data_9R73
# 
_entry.id   9R73 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9R73         pdb_00009r73 10.2210/pdb9r73/pdb 
WWPDB D_1292147794 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9R73 
_pdbx_database_status.recvd_initial_deposition_date   2025-05-13 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB WT               2WL1 unspecified 
PDB 'related mutant' 9R6Y unspecified 
PDB 'related mutant' 9R70 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mittl@bioc.uzh.ch 
_pdbx_contact_author.name_first         Peer 
_pdbx_contact_author.name_last          Mittl 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3348-3147 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mittl, P.'   1 0000-0002-3348-3147 
'Possner, D.' 2 ?                   
# 
_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                     'Pyrin B30.2 domain, FMF mutation delta-Ile692' 
_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 'Mittl, P.'   1 ? 
primary 'Possner, D.' 2 ? 
# 
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 Pyrin             20950.922 1   ? delte-Ile692 ? 'Pyrin B30.2 domain with FMF mutation deletion of Ile692' 
2 non-polymer syn 'THIOCYANATE ION' 58.082    2   ? ?            ? ?                                                         
3 non-polymer syn 1,2-ETHANEDIOL    62.068    1   ? ?            ? ?                                                         
4 water       nat water             18.015    142 ? ?            ? ?                                                         
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Marenostrin 
# 
_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       
;NVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAW
ILGACKTSISRKGNMTLSPENGYWVVMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASC
SFSGPLQPIFSPGTRDGGKNTAPLTICPVG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAW
ILGACKTSISRKGNMTLSPENGYWVVMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASC
SFSGPLQPIFSPGTRDGGKNTAPLTICPVG
;
_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 'THIOCYANATE ION' SCN 
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   ASN n 
1 2   VAL n 
1 3   PRO n 
1 4   GLU n 
1 5   LEU n 
1 6   ILE n 
1 7   GLY n 
1 8   ALA n 
1 9   GLN n 
1 10  ALA n 
1 11  HIS n 
1 12  ALA n 
1 13  VAL n 
1 14  ASN n 
1 15  VAL n 
1 16  ILE n 
1 17  LEU n 
1 18  ASP n 
1 19  ALA n 
1 20  GLU n 
1 21  THR n 
1 22  ALA n 
1 23  TYR n 
1 24  PRO n 
1 25  ASN n 
1 26  LEU n 
1 27  ILE n 
1 28  PHE n 
1 29  SER n 
1 30  ASP n 
1 31  ASP n 
1 32  LEU n 
1 33  LYS n 
1 34  SER n 
1 35  VAL n 
1 36  ARG n 
1 37  LEU n 
1 38  GLY n 
1 39  ASN n 
1 40  LYS n 
1 41  TRP n 
1 42  GLU n 
1 43  ARG n 
1 44  LEU n 
1 45  PRO n 
1 46  ASP n 
1 47  GLY n 
1 48  PRO n 
1 49  GLN n 
1 50  ARG n 
1 51  PHE n 
1 52  ASP n 
1 53  SER n 
1 54  CYS n 
1 55  ILE n 
1 56  ILE n 
1 57  VAL n 
1 58  LEU n 
1 59  GLY n 
1 60  SER n 
1 61  PRO n 
1 62  SER n 
1 63  PHE n 
1 64  LEU n 
1 65  SER n 
1 66  GLY n 
1 67  ARG n 
1 68  ARG n 
1 69  TYR n 
1 70  TRP n 
1 71  GLU n 
1 72  VAL n 
1 73  GLU n 
1 74  VAL n 
1 75  GLY n 
1 76  ASP n 
1 77  LYS n 
1 78  THR n 
1 79  ALA n 
1 80  TRP n 
1 81  ILE n 
1 82  LEU n 
1 83  GLY n 
1 84  ALA n 
1 85  CYS n 
1 86  LYS n 
1 87  THR n 
1 88  SER n 
1 89  ILE n 
1 90  SER n 
1 91  ARG n 
1 92  LYS n 
1 93  GLY n 
1 94  ASN n 
1 95  MET n 
1 96  THR n 
1 97  LEU n 
1 98  SER n 
1 99  PRO n 
1 100 GLU n 
1 101 ASN n 
1 102 GLY n 
1 103 TYR n 
1 104 TRP n 
1 105 VAL n 
1 106 VAL n 
1 107 MET n 
1 108 MET n 
1 109 LYS n 
1 110 GLU n 
1 111 ASN n 
1 112 GLU n 
1 113 TYR n 
1 114 GLN n 
1 115 ALA n 
1 116 SER n 
1 117 SER n 
1 118 VAL n 
1 119 PRO n 
1 120 PRO n 
1 121 THR n 
1 122 ARG n 
1 123 LEU n 
1 124 LEU n 
1 125 ILE n 
1 126 LYS n 
1 127 GLU n 
1 128 PRO n 
1 129 PRO n 
1 130 LYS n 
1 131 ARG n 
1 132 VAL n 
1 133 GLY n 
1 134 ILE n 
1 135 PHE n 
1 136 VAL n 
1 137 ASP n 
1 138 TYR n 
1 139 ARG n 
1 140 VAL n 
1 141 GLY n 
1 142 SER n 
1 143 ILE n 
1 144 SER n 
1 145 PHE n 
1 146 TYR n 
1 147 ASN n 
1 148 VAL n 
1 149 THR n 
1 150 ALA n 
1 151 ARG n 
1 152 SER n 
1 153 HIS n 
1 154 ILE n 
1 155 TYR n 
1 156 THR n 
1 157 PHE n 
1 158 ALA n 
1 159 SER n 
1 160 CYS n 
1 161 SER n 
1 162 PHE n 
1 163 SER n 
1 164 GLY n 
1 165 PRO n 
1 166 LEU n 
1 167 GLN n 
1 168 PRO n 
1 169 ILE n 
1 170 PHE n 
1 171 SER n 
1 172 PRO n 
1 173 GLY n 
1 174 THR n 
1 175 ARG n 
1 176 ASP n 
1 177 GLY n 
1 178 GLY n 
1 179 LYS n 
1 180 ASN n 
1 181 THR n 
1 182 ALA n 
1 183 PRO n 
1 184 LEU n 
1 185 THR n 
1 186 ILE n 
1 187 CYS n 
1 188 PRO n 
1 189 VAL n 
1 190 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   190 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MEFV, MEF, TRIM20' 
_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 
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 
SCN non-polymer         . 'THIOCYANATE ION' ?                 'C N S -1'       58.082  
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   ASN 1   586 586 ASN ASN A . n 
A 1 2   VAL 2   587 587 VAL VAL A . n 
A 1 3   PRO 3   588 588 PRO PRO A . n 
A 1 4   GLU 4   589 589 GLU GLU A . n 
A 1 5   LEU 5   590 590 LEU LEU A . n 
A 1 6   ILE 6   591 591 ILE ILE A . n 
A 1 7   GLY 7   592 592 GLY GLY A . n 
A 1 8   ALA 8   593 593 ALA ALA A . n 
A 1 9   GLN 9   594 594 GLN GLN A . n 
A 1 10  ALA 10  595 595 ALA ALA A . n 
A 1 11  HIS 11  596 596 HIS HIS A . n 
A 1 12  ALA 12  597 597 ALA ALA A . n 
A 1 13  VAL 13  598 598 VAL VAL A . n 
A 1 14  ASN 14  599 599 ASN ASN A . n 
A 1 15  VAL 15  600 600 VAL VAL A . n 
A 1 16  ILE 16  601 601 ILE ILE A . n 
A 1 17  LEU 17  602 602 LEU LEU A . n 
A 1 18  ASP 18  603 603 ASP ASP A . n 
A 1 19  ALA 19  604 604 ALA ALA A . n 
A 1 20  GLU 20  605 605 GLU GLU A . n 
A 1 21  THR 21  606 606 THR THR A . n 
A 1 22  ALA 22  607 607 ALA ALA A . n 
A 1 23  TYR 23  608 608 TYR TYR A . n 
A 1 24  PRO 24  609 609 PRO PRO A . n 
A 1 25  ASN 25  610 610 ASN ASN A . n 
A 1 26  LEU 26  611 611 LEU LEU A . n 
A 1 27  ILE 27  612 612 ILE ILE A . n 
A 1 28  PHE 28  613 613 PHE PHE A . n 
A 1 29  SER 29  614 614 SER SER A . n 
A 1 30  ASP 30  615 615 ASP ASP A . n 
A 1 31  ASP 31  616 616 ASP ASP A . n 
A 1 32  LEU 32  617 617 LEU LEU A . n 
A 1 33  LYS 33  618 618 LYS LYS A . n 
A 1 34  SER 34  619 619 SER SER A . n 
A 1 35  VAL 35  620 620 VAL VAL A . n 
A 1 36  ARG 36  621 621 ARG ARG A . n 
A 1 37  LEU 37  622 622 LEU LEU A . n 
A 1 38  GLY 38  623 623 GLY GLY A . n 
A 1 39  ASN 39  624 624 ASN ASN A . n 
A 1 40  LYS 40  625 625 LYS LYS A . n 
A 1 41  TRP 41  626 626 TRP TRP A . n 
A 1 42  GLU 42  627 627 GLU GLU A . n 
A 1 43  ARG 43  628 628 ARG ARG A . n 
A 1 44  LEU 44  629 629 LEU LEU A . n 
A 1 45  PRO 45  630 630 PRO PRO A . n 
A 1 46  ASP 46  631 631 ASP ASP A . n 
A 1 47  GLY 47  632 632 GLY GLY A . n 
A 1 48  PRO 48  633 633 PRO PRO A . n 
A 1 49  GLN 49  634 634 GLN GLN A . n 
A 1 50  ARG 50  635 635 ARG ARG A . n 
A 1 51  PHE 51  636 636 PHE PHE A . n 
A 1 52  ASP 52  637 637 ASP ASP A . n 
A 1 53  SER 53  638 638 SER SER A . n 
A 1 54  CYS 54  639 639 CYS CYS A . n 
A 1 55  ILE 55  640 640 ILE ILE A . n 
A 1 56  ILE 56  641 641 ILE ILE A . n 
A 1 57  VAL 57  642 642 VAL VAL A . n 
A 1 58  LEU 58  643 643 LEU LEU A . n 
A 1 59  GLY 59  644 644 GLY GLY A . n 
A 1 60  SER 60  645 645 SER SER A . n 
A 1 61  PRO 61  646 646 PRO PRO A . n 
A 1 62  SER 62  647 647 SER SER A . n 
A 1 63  PHE 63  648 648 PHE PHE A . n 
A 1 64  LEU 64  649 649 LEU LEU A . n 
A 1 65  SER 65  650 650 SER SER A . n 
A 1 66  GLY 66  651 651 GLY GLY A . n 
A 1 67  ARG 67  652 652 ARG ARG A . n 
A 1 68  ARG 68  653 653 ARG ARG A . n 
A 1 69  TYR 69  654 654 TYR TYR A . n 
A 1 70  TRP 70  655 655 TRP TRP A . n 
A 1 71  GLU 71  656 656 GLU GLU A . n 
A 1 72  VAL 72  657 657 VAL VAL A . n 
A 1 73  GLU 73  658 658 GLU GLU A . n 
A 1 74  VAL 74  659 659 VAL VAL A . n 
A 1 75  GLY 75  660 660 GLY GLY A . n 
A 1 76  ASP 76  661 661 ASP ASP A . n 
A 1 77  LYS 77  662 662 LYS LYS A . n 
A 1 78  THR 78  663 663 THR THR A . n 
A 1 79  ALA 79  664 664 ALA ALA A . n 
A 1 80  TRP 80  665 665 TRP TRP A . n 
A 1 81  ILE 81  666 666 ILE ILE A . n 
A 1 82  LEU 82  667 667 LEU LEU A . n 
A 1 83  GLY 83  668 668 GLY GLY A . n 
A 1 84  ALA 84  669 669 ALA ALA A . n 
A 1 85  CYS 85  670 670 CYS CYS A . n 
A 1 86  LYS 86  671 671 LYS LYS A . n 
A 1 87  THR 87  672 672 THR THR A . n 
A 1 88  SER 88  673 673 SER SER A . n 
A 1 89  ILE 89  674 674 ILE ILE A . n 
A 1 90  SER 90  675 675 SER SER A . n 
A 1 91  ARG 91  676 676 ARG ARG A . n 
A 1 92  LYS 92  677 677 LYS LYS A . n 
A 1 93  GLY 93  678 678 GLY GLY A . n 
A 1 94  ASN 94  679 679 ASN ASN A . n 
A 1 95  MET 95  680 680 MET MET A . n 
A 1 96  THR 96  681 681 THR THR A . n 
A 1 97  LEU 97  682 682 LEU LEU A . n 
A 1 98  SER 98  683 683 SER SER A . n 
A 1 99  PRO 99  684 684 PRO PRO A . n 
A 1 100 GLU 100 685 685 GLU GLU A . n 
A 1 101 ASN 101 686 686 ASN ASN A . n 
A 1 102 GLY 102 687 687 GLY GLY A . n 
A 1 103 TYR 103 688 688 TYR TYR A . n 
A 1 104 TRP 104 689 689 TRP TRP A . n 
A 1 105 VAL 105 690 690 VAL VAL A . n 
A 1 106 VAL 106 691 691 VAL VAL A . n 
A 1 107 MET 107 693 693 MET MET A . n 
A 1 108 MET 108 694 694 MET MET A . n 
A 1 109 LYS 109 695 695 LYS LYS A . n 
A 1 110 GLU 110 696 696 GLU GLU A . n 
A 1 111 ASN 111 697 697 ASN ASN A . n 
A 1 112 GLU 112 698 698 GLU GLU A . n 
A 1 113 TYR 113 699 699 TYR TYR A . n 
A 1 114 GLN 114 700 700 GLN GLN A . n 
A 1 115 ALA 115 701 701 ALA ALA A . n 
A 1 116 SER 116 702 702 SER SER A . n 
A 1 117 SER 117 703 703 SER SER A . n 
A 1 118 VAL 118 704 704 VAL VAL A . n 
A 1 119 PRO 119 705 705 PRO PRO A . n 
A 1 120 PRO 120 706 706 PRO PRO A . n 
A 1 121 THR 121 707 707 THR THR A . n 
A 1 122 ARG 122 708 708 ARG ARG A . n 
A 1 123 LEU 123 709 709 LEU LEU A . n 
A 1 124 LEU 124 710 710 LEU LEU A . n 
A 1 125 ILE 125 711 711 ILE ILE A . n 
A 1 126 LYS 126 712 712 LYS LYS A . n 
A 1 127 GLU 127 713 713 GLU GLU A . n 
A 1 128 PRO 128 714 714 PRO PRO A . n 
A 1 129 PRO 129 715 715 PRO PRO A . n 
A 1 130 LYS 130 716 716 LYS LYS A . n 
A 1 131 ARG 131 717 717 ARG ARG A . n 
A 1 132 VAL 132 718 718 VAL VAL A . n 
A 1 133 GLY 133 719 719 GLY GLY A . n 
A 1 134 ILE 134 720 720 ILE ILE A . n 
A 1 135 PHE 135 721 721 PHE PHE A . n 
A 1 136 VAL 136 722 722 VAL VAL A . n 
A 1 137 ASP 137 723 723 ASP ASP A . n 
A 1 138 TYR 138 724 724 TYR TYR A . n 
A 1 139 ARG 139 725 725 ARG ARG A . n 
A 1 140 VAL 140 726 726 VAL VAL A . n 
A 1 141 GLY 141 727 727 GLY GLY A . n 
A 1 142 SER 142 728 728 SER SER A . n 
A 1 143 ILE 143 729 729 ILE ILE A . n 
A 1 144 SER 144 730 730 SER SER A . n 
A 1 145 PHE 145 731 731 PHE PHE A . n 
A 1 146 TYR 146 732 732 TYR TYR A . n 
A 1 147 ASN 147 733 733 ASN ASN A . n 
A 1 148 VAL 148 734 734 VAL VAL A . n 
A 1 149 THR 149 735 735 THR THR A . n 
A 1 150 ALA 150 736 736 ALA ALA A . n 
A 1 151 ARG 151 737 737 ARG ARG A . n 
A 1 152 SER 152 738 738 SER SER A . n 
A 1 153 HIS 153 739 739 HIS HIS A . n 
A 1 154 ILE 154 740 740 ILE ILE A . n 
A 1 155 TYR 155 741 741 TYR TYR A . n 
A 1 156 THR 156 742 742 THR THR A . n 
A 1 157 PHE 157 743 743 PHE PHE A . n 
A 1 158 ALA 158 744 744 ALA ALA A . n 
A 1 159 SER 159 745 745 SER SER A . n 
A 1 160 CYS 160 746 746 CYS CYS A . n 
A 1 161 SER 161 747 747 SER SER A . n 
A 1 162 PHE 162 748 748 PHE PHE A . n 
A 1 163 SER 163 749 749 SER SER A . n 
A 1 164 GLY 164 750 750 GLY GLY A . n 
A 1 165 PRO 165 751 751 PRO PRO A . n 
A 1 166 LEU 166 752 752 LEU LEU A . n 
A 1 167 GLN 167 753 753 GLN GLN A . n 
A 1 168 PRO 168 754 754 PRO PRO A . n 
A 1 169 ILE 169 755 755 ILE ILE A . n 
A 1 170 PHE 170 756 756 PHE PHE A . n 
A 1 171 SER 171 757 757 SER SER A . n 
A 1 172 PRO 172 758 758 PRO PRO A . n 
A 1 173 GLY 173 759 759 GLY GLY A . n 
A 1 174 THR 174 760 760 THR THR A . n 
A 1 175 ARG 175 761 761 ARG ARG A . n 
A 1 176 ASP 176 762 762 ASP ASP A . n 
A 1 177 GLY 177 763 763 GLY GLY A . n 
A 1 178 GLY 178 764 764 GLY GLY A . n 
A 1 179 LYS 179 765 765 LYS LYS A . n 
A 1 180 ASN 180 766 766 ASN ASN A . n 
A 1 181 THR 181 767 767 THR THR A . n 
A 1 182 ALA 182 768 768 ALA ALA A . n 
A 1 183 PRO 183 769 769 PRO PRO A . n 
A 1 184 LEU 184 770 770 LEU LEU A . n 
A 1 185 THR 185 771 771 THR THR A . n 
A 1 186 ILE 186 772 772 ILE ILE A . n 
A 1 187 CYS 187 773 773 CYS CYS A . n 
A 1 188 PRO 188 774 774 PRO PRO A . n 
A 1 189 VAL 189 775 775 VAL VAL A . n 
A 1 190 GLY 190 776 776 GLY GLY A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SCN 1   801  2   SCN SCN A . 
C 2 SCN 1   802  3   SCN SCN A . 
D 3 EDO 1   803  4   EDO EDO A . 
E 4 HOH 1   901  49  HOH HOH A . 
E 4 HOH 2   902  145 HOH HOH A . 
E 4 HOH 3   903  77  HOH HOH A . 
E 4 HOH 4   904  74  HOH HOH A . 
E 4 HOH 5   905  90  HOH HOH A . 
E 4 HOH 6   906  11  HOH HOH A . 
E 4 HOH 7   907  84  HOH HOH A . 
E 4 HOH 8   908  42  HOH HOH A . 
E 4 HOH 9   909  13  HOH HOH A . 
E 4 HOH 10  910  16  HOH HOH A . 
E 4 HOH 11  911  5   HOH HOH A . 
E 4 HOH 12  912  88  HOH HOH A . 
E 4 HOH 13  913  7   HOH HOH A . 
E 4 HOH 14  914  150 HOH HOH A . 
E 4 HOH 15  915  110 HOH HOH A . 
E 4 HOH 16  916  114 HOH HOH A . 
E 4 HOH 17  917  108 HOH HOH A . 
E 4 HOH 18  918  126 HOH HOH A . 
E 4 HOH 19  919  75  HOH HOH A . 
E 4 HOH 20  920  111 HOH HOH A . 
E 4 HOH 21  921  97  HOH HOH A . 
E 4 HOH 22  922  112 HOH HOH A . 
E 4 HOH 23  923  30  HOH HOH A . 
E 4 HOH 24  924  121 HOH HOH A . 
E 4 HOH 25  925  146 HOH HOH A . 
E 4 HOH 26  926  95  HOH HOH A . 
E 4 HOH 27  927  9   HOH HOH A . 
E 4 HOH 28  928  26  HOH HOH A . 
E 4 HOH 29  929  130 HOH HOH A . 
E 4 HOH 30  930  119 HOH HOH A . 
E 4 HOH 31  931  125 HOH HOH A . 
E 4 HOH 32  932  12  HOH HOH A . 
E 4 HOH 33  933  99  HOH HOH A . 
E 4 HOH 34  934  91  HOH HOH A . 
E 4 HOH 35  935  129 HOH HOH A . 
E 4 HOH 36  936  47  HOH HOH A . 
E 4 HOH 37  937  2   HOH HOH A . 
E 4 HOH 38  938  138 HOH HOH A . 
E 4 HOH 39  939  18  HOH HOH A . 
E 4 HOH 40  940  96  HOH HOH A . 
E 4 HOH 41  941  123 HOH HOH A . 
E 4 HOH 42  942  59  HOH HOH A . 
E 4 HOH 43  943  34  HOH HOH A . 
E 4 HOH 44  944  132 HOH HOH A . 
E 4 HOH 45  945  33  HOH HOH A . 
E 4 HOH 46  946  101 HOH HOH A . 
E 4 HOH 47  947  133 HOH HOH A . 
E 4 HOH 48  948  136 HOH HOH A . 
E 4 HOH 49  949  92  HOH HOH A . 
E 4 HOH 50  950  137 HOH HOH A . 
E 4 HOH 51  951  51  HOH HOH A . 
E 4 HOH 52  952  45  HOH HOH A . 
E 4 HOH 53  953  58  HOH HOH A . 
E 4 HOH 54  954  113 HOH HOH A . 
E 4 HOH 55  955  109 HOH HOH A . 
E 4 HOH 56  956  4   HOH HOH A . 
E 4 HOH 57  957  32  HOH HOH A . 
E 4 HOH 58  958  71  HOH HOH A . 
E 4 HOH 59  959  55  HOH HOH A . 
E 4 HOH 60  960  53  HOH HOH A . 
E 4 HOH 61  961  117 HOH HOH A . 
E 4 HOH 62  962  93  HOH HOH A . 
E 4 HOH 63  963  72  HOH HOH A . 
E 4 HOH 64  964  10  HOH HOH A . 
E 4 HOH 65  965  52  HOH HOH A . 
E 4 HOH 66  966  27  HOH HOH A . 
E 4 HOH 67  967  66  HOH HOH A . 
E 4 HOH 68  968  40  HOH HOH A . 
E 4 HOH 69  969  78  HOH HOH A . 
E 4 HOH 70  970  124 HOH HOH A . 
E 4 HOH 71  971  81  HOH HOH A . 
E 4 HOH 72  972  48  HOH HOH A . 
E 4 HOH 73  973  29  HOH HOH A . 
E 4 HOH 74  974  37  HOH HOH A . 
E 4 HOH 75  975  120 HOH HOH A . 
E 4 HOH 76  976  98  HOH HOH A . 
E 4 HOH 77  977  147 HOH HOH A . 
E 4 HOH 78  978  76  HOH HOH A . 
E 4 HOH 79  979  31  HOH HOH A . 
E 4 HOH 80  980  56  HOH HOH A . 
E 4 HOH 81  981  140 HOH HOH A . 
E 4 HOH 82  982  25  HOH HOH A . 
E 4 HOH 83  983  128 HOH HOH A . 
E 4 HOH 84  984  94  HOH HOH A . 
E 4 HOH 85  985  36  HOH HOH A . 
E 4 HOH 86  986  70  HOH HOH A . 
E 4 HOH 87  987  57  HOH HOH A . 
E 4 HOH 88  988  127 HOH HOH A . 
E 4 HOH 89  989  103 HOH HOH A . 
E 4 HOH 90  990  39  HOH HOH A . 
E 4 HOH 91  991  79  HOH HOH A . 
E 4 HOH 92  992  135 HOH HOH A . 
E 4 HOH 93  993  82  HOH HOH A . 
E 4 HOH 94  994  102 HOH HOH A . 
E 4 HOH 95  995  118 HOH HOH A . 
E 4 HOH 96  996  87  HOH HOH A . 
E 4 HOH 97  997  60  HOH HOH A . 
E 4 HOH 98  998  43  HOH HOH A . 
E 4 HOH 99  999  17  HOH HOH A . 
E 4 HOH 100 1000 54  HOH HOH A . 
E 4 HOH 101 1001 46  HOH HOH A . 
E 4 HOH 102 1002 122 HOH HOH A . 
E 4 HOH 103 1003 149 HOH HOH A . 
E 4 HOH 104 1004 105 HOH HOH A . 
E 4 HOH 105 1005 73  HOH HOH A . 
E 4 HOH 106 1006 106 HOH HOH A . 
E 4 HOH 107 1007 38  HOH HOH A . 
E 4 HOH 108 1008 107 HOH HOH A . 
E 4 HOH 109 1009 100 HOH HOH A . 
E 4 HOH 110 1010 50  HOH HOH A . 
E 4 HOH 111 1011 134 HOH HOH A . 
E 4 HOH 112 1012 1   HOH HOH A . 
E 4 HOH 113 1013 83  HOH HOH A . 
E 4 HOH 114 1014 148 HOH HOH A . 
E 4 HOH 115 1015 21  HOH HOH A . 
E 4 HOH 116 1016 20  HOH HOH A . 
E 4 HOH 117 1017 139 HOH HOH A . 
E 4 HOH 118 1018 85  HOH HOH A . 
E 4 HOH 119 1019 115 HOH HOH A . 
E 4 HOH 120 1020 28  HOH HOH A . 
E 4 HOH 121 1021 23  HOH HOH A . 
E 4 HOH 122 1022 116 HOH HOH A . 
E 4 HOH 123 1023 86  HOH HOH A . 
E 4 HOH 124 1024 144 HOH HOH A . 
E 4 HOH 125 1025 89  HOH HOH A . 
E 4 HOH 126 1026 104 HOH HOH A . 
E 4 HOH 127 1027 141 HOH HOH A . 
E 4 HOH 128 1028 63  HOH HOH A . 
E 4 HOH 129 1029 142 HOH HOH A . 
E 4 HOH 130 1030 41  HOH HOH A . 
E 4 HOH 131 1031 24  HOH HOH A . 
E 4 HOH 132 1032 68  HOH HOH A . 
E 4 HOH 133 1033 19  HOH HOH A . 
E 4 HOH 134 1034 65  HOH HOH A . 
E 4 HOH 135 1035 44  HOH HOH A . 
E 4 HOH 136 1036 67  HOH HOH A . 
E 4 HOH 137 1037 6   HOH HOH A . 
E 4 HOH 138 1038 61  HOH HOH A . 
E 4 HOH 139 1039 35  HOH HOH A . 
E 4 HOH 140 1040 8   HOH HOH A . 
E 4 HOH 141 1041 143 HOH HOH A . 
E 4 HOH 142 1042 69  HOH HOH A . 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0430 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .        ? 5 
# 
_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                     9R73 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.540 
_cell.length_a_esd                 ? 
_cell.length_b                     59.540 
_cell.length_b_esd                 ? 
_cell.length_c                     179.414 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9R73 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_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                   9R73 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.86 
_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              ? 
_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    '0.1 M Tris-AcOH, pH 7.6; 0.2 M KSCN; 30 % (w/v) PEG 2k MME' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2009-06-04 
_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   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9R73 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.44 
_reflns.d_resolution_low                               44.85 
_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                                     35210 
_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                          15.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.94 
_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                                0.133 
_reflns.pdbx_Rpim_I_all                                0.028 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       729664 
_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                              0.130 
_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                                    1.44 
_reflns_shell.d_res_low                                     1.46 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           26458 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1690 
_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                               15.7 
_reflns_shell.pdbx_chi_squared                              0.72 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               3.226 
_reflns_shell.pdbx_Rpim_I_all                               0.772 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.407 
_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                                  3.125 
_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]                            -0.04 
_refine.aniso_B[1][2]                            -0.02 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.04 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.13 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.590 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_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                                 9R73 
_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                            1.44 
_refine.ls_d_res_low                             44.74 
_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                     33360 
_refine.ls_number_reflns_R_free                  1749 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17593 
_refine.ls_R_factor_R_free                       0.19711 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17478 
_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          'FOURIER SYNTHESIS' 
_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                       0.064 
_refine.pdbx_overall_ESU_R_Free                  0.065 
_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                             2.735 
_refine.overall_SU_ML                            0.049 
_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                       1.44 
_refine_hist.d_res_low                        44.74 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               1626 
_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        1474 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.012  1591 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1495 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.948  1.800  2174 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.639  1.745  3461 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 8.011  5.000  209  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 14.232 5.000  12   ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 11.983 10.000 258  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.095  0.200  237  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  1919 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  373  ? 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' ? 2.365  1.637  799  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.331  1.629  796  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 3.954  2.907  1007 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.957  2.910  1008 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 3.115  2.024  792  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 3.117  2.026  793  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 4.644  3.534  1164 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 8.414  23.11  1845 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 8.363  21.17  1807 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? 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                          1.440 
_refine_ls_shell.d_res_low                           1.477 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                118 
_refine_ls_shell.number_reflns_R_work                2410 
_refine_ls_shell.percent_reflns_obs                  99.96 
_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                     0.340 
_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                     0.374 
# 
_struct.entry_id                     9R73 
_struct.title                        'Pyrin B30.2 domain, FMF mutation delta-Ile692' 
_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        9R73 
_struct_keywords.text            'Familial Mediterranean fever, MEFV, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
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 2 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MEFV_HUMAN 
_struct_ref.pdbx_db_accession          O15553 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAW
ILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFAS
CSFSGPLQPIFSPGTRDGGKNTAPLTICPVG
;
_struct_ref.pdbx_align_begin           586 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9R73 
_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                 190 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O15553 
_struct_ref_seq.db_align_beg                  586 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  776 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       586 
_struct_ref_seq.pdbx_auth_seq_align_end       776 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9R73 
_struct_ref_seq_dif.mon_id                       ? 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      ? 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   O15553 
_struct_ref_seq_dif.db_mon_id                    ILE 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          692 
_struct_ref_seq_dif.details                      deletion 
_struct_ref_seq_dif.pdbx_auth_seq_num            ? 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)' 340  ? 
1 MORE         1    ? 
1 'SSA (A^2)'  9510 ? 
# 
_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 GLU A 4   ? ALA A 10  ? GLU A 589 ALA A 595 1 ? 7 
HELX_P HELX_P2 AA2 ALA A 19  ? ALA A 22  ? ALA A 604 ALA A 607 5 ? 4 
HELX_P HELX_P3 AA3 SER A 98  ? ASN A 101 ? SER A 683 ASN A 686 5 ? 4 
HELX_P HELX_P4 AA4 ARG A 175 ? LYS A 179 ? ARG A 761 LYS A 765 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 60  A . ? SER 645 A PRO 61  A ? PRO 646 A 1 0.88  
2 SER 60  A . ? SER 645 A PRO 61  A ? PRO 646 A 1 0.85  
3 VAL 118 A . ? VAL 704 A PRO 119 A ? PRO 705 A 1 -2.73 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
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 
AA2 6 7 ? 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 ILE A 16  ? LEU A 17  ? ILE A 601 LEU A 602 
AA1 2 VAL A 57  ? SER A 60  ? VAL A 642 SER A 645 
AA1 3 LEU A 166 ? SER A 171 ? LEU A 752 SER A 757 
AA1 4 TRP A 80  ? LYS A 86  ? TRP A 665 LYS A 671 
AA1 5 TYR A 103 ? LYS A 109 ? TYR A 688 LYS A 695 
AA1 6 GLU A 112 ? ALA A 115 ? GLU A 698 ALA A 701 
AA1 7 THR A 121 ? LEU A 123 ? THR A 707 LEU A 709 
AA2 1 LEU A 26  ? PHE A 28  ? LEU A 611 PHE A 613 
AA2 2 SER A 34  ? LEU A 37  ? SER A 619 LEU A 622 
AA2 3 LEU A 184 ? CYS A 187 ? LEU A 770 CYS A 773 
AA2 4 ARG A 67  ? GLU A 73  ? ARG A 652 GLU A 658 
AA2 5 ARG A 131 ? ASP A 137 ? ARG A 717 ASP A 723 
AA2 6 SER A 142 ? ASN A 147 ? SER A 728 ASN A 733 
AA2 7 SER A 152 ? PHE A 157 ? SER A 738 PHE A 743 
# 
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 16  ? N ILE A 601 O SER A 60  ? O SER A 645 
AA1 2 3 N GLY A 59  ? N GLY A 644 O PRO A 168 ? O PRO A 754 
AA1 3 4 O GLN A 167 ? O GLN A 753 N CYS A 85  ? N CYS A 670 
AA1 4 5 N ALA A 84  ? N ALA A 669 O TRP A 104 ? O TRP A 689 
AA1 5 6 N MET A 107 ? N MET A 693 O GLN A 114 ? O GLN A 700 
AA1 6 7 N TYR A 113 ? N TYR A 699 O LEU A 123 ? O LEU A 709 
AA2 1 2 N ILE A 27  ? N ILE A 612 O ARG A 36  ? O ARG A 621 
AA2 2 3 N VAL A 35  ? N VAL A 620 O LEU A 184 ? O LEU A 770 
AA2 3 4 O THR A 185 ? O THR A 771 N GLU A 73  ? N GLU A 658 
AA2 4 5 N ARG A 68  ? N ARG A 653 O VAL A 136 ? O VAL A 722 
AA2 5 6 N ASP A 137 ? N ASP A 723 O SER A 142 ? O SER A 728 
AA2 6 7 N PHE A 145 ? N PHE A 731 O ILE A 154 ? O ILE A 740 
# 
_pdbx_entry_details.entry_id                   9R73 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 916 ? ? O A HOH 1029 ? ? 1.80 
2 1 O A HOH 902 ? ? O A HOH 1006 ? ? 1.93 
3 1 O A HOH 993 ? ? O A HOH 1017 ? ? 1.93 
4 1 O A HOH 981 ? ? O A HOH 1027 ? ? 2.09 
5 1 O A HOH 939 ? ? O A HOH 999  ? ? 2.10 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 1027 ? ? 1_555 O A HOH 1027 ? ? 10_555 1.43 
2 1 O A HOH 902  ? ? 1_555 O A HOH 913  ? ? 6_554  2.14 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             656 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             656 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.153 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.099 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A GLU 656 ? ? CD A GLU 656 ? ? OE1 A GLU 656 ? ? 131.10 118.30 12.80  2.00 N 
2 1 CG A GLU 656 ? ? CD A GLU 656 ? ? OE2 A GLU 656 ? ? 103.71 118.30 -14.59 2.00 N 
3 1 NE A ARG 737 ? A CZ A ARG 737 ? A NH1 A ARG 737 ? A 116.79 120.30 -3.51  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 638 ? ? -123.67 -52.52 
2 1 LEU A 649 ? ? -140.63 32.78  
3 1 MET A 680 ? ? -154.01 87.58  
4 1 SER A 702 ? A -87.79  48.54  
5 1 SER A 702 ? B -77.30  38.14  
6 1 SER A 703 ? ? -51.77  170.13 
7 1 ARG A 737 ? B 73.34   34.93  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   MET 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    680 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   THR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    681 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            144.13 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 708 ? ? 0.146 'SIDE CHAIN' 
2 1 ARG A 737 ? A 0.233 'SIDE CHAIN' 
# 
_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     1023 
_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_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         10.8002 
_pdbx_refine_tls.origin_y         -21.8624 
_pdbx_refine_tls.origin_z         6.6690 
_pdbx_refine_tls.T[1][1]          0.0204 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0144 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0015 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0183 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0016 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0444 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.6241 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.5727 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.2167 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.2339 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.9801 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.1210 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0066 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0406 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.3222 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0896 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0216 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0240 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1832 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0767 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0150 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     586 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     775 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SCN S    S N N 300 
SCN C    C N N 301 
SCN N    N N N 302 
SER N    N N N 303 
SER CA   C N S 304 
SER C    C N N 305 
SER O    O N N 306 
SER CB   C N N 307 
SER OG   O N N 308 
SER OXT  O N N 309 
SER H    H N N 310 
SER H2   H N N 311 
SER HA   H N N 312 
SER HB2  H N N 313 
SER HB3  H N N 314 
SER HG   H N N 315 
SER HXT  H N N 316 
THR N    N N N 317 
THR CA   C N S 318 
THR C    C N N 319 
THR O    O N N 320 
THR CB   C N R 321 
THR OG1  O N N 322 
THR CG2  C N N 323 
THR OXT  O N N 324 
THR H    H N N 325 
THR H2   H N N 326 
THR HA   H N N 327 
THR HB   H N N 328 
THR HG1  H N N 329 
THR HG21 H N N 330 
THR HG22 H N N 331 
THR HG23 H N N 332 
THR HXT  H N N 333 
TRP N    N N N 334 
TRP CA   C N S 335 
TRP C    C N N 336 
TRP O    O N N 337 
TRP CB   C N N 338 
TRP CG   C Y N 339 
TRP CD1  C Y N 340 
TRP CD2  C Y N 341 
TRP NE1  N Y N 342 
TRP CE2  C Y N 343 
TRP CE3  C Y N 344 
TRP CZ2  C Y N 345 
TRP CZ3  C Y N 346 
TRP CH2  C Y N 347 
TRP OXT  O N N 348 
TRP H    H N N 349 
TRP H2   H N N 350 
TRP HA   H N N 351 
TRP HB2  H N N 352 
TRP HB3  H N N 353 
TRP HD1  H N N 354 
TRP HE1  H N N 355 
TRP HE3  H N N 356 
TRP HZ2  H N N 357 
TRP HZ3  H N N 358 
TRP HH2  H N N 359 
TRP HXT  H N N 360 
TYR N    N N N 361 
TYR CA   C N S 362 
TYR C    C N N 363 
TYR O    O N N 364 
TYR CB   C N N 365 
TYR CG   C Y N 366 
TYR CD1  C Y N 367 
TYR CD2  C Y N 368 
TYR CE1  C Y N 369 
TYR CE2  C Y N 370 
TYR CZ   C Y N 371 
TYR OH   O N N 372 
TYR OXT  O N N 373 
TYR H    H N N 374 
TYR H2   H N N 375 
TYR HA   H N N 376 
TYR HB2  H N N 377 
TYR HB3  H N N 378 
TYR HD1  H N N 379 
TYR HD2  H N N 380 
TYR HE1  H N N 381 
TYR HE2  H N N 382 
TYR HH   H N N 383 
TYR HXT  H N N 384 
VAL N    N N N 385 
VAL CA   C N S 386 
VAL C    C N N 387 
VAL O    O N N 388 
VAL CB   C N N 389 
VAL CG1  C N N 390 
VAL CG2  C N N 391 
VAL OXT  O N N 392 
VAL H    H N N 393 
VAL H2   H N N 394 
VAL HA   H N N 395 
VAL HB   H N N 396 
VAL HG11 H N N 397 
VAL HG12 H N N 398 
VAL HG13 H N N 399 
VAL HG21 H N N 400 
VAL HG22 H N N 401 
VAL HG23 H N N 402 
VAL HXT  H N N 403 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SCN S   C    sing N N 286 
SCN C   N    trip N N 287 
SER N   CA   sing N N 288 
SER N   H    sing N N 289 
SER N   H2   sing N N 290 
SER CA  C    sing N N 291 
SER CA  CB   sing N N 292 
SER CA  HA   sing N N 293 
SER C   O    doub N N 294 
SER C   OXT  sing N N 295 
SER CB  OG   sing N N 296 
SER CB  HB2  sing N N 297 
SER CB  HB3  sing N N 298 
SER OG  HG   sing N N 299 
SER OXT HXT  sing N N 300 
THR N   CA   sing N N 301 
THR N   H    sing N N 302 
THR N   H2   sing N N 303 
THR CA  C    sing N N 304 
THR CA  CB   sing N N 305 
THR CA  HA   sing N N 306 
THR C   O    doub N N 307 
THR C   OXT  sing N N 308 
THR CB  OG1  sing N N 309 
THR CB  CG2  sing N N 310 
THR CB  HB   sing N N 311 
THR OG1 HG1  sing N N 312 
THR CG2 HG21 sing N N 313 
THR CG2 HG22 sing N N 314 
THR CG2 HG23 sing N N 315 
THR OXT HXT  sing N N 316 
TRP N   CA   sing N N 317 
TRP N   H    sing N N 318 
TRP N   H2   sing N N 319 
TRP CA  C    sing N N 320 
TRP CA  CB   sing N N 321 
TRP CA  HA   sing N N 322 
TRP C   O    doub N N 323 
TRP C   OXT  sing N N 324 
TRP CB  CG   sing N N 325 
TRP CB  HB2  sing N N 326 
TRP CB  HB3  sing N N 327 
TRP CG  CD1  doub Y N 328 
TRP CG  CD2  sing Y N 329 
TRP CD1 NE1  sing Y N 330 
TRP CD1 HD1  sing N N 331 
TRP CD2 CE2  doub Y N 332 
TRP CD2 CE3  sing Y N 333 
TRP NE1 CE2  sing Y N 334 
TRP NE1 HE1  sing N N 335 
TRP CE2 CZ2  sing Y N 336 
TRP CE3 CZ3  doub Y N 337 
TRP CE3 HE3  sing N N 338 
TRP CZ2 CH2  doub Y N 339 
TRP CZ2 HZ2  sing N N 340 
TRP CZ3 CH2  sing Y N 341 
TRP CZ3 HZ3  sing N N 342 
TRP CH2 HH2  sing N N 343 
TRP OXT HXT  sing N N 344 
TYR N   CA   sing N N 345 
TYR N   H    sing N N 346 
TYR N   H2   sing N N 347 
TYR CA  C    sing N N 348 
TYR CA  CB   sing N N 349 
TYR CA  HA   sing N N 350 
TYR C   O    doub N N 351 
TYR C   OXT  sing N N 352 
TYR CB  CG   sing N N 353 
TYR CB  HB2  sing N N 354 
TYR CB  HB3  sing N N 355 
TYR CG  CD1  doub Y N 356 
TYR CG  CD2  sing Y N 357 
TYR CD1 CE1  sing Y N 358 
TYR CD1 HD1  sing N N 359 
TYR CD2 CE2  doub Y N 360 
TYR CD2 HD2  sing N N 361 
TYR CE1 CZ   doub Y N 362 
TYR CE1 HE1  sing N N 363 
TYR CE2 CZ   sing Y N 364 
TYR CE2 HE2  sing N N 365 
TYR CZ  OH   sing N N 366 
TYR OH  HH   sing N N 367 
TYR OXT HXT  sing N N 368 
VAL N   CA   sing N N 369 
VAL N   H    sing N N 370 
VAL N   H2   sing N N 371 
VAL CA  C    sing N N 372 
VAL CA  CB   sing N N 373 
VAL CA  HA   sing N N 374 
VAL C   O    doub N N 375 
VAL C   OXT  sing N N 376 
VAL CB  CG1  sing N N 377 
VAL CB  CG2  sing N N 378 
VAL CB  HB   sing N N 379 
VAL CG1 HG11 sing N N 380 
VAL CG1 HG12 sing N N 381 
VAL CG1 HG13 sing N N 382 
VAL CG2 HG21 sing N N 383 
VAL CG2 HG22 sing N N 384 
VAL CG2 HG23 sing N N 385 
VAL OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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   2WL1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9R73 
_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]   0.016795 
_atom_sites.fract_transf_matrix[1][2]   0.009697 
_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]   0.019394 
_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]   0.005574 
_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 
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   . ASN A 1 1   ? -1.559  -3.292  1.850   1.00 80.58  ? 586  ASN A N   1 
ATOM   2    C CA  . ASN A 1 1   ? -0.756  -3.586  0.629   1.00 75.37  ? 586  ASN A CA  1 
ATOM   3    C C   . ASN A 1 1   ? 0.391   -4.527  1.007   1.00 64.01  ? 586  ASN A C   1 
ATOM   4    O O   . ASN A 1 1   ? 0.970   -4.396  2.093   1.00 55.13  ? 586  ASN A O   1 
ATOM   5    C CB  . ASN A 1 1   ? -0.261  -2.309  -0.047  1.00 78.47  ? 586  ASN A CB  1 
ATOM   6    C CG  . ASN A 1 1   ? 1.010   -1.783  0.585   1.00 88.84  ? 586  ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 1   ? 0.965   -1.170  1.659   1.00 99.82  ? 586  ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 1   ? 2.152   -2.015  -0.051  1.00 82.68  ? 586  ASN A ND2 1 
ATOM   9    N N   . VAL A 1 2   ? 0.668   -5.478  0.097   1.00 53.45  ? 587  VAL A N   1 
ATOM   10   C CA  . VAL A 1 2   ? 1.819   -6.382  0.156   1.00 43.46  ? 587  VAL A CA  1 
ATOM   11   C C   . VAL A 1 2   ? 2.912   -5.759  -0.699  1.00 36.87  ? 587  VAL A C   1 
ATOM   12   O O   . VAL A 1 2   ? 2.679   -5.490  -1.895  1.00 34.42  ? 587  VAL A O   1 
ATOM   13   C CB  . VAL A 1 2   ? 1.578   -7.813  -0.379  1.00 42.67  ? 587  VAL A CB  1 
ATOM   14   C CG1 . VAL A 1 2   ? 0.876   -7.822  -1.736  1.00 43.61  ? 587  VAL A CG1 1 
ATOM   15   C CG2 . VAL A 1 2   ? 2.880   -8.584  -0.547  1.00 36.70  ? 587  VAL A CG2 1 
ATOM   16   N N   . PRO A 1 3   ? 4.120   -5.537  -0.127  1.00 28.30  ? 588  PRO A N   1 
ATOM   17   C CA  . PRO A 1 3   ? 5.092   -4.743  -0.808  1.00 30.44  ? 588  PRO A CA  1 
ATOM   18   C C   . PRO A 1 3   ? 5.770   -5.579  -1.849  1.00 26.16  ? 588  PRO A C   1 
ATOM   19   O O   . PRO A 1 3   ? 5.676   -6.816  -1.918  1.00 24.07  ? 588  PRO A O   1 
ATOM   20   C CB  . PRO A 1 3   ? 6.037   -4.239  0.278   1.00 32.91  ? 588  PRO A CB  1 
ATOM   21   C CG  . PRO A 1 3   ? 5.976   -5.330  1.265   1.00 28.36  ? 588  PRO A CG  1 
ATOM   22   C CD  . PRO A 1 3   ? 4.609   -5.944  1.202   1.00 25.99  ? 588  PRO A CD  1 
ATOM   23   N N   . GLU A 1 4   ? 6.432   -4.824  -2.667  1.00 27.03  ? 589  GLU A N   1 
ATOM   24   C CA  . GLU A 1 4   ? 7.407   -5.395  -3.545  1.00 27.16  ? 589  GLU A CA  1 
ATOM   25   C C   . GLU A 1 4   ? 8.565   -5.799  -2.647  1.00 23.51  ? 589  GLU A C   1 
ATOM   26   O O   . GLU A 1 4   ? 8.689   -5.346  -1.499  1.00 21.37  ? 589  GLU A O   1 
ATOM   27   C CB  . GLU A 1 4   ? 7.753   -4.400  -4.626  1.00 29.44  ? 589  GLU A CB  1 
ATOM   28   C CG  . GLU A 1 4   ? 6.545   -4.136  -5.527  1.00 31.41  ? 589  GLU A CG  1 
ATOM   29   C CD  . GLU A 1 4   ? 6.621   -2.783  -6.179  1.00 33.78  ? 589  GLU A CD  1 
ATOM   30   O OE1 . GLU A 1 4   ? 6.556   -2.742  -7.419  1.00 34.37  ? 589  GLU A OE1 1 
ATOM   31   O OE2 . GLU A 1 4   ? 6.760   -1.828  -5.358  1.00 34.65  ? 589  GLU A OE2 1 
ATOM   32   N N   . LEU A 1 5   ? 9.339   -6.713  -3.167  1.00 21.52  ? 590  LEU A N   1 
ATOM   33   C CA  . LEU A 1 5   ? 10.455  -7.305  -2.467  1.00 19.64  ? 590  LEU A CA  1 
ATOM   34   C C   . LEU A 1 5   ? 11.372  -6.221  -1.896  1.00 19.81  ? 590  LEU A C   1 
ATOM   35   O O   . LEU A 1 5   ? 11.810  -6.342  -0.742  1.00 17.51  ? 590  LEU A O   1 
ATOM   36   C CB  . LEU A 1 5   ? 11.216  -8.218  -3.401  1.00 20.14  ? 590  LEU A CB  1 
ATOM   37   C CG  . LEU A 1 5   ? 12.509  -8.813  -2.844  1.00 19.49  ? 590  LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 5   ? 12.302  -9.603  -1.544  1.00 17.03  ? 590  LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 5   ? 13.179  -9.635  -3.902  1.00 20.82  ? 590  LEU A CD2 1 
ATOM   40   N N   . ILE A 1 6   ? 11.682  -5.208  -2.662  1.00 21.24  ? 591  ILE A N   1 
ATOM   41   C CA  . ILE A 1 6   ? 12.640  -4.203  -2.216  1.00 22.94  ? 591  ILE A CA  1 
ATOM   42   C C   . ILE A 1 6   ? 12.083  -3.470  -0.993  1.00 23.69  ? 591  ILE A C   1 
ATOM   43   O O   . ILE A 1 6   ? 12.855  -3.125  -0.091  1.00 25.67  ? 591  ILE A O   1 
ATOM   44   C CB  . ILE A 1 6   ? 13.063  -3.293  -3.381  1.00 29.48  ? 591  ILE A CB  1 
ATOM   45   C CG1 . ILE A 1 6   ? 14.245  -2.428  -3.011  1.00 32.14  ? 591  ILE A CG1 1 
ATOM   46   C CG2 . ILE A 1 6   ? 11.894  -2.491  -3.939  1.00 31.56  ? 591  ILE A CG2 1 
ATOM   47   C CD1 . ILE A 1 6   ? 14.992  -1.945  -4.248  1.00 36.30  ? 591  ILE A CD1 1 
ATOM   48   N N   . GLY A 1 7   ? 10.749  -3.310  -0.928  1.00 21.02  ? 592  GLY A N   1 
ATOM   49   C CA  . GLY A 1 7   ? 10.131  -2.735  0.265   1.00 20.33  ? 592  GLY A CA  1 
ATOM   50   C C   . GLY A 1 7   ? 10.259  -3.672  1.444   1.00 18.48  ? 592  GLY A C   1 
ATOM   51   O O   . GLY A 1 7   ? 10.517  -3.235  2.578   1.00 20.01  ? 592  GLY A O   1 
ATOM   52   N N   . ALA A 1 8   ? 9.922   -4.931  1.247   1.00 17.02  ? 593  ALA A N   1 
ATOM   53   C CA  . ALA A 1 8   ? 9.999   -5.931  2.303   1.00 15.01  ? 593  ALA A CA  1 
ATOM   54   C C   . ALA A 1 8   ? 11.411  -6.030  2.889   1.00 15.65  ? 593  ALA A C   1 
ATOM   55   O O   . ALA A 1 8   ? 11.583  -6.127  4.124   1.00 14.59  ? 593  ALA A O   1 
ATOM   56   C CB  . ALA A 1 8   ? 9.555   -7.266  1.785   1.00 14.46  ? 593  ALA A CB  1 
ATOM   57   N N   . GLN A 1 9   ? 12.430  -5.930  2.047   1.00 16.16  ? 594  GLN A N   1 
ATOM   58   C CA  . GLN A 1 9   ? 13.806  -6.099  2.487   1.00 15.69  ? 594  GLN A CA  1 
ATOM   59   C C   . GLN A 1 9   ? 14.243  -4.978  3.436   1.00 15.96  ? 594  GLN A C   1 
ATOM   60   O O   . GLN A 1 9   ? 15.237  -5.131  4.169   1.00 16.45  ? 594  GLN A O   1 
ATOM   61   C CB  . GLN A 1 9   ? 14.720  -6.157  1.277   1.00 17.34  ? 594  GLN A CB  1 
ATOM   62   C CG  . GLN A 1 9   ? 14.576  -7.472  0.528   1.00 18.18  ? 594  GLN A CG  1 
ATOM   63   C CD  . GLN A 1 9   ? 15.480  -7.519  -0.676  1.00 19.53  ? 594  GLN A CD  1 
ATOM   64   O OE1 . GLN A 1 9   ? 15.729  -6.506  -1.321  1.00 22.42  ? 594  GLN A OE1 1 
ATOM   65   N NE2 . GLN A 1 9   ? 16.026  -8.699  -0.938  1.00 20.92  ? 594  GLN A NE2 1 
ATOM   66   N N   . ALA A 1 10  ? 13.572  -3.837  3.443   1.00 16.45  ? 595  ALA A N   1 
ATOM   67   C CA  . ALA A 1 10  ? 13.909  -2.774  4.381   1.00 17.28  ? 595  ALA A CA  1 
ATOM   68   C C   . ALA A 1 10  ? 13.674  -3.198  5.834   1.00 16.55  ? 595  ALA A C   1 
ATOM   69   O O   . ALA A 1 10  ? 14.136  -2.486  6.714   1.00 19.02  ? 595  ALA A O   1 
ATOM   70   C CB  . ALA A 1 10  ? 13.130  -1.532  4.063   1.00 19.90  ? 595  ALA A CB  1 
ATOM   71   N N   . HIS A 1 11  ? 12.914  -4.257  6.033   1.00 13.84  ? 596  HIS A N   1 
ATOM   72   C CA  . HIS A 1 11  ? 12.553  -4.723  7.380   1.00 12.45  ? 596  HIS A CA  1 
ATOM   73   C C   . HIS A 1 11  ? 13.350  -5.968  7.790   1.00 12.48  ? 596  HIS A C   1 
ATOM   74   O O   . HIS A 1 11  ? 12.913  -6.730  8.666   1.00 12.10  ? 596  HIS A O   1 
ATOM   75   C CB  . HIS A 1 11  ? 11.053  -4.993  7.446   1.00 11.87  ? 596  HIS A CB  1 
ATOM   76   C CG  . HIS A 1 11  ? 10.276  -3.782  7.172   1.00 13.58  ? 596  HIS A CG  1 
ATOM   77   N ND1 . HIS A 1 11  ? 9.726   -3.370  5.948   1.00 15.77  ? 596  HIS A ND1 1 
ATOM   78   C CD2 . HIS A 1 11  ? 10.009  -2.824  7.993   1.00 12.47  ? 596  HIS A CD2 1 
ATOM   79   C CE1 . HIS A 1 11  ? 9.164   -2.210  6.112   1.00 13.67  ? 596  HIS A CE1 1 
ATOM   80   N NE2 . HIS A 1 11  ? 9.329   -1.825  7.396   1.00 18.03  ? 596  HIS A NE2 1 
ATOM   81   N N   . ALA A 1 12  ? 14.483  -6.211  7.133   1.00 13.52  ? 597  ALA A N   1 
ATOM   82   C CA  . ALA A 1 12  ? 15.381  -7.334  7.385   1.00 13.36  ? 597  ALA A CA  1 
ATOM   83   C C   . ALA A 1 12  ? 15.731  -7.458  8.874   1.00 13.02  ? 597  ALA A C   1 
ATOM   84   O O   . ALA A 1 12  ? 16.129  -6.462  9.483   1.00 14.86  ? 597  ALA A O   1 
ATOM   85   C CB  . ALA A 1 12  ? 16.663  -7.182  6.600   1.00 15.33  ? 597  ALA A CB  1 
ATOM   86   N N   . VAL A 1 13  ? 15.620  -8.680  9.362   1.00 12.10  ? 598  VAL A N   1 
ATOM   87   C CA  . VAL A 1 13  ? 15.995  -8.990  10.723  1.00 12.36  ? 598  VAL A CA  1 
ATOM   88   C C   . VAL A 1 13  ? 17.027  -10.116 10.714  1.00 13.01  ? 598  VAL A C   1 
ATOM   89   O O   . VAL A 1 13  ? 17.345  -10.685 9.677   1.00 15.71  ? 598  VAL A O   1 
ATOM   90   C CB  . VAL A 1 13  ? 14.796  -9.367  11.570  1.00 13.54  ? 598  VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 13  ? 13.891  -8.139  11.691  1.00 13.74  ? 598  VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 13  ? 14.065  -10.571 11.088  1.00 13.42  ? 598  VAL A CG2 1 
ATOM   93   N N   . ASN A 1 14  ? 17.563  -10.367 11.899  1.00 12.08  ? 599  ASN A N   1 
ATOM   94   C CA  A ASN A 1 14  ? 18.669  -11.290 12.116  0.46 13.08  ? 599  ASN A CA  1 
ATOM   95   C CA  B ASN A 1 14  ? 18.659  -11.305 12.099  0.54 13.15  ? 599  ASN A CA  1 
ATOM   96   C C   . ASN A 1 14  ? 18.137  -12.578 12.756  1.00 13.19  ? 599  ASN A C   1 
ATOM   97   O O   . ASN A 1 14  ? 17.976  -12.621 13.966  1.00 16.96  ? 599  ASN A O   1 
ATOM   98   C CB  A ASN A 1 14  ? 19.736  -10.619 12.961  0.46 14.11  ? 599  ASN A CB  1 
ATOM   99   C CB  B ASN A 1 14  ? 19.766  -10.778 12.987  0.54 14.22  ? 599  ASN A CB  1 
ATOM   100  C CG  A ASN A 1 14  ? 20.984  -11.442 13.122  0.46 15.53  ? 599  ASN A CG  1 
ATOM   101  C CG  B ASN A 1 14  ? 20.405  -9.532  12.445  0.54 16.36  ? 599  ASN A CG  1 
ATOM   102  O OD1 A ASN A 1 14  ? 21.241  -12.275 12.257  0.46 18.35  ? 599  ASN A OD1 1 
ATOM   103  O OD1 B ASN A 1 14  ? 20.550  -9.441  11.216  0.54 18.74  ? 599  ASN A OD1 1 
ATOM   104  N ND2 A ASN A 1 14  ? 21.788  -11.156 14.136  0.46 17.92  ? 599  ASN A ND2 1 
ATOM   105  N ND2 B ASN A 1 14  ? 20.757  -8.578  13.297  0.54 18.26  ? 599  ASN A ND2 1 
ATOM   106  N N   . VAL A 1 15  ? 17.913  -13.600 11.950  1.00 13.09  ? 600  VAL A N   1 
ATOM   107  C CA  . VAL A 1 15  ? 17.326  -14.853 12.418  1.00 14.37  ? 600  VAL A CA  1 
ATOM   108  C C   . VAL A 1 15  ? 18.434  -15.851 12.675  1.00 14.76  ? 600  VAL A C   1 
ATOM   109  O O   . VAL A 1 15  ? 19.356  -15.975 11.861  1.00 14.83  ? 600  VAL A O   1 
ATOM   110  C CB  . VAL A 1 15  ? 16.301  -15.365 11.396  1.00 14.78  ? 600  VAL A CB  1 
ATOM   111  C CG1 . VAL A 1 15  ? 15.781  -16.767 11.746  1.00 14.46  ? 600  VAL A CG1 1 
ATOM   112  C CG2 . VAL A 1 15  ? 15.139  -14.430 11.225  1.00 14.13  ? 600  VAL A CG2 1 
ATOM   113  N N   . ILE A 1 16  ? 18.303  -16.611 13.753  1.00 15.12  ? 601  ILE A N   1 
ATOM   114  C CA  . ILE A 1 16  ? 19.209  -17.730 14.005  1.00 17.83  ? 601  ILE A CA  1 
ATOM   115  C C   . ILE A 1 16  ? 18.392  -18.969 14.353  1.00 18.15  ? 601  ILE A C   1 
ATOM   116  O O   . ILE A 1 16  ? 17.233  -18.861 14.749  1.00 19.93  ? 601  ILE A O   1 
ATOM   117  C CB  . ILE A 1 16  ? 20.250  -17.440 15.078  1.00 24.13  ? 601  ILE A CB  1 
ATOM   118  C CG1 . ILE A 1 16  ? 19.578  -17.077 16.371  1.00 25.14  ? 601  ILE A CG1 1 
ATOM   119  C CG2 . ILE A 1 16  ? 21.235  -16.353 14.598  1.00 25.55  ? 601  ILE A CG2 1 
ATOM   120  C CD1 . ILE A 1 16  ? 20.559  -17.044 17.517  1.00 29.96  ? 601  ILE A CD1 1 
ATOM   121  N N   . LEU A 1 17  ? 18.975  -20.123 14.118  1.00 16.18  ? 602  LEU A N   1 
ATOM   122  C CA  . LEU A 1 17  ? 18.259  -21.372 14.402  1.00 16.58  ? 602  LEU A CA  1 
ATOM   123  C C   . LEU A 1 17  ? 18.391  -21.744 15.872  1.00 18.31  ? 602  LEU A C   1 
ATOM   124  O O   . LEU A 1 17  ? 19.424  -21.567 16.521  1.00 21.40  ? 602  LEU A O   1 
ATOM   125  C CB  . LEU A 1 17  ? 18.941  -22.409 13.531  1.00 17.25  ? 602  LEU A CB  1 
ATOM   126  C CG  . LEU A 1 17  ? 18.796  -22.142 12.036  1.00 16.66  ? 602  LEU A CG  1 
ATOM   127  C CD1 . LEU A 1 17  ? 19.686  -22.985 11.210  1.00 18.10  ? 602  LEU A CD1 1 
ATOM   128  C CD2 . LEU A 1 17  ? 17.359  -22.290 11.585  1.00 17.43  ? 602  LEU A CD2 1 
ATOM   129  N N   . ASP A 1 18  ? 17.292  -22.307 16.378  1.00 19.15  ? 603  ASP A N   1 
ATOM   130  C CA  . ASP A 1 18  ? 17.227  -22.854 17.731  1.00 21.79  ? 603  ASP A CA  1 
ATOM   131  C C   . ASP A 1 18  ? 17.599  -24.329 17.688  1.00 24.47  ? 603  ASP A C   1 
ATOM   132  O O   . ASP A 1 18  ? 16.774  -25.196 17.422  1.00 25.66  ? 603  ASP A O   1 
ATOM   133  C CB  . ASP A 1 18  ? 15.826  -22.667 18.279  1.00 25.11  ? 603  ASP A CB  1 
ATOM   134  C CG  . ASP A 1 18  ? 15.656  -23.146 19.710  1.00 33.09  ? 603  ASP A CG  1 
ATOM   135  O OD1 . ASP A 1 18  ? 16.607  -23.759 20.233  1.00 34.94  ? 603  ASP A OD1 1 
ATOM   136  O OD2 . ASP A 1 18  ? 14.573  -22.899 20.253  1.00 41.84  ? 603  ASP A OD2 1 
ATOM   137  N N   . ALA A 1 19  ? 18.844  -24.634 17.985  1.00 25.23  ? 604  ALA A N   1 
ATOM   138  C CA  . ALA A 1 19  ? 19.284  -26.017 17.847  1.00 28.88  ? 604  ALA A CA  1 
ATOM   139  C C   . ALA A 1 19  ? 18.699  -26.865 18.975  1.00 34.53  ? 604  ALA A C   1 
ATOM   140  O O   . ALA A 1 19  ? 18.622  -28.075 18.843  1.00 40.74  ? 604  ALA A O   1 
ATOM   141  C CB  . ALA A 1 19  ? 20.782  -26.060 17.818  1.00 30.49  ? 604  ALA A CB  1 
ATOM   142  N N   . GLU A 1 20  ? 18.278  -26.233 20.074  1.00 36.16  ? 605  GLU A N   1 
ATOM   143  C CA  . GLU A 1 20  ? 17.823  -26.963 21.243  1.00 44.64  ? 605  GLU A CA  1 
ATOM   144  C C   . GLU A 1 20  ? 16.589  -27.795 20.919  1.00 45.05  ? 605  GLU A C   1 
ATOM   145  O O   . GLU A 1 20  ? 16.444  -28.905 21.414  1.00 52.33  ? 605  GLU A O   1 
ATOM   146  C CB  . GLU A 1 20  ? 17.490  -26.042 22.413  1.00 48.74  ? 605  GLU A CB  1 
ATOM   147  C CG  . GLU A 1 20  ? 17.676  -26.733 23.753  1.00 60.25  ? 605  GLU A CG  1 
ATOM   148  C CD  . GLU A 1 20  ? 17.127  -25.919 24.900  1.00 66.32  ? 605  GLU A CD  1 
ATOM   149  O OE1 . GLU A 1 20  ? 16.561  -24.817 24.641  1.00 65.23  ? 605  GLU A OE1 1 
ATOM   150  O OE2 . GLU A 1 20  ? 17.273  -26.423 26.038  1.00 65.90  ? 605  GLU A OE2 1 
ATOM   151  N N   . THR A 1 21  ? 15.713  -27.276 20.075  1.00 44.13  ? 606  THR A N   1 
ATOM   152  C CA  . THR A 1 21  ? 14.427  -27.921 19.892  1.00 48.48  ? 606  THR A CA  1 
ATOM   153  C C   . THR A 1 21  ? 14.290  -28.499 18.481  1.00 44.53  ? 606  THR A C   1 
ATOM   154  O O   . THR A 1 21  ? 13.174  -28.813 18.056  1.00 45.89  ? 606  THR A O   1 
ATOM   155  C CB  . THR A 1 21  ? 13.375  -26.869 20.220  1.00 47.94  ? 606  THR A CB  1 
ATOM   156  O OG1 . THR A 1 21  ? 13.472  -25.869 19.195  1.00 39.04  ? 606  THR A OG1 1 
ATOM   157  C CG2 . THR A 1 21  ? 13.572  -26.351 21.639  1.00 50.38  ? 606  THR A CG2 1 
ATOM   158  N N   . ALA A 1 22  ? 15.431  -28.666 17.788  1.00 38.06  ? 607  ALA A N   1 
ATOM   159  C CA  . ALA A 1 22  ? 15.480  -29.243 16.451  1.00 36.89  ? 607  ALA A CA  1 
ATOM   160  C C   . ALA A 1 22  ? 15.236  -30.758 16.484  1.00 37.65  ? 607  ALA A C   1 
ATOM   161  O O   . ALA A 1 22  ? 15.654  -31.415 17.431  1.00 36.80  ? 607  ALA A O   1 
ATOM   162  C CB  . ALA A 1 22  ? 16.854  -28.972 15.901  1.00 36.81  ? 607  ALA A CB  1 
ATOM   163  N N   . TYR A 1 23  ? 14.571  -31.284 15.431  1.00 35.79  ? 608  TYR A N   1 
ATOM   164  C CA  . TYR A 1 23  ? 14.615  -32.710 15.103  1.00 38.69  ? 608  TYR A CA  1 
ATOM   165  C C   . TYR A 1 23  ? 16.061  -33.202 15.279  1.00 39.99  ? 608  TYR A C   1 
ATOM   166  O O   . TYR A 1 23  ? 16.976  -32.525 14.802  1.00 38.49  ? 608  TYR A O   1 
ATOM   167  C CB  . TYR A 1 23  ? 14.067  -32.878 13.678  1.00 37.90  ? 608  TYR A CB  1 
ATOM   168  C CG  . TYR A 1 23  ? 14.052  -34.331 13.221  1.00 42.15  ? 608  TYR A CG  1 
ATOM   169  C CD1 . TYR A 1 23  ? 13.017  -35.165 13.612  1.00 45.31  ? 608  TYR A CD1 1 
ATOM   170  C CD2 . TYR A 1 23  ? 15.046  -34.845 12.384  1.00 43.26  ? 608  TYR A CD2 1 
ATOM   171  C CE1 . TYR A 1 23  ? 13.002  -36.500 13.235  1.00 49.75  ? 608  TYR A CE1 1 
ATOM   172  C CE2 . TYR A 1 23  ? 15.033  -36.175 11.983  1.00 45.31  ? 608  TYR A CE2 1 
ATOM   173  C CZ  . TYR A 1 23  ? 14.004  -37.002 12.416  1.00 48.86  ? 608  TYR A CZ  1 
ATOM   174  O OH  . TYR A 1 23  ? 13.934  -38.316 12.056  1.00 50.68  ? 608  TYR A OH  1 
ATOM   175  N N   . PRO A 1 24  ? 16.333  -34.308 16.022  1.00 41.79  ? 609  PRO A N   1 
ATOM   176  C CA  . PRO A 1 24  ? 17.696  -34.599 16.477  1.00 43.28  ? 609  PRO A CA  1 
ATOM   177  C C   . PRO A 1 24  ? 18.726  -35.101 15.452  1.00 44.17  ? 609  PRO A C   1 
ATOM   178  O O   . PRO A 1 24  ? 19.905  -35.185 15.775  1.00 44.94  ? 609  PRO A O   1 
ATOM   179  C CB  . PRO A 1 24  ? 17.501  -35.667 17.555  1.00 46.41  ? 609  PRO A CB  1 
ATOM   180  C CG  . PRO A 1 24  ? 16.171  -36.309 17.183  1.00 46.47  ? 609  PRO A CG  1 
ATOM   181  C CD  . PRO A 1 24  ? 15.329  -35.226 16.586  1.00 44.83  ? 609  PRO A CD  1 
ATOM   182  N N   . ASN A 1 25  ? 18.332  -35.428 14.215  1.00 44.54  ? 610  ASN A N   1 
ATOM   183  C CA  . ASN A 1 25  ? 19.331  -35.792 13.215  1.00 44.37  ? 610  ASN A CA  1 
ATOM   184  C C   . ASN A 1 25  ? 19.772  -34.555 12.429  1.00 38.86  ? 610  ASN A C   1 
ATOM   185  O O   . ASN A 1 25  ? 20.502  -34.665 11.451  1.00 39.96  ? 610  ASN A O   1 
ATOM   186  C CB  . ASN A 1 25  ? 18.832  -36.888 12.283  1.00 46.98  ? 610  ASN A CB  1 
ATOM   187  C CG  . ASN A 1 25  ? 18.663  -38.203 13.006  1.00 53.06  ? 610  ASN A CG  1 
ATOM   188  O OD1 . ASN A 1 25  ? 17.543  -38.573 13.370  1.00 60.29  ? 610  ASN A OD1 1 
ATOM   189  N ND2 . ASN A 1 25  ? 19.758  -38.903 13.257  1.00 56.33  ? 610  ASN A ND2 1 
ATOM   190  N N   . LEU A 1 26  ? 19.319  -33.370 12.836  1.00 36.51  ? 611  LEU A N   1 
ATOM   191  C CA  . LEU A 1 26  ? 19.755  -32.143 12.205  1.00 32.17  ? 611  LEU A CA  1 
ATOM   192  C C   . LEU A 1 26  ? 21.164  -31.781 12.687  1.00 31.29  ? 611  LEU A C   1 
ATOM   193  O O   . LEU A 1 26  ? 21.565  -32.036 13.816  1.00 32.71  ? 611  LEU A O   1 
ATOM   194  C CB  . LEU A 1 26  ? 18.717  -31.048 12.449  1.00 29.99  ? 611  LEU A CB  1 
ATOM   195  C CG  . LEU A 1 26  ? 17.345  -31.293 11.828  1.00 28.78  ? 611  LEU A CG  1 
ATOM   196  C CD1 . LEU A 1 26  ? 16.403  -30.156 12.165  1.00 28.88  ? 611  LEU A CD1 1 
ATOM   197  C CD2 . LEU A 1 26  ? 17.403  -31.427 10.312  1.00 29.71  ? 611  LEU A CD2 1 
ATOM   198  N N   . ILE A 1 27  ? 21.914  -31.200 11.757  1.00 29.76  ? 612  ILE A N   1 
ATOM   199  C CA  . ILE A 1 27  ? 23.279  -30.757 11.945  1.00 28.37  ? 612  ILE A CA  1 
ATOM   200  C C   . ILE A 1 27  ? 23.290  -29.260 11.645  1.00 24.90  ? 612  ILE A C   1 
ATOM   201  O O   . ILE A 1 27  ? 22.685  -28.827 10.681  1.00 24.24  ? 612  ILE A O   1 
ATOM   202  C CB  . ILE A 1 27  ? 24.218  -31.451 10.970  1.00 30.37  ? 612  ILE A CB  1 
ATOM   203  C CG1 . ILE A 1 27  ? 24.270  -32.945 11.225  1.00 34.82  ? 612  ILE A CG1 1 
ATOM   204  C CG2 . ILE A 1 27  ? 25.577  -30.756 10.985  1.00 30.31  ? 612  ILE A CG2 1 
ATOM   205  C CD1 . ILE A 1 27  ? 25.295  -33.672 10.385  1.00 38.22  ? 612  ILE A CD1 1 
ATOM   206  N N   . PHE A 1 28  ? 23.841  -28.488 12.575  1.00 24.59  ? 613  PHE A N   1 
ATOM   207  C CA  . PHE A 1 28  ? 23.843  -27.034 12.461  1.00 23.91  ? 613  PHE A CA  1 
ATOM   208  C C   . PHE A 1 28  ? 25.247  -26.515 12.241  1.00 25.01  ? 613  PHE A C   1 
ATOM   209  O O   . PHE A 1 28  ? 26.197  -27.070 12.765  1.00 28.16  ? 613  PHE A O   1 
ATOM   210  C CB  . PHE A 1 28  ? 23.311  -26.363 13.723  1.00 24.49  ? 613  PHE A CB  1 
ATOM   211  C CG  . PHE A 1 28  ? 21.870  -26.721 13.953  1.00 24.52  ? 613  PHE A CG  1 
ATOM   212  C CD1 . PHE A 1 28  ? 21.527  -27.921 14.573  1.00 26.29  ? 613  PHE A CD1 1 
ATOM   213  C CD2 . PHE A 1 28  ? 20.874  -25.907 13.428  1.00 23.82  ? 613  PHE A CD2 1 
ATOM   214  C CE1 . PHE A 1 28  ? 20.191  -28.290 14.668  1.00 26.36  ? 613  PHE A CE1 1 
ATOM   215  C CE2 . PHE A 1 28  ? 19.546  -26.261 13.578  1.00 25.65  ? 613  PHE A CE2 1 
ATOM   216  C CZ  . PHE A 1 28  ? 19.214  -27.447 14.209  1.00 24.10  ? 613  PHE A CZ  1 
ATOM   217  N N   . SER A 1 29  ? 25.361  -25.392 11.544  1.00 24.51  ? 614  SER A N   1 
ATOM   218  C CA  . SER A 1 29  ? 26.625  -24.665 11.492  1.00 24.83  ? 614  SER A CA  1 
ATOM   219  C C   . SER A 1 29  ? 26.884  -23.986 12.841  1.00 26.33  ? 614  SER A C   1 
ATOM   220  O O   . SER A 1 29  ? 25.976  -23.674 13.601  1.00 25.35  ? 614  SER A O   1 
ATOM   221  C CB  . SER A 1 29  ? 26.604  -23.651 10.394  1.00 24.15  ? 614  SER A CB  1 
ATOM   222  O OG  . SER A 1 29  ? 25.539  -22.736 10.602  1.00 23.02  ? 614  SER A OG  1 
ATOM   223  N N   . ASP A 1 30  ? 28.156  -23.652 13.073  1.00 27.54  ? 615  ASP A N   1 
ATOM   224  C CA  . ASP A 1 30  ? 28.523  -23.048 14.338  1.00 30.95  ? 615  ASP A CA  1 
ATOM   225  C C   . ASP A 1 30  ? 27.800  -21.731 14.556  1.00 28.04  ? 615  ASP A C   1 
ATOM   226  O O   . ASP A 1 30  ? 27.475  -21.420 15.693  1.00 30.53  ? 615  ASP A O   1 
ATOM   227  C CB  . ASP A 1 30  ? 30.024  -22.827 14.445  1.00 33.58  ? 615  ASP A CB  1 
ATOM   228  C CG  . ASP A 1 30  ? 30.874  -24.028 14.824  1.00 42.53  ? 615  ASP A CG  1 
ATOM   229  O OD1 . ASP A 1 30  ? 30.336  -25.157 14.955  1.00 50.04  ? 615  ASP A OD1 1 
ATOM   230  O OD2 . ASP A 1 30  ? 32.102  -23.845 14.962  1.00 49.88  ? 615  ASP A OD2 1 
ATOM   231  N N   . ASP A 1 31  ? 27.501  -20.972 13.490  1.00 25.21  ? 616  ASP A N   1 
ATOM   232  C CA  . ASP A 1 31  ? 26.906  -19.662 13.616  1.00 24.28  ? 616  ASP A CA  1 
ATOM   233  C C   . ASP A 1 31  ? 25.376  -19.724 13.658  1.00 21.97  ? 616  ASP A C   1 
ATOM   234  O O   . ASP A 1 31  ? 24.688  -18.728 13.655  1.00 20.68  ? 616  ASP A O   1 
ATOM   235  C CB  . ASP A 1 31  ? 27.291  -18.748 12.472  1.00 25.39  ? 616  ASP A CB  1 
ATOM   236  C CG  . ASP A 1 31  ? 26.933  -19.219 11.065  1.00 26.27  ? 616  ASP A CG  1 
ATOM   237  O OD1 . ASP A 1 31  ? 26.212  -20.255 10.899  1.00 22.88  ? 616  ASP A OD1 1 
ATOM   238  O OD2 . ASP A 1 31  ? 27.385  -18.544 10.114  1.00 29.17  ? 616  ASP A OD2 1 
ATOM   239  N N   . LEU A 1 32  ? 24.853  -20.947 13.640  1.00 21.35  ? 617  LEU A N   1 
ATOM   240  C CA  . LEU A 1 32  ? 23.416  -21.172 13.731  1.00 19.87  ? 617  LEU A CA  1 
ATOM   241  C C   . LEU A 1 32  ? 22.633  -20.510 12.597  1.00 16.90  ? 617  LEU A C   1 
ATOM   242  O O   . LEU A 1 32  ? 21.448  -20.216 12.704  1.00 16.39  ? 617  LEU A O   1 
ATOM   243  C CB  . LEU A 1 32  ? 22.844  -20.785 15.098  1.00 21.35  ? 617  LEU A CB  1 
ATOM   244  C CG  . LEU A 1 32  ? 23.411  -21.605 16.255  1.00 25.47  ? 617  LEU A CG  1 
ATOM   245  C CD1 . LEU A 1 32  ? 22.948  -21.058 17.607  1.00 26.83  ? 617  LEU A CD1 1 
ATOM   246  C CD2 . LEU A 1 32  ? 23.015  -23.050 16.136  1.00 27.70  ? 617  LEU A CD2 1 
ATOM   247  N N   . LYS A 1 33  ? 23.251  -20.429 11.399  1.00 16.88  ? 618  LYS A N   1 
ATOM   248  C CA  . LYS A 1 33  ? 22.575  -19.911 10.229  1.00 15.85  ? 618  LYS A CA  1 
ATOM   249  C C   . LYS A 1 33  ? 22.218  -21.033 9.238   1.00 14.89  ? 618  LYS A C   1 
ATOM   250  O O   . LYS A 1 33  ? 21.370  -20.827 8.391   1.00 15.12  ? 618  LYS A O   1 
ATOM   251  C CB  . LYS A 1 33  ? 23.445  -18.914 9.461   1.00 17.01  ? 618  LYS A CB  1 
ATOM   252  C CG  . LYS A 1 33  ? 23.670  -17.630 10.217  1.00 19.93  ? 618  LYS A CG  1 
ATOM   253  C CD  . LYS A 1 33  ? 22.473  -16.723 10.384  1.00 21.92  ? 618  LYS A CD  1 
ATOM   254  C CE  . LYS A 1 33  ? 22.892  -15.540 11.179  1.00 25.08  ? 618  LYS A CE  1 
ATOM   255  N NZ  . LYS A 1 33  ? 21.735  -14.665 11.339  1.00 26.94  ? 618  LYS A NZ  1 
ATOM   256  N N   A SER A 1 34  ? 22.802  -22.211 9.408   0.50 15.33  ? 619  SER A N   1 
ATOM   257  N N   B SER A 1 34  ? 22.851  -22.215 9.332   0.50 16.26  ? 619  SER A N   1 
ATOM   258  C CA  A SER A 1 34  ? 22.518  -23.311 8.498   0.50 15.47  ? 619  SER A CA  1 
ATOM   259  C CA  B SER A 1 34  ? 22.680  -23.305 8.355   0.50 17.20  ? 619  SER A CA  1 
ATOM   260  C C   A SER A 1 34  ? 22.076  -24.556 9.262   0.50 16.37  ? 619  SER A C   1 
ATOM   261  C C   B SER A 1 34  ? 22.288  -24.601 9.106   0.50 17.71  ? 619  SER A C   1 
ATOM   262  O O   A SER A 1 34  ? 22.437  -24.819 10.410  0.50 16.82  ? 619  SER A O   1 
ATOM   263  O O   B SER A 1 34  ? 22.850  -24.904 10.171  0.50 18.29  ? 619  SER A O   1 
ATOM   264  C CB  A SER A 1 34  ? 23.724  -23.638 7.706   0.50 16.19  ? 619  SER A CB  1 
ATOM   265  C CB  B SER A 1 34  ? 23.986  -23.438 7.500   0.50 19.23  ? 619  SER A CB  1 
ATOM   266  O OG  A SER A 1 34  ? 24.192  -22.508 7.000   0.50 15.14  ? 619  SER A OG  1 
ATOM   267  O OG  B SER A 1 34  ? 23.926  -24.313 6.360   0.50 20.72  ? 619  SER A OG  1 
ATOM   268  N N   . VAL A 1 35  ? 21.335  -25.371 8.537   1.00 17.47  ? 620  VAL A N   1 
ATOM   269  C CA  . VAL A 1 35  ? 20.862  -26.633 9.077   1.00 18.36  ? 620  VAL A CA  1 
ATOM   270  C C   . VAL A 1 35  ? 20.712  -27.611 7.922   1.00 17.60  ? 620  VAL A C   1 
ATOM   271  O O   . VAL A 1 35  ? 20.151  -27.267 6.879   1.00 17.70  ? 620  VAL A O   1 
ATOM   272  C CB  . VAL A 1 35  ? 19.518  -26.463 9.822   1.00 18.85  ? 620  VAL A CB  1 
ATOM   273  C CG1 . VAL A 1 35  ? 18.409  -25.860 9.002   1.00 17.85  ? 620  VAL A CG1 1 
ATOM   274  C CG2 . VAL A 1 35  ? 19.118  -27.788 10.439  1.00 20.95  ? 620  VAL A CG2 1 
ATOM   275  N N   . ARG A 1 36  ? 21.183  -28.835 8.148   1.00 19.20  ? 621  ARG A N   1 
ATOM   276  C CA  . ARG A 1 36  ? 20.979  -29.907 7.191   1.00 19.89  ? 621  ARG A CA  1 
ATOM   277  C C   . ARG A 1 36  ? 20.586  -31.163 7.948   1.00 21.82  ? 621  ARG A C   1 
ATOM   278  O O   . ARG A 1 36  ? 20.840  -31.309 9.150   1.00 22.84  ? 621  ARG A O   1 
ATOM   279  C CB  . ARG A 1 36  ? 22.235  -30.098 6.334   1.00 21.26  ? 621  ARG A CB  1 
ATOM   280  C CG  . ARG A 1 36  ? 23.472  -30.551 7.086   1.00 23.29  ? 621  ARG A CG  1 
ATOM   281  C CD  . ARG A 1 36  ? 24.700  -30.477 6.231   1.00 25.07  ? 621  ARG A CD  1 
ATOM   282  N NE  . ARG A 1 36  ? 25.872  -30.994 6.950   1.00 30.15  ? 621  ARG A NE  1 
ATOM   283  C CZ  . ARG A 1 36  ? 26.125  -32.274 7.207   1.00 33.45  ? 621  ARG A CZ  1 
ATOM   284  N NH1 . ARG A 1 36  ? 25.426  -33.264 6.651   1.00 34.48  ? 621  ARG A NH1 1 
ATOM   285  N NH2 . ARG A 1 36  ? 27.104  -32.620 8.031   1.00 39.83  ? 621  ARG A NH2 1 
ATOM   286  N N   . LEU A 1 37  ? 20.053  -32.145 7.196   1.00 22.56  ? 622  LEU A N   1 
ATOM   287  C CA  . LEU A 1 37  ? 19.754  -33.442 7.758   1.00 25.85  ? 622  LEU A CA  1 
ATOM   288  C C   . LEU A 1 37  ? 20.979  -34.317 7.597   1.00 27.70  ? 622  LEU A C   1 
ATOM   289  O O   . LEU A 1 37  ? 21.415  -34.569 6.476   1.00 29.37  ? 622  LEU A O   1 
ATOM   290  C CB  . LEU A 1 37  ? 18.567  -34.012 6.990   1.00 26.18  ? 622  LEU A CB  1 
ATOM   291  C CG  . LEU A 1 37  ? 18.034  -35.334 7.540   1.00 29.34  ? 622  LEU A CG  1 
ATOM   292  C CD1 . LEU A 1 37  ? 17.667  -35.138 9.011   1.00 30.21  ? 622  LEU A CD1 1 
ATOM   293  C CD2 . LEU A 1 37  ? 16.864  -35.752 6.657   1.00 30.80  ? 622  LEU A CD2 1 
ATOM   294  N N   . GLY A 1 38  ? 21.501  -34.795 8.722   1.00 30.09  ? 623  GLY A N   1 
ATOM   295  C CA  . GLY A 1 38  ? 22.556  -35.810 8.739   1.00 35.33  ? 623  GLY A CA  1 
ATOM   296  C C   . GLY A 1 38  ? 21.989  -37.228 8.567   1.00 40.12  ? 623  GLY A C   1 
ATOM   297  O O   . GLY A 1 38  ? 20.839  -37.402 8.177   1.00 38.48  ? 623  GLY A O   1 
ATOM   298  N N   . ASN A 1 39  ? 22.777  -38.244 8.931   1.00 51.38  ? 624  ASN A N   1 
ATOM   299  C CA  . ASN A 1 39  ? 22.349  -39.640 8.872   1.00 58.08  ? 624  ASN A CA  1 
ATOM   300  C C   . ASN A 1 39  ? 21.654  -40.101 10.158  1.00 62.61  ? 624  ASN A C   1 
ATOM   301  O O   . ASN A 1 39  ? 21.427  -39.318 11.065  1.00 59.63  ? 624  ASN A O   1 
ATOM   302  C CB  . ASN A 1 39  ? 23.547  -40.532 8.575   1.00 63.78  ? 624  ASN A CB  1 
ATOM   303  C CG  . ASN A 1 39  ? 24.155  -40.186 7.240   1.00 68.69  ? 624  ASN A CG  1 
ATOM   304  O OD1 . ASN A 1 39  ? 25.340  -39.833 7.169   1.00 73.99  ? 624  ASN A OD1 1 
ATOM   305  N ND2 . ASN A 1 39  ? 23.358  -40.273 6.186   1.00 69.18  ? 624  ASN A ND2 1 
ATOM   306  N N   . LYS A 1 40  ? 21.338  -41.405 10.243  1.00 72.74  ? 625  LYS A N   1 
ATOM   307  C CA  . LYS A 1 40  ? 20.749  -41.989 11.445  1.00 78.58  ? 625  LYS A CA  1 
ATOM   308  C C   . LYS A 1 40  ? 21.724  -41.975 12.633  1.00 84.31  ? 625  LYS A C   1 
ATOM   309  O O   . LYS A 1 40  ? 21.286  -42.020 13.782  1.00 86.90  ? 625  LYS A O   1 
ATOM   310  C CB  . LYS A 1 40  ? 20.256  -43.421 11.191  1.00 78.93  ? 625  LYS A CB  1 
ATOM   311  C CG  . LYS A 1 40  ? 19.009  -43.569 10.328  1.00 78.85  ? 625  LYS A CG  1 
ATOM   312  C CD  . LYS A 1 40  ? 18.185  -44.817 10.648  1.00 83.56  ? 625  LYS A CD  1 
ATOM   313  C CE  . LYS A 1 40  ? 18.935  -46.116 10.563  1.00 87.98  ? 625  LYS A CE  1 
ATOM   314  N NZ  . LYS A 1 40  ? 19.149  -46.538 9.175   1.00 89.35  ? 625  LYS A NZ  1 
ATOM   315  N N   . TRP A 1 41  ? 23.038  -41.905 12.369  1.00 88.53  ? 626  TRP A N   1 
ATOM   316  C CA  . TRP A 1 41  ? 24.056  -41.945 13.416  1.00 93.85  ? 626  TRP A CA  1 
ATOM   317  C C   . TRP A 1 41  ? 24.532  -40.539 13.803  1.00 89.25  ? 626  TRP A C   1 
ATOM   318  O O   . TRP A 1 41  ? 25.307  -40.383 14.747  1.00 86.15  ? 626  TRP A O   1 
ATOM   319  C CB  . TRP A 1 41  ? 25.242  -42.825 12.985  1.00 98.14  ? 626  TRP A CB  1 
ATOM   320  C CG  . TRP A 1 41  ? 25.752  -42.527 11.598  1.00 105.15 ? 626  TRP A CG  1 
ATOM   321  C CD1 . TRP A 1 41  ? 26.695  -41.606 11.241  1.00 108.07 ? 626  TRP A CD1 1 
ATOM   322  C CD2 . TRP A 1 41  ? 25.311  -43.150 10.369  1.00 111.57 ? 626  TRP A CD2 1 
ATOM   323  N NE1 . TRP A 1 41  ? 26.880  -41.617 9.882   1.00 111.22 ? 626  TRP A NE1 1 
ATOM   324  C CE2 . TRP A 1 41  ? 26.045  -42.550 9.319   1.00 111.11 ? 626  TRP A CE2 1 
ATOM   325  C CE3 . TRP A 1 41  ? 24.375  -44.148 10.057  1.00 111.07 ? 626  TRP A CE3 1 
ATOM   326  C CZ2 . TRP A 1 41  ? 25.867  -42.920 7.985   1.00 108.94 ? 626  TRP A CZ2 1 
ATOM   327  C CZ3 . TRP A 1 41  ? 24.200  -44.507 8.737   1.00 110.58 ? 626  TRP A CZ3 1 
ATOM   328  C CH2 . TRP A 1 41  ? 24.933  -43.897 7.717   1.00 108.94 ? 626  TRP A CH2 1 
ATOM   329  N N   . GLU A 1 42  ? 24.082  -39.509 13.075  1.00 81.06  ? 627  GLU A N   1 
ATOM   330  C CA  . GLU A 1 42  ? 24.400  -38.138 13.435  1.00 78.81  ? 627  GLU A CA  1 
ATOM   331  C C   . GLU A 1 42  ? 23.192  -37.551 14.158  1.00 75.28  ? 627  GLU A C   1 
ATOM   332  O O   . GLU A 1 42  ? 22.177  -37.265 13.526  1.00 70.41  ? 627  GLU A O   1 
ATOM   333  C CB  . GLU A 1 42  ? 24.786  -37.347 12.186  1.00 76.78  ? 627  GLU A CB  1 
ATOM   334  C CG  . GLU A 1 42  ? 25.845  -38.043 11.334  1.00 78.22  ? 627  GLU A CG  1 
ATOM   335  C CD  . GLU A 1 42  ? 26.163  -37.276 10.068  1.00 74.14  ? 627  GLU A CD  1 
ATOM   336  O OE1 . GLU A 1 42  ? 25.316  -37.302 9.150   1.00 71.40  ? 627  GLU A OE1 1 
ATOM   337  O OE2 . GLU A 1 42  ? 27.218  -36.608 10.017  1.00 73.30  ? 627  GLU A OE2 1 
ATOM   338  N N   . ARG A 1 43  ? 23.310  -37.412 15.487  1.00 75.34  ? 628  ARG A N   1 
ATOM   339  C CA  . ARG A 1 43  ? 22.190  -37.051 16.347  1.00 78.13  ? 628  ARG A CA  1 
ATOM   340  C C   . ARG A 1 43  ? 22.607  -35.955 17.334  1.00 72.57  ? 628  ARG A C   1 
ATOM   341  O O   . ARG A 1 43  ? 23.734  -35.957 17.822  1.00 71.15  ? 628  ARG A O   1 
ATOM   342  C CB  . ARG A 1 43  ? 21.687  -38.302 17.083  1.00 82.64  ? 628  ARG A CB  1 
ATOM   343  C CG  . ARG A 1 43  ? 21.030  -39.359 16.204  1.00 84.90  ? 628  ARG A CG  1 
ATOM   344  C CD  . ARG A 1 43  ? 20.666  -40.646 16.950  1.00 91.42  ? 628  ARG A CD  1 
ATOM   345  N NE  . ARG A 1 43  ? 19.811  -40.405 18.118  1.00 95.29  ? 628  ARG A NE  1 
ATOM   346  C CZ  . ARG A 1 43  ? 18.611  -39.828 18.085  1.00 96.49  ? 628  ARG A CZ  1 
ATOM   347  N NH1 . ARG A 1 43  ? 18.023  -39.575 16.929  1.00 91.76  ? 628  ARG A NH1 1 
ATOM   348  N NH2 . ARG A 1 43  ? 17.987  -39.523 19.209  1.00 100.54 ? 628  ARG A NH2 1 
ATOM   349  N N   . LEU A 1 44  ? 21.685  -35.029 17.632  1.00 65.50  ? 629  LEU A N   1 
ATOM   350  C CA  . LEU A 1 44  ? 21.879  -34.021 18.670  1.00 65.77  ? 629  LEU A CA  1 
ATOM   351  C C   . LEU A 1 44  ? 21.546  -34.636 20.031  1.00 71.13  ? 629  LEU A C   1 
ATOM   352  O O   . LEU A 1 44  ? 20.845  -35.646 20.067  1.00 70.76  ? 629  LEU A O   1 
ATOM   353  C CB  . LEU A 1 44  ? 20.979  -32.818 18.386  1.00 61.22  ? 629  LEU A CB  1 
ATOM   354  C CG  . LEU A 1 44  ? 21.179  -32.122 17.033  1.00 56.82  ? 629  LEU A CG  1 
ATOM   355  C CD1 . LEU A 1 44  ? 19.973  -31.252 16.712  1.00 52.00  ? 629  LEU A CD1 1 
ATOM   356  C CD2 . LEU A 1 44  ? 22.467  -31.297 17.017  1.00 57.50  ? 629  LEU A CD2 1 
ATOM   357  N N   . PRO A 1 45  ? 21.991  -34.049 21.178  1.00 73.93  ? 630  PRO A N   1 
ATOM   358  C CA  . PRO A 1 45  ? 21.675  -34.601 22.498  1.00 79.04  ? 630  PRO A CA  1 
ATOM   359  C C   . PRO A 1 45  ? 20.171  -34.655 22.775  1.00 80.71  ? 630  PRO A C   1 
ATOM   360  O O   . PRO A 1 45  ? 19.450  -33.709 22.465  1.00 80.05  ? 630  PRO A O   1 
ATOM   361  C CB  . PRO A 1 45  ? 22.415  -33.687 23.485  1.00 78.44  ? 630  PRO A CB  1 
ATOM   362  C CG  . PRO A 1 45  ? 23.403  -32.897 22.644  1.00 77.50  ? 630  PRO A CG  1 
ATOM   363  C CD  . PRO A 1 45  ? 22.825  -32.835 21.255  1.00 73.98  ? 630  PRO A CD  1 
ATOM   364  N N   . ASP A 1 46  ? 19.705  -35.766 23.363  1.00 83.43  ? 631  ASP A N   1 
ATOM   365  C CA  . ASP A 1 46  ? 18.280  -36.044 23.510  1.00 86.57  ? 631  ASP A CA  1 
ATOM   366  C C   . ASP A 1 46  ? 17.602  -34.997 24.396  1.00 85.27  ? 631  ASP A C   1 
ATOM   367  O O   . ASP A 1 46  ? 18.248  -34.364 25.229  1.00 86.61  ? 631  ASP A O   1 
ATOM   368  C CB  . ASP A 1 46  ? 18.052  -37.433 24.089  1.00 92.23  ? 631  ASP A CB  1 
ATOM   369  C CG  . ASP A 1 46  ? 18.454  -38.607 23.206  1.00 93.73  ? 631  ASP A CG  1 
ATOM   370  O OD1 . ASP A 1 46  ? 18.684  -39.703 23.775  1.00 97.18  ? 631  ASP A OD1 1 
ATOM   371  O OD2 . ASP A 1 46  ? 18.505  -38.425 21.964  1.00 88.58  ? 631  ASP A OD2 1 
ATOM   372  N N   . GLY A 1 47  ? 16.284  -34.830 24.220  1.00 82.44  ? 632  GLY A N   1 
ATOM   373  C CA  . GLY A 1 47  ? 15.536  -33.873 25.022  1.00 81.49  ? 632  GLY A CA  1 
ATOM   374  C C   . GLY A 1 47  ? 14.028  -33.946 24.781  1.00 78.87  ? 632  GLY A C   1 
ATOM   375  O O   . GLY A 1 47  ? 13.587  -34.226 23.669  1.00 70.45  ? 632  GLY A O   1 
ATOM   376  N N   . PRO A 1 48  ? 13.190  -33.664 25.809  1.00 83.93  ? 633  PRO A N   1 
ATOM   377  C CA  . PRO A 1 48  ? 11.736  -33.682 25.655  1.00 83.59  ? 633  PRO A CA  1 
ATOM   378  C C   . PRO A 1 48  ? 11.154  -32.520 24.849  1.00 79.50  ? 633  PRO A C   1 
ATOM   379  O O   . PRO A 1 48  ? 9.955   -32.503 24.584  1.00 82.03  ? 633  PRO A O   1 
ATOM   380  C CB  . PRO A 1 48  ? 11.212  -33.623 27.095  1.00 87.88  ? 633  PRO A CB  1 
ATOM   381  C CG  . PRO A 1 48  ? 12.431  -33.850 27.985  1.00 90.63  ? 633  PRO A CG  1 
ATOM   382  C CD  . PRO A 1 48  ? 13.597  -33.352 27.191  1.00 87.55  ? 633  PRO A CD  1 
ATOM   383  N N   . GLN A 1 49  ? 12.009  -31.563 24.460  1.00 71.57  ? 634  GLN A N   1 
ATOM   384  C CA  . GLN A 1 49  ? 11.580  -30.325 23.835  1.00 66.96  ? 634  GLN A CA  1 
ATOM   385  C C   . GLN A 1 49  ? 11.694  -30.396 22.306  1.00 60.04  ? 634  GLN A C   1 
ATOM   386  O O   . GLN A 1 49  ? 11.281  -29.453 21.628  1.00 54.39  ? 634  GLN A O   1 
ATOM   387  C CB  . GLN A 1 49  ? 12.384  -29.156 24.421  1.00 68.51  ? 634  GLN A CB  1 
ATOM   388  C CG  . GLN A 1 49  ? 13.834  -29.047 23.945  1.00 67.33  ? 634  GLN A CG  1 
ATOM   389  C CD  . GLN A 1 49  ? 14.774  -30.064 24.560  1.00 72.62  ? 634  GLN A CD  1 
ATOM   390  O OE1 . GLN A 1 49  ? 14.467  -30.710 25.571  1.00 76.74  ? 634  GLN A OE1 1 
ATOM   391  N NE2 . GLN A 1 49  ? 15.945  -30.210 23.955  1.00 70.58  ? 634  GLN A NE2 1 
ATOM   392  N N   . ARG A 1 50  ? 12.232  -31.498 21.754  1.00 54.30  ? 635  ARG A N   1 
ATOM   393  C CA  . ARG A 1 50  ? 12.541  -31.566 20.321  1.00 51.11  ? 635  ARG A CA  1 
ATOM   394  C C   . ARG A 1 50  ? 11.350  -32.078 19.501  1.00 50.39  ? 635  ARG A C   1 
ATOM   395  O O   . ARG A 1 50  ? 10.462  -32.766 20.012  1.00 48.25  ? 635  ARG A O   1 
ATOM   396  C CB  . ARG A 1 50  ? 13.744  -32.470 20.005  1.00 50.00  ? 635  ARG A CB  1 
ATOM   397  C CG  . ARG A 1 50  ? 15.077  -31.954 20.532  1.00 50.76  ? 635  ARG A CG  1 
ATOM   398  C CD  . ARG A 1 50  ? 16.240  -32.894 20.275  1.00 51.50  ? 635  ARG A CD  1 
ATOM   399  N NE  . ARG A 1 50  ? 17.495  -32.363 20.822  1.00 53.37  ? 635  ARG A NE  1 
ATOM   400  C CZ  . ARG A 1 50  ? 18.185  -31.330 20.319  1.00 53.70  ? 635  ARG A CZ  1 
ATOM   401  N NH1 . ARG A 1 50  ? 19.267  -30.891 20.947  1.00 53.59  ? 635  ARG A NH1 1 
ATOM   402  N NH2 . ARG A 1 50  ? 17.808  -30.735 19.189  1.00 49.38  ? 635  ARG A NH2 1 
ATOM   403  N N   . PHE A 1 51  ? 11.383  -31.768 18.192  1.00 47.68  ? 636  PHE A N   1 
ATOM   404  C CA  . PHE A 1 51  ? 10.515  -32.400 17.206  1.00 47.75  ? 636  PHE A CA  1 
ATOM   405  C C   . PHE A 1 51  ? 10.954  -33.854 17.062  1.00 53.38  ? 636  PHE A C   1 
ATOM   406  O O   . PHE A 1 51  ? 12.141  -34.113 16.892  1.00 53.53  ? 636  PHE A O   1 
ATOM   407  C CB  . PHE A 1 51  ? 10.568  -31.628 15.883  1.00 48.59  ? 636  PHE A CB  1 
ATOM   408  C CG  . PHE A 1 51  ? 9.923   -30.250 15.971  1.00 48.00  ? 636  PHE A CG  1 
ATOM   409  C CD1 . PHE A 1 51  ? 8.578   -30.075 15.649  1.00 52.76  ? 636  PHE A CD1 1 
ATOM   410  C CD2 . PHE A 1 51  ? 10.651  -29.137 16.389  1.00 49.57  ? 636  PHE A CD2 1 
ATOM   411  C CE1 . PHE A 1 51  ? 7.987   -28.817 15.708  1.00 51.30  ? 636  PHE A CE1 1 
ATOM   412  C CE2 . PHE A 1 51  ? 10.055  -27.889 16.468  1.00 51.10  ? 636  PHE A CE2 1 
ATOM   413  C CZ  . PHE A 1 51  ? 8.718   -27.731 16.141  1.00 51.72  ? 636  PHE A CZ  1 
ATOM   414  N N   . ASP A 1 52  ? 9.994   -34.784 17.166  1.00 56.10  ? 637  ASP A N   1 
ATOM   415  C CA  . ASP A 1 52  ? 10.287  -36.211 17.181  1.00 60.81  ? 637  ASP A CA  1 
ATOM   416  C C   . ASP A 1 52  ? 9.904   -36.877 15.858  1.00 65.14  ? 637  ASP A C   1 
ATOM   417  O O   . ASP A 1 52  ? 10.325  -38.008 15.617  1.00 62.45  ? 637  ASP A O   1 
ATOM   418  C CB  . ASP A 1 52  ? 9.602   -36.923 18.343  1.00 62.72  ? 637  ASP A CB  1 
ATOM   419  C CG  . ASP A 1 52  ? 8.073   -36.922 18.354  1.00 63.68  ? 637  ASP A CG  1 
ATOM   420  O OD1 . ASP A 1 52  ? 7.456   -36.160 17.573  1.00 59.70  ? 637  ASP A OD1 1 
ATOM   421  O OD2 . ASP A 1 52  ? 7.500   -37.704 19.140  1.00 67.96  ? 637  ASP A OD2 1 
ATOM   422  N N   . SER A 1 53  ? 9.077   -36.214 15.026  1.00 66.34  ? 638  SER A N   1 
ATOM   423  C CA  . SER A 1 53  ? 8.640   -36.803 13.762  1.00 69.47  ? 638  SER A CA  1 
ATOM   424  C C   . SER A 1 53  ? 8.991   -35.891 12.592  1.00 67.61  ? 638  SER A C   1 
ATOM   425  O O   . SER A 1 53  ? 9.599   -36.337 11.616  1.00 72.51  ? 638  SER A O   1 
ATOM   426  C CB  . SER A 1 53  ? 7.161   -37.153 13.752  1.00 73.05  ? 638  SER A CB  1 
ATOM   427  O OG  . SER A 1 53  ? 6.360   -36.214 14.460  1.00 78.19  ? 638  SER A OG  1 
ATOM   428  N N   . CYS A 1 54  ? 8.581   -34.621 12.692  1.00 59.46  ? 639  CYS A N   1 
ATOM   429  C CA  . CYS A 1 54  ? 8.774   -33.670 11.610  1.00 51.58  ? 639  CYS A CA  1 
ATOM   430  C C   . CYS A 1 54  ? 10.209  -33.164 11.642  1.00 43.40  ? 639  CYS A C   1 
ATOM   431  O O   . CYS A 1 54  ? 10.748  -32.862 12.712  1.00 38.98  ? 639  CYS A O   1 
ATOM   432  C CB  . CYS A 1 54  ? 7.767   -32.534 11.697  1.00 55.40  ? 639  CYS A CB  1 
ATOM   433  S SG  . CYS A 1 54  ? 6.069   -33.101 11.409  1.00 63.78  ? 639  CYS A SG  1 
ATOM   434  N N   . ILE A 1 55  ? 10.805  -33.088 10.450  1.00 36.25  ? 640  ILE A N   1 
ATOM   435  C CA  . ILE A 1 55  ? 12.184  -32.666 10.323  1.00 31.54  ? 640  ILE A CA  1 
ATOM   436  C C   . ILE A 1 55  ? 12.167  -31.137 10.382  1.00 26.81  ? 640  ILE A C   1 
ATOM   437  O O   . ILE A 1 55  ? 12.425  -30.450 9.416   1.00 26.40  ? 640  ILE A O   1 
ATOM   438  C CB  . ILE A 1 55  ? 12.794  -33.239 9.035   1.00 33.70  ? 640  ILE A CB  1 
ATOM   439  C CG1 . ILE A 1 55  ? 12.640  -34.767 9.034   1.00 39.56  ? 640  ILE A CG1 1 
ATOM   440  C CG2 . ILE A 1 55  ? 14.261  -32.852 8.879   1.00 35.33  ? 640  ILE A CG2 1 
ATOM   441  C CD1 . ILE A 1 55  ? 13.123  -35.461 7.774   1.00 45.20  ? 640  ILE A CD1 1 
ATOM   442  N N   . ILE A 1 56  ? 11.840  -30.623 11.547  1.00 26.29  ? 641  ILE A N   1 
ATOM   443  C CA  . ILE A 1 56  ? 11.597  -29.196 11.714  1.00 25.82  ? 641  ILE A CA  1 
ATOM   444  C C   . ILE A 1 56  ? 12.630  -28.597 12.654  1.00 24.73  ? 641  ILE A C   1 
ATOM   445  O O   . ILE A 1 56  ? 12.999  -29.225 13.662  1.00 24.73  ? 641  ILE A O   1 
ATOM   446  C CB  . ILE A 1 56  ? 10.180  -28.958 12.254  1.00 28.63  ? 641  ILE A CB  1 
ATOM   447  C CG1 . ILE A 1 56  ? 9.113   -29.343 11.219  1.00 32.99  ? 641  ILE A CG1 1 
ATOM   448  C CG2 . ILE A 1 56  ? 9.985   -27.511 12.696  1.00 30.18  ? 641  ILE A CG2 1 
ATOM   449  C CD1 . ILE A 1 56  ? 9.126   -28.488 9.970   1.00 32.90  ? 641  ILE A CD1 1 
ATOM   450  N N   . VAL A 1 57  ? 12.959  -27.322 12.367  1.00 20.70  ? 642  VAL A N   1 
ATOM   451  C CA  . VAL A 1 57  ? 13.724  -26.518 13.300  1.00 20.51  ? 642  VAL A CA  1 
ATOM   452  C C   . VAL A 1 57  ? 13.057  -25.155 13.357  1.00 16.83  ? 642  VAL A C   1 
ATOM   453  O O   . VAL A 1 57  ? 12.606  -24.629 12.366  1.00 16.41  ? 642  VAL A O   1 
ATOM   454  C CB  . VAL A 1 57  ? 15.257  -26.402 13.080  1.00 22.56  ? 642  VAL A CB  1 
ATOM   455  C CG1 . VAL A 1 57  ? 15.625  -25.950 11.736  1.00 21.97  ? 642  VAL A CG1 1 
ATOM   456  C CG2 . VAL A 1 57  ? 15.991  -25.504 14.075  1.00 25.78  ? 642  VAL A CG2 1 
ATOM   457  N N   . LEU A 1 58  ? 13.057  -24.578 14.578  1.00 16.53  ? 643  LEU A N   1 
ATOM   458  C CA  . LEU A 1 58  ? 12.540  -23.242 14.790  1.00 15.76  ? 643  LEU A CA  1 
ATOM   459  C C   . LEU A 1 58  ? 13.663  -22.246 14.769  1.00 15.64  ? 643  LEU A C   1 
ATOM   460  O O   . LEU A 1 58  ? 14.820  -22.604 15.059  1.00 16.76  ? 643  LEU A O   1 
ATOM   461  C CB  . LEU A 1 58  ? 11.820  -23.208 16.138  1.00 17.13  ? 643  LEU A CB  1 
ATOM   462  C CG  . LEU A 1 58  ? 10.654  -24.198 16.235  1.00 20.15  ? 643  LEU A CG  1 
ATOM   463  C CD1 . LEU A 1 58  ? 10.131  -24.225 17.656  1.00 23.30  ? 643  LEU A CD1 1 
ATOM   464  C CD2 . LEU A 1 58  ? 9.605   -23.879 15.240  1.00 22.01  ? 643  LEU A CD2 1 
ATOM   465  N N   . GLY A 1 59  ? 13.280  -21.017 14.526  1.00 15.76  ? 644  GLY A N   1 
ATOM   466  C CA  . GLY A 1 59  ? 14.207  -19.905 14.556  1.00 16.23  ? 644  GLY A CA  1 
ATOM   467  C C   . GLY A 1 59  ? 13.879  -18.927 15.667  1.00 17.03  ? 644  GLY A C   1 
ATOM   468  O O   . GLY A 1 59  ? 12.791  -18.865 16.215  1.00 17.02  ? 644  GLY A O   1 
ATOM   469  N N   . SER A 1 60  ? 14.875  -18.092 15.934  1.00 18.09  ? 645  SER A N   1 
ATOM   470  C CA  A SER A 1 60  ? 14.711  -16.958 16.824  0.40 21.10  ? 645  SER A CA  1 
ATOM   471  C CA  B SER A 1 60  ? 14.711  -16.962 16.826  0.60 22.00  ? 645  SER A CA  1 
ATOM   472  C C   . SER A 1 60  ? 15.039  -15.693 16.057  1.00 23.63  ? 645  SER A C   1 
ATOM   473  O O   . SER A 1 60  ? 15.788  -15.742 15.103  1.00 22.01  ? 645  SER A O   1 
ATOM   474  C CB  A SER A 1 60  ? 15.600  -17.048 18.019  0.40 24.48  ? 645  SER A CB  1 
ATOM   475  C CB  B SER A 1 60  ? 15.586  -17.103 18.035  0.60 27.94  ? 645  SER A CB  1 
ATOM   476  O OG  A SER A 1 60  ? 16.788  -16.297 17.791  0.40 23.68  ? 645  SER A OG  1 
ATOM   477  O OG  B SER A 1 60  ? 15.687  -18.460 18.444  0.60 30.49  ? 645  SER A OG  1 
ATOM   478  N N   . PRO A 1 61  ? 14.534  -14.516 16.405  1.00 25.44  ? 646  PRO A N   1 
ATOM   479  C CA  . PRO A 1 61  ? 13.650  -14.295 17.535  1.00 24.25  ? 646  PRO A CA  1 
ATOM   480  C C   . PRO A 1 61  ? 12.202  -14.680 17.262  1.00 18.72  ? 646  PRO A C   1 
ATOM   481  O O   . PRO A 1 61  ? 11.755  -14.722 16.140  1.00 19.87  ? 646  PRO A O   1 
ATOM   482  C CB  . PRO A 1 61  ? 13.693  -12.743 17.617  1.00 27.08  ? 646  PRO A CB  1 
ATOM   483  C CG  . PRO A 1 61  ? 14.927  -12.353 16.837  1.00 28.70  ? 646  PRO A CG  1 
ATOM   484  C CD  . PRO A 1 61  ? 14.811  -13.281 15.656  1.00 27.41  ? 646  PRO A CD  1 
ATOM   485  N N   . SER A 1 62  ? 11.472  -14.905 18.355  1.00 17.98  ? 647  SER A N   1 
ATOM   486  C CA  A SER A 1 62  ? 10.022  -14.875 18.384  0.36 18.33  ? 647  SER A CA  1 
ATOM   487  C CA  B SER A 1 62  ? 10.018  -14.864 18.287  0.64 18.01  ? 647  SER A CA  1 
ATOM   488  C C   . SER A 1 62  ? 9.645   -13.405 18.437  1.00 19.45  ? 647  SER A C   1 
ATOM   489  O O   . SER A 1 62  ? 10.426  -12.636 19.014  1.00 28.78  ? 647  SER A O   1 
ATOM   490  C CB  A SER A 1 62  ? 9.529   -15.649 19.583  0.36 19.96  ? 647  SER A CB  1 
ATOM   491  C CB  B SER A 1 62  ? 9.338   -15.694 19.307  0.64 20.61  ? 647  SER A CB  1 
ATOM   492  O OG  A SER A 1 62  ? 10.054  -16.976 19.514  0.36 21.31  ? 647  SER A OG  1 
ATOM   493  O OG  B SER A 1 62  ? 9.785   -15.327 20.588  0.64 22.25  ? 647  SER A OG  1 
ATOM   494  N N   . PHE A 1 63  ? 8.573   -13.008 17.808  1.00 15.34  ? 648  PHE A N   1 
ATOM   495  C CA  . PHE A 1 63  ? 8.173   -11.614 17.810  1.00 14.31  ? 648  PHE A CA  1 
ATOM   496  C C   . PHE A 1 63  ? 6.663   -11.507 17.843  1.00 14.36  ? 648  PHE A C   1 
ATOM   497  O O   . PHE A 1 63  ? 5.944   -12.441 17.441  1.00 15.51  ? 648  PHE A O   1 
ATOM   498  C CB  . PHE A 1 63  ? 8.730   -10.837 16.622  1.00 13.85  ? 648  PHE A CB  1 
ATOM   499  C CG  . PHE A 1 63  ? 8.349   -11.418 15.270  1.00 14.19  ? 648  PHE A CG  1 
ATOM   500  C CD1 . PHE A 1 63  ? 9.103   -12.421 14.735  1.00 15.38  ? 648  PHE A CD1 1 
ATOM   501  C CD2 . PHE A 1 63  ? 7.199   -11.022 14.616  1.00 16.31  ? 648  PHE A CD2 1 
ATOM   502  C CE1 . PHE A 1 63  ? 8.777   -12.992 13.510  1.00 15.57  ? 648  PHE A CE1 1 
ATOM   503  C CE2 . PHE A 1 63  ? 6.867   -11.571 13.382  1.00 15.94  ? 648  PHE A CE2 1 
ATOM   504  C CZ  . PHE A 1 63  ? 7.626   -12.586 12.867  1.00 17.27  ? 648  PHE A CZ  1 
ATOM   505  N N   . LEU A 1 64  ? 6.187   -10.363 18.284  1.00 14.53  ? 649  LEU A N   1 
ATOM   506  C CA  . LEU A 1 64  ? 4.747   -10.159 18.353  1.00 16.78  ? 649  LEU A CA  1 
ATOM   507  C C   . LEU A 1 64  ? 4.347   -8.757  17.940  1.00 15.42  ? 649  LEU A C   1 
ATOM   508  O O   . LEU A 1 64  ? 3.342   -8.262  18.374  1.00 16.61  ? 649  LEU A O   1 
ATOM   509  C CB  . LEU A 1 64  ? 4.159   -10.557 19.682  1.00 21.02  ? 649  LEU A CB  1 
ATOM   510  C CG  . LEU A 1 64  ? 4.750   -9.812  20.848  1.00 21.61  ? 649  LEU A CG  1 
ATOM   511  C CD1 . LEU A 1 64  ? 3.704   -9.482  21.918  1.00 24.43  ? 649  LEU A CD1 1 
ATOM   512  C CD2 . LEU A 1 64  ? 5.910   -10.634 21.454  1.00 24.48  ? 649  LEU A CD2 1 
ATOM   513  N N   . SER A 1 65  ? 5.116   -8.192  16.994  1.00 14.10  ? 650  SER A N   1 
ATOM   514  C CA  . SER A 1 65  ? 4.917   -6.798  16.609  1.00 14.17  ? 650  SER A CA  1 
ATOM   515  C C   . SER A 1 65  ? 5.710   -6.559  15.332  1.00 13.32  ? 650  SER A C   1 
ATOM   516  O O   . SER A 1 65  ? 6.667   -7.242  15.079  1.00 14.09  ? 650  SER A O   1 
ATOM   517  C CB  . SER A 1 65  ? 5.354   -5.868  17.668  1.00 14.55  ? 650  SER A CB  1 
ATOM   518  O OG  . SER A 1 65  ? 6.775   -5.946  17.838  1.00 13.94  ? 650  SER A OG  1 
ATOM   519  N N   . GLY A 1 66  ? 5.251   -5.504  14.630  1.00 15.20  ? 651  GLY A N   1 
ATOM   520  C CA  . GLY A 1 66  ? 6.050   -4.905  13.562  1.00 15.81  ? 651  GLY A CA  1 
ATOM   521  C C   . GLY A 1 66  ? 6.076   -5.664  12.242  1.00 15.39  ? 651  GLY A C   1 
ATOM   522  O O   . GLY A 1 66  ? 5.376   -6.675  12.030  1.00 16.94  ? 651  GLY A O   1 
ATOM   523  N N   . ARG A 1 67  ? 7.066   -5.324  11.441  1.00 12.81  ? 652  ARG A N   1 
ATOM   524  C CA  . ARG A 1 67  ? 7.346   -5.888  10.155  1.00 12.43  ? 652  ARG A CA  1 
ATOM   525  C C   . ARG A 1 67  ? 8.716   -6.532  10.186  1.00 12.83  ? 652  ARG A C   1 
ATOM   526  O O   . ARG A 1 67  ? 9.648   -5.895  10.716  1.00 14.26  ? 652  ARG A O   1 
ATOM   527  C CB  . ARG A 1 67  ? 7.291   -4.780  9.091   1.00 13.55  ? 652  ARG A CB  1 
ATOM   528  C CG  . ARG A 1 67  ? 5.842   -4.431  8.779   1.00 15.17  ? 652  ARG A CG  1 
ATOM   529  C CD  . ARG A 1 67  ? 5.655   -3.195  7.899   1.00 17.54  ? 652  ARG A CD  1 
ATOM   530  N NE  . ARG A 1 67  ? 5.861   -1.956  8.629   1.00 18.60  ? 652  ARG A NE  1 
ATOM   531  C CZ  . ARG A 1 67  ? 6.085   -0.773  8.059   1.00 20.82  ? 652  ARG A CZ  1 
ATOM   532  N NH1 . ARG A 1 67  ? 6.140   -0.708  6.735   1.00 21.30  ? 652  ARG A NH1 1 
ATOM   533  N NH2 . ARG A 1 67  ? 6.305   0.278   8.783   1.00 23.18  ? 652  ARG A NH2 1 
ATOM   534  N N   . ARG A 1 68  ? 8.808   -7.768  9.708   1.00 11.74  ? 653  ARG A N   1 
ATOM   535  C CA  . ARG A 1 68  ? 10.014  -8.579  9.866   1.00 12.49  ? 653  ARG A CA  1 
ATOM   536  C C   . ARG A 1 68  ? 10.263  -9.305  8.553   1.00 12.62  ? 653  ARG A C   1 
ATOM   537  O O   . ARG A 1 68  ? 9.343   -9.969  8.051   1.00 13.31  ? 653  ARG A O   1 
ATOM   538  C CB  . ARG A 1 68  ? 9.867   -9.637  10.964  1.00 12.71  ? 653  ARG A CB  1 
ATOM   539  C CG  . ARG A 1 68  ? 9.291   -9.172  12.291  1.00 15.86  ? 653  ARG A CG  1 
ATOM   540  C CD  . ARG A 1 68  ? 10.182  -8.393  13.197  1.00 14.45  ? 653  ARG A CD  1 
ATOM   541  N NE  . ARG A 1 68  ? 9.496   -7.817  14.367  1.00 13.55  ? 653  ARG A NE  1 
ATOM   542  C CZ  . ARG A 1 68  ? 9.939   -7.612  15.602  1.00 13.87  ? 653  ARG A CZ  1 
ATOM   543  N NH1 . ARG A 1 68  ? 11.146  -8.024  15.942  1.00 15.22  ? 653  ARG A NH1 1 
ATOM   544  N NH2 . ARG A 1 68  ? 9.209   -6.977  16.430  1.00 14.34  ? 653  ARG A NH2 1 
ATOM   545  N N   . TYR A 1 69  ? 11.499  -9.254  8.078   1.00 11.33  ? 654  TYR A N   1 
ATOM   546  C CA  . TYR A 1 69  ? 11.871  -9.896  6.827   1.00 11.25  ? 654  TYR A CA  1 
ATOM   547  C C   . TYR A 1 69  ? 13.113  -10.749 7.063   1.00 11.03  ? 654  TYR A C   1 
ATOM   548  O O   . TYR A 1 69  ? 14.064  -10.290 7.699   1.00 11.22  ? 654  TYR A O   1 
ATOM   549  C CB  . TYR A 1 69  ? 12.149  -8.873  5.746   1.00 12.06  ? 654  TYR A CB  1 
ATOM   550  C CG  . TYR A 1 69  ? 12.615  -9.490  4.444   1.00 12.38  ? 654  TYR A CG  1 
ATOM   551  C CD1 . TYR A 1 69  ? 11.682  -9.977  3.531   1.00 12.98  ? 654  TYR A CD1 1 
ATOM   552  C CD2 . TYR A 1 69  ? 13.953  -9.591  4.151   1.00 13.31  ? 654  TYR A CD2 1 
ATOM   553  C CE1 . TYR A 1 69  ? 12.112  -10.496 2.338   1.00 14.30  ? 654  TYR A CE1 1 
ATOM   554  C CE2 . TYR A 1 69  ? 14.394  -10.207 2.991   1.00 14.51  ? 654  TYR A CE2 1 
ATOM   555  C CZ  . TYR A 1 69  ? 13.453  -10.638 2.086   1.00 14.40  ? 654  TYR A CZ  1 
ATOM   556  O OH  . TYR A 1 69  ? 13.863  -11.186 0.883   1.00 16.15  ? 654  TYR A OH  1 
ATOM   557  N N   . TRP A 1 70  ? 13.153  -11.931 6.455   1.00 10.48  ? 655  TRP A N   1 
ATOM   558  C CA  . TRP A 1 70  ? 14.388  -12.678 6.411   1.00 10.43  ? 655  TRP A CA  1 
ATOM   559  C C   . TRP A 1 70  ? 14.463  -13.443 5.096   1.00 11.30  ? 655  TRP A C   1 
ATOM   560  O O   . TRP A 1 70  ? 13.443  -13.662 4.433   1.00 11.79  ? 655  TRP A O   1 
ATOM   561  C CB  . TRP A 1 70  ? 14.589  -13.525 7.687   1.00 10.57  ? 655  TRP A CB  1 
ATOM   562  C CG  . TRP A 1 70  ? 13.604  -14.626 7.887   1.00 10.79  ? 655  TRP A CG  1 
ATOM   563  C CD1 . TRP A 1 70  ? 13.710  -15.949 7.544   1.00 11.21  ? 655  TRP A CD1 1 
ATOM   564  C CD2 . TRP A 1 70  ? 12.303  -14.489 8.488   1.00 10.19  ? 655  TRP A CD2 1 
ATOM   565  N NE1 . TRP A 1 70  ? 12.555  -16.603 7.921   1.00 11.58  ? 655  TRP A NE1 1 
ATOM   566  C CE2 . TRP A 1 70  ? 11.688  -15.744 8.499   1.00 10.31  ? 655  TRP A CE2 1 
ATOM   567  C CE3 . TRP A 1 70  ? 11.596  -13.406 9.042   1.00 12.07  ? 655  TRP A CE3 1 
ATOM   568  C CZ2 . TRP A 1 70  ? 10.416  -15.958 9.008   1.00 11.77  ? 655  TRP A CZ2 1 
ATOM   569  C CZ3 . TRP A 1 70  ? 10.367  -13.631 9.610   1.00 12.99  ? 655  TRP A CZ3 1 
ATOM   570  C CH2 . TRP A 1 70  ? 9.758   -14.885 9.556   1.00 12.79  ? 655  TRP A CH2 1 
ATOM   571  N N   . GLU A 1 71  ? 15.654  -13.969 4.792   1.00 12.07  ? 656  GLU A N   1 
ATOM   572  C CA  . GLU A 1 71  ? 15.920  -14.626 3.532   1.00 12.32  ? 656  GLU A CA  1 
ATOM   573  C C   . GLU A 1 71  ? 16.687  -15.914 3.815   1.00 12.88  ? 656  GLU A C   1 
ATOM   574  O O   . GLU A 1 71  ? 17.585  -15.928 4.662   1.00 13.60  ? 656  GLU A O   1 
ATOM   575  C CB  . GLU A 1 71  ? 16.812  -13.791 2.606   1.00 18.34  ? 656  GLU A CB  1 
ATOM   576  C CG  . GLU A 1 71  ? 16.139  -12.594 2.008   1.00 22.03  ? 656  GLU A CG  1 
ATOM   577  C CD  . GLU A 1 71  ? 17.008  -11.909 0.923   1.00 16.51  ? 656  GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 71  ? 18.165  -12.139 0.540   1.00 24.33  ? 656  GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 71  ? 16.327  -11.073 0.515   1.00 20.87  ? 656  GLU A OE2 1 
ATOM   580  N N   . VAL A 1 72  ? 16.381  -16.934 3.022   1.00 11.92  ? 657  VAL A N   1 
ATOM   581  C CA  . VAL A 1 72  ? 16.971  -18.253 3.195   1.00 12.25  ? 657  VAL A CA  1 
ATOM   582  C C   . VAL A 1 72  ? 17.427  -18.765 1.847   1.00 13.24  ? 657  VAL A C   1 
ATOM   583  O O   . VAL A 1 72  ? 16.629  -18.793 0.912   1.00 13.44  ? 657  VAL A O   1 
ATOM   584  C CB  . VAL A 1 72  ? 15.996  -19.251 3.850   1.00 12.68  ? 657  VAL A CB  1 
ATOM   585  C CG1 . VAL A 1 72  ? 16.685  -20.570 4.153   1.00 14.03  ? 657  VAL A CG1 1 
ATOM   586  C CG2 . VAL A 1 72  ? 15.366  -18.656 5.095   1.00 13.85  ? 657  VAL A CG2 1 
ATOM   587  N N   . GLU A 1 73  ? 18.673  -19.237 1.761   1.00 14.08  ? 658  GLU A N   1 
ATOM   588  C CA  . GLU A 1 73  ? 19.141  -19.886 0.552   1.00 15.72  ? 658  GLU A CA  1 
ATOM   589  C C   . GLU A 1 73  ? 18.618  -21.310 0.563   1.00 15.38  ? 658  GLU A C   1 
ATOM   590  O O   . GLU A 1 73  ? 18.776  -22.045 1.549   1.00 14.39  ? 658  GLU A O   1 
ATOM   591  C CB  . GLU A 1 73  ? 20.656  -19.932 0.520   1.00 18.39  ? 658  GLU A CB  1 
ATOM   592  C CG  . GLU A 1 73  ? 21.283  -18.553 0.412   1.00 25.32  ? 658  GLU A CG  1 
ATOM   593  C CD  . GLU A 1 73  ? 22.726  -18.530 -0.062  1.00 40.65  ? 658  GLU A CD  1 
ATOM   594  O OE1 . GLU A 1 73  ? 23.360  -19.626 -0.018  1.00 40.00  ? 658  GLU A OE1 1 
ATOM   595  O OE2 . GLU A 1 73  ? 23.176  -17.438 -0.513  1.00 46.56  ? 658  GLU A OE2 1 
ATOM   596  N N   . VAL A 1 74  ? 17.931  -21.695 -0.527  1.00 14.41  ? 659  VAL A N   1 
ATOM   597  C CA  . VAL A 1 74  ? 17.458  -23.051 -0.739  1.00 13.33  ? 659  VAL A CA  1 
ATOM   598  C C   . VAL A 1 74  ? 18.252  -23.756 -1.843  1.00 14.42  ? 659  VAL A C   1 
ATOM   599  O O   . VAL A 1 74  ? 18.196  -24.976 -1.979  1.00 14.76  ? 659  VAL A O   1 
ATOM   600  C CB  . VAL A 1 74  ? 15.945  -23.104 -1.051  1.00 13.86  ? 659  VAL A CB  1 
ATOM   601  C CG1 . VAL A 1 74  ? 15.162  -22.600 0.137   1.00 13.67  ? 659  VAL A CG1 1 
ATOM   602  C CG2 . VAL A 1 74  ? 15.586  -22.390 -2.341  1.00 14.30  ? 659  VAL A CG2 1 
ATOM   603  N N   . GLY A 1 75  ? 18.915  -22.966 -2.694  1.00 15.38  ? 660  GLY A N   1 
ATOM   604  C CA  . GLY A 1 75  ? 19.747  -23.518 -3.738  1.00 16.52  ? 660  GLY A CA  1 
ATOM   605  C C   . GLY A 1 75  ? 19.035  -24.530 -4.615  1.00 16.92  ? 660  GLY A C   1 
ATOM   606  O O   . GLY A 1 75  ? 17.883  -24.344 -5.024  1.00 16.40  ? 660  GLY A O   1 
ATOM   607  N N   . ASP A 1 76  ? 19.713  -25.644 -4.890  1.00 17.57  ? 661  ASP A N   1 
ATOM   608  C CA  . ASP A 1 76  ? 19.268  -26.666 -5.818  1.00 19.14  ? 661  ASP A CA  1 
ATOM   609  C C   . ASP A 1 76  ? 18.645  -27.831 -5.061  1.00 18.15  ? 661  ASP A C   1 
ATOM   610  O O   . ASP A 1 76  ? 18.487  -28.925 -5.591  1.00 20.62  ? 661  ASP A O   1 
ATOM   611  C CB  . ASP A 1 76  ? 20.432  -27.124 -6.710  1.00 20.91  ? 661  ASP A CB  1 
ATOM   612  C CG  . ASP A 1 76  ? 21.087  -26.016 -7.549  1.00 23.75  ? 661  ASP A CG  1 
ATOM   613  O OD1 . ASP A 1 76  ? 20.428  -24.991 -7.764  1.00 25.40  ? 661  ASP A OD1 1 
ATOM   614  O OD2 . ASP A 1 76  ? 22.303  -26.118 -7.871  1.00 24.60  ? 661  ASP A OD2 1 
ATOM   615  N N   . LYS A 1 77  ? 18.206  -27.540 -3.813  1.00 17.80  ? 662  LYS A N   1 
ATOM   616  C CA  . LYS A 1 77  ? 17.575  -28.583 -3.026  1.00 17.18  ? 662  LYS A CA  1 
ATOM   617  C C   . LYS A 1 77  ? 16.288  -29.033 -3.706  1.00 18.44  ? 662  LYS A C   1 
ATOM   618  O O   . LYS A 1 77  ? 15.720  -28.257 -4.455  1.00 19.88  ? 662  LYS A O   1 
ATOM   619  C CB  . LYS A 1 77  ? 17.247  -28.066 -1.633  1.00 16.32  ? 662  LYS A CB  1 
ATOM   620  C CG  . LYS A 1 77  ? 18.502  -27.901 -0.785  1.00 16.34  ? 662  LYS A CG  1 
ATOM   621  C CD  . LYS A 1 77  ? 18.249  -27.347 0.597   1.00 16.08  ? 662  LYS A CD  1 
ATOM   622  C CE  . LYS A 1 77  ? 17.397  -28.209 1.474   1.00 16.10  ? 662  LYS A CE  1 
ATOM   623  N NZ  . LYS A 1 77  ? 17.838  -29.570 1.651   1.00 16.49  ? 662  LYS A NZ  1 
ATOM   624  N N   . THR A 1 78  ? 15.847  -30.231 -3.387  1.00 18.58  ? 663  THR A N   1 
ATOM   625  C CA  . THR A 1 78  ? 14.660  -30.828 -3.970  1.00 20.22  ? 663  THR A CA  1 
ATOM   626  C C   . THR A 1 78  ? 13.472  -30.822 -2.999  1.00 19.69  ? 663  THR A C   1 
ATOM   627  O O   . THR A 1 78  ? 12.372  -31.161 -3.443  1.00 20.19  ? 663  THR A O   1 
ATOM   628  C CB  . THR A 1 78  ? 14.924  -32.249 -4.429  1.00 22.06  ? 663  THR A CB  1 
ATOM   629  O OG1 . THR A 1 78  ? 15.236  -33.067 -3.302  1.00 22.41  ? 663  THR A OG1 1 
ATOM   630  C CG2 . THR A 1 78  ? 16.012  -32.378 -5.475  1.00 23.29  ? 663  THR A CG2 1 
ATOM   631  N N   . ALA A 1 79  ? 13.688  -30.529 -1.712  1.00 17.79  ? 664  ALA A N   1 
ATOM   632  C CA  . ALA A 1 79  ? 12.577  -30.466 -0.785  1.00 17.87  ? 664  ALA A CA  1 
ATOM   633  C C   . ALA A 1 79  ? 12.959  -29.595 0.399   1.00 17.52  ? 664  ALA A C   1 
ATOM   634  O O   . ALA A 1 79  ? 14.113  -29.619 0.851   1.00 17.70  ? 664  ALA A O   1 
ATOM   635  C CB  . ALA A 1 79  ? 12.172  -31.805 -0.315  1.00 18.69  ? 664  ALA A CB  1 
ATOM   636  N N   . TRP A 1 80  ? 11.996  -28.805 0.854   1.00 15.74  ? 665  TRP A N   1 
ATOM   637  C CA  . TRP A 1 80  ? 12.194  -27.941 2.016   1.00 14.56  ? 665  TRP A CA  1 
ATOM   638  C C   . TRP A 1 80  ? 10.872  -27.320 2.435   1.00 14.56  ? 665  TRP A C   1 
ATOM   639  O O   . TRP A 1 80  ? 9.897   -27.391 1.704   1.00 14.77  ? 665  TRP A O   1 
ATOM   640  C CB  . TRP A 1 80  ? 13.232  -26.850 1.765   1.00 13.70  ? 665  TRP A CB  1 
ATOM   641  C CG  . TRP A 1 80  ? 13.083  -26.151 0.455   1.00 14.71  ? 665  TRP A CG  1 
ATOM   642  C CD1 . TRP A 1 80  ? 13.835  -26.399 -0.654  1.00 16.58  ? 665  TRP A CD1 1 
ATOM   643  C CD2 . TRP A 1 80  ? 12.193  -25.068 0.110   1.00 14.06  ? 665  TRP A CD2 1 
ATOM   644  N NE1 . TRP A 1 80  ? 13.478  -25.513 -1.643  1.00 15.93  ? 665  TRP A NE1 1 
ATOM   645  C CE2 . TRP A 1 80  ? 12.431  -24.742 -1.244  1.00 15.33  ? 665  TRP A CE2 1 
ATOM   646  C CE3 . TRP A 1 80  ? 11.148  -24.408 0.786   1.00 14.46  ? 665  TRP A CE3 1 
ATOM   647  C CZ2 . TRP A 1 80  ? 11.728  -23.723 -1.870  1.00 14.84  ? 665  TRP A CZ2 1 
ATOM   648  C CZ3 . TRP A 1 80  ? 10.457  -23.410 0.133   1.00 14.81  ? 665  TRP A CZ3 1 
ATOM   649  C CH2 . TRP A 1 80  ? 10.743  -23.087 -1.182  1.00 15.17  ? 665  TRP A CH2 1 
ATOM   650  N N   . ILE A 1 81  ? 10.834  -26.827 3.668   1.00 13.59  ? 666  ILE A N   1 
ATOM   651  C CA  . ILE A 1 81  ? 9.734   -26.002 4.163   1.00 13.80  ? 666  ILE A CA  1 
ATOM   652  C C   . ILE A 1 81  ? 10.284  -24.702 4.741   1.00 12.81  ? 666  ILE A C   1 
ATOM   653  O O   . ILE A 1 81  ? 11.269  -24.743 5.475   1.00 13.31  ? 666  ILE A O   1 
ATOM   654  C CB  . ILE A 1 81  ? 8.974   -26.746 5.249   1.00 15.68  ? 666  ILE A CB  1 
ATOM   655  C CG1 . ILE A 1 81  ? 8.497   -28.125 4.765   1.00 17.79  ? 666  ILE A CG1 1 
ATOM   656  C CG2 . ILE A 1 81  ? 7.838   -25.874 5.760   1.00 17.07  ? 666  ILE A CG2 1 
ATOM   657  C CD1 . ILE A 1 81  ? 7.897   -28.991 5.847   1.00 19.23  ? 666  ILE A CD1 1 
ATOM   658  N N   . LEU A 1 82  ? 9.639   -23.579 4.490   1.00 11.80  ? 667  LEU A N   1 
ATOM   659  C CA  . LEU A 1 82  ? 10.011  -22.301 5.055   1.00 11.92  ? 667  LEU A CA  1 
ATOM   660  C C   . LEU A 1 82  ? 8.779   -21.500 5.419   1.00 12.55  ? 667  LEU A C   1 
ATOM   661  O O   . LEU A 1 82  ? 7.837   -21.450 4.672   1.00 12.81  ? 667  LEU A O   1 
ATOM   662  C CB  . LEU A 1 82  ? 10.808  -21.455 4.077   1.00 12.21  ? 667  LEU A CB  1 
ATOM   663  C CG  . LEU A 1 82  ? 12.190  -21.959 3.691   1.00 13.51  ? 667  LEU A CG  1 
ATOM   664  C CD1 . LEU A 1 82  ? 12.796  -21.119 2.584   1.00 13.57  ? 667  LEU A CD1 1 
ATOM   665  C CD2 . LEU A 1 82  ? 13.087  -21.939 4.919   1.00 13.72  ? 667  LEU A CD2 1 
ATOM   666  N N   . GLY A 1 83  ? 8.838   -20.791 6.554   1.00 11.89  ? 668  GLY A N   1 
ATOM   667  C CA  . GLY A 1 83  ? 7.834   -19.772 6.814   1.00 11.30  ? 668  GLY A CA  1 
ATOM   668  C C   . GLY A 1 83  ? 7.888   -19.387 8.285   1.00 10.92  ? 668  GLY A C   1 
ATOM   669  O O   . GLY A 1 83  ? 8.963   -19.190 8.845   1.00 11.37  ? 668  GLY A O   1 
ATOM   670  N N   . ALA A 1 84  ? 6.714   -19.260 8.865   1.00 11.44  ? 669  ALA A N   1 
ATOM   671  C CA  . ALA A 1 84  ? 6.606   -18.875 10.278  1.00 11.91  ? 669  ALA A CA  1 
ATOM   672  C C   . ALA A 1 84  ? 5.516   -19.655 10.942  1.00 13.23  ? 669  ALA A C   1 
ATOM   673  O O   . ALA A 1 84  ? 4.613   -20.189 10.286  1.00 13.14  ? 669  ALA A O   1 
ATOM   674  C CB  . ALA A 1 84  ? 6.349   -17.372 10.415  1.00 11.66  ? 669  ALA A CB  1 
ATOM   675  N N   . CYS A 1 85  ? 5.547   -19.677 12.274  1.00 12.86  ? 670  CYS A N   1 
ATOM   676  C CA  . CYS A 1 85  ? 4.550   -20.348 13.023  1.00 15.30  ? 670  CYS A CA  1 
ATOM   677  C C   . CYS A 1 85  ? 4.342   -19.687 14.372  1.00 15.51  ? 670  CYS A C   1 
ATOM   678  O O   . CYS A 1 85  ? 5.192   -18.930 14.827  1.00 14.62  ? 670  CYS A O   1 
ATOM   679  C CB  . CYS A 1 85  ? 4.949   -21.801 13.184  1.00 15.99  ? 670  CYS A CB  1 
ATOM   680  S SG  . CYS A 1 85  ? 6.413   -22.075 14.216  1.00 18.88  ? 670  CYS A SG  1 
ATOM   681  N N   A LYS A 1 86  ? 3.217   -20.013 15.013  0.50 15.88  ? 671  LYS A N   1 
ATOM   682  N N   B LYS A 1 86  ? 3.197   -19.962 14.986  0.50 15.94  ? 671  LYS A N   1 
ATOM   683  C CA  A LYS A 1 86  ? 2.964   -19.593 16.387  0.50 17.50  ? 671  LYS A CA  1 
ATOM   684  C CA  B LYS A 1 86  ? 3.000   -19.576 16.372  0.50 17.73  ? 671  LYS A CA  1 
ATOM   685  C C   A LYS A 1 86  ? 3.957   -20.316 17.297  0.50 18.98  ? 671  LYS A C   1 
ATOM   686  C C   B LYS A 1 86  ? 4.094   -20.245 17.189  0.50 18.66  ? 671  LYS A C   1 
ATOM   687  O O   A LYS A 1 86  ? 4.158   -21.534 17.204  0.50 19.00  ? 671  LYS A O   1 
ATOM   688  O O   B LYS A 1 86  ? 4.499   -21.367 16.894  0.50 18.63  ? 671  LYS A O   1 
ATOM   689  C CB  A LYS A 1 86  ? 1.484   -19.847 16.740  0.50 20.01  ? 671  LYS A CB  1 
ATOM   690  C CB  B LYS A 1 86  ? 1.615   -20.028 16.849  0.50 20.89  ? 671  LYS A CB  1 
ATOM   691  C CG  A LYS A 1 86  ? 0.492   -18.995 15.930  0.50 21.01  ? 671  LYS A CG  1 
ATOM   692  C CG  B LYS A 1 86  ? 0.475   -19.222 16.276  0.50 22.54  ? 671  LYS A CG  1 
ATOM   693  C CD  A LYS A 1 86  ? -1.018  -19.174 16.119  0.50 23.90  ? 671  LYS A CD  1 
ATOM   694  C CD  B LYS A 1 86  ? -0.843  -19.492 16.982  0.50 26.90  ? 671  LYS A CD  1 
ATOM   695  C CE  A LYS A 1 86  ? -1.533  -18.232 17.194  0.50 27.28  ? 671  LYS A CE  1 
ATOM   696  C CE  B LYS A 1 86  ? -1.537  -20.729 16.559  0.50 29.35  ? 671  LYS A CE  1 
ATOM   697  N NZ  A LYS A 1 86  ? -2.978  -17.915 17.200  0.50 26.73  ? 671  LYS A NZ  1 
ATOM   698  N NZ  B LYS A 1 86  ? -2.680  -20.970 17.465  0.50 31.66  ? 671  LYS A NZ  1 
ATOM   699  N N   . THR A 1 87  ? 4.524   -19.591 18.271  1.00 19.41  ? 672  THR A N   1 
ATOM   700  C CA  . THR A 1 87  ? 5.486   -20.236 19.171  1.00 22.01  ? 672  THR A CA  1 
ATOM   701  C C   . THR A 1 87  ? 4.876   -21.371 19.987  1.00 27.58  ? 672  THR A C   1 
ATOM   702  O O   . THR A 1 87  ? 5.595   -22.249 20.472  1.00 30.76  ? 672  THR A O   1 
ATOM   703  C CB  . THR A 1 87  ? 6.099   -19.186 20.077  1.00 23.54  ? 672  THR A CB  1 
ATOM   704  O OG1 . THR A 1 87  ? 4.965   -18.625 20.750  1.00 25.85  ? 672  THR A OG1 1 
ATOM   705  C CG2 . THR A 1 87  ? 6.822   -18.114 19.325  1.00 22.23  ? 672  THR A CG2 1 
ATOM   706  N N   . SER A 1 88  ? 3.554   -21.457 20.074  1.00 29.47  ? 673  SER A N   1 
ATOM   707  C CA  . SER A 1 88  ? 2.894   -22.563 20.765  1.00 35.32  ? 673  SER A CA  1 
ATOM   708  C C   . SER A 1 88  ? 2.657   -23.844 19.948  1.00 37.43  ? 673  SER A C   1 
ATOM   709  O O   . SER A 1 88  ? 1.939   -24.724 20.406  1.00 40.62  ? 673  SER A O   1 
ATOM   710  C CB  . SER A 1 88  ? 1.550   -22.102 21.290  1.00 36.63  ? 673  SER A CB  1 
ATOM   711  O OG  . SER A 1 88  ? 0.890   -21.474 20.189  1.00 38.67  ? 673  SER A OG  1 
ATOM   712  N N   . ILE A 1 89  ? 3.190   -23.999 18.748  1.00 38.97  ? 674  ILE A N   1 
ATOM   713  C CA  . ILE A 1 89  ? 2.940   -25.225 18.012  1.00 42.62  ? 674  ILE A CA  1 
ATOM   714  C C   . ILE A 1 89  ? 3.378   -26.468 18.798  1.00 44.46  ? 674  ILE A C   1 
ATOM   715  O O   . ILE A 1 89  ? 4.389   -26.480 19.494  1.00 44.85  ? 674  ILE A O   1 
ATOM   716  C CB  . ILE A 1 89  ? 3.623   -25.077 16.649  1.00 49.58  ? 674  ILE A CB  1 
ATOM   717  C CG1 . ILE A 1 89  ? 2.669   -24.349 15.727  1.00 48.36  ? 674  ILE A CG1 1 
ATOM   718  C CG2 . ILE A 1 89  ? 4.095   -26.422 16.102  1.00 56.41  ? 674  ILE A CG2 1 
ATOM   719  C CD1 . ILE A 1 89  ? 3.358   -23.614 14.615  1.00 55.46  ? 674  ILE A CD1 1 
ATOM   720  N N   . SER A 1 90  ? 2.598   -27.554 18.710  1.00 51.01  ? 675  SER A N   1 
ATOM   721  C CA  . SER A 1 90  ? 3.032   -28.814 19.307  1.00 52.87  ? 675  SER A CA  1 
ATOM   722  C C   . SER A 1 90  ? 4.184   -29.379 18.480  1.00 51.56  ? 675  SER A C   1 
ATOM   723  O O   . SER A 1 90  ? 4.173   -29.272 17.259  1.00 47.73  ? 675  SER A O   1 
ATOM   724  C CB  . SER A 1 90  ? 1.922   -29.819 19.404  1.00 56.24  ? 675  SER A CB  1 
ATOM   725  O OG  . SER A 1 90  ? 2.374   -30.952 20.132  1.00 59.07  ? 675  SER A OG  1 
ATOM   726  N N   . ARG A 1 91  ? 5.165   -29.975 19.163  1.00 56.66  ? 676  ARG A N   1 
ATOM   727  C CA  . ARG A 1 91  ? 6.356   -30.517 18.527  1.00 63.08  ? 676  ARG A CA  1 
ATOM   728  C C   . ARG A 1 91  ? 6.309   -32.047 18.454  1.00 65.45  ? 676  ARG A C   1 
ATOM   729  O O   . ARG A 1 91  ? 7.056   -32.648 17.680  1.00 59.27  ? 676  ARG A O   1 
ATOM   730  C CB  . ARG A 1 91  ? 7.589   -30.054 19.310  1.00 67.28  ? 676  ARG A CB  1 
ATOM   731  C CG  . ARG A 1 91  ? 7.586   -28.557 19.578  1.00 64.49  ? 676  ARG A CG  1 
ATOM   732  C CD  . ARG A 1 91  ? 8.944   -28.120 20.065  1.00 61.60  ? 676  ARG A CD  1 
ATOM   733  N NE  . ARG A 1 91  ? 9.022   -26.663 20.189  1.00 54.86  ? 676  ARG A NE  1 
ATOM   734  C CZ  . ARG A 1 91  ? 9.698   -26.037 21.135  1.00 55.78  ? 676  ARG A CZ  1 
ATOM   735  N NH1 . ARG A 1 91  ? 10.512  -26.711 21.932  1.00 57.91  ? 676  ARG A NH1 1 
ATOM   736  N NH2 . ARG A 1 91  ? 9.581   -24.727 21.259  1.00 51.21  ? 676  ARG A NH2 1 
ATOM   737  N N   . LYS A 1 92  ? 5.455   -32.671 19.271  1.00 71.22  ? 677  LYS A N   1 
ATOM   738  C CA  . LYS A 1 92  ? 5.281   -34.116 19.244  1.00 80.24  ? 677  LYS A CA  1 
ATOM   739  C C   . LYS A 1 92  ? 4.063   -34.444 18.378  1.00 88.53  ? 677  LYS A C   1 
ATOM   740  O O   . LYS A 1 92  ? 2.935   -34.424 18.862  1.00 97.51  ? 677  LYS A O   1 
ATOM   741  C CB  . LYS A 1 92  ? 5.209   -34.649 20.683  1.00 80.78  ? 677  LYS A CB  1 
ATOM   742  C CG  . LYS A 1 92  ? 6.553   -34.843 21.409  1.00 82.71  ? 677  LYS A CG  1 
ATOM   743  C CD  . LYS A 1 92  ? 7.416   -33.593 21.569  1.00 82.02  ? 677  LYS A CD  1 
ATOM   744  C CE  . LYS A 1 92  ? 8.631   -33.760 22.442  1.00 83.19  ? 677  LYS A CE  1 
ATOM   745  N NZ  . LYS A 1 92  ? 9.644   -34.686 21.923  1.00 82.84  ? 677  LYS A NZ  1 
ATOM   746  N N   . GLY A 1 93  ? 4.298   -34.729 17.088  1.00 97.42  ? 678  GLY A N   1 
ATOM   747  C CA  . GLY A 1 93  ? 3.227   -34.890 16.113  1.00 104.52 ? 678  GLY A CA  1 
ATOM   748  C C   . GLY A 1 93  ? 2.357   -33.632 15.999  1.00 108.04 ? 678  GLY A C   1 
ATOM   749  O O   . GLY A 1 93  ? 2.880   -32.532 15.831  1.00 102.88 ? 678  GLY A O   1 
ATOM   750  N N   . ASN A 1 94  ? 1.026   -33.821 16.076  1.00 107.55 ? 679  ASN A N   1 
ATOM   751  C CA  . ASN A 1 94  ? 0.038   -32.755 16.238  1.00 102.42 ? 679  ASN A CA  1 
ATOM   752  C C   . ASN A 1 94  ? 0.162   -31.630 15.205  1.00 88.00  ? 679  ASN A C   1 
ATOM   753  O O   . ASN A 1 94  ? -0.092  -30.468 15.525  1.00 72.49  ? 679  ASN A O   1 
ATOM   754  C CB  . ASN A 1 94  ? 0.123   -32.135 17.632  1.00 104.68 ? 679  ASN A CB  1 
ATOM   755  C CG  . ASN A 1 94  ? -1.020  -32.525 18.536  1.00 110.61 ? 679  ASN A CG  1 
ATOM   756  O OD1 . ASN A 1 94  ? -1.955  -33.213 18.111  1.00 123.07 ? 679  ASN A OD1 1 
ATOM   757  N ND2 . ASN A 1 94  ? -0.978  -32.063 19.778  1.00 109.69 ? 679  ASN A ND2 1 
ATOM   758  N N   . MET A 1 95  ? 0.504   -31.951 13.954  1.00 83.71  ? 680  MET A N   1 
ATOM   759  C CA  . MET A 1 95  ? 0.845   -30.882 13.033  1.00 78.02  ? 680  MET A CA  1 
ATOM   760  C C   . MET A 1 95  ? 0.598   -31.264 11.577  1.00 65.73  ? 680  MET A C   1 
ATOM   761  O O   . MET A 1 95  ? 1.496   -31.704 10.859  1.00 61.83  ? 680  MET A O   1 
ATOM   762  C CB  . MET A 1 95  ? 2.291   -30.417 13.254  1.00 85.16  ? 680  MET A CB  1 
ATOM   763  C CG  . MET A 1 95  ? 3.371   -31.440 12.942  1.00 90.37  ? 680  MET A CG  1 
ATOM   764  S SD  . MET A 1 95  ? 5.011   -30.776 13.299  1.00 97.98  ? 680  MET A SD  1 
ATOM   765  C CE  . MET A 1 95  ? 5.138   -31.098 15.062  1.00 96.86  ? 680  MET A CE  1 
ATOM   766  N N   . THR A 1 96  ? -0.637  -31.021 11.141  1.00 55.67  ? 681  THR A N   1 
ATOM   767  C CA  . THR A 1 96  ? -0.860  -30.580 9.776   1.00 51.32  ? 681  THR A CA  1 
ATOM   768  C C   . THR A 1 96  ? -0.362  -29.140 9.738   1.00 40.70  ? 681  THR A C   1 
ATOM   769  O O   . THR A 1 96  ? -0.717  -28.357 10.618  1.00 38.47  ? 681  THR A O   1 
ATOM   770  C CB  . THR A 1 96  ? -2.335  -30.684 9.406   1.00 53.96  ? 681  THR A CB  1 
ATOM   771  O OG1 . THR A 1 96  ? -2.512  -32.082 9.190   1.00 62.27  ? 681  THR A OG1 1 
ATOM   772  C CG2 . THR A 1 96  ? -2.700  -29.943 8.133   1.00 54.01  ? 681  THR A CG2 1 
ATOM   773  N N   . LEU A 1 97  ? 0.536   -28.819 8.808   1.00 34.93  ? 682  LEU A N   1 
ATOM   774  C CA  . LEU A 1 97  ? 0.988   -27.446 8.694   1.00 32.61  ? 682  LEU A CA  1 
ATOM   775  C C   . LEU A 1 97  ? -0.110  -26.676 7.966   1.00 33.47  ? 682  LEU A C   1 
ATOM   776  O O   . LEU A 1 97  ? -0.430  -26.938 6.790   1.00 35.97  ? 682  LEU A O   1 
ATOM   777  C CB  . LEU A 1 97  ? 2.349   -27.362 8.009   1.00 33.59  ? 682  LEU A CB  1 
ATOM   778  C CG  . LEU A 1 97  ? 3.420   -28.310 8.562   1.00 35.16  ? 682  LEU A CG  1 
ATOM   779  C CD1 . LEU A 1 97  ? 4.739   -28.003 7.899   1.00 40.86  ? 682  LEU A CD1 1 
ATOM   780  C CD2 . LEU A 1 97  ? 3.581   -28.228 10.066  1.00 38.91  ? 682  LEU A CD2 1 
ATOM   781  N N   . SER A 1 98  ? -0.862  -25.926 8.769   1.00 26.91  ? 683  SER A N   1 
ATOM   782  C CA  . SER A 1 98  ? -1.972  -25.134 8.290   1.00 24.53  ? 683  SER A CA  1 
ATOM   783  C C   . SER A 1 98  ? -2.078  -23.858 9.097   1.00 21.59  ? 683  SER A C   1 
ATOM   784  O O   . SER A 1 98  ? -1.697  -23.857 10.281  1.00 19.64  ? 683  SER A O   1 
ATOM   785  C CB  . SER A 1 98  ? -3.261  -25.854 8.413   1.00 26.35  ? 683  SER A CB  1 
ATOM   786  O OG  . SER A 1 98  ? -3.669  -26.014 9.763   1.00 27.98  ? 683  SER A OG  1 
ATOM   787  N N   . PRO A 1 99  ? -2.574  -22.762 8.490   1.00 20.76  ? 684  PRO A N   1 
ATOM   788  C CA  . PRO A 1 99  ? -2.907  -21.542 9.216   1.00 21.42  ? 684  PRO A CA  1 
ATOM   789  C C   . PRO A 1 99  ? -3.750  -21.769 10.463  1.00 23.27  ? 684  PRO A C   1 
ATOM   790  O O   . PRO A 1 99  ? -3.435  -21.230 11.548  1.00 23.87  ? 684  PRO A O   1 
ATOM   791  C CB  . PRO A 1 99  ? -3.540  -20.639 8.175   1.00 20.75  ? 684  PRO A CB  1 
ATOM   792  C CG  . PRO A 1 99  ? -2.866  -21.109 6.897   1.00 20.39  ? 684  PRO A CG  1 
ATOM   793  C CD  . PRO A 1 99  ? -2.739  -22.577 7.031   1.00 20.87  ? 684  PRO A CD  1 
ATOM   794  N N   . GLU A 1 100 ? -4.773  -22.616 10.371  1.00 23.65  ? 685  GLU A N   1 
ATOM   795  C CA  . GLU A 1 100 ? -5.578  -22.920 11.533  1.00 25.86  ? 685  GLU A CA  1 
ATOM   796  C C   . GLU A 1 100 ? -4.780  -23.524 12.687  1.00 26.17  ? 685  GLU A C   1 
ATOM   797  O O   . GLU A 1 100 ? -5.127  -23.275 13.861  1.00 27.35  ? 685  GLU A O   1 
ATOM   798  C CB  . GLU A 1 100 ? -6.723  -23.861 11.131  1.00 29.90  ? 685  GLU A CB  1 
ATOM   799  C CG  . GLU A 1 100 ? -7.754  -24.093 12.223  1.00 35.46  ? 685  GLU A CG  1 
ATOM   800  C CD  . GLU A 1 100 ? -8.940  -24.861 11.640  1.00 40.87  ? 685  GLU A CD  1 
ATOM   801  O OE1 . GLU A 1 100 ? -9.143  -26.005 12.124  1.00 44.49  ? 685  GLU A OE1 1 
ATOM   802  O OE2 . GLU A 1 100 ? -9.649  -24.320 10.731  1.00 41.05  ? 685  GLU A OE2 1 
ATOM   803  N N   A ASN A 1 101 ? -3.781  -24.357 12.361  0.50 25.01  ? 686  ASN A N   1 
ATOM   804  N N   B ASN A 1 101 ? -3.772  -24.335 12.379  0.50 25.86  ? 686  ASN A N   1 
ATOM   805  C CA  A ASN A 1 101 ? -2.867  -24.968 13.323  0.50 25.16  ? 686  ASN A CA  1 
ATOM   806  C CA  B ASN A 1 101 ? -2.934  -24.923 13.409  0.50 26.93  ? 686  ASN A CA  1 
ATOM   807  C C   A ASN A 1 101 ? -1.643  -24.096 13.625  0.50 23.44  ? 686  ASN A C   1 
ATOM   808  C C   B ASN A 1 101 ? -1.784  -24.002 13.814  0.50 24.85  ? 686  ASN A C   1 
ATOM   809  O O   A ASN A 1 101 ? -0.707  -24.595 14.242  0.50 23.15  ? 686  ASN A O   1 
ATOM   810  O O   B ASN A 1 101 ? -1.046  -24.369 14.715  0.50 25.84  ? 686  ASN A O   1 
ATOM   811  C CB  A ASN A 1 101 ? -2.337  -26.319 12.855  0.50 25.55  ? 686  ASN A CB  1 
ATOM   812  C CB  B ASN A 1 101 ? -2.345  -26.256 12.983  0.50 27.93  ? 686  ASN A CB  1 
ATOM   813  C CG  A ASN A 1 101 ? -3.415  -27.382 12.801  0.50 28.33  ? 686  ASN A CG  1 
ATOM   814  C CG  B ASN A 1 101 ? -1.958  -27.108 14.167  0.50 31.24  ? 686  ASN A CG  1 
ATOM   815  O OD1 A ASN A 1 101 ? -3.267  -28.389 12.099  0.50 30.87  ? 686  ASN A OD1 1 
ATOM   816  O OD1 B ASN A 1 101 ? -2.499  -26.962 15.271  0.50 33.58  ? 686  ASN A OD1 1 
ATOM   817  N ND2 A ASN A 1 101 ? -4.501  -27.125 13.483  0.50 28.62  ? 686  ASN A ND2 1 
ATOM   818  N ND2 B ASN A 1 101 ? -1.044  -28.036 13.946  0.50 32.60  ? 686  ASN A ND2 1 
ATOM   819  N N   . GLY A 1 102 ? -1.648  -22.840 13.166  1.00 22.33  ? 687  GLY A N   1 
ATOM   820  C CA  . GLY A 1 102 ? -0.592  -21.878 13.502  1.00 22.04  ? 687  GLY A CA  1 
ATOM   821  C C   . GLY A 1 102 ? 0.673   -22.029 12.676  1.00 20.78  ? 687  GLY A C   1 
ATOM   822  O O   . GLY A 1 102 ? 1.770   -21.631 13.124  1.00 19.48  ? 687  GLY A O   1 
ATOM   823  N N   . TYR A 1 103 ? 0.541   -22.439 11.407  1.00 18.19  ? 688  TYR A N   1 
ATOM   824  C CA  . TYR A 1 103 ? 1.674   -22.499 10.512  1.00 17.90  ? 688  TYR A CA  1 
ATOM   825  C C   . TYR A 1 103 ? 1.373   -21.813 9.191   1.00 16.08  ? 688  TYR A C   1 
ATOM   826  O O   . TYR A 1 103 ? 0.322   -22.054 8.608   1.00 17.36  ? 688  TYR A O   1 
ATOM   827  C CB  . TYR A 1 103 ? 2.055   -23.913 10.104  1.00 19.79  ? 688  TYR A CB  1 
ATOM   828  C CG  . TYR A 1 103 ? 2.446   -24.833 11.238  1.00 24.13  ? 688  TYR A CG  1 
ATOM   829  C CD1 . TYR A 1 103 ? 1.489   -25.571 11.922  1.00 28.09  ? 688  TYR A CD1 1 
ATOM   830  C CD2 . TYR A 1 103 ? 3.781   -25.010 11.564  1.00 26.02  ? 688  TYR A CD2 1 
ATOM   831  C CE1 . TYR A 1 103 ? 1.851   -26.416 12.948  1.00 31.37  ? 688  TYR A CE1 1 
ATOM   832  C CE2 . TYR A 1 103 ? 4.156   -25.855 12.593  1.00 30.68  ? 688  TYR A CE2 1 
ATOM   833  C CZ  . TYR A 1 103 ? 3.189   -26.617 13.224  1.00 34.92  ? 688  TYR A CZ  1 
ATOM   834  O OH  . TYR A 1 103 ? 3.483   -27.487 14.228  1.00 42.37  ? 688  TYR A OH  1 
ATOM   835  N N   . TRP A 1 104 ? 2.298   -21.005 8.726   1.00 13.63  ? 689  TRP A N   1 
ATOM   836  C CA  . TRP A 1 104 ? 2.189   -20.320 7.450   1.00 13.10  ? 689  TRP A CA  1 
ATOM   837  C C   . TRP A 1 104 ? 3.480   -20.571 6.692   1.00 13.04  ? 689  TRP A C   1 
ATOM   838  O O   . TRP A 1 104 ? 4.505   -19.895 6.936   1.00 12.24  ? 689  TRP A O   1 
ATOM   839  C CB  . TRP A 1 104 ? 1.933   -18.812 7.620   1.00 12.89  ? 689  TRP A CB  1 
ATOM   840  C CG  . TRP A 1 104 ? 0.726   -18.461 8.421   1.00 14.54  ? 689  TRP A CG  1 
ATOM   841  C CD1 . TRP A 1 104 ? -0.509  -18.224 7.921   1.00 16.74  ? 689  TRP A CD1 1 
ATOM   842  C CD2 . TRP A 1 104 ? 0.595   -18.405 9.858   1.00 15.20  ? 689  TRP A CD2 1 
ATOM   843  N NE1 . TRP A 1 104 ? -1.402  -18.005 8.928   1.00 17.01  ? 689  TRP A NE1 1 
ATOM   844  C CE2 . TRP A 1 104 ? -0.757  -18.113 10.120  1.00 16.59  ? 689  TRP A CE2 1 
ATOM   845  C CE3 . TRP A 1 104 ? 1.480   -18.551 10.908  1.00 15.69  ? 689  TRP A CE3 1 
ATOM   846  C CZ2 . TRP A 1 104 ? -1.247  -17.919 11.415  1.00 19.32  ? 689  TRP A CZ2 1 
ATOM   847  C CZ3 . TRP A 1 104 ? 1.001   -18.372 12.188  1.00 18.50  ? 689  TRP A CZ3 1 
ATOM   848  C CH2 . TRP A 1 104 ? -0.329  -18.045 12.415  1.00 19.23  ? 689  TRP A CH2 1 
ATOM   849  N N   . VAL A 1 105 ? 3.464   -21.592 5.792   1.00 13.26  ? 690  VAL A N   1 
ATOM   850  C CA  . VAL A 1 105 ? 4.706   -22.024 5.186   1.00 12.58  ? 690  VAL A CA  1 
ATOM   851  C C   . VAL A 1 105 ? 4.490   -22.258 3.698   1.00 13.27  ? 690  VAL A C   1 
ATOM   852  O O   . VAL A 1 105 ? 3.359   -22.482 3.243   1.00 14.35  ? 690  VAL A O   1 
ATOM   853  C CB  . VAL A 1 105 ? 5.271   -23.284 5.850   1.00 13.55  ? 690  VAL A CB  1 
ATOM   854  C CG1 . VAL A 1 105 ? 5.598   -23.043 7.332   1.00 15.05  ? 690  VAL A CG1 1 
ATOM   855  C CG2 . VAL A 1 105 ? 4.405   -24.483 5.685   1.00 14.76  ? 690  VAL A CG2 1 
ATOM   856  N N   A VAL A 1 106 ? 5.614   -22.210 3.000   0.50 12.64  ? 691  VAL A N   1 
ATOM   857  N N   B VAL A 1 106 ? 5.605   -22.210 2.992   0.50 13.30  ? 691  VAL A N   1 
ATOM   858  C CA  A VAL A 1 106 ? 5.740   -22.667 1.632   0.50 13.11  ? 691  VAL A CA  1 
ATOM   859  C CA  B VAL A 1 106 ? 5.691   -22.668 1.623   0.50 14.35  ? 691  VAL A CA  1 
ATOM   860  C C   A VAL A 1 106 ? 6.653   -23.880 1.650   0.50 14.80  ? 691  VAL A C   1 
ATOM   861  C C   B VAL A 1 106 ? 6.668   -23.832 1.610   0.50 15.50  ? 691  VAL A C   1 
ATOM   862  O O   A VAL A 1 106 ? 7.579   -23.994 2.439   0.50 14.38  ? 691  VAL A O   1 
ATOM   863  O O   B VAL A 1 106 ? 7.655   -23.838 2.340   0.50 14.84  ? 691  VAL A O   1 
ATOM   864  C CB  A VAL A 1 106 ? 6.238   -21.568 0.681   0.50 12.73  ? 691  VAL A CB  1 
ATOM   865  C CB  B VAL A 1 106 ? 6.085   -21.545 0.651   0.50 15.19  ? 691  VAL A CB  1 
ATOM   866  C CG1 A VAL A 1 106 ? 6.729   -22.113 -0.665  0.50 13.46  ? 691  VAL A CG1 1 
ATOM   867  C CG1 B VAL A 1 106 ? 5.043   -20.435 0.643   0.50 15.45  ? 691  VAL A CG1 1 
ATOM   868  C CG2 A VAL A 1 106 ? 5.157   -20.514 0.491   0.50 13.08  ? 691  VAL A CG2 1 
ATOM   869  C CG2 B VAL A 1 106 ? 7.463   -20.976 0.950   0.50 16.47  ? 691  VAL A CG2 1 
ATOM   870  N N   . MET A 1 107 ? 6.390   -24.805 0.754   1.00 16.60  ? 693  MET A N   1 
ATOM   871  C CA  . MET A 1 107 ? 7.161   -26.019 0.729   1.00 18.02  ? 693  MET A CA  1 
ATOM   872  C C   . MET A 1 107 ? 7.428   -26.418 -0.711  1.00 18.78  ? 693  MET A C   1 
ATOM   873  O O   . MET A 1 107 ? 6.595   -26.244 -1.607  1.00 19.82  ? 693  MET A O   1 
ATOM   874  C CB  . MET A 1 107 ? 6.467   -27.147 1.453   1.00 23.31  ? 693  MET A CB  1 
ATOM   875  C CG  . MET A 1 107 ? 5.226   -27.563 0.919   1.00 29.81  ? 693  MET A CG  1 
ATOM   876  S SD  . MET A 1 107 ? 4.606   -28.729 2.155   1.00 50.39  ? 693  MET A SD  1 
ATOM   877  C CE  . MET A 1 107 ? 5.895   -29.994 2.252   1.00 33.89  ? 693  MET A CE  1 
ATOM   878  N N   . MET A 1 108 ? 8.589   -27.031 -0.871  1.00 17.38  ? 694  MET A N   1 
ATOM   879  C CA  . MET A 1 108 ? 8.943   -27.716 -2.101  1.00 17.80  ? 694  MET A CA  1 
ATOM   880  C C   . MET A 1 108 ? 8.964   -29.207 -1.839  1.00 19.66  ? 694  MET A C   1 
ATOM   881  O O   . MET A 1 108 ? 9.502   -29.644 -0.836  1.00 19.01  ? 694  MET A O   1 
ATOM   882  C CB  . MET A 1 108 ? 10.338  -27.284 -2.557  1.00 17.81  ? 694  MET A CB  1 
ATOM   883  C CG  . MET A 1 108 ? 10.725  -27.888 -3.912  1.00 19.17  ? 694  MET A CG  1 
ATOM   884  S SD  . MET A 1 108 ? 12.459  -27.478 -4.274  1.00 20.87  ? 694  MET A SD  1 
ATOM   885  C CE  . MET A 1 108 ? 12.490  -27.963 -5.997  1.00 22.79  ? 694  MET A CE  1 
ATOM   886  N N   . LYS A 1 109 ? 8.409   -29.974 -2.777  1.00 22.96  ? 695  LYS A N   1 
ATOM   887  C CA  . LYS A 1 109 ? 8.406   -31.425 -2.694  1.00 29.65  ? 695  LYS A CA  1 
ATOM   888  C C   . LYS A 1 109 ? 7.993   -31.959 -4.062  1.00 33.66  ? 695  LYS A C   1 
ATOM   889  O O   . LYS A 1 109 ? 7.026   -31.465 -4.632  1.00 33.51  ? 695  LYS A O   1 
ATOM   890  C CB  . LYS A 1 109 ? 7.432   -31.870 -1.600  1.00 34.29  ? 695  LYS A CB  1 
ATOM   891  C CG  . LYS A 1 109 ? 7.290   -33.369 -1.430  1.00 43.91  ? 695  LYS A CG  1 
ATOM   892  C CD  . LYS A 1 109 ? 6.413   -33.685 -0.221  1.00 53.75  ? 695  LYS A CD  1 
ATOM   893  C CE  . LYS A 1 109 ? 6.123   -35.149 -0.042  1.00 60.72  ? 695  LYS A CE  1 
ATOM   894  N NZ  . LYS A 1 109 ? 5.564   -35.336 1.297   1.00 64.25  ? 695  LYS A NZ  1 
ATOM   895  N N   . GLU A 1 110 ? 8.755   -32.932 -4.570  1.00 39.23  ? 696  GLU A N   1 
ATOM   896  C CA  . GLU A 1 110 ? 8.387   -33.701 -5.745  1.00 41.51  ? 696  GLU A CA  1 
ATOM   897  C C   . GLU A 1 110 ? 8.218   -32.774 -6.943  1.00 38.85  ? 696  GLU A C   1 
ATOM   898  O O   . GLU A 1 110 ? 7.265   -32.867 -7.705  1.00 39.26  ? 696  GLU A O   1 
ATOM   899  C CB  . GLU A 1 110 ? 7.227   -34.612 -5.349  1.00 46.98  ? 696  GLU A CB  1 
ATOM   900  C CG  . GLU A 1 110 ? 7.692   -35.595 -4.277  1.00 52.44  ? 696  GLU A CG  1 
ATOM   901  C CD  . GLU A 1 110 ? 6.813   -36.791 -3.980  1.00 61.35  ? 696  GLU A CD  1 
ATOM   902  O OE1 . GLU A 1 110 ? 6.987   -37.811 -4.678  1.00 70.25  ? 696  GLU A OE1 1 
ATOM   903  O OE2 . GLU A 1 110 ? 5.977   -36.697 -3.048  1.00 69.32  ? 696  GLU A OE2 1 
ATOM   904  N N   . ASN A 1 111 ? 9.213   -31.918 -7.105  1.00 35.44  ? 697  ASN A N   1 
ATOM   905  C CA  . ASN A 1 111 ? 9.336   -30.962 -8.188  1.00 40.05  ? 697  ASN A CA  1 
ATOM   906  C C   . ASN A 1 111 ? 8.134   -30.025 -8.245  1.00 39.78  ? 697  ASN A C   1 
ATOM   907  O O   . ASN A 1 111 ? 7.788   -29.516 -9.311  1.00 40.75  ? 697  ASN A O   1 
ATOM   908  C CB  . ASN A 1 111 ? 9.602   -31.654 -9.524  1.00 46.54  ? 697  ASN A CB  1 
ATOM   909  C CG  . ASN A 1 111 ? 10.796  -31.037 -10.219 1.00 53.06  ? 697  ASN A CG  1 
ATOM   910  O OD1 . ASN A 1 111 ? 11.398  -30.082 -9.708  1.00 57.48  ? 697  ASN A OD1 1 
ATOM   911  N ND2 . ASN A 1 111 ? 11.167  -31.572 -11.372 1.00 63.54  ? 697  ASN A ND2 1 
ATOM   912  N N   . GLU A 1 112 ? 7.536   -29.746 -7.084  1.00 31.71  ? 698  GLU A N   1 
ATOM   913  C CA  . GLU A 1 112 ? 6.385   -28.888 -7.033  1.00 31.17  ? 698  GLU A CA  1 
ATOM   914  C C   . GLU A 1 112 ? 6.515   -28.017 -5.795  1.00 25.47  ? 698  GLU A C   1 
ATOM   915  O O   . GLU A 1 112 ? 7.164   -28.395 -4.814  1.00 24.50  ? 698  GLU A O   1 
ATOM   916  C CB  . GLU A 1 112 ? 5.083   -29.693 -6.974  1.00 36.38  ? 698  GLU A CB  1 
ATOM   917  C CG  . GLU A 1 112 ? 3.856   -28.876 -6.599  1.00 45.78  ? 698  GLU A CG  1 
ATOM   918  C CD  . GLU A 1 112 ? 2.517   -29.554 -6.842  1.00 56.89  ? 698  GLU A CD  1 
ATOM   919  O OE1 . GLU A 1 112 ? 2.273   -30.132 -7.943  1.00 60.39  ? 698  GLU A OE1 1 
ATOM   920  O OE2 . GLU A 1 112 ? 1.689   -29.450 -5.902  1.00 68.47  ? 698  GLU A OE2 1 
ATOM   921  N N   . TYR A 1 113 ? 5.944   -26.814 -5.901  1.00 22.97  ? 699  TYR A N   1 
ATOM   922  C CA  . TYR A 1 113 ? 5.911   -25.887 -4.805  1.00 20.80  ? 699  TYR A CA  1 
ATOM   923  C C   . TYR A 1 113 ? 4.463   -25.701 -4.377  1.00 21.07  ? 699  TYR A C   1 
ATOM   924  O O   . TYR A 1 113 ? 3.596   -25.567 -5.215  1.00 22.44  ? 699  TYR A O   1 
ATOM   925  C CB  . TYR A 1 113 ? 6.492   -24.550 -5.237  1.00 20.28  ? 699  TYR A CB  1 
ATOM   926  C CG  . TYR A 1 113 ? 7.933   -24.643 -5.739  1.00 18.95  ? 699  TYR A CG  1 
ATOM   927  C CD1 . TYR A 1 113 ? 8.210   -24.838 -7.074  1.00 20.55  ? 699  TYR A CD1 1 
ATOM   928  C CD2 . TYR A 1 113 ? 8.996   -24.479 -4.872  1.00 18.04  ? 699  TYR A CD2 1 
ATOM   929  C CE1 . TYR A 1 113 ? 9.523   -24.945 -7.526  1.00 20.81  ? 699  TYR A CE1 1 
ATOM   930  C CE2 . TYR A 1 113 ? 10.312  -24.577 -5.311  1.00 17.76  ? 699  TYR A CE2 1 
ATOM   931  C CZ  . TYR A 1 113 ? 10.572  -24.746 -6.647  1.00 19.17  ? 699  TYR A CZ  1 
ATOM   932  O OH  . TYR A 1 113 ? 11.848  -24.868 -7.103  1.00 20.72  ? 699  TYR A OH  1 
ATOM   933  N N   . GLN A 1 114 ? 4.272   -25.614 -3.049  1.00 19.01  ? 700  GLN A N   1 
ATOM   934  C CA  . GLN A 1 114 ? 2.939   -25.396 -2.500  1.00 19.90  ? 700  GLN A CA  1 
ATOM   935  C C   . GLN A 1 114 ? 3.002   -24.408 -1.347  1.00 17.22  ? 700  GLN A C   1 
ATOM   936  O O   . GLN A 1 114 ? 3.954   -24.381 -0.604  1.00 17.91  ? 700  GLN A O   1 
ATOM   937  C CB  . GLN A 1 114 ? 2.363   -26.706 -1.906  1.00 22.80  ? 700  GLN A CB  1 
ATOM   938  C CG  . GLN A 1 114 ? 2.106   -27.853 -2.851  1.00 30.53  ? 700  GLN A CG  1 
ATOM   939  C CD  . GLN A 1 114 ? 1.576   -29.069 -2.114  1.00 31.90  ? 700  GLN A CD  1 
ATOM   940  O OE1 . GLN A 1 114 ? 1.647   -29.180 -0.882  1.00 34.67  ? 700  GLN A OE1 1 
ATOM   941  N NE2 . GLN A 1 114 ? 1.072   -29.998 -2.889  1.00 44.66  ? 700  GLN A NE2 1 
ATOM   942  N N   . ALA A 1 115 ? 1.980   -23.572 -1.211  1.00 16.35  ? 701  ALA A N   1 
ATOM   943  C CA  . ALA A 1 115 ? 1.714   -22.877 0.045   1.00 15.14  ? 701  ALA A CA  1 
ATOM   944  C C   . ALA A 1 115 ? 0.791   -23.757 0.891   1.00 16.54  ? 701  ALA A C   1 
ATOM   945  O O   . ALA A 1 115 ? -0.157  -24.336 0.377   1.00 17.44  ? 701  ALA A O   1 
ATOM   946  C CB  . ALA A 1 115 ? 1.041   -21.541 -0.204  1.00 16.70  ? 701  ALA A CB  1 
ATOM   947  N N   A SER A 1 116 ? 1.090   -23.931 2.169   0.50 16.24  ? 702  SER A N   1 
ATOM   948  N N   B SER A 1 116 ? 1.032   -23.649 2.233   0.50 16.30  ? 702  SER A N   1 
ATOM   949  C CA  A SER A 1 116 ? 0.349   -24.920 2.914   0.50 18.00  ? 702  SER A CA  1 
ATOM   950  C CA  B SER A 1 116 ? 0.437   -24.397 3.350   0.50 17.82  ? 702  SER A CA  1 
ATOM   951  C C   A SER A 1 116 ? -0.921  -24.318 3.511   0.50 18.17  ? 702  SER A C   1 
ATOM   952  C C   B SER A 1 116 ? -0.953  -23.919 3.696   0.50 18.49  ? 702  SER A C   1 
ATOM   953  O O   A SER A 1 116 ? -1.219  -24.578 4.683   0.50 18.86  ? 702  SER A O   1 
ATOM   954  O O   B SER A 1 116 ? -1.347  -23.850 4.851   0.50 19.55  ? 702  SER A O   1 
ATOM   955  C CB  A SER A 1 116 ? 1.285   -25.594 3.924   0.50 18.98  ? 702  SER A CB  1 
ATOM   956  C CB  B SER A 1 116 ? 1.294   -24.335 4.667   0.50 16.61  ? 702  SER A CB  1 
ATOM   957  O OG  A SER A 1 116 ? 2.395   -26.171 3.225   0.50 21.38  ? 702  SER A OG  1 
ATOM   958  O OG  B SER A 1 116 ? 1.075   -23.297 5.674   0.50 15.21  ? 702  SER A OG  1 
ATOM   959  N N   . SER A 1 117 ? -1.728  -23.577 2.687   1.00 18.13  ? 703  SER A N   1 
ATOM   960  C CA  . SER A 1 117 ? -3.171  -23.450 2.884   1.00 18.39  ? 703  SER A CA  1 
ATOM   961  C C   . SER A 1 117 ? -3.738  -24.850 3.012   1.00 18.61  ? 703  SER A C   1 
ATOM   962  O O   . SER A 1 117 ? -3.035  -25.821 2.718   1.00 18.93  ? 703  SER A O   1 
ATOM   963  C CB  . SER A 1 117 ? -3.809  -22.658 1.775   1.00 18.46  ? 703  SER A CB  1 
ATOM   964  O OG  . SER A 1 117 ? -3.563  -23.296 0.511   1.00 18.39  ? 703  SER A OG  1 
ATOM   965  N N   . VAL A 1 118 ? -5.021  -24.966 3.402   1.00 19.10  ? 704  VAL A N   1 
ATOM   966  C CA  . VAL A 1 118 ? -5.708  -26.245 3.421   1.00 21.70  ? 704  VAL A CA  1 
ATOM   967  C C   . VAL A 1 118 ? -6.978  -26.075 2.617   1.00 22.59  ? 704  VAL A C   1 
ATOM   968  O O   . VAL A 1 118 ? -7.874  -25.355 3.047   1.00 23.22  ? 704  VAL A O   1 
ATOM   969  C CB  . VAL A 1 118 ? -6.064  -26.724 4.846   1.00 23.63  ? 704  VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 118 ? -6.602  -28.158 4.858   1.00 26.56  ? 704  VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 118 ? -4.841  -26.647 5.752   1.00 23.56  ? 704  VAL A CG2 1 
ATOM   972  N N   . PRO A 1 119 ? -7.120  -26.711 1.437   1.00 22.96  ? 705  PRO A N   1 
ATOM   973  C CA  . PRO A 1 119 ? -6.094  -27.537 0.819   1.00 22.87  ? 705  PRO A CA  1 
ATOM   974  C C   . PRO A 1 119 ? -4.907  -26.739 0.332   1.00 21.23  ? 705  PRO A C   1 
ATOM   975  O O   . PRO A 1 119 ? -4.986  -25.536 0.192   1.00 20.13  ? 705  PRO A O   1 
ATOM   976  C CB  . PRO A 1 119 ? -6.804  -28.099 -0.407  1.00 24.55  ? 705  PRO A CB  1 
ATOM   977  C CG  . PRO A 1 119 ? -8.283  -28.001 -0.055  1.00 26.33  ? 705  PRO A CG  1 
ATOM   978  C CD  . PRO A 1 119 ? -8.327  -26.663 0.619   1.00 25.04  ? 705  PRO A CD  1 
ATOM   979  N N   . PRO A 1 120 ? -3.715  -27.358 0.156   1.00 20.93  ? 706  PRO A N   1 
ATOM   980  C CA  . PRO A 1 120 ? -2.551  -26.637 -0.293  1.00 19.92  ? 706  PRO A CA  1 
ATOM   981  C C   . PRO A 1 120 ? -2.691  -26.043 -1.679  1.00 19.58  ? 706  PRO A C   1 
ATOM   982  O O   . PRO A 1 120 ? -3.390  -26.559 -2.519  1.00 21.03  ? 706  PRO A O   1 
ATOM   983  C CB  . PRO A 1 120 ? -1.400  -27.663 -0.185  1.00 20.03  ? 706  PRO A CB  1 
ATOM   984  C CG  . PRO A 1 120 ? -1.995  -28.903 0.300   1.00 22.97  ? 706  PRO A CG  1 
ATOM   985  C CD  . PRO A 1 120 ? -3.455  -28.781 0.416   1.00 23.27  ? 706  PRO A CD  1 
ATOM   986  N N   . THR A 1 121 ? -2.073  -24.860 -1.805  1.00 18.65  ? 707  THR A N   1 
ATOM   987  C CA  . THR A 1 121 ? -2.153  -24.138 -3.063  1.00 19.82  ? 707  THR A CA  1 
ATOM   988  C C   . THR A 1 121 ? -0.908  -24.481 -3.853  1.00 20.61  ? 707  THR A C   1 
ATOM   989  O O   . THR A 1 121 ? 0.198   -24.199 -3.410  1.00 20.55  ? 707  THR A O   1 
ATOM   990  C CB  . THR A 1 121 ? -2.218  -22.636 -2.770  1.00 19.60  ? 707  THR A CB  1 
ATOM   991  O OG1 . THR A 1 121 ? -3.420  -22.305 -2.059  1.00 20.74  ? 707  THR A OG1 1 
ATOM   992  C CG2 . THR A 1 121 ? -2.212  -21.863 -4.075  1.00 21.53  ? 707  THR A CG2 1 
ATOM   993  N N   . ARG A 1 122 ? -1.087  -25.050 -5.024  1.00 23.77  ? 708  ARG A N   1 
ATOM   994  C CA  . ARG A 1 122 ? 0.072   -25.378 -5.841  1.00 27.00  ? 708  ARG A CA  1 
ATOM   995  C C   . ARG A 1 122 ? 0.480   -24.082 -6.531  1.00 27.46  ? 708  ARG A C   1 
ATOM   996  O O   . ARG A 1 122 ? -0.363  -23.357 -7.091  1.00 31.27  ? 708  ARG A O   1 
ATOM   997  C CB  . ARG A 1 122 ? -0.364  -26.544 -6.720  1.00 35.26  ? 708  ARG A CB  1 
ATOM   998  C CG  . ARG A 1 122 ? 0.601   -27.146 -7.725  1.00 45.18  ? 708  ARG A CG  1 
ATOM   999  C CD  . ARG A 1 122 ? -0.267  -28.217 -8.426  1.00 58.91  ? 708  ARG A CD  1 
ATOM   1000 N NE  . ARG A 1 122 ? -1.453  -28.620 -7.635  1.00 64.08  ? 708  ARG A NE  1 
ATOM   1001 C CZ  . ARG A 1 122 ? -1.502  -29.375 -6.526  1.00 67.03  ? 708  ARG A CZ  1 
ATOM   1002 N NH1 . ARG A 1 122 ? -2.430  -29.126 -5.608  1.00 65.49  ? 708  ARG A NH1 1 
ATOM   1003 N NH2 . ARG A 1 122 ? -0.545  -30.254 -6.268  1.00 72.81  ? 708  ARG A NH2 1 
ATOM   1004 N N   . LEU A 1 123 ? 1.781   -23.825 -6.523  1.00 25.67  ? 709  LEU A N   1 
ATOM   1005 C CA  . LEU A 1 123 ? 2.318   -22.556 -6.988  1.00 26.82  ? 709  LEU A CA  1 
ATOM   1006 C C   . LEU A 1 123 ? 2.911   -22.809 -8.375  1.00 29.81  ? 709  LEU A C   1 
ATOM   1007 O O   . LEU A 1 123 ? 3.564   -23.813 -8.558  1.00 31.04  ? 709  LEU A O   1 
ATOM   1008 C CB  . LEU A 1 123 ? 3.352   -22.030 -6.019  1.00 25.40  ? 709  LEU A CB  1 
ATOM   1009 C CG  . LEU A 1 123 ? 2.870   -21.787 -4.579  1.00 24.68  ? 709  LEU A CG  1 
ATOM   1010 C CD1 . LEU A 1 123 ? 3.995   -21.544 -3.664  1.00 25.13  ? 709  LEU A CD1 1 
ATOM   1011 C CD2 . LEU A 1 123 ? 1.906   -20.645 -4.476  1.00 26.46  ? 709  LEU A CD2 1 
ATOM   1012 N N   . LEU A 1 124 ? 2.648   -21.923 -9.321  1.00 32.75  ? 710  LEU A N   1 
ATOM   1013 C CA  . LEU A 1 124 ? 3.237   -22.002 -10.651 1.00 37.35  ? 710  LEU A CA  1 
ATOM   1014 C C   . LEU A 1 124 ? 4.507   -21.149 -10.635 1.00 34.11  ? 710  LEU A C   1 
ATOM   1015 O O   . LEU A 1 124 ? 4.471   -19.920 -10.615 1.00 35.60  ? 710  LEU A O   1 
ATOM   1016 C CB  . LEU A 1 124 ? 2.229   -21.524 -11.692 1.00 43.28  ? 710  LEU A CB  1 
ATOM   1017 C CG  . LEU A 1 124 ? 2.792   -21.313 -13.109 1.00 51.03  ? 710  LEU A CG  1 
ATOM   1018 C CD1 . LEU A 1 124 ? 3.330   -22.580 -13.758 1.00 55.74  ? 710  LEU A CD1 1 
ATOM   1019 C CD2 . LEU A 1 124 ? 1.736   -20.677 -13.993 1.00 58.17  ? 710  LEU A CD2 1 
ATOM   1020 N N   . ILE A 1 125 ? 5.649   -21.805 -10.536 1.00 34.62  ? 711  ILE A N   1 
ATOM   1021 C CA  . ILE A 1 125 ? 6.893   -21.056 -10.463 1.00 33.87  ? 711  ILE A CA  1 
ATOM   1022 C C   . ILE A 1 125 ? 7.658   -21.361 -11.735 1.00 35.64  ? 711  ILE A C   1 
ATOM   1023 O O   . ILE A 1 125 ? 7.960   -22.520 -11.993 1.00 41.58  ? 711  ILE A O   1 
ATOM   1024 C CB  . ILE A 1 125 ? 7.651   -21.410 -9.169  1.00 36.54  ? 711  ILE A CB  1 
ATOM   1025 C CG1 . ILE A 1 125 ? 6.841   -20.908 -7.948  1.00 35.25  ? 711  ILE A CG1 1 
ATOM   1026 C CG2 . ILE A 1 125 ? 9.075   -20.860 -9.219  1.00 36.50  ? 711  ILE A CG2 1 
ATOM   1027 C CD1 . ILE A 1 125 ? 7.559   -20.904 -6.624  1.00 37.51  ? 711  ILE A CD1 1 
ATOM   1028 N N   . LYS A 1 126 ? 7.843   -20.354 -12.582 1.00 34.70  ? 712  LYS A N   1 
ATOM   1029 C CA  . LYS A 1 126 ? 8.525   -20.603 -13.852 1.00 39.95  ? 712  LYS A CA  1 
ATOM   1030 C C   . LYS A 1 126 ? 10.048  -20.536 -13.673 1.00 33.72  ? 712  LYS A C   1 
ATOM   1031 O O   . LYS A 1 126 ? 10.788  -21.200 -14.378 1.00 35.92  ? 712  LYS A O   1 
ATOM   1032 C CB  . LYS A 1 126 ? 7.966   -19.673 -14.933 1.00 47.55  ? 712  LYS A CB  1 
ATOM   1033 C CG  . LYS A 1 126 ? 6.577   -20.066 -15.456 1.00 56.74  ? 712  LYS A CG  1 
ATOM   1034 C CD  . LYS A 1 126 ? 6.092   -19.310 -16.695 1.00 67.67  ? 712  LYS A CD  1 
ATOM   1035 C CE  . LYS A 1 126 ? 5.818   -17.851 -16.449 1.00 74.21  ? 712  LYS A CE  1 
ATOM   1036 N NZ  . LYS A 1 126 ? 4.588   -17.616 -15.686 1.00 75.17  ? 712  LYS A NZ  1 
ATOM   1037 N N   . GLU A 1 127 ? 10.535  -19.745 -12.719 1.00 30.12  ? 713  GLU A N   1 
ATOM   1038 C CA  . GLU A 1 127 ? 11.964  -19.649 -12.446 1.00 29.59  ? 713  GLU A CA  1 
ATOM   1039 C C   . GLU A 1 127 ? 12.241  -20.143 -11.033 1.00 24.24  ? 713  GLU A C   1 
ATOM   1040 O O   . GLU A 1 127 ? 11.876  -19.469 -10.090 1.00 24.32  ? 713  GLU A O   1 
ATOM   1041 C CB  . GLU A 1 127 ? 12.372  -18.189 -12.612 1.00 35.96  ? 713  GLU A CB  1 
ATOM   1042 C CG  . GLU A 1 127 ? 13.842  -17.927 -12.294 1.00 45.07  ? 713  GLU A CG  1 
ATOM   1043 C CD  . GLU A 1 127 ? 14.337  -16.498 -12.525 1.00 48.59  ? 713  GLU A CD  1 
ATOM   1044 O OE1 . GLU A 1 127 ? 13.580  -15.706 -13.144 1.00 48.60  ? 713  GLU A OE1 1 
ATOM   1045 O OE2 . GLU A 1 127 ? 15.492  -16.212 -12.079 1.00 49.55  ? 713  GLU A OE2 1 
ATOM   1046 N N   . PRO A 1 128 ? 12.807  -21.340 -10.839 1.00 24.70  ? 714  PRO A N   1 
ATOM   1047 C CA  . PRO A 1 128 ? 12.884  -21.897 -9.494  1.00 23.77  ? 714  PRO A CA  1 
ATOM   1048 C C   . PRO A 1 128 ? 13.694  -20.987 -8.591  1.00 21.41  ? 714  PRO A C   1 
ATOM   1049 O O   . PRO A 1 128 ? 14.814  -20.573 -8.944  1.00 22.40  ? 714  PRO A O   1 
ATOM   1050 C CB  . PRO A 1 128 ? 13.501  -23.268 -9.678  1.00 26.70  ? 714  PRO A CB  1 
ATOM   1051 C CG  . PRO A 1 128 ? 13.324  -23.560 -11.141 1.00 29.97  ? 714  PRO A CG  1 
ATOM   1052 C CD  . PRO A 1 128 ? 13.299  -22.266 -11.869 1.00 29.65  ? 714  PRO A CD  1 
ATOM   1053 N N   . PRO A 1 129 ? 13.202  -20.727 -7.362  1.00 18.82  ? 715  PRO A N   1 
ATOM   1054 C CA  . PRO A 1 129 ? 13.950  -19.880 -6.444  1.00 17.01  ? 715  PRO A CA  1 
ATOM   1055 C C   . PRO A 1 129 ? 15.196  -20.590 -5.903  1.00 18.05  ? 715  PRO A C   1 
ATOM   1056 O O   . PRO A 1 129 ? 15.142  -21.782 -5.617  1.00 18.74  ? 715  PRO A O   1 
ATOM   1057 C CB  . PRO A 1 129 ? 12.948  -19.652 -5.327  1.00 16.98  ? 715  PRO A CB  1 
ATOM   1058 C CG  . PRO A 1 129 ? 12.066  -20.869 -5.406  1.00 17.08  ? 715  PRO A CG  1 
ATOM   1059 C CD  . PRO A 1 129 ? 11.910  -21.183 -6.822  1.00 17.99  ? 715  PRO A CD  1 
ATOM   1060 N N   . LYS A 1 130 ? 16.299  -19.865 -5.785  1.00 16.67  ? 716  LYS A N   1 
ATOM   1061 C CA  . LYS A 1 130 ? 17.481  -20.337 -5.079  1.00 17.57  ? 716  LYS A CA  1 
ATOM   1062 C C   . LYS A 1 130 ? 17.553  -19.673 -3.712  1.00 15.94  ? 716  LYS A C   1 
ATOM   1063 O O   . LYS A 1 130 ? 18.310  -20.116 -2.872  1.00 15.46  ? 716  LYS A O   1 
ATOM   1064 C CB  . LYS A 1 130 ? 18.723  -20.046 -5.923  1.00 18.31  ? 716  LYS A CB  1 
ATOM   1065 C CG  . LYS A 1 130 ? 18.609  -20.564 -7.349  1.00 21.22  ? 716  LYS A CG  1 
ATOM   1066 C CD  . LYS A 1 130 ? 18.325  -22.053 -7.440  1.00 23.56  ? 716  LYS A CD  1 
ATOM   1067 C CE  . LYS A 1 130 ? 18.344  -22.531 -8.863  1.00 27.06  ? 716  LYS A CE  1 
ATOM   1068 N NZ  . LYS A 1 130 ? 18.103  -23.974 -8.995  1.00 28.82  ? 716  LYS A NZ  1 
ATOM   1069 N N   . ARG A 1 131 ? 16.782  -18.588 -3.519  1.00 14.56  ? 717  ARG A N   1 
ATOM   1070 C CA  . ARG A 1 131 ? 16.683  -17.895 -2.256  1.00 13.76  ? 717  ARG A CA  1 
ATOM   1071 C C   . ARG A 1 131 ? 15.233  -17.429 -2.109  1.00 12.71  ? 717  ARG A C   1 
ATOM   1072 O O   . ARG A 1 131 ? 14.661  -16.962 -3.113  1.00 13.56  ? 717  ARG A O   1 
ATOM   1073 C CB  . ARG A 1 131 ? 17.644  -16.718 -2.286  1.00 17.36  ? 717  ARG A CB  1 
ATOM   1074 C CG  . ARG A 1 131 ? 17.792  -16.015 -0.975  1.00 20.01  ? 717  ARG A CG  1 
ATOM   1075 C CD  . ARG A 1 131 ? 18.663  -14.783 -1.153  1.00 27.58  ? 717  ARG A CD  1 
ATOM   1076 N NE  . ARG A 1 131 ? 20.066  -15.156 -1.240  1.00 31.28  ? 717  ARG A NE  1 
ATOM   1077 C CZ  . ARG A 1 131 ? 21.033  -14.451 -0.612  1.00 39.60  ? 717  ARG A CZ  1 
ATOM   1078 N NH1 . ARG A 1 131 ? 20.825  -13.271 -0.066  1.00 38.41  ? 717  ARG A NH1 1 
ATOM   1079 N NH2 . ARG A 1 131 ? 22.250  -14.923 -0.546  1.00 43.10  ? 717  ARG A NH2 1 
ATOM   1080 N N   . VAL A 1 132 ? 14.729  -17.591 -0.913  1.00 12.21  ? 718  VAL A N   1 
ATOM   1081 C CA  . VAL A 1 132 ? 13.342  -17.290 -0.583  1.00 11.58  ? 718  VAL A CA  1 
ATOM   1082 C C   . VAL A 1 132 ? 13.347  -16.234 0.496   1.00 12.14  ? 718  VAL A C   1 
ATOM   1083 O O   . VAL A 1 132 ? 14.067  -16.382 1.493   1.00 13.30  ? 718  VAL A O   1 
ATOM   1084 C CB  . VAL A 1 132 ? 12.586  -18.554 -0.155  1.00 11.55  ? 718  VAL A CB  1 
ATOM   1085 C CG1 . VAL A 1 132 ? 11.182  -18.254 0.275   1.00 12.03  ? 718  VAL A CG1 1 
ATOM   1086 C CG2 . VAL A 1 132 ? 12.604  -19.569 -1.258  1.00 12.39  ? 718  VAL A CG2 1 
ATOM   1087 N N   . GLY A 1 133 ? 12.501  -15.226 0.307   1.00 11.45  ? 719  GLY A N   1 
ATOM   1088 C CA  . GLY A 1 133 ? 12.294  -14.212 1.303   1.00 12.18  ? 719  GLY A CA  1 
ATOM   1089 C C   . GLY A 1 133 ? 10.931  -14.323 1.926   1.00 11.97  ? 719  GLY A C   1 
ATOM   1090 O O   . GLY A 1 133 ? 9.939   -14.676 1.279   1.00 11.54  ? 719  GLY A O   1 
ATOM   1091 N N   . ILE A 1 134 ? 10.900  -14.093 3.250   1.00 11.52  ? 720  ILE A N   1 
ATOM   1092 C CA  . ILE A 1 134 ? 9.718   -14.225 4.083   1.00 12.17  ? 720  ILE A CA  1 
ATOM   1093 C C   . ILE A 1 134 ? 9.486   -12.882 4.765   1.00 12.31  ? 720  ILE A C   1 
ATOM   1094 O O   . ILE A 1 134 ? 10.398  -12.393 5.471   1.00 12.25  ? 720  ILE A O   1 
ATOM   1095 C CB  . ILE A 1 134 ? 9.831   -15.367 5.083   1.00 12.57  ? 720  ILE A CB  1 
ATOM   1096 C CG1 . ILE A 1 134 ? 10.181  -16.692 4.407   1.00 13.69  ? 720  ILE A CG1 1 
ATOM   1097 C CG2 . ILE A 1 134 ? 8.530   -15.468 5.911   1.00 13.67  ? 720  ILE A CG2 1 
ATOM   1098 C CD1 . ILE A 1 134 ? 11.684  -16.990 4.342   1.00 16.84  ? 720  ILE A CD1 1 
ATOM   1099 N N   . PHE A 1 135 ? 8.293   -12.319 4.595   1.00 11.41  ? 721  PHE A N   1 
ATOM   1100 C CA  . PHE A 1 135 ? 7.946   -11.006 5.117   1.00 11.41  ? 721  PHE A CA  1 
ATOM   1101 C C   . PHE A 1 135 ? 6.679   -11.091 5.947   1.00 12.52  ? 721  PHE A C   1 
ATOM   1102 O O   . PHE A 1 135 ? 5.624   -11.353 5.411   1.00 13.13  ? 721  PHE A O   1 
ATOM   1103 C CB  . PHE A 1 135 ? 7.732   -9.991  4.005   1.00 12.60  ? 721  PHE A CB  1 
ATOM   1104 C CG  . PHE A 1 135 ? 7.356   -8.619  4.488   1.00 13.98  ? 721  PHE A CG  1 
ATOM   1105 C CD1 . PHE A 1 135 ? 8.210   -7.808  5.227   1.00 14.60  ? 721  PHE A CD1 1 
ATOM   1106 C CD2 . PHE A 1 135 ? 6.106   -8.117  4.183   1.00 17.08  ? 721  PHE A CD2 1 
ATOM   1107 C CE1 . PHE A 1 135 ? 7.808   -6.556  5.629   1.00 14.61  ? 721  PHE A CE1 1 
ATOM   1108 C CE2 . PHE A 1 135 ? 5.694   -6.876  4.615   1.00 17.50  ? 721  PHE A CE2 1 
ATOM   1109 C CZ  . PHE A 1 135 ? 6.564   -6.088  5.345   1.00 17.23  ? 721  PHE A CZ  1 
ATOM   1110 N N   . VAL A 1 136 ? 6.782   -10.792 7.254   1.00 11.89  ? 722  VAL A N   1 
ATOM   1111 C CA  . VAL A 1 136 ? 5.639   -10.779 8.135   1.00 12.29  ? 722  VAL A CA  1 
ATOM   1112 C C   . VAL A 1 136 ? 5.277   -9.344  8.454   1.00 12.38  ? 722  VAL A C   1 
ATOM   1113 O O   . VAL A 1 136 ? 6.135   -8.577  8.904   1.00 13.38  ? 722  VAL A O   1 
ATOM   1114 C CB  . VAL A 1 136 ? 5.885   -11.565 9.410   1.00 12.44  ? 722  VAL A CB  1 
ATOM   1115 C CG1 . VAL A 1 136 ? 4.675   -11.522 10.334  1.00 14.90  ? 722  VAL A CG1 1 
ATOM   1116 C CG2 . VAL A 1 136 ? 6.309   -13.002 9.124   1.00 12.83  ? 722  VAL A CG2 1 
ATOM   1117 N N   . ASP A 1 137 ? 4.018   -8.986  8.253   1.00 12.76  ? 723  ASP A N   1 
ATOM   1118 C CA  . ASP A 1 137 ? 3.478   -7.722  8.690   1.00 13.23  ? 723  ASP A CA  1 
ATOM   1119 C C   . ASP A 1 137 ? 2.514   -8.051  9.802   1.00 13.46  ? 723  ASP A C   1 
ATOM   1120 O O   . ASP A 1 137 ? 1.368   -8.418  9.553   1.00 13.94  ? 723  ASP A O   1 
ATOM   1121 C CB  . ASP A 1 137 ? 2.854   -6.915  7.562   1.00 15.00  ? 723  ASP A CB  1 
ATOM   1122 C CG  . ASP A 1 137 ? 2.413   -5.528  7.997   1.00 18.90  ? 723  ASP A CG  1 
ATOM   1123 O OD1 . ASP A 1 137 ? 2.114   -5.303  9.198   1.00 18.65  ? 723  ASP A OD1 1 
ATOM   1124 O OD2 . ASP A 1 137 ? 2.350   -4.653  7.098   1.00 23.06  ? 723  ASP A OD2 1 
ATOM   1125 N N   . TYR A 1 138 ? 2.971   -7.916  11.056  1.00 13.83  ? 724  TYR A N   1 
ATOM   1126 C CA  . TYR A 1 138 ? 2.210   -8.477  12.168  1.00 14.91  ? 724  TYR A CA  1 
ATOM   1127 C C   . TYR A 1 138 ? 0.884   -7.779  12.322  1.00 17.17  ? 724  TYR A C   1 
ATOM   1128 O O   . TYR A 1 138 ? -0.154  -8.419  12.469  1.00 17.63  ? 724  TYR A O   1 
ATOM   1129 C CB  . TYR A 1 138 ? 3.032   -8.379  13.469  1.00 15.53  ? 724  TYR A CB  1 
ATOM   1130 C CG  . TYR A 1 138 ? 2.441   -9.172  14.603  1.00 15.11  ? 724  TYR A CG  1 
ATOM   1131 C CD1 . TYR A 1 138 ? 1.411   -8.651  15.336  1.00 17.48  ? 724  TYR A CD1 1 
ATOM   1132 C CD2 . TYR A 1 138 ? 2.873   -10.461 14.859  1.00 15.62  ? 724  TYR A CD2 1 
ATOM   1133 C CE1 . TYR A 1 138 ? 0.812   -9.388  16.334  1.00 18.19  ? 724  TYR A CE1 1 
ATOM   1134 C CE2 . TYR A 1 138 ? 2.304   -11.207 15.880  1.00 16.59  ? 724  TYR A CE2 1 
ATOM   1135 C CZ  . TYR A 1 138 ? 1.248   -10.672 16.572  1.00 17.92  ? 724  TYR A CZ  1 
ATOM   1136 O OH  . TYR A 1 138 ? 0.623   -11.348 17.591  1.00 20.42  ? 724  TYR A OH  1 
ATOM   1137 N N   . ARG A 1 139 ? 0.901   -6.442  12.277  1.00 18.61  ? 725  ARG A N   1 
ATOM   1138 C CA  . ARG A 1 139 ? -0.296  -5.665  12.517  1.00 24.77  ? 725  ARG A CA  1 
ATOM   1139 C C   . ARG A 1 139 ? -1.364  -5.871  11.453  1.00 22.21  ? 725  ARG A C   1 
ATOM   1140 O O   . ARG A 1 139 ? -2.547  -5.894  11.778  1.00 24.77  ? 725  ARG A O   1 
ATOM   1141 C CB  . ARG A 1 139 ? 0.163   -4.199  12.581  1.00 30.17  ? 725  ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 139 ? -0.846  -3.145  12.981  1.00 40.86  ? 725  ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 139 ? -0.276  -1.741  12.687  1.00 50.31  ? 725  ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 139 ? 0.027   -1.530  11.258  1.00 55.99  ? 725  ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 139 ? -0.727  -0.863  10.361  1.00 64.54  ? 725  ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 139 ? -1.911  -0.378  10.702  1.00 65.38  ? 725  ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 139 ? -0.312  -0.699  9.107   1.00 62.93  ? 725  ARG A NH2 1 
ATOM   1148 N N   . VAL A 1 140 ? -0.955  -5.971  10.203  1.00 21.79  ? 726  VAL A N   1 
ATOM   1149 C CA  . VAL A 1 140 ? -1.865  -6.151  9.078   1.00 23.41  ? 726  VAL A CA  1 
ATOM   1150 C C   . VAL A 1 140 ? -2.341  -7.599  8.994   1.00 22.93  ? 726  VAL A C   1 
ATOM   1151 O O   . VAL A 1 140 ? -3.398  -7.860  8.421   1.00 23.08  ? 726  VAL A O   1 
ATOM   1152 C CB  . VAL A 1 140 ? -1.164  -5.729  7.776   1.00 26.35  ? 726  VAL A CB  1 
ATOM   1153 C CG1 . VAL A 1 140 ? -1.883  -6.215  6.522   1.00 33.40  ? 726  VAL A CG1 1 
ATOM   1154 C CG2 . VAL A 1 140 ? -1.035  -4.211  7.802   1.00 28.49  ? 726  VAL A CG2 1 
ATOM   1155 N N   . GLY A 1 141 ? -1.558  -8.517  9.544   1.00 18.59  ? 727  GLY A N   1 
ATOM   1156 C CA  . GLY A 1 141 ? -1.896  -9.922  9.539   1.00 18.22  ? 727  GLY A CA  1 
ATOM   1157 C C   . GLY A 1 141 ? -1.555  -10.601 8.213   1.00 17.93  ? 727  GLY A C   1 
ATOM   1158 O O   . GLY A 1 141 ? -2.339  -11.387 7.706   1.00 19.21  ? 727  GLY A O   1 
ATOM   1159 N N   . SER A 1 142 ? -0.401  -10.291 7.630   1.00 16.04  ? 728  SER A N   1 
ATOM   1160 C CA  . SER A 1 142 ? -0.013  -10.868 6.365   1.00 15.51  ? 728  SER A CA  1 
ATOM   1161 C C   . SER A 1 142 ? 1.382   -11.448 6.484   1.00 13.46  ? 728  SER A C   1 
ATOM   1162 O O   . SER A 1 142 ? 2.247   -10.978 7.241   1.00 13.99  ? 728  SER A O   1 
ATOM   1163 C CB  . SER A 1 142 ? -0.096  -9.936  5.199   1.00 18.48  ? 728  SER A CB  1 
ATOM   1164 O OG  . SER A 1 142 ? 0.839   -8.866  5.327   1.00 20.87  ? 728  SER A OG  1 
ATOM   1165 N N   . ILE A 1 143 ? 1.594   -12.548 5.776   1.00 14.01  ? 729  ILE A N   1 
ATOM   1166 C CA  . ILE A 1 143 ? 2.897   -13.135 5.606   1.00 12.76  ? 729  ILE A CA  1 
ATOM   1167 C C   . ILE A 1 143 ? 3.083   -13.457 4.135   1.00 13.73  ? 729  ILE A C   1 
ATOM   1168 O O   . ILE A 1 143 ? 2.251   -14.139 3.501   1.00 14.25  ? 729  ILE A O   1 
ATOM   1169 C CB  . ILE A 1 143 ? 3.163   -14.348 6.519   1.00 14.21  ? 729  ILE A CB  1 
ATOM   1170 C CG1 . ILE A 1 143 ? 4.513   -14.953 6.193   1.00 13.78  ? 729  ILE A CG1 1 
ATOM   1171 C CG2 . ILE A 1 143 ? 2.046   -15.355 6.526   1.00 15.51  ? 729  ILE A CG2 1 
ATOM   1172 C CD1 . ILE A 1 143 ? 5.068   -16.011 7.122   1.00 16.03  ? 729  ILE A CD1 1 
ATOM   1173 N N   . SER A 1 144 ? 4.141   -12.898 3.572   1.00 12.08  ? 730  SER A N   1 
ATOM   1174 C CA  . SER A 1 144 ? 4.374   -12.960 2.139   1.00 12.73  ? 730  SER A CA  1 
ATOM   1175 C C   . SER A 1 144 ? 5.701   -13.645 1.856   1.00 12.66  ? 730  SER A C   1 
ATOM   1176 O O   . SER A 1 144 ? 6.664   -13.520 2.626   1.00 13.32  ? 730  SER A O   1 
ATOM   1177 C CB  . SER A 1 144 ? 4.408   -11.581 1.527   1.00 14.21  ? 730  SER A CB  1 
ATOM   1178 O OG  . SER A 1 144 ? 3.218   -10.857 1.715   1.00 16.25  ? 730  SER A OG  1 
ATOM   1179 N N   . PHE A 1 145 ? 5.774   -14.327 0.721   1.00 11.91  ? 731  PHE A N   1 
ATOM   1180 C CA  . PHE A 1 145 ? 6.893   -15.114 0.283   1.00 11.53  ? 731  PHE A CA  1 
ATOM   1181 C C   . PHE A 1 145 ? 7.326   -14.611 -1.070  1.00 12.15  ? 731  PHE A C   1 
ATOM   1182 O O   . PHE A 1 145 ? 6.494   -14.356 -1.927  1.00 14.10  ? 731  PHE A O   1 
ATOM   1183 C CB  . PHE A 1 145 ? 6.517   -16.590 0.184   1.00 12.07  ? 731  PHE A CB  1 
ATOM   1184 C CG  . PHE A 1 145 ? 6.207   -17.209 1.524   1.00 12.47  ? 731  PHE A CG  1 
ATOM   1185 C CD1 . PHE A 1 145 ? 4.966   -17.052 2.088   1.00 12.68  ? 731  PHE A CD1 1 
ATOM   1186 C CD2 . PHE A 1 145 ? 7.172   -17.921 2.206   1.00 12.31  ? 731  PHE A CD2 1 
ATOM   1187 C CE1 . PHE A 1 145 ? 4.703   -17.582 3.325   1.00 12.27  ? 731  PHE A CE1 1 
ATOM   1188 C CE2 . PHE A 1 145 ? 6.883   -18.442 3.475   1.00 11.79  ? 731  PHE A CE2 1 
ATOM   1189 C CZ  . PHE A 1 145 ? 5.665   -18.273 3.988   1.00 12.15  ? 731  PHE A CZ  1 
ATOM   1190 N N   . TYR A 1 146 ? 8.643   -14.504 -1.224  1.00 11.80  ? 732  TYR A N   1 
ATOM   1191 C CA  . TYR A 1 146 ? 9.263   -13.962 -2.419  1.00 12.94  ? 732  TYR A CA  1 
ATOM   1192 C C   . TYR A 1 146 ? 10.308  -14.933 -2.943  1.00 13.80  ? 732  TYR A C   1 
ATOM   1193 O O   . TYR A 1 146 ? 11.056  -15.530 -2.178  1.00 13.39  ? 732  TYR A O   1 
ATOM   1194 C CB  . TYR A 1 146 ? 9.970   -12.634 -2.122  1.00 14.10  ? 732  TYR A CB  1 
ATOM   1195 C CG  . TYR A 1 146 ? 9.012   -11.582 -1.629  1.00 13.32  ? 732  TYR A CG  1 
ATOM   1196 C CD1 . TYR A 1 146 ? 8.753   -11.504 -0.268  1.00 13.18  ? 732  TYR A CD1 1 
ATOM   1197 C CD2 . TYR A 1 146 ? 8.346   -10.711 -2.475  1.00 15.99  ? 732  TYR A CD2 1 
ATOM   1198 C CE1 . TYR A 1 146 ? 7.889   -10.538 0.217   1.00 14.17  ? 732  TYR A CE1 1 
ATOM   1199 C CE2 . TYR A 1 146 ? 7.468   -9.743  -1.981  1.00 16.21  ? 732  TYR A CE2 1 
ATOM   1200 C CZ  . TYR A 1 146 ? 7.223   -9.693  -0.635  1.00 16.29  ? 732  TYR A CZ  1 
ATOM   1201 O OH  . TYR A 1 146 ? 6.376   -8.753  -0.118  1.00 18.94  ? 732  TYR A OH  1 
ATOM   1202 N N   . ASN A 1 147 ? 10.395  -14.986 -4.264  1.00 13.77  ? 733  ASN A N   1 
ATOM   1203 C CA  . ASN A 1 147 ? 11.481  -15.605 -4.967  1.00 14.66  ? 733  ASN A CA  1 
ATOM   1204 C C   . ASN A 1 147 ? 12.556  -14.525 -5.138  1.00 15.38  ? 733  ASN A C   1 
ATOM   1205 O O   . ASN A 1 147 ? 12.424  -13.640 -5.980  1.00 15.80  ? 733  ASN A O   1 
ATOM   1206 C CB  . ASN A 1 147 ? 10.932  -16.129 -6.278  1.00 16.92  ? 733  ASN A CB  1 
ATOM   1207 C CG  . ASN A 1 147 ? 11.978  -16.772 -7.130  1.00 17.23  ? 733  ASN A CG  1 
ATOM   1208 O OD1 . ASN A 1 147 ? 13.188  -16.551 -6.968  1.00 16.75  ? 733  ASN A OD1 1 
ATOM   1209 N ND2 . ASN A 1 147 ? 11.543  -17.537 -8.128  1.00 19.76  ? 733  ASN A ND2 1 
ATOM   1210 N N   . VAL A 1 148 ? 13.574  -14.571 -4.285  1.00 14.50  ? 734  VAL A N   1 
ATOM   1211 C CA  . VAL A 1 148 ? 14.579  -13.509 -4.285  1.00 15.52  ? 734  VAL A CA  1 
ATOM   1212 C C   . VAL A 1 148 ? 15.441  -13.579 -5.544  1.00 17.47  ? 734  VAL A C   1 
ATOM   1213 O O   . VAL A 1 148 ? 15.941  -12.529 -6.011  1.00 19.69  ? 734  VAL A O   1 
ATOM   1214 C CB  . VAL A 1 148 ? 15.346  -13.544 -2.945  1.00 15.96  ? 734  VAL A CB  1 
ATOM   1215 C CG1 . VAL A 1 148 ? 16.502  -12.529 -2.968  1.00 17.36  ? 734  VAL A CG1 1 
ATOM   1216 C CG2 . VAL A 1 148 ? 14.450  -13.324 -1.744  1.00 16.35  ? 734  VAL A CG2 1 
ATOM   1217 N N   . THR A 1 149 ? 15.641  -14.793 -6.071  1.00 17.67  ? 735  THR A N   1 
ATOM   1218 C CA  . THR A 1 149 ? 16.400  -14.973 -7.300  1.00 19.17  ? 735  THR A CA  1 
ATOM   1219 C C   . THR A 1 149 ? 15.745  -14.210 -8.458  1.00 20.71  ? 735  THR A C   1 
ATOM   1220 O O   . THR A 1 149 ? 16.417  -13.545 -9.225  1.00 22.91  ? 735  THR A O   1 
ATOM   1221 C CB  . THR A 1 149 ? 16.480  -16.478 -7.610  1.00 20.28  ? 735  THR A CB  1 
ATOM   1222 O OG1 . THR A 1 149 ? 16.949  -17.130 -6.435  1.00 19.37  ? 735  THR A OG1 1 
ATOM   1223 C CG2 . THR A 1 149 ? 17.369  -16.796 -8.782  1.00 23.48  ? 735  THR A CG2 1 
ATOM   1224 N N   . ALA A 1 150 ? 14.435  -14.366 -8.644  1.00 21.10  ? 736  ALA A N   1 
ATOM   1225 C CA  . ALA A 1 150 ? 13.700  -13.710 -9.702  1.00 22.35  ? 736  ALA A CA  1 
ATOM   1226 C C   . ALA A 1 150 ? 13.278  -12.290 -9.301  1.00 22.11  ? 736  ALA A C   1 
ATOM   1227 O O   . ALA A 1 150 ? 12.956  -11.508 -10.179 1.00 24.25  ? 736  ALA A O   1 
ATOM   1228 C CB  . ALA A 1 150 ? 12.464  -14.550 -10.021 1.00 23.04  ? 736  ALA A CB  1 
ATOM   1229 N N   A ARG A 1 151 ? 13.329  -11.989 -7.999  0.50 19.11  ? 737  ARG A N   1 
ATOM   1230 N N   B ARG A 1 151 ? 13.240  -12.011 -7.995  0.50 20.52  ? 737  ARG A N   1 
ATOM   1231 C CA  A ARG A 1 151 ? 12.765  -10.791 -7.383  0.50 18.81  ? 737  ARG A CA  1 
ATOM   1232 C CA  B ARG A 1 151 ? 12.768  -10.750 -7.432  0.50 21.68  ? 737  ARG A CA  1 
ATOM   1233 C C   A ARG A 1 151 ? 11.288  -10.702 -7.729  0.50 19.81  ? 737  ARG A C   1 
ATOM   1234 C C   B ARG A 1 151 ? 11.248  -10.633 -7.521  0.50 21.32  ? 737  ARG A C   1 
ATOM   1235 O O   A ARG A 1 151 ? 10.847  -9.732  -8.353  0.50 20.95  ? 737  ARG A O   1 
ATOM   1236 O O   B ARG A 1 151 ? 10.705  -9.540  -7.688  0.50 23.12  ? 737  ARG A O   1 
ATOM   1237 C CB  A ARG A 1 151 ? 13.464  -9.468  -7.715  0.50 19.30  ? 737  ARG A CB  1 
ATOM   1238 C CB  B ARG A 1 151 ? 13.444  -9.537  -8.076  0.50 24.38  ? 737  ARG A CB  1 
ATOM   1239 C CG  A ARG A 1 151 ? 14.958  -9.485  -7.407  0.50 19.08  ? 737  ARG A CG  1 
ATOM   1240 C CG  B ARG A 1 151 ? 14.921  -9.410  -7.738  0.50 26.55  ? 737  ARG A CG  1 
ATOM   1241 C CD  A ARG A 1 151 ? 15.688  -10.031 -8.586  0.50 19.70  ? 737  ARG A CD  1 
ATOM   1242 C CD  B ARG A 1 151 ? 15.908  -10.194 -8.571  0.50 28.98  ? 737  ARG A CD  1 
ATOM   1243 N NE  A ARG A 1 151 ? 15.388  -9.243  -9.786  0.50 21.09  ? 737  ARG A NE  1 
ATOM   1244 N NE  B ARG A 1 151 ? 17.173  -9.731  -7.990  0.50 31.02  ? 737  ARG A NE  1 
ATOM   1245 C CZ  A ARG A 1 151 ? 15.980  -8.093  -10.155 0.50 22.38  ? 737  ARG A CZ  1 
ATOM   1246 C CZ  B ARG A 1 151 ? 17.409  -8.419  -7.854  0.50 31.66  ? 737  ARG A CZ  1 
ATOM   1247 N NH1 A ARG A 1 151 ? 15.401  -7.416  -11.057 0.50 22.81  ? 737  ARG A NH1 1 
ATOM   1248 N NH1 B ARG A 1 151 ? 17.828  -7.927  -6.695  0.50 27.91  ? 737  ARG A NH1 1 
ATOM   1249 N NH2 A ARG A 1 151 ? 17.092  -7.638  -9.564  0.50 22.66  ? 737  ARG A NH2 1 
ATOM   1250 N NH2 B ARG A 1 151 ? 16.961  -7.583  -8.775  0.50 32.87  ? 737  ARG A NH2 1 
ATOM   1251 N N   . SER A 1 152 ? 10.553  -11.759 -7.371  1.00 19.34  ? 738  SER A N   1 
ATOM   1252 C CA  . SER A 1 152 ? 9.120   -11.851 -7.658  1.00 20.32  ? 738  SER A CA  1 
ATOM   1253 C C   . SER A 1 152 ? 8.379   -12.345 -6.436  1.00 19.28  ? 738  SER A C   1 
ATOM   1254 O O   . SER A 1 152 ? 8.949   -12.994 -5.553  1.00 19.30  ? 738  SER A O   1 
ATOM   1255 C CB  . SER A 1 152 ? 8.811   -12.781 -8.841  1.00 22.64  ? 738  SER A CB  1 
ATOM   1256 O OG  . SER A 1 152 ? 9.314   -14.085 -8.533  1.00 25.10  ? 738  SER A OG  1 
ATOM   1257 N N   . HIS A 1 153 ? 7.113   -11.977 -6.332  1.00 19.61  ? 739  HIS A N   1 
ATOM   1258 C CA  . HIS A 1 153 ? 6.253   -12.419 -5.242  1.00 18.64  ? 739  HIS A CA  1 
ATOM   1259 C C   . HIS A 1 153 ? 5.748   -13.827 -5.583  1.00 20.52  ? 739  HIS A C   1 
ATOM   1260 O O   . HIS A 1 153 ? 5.437   -14.132 -6.737  1.00 21.98  ? 739  HIS A O   1 
ATOM   1261 C CB  . HIS A 1 153 ? 5.077   -11.452 -5.115  1.00 20.94  ? 739  HIS A CB  1 
ATOM   1262 C CG  . HIS A 1 153 ? 3.983   -11.895 -4.206  1.00 21.09  ? 739  HIS A CG  1 
ATOM   1263 N ND1 . HIS A 1 153 ? 2.822   -12.501 -4.682  1.00 23.43  ? 739  HIS A ND1 1 
ATOM   1264 C CD2 . HIS A 1 153 ? 3.905   -11.883 -2.877  1.00 20.36  ? 739  HIS A CD2 1 
ATOM   1265 C CE1 . HIS A 1 153 ? 2.073   -12.791 -3.619  1.00 19.77  ? 739  HIS A CE1 1 
ATOM   1266 N NE2 . HIS A 1 153 ? 2.689   -12.402 -2.516  1.00 20.08  ? 739  HIS A NE2 1 
ATOM   1267 N N   . ILE A 1 154 ? 5.766   -14.738 -4.622  1.00 17.22  ? 740  ILE A N   1 
ATOM   1268 C CA  . ILE A 1 154 ? 5.344   -16.144 -4.759  1.00 18.07  ? 740  ILE A CA  1 
ATOM   1269 C C   . ILE A 1 154 ? 3.908   -16.238 -4.205  1.00 17.52  ? 740  ILE A C   1 
ATOM   1270 O O   . ILE A 1 154 ? 3.048   -16.841 -4.821  1.00 19.05  ? 740  ILE A O   1 
ATOM   1271 C CB  . ILE A 1 154 ? 6.286   -17.104 -3.977  1.00 20.04  ? 740  ILE A CB  1 
ATOM   1272 C CG1 . ILE A 1 154 ? 7.712   -17.188 -4.567  1.00 22.92  ? 740  ILE A CG1 1 
ATOM   1273 C CG2 . ILE A 1 154 ? 5.698   -18.541 -3.863  1.00 22.02  ? 740  ILE A CG2 1 
ATOM   1274 C CD1 . ILE A 1 154 ? 8.640   -18.043 -3.730  1.00 21.79  ? 740  ILE A CD1 1 
ATOM   1275 N N   . TYR A 1 155 ? 3.687   -15.820 -2.946  1.00 15.46  ? 741  TYR A N   1 
ATOM   1276 C CA  . TYR A 1 155 ? 2.425   -16.070 -2.265  1.00 15.44  ? 741  TYR A CA  1 
ATOM   1277 C C   . TYR A 1 155 ? 2.283   -15.196 -1.035  1.00 15.19  ? 741  TYR A C   1 
ATOM   1278 O O   . TYR A 1 155 ? 3.276   -14.991 -0.341  1.00 15.07  ? 741  TYR A O   1 
ATOM   1279 C CB  . TYR A 1 155 ? 2.401   -17.545 -1.811  1.00 16.64  ? 741  TYR A CB  1 
ATOM   1280 C CG  . TYR A 1 155 ? 1.058   -17.994 -1.271  1.00 15.91  ? 741  TYR A CG  1 
ATOM   1281 C CD1 . TYR A 1 155 ? 0.059   -18.308 -2.152  1.00 16.90  ? 741  TYR A CD1 1 
ATOM   1282 C CD2 . TYR A 1 155 ? 0.782   -18.038 0.094   1.00 15.30  ? 741  TYR A CD2 1 
ATOM   1283 C CE1 . TYR A 1 155 ? -1.215  -18.684 -1.740  1.00 18.07  ? 741  TYR A CE1 1 
ATOM   1284 C CE2 . TYR A 1 155 ? -0.471  -18.423 0.523   1.00 16.73  ? 741  TYR A CE2 1 
ATOM   1285 C CZ  . TYR A 1 155 ? -1.460  -18.724 -0.373  1.00 17.81  ? 741  TYR A CZ  1 
ATOM   1286 O OH  . TYR A 1 155 ? -2.743  -19.076 0.002   1.00 21.58  ? 741  TYR A OH  1 
ATOM   1287 N N   . THR A 1 156 ? 1.066   -14.809 -0.725  1.00 14.81  ? 742  THR A N   1 
ATOM   1288 C CA  . THR A 1 156 ? 0.758   -14.129 0.529   1.00 14.83  ? 742  THR A CA  1 
ATOM   1289 C C   . THR A 1 156 ? -0.409  -14.847 1.187   1.00 15.31  ? 742  THR A C   1 
ATOM   1290 O O   . THR A 1 156 ? -1.441  -15.079 0.555   1.00 16.99  ? 742  THR A O   1 
ATOM   1291 C CB  . THR A 1 156 ? 0.384   -12.661 0.276   1.00 17.60  ? 742  THR A CB  1 
ATOM   1292 O OG1 . THR A 1 156 ? 1.608   -12.034 -0.080  1.00 17.81  ? 742  THR A OG1 1 
ATOM   1293 C CG2 . THR A 1 156 ? -0.150  -11.984 1.519   1.00 17.92  ? 742  THR A CG2 1 
ATOM   1294 N N   . PHE A 1 157 ? -0.246  -15.088 2.479   1.00 14.63  ? 743  PHE A N   1 
ATOM   1295 C CA  . PHE A 1 157 ? -1.367  -15.380 3.335   1.00 15.21  ? 743  PHE A CA  1 
ATOM   1296 C C   . PHE A 1 157 ? -1.855  -14.087 3.955   1.00 16.89  ? 743  PHE A C   1 
ATOM   1297 O O   . PHE A 1 157 ? -1.069  -13.414 4.622   1.00 16.38  ? 743  PHE A O   1 
ATOM   1298 C CB  . PHE A 1 157 ? -0.976  -16.294 4.481   1.00 14.19  ? 743  PHE A CB  1 
ATOM   1299 C CG  . PHE A 1 157 ? -0.501  -17.688 4.162   1.00 13.92  ? 743  PHE A CG  1 
ATOM   1300 C CD1 . PHE A 1 157 ? 0.811   -17.921 3.850   1.00 13.96  ? 743  PHE A CD1 1 
ATOM   1301 C CD2 . PHE A 1 157 ? -1.384  -18.760 4.176   1.00 15.88  ? 743  PHE A CD2 1 
ATOM   1302 C CE1 . PHE A 1 157 ? 1.284   -19.206 3.608   1.00 15.03  ? 743  PHE A CE1 1 
ATOM   1303 C CE2 . PHE A 1 157 ? -0.886  -20.042 3.956   1.00 15.90  ? 743  PHE A CE2 1 
ATOM   1304 C CZ  . PHE A 1 157 ? 0.406   -20.252 3.655   1.00 15.73  ? 743  PHE A CZ  1 
ATOM   1305 N N   . ALA A 1 158 ? -3.093  -13.719 3.733   1.00 19.47  ? 744  ALA A N   1 
ATOM   1306 C CA  . ALA A 1 158 ? -3.637  -12.470 4.264   1.00 20.86  ? 744  ALA A CA  1 
ATOM   1307 C C   . ALA A 1 158 ? -4.729  -12.785 5.277   1.00 23.05  ? 744  ALA A C   1 
ATOM   1308 O O   . ALA A 1 158 ? -5.271  -13.885 5.310   1.00 23.97  ? 744  ALA A O   1 
ATOM   1309 C CB  . ALA A 1 158 ? -4.173  -11.614 3.130   1.00 24.55  ? 744  ALA A CB  1 
ATOM   1310 N N   . SER A 1 159 ? -5.114  -11.764 6.029   1.00 23.75  ? 745  SER A N   1 
ATOM   1311 C CA  . SER A 1 159 ? -6.123  -11.884 7.064   1.00 27.21  ? 745  SER A CA  1 
ATOM   1312 C C   . SER A 1 159 ? -5.762  -13.017 8.016   1.00 25.92  ? 745  SER A C   1 
ATOM   1313 O O   . SER A 1 159 ? -6.648  -13.766 8.432   1.00 27.64  ? 745  SER A O   1 
ATOM   1314 C CB  . SER A 1 159 ? -7.524  -12.095 6.482   1.00 32.58  ? 745  SER A CB  1 
ATOM   1315 O OG  . SER A 1 159 ? -7.837  -11.100 5.517   1.00 37.32  ? 745  SER A OG  1 
ATOM   1316 N N   . CYS A 1 160 ? -4.507  -13.099 8.424   1.00 22.36  ? 746  CYS A N   1 
ATOM   1317 C CA  . CYS A 1 160 ? -4.067  -14.170 9.302   1.00 22.39  ? 746  CYS A CA  1 
ATOM   1318 C C   . CYS A 1 160 ? -4.491  -13.940 10.750  1.00 25.29  ? 746  CYS A C   1 
ATOM   1319 O O   . CYS A 1 160 ? -4.420  -14.876 11.528  1.00 28.22  ? 746  CYS A O   1 
ATOM   1320 C CB  . CYS A 1 160 ? -2.547  -14.304 9.297   1.00 20.22  ? 746  CYS A CB  1 
ATOM   1321 S SG  . CYS A 1 160 ? -1.896  -14.767 7.668   1.00 20.53  ? 746  CYS A SG  1 
ATOM   1322 N N   . SER A 1 161 ? -4.847  -12.699 11.108  1.00 25.77  ? 747  SER A N   1 
ATOM   1323 C CA  . SER A 1 161 ? -5.293  -12.370 12.463  1.00 30.77  ? 747  SER A CA  1 
ATOM   1324 C C   . SER A 1 161 ? -4.324  -12.927 13.503  1.00 27.86  ? 747  SER A C   1 
ATOM   1325 O O   . SER A 1 161 ? -4.730  -13.599 14.419  1.00 31.35  ? 747  SER A O   1 
ATOM   1326 C CB  . SER A 1 161 ? -6.694  -12.877 12.748  1.00 38.37  ? 747  SER A CB  1 
ATOM   1327 O OG  . SER A 1 161 ? -7.592  -12.375 11.773  1.00 45.80  ? 747  SER A OG  1 
ATOM   1328 N N   . PHE A 1 162 ? -3.037  -12.614 13.371  1.00 23.52  ? 748  PHE A N   1 
ATOM   1329 C CA  . PHE A 1 162 ? -2.025  -13.100 14.277  1.00 22.37  ? 748  PHE A CA  1 
ATOM   1330 C C   . PHE A 1 162 ? -2.274  -12.610 15.691  1.00 23.74  ? 748  PHE A C   1 
ATOM   1331 O O   . PHE A 1 162 ? -2.537  -11.431 15.946  1.00 25.79  ? 748  PHE A O   1 
ATOM   1332 C CB  . PHE A 1 162 ? -0.657  -12.519 13.885  1.00 19.63  ? 748  PHE A CB  1 
ATOM   1333 C CG  . PHE A 1 162 ? -0.142  -12.901 12.521  1.00 18.75  ? 748  PHE A CG  1 
ATOM   1334 C CD1 . PHE A 1 162 ? -0.154  -14.222 12.107  1.00 17.93  ? 748  PHE A CD1 1 
ATOM   1335 C CD2 . PHE A 1 162 ? 0.369   -11.943 11.640  1.00 17.33  ? 748  PHE A CD2 1 
ATOM   1336 C CE1 . PHE A 1 162 ? 0.354   -14.587 10.908  1.00 17.97  ? 748  PHE A CE1 1 
ATOM   1337 C CE2 . PHE A 1 162 ? 0.821   -12.293 10.404  1.00 16.75  ? 748  PHE A CE2 1 
ATOM   1338 C CZ  . PHE A 1 162 ? 0.857   -13.631 10.053  1.00 18.05  ? 748  PHE A CZ  1 
ATOM   1339 N N   . SER A 1 163 ? -2.106  -13.523 16.658  1.00 22.65  ? 749  SER A N   1 
ATOM   1340 C CA  . SER A 1 163 ? -2.149  -13.146 18.065  1.00 22.48  ? 749  SER A CA  1 
ATOM   1341 C C   . SER A 1 163 ? -1.074  -13.994 18.750  1.00 20.52  ? 749  SER A C   1 
ATOM   1342 O O   . SER A 1 163 ? -0.865  -15.163 18.434  1.00 19.56  ? 749  SER A O   1 
ATOM   1343 C CB  . SER A 1 163 ? -3.513  -13.297 18.666  1.00 27.09  ? 749  SER A CB  1 
ATOM   1344 O OG  . SER A 1 163 ? -3.959  -14.621 18.464  1.00 30.24  ? 749  SER A OG  1 
ATOM   1345 N N   . GLY A 1 164 ? -0.347  -13.351 19.656  1.00 19.99  ? 750  GLY A N   1 
ATOM   1346 C CA  . GLY A 1 164 ? 0.774   -13.944 20.340  1.00 19.17  ? 750  GLY A CA  1 
ATOM   1347 C C   . GLY A 1 164 ? 1.992   -14.054 19.449  1.00 18.24  ? 750  GLY A C   1 
ATOM   1348 O O   . GLY A 1 164 ? 2.002   -13.601 18.307  1.00 17.54  ? 750  GLY A O   1 
ATOM   1349 N N   . PRO A 1 165 ? 3.079   -14.605 19.968  1.00 17.61  ? 751  PRO A N   1 
ATOM   1350 C CA  . PRO A 1 165 ? 4.334   -14.572 19.247  1.00 17.18  ? 751  PRO A CA  1 
ATOM   1351 C C   . PRO A 1 165 ? 4.388   -15.534 18.067  1.00 15.97  ? 751  PRO A C   1 
ATOM   1352 O O   . PRO A 1 165 ? 3.844   -16.645 18.131  1.00 16.37  ? 751  PRO A O   1 
ATOM   1353 C CB  . PRO A 1 165 ? 5.330   -14.906 20.331  1.00 19.00  ? 751  PRO A CB  1 
ATOM   1354 C CG  . PRO A 1 165 ? 4.688   -14.869 21.608  1.00 22.38  ? 751  PRO A CG  1 
ATOM   1355 C CD  . PRO A 1 165 ? 3.230   -15.066 21.345  1.00 20.42  ? 751  PRO A CD  1 
ATOM   1356 N N   . LEU A 1 166 ? 5.148   -15.096 17.083  1.00 13.95  ? 752  LEU A N   1 
ATOM   1357 C CA  . LEU A 1 166 ? 5.435   -15.867 15.892  1.00 14.11  ? 752  LEU A CA  1 
ATOM   1358 C C   . LEU A 1 166 ? 6.936   -16.096 15.843  1.00 14.52  ? 752  LEU A C   1 
ATOM   1359 O O   . LEU A 1 166 ? 7.707   -15.284 16.372  1.00 14.72  ? 752  LEU A O   1 
ATOM   1360 C CB  . LEU A 1 166 ? 5.018   -15.189 14.593  1.00 14.13  ? 752  LEU A CB  1 
ATOM   1361 C CG  . LEU A 1 166 ? 3.582   -14.688 14.535  1.00 17.32  ? 752  LEU A CG  1 
ATOM   1362 C CD1 . LEU A 1 166 ? 3.403   -14.049 13.214  1.00 17.77  ? 752  LEU A CD1 1 
ATOM   1363 C CD2 . LEU A 1 166 ? 2.586   -15.819 14.694  1.00 20.70  ? 752  LEU A CD2 1 
ATOM   1364 N N   . GLN A 1 167 ? 7.350   -17.184 15.188  1.00 13.78  ? 753  GLN A N   1 
ATOM   1365 C CA  . GLN A 1 167 ? 8.791   -17.388 15.008  1.00 13.01  ? 753  GLN A CA  1 
ATOM   1366 C C   . GLN A 1 167 ? 9.025   -18.014 13.645  1.00 12.96  ? 753  GLN A C   1 
ATOM   1367 O O   . GLN A 1 167 ? 8.149   -18.693 13.099  1.00 13.08  ? 753  GLN A O   1 
ATOM   1368 C CB  . GLN A 1 167 ? 9.460   -18.226 16.062  1.00 15.50  ? 753  GLN A CB  1 
ATOM   1369 C CG  . GLN A 1 167 ? 9.004   -19.671 16.108  1.00 15.79  ? 753  GLN A CG  1 
ATOM   1370 C CD  . GLN A 1 167 ? 9.440   -20.373 17.351  1.00 18.61  ? 753  GLN A CD  1 
ATOM   1371 O OE1 . GLN A 1 167 ? 8.626   -21.037 18.007  1.00 23.02  ? 753  GLN A OE1 1 
ATOM   1372 N NE2 . GLN A 1 167 ? 10.706  -20.252 17.714  1.00 19.70  ? 753  GLN A NE2 1 
ATOM   1373 N N   . PRO A 1 168 ? 10.212  -17.859 13.072  1.00 11.84  ? 754  PRO A N   1 
ATOM   1374 C CA  . PRO A 1 168 ? 10.557  -18.545 11.830  1.00 11.51  ? 754  PRO A CA  1 
ATOM   1375 C C   . PRO A 1 168 ? 10.580  -20.066 12.025  1.00 12.68  ? 754  PRO A C   1 
ATOM   1376 O O   . PRO A 1 168 ? 10.881  -20.568 13.085  1.00 12.56  ? 754  PRO A O   1 
ATOM   1377 C CB  . PRO A 1 168 ? 11.952  -18.049 11.517  1.00 11.88  ? 754  PRO A CB  1 
ATOM   1378 C CG  . PRO A 1 168 ? 12.036  -16.710 12.240  1.00 11.87  ? 754  PRO A CG  1 
ATOM   1379 C CD  . PRO A 1 168 ? 11.293  -16.952 13.524  1.00 12.51  ? 754  PRO A CD  1 
ATOM   1380 N N   . ILE A 1 169 ? 10.254  -20.797 10.963  1.00 11.85  ? 755  ILE A N   1 
ATOM   1381 C CA  . ILE A 1 169 ? 10.285  -22.250 10.960  1.00 12.71  ? 755  ILE A CA  1 
ATOM   1382 C C   . ILE A 1 169 ? 10.923  -22.723 9.654   1.00 12.24  ? 755  ILE A C   1 
ATOM   1383 O O   . ILE A 1 169 ? 10.813  -22.066 8.634   1.00 12.09  ? 755  ILE A O   1 
ATOM   1384 C CB  . ILE A 1 169 ? 8.877   -22.855 11.162  1.00 13.61  ? 755  ILE A CB  1 
ATOM   1385 C CG1 . ILE A 1 169 ? 8.906   -24.372 11.312  1.00 16.43  ? 755  ILE A CG1 1 
ATOM   1386 C CG2 . ILE A 1 169 ? 7.963   -22.447 10.049  1.00 14.14  ? 755  ILE A CG2 1 
ATOM   1387 C CD1 . ILE A 1 169 ? 7.553   -24.955 11.717  1.00 18.97  ? 755  ILE A CD1 1 
ATOM   1388 N N   . PHE A 1 170 ? 11.635  -23.852 9.753   1.00 12.86  ? 756  PHE A N   1 
ATOM   1389 C CA  . PHE A 1 170 ? 12.391  -24.386 8.639   1.00 13.08  ? 756  PHE A CA  1 
ATOM   1390 C C   . PHE A 1 170 ? 12.317  -25.907 8.637   1.00 14.43  ? 756  PHE A C   1 
ATOM   1391 O O   . PHE A 1 170 ? 12.344  -26.563 9.655   1.00 15.62  ? 756  PHE A O   1 
ATOM   1392 C CB  . PHE A 1 170 ? 13.872  -24.050 8.820   1.00 13.72  ? 756  PHE A CB  1 
ATOM   1393 C CG  . PHE A 1 170 ? 14.165  -22.593 9.117   1.00 13.35  ? 756  PHE A CG  1 
ATOM   1394 C CD1 . PHE A 1 170 ? 14.066  -22.143 10.429  1.00 14.68  ? 756  PHE A CD1 1 
ATOM   1395 C CD2 . PHE A 1 170 ? 14.602  -21.713 8.140   1.00 13.81  ? 756  PHE A CD2 1 
ATOM   1396 C CE1 . PHE A 1 170 ? 14.315  -20.793 10.695  1.00 14.05  ? 756  PHE A CE1 1 
ATOM   1397 C CE2 . PHE A 1 170 ? 14.858  -20.391 8.445   1.00 14.36  ? 756  PHE A CE2 1 
ATOM   1398 C CZ  . PHE A 1 170 ? 14.693  -19.954 9.724   1.00 13.30  ? 756  PHE A CZ  1 
ATOM   1399 N N   . SER A 1 171 ? 12.424  -26.471 7.433   1.00 13.80  ? 757  SER A N   1 
ATOM   1400 C CA  . SER A 1 171 ? 12.772  -27.879 7.305   1.00 15.00  ? 757  SER A CA  1 
ATOM   1401 C C   . SER A 1 171 ? 13.688  -28.061 6.111   1.00 14.34  ? 757  SER A C   1 
ATOM   1402 O O   . SER A 1 171 ? 13.324  -27.633 5.034   1.00 14.50  ? 757  SER A O   1 
ATOM   1403 C CB  . SER A 1 171 ? 11.586  -28.815 7.120   1.00 16.29  ? 757  SER A CB  1 
ATOM   1404 O OG  . SER A 1 171 ? 12.060  -30.158 6.910   1.00 18.58  ? 757  SER A OG  1 
ATOM   1405 N N   . PRO A 1 172 ? 14.856  -28.726 6.262   1.00 15.35  ? 758  PRO A N   1 
ATOM   1406 C CA  . PRO A 1 172 ? 15.675  -29.017 5.086   1.00 16.99  ? 758  PRO A CA  1 
ATOM   1407 C C   . PRO A 1 172 ? 15.202  -30.198 4.244   1.00 17.09  ? 758  PRO A C   1 
ATOM   1408 O O   . PRO A 1 172 ? 15.830  -30.584 3.255   1.00 18.39  ? 758  PRO A O   1 
ATOM   1409 C CB  . PRO A 1 172 ? 17.061  -29.274 5.687   1.00 17.51  ? 758  PRO A CB  1 
ATOM   1410 C CG  . PRO A 1 172 ? 16.732  -29.852 7.032   1.00 17.85  ? 758  PRO A CG  1 
ATOM   1411 C CD  . PRO A 1 172 ? 15.466  -29.177 7.531   1.00 16.04  ? 758  PRO A CD  1 
ATOM   1412 N N   . GLY A 1 173 ? 14.069  -30.795 4.614   1.00 18.44  ? 759  GLY A N   1 
ATOM   1413 C CA  . GLY A 1 173 ? 13.537  -31.934 3.881   1.00 19.87  ? 759  GLY A CA  1 
ATOM   1414 C C   . GLY A 1 173 ? 14.298  -33.238 4.120   1.00 23.90  ? 759  GLY A C   1 
ATOM   1415 O O   . GLY A 1 173 ? 15.298  -33.287 4.834   1.00 22.42  ? 759  GLY A O   1 
ATOM   1416 N N   . THR A 1 174 ? 13.837  -34.321 3.478   1.00 29.20  ? 760  THR A N   1 
ATOM   1417 C CA  . THR A 1 174 ? 14.557  -35.585 3.585   1.00 32.12  ? 760  THR A CA  1 
ATOM   1418 C C   . THR A 1 174 ? 15.694  -35.628 2.560   1.00 32.59  ? 760  THR A C   1 
ATOM   1419 O O   . THR A 1 174 ? 15.817  -34.764 1.717   1.00 30.09  ? 760  THR A O   1 
ATOM   1420 C CB  . THR A 1 174 ? 13.643  -36.806 3.504   1.00 38.83  ? 760  THR A CB  1 
ATOM   1421 O OG1 . THR A 1 174 ? 13.259  -36.812 2.143   1.00 40.58  ? 760  THR A OG1 1 
ATOM   1422 C CG2 . THR A 1 174 ? 12.400  -36.651 4.361   1.00 39.97  ? 760  THR A CG2 1 
ATOM   1423 N N   . ARG A 1 175 ? 16.586  -36.624 2.664   1.00 33.56  ? 761  ARG A N   1 
ATOM   1424 C CA  . ARG A 1 175 ? 17.859  -36.570 1.952   1.00 35.32  ? 761  ARG A CA  1 
ATOM   1425 C C   . ARG A 1 175 ? 17.711  -36.865 0.449   1.00 34.21  ? 761  ARG A C   1 
ATOM   1426 O O   . ARG A 1 175 ? 18.637  -36.532 -0.292  1.00 30.85  ? 761  ARG A O   1 
ATOM   1427 C CB  . ARG A 1 175 ? 18.881  -37.523 2.602   1.00 38.75  ? 761  ARG A CB  1 
ATOM   1428 C CG  . ARG A 1 175 ? 19.375  -37.030 3.966   1.00 41.29  ? 761  ARG A CG  1 
ATOM   1429 C CD  . ARG A 1 175 ? 20.301  -37.995 4.764   1.00 46.45  ? 761  ARG A CD  1 
ATOM   1430 N NE  . ARG A 1 175 ? 21.548  -38.345 4.063   1.00 47.46  ? 761  ARG A NE  1 
ATOM   1431 C CZ  . ARG A 1 175 ? 22.754  -37.778 4.261   1.00 50.38  ? 761  ARG A CZ  1 
ATOM   1432 N NH1 . ARG A 1 175 ? 22.949  -36.844 5.185   1.00 47.90  ? 761  ARG A NH1 1 
ATOM   1433 N NH2 . ARG A 1 175 ? 23.790  -38.159 3.536   1.00 51.39  ? 761  ARG A NH2 1 
ATOM   1434 N N   . ASP A 1 176 ? 16.592  -37.504 0.041   1.00 33.20  ? 762  ASP A N   1 
ATOM   1435 C CA  . ASP A 1 176 ? 16.178  -37.731 -1.342  1.00 33.87  ? 762  ASP A CA  1 
ATOM   1436 C C   . ASP A 1 176 ? 17.272  -38.459 -2.132  1.00 35.51  ? 762  ASP A C   1 
ATOM   1437 O O   . ASP A 1 176 ? 17.733  -37.976 -3.171  1.00 35.03  ? 762  ASP A O   1 
ATOM   1438 C CB  . ASP A 1 176 ? 15.690  -36.478 -2.039  1.00 33.10  ? 762  ASP A CB  1 
ATOM   1439 C CG  . ASP A 1 176 ? 15.090  -36.652 -3.435  1.00 35.04  ? 762  ASP A CG  1 
ATOM   1440 O OD1 . ASP A 1 176 ? 14.587  -37.772 -3.761  1.00 38.03  ? 762  ASP A OD1 1 
ATOM   1441 O OD2 . ASP A 1 176 ? 15.171  -35.654 -4.217  1.00 32.54  ? 762  ASP A OD2 1 
ATOM   1442 N N   . GLY A 1 177 ? 17.684  -39.591 -1.570  1.00 37.41  ? 763  GLY A N   1 
ATOM   1443 C CA  . GLY A 1 177 ? 18.698  -40.467 -2.117  1.00 39.99  ? 763  GLY A CA  1 
ATOM   1444 C C   . GLY A 1 177 ? 20.021  -39.764 -2.405  1.00 39.27  ? 763  GLY A C   1 
ATOM   1445 O O   . GLY A 1 177 ? 20.771  -40.237 -3.247  1.00 47.72  ? 763  GLY A O   1 
ATOM   1446 N N   . GLY A 1 178 ? 20.326  -38.676 -1.702  1.00 37.79  ? 764  GLY A N   1 
ATOM   1447 C CA  . GLY A 1 178 ? 21.537  -37.915 -1.967  1.00 35.12  ? 764  GLY A CA  1 
ATOM   1448 C C   . GLY A 1 178 ? 21.336  -36.644 -2.793  1.00 31.96  ? 764  GLY A C   1 
ATOM   1449 O O   . GLY A 1 178 ? 22.234  -35.819 -2.886  1.00 32.63  ? 764  GLY A O   1 
ATOM   1450 N N   . LYS A 1 179 ? 20.117  -36.360 -3.265  1.00 28.97  ? 765  LYS A N   1 
ATOM   1451 C CA  . LYS A 1 179 ? 19.893  -35.161 -4.063  1.00 28.80  ? 765  LYS A CA  1 
ATOM   1452 C C   . LYS A 1 179 ? 19.546  -33.949 -3.202  1.00 25.27  ? 765  LYS A C   1 
ATOM   1453 O O   . LYS A 1 179 ? 19.571  -32.799 -3.673  1.00 26.60  ? 765  LYS A O   1 
ATOM   1454 C CB  . LYS A 1 179 ? 18.778  -35.425 -5.090  1.00 31.57  ? 765  LYS A CB  1 
ATOM   1455 C CG  . LYS A 1 179 ? 19.121  -36.484 -6.103  1.00 37.39  ? 765  LYS A CG  1 
ATOM   1456 C CD  . LYS A 1 179 ? 17.956  -36.979 -6.952  1.00 44.29  ? 765  LYS A CD  1 
ATOM   1457 C CE  . LYS A 1 179 ? 18.427  -38.066 -7.854  1.00 53.26  ? 765  LYS A CE  1 
ATOM   1458 N NZ  . LYS A 1 179 ? 17.388  -38.891 -8.486  1.00 62.20  ? 765  LYS A NZ  1 
ATOM   1459 N N   . ASN A 1 180 ? 19.235  -34.173 -1.907  1.00 23.33  ? 766  ASN A N   1 
ATOM   1460 C CA  . ASN A 1 180 ? 18.686  -33.118 -1.064  1.00 20.90  ? 766  ASN A CA  1 
ATOM   1461 C C   . ASN A 1 180 ? 19.452  -32.945 0.240   1.00 20.53  ? 766  ASN A C   1 
ATOM   1462 O O   . ASN A 1 180 ? 18.892  -32.439 1.200   1.00 19.93  ? 766  ASN A O   1 
ATOM   1463 C CB  . ASN A 1 180 ? 17.197  -33.321 -0.759  1.00 20.75  ? 766  ASN A CB  1 
ATOM   1464 C CG  . ASN A 1 180 ? 16.541  -32.067 -0.252  1.00 18.84  ? 766  ASN A CG  1 
ATOM   1465 O OD1 . ASN A 1 180 ? 16.827  -30.966 -0.734  1.00 18.44  ? 766  ASN A OD1 1 
ATOM   1466 N ND2 . ASN A 1 180 ? 15.650  -32.200 0.717   1.00 19.39  ? 766  ASN A ND2 1 
ATOM   1467 N N   . THR A 1 181 ? 20.758  -33.262 0.259   1.00 21.71  ? 767  THR A N   1 
ATOM   1468 C CA  . THR A 1 181 ? 21.524  -33.143 1.485   1.00 21.53  ? 767  THR A CA  1 
ATOM   1469 C C   . THR A 1 181 ? 21.990  -31.723 1.774   1.00 19.77  ? 767  THR A C   1 
ATOM   1470 O O   . THR A 1 181 ? 22.467  -31.505 2.881   1.00 21.34  ? 767  THR A O   1 
ATOM   1471 C CB  . THR A 1 181 ? 22.722  -34.088 1.449   1.00 23.82  ? 767  THR A CB  1 
ATOM   1472 O OG1 . THR A 1 181 ? 23.537  -33.716 0.342   1.00 25.34  ? 767  THR A OG1 1 
ATOM   1473 C CG2 . THR A 1 181 ? 22.302  -35.539 1.259   1.00 25.74  ? 767  THR A CG2 1 
ATOM   1474 N N   . ALA A 1 182 ? 21.927  -30.790 0.835   1.00 18.27  ? 768  ALA A N   1 
ATOM   1475 C CA  . ALA A 1 182 ? 22.411  -29.441 1.109   1.00 18.04  ? 768  ALA A CA  1 
ATOM   1476 C C   . ALA A 1 182 ? 21.608  -28.830 2.263   1.00 16.93  ? 768  ALA A C   1 
ATOM   1477 O O   . ALA A 1 182 ? 20.412  -29.148 2.457   1.00 16.23  ? 768  ALA A O   1 
ATOM   1478 C CB  . ALA A 1 182 ? 22.369  -28.590 -0.142  1.00 17.94  ? 768  ALA A CB  1 
ATOM   1479 N N   . PRO A 1 183 ? 22.206  -27.898 3.008   1.00 16.47  ? 769  PRO A N   1 
ATOM   1480 C CA  . PRO A 1 183 ? 21.482  -27.212 4.067   1.00 15.82  ? 769  PRO A CA  1 
ATOM   1481 C C   . PRO A 1 183 ? 20.580  -26.107 3.541   1.00 15.29  ? 769  PRO A C   1 
ATOM   1482 O O   . PRO A 1 183 ? 20.681  -25.656 2.392   1.00 15.24  ? 769  PRO A O   1 
ATOM   1483 C CB  . PRO A 1 183 ? 22.593  -26.502 4.855   1.00 16.37  ? 769  PRO A CB  1 
ATOM   1484 C CG  . PRO A 1 183 ? 23.650  -26.260 3.782   1.00 17.13  ? 769  PRO A CG  1 
ATOM   1485 C CD  . PRO A 1 183 ? 23.600  -27.442 2.889   1.00 17.23  ? 769  PRO A CD  1 
ATOM   1486 N N   . LEU A 1 184 ? 19.657  -25.648 4.391   1.00 14.03  ? 770  LEU A N   1 
ATOM   1487 C CA  . LEU A 1 184 ? 19.092  -24.308 4.314   1.00 13.73  ? 770  LEU A CA  1 
ATOM   1488 C C   . LEU A 1 184 ? 20.046  -23.374 5.004   1.00 13.72  ? 770  LEU A C   1 
ATOM   1489 O O   . LEU A 1 184 ? 20.562  -23.739 6.065   1.00 15.56  ? 770  LEU A O   1 
ATOM   1490 C CB  . LEU A 1 184 ? 17.755  -24.247 5.034   1.00 13.57  ? 770  LEU A CB  1 
ATOM   1491 C CG  . LEU A 1 184 ? 16.664  -25.128 4.450   1.00 14.03  ? 770  LEU A CG  1 
ATOM   1492 C CD1 . LEU A 1 184 ? 15.457  -25.129 5.380   1.00 14.49  ? 770  LEU A CD1 1 
ATOM   1493 C CD2 . LEU A 1 184 ? 16.262  -24.713 3.068   1.00 14.79  ? 770  LEU A CD2 1 
ATOM   1494 N N   . THR A 1 185 ? 20.260  -22.195 4.462   1.00 13.00  ? 771  THR A N   1 
ATOM   1495 C CA  . THR A 1 185 ? 21.166  -21.236 5.055   1.00 13.14  ? 771  THR A CA  1 
ATOM   1496 C C   . THR A 1 185 ? 20.490  -19.879 5.103   1.00 12.87  ? 771  THR A C   1 
ATOM   1497 O O   . THR A 1 185 ? 20.156  -19.290 4.084   1.00 13.45  ? 771  THR A O   1 
ATOM   1498 C CB  . THR A 1 185 ? 22.467  -21.169 4.267   1.00 14.23  ? 771  THR A CB  1 
ATOM   1499 O OG1 . THR A 1 185 ? 23.139  -22.438 4.336   1.00 15.97  ? 771  THR A OG1 1 
ATOM   1500 C CG2 . THR A 1 185 ? 23.404  -20.131 4.828   1.00 15.36  ? 771  THR A CG2 1 
ATOM   1501 N N   . ILE A 1 186 ? 20.301  -19.349 6.315   1.00 12.77  ? 772  ILE A N   1 
ATOM   1502 C CA  . ILE A 1 186 ? 19.801  -17.999 6.484   1.00 12.66  ? 772  ILE A CA  1 
ATOM   1503 C C   . ILE A 1 186 ? 20.896  -17.033 6.018   1.00 13.93  ? 772  ILE A C   1 
ATOM   1504 O O   . ILE A 1 186 ? 22.038  -17.125 6.436   1.00 15.18  ? 772  ILE A O   1 
ATOM   1505 C CB  . ILE A 1 186 ? 19.482  -17.765 7.971   1.00 13.11  ? 772  ILE A CB  1 
ATOM   1506 C CG1 . ILE A 1 186 ? 18.408  -18.639 8.423   1.00 12.80  ? 772  ILE A CG1 1 
ATOM   1507 C CG2 . ILE A 1 186 ? 19.171  -16.283 8.194   1.00 13.72  ? 772  ILE A CG2 1 
ATOM   1508 C CD1 . ILE A 1 186 ? 18.444  -18.933 9.898   1.00 13.04  ? 772  ILE A CD1 1 
ATOM   1509 N N   . CYS A 1 187 ? 20.534  -16.047 5.182   1.00 15.13  ? 773  CYS A N   1 
ATOM   1510 C CA  A CYS A 1 187 ? 21.534  -15.188 4.580   0.64 18.56  ? 773  CYS A CA  1 
ATOM   1511 C CA  B CYS A 1 187 ? 21.547  -15.192 4.591   0.36 18.13  ? 773  CYS A CA  1 
ATOM   1512 C C   . CYS A 1 187 ? 21.180  -13.731 4.784   1.00 19.71  ? 773  CYS A C   1 
ATOM   1513 O O   . CYS A 1 187 ? 20.010  -13.357 4.683   1.00 21.14  ? 773  CYS A O   1 
ATOM   1514 C CB  A CYS A 1 187 ? 21.733  -15.511 3.102   0.64 21.80  ? 773  CYS A CB  1 
ATOM   1515 C CB  B CYS A 1 187 ? 21.772  -15.473 3.106   0.36 19.76  ? 773  CYS A CB  1 
ATOM   1516 S SG  A CYS A 1 187 ? 20.195  -15.478 2.131   0.64 22.67  ? 773  CYS A SG  1 
ATOM   1517 S SG  B CYS A 1 187 ? 22.488  -17.093 2.708   0.36 20.67  ? 773  CYS A SG  1 
ATOM   1518 N N   . PRO A 1 188 ? 22.195  -12.852 4.878   1.00 21.82  ? 774  PRO A N   1 
ATOM   1519 C CA  . PRO A 1 188 ? 21.917  -11.410 4.954   1.00 23.79  ? 774  PRO A CA  1 
ATOM   1520 C C   . PRO A 1 188 ? 21.341  -10.917 3.623   1.00 25.99  ? 774  PRO A C   1 
ATOM   1521 O O   . PRO A 1 188 ? 21.687  -11.446 2.579   1.00 27.66  ? 774  PRO A O   1 
ATOM   1522 C CB  . PRO A 1 188 ? 23.309  -10.851 5.258   1.00 27.92  ? 774  PRO A CB  1 
ATOM   1523 C CG  . PRO A 1 188 ? 24.309  -11.878 4.771   1.00 28.19  ? 774  PRO A CG  1 
ATOM   1524 C CD  . PRO A 1 188 ? 23.608  -13.223 4.782   1.00 25.06  ? 774  PRO A CD  1 
ATOM   1525 N N   . VAL A 1 189 ? 20.446  -9.903  3.630   1.00 28.30  ? 775  VAL A N   1 
ATOM   1526 C CA  . VAL A 1 189 ? 20.039  -9.253  2.385   1.00 33.24  ? 775  VAL A CA  1 
ATOM   1527 C C   . VAL A 1 189 ? 21.276  -8.648  1.740   1.00 40.26  ? 775  VAL A C   1 
ATOM   1528 O O   . VAL A 1 189 ? 21.973  -7.909  2.407   1.00 40.75  ? 775  VAL A O   1 
ATOM   1529 C CB  . VAL A 1 189 ? 19.031  -8.101  2.543   1.00 35.21  ? 775  VAL A CB  1 
ATOM   1530 C CG1 . VAL A 1 189 ? 18.892  -7.302  1.241   1.00 37.18  ? 775  VAL A CG1 1 
ATOM   1531 C CG2 . VAL A 1 189 ? 17.693  -8.591  3.048   1.00 29.69  ? 775  VAL A CG2 1 
ATOM   1532 N N   . GLY A 1 190 ? 21.486  -8.904  0.449   1.00 45.75  ? 776  GLY A N   1 
ATOM   1533 C CA  . GLY A 1 190 ? 22.550  -8.218  -0.275  1.00 53.59  ? 776  GLY A CA  1 
ATOM   1534 C C   . GLY A 1 190 ? 22.004  -7.064  -1.097  1.00 61.46  ? 776  GLY A C   1 
ATOM   1535 O O   . GLY A 1 190 ? 22.369  -7.009  -2.298  1.00 69.85  ? 776  GLY A O   1 
HETATM 1536 S S   . SCN B 2 .   ? 0.960   -12.220 23.778  1.00 28.76  ? 801  SCN A S   1 
HETATM 1537 C C   . SCN B 2 .   ? 1.078   -13.735 23.917  1.00 16.33  ? 801  SCN A C   1 
HETATM 1538 N N   . SCN B 2 .   ? 1.193   -14.908 24.054  1.00 23.02  ? 801  SCN A N   1 
HETATM 1539 S S   . SCN C 2 .   ? -4.955  -24.374 -8.554  1.00 29.69  ? 802  SCN A S   1 
HETATM 1540 C C   . SCN C 2 .   ? -4.225  -24.841 -7.252  1.00 23.37  ? 802  SCN A C   1 
HETATM 1541 N N   . SCN C 2 .   ? -3.666  -25.328 -6.370  1.00 24.61  ? 802  SCN A N   1 
HETATM 1542 C C1  . EDO D 3 .   ? 17.051  -3.844  8.106   1.00 35.68  ? 803  EDO A C1  1 
HETATM 1543 O O1  . EDO D 3 .   ? 17.494  -3.165  6.901   1.00 44.83  ? 803  EDO A O1  1 
HETATM 1544 C C2  . EDO D 3 .   ? 18.144  -4.391  8.998   1.00 27.67  ? 803  EDO A C2  1 
HETATM 1545 O O2  . EDO D 3 .   ? 19.366  -3.604  8.966   1.00 39.47  ? 803  EDO A O2  1 
HETATM 1546 O O   . HOH E 4 .   ? 25.826  -36.112 7.345   1.00 43.58  ? 901  HOH A O   1 
HETATM 1547 O O   . HOH E 4 .   ? 17.156  -8.337  -4.526  1.00 53.27  ? 902  HOH A O   1 
HETATM 1548 O O   . HOH E 4 .   ? 11.185  -10.550 19.658  1.00 23.94  ? 903  HOH A O   1 
HETATM 1549 O O   . HOH E 4 .   ? -9.698  -22.171 9.755   1.00 44.10  ? 904  HOH A O   1 
HETATM 1550 O O   . HOH E 4 .   ? 9.536   -7.685  -6.751  1.00 50.57  ? 905  HOH A O   1 
HETATM 1551 O O   . HOH E 4 .   ? 17.383  -6.081  -2.997  1.00 40.20  ? 906  HOH A O   1 
HETATM 1552 O O   . HOH E 4 .   ? 14.121  -25.914 16.890  1.00 24.48  ? 907  HOH A O   1 
HETATM 1553 O O   . HOH E 4 .   ? -11.275 -27.004 11.608  1.00 37.53  ? 908  HOH A O   1 
HETATM 1554 O O   . HOH E 4 .   ? 14.590  -35.857 -6.550  1.00 48.59  ? 909  HOH A O   1 
HETATM 1555 O O   . HOH E 4 .   ? -2.153  -23.355 17.336  1.00 53.36  ? 910  HOH A O   1 
HETATM 1556 O O   . HOH E 4 .   ? -0.862  -31.034 -8.572  1.00 44.76  ? 911  HOH A O   1 
HETATM 1557 O O   . HOH E 4 .   ? 23.497  -20.902 -2.112  1.00 32.21  ? 912  HOH A O   1 
HETATM 1558 O O   . HOH E 4 .   ? 1.724   -16.927 25.541  1.00 41.03  ? 913  HOH A O   1 
HETATM 1559 O O   . HOH E 4 .   ? 26.858  -28.654 7.339   1.00 40.21  ? 914  HOH A O   1 
HETATM 1560 O O   . HOH E 4 .   ? -4.341  -19.811 -1.911  1.00 21.69  ? 915  HOH A O   1 
HETATM 1561 O O   . HOH E 4 .   ? 16.115  -24.756 -7.508  1.00 33.32  ? 916  HOH A O   1 
HETATM 1562 O O   . HOH E 4 .   ? 19.281  -10.544 -1.192  1.00 26.92  ? 917  HOH A O   1 
HETATM 1563 O O   . HOH E 4 .   ? 22.647  -33.345 -2.175  1.00 31.43  ? 918  HOH A O   1 
HETATM 1564 O O   . HOH E 4 .   ? 27.135  -22.626 17.990  1.00 52.17  ? 919  HOH A O   1 
HETATM 1565 O O   . HOH E 4 .   ? 17.237  -4.390  -1.012  1.00 44.05  ? 920  HOH A O   1 
HETATM 1566 O O   . HOH E 4 .   ? 23.656  -28.349 -7.649  1.00 21.08  ? 921  HOH A O   1 
HETATM 1567 O O   . HOH E 4 .   ? 23.039  -33.319 4.845   1.00 23.06  ? 922  HOH A O   1 
HETATM 1568 O O   . HOH E 4 .   ? 19.417  -16.482 -5.828  1.00 29.32  ? 923  HOH A O   1 
HETATM 1569 O O   . HOH E 4 .   ? 25.381  -22.537 2.971   1.00 19.62  ? 924  HOH A O   1 
HETATM 1570 O O   . HOH E 4 .   ? 0.090   -27.016 16.093  1.00 50.88  ? 925  HOH A O   1 
HETATM 1571 O O   . HOH E 4 .   ? 17.986  -13.152 6.359   1.00 14.26  ? 926  HOH A O   1 
HETATM 1572 O O   . HOH E 4 .   ? 14.358  -23.199 22.863  1.00 48.74  ? 927  HOH A O   1 
HETATM 1573 O O   . HOH E 4 .   ? 24.665  -16.830 6.359   1.00 30.36  ? 928  HOH A O   1 
HETATM 1574 O O   . HOH E 4 .   ? 5.591   -17.890 23.216  1.00 41.82  ? 929  HOH A O   1 
HETATM 1575 O O   . HOH E 4 .   ? 23.659  -24.474 -9.444  1.00 27.78  ? 930  HOH A O   1 
HETATM 1576 O O   . HOH E 4 .   ? -3.775  -16.247 0.094   1.00 31.92  ? 931  HOH A O   1 
HETATM 1577 O O   . HOH E 4 .   ? 7.263   -33.842 15.238  1.00 50.78  ? 932  HOH A O   1 
HETATM 1578 O O   . HOH E 4 .   ? 13.700  -24.034 -5.390  1.00 21.57  ? 933  HOH A O   1 
HETATM 1579 O O   . HOH E 4 .   ? -8.423  -22.802 3.554   1.00 20.53  ? 934  HOH A O   1 
HETATM 1580 O O   . HOH E 4 .   ? -3.858  -16.560 13.513  1.00 33.57  ? 935  HOH A O   1 
HETATM 1581 O O   . HOH E 4 .   ? 17.832  -10.547 -5.537  1.00 32.74  ? 936  HOH A O   1 
HETATM 1582 O O   . HOH E 4 .   ? 11.633  -31.767 -5.934  1.00 27.96  ? 937  HOH A O   1 
HETATM 1583 O O   . HOH E 4 .   ? 16.497  -20.114 -10.969 1.00 33.46  ? 938  HOH A O   1 
HETATM 1584 O O   . HOH E 4 .   ? 2.051   -2.009  7.359   1.00 43.70  ? 939  HOH A O   1 
HETATM 1585 O O   . HOH E 4 .   ? 18.460  -13.062 9.151   1.00 14.47  ? 940  HOH A O   1 
HETATM 1586 O O   . HOH E 4 .   ? 12.310  -21.479 19.934  1.00 29.12  ? 941  HOH A O   1 
HETATM 1587 O O   . HOH E 4 .   ? -3.979  -19.404 13.450  1.00 32.97  ? 942  HOH A O   1 
HETATM 1588 O O   . HOH E 4 .   ? 8.425   -22.155 20.451  1.00 27.96  ? 943  HOH A O   1 
HETATM 1589 O O   . HOH E 4 .   ? 13.276  -30.882 -7.942  1.00 35.57  ? 944  HOH A O   1 
HETATM 1590 O O   . HOH E 4 .   ? 19.819  -31.253 -5.954  1.00 25.65  ? 945  HOH A O   1 
HETATM 1591 O O   . HOH E 4 .   ? 15.433  -25.589 -4.047  1.00 17.59  ? 946  HOH A O   1 
HETATM 1592 O O   . HOH E 4 .   ? -3.410  -30.458 -8.078  1.00 30.74  ? 947  HOH A O   1 
HETATM 1593 O O   . HOH E 4 .   ? 17.878  -4.491  4.324   1.00 36.26  ? 948  HOH A O   1 
HETATM 1594 O O   . HOH E 4 .   ? 7.712   -8.076  19.269  1.00 13.12  ? 949  HOH A O   1 
HETATM 1595 O O   . HOH E 4 .   ? 19.742  -20.421 18.990  1.00 32.52  ? 950  HOH A O   1 
HETATM 1596 O O   . HOH E 4 .   ? -4.131  -18.382 2.264   1.00 35.39  ? 951  HOH A O   1 
HETATM 1597 O O   . HOH E 4 .   ? -2.802  -9.606  17.982  1.00 35.12  ? 952  HOH A O   1 
HETATM 1598 O O   . HOH E 4 .   ? 25.185  -16.026 13.622  1.00 40.75  ? 953  HOH A O   1 
HETATM 1599 O O   . HOH E 4 .   ? 17.876  -33.252 3.622   1.00 22.35  ? 954  HOH A O   1 
HETATM 1600 O O   . HOH E 4 .   ? 4.921   -26.204 -8.477  1.00 27.17  ? 955  HOH A O   1 
HETATM 1601 O O   . HOH E 4 .   ? -1.777  -16.139 15.461  1.00 31.80  ? 956  HOH A O   1 
HETATM 1602 O O   . HOH E 4 .   ? 3.300   -18.056 -7.287  1.00 37.84  ? 957  HOH A O   1 
HETATM 1603 O O   . HOH E 4 .   ? 1.886   -13.354 -7.136  1.00 40.77  ? 958  HOH A O   1 
HETATM 1604 O O   . HOH E 4 .   ? -12.061 -24.364 9.382   1.00 38.55  ? 959  HOH A O   1 
HETATM 1605 O O   . HOH E 4 .   ? 8.462   -16.689 -8.906  1.00 35.99  ? 960  HOH A O   1 
HETATM 1606 O O   . HOH E 4 .   ? 15.785  -0.454  7.610   1.00 34.35  ? 961  HOH A O   1 
HETATM 1607 O O   . HOH E 4 .   ? 3.232   -9.791  4.281   1.00 17.69  ? 962  HOH A O   1 
HETATM 1608 O O   . HOH E 4 .   ? 8.450   0.079   -4.270  1.00 28.01  ? 963  HOH A O   1 
HETATM 1609 O O   . HOH E 4 .   ? 5.095   -7.855  -4.420  1.00 47.03  ? 964  HOH A O   1 
HETATM 1610 O O   . HOH E 4 .   ? 26.525  -18.620 7.476   1.00 36.31  ? 965  HOH A O   1 
HETATM 1611 O O   . HOH E 4 .   ? 24.873  -36.232 -2.126  1.00 26.50  ? 966  HOH A O   1 
HETATM 1612 O O   . HOH E 4 .   ? -1.528  -27.620 4.216   1.00 37.04  ? 967  HOH A O   1 
HETATM 1613 O O   . HOH E 4 .   ? 1.812   -5.937  18.207  1.00 29.87  ? 968  HOH A O   1 
HETATM 1614 O O   . HOH E 4 .   ? 21.157  -13.112 9.091   1.00 30.24  ? 969  HOH A O   1 
HETATM 1615 O O   . HOH E 4 .   ? 25.684  -33.582 3.877   1.00 33.38  ? 970  HOH A O   1 
HETATM 1616 O O   . HOH E 4 .   ? -5.092  -15.873 16.020  1.00 41.83  ? 971  HOH A O   1 
HETATM 1617 O O   . HOH E 4 .   ? 21.792  -22.638 -8.459  1.00 39.28  ? 972  HOH A O   1 
HETATM 1618 O O   . HOH E 4 .   ? 1.415   -19.552 -8.436  1.00 35.70  ? 973  HOH A O   1 
HETATM 1619 O O   . HOH E 4 .   ? 17.640  -10.465 6.885   1.00 25.20  ? 974  HOH A O   1 
HETATM 1620 O O   . HOH E 4 .   ? 20.076  -8.878  6.228   1.00 34.95  ? 975  HOH A O   1 
HETATM 1621 O O   . HOH E 4 .   ? 11.563  -19.346 7.763   1.00 12.53  ? 976  HOH A O   1 
HETATM 1622 O O   . HOH E 4 .   ? -2.786  -30.644 14.701  1.00 46.55  ? 977  HOH A O   1 
HETATM 1623 O O   . HOH E 4 .   ? 12.306  -26.655 -9.250  1.00 35.36  ? 978  HOH A O   1 
HETATM 1624 O O   . HOH E 4 .   ? 3.143   -4.749  11.868  1.00 26.60  ? 979  HOH A O   1 
HETATM 1625 O O   . HOH E 4 .   ? 6.205   -1.996  -2.470  1.00 44.06  ? 980  HOH A O   1 
HETATM 1626 O O   . HOH E 4 .   ? 2.703   -4.438  15.318  1.00 33.05  ? 981  HOH A O   1 
HETATM 1627 O O   . HOH E 4 .   ? -5.480  -10.177 9.927   1.00 32.91  ? 982  HOH A O   1 
HETATM 1628 O O   . HOH E 4 .   ? -4.023  -9.125  5.916   1.00 29.49  ? 983  HOH A O   1 
HETATM 1629 O O   . HOH E 4 .   ? 12.355  -5.043  11.077  1.00 13.25  ? 984  HOH A O   1 
HETATM 1630 O O   . HOH E 4 .   ? 6.062   -10.252 -8.368  1.00 31.05  ? 985  HOH A O   1 
HETATM 1631 O O   . HOH E 4 .   ? 25.708  -19.981 1.597   1.00 39.79  ? 986  HOH A O   1 
HETATM 1632 O O   . HOH E 4 .   ? 16.552  -38.773 4.569   1.00 40.05  ? 987  HOH A O   1 
HETATM 1633 O O   . HOH E 4 .   ? 20.387  -22.897 19.680  1.00 36.51  ? 988  HOH A O   1 
HETATM 1634 O O   . HOH E 4 .   ? -5.887  -22.621 4.832   1.00 20.58  ? 989  HOH A O   1 
HETATM 1635 O O   . HOH E 4 .   ? 25.043  -29.711 14.897  1.00 29.89  ? 990  HOH A O   1 
HETATM 1636 O O   . HOH E 4 .   ? -2.322  -9.063  14.275  1.00 38.88  ? 991  HOH A O   1 
HETATM 1637 O O   . HOH E 4 .   ? 15.925  -28.375 -7.345  1.00 40.72  ? 992  HOH A O   1 
HETATM 1638 O O   . HOH E 4 .   ? -4.174  -17.442 9.572   1.00 46.03  ? 993  HOH A O   1 
HETATM 1639 O O   . HOH E 4 .   ? 19.597  -31.343 4.432   1.00 18.23  ? 994  HOH A O   1 
HETATM 1640 O O   . HOH E 4 .   ? 20.949  -30.866 -1.982  1.00 21.48  ? 995  HOH A O   1 
HETATM 1641 O O   . HOH E 4 .   ? 5.598   -2.569  4.552   1.00 30.15  ? 996  HOH A O   1 
HETATM 1642 O O   . HOH E 4 .   ? 18.726  -39.230 7.317   1.00 52.58  ? 997  HOH A O   1 
HETATM 1643 O O   . HOH E 4 .   ? 0.267   -16.147 -5.416  1.00 37.34  ? 998  HOH A O   1 
HETATM 1644 O O   . HOH E 4 .   ? 2.155   -2.371  9.426   1.00 39.32  ? 999  HOH A O   1 
HETATM 1645 O O   . HOH E 4 .   ? -0.948  -10.539 20.311  1.00 31.28  ? 1000 HOH A O   1 
HETATM 1646 O O   . HOH E 4 .   ? 29.429  -21.304 11.278  1.00 34.84  ? 1001 HOH A O   1 
HETATM 1647 O O   . HOH E 4 .   ? 4.440   -1.918  11.221  1.00 28.70  ? 1002 HOH A O   1 
HETATM 1648 O O   . HOH E 4 .   ? 30.231  -24.198 11.036  1.00 44.57  ? 1003 HOH A O   1 
HETATM 1649 O O   . HOH E 4 .   ? -0.889  -14.956 -2.951  1.00 24.40  ? 1004 HOH A O   1 
HETATM 1650 O O   . HOH E 4 .   ? 0.762   -8.656  19.880  1.00 39.78  ? 1005 HOH A O   1 
HETATM 1651 O O   . HOH E 4 .   ? 18.124  -9.136  -3.066  1.00 31.12  ? 1006 HOH A O   1 
HETATM 1652 O O   . HOH E 4 .   ? 25.799  -25.277 16.158  1.00 46.43  ? 1007 HOH A O   1 
HETATM 1653 O O   . HOH E 4 .   ? 8.756   -17.782 -11.255 1.00 35.65  ? 1008 HOH A O   1 
HETATM 1654 O O   . HOH E 4 .   ? 7.988   -8.378  -5.311  1.00 30.10  ? 1009 HOH A O   1 
HETATM 1655 O O   . HOH E 4 .   ? 24.027  -13.259 1.322   1.00 43.75  ? 1010 HOH A O   1 
HETATM 1656 O O   . HOH E 4 .   ? 6.153   -24.846 -10.708 1.00 44.75  ? 1011 HOH A O   1 
HETATM 1657 O O   . HOH E 4 .   ? 12.897  -10.327 14.822  1.00 29.78  ? 1012 HOH A O   1 
HETATM 1658 O O   . HOH E 4 .   ? 23.940  -13.443 14.498  0.50 29.15  ? 1013 HOH A O   1 
HETATM 1659 O O   . HOH E 4 .   ? 9.398   -34.066 7.773   1.00 49.91  ? 1014 HOH A O   1 
HETATM 1660 O O   . HOH E 4 .   ? 11.413  -34.212 -3.246  1.00 40.40  ? 1015 HOH A O   1 
HETATM 1661 O O   . HOH E 4 .   ? -3.033  -4.990  -0.458  1.00 51.05  ? 1016 HOH A O   1 
HETATM 1662 O O   . HOH E 4 .   ? -4.299  -17.400 7.642   1.00 43.16  ? 1017 HOH A O   1 
HETATM 1663 O O   . HOH E 4 .   ? 14.114  -8.859  14.924  0.50 18.45  ? 1018 HOH A O   1 
HETATM 1664 O O   . HOH E 4 .   ? 7.775   -15.832 23.110  1.00 42.91  ? 1019 HOH A O   1 
HETATM 1665 O O   . HOH E 4 .   ? 26.762  -15.348 10.412  1.00 36.75  ? 1020 HOH A O   1 
HETATM 1666 O O   . HOH E 4 .   ? 10.757  -33.418 2.643   1.00 42.32  ? 1021 HOH A O   1 
HETATM 1667 O O   . HOH E 4 .   ? 21.580  -20.501 -3.493  1.00 30.20  ? 1022 HOH A O   1 
HETATM 1668 O O   . HOH E 4 .   ? 16.391  -9.463  14.951  0.50 11.72  ? 1023 HOH A O   1 
HETATM 1669 O O   . HOH E 4 .   ? 21.160  -17.612 -3.414  1.00 47.64  ? 1024 HOH A O   1 
HETATM 1670 O O   . HOH E 4 .   ? 7.162   -2.308  3.004   1.00 45.02  ? 1025 HOH A O   1 
HETATM 1671 O O   . HOH E 4 .   ? 24.992  -38.486 0.241   1.00 47.98  ? 1026 HOH A O   1 
HETATM 1672 O O   . HOH E 4 .   ? 3.532   -2.534  15.524  1.00 36.46  ? 1027 HOH A O   1 
HETATM 1673 O O   . HOH E 4 .   ? 26.140  -35.699 2.508   1.00 44.08  ? 1028 HOH A O   1 
HETATM 1674 O O   . HOH E 4 .   ? 15.476  -26.333 -8.099  1.00 49.41  ? 1029 HOH A O   1 
HETATM 1675 O O   . HOH E 4 .   ? -7.542  -21.305 8.255   1.00 36.40  ? 1030 HOH A O   1 
HETATM 1676 O O   . HOH E 4 .   ? 9.816   -31.198 2.802   1.00 37.83  ? 1031 HOH A O   1 
HETATM 1677 O O   . HOH E 4 .   ? 19.854  -6.068  5.499   1.00 41.69  ? 1032 HOH A O   1 
HETATM 1678 O O   . HOH E 4 .   ? -4.389  -3.537  4.742   1.00 51.40  ? 1033 HOH A O   1 
HETATM 1679 O O   . HOH E 4 .   ? 31.261  -19.581 12.311  1.00 47.32  ? 1034 HOH A O   1 
HETATM 1680 O O   . HOH E 4 .   ? 18.719  -32.692 -8.040  1.00 41.66  ? 1035 HOH A O   1 
HETATM 1681 O O   . HOH E 4 .   ? 25.462  -14.608 8.326   1.00 34.56  ? 1036 HOH A O   1 
HETATM 1682 O O   . HOH E 4 .   ? 21.393  -17.990 -7.611  1.00 39.82  ? 1037 HOH A O   1 
HETATM 1683 O O   . HOH E 4 .   ? 28.024  -31.062 14.638  1.00 49.60  ? 1038 HOH A O   1 
HETATM 1684 O O   . HOH E 4 .   ? -5.181  -20.143 4.091   1.00 35.21  ? 1039 HOH A O   1 
HETATM 1685 O O   . HOH E 4 .   ? 22.114  -19.286 20.194  1.00 49.79  ? 1040 HOH A O   1 
HETATM 1686 O O   . HOH E 4 .   ? 22.263  -20.359 -6.584  1.00 37.51  ? 1041 HOH A O   1 
HETATM 1687 O O   . HOH E 4 .   ? 24.260  -26.210 18.375  1.00 47.09  ? 1042 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   . ASN A 1   ? 1.0415 1.0325 0.9875 0.1446  -0.0480 -0.0001 586 ASN A N   
2    C CA  . ASN A 1   ? 0.9891 0.9632 0.9112 0.1411  -0.0474 0.0121  586 ASN A CA  
3    C C   . ASN A 1   ? 0.8439 0.8190 0.7691 0.1190  -0.0373 0.0118  586 ASN A C   
4    O O   . ASN A 1   ? 0.7297 0.6994 0.6656 0.1086  -0.0294 0.0082  586 ASN A O   
5    C CB  . ASN A 1   ? 1.0502 0.9830 0.9483 0.1515  -0.0454 0.0267  586 ASN A CB  
6    C CG  . ASN A 1   ? 1.1914 1.0950 1.0890 0.1375  -0.0319 0.0309  586 ASN A CG  
7    O OD1 . ASN A 1   ? 1.3272 1.2258 1.2397 0.1368  -0.0289 0.0238  586 ASN A OD1 
8    N ND2 . ASN A 1   ? 1.1240 1.0107 1.0064 0.1261  -0.0237 0.0407  586 ASN A ND2 
9    N N   . VAL A 2   ? 0.7105 0.6940 0.6264 0.1137  -0.0388 0.0142  587 VAL A N   
10   C CA  . VAL A 2   ? 0.5846 0.5665 0.5003 0.0957  -0.0303 0.0151  587 VAL A CA  
11   C C   . VAL A 2   ? 0.5193 0.4698 0.4116 0.0950  -0.0233 0.0282  587 VAL A C   
12   O O   . VAL A 2   ? 0.4983 0.4408 0.3687 0.1060  -0.0276 0.0360  587 VAL A O   
13   C CB  . VAL A 2   ? 0.5646 0.5718 0.4846 0.0897  -0.0346 0.0088  587 VAL A CB  
14   C CG1 . VAL A 2   ? 0.5798 0.5936 0.4836 0.1035  -0.0451 0.0102  587 VAL A CG1 
15   C CG2 . VAL A 2   ? 0.4930 0.4925 0.4088 0.0749  -0.0260 0.0114  587 VAL A CG2 
16   N N   . PRO A 3   ? 0.4152 0.3488 0.3110 0.0821  -0.0122 0.0306  588 PRO A N   
17   C CA  . PRO A 3   ? 0.4585 0.3615 0.3366 0.0806  -0.0034 0.0426  588 PRO A CA  
18   C C   . PRO A 3   ? 0.4076 0.3141 0.2720 0.0746  0.0004  0.0465  588 PRO A C   
19   O O   . PRO A 3   ? 0.3707 0.3013 0.2425 0.0694  -0.0031 0.0387  588 PRO A O   
20   C CB  . PRO A 3   ? 0.4891 0.3790 0.3822 0.0687  0.0056  0.0396  588 PRO A CB  
21   C CG  . PRO A 3   ? 0.4154 0.3332 0.3287 0.0599  0.0028  0.0277  588 PRO A CG  
22   C CD  . PRO A 3   ? 0.3760 0.3187 0.2928 0.0691  -0.0077 0.0222  588 PRO A CD  
23   N N   . GLU A 4   ? 0.4342 0.3143 0.2783 0.0758  0.0087  0.0590  589 GLU A N   
24   C CA  . GLU A 4   ? 0.4405 0.3190 0.2721 0.0675  0.0175  0.0632  589 GLU A CA  
25   C C   . GLU A 4   ? 0.3851 0.2678 0.2404 0.0498  0.0265  0.0560  589 GLU A C   
26   O O   . GLU A 4   ? 0.3527 0.2320 0.2270 0.0451  0.0270  0.0510  589 GLU A O   
27   C CB  . GLU A 4   ? 0.4895 0.3374 0.2914 0.0736  0.0258  0.0800  589 GLU A CB  
28   C CG  . GLU A 4   ? 0.5232 0.3708 0.2995 0.0941  0.0135  0.0864  589 GLU A CG  
29   C CD  . GLU A 4   ? 0.5748 0.3843 0.3240 0.1040  0.0196  0.1050  589 GLU A CD  
30   O OE1 . GLU A 4   ? 0.5961 0.3978 0.3118 0.1134  0.0200  0.1163  589 GLU A OE1 
31   O OE2 . GLU A 4   ? 0.5884 0.3767 0.3514 0.1015  0.0241  0.1069  589 GLU A OE2 
32   N N   . LEU A 5   ? 0.3569 0.2498 0.2109 0.0416  0.0319  0.0538  590 LEU A N   
33   C CA  . LEU A 5   ? 0.3228 0.2244 0.1990 0.0270  0.0385  0.0461  590 LEU A CA  
34   C C   . LEU A 5   ? 0.3284 0.2096 0.2147 0.0185  0.0490  0.0492  590 LEU A C   
35   O O   . LEU A 5   ? 0.2889 0.1778 0.1986 0.0107  0.0480  0.0401  590 LEU A O   
36   C CB  . LEU A 5   ? 0.3284 0.2389 0.1976 0.0221  0.0448  0.0451  590 LEU A CB  
37   C CG  . LEU A 5   ? 0.3097 0.2290 0.2017 0.0085  0.0523  0.0374  590 LEU A CG  
38   C CD1 . LEU A 5   ? 0.2645 0.2014 0.1809 0.0056  0.0427  0.0264  590 LEU A CD1 
39   C CD2 . LEU A 5   ? 0.3266 0.2542 0.2100 0.0061  0.0592  0.0360  590 LEU A CD2 
40   N N   . ILE A 6   ? 0.3607 0.2164 0.2298 0.0196  0.0589  0.0611  591 ILE A N   
41   C CA  . ILE A 6   ? 0.3848 0.2201 0.2664 0.0090  0.0707  0.0630  591 ILE A CA  
42   C C   . ILE A 6   ? 0.3913 0.2204 0.2881 0.0119  0.0630  0.0569  591 ILE A C   
43   O O   . ILE A 6   ? 0.4095 0.2371 0.3287 0.0012  0.0671  0.0488  591 ILE A O   
44   C CB  . ILE A 6   ? 0.4854 0.2912 0.3434 0.0087  0.0852  0.0792  591 ILE A CB  
45   C CG1 . ILE A 6   ? 0.5192 0.3067 0.3952 -0.0065 0.1004  0.0794  591 ILE A CG1 
46   C CG2 . ILE A 6   ? 0.5280 0.3125 0.3585 0.0258  0.0789  0.0920  591 ILE A CG2 
47   C CD1 . ILE A 6   ? 0.5857 0.3517 0.4416 -0.0121 0.1196  0.0944  591 ILE A CD1 
48   N N   . GLY A 7   ? 0.3607 0.1907 0.2473 0.0266  0.0512  0.0583  592 GLY A N   
49   C CA  . GLY A 7   ? 0.3472 0.1763 0.2487 0.0307  0.0438  0.0503  592 GLY A CA  
50   C C   . GLY A 7   ? 0.3068 0.1647 0.2305 0.0239  0.0377  0.0356  592 GLY A C   
51   O O   . GLY A 7   ? 0.3208 0.1780 0.2614 0.0193  0.0372  0.0265  592 GLY A O   
52   N N   . ALA A 8   ? 0.2806 0.1630 0.2031 0.0250  0.0319  0.0329  593 ALA A N   
53   C CA  . ALA A 8   ? 0.2411 0.1481 0.1811 0.0194  0.0266  0.0218  593 ALA A CA  
54   C C   . ALA A 8   ? 0.2435 0.1514 0.1996 0.0064  0.0329  0.0161  593 ALA A C   
55   O O   . ALA A 8   ? 0.2220 0.1397 0.1925 0.0031  0.0290  0.0069  593 ALA A O   
56   C CB  . ALA A 8   ? 0.2286 0.1559 0.1646 0.0211  0.0215  0.0212  593 ALA A CB  
57   N N   . GLN A 9   ? 0.2538 0.1524 0.2075 -0.0005 0.0427  0.0209  594 GLN A N   
58   C CA  . GLN A 9   ? 0.2398 0.1439 0.2124 -0.0126 0.0484  0.0140  594 GLN A CA  
59   C C   . GLN A 9   ? 0.2420 0.1348 0.2293 -0.0178 0.0502  0.0074  594 GLN A C   
60   O O   . GLN A 9   ? 0.2380 0.1414 0.2453 -0.0264 0.0505  -0.0025 594 GLN A O   
61   C CB  . GLN A 9   ? 0.2646 0.1622 0.2318 -0.0189 0.0607  0.0203  594 GLN A CB  
62   C CG  . GLN A 9   ? 0.2726 0.1870 0.2311 -0.0156 0.0583  0.0212  594 GLN A CG  
63   C CD  . GLN A 9   ? 0.2936 0.2034 0.2450 -0.0210 0.0717  0.0263  594 GLN A CD  
64   O OE1 . GLN A 9   ? 0.3406 0.2296 0.2816 -0.0234 0.0827  0.0353  594 GLN A OE1 
65   N NE2 . GLN A 9   ? 0.3027 0.2313 0.2609 -0.0234 0.0719  0.0204  594 GLN A NE2 
66   N N   . ALA A 10  ? 0.2579 0.1295 0.2374 -0.0122 0.0507  0.0113  595 ALA A N   
67   C CA  . ALA A 10  ? 0.2673 0.1272 0.2619 -0.0166 0.0516  0.0025  595 ALA A CA  
68   C C   . ALA A 10  ? 0.2469 0.1286 0.2533 -0.0148 0.0404  -0.0113 595 ALA A C   
69   O O   . ALA A 10  ? 0.2746 0.1526 0.2954 -0.0195 0.0399  -0.0223 595 ALA A O   
70   C CB  . ALA A 10  ? 0.3141 0.1451 0.2969 -0.0087 0.0537  0.0096  595 ALA A CB  
71   N N   . HIS A 11  ? 0.2084 0.1101 0.2072 -0.0080 0.0325  -0.0104 596 HIS A N   
72   C CA  . HIS A 11  ? 0.1823 0.1036 0.1869 -0.0052 0.0233  -0.0205 596 HIS A CA  
73   C C   . HIS A 11  ? 0.1728 0.1158 0.1854 -0.0106 0.0201  -0.0243 596 HIS A C   
74   O O   . HIS A 11  ? 0.1631 0.1227 0.1738 -0.0070 0.0131  -0.0276 596 HIS A O   
75   C CB  . HIS A 11  ? 0.1769 0.1047 0.1693 0.0059  0.0179  -0.0169 596 HIS A CB  
76   C CG  . HIS A 11  ? 0.2070 0.1155 0.1935 0.0138  0.0191  -0.0147 596 HIS A CG  
77   N ND1 . HIS A 11  ? 0.2444 0.1366 0.2179 0.0206  0.0216  -0.0034 596 HIS A ND1 
78   C CD2 . HIS A 11  ? 0.1938 0.0946 0.1851 0.0172  0.0177  -0.0231 596 HIS A CD2 
79   C CE1 . HIS A 11  ? 0.2241 0.0988 0.1961 0.0282  0.0213  -0.0045 596 HIS A CE1 
80   N NE2 . HIS A 11  ? 0.2738 0.1531 0.2581 0.0259  0.0193  -0.0177 596 HIS A NE2 
81   N N   . ALA A 12  ? 0.1835 0.1259 0.2042 -0.0186 0.0258  -0.0232 597 ALA A N   
82   C CA  . ALA A 12  ? 0.1719 0.1331 0.2027 -0.0225 0.0229  -0.0271 597 ALA A CA  
83   C C   . ALA A 12  ? 0.1596 0.1353 0.1997 -0.0221 0.0139  -0.0386 597 ALA A C   
84   O O   . ALA A 12  ? 0.1812 0.1524 0.2309 -0.0253 0.0136  -0.0480 597 ALA A O   
85   C CB  . ALA A 12  ? 0.1933 0.1518 0.2370 -0.0316 0.0319  -0.0280 597 ALA A CB  
86   N N   . VAL A 13  ? 0.1439 0.1351 0.1804 -0.0182 0.0072  -0.0374 598 VAL A N   
87   C CA  . VAL A 13  ? 0.1412 0.1468 0.1814 -0.0160 -0.0019 -0.0459 598 VAL A CA  
88   C C   . VAL A 13  ? 0.1418 0.1608 0.1917 -0.0167 -0.0056 -0.0467 598 VAL A C   
89   O O   . VAL A 13  ? 0.1752 0.1926 0.2288 -0.0190 -0.0005 -0.0415 598 VAL A O   
90   C CB  . VAL A 13  ? 0.1601 0.1703 0.1839 -0.0087 -0.0067 -0.0427 598 VAL A CB  
91   C CG1 . VAL A 13  ? 0.1680 0.1675 0.1864 -0.0065 -0.0038 -0.0453 598 VAL A CG1 
92   C CG2 . VAL A 13  ? 0.1611 0.1734 0.1753 -0.0060 -0.0058 -0.0316 598 VAL A CG2 
93   N N   . ASN A 14  ? 0.1244 0.1567 0.1777 -0.0136 -0.0151 -0.0544 599 ASN A N   
94   C CA  A ASN A 14  ? 0.1285 0.1750 0.1932 -0.0119 -0.0215 -0.0577 599 ASN A CA  
95   C CA  B ASN A 14  ? 0.1296 0.1759 0.1941 -0.0119 -0.0214 -0.0575 599 ASN A CA  
96   C C   . ASN A 14  ? 0.1342 0.1845 0.1823 -0.0034 -0.0283 -0.0489 599 ASN A C   
97   O O   . ASN A 14  ? 0.1832 0.2401 0.2208 0.0021  -0.0363 -0.0513 599 ASN A O   
98   C CB  A ASN A 14  ? 0.1317 0.1911 0.2130 -0.0135 -0.0286 -0.0735 599 ASN A CB  
99   C CB  B ASN A 14  ? 0.1330 0.1935 0.2138 -0.0127 -0.0294 -0.0729 599 ASN A CB  
100  C CG  A ASN A 14  ? 0.1384 0.2152 0.2362 -0.0108 -0.0361 -0.0792 599 ASN A CG  
101  C CG  B ASN A 14  ? 0.1545 0.2109 0.2559 -0.0231 -0.0218 -0.0827 599 ASN A CG  
102  O OD1 A ASN A 14  ? 0.1727 0.2488 0.2754 -0.0107 -0.0318 -0.0726 599 ASN A OD1 
103  O OD1 B ASN A 14  ? 0.1856 0.2329 0.2935 -0.0294 -0.0104 -0.0771 599 ASN A OD1 
104  N ND2 A ASN A 14  ? 0.1596 0.2529 0.2680 -0.0083 -0.0473 -0.0930 599 ASN A ND2 
105  N ND2 B ASN A 14  ? 0.1740 0.2354 0.2844 -0.0254 -0.0270 -0.0971 599 ASN A ND2 
106  N N   . VAL A 15  ? 0.1352 0.1808 0.1810 -0.0027 -0.0247 -0.0395 600 VAL A N   
107  C CA  . VAL A 15  ? 0.1567 0.2009 0.1882 0.0034  -0.0287 -0.0297 600 VAL A CA  
108  C C   . VAL A 15  ? 0.1561 0.2079 0.1967 0.0089  -0.0364 -0.0310 600 VAL A C   
109  O O   . VAL A 15  ? 0.1495 0.2055 0.2085 0.0068  -0.0344 -0.0362 600 VAL A O   
110  C CB  . VAL A 15  ? 0.1677 0.2011 0.1927 0.0007  -0.0206 -0.0204 600 VAL A CB  
111  C CG1 . VAL A 15  ? 0.1681 0.1977 0.1833 0.0047  -0.0230 -0.0108 600 VAL A CG1 
112  C CG2 . VAL A 15  ? 0.1644 0.1921 0.1803 -0.0018 -0.0151 -0.0191 600 VAL A CG2 
113  N N   . ILE A 16  ? 0.1648 0.2178 0.1918 0.0168  -0.0444 -0.0255 601 ILE A N   
114  C CA  . ILE A 16  ? 0.1962 0.2527 0.2285 0.0249  -0.0528 -0.0238 601 ILE A CA  
115  C C   . ILE A 16  ? 0.2110 0.2538 0.2246 0.0295  -0.0526 -0.0087 601 ILE A C   
116  O O   . ILE A 16  ? 0.2418 0.2778 0.2376 0.0270  -0.0477 -0.0013 601 ILE A O   
117  C CB  . ILE A 16  ? 0.2691 0.3418 0.3057 0.0324  -0.0659 -0.0333 601 ILE A CB  
118  C CG1 . ILE A 16  ? 0.2898 0.3634 0.3018 0.0364  -0.0705 -0.0306 601 ILE A CG1 
119  C CG2 . ILE A 16  ? 0.2735 0.3604 0.3368 0.0258  -0.0650 -0.0500 601 ILE A CG2 
120  C CD1 . ILE A 16  ? 0.3459 0.4356 0.3566 0.0468  -0.0861 -0.0388 601 ILE A CD1 
121  N N   . LEU A 17  ? 0.1855 0.2235 0.2055 0.0355  -0.0563 -0.0048 602 LEU A N   
122  C CA  . LEU A 17  ? 0.2016 0.2222 0.2060 0.0389  -0.0551 0.0100  602 LEU A CA  
123  C C   . LEU A 17  ? 0.2308 0.2505 0.2143 0.0495  -0.0646 0.0180  602 LEU A C   
124  O O   . LEU A 17  ? 0.2649 0.2972 0.2510 0.0588  -0.0766 0.0117  602 LEU A O   
125  C CB  . LEU A 17  ? 0.2065 0.2208 0.2278 0.0422  -0.0558 0.0091  602 LEU A CB  
126  C CG  . LEU A 17  ? 0.1934 0.2084 0.2309 0.0328  -0.0458 0.0016  602 LEU A CG  
127  C CD1 . LEU A 17  ? 0.2058 0.2199 0.2619 0.0371  -0.0469 -0.0036 602 LEU A CD1 
128  C CD2 . LEU A 17  ? 0.2109 0.2137 0.2377 0.0242  -0.0362 0.0087  602 LEU A CD2 
129  N N   . ASP A 18  ? 0.2534 0.2585 0.2156 0.0479  -0.0587 0.0324  603 ASP A N   
130  C CA  . ASP A 18  ? 0.2978 0.2966 0.2336 0.0576  -0.0646 0.0448  603 ASP A CA  
131  C C   . ASP A 18  ? 0.3385 0.3176 0.2734 0.0656  -0.0679 0.0569  603 ASP A C   
132  O O   . ASP A 18  ? 0.3619 0.3208 0.2924 0.0601  -0.0584 0.0686  603 ASP A O   
133  C CB  . ASP A 18  ? 0.3487 0.3422 0.2630 0.0504  -0.0535 0.0542  603 ASP A CB  
134  C CG  . ASP A 18  ? 0.4627 0.4498 0.3446 0.0595  -0.0566 0.0684  603 ASP A CG  
135  O OD1 . ASP A 18  ? 0.4898 0.4732 0.3645 0.0727  -0.0686 0.0729  603 ASP A OD1 
136  O OD2 . ASP A 18  ? 0.5796 0.5663 0.4438 0.0539  -0.0467 0.0746  603 ASP A OD2 
137  N N   . ALA A 19  ? 0.3445 0.3292 0.2849 0.0791  -0.0818 0.0533  604 ALA A N   
138  C CA  . ALA A 19  ? 0.3966 0.3611 0.3395 0.0886  -0.0858 0.0633  604 ALA A CA  
139  C C   . ALA A 19  ? 0.4869 0.4289 0.3960 0.0952  -0.0852 0.0855  604 ALA A C   
140  O O   . ALA A 19  ? 0.5749 0.4909 0.4820 0.0989  -0.0832 0.0982  604 ALA A O   
141  C CB  . ALA A 19  ? 0.4058 0.3856 0.3670 0.1024  -0.1012 0.0518  604 ALA A CB  
142  N N   . GLU A 20  ? 0.5138 0.4643 0.3957 0.0965  -0.0859 0.0900  605 GLU A N   
143  C CA  . GLU A 20  ? 0.6400 0.5710 0.4851 0.1040  -0.0849 0.1118  605 GLU A CA  
144  C C   . GLU A 20  ? 0.6559 0.5594 0.4965 0.0910  -0.0666 0.1276  605 GLU A C   
145  O O   . GLU A 20  ? 0.7634 0.6393 0.5856 0.0967  -0.0646 0.1474  605 GLU A O   
146  C CB  . GLU A 20  ? 0.6958 0.6439 0.5119 0.1062  -0.0865 0.1115  605 GLU A CB  
147  C CG  . GLU A 20  ? 0.8595 0.7944 0.6353 0.1225  -0.0939 0.1308  605 GLU A CG  
148  C CD  . GLU A 20  ? 0.9425 0.8922 0.6849 0.1232  -0.0917 0.1316  605 GLU A CD  
149  O OE1 . GLU A 20  ? 0.9186 0.8876 0.6720 0.1106  -0.0841 0.1166  605 GLU A OE1 
150  O OE2 . GLU A 20  ? 0.9531 0.8934 0.6574 0.1374  -0.0977 0.1477  605 GLU A OE2 
151  N N   . THR A 21  ? 0.6359 0.5465 0.4943 0.0736  -0.0537 0.1187  606 THR A N   
152  C CA  . THR A 21  ? 0.6987 0.5896 0.5538 0.0598  -0.0363 0.1310  606 THR A CA  
153  C C   . THR A 21  ? 0.6412 0.5218 0.5286 0.0504  -0.0312 0.1238  606 THR A C   
154  O O   . THR A 21  ? 0.6592 0.5310 0.5533 0.0360  -0.0173 0.1269  606 THR A O   
155  C CB  . THR A 21  ? 0.6884 0.5982 0.5348 0.0490  -0.0260 0.1266  606 THR A CB  
156  O OG1 . THR A 21  ? 0.5596 0.4906 0.4329 0.0425  -0.0276 0.1059  606 THR A OG1 
157  C CG2 . THR A 21  ? 0.7271 0.6472 0.5397 0.0597  -0.0316 0.1321  606 THR A CG2 
158  N N   . ALA A 22  ? 0.5517 0.4350 0.4592 0.0590  -0.0425 0.1131  607 ALA A N   
159  C CA  . ALA A 22  ? 0.5303 0.4050 0.4664 0.0529  -0.0392 0.1042  607 ALA A CA  
160  C C   . ALA A 22  ? 0.5523 0.3913 0.4865 0.0537  -0.0347 0.1191  607 ALA A C   
161  O O   . ALA A 22  ? 0.5543 0.3753 0.4687 0.0661  -0.0404 0.1348  607 ALA A O   
162  C CB  . ALA A 22  ? 0.5179 0.4077 0.4730 0.0636  -0.0519 0.0892  607 ALA A CB  
163  N N   . TYR A 23  ? 0.5254 0.3540 0.4802 0.0410  -0.0252 0.1134  608 TYR A N   
164  C CA  . TYR A 23  ? 0.5702 0.3656 0.5341 0.0422  -0.0230 0.1201  608 TYR A CA  
165  C C   . TYR A 23  ? 0.5887 0.3765 0.5541 0.0629  -0.0380 0.1204  608 TYR A C   
166  O O   . TYR A 23  ? 0.5566 0.3698 0.5357 0.0698  -0.0473 0.1044  608 TYR A O   
167  C CB  . TYR A 23  ? 0.5499 0.3479 0.5419 0.0285  -0.0159 0.1036  608 TYR A CB  
168  C CG  . TYR A 23  ? 0.6107 0.3745 0.6163 0.0279  -0.0132 0.1062  608 TYR A CG  
169  C CD1 . TYR A 23  ? 0.6613 0.3978 0.6622 0.0164  -0.0012 0.1202  608 TYR A CD1 
170  C CD2 . TYR A 23  ? 0.6197 0.3790 0.6447 0.0380  -0.0213 0.0935  608 TYR A CD2 
171  C CE1 . TYR A 23  ? 0.7248 0.4263 0.7392 0.0152  0.0016  0.1224  608 TYR A CE1 
172  C CE2 . TYR A 23  ? 0.6524 0.3785 0.6906 0.0384  -0.0190 0.0944  608 TYR A CE2 
173  C CZ  . TYR A 23  ? 0.7093 0.4049 0.7422 0.0267  -0.0078 0.1090  608 TYR A CZ  
174  O OH  . TYR A 23  ? 0.7398 0.3990 0.7869 0.0255  -0.0045 0.1099  608 TYR A OH  
175  N N   . PRO A 24  ? 0.6272 0.3822 0.5785 0.0741  -0.0411 0.1388  609 PRO A N   
176  C CA  . PRO A 24  ? 0.6480 0.4009 0.5954 0.0973  -0.0579 0.1410  609 PRO A CA  
177  C C   . PRO A 24  ? 0.6488 0.4021 0.6273 0.1072  -0.0663 0.1242  609 PRO A C   
178  O O   . PRO A 24  ? 0.6557 0.4157 0.6359 0.1269  -0.0812 0.1221  609 PRO A O   
179  C CB  . PRO A 24  ? 0.7102 0.4232 0.6299 0.1060  -0.0569 0.1683  609 PRO A CB  
180  C CG  . PRO A 24  ? 0.7181 0.4049 0.6424 0.0849  -0.0377 0.1755  609 PRO A CG  
181  C CD  . PRO A 24  ? 0.6826 0.4023 0.6183 0.0654  -0.0283 0.1598  609 PRO A CD  
182  N N   . ASN A 25  ? 0.6465 0.3955 0.6503 0.0949  -0.0575 0.1105  610 ASN A N   
183  C CA  . ASN A 25  ? 0.6330 0.3874 0.6654 0.1044  -0.0643 0.0920  610 ASN A CA  
184  C C   . ASN A 25  ? 0.5433 0.3412 0.5919 0.0997  -0.0655 0.0701  610 ASN A C   
185  O O   . ASN A 25  ? 0.5454 0.3545 0.6184 0.1039  -0.0676 0.0522  610 ASN A O   
186  C CB  . ASN A 25  ? 0.6695 0.3954 0.7201 0.0964  -0.0556 0.0869  610 ASN A CB  
187  C CG  . ASN A 25  ? 0.7662 0.4446 0.8052 0.1037  -0.0553 0.1078  610 ASN A CG  
188  O OD1 . ASN A 25  ? 0.8696 0.5245 0.8963 0.0896  -0.0436 0.1222  610 ASN A OD1 
189  N ND2 . ASN A 25  ? 0.8112 0.4750 0.8540 0.1259  -0.0677 0.1105  610 ASN A ND2 
190  N N   . LEU A 26  ? 0.5103 0.3317 0.5452 0.0908  -0.0629 0.0713  611 LEU A N   
191  C CA  . LEU A 26  ? 0.4386 0.2970 0.4864 0.0865  -0.0636 0.0532  611 LEU A CA  
192  C C   . LEU A 26  ? 0.4185 0.2977 0.4725 0.1037  -0.0778 0.0473  611 LEU A C   
193  O O   . LEU A 26  ? 0.4439 0.3166 0.4823 0.1173  -0.0883 0.0594  611 LEU A O   
194  C CB  . LEU A 26  ? 0.4113 0.2837 0.4442 0.0714  -0.0556 0.0560  611 LEU A CB  
195  C CG  . LEU A 26  ? 0.4001 0.2601 0.4332 0.0542  -0.0422 0.0573  611 LEU A CG  
196  C CD1 . LEU A 26  ? 0.4002 0.2770 0.4199 0.0426  -0.0360 0.0595  611 LEU A CD1 
197  C CD2 . LEU A 26  ? 0.4021 0.2680 0.4584 0.0483  -0.0378 0.0394  611 LEU A CD2 
198  N N   . ILE A 27  ? 0.3825 0.2878 0.4604 0.1027  -0.0777 0.0277  612 ILE A N   
199  C CA  . ILE A 27  ? 0.3508 0.2829 0.4443 0.1155  -0.0890 0.0164  612 ILE A CA  
200  C C   . ILE A 27  ? 0.2948 0.2580 0.3930 0.1030  -0.0840 0.0049  612 ILE A C   
201  O O   . ILE A 27  ? 0.2842 0.2503 0.3864 0.0886  -0.0718 -0.0012 612 ILE A O   
202  C CB  . ILE A 27  ? 0.3652 0.3006 0.4880 0.1240  -0.0900 0.0016  612 ILE A CB  
203  C CG1 . ILE A 27  ? 0.4335 0.3350 0.5543 0.1377  -0.0954 0.0117  612 ILE A CG1 
204  C CG2 . ILE A 27  ? 0.3448 0.3166 0.4901 0.1328  -0.0984 -0.0142 612 ILE A CG2 
205  C CD1 . ILE A 27  ? 0.4652 0.3706 0.6161 0.1499  -0.0983 -0.0041 612 ILE A CD1 
206  N N   . PHE A 28  ? 0.2858 0.2688 0.3796 0.1088  -0.0937 0.0039  613 PHE A N   
207  C CA  . PHE A 28  ? 0.2674 0.2761 0.3649 0.0971  -0.0896 -0.0060 613 PHE A CA  
208  C C   . PHE A 28  ? 0.2614 0.3010 0.3879 0.1028  -0.0959 -0.0242 613 PHE A C   
209  O O   . PHE A 28  ? 0.2957 0.3422 0.4320 0.1192  -0.1093 -0.0267 613 PHE A O   
210  C CB  . PHE A 28  ? 0.2830 0.2932 0.3543 0.0965  -0.0946 0.0034  613 PHE A CB  
211  C CG  . PHE A 28  ? 0.3007 0.2852 0.3457 0.0884  -0.0857 0.0200  613 PHE A CG  
212  C CD1 . PHE A 28  ? 0.3378 0.2954 0.3656 0.0970  -0.0887 0.0368  613 PHE A CD1 
213  C CD2 . PHE A 28  ? 0.2925 0.2791 0.3333 0.0721  -0.0733 0.0183  613 PHE A CD2 
214  C CE1 . PHE A 28  ? 0.3525 0.2876 0.3615 0.0869  -0.0778 0.0507  613 PHE A CE1 
215  C CE2 . PHE A 28  ? 0.3285 0.2955 0.3505 0.0643  -0.0647 0.0314  613 PHE A CE2 
216  C CZ  . PHE A 28  ? 0.3220 0.2644 0.3293 0.0707  -0.0664 0.0471  613 PHE A CZ  
217  N N   . SER A 29  ? 0.2441 0.3029 0.3839 0.0895  -0.0866 -0.0363 614 SER A N   
218  C CA  . SER A 29  ? 0.2282 0.3190 0.3961 0.0912  -0.0909 -0.0537 614 SER A CA  
219  C C   . SER A 29  ? 0.2454 0.3501 0.4049 0.0964  -0.1046 -0.0542 614 SER A C   
220  O O   . SER A 29  ? 0.2464 0.3390 0.3776 0.0934  -0.1057 -0.0431 614 SER A O   
221  C CB  . SER A 29  ? 0.2112 0.3137 0.3926 0.0742  -0.0751 -0.0639 614 SER A CB  
222  O OG  . SER A 29  ? 0.2073 0.3007 0.3665 0.0620  -0.0689 -0.0564 614 SER A OG  
223  N N   . ASP A 30  ? 0.2416 0.3759 0.4286 0.1030  -0.1142 -0.0703 615 ASP A N   
224  C CA  . ASP A 30  ? 0.2810 0.4323 0.4627 0.1094  -0.1296 -0.0746 615 ASP A CA  
225  C C   . ASP A 30  ? 0.2482 0.4003 0.4168 0.0933  -0.1220 -0.0756 615 ASP A C   
226  O O   . ASP A 30  ? 0.2871 0.4392 0.4335 0.0980  -0.1321 -0.0715 615 ASP A O   
227  C CB  . ASP A 30  ? 0.2894 0.4769 0.5093 0.1172  -0.1408 -0.0954 615 ASP A CB  
228  C CG  . ASP A 30  ? 0.3978 0.5904 0.6275 0.1406  -0.1575 -0.0957 615 ASP A CG  
229  O OD1 . ASP A 30  ? 0.5106 0.6738 0.7169 0.1514  -0.1598 -0.0780 615 ASP A OD1 
230  O OD2 . ASP A 30  ? 0.4684 0.6948 0.7320 0.1482  -0.1682 -0.1143 615 ASP A OD2 
231  N N   . ASP A 31  ? 0.2090 0.3601 0.3884 0.0756  -0.1044 -0.0803 616 ASP A N   
232  C CA  . ASP A 31  ? 0.2001 0.3512 0.3711 0.0613  -0.0971 -0.0827 616 ASP A CA  
233  C C   . ASP A 31  ? 0.1919 0.3150 0.3277 0.0563  -0.0892 -0.0651 616 ASP A C   
234  O O   . ASP A 31  ? 0.1801 0.2989 0.3065 0.0455  -0.0818 -0.0651 616 ASP A O   
235  C CB  . ASP A 31  ? 0.2023 0.3629 0.3992 0.0454  -0.0815 -0.0942 616 ASP A CB  
236  C CG  . ASP A 31  ? 0.2180 0.3644 0.4158 0.0391  -0.0652 -0.0880 616 ASP A CG  
237  O OD1 . ASP A 31  ? 0.1882 0.3145 0.3666 0.0452  -0.0650 -0.0749 616 ASP A OD1 
238  O OD2 . ASP A 31  ? 0.2450 0.4002 0.4629 0.0275  -0.0520 -0.0968 616 ASP A OD2 
239  N N   . LEU A 32  ? 0.1960 0.2998 0.3153 0.0641  -0.0901 -0.0508 617 LEU A N   
240  C CA  . LEU A 32  ? 0.1953 0.2749 0.2848 0.0596  -0.0829 -0.0347 617 LEU A CA  
241  C C   . LEU A 32  ? 0.1597 0.2319 0.2505 0.0443  -0.0664 -0.0351 617 LEU A C   
242  O O   . LEU A 32  ? 0.1640 0.2238 0.2348 0.0383  -0.0604 -0.0266 617 LEU A O   
243  C CB  . LEU A 32  ? 0.2233 0.3016 0.2862 0.0634  -0.0903 -0.0286 617 LEU A CB  
244  C CG  . LEU A 32  ? 0.2785 0.3590 0.3301 0.0808  -0.1068 -0.0235 617 LEU A CG  
245  C CD1 . LEU A 32  ? 0.3039 0.3876 0.3277 0.0845  -0.1139 -0.0201 617 LEU A CD1 
246  C CD2 . LEU A 32  ? 0.3189 0.3750 0.3583 0.0880  -0.1056 -0.0069 617 LEU A CD2 
247  N N   . LYS A 33  ? 0.1496 0.2286 0.2631 0.0391  -0.0585 -0.0439 618 LYS A N   
248  C CA  . LYS A 33  ? 0.1398 0.2109 0.2515 0.0270  -0.0437 -0.0430 618 LYS A CA  
249  C C   . LYS A 33  ? 0.1324 0.1903 0.2428 0.0281  -0.0377 -0.0382 618 LYS A C   
250  O O   . LYS A 33  ? 0.1414 0.1900 0.2429 0.0204  -0.0279 -0.0348 618 LYS A O   
251  C CB  . LYS A 33  ? 0.1419 0.2282 0.2761 0.0186  -0.0357 -0.0558 618 LYS A CB  
252  C CG  . LYS A 33  ? 0.1743 0.2706 0.3122 0.0138  -0.0387 -0.0627 618 LYS A CG  
253  C CD  . LYS A 33  ? 0.2110 0.2939 0.3279 0.0069  -0.0337 -0.0560 618 LYS A CD  
254  C CE  . LYS A 33  ? 0.2448 0.3383 0.3696 0.0035  -0.0379 -0.0662 618 LYS A CE  
255  N NZ  . LYS A 33  ? 0.2794 0.3592 0.3850 -0.0015 -0.0331 -0.0609 618 LYS A NZ  
256  N N   A SER A 34  ? 0.1360 0.1925 0.2540 0.0387  -0.0448 -0.0381 619 SER A N   
257  N N   B SER A 34  ? 0.1470 0.2041 0.2664 0.0386  -0.0444 -0.0388 619 SER A N   
258  C CA  A SER A 34  ? 0.1418 0.1849 0.2609 0.0401  -0.0398 -0.0360 619 SER A CA  
259  C CA  B SER A 34  ? 0.1618 0.2071 0.2844 0.0402  -0.0391 -0.0380 619 SER A CA  
260  C C   A SER A 34  ? 0.1638 0.1878 0.2704 0.0493  -0.0478 -0.0245 619 SER A C   
261  C C   B SER A 34  ? 0.1785 0.2047 0.2897 0.0500  -0.0476 -0.0269 619 SER A C   
262  O O   A SER A 34  ? 0.1710 0.1951 0.2727 0.0590  -0.0590 -0.0196 619 SER A O   
263  O O   B SER A 34  ? 0.1852 0.2139 0.2958 0.0609  -0.0594 -0.0240 619 SER A O   
264  C CB  A SER A 34  ? 0.1379 0.1947 0.2824 0.0442  -0.0378 -0.0488 619 SER A CB  
265  C CB  B SER A 34  ? 0.1726 0.2352 0.3228 0.0429  -0.0359 -0.0524 619 SER A CB  
266  O OG  A SER A 34  ? 0.1152 0.1886 0.2714 0.0346  -0.0281 -0.0582 619 SER A OG  
267  O OG  B SER A 34  ? 0.1923 0.2473 0.3475 0.0436  -0.0288 -0.0560 619 SER A OG  
268  N N   . VAL A 35  ? 0.1849 0.1918 0.2871 0.0463  -0.0417 -0.0210 620 VAL A N   
269  C CA  . VAL A 35  ? 0.2068 0.1909 0.2997 0.0525  -0.0462 -0.0100 620 VAL A CA  
270  C C   . VAL A 35  ? 0.1979 0.1700 0.3008 0.0514  -0.0403 -0.0156 620 VAL A C   
271  O O   . VAL A 35  ? 0.1981 0.1732 0.3011 0.0416  -0.0312 -0.0215 620 VAL A O   
272  C CB  . VAL A 35  ? 0.2251 0.1964 0.2944 0.0456  -0.0438 0.0037  620 VAL A CB  
273  C CG1 . VAL A 35  ? 0.2138 0.1863 0.2782 0.0322  -0.0334 0.0017  620 VAL A CG1 
274  C CG2 . VAL A 35  ? 0.2634 0.2092 0.3235 0.0512  -0.0467 0.0166  620 VAL A CG2 
275  N N   . ARG A 36  ? 0.2207 0.1781 0.3305 0.0626  -0.0464 -0.0136 621 ARG A N   
276  C CA  . ARG A 36  ? 0.2316 0.1732 0.3507 0.0624  -0.0418 -0.0193 621 ARG A CA  
277  C C   . ARG A 36  ? 0.2688 0.1796 0.3805 0.0686  -0.0465 -0.0061 621 ARG A C   
278  O O   . ARG A 36  ? 0.2874 0.1913 0.3889 0.0776  -0.0548 0.0063  621 ARG A O   
279  C CB  . ARG A 36  ? 0.2360 0.1930 0.3786 0.0705  -0.0419 -0.0361 621 ARG A CB  
280  C CG  . ARG A 36  ? 0.2560 0.2173 0.4116 0.0876  -0.0535 -0.0367 621 ARG A CG  
281  C CD  . ARG A 36  ? 0.2619 0.2466 0.4439 0.0936  -0.0516 -0.0553 621 ARG A CD  
282  N NE  . ARG A 36  ? 0.3191 0.3097 0.5168 0.1120  -0.0645 -0.0574 621 ARG A NE  
283  C CZ  . ARG A 36  ? 0.3664 0.3352 0.5693 0.1269  -0.0722 -0.0543 621 ARG A CZ  
284  N NH1 . ARG A 36  ? 0.3902 0.3304 0.5893 0.1247  -0.0670 -0.0527 621 ARG A NH1 
285  N NH2 . ARG A 36  ? 0.4419 0.4164 0.6549 0.1452  -0.0863 -0.0534 621 ARG A NH2 
286  N N   . LEU A 37  ? 0.2828 0.1737 0.4006 0.0650  -0.0414 -0.0098 622 LEU A N   
287  C CA  . LEU A 37  ? 0.3367 0.1937 0.4515 0.0702  -0.0441 0.0014  622 LEU A CA  
288  C C   . LEU A 37  ? 0.3563 0.2069 0.4889 0.0875  -0.0516 -0.0058 622 LEU A C   
289  O O   . LEU A 37  ? 0.3688 0.2271 0.5197 0.0888  -0.0484 -0.0236 622 LEU A O   
290  C CB  . LEU A 37  ? 0.3457 0.1862 0.4625 0.0563  -0.0349 -0.0020 622 LEU A CB  
291  C CG  . LEU A 37  ? 0.3996 0.2010 0.5142 0.0568  -0.0344 0.0104  622 LEU A CG  
292  C CD1 . LEU A 37  ? 0.4215 0.2129 0.5133 0.0576  -0.0362 0.0337  622 LEU A CD1 
293  C CD2 . LEU A 37  ? 0.4187 0.2108 0.5405 0.0407  -0.0253 0.0019  622 LEU A CD2 
294  N N   . GLY A 38  ? 0.3936 0.2301 0.5194 0.1019  -0.0615 0.0078  623 GLY A N   
295  C CA  . GLY A 38  ? 0.4589 0.2827 0.6004 0.1213  -0.0703 0.0039  623 GLY A CA  
296  C C   . GLY A 38  ? 0.5334 0.3140 0.6769 0.1217  -0.0671 0.0095  623 GLY A C   
297  O O   . GLY A 38  ? 0.5189 0.2854 0.6576 0.1048  -0.0569 0.0109  623 GLY A O   
298  N N   . ASN A 39  ? 0.6807 0.4393 0.8318 0.1412  -0.0763 0.0132  624 ASN A N   
299  C CA  . ASN A 39  ? 0.7802 0.4923 0.9341 0.1435  -0.0739 0.0198  624 ASN A CA  
300  C C   . ASN A 39  ? 0.8588 0.5347 0.9853 0.1431  -0.0743 0.0493  624 ASN A C   
301  O O   . ASN A 39  ? 0.8242 0.5133 0.9279 0.1406  -0.0761 0.0636  624 ASN A O   
302  C CB  . ASN A 39  ? 0.8478 0.5511 1.0243 0.1662  -0.0832 0.0087  624 ASN A CB  
303  C CG  . ASN A 39  ? 0.8897 0.6268 1.0930 0.1651  -0.0795 -0.0208 624 ASN A CG  
304  O OD1 . ASN A 39  ? 0.9420 0.7088 1.1605 0.1799  -0.0871 -0.0321 624 ASN A OD1 
305  N ND2 . ASN A 39  ? 0.8948 0.6296 1.1039 0.1478  -0.0676 -0.0339 624 ASN A ND2 
306  N N   . LYS A 40  ? 1.0023 0.6307 1.1306 0.1460  -0.0720 0.0585  625 LYS A N   
307  C CA  . LYS A 40  ? 1.0986 0.6868 1.2003 0.1467  -0.0705 0.0885  625 LYS A CA  
308  C C   . LYS A 40  ? 1.1778 0.7646 1.2606 0.1720  -0.0862 0.1057  625 LYS A C   
309  O O   . LYS A 40  ? 1.2275 0.7950 1.2791 0.1727  -0.0858 0.1318  625 LYS A O   
310  C CB  . LYS A 40  ? 1.1177 0.6521 1.2289 0.1436  -0.0635 0.0934  625 LYS A CB  
311  C CG  . LYS A 40  ? 1.1145 0.6426 1.2386 0.1162  -0.0477 0.0821  625 LYS A CG  
312  C CD  . LYS A 40  ? 1.1939 0.6644 1.3164 0.1075  -0.0379 0.0982  625 LYS A CD  
313  C CE  . LYS A 40  ? 1.2600 0.6867 1.3960 0.1268  -0.0445 0.0987  625 LYS A CE  
314  N NZ  . LYS A 40  ? 1.2641 0.6958 1.4347 0.1250  -0.0439 0.0664  625 LYS A NZ  
315  N N   . TRP A 41  ? 1.2177 0.8270 1.3189 0.1932  -0.1001 0.0906  626 TRP A N   
316  C CA  . TRP A 41  ? 1.2886 0.9003 1.3767 0.2200  -0.1180 0.1031  626 TRP A CA  
317  C C   . TRP A 41  ? 1.2145 0.8799 1.2964 0.2206  -0.1256 0.0962  626 TRP A C   
318  O O   . TRP A 41  ? 1.1763 0.8514 1.2454 0.2410  -0.1414 0.1049  626 TRP A O   
319  C CB  . TRP A 41  ? 1.3367 0.9397 1.4522 0.2453  -0.1301 0.0903  626 TRP A CB  
320  C CG  . TRP A 41  ? 1.4013 1.0389 1.5550 0.2407  -0.1263 0.0566  626 TRP A CG  
321  C CD1 . TRP A 41  ? 1.4141 1.1050 1.5870 0.2463  -0.1328 0.0359  626 TRP A CD1 
322  C CD2 . TRP A 41  ? 1.4803 1.1019 1.6568 0.2285  -0.1139 0.0393  626 TRP A CD2 
323  N NE1 . TRP A 41  ? 1.4382 1.1463 1.6414 0.2388  -0.1240 0.0088  626 TRP A NE1 
324  C CE2 . TRP A 41  ? 1.4498 1.1171 1.6548 0.2286  -0.1132 0.0096  626 TRP A CE2 
325  C CE3 . TRP A 41  ? 1.4900 1.0638 1.6660 0.2170  -0.1030 0.0450  626 TRP A CE3 
326  C CZ2 . TRP A 41  ? 1.4144 1.0815 1.6431 0.2192  -0.1027 -0.0138 626 TRP A CZ2 
327  C CZ3 . TRP A 41  ? 1.4747 1.0493 1.6774 0.2073  -0.0940 0.0197  626 TRP A CZ3 
328  C CH2 . TRP A 41  ? 1.4304 1.0514 1.6570 0.2091  -0.0942 -0.0091 626 TRP A CH2 
329  N N   . GLU A 42  ? 1.0961 0.7961 1.1874 0.1990  -0.1151 0.0799  627 GLU A N   
330  C CA  . GLU A 42  ? 1.0542 0.8003 1.1397 0.1963  -0.1199 0.0738  627 GLU A CA  
331  C C   . GLU A 42  ? 1.0221 0.7627 1.0752 0.1787  -0.1107 0.0916  627 GLU A C   
332  O O   . GLU A 42  ? 0.9599 0.7003 1.0149 0.1564  -0.0957 0.0875  627 GLU A O   
333  C CB  . GLU A 42  ? 1.0049 0.7912 1.1211 0.1862  -0.1143 0.0453  627 GLU A CB  
334  C CG  . GLU A 42  ? 1.0107 0.8007 1.1605 0.2013  -0.1193 0.0262  627 GLU A CG  
335  C CD  . GLU A 42  ? 0.9374 0.7658 1.1137 0.1898  -0.1105 -0.0002 627 GLU A CD  
336  O OE1 . GLU A 42  ? 0.9047 0.7255 1.0827 0.1717  -0.0964 -0.0065 627 GLU A OE1 
337  O OE2 . GLU A 42  ? 0.9081 0.7748 1.1021 0.1980  -0.1174 -0.0142 627 GLU A OE2 
338  N N   . ARG A 43  ? 1.0342 0.7709 1.0574 0.1903  -0.1202 0.1106  628 ARG A N   
339  C CA  . ARG A 43  ? 1.0844 0.8108 1.0731 0.1771  -0.1113 0.1304  628 ARG A CA  
340  C C   . ARG A 43  ? 1.0094 0.7695 0.9784 0.1845  -0.1225 0.1315  628 ARG A C   
341  O O   . ARG A 43  ? 0.9864 0.7601 0.9569 0.2065  -0.1404 0.1286  628 ARG A O   
342  C CB  . ARG A 43  ? 1.1675 0.8409 1.1314 0.1832  -0.1081 0.1583  628 ARG A CB  
343  C CG  . ARG A 43  ? 1.2025 0.8387 1.1843 0.1712  -0.0945 0.1579  628 ARG A CG  
344  C CD  . ARG A 43  ? 1.3115 0.8908 1.2711 0.1782  -0.0913 0.1862  628 ARG A CD  
345  N NE  . ARG A 43  ? 1.3775 0.9459 1.2969 0.1708  -0.0834 0.2118  628 ARG A NE  
346  C CZ  . ARG A 43  ? 1.3916 0.9699 1.3045 0.1457  -0.0666 0.2129  628 ARG A CZ  
347  N NH1 . ARG A 43  ? 1.3170 0.9096 1.2597 0.1251  -0.0558 0.1924  628 ARG A NH1 
348  N NH2 . ARG A 43  ? 1.4565 1.0310 1.3324 0.1420  -0.0605 0.2342  628 ARG A NH2 
349  N N   . LEU A 44  ? 0.9208 0.6950 0.8727 0.1668  -0.1123 0.1342  629 LEU A N   
350  C CA  . LEU A 44  ? 0.9229 0.7242 0.8517 0.1721  -0.1210 0.1362  629 LEU A CA  
351  C C   . LEU A 44  ? 1.0150 0.7870 0.9004 0.1833  -0.1238 0.1648  629 LEU A C   
352  O O   . LEU A 44  ? 1.0276 0.7588 0.9020 0.1789  -0.1129 0.1834  629 LEU A O   
353  C CB  . LEU A 44  ? 0.8571 0.6825 0.7861 0.1493  -0.1080 0.1269  629 LEU A CB  
354  C CG  . LEU A 44  ? 0.7804 0.6322 0.7461 0.1368  -0.1030 0.1016  629 LEU A CG  
355  C CD1 . LEU A 44  ? 0.7176 0.5789 0.6792 0.1142  -0.0875 0.0987  629 LEU A CD1 
356  C CD2 . LEU A 44  ? 0.7704 0.6599 0.7543 0.1476  -0.1175 0.0826  629 LEU A CD2 
357  N N   . PRO A 45  ? 1.0531 0.8441 0.9117 0.1971  -0.1374 0.1692  630 PRO A N   
358  C CA  . PRO A 45  ? 1.1426 0.9065 0.9541 0.2090  -0.1395 0.1976  630 PRO A CA  
359  C C   . PRO A 45  ? 1.1791 0.9213 0.9661 0.1877  -0.1165 0.2152  630 PRO A C   
360  O O   . PRO A 45  ? 1.1604 0.9261 0.9549 0.1680  -0.1050 0.2034  630 PRO A O   
361  C CB  . PRO A 45  ? 1.1292 0.9291 0.9218 0.2246  -0.1584 0.1907  630 PRO A CB  
362  C CG  . PRO A 45  ? 1.0884 0.9303 0.9258 0.2251  -0.1692 0.1587  630 PRO A CG  
363  C CD  . PRO A 45  ? 1.0332 0.8723 0.9054 0.2018  -0.1508 0.1465  630 PRO A CD  
364  N N   . ASP A 46  ? 1.2379 0.9350 0.9968 0.1919  -0.1093 0.2437  631 ASP A N   
365  C CA  . ASP A 46  ? 1.2913 0.9637 1.0340 0.1702  -0.0847 0.2607  631 ASP A CA  
366  C C   . ASP A 46  ? 1.2766 0.9747 0.9884 0.1623  -0.0781 0.2633  631 ASP A C   
367  O O   . ASP A 46  ? 1.2932 1.0151 0.9823 0.1786  -0.0938 0.2609  631 ASP A O   
368  C CB  . ASP A 46  ? 1.3902 1.0075 1.1064 0.1780  -0.0787 0.2924  631 ASP A CB  
369  C CG  . ASP A 46  ? 1.4106 0.9932 1.1572 0.1823  -0.0804 0.2917  631 ASP A CG  
370  O OD1 . ASP A 46  ? 1.4765 1.0149 1.2008 0.1976  -0.0831 0.3165  631 ASP A OD1 
371  O OD2 . ASP A 46  ? 1.3256 0.9240 1.1160 0.1707  -0.0783 0.2670  631 ASP A OD2 
372  N N   . GLY A 47  ? 1.2417 0.9362 0.9542 0.1378  -0.0552 0.2668  632 GLY A N   
373  C CA  . GLY A 47  ? 1.2308 0.9490 0.9163 0.1297  -0.0464 0.2683  632 GLY A CA  
374  C C   . GLY A 47  ? 1.1988 0.9082 0.8894 0.1029  -0.0195 0.2741  632 GLY A C   
375  O O   . GLY A 47  ? 1.0818 0.7855 0.8095 0.0870  -0.0105 0.2638  632 GLY A O   
376  N N   . PRO A 48  ? 1.2741 0.9859 0.9287 0.0975  -0.0059 0.2887  633 PRO A N   
377  C CA  . PRO A 48  ? 1.2685 0.9774 0.9301 0.0722  0.0203  0.2928  633 PRO A CA  
378  C C   . PRO A 48  ? 1.1924 0.9412 0.8871 0.0562  0.0245  0.2651  633 PRO A C   
379  O O   . PRO A 48  ? 1.2193 0.9704 0.9269 0.0357  0.0444  0.2646  633 PRO A O   
380  C CB  . PRO A 48  ? 1.3415 1.0462 0.9512 0.0755  0.0314  0.3153  633 PRO A CB  
381  C CG  . PRO A 48  ? 1.3920 1.0874 0.9641 0.1043  0.0098  0.3275  633 PRO A CG  
382  C CD  . PRO A 48  ? 1.3344 1.0529 0.9392 0.1161  -0.0149 0.3015  633 PRO A CD  
383  N N   . GLN A 49  ? 1.0767 0.8565 0.7860 0.0658  0.0059  0.2422  634 GLN A N   
384  C CA  . GLN A 49  ? 0.9979 0.8144 0.7317 0.0544  0.0078  0.2176  634 GLN A CA  
385  C C   . GLN A 49  ? 0.8940 0.7129 0.6742 0.0452  0.0056  0.1994  634 GLN A C   
386  O O   . GLN A 49  ? 0.8063 0.6515 0.6084 0.0353  0.0080  0.1804  634 GLN A O   
387  C CB  . GLN A 49  ? 1.0119 0.8597 0.7312 0.0690  -0.0089 0.2041  634 GLN A CB  
388  C CG  . GLN A 49  ? 0.9887 0.8439 0.7254 0.0841  -0.0316 0.1906  634 GLN A CG  
389  C CD  . GLN A 49  ? 1.0710 0.9018 0.7864 0.1039  -0.0444 0.2077  634 GLN A CD  
390  O OE1 . GLN A 49  ? 1.1430 0.9520 0.8207 0.1098  -0.0389 0.2315  634 GLN A OE1 
391  N NE2 . GLN A 49  ? 1.0360 0.8704 0.7750 0.1153  -0.0615 0.1961  634 GLN A NE2 
392  N N   . ARG A 50  ? 0.8259 0.6171 0.6199 0.0493  0.0012  0.2050  635 ARG A N   
393  C CA  . ARG A 50  ? 0.7707 0.5659 0.6052 0.0441  -0.0032 0.1860  635 ARG A CA  
394  C C   . ARG A 50  ? 0.7575 0.5417 0.6153 0.0231  0.0140  0.1844  635 ARG A C   
395  O O   . ARG A 50  ? 0.7411 0.5043 0.5875 0.0134  0.0292  0.2013  635 ARG A O   
396  C CB  . ARG A 50  ? 0.7609 0.5350 0.6038 0.0596  -0.0171 0.1879  635 ARG A CB  
397  C CG  . ARG A 50  ? 0.7684 0.5597 0.6002 0.0809  -0.0375 0.1828  635 ARG A CG  
398  C CD  . ARG A 50  ? 0.7808 0.5530 0.6226 0.0979  -0.0513 0.1846  635 ARG A CD  
399  N NE  . ARG A 50  ? 0.7999 0.5938 0.6340 0.1183  -0.0716 0.1778  635 ARG A NE  
400  C CZ  . ARG A 50  ? 0.7848 0.6147 0.6407 0.1195  -0.0811 0.1543  635 ARG A CZ  
401  N NH1 . ARG A 50  ? 0.7790 0.6290 0.6281 0.1371  -0.0992 0.1484  635 ARG A NH1 
402  N NH2 . ARG A 50  ? 0.7152 0.5610 0.5998 0.1033  -0.0726 0.1367  635 ARG A NH2 
403  N N   . PHE A 51  ? 0.7072 0.5059 0.5985 0.0163  0.0114  0.1633  636 PHE A N   
404  C CA  . PHE A 51  ? 0.7027 0.4908 0.6209 -0.0003 0.0226  0.1575  636 PHE A CA  
405  C C   . PHE A 51  ? 0.7854 0.5342 0.7086 0.0039  0.0217  0.1678  636 PHE A C   
406  O O   . PHE A 51  ? 0.7889 0.5310 0.7140 0.0197  0.0078  0.1651  636 PHE A O   
407  C CB  . PHE A 51  ? 0.6950 0.5098 0.6413 -0.0050 0.0177  0.1325  636 PHE A CB  
408  C CG  . PHE A 51  ? 0.6773 0.5257 0.6205 -0.0107 0.0207  0.1234  636 PHE A CG  
409  C CD1 . PHE A 51  ? 0.7303 0.5889 0.6854 -0.0268 0.0333  0.1190  636 PHE A CD1 
410  C CD2 . PHE A 51  ? 0.6942 0.5640 0.6250 0.0001  0.0107  0.1181  636 PHE A CD2 
411  C CE1 . PHE A 51  ? 0.7024 0.5906 0.6560 -0.0300 0.0354  0.1101  636 PHE A CE1 
412  C CE2 . PHE A 51  ? 0.7054 0.6020 0.6342 -0.0044 0.0137  0.1094  636 PHE A CE2 
413  C CZ  . PHE A 51  ? 0.7069 0.6120 0.6462 -0.0187 0.0259  0.1060  636 PHE A CZ  
414  N N   . ASP A 52  ? 0.8272 0.5502 0.7541 -0.0101 0.0370  0.1792  637 ASP A N   
415  C CA  . ASP A 52  ? 0.9006 0.5797 0.8300 -0.0072 0.0385  0.1921  637 ASP A CA  
416  C C   . ASP A 52  ? 0.9459 0.6159 0.9132 -0.0201 0.0424  0.1750  637 ASP A C   
417  O O   . ASP A 52  ? 0.9206 0.5556 0.8966 -0.0158 0.0407  0.1792  637 ASP A O   
418  C CB  . ASP A 52  ? 0.9434 0.5920 0.8473 -0.0131 0.0538  0.2200  637 ASP A CB  
419  C CG  . ASP A 52  ? 0.9503 0.6045 0.8647 -0.0381 0.0752  0.2209  637 ASP A CG  
420  O OD1 . ASP A 52  ? 0.8807 0.5689 0.8187 -0.0496 0.0768  0.1996  637 ASP A OD1 
421  O OD2 . ASP A 52  ? 1.0195 0.6436 0.9189 -0.0459 0.0907  0.2434  637 ASP A OD2 
422  N N   . SER A 53  ? 0.9437 0.6438 0.9328 -0.0351 0.0473  0.1557  638 SER A N   
423  C CA  . SER A 53  ? 0.9734 0.6689 0.9970 -0.0474 0.0500  0.1372  638 SER A CA  
424  C C   . SER A 53  ? 0.9327 0.6637 0.9724 -0.0440 0.0391  0.1116  638 SER A C   
425  O O   . SER A 53  ? 0.9908 0.7158 1.0482 -0.0391 0.0317  0.0971  638 SER A O   
426  C CB  . SER A 53  ? 1.0147 0.7078 1.0531 -0.0707 0.0674  0.1379  638 SER A CB  
427  O OG  . SER A 53  ? 1.0753 0.7955 1.0999 -0.0775 0.0757  0.1437  638 SER A OG  
428  N N   . CYS A 54  ? 0.8199 0.5865 0.8526 -0.0464 0.0392  0.1063  639 CYS A N   
429  C CA  . CYS A 54  ? 0.7052 0.5039 0.7504 -0.0445 0.0312  0.0845  639 CYS A CA  
430  C C   . CYS A 54  ? 0.6029 0.4084 0.6374 -0.0261 0.0179  0.0828  639 CYS A C   
431  O O   . CYS A 54  ? 0.5548 0.3586 0.5674 -0.0160 0.0144  0.0965  639 CYS A O   
432  C CB  . CYS A 54  ? 0.7437 0.5742 0.7869 -0.0534 0.0365  0.0800  639 CYS A CB  
433  S SG  . CYS A 54  ? 0.8420 0.6734 0.9078 -0.0758 0.0510  0.0755  639 CYS A SG  
434  N N   . ILE A 55  ? 0.5040 0.3186 0.5548 -0.0222 0.0109  0.0647  640 ILE A N   
435  C CA  . ILE A 55  ? 0.4425 0.2659 0.4900 -0.0065 0.0000  0.0599  640 ILE A CA  
436  C C   . ILE A 55  ? 0.3746 0.2306 0.4132 -0.0062 -0.0020 0.0550  640 ILE A C   
437  O O   . ILE A 55  ? 0.3601 0.2354 0.4075 -0.0061 -0.0046 0.0402  640 ILE A O   
438  C CB  . ILE A 55  ? 0.4641 0.2840 0.5323 -0.0032 -0.0039 0.0426  640 ILE A CB  
439  C CG1 . ILE A 55  ? 0.5469 0.3309 0.6252 -0.0049 -0.0009 0.0470  640 ILE A CG1 
440  C CG2 . ILE A 55  ? 0.4806 0.3120 0.5495 0.0123  -0.0137 0.0365  640 ILE A CG2 
441  C CD1 . ILE A 55  ? 0.6131 0.3915 0.7127 -0.0022 -0.0039 0.0279  640 ILE A CD1 
442  N N   . ILE A 56  ? 0.3731 0.2329 0.3928 -0.0060 0.0000  0.0680  641 ILE A N   
443  C CA  . ILE A 56  ? 0.3606 0.2480 0.3723 -0.0073 -0.0003 0.0637  641 ILE A CA  
444  C C   . ILE A 56  ? 0.3498 0.2440 0.3458 0.0055  -0.0089 0.0689  641 ILE A C   
445  O O   . ILE A 56  ? 0.3599 0.2380 0.3415 0.0132  -0.0116 0.0828  641 ILE A O   
446  C CB  . ILE A 56  ? 0.3969 0.2888 0.4019 -0.0189 0.0100  0.0702  641 ILE A CB  
447  C CG1 . ILE A 56  ? 0.4449 0.3385 0.4700 -0.0321 0.0167  0.0603  641 ILE A CG1 
448  C CG2 . ILE A 56  ? 0.4120 0.3288 0.4057 -0.0174 0.0092  0.0675  641 ILE A CG2 
449  C CD1 . ILE A 56  ? 0.4327 0.3480 0.4691 -0.0324 0.0125  0.0427  641 ILE A CD1 
450  N N   . VAL A 57  ? 0.2903 0.2085 0.2877 0.0070  -0.0125 0.0582  642 VAL A N   
451  C CA  . VAL A 57  ? 0.2883 0.2181 0.2726 0.0162  -0.0199 0.0599  642 VAL A CA  
452  C C   . VAL A 57  ? 0.2365 0.1864 0.2164 0.0102  -0.0162 0.0540  642 VAL A C   
453  O O   . VAL A 57  ? 0.2244 0.1830 0.2157 0.0034  -0.0123 0.0445  642 VAL A O   
454  C CB  . VAL A 57  ? 0.3088 0.2456 0.3028 0.0276  -0.0308 0.0516  642 VAL A CB  
455  C CG1 . VAL A 57  ? 0.2909 0.2392 0.3046 0.0239  -0.0295 0.0365  642 VAL A CG1 
456  C CG2 . VAL A 57  ? 0.3479 0.3003 0.3311 0.0360  -0.0394 0.0505  642 VAL A CG2 
457  N N   . LEU A 58  ? 0.2367 0.1932 0.1981 0.0146  -0.0184 0.0594  643 LEU A N   
458  C CA  . LEU A 58  ? 0.2226 0.1969 0.1793 0.0113  -0.0160 0.0528  643 LEU A CA  
459  C C   . LEU A 58  ? 0.2147 0.2029 0.1764 0.0175  -0.0249 0.0416  643 LEU A C   
460  O O   . LEU A 58  ? 0.2288 0.2160 0.1919 0.0262  -0.0341 0.0411  643 LEU A O   
461  C CB  . LEU A 58  ? 0.2477 0.2219 0.1813 0.0119  -0.0118 0.0633  643 LEU A CB  
462  C CG  . LEU A 58  ? 0.2914 0.2522 0.2220 0.0035  -0.0002 0.0751  643 LEU A CG  
463  C CD1 . LEU A 58  ? 0.3401 0.3004 0.2447 0.0052  0.0049  0.0872  643 LEU A CD1 
464  C CD2 . LEU A 58  ? 0.3063 0.2752 0.2544 -0.0073 0.0074  0.0669  643 LEU A CD2 
465  N N   . GLY A 59  ? 0.2112 0.2118 0.1756 0.0133  -0.0222 0.0328  644 GLY A N   
466  C CA  . GLY A 59  ? 0.2110 0.2240 0.1814 0.0165  -0.0285 0.0214  644 GLY A CA  
467  C C   . GLY A 59  ? 0.2228 0.2455 0.1786 0.0186  -0.0298 0.0187  644 GLY A C   
468  O O   . GLY A 59  ? 0.2271 0.2497 0.1696 0.0165  -0.0237 0.0240  644 GLY A O   
469  N N   . SER A 60  ? 0.2310 0.2638 0.1924 0.0222  -0.0374 0.0079  645 SER A N   
470  C CA  A SER A 60  ? 0.2689 0.3119 0.2209 0.0238  -0.0395 0.0001  645 SER A CA  
471  C CA  B SER A 60  ? 0.2803 0.3233 0.2323 0.0238  -0.0395 0.0001  645 SER A CA  
472  C C   . SER A 60  ? 0.2934 0.3407 0.2635 0.0185  -0.0380 -0.0130 645 SER A C   
473  O O   . SER A 60  ? 0.2675 0.3134 0.2553 0.0157  -0.0379 -0.0165 645 SER A O   
474  C CB  A SER A 60  ? 0.3124 0.3638 0.2538 0.0331  -0.0512 -0.0026 645 SER A CB  
475  C CB  B SER A 60  ? 0.3565 0.4076 0.2972 0.0333  -0.0511 -0.0020 645 SER A CB  
476  O OG  A SER A 60  ? 0.2922 0.3543 0.2530 0.0335  -0.0588 -0.0176 645 SER A OG  
477  O OG  B SER A 60  ? 0.3959 0.4383 0.3240 0.0395  -0.0539 0.0119  645 SER A OG  
478  N N   . PRO A 61  ? 0.3163 0.3674 0.2828 0.0171  -0.0357 -0.0207 646 PRO A N   
479  C CA  . PRO A 61  ? 0.3065 0.3621 0.2528 0.0206  -0.0345 -0.0194 646 PRO A CA  
480  C C   . PRO A 61  ? 0.2405 0.2911 0.1795 0.0173  -0.0240 -0.0095 646 PRO A C   
481  O O   . PRO A 61  ? 0.2532 0.2979 0.2039 0.0123  -0.0184 -0.0072 646 PRO A O   
482  C CB  . PRO A 61  ? 0.3386 0.3980 0.2922 0.0191  -0.0348 -0.0347 646 PRO A CB  
483  C CG  . PRO A 61  ? 0.3519 0.4104 0.3280 0.0153  -0.0385 -0.0429 646 PRO A CG  
484  C CD  . PRO A 61  ? 0.3362 0.3861 0.3191 0.0118  -0.0331 -0.0315 646 PRO A CD  
485  N N   . SER A 62  ? 0.2361 0.2915 0.1553 0.0205  -0.0213 -0.0048 647 SER A N   
486  C CA  A SER A 62  ? 0.2415 0.2989 0.1557 0.0175  -0.0106 -0.0006 647 SER A CA  
487  C CA  B SER A 62  ? 0.2372 0.2942 0.1529 0.0171  -0.0105 -0.0007 647 SER A CA  
488  C C   . SER A 62  ? 0.2521 0.3158 0.1709 0.0188  -0.0096 -0.0144 647 SER A C   
489  O O   . SER A 62  ? 0.3697 0.4372 0.2863 0.0227  -0.0168 -0.0253 647 SER A O   
490  C CB  A SER A 62  ? 0.2688 0.3295 0.1599 0.0202  -0.0066 0.0093  647 SER A CB  
491  C CB  B SER A 62  ? 0.2761 0.3356 0.1714 0.0184  -0.0047 0.0100  647 SER A CB  
492  O OG  A SER A 62  ? 0.2907 0.3406 0.1781 0.0202  -0.0089 0.0223  647 SER A OG  
493  O OG  B SER A 62  ? 0.3010 0.3681 0.1762 0.0258  -0.0101 0.0057  647 SER A OG  
494  N N   . PHE A 63  ? 0.1970 0.2614 0.1243 0.0162  -0.0024 -0.0153 648 PHE A N   
495  C CA  . PHE A 63  ? 0.1814 0.2485 0.1137 0.0191  -0.0016 -0.0278 648 PHE A CA  
496  C C   . PHE A 63  ? 0.1790 0.2547 0.1116 0.0197  0.0073  -0.0270 648 PHE A C   
497  O O   . PHE A 63  ? 0.1918 0.2699 0.1276 0.0154  0.0130  -0.0174 648 PHE A O   
498  C CB  . PHE A 63  ? 0.1736 0.2294 0.1229 0.0172  -0.0047 -0.0328 648 PHE A CB  
499  C CG  . PHE A 63  ? 0.1766 0.2262 0.1362 0.0132  -0.0014 -0.0241 648 PHE A CG  
500  C CD1 . PHE A 63  ? 0.1923 0.2370 0.1550 0.0093  -0.0036 -0.0169 648 PHE A CD1 
501  C CD2 . PHE A 63  ? 0.2011 0.2520 0.1663 0.0145  0.0029  -0.0242 648 PHE A CD2 
502  C CE1 . PHE A 63  ? 0.1935 0.2336 0.1643 0.0059  -0.0012 -0.0110 648 PHE A CE1 
503  C CE2 . PHE A 63  ? 0.1950 0.2424 0.1679 0.0116  0.0041  -0.0180 648 PHE A CE2 
504  C CZ  . PHE A 63  ? 0.2130 0.2553 0.1879 0.0069  0.0024  -0.0117 648 PHE A CZ  
505  N N   . LEU A 64  ? 0.1796 0.2606 0.1118 0.0249  0.0085  -0.0385 649 LEU A N   
506  C CA  . LEU A 64  ? 0.2031 0.2958 0.1386 0.0271  0.0169  -0.0403 649 LEU A CA  
507  C C   . LEU A 64  ? 0.1833 0.2726 0.1299 0.0333  0.0156  -0.0524 649 LEU A C   
508  O O   . LEU A 64  ? 0.1941 0.2951 0.1418 0.0385  0.0208  -0.0594 649 LEU A O   
509  C CB  . LEU A 64  ? 0.2571 0.3653 0.1760 0.0284  0.0242  -0.0397 649 LEU A CB  
510  C CG  . LEU A 64  ? 0.2688 0.3802 0.1718 0.0346  0.0201  -0.0511 649 LEU A CG  
511  C CD1 . LEU A 64  ? 0.3022 0.4318 0.1941 0.0395  0.0296  -0.0581 649 LEU A CD1 
512  C CD2 . LEU A 64  ? 0.3123 0.4194 0.1982 0.0333  0.0137  -0.0437 649 LEU A CD2 
513  N N   . SER A 65  ? 0.1692 0.2414 0.1250 0.0327  0.0095  -0.0535 650 SER A N   
514  C CA  . SER A 65  ? 0.1705 0.2327 0.1350 0.0390  0.0079  -0.0634 650 SER A CA  
515  C C   . SER A 65  ? 0.1636 0.2059 0.1364 0.0355  0.0041  -0.0581 650 SER A C   
516  O O   . SER A 65  ? 0.1750 0.2132 0.1468 0.0289  0.0018  -0.0522 650 SER A O   
517  C CB  . SER A 65  ? 0.1774 0.2387 0.1365 0.0428  0.0057  -0.0777 650 SER A CB  
518  O OG  . SER A 65  ? 0.1731 0.2262 0.1302 0.0375  -0.0003 -0.0792 650 SER A OG  
519  N N   . GLY A 66  ? 0.1891 0.2193 0.1690 0.0415  0.0041  -0.0613 651 GLY A N   
520  C CA  . GLY A 66  ? 0.2028 0.2100 0.1877 0.0393  0.0023  -0.0578 651 GLY A CA  
521  C C   . GLY A 66  ? 0.1985 0.2022 0.1840 0.0359  0.0025  -0.0447 651 GLY A C   
522  O O   . GLY A 66  ? 0.2135 0.2320 0.1981 0.0354  0.0031  -0.0389 651 GLY A O   
523  N N   . ARG A 67  ? 0.1714 0.1567 0.1585 0.0315  0.0027  -0.0409 652 ARG A N   
524  C CA  . ARG A 67  ? 0.1691 0.1483 0.1547 0.0281  0.0036  -0.0302 652 ARG A CA  
525  C C   . ARG A 67  ? 0.1733 0.1524 0.1617 0.0182  0.0041  -0.0291 652 ARG A C   
526  O O   . ARG A 67  ? 0.1919 0.1641 0.1858 0.0143  0.0042  -0.0362 652 ARG A O   
527  C CB  . ARG A 67  ? 0.1917 0.1478 0.1752 0.0329  0.0054  -0.0259 652 ARG A CB  
528  C CG  . ARG A 67  ? 0.2119 0.1716 0.1926 0.0451  0.0029  -0.0249 652 ARG A CG  
529  C CD  . ARG A 67  ? 0.2521 0.1861 0.2279 0.0536  0.0034  -0.0202 652 ARG A CD  
530  N NE  . ARG A 67  ? 0.2696 0.1868 0.2504 0.0561  0.0049  -0.0286 652 ARG A NE  
531  C CZ  . ARG A 67  ? 0.3086 0.1955 0.2868 0.0601  0.0074  -0.0249 652 ARG A CZ  
532  N NH1 . ARG A 67  ? 0.3237 0.1949 0.2907 0.0625  0.0089  -0.0111 652 ARG A NH1 
533  N NH2 . ARG A 67  ? 0.3413 0.2128 0.3266 0.0610  0.0088  -0.0345 652 ARG A NH2 
534  N N   . ARG A 68  ? 0.1569 0.1451 0.1439 0.0147  0.0038  -0.0225 653 ARG A N   
535  C CA  . ARG A 68  ? 0.1638 0.1559 0.1549 0.0074  0.0031  -0.0223 653 ARG A CA  
536  C C   . ARG A 68  ? 0.1666 0.1557 0.1570 0.0047  0.0053  -0.0147 653 ARG A C   
537  O O   . ARG A 68  ? 0.1747 0.1699 0.1610 0.0073  0.0046  -0.0104 653 ARG A O   
538  C CB  . ARG A 68  ? 0.1619 0.1702 0.1507 0.0070  0.0000  -0.0231 653 ARG A CB  
539  C CG  . ARG A 68  ? 0.2007 0.2169 0.1849 0.0111  -0.0013 -0.0298 653 ARG A CG  
540  C CD  . ARG A 68  ? 0.1826 0.1972 0.1690 0.0106  -0.0043 -0.0400 653 ARG A CD  
541  N NE  . ARG A 68  ? 0.1709 0.1929 0.1508 0.0160  -0.0050 -0.0482 653 ARG A NE  
542  C CZ  . ARG A 68  ? 0.1740 0.2038 0.1492 0.0174  -0.0090 -0.0575 653 ARG A CZ  
543  N NH1 . ARG A 68  ? 0.1892 0.2224 0.1665 0.0141  -0.0143 -0.0598 653 ARG A NH1 
544  N NH2 . ARG A 68  ? 0.1801 0.2153 0.1493 0.0229  -0.0081 -0.0656 653 ARG A NH2 
545  N N   . TYR A 69  ? 0.1506 0.1334 0.1466 -0.0008 0.0080  -0.0149 654 TYR A N   
546  C CA  . TYR A 69  ? 0.1507 0.1314 0.1453 -0.0032 0.0113  -0.0094 654 TYR A CA  
547  C C   . TYR A 69  ? 0.1419 0.1304 0.1466 -0.0085 0.0108  -0.0125 654 TYR A C   
548  O O   . TYR A 69  ? 0.1407 0.1301 0.1553 -0.0119 0.0104  -0.0187 654 TYR A O   
549  C CB  . TYR A 69  ? 0.1679 0.1317 0.1583 -0.0038 0.0180  -0.0055 654 TYR A CB  
550  C CG  . TYR A 69  ? 0.1737 0.1365 0.1598 -0.0061 0.0227  -0.0006 654 TYR A CG  
551  C CD1 . TYR A 69  ? 0.1849 0.1496 0.1586 -0.0006 0.0210  0.0043  654 TYR A CD1 
552  C CD2 . TYR A 69  ? 0.1826 0.1451 0.1781 -0.0133 0.0287  -0.0027 654 TYR A CD2 
553  C CE1 . TYR A 69  ? 0.2038 0.1680 0.1713 -0.0019 0.0253  0.0071  654 TYR A CE1 
554  C CE2 . TYR A 69  ? 0.1986 0.1625 0.1900 -0.0149 0.0341  0.0002  654 TYR A CE2 
555  C CZ  . TYR A 69  ? 0.2026 0.1663 0.1782 -0.0089 0.0323  0.0053  654 TYR A CZ  
556  O OH  . TYR A 69  ? 0.2267 0.1917 0.1951 -0.0096 0.0378  0.0070  654 TYR A OH  
557  N N   . TRP A 70  ? 0.1334 0.1273 0.1375 -0.0087 0.0105  -0.0095 655 TRP A N   
558  C CA  . TRP A 70  ? 0.1271 0.1269 0.1421 -0.0121 0.0108  -0.0126 655 TRP A CA  
559  C C   . TRP A 70  ? 0.1393 0.1384 0.1515 -0.0125 0.0148  -0.0100 655 TRP A C   
560  O O   . TRP A 70  ? 0.1498 0.1468 0.1514 -0.0097 0.0146  -0.0063 655 TRP A O   
561  C CB  . TRP A 70  ? 0.1243 0.1337 0.1436 -0.0102 0.0033  -0.0148 655 TRP A CB  
562  C CG  . TRP A 70  ? 0.1287 0.1404 0.1408 -0.0075 0.0003  -0.0098 655 TRP A CG  
563  C CD1 . TRP A 70  ? 0.1327 0.1456 0.1474 -0.0073 -0.0007 -0.0078 655 TRP A CD1 
564  C CD2 . TRP A 70  ? 0.1236 0.1366 0.1269 -0.0054 -0.0008 -0.0069 655 TRP A CD2 
565  N NE1 . TRP A 70  ? 0.1394 0.1526 0.1478 -0.0065 -0.0020 -0.0034 655 TRP A NE1 
566  C CE2 . TRP A 70  ? 0.1249 0.1400 0.1267 -0.0056 -0.0017 -0.0028 655 TRP A CE2 
567  C CE3 . TRP A 70  ? 0.1492 0.1620 0.1472 -0.0034 -0.0005 -0.0085 655 TRP A CE3 
568  C CZ2 . TRP A 70  ? 0.1437 0.1628 0.1406 -0.0053 -0.0011 0.0000  655 TRP A CZ2 
569  C CZ3 . TRP A 70  ? 0.1609 0.1792 0.1532 -0.0014 -0.0007 -0.0063 655 TRP A CZ3 
570  C CH2 . TRP A 70  ? 0.1571 0.1793 0.1493 -0.0030 -0.0004 -0.0018 655 TRP A CH2 
571  N N   . GLU A 71  ? 0.1438 0.1477 0.1671 -0.0151 0.0172  -0.0138 656 GLU A N   
572  C CA  . GLU A 71  ? 0.1474 0.1518 0.1689 -0.0153 0.0223  -0.0137 656 GLU A CA  
573  C C   . GLU A 71  ? 0.1472 0.1604 0.1817 -0.0141 0.0185  -0.0186 656 GLU A C   
574  O O   . GLU A 71  ? 0.1496 0.1693 0.1977 -0.0143 0.0153  -0.0227 656 GLU A O   
575  C CB  . GLU A 71  ? 0.2242 0.2250 0.2475 -0.0199 0.0331  -0.0143 656 GLU A CB  
576  C CG  . GLU A 71  ? 0.2809 0.2681 0.2881 -0.0199 0.0384  -0.0075 656 GLU A CG  
577  C CD  . GLU A 71  ? 0.2138 0.1945 0.2190 -0.0250 0.0519  -0.0054 656 GLU A CD  
578  O OE1 . GLU A 71  ? 0.3064 0.2941 0.3237 -0.0300 0.0597  -0.0098 656 GLU A OE1 
579  O OE2 . GLU A 71  ? 0.2786 0.2461 0.2681 -0.0229 0.0542  0.0017  656 GLU A OE2 
580  N N   . VAL A 72  ? 0.1362 0.1495 0.1671 -0.0120 0.0188  -0.0191 657 VAL A N   
581  C CA  . VAL A 72  ? 0.1351 0.1528 0.1775 -0.0093 0.0151  -0.0235 657 VAL A CA  
582  C C   . VAL A 72  ? 0.1465 0.1665 0.1898 -0.0091 0.0217  -0.0289 657 VAL A C   
583  O O   . VAL A 72  ? 0.1547 0.1713 0.1844 -0.0091 0.0241  -0.0280 657 VAL A O   
584  C CB  . VAL A 72  ? 0.1432 0.1564 0.1820 -0.0069 0.0077  -0.0199 657 VAL A CB  
585  C CG1 . VAL A 72  ? 0.1565 0.1694 0.2072 -0.0030 0.0035  -0.0229 657 VAL A CG1 
586  C CG2 . VAL A 72  ? 0.1602 0.1722 0.1935 -0.0071 0.0033  -0.0143 657 VAL A CG2 
587  N N   . GLU A 73  ? 0.1492 0.1769 0.2088 -0.0079 0.0238  -0.0357 658 GLU A N   
588  C CA  . GLU A 73  ? 0.1680 0.1996 0.2295 -0.0066 0.0303  -0.0428 658 GLU A CA  
589  C C   . GLU A 73  ? 0.1651 0.1914 0.2278 -0.0019 0.0233  -0.0456 658 GLU A C   
590  O O   . GLU A 73  ? 0.1500 0.1735 0.2230 0.0016  0.0153  -0.0446 658 GLU A O   
591  C CB  . GLU A 73  ? 0.1907 0.2348 0.2733 -0.0063 0.0352  -0.0508 658 GLU A CB  
592  C CG  . GLU A 73  ? 0.2757 0.3249 0.3615 -0.0133 0.0445  -0.0497 658 GLU A CG  
593  C CD  . GLU A 73  ? 0.4575 0.5224 0.5645 -0.0153 0.0543  -0.0593 658 GLU A CD  
594  O OE1 . GLU A 73  ? 0.4408 0.5148 0.5639 -0.0089 0.0505  -0.0679 658 GLU A OE1 
595  O OE2 . GLU A 73  ? 0.5314 0.5985 0.6390 -0.0232 0.0665  -0.0582 658 GLU A OE2 
596  N N   . VAL A 74  ? 0.1577 0.1814 0.2084 -0.0018 0.0259  -0.0489 659 VAL A N   
597  C CA  . VAL A 74  ? 0.1447 0.1628 0.1987 0.0010  0.0208  -0.0546 659 VAL A CA  
598  C C   . VAL A 74  ? 0.1548 0.1786 0.2145 0.0044  0.0265  -0.0671 659 VAL A C   
599  O O   . VAL A 74  ? 0.1580 0.1766 0.2262 0.0078  0.0227  -0.0747 659 VAL A O   
600  C CB  . VAL A 74  ? 0.1580 0.1710 0.1976 -0.0013 0.0170  -0.0524 659 VAL A CB  
601  C CG1 . VAL A 74  ? 0.1577 0.1665 0.1951 -0.0039 0.0119  -0.0417 659 VAL A CG1 
602  C CG2 . VAL A 74  ? 0.1679 0.1864 0.1890 -0.0016 0.0225  -0.0547 659 VAL A CG2 
603  N N   . GLY A 75  ? 0.1657 0.1991 0.2195 0.0031  0.0369  -0.0695 660 GLY A N   
604  C CA  . GLY A 75  ? 0.1758 0.2177 0.2341 0.0064  0.0447  -0.0819 660 GLY A CA  
605  C C   . GLY A 75  ? 0.1848 0.2230 0.2348 0.0095  0.0418  -0.0918 660 GLY A C   
606  O O   . GLY A 75  ? 0.1858 0.2199 0.2175 0.0077  0.0384  -0.0895 660 GLY A O   
607  N N   . ASP A 76  ? 0.1872 0.2273 0.2528 0.0148  0.0422  -0.1049 661 ASP A N   
608  C CA  . ASP A 76  ? 0.2094 0.2471 0.2707 0.0180  0.0406  -0.1188 661 ASP A CA  
609  C C   . ASP A 76  ? 0.1975 0.2191 0.2729 0.0190  0.0290  -0.1203 661 ASP A C   
610  O O   . ASP A 76  ? 0.2287 0.2448 0.3100 0.0221  0.0267  -0.1340 661 ASP A O   
611  C CB  . ASP A 76  ? 0.2251 0.2748 0.2944 0.0236  0.0504  -0.1342 661 ASP A CB  
612  C CG  . ASP A 76  ? 0.2607 0.3260 0.3154 0.0212  0.0654  -0.1324 661 ASP A CG  
613  O OD1 . ASP A 76  ? 0.2898 0.3535 0.3214 0.0164  0.0674  -0.1210 661 ASP A OD1 
614  O OD2 . ASP A 76  ? 0.2625 0.3410 0.3311 0.0240  0.0756  -0.1410 661 ASP A OD2 
615  N N   . LYS A 77  ? 0.1948 0.2075 0.2737 0.0157  0.0225  -0.1056 662 LYS A N   
616  C CA  . LYS A 77  ? 0.1893 0.1845 0.2790 0.0154  0.0137  -0.1038 662 LYS A CA  
617  C C   . LYS A 77  ? 0.2093 0.2003 0.2909 0.0107  0.0106  -0.1111 662 LYS A C   
618  O O   . LYS A 77  ? 0.2298 0.2318 0.2937 0.0081  0.0127  -0.1120 662 LYS A O   
619  C CB  . LYS A 77  ? 0.1805 0.1695 0.2700 0.0123  0.0090  -0.0864 662 LYS A CB  
620  C CG  . LYS A 77  ? 0.1756 0.1677 0.2775 0.0181  0.0084  -0.0815 662 LYS A CG  
621  C CD  . LYS A 77  ? 0.1747 0.1627 0.2734 0.0162  0.0033  -0.0660 662 LYS A CD  
622  C CE  . LYS A 77  ? 0.1812 0.1502 0.2802 0.0150  -0.0028 -0.0579 662 LYS A CE  
623  N NZ  . LYS A 77  ? 0.1867 0.1401 0.2995 0.0216  -0.0064 -0.0616 662 LYS A NZ  
624  N N   . THR A 78  ? 0.2120 0.1868 0.3070 0.0098  0.0054  -0.1154 663 THR A N   
625  C CA  . THR A 78  ? 0.2342 0.2053 0.3285 0.0042  0.0019  -0.1256 663 THR A CA  
626  C C   . THR A 78  ? 0.2297 0.1918 0.3265 -0.0042 -0.0022 -0.1134 663 THR A C   
627  O O   . THR A 78  ? 0.2350 0.1984 0.3334 -0.0104 -0.0052 -0.1218 663 THR A O   
628  C CB  . THR A 78  ? 0.2564 0.2145 0.3671 0.0073  0.0005  -0.1425 663 THR A CB  
629  O OG1 . THR A 78  ? 0.2626 0.1983 0.3902 0.0087  -0.0018 -0.1335 663 THR A OG1 
630  C CG2 . THR A 78  ? 0.2687 0.2377 0.3782 0.0160  0.0056  -0.1581 663 THR A CG2 
631  N N   . ALA A 79  ? 0.2075 0.1620 0.3062 -0.0044 -0.0024 -0.0959 664 ALA A N   
632  C CA  . ALA A 79  ? 0.2105 0.1587 0.3096 -0.0125 -0.0042 -0.0842 664 ALA A CA  
633  C C   . ALA A 79  ? 0.2081 0.1577 0.2997 -0.0105 -0.0036 -0.0662 664 ALA A C   
634  O O   . ALA A 79  ? 0.2107 0.1567 0.3049 -0.0032 -0.0038 -0.0620 664 ALA A O   
635  C CB  . ALA A 79  ? 0.2229 0.1488 0.3381 -0.0168 -0.0052 -0.0850 664 ALA A CB  
636  N N   . TRP A 80  ? 0.1858 0.1430 0.2692 -0.0161 -0.0035 -0.0579 665 TRP A N   
637  C CA  . TRP A 80  ? 0.1728 0.1320 0.2481 -0.0149 -0.0032 -0.0426 665 TRP A CA  
638  C C   . TRP A 80  ? 0.1722 0.1389 0.2420 -0.0217 -0.0025 -0.0368 665 TRP A C   
639  O O   . TRP A 80  ? 0.1716 0.1457 0.2438 -0.0265 -0.0031 -0.0451 665 TRP A O   
640  C CB  . TRP A 80  ? 0.1605 0.1320 0.2278 -0.0088 -0.0020 -0.0424 665 TRP A CB  
641  C CG  . TRP A 80  ? 0.1716 0.1567 0.2303 -0.0088 0.0002  -0.0515 665 TRP A CG  
642  C CD1 . TRP A 80  ? 0.1938 0.1830 0.2531 -0.0049 0.0027  -0.0628 665 TRP A CD1 
643  C CD2 . TRP A 80  ? 0.1641 0.1600 0.2099 -0.0111 0.0005  -0.0494 665 TRP A CD2 
644  N NE1 . TRP A 80  ? 0.1865 0.1875 0.2311 -0.0050 0.0051  -0.0661 665 TRP A NE1 
645  C CE2 . TRP A 80  ? 0.1805 0.1848 0.2169 -0.0083 0.0028  -0.0583 665 TRP A CE2 
646  C CE3 . TRP A 80  ? 0.1696 0.1690 0.2107 -0.0145 -0.0009 -0.0415 665 TRP A CE3 
647  C CZ2 . TRP A 80  ? 0.1764 0.1899 0.1973 -0.0076 0.0027  -0.0571 665 TRP A CZ2 
648  C CZ3 . TRP A 80  ? 0.1744 0.1845 0.2037 -0.0136 -0.0013 -0.0424 665 TRP A CZ3 
649  C CH2 . TRP A 80  ? 0.1806 0.1964 0.1991 -0.0098 -0.0001 -0.0494 665 TRP A CH2 
650  N N   . ILE A 81  ? 0.1623 0.1275 0.2263 -0.0217 -0.0019 -0.0236 666 ILE A N   
651  C CA  . ILE A 81  ? 0.1636 0.1391 0.2214 -0.0262 -0.0005 -0.0182 666 ILE A CA  
652  C C   . ILE A 81  ? 0.1525 0.1357 0.1985 -0.0211 -0.0009 -0.0116 666 ILE A C   
653  O O   . ILE A 81  ? 0.1615 0.1387 0.2056 -0.0166 -0.0022 -0.0060 666 ILE A O   
654  C CB  . ILE A 81  ? 0.1893 0.1547 0.2516 -0.0325 0.0025  -0.0093 666 ILE A CB  
655  C CG1 . ILE A 81  ? 0.2149 0.1684 0.2926 -0.0392 0.0038  -0.0160 666 ILE A CG1 
656  C CG2 . ILE A 81  ? 0.2036 0.1832 0.2615 -0.0366 0.0050  -0.0056 666 ILE A CG2 
657  C CD1 . ILE A 81  ? 0.2367 0.1747 0.3191 -0.0465 0.0092  -0.0051 666 ILE A CD1 
658  N N   . LEU A 82  ? 0.1377 0.1335 0.1769 -0.0214 -0.0005 -0.0126 667 LEU A N   
659  C CA  . LEU A 82  ? 0.1407 0.1418 0.1703 -0.0177 -0.0005 -0.0076 667 LEU A CA  
660  C C   . LEU A 82  ? 0.1468 0.1574 0.1724 -0.0194 0.0004  -0.0056 667 LEU A C   
661  O O   . LEU A 82  ? 0.1467 0.1649 0.1748 -0.0209 -0.0001 -0.0109 667 LEU A O   
662  C CB  . LEU A 82  ? 0.1447 0.1496 0.1696 -0.0138 -0.0001 -0.0124 667 LEU A CB  
663  C CG  . LEU A 82  ? 0.1607 0.1613 0.1910 -0.0111 0.0003  -0.0160 667 LEU A CG  
664  C CD1 . LEU A 82  ? 0.1616 0.1672 0.1865 -0.0092 0.0037  -0.0206 667 LEU A CD1 
665  C CD2 . LEU A 82  ? 0.1635 0.1610 0.1967 -0.0085 -0.0016 -0.0106 667 LEU A CD2 
666  N N   . GLY A 83  ? 0.1401 0.1520 0.1596 -0.0178 0.0011  0.0004  668 GLY A N   
667  C CA  . GLY A 83  ? 0.1305 0.1525 0.1461 -0.0171 0.0020  0.0004  668 GLY A CA  
668  C C   . GLY A 83  ? 0.1277 0.1501 0.1370 -0.0161 0.0035  0.0063  668 GLY A C   
669  O O   . GLY A 83  ? 0.1367 0.1539 0.1413 -0.0131 0.0015  0.0084  668 GLY A O   
670  N N   . ALA A 84  ? 0.1312 0.1622 0.1411 -0.0182 0.0067  0.0073  669 ALA A N   
671  C CA  . ALA A 84  ? 0.1391 0.1728 0.1403 -0.0168 0.0092  0.0120  669 ALA A CA  
672  C C   . ALA A 84  ? 0.1532 0.1917 0.1575 -0.0228 0.0158  0.0162  669 ALA A C   
673  O O   . ALA A 84  ? 0.1460 0.1901 0.1629 -0.0282 0.0181  0.0129  669 ALA A O   
674  C CB  . ALA A 84  ? 0.1349 0.1764 0.1318 -0.0114 0.0083  0.0071  669 ALA A CB  
675  N N   . CYS A 85  ? 0.1524 0.1907 0.1453 -0.0222 0.0194  0.0227  670 CYS A N   
676  C CA  . CYS A 85  ? 0.1817 0.2242 0.1751 -0.0285 0.0285  0.0284  670 CYS A CA  
677  C C   . CYS A 85  ? 0.1870 0.2373 0.1647 -0.0248 0.0327  0.0312  670 CYS A C   
678  O O   . CYS A 85  ? 0.1804 0.2290 0.1459 -0.0173 0.0269  0.0294  670 CYS A O   
679  C CB  . CYS A 85  ? 0.1964 0.2216 0.1893 -0.0335 0.0307  0.0380  670 CYS A CB  
680  S SG  . CYS A 85  ? 0.2455 0.2548 0.2170 -0.0254 0.0252  0.0482  670 CYS A SG  
681  N N   A LYS A 86  ? 0.1881 0.2480 0.1673 -0.0307 0.0435  0.0344  671 LYS A N   
682  N N   B LYS A 86  ? 0.1885 0.2490 0.1681 -0.0305 0.0433  0.0339  671 LYS A N   
683  C CA  A LYS A 86  ? 0.2121 0.2795 0.1733 -0.0278 0.0500  0.0380  671 LYS A CA  
684  C CA  B LYS A 86  ? 0.2151 0.2822 0.1762 -0.0276 0.0496  0.0379  671 LYS A CA  
685  C C   A LYS A 86  ? 0.2439 0.2942 0.1828 -0.0252 0.0486  0.0508  671 LYS A C   
686  C C   B LYS A 86  ? 0.2398 0.2894 0.1795 -0.0243 0.0468  0.0498  671 LYS A C   
687  O O   A LYS A 86  ? 0.2493 0.2836 0.1890 -0.0303 0.0509  0.0612  671 LYS A O   
688  O O   B LYS A 86  ? 0.2443 0.2772 0.1864 -0.0281 0.0461  0.0582  671 LYS A O   
689  C CB  A LYS A 86  ? 0.2351 0.3189 0.2062 -0.0360 0.0641  0.0381  671 LYS A CB  
690  C CB  B LYS A 86  ? 0.2484 0.3287 0.2166 -0.0364 0.0644  0.0406  671 LYS A CB  
691  C CG  A LYS A 86  ? 0.2334 0.3381 0.2265 -0.0351 0.0632  0.0238  671 LYS A CG  
692  C CG  B LYS A 86  ? 0.2547 0.3581 0.2436 -0.0367 0.0664  0.0273  671 LYS A CG  
693  C CD  A LYS A 86  ? 0.2566 0.3837 0.2675 -0.0428 0.0759  0.0199  671 LYS A CD  
694  C CD  B LYS A 86  ? 0.3012 0.4232 0.2974 -0.0444 0.0823  0.0280  671 LYS A CD  
695  C CE  A LYS A 86  ? 0.2971 0.4418 0.2975 -0.0368 0.0830  0.0156  671 LYS A CE  
696  C CE  B LYS A 86  ? 0.3260 0.4469 0.3422 -0.0585 0.0908  0.0320  671 LYS A CE  
697  N NZ  A LYS A 86  ? 0.2733 0.4468 0.2956 -0.0395 0.0924  0.0057  671 LYS A NZ  
698  N NZ  B LYS A 86  ? 0.3479 0.4864 0.3685 -0.0669 0.1090  0.0344  671 LYS A NZ  
699  N N   . THR A 87  ? 0.2552 0.3088 0.1733 -0.0165 0.0448  0.0500  672 THR A N   
700  C CA  . THR A 87  ? 0.3006 0.3402 0.1955 -0.0113 0.0410  0.0615  672 THR A CA  
701  C C   . THR A 87  ? 0.3785 0.4098 0.2596 -0.0172 0.0539  0.0781  672 THR A C   
702  O O   . THR A 87  ? 0.4303 0.4435 0.2949 -0.0139 0.0512  0.0913  672 THR A O   
703  C CB  . THR A 87  ? 0.3232 0.3720 0.1992 -0.0009 0.0339  0.0546  672 THR A CB  
704  O OG1 . THR A 87  ? 0.3490 0.4143 0.2188 -0.0025 0.0452  0.0511  672 THR A OG1 
705  C CG2 . THR A 87  ? 0.3006 0.3533 0.1905 0.0035  0.0224  0.0397  672 THR A CG2 
706  N N   . SER A 88  ? 0.3957 0.4383 0.2854 -0.0265 0.0685  0.0784  673 SER A N   
707  C CA  . SER A 88  ? 0.4761 0.5097 0.3562 -0.0352 0.0841  0.0946  673 SER A CA  
708  C C   . SER A 88  ? 0.5019 0.5175 0.4028 -0.0467 0.0886  0.1018  673 SER A C   
709  O O   . SER A 88  ? 0.5453 0.5535 0.4444 -0.0570 0.1039  0.1140  673 SER A O   
710  C CB  . SER A 88  ? 0.4839 0.5408 0.3670 -0.0413 0.1001  0.0905  673 SER A CB  
711  O OG  . SER A 88  ? 0.4930 0.5674 0.4088 -0.0448 0.0975  0.0737  673 SER A OG  
712  N N   . ILE A 89  ? 0.5170 0.5252 0.4382 -0.0464 0.0772  0.0941  674 ILE A N   
713  C CA  . ILE A 89  ? 0.5623 0.5537 0.5031 -0.0571 0.0815  0.0985  674 ILE A CA  
714  C C   . ILE A 89  ? 0.6020 0.5637 0.5233 -0.0579 0.0869  0.1194  674 ILE A C   
715  O O   . ILE A 89  ? 0.6197 0.5695 0.5149 -0.0458 0.0790  0.1285  674 ILE A O   
716  C CB  . ILE A 89  ? 0.6448 0.6341 0.6049 -0.0535 0.0669  0.0857  674 ILE A CB  
717  C CG1 . ILE A 89  ? 0.6130 0.6266 0.5976 -0.0585 0.0675  0.0692  674 ILE A CG1 
718  C CG2 . ILE A 89  ? 0.7371 0.6999 0.7063 -0.0575 0.0654  0.0920  674 ILE A CG2 
719  C CD1 . ILE A 89  ? 0.6987 0.7170 0.6915 -0.0507 0.0533  0.0562  674 ILE A CD1 
720  N N   . SER A 90  ? 0.6849 0.6336 0.6194 -0.0721 0.1006  0.1273  675 SER A N   
721  C CA  . SER A 90  ? 0.7256 0.6396 0.6434 -0.0728 0.1057  0.1482  675 SER A CA  
722  C C   . SER A 90  ? 0.7136 0.6060 0.6394 -0.0650 0.0900  0.1457  675 SER A C   
723  O O   . SER A 90  ? 0.6532 0.5535 0.6067 -0.0682 0.0830  0.1292  675 SER A O   
724  C CB  . SER A 90  ? 0.7671 0.6700 0.6996 -0.0915 0.1257  0.1570  675 SER A CB  
725  O OG  . SER A 90  ? 0.8229 0.6882 0.7331 -0.0905 0.1315  0.1804  675 SER A OG  
726  N N   . ARG A 91  ? 0.7953 0.6618 0.6957 -0.0537 0.0844  0.1619  676 ARG A N   
727  C CA  . ARG A 91  ? 0.8810 0.7281 0.7876 -0.0436 0.0694  0.1600  676 ARG A CA  
728  C C   . ARG A 91  ? 0.9220 0.7305 0.8342 -0.0498 0.0765  0.1740  676 ARG A C   
729  O O   . ARG A 91  ? 0.8444 0.6364 0.7711 -0.0448 0.0666  0.1687  676 ARG A O   
730  C CB  . ARG A 91  ? 0.9437 0.7914 0.8211 -0.0238 0.0550  0.1655  676 ARG A CB  
731  C CG  . ARG A 91  ? 0.8995 0.7816 0.7693 -0.0187 0.0498  0.1527  676 ARG A CG  
732  C CD  . ARG A 91  ? 0.8681 0.7530 0.7192 -0.0002 0.0324  0.1520  676 ARG A CD  
733  N NE  . ARG A 91  ? 0.7731 0.6889 0.6221 0.0036  0.0266  0.1366  676 ARG A NE  
734  C CZ  . ARG A 91  ? 0.7897 0.7153 0.6144 0.0163  0.0174  0.1369  676 ARG A CZ  
735  N NH1 . ARG A 91  ? 0.8300 0.7393 0.6309 0.0290  0.0097  0.1508  676 ARG A NH1 
736  N NH2 . ARG A 91  ? 0.7231 0.6746 0.5480 0.0173  0.0148  0.1222  676 ARG A NH2 
737  N N   . LYS A 92  ? 1.0040 0.7972 0.9046 -0.0604 0.0945  0.1917  677 LYS A N   
738  C CA  . LYS A 92  ? 1.1294 0.8825 1.0366 -0.0689 0.1042  0.2062  677 LYS A CA  
739  C C   . LYS A 92  ? 1.2190 0.9795 1.1653 -0.0917 0.1174  0.1929  677 LYS A C   
740  O O   . LYS A 92  ? 1.3291 1.0984 1.2774 -0.1067 0.1357  0.1982  677 LYS A O   
741  C CB  . LYS A 92  ? 1.1577 0.8854 1.0258 -0.0659 0.1162  0.2358  677 LYS A CB  
742  C CG  . LYS A 92  ? 1.2008 0.9080 1.0334 -0.0418 0.1006  0.2511  677 LYS A CG  
743  C CD  . LYS A 92  ? 1.1858 0.9261 1.0045 -0.0240 0.0815  0.2383  677 LYS A CD  
744  C CE  . LYS A 92  ? 1.2175 0.9428 1.0006 -0.0006 0.0666  0.2529  677 LYS A CE  
745  N NZ  . LYS A 92  ? 1.2193 0.9153 1.0129 0.0109  0.0534  0.2552  677 LYS A NZ  
746  N N   . GLY A 93  ? 1.3214 1.0809 1.2992 -0.0937 0.1078  0.1742  678 GLY A N   
747  C CA  . GLY A 93  ? 1.3936 1.1674 1.4101 -0.1128 0.1152  0.1559  678 GLY A CA  
748  C C   . GLY A 93  ? 1.4200 1.2403 1.4445 -0.1178 0.1176  0.1414  678 GLY A C   
749  O O   . GLY A 93  ? 1.3500 1.1942 1.3645 -0.1046 0.1046  0.1321  678 GLY A O   
750  N N   . ASN A 94  ? 1.4032 1.2353 1.4479 -0.1371 0.1346  0.1388  679 ASN A N   
751  C CA  . ASN A 94  ? 1.3220 1.1960 1.3732 -0.1423 0.1408  0.1289  679 ASN A CA  
752  C C   . ASN A 94  ? 1.1239 1.0316 1.1881 -0.1333 0.1238  0.1051  679 ASN A C   
753  O O   . ASN A 94  ? 0.9209 0.8576 0.9757 -0.1270 0.1223  0.1005  679 ASN A O   
754  C CB  . ASN A 94  ? 1.3615 1.2406 1.3751 -0.1343 0.1481  0.1464  679 ASN A CB  
755  C CG  . ASN A 94  ? 1.4361 1.3166 1.4498 -0.1510 0.1731  0.1589  679 ASN A CG  
756  O OD1 . ASN A 94  ? 1.5829 1.4634 1.6297 -0.1704 0.1856  0.1532  679 ASN A OD1 
757  N ND2 . ASN A 94  ? 1.4351 1.3195 1.4131 -0.1441 0.1810  0.1744  679 ASN A ND2 
758  N N   . MET A 95  ? 1.0638 0.9675 1.1492 -0.1326 0.1116  0.0895  680 MET A N   
759  C CA  . MET A 95  ? 0.9820 0.9116 1.0708 -0.1212 0.0953  0.0715  680 MET A CA  
760  C C   . MET A 95  ? 0.8141 0.7496 0.9336 -0.1268 0.0876  0.0505  680 MET A C   
761  O O   . MET A 95  ? 0.7703 0.6887 0.8902 -0.1202 0.0773  0.0459  680 MET A O   
762  C CB  . MET A 95  ? 1.0855 1.0039 1.1460 -0.1022 0.0823  0.0784  680 MET A CB  
763  C CG  . MET A 95  ? 1.1634 1.0483 1.2218 -0.0969 0.0755  0.0833  680 MET A CG  
764  S SD  . MET A 95  ? 1.2709 1.1512 1.3003 -0.0747 0.0605  0.0893  680 MET A SD  
765  C CE  . MET A 95  ? 1.2742 1.1352 1.2709 -0.0713 0.0696  0.1161  680 MET A CE  
766  N N   . THR A 96  ? 0.6687 0.6325 0.8139 -0.1377 0.0919  0.0361  681 THR A N   
767  C CA  . THR A 96  ? 0.5997 0.5867 0.7634 -0.1348 0.0789  0.0133  681 THR A CA  
768  C C   . THR A 96  ? 0.4663 0.4718 0.6081 -0.1179 0.0685  0.0123  681 THR A C   
769  O O   . THR A 96  ? 0.4373 0.4567 0.5676 -0.1154 0.0744  0.0196  681 THR A O   
770  C CB  . THR A 96  ? 0.6125 0.6274 0.8100 -0.1495 0.0850  -0.0020 681 THR A CB  
771  O OG1 . THR A 96  ? 0.7185 0.7103 0.9373 -0.1644 0.0916  -0.0039 681 THR A OG1 
772  C CG2 . THR A 96  ? 0.5984 0.6444 0.8092 -0.1428 0.0702  -0.0245 681 THR A CG2 
773  N N   . LEU A 97  ? 0.3967 0.3994 0.5311 -0.1063 0.0546  0.0046  682 LEU A N   
774  C CA  . LEU A 97  ? 0.3681 0.3863 0.4845 -0.0921 0.0461  0.0033  682 LEU A CA  
775  C C   . LEU A 97  ? 0.3630 0.4136 0.4950 -0.0925 0.0422  -0.0123 682 LEU A C   
776  O O   . LEU A 97  ? 0.3864 0.4459 0.5344 -0.0942 0.0350  -0.0276 682 LEU A O   
777  C CB  . LEU A 97  ? 0.3896 0.3936 0.4928 -0.0807 0.0352  0.0018  682 LEU A CB  
778  C CG  . LEU A 97  ? 0.4231 0.3959 0.5166 -0.0791 0.0369  0.0142  682 LEU A CG  
779  C CD1 . LEU A 97  ? 0.5008 0.4676 0.5839 -0.0668 0.0265  0.0106  682 LEU A CD1 
780  C CD2 . LEU A 97  ? 0.4799 0.4433 0.5550 -0.0778 0.0443  0.0327  682 LEU A CD2 
781  N N   . SER A 98  ? 0.2741 0.3431 0.4050 -0.0926 0.0486  -0.0089 683 SER A N   
782  C CA  . SER A 98  ? 0.2281 0.3294 0.3745 -0.0911 0.0455  -0.0224 683 SER A CA  
783  C C   . SER A 98  ? 0.1919 0.3056 0.3226 -0.0816 0.0474  -0.0170 683 SER A C   
784  O O   . SER A 98  ? 0.1765 0.2786 0.2908 -0.0820 0.0559  -0.0033 683 SER A O   
785  C CB  . SER A 98  ? 0.2357 0.3532 0.4121 -0.1064 0.0548  -0.0297 683 SER A CB  
786  O OG  . SER A 98  ? 0.2574 0.3739 0.4316 -0.1143 0.0710  -0.0172 683 SER A OG  
787  N N   . PRO A 99  ? 0.1728 0.3089 0.3071 -0.0718 0.0390  -0.0276 684 PRO A N   
788  C CA  . PRO A 99  ? 0.1794 0.3296 0.3047 -0.0630 0.0412  -0.0259 684 PRO A CA  
789  C C   . PRO A 99  ? 0.1961 0.3584 0.3295 -0.0720 0.0567  -0.0216 684 PRO A C   
790  O O   . PRO A 99  ? 0.2116 0.3695 0.3258 -0.0676 0.0628  -0.0126 684 PRO A O   
791  C CB  . PRO A 99  ? 0.1605 0.3325 0.2954 -0.0526 0.0297  -0.0396 684 PRO A CB  
792  C CG  . PRO A 99  ? 0.1612 0.3202 0.2930 -0.0512 0.0189  -0.0436 684 PRO A CG  
793  C CD  . PRO A 99  ? 0.1679 0.3142 0.3108 -0.0661 0.0257  -0.0415 684 PRO A CD  
794  N N   . GLU A 100 ? 0.1867 0.3638 0.3479 -0.0855 0.0644  -0.0280 685 GLU A N   
795  C CA  . GLU A 100 ? 0.2080 0.3965 0.3778 -0.0962 0.0822  -0.0231 685 GLU A CA  
796  C C   . GLU A 100 ? 0.2302 0.3898 0.3743 -0.1012 0.0935  -0.0033 685 GLU A C   
797  O O   . GLU A 100 ? 0.2459 0.4127 0.3804 -0.1027 0.1067  0.0040  685 GLU A O   
798  C CB  . GLU A 100 ? 0.2404 0.4473 0.4483 -0.1128 0.0892  -0.0339 685 GLU A CB  
799  C CG  . GLU A 100 ? 0.2995 0.5252 0.5224 -0.1252 0.1098  -0.0314 685 GLU A CG  
800  C CD  . GLU A 100 ? 0.3449 0.5950 0.6128 -0.1413 0.1144  -0.0469 685 GLU A CD  
801  O OE1 . GLU A 100 ? 0.3916 0.6286 0.6702 -0.1601 0.1305  -0.0392 685 GLU A OE1 
802  O OE2 . GLU A 100 ? 0.3288 0.6101 0.6207 -0.1348 0.1020  -0.0665 685 GLU A OE2 
803  N N   A ASN A 101 ? 0.2290 0.3580 0.3628 -0.1032 0.0887  0.0045  686 ASN A N   
804  N N   B ASN A 101 ? 0.2400 0.3691 0.3733 -0.1029 0.0887  0.0047  686 ASN A N   
805  C CA  A ASN A 101 ? 0.2498 0.3484 0.3575 -0.1044 0.0954  0.0237  686 ASN A CA  
806  C CA  B ASN A 101 ? 0.2718 0.3721 0.3793 -0.1045 0.0964  0.0239  686 ASN A CA  
807  C C   A ASN A 101 ? 0.2425 0.3294 0.3187 -0.0880 0.0849  0.0296  686 ASN A C   
808  C C   B ASN A 101 ? 0.2595 0.3496 0.3349 -0.0883 0.0870  0.0301  686 ASN A C   
809  O O   A ASN A 101 ? 0.2543 0.3162 0.3090 -0.0860 0.0857  0.0435  686 ASN A O   
810  O O   B ASN A 101 ? 0.2867 0.3563 0.3385 -0.0866 0.0909  0.0450  686 ASN A O   
811  C CB  A ASN A 101 ? 0.2624 0.3324 0.3760 -0.1129 0.0947  0.0287  686 ASN A CB  
812  C CB  B ASN A 101 ? 0.2930 0.3635 0.4044 -0.1125 0.0956  0.0298  686 ASN A CB  
813  C CG  A ASN A 101 ? 0.2864 0.3602 0.4297 -0.1321 0.1080  0.0257  686 ASN A CG  
814  C CG  B ASN A 101 ? 0.3504 0.3940 0.4422 -0.1179 0.1083  0.0506  686 ASN A CG  
815  O OD1 A ASN A 101 ? 0.3190 0.3761 0.4778 -0.1400 0.1056  0.0222  686 ASN A OD1 
816  O OD1 B ASN A 101 ? 0.3808 0.4320 0.4629 -0.1216 0.1224  0.0597  686 ASN A OD1 
817  N ND2 A ASN A 101 ? 0.2787 0.3759 0.4327 -0.1396 0.1218  0.0250  686 ASN A ND2 
818  N ND2 B ASN A 101 ? 0.3805 0.3922 0.4656 -0.1177 0.1039  0.0586  686 ASN A ND2 
819  N N   . GLY A 102 ? 0.2231 0.3270 0.2983 -0.0765 0.0749  0.0188  687 GLY A N   
820  C CA  . GLY A 102 ? 0.2306 0.3263 0.2803 -0.0626 0.0665  0.0221  687 GLY A CA  
821  C C   . GLY A 102 ? 0.2237 0.2993 0.2664 -0.0569 0.0538  0.0226  687 GLY A C   
822  O O   . GLY A 102 ? 0.2181 0.2814 0.2405 -0.0486 0.0487  0.0282  687 GLY A O   
823  N N   . TYR A 103 ? 0.1849 0.2609 0.2451 -0.0598 0.0478  0.0140  688 TYR A N   
824  C CA  . TYR A 103 ? 0.1881 0.2490 0.2427 -0.0540 0.0371  0.0122  688 TYR A CA  
825  C C   . TYR A 103 ? 0.1575 0.2318 0.2215 -0.0489 0.0282  -0.0007 688 TYR A C   
826  O O   . TYR A 103 ? 0.1623 0.2521 0.2449 -0.0538 0.0285  -0.0097 688 TYR A O   
827  C CB  . TYR A 103 ? 0.2156 0.2579 0.2782 -0.0614 0.0377  0.0147  688 TYR A CB  
828  C CG  . TYR A 103 ? 0.2808 0.3029 0.3330 -0.0657 0.0455  0.0297  688 TYR A CG  
829  C CD1 . TYR A 103 ? 0.3280 0.3505 0.3885 -0.0773 0.0582  0.0356  688 TYR A CD1 
830  C CD2 . TYR A 103 ? 0.3168 0.3196 0.3521 -0.0579 0.0402  0.0379  688 TYR A CD2 
831  C CE1 . TYR A 103 ? 0.3814 0.3820 0.4283 -0.0803 0.0659  0.0518  688 TYR A CE1 
832  C CE2 . TYR A 103 ? 0.3865 0.3696 0.4095 -0.0592 0.0457  0.0527  688 TYR A CE2 
833  C CZ  . TYR A 103 ? 0.4398 0.4192 0.4676 -0.0705 0.0586  0.0605  688 TYR A CZ  
834  O OH  . TYR A 103 ? 0.5467 0.5035 0.5595 -0.0719 0.0653  0.0776  688 TYR A OH  
835  N N   . TRP A 104 ? 0.1328 0.2009 0.1840 -0.0392 0.0205  -0.0015 689 TRP A N   
836  C CA  . TRP A 104 ? 0.1228 0.1986 0.1761 -0.0328 0.0124  -0.0106 689 TRP A CA  
837  C C   . TRP A 104 ? 0.1304 0.1897 0.1753 -0.0299 0.0075  -0.0099 689 TRP A C   
838  O O   . TRP A 104 ? 0.1277 0.1778 0.1595 -0.0242 0.0061  -0.0054 689 TRP A O   
839  C CB  . TRP A 104 ? 0.1198 0.2048 0.1651 -0.0232 0.0102  -0.0121 689 TRP A CB  
840  C CG  . TRP A 104 ? 0.1317 0.2350 0.1856 -0.0241 0.0155  -0.0142 689 TRP A CG  
841  C CD1 . TRP A 104 ? 0.1474 0.2718 0.2167 -0.0227 0.0136  -0.0233 689 TRP A CD1 
842  C CD2 . TRP A 104 ? 0.1412 0.2461 0.1899 -0.0266 0.0241  -0.0083 689 TRP A CD2 
843  N NE1 . TRP A 104 ? 0.1430 0.2831 0.2199 -0.0246 0.0213  -0.0241 689 TRP A NE1 
844  C CE2 . TRP A 104 ? 0.1465 0.2745 0.2093 -0.0273 0.0285  -0.0147 689 TRP A CE2 
845  C CE3 . TRP A 104 ? 0.1573 0.2485 0.1903 -0.0273 0.0277  0.0007  689 TRP A CE3 
846  C CZ2 . TRP A 104 ? 0.1788 0.3160 0.2391 -0.0289 0.0384  -0.0120 689 TRP A CZ2 
847  C CZ3 . TRP A 104 ? 0.1920 0.2912 0.2196 -0.0283 0.0360  0.0040  689 TRP A CZ3 
848  C CH2 . TRP A 104 ? 0.1895 0.3109 0.2299 -0.0293 0.0420  -0.0022 689 TRP A CH2 
849  N N   . VAL A 105 ? 0.1309 0.1872 0.1855 -0.0345 0.0054  -0.0157 690 VAL A N   
850  C CA  . VAL A 105 ? 0.1294 0.1707 0.1779 -0.0323 0.0027  -0.0156 690 VAL A CA  
851  C C   . VAL A 105 ? 0.1348 0.1820 0.1874 -0.0311 -0.0026 -0.0270 690 VAL A C   
852  O O   . VAL A 105 ? 0.1399 0.2011 0.2039 -0.0341 -0.0048 -0.0354 690 VAL A O   
853  C CB  . VAL A 105 ? 0.1456 0.1705 0.1985 -0.0380 0.0064  -0.0098 690 VAL A CB  
854  C CG1 . VAL A 105 ? 0.1699 0.1888 0.2132 -0.0371 0.0106  0.0021  690 VAL A CG1 
855  C CG2 . VAL A 105 ? 0.1555 0.1799 0.2254 -0.0477 0.0092  -0.0144 690 VAL A CG2 
856  N N   A VAL A 106 ? 0.1330 0.1710 0.1763 -0.0264 -0.0045 -0.0279 691 VAL A N   
857  N N   B VAL A 106 ? 0.1413 0.1794 0.1847 -0.0264 -0.0045 -0.0280 691 VAL A N   
858  C CA  A VAL A 106 ? 0.1382 0.1780 0.1817 -0.0249 -0.0083 -0.0385 691 VAL A CA  
859  C CA  B VAL A 106 ? 0.1537 0.1940 0.1974 -0.0250 -0.0084 -0.0387 691 VAL A CA  
860  C C   A VAL A 106 ? 0.1624 0.1873 0.2125 -0.0282 -0.0063 -0.0399 691 VAL A C   
861  C C   B VAL A 106 ? 0.1713 0.1966 0.2208 -0.0279 -0.0064 -0.0400 691 VAL A C   
862  O O   A VAL A 106 ? 0.1616 0.1748 0.2098 -0.0274 -0.0034 -0.0317 691 VAL A O   
863  O O   B VAL A 106 ? 0.1677 0.1818 0.2140 -0.0264 -0.0036 -0.0319 691 VAL A O   
864  C CB  A VAL A 106 ? 0.1384 0.1809 0.1641 -0.0161 -0.0104 -0.0388 691 VAL A CB  
865  C CB  B VAL A 106 ? 0.1690 0.2130 0.1951 -0.0161 -0.0109 -0.0394 691 VAL A CB  
866  C CG1 A VAL A 106 ? 0.1496 0.1914 0.1704 -0.0138 -0.0124 -0.0485 691 VAL A CG1 
867  C CG1 B VAL A 106 ? 0.1696 0.2262 0.1908 -0.0112 -0.0141 -0.0381 691 VAL A CG1 
868  C CG2 A VAL A 106 ? 0.1403 0.1960 0.1606 -0.0111 -0.0142 -0.0389 691 VAL A CG2 
869  C CG2 B VAL A 106 ? 0.1923 0.2247 0.2085 -0.0130 -0.0066 -0.0314 691 VAL A CG2 
870  N N   . MET A 107 ? 0.1819 0.2079 0.2406 -0.0309 -0.0088 -0.0519 693 MET A N   
871  C CA  . MET A 107 ? 0.2022 0.2126 0.2695 -0.0332 -0.0072 -0.0550 693 MET A CA  
872  C C   . MET A 107 ? 0.2112 0.2254 0.2768 -0.0301 -0.0106 -0.0701 693 MET A C   
873  O O   . MET A 107 ? 0.2201 0.2488 0.2841 -0.0297 -0.0153 -0.0807 693 MET A O   
874  C CB  . MET A 107 ? 0.2663 0.2677 0.3515 -0.0429 -0.0047 -0.0543 693 MET A CB  
875  C CG  . MET A 107 ? 0.3401 0.3531 0.4393 -0.0500 -0.0070 -0.0663 693 MET A CG  
876  S SD  . MET A 107 ? 0.5995 0.5967 0.7185 -0.0632 0.0004  -0.0589 693 MET A SD  
877  C CE  . MET A 107 ? 0.3999 0.3659 0.5216 -0.0613 0.0021  -0.0566 693 MET A CE  
878  N N   . MET A 108 ? 0.1973 0.1991 0.2640 -0.0271 -0.0085 -0.0720 694 MET A N   
879  C CA  . MET A 108 ? 0.2019 0.2044 0.2699 -0.0246 -0.0102 -0.0880 694 MET A CA  
880  C C   . MET A 108 ? 0.2244 0.2100 0.3123 -0.0298 -0.0100 -0.0944 694 MET A C   
881  O O   . MET A 108 ? 0.2194 0.1887 0.3140 -0.0302 -0.0072 -0.0838 694 MET A O   
882  C CB  . MET A 108 ? 0.2061 0.2080 0.2623 -0.0164 -0.0066 -0.0871 694 MET A CB  
883  C CG  . MET A 108 ? 0.2230 0.2286 0.2768 -0.0126 -0.0069 -0.1047 694 MET A CG  
884  S SD  . MET A 108 ? 0.2470 0.2532 0.2925 -0.0045 0.0006  -0.1031 694 MET A SD  
885  C CE  . MET A 108 ? 0.2714 0.2876 0.3070 -0.0002 0.0007  -0.1246 694 MET A CE  
886  N N   . LYS A 109 ? 0.2622 0.2513 0.3588 -0.0328 -0.0135 -0.1124 695 LYS A N   
887  C CA  . LYS A 109 ? 0.3462 0.3168 0.4635 -0.0381 -0.0132 -0.1214 695 LYS A CA  
888  C C   . LYS A 109 ? 0.3922 0.3730 0.5136 -0.0385 -0.0182 -0.1459 695 LYS A C   
889  O O   . LYS A 109 ? 0.3850 0.3861 0.5021 -0.0404 -0.0232 -0.1535 695 LYS A O   
890  C CB  . LYS A 109 ? 0.4029 0.3638 0.5362 -0.0496 -0.0109 -0.1122 695 LYS A CB  
891  C CG  . LYS A 109 ? 0.5251 0.4622 0.6810 -0.0573 -0.0090 -0.1193 695 LYS A CG  
892  C CD  . LYS A 109 ? 0.6493 0.5755 0.8174 -0.0692 -0.0035 -0.1055 695 LYS A CD  
893  C CE  . LYS A 109 ? 0.7385 0.6382 0.9302 -0.0792 0.0000  -0.1111 695 LYS A CE  
894  N NZ  . LYS A 109 ? 0.7863 0.6720 0.9827 -0.0887 0.0082  -0.0913 695 LYS A NZ  
895  N N   . GLU A 110 ? 0.4646 0.4323 0.5936 -0.0352 -0.0176 -0.1586 696 GLU A N   
896  C CA  . GLU A 110 ? 0.4892 0.4623 0.6257 -0.0363 -0.0224 -0.1846 696 GLU A CA  
897  C C   . GLU A 110 ? 0.4541 0.4552 0.5666 -0.0291 -0.0268 -0.1943 696 GLU A C   
898  O O   . GLU A 110 ? 0.4535 0.4706 0.5673 -0.0318 -0.0340 -0.2108 696 GLU A O   
899  C CB  . GLU A 110 ? 0.5525 0.5166 0.7156 -0.0503 -0.0243 -0.1914 696 GLU A CB  
900  C CG  . GLU A 110 ? 0.6271 0.5571 0.8079 -0.0545 -0.0182 -0.1800 696 GLU A CG  
901  C CD  . GLU A 110 ? 0.7365 0.6481 0.9463 -0.0688 -0.0171 -0.1883 696 GLU A CD  
902  O OE1 . GLU A 110 ? 0.8485 0.7481 1.0726 -0.0693 -0.0191 -0.2090 696 GLU A OE1 
903  O OE2 . GLU A 110 ? 0.8354 0.7443 1.0540 -0.0797 -0.0131 -0.1745 696 GLU A OE2 
904  N N   . ASN A 111 ? 0.4166 0.4224 0.5075 -0.0195 -0.0222 -0.1840 697 ASN A N   
905  C CA  . ASN A 111 ? 0.4774 0.5041 0.5400 -0.0110 -0.0232 -0.1879 697 ASN A CA  
906  C C   . ASN A 111 ? 0.4717 0.5160 0.5237 -0.0125 -0.0296 -0.1826 697 ASN A C   
907  O O   . ASN A 111 ? 0.4850 0.5471 0.5160 -0.0061 -0.0345 -0.1913 697 ASN A O   
908  C CB  . ASN A 111 ? 0.5592 0.5927 0.6163 -0.0057 -0.0252 -0.2131 697 ASN A CB  
909  C CG  . ASN A 111 ? 0.6477 0.6878 0.6803 0.0045  -0.0172 -0.2107 697 ASN A CG  
910  O OD1 . ASN A 111 ? 0.7074 0.7467 0.7297 0.0066  -0.0105 -0.1907 697 ASN A OD1 
911  N ND2 . ASN A 111 ? 0.7809 0.8281 0.8051 0.0104  -0.0167 -0.2318 697 ASN A ND2 
912  N N   . GLU A 112 ? 0.3670 0.4066 0.4312 -0.0195 -0.0294 -0.1674 698 GLU A N   
913  C CA  . GLU A 112 ? 0.3563 0.4130 0.4149 -0.0202 -0.0352 -0.1630 698 GLU A CA  
914  C C   . GLU A 112 ? 0.2869 0.3369 0.3437 -0.0215 -0.0298 -0.1392 698 GLU A C   
915  O O   . GLU A 112 ? 0.2770 0.3095 0.3444 -0.0252 -0.0235 -0.1288 698 GLU A O   
916  C CB  . GLU A 112 ? 0.4112 0.4754 0.4954 -0.0300 -0.0422 -0.1776 698 GLU A CB  
917  C CG  . GLU A 112 ? 0.5234 0.6058 0.6102 -0.0318 -0.0472 -0.1717 698 GLU A CG  
918  C CD  . GLU A 112 ? 0.6501 0.7488 0.7625 -0.0405 -0.0553 -0.1909 698 GLU A CD  
919  O OE1 . GLU A 112 ? 0.6902 0.7998 0.8043 -0.0389 -0.0635 -0.2139 698 GLU A OE1 
920  O OE2 . GLU A 112 ? 0.7892 0.8917 0.9204 -0.0490 -0.0532 -0.1835 698 GLU A OE2 
921  N N   . TYR A 113 ? 0.2559 0.3200 0.2969 -0.0165 -0.0329 -0.1315 699 TYR A N   
922  C CA  . TYR A 113 ? 0.2303 0.2907 0.2691 -0.0170 -0.0288 -0.1121 699 TYR A CA  
923  C C   . TYR A 113 ? 0.2245 0.2992 0.2767 -0.0215 -0.0342 -0.1134 699 TYR A C   
924  O O   . TYR A 113 ? 0.2365 0.3294 0.2865 -0.0181 -0.0428 -0.1254 699 TYR A O   
925  C CB  . TYR A 113 ? 0.2323 0.2949 0.2433 -0.0071 -0.0266 -0.1015 699 TYR A CB  
926  C CG  . TYR A 113 ? 0.2226 0.2755 0.2218 -0.0033 -0.0195 -0.1011 699 TYR A CG  
927  C CD1 . TYR A 113 ? 0.2458 0.3053 0.2295 0.0024  -0.0205 -0.1133 699 TYR A CD1 
928  C CD2 . TYR A 113 ? 0.2139 0.2539 0.2174 -0.0049 -0.0117 -0.0893 699 TYR A CD2 
929  C CE1 . TYR A 113 ? 0.2540 0.3072 0.2292 0.0055  -0.0121 -0.1141 699 TYR A CE1 
930  C CE2 . TYR A 113 ? 0.2140 0.2490 0.2117 -0.0016 -0.0048 -0.0907 699 TYR A CE2 
931  C CZ  . TYR A 113 ? 0.2344 0.2763 0.2176 0.0033  -0.0039 -0.1024 699 TYR A CZ  
932  O OH  . TYR A 113 ? 0.2561 0.2958 0.2353 0.0062  0.0044  -0.1050 699 TYR A OH  
933  N N   . GLN A 114 ? 0.1966 0.2644 0.2609 -0.0278 -0.0290 -0.1007 700 GLN A N   
934  C CA  . GLN A 114 ? 0.1981 0.2808 0.2771 -0.0326 -0.0314 -0.1012 700 GLN A CA  
935  C C   . GLN A 114 ? 0.1674 0.2468 0.2400 -0.0309 -0.0260 -0.0834 700 GLN A C   
936  O O   . GLN A 114 ? 0.1836 0.2461 0.2506 -0.0314 -0.0196 -0.0716 700 GLN A O   
937  C CB  . GLN A 114 ? 0.2266 0.3047 0.3349 -0.0467 -0.0281 -0.1076 700 GLN A CB  
938  C CG  . GLN A 114 ? 0.3188 0.3993 0.4418 -0.0517 -0.0331 -0.1281 700 GLN A CG  
939  C CD  . GLN A 114 ? 0.3295 0.4000 0.4825 -0.0673 -0.0273 -0.1313 700 GLN A CD  
940  O OE1 . GLN A 114 ? 0.3673 0.4242 0.5255 -0.0734 -0.0182 -0.1155 700 GLN A OE1 
941  N NE2 . GLN A 114 ? 0.4830 0.5592 0.6545 -0.0736 -0.0322 -0.1520 700 GLN A NE2 
942  N N   . ALA A 115 ? 0.1501 0.2471 0.2240 -0.0277 -0.0295 -0.0830 701 ALA A N   
943  C CA  . ALA A 115 ? 0.1342 0.2311 0.2099 -0.0288 -0.0239 -0.0702 701 ALA A CA  
944  C C   . ALA A 115 ? 0.1411 0.2441 0.2431 -0.0416 -0.0190 -0.0731 701 ALA A C   
945  O O   . ALA A 115 ? 0.1409 0.2598 0.2618 -0.0468 -0.0232 -0.0871 701 ALA A O   
946  C CB  . ALA A 115 ? 0.1520 0.2645 0.2180 -0.0180 -0.0294 -0.0692 701 ALA A CB  
947  N N   A SER A 116 ? 0.1411 0.2313 0.2446 -0.0474 -0.0097 -0.0606 702 SER A N   
948  N N   B SER A 116 ? 0.1419 0.2344 0.2430 -0.0456 -0.0100 -0.0594 702 SER A N   
949  C CA  A SER A 116 ? 0.1556 0.2466 0.2816 -0.0609 -0.0025 -0.0614 702 SER A CA  
950  C CA  B SER A 116 ? 0.1557 0.2469 0.2744 -0.0578 -0.0008 -0.0552 702 SER A CA  
951  C C   A SER A 116 ? 0.1459 0.2604 0.2841 -0.0630 0.0002  -0.0625 702 SER A C   
952  C C   B SER A 116 ? 0.1504 0.2675 0.2844 -0.0602 0.0004  -0.0600 702 SER A C   
953  O O   A SER A 116 ? 0.1535 0.2650 0.2981 -0.0710 0.0107  -0.0537 702 SER A O   
954  O O   B SER A 116 ? 0.1617 0.2808 0.3002 -0.0654 0.0097  -0.0518 702 SER A O   
955  C CB  A SER A 116 ? 0.1791 0.2432 0.2989 -0.0656 0.0059  -0.0472 702 SER A CB  
956  C CB  B SER A 116 ? 0.1515 0.2228 0.2566 -0.0582 0.0074  -0.0376 702 SER A CB  
957  O OG  A SER A 116 ? 0.2177 0.2641 0.3306 -0.0623 0.0022  -0.0497 702 SER A OG  
958  O OG  B SER A 116 ? 0.1345 0.2130 0.2301 -0.0539 0.0113  -0.0287 702 SER A OG  
959  N N   . SER A 117 ? 0.1357 0.2750 0.2779 -0.0553 -0.0090 -0.0740 703 SER A N   
960  C CA  . SER A 117 ? 0.1212 0.2896 0.2878 -0.0594 -0.0085 -0.0834 703 SER A CA  
961  C C   . SER A 117 ? 0.1139 0.2838 0.3094 -0.0772 -0.0021 -0.0915 703 SER A C   
962  O O   . SER A 117 ? 0.1255 0.2738 0.3199 -0.0832 -0.0013 -0.0918 703 SER A O   
963  C CB  . SER A 117 ? 0.1142 0.3066 0.2805 -0.0468 -0.0225 -0.0961 703 SER A CB  
964  O OG  . SER A 117 ? 0.1140 0.3051 0.2794 -0.0461 -0.0321 -0.1083 703 SER A OG  
965  N N   . VAL A 118 ? 0.1021 0.2977 0.3258 -0.0858 0.0025  -0.0996 704 VAL A N   
966  C CA  . VAL A 118 ? 0.1226 0.3227 0.3790 -0.1044 0.0089  -0.1099 704 VAL A CA  
967  C C   . VAL A 118 ? 0.1111 0.3510 0.3962 -0.1040 -0.0010 -0.1324 704 VAL A C   
968  O O   . VAL A 118 ? 0.1059 0.3731 0.4030 -0.1010 0.0007  -0.1347 704 VAL A O   
969  C CB  . VAL A 118 ? 0.1455 0.3388 0.4134 -0.1195 0.0285  -0.0972 704 VAL A CB  
970  C CG1 . VAL A 118 ? 0.1732 0.3619 0.4737 -0.1408 0.0374  -0.1053 704 VAL A CG1 
971  C CG2 . VAL A 118 ? 0.1671 0.3258 0.4022 -0.1154 0.0359  -0.0742 704 VAL A CG2 
972  N N   . PRO A 119 ? 0.1092 0.3561 0.4070 -0.1057 -0.0127 -0.1512 705 PRO A N   
973  C CA  . PRO A 119 ? 0.1223 0.3396 0.4070 -0.1075 -0.0157 -0.1518 705 PRO A CA  
974  C C   . PRO A 119 ? 0.1209 0.3209 0.3646 -0.0890 -0.0236 -0.1413 705 PRO A C   
975  O O   . PRO A 119 ? 0.1085 0.3212 0.3348 -0.0741 -0.0301 -0.1372 705 PRO A O   
976  C CB  . PRO A 119 ? 0.1276 0.3686 0.4365 -0.1104 -0.0290 -0.1793 705 PRO A CB  
977  C CG  . PRO A 119 ? 0.1247 0.4038 0.4718 -0.1191 -0.0267 -0.1915 705 PRO A CG  
978  C CD  . PRO A 119 ? 0.1123 0.3995 0.4394 -0.1052 -0.0246 -0.1755 705 PRO A CD  
979  N N   . PRO A 120 ? 0.1333 0.3015 0.3604 -0.0896 -0.0216 -0.1351 706 PRO A N   
980  C CA  . PRO A 120 ? 0.1373 0.2906 0.3288 -0.0740 -0.0268 -0.1258 706 PRO A CA  
981  C C   . PRO A 120 ? 0.1311 0.3029 0.3098 -0.0601 -0.0422 -0.1394 706 PRO A C   
982  O O   . PRO A 120 ? 0.1377 0.3281 0.3332 -0.0628 -0.0510 -0.1594 706 PRO A O   
983  C CB  . PRO A 120 ? 0.1516 0.2715 0.3378 -0.0797 -0.0208 -0.1205 706 PRO A CB  
984  C CG  . PRO A 120 ? 0.1806 0.2947 0.3975 -0.0976 -0.0129 -0.1259 706 PRO A CG  
985  C CD  . PRO A 120 ? 0.1649 0.3100 0.4092 -0.1054 -0.0131 -0.1369 706 PRO A CD  
986  N N   . THR A 121 ? 0.1311 0.2981 0.2792 -0.0452 -0.0447 -0.1271 707 THR A N   
987  C CA  . THR A 121 ? 0.1479 0.3287 0.2765 -0.0299 -0.0579 -0.1350 707 THR A CA  
988  C C   . THR A 121 ? 0.1722 0.3327 0.2780 -0.0260 -0.0581 -0.1347 707 THR A C   
989  O O   . THR A 121 ? 0.1847 0.3226 0.2735 -0.0242 -0.0500 -0.1193 707 THR A O   
990  C CB  . THR A 121 ? 0.1505 0.3347 0.2594 -0.0164 -0.0591 -0.1211 707 THR A CB  
991  O OG1 . THR A 121 ? 0.1499 0.3563 0.2817 -0.0187 -0.0588 -0.1236 707 THR A OG1 
992  C CG2 . THR A 121 ? 0.1807 0.3733 0.2640 0.0006  -0.0717 -0.1254 707 THR A CG2 
993  N N   . ARG A 122 ? 0.2087 0.3796 0.3149 -0.0240 -0.0675 -0.1530 708 ARG A N   
994  C CA  . ARG A 122 ? 0.2623 0.4168 0.3466 -0.0194 -0.0668 -0.1548 708 ARG A CA  
995  C C   . ARG A 122 ? 0.2800 0.4357 0.3275 -0.0025 -0.0707 -0.1449 708 ARG A C   
996  O O   . ARG A 122 ? 0.3243 0.5002 0.3636 0.0079  -0.0814 -0.1491 708 ARG A O   
997  C CB  . ARG A 122 ? 0.3576 0.5232 0.4586 -0.0249 -0.0746 -0.1801 708 ARG A CB  
998  C CG  . ARG A 122 ? 0.4925 0.6471 0.5768 -0.0209 -0.0755 -0.1901 708 ARG A CG  
999  C CD  . ARG A 122 ? 0.6523 0.8245 0.7613 -0.0278 -0.0855 -0.2187 708 ARG A CD  
1000 N NE  . ARG A 122 ? 0.7008 0.8854 0.8485 -0.0414 -0.0857 -0.2243 708 ARG A NE  
1001 C CZ  . ARG A 122 ? 0.7343 0.9022 0.9102 -0.0576 -0.0742 -0.2183 708 ARG A CZ  
1002 N NH1 . ARG A 122 ? 0.7036 0.8830 0.9015 -0.0656 -0.0706 -0.2120 708 ARG A NH1 
1003 N NH2 . ARG A 122 ? 0.8165 0.9550 0.9947 -0.0639 -0.0652 -0.2150 708 ARG A NH2 
1004 N N   . LEU A 123 ? 0.2717 0.4056 0.2980 0.0004  -0.0620 -0.1323 709 LEU A N   
1005 C CA  . LEU A 123 ? 0.2991 0.4279 0.2919 0.0135  -0.0612 -0.1189 709 LEU A CA  
1006 C C   . LEU A 123 ? 0.3449 0.4743 0.3135 0.0208  -0.0639 -0.1284 709 LEU A C   
1007 O O   . LEU A 123 ? 0.3604 0.4824 0.3364 0.0146  -0.0597 -0.1375 709 LEU A O   
1008 C CB  . LEU A 123 ? 0.2899 0.3970 0.2780 0.0106  -0.0488 -0.0997 709 LEU A CB  
1009 C CG  . LEU A 123 ? 0.2745 0.3803 0.2826 0.0039  -0.0450 -0.0902 709 LEU A CG  
1010 C CD1 . LEU A 123 ? 0.2880 0.3737 0.2932 0.0004  -0.0343 -0.0757 709 LEU A CD1 
1011 C CD2 . LEU A 123 ? 0.2946 0.4130 0.2977 0.0124  -0.0509 -0.0856 709 LEU A CD2 
1012 N N   . LEU A 124 ? 0.3890 0.5268 0.3284 0.0347  -0.0707 -0.1264 710 LEU A N   
1013 C CA  . LEU A 124 ? 0.4573 0.5954 0.3663 0.0433  -0.0716 -0.1328 710 LEU A CA  
1014 C C   . LEU A 124 ? 0.4318 0.5485 0.3154 0.0464  -0.0575 -0.1128 710 LEU A C   
1015 O O   . LEU A 124 ? 0.4597 0.5698 0.3231 0.0544  -0.0560 -0.0963 710 LEU A O   
1016 C CB  . LEU A 124 ? 0.5323 0.6912 0.4207 0.0577  -0.0871 -0.1406 710 LEU A CB  
1017 C CG  . LEU A 124 ? 0.6447 0.8035 0.4906 0.0701  -0.0877 -0.1427 710 LEU A CG  
1018 C CD1 . LEU A 124 ? 0.7019 0.8643 0.5516 0.0646  -0.0860 -0.1633 710 LEU A CD1 
1019 C CD2 . LEU A 124 ? 0.7365 0.9146 0.5590 0.0870  -0.1047 -0.1465 710 LEU A CD2 
1020 N N   . ILE A 125 ? 0.4404 0.5453 0.3295 0.0391  -0.0464 -0.1145 711 ILE A N   
1021 C CA  . ILE A 125 ? 0.4425 0.5302 0.3142 0.0399  -0.0321 -0.0978 711 ILE A CA  
1022 C C   . ILE A 125 ? 0.4726 0.5622 0.3193 0.0451  -0.0269 -0.1058 711 ILE A C   
1023 O O   . ILE A 125 ? 0.5421 0.6360 0.4018 0.0410  -0.0269 -0.1226 711 ILE A O   
1024 C CB  . ILE A 125 ? 0.4712 0.5459 0.3712 0.0284  -0.0229 -0.0916 711 ILE A CB  
1025 C CG1 . ILE A 125 ? 0.4493 0.5231 0.3667 0.0249  -0.0270 -0.0821 711 ILE A CG1 
1026 C CG2 . ILE A 125 ? 0.4792 0.5406 0.3668 0.0280  -0.0082 -0.0802 711 ILE A CG2 
1027 C CD1 . ILE A 125 ? 0.4760 0.5366 0.4125 0.0165  -0.0186 -0.0720 711 ILE A CD1 
1028 N N   . LYS A 126 ? 0.4740 0.5608 0.2836 0.0551  -0.0234 -0.0949 712 LYS A N   
1029 C CA  . LYS A 126 ? 0.5489 0.6391 0.3298 0.0609  -0.0171 -0.1021 712 LYS A CA  
1030 C C   . LYS A 126 ? 0.4735 0.5509 0.2566 0.0541  0.0025  -0.0944 712 LYS A C   
1031 O O   . LYS A 126 ? 0.5019 0.5841 0.2787 0.0544  0.0097  -0.1061 712 LYS A O   
1032 C CB  . LYS A 126 ? 0.6586 0.7524 0.3954 0.0756  -0.0226 -0.0945 712 LYS A CB  
1033 C CG  . LYS A 126 ? 0.7691 0.8838 0.5031 0.0844  -0.0440 -0.1107 712 LYS A CG  
1034 C CD  . LYS A 126 ? 0.9217 1.0423 0.6071 0.1022  -0.0515 -0.1059 712 LYS A CD  
1035 C CE  . LYS A 126 ? 1.0161 1.1214 0.6820 0.1103  -0.0505 -0.0801 712 LYS A CE  
1036 N NZ  . LYS A 126 ? 1.0169 1.1311 0.7079 0.1124  -0.0663 -0.0813 712 LYS A NZ  
1037 N N   . GLU A 127 ? 0.4289 0.4921 0.2232 0.0482  0.0111  -0.0768 713 GLU A N   
1038 C CA  . GLU A 127 ? 0.4223 0.4768 0.2249 0.0411  0.0286  -0.0711 713 GLU A CA  
1039 C C   . GLU A 127 ? 0.3423 0.3927 0.1858 0.0312  0.0275  -0.0721 713 GLU A C   
1040 O O   . GLU A 127 ? 0.3426 0.3856 0.1957 0.0286  0.0246  -0.0603 713 GLU A O   
1041 C CB  . GLU A 127 ? 0.5157 0.5565 0.2939 0.0428  0.0402  -0.0496 713 GLU A CB  
1042 C CG  . GLU A 127 ? 0.6294 0.6632 0.4197 0.0339  0.0591  -0.0436 713 GLU A CG  
1043 C CD  . GLU A 127 ? 0.6865 0.7049 0.4548 0.0332  0.0735  -0.0232 713 GLU A CD  
1044 O OE1 . GLU A 127 ? 0.7000 0.7108 0.4355 0.0420  0.0697  -0.0123 713 GLU A OE1 
1045 O OE2 . GLU A 127 ? 0.6942 0.7082 0.4800 0.0238  0.0882  -0.0191 713 GLU A OE2 
1046 N N   . PRO A 128 ? 0.3390 0.3935 0.2059 0.0270  0.0286  -0.0863 714 PRO A N   
1047 C CA  . PRO A 128 ? 0.3173 0.3667 0.2192 0.0198  0.0248  -0.0864 714 PRO A CA  
1048 C C   . PRO A 128 ? 0.2875 0.3281 0.1976 0.0152  0.0337  -0.0709 714 PRO A C   
1049 O O   . PRO A 128 ? 0.3020 0.3421 0.2070 0.0142  0.0467  -0.0678 714 PRO A O   
1050 C CB  . PRO A 128 ? 0.3472 0.3999 0.2672 0.0187  0.0259  -0.1036 714 PRO A CB  
1051 C CG  . PRO A 128 ? 0.3934 0.4562 0.2889 0.0253  0.0260  -0.1169 714 PRO A CG  
1052 C CD  . PRO A 128 ? 0.4008 0.4642 0.2613 0.0302  0.0322  -0.1036 714 PRO A CD  
1053 N N   . PRO A 129 ? 0.2514 0.2864 0.1773 0.0114  0.0274  -0.0629 715 PRO A N   
1054 C CA  . PRO A 129 ? 0.2277 0.2556 0.1627 0.0072  0.0341  -0.0509 715 PRO A CA  
1055 C C   . PRO A 129 ? 0.2325 0.2616 0.1916 0.0037  0.0392  -0.0565 715 PRO A C   
1056 O O   . PRO A 129 ? 0.2355 0.2657 0.2107 0.0038  0.0334  -0.0658 715 PRO A O   
1057 C CB  . PRO A 129 ? 0.2254 0.2499 0.1697 0.0056  0.0244  -0.0448 715 PRO A CB  
1058 C CG  . PRO A 129 ? 0.2218 0.2518 0.1751 0.0059  0.0146  -0.0561 715 PRO A CG  
1059 C CD  . PRO A 129 ? 0.2369 0.2739 0.1725 0.0108  0.0145  -0.0659 715 PRO A CD  
1060 N N   . LYS A 130 ? 0.2140 0.2427 0.1765 0.0009  0.0499  -0.0513 716 LYS A N   
1061 C CA  . LYS A 130 ? 0.2155 0.2480 0.2040 -0.0015 0.0529  -0.0558 716 LYS A CA  
1062 C C   . LYS A 130 ? 0.1920 0.2199 0.1935 -0.0051 0.0490  -0.0468 716 LYS A C   
1063 O O   . LYS A 130 ? 0.1776 0.2088 0.2008 -0.0056 0.0468  -0.0499 716 LYS A O   
1064 C CB  . LYS A 130 ? 0.2225 0.2628 0.2104 -0.0027 0.0680  -0.0595 716 LYS A CB  
1065 C CG  . LYS A 130 ? 0.2639 0.3095 0.2326 0.0016  0.0731  -0.0683 716 LYS A CG  
1066 C CD  . LYS A 130 ? 0.2890 0.3375 0.2685 0.0062  0.0640  -0.0828 716 LYS A CD  
1067 C CE  . LYS A 130 ? 0.3370 0.3929 0.2982 0.0108  0.0695  -0.0946 716 LYS A CE  
1068 N NZ  . LYS A 130 ? 0.3548 0.4118 0.3285 0.0148  0.0611  -0.1110 716 LYS A NZ  
1069 N N   . ARG A 131 ? 0.1817 0.2025 0.1689 -0.0064 0.0477  -0.0365 717 ARG A N   
1070 C CA  . ARG A 131 ? 0.1701 0.1864 0.1664 -0.0091 0.0435  -0.0295 717 ARG A CA  
1071 C C   . ARG A 131 ? 0.1638 0.1739 0.1450 -0.0068 0.0363  -0.0230 717 ARG A C   
1072 O O   . ARG A 131 ? 0.1824 0.1898 0.1430 -0.0039 0.0386  -0.0201 717 ARG A O   
1073 C CB  . ARG A 131 ? 0.2152 0.2300 0.2141 -0.0140 0.0543  -0.0255 717 ARG A CB  
1074 C CG  . ARG A 131 ? 0.2454 0.2577 0.2571 -0.0171 0.0502  -0.0222 717 ARG A CG  
1075 C CD  . ARG A 131 ? 0.3411 0.3503 0.3563 -0.0236 0.0619  -0.0195 717 ARG A CD  
1076 N NE  . ARG A 131 ? 0.3765 0.3985 0.4132 -0.0272 0.0689  -0.0281 717 ARG A NE  
1077 C CZ  . ARG A 131 ? 0.4736 0.5003 0.5308 -0.0337 0.0730  -0.0312 717 ARG A CZ  
1078 N NH1 . ARG A 131 ? 0.4621 0.4788 0.5182 -0.0382 0.0735  -0.0264 717 ARG A NH1 
1079 N NH2 . ARG A 131 ? 0.5043 0.5472 0.5858 -0.0356 0.0765  -0.0411 717 ARG A NH2 
1080 N N   . VAL A 132 ? 0.1545 0.1639 0.1455 -0.0074 0.0283  -0.0212 718 VAL A N   
1081 C CA  . VAL A 132 ? 0.1499 0.1573 0.1326 -0.0053 0.0214  -0.0170 718 VAL A CA  
1082 C C   . VAL A 132 ? 0.1575 0.1606 0.1432 -0.0067 0.0210  -0.0111 718 VAL A C   
1083 O O   . VAL A 132 ? 0.1672 0.1717 0.1664 -0.0092 0.0201  -0.0122 718 VAL A O   
1084 C CB  . VAL A 132 ? 0.1454 0.1567 0.1368 -0.0054 0.0137  -0.0214 718 VAL A CB  
1085 C CG1 . VAL A 132 ? 0.1520 0.1653 0.1397 -0.0044 0.0080  -0.0184 718 VAL A CG1 
1086 C CG2 . VAL A 132 ? 0.1553 0.1700 0.1453 -0.0042 0.0138  -0.0299 718 VAL A CG2 
1087 N N   . GLY A 133 ? 0.1546 0.1529 0.1276 -0.0038 0.0205  -0.0059 719 GLY A N   
1088 C CA  . GLY A 133 ? 0.1647 0.1581 0.1399 -0.0040 0.0194  -0.0021 719 GLY A CA  
1089 C C   . GLY A 133 ? 0.1606 0.1589 0.1353 -0.0007 0.0121  -0.0019 719 GLY A C   
1090 O O   . GLY A 133 ? 0.1554 0.1588 0.1240 0.0028  0.0083  -0.0029 719 GLY A O   
1091 N N   . ILE A 134 ? 0.1517 0.1513 0.1344 -0.0021 0.0100  -0.0019 720 ILE A N   
1092 C CA  . ILE A 134 ? 0.1571 0.1636 0.1417 -0.0002 0.0053  -0.0021 720 ILE A CA  
1093 C C   . ILE A 134 ? 0.1613 0.1629 0.1433 0.0026  0.0057  -0.0011 720 ILE A C   
1094 O O   . ILE A 134 ? 0.1607 0.1579 0.1469 0.0000  0.0074  -0.0024 720 ILE A O   
1095 C CB  . ILE A 134 ? 0.1571 0.1695 0.1507 -0.0039 0.0033  -0.0032 720 ILE A CB  
1096 C CG1 . ILE A 134 ? 0.1695 0.1828 0.1677 -0.0064 0.0030  -0.0052 720 ILE A CG1 
1097 C CG2 . ILE A 134 ? 0.1680 0.1885 0.1629 -0.0031 0.0013  -0.0027 720 ILE A CG2 
1098 C CD1 . ILE A 134 ? 0.2089 0.2183 0.2125 -0.0078 0.0050  -0.0066 720 ILE A CD1 
1099 N N   . PHE A 135 ? 0.1508 0.1546 0.1280 0.0084  0.0034  -0.0006 721 PHE A N   
1100 C CA  . PHE A 135 ? 0.1537 0.1512 0.1285 0.0131  0.0036  -0.0007 721 PHE A CA  
1101 C C   . PHE A 135 ? 0.1618 0.1727 0.1411 0.0166  0.0005  -0.0039 721 PHE A C   
1102 O O   . PHE A 135 ? 0.1662 0.1864 0.1460 0.0207  -0.0023 -0.0046 721 PHE A O   
1103 C CB  . PHE A 135 ? 0.1767 0.1614 0.1404 0.0196  0.0045  0.0035  721 PHE A CB  
1104 C CG  . PHE A 135 ? 0.1983 0.1724 0.1604 0.0257  0.0046  0.0033  721 PHE A CG  
1105 C CD1 . PHE A 135 ? 0.2084 0.1709 0.1751 0.0217  0.0084  0.0010  721 PHE A CD1 
1106 C CD2 . PHE A 135 ? 0.2380 0.2147 0.1960 0.0362  0.0001  0.0037  721 PHE A CD2 
1107 C CE1 . PHE A 135 ? 0.2126 0.1636 0.1788 0.0277  0.0083  -0.0006 721 PHE A CE1 
1108 C CE2 . PHE A 135 ? 0.2470 0.2131 0.2046 0.0436  -0.0002 0.0026  721 PHE A CE2 
1109 C CZ  . PHE A 135 ? 0.2472 0.1989 0.2086 0.0390  0.0043  0.0004  721 PHE A CZ  
1110 N N   . VAL A 136 ? 0.1518 0.1651 0.1348 0.0155  0.0014  -0.0070 722 VAL A N   
1111 C CA  . VAL A 136 ? 0.1512 0.1780 0.1377 0.0186  0.0009  -0.0105 722 VAL A CA  
1112 C C   . VAL A 136 ? 0.1549 0.1755 0.1397 0.0263  0.0007  -0.0144 722 VAL A C   
1113 O O   . VAL A 136 ? 0.1722 0.1807 0.1554 0.0254  0.0018  -0.0166 722 VAL A O   
1114 C CB  . VAL A 136 ? 0.1497 0.1850 0.1378 0.0131  0.0026  -0.0112 722 VAL A CB  
1115 C CG1 . VAL A 136 ? 0.1750 0.2256 0.1655 0.0157  0.0048  -0.0146 722 VAL A CG1 
1116 C CG2 . VAL A 136 ? 0.1534 0.1903 0.1437 0.0063  0.0028  -0.0068 722 VAL A CG2 
1117 N N   . ASP A 137 ? 0.1559 0.1852 0.1435 0.0342  -0.0010 -0.0167 723 ASP A N   
1118 C CA  . ASP A 137 ? 0.1630 0.1885 0.1511 0.0434  -0.0014 -0.0218 723 ASP A CA  
1119 C C   . ASP A 137 ? 0.1561 0.2038 0.1515 0.0441  0.0007  -0.0283 723 ASP A C   
1120 O O   . ASP A 137 ? 0.1536 0.2190 0.1569 0.0475  -0.0001 -0.0301 723 ASP A O   
1121 C CB  . ASP A 137 ? 0.1893 0.2060 0.1744 0.0545  -0.0054 -0.0193 723 ASP A CB  
1122 C CG  . ASP A 137 ? 0.2415 0.2488 0.2278 0.0653  -0.0060 -0.0245 723 ASP A CG  
1123 O OD1 . ASP A 137 ? 0.2330 0.2501 0.2253 0.0659  -0.0037 -0.0330 723 ASP A OD1 
1124 O OD2 . ASP A 137 ? 0.3026 0.2912 0.2822 0.0742  -0.0086 -0.0198 723 ASP A OD2 
1125 N N   . TYR A 138 ? 0.1613 0.2100 0.1541 0.0410  0.0039  -0.0326 724 TYR A N   
1126 C CA  . TYR A 138 ? 0.1668 0.2371 0.1624 0.0393  0.0084  -0.0365 724 TYR A CA  
1127 C C   . TYR A 138 ? 0.1881 0.2722 0.1921 0.0493  0.0093  -0.0442 724 TYR A C   
1128 O O   . TYR A 138 ? 0.1835 0.2897 0.1966 0.0483  0.0127  -0.0457 724 TYR A O   
1129 C CB  . TYR A 138 ? 0.1784 0.2465 0.1648 0.0360  0.0104  -0.0399 724 TYR A CB  
1130 C CG  . TYR A 138 ? 0.1677 0.2555 0.1507 0.0328  0.0166  -0.0402 724 TYR A CG  
1131 C CD1 . TYR A 138 ? 0.1917 0.2951 0.1773 0.0389  0.0213  -0.0485 724 TYR A CD1 
1132 C CD2 . TYR A 138 ? 0.1753 0.2651 0.1530 0.0240  0.0186  -0.0315 724 TYR A CD2 
1133 C CE1 . TYR A 138 ? 0.1957 0.3179 0.1773 0.0351  0.0296  -0.0476 724 TYR A CE1 
1134 C CE2 . TYR A 138 ? 0.1845 0.2892 0.1566 0.0206  0.0261  -0.0291 724 TYR A CE2 
1135 C CZ  . TYR A 138 ? 0.1950 0.3165 0.1691 0.0255  0.0323  -0.0368 724 TYR A CZ  
1136 O OH  . TYR A 138 ? 0.2236 0.3609 0.1914 0.0216  0.0423  -0.0342 724 TYR A OH  
1137 N N   . ARG A 139 ? 0.2108 0.2819 0.2142 0.0591  0.0067  -0.0501 725 ARG A N   
1138 C CA  . ARG A 139 ? 0.2818 0.3651 0.2942 0.0711  0.0070  -0.0592 725 ARG A CA  
1139 C C   . ARG A 139 ? 0.2416 0.3372 0.2649 0.0777  0.0029  -0.0574 725 ARG A C   
1140 O O   . ARG A 139 ? 0.2616 0.3817 0.2978 0.0833  0.0049  -0.0649 725 ARG A O   
1141 C CB  . ARG A 139 ? 0.3595 0.4184 0.3681 0.0799  0.0043  -0.0648 725 ARG A CB  
1142 C CG  . ARG A 139 ? 0.4902 0.5550 0.5072 0.0945  0.0042  -0.0764 725 ARG A CG  
1143 C CD  . ARG A 139 ? 0.6221 0.6535 0.6358 0.1025  0.0006  -0.0788 725 ARG A CD  
1144 N NE  . ARG A 139 ? 0.7031 0.7116 0.7124 0.1049  -0.0043 -0.0663 725 ARG A NE  
1145 C CZ  . ARG A 139 ? 0.8136 0.8135 0.8250 0.1196  -0.0096 -0.0634 725 ARG A CZ  
1146 N NH1 . ARG A 139 ? 0.8154 0.8309 0.8379 0.1339  -0.0114 -0.0734 725 ARG A NH1 
1147 N NH2 . ARG A 139 ? 0.8040 0.7812 0.8057 0.1211  -0.0132 -0.0504 725 ARG A NH2 
1148 N N   . VAL A 140 ? 0.2428 0.3234 0.2614 0.0778  -0.0028 -0.0488 726 VAL A N   
1149 C CA  . VAL A 140 ? 0.2573 0.3489 0.2831 0.0853  -0.0093 -0.0476 726 VAL A CA  
1150 C C   . VAL A 140 ? 0.2395 0.3563 0.2754 0.0745  -0.0073 -0.0474 726 VAL A C   
1151 O O   . VAL A 140 ? 0.2300 0.3677 0.2790 0.0797  -0.0117 -0.0517 726 VAL A O   
1152 C CB  . VAL A 140 ? 0.3081 0.3727 0.3201 0.0892  -0.0154 -0.0379 726 VAL A CB  
1153 C CG1 . VAL A 140 ? 0.3927 0.4695 0.4069 0.0948  -0.0232 -0.0356 726 VAL A CG1 
1154 C CG2 . VAL A 140 ? 0.3454 0.3854 0.3514 0.1018  -0.0170 -0.0386 726 VAL A CG2 
1155 N N   . GLY A 141 ? 0.1871 0.3013 0.2179 0.0602  -0.0014 -0.0430 727 GLY A N   
1156 C CA  . GLY A 141 ? 0.1734 0.3054 0.2133 0.0486  0.0018  -0.0418 727 GLY A CA  
1157 C C   . GLY A 141 ? 0.1727 0.2979 0.2104 0.0454  -0.0043 -0.0368 727 GLY A C   
1158 O O   . GLY A 141 ? 0.1784 0.3221 0.2293 0.0424  -0.0063 -0.0404 727 GLY A O   
1159 N N   . SER A 142 ? 0.1623 0.2624 0.1844 0.0457  -0.0071 -0.0299 728 SER A N   
1160 C CA  . SER A 142 ? 0.1595 0.2531 0.1766 0.0436  -0.0120 -0.0260 728 SER A CA  
1161 C C   . SER A 142 ? 0.1424 0.2188 0.1501 0.0333  -0.0081 -0.0196 728 SER A C   
1162 O O   . SER A 142 ? 0.1557 0.2190 0.1569 0.0314  -0.0044 -0.0172 728 SER A O   
1163 C CB  . SER A 142 ? 0.2042 0.2867 0.2111 0.0562  -0.0193 -0.0238 728 SER A CB  
1164 O OG  . SER A 142 ? 0.2477 0.3041 0.2410 0.0596  -0.0169 -0.0183 728 SER A OG  
1165 N N   . ILE A 143 ? 0.1481 0.2266 0.1574 0.0267  -0.0093 -0.0186 729 ILE A N   
1166 C CA  . ILE A 143 ? 0.1396 0.2032 0.1417 0.0193  -0.0070 -0.0136 729 ILE A CA  
1167 C C   . ILE A 143 ? 0.1550 0.2151 0.1513 0.0212  -0.0114 -0.0135 729 ILE A C   
1168 O O   . ILE A 143 ? 0.1544 0.2288 0.1580 0.0211  -0.0155 -0.0188 729 ILE A O   
1169 C CB  . ILE A 143 ? 0.1544 0.2217 0.1636 0.0086  -0.0023 -0.0126 729 ILE A CB  
1170 C CG1 . ILE A 143 ? 0.1556 0.2085 0.1592 0.0037  -0.0017 -0.0088 729 ILE A CG1 
1171 C CG2 . ILE A 143 ? 0.1601 0.2451 0.1838 0.0035  -0.0016 -0.0168 729 ILE A CG2 
1172 C CD1 . ILE A 143 ? 0.1840 0.2342 0.1907 -0.0039 0.0017  -0.0056 729 ILE A CD1 
1173 N N   . SER A 144 ? 0.1445 0.1869 0.1276 0.0230  -0.0101 -0.0086 730 SER A N   
1174 C CA  . SER A 144 ? 0.1581 0.1955 0.1299 0.0266  -0.0128 -0.0075 730 SER A CA  
1175 C C   . SER A 144 ? 0.1614 0.1893 0.1303 0.0189  -0.0081 -0.0057 730 SER A C   
1176 O O   . SER A 144 ? 0.1717 0.1910 0.1433 0.0139  -0.0032 -0.0032 730 SER A O   
1177 C CB  . SER A 144 ? 0.1867 0.2102 0.1430 0.0367  -0.0136 -0.0018 730 SER A CB  
1178 O OG  . SER A 144 ? 0.2090 0.2402 0.1680 0.0466  -0.0189 -0.0038 730 SER A OG  
1179 N N   . PHE A 145 ? 0.1527 0.1834 0.1163 0.0192  -0.0101 -0.0084 731 PHE A N   
1180 C CA  . PHE A 145 ? 0.1501 0.1753 0.1126 0.0134  -0.0060 -0.0093 731 PHE A CA  
1181 C C   . PHE A 145 ? 0.1668 0.1845 0.1100 0.0188  -0.0042 -0.0066 731 PHE A C   
1182 O O   . PHE A 145 ? 0.1936 0.2164 0.1255 0.0267  -0.0099 -0.0076 731 PHE A O   
1183 C CB  . PHE A 145 ? 0.1491 0.1854 0.1240 0.0082  -0.0091 -0.0174 731 PHE A CB  
1184 C CG  . PHE A 145 ? 0.1473 0.1877 0.1388 0.0016  -0.0083 -0.0176 731 PHE A CG  
1185 C CD1 . PHE A 145 ? 0.1434 0.1954 0.1429 0.0023  -0.0109 -0.0192 731 PHE A CD1 
1186 C CD2 . PHE A 145 ? 0.1456 0.1785 0.1436 -0.0041 -0.0045 -0.0157 731 PHE A CD2 
1187 C CE1 . PHE A 145 ? 0.1333 0.1882 0.1446 -0.0039 -0.0078 -0.0178 731 PHE A CE1 
1188 C CE2 . PHE A 145 ? 0.1351 0.1695 0.1433 -0.0090 -0.0033 -0.0134 731 PHE A CE2 
1189 C CZ  . PHE A 145 ? 0.1345 0.1793 0.1479 -0.0094 -0.0041 -0.0141 731 PHE A CZ  
1190 N N   . TYR A 146 ? 0.1670 0.1742 0.1070 0.0147  0.0036  -0.0035 732 TYR A N   
1191 C CA  . TYR A 146 ? 0.1909 0.1890 0.1116 0.0179  0.0094  0.0008  732 TYR A CA  
1192 C C   . TYR A 146 ? 0.1999 0.2008 0.1236 0.0127  0.0148  -0.0045 732 TYR A C   
1193 O O   . TYR A 146 ? 0.1884 0.1909 0.1295 0.0061  0.0172  -0.0077 732 TYR A O   
1194 C CB  . TYR A 146 ? 0.2128 0.1941 0.1286 0.0169  0.0173  0.0099  732 TYR A CB  
1195 C CG  . TYR A 146 ? 0.2059 0.1815 0.1186 0.0235  0.0125  0.0146  732 TYR A CG  
1196 C CD1 . TYR A 146 ? 0.1971 0.1766 0.1270 0.0206  0.0097  0.0116  732 TYR A CD1 
1197 C CD2 . TYR A 146 ? 0.2494 0.2163 0.1416 0.0338  0.0103  0.0214  732 TYR A CD2 
1198 C CE1 . TYR A 146 ? 0.2114 0.1869 0.1401 0.0272  0.0060  0.0138  732 TYR A CE1 
1199 C CE2 . TYR A 146 ? 0.2541 0.2156 0.1460 0.0416  0.0054  0.0245  732 TYR A CE2 
1200 C CZ  . TYR A 146 ? 0.2467 0.2138 0.1583 0.0379  0.0034  0.0197  732 TYR A CZ  
1201 O OH  . TYR A 146 ? 0.2812 0.2443 0.1940 0.0460  -0.0006 0.0208  732 TYR A OH  
1202 N N   . ASN A 147 ? 0.2058 0.2069 0.1104 0.0170  0.0171  -0.0050 733 ASN A N   
1203 C CA  . ASN A 147 ? 0.2172 0.2198 0.1200 0.0137  0.0252  -0.0095 733 ASN A CA  
1204 C C   . ASN A 147 ? 0.2332 0.2228 0.1282 0.0107  0.0384  0.0000  733 ASN A C   
1205 O O   . ASN A 147 ? 0.2499 0.2298 0.1207 0.0156  0.0430  0.0086  733 ASN A O   
1206 C CB  . ASN A 147 ? 0.2495 0.2600 0.1332 0.0204  0.0210  -0.0157 733 ASN A CB  
1207 C CG  . ASN A 147 ? 0.2541 0.2676 0.1329 0.0185  0.0300  -0.0222 733 ASN A CG  
1208 O OD1 . ASN A 147 ? 0.2473 0.2561 0.1329 0.0129  0.0417  -0.0193 733 ASN A OD1 
1209 N ND2 . ASN A 147 ? 0.2868 0.3102 0.1538 0.0235  0.0250  -0.0324 733 ASN A ND2 
1210 N N   . VAL A 148 ? 0.2151 0.2041 0.1314 0.0029  0.0440  -0.0014 734 VAL A N   
1211 C CA  . VAL A 148 ? 0.2317 0.2100 0.1477 -0.0022 0.0565  0.0056  734 VAL A CA  
1212 C C   . VAL A 148 ? 0.2608 0.2395 0.1633 -0.0035 0.0698  0.0058  734 VAL A C   
1213 O O   . VAL A 148 ? 0.2971 0.2632 0.1878 -0.0062 0.0822  0.0152  734 VAL A O   
1214 C CB  . VAL A 148 ? 0.2267 0.2082 0.1714 -0.0095 0.0562  0.0015  734 VAL A CB  
1215 C CG1 . VAL A 148 ? 0.2451 0.2186 0.1958 -0.0170 0.0697  0.0053  734 VAL A CG1 
1216 C CG2 . VAL A 148 ? 0.2297 0.2098 0.1817 -0.0076 0.0451  0.0026  734 VAL A CG2 
1217 N N   . THR A 149 ? 0.2581 0.2502 0.1630 -0.0019 0.0685  -0.0046 735 THR A N   
1218 C CA  . THR A 149 ? 0.2806 0.2764 0.1713 -0.0020 0.0813  -0.0067 735 THR A CA  
1219 C C   . THR A 149 ? 0.3164 0.3019 0.1686 0.0050  0.0845  0.0037  735 THR A C   
1220 O O   . THR A 149 ? 0.3522 0.3304 0.1878 0.0028  0.0999  0.0114  735 THR A O   
1221 C CB  . THR A 149 ? 0.2865 0.2977 0.1861 0.0006  0.0760  -0.0222 735 THR A CB  
1222 O OG1 . THR A 149 ? 0.2621 0.2789 0.1947 -0.0036 0.0709  -0.0289 735 THR A OG1 
1223 C CG2 . THR A 149 ? 0.3281 0.3467 0.2170 0.0008  0.0898  -0.0278 735 THR A CG2 
1224 N N   . ALA A 150 ? 0.3258 0.3123 0.1633 0.0140  0.0701  0.0035  736 ALA A N   
1225 C CA  . ALA A 150 ? 0.3568 0.3354 0.1568 0.0238  0.0690  0.0127  736 ALA A CA  
1226 C C   . ALA A 150 ? 0.3635 0.3218 0.1547 0.0259  0.0694  0.0290  736 ALA A C   
1227 O O   . ALA A 150 ? 0.4058 0.3514 0.1641 0.0338  0.0726  0.0410  736 ALA A O   
1228 C CB  . ALA A 150 ? 0.3630 0.3555 0.1569 0.0330  0.0513  0.0022  736 ALA A CB  
1229 N N   A ARG A 151 ? 0.3174 0.2721 0.1365 0.0195  0.0665  0.0291  737 ARG A N   
1230 N N   B ARG A 151 ? 0.3352 0.2903 0.1539 0.0202  0.0654  0.0289  737 ARG A N   
1231 C CA  A ARG A 151 ? 0.3198 0.2575 0.1374 0.0222  0.0634  0.0400  737 ARG A CA  
1232 C CA  B ARG A 151 ? 0.3569 0.2937 0.1729 0.0224  0.0638  0.0406  737 ARG A CA  
1233 C C   A ARG A 151 ? 0.3378 0.2778 0.1371 0.0361  0.0480  0.0416  737 ARG A C   
1234 C C   B ARG A 151 ? 0.3558 0.2951 0.1590 0.0356  0.0473  0.0416  737 ARG A C   
1235 O O   A ARG A 151 ? 0.3665 0.2903 0.1390 0.0454  0.0486  0.0542  737 ARG A O   
1236 O O   B ARG A 151 ? 0.3900 0.3124 0.1759 0.0435  0.0461  0.0534  737 ARG A O   
1237 C CB  A ARG A 151 ? 0.3388 0.2518 0.1425 0.0187  0.0793  0.0550  737 ARG A CB  
1238 C CB  B ARG A 151 ? 0.4058 0.3192 0.2012 0.0205  0.0803  0.0560  737 ARG A CB  
1239 C CG  A ARG A 151 ? 0.3284 0.2423 0.1541 0.0039  0.0954  0.0519  737 ARG A CG  
1240 C CG  B ARG A 151 ? 0.4267 0.3383 0.2436 0.0055  0.0972  0.0544  737 ARG A CG  
1241 C CD  A ARG A 151 ? 0.3389 0.2604 0.1490 0.0024  0.1077  0.0506  737 ARG A CD  
1242 C CD  B ARG A 151 ? 0.4538 0.3787 0.2683 0.0005  0.1094  0.0483  737 ARG A CD  
1243 N NE  A ARG A 151 ? 0.3763 0.2797 0.1450 0.0100  0.1154  0.0662  737 ARG A NE  
1244 N NE  B ARG A 151 ? 0.4720 0.3936 0.3130 -0.0135 0.1238  0.0476  737 ARG A NE  
1245 C CZ  A ARG A 151 ? 0.4051 0.2845 0.1604 0.0049  0.1330  0.0815  737 ARG A CZ  
1246 C CZ  B ARG A 151 ? 0.4888 0.3871 0.3268 -0.0187 0.1340  0.0600  737 ARG A CZ  
1247 N NH1 A ARG A 151 ? 0.4299 0.2907 0.1459 0.0153  0.1346  0.0969  737 ARG A NH1 
1248 N NH1 B ARG A 151 ? 0.4321 0.3272 0.3009 -0.0276 0.1336  0.0561  737 ARG A NH1 
1249 N NH2 A ARG A 151 ? 0.4011 0.2756 0.1840 -0.0103 0.1474  0.0808  737 ARG A NH2 
1250 N NH2 B ARG A 151 ? 0.5236 0.3996 0.3256 -0.0122 0.1403  0.0764  737 ARG A NH2 
1251 N N   . SER A 152 ? 0.3199 0.2804 0.1345 0.0378  0.0346  0.0285  738 SER A N   
1252 C CA  . SER A 152 ? 0.3324 0.3022 0.1372 0.0499  0.0188  0.0257  738 SER A CA  
1253 C C   . SER A 152 ? 0.3047 0.2877 0.1399 0.0467  0.0084  0.0166  738 SER A C   
1254 O O   . SER A 152 ? 0.2952 0.2830 0.1551 0.0361  0.0116  0.0104  738 SER A O   
1255 C CB  . SER A 152 ? 0.3622 0.3478 0.1502 0.0559  0.0130  0.0164  738 SER A CB  
1256 O OG  . SER A 152 ? 0.3808 0.3806 0.1922 0.0461  0.0141  0.0021  738 SER A OG  
1257 N N   . HIS A 153 ? 0.3077 0.2962 0.1410 0.0565  -0.0034 0.0165  739 HIS A N   
1258 C CA  . HIS A 153 ? 0.2814 0.2848 0.1420 0.0539  -0.0121 0.0079  739 HIS A CA  
1259 C C   . HIS A 153 ? 0.2942 0.3200 0.1654 0.0515  -0.0200 -0.0068 739 HIS A C   
1260 O O   . HIS A 153 ? 0.3158 0.3493 0.1697 0.0586  -0.0256 -0.0114 739 HIS A O   
1261 C CB  . HIS A 153 ? 0.3122 0.3154 0.1680 0.0664  -0.0211 0.0120  739 HIS A CB  
1262 C CG  . HIS A 153 ? 0.2987 0.3221 0.1805 0.0656  -0.0300 0.0020  739 HIS A CG  
1263 N ND1 . HIS A 153 ? 0.3187 0.3656 0.2056 0.0718  -0.0424 -0.0087 739 HIS A ND1 
1264 C CD2 . HIS A 153 ? 0.2812 0.3067 0.1855 0.0585  -0.0273 0.0002  739 HIS A CD2 
1265 C CE1 . HIS A 153 ? 0.2586 0.3202 0.1724 0.0673  -0.0452 -0.0157 739 HIS A CE1 
1266 N NE2 . HIS A 153 ? 0.2639 0.3124 0.1863 0.0601  -0.0361 -0.0097 739 HIS A NE2 
1267 N N   . ILE A 154 ? 0.2406 0.2750 0.1388 0.0411  -0.0198 -0.0145 740 ILE A N   
1268 C CA  . ILE A 154 ? 0.2404 0.2919 0.1543 0.0360  -0.0255 -0.0287 740 ILE A CA  
1269 C C   . ILE A 154 ? 0.2217 0.2903 0.1533 0.0378  -0.0351 -0.0349 740 ILE A C   
1270 O O   . ILE A 154 ? 0.2340 0.3199 0.1699 0.0404  -0.0443 -0.0464 740 ILE A O   
1271 C CB  . ILE A 154 ? 0.2606 0.3073 0.1935 0.0236  -0.0180 -0.0313 740 ILE A CB  
1272 C CG1 . ILE A 154 ? 0.3047 0.3402 0.2260 0.0216  -0.0085 -0.0289 740 ILE A CG1 
1273 C CG2 . ILE A 154 ? 0.2743 0.3342 0.2280 0.0172  -0.0233 -0.0448 740 ILE A CG2 
1274 C CD1 . ILE A 154 ? 0.2849 0.3165 0.2263 0.0122  -0.0030 -0.0312 740 ILE A CD1 
1275 N N   . TYR A 155 ? 0.1915 0.2579 0.1377 0.0343  -0.0322 -0.0300 741 TYR A N   
1276 C CA  . TYR A 155 ? 0.1781 0.2629 0.1456 0.0332  -0.0379 -0.0368 741 TYR A CA  
1277 C C   . TYR A 155 ? 0.1745 0.2542 0.1484 0.0335  -0.0336 -0.0293 741 TYR A C   
1278 O O   . TYR A 155 ? 0.1788 0.2429 0.1506 0.0282  -0.0255 -0.0221 741 TYR A O   
1279 C CB  . TYR A 155 ? 0.1834 0.2754 0.1732 0.0200  -0.0358 -0.0456 741 TYR A CB  
1280 C CG  . TYR A 155 ? 0.1590 0.2723 0.1733 0.0162  -0.0398 -0.0543 741 TYR A CG  
1281 C CD1 . TYR A 155 ? 0.1625 0.2963 0.1832 0.0202  -0.0500 -0.0670 741 TYR A CD1 
1282 C CD2 . TYR A 155 ? 0.1454 0.2600 0.1757 0.0090  -0.0334 -0.0505 741 TYR A CD2 
1283 C CE1 . TYR A 155 ? 0.1607 0.3180 0.2078 0.0162  -0.0535 -0.0771 741 TYR A CE1 
1284 C CE2 . TYR A 155 ? 0.1487 0.2847 0.2021 0.0048  -0.0350 -0.0587 741 TYR A CE2 
1285 C CZ  . TYR A 155 ? 0.1517 0.3093 0.2156 0.0078  -0.0446 -0.0721 741 TYR A CZ  
1286 O OH  . TYR A 155 ? 0.1818 0.3647 0.2732 0.0030  -0.0460 -0.0824 741 TYR A OH  
1287 N N   . THR A 156 ? 0.1608 0.2564 0.1453 0.0391  -0.0392 -0.0334 742 THR A N   
1288 C CA  . THR A 156 ? 0.1580 0.2535 0.1519 0.0391  -0.0349 -0.0298 742 THR A CA  
1289 C C   . THR A 156 ? 0.1471 0.2673 0.1669 0.0334  -0.0359 -0.0393 742 THR A C   
1290 O O   . THR A 156 ? 0.1582 0.2993 0.1879 0.0378  -0.0442 -0.0489 742 THR A O   
1291 C CB  . THR A 156 ? 0.1993 0.2888 0.1803 0.0543  -0.0392 -0.0249 742 THR A CB  
1292 O OG1 . THR A 156 ? 0.2179 0.2810 0.1778 0.0552  -0.0340 -0.0145 742 THR A OG1 
1293 C CG2 . THR A 156 ? 0.1979 0.2917 0.1912 0.0560  -0.0361 -0.0252 742 THR A CG2 
1294 N N   . PHE A 157 ? 0.1358 0.2542 0.1658 0.0244  -0.0273 -0.0366 743 PHE A N   
1295 C CA  . PHE A 157 ? 0.1286 0.2685 0.1805 0.0201  -0.0247 -0.0428 743 PHE A CA  
1296 C C   . PHE A 157 ? 0.1493 0.2926 0.1997 0.0307  -0.0244 -0.0415 743 PHE A C   
1297 O O   . PHE A 157 ? 0.1528 0.2783 0.1909 0.0318  -0.0195 -0.0342 743 PHE A O   
1298 C CB  . PHE A 157 ? 0.1148 0.2498 0.1744 0.0060  -0.0142 -0.0390 743 PHE A CB  
1299 C CG  . PHE A 157 ? 0.1118 0.2404 0.1764 -0.0054 -0.0125 -0.0398 743 PHE A CG  
1300 C CD1 . PHE A 157 ? 0.1245 0.2316 0.1743 -0.0064 -0.0120 -0.0339 743 PHE A CD1 
1301 C CD2 . PHE A 157 ? 0.1239 0.2683 0.2108 -0.0153 -0.0109 -0.0478 743 PHE A CD2 
1302 C CE1 . PHE A 157 ? 0.1387 0.2383 0.1940 -0.0155 -0.0104 -0.0354 743 PHE A CE1 
1303 C CE2 . PHE A 157 ? 0.1262 0.2599 0.2181 -0.0258 -0.0086 -0.0484 743 PHE A CE2 
1304 C CZ  . PHE A 157 ? 0.1367 0.2483 0.2126 -0.0248 -0.0090 -0.0426 743 PHE A CZ  
1305 N N   . ALA A 158 ? 0.1699 0.3361 0.2338 0.0390  -0.0303 -0.0500 744 ALA A N   
1306 C CA  . ALA A 158 ? 0.1860 0.3562 0.2504 0.0513  -0.0308 -0.0506 744 ALA A CA  
1307 C C   . ALA A 158 ? 0.1959 0.3939 0.2858 0.0461  -0.0244 -0.0591 744 ALA A C   
1308 O O   . ALA A 158 ? 0.1950 0.4116 0.3040 0.0346  -0.0216 -0.0652 744 ALA A O   
1309 C CB  . ALA A 158 ? 0.2339 0.4073 0.2916 0.0692  -0.0437 -0.0531 744 ALA A CB  
1310 N N   . SER A 159 ? 0.2032 0.4046 0.2945 0.0553  -0.0219 -0.0606 745 SER A N   
1311 C CA  . SER A 159 ? 0.2305 0.4591 0.3441 0.0519  -0.0137 -0.0688 745 SER A CA  
1312 C C   . SER A 159 ? 0.2136 0.4412 0.3300 0.0326  -0.0003 -0.0644 745 SER A C   
1313 O O   . SER A 159 ? 0.2196 0.4721 0.3584 0.0232  0.0068  -0.0707 745 SER A O   
1314 C CB  . SER A 159 ? 0.2773 0.5417 0.4186 0.0568  -0.0204 -0.0822 745 SER A CB  
1315 O OG  . SER A 159 ? 0.3395 0.6033 0.4751 0.0769  -0.0349 -0.0849 745 SER A OG  
1316 N N   . CYS A 160 ? 0.1850 0.3847 0.2796 0.0274  0.0036  -0.0537 746 CYS A N   
1317 C CA  . CYS A 160 ? 0.1877 0.3824 0.2805 0.0117  0.0146  -0.0473 746 CYS A CA  
1318 C C   . CYS A 160 ? 0.2201 0.4262 0.3145 0.0097  0.0266  -0.0481 746 CYS A C   
1319 O O   . CYS A 160 ? 0.2572 0.4636 0.3515 -0.0028 0.0371  -0.0427 746 CYS A O   
1320 C CB  . CYS A 160 ? 0.1782 0.3419 0.2480 0.0089  0.0134  -0.0367 746 CYS A CB  
1321 S SG  . CYS A 160 ? 0.1883 0.3381 0.2536 0.0091  0.0028  -0.0353 746 CYS A SG  
1322 N N   . SER A 161 ? 0.2247 0.4369 0.3175 0.0226  0.0253  -0.0540 747 SER A N   
1323 C CA  . SER A 161 ? 0.2836 0.5090 0.3766 0.0227  0.0368  -0.0572 747 SER A CA  
1324 C C   . SER A 161 ? 0.2593 0.4677 0.3313 0.0131  0.0452  -0.0468 747 SER A C   
1325 O O   . SER A 161 ? 0.2990 0.5192 0.3728 0.0040  0.0576  -0.0445 747 SER A O   
1326 C CB  . SER A 161 ? 0.3592 0.6195 0.4791 0.0173  0.0458  -0.0655 747 SER A CB  
1327 O OG  . SER A 161 ? 0.4400 0.7191 0.5808 0.0280  0.0358  -0.0765 747 SER A OG  
1328 N N   . PHE A 162 ? 0.2202 0.4013 0.2719 0.0157  0.0384  -0.0405 748 PHE A N   
1329 C CA  . PHE A 162 ? 0.2174 0.3831 0.2492 0.0092  0.0429  -0.0316 748 PHE A CA  
1330 C C   . PHE A 162 ? 0.2349 0.4106 0.2564 0.0122  0.0517  -0.0351 748 PHE A C   
1331 O O   . PHE A 162 ? 0.2592 0.4400 0.2808 0.0230  0.0499  -0.0448 748 PHE A O   
1332 C CB  . PHE A 162 ? 0.1964 0.3363 0.2130 0.0141  0.0330  -0.0287 748 PHE A CB  
1333 C CG  . PHE A 162 ? 0.1883 0.3152 0.2088 0.0122  0.0249  -0.0249 748 PHE A CG  
1334 C CD1 . PHE A 162 ? 0.1758 0.3028 0.2026 0.0021  0.0266  -0.0194 748 PHE A CD1 
1335 C CD2 . PHE A 162 ? 0.1761 0.2891 0.1933 0.0204  0.0164  -0.0268 748 PHE A CD2 
1336 C CE1 . PHE A 162 ? 0.1793 0.2954 0.2080 0.0010  0.0196  -0.0175 748 PHE A CE1 
1337 C CE2 . PHE A 162 ? 0.1719 0.2746 0.1897 0.0189  0.0106  -0.0233 748 PHE A CE2 
1338 C CZ  . PHE A 162 ? 0.1859 0.2909 0.2089 0.0094  0.0119  -0.0194 748 PHE A CZ  
1339 N N   . SER A 163 ? 0.2249 0.4009 0.2346 0.0033  0.0613  -0.0266 749 SER A N   
1340 C CA  . SER A 163 ? 0.2261 0.4094 0.2185 0.0064  0.0696  -0.0285 749 SER A CA  
1341 C C   . SER A 163 ? 0.2152 0.3808 0.1835 0.0008  0.0703  -0.0153 749 SER A C   
1342 O O   . SER A 163 ? 0.2056 0.3618 0.1756 -0.0084 0.0720  -0.0041 749 SER A O   
1343 C CB  . SER A 163 ? 0.2713 0.4825 0.2754 0.0034  0.0842  -0.0331 749 SER A CB  
1344 O OG  . SER A 163 ? 0.3064 0.5213 0.3212 -0.0103 0.0928  -0.0237 749 SER A OG  
1345 N N   . GLY A 164 ? 0.2175 0.3779 0.1640 0.0079  0.0674  -0.0182 750 GLY A N   
1346 C CA  . GLY A 164 ? 0.2202 0.3654 0.1424 0.0067  0.0644  -0.0081 750 GLY A CA  
1347 C C   . GLY A 164 ? 0.2144 0.3389 0.1398 0.0069  0.0507  -0.0052 750 GLY A C   
1348 O O   . GLY A 164 ? 0.2010 0.3213 0.1441 0.0079  0.0443  -0.0105 750 GLY A O   
1349 N N   . PRO A 165 ? 0.2167 0.3286 0.1238 0.0072  0.0458  0.0027  751 PRO A N   
1350 C CA  . PRO A 165 ? 0.2153 0.3111 0.1264 0.0085  0.0332  0.0027  751 PRO A CA  
1351 C C   . PRO A 165 ? 0.1981 0.2837 0.1250 0.0014  0.0323  0.0107  751 PRO A C   
1352 O O   . PRO A 165 ? 0.2031 0.2879 0.1308 -0.0053 0.0401  0.0208  751 PRO A O   
1353 C CB  . PRO A 165 ? 0.2479 0.3387 0.1351 0.0127  0.0284  0.0075  751 PRO A CB  
1354 C CG  . PRO A 165 ? 0.2935 0.3963 0.1602 0.0151  0.0372  0.0085  751 PRO A CG  
1355 C CD  . PRO A 165 ? 0.2606 0.3748 0.1404 0.0087  0.0510  0.0100  751 PRO A CD  
1356 N N   . LEU A 166 ? 0.1719 0.2486 0.1094 0.0031  0.0233  0.0058  752 LEU A N   
1357 C CA  . LEU A 166 ? 0.1729 0.2397 0.1235 -0.0017 0.0207  0.0105  752 LEU A CA  
1358 C C   . LEU A 166 ? 0.1837 0.2382 0.1296 0.0004  0.0119  0.0124  752 LEU A C   
1359 O O   . LEU A 166 ? 0.1883 0.2435 0.1275 0.0056  0.0063  0.0061  752 LEU A O   
1360 C CB  . LEU A 166 ? 0.1672 0.2355 0.1341 -0.0013 0.0185  0.0033  752 LEU A CB  
1361 C CG  . LEU A 166 ? 0.1996 0.2832 0.1750 -0.0004 0.0242  -0.0020 752 LEU A CG  
1362 C CD1 . LEU A 166 ? 0.2021 0.2837 0.1893 0.0026  0.0192  -0.0073 752 LEU A CD1 
1363 C CD2 . LEU A 166 ? 0.2373 0.3300 0.2192 -0.0081 0.0328  0.0035  752 LEU A CD2 
1364 N N   . GLN A 167 ? 0.1756 0.2202 0.1276 -0.0032 0.0106  0.0191  753 GLN A N   
1365 C CA  . GLN A 167 ? 0.1688 0.2044 0.1209 -0.0002 0.0023  0.0190  753 GLN A CA  
1366 C C   . GLN A 167 ? 0.1658 0.1938 0.1327 -0.0040 0.0016  0.0194  753 GLN A C   
1367 O O   . GLN A 167 ? 0.1653 0.1925 0.1390 -0.0092 0.0066  0.0223  753 GLN A O   
1368 C CB  . GLN A 167 ? 0.2068 0.2373 0.1445 0.0033  -0.0007 0.0273  753 GLN A CB  
1369 C CG  . GLN A 167 ? 0.2147 0.2350 0.1503 -0.0009 0.0047  0.0399  753 GLN A CG  
1370 C CD  . GLN A 167 ? 0.2594 0.2731 0.1743 0.0043  0.0030  0.0508  753 GLN A CD  
1371 O OE1 . GLN A 167 ? 0.3203 0.3302 0.2238 0.0009  0.0119  0.0616  753 GLN A OE1 
1372 N NE2 . GLN A 167 ? 0.2753 0.2882 0.1848 0.0127  -0.0080 0.0485  753 GLN A NE2 
1373 N N   . PRO A 168 ? 0.1510 0.1747 0.1243 -0.0019 -0.0042 0.0153  754 PRO A N   
1374 C CA  . PRO A 168 ? 0.1450 0.1621 0.1300 -0.0045 -0.0044 0.0149  754 PRO A CA  
1375 C C   . PRO A 168 ? 0.1630 0.1708 0.1479 -0.0057 -0.0039 0.0230  754 PRO A C   
1376 O O   . PRO A 168 ? 0.1661 0.1699 0.1410 -0.0025 -0.0057 0.0299  754 PRO A O   
1377 C CB  . PRO A 168 ? 0.1478 0.1648 0.1388 -0.0015 -0.0095 0.0089  754 PRO A CB  
1378 C CG  . PRO A 168 ? 0.1471 0.1707 0.1331 0.0006  -0.0110 0.0034  754 PRO A CG  
1379 C CD  . PRO A 168 ? 0.1587 0.1857 0.1307 0.0025  -0.0102 0.0085  754 PRO A CD  
1380 N N   . ILE A 169 ? 0.1507 0.1536 0.1459 -0.0100 -0.0015 0.0220  755 ILE A N   
1381 C CA  . ILE A 169 ? 0.1645 0.1550 0.1633 -0.0119 -0.0006 0.0279  755 ILE A CA  
1382 C C   . ILE A 169 ? 0.1558 0.1419 0.1672 -0.0117 -0.0028 0.0208  755 ILE A C   
1383 O O   . ILE A 169 ? 0.1500 0.1434 0.1659 -0.0129 -0.0022 0.0130  755 ILE A O   
1384 C CB  . ILE A 169 ? 0.1759 0.1653 0.1759 -0.0196 0.0067  0.0326  755 ILE A CB  
1385 C CG1 . ILE A 169 ? 0.2163 0.1880 0.2198 -0.0226 0.0090  0.0401  755 ILE A CG1 
1386 C CG2 . ILE A 169 ? 0.1754 0.1753 0.1864 -0.0243 0.0088  0.0235  755 ILE A CG2 
1387 C CD1 . ILE A 169 ? 0.2481 0.2185 0.2540 -0.0323 0.0185  0.0457  755 ILE A CD1 
1388 N N   . PHE A 170 ? 0.1667 0.1401 0.1817 -0.0089 -0.0052 0.0241  756 PHE A N   
1389 C CA  . PHE A 170 ? 0.1667 0.1363 0.1938 -0.0071 -0.0072 0.0163  756 PHE A CA  
1390 C C   . PHE A 170 ? 0.1878 0.1394 0.2210 -0.0079 -0.0066 0.0200  756 PHE A C   
1391 O O   . PHE A 170 ? 0.2091 0.1483 0.2359 -0.0057 -0.0072 0.0308  756 PHE A O   
1392 C CB  . PHE A 170 ? 0.1728 0.1464 0.2021 0.0009  -0.0128 0.0134  756 PHE A CB  
1393 C CG  . PHE A 170 ? 0.1649 0.1527 0.1894 0.0018  -0.0138 0.0104  756 PHE A CG  
1394 C CD1 . PHE A 170 ? 0.1848 0.1752 0.1978 0.0043  -0.0166 0.0164  756 PHE A CD1 
1395 C CD2 . PHE A 170 ? 0.1659 0.1625 0.1964 0.0003  -0.0116 0.0018  756 PHE A CD2 
1396 C CE1 . PHE A 170 ? 0.1737 0.1757 0.1842 0.0046  -0.0176 0.0113  756 PHE A CE1 
1397 C CE2 . PHE A 170 ? 0.1708 0.1763 0.1985 0.0000  -0.0117 -0.0007 756 PHE A CE2 
1398 C CZ  . PHE A 170 ? 0.1594 0.1674 0.1784 0.0021  -0.0152 0.0031  756 PHE A CZ  
1399 N N   . SER A 171 ? 0.1767 0.1256 0.2220 -0.0094 -0.0060 0.0104  757 SER A N   
1400 C CA  . SER A 171 ? 0.1952 0.1253 0.2495 -0.0074 -0.0070 0.0106  757 SER A CA  
1401 C C   . SER A 171 ? 0.1818 0.1157 0.2472 -0.0028 -0.0089 -0.0028 757 SER A C   
1402 O O   . SER A 171 ? 0.1795 0.1245 0.2468 -0.0068 -0.0065 -0.0129 757 SER A O   
1403 C CB  . SER A 171 ? 0.2133 0.1312 0.2742 -0.0170 -0.0020 0.0111  757 SER A CB  
1404 O OG  . SER A 171 ? 0.2460 0.1425 0.3173 -0.0143 -0.0031 0.0097  757 SER A OG  
1405 N N   . PRO A 172 ? 0.1952 0.1207 0.2673 0.0065  -0.0132 -0.0034 758 PRO A N   
1406 C CA  . PRO A 172 ? 0.2102 0.1403 0.2948 0.0107  -0.0132 -0.0178 758 PRO A CA  
1407 C C   . PRO A 172 ? 0.2128 0.1288 0.3076 0.0075  -0.0111 -0.0266 758 PRO A C   
1408 O O   . PRO A 172 ? 0.2251 0.1437 0.3297 0.0116  -0.0107 -0.0401 758 PRO A O   
1409 C CB  . PRO A 172 ? 0.2152 0.1441 0.3060 0.0230  -0.0192 -0.0160 758 PRO A CB  
1410 C CG  . PRO A 172 ? 0.2286 0.1389 0.3105 0.0255  -0.0229 0.0000  758 PRO A CG  
1411 C CD  . PRO A 172 ? 0.2095 0.1230 0.2770 0.0149  -0.0184 0.0087  758 PRO A CD  
1412 N N   . GLY A 173 ? 0.2351 0.1365 0.3289 -0.0005 -0.0091 -0.0204 759 GLY A N   
1413 C CA  . GLY A 173 ? 0.2539 0.1408 0.3602 -0.0054 -0.0073 -0.0302 759 GLY A CA  
1414 C C   . GLY A 173 ? 0.3098 0.1712 0.4270 0.0025  -0.0098 -0.0295 759 GLY A C   
1415 O O   . GLY A 173 ? 0.2934 0.1499 0.4084 0.0137  -0.0141 -0.0214 759 GLY A O   
1416 N N   . THR A 174 ? 0.3780 0.2229 0.5086 -0.0022 -0.0080 -0.0398 760 THR A N   
1417 C CA  . THR A 174 ? 0.4200 0.2376 0.5626 0.0064  -0.0105 -0.0410 760 THR A CA  
1418 C C   . THR A 174 ? 0.4187 0.2487 0.5706 0.0175  -0.0132 -0.0593 760 THR A C   
1419 O O   . THR A 174 ? 0.3794 0.2364 0.5272 0.0164  -0.0117 -0.0703 760 THR A O   
1420 C CB  . THR A 174 ? 0.5102 0.2996 0.6653 -0.0034 -0.0068 -0.0432 760 THR A CB  
1421 O OG1 . THR A 174 ? 0.5242 0.3286 0.6889 -0.0092 -0.0060 -0.0663 760 THR A OG1 
1422 C CG2 . THR A 174 ? 0.5289 0.3127 0.6769 -0.0173 -0.0012 -0.0277 760 THR A CG2 
1423 N N   . ARG A 175 ? 0.4338 0.2437 0.5976 0.0295  -0.0166 -0.0617 761 ARG A N   
1424 C CA  . ARG A 175 ? 0.4479 0.2730 0.6210 0.0426  -0.0188 -0.0767 761 ARG A CA  
1425 C C   . ARG A 175 ? 0.4278 0.2619 0.6100 0.0393  -0.0149 -0.1016 761 ARG A C   
1426 O O   . ARG A 175 ? 0.3769 0.2321 0.5631 0.0473  -0.0137 -0.1150 761 ARG A O   
1427 C CB  . ARG A 175 ? 0.4952 0.2976 0.6793 0.0591  -0.0250 -0.0716 761 ARG A CB  
1428 C CG  . ARG A 175 ? 0.5307 0.3344 0.7034 0.0670  -0.0309 -0.0504 761 ARG A CG  
1429 C CD  . ARG A 175 ? 0.6020 0.3811 0.7818 0.0856  -0.0395 -0.0419 761 ARG A CD  
1430 N NE  . ARG A 175 ? 0.6041 0.3942 0.8047 0.1010  -0.0429 -0.0604 761 ARG A NE  
1431 C CZ  . ARG A 175 ? 0.6301 0.4467 0.8374 0.1141  -0.0486 -0.0640 761 ARG A CZ  
1432 N NH1 . ARG A 175 ? 0.5972 0.4308 0.7918 0.1147  -0.0531 -0.0505 761 ARG A NH1 
1433 N NH2 . ARG A 175 ? 0.6317 0.4597 0.8609 0.1267  -0.0497 -0.0829 761 ARG A NH2 
1434 N N   . ASP A 176 ? 0.4186 0.2379 0.6047 0.0278  -0.0129 -0.1085 762 ASP A N   
1435 C CA  . ASP A 176 ? 0.4220 0.2516 0.6133 0.0227  -0.0105 -0.1327 762 ASP A CA  
1436 C C   . ASP A 176 ? 0.4388 0.2663 0.6440 0.0360  -0.0109 -0.1525 762 ASP A C   
1437 O O   . ASP A 176 ? 0.4255 0.2790 0.6265 0.0396  -0.0079 -0.1685 762 ASP A O   
1438 C CB  . ASP A 176 ? 0.4065 0.2696 0.5812 0.0156  -0.0080 -0.1368 762 ASP A CB  
1439 C CG  . ASP A 176 ? 0.4271 0.3024 0.6017 0.0105  -0.0071 -0.1606 762 ASP A CG  
1440 O OD1 . ASP A 176 ? 0.4663 0.3227 0.6559 0.0064  -0.0086 -0.1742 762 ASP A OD1 
1441 O OD2 . ASP A 176 ? 0.3913 0.2948 0.5500 0.0112  -0.0050 -0.1660 762 ASP A OD2 
1442 N N   . GLY A 177 ? 0.4684 0.2639 0.6888 0.0439  -0.0139 -0.1495 763 GLY A N   
1443 C CA  . GLY A 177 ? 0.4982 0.2853 0.7359 0.0585  -0.0151 -0.1671 763 GLY A CA  
1444 C C   . GLY A 177 ? 0.4789 0.2968 0.7162 0.0719  -0.0142 -0.1723 763 GLY A C   
1445 O O   . GLY A 177 ? 0.5796 0.4038 0.8295 0.0820  -0.0125 -0.1935 763 GLY A O   
1446 N N   . GLY A 178 ? 0.4578 0.2949 0.6831 0.0720  -0.0147 -0.1547 764 GLY A N   
1447 C CA  . GLY A 178 ? 0.4127 0.2813 0.6404 0.0817  -0.0125 -0.1601 764 GLY A CA  
1448 C C   . GLY A 178 ? 0.3666 0.2695 0.5780 0.0721  -0.0047 -0.1651 764 GLY A C   
1449 O O   . GLY A 178 ? 0.3663 0.2953 0.5781 0.0764  -0.0010 -0.1656 764 GLY A O   
1450 N N   . LYS A 179 ? 0.3338 0.2368 0.5300 0.0584  -0.0025 -0.1659 765 LYS A N   
1451 C CA  . LYS A 179 ? 0.3281 0.2601 0.5058 0.0512  0.0039  -0.1689 765 LYS A CA  
1452 C C   . LYS A 179 ? 0.2854 0.2259 0.4486 0.0441  0.0032  -0.1471 765 LYS A C   
1453 O O   . LYS A 179 ? 0.2996 0.2625 0.4483 0.0400  0.0088  -0.1456 765 LYS A O   
1454 C CB  . LYS A 179 ? 0.3665 0.2980 0.5347 0.0426  0.0048  -0.1830 765 LYS A CB  
1455 C CG  . LYS A 179 ? 0.4377 0.3651 0.6175 0.0493  0.0062  -0.2085 765 LYS A CG  
1456 C CD  . LYS A 179 ? 0.5283 0.4512 0.7030 0.0411  0.0040  -0.2246 765 LYS A CD  
1457 C CE  . LYS A 179 ? 0.6393 0.5569 0.8273 0.0492  0.0050  -0.2514 765 LYS A CE  
1458 N NZ  . LYS A 179 ? 0.7550 0.6611 0.9471 0.0421  0.0006  -0.2701 765 LYS A NZ  
1459 N N   . ASN A 180 ? 0.2663 0.1878 0.4323 0.0432  -0.0030 -0.1294 766 ASN A N   
1460 C CA  . ASN A 180 ? 0.2384 0.1658 0.3898 0.0357  -0.0040 -0.1106 766 ASN A CA  
1461 C C   . ASN A 180 ? 0.2334 0.1574 0.3892 0.0431  -0.0090 -0.0955 766 ASN A C   
1462 O O   . ASN A 180 ? 0.2305 0.1508 0.3757 0.0381  -0.0115 -0.0792 766 ASN A O   
1463 C CB  . ASN A 180 ? 0.2439 0.1568 0.3877 0.0242  -0.0057 -0.1032 766 ASN A CB  
1464 C CG  . ASN A 180 ? 0.2208 0.1465 0.3482 0.0165  -0.0049 -0.0892 766 ASN A CG  
1465 O OD1 . ASN A 180 ? 0.2120 0.1590 0.3296 0.0162  -0.0014 -0.0907 766 ASN A OD1 
1466 N ND2 . ASN A 180 ? 0.2333 0.1456 0.3576 0.0102  -0.0070 -0.0755 766 ASN A ND2 
1467 N N   . THR A 181 ? 0.2413 0.1708 0.4125 0.0556  -0.0106 -0.1021 767 THR A N   
1468 C CA  . THR A 181 ? 0.2377 0.1665 0.4138 0.0646  -0.0178 -0.0898 767 THR A CA  
1469 C C   . THR A 181 ? 0.2082 0.1640 0.3788 0.0617  -0.0160 -0.0852 767 THR A C   
1470 O O   . THR A 181 ? 0.2272 0.1843 0.3993 0.0677  -0.0232 -0.0750 767 THR A O   
1471 C CB  . THR A 181 ? 0.2606 0.1857 0.4585 0.0809  -0.0221 -0.0996 767 THR A CB  
1472 O OG1 . THR A 181 ? 0.2674 0.2191 0.4761 0.0828  -0.0145 -0.1180 767 THR A OG1 
1473 C CG2 . THR A 181 ? 0.2933 0.1862 0.4982 0.0846  -0.0243 -0.1039 767 THR A CG2 
1474 N N   . ALA A 182 ? 0.1844 0.1605 0.3490 0.0536  -0.0070 -0.0927 768 ALA A N   
1475 C CA  . ALA A 182 ? 0.1751 0.1733 0.3370 0.0500  -0.0043 -0.0885 768 ALA A CA  
1476 C C   . ALA A 182 ? 0.1688 0.1592 0.3152 0.0444  -0.0097 -0.0712 768 ALA A C   
1477 O O   . ALA A 182 ? 0.1699 0.1432 0.3033 0.0387  -0.0110 -0.0635 768 ALA A O   
1478 C CB  . ALA A 182 ? 0.1707 0.1859 0.3250 0.0420  0.0076  -0.0970 768 ALA A CB  
1479 N N   . PRO A 183 ? 0.1575 0.1623 0.3059 0.0450  -0.0122 -0.0666 769 PRO A N   
1480 C CA  . PRO A 183 ? 0.1560 0.1562 0.2888 0.0402  -0.0165 -0.0526 769 PRO A CA  
1481 C C   . PRO A 183 ? 0.1528 0.1579 0.2700 0.0281  -0.0087 -0.0503 769 PRO A C   
1482 O O   . PRO A 183 ? 0.1492 0.1638 0.2661 0.0237  0.0000  -0.0583 769 PRO A O   
1483 C CB  . PRO A 183 ? 0.1533 0.1716 0.2970 0.0451  -0.0216 -0.0537 769 PRO A CB  
1484 C CG  . PRO A 183 ? 0.1500 0.1882 0.3127 0.0454  -0.0135 -0.0689 769 PRO A CG  
1485 C CD  . PRO A 183 ? 0.1528 0.1809 0.3206 0.0500  -0.0107 -0.0765 769 PRO A CD  
1486 N N   . LEU A 184 ? 0.1441 0.1424 0.2464 0.0237  -0.0117 -0.0387 770 LEU A N   
1487 C CA  . LEU A 184 ? 0.1416 0.1478 0.2320 0.0155  -0.0071 -0.0356 770 LEU A CA  
1488 C C   . LEU A 184 ? 0.1346 0.1545 0.2321 0.0170  -0.0094 -0.0365 770 LEU A C   
1489 O O   . LEU A 184 ? 0.1562 0.1762 0.2588 0.0240  -0.0181 -0.0338 770 LEU A O   
1490 C CB  . LEU A 184 ? 0.1484 0.1439 0.2233 0.0113  -0.0095 -0.0248 770 LEU A CB  
1491 C CG  . LEU A 184 ? 0.1595 0.1431 0.2305 0.0077  -0.0076 -0.0248 770 LEU A CG  
1492 C CD1 . LEU A 184 ? 0.1715 0.1473 0.2317 0.0035  -0.0091 -0.0141 770 LEU A CD1 
1493 C CD2 . LEU A 184 ? 0.1682 0.1584 0.2352 0.0032  -0.0014 -0.0327 770 LEU A CD2 
1494 N N   . THR A 185 ? 0.1221 0.1523 0.2195 0.0109  -0.0022 -0.0400 771 THR A N   
1495 C CA  . THR A 185 ? 0.1160 0.1596 0.2237 0.0101  -0.0033 -0.0433 771 THR A CA  
1496 C C   . THR A 185 ? 0.1173 0.1591 0.2123 0.0021  0.0011  -0.0389 771 THR A C   
1497 O O   . THR A 185 ? 0.1278 0.1674 0.2156 -0.0034 0.0105  -0.0389 771 THR A O   
1498 C CB  . THR A 185 ? 0.1178 0.1766 0.2463 0.0101  0.0032  -0.0548 771 THR A CB  
1499 O OG1 . THR A 185 ? 0.1344 0.1953 0.2770 0.0200  -0.0026 -0.0600 771 THR A OG1 
1500 C CG2 . THR A 185 ? 0.1217 0.1962 0.2655 0.0070  0.0029  -0.0603 771 THR A CG2 
1501 N N   . ILE A 186 ? 0.1173 0.1597 0.2082 0.0028  -0.0058 -0.0354 772 ILE A N   
1502 C CA  . ILE A 186 ? 0.1192 0.1601 0.2016 -0.0034 -0.0022 -0.0335 772 ILE A CA  
1503 C C   . ILE A 186 ? 0.1265 0.1774 0.2253 -0.0091 0.0048  -0.0419 772 ILE A C   
1504 O O   . ILE A 186 ? 0.1312 0.1958 0.2496 -0.0073 0.0010  -0.0501 772 ILE A O   
1505 C CB  . ILE A 186 ? 0.1271 0.1684 0.2026 -0.0001 -0.0118 -0.0306 772 ILE A CB  
1506 C CG1 . ILE A 186 ? 0.1316 0.1629 0.1917 0.0034  -0.0156 -0.0214 772 ILE A CG1 
1507 C CG2 . ILE A 186 ? 0.1363 0.1770 0.2077 -0.0059 -0.0085 -0.0321 772 ILE A CG2 
1508 C CD1 . ILE A 186 ? 0.1363 0.1693 0.1898 0.0096  -0.0255 -0.0180 772 ILE A CD1 
1509 N N   . CYS A 187 ? 0.1464 0.1905 0.2377 -0.0161 0.0152  -0.0397 773 CYS A N   
1510 C CA  A CYS A 187 ? 0.1829 0.2332 0.2889 -0.0234 0.0256  -0.0458 773 CYS A CA  
1511 C CA  B CYS A 187 ? 0.1773 0.2278 0.2837 -0.0234 0.0255  -0.0459 773 CYS A CA  
1512 C C   . CYS A 187 ? 0.2025 0.2434 0.3030 -0.0299 0.0298  -0.0434 773 CYS A C   
1513 O O   . CYS A 187 ? 0.2320 0.2590 0.3120 -0.0287 0.0297  -0.0353 773 CYS A O   
1514 C CB  A CYS A 187 ? 0.2253 0.2746 0.3283 -0.0254 0.0377  -0.0453 773 CYS A CB  
1515 C CB  B CYS A 187 ? 0.1991 0.2487 0.3028 -0.0257 0.0380  -0.0455 773 CYS A CB  
1516 S SG  A CYS A 187 ? 0.2528 0.2844 0.3238 -0.0240 0.0413  -0.0341 773 CYS A SG  
1517 S SG  B CYS A 187 ? 0.2022 0.2640 0.3191 -0.0184 0.0355  -0.0528 773 CYS A SG  
1518 N N   . PRO A 188 ? 0.2203 0.2679 0.3405 -0.0375 0.0355  -0.0512 774 PRO A N   
1519 C CA  . PRO A 188 ? 0.2510 0.2853 0.3676 -0.0447 0.0414  -0.0494 774 PRO A CA  
1520 C C   . PRO A 188 ? 0.2913 0.3075 0.3885 -0.0478 0.0549  -0.0385 774 PRO A C   
1521 O O   . PRO A 188 ? 0.3120 0.3315 0.4074 -0.0484 0.0634  -0.0368 774 PRO A O   
1522 C CB  . PRO A 188 ? 0.2881 0.3367 0.4360 -0.0532 0.0450  -0.0624 774 PRO A CB  
1523 C CG  . PRO A 188 ? 0.2792 0.3472 0.4447 -0.0516 0.0472  -0.0685 774 PRO A CG  
1524 C CD  . PRO A 188 ? 0.2455 0.3128 0.3937 -0.0398 0.0378  -0.0623 774 PRO A CD  
1525 N N   . VAL A 189 ? 0.3324 0.3293 0.4134 -0.0483 0.0566  -0.0313 775 VAL A N   
1526 C CA  . VAL A 189 ? 0.4075 0.3857 0.4697 -0.0503 0.0693  -0.0204 775 VAL A CA  
1527 C C   . VAL A 189 ? 0.4911 0.4691 0.5694 -0.0619 0.0855  -0.0230 775 VAL A C   
1528 O O   . VAL A 189 ? 0.4894 0.4692 0.5897 -0.0699 0.0870  -0.0311 775 VAL A O   
1529 C CB  . VAL A 189 ? 0.4453 0.4012 0.4914 -0.0482 0.0687  -0.0130 775 VAL A CB  
1530 C CG1 . VAL A 189 ? 0.4834 0.4178 0.5113 -0.0505 0.0831  -0.0009 775 VAL A CG1 
1531 C CG2 . VAL A 189 ? 0.3803 0.3372 0.4105 -0.0374 0.0555  -0.0100 775 VAL A CG2 
1532 N N   . GLY A 190 ? 0.5653 0.5410 0.6320 -0.0631 0.0980  -0.0166 776 GLY A N   
1533 C CA  . GLY A 190 ? 0.6616 0.6345 0.7400 -0.0752 0.1172  -0.0164 776 GLY A CA  
1534 C C   . GLY A 190 ? 0.7798 0.7223 0.8328 -0.0775 0.1296  -0.0011 776 GLY A C   
1535 O O   . GLY A 190 ? 0.8920 0.8295 0.9322 -0.0811 0.1460  0.0065  776 GLY A O   
# 
