data_9QBA
# 
_entry.id   9QBA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9QBA         pdb_00009qba 10.2210/pdb9qba/pdb 
WWPDB D_1292145993 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
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' 'Database references' 
2 2 'Structure model' 'Structure summary'   
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' audit_author    
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_audit_author.name'    
2 2 'Structure model' '_citation_author.name' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9QBA 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              knapp@phamchem.uni-frankfurt.de 
_pdbx_contact_author.name_first         Stefan 
_pdbx_contact_author.name_last          Knapp 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5995-6494 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kim, Y.'                              1 ? 
'Lucic, A.'                            2 ? 
'Knapp, S.'                            3 ? 
'Kraemer, A.'                          4 ? 
'Structural Genomics Consortium (SGC)' 5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Human TRIM21 PRYSPRY domain in complex with AL236' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kim, Y.'                              1 ? 
primary 'Lucic, A.'                            2 ? 
primary 'Knapp, S.'                            3 ? 
primary 'Kraemer, A.'                          4 ? 
primary 'Structural Genomics Consortium (SGC)' 5 ? 
# 
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 'E3 ubiquitin-protein ligase TRIM21'                                                         20332.859 1   
2.3.2.27 ? ? ? 
2 non-polymer syn '~{N}-(cyclohexylmethyl)-4-(4-fluoranyl-2-methylsulfanyl-phenyl)-2-methylsulfonyl-benzamide' 435.575   1   ? ? ? 
? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                               62.068    2   ? ? ? 
? 
4 water       nat water                                                                                        18.015    123 ? ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;52 kDa Ro protein,52 kDa ribonucleoprotein autoantigen Ro/SS-A,RING finger protein 81,Ro(SS-A),Sjoegren syndrome type A antigen,SS-A,Tripartite motif-containing protein 21
;
# 
_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       
;VHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRK
GHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFF
SPGFNDGGKNTAPLTLCPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRK
GHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFF
SPGFNDGGKNTAPLTLCPL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '~{N}-(cyclohexylmethyl)-4-(4-fluoranyl-2-methylsulfanyl-phenyl)-2-methylsulfonyl-benzamide' A1I41 
3 1,2-ETHANEDIOL                                                                               EDO   
4 water                                                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   HIS n 
1 3   ILE n 
1 4   THR n 
1 5   LEU n 
1 6   ASP n 
1 7   PRO n 
1 8   ASP n 
1 9   THR n 
1 10  ALA n 
1 11  ASN n 
1 12  PRO n 
1 13  TRP n 
1 14  LEU n 
1 15  ILE n 
1 16  LEU n 
1 17  SER n 
1 18  GLU n 
1 19  ASP n 
1 20  ARG n 
1 21  ARG n 
1 22  GLN n 
1 23  VAL n 
1 24  ARG n 
1 25  LEU n 
1 26  GLY n 
1 27  ASP n 
1 28  THR n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  ILE n 
1 33  PRO n 
1 34  GLY n 
1 35  ASN n 
1 36  GLU n 
1 37  GLU n 
1 38  ARG n 
1 39  PHE n 
1 40  ASP n 
1 41  SER n 
1 42  TYR n 
1 43  PRO n 
1 44  MET n 
1 45  VAL n 
1 46  LEU n 
1 47  GLY n 
1 48  ALA n 
1 49  GLN n 
1 50  HIS n 
1 51  PHE n 
1 52  HIS n 
1 53  SER n 
1 54  GLY n 
1 55  LYS n 
1 56  HIS n 
1 57  TYR n 
1 58  TRP n 
1 59  GLU n 
1 60  VAL n 
1 61  ASP n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  LYS n 
1 66  GLU n 
1 67  ALA n 
1 68  TRP n 
1 69  ASP n 
1 70  LEU n 
1 71  GLY n 
1 72  VAL n 
1 73  CYS n 
1 74  ARG n 
1 75  ASP n 
1 76  SER n 
1 77  VAL n 
1 78  ARG n 
1 79  ARG n 
1 80  LYS n 
1 81  GLY n 
1 82  HIS n 
1 83  PHE n 
1 84  LEU n 
1 85  LEU n 
1 86  SER n 
1 87  SER n 
1 88  LYS n 
1 89  SER n 
1 90  GLY n 
1 91  PHE n 
1 92  TRP n 
1 93  THR n 
1 94  ILE n 
1 95  TRP n 
1 96  LEU n 
1 97  TRP n 
1 98  ASN n 
1 99  LYS n 
1 100 GLN n 
1 101 LYS n 
1 102 TYR n 
1 103 GLU n 
1 104 ALA n 
1 105 GLY n 
1 106 THR n 
1 107 TYR n 
1 108 PRO n 
1 109 GLN n 
1 110 THR n 
1 111 PRO n 
1 112 LEU n 
1 113 HIS n 
1 114 LEU n 
1 115 GLN n 
1 116 VAL n 
1 117 PRO n 
1 118 PRO n 
1 119 CYS n 
1 120 GLN n 
1 121 VAL n 
1 122 GLY n 
1 123 ILE n 
1 124 PHE n 
1 125 LEU n 
1 126 ASP n 
1 127 TYR n 
1 128 GLU n 
1 129 ALA n 
1 130 GLY n 
1 131 MET n 
1 132 VAL n 
1 133 SER n 
1 134 PHE n 
1 135 TYR n 
1 136 ASN n 
1 137 ILE n 
1 138 THR n 
1 139 ASP n 
1 140 HIS n 
1 141 GLY n 
1 142 SER n 
1 143 LEU n 
1 144 ILE n 
1 145 TYR n 
1 146 SER n 
1 147 PHE n 
1 148 SER n 
1 149 GLU n 
1 150 CYS n 
1 151 ALA n 
1 152 PHE n 
1 153 THR n 
1 154 GLY n 
1 155 PRO n 
1 156 LEU n 
1 157 ARG n 
1 158 PRO n 
1 159 PHE n 
1 160 PHE n 
1 161 SER n 
1 162 PRO n 
1 163 GLY n 
1 164 PHE n 
1 165 ASN n 
1 166 ASP n 
1 167 GLY n 
1 168 GLY n 
1 169 LYS n 
1 170 ASN n 
1 171 THR n 
1 172 ALA n 
1 173 PRO n 
1 174 LEU n 
1 175 THR n 
1 176 LEU n 
1 177 CYS n 
1 178 PRO n 
1 179 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   179 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TRIM21, RNF81, RO52, SSA1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1I41 non-polymer         . '~{N}-(cyclohexylmethyl)-4-(4-fluoranyl-2-methylsulfanyl-phenyl)-2-methylsulfonyl-benzamide' ? 
'C22 H26 F N O3 S2' 435.575 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                                               
'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
GLN   'L-peptide linking' y GLUTAMINE                                                                                    ? 
'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                              ? 
'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                                      ? 
'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'     149.211 
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 
# 
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   VAL 1   287 287 VAL VAL A . n 
A 1 2   HIS 2   288 288 HIS HIS A . n 
A 1 3   ILE 3   289 289 ILE ILE A . n 
A 1 4   THR 4   290 290 THR THR A . n 
A 1 5   LEU 5   291 291 LEU LEU A . n 
A 1 6   ASP 6   292 292 ASP ASP A . n 
A 1 7   PRO 7   293 293 PRO PRO A . n 
A 1 8   ASP 8   294 294 ASP ASP A . n 
A 1 9   THR 9   295 295 THR THR A . n 
A 1 10  ALA 10  296 296 ALA ALA A . n 
A 1 11  ASN 11  297 297 ASN ASN A . n 
A 1 12  PRO 12  298 298 PRO PRO A . n 
A 1 13  TRP 13  299 299 TRP TRP A . n 
A 1 14  LEU 14  300 300 LEU LEU A . n 
A 1 15  ILE 15  301 301 ILE ILE A . n 
A 1 16  LEU 16  302 302 LEU LEU A . n 
A 1 17  SER 17  303 303 SER SER A . n 
A 1 18  GLU 18  304 304 GLU GLU A . n 
A 1 19  ASP 19  305 305 ASP ASP A . n 
A 1 20  ARG 20  306 306 ARG ARG A . n 
A 1 21  ARG 21  307 307 ARG ARG A . n 
A 1 22  GLN 22  308 308 GLN GLN A . n 
A 1 23  VAL 23  309 309 VAL VAL A . n 
A 1 24  ARG 24  310 310 ARG ARG A . n 
A 1 25  LEU 25  311 311 LEU LEU A . n 
A 1 26  GLY 26  312 312 GLY GLY A . n 
A 1 27  ASP 27  313 313 ASP ASP A . n 
A 1 28  THR 28  314 314 THR THR A . n 
A 1 29  GLN 29  315 315 GLN GLN A . n 
A 1 30  GLN 30  316 316 GLN GLN A . n 
A 1 31  SER 31  317 317 SER SER A . n 
A 1 32  ILE 32  318 318 ILE ILE A . n 
A 1 33  PRO 33  319 319 PRO PRO A . n 
A 1 34  GLY 34  320 320 GLY GLY A . n 
A 1 35  ASN 35  321 321 ASN ASN A . n 
A 1 36  GLU 36  322 322 GLU GLU A . n 
A 1 37  GLU 37  323 323 GLU GLU A . n 
A 1 38  ARG 38  324 324 ARG ARG A . n 
A 1 39  PHE 39  325 325 PHE PHE A . n 
A 1 40  ASP 40  326 326 ASP ASP A . n 
A 1 41  SER 41  327 327 SER SER A . n 
A 1 42  TYR 42  328 328 TYR TYR A . n 
A 1 43  PRO 43  329 329 PRO PRO A . n 
A 1 44  MET 44  330 330 MET MET A . n 
A 1 45  VAL 45  331 331 VAL VAL A . n 
A 1 46  LEU 46  332 332 LEU LEU A . n 
A 1 47  GLY 47  333 333 GLY GLY A . n 
A 1 48  ALA 48  334 334 ALA ALA A . n 
A 1 49  GLN 49  335 335 GLN GLN A . n 
A 1 50  HIS 50  336 336 HIS HIS A . n 
A 1 51  PHE 51  337 337 PHE PHE A . n 
A 1 52  HIS 52  338 338 HIS HIS A . n 
A 1 53  SER 53  339 339 SER SER A . n 
A 1 54  GLY 54  340 340 GLY GLY A . n 
A 1 55  LYS 55  341 341 LYS LYS A . n 
A 1 56  HIS 56  342 342 HIS HIS A . n 
A 1 57  TYR 57  343 343 TYR TYR A . n 
A 1 58  TRP 58  344 344 TRP TRP A . n 
A 1 59  GLU 59  345 345 GLU GLU A . n 
A 1 60  VAL 60  346 346 VAL VAL A . n 
A 1 61  ASP 61  347 347 ASP ASP A . n 
A 1 62  VAL 62  348 348 VAL VAL A . n 
A 1 63  THR 63  349 349 THR THR A . n 
A 1 64  GLY 64  350 350 GLY GLY A . n 
A 1 65  LYS 65  351 351 LYS LYS A . n 
A 1 66  GLU 66  352 352 GLU GLU A . n 
A 1 67  ALA 67  353 353 ALA ALA A . n 
A 1 68  TRP 68  354 354 TRP TRP A . n 
A 1 69  ASP 69  355 355 ASP ASP A . n 
A 1 70  LEU 70  356 356 LEU LEU A . n 
A 1 71  GLY 71  357 357 GLY GLY A . n 
A 1 72  VAL 72  358 358 VAL VAL A . n 
A 1 73  CYS 73  359 359 CYS CYS A . n 
A 1 74  ARG 74  360 360 ARG ARG A . n 
A 1 75  ASP 75  361 361 ASP ASP A . n 
A 1 76  SER 76  362 362 SER SER A . n 
A 1 77  VAL 77  363 363 VAL VAL A . n 
A 1 78  ARG 78  364 364 ARG ARG A . n 
A 1 79  ARG 79  365 365 ARG ARG A . n 
A 1 80  LYS 80  366 366 LYS LYS A . n 
A 1 81  GLY 81  367 367 GLY GLY A . n 
A 1 82  HIS 82  368 368 HIS HIS A . n 
A 1 83  PHE 83  369 369 PHE PHE A . n 
A 1 84  LEU 84  370 370 LEU LEU A . n 
A 1 85  LEU 85  371 371 LEU LEU A . n 
A 1 86  SER 86  372 372 SER SER A . n 
A 1 87  SER 87  373 373 SER SER A . n 
A 1 88  LYS 88  374 374 LYS LYS A . n 
A 1 89  SER 89  375 375 SER SER A . n 
A 1 90  GLY 90  376 376 GLY GLY A . n 
A 1 91  PHE 91  377 377 PHE PHE A . n 
A 1 92  TRP 92  378 378 TRP TRP A . n 
A 1 93  THR 93  379 379 THR THR A . n 
A 1 94  ILE 94  380 380 ILE ILE A . n 
A 1 95  TRP 95  381 381 TRP TRP A . n 
A 1 96  LEU 96  382 382 LEU LEU A . n 
A 1 97  TRP 97  383 383 TRP TRP A . n 
A 1 98  ASN 98  384 384 ASN ASN A . n 
A 1 99  LYS 99  385 385 LYS LYS A . n 
A 1 100 GLN 100 386 386 GLN GLN A . n 
A 1 101 LYS 101 387 387 LYS LYS A . n 
A 1 102 TYR 102 388 388 TYR TYR A . n 
A 1 103 GLU 103 389 389 GLU GLU A . n 
A 1 104 ALA 104 390 390 ALA ALA A . n 
A 1 105 GLY 105 391 391 GLY GLY A . n 
A 1 106 THR 106 392 392 THR THR A . n 
A 1 107 TYR 107 393 393 TYR TYR A . n 
A 1 108 PRO 108 394 394 PRO PRO A . n 
A 1 109 GLN 109 395 395 GLN GLN A . n 
A 1 110 THR 110 396 396 THR THR A . n 
A 1 111 PRO 111 397 397 PRO PRO A . n 
A 1 112 LEU 112 398 398 LEU LEU A . n 
A 1 113 HIS 113 399 399 HIS HIS A . n 
A 1 114 LEU 114 400 400 LEU LEU A . n 
A 1 115 GLN 115 401 401 GLN GLN A . n 
A 1 116 VAL 116 402 402 VAL VAL A . n 
A 1 117 PRO 117 403 403 PRO PRO A . n 
A 1 118 PRO 118 404 404 PRO PRO A . n 
A 1 119 CYS 119 405 405 CYS CYS A . n 
A 1 120 GLN 120 406 406 GLN GLN A . n 
A 1 121 VAL 121 407 407 VAL VAL A . n 
A 1 122 GLY 122 408 408 GLY GLY A . n 
A 1 123 ILE 123 409 409 ILE ILE A . n 
A 1 124 PHE 124 410 410 PHE PHE A . n 
A 1 125 LEU 125 411 411 LEU LEU A . n 
A 1 126 ASP 126 412 412 ASP ASP A . n 
A 1 127 TYR 127 413 413 TYR TYR A . n 
A 1 128 GLU 128 414 414 GLU GLU A . n 
A 1 129 ALA 129 415 415 ALA ALA A . n 
A 1 130 GLY 130 416 416 GLY GLY A . n 
A 1 131 MET 131 417 417 MET MET A . n 
A 1 132 VAL 132 418 418 VAL VAL A . n 
A 1 133 SER 133 419 419 SER SER A . n 
A 1 134 PHE 134 420 420 PHE PHE A . n 
A 1 135 TYR 135 421 421 TYR TYR A . n 
A 1 136 ASN 136 422 422 ASN ASN A . n 
A 1 137 ILE 137 423 423 ILE ILE A . n 
A 1 138 THR 138 424 424 THR THR A . n 
A 1 139 ASP 139 425 425 ASP ASP A . n 
A 1 140 HIS 140 426 426 HIS HIS A . n 
A 1 141 GLY 141 427 427 GLY GLY A . n 
A 1 142 SER 142 428 428 SER SER A . n 
A 1 143 LEU 143 429 429 LEU LEU A . n 
A 1 144 ILE 144 430 430 ILE ILE A . n 
A 1 145 TYR 145 431 431 TYR TYR A . n 
A 1 146 SER 146 432 432 SER SER A . n 
A 1 147 PHE 147 433 433 PHE PHE A . n 
A 1 148 SER 148 434 434 SER SER A . n 
A 1 149 GLU 149 435 435 GLU GLU A . n 
A 1 150 CYS 150 436 436 CYS CYS A . n 
A 1 151 ALA 151 437 437 ALA ALA A . n 
A 1 152 PHE 152 438 438 PHE PHE A . n 
A 1 153 THR 153 439 439 THR THR A . n 
A 1 154 GLY 154 440 440 GLY GLY A . n 
A 1 155 PRO 155 441 441 PRO PRO A . n 
A 1 156 LEU 156 442 442 LEU LEU A . n 
A 1 157 ARG 157 443 443 ARG ARG A . n 
A 1 158 PRO 158 444 444 PRO PRO A . n 
A 1 159 PHE 159 445 445 PHE PHE A . n 
A 1 160 PHE 160 446 446 PHE PHE A . n 
A 1 161 SER 161 447 447 SER SER A . n 
A 1 162 PRO 162 448 448 PRO PRO A . n 
A 1 163 GLY 163 449 449 GLY GLY A . n 
A 1 164 PHE 164 450 450 PHE PHE A . n 
A 1 165 ASN 165 451 451 ASN ASN A . n 
A 1 166 ASP 166 452 452 ASP ASP A . n 
A 1 167 GLY 167 453 453 GLY GLY A . n 
A 1 168 GLY 168 454 454 GLY GLY A . n 
A 1 169 LYS 169 455 455 LYS LYS A . n 
A 1 170 ASN 170 456 456 ASN ASN A . n 
A 1 171 THR 171 457 457 THR THR A . n 
A 1 172 ALA 172 458 458 ALA ALA A . n 
A 1 173 PRO 173 459 459 PRO PRO A . n 
A 1 174 LEU 174 460 460 LEU LEU A . n 
A 1 175 THR 175 461 461 THR THR A . n 
A 1 176 LEU 176 462 462 LEU LEU A . n 
A 1 177 CYS 177 463 463 CYS CYS A . n 
A 1 178 PRO 178 464 464 PRO PRO A . n 
A 1 179 LEU 179 465 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1I41 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1I41 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 A1I41 1   501 501 A1I41 236 A . 
C 3 EDO   1   502 502 EDO   EDO A . 
D 3 EDO   1   503 506 EDO   EDO A . 
E 4 HOH   1   601 87  HOH   HOH A . 
E 4 HOH   2   602 52  HOH   HOH A . 
E 4 HOH   3   603 121 HOH   HOH A . 
E 4 HOH   4   604 124 HOH   HOH A . 
E 4 HOH   5   605 25  HOH   HOH A . 
E 4 HOH   6   606 66  HOH   HOH A . 
E 4 HOH   7   607 21  HOH   HOH A . 
E 4 HOH   8   608 129 HOH   HOH A . 
E 4 HOH   9   609 115 HOH   HOH A . 
E 4 HOH   10  610 35  HOH   HOH A . 
E 4 HOH   11  611 74  HOH   HOH A . 
E 4 HOH   12  612 132 HOH   HOH A . 
E 4 HOH   13  613 63  HOH   HOH A . 
E 4 HOH   14  614 8   HOH   HOH A . 
E 4 HOH   15  615 38  HOH   HOH A . 
E 4 HOH   16  616 46  HOH   HOH A . 
E 4 HOH   17  617 29  HOH   HOH A . 
E 4 HOH   18  618 94  HOH   HOH A . 
E 4 HOH   19  619 71  HOH   HOH A . 
E 4 HOH   20  620 31  HOH   HOH A . 
E 4 HOH   21  621 55  HOH   HOH A . 
E 4 HOH   22  622 11  HOH   HOH A . 
E 4 HOH   23  623 33  HOH   HOH A . 
E 4 HOH   24  624 92  HOH   HOH A . 
E 4 HOH   25  625 39  HOH   HOH A . 
E 4 HOH   26  626 90  HOH   HOH A . 
E 4 HOH   27  627 13  HOH   HOH A . 
E 4 HOH   28  628 133 HOH   HOH A . 
E 4 HOH   29  629 53  HOH   HOH A . 
E 4 HOH   30  630 30  HOH   HOH A . 
E 4 HOH   31  631 23  HOH   HOH A . 
E 4 HOH   32  632 128 HOH   HOH A . 
E 4 HOH   33  633 54  HOH   HOH A . 
E 4 HOH   34  634 58  HOH   HOH A . 
E 4 HOH   35  635 78  HOH   HOH A . 
E 4 HOH   36  636 72  HOH   HOH A . 
E 4 HOH   37  637 10  HOH   HOH A . 
E 4 HOH   38  638 69  HOH   HOH A . 
E 4 HOH   39  639 118 HOH   HOH A . 
E 4 HOH   40  640 27  HOH   HOH A . 
E 4 HOH   41  641 37  HOH   HOH A . 
E 4 HOH   42  642 51  HOH   HOH A . 
E 4 HOH   43  643 76  HOH   HOH A . 
E 4 HOH   44  644 61  HOH   HOH A . 
E 4 HOH   45  645 57  HOH   HOH A . 
E 4 HOH   46  646 83  HOH   HOH A . 
E 4 HOH   47  647 70  HOH   HOH A . 
E 4 HOH   48  648 64  HOH   HOH A . 
E 4 HOH   49  649 109 HOH   HOH A . 
E 4 HOH   50  650 110 HOH   HOH A . 
E 4 HOH   51  651 122 HOH   HOH A . 
E 4 HOH   52  652 81  HOH   HOH A . 
E 4 HOH   53  653 125 HOH   HOH A . 
E 4 HOH   54  654 26  HOH   HOH A . 
E 4 HOH   55  655 108 HOH   HOH A . 
E 4 HOH   56  656 12  HOH   HOH A . 
E 4 HOH   57  657 73  HOH   HOH A . 
E 4 HOH   58  658 49  HOH   HOH A . 
E 4 HOH   59  659 34  HOH   HOH A . 
E 4 HOH   60  660 6   HOH   HOH A . 
E 4 HOH   61  661 77  HOH   HOH A . 
E 4 HOH   62  662 85  HOH   HOH A . 
E 4 HOH   63  663 9   HOH   HOH A . 
E 4 HOH   64  664 130 HOH   HOH A . 
E 4 HOH   65  665 119 HOH   HOH A . 
E 4 HOH   66  666 131 HOH   HOH A . 
E 4 HOH   67  667 42  HOH   HOH A . 
E 4 HOH   68  668 17  HOH   HOH A . 
E 4 HOH   69  669 20  HOH   HOH A . 
E 4 HOH   70  670 59  HOH   HOH A . 
E 4 HOH   71  671 91  HOH   HOH A . 
E 4 HOH   72  672 89  HOH   HOH A . 
E 4 HOH   73  673 45  HOH   HOH A . 
E 4 HOH   74  674 67  HOH   HOH A . 
E 4 HOH   75  675 62  HOH   HOH A . 
E 4 HOH   76  676 56  HOH   HOH A . 
E 4 HOH   77  677 28  HOH   HOH A . 
E 4 HOH   78  678 88  HOH   HOH A . 
E 4 HOH   79  679 7   HOH   HOH A . 
E 4 HOH   80  680 82  HOH   HOH A . 
E 4 HOH   81  681 123 HOH   HOH A . 
E 4 HOH   82  682 24  HOH   HOH A . 
E 4 HOH   83  683 102 HOH   HOH A . 
E 4 HOH   84  684 65  HOH   HOH A . 
E 4 HOH   85  685 18  HOH   HOH A . 
E 4 HOH   86  686 32  HOH   HOH A . 
E 4 HOH   87  687 41  HOH   HOH A . 
E 4 HOH   88  688 43  HOH   HOH A . 
E 4 HOH   89  689 44  HOH   HOH A . 
E 4 HOH   90  690 19  HOH   HOH A . 
E 4 HOH   91  691 40  HOH   HOH A . 
E 4 HOH   92  692 14  HOH   HOH A . 
E 4 HOH   93  693 60  HOH   HOH A . 
E 4 HOH   94  694 2   HOH   HOH A . 
E 4 HOH   95  695 5   HOH   HOH A . 
E 4 HOH   96  696 1   HOH   HOH A . 
E 4 HOH   97  697 16  HOH   HOH A . 
E 4 HOH   98  698 79  HOH   HOH A . 
E 4 HOH   99  699 3   HOH   HOH A . 
E 4 HOH   100 700 75  HOH   HOH A . 
E 4 HOH   101 701 48  HOH   HOH A . 
E 4 HOH   102 702 93  HOH   HOH A . 
E 4 HOH   103 703 96  HOH   HOH A . 
E 4 HOH   104 704 4   HOH   HOH A . 
E 4 HOH   105 705 99  HOH   HOH A . 
E 4 HOH   106 706 112 HOH   HOH A . 
E 4 HOH   107 707 113 HOH   HOH A . 
E 4 HOH   108 708 15  HOH   HOH A . 
E 4 HOH   109 709 80  HOH   HOH A . 
E 4 HOH   110 710 111 HOH   HOH A . 
E 4 HOH   111 711 117 HOH   HOH A . 
E 4 HOH   112 712 47  HOH   HOH A . 
E 4 HOH   113 713 97  HOH   HOH A . 
E 4 HOH   114 714 50  HOH   HOH A . 
E 4 HOH   115 715 84  HOH   HOH A . 
E 4 HOH   116 716 98  HOH   HOH A . 
E 4 HOH   117 717 107 HOH   HOH A . 
E 4 HOH   118 718 103 HOH   HOH A . 
E 4 HOH   119 719 116 HOH   HOH A . 
E 4 HOH   120 720 100 HOH   HOH A . 
E 4 HOH   121 721 104 HOH   HOH A . 
E 4 HOH   122 722 114 HOH   HOH A . 
E 4 HOH   123 723 126 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 385 ? CG  ? A LYS 99  CG  
2  1 Y 1 A LYS 385 ? CD  ? A LYS 99  CD  
3  1 Y 1 A LYS 385 ? CE  ? A LYS 99  CE  
4  1 Y 1 A LYS 385 ? NZ  ? A LYS 99  NZ  
5  1 Y 1 A GLN 386 ? CG  ? A GLN 100 CG  
6  1 Y 1 A GLN 386 ? CD  ? A GLN 100 CD  
7  1 Y 1 A GLN 386 ? OE1 ? A GLN 100 OE1 
8  1 Y 1 A GLN 386 ? NE2 ? A GLN 100 NE2 
9  1 Y 1 A LYS 387 ? CD  ? A LYS 101 CD  
10 1 Y 1 A LYS 387 ? CE  ? A LYS 101 CE  
11 1 Y 1 A LYS 387 ? NZ  ? A LYS 101 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QBA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.750 
_cell.length_a_esd                 ? 
_cell.length_b                     67.750 
_cell.length_b_esd                 ? 
_cell.length_c                     71.114 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9QBA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                171 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 62' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9QBA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              3.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;2.3 M Sodium Chloride 
0.1 M Sodium Citrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2025-02-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9QBA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.45 
_reflns.d_resolution_low                               58.67 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     32898 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.92 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.081 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       681895 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.45 
_reflns_shell.d_res_low                                     1.47 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           31898 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1643 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               19.4 
_reflns_shell.pdbx_chi_squared                              0.84 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               1.557 
_reflns_shell.pdbx_Rpim_I_all                               0.349 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.819 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.516 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.39 
_refine.aniso_B[1][2]                            -0.20 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.39 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            1.28 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.862 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.976 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9QBA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.45 
_refine.ls_d_res_low                             58.67 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     31293 
_refine.ls_number_reflns_R_free                  1571 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15102 
_refine.ls_R_factor_R_free                       0.16200 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15044 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.068 
_refine.pdbx_overall_ESU_R_Free                  0.054 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.506 
_refine.overall_SU_ML                            0.042 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        58.67 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               1578 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1418 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  0.012  1511 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1331 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.356  1.788  2061 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.491  1.765  3070 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.390  5.000  179  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.237  5.000  8    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.217 10.000 213  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  207  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1841 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  371  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.016  2.173  716  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.974  2.172  716  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.207  3.916  895  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.210  3.916  896  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.173  2.338  795  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.170  2.340  796  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.336  4.196  1167 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.809 24.04  1669 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.611 23.67  1652 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 1.924  3.000  2842 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.450 
_refine_ls_shell.d_res_low                           1.488 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                91 
_refine_ls_shell.number_reflns_R_work                2345 
_refine_ls_shell.percent_reflns_obs                  100.00 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.214 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.267 
# 
_struct.entry_id                     9QBA 
_struct.title                        'Human TRIM21 PRYSPRY domain in complex with AL236' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9QBA 
_struct_keywords.text            'TRIM21, PRYSPRY Domain, E3 ligase, Inhibitor, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RO52_HUMAN 
_struct_ref.pdbx_db_accession          P19474 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRK
GHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFF
SPGFNDGGKNTAPLTLCPL
;
_struct_ref.pdbx_align_begin           287 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9QBA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 179 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P19474 
_struct_ref_seq.db_align_beg                  287 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  465 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       287 
_struct_ref_seq.pdbx_auth_seq_align_end       465 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 440  ? 
1 MORE         6    ? 
1 'SSA (A^2)'  8530 ? 
# 
_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,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 6  ? ALA A 10 ? ASP A 292 ALA A 296 5 ? 5 
HELX_P HELX_P2 AA2 SER A 86 ? SER A 89 ? SER A 372 SER A 375 5 ? 4 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           107 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            393 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    108 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     394 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -11.96 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 14  ? LEU A 16  ? LEU A 300 LEU A 302 
AA1 2 GLN A 22  ? LEU A 25  ? GLN A 308 LEU A 311 
AA1 3 LEU A 174 ? LEU A 176 ? LEU A 460 LEU A 462 
AA1 4 LYS A 55  ? ASP A 61  ? LYS A 341 ASP A 347 
AA1 5 GLN A 120 ? ASP A 126 ? GLN A 406 ASP A 412 
AA1 6 MET A 131 ? ASN A 136 ? MET A 417 ASN A 422 
AA1 7 SER A 142 ? PHE A 147 ? SER A 428 PHE A 433 
AA2 1 VAL A 45  ? LEU A 46  ? VAL A 331 LEU A 332 
AA2 2 LEU A 156 ? SER A 161 ? LEU A 442 SER A 447 
AA2 3 TRP A 68  ? ARG A 74  ? TRP A 354 ARG A 360 
AA2 4 PHE A 91  ? TRP A 97  ? PHE A 377 TRP A 383 
AA2 5 LYS A 101 ? ALA A 104 ? LYS A 387 ALA A 390 
AA2 6 THR A 110 ? LEU A 112 ? THR A 396 LEU A 398 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 15  ? N ILE A 301 O ARG A 24  ? O ARG A 310 
AA1 2 3 N VAL A 23  ? N VAL A 309 O LEU A 174 ? O LEU A 460 
AA1 3 4 O THR A 175 ? O THR A 461 N ASP A 61  ? N ASP A 347 
AA1 4 5 N TRP A 58  ? N TRP A 344 O ILE A 123 ? O ILE A 409 
AA1 5 6 N PHE A 124 ? N PHE A 410 O SER A 133 ? O SER A 419 
AA1 6 7 N ASN A 136 ? N ASN A 422 O SER A 142 ? O SER A 428 
AA2 1 2 N VAL A 45  ? N VAL A 331 O PHE A 160 ? O PHE A 446 
AA2 2 3 O ARG A 157 ? O ARG A 443 N CYS A 73  ? N CYS A 359 
AA2 3 4 N VAL A 72  ? N VAL A 358 O TRP A 92  ? O TRP A 378 
AA2 4 5 N TRP A 97  ? N TRP A 383 O LYS A 101 ? O LYS A 387 
AA2 5 6 N TYR A 102 ? N TYR A 388 O LEU A 112 ? O LEU A 398 
# 
_pdbx_entry_details.entry_id                   9QBA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 LYS A 385 ? ? 76.78   -33.00 
2 1 ASP A 425 ? ? -87.45  46.46  
3 1 ASP A 452 ? ? -151.27 45.29  
4 1 ASN A 456 ? ? -148.08 39.67  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     645 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     LEU 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      465 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    LEU 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     179 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1I41 C2   C N N 1   
A1I41 C6   C N N 2   
A1I41 C9   C N N 3   
A1I41 C12  C Y N 4   
A1I41 C15  C N N 5   
A1I41 C18  C Y N 6   
A1I41 C21  C Y N 7   
A1I41 C27  C N N 8   
A1I41 C29  C Y N 9   
A1I41 O1   O N N 10  
A1I41 N3   N N N 11  
A1I41 C4   C N N 12  
A1I41 C5   C N N 13  
A1I41 C7   C N N 14  
A1I41 C8   C N N 15  
A1I41 C10  C N N 16  
A1I41 C11  C Y N 17  
A1I41 S13  S N N 18  
A1I41 O14  O N N 19  
A1I41 O16  O N N 20  
A1I41 C17  C Y N 21  
A1I41 C19  C Y N 22  
A1I41 C20  C Y N 23  
A1I41 C22  C Y N 24  
A1I41 F23  F N N 25  
A1I41 C24  C Y N 26  
A1I41 C25  C Y N 27  
A1I41 S26  S N N 28  
A1I41 C28  C Y N 29  
A1I41 H1   H N N 30  
A1I41 H2   H N N 31  
A1I41 H3   H N N 32  
A1I41 H4   H N N 33  
A1I41 H5   H N N 34  
A1I41 H6   H N N 35  
A1I41 H7   H N N 36  
A1I41 H8   H N N 37  
A1I41 H9   H N N 38  
A1I41 H10  H N N 39  
A1I41 H11  H N N 40  
A1I41 H12  H N N 41  
A1I41 H13  H N N 42  
A1I41 H14  H N N 43  
A1I41 H15  H N N 44  
A1I41 H16  H N N 45  
A1I41 H17  H N N 46  
A1I41 H18  H N N 47  
A1I41 H19  H N N 48  
A1I41 H20  H N N 49  
A1I41 H21  H N N 50  
A1I41 H22  H N N 51  
A1I41 H23  H N N 52  
A1I41 H24  H N N 53  
A1I41 H25  H N N 54  
A1I41 H26  H N N 55  
ALA   N    N N N 56  
ALA   CA   C N S 57  
ALA   C    C N N 58  
ALA   O    O N N 59  
ALA   CB   C N N 60  
ALA   OXT  O N N 61  
ALA   H    H N N 62  
ALA   H2   H N N 63  
ALA   HA   H N N 64  
ALA   HB1  H N N 65  
ALA   HB2  H N N 66  
ALA   HB3  H N N 67  
ALA   HXT  H N N 68  
ARG   N    N N N 69  
ARG   CA   C N S 70  
ARG   C    C N N 71  
ARG   O    O N N 72  
ARG   CB   C N N 73  
ARG   CG   C N N 74  
ARG   CD   C N N 75  
ARG   NE   N N N 76  
ARG   CZ   C N N 77  
ARG   NH1  N N N 78  
ARG   NH2  N N N 79  
ARG   OXT  O N N 80  
ARG   H    H N N 81  
ARG   H2   H N N 82  
ARG   HA   H N N 83  
ARG   HB2  H N N 84  
ARG   HB3  H N N 85  
ARG   HG2  H N N 86  
ARG   HG3  H N N 87  
ARG   HD2  H N N 88  
ARG   HD3  H N N 89  
ARG   HE   H N N 90  
ARG   HH11 H N N 91  
ARG   HH12 H N N 92  
ARG   HH21 H N N 93  
ARG   HH22 H N N 94  
ARG   HXT  H N N 95  
ASN   N    N N N 96  
ASN   CA   C N S 97  
ASN   C    C N N 98  
ASN   O    O N N 99  
ASN   CB   C N N 100 
ASN   CG   C N N 101 
ASN   OD1  O N N 102 
ASN   ND2  N N N 103 
ASN   OXT  O N N 104 
ASN   H    H N N 105 
ASN   H2   H N N 106 
ASN   HA   H N N 107 
ASN   HB2  H N N 108 
ASN   HB3  H N N 109 
ASN   HD21 H N N 110 
ASN   HD22 H N N 111 
ASN   HXT  H N N 112 
ASP   N    N N N 113 
ASP   CA   C N S 114 
ASP   C    C N N 115 
ASP   O    O N N 116 
ASP   CB   C N N 117 
ASP   CG   C N N 118 
ASP   OD1  O N N 119 
ASP   OD2  O N N 120 
ASP   OXT  O N N 121 
ASP   H    H N N 122 
ASP   H2   H N N 123 
ASP   HA   H N N 124 
ASP   HB2  H N N 125 
ASP   HB3  H N N 126 
ASP   HD2  H N N 127 
ASP   HXT  H N N 128 
CYS   N    N N N 129 
CYS   CA   C N R 130 
CYS   C    C N N 131 
CYS   O    O N N 132 
CYS   CB   C N N 133 
CYS   SG   S N N 134 
CYS   OXT  O N N 135 
CYS   H    H N N 136 
CYS   H2   H N N 137 
CYS   HA   H N N 138 
CYS   HB2  H N N 139 
CYS   HB3  H N N 140 
CYS   HG   H N N 141 
CYS   HXT  H N N 142 
EDO   C1   C N N 143 
EDO   O1   O N N 144 
EDO   C2   C N N 145 
EDO   O2   O N N 146 
EDO   H11  H N N 147 
EDO   H12  H N N 148 
EDO   HO1  H N N 149 
EDO   H21  H N N 150 
EDO   H22  H N N 151 
EDO   HO2  H N N 152 
GLN   N    N N N 153 
GLN   CA   C N S 154 
GLN   C    C N N 155 
GLN   O    O N N 156 
GLN   CB   C N N 157 
GLN   CG   C N N 158 
GLN   CD   C N N 159 
GLN   OE1  O N N 160 
GLN   NE2  N N N 161 
GLN   OXT  O N N 162 
GLN   H    H N N 163 
GLN   H2   H N N 164 
GLN   HA   H N N 165 
GLN   HB2  H N N 166 
GLN   HB3  H N N 167 
GLN   HG2  H N N 168 
GLN   HG3  H N N 169 
GLN   HE21 H N N 170 
GLN   HE22 H N N 171 
GLN   HXT  H N N 172 
GLU   N    N N N 173 
GLU   CA   C N S 174 
GLU   C    C N N 175 
GLU   O    O N N 176 
GLU   CB   C N N 177 
GLU   CG   C N N 178 
GLU   CD   C N N 179 
GLU   OE1  O N N 180 
GLU   OE2  O N N 181 
GLU   OXT  O N N 182 
GLU   H    H N N 183 
GLU   H2   H N N 184 
GLU   HA   H N N 185 
GLU   HB2  H N N 186 
GLU   HB3  H N N 187 
GLU   HG2  H N N 188 
GLU   HG3  H N N 189 
GLU   HE2  H N N 190 
GLU   HXT  H N N 191 
GLY   N    N N N 192 
GLY   CA   C N N 193 
GLY   C    C N N 194 
GLY   O    O N N 195 
GLY   OXT  O N N 196 
GLY   H    H N N 197 
GLY   H2   H N N 198 
GLY   HA2  H N N 199 
GLY   HA3  H N N 200 
GLY   HXT  H N N 201 
HIS   N    N N N 202 
HIS   CA   C N S 203 
HIS   C    C N N 204 
HIS   O    O N N 205 
HIS   CB   C N N 206 
HIS   CG   C Y N 207 
HIS   ND1  N Y N 208 
HIS   CD2  C Y N 209 
HIS   CE1  C Y N 210 
HIS   NE2  N Y N 211 
HIS   OXT  O N N 212 
HIS   H    H N N 213 
HIS   H2   H N N 214 
HIS   HA   H N N 215 
HIS   HB2  H N N 216 
HIS   HB3  H N N 217 
HIS   HD1  H N N 218 
HIS   HD2  H N N 219 
HIS   HE1  H N N 220 
HIS   HE2  H N N 221 
HIS   HXT  H N N 222 
HOH   O    O N N 223 
HOH   H1   H N N 224 
HOH   H2   H N N 225 
ILE   N    N N N 226 
ILE   CA   C N S 227 
ILE   C    C N N 228 
ILE   O    O N N 229 
ILE   CB   C N S 230 
ILE   CG1  C N N 231 
ILE   CG2  C N N 232 
ILE   CD1  C N N 233 
ILE   OXT  O N N 234 
ILE   H    H N N 235 
ILE   H2   H N N 236 
ILE   HA   H N N 237 
ILE   HB   H N N 238 
ILE   HG12 H N N 239 
ILE   HG13 H N N 240 
ILE   HG21 H N N 241 
ILE   HG22 H N N 242 
ILE   HG23 H N N 243 
ILE   HD11 H N N 244 
ILE   HD12 H N N 245 
ILE   HD13 H N N 246 
ILE   HXT  H N N 247 
LEU   N    N N N 248 
LEU   CA   C N S 249 
LEU   C    C N N 250 
LEU   O    O N N 251 
LEU   CB   C N N 252 
LEU   CG   C N N 253 
LEU   CD1  C N N 254 
LEU   CD2  C N N 255 
LEU   OXT  O N N 256 
LEU   H    H N N 257 
LEU   H2   H N N 258 
LEU   HA   H N N 259 
LEU   HB2  H N N 260 
LEU   HB3  H N N 261 
LEU   HG   H N N 262 
LEU   HD11 H N N 263 
LEU   HD12 H N N 264 
LEU   HD13 H N N 265 
LEU   HD21 H N N 266 
LEU   HD22 H N N 267 
LEU   HD23 H N N 268 
LEU   HXT  H N N 269 
LYS   N    N N N 270 
LYS   CA   C N S 271 
LYS   C    C N N 272 
LYS   O    O N N 273 
LYS   CB   C N N 274 
LYS   CG   C N N 275 
LYS   CD   C N N 276 
LYS   CE   C N N 277 
LYS   NZ   N N N 278 
LYS   OXT  O N N 279 
LYS   H    H N N 280 
LYS   H2   H N N 281 
LYS   HA   H N N 282 
LYS   HB2  H N N 283 
LYS   HB3  H N N 284 
LYS   HG2  H N N 285 
LYS   HG3  H N N 286 
LYS   HD2  H N N 287 
LYS   HD3  H N N 288 
LYS   HE2  H N N 289 
LYS   HE3  H N N 290 
LYS   HZ1  H N N 291 
LYS   HZ2  H N N 292 
LYS   HZ3  H N N 293 
LYS   HXT  H N N 294 
MET   N    N N N 295 
MET   CA   C N S 296 
MET   C    C N N 297 
MET   O    O N N 298 
MET   CB   C N N 299 
MET   CG   C N N 300 
MET   SD   S N N 301 
MET   CE   C N N 302 
MET   OXT  O N N 303 
MET   H    H N N 304 
MET   H2   H N N 305 
MET   HA   H N N 306 
MET   HB2  H N N 307 
MET   HB3  H N N 308 
MET   HG2  H N N 309 
MET   HG3  H N N 310 
MET   HE1  H N N 311 
MET   HE2  H N N 312 
MET   HE3  H N N 313 
MET   HXT  H N N 314 
PHE   N    N N N 315 
PHE   CA   C N S 316 
PHE   C    C N N 317 
PHE   O    O N N 318 
PHE   CB   C N N 319 
PHE   CG   C Y N 320 
PHE   CD1  C Y N 321 
PHE   CD2  C Y N 322 
PHE   CE1  C Y N 323 
PHE   CE2  C Y N 324 
PHE   CZ   C Y N 325 
PHE   OXT  O N N 326 
PHE   H    H N N 327 
PHE   H2   H N N 328 
PHE   HA   H N N 329 
PHE   HB2  H N N 330 
PHE   HB3  H N N 331 
PHE   HD1  H N N 332 
PHE   HD2  H N N 333 
PHE   HE1  H N N 334 
PHE   HE2  H N N 335 
PHE   HZ   H N N 336 
PHE   HXT  H N N 337 
PRO   N    N N N 338 
PRO   CA   C N S 339 
PRO   C    C N N 340 
PRO   O    O N N 341 
PRO   CB   C N N 342 
PRO   CG   C N N 343 
PRO   CD   C N N 344 
PRO   OXT  O N N 345 
PRO   H    H N N 346 
PRO   HA   H N N 347 
PRO   HB2  H N N 348 
PRO   HB3  H N N 349 
PRO   HG2  H N N 350 
PRO   HG3  H N N 351 
PRO   HD2  H N N 352 
PRO   HD3  H N N 353 
PRO   HXT  H N N 354 
SER   N    N N N 355 
SER   CA   C N S 356 
SER   C    C N N 357 
SER   O    O N N 358 
SER   CB   C N N 359 
SER   OG   O N N 360 
SER   OXT  O N N 361 
SER   H    H N N 362 
SER   H2   H N N 363 
SER   HA   H N N 364 
SER   HB2  H N N 365 
SER   HB3  H N N 366 
SER   HG   H N N 367 
SER   HXT  H N N 368 
THR   N    N N N 369 
THR   CA   C N S 370 
THR   C    C N N 371 
THR   O    O N N 372 
THR   CB   C N R 373 
THR   OG1  O N N 374 
THR   CG2  C N N 375 
THR   OXT  O N N 376 
THR   H    H N N 377 
THR   H2   H N N 378 
THR   HA   H N N 379 
THR   HB   H N N 380 
THR   HG1  H N N 381 
THR   HG21 H N N 382 
THR   HG22 H N N 383 
THR   HG23 H N N 384 
THR   HXT  H N N 385 
TRP   N    N N N 386 
TRP   CA   C N S 387 
TRP   C    C N N 388 
TRP   O    O N N 389 
TRP   CB   C N N 390 
TRP   CG   C Y N 391 
TRP   CD1  C Y N 392 
TRP   CD2  C Y N 393 
TRP   NE1  N Y N 394 
TRP   CE2  C Y N 395 
TRP   CE3  C Y N 396 
TRP   CZ2  C Y N 397 
TRP   CZ3  C Y N 398 
TRP   CH2  C Y N 399 
TRP   OXT  O N N 400 
TRP   H    H N N 401 
TRP   H2   H N N 402 
TRP   HA   H N N 403 
TRP   HB2  H N N 404 
TRP   HB3  H N N 405 
TRP   HD1  H N N 406 
TRP   HE1  H N N 407 
TRP   HE3  H N N 408 
TRP   HZ2  H N N 409 
TRP   HZ3  H N N 410 
TRP   HH2  H N N 411 
TRP   HXT  H N N 412 
TYR   N    N N N 413 
TYR   CA   C N S 414 
TYR   C    C N N 415 
TYR   O    O N N 416 
TYR   CB   C N N 417 
TYR   CG   C Y N 418 
TYR   CD1  C Y N 419 
TYR   CD2  C Y N 420 
TYR   CE1  C Y N 421 
TYR   CE2  C Y N 422 
TYR   CZ   C Y N 423 
TYR   OH   O N N 424 
TYR   OXT  O N N 425 
TYR   H    H N N 426 
TYR   H2   H N N 427 
TYR   HA   H N N 428 
TYR   HB2  H N N 429 
TYR   HB3  H N N 430 
TYR   HD1  H N N 431 
TYR   HD2  H N N 432 
TYR   HE1  H N N 433 
TYR   HE2  H N N 434 
TYR   HH   H N N 435 
TYR   HXT  H N N 436 
VAL   N    N N N 437 
VAL   CA   C N S 438 
VAL   C    C N N 439 
VAL   O    O N N 440 
VAL   CB   C N N 441 
VAL   CG1  C N N 442 
VAL   CG2  C N N 443 
VAL   OXT  O N N 444 
VAL   H    H N N 445 
VAL   H2   H N N 446 
VAL   HA   H N N 447 
VAL   HB   H N N 448 
VAL   HG11 H N N 449 
VAL   HG12 H N N 450 
VAL   HG13 H N N 451 
VAL   HG21 H N N 452 
VAL   HG22 H N N 453 
VAL   HG23 H N N 454 
VAL   HXT  H N N 455 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1I41 F23 C22  sing N N 1   
A1I41 C24 C22  doub Y N 2   
A1I41 C24 C25  sing Y N 3   
A1I41 C22 C21  sing Y N 4   
A1I41 S26 C25  sing N N 5   
A1I41 S26 C27  sing N N 6   
A1I41 C25 C19  doub Y N 7   
A1I41 C21 C20  doub Y N 8   
A1I41 C7  C8   sing N N 9   
A1I41 C7  C6   sing N N 10  
A1I41 C19 C20  sing Y N 11  
A1I41 C19 C18  sing N N 12  
A1I41 C28 C18  doub Y N 13  
A1I41 C28 C29  sing Y N 14  
A1I41 C18 C17  sing Y N 15  
A1I41 C29 C11  doub Y N 16  
A1I41 C8  C9   sing N N 17  
A1I41 C6  C5   sing N N 18  
A1I41 C17 C12  doub Y N 19  
A1I41 C11 C2   sing N N 20  
A1I41 C11 C12  sing Y N 21  
A1I41 O1  C2   doub N N 22  
A1I41 C2  N3   sing N N 23  
A1I41 C12 S13  sing N N 24  
A1I41 C9  C10  sing N N 25  
A1I41 C15 S13  sing N N 26  
A1I41 C5  C10  sing N N 27  
A1I41 C5  C4   sing N N 28  
A1I41 N3  C4   sing N N 29  
A1I41 S13 O16  doub N N 30  
A1I41 S13 O14  doub N N 31  
A1I41 C6  H1   sing N N 32  
A1I41 C6  H2   sing N N 33  
A1I41 C9  H3   sing N N 34  
A1I41 C9  H4   sing N N 35  
A1I41 C15 H5   sing N N 36  
A1I41 C15 H6   sing N N 37  
A1I41 C15 H7   sing N N 38  
A1I41 C21 H8   sing N N 39  
A1I41 C27 H9   sing N N 40  
A1I41 C27 H10  sing N N 41  
A1I41 C27 H11  sing N N 42  
A1I41 C29 H12  sing N N 43  
A1I41 N3  H13  sing N N 44  
A1I41 C4  H14  sing N N 45  
A1I41 C4  H15  sing N N 46  
A1I41 C5  H16  sing N N 47  
A1I41 C7  H17  sing N N 48  
A1I41 C7  H18  sing N N 49  
A1I41 C8  H19  sing N N 50  
A1I41 C8  H20  sing N N 51  
A1I41 C10 H21  sing N N 52  
A1I41 C10 H22  sing N N 53  
A1I41 C17 H23  sing N N 54  
A1I41 C20 H24  sing N N 55  
A1I41 C24 H25  sing N N 56  
A1I41 C28 H26  sing N N 57  
ALA   N   CA   sing N N 58  
ALA   N   H    sing N N 59  
ALA   N   H2   sing N N 60  
ALA   CA  C    sing N N 61  
ALA   CA  CB   sing N N 62  
ALA   CA  HA   sing N N 63  
ALA   C   O    doub N N 64  
ALA   C   OXT  sing N N 65  
ALA   CB  HB1  sing N N 66  
ALA   CB  HB2  sing N N 67  
ALA   CB  HB3  sing N N 68  
ALA   OXT HXT  sing N N 69  
ARG   N   CA   sing N N 70  
ARG   N   H    sing N N 71  
ARG   N   H2   sing N N 72  
ARG   CA  C    sing N N 73  
ARG   CA  CB   sing N N 74  
ARG   CA  HA   sing N N 75  
ARG   C   O    doub N N 76  
ARG   C   OXT  sing N N 77  
ARG   CB  CG   sing N N 78  
ARG   CB  HB2  sing N N 79  
ARG   CB  HB3  sing N N 80  
ARG   CG  CD   sing N N 81  
ARG   CG  HG2  sing N N 82  
ARG   CG  HG3  sing N N 83  
ARG   CD  NE   sing N N 84  
ARG   CD  HD2  sing N N 85  
ARG   CD  HD3  sing N N 86  
ARG   NE  CZ   sing N N 87  
ARG   NE  HE   sing N N 88  
ARG   CZ  NH1  sing N N 89  
ARG   CZ  NH2  doub N N 90  
ARG   NH1 HH11 sing N N 91  
ARG   NH1 HH12 sing N N 92  
ARG   NH2 HH21 sing N N 93  
ARG   NH2 HH22 sing N N 94  
ARG   OXT HXT  sing N N 95  
ASN   N   CA   sing N N 96  
ASN   N   H    sing N N 97  
ASN   N   H2   sing N N 98  
ASN   CA  C    sing N N 99  
ASN   CA  CB   sing N N 100 
ASN   CA  HA   sing N N 101 
ASN   C   O    doub N N 102 
ASN   C   OXT  sing N N 103 
ASN   CB  CG   sing N N 104 
ASN   CB  HB2  sing N N 105 
ASN   CB  HB3  sing N N 106 
ASN   CG  OD1  doub N N 107 
ASN   CG  ND2  sing N N 108 
ASN   ND2 HD21 sing N N 109 
ASN   ND2 HD22 sing N N 110 
ASN   OXT HXT  sing N N 111 
ASP   N   CA   sing N N 112 
ASP   N   H    sing N N 113 
ASP   N   H2   sing N N 114 
ASP   CA  C    sing N N 115 
ASP   CA  CB   sing N N 116 
ASP   CA  HA   sing N N 117 
ASP   C   O    doub N N 118 
ASP   C   OXT  sing N N 119 
ASP   CB  CG   sing N N 120 
ASP   CB  HB2  sing N N 121 
ASP   CB  HB3  sing N N 122 
ASP   CG  OD1  doub N N 123 
ASP   CG  OD2  sing N N 124 
ASP   OD2 HD2  sing N N 125 
ASP   OXT HXT  sing N N 126 
CYS   N   CA   sing N N 127 
CYS   N   H    sing N N 128 
CYS   N   H2   sing N N 129 
CYS   CA  C    sing N N 130 
CYS   CA  CB   sing N N 131 
CYS   CA  HA   sing N N 132 
CYS   C   O    doub N N 133 
CYS   C   OXT  sing N N 134 
CYS   CB  SG   sing N N 135 
CYS   CB  HB2  sing N N 136 
CYS   CB  HB3  sing N N 137 
CYS   SG  HG   sing N N 138 
CYS   OXT HXT  sing N N 139 
EDO   C1  O1   sing N N 140 
EDO   C1  C2   sing N N 141 
EDO   C1  H11  sing N N 142 
EDO   C1  H12  sing N N 143 
EDO   O1  HO1  sing N N 144 
EDO   C2  O2   sing N N 145 
EDO   C2  H21  sing N N 146 
EDO   C2  H22  sing N N 147 
EDO   O2  HO2  sing N N 148 
GLN   N   CA   sing N N 149 
GLN   N   H    sing N N 150 
GLN   N   H2   sing N N 151 
GLN   CA  C    sing N N 152 
GLN   CA  CB   sing N N 153 
GLN   CA  HA   sing N N 154 
GLN   C   O    doub N N 155 
GLN   C   OXT  sing N N 156 
GLN   CB  CG   sing N N 157 
GLN   CB  HB2  sing N N 158 
GLN   CB  HB3  sing N N 159 
GLN   CG  CD   sing N N 160 
GLN   CG  HG2  sing N N 161 
GLN   CG  HG3  sing N N 162 
GLN   CD  OE1  doub N N 163 
GLN   CD  NE2  sing N N 164 
GLN   NE2 HE21 sing N N 165 
GLN   NE2 HE22 sing N N 166 
GLN   OXT HXT  sing N N 167 
GLU   N   CA   sing N N 168 
GLU   N   H    sing N N 169 
GLU   N   H2   sing N N 170 
GLU   CA  C    sing N N 171 
GLU   CA  CB   sing N N 172 
GLU   CA  HA   sing N N 173 
GLU   C   O    doub N N 174 
GLU   C   OXT  sing N N 175 
GLU   CB  CG   sing N N 176 
GLU   CB  HB2  sing N N 177 
GLU   CB  HB3  sing N N 178 
GLU   CG  CD   sing N N 179 
GLU   CG  HG2  sing N N 180 
GLU   CG  HG3  sing N N 181 
GLU   CD  OE1  doub N N 182 
GLU   CD  OE2  sing N N 183 
GLU   OE2 HE2  sing N N 184 
GLU   OXT HXT  sing N N 185 
GLY   N   CA   sing N N 186 
GLY   N   H    sing N N 187 
GLY   N   H2   sing N N 188 
GLY   CA  C    sing N N 189 
GLY   CA  HA2  sing N N 190 
GLY   CA  HA3  sing N N 191 
GLY   C   O    doub N N 192 
GLY   C   OXT  sing N N 193 
GLY   OXT HXT  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
THR   N   CA   sing N N 356 
THR   N   H    sing N N 357 
THR   N   H2   sing N N 358 
THR   CA  C    sing N N 359 
THR   CA  CB   sing N N 360 
THR   CA  HA   sing N N 361 
THR   C   O    doub N N 362 
THR   C   OXT  sing N N 363 
THR   CB  OG1  sing N N 364 
THR   CB  CG2  sing N N 365 
THR   CB  HB   sing N N 366 
THR   OG1 HG1  sing N N 367 
THR   CG2 HG21 sing N N 368 
THR   CG2 HG22 sing N N 369 
THR   CG2 HG23 sing N N 370 
THR   OXT HXT  sing N N 371 
TRP   N   CA   sing N N 372 
TRP   N   H    sing N N 373 
TRP   N   H2   sing N N 374 
TRP   CA  C    sing N N 375 
TRP   CA  CB   sing N N 376 
TRP   CA  HA   sing N N 377 
TRP   C   O    doub N N 378 
TRP   C   OXT  sing N N 379 
TRP   CB  CG   sing N N 380 
TRP   CB  HB2  sing N N 381 
TRP   CB  HB3  sing N N 382 
TRP   CG  CD1  doub Y N 383 
TRP   CG  CD2  sing Y N 384 
TRP   CD1 NE1  sing Y N 385 
TRP   CD1 HD1  sing N N 386 
TRP   CD2 CE2  doub Y N 387 
TRP   CD2 CE3  sing Y N 388 
TRP   NE1 CE2  sing Y N 389 
TRP   NE1 HE1  sing N N 390 
TRP   CE2 CZ2  sing Y N 391 
TRP   CE3 CZ3  doub Y N 392 
TRP   CE3 HE3  sing N N 393 
TRP   CZ2 CH2  doub Y N 394 
TRP   CZ2 HZ2  sing N N 395 
TRP   CZ3 CH2  sing Y N 396 
TRP   CZ3 HZ3  sing N N 397 
TRP   CH2 HH2  sing N N 398 
TRP   OXT HXT  sing N N 399 
TYR   N   CA   sing N N 400 
TYR   N   H    sing N N 401 
TYR   N   H2   sing N N 402 
TYR   CA  C    sing N N 403 
TYR   CA  CB   sing N N 404 
TYR   CA  HA   sing N N 405 
TYR   C   O    doub N N 406 
TYR   C   OXT  sing N N 407 
TYR   CB  CG   sing N N 408 
TYR   CB  HB2  sing N N 409 
TYR   CB  HB3  sing N N 410 
TYR   CG  CD1  doub Y N 411 
TYR   CG  CD2  sing Y N 412 
TYR   CD1 CE1  sing Y N 413 
TYR   CD1 HD1  sing N N 414 
TYR   CD2 CE2  doub Y N 415 
TYR   CD2 HD2  sing N N 416 
TYR   CE1 CZ   doub Y N 417 
TYR   CE1 HE1  sing N N 418 
TYR   CE2 CZ   sing Y N 419 
TYR   CE2 HE2  sing N N 420 
TYR   CZ  OH   sing N N 421 
TYR   OH  HH   sing N N 422 
TYR   OXT HXT  sing N N 423 
VAL   N   CA   sing N N 424 
VAL   N   H    sing N N 425 
VAL   N   H2   sing N N 426 
VAL   CA  C    sing N N 427 
VAL   CA  CB   sing N N 428 
VAL   CA  HA   sing N N 429 
VAL   C   O    doub N N 430 
VAL   C   OXT  sing N N 431 
VAL   CB  CG1  sing N N 432 
VAL   CB  CG2  sing N N 433 
VAL   CB  HB   sing N N 434 
VAL   CG1 HG11 sing N N 435 
VAL   CG1 HG12 sing N N 436 
VAL   CG1 HG13 sing N N 437 
VAL   CG2 HG21 sing N N 438 
VAL   CG2 HG22 sing N N 439 
VAL   CG2 HG23 sing N N 440 
VAL   OXT HXT  sing N N 441 
# 
_pdbx_audit_support.funding_organization   'Innovative Medicines Initiative' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           875510 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2iwg 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9QBA 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014760 
_atom_sites.fract_transf_matrix[1][2]   0.008522 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017044 
_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]   0.014062 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
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   . VAL   A 1 1   ? -19.828 12.291 -16.370 1.00 34.93 ? 287 VAL   A N   1 
ATOM   2    C CA  . VAL   A 1 1   ? -21.135 12.877 -15.933 1.00 33.85 ? 287 VAL   A CA  1 
ATOM   3    C C   . VAL   A 1 1   ? -20.854 13.970 -14.903 1.00 32.46 ? 287 VAL   A C   1 
ATOM   4    O O   . VAL   A 1 1   ? -19.916 13.869 -14.108 1.00 35.66 ? 287 VAL   A O   1 
ATOM   5    C CB  . VAL   A 1 1   ? -22.106 11.811 -15.385 1.00 34.65 ? 287 VAL   A CB  1 
ATOM   6    C CG1 . VAL   A 1 1   ? -21.592 11.182 -14.098 1.00 35.05 ? 287 VAL   A CG1 1 
ATOM   7    C CG2 . VAL   A 1 1   ? -23.523 12.343 -15.197 1.00 35.33 ? 287 VAL   A CG2 1 
ATOM   8    N N   . HIS   A 1 2   ? -21.692 15.007 -14.934 1.00 28.19 ? 288 HIS   A N   1 
ATOM   9    C CA  . HIS   A 1 2   ? -21.649 16.130 -14.005 1.00 28.32 ? 288 HIS   A CA  1 
ATOM   10   C C   . HIS   A 1 2   ? -22.271 15.683 -12.678 1.00 26.07 ? 288 HIS   A C   1 
ATOM   11   O O   . HIS   A 1 2   ? -23.449 15.346 -12.636 1.00 28.65 ? 288 HIS   A O   1 
ATOM   12   C CB  . HIS   A 1 2   ? -22.407 17.263 -14.712 1.00 32.44 ? 288 HIS   A CB  1 
ATOM   13   C CG  . HIS   A 1 2   ? -22.530 18.612 -14.088 1.00 36.16 ? 288 HIS   A CG  1 
ATOM   14   N ND1 . HIS   A 1 2   ? -23.658 19.009 -13.396 1.00 37.86 ? 288 HIS   A ND1 1 
ATOM   15   C CD2 . HIS   A 1 2   ? -21.743 19.697 -14.171 1.00 37.18 ? 288 HIS   A CD2 1 
ATOM   16   C CE1 . HIS   A 1 2   ? -23.530 20.280 -13.043 1.00 37.25 ? 288 HIS   A CE1 1 
ATOM   17   N NE2 . HIS   A 1 2   ? -22.367 20.714 -13.495 1.00 37.81 ? 288 HIS   A NE2 1 
ATOM   18   N N   . ILE   A 1 3   ? -21.490 15.664 -11.592 1.00 21.59 ? 289 ILE   A N   1 
ATOM   19   C CA  . ILE   A 1 3   ? -22.015 15.240 -10.298 1.00 21.30 ? 289 ILE   A CA  1 
ATOM   20   C C   . ILE   A 1 3   ? -22.989 16.293 -9.777  1.00 19.76 ? 289 ILE   A C   1 
ATOM   21   O O   . ILE   A 1 3   ? -22.705 17.486 -9.817  1.00 21.35 ? 289 ILE   A O   1 
ATOM   22   C CB  . ILE   A 1 3   ? -20.896 14.979 -9.268  1.00 22.71 ? 289 ILE   A CB  1 
ATOM   23   C CG1 . ILE   A 1 3   ? -19.914 13.932 -9.752  1.00 24.55 ? 289 ILE   A CG1 1 
ATOM   24   C CG2 . ILE   A 1 3   ? -21.476 14.606 -7.901  1.00 23.68 ? 289 ILE   A CG2 1 
ATOM   25   C CD1 . ILE   A 1 3   ? -20.545 12.590 -10.062 1.00 26.24 ? 289 ILE   A CD1 1 
ATOM   26   N N   . THR   A 1 4   ? -24.118 15.828 -9.229  1.00 19.28 ? 290 THR   A N   1 
ATOM   27   C CA  . THR   A 1 4   ? -25.065 16.703 -8.570  1.00 19.72 ? 290 THR   A CA  1 
ATOM   28   C C   . THR   A 1 4   ? -25.462 16.037 -7.257  1.00 18.68 ? 290 THR   A C   1 
ATOM   29   O O   . THR   A 1 4   ? -25.403 14.814 -7.111  1.00 20.58 ? 290 THR   A O   1 
ATOM   30   C CB  . THR   A 1 4   ? -26.287 16.985 -9.446  1.00 21.65 ? 290 THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 4   ? -26.865 15.733 -9.807  1.00 24.27 ? 290 THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 4   ? -25.937 17.803 -10.676 1.00 22.82 ? 290 THR   A CG2 1 
ATOM   33   N N   . LEU   A 1 5   ? -25.878 16.865 -6.307  1.00 16.96 ? 291 LEU   A N   1 
ATOM   34   C CA  . LEU   A 1 5   ? -26.277 16.366 -5.003  1.00 17.07 ? 291 LEU   A CA  1 
ATOM   35   C C   . LEU   A 1 5   ? -27.746 15.970 -5.045  1.00 18.05 ? 291 LEU   A C   1 
ATOM   36   O O   . LEU   A 1 5   ? -28.554 16.585 -5.737  1.00 20.46 ? 291 LEU   A O   1 
ATOM   37   C CB  . LEU   A 1 5   ? -25.998 17.439 -3.956  1.00 17.78 ? 291 LEU   A CB  1 
ATOM   38   C CG  . LEU   A 1 5   ? -24.542 17.887 -3.856  1.00 18.16 ? 291 LEU   A CG  1 
ATOM   39   C CD1 . LEU   A 1 5   ? -24.387 19.006 -2.841  1.00 18.72 ? 291 LEU   A CD1 1 
ATOM   40   C CD2 . LEU   A 1 5   ? -23.683 16.692 -3.474  1.00 18.35 ? 291 LEU   A CD2 1 
ATOM   41   N N   . ASP   A 1 6   ? -28.081 14.937 -4.279  1.00 17.89 ? 292 ASP   A N   1 
ATOM   42   C CA  . ASP   A 1 6   ? -29.410 14.355 -4.269  1.00 18.39 ? 292 ASP   A CA  1 
ATOM   43   C C   . ASP   A 1 6   ? -30.169 14.876 -3.048  1.00 18.26 ? 292 ASP   A C   1 
ATOM   44   O O   . ASP   A 1 6   ? -29.915 14.453 -1.914  1.00 17.39 ? 292 ASP   A O   1 
ATOM   45   C CB  . ASP   A 1 6   ? -29.303 12.843 -4.289  1.00 20.00 ? 292 ASP   A CB  1 
ATOM   46   C CG  . ASP   A 1 6   ? -30.623 12.093 -4.247  1.00 22.16 ? 292 ASP   A CG  1 
ATOM   47   O OD1 . ASP   A 1 6   ? -31.653 12.714 -3.886  1.00 23.82 ? 292 ASP   A OD1 1 
ATOM   48   O OD2 . ASP   A 1 6   ? -30.599 10.893 -4.563  1.00 23.62 ? 292 ASP   A OD2 1 
ATOM   49   N N   . PRO   A 1 7   ? -31.130 15.807 -3.237  1.00 18.96 ? 293 PRO   A N   1 
ATOM   50   C CA  . PRO   A 1 7   ? -31.789 16.440 -2.101  1.00 19.95 ? 293 PRO   A CA  1 
ATOM   51   C C   . PRO   A 1 7   ? -32.543 15.462 -1.207  1.00 19.79 ? 293 PRO   A C   1 
ATOM   52   O O   . PRO   A 1 7   ? -32.690 15.727 -0.016  1.00 21.31 ? 293 PRO   A O   1 
ATOM   53   C CB  . PRO   A 1 7   ? -32.704 17.488 -2.717  1.00 21.66 ? 293 PRO   A CB  1 
ATOM   54   C CG  . PRO   A 1 7   ? -32.244 17.609 -4.142  1.00 22.29 ? 293 PRO   A CG  1 
ATOM   55   C CD  . PRO   A 1 7   ? -31.591 16.335 -4.533  1.00 20.21 ? 293 PRO   A CD  1 
ATOM   56   N N   . ASP   A 1 8   ? -33.009 14.337 -1.763  1.00 18.34 ? 294 ASP   A N   1 
ATOM   57   C CA  . ASP   A 1 8   ? -33.788 13.401 -0.965  1.00 19.90 ? 294 ASP   A CA  1 
ATOM   58   C C   . ASP   A 1 8   ? -32.907 12.676 0.051   1.00 18.92 ? 294 ASP   A C   1 
ATOM   59   O O   . ASP   A 1 8   ? -33.432 12.074 0.981   1.00 20.74 ? 294 ASP   A O   1 
ATOM   60   C CB  . ASP   A 1 8   ? -34.531 12.395 -1.826  1.00 21.79 ? 294 ASP   A CB  1 
ATOM   61   C CG  . ASP   A 1 8   ? -35.646 12.960 -2.695  1.00 26.49 ? 294 ASP   A CG  1 
ATOM   62   O OD1 . ASP   A 1 8   ? -36.094 14.091 -2.429  1.00 29.87 ? 294 ASP   A OD1 1 
ATOM   63   O OD2 . ASP   A 1 8   ? -36.031 12.272 -3.658  1.00 32.47 ? 294 ASP   A OD2 1 
ATOM   64   N N   . THR   A 1 9   ? -31.579 12.718 -0.128  1.00 17.66 ? 295 THR   A N   1 
ATOM   65   C CA  . THR   A 1 9   ? -30.661 12.073 0.797   1.00 17.55 ? 295 THR   A CA  1 
ATOM   66   C C   . THR   A 1 9   ? -30.188 13.031 1.888   1.00 17.29 ? 295 THR   A C   1 
ATOM   67   O O   . THR   A 1 9   ? -29.625 12.569 2.876   1.00 17.01 ? 295 THR   A O   1 
ATOM   68   C CB  . THR   A 1 9   ? -29.450 11.480 0.075   1.00 17.07 ? 295 THR   A CB  1 
ATOM   69   O OG1 . THR   A 1 9   ? -28.630 12.528 -0.445  1.00 17.04 ? 295 THR   A OG1 1 
ATOM   70   C CG2 . THR   A 1 9   ? -29.876 10.517 -1.020  1.00 18.05 ? 295 THR   A CG2 1 
ATOM   71   N N   . ALA   A 1 10  ? -30.363 14.340 1.696   1.00 17.50 ? 296 ALA   A N   1 
ATOM   72   C CA  . ALA   A 1 10  ? -29.662 15.329 2.503   1.00 17.21 ? 296 ALA   A CA  1 
ATOM   73   C C   . ALA   A 1 10  ? -30.306 15.487 3.877   1.00 17.95 ? 296 ALA   A C   1 
ATOM   74   O O   . ALA   A 1 10  ? -31.485 15.805 3.997   1.00 19.49 ? 296 ALA   A O   1 
ATOM   75   C CB  . ALA   A 1 10  ? -29.639 16.651 1.774   1.00 17.81 ? 296 ALA   A CB  1 
ATOM   76   N N   . ASN   A 1 11  ? -29.487 15.303 4.920   1.00 17.32 ? 297 ASN   A N   1 
ATOM   77   C CA  . ASN   A 1 11  ? -29.910 15.545 6.292   1.00 17.58 ? 297 ASN   A CA  1 
ATOM   78   C C   . ASN   A 1 11  ? -30.471 16.959 6.455   1.00 18.56 ? 297 ASN   A C   1 
ATOM   79   O O   . ASN   A 1 11  ? -30.027 17.888 5.787   1.00 19.31 ? 297 ASN   A O   1 
ATOM   80   C CB  . ASN   A 1 11  ? -28.719 15.349 7.222   1.00 17.02 ? 297 ASN   A CB  1 
ATOM   81   C CG  . ASN   A 1 11  ? -28.997 15.676 8.667   1.00 17.72 ? 297 ASN   A CG  1 
ATOM   82   O OD1 . ASN   A 1 11  ? -28.679 16.784 9.112   1.00 19.94 ? 297 ASN   A OD1 1 
ATOM   83   N ND2 . ASN   A 1 11  ? -29.518 14.713 9.409   1.00 17.75 ? 297 ASN   A ND2 1 
ATOM   84   N N   . PRO   A 1 12  ? -31.448 17.192 7.365   1.00 20.62 ? 298 PRO   A N   1 
ATOM   85   C CA  . PRO   A 1 12  ? -32.007 18.536 7.551   1.00 21.77 ? 298 PRO   A CA  1 
ATOM   86   C C   . PRO   A 1 12  ? -31.061 19.645 8.030   1.00 20.71 ? 298 PRO   A C   1 
ATOM   87   O O   . PRO   A 1 12  ? -31.413 20.817 7.918   1.00 23.15 ? 298 PRO   A O   1 
ATOM   88   C CB  . PRO   A 1 12  ? -33.116 18.317 8.582   1.00 23.41 ? 298 PRO   A CB  1 
ATOM   89   C CG  . PRO   A 1 12  ? -33.458 16.843 8.464   1.00 23.20 ? 298 PRO   A CG  1 
ATOM   90   C CD  . PRO   A 1 12  ? -32.163 16.165 8.150   1.00 21.91 ? 298 PRO   A CD  1 
ATOM   91   N N   . TRP   A 1 13  ? -29.880 19.314 8.576   1.00 21.16 ? 299 TRP   A N   1 
ATOM   92   C CA  . TRP   A 1 13  ? -28.887 20.329 8.909   1.00 21.15 ? 299 TRP   A CA  1 
ATOM   93   C C   . TRP   A 1 13  ? -28.259 20.945 7.658   1.00 20.17 ? 299 TRP   A C   1 
ATOM   94   O O   . TRP   A 1 13  ? -27.458 21.864 7.800   1.00 21.06 ? 299 TRP   A O   1 
ATOM   95   C CB  . TRP   A 1 13  ? -27.768 19.775 9.808   1.00 22.96 ? 299 TRP   A CB  1 
ATOM   96   C CG  . TRP   A 1 13  ? -28.049 19.854 11.281  1.00 24.95 ? 299 TRP   A CG  1 
ATOM   97   C CD1 . TRP   A 1 13  ? -28.351 18.822 12.114  1.00 26.47 ? 299 TRP   A CD1 1 
ATOM   98   C CD2 . TRP   A 1 13  ? -28.033 21.048 12.090  1.00 26.78 ? 299 TRP   A CD2 1 
ATOM   99   N NE1 . TRP   A 1 13  ? -28.544 19.291 13.385  1.00 26.73 ? 299 TRP   A NE1 1 
ATOM   100  C CE2 . TRP   A 1 13  ? -28.352 20.649 13.404  1.00 27.47 ? 299 TRP   A CE2 1 
ATOM   101  C CE3 . TRP   A 1 13  ? -27.786 22.400 11.829  1.00 27.40 ? 299 TRP   A CE3 1 
ATOM   102  C CZ2 . TRP   A 1 13  ? -28.432 21.562 14.454  1.00 28.23 ? 299 TRP   A CZ2 1 
ATOM   103  C CZ3 . TRP   A 1 13  ? -27.871 23.302 12.865  1.00 27.96 ? 299 TRP   A CZ3 1 
ATOM   104  C CH2 . TRP   A 1 13  ? -28.188 22.886 14.157  1.00 27.97 ? 299 TRP   A CH2 1 
ATOM   105  N N   . LEU   A 1 14  ? -28.565 20.402 6.466   1.00 18.42 ? 300 LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 14  ? -27.913 20.822 5.235   1.00 17.38 ? 300 LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 14  ? -28.798 21.753 4.415   1.00 16.89 ? 300 LEU   A C   1 
ATOM   108  O O   . LEU   A 1 14  ? -30.005 21.566 4.310   1.00 20.31 ? 300 LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 14  ? -27.530 19.598 4.406   1.00 16.30 ? 300 LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 14  ? -26.624 18.587 5.114   1.00 16.85 ? 300 LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 14  ? -26.349 17.426 4.196   1.00 17.08 ? 300 LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 14  ? -25.331 19.211 5.569   1.00 17.74 ? 300 LEU   A CD2 1 
ATOM   113  N N   . ILE   A 1 15  ? -28.120 22.705 3.779   1.00 16.22 ? 301 ILE   A N   1 
ATOM   114  C CA  . ILE   A 1 15  ? -28.671 23.575 2.753   1.00 15.70 ? 301 ILE   A CA  1 
ATOM   115  C C   . ILE   A 1 15  ? -27.991 23.241 1.428   1.00 15.62 ? 301 ILE   A C   1 
ATOM   116  O O   . ILE   A 1 15  ? -26.767 23.232 1.370   1.00 16.33 ? 301 ILE   A O   1 
ATOM   117  C CB  . ILE   A 1 15  ? -28.409 25.042 3.115   1.00 16.59 ? 301 ILE   A CB  1 
ATOM   118  C CG1 . ILE   A 1 15  ? -29.053 25.418 4.464   1.00 17.27 ? 301 ILE   A CG1 1 
ATOM   119  C CG2 . ILE   A 1 15  ? -28.842 25.961 1.972   1.00 17.38 ? 301 ILE   A CG2 1 
ATOM   120  C CD1 . ILE   A 1 15  ? -28.687 26.807 4.970   1.00 18.45 ? 301 ILE   A CD1 1 
ATOM   121  N N   . LEU   A 1 16  ? -28.798 22.989 0.391   1.00 16.68 ? 302 LEU   A N   1 
ATOM   122  C CA  . LEU   A 1 16  ? -28.292 22.702 -0.942  1.00 17.29 ? 302 LEU   A CA  1 
ATOM   123  C C   . LEU   A 1 16  ? -28.583 23.905 -1.834  1.00 17.09 ? 302 LEU   A C   1 
ATOM   124  O O   . LEU   A 1 16  ? -29.628 24.530 -1.723  1.00 17.97 ? 302 LEU   A O   1 
ATOM   125  C CB  . LEU   A 1 16  ? -28.927 21.453 -1.550  1.00 19.71 ? 302 LEU   A CB  1 
ATOM   126  C CG  . LEU   A 1 16  ? -28.336 20.099 -1.140  1.00 22.18 ? 302 LEU   A CG  1 
ATOM   127  C CD1 . LEU   A 1 16  ? -28.447 19.793 0.334   1.00 22.93 ? 302 LEU   A CD1 1 
ATOM   128  C CD2 . LEU   A 1 16  ? -29.017 19.009 -1.948  1.00 22.94 ? 302 LEU   A CD2 1 
ATOM   129  N N   . SER   A 1 17  ? -27.661 24.199 -2.747  1.00 17.17 ? 303 SER   A N   1 
ATOM   130  C CA  . SER   A 1 17  ? -27.904 25.231 -3.740  1.00 17.47 ? 303 SER   A CA  1 
ATOM   131  C C   . SER   A 1 17  ? -28.907 24.748 -4.793  1.00 17.55 ? 303 SER   A C   1 
ATOM   132  O O   . SER   A 1 17  ? -29.121 23.556 -4.977  1.00 17.53 ? 303 SER   A O   1 
ATOM   133  C CB  . SER   A 1 17  ? -26.616 25.672 -4.363  1.00 17.75 ? 303 SER   A CB  1 
ATOM   134  O OG  . SER   A 1 17  ? -25.999 24.590 -5.046  1.00 17.38 ? 303 SER   A OG  1 
ATOM   135  N N   . GLU   A 1 18  ? -29.485 25.705 -5.518  1.00 18.84 ? 304 GLU   A N   1 
ATOM   136  C CA  . GLU   A 1 18  ? -30.469 25.420 -6.553  1.00 21.22 ? 304 GLU   A CA  1 
ATOM   137  C C   . GLU   A 1 18  ? -29.892 24.485 -7.618  1.00 19.70 ? 304 GLU   A C   1 
ATOM   138  O O   . GLU   A 1 18  ? -30.600 23.599 -8.102  1.00 21.15 ? 304 GLU   A O   1 
ATOM   139  C CB  . GLU   A 1 18  ? -30.945 26.732 -7.181  1.00 23.39 ? 304 GLU   A CB  1 
ATOM   140  C CG  . GLU   A 1 18  ? -31.820 26.560 -8.419  1.00 26.15 ? 304 GLU   A CG  1 
ATOM   141  C CD  . GLU   A 1 18  ? -33.122 25.818 -8.204  1.00 28.42 ? 304 GLU   A CD  1 
ATOM   142  O OE1 . GLU   A 1 18  ? -33.558 25.706 -7.047  1.00 32.03 ? 304 GLU   A OE1 1 
ATOM   143  O OE2 . GLU   A 1 18  ? -33.673 25.302 -9.198  1.00 32.60 ? 304 GLU   A OE2 1 
ATOM   144  N N   . ASP   A 1 19  ? -28.621 24.702 -7.994  1.00 18.13 ? 305 ASP   A N   1 
ATOM   145  C CA  . ASP   A 1 19  ? -27.966 23.893 -9.014  1.00 17.69 ? 305 ASP   A CA  1 
ATOM   146  C C   . ASP   A 1 19  ? -27.462 22.563 -8.455  1.00 17.58 ? 305 ASP   A C   1 
ATOM   147  O O   . ASP   A 1 19  ? -26.910 21.756 -9.194  1.00 17.59 ? 305 ASP   A O   1 
ATOM   148  C CB  . ASP   A 1 19  ? -26.853 24.652 -9.720  1.00 17.62 ? 305 ASP   A CB  1 
ATOM   149  C CG  . ASP   A 1 19  ? -25.590 24.974 -8.937  1.00 18.23 ? 305 ASP   A CG  1 
ATOM   150  O OD1 . ASP   A 1 19  ? -25.501 24.582 -7.765  1.00 17.22 ? 305 ASP   A OD1 1 
ATOM   151  O OD2 . ASP   A 1 19  ? -24.678 25.600 -9.533  1.00 20.37 ? 305 ASP   A OD2 1 
ATOM   152  N N   . ARG   A 1 20  ? -27.623 22.340 -7.142  1.00 17.12 ? 306 ARG   A N   1 
ATOM   153  C CA  . ARG   A 1 20  ? -27.300 21.066 -6.522  1.00 17.43 ? 306 ARG   A CA  1 
ATOM   154  C C   . ARG   A 1 20  ? -25.808 20.762 -6.650  1.00 15.95 ? 306 ARG   A C   1 
ATOM   155  O O   . ARG   A 1 20  ? -25.422 19.593 -6.681  1.00 16.58 ? 306 ARG   A O   1 
ATOM   156  C CB  . ARG   A 1 20  ? -28.188 19.953 -7.095  1.00 19.00 ? 306 ARG   A CB  1 
ATOM   157  C CG  . ARG   A 1 20  ? -29.662 20.207 -6.830  1.00 21.00 ? 306 ARG   A CG  1 
ATOM   158  C CD  . ARG   A 1 20  ? -30.489 19.077 -7.378  1.00 23.20 ? 306 ARG   A CD  1 
ATOM   159  N NE  . ARG   A 1 20  ? -31.921 19.374 -7.271  1.00 24.53 ? 306 ARG   A NE  1 
ATOM   160  C CZ  . ARG   A 1 20  ? -32.883 18.490 -7.487  1.00 25.39 ? 306 ARG   A CZ  1 
ATOM   161  N NH1 . ARG   A 1 20  ? -32.595 17.253 -7.850  1.00 26.65 ? 306 ARG   A NH1 1 
ATOM   162  N NH2 . ARG   A 1 20  ? -34.140 18.845 -7.330  1.00 28.66 ? 306 ARG   A NH2 1 
ATOM   163  N N   . ARG   A 1 21  ? -24.978 21.817 -6.706  1.00 15.19 ? 307 ARG   A N   1 
ATOM   164  C CA  . ARG   A 1 21  ? -23.531 21.658 -6.756  1.00 15.20 ? 307 ARG   A CA  1 
ATOM   165  C C   . ARG   A 1 21  ? -22.875 22.095 -5.452  1.00 15.10 ? 307 ARG   A C   1 
ATOM   166  O O   . ARG   A 1 21  ? -21.669 21.933 -5.312  1.00 15.93 ? 307 ARG   A O   1 
ATOM   167  C CB  . ARG   A 1 21  ? -22.939 22.485 -7.901  1.00 16.11 ? 307 ARG   A CB  1 
ATOM   168  C CG  . ARG   A 1 21  ? -23.448 21.964 -9.231  1.00 17.78 ? 307 ARG   A CG  1 
ATOM   169  C CD  . ARG   A 1 21  ? -22.671 20.753 -9.726  1.00 18.45 ? 307 ARG   A CD  1 
ATOM   170  N NE  . ARG   A 1 21  ? -21.362 21.142 -10.254 1.00 18.94 ? 307 ARG   A NE  1 
ATOM   171  C CZ  . ARG   A 1 21  ? -20.431 20.326 -10.749 1.00 18.96 ? 307 ARG   A CZ  1 
ATOM   172  N NH1 . ARG   A 1 21  ? -20.623 19.025 -10.781 1.00 19.27 ? 307 ARG   A NH1 1 
ATOM   173  N NH2 . ARG   A 1 21  ? -19.288 20.818 -11.192 1.00 19.84 ? 307 ARG   A NH2 1 
ATOM   174  N N   . GLN   A 1 22  ? -23.665 22.623 -4.505  1.00 14.27 ? 308 GLN   A N   1 
ATOM   175  C CA  . GLN   A 1 22  ? -23.110 23.129 -3.258  1.00 14.78 ? 308 GLN   A CA  1 
ATOM   176  C C   . GLN   A 1 22  ? -23.954 22.664 -2.080  1.00 13.98 ? 308 GLN   A C   1 
ATOM   177  O O   . GLN   A 1 22  ? -25.174 22.567 -2.176  1.00 15.18 ? 308 GLN   A O   1 
ATOM   178  C CB  . GLN   A 1 22  ? -23.106 24.651 -3.246  1.00 15.81 ? 308 GLN   A CB  1 
ATOM   179  C CG  . GLN   A 1 22  ? -22.363 25.262 -2.069  1.00 17.10 ? 308 GLN   A CG  1 
ATOM   180  C CD  . GLN   A 1 22  ? -22.331 26.765 -2.191  1.00 18.44 ? 308 GLN   A CD  1 
ATOM   181  O OE1 . GLN   A 1 22  ? -23.310 27.447 -1.865  1.00 21.49 ? 308 GLN   A OE1 1 
ATOM   182  N NE2 . GLN   A 1 22  ? -21.230 27.284 -2.716  1.00 17.85 ? 308 GLN   A NE2 1 
ATOM   183  N N   . VAL   A 1 23  ? -23.266 22.373 -0.972  1.00 13.94 ? 309 VAL   A N   1 
ATOM   184  C CA  . VAL   A 1 23  ? -23.943 22.028 0.268   1.00 14.20 ? 309 VAL   A CA  1 
ATOM   185  C C   . VAL   A 1 23  ? -23.210 22.686 1.434   1.00 14.30 ? 309 VAL   A C   1 
ATOM   186  O O   . VAL   A 1 23  ? -21.985 22.829 1.435   1.00 14.39 ? 309 VAL   A O   1 
ATOM   187  C CB  . VAL   A 1 23  ? -24.033 20.502 0.442   1.00 15.25 ? 309 VAL   A CB  1 
ATOM   188  C CG1 . VAL   A 1 23  ? -22.651 19.856 0.419   1.00 15.49 ? 309 VAL   A CG1 1 
ATOM   189  C CG2 . VAL   A 1 23  ? -24.821 20.104 1.687   1.00 15.64 ? 309 VAL   A CG2 1 
ATOM   190  N N   . ARG   A 1 24  ? -23.992 23.079 2.435   1.00 14.38 ? 310 ARG   A N   1 
ATOM   191  C CA  . ARG   A 1 24  ? -23.425 23.719 3.607   1.00 14.68 ? 310 ARG   A CA  1 
ATOM   192  C C   . ARG   A 1 24  ? -24.341 23.479 4.800   1.00 15.04 ? 310 ARG   A C   1 
ATOM   193  O O   . ARG   A 1 24  ? -25.495 23.104 4.656   1.00 16.10 ? 310 ARG   A O   1 
ATOM   194  C CB  . ARG   A 1 24  ? -23.219 25.213 3.357   1.00 15.27 ? 310 ARG   A CB  1 
ATOM   195  C CG  . ARG   A 1 24  ? -24.512 25.987 3.163   1.00 15.90 ? 310 ARG   A CG  1 
ATOM   196  C CD  . ARG   A 1 24  ? -24.213 27.351 2.585   1.00 17.97 ? 310 ARG   A CD  1 
ATOM   197  N NE  . ARG   A 1 24  ? -25.405 28.140 2.270   1.00 18.93 ? 310 ARG   A NE  1 
ATOM   198  C CZ  . ARG   A 1 24  ? -26.053 28.912 3.121   1.00 20.23 ? 310 ARG   A CZ  1 
ATOM   199  N NH1 . ARG   A 1 24  ? -25.620 29.042 4.365   1.00 21.36 ? 310 ARG   A NH1 1 
ATOM   200  N NH2 . ARG   A 1 24  ? -27.112 29.576 2.702   1.00 21.59 ? 310 ARG   A NH2 1 
ATOM   201  N N   . LEU   A 1 25  ? -23.790 23.715 5.988   1.00 15.59 ? 311 LEU   A N   1 
ATOM   202  C CA  . LEU   A 1 25  ? -24.545 23.614 7.222   1.00 16.48 ? 311 LEU   A CA  1 
ATOM   203  C C   . LEU   A 1 25  ? -25.430 24.838 7.397   1.00 17.50 ? 311 LEU   A C   1 
ATOM   204  O O   . LEU   A 1 25  ? -24.955 25.970 7.331   1.00 18.70 ? 311 LEU   A O   1 
ATOM   205  C CB  . LEU   A 1 25  ? -23.580 23.545 8.402   1.00 16.83 ? 311 LEU   A CB  1 
ATOM   206  C CG  . LEU   A 1 25  ? -22.708 22.293 8.534   1.00 19.09 ? 311 LEU   A CG  1 
ATOM   207  C CD1 . LEU   A 1 25  ? -21.652 22.386 9.612   1.00 18.73 ? 311 LEU   A CD1 1 
ATOM   208  C CD2 . LEU   A 1 25  ? -23.555 21.048 8.754   1.00 20.22 ? 311 LEU   A CD2 1 
ATOM   209  N N   . GLY   A 1 26  ? -26.676 24.553 7.786   1.00 18.43 ? 312 GLY   A N   1 
ATOM   210  C CA  . GLY   A 1 26  ? -27.569 25.593 8.256   1.00 21.11 ? 312 GLY   A CA  1 
ATOM   211  C C   . GLY   A 1 26  ? -27.281 25.956 9.713   1.00 23.68 ? 312 GLY   A C   1 
ATOM   212  O O   . GLY   A 1 26  ? -26.452 25.329 10.375  1.00 24.90 ? 312 GLY   A O   1 
ATOM   213  N N   . ASP   A 1 27  ? -27.965 27.003 10.185  1.00 26.78 ? 313 ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 27  ? -27.878 27.440 11.571  1.00 28.29 ? 313 ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 27  ? -28.918 26.696 12.403  1.00 29.64 ? 313 ASP   A C   1 
ATOM   216  O O   . ASP   A 1 27  ? -28.767 26.568 13.618  1.00 31.35 ? 313 ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 27  ? -28.074 28.942 11.677  1.00 31.43 ? 313 ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 27  ? -27.025 29.792 10.974  1.00 34.31 ? 313 ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 27  ? -25.876 29.317 10.827  1.00 37.74 ? 313 ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 27  ? -27.372 30.923 10.573  1.00 39.43 ? 313 ASP   A OD2 1 
ATOM   221  N N   . THR   A 1 28  ? -29.985 26.235 11.738  1.00 28.32 ? 314 THR   A N   1 
ATOM   222  C CA  . THR   A 1 28  ? -30.936 25.308 12.330  1.00 29.54 ? 314 THR   A CA  1 
ATOM   223  C C   . THR   A 1 28  ? -31.268 24.235 11.298  1.00 29.24 ? 314 THR   A C   1 
ATOM   224  O O   . THR   A 1 28  ? -30.927 24.356 10.120  1.00 28.72 ? 314 THR   A O   1 
ATOM   225  C CB  . THR   A 1 28  ? -32.207 26.027 12.781  1.00 31.36 ? 314 THR   A CB  1 
ATOM   226  O OG1 . THR   A 1 28  ? -32.832 26.494 11.590  1.00 33.11 ? 314 THR   A OG1 1 
ATOM   227  C CG2 . THR   A 1 28  ? -31.939 27.177 13.734  1.00 32.65 ? 314 THR   A CG2 1 
ATOM   228  N N   . GLN   A 1 29  ? -31.944 23.187 11.768  1.00 27.76 ? 315 GLN   A N   1 
ATOM   229  C CA  . GLN   A 1 29  ? -32.427 22.124 10.907  1.00 28.25 ? 315 GLN   A CA  1 
ATOM   230  C C   . GLN   A 1 29  ? -33.661 22.607 10.157  1.00 28.37 ? 315 GLN   A C   1 
ATOM   231  O O   . GLN   A 1 29  ? -34.542 23.229 10.742  1.00 31.22 ? 315 GLN   A O   1 
ATOM   232  C CB  . GLN   A 1 29  ? -32.777 20.876 11.718  1.00 29.06 ? 315 GLN   A CB  1 
ATOM   233  C CG  . GLN   A 1 29  ? -31.557 20.233 12.366  1.00 30.94 ? 315 GLN   A CG  1 
ATOM   234  C CD  . GLN   A 1 29  ? -31.873 18.948 13.092  1.00 33.26 ? 315 GLN   A CD  1 
ATOM   235  O OE1 . GLN   A 1 29  ? -31.894 18.898 14.329  1.00 37.09 ? 315 GLN   A OE1 1 
ATOM   236  N NE2 . GLN   A 1 29  ? -32.132 17.900 12.324  1.00 35.73 ? 315 GLN   A NE2 1 
ATOM   237  N N   . GLN   A 1 30  ? -33.700 22.320 8.854   1.00 28.56 ? 316 GLN   A N   1 
ATOM   238  C CA  . GLN   A 1 30  ? -34.896 22.518 8.057   1.00 29.10 ? 316 GLN   A CA  1 
ATOM   239  C C   . GLN   A 1 30  ? -35.951 21.491 8.450   1.00 29.89 ? 316 GLN   A C   1 
ATOM   240  O O   . GLN   A 1 30  ? -35.627 20.387 8.882   1.00 32.01 ? 316 GLN   A O   1 
ATOM   241  C CB  . GLN   A 1 30  ? -34.635 22.302 6.567   1.00 29.03 ? 316 GLN   A CB  1 
ATOM   242  C CG  . GLN   A 1 30  ? -33.632 23.273 5.960   1.00 30.14 ? 316 GLN   A CG  1 
ATOM   243  C CD  . GLN   A 1 30  ? -33.563 23.162 4.455   1.00 30.25 ? 316 GLN   A CD  1 
ATOM   244  O OE1 . GLN   A 1 30  ? -34.555 23.378 3.746   1.00 33.13 ? 316 GLN   A OE1 1 
ATOM   245  N NE2 . GLN   A 1 30  ? -32.384 22.838 3.950   1.00 29.42 ? 316 GLN   A NE2 1 
ATOM   246  N N   . SER   A 1 31  ? -37.215 21.868 8.256   1.00 32.10 ? 317 SER   A N   1 
ATOM   247  C CA  . SER   A 1 31  ? -38.339 20.962 8.408   1.00 33.55 ? 317 SER   A CA  1 
ATOM   248  C C   . SER   A 1 31  ? -38.673 20.368 7.041   1.00 34.91 ? 317 SER   A C   1 
ATOM   249  O O   . SER   A 1 31  ? -39.259 21.046 6.200   1.00 36.60 ? 317 SER   A O   1 
ATOM   250  C CB  . SER   A 1 31  ? -39.515 21.690 9.009   1.00 34.79 ? 317 SER   A CB  1 
ATOM   251  O OG  . SER   A 1 31  ? -40.605 20.806 9.225   1.00 38.03 ? 317 SER   A OG  1 
ATOM   252  N N   . ILE   A 1 32  ? -38.262 19.110 6.821   1.00 34.98 ? 318 ILE   A N   1 
ATOM   253  C CA  . ILE   A 1 32  ? -38.423 18.437 5.538   1.00 33.57 ? 318 ILE   A CA  1 
ATOM   254  C C   . ILE   A 1 32  ? -38.893 17.003 5.801   1.00 34.44 ? 318 ILE   A C   1 
ATOM   255  O O   . ILE   A 1 32  ? -38.842 16.535 6.941   1.00 34.60 ? 318 ILE   A O   1 
ATOM   256  C CB  . ILE   A 1 32  ? -37.109 18.513 4.727   1.00 32.51 ? 318 ILE   A CB  1 
ATOM   257  C CG1 . ILE   A 1 32  ? -35.909 17.953 5.507   1.00 32.39 ? 318 ILE   A CG1 1 
ATOM   258  C CG2 . ILE   A 1 32  ? -36.844 19.946 4.258   1.00 32.39 ? 318 ILE   A CG2 1 
ATOM   259  C CD1 . ILE   A 1 32  ? -34.577 18.073 4.780   1.00 32.26 ? 318 ILE   A CD1 1 
ATOM   260  N N   . PRO   A 1 33  ? -39.399 16.266 4.780   1.00 34.99 ? 319 PRO   A N   1 
ATOM   261  C CA  . PRO   A 1 33  ? -39.842 14.883 4.962   1.00 34.86 ? 319 PRO   A CA  1 
ATOM   262  C C   . PRO   A 1 33  ? -38.822 13.965 5.638   1.00 34.93 ? 319 PRO   A C   1 
ATOM   263  O O   . PRO   A 1 33  ? -37.617 14.218 5.583   1.00 36.07 ? 319 PRO   A O   1 
ATOM   264  C CB  . PRO   A 1 33  ? -40.140 14.427 3.534   1.00 34.69 ? 319 PRO   A CB  1 
ATOM   265  C CG  . PRO   A 1 33  ? -40.606 15.719 2.888   1.00 34.72 ? 319 PRO   A CG  1 
ATOM   266  C CD  . PRO   A 1 33  ? -39.653 16.750 3.413   1.00 34.73 ? 319 PRO   A CD  1 
ATOM   267  N N   . GLY   A 1 34  ? -39.328 12.891 6.263   1.00 35.24 ? 320 GLY   A N   1 
ATOM   268  C CA  . GLY   A 1 34  ? -38.499 11.864 6.878   1.00 34.51 ? 320 GLY   A CA  1 
ATOM   269  C C   . GLY   A 1 34  ? -38.478 10.592 6.033   1.00 34.14 ? 320 GLY   A C   1 
ATOM   270  O O   . GLY   A 1 34  ? -38.612 9.482  6.554   1.00 33.72 ? 320 GLY   A O   1 
ATOM   271  N N   . ASN   A 1 35  ? -38.311 10.792 4.720   1.00 31.82 ? 321 ASN   A N   1 
ATOM   272  C CA  . ASN   A 1 35  ? -38.291 9.726  3.732   1.00 31.21 ? 321 ASN   A CA  1 
ATOM   273  C C   . ASN   A 1 35  ? -37.062 8.838  3.906   1.00 29.11 ? 321 ASN   A C   1 
ATOM   274  O O   . ASN   A 1 35  ? -36.040 9.265  4.450   1.00 27.83 ? 321 ASN   A O   1 
ATOM   275  C CB  . ASN   A 1 35  ? -38.323 10.291 2.318   1.00 32.25 ? 321 ASN   A CB  1 
ATOM   276  C CG  . ASN   A 1 35  ? -37.168 11.228 2.063   1.00 33.76 ? 321 ASN   A CG  1 
ATOM   277  O OD1 . ASN   A 1 35  ? -37.044 12.258 2.739   1.00 35.17 ? 321 ASN   A OD1 1 
ATOM   278  N ND2 . ASN   A 1 35  ? -36.311 10.885 1.117   1.00 33.76 ? 321 ASN   A ND2 1 
ATOM   279  N N   . GLU   A 1 36  ? -37.180 7.615  3.375   1.00 28.53 ? 322 GLU   A N   1 
ATOM   280  C CA  . GLU   A 1 36  ? -36.290 6.502  3.668   1.00 30.82 ? 322 GLU   A CA  1 
ATOM   281  C C   . GLU   A 1 36  ? -34.841 6.790  3.270   1.00 27.53 ? 322 GLU   A C   1 
ATOM   282  O O   . GLU   A 1 36  ? -33.923 6.312  3.928   1.00 28.61 ? 322 GLU   A O   1 
ATOM   283  C CB  . GLU   A 1 36  ? -36.838 5.235  3.004   1.00 34.61 ? 322 GLU   A CB  1 
ATOM   284  C CG  . GLU   A 1 36  ? -36.887 5.282  1.479   1.00 38.13 ? 322 GLU   A CG  1 
ATOM   285  C CD  . GLU   A 1 36  ? -35.700 4.652  0.775   1.00 42.38 ? 322 GLU   A CD  1 
ATOM   286  O OE1 . GLU   A 1 36  ? -35.806 4.433  -0.452  1.00 46.55 ? 322 GLU   A OE1 1 
ATOM   287  O OE2 . GLU   A 1 36  ? -34.674 4.389  1.447   1.00 45.43 ? 322 GLU   A OE2 1 
ATOM   288  N N   . GLU   A 1 37  ? -34.631 7.575  2.209   1.00 24.88 ? 323 GLU   A N   1 
ATOM   289  C CA  . GLU   A 1 37  ? -33.296 7.802  1.683   1.00 24.40 ? 323 GLU   A CA  1 
ATOM   290  C C   . GLU   A 1 37  ? -32.488 8.780  2.539   1.00 20.37 ? 323 GLU   A C   1 
ATOM   291  O O   . GLU   A 1 37  ? -31.272 8.836  2.386   1.00 21.74 ? 323 GLU   A O   1 
ATOM   292  C CB  . GLU   A 1 37  ? -33.375 8.343  0.252   1.00 25.65 ? 323 GLU   A CB  1 
ATOM   293  C CG  . GLU   A 1 37  ? -33.908 7.327  -0.758  1.00 28.10 ? 323 GLU   A CG  1 
ATOM   294  C CD  . GLU   A 1 37  ? -34.115 7.828  -2.176  1.00 31.16 ? 323 GLU   A CD  1 
ATOM   295  O OE1 . GLU   A 1 37  ? -33.966 9.047  -2.415  1.00 35.67 ? 323 GLU   A OE1 1 
ATOM   296  O OE2 . GLU   A 1 37  ? -34.435 6.992  -3.051  1.00 36.30 ? 323 GLU   A OE2 1 
ATOM   297  N N   . ARG   A 1 38  ? -33.152 9.588  3.378   1.00 19.90 ? 324 ARG   A N   1 
ATOM   298  C CA  . ARG   A 1 38  ? -32.512 10.739 4.005   1.00 19.52 ? 324 ARG   A CA  1 
ATOM   299  C C   . ARG   A 1 38  ? -31.654 10.304 5.192   1.00 18.62 ? 324 ARG   A C   1 
ATOM   300  O O   . ARG   A 1 38  ? -32.124 9.587  6.072   1.00 19.20 ? 324 ARG   A O   1 
ATOM   301  C CB  . ARG   A 1 38  ? -33.553 11.754 4.500   1.00 20.46 ? 324 ARG   A CB  1 
ATOM   302  C CG  . ARG   A 1 38  ? -32.977 13.134 4.790   1.00 20.67 ? 324 ARG   A CG  1 
ATOM   303  C CD  . ARG   A 1 38  ? -34.030 14.194 5.099   1.00 22.12 ? 324 ARG   A CD  1 
ATOM   304  N NE  . ARG   A 1 38  ? -35.102 14.317 4.100   1.00 24.13 ? 324 ARG   A NE  1 
ATOM   305  C CZ  . ARG   A 1 38  ? -34.981 14.845 2.879   1.00 24.00 ? 324 ARG   A CZ  1 
ATOM   306  N NH1 . ARG   A 1 38  ? -36.006 14.842 2.047   1.00 25.36 ? 324 ARG   A NH1 1 
ATOM   307  N NH2 . ARG   A 1 38  ? -33.839 15.371 2.483   1.00 24.77 ? 324 ARG   A NH2 1 
ATOM   308  N N   . PHE   A 1 39  ? -30.408 10.782 5.250   1.00 17.02 ? 325 PHE   A N   1 
ATOM   309  C CA  . PHE   A 1 39  ? -29.579 10.576 6.430   1.00 16.65 ? 325 PHE   A CA  1 
ATOM   310  C C   . PHE   A 1 39  ? -30.157 11.367 7.602   1.00 16.73 ? 325 PHE   A C   1 
ATOM   311  O O   . PHE   A 1 39  ? -30.225 12.590 7.540   1.00 18.28 ? 325 PHE   A O   1 
ATOM   312  C CB  . PHE   A 1 39  ? -28.134 11.009 6.177   1.00 16.62 ? 325 PHE   A CB  1 
ATOM   313  C CG  . PHE   A 1 39  ? -27.361 10.080 5.253   1.00 16.11 ? 325 PHE   A CG  1 
ATOM   314  C CD1 . PHE   A 1 39  ? -26.870 8.867  5.728   1.00 16.57 ? 325 PHE   A CD1 1 
ATOM   315  C CD2 . PHE   A 1 39  ? -27.088 10.443 3.934   1.00 16.84 ? 325 PHE   A CD2 1 
ATOM   316  C CE1 . PHE   A 1 39  ? -26.138 8.023  4.905   1.00 16.48 ? 325 PHE   A CE1 1 
ATOM   317  C CE2 . PHE   A 1 39  ? -26.346 9.605  3.123   1.00 16.30 ? 325 PHE   A CE2 1 
ATOM   318  C CZ  . PHE   A 1 39  ? -25.880 8.394  3.606   1.00 16.82 ? 325 PHE   A CZ  1 
ATOM   319  N N   . ASP   A 1 40  ? -30.534 10.672 8.682   1.00 16.88 ? 326 ASP   A N   1 
ATOM   320  C CA  . ASP   A 1 40  ? -31.308 11.304 9.739   1.00 17.34 ? 326 ASP   A CA  1 
ATOM   321  C C   . ASP   A 1 40  ? -30.481 11.732 10.950  1.00 15.69 ? 326 ASP   A C   1 
ATOM   322  O O   . ASP   A 1 40  ? -31.019 12.466 11.779  1.00 17.34 ? 326 ASP   A O   1 
ATOM   323  C CB  . ASP   A 1 40  ? -32.501 10.451 10.131  1.00 18.45 ? 326 ASP   A CB  1 
ATOM   324  C CG  . ASP   A 1 40  ? -32.229 9.280  11.063  1.00 19.34 ? 326 ASP   A CG  1 
ATOM   325  O OD1 . ASP   A 1 40  ? -31.044 8.932  11.266  1.00 20.21 ? 326 ASP   A OD1 1 
ATOM   326  O OD2 . ASP   A 1 40  ? -33.222 8.720  11.568  1.00 21.31 ? 326 ASP   A OD2 1 
ATOM   327  N N   . SER   A 1 41  ? -29.225 11.278 11.093  1.00 15.71 ? 327 SER   A N   1 
ATOM   328  C CA  . SER   A 1 41  ? -28.476 11.508 12.323  1.00 17.30 ? 327 SER   A CA  1 
ATOM   329  C C   . SER   A 1 41  ? -27.143 12.213 12.101  1.00 17.44 ? 327 SER   A C   1 
ATOM   330  O O   . SER   A 1 41  ? -26.442 12.498 13.070  1.00 19.00 ? 327 SER   A O   1 
ATOM   331  C CB  . SER   A 1 41  ? -28.240 10.215 13.061  1.00 17.54 ? 327 SER   A CB  1 
ATOM   332  O OG  . SER   A 1 41  ? -29.468 9.616  13.439  1.00 18.10 ? 327 SER   A OG  1 
ATOM   333  N N   . TYR   A 1 42  ? -26.787 12.489 10.839  1.00 17.07 ? 328 TYR   A N   1 
ATOM   334  C CA  . TYR   A 1 42  ? -25.520 13.104 10.497  1.00 16.90 ? 328 TYR   A CA  1 
ATOM   335  C C   . TYR   A 1 42  ? -25.702 14.036 9.308   1.00 16.88 ? 328 TYR   A C   1 
ATOM   336  O O   . TYR   A 1 42  ? -26.575 13.808 8.486   1.00 16.56 ? 328 TYR   A O   1 
ATOM   337  C CB  . TYR   A 1 42  ? -24.491 12.096 9.999   1.00 16.85 ? 328 TYR   A CB  1 
ATOM   338  C CG  . TYR   A 1 42  ? -24.129 10.997 10.980  1.00 16.49 ? 328 TYR   A CG  1 
ATOM   339  C CD1 . TYR   A 1 42  ? -23.198 11.207 11.986  1.00 17.12 ? 328 TYR   A CD1 1 
ATOM   340  C CD2 . TYR   A 1 42  ? -24.654 9.725  10.837  1.00 17.46 ? 328 TYR   A CD2 1 
ATOM   341  C CE1 . TYR   A 1 42  ? -22.840 10.186 12.851  1.00 17.07 ? 328 TYR   A CE1 1 
ATOM   342  C CE2 . TYR   A 1 42  ? -24.298 8.695  11.689  1.00 17.62 ? 328 TYR   A CE2 1 
ATOM   343  C CZ  . TYR   A 1 42  ? -23.396 8.931  12.710  1.00 17.05 ? 328 TYR   A CZ  1 
ATOM   344  O OH  . TYR   A 1 42  ? -23.051 7.911  13.552  1.00 17.62 ? 328 TYR   A OH  1 
ATOM   345  N N   . PRO   A 1 43  ? -24.897 15.110 9.195   1.00 16.92 ? 329 PRO   A N   1 
ATOM   346  C CA  . PRO   A 1 43  ? -24.968 16.020 8.056   1.00 16.12 ? 329 PRO   A CA  1 
ATOM   347  C C   . PRO   A 1 43  ? -24.305 15.436 6.823   1.00 14.95 ? 329 PRO   A C   1 
ATOM   348  O O   . PRO   A 1 43  ? -23.200 15.818 6.468   1.00 15.15 ? 329 PRO   A O   1 
ATOM   349  C CB  . PRO   A 1 43  ? -24.288 17.284 8.570   1.00 18.48 ? 329 PRO   A CB  1 
ATOM   350  C CG  . PRO   A 1 43  ? -24.272 17.095 10.069  1.00 20.41 ? 329 PRO   A CG  1 
ATOM   351  C CD  . PRO   A 1 43  ? -23.994 15.627 10.230  1.00 18.87 ? 329 PRO   A CD  1 
ATOM   352  N N   . MET   A 1 44  ? -25.022 14.505 6.201   1.00 15.00 ? 330 MET   A N   1 
ATOM   353  C CA  . MET   A 1 44  ? -24.522 13.769 5.052   1.00 14.70 ? 330 MET   A CA  1 
ATOM   354  C C   . MET   A 1 44  ? -25.477 13.920 3.872   1.00 14.42 ? 330 MET   A C   1 
ATOM   355  O O   . MET   A 1 44  ? -26.676 14.090 4.051   1.00 14.87 ? 330 MET   A O   1 
ATOM   356  C CB  . MET   A 1 44  ? -24.398 12.285 5.395   1.00 14.99 ? 330 MET   A CB  1 
ATOM   357  C CG  . MET   A 1 44  ? -23.357 12.001 6.461   1.00 15.50 ? 330 MET   A CG  1 
ATOM   358  S SD  . MET   A 1 44  ? -23.513 10.302 7.035   1.00 16.82 ? 330 MET   A SD  1 
ATOM   359  C CE  . MET   A 1 44  ? -22.141 10.190 8.192   1.00 15.77 ? 330 MET   A CE  1 
ATOM   360  N N   . VAL   A 1 45  ? -24.913 13.804 2.662   1.00 14.53 ? 331 VAL   A N   1 
ATOM   361  C CA  . VAL   A 1 45  ? -25.685 13.848 1.427   1.00 14.33 ? 331 VAL   A CA  1 
ATOM   362  C C   . VAL   A 1 45  ? -24.937 13.030 0.373   1.00 14.53 ? 331 VAL   A C   1 
ATOM   363  O O   . VAL   A 1 45  ? -23.705 12.953 0.408   1.00 14.11 ? 331 VAL   A O   1 
ATOM   364  C CB  . VAL   A 1 45  ? -25.903 15.305 0.971   1.00 14.84 ? 331 VAL   A CB  1 
ATOM   365  C CG1 . VAL   A 1 45  ? -24.585 16.035 0.727   1.00 15.57 ? 331 VAL   A CG1 1 
ATOM   366  C CG2 . VAL   A 1 45  ? -26.803 15.398 -0.265  1.00 15.02 ? 331 VAL   A CG2 1 
ATOM   367  N N   . LEU   A 1 46  ? -25.702 12.415 -0.544  1.00 14.87 ? 332 LEU   A N   1 
ATOM   368  C CA  . LEU   A 1 46  ? -25.142 11.655 -1.655  1.00 15.18 ? 332 LEU   A CA  1 
ATOM   369  C C   . LEU   A 1 46  ? -25.216 12.454 -2.951  1.00 15.94 ? 332 LEU   A C   1 
ATOM   370  O O   . LEU   A 1 46  ? -26.096 13.288 -3.143  1.00 16.31 ? 332 LEU   A O   1 
ATOM   371  C CB  . LEU   A 1 46  ? -25.897 10.344 -1.855  1.00 16.27 ? 332 LEU   A CB  1 
ATOM   372  C CG  . LEU   A 1 46  ? -25.944 9.408  -0.649  1.00 16.54 ? 332 LEU   A CG  1 
ATOM   373  C CD1 . LEU   A 1 46  ? -26.578 8.088  -1.047  1.00 17.37 ? 332 LEU   A CD1 1 
ATOM   374  C CD2 . LEU   A 1 46  ? -24.579 9.191  -0.030  1.00 16.67 ? 332 LEU   A CD2 1 
ATOM   375  N N   . GLY   A 1 47  ? -24.327 12.100 -3.880  1.00 16.05 ? 333 GLY   A N   1 
ATOM   376  C CA  . GLY   A 1 47  ? -24.509 12.478 -5.271  1.00 16.15 ? 333 GLY   A CA  1 
ATOM   377  C C   . GLY   A 1 47  ? -25.689 11.699 -5.848  1.00 17.09 ? 333 GLY   A C   1 
ATOM   378  O O   . GLY   A 1 47  ? -25.957 10.580 -5.415  1.00 17.52 ? 333 GLY   A O   1 
ATOM   379  N N   . ALA   A 1 48  ? -26.385 12.289 -6.826  1.00 17.81 ? 334 ALA   A N   1 
ATOM   380  C CA  . ALA   A 1 48  ? -27.529 11.649 -7.464  1.00 19.49 ? 334 ALA   A CA  1 
ATOM   381  C C   . ALA   A 1 48  ? -27.104 10.445 -8.301  1.00 20.48 ? 334 ALA   A C   1 
ATOM   382  O O   . ALA   A 1 48  ? -27.882 9.516  -8.493  1.00 23.38 ? 334 ALA   A O   1 
ATOM   383  C CB  . ALA   A 1 48  ? -28.273 12.650 -8.324  1.00 20.45 ? 334 ALA   A CB  1 
ATOM   384  N N   . GLN   A 1 49  ? -25.873 10.486 -8.810  1.00 20.48 ? 335 GLN   A N   1 
ATOM   385  C CA  . GLN   A 1 49  ? -25.387 9.498  -9.752  1.00 21.76 ? 335 GLN   A CA  1 
ATOM   386  C C   . GLN   A 1 49  ? -25.175 8.150  -9.068  1.00 22.67 ? 335 GLN   A C   1 
ATOM   387  O O   . GLN   A 1 49  ? -24.700 8.083  -7.933  1.00 21.83 ? 335 GLN   A O   1 
ATOM   388  C CB  . GLN   A 1 49  ? -24.087 10.011 -10.362 1.00 22.99 ? 335 GLN   A CB  1 
ATOM   389  C CG  . GLN   A 1 49  ? -24.267 11.215 -11.288 1.00 24.48 ? 335 GLN   A CG  1 
ATOM   390  C CD  . GLN   A 1 49  ? -24.616 12.501 -10.564 1.00 25.16 ? 335 GLN   A CD  1 
ATOM   391  O OE1 . GLN   A 1 49  ? -24.162 12.755 -9.436  1.00 22.26 ? 335 GLN   A OE1 1 
ATOM   392  N NE2 . GLN   A 1 49  ? -25.429 13.329 -11.221 1.00 25.82 ? 335 GLN   A NE2 1 
ATOM   393  N N   . HIS   A 1 50  ? -25.512 7.077  -9.795  1.00 23.89 ? 336 HIS   A N   1 
ATOM   394  C CA  . HIS   A 1 50  ? -25.239 5.713  -9.378  1.00 24.82 ? 336 HIS   A CA  1 
ATOM   395  C C   . HIS   A 1 50  ? -24.229 5.113  -10.352 1.00 24.85 ? 336 HIS   A C   1 
ATOM   396  O O   . HIS   A 1 50  ? -24.538 4.991  -11.531 1.00 28.05 ? 336 HIS   A O   1 
ATOM   397  C CB  . HIS   A 1 50  ? -26.500 4.840  -9.441  1.00 26.29 ? 336 HIS   A CB  1 
ATOM   398  C CG  . HIS   A 1 50  ? -27.613 5.202  -8.521  1.00 28.31 ? 336 HIS   A CG  1 
ATOM   399  N ND1 . HIS   A 1 50  ? -28.092 6.476  -8.306  1.00 30.71 ? 336 HIS   A ND1 1 
ATOM   400  C CD2 . HIS   A 1 50  ? -28.380 4.390  -7.788  1.00 28.95 ? 336 HIS   A CD2 1 
ATOM   401  C CE1 . HIS   A 1 50  ? -29.098 6.425  -7.441  1.00 29.24 ? 336 HIS   A CE1 1 
ATOM   402  N NE2 . HIS   A 1 50  ? -29.284 5.172  -7.109  1.00 29.09 ? 336 HIS   A NE2 1 
ATOM   403  N N   . PHE   A 1 51  ? -23.055 4.710  -9.853  1.00 23.83 ? 337 PHE   A N   1 
ATOM   404  C CA  . PHE   A 1 51  ? -21.991 4.180  -10.695 1.00 24.96 ? 337 PHE   A CA  1 
ATOM   405  C C   . PHE   A 1 51  ? -21.933 2.659  -10.596 1.00 25.91 ? 337 PHE   A C   1 
ATOM   406  O O   . PHE   A 1 51  ? -21.855 2.115  -9.495  1.00 26.38 ? 337 PHE   A O   1 
ATOM   407  C CB  . PHE   A 1 51  ? -20.619 4.704  -10.270 1.00 26.40 ? 337 PHE   A CB  1 
ATOM   408  C CG  . PHE   A 1 51  ? -20.482 6.217  -10.316 1.00 29.00 ? 337 PHE   A CG  1 
ATOM   409  C CD1 . PHE   A 1 51  ? -20.818 6.931  -11.463 1.00 29.97 ? 337 PHE   A CD1 1 
ATOM   410  C CD2 . PHE   A 1 51  ? -20.044 6.917  -9.198  1.00 30.26 ? 337 PHE   A CD2 1 
ATOM   411  C CE1 . PHE   A 1 51  ? -20.701 8.313  -11.490 1.00 31.52 ? 337 PHE   A CE1 1 
ATOM   412  C CE2 . PHE   A 1 51  ? -19.921 8.294  -9.235  1.00 30.77 ? 337 PHE   A CE2 1 
ATOM   413  C CZ  . PHE   A 1 51  ? -20.249 8.985  -10.379 1.00 31.22 ? 337 PHE   A CZ  1 
ATOM   414  N N   . HIS   A 1 52  ? -21.909 1.995  -11.759 1.00 27.83 ? 338 HIS   A N   1 
ATOM   415  C CA  . HIS   A 1 52  ? -21.890 0.541  -11.856 1.00 29.81 ? 338 HIS   A CA  1 
ATOM   416  C C   . HIS   A 1 52  ? -20.608 0.052  -12.532 1.00 28.65 ? 338 HIS   A C   1 
ATOM   417  O O   . HIS   A 1 52  ? -20.342 -1.149 -12.559 1.00 30.41 ? 338 HIS   A O   1 
ATOM   418  C CB  . HIS   A 1 52  ? -23.087 0.044  -12.681 1.00 33.55 ? 338 HIS   A CB  1 
ATOM   419  C CG  . HIS   A 1 52  ? -24.408 0.529  -12.183 1.00 37.16 ? 338 HIS   A CG  1 
ATOM   420  N ND1 . HIS   A 1 52  ? -24.983 1.707  -12.610 1.00 41.56 ? 338 HIS   A ND1 1 
ATOM   421  C CD2 . HIS   A 1 52  ? -25.258 0.001  -11.293 1.00 37.11 ? 338 HIS   A CD2 1 
ATOM   422  C CE1 . HIS   A 1 52  ? -26.138 1.880  -11.985 1.00 41.15 ? 338 HIS   A CE1 1 
ATOM   423  N NE2 . HIS   A 1 52  ? -26.324 0.855  -11.180 1.00 39.48 ? 338 HIS   A NE2 1 
ATOM   424  N N   . SER   A 1 53  ? -19.842 0.984  -13.110 1.00 27.31 ? 339 SER   A N   1 
ATOM   425  C CA  . SER   A 1 53  ? -18.696 0.667  -13.947 1.00 27.75 ? 339 SER   A CA  1 
ATOM   426  C C   . SER   A 1 53  ? -17.942 1.959  -14.230 1.00 27.74 ? 339 SER   A C   1 
ATOM   427  O O   . SER   A 1 53  ? -18.431 3.035  -13.905 1.00 28.02 ? 339 SER   A O   1 
ATOM   428  C CB  . SER   A 1 53  ? -19.113 0.003  -15.239 1.00 29.92 ? 339 SER   A CB  1 
ATOM   429  O OG  . SER   A 1 53  ? -19.900 0.885  -16.033 1.00 31.95 ? 339 SER   A OG  1 
ATOM   430  N N   . GLY   A 1 54  ? -16.744 1.837  -14.803 1.00 27.38 ? 340 GLY   A N   1 
ATOM   431  C CA  . GLY   A 1 54  ? -16.066 2.965  -15.412 1.00 27.46 ? 340 GLY   A CA  1 
ATOM   432  C C   . GLY   A 1 54  ? -15.253 3.775  -14.407 1.00 25.85 ? 340 GLY   A C   1 
ATOM   433  O O   . GLY   A 1 54  ? -15.275 3.518  -13.204 1.00 27.10 ? 340 GLY   A O   1 
ATOM   434  N N   . LYS   A 1 55  ? -14.556 4.770  -14.960 1.00 23.64 ? 341 LYS   A N   1 
ATOM   435  C CA  . LYS   A 1 55  ? -13.787 5.732  -14.201 1.00 22.93 ? 341 LYS   A CA  1 
ATOM   436  C C   . LYS   A 1 55  ? -14.552 7.047  -14.147 1.00 21.29 ? 341 LYS   A C   1 
ATOM   437  O O   . LYS   A 1 55  ? -15.152 7.478  -15.132 1.00 21.63 ? 341 LYS   A O   1 
ATOM   438  C CB  . LYS   A 1 55  ? -12.425 5.977  -14.849 1.00 25.39 ? 341 LYS   A CB  1 
ATOM   439  C CG  . LYS   A 1 55  ? -11.562 4.732  -14.988 1.00 27.88 ? 341 LYS   A CG  1 
ATOM   440  C CD  . LYS   A 1 55  ? -10.281 4.977  -15.769 1.00 30.04 ? 341 LYS   A CD  1 
ATOM   441  C CE  . LYS   A 1 55  ? -9.461  3.736  -15.868 1.00 33.10 ? 341 LYS   A CE  1 
ATOM   442  N NZ  . LYS   A 1 55  ? -8.349  3.902  -16.810 1.00 34.95 ? 341 LYS   A NZ  1 
ATOM   443  N N   . HIS   A 1 56  ? -14.445 7.704  -12.994 1.00 20.10 ? 342 HIS   A N   1 
ATOM   444  C CA  . HIS   A 1 56  ? -15.233 8.874  -12.669 1.00 19.61 ? 342 HIS   A CA  1 
ATOM   445  C C   . HIS   A 1 56  ? -14.349 9.815  -11.865 1.00 18.98 ? 342 HIS   A C   1 
ATOM   446  O O   . HIS   A 1 56  ? -13.499 9.376  -11.095 1.00 20.68 ? 342 HIS   A O   1 
ATOM   447  C CB  . HIS   A 1 56  ? -16.506 8.477  -11.909 1.00 20.11 ? 342 HIS   A CB  1 
ATOM   448  C CG  . HIS   A 1 56  ? -17.329 7.504  -12.683 1.00 21.89 ? 342 HIS   A CG  1 
ATOM   449  N ND1 . HIS   A 1 56  ? -18.188 7.889  -13.688 1.00 24.13 ? 342 HIS   A ND1 1 
ATOM   450  C CD2 . HIS   A 1 56  ? -17.368 6.170  -12.653 1.00 23.40 ? 342 HIS   A CD2 1 
ATOM   451  C CE1 . HIS   A 1 56  ? -18.738 6.810  -14.234 1.00 24.70 ? 342 HIS   A CE1 1 
ATOM   452  N NE2 . HIS   A 1 56  ? -18.255 5.753  -13.619 1.00 24.96 ? 342 HIS   A NE2 1 
ATOM   453  N N   . TYR   A 1 57  ? -14.586 11.109 -12.027 1.00 18.18 ? 343 TYR   A N   1 
ATOM   454  C CA  . TYR   A 1 57  ? -13.764 12.108 -11.383 1.00 17.68 ? 343 TYR   A CA  1 
ATOM   455  C C   . TYR   A 1 57  ? -14.618 13.312 -11.024 1.00 17.07 ? 343 TYR   A C   1 
ATOM   456  O O   . TYR   A 1 57  ? -15.462 13.733 -11.801 1.00 17.33 ? 343 TYR   A O   1 
ATOM   457  C CB  . TYR   A 1 57  ? -12.601 12.560 -12.270 1.00 18.60 ? 343 TYR   A CB  1 
ATOM   458  C CG  . TYR   A 1 57  ? -11.866 13.738 -11.648 1.00 19.53 ? 343 TYR   A CG  1 
ATOM   459  C CD1 . TYR   A 1 57  ? -10.939 13.553 -10.631 1.00 19.21 ? 343 TYR   A CD1 1 
ATOM   460  C CD2 . TYR   A 1 57  ? -12.129 15.039 -12.059 1.00 21.31 ? 343 TYR   A CD2 1 
ATOM   461  C CE1 . TYR   A 1 57  ? -10.288 14.626 -10.052 1.00 19.04 ? 343 TYR   A CE1 1 
ATOM   462  C CE2 . TYR   A 1 57  ? -11.479 16.122 -11.490 1.00 21.35 ? 343 TYR   A CE2 1 
ATOM   463  C CZ  . TYR   A 1 57  ? -10.567 15.914 -10.469 1.00 20.00 ? 343 TYR   A CZ  1 
ATOM   464  O OH  . TYR   A 1 57  ? -9.920  16.968 -9.895  1.00 22.19 ? 343 TYR   A OH  1 
ATOM   465  N N   . TRP   A 1 58  ? -14.386 13.864 -9.832  1.00 16.48 ? 344 TRP   A N   1 
ATOM   466  C CA  . TRP   A 1 58  ? -14.987 15.132 -9.465  1.00 15.57 ? 344 TRP   A CA  1 
ATOM   467  C C   . TRP   A 1 58  ? -14.063 15.882 -8.510  1.00 15.16 ? 344 TRP   A C   1 
ATOM   468  O O   . TRP   A 1 58  ? -13.146 15.296 -7.932  1.00 16.04 ? 344 TRP   A O   1 
ATOM   469  C CB  . TRP   A 1 58  ? -16.406 14.950 -8.905  1.00 15.75 ? 344 TRP   A CB  1 
ATOM   470  C CG  . TRP   A 1 58  ? -16.564 14.040 -7.715  1.00 15.55 ? 344 TRP   A CG  1 
ATOM   471  C CD1 . TRP   A 1 58  ? -16.688 14.413 -6.408  1.00 15.46 ? 344 TRP   A CD1 1 
ATOM   472  C CD2 . TRP   A 1 58  ? -16.701 12.606 -7.746  1.00 16.13 ? 344 TRP   A CD2 1 
ATOM   473  N NE1 . TRP   A 1 58  ? -16.857 13.304 -5.623  1.00 14.80 ? 344 TRP   A NE1 1 
ATOM   474  C CE2 . TRP   A 1 58  ? -16.872 12.179 -6.411  1.00 15.70 ? 344 TRP   A CE2 1 
ATOM   475  C CE3 . TRP   A 1 58  ? -16.703 11.642 -8.761  1.00 17.24 ? 344 TRP   A CE3 1 
ATOM   476  C CZ2 . TRP   A 1 58  ? -17.030 10.836 -6.071  1.00 16.98 ? 344 TRP   A CZ2 1 
ATOM   477  C CZ3 . TRP   A 1 58  ? -16.861 10.316 -8.420  1.00 18.24 ? 344 TRP   A CZ3 1 
ATOM   478  C CH2 . TRP   A 1 58  ? -17.025 9.918  -7.094  1.00 18.06 ? 344 TRP   A CH2 1 
ATOM   479  N N   . GLU   A 1 59  ? -14.325 17.186 -8.394  1.00 15.07 ? 345 GLU   A N   1 
ATOM   480  C CA  . GLU   A 1 59  ? -13.473 18.108 -7.659  1.00 14.97 ? 345 GLU   A CA  1 
ATOM   481  C C   . GLU   A 1 59  ? -14.332 18.876 -6.667  1.00 14.21 ? 345 GLU   A C   1 
ATOM   482  O O   . GLU   A 1 59  ? -15.384 19.390 -7.037  1.00 14.68 ? 345 GLU   A O   1 
ATOM   483  C CB  . GLU   A 1 59  ? -12.777 19.078 -8.617  1.00 15.90 ? 345 GLU   A CB  1 
ATOM   484  C CG  . GLU   A 1 59  ? -11.976 20.173 -7.921  1.00 17.07 ? 345 GLU   A CG  1 
ATOM   485  C CD  . GLU   A 1 59  ? -11.294 21.191 -8.808  1.00 18.01 ? 345 GLU   A CD  1 
ATOM   486  O OE1 . GLU   A 1 59  ? -10.703 22.150 -8.294  1.00 19.31 ? 345 GLU   A OE1 1 
ATOM   487  O OE2 . GLU   A 1 59  ? -11.345 21.022 -10.034 1.00 20.33 ? 345 GLU   A OE2 1 
ATOM   488  N N   . VAL   A 1 60  ? -13.870 18.952 -5.407  1.00 13.79 ? 346 VAL   A N   1 
ATOM   489  C CA  . VAL   A 1 60  ? -14.648 19.605 -4.372  1.00 13.63 ? 346 VAL   A CA  1 
ATOM   490  C C   . VAL   A 1 60  ? -13.805 20.690 -3.705  1.00 13.99 ? 346 VAL   A C   1 
ATOM   491  O O   . VAL   A 1 60  ? -12.673 20.428 -3.297  1.00 15.39 ? 346 VAL   A O   1 
ATOM   492  C CB  . VAL   A 1 60  ? -15.149 18.606 -3.315  1.00 14.39 ? 346 VAL   A CB  1 
ATOM   493  C CG1 . VAL   A 1 60  ? -15.977 19.320 -2.265  1.00 14.49 ? 346 VAL   A CG1 1 
ATOM   494  C CG2 . VAL   A 1 60  ? -15.940 17.463 -3.940  1.00 14.67 ? 346 VAL   A CG2 1 
ATOM   495  N N   . ASP   A 1 61  ? -14.401 21.879 -3.559  1.00 13.73 ? 347 ASP   A N   1 
ATOM   496  C CA  . ASP   A 1 61  ? -13.786 22.986 -2.845  1.00 13.80 ? 347 ASP   A CA  1 
ATOM   497  C C   . ASP   A 1 61  ? -14.214 22.933 -1.380  1.00 13.54 ? 347 ASP   A C   1 
ATOM   498  O O   . ASP   A 1 61  ? -15.407 22.840 -1.092  1.00 14.14 ? 347 ASP   A O   1 
ATOM   499  C CB  . ASP   A 1 61  ? -14.153 24.309 -3.496  1.00 14.53 ? 347 ASP   A CB  1 
ATOM   500  C CG  . ASP   A 1 61  ? -13.420 25.509 -2.930  1.00 16.04 ? 347 ASP   A CG  1 
ATOM   501  O OD1 . ASP   A 1 61  ? -13.579 25.739 -1.731  1.00 17.69 ? 347 ASP   A OD1 1 
ATOM   502  O OD2 . ASP   A 1 61  ? -12.709 26.197 -3.686  1.00 19.32 ? 347 ASP   A OD2 1 
ATOM   503  N N   . VAL   A 1 62  ? -13.204 23.008 -0.488  1.00 13.80 ? 348 VAL   A N   1 
ATOM   504  C CA  . VAL   A 1 62  ? -13.364 22.900 0.958   1.00 14.82 ? 348 VAL   A CA  1 
ATOM   505  C C   . VAL   A 1 62  ? -12.751 24.123 1.649   1.00 15.05 ? 348 VAL   A C   1 
ATOM   506  O O   . VAL   A 1 62  ? -12.369 24.056 2.825   1.00 15.81 ? 348 VAL   A O   1 
ATOM   507  C CB  . VAL   A 1 62  ? -12.725 21.595 1.481   1.00 15.77 ? 348 VAL   A CB  1 
ATOM   508  C CG1 . VAL   A 1 62  ? -13.403 20.358 0.919   1.00 17.12 ? 348 VAL   A CG1 1 
ATOM   509  C CG2 . VAL   A 1 62  ? -11.231 21.524 1.198   1.00 15.73 ? 348 VAL   A CG2 1 
ATOM   510  N N   . THR   A 1 63  ? -12.642 25.243 0.927   1.00 14.61 ? 349 THR   A N   1 
ATOM   511  C CA  . THR   A 1 63  ? -11.940 26.421 1.421   1.00 15.33 ? 349 THR   A CA  1 
ATOM   512  C C   . THR   A 1 63  ? -12.556 26.910 2.727   1.00 15.46 ? 349 THR   A C   1 
ATOM   513  O O   . THR   A 1 63  ? -13.755 27.143 2.807   1.00 16.56 ? 349 THR   A O   1 
ATOM   514  C CB  . THR   A 1 63  ? -11.977 27.546 0.385   1.00 15.32 ? 349 THR   A CB  1 
ATOM   515  O OG1 . THR   A 1 63  ? -11.365 27.080 -0.816  1.00 16.14 ? 349 THR   A OG1 1 
ATOM   516  C CG2 . THR   A 1 63  ? -11.250 28.792 0.865   1.00 16.04 ? 349 THR   A CG2 1 
ATOM   517  N N   . GLY   A 1 64  ? -11.708 27.140 3.730   1.00 15.32 ? 350 GLY   A N   1 
ATOM   518  C CA  . GLY   A 1 64  ? -12.152 27.787 4.954   1.00 15.96 ? 350 GLY   A CA  1 
ATOM   519  C C   . GLY   A 1 64  ? -12.977 26.867 5.856   1.00 16.96 ? 350 GLY   A C   1 
ATOM   520  O O   . GLY   A 1 64  ? -13.618 27.341 6.800   1.00 19.02 ? 350 GLY   A O   1 
ATOM   521  N N   . LYS   A 1 65  ? -12.926 25.555 5.612   1.00 16.04 ? 351 LYS   A N   1 
ATOM   522  C CA  . LYS   A 1 65  ? -13.649 24.594 6.431   1.00 15.44 ? 351 LYS   A CA  1 
ATOM   523  C C   . LYS   A 1 65  ? -12.730 23.942 7.456   1.00 16.41 ? 351 LYS   A C   1 
ATOM   524  O O   . LYS   A 1 65  ? -11.615 23.546 7.140   1.00 17.31 ? 351 LYS   A O   1 
ATOM   525  C CB  . LYS   A 1 65  ? -14.287 23.505 5.567   1.00 14.89 ? 351 LYS   A CB  1 
ATOM   526  C CG  . LYS   A 1 65  ? -15.333 24.079 4.622   1.00 15.24 ? 351 LYS   A CG  1 
ATOM   527  C CD  . LYS   A 1 65  ? -16.248 23.057 3.965   1.00 15.16 ? 351 LYS   A CD  1 
ATOM   528  C CE  . LYS   A 1 65  ? -17.034 22.205 4.911   1.00 15.11 ? 351 LYS   A CE  1 
ATOM   529  N NZ  . LYS   A 1 65  ? -17.814 23.015 5.861   1.00 15.00 ? 351 LYS   A NZ  1 
ATOM   530  N N   . GLU   A 1 66  ? -13.257 23.793 8.680   1.00 16.55 ? 352 GLU   A N   1 
ATOM   531  C CA  . GLU   A 1 66  ? -12.536 23.152 9.764   1.00 17.24 ? 352 GLU   A CA  1 
ATOM   532  C C   . GLU   A 1 66  ? -12.687 21.638 9.716   1.00 16.30 ? 352 GLU   A C   1 
ATOM   533  O O   . GLU   A 1 66  ? -11.923 20.941 10.376  1.00 16.74 ? 352 GLU   A O   1 
ATOM   534  C CB  . GLU   A 1 66  ? -12.976 23.661 11.145  1.00 19.19 ? 352 GLU   A CB  1 
ATOM   535  C CG  . GLU   A 1 66  ? -14.450 23.434 11.470  1.00 22.95 ? 352 GLU   A CG  1 
ATOM   536  C CD  . GLU   A 1 66  ? -14.864 23.525 12.935  1.00 25.54 ? 352 GLU   A CD  1 
ATOM   537  O OE1 . GLU   A 1 66  ? -14.002 23.882 13.774  1.00 27.97 ? 352 GLU   A OE1 1 
ATOM   538  O OE2 . GLU   A 1 66  ? -16.052 23.217 13.251  1.00 27.01 ? 352 GLU   A OE2 1 
ATOM   539  N N   . ALA   A 1 67  ? -13.689 21.135 8.986   1.00 15.57 ? 353 ALA   A N   1 
ATOM   540  C CA  . ALA   A 1 67  ? -13.972 19.705 8.956   1.00 15.37 ? 353 ALA   A CA  1 
ATOM   541  C C   . ALA   A 1 67  ? -14.808 19.392 7.722   1.00 14.66 ? 353 ALA   A C   1 
ATOM   542  O O   . ALA   A 1 67  ? -15.575 20.231 7.273   1.00 15.26 ? 353 ALA   A O   1 
ATOM   543  C CB  . ALA   A 1 67  ? -14.691 19.270 10.221  1.00 15.52 ? 353 ALA   A CB  1 
ATOM   544  N N   . TRP   A 1 68  ? -14.618 18.185 7.188   1.00 13.89 ? 354 TRP   A N   1 
ATOM   545  C CA  . TRP   A 1 68  ? -15.395 17.673 6.073   1.00 14.22 ? 354 TRP   A CA  1 
ATOM   546  C C   . TRP   A 1 68  ? -15.074 16.197 5.902   1.00 13.78 ? 354 TRP   A C   1 
ATOM   547  O O   . TRP   A 1 68  ? -14.055 15.720 6.400   1.00 14.16 ? 354 TRP   A O   1 
ATOM   548  C CB  . TRP   A 1 68  ? -15.108 18.445 4.777   1.00 14.65 ? 354 TRP   A CB  1 
ATOM   549  C CG  . TRP   A 1 68  ? -13.650 18.622 4.442   1.00 14.72 ? 354 TRP   A CG  1 
ATOM   550  C CD1 . TRP   A 1 68  ? -12.923 19.760 4.621   1.00 15.77 ? 354 TRP   A CD1 1 
ATOM   551  C CD2 . TRP   A 1 68  ? -12.745 17.665 3.847   1.00 14.68 ? 354 TRP   A CD2 1 
ATOM   552  N NE1 . TRP   A 1 68  ? -11.633 19.581 4.211   1.00 16.01 ? 354 TRP   A NE1 1 
ATOM   553  C CE2 . TRP   A 1 68  ? -11.492 18.312 3.723   1.00 14.56 ? 354 TRP   A CE2 1 
ATOM   554  C CE3 . TRP   A 1 68  ? -12.859 16.341 3.397   1.00 15.05 ? 354 TRP   A CE3 1 
ATOM   555  C CZ2 . TRP   A 1 68  ? -10.378 17.683 3.171   1.00 15.36 ? 354 TRP   A CZ2 1 
ATOM   556  C CZ3 . TRP   A 1 68  ? -11.752 15.724 2.851   1.00 15.33 ? 354 TRP   A CZ3 1 
ATOM   557  C CH2 . TRP   A 1 68  ? -10.534 16.385 2.746   1.00 15.03 ? 354 TRP   A CH2 1 
ATOM   558  N N   . ASP   A 1 69  ? -15.956 15.493 5.186   1.00 13.63 ? 355 ASP   A N   1 
ATOM   559  C CA  . ASP   A 1 69  ? -15.688 14.130 4.767   1.00 13.83 ? 355 ASP   A CA  1 
ATOM   560  C C   . ASP   A 1 69  ? -16.081 13.999 3.298   1.00 13.85 ? 355 ASP   A C   1 
ATOM   561  O O   . ASP   A 1 69  ? -17.122 14.501 2.884   1.00 13.60 ? 355 ASP   A O   1 
ATOM   562  C CB  . ASP   A 1 69  ? -16.429 13.127 5.632   1.00 14.57 ? 355 ASP   A CB  1 
ATOM   563  C CG  . ASP   A 1 69  ? -16.180 11.676 5.247   1.00 15.28 ? 355 ASP   A CG  1 
ATOM   564  O OD1 . ASP   A 1 69  ? -16.705 11.250 4.186   1.00 15.81 ? 355 ASP   A OD1 1 
ATOM   565  O OD2 . ASP   A 1 69  ? -15.434 10.988 5.997   1.00 16.30 ? 355 ASP   A OD2 1 
ATOM   566  N N   . LEU   A 1 70  ? -15.215 13.347 2.519   1.00 13.58 ? 356 LEU   A N   1 
ATOM   567  C CA  . LEU   A 1 70  ? -15.467 13.148 1.099   1.00 14.27 ? 356 LEU   A CA  1 
ATOM   568  C C   . LEU   A 1 70  ? -15.116 11.724 0.736   1.00 14.29 ? 356 LEU   A C   1 
ATOM   569  O O   . LEU   A 1 70  ? -14.099 11.207 1.184   1.00 15.13 ? 356 LEU   A O   1 
ATOM   570  C CB  . LEU   A 1 70  ? -14.622 14.095 0.257   1.00 14.13 ? 356 LEU   A CB  1 
ATOM   571  C CG  . LEU   A 1 70  ? -14.925 15.582 0.412   1.00 15.41 ? 356 LEU   A CG  1 
ATOM   572  C CD1 . LEU   A 1 70  ? -13.854 16.415 -0.260  1.00 16.13 ? 356 LEU   A CD1 1 
ATOM   573  C CD2 . LEU   A 1 70  ? -16.292 15.897 -0.140  1.00 16.01 ? 356 LEU   A CD2 1 
ATOM   574  N N   . GLY   A 1 71  ? -15.935 11.137 -0.136  1.00 14.61 ? 357 GLY   A N   1 
ATOM   575  C CA  . GLY   A 1 71  ? -15.554 9.884  -0.751  1.00 15.02 ? 357 GLY   A CA  1 
ATOM   576  C C   . GLY   A 1 71  ? -16.681 9.284  -1.576  1.00 14.89 ? 357 GLY   A C   1 
ATOM   577  O O   . GLY   A 1 71  ? -17.397 9.988  -2.296  1.00 14.43 ? 357 GLY   A O   1 
ATOM   578  N N   . VAL   A 1 72  ? -16.773 7.959  -1.473  1.00 16.28 ? 358 VAL   A N   1 
ATOM   579  C CA  . VAL   A 1 72  ? -17.721 7.151  -2.213  1.00 17.04 ? 358 VAL   A CA  1 
ATOM   580  C C   . VAL   A 1 72  ? -18.348 6.170  -1.233  1.00 17.21 ? 358 VAL   A C   1 
ATOM   581  O O   . VAL   A 1 72  ? -17.703 5.752  -0.260  1.00 18.27 ? 358 VAL   A O   1 
ATOM   582  C CB  . VAL   A 1 72  ? -16.975 6.411  -3.340  1.00 19.88 ? 358 VAL   A CB  1 
ATOM   583  C CG1 . VAL   A 1 72  ? -17.810 5.329  -4.013  1.00 23.02 ? 358 VAL   A CG1 1 
ATOM   584  C CG2 . VAL   A 1 72  ? -16.443 7.391  -4.374  1.00 19.73 ? 358 VAL   A CG2 1 
ATOM   585  N N   . CYS   A 1 73  ? -19.595 5.778  -1.510  1.00 17.22 ? 359 CYS   A N   1 
ATOM   586  C CA  . CYS   A 1 73  ? -20.230 4.767  -0.683  1.00 17.90 ? 359 CYS   A CA  1 
ATOM   587  C C   . CYS   A 1 73  ? -21.129 3.860  -1.512  1.00 18.86 ? 359 CYS   A C   1 
ATOM   588  O O   . CYS   A 1 73  ? -21.510 4.191  -2.628  1.00 19.53 ? 359 CYS   A O   1 
ATOM   589  C CB  . CYS   A 1 73  ? -20.990 5.390  0.484   1.00 18.43 ? 359 CYS   A CB  1 
ATOM   590  S SG  . CYS   A 1 73  ? -22.478 6.300  -0.006  1.00 19.05 ? 359 CYS   A SG  1 
ATOM   591  N N   . ARG   A 1 74  ? -21.444 2.694  -0.950  1.00 18.74 ? 360 ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 74  ? -22.426 1.808  -1.546  1.00 20.48 ? 360 ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 74  ? -23.799 2.470  -1.542  1.00 19.98 ? 360 ARG   A C   1 
ATOM   594  O O   . ARG   A 1 74  ? -24.162 3.184  -0.616  1.00 20.55 ? 360 ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 74  ? -22.551 0.480  -0.797  1.00 22.00 ? 360 ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 74  ? -21.259 -0.321 -0.735  1.00 24.55 ? 360 ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 74  ? -21.456 -1.715 -0.152  1.00 26.39 ? 360 ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 74  ? -20.216 -2.485 -0.308  1.00 29.50 ? 360 ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 74  ? -19.403 -2.899 0.664   1.00 32.35 ? 360 ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 74  ? -19.753 -2.803 1.935   1.00 32.84 ? 360 ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 74  ? -18.233 -3.432 0.356   1.00 34.26 ? 360 ARG   A NH2 1 
ATOM   602  N N   . ASP   A 1 75  ? -24.584 2.188  -2.581  1.00 21.37 ? 361 ASP   A N   1 
ATOM   603  C CA  . ASP   A 1 75  ? -25.961 2.640  -2.635  1.00 21.98 ? 361 ASP   A CA  1 
ATOM   604  C C   . ASP   A 1 75  ? -26.736 2.124  -1.423  1.00 21.84 ? 361 ASP   A C   1 
ATOM   605  O O   . ASP   A 1 75  ? -27.640 2.792  -0.933  1.00 23.99 ? 361 ASP   A O   1 
ATOM   606  C CB  . ASP   A 1 75  ? -26.621 2.192  -3.924  1.00 23.52 ? 361 ASP   A CB  1 
ATOM   607  C CG  . ASP   A 1 75  ? -28.058 2.647  -4.083  1.00 24.39 ? 361 ASP   A CG  1 
ATOM   608  O OD1 . ASP   A 1 75  ? -28.263 3.863  -4.218  1.00 25.59 ? 361 ASP   A OD1 1 
ATOM   609  O OD2 . ASP   A 1 75  ? -28.951 1.782  -4.032  1.00 28.39 ? 361 ASP   A OD2 1 
ATOM   610  N N   . SER   A 1 76  ? -26.355 0.940  -0.940  1.00 22.79 ? 362 SER   A N   1 
ATOM   611  C CA  . SER   A 1 76  ? -27.106 0.227  0.081   1.00 23.92 ? 362 SER   A CA  1 
ATOM   612  C C   . SER   A 1 76  ? -26.790 0.703  1.501   1.00 23.81 ? 362 SER   A C   1 
ATOM   613  O O   . SER   A 1 76  ? -27.323 0.130  2.442   1.00 26.20 ? 362 SER   A O   1 
ATOM   614  C CB  . SER   A 1 76  ? -26.856 -1.260 -0.038  1.00 25.38 ? 362 SER   A CB  1 
ATOM   615  O OG  . SER   A 1 76  ? -25.490 -1.568 0.211   1.00 27.56 ? 362 SER   A OG  1 
ATOM   616  N N   . VAL   A 1 77  ? -25.937 1.721  1.687   1.00 22.90 ? 363 VAL   A N   1 
ATOM   617  C CA  . VAL   A 1 77  ? -25.553 2.122  3.034   1.00 22.68 ? 363 VAL   A CA  1 
ATOM   618  C C   . VAL   A 1 77  ? -26.804 2.522  3.819   1.00 23.41 ? 363 VAL   A C   1 
ATOM   619  O O   . VAL   A 1 77  ? -27.736 3.121  3.278   1.00 23.28 ? 363 VAL   A O   1 
ATOM   620  C CB  . VAL   A 1 77  ? -24.491 3.238  3.112   1.00 21.97 ? 363 VAL   A CB  1 
ATOM   621  C CG1 . VAL   A 1 77  ? -23.152 2.787  2.541   1.00 22.35 ? 363 VAL   A CG1 1 
ATOM   622  C CG2 . VAL   A 1 77  ? -24.954 4.534  2.457   1.00 21.02 ? 363 VAL   A CG2 1 
ATOM   623  N N   . ARG   A 1 78  ? -26.807 2.181  5.113   1.00 23.19 ? 364 ARG   A N   1 
ATOM   624  C CA  . ARG   A 1 78  ? -27.868 2.597  6.021   1.00 24.91 ? 364 ARG   A CA  1 
ATOM   625  C C   . ARG   A 1 78  ? -27.931 4.126  6.093   1.00 22.30 ? 364 ARG   A C   1 
ATOM   626  O O   . ARG   A 1 78  ? -26.910 4.806  6.070   1.00 24.64 ? 364 ARG   A O   1 
ATOM   627  C CB  . ARG   A 1 78  ? -27.679 1.961  7.404   1.00 25.94 ? 364 ARG   A CB  1 
ATOM   628  C CG  . ARG   A 1 78  ? -28.781 2.335  8.389   1.00 27.37 ? 364 ARG   A CG  1 
ATOM   629  C CD  . ARG   A 1 78  ? -28.915 1.381  9.561   1.00 26.74 ? 364 ARG   A CD  1 
ATOM   630  N NE  . ARG   A 1 78  ? -27.624 1.056  10.178  1.00 24.84 ? 364 ARG   A NE  1 
ATOM   631  C CZ  . ARG   A 1 78  ? -27.106 1.594  11.271  1.00 24.08 ? 364 ARG   A CZ  1 
ATOM   632  N NH1 . ARG   A 1 78  ? -25.993 1.102  11.776  1.00 23.25 ? 364 ARG   A NH1 1 
ATOM   633  N NH2 . ARG   A 1 78  ? -27.692 2.624  11.846  1.00 24.80 ? 364 ARG   A NH2 1 
ATOM   634  N N   . ARG   A 1 79  ? -29.157 4.652  6.164   1.00 21.23 ? 365 ARG   A N   1 
ATOM   635  C CA  . ARG   A 1 79  ? -29.402 6.083  6.225   1.00 20.01 ? 365 ARG   A CA  1 
ATOM   636  C C   . ARG   A 1 79  ? -29.830 6.522  7.624   1.00 19.80 ? 365 ARG   A C   1 
ATOM   637  O O   . ARG   A 1 79  ? -29.658 7.682  7.967   1.00 19.44 ? 365 ARG   A O   1 
ATOM   638  C CB  . ARG   A 1 79  ? -30.482 6.482  5.215   1.00 20.71 ? 365 ARG   A CB  1 
ATOM   639  C CG  . ARG   A 1 79  ? -30.247 5.934  3.815   1.00 19.91 ? 365 ARG   A CG  1 
ATOM   640  C CD  . ARG   A 1 79  ? -28.888 6.318  3.228   1.00 20.11 ? 365 ARG   A CD  1 
ATOM   641  N NE  . ARG   A 1 79  ? -28.626 5.655  1.944   1.00 21.04 ? 365 ARG   A NE  1 
ATOM   642  C CZ  . ARG   A 1 79  ? -29.126 6.013  0.765   1.00 21.34 ? 365 ARG   A CZ  1 
ATOM   643  N NH1 . ARG   A 1 79  ? -29.846 7.119  0.651   1.00 21.24 ? 365 ARG   A NH1 1 
ATOM   644  N NH2 . ARG   A 1 79  ? -28.868 5.284  -0.314  1.00 21.37 ? 365 ARG   A NH2 1 
ATOM   645  N N   . LYS   A 1 80  ? -30.409 5.608  8.415   1.00 20.83 ? 366 LYS   A N   1 
ATOM   646  C CA  . LYS   A 1 80  ? -31.026 5.970  9.682   1.00 21.19 ? 366 LYS   A CA  1 
ATOM   647  C C   . LYS   A 1 80  ? -30.167 5.485  10.842  1.00 20.86 ? 366 LYS   A C   1 
ATOM   648  O O   . LYS   A 1 80  ? -29.610 4.394  10.799  1.00 23.24 ? 366 LYS   A O   1 
ATOM   649  C CB  . LYS   A 1 80  ? -32.430 5.378  9.816   1.00 21.89 ? 366 LYS   A CB  1 
ATOM   650  C CG  . LYS   A 1 80  ? -33.344 5.668  8.635   1.00 22.79 ? 366 LYS   A CG  1 
ATOM   651  C CD  . LYS   A 1 80  ? -33.581 7.144  8.325   1.00 23.49 ? 366 LYS   A CD  1 
ATOM   652  C CE  . LYS   A 1 80  ? -34.460 7.327  7.113   1.00 24.43 ? 366 LYS   A CE  1 
ATOM   653  N NZ  . LYS   A 1 80  ? -34.646 8.725  6.707   1.00 25.12 ? 366 LYS   A NZ  1 
ATOM   654  N N   . GLY   A 1 81  ? -30.085 6.323  11.878  1.00 21.03 ? 367 GLY   A N   1 
ATOM   655  C CA  . GLY   A 1 81  ? -29.337 6.002  13.074  1.00 20.93 ? 367 GLY   A CA  1 
ATOM   656  C C   . GLY   A 1 81  ? -27.851 6.320  12.944  1.00 19.57 ? 367 GLY   A C   1 
ATOM   657  O O   . GLY   A 1 81  ? -27.425 7.111  12.101  1.00 19.33 ? 367 GLY   A O   1 
ATOM   658  N N   . HIS   A 1 82  ? -27.067 5.679  13.813  1.00 19.77 ? 368 HIS   A N   1 
ATOM   659  C CA  . HIS   A 1 82  ? -25.649 5.941  13.939  1.00 19.97 ? 368 HIS   A CA  1 
ATOM   660  C C   . HIS   A 1 82  ? -24.858 4.744  13.426  1.00 19.59 ? 368 HIS   A C   1 
ATOM   661  O O   . HIS   A 1 82  ? -25.291 3.590  13.539  1.00 21.00 ? 368 HIS   A O   1 
ATOM   662  C CB  . HIS   A 1 82  ? -25.305 6.246  15.402  1.00 20.01 ? 368 HIS   A CB  1 
ATOM   663  C CG  . HIS   A 1 82  ? -25.886 7.529  15.902  1.00 21.09 ? 368 HIS   A CG  1 
ATOM   664  N ND1 . HIS   A 1 82  ? -27.153 7.637  16.428  1.00 21.20 ? 368 HIS   A ND1 1 
ATOM   665  C CD2 . HIS   A 1 82  ? -25.351 8.760  15.972  1.00 21.32 ? 368 HIS   A CD2 1 
ATOM   666  C CE1 . HIS   A 1 82  ? -27.361 8.897  16.804  1.00 21.48 ? 368 HIS   A CE1 1 
ATOM   667  N NE2 . HIS   A 1 82  ? -26.280 9.600  16.520  1.00 21.78 ? 368 HIS   A NE2 1 
ATOM   668  N N   . PHE   A 1 83  ? -23.670 5.039  12.890  1.00 18.59 ? 369 PHE   A N   1 
ATOM   669  C CA  . PHE   A 1 83  ? -22.843 4.023  12.271  1.00 19.22 ? 369 PHE   A CA  1 
ATOM   670  C C   . PHE   A 1 83  ? -21.457 4.601  12.034  1.00 19.45 ? 369 PHE   A C   1 
ATOM   671  O O   . PHE   A 1 83  ? -21.284 5.816  12.042  1.00 20.82 ? 369 PHE   A O   1 
ATOM   672  C CB  . PHE   A 1 83  ? -23.445 3.573  10.935  1.00 19.60 ? 369 PHE   A CB  1 
ATOM   673  C CG  . PHE   A 1 83  ? -23.870 4.718  10.021  1.00 19.54 ? 369 PHE   A CG  1 
ATOM   674  C CD1 . PHE   A 1 83  ? -22.949 5.352  9.197   1.00 20.14 ? 369 PHE   A CD1 1 
ATOM   675  C CD2 . PHE   A 1 83  ? -25.192 5.158  9.990   1.00 19.82 ? 369 PHE   A CD2 1 
ATOM   676  C CE1 . PHE   A 1 83  ? -23.334 6.411  8.390   1.00 19.81 ? 369 PHE   A CE1 1 
ATOM   677  C CE2 . PHE   A 1 83  ? -25.578 6.207  9.164   1.00 19.45 ? 369 PHE   A CE2 1 
ATOM   678  C CZ  . PHE   A 1 83  ? -24.647 6.836  8.374   1.00 19.47 ? 369 PHE   A CZ  1 
ATOM   679  N N   . LEU   A 1 84  ? -20.489 3.710  11.810  1.00 19.98 ? 370 LEU   A N   1 
ATOM   680  C CA  . LEU   A 1 84  ? -19.147 4.111  11.432  1.00 20.35 ? 370 LEU   A CA  1 
ATOM   681  C C   . LEU   A 1 84  ? -19.012 4.083  9.913   1.00 20.31 ? 370 LEU   A C   1 
ATOM   682  O O   . LEU   A 1 84  ? -19.653 3.286  9.224   1.00 22.04 ? 370 LEU   A O   1 
ATOM   683  C CB  . LEU   A 1 84  ? -18.114 3.200  12.086  1.00 21.04 ? 370 LEU   A CB  1 
ATOM   684  C CG  . LEU   A 1 84  ? -18.154 3.169  13.617  1.00 21.99 ? 370 LEU   A CG  1 
ATOM   685  C CD1 . LEU   A 1 84  ? -17.045 2.289  14.138  1.00 22.74 ? 370 LEU   A CD1 1 
ATOM   686  C CD2 . LEU   A 1 84  ? -18.062 4.572  14.209  1.00 23.10 ? 370 LEU   A CD2 1 
ATOM   687  N N   . LEU   A 1 85  ? -18.135 4.951  9.417   1.00 20.99 ? 371 LEU   A N   1 
ATOM   688  C CA  . LEU   A 1 85  ? -17.830 5.025  8.000   1.00 20.52 ? 371 LEU   A CA  1 
ATOM   689  C C   . LEU   A 1 85  ? -16.673 4.086  7.665   1.00 22.60 ? 371 LEU   A C   1 
ATOM   690  O O   . LEU   A 1 85  ? -15.578 4.550  7.369   1.00 27.71 ? 371 LEU   A O   1 
ATOM   691  C CB  . LEU   A 1 85  ? -17.469 6.466  7.652   1.00 19.65 ? 371 LEU   A CB  1 
ATOM   692  C CG  . LEU   A 1 85  ? -18.526 7.532  7.940   1.00 19.88 ? 371 LEU   A CG  1 
ATOM   693  C CD1 . LEU   A 1 85  ? -18.059 8.881  7.401   1.00 19.90 ? 371 LEU   A CD1 1 
ATOM   694  C CD2 . LEU   A 1 85  ? -19.884 7.179  7.374   1.00 20.96 ? 371 LEU   A CD2 1 
ATOM   695  N N   . SER   A 1 86  ? -16.908 2.778  7.719   1.00 25.37 ? 372 SER   A N   1 
ATOM   696  C CA  . SER   A 1 86  ? -15.868 1.819  7.382   1.00 26.53 ? 372 SER   A CA  1 
ATOM   697  C C   . SER   A 1 86  ? -16.187 1.211  6.023   1.00 26.00 ? 372 SER   A C   1 
ATOM   698  O O   . SER   A 1 86  ? -17.338 1.230  5.595   1.00 24.35 ? 372 SER   A O   1 
ATOM   699  C CB  . SER   A 1 86  ? -15.748 0.739  8.434   1.00 28.08 ? 372 SER   A CB  1 
ATOM   700  O OG  . SER   A 1 86  ? -16.826 -0.176 8.305   1.00 32.65 ? 372 SER   A OG  1 
ATOM   701  N N   A SER   A 1 87  ? -15.165 0.661  5.363   0.50 27.03 ? 373 SER   A N   1 
ATOM   702  N N   B SER   A 1 87  ? -15.157 0.664  5.366   0.50 26.19 ? 373 SER   A N   1 
ATOM   703  C CA  A SER   A 1 87  ? -15.373 -0.090 4.137   0.50 29.30 ? 373 SER   A CA  1 
ATOM   704  C CA  B SER   A 1 87  ? -15.343 -0.104 4.144   0.50 27.95 ? 373 SER   A CA  1 
ATOM   705  C C   A SER   A 1 87  ? -16.313 -1.267 4.393   0.50 31.00 ? 373 SER   A C   1 
ATOM   706  C C   B SER   A 1 87  ? -16.306 -1.263 4.394   0.50 30.45 ? 373 SER   A C   1 
ATOM   707  O O   A SER   A 1 87  ? -17.084 -1.650 3.515   0.50 33.90 ? 373 SER   A O   1 
ATOM   708  O O   B SER   A 1 87  ? -17.072 -1.640 3.510   0.50 33.47 ? 373 SER   A O   1 
ATOM   709  C CB  A SER   A 1 87  ? -14.060 -0.534 3.558   0.50 30.16 ? 373 SER   A CB  1 
ATOM   710  C CB  B SER   A 1 87  ? -14.028 -0.602 3.600   0.50 27.39 ? 373 SER   A CB  1 
ATOM   711  O OG  A SER   A 1 87  ? -13.262 0.601  3.248   0.50 30.80 ? 373 SER   A OG  1 
ATOM   712  O OG  B SER   A 1 87  ? -13.459 -1.581 4.456   0.50 26.18 ? 373 SER   A OG  1 
ATOM   713  N N   . LYS   A 1 88  ? -16.266 -1.814 5.612   1.00 32.29 ? 374 LYS   A N   1 
ATOM   714  C CA  . LYS   A 1 88  ? -17.184 -2.863 6.023   1.00 35.99 ? 374 LYS   A CA  1 
ATOM   715  C C   . LYS   A 1 88  ? -18.638 -2.405 5.927   1.00 37.28 ? 374 LYS   A C   1 
ATOM   716  O O   . LYS   A 1 88  ? -19.509 -3.202 5.587   1.00 41.59 ? 374 LYS   A O   1 
ATOM   717  C CB  . LYS   A 1 88  ? -16.872 -3.307 7.458   1.00 38.46 ? 374 LYS   A CB  1 
ATOM   718  C CG  . LYS   A 1 88  ? -15.607 -4.136 7.616   1.00 41.38 ? 374 LYS   A CG  1 
ATOM   719  C CD  . LYS   A 1 88  ? -15.620 -5.359 6.708   1.00 43.01 ? 374 LYS   A CD  1 
ATOM   720  C CE  . LYS   A 1 88  ? -14.907 -6.544 7.270   1.00 43.94 ? 374 LYS   A CE  1 
ATOM   721  N NZ  . LYS   A 1 88  ? -15.619 -7.774 6.906   1.00 45.30 ? 374 LYS   A NZ  1 
ATOM   722  N N   . SER   A 1 89  ? -18.893 -1.128 6.239   1.00 36.46 ? 375 SER   A N   1 
ATOM   723  C CA  . SER   A 1 89  ? -20.236 -0.572 6.229   1.00 35.28 ? 375 SER   A CA  1 
ATOM   724  C C   . SER   A 1 89  ? -20.536 0.109  4.883   1.00 32.46 ? 375 SER   A C   1 
ATOM   725  O O   . SER   A 1 89  ? -21.600 0.696  4.711   1.00 35.20 ? 375 SER   A O   1 
ATOM   726  C CB  . SER   A 1 89  ? -20.414 0.374  7.403   1.00 37.55 ? 375 SER   A CB  1 
ATOM   727  O OG  . SER   A 1 89  ? -20.212 -0.282 8.655   1.00 42.72 ? 375 SER   A OG  1 
ATOM   728  N N   . GLY   A 1 90  ? -19.590 0.045  3.936   1.00 27.11 ? 376 GLY   A N   1 
ATOM   729  C CA  . GLY   A 1 90  ? -19.804 0.484  2.562   1.00 24.70 ? 376 GLY   A CA  1 
ATOM   730  C C   . GLY   A 1 90  ? -19.298 1.899  2.285   1.00 21.16 ? 376 GLY   A C   1 
ATOM   731  O O   . GLY   A 1 90  ? -19.815 2.555  1.389   1.00 20.92 ? 376 GLY   A O   1 
ATOM   732  N N   . PHE   A 1 91  ? -18.262 2.354  3.000   1.00 19.22 ? 377 PHE   A N   1 
ATOM   733  C CA  . PHE   A 1 91  ? -17.754 3.711  2.840   1.00 18.38 ? 377 PHE   A CA  1 
ATOM   734  C C   . PHE   A 1 91  ? -16.257 3.693  2.559   1.00 18.59 ? 377 PHE   A C   1 
ATOM   735  O O   . PHE   A 1 91  ? -15.510 3.004  3.245   1.00 18.96 ? 377 PHE   A O   1 
ATOM   736  C CB  . PHE   A 1 91  ? -17.969 4.558  4.094   1.00 17.99 ? 377 PHE   A CB  1 
ATOM   737  C CG  . PHE   A 1 91  ? -19.429 4.792  4.428   1.00 18.08 ? 377 PHE   A CG  1 
ATOM   738  C CD1 . PHE   A 1 91  ? -20.120 5.884  3.918   1.00 18.04 ? 377 PHE   A CD1 1 
ATOM   739  C CD2 . PHE   A 1 91  ? -20.109 3.906  5.257   1.00 18.80 ? 377 PHE   A CD2 1 
ATOM   740  C CE1 . PHE   A 1 91  ? -21.456 6.077  4.225   1.00 18.86 ? 377 PHE   A CE1 1 
ATOM   741  C CE2 . PHE   A 1 91  ? -21.443 4.109  5.563   1.00 18.91 ? 377 PHE   A CE2 1 
ATOM   742  C CZ  . PHE   A 1 91  ? -22.106 5.200  5.067   1.00 19.10 ? 377 PHE   A CZ  1 
ATOM   743  N N   . TRP   A 1 92  ? -15.857 4.482  1.554   1.00 17.68 ? 378 TRP   A N   1 
ATOM   744  C CA  . TRP   A 1 92  ? -14.460 4.754  1.269   1.00 18.01 ? 378 TRP   A CA  1 
ATOM   745  C C   . TRP   A 1 92  ? -14.260 6.263  1.268   1.00 17.19 ? 378 TRP   A C   1 
ATOM   746  O O   . TRP   A 1 92  ? -14.617 6.937  0.295   1.00 16.76 ? 378 TRP   A O   1 
ATOM   747  C CB  . TRP   A 1 92  ? -14.061 4.129  -0.073  1.00 18.03 ? 378 TRP   A CB  1 
ATOM   748  C CG  . TRP   A 1 92  ? -14.248 2.640  -0.087  1.00 19.91 ? 378 TRP   A CG  1 
ATOM   749  C CD1 . TRP   A 1 92  ? -13.318 1.704  0.248   1.00 20.80 ? 378 TRP   A CD1 1 
ATOM   750  C CD2 . TRP   A 1 92  ? -15.461 1.917  -0.391  1.00 20.78 ? 378 TRP   A CD2 1 
ATOM   751  N NE1 . TRP   A 1 92  ? -13.854 0.450  0.150   1.00 21.95 ? 378 TRP   A NE1 1 
ATOM   752  C CE2 . TRP   A 1 92  ? -15.164 0.545  -0.233  1.00 21.67 ? 378 TRP   A CE2 1 
ATOM   753  C CE3 . TRP   A 1 92  ? -16.753 2.289  -0.777  1.00 21.77 ? 378 TRP   A CE3 1 
ATOM   754  C CZ2 . TRP   A 1 92  ? -16.114 -0.448 -0.456  1.00 21.87 ? 378 TRP   A CZ2 1 
ATOM   755  C CZ3 . TRP   A 1 92  ? -17.693 1.303  -0.991  1.00 22.58 ? 378 TRP   A CZ3 1 
ATOM   756  C CH2 . TRP   A 1 92  ? -17.369 -0.044 -0.847  1.00 22.70 ? 378 TRP   A CH2 1 
ATOM   757  N N   . THR   A 1 93  ? -13.770 6.792  2.398   1.00 16.51 ? 379 THR   A N   1 
ATOM   758  C CA  . THR   A 1 93  ? -13.717 8.237  2.570   1.00 16.08 ? 379 THR   A CA  1 
ATOM   759  C C   . THR   A 1 93  ? -12.412 8.652  3.230   1.00 15.62 ? 379 THR   A C   1 
ATOM   760  O O   . THR   A 1 93  ? -11.737 7.852  3.881   1.00 16.80 ? 379 THR   A O   1 
ATOM   761  C CB  . THR   A 1 93  ? -14.900 8.824  3.354   1.00 15.62 ? 379 THR   A CB  1 
ATOM   762  O OG1 . THR   A 1 93  ? -14.621 8.776  4.755   1.00 16.74 ? 379 THR   A OG1 1 
ATOM   763  C CG2 . THR   A 1 93  ? -16.234 8.180  3.032   1.00 15.81 ? 379 THR   A CG2 1 
ATOM   764  N N   . ILE   A 1 94  ? -12.090 9.932  3.044   1.00 15.20 ? 380 ILE   A N   1 
ATOM   765  C CA  . ILE   A 1 94  ? -11.115 10.629 3.868   1.00 15.58 ? 380 ILE   A CA  1 
ATOM   766  C C   . ILE   A 1 94  ? -11.818 11.818 4.513   1.00 15.55 ? 380 ILE   A C   1 
ATOM   767  O O   . ILE   A 1 94  ? -12.881 12.255 4.069   1.00 14.89 ? 380 ILE   A O   1 
ATOM   768  C CB  . ILE   A 1 94  ? -9.879  11.076 3.060   1.00 16.34 ? 380 ILE   A CB  1 
ATOM   769  C CG1 . ILE   A 1 94  ? -10.204 12.221 2.111   1.00 16.44 ? 380 ILE   A CG1 1 
ATOM   770  C CG2 . ILE   A 1 94  ? -9.233  9.883  2.353   1.00 16.99 ? 380 ILE   A CG2 1 
ATOM   771  C CD1 . ILE   A 1 94  ? -8.981  12.876 1.491   1.00 17.24 ? 380 ILE   A CD1 1 
ATOM   772  N N   . TRP   A 1 95  ? -11.201 12.358 5.562   1.00 15.31 ? 381 TRP   A N   1 
ATOM   773  C CA  . TRP   A 1 95  ? -11.811 13.473 6.258   1.00 15.52 ? 381 TRP   A CA  1 
ATOM   774  C C   . TRP   A 1 95  ? -10.769 14.374 6.896   1.00 15.24 ? 381 TRP   A C   1 
ATOM   775  O O   . TRP   A 1 95  ? -9.625  13.986 7.114   1.00 15.90 ? 381 TRP   A O   1 
ATOM   776  C CB  . TRP   A 1 95  ? -12.822 12.987 7.306   1.00 15.67 ? 381 TRP   A CB  1 
ATOM   777  C CG  . TRP   A 1 95  ? -12.272 12.179 8.454   1.00 16.04 ? 381 TRP   A CG  1 
ATOM   778  C CD1 . TRP   A 1 95  ? -11.762 12.625 9.640   1.00 16.55 ? 381 TRP   A CD1 1 
ATOM   779  C CD2 . TRP   A 1 95  ? -12.270 10.741 8.539   1.00 16.26 ? 381 TRP   A CD2 1 
ATOM   780  N NE1 . TRP   A 1 95  ? -11.426 11.567 10.441  1.00 16.80 ? 381 TRP   A NE1 1 
ATOM   781  C CE2 . TRP   A 1 95  ? -11.743 10.398 9.805   1.00 16.50 ? 381 TRP   A CE2 1 
ATOM   782  C CE3 . TRP   A 1 95  ? -12.671 9.715  7.676   1.00 16.76 ? 381 TRP   A CE3 1 
ATOM   783  C CZ2 . TRP   A 1 95  ? -11.588 9.075  10.203  1.00 18.09 ? 381 TRP   A CZ2 1 
ATOM   784  C CZ3 . TRP   A 1 95  ? -12.538 8.407  8.083   1.00 18.09 ? 381 TRP   A CZ3 1 
ATOM   785  C CH2 . TRP   A 1 95  ? -12.009 8.095  9.333   1.00 18.00 ? 381 TRP   A CH2 1 
ATOM   786  N N   . LEU   A 1 96  ? -11.250 15.586 7.170   1.00 15.82 ? 382 LEU   A N   1 
ATOM   787  C CA  . LEU   A 1 96  ? -10.617 16.544 8.048   1.00 15.88 ? 382 LEU   A CA  1 
ATOM   788  C C   . LEU   A 1 96  ? -11.460 16.651 9.309   1.00 15.98 ? 382 LEU   A C   1 
ATOM   789  O O   . LEU   A 1 96  ? -12.668 16.852 9.235   1.00 15.90 ? 382 LEU   A O   1 
ATOM   790  C CB  . LEU   A 1 96  ? -10.510 17.899 7.351   1.00 16.36 ? 382 LEU   A CB  1 
ATOM   791  C CG  . LEU   A 1 96  ? -10.055 19.069 8.232   1.00 16.37 ? 382 LEU   A CG  1 
ATOM   792  C CD1 . LEU   A 1 96  ? -8.641  18.852 8.731   1.00 16.70 ? 382 LEU   A CD1 1 
ATOM   793  C CD2 . LEU   A 1 96  ? -10.151 20.377 7.469   1.00 16.76 ? 382 LEU   A CD2 1 
ATOM   794  N N   . TRP   A 1 97  ? -10.766 16.547 10.442  1.00 18.26 ? 383 TRP   A N   1 
ATOM   795  C CA  . TRP   A 1 97  ? -11.347 16.735 11.760  1.00 21.99 ? 383 TRP   A CA  1 
ATOM   796  C C   . TRP   A 1 97  ? -10.585 17.859 12.464  1.00 24.54 ? 383 TRP   A C   1 
ATOM   797  O O   . TRP   A 1 97  ? -9.372  17.911 12.374  1.00 29.41 ? 383 TRP   A O   1 
ATOM   798  C CB  . TRP   A 1 97  ? -11.212 15.418 12.540  1.00 25.79 ? 383 TRP   A CB  1 
ATOM   799  C CG  . TRP   A 1 97  ? -12.039 15.360 13.788  1.00 29.04 ? 383 TRP   A CG  1 
ATOM   800  C CD1 . TRP   A 1 97  ? -11.620 15.489 15.081  1.00 30.95 ? 383 TRP   A CD1 1 
ATOM   801  C CD2 . TRP   A 1 97  ? -13.470 15.181 13.837  1.00 31.91 ? 383 TRP   A CD2 1 
ATOM   802  N NE1 . TRP   A 1 97  ? -12.688 15.392 15.932  1.00 33.45 ? 383 TRP   A NE1 1 
ATOM   803  C CE2 . TRP   A 1 97  ? -13.835 15.208 15.198  1.00 32.86 ? 383 TRP   A CE2 1 
ATOM   804  C CE3 . TRP   A 1 97  ? -14.466 15.003 12.870  1.00 33.70 ? 383 TRP   A CE3 1 
ATOM   805  C CZ2 . TRP   A 1 97  ? -15.159 15.057 15.609  1.00 35.73 ? 383 TRP   A CZ2 1 
ATOM   806  C CZ3 . TRP   A 1 97  ? -15.773 14.861 13.276  1.00 35.83 ? 383 TRP   A CZ3 1 
ATOM   807  C CH2 . TRP   A 1 97  ? -16.112 14.886 14.629  1.00 35.61 ? 383 TRP   A CH2 1 
ATOM   808  N N   . ASN   A 1 98  ? -11.269 18.759 13.174  1.00 30.25 ? 384 ASN   A N   1 
ATOM   809  C CA  . ASN   A 1 98  ? -10.594 19.658 14.102  1.00 35.53 ? 384 ASN   A CA  1 
ATOM   810  C C   . ASN   A 1 98  ? -9.515  20.510 13.426  1.00 40.08 ? 384 ASN   A C   1 
ATOM   811  O O   . ASN   A 1 98  ? -8.476  20.769 14.036  1.00 40.91 ? 384 ASN   A O   1 
ATOM   812  C CB  . ASN   A 1 98  ? -9.924  18.883 15.233  1.00 37.64 ? 384 ASN   A CB  1 
ATOM   813  C CG  . ASN   A 1 98  ? -9.865  19.676 16.518  1.00 41.63 ? 384 ASN   A CG  1 
ATOM   814  O OD1 . ASN   A 1 98  ? -10.520 20.720 16.640  1.00 46.77 ? 384 ASN   A OD1 1 
ATOM   815  N ND2 . ASN   A 1 98  ? -9.105  19.198 17.494  1.00 45.00 ? 384 ASN   A ND2 1 
ATOM   816  N N   . LYS   A 1 99  ? -9.753  20.943 12.179  1.00 41.83 ? 385 LYS   A N   1 
ATOM   817  C CA  . LYS   A 1 99  ? -8.930  21.954 11.525  1.00 42.96 ? 385 LYS   A CA  1 
ATOM   818  C C   . LYS   A 1 99  ? -7.589  21.410 11.019  1.00 43.31 ? 385 LYS   A C   1 
ATOM   819  O O   . LYS   A 1 99  ? -7.107  21.901 10.002  1.00 46.67 ? 385 LYS   A O   1 
ATOM   820  C CB  . LYS   A 1 99  ? -8.695  23.156 12.454  1.00 44.57 ? 385 LYS   A CB  1 
ATOM   821  N N   . GLN   A 1 100 ? -6.969  20.427 11.696  1.00 40.72 ? 386 GLN   A N   1 
ATOM   822  C CA  . GLN   A 1 100 ? -5.611  20.036 11.337  1.00 37.89 ? 386 GLN   A CA  1 
ATOM   823  C C   . GLN   A 1 100 ? -5.455  18.534 11.084  1.00 32.83 ? 386 GLN   A C   1 
ATOM   824  O O   . GLN   A 1 100 ? -4.436  18.121 10.534  1.00 33.39 ? 386 GLN   A O   1 
ATOM   825  C CB  . GLN   A 1 100 ? -4.647  20.455 12.447  1.00 40.15 ? 386 GLN   A CB  1 
ATOM   826  N N   . LYS   A 1 101 ? -6.437  17.716 11.481  1.00 27.61 ? 387 LYS   A N   1 
ATOM   827  C CA  . LYS   A 1 101 ? -6.241  16.277 11.514  1.00 24.80 ? 387 LYS   A CA  1 
ATOM   828  C C   . LYS   A 1 101 ? -6.938  15.653 10.309  1.00 20.31 ? 387 LYS   A C   1 
ATOM   829  O O   . LYS   A 1 101 ? -8.159  15.569 10.290  1.00 20.28 ? 387 LYS   A O   1 
ATOM   830  C CB  . LYS   A 1 101 ? -6.740  15.682 12.840  1.00 26.79 ? 387 LYS   A CB  1 
ATOM   831  C CG  . LYS   A 1 101 ? -6.247  16.382 14.110  1.00 30.10 ? 387 LYS   A CG  1 
ATOM   832  N N   . TYR   A 1 102 ? -6.142  15.231 9.321   1.00 18.82 ? 388 TYR   A N   1 
ATOM   833  C CA  . TYR   A 1 102 ? -6.648  14.532 8.152   1.00 17.57 ? 388 TYR   A CA  1 
ATOM   834  C C   . TYR   A 1 102 ? -6.461  13.031 8.363   1.00 17.77 ? 388 TYR   A C   1 
ATOM   835  O O   . TYR   A 1 102 ? -5.427  12.609 8.879   1.00 19.01 ? 388 TYR   A O   1 
ATOM   836  C CB  . TYR   A 1 102 ? -5.921  14.984 6.877   1.00 17.70 ? 388 TYR   A CB  1 
ATOM   837  C CG  . TYR   A 1 102 ? -6.108  16.452 6.511   1.00 16.66 ? 388 TYR   A CG  1 
ATOM   838  C CD1 . TYR   A 1 102 ? -5.251  17.429 6.995   1.00 17.14 ? 388 TYR   A CD1 1 
ATOM   839  C CD2 . TYR   A 1 102 ? -7.143  16.865 5.676   1.00 16.95 ? 388 TYR   A CD2 1 
ATOM   840  C CE1 . TYR   A 1 102 ? -5.403  18.765 6.654   1.00 17.69 ? 388 TYR   A CE1 1 
ATOM   841  C CE2 . TYR   A 1 102 ? -7.328  18.200 5.354   1.00 16.45 ? 388 TYR   A CE2 1 
ATOM   842  C CZ  . TYR   A 1 102 ? -6.452  19.157 5.842   1.00 17.08 ? 388 TYR   A CZ  1 
ATOM   843  O OH  . TYR   A 1 102 ? -6.593  20.482 5.553   1.00 17.65 ? 388 TYR   A OH  1 
ATOM   844  N N   . GLU   A 1 103 ? -7.445  12.240 7.919   1.00 17.24 ? 389 GLU   A N   1 
ATOM   845  C CA  . GLU   A 1 103 ? -7.422  10.796 8.096   1.00 18.20 ? 389 GLU   A CA  1 
ATOM   846  C C   . GLU   A 1 103 ? -8.083  10.097 6.916   1.00 17.29 ? 389 GLU   A C   1 
ATOM   847  O O   . GLU   A 1 103 ? -9.022  10.638 6.339   1.00 16.55 ? 389 GLU   A O   1 
ATOM   848  C CB  . GLU   A 1 103 ? -8.276  10.427 9.308   1.00 20.11 ? 389 GLU   A CB  1 
ATOM   849  C CG  . GLU   A 1 103 ? -7.854  11.122 10.596  1.00 22.28 ? 389 GLU   A CG  1 
ATOM   850  C CD  . GLU   A 1 103 ? -6.641  10.549 11.302  1.00 23.81 ? 389 GLU   A CD  1 
ATOM   851  O OE1 . GLU   A 1 103 ? -6.116  11.286 12.159  1.00 30.22 ? 389 GLU   A OE1 1 
ATOM   852  O OE2 . GLU   A 1 103 ? -6.251  9.394  11.043  1.00 27.13 ? 389 GLU   A OE2 1 
ATOM   853  N N   . ALA   A 1 104 ? -7.615  8.881  6.617   1.00 17.01 ? 390 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 104 ? -8.298  7.974  5.711   1.00 17.42 ? 390 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 104 ? -9.041  6.903  6.505   1.00 17.17 ? 390 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 104 ? -8.501  6.370  7.483   1.00 18.11 ? 390 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 104 ? -7.314  7.335  4.763   1.00 18.66 ? 390 ALA   A CB  1 
ATOM   858  N N   . GLY   A 1 105 ? -10.241 6.555  6.019   1.00 17.46 ? 391 GLY   A N   1 
ATOM   859  C CA  . GLY   A 1 105 ? -11.161 5.652  6.689   1.00 17.88 ? 391 GLY   A CA  1 
ATOM   860  C C   . GLY   A 1 105 ? -10.810 4.175  6.521   1.00 18.48 ? 391 GLY   A C   1 
ATOM   861  O O   . GLY   A 1 105 ? -11.676 3.374  6.185   1.00 19.45 ? 391 GLY   A O   1 
ATOM   862  N N   . THR   A 1 106 ? -9.546  3.825  6.784   1.00 20.28 ? 392 THR   A N   1 
ATOM   863  C CA  . THR   A 1 106 ? -9.122  2.446  6.946   1.00 21.13 ? 392 THR   A CA  1 
ATOM   864  C C   . THR   A 1 106 ? -9.428  2.017  8.380   1.00 21.59 ? 392 THR   A C   1 
ATOM   865  O O   . THR   A 1 106 ? -9.639  2.862  9.248   1.00 22.16 ? 392 THR   A O   1 
ATOM   866  C CB  . THR   A 1 106 ? -7.626  2.326  6.650   1.00 21.82 ? 392 THR   A CB  1 
ATOM   867  O OG1 . THR   A 1 106 ? -6.924  3.239  7.487   1.00 21.31 ? 392 THR   A OG1 1 
ATOM   868  C CG2 . THR   A 1 106 ? -7.278  2.661  5.213   1.00 22.70 ? 392 THR   A CG2 1 
ATOM   869  N N   . TYR   A 1 107 ? -9.431  0.703  8.625   1.00 22.60 ? 393 TYR   A N   1 
ATOM   870  C CA  . TYR   A 1 107 ? -9.389  0.225  9.994   1.00 24.76 ? 393 TYR   A CA  1 
ATOM   871  C C   . TYR   A 1 107 ? -8.061  -0.458 10.303  1.00 27.77 ? 393 TYR   A C   1 
ATOM   872  O O   . TYR   A 1 107 ? -7.711  -1.404 9.606   1.00 29.35 ? 393 TYR   A O   1 
ATOM   873  C CB  . TYR   A 1 107 ? -10.535 -0.735 10.328  1.00 24.74 ? 393 TYR   A CB  1 
ATOM   874  C CG  . TYR   A 1 107 ? -10.238 -1.542 11.583  1.00 24.85 ? 393 TYR   A CG  1 
ATOM   875  C CD1 . TYR   A 1 107 ? -10.117 -0.923 12.824  1.00 24.17 ? 393 TYR   A CD1 1 
ATOM   876  C CD2 . TYR   A 1 107 ? -10.058 -2.919 11.526  1.00 25.34 ? 393 TYR   A CD2 1 
ATOM   877  C CE1 . TYR   A 1 107 ? -9.806  -1.648 13.963  1.00 24.66 ? 393 TYR   A CE1 1 
ATOM   878  C CE2 . TYR   A 1 107 ? -9.757  -3.655 12.660  1.00 25.58 ? 393 TYR   A CE2 1 
ATOM   879  C CZ  . TYR   A 1 107 ? -9.635  -3.019 13.882  1.00 24.63 ? 393 TYR   A CZ  1 
ATOM   880  O OH  . TYR   A 1 107 ? -9.349  -3.763 14.990  1.00 26.65 ? 393 TYR   A OH  1 
ATOM   881  N N   . PRO   A 1 108 ? -7.273  0.013  11.304  1.00 30.08 ? 394 PRO   A N   1 
ATOM   882  C CA  . PRO   A 1 108 ? -7.496  1.301  11.956  1.00 30.01 ? 394 PRO   A CA  1 
ATOM   883  C C   . PRO   A 1 108 ? -7.260  2.481  11.015  1.00 28.75 ? 394 PRO   A C   1 
ATOM   884  O O   . PRO   A 1 108 ? -6.741  2.280  9.919   1.00 29.70 ? 394 PRO   A O   1 
ATOM   885  C CB  . PRO   A 1 108 ? -6.498  1.302  13.113  1.00 31.78 ? 394 PRO   A CB  1 
ATOM   886  C CG  . PRO   A 1 108 ? -5.393  0.408  12.586  1.00 33.77 ? 394 PRO   A CG  1 
ATOM   887  C CD  . PRO   A 1 108 ? -6.103  -0.689 11.853  1.00 32.14 ? 394 PRO   A CD  1 
ATOM   888  N N   . GLN   A 1 109 ? -7.650  3.693  11.446  1.00 27.72 ? 395 GLN   A N   1 
ATOM   889  C CA  . GLN   A 1 109 ? -7.575  4.878  10.601  1.00 27.60 ? 395 GLN   A CA  1 
ATOM   890  C C   . GLN   A 1 109 ? -6.114  5.138  10.249  1.00 25.89 ? 395 GLN   A C   1 
ATOM   891  O O   . GLN   A 1 109 ? -5.214  4.810  11.021  1.00 26.11 ? 395 GLN   A O   1 
ATOM   892  C CB  . GLN   A 1 109 ? -8.250  6.115  11.208  1.00 31.00 ? 395 GLN   A CB  1 
ATOM   893  C CG  . GLN   A 1 109 ? -7.582  6.689  12.453  1.00 33.68 ? 395 GLN   A CG  1 
ATOM   894  C CD  . GLN   A 1 109 ? -8.317  7.891  13.017  1.00 37.37 ? 395 GLN   A CD  1 
ATOM   895  O OE1 . GLN   A 1 109 ? -9.475  8.161  12.684  1.00 38.18 ? 395 GLN   A OE1 1 
ATOM   896  N NE2 . GLN   A 1 109 ? -7.646  8.635  13.884  1.00 41.06 ? 395 GLN   A NE2 1 
ATOM   897  N N   . THR   A 1 110 ? -5.905  5.673  9.045   1.00 24.15 ? 396 THR   A N   1 
ATOM   898  C CA  . THR   A 1 110 ? -4.595  6.044  8.538   1.00 23.09 ? 396 THR   A CA  1 
ATOM   899  C C   . THR   A 1 110 ? -4.479  7.561  8.647   1.00 22.50 ? 396 THR   A C   1 
ATOM   900  O O   . THR   A 1 110 ? -5.176  8.297  7.954   1.00 21.76 ? 396 THR   A O   1 
ATOM   901  C CB  . THR   A 1 110 ? -4.436  5.571  7.090   1.00 23.82 ? 396 THR   A CB  1 
ATOM   902  O OG1 . THR   A 1 110 ? -4.444  4.146  7.068   1.00 24.42 ? 396 THR   A OG1 1 
ATOM   903  C CG2 . THR   A 1 110 ? -3.138  6.051  6.469   1.00 24.53 ? 396 THR   A CG2 1 
ATOM   904  N N   . PRO   A 1 111 ? -3.621  8.100  9.536   1.00 23.26 ? 397 PRO   A N   1 
ATOM   905  C CA  . PRO   A 1 111 ? -3.364  9.531  9.554   1.00 24.58 ? 397 PRO   A CA  1 
ATOM   906  C C   . PRO   A 1 111 ? -2.704  9.995  8.267   1.00 24.09 ? 397 PRO   A C   1 
ATOM   907  O O   . PRO   A 1 111 ? -1.825  9.318  7.736   1.00 25.91 ? 397 PRO   A O   1 
ATOM   908  C CB  . PRO   A 1 111 ? -2.450  9.730  10.757  1.00 25.43 ? 397 PRO   A CB  1 
ATOM   909  C CG  . PRO   A 1 111 ? -2.654  8.471  11.572  1.00 25.94 ? 397 PRO   A CG  1 
ATOM   910  C CD  . PRO   A 1 111 ? -2.877  7.385  10.579  1.00 25.11 ? 397 PRO   A CD  1 
ATOM   911  N N   . LEU   A 1 112 ? -3.160  11.142 7.770   1.00 23.65 ? 398 LEU   A N   1 
ATOM   912  C CA  . LEU   A 1 112 ? -2.652  11.703 6.533   1.00 23.45 ? 398 LEU   A CA  1 
ATOM   913  C C   . LEU   A 1 112 ? -1.900  12.975 6.899   1.00 26.63 ? 398 LEU   A C   1 
ATOM   914  O O   . LEU   A 1 112 ? -2.426  13.827 7.619   1.00 30.67 ? 398 LEU   A O   1 
ATOM   915  C CB  . LEU   A 1 112 ? -3.814  11.984 5.581   1.00 22.36 ? 398 LEU   A CB  1 
ATOM   916  C CG  . LEU   A 1 112 ? -4.719  10.792 5.255   1.00 21.45 ? 398 LEU   A CG  1 
ATOM   917  C CD1 . LEU   A 1 112 ? -5.953  11.270 4.504   1.00 20.85 ? 398 LEU   A CD1 1 
ATOM   918  C CD2 . LEU   A 1 112 ? -3.966  9.739  4.458   1.00 22.45 ? 398 LEU   A CD2 1 
ATOM   919  N N   . HIS   A 1 113 ? -0.660  13.079 6.431   1.00 28.05 ? 399 HIS   A N   1 
ATOM   920  C CA  . HIS   A 1 113 ? 0.189   14.189 6.825   1.00 29.40 ? 399 HIS   A CA  1 
ATOM   921  C C   . HIS   A 1 113 ? 0.290   15.125 5.631   1.00 29.53 ? 399 HIS   A C   1 
ATOM   922  O O   . HIS   A 1 113 ? 1.050   14.860 4.710   1.00 31.60 ? 399 HIS   A O   1 
ATOM   923  C CB  . HIS   A 1 113 ? 1.511   13.657 7.380   1.00 31.61 ? 399 HIS   A CB  1 
ATOM   924  C CG  . HIS   A 1 113 ? 1.280   12.677 8.482   1.00 32.87 ? 399 HIS   A CG  1 
ATOM   925  N ND1 . HIS   A 1 113 ? 0.798   13.049 9.720   1.00 35.58 ? 399 HIS   A ND1 1 
ATOM   926  C CD2 . HIS   A 1 113 ? 1.420   11.345 8.526   1.00 34.35 ? 399 HIS   A CD2 1 
ATOM   927  C CE1 . HIS   A 1 113 ? 0.674   11.976 10.485  1.00 35.08 ? 399 HIS   A CE1 1 
ATOM   928  N NE2 . HIS   A 1 113 ? 1.062   10.930 9.787   1.00 35.29 ? 399 HIS   A NE2 1 
ATOM   929  N N   . LEU   A 1 114 ? -0.544  16.173 5.655   1.00 29.14 ? 400 LEU   A N   1 
ATOM   930  C CA  . LEU   A 1 114 ? -0.645  17.148 4.584   1.00 29.61 ? 400 LEU   A CA  1 
ATOM   931  C C   . LEU   A 1 114 ? 0.035   18.443 5.027   1.00 31.62 ? 400 LEU   A C   1 
ATOM   932  O O   . LEU   A 1 114 ? -0.534  19.212 5.795   1.00 35.94 ? 400 LEU   A O   1 
ATOM   933  C CB  . LEU   A 1 114 ? -2.128  17.370 4.287   1.00 27.85 ? 400 LEU   A CB  1 
ATOM   934  C CG  . LEU   A 1 114 ? -2.840  16.297 3.463   1.00 29.63 ? 400 LEU   A CG  1 
ATOM   935  C CD1 . LEU   A 1 114 ? -2.741  14.899 3.989   1.00 33.26 ? 400 LEU   A CD1 1 
ATOM   936  C CD2 . LEU   A 1 114 ? -4.307  16.685 3.276   1.00 25.76 ? 400 LEU   A CD2 1 
ATOM   937  N N   . GLN   A 1 115 ? 1.242   18.693 4.521   1.00 32.77 ? 401 GLN   A N   1 
ATOM   938  C CA  . GLN   A 1 115 ? 1.955   19.923 4.823   1.00 34.13 ? 401 GLN   A CA  1 
ATOM   939  C C   . GLN   A 1 115 ? 1.240   21.127 4.217   1.00 30.76 ? 401 GLN   A C   1 
ATOM   940  O O   . GLN   A 1 115 ? 1.342   22.227 4.756   1.00 30.56 ? 401 GLN   A O   1 
ATOM   941  C CB  . GLN   A 1 115 ? 3.374   19.920 4.260   1.00 39.30 ? 401 GLN   A CB  1 
ATOM   942  C CG  . GLN   A 1 115 ? 4.280   18.841 4.839   1.00 43.80 ? 401 GLN   A CG  1 
ATOM   943  C CD  . GLN   A 1 115 ? 5.728   19.063 4.461   1.00 49.71 ? 401 GLN   A CD  1 
ATOM   944  O OE1 . GLN   A 1 115 ? 6.419   19.903 5.049   1.00 55.75 ? 401 GLN   A OE1 1 
ATOM   945  N NE2 . GLN   A 1 115 ? 6.201   18.323 3.468   1.00 52.91 ? 401 GLN   A NE2 1 
ATOM   946  N N   . VAL   A 1 116 ? 0.556   20.919 3.081   1.00 28.21 ? 402 VAL   A N   1 
ATOM   947  C CA  . VAL   A 1 116 ? -0.228  21.972 2.451   1.00 25.48 ? 402 VAL   A CA  1 
ATOM   948  C C   . VAL   A 1 116 ? -1.709  21.625 2.593   1.00 23.05 ? 402 VAL   A C   1 
ATOM   949  O O   . VAL   A 1 116 ? -2.199  20.723 1.915   1.00 25.14 ? 402 VAL   A O   1 
ATOM   950  C CB  . VAL   A 1 116 ? 0.173   22.164 0.976   1.00 27.45 ? 402 VAL   A CB  1 
ATOM   951  C CG1 . VAL   A 1 116 ? -0.689  23.208 0.277   1.00 28.44 ? 402 VAL   A CG1 1 
ATOM   952  C CG2 . VAL   A 1 116 ? 1.646   22.516 0.836   1.00 27.66 ? 402 VAL   A CG2 1 
ATOM   953  N N   . PRO   A 1 117 ? -2.491  22.323 3.449   1.00 22.29 ? 403 PRO   A N   1 
ATOM   954  C CA  . PRO   A 1 117 ? -3.915  22.031 3.572   1.00 21.59 ? 403 PRO   A CA  1 
ATOM   955  C C   . PRO   A 1 117 ? -4.672  22.251 2.269   1.00 19.65 ? 403 PRO   A C   1 
ATOM   956  O O   . PRO   A 1 117 ? -4.569  23.325 1.672   1.00 21.06 ? 403 PRO   A O   1 
ATOM   957  C CB  . PRO   A 1 117 ? -4.420  23.020 4.616   1.00 23.07 ? 403 PRO   A CB  1 
ATOM   958  C CG  . PRO   A 1 117 ? -3.176  23.425 5.353   1.00 24.51 ? 403 PRO   A CG  1 
ATOM   959  C CD  . PRO   A 1 117 ? -2.057  23.386 4.370   1.00 23.25 ? 403 PRO   A CD  1 
ATOM   960  N N   . PRO   A 1 118 ? -5.422  21.252 1.756   1.00 17.50 ? 404 PRO   A N   1 
ATOM   961  C CA  . PRO   A 1 118 ? -6.129  21.449 0.497   1.00 16.84 ? 404 PRO   A CA  1 
ATOM   962  C C   . PRO   A 1 118 ? -7.290  22.427 0.603   1.00 16.68 ? 404 PRO   A C   1 
ATOM   963  O O   . PRO   A 1 118 ? -8.066  22.364 1.557   1.00 17.77 ? 404 PRO   A O   1 
ATOM   964  C CB  . PRO   A 1 118 ? -6.628  20.068 0.113   1.00 17.62 ? 404 PRO   A CB  1 
ATOM   965  C CG  . PRO   A 1 118 ? -6.561  19.246 1.380   1.00 17.34 ? 404 PRO   A CG  1 
ATOM   966  C CD  . PRO   A 1 118 ? -5.547  19.883 2.281   1.00 17.34 ? 404 PRO   A CD  1 
ATOM   967  N N   . CYS   A 1 119 ? -7.398  23.313 -0.404  1.00 16.06 ? 405 CYS   A N   1 
ATOM   968  C CA  . CYS   A 1 119 ? -8.605  24.094 -0.618  1.00 16.01 ? 405 CYS   A CA  1 
ATOM   969  C C   . CYS   A 1 119 ? -9.514  23.413 -1.632  1.00 15.16 ? 405 CYS   A C   1 
ATOM   970  O O   . CYS   A 1 119 ? -10.716 23.644 -1.623  1.00 15.10 ? 405 CYS   A O   1 
ATOM   971  C CB  . CYS   A 1 119 ? -8.311  25.514 -1.065  1.00 17.15 ? 405 CYS   A CB  1 
ATOM   972  S SG  . CYS   A 1 119 ? -7.475  26.521 0.182   1.00 21.31 ? 405 CYS   A SG  1 
ATOM   973  N N   . GLN   A 1 120 ? -8.924  22.589 -2.505  1.00 15.36 ? 406 GLN   A N   1 
ATOM   974  C CA  . GLN   A 1 120 ? -9.700  21.752 -3.407  1.00 15.44 ? 406 GLN   A CA  1 
ATOM   975  C C   . GLN   A 1 120 ? -9.123  20.347 -3.381  1.00 14.90 ? 406 GLN   A C   1 
ATOM   976  O O   . GLN   A 1 120 ? -7.907  20.170 -3.309  1.00 16.26 ? 406 GLN   A O   1 
ATOM   977  C CB  . GLN   A 1 120 ? -9.770  22.223 -4.863  1.00 16.27 ? 406 GLN   A CB  1 
ATOM   978  C CG  . GLN   A 1 120 ? -10.373 23.610 -5.045  1.00 17.06 ? 406 GLN   A CG  1 
ATOM   979  C CD  . GLN   A 1 120 ? -9.355  24.716 -4.875  1.00 17.91 ? 406 GLN   A CD  1 
ATOM   980  O OE1 . GLN   A 1 120 ? -8.181  24.575 -5.238  1.00 19.02 ? 406 GLN   A OE1 1 
ATOM   981  N NE2 . GLN   A 1 120 ? -9.788  25.821 -4.283  1.00 18.68 ? 406 GLN   A NE2 1 
ATOM   982  N N   . VAL   A 1 121 ? -10.034 19.373 -3.434  1.00 14.82 ? 407 VAL   A N   1 
ATOM   983  C CA  . VAL   A 1 121 ? -9.708  17.960 -3.419  1.00 15.27 ? 407 VAL   A CA  1 
ATOM   984  C C   . VAL   A 1 121 ? -10.248 17.354 -4.711  1.00 14.96 ? 407 VAL   A C   1 
ATOM   985  O O   . VAL   A 1 121 ? -11.400 17.582 -5.059  1.00 16.31 ? 407 VAL   A O   1 
ATOM   986  C CB  . VAL   A 1 121 ? -10.294 17.257 -2.178  1.00 15.36 ? 407 VAL   A CB  1 
ATOM   987  C CG1 . VAL   A 1 121 ? -10.014 15.758 -2.187  1.00 16.40 ? 407 VAL   A CG1 1 
ATOM   988  C CG2 . VAL   A 1 121 ? -9.766  17.912 -0.911  1.00 15.51 ? 407 VAL   A CG2 1 
ATOM   989  N N   . GLY   A 1 122 ? -9.417  16.556 -5.377  1.00 15.38 ? 408 GLY   A N   1 
ATOM   990  C CA  . GLY   A 1 122 ? -9.839  15.797 -6.541  1.00 15.96 ? 408 GLY   A CA  1 
ATOM   991  C C   . GLY   A 1 122 ? -10.087 14.343 -6.165  1.00 16.03 ? 408 GLY   A C   1 
ATOM   992  O O   . GLY   A 1 122 ? -9.283  13.753 -5.449  1.00 17.69 ? 408 GLY   A O   1 
ATOM   993  N N   . ILE   A 1 123 ? -11.223 13.800 -6.607  1.00 16.82 ? 409 ILE   A N   1 
ATOM   994  C CA  . ILE   A 1 123 ? -11.633 12.453 -6.239  1.00 17.36 ? 409 ILE   A CA  1 
ATOM   995  C C   . ILE   A 1 123 ? -11.792 11.635 -7.514  1.00 18.00 ? 409 ILE   A C   1 
ATOM   996  O O   . ILE   A 1 123 ? -12.564 12.008 -8.391  1.00 18.17 ? 409 ILE   A O   1 
ATOM   997  C CB  . ILE   A 1 123 ? -12.936 12.454 -5.418  1.00 18.63 ? 409 ILE   A CB  1 
ATOM   998  C CG1 . ILE   A 1 123 ? -12.815 13.300 -4.138  1.00 20.09 ? 409 ILE   A CG1 1 
ATOM   999  C CG2 . ILE   A 1 123 ? -13.382 11.027 -5.110  1.00 19.46 ? 409 ILE   A CG2 1 
ATOM   1000 C CD1 . ILE   A 1 123 ? -13.495 14.651 -4.186  1.00 23.03 ? 409 ILE   A CD1 1 
ATOM   1001 N N   . PHE   A 1 124 ? -11.064 10.520 -7.584  1.00 17.88 ? 410 PHE   A N   1 
ATOM   1002 C CA  . PHE   A 1 124 ? -11.191 9.578  -8.678  1.00 18.59 ? 410 PHE   A CA  1 
ATOM   1003 C C   . PHE   A 1 124 ? -11.759 8.261  -8.176  1.00 18.37 ? 410 PHE   A C   1 
ATOM   1004 O O   . PHE   A 1 124 ? -11.291 7.725  -7.172  1.00 20.32 ? 410 PHE   A O   1 
ATOM   1005 C CB  . PHE   A 1 124 ? -9.847  9.226  -9.319  1.00 20.30 ? 410 PHE   A CB  1 
ATOM   1006 C CG  . PHE   A 1 124 ? -9.180  10.307 -10.151 1.00 21.53 ? 410 PHE   A CG  1 
ATOM   1007 C CD1 . PHE   A 1 124 ? -8.317  11.233 -9.577  1.00 22.55 ? 410 PHE   A CD1 1 
ATOM   1008 C CD2 . PHE   A 1 124 ? -9.375  10.350 -11.524 1.00 22.92 ? 410 PHE   A CD2 1 
ATOM   1009 C CE1 . PHE   A 1 124 ? -7.688  12.193 -10.356 1.00 23.95 ? 410 PHE   A CE1 1 
ATOM   1010 C CE2 . PHE   A 1 124 ? -8.745  11.309 -12.294 1.00 24.12 ? 410 PHE   A CE2 1 
ATOM   1011 C CZ  . PHE   A 1 124 ? -7.905  12.228 -11.711 1.00 24.56 ? 410 PHE   A CZ  1 
ATOM   1012 N N   . LEU   A 1 125 ? -12.741 7.740  -8.915  1.00 19.10 ? 411 LEU   A N   1 
ATOM   1013 C CA  . LEU   A 1 125 ? -13.230 6.384  -8.751  1.00 20.47 ? 411 LEU   A CA  1 
ATOM   1014 C C   . LEU   A 1 125 ? -12.919 5.598  -10.023 1.00 21.94 ? 411 LEU   A C   1 
ATOM   1015 O O   . LEU   A 1 125 ? -13.262 6.031  -11.116 1.00 23.03 ? 411 LEU   A O   1 
ATOM   1016 C CB  . LEU   A 1 125 ? -14.730 6.405  -8.469  1.00 20.42 ? 411 LEU   A CB  1 
ATOM   1017 C CG  . LEU   A 1 125 ? -15.450 5.058  -8.591  1.00 22.07 ? 411 LEU   A CG  1 
ATOM   1018 C CD1 . LEU   A 1 125 ? -14.989 4.090  -7.514  1.00 21.70 ? 411 LEU   A CD1 1 
ATOM   1019 C CD2 . LEU   A 1 125 ? -16.960 5.238  -8.560  1.00 23.84 ? 411 LEU   A CD2 1 
ATOM   1020 N N   . ASP   A 1 126 ? -12.259 4.449  -9.855  1.00 23.22 ? 412 ASP   A N   1 
ATOM   1021 C CA  . ASP   A 1 126 ? -12.043 3.483  -10.919 1.00 24.04 ? 412 ASP   A CA  1 
ATOM   1022 C C   . ASP   A 1 126 ? -12.744 2.201  -10.487 1.00 24.55 ? 412 ASP   A C   1 
ATOM   1023 O O   . ASP   A 1 126 ? -12.201 1.432  -9.694  1.00 23.96 ? 412 ASP   A O   1 
ATOM   1024 C CB  . ASP   A 1 126 ? -10.555 3.291  -11.155 1.00 25.97 ? 412 ASP   A CB  1 
ATOM   1025 C CG  . ASP   A 1 126 ? -10.155 2.350  -12.278 1.00 28.60 ? 412 ASP   A CG  1 
ATOM   1026 O OD1 . ASP   A 1 126 ? -11.032 1.610  -12.772 1.00 30.78 ? 412 ASP   A OD1 1 
ATOM   1027 O OD2 . ASP   A 1 126 ? -8.963  2.379  -12.646 1.00 32.70 ? 412 ASP   A OD2 1 
ATOM   1028 N N   . TYR   A 1 127 ? -13.969 2.013  -10.987 1.00 24.74 ? 413 TYR   A N   1 
ATOM   1029 C CA  . TYR   A 1 127 ? -14.837 0.945  -10.527 1.00 24.86 ? 413 TYR   A CA  1 
ATOM   1030 C C   . TYR   A 1 127 ? -14.173 -0.412 -10.758 1.00 26.24 ? 413 TYR   A C   1 
ATOM   1031 O O   . TYR   A 1 127 ? -14.116 -1.239 -9.847  1.00 26.65 ? 413 TYR   A O   1 
ATOM   1032 C CB  . TYR   A 1 127 ? -16.214 1.038  -11.192 1.00 25.18 ? 413 TYR   A CB  1 
ATOM   1033 C CG  . TYR   A 1 127 ? -17.213 0.088  -10.549 1.00 25.61 ? 413 TYR   A CG  1 
ATOM   1034 C CD1 . TYR   A 1 127 ? -17.151 -1.288 -10.763 1.00 26.73 ? 413 TYR   A CD1 1 
ATOM   1035 C CD2 . TYR   A 1 127 ? -18.206 0.563  -9.707  1.00 25.38 ? 413 TYR   A CD2 1 
ATOM   1036 C CE1 . TYR   A 1 127 ? -18.044 -2.154 -10.153 1.00 26.78 ? 413 TYR   A CE1 1 
ATOM   1037 C CE2 . TYR   A 1 127 ? -19.108 -0.293 -9.099  1.00 26.21 ? 413 TYR   A CE2 1 
ATOM   1038 C CZ  . TYR   A 1 127 ? -19.032 -1.654 -9.326  1.00 26.98 ? 413 TYR   A CZ  1 
ATOM   1039 O OH  . TYR   A 1 127 ? -19.918 -2.485 -8.709  1.00 28.42 ? 413 TYR   A OH  1 
ATOM   1040 N N   . GLU   A 1 128 ? -13.690 -0.653 -11.983 1.00 27.77 ? 414 GLU   A N   1 
ATOM   1041 C CA  . GLU   A 1 128 ? -13.188 -1.974 -12.338 1.00 29.85 ? 414 GLU   A CA  1 
ATOM   1042 C C   . GLU   A 1 128 ? -11.897 -2.291 -11.580 1.00 28.67 ? 414 GLU   A C   1 
ATOM   1043 O O   . GLU   A 1 128 ? -11.692 -3.434 -11.176 1.00 30.65 ? 414 GLU   A O   1 
ATOM   1044 C CB  . GLU   A 1 128 ? -13.028 -2.152 -13.846 1.00 31.71 ? 414 GLU   A CB  1 
ATOM   1045 C CG  . GLU   A 1 128 ? -14.317 -2.606 -14.528 1.00 34.74 ? 414 GLU   A CG  1 
ATOM   1046 C CD  . GLU   A 1 128 ? -15.405 -1.560 -14.610 1.00 39.43 ? 414 GLU   A CD  1 
ATOM   1047 O OE1 . GLU   A 1 128 ? -16.576 -1.962 -14.751 1.00 44.93 ? 414 GLU   A OE1 1 
ATOM   1048 O OE2 . GLU   A 1 128 ? -15.086 -0.351 -14.551 1.00 45.06 ? 414 GLU   A OE2 1 
ATOM   1049 N N   . ALA   A 1 129 ? -11.047 -1.282 -11.366 1.00 27.96 ? 415 ALA   A N   1 
ATOM   1050 C CA  . ALA   A 1 129 ? -9.785  -1.472 -10.667 1.00 27.37 ? 415 ALA   A CA  1 
ATOM   1051 C C   . ALA   A 1 129 ? -10.002 -1.608 -9.162  1.00 27.70 ? 415 ALA   A C   1 
ATOM   1052 O O   . ALA   A 1 129 ? -9.099  -2.050 -8.457  1.00 29.10 ? 415 ALA   A O   1 
ATOM   1053 C CB  . ALA   A 1 129 ? -8.852  -0.322 -10.955 1.00 28.72 ? 415 ALA   A CB  1 
ATOM   1054 N N   . GLY   A 1 130 ? -11.174 -1.183 -8.669  1.00 26.74 ? 416 GLY   A N   1 
ATOM   1055 C CA  . GLY   A 1 130 ? -11.442 -1.168 -7.239  1.00 26.82 ? 416 GLY   A CA  1 
ATOM   1056 C C   . GLY   A 1 130 ? -10.593 -0.123 -6.521  1.00 26.29 ? 416 GLY   A C   1 
ATOM   1057 O O   . GLY   A 1 130 ? -10.055 -0.398 -5.448  1.00 27.06 ? 416 GLY   A O   1 
ATOM   1058 N N   . MET   A 1 131 ? -10.499 1.076  -7.112  1.00 25.16 ? 417 MET   A N   1 
ATOM   1059 C CA  . MET   A 1 131 ? -9.653  2.129  -6.573  1.00 25.26 ? 417 MET   A CA  1 
ATOM   1060 C C   . MET   A 1 131 ? -10.452 3.414  -6.360  1.00 22.82 ? 417 MET   A C   1 
ATOM   1061 O O   . MET   A 1 131 ? -11.277 3.795  -7.187  1.00 22.53 ? 417 MET   A O   1 
ATOM   1062 C CB  . MET   A 1 131 ? -8.480  2.426  -7.513  1.00 28.13 ? 417 MET   A CB  1 
ATOM   1063 C CG  . MET   A 1 131 ? -7.438  3.335  -6.903  1.00 31.01 ? 417 MET   A CG  1 
ATOM   1064 S SD  . MET   A 1 131 ? -5.988  3.603  -7.938  1.00 37.67 ? 417 MET   A SD  1 
ATOM   1065 C CE  . MET   A 1 131 ? -5.567  1.891  -8.293  1.00 38.14 ? 417 MET   A CE  1 
ATOM   1066 N N   . VAL   A 1 132 ? -10.179 4.079  -5.231  1.00 21.43 ? 418 VAL   A N   1 
ATOM   1067 C CA  . VAL   A 1 132 ? -10.708 5.399  -4.923  1.00 19.46 ? 418 VAL   A CA  1 
ATOM   1068 C C   . VAL   A 1 132 ? -9.511  6.246  -4.508  1.00 18.90 ? 418 VAL   A C   1 
ATOM   1069 O O   . VAL   A 1 132 ? -8.874  5.930  -3.497  1.00 20.03 ? 418 VAL   A O   1 
ATOM   1070 C CB  . VAL   A 1 132 ? -11.767 5.423  -3.801  1.00 19.48 ? 418 VAL   A CB  1 
ATOM   1071 C CG1 . VAL   A 1 132 ? -12.381 6.808  -3.639  1.00 19.37 ? 418 VAL   A CG1 1 
ATOM   1072 C CG2 . VAL   A 1 132 ? -12.862 4.391  -4.012  1.00 20.26 ? 418 VAL   A CG2 1 
ATOM   1073 N N   . SER   A 1 133 ? -9.221  7.315  -5.263  1.00 19.33 ? 419 SER   A N   1 
ATOM   1074 C CA  . SER   A 1 133 ? -8.049  8.134  -4.989  1.00 19.61 ? 419 SER   A CA  1 
ATOM   1075 C C   . SER   A 1 133 ? -8.439  9.584  -4.736  1.00 17.83 ? 419 SER   A C   1 
ATOM   1076 O O   . SER   A 1 133 ? -9.379  10.111 -5.332  1.00 18.70 ? 419 SER   A O   1 
ATOM   1077 C CB  . SER   A 1 133 ? -7.029  8.082  -6.114  1.00 20.60 ? 419 SER   A CB  1 
ATOM   1078 O OG  . SER   A 1 133 ? -6.625  6.755  -6.417  1.00 23.11 ? 419 SER   A OG  1 
ATOM   1079 N N   . PHE   A 1 134 ? -7.636  10.226 -3.883  1.00 17.62 ? 420 PHE   A N   1 
ATOM   1080 C CA  . PHE   A 1 134 ? -7.846  11.589 -3.435  1.00 16.96 ? 420 PHE   A CA  1 
ATOM   1081 C C   . PHE   A 1 134 ? -6.562  12.370 -3.674  1.00 17.24 ? 420 PHE   A C   1 
ATOM   1082 O O   . PHE   A 1 134 ? -5.492  11.945 -3.244  1.00 18.09 ? 420 PHE   A O   1 
ATOM   1083 C CB  . PHE   A 1 134 ? -8.181  11.633 -1.940  1.00 16.93 ? 420 PHE   A CB  1 
ATOM   1084 C CG  . PHE   A 1 134 ? -9.444  10.870 -1.582  1.00 16.77 ? 420 PHE   A CG  1 
ATOM   1085 C CD1 . PHE   A 1 134 ? -9.398  9.500  -1.351  1.00 17.34 ? 420 PHE   A CD1 1 
ATOM   1086 C CD2 . PHE   A 1 134 ? -10.675 11.511 -1.516  1.00 17.25 ? 420 PHE   A CD2 1 
ATOM   1087 C CE1 . PHE   A 1 134 ? -10.551 8.793  -1.063  1.00 16.97 ? 420 PHE   A CE1 1 
ATOM   1088 C CE2 . PHE   A 1 134 ? -11.824 10.800 -1.213  1.00 16.56 ? 420 PHE   A CE2 1 
ATOM   1089 C CZ  . PHE   A 1 134 ? -11.762 9.443  -0.989  1.00 16.74 ? 420 PHE   A CZ  1 
ATOM   1090 N N   . TYR   A 1 135 ? -6.692  13.526 -4.321  1.00 17.36 ? 421 TYR   A N   1 
ATOM   1091 C CA  . TYR   A 1 135 ? -5.560  14.367 -4.668  1.00 17.88 ? 421 TYR   A CA  1 
ATOM   1092 C C   . TYR   A 1 135 ? -5.722  15.755 -4.068  1.00 17.71 ? 421 TYR   A C   1 
ATOM   1093 O O   . TYR   A 1 135 ? -6.818  16.318 -4.023  1.00 17.22 ? 421 TYR   A O   1 
ATOM   1094 C CB  . TYR   A 1 135 ? -5.444  14.512 -6.188  1.00 18.66 ? 421 TYR   A CB  1 
ATOM   1095 C CG  . TYR   A 1 135 ? -4.947  13.240 -6.845  1.00 20.40 ? 421 TYR   A CG  1 
ATOM   1096 C CD1 . TYR   A 1 135 ? -5.825  12.220 -7.178  1.00 20.81 ? 421 TYR   A CD1 1 
ATOM   1097 C CD2 . TYR   A 1 135 ? -3.591  13.036 -7.070  1.00 21.03 ? 421 TYR   A CD2 1 
ATOM   1098 C CE1 . TYR   A 1 135 ? -5.369  11.060 -7.783  1.00 21.50 ? 421 TYR   A CE1 1 
ATOM   1099 C CE2 . TYR   A 1 135 ? -3.121  11.870 -7.647  1.00 21.51 ? 421 TYR   A CE2 1 
ATOM   1100 C CZ  . TYR   A 1 135 ? -4.013  10.875 -7.990  1.00 20.83 ? 421 TYR   A CZ  1 
ATOM   1101 O OH  . TYR   A 1 135 ? -3.567  9.720  -8.552  1.00 23.28 ? 421 TYR   A OH  1 
ATOM   1102 N N   . ASN   A 1 136 ? -4.580  16.287 -3.641  1.00 17.87 ? 422 ASN   A N   1 
ATOM   1103 C CA  . ASN   A 1 136 ? -4.457  17.612 -3.077  1.00 18.19 ? 422 ASN   A CA  1 
ATOM   1104 C C   . ASN   A 1 136 ? -4.211  18.588 -4.214  1.00 18.65 ? 422 ASN   A C   1 
ATOM   1105 O O   . ASN   A 1 136 ? -3.075  18.789 -4.632  1.00 19.80 ? 422 ASN   A O   1 
ATOM   1106 C CB  . ASN   A 1 136 ? -3.326  17.620 -2.060  1.00 18.93 ? 422 ASN   A CB  1 
ATOM   1107 C CG  . ASN   A 1 136 ? -3.240  18.906 -1.278  1.00 19.67 ? 422 ASN   A CG  1 
ATOM   1108 O OD1 . ASN   A 1 136 ? -3.727  19.960 -1.704  1.00 19.76 ? 422 ASN   A OD1 1 
ATOM   1109 N ND2 . ASN   A 1 136 ? -2.573  18.828 -0.141  1.00 20.05 ? 422 ASN   A ND2 1 
ATOM   1110 N N   . ILE   A 1 137 ? -5.289  19.176 -4.725  1.00 17.88 ? 423 ILE   A N   1 
ATOM   1111 C CA  . ILE   A 1 137 ? -5.141  20.058 -5.859  1.00 18.88 ? 423 ILE   A CA  1 
ATOM   1112 C C   . ILE   A 1 137 ? -4.232  21.227 -5.484  1.00 19.49 ? 423 ILE   A C   1 
ATOM   1113 O O   . ILE   A 1 137 ? -3.361  21.601 -6.270  1.00 21.71 ? 423 ILE   A O   1 
ATOM   1114 C CB  . ILE   A 1 137 ? -6.517  20.463 -6.407  1.00 19.42 ? 423 ILE   A CB  1 
ATOM   1115 C CG1 . ILE   A 1 137 ? -7.249  19.214 -6.926  1.00 19.59 ? 423 ILE   A CG1 1 
ATOM   1116 C CG2 . ILE   A 1 137 ? -6.370  21.537 -7.483  1.00 20.89 ? 423 ILE   A CG2 1 
ATOM   1117 C CD1 . ILE   A 1 137 ? -8.661  19.471 -7.398  1.00 19.73 ? 423 ILE   A CD1 1 
ATOM   1118 N N   . THR   A 1 138 ? -4.408  21.780 -4.281  1.00 19.00 ? 424 THR   A N   1 
ATOM   1119 C CA  . THR   A 1 138 ? -3.664  22.945 -3.836  1.00 20.57 ? 424 THR   A CA  1 
ATOM   1120 C C   . THR   A 1 138 ? -2.162  22.671 -3.875  1.00 20.85 ? 424 THR   A C   1 
ATOM   1121 O O   . THR   A 1 138 ? -1.385  23.530 -4.288  1.00 24.20 ? 424 THR   A O   1 
ATOM   1122 C CB  . THR   A 1 138 ? -4.131  23.309 -2.428  1.00 20.33 ? 424 THR   A CB  1 
ATOM   1123 O OG1 . THR   A 1 138 ? -5.542  23.489 -2.498  1.00 20.48 ? 424 THR   A OG1 1 
ATOM   1124 C CG2 . THR   A 1 138 ? -3.447  24.563 -1.908  1.00 20.19 ? 424 THR   A CG2 1 
ATOM   1125 N N   . ASP   A 1 139 ? -1.765  21.466 -3.451  1.00 21.58 ? 425 ASP   A N   1 
ATOM   1126 C CA  . ASP   A 1 139 ? -0.369  21.057 -3.412  1.00 23.64 ? 425 ASP   A CA  1 
ATOM   1127 C C   . ASP   A 1 139 ? 0.072   20.453 -4.749  1.00 24.57 ? 425 ASP   A C   1 
ATOM   1128 O O   . ASP   A 1 139 ? 0.730   19.414 -4.780  1.00 25.92 ? 425 ASP   A O   1 
ATOM   1129 C CB  . ASP   A 1 139 ? -0.135  20.096 -2.260  1.00 24.63 ? 425 ASP   A CB  1 
ATOM   1130 C CG  . ASP   A 1 139 ? 1.322   19.758 -2.008  1.00 26.41 ? 425 ASP   A CG  1 
ATOM   1131 O OD1 . ASP   A 1 139 ? 2.139   20.689 -2.091  1.00 27.02 ? 425 ASP   A OD1 1 
ATOM   1132 O OD2 . ASP   A 1 139 ? 1.608   18.576 -1.727  1.00 30.84 ? 425 ASP   A OD2 1 
ATOM   1133 N N   . HIS   A 1 140 ? -0.278  21.132 -5.846  1.00 24.57 ? 426 HIS   A N   1 
ATOM   1134 C CA  . HIS   A 1 140 ? 0.073   20.736 -7.206  1.00 25.21 ? 426 HIS   A CA  1 
ATOM   1135 C C   . HIS   A 1 140 ? -0.239  19.264 -7.461  1.00 23.97 ? 426 HIS   A C   1 
ATOM   1136 O O   . HIS   A 1 140 ? 0.565   18.553 -8.058  1.00 26.16 ? 426 HIS   A O   1 
ATOM   1137 C CB  . HIS   A 1 140 ? 1.538   21.067 -7.513  1.00 26.95 ? 426 HIS   A CB  1 
ATOM   1138 C CG  . HIS   A 1 140 ? 1.840   22.519 -7.375  1.00 31.87 ? 426 HIS   A CG  1 
ATOM   1139 N ND1 . HIS   A 1 140 ? 2.944   22.983 -6.695  1.00 36.87 ? 426 HIS   A ND1 1 
ATOM   1140 C CD2 . HIS   A 1 140 ? 1.167   23.603 -7.773  1.00 34.01 ? 426 HIS   A CD2 1 
ATOM   1141 C CE1 . HIS   A 1 140 ? 2.949   24.307 -6.725  1.00 37.21 ? 426 HIS   A CE1 1 
ATOM   1142 N NE2 . HIS   A 1 140 ? 1.877   24.704 -7.369  1.00 34.33 ? 426 HIS   A NE2 1 
ATOM   1143 N N   . GLY   A 1 141 ? -1.427  18.821 -7.033  1.00 23.38 ? 427 GLY   A N   1 
ATOM   1144 C CA  . GLY   A 1 141 ? -1.966  17.535 -7.447  1.00 23.22 ? 427 GLY   A CA  1 
ATOM   1145 C C   . GLY   A 1 141 ? -1.274  16.351 -6.777  1.00 24.14 ? 427 GLY   A C   1 
ATOM   1146 O O   . GLY   A 1 141 ? -1.259  15.257 -7.330  1.00 26.64 ? 427 GLY   A O   1 
ATOM   1147 N N   . SER   A 1 142 ? -0.742  16.553 -5.566  1.00 24.12 ? 428 SER   A N   1 
ATOM   1148 C CA  . SER   A 1 142 ? -0.107  15.459 -4.849  1.00 24.23 ? 428 SER   A CA  1 
ATOM   1149 C C   . SER   A 1 142 ? -1.170  14.466 -4.393  1.00 23.14 ? 428 SER   A C   1 
ATOM   1150 O O   . SER   A 1 142 ? -2.275  14.855 -4.012  1.00 21.96 ? 428 SER   A O   1 
ATOM   1151 C CB  . SER   A 1 142 ? 0.740   15.945 -3.695  1.00 24.91 ? 428 SER   A CB  1 
ATOM   1152 O OG  . SER   A 1 142 ? -0.002  16.705 -2.751  1.00 27.21 ? 428 SER   A OG  1 
ATOM   1153 N N   . LEU   A 1 143 ? -0.816  13.175 -4.415  1.00 23.78 ? 429 LEU   A N   1 
ATOM   1154 C CA  . LEU   A 1 143 ? -1.718  12.136 -3.943  1.00 23.52 ? 429 LEU   A CA  1 
ATOM   1155 C C   . LEU   A 1 143 ? -1.845  12.238 -2.424  1.00 23.08 ? 429 LEU   A C   1 
ATOM   1156 O O   . LEU   A 1 143 ? -0.836  12.218 -1.719  1.00 25.01 ? 429 LEU   A O   1 
ATOM   1157 C CB  . LEU   A 1 143 ? -1.210  10.750 -4.338  1.00 24.97 ? 429 LEU   A CB  1 
ATOM   1158 C CG  . LEU   A 1 143 ? -2.052  9.562  -3.856  1.00 26.16 ? 429 LEU   A CG  1 
ATOM   1159 C CD1 . LEU   A 1 143 ? -3.378  9.510  -4.608  1.00 25.66 ? 429 LEU   A CD1 1 
ATOM   1160 C CD2 . LEU   A 1 143 ? -1.276  8.271  -4.032  1.00 27.33 ? 429 LEU   A CD2 1 
ATOM   1161 N N   . ILE   A 1 144 ? -3.093  12.319 -1.938  1.00 21.44 ? 430 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 144 ? -3.395  12.270 -0.512  1.00 21.08 ? 430 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 144 ? -3.469  10.814 -0.066  1.00 20.42 ? 430 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 144 ? -2.799  10.410 0.887   1.00 21.91 ? 430 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 144 ? -4.711  13.007 -0.203  1.00 20.51 ? 430 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 144 ? -4.592  14.498 -0.515  1.00 20.27 ? 430 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 144 ? -5.145  12.753 1.248   1.00 20.57 ? 430 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 144 ? -5.906  15.249 -0.459  1.00 19.85 ? 430 ILE   A CD1 1 
ATOM   1169 N N   . TYR   A 1 145 ? -4.324  10.041 -0.743  1.00 20.23 ? 431 TYR   A N   1 
ATOM   1170 C CA  . TYR   A 1 145 ? -4.562  8.669  -0.344  1.00 20.67 ? 431 TYR   A CA  1 
ATOM   1171 C C   . TYR   A 1 145 ? -5.259  7.921  -1.474  1.00 20.06 ? 431 TYR   A C   1 
ATOM   1172 O O   . TYR   A 1 145 ? -6.075  8.495  -2.183  1.00 20.90 ? 431 TYR   A O   1 
ATOM   1173 C CB  . TYR   A 1 145 ? -5.408  8.608  0.936   1.00 20.83 ? 431 TYR   A CB  1 
ATOM   1174 C CG  . TYR   A 1 145 ? -5.468  7.188  1.480   1.00 21.54 ? 431 TYR   A CG  1 
ATOM   1175 C CD1 . TYR   A 1 145 ? -4.377  6.628  2.136   1.00 21.51 ? 431 TYR   A CD1 1 
ATOM   1176 C CD2 . TYR   A 1 145 ? -6.569  6.374  1.242   1.00 21.35 ? 431 TYR   A CD2 1 
ATOM   1177 C CE1 . TYR   A 1 145 ? -4.396  5.309  2.554   1.00 22.76 ? 431 TYR   A CE1 1 
ATOM   1178 C CE2 . TYR   A 1 145 ? -6.596  5.052  1.646   1.00 22.95 ? 431 TYR   A CE2 1 
ATOM   1179 C CZ  . TYR   A 1 145 ? -5.504  4.516  2.306   1.00 22.37 ? 431 TYR   A CZ  1 
ATOM   1180 O OH  . TYR   A 1 145 ? -5.497  3.206  2.702   1.00 26.20 ? 431 TYR   A OH  1 
ATOM   1181 N N   . SER   A 1 146 ? -4.948  6.628  -1.589  1.00 21.06 ? 432 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 146 ? -5.640  5.726  -2.490  1.00 22.55 ? 432 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 146 ? -6.078  4.464  -1.748  1.00 22.60 ? 432 SER   A C   1 
ATOM   1184 O O   . SER   A 1 146 ? -5.259  3.776  -1.136  1.00 24.88 ? 432 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 146 ? -4.761  5.396  -3.668  1.00 26.16 ? 432 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 146 ? -5.552  4.966  -4.757  1.00 31.21 ? 432 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 147 ? -7.388  4.204  -1.782  1.00 21.81 ? 433 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 147 ? -7.946  2.906  -1.433  1.00 21.39 ? 433 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 147 ? -7.823  1.989  -2.643  1.00 24.09 ? 433 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 147 ? -8.309  2.325  -3.718  1.00 24.82 ? 433 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 147 ? -9.435  2.953  -1.078  1.00 21.42 ? 433 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 147 ? -9.774  3.690  0.209   1.00 20.13 ? 433 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 147 ? -9.958  5.065  0.217   1.00 20.11 ? 433 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 147 ? -9.938  2.998  1.405   1.00 20.37 ? 433 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 147 ? -10.300 5.730  1.381   1.00 19.86 ? 433 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 147 ? -10.270 3.669  2.573   1.00 20.68 ? 433 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 147 ? -10.430 5.034  2.564   1.00 19.42 ? 433 PHE   A CZ  1 
ATOM   1198 N N   . SER   A 1 148 ? -7.228  0.815  -2.442  1.00 26.20 ? 434 SER   A N   1 
ATOM   1199 C CA  . SER   A 1 148 ? -7.069  -0.135 -3.531  1.00 28.39 ? 434 SER   A CA  1 
ATOM   1200 C C   . SER   A 1 148 ? -7.706  -1.472 -3.157  1.00 30.61 ? 434 SER   A C   1 
ATOM   1201 O O   . SER   A 1 148 ? -7.971  -1.738 -1.985  1.00 31.34 ? 434 SER   A O   1 
ATOM   1202 C CB  . SER   A 1 148 ? -5.619  -0.283 -3.918  1.00 31.19 ? 434 SER   A CB  1 
ATOM   1203 O OG  . SER   A 1 148 ? -4.838  -0.772 -2.835  1.00 34.29 ? 434 SER   A OG  1 
ATOM   1204 N N   . GLU   A 1 149 ? -7.969  -2.291 -4.184  1.00 32.86 ? 435 GLU   A N   1 
ATOM   1205 C CA  . GLU   A 1 149 ? -8.558  -3.615 -4.032  1.00 35.65 ? 435 GLU   A CA  1 
ATOM   1206 C C   . GLU   A 1 149 ? -9.875  -3.537 -3.261  1.00 33.37 ? 435 GLU   A C   1 
ATOM   1207 O O   . GLU   A 1 149 ? -10.137 -4.367 -2.397  1.00 35.65 ? 435 GLU   A O   1 
ATOM   1208 C CB  . GLU   A 1 149 ? -7.592  -4.581 -3.341  1.00 39.32 ? 435 GLU   A CB  1 
ATOM   1209 C CG  . GLU   A 1 149 ? -6.206  -4.616 -3.979  1.00 42.77 ? 435 GLU   A CG  1 
ATOM   1210 C CD  . GLU   A 1 149 ? -5.115  -4.699 -2.926  1.00 48.29 ? 435 GLU   A CD  1 
ATOM   1211 O OE1 . GLU   A 1 149 ? -4.888  -5.810 -2.397  1.00 50.12 ? 435 GLU   A OE1 1 
ATOM   1212 O OE2 . GLU   A 1 149 ? -4.525  -3.635 -2.608  1.00 52.11 ? 435 GLU   A OE2 1 
ATOM   1213 N N   . CYS   A 1 150 ? -10.716 -2.557 -3.611  1.00 30.99 ? 436 CYS   A N   1 
ATOM   1214 C CA  . CYS   A 1 150 ? -11.999 -2.345 -2.958  1.00 30.06 ? 436 CYS   A CA  1 
ATOM   1215 C C   . CYS   A 1 150 ? -13.014 -3.431 -3.325  1.00 30.86 ? 436 CYS   A C   1 
ATOM   1216 O O   . CYS   A 1 150 ? -13.956 -3.662 -2.570  1.00 30.36 ? 436 CYS   A O   1 
ATOM   1217 C CB  . CYS   A 1 150 ? -12.548 -0.965 -3.298  1.00 29.09 ? 436 CYS   A CB  1 
ATOM   1218 S SG  . CYS   A 1 150 ? -11.579 0.385  -2.575  1.00 27.58 ? 436 CYS   A SG  1 
ATOM   1219 N N   . ALA   A 1 151 ? -12.843 -4.061 -4.497  1.00 31.90 ? 437 ALA   A N   1 
ATOM   1220 C CA  . ALA   A 1 151 ? -13.626 -5.225 -4.900  1.00 35.60 ? 437 ALA   A CA  1 
ATOM   1221 C C   . ALA   A 1 151 ? -15.130 -4.933 -4.861  1.00 35.26 ? 437 ALA   A C   1 
ATOM   1222 O O   . ALA   A 1 151 ? -15.911 -5.696 -4.295  1.00 37.19 ? 437 ALA   A O   1 
ATOM   1223 C CB  . ALA   A 1 151 ? -13.256 -6.419 -4.038  1.00 37.55 ? 437 ALA   A CB  1 
ATOM   1224 N N   . PHE   A 1 152 ? -15.524 -3.834 -5.508  1.00 31.41 ? 438 PHE   A N   1 
ATOM   1225 C CA  . PHE   A 1 152 ? -16.910 -3.404 -5.606  1.00 31.38 ? 438 PHE   A CA  1 
ATOM   1226 C C   . PHE   A 1 152 ? -17.760 -4.441 -6.334  1.00 34.20 ? 438 PHE   A C   1 
ATOM   1227 O O   . PHE   A 1 152 ? -17.294 -5.037 -7.307  1.00 38.30 ? 438 PHE   A O   1 
ATOM   1228 C CB  . PHE   A 1 152 ? -16.919 -2.115 -6.431  1.00 29.73 ? 438 PHE   A CB  1 
ATOM   1229 C CG  . PHE   A 1 152 ? -16.115 -0.962 -5.850  1.00 26.91 ? 438 PHE   A CG  1 
ATOM   1230 C CD1 . PHE   A 1 152 ? -16.316 -0.546 -4.539  1.00 26.57 ? 438 PHE   A CD1 1 
ATOM   1231 C CD2 . PHE   A 1 152 ? -15.163 -0.291 -6.616  1.00 26.92 ? 438 PHE   A CD2 1 
ATOM   1232 C CE1 . PHE   A 1 152 ? -15.593 0.512  -4.013  1.00 25.35 ? 438 PHE   A CE1 1 
ATOM   1233 C CE2 . PHE   A 1 152 ? -14.444 0.771  -6.082  1.00 26.84 ? 438 PHE   A CE2 1 
ATOM   1234 C CZ  . PHE   A 1 152 ? -14.666 1.174  -4.785  1.00 26.27 ? 438 PHE   A CZ  1 
ATOM   1235 N N   . THR   A 1 153 ? -19.021 -4.605 -5.906  1.00 35.14 ? 439 THR   A N   1 
ATOM   1236 C CA  . THR   A 1 153 ? -19.921 -5.556 -6.551  1.00 37.20 ? 439 THR   A CA  1 
ATOM   1237 C C   . THR   A 1 153 ? -21.252 -4.915 -6.949  1.00 35.32 ? 439 THR   A C   1 
ATOM   1238 O O   . THR   A 1 153 ? -21.950 -5.456 -7.802  1.00 38.94 ? 439 THR   A O   1 
ATOM   1239 C CB  . THR   A 1 153 ? -20.137 -6.777 -5.654  1.00 38.42 ? 439 THR   A CB  1 
ATOM   1240 O OG1 . THR   A 1 153 ? -20.689 -6.329 -4.420  1.00 42.08 ? 439 THR   A OG1 1 
ATOM   1241 C CG2 . THR   A 1 153 ? -18.842 -7.524 -5.393  1.00 39.61 ? 439 THR   A CG2 1 
ATOM   1242 N N   . GLY   A 1 154 ? -21.613 -3.780 -6.341  1.00 31.13 ? 440 GLY   A N   1 
ATOM   1243 C CA  . GLY   A 1 154 ? -22.909 -3.172 -6.590  1.00 28.60 ? 440 GLY   A CA  1 
ATOM   1244 C C   . GLY   A 1 154 ? -22.767 -1.688 -6.907  1.00 26.69 ? 440 GLY   A C   1 
ATOM   1245 O O   . GLY   A 1 154 ? -21.658 -1.199 -7.126  1.00 26.52 ? 440 GLY   A O   1 
ATOM   1246 N N   . PRO   A 1 155 ? -23.880 -0.922 -6.937  1.00 27.31 ? 441 PRO   A N   1 
ATOM   1247 C CA  . PRO   A 1 155 ? -23.804 0.482  -7.317  1.00 26.26 ? 441 PRO   A CA  1 
ATOM   1248 C C   . PRO   A 1 155 ? -23.146 1.341  -6.243  1.00 24.23 ? 441 PRO   A C   1 
ATOM   1249 O O   . PRO   A 1 155 ? -23.319 1.087  -5.047  1.00 24.96 ? 441 PRO   A O   1 
ATOM   1250 C CB  . PRO   A 1 155 ? -25.248 0.898  -7.563  1.00 27.15 ? 441 PRO   A CB  1 
ATOM   1251 C CG  . PRO   A 1 155 ? -26.118 -0.277 -7.152  1.00 29.37 ? 441 PRO   A CG  1 
ATOM   1252 C CD  . PRO   A 1 155 ? -25.244 -1.377 -6.627  1.00 28.10 ? 441 PRO   A CD  1 
ATOM   1253 N N   . LEU   A 1 156 ? -22.403 2.357  -6.692  1.00 22.76 ? 442 LEU   A N   1 
ATOM   1254 C CA  . LEU   A 1 156 ? -21.749 3.291  -5.793  1.00 20.97 ? 442 LEU   A CA  1 
ATOM   1255 C C   . LEU   A 1 156 ? -22.299 4.700  -5.985  1.00 19.34 ? 442 LEU   A C   1 
ATOM   1256 O O   . LEU   A 1 156 ? -22.878 5.031  -7.014  1.00 20.06 ? 442 LEU   A O   1 
ATOM   1257 C CB  . LEU   A 1 156 ? -20.241 3.273  -6.021  1.00 21.72 ? 442 LEU   A CB  1 
ATOM   1258 C CG  . LEU   A 1 156 ? -19.551 1.919  -5.861  1.00 22.45 ? 442 LEU   A CG  1 
ATOM   1259 C CD1 . LEU   A 1 156 ? -18.103 2.067  -6.278  1.00 23.26 ? 442 LEU   A CD1 1 
ATOM   1260 C CD2 . LEU   A 1 156 ? -19.670 1.377  -4.439  1.00 23.85 ? 442 LEU   A CD2 1 
ATOM   1261 N N   . ARG   A 1 157 ? -22.062 5.538  -4.972  1.00 18.73 ? 443 ARG   A N   1 
ATOM   1262 C CA  . ARG   A 1 157 ? -22.589 6.888  -4.931  1.00 17.74 ? 443 ARG   A CA  1 
ATOM   1263 C C   . ARG   A 1 157 ? -21.495 7.830  -4.445  1.00 17.11 ? 443 ARG   A C   1 
ATOM   1264 O O   . ARG   A 1 157 ? -20.742 7.477  -3.535  1.00 18.03 ? 443 ARG   A O   1 
ATOM   1265 C CB  . ARG   A 1 157 ? -23.737 7.003  -3.920  1.00 17.92 ? 443 ARG   A CB  1 
ATOM   1266 C CG  . ARG   A 1 157 ? -24.890 6.017  -4.074  1.00 19.44 ? 443 ARG   A CG  1 
ATOM   1267 C CD  . ARG   A 1 157 ? -25.653 6.236  -5.375  1.00 20.24 ? 443 ARG   A CD  1 
ATOM   1268 N NE  . ARG   A 1 157 ? -26.418 7.491  -5.372  1.00 19.62 ? 443 ARG   A NE  1 
ATOM   1269 C CZ  . ARG   A 1 157 ? -27.549 7.703  -4.715  1.00 19.88 ? 443 ARG   A CZ  1 
ATOM   1270 N NH1 . ARG   A 1 157 ? -28.166 6.708  -4.102  1.00 20.46 ? 443 ARG   A NH1 1 
ATOM   1271 N NH2 . ARG   A 1 157 ? -28.067 8.912  -4.659  1.00 20.59 ? 443 ARG   A NH2 1 
ATOM   1272 N N   . PRO   A 1 158 ? -21.382 9.055  -5.000  1.00 16.51 ? 444 PRO   A N   1 
ATOM   1273 C CA  . PRO   A 1 158 ? -20.568 10.080 -4.363  1.00 15.65 ? 444 PRO   A CA  1 
ATOM   1274 C C   . PRO   A 1 158 ? -21.106 10.375 -2.969  1.00 15.34 ? 444 PRO   A C   1 
ATOM   1275 O O   . PRO   A 1 158 ? -22.322 10.409 -2.797  1.00 16.14 ? 444 PRO   A O   1 
ATOM   1276 C CB  . PRO   A 1 158 ? -20.692 11.290 -5.290  1.00 16.04 ? 444 PRO   A CB  1 
ATOM   1277 C CG  . PRO   A 1 158 ? -21.190 10.712 -6.600  1.00 16.58 ? 444 PRO   A CG  1 
ATOM   1278 C CD  . PRO   A 1 158 ? -22.044 9.538  -6.226  1.00 16.77 ? 444 PRO   A CD  1 
ATOM   1279 N N   . PHE   A 1 159 ? -20.195 10.589 -2.010  1.00 14.98 ? 445 PHE   A N   1 
ATOM   1280 C CA  . PHE   A 1 159 ? -20.560 10.793 -0.617  1.00 14.68 ? 445 PHE   A CA  1 
ATOM   1281 C C   . PHE   A 1 159 ? -19.924 12.081 -0.095  1.00 14.00 ? 445 PHE   A C   1 
ATOM   1282 O O   . PHE   A 1 159 ? -18.737 12.322 -0.331  1.00 14.39 ? 445 PHE   A O   1 
ATOM   1283 C CB  . PHE   A 1 159 ? -20.072 9.598  0.205   1.00 15.21 ? 445 PHE   A CB  1 
ATOM   1284 C CG  . PHE   A 1 159 ? -20.396 9.754  1.680   1.00 15.31 ? 445 PHE   A CG  1 
ATOM   1285 C CD1 . PHE   A 1 159 ? -21.660 9.439  2.173   1.00 15.62 ? 445 PHE   A CD1 1 
ATOM   1286 C CD2 . PHE   A 1 159 ? -19.437 10.237 2.565   1.00 15.19 ? 445 PHE   A CD2 1 
ATOM   1287 C CE1 . PHE   A 1 159 ? -21.950 9.588  3.524   1.00 16.12 ? 445 PHE   A CE1 1 
ATOM   1288 C CE2 . PHE   A 1 159 ? -19.743 10.394 3.910   1.00 15.73 ? 445 PHE   A CE2 1 
ATOM   1289 C CZ  . PHE   A 1 159 ? -20.994 10.072 4.374   1.00 15.79 ? 445 PHE   A CZ  1 
ATOM   1290 N N   . PHE   A 1 160 ? -20.713 12.895 0.621   1.00 14.03 ? 446 PHE   A N   1 
ATOM   1291 C CA  . PHE   A 1 160 ? -20.220 14.162 1.142   1.00 13.52 ? 446 PHE   A CA  1 
ATOM   1292 C C   . PHE   A 1 160 ? -20.767 14.482 2.536   1.00 13.00 ? 446 PHE   A C   1 
ATOM   1293 O O   . PHE   A 1 160 ? -21.929 14.213 2.841   1.00 13.96 ? 446 PHE   A O   1 
ATOM   1294 C CB  . PHE   A 1 160 ? -20.694 15.323 0.267   1.00 14.51 ? 446 PHE   A CB  1 
ATOM   1295 C CG  . PHE   A 1 160 ? -20.494 15.133 -1.231  1.00 14.51 ? 446 PHE   A CG  1 
ATOM   1296 C CD1 . PHE   A 1 160 ? -21.437 14.439 -1.974  1.00 14.77 ? 446 PHE   A CD1 1 
ATOM   1297 C CD2 . PHE   A 1 160 ? -19.393 15.665 -1.896  1.00 15.20 ? 446 PHE   A CD2 1 
ATOM   1298 C CE1 . PHE   A 1 160 ? -21.272 14.263 -3.331  1.00 14.92 ? 446 PHE   A CE1 1 
ATOM   1299 C CE2 . PHE   A 1 160 ? -19.231 15.479 -3.264  1.00 15.01 ? 446 PHE   A CE2 1 
ATOM   1300 C CZ  . PHE   A 1 160 ? -20.171 14.789 -3.974  1.00 14.88 ? 446 PHE   A CZ  1 
ATOM   1301 N N   . SER   A 1 161 ? -19.918 15.123 3.355   1.00 12.72 ? 447 SER   A N   1 
ATOM   1302 C CA  . SER   A 1 161 ? -20.381 15.840 4.534   1.00 13.13 ? 447 SER   A CA  1 
ATOM   1303 C C   . SER   A 1 161 ? -19.631 17.158 4.662   1.00 13.18 ? 447 SER   A C   1 
ATOM   1304 O O   . SER   A 1 161 ? -18.402 17.155 4.699   1.00 13.72 ? 447 SER   A O   1 
ATOM   1305 C CB  . SER   A 1 161 ? -20.177 15.059 5.813   1.00 12.97 ? 447 SER   A CB  1 
ATOM   1306 O OG  . SER   A 1 161 ? -20.552 15.863 6.929   1.00 13.37 ? 447 SER   A OG  1 
ATOM   1307 N N   . PRO   A 1 162 ? -20.341 18.295 4.834   1.00 14.27 ? 448 PRO   A N   1 
ATOM   1308 C CA  . PRO   A 1 162 ? -19.682 19.554 5.131   1.00 14.31 ? 448 PRO   A CA  1 
ATOM   1309 C C   . PRO   A 1 162 ? -19.387 19.763 6.614   1.00 14.70 ? 448 PRO   A C   1 
ATOM   1310 O O   . PRO   A 1 162 ? -19.040 20.867 7.004   1.00 15.43 ? 448 PRO   A O   1 
ATOM   1311 C CB  . PRO   A 1 162 ? -20.694 20.577 4.641   1.00 14.38 ? 448 PRO   A CB  1 
ATOM   1312 C CG  . PRO   A 1 162 ? -22.015 19.909 4.996   1.00 14.64 ? 448 PRO   A CG  1 
ATOM   1313 C CD  . PRO   A 1 162 ? -21.802 18.452 4.679   1.00 14.39 ? 448 PRO   A CD  1 
ATOM   1314 N N   . GLY   A 1 163 ? -19.516 18.706 7.424   1.00 15.57 ? 449 GLY   A N   1 
ATOM   1315 C CA  . GLY   A 1 163 ? -19.137 18.779 8.825   1.00 16.36 ? 449 GLY   A CA  1 
ATOM   1316 C C   . GLY   A 1 163 ? -20.321 18.549 9.744   1.00 18.09 ? 449 GLY   A C   1 
ATOM   1317 O O   . GLY   A 1 163 ? -21.436 18.351 9.281   1.00 21.10 ? 449 GLY   A O   1 
ATOM   1318 N N   . PHE   A 1 164 ? -20.038 18.593 11.045  1.00 19.78 ? 450 PHE   A N   1 
ATOM   1319 C CA  . PHE   A 1 164 ? -21.058 18.638 12.080  1.00 21.97 ? 450 PHE   A CA  1 
ATOM   1320 C C   . PHE   A 1 164 ? -21.363 20.085 12.437  1.00 23.09 ? 450 PHE   A C   1 
ATOM   1321 O O   . PHE   A 1 164 ? -20.459 20.911 12.422  1.00 24.04 ? 450 PHE   A O   1 
ATOM   1322 C CB  . PHE   A 1 164 ? -20.519 17.957 13.332  1.00 23.12 ? 450 PHE   A CB  1 
ATOM   1323 C CG  . PHE   A 1 164 ? -20.439 16.454 13.173  1.00 25.69 ? 450 PHE   A CG  1 
ATOM   1324 C CD1 . PHE   A 1 164 ? -21.581 15.674 13.332  1.00 26.73 ? 450 PHE   A CD1 1 
ATOM   1325 C CD2 . PHE   A 1 164 ? -19.229 15.832 12.887  1.00 26.54 ? 450 PHE   A CD2 1 
ATOM   1326 C CE1 . PHE   A 1 164 ? -21.519 14.303 13.171  1.00 27.91 ? 450 PHE   A CE1 1 
ATOM   1327 C CE2 . PHE   A 1 164 ? -19.170 14.453 12.738  1.00 28.93 ? 450 PHE   A CE2 1 
ATOM   1328 C CZ  . PHE   A 1 164 ? -20.312 13.695 12.874  1.00 29.05 ? 450 PHE   A CZ  1 
ATOM   1329 N N   . ASN   A 1 165 ? -22.596 20.389 12.853  1.00 25.70 ? 451 ASN   A N   1 
ATOM   1330 C CA  . ASN   A 1 165 ? -22.869 21.748 13.307  1.00 28.49 ? 451 ASN   A CA  1 
ATOM   1331 C C   . ASN   A 1 165 ? -21.999 22.035 14.532  1.00 29.60 ? 451 ASN   A C   1 
ATOM   1332 O O   . ASN   A 1 165 ? -21.835 21.180 15.406  1.00 30.29 ? 451 ASN   A O   1 
ATOM   1333 C CB  . ASN   A 1 165 ? -24.361 22.014 13.484  1.00 32.45 ? 451 ASN   A CB  1 
ATOM   1334 C CG  . ASN   A 1 165 ? -24.924 21.405 14.740  1.00 35.33 ? 451 ASN   A CG  1 
ATOM   1335 O OD1 . ASN   A 1 165 ? -25.149 20.191 14.787  1.00 39.55 ? 451 ASN   A OD1 1 
ATOM   1336 N ND2 . ASN   A 1 165 ? -25.186 22.227 15.749  1.00 38.15 ? 451 ASN   A ND2 1 
ATOM   1337 N N   . ASP   A 1 166 ? -21.408 23.239 14.563  1.00 30.99 ? 452 ASP   A N   1 
ATOM   1338 C CA  . ASP   A 1 166 ? -20.364 23.563 15.522  1.00 32.62 ? 452 ASP   A CA  1 
ATOM   1339 C C   . ASP   A 1 166 ? -20.364 25.060 15.838  1.00 33.11 ? 452 ASP   A C   1 
ATOM   1340 O O   . ASP   A 1 166 ? -19.309 25.695 15.863  1.00 31.38 ? 452 ASP   A O   1 
ATOM   1341 C CB  . ASP   A 1 166 ? -19.004 23.119 15.004  1.00 32.67 ? 452 ASP   A CB  1 
ATOM   1342 C CG  . ASP   A 1 166 ? -17.884 23.135 16.035  1.00 32.49 ? 452 ASP   A CG  1 
ATOM   1343 O OD1 . ASP   A 1 166 ? -18.195 23.160 17.244  1.00 34.59 ? 452 ASP   A OD1 1 
ATOM   1344 O OD2 . ASP   A 1 166 ? -16.711 23.164 15.625  1.00 33.69 ? 452 ASP   A OD2 1 
ATOM   1345 N N   . GLY   A 1 167 ? -21.558 25.618 16.072  1.00 34.49 ? 453 GLY   A N   1 
ATOM   1346 C CA  . GLY   A 1 167 ? -21.696 26.980 16.565  1.00 34.17 ? 453 GLY   A CA  1 
ATOM   1347 C C   . GLY   A 1 167 ? -21.200 28.033 15.576  1.00 33.89 ? 453 GLY   A C   1 
ATOM   1348 O O   . GLY   A 1 167 ? -20.853 29.138 15.988  1.00 36.04 ? 453 GLY   A O   1 
ATOM   1349 N N   . GLY   A 1 168 ? -21.162 27.690 14.281  1.00 31.66 ? 454 GLY   A N   1 
ATOM   1350 C CA  . GLY   A 1 168 ? -20.812 28.643 13.236  1.00 31.17 ? 454 GLY   A CA  1 
ATOM   1351 C C   . GLY   A 1 168 ? -19.379 28.483 12.730  1.00 29.02 ? 454 GLY   A C   1 
ATOM   1352 O O   . GLY   A 1 168 ? -18.986 29.168 11.778  1.00 31.19 ? 454 GLY   A O   1 
ATOM   1353 N N   . LYS   A 1 169 ? -18.628 27.536 13.310  1.00 26.45 ? 455 LYS   A N   1 
ATOM   1354 C CA  . LYS   A 1 169 ? -17.212 27.354 13.007  1.00 27.60 ? 455 LYS   A CA  1 
ATOM   1355 C C   . LYS   A 1 169 ? -16.997 26.573 11.713  1.00 26.11 ? 455 LYS   A C   1 
ATOM   1356 O O   . LYS   A 1 169 ? -15.858 26.369 11.289  1.00 27.58 ? 455 LYS   A O   1 
ATOM   1357 C CB  . LYS   A 1 169 ? -16.519 26.675 14.194  1.00 30.71 ? 455 LYS   A CB  1 
ATOM   1358 C CG  . LYS   A 1 169 ? -16.266 27.638 15.344  1.00 34.61 ? 455 LYS   A CG  1 
ATOM   1359 C CD  . LYS   A 1 169 ? -16.411 27.080 16.755  1.00 39.00 ? 455 LYS   A CD  1 
ATOM   1360 C CE  . LYS   A 1 169 ? -15.642 25.836 17.028  1.00 42.49 ? 455 LYS   A CE  1 
ATOM   1361 N NZ  . LYS   A 1 169 ? -14.193 26.050 16.989  1.00 45.02 ? 455 LYS   A NZ  1 
ATOM   1362 N N   . ASN   A 1 170 ? -18.070 26.135 11.066  1.00 21.55 ? 456 ASN   A N   1 
ATOM   1363 C CA  . ASN   A 1 170 ? -17.861 25.341 9.867   1.00 19.39 ? 456 ASN   A CA  1 
ATOM   1364 C C   . ASN   A 1 170 ? -18.972 25.548 8.839   1.00 18.14 ? 456 ASN   A C   1 
ATOM   1365 O O   . ASN   A 1 170 ? -19.348 24.600 8.153   1.00 17.38 ? 456 ASN   A O   1 
ATOM   1366 C CB  . ASN   A 1 170 ? -17.685 23.879 10.241  1.00 18.86 ? 456 ASN   A CB  1 
ATOM   1367 C CG  . ASN   A 1 170 ? -16.986 23.074 9.168   1.00 17.59 ? 456 ASN   A CG  1 
ATOM   1368 O OD1 . ASN   A 1 170 ? -16.347 23.629 8.259   1.00 17.94 ? 456 ASN   A OD1 1 
ATOM   1369 N ND2 . ASN   A 1 170 ? -17.076 21.761 9.270   1.00 17.81 ? 456 ASN   A ND2 1 
ATOM   1370 N N   . THR   A 1 171 ? -19.428 26.796 8.692   1.00 16.41 ? 457 THR   A N   1 
ATOM   1371 C CA  . THR   A 1 171 ? -20.521 27.126 7.790   1.00 15.80 ? 457 THR   A CA  1 
ATOM   1372 C C   . THR   A 1 171 ? -20.031 27.335 6.355   1.00 14.91 ? 457 THR   A C   1 
ATOM   1373 O O   . THR   A 1 171 ? -20.861 27.493 5.471   1.00 15.69 ? 457 THR   A O   1 
ATOM   1374 C CB  . THR   A 1 171 ? -21.281 28.344 8.312   1.00 16.58 ? 457 THR   A CB  1 
ATOM   1375 O OG1 . THR   A 1 171 ? -20.352 29.382 8.617   1.00 18.25 ? 457 THR   A OG1 1 
ATOM   1376 C CG2 . THR   A 1 171 ? -22.059 28.016 9.575   1.00 16.93 ? 457 THR   A CG2 1 
ATOM   1377 N N   . ALA   A 1 172 ? -18.718 27.342 6.102   1.00 14.73 ? 458 ALA   A N   1 
ATOM   1378 C CA  . ALA   A 1 172 ? -18.252 27.502 4.728   1.00 14.77 ? 458 ALA   A CA  1 
ATOM   1379 C C   . ALA   A 1 172 ? -18.771 26.351 3.873   1.00 14.49 ? 458 ALA   A C   1 
ATOM   1380 O O   . ALA   A 1 172 ? -18.847 25.212 4.328   1.00 14.62 ? 458 ALA   A O   1 
ATOM   1381 C CB  . ALA   A 1 172 ? -16.751 27.560 4.643   1.00 15.99 ? 458 ALA   A CB  1 
ATOM   1382 N N   . PRO   A 1 173 ? -19.138 26.612 2.598   1.00 15.21 ? 459 PRO   A N   1 
ATOM   1383 C CA  . PRO   A 1 173 ? -19.700 25.564 1.758   1.00 14.99 ? 459 PRO   A CA  1 
ATOM   1384 C C   . PRO   A 1 173 ? -18.682 24.550 1.232   1.00 15.02 ? 459 PRO   A C   1 
ATOM   1385 O O   . PRO   A 1 173 ? -17.485 24.837 1.147   1.00 15.17 ? 459 PRO   A O   1 
ATOM   1386 C CB  . PRO   A 1 173 ? -20.342 26.342 0.608   1.00 15.59 ? 459 PRO   A CB  1 
ATOM   1387 C CG  . PRO   A 1 173 ? -19.466 27.574 0.514   1.00 16.06 ? 459 PRO   A CG  1 
ATOM   1388 C CD  . PRO   A 1 173 ? -19.106 27.924 1.930   1.00 15.79 ? 459 PRO   A CD  1 
ATOM   1389 N N   . LEU   A 1 174 ? -19.211 23.363 0.892   1.00 14.78 ? 460 LEU   A N   1 
ATOM   1390 C CA  . LEU   A 1 174 ? -18.580 22.392 0.014   1.00 15.28 ? 460 LEU   A CA  1 
ATOM   1391 C C   . LEU   A 1 174 ? -19.161 22.621 -1.372  1.00 14.67 ? 460 LEU   A C   1 
ATOM   1392 O O   . LEU   A 1 174 ? -20.386 22.576 -1.501  1.00 15.06 ? 460 LEU   A O   1 
ATOM   1393 C CB  . LEU   A 1 174 ? -18.917 20.948 0.379   1.00 18.25 ? 460 LEU   A CB  1 
ATOM   1394 C CG  . LEU   A 1 174 ? -18.224 20.284 1.557   1.00 19.83 ? 460 LEU   A CG  1 
ATOM   1395 C CD1 . LEU   A 1 174 ? -18.772 18.862 1.621   1.00 18.58 ? 460 LEU   A CD1 1 
ATOM   1396 C CD2 . LEU   A 1 174 ? -16.713 20.283 1.475   1.00 19.66 ? 460 LEU   A CD2 1 
ATOM   1397 N N   . THR   A 1 175 ? -18.299 22.776 -2.385  1.00 13.57 ? 461 THR   A N   1 
ATOM   1398 C CA  . THR   A 1 175 ? -18.791 23.066 -3.728  1.00 14.15 ? 461 THR   A CA  1 
ATOM   1399 C C   . THR   A 1 175 ? -18.098 22.160 -4.748  1.00 13.81 ? 461 THR   A C   1 
ATOM   1400 O O   . THR   A 1 175 ? -16.878 22.074 -4.791  1.00 14.58 ? 461 THR   A O   1 
ATOM   1401 C CB  . THR   A 1 175 ? -18.567 24.535 -4.092  1.00 14.98 ? 461 THR   A CB  1 
ATOM   1402 O OG1 . THR   A 1 175 ? -18.972 25.376 -3.010  1.00 16.19 ? 461 THR   A OG1 1 
ATOM   1403 C CG2 . THR   A 1 175 ? -19.364 24.939 -5.323  1.00 16.50 ? 461 THR   A CG2 1 
ATOM   1404 N N   . LEU   A 1 176 ? -18.909 21.495 -5.579  1.00 14.10 ? 462 LEU   A N   1 
ATOM   1405 C CA  . LEU   A 1 176 ? -18.398 20.774 -6.732  1.00 14.30 ? 462 LEU   A CA  1 
ATOM   1406 C C   . LEU   A 1 176 ? -17.944 21.785 -7.779  1.00 15.61 ? 462 LEU   A C   1 
ATOM   1407 O O   . LEU   A 1 176 ? -18.662 22.728 -8.068  1.00 17.75 ? 462 LEU   A O   1 
ATOM   1408 C CB  . LEU   A 1 176 ? -19.495 19.852 -7.247  1.00 14.56 ? 462 LEU   A CB  1 
ATOM   1409 C CG  . LEU   A 1 176 ? -19.751 18.615 -6.381  1.00 15.15 ? 462 LEU   A CG  1 
ATOM   1410 C CD1 . LEU   A 1 176 ? -21.181 18.121 -6.489  1.00 16.58 ? 462 LEU   A CD1 1 
ATOM   1411 C CD2 . LEU   A 1 176 ? -18.762 17.514 -6.746  1.00 15.13 ? 462 LEU   A CD2 1 
ATOM   1412 N N   . CYS   A 1 177 ? -16.739 21.566 -8.308  1.00 16.33 ? 463 CYS   A N   1 
ATOM   1413 C CA  . CYS   A 1 177 ? -16.104 22.500 -9.220  1.00 17.67 ? 463 CYS   A CA  1 
ATOM   1414 C C   . CYS   A 1 177 ? -16.189 21.985 -10.652 1.00 19.89 ? 463 CYS   A C   1 
ATOM   1415 O O   . CYS   A 1 177 ? -16.094 20.784 -10.886 1.00 19.79 ? 463 CYS   A O   1 
ATOM   1416 C CB  . CYS   A 1 177 ? -14.625 22.659 -8.906  1.00 18.81 ? 463 CYS   A CB  1 
ATOM   1417 S SG  . CYS   A 1 177 ? -14.330 23.213 -7.211  1.00 20.39 ? 463 CYS   A SG  1 
ATOM   1418 N N   . PRO   A 1 178 ? -16.362 22.879 -11.645 1.00 21.38 ? 464 PRO   A N   1 
ATOM   1419 C CA  . PRO   A 1 178 ? -16.410 22.442 -13.032 1.00 23.40 ? 464 PRO   A CA  1 
ATOM   1420 C C   . PRO   A 1 178 ? -15.114 21.759 -13.456 1.00 26.94 ? 464 PRO   A C   1 
ATOM   1421 O O   . PRO   A 1 178 ? -15.253 21.004 -14.462 1.00 34.18 ? 464 PRO   A O   1 
ATOM   1422 C CB  . PRO   A 1 178 ? -16.782 23.711 -13.789 1.00 23.00 ? 464 PRO   A CB  1 
ATOM   1423 C CG  . PRO   A 1 178 ? -16.590 24.869 -12.842 1.00 22.97 ? 464 PRO   A CG  1 
ATOM   1424 C CD  . PRO   A 1 178 ? -16.564 24.323 -11.453 1.00 21.97 ? 464 PRO   A CD  1 
HETATM 1425 C C2  . A1I41 B 2 .   ? -16.088 7.418  11.595  1.00 18.34 ? 501 A1I41 A C2  1 
HETATM 1426 C C6  . A1I41 B 2 .   ? -14.063 4.870  10.440  1.00 23.39 ? 501 A1I41 A C6  1 
HETATM 1427 C C9  . A1I41 B 2 .   ? -12.315 2.887  11.678  1.00 24.96 ? 501 A1I41 A C9  1 
HETATM 1428 C C12 . A1I41 B 2 .   ? -17.294 9.671  11.622  1.00 17.45 ? 501 A1I41 A C12 1 
HETATM 1429 C C15 . A1I41 B 2 .   ? -19.730 8.415  11.835  1.00 19.92 ? 501 A1I41 A C15 1 
HETATM 1430 C C18 . A1I41 B 2 .   ? -16.561 11.456 10.175  1.00 16.18 ? 501 A1I41 A C18 1 
HETATM 1431 C C21 . A1I41 B 2 .   ? -15.588 14.970 9.341   1.00 15.65 ? 501 A1I41 A C21 1 
HETATM 1432 C C27 . A1I41 B 2 .   ? -20.689 13.569 9.425   1.00 19.21 ? 501 A1I41 A C27 1 
HETATM 1433 C C29 . A1I41 B 2 .   ? -15.399 9.340  10.206  1.00 17.00 ? 501 A1I41 A C29 1 
HETATM 1434 O O1  . A1I41 B 2 .   ? -16.937 6.558  11.353  1.00 18.68 ? 501 A1I41 A O1  1 
HETATM 1435 N N3  . A1I41 B 2 .   ? -14.939 7.141  12.218  1.00 20.13 ? 501 A1I41 A N3  1 
HETATM 1436 C C4  . A1I41 B 2 .   ? -14.629 5.813  12.710  1.00 21.64 ? 501 A1I41 A C4  1 
HETATM 1437 C C5  . A1I41 B 2 .   ? -13.597 5.074  11.879  1.00 22.58 ? 501 A1I41 A C5  1 
HETATM 1438 C C7  . A1I41 B 2 .   ? -13.093 4.011  9.638   1.00 23.76 ? 501 A1I41 A C7  1 
HETATM 1439 C C8  . A1I41 B 2 .   ? -12.861 2.675  10.303  1.00 25.16 ? 501 A1I41 A C8  1 
HETATM 1440 C C10 . A1I41 B 2 .   ? -13.272 3.724  12.520  1.00 24.32 ? 501 A1I41 A C10 1 
HETATM 1441 C C11 . A1I41 B 2 .   ? -16.273 8.834  11.158  1.00 17.64 ? 501 A1I41 A C11 1 
HETATM 1442 S S13 . A1I41 B 2 .   ? -18.489 9.169  12.815  1.00 20.31 ? 501 A1I41 A S13 1 
HETATM 1443 O O14 . A1I41 B 2 .   ? -17.905 8.170  13.666  1.00 22.02 ? 501 A1I41 A O14 1 
HETATM 1444 O O16 . A1I41 B 2 .   ? -19.031 10.353 13.427  1.00 21.10 ? 501 A1I41 A O16 1 
HETATM 1445 C C17 . A1I41 B 2 .   ? -17.437 10.962 11.138  1.00 16.58 ? 501 A1I41 A C17 1 
HETATM 1446 C C19 . A1I41 B 2 .   ? -16.700 12.852 9.681   1.00 15.86 ? 501 A1I41 A C19 1 
HETATM 1447 C C20 . A1I41 B 2 .   ? -15.553 13.642 9.712   1.00 15.84 ? 501 A1I41 A C20 1 
HETATM 1448 C C22 . A1I41 B 2 .   ? -16.775 15.496 8.937   1.00 16.24 ? 501 A1I41 A C22 1 
HETATM 1449 F F23 . A1I41 B 2 .   ? -16.821 16.805 8.592   1.00 17.47 ? 501 A1I41 A F23 1 
HETATM 1450 C C24 . A1I41 B 2 .   ? -17.940 14.777 8.874   1.00 16.48 ? 501 A1I41 A C24 1 
HETATM 1451 C C25 . A1I41 B 2 .   ? -17.903 13.440 9.247   1.00 17.00 ? 501 A1I41 A C25 1 
HETATM 1452 S S26 . A1I41 B 2 .   ? -19.344 12.427 9.112   1.00 20.26 ? 501 A1I41 A S26 1 
HETATM 1453 C C28 . A1I41 B 2 .   ? -15.545 10.628 9.722   1.00 16.57 ? 501 A1I41 A C28 1 
HETATM 1454 C C1  . EDO   C 3 .   ? -7.167  24.850 3.947   1.00 30.75 ? 502 EDO   A C1  1 
HETATM 1455 O O1  . EDO   C 3 .   ? -6.727  25.614 5.058   1.00 32.09 ? 502 EDO   A O1  1 
HETATM 1456 C C2  . EDO   C 3 .   ? -8.597  25.006 3.629   1.00 30.97 ? 502 EDO   A C2  1 
HETATM 1457 O O2  . EDO   C 3 .   ? -9.073  26.308 3.854   1.00 33.38 ? 502 EDO   A O2  1 
HETATM 1458 C C1  . EDO   D 3 .   ? -15.701 18.872 14.103  1.00 43.67 ? 503 EDO   A C1  1 
HETATM 1459 O O1  . EDO   D 3 .   ? -16.364 20.102 13.878  1.00 42.95 ? 503 EDO   A O1  1 
HETATM 1460 C C2  . EDO   D 3 .   ? -14.222 18.976 14.085  1.00 42.43 ? 503 EDO   A C2  1 
HETATM 1461 O O2  . EDO   D 3 .   ? -13.723 20.262 13.717  1.00 42.75 ? 503 EDO   A O2  1 
HETATM 1462 O O   . HOH   E 4 .   ? -32.857 9.786  -4.239  1.00 44.25 ? 601 HOH   A O   1 
HETATM 1463 O O   . HOH   E 4 .   ? -6.415  22.087 7.729   1.00 34.77 ? 602 HOH   A O   1 
HETATM 1464 O O   . HOH   E 4 .   ? -17.818 -0.293 10.474  1.00 36.39 ? 603 HOH   A O   1 
HETATM 1465 O O   . HOH   E 4 .   ? -13.326 1.300  -14.110 1.00 39.71 ? 604 HOH   A O   1 
HETATM 1466 O O   . HOH   E 4 .   ? -18.047 20.713 11.782  1.00 23.10 ? 605 HOH   A O   1 
HETATM 1467 O O   . HOH   E 4 .   ? -2.999  23.193 -8.218  1.00 34.83 ? 606 HOH   A O   1 
HETATM 1468 O O   . HOH   E 4 .   ? -14.543 6.289  5.767   1.00 19.69 ? 607 HOH   A O   1 
HETATM 1469 O O   . HOH   E 4 .   ? -4.288  10.652 13.882  1.00 37.71 ? 608 HOH   A O   1 
HETATM 1470 O O   . HOH   E 4 .   ? -36.671 8.581  -0.025  1.00 38.77 ? 609 HOH   A O   1 
HETATM 1471 O O   . HOH   E 4 .   ? -5.925  25.402 -4.250  1.00 25.04 ? 610 HOH   A O   1 
HETATM 1472 O O   . HOH   E 4 .   ? -17.519 14.493 -13.207 1.00 35.27 ? 611 HOH   A O   1 
HETATM 1473 O O   . HOH   E 4 .   ? -32.101 4.026  1.182   1.00 35.57 ? 612 HOH   A O   1 
HETATM 1474 O O   . HOH   E 4 .   ? -3.252  15.441 9.500   1.00 34.35 ? 613 HOH   A O   1 
HETATM 1475 O O   . HOH   E 4 .   ? -16.759 25.664 -1.647  1.00 16.56 ? 614 HOH   A O   1 
HETATM 1476 O O   . HOH   E 4 .   ? -9.949  19.057 -11.498 1.00 27.31 ? 615 HOH   A O   1 
HETATM 1477 O O   . HOH   E 4 .   ? -25.512 28.671 8.292   1.00 28.32 ? 616 HOH   A O   1 
HETATM 1478 O O   . HOH   E 4 .   ? -3.706  25.852 1.737   1.00 28.05 ? 617 HOH   A O   1 
HETATM 1479 O O   . HOH   E 4 .   ? -23.862 1.127  6.065   1.00 37.12 ? 618 HOH   A O   1 
HETATM 1480 O O   . HOH   E 4 .   ? 3.706   16.921 -1.728  1.00 54.73 ? 619 HOH   A O   1 
HETATM 1481 O O   . HOH   E 4 .   ? -13.383 26.783 -6.205  1.00 24.24 ? 620 HOH   A O   1 
HETATM 1482 O O   . HOH   E 4 .   ? -33.123 14.012 11.170  1.00 27.73 ? 621 HOH   A O   1 
HETATM 1483 O O   . HOH   E 4 .   ? -8.635  21.146 3.946   1.00 16.75 ? 622 HOH   A O   1 
HETATM 1484 O O   . HOH   E 4 .   ? -23.547 27.702 5.843   1.00 19.67 ? 623 HOH   A O   1 
HETATM 1485 O O   . HOH   E 4 .   ? -32.009 28.795 10.475  1.00 42.86 ? 624 HOH   A O   1 
HETATM 1486 O O   . HOH   E 4 .   ? -30.374 23.667 7.581   1.00 24.69 ? 625 HOH   A O   1 
HETATM 1487 O O   . HOH   E 4 .   ? -0.245  8.548  5.701   1.00 37.54 ? 626 HOH   A O   1 
HETATM 1488 O O   . HOH   E 4 .   ? -15.928 27.176 1.220   1.00 17.31 ? 627 HOH   A O   1 
HETATM 1489 O O   . HOH   E 4 .   ? -30.466 9.540  -7.727  1.00 38.04 ? 628 HOH   A O   1 
HETATM 1490 O O   . HOH   E 4 .   ? -22.791 -1.268 -3.830  1.00 32.55 ? 629 HOH   A O   1 
HETATM 1491 O O   . HOH   E 4 .   ? -13.442 4.344  4.363   1.00 19.84 ? 630 HOH   A O   1 
HETATM 1492 O O   . HOH   E 4 .   ? -12.474 0.790  6.387   1.00 27.51 ? 631 HOH   A O   1 
HETATM 1493 O O   . HOH   E 4 .   ? -26.091 12.273 16.062  1.00 35.91 ? 632 HOH   A O   1 
HETATM 1494 O O   . HOH   E 4 .   ? -24.242 25.145 11.948  1.00 45.43 ? 633 HOH   A O   1 
HETATM 1495 O O   . HOH   E 4 .   ? -24.576 3.695  6.916   1.00 25.61 ? 634 HOH   A O   1 
HETATM 1496 O O   . HOH   E 4 .   ? -9.042  24.237 7.715   1.00 39.95 ? 635 HOH   A O   1 
HETATM 1497 O O   . HOH   E 4 .   ? -34.050 3.928  5.245   1.00 33.03 ? 636 HOH   A O   1 
HETATM 1498 O O   . HOH   E 4 .   ? -20.869 24.089 5.943   1.00 15.52 ? 637 HOH   A O   1 
HETATM 1499 O O   . HOH   E 4 .   ? -26.590 21.465 -11.891 1.00 33.64 ? 638 HOH   A O   1 
HETATM 1500 O O   . HOH   E 4 .   ? -18.734 -3.165 -13.567 1.00 36.31 ? 639 HOH   A O   1 
HETATM 1501 O O   . HOH   E 4 .   ? -9.980  28.816 -2.434  1.00 22.88 ? 640 HOH   A O   1 
HETATM 1502 O O   . HOH   E 4 .   ? -16.612 18.285 -9.856  1.00 22.56 ? 641 HOH   A O   1 
HETATM 1503 O O   . HOH   E 4 .   ? -9.019  -0.438 0.205   1.00 43.40 ? 642 HOH   A O   1 
HETATM 1504 O O   . HOH   E 4 .   ? -1.220  12.051 2.454   1.00 33.67 ? 643 HOH   A O   1 
HETATM 1505 O O   . HOH   E 4 .   ? -36.784 17.887 9.163   1.00 34.53 ? 644 HOH   A O   1 
HETATM 1506 O O   . HOH   E 4 .   ? -16.938 29.337 9.913   0.50 25.80 ? 645 HOH   A O   1 
HETATM 1507 O O   . HOH   E 4 .   ? -15.812 0.077  -17.201 1.00 45.90 ? 646 HOH   A O   1 
HETATM 1508 O O   . HOH   E 4 .   ? -4.766  27.286 4.012   1.00 33.38 ? 647 HOH   A O   1 
HETATM 1509 O O   . HOH   E 4 .   ? -29.789 15.859 -8.122  1.00 35.54 ? 648 HOH   A O   1 
HETATM 1510 O O   . HOH   E 4 .   ? -28.962 5.519  16.434  1.00 21.73 ? 649 HOH   A O   1 
HETATM 1511 O O   . HOH   E 4 .   ? -35.539 10.817 8.315   1.00 38.20 ? 650 HOH   A O   1 
HETATM 1512 O O   . HOH   E 4 .   ? -13.763 -3.474 -8.212  1.00 37.15 ? 651 HOH   A O   1 
HETATM 1513 O O   . HOH   E 4 .   ? -30.163 2.181  2.265   1.00 39.48 ? 652 HOH   A O   1 
HETATM 1514 O O   . HOH   E 4 .   ? -36.494 15.094 7.988   1.00 36.81 ? 653 HOH   A O   1 
HETATM 1515 O O   . HOH   E 4 .   ? -0.808  16.320 -0.099  1.00 26.36 ? 654 HOH   A O   1 
HETATM 1516 O O   . HOH   E 4 .   ? -28.013 8.889  9.898   1.00 18.39 ? 655 HOH   A O   1 
HETATM 1517 O O   . HOH   E 4 .   ? -10.819 22.525 4.605   1.00 17.34 ? 656 HOH   A O   1 
HETATM 1518 O O   . HOH   E 4 .   ? -32.303 17.171 16.513  1.00 31.86 ? 657 HOH   A O   1 
HETATM 1519 O O   . HOH   E 4 .   ? -35.905 16.264 -0.635  1.00 36.80 ? 658 HOH   A O   1 
HETATM 1520 O O   . HOH   E 4 .   ? -31.511 19.257 3.635   1.00 25.78 ? 659 HOH   A O   1 
HETATM 1521 O O   . HOH   E 4 .   ? -17.189 12.775 -2.802  1.00 15.68 ? 660 HOH   A O   1 
HETATM 1522 O O   . HOH   E 4 .   ? -3.186  2.814  0.571   1.00 56.35 ? 661 HOH   A O   1 
HETATM 1523 O O   . HOH   E 4 .   ? -9.024  0.457  -14.774 1.00 46.12 ? 662 HOH   A O   1 
HETATM 1524 O O   . HOH   E 4 .   ? -13.681 28.759 -2.829  1.00 20.35 ? 663 HOH   A O   1 
HETATM 1525 O O   . HOH   E 4 .   ? 1.600   8.155  10.290  1.00 37.15 ? 664 HOH   A O   1 
HETATM 1526 O O   . HOH   E 4 .   ? -28.370 1.358  -9.224  1.00 45.46 ? 665 HOH   A O   1 
HETATM 1527 O O   . HOH   E 4 .   ? -0.094  7.058  8.219   1.00 37.41 ? 666 HOH   A O   1 
HETATM 1528 O O   . HOH   E 4 .   ? -20.751 31.381 10.667  1.00 29.68 ? 667 HOH   A O   1 
HETATM 1529 O O   . HOH   E 4 .   ? -16.383 27.460 7.819   1.00 20.82 ? 668 HOH   A O   1 
HETATM 1530 O O   . HOH   E 4 .   ? -27.299 27.266 -7.660  1.00 19.43 ? 669 HOH   A O   1 
HETATM 1531 O O   . HOH   E 4 .   ? 0.287   11.053 4.563   1.00 30.91 ? 670 HOH   A O   1 
HETATM 1532 O O   . HOH   E 4 .   ? -35.368 22.224 1.195   1.00 43.38 ? 671 HOH   A O   1 
HETATM 1533 O O   . HOH   E 4 .   ? -30.764 21.715 -10.323 1.00 40.82 ? 672 HOH   A O   1 
HETATM 1534 O O   . HOH   E 4 .   ? -10.443 0.051  3.842   1.00 28.77 ? 673 HOH   A O   1 
HETATM 1535 O O   . HOH   E 4 .   ? -34.035 13.976 -5.092  1.00 44.69 ? 674 HOH   A O   1 
HETATM 1536 O O   . HOH   E 4 .   ? -28.643 28.904 0.235   1.00 34.19 ? 675 HOH   A O   1 
HETATM 1537 O O   . HOH   E 4 .   ? -24.375 -1.376 2.972   1.00 51.17 ? 676 HOH   A O   1 
HETATM 1538 O O   . HOH   E 4 .   ? 1.805   12.354 -5.592  1.00 43.63 ? 677 HOH   A O   1 
HETATM 1539 O O   . HOH   E 4 .   ? -1.683  17.073 8.279   1.00 35.05 ? 678 HOH   A O   1 
HETATM 1540 O O   . HOH   E 4 .   ? -31.757 23.034 0.900   1.00 21.76 ? 679 HOH   A O   1 
HETATM 1541 O O   . HOH   E 4 .   ? -10.428 10.985 13.217  1.00 36.16 ? 680 HOH   A O   1 
HETATM 1542 O O   . HOH   E 4 .   ? -24.779 18.277 12.479  1.00 37.45 ? 681 HOH   A O   1 
HETATM 1543 O O   . HOH   E 4 .   ? -2.194  5.866  -0.595  1.00 29.49 ? 682 HOH   A O   1 
HETATM 1544 O O   . HOH   E 4 .   ? -20.581 23.057 -14.204 1.00 49.69 ? 683 HOH   A O   1 
HETATM 1545 O O   . HOH   E 4 .   ? -14.310 4.761  -17.984 1.00 37.20 ? 684 HOH   A O   1 
HETATM 1546 O O   . HOH   E 4 .   ? -30.148 28.139 8.410   1.00 28.65 ? 685 HOH   A O   1 
HETATM 1547 O O   . HOH   E 4 .   ? -10.765 -4.815 -6.611  1.00 38.74 ? 686 HOH   A O   1 
HETATM 1548 O O   . HOH   E 4 .   ? -27.466 7.351  -12.133 1.00 41.46 ? 687 HOH   A O   1 
HETATM 1549 O O   . HOH   E 4 .   ? -32.133 24.578 -11.748 1.00 33.82 ? 688 HOH   A O   1 
HETATM 1550 O O   . HOH   E 4 .   ? -23.633 23.379 -12.651 1.00 33.14 ? 689 HOH   A O   1 
HETATM 1551 O O   . HOH   E 4 .   ? -23.702 15.296 -17.254 1.00 27.39 ? 690 HOH   A O   1 
HETATM 1552 O O   . HOH   E 4 .   ? -13.815 9.684  13.558  1.00 39.36 ? 691 HOH   A O   1 
HETATM 1553 O O   . HOH   E 4 .   ? -31.688 2.888  6.399   1.00 25.29 ? 692 HOH   A O   1 
HETATM 1554 O O   . HOH   E 4 .   ? -25.154 -1.125 -2.937  1.00 35.36 ? 693 HOH   A O   1 
HETATM 1555 O O   . HOH   E 4 .   ? -19.905 -2.731 -3.567  1.00 22.00 ? 694 HOH   A O   1 
HETATM 1556 O O   . HOH   E 4 .   ? -29.346 28.603 -4.356  1.00 16.43 ? 695 HOH   A O   1 
HETATM 1557 O O   . HOH   E 4 .   ? -30.770 7.271  -2.464  1.00 13.94 ? 696 HOH   A O   1 
HETATM 1558 O O   . HOH   E 4 .   ? -21.730 3.832  -14.289 1.00 34.32 ? 697 HOH   A O   1 
HETATM 1559 O O   . HOH   E 4 .   ? 0.569   18.293 1.362   1.00 31.23 ? 698 HOH   A O   1 
HETATM 1560 O O   . HOH   E 4 .   ? -18.535 16.951 -11.945 1.00 14.07 ? 699 HOH   A O   1 
HETATM 1561 O O   . HOH   E 4 .   ? -13.452 -1.376 7.621   1.00 38.80 ? 700 HOH   A O   1 
HETATM 1562 O O   . HOH   E 4 .   ? -8.863  4.062  14.373  1.00 36.55 ? 701 HOH   A O   1 
HETATM 1563 O O   . HOH   E 4 .   ? -9.120  -0.917 5.892   1.00 41.54 ? 702 HOH   A O   1 
HETATM 1564 O O   . HOH   E 4 .   ? -29.003 18.681 16.495  1.00 45.96 ? 703 HOH   A O   1 
HETATM 1565 O O   . HOH   E 4 .   ? -21.060 25.346 12.070  1.00 17.25 ? 704 HOH   A O   1 
HETATM 1566 O O   . HOH   E 4 .   ? -6.459  0.487  0.712   1.00 44.41 ? 705 HOH   A O   1 
HETATM 1567 O O   . HOH   E 4 .   ? -31.369 13.400 -7.230  1.00 33.41 ? 706 HOH   A O   1 
HETATM 1568 O O   . HOH   E 4 .   ? -30.440 7.752  17.715  1.00 33.62 ? 707 HOH   A O   1 
HETATM 1569 O O   . HOH   E 4 .   ? -15.950 28.334 -1.252  1.00 17.99 ? 708 HOH   A O   1 
HETATM 1570 O O   . HOH   E 4 .   ? -11.682 7.698  15.456  1.00 55.80 ? 709 HOH   A O   1 
HETATM 1571 O O   . HOH   E 4 .   ? -28.406 7.342  19.795  1.00 24.44 ? 710 HOH   A O   1 
HETATM 1572 O O   . HOH   E 4 .   ? -22.716 32.080 9.155   1.00 39.20 ? 711 HOH   A O   1 
HETATM 1573 O O   . HOH   E 4 .   ? -31.592 26.044 6.973   1.00 30.05 ? 712 HOH   A O   1 
HETATM 1574 O O   . HOH   E 4 .   ? -11.502 25.790 -8.395  1.00 15.84 ? 713 HOH   A O   1 
HETATM 1575 O O   . HOH   E 4 .   ? -24.155 30.866 7.429   1.00 35.93 ? 714 HOH   A O   1 
HETATM 1576 O O   . HOH   E 4 .   ? -5.275  27.579 -2.891  1.00 33.63 ? 715 HOH   A O   1 
HETATM 1577 O O   . HOH   E 4 .   ? -34.276 13.356 8.548   1.00 26.23 ? 716 HOH   A O   1 
HETATM 1578 O O   . HOH   E 4 .   ? -6.316  -1.008 5.589   1.00 46.81 ? 717 HOH   A O   1 
HETATM 1579 O O   . HOH   E 4 .   ? -12.152 -3.704 7.981   1.00 34.38 ? 718 HOH   A O   1 
HETATM 1580 O O   . HOH   E 4 .   ? -14.168 26.280 -10.077 1.00 33.11 ? 719 HOH   A O   1 
HETATM 1581 O O   . HOH   E 4 .   ? -0.991  7.104  3.597   1.00 38.30 ? 720 HOH   A O   1 
HETATM 1582 O O   . HOH   E 4 .   ? -0.899  4.029  4.001   1.00 37.39 ? 721 HOH   A O   1 
HETATM 1583 O O   . HOH   E 4 .   ? -36.133 3.474  7.064   1.00 32.85 ? 722 HOH   A O   1 
HETATM 1584 O O   . HOH   E 4 .   ? -3.842  27.552 -0.559  1.00 33.30 ? 723 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . VAL   A 1   ? 0.5449 0.4923 0.2898 0.0534  -0.0154 0.0014  287 VAL   A N   
2    C CA  . VAL   A 1   ? 0.5481 0.4967 0.2414 0.0477  -0.0076 -0.0054 287 VAL   A CA  
3    C C   . VAL   A 1   ? 0.5220 0.5170 0.1942 0.0346  -0.0293 -0.0051 287 VAL   A C   
4    O O   . VAL   A 1   ? 0.5249 0.5757 0.2542 0.0552  -0.0454 -0.0078 287 VAL   A O   
5    C CB  . VAL   A 1   ? 0.5584 0.5044 0.2536 0.0484  0.0033  -0.0080 287 VAL   A CB  
6    C CG1 . VAL   A 1   ? 0.5621 0.5147 0.2547 0.0491  0.0250  0.0117  287 VAL   A CG1 
7    C CG2 . VAL   A 1   ? 0.5748 0.5110 0.2565 0.0417  -0.0100 0.0136  287 VAL   A CG2 
8    N N   . HIS   A 2   ? 0.4658 0.5067 0.0986 0.0165  -0.0175 -0.0130 288 HIS   A N   
9    C CA  . HIS   A 2   ? 0.4673 0.5068 0.1016 -0.0112 -0.0045 -0.0102 288 HIS   A CA  
10   C C   . HIS   A 2   ? 0.4148 0.4707 0.1051 -0.0253 -0.0255 0.0043  288 HIS   A C   
11   O O   . HIS   A 2   ? 0.4335 0.5576 0.0973 -0.0551 -0.0037 0.0179  288 HIS   A O   
12   C CB  . HIS   A 2   ? 0.5141 0.5254 0.1929 0.0048  -0.0064 -0.0130 288 HIS   A CB  
13   C CG  . HIS   A 2   ? 0.5791 0.5768 0.2179 0.0006  0.0165  -0.0374 288 HIS   A CG  
14   N ND1 . HIS   A 2   ? 0.5927 0.5984 0.2474 0.0009  0.0236  -0.0533 288 HIS   A ND1 
15   C CD2 . HIS   A 2   ? 0.5943 0.5875 0.2306 -0.0058 0.0116  -0.0391 288 HIS   A CD2 
16   C CE1 . HIS   A 2   ? 0.6304 0.5991 0.1856 -0.0180 0.0088  -0.0351 288 HIS   A CE1 
17   N NE2 . HIS   A 2   ? 0.6230 0.5980 0.2155 0.0012  0.0012  -0.0393 288 HIS   A NE2 
18   N N   . ILE   A 3   ? 0.3635 0.3566 0.1001 -0.0254 -0.0126 -0.0275 289 ILE   A N   
19   C CA  . ILE   A 3   ? 0.3607 0.3425 0.1061 -0.0197 -0.0238 0.0004  289 ILE   A CA  
20   C C   . ILE   A 3   ? 0.3647 0.3176 0.0683 -0.0275 -0.0121 0.0039  289 ILE   A C   
21   O O   . ILE   A 3   ? 0.3776 0.3244 0.1091 -0.0298 0.0075  0.0144  289 ILE   A O   
22   C CB  . ILE   A 3   ? 0.3793 0.3639 0.1196 -0.0176 -0.0293 -0.0060 289 ILE   A CB  
23   C CG1 . ILE   A 3   ? 0.3714 0.3762 0.1848 -0.0064 -0.0369 -0.0083 289 ILE   A CG1 
24   C CG2 . ILE   A 3   ? 0.4008 0.3763 0.1225 -0.0166 -0.0266 -0.0038 289 ILE   A CG2 
25   C CD1 . ILE   A 3   ? 0.3869 0.3782 0.2319 -0.0038 -0.0223 -0.0063 289 ILE   A CD1 
26   N N   . THR   A 4   ? 0.3736 0.3068 0.0519 -0.0186 -0.0089 0.0021  290 THR   A N   
27   C CA  . THR   A 4   ? 0.3776 0.3025 0.0691 -0.0181 0.0062  0.0199  290 THR   A CA  
28   C C   . THR   A 4   ? 0.3610 0.2751 0.0734 -0.0124 0.0006  0.0246  290 THR   A C   
29   O O   . THR   A 4   ? 0.4127 0.2770 0.0921 -0.0284 0.0053  0.0259  290 THR   A O   
30   C CB  . THR   A 4   ? 0.3982 0.3334 0.0909 -0.0080 0.0004  0.0191  290 THR   A CB  
31   O OG1 . THR   A 4   ? 0.4056 0.3824 0.1340 -0.0138 -0.0458 0.0083  290 THR   A OG1 
32   C CG2 . THR   A 4   ? 0.4180 0.3477 0.1011 -0.0074 -0.0046 0.0310  290 THR   A CG2 
33   N N   . LEU   A 5   ? 0.3185 0.2645 0.0611 -0.0135 -0.0033 0.0320  291 LEU   A N   
34   C CA  . LEU   A 5   ? 0.3013 0.2801 0.0670 -0.0072 -0.0025 0.0407  291 LEU   A CA  
35   C C   . LEU   A 5   ? 0.2945 0.2976 0.0936 -0.0116 -0.0136 0.0463  291 LEU   A C   
36   O O   . LEU   A 5   ? 0.2895 0.3295 0.1581 -0.0069 -0.0196 0.0759  291 LEU   A O   
37   C CB  . LEU   A 5   ? 0.3124 0.2821 0.0810 -0.0003 -0.0226 0.0381  291 LEU   A CB  
38   C CG  . LEU   A 5   ? 0.3156 0.2914 0.0827 0.0021  -0.0154 0.0231  291 LEU   A CG  
39   C CD1 . LEU   A 5   ? 0.3263 0.2899 0.0948 0.0065  -0.0052 0.0147  291 LEU   A CD1 
40   C CD2 . LEU   A 5   ? 0.3104 0.2902 0.0965 0.0013  -0.0224 0.0172  291 LEU   A CD2 
41   N N   . ASP   A 6   ? 0.2771 0.2989 0.1036 -0.0121 -0.0119 0.0519  292 ASP   A N   
42   C CA  . ASP   A 6   ? 0.2746 0.3171 0.1067 -0.0162 -0.0129 0.0378  292 ASP   A CA  
43   C C   . ASP   A 6   ? 0.2707 0.3145 0.1084 -0.0147 -0.0062 0.0476  292 ASP   A C   
44   O O   . ASP   A 6   ? 0.2523 0.2999 0.1084 -0.0232 -0.0019 0.0490  292 ASP   A O   
45   C CB  . ASP   A 6   ? 0.2985 0.3271 0.1341 -0.0229 -0.0119 0.0236  292 ASP   A CB  
46   C CG  . ASP   A 6   ? 0.3232 0.3369 0.1815 -0.0318 -0.0142 0.0167  292 ASP   A CG  
47   O OD1 . ASP   A 6   ? 0.3102 0.3637 0.2312 -0.0310 -0.0075 0.0108  292 ASP   A OD1 
48   O OD2 . ASP   A 6   ? 0.3806 0.3497 0.1669 -0.0346 -0.0228 -0.0158 292 ASP   A OD2 
49   N N   . PRO   A 7   ? 0.2843 0.3203 0.1156 -0.0011 -0.0069 0.0667  293 PRO   A N   
50   C CA  . PRO   A 7   ? 0.2904 0.3310 0.1366 0.0000  -0.0068 0.0596  293 PRO   A CA  
51   C C   . PRO   A 7   ? 0.2832 0.3258 0.1429 -0.0173 -0.0049 0.0536  293 PRO   A C   
52   O O   . PRO   A 7   ? 0.3227 0.3555 0.1315 -0.0262 -0.0071 0.0545  293 PRO   A O   
53   C CB  . PRO   A 7   ? 0.3017 0.3433 0.1777 0.0059  -0.0188 0.0558  293 PRO   A CB  
54   C CG  . PRO   A 7   ? 0.3263 0.3467 0.1735 0.0196  -0.0250 0.0682  293 PRO   A CG  
55   C CD  . PRO   A 7   ? 0.2957 0.3337 0.1385 0.0129  -0.0217 0.0718  293 PRO   A CD  
56   N N   . ASP   A 8   ? 0.2562 0.3201 0.1202 -0.0231 -0.0094 0.0659  294 ASP   A N   
57   C CA  . ASP   A 8   ? 0.2688 0.3354 0.1517 -0.0381 -0.0076 0.0591  294 ASP   A CA  
58   C C   . ASP   A 8   ? 0.2635 0.3192 0.1358 -0.0382 0.0037  0.0605  294 ASP   A C   
59   O O   . ASP   A 8   ? 0.2681 0.3359 0.1839 -0.0508 0.0146  0.0891  294 ASP   A O   
60   C CB  . ASP   A 8   ? 0.3094 0.3525 0.1658 -0.0503 -0.0230 0.0418  294 ASP   A CB  
61   C CG  . ASP   A 8   ? 0.3571 0.4018 0.2473 -0.0200 -0.0619 0.0144  294 ASP   A CG  
62   O OD1 . ASP   A 8   ? 0.3871 0.4374 0.3101 0.0065  -0.0800 -0.0041 294 ASP   A OD1 
63   O OD2 . ASP   A 8   ? 0.4543 0.4817 0.2977 -0.0240 -0.0979 -0.0340 294 ASP   A OD2 
64   N N   . THR   A 9   ? 0.2503 0.3038 0.1169 -0.0231 0.0033  0.0532  295 THR   A N   
65   C CA  . THR   A 9   ? 0.2643 0.2891 0.1133 -0.0191 -0.0064 0.0491  295 THR   A CA  
66   C C   . THR   A 9   ? 0.2521 0.2931 0.1114 -0.0029 -0.0047 0.0488  295 THR   A C   
67   O O   . THR   A 9   ? 0.2543 0.2913 0.1004 0.0059  0.0139  0.0728  295 THR   A O   
68   C CB  . THR   A 9   ? 0.2681 0.2871 0.0931 -0.0231 -0.0058 0.0496  295 THR   A CB  
69   O OG1 . THR   A 9   ? 0.2676 0.2862 0.0937 -0.0251 0.0111  0.0300  295 THR   A OG1 
70   C CG2 . THR   A 9   ? 0.2826 0.3006 0.1024 -0.0231 -0.0065 0.0437  295 THR   A CG2 
71   N N   . ALA   A 10  ? 0.2564 0.2973 0.1112 -0.0002 0.0050  0.0506  296 ALA   A N   
72   C CA  . ALA   A 10  ? 0.2451 0.3023 0.1065 0.0017  0.0131  0.0490  296 ALA   A CA  
73   C C   . ALA   A 10  ? 0.2508 0.3216 0.1093 0.0068  0.0213  0.0664  296 ALA   A C   
74   O O   . ALA   A 10  ? 0.2628 0.3635 0.1140 0.0091  0.0277  0.0889  296 ALA   A O   
75   C CB  . ALA   A 10  ? 0.2563 0.2984 0.1220 0.0038  0.0163  0.0470  296 ALA   A CB  
76   N N   . ASN   A 11  ? 0.2507 0.3162 0.0913 0.0139  0.0358  0.0654  297 ASN   A N   
77   C CA  . ASN   A 11  ? 0.2635 0.3020 0.1022 0.0146  0.0508  0.0504  297 ASN   A CA  
78   C C   . ASN   A 11  ? 0.2772 0.3073 0.1205 0.0200  0.0487  0.0551  297 ASN   A C   
79   O O   . ASN   A 11  ? 0.2913 0.2887 0.1536 0.0131  0.0548  0.0529  297 ASN   A O   
80   C CB  . ASN   A 11  ? 0.2706 0.2821 0.0938 0.0142  0.0452  0.0470  297 ASN   A CB  
81   C CG  . ASN   A 11  ? 0.2805 0.2867 0.1059 0.0115  0.0541  0.0378  297 ASN   A CG  
82   O OD1 . ASN   A 11  ? 0.3261 0.3019 0.1296 -0.0044 0.0610  0.0326  297 ASN   A OD1 
83   N ND2 . ASN   A 11  ? 0.2706 0.2887 0.1151 0.0145  0.0461  0.0413  297 ASN   A ND2 
84   N N   . PRO   A 12  ? 0.3041 0.3225 0.1569 0.0216  0.0854  0.0641  298 PRO   A N   
85   C CA  . PRO   A 12  ? 0.3228 0.3276 0.1764 0.0230  0.0991  0.0625  298 PRO   A CA  
86   C C   . PRO   A 12  ? 0.3266 0.3096 0.1504 0.0194  0.1063  0.0641  298 PRO   A C   
87   O O   . PRO   A 12  ? 0.3693 0.3127 0.1973 0.0000  0.0977  0.0574  298 PRO   A O   
88   C CB  . PRO   A 12  ? 0.3065 0.3583 0.2245 0.0173  0.1116  0.0512  298 PRO   A CB  
89   C CG  . PRO   A 12  ? 0.3154 0.3540 0.2118 0.0156  0.1058  0.0731  298 PRO   A CG  
90   C CD  . PRO   A 12  ? 0.3071 0.3403 0.1848 0.0172  0.0896  0.0668  298 PRO   A CD  
91   N N   . TRP   A 13  ? 0.3444 0.3012 0.1581 0.0010  0.0906  0.0519  299 TRP   A N   
92   C CA  . TRP   A 13  ? 0.3651 0.2983 0.1402 0.0046  0.0755  0.0373  299 TRP   A CA  
93   C C   . TRP   A 13  ? 0.3540 0.2826 0.1296 -0.0080 0.0663  0.0276  299 TRP   A C   
94   O O   . TRP   A 13  ? 0.3754 0.3026 0.1220 -0.0226 0.0594  0.0354  299 TRP   A O   
95   C CB  . TRP   A 13  ? 0.3916 0.3267 0.1539 0.0048  0.0678  0.0227  299 TRP   A CB  
96   C CG  . TRP   A 13  ? 0.4472 0.3419 0.1588 -0.0155 0.0689  -0.0046 299 TRP   A CG  
97   C CD1 . TRP   A 13  ? 0.4809 0.3633 0.1612 -0.0163 0.0667  -0.0004 299 TRP   A CD1 
98   C CD2 . TRP   A 13  ? 0.4876 0.3591 0.1707 -0.0181 0.0566  -0.0194 299 TRP   A CD2 
99   N NE1 . TRP   A 13  ? 0.5001 0.3685 0.1469 -0.0283 0.0667  0.0043  299 TRP   A NE1 
100  C CE2 . TRP   A 13  ? 0.4929 0.3734 0.1772 -0.0224 0.0546  -0.0197 299 TRP   A CE2 
101  C CE3 . TRP   A 13  ? 0.5046 0.3706 0.1658 -0.0140 0.0308  -0.0233 299 TRP   A CE3 
102  C CZ2 . TRP   A 13  ? 0.5132 0.3803 0.1789 -0.0267 0.0398  -0.0350 299 TRP   A CZ2 
103  C CZ3 . TRP   A 13  ? 0.5155 0.3614 0.1853 -0.0146 0.0343  -0.0295 299 TRP   A CZ3 
104  C CH2 . TRP   A 13  ? 0.5189 0.3729 0.1707 -0.0094 0.0429  -0.0420 299 TRP   A CH2 
105  N N   . LEU   A 14  ? 0.3214 0.2649 0.1132 0.0052  0.0599  0.0397  300 LEU   A N   
106  C CA  . LEU   A 14  ? 0.2851 0.2580 0.1172 0.0131  0.0507  0.0437  300 LEU   A CA  
107  C C   . LEU   A 14  ? 0.2644 0.2701 0.1070 0.0133  0.0468  0.0412  300 LEU   A C   
108  O O   . LEU   A 14  ? 0.2711 0.3102 0.1901 0.0204  0.0499  0.0655  300 LEU   A O   
109  C CB  . LEU   A 14  ? 0.2652 0.2537 0.1004 0.0136  0.0504  0.0385  300 LEU   A CB  
110  C CG  . LEU   A 14  ? 0.2700 0.2589 0.1113 0.0155  0.0416  0.0345  300 LEU   A CG  
111  C CD1 . LEU   A 14  ? 0.2621 0.2689 0.1179 0.0150  0.0492  0.0254  300 LEU   A CD1 
112  C CD2 . LEU   A 14  ? 0.2833 0.2674 0.1230 0.0206  0.0354  0.0286  300 LEU   A CD2 
113  N N   . ILE   A 15  ? 0.2585 0.2567 0.1011 0.0176  0.0355  0.0476  301 ILE   A N   
114  C CA  . ILE   A 15  ? 0.2555 0.2676 0.0734 0.0232  0.0404  0.0414  301 ILE   A CA  
115  C C   . ILE   A 15  ? 0.2445 0.2756 0.0731 0.0171  0.0345  0.0384  301 ILE   A C   
116  O O   . ILE   A 15  ? 0.2484 0.3067 0.0653 0.0135  0.0185  0.0260  301 ILE   A O   
117  C CB  . ILE   A 15  ? 0.2697 0.2693 0.0910 0.0248  0.0354  0.0405  301 ILE   A CB  
118  C CG1 . ILE   A 15  ? 0.2817 0.2794 0.0950 0.0276  0.0370  0.0338  301 ILE   A CG1 
119  C CG2 . ILE   A 15  ? 0.2906 0.2676 0.1021 0.0265  0.0311  0.0408  301 ILE   A CG2 
120  C CD1 . ILE   A 15  ? 0.2996 0.2926 0.1086 0.0314  0.0246  0.0249  301 ILE   A CD1 
121  N N   . LEU   A 16  ? 0.2587 0.2896 0.0854 0.0136  0.0201  0.0471  302 LEU   A N   
122  C CA  . LEU   A 16  ? 0.2798 0.2823 0.0946 0.0137  0.0193  0.0424  302 LEU   A CA  
123  C C   . LEU   A 16  ? 0.2658 0.2879 0.0953 0.0218  -0.0011 0.0428  302 LEU   A C   
124  O O   . LEU   A 16  ? 0.2608 0.3232 0.0987 0.0291  0.0131  0.0523  302 LEU   A O   
125  C CB  . LEU   A 16  ? 0.3081 0.3002 0.1405 0.0033  -0.0016 0.0366  302 LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3489 0.3077 0.1859 0.0016  -0.0097 0.0377  302 LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3645 0.3305 0.1760 0.0056  -0.0275 0.0230  302 LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.3560 0.3155 0.2000 0.0099  -0.0125 0.0235  302 LEU   A CD2 
129  N N   . SER   A 17  ? 0.2661 0.2883 0.0977 0.0269  -0.0048 0.0418  303 SER   A N   
130  C CA  . SER   A 17  ? 0.2685 0.2917 0.1036 0.0303  -0.0084 0.0462  303 SER   A CA  
131  C C   . SER   A 17  ? 0.2661 0.2942 0.1062 0.0175  0.0041  0.0334  303 SER   A C   
132  O O   . SER   A 17  ? 0.2668 0.2969 0.1022 -0.0064 -0.0101 0.0504  303 SER   A O   
133  C CB  . SER   A 17  ? 0.2664 0.2882 0.1197 0.0311  -0.0170 0.0459  303 SER   A CB  
134  O OG  . SER   A 17  ? 0.2700 0.2911 0.0993 0.0346  -0.0254 0.0350  303 SER   A OG  
135  N N   . GLU   A 18  ? 0.2813 0.3167 0.1179 0.0290  -0.0139 0.0321  304 GLU   A N   
136  C CA  . GLU   A 18  ? 0.3086 0.3432 0.1542 0.0215  -0.0310 0.0270  304 GLU   A CA  
137  C C   . GLU   A 18  ? 0.2932 0.3161 0.1391 0.0218  -0.0403 0.0282  304 GLU   A C   
138  O O   . GLU   A 18  ? 0.3139 0.3433 0.1462 0.0190  -0.0497 0.0456  304 GLU   A O   
139  C CB  . GLU   A 18  ? 0.3402 0.3655 0.1830 0.0291  -0.0333 0.0431  304 GLU   A CB  
140  C CG  . GLU   A 18  ? 0.3730 0.4202 0.2002 0.0180  -0.0461 0.0622  304 GLU   A CG  
141  C CD  . GLU   A 18  ? 0.3982 0.4642 0.2173 0.0009  -0.0631 0.0656  304 GLU   A CD  
142  O OE1 . GLU   A 18  ? 0.4378 0.5264 0.2528 0.0172  -0.0183 0.0590  304 GLU   A OE1 
143  O OE2 . GLU   A 18  ? 0.4631 0.5419 0.2333 -0.0197 -0.0910 0.0399  304 GLU   A OE2 
144  N N   . ASP   A 19  ? 0.2869 0.3028 0.0990 0.0143  -0.0460 0.0307  305 ASP   A N   
145  C CA  . ASP   A 19  ? 0.2804 0.2884 0.1032 0.0081  -0.0540 0.0249  305 ASP   A CA  
146  C C   . ASP   A 19  ? 0.2848 0.2796 0.1034 -0.0026 -0.0381 0.0356  305 ASP   A C   
147  O O   . ASP   A 19  ? 0.2982 0.2684 0.1017 -0.0057 -0.0398 0.0341  305 ASP   A O   
148  C CB  . ASP   A 19  ? 0.2923 0.2830 0.0941 0.0085  -0.0417 0.0325  305 ASP   A CB  
149  C CG  . ASP   A 19  ? 0.2862 0.2893 0.1170 0.0026  -0.0291 0.0585  305 ASP   A CG  
150  O OD1 . ASP   A 19  ? 0.2875 0.2720 0.0947 0.0064  -0.0279 0.0327  305 ASP   A OD1 
151  O OD2 . ASP   A 19  ? 0.3054 0.3197 0.1485 -0.0016 0.0019  0.0741  305 ASP   A OD2 
152  N N   . ARG   A 20  ? 0.2741 0.2759 0.1004 -0.0036 -0.0411 0.0269  306 ARG   A N   
153  C CA  . ARG   A 20  ? 0.2693 0.2748 0.1181 -0.0071 -0.0352 0.0353  306 ARG   A CA  
154  C C   . ARG   A 20  ? 0.2603 0.2549 0.0907 -0.0088 -0.0323 0.0327  306 ARG   A C   
155  O O   . ARG   A 20  ? 0.2639 0.2463 0.1195 -0.0159 -0.0339 0.0279  306 ARG   A O   
156  C CB  . ARG   A 20  ? 0.2722 0.2910 0.1586 -0.0134 -0.0411 0.0521  306 ARG   A CB  
157  C CG  . ARG   A 20  ? 0.2836 0.3202 0.1940 -0.0218 -0.0387 0.0633  306 ARG   A CG  
158  C CD  . ARG   A 20  ? 0.3072 0.3533 0.2209 -0.0277 -0.0411 0.0675  306 ARG   A CD  
159  N NE  . ARG   A 20  ? 0.3173 0.3855 0.2291 -0.0201 -0.0376 0.0692  306 ARG   A NE  
160  C CZ  . ARG   A 20  ? 0.3213 0.4043 0.2388 -0.0294 -0.0395 0.0816  306 ARG   A CZ  
161  N NH1 . ARG   A 20  ? 0.3534 0.4128 0.2463 -0.0341 -0.0470 0.0630  306 ARG   A NH1 
162  N NH2 . ARG   A 20  ? 0.3288 0.4557 0.3044 -0.0294 -0.0293 0.0757  306 ARG   A NH2 
163  N N   . ARG   A 21  ? 0.2477 0.2509 0.0784 -0.0042 -0.0219 0.0197  307 ARG   A N   
164  C CA  . ARG   A 21  ? 0.2473 0.2622 0.0679 -0.0119 -0.0155 0.0221  307 ARG   A CA  
165  C C   . ARG   A 21  ? 0.2429 0.2646 0.0661 0.0001  -0.0052 0.0066  307 ARG   A C   
166  O O   . ARG   A 21  ? 0.2506 0.2975 0.0570 0.0101  -0.0162 -0.0127 307 ARG   A O   
167  C CB  . ARG   A 21  ? 0.2554 0.2743 0.0824 -0.0148 -0.0119 0.0293  307 ARG   A CB  
168  C CG  . ARG   A 21  ? 0.2804 0.3015 0.0934 -0.0176 -0.0183 0.0145  307 ARG   A CG  
169  C CD  . ARG   A 21  ? 0.2870 0.3119 0.1021 -0.0159 -0.0171 0.0176  307 ARG   A CD  
170  N NE  . ARG   A 21  ? 0.2992 0.3286 0.0917 -0.0128 0.0030  0.0137  307 ARG   A NE  
171  C CZ  . ARG   A 21  ? 0.3004 0.3338 0.0860 -0.0115 0.0133  0.0116  307 ARG   A CZ  
172  N NH1 . ARG   A 21  ? 0.3087 0.3303 0.0930 -0.0052 0.0280  -0.0072 307 ARG   A NH1 
173  N NH2 . ARG   A 21  ? 0.2971 0.3537 0.1028 -0.0130 0.0274  -0.0005 307 ARG   A NH2 
174  N N   . GLN   A 22  ? 0.2313 0.2519 0.0587 -0.0037 -0.0018 0.0119  308 GLN   A N   
175  C CA  . GLN   A 22  ? 0.2457 0.2582 0.0577 -0.0123 0.0047  0.0128  308 GLN   A CA  
176  C C   . GLN   A 22  ? 0.2251 0.2561 0.0497 -0.0026 -0.0008 0.0161  308 GLN   A C   
177  O O   . GLN   A 22  ? 0.2330 0.2712 0.0723 0.0029  -0.0036 0.0133  308 GLN   A O   
178  C CB  . GLN   A 22  ? 0.2700 0.2613 0.0693 -0.0162 -0.0011 0.0118  308 GLN   A CB  
179  C CG  . GLN   A 22  ? 0.2870 0.2716 0.0910 -0.0127 -0.0262 0.0153  308 GLN   A CG  
180  C CD  . GLN   A 22  ? 0.3035 0.2757 0.1215 -0.0180 -0.0402 0.0119  308 GLN   A CD  
181  O OE1 . GLN   A 22  ? 0.3370 0.3030 0.1763 -0.0044 -0.0365 0.0015  308 GLN   A OE1 
182  N NE2 . GLN   A 22  ? 0.2939 0.2686 0.1156 -0.0155 -0.0497 0.0200  308 GLN   A NE2 
183  N N   . VAL   A 23  ? 0.2242 0.2610 0.0443 -0.0011 0.0036  0.0144  309 VAL   A N   
184  C CA  . VAL   A 23  ? 0.2225 0.2601 0.0568 -0.0025 0.0110  0.0152  309 VAL   A CA  
185  C C   . VAL   A 23  ? 0.2295 0.2512 0.0624 0.0004  0.0098  0.0087  309 VAL   A C   
186  O O   . VAL   A 23  ? 0.2347 0.2654 0.0465 0.0121  0.0124  0.0043  309 VAL   A O   
187  C CB  . VAL   A 23  ? 0.2494 0.2615 0.0685 -0.0075 0.0134  0.0124  309 VAL   A CB  
188  C CG1 . VAL   A 23  ? 0.2622 0.2539 0.0724 0.0005  0.0007  0.0149  309 VAL   A CG1 
189  C CG2 . VAL   A 23  ? 0.2557 0.2625 0.0760 -0.0110 0.0186  0.0185  309 VAL   A CG2 
190  N N   . ARG   A 24  ? 0.2365 0.2553 0.0544 -0.0004 0.0089  0.0101  310 ARG   A N   
191  C CA  . ARG   A 24  ? 0.2380 0.2592 0.0604 -0.0035 0.0140  0.0061  310 ARG   A CA  
192  C C   . ARG   A 24  ? 0.2548 0.2508 0.0656 -0.0060 0.0258  0.0005  310 ARG   A C   
193  O O   . ARG   A 24  ? 0.2682 0.2629 0.0803 -0.0144 0.0327  0.0106  310 ARG   A O   
194  C CB  . ARG   A 24  ? 0.2438 0.2661 0.0700 0.0005  0.0234  0.0086  310 ARG   A CB  
195  C CG  . ARG   A 24  ? 0.2407 0.2715 0.0917 -0.0008 0.0247  0.0129  310 ARG   A CG  
196  C CD  . ARG   A 24  ? 0.2623 0.2841 0.1362 0.0006  0.0276  0.0250  310 ARG   A CD  
197  N NE  . ARG   A 24  ? 0.2729 0.2811 0.1651 0.0059  0.0289  0.0297  310 ARG   A NE  
198  C CZ  . ARG   A 24  ? 0.2993 0.2857 0.1836 0.0154  0.0218  0.0203  310 ARG   A CZ  
199  N NH1 . ARG   A 24  ? 0.3201 0.3035 0.1879 0.0091  0.0040  0.0335  310 ARG   A NH1 
200  N NH2 . ARG   A 24  ? 0.3137 0.2875 0.2191 0.0259  0.0166  0.0156  310 ARG   A NH2 
201  N N   . LEU   A 25  ? 0.2681 0.2641 0.0599 -0.0141 0.0205  0.0120  311 LEU   A N   
202  C CA  . LEU   A 25  ? 0.2818 0.2782 0.0660 -0.0079 0.0352  0.0014  311 LEU   A CA  
203  C C   . LEU   A 25  ? 0.3023 0.2843 0.0781 0.0021  0.0325  0.0132  311 LEU   A C   
204  O O   . LEU   A 25  ? 0.3216 0.2907 0.0979 -0.0085 0.0397  0.0145  311 LEU   A O   
205  C CB  . LEU   A 25  ? 0.2857 0.2894 0.0643 -0.0113 0.0276  0.0025  311 LEU   A CB  
206  C CG  . LEU   A 25  ? 0.3089 0.3049 0.1114 -0.0098 0.0240  0.0076  311 LEU   A CG  
207  C CD1 . LEU   A 25  ? 0.3169 0.3016 0.0931 0.0005  0.0208  -0.0028 311 LEU   A CD1 
208  C CD2 . LEU   A 25  ? 0.3266 0.3132 0.1282 -0.0062 -0.0108 0.0033  311 LEU   A CD2 
209  N N   . GLY   A 26  ? 0.3171 0.2873 0.0957 0.0062  0.0503  0.0195  312 GLY   A N   
210  C CA  . GLY   A 26  ? 0.3513 0.3145 0.1360 0.0211  0.0547  0.0033  312 GLY   A CA  
211  C C   . GLY   A 26  ? 0.4099 0.3413 0.1484 0.0271  0.0537  -0.0198 312 GLY   A C   
212  O O   . GLY   A 26  ? 0.4402 0.3503 0.1553 0.0181  0.0434  -0.0152 312 GLY   A O   
213  N N   . ASP   A 27  ? 0.4496 0.3733 0.1946 0.0384  0.0636  -0.0319 313 ASP   A N   
214  C CA  . ASP   A 27  ? 0.4846 0.3955 0.1945 0.0326  0.0844  -0.0339 313 ASP   A CA  
215  C C   . ASP   A 27  ? 0.4941 0.4171 0.2150 0.0203  0.0795  -0.0291 313 ASP   A C   
216  O O   . ASP   A 27  ? 0.5203 0.4586 0.2121 0.0079  0.0491  -0.0774 313 ASP   A O   
217  C CB  . ASP   A 27  ? 0.5377 0.4081 0.2481 0.0346  0.0968  -0.0371 313 ASP   A CB  
218  C CG  . ASP   A 27  ? 0.5680 0.4213 0.3140 0.0284  0.1094  -0.0310 313 ASP   A CG  
219  O OD1 . ASP   A 27  ? 0.5784 0.4770 0.3785 0.0303  0.1194  -0.0548 313 ASP   A OD1 
220  O OD2 . ASP   A 27  ? 0.6393 0.4648 0.3938 0.0517  0.0777  0.0084  313 ASP   A OD2 
221  N N   . THR   A 28  ? 0.4813 0.4061 0.1885 0.0159  0.0825  -0.0374 314 THR   A N   
222  C CA  . THR   A 28  ? 0.4786 0.4070 0.2365 0.0167  0.0745  -0.0423 314 THR   A CA  
223  C C   . THR   A 28  ? 0.4686 0.4239 0.2181 0.0131  0.0622  -0.0349 314 THR   A C   
224  O O   . THR   A 28  ? 0.4452 0.4254 0.2202 0.0006  0.0392  0.0193  314 THR   A O   
225  C CB  . THR   A 28  ? 0.4784 0.4475 0.2655 0.0129  0.0899  -0.0482 314 THR   A CB  
226  O OG1 . THR   A 28  ? 0.4783 0.4758 0.3040 0.0331  0.0977  -0.0433 314 THR   A OG1 
227  C CG2 . THR   A 28  ? 0.4994 0.4586 0.2822 0.0064  0.0751  -0.0489 314 THR   A CG2 
228  N N   . GLN   A 29  ? 0.4418 0.4308 0.1821 0.0258  0.0737  -0.0138 315 GLN   A N   
229  C CA  . GLN   A 29  ? 0.4392 0.4280 0.2060 0.0355  0.0755  -0.0107 315 GLN   A CA  
230  C C   . GLN   A 29  ? 0.4152 0.4345 0.2280 0.0566  0.0847  0.0021  315 GLN   A C   
231  O O   . GLN   A 29  ? 0.4369 0.4494 0.2999 0.0775  0.0810  -0.0306 315 GLN   A O   
232  C CB  . GLN   A 29  ? 0.4666 0.4441 0.1935 0.0304  0.0705  0.0063  315 GLN   A CB  
233  C CG  . GLN   A 29  ? 0.4799 0.4723 0.2231 0.0156  0.0604  0.0157  315 GLN   A CG  
234  C CD  . GLN   A 29  ? 0.5270 0.5023 0.2341 0.0135  0.0467  0.0447  315 GLN   A CD  
235  O OE1 . GLN   A 29  ? 0.5427 0.6222 0.2443 0.0155  0.0581  0.0440  315 GLN   A OE1 
236  N NE2 . GLN   A 29  ? 0.5543 0.5134 0.2897 -0.0021 0.0358  0.0573  315 GLN   A NE2 
237  N N   . GLN   A 30  ? 0.4043 0.4422 0.2383 0.0587  0.0767  0.0041  316 GLN   A N   
238  C CA  . GLN   A 30  ? 0.3881 0.4513 0.2661 0.0650  0.0675  0.0218  316 GLN   A CA  
239  C C   . GLN   A 30  ? 0.3865 0.4797 0.2693 0.0644  0.0767  0.0375  316 GLN   A C   
240  O O   . GLN   A 30  ? 0.3995 0.4863 0.3302 0.0544  0.0766  0.0699  316 GLN   A O   
241  C CB  . GLN   A 30  ? 0.3777 0.4668 0.2584 0.0616  0.0624  0.0397  316 GLN   A CB  
242  C CG  . GLN   A 30  ? 0.3674 0.4956 0.2820 0.0627  0.0535  0.0480  316 GLN   A CG  
243  C CD  . GLN   A 30  ? 0.3639 0.5026 0.2827 0.0697  0.0383  0.0484  316 GLN   A CD  
244  O OE1 . GLN   A 30  ? 0.3682 0.5355 0.3550 0.0650  0.0241  0.0461  316 GLN   A OE1 
245  N NE2 . GLN   A 30  ? 0.3522 0.4920 0.2736 0.0699  0.0278  0.0618  316 GLN   A NE2 
246  N N   . SER   A 31  ? 0.3945 0.5019 0.3233 0.0661  0.0685  0.0354  317 SER   A N   
247  C CA  . SER   A 31  ? 0.3982 0.5188 0.3576 0.0570  0.0665  0.0174  317 SER   A CA  
248  C C   . SER   A 31  ? 0.4290 0.5335 0.3638 0.0538  0.0495  0.0028  317 SER   A C   
249  O O   . SER   A 31  ? 0.4285 0.5433 0.4185 0.0502  0.0221  0.0128  317 SER   A O   
250  C CB  . SER   A 31  ? 0.3980 0.5328 0.3907 0.0586  0.0839  0.0112  317 SER   A CB  
251  O OG  . SER   A 31  ? 0.4474 0.5543 0.4433 0.0441  0.0899  -0.0050 317 SER   A OG  
252  N N   . ILE   A 32  ? 0.4520 0.5403 0.3367 0.0309  0.0418  0.0035  318 ILE   A N   
253  C CA  . ILE   A 32  ? 0.4391 0.5340 0.3021 0.0262  0.0643  0.0155  318 ILE   A CA  
254  C C   . ILE   A 32  ? 0.4553 0.5614 0.2917 -0.0171 0.0542  0.0119  318 ILE   A C   
255  O O   . ILE   A 32  ? 0.4296 0.5845 0.3004 -0.0414 0.0751  0.0228  318 ILE   A O   
256  C CB  . ILE   A 32  ? 0.4460 0.5195 0.2694 0.0374  0.0577  0.0354  318 ILE   A CB  
257  C CG1 . ILE   A 32  ? 0.4454 0.5060 0.2792 0.0413  0.0544  0.0493  318 ILE   A CG1 
258  C CG2 . ILE   A 32  ? 0.4545 0.5251 0.2508 0.0417  0.0701  0.0339  318 ILE   A CG2 
259  C CD1 . ILE   A 32  ? 0.4546 0.5032 0.2680 0.0392  0.0487  0.0387  318 ILE   A CD1 
260  N N   . PRO   A 33  ? 0.4920 0.5676 0.2697 -0.0410 0.0432  0.0266  319 PRO   A N   
261  C CA  . PRO   A 33  ? 0.4878 0.5740 0.2626 -0.0381 0.0476  0.0164  319 PRO   A CA  
262  C C   . PRO   A 33  ? 0.4597 0.5780 0.2893 -0.0565 0.0607  0.0246  319 PRO   A C   
263  O O   . PRO   A 33  ? 0.4448 0.6147 0.3109 -0.0731 0.0715  -0.0006 319 PRO   A O   
264  C CB  . PRO   A 33  ? 0.4962 0.5639 0.2580 -0.0407 0.0397  0.0267  319 PRO   A CB  
265  C CG  . PRO   A 33  ? 0.4922 0.5541 0.2728 -0.0353 0.0321  0.0280  319 PRO   A CG  
266  C CD  . PRO   A 33  ? 0.4777 0.5567 0.2850 -0.0319 0.0398  0.0351  319 PRO   A CD  
267  N N   . GLY   A 34  ? 0.4502 0.5761 0.3126 -0.0761 0.0542  0.0308  320 GLY   A N   
268  C CA  . GLY   A 34  ? 0.4614 0.5778 0.2719 -0.0844 0.0389  0.0248  320 GLY   A CA  
269  C C   . GLY   A 34  ? 0.4586 0.5838 0.2547 -0.0875 0.0243  0.0252  320 GLY   A C   
270  O O   . GLY   A 34  ? 0.4850 0.5916 0.2044 -0.1061 0.0334  0.0061  320 GLY   A O   
271  N N   . ASN   A 35  ? 0.4112 0.5575 0.2400 -0.0808 0.0071  0.0400  321 ASN   A N   
272  C CA  . ASN   A 35  ? 0.3843 0.5439 0.2573 -0.0890 -0.0067 0.0414  321 ASN   A CA  
273  C C   . ASN   A 35  ? 0.3367 0.5326 0.2367 -0.1055 -0.0095 0.0175  321 ASN   A C   
274  O O   . ASN   A 35  ? 0.3383 0.5031 0.2157 -0.0920 -0.0155 -0.0068 321 ASN   A O   
275  C CB  . ASN   A 35  ? 0.3940 0.5493 0.2819 -0.0763 -0.0163 0.0707  321 ASN   A CB  
276  C CG  . ASN   A 35  ? 0.4233 0.5453 0.3139 -0.0652 -0.0119 0.0774  321 ASN   A CG  
277  O OD1 . ASN   A 35  ? 0.4675 0.5570 0.3117 -0.0649 -0.0386 0.0878  321 ASN   A OD1 
278  N ND2 . ASN   A 35  ? 0.4193 0.5440 0.3195 -0.0635 0.0347  0.1077  321 ASN   A ND2 
279  N N   . GLU   A 36  ? 0.3266 0.5241 0.2331 -0.1126 0.0046  0.0258  322 GLU   A N   
280  C CA  . GLU   A 36  ? 0.3463 0.5486 0.2761 -0.1033 0.0082  0.0259  322 GLU   A CA  
281  C C   . GLU   A 36  ? 0.3343 0.5066 0.2050 -0.0979 0.0125  0.0463  322 GLU   A C   
282  O O   . GLU   A 36  ? 0.3506 0.5117 0.2247 -0.0681 0.0331  0.0656  322 GLU   A O   
283  C CB  . GLU   A 36  ? 0.3895 0.5765 0.3488 -0.1096 0.0178  0.0131  322 GLU   A CB  
284  C CG  . GLU   A 36  ? 0.4503 0.6199 0.3784 -0.0898 0.0077  0.0050  322 GLU   A CG  
285  C CD  . GLU   A 36  ? 0.4988 0.6521 0.4591 -0.0637 0.0086  0.0007  322 GLU   A CD  
286  O OE1 . GLU   A 36  ? 0.5779 0.7166 0.4742 -0.0678 -0.0155 -0.0132 322 GLU   A OE1 
287  O OE2 . GLU   A 36  ? 0.5401 0.6794 0.5064 -0.0615 -0.0079 -0.0017 322 GLU   A OE2 
288  N N   . GLU   A 37  ? 0.3250 0.4565 0.1635 -0.0938 -0.0244 0.0195  323 GLU   A N   
289  C CA  . GLU   A 37  ? 0.3221 0.4382 0.1667 -0.0784 -0.0197 0.0198  323 GLU   A CA  
290  C C   . GLU   A 37  ? 0.2809 0.3962 0.0966 -0.0571 -0.0118 0.0411  323 GLU   A C   
291  O O   . GLU   A 37  ? 0.2804 0.4019 0.1434 -0.0757 -0.0187 0.0261  323 GLU   A O   
292  C CB  . GLU   A 37  ? 0.3539 0.4568 0.1640 -0.0847 -0.0124 0.0184  323 GLU   A CB  
293  C CG  . GLU   A 37  ? 0.4014 0.4861 0.1800 -0.0978 -0.0169 0.0130  323 GLU   A CG  
294  C CD  . GLU   A 37  ? 0.4602 0.5276 0.1959 -0.0955 -0.0288 0.0152  323 GLU   A CD  
295  O OE1 . GLU   A 37  ? 0.5449 0.5534 0.2571 -0.0821 -0.0493 -0.0046 323 GLU   A OE1 
296  O OE2 . GLU   A 37  ? 0.5270 0.5692 0.2828 -0.1000 -0.0595 -0.0224 323 GLU   A OE2 
297  N N   . ARG   A 38  ? 0.2780 0.3680 0.1101 -0.0539 -0.0011 0.0567  324 ARG   A N   
298  C CA  . ARG   A 38  ? 0.2659 0.3529 0.1228 -0.0407 0.0055  0.0524  324 ARG   A CA  
299  C C   . ARG   A 38  ? 0.2659 0.3238 0.1175 -0.0336 0.0150  0.0589  324 ARG   A C   
300  O O   . ARG   A 38  ? 0.2602 0.3392 0.1301 -0.0522 0.0082  0.0711  324 ARG   A O   
301  C CB  . ARG   A 38  ? 0.2772 0.3655 0.1345 -0.0262 0.0054  0.0591  324 ARG   A CB  
302  C CG  . ARG   A 38  ? 0.2839 0.3625 0.1389 -0.0233 0.0288  0.0780  324 ARG   A CG  
303  C CD  . ARG   A 38  ? 0.2928 0.3798 0.1676 -0.0091 0.0272  0.0748  324 ARG   A CD  
304  N NE  . ARG   A 38  ? 0.3068 0.4077 0.2024 -0.0054 0.0195  0.0732  324 ARG   A NE  
305  C CZ  . ARG   A 38  ? 0.3106 0.4004 0.2009 0.0138  0.0019  0.0620  324 ARG   A CZ  
306  N NH1 . ARG   A 38  ? 0.3140 0.4174 0.2319 0.0233  -0.0108 0.0574  324 ARG   A NH1 
307  N NH2 . ARG   A 38  ? 0.2999 0.4080 0.2331 0.0060  0.0013  0.0536  324 ARG   A NH2 
308  N N   . PHE   A 39  ? 0.2667 0.3001 0.0798 -0.0269 0.0116  0.0514  325 PHE   A N   
309  C CA  . PHE   A 39  ? 0.2635 0.2878 0.0812 -0.0095 0.0139  0.0449  325 PHE   A CA  
310  C C   . PHE   A 39  ? 0.2622 0.2853 0.0880 -0.0012 0.0236  0.0495  325 PHE   A C   
311  O O   . PHE   A 39  ? 0.2959 0.3011 0.0974 0.0000  0.0334  0.0453  325 PHE   A O   
312  C CB  . PHE   A 39  ? 0.2659 0.2764 0.0889 -0.0065 0.0122  0.0404  325 PHE   A CB  
313  C CG  . PHE   A 39  ? 0.2583 0.2652 0.0884 -0.0151 0.0112  0.0349  325 PHE   A CG  
314  C CD1 . PHE   A 39  ? 0.2730 0.2751 0.0813 -0.0051 0.0030  0.0332  325 PHE   A CD1 
315  C CD2 . PHE   A 39  ? 0.2704 0.2743 0.0948 -0.0144 0.0028  0.0423  325 PHE   A CD2 
316  C CE1 . PHE   A 39  ? 0.2694 0.2639 0.0926 -0.0036 0.0026  0.0474  325 PHE   A CE1 
317  C CE2 . PHE   A 39  ? 0.2718 0.2641 0.0832 -0.0147 0.0055  0.0415  325 PHE   A CE2 
318  C CZ  . PHE   A 39  ? 0.2785 0.2653 0.0953 -0.0131 0.0088  0.0487  325 PHE   A CZ  
319  N N   . ASP   A 40  ? 0.2630 0.2834 0.0948 0.0076  0.0347  0.0504  326 ASP   A N   
320  C CA  . ASP   A 40  ? 0.2708 0.2917 0.0963 0.0008  0.0417  0.0404  326 ASP   A CA  
321  C C   . ASP   A 40  ? 0.2424 0.2717 0.0818 0.0017  0.0554  0.0391  326 ASP   A C   
322  O O   . ASP   A 40  ? 0.2681 0.2871 0.1036 0.0204  0.0608  0.0364  326 ASP   A O   
323  C CB  . ASP   A 40  ? 0.2887 0.3170 0.0951 -0.0060 0.0472  0.0383  326 ASP   A CB  
324  C CG  . ASP   A 40  ? 0.3110 0.3199 0.1038 -0.0148 0.0360  0.0383  326 ASP   A CG  
325  O OD1 . ASP   A 40  ? 0.3210 0.3412 0.1054 -0.0156 0.0305  0.0549  326 ASP   A OD1 
326  O OD2 . ASP   A 40  ? 0.3467 0.3297 0.1333 -0.0344 0.0474  0.0360  326 ASP   A OD2 
327  N N   . SER   A 41  ? 0.2510 0.2780 0.0679 0.0041  0.0502  0.0289  327 SER   A N   
328  C CA  . SER   A 41  ? 0.2647 0.3072 0.0853 0.0003  0.0388  0.0280  327 SER   A CA  
329  C C   . SER   A 41  ? 0.2774 0.3103 0.0749 -0.0106 0.0328  0.0351  327 SER   A C   
330  O O   . SER   A 41  ? 0.2992 0.3431 0.0796 -0.0115 0.0267  0.0249  327 SER   A O   
331  C CB  . SER   A 41  ? 0.2645 0.3113 0.0907 -0.0052 0.0307  0.0339  327 SER   A CB  
332  O OG  . SER   A 41  ? 0.2785 0.3246 0.0844 -0.0150 0.0546  0.0318  327 SER   A OG  
333  N N   . TYR   A 42  ? 0.2705 0.3037 0.0740 -0.0046 0.0257  0.0439  328 TYR   A N   
334  C CA  . TYR   A 42  ? 0.2726 0.2948 0.0747 -0.0040 0.0197  0.0470  328 TYR   A CA  
335  C C   . TYR   A 42  ? 0.2684 0.2906 0.0823 -0.0063 0.0190  0.0483  328 TYR   A C   
336  O O   . TYR   A 42  ? 0.2679 0.2932 0.0679 -0.0024 0.0278  0.0395  328 TYR   A O   
337  C CB  . TYR   A 42  ? 0.2757 0.2888 0.0754 -0.0036 0.0314  0.0572  328 TYR   A CB  
338  C CG  . TYR   A 42  ? 0.2781 0.2735 0.0747 0.0001  0.0320  0.0534  328 TYR   A CG  
339  C CD1 . TYR   A 42  ? 0.2865 0.2665 0.0973 -0.0046 0.0259  0.0559  328 TYR   A CD1 
340  C CD2 . TYR   A 42  ? 0.2909 0.2784 0.0941 -0.0093 0.0256  0.0546  328 TYR   A CD2 
341  C CE1 . TYR   A 42  ? 0.2952 0.2652 0.0881 0.0069  0.0211  0.0476  328 TYR   A CE1 
342  C CE2 . TYR   A 42  ? 0.3025 0.2757 0.0911 -0.0039 0.0211  0.0523  328 TYR   A CE2 
343  C CZ  . TYR   A 42  ? 0.2916 0.2681 0.0882 0.0035  0.0248  0.0446  328 TYR   A CZ  
344  O OH  . TYR   A 42  ? 0.3099 0.2675 0.0921 0.0196  0.0376  0.0429  328 TYR   A OH  
345  N N   . PRO   A 43  ? 0.2624 0.3005 0.0799 -0.0169 0.0086  0.0410  329 PRO   A N   
346  C CA  . PRO   A 43  ? 0.2586 0.2867 0.0668 -0.0102 0.0178  0.0268  329 PRO   A CA  
347  C C   . PRO   A 43  ? 0.2254 0.2708 0.0716 -0.0088 0.0073  0.0241  329 PRO   A C   
348  O O   . PRO   A 43  ? 0.2290 0.2777 0.0688 -0.0298 0.0037  0.0127  329 PRO   A O   
349  C CB  . PRO   A 43  ? 0.2811 0.3123 0.1085 -0.0191 0.0180  0.0264  329 PRO   A CB  
350  C CG  . PRO   A 43  ? 0.3110 0.3476 0.1166 -0.0235 0.0025  0.0310  329 PRO   A CG  
351  C CD  . PRO   A 43  ? 0.2941 0.3302 0.0924 -0.0165 -0.0122 0.0426  329 PRO   A CD  
352  N N   . MET   A 44  ? 0.2303 0.2671 0.0725 -0.0106 0.0124  0.0141  330 MET   A N   
353  C CA  . MET   A 44  ? 0.2296 0.2600 0.0687 -0.0063 0.0103  0.0140  330 MET   A CA  
354  C C   . MET   A 44  ? 0.2256 0.2450 0.0771 -0.0063 0.0074  0.0175  330 MET   A C   
355  O O   . MET   A 44  ? 0.2300 0.2515 0.0832 -0.0090 0.0059  0.0206  330 MET   A O   
356  C CB  . MET   A 44  ? 0.2373 0.2682 0.0638 -0.0046 0.0120  0.0238  330 MET   A CB  
357  C CG  . MET   A 44  ? 0.2393 0.2742 0.0753 0.0013  0.0096  0.0349  330 MET   A CG  
358  S SD  . MET   A 44  ? 0.2630 0.2795 0.0966 0.0024  0.0166  0.0570  330 MET   A SD  
359  C CE  . MET   A 44  ? 0.2637 0.2717 0.0637 0.0098  0.0242  0.0507  330 MET   A CE  
360  N N   . VAL   A 45  ? 0.2304 0.2521 0.0695 -0.0060 -0.0009 0.0056  331 VAL   A N   
361  C CA  . VAL   A 45  ? 0.2352 0.2455 0.0635 -0.0085 0.0005  0.0049  331 VAL   A CA  
362  C C   . VAL   A 45  ? 0.2413 0.2384 0.0722 -0.0129 0.0003  0.0002  331 VAL   A C   
363  O O   . VAL   A 45  ? 0.2407 0.2443 0.0508 -0.0098 -0.0003 0.0009  331 VAL   A O   
364  C CB  . VAL   A 45  ? 0.2467 0.2491 0.0681 -0.0078 -0.0092 -0.0002 331 VAL   A CB  
365  C CG1 . VAL   A 45  ? 0.2589 0.2475 0.0851 -0.0095 0.0043  0.0032  331 VAL   A CG1 
366  C CG2 . VAL   A 45  ? 0.2615 0.2507 0.0585 -0.0114 -0.0116 -0.0040 331 VAL   A CG2 
367  N N   . LEU   A 46  ? 0.2541 0.2437 0.0671 -0.0189 -0.0005 0.0046  332 LEU   A N   
368  C CA  . LEU   A 46  ? 0.2637 0.2396 0.0735 -0.0125 0.0060  0.0099  332 LEU   A CA  
369  C C   . LEU   A 46  ? 0.2724 0.2488 0.0845 -0.0101 0.0016  0.0191  332 LEU   A C   
370  O O   . LEU   A 46  ? 0.2788 0.2717 0.0691 0.0012  0.0084  0.0329  332 LEU   A O   
371  C CB  . LEU   A 46  ? 0.2840 0.2455 0.0885 -0.0121 -0.0025 0.0135  332 LEU   A CB  
372  C CG  . LEU   A 46  ? 0.2877 0.2524 0.0881 -0.0175 0.0016  0.0177  332 LEU   A CG  
373  C CD1 . LEU   A 46  ? 0.3082 0.2525 0.0993 -0.0135 -0.0051 0.0217  332 LEU   A CD1 
374  C CD2 . LEU   A 46  ? 0.2835 0.2609 0.0889 -0.0140 0.0091  0.0130  332 LEU   A CD2 
375  N N   . GLY   A 47  ? 0.2854 0.2596 0.0645 -0.0046 -0.0059 0.0121  333 GLY   A N   
376  C CA  . GLY   A 47  ? 0.2960 0.2482 0.0693 -0.0044 -0.0030 0.0212  333 GLY   A CA  
377  C C   . GLY   A 47  ? 0.3086 0.2494 0.0912 -0.0078 -0.0129 0.0116  333 GLY   A C   
378  O O   . GLY   A 47  ? 0.3198 0.2517 0.0942 -0.0172 -0.0204 0.0102  333 GLY   A O   
379  N N   . ALA   A 48  ? 0.3306 0.2612 0.0846 -0.0164 -0.0169 0.0213  334 ALA   A N   
380  C CA  . ALA   A 48  ? 0.3399 0.2920 0.1085 -0.0124 -0.0327 0.0038  334 ALA   A CA  
381  C C   . ALA   A 48  ? 0.3491 0.3080 0.1208 -0.0163 -0.0382 -0.0095 334 ALA   A C   
382  O O   . ALA   A 48  ? 0.3668 0.3295 0.1920 -0.0140 -0.0444 -0.0417 334 ALA   A O   
383  C CB  . ALA   A 48  ? 0.3549 0.3188 0.1030 -0.0090 -0.0560 0.0036  334 ALA   A CB  
384  N N   . GLN   A 49  ? 0.3594 0.3202 0.0985 -0.0161 -0.0436 -0.0134 335 GLN   A N   
385  C CA  . GLN   A 49  ? 0.3904 0.3310 0.1054 -0.0133 -0.0579 -0.0286 335 GLN   A CA  
386  C C   . GLN   A 49  ? 0.4006 0.3373 0.1233 -0.0049 -0.0685 -0.0376 335 GLN   A C   
387  O O   . GLN   A 49  ? 0.3933 0.3203 0.1157 -0.0035 -0.0674 -0.0541 335 GLN   A O   
388  C CB  . GLN   A 49  ? 0.4095 0.3506 0.1133 -0.0246 -0.0421 -0.0302 335 GLN   A CB  
389  C CG  . GLN   A 49  ? 0.4286 0.3559 0.1456 -0.0344 -0.0373 -0.0246 335 GLN   A CG  
390  C CD  . GLN   A 49  ? 0.4313 0.3620 0.1627 -0.0331 -0.0203 -0.0200 335 GLN   A CD  
391  O OE1 . GLN   A 49  ? 0.3668 0.3432 0.1355 -0.0552 0.0450  -0.0690 335 GLN   A OE1 
392  N NE2 . GLN   A 49  ? 0.4337 0.3829 0.1641 -0.0394 -0.0246 -0.0241 335 GLN   A NE2 
393  N N   . HIS   A 50  ? 0.4244 0.3531 0.1300 -0.0042 -0.0778 -0.0555 336 HIS   A N   
394  C CA  . HIS   A 50  ? 0.4236 0.3593 0.1601 0.0146  -0.0754 -0.0652 336 HIS   A CA  
395  C C   . HIS   A 50  ? 0.4343 0.3525 0.1573 0.0233  -0.0696 -0.0624 336 HIS   A C   
396  O O   . HIS   A 50  ? 0.4710 0.4389 0.1557 0.0634  -0.0837 -0.0669 336 HIS   A O   
397  C CB  . HIS   A 50  ? 0.4231 0.3868 0.1888 0.0070  -0.0638 -0.0641 336 HIS   A CB  
398  C CG  . HIS   A 50  ? 0.4301 0.4225 0.2230 0.0121  -0.0566 -0.0585 336 HIS   A CG  
399  N ND1 . HIS   A 50  ? 0.4498 0.4426 0.2744 0.0077  -0.0519 -0.0687 336 HIS   A ND1 
400  C CD2 . HIS   A 50  ? 0.4378 0.4362 0.2259 0.0149  -0.0587 -0.0304 336 HIS   A CD2 
401  C CE1 . HIS   A 50  ? 0.4369 0.4355 0.2383 -0.0029 -0.0647 -0.0736 336 HIS   A CE1 
402  N NE2 . HIS   A 50  ? 0.4385 0.4480 0.2185 0.0120  -0.0662 -0.0526 336 HIS   A NE2 
403  N N   . PHE   A 51  ? 0.4254 0.3015 0.1782 0.0153  -0.0543 -0.0582 337 PHE   A N   
404  C CA  . PHE   A 51  ? 0.4514 0.3120 0.1847 0.0100  -0.0233 -0.0572 337 PHE   A CA  
405  C C   . PHE   A 51  ? 0.4737 0.3087 0.2021 0.0093  -0.0191 -0.0662 337 PHE   A C   
406  O O   . PHE   A 51  ? 0.5161 0.2982 0.1879 0.0095  0.0071  -0.0724 337 PHE   A O   
407  C CB  . PHE   A 51  ? 0.4535 0.3159 0.2336 0.0159  -0.0083 -0.0517 337 PHE   A CB  
408  C CG  . PHE   A 51  ? 0.4681 0.3160 0.3177 0.0213  0.0252  -0.0488 337 PHE   A CG  
409  C CD1 . PHE   A 51  ? 0.4777 0.3121 0.3487 0.0231  0.0447  -0.0448 337 PHE   A CD1 
410  C CD2 . PHE   A 51  ? 0.4586 0.3173 0.3736 0.0237  0.0309  -0.0548 337 PHE   A CD2 
411  C CE1 . PHE   A 51  ? 0.4743 0.3259 0.3973 0.0102  0.0717  -0.0333 337 PHE   A CE1 
412  C CE2 . PHE   A 51  ? 0.4482 0.3118 0.4091 0.0246  0.0546  -0.0628 337 PHE   A CE2 
413  C CZ  . PHE   A 51  ? 0.4537 0.3222 0.4102 0.0157  0.0705  -0.0424 337 PHE   A CZ  
414  N N   . HIS   A 52  ? 0.5100 0.3369 0.2103 0.0166  0.0068  -0.0813 338 HIS   A N   
415  C CA  . HIS   A 52  ? 0.5231 0.3522 0.2572 0.0008  -0.0039 -0.1030 338 HIS   A CA  
416  C C   . HIS   A 52  ? 0.5234 0.3316 0.2335 -0.0138 -0.0026 -0.1054 338 HIS   A C   
417  O O   . HIS   A 52  ? 0.5601 0.3296 0.2655 -0.0220 0.0120  -0.0820 338 HIS   A O   
418  C CB  . HIS   A 52  ? 0.5305 0.4035 0.3405 -0.0125 -0.0042 -0.1171 338 HIS   A CB  
419  C CG  . HIS   A 52  ? 0.5491 0.4680 0.3946 -0.0088 -0.0028 -0.1070 338 HIS   A CG  
420  N ND1 . HIS   A 52  ? 0.5807 0.5213 0.4768 0.0003  0.0038  -0.0835 338 HIS   A ND1 
421  C CD2 . HIS   A 52  ? 0.5456 0.5094 0.3549 -0.0088 -0.0069 -0.1061 338 HIS   A CD2 
422  C CE1 . HIS   A 52  ? 0.5738 0.5279 0.4618 -0.0001 0.0101  -0.0892 338 HIS   A CE1 
423  N NE2 . HIS   A 52  ? 0.5683 0.5295 0.4021 0.0027  -0.0130 -0.0949 338 HIS   A NE2 
424  N N   . SER   A 53  ? 0.5243 0.3131 0.2001 -0.0178 -0.0096 -0.1127 339 SER   A N   
425  C CA  . SER   A 53  ? 0.5180 0.3166 0.2194 -0.0131 -0.0075 -0.1063 339 SER   A CA  
426  C C   . SER   A 53  ? 0.5104 0.3271 0.2164 -0.0125 0.0079  -0.1036 339 SER   A C   
427  O O   . SER   A 53  ? 0.5065 0.3103 0.2476 -0.0249 0.0331  -0.1060 339 SER   A O   
428  C CB  . SER   A 53  ? 0.5434 0.3475 0.2459 -0.0336 -0.0340 -0.1073 339 SER   A CB  
429  O OG  . SER   A 53  ? 0.5822 0.3740 0.2577 -0.0390 -0.0373 -0.0879 339 SER   A OG  
430  N N   . GLY   A 54  ? 0.5138 0.3341 0.1923 -0.0262 0.0161  -0.0924 340 GLY   A N   
431  C CA  . GLY   A 54  ? 0.5076 0.3398 0.1956 -0.0285 0.0095  -0.0849 340 GLY   A CA  
432  C C   . GLY   A 54  ? 0.4832 0.3293 0.1695 -0.0229 0.0346  -0.0818 340 GLY   A C   
433  O O   . GLY   A 54  ? 0.4949 0.3435 0.1913 -0.0242 0.0273  -0.0490 340 GLY   A O   
434  N N   . LYS   A 55  ? 0.4550 0.3066 0.1365 -0.0092 0.0503  -0.0809 341 LYS   A N   
435  C CA  . LYS   A 55  ? 0.4342 0.3145 0.1222 -0.0041 0.0250  -0.0569 341 LYS   A CA  
436  C C   . LYS   A 55  ? 0.4097 0.3107 0.0884 -0.0019 0.0037  -0.0552 341 LYS   A C   
437  O O   . LYS   A 55  ? 0.4241 0.3109 0.0867 0.0102  0.0070  -0.0498 341 LYS   A O   
438  C CB  . LYS   A 55  ? 0.4522 0.3553 0.1571 0.0062  0.0474  -0.0591 341 LYS   A CB  
439  C CG  . LYS   A 55  ? 0.4774 0.3837 0.1981 0.0171  0.0669  -0.0572 341 LYS   A CG  
440  C CD  . LYS   A 55  ? 0.4858 0.4286 0.2266 0.0126  0.0885  -0.0552 341 LYS   A CD  
441  C CE  . LYS   A 55  ? 0.5205 0.4592 0.2778 0.0205  0.0923  -0.0432 341 LYS   A CE  
442  N NZ  . LYS   A 55  ? 0.5313 0.5087 0.2880 0.0269  0.0954  -0.0421 341 LYS   A NZ  
443  N N   . HIS   A 56  ? 0.3943 0.2906 0.0788 0.0070  -0.0115 -0.0424 342 HIS   A N   
444  C CA  . HIS   A 56  ? 0.3791 0.2787 0.0872 0.0008  -0.0204 -0.0298 342 HIS   A CA  
445  C C   . HIS   A 56  ? 0.3713 0.2711 0.0786 0.0059  -0.0284 -0.0190 342 HIS   A C   
446  O O   . HIS   A 56  ? 0.3943 0.2809 0.1106 0.0220  -0.0556 -0.0287 342 HIS   A O   
447  C CB  . HIS   A 56  ? 0.3895 0.2814 0.0931 -0.0097 -0.0051 -0.0297 342 HIS   A CB  
448  C CG  . HIS   A 56  ? 0.4026 0.3054 0.1237 -0.0287 0.0053  -0.0413 342 HIS   A CG  
449  N ND1 . HIS   A 56  ? 0.4174 0.3332 0.1662 -0.0323 -0.0221 -0.0566 342 HIS   A ND1 
450  C CD2 . HIS   A 56  ? 0.4169 0.3203 0.1516 -0.0357 0.0104  -0.0530 342 HIS   A CD2 
451  C CE1 . HIS   A 56  ? 0.4257 0.3331 0.1794 -0.0372 -0.0044 -0.0505 342 HIS   A CE1 
452  N NE2 . HIS   A 56  ? 0.4302 0.3421 0.1761 -0.0341 -0.0144 -0.0516 342 HIS   A NE2 
453  N N   . TYR   A 57  ? 0.3469 0.2686 0.0752 0.0032  -0.0106 -0.0078 343 TYR   A N   
454  C CA  . TYR   A 57  ? 0.3198 0.2699 0.0818 0.0011  -0.0066 -0.0157 343 TYR   A CA  
455  C C   . TYR   A 57  ? 0.3038 0.2641 0.0806 0.0033  -0.0086 -0.0137 343 TYR   A C   
456  O O   . TYR   A 57  ? 0.3155 0.2628 0.0800 0.0102  -0.0214 -0.0275 343 TYR   A O   
457  C CB  . TYR   A 57  ? 0.3176 0.2849 0.1042 -0.0056 0.0077  -0.0293 343 TYR   A CB  
458  C CG  . TYR   A 57  ? 0.3192 0.3085 0.1141 -0.0215 0.0047  -0.0346 343 TYR   A CG  
459  C CD1 . TYR   A 57  ? 0.3091 0.3128 0.1079 -0.0299 0.0149  -0.0366 343 TYR   A CD1 
460  C CD2 . TYR   A 57  ? 0.3527 0.3106 0.1462 -0.0275 -0.0131 -0.0405 343 TYR   A CD2 
461  C CE1 . TYR   A 57  ? 0.3062 0.3269 0.0903 -0.0362 0.0233  -0.0447 343 TYR   A CE1 
462  C CE2 . TYR   A 57  ? 0.3387 0.3159 0.1566 -0.0319 -0.0079 -0.0407 343 TYR   A CE2 
463  C CZ  . TYR   A 57  ? 0.3119 0.3271 0.1206 -0.0399 0.0093  -0.0583 343 TYR   A CZ  
464  O OH  . TYR   A 57  ? 0.3280 0.3679 0.1470 -0.0457 0.0274  -0.1034 343 TYR   A OH  
465  N N   . TRP   A 58  ? 0.2985 0.2459 0.0814 -0.0010 -0.0130 -0.0063 344 TRP   A N   
466  C CA  . TRP   A 58  ? 0.2841 0.2460 0.0613 -0.0027 0.0039  -0.0081 344 TRP   A CA  
467  C C   . TRP   A 58  ? 0.2694 0.2510 0.0555 -0.0003 0.0074  0.0001  344 TRP   A C   
468  O O   . TRP   A 58  ? 0.2701 0.2666 0.0726 0.0171  0.0152  -0.0087 344 TRP   A O   
469  C CB  . TRP   A 58  ? 0.2903 0.2433 0.0646 -0.0024 0.0049  -0.0086 344 TRP   A CB  
470  C CG  . TRP   A 58  ? 0.2944 0.2393 0.0569 -0.0026 0.0163  -0.0161 344 TRP   A CG  
471  C CD1 . TRP   A 58  ? 0.2970 0.2343 0.0558 0.0023  0.0091  -0.0156 344 TRP   A CD1 
472  C CD2 . TRP   A 58  ? 0.3073 0.2409 0.0645 -0.0100 0.0128  -0.0108 344 TRP   A CD2 
473  N NE1 . TRP   A 58  ? 0.2924 0.2338 0.0359 -0.0038 0.0116  -0.0163 344 TRP   A NE1 
474  C CE2 . TRP   A 58  ? 0.3027 0.2319 0.0617 -0.0075 0.0161  -0.0143 344 TRP   A CE2 
475  C CE3 . TRP   A 58  ? 0.3346 0.2476 0.0727 -0.0121 0.0264  -0.0127 344 TRP   A CE3 
476  C CZ2 . TRP   A 58  ? 0.3250 0.2446 0.0754 -0.0155 0.0171  -0.0145 344 TRP   A CZ2 
477  C CZ3 . TRP   A 58  ? 0.3515 0.2444 0.0969 -0.0260 0.0216  -0.0285 344 TRP   A CZ3 
478  C CH2 . TRP   A 58  ? 0.3389 0.2490 0.0982 -0.0218 0.0137  -0.0200 344 TRP   A CH2 
479  N N   . GLU   A 59  ? 0.2549 0.2561 0.0613 -0.0063 0.0115  -0.0067 345 GLU   A N   
480  C CA  . GLU   A 59  ? 0.2471 0.2580 0.0636 -0.0067 0.0111  -0.0003 345 GLU   A CA  
481  C C   . GLU   A 59  ? 0.2278 0.2550 0.0570 0.0038  0.0089  0.0099  345 GLU   A C   
482  O O   . GLU   A 59  ? 0.2285 0.2717 0.0572 0.0042  0.0201  0.0142  345 GLU   A O   
483  C CB  . GLU   A 59  ? 0.2541 0.2780 0.0717 -0.0180 0.0265  -0.0011 345 GLU   A CB  
484  C CG  . GLU   A 59  ? 0.2637 0.3032 0.0815 -0.0294 0.0249  -0.0034 345 GLU   A CG  
485  C CD  . GLU   A 59  ? 0.2774 0.3173 0.0894 -0.0388 0.0162  0.0000  345 GLU   A CD  
486  O OE1 . GLU   A 59  ? 0.3009 0.3302 0.1025 -0.0499 0.0337  -0.0168 345 GLU   A OE1 
487  O OE2 . GLU   A 59  ? 0.3246 0.3563 0.0912 -0.0400 0.0070  -0.0123 345 GLU   A OE2 
488  N N   . VAL   A 60  ? 0.2252 0.2436 0.0550 0.0092  0.0098  0.0084  346 VAL   A N   
489  C CA  . VAL   A 60  ? 0.2299 0.2334 0.0543 0.0023  0.0081  0.0022  346 VAL   A CA  
490  C C   . VAL   A 60  ? 0.2318 0.2397 0.0599 -0.0058 0.0122  0.0020  346 VAL   A C   
491  O O   . VAL   A 60  ? 0.2377 0.2617 0.0851 0.0113  -0.0037 -0.0135 346 VAL   A O   
492  C CB  . VAL   A 60  ? 0.2429 0.2388 0.0647 -0.0039 0.0063  0.0052  346 VAL   A CB  
493  C CG1 . VAL   A 60  ? 0.2549 0.2490 0.0466 0.0008  0.0056  0.0072  346 VAL   A CG1 
494  C CG2 . VAL   A 60  ? 0.2465 0.2413 0.0695 -0.0180 0.0017  0.0122  346 VAL   A CG2 
495  N N   . ASP   A 61  ? 0.2469 0.2363 0.0384 -0.0114 0.0097  0.0022  347 ASP   A N   
496  C CA  . ASP   A 61  ? 0.2508 0.2271 0.0462 -0.0153 0.0178  0.0046  347 ASP   A CA  
497  C C   . ASP   A 61  ? 0.2374 0.2332 0.0438 -0.0182 0.0102  0.0033  347 ASP   A C   
498  O O   . ASP   A 61  ? 0.2361 0.2495 0.0516 -0.0121 0.0042  0.0041  347 ASP   A O   
499  C CB  . ASP   A 61  ? 0.2729 0.2288 0.0504 -0.0118 0.0208  0.0034  347 ASP   A CB  
500  C CG  . ASP   A 61  ? 0.3019 0.2387 0.0688 -0.0154 0.0241  -0.0047 347 ASP   A CG  
501  O OD1 . ASP   A 61  ? 0.3417 0.2644 0.0659 -0.0240 0.0193  -0.0074 347 ASP   A OD1 
502  O OD2 . ASP   A 61  ? 0.3273 0.2770 0.1295 -0.0378 0.0428  -0.0139 347 ASP   A OD2 
503  N N   . VAL   A 62  ? 0.2454 0.2403 0.0384 -0.0135 0.0033  0.0025  348 VAL   A N   
504  C CA  . VAL   A 62  ? 0.2751 0.2485 0.0394 -0.0143 0.0011  0.0056  348 VAL   A CA  
505  C C   . VAL   A 62  ? 0.2719 0.2450 0.0547 -0.0104 0.0119  -0.0033 348 VAL   A C   
506  O O   . VAL   A 62  ? 0.2816 0.2610 0.0580 0.0014  0.0006  -0.0125 348 VAL   A O   
507  C CB  . VAL   A 62  ? 0.3141 0.2432 0.0417 -0.0181 -0.0086 0.0141  348 VAL   A CB  
508  C CG1 . VAL   A 62  ? 0.3449 0.2493 0.0560 -0.0189 -0.0088 0.0189  348 VAL   A CG1 
509  C CG2 . VAL   A 62  ? 0.3250 0.2310 0.0415 -0.0099 -0.0059 0.0124  348 VAL   A CG2 
510  N N   . THR   A 63  ? 0.2672 0.2372 0.0506 -0.0113 0.0055  -0.0063 349 THR   A N   
511  C CA  . THR   A 63  ? 0.2670 0.2498 0.0654 -0.0154 0.0036  -0.0111 349 THR   A CA  
512  C C   . THR   A 63  ? 0.2660 0.2508 0.0707 -0.0168 0.0067  -0.0108 349 THR   A C   
513  O O   . THR   A 63  ? 0.2793 0.2765 0.0734 -0.0200 0.0127  -0.0228 349 THR   A O   
514  C CB  . THR   A 63  ? 0.2681 0.2454 0.0684 -0.0173 0.0091  -0.0160 349 THR   A CB  
515  O OG1 . THR   A 63  ? 0.2695 0.2752 0.0685 -0.0167 0.0206  -0.0136 349 THR   A OG1 
516  C CG2 . THR   A 63  ? 0.2762 0.2528 0.0803 -0.0218 0.0135  -0.0208 349 THR   A CG2 
517  N N   . GLY   A 64  ? 0.2607 0.2639 0.0575 -0.0110 0.0138  -0.0122 350 GLY   A N   
518  C CA  . GLY   A 64  ? 0.2745 0.2685 0.0631 -0.0165 0.0078  -0.0259 350 GLY   A CA  
519  C C   . GLY   A 64  ? 0.3004 0.2740 0.0699 -0.0174 0.0082  -0.0130 350 GLY   A C   
520  O O   . GLY   A 64  ? 0.3517 0.2895 0.0812 -0.0138 0.0265  -0.0173 350 GLY   A O   
521  N N   . LYS   A 65  ? 0.2947 0.2642 0.0504 -0.0239 0.0143  -0.0089 351 LYS   A N   
522  C CA  . LYS   A 65  ? 0.2818 0.2619 0.0428 -0.0164 0.0151  -0.0024 351 LYS   A CA  
523  C C   . LYS   A 65  ? 0.2828 0.2870 0.0535 -0.0180 0.0070  -0.0029 351 LYS   A C   
524  O O   . LYS   A 65  ? 0.2966 0.3084 0.0525 -0.0103 -0.0018 -0.0025 351 LYS   A O   
525  C CB  . LYS   A 65  ? 0.2729 0.2537 0.0390 -0.0173 0.0138  0.0044  351 LYS   A CB  
526  C CG  . LYS   A 65  ? 0.2687 0.2531 0.0571 -0.0084 0.0139  0.0055  351 LYS   A CG  
527  C CD  . LYS   A 65  ? 0.2723 0.2435 0.0602 -0.0050 0.0126  0.0024  351 LYS   A CD  
528  C CE  . LYS   A 65  ? 0.2712 0.2382 0.0645 -0.0024 0.0136  0.0081  351 LYS   A CE  
529  N NZ  . LYS   A 65  ? 0.2709 0.2349 0.0638 -0.0021 0.0148  0.0074  351 LYS   A NZ  
530  N N   . GLU   A 66  ? 0.2944 0.2806 0.0537 -0.0197 0.0072  0.0067  352 GLU   A N   
531  C CA  . GLU   A 66  ? 0.3033 0.2910 0.0605 -0.0179 -0.0066 0.0047  352 GLU   A CA  
532  C C   . GLU   A 66  ? 0.2857 0.2814 0.0521 -0.0087 -0.0070 0.0072  352 GLU   A C   
533  O O   . GLU   A 66  ? 0.2967 0.2687 0.0704 0.0016  -0.0185 0.0094  352 GLU   A O   
534  C CB  . GLU   A 66  ? 0.3457 0.3182 0.0651 -0.0164 -0.0035 -0.0024 352 GLU   A CB  
535  C CG  . GLU   A 66  ? 0.3750 0.3718 0.1249 -0.0197 -0.0063 0.0019  352 GLU   A CG  
536  C CD  . GLU   A 66  ? 0.4107 0.4256 0.1341 -0.0185 -0.0012 0.0254  352 GLU   A CD  
537  O OE1 . GLU   A 66  ? 0.4339 0.4427 0.1860 -0.0236 -0.0353 0.0280  352 GLU   A OE1 
538  O OE2 . GLU   A 66  ? 0.4120 0.4551 0.1588 0.0030  0.0162  0.0796  352 GLU   A OE2 
539  N N   . ALA   A 67  ? 0.2877 0.2620 0.0419 -0.0096 -0.0069 0.0086  353 ALA   A N   
540  C CA  . ALA   A 67  ? 0.2785 0.2642 0.0410 -0.0023 0.0041  0.0055  353 ALA   A CA  
541  C C   . ALA   A 67  ? 0.2570 0.2513 0.0484 0.0051  0.0045  0.0043  353 ALA   A C   
542  O O   . ALA   A 67  ? 0.2725 0.2520 0.0552 0.0117  0.0078  0.0016  353 ALA   A O   
543  C CB  . ALA   A 67  ? 0.2817 0.2665 0.0411 -0.0092 0.0028  0.0095  353 ALA   A CB  
544  N N   . TRP   A 68  ? 0.2368 0.2513 0.0392 0.0114  -0.0029 0.0023  354 TRP   A N   
545  C CA  . TRP   A 68  ? 0.2395 0.2556 0.0451 0.0068  -0.0068 0.0104  354 TRP   A CA  
546  C C   . TRP   A 68  ? 0.2215 0.2538 0.0481 0.0152  0.0046  0.0069  354 TRP   A C   
547  O O   . TRP   A 68  ? 0.2373 0.2523 0.0482 0.0292  0.0058  0.0047  354 TRP   A O   
548  C CB  . TRP   A 68  ? 0.2461 0.2630 0.0472 0.0072  -0.0093 0.0178  354 TRP   A CB  
549  C CG  . TRP   A 68  ? 0.2491 0.2702 0.0399 -0.0021 -0.0235 0.0248  354 TRP   A CG  
550  C CD1 . TRP   A 68  ? 0.2628 0.2734 0.0629 -0.0087 -0.0194 0.0257  354 TRP   A CD1 
551  C CD2 . TRP   A 68  ? 0.2445 0.2700 0.0431 -0.0047 -0.0103 0.0240  354 TRP   A CD2 
552  N NE1 . TRP   A 68  ? 0.2678 0.2755 0.0651 -0.0119 -0.0218 0.0201  354 TRP   A NE1 
553  C CE2 . TRP   A 68  ? 0.2484 0.2689 0.0358 -0.0016 -0.0174 0.0292  354 TRP   A CE2 
554  C CE3 . TRP   A 68  ? 0.2426 0.2698 0.0591 -0.0009 0.0033  0.0258  354 TRP   A CE3 
555  C CZ2 . TRP   A 68  ? 0.2454 0.2919 0.0459 -0.0039 -0.0083 0.0275  354 TRP   A CZ2 
556  C CZ3 . TRP   A 68  ? 0.2540 0.2769 0.0515 -0.0014 0.0011  0.0188  354 TRP   A CZ3 
557  C CH2 . TRP   A 68  ? 0.2400 0.2933 0.0377 0.0012  0.0075  0.0172  354 TRP   A CH2 
558  N N   . ASP   A 69  ? 0.2237 0.2459 0.0481 0.0181  0.0009  0.0084  355 ASP   A N   
559  C CA  . ASP   A 69  ? 0.2278 0.2445 0.0528 0.0167  0.0002  0.0118  355 ASP   A CA  
560  C C   . ASP   A 69  ? 0.2256 0.2455 0.0552 0.0182  -0.0046 0.0144  355 ASP   A C   
561  O O   . ASP   A 69  ? 0.2262 0.2353 0.0550 0.0191  0.0085  0.0166  355 ASP   A O   
562  C CB  . ASP   A 69  ? 0.2345 0.2550 0.0638 0.0193  0.0010  0.0201  355 ASP   A CB  
563  C CG  . ASP   A 69  ? 0.2481 0.2527 0.0796 0.0124  -0.0017 0.0151  355 ASP   A CG  
564  O OD1 . ASP   A 69  ? 0.2515 0.2576 0.0913 0.0107  -0.0199 0.0203  355 ASP   A OD1 
565  O OD2 . ASP   A 69  ? 0.2588 0.2774 0.0829 0.0287  0.0029  0.0220  355 ASP   A OD2 
566  N N   . LEU   A 70  ? 0.2228 0.2409 0.0519 0.0231  -0.0087 0.0180  356 LEU   A N   
567  C CA  . LEU   A 70  ? 0.2424 0.2471 0.0525 0.0105  -0.0045 0.0171  356 LEU   A CA  
568  C C   . LEU   A 70  ? 0.2427 0.2488 0.0515 0.0095  0.0121  0.0206  356 LEU   A C   
569  O O   . LEU   A 70  ? 0.2534 0.2655 0.0560 0.0202  0.0070  0.0059  356 LEU   A O   
570  C CB  . LEU   A 70  ? 0.2516 0.2464 0.0388 0.0038  -0.0123 0.0203  356 LEU   A CB  
571  C CG  . LEU   A 70  ? 0.2653 0.2485 0.0713 0.0014  0.0010  0.0226  356 LEU   A CG  
572  C CD1 . LEU   A 70  ? 0.2725 0.2572 0.0830 -0.0034 -0.0033 0.0338  356 LEU   A CD1 
573  C CD2 . LEU   A 70  ? 0.2689 0.2483 0.0909 -0.0001 0.0040  0.0206  356 LEU   A CD2 
574  N N   . GLY   A 71  ? 0.2439 0.2365 0.0745 0.0098  0.0060  0.0221  357 GLY   A N   
575  C CA  . GLY   A 71  ? 0.2558 0.2364 0.0783 0.0121  0.0170  0.0138  357 GLY   A CA  
576  C C   . GLY   A 71  ? 0.2671 0.2349 0.0637 0.0198  0.0116  0.0101  357 GLY   A C   
577  O O   . GLY   A 71  ? 0.2753 0.2088 0.0642 0.0240  0.0147  0.0084  357 GLY   A O   
578  N N   . VAL   A 72  ? 0.2891 0.2497 0.0796 0.0079  0.0060  0.0143  358 VAL   A N   
579  C CA  . VAL   A 72  ? 0.3147 0.2522 0.0802 0.0034  0.0005  0.0112  358 VAL   A CA  
580  C C   . VAL   A 72  ? 0.3144 0.2359 0.1035 0.0036  -0.0036 0.0191  358 VAL   A C   
581  O O   . VAL   A 72  ? 0.3319 0.2428 0.1192 0.0103  -0.0228 0.0178  358 VAL   A O   
582  C CB  . VAL   A 72  ? 0.3619 0.2941 0.0992 0.0068  0.0150  -0.0017 358 VAL   A CB  
583  C CG1 . VAL   A 72  ? 0.3982 0.3141 0.1622 -0.0037 0.0121  0.0156  358 VAL   A CG1 
584  C CG2 . VAL   A 72  ? 0.3911 0.2862 0.0720 0.0084  0.0090  -0.0086 358 VAL   A CG2 
585  N N   . CYS   A 73  ? 0.3138 0.2357 0.1047 0.0005  -0.0065 0.0106  359 CYS   A N   
586  C CA  . CYS   A 73  ? 0.3220 0.2360 0.1218 -0.0117 -0.0010 0.0079  359 CYS   A CA  
587  C C   . CYS   A 73  ? 0.3465 0.2317 0.1383 -0.0229 -0.0046 0.0078  359 CYS   A C   
588  O O   . CYS   A 73  ? 0.3616 0.2436 0.1366 -0.0334 -0.0176 -0.0028 359 CYS   A O   
589  C CB  . CYS   A 73  ? 0.3270 0.2447 0.1285 -0.0107 -0.0060 -0.0092 359 CYS   A CB  
590  S SG  . CYS   A 73  ? 0.3264 0.2531 0.1441 -0.0022 -0.0058 0.0081  359 CYS   A SG  
591  N N   . ARG   A 74  ? 0.3696 0.2352 0.1069 -0.0343 -0.0155 0.0096  360 ARG   A N   
592  C CA  . ARG   A 74  ? 0.3885 0.2462 0.1433 -0.0380 -0.0250 -0.0031 360 ARG   A CA  
593  C C   . ARG   A 74  ? 0.3826 0.2394 0.1369 -0.0378 -0.0214 -0.0086 360 ARG   A C   
594  O O   . ARG   A 74  ? 0.3853 0.2792 0.1162 -0.0215 -0.0205 -0.0005 360 ARG   A O   
595  C CB  . ARG   A 74  ? 0.4178 0.2517 0.1661 -0.0248 -0.0233 0.0080  360 ARG   A CB  
596  C CG  . ARG   A 74  ? 0.4469 0.2720 0.2139 -0.0099 -0.0191 0.0078  360 ARG   A CG  
597  C CD  . ARG   A 74  ? 0.4825 0.2810 0.2390 -0.0117 -0.0183 0.0184  360 ARG   A CD  
598  N NE  . ARG   A 74  ? 0.5286 0.3090 0.2833 0.0055  -0.0228 0.0261  360 ARG   A NE  
599  C CZ  . ARG   A 74  ? 0.5785 0.3328 0.3177 0.0258  -0.0239 0.0505  360 ARG   A CZ  
600  N NH1 . ARG   A 74  ? 0.6191 0.3201 0.3083 0.0236  -0.0320 0.0354  360 ARG   A NH1 
601  N NH2 . ARG   A 74  ? 0.5934 0.3600 0.3482 0.0379  -0.0221 0.0742  360 ARG   A NH2 
602  N N   . ASP   A 75  ? 0.3951 0.2762 0.1407 -0.0370 -0.0267 0.0035  361 ASP   A N   
603  C CA  . ASP   A 75  ? 0.3845 0.2774 0.1730 -0.0489 -0.0265 0.0034  361 ASP   A CA  
604  C C   . ASP   A 75  ? 0.3748 0.2839 0.1709 -0.0516 -0.0224 -0.0047 361 ASP   A C   
605  O O   . ASP   A 75  ? 0.3774 0.3008 0.2329 -0.0391 -0.0287 -0.0049 361 ASP   A O   
606  C CB  . ASP   A 75  ? 0.4023 0.2819 0.2094 -0.0571 -0.0351 -0.0191 361 ASP   A CB  
607  C CG  . ASP   A 75  ? 0.4049 0.2889 0.2326 -0.0553 -0.0363 -0.0185 361 ASP   A CG  
608  O OD1 . ASP   A 75  ? 0.4139 0.3064 0.2519 -0.0415 -0.0380 -0.0036 361 ASP   A OD1 
609  O OD2 . ASP   A 75  ? 0.4223 0.3382 0.3182 -0.0799 -0.0416 -0.0159 361 ASP   A OD2 
610  N N   . SER   A 76  ? 0.3953 0.3024 0.1681 -0.0432 -0.0083 0.0160  362 SER   A N   
611  C CA  . SER   A 76  ? 0.4123 0.3023 0.1941 -0.0510 -0.0035 0.0263  362 SER   A CA  
612  C C   . SER   A 76  ? 0.4231 0.2952 0.1862 -0.0627 -0.0015 0.0306  362 SER   A C   
613  O O   . SER   A 76  ? 0.4843 0.3237 0.1871 -0.0793 -0.0065 0.0455  362 SER   A O   
614  C CB  . SER   A 76  ? 0.4291 0.3068 0.2285 -0.0485 -0.0035 0.0269  362 SER   A CB  
615  O OG  . SER   A 76  ? 0.4439 0.3216 0.2815 -0.0253 -0.0048 0.0338  362 SER   A OG  
616  N N   . VAL   A 77  ? 0.4201 0.2949 0.1547 -0.0608 0.0065  0.0361  363 VAL   A N   
617  C CA  . VAL   A 77  ? 0.4110 0.3033 0.1470 -0.0504 0.0000  0.0507  363 VAL   A CA  
618  C C   . VAL   A 77  ? 0.4251 0.3193 0.1452 -0.0507 0.0009  0.0428  363 VAL   A C   
619  O O   . VAL   A 77  ? 0.4272 0.3337 0.1237 -0.0553 0.0154  0.0423  363 VAL   A O   
620  C CB  . VAL   A 77  ? 0.3891 0.3135 0.1321 -0.0433 -0.0010 0.0413  363 VAL   A CB  
621  C CG1 . VAL   A 77  ? 0.3881 0.3155 0.1452 -0.0385 -0.0055 0.0354  363 VAL   A CG1 
622  C CG2 . VAL   A 77  ? 0.3762 0.3107 0.1117 -0.0446 0.0020  0.0438  363 VAL   A CG2 
623  N N   . ARG   A 78  ? 0.4155 0.3242 0.1414 -0.0436 0.0007  0.0483  364 ARG   A N   
624  C CA  . ARG   A 78  ? 0.4223 0.3365 0.1875 -0.0302 0.0030  0.0516  364 ARG   A CA  
625  C C   . ARG   A 78  ? 0.3866 0.3289 0.1318 -0.0281 0.0041  0.0575  364 ARG   A C   
626  O O   . ARG   A 78  ? 0.4112 0.3332 0.1917 -0.0296 -0.0280 0.0339  364 ARG   A O   
627  C CB  . ARG   A 78  ? 0.4502 0.3481 0.1873 -0.0252 0.0010  0.0469  364 ARG   A CB  
628  C CG  . ARG   A 78  ? 0.4700 0.3530 0.2168 -0.0150 -0.0013 0.0535  364 ARG   A CG  
629  C CD  . ARG   A 78  ? 0.4540 0.3512 0.2105 -0.0151 -0.0039 0.0479  364 ARG   A CD  
630  N NE  . ARG   A 78  ? 0.4526 0.3357 0.1555 -0.0192 -0.0280 0.0413  364 ARG   A NE  
631  C CZ  . ARG   A 78  ? 0.4394 0.3262 0.1493 -0.0212 -0.0064 0.0308  364 ARG   A CZ  
632  N NH1 . ARG   A 78  ? 0.4453 0.3140 0.1239 -0.0102 0.0014  0.0277  364 ARG   A NH1 
633  N NH2 . ARG   A 78  ? 0.4322 0.3610 0.1488 -0.0138 -0.0186 0.0106  364 ARG   A NH2 
634  N N   . ARG   A 79  ? 0.3728 0.3124 0.1212 -0.0343 -0.0008 0.0668  365 ARG   A N   
635  C CA  . ARG   A 79  ? 0.3465 0.2988 0.1149 -0.0405 0.0023  0.0680  365 ARG   A CA  
636  C C   . ARG   A 79  ? 0.3383 0.2941 0.1198 -0.0373 0.0002  0.0600  365 ARG   A C   
637  O O   . ARG   A 79  ? 0.3359 0.2935 0.1088 -0.0419 0.0274  0.0584  365 ARG   A O   
638  C CB  . ARG   A 79  ? 0.3511 0.3054 0.1302 -0.0445 -0.0101 0.0616  365 ARG   A CB  
639  C CG  . ARG   A 79  ? 0.3380 0.2978 0.1204 -0.0540 -0.0195 0.0527  365 ARG   A CG  
640  C CD  . ARG   A 79  ? 0.3411 0.2969 0.1258 -0.0561 -0.0126 0.0381  365 ARG   A CD  
641  N NE  . ARG   A 79  ? 0.3408 0.3039 0.1544 -0.0497 -0.0067 0.0195  365 ARG   A NE  
642  C CZ  . ARG   A 79  ? 0.3511 0.3158 0.1438 -0.0550 -0.0077 0.0062  365 ARG   A CZ  
643  N NH1 . ARG   A 79  ? 0.3534 0.3284 0.1251 -0.0471 -0.0110 0.0011  365 ARG   A NH1 
644  N NH2 . ARG   A 79  ? 0.3581 0.3066 0.1472 -0.0561 -0.0038 -0.0020 365 ARG   A NH2 
645  N N   . LYS   A 80  ? 0.3457 0.3084 0.1373 -0.0396 0.0175  0.0578  366 LYS   A N   
646  C CA  . LYS   A 80  ? 0.3417 0.3366 0.1266 -0.0371 0.0073  0.0637  366 LYS   A CA  
647  C C   . LYS   A 80  ? 0.3501 0.3222 0.1201 -0.0270 0.0188  0.0738  366 LYS   A C   
648  O O   . LYS   A 80  ? 0.4063 0.3381 0.1384 -0.0129 -0.0074 0.0512  366 LYS   A O   
649  C CB  . LYS   A 80  ? 0.3458 0.3486 0.1373 -0.0449 0.0089  0.0750  366 LYS   A CB  
650  C CG  . LYS   A 80  ? 0.3458 0.3892 0.1307 -0.0553 0.0026  0.0774  366 LYS   A CG  
651  C CD  . LYS   A 80  ? 0.3295 0.4030 0.1599 -0.0597 0.0028  0.0780  366 LYS   A CD  
652  C CE  . LYS   A 80  ? 0.3191 0.4363 0.1727 -0.0634 0.0035  0.0938  366 LYS   A CE  
653  N NZ  . LYS   A 80  ? 0.3153 0.4497 0.1894 -0.0686 0.0186  0.1026  366 LYS   A NZ  
654  N N   . GLY   A 81  ? 0.3497 0.3135 0.1359 -0.0216 0.0231  0.0804  367 GLY   A N   
655  C CA  . GLY   A 81  ? 0.3430 0.3123 0.1397 -0.0068 0.0247  0.0827  367 GLY   A CA  
656  C C   . GLY   A 81  ? 0.3406 0.2988 0.1040 -0.0018 0.0406  0.0847  367 GLY   A C   
657  O O   . GLY   A 81  ? 0.3300 0.3024 0.1018 0.0079  0.0338  0.0953  367 GLY   A O   
658  N N   . HIS   A 82  ? 0.3504 0.3108 0.0897 -0.0015 0.0290  0.0756  368 HIS   A N   
659  C CA  . HIS   A 82  ? 0.3512 0.3115 0.0960 0.0010  0.0281  0.0646  368 HIS   A CA  
660  C C   . HIS   A 82  ? 0.3511 0.2945 0.0986 -0.0024 0.0369  0.0649  368 HIS   A C   
661  O O   . HIS   A 82  ? 0.3750 0.2773 0.1454 0.0149  0.0437  0.0750  368 HIS   A O   
662  C CB  . HIS   A 82  ? 0.3357 0.3278 0.0967 -0.0010 0.0310  0.0468  368 HIS   A CB  
663  C CG  . HIS   A 82  ? 0.3352 0.3512 0.1148 0.0024  0.0211  0.0352  368 HIS   A CG  
664  N ND1 . HIS   A 82  ? 0.3412 0.3609 0.1032 -0.0015 0.0251  0.0385  368 HIS   A ND1 
665  C CD2 . HIS   A 82  ? 0.3263 0.3610 0.1228 -0.0069 0.0483  0.0309  368 HIS   A CD2 
666  C CE1 . HIS   A 82  ? 0.3370 0.3616 0.1174 -0.0050 0.0285  0.0264  368 HIS   A CE1 
667  N NE2 . HIS   A 82  ? 0.3309 0.3677 0.1286 -0.0024 0.0267  0.0157  368 HIS   A NE2 
668  N N   . PHE   A 83  ? 0.3380 0.2891 0.0791 0.0087  0.0197  0.0582  369 PHE   A N   
669  C CA  . PHE   A 83  ? 0.3408 0.3003 0.0890 0.0127  0.0150  0.0454  369 PHE   A CA  
670  C C   . PHE   A 83  ? 0.3516 0.2997 0.0876 0.0053  0.0228  0.0507  369 PHE   A C   
671  O O   . PHE   A 83  ? 0.3513 0.3068 0.1328 0.0098  0.0259  0.0475  369 PHE   A O   
672  C CB  . PHE   A 83  ? 0.3406 0.3049 0.0990 0.0188  0.0033  0.0433  369 PHE   A CB  
673  C CG  . PHE   A 83  ? 0.3284 0.3244 0.0897 0.0270  0.0103  0.0517  369 PHE   A CG  
674  C CD1 . PHE   A 83  ? 0.3219 0.3303 0.1130 0.0321  0.0197  0.0475  369 PHE   A CD1 
675  C CD2 . PHE   A 83  ? 0.3212 0.3262 0.1057 0.0323  0.0116  0.0574  369 PHE   A CD2 
676  C CE1 . PHE   A 83  ? 0.3118 0.3470 0.0937 0.0352  0.0206  0.0607  369 PHE   A CE1 
677  C CE2 . PHE   A 83  ? 0.2987 0.3286 0.1116 0.0355  0.0021  0.0549  369 PHE   A CE2 
678  C CZ  . PHE   A 83  ? 0.3172 0.3339 0.0886 0.0445  0.0031  0.0696  369 PHE   A CZ  
679  N N   . LEU   A 84  ? 0.3602 0.2947 0.1042 0.0083  0.0249  0.0572  370 LEU   A N   
680  C CA  . LEU   A 84  ? 0.3612 0.3145 0.0972 0.0019  0.0176  0.0522  370 LEU   A CA  
681  C C   . LEU   A 84  ? 0.3534 0.3227 0.0953 0.0139  0.0044  0.0610  370 LEU   A C   
682  O O   . LEU   A 84  ? 0.3852 0.3477 0.1042 -0.0080 0.0121  0.0583  370 LEU   A O   
683  C CB  . LEU   A 84  ? 0.3829 0.3187 0.0975 -0.0037 0.0120  0.0542  370 LEU   A CB  
684  C CG  . LEU   A 84  ? 0.4083 0.3279 0.0992 -0.0210 0.0196  0.0492  370 LEU   A CG  
685  C CD1 . LEU   A 84  ? 0.4070 0.3400 0.1168 -0.0224 0.0020  0.0630  370 LEU   A CD1 
686  C CD2 . LEU   A 84  ? 0.4327 0.3401 0.1048 -0.0414 0.0232  0.0384  370 LEU   A CD2 
687  N N   . LEU   A 85  ? 0.3487 0.3612 0.0875 0.0161  0.0039  0.0711  371 LEU   A N   
688  C CA  . LEU   A 85  ? 0.3406 0.3490 0.0900 0.0384  0.0174  0.0589  371 LEU   A CA  
689  C C   . LEU   A 85  ? 0.3622 0.3657 0.1306 0.0677  0.0065  0.0872  371 LEU   A C   
690  O O   . LEU   A 85  ? 0.3675 0.4221 0.2632 0.0942  0.0353  0.1011  371 LEU   A O   
691  C CB  . LEU   A 85  ? 0.3167 0.3353 0.0946 0.0373  0.0046  0.0643  371 LEU   A CB  
692  C CG  . LEU   A 85  ? 0.3294 0.3178 0.1079 0.0313  0.0073  0.0601  371 LEU   A CG  
693  C CD1 . LEU   A 85  ? 0.3301 0.3116 0.1144 0.0296  0.0003  0.0595  371 LEU   A CD1 
694  C CD2 . LEU   A 85  ? 0.3383 0.3265 0.1316 0.0272  0.0128  0.0408  371 LEU   A CD2 
695  N N   . SER   A 86  ? 0.4189 0.3905 0.1544 0.0731  -0.0065 0.0152  372 SER   A N   
696  C CA  . SER   A 86  ? 0.4725 0.3682 0.1672 0.0821  -0.0124 0.0362  372 SER   A CA  
697  C C   . SER   A 86  ? 0.4733 0.3553 0.1592 0.0828  -0.0201 0.0460  372 SER   A C   
698  O O   . SER   A 86  ? 0.4465 0.3256 0.1529 0.0951  0.0040  0.0493  372 SER   A O   
699  C CB  . SER   A 86  ? 0.5050 0.3964 0.1654 0.0604  0.0013  0.0553  372 SER   A CB  
700  O OG  . SER   A 86  ? 0.6101 0.4189 0.2112 0.0361  0.0045  0.0710  372 SER   A OG  
701  N N   A SER   A 87  ? 0.4828 0.3516 0.1926 0.0843  -0.0163 0.0582  373 SER   A N   
702  N N   B SER   A 87  ? 0.4859 0.3422 0.1668 0.0826  -0.0169 0.0519  373 SER   A N   
703  C CA  A SER   A 87  ? 0.5147 0.3554 0.2430 0.0678  -0.0308 0.0389  373 SER   A CA  
704  C CA  B SER   A 87  ? 0.5150 0.3415 0.2054 0.0694  -0.0260 0.0315  373 SER   A CA  
705  C C   A SER   A 87  ? 0.5411 0.3494 0.2871 0.0640  -0.0331 0.0499  373 SER   A C   
706  C C   B SER   A 87  ? 0.5412 0.3422 0.2733 0.0636  -0.0307 0.0420  373 SER   A C   
707  O O   A SER   A 87  ? 0.5765 0.3577 0.3537 0.0568  -0.0585 0.0212  373 SER   A O   
708  O O   B SER   A 87  ? 0.5787 0.3515 0.3414 0.0560  -0.0588 0.0159  373 SER   A O   
709  C CB  A SER   A 87  ? 0.5125 0.3663 0.2669 0.0659  -0.0269 0.0430  373 SER   A CB  
710  C CB  B SER   A 87  ? 0.5133 0.3356 0.1915 0.0676  -0.0215 0.0327  373 SER   A CB  
711  O OG  A SER   A 87  ? 0.5200 0.3627 0.2875 0.0680  -0.0438 0.0567  373 SER   A OG  
712  O OG  B SER   A 87  ? 0.5176 0.3235 0.1533 0.0646  -0.0230 0.0220  373 SER   A OG  
713  N N   . LYS   A 88  ? 0.5590 0.3566 0.3112 0.0534  -0.0370 0.0668  374 LYS   A N   
714  C CA  . LYS   A 88  ? 0.5873 0.3808 0.3992 0.0262  -0.0216 0.0941  374 LYS   A CA  
715  C C   . LYS   A 88  ? 0.6008 0.3673 0.4481 -0.0074 -0.0196 0.1152  374 LYS   A C   
716  O O   . LYS   A 88  ? 0.6657 0.3384 0.5759 -0.0514 -0.0006 0.1048  374 LYS   A O   
717  C CB  . LYS   A 88  ? 0.6003 0.4280 0.4327 0.0337  -0.0196 0.1017  374 LYS   A CB  
718  C CG  . LYS   A 88  ? 0.6107 0.4700 0.4914 0.0341  -0.0165 0.0856  374 LYS   A CG  
719  C CD  . LYS   A 88  ? 0.6292 0.4952 0.5097 0.0266  -0.0190 0.0704  374 LYS   A CD  
720  C CE  . LYS   A 88  ? 0.6321 0.5122 0.5251 0.0238  -0.0338 0.0796  374 LYS   A CE  
721  N NZ  . LYS   A 88  ? 0.6588 0.5251 0.5371 0.0257  -0.0275 0.0653  374 LYS   A NZ  
722  N N   . SER   A 89  ? 0.6044 0.3479 0.4329 -0.0147 -0.0112 0.1807  375 SER   A N   
723  C CA  . SER   A 89  ? 0.5974 0.3794 0.3636 -0.0196 -0.0125 0.2071  375 SER   A CA  
724  C C   . SER   A 89  ? 0.5377 0.3529 0.3424 -0.0156 -0.0292 0.1712  375 SER   A C   
725  O O   . SER   A 89  ? 0.5429 0.4285 0.3657 -0.0417 -0.0732 0.1812  375 SER   A O   
726  C CB  . SER   A 89  ? 0.6354 0.3988 0.3922 -0.0156 -0.0093 0.2190  375 SER   A CB  
727  O OG  . SER   A 89  ? 0.7240 0.4526 0.4462 -0.0126 -0.0210 0.2704  375 SER   A OG  
728  N N   . GLY   A 90  ? 0.4791 0.2979 0.2530 0.0005  -0.0609 0.1078  376 GLY   A N   
729  C CA  . GLY   A 90  ? 0.4179 0.2865 0.2342 0.0009  -0.0312 0.0851  376 GLY   A CA  
730  C C   . GLY   A 90  ? 0.3695 0.2607 0.1735 0.0124  -0.0298 0.0514  376 GLY   A C   
731  O O   . GLY   A 90  ? 0.3774 0.2706 0.1467 0.0133  -0.0464 0.0223  376 GLY   A O   
732  N N   . PHE   A 91  ? 0.3505 0.2575 0.1219 0.0156  -0.0113 0.0533  377 PHE   A N   
733  C CA  . PHE   A 91  ? 0.3350 0.2593 0.1040 0.0256  0.0020  0.0289  377 PHE   A CA  
734  C C   . PHE   A 91  ? 0.3269 0.2532 0.1262 0.0282  -0.0065 0.0286  377 PHE   A C   
735  O O   . PHE   A 91  ? 0.3335 0.2640 0.1227 0.0365  -0.0085 0.0344  377 PHE   A O   
736  C CB  . PHE   A 91  ? 0.3376 0.2637 0.0821 0.0173  0.0066  0.0336  377 PHE   A CB  
737  C CG  . PHE   A 91  ? 0.3311 0.2814 0.0744 0.0111  -0.0030 0.0387  377 PHE   A CG  
738  C CD1 . PHE   A 91  ? 0.3351 0.2739 0.0763 0.0105  0.0174  0.0297  377 PHE   A CD1 
739  C CD2 . PHE   A 91  ? 0.3329 0.2796 0.1016 0.0074  0.0142  0.0347  377 PHE   A CD2 
740  C CE1 . PHE   A 91  ? 0.3322 0.2879 0.0963 0.0111  -0.0015 0.0299  377 PHE   A CE1 
741  C CE2 . PHE   A 91  ? 0.3360 0.2876 0.0949 0.0078  0.0091  0.0264  377 PHE   A CE2 
742  C CZ  . PHE   A 91  ? 0.3311 0.3005 0.0940 0.0130  0.0050  0.0255  377 PHE   A CZ  
743  N N   . TRP   A 92  ? 0.3171 0.2548 0.0997 0.0306  0.0078  0.0070  378 TRP   A N   
744  C CA  . TRP   A 92  ? 0.3185 0.2585 0.1070 0.0391  0.0113  0.0115  378 TRP   A CA  
745  C C   . TRP   A 92  ? 0.3082 0.2547 0.0901 0.0430  0.0113  0.0195  378 TRP   A C   
746  O O   . TRP   A 92  ? 0.3077 0.2468 0.0823 0.0336  0.0046  0.0221  378 TRP   A O   
747  C CB  . TRP   A 92  ? 0.3157 0.2578 0.1112 0.0450  0.0082  0.0109  378 TRP   A CB  
748  C CG  . TRP   A 92  ? 0.3435 0.2644 0.1484 0.0414  0.0123  0.0102  378 TRP   A CG  
749  C CD1 . TRP   A 92  ? 0.3515 0.2747 0.1638 0.0511  0.0056  -0.0013 378 TRP   A CD1 
750  C CD2 . TRP   A 92  ? 0.3591 0.2631 0.1671 0.0364  0.0027  0.0037  378 TRP   A CD2 
751  N NE1 . TRP   A 92  ? 0.3762 0.2660 0.1915 0.0503  0.0012  0.0082  378 TRP   A NE1 
752  C CE2 . TRP   A 92  ? 0.3689 0.2676 0.1867 0.0402  0.0069  -0.0028 378 TRP   A CE2 
753  C CE3 . TRP   A 92  ? 0.3613 0.2559 0.2098 0.0378  0.0060  0.0056  378 TRP   A CE3 
754  C CZ2 . TRP   A 92  ? 0.3811 0.2438 0.2059 0.0304  0.0106  0.0043  378 TRP   A CZ2 
755  C CZ3 . TRP   A 92  ? 0.3725 0.2647 0.2204 0.0361  0.0078  -0.0012 378 TRP   A CZ3 
756  C CH2 . TRP   A 92  ? 0.3814 0.2611 0.2198 0.0290  0.0136  0.0019  378 TRP   A CH2 
757  N N   . THR   A 93  ? 0.2881 0.2616 0.0773 0.0400  0.0121  0.0253  379 THR   A N   
758  C CA  . THR   A 93  ? 0.2808 0.2514 0.0785 0.0358  0.0173  0.0300  379 THR   A CA  
759  C C   . THR   A 93  ? 0.2671 0.2526 0.0738 0.0436  0.0176  0.0263  379 THR   A C   
760  O O   . THR   A 93  ? 0.2775 0.2618 0.0987 0.0605  0.0114  0.0178  379 THR   A O   
761  C CB  . THR   A 93  ? 0.2765 0.2554 0.0617 0.0274  0.0200  0.0275  379 THR   A CB  
762  O OG1 . THR   A 93  ? 0.2886 0.2794 0.0680 0.0347  0.0116  0.0295  379 THR   A OG1 
763  C CG2 . THR   A 93  ? 0.2786 0.2568 0.0650 0.0239  0.0293  0.0353  379 THR   A CG2 
764  N N   . ILE   A 94  ? 0.2587 0.2537 0.0649 0.0350  0.0072  0.0203  380 ILE   A N   
765  C CA  . ILE   A 94  ? 0.2579 0.2666 0.0675 0.0311  0.0081  0.0166  380 ILE   A CA  
766  C C   . ILE   A 94  ? 0.2538 0.2657 0.0711 0.0330  0.0059  0.0176  380 ILE   A C   
767  O O   . ILE   A 94  ? 0.2569 0.2583 0.0505 0.0312  0.0084  0.0118  380 ILE   A O   
768  C CB  . ILE   A 94  ? 0.2580 0.2839 0.0786 0.0291  0.0105  0.0063  380 ILE   A CB  
769  C CG1 . ILE   A 94  ? 0.2636 0.2774 0.0834 0.0218  0.0113  0.0003  380 ILE   A CG1 
770  C CG2 . ILE   A 94  ? 0.2697 0.2951 0.0807 0.0395  0.0104  0.0147  380 ILE   A CG2 
771  C CD1 . ILE   A 94  ? 0.2738 0.2887 0.0924 0.0135  0.0156  -0.0078 380 ILE   A CD1 
772  N N   . TRP   A 95  ? 0.2510 0.2631 0.0673 0.0423  -0.0001 0.0161  381 TRP   A N   
773  C CA  . TRP   A 95  ? 0.2582 0.2680 0.0632 0.0307  0.0015  0.0109  381 TRP   A CA  
774  C C   . TRP   A 95  ? 0.2538 0.2711 0.0539 0.0314  -0.0069 0.0151  381 TRP   A C   
775  O O   . TRP   A 95  ? 0.2509 0.2751 0.0778 0.0324  -0.0087 0.0150  381 TRP   A O   
776  C CB  . TRP   A 95  ? 0.2609 0.2723 0.0622 0.0304  0.0041  0.0157  381 TRP   A CB  
777  C CG  . TRP   A 95  ? 0.2632 0.2920 0.0541 0.0231  0.0096  0.0193  381 TRP   A CG  
778  C CD1 . TRP   A 95  ? 0.2657 0.2972 0.0658 0.0175  0.0066  0.0198  381 TRP   A CD1 
779  C CD2 . TRP   A 95  ? 0.2584 0.2921 0.0671 0.0198  0.0061  0.0283  381 TRP   A CD2 
780  N NE1 . TRP   A 95  ? 0.2712 0.3032 0.0638 0.0130  0.0105  0.0260  381 TRP   A NE1 
781  C CE2 . TRP   A 95  ? 0.2695 0.2945 0.0629 0.0173  0.0150  0.0318  381 TRP   A CE2 
782  C CE3 . TRP   A 95  ? 0.2621 0.2842 0.0904 0.0208  0.0082  0.0223  381 TRP   A CE3 
783  C CZ2 . TRP   A 95  ? 0.2784 0.2979 0.1110 0.0206  0.0135  0.0274  381 TRP   A CZ2 
784  C CZ3 . TRP   A 95  ? 0.2699 0.2919 0.1255 0.0233  -0.0009 0.0208  381 TRP   A CZ3 
785  C CH2 . TRP   A 95  ? 0.2805 0.2896 0.1138 0.0211  0.0132  0.0302  381 TRP   A CH2 
786  N N   . LEU   A 96  ? 0.2508 0.2734 0.0767 0.0238  -0.0125 -0.0011 382 LEU   A N   
787  C CA  . LEU   A 96  ? 0.2634 0.2789 0.0611 0.0159  0.0020  -0.0021 382 LEU   A CA  
788  C C   . LEU   A 96  ? 0.2603 0.2811 0.0658 0.0137  0.0054  -0.0093 382 LEU   A C   
789  O O   . LEU   A 96  ? 0.2660 0.2758 0.0620 0.0060  -0.0017 -0.0110 382 LEU   A O   
790  C CB  . LEU   A 96  ? 0.2779 0.2765 0.0671 0.0144  -0.0020 0.0011  382 LEU   A CB  
791  C CG  . LEU   A 96  ? 0.2804 0.2807 0.0606 0.0133  -0.0032 0.0008  382 LEU   A CG  
792  C CD1 . LEU   A 96  ? 0.2789 0.3000 0.0553 0.0072  -0.0066 -0.0043 382 LEU   A CD1 
793  C CD2 . LEU   A 96  ? 0.2924 0.2755 0.0686 0.0196  0.0016  -0.0008 382 LEU   A CD2 
794  N N   . TRP   A 97  ? 0.2894 0.3267 0.0777 0.0109  -0.0108 -0.0024 383 TRP   A N   
795  C CA  . TRP   A 97  ? 0.3599 0.3838 0.0915 0.0007  0.0074  0.0039  383 TRP   A CA  
796  C C   . TRP   A 97  ? 0.4174 0.4133 0.1014 -0.0017 0.0022  -0.0320 383 TRP   A C   
797  O O   . TRP   A 97  ? 0.4436 0.4769 0.1967 -0.0193 0.0104  -0.0614 383 TRP   A O   
798  C CB  . TRP   A 97  ? 0.4232 0.4178 0.1387 -0.0256 0.0101  0.0257  383 TRP   A CB  
799  C CG  . TRP   A 97  ? 0.4716 0.4828 0.1487 -0.0366 0.0239  0.0379  383 TRP   A CG  
800  C CD1 . TRP   A 97  ? 0.5008 0.5086 0.1666 -0.0538 0.0045  0.0561  383 TRP   A CD1 
801  C CD2 . TRP   A 97  ? 0.5007 0.5443 0.1674 -0.0734 0.0390  0.0547  383 TRP   A CD2 
802  N NE1 . TRP   A 97  ? 0.5142 0.5497 0.2070 -0.0708 0.0305  0.0336  383 TRP   A NE1 
803  C CE2 . TRP   A 97  ? 0.5327 0.5603 0.1555 -0.0658 0.0298  0.0638  383 TRP   A CE2 
804  C CE3 . TRP   A 97  ? 0.5425 0.5876 0.1504 -0.0928 0.0397  0.0278  383 TRP   A CE3 
805  C CZ2 . TRP   A 97  ? 0.5331 0.5943 0.2301 -0.0796 0.0224  0.0459  383 TRP   A CZ2 
806  C CZ3 . TRP   A 97  ? 0.5532 0.6200 0.1881 -0.0880 0.0433  0.0218  383 TRP   A CZ3 
807  C CH2 . TRP   A 97  ? 0.5591 0.6004 0.1934 -0.0873 0.0480  0.0271  383 TRP   A CH2 
808  N N   . ASN   A 98  ? 0.4770 0.4568 0.2155 0.0277  -0.0063 -0.0252 384 ASN   A N   
809  C CA  . ASN   A 98  ? 0.5503 0.5132 0.2865 0.0097  -0.0240 -0.0549 384 ASN   A CA  
810  C C   . ASN   A 98  ? 0.5768 0.5757 0.3702 -0.0226 -0.0492 -0.0596 384 ASN   A C   
811  O O   . ASN   A 98  ? 0.6397 0.5862 0.3283 -0.0460 -0.0861 -0.1331 384 ASN   A O   
812  C CB  . ASN   A 98  ? 0.5993 0.5624 0.2684 0.0023  -0.0413 -0.0455 384 ASN   A CB  
813  C CG  . ASN   A 98  ? 0.6681 0.6178 0.2958 0.0286  -0.0300 -0.0537 384 ASN   A CG  
814  O OD1 . ASN   A 98  ? 0.7357 0.6725 0.3686 0.0614  -0.0117 -0.0679 384 ASN   A OD1 
815  N ND2 . ASN   A 98  ? 0.6878 0.6688 0.3531 0.0438  -0.0469 -0.0253 384 ASN   A ND2 
816  N N   . LYS   A 99  ? 0.6062 0.5976 0.3856 -0.0382 -0.0660 -0.0730 385 LYS   A N   
817  C CA  . LYS   A 99  ? 0.6141 0.5763 0.4420 -0.0525 -0.0551 -0.0818 385 LYS   A CA  
818  C C   . LYS   A 99  ? 0.6284 0.5776 0.4394 -0.0280 -0.0628 -0.0396 385 LYS   A C   
819  O O   . LYS   A 99  ? 0.6943 0.6346 0.4440 -0.0473 -0.0490 -0.0232 385 LYS   A O   
820  C CB  . LYS   A 99  ? 0.6336 0.6067 0.4531 -0.0721 -0.0898 -0.1023 385 LYS   A CB  
821  N N   . GLN   A 100 ? 0.5620 0.5818 0.4033 0.0002  -0.0882 -0.0387 386 GLN   A N   
822  C CA  . GLN   A 100 ? 0.5353 0.5511 0.3532 -0.0026 -0.0981 -0.0173 386 GLN   A CA  
823  C C   . GLN   A 100 ? 0.4605 0.5223 0.2645 -0.0238 -0.0979 -0.0198 386 GLN   A C   
824  O O   . GLN   A 100 ? 0.4512 0.5208 0.2966 -0.0286 -0.1201 -0.0105 386 GLN   A O   
825  C CB  . GLN   A 100 ? 0.5241 0.5708 0.4302 -0.0158 -0.0800 -0.0472 386 GLN   A CB  
826  N N   . LYS   A 101 ? 0.4119 0.4760 0.1609 -0.0052 -0.0949 -0.0189 387 LYS   A N   
827  C CA  . LYS   A 101 ? 0.3550 0.4553 0.1320 -0.0048 -0.0700 -0.0036 387 LYS   A CA  
828  C C   . LYS   A 101 ? 0.2966 0.3930 0.0817 0.0189  -0.0376 0.0125  387 LYS   A C   
829  O O   . LYS   A 101 ? 0.3014 0.3968 0.0720 0.0125  -0.0200 0.0141  387 LYS   A O   
830  C CB  . LYS   A 101 ? 0.3917 0.4917 0.1344 0.0073  -0.0688 0.0129  387 LYS   A CB  
831  C CG  . LYS   A 101 ? 0.4399 0.5060 0.1977 -0.0086 -0.0597 -0.0113 387 LYS   A CG  
832  N N   . TYR   A 102 ? 0.2576 0.3632 0.0941 0.0129  -0.0240 0.0371  388 TYR   A N   
833  C CA  . TYR   A 102 ? 0.2415 0.3380 0.0877 0.0177  -0.0095 0.0290  388 TYR   A CA  
834  C C   . TYR   A 102 ? 0.2453 0.3310 0.0988 0.0261  -0.0056 0.0280  388 TYR   A C   
835  O O   . TYR   A 102 ? 0.2582 0.3292 0.1347 0.0387  -0.0123 0.0451  388 TYR   A O   
836  C CB  . TYR   A 102 ? 0.2542 0.3369 0.0812 0.0039  -0.0095 0.0177  388 TYR   A CB  
837  C CG  . TYR   A 102 ? 0.2505 0.3194 0.0630 -0.0096 -0.0071 0.0140  388 TYR   A CG  
838  C CD1 . TYR   A 102 ? 0.2499 0.3222 0.0792 -0.0145 -0.0165 0.0102  388 TYR   A CD1 
839  C CD2 . TYR   A 102 ? 0.2565 0.3201 0.0670 -0.0151 -0.0071 0.0150  388 TYR   A CD2 
840  C CE1 . TYR   A 102 ? 0.2659 0.3256 0.0805 -0.0137 -0.0232 0.0062  388 TYR   A CE1 
841  C CE2 . TYR   A 102 ? 0.2612 0.3161 0.0476 -0.0153 -0.0024 0.0103  388 TYR   A CE2 
842  C CZ  . TYR   A 102 ? 0.2668 0.3183 0.0637 -0.0166 -0.0110 0.0113  388 TYR   A CZ  
843  O OH  . TYR   A 102 ? 0.2746 0.3073 0.0884 -0.0174 0.0093  0.0023  388 TYR   A OH  
844  N N   . GLU   A 103 ? 0.2359 0.3163 0.1026 0.0327  -0.0032 0.0369  389 GLU   A N   
845  C CA  . GLU   A 103 ? 0.2561 0.3201 0.1152 0.0276  -0.0144 0.0364  389 GLU   A CA  
846  C C   . GLU   A 103 ? 0.2480 0.2974 0.1113 0.0376  0.0033  0.0299  389 GLU   A C   
847  O O   . GLU   A 103 ? 0.2476 0.2942 0.0868 0.0377  0.0028  0.0257  389 GLU   A O   
848  C CB  . GLU   A 103 ? 0.2810 0.3448 0.1382 0.0239  -0.0020 0.0318  389 GLU   A CB  
849  C CG  . GLU   A 103 ? 0.3156 0.3772 0.1535 0.0190  -0.0192 0.0264  389 GLU   A CG  
850  C CD  . GLU   A 103 ? 0.3475 0.4137 0.1431 0.0160  -0.0433 0.0372  389 GLU   A CD  
851  O OE1 . GLU   A 103 ? 0.4336 0.4913 0.2230 -0.0193 -0.0680 0.0066  389 GLU   A OE1 
852  O OE2 . GLU   A 103 ? 0.3874 0.4517 0.1915 0.0504  -0.0403 0.0400  389 GLU   A OE2 
853  N N   . ALA   A 104 ? 0.2488 0.2830 0.1143 0.0366  0.0014  0.0443  390 ALA   A N   
854  C CA  . ALA   A 104 ? 0.2588 0.2843 0.1185 0.0386  0.0029  0.0282  390 ALA   A CA  
855  C C   . ALA   A 104 ? 0.2694 0.2748 0.1081 0.0427  -0.0023 0.0393  390 ALA   A C   
856  O O   . ALA   A 104 ? 0.2981 0.2852 0.1047 0.0423  -0.0114 0.0395  390 ALA   A O   
857  C CB  . ALA   A 104 ? 0.2768 0.3014 0.1305 0.0361  0.0167  0.0175  390 ALA   A CB  
858  N N   . GLY   A 105 ? 0.2844 0.2763 0.1025 0.0305  0.0028  0.0391  391 GLY   A N   
859  C CA  . GLY   A 105 ? 0.2855 0.2769 0.1166 0.0272  -0.0026 0.0348  391 GLY   A CA  
860  C C   . GLY   A 105 ? 0.2950 0.2759 0.1311 0.0292  -0.0064 0.0358  391 GLY   A C   
861  O O   . GLY   A 105 ? 0.2878 0.2760 0.1750 0.0346  -0.0163 0.0449  391 GLY   A O   
862  N N   . THR   A 106 ? 0.3171 0.2873 0.1660 0.0412  -0.0029 0.0384  392 THR   A N   
863  C CA  . THR   A 106 ? 0.3354 0.2963 0.1710 0.0487  0.0077  0.0498  392 THR   A CA  
864  C C   . THR   A 106 ? 0.3468 0.2965 0.1769 0.0469  0.0234  0.0496  392 THR   A C   
865  O O   . THR   A 106 ? 0.3384 0.2990 0.2043 0.0476  0.0402  0.0404  392 THR   A O   
866  C CB  . THR   A 106 ? 0.3402 0.3036 0.1851 0.0544  0.0196  0.0470  392 THR   A CB  
867  O OG1 . THR   A 106 ? 0.3310 0.3196 0.1590 0.0597  0.0029  0.0418  392 THR   A OG1 
868  C CG2 . THR   A 106 ? 0.3497 0.3195 0.1931 0.0500  0.0166  0.0542  392 THR   A CG2 
869  N N   . TYR   A 107 ? 0.3604 0.3061 0.1920 0.0535  0.0280  0.0727  393 TYR   A N   
870  C CA  . TYR   A 107 ? 0.3939 0.3234 0.2231 0.0542  0.0360  0.0919  393 TYR   A CA  
871  C C   . TYR   A 107 ? 0.4111 0.3632 0.2808 0.0563  0.0429  0.1044  393 TYR   A C   
872  O O   . TYR   A 107 ? 0.4530 0.3461 0.3159 0.0875  0.0833  0.1102  393 TYR   A O   
873  C CB  . TYR   A 107 ? 0.3948 0.3104 0.2347 0.0536  0.0392  0.0733  393 TYR   A CB  
874  C CG  . TYR   A 107 ? 0.4032 0.3166 0.2243 0.0492  0.0417  0.0700  393 TYR   A CG  
875  C CD1 . TYR   A 107 ? 0.3821 0.3219 0.2141 0.0466  0.0552  0.0698  393 TYR   A CD1 
876  C CD2 . TYR   A 107 ? 0.4070 0.3262 0.2293 0.0559  0.0297  0.0656  393 TYR   A CD2 
877  C CE1 . TYR   A 107 ? 0.3770 0.3378 0.2222 0.0420  0.0425  0.0692  393 TYR   A CE1 
878  C CE2 . TYR   A 107 ? 0.4049 0.3329 0.2338 0.0492  0.0334  0.0746  393 TYR   A CE2 
879  C CZ  . TYR   A 107 ? 0.3806 0.3315 0.2237 0.0483  0.0384  0.0828  393 TYR   A CZ  
880  O OH  . TYR   A 107 ? 0.3921 0.3652 0.2552 0.0485  0.0324  0.1112  393 TYR   A OH  
881  N N   . PRO   A 108 ? 0.4284 0.4166 0.2978 0.0394  0.0147  0.1115  394 PRO   A N   
882  C CA  . PRO   A 108 ? 0.4255 0.4376 0.2770 0.0291  0.0183  0.1138  394 PRO   A CA  
883  C C   . PRO   A 108 ? 0.3784 0.4479 0.2660 0.0268  0.0086  0.1240  394 PRO   A C   
884  O O   . PRO   A 108 ? 0.3394 0.5114 0.2776 0.0397  -0.0158 0.1214  394 PRO   A O   
885  C CB  . PRO   A 108 ? 0.4348 0.4572 0.3155 0.0285  0.0007  0.1067  394 PRO   A CB  
886  C CG  . PRO   A 108 ? 0.4599 0.4774 0.3458 0.0346  -0.0025 0.0846  394 PRO   A CG  
887  C CD  . PRO   A 108 ? 0.4388 0.4475 0.3346 0.0390  -0.0032 0.0944  394 PRO   A CD  
888  N N   . GLN   A 109 ? 0.3487 0.4606 0.2438 0.0264  0.0044  0.1091  395 GLN   A N   
889  C CA  . GLN   A 109 ? 0.3455 0.4576 0.2453 0.0354  0.0136  0.0979  395 GLN   A CA  
890  C C   . GLN   A 109 ? 0.3291 0.4396 0.2146 0.0300  -0.0047 0.0907  395 GLN   A C   
891  O O   . GLN   A 109 ? 0.3429 0.4477 0.2015 0.0172  0.0031  0.1326  395 GLN   A O   
892  C CB  . GLN   A 109 ? 0.3971 0.4924 0.2884 0.0415  0.0086  0.0699  395 GLN   A CB  
893  C CG  . GLN   A 109 ? 0.4356 0.5288 0.3153 0.0446  -0.0023 0.0558  395 GLN   A CG  
894  C CD  . GLN   A 109 ? 0.4874 0.5596 0.3727 0.0451  0.0129  0.0330  395 GLN   A CD  
895  O OE1 . GLN   A 109 ? 0.4921 0.6005 0.3577 0.0971  0.0206  0.0557  395 GLN   A OE1 
896  N NE2 . GLN   A 109 ? 0.5530 0.5749 0.4319 0.0304  0.0202  0.0189  395 GLN   A NE2 
897  N N   . THR   A 110 ? 0.2940 0.4198 0.2038 0.0295  0.0042  0.0813  396 THR   A N   
898  C CA  . THR   A 110 ? 0.2780 0.4178 0.1815 0.0345  -0.0062 0.0732  396 THR   A CA  
899  C C   . THR   A 110 ? 0.2729 0.4218 0.1601 0.0417  -0.0089 0.0680  396 THR   A C   
900  O O   . THR   A 110 ? 0.2622 0.4056 0.1587 0.0333  -0.0242 0.0548  396 THR   A O   
901  C CB  . THR   A 110 ? 0.3005 0.4018 0.2024 0.0396  0.0159  0.0653  396 THR   A CB  
902  O OG1 . THR   A 110 ? 0.3162 0.4047 0.2067 0.0517  0.0248  0.0715  396 THR   A OG1 
903  C CG2 . THR   A 110 ? 0.3016 0.4128 0.2177 0.0431  0.0209  0.0626  396 THR   A CG2 
904  N N   . PRO   A 111 ? 0.2803 0.4402 0.1633 0.0465  -0.0314 0.0725  397 PRO   A N   
905  C CA  . PRO   A 111 ? 0.3044 0.4546 0.1748 0.0415  -0.0294 0.0680  397 PRO   A CA  
906  C C   . PRO   A 111 ? 0.2818 0.4606 0.1728 0.0443  -0.0211 0.0592  397 PRO   A C   
907  O O   . PRO   A 111 ? 0.2804 0.4735 0.2304 0.0563  0.0054  0.0846  397 PRO   A O   
908  C CB  . PRO   A 111 ? 0.3214 0.4693 0.1752 0.0290  -0.0357 0.0627  397 PRO   A CB  
909  C CG  . PRO   A 111 ? 0.3443 0.4642 0.1769 0.0363  -0.0584 0.0682  397 PRO   A CG  
910  C CD  . PRO   A 111 ? 0.3342 0.4619 0.1580 0.0459  -0.0527 0.0783  397 PRO   A CD  
911  N N   . LEU   A 112 ? 0.2871 0.4576 0.1538 0.0445  0.0023  0.0520  398 LEU   A N   
912  C CA  . LEU   A 112 ? 0.2832 0.4594 0.1484 0.0366  0.0074  0.0409  398 LEU   A CA  
913  C C   . LEU   A 112 ? 0.3081 0.4900 0.2136 0.0241  0.0022  0.0322  398 LEU   A C   
914  O O   . LEU   A 112 ? 0.3603 0.4967 0.3082 0.0205  0.0316  -0.0215 398 LEU   A O   
915  C CB  . LEU   A 112 ? 0.2796 0.4426 0.1270 0.0243  0.0082  0.0406  398 LEU   A CB  
916  C CG  . LEU   A 112 ? 0.2839 0.4223 0.1089 0.0280  0.0082  0.0301  398 LEU   A CG  
917  C CD1 . LEU   A 112 ? 0.2871 0.4215 0.0835 0.0227  0.0040  0.0330  398 LEU   A CD1 
918  C CD2 . LEU   A 112 ? 0.3084 0.4136 0.1309 0.0230  0.0113  0.0230  398 LEU   A CD2 
919  N N   . HIS   A 113 ? 0.2945 0.5076 0.2634 0.0278  -0.0210 0.0428  399 HIS   A N   
920  C CA  . HIS   A 113 ? 0.3102 0.5355 0.2714 0.0109  -0.0482 0.0586  399 HIS   A CA  
921  C C   . HIS   A 113 ? 0.3213 0.5428 0.2576 0.0100  -0.0548 0.0588  399 HIS   A C   
922  O O   . HIS   A 113 ? 0.3350 0.5672 0.2983 0.0289  -0.0351 0.0633  399 HIS   A O   
923  C CB  . HIS   A 113 ? 0.3188 0.5632 0.3191 0.0150  -0.0658 0.0598  399 HIS   A CB  
924  C CG  . HIS   A 113 ? 0.3319 0.5932 0.3236 -0.0036 -0.0928 0.0736  399 HIS   A CG  
925  N ND1 . HIS   A 113 ? 0.3808 0.6142 0.3568 0.0000  -0.0850 0.0466  399 HIS   A ND1 
926  C CD2 . HIS   A 113 ? 0.3433 0.6101 0.3517 -0.0192 -0.0999 0.0576  399 HIS   A CD2 
927  C CE1 . HIS   A 113 ? 0.3588 0.6262 0.3477 -0.0043 -0.1164 0.0558  399 HIS   A CE1 
928  N NE2 . HIS   A 113 ? 0.3634 0.6370 0.3402 -0.0181 -0.1136 0.0696  399 HIS   A NE2 
929  N N   . LEU   A 114 ? 0.3548 0.5344 0.2178 -0.0003 -0.0758 0.0421  400 LEU   A N   
930  C CA  . LEU   A 114 ? 0.3710 0.5475 0.2064 -0.0018 -0.0786 0.0371  400 LEU   A CA  
931  C C   . LEU   A 114 ? 0.3905 0.5652 0.2456 -0.0169 -0.0564 0.0284  400 LEU   A C   
932  O O   . LEU   A 114 ? 0.4469 0.6396 0.2790 -0.0566 -0.0423 -0.0244 400 LEU   A O   
933  C CB  . LEU   A 114 ? 0.3720 0.5400 0.1460 0.0104  -0.0863 0.0508  400 LEU   A CB  
934  C CG  . LEU   A 114 ? 0.3603 0.5481 0.2173 -0.0017 -0.1041 0.0509  400 LEU   A CG  
935  C CD1 . LEU   A 114 ? 0.3927 0.5832 0.2878 -0.0039 -0.1148 0.0545  400 LEU   A CD1 
936  C CD2 . LEU   A 114 ? 0.3331 0.5047 0.1408 0.0094  -0.0968 0.0368  400 LEU   A CD2 
937  N N   . GLN   A 115 ? 0.3824 0.5787 0.2840 -0.0170 -0.0725 0.0383  401 GLN   A N   
938  C CA  . GLN   A 115 ? 0.4336 0.5813 0.2815 -0.0258 -0.0677 0.0131  401 GLN   A CA  
939  C C   . GLN   A 115 ? 0.3781 0.5442 0.2463 -0.0447 -0.0787 0.0002  401 GLN   A C   
940  O O   . GLN   A 115 ? 0.4023 0.5348 0.2239 -0.0476 -0.0699 0.0074  401 GLN   A O   
941  C CB  . GLN   A 115 ? 0.4571 0.6403 0.3956 -0.0385 -0.0632 -0.0048 401 GLN   A CB  
942  C CG  . GLN   A 115 ? 0.5249 0.6849 0.4542 -0.0229 -0.0839 -0.0281 401 GLN   A CG  
943  C CD  . GLN   A 115 ? 0.5928 0.7634 0.5323 -0.0589 -0.0455 -0.0576 401 GLN   A CD  
944  O OE1 . GLN   A 115 ? 0.6876 0.8340 0.5963 -0.1008 -0.0599 -0.0914 401 GLN   A OE1 
945  N NE2 . GLN   A 115 ? 0.6556 0.7853 0.5693 -0.0583 -0.0417 -0.0878 401 GLN   A NE2 
946  N N   . VAL   A 116 ? 0.3586 0.5116 0.2014 -0.0308 -0.0522 0.0296  402 VAL   A N   
947  C CA  . VAL   A 116 ? 0.3288 0.5016 0.1376 -0.0485 -0.0595 0.0232  402 VAL   A CA  
948  C C   . VAL   A 116 ? 0.3144 0.4481 0.1131 -0.0395 -0.0515 0.0152  402 VAL   A C   
949  O O   . VAL   A 116 ? 0.3264 0.4509 0.1778 -0.0435 -0.0561 -0.0144 402 VAL   A O   
950  C CB  . VAL   A 116 ? 0.3573 0.5315 0.1539 -0.0490 -0.0334 0.0253  402 VAL   A CB  
951  C CG1 . VAL   A 116 ? 0.3648 0.5423 0.1734 -0.0438 -0.0241 0.0304  402 VAL   A CG1 
952  C CG2 . VAL   A 116 ? 0.3693 0.5533 0.1284 -0.0545 -0.0202 0.0146  402 VAL   A CG2 
953  N N   . PRO   A 117 ? 0.3213 0.4207 0.1047 -0.0499 -0.0576 -0.0127 403 PRO   A N   
954  C CA  . PRO   A 117 ? 0.3177 0.3926 0.1097 -0.0481 -0.0481 0.0012  403 PRO   A CA  
955  C C   . PRO   A 117 ? 0.2973 0.3577 0.0914 -0.0420 -0.0288 0.0132  403 PRO   A C   
956  O O   . PRO   A 117 ? 0.3172 0.3608 0.1220 -0.0619 -0.0329 0.0249  403 PRO   A O   
957  C CB  . PRO   A 117 ? 0.3442 0.4156 0.1167 -0.0424 -0.0357 -0.0078 403 PRO   A CB  
958  C CG  . PRO   A 117 ? 0.3539 0.4322 0.1448 -0.0521 -0.0354 -0.0292 403 PRO   A CG  
959  C CD  . PRO   A 117 ? 0.3386 0.4312 0.1133 -0.0592 -0.0434 -0.0249 403 PRO   A CD  
960  N N   . PRO   A 118 ? 0.2604 0.3273 0.0772 -0.0256 -0.0237 0.0325  404 PRO   A N   
961  C CA  . PRO   A 118 ? 0.2488 0.3194 0.0714 -0.0167 -0.0212 0.0263  404 PRO   A CA  
962  C C   . PRO   A 118 ? 0.2495 0.3106 0.0735 -0.0143 -0.0109 0.0252  404 PRO   A C   
963  O O   . PRO   A 118 ? 0.2631 0.3143 0.0975 -0.0001 0.0018  0.0256  404 PRO   A O   
964  C CB  . PRO   A 118 ? 0.2599 0.3200 0.0893 -0.0128 -0.0181 0.0250  404 PRO   A CB  
965  C CG  . PRO   A 118 ? 0.2557 0.3181 0.0851 -0.0235 -0.0130 0.0237  404 PRO   A CG  
966  C CD  . PRO   A 118 ? 0.2511 0.3285 0.0792 -0.0255 -0.0170 0.0324  404 PRO   A CD  
967  N N   . CYS   A 119 ? 0.2495 0.3002 0.0603 -0.0227 0.0119  0.0212  405 CYS   A N   
968  C CA  . CYS   A 119 ? 0.2643 0.2896 0.0543 -0.0224 -0.0023 0.0194  405 CYS   A CA  
969  C C   . CYS   A 119 ? 0.2427 0.2723 0.0607 -0.0159 0.0028  0.0251  405 CYS   A C   
970  O O   . CYS   A 119 ? 0.2323 0.2703 0.0709 -0.0075 -0.0102 0.0103  405 CYS   A O   
971  C CB  . CYS   A 119 ? 0.2878 0.2908 0.0730 -0.0298 -0.0099 0.0214  405 CYS   A CB  
972  S SG  . CYS   A 119 ? 0.3548 0.3174 0.1375 -0.0552 -0.0266 -0.0039 405 CYS   A SG  
973  N N   . GLN   A 120 ? 0.2421 0.2818 0.0594 -0.0177 0.0051  0.0165  406 GLN   A N   
974  C CA  . GLN   A 120 ? 0.2383 0.2879 0.0603 -0.0155 0.0102  0.0123  406 GLN   A CA  
975  C C   . GLN   A 120 ? 0.2277 0.2867 0.0516 -0.0118 0.0118  0.0045  406 GLN   A C   
976  O O   . GLN   A 120 ? 0.2310 0.3090 0.0778 -0.0208 0.0058  0.0029  406 GLN   A O   
977  C CB  . GLN   A 120 ? 0.2529 0.2983 0.0669 -0.0205 0.0153  0.0236  406 GLN   A CB  
978  C CG  . GLN   A 120 ? 0.2716 0.3045 0.0720 -0.0198 0.0178  0.0212  406 GLN   A CG  
979  C CD  . GLN   A 120 ? 0.2823 0.3132 0.0848 -0.0200 0.0198  0.0100  406 GLN   A CD  
980  O OE1 . GLN   A 120 ? 0.2971 0.3378 0.0876 -0.0205 0.0434  0.0095  406 GLN   A OE1 
981  N NE2 . GLN   A 120 ? 0.2954 0.3119 0.1023 -0.0162 0.0232  -0.0032 406 GLN   A NE2 
982  N N   . VAL   A 121 ? 0.2222 0.2709 0.0699 -0.0002 0.0105  -0.0078 407 VAL   A N   
983  C CA  . VAL   A 121 ? 0.2380 0.2718 0.0701 -0.0046 0.0042  -0.0056 407 VAL   A CA  
984  C C   . VAL   A 121 ? 0.2265 0.2752 0.0664 0.0063  -0.0022 -0.0063 407 VAL   A C   
985  O O   . VAL   A 121 ? 0.2392 0.2946 0.0859 0.0054  -0.0122 -0.0208 407 VAL   A O   
986  C CB  . VAL   A 121 ? 0.2444 0.2705 0.0685 -0.0083 0.0024  -0.0074 407 VAL   A CB  
987  C CG1 . VAL   A 121 ? 0.2570 0.2820 0.0842 -0.0055 -0.0037 -0.0018 407 VAL   A CG1 
988  C CG2 . VAL   A 121 ? 0.2512 0.2734 0.0644 -0.0156 0.0081  -0.0077 407 VAL   A CG2 
989  N N   . GLY   A 122 ? 0.2329 0.2717 0.0796 0.0070  -0.0087 -0.0026 408 GLY   A N   
990  C CA  . GLY   A 122 ? 0.2547 0.2715 0.0802 0.0134  -0.0012 -0.0055 408 GLY   A CA  
991  C C   . GLY   A 122 ? 0.2540 0.2679 0.0868 0.0291  -0.0029 0.0040  408 GLY   A C   
992  O O   . GLY   A 122 ? 0.2656 0.2752 0.1311 0.0478  -0.0174 0.0016  408 GLY   A O   
993  N N   . ILE   A 123 ? 0.2753 0.2710 0.0926 0.0293  -0.0094 0.0010  409 ILE   A N   
994  C CA  . ILE   A 123 ? 0.2841 0.2791 0.0964 0.0204  -0.0165 -0.0004 409 ILE   A CA  
995  C C   . ILE   A 123 ? 0.2929 0.2845 0.1063 0.0205  -0.0031 -0.0077 409 ILE   A C   
996  O O   . ILE   A 123 ? 0.2930 0.2888 0.1085 0.0151  -0.0072 -0.0101 409 ILE   A O   
997  C CB  . ILE   A 123 ? 0.3055 0.3072 0.0949 0.0204  -0.0233 0.0018  409 ILE   A CB  
998  C CG1 . ILE   A 123 ? 0.3387 0.3225 0.1020 0.0163  -0.0485 -0.0025 409 ILE   A CG1 
999  C CG2 . ILE   A 123 ? 0.3205 0.3190 0.0998 0.0194  -0.0154 0.0003  409 ILE   A CG2 
1000 C CD1 . ILE   A 123 ? 0.3630 0.3597 0.1522 0.0173  -0.0492 -0.0110 409 ILE   A CD1 
1001 N N   . PHE   A 124 ? 0.2987 0.2740 0.1064 0.0132  0.0022  -0.0014 410 PHE   A N   
1002 C CA  . PHE   A 124 ? 0.3227 0.2799 0.1037 0.0191  0.0038  -0.0047 410 PHE   A CA  
1003 C C   . PHE   A 124 ? 0.3327 0.2741 0.0909 0.0219  0.0035  -0.0053 410 PHE   A C   
1004 O O   . PHE   A 124 ? 0.3613 0.2979 0.1127 0.0123  -0.0099 0.0197  410 PHE   A O   
1005 C CB  . PHE   A 124 ? 0.3370 0.3052 0.1290 0.0215  0.0180  -0.0028 410 PHE   A CB  
1006 C CG  . PHE   A 124 ? 0.3446 0.3242 0.1492 0.0192  0.0300  -0.0035 410 PHE   A CG  
1007 C CD1 . PHE   A 124 ? 0.3486 0.3389 0.1694 0.0123  0.0390  -0.0048 410 PHE   A CD1 
1008 C CD2 . PHE   A 124 ? 0.3734 0.3428 0.1544 0.0144  0.0182  -0.0077 410 PHE   A CD2 
1009 C CE1 . PHE   A 124 ? 0.3574 0.3668 0.1858 0.0103  0.0386  0.0001  410 PHE   A CE1 
1010 C CE2 . PHE   A 124 ? 0.3779 0.3611 0.1772 0.0175  0.0265  0.0097  410 PHE   A CE2 
1011 C CZ  . PHE   A 124 ? 0.3763 0.3652 0.1915 0.0118  0.0252  0.0138  410 PHE   A CZ  
1012 N N   . LEU   A 125 ? 0.3503 0.2708 0.1043 0.0290  -0.0028 -0.0107 411 LEU   A N   
1013 C CA  . LEU   A 125 ? 0.3908 0.2734 0.1135 0.0292  -0.0008 -0.0319 411 LEU   A CA  
1014 C C   . LEU   A 125 ? 0.4138 0.2884 0.1312 0.0364  0.0120  -0.0471 411 LEU   A C   
1015 O O   . LEU   A 125 ? 0.4463 0.3031 0.1253 0.0543  0.0164  -0.0500 411 LEU   A O   
1016 C CB  . LEU   A 125 ? 0.3905 0.2783 0.1067 0.0331  -0.0103 -0.0255 411 LEU   A CB  
1017 C CG  . LEU   A 125 ? 0.4137 0.2947 0.1299 0.0230  -0.0022 -0.0232 411 LEU   A CG  
1018 C CD1 . LEU   A 125 ? 0.4231 0.2964 0.1050 0.0261  0.0042  -0.0332 411 LEU   A CD1 
1019 C CD2 . LEU   A 125 ? 0.4299 0.3132 0.1626 0.0295  0.0006  -0.0279 411 LEU   A CD2 
1020 N N   . ASP   A 126 ? 0.4474 0.2920 0.1427 0.0374  0.0086  -0.0639 412 ASP   A N   
1021 C CA  . ASP   A 126 ? 0.4541 0.2963 0.1629 0.0303  0.0240  -0.0749 412 ASP   A CA  
1022 C C   . ASP   A 126 ? 0.4682 0.2915 0.1730 0.0317  0.0309  -0.0782 412 ASP   A C   
1023 O O   . ASP   A 126 ? 0.4630 0.2935 0.1536 0.0435  0.0509  -0.0734 412 ASP   A O   
1024 C CB  . ASP   A 126 ? 0.4561 0.3255 0.2048 0.0364  0.0324  -0.0683 412 ASP   A CB  
1025 C CG  . ASP   A 126 ? 0.4769 0.3739 0.2358 0.0554  0.0472  -0.0780 412 ASP   A CG  
1026 O OD1 . ASP   A 126 ? 0.4718 0.3952 0.3024 0.0350  0.0525  -0.0711 412 ASP   A OD1 
1027 O OD2 . ASP   A 126 ? 0.4879 0.4506 0.3039 0.0650  0.0534  -0.0434 412 ASP   A OD2 
1028 N N   . TYR   A 127 ? 0.4838 0.2924 0.1638 0.0233  0.0359  -0.0825 413 TYR   A N   
1029 C CA  . TYR   A 127 ? 0.4992 0.2843 0.1607 0.0124  0.0479  -0.0833 413 TYR   A CA  
1030 C C   . TYR   A 127 ? 0.5111 0.2916 0.1943 0.0225  0.0542  -0.0789 413 TYR   A C   
1031 O O   . TYR   A 127 ? 0.4905 0.2911 0.2309 0.0223  0.0576  -0.0593 413 TYR   A O   
1032 C CB  . TYR   A 127 ? 0.5143 0.2700 0.1723 0.0037  0.0485  -0.0797 413 TYR   A CB  
1033 C CG  . TYR   A 127 ? 0.5120 0.2616 0.1995 -0.0081 0.0469  -0.0837 413 TYR   A CG  
1034 C CD1 . TYR   A 127 ? 0.5312 0.2637 0.2203 -0.0060 0.0410  -0.0826 413 TYR   A CD1 
1035 C CD2 . TYR   A 127 ? 0.5190 0.2533 0.1918 -0.0088 0.0446  -0.0851 413 TYR   A CD2 
1036 C CE1 . TYR   A 127 ? 0.5270 0.2671 0.2231 -0.0140 0.0404  -0.0885 413 TYR   A CE1 
1037 C CE2 . TYR   A 127 ? 0.5248 0.2752 0.1956 -0.0157 0.0474  -0.0799 413 TYR   A CE2 
1038 C CZ  . TYR   A 127 ? 0.5270 0.2757 0.2221 -0.0157 0.0472  -0.0637 413 TYR   A CZ  
1039 O OH  . TYR   A 127 ? 0.5431 0.3153 0.2213 -0.0285 0.0498  -0.0335 413 TYR   A OH  
1040 N N   . GLU   A 128 ? 0.5295 0.3015 0.2238 0.0331  0.0783  -0.0871 414 GLU   A N   
1041 C CA  . GLU   A 128 ? 0.5550 0.3158 0.2630 0.0519  0.0579  -0.1037 414 GLU   A CA  
1042 C C   . GLU   A 128 ? 0.5398 0.3044 0.2451 0.0620  0.0619  -0.0919 414 GLU   A C   
1043 O O   . GLU   A 128 ? 0.5798 0.3216 0.2631 0.0751  0.0440  -0.0958 414 GLU   A O   
1044 C CB  . GLU   A 128 ? 0.5821 0.3453 0.2772 0.0580  0.0630  -0.1384 414 GLU   A CB  
1045 C CG  . GLU   A 128 ? 0.6233 0.3980 0.2985 0.0476  0.0454  -0.1555 414 GLU   A CG  
1046 C CD  . GLU   A 128 ? 0.6555 0.4713 0.3712 0.0444  0.0203  -0.1352 414 GLU   A CD  
1047 O OE1 . GLU   A 128 ? 0.7032 0.5402 0.4635 -0.0272 0.0028  -0.1575 414 GLU   A OE1 
1048 O OE2 . GLU   A 128 ? 0.7268 0.5152 0.4700 0.0160  0.0211  -0.1078 414 GLU   A OE2 
1049 N N   . ALA   A 129 ? 0.5256 0.3014 0.2353 0.0613  0.0478  -0.0713 415 ALA   A N   
1050 C CA  . ALA   A 129 ? 0.5056 0.3018 0.2326 0.0718  0.0596  -0.0726 415 ALA   A CA  
1051 C C   . ALA   A 129 ? 0.5062 0.3210 0.2252 0.0692  0.0295  -0.0525 415 ALA   A C   
1052 O O   . ALA   A 129 ? 0.5158 0.3585 0.2314 0.0670  0.0117  -0.0556 415 ALA   A O   
1053 C CB  . ALA   A 129 ? 0.5042 0.3335 0.2535 0.0658  0.0670  -0.0594 415 ALA   A CB  
1054 N N   . GLY   A 130 ? 0.5021 0.3194 0.1943 0.0651  0.0140  -0.0535 416 GLY   A N   
1055 C CA  . GLY   A 130 ? 0.4992 0.3267 0.1930 0.0539  0.0094  -0.0378 416 GLY   A CA  
1056 C C   . GLY   A 130 ? 0.4832 0.3167 0.1990 0.0498  0.0207  -0.0274 416 GLY   A C   
1057 O O   . GLY   A 130 ? 0.5095 0.3217 0.1970 0.0595  0.0062  -0.0436 416 GLY   A O   
1058 N N   . MET   A 131 ? 0.4543 0.3094 0.1920 0.0581  0.0388  -0.0343 417 MET   A N   
1059 C CA  . MET   A 131 ? 0.4408 0.3259 0.1929 0.0552  0.0427  -0.0419 417 MET   A CA  
1060 C C   . MET   A 131 ? 0.4130 0.2955 0.1583 0.0443  0.0226  -0.0396 417 MET   A C   
1061 O O   . MET   A 131 ? 0.3911 0.3014 0.1635 0.0515  0.0233  -0.0541 417 MET   A O   
1062 C CB  . MET   A 131 ? 0.4579 0.3598 0.2511 0.0471  0.0665  -0.0333 417 MET   A CB  
1063 C CG  . MET   A 131 ? 0.4839 0.4060 0.2880 0.0370  0.0744  -0.0403 417 MET   A CG  
1064 S SD  . MET   A 131 ? 0.5131 0.4958 0.4221 0.0308  0.1159  -0.0561 417 MET   A SD  
1065 C CE  . MET   A 131 ? 0.5392 0.4895 0.4202 0.0543  0.1247  -0.0699 417 MET   A CE  
1066 N N   . VAL   A 132 ? 0.3904 0.2734 0.1503 0.0513  0.0059  -0.0274 418 VAL   A N   
1067 C CA  . VAL   A 132 ? 0.3435 0.2747 0.1210 0.0513  0.0131  -0.0191 418 VAL   A CA  
1068 C C   . VAL   A 132 ? 0.3350 0.2775 0.1055 0.0480  0.0120  -0.0116 418 VAL   A C   
1069 O O   . VAL   A 132 ? 0.3478 0.2999 0.1132 0.0689  -0.0014 -0.0131 418 VAL   A O   
1070 C CB  . VAL   A 132 ? 0.3303 0.2782 0.1314 0.0378  0.0147  -0.0286 418 VAL   A CB  
1071 C CG1 . VAL   A 132 ? 0.3223 0.2794 0.1341 0.0323  0.0139  -0.0328 418 VAL   A CG1 
1072 C CG2 . VAL   A 132 ? 0.3441 0.2653 0.1603 0.0412  0.0287  -0.0327 418 VAL   A CG2 
1073 N N   . SER   A 133 ? 0.3259 0.2971 0.1115 0.0414  0.0253  -0.0039 419 SER   A N   
1074 C CA  . SER   A 133 ? 0.3208 0.3144 0.1098 0.0417  0.0375  -0.0052 419 SER   A CA  
1075 C C   . SER   A 133 ? 0.2812 0.3110 0.0853 0.0377  0.0319  -0.0076 419 SER   A C   
1076 O O   . SER   A 133 ? 0.2989 0.3094 0.1019 0.0439  0.0008  -0.0210 419 SER   A O   
1077 C CB  . SER   A 133 ? 0.3390 0.3210 0.1225 0.0510  0.0571  -0.0017 419 SER   A CB  
1078 O OG  . SER   A 133 ? 0.3631 0.3432 0.1717 0.0680  0.0681  -0.0170 419 SER   A OG  
1079 N N   . PHE   A 134 ? 0.2653 0.3172 0.0870 0.0306  0.0295  -0.0053 420 PHE   A N   
1080 C CA  . PHE   A 134 ? 0.2535 0.3144 0.0761 0.0357  0.0314  -0.0065 420 PHE   A CA  
1081 C C   . PHE   A 134 ? 0.2536 0.3194 0.0819 0.0382  0.0307  -0.0091 420 PHE   A C   
1082 O O   . PHE   A 134 ? 0.2481 0.3421 0.0968 0.0385  0.0248  0.0103  420 PHE   A O   
1083 C CB  . PHE   A 134 ? 0.2594 0.3054 0.0784 0.0333  0.0316  -0.0098 420 PHE   A CB  
1084 C CG  . PHE   A 134 ? 0.2611 0.2920 0.0838 0.0314  0.0255  -0.0012 420 PHE   A CG  
1085 C CD1 . PHE   A 134 ? 0.2712 0.2910 0.0965 0.0378  0.0265  -0.0035 420 PHE   A CD1 
1086 C CD2 . PHE   A 134 ? 0.2709 0.2899 0.0945 0.0341  0.0231  -0.0015 420 PHE   A CD2 
1087 C CE1 . PHE   A 134 ? 0.2720 0.2776 0.0951 0.0365  0.0312  0.0036  420 PHE   A CE1 
1088 C CE2 . PHE   A 134 ? 0.2596 0.2951 0.0742 0.0397  0.0174  -0.0052 420 PHE   A CE2 
1089 C CZ  . PHE   A 134 ? 0.2650 0.2948 0.0763 0.0320  0.0235  0.0054  420 PHE   A CZ  
1090 N N   . TYR   A 135 ? 0.2501 0.3186 0.0908 0.0338  0.0241  0.0050  421 TYR   A N   
1091 C CA  . TYR   A 135 ? 0.2547 0.3343 0.0900 0.0306  0.0328  -0.0008 421 TYR   A CA  
1092 C C   . TYR   A 135 ? 0.2424 0.3363 0.0939 0.0258  0.0215  0.0049  421 TYR   A C   
1093 O O   . TYR   A 135 ? 0.2391 0.3443 0.0707 0.0292  0.0113  -0.0084 421 TYR   A O   
1094 C CB  . TYR   A 135 ? 0.2874 0.3298 0.0916 0.0217  0.0326  0.0037  421 TYR   A CB  
1095 C CG  . TYR   A 135 ? 0.3165 0.3383 0.1201 0.0240  0.0435  -0.0070 421 TYR   A CG  
1096 C CD1 . TYR   A 135 ? 0.3327 0.3272 0.1308 0.0245  0.0433  -0.0253 421 TYR   A CD1 
1097 C CD2 . TYR   A 135 ? 0.3290 0.3380 0.1318 0.0264  0.0499  -0.0111 421 TYR   A CD2 
1098 C CE1 . TYR   A 135 ? 0.3464 0.3268 0.1435 0.0296  0.0533  -0.0262 421 TYR   A CE1 
1099 C CE2 . TYR   A 135 ? 0.3465 0.3452 0.1254 0.0318  0.0514  -0.0118 421 TYR   A CE2 
1100 C CZ  . TYR   A 135 ? 0.3503 0.3213 0.1198 0.0377  0.0596  -0.0314 421 TYR   A CZ  
1101 O OH  . TYR   A 135 ? 0.3978 0.3359 0.1506 0.0585  0.0734  -0.0476 421 TYR   A OH  
1102 N N   . ASN   A 136 ? 0.2385 0.3522 0.0880 0.0287  0.0159  -0.0060 422 ASN   A N   
1103 C CA  . ASN   A 136 ? 0.2512 0.3602 0.0796 0.0154  0.0211  0.0033  422 ASN   A CA  
1104 C C   . ASN   A 136 ? 0.2515 0.3692 0.0878 0.0002  0.0257  0.0067  422 ASN   A C   
1105 O O   . ASN   A 136 ? 0.2695 0.3856 0.0971 -0.0133 0.0487  0.0037  422 ASN   A O   
1106 C CB  . ASN   A 136 ? 0.2537 0.3852 0.0804 0.0156  0.0187  -0.0031 422 ASN   A CB  
1107 C CG  . ASN   A 136 ? 0.2631 0.3898 0.0943 0.0186  0.0089  -0.0074 422 ASN   A CG  
1108 O OD1 . ASN   A 136 ? 0.2674 0.3805 0.1026 0.0128  0.0319  -0.0190 422 ASN   A OD1 
1109 N ND2 . ASN   A 136 ? 0.2777 0.4023 0.0818 0.0219  0.0061  -0.0039 422 ASN   A ND2 
1110 N N   . ILE   A 137 ? 0.2680 0.3476 0.0634 -0.0063 0.0347  0.0299  423 ILE   A N   
1111 C CA  . ILE   A 137 ? 0.2816 0.3610 0.0744 -0.0191 0.0279  0.0447  423 ILE   A CA  
1112 C C   . ILE   A 137 ? 0.2886 0.3724 0.0795 -0.0327 0.0264  0.0414  423 ILE   A C   
1113 O O   . ILE   A 137 ? 0.3078 0.4332 0.0840 -0.0629 0.0352  0.0328  423 ILE   A O   
1114 C CB  . ILE   A 137 ? 0.2934 0.3666 0.0776 -0.0216 0.0162  0.0440  423 ILE   A CB  
1115 C CG1 . ILE   A 137 ? 0.2915 0.3665 0.0860 -0.0164 0.0145  0.0512  423 ILE   A CG1 
1116 C CG2 . ILE   A 137 ? 0.3214 0.3649 0.1071 -0.0288 0.0015  0.0560  423 ILE   A CG2 
1117 C CD1 . ILE   A 137 ? 0.2883 0.3629 0.0982 -0.0108 0.0067  0.0425  423 ILE   A CD1 
1118 N N   . THR   A 138 ? 0.2786 0.3529 0.0902 -0.0406 0.0402  0.0406  424 THR   A N   
1119 C CA  . THR   A 138 ? 0.2891 0.3847 0.1075 -0.0455 0.0373  0.0233  424 THR   A CA  
1120 C C   . THR   A 138 ? 0.2742 0.3921 0.1257 -0.0599 0.0345  0.0079  424 THR   A C   
1121 O O   . THR   A 138 ? 0.3015 0.4246 0.1934 -0.0763 0.0381  0.0230  424 THR   A O   
1122 C CB  . THR   A 138 ? 0.2881 0.3743 0.1101 -0.0443 0.0364  0.0105  424 THR   A CB  
1123 O OG1 . THR   A 138 ? 0.2929 0.3720 0.1132 -0.0381 0.0437  0.0074  424 THR   A OG1 
1124 C CG2 . THR   A 138 ? 0.2836 0.3760 0.1075 -0.0427 0.0354  0.0013  424 THR   A CG2 
1125 N N   . ASP   A 139 ? 0.2713 0.4225 0.1259 -0.0440 0.0302  -0.0027 425 ASP   A N   
1126 C CA  . ASP   A 139 ? 0.2793 0.4555 0.1632 -0.0319 0.0301  -0.0084 425 ASP   A CA  
1127 C C   . ASP   A 139 ? 0.2918 0.4667 0.1748 -0.0320 0.0444  -0.0178 425 ASP   A C   
1128 O O   . ASP   A 139 ? 0.3241 0.4890 0.1716 -0.0175 0.0269  -0.0112 425 ASP   A O   
1129 C CB  . ASP   A 139 ? 0.2780 0.4821 0.1757 -0.0125 0.0267  -0.0063 425 ASP   A CB  
1130 C CG  . ASP   A 139 ? 0.2809 0.5004 0.2220 -0.0082 0.0109  -0.0218 425 ASP   A CG  
1131 O OD1 . ASP   A 139 ? 0.2817 0.5127 0.2319 -0.0011 0.0210  -0.0295 425 ASP   A OD1 
1132 O OD2 . ASP   A 139 ? 0.3105 0.5480 0.3133 0.0157  -0.0132 -0.0055 425 ASP   A OD2 
1133 N N   . HIS   A 140 ? 0.3151 0.4618 0.1564 -0.0386 0.0783  -0.0150 426 HIS   A N   
1134 C CA  . HIS   A 140 ? 0.3307 0.4667 0.1603 -0.0554 0.0834  -0.0226 426 HIS   A CA  
1135 C C   . HIS   A 140 ? 0.3052 0.4573 0.1482 -0.0396 0.0894  -0.0373 426 HIS   A C   
1136 O O   . HIS   A 140 ? 0.3223 0.4711 0.2003 -0.0463 0.1127  -0.0652 426 HIS   A O   
1137 C CB  . HIS   A 140 ? 0.3544 0.4841 0.1851 -0.0681 0.0889  -0.0099 426 HIS   A CB  
1138 C CG  . HIS   A 140 ? 0.4525 0.5007 0.2576 -0.0650 0.0539  0.0048  426 HIS   A CG  
1139 N ND1 . HIS   A 140 ? 0.5031 0.5221 0.3754 -0.0677 -0.0012 -0.0085 426 HIS   A ND1 
1140 C CD2 . HIS   A 140 ? 0.4996 0.5093 0.2832 -0.0654 0.0268  0.0171  426 HIS   A CD2 
1141 C CE1 . HIS   A 140 ? 0.5288 0.5109 0.3740 -0.0713 -0.0062 0.0103  426 HIS   A CE1 
1142 N NE2 . HIS   A 140 ? 0.5331 0.5032 0.2681 -0.0814 0.0021  0.0257  426 HIS   A NE2 
1143 N N   . GLY   A 141 ? 0.3026 0.4664 0.1190 -0.0253 0.0913  -0.0234 427 GLY   A N   
1144 C CA  . GLY   A 141 ? 0.2948 0.4581 0.1292 -0.0211 0.0815  -0.0047 427 GLY   A CA  
1145 C C   . GLY   A 141 ? 0.3115 0.4615 0.1441 -0.0092 0.0736  -0.0132 427 GLY   A C   
1146 O O   . GLY   A 141 ? 0.3647 0.4714 0.1760 0.0038  0.0662  -0.0139 427 GLY   A O   
1147 N N   . SER   A 142 ? 0.3092 0.4568 0.1503 0.0097  0.0508  -0.0013 428 SER   A N   
1148 C CA  . SER   A 142 ? 0.2944 0.4659 0.1601 0.0224  0.0528  0.0028  428 SER   A CA  
1149 C C   . SER   A 142 ? 0.2832 0.4394 0.1563 0.0401  0.0553  0.0044  428 SER   A C   
1150 O O   . SER   A 142 ? 0.2600 0.4159 0.1583 0.0413  0.0351  0.0120  428 SER   A O   
1151 C CB  . SER   A 142 ? 0.2932 0.4928 0.1604 0.0259  0.0398  0.0079  428 SER   A CB  
1152 O OG  . SER   A 142 ? 0.3305 0.5283 0.1749 0.0252  0.0406  0.0012  428 SER   A OG  
1153 N N   . LEU   A 143 ? 0.2896 0.4508 0.1629 0.0597  0.0658  0.0170  429 LEU   A N   
1154 C CA  . LEU   A 143 ? 0.3010 0.4399 0.1526 0.0586  0.0723  0.0312  429 LEU   A CA  
1155 C C   . LEU   A 143 ? 0.2843 0.4477 0.1447 0.0483  0.0474  0.0312  429 LEU   A C   
1156 O O   . LEU   A 143 ? 0.2838 0.4920 0.1744 0.0334  0.0519  0.0229  429 LEU   A O   
1157 C CB  . LEU   A 143 ? 0.3185 0.4564 0.1736 0.0762  0.0812  0.0297  429 LEU   A CB  
1158 C CG  . LEU   A 143 ? 0.3380 0.4567 0.1993 0.0860  0.0733  0.0304  429 LEU   A CG  
1159 C CD1 . LEU   A 143 ? 0.3363 0.4657 0.1729 0.0895  0.0837  0.0275  429 LEU   A CD1 
1160 C CD2 . LEU   A 143 ? 0.3536 0.4555 0.2291 0.0956  0.0475  0.0548  429 LEU   A CD2 
1161 N N   . ILE   A 144 ? 0.2637 0.4309 0.1197 0.0400  0.0234  0.0315  430 ILE   A N   
1162 C CA  . ILE   A 144 ? 0.2645 0.4174 0.1189 0.0440  0.0169  0.0378  430 ILE   A CA  
1163 C C   . ILE   A 144 ? 0.2499 0.4044 0.1212 0.0482  0.0094  0.0305  430 ILE   A C   
1164 O O   . ILE   A 144 ? 0.2744 0.4068 0.1510 0.0586  -0.0074 0.0504  430 ILE   A O   
1165 C CB  . ILE   A 144 ? 0.2617 0.4069 0.1104 0.0363  0.0145  0.0414  430 ILE   A CB  
1166 C CG1 . ILE   A 144 ? 0.2596 0.4127 0.0978 0.0371  -0.0017 0.0354  430 ILE   A CG1 
1167 C CG2 . ILE   A 144 ? 0.2625 0.4070 0.1118 0.0449  0.0122  0.0508  430 ILE   A CG2 
1168 C CD1 . ILE   A 144 ? 0.2565 0.4101 0.0875 0.0376  0.0098  0.0249  430 ILE   A CD1 
1169 N N   . TYR   A 145 ? 0.2605 0.3883 0.1197 0.0475  0.0164  0.0233  431 TYR   A N   
1170 C CA  . TYR   A 145 ? 0.2717 0.3819 0.1317 0.0625  0.0257  0.0153  431 TYR   A CA  
1171 C C   . TYR   A 145 ? 0.2823 0.3699 0.1097 0.0740  0.0372  0.0152  431 TYR   A C   
1172 O O   . TYR   A 145 ? 0.3022 0.3631 0.1287 0.0883  0.0211  0.0203  431 TYR   A O   
1173 C CB  . TYR   A 145 ? 0.2848 0.3706 0.1358 0.0585  0.0401  0.0212  431 TYR   A CB  
1174 C CG  . TYR   A 145 ? 0.3065 0.3679 0.1440 0.0657  0.0338  0.0288  431 TYR   A CG  
1175 C CD1 . TYR   A 145 ? 0.3153 0.3603 0.1416 0.0573  0.0287  0.0386  431 TYR   A CD1 
1176 C CD2 . TYR   A 145 ? 0.3300 0.3732 0.1080 0.0607  0.0367  0.0316  431 TYR   A CD2 
1177 C CE1 . TYR   A 145 ? 0.3329 0.3636 0.1681 0.0694  0.0374  0.0441  431 TYR   A CE1 
1178 C CE2 . TYR   A 145 ? 0.3530 0.3717 0.1473 0.0680  0.0465  0.0227  431 TYR   A CE2 
1179 C CZ  . TYR   A 145 ? 0.3458 0.3574 0.1467 0.0702  0.0446  0.0442  431 TYR   A CZ  
1180 O OH  . TYR   A 145 ? 0.4055 0.3726 0.2172 0.0758  0.0651  0.0725  431 TYR   A OH  
1181 N N   . SER   A 146 ? 0.3078 0.3683 0.1239 0.0856  0.0286  0.0245  432 SER   A N   
1182 C CA  . SER   A 146 ? 0.3527 0.3642 0.1396 0.0849  0.0314  0.0098  432 SER   A CA  
1183 C C   . SER   A 146 ? 0.3567 0.3392 0.1627 0.0983  0.0369  0.0031  432 SER   A C   
1184 O O   . SER   A 146 ? 0.3641 0.3594 0.2219 0.1021  0.0397  0.0239  432 SER   A O   
1185 C CB  . SER   A 146 ? 0.3730 0.4097 0.2113 0.0959  0.0552  -0.0222 432 SER   A CB  
1186 O OG  . SER   A 146 ? 0.4476 0.4970 0.2410 0.0971  0.0315  -0.0160 432 SER   A OG  
1187 N N   . PHE   A 147 ? 0.3661 0.3089 0.1536 0.1012  0.0226  -0.0016 433 PHE   A N   
1188 C CA  . PHE   A 147 ? 0.3834 0.3018 0.1275 0.1015  0.0245  0.0029  433 PHE   A CA  
1189 C C   . PHE   A 147 ? 0.4265 0.3197 0.1689 0.1090  0.0342  -0.0191 433 PHE   A C   
1190 O O   . PHE   A 147 ? 0.4655 0.3372 0.1401 0.1038  0.0242  -0.0434 433 PHE   A O   
1191 C CB  . PHE   A 147 ? 0.3790 0.2910 0.1437 0.0866  0.0212  0.0043  433 PHE   A CB  
1192 C CG  . PHE   A 147 ? 0.3548 0.2606 0.1491 0.0717  0.0346  0.0068  433 PHE   A CG  
1193 C CD1 . PHE   A 147 ? 0.3458 0.2602 0.1580 0.0601  0.0427  0.0217  433 PHE   A CD1 
1194 C CD2 . PHE   A 147 ? 0.3585 0.2542 0.1609 0.0672  0.0282  0.0093  433 PHE   A CD2 
1195 C CE1 . PHE   A 147 ? 0.3432 0.2510 0.1604 0.0657  0.0352  0.0169  433 PHE   A CE1 
1196 C CE2 . PHE   A 147 ? 0.3509 0.2606 0.1744 0.0739  0.0365  0.0090  433 PHE   A CE2 
1197 C CZ  . PHE   A 147 ? 0.3371 0.2461 0.1545 0.0637  0.0370  0.0133  433 PHE   A CZ  
1198 N N   . SER   A 148 ? 0.4536 0.3252 0.2165 0.1206  0.0244  -0.0255 434 SER   A N   
1199 C CA  . SER   A 148 ? 0.4824 0.3434 0.2528 0.1285  0.0078  -0.0510 434 SER   A CA  
1200 C C   . SER   A 148 ? 0.5198 0.3502 0.2930 0.1162  -0.0105 -0.0317 434 SER   A C   
1201 O O   . SER   A 148 ? 0.5545 0.3419 0.2942 0.1241  -0.0291 -0.0282 434 SER   A O   
1202 C CB  . SER   A 148 ? 0.4837 0.3845 0.3169 0.1128  0.0048  -0.0426 434 SER   A CB  
1203 O OG  . SER   A 148 ? 0.4989 0.4311 0.3725 0.1167  -0.0082 -0.0295 434 SER   A OG  
1204 N N   . GLU   A 149 ? 0.5583 0.3531 0.3370 0.1078  -0.0237 -0.0389 435 GLU   A N   
1205 C CA  . GLU   A 149 ? 0.5969 0.3660 0.3914 0.0942  -0.0288 -0.0260 435 GLU   A CA  
1206 C C   . GLU   A 149 ? 0.5982 0.3502 0.3196 0.0833  -0.0284 0.0034  435 GLU   A C   
1207 O O   . GLU   A 149 ? 0.6274 0.3343 0.3928 0.0579  -0.0416 0.0329  435 GLU   A O   
1208 C CB  . GLU   A 149 ? 0.6359 0.4088 0.4493 0.0982  -0.0498 -0.0146 435 GLU   A CB  
1209 C CG  . GLU   A 149 ? 0.6634 0.4316 0.5299 0.1101  -0.0559 -0.0084 435 GLU   A CG  
1210 C CD  . GLU   A 149 ? 0.7482 0.5013 0.5852 0.1057  -0.0816 0.0135  435 GLU   A CD  
1211 O OE1 . GLU   A 149 ? 0.7600 0.5035 0.6405 0.1448  -0.0795 0.0379  435 GLU   A OE1 
1212 O OE2 . GLU   A 149 ? 0.8253 0.5350 0.6196 0.0854  -0.0891 -0.0141 435 GLU   A OE2 
1213 N N   . CYS   A 150 ? 0.5633 0.3218 0.2923 0.0799  0.0053  -0.0048 436 CYS   A N   
1214 C CA  . CYS   A 150 ? 0.5544 0.3187 0.2690 0.0672  0.0127  -0.0011 436 CYS   A CA  
1215 C C   . CYS   A 150 ? 0.5635 0.3281 0.2807 0.0532  0.0196  0.0116  436 CYS   A C   
1216 O O   . CYS   A 150 ? 0.5736 0.3317 0.2481 0.0468  0.0369  0.0304  436 CYS   A O   
1217 C CB  . CYS   A 150 ? 0.5226 0.3151 0.2675 0.0784  0.0206  -0.0254 436 CYS   A CB  
1218 S SG  . CYS   A 150 ? 0.4984 0.3383 0.2112 0.0648  0.0277  -0.0413 436 CYS   A SG  
1219 N N   . ALA   A 151 ? 0.5828 0.3416 0.2877 0.0367  0.0138  0.0044  437 ALA   A N   
1220 C CA  . ALA   A 151 ? 0.5985 0.3739 0.3800 0.0258  0.0105  0.0084  437 ALA   A CA  
1221 C C   . ALA   A 151 ? 0.5979 0.3636 0.3779 0.0175  0.0086  0.0047  437 ALA   A C   
1222 O O   . ALA   A 151 ? 0.6172 0.3926 0.4030 0.0219  0.0279  0.0277  437 ALA   A O   
1223 C CB  . ALA   A 151 ? 0.6126 0.4033 0.4106 0.0201  0.0193  0.0286  437 ALA   A CB  
1224 N N   . PHE   A 152 ? 0.5570 0.3098 0.3265 0.0177  -0.0150 -0.0329 438 PHE   A N   
1225 C CA  . PHE   A 152 ? 0.5500 0.3107 0.3315 0.0240  0.0040  -0.0593 438 PHE   A CA  
1226 C C   . PHE   A 152 ? 0.5674 0.3323 0.3996 0.0106  -0.0086 -0.0784 438 PHE   A C   
1227 O O   . PHE   A 152 ? 0.5727 0.4193 0.4633 0.0369  -0.0040 -0.1180 438 PHE   A O   
1228 C CB  . PHE   A 152 ? 0.5123 0.3145 0.3028 0.0424  0.0130  -0.0495 438 PHE   A CB  
1229 C CG  . PHE   A 152 ? 0.4992 0.2790 0.2441 0.0554  0.0180  -0.0435 438 PHE   A CG  
1230 C CD1 . PHE   A 152 ? 0.4889 0.2905 0.2302 0.0550  0.0212  -0.0251 438 PHE   A CD1 
1231 C CD2 . PHE   A 152 ? 0.4906 0.2886 0.2434 0.0529  0.0142  -0.0485 438 PHE   A CD2 
1232 C CE1 . PHE   A 152 ? 0.4740 0.2849 0.2042 0.0546  0.0159  -0.0303 438 PHE   A CE1 
1233 C CE2 . PHE   A 152 ? 0.4793 0.2876 0.2527 0.0541  0.0168  -0.0267 438 PHE   A CE2 
1234 C CZ  . PHE   A 152 ? 0.4715 0.2929 0.2336 0.0482  -0.0002 -0.0224 438 PHE   A CZ  
1235 N N   . THR   A 153 ? 0.5849 0.3306 0.4193 -0.0188 -0.0029 -0.0811 439 THR   A N   
1236 C CA  . THR   A 153 ? 0.5965 0.3504 0.4663 -0.0272 -0.0243 -0.0712 439 THR   A CA  
1237 C C   . THR   A 153 ? 0.5629 0.3405 0.4385 -0.0389 -0.0309 -0.0962 439 THR   A C   
1238 O O   . THR   A 153 ? 0.5899 0.3949 0.4946 -0.0432 -0.0714 -0.1070 439 THR   A O   
1239 C CB  . THR   A 153 ? 0.6201 0.3426 0.4967 -0.0404 -0.0140 -0.0550 439 THR   A CB  
1240 O OG1 . THR   A 153 ? 0.6396 0.3966 0.5623 -0.0282 0.0241  -0.0342 439 THR   A OG1 
1241 C CG2 . THR   A 153 ? 0.6302 0.3685 0.5062 -0.0466 -0.0091 -0.0481 439 THR   A CG2 
1242 N N   . GLY   A 154 ? 0.5055 0.3279 0.3492 -0.0470 -0.0251 -0.0780 440 GLY   A N   
1243 C CA  . GLY   A 154 ? 0.4920 0.3075 0.2869 -0.0579 -0.0274 -0.0670 440 GLY   A CA  
1244 C C   . GLY   A 154 ? 0.4659 0.3088 0.2394 -0.0663 -0.0397 -0.0597 440 GLY   A C   
1245 O O   . GLY   A 154 ? 0.4682 0.3164 0.2228 -0.0701 -0.0329 -0.0600 440 GLY   A O   
1246 N N   . PRO   A 155 ? 0.4773 0.3237 0.2364 -0.0690 -0.0148 -0.0649 441 PRO   A N   
1247 C CA  . PRO   A 155 ? 0.4715 0.3077 0.2185 -0.0633 -0.0133 -0.0755 441 PRO   A CA  
1248 C C   . PRO   A 155 ? 0.4482 0.2894 0.1829 -0.0526 -0.0093 -0.0599 441 PRO   A C   
1249 O O   . PRO   A 155 ? 0.4492 0.3105 0.1886 -0.0652 -0.0041 -0.0499 441 PRO   A O   
1250 C CB  . PRO   A 155 ? 0.4800 0.3310 0.2203 -0.0655 -0.0286 -0.0683 441 PRO   A CB  
1251 C CG  . PRO   A 155 ? 0.4863 0.3550 0.2747 -0.0657 -0.0150 -0.0532 441 PRO   A CG  
1252 C CD  . PRO   A 155 ? 0.4776 0.3368 0.2531 -0.0698 -0.0153 -0.0505 441 PRO   A CD  
1253 N N   . LEU   A 156 ? 0.4249 0.2797 0.1601 -0.0252 -0.0043 -0.0476 442 LEU   A N   
1254 C CA  . LEU   A 156 ? 0.3981 0.2572 0.1415 -0.0202 0.0030  -0.0384 442 LEU   A CA  
1255 C C   . LEU   A 156 ? 0.3615 0.2600 0.1132 -0.0172 0.0009  -0.0281 442 LEU   A C   
1256 O O   . LEU   A 156 ? 0.3708 0.2509 0.1403 -0.0071 -0.0124 -0.0158 442 LEU   A O   
1257 C CB  . LEU   A 156 ? 0.3966 0.2697 0.1588 -0.0088 0.0059  -0.0290 442 LEU   A CB  
1258 C CG  . LEU   A 156 ? 0.4034 0.2811 0.1684 -0.0003 0.0059  -0.0191 442 LEU   A CG  
1259 C CD1 . LEU   A 156 ? 0.4109 0.2913 0.1813 -0.0011 0.0108  -0.0144 442 LEU   A CD1 
1260 C CD2 . LEU   A 156 ? 0.4183 0.3065 0.1811 0.0072  0.0142  -0.0015 442 LEU   A CD2 
1261 N N   . ARG   A 157 ? 0.3404 0.2616 0.1097 -0.0205 -0.0190 -0.0216 443 ARG   A N   
1262 C CA  . ARG   A 157 ? 0.3231 0.2574 0.0933 -0.0216 -0.0170 -0.0077 443 ARG   A CA  
1263 C C   . ARG   A 157 ? 0.3046 0.2549 0.0905 -0.0187 -0.0037 0.0010  443 ARG   A C   
1264 O O   . ARG   A 157 ? 0.3475 0.2506 0.0869 -0.0071 -0.0142 0.0123  443 ARG   A O   
1265 C CB  . ARG   A 157 ? 0.3163 0.2653 0.0991 -0.0204 -0.0159 -0.0031 443 ARG   A CB  
1266 C CG  . ARG   A 157 ? 0.3316 0.2802 0.1267 -0.0266 -0.0213 0.0077  443 ARG   A CG  
1267 C CD  . ARG   A 157 ? 0.3377 0.3016 0.1297 -0.0300 -0.0257 0.0019  443 ARG   A CD  
1268 N NE  . ARG   A 157 ? 0.3238 0.3015 0.1201 -0.0313 -0.0326 0.0290  443 ARG   A NE  
1269 C CZ  . ARG   A 157 ? 0.3154 0.3164 0.1233 -0.0342 -0.0357 0.0213  443 ARG   A CZ  
1270 N NH1 . ARG   A 157 ? 0.3218 0.3166 0.1387 -0.0358 -0.0014 0.0056  443 ARG   A NH1 
1271 N NH2 . ARG   A 157 ? 0.3188 0.3287 0.1346 -0.0431 -0.0343 0.0254  443 ARG   A NH2 
1272 N N   . PRO   A 158 ? 0.2968 0.2468 0.0837 -0.0153 -0.0140 0.0012  444 PRO   A N   
1273 C CA  . PRO   A 158 ? 0.2801 0.2455 0.0687 -0.0185 -0.0065 0.0033  444 PRO   A CA  
1274 C C   . PRO   A 158 ? 0.2684 0.2457 0.0688 -0.0110 -0.0082 0.0067  444 PRO   A C   
1275 O O   . PRO   A 158 ? 0.2798 0.2589 0.0745 -0.0121 0.0029  -0.0002 444 PRO   A O   
1276 C CB  . PRO   A 158 ? 0.2887 0.2446 0.0759 -0.0186 -0.0109 0.0022  444 PRO   A CB  
1277 C CG  . PRO   A 158 ? 0.3011 0.2570 0.0718 -0.0207 -0.0123 0.0035  444 PRO   A CG  
1278 C CD  . PRO   A 158 ? 0.3089 0.2537 0.0744 -0.0224 -0.0110 0.0060  444 PRO   A CD  
1279 N N   . PHE   A 159 ? 0.2503 0.2521 0.0664 -0.0053 -0.0038 0.0079  445 PHE   A N   
1280 C CA  . PHE   A 159 ? 0.2484 0.2465 0.0628 -0.0057 -0.0011 0.0160  445 PHE   A CA  
1281 C C   . PHE   A 159 ? 0.2404 0.2376 0.0538 -0.0023 -0.0002 0.0124  445 PHE   A C   
1282 O O   . PHE   A 159 ? 0.2475 0.2463 0.0530 -0.0016 0.0024  0.0050  445 PHE   A O   
1283 C CB  . PHE   A 159 ? 0.2543 0.2482 0.0753 0.0008  -0.0021 0.0105  445 PHE   A CB  
1284 C CG  . PHE   A 159 ? 0.2501 0.2560 0.0756 0.0017  0.0034  0.0203  445 PHE   A CG  
1285 C CD1 . PHE   A 159 ? 0.2499 0.2693 0.0743 -0.0060 -0.0027 0.0158  445 PHE   A CD1 
1286 C CD2 . PHE   A 159 ? 0.2528 0.2538 0.0702 0.0007  0.0024  0.0181  445 PHE   A CD2 
1287 C CE1 . PHE   A 159 ? 0.2633 0.2701 0.0789 -0.0041 0.0077  0.0225  445 PHE   A CE1 
1288 C CE2 . PHE   A 159 ? 0.2568 0.2680 0.0728 0.0055  0.0074  0.0278  445 PHE   A CE2 
1289 C CZ  . PHE   A 159 ? 0.2566 0.2737 0.0694 0.0046  0.0065  0.0282  445 PHE   A CZ  
1290 N N   . PHE   A 160 ? 0.2357 0.2331 0.0639 -0.0073 0.0045  0.0149  446 PHE   A N   
1291 C CA  . PHE   A 160 ? 0.2241 0.2289 0.0605 -0.0055 0.0046  0.0065  446 PHE   A CA  
1292 C C   . PHE   A 160 ? 0.2071 0.2287 0.0579 -0.0051 0.0034  0.0148  446 PHE   A C   
1293 O O   . PHE   A 160 ? 0.2059 0.2472 0.0772 -0.0136 -0.0083 0.0144  446 PHE   A O   
1294 C CB  . PHE   A 160 ? 0.2418 0.2304 0.0790 -0.0105 0.0029  0.0112  446 PHE   A CB  
1295 C CG  . PHE   A 160 ? 0.2383 0.2365 0.0763 -0.0209 -0.0063 0.0085  446 PHE   A CG  
1296 C CD1 . PHE   A 160 ? 0.2385 0.2397 0.0827 -0.0177 -0.0067 0.0055  446 PHE   A CD1 
1297 C CD2 . PHE   A 160 ? 0.2460 0.2580 0.0733 -0.0252 -0.0099 0.0087  446 PHE   A CD2 
1298 C CE1 . PHE   A 160 ? 0.2455 0.2404 0.0808 -0.0257 -0.0050 0.0067  446 PHE   A CE1 
1299 C CE2 . PHE   A 160 ? 0.2457 0.2478 0.0765 -0.0365 0.0039  0.0113  446 PHE   A CE2 
1300 C CZ  . PHE   A 160 ? 0.2449 0.2549 0.0653 -0.0263 -0.0098 0.0203  446 PHE   A CZ  
1301 N N   . SER   A 161 ? 0.2034 0.2222 0.0575 0.0061  0.0086  0.0037  447 SER   A N   
1302 C CA  . SER   A 161 ? 0.2206 0.2222 0.0557 0.0130  0.0137  0.0070  447 SER   A CA  
1303 C C   . SER   A 161 ? 0.2226 0.2271 0.0509 0.0145  0.0123  0.0142  447 SER   A C   
1304 O O   . SER   A 161 ? 0.2251 0.2335 0.0624 0.0242  0.0129  0.0062  447 SER   A O   
1305 C CB  . SER   A 161 ? 0.2196 0.2156 0.0574 0.0137  0.0119  0.0084  447 SER   A CB  
1306 O OG  . SER   A 161 ? 0.2355 0.2219 0.0503 0.0125  0.0231  0.0136  447 SER   A OG  
1307 N N   . PRO   A 162 ? 0.2411 0.2375 0.0633 0.0193  0.0176  0.0089  448 PRO   A N   
1308 C CA  . PRO   A 162 ? 0.2480 0.2452 0.0503 0.0151  0.0136  0.0049  448 PRO   A CA  
1309 C C   . PRO   A 162 ? 0.2564 0.2485 0.0535 0.0126  0.0047  0.0033  448 PRO   A C   
1310 O O   . PRO   A 162 ? 0.2770 0.2505 0.0587 0.0030  0.0243  0.0030  448 PRO   A O   
1311 C CB  . PRO   A 162 ? 0.2458 0.2446 0.0560 0.0153  0.0170  0.0101  448 PRO   A CB  
1312 C CG  . PRO   A 162 ? 0.2461 0.2405 0.0694 0.0167  0.0185  0.0106  448 PRO   A CG  
1313 C CD  . PRO   A 162 ? 0.2445 0.2344 0.0679 0.0189  0.0159  0.0161  448 PRO   A CD  
1314 N N   . GLY   A 163 ? 0.2731 0.2759 0.0423 0.0038  0.0029  0.0000  449 GLY   A N   
1315 C CA  . GLY   A 163 ? 0.2751 0.3002 0.0461 0.0055  -0.0028 -0.0004 449 GLY   A CA  
1316 C C   . GLY   A 163 ? 0.2828 0.3360 0.0682 0.0068  0.0055  -0.0092 449 GLY   A C   
1317 O O   . GLY   A 163 ? 0.3011 0.4140 0.0863 -0.0175 0.0087  -0.0097 449 GLY   A O   
1318 N N   . PHE   A 164 ? 0.3247 0.3634 0.0633 -0.0026 0.0083  0.0142  450 PHE   A N   
1319 C CA  . PHE   A 164 ? 0.3587 0.3880 0.0877 0.0121  0.0224  0.0155  450 PHE   A CA  
1320 C C   . PHE   A 164 ? 0.3945 0.3951 0.0875 0.0268  0.0358  0.0193  450 PHE   A C   
1321 O O   . PHE   A 164 ? 0.3964 0.4032 0.1138 0.0236  0.0461  0.0258  450 PHE   A O   
1322 C CB  . PHE   A 164 ? 0.4083 0.3889 0.0811 0.0135  0.0196  0.0109  450 PHE   A CB  
1323 C CG  . PHE   A 164 ? 0.4614 0.3889 0.1255 0.0208  0.0159  0.0066  450 PHE   A CG  
1324 C CD1 . PHE   A 164 ? 0.4773 0.3813 0.1570 0.0304  -0.0057 0.0095  450 PHE   A CD1 
1325 C CD2 . PHE   A 164 ? 0.4795 0.3784 0.1502 0.0314  0.0192  -0.0056 450 PHE   A CD2 
1326 C CE1 . PHE   A 164 ? 0.5038 0.3667 0.1898 0.0134  0.0055  0.0229  450 PHE   A CE1 
1327 C CE2 . PHE   A 164 ? 0.5112 0.3787 0.2092 0.0230  0.0191  0.0021  450 PHE   A CE2 
1328 C CZ  . PHE   A 164 ? 0.5104 0.3805 0.2125 0.0224  0.0134  0.0147  450 PHE   A CZ  
1329 N N   . ASN   A 165 ? 0.4078 0.4110 0.1576 0.0290  0.0387  0.0566  451 ASN   A N   
1330 C CA  . ASN   A 165 ? 0.4692 0.4248 0.1885 0.0318  0.0528  0.0351  451 ASN   A CA  
1331 C C   . ASN   A 165 ? 0.5001 0.4307 0.1936 0.0262  0.0509  0.0226  451 ASN   A C   
1332 O O   . ASN   A 165 ? 0.5434 0.4449 0.1625 0.0106  0.0584  0.0173  451 ASN   A O   
1333 C CB  . ASN   A 165 ? 0.4949 0.4528 0.2852 0.0333  0.0333  0.0206  451 ASN   A CB  
1334 C CG  . ASN   A 165 ? 0.5318 0.4865 0.3237 0.0238  0.0263  0.0273  451 ASN   A CG  
1335 O OD1 . ASN   A 165 ? 0.5770 0.4962 0.4294 0.0231  -0.0235 0.0180  451 ASN   A OD1 
1336 N ND2 . ASN   A 165 ? 0.5598 0.4991 0.3904 0.0284  0.0223  -0.0018 451 ASN   A ND2 
1337 N N   . ASP   A 166 ? 0.5346 0.4546 0.1883 0.0283  0.0562  0.0072  452 ASP   A N   
1338 C CA  . ASP   A 166 ? 0.5631 0.4747 0.2017 0.0345  0.0507  -0.0179 452 ASP   A CA  
1339 C C   . ASP   A 166 ? 0.5768 0.4761 0.2049 0.0283  0.0499  -0.0168 452 ASP   A C   
1340 O O   . ASP   A 166 ? 0.5830 0.4574 0.1517 0.0227  0.0193  -0.0108 452 ASP   A O   
1341 C CB  . ASP   A 166 ? 0.5707 0.4993 0.1710 0.0478  0.0504  -0.0232 452 ASP   A CB  
1342 C CG  . ASP   A 166 ? 0.5984 0.5252 0.1108 0.0617  0.0490  -0.0440 452 ASP   A CG  
1343 O OD1 . ASP   A 166 ? 0.6322 0.5769 0.1051 0.0629  0.0475  0.0212  452 ASP   A OD1 
1344 O OD2 . ASP   A 166 ? 0.5872 0.5051 0.1874 0.0552  0.0304  -0.0406 452 ASP   A OD2 
1345 N N   . GLY   A 167 ? 0.5836 0.4855 0.2413 0.0221  0.0596  -0.0251 453 GLY   A N   
1346 C CA  . GLY   A 167 ? 0.5787 0.4853 0.2343 0.0218  0.0586  -0.0328 453 GLY   A CA  
1347 C C   . GLY   A 167 ? 0.5822 0.4670 0.2384 0.0215  0.0336  -0.0454 453 GLY   A C   
1348 O O   . GLY   A 167 ? 0.5977 0.4768 0.2945 0.0181  0.0219  -0.0811 453 GLY   A O   
1349 N N   . GLY   A 168 ? 0.5439 0.4474 0.2116 0.0044  0.0075  -0.0272 454 GLY   A N   
1350 C CA  . GLY   A 168 ? 0.5361 0.4461 0.2020 0.0175  -0.0151 -0.0220 454 GLY   A CA  
1351 C C   . GLY   A 168 ? 0.5226 0.4224 0.1576 0.0336  -0.0192 -0.0272 454 GLY   A C   
1352 O O   . GLY   A 168 ? 0.5330 0.4392 0.2129 0.0400  -0.0234 0.0240  454 GLY   A O   
1353 N N   . LYS   A 169 ? 0.5095 0.3891 0.1064 0.0283  -0.0337 -0.0470 455 LYS   A N   
1354 C CA  . LYS   A 169 ? 0.4986 0.3804 0.1697 0.0365  -0.0446 -0.0400 455 LYS   A CA  
1355 C C   . LYS   A 169 ? 0.4446 0.3651 0.1822 0.0426  -0.0536 -0.0351 455 LYS   A C   
1356 O O   . LYS   A 169 ? 0.4454 0.4072 0.1953 0.0545  -0.0403 -0.0101 455 LYS   A O   
1357 C CB  . LYS   A 169 ? 0.5248 0.4105 0.2313 0.0488  -0.0545 -0.0206 455 LYS   A CB  
1358 C CG  . LYS   A 169 ? 0.5694 0.4550 0.2903 0.0330  -0.0453 -0.0670 455 LYS   A CG  
1359 C CD  . LYS   A 169 ? 0.6085 0.5092 0.3641 0.0085  -0.0314 -0.0338 455 LYS   A CD  
1360 C CE  . LYS   A 169 ? 0.6065 0.5416 0.4661 0.0172  -0.0148 -0.0875 455 LYS   A CE  
1361 N NZ  . LYS   A 169 ? 0.6149 0.5801 0.5155 -0.0063 0.0142  -0.1126 455 LYS   A NZ  
1362 N N   . ASN   A 170 ? 0.3961 0.2970 0.1254 0.0613  -0.0629 -0.0457 456 ASN   A N   
1363 C CA  . ASN   A 170 ? 0.3581 0.2916 0.0871 0.0364  -0.0229 -0.0198 456 ASN   A CA  
1364 C C   . ASN   A 170 ? 0.3289 0.2703 0.0898 0.0202  -0.0096 0.0016  456 ASN   A C   
1365 O O   . ASN   A 170 ? 0.3251 0.2491 0.0861 0.0099  0.0070  0.0169  456 ASN   A O   
1366 C CB  . ASN   A 170 ? 0.3641 0.2936 0.0589 0.0297  -0.0036 -0.0191 456 ASN   A CB  
1367 C CG  . ASN   A 170 ? 0.3316 0.2855 0.0509 0.0173  0.0006  -0.0167 456 ASN   A CG  
1368 O OD1 . ASN   A 170 ? 0.3345 0.2816 0.0656 0.0050  -0.0021 -0.0129 456 ASN   A OD1 
1369 N ND2 . ASN   A 170 ? 0.3250 0.2958 0.0557 0.0171  0.0161  -0.0023 456 ASN   A ND2 
1370 N N   . THR   A 171 ? 0.2870 0.2626 0.0737 0.0181  0.0083  -0.0122 457 THR   A N   
1371 C CA  . THR   A 171 ? 0.2668 0.2664 0.0669 0.0075  0.0219  0.0017  457 THR   A CA  
1372 C C   . THR   A 171 ? 0.2499 0.2541 0.0625 0.0040  0.0137  -0.0021 457 THR   A C   
1373 O O   . THR   A 171 ? 0.2582 0.2661 0.0717 -0.0007 0.0094  0.0108  457 THR   A O   
1374 C CB  . THR   A 171 ? 0.2662 0.2798 0.0838 0.0044  0.0382  0.0087  457 THR   A CB  
1375 O OG1 . THR   A 171 ? 0.3013 0.2865 0.1053 -0.0034 0.0355  -0.0134 457 THR   A OG1 
1376 C CG2 . THR   A 171 ? 0.2704 0.2858 0.0868 0.0021  0.0468  0.0079  457 THR   A CG2 
1377 N N   . ALA   A 172 ? 0.2526 0.2530 0.0538 -0.0011 0.0119  0.0133  458 ALA   A N   
1378 C CA  . ALA   A 172 ? 0.2558 0.2498 0.0555 -0.0045 0.0108  0.0143  458 ALA   A CA  
1379 C C   . ALA   A 172 ? 0.2571 0.2439 0.0494 0.0012  0.0119  0.0117  458 ALA   A C   
1380 O O   . ALA   A 172 ? 0.2628 0.2463 0.0463 -0.0082 0.0138  0.0071  458 ALA   A O   
1381 C CB  . ALA   A 172 ? 0.2610 0.2628 0.0836 -0.0093 0.0049  0.0192  458 ALA   A CB  
1382 N N   . PRO   A 173 ? 0.2696 0.2572 0.0509 -0.0034 0.0091  0.0163  459 PRO   A N   
1383 C CA  . PRO   A 173 ? 0.2647 0.2567 0.0479 -0.0080 0.0123  0.0172  459 PRO   A CA  
1384 C C   . PRO   A 173 ? 0.2573 0.2616 0.0517 -0.0085 0.0205  0.0173  459 PRO   A C   
1385 O O   . PRO   A 173 ? 0.2677 0.2666 0.0418 -0.0104 0.0179  -0.0028 459 PRO   A O   
1386 C CB  . PRO   A 173 ? 0.2669 0.2699 0.0554 0.0040  0.0038  0.0170  459 PRO   A CB  
1387 C CG  . PRO   A 173 ? 0.2758 0.2703 0.0637 0.0011  0.0027  0.0272  459 PRO   A CG  
1388 C CD  . PRO   A 173 ? 0.2669 0.2582 0.0746 -0.0089 0.0039  0.0122  459 PRO   A CD  
1389 N N   . LEU   A 174 ? 0.2514 0.2675 0.0426 -0.0149 0.0248  0.0200  460 LEU   A N   
1390 C CA  . LEU   A 174 ? 0.2551 0.2663 0.0589 -0.0142 0.0113  0.0205  460 LEU   A CA  
1391 C C   . LEU   A 174 ? 0.2393 0.2626 0.0551 -0.0125 0.0063  0.0022  460 LEU   A C   
1392 O O   . LEU   A 174 ? 0.2339 0.2849 0.0533 -0.0086 0.0120  -0.0019 460 LEU   A O   
1393 C CB  . LEU   A 174 ? 0.2881 0.2931 0.1121 -0.0411 0.0170  0.0224  460 LEU   A CB  
1394 C CG  . LEU   A 174 ? 0.3111 0.3281 0.1140 -0.0415 0.0267  0.0418  460 LEU   A CG  
1395 C CD1 . LEU   A 174 ? 0.3147 0.3235 0.0674 -0.0371 0.0339  0.0489  460 LEU   A CD1 
1396 C CD2 . LEU   A 174 ? 0.3037 0.3247 0.1183 -0.0347 0.0222  0.0432  460 LEU   A CD2 
1397 N N   . THR   A 175 ? 0.2335 0.2403 0.0417 -0.0042 0.0006  0.0034  461 THR   A N   
1398 C CA  . THR   A 175 ? 0.2435 0.2498 0.0440 0.0007  -0.0086 -0.0032 461 THR   A CA  
1399 C C   . THR   A 175 ? 0.2371 0.2492 0.0381 -0.0004 -0.0007 0.0069  461 THR   A C   
1400 O O   . THR   A 175 ? 0.2517 0.2651 0.0370 0.0104  0.0168  0.0082  461 THR   A O   
1401 C CB  . THR   A 175 ? 0.2652 0.2568 0.0470 0.0037  -0.0042 0.0035  461 THR   A CB  
1402 O OG1 . THR   A 175 ? 0.2834 0.2522 0.0796 0.0098  0.0022  -0.0105 461 THR   A OG1 
1403 C CG2 . THR   A 175 ? 0.2806 0.2827 0.0634 0.0028  -0.0114 0.0123  461 THR   A CG2 
1404 N N   . LEU   A 176 ? 0.2323 0.2507 0.0527 0.0024  0.0016  -0.0006 462 LEU   A N   
1405 C CA  . LEU   A 176 ? 0.2509 0.2461 0.0462 -0.0004 0.0092  0.0087  462 LEU   A CA  
1406 C C   . LEU   A 176 ? 0.2756 0.2509 0.0664 0.0018  0.0130  0.0193  462 LEU   A C   
1407 O O   . LEU   A 176 ? 0.3128 0.2680 0.0933 0.0121  0.0236  0.0402  462 LEU   A O   
1408 C CB  . LEU   A 176 ? 0.2512 0.2573 0.0446 -0.0006 0.0024  -0.0002 462 LEU   A CB  
1409 C CG  . LEU   A 176 ? 0.2548 0.2544 0.0664 -0.0001 -0.0018 0.0004  462 LEU   A CG  
1410 C CD1 . LEU   A 176 ? 0.2634 0.2625 0.1038 -0.0031 0.0001  0.0018  462 LEU   A CD1 
1411 C CD2 . LEU   A 176 ? 0.2647 0.2579 0.0520 0.0022  -0.0025 0.0009  462 LEU   A CD2 
1412 N N   . CYS   A 177 ? 0.2819 0.2581 0.0803 -0.0062 0.0177  0.0252  463 CYS   A N   
1413 C CA  . CYS   A 177 ? 0.3065 0.2815 0.0831 -0.0323 0.0269  0.0180  463 CYS   A CA  
1414 C C   . CYS   A 177 ? 0.3609 0.3132 0.0815 -0.0335 0.0114  0.0209  463 CYS   A C   
1415 O O   . CYS   A 177 ? 0.3689 0.3185 0.0641 -0.0390 0.0276  0.0189  463 CYS   A O   
1416 C CB  . CYS   A 177 ? 0.3270 0.2866 0.1010 -0.0411 -0.0017 0.0130  463 CYS   A CB  
1417 S SG  . CYS   A 177 ? 0.3327 0.3285 0.1133 -0.0472 -0.0056 -0.0025 463 CYS   A SG  
1418 N N   . PRO   A 178 ? 0.3811 0.3467 0.0842 -0.0366 -0.0041 0.0246  464 PRO   A N   
1419 C CA  . PRO   A 178 ? 0.4359 0.3738 0.0794 -0.0367 -0.0052 0.0272  464 PRO   A CA  
1420 C C   . PRO   A 178 ? 0.4933 0.4212 0.1087 -0.0071 0.0307  0.0120  464 PRO   A C   
1421 O O   . PRO   A 178 ? 0.5929 0.5245 0.1813 -0.0376 -0.0365 -0.0253 464 PRO   A O   
1422 C CB  . PRO   A 178 ? 0.4125 0.3802 0.0809 -0.0304 -0.0189 0.0349  464 PRO   A CB  
1423 C CG  . PRO   A 178 ? 0.4188 0.3515 0.1022 -0.0284 -0.0121 0.0506  464 PRO   A CG  
1424 C CD  . PRO   A 178 ? 0.3989 0.3459 0.0897 -0.0267 -0.0228 0.0354  464 PRO   A CD  
1425 C C2  . A1I41 B .   ? 0.3033 0.2918 0.1015 0.0421  0.0505  0.0461  501 A1I41 A C2  
1426 C C6  . A1I41 B .   ? 0.3762 0.3392 0.1733 0.0638  0.0778  0.0953  501 A1I41 A C6  
1427 C C9  . A1I41 B .   ? 0.3945 0.3343 0.2193 0.0798  0.0831  0.1052  501 A1I41 A C9  
1428 C C12 . A1I41 B .   ? 0.2991 0.2735 0.0902 0.0337  0.0418  0.0424  501 A1I41 A C12 
1429 C C15 . A1I41 B .   ? 0.3297 0.2815 0.1456 0.0166  0.0809  0.0868  501 A1I41 A C15 
1430 C C18 . A1I41 B .   ? 0.2636 0.2710 0.0802 0.0234  0.0220  0.0285  501 A1I41 A C18 
1431 C C21 . A1I41 B .   ? 0.2493 0.2648 0.0802 0.0075  0.0246  0.0171  501 A1I41 A C21 
1432 C C27 . A1I41 B .   ? 0.2599 0.3158 0.1540 0.0082  0.0080  0.0767  501 A1I41 A C27 
1433 C C29 . A1I41 B .   ? 0.2744 0.2840 0.0875 0.0351  0.0388  0.0284  501 A1I41 A C29 
1434 O O1  . A1I41 B .   ? 0.3116 0.2908 0.1071 0.0389  0.0471  0.0517  501 A1I41 A O1  
1435 N N3  . A1I41 B .   ? 0.3304 0.3165 0.1179 0.0614  0.0441  0.0508  501 A1I41 A N3  
1436 C C4  . A1I41 B .   ? 0.3572 0.3298 0.1349 0.0667  0.0623  0.0772  501 A1I41 A C4  
1437 C C5  . A1I41 B .   ? 0.3638 0.3306 0.1636 0.0786  0.0735  0.0921  501 A1I41 A C5  
1438 C C7  . A1I41 B .   ? 0.3751 0.3368 0.1907 0.0666  0.0841  0.1017  501 A1I41 A C7  
1439 C C8  . A1I41 B .   ? 0.3817 0.3432 0.2311 0.0741  0.0802  0.0976  501 A1I41 A C8  
1440 C C10 . A1I41 B .   ? 0.3885 0.3429 0.1926 0.0855  0.0742  0.1048  501 A1I41 A C10 
1441 C C11 . A1I41 B .   ? 0.2879 0.2856 0.0968 0.0339  0.0343  0.0388  501 A1I41 A C11 
1442 S S13 . A1I41 B .   ? 0.3496 0.2881 0.1340 0.0354  0.0800  0.0563  501 A1I41 A S13 
1443 O O14 . A1I41 B .   ? 0.4002 0.3070 0.1292 0.0639  0.0779  0.0572  501 A1I41 A O14 
1444 O O16 . A1I41 B .   ? 0.3709 0.2732 0.1574 0.0341  0.0775  0.0617  501 A1I41 A O16 
1445 C C17 . A1I41 B .   ? 0.2798 0.2658 0.0843 0.0273  0.0348  0.0293  501 A1I41 A C17 
1446 C C19 . A1I41 B .   ? 0.2532 0.2710 0.0783 0.0178  0.0212  0.0274  501 A1I41 A C19 
1447 C C20 . A1I41 B .   ? 0.2518 0.2728 0.0773 0.0172  0.0260  0.0164  501 A1I41 A C20 
1448 C C22 . A1I41 B .   ? 0.2516 0.2735 0.0919 0.0116  0.0272  0.0223  501 A1I41 A C22 
1449 F F23 . A1I41 B .   ? 0.2717 0.2703 0.1217 0.0006  0.0298  0.0279  501 A1I41 A F23 
1450 C C24 . A1I41 B .   ? 0.2494 0.2772 0.0993 0.0110  0.0230  0.0349  501 A1I41 A C24 
1451 C C25 . A1I41 B .   ? 0.2487 0.2880 0.1090 0.0198  0.0287  0.0298  501 A1I41 A C25 
1452 S S26 . A1I41 B .   ? 0.2671 0.3207 0.1818 0.0022  0.0123  0.0407  501 A1I41 A S26 
1453 C C28 . A1I41 B .   ? 0.2654 0.2792 0.0848 0.0266  0.0328  0.0313  501 A1I41 A C28 
1454 C C1  . EDO   C .   ? 0.3989 0.4471 0.3224 -0.0268 -0.1025 -0.0823 502 EDO   A C1  
1455 O O1  . EDO   C .   ? 0.4307 0.4748 0.3137 -0.0312 -0.0947 -0.0922 502 EDO   A O1  
1456 C C2  . EDO   C .   ? 0.3835 0.4339 0.3593 -0.0170 -0.0904 -0.0689 502 EDO   A C2  
1457 O O2  . EDO   C .   ? 0.3675 0.4457 0.4550 -0.0218 -0.1090 -0.1062 502 EDO   A O2  
1458 C C1  . EDO   D .   ? 0.5049 0.7859 0.3684 0.0961  -0.0841 -0.1349 503 EDO   A C1  
1459 O O1  . EDO   D .   ? 0.4970 0.7599 0.3748 0.1105  -0.0816 -0.1606 503 EDO   A O1  
1460 C C2  . EDO   D .   ? 0.4816 0.7939 0.3365 0.1152  -0.0736 -0.1231 503 EDO   A C2  
1461 O O2  . EDO   D .   ? 0.4914 0.8117 0.3210 0.1176  -0.0877 -0.1233 503 EDO   A O2  
1462 O O   . HOH   E .   ? 0.5690 0.5084 0.6037 -0.2440 0.0743  -0.0612 601 HOH   A O   
1463 O O   . HOH   E .   ? 0.7232 0.3921 0.2058 -0.0936 -0.0145 -0.0941 602 HOH   A O   
1464 O O   . HOH   E .   ? 0.4524 0.5970 0.3332 -0.0405 0.0600  0.0045  603 HOH   A O   
1465 O O   . HOH   E .   ? 0.6318 0.5220 0.3548 0.0343  0.0667  -0.0283 604 HOH   A O   
1466 O O   . HOH   E .   ? 0.4097 0.3783 0.0894 -0.0295 0.0782  -0.0078 605 HOH   A O   
1467 O O   . HOH   E .   ? 0.3816 0.5956 0.3460 0.0449  0.1212  0.2718  606 HOH   A O   
1468 O O   . HOH   E .   ? 0.3121 0.3112 0.1248 0.0265  0.0434  0.0375  607 HOH   A O   
1469 O O   . HOH   E .   ? 0.4999 0.5265 0.4064 0.0071  0.0014  0.0092  608 HOH   A O   
1470 O O   . HOH   E .   ? 0.5244 0.6123 0.3361 0.0458  0.0422  0.1760  609 HOH   A O   
1471 O O   . HOH   E .   ? 0.3848 0.4203 0.1462 -0.0566 0.0101  0.0844  610 HOH   A O   
1472 O O   . HOH   E .   ? 0.5041 0.4561 0.3798 0.0674  -0.1199 -0.1453 611 HOH   A O   
1473 O O   . HOH   E .   ? 0.4329 0.5373 0.3812 -0.0147 0.0239  -0.0510 612 HOH   A O   
1474 O O   . HOH   E .   ? 0.3471 0.5992 0.3588 -0.0094 -0.1253 -0.0556 613 HOH   A O   
1475 O O   . HOH   E .   ? 0.2996 0.2504 0.0791 -0.0040 0.0103  -0.0031 614 HOH   A O   
1476 O O   . HOH   E .   ? 0.3322 0.3869 0.3183 -0.0623 0.0015  -0.0243 615 HOH   A O   
1477 O O   . HOH   E .   ? 0.4208 0.4227 0.2325 0.0559  0.0503  -0.0513 616 HOH   A O   
1478 O O   . HOH   E .   ? 0.5238 0.3646 0.1774 -0.1158 0.0056  -0.0089 617 HOH   A O   
1479 O O   . HOH   E .   ? 0.5654 0.5485 0.2964 -0.1549 -0.0357 0.1845  618 HOH   A O   
1480 O O   . HOH   E .   ? 0.3632 0.8943 0.8220 0.0487  -0.1450 0.0965  619 HOH   A O   
1481 O O   . HOH   E .   ? 0.3972 0.3931 0.1306 -0.0078 0.0260  0.0393  620 HOH   A O   
1482 O O   . HOH   E .   ? 0.3612 0.4710 0.2211 0.0832  0.0420  0.1110  621 HOH   A O   
1483 O O   . HOH   E .   ? 0.2618 0.3159 0.0585 0.0104  0.0041  0.0087  622 HOH   A O   
1484 O O   . HOH   E .   ? 0.3114 0.3188 0.1169 0.0010  -0.0282 0.0046  623 HOH   A O   
1485 O O   . HOH   E .   ? 0.6186 0.6792 0.3307 0.0162  0.1808  -0.0562 624 HOH   A O   
1486 O O   . HOH   E .   ? 0.3259 0.3816 0.2306 0.0211  0.0215  0.0256  625 HOH   A O   
1487 O O   . HOH   E .   ? 0.4342 0.6562 0.3359 0.0746  -0.0620 0.0588  626 HOH   A O   
1488 O O   . HOH   E .   ? 0.2656 0.3128 0.0790 -0.0029 0.0168  0.0098  627 HOH   A O   
1489 O O   . HOH   E .   ? 0.4182 0.5271 0.4999 -0.0341 0.0527  -0.0306 628 HOH   A O   
1490 O O   . HOH   E .   ? 0.6534 0.3899 0.1932 -0.0771 0.0269  0.0049  629 HOH   A O   
1491 O O   . HOH   E .   ? 0.3472 0.2957 0.1110 0.0447  0.0155  0.0482  630 HOH   A O   
1492 O O   . HOH   E .   ? 0.4520 0.3384 0.2545 0.0158  0.0059  0.0291  631 HOH   A O   
1493 O O   . HOH   E .   ? 0.5291 0.4666 0.3684 -0.0050 0.0897  0.0406  632 HOH   A O   
1494 O O   . HOH   E .   ? 0.4715 1.0448 0.2099 0.1850  0.0020  0.0310  633 HOH   A O   
1495 O O   . HOH   E .   ? 0.4228 0.3854 0.1646 -0.0137 0.0094  -0.0445 634 HOH   A O   
1496 O O   . HOH   E .   ? 0.3972 0.6048 0.5159 -0.0567 -0.0674 -0.1202 635 HOH   A O   
1497 O O   . HOH   E .   ? 0.5647 0.4949 0.1952 -0.0693 0.0557  0.0297  636 HOH   A O   
1498 O O   . HOH   E .   ? 0.2725 0.2487 0.0683 0.0002  0.0049  -0.0079 637 HOH   A O   
1499 O O   . HOH   E .   ? 0.8038 0.3713 0.1030 0.0378  -0.1303 -0.0351 638 HOH   A O   
1500 O O   . HOH   E .   ? 0.5386 0.4598 0.3811 0.0559  -0.0273 -0.1111 639 HOH   A O   
1501 O O   . HOH   E .   ? 0.3656 0.3290 0.1745 0.0085  0.1253  0.0489  640 HOH   A O   
1502 O O   . HOH   E .   ? 0.3694 0.3329 0.1548 -0.0101 -0.1148 0.0094  641 HOH   A O   
1503 O O   . HOH   E .   ? 0.7542 0.4732 0.4214 0.2417  0.1490  0.0672  642 HOH   A O   
1504 O O   . HOH   E .   ? 0.3939 0.6000 0.2852 -0.0728 -0.0505 0.0312  643 HOH   A O   
1505 O O   . HOH   E .   ? 0.3902 0.6318 0.2899 -0.0316 0.0640  -0.0480 644 HOH   A O   
1506 O O   . HOH   E .   ? 0.4637 0.3371 0.1793 0.0586  -0.0001 0.0002  645 HOH   A O   
1507 O O   . HOH   E .   ? 0.6488 0.4682 0.6267 0.0294  -0.0265 -0.2293 646 HOH   A O   
1508 O O   . HOH   E .   ? 0.5165 0.3911 0.3604 -0.0264 0.0105  0.0328  647 HOH   A O   
1509 O O   . HOH   E .   ? 0.6780 0.4402 0.2321 0.0637  -0.1344 -0.0587 648 HOH   A O   
1510 O O   . HOH   E .   ? 0.3413 0.3763 0.1081 -0.0196 0.0155  0.0377  649 HOH   A O   
1511 O O   . HOH   E .   ? 0.4069 0.6917 0.3527 0.1860  0.0042  0.0335  650 HOH   A O   
1512 O O   . HOH   E .   ? 0.5829 0.4079 0.4207 -0.0008 0.0585  -0.0040 651 HOH   A O   
1513 O O   . HOH   E .   ? 0.4984 0.4425 0.5591 -0.0187 -0.1075 -0.1444 652 HOH   A O   
1514 O O   . HOH   E .   ? 0.4306 0.5436 0.4244 0.0219  0.0317  0.1569  653 HOH   A O   
1515 O O   . HOH   E .   ? 0.2910 0.5206 0.1899 0.0874  0.0420  0.0419  654 HOH   A O   
1516 O O   . HOH   E .   ? 0.3063 0.3180 0.0743 0.0142  0.0202  0.0242  655 HOH   A O   
1517 O O   . HOH   E .   ? 0.2990 0.2959 0.0639 -0.0047 -0.0036 0.0061  656 HOH   A O   
1518 O O   . HOH   E .   ? 0.4021 0.4799 0.3282 -0.0850 0.0571  0.0630  657 HOH   A O   
1519 O O   . HOH   E .   ? 0.3525 0.6439 0.4018 0.0556  -0.0088 0.2353  658 HOH   A O   
1520 O O   . HOH   E .   ? 0.3370 0.3833 0.2591 0.0108  0.0270  0.1111  659 HOH   A O   
1521 O O   . HOH   E .   ? 0.2820 0.2265 0.0872 0.0017  0.0013  0.0249  660 HOH   A O   
1522 O O   . HOH   E .   ? 1.2566 0.6222 0.2622 0.5687  0.1341  0.0628  661 HOH   A O   
1523 O O   . HOH   E .   ? 0.7847 0.6083 0.3590 0.1432  -0.0061 -0.1502 662 HOH   A O   
1524 O O   . HOH   E .   ? 0.3305 0.2540 0.1885 -0.0381 0.0324  -0.0057 663 HOH   A O   
1525 O O   . HOH   E .   ? 0.4609 0.5212 0.4293 0.0078  -0.1402 0.0357  664 HOH   A O   
1526 O O   . HOH   E .   ? 0.6856 0.4584 0.5830 -0.0338 -0.1711 -0.0465 665 HOH   A O   
1527 O O   . HOH   E .   ? 0.4533 0.5189 0.4493 0.0392  -0.0750 -0.0009 666 HOH   A O   
1528 O O   . HOH   E .   ? 0.4422 0.3970 0.2883 0.0001  0.1305  -0.0297 667 HOH   A O   
1529 O O   . HOH   E .   ? 0.2751 0.3992 0.1165 -0.0260 -0.0122 0.0121  668 HOH   A O   
1530 O O   . HOH   E .   ? 0.3376 0.2973 0.1030 0.0223  0.0131  0.0565  669 HOH   A O   
1531 O O   . HOH   E .   ? 0.3483 0.6119 0.2142 0.0242  0.0125  0.0051  670 HOH   A O   
1532 O O   . HOH   E .   ? 0.5223 0.6838 0.4418 -0.0383 0.0351  0.2128  671 HOH   A O   
1533 O O   . HOH   E .   ? 0.5692 0.7474 0.2341 -0.0800 -0.0964 -0.0239 672 HOH   A O   
1534 O O   . HOH   E .   ? 0.4804 0.3975 0.2149 0.0626  0.0922  0.0408  673 HOH   A O   
1535 O O   . HOH   E .   ? 0.4008 0.5003 0.7969 -0.0153 -0.0354 0.0916  674 HOH   A O   
1536 O O   . HOH   E .   ? 0.5741 0.4281 0.2968 -0.0211 -0.0860 0.0665  675 HOH   A O   
1537 O O   . HOH   E .   ? 0.4359 0.5308 0.9774 -0.0389 -0.1472 -0.0995 676 HOH   A O   
1538 O O   . HOH   E .   ? 0.3803 0.5418 0.7354 0.1220  0.2900  0.0629  677 HOH   A O   
1539 O O   . HOH   E .   ? 0.4259 0.6661 0.2398 0.0333  -0.0826 0.0000  678 HOH   A O   
1540 O O   . HOH   E .   ? 0.2660 0.4250 0.1357 -0.0057 0.0288  0.0749  679 HOH   A O   
1541 O O   . HOH   E .   ? 0.6123 0.6135 0.1479 0.0850  -0.0145 0.0664  680 HOH   A O   
1542 O O   . HOH   E .   ? 0.4259 0.5030 0.4940 -0.0062 0.0427  0.0381  681 HOH   A O   
1543 O O   . HOH   E .   ? 0.3431 0.5658 0.2115 0.1513  0.0306  0.0669  682 HOH   A O   
1544 O O   . HOH   E .   ? 0.5253 0.6815 0.6810 0.0897  -0.2923 -0.0401 683 HOH   A O   
1545 O O   . HOH   E .   ? 0.7727 0.5104 0.1302 -0.0613 0.0207  -0.0461 684 HOH   A O   
1546 O O   . HOH   E .   ? 0.4324 0.4356 0.2206 0.1048  0.0101  -0.0601 685 HOH   A O   
1547 O O   . HOH   E .   ? 0.6180 0.4013 0.4524 0.1253  0.1165  -0.0874 686 HOH   A O   
1548 O O   . HOH   E .   ? 0.8086 0.5288 0.2378 0.1157  -0.2472 -0.0962 687 HOH   A O   
1549 O O   . HOH   E .   ? 0.4708 0.6483 0.1659 0.1144  0.0076  0.1204  688 HOH   A O   
1550 O O   . HOH   E .   ? 0.5081 0.6110 0.1399 0.1943  0.0339  0.0344  689 HOH   A O   
1551 O O   . HOH   E .   ? 0.4166 0.4701 0.1539 0.1422  -0.1327 -0.0165 690 HOH   A O   
1552 O O   . HOH   E .   ? 0.4497 0.8526 0.1931 -0.0886 0.0407  -0.1483 691 HOH   A O   
1553 O O   . HOH   E .   ? 0.3660 0.3423 0.2524 -0.0913 -0.0111 0.0877  692 HOH   A O   
1554 O O   . HOH   E .   ? 0.5587 0.3645 0.4201 -0.0854 0.0034  -0.0709 693 HOH   A O   
1555 O O   . HOH   E .   ? 0.4638 0.2060 0.1658 -0.0006 0.0362  -0.0284 694 HOH   A O   
1556 O O   . HOH   E .   ? 0.3438 0.2275 0.0528 0.0374  -0.0113 0.0212  695 HOH   A O   
1557 O O   . HOH   E .   ? 0.2219 0.3001 0.0074 -0.0530 -0.0141 -0.0036 696 HOH   A O   
1558 O O   . HOH   E .   ? 0.6315 0.5844 0.0880 0.1587  0.0088  0.0406  697 HOH   A O   
1559 O O   . HOH   E .   ? 0.3079 0.4902 0.3885 -0.0221 -0.0399 -0.0294 698 HOH   A O   
1560 O O   . HOH   E .   ? 0.2151 0.2626 0.0568 -0.0094 -0.0190 -0.0714 699 HOH   A O   
1561 O O   . HOH   E .   ? 0.4569 0.6565 0.3607 -0.0727 -0.0738 0.2909  700 HOH   A O   
1562 O O   . HOH   E .   ? 0.5574 0.6215 0.2099 -0.2344 0.1761  -0.0479 701 HOH   A O   
1563 O O   . HOH   E .   ? 0.9331 0.3565 0.2886 0.1151  -0.0666 -0.0746 702 HOH   A O   
1564 O O   . HOH   E .   ? 0.8045 0.6752 0.2664 0.0072  0.0289  0.1759  703 HOH   A O   
1565 O O   . HOH   E .   ? 0.3354 0.2447 0.0752 0.0215  -0.0109 0.0099  704 HOH   A O   
1566 O O   . HOH   E .   ? 0.6373 0.3529 0.6969 0.1247  -0.2611 0.0670  705 HOH   A O   
1567 O O   . HOH   E .   ? 0.4216 0.5549 0.2929 -0.1206 -0.0853 0.0149  706 HOH   A O   
1568 O O   . HOH   E .   ? 0.6703 0.4674 0.1393 0.1780  0.1203  0.0448  707 HOH   A O   
1569 O O   . HOH   E .   ? 0.3174 0.2703 0.0958 -0.0280 0.0107  -0.0068 708 HOH   A O   
1570 O O   . HOH   E .   ? 0.7787 0.8133 0.5282 -0.0360 0.3195  0.2073  709 HOH   A O   
1571 O O   . HOH   E .   ? 0.3422 0.3541 0.2320 0.0085  0.0754  0.0537  710 HOH   A O   
1572 O O   . HOH   E .   ? 0.5672 0.5404 0.3817 0.0954  0.0430  -0.0589 711 HOH   A O   
1573 O O   . HOH   E .   ? 0.4627 0.4431 0.2358 0.0857  0.1169  0.0545  712 HOH   A O   
1574 O O   . HOH   E .   ? 0.2557 0.2971 0.0490 -0.0068 0.1029  0.0044  713 HOH   A O   
1575 O O   . HOH   E .   ? 0.4390 0.5277 0.3983 0.0603  0.1041  -0.0788 714 HOH   A O   
1576 O O   . HOH   E .   ? 0.4719 0.4684 0.3372 0.0571  0.0340  -0.0199 715 HOH   A O   
1577 O O   . HOH   E .   ? 0.3916 0.4203 0.1847 0.0531  0.0919  0.1218  716 HOH   A O   
1578 O O   . HOH   E .   ? 0.6976 0.5021 0.5789 0.1366  0.0883  -0.1033 717 HOH   A O   
1579 O O   . HOH   E .   ? 0.4620 0.4975 0.3466 0.0832  -0.0693 -0.0662 718 HOH   A O   
1580 O O   . HOH   E .   ? 0.4773 0.4576 0.3229 0.0394  -0.0547 -0.0013 719 HOH   A O   
1581 O O   . HOH   E .   ? 0.4630 0.6837 0.3084 0.0905  0.0241  0.0102  720 HOH   A O   
1582 O O   . HOH   E .   ? 0.3965 0.5394 0.4845 0.0821  0.1229  0.0753  721 HOH   A O   
1583 O O   . HOH   E .   ? 0.4645 0.5033 0.2802 -0.0984 0.0418  -0.0202 722 HOH   A O   
1584 O O   . HOH   E .   ? 0.5375 0.4160 0.3116 0.0345  0.0750  0.0048  723 HOH   A O   
# 
