASN B N   1 
ATOM   3623 C CA  . ASN B 1 228 ? 5.721   66.965 73.520 1.00 56.52 ? 222 ASN B CA  1 
ATOM   3624 C C   . ASN B 1 228 ? 4.882   68.237 73.393 1.00 31.50 ? 222 ASN B C   1 
ATOM   3625 O O   . ASN B 1 228 ? 4.662   68.725 72.295 1.00 26.26 ? 222 ASN B O   1 
ATOM   3626 C CB  . ASN B 1 228 ? 6.907   67.207 74.472 1.00 10.55 ? 222 ASN B CB  1 
ATOM   3627 C CG  . ASN B 1 228 ? 6.584   66.804 75.897 1.00 42.16 ? 222 ASN B CG  1 
ATOM   3628 O OD1 . ASN B 1 228 ? 5.508   67.111 76.411 1.00 39.34 ? 222 ASN B OD1 1 
ATOM   3629 N ND2 . ASN B 1 228 ? 7.482   66.068 76.522 1.00 30.24 ? 222 ASN B ND2 1 
ATOM   3630 N N   . ALA B 1 229 ? 4.436   68.792 74.515 1.00 3.84  ? 223 ALA B N   1 
ATOM   3631 C CA  . ALA B 1 229 ? 3.395   69.830 74.441 1.00 22.08 ? 223 ALA B CA  1 
ATOM   3632 C C   . ALA B 1 229 ? 3.962   71.246 74.365 1.00 7.08  ? 223 ALA B C   1 
ATOM   3633 O O   . ALA B 1 229 ? 3.259   72.200 74.032 1.00 19.67 ? 223 ALA B O   1 
ATOM   3634 C CB  . ALA B 1 229 ? 2.429   69.702 75.626 1.00 2.99  ? 223 ALA B CB  1 
ATOM   3635 N N   . ASP B 1 230 ? 5.232   71.390 74.728 1.00 2.00  ? 224 ASP B N   1 
ATOM   3636 C CA  . ASP B 1 230 ? 5.848   72.699 74.662 1.00 14.85 ? 224 ASP B CA  1 
ATOM   3637 C C   . ASP B 1 230 ? 6.347   73.075 73.268 1.00 31.48 ? 224 ASP B C   1 
ATOM   3638 O O   . ASP B 1 230 ? 6.653   74.226 73.005 1.00 29.02 ? 224 ASP B O   1 
ATOM   3639 C CB  . ASP B 1 230 ? 6.971   72.796 75.691 1.00 10.18 ? 224 ASP B CB  1 
ATOM   3640 C CG  . ASP B 1 230 ? 8.124   71.888 75.379 1.00 50.99 ? 224 ASP B CG  1 
ATOM   3641 O OD1 . ASP B 1 230 ? 7.884   70.764 74.836 1.00 5.19  ? 224 ASP B OD1 1 
ATOM   3642 O OD2 . ASP B 1 230 ? 9.255   72.307 75.722 1.00 5.70  ? 224 ASP B OD2 1 
ATOM   3643 N N   . TRP B 1 231 ? 6.455   72.105 72.374 1.00 23.03 ? 225 TRP B N   1 
ATOM   3644 C CA  . TRP B 1 231 ? 6.654   72.457 70.984 1.00 8.70  ? 225 TRP B CA  1 
ATOM   3645 C C   . TRP B 1 231 ? 5.283   72.812 70.401 1.00 2.00  ? 225 TRP B C   1 
ATOM   3646 O O   . TRP B 1 231 ? 4.260   72.156 70.702 1.00 9.86  ? 225 TRP B O   1 
ATOM   3647 C CB  . TRP B 1 231 ? 7.340   71.315 70.204 1.00 4.73  ? 225 TRP B CB  1 
ATOM   3648 C CG  . TRP B 1 231 ? 7.392   71.562 68.697 1.00 32.25 ? 225 TRP B CG  1 
ATOM   3649 C CD1 . TRP B 1 231 ? 8.430   72.173 67.986 1.00 2.05  ? 225 TRP B CD1 1 
ATOM   3650 C CD2 . TRP B 1 231 ? 6.287   71.447 67.756 1.00 3.48  ? 225 TRP B CD2 1 
ATOM   3651 N NE1 . TRP B 1 231 ? 7.996   72.463 66.704 1.00 18.25 ? 225 TRP B NE1 1 
ATOM   3652 C CE2 . TRP B 1 231 ? 6.698   72.041 66.538 1.00 25.80 ? 225 TRP B CE2 1 
ATOM   3653 C CE3 . TRP B 1 231 ? 4.991   70.908 67.833 1.00 37.31 ? 225 TRP B CE3 1 
ATOM   3654 C CZ2 . TRP B 1 231 ? 5.861   72.126 65.422 1.00 6.14  ? 225 TRP B CZ2 1 
ATOM   3655 C CZ3 . TRP B 1 231 ? 4.162   70.997 66.720 1.00 2.00  ? 225 TRP B CZ3 1 
ATOM   3656 C CH2 . TRP B 1 231 ? 4.594   71.605 65.538 1.00 16.14 ? 225 TRP B CH2 1 
ATOM   3657 N N   . GLY B 1 232 ? 5.234   73.966 69.746 1.00 44.92 ? 226 GLY B N   1 
ATOM   3658 C CA  . GLY B 1 232 ? 4.033   74.388 69.048 1.00 10.39 ? 226 GLY B CA  1 
ATOM   3659 C C   . GLY B 1 232 ? 2.828   74.633 69.928 1.00 30.44 ? 226 GLY B C   1 
ATOM   3660 O O   . GLY B 1 232 ? 2.936   74.772 71.149 1.00 50.15 ? 226 GLY B O   1 
ATOM   3661 N N   . ASP B 1 233 ? 1.660   74.569 69.308 1.00 20.28 ? 227 ASP B N   1 
ATOM   3662 C CA  . ASP B 1 233 ? 0.411   74.950 69.954 1.00 2.00  ? 227 ASP B CA  1 
ATOM   3663 C C   . ASP B 1 233 ? -0.052  73.874 70.941 1.00 13.66 ? 227 ASP B C   1 
ATOM   3664 O O   . ASP B 1 233 ? -1.069  73.196 70.720 1.00 24.90 ? 227 ASP B O   1 
ATOM   3665 C CB  . ASP B 1 233 ? -0.646  75.204 68.875 1.00 5.59  ? 227 ASP B CB  1 
ATOM   3666 C CG  . ASP B 1 233 ? -1.991  75.551 69.441 1.00 39.09 ? 227 ASP B CG  1 
ATOM   3667 O OD1 . ASP B 1 233 ? -2.040  76.400 70.345 1.00 18.05 ? 227 ASP B OD1 1 
ATOM   3668 O OD2 . ASP B 1 233 ? -2.991  74.940 69.007 1.00 79.39 ? 227 ASP B OD2 1 
ATOM   3669 N N   . ASN B 1 234 ? 0.645   73.790 72.079 1.00 16.78 ? 228 ASN B N   1 
ATOM   3670 C CA  . ASN B 1 234 ? 0.376   72.767 73.098 1.00 67.77 ? 228 ASN B CA  1 
ATOM   3671 C C   . ASN B 1 234 ? 0.506   71.340 72.577 1.00 37.42 ? 228 ASN B C   1 
ATOM   3672 O O   . ASN B 1 234 ? -0.235  70.443 72.989 1.00 24.91 ? 228 ASN B O   1 
ATOM   3673 C CB  . ASN B 1 234 ? -1.013  72.975 73.699 1.00 12.68 ? 228 ASN B CB  1 
ATOM   3674 C CG  . ASN B 1 234 ? -1.105  74.260 74.496 1.00 43.97 ? 228 ASN B CG  1 
ATOM   3675 O OD1 . ASN B 1 234 ? -0.182  74.618 75.241 1.00 2.00  ? 228 ASN B OD1 1 
ATOM   3676 N ND2 . ASN B 1 234 ? -2.188  74.990 74.303 1.00 5.98  ? 228 ASN B ND2 1 
ATOM   3677 N N   . GLY B 1 235 ? 1.452   71.150 71.661 1.00 66.95 ? 229 GLY B N   1 
ATOM   3678 C CA  . GLY B 1 235 ? 1.633   69.862 71.020 1.00 25.78 ? 229 GLY B CA  1 
ATOM   3679 C C   . GLY B 1 235 ? 0.896   69.659 69.712 1.00 37.77 ? 229 GLY B C   1 
ATOM   3680 O O   . GLY B 1 235 ? 1.203   68.710 68.998 1.00 12.78 ? 229 GLY B O   1 
ATOM   3681 N N   . PHE B 1 236 ? -0.116  70.476 69.424 1.00 2.00  ? 230 PHE B N   1 
ATOM   3682 C CA  . PHE B 1 236 ? -0.879  70.326 68.186 1.00 2.00  ? 230 PHE B CA  1 
ATOM   3683 C C   . PHE B 1 236 ? -0.387  71.328 67.146 1.00 27.72 ? 230 PHE B C   1 
ATOM   3684 O O   . PHE B 1 236 ? 0.387   72.231 67.468 1.00 16.41 ? 230 PHE B O   1 
ATOM   3685 C CB  . PHE B 1 236 ? -2.382  70.542 68.427 1.00 2.45  ? 230 PHE B CB  1 
ATOM   3686 C CG  . PHE B 1 236 ? -3.003  69.569 69.431 1.00 22.72 ? 230 PHE B CG  1 
ATOM   3687 C CD1 . PHE B 1 236 ? -2.640  69.597 70.778 1.00 66.36 ? 230 PHE B CD1 1 
ATOM   3688 C CD2 . PHE B 1 236 ? -3.934  68.624 69.025 1.00 25.30 ? 230 PHE B CD2 1 
ATOM   3689 C CE1 . PHE B 1 236 ? -3.185  68.691 71.687 1.00 35.78 ? 230 PHE B CE1 1 
ATOM   3690 C CE2 . PHE B 1 236 ? -4.480  67.716 69.933 1.00 26.79 ? 230 PHE B CE2 1 
ATOM   3691 C CZ  . PHE B 1 236 ? -4.101  67.748 71.258 1.00 25.83 ? 230 PHE B CZ  1 
ATOM   3692 N N   . PHE B 1 237 ? -0.715  71.089 65.879 1.00 2.00  ? 231 PHE B N   1 
ATOM   3693 C CA  . PHE B 1 237 ? -0.623  72.152 64.873 1.00 12.12 ? 231 PHE B CA  1 
ATOM   3694 C C   . PHE B 1 237 ? -1.758  72.094 63.909 1.00 19.76 ? 231 PHE B C   1 
ATOM   3695 O O   . PHE B 1 237 ? -2.488  71.103 63.860 1.00 10.31 ? 231 PHE B O   1 
ATOM   3696 C CB  . PHE B 1 237 ? 0.682   72.123 64.080 1.00 14.15 ? 231 PHE B CB  1 
ATOM   3697 C CG  . PHE B 1 237 ? 0.863   70.899 63.225 1.00 31.85 ? 231 PHE B CG  1 
ATOM   3698 C CD1 . PHE B 1 237 ? 1.298   69.713 63.782 1.00 2.00  ? 231 PHE B CD1 1 
ATOM   3699 C CD2 . PHE B 1 237 ? 0.668   70.958 61.860 1.00 3.52  ? 231 PHE B CD2 1 
ATOM   3700 C CE1 . PHE B 1 237 ? 1.548   68.605 62.991 1.00 38.16 ? 231 PHE B CE1 1 
ATOM   3701 C CE2 . PHE B 1 237 ? 0.894   69.849 61.066 1.00 2.00  ? 231 PHE B CE2 1 
ATOM   3702 C CZ  . PHE B 1 237 ? 1.341   68.672 61.631 1.00 9.43  ? 231 PHE B CZ  1 
ATOM   3703 N N   . LYS B 1 238 ? -1.931  73.195 63.191 1.00 4.40  ? 232 LYS B N   1 
ATOM   3704 C CA  . LYS B 1 238 ? -2.893  73.273 62.081 1.00 2.48  ? 232 LYS B CA  1 
ATOM   3705 C C   . LYS B 1 238 ? -2.104  73.374 60.776 1.00 25.45 ? 232 LYS B C   1 
ATOM   3706 O O   . LYS B 1 238 ? -1.113  74.102 60.704 1.00 21.11 ? 232 LYS B O   1 
ATOM   3707 C CB  . LYS B 1 238 ? -3.776  74.519 62.222 1.00 13.15 ? 232 LYS B CB  1 
ATOM   3708 C CG  . LYS B 1 238 ? -4.612  74.539 63.475 1.00 32.98 ? 232 LYS B CG  1 
ATOM   3709 C CD  . LYS B 1 238 ? -5.510  75.750 63.488 1.00 16.65 ? 232 LYS B CD  1 
ATOM   3710 C CE  . LYS B 1 238 ? -5.770  76.218 64.923 1.00 16.55 ? 232 LYS B CE  1 
ATOM   3711 N NZ  . LYS B 1 238 ? -4.613  76.935 65.572 1.00 82.19 ? 232 LYS B NZ  1 
ATOM   3712 N N   . ILE B 1 239 ? -2.494  72.592 59.777 1.00 14.42 ? 233 ILE B N   1 
ATOM   3713 C CA  . ILE B 1 239 ? -1.908  72.707 58.443 1.00 6.48  ? 233 ILE B CA  1 
ATOM   3714 C C   . ILE B 1 239 ? -3.055  72.842 57.439 1.00 48.34 ? 233 ILE B C   1 
ATOM   3715 O O   . ILE B 1 239 ? -4.108  72.219 57.597 1.00 2.00  ? 233 ILE B O   1 
ATOM   3716 C CB  . ILE B 1 239 ? -1.070  71.456 58.090 1.00 12.23 ? 233 ILE B CB  1 
ATOM   3717 C CG1 . ILE B 1 239 ? -0.234  71.704 56.834 1.00 14.36 ? 233 ILE B CG1 1 
ATOM   3718 C CG2 . ILE B 1 239 ? -1.998  70.253 57.852 1.00 3.32  ? 233 ILE B CG2 1 
ATOM   3719 C CD1 . ILE B 1 239 ? 0.979   70.800 56.695 1.00 2.00  ? 233 ILE B CD1 1 
ATOM   3720 N N   . LEU B 1 240 ? -2.857  73.685 56.434 1.00 2.00  ? 234 LEU B N   1 
ATOM   3721 C CA  . LEU B 1 240 ? -3.870  73.941 55.394 1.00 25.05 ? 234 LEU B CA  1 
ATOM   3722 C C   . LEU B 1 240 ? -4.533  72.672 54.841 1.00 8.03  ? 234 LEU B C   1 
ATOM   3723 O O   . LEU B 1 240 ? -3.877  71.635 54.723 1.00 13.80 ? 234 LEU B O   1 
ATOM   3724 C CB  . LEU B 1 240 ? -3.219  74.724 54.245 1.00 6.24  ? 234 LEU B CB  1 
ATOM   3725 C CG  . LEU B 1 240 ? -4.030  74.989 52.976 1.00 6.01  ? 234 LEU B CG  1 
ATOM   3726 C CD1 . LEU B 1 240 ? -5.183  75.956 53.284 1.00 9.51  ? 234 LEU B CD1 1 
ATOM   3727 C CD2 . LEU B 1 240 ? -3.118  75.564 51.910 1.00 11.35 ? 234 LEU B CD2 1 
ATOM   3728 N N   . ARG B 1 241 ? -5.735  72.817 54.277 1.00 7.46  ? 235 ARG B N   1 
ATOM   3729 C CA  . ARG B 1 241 ? -6.487  71.671 53.788 1.00 21.48 ? 235 ARG B CA  1 
ATOM   3730 C C   . ARG B 1 241 ? -7.042  71.767 52.357 1.00 2.00  ? 235 ARG B C   1 
ATOM   3731 O O   . ARG B 1 241 ? -7.633  72.778 51.985 1.00 21.52 ? 235 ARG B O   1 
ATOM   3732 C CB  . ARG B 1 241 ? -7.626  71.387 54.761 1.00 15.52 ? 235 ARG B CB  1 
ATOM   3733 C CG  . ARG B 1 241 ? -8.412  70.148 54.469 1.00 2.00  ? 235 ARG B CG  1 
ATOM   3734 C CD  . ARG B 1 241 ? -9.461  69.929 55.543 1.00 2.16  ? 235 ARG B CD  1 
ATOM   3735 N NE  . ARG B 1 241 ? -10.768 70.486 55.200 1.00 38.12 ? 235 ARG B NE  1 
ATOM   3736 C CZ  . ARG B 1 241 ? -11.303 71.553 55.783 1.00 29.37 ? 235 ARG B CZ  1 
ATOM   3737 N NH1 . ARG B 1 241 ? -10.570 72.310 56.580 1.00 14.56 ? 235 ARG B NH1 1 
ATOM   3738 N NH2 . ARG B 1 241 ? -12.539 71.921 55.488 1.00 47.58 ? 235 ARG B NH2 1 
ATOM   3739 N N   . GLY B 1 242 ? -7.081  70.622 51.682 1.00 11.61 ? 236 GLY B N   1 
ATOM   3740 C CA  . GLY B 1 242 ? -7.612  70.542 50.328 1.00 49.31 ? 236 GLY B CA  1 
ATOM   3741 C C   . GLY B 1 242 ? -6.615  70.735 49.186 1.00 5.75  ? 236 GLY B C   1 
ATOM   3742 O O   . GLY B 1 242 ? -6.992  70.773 48.014 1.00 19.57 ? 236 GLY B O   1 
ATOM   3743 N N   . GLU B 1 243 ? -5.342  70.864 49.516 1.00 9.98  ? 237 GLU B N   1 
ATOM   3744 C CA  . GLU B 1 243 ? -4.366  71.272 48.509 1.00 19.19 ? 237 GLU B CA  1 
ATOM   3745 C C   . GLU B 1 243 ? -3.227  70.249 48.408 1.00 18.32 ? 237 GLU B C   1 
ATOM   3746 O O   . GLU B 1 243 ? -2.128  70.601 47.986 1.00 6.72  ? 237 GLU B O   1 
ATOM   3747 C CB  . GLU B 1 243 ? -3.793  72.626 48.904 1.00 2.00  ? 237 GLU B CB  1 
ATOM   3748 C CG  . GLU B 1 243 ? -4.043  73.692 47.923 1.00 36.38 ? 237 GLU B CG  1 
ATOM   3749 C CD  . GLU B 1 243 ? -3.187  74.886 48.207 1.00 73.72 ? 237 GLU B CD  1 
ATOM   3750 O OE1 . GLU B 1 243 ? -2.016  74.708 48.630 1.00 40.49 ? 237 GLU B OE1 1 
ATOM   3751 O OE2 . GLU B 1 243 ? -3.715  76.002 48.075 1.00 38.12 ? 237 GLU B OE2 1 
ATOM   3752 N N   . ASN B 1 244 ? -3.468  69.037 48.927 1.00 2.40  ? 238 ASN B N   1 
ATOM   3753 C CA  . ASN B 1 244 ? -2.434  68.043 49.194 1.00 2.00  ? 238 ASN B CA  1 
ATOM   3754 C C   . ASN B 1 244 ? -1.186  68.699 49.742 1.00 7.27  ? 238 ASN B C   1 
ATOM   3755 O O   . ASN B 1 244 ? -0.080  68.216 49.546 1.00 14.52 ? 238 ASN B O   1 
ATOM   3756 C CB  . ASN B 1 244 ? -2.104  67.265 47.924 1.00 9.49  ? 238 ASN B CB  1 
ATOM   3757 C CG  . ASN B 1 244 ? -1.410  65.959 48.205 1.00 17.89 ? 238 ASN B CG  1 
ATOM   3758 O OD1 . ASN B 1 244 ? -0.686  65.416 47.340 1.00 2.00  ? 238 ASN B OD1 1 
ATOM   3759 N ND2 . ASN B 1 244 ? -1.685  65.390 49.386 1.00 2.00  ? 238 ASN B ND2 1 
ATOM   3760 N N   . HIS B 1 245 ? -1.391  69.777 50.492 1.00 18.81 ? 239 HIS B N   1 
ATOM   3761 C CA  . HIS B 1 245 ? -0.288  70.639 50.907 1.00 2.18  ? 239 HIS B CA  1 
ATOM   3762 C C   . HIS B 1 245 ? 0.785   69.832 51.660 1.00 26.45 ? 239 HIS B C   1 
ATOM   3763 O O   . HIS B 1 245 ? 0.470   69.119 52.606 1.00 13.59 ? 239 HIS B O   1 
ATOM   3764 C CB  . HIS B 1 245 ? -0.821  71.804 51.763 1.00 39.02 ? 239 HIS B CB  1 
ATOM   3765 C CG  . HIS B 1 245 ? 0.174   72.898 51.969 1.00 3.87  ? 239 HIS B CG  1 
ATOM   3766 N ND1 . HIS B 1 245 ? 1.102   72.855 52.997 1.00 11.80 ? 239 HIS B ND1 1 
ATOM   3767 C CD2 . HIS B 1 245 ? 0.595   73.883 51.133 1.00 2.31  ? 239 HIS B CD2 1 
ATOM   3768 C CE1 . HIS B 1 245 ? 2.059   73.729 52.760 1.00 10.35 ? 239 HIS B CE1 1 
ATOM   3769 N NE2 . HIS B 1 245 ? 1.772   74.366 51.634 1.00 9.55  ? 239 HIS B NE2 1 
ATOM   3770 N N   . CYS B 1 246 ? 2.006   69.826 51.120 1.00 33.97 ? 240 CYS B N   1 
ATOM   3771 C CA  . CYS B 1 246 ? 3.144   69.059 51.658 1.00 13.40 ? 240 CYS B CA  1 
ATOM   3772 C C   . CYS B 1 246 ? 2.804   67.581 51.837 1.00 2.15  ? 240 CYS B C   1 
ATOM   3773 O O   . CYS B 1 246 ? 3.379   66.885 52.668 1.00 11.32 ? 240 CYS B O   1 
ATOM   3774 C CB  . CYS B 1 246 ? 3.623   69.655 52.987 1.00 5.63  ? 240 CYS B CB  1 
ATOM   3775 S SG  . CYS B 1 246 ? 4.629   71.176 52.907 1.00 24.37 ? 240 CYS B SG  1 
ATOM   3776 N N   . GLY B 1 247 ? 1.901   67.093 50.990 1.00 2.00  ? 241 GLY B N   1 
ATOM   3777 C CA  . GLY B 1 247 ? 1.547   65.685 50.987 1.00 70.10 ? 241 GLY B CA  1 
ATOM   3778 C C   . GLY B 1 247 ? 0.558   65.256 52.051 1.00 2.00  ? 241 GLY B C   1 
ATOM   3779 O O   . GLY B 1 247 ? 0.324   64.046 52.235 1.00 9.57  ? 241 GLY B O   1 
ATOM   3780 N N   . ILE B 1 248 ? -0.048  66.220 52.732 1.00 2.00  ? 242 ILE B N   1 
ATOM   3781 C CA  . ILE B 1 248 ? -0.870  65.931 53.929 1.00 2.00  ? 242 ILE B CA  1 
ATOM   3782 C C   . ILE B 1 248 ? -2.041  64.982 53.668 1.00 11.31 ? 242 ILE B C   1 
ATOM   3783 O O   . ILE B 1 248 ? -2.473  64.274 54.556 1.00 5.05  ? 242 ILE B O   1 
ATOM   3784 C CB  . ILE B 1 248 ? -1.430  67.252 54.588 1.00 6.03  ? 242 ILE B CB  1 
ATOM   3785 C CG1 . ILE B 1 248 ? -1.731  67.022 56.073 1.00 11.04 ? 242 ILE B CG1 1 
ATOM   3786 C CG2 . ILE B 1 248 ? -2.710  67.706 53.885 1.00 19.87 ? 242 ILE B CG2 1 
ATOM   3787 C CD1 . ILE B 1 248 ? -0.578  66.426 56.821 1.00 15.69 ? 242 ILE B CD1 1 
ATOM   3788 N N   . GLU B 1 249 ? -2.557  64.980 52.445 1.00 2.00  ? 243 GLU B N   1 
ATOM   3789 C CA  . GLU B 1 249 ? -3.723  64.166 52.111 1.00 14.71 ? 243 GLU B CA  1 
ATOM   3790 C C   . GLU B 1 249 ? -3.292  62.936 51.325 1.00 2.00  ? 243 GLU B C   1 
ATOM   3791 O O   . GLU B 1 249 ? -4.126  62.210 50.789 1.00 11.58 ? 243 GLU B O   1 
ATOM   3792 C CB  . GLU B 1 249 ? -4.734  64.979 51.292 1.00 2.00  ? 243 GLU B CB  1 
ATOM   3793 C CG  . GLU B 1 249 ? -5.573  65.946 52.132 1.00 9.41  ? 243 GLU B CG  1 
ATOM   3794 C CD  . GLU B 1 249 ? -5.600  67.363 51.571 1.00 34.96 ? 243 GLU B CD  1 
ATOM   3795 O OE1 . GLU B 1 249 ? -5.463  67.511 50.346 1.00 12.68 ? 243 GLU B OE1 1 
ATOM   3796 O OE2 . GLU B 1 249 ? -5.726  68.334 52.348 1.00 2.00  ? 243 GLU B OE2 1 
ATOM   3797 N N   . SER B 1 250 ? -1.979  62.774 51.186 1.00 2.00  ? 244 SER B N   1 
ATOM   3798 C CA  . SER B 1 250 ? -1.424  61.732 50.351 1.00 2.00  ? 244 SER B CA  1 
ATOM   3799 C C   . SER B 1 250 ? -1.242  60.362 51.026 1.00 2.00  ? 244 SER B C   1 
ATOM   3800 O O   . SER B 1 250 ? -1.180  59.350 50.342 1.00 15.69 ? 244 SER B O   1 
ATOM   3801 C CB  . SER B 1 250 ? -0.085  62.179 49.772 1.00 39.55 ? 244 SER B CB  1 
ATOM   3802 O OG  . SER B 1 250 ? -0.293  62.879 48.565 1.00 19.56 ? 244 SER B OG  1 
ATOM   3803 N N   . GLU B 1 251 ? -1.026  60.335 52.332 1.00 30.27 ? 245 GLU B N   1 
ATOM   3804 C CA  . GLU B 1 251 ? -0.629  59.084 52.968 1.00 19.61 ? 245 GLU B CA  1 
ATOM   3805 C C   . GLU B 1 251 ? -1.325  58.785 54.286 1.00 16.20 ? 245 GLU B C   1 
ATOM   3806 O O   . GLU B 1 251 ? -0.690  58.703 55.321 1.00 6.91  ? 245 GLU B O   1 
ATOM   3807 C CB  . GLU B 1 251 ? 0.861   59.087 53.168 1.00 2.00  ? 245 GLU B CB  1 
ATOM   3808 C CG  . GLU B 1 251 ? 1.670   59.156 51.911 1.00 30.70 ? 245 GLU B CG  1 
ATOM   3809 C CD  . GLU B 1 251 ? 3.127   59.073 52.235 1.00 40.11 ? 245 GLU B CD  1 
ATOM   3810 O OE1 . GLU B 1 251 ? 3.713   60.077 52.676 1.00 23.81 ? 245 GLU B OE1 1 
ATOM   3811 O OE2 . GLU B 1 251 ? 3.640   57.948 52.284 1.00 14.55 ? 245 GLU B OE2 1 
ATOM   3812 N N   . ILE B 1 252 ? -2.620  58.507 54.188 1.00 2.00  ? 246 ILE B N   1 
ATOM   3813 C CA  . ILE B 1 252 ? -3.507  58.335 55.328 1.00 2.79  ? 246 ILE B CA  1 
ATOM   3814 C C   . ILE B 1 252 ? -3.785  56.857 55.503 1.00 28.77 ? 246 ILE B C   1 
ATOM   3815 O O   . ILE B 1 252 ? -4.401  56.219 54.642 1.00 13.54 ? 246 ILE B O   1 
ATOM   3816 C CB  . ILE B 1 252 ? -4.870  59.030 55.064 1.00 3.67  ? 246 ILE B CB  1 
ATOM   3817 C CG1 . ILE B 1 252 ? -4.637  60.474 54.652 1.00 2.04  ? 246 ILE B CG1 1 
ATOM   3818 C CG2 . ILE B 1 252 ? -5.783  58.874 56.267 1.00 13.40 ? 246 ILE B CG2 1 
ATOM   3819 C CD1 . ILE B 1 252 ? -3.842  61.282 55.657 1.00 18.53 ? 246 ILE B CD1 1 
ATOM   3820 N N   . VAL B 1 253 ? -3.513  56.372 56.699 1.00 14.02 ? 247 VAL B N   1 
ATOM   3821 C CA  . VAL B 1 253 ? -3.717  54.965 57.013 1.00 16.32 ? 247 VAL B CA  1 
ATOM   3822 C C   . VAL B 1 253 ? -4.497  54.875 58.299 1.00 32.42 ? 247 VAL B C   1 
ATOM   3823 O O   . VAL B 1 253 ? -4.464  55.792 59.134 1.00 2.00  ? 247 VAL B O   1 
ATOM   3824 C CB  . VAL B 1 253 ? -2.403  54.232 57.224 1.00 2.00  ? 247 VAL B CB  1 
ATOM   3825 C CG1 . VAL B 1 253 ? -2.622  52.739 57.129 1.00 17.71 ? 247 VAL B CG1 1 
ATOM   3826 C CG2 . VAL B 1 253 ? -1.390  54.681 56.203 1.00 32.21 ? 247 VAL B CG2 1 
ATOM   3827 N N   . ALA B 1 254 ? -5.187  53.756 58.453 1.00 4.98  ? 248 ALA B N   1 
ATOM   3828 C CA  . ALA B 1 254 ? -6.123  53.558 59.537 1.00 11.48 ? 248 ALA B CA  1 
ATOM   3829 C C   . ALA B 1 254 ? -6.470  52.068 59.637 1.00 2.15  ? 248 ALA B C   1 
ATOM   3830 O O   . ALA B 1 254 ? -5.880  51.239 58.947 1.00 2.00  ? 248 ALA B O   1 
ATOM   3831 C CB  . ALA B 1 254 ? -7.370  54.396 59.283 1.00 2.00  ? 248 ALA B CB  1 
ATOM   3832 N N   . GLY B 1 255 ? -7.524  51.779 60.401 1.00 8.80  ? 249 GLY B N   1 
ATOM   3833 C CA  . GLY B 1 255 ? -7.864  50.434 60.814 1.00 2.00  ? 249 GLY B CA  1 
ATOM   3834 C C   . GLY B 1 255 ? -8.962  50.386 61.882 1.00 13.46 ? 249 GLY B C   1 
ATOM   3835 O O   . GLY B 1 255 ? -9.310  51.381 62.509 1.00 2.00  ? 249 GLY B O   1 
ATOM   3836 N N   . ILE B 1 256 ? -9.596  49.235 62.018 1.00 2.00  ? 250 ILE B N   1 
ATOM   3837 C CA  . ILE B 1 256 ? -10.664 49.080 62.980 1.00 21.29 ? 250 ILE B CA  1 
ATOM   3838 C C   . ILE B 1 256 ? -10.199 48.045 63.991 1.00 7.31  ? 250 ILE B C   1 
ATOM   3839 O O   . ILE B 1 256 ? -9.749  46.962 63.604 1.00 7.20  ? 250 ILE B O   1 
ATOM   3840 C CB  . ILE B 1 256 ? -11.965 48.602 62.289 1.00 3.89  ? 250 ILE B CB  1 
ATOM   3841 C CG1 . ILE B 1 256 ? -12.407 49.603 61.229 1.00 3.92  ? 250 ILE B CG1 1 
ATOM   3842 C CG2 . ILE B 1 256 ? -13.067 48.428 63.306 1.00 63.99 ? 250 ILE B CG2 1 
ATOM   3843 C CD1 . ILE B 1 256 ? -12.200 51.055 61.594 1.00 2.00  ? 250 ILE B CD1 1 
ATOM   3844 N N   . PRO B 1 257 ? -10.224 48.387 65.301 1.00 22.72 ? 251 PRO B N   1 
ATOM   3845 C CA  . PRO B 1 257 ? -9.860  47.428 66.358 1.00 2.00  ? 251 PRO B CA  1 
ATOM   3846 C C   . PRO B 1 257 ? -10.640 46.104 66.291 1.00 10.45 ? 251 PRO B C   1 
ATOM   3847 O O   . PRO B 1 257 ? -11.812 46.082 65.852 1.00 2.00  ? 251 PRO B O   1 
ATOM   3848 C CB  . PRO B 1 257 ? -10.180 48.191 67.647 1.00 2.00  ? 251 PRO B CB  1 
ATOM   3849 C CG  . PRO B 1 257 ? -11.281 49.126 67.231 1.00 34.68 ? 251 PRO B CG  1 
ATOM   3850 C CD  . PRO B 1 257 ? -10.847 49.597 65.870 1.00 2.00  ? 251 PRO B CD  1 
ATOM   3851 N N   . ARG B 1 258 ? -9.973  44.987 66.621 1.00 2.00  ? 252 ARG B N   1 
ATOM   3852 C CA  . ARG B 1 258 ? -10.725 43.755 66.904 1.00 2.00  ? 252 ARG B CA  1 
ATOM   3853 C C   . ARG B 1 258 ? -11.234 43.833 68.334 1.00 41.57 ? 252 ARG B C   1 
ATOM   3854 O O   . ARG B 1 258 ? -10.441 43.991 69.280 1.00 28.54 ? 252 ARG B O   1 
ATOM   3855 C CB  . ARG B 1 258 ? -9.893  42.487 66.769 1.00 8.77  ? 252 ARG B CB  1 
ATOM   3856 C CG  . ARG B 1 258 ? -10.762 41.191 66.897 1.00 16.42 ? 252 ARG B CG  1 
ATOM   3857 C CD  . ARG B 1 258 ? -9.976  39.896 66.771 1.00 2.01  ? 252 ARG B CD  1 
ATOM   3858 N NE  . ARG B 1 258 ? -8.942  39.753 67.799 1.00 26.03 ? 252 ARG B NE  1 
ATOM   3859 C CZ  . ARG B 1 258 ? -9.167  39.342 69.044 1.00 3.48  ? 252 ARG B CZ  1 
ATOM   3860 N NH1 . ARG B 1 258 ? -10.408 39.096 69.454 1.00 25.25 ? 252 ARG B NH1 1 
ATOM   3861 N NH2 . ARG B 1 258 ? -8.147  39.169 69.874 1.00 44.04 ? 252 ARG B NH2 1 
ATOM   3862 N N   . THR B 1 259 ? -12.557 43.771 68.475 1.00 7.08  ? 253 THR B N   1 
ATOM   3863 C CA  . THR B 1 259 ? -13.216 43.959 69.773 1.00 88.53 ? 253 THR B CA  1 
ATOM   3864 C C   . THR B 1 259 ? -14.502 43.144 69.911 1.00 48.05 ? 253 THR B C   1 
ATOM   3865 O O   . THR B 1 259 ? -14.716 42.487 70.930 1.00 75.21 ? 253 THR B O   1 
ATOM   3866 C CB  . THR B 1 259 ? -13.560 45.452 70.026 1.00 44.68 ? 253 THR B CB  1 
ATOM   3867 O OG1 . THR B 1 259 ? -14.046 46.043 68.817 1.00 17.92 ? 253 THR B OG1 1 
ATOM   3868 C CG2 . THR B 1 259 ? -12.324 46.222 70.467 1.00 33.31 ? 253 THR B CG2 1 
HETATM 3869 O O   . HOH C 2 .   ? 2.226   37.152 32.255 0.96 18.92 ? 601 HOH A O   1 
HETATM 3870 O O   . HOH C 2 .   ? 3.507   45.118 25.601 1.00 17.49 ? 602 HOH A O   1 
HETATM 3871 O O   . HOH C 2 .   ? -3.882  46.529 18.812 0.86 25.74 ? 603 HOH A O   1 
HETATM 3872 O O   . HOH C 2 .   ? 1.955   47.420 19.258 1.00 30.25 ? 604 HOH A O   1 
HETATM 3873 O O   . HOH C 2 .   ? 4.257   48.699 18.983 1.00 20.93 ? 605 HOH A O   1 
HETATM 3874 O O   . HOH C 2 .   ? 7.837   48.674 23.465 0.79 8.91  ? 606 HOH A O   1 
HETATM 3875 O O   . HOH C 2 .   ? 0.468   51.115 24.965 1.00 3.30  ? 607 HOH A O   1 
HETATM 3876 O O   . HOH C 2 .   ? 5.775   54.739 28.767 1.00 26.27 ? 608 HOH A O   1 
HETATM 3877 O O   . HOH C 2 .   ? 14.890  62.725 28.874 1.00 2.00  ? 610 HOH A O   1 
HETATM 3878 O O   . HOH C 2 .   ? 11.345  67.013 23.028 1.00 37.65 ? 611 HOH A O   1 
HETATM 3879 O O   . HOH C 2 .   ? 10.088  66.081 20.126 0.98 11.21 ? 612 HOH A O   1 
HETATM 3880 O O   . HOH C 2 .   ? 15.825  52.726 34.476 1.00 5.09  ? 614 HOH A O   1 
HETATM 3881 O O   . HOH C 2 .   ? 10.002  56.150 37.721 1.00 2.01  ? 615 HOH A O   1 
HETATM 3882 O O   . HOH C 2 .   ? 9.181   53.932 36.422 1.00 2.00  ? 616 HOH A O   1 
HETATM 3883 O O   . HOH C 2 .   ? -1.256  53.581 49.487 1.00 33.77 ? 617 HOH A O   1 
HETATM 3884 O O   . HOH C 2 .   ? -8.458  57.732 26.910 0.92 12.19 ? 618 HOH A O   1 
HETATM 3885 O O   . HOH C 2 .   ? 5.894   63.179 27.742 0.91 5.26  ? 619 HOH A O   1 
HETATM 3886 O O   . HOH C 2 .   ? 4.479   69.888 41.080 1.00 2.98  ? 620 HOH A O   1 
HETATM 3887 O O   . HOH C 2 .   ? -4.959  59.566 43.773 0.96 8.11  ? 624 HOH A O   1 
HETATM 3888 O O   . HOH C 2 .   ? -1.320  60.705 20.923 0.69 43.92 ? 626 HOH A O   1 
HETATM 3889 O O   . HOH C 2 .   ? 1.941   63.297 16.964 0.97 14.50 ? 627 HOH A O   1 
HETATM 3890 O O   . HOH C 2 .   ? 21.007  55.967 33.123 1.00 4.03  ? 628 HOH A O   1 
HETATM 3891 O O   . HOH C 2 .   ? 27.329  59.354 34.351 1.00 29.31 ? 629 HOH A O   1 
HETATM 3892 O O   . HOH C 2 .   ? 3.099   43.586 53.270 0.98 7.23  ? 630 HOH A O   1 
HETATM 3893 O O   . HOH C 2 .   ? 3.254   45.757 55.604 0.99 2.00  ? 632 HOH A O   1 
HETATM 3894 O O   . HOH C 2 .   ? 16.799  50.765 48.087 1.00 14.20 ? 636 HOH A O   1 
HETATM 3895 O O   . HOH C 2 .   ? -7.832  50.634 50.473 1.00 32.91 ? 637 HOH A O   1 
HETATM 3896 O O   . HOH C 2 .   ? 21.779  45.591 45.069 0.85 13.58 ? 638 HOH A O   1 
HETATM 3897 O O   . HOH C 2 .   ? 17.758  38.789 37.204 1.00 30.16 ? 639 HOH A O   1 
HETATM 3898 O O   . HOH C 2 .   ? 5.494   74.635 36.398 1.00 6.61  ? 642 HOH A O   1 
HETATM 3899 O O   . HOH C 2 .   ? 22.805  49.820 36.473 0.97 10.83 ? 643 HOH A O   1 
HETATM 3900 O O   . HOH C 2 .   ? 8.355   43.310 50.159 0.80 4.30  ? 644 HOH A O   1 
HETATM 3901 O O   . HOH C 2 .   ? 4.706   51.961 47.383 1.00 2.00  ? 645 HOH A O   1 
HETATM 3902 O O   . HOH C 2 .   ? 0.024   50.846 49.259 1.00 5.63  ? 646 HOH A O   1 
HETATM 3903 O O   . HOH C 2 .   ? -17.371 58.793 32.206 1.00 34.37 ? 649 HOH A O   1 
HETATM 3904 O O   . HOH C 2 .   ? 11.402  62.339 47.644 0.67 22.33 ? 667 HOH A O   1 
HETATM 3905 O O   . HOH C 2 .   ? 4.058   58.277 47.619 1.00 49.58 ? 675 HOH A O   1 
HETATM 3906 O O   . HOH C 2 .   ? 8.782   66.483 47.922 1.00 21.76 ? 681 HOH A O   1 
HETATM 3907 O O   . HOH C 2 .   ? 3.514   46.290 21.577 0.90 23.41 ? 685 HOH A O   1 
HETATM 3908 O O   . HOH C 2 .   ? 5.184   51.085 18.375 1.00 38.21 ? 686 HOH A O   1 
HETATM 3909 O O   . HOH C 2 .   ? 8.116   53.005 31.727 0.90 7.05  ? 687 HOH A O   1 
HETATM 3910 O O   . HOH C 2 .   ? 4.480   52.844 30.318 1.00 2.87  ? 690 HOH A O   1 
HETATM 3911 O O   . HOH C 2 .   ? -8.947  48.913 32.805 1.00 51.52 ? 691 HOH A O   1 
HETATM 3912 O O   . HOH C 2 .   ? 11.446  61.235 29.012 0.85 25.31 ? 692 HOH A O   1 
HETATM 3913 O O   . HOH C 2 .   ? 8.560   58.754 22.309 0.94 26.96 ? 693 HOH A O   1 
HETATM 3914 O O   . HOH C 2 .   ? 4.502   73.220 41.937 1.00 74.23 ? 694 HOH A O   1 
HETATM 3915 O O   . HOH C 2 .   ? 8.203   69.071 47.604 1.00 43.46 ? 695 HOH A O   1 
HETATM 3916 O O   . HOH C 2 .   ? 1.189   59.903 47.079 0.85 10.29 ? 696 HOH A O   1 
HETATM 3917 O O   . HOH C 2 .   ? -9.208  61.194 41.825 0.63 6.53  ? 698 HOH A O   1 
HETATM 3918 O O   . HOH C 2 .   ? -8.260  70.183 39.771 0.85 20.13 ? 699 HOH A O   1 
HETATM 3919 O O   . HOH C 2 .   ? 4.052   59.598 16.707 0.85 13.54 ? 701 HOH A O   1 
HETATM 3920 O O   . HOH C 2 .   ? -2.705  74.405 21.254 1.00 31.61 ? 702 HOH A O   1 
HETATM 3921 O O   . HOH C 2 .   ? -5.291  75.374 25.325 1.00 25.10 ? 703 HOH A O   1 
HETATM 3922 O O   . HOH C 2 .   ? -8.861  69.751 31.163 0.94 17.87 ? 704 HOH A O   1 
HETATM 3923 O O   . HOH C 2 .   ? -3.384  72.486 32.856 0.94 27.26 ? 705 HOH A O   1 
HETATM 3924 O O   . HOH C 2 .   ? -6.854  74.423 23.428 1.00 18.38 ? 706 HOH A O   1 
HETATM 3925 O O   . HOH C 2 .   ? 0.937   41.494 52.819 1.00 17.10 ? 707 HOH A O   1 
HETATM 3926 O O   . HOH C 2 .   ? 11.380  56.091 55.793 0.78 31.63 ? 708 HOH A O   1 
HETATM 3927 O O   . HOH C 2 .   ? 7.435   54.409 50.802 1.00 13.48 ? 709 HOH A O   1 
HETATM 3928 O O   . HOH C 2 .   ? 12.591  47.206 54.885 0.80 16.10 ? 710 HOH A O   1 
HETATM 3929 O O   . HOH C 2 .   ? 9.208   34.607 37.933 0.83 23.59 ? 712 HOH A O   1 
HETATM 3930 O O   . HOH C 2 .   ? 21.344  47.904 30.815 0.91 6.73  ? 714 HOH A O   1 
HETATM 3931 O O   . HOH C 2 .   ? -5.710  40.427 32.900 1.00 45.91 ? 731 HOH A O   1 
HETATM 3932 O O   . HOH C 2 .   ? -0.336  48.743 18.397 1.00 57.43 ? 736 HOH A O   1 
HETATM 3933 O O   . HOH C 2 .   ? 13.863  60.969 27.260 1.00 28.86 ? 737 HOH A O   1 
HETATM 3934 O O   . HOH C 2 .   ? 19.574  60.384 39.377 1.00 31.42 ? 738 HOH A O   1 
HETATM 3935 O O   . HOH C 2 .   ? 7.887   69.646 16.947 0.75 17.96 ? 739 HOH A O   1 
HETATM 3936 O O   . HOH C 2 .   ? 3.226   65.663 16.123 1.00 55.29 ? 740 HOH A O   1 
HETATM 3937 O O   . HOH C 2 .   ? 6.669   61.902 48.573 1.00 27.55 ? 741 HOH A O   1 
HETATM 3938 O O   . HOH C 2 .   ? -10.329 60.720 27.658 1.00 61.52 ? 742 HOH A O   1 
HETATM 3939 O O   . HOH C 2 .   ? -4.381  73.454 44.490 0.66 24.95 ? 743 HOH A O   1 
HETATM 3940 O O   . HOH C 2 .   ? -12.739 68.514 40.822 0.94 59.18 ? 744 HOH A O   1 
HETATM 3941 O O   . HOH C 2 .   ? -12.626 60.193 41.231 0.72 27.47 ? 745 HOH A O   1 
HETATM 3942 O O   . HOH C 2 .   ? 28.771  52.217 38.607 0.75 56.84 ? 746 HOH A O   1 
HETATM 3943 O O   . HOH C 2 .   ? 15.626  64.863 46.435 0.88 44.88 ? 747 HOH A O   1 
HETATM 3944 O O   . HOH C 2 .   ? 11.910  65.804 48.705 0.59 7.66  ? 752 HOH A O   1 
HETATM 3945 O O   . HOH C 2 .   ? -11.177 64.864 42.824 1.00 53.63 ? 754 HOH A O   1 
HETATM 3946 O O   . HOH C 2 .   ? -11.229 67.732 27.378 0.59 11.17 ? 756 HOH A O   1 
HETATM 3947 O O   . HOH C 2 .   ? 2.918   25.935 40.023 0.98 32.36 ? 761 HOH A O   1 
HETATM 3948 O O   . HOH C 2 .   ? 2.994   72.467 28.832 1.00 34.57 ? 762 HOH A O   1 
HETATM 3949 O O   . HOH C 2 .   ? 25.911  45.460 41.868 0.77 5.98  ? 763 HOH A O   1 
HETATM 3950 O O   . HOH C 2 .   ? 7.704   75.897 38.874 0.78 27.00 ? 764 HOH A O   1 
HETATM 3951 O O   . HOH C 2 .   ? 0.742   55.208 52.572 0.88 37.57 ? 767 HOH A O   1 
HETATM 3952 O O   . HOH C 2 .   ? 7.411   33.507 28.287 0.97 55.73 ? 770 HOH A O   1 
HETATM 3953 O O   . HOH C 2 .   ? -16.247 56.730 42.752 0.70 41.98 ? 771 HOH A O   1 
HETATM 3954 O O   . HOH C 2 .   ? -4.446  59.219 20.566 1.00 44.21 ? 772 HOH A O   1 
HETATM 3955 O O   . HOH C 2 .   ? 26.838  47.106 44.043 0.83 5.63  ? 774 HOH A O   1 
HETATM 3956 O O   . HOH C 2 .   ? -3.379  73.343 35.486 0.91 56.06 ? 776 HOH A O   1 
HETATM 3957 O O   . HOH C 2 .   ? 9.472   56.553 51.393 0.93 28.78 ? 778 HOH A O   1 
HETATM 3958 O O   . HOH C 2 .   ? -2.425  54.046 25.450 1.00 19.00 ? 780 HOH A O   1 
HETATM 3959 O O   . HOH C 2 .   ? -5.400  55.231 18.728 1.00 43.05 ? 781 HOH A O   1 
HETATM 3960 O O   . HOH C 2 .   ? 8.170   60.688 27.732 1.00 23.12 ? 782 HOH A O   1 
HETATM 3961 O O   . HOH C 2 .   ? -1.507  40.291 51.233 0.81 24.46 ? 784 HOH A O   1 
HETATM 3962 O O   . HOH C 2 .   ? 26.540  53.211 45.867 0.86 11.63 ? 785 HOH A O   1 
HETATM 3963 O O   . HOH C 2 .   ? 15.322  59.264 44.201 0.99 37.04 ? 786 HOH A O   1 
HETATM 3964 O O   . HOH C 2 .   ? 12.577  30.345 37.345 0.81 28.07 ? 787 HOH A O   1 
HETATM 3965 O O   . HOH D 2 .   ? 5.302   49.052 88.458 1.00 59.79 ? 609 HOH B O   1 
HETATM 3966 O O   . HOH D 2 .   ? 7.307   53.346 83.814 1.00 31.13 ? 613 HOH B O   1 
HETATM 3967 O O   . HOH D 2 .   ? 3.688   71.762 49.741 1.00 54.70 ? 621 HOH B O   1 
HETATM 3968 O O   . HOH D 2 .   ? 5.696   72.342 48.157 1.00 43.22 ? 622 HOH B O   1 
HETATM 3969 O O   . HOH D 2 .   ? -4.024  65.248 45.336 1.00 29.97 ? 623 HOH B O   1 
HETATM 3970 O O   . HOH D 2 .   ? -11.373 55.719 46.519 0.83 12.81 ? 625 HOH B O   1 
HETATM 3971 O O   . HOH D 2 .   ? 0.770   41.613 57.463 1.00 39.28 ? 631 HOH B O   1 
HETATM 3972 O O   . HOH D 2 .   ? -1.478  49.167 56.330 1.00 5.19  ? 633 HOH B O   1 
HETATM 3973 O O   . HOH D 2 .   ? -2.399  50.299 54.079 0.92 2.00  ? 634 HOH B O   1 
HETATM 3974 O O   . HOH D 2 .   ? -6.106  44.195 56.481 0.69 8.20  ? 635 HOH B O   1 
HETATM 3975 O O   . HOH D 2 .   ? 13.815  52.915 56.498 1.00 33.60 ? 640 HOH B O   1 
HETATM 3976 O O   . HOH D 2 .   ? 14.986  55.205 56.160 1.00 37.87 ? 641 HOH B O   1 
HETATM 3977 O O   . HOH D 2 .   ? 3.965   54.067 55.022 1.00 21.37 ? 647 HOH B O   1 
HETATM 3978 O O   . HOH D 2 .   ? -1.914  55.394 52.162 0.82 15.29 ? 648 HOH B O   1 
HETATM 3979 O O   . HOH D 2 .   ? -16.261 68.738 67.747 1.00 22.31 ? 650 HOH B O   1 
HETATM 3980 O O   . HOH D 2 .   ? -10.855 63.099 74.651 1.00 19.64 ? 651 HOH B O   1 
HETATM 3981 O O   . HOH D 2 .   ? -9.241  57.068 74.887 1.00 14.26 ? 652 HOH B O   1 
HETATM 3982 O O   . HOH D 2 .   ? -1.485  67.854 75.699 1.00 29.65 ? 653 HOH B O   1 
HETATM 3983 O O   . HOH D 2 .   ? -0.686  62.555 70.051 0.86 8.36  ? 654 HOH B O   1 
HETATM 3984 O O   . HOH D 2 .   ? -2.154  59.618 72.336 1.00 25.21 ? 655 HOH B O   1 
HETATM 3985 O O   . HOH D 2 .   ? 4.106   68.026 69.531 1.00 2.00  ? 656 HOH B O   1 
HETATM 3986 O O   . HOH D 2 .   ? 1.528   62.334 66.551 1.00 2.41  ? 657 HOH B O   1 
HETATM 3987 O O   . HOH D 2 .   ? 2.080   62.999 70.515 0.95 19.16 ? 658 HOH B O   1 
HETATM 3988 O O   . HOH D 2 .   ? 15.710  61.031 75.113 0.95 11.15 ? 659 HOH B O   1 
HETATM 3989 O O   . HOH D 2 .   ? 9.327   60.195 76.033 1.00 3.63  ? 660 HOH B O   1 
HETATM 3990 O O   . HOH D 2 .   ? 10.359  48.611 62.977 1.00 25.30 ? 661 HOH B O   1 
HETATM 3991 O O   . HOH D 2 .   ? -16.239 59.391 82.111 1.00 67.60 ? 662 HOH B O   1 
HETATM 3992 O O   . HOH D 2 .   ? -8.888  46.086 70.123 0.80 11.32 ? 663 HOH B O   1 
HETATM 3993 O O   . HOH D 2 .   ? 5.518   52.748 74.784 0.81 27.57 ? 664 HOH B O   1 
HETATM 3994 O O   . HOH D 2 .   ? -4.243  46.261 78.066 1.00 15.36 ? 665 HOH B O   1 
HETATM 3995 O O   . HOH D 2 .   ? -5.494  43.402 78.777 1.00 55.54 ? 666 HOH B O   1 
HETATM 3996 O O   . HOH D 2 .   ? 4.925   56.525 87.886 0.68 14.59 ? 668 HOH B O   1 
HETATM 3997 O O   . HOH D 2 .   ? 9.238   54.271 81.179 0.92 26.08 ? 669 HOH B O   1 
HETATM 3998 O O   . HOH D 2 .   ? -1.183  82.333 52.269 0.73 13.13 ? 670 HOH B O   1 
HETATM 3999 O O   . HOH D 2 .   ? 5.978   58.871 74.765 0.82 25.61 ? 671 HOH B O   1 
HETATM 4000 O O   . HOH D 2 .   ? 0.485   57.414 80.665 0.99 15.10 ? 672 HOH B O   1 
HETATM 4001 O O   . HOH D 2 .   ? -8.394  45.476 72.612 1.00 37.94 ? 673 HOH B O   1 
HETATM 4002 O O   . HOH D 2 .   ? -4.128  59.588 51.539 0.97 10.08 ? 674 HOH B O   1 
HETATM 4003 O O   . HOH D 2 .   ? -0.886  62.203 54.601 1.00 10.59 ? 676 HOH B O   1 
HETATM 4004 O O   . HOH D 2 .   ? 2.923   62.774 52.258 0.99 3.63  ? 677 HOH B O   1 
HETATM 4005 O O   . HOH D 2 .   ? -6.477  66.504 48.075 0.98 29.62 ? 678 HOH B O   1 
HETATM 4006 O O   . HOH D 2 .   ? -3.863  70.424 52.141 1.00 16.42 ? 679 HOH B O   1 
HETATM 4007 O O   . HOH D 2 .   ? 6.356   71.334 55.951 0.77 2.00  ? 680 HOH B O   1 
HETATM 4008 O O   . HOH D 2 .   ? -1.888  80.122 50.552 0.85 63.81 ? 682 HOH B O   1 
HETATM 4009 O O   . HOH D 2 .   ? -7.797  74.825 49.940 1.00 40.71 ? 683 HOH B O   1 
HETATM 4010 O O   . HOH D 2 .   ? 4.239   62.889 76.601 1.00 50.58 ? 684 HOH B O   1 
HETATM 4011 O O   . HOH D 2 .   ? 2.952   48.426 85.440 1.00 30.92 ? 688 HOH B O   1 
HETATM 4012 O O   . HOH D 2 .   ? 6.704   41.019 87.079 0.87 57.45 ? 689 HOH B O   1 
HETATM 4013 O O   . HOH D 2 .   ? -5.395  58.444 46.395 1.00 9.79  ? 697 HOH B O   1 
HETATM 4014 O O   . HOH D 2 .   ? 9.774   62.395 82.356 0.78 9.88  ? 700 HOH B O   1 
HETATM 4015 O O   . HOH D 2 .   ? 18.075  53.831 57.811 0.87 14.93 ? 711 HOH B O   1 
HETATM 4016 O O   . HOH D 2 .   ? 20.674  49.077 71.277 0.74 9.85  ? 713 HOH B O   1 
HETATM 4017 O O   . HOH D 2 .   ? -2.859  57.567 50.004 0.71 2.27  ? 715 HOH B O   1 
HETATM 4018 O O   . HOH D 2 .   ? 1.857   57.160 55.329 1.00 43.00 ? 716 HOH B O   1 
HETATM 4019 O O   . HOH D 2 .   ? -23.067 64.488 55.489 1.00 41.54 ? 717 HOH B O   1 
HETATM 4020 O O   . HOH D 2 .   ? -14.845 72.980 56.681 0.80 30.35 ? 718 HOH B O   1 
HETATM 4021 O O   . HOH D 2 .   ? -7.965  53.743 74.344 1.00 25.41 ? 719 HOH B O   1 
HETATM 4022 O O   . HOH D 2 .   ? 15.819  60.833 65.588 1.00 29.95 ? 720 HOH B O   1 
HETATM 4023 O O   . HOH D 2 .   ? 17.257  63.310 75.478 1.00 24.82 ? 721 HOH B O   1 
HETATM 4024 O O   . HOH D 2 .   ? 3.761   55.831 74.687 1.00 43.26 ? 722 HOH B O   1 
HETATM 4025 O O   . HOH D 2 .   ? 14.429  48.232 64.254 0.76 9.18  ? 723 HOH B O   1 
HETATM 4026 O O   . HOH D 2 .   ? 8.505   49.275 79.169 1.00 39.71 ? 724 HOH B O   1 
HETATM 4027 O O   . HOH D 2 .   ? 7.217   59.905 77.511 0.79 3.99  ? 725 HOH B O   1 
HETATM 4028 O O   . HOH D 2 .   ? 15.114  52.621 76.130 0.74 14.84 ? 726 HOH B O   1 
HETATM 4029 O O   . HOH D 2 .   ? 5.472   39.688 80.612 0.82 9.26  ? 727 HOH B O   1 
HETATM 4030 O O   . HOH D 2 .   ? 9.533   69.972 72.558 1.00 13.66 ? 728 HOH B O   1 
HETATM 4031 O O   . HOH D 2 .   ? 7.717   75.787 67.980 0.96 18.41 ? 729 HOH B O   1 
HETATM 4032 O O   . HOH D 2 .   ? 4.905   41.111 69.283 0.96 2.00  ? 730 HOH B O   1 
HETATM 4033 O O   . HOH D 2 .   ? -9.733  46.489 54.460 1.00 49.12 ? 732 HOH B O   1 
HETATM 4034 O O   . HOH D 2 .   ? -9.161  66.505 47.576 0.60 23.46 ? 733 HOH B O   1 
HETATM 4035 O O   . HOH D 2 .   ? 5.836   62.708 52.634 0.81 23.95 ? 734 HOH B O   1 
HETATM 4036 O O   . HOH D 2 .   ? 0.597   37.443 68.699 0.91 32.93 ? 748 HOH B O   1 
HETATM 4037 O O   . HOH D 2 .   ? 4.105   61.804 65.452 1.00 24.09 ? 749 HOH B O   1 
HETATM 4038 O O   . HOH D 2 .   ? 10.162  45.457 73.841 1.00 35.70 ? 750 HOH B O   1 
HETATM 4039 O O   . HOH D 2 .   ? -14.232 39.836 69.360 1.00 54.98 ? 751 HOH B O   1 
HETATM 4040 O O   . HOH D 2 .   ? 0.951   81.699 60.791 0.82 7.16  ? 753 HOH B O   1 
HETATM 4041 O O   . HOH D 2 .   ? -13.201 65.441 47.999 0.82 17.32 ? 755 HOH B O   1 
HETATM 4042 O O   . HOH D 2 .   ? -20.344 67.365 50.604 0.72 4.35  ? 757 HOH B O   1 
HETATM 4043 O O   . HOH D 2 .   ? 13.688  63.484 67.418 1.00 67.11 ? 758 HOH B O   1 
HETATM 4044 O O   . HOH D 2 .   ? 11.067  47.074 64.845 0.94 27.60 ? 759 HOH B O   1 
HETATM 4045 O O   . HOH D 2 .   ? 3.328   38.690 69.834 1.00 27.74 ? 760 HOH B O   1 
HETATM 4046 O O   . HOH D 2 .   ? -3.839  37.495 61.661 1.00 37.12 ? 765 HOH B O   1 
HETATM 4047 O O   . HOH D 2 .   ? 3.433   40.467 83.011 1.00 12.55 ? 766 HOH B O   1 
HETATM 4048 O O   . HOH D 2 .   ? 0.031   57.756 48.508 0.88 11.24 ? 768 HOH B O   1 
HETATM 4049 O O   . HOH D 2 .   ? 17.442  72.584 60.904 0.93 53.36 ? 769 HOH B O   1 
HETATM 4050 O O   . HOH D 2 .   ? 2.600   41.437 60.457 1.00 29.43 ? 773 HOH B O   1 
HETATM 4051 O O   . HOH D 2 .   ? -11.672 73.517 71.139 0.61 55.03 ? 775 HOH B O   1 
HETATM 4052 O O   . HOH D 2 .   ? 10.812  47.506 77.104 0.86 52.78 ? 777 HOH B O   1 
HETATM 4053 O O   . HOH D 2 .   ? 9.153   58.283 60.475 1.00 33.40 ? 779 HOH B O   1 
HETATM 4054 O O   . HOH D 2 .   ? 17.328  57.903 66.057 1.00 21.32 ? 783 HOH B O   1 
HETATM 4055 O O   . HOH D 2 .   ? -18.626 58.978 79.780 0.90 37.22 ? 788 HOH B O   1 
HETATM 4056 O O   . HOH D 2 .   ? 5.318   82.218 56.880 0.82 26.49 ? 789 HOH B O   1 
HETATM 4057 O O   . HOH D 2 .   ? 19.496  56.904 58.684 0.98 26.16 ? 790 HOH B O   1 
HETATM 4058 O O   . HOH D 2 .   ? 12.555  66.864 66.687 0.80 29.06 ? 791 HOH B O   1 
# 
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   PHE 1   -5  ?   ?   ?   A . n 
A 1 2   SER 2   -4  ?   ?   ?   A . n 
A 1 3   GLU 3   -3  ?   ?   ?   A . n 
A 1 4   ASP 4   -2  ?   ?   ?   A . n 
A 1 5   ILE 5   -1  ?   ?   ?   A . n 
A 1 6   ASN 6   0   ?   ?   ?   A . n 
A 1 7   LEU 7   1   1   LEU LEU A . n 
A 1 8   PRO 8   2   2   PRO PRO A . n 
A 1 9   GLU 9   3   3   GLU GLU A . n 
A 1 10  SER 10  4   4   SER SER A . n 
A 1 11  PHE 11  5   5   PHE PHE A . n 
A 1 12  ASP 12  6   6   ASP ASP A . n 
A 1 13  ALA 13  7   7   ALA ALA A . n 
A 1 14  ARG 14  8   8   ARG ARG A . n 
A 1 15  GLU 15  9   9   GLU GLU A . n 
A 1 16  GLN 16  10  10  GLN GLN A . n 
A 1 17  TRP 17  11  11  TRP TRP A . n 
A 1 18  SER 18  12  12  SER SER A . n 
A 1 19  ASN 19  13  13  ASN ASN A . n 
A 1 20  CYS 20  14  14  CYS CYS A . n 
A 1 21  PRO 21  15  15  PRO PRO A . n 
A 1 22  THR 22  16  16  THR THR A . n 
A 1 23  ILE 23  17  17  ILE ILE A . n 
A 1 24  ALA 24  18  18  ALA ALA A . n 
A 1 25  GLN 25  19  19  GLN GLN A . n 
A 1 26  ILE 26  20  20  ILE ILE A . n 
A 1 27  ARG 27  21  21  ARG ARG A . n 
A 1 28  ASP 28  22  22  ASP ASP A . n 
A 1 29  GLN 29  23  23  GLN GLN A . n 
A 1 30  GLY 30  24  24  GLY GLY A . n 
A 1 31  SER 31  25  25  SER SER A . n 
A 1 32  CYS 32  26  26  CYS CYS A . n 
A 1 33  GLY 33  27  27  GLY GLY A . n 
A 1 34  SER 34  28  28  SER SER A . n 
A 1 35  CYS 35  29  29  CYS CYS A . n 
A 1 36  TRP 36  30  30  TRP TRP A . n 
A 1 37  ALA 37  31  31  ALA ALA A . n 
A 1 38  PHE 38  32  32  PHE PHE A . n 
A 1 39  GLY 39  33  33  GLY GLY A . n 
A 1 40  ALA 40  34  34  ALA ALA A . n 
A 1 41  VAL 41  35  35  VAL VAL A . n 
A 1 42  GLU 42  36  36  GLU GLU A . n 
A 1 43  ALA 43  37  37  ALA ALA A . n 
A 1 44  MET 44  38  38  MET MET A . n 
A 1 45  SER 45  39  39  SER SER A . n 
A 1 46  ASP 46  40  40  ASP ASP A . n 
A 1 47  ARG 47  41  41  ARG ARG A . n 
A 1 48  ILE 48  42  42  ILE ILE A . n 
A 1 49  CYS 49  43  43  CYS CYS A . n 
A 1 50  ILE 50  44  44  ILE ILE A . n 
A 1 51  HIS 51  45  45  HIS HIS A . n 
A 1 52  THR 52  46  46  THR THR A . n 
A 1 53  ASN 53  47  47  ASN ASN A . n 
A 1 54  GLY 54  48  48  GLY GLY A . n 
A 1 55  ARG 55  49  49  ARG ARG A . n 
A 1 56  VAL 56  50  50  VAL VAL A . n 
A 1 57  ASN 57  51  51  ASN ASN A . n 
A 1 58  VAL 58  52  52  VAL VAL A . n 
A 1 59  GLU 59  53  53  GLU GLU A . n 
A 1 60  VAL 60  54  54  VAL VAL A . n 
A 1 61  SER 61  55  55  SER SER A . n 
A 1 62  ALA 62  56  56  ALA ALA A . n 
A 1 63  GLU 63  57  57  GLU GLU A . n 
A 1 64  ASP 64  58  58  ASP ASP A . n 
A 1 65  LEU 65  59  59  LEU LEU A . n 
A 1 66  LEU 66  60  60  LEU LEU A . n 
A 1 67  THR 67  61  61  THR THR A . n 
A 1 68  CYS 68  62  62  CYS CYS A . n 
A 1 69  CYS 69  63  63  CYS CYS A . n 
A 1 70  GLY 70  64  64  GLY GLY A . n 
A 1 71  ILE 71  65  65  ILE ILE A . n 
A 1 72  GLN 72  66  66  GLN GLN A . n 
A 1 73  CYS 73  67  67  CYS CYS A . n 
A 1 74  GLY 74  68  68  GLY GLY A . n 
A 1 75  ASP 75  69  69  ASP ASP A . n 
A 1 76  GLY 76  70  70  GLY GLY A . n 
A 1 77  CYS 77  71  71  CYS CYS A . n 
A 1 78  ASN 78  72  72  ASN ASN A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  GLY 80  74  74  GLY GLY A . n 
A 1 81  TYR 81  75  75  TYR TYR A . n 
A 1 82  PRO 82  76  76  PRO PRO A . n 
A 1 83  SER 83  77  77  SER SER A . n 
A 1 84  GLY 84  78  78  GLY GLY A . n 
A 1 85  ALA 85  79  79  ALA ALA A . n 
A 1 86  TRP 86  80  80  TRP TRP A . n 
A 1 87  ASN 87  81  81  ASN ASN A . n 
A 1 88  PHE 88  82  82  PHE PHE A . n 
A 1 89  TRP 89  83  83  TRP TRP A . n 
A 1 90  THR 90  84  84  THR THR A . n 
A 1 91  ARG 91  85  85  ARG ARG A . n 
A 1 92  LYS 92  86  86  LYS LYS A . n 
A 1 93  GLY 93  87  87  GLY GLY A . n 
A 1 94  LEU 94  88  88  LEU LEU A . n 
A 1 95  VAL 95  89  89  VAL VAL A . n 
A 1 96  SER 96  90  90  SER SER A . n 
A 1 97  GLY 97  91  91  GLY GLY A . n 
A 1 98  GLY 98  92  92  GLY GLY A . n 
A 1 99  VAL 99  93  93  VAL VAL A . n 
A 1 100 TYR 100 94  94  TYR TYR A . n 
A 1 101 ASN 101 95  95  ASN ASN A . n 
A 1 102 SER 102 96  96  SER SER A . n 
A 1 103 HIS 103 97  97  HIS HIS A . n 
A 1 104 ILE 104 98  98  ILE ILE A . n 
A 1 105 GLY 105 99  99  GLY GLY A . n 
A 1 106 CYS 106 100 100 CYS CYS A . n 
A 1 107 LEU 107 101 101 LEU LEU A . n 
A 1 108 PRO 108 102 102 PRO PRO A . n 
A 1 109 TYR 109 103 103 TYR TYR A . n 
A 1 110 THR 110 104 104 THR THR A . n 
A 1 111 ILE 111 105 105 ILE ILE A . n 
A 1 112 PRO 112 106 106 PRO PRO A . n 
A 1 113 PRO 113 107 107 PRO PRO A . n 
A 1 114 CYS 114 108 108 CYS CYS A . n 
A 1 115 GLU 115 109 109 GLU GLU A . n 
A 1 116 HIS 116 110 110 HIS HIS A . n 
A 1 117 HIS 117 111 111 HIS HIS A . n 
A 1 118 VAL 118 112 112 VAL VAL A . n 
A 1 119 ASN 119 113 113 ASN ASN A . n 
A 1 120 GLY 120 114 114 GLY GLY A . n 
A 1 121 ALA 121 115 115 ALA ALA A . n 
A 1 122 ARG 122 116 116 ARG ARG A . n 
A 1 123 PRO 123 117 117 PRO PRO A . n 
A 1 124 PRO 124 118 118 PRO PRO A . n 
A 1 125 CYS 125 119 119 CYS CYS A . n 
A 1 126 THR 126 120 120 THR THR A . n 
A 1 127 GLY 127 121 121 GLY GLY A . n 
A 1 128 GLU 128 122 122 GLU GLU A . n 
A 1 129 GLY 129 123 123 GLY GLY A . n 
A 1 130 ASP 130 124 124 ASP ASP A . n 
A 1 131 THR 131 125 125 THR THR A . n 
A 1 132 PRO 132 126 126 PRO PRO A . n 
A 1 133 LYS 133 127 127 LYS LYS A . n 
A 1 134 CYS 134 128 128 CYS CYS A . n 
A 1 135 ASN 135 129 129 ASN ASN A . n 
A 1 136 LYS 136 130 130 LYS LYS A . n 
A 1 137 MET 137 131 131 MET MET A . n 
A 1 138 CYS 138 132 132 CYS CYS A . n 
A 1 139 GLU 139 133 133 GLU GLU A . n 
A 1 140 ALA 140 134 134 ALA ALA A . n 
A 1 141 GLY 141 135 135 GLY GLY A . n 
A 1 142 TYR 142 136 136 TYR TYR A . n 
A 1 143 SER 143 137 137 SER SER A . n 
A 1 144 THR 144 138 138 THR THR A . n 
A 1 145 SER 145 139 139 SER SER A . n 
A 1 146 TYR 146 140 140 TYR TYR A . n 
A 1 147 LYS 147 141 141 LYS LYS A . n 
A 1 148 GLU 148 142 142 GLU GLU A . n 
A 1 149 ASP 149 143 143 ASP ASP A . n 
A 1 150 LYS 150 144 144 LYS LYS A . n 
A 1 151 HIS 151 145 145 HIS HIS A . n 
A 1 152 TYR 152 146 146 TYR TYR A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 TYR 154 148 148 TYR TYR A . n 
A 1 155 THR 155 149 149 THR THR A . n 
A 1 156 SER 156 150 150 SER SER A . n 
A 1 157 TYR 157 151 151 TYR TYR A . n 
A 1 158 SER 158 152 152 SER SER A . n 
A 1 159 VAL 159 153 153 VAL VAL A . n 
A 1 160 SER 160 154 154 SER SER A . n 
A 1 161 ASP 161 155 155 ASP ASP A . n 
A 1 162 SER 162 156 156 SER SER A . n 
A 1 163 GLU 163 157 157 GLU GLU A . n 
A 1 164 LYS 164 158 158 LYS LYS A . n 
A 1 165 GLU 165 159 159 GLU GLU A . n 
A 1 166 ILE 166 160 160 ILE ILE A . n 
A 1 167 MET 167 161 161 MET MET A . n 
A 1 168 ALA 168 162 162 ALA ALA A . n 
A 1 169 GLU 169 163 163 GLU GLU A . n 
A 1 170 ILE 170 164 164 ILE ILE A . n 
A 1 171 TYR 171 165 165 TYR TYR A . n 
A 1 172 LYS 172 166 166 LYS LYS A . n 
A 1 173 ASN 173 167 167 ASN ASN A . n 
A 1 174 GLY 174 168 168 GLY GLY A . n 
A 1 175 PRO 175 169 169 PRO PRO A . n 
A 1 176 VAL 176 170 170 VAL VAL A . n 
A 1 177 GLU 177 171 171 GLU GLU A . n 
A 1 178 GLY 178 172 172 GLY GLY A . n 
A 1 179 ALA 179 173 173 ALA ALA A . n 
A 1 180 PHE 180 174 174 PHE PHE A . n 
A 1 181 THR 181 175 175 THR THR A . n 
A 1 182 VAL 182 176 176 VAL VAL A . n 
A 1 183 PHE 183 177 177 PHE PHE A . n 
A 1 184 SER 184 178 178 SER SER A . n 
A 1 185 ASP 185 179 179 ASP ASP A . n 
A 1 186 PHE 186 180 180 PHE PHE A . n 
A 1 187 LEU 187 181 181 LEU LEU A . n 
A 1 188 THR 188 182 182 THR THR A . n 
A 1 189 TYR 189 183 183 TYR TYR A . n 
A 1 190 LYS 190 184 184 LYS LYS A . n 
A 1 191 SER 191 185 185 SER SER A . n 
A 1 192 GLY 192 186 186 GLY GLY A . n 
A 1 193 VAL 193 187 187 VAL VAL A . n 
A 1 194 TYR 194 188 188 TYR TYR A . n 
A 1 195 LYS 195 189 189 LYS LYS A . n 
A 1 196 HIS 196 190 190 HIS HIS A . n 
A 1 197 GLU 197 191 191 GLU GLU A . n 
A 1 198 ALA 198 192 192 ALA ALA A . n 
A 1 199 GLY 199 193 193 GLY GLY A . n 
A 1 200 ASP 200 194 194 ASP ASP A . n 
A 1 201 VAL 201 195 195 VAL VAL A . n 
A 1 202 MET 202 196 196 MET MET A . n 
A 1 203 GLY 203 197 197 GLY GLY A . n 
A 1 204 GLY 204 198 198 GLY GLY A . n 
A 1 205 HIS 205 199 199 HIS HIS A . n 
A 1 206 ALA 206 200 200 ALA ALA A . n 
A 1 207 ILE 207 201 201 ILE ILE A . n 
A 1 208 ARG 208 202 202 ARG ARG A . n 
A 1 209 ILE 209 203 203 ILE ILE A . n 
A 1 210 LEU 210 204 204 LEU LEU A . n 
A 1 211 GLY 211 205 205 GLY GLY A . n 
A 1 212 TRP 212 206 206 TRP TRP A . n 
A 1 213 GLY 213 207 207 GLY GLY A . n 
A 1 214 ILE 214 208 208 ILE ILE A . n 
A 1 215 GLU 215 209 209 GLU GLU A . n 
A 1 216 ASN 216 210 210 ASN ASN A . n 
A 1 217 GLY 217 211 211 GLY GLY A . n 
A 1 218 VAL 218 212 212 VAL VAL A . n 
A 1 219 PRO 219 213 213 PRO PRO A . n 
A 1 220 TYR 220 214 214 TYR TYR A . n 
A 1 221 TRP 221 215 215 TRP TRP A . n 
A 1 222 LEU 222 216 216 LEU LEU A . n 
A 1 223 VAL 223 217 217 VAL VAL A . n 
A 1 224 ALA 224 218 218 ALA ALA A . n 
A 1 225 ASN 225 219 219 ASN ASN A . n 
A 1 226 SER 226 220 220 SER SER A . n 
A 1 227 TRP 227 221 221 TRP TRP A . n 
A 1 228 ASN 228 222 222 ASN ASN A . n 
A 1 229 ALA 229 223 223 ALA ALA A . n 
A 1 230 ASP 230 224 224 ASP ASP A . n 
A 1 231 TRP 231 225 225 TRP TRP A . n 
A 1 232 GLY 232 226 226 GLY GLY A . n 
A 1 233 ASP 233 227 227 ASP ASP A . n 
A 1 234 ASN 234 228 228 ASN ASN A . n 
A 1 235 GLY 235 229 229 GLY GLY A . n 
A 1 236 PHE 236 230 230 PHE PHE A . n 
A 1 237 PHE 237 231 231 PHE PHE A . n 
A 1 238 LYS 238 232 232 LYS LYS A . n 
A 1 239 ILE 239 233 233 ILE ILE A . n 
A 1 240 LEU 240 234 234 LEU LEU A . n 
A 1 241 ARG 241 235 235 ARG ARG A . n 
A 1 242 GLY 242 236 236 GLY GLY A . n 
A 1 243 GLU 243 237 237 GLU GLU A . n 
A 1 244 ASN 244 238 238 ASN ASN A . n 
A 1 245 HIS 245 239 239 HIS HIS A . n 
A 1 246 CYS 246 240 240 CYS CYS A . n 
A 1 247 GLY 247 241 241 GLY GLY A . n 
A 1 248 ILE 248 242 242 ILE ILE A . n 
A 1 249 GLU 249 243 243 GLU GLU A . n 
A 1 250 SER 250 244 244 SER SER A . n 
A 1 251 GLU 251 245 245 GLU GLU A . n 
A 1 252 ILE 252 246 246 ILE ILE A . n 
A 1 253 VAL 253 247 247 VAL VAL A . n 
A 1 254 ALA 254 248 248 ALA ALA A . n 
A 1 255 GLY 255 249 249 GLY GLY A . n 
A 1 256 ILE 256 250 250 ILE ILE A . n 
A 1 257 PRO 257 251 251 PRO PRO A . n 
A 1 258 ARG 258 252 252 ARG ARG A . n 
A 1 259 THR 259 253 253 THR THR A . n 
A 1 260 GLN 260 254 ?   ?   ?   A . n 
B 1 1   PHE 1   -5  ?   ?   ?   B . n 
B 1 2   SER 2   -4  ?   ?   ?   B . n 
B 1 3   GLU 3   -3  ?   ?   ?   B . n 
B 1 4   ASP 4   -2  ?   ?   ?   B . n 
B 1 5   ILE 5   -1  ?   ?   ?   B . n 
B 1 6   ASN 6   0   ?   ?   ?   B . n 
B 1 7   LEU 7   1   1   LEU LEU B . n 
B 1 8   PRO 8   2   2   PRO PRO B . n 
B 1 9   GLU 9   3   3   GLU GLU B . n 
B 1 10  SER 10  4   4   SER SER B . n 
B 1 11  PHE 11  5   5   PHE PHE B . n 
B 1 12  ASP 12  6   6   ASP ASP B . n 
B 1 13  ALA 13  7   7   ALA ALA B . n 
B 1 14  ARG 14  8   8   ARG ARG B . n 
B 1 15  GLU 15  9   9   GLU GLU B . n 
B 1 16  GLN 16  10  10  GLN GLN B . n 
B 1 17  TRP 17  11  11  TRP TRP B . n 
B 1 18  SER 18  12  12  SER SER B . n 
B 1 19  ASN 19  13  13  ASN ASN B . n 
B 1 20  CYS 20  14  14  CYS CYS B . n 
B 1 21  PRO 21  15  15  PRO PRO B . n 
B 1 22  THR 22  16  16  THR THR B . n 
B 1 23  ILE 23  17  17  ILE ILE B . n 
B 1 24  ALA 24  18  18  ALA ALA B . n 
B 1 25  GLN 25  19  19  GLN GLN B . n 
B 1 26  ILE 26  20  20  ILE ILE B . n 
B 1 27  ARG 27  21  21  ARG ARG B . n 
B 1 28  ASP 28  22  22  ASP ASP B . n 
B 1 29  GLN 29  23  23  GLN GLN B . n 
B 1 30  GLY 30  24  24  GLY GLY B . n 
B 1 31  SER 31  25  25  SER SER B . n 
B 1 32  CYS 32  26  26  CYS CYS B . n 
B 1 33  GLY 33  27  27  GLY GLY B . n 
B 1 34  SER 34  28  28  SER SER B . n 
B 1 35  CYS 35  29  29  CYS CYS B . n 
B 1 36  TRP 36  30  30  TRP TRP B . n 
B 1 37  ALA 37  31  31  ALA ALA B . n 
B 1 38  PHE 38  32  32  PHE PHE B . n 
B 1 39  GLY 39  33  33  GLY GLY B . n 
B 1 40  ALA 40  34  34  ALA ALA B . n 
B 1 41  VAL 41  35  35  VAL VAL B . n 
B 1 42  GLU 42  36  36  GLU GLU B . n 
B 1 43  ALA 43  37  37  ALA ALA B . n 
B 1 44  MET 44  38  38  MET MET B . n 
B 1 45  SER 45  39  39  SER SER B . n 
B 1 46  ASP 46  40  40  ASP ASP B . n 
B 1 47  ARG 47  41  41  ARG ARG B . n 
B 1 48  ILE 48  42  42  ILE ILE B . n 
B 1 49  CYS 49  43  43  CYS CYS B . n 
B 1 50  ILE 50  44  44  ILE ILE B . n 
B 1 51  HIS 51  45  45  HIS HIS B . n 
B 1 52  THR 52  46  46  THR THR B . n 
B 1 53  ASN 53  47  47  ASN ASN B . n 
B 1 54  GLY 54  48  48  GLY GLY B . n 
B 1 55  ARG 55  49  49  ARG ARG B . n 
B 1 56  VAL 56  50  50  VAL VAL B . n 
B 1 57  ASN 57  51  51  ASN ASN B . n 
B 1 58  VAL 58  52  52  VAL VAL B . n 
B 1 59  GLU 59  53  53  GLU GLU B . n 
B 1 60  VAL 60  54  54  VAL VAL B . n 
B 1 61  SER 61  55  55  SER SER B . n 
B 1 62  ALA 62  56  56  ALA ALA B . n 
B 1 63  GLU 63  57  57  GLU GLU B . n 
B 1 64  ASP 64  58  58  ASP ASP B . n 
B 1 65  LEU 65  59  59  LEU LEU B . n 
B 1 66  LEU 66  60  60  LEU LEU B . n 
B 1 67  THR 67  61  61  THR THR B . n 
B 1 68  CYS 68  62  62  CYS CYS B . n 
B 1 69  CYS 69  63  63  CYS CYS B . n 
B 1 70  GLY 70  64  64  GLY GLY B . n 
B 1 71  ILE 71  65  65  ILE ILE B . n 
B 1 72  GLN 72  66  66  GLN GLN B . n 
B 1 73  CYS 73  67  67  CYS CYS B . n 
B 1 74  GLY 74  68  68  GLY GLY B . n 
B 1 75  ASP 75  69  69  ASP ASP B . n 
B 1 76  GLY 76  70  70  GLY GLY B . n 
B 1 77  CYS 77  71  71  CYS CYS B . n 
B 1 78  ASN 78  72  72  ASN ASN B . n 
B 1 79  GLY 79  73  73  GLY GLY B . n 
B 1 80  GLY 80  74  74  GLY GLY B . n 
B 1 81  TYR 81  75  75  TYR TYR B . n 
B 1 82  PRO 82  76  76  PRO PRO B . n 
B 1 83  SER 83  77  77  SER SER B . n 
B 1 84  GLY 84  78  78  GLY GLY B . n 
B 1 85  ALA 85  79  79  ALA ALA B . n 
B 1 86  TRP 86  80  80  TRP TRP B . n 
B 1 87  ASN 87  81  81  ASN ASN B . n 
B 1 88  PHE 88  82  82  PHE PHE B . n 
B 1 89  TRP 89  83  83  TRP TRP B . n 
B 1 90  THR 90  84  84  THR THR B . n 
B 1 91  ARG 91  85  85  ARG ARG B . n 
B 1 92  LYS 92  86  86  LYS LYS B . n 
B 1 93  GLY 93  87  87  GLY GLY B . n 
B 1 94  LEU 94  88  88  LEU LEU B . n 
B 1 95  VAL 95  89  89  VAL VAL B . n 
B 1 96  SER 96  90  90  SER SER B . n 
B 1 97  GLY 97  91  91  GLY GLY B . n 
B 1 98  GLY 98  92  92  GLY GLY B . n 
B 1 99  VAL 99  93  93  VAL VAL B . n 
B 1 100 TYR 100 94  94  TYR TYR B . n 
B 1 101 ASN 101 95  95  ASN ASN B . n 
B 1 102 SER 102 96  96  SER SER B . n 
B 1 103 HIS 103 97  97  HIS HIS B . n 
B 1 104 ILE 104 98  98  ILE ILE B . n 
B 1 105 GLY 105 99  99  GLY GLY B . n 
B 1 106 CYS 106 100 100 CYS CYS B . n 
B 1 107 LEU 107 101 101 LEU LEU B . n 
B 1 108 PRO 108 102 102 PRO PRO B . n 
B 1 109 TYR 109 103 103 TYR TYR B . n 
B 1 110 THR 110 104 104 THR THR B . n 
B 1 111 ILE 111 105 105 ILE ILE B . n 
B 1 112 PRO 112 106 106 PRO PRO B . n 
B 1 113 PRO 113 107 107 PRO PRO B . n 
B 1 114 CYS 114 108 108 CYS CYS B . n 
B 1 115 GLU 115 109 109 GLU GLU B . n 
B 1 116 HIS 116 110 110 HIS HIS B . n 
B 1 117 HIS 117 111 111 HIS HIS B . n 
B 1 118 VAL 118 112 112 VAL VAL B . n 
B 1 119 ASN 119 113 113 ASN ASN B . n 
B 1 120 GLY 120 114 114 GLY GLY B . n 
B 1 121 ALA 121 115 115 ALA ALA B . n 
B 1 122 ARG 122 116 116 ARG ARG B . n 
B 1 123 PRO 123 117 117 PRO PRO B . n 
B 1 124 PRO 124 118 118 PRO PRO B . n 
B 1 125 CYS 125 119 119 CYS CYS B . n 
B 1 126 THR 126 120 120 THR THR B . n 
B 1 127 GLY 127 121 121 GLY GLY B . n 
B 1 128 GLU 128 122 122 GLU GLU B . n 
B 1 129 GLY 129 123 123 GLY GLY B . n 
B 1 130 ASP 130 124 124 ASP ASP B . n 
B 1 131 THR 131 125 125 THR THR B . n 
B 1 132 PRO 132 126 126 PRO PRO B . n 
B 1 133 LYS 133 127 127 LYS LYS B . n 
B 1 134 CYS 134 128 128 CYS CYS B . n 
B 1 135 ASN 135 129 129 ASN ASN B . n 
B 1 136 LYS 136 130 130 LYS LYS B . n 
B 1 137 MET 137 131 131 MET MET B . n 
B 1 138 CYS 138 132 132 CYS CYS B . n 
B 1 139 GLU 139 133 133 GLU GLU B . n 
B 1 140 ALA 140 134 134 ALA ALA B . n 
B 1 141 GLY 141 135 135 GLY GLY B . n 
B 1 142 TYR 142 136 136 TYR TYR B . n 
B 1 143 SER 143 137 137 SER SER B . n 
B 1 144 THR 144 138 138 THR THR B . n 
B 1 145 SER 145 139 139 SER SER B . n 
B 1 146 TYR 146 140 140 TYR TYR B . n 
B 1 147 LYS 147 141 141 LYS LYS B . n 
B 1 148 GLU 148 142 142 GLU GLU B . n 
B 1 149 ASP 149 143 143 ASP ASP B . n 
B 1 150 LYS 150 144 144 LYS LYS B . n 
B 1 151 HIS 151 145 145 HIS HIS B . n 
B 1 152 TYR 152 146 146 TYR TYR B . n 
B 1 153 GLY 153 147 147 GLY GLY B . n 
B 1 154 TYR 154 148 148 TYR TYR B . n 
B 1 155 THR 155 149 149 THR THR B . n 
B 1 156 SER 156 150 150 SER SER B . n 
B 1 157 TYR 157 151 151 TYR TYR B . n 
B 1 158 SER 158 152 152 SER SER B . n 
B 1 159 VAL 159 153 153 VAL VAL B . n 
B 1 160 SER 160 154 154 SER SER B . n 
B 1 161 ASP 161 155 155 ASP ASP B . n 
B 1 162 SER 162 156 156 SER SER B . n 
B 1 163 GLU 163 157 157 GLU GLU B . n 
B 1 164 LYS 164 158 158 LYS LYS B . n 
B 1 165 GLU 165 159 159 GLU GLU B . n 
B 1 166 ILE 166 160 160 ILE ILE B . n 
B 1 167 MET 167 161 161 MET MET B . n 
B 1 168 ALA 168 162 162 ALA ALA B . n 
B 1 169 GLU 169 163 163 GLU GLU B . n 
B 1 170 ILE 170 164 164 ILE ILE B . n 
B 1 171 TYR 171 165 165 TYR TYR B . n 
B 1 172 LYS 172 166 166 LYS LYS B . n 
B 1 173 ASN 173 167 167 ASN ASN B . n 
B 1 174 GLY 174 168 168 GLY GLY B . n 
B 1 175 PRO 175 169 169 PRO PRO B . n 
B 1 176 VAL 176 170 170 VAL VAL B . n 
B 1 177 GLU 177 171 171 GLU GLU B . n 
B 1 178 GLY 178 172 172 GLY GLY B . n 
B 1 179 ALA 179 173 173 ALA ALA B . n 
B 1 180 PHE 180 174 174 PHE PHE B . n 
B 1 181 THR 181 175 175 THR THR B . n 
B 1 182 VAL 182 176 176 VAL VAL B . n 
B 1 183 PHE 183 177 177 PHE PHE B . n 
B 1 184 SER 184 178 178 SER SER B . n 
B 1 185 ASP 185 179 179 ASP ASP B . n 
B 1 186 PHE 186 180 180 PHE PHE B . n 
B 1 187 LEU 187 181 181 LEU LEU B . n 
B 1 188 THR 188 182 182 THR THR B . n 
B 1 189 TYR 189 183 183 TYR TYR B . n 
B 1 190 LYS 190 184 184 LYS LYS B . n 
B 1 191 SER 191 185 185 SER SER B . n 
B 1 192 GLY 192 186 186 GLY GLY B . n 
B 1 193 VAL 193 187 187 VAL VAL B . n 
B 1 194 TYR 194 188 188 TYR TYR B . n 
B 1 195 LYS 195 189 189 LYS LYS B . n 
B 1 196 HIS 196 190 190 HIS HIS B . n 
B 1 197 GLU 197 191 191 GLU GLU B . n 
B 1 198 ALA 198 192 192 ALA ALA B . n 
B 1 199 GLY 199 193 193 GLY GLY B . n 
B 1 200 ASP 200 194 194 ASP ASP B . n 
B 1 201 VAL 201 195 195 VAL VAL B . n 
B 1 202 MET 202 196 196 MET MET B . n 
B 1 203 GLY 203 197 197 GLY GLY B . n 
B 1 204 GLY 204 198 198 GLY GLY B . n 
B 1 205 HIS 205 199 199 HIS HIS B . n 
B 1 206 ALA 206 200 200 ALA ALA B . n 
B 1 207 ILE 207 201 201 ILE ILE B . n 
B 1 208 ARG 208 202 202 ARG ARG B . n 
B 1 209 ILE 209 203 203 ILE ILE B . n 
B 1 210 LEU 210 204 204 LEU LEU B . n 
B 1 211 GLY 211 205 205 GLY GLY B . n 
B 1 212 TRP 212 206 206 TRP TRP B . n 
B 1 213 GLY 213 207 207 GLY GLY B . n 
B 1 214 ILE 214 208 208 ILE ILE B . n 
B 1 215 GLU 215 209 209 GLU GLU B . n 
B 1 216 ASN 216 210 210 ASN ASN B . n 
B 1 217 GLY 217 211 211 GLY GLY B . n 
B 1 218 VAL 218 212 212 VAL VAL B . n 
B 1 219 PRO 219 213 213 PRO PRO B . n 
B 1 220 TYR 220 214 214 TYR TYR B . n 
B 1 221 TRP 221 215 215 TRP TRP B . n 
B 1 222 LEU 222 216 216 LEU LEU B . n 
B 1 223 VAL 223 217 217 VAL VAL B . n 
B 1 224 ALA 224 218 218 ALA ALA B . n 
B 1 225 ASN 225 219 219 ASN ASN B . n 
B 1 226 SER 226 220 220 SER SER B . n 
B 1 227 TRP 227 221 221 TRP TRP B . n 
B 1 228 ASN 228 222 222 ASN ASN B . n 
B 1 229 ALA 229 223 223 ALA ALA B . n 
B 1 230 ASP 230 224 224 ASP ASP B . n 
B 1 231 TRP 231 225 225 TRP TRP B . n 
B 1 232 GLY 232 226 226 GLY GLY B . n 
B 1 233 ASP 233 227 227 ASP ASP B . n 
B 1 234 ASN 234 228 228 ASN ASN B . n 
B 1 235 GLY 235 229 229 GLY GLY B . n 
B 1 236 PHE 236 230 230 PHE PHE B . n 
B 1 237 PHE 237 231 231 PHE PHE B . n 
B 1 238 LYS 238 232 232 LYS LYS B . n 
B 1 239 ILE 239 233 233 ILE ILE B . n 
B 1 240 LEU 240 234 234 LEU LEU B . n 
B 1 241 ARG 241 235 235 ARG ARG B . n 
B 1 242 GLY 242 236 236 GLY GLY B . n 
B 1 243 GLU 243 237 237 GLU GLU B . n 
B 1 244 ASN 244 238 238 ASN ASN B . n 
B 1 245 HIS 245 239 239 HIS HIS B . n 
B 1 246 CYS 246 240 240 CYS CYS B . n 
B 1 247 GLY 247 241 241 GLY GLY B . n 
B 1 248 ILE 248 242 242 ILE ILE B . n 
B 1 249 GLU 249 243 243 GLU GLU B . n 
B 1 250 SER 250 244 244 SER SER B . n 
B 1 251 GLU 251 245 245 GLU GLU B . n 
B 1 252 ILE 252 246 246 ILE ILE B . n 
B 1 253 VAL 253 247 247 VAL VAL B . n 
B 1 254 ALA 254 248 248 ALA ALA B . n 
B 1 255 GLY 255 249 249 GLY GLY B . n 
B 1 256 ILE 256 250 250 ILE ILE B . n 
B 1 257 PRO 257 251 251 PRO PRO B . n 
B 1 258 ARG 258 252 252 ARG ARG B . n 
B 1 259 THR 259 253 253 THR THR B . n 
B 1 260 GLN 260 254 ?   ?   ?   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 HOH 1  601 601 HOH HOH A . 
C 2 HOH 2  602 602 HOH HOH A . 
C 2 HOH 3  603 603 HOH HOH A . 
C 2 HOH 4  604 604 HOH HOH A . 
C 2 HOH 5  605 605 HOH HOH A . 
C 2 HOH 6  606 606 HOH HOH A . 
C 2 HOH 7  607 607 HOH HOH A . 
C 2 HOH 8  608 608 HOH HOH A . 
C 2 HOH 9  610 610 HOH HOH A . 
C 2 HOH 10 611 611 HOH HOH A . 
C 2 HOH 11 612 612 HOH HOH A . 
C 2 HOH 12 614 614 HOH HOH A . 
C 2 HOH 13 615 615 HOH HOH A . 
C 2 HOH 14 616 616 HOH HOH A . 
C 2 HOH 15 617 617 HOH HOH A . 
C 2 HOH 16 618 618 HOH HOH A . 
C 2 HOH 17 619 619 HOH HOH A . 
C 2 HOH 18 620 620 HOH HOH A . 
C 2 HOH 19 624 624 HOH HOH A . 
C 2 HOH 20 626 626 HOH HOH A . 
C 2 HOH 21 627 627 HOH HOH A . 
C 2 HOH 22 628 628 HOH HOH A . 
C 2 HOH 23 629 629 HOH HOH A . 
C 2 HOH 24 630 630 HOH HOH A . 
C 2 HOH 25 632 632 HOH HOH A . 
C 2 HOH 26 636 636 HOH HOH A . 
C 2 HOH 27 637 637 HOH HOH A . 
C 2 HOH 28 638 638 HOH HOH A . 
C 2 HOH 29 639 639 HOH HOH A . 
C 2 HOH 30 642 642 HOH HOH A . 
C 2 HOH 31 643 643 HOH HOH A . 
C 2 HOH 32 644 644 HOH HOH A . 
C 2 HOH 33 645 645 HOH HOH A . 
C 2 HOH 34 646 646 HOH HOH A . 
C 2 HOH 35 649 649 HOH HOH A . 
C 2 HOH 36 667 667 HOH HOH A . 
C 2 HOH 37 675 675 HOH HOH A . 
C 2 HOH 38 681 681 HOH HOH A . 
C 2 HOH 39 685 685 HOH HOH A . 
C 2 HOH 40 686 686 HOH HOH A . 
C 2 HOH 41 687 687 HOH HOH A . 
C 2 HOH 42 690 690 HOH HOH A . 
C 2 HOH 43 691 691 HOH HOH A . 
C 2 HOH 44 692 692 HOH HOH A . 
C 2 HOH 45 693 693 HOH HOH A . 
C 2 HOH 46 694 694 HOH HOH A . 
C 2 HOH 47 695 695 HOH HOH A . 
C 2 HOH 48 696 696 HOH HOH A . 
C 2 HOH 49 698 698 HOH HOH A . 
C 2 HOH 50 699 699 HOH HOH A . 
C 2 HOH 51 701 701 HOH HOH A . 
C 2 HOH 52 702 702 HOH HOH A . 
C 2 HOH 53 703 703 HOH HOH A . 
C 2 HOH 54 704 704 HOH HOH A . 
C 2 HOH 55 705 705 HOH HOH A . 
C 2 HOH 56 706 706 HOH HOH A . 
C 2 HOH 57 707 707 HOH HOH A . 
C 2 HOH 58 708 708 HOH HOH A . 
C 2 HOH 59 709 709 HOH HOH A . 
C 2 HOH 60 710 710 HOH HOH A . 
C 2 HOH 61 712 712 HOH HOH A . 
C 2 HOH 62 714 714 HOH HOH A . 
C 2 HOH 63 731 731 HOH HOH A . 
C 2 HOH 64 736 736 HOH HOH A . 
C 2 HOH 65 737 737 HOH HOH A . 
C 2 HOH 66 738 738 HOH HOH A . 
C 2 HOH 67 739 739 HOH HOH A . 
C 2 HOH 68 740 740 HOH HOH A . 
C 2 HOH 69 741 741 HOH HOH A . 
C 2 HOH 70 742 742 HOH HOH A . 
C 2 HOH 71 743 743 HOH HOH A . 
C 2 HOH 72 744 744 HOH HOH A . 
C 2 HOH 73 745 745 HOH HOH A . 
C 2 HOH 74 746 746 HOH HOH A . 
C 2 HOH 75 747 747 HOH HOH A . 
C 2 HOH 76 752 752 HOH HOH A . 
C 2 HOH 77 754 754 HOH HOH A . 
C 2 HOH 78 756 756 HOH HOH A . 
C 2 HOH 79 761 761 HOH HOH A . 
C 2 HOH 80 762 762 HOH HOH A . 
C 2 HOH 81 763 763 HOH HOH A . 
C 2 HOH 82 764 764 HOH HOH A . 
C 2 HOH 83 767 767 HOH HOH A . 
C 2 HOH 84 770 770 HOH HOH A . 
C 2 HOH 85 771 771 HOH HOH A . 
C 2 HOH 86 772 772 HOH HOH A . 
C 2 HOH 87 774 774 HOH HOH A . 
C 2 HOH 88 776 776 HOH HOH A . 
C 2 HOH 89 778 778 HOH HOH A . 
C 2 HOH 90 780 780 HOH HOH A . 
C 2 HOH 91 781 781 HOH HOH A . 
C 2 HOH 92 782 782 HOH HOH A . 
C 2 HOH 93 784 784 HOH HOH A . 
C 2 HOH 94 785 785 HOH HOH A . 
C 2 HOH 95 786 786 HOH HOH A . 
C 2 HOH 96 787 787 HOH HOH A . 
D 2 HOH 1  609 609 HOH HOH B . 
D 2 HOH 2  613 613 HOH HOH B . 
D 2 HOH 3  621 621 HOH HOH B . 
D 2 HOH 4  622 622 HOH HOH B . 
D 2 HOH 5  623 623 HOH HOH B . 
D 2 HOH 6  625 625 HOH HOH B . 
D 2 HOH 7  631 631 HOH HOH B . 
D 2 HOH 8  633 633 HOH HOH B . 
D 2 HOH 9  634 634 HOH HOH B . 
D 2 HOH 10 635 635 HOH HOH B . 
D 2 HOH 11 640 640 HOH HOH B . 
D 2 HOH 12 641 641 HOH HOH B . 
D 2 HOH 13 647 647 HOH HOH B . 
D 2 HOH 14 648 648 HOH HOH B . 
D 2 HOH 15 650 650 HOH HOH B . 
D 2 HOH 16 651 651 HOH HOH B . 
D 2 HOH 17 652 652 HOH HOH B . 
D 2 HOH 18 653 653 HOH HOH B . 
D 2 HOH 19 654 654 HOH HOH B . 
D 2 HOH 20 655 655 HOH HOH B . 
D 2 HOH 21 656 656 HOH HOH B . 
D 2 HOH 22 657 657 HOH HOH B . 
D 2 HOH 23 658 658 HOH HOH B . 
D 2 HOH 24 659 659 HOH HOH B . 
D 2 HOH 25 660 660 HOH HOH B . 
D 2 HOH 26 661 661 HOH HOH B . 
D 2 HOH 27 662 662 HOH HOH B . 
D 2 HOH 28 663 663 HOH HOH B . 
D 2 HOH 29 664 664 HOH HOH B . 
D 2 HOH 30 665 665 HOH HOH B . 
D 2 HOH 31 666 666 HOH HOH B . 
D 2 HOH 32 668 668 HOH HOH B . 
D 2 HOH 33 669 669 HOH HOH B . 
D 2 HOH 34 670 670 HOH HOH B . 
D 2 HOH 35 671 671 HOH HOH B . 
D 2 HOH 36 672 672 HOH HOH B . 
D 2 HOH 37 673 673 HOH HOH B . 
D 2 HOH 38 674 674 HOH HOH B . 
D 2 HOH 39 676 676 HOH HOH B . 
D 2 HOH 40 677 677 HOH HOH B . 
D 2 HOH 41 678 678 HOH HOH B . 
D 2 HOH 42 679 679 HOH HOH B . 
D 2 HOH 43 680 680 HOH HOH B . 
D 2 HOH 44 682 682 HOH HOH B . 
D 2 HOH 45 683 683 HOH HOH B . 
D 2 HOH 46 684 684 HOH HOH B . 
D 2 HOH 47 688 688 HOH HOH B . 
D 2 HOH 48 689 689 HOH HOH B . 
D 2 HOH 49 697 697 HOH HOH B . 
D 2 HOH 50 700 700 HOH HOH B . 
D 2 HOH 51 711 711 HOH HOH B . 
D 2 HOH 52 713 713 HOH HOH B . 
D 2 HOH 53 715 715 HOH HOH B . 
D 2 HOH 54 716 716 HOH HOH B . 
D 2 HOH 55 717 717 HOH HOH B . 
D 2 HOH 56 718 718 HOH HOH B . 
D 2 HOH 57 719 719 HOH HOH B . 
D 2 HOH 58 720 720 HOH HOH B . 
D 2 HOH 59 721 721 HOH HOH B . 
D 2 HOH 60 722 722 HOH HOH B . 
D 2 HOH 61 723 723 HOH HOH B . 
D 2 HOH 62 724 724 HOH HOH B . 
D 2 HOH 63 725 725 HOH HOH B . 
D 2 HOH 64 726 726 HOH HOH B . 
D 2 HOH 65 727 727 HOH HOH B . 
D 2 HOH 66 728 728 HOH HOH B . 
D 2 HOH 67 729 729 HOH HOH B . 
D 2 HOH 68 730 730 HOH HOH B . 
D 2 HOH 69 732 732 HOH HOH B . 
D 2 HOH 70 733 733 HOH HOH B . 
D 2 HOH 71 734 734 HOH HOH B . 
D 2 HOH 72 748 748 HOH HOH B . 
D 2 HOH 73 749 749 HOH HOH B . 
D 2 HOH 74 750 750 HOH HOH B . 
D 2 HOH 75 751 751 HOH HOH B . 
D 2 HOH 76 753 753 HOH HOH B . 
D 2 HOH 77 755 755 HOH HOH B . 
D 2 HOH 78 757 757 HOH HOH B . 
D 2 HOH 79 758 758 HOH HOH B . 
D 2 HOH 80 759 759 HOH HOH B . 
D 2 HOH 81 760 760 HOH HOH B . 
D 2 HOH 82 765 765 HOH HOH B . 
D 2 HOH 83 766 766 HOH HOH B . 
D 2 HOH 84 768 768 HOH HOH B . 
D 2 HOH 85 769 769 HOH HOH B . 
D 2 HOH 86 773 773 HOH HOH B . 
D 2 HOH 87 775 775 HOH HOH B . 
D 2 HOH 88 777 777 HOH HOH B . 
D 2 HOH 89 779 779 HOH HOH B . 
D 2 HOH 90 783 783 HOH HOH B . 
D 2 HOH 91 788 788 HOH HOH B . 
D 2 HOH 92 789 789 HOH HOH B . 
D 2 HOH 93 790 790 HOH HOH B . 
D 2 HOH 94 791 791 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,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 1995-12-07 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SDMS   'data collection' .   ? 1 
X-PLOR 'model building'  3.0 ? 2 
X-PLOR refinement        3.0 ? 3 
SDMS   'data reduction'  .   ? 4 
X-PLOR phasing           3.0 ? 5 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
THERE IS A BIFURCATED SHEET IN EACH MOLECULE.  EACH IS
REPRESENTED BY TWO SHEETS WITH SOME STRANDS IN COMMON.
THUS STRANDS 4, 5, 6 OF SHEETS SA1 AND SA2 ARE IDENTICAL TO
STRANDS 2, 3, 4 OF SHEETS SA2 AND SB2 IN CHAINS A AND B,
RESPECTIVELY.
;
# 
_pdbx_entry_details.entry_id             1CPJ 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;THE V223A SUBSTITUTION WAS PRESENT IN THE PLASMID
SUPPLIED TO DR. J. S. MORT BY DR. SHU CHAN ALTHOUGH IT
IS NOT MENTIONED IN THE PAPER GIVING THE CDNA SEQUENCE.
IT IS POSSIBLE THAT THIS CHANGE, ALSO WITH RESPECT TO
THE ORIGINAL PROTEIN SEQUENCE FROM A PREPARATION OF
PURIFIED PROTEIN, COULD REPRESENT A POLYMORPHISM
BETWEEN THE STRAINS OF RAT THAT WERE USED IN EACH
CASE.  THE SUBSTITUTION IS NOT STRUCTURALLY IMPORTANT.
;
# 
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 LYS 127 ? ? CG  A LYS 127 ? ? 0.809 1.521 -0.712 0.027 N 
2 1 CD B GLU 122 ? ? OE2 B GLU 122 ? ? 1.336 1.252 0.084  0.011 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 CA  A LYS 127 ? ? CB A LYS 127 ? ? CG  A LYS 127 ? ? 148.45 113.40 35.05  2.20 N 
2 1 OE1 A GLU 142 ? ? CD A GLU 142 ? ? OE2 A GLU 142 ? ? 107.83 123.30 -15.47 1.20 N 
3 1 CG  A GLU 142 ? ? CD A GLU 142 ? ? OE2 A GLU 142 ? ? 133.24 118.30 14.94  2.00 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 TYR A 94  ? ? -34.97  129.33  
2  1 ASN A 95  ? ? 44.53   24.75   
3  1 ASP A 155 ? ? -59.84  75.89   
4  1 PRO A 169 ? ? -41.00  152.86  
5  1 SER A 178 ? ? -23.90  -53.34  
6  1 SER A 185 ? ? 179.91  168.71  
7  1 GLU A 191 ? ? -133.19 -45.66  
8  1 ASN A 210 ? ? 60.40   62.01   
9  1 SER A 220 ? ? -103.12 40.50   
10 1 ASN A 222 ? ? 62.14   -179.96 
11 1 LEU A 234 ? ? -36.49  130.58  
12 1 GLU A 237 ? ? -106.51 50.30   
13 1 ASN A 238 ? ? 38.41   26.99   
14 1 CYS B 14  ? ? -113.51 79.48   
15 1 ASN B 95  ? ? 59.85   19.74   
16 1 CYS B 100 ? ? -68.75  -71.57  
17 1 GLU B 122 ? ? -43.43  106.42  
18 1 LYS B 130 ? ? -85.67  37.60   
19 1 ASP B 155 ? ? -63.52  69.69   
20 1 ASN B 167 ? ? -140.88 -12.39  
21 1 PRO B 169 ? ? -40.38  153.86  
22 1 LYS B 184 ? ? -141.00 -40.26  
23 1 GLU B 191 ? ? -91.85  -96.79  
24 1 ASN B 222 ? ? 66.91   178.60  
25 1 LEU B 234 ? ? -45.50  157.20  
26 1 ASN B 238 ? ? 39.33   32.62   
27 1 ALA B 248 ? ? -165.58 -166.56 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER A 96 ? ? 11.99 
2 1 GLY B 91 ? ? 10.25 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1  1 PHE A 32  ? ? 0.078 'SIDE CHAIN' 
2  1 ARG A 85  ? ? 0.081 'SIDE CHAIN' 
3  1 TYR A 94  ? ? 0.097 'SIDE CHAIN' 
4  1 TYR A 103 ? ? 0.081 'SIDE CHAIN' 
5  1 TYR A 136 ? ? 0.105 'SIDE CHAIN' 
6  1 TYR A 140 ? ? 0.066 'SIDE CHAIN' 
7  1 ARG A 202 ? ? 0.105 'SIDE CHAIN' 
8  1 TYR A 214 ? ? 0.101 'SIDE CHAIN' 
9  1 TYR B 75  ? ? 0.081 'SIDE CHAIN' 
10 1 TYR B 151 ? ? 0.079 'SIDE CHAIN' 
11 1 TYR B 214 ? ? 0.075 'SIDE CHAIN' 
# 
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 0 A GLU 122 ? CB  ? A GLU 128 CB  
2  1 Y 0 A GLU 122 ? CG  ? A GLU 128 CG  
3  1 Y 0 A GLU 122 ? CD  ? A GLU 128 CD  
4  1 Y 0 A GLU 122 ? OE1 ? A GLU 128 OE1 
5  1 Y 0 A GLU 122 ? OE2 ? A GLU 128 OE2 
6  1 Y 0 A LYS 127 ? CG  ? A LYS 133 CG  
7  1 Y 0 A LYS 127 ? CD  ? A LYS 133 CD  
8  1 Y 0 A LYS 127 ? CE  ? A LYS 133 CE  
9  1 Y 0 A LYS 127 ? NZ  ? A LYS 133 NZ  
10 1 Y 0 A GLU 142 ? CG  ? A GLU 148 CG  
11 1 Y 0 A GLU 142 ? CD  ? A GLU 148 CD  
12 1 Y 0 A GLU 142 ? OE1 ? A GLU 148 OE1 
13 1 Y 0 A GLU 142 ? OE2 ? A GLU 148 OE2 
14 1 Y 0 A LYS 158 ? CG  ? A LYS 164 CG  
15 1 Y 0 A LYS 158 ? CD  ? A LYS 164 CD  
16 1 Y 0 A LYS 158 ? CE  ? A LYS 164 CE  
17 1 Y 0 A LYS 158 ? NZ  ? A LYS 164 NZ  
18 1 Y 0 B GLU 122 ? CB  ? B GLU 128 CB  
19 1 Y 0 B GLU 122 ? CG  ? B GLU 128 CG  
20 1 Y 0 B GLU 122 ? CD  ? B GLU 128 CD  
21 1 Y 0 B GLU 122 ? OE1 ? B GLU 128 OE1 
22 1 Y 0 B GLU 122 ? OE2 ? B GLU 128 OE2 
23 1 Y 0 B LYS 127 ? CG  ? B LYS 133 CG  
24 1 Y 0 B LYS 127 ? CD  ? B LYS 133 CD  
25 1 Y 0 B LYS 127 ? CE  ? B LYS 133 CE  
26 1 Y 0 B LYS 127 ? NZ  ? B LYS 133 NZ  
27 1 Y 0 B LYS 158 ? CG  ? B LYS 164 CG  
28 1 Y 0 B LYS 158 ? CD  ? B LYS 164 CD  
29 1 Y 0 B LYS 158 ? CE  ? B LYS 164 CE  
30 1 Y 0 B LYS 158 ? NZ  ? B LYS 164 NZ  
31 1 Y 0 B LYS 184 ? CG  ? B LYS 190 CG  
32 1 Y 0 B LYS 184 ? CD  ? B LYS 190 CD  
33 1 Y 0 B LYS 184 ? CE  ? B LYS 190 CE  
34 1 Y 0 B LYS 184 ? NZ  ? B LYS 190 NZ  
35 1 Y 0 B ASP 194 ? CG  ? B ASP 200 CG  
36 1 Y 0 B ASP 194 ? OD1 ? B ASP 200 OD1 
37 1 Y 0 B ASP 194 ? OD2 ? B ASP 200 OD2 
# 
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 PHE -5  ? A PHE 1   
2  1 Y 1 A SER -4  ? A SER 2   
3  1 Y 1 A GLU -3  ? A GLU 3   
4  1 Y 1 A ASP -2  ? A ASP 4   
5  1 Y 1 A ILE -1  ? A ILE 5   
6  1 Y 1 A ASN 0   ? A ASN 6   
7  1 Y 1 A GLN 254 ? A GLN 260 
8  1 Y 1 B PHE -5  ? B PHE 1   
9  1 Y 1 B SER -4  ? B SER 2   
10 1 Y 1 B GLU -3  ? B GLU 3   
11 1 Y 1 B ASP -2  ? B ASP 4   
12 1 Y 1 B ILE -1  ? B ILE 5   
13 1 Y 1 B ASN 0   ? B ASN 6   
14 1 Y 1 B GLN 254 ? B GLN 260 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
