data_7HVB
# 
_entry.id   7HVB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HVB         pdb_00007hvb 10.2210/pdb7hvb/pdb 
WWPDB D_1001407976 ?            ?                   
# 
_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       2025-02-26 
_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.entry_id                        7HVB 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                     15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-N~1~-[2-(methoxymethyl)phenyl]piperidine-1,3-dicarboxamide' 291.346   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                        65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                              78.133    1   ?         ? ? ? 
5 water       nat water                                                             18.015    117 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_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       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_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 '(3S)-N~1~-[2-(methoxymethyl)phenyl]piperidine-1,3-dicarboxamide' A1BPV 
3 'ZINC ION'                                                        ZN    
4 'DIMETHYL SULFOXIDE'                                              DMS   
5 water                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_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 
A1BPV non-polymer         . '(3S)-N~1~-[2-(methoxymethyl)phenyl]piperidine-1,3-dicarboxamide' ? 'C15 H21 N3 O3'  291.346 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                              ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                         ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                   ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                           ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                         ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                             ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                            ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                        ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                     ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                           ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                            ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                         ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                        ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                          ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                            ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                        ? 'Zn 2'           65.409  
# 
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   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BPV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPV 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BPV 1   201 201 A1BPV LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 9   HOH   HOH A . 
E 5 HOH   2   302 116 HOH   HOH A . 
E 5 HOH   3   303 10  HOH   HOH A . 
E 5 HOH   4   304 24  HOH   HOH A . 
E 5 HOH   5   305 15  HOH   HOH A . 
E 5 HOH   6   306 66  HOH   HOH A . 
E 5 HOH   7   307 43  HOH   HOH A . 
E 5 HOH   8   308 38  HOH   HOH A . 
E 5 HOH   9   309 67  HOH   HOH A . 
E 5 HOH   10  310 86  HOH   HOH A . 
E 5 HOH   11  311 108 HOH   HOH A . 
E 5 HOH   12  312 115 HOH   HOH A . 
E 5 HOH   13  313 11  HOH   HOH A . 
E 5 HOH   14  314 120 HOH   HOH A . 
E 5 HOH   15  315 76  HOH   HOH A . 
E 5 HOH   16  316 37  HOH   HOH A . 
E 5 HOH   17  317 97  HOH   HOH A . 
E 5 HOH   18  318 29  HOH   HOH A . 
E 5 HOH   19  319 117 HOH   HOH A . 
E 5 HOH   20  320 64  HOH   HOH A . 
E 5 HOH   21  321 1   HOH   HOH A . 
E 5 HOH   22  322 4   HOH   HOH A . 
E 5 HOH   23  323 59  HOH   HOH A . 
E 5 HOH   24  324 89  HOH   HOH A . 
E 5 HOH   25  325 110 HOH   HOH A . 
E 5 HOH   26  326 61  HOH   HOH A . 
E 5 HOH   27  327 3   HOH   HOH A . 
E 5 HOH   28  328 16  HOH   HOH A . 
E 5 HOH   29  329 12  HOH   HOH A . 
E 5 HOH   30  330 65  HOH   HOH A . 
E 5 HOH   31  331 70  HOH   HOH A . 
E 5 HOH   32  332 75  HOH   HOH A . 
E 5 HOH   33  333 28  HOH   HOH A . 
E 5 HOH   34  334 87  HOH   HOH A . 
E 5 HOH   35  335 93  HOH   HOH A . 
E 5 HOH   36  336 118 HOH   HOH A . 
E 5 HOH   37  337 95  HOH   HOH A . 
E 5 HOH   38  338 27  HOH   HOH A . 
E 5 HOH   39  339 44  HOH   HOH A . 
E 5 HOH   40  340 26  HOH   HOH A . 
E 5 HOH   41  341 63  HOH   HOH A . 
E 5 HOH   42  342 18  HOH   HOH A . 
E 5 HOH   43  343 14  HOH   HOH A . 
E 5 HOH   44  344 71  HOH   HOH A . 
E 5 HOH   45  345 5   HOH   HOH A . 
E 5 HOH   46  346 60  HOH   HOH A . 
E 5 HOH   47  347 13  HOH   HOH A . 
E 5 HOH   48  348 90  HOH   HOH A . 
E 5 HOH   49  349 74  HOH   HOH A . 
E 5 HOH   50  350 42  HOH   HOH A . 
E 5 HOH   51  351 91  HOH   HOH A . 
E 5 HOH   52  352 31  HOH   HOH A . 
E 5 HOH   53  353 25  HOH   HOH A . 
E 5 HOH   54  354 58  HOH   HOH A . 
E 5 HOH   55  355 56  HOH   HOH A . 
E 5 HOH   56  356 17  HOH   HOH A . 
E 5 HOH   57  357 101 HOH   HOH A . 
E 5 HOH   58  358 72  HOH   HOH A . 
E 5 HOH   59  359 22  HOH   HOH A . 
E 5 HOH   60  360 57  HOH   HOH A . 
E 5 HOH   61  361 84  HOH   HOH A . 
E 5 HOH   62  362 52  HOH   HOH A . 
E 5 HOH   63  363 69  HOH   HOH A . 
E 5 HOH   64  364 41  HOH   HOH A . 
E 5 HOH   65  365 6   HOH   HOH A . 
E 5 HOH   66  366 34  HOH   HOH A . 
E 5 HOH   67  367 54  HOH   HOH A . 
E 5 HOH   68  368 8   HOH   HOH A . 
E 5 HOH   69  369 50  HOH   HOH A . 
E 5 HOH   70  370 78  HOH   HOH A . 
E 5 HOH   71  371 80  HOH   HOH A . 
E 5 HOH   72  372 30  HOH   HOH A . 
E 5 HOH   73  373 19  HOH   HOH A . 
E 5 HOH   74  374 55  HOH   HOH A . 
E 5 HOH   75  375 53  HOH   HOH A . 
E 5 HOH   76  376 83  HOH   HOH A . 
E 5 HOH   77  377 40  HOH   HOH A . 
E 5 HOH   78  378 45  HOH   HOH A . 
E 5 HOH   79  379 92  HOH   HOH A . 
E 5 HOH   80  380 39  HOH   HOH A . 
E 5 HOH   81  381 79  HOH   HOH A . 
E 5 HOH   82  382 77  HOH   HOH A . 
E 5 HOH   83  383 85  HOH   HOH A . 
E 5 HOH   84  384 82  HOH   HOH A . 
E 5 HOH   85  385 107 HOH   HOH A . 
E 5 HOH   86  386 33  HOH   HOH A . 
E 5 HOH   87  387 32  HOH   HOH A . 
E 5 HOH   88  388 113 HOH   HOH A . 
E 5 HOH   89  389 94  HOH   HOH A . 
E 5 HOH   90  390 48  HOH   HOH A . 
E 5 HOH   91  391 104 HOH   HOH A . 
E 5 HOH   92  392 119 HOH   HOH A . 
E 5 HOH   93  393 51  HOH   HOH A . 
E 5 HOH   94  394 105 HOH   HOH A . 
E 5 HOH   95  395 68  HOH   HOH A . 
E 5 HOH   96  396 103 HOH   HOH A . 
E 5 HOH   97  397 111 HOH   HOH A . 
E 5 HOH   98  398 106 HOH   HOH A . 
E 5 HOH   99  399 7   HOH   HOH A . 
E 5 HOH   100 400 62  HOH   HOH A . 
E 5 HOH   101 401 88  HOH   HOH A . 
E 5 HOH   102 402 35  HOH   HOH A . 
E 5 HOH   103 403 109 HOH   HOH A . 
E 5 HOH   104 404 81  HOH   HOH A . 
E 5 HOH   105 405 100 HOH   HOH A . 
E 5 HOH   106 406 20  HOH   HOH A . 
E 5 HOH   107 407 73  HOH   HOH A . 
E 5 HOH   108 408 23  HOH   HOH A . 
E 5 HOH   109 409 114 HOH   HOH A . 
E 5 HOH   110 410 96  HOH   HOH A . 
E 5 HOH   111 411 112 HOH   HOH A . 
E 5 HOH   112 412 21  HOH   HOH A . 
E 5 HOH   113 413 98  HOH   HOH A . 
E 5 HOH   114 414 99  HOH   HOH A . 
E 5 HOH   115 415 2   HOH   HOH A . 
E 5 HOH   116 416 47  HOH   HOH A . 
E 5 HOH   117 417 102 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HVB 
_cell.length_a           72.720 
_cell.length_b           61.664 
_cell.length_c           32.794 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.97 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVB 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7HVB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.76 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92202 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.31 
_reflns.d_resolution_high            1.46 
_reflns.number_obs                   25105 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.136 
_reflns.pdbx_netI_over_sigmaI        5.2 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.147 
_reflns.pdbx_Rpim_I_all              0.057 
_reflns.pdbx_CC_half                 0.991 
_reflns.pdbx_number_measured_all     162300 
_reflns.pdbx_chi_squared             0.83 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.46 
_reflns_shell.d_res_low                   1.54 
_reflns_shell.number_measured_all         18353 
_reflns_shell.number_unique_obs           3665 
_reflns_shell.Rmerge_I_obs                1.465 
_reflns_shell.pdbx_chi_squared            0.82 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.640 
_reflns_shell.pdbx_Rpim_I_all             0.723 
_reflns_shell.pdbx_CC_half                0.402 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HVB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25076 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.31 
_refine.ls_d_res_high                            1.461 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.2249 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2234 
_refine.ls_R_factor_R_free                       0.2584 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.570 
_refine.ls_number_reflns_R_free                  1147 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_refine.B_iso_mean                               29.75 
_refine.aniso_B[1][1]                            -1.19310 
_refine.aniso_B[2][2]                            -2.21980 
_refine.aniso_B[3][3]                            3.41290 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.19360 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.080 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.083 
_refine.pdbx_overall_SU_R_Blow_DPI               0.082 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.085 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVB 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               1217 
_refine_hist.d_res_high                       1.461 
_refine_hist.d_res_low                        36.31 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  1129 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  1535 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1129 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.25  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.70 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  936  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.46 
_refine_ls_shell.d_res_low                        1.47 
_refine_ls_shell.number_reflns_R_work             487 
_refine_ls_shell.R_factor_R_work                  0.3575 
_refine_ls_shell.percent_reflns_obs               93.85 
_refine_ls_shell.R_factor_R_free                  0.4003 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            2.99 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.number_reflns_all                502 
_refine_ls_shell.R_factor_all                     0.3589 
# 
_struct.entry_id                  7HVB 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0032369-001 (A71EV2A-x3483)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVB 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HVB 
_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                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_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 
# 
_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_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 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 112.7 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.5 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.7 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.3 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.4 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
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 
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 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7HVB 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    312 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    315 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -134.96 
_pdbx_validate_torsion.psi             -30.46 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.0701 
_pdbx_refine_tls.origin_y         7.1385 
_pdbx_refine_tls.origin_z         14.2990 
_pdbx_refine_tls.T[1][1]          0.0003 
_pdbx_refine_tls.T[2][2]          -0.0560 
_pdbx_refine_tls.T[3][3]          -0.0069 
_pdbx_refine_tls.T[1][2]          0.0136 
_pdbx_refine_tls.T[1][3]          -0.0160 
_pdbx_refine_tls.T[2][3]          -0.0156 
_pdbx_refine_tls.L[1][1]          0.8517 
_pdbx_refine_tls.L[2][2]          8.4799 
_pdbx_refine_tls.L[3][3]          0.4488 
_pdbx_refine_tls.L[1][2]          2.1446 
_pdbx_refine_tls.L[1][3]          -0.7476 
_pdbx_refine_tls.L[2][3]          -2.3441 
_pdbx_refine_tls.S[1][1]          -0.0725 
_pdbx_refine_tls.S[1][2]          0.1271 
_pdbx_refine_tls.S[1][3]          -0.0312 
_pdbx_refine_tls.S[2][1]          0.5287 
_pdbx_refine_tls.S[2][2]          0.1484 
_pdbx_refine_tls.S[2][3]          -0.3448 
_pdbx_refine_tls.S[3][1]          -0.0970 
_pdbx_refine_tls.S[3][2]          -0.1580 
_pdbx_refine_tls.S[3][3]          -0.0759 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1BPV N1   N  N N 1   
A1BPV C4   C  Y N 2   
A1BPV C5   C  Y N 3   
A1BPV C6   C  Y N 4   
A1BPV C7   C  Y N 5   
A1BPV C8   C  N N 6   
A1BPV C10  C  N N 7   
A1BPV C13  C  N N 8   
A1BPV O2   O  N N 9   
A1BPV N2   N  N N 10  
A1BPV C12  C  N S 11  
A1BPV C11  C  N N 12  
A1BPV C9   C  N N 13  
A1BPV C14  C  N N 14  
A1BPV O1   O  N N 15  
A1BPV N    N  N N 16  
A1BPV C3   C  Y N 17  
A1BPV C2   C  Y N 18  
A1BPV C1   C  N N 19  
A1BPV O    O  N N 20  
A1BPV C    C  N N 21  
A1BPV H7   H  N N 22  
A1BPV H8   H  N N 23  
A1BPV H9   H  N N 24  
A1BPV H14  H  N N 25  
A1BPV H13  H  N N 26  
A1BPV H18  H  N N 27  
A1BPV H17  H  N N 28  
A1BPV H    H  N N 29  
A1BPV H15  H  N N 30  
A1BPV H16  H  N N 31  
A1BPV H11  H  N N 32  
A1BPV H12  H  N N 33  
A1BPV H19  H  N N 34  
A1BPV H20  H  N N 35  
A1BPV H10  H  N N 36  
A1BPV H6   H  N N 37  
A1BPV H4   H  N N 38  
A1BPV H5   H  N N 39  
A1BPV H2   H  N N 40  
A1BPV H3   H  N N 41  
A1BPV H1   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
DMS   S    S  N N 130 
DMS   O    O  N N 131 
DMS   C1   C  N N 132 
DMS   C2   C  N N 133 
DMS   H11  H  N N 134 
DMS   H12  H  N N 135 
DMS   H13  H  N N 136 
DMS   H21  H  N N 137 
DMS   H22  H  N N 138 
DMS   H23  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
ZN    ZN   ZN N N 443 
# 
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 
A1BPV C   O    sing N N 1   
A1BPV O   C1   sing N N 2   
A1BPV C1  C2   sing N N 3   
A1BPV C2  C3   doub Y N 4   
A1BPV C3  C4   sing Y N 5   
A1BPV C4  C5   doub Y N 6   
A1BPV C5  C6   sing Y N 7   
A1BPV C6  C7   doub Y N 8   
A1BPV C2  C7   sing Y N 9   
A1BPV C7  N    sing N N 10  
A1BPV N   C8   sing N N 11  
A1BPV O1  C8   doub N N 12  
A1BPV C8  N1   sing N N 13  
A1BPV N1  C9   sing N N 14  
A1BPV C9  C10  sing N N 15  
A1BPV C10 C11  sing N N 16  
A1BPV C11 C12  sing N N 17  
A1BPV C12 C13  sing N N 18  
A1BPV N2  C13  sing N N 19  
A1BPV C13 O2   doub N N 20  
A1BPV C14 C12  sing N N 21  
A1BPV N1  C14  sing N N 22  
A1BPV C4  H7   sing N N 23  
A1BPV C5  H8   sing N N 24  
A1BPV C6  H9   sing N N 25  
A1BPV C10 H14  sing N N 26  
A1BPV C10 H13  sing N N 27  
A1BPV N2  H18  sing N N 28  
A1BPV N2  H17  sing N N 29  
A1BPV C12 H    sing N N 30  
A1BPV C11 H15  sing N N 31  
A1BPV C11 H16  sing N N 32  
A1BPV C9  H11  sing N N 33  
A1BPV C9  H12  sing N N 34  
A1BPV C14 H19  sing N N 35  
A1BPV C14 H20  sing N N 36  
A1BPV N   H10  sing N N 37  
A1BPV C3  H6   sing N N 38  
A1BPV C1  H4   sing N N 39  
A1BPV C1  H5   sing N N 40  
A1BPV C   H2   sing N N 41  
A1BPV C   H3   sing N N 42  
A1BPV C   H1   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
DMS   S   O    doub N N 126 
DMS   S   C1   sing N N 127 
DMS   S   C2   sing N N 128 
DMS   C1  H11  sing N N 129 
DMS   C1  H12  sing N N 130 
DMS   C1  H13  sing N N 131 
DMS   C2  H21  sing N N 132 
DMS   C2  H22  sing N N 133 
DMS   C2  H23  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_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   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HVB 
_atom_sites.fract_transf_matrix[1][1]   0.013751 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000713 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016217 
_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]   0.030534 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.832 6.857   24.254 1.00 36.88  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.063 6.831   23.457 1.00 37.04  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.103 5.632   22.508 1.00 34.01  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.423 4.614   22.762 1.00 33.25  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.280 6.791   24.379 1.00 39.89  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.162 5.628   25.179 1.00 43.57  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.900 5.765   21.440 1.00 31.52  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.129 4.742   20.421 1.00 30.36  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.437 5.296   19.031 1.00 28.28  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.069 6.421   18.698 1.00 26.77  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.089 4.490   18.192 1.00 27.22  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.464 4.911   16.844 1.00 26.07  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.515 3.731   15.850 1.00 25.07  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.564 2.570   16.255 1.00 25.63  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.842 5.584   16.908 1.00 26.63  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.503 4.047   14.547 1.00 24.44  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.664 3.100   13.454 1.00 24.05  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.043 3.328   12.829 1.00 26.50  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.382 4.441   12.409 1.00 26.29  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.575 3.297   12.380 1.00 23.60  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.191 3.274   13.002 1.00 23.19  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.699 2.197   11.314 1.00 24.78  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.149 3.834   12.010 1.00 22.46  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.833 2.264   12.776 1.00 29.27  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.180 2.260   12.213 1.00 31.58  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.171 1.482   10.893 1.00 32.28  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.026 0.265   10.902 1.00 32.69  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.141 1.610   13.221 1.00 32.66  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.273 2.435   14.480 1.00 34.04  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.078 3.565   14.512 1.00 35.62  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.524 2.140   15.610 1.00 35.50  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.135 4.380   15.636 1.00 37.01  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.571 2.950   16.738 1.00 36.51  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.418 4.042   16.764 1.00 37.42  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.519 4.819   17.886 1.00 38.77  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.277 2.180   9.766  1.00 33.47  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.235 1.579   8.429  1.00 34.74  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.343 2.195   7.564  1.00 36.08  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.387 3.419   7.406  1.00 36.83  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.836 1.784   7.782  1.00 36.08  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.422 3.259   7.808  1.00 35.55  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.815 1.244   6.359  1.00 37.49  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.262 1.377   7.049  1.00 36.77  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.383 1.897   6.268  1.00 38.78  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.228 2.870   7.073  1.00 41.79  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.478 2.619   8.251  1.00 42.94  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.536 4.042   6.516  1.00 42.21  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.292 5.064   7.251  1.00 43.03  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.362 6.138   7.875  1.00 39.46  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.774 7.284   8.093  1.00 39.63  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.334 5.701   6.350  1.00 48.19  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.546 4.832   6.097  1.00 55.41  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.952 4.011   6.927  1.00 58.15  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.171 4.996   4.941  1.00 58.07  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.112 5.738   8.213  1.00 35.88  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.092 6.654   8.760  1.00 33.31  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.537 6.207   10.111 1.00 31.31  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.346 5.018   10.357 1.00 31.11  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.889 6.731   7.795  1.00 31.65  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.226 7.317   6.449  1.00 32.57  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.810 8.571   6.345  1.00 33.86  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.969 6.618   5.278  1.00 33.69  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.169 9.101   5.115  1.00 35.82  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.311 7.142   4.036  1.00 35.75  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.911 8.390   3.959  1.00 37.67  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.242 8.976   2.754  1.00 39.80  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.187 7.195   10.938 1.00 30.11  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.500 7.029   12.214 1.00 27.68  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.203 7.856   12.140 1.00 24.80  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.205 9.074   11.914 1.00 23.34  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.388 7.452   13.394 1.00 27.13  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.686 7.682   14.729 1.00 28.87  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.688 8.101   15.794 1.00 33.20  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.166 9.123   16.705 1.00 35.00  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.674 8.869   17.914 1.00 37.01  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.556 7.613   18.342 1.00 36.43  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.260 9.865   18.690 1.00 36.24  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.058 7.173   12.296 1.00 22.70  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.748 7.828   12.260 1.00 21.34  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.236 7.967   13.670 1.00 20.39  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.051 6.951   14.333 1.00 20.69  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.718 7.019   11.460 1.00 20.84  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.440 7.881   11.265 1.00 19.95  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.282 6.523   10.121 1.00 21.31  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.934 9.189   14.123 1.00 20.38  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.438 9.385   15.500 1.00 21.49  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.213 10.352  15.470 1.00 19.65  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.007 11.067  14.478 1.00 19.89  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.544 10.041  16.371 1.00 24.46  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.690 9.098   16.598 1.00 27.03  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.025 11.340  15.729 1.00 23.75  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.458 10.453  16.599 1.00 17.94  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.410 11.485  16.719 1.00 17.40  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.142 12.830  16.720 1.00 18.50  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.152 12.991  17.476 1.00 20.14  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.683 11.379  18.081 1.00 18.20  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.828 10.153  18.173 1.00 19.77  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.302 9.093   18.618 1.00 20.02  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.603 10.233  17.687 1.00 17.48  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.688 13.776  15.893 1.00 17.51  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.366 15.072  15.825 1.00 16.82  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.396 15.780  17.178 1.00 19.34  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.403 16.439  17.501 1.00 21.14  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.715 15.989  14.758 1.00 17.12  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.501 17.298  14.434 1.00 16.39  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.562 18.167  13.622 1.00 16.85  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.142 19.421  13.087 1.00 16.75  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.183 20.560  13.767 1.00 21.93  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.814 20.595  15.048 1.00 20.44  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.623 21.676  13.182 1.00 21.69  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.332 15.611  18.006 1.00 20.02  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.309 16.310  19.308 1.00 22.64  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.288 15.716  20.355 1.00 25.80  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.616 16.373  21.361 1.00 28.48  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.884 16.435  19.853 1.00 23.34  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.302 15.161  20.383 1.00 23.62  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.641 14.256  19.559 1.00 24.00  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.257 14.701  21.657 1.00 23.86  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.252 13.260  20.356 1.00 24.98  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.571 13.497  21.629 1.00 25.26  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.852 14.538  20.059 1.00 25.71  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.815 13.888  20.948 1.00 26.73  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.263 13.884  20.361 1.00 28.40  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.153 13.216  20.917 1.00 29.48  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.329 12.442  21.233 1.00 26.70  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.992 12.336  21.997 1.00 28.41  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.614 10.898  22.262 1.00 27.83  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.037 13.062  23.317 1.00 30.48  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.470 14.545  19.174 1.00 27.86  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.762 14.537  18.504 1.00 28.30  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.809 15.197  19.397 1.00 30.83  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.473 16.190  20.038 1.00 32.84  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.676 15.282  17.176 1.00 26.50  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.051 14.707  19.374 1.00 32.61  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.194 15.230  20.180 1.00 35.46  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.048 16.292  19.431 1.00 38.22  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.823 16.525  18.248 1.00 37.88  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.116 14.043  20.527 1.00 37.25  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.771 13.627  19.330 1.00 40.67  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.395 12.899  21.175 1.00 36.19  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.108 16.888  20.098 1.00 40.02  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.997 17.819  19.412 1.00 41.70  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.718 17.107  18.270 1.00 41.02  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.824 17.685  17.199 1.00 41.78  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.050 18.393  20.373 1.00 45.59  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.533 19.423  21.325 1.00 51.91  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.102 20.652  20.891 1.00 56.17  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.514 19.406  22.679 1.00 55.21  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.797 21.334  21.986 1.00 57.12  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.002 20.605  23.086 1.00 57.26  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.184 15.844  18.487 1.00 40.63  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.880 15.059  17.454 1.00 41.34  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.982 14.829  16.250 1.00 38.56  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.447 14.954  15.122 1.00 39.02  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.339 13.717  18.006 1.00 45.80  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.125 12.864  17.036 1.00 55.56  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.284 13.165  16.701 1.00 59.56  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.516 11.770  16.582 1.00 56.71  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.699 14.468  16.475 1.00 35.99  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.719 14.300  15.400 1.00 32.98  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.611 15.596  14.561 1.00 31.02  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.679 15.534  13.345 1.00 30.76  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.350 13.990  16.000 1.00 32.02  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.181 12.568  16.486 1.00 32.94  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.769 11.646  15.864 1.00 32.17  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.499 12.375  17.504 1.00 36.26  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.474 16.775  15.200 1.00 30.88  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.348 18.034  14.477 1.00 30.61  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.697 18.440  13.799 1.00 33.87  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.671 19.085  12.757 1.00 34.39  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.842 19.125  15.454 1.00 28.44  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.344 19.196  15.569 1.00 26.50  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.572 18.743  16.602 1.00 26.83  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.444 19.727  14.596 1.00 23.85  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.246 18.978  16.336 1.00 26.13  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.138 19.599  15.115 1.00 24.73  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.618 20.341  13.355 1.00 24.53  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.003 20.039  14.419 1.00 23.99  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.493 20.792  12.669 1.00 24.00  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.200 20.613  13.192 1.00 23.48  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.858 18.041  14.384 1.00 35.15  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.188 18.319  13.818 1.00 37.66  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.505 17.432  12.603 1.00 39.43  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.395 17.767  11.810 1.00 41.25  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.280 18.135  14.876 1.00 38.49  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.807 16.275  12.492 1.00 37.48  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.912 15.321  11.395 1.00 36.92  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.548 15.217  10.691 1.00 33.36  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.179 14.151  10.274 1.00 32.85  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.360 13.977  11.932 1.00 40.14  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.778 14.059  12.450 1.00 46.71  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.715 14.313  11.687 1.00 48.35  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.950 13.852  13.746 1.00 48.65  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.818 16.312  10.568 1.00 30.51  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.478 16.336  9.972  1.00 28.33  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.490 15.917  8.504  1.00 29.80  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.360 16.355  7.768  1.00 32.39  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.930 17.767  10.083 1.00 26.51  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.513 17.970  9.492  1.00 26.59  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.466 17.123  10.259 1.00 26.54  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.113 19.426  9.507  1.00 25.96  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.543 15.042  8.077  1.00 27.47  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.358 14.637  6.685  1.00 26.60  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.008 15.284  6.209  1.00 25.82  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.943 15.985  5.187  1.00 27.85  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.300 13.093  6.543  1.00 27.27  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.778 12.712  5.170  1.00 27.70  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.662 12.431  6.821  1.00 29.29  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.950 15.105  7.013  1.00 22.87  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.627 15.638  6.703  1.00 21.20  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.759 15.705  7.979  1.00 19.74  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.881 14.870  8.878  1.00 19.58  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.968 14.691  5.653  1.00 20.88  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.494 14.874  5.402  1.00 20.66  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.896 15.767  4.562  1.00 22.84  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.431 14.118  6.007  1.00 19.87  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.525 15.613  4.602  1.00 22.50  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.212 14.612  5.491  1.00 20.69  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.393 13.117  6.976  1.00 20.21  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.969 14.035  5.820  1.00 19.85  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.169 12.534  7.280  1.00 19.73  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.970 13.063  6.787  1.00 18.98  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.893 16.710  8.061  1.00 18.39  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.943 16.790  9.174  1.00 17.53  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.636 17.367  8.667  1.00 16.16  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.615 18.162  7.722  1.00 16.85  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.518 17.556  10.381 1.00 20.05  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.124 18.905  10.031 1.00 20.07  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.152 20.057  9.886  1.00 24.15  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.448 20.998  9.114  1.00 26.33  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.091 20.026  10.544 1.00 22.33  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.552 17.003  9.333  1.00 14.34  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.240 17.509  8.971  1.00 14.19  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.406 17.663  10.255 1.00 14.90  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.970 16.655  10.826 1.00 16.15  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.582 16.607  7.917  1.00 16.42  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.290 17.156  7.378  1.00 21.51  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.615 17.905  8.106  1.00 21.42  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.930 16.805  6.231  1.00 23.73  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.194 18.926  10.719 1.00 13.93  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.424 19.196  11.924 0.50 15.43  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.409 19.174  11.945 0.50 15.51  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.992 18.643  11.788 1.00 16.22  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.413 18.179  12.757 1.00 17.04  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.368 20.707  12.141 0.50 18.03  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.298 20.670  12.261 0.50 18.43  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.961 21.032  13.452 0.50 19.48  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 16.529 21.311  12.541 0.50 21.13  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.415 18.741  10.571 1.00 15.62  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.033 18.280  10.372 1.00 16.20  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.873 16.777  10.513 1.00 16.63  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.751 16.324  10.695 1.00 18.77  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.493 18.718  9.018  1.00 19.94  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.011 17.932  7.954  1.00 23.96  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.961 16.028  10.443 1.00 13.91  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.939 14.547  10.605 1.00 13.80  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.530 14.114  11.949 1.00 14.38  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.475 12.931  12.263 1.00 14.40  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.731 13.857  9.444  1.00 14.09  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.108 14.130  8.076  1.00 14.35  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.865 13.447  6.946  1.00 12.84  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.845 11.985  7.082  1.00 13.85  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.040 11.143  6.062  1.00 14.04  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.186 11.607  4.820  1.00 16.12  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.997 9.825   6.263  1.00 17.13  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.163 15.021  12.709 1.00 15.31  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.902 14.704  13.958 1.00 14.46  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.079 13.733  13.644 1.00 14.66  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.362 12.859  14.447 1.00 15.59  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.999 14.138  15.068 1.00 15.09  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.713 13.889  16.376 1.00 17.12  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.501 14.742  16.780 1.00 18.19  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.497 12.796  16.990 1.00 18.35  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.701 13.845  12.446 1.00 13.99  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.852 12.993  12.103 1.00 13.18  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.125 13.783  11.832 1.00 14.12  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.110 14.900  11.326 1.00 15.60  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.574 12.216  10.813 1.00 14.29  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.518 11.068  10.881 1.00 15.13  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.459 10.382  9.502  1.00 15.22  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.852 10.009  11.936 1.00 14.48  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.251 13.170  12.155 1.00 14.85  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.570 13.729  11.882 1.00 17.13  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.456 12.541  11.567 1.00 18.29  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.307 11.505  12.211 1.00 19.78  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.111 14.559  13.092 1.00 18.41  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.540 15.113  12.908 1.00 19.31  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.715 16.474  13.551 1.00 20.47  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.627 14.168  13.518 1.00 21.37  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.282 12.633  10.496 1.00 18.96  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.217 11.574  10.120 1.00 20.87  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.625 12.200  10.195 1.00 22.79  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.866 13.313  9.675  1.00 21.93  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.955 11.029  8.705  1.00 21.77  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.020 9.972   8.303  1.00 22.70  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.541 10.442  8.617  1.00 21.17  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.511 11.514  10.901 1.00 24.65  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.905 11.940  11.035 1.00 27.82  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.807 10.849  10.466 1.00 30.50  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.410 9.694   10.342 1.00 28.85  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.231 12.250  12.490 1.00 28.72  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.149 11.106  13.321 1.00 29.58  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.046 11.212  10.126 1.00 34.01  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.011 10.256  9.581  1.00 37.80  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.854 9.578   10.673 1.00 42.40  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.133 10.188  11.694 1.00 43.48  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.907 10.947  8.563  1.00 38.65  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.575 12.037  9.178  1.00 42.28  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.223 8.314   10.479 1.00 45.58  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.005 7.562   11.467 1.00 50.03  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.294 7.041   10.852 1.00 55.94  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.316 6.753   9.658  1.00 57.25  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.217 6.344   11.961 1.00 50.83  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.085 5.402   10.896 1.00 51.59  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.853 6.704   12.509 1.00 50.01  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.320 6.796   11.684 1.00 59.05  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.591 6.210   11.235 1.00 62.21  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.503 4.673   11.131 1.00 63.72  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.347 4.048   10.476 1.00 66.53  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.709 6.584   12.212 1.00 64.43  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.355 6.083   13.506 1.00 67.43  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.989 8.067   12.264 1.00 64.12  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.552 4.039   11.840 1.00 61.97  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.409 2.589   11.798 1.00 60.79  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.224 2.198   10.915 1.00 58.68  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.286 2.972   10.754 1.00 57.93  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.239 2.037   13.202 1.00 61.61  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.290 1.025   10.305 1.00 58.08  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.275 0.514   9.380  1.00 57.99  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.047 -0.118  10.083 1.00 56.03  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.192 -1.070  10.851 1.00 56.35  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.960 -0.504  8.431  1.00 61.08  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.019 -1.365  7.577  1.00 65.69  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.614 -0.704  6.279  1.00 72.57  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.123 0.363   5.895  1.00 75.16  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.691 -1.337  5.567  1.00 73.40  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.855 0.379   9.752  1.00 53.24  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.570 -0.070  10.282 1.00 51.55  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.962 -1.247  9.538  1.00 48.83  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.009 -1.307  8.303  1.00 48.70  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.324 -2.158  10.277 1.00 45.90  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.786 -3.360  9.677  1.00 44.24  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.274 -3.551  9.769  1.00 40.93  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.829 -4.701  9.663  1.00 41.75  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.509 -4.571  10.239 1.00 46.70  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.060 -4.915  9.410  1.00 55.56  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.483 -2.472  9.913  1.00 37.37  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.029 -2.637  9.945  1.00 36.12  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.508 -2.641  8.531  1.00 35.43  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.032 -1.946  7.647  1.00 37.53  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.329 -1.500  10.713 1.00 37.00  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.565 -1.538  12.191 1.00 40.53  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.549 -2.639  12.765 1.00 42.58  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.748 -0.462  12.783 1.00 40.68  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.482 -3.403  8.321  1.00 33.18  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.833 -3.495  7.032  1.00 32.26  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.622 -2.610  7.141  1.00 29.70  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.916 -2.703  8.140  1.00 30.06  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.413 -4.953  6.786  1.00 34.82  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.596 -5.655  6.409  1.00 37.29  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.393 -5.083  5.682  1.00 34.26  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.420 -1.712  6.175  1.00 27.09  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.237 -0.871  6.188  1.00 25.08  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.185 -1.566  5.321  1.00 23.98  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.517 -2.055  4.207  1.00 25.48  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.523 0.546   5.653  1.00 25.23  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.697 1.225   6.397  1.00 27.17  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.232 1.410   5.708  1.00 25.47  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.429 1.563   7.901  1.00 27.59  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.949 -1.667  5.827  1.00 21.60  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.839 -2.217  5.080  1.00 21.19  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.440 -1.311  3.915  1.00 22.15  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.456 -0.095  4.058  1.00 21.03  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.629 -2.422  5.998  1.00 19.85  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.048 -1.910  2.750  1.00 24.55  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.595 -1.155  1.560  1.00 26.90  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.237 -1.783  1.209  1.00 28.51  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.188 -2.744  0.434  1.00 31.44  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.629 -1.278  0.402  1.00 28.31  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.034 -0.787  0.777  1.00 27.51  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.088 0.686   1.236  1.00 29.10  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.458 1.108   1.551  1.00 27.65  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.761 2.257   2.154  1.00 28.88  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.806 3.106   2.496  1.00 27.05  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.024 2.560   2.423  1.00 28.91  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.137 -1.297  1.847  1.00 27.47  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.829 -1.998  1.792  1.00 28.34  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.669  -1.074  2.246  1.00 28.91  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.915  0.056   2.649  1.00 28.23  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.925 -3.189  2.740  1.00 28.81  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.015 -2.707  4.509  1.00 25.86  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.405  -1.588  2.237  1.00 28.71  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.266  -0.853  2.781  1.00 29.15  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.610  -1.662  3.926  1.00 28.11  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.402  -1.550  4.156  1.00 29.31  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.232  -0.449  1.684  1.00 32.75  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.453  -1.604  1.102  1.00 39.93  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.807  -2.776  1.393  1.00 41.86  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.487  -1.346  0.321  1.00 45.08  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.419  -2.455  4.687  1.00 25.38  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.953  -3.227  5.858  1.00 22.94  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.228  -2.296  6.823  1.00 21.68  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.653  -1.144  7.033  1.00 21.04  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.116  -3.919  6.583  1.00 22.56  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.674  -5.480  5.830  1.00 24.17  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.160  -2.791  7.402  1.00 19.53  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.456  -2.088  8.450  1.00 19.47  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.409  -2.893  9.743  1.00 16.54  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.568  -2.645  10.596 1.00 17.77  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.043  -1.669  8.013  1.00 22.36  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.992  -0.350  7.263  1.00 26.15  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.562  0.035   6.961  1.00 30.89  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.090  -0.076  5.830  1.00 33.84  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.836  0.463   7.989  1.00 32.08  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.250  -3.982  9.872  1.00 15.82  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.385  -4.758  11.108 1.00 14.71  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.898  -4.911  11.347 1.00 13.73  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.700  -5.006  10.401 1.00 14.80  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.694  -6.170  11.059 1.00 18.58  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.373  -6.965  10.088 1.00 22.14  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.220  -6.115  10.673 1.00 20.52  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.255  -4.953  12.619 1.00 12.50  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.656  -5.126  12.982 1.00 13.03  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.796  -5.253  14.486 1.00 12.64  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.809  -5.505  15.174 1.00 14.38  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.024 -5.112  14.959 1.00 11.18  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.344 -5.248  16.388 1.00 11.25  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.209 -4.020  16.778 1.00 12.80  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.181 -3.723  16.091 1.00 13.59  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.072 -6.603  16.682 1.00 12.82  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.558 -6.678  18.158 1.00 13.66  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.162 -7.793  16.367 1.00 13.90  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.924 -3.403  17.930 1.00 13.50  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.773 -2.296  18.396 1.00 12.44  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.339 -2.578  19.760 1.00 14.48  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.775 -3.351  20.527 1.00 14.96  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.059 -0.897  18.344 1.00 11.97  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.109 -0.642  19.512 1.00 14.29  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.858  -1.259  19.572 1.00 15.50  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.427 0.276   20.506 1.00 17.05  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.951  -0.959  20.591 1.00 18.22  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.541  0.553   21.540 1.00 18.67  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.328  -0.108  21.610 1.00 18.72  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.455  0.191   22.636 1.00 21.36  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.461 -1.940  20.079 1.00 14.21  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.098 -2.075  21.382 1.00 16.33  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.611 -0.906  22.266 1.00 17.14  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.737 0.271   21.886 1.00 17.16  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.637 -2.097  21.275 1.00 17.66  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.242 -2.194  22.662 1.00 20.35  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.064 -3.329  23.427 1.00 22.71  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.866 -1.098  23.251 1.00 22.34  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.601 -3.430  24.712 1.00 25.17  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.402 -1.177  24.536 1.00 24.83  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.241 -2.344  25.269 1.00 27.47  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.740 -2.439  26.553 1.00 32.55  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.089 -1.224  23.469 1.00 19.37  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.583 -0.207  24.412 1.00 21.74  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.467 -0.229  25.681 1.00 24.78  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.330 -1.135  26.500 1.00 26.58  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.115 -0.484  24.731 1.00 23.74  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.447 0.460   26.130 1.00 25.64  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.394 0.754   25.787 1.00 25.44  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.363 0.821   26.877 1.00 28.07  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.730 0.976   28.243 1.00 30.49  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.216 0.357   29.178 1.00 33.08  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.377 1.938   26.658 1.00 31.38  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.749 3.198   26.536 1.00 38.79  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.609 1.702   28.357 1.00 30.33  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.909 1.838   29.641 1.00 31.57  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.261 0.544   30.151 1.00 31.81  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.749 0.554   31.283 1.00 35.31  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.853 2.922   29.589 1.00 32.66  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.817 2.643   28.660 1.00 33.33  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.274 -0.528  29.357 1.00 29.33  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.769 -1.826  29.769 1.00 28.78  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.841 -2.899  29.620 1.00 30.58  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.551 -4.077  29.909 1.00 32.20  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.519 -2.203  28.933 1.00 28.82  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.269  -1.371  29.253 1.00 29.95  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.690  -1.709  30.641 1.00 33.67  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.488  -0.931  30.901 1.00 37.73  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.488  0.269   31.479 1.00 42.47  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.621  0.800   31.926 1.00 43.99  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.355  0.942   31.626 1.00 45.37  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.053 -2.557  29.062 1.00 31.10  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.116 -3.528  28.724 1.00 32.46  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.507 -4.699  27.928 1.00 31.26  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.796 -5.881  28.186 1.00 31.92  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.870 -4.009  29.971 1.00 35.49  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.782 -2.961  30.560 1.00 42.03  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.368 -3.553  31.822 1.00 48.36  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.235 -2.627  32.522 1.00 56.56  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.549 -2.717  33.810 1.00 62.97  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.084 -3.719  34.547 1.00 64.55  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 19.318 -1.797  34.375 1.00 64.89  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.578 -4.365  26.989 1.00 28.43  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.878 -5.426  26.263 1.00 25.95  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.645 -5.047  24.808 1.00 22.44  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.549 -3.849  24.517 1.00 21.36  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.456 -5.621  26.845 1.00 29.40  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.267 -6.651  27.937 1.00 38.19  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.759  -6.920  28.052 1.00 45.58  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.379  -8.043  28.985 1.00 50.37  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.381  -7.603  30.404 1.00 53.11  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.498 -6.041  23.946 1.00 20.02  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.090 -5.800  22.555 1.00 17.68  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.567 -6.066  22.457 1.00 19.00  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.031 -6.994  23.090 1.00 20.50  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.825 -6.713  21.555 1.00 16.98  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.301 -6.517  21.514 1.00 17.94  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.914 -5.763  20.506 1.00 19.74  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.241 -6.986  22.336 1.00 18.51  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.206 -5.804  20.781 1.00 19.09  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.449 -6.514  21.872 1.00 21.29  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.850  -5.263  21.644 1.00 16.69  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.399  -5.476  21.454 1.00 16.45  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.072  -5.557  19.971 1.00 15.44  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.543  -4.745  19.168 1.00 14.17  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.580  -4.292  22.026 1.00 18.28  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.630  -4.235  23.539 1.00 20.61  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.905  -5.135  24.317 1.00 22.59  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.343  -3.241  24.194 1.00 22.94  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.945  -5.082  25.717 1.00 24.94  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.385  -3.178  25.590 1.00 24.92  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.708  -4.115  26.344 1.00 25.76  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.739  -4.014  27.738 1.00 30.53  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.205  -6.505  19.578 1.00 16.35  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.696  -6.520  18.189 1.00 16.02  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.636  -5.423  18.018 1.00 17.27  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.831  -5.207  18.950 1.00 19.81  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.027  -7.896  18.070 1.00 17.67  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.684  -8.266  19.498 1.00 19.24  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.516  -7.499  20.448 1.00 17.96  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.609  -4.742  16.853 1.00 15.98  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.638  -3.667  16.631 1.00 17.28  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.147  -3.647  15.200 1.00 15.96  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.896  -3.968  14.265 1.00 16.49  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.237  -2.255  16.944 1.00 19.80  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.287  -1.977  18.446 1.00 22.57  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.601  -2.074  16.274 1.00 19.93  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.951  -3.091  15.012 1.00 15.91  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.443  -2.657  13.701 1.00 17.75  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.650  -1.133  13.684 1.00 19.97  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.482  -0.490  14.734 1.00 22.83  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.956  -2.958  13.514 1.00 20.66  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.763  -4.361  13.578 1.00 27.53  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.142  -0.581  12.570 1.00 16.08  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.433  0.859   12.532 1.00 16.48  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.931  1.474   11.284 1.00 18.62  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.734  0.784   10.267 1.00 20.52  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.935  1.134   12.769 1.00 15.80  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.915  0.395   11.876 1.00 14.40  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.351  -0.884  12.207 1.00 13.36  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.413  0.987   10.714 1.00 14.46  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.301  -1.531  11.428 1.00 14.09  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.321  0.308   9.903  1.00 15.41  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.762  -0.950  10.261 1.00 14.50  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.620  2.803   11.343 1.00 18.45  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.022  3.440   10.194 1.00 20.24  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.055  3.783   9.086  1.00 20.58  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.258  3.621   9.280  1.00 19.12  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.235  4.683   10.621 1.00 22.73  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.160  5.633   11.132 1.00 24.13  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.598  4.228   7.923  1.00 23.03  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.507  4.646   6.832  1.00 24.21  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.153  6.004   7.172  1.00 24.20  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.538  6.796   7.879  1.00 24.59  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.713  4.729   5.510  1.00 28.48  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 1.979  3.425   5.258  1.00 35.59  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.247  3.373   3.917  1.00 42.91  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.964  2.486   2.920  1.00 47.80  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 3.289  3.059   2.546  1.00 50.48  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.411  6.272   6.733  1.00 23.29  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.046  7.562   7.081  1.00 23.14  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.208  8.766   6.635  1.00 24.07  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.694  8.835   5.490  1.00 24.37  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.425  7.517   6.410  1.00 24.81  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.456  6.315   5.543  1.00 26.44  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.299  5.402   5.929  1.00 23.53  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.983  9.678   7.579  1.00 24.09  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.101  10.816  7.297  1.00 26.04  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.441  12.023  8.165  1.00 25.33  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.350  11.953  9.011  1.00 22.78  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.648  10.380  7.485  1.00 30.38  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.420  10.164  8.865  1.00 36.63  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.750  13.159  7.904  1.00 25.89  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.900  14.400  8.661  1.00 26.83  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.952  14.285  9.845  1.00 28.40  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.716  14.175  9.657  1.00 30.69  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.438  15.592  7.804  1.00 27.25  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.490  16.220  6.944  1.00 30.65  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.859  17.262  5.993  1.00 32.76  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.485  16.925  7.791  1.00 31.89  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.497  14.321  11.049 1.00 27.75  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.721  14.142  12.271 1.00 29.47  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.039  15.318  13.211 1.00 32.07  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.212  15.675  13.389 1.00 30.80  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.075  12.764  12.892 1.00 29.97  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.479  11.624  12.044 1.00 30.94  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.627  12.657  14.344 1.00 30.99  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.955  10.292  12.339 1.00 31.79  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.990  15.949  13.790 1.00 34.44  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.221  17.068  14.711 1.00 38.14  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.888  16.545  15.992 1.00 37.67  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.495  15.518  16.523 1.00 39.50  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.894  17.768  15.070 1.00 41.65  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.078  19.085  15.786 1.00 45.29  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.248  20.256  15.078 1.00 48.13  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.058  19.149  17.169 1.00 47.34  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.419  21.471  15.737 1.00 49.94  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.217  20.365  17.827 1.00 48.97  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.380  21.516  17.108 1.00 49.74  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.939  17.212  16.445 1.00 35.92  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.687  16.858  17.646 1.00 35.16  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.697  18.094  18.558 1.00 37.08  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.065  19.209  18.142 1.00 36.01  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.132  16.362  17.324 1.00 34.09  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.882  15.952  18.591 1.00 34.16  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.107  15.224  16.322 1.00 32.54  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.278  17.881  19.802 1.00 39.75  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.190  18.922  20.831 1.00 41.39  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.542  19.555  21.079 1.00 41.58  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.572  18.871  20.967 1.00 41.89  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.740  18.279  22.153 1.00 45.23  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.551  17.352  22.016 1.00 53.08  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.398  17.689  22.939 1.00 63.31  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.312  18.854  23.388 1.00 66.05  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.582  16.779  23.216 1.00 66.66  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.544  20.834  21.530 1.00 41.65  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.796  21.526  21.822 1.00 41.83  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.597  20.803  22.901 1.00 41.91  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.032  20.154  23.780 1.00 43.35  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.522  22.976  22.239 1.00 42.23  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.904  20.866  22.802 1.00 40.48  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.803  20.261  23.773 1.00 40.26  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.981 21.245  23.996 1.00 41.92  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.041 22.321  23.376 1.00 41.71  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.298 18.893  23.263 1.00 40.30  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.370 19.045  22.345 1.00 41.19  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.918 20.874  24.871 1.00 42.55  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.142 21.627  25.118 1.00 42.79  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.072 21.674  23.890 1.00 41.12  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.931 22.546  23.799 1.00 42.40  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.872 21.084  26.369 1.00 48.12  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.751 19.575  26.565 1.00 55.63  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.537 18.971  27.713 1.00 68.48  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 14.057 19.026  28.871 1.00 70.12  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.622 18.404  27.446 1.00 73.09  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.891 20.761  22.919 1.00 38.05  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.738 20.715  21.726 1.00 35.17  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.091 21.364  20.492 1.00 31.92  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.809 21.758  19.580 1.00 32.60  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.115 19.239  21.399 1.00 34.49  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.550 18.453  22.616 1.00 35.60  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.862 18.490  23.059 1.00 36.78  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.654 17.655  23.306 1.00 36.60  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.263 17.765  24.178 1.00 37.96  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.027 16.979  24.456 1.00 38.64  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.331 17.043  24.897 1.00 40.06  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.680 16.349  26.040 1.00 42.80  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.754 21.430  20.424 1.00 30.03  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.075 22.007  19.238 1.00 28.13  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.772 22.692  19.638 1.00 30.75  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.107 22.257  20.579 1.00 32.13  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.645 20.863  18.242 1.00 25.49  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.714 19.922  17.728 1.00 22.51  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.564 20.301  16.695 1.00 21.56  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.811 18.618  18.204 1.00 21.50  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.520 19.431  16.194 1.00 20.77  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.731 17.723  17.672 1.00 19.99  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.590 18.131  16.670 1.00 19.98  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.575 17.295  16.161 1.00 18.10  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.331 23.712  18.866 1.00 31.24  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.957  24.220  19.086 1.00 32.41  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.919  23.211  18.524 1.00 33.99  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.297  22.209  17.875 1.00 33.38  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.931  25.528  18.306 1.00 32.76  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.007 25.364  17.242 1.00 32.60  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.968 24.288  17.660 1.00 31.11  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.617  23.455  18.745 1.00 35.80  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.563  22.569  18.232 1.00 36.44  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.596  22.656  16.694 1.00 34.30  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.810  23.741  16.137 1.00 35.06  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.210  23.014  18.762 1.00 38.07  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.576  21.481  16.022 1.00 31.59  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.778  21.469  14.572 1.00 30.28  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.309  20.125  13.980 1.00 28.94  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.039  19.186  14.730 1.00 29.37  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.300  21.659  14.299 1.00 30.23  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.131  20.348  14.499 1.00 29.61  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.571  20.573  14.921 1.00 28.93  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.473 19.473  14.543 1.00 27.28  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.566 18.312  15.188 1.00 25.65  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.455 17.398  14.800 1.00 21.81  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.791  18.062  16.238 1.00 26.14  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.272  20.029  12.640 1.00 28.61  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.048  18.742  12.004 1.00 29.19  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.407  18.105  11.783 1.00 23.74  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.347  18.748  11.297 1.00 21.71  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.349  18.884  10.659 1.00 32.69  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.923  19.374  10.719 1.00 37.46  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.862  18.483  10.679 1.00 40.34  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.635  20.729  10.660 1.00 40.19  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.545  18.931  10.664 1.00 42.72  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.330  21.190  10.638 1.00 42.44  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.284  20.288  10.652 1.00 44.64  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.007 20.745  10.616 1.00 48.68  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.535  16.859  12.220 1.00 20.32  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.774  16.108  11.981 1.00 18.45  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.476  15.196  10.786 1.00 18.40  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.423  14.561  10.730 1.00 19.55  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.247  15.330  13.226 1.00 17.01  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.460  14.404  12.949 1.00 17.30  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.122 13.920  14.199 1.00 18.02  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.303 14.640  15.173 1.00 17.68  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.595 12.677  14.182 1.00 15.55  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.349  15.194  9.791  1.00 15.98  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.147  14.416  8.582  1.00 16.32  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.835  13.046  8.696  1.00 17.44  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.665  12.813  9.608  1.00 17.22  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.667  15.204  7.371  1.00 17.69  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.077 15.365  7.464  1.00 18.71  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.379  12.102  7.842  1.00 17.24  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.949  10.778  7.760  1.00 16.43  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.811  10.019  9.067  1.00 15.81  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.692  9.212   9.377  1.00 14.82  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.409 10.878  7.315  1.00 16.08  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.556 11.495  5.943  1.00 18.98  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.632 10.706  4.796  1.00 22.16  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.598 12.799  5.576  1.00 21.21  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.705 11.554  3.772  1.00 22.83  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.692 12.825  4.186  1.00 22.83  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.735  10.302  9.834  1.00 17.21  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.514  9.694   11.163 1.00 16.74  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.474  8.560   11.064 1.00 16.47  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.462  8.720   10.399 1.00 17.28  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.009  10.796  12.146 1.00 18.16  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.887  10.400  13.633 1.00 19.59  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.243  9.958   14.226 1.00 19.35  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.314  11.607  14.475 1.00 22.20  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.693  7.434   11.770 1.00 16.03  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.745  6.289   11.753 1.00 16.55  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.306  6.023   13.175 1.00 18.06  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.191  5.966   14.043 1.00 18.76  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.529  5.062   11.252 1.00 15.55  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.009  5.273   9.790  1.00 16.82  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.065  3.981   9.226  1.00 20.23  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.446  4.156   10.364 1.00 19.32  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.983  5.867   13.452 1.00 17.51  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.547  5.622   14.816 1.00 18.54  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.149  4.173   15.030 1.00 18.71  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.618  3.515   14.126 1.00 18.58  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.324  6.518   15.238 1.00 21.59  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.572  8.012   15.308 1.00 24.86  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.332  8.729   15.835 1.00 27.71  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.757  8.351   16.177 1.00 25.79  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.304  3.745   16.267 1.00 18.20  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.869  2.412   16.701 1.00 19.09  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.283  2.507   18.107 1.00 21.36  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.540  3.469   18.824 1.00 21.70  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.054  1.458   16.732 1.00 19.78  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.447  1.527   18.485 1.00 22.12  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.946  1.442   19.845 1.00 24.70  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.993  0.690   20.604 1.00 25.94  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.280  -0.472  20.284 1.00 26.21  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.428 0.747   19.922 1.00 27.45  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.846 0.578   21.364 1.00 28.65  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.463 1.590   19.181 1.00 28.63  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.560  1.335   21.597 1.00 26.40  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.613  0.718   22.383 1.00 28.18  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.154  1.657   23.425 1.00 28.34  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.906  2.863   23.377 1.00 28.42  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.892  1.111   24.382 1.00 28.22  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.505  1.905   25.420 1.00 28.87  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.729  2.687   24.954 1.00 28.59  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.575  2.160   24.241 1.00 27.95  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.889  1.047   26.622 1.00 29.81  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.383  1.880   27.764 1.00 32.74  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.552  2.794   28.401 1.00 36.45  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.637  2.021   28.252 1.00 34.54  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.325  3.439   29.268 1.00 37.08  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.578  2.980   29.235 1.00 37.17  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.856  3.908   25.429 1.00 29.91  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.006  4.744   25.157 1.00 30.95  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.985  5.915   26.106 1.00 34.47  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.924  6.447   26.396 1.00 37.23  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.026  5.232   23.711 1.00 32.01  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.959  6.132   23.470 1.00 35.49  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.127  6.233   26.668 1.00 35.03  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.258  7.378   27.559 1.00 37.74  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.592 8.083   27.264 1.00 39.93  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.431 7.532   26.531 1.00 39.68  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.061  7.009   29.042 1.00 40.19  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.801  5.765   29.468 1.00 43.95  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.479  5.335   30.886 1.00 47.06  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.086 5.906   31.815 1.00 51.85  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.612  4.451   31.069 1.00 45.13  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.800 9.345   27.731 1.00 42.10  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.084 9.999   27.459 1.00 43.07  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.241 9.172   28.011 1.00 41.50  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.177 8.632   29.145 1.00 44.10  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.925 11.396  28.054 1.00 44.71  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.860 11.279  29.042 1.00 44.98  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.939  10.179  28.588 1.00 42.55  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.208 8.979   27.119 1.00 37.71  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.360 8.101   27.282 1.00 35.36  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.306 6.952   26.268 1.00 32.17  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.310 6.281   26.000 1.00 32.69  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.113 6.685   25.702 1.00 29.32  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.944 5.611   24.723 1.00 26.77  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.366 5.982   23.306 1.00 24.83  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.527 5.079   22.462 1.00 24.39  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.504 5.059   24.724 1.00 27.45  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.231 4.163   25.925 1.00 29.42  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.161 3.510   26.377 1.00 27.91  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.069 4.124   26.396 1.00 28.87  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.551 7.285   23.026 1.00 23.83  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.951 7.715   21.672 1.00 21.74  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.270 7.053   21.263 1.00 21.59  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.172 6.870   22.100 1.00 22.97  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.038 9.240   21.563 1.00 21.60  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.433 10.089  21.528 1.00 24.65  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.337 6.599   20.017 1.00 19.57  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.552 5.957   19.540 1.00 19.20  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.433 4.451   19.453 1.00 20.27  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.268 3.817   18.800 1.00 21.28  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.437 3.850   20.139 1.00 18.47  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.194 2.410   20.033 1.00 15.74  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.866 2.031   18.586 1.00 14.63  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.144 2.772   17.915 1.00 16.75  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.421 0.913   18.104 1.00 13.98  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.213 0.544   16.702 1.00 14.39  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.912 -0.169  16.498 1.00 13.75  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.543 -1.071  17.285 1.00 14.51  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.457 -0.299  16.203 1.00 17.36  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.658 0.649   15.911 1.00 20.19  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.154 -1.260  15.045 1.00 19.53  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.958 -0.163  15.596 1.00 22.75  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.282 0.094   15.315 1.00 11.73  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.102 -0.656  14.859 1.00 11.91  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.612 -1.465  13.645 1.00 12.97  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.241 -0.902  12.734 1.00 13.97  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.016 0.322   14.367 1.00 13.18  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.814 -0.329  13.566 1.00 12.91  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.011 -1.262  14.475 1.00 12.76  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.836  0.804   13.042 1.00 15.47  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.354 -2.795  13.647 1.00 13.82  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.814 -3.693  12.597 1.00 14.83  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.710 -4.536  12.057 1.00 15.72  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.860 -4.992  12.816 1.00 15.48  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.855 -4.695  13.183 1.00 17.54  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.096 -4.134  13.797 1.00 24.27  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.006 -5.272  14.284 1.00 27.82  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.574 -5.914  13.103 1.00 30.89  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.759 -5.608  12.596 1.00 31.95  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.592 -4.814  13.264 1.00 34.78  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.131 -6.106  11.437 1.00 31.56  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.780 -4.841  10.763 1.00 16.08  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.870 -5.824  10.128 1.00 18.63  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.771 -6.975  9.612  1.00 20.98  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.976 -6.942  9.853  1.00 20.82  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.059 -5.177  9.005  1.00 19.78  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.078 -4.573  7.604  1.00 20.02  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.213 -8.003  8.921  1.00 23.26  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.043 -9.100  8.425  1.00 25.99  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.100 -8.662  7.372  1.00 27.55  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.043 -9.424  7.084  1.00 29.00  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.161 -10.171 7.800  1.00 29.09  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.385 -9.671  6.580  1.00 32.97  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.459 -10.780 6.117  1.00 39.67  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.335  -10.927 6.612  1.00 41.34  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.940 -11.621 5.217  1.00 40.82  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.961 -7.434  6.817  1.00 26.99  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.882 -6.885  5.806  1.00 25.96  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.052 -6.096  6.426  1.00 24.81  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.998 -5.762  5.713  1.00 26.75  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.120 -5.992  4.794  1.00 26.83  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.972 -6.687  4.106  1.00 29.67  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.658 -6.292  4.305  1.00 30.94  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.984 -7.677  3.182  1.00 32.16  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.912 -7.114  3.590  1.00 33.40  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.663 -7.968  2.897  1.00 33.81  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.952 -5.732  7.717  1.00 22.29  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.993 -4.941  8.359  1.00 20.10  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.466 -3.758  9.160  1.00 17.85  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.305 -3.751  9.545  1.00 17.46  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.306 -2.751  9.361  1.00 16.81  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.946 -1.561  10.142 1.00 16.87  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.959 -0.676  9.402  1.00 15.70  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.233 -0.266  8.270  1.00 17.57  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.190 -0.754  10.577 1.00 17.97  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.766 0.523   11.306 1.00 17.87  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.099 -1.601  11.490 1.00 19.19  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.839 -0.338  10.054 1.00 14.38  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.806 0.508   9.459  1.00 14.06  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.935 1.978   9.945  1.00 12.77  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.755 2.923   9.180  1.00 13.54  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.416 -0.050  9.866  1.00 15.13  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.288 0.889   9.454  1.00 16.72  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.169 -1.458  9.314  1.00 16.45  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.219 2.151   11.232 1.00 11.57  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.299 3.513   11.784 1.00 12.56  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.683 3.512   13.235 1.00 12.91  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.093 2.472   13.769 1.00 12.73  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.575 4.677   13.873 1.00 12.46  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.927 4.771   15.291 1.00 12.66  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.810 5.490   16.044 1.00 13.21  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.131 6.362   15.504 1.00 12.78  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.274 5.514   15.495 1.00 15.32  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.348 6.824   14.710 1.00 18.43  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.487 4.649   15.244 1.00 16.41  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.540 7.760   15.255 1.00 21.10  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.618 5.118   17.342 1.00 13.73  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.638 5.802   18.177 1.00 13.10  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.937 7.314   18.209 1.00 13.59  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.079 7.695   18.397 1.00 15.04  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.645 5.236   19.612 1.00 14.03  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.714 6.054   20.504 1.00 15.34  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.228 3.747   19.649 1.00 14.35  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.911 8.141   18.031 1.00 14.19  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.059 9.586   17.981 1.00 15.39  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.020 10.330  18.800 1.00 19.14  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.293 11.472  19.246 1.00 19.88  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.967 10.044  16.520 1.00 15.38  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.095 11.459  16.431 1.00 17.55  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.794  9.766   18.943 1.00 21.32  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.707  10.442  19.725 1.00 24.07  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.960  9.412   20.607 1.00 27.17  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.133  8.203   20.450 1.00 25.47  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.713  11.222  18.806 1.00 25.25  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.867  10.329  18.089 1.00 27.30  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.379  12.220  17.865 1.00 25.84  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.126  9.895   21.522 1.00 30.47  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.343  8.997   22.355 1.00 33.58  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.304  9.712   23.179 1.00 37.05  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.149  10.934  23.076 1.00 37.70  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.607  8.926   23.980 1.00 40.04  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.582  9.427   24.886 1.00 43.61  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.204  8.928   24.521 1.00 45.76  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.934  8.676   23.352 1.00 45.37  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.310  8.863   25.508 1.00 46.94  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.071 8.416   25.340 1.00 48.24  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.241 6.935   24.930 1.00 46.26  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.297 6.560   24.425 1.00 48.16  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.793 9.351   24.362 1.00 51.54  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.910 10.765  24.897 1.00 56.92  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.103 10.978  26.111 1.00 59.03  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.851 11.759  24.012 1.00 57.11  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.731  6.077   25.232 1.00 43.11  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.675  4.677   24.824 1.00 39.80  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.053  4.502   23.354 1.00 36.19  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.775  3.462   22.753 1.00 36.43  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.759  5.478   22.802 1.00 32.95  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.207  5.511   21.417 1.00 30.22  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.727  5.612   21.374 1.00 28.29  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.317  6.323   22.185 1.00 31.92  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.606  6.754   20.711 1.00 30.42  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.070  6.769   20.596 1.00 32.10  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.453 8.167   20.241 1.00 34.40  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.399 5.732   19.584 1.00 32.39  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.331  5.105   20.298 1.00 22.62  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.760  5.269   20.070 1.00 20.71  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.970  5.700   18.598 1.00 19.23  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.324  5.142   17.709 1.00 19.79  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.548  3.984   20.406 1.00 21.02  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.993  2.744   19.703 1.00 22.43  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.026  4.156   20.098 1.00 21.91  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.792  6.721   18.373 1.00 17.58  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.047  7.196   17.025 1.00 16.92  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.463  6.919   16.575 1.00 16.94  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.403  7.083   17.354 1.00 17.61  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.624  6.471   15.293 1.00 14.48  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.948  6.135   14.752 1.00 13.31  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.280 7.029   13.558 1.00 13.41  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.464  7.154   12.638 1.00 13.97  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.980  4.676   14.259 1.00 12.54  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.487  3.660   15.270 1.00 12.90  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.336 3.161   16.247 1.00 13.71  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.159  3.233   15.267 1.00 14.96  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.873  2.223   17.181 1.00 13.46  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.704  2.293   16.193 1.00 15.41  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.566  1.809   17.156 1.00 14.26  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.524 7.540   13.530 1.00 12.71  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.987 8.316   12.385 1.00 11.81  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.437 7.262   11.338 1.00 11.64  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.362 6.475   11.592 1.00 11.71  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.182 9.179   12.791 1.00 11.66  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.825 7.262   10.144 1.00 12.60  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.181 6.320   9.082  1.00 13.36  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.541 6.653   8.492  1.00 14.12  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.894 7.838   8.306  1.00 14.86  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.119 6.422   7.956  1.00 14.48  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.325 5.395   6.874  1.00 20.84  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.435 4.217   7.207  1.00 19.14  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.482 5.795   5.691  1.00 25.53  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.317 5.591   8.108  1.00 13.29  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.598 5.818   7.404  1.00 14.36  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.633 5.041   6.069  1.00 16.03  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.672 5.088   5.397  1.00 18.86  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.860 5.474   8.246  1.00 15.24  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.898 6.281   9.563  1.00 15.88  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.950 3.966   8.542  1.00 15.28  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.549 4.323   5.705  1.00 15.89  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.545 3.478   4.522  1.00 16.52  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.657 4.221   3.211  1.00 20.36  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.109 3.628   2.221  1.00 23.22  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.311 2.569   4.520  1.00 16.12  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.256 1.646   5.693  1.00 16.06  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.916 0.899   5.649  1.00 15.76  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.777 1.753   5.988  1.00 16.81  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.535  1.334   6.158  1.00 20.09  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.215  0.069   5.906  1.00 19.90  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.599  2.174   6.581  1.00 21.73  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.265 5.497   3.182  1.00 20.86  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.382 6.277   1.947  1.00 22.24  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.815 6.837   1.734  1.00 21.98  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.115 7.354   0.635  1.00 23.02  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.356 7.423   1.905  1.00 23.58  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.579 8.466   2.975  1.00 25.57  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.882 8.074   4.144  1.00 24.05  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.446 9.678   2.665  1.00 25.91  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.721 6.746   2.739  1.00 21.48  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.089 7.326   2.633  1.00 20.99  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.008 6.377   1.916  1.00 23.53  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.840 5.704   2.535  1.00 24.11  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.632 7.692   4.015  1.00 19.35  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.692 8.565   4.855  1.00 18.74  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.304 8.831   6.221  1.00 18.63  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.425 9.925   4.159  1.00 19.35  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.824 6.294   0.583  1.00 25.26  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.499 5.291   -0.239 1.00 27.64  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.018 5.450   -0.236 1.00 30.11  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.738 4.453   -0.301 1.00 30.84  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.929 5.235   -1.676 1.00 28.40  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.415 5.151   -1.874 1.00 30.80  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.082 4.974   -3.352 1.00 33.97  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.784 4.019   -1.034 1.00 31.74  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.511 6.698   -0.057 1.00 30.90  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.941 6.997   0.003  1.00 30.99  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.674 6.385   1.219  1.00 32.49  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.908 6.336   1.206  1.00 34.57  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.178 8.513   -0.068 1.00 29.64  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.417 9.307   0.971  1.00 27.96  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.173 9.855   0.846  1.00 27.10  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.865 9.631   2.298  1.00 27.61  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.859 10.576  1.979  1.00 27.16  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.863 10.422  2.898  1.00 27.19  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.069 9.430   2.993  1.00 28.28  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.009 10.976  4.171  1.00 28.15  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.205 9.978   4.261  1.00 29.06  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.170 10.714  4.849  1.00 28.54  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.946 5.905   2.265  1.00 31.13  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.619 5.323   3.429  1.00 32.02  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.525 4.144   3.063  1.00 37.55  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.432 3.824   3.823  1.00 37.94  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.605 4.913   4.512  1.00 29.78  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.915 6.067   5.221  1.00 27.95  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.882 5.529   6.216  1.00 27.40  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.932 6.937   5.996  1.00 27.31  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.264 3.482   1.918  1.00 41.57  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.080 2.368   1.452  1.00 46.71  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.172 2.798   0.482  1.00 52.74  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 27.249 2.195   0.497  1.00 55.64  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.216 1.350   0.720  1.00 47.92  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.052 0.865   1.510  1.00 50.19  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.274 0.304   2.603  1.00 51.69  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.911 1.009   1.024  1.00 51.95  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.879 3.726   -0.447 1.00 54.93  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.871 4.103   -1.464 1.00 58.23  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.732 5.297   -1.087 1.00 60.41  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.667 5.630   -1.835 1.00 62.02  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.212 4.330   -2.834 1.00 61.80  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.094 5.356   -2.798 1.00 67.48  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.770 4.862   -3.347 1.00 73.61  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 22.912 5.715   -3.672 1.00 74.41  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.585 3.627   -3.455 1.00 76.15  ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BPV B 2 .   ? 9.922  14.243  22.439 1.00 34.04  ? 201 A1BPV A N1  1 
HETATM 1079 C  C4  . A1BPV B 2 .   ? 6.932  10.064  26.230 1.00 43.23  ? 201 A1BPV A C4  1 
HETATM 1080 C  C5  . A1BPV B 2 .   ? 6.470  11.350  26.327 1.00 43.38  ? 201 A1BPV A C5  1 
HETATM 1081 C  C6  . A1BPV B 2 .   ? 7.096  12.373  25.629 1.00 42.88  ? 201 A1BPV A C6  1 
HETATM 1082 C  C7  . A1BPV B 2 .   ? 8.212  12.089  24.841 1.00 41.69  ? 201 A1BPV A C7  1 
HETATM 1083 C  C8  . A1BPV B 2 .   ? 9.045  13.284  22.858 1.00 35.39  ? 201 A1BPV A C8  1 
HETATM 1084 C  C10 . A1BPV B 2 .   ? 12.194 15.199  22.592 1.00 31.54  ? 201 A1BPV A C10 1 
HETATM 1085 C  C13 . A1BPV B 2 .   ? 11.029 15.031  18.881 1.00 25.97  ? 201 A1BPV A C13 1 
HETATM 1086 O  O2  . A1BPV B 2 .   ? 10.663 16.183  18.602 1.00 25.83  ? 201 A1BPV A O2  1 
HETATM 1087 N  N2  . A1BPV B 2 .   ? 11.314 14.122  17.964 1.00 23.47  ? 201 A1BPV A N2  1 
HETATM 1088 C  C12 . A1BPV B 2 .   ? 11.158 14.576  20.325 1.00 29.17  ? 201 A1BPV A C12 1 
HETATM 1089 C  C11 . A1BPV B 2 .   ? 12.277 15.335  21.066 1.00 30.64  ? 201 A1BPV A C11 1 
HETATM 1090 C  C9  . A1BPV B 2 .   ? 11.277 14.074  22.993 1.00 33.25  ? 201 A1BPV A C9  1 
HETATM 1091 C  C14 . A1BPV B 2 .   ? 9.828  14.747  21.062 1.00 31.74  ? 201 A1BPV A C14 1 
HETATM 1092 O  O1  . A1BPV B 2 .   ? 8.269  12.741  22.086 1.00 33.23  ? 201 A1BPV A O1  1 
HETATM 1093 N  N   . A1BPV B 2 .   ? 8.970  13.094  24.201 1.00 39.61  ? 201 A1BPV A N   1 
HETATM 1094 C  C3  . A1BPV B 2 .   ? 8.017  9.771   25.425 1.00 42.97  ? 201 A1BPV A C3  1 
HETATM 1095 C  C2  . A1BPV B 2 .   ? 8.677  10.772  24.720 1.00 42.03  ? 201 A1BPV A C2  1 
HETATM 1096 C  C1  . A1BPV B 2 .   ? 9.852  10.387  23.858 1.00 41.80  ? 201 A1BPV A C1  1 
HETATM 1097 O  O   . A1BPV B 2 .   ? 10.152 9.028   24.041 1.00 41.43  ? 201 A1BPV A O   1 
HETATM 1098 C  C   . A1BPV B 2 .   ? 10.501 8.415   22.830 1.00 41.27  ? 201 A1BPV A C   1 
HETATM 1099 ZN ZN  . ZN    C 3 .   ? 10.859 -4.750  5.610  1.00 23.50  2 202 ZN    A ZN  1 
HETATM 1100 S  S   . DMS   D 4 .   ? 20.883 0.971   21.881 1.00 105.09 ? 203 DMS   A S   1 
HETATM 1101 O  O   . DMS   D 4 .   ? 19.536 1.567   21.591 1.00 105.07 ? 203 DMS   A O   1 
HETATM 1102 C  C1  . DMS   D 4 .   ? 20.629 -0.450  22.973 1.00 105.09 ? 203 DMS   A C1  1 
HETATM 1103 C  C2  . DMS   D 4 .   ? 21.697 1.997   23.137 1.00 105.09 ? 203 DMS   A C2  1 
HETATM 1104 O  O   . HOH   E 5 .   ? 23.678 -0.024  14.963 1.00 30.00  ? 301 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 19.991 22.542  7.894  1.00 29.61  ? 302 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 17.832 2.459   23.144 1.00 27.25  ? 303 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 8.768  2.290   2.890  1.00 29.62  ? 304 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 2.342  7.881   9.983  1.00 38.72  ? 305 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 8.152  19.689  18.218 1.00 29.74  ? 306 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 23.018 18.191  19.396 1.00 43.20  ? 307 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 3.458  -5.076  21.132 1.00 34.97  ? 308 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 23.604 21.918  8.029  1.00 28.27  ? 309 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 4.909  26.104  16.713 1.00 43.97  ? 310 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 22.649 -1.712  4.124  1.00 36.47  ? 311 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 6.501  14.502  22.861 1.00 38.46  ? 312 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 10.464 7.973   4.629  1.00 25.60  ? 313 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 1.048  14.194  18.279 1.00 40.52  ? 314 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 6.738  16.588  22.271 1.00 34.15  ? 315 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 0.868  -2.697  20.554 1.00 41.82  ? 316 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 12.136 10.620  0.546  1.00 36.60  ? 317 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 6.005  1.290   6.145  1.00 37.80  ? 318 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 8.098  -3.882  0.549  1.00 26.44  ? 319 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 10.748 17.070  5.503  1.00 33.77  ? 320 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 19.963 8.849   19.022 1.00 22.43  ? 321 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 0.440  -0.448  16.488 1.00 23.68  ? 322 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 10.786 -4.955  31.751 1.00 33.81  ? 323 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 18.294 4.658   26.844 1.00 36.42  ? 324 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 17.190 20.740  18.816 1.00 36.16  ? 325 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 18.167 18.904  5.567  1.00 36.33  ? 326 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 14.648 2.445   23.227 1.00 19.59  ? 327 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 17.770 21.129  9.663  1.00 22.77  ? 328 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 11.236 11.386  11.324 1.00 13.40  ? 329 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 21.161 19.036  17.968 1.00 39.27  ? 330 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 16.194 -11.112 5.247  1.00 43.93  ? 331 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 6.479  -6.019  29.140 1.00 35.00  ? 332 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 9.830  4.200   33.981 1.00 29.57  ? 333 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 9.286  18.241  19.843 1.00 28.72  ? 334 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 30.558 10.530  15.024 1.00 39.57  ? 335 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 21.717 -5.714  10.432 1.00 34.12  ? 336 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 9.222  20.757  10.723 1.00 34.30  ? 337 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 11.250 2.128   33.557 1.00 25.32  ? 338 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? -0.959 -4.988  15.709 0.50 24.80  ? 339 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 10.148 4.601   3.496  1.00 23.11  ? 340 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 31.268 20.434  16.631 1.00 33.26  ? 341 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 17.935 18.776  17.059 1.00 19.73  ? 342 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 2.831  3.282   27.703 1.00 38.16  ? 343 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 14.829 11.255  0.722  1.00 46.32  ? 344 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 13.009 10.357  9.331  1.00 12.83  ? 345 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 14.711 -4.553  17.148 1.00 25.41  ? 346 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 5.382  -1.714  24.398 1.00 28.93  ? 347 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 16.644 17.456  4.023  1.00 48.11  ? 348 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? -1.412 15.449  24.797 1.00 39.61  ? 349 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 18.377 9.267   25.757 1.00 37.88  ? 350 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 17.986 -6.919  3.267  1.00 30.35  ? 351 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 29.942 10.990  19.425 1.00 31.66  ? 352 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 6.743  3.412   33.077 1.00 36.77  ? 353 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 5.648  22.474  11.103 1.00 37.84  ? 354 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 18.643 -0.371  19.607 1.00 28.78  ? 355 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 4.199  -5.428  6.602  1.00 34.16  ? 356 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 28.432 -2.270  13.196 1.00 43.25  ? 357 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 27.546 15.937  2.742  1.00 42.06  ? 358 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 22.371 18.882  6.149  1.00 25.51  ? 359 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 14.236 14.238  3.514  1.00 30.31  ? 360 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 16.735 -7.699  10.842 1.00 35.52  ? 361 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 14.347 20.842  8.401  1.00 36.22  ? 362 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 5.178  7.670   28.457 1.00 39.23  ? 363 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 14.792 12.252  24.209 1.00 30.57  ? 364 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 19.563 23.631  15.451 1.00 27.45  ? 365 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 6.705  12.368  5.348  1.00 28.85  ? 366 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 15.643 -4.742  1.848  1.00 28.50  ? 367 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 8.621  -7.656  9.237  1.00 37.59  ? 368 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 18.518 12.513  1.968  1.00 41.57  ? 369 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 32.554 14.369  20.774 1.00 36.80  ? 370 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 30.304 6.061   17.709 1.00 44.91  ? 371 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 28.973 16.553  23.132 1.00 47.13  ? 372 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 1.349  -2.841  17.609 1.00 26.61  ? 373 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 11.715 21.255  12.384 1.00 31.18  ? 374 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 2.430  -6.658  14.739 1.00 38.51  ? 375 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 19.576 -0.018  26.991 1.00 30.35  ? 376 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 3.952  5.419   25.122 1.00 36.65  ? 377 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 0.663  0.801   24.352 1.00 39.08  ? 378 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 18.183 0.979   29.875 1.00 43.92  ? 379 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 4.101  -2.558  21.754 1.00 52.30  ? 380 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 12.324 -8.066  13.234 1.00 37.07  ? 381 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? -0.136 12.111  20.972 1.00 43.18  ? 382 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 6.964  -5.323  2.852  1.00 35.14  ? 383 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 5.934  -7.915  14.374 1.00 30.33  ? 384 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 17.200 22.547  16.997 1.00 34.76  ? 385 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 23.799 2.151   19.552 1.00 42.67  ? 386 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 22.150 8.663   20.871 1.00 31.57  ? 387 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 21.499 -4.136  35.155 1.00 48.40  ? 388 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 30.876 15.336  22.446 1.00 33.11  ? 389 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 3.949  10.803  19.628 1.00 49.12  ? 390 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 2.525  13.078  23.121 1.00 49.79  ? 391 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? -0.976 14.861  12.434 1.00 38.26  ? 392 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 7.904  19.199  7.921  1.00 43.29  ? 393 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 4.723  -1.521  28.891 1.00 50.21  ? 394 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 13.420 -6.155  32.589 1.00 49.56  ? 395 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 3.601  12.503  17.955 1.00 58.06  ? 396 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 10.626 15.248  26.527 1.00 44.80  ? 397 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 10.892 17.957  26.693 1.00 45.45  ? 398 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 20.869 22.008  17.707 1.00 28.01  ? 399 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 19.197 8.749   -2.133 1.00 37.09  ? 400 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 31.671 8.277   15.788 1.00 37.79  ? 401 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 0.131  -3.203  9.398  1.00 52.76  ? 402 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 8.415  17.442  25.877 1.00 36.75  ? 403 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 17.077 -3.708  18.255 1.00 34.18  ? 404 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 4.736  14.446  21.360 1.00 30.83  ? 405 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 1.941  1.105   26.785 1.00 37.76  ? 406 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 11.602 23.267  14.182 1.00 37.57  ? 407 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 8.410  22.524  26.694 1.00 43.12  ? 408 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 25.229 -2.589  0.614  1.00 58.39  ? 409 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 32.883 21.763  12.211 1.00 41.33  ? 410 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 13.356 13.970  26.332 1.00 55.42  ? 411 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 0.751  -2.122  23.791 1.00 37.20  ? 412 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 32.710 21.837  14.782 1.00 36.98  ? 413 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 9.323  -8.788  12.350 1.00 34.62  ? 414 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 19.942 -3.786  22.140 1.00 59.08  ? 415 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 0.779  11.557  18.356 1.00 46.62  ? 416 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 9.714  24.917  13.140 1.00 38.39  ? 417 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   . SER   A 1   ? 0.7570 0.2457 0.3985 -0.0459 -0.2085 0.0101  7   SER   A N   
2    C CA  . SER   A 1   ? 0.7091 0.2502 0.4482 -0.0469 -0.2358 0.0179  7   SER   A CA  
3    C C   . SER   A 1   ? 0.6160 0.2323 0.4440 -0.0370 -0.2207 0.0159  7   SER   A C   
4    O O   . SER   A 1   ? 0.6120 0.2292 0.4221 -0.0348 -0.2070 0.0121  7   SER   A O   
5    C CB  . SER   A 1   ? 0.7680 0.2510 0.4965 -0.0689 -0.2962 0.0346  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.8353 0.2856 0.5346 -0.0785 -0.3127 0.0394  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5359 0.2075 0.4542 -0.0322 -0.2207 0.0183  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4727 0.2059 0.4749 -0.0253 -0.2027 0.0163  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4078 0.1935 0.4732 -0.0165 -0.1777 0.0116  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3962 0.1849 0.4361 -0.0117 -0.1648 0.0065  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3555 0.1780 0.5008 -0.0151 -0.1668 0.0132  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3101 0.1707 0.5095 -0.0093 -0.1391 0.0085  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2709 0.1627 0.5189 -0.0075 -0.1068 0.0029  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2744 0.1628 0.5368 -0.0104 -0.1117 0.0058  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2995 0.1509 0.5615 -0.0134 -0.1642 0.0221  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2490 0.1645 0.5153 -0.0046 -0.0730 -0.0053 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2269 0.1579 0.5290 -0.0061 -0.0369 -0.0116 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2301 0.1609 0.6160 -0.0063 -0.0248 -0.0047 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2247 0.1566 0.6177 -0.0043 -0.0226 -0.0041 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2352 0.1789 0.4826 -0.0071 -0.0065 -0.0247 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2520 0.1977 0.4316 -0.0055 -0.0177 -0.0273 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2442 0.1883 0.5092 -0.0133 0.0303  -0.0320 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2528 0.2112 0.3895 -0.0078 0.0011  -0.0332 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2430 0.1713 0.6978 -0.0083 -0.0145 0.0018  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2404 0.1656 0.7940 -0.0079 0.0045  0.0117  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2483 0.1687 0.8095 -0.0103 0.0641  -0.0008 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2519 0.1691 0.8210 -0.0129 0.0790  -0.0031 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2277 0.1469 0.8662 -0.0099 -0.0290 0.0335  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2549 0.1626 0.8759 -0.0128 -0.0901 0.0474  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2630 0.1659 0.9246 -0.0129 -0.1090 0.0591  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3014 0.1955 0.8521 -0.0170 -0.1263 0.0475  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2992 0.1810 0.9260 -0.0188 -0.1647 0.0703  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3360 0.2039 0.8472 -0.0230 -0.1778 0.0579  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3373 0.1972 0.8873 -0.0250 -0.1990 0.0700  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3819 0.2055 0.8858 -0.0344 -0.2513 0.0810  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2700 0.1832 0.8183 -0.0112 0.0988  -0.0096 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2988 0.1905 0.8305 -0.0179 0.1580  -0.0229 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3012 0.1748 0.8949 -0.0166 0.1951  -0.0195 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3134 0.1929 0.8930 -0.0140 0.1832  -0.0190 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3563 0.2451 0.7694 -0.0259 0.1638  -0.0398 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3584 0.2607 0.7315 -0.0228 0.1391  -0.0398 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3985 0.2500 0.7760 -0.0385 0.2207  -0.0529 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2928 0.1430 0.9613 -0.0177 0.2419  -0.0157 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3016 0.1298 1.0421 -0.0154 0.2843  -0.0103 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3017 0.1553 1.1306 -0.0057 0.2409  0.0109  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2910 0.1666 1.1741 -0.0023 0.1910  0.0282  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3095 0.1578 1.1367 -0.0036 0.2512  0.0096  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2876 0.1571 1.1903 0.0038  0.2068  0.0296  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2664 0.1582 1.0749 0.0041  0.1507  0.0235  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2580 0.1578 1.0900 0.0079  0.1260  0.0321  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3346 0.1845 1.3119 0.0073  0.2531  0.0352  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3865 0.2173 1.5016 0.0102  0.2985  0.0522  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3898 0.2334 1.5863 0.0114  0.2731  0.0708  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4209 0.2164 1.5692 0.0108  0.3693  0.0480  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2519 0.1517 0.9599 0.0001  0.1318  0.0103  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2442 0.1597 0.8617 0.0006  0.0898  0.0042  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2246 0.1496 0.8153 0.0004  0.0400  0.0099  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2212 0.1445 0.8163 -0.0021 0.0444  0.0094  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2601 0.1710 0.7714 -0.0052 0.1177  -0.0163 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2804 0.1717 0.7853 -0.0088 0.1631  -0.0240 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2854 0.1811 0.8200 -0.0035 0.1561  -0.0181 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3190 0.1800 0.7810 -0.0194 0.2132  -0.0370 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3199 0.1928 0.8483 -0.0072 0.2000  -0.0248 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3614 0.1910 0.8059 -0.0257 0.2573  -0.0441 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3716 0.2088 0.8510 -0.0188 0.2512  -0.0381 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4167 0.2203 0.8752 -0.0251 0.2946  -0.0449 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2217 0.1509 0.7715 0.0020  -0.0030 0.0134  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2099 0.1353 0.7067 0.0003  -0.0463 0.0162  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2049 0.1352 0.6021 0.0021  -0.0460 0.0029  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1910 0.1227 0.5731 0.0045  -0.0488 0.0021  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1932 0.1028 0.7347 -0.0029 -0.0982 0.0367  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2491 0.1370 0.7107 -0.0075 -0.1429 0.0385  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3004 0.1601 0.8008 -0.0162 -0.1975 0.0608  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3639 0.1916 0.7743 -0.0210 -0.2302 0.0596  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4266 0.2155 0.7639 -0.0300 -0.2626 0.0622  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4188 0.2034 0.7619 -0.0339 -0.2689 0.0656  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4588 0.2076 0.7106 -0.0354 -0.2847 0.0605  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1978 0.1313 0.5334 0.0010  -0.0406 -0.0059 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2052 0.1442 0.4616 0.0028  -0.0386 -0.0142 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2142 0.1348 0.4258 0.0037  -0.0710 -0.0096 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2231 0.1350 0.4280 0.0015  -0.0803 -0.0080 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2072 0.1579 0.4268 -0.0006 -0.0106 -0.0241 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2132 0.1726 0.3722 0.0005  -0.0092 -0.0270 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2026 0.1534 0.4537 -0.0062 0.0254  -0.0296 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2306 0.1394 0.4044 0.0060  -0.0843 -0.0082 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2752 0.1498 0.3915 0.0047  -0.1089 -0.0049 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2715 0.1456 0.3294 0.0100  -0.0929 -0.0098 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2621 0.1616 0.3319 0.0133  -0.0746 -0.0127 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3201 0.1602 0.4489 -0.0012 -0.1469 0.0063  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3312 0.1684 0.5274 -0.0076 -0.1685 0.0173  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3003 0.1509 0.4512 0.0018  -0.1433 0.0069  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2825 0.1207 0.2784 0.0098  -0.0991 -0.0091 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2937 0.1229 0.2447 0.0153  -0.0812 -0.0105 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3112 0.1269 0.2648 0.0146  -0.0934 -0.0081 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3456 0.1251 0.2944 0.0070  -0.1247 -0.0033 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3450 0.1203 0.2262 0.0139  -0.0815 -0.0097 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3631 0.1490 0.2389 0.0159  -0.0670 -0.0112 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3690 0.1440 0.2476 0.0103  -0.0841 -0.0109 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3251 0.1358 0.2032 0.0229  -0.0379 -0.0107 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2865 0.1287 0.2500 0.0205  -0.0737 -0.0092 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2793 0.1118 0.2478 0.0205  -0.0834 -0.0074 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3539 0.1220 0.2589 0.0162  -0.0982 -0.0052 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3845 0.1277 0.2912 0.0102  -0.1243 -0.0016 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2659 0.1347 0.2501 0.0270  -0.0587 -0.0078 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2511 0.1198 0.2518 0.0278  -0.0663 -0.0065 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2468 0.1430 0.2504 0.0334  -0.0420 -0.0048 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2363 0.1410 0.2590 0.0351  -0.0438 -0.0038 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3214 0.1954 0.3166 0.0371  -0.0473 -0.0022 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3376 0.1607 0.2782 0.0358  -0.0496 -0.0022 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3071 0.1939 0.3231 0.0392  -0.0470 -0.0011 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3940 0.1268 0.2398 0.0173  -0.0819 -0.0065 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4799 0.1337 0.2466 0.0103  -0.0894 -0.0058 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5500 0.1477 0.2825 -0.0054 -0.1319 -0.0021 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.6321 0.1548 0.2952 -0.0174 -0.1507 0.0002  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.5164 0.1395 0.2308 0.0162  -0.0502 -0.0073 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5315 0.1412 0.2247 0.0151  -0.0434 -0.0082 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4972 0.1699 0.2447 0.0233  -0.0271 -0.0076 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5851 0.1194 0.2023 0.0053  -0.0504 -0.0092 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5324 0.1729 0.2437 0.0202  -0.0247 -0.0085 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5907 0.1471 0.2219 0.0098  -0.0365 -0.0097 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5205 0.1515 0.3050 -0.0077 -0.1505 0.0005  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5525 0.1388 0.3242 -0.0235 -0.1953 0.0086  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5329 0.1527 0.3934 -0.0276 -0.2287 0.0184  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5478 0.1444 0.4279 -0.0404 -0.2686 0.0299  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5521 0.1431 0.3191 -0.0235 -0.1896 0.0071  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.6173 0.1633 0.2989 -0.0212 -0.1587 0.0005  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.6076 0.1596 0.2902 -0.0216 -0.1564 -0.0001 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.7127 0.1567 0.2888 -0.0361 -0.1733 0.0024  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4865 0.1627 0.4095 -0.0167 -0.2095 0.0154  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4505 0.1593 0.4656 -0.0180 -0.2286 0.0243  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5040 0.1580 0.5092 -0.0334 -0.2787 0.0386  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5716 0.1765 0.4998 -0.0387 -0.2844 0.0364  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3946 0.1573 0.4549 -0.0054 -0.1958 0.0174  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4972 0.1581 0.5838 -0.0412 -0.3126 0.0547  24  THR   A N   
135  C CA  . THR   A 18  ? 0.5465 0.1570 0.6437 -0.0596 -0.3710 0.0751  24  THR   A CA  
136  C C   . THR   A 18  ? 0.5484 0.1861 0.7179 -0.0550 -0.3733 0.0814  24  THR   A C   
137  O O   . THR   A 18  ? 0.5101 0.2056 0.7238 -0.0378 -0.3282 0.0697  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5450 0.1537 0.7164 -0.0707 -0.4085 0.0951  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5229 0.2004 0.8219 -0.0575 -0.3827 0.0983  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5575 0.1454 0.6722 -0.0749 -0.4068 0.0902  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5803 0.1734 0.7669 -0.0726 -0.4294 0.1025  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5660 0.1852 0.8331 -0.0683 -0.4334 0.1112  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4874 0.1756 0.8954 -0.0550 -0.4070 0.1172  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4672 0.1984 0.9217 -0.0405 -0.3694 0.1091  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6345 0.1917 0.9061 -0.0926 -0.5054 0.1376  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7864 0.2661 0.9197 -0.1072 -0.5266 0.1315  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.8513 0.3387 0.9441 -0.0963 -0.4945 0.1158  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.8933 0.2795 0.9250 -0.1345 -0.5784 0.1419  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.9340 0.3333 0.9028 -0.1154 -0.5221 0.1155  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.9746 0.3062 0.8947 -0.1397 -0.5717 0.1300  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4595 0.1528 0.9313 -0.0605 -0.4225 0.1312  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4057 0.1537 1.0114 -0.0489 -0.3906 0.1377  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3614 0.1574 0.9464 -0.0293 -0.3181 0.1096  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3293 0.1615 0.9919 -0.0183 -0.2792 0.1076  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4461 0.1857 1.1083 -0.0587 -0.4172 0.1561  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5067 0.2928 1.3115 -0.0480 -0.3809 0.1651  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5136 0.3096 1.4399 -0.0484 -0.3898 0.1873  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5166 0.3270 1.3110 -0.0390 -0.3370 0.1491  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3652 0.1563 0.8461 -0.0266 -0.2998 0.0898  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3242 0.1544 0.7746 -0.0122 -0.2400 0.0661  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2960 0.1440 0.7386 -0.0037 -0.2152 0.0569  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2680 0.1491 0.7516 0.0050  -0.1726 0.0491  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3542 0.1683 0.6942 -0.0127 -0.2351 0.0517  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3672 0.1757 0.7087 -0.0172 -0.2415 0.0543  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3208 0.1561 0.7454 -0.0146 -0.2252 0.0588  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4483 0.2210 0.7085 -0.0238 -0.2606 0.0523  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3223 0.1420 0.7090 -0.0078 -0.2411 0.0584  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3162 0.1519 0.6949 0.0000  -0.2200 0.0507  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3159 0.1681 0.8031 0.0019  -0.2209 0.0638  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3081 0.1864 0.8121 0.0108  -0.1865 0.0555  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3335 0.1263 0.6209 -0.0060 -0.2457 0.0493  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3411 0.1312 0.5348 -0.0006 -0.2179 0.0329  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3844 0.1355 0.4996 -0.0067 -0.2274 0.0302  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3010 0.1270 0.4782 0.0110  -0.1755 0.0201  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3899 0.1530 0.4501 0.0022  -0.1904 0.0172  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3435 0.1537 0.4424 0.0123  -0.1616 0.0122  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2821 0.1471 0.5027 0.0189  -0.1491 0.0164  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3327 0.1704 0.4083 0.0212  -0.1258 0.0039  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2798 0.1679 0.4643 0.0258  -0.1167 0.0068  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2987 0.1758 0.4177 0.0268  -0.1070 0.0022  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3119 0.1468 0.8766 -0.0074 -0.2602 0.0863  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2983 0.1472 0.9854 -0.0056 -0.2608 0.1036  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2820 0.1654 1.0509 0.0047  -0.2050 0.0995  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2702 0.1670 1.1302 0.0103  -0.1820 0.1073  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2979 0.1145 1.0499 -0.0211 -0.3252 0.1343  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2657 0.1566 1.0016 0.0058  -0.1819 0.0880  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2354 0.1467 1.0208 0.0125  -0.1258 0.0804  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2210 0.1444 0.9020 0.0167  -0.0858 0.0535  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2156 0.1438 0.8890 0.0167  -0.0566 0.0452  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2577 0.1631 1.1043 0.0072  -0.1394 0.0947  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3024 0.1979 1.2746 0.0017  -0.1772 0.1267  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2861 0.1904 1.3606 0.0074  -0.1489 0.1368  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3369 0.2089 1.3029 -0.0111 -0.2421 0.1450  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2088 0.1352 0.8152 0.0191  -0.0867 0.0425  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2079 0.1455 0.7230 0.0210  -0.0580 0.0227  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2192 0.1651 0.7480 0.0219  -0.0033 0.0124  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2339 0.1777 0.8191 0.0242  0.0191  0.0158  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2033 0.1419 0.6619 0.0236  -0.0696 0.0185  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2275 0.1790 0.6037 0.0247  -0.0456 0.0039  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2475 0.1943 0.5667 0.0223  -0.0561 0.0002  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2308 0.1844 0.5711 0.0280  -0.0525 0.0027  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2073 0.1555 0.6808 0.0182  0.0190  0.0005  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2043 0.1463 0.6603 0.0135  0.0683  -0.0107 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2227 0.1727 0.5858 0.0097  0.0693  -0.0203 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2571 0.2020 0.5993 0.0062  0.0915  -0.0248 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2138 0.1461 0.6763 0.0084  0.0891  -0.0142 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2438 0.1579 0.6508 -0.0015 0.1344  -0.0276 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2067 0.1304 0.7759 0.0116  0.0957  -0.0017 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1984 0.1589 0.5118 0.0100  0.0434  -0.0207 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1971 0.1674 0.4411 0.0068  0.0415  -0.0243 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1864 0.1638 0.3999 0.0118  0.0114  -0.0206 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1835 0.1545 0.4058 0.0132  -0.0025 -0.0189 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2093 0.1709 0.4132 -0.0056 0.0678  -0.0311 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2237 0.1952 0.3662 -0.0122 0.0596  -0.0297 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2613 0.2349 0.3715 -0.0191 0.0620  -0.0270 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2197 0.1999 0.3352 -0.0133 0.0463  -0.0276 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2659 0.2505 0.3386 -0.0249 0.0490  -0.0208 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2403 0.2293 0.3164 -0.0206 0.0411  -0.0215 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2205 0.2014 0.3458 -0.0087 0.0369  -0.0283 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2344 0.2328 0.2870 -0.0237 0.0305  -0.0157 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2230 0.2113 0.3155 -0.0115 0.0292  -0.0255 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2204 0.2189 0.2817 -0.0174 0.0257  -0.0185 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1783 0.1641 0.3565 0.0141  0.0043  -0.0184 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1794 0.1632 0.3235 0.0184  -0.0126 -0.0150 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1680 0.1662 0.2799 0.0168  -0.0044 -0.0114 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1728 0.1803 0.2870 0.0138  0.0040  -0.0099 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2165 0.1811 0.3643 0.0245  -0.0359 -0.0114 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2102 0.1765 0.3758 0.0274  -0.0373 -0.0094 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2700 0.2437 0.4041 0.0306  -0.0307 -0.0073 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2888 0.2734 0.4383 0.0314  -0.0237 -0.0066 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2610 0.2280 0.3596 0.0326  -0.0302 -0.0052 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1533 0.1512 0.2402 0.0185  -0.0074 -0.0078 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1515 0.1637 0.2239 0.0172  -0.0012 0.0011  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1709 0.1696 0.2257 0.0258  -0.0020 0.0059  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1929 0.1844 0.2361 0.0257  -0.0018 0.0053  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1778 0.2025 0.2435 0.0047  0.0047  0.0038  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2379 0.2782 0.3011 -0.0005 0.0041  0.0186  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2333 0.2764 0.3041 0.0090  0.0052  0.0271  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2680 0.3123 0.3213 -0.0159 0.0028  0.0233  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1633 0.1527 0.2132 0.0327  0.0009  0.0104  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1991 0.1620 0.2250 0.0400  0.0093  0.0145  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2005 0.1629 0.2259 0.0400  0.0094  0.0145  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2011 0.1792 0.2362 0.0397  0.0229  0.0257  36  SER   A C   
244  O O   . SER   A 30  ? 0.2256 0.1801 0.2417 0.0439  0.0323  0.0268  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2371 0.1880 0.2598 0.0458  0.0166  0.0185  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2441 0.1920 0.2641 0.0462  0.0176  0.0186  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2831 0.1884 0.2686 0.0512  0.0281  0.0187  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2882 0.2163 0.2985 0.0461  0.0033  0.0108  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1720 0.1852 0.2364 0.0331  0.0226  0.0362  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1673 0.1962 0.2521 0.0304  0.0294  0.0523  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1764 0.2048 0.2506 0.0256  0.0249  0.0479  37  SER   A C   
252  O O   . SER   A 31  ? 0.1963 0.2304 0.2866 0.0257  0.0318  0.0608  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1946 0.2542 0.3089 0.0192  0.0209  0.0680  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2474 0.3151 0.3477 0.0041  0.0063  0.0615  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1506 0.1720 0.2057 0.0217  0.0152  0.0320  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1534 0.1724 0.1986 0.0173  0.0119  0.0263  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1788 0.1671 0.2006 0.0254  0.0115  0.0154  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1829 0.1669 0.1972 0.0234  0.0095  0.0115  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1544 0.1828 0.1983 0.0043  0.0046  0.0180  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1505 0.1954 0.1993 -0.0100 0.0009  0.0294  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1400 0.1768 0.1710 -0.0253 0.0010  0.0197  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1592 0.1884 0.1787 -0.0303 0.0029  0.0133  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1737 0.1894 0.1702 -0.0476 0.0064  0.0087  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2113 0.2147 0.1865 -0.0636 0.0075  0.0106  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2183 0.2266 0.2061 -0.0511 0.0098  0.0029  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2042 0.1669 0.2106 0.0319  0.0098  0.0110  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2171 0.1396 0.1925 0.0341  0.0002  0.0027  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2117 0.1416 0.2036 0.0279  -0.0169 -0.0053 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2355 0.1440 0.2130 0.0264  -0.0262 -0.0084 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2457 0.1380 0.1897 0.0377  0.0119  0.0052  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3046 0.1433 0.2025 0.0357  -0.0017 -0.0015 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3341 0.1442 0.2127 0.0339  -0.0141 -0.0039 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3317 0.1542 0.2113 0.0339  -0.0031 -0.0033 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1836 0.1407 0.2073 0.0235  -0.0174 -0.0074 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1639 0.1235 0.2134 0.0185  -0.0245 -0.0135 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1675 0.1237 0.2453 0.0188  -0.0322 -0.0147 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1828 0.1470 0.2631 0.0205  -0.0276 -0.0131 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1663 0.1492 0.2275 0.0106  -0.0100 -0.0155 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1806 0.1692 0.2252 0.0070  -0.0051 -0.0139 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1773 0.1767 0.2241 -0.0056 0.0065  -0.0164 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1783 0.1507 0.2213 0.0096  -0.0134 -0.0174 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1705 0.1158 0.2779 0.0168  -0.0443 -0.0155 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1853 0.1280 0.3376 0.0167  -0.0515 -0.0134 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1825 0.1277 0.3847 0.0129  -0.0467 -0.0135 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2057 0.1431 0.4028 0.0111  -0.0551 -0.0126 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2149 0.1272 0.3573 0.0176  -0.0819 -0.0070 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2080 0.1171 0.4087 0.0164  -0.0958 -0.0008 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2388 0.1245 0.4146 0.0167  -0.1163 0.0035  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2221 0.1162 0.4738 0.0109  -0.1198 0.0086  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1725 0.1265 0.4213 0.0117  -0.0268 -0.0147 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1782 0.1293 0.4853 0.0088  -0.0127 -0.0135 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1802 0.1251 0.5605 0.0113  -0.0222 -0.0034 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1667 0.1150 0.5515 0.0136  -0.0159 -0.0038 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1923 0.1463 0.4887 0.0030  0.0289  -0.0231 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1861 0.1285 0.5479 0.0006  0.0534  -0.0218 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2049 0.1649 0.4346 -0.0017 0.0318  -0.0292 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1869 0.1225 0.6271 0.0100  -0.0414 0.0080  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1997 0.1290 0.7284 0.0107  -0.0552 0.0233  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2042 0.1334 0.8213 0.0101  -0.0260 0.0292  43  SER   A C   
300  O O   . SER   A 37  ? 0.1873 0.1169 0.7921 0.0080  -0.0082 0.0231  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2174 0.1275 0.7464 0.0063  -0.1128 0.0384  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2316 0.1309 0.7612 0.0010  -0.1334 0.0445  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2176 0.1442 0.9305 0.0122  -0.0186 0.0425  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2334 0.1551 1.0477 0.0128  0.0164  0.0514  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2628 0.1808 1.1673 0.0092  -0.0263 0.0768  44  SER   A C   
306  O O   . SER   A 38  ? 0.2762 0.1888 1.1869 0.0050  -0.0840 0.0922  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2235 0.1404 1.1045 0.0172  0.0556  0.0544  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2530 0.1735 1.1799 0.0186  0.0123  0.0714  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2831 0.1983 1.2505 0.0086  -0.0002 0.0820  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3096 0.2216 1.3697 0.0036  -0.0413 0.1090  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3338 0.2431 1.5484 0.0070  -0.0034 0.1290  45  THR   A C   
312  O O   . THR   A 39  ? 0.3496 0.2525 1.5731 0.0123  0.0681  0.1145  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3380 0.2498 1.3436 -0.0002 -0.0464 0.1007  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3438 0.2549 1.3616 0.0034  0.0221  0.0866  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3764 0.2881 1.2358 -0.0023 -0.0721 0.0812  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3338 0.2415 1.6683 0.0019  -0.0495 0.1635  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3170 0.2228 1.8241 0.0051  -0.0162 0.1896  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3251 0.2284 1.8674 0.0051  0.0188  0.1890  46  THR   A C   
319  O O   . THR   A 40  ? 0.3190 0.2161 1.9926 0.0098  0.0701  0.2040  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3040 0.2090 1.9349 -0.0031 -0.0889 0.2327  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3590 0.2576 1.9455 -0.0161 -0.1614 0.2439  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3045 0.2082 1.9234 -0.0036 -0.1194 0.2373  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3372 0.2430 1.7745 -0.0002 -0.0085 0.1749  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3146 0.2186 1.7767 -0.0007 0.0211  0.1733  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3343 0.2332 1.6619 0.0025  0.0797  0.1331  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3664 0.2680 1.5667 0.0026  0.0727  0.1098  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3268 0.2328 1.7812 -0.0109 -0.0545 0.1910  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3196 0.2078 1.6795 0.0038  0.1378  0.1270  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3631 0.2369 1.6033 0.0028  0.1947  0.0924  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3717 0.2572 1.5001 -0.0020 0.1581  0.0783  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3576 0.2491 1.5343 -0.0041 0.1347  0.0923  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3840 0.2292 1.7075 0.0041  0.2783  0.0930  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4891 0.3084 1.6985 -0.0017 0.3339  0.0620  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6208 0.4072 1.7295 -0.0059 0.3880  0.0359  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6480 0.4312 1.7765 -0.0025 0.3936  0.0391  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6786 0.4356 1.6746 -0.0156 0.4270  0.0106  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3831 0.2699 1.3700 -0.0039 0.1576  0.0523  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3955 0.2918 1.2713 -0.0075 0.1300  0.0377  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3818 0.2631 1.2102 -0.0121 0.1804  0.0195  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3956 0.2509 1.2037 -0.0156 0.2406  0.0056  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3519 0.2430 1.1493 -0.0141 0.1554  0.0185  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3486 0.2248 1.1073 -0.0195 0.1980  0.0036  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3469 0.2302 0.9781 -0.0241 0.1818  -0.0145 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3672 0.2431 0.9761 -0.0287 0.2001  -0.0218 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3459 0.2230 1.2056 -0.0182 0.1992  0.0204  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4178 0.2696 1.4238 -0.0158 0.2637  0.0349  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3233 0.2190 0.8774 -0.0233 0.1518  -0.0206 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3405 0.2429 0.7888 -0.0275 0.1399  -0.0340 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3619 0.2409 0.7432 -0.0384 0.1835  -0.0503 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3927 0.2534 0.7799 -0.0412 0.2112  -0.0532 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3623 0.2833 0.7602 -0.0226 0.0935  -0.0315 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3944 0.3238 0.8215 -0.0170 0.0458  -0.0173 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4144 0.3435 0.8602 -0.0179 0.0388  -0.0134 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3969 0.3278 0.8211 -0.0136 0.0144  -0.0101 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3572 0.2317 0.6717 -0.0464 0.1876  -0.0595 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3823 0.2264 0.6172 -0.0623 0.2191  -0.0727 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3664 0.2307 0.5314 -0.0639 0.1838  -0.0726 52  THR   A C   
358  O O   . THR   A 46  ? 0.3636 0.2564 0.5222 -0.0563 0.1487  -0.0674 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4299 0.2548 0.6383 -0.0724 0.2401  -0.0798 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4488 0.2452 0.7228 -0.0727 0.2858  -0.0801 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4680 0.2607 0.5730 -0.0931 0.2537  -0.0904 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3543 0.2018 0.4731 -0.0731 0.1938  -0.0764 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3416 0.2077 0.4036 -0.0759 0.1620  -0.0730 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3619 0.2027 0.3466 -0.0971 0.1686  -0.0774 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4094 0.2012 0.3577 -0.1150 0.2047  -0.0860 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3464 0.2101 0.4022 -0.0757 0.1619  -0.0714 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3390 0.2202 0.4732 -0.0578 0.1563  -0.0660 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3582 0.2435 0.3659 -0.0781 0.1287  -0.0645 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3234 0.2408 0.4842 -0.0418 0.1131  -0.0567 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3317 0.1981 0.2910 -0.0968 0.1364  -0.0705 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3553 0.2017 0.2482 -0.1182 0.1315  -0.0693 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3950 0.2156 0.2309 -0.1376 0.1283  -0.0658 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3682 0.2102 0.2208 -0.1286 0.1142  -0.0598 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3239 0.2082 0.2222 -0.1103 0.0976  -0.0586 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4673 0.2360 0.2294 -0.1670 0.1391  -0.0688 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.5324 0.2640 0.2255 -0.1925 0.1306  -0.0632 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5747 0.2939 0.2145 -0.2163 0.0998  -0.0512 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.6528 0.3143 0.2275 -0.2419 0.1151  -0.0578 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5913 0.2496 0.2347 -0.2107 0.1778  -0.0781 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5534 0.2246 0.2675 -0.1864 0.2108  -0.0870 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5426 0.2619 0.3010 -0.1680 0.1856  -0.0781 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4990 0.2256 0.3259 -0.1480 0.2138  -0.0845 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4832 0.2517 0.3622 -0.1283 0.1956  -0.0783 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4511 0.2560 0.3206 -0.1249 0.1556  -0.0672 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4603 0.2323 0.4060 -0.1126 0.2180  -0.0814 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.5331 0.3044 0.2063 -0.2073 0.0582  -0.0324 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.5505 0.3235 0.2029 -0.2240 0.0267  -0.0170 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5263 0.3493 0.2227 -0.2162 -0.0140 0.0084  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4941 0.3480 0.2304 -0.1974 -0.0147 0.0111  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.5372 0.3319 0.2256 -0.2069 0.0391  -0.0257 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4422 0.3124 0.2280 -0.1628 0.0337  -0.0233 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5214 0.3516 0.2179 -0.2299 -0.0456 0.0283  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4906 0.3692 0.2477 -0.2198 -0.0772 0.0552  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4468 0.3634 0.2577 -0.2001 -0.0786 0.0602  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4400 0.3812 0.2924 -0.2016 -0.1047 0.0864  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5542 0.4086 0.2815 -0.2553 -0.1193 0.0839  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6712 0.4905 0.3552 -0.2871 -0.1435 0.0955  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.7058 0.5133 0.3714 -0.2834 -0.1220 0.0771  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7481 0.5484 0.4163 -0.3183 -0.1871 0.1248  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4087 0.3297 0.2261 -0.1807 -0.0493 0.0371  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3527 0.3045 0.2145 -0.1606 -0.0463 0.0386  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3017 0.2952 0.2270 -0.1374 -0.0539 0.0557  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2849 0.2889 0.2255 -0.1244 -0.0479 0.0541  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3474 0.2977 0.2122 -0.1420 -0.0160 0.0129  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4011 0.3058 0.2115 -0.1639 0.0018  -0.0047 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2559 0.2685 0.2177 -0.1325 -0.0632 0.0720  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2248 0.2676 0.2471 -0.1088 -0.0591 0.0870  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1789 0.2300 0.2197 -0.0868 -0.0399 0.0781  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1745 0.2404 0.2604 -0.0712 -0.0331 0.0930  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2420 0.2985 0.3091 -0.1214 -0.0848 0.1227  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2877 0.3451 0.3609 -0.1311 -0.0996 0.1367  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3212 0.3951 0.4574 -0.1423 -0.1266 0.1772  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3688 0.4276 0.4892 -0.1743 -0.1626 0.1968  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3035 0.4026 0.5130 -0.1177 -0.1092 0.1926  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1857 0.2228 0.1925 -0.0875 -0.0293 0.0554  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1672 0.2074 0.1843 -0.0682 -0.0132 0.0453  60  THR   A CA  
417  C C   . THR   A 54  ? 0.1680 0.1944 0.1593 -0.0616 0.0001  0.0199  60  THR   A C   
418  O O   . THR   A 54  ? 0.1951 0.2072 0.1601 -0.0759 0.0012  0.0091  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2160 0.2560 0.2340 -0.0775 -0.0185 0.0500  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2822 0.3018 0.2572 -0.0980 -0.0210 0.0361  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2247 0.2772 0.2777 -0.0885 -0.0374 0.0796  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1500 0.1750 0.1499 -0.0417 0.0107  0.0127  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1644 0.1770 0.1536 -0.0360 0.0172  -0.0056 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1619 0.1650 0.1534 -0.0185 0.0210  -0.0081 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1826 0.1856 0.1782 -0.0116 0.0250  0.0007  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1487 0.1386 0.1373 -0.0136 0.0192  -0.0186 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1602 0.1285 0.1387 -0.0024 0.0161  -0.0205 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1876 0.1396 0.1593 0.0022  0.0083  -0.0221 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1899 0.1483 0.1781 -0.0028 0.0044  -0.0269 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1790 0.1423 0.1660 -0.0053 0.0127  -0.0279 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2053 0.1378 0.1760 0.0018  0.0014  -0.0276 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1875 0.1638 0.1768 -0.0098 0.0205  -0.0265 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2149 0.1384 0.1596 0.0105  0.0078  -0.0183 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2145 0.1139 0.1445 0.0122  -0.0031 -0.0195 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2660 0.1205 0.1636 0.0121  -0.0178 -0.0201 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2861 0.1213 0.1609 0.0138  -0.0130 -0.0191 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2142 0.1091 0.1316 0.0177  0.0086  -0.0135 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2689 0.1251 0.1489 0.0253  0.0245  -0.0081 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2779 0.1430 0.1679 0.0295  0.0436  -0.0012 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3360 0.1413 0.1704 0.0272  0.0237  -0.0089 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3354 0.1601 0.1969 0.0375  0.0675  0.0048  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3869 0.1440 0.1785 0.0330  0.0472  -0.0048 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3794 0.1455 0.1862 0.0389  0.0716  0.0016  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4438 0.1558 0.2119 0.0454  0.1030  0.0063  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2710 0.1041 0.1648 0.0084  -0.0384 -0.0202 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3279 0.1081 0.1843 0.0030  -0.0621 -0.0173 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3781 0.1049 0.1680 0.0045  -0.0564 -0.0155 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3766 0.1071 0.1682 0.0064  -0.0534 -0.0153 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3310 0.1122 0.2276 -0.0051 -0.0929 -0.0137 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4002 0.1192 0.2538 -0.0153 -0.1263 -0.0062 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4440 0.1408 0.2779 -0.0194 -0.1341 -0.0039 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4513 0.1257 0.2716 -0.0226 -0.1506 -0.0007 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5140 0.1442 0.2983 -0.0329 -0.1695 0.0050  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5235 0.1284 0.2914 -0.0372 -0.1873 0.0084  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5721 0.1529 0.3188 -0.0430 -0.1969 0.0115  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.6832 0.1860 0.3675 -0.0613 -0.2370 0.0222  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4465 0.1163 0.1730 0.0025  -0.0525 -0.0143 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.5249 0.1262 0.1748 0.0021  -0.0387 -0.0135 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.6140 0.1343 0.1934 -0.0142 -0.0739 -0.0104 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.6625 0.1441 0.2033 -0.0203 -0.0796 -0.0092 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5619 0.1506 0.1894 0.0119  0.0036  -0.0133 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.6578 0.1382 0.1781 0.0100  0.0327  -0.0128 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.6353 0.1304 0.2009 -0.0231 -0.1009 -0.0075 66  SER   A N   
464  C CA  . SER   A 60  ? 0.7145 0.1323 0.2196 -0.0434 -0.1458 -0.0004 66  SER   A CA  
465  C C   . SER   A 60  ? 0.8218 0.1328 0.2037 -0.0533 -0.1338 -0.0015 66  SER   A C   
466  O O   . SER   A 60  ? 0.8923 0.1422 0.2222 -0.0710 -0.1676 0.0048  66  SER   A O   
467  C CB  . SER   A 60  ? 0.7540 0.1663 0.2719 -0.0510 -0.1754 0.0045  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.8654 0.2614 0.3470 -0.0436 -0.1435 -0.0014 66  SER   A OG  
469  N N   . SER   A 61  ? 0.8431 0.1285 0.1809 -0.0428 -0.0832 -0.0081 67  SER   A N   
470  C CA  . SER   A 61  ? 0.9366 0.1101 0.1529 -0.0513 -0.0578 -0.0103 67  SER   A CA  
471  C C   . SER   A 61  ? 0.9506 0.1096 0.1484 -0.0498 -0.0425 -0.0111 67  SER   A C   
472  O O   . SER   A 61  ? 1.0660 0.1208 0.1547 -0.0592 -0.0214 -0.0128 67  SER   A O   
473  C CB  . SER   A 61  ? 0.9664 0.1178 0.1569 -0.0383 0.0010  -0.0151 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.9158 0.1543 0.1963 -0.0151 0.0435  -0.0157 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.8560 0.1083 0.1502 -0.0394 -0.0499 -0.0103 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.8532 0.1004 0.1400 -0.0382 -0.0407 -0.0104 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.8466 0.1314 0.1840 -0.0482 -0.0935 -0.0047 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.8651 0.1530 0.2053 -0.0479 -0.0916 -0.0042 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.8037 0.1272 0.1641 -0.0151 0.0096  -0.0134 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.8458 0.1255 0.1665 -0.0043 0.0692  -0.0144 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.9662 0.1346 0.1783 -0.0117 0.0964  -0.0157 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 1.0401 0.1658 0.2277 0.0002  0.1623  -0.0151 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.1551 0.1957 0.2630 -0.0063 0.1831  -0.0170 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.2179 0.2013 0.2522 -0.0269 0.1376  -0.0197 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.2038 0.2120 0.3079 0.0069  0.2499  -0.0146 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.8215 0.1442 0.2159 -0.0549 -0.1363 0.0008  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.7970 0.1674 0.2688 -0.0615 -0.1798 0.0089  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.7297 0.1809 0.2772 -0.0456 -0.1519 0.0034  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.7294 0.1860 0.2973 -0.0509 -0.1700 0.0079  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.8853 0.1712 0.2920 -0.0864 -0.2302 0.0211  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 1.0102 0.2250 0.3619 -0.1073 -0.2736 0.0309  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.1450 0.2686 0.4240 -0.1355 -0.3260 0.0455  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.2991 0.3383 0.5117 -0.1618 -0.3769 0.0584  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.4580 0.3786 0.5560 -0.1929 -0.4204 0.0703  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.5128 0.3874 0.5525 -0.2002 -0.4174 0.0704  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.5300 0.3710 0.5646 -0.2190 -0.4687 0.0827  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.6626 0.1709 0.2469 -0.0274 -0.1079 -0.0051 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.5899 0.1636 0.2325 -0.0155 -0.0826 -0.0093 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4943 0.1473 0.2110 -0.0042 -0.0627 -0.0133 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4839 0.1350 0.1925 -0.0010 -0.0539 -0.0140 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6617 0.2032 0.2522 -0.0073 -0.0421 -0.0122 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.8083 0.2967 0.3461 -0.0141 -0.0466 -0.0106 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.9082 0.3922 0.4313 -0.0008 0.0039  -0.0129 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.9977 0.4384 0.4776 -0.0043 0.0086  -0.0123 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.1110 0.4348 0.4720 -0.0172 0.0091  -0.0114 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.4232 0.1361 0.2014 0.0001  -0.0547 -0.0157 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3544 0.1307 0.1865 0.0069  -0.0346 -0.0189 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3696 0.1575 0.1948 0.0154  -0.0025 -0.0179 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3997 0.1715 0.2076 0.0168  0.0047  -0.0172 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3075 0.1327 0.2049 0.0031  -0.0418 -0.0216 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3108 0.1317 0.2393 -0.0040 -0.0682 -0.0189 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3117 0.1596 0.2787 -0.0043 -0.0660 -0.0205 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3261 0.1182 0.2590 -0.0116 -0.0973 -0.0123 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2966 0.1324 0.2961 -0.0106 -0.0914 -0.0143 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3410 0.1440 0.3239 -0.0160 -0.1137 -0.0078 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3240 0.1405 0.1695 0.0206  0.0156  -0.0153 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3117 0.1436 0.1698 0.0274  0.0423  -0.0087 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2620 0.1521 0.1727 0.0239  0.0425  -0.0057 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2351 0.1432 0.1601 0.0205  0.0353  -0.0067 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3548 0.1526 0.1871 0.0353  0.0664  -0.0017 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4332 0.1553 0.1948 0.0362  0.0744  -0.0040 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4743 0.1690 0.2151 0.0394  0.0921  -0.0021 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.4978 0.1676 0.2062 0.0319  0.0654  -0.0073 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5586 0.1698 0.2193 0.0370  0.1011  -0.0045 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5789 0.1633 0.2045 0.0277  0.0709  -0.0090 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6092 0.1621 0.2076 0.0296  0.0889  -0.0081 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.7349 0.1890 0.2362 0.0224  0.0965  -0.0100 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2571 0.1718 0.1923 0.0228  0.0499  -0.0009 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2263 0.1834 0.1991 0.0150  0.0473  0.0056  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2338 0.1961 0.2261 0.0197  0.0594  0.0213  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2746 0.2137 0.2642 0.0305  0.0797  0.0295  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2377 0.2086 0.2251 0.0114  0.0494  0.0085  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2760 0.2136 0.2414 0.0228  0.0631  0.0088  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2869 0.1841 0.2115 0.0277  0.0615  0.0015  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2021 0.1898 0.2152 0.0113  0.0497  0.0269  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2061 0.2017 0.2488 0.0146  0.0581  0.0452  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1685 0.1962 0.2418 -0.0015 0.0402  0.0582  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1788 0.2139 0.2338 -0.0157 0.0242  0.0479  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2499 0.2276 0.2750 0.0216  0.0634  0.0410  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3122 0.2431 0.3022 0.0352  0.0842  0.0362  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2560 0.2399 0.2614 0.0131  0.0447  0.0255  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1486 0.1886 0.2675 -0.0008 0.0437  0.0825  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1543 0.2174 0.3027 -0.0182 0.0213  0.1009  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1804 0.2418 0.3366 -0.0115 0.0276  0.1048  75  SER   A C   
545  O O   . SER   A 69  ? 0.2201 0.2646 0.3829 0.0070  0.0537  0.1057  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1651 0.2444 0.3756 -0.0230 0.0163  0.1318  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2547 0.3343 0.4570 -0.0287 0.0111  0.1278  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1325 0.2024 0.2760 -0.0264 0.0073  0.1037  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1361 0.2051 0.2849 -0.0200 0.0126  0.1057  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1491 0.2348 0.3237 -0.0384 -0.0113 0.1268  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1754 0.2646 0.3397 -0.0612 -0.0368 0.1331  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1502 0.2028 0.2474 -0.0147 0.0171  0.0772  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1452 0.1961 0.2057 -0.0306 0.0023  0.0601  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1417 0.1843 0.1817 -0.0310 0.0052  0.0456  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1503 0.2026 0.1967 -0.0454 -0.0101 0.0587  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1629 0.1980 0.1744 -0.0444 0.0001  0.0300  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1785 0.2183 0.1887 -0.0600 -0.0140 0.0425  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1747 0.2059 0.1704 -0.0591 -0.0069 0.0284  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1338 0.2253 0.3421 -0.0309 -0.0045 0.1411  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1402 0.2474 0.3816 -0.0497 -0.0310 0.1667  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1656 0.2649 0.3515 -0.0674 -0.0506 0.1515  77  SER   A C   
562  O O   . SER   A 71  ? 0.1689 0.2543 0.3034 -0.0615 -0.0392 0.1219  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1462 0.2630 0.4544 -0.0358 -0.0149 0.1910  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1793 0.2828 0.4547 -0.0204 0.0062  0.1700  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1913 0.2950 0.3886 -0.0904 -0.0800 0.1732  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2306 0.3181 0.3711 -0.1086 -0.0945 0.1605  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2264 0.3194 0.3737 -0.0907 -0.0766 0.1518  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2077 0.3162 0.4106 -0.0733 -0.0635 0.1672  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2857 0.3668 0.4295 -0.1427 -0.1357 0.1904  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3804 0.4527 0.5190 -0.1619 -0.1566 0.2019  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.4809 0.5363 0.6131 -0.2015 -0.2054 0.2341  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.5902 0.5990 0.6269 -0.2331 -0.2209 0.2184  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.6615 0.6396 0.6169 -0.2342 -0.1980 0.1832  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2384 0.3151 0.3315 -0.0938 -0.0717 0.1270  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2324 0.3138 0.3331 -0.0771 -0.0568 0.1191  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2236 0.3203 0.3705 -0.0820 -0.0701 0.1482  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2289 0.3227 0.3742 -0.1082 -0.0998 0.1685  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2799 0.3401 0.3228 -0.0855 -0.0536 0.0934  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3221 0.3607 0.3218 -0.1102 -0.0655 0.0898  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2724 0.3220 0.2995 -0.1121 -0.0752 0.1061  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2062 0.3141 0.3951 -0.0587 -0.0488 0.1531  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2054 0.3299 0.4543 -0.0601 -0.0557 0.1837  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1915 0.3150 0.4560 -0.0357 -0.0262 0.1764  80  SER   A C   
584  O O   . SER   A 74  ? 0.1782 0.2849 0.4024 -0.0197 -0.0048 0.1486  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2321 0.3712 0.5508 -0.0629 -0.0621 0.2169  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3063 0.4407 0.6448 -0.0371 -0.0254 0.2097  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1749 0.3125 0.4964 -0.0355 -0.0279 0.2029  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1818 0.3147 0.5229 -0.0145 0.0020  0.2005  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1878 0.3132 0.5782 0.0043  0.0364  0.2134  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1855 0.3277 0.6526 -0.0002 0.0327  0.2476  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1643 0.3158 0.5554 -0.0240 -0.0137 0.2278  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2251 0.3738 0.5658 -0.0344 -0.0309 0.2118  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2284 0.3951 0.6211 -0.0485 -0.0532 0.2443  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2574 0.3902 0.5642 -0.0132 -0.0018 0.1843  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2036 0.2984 0.5521 0.0235  0.0695  0.1891  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2253 0.2961 0.5984 0.0405  0.1096  0.1959  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2775 0.3114 0.6297 0.0577  0.1480  0.1858  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2901 0.3054 0.5747 0.0589  0.1425  0.1593  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2555 0.3083 0.5750 0.0418  0.1103  0.1744  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2470 0.3312 0.5973 0.0250  0.0790  0.1898  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2858 0.2948 0.5970 0.0599  0.1567  0.1714  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2782 0.3526 0.5772 0.0224  0.0719  0.1687  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2917 0.3113 0.7055 0.0699  0.1881  0.2090  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3637 0.3360 0.7495 0.0845  0.2305  0.1996  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4113 0.3213 0.6988 0.0916  0.2525  0.1686  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4422 0.3371 0.7215 0.0936  0.2634  0.1676  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3806 0.3433 0.8585 0.0960  0.2776  0.2327  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4508 0.3646 0.9054 0.1082  0.3222  0.2263  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4678 0.4067 0.9544 0.1059  0.3105  0.2354  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5230 0.3585 0.9174 0.1202  0.3769  0.2116  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5145 0.4055 0.9774 0.1165  0.3527  0.2291  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5732 0.3523 0.9352 0.1286  0.4199  0.2054  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5600 0.3695 0.9603 0.1274  0.4082  0.2145  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.4269 0.2999 0.6381 0.0930  0.2533  0.1445  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4734 0.2790 0.5835 0.0948  0.2648  0.1175  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5343 0.2709 0.6036 0.1025  0.3077  0.1137  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5144 0.2610 0.5927 0.1024  0.3027  0.1145  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4756 0.2944 0.5254 0.0841  0.2152  0.0926  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5332 0.2799 0.4848 0.0827  0.2192  0.0701  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4226 0.3032 0.5106 0.0754  0.1792  0.0964  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6102 0.2707 0.6293 0.1078  0.3522  0.1094  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6798 0.2516 0.6411 0.1127  0.4027  0.1045  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.7254 0.2605 0.5937 0.1034  0.3734  0.0810  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.7395 0.2889 0.5631 0.0934  0.3232  0.0646  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.7808 0.2635 0.6742 0.1147  0.4480  0.0983  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8402 0.3571 0.8193 0.1229  0.4709  0.1193  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9940 0.4325 0.9792 0.1340  0.5529  0.1320  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0609 0.4344 1.0141 0.1373  0.5974  0.1310  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.0241 0.4623 1.0462 0.1392  0.5757  0.1431  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7560 0.2341 0.5926 0.1058  0.4077  0.0802  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.8016 0.2377 0.5502 0.0956  0.3798  0.0604  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.8701 0.2260 0.4963 0.0821  0.3605  0.0396  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.9242 0.2181 0.5048 0.0818  0.3931  0.0384  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.8337 0.2088 0.5619 0.0997  0.4277  0.0637  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.8663 0.2250 0.4466 0.0701  0.3057  0.0257  87  SER   A N   
636  C CA  . SER   A 81  ? 0.9248 0.2089 0.3960 0.0536  0.2754  0.0102  87  SER   A CA  
637  C C   . SER   A 81  ? 0.9821 0.2220 0.3888 0.0406  0.2430  0.0008  87  SER   A C   
638  O O   . SER   A 81  ? 0.9545 0.2265 0.4037 0.0466  0.2487  0.0047  87  SER   A O   
639  C CB  . SER   A 81  ? 0.8891 0.2431 0.3991 0.0506  0.2257  0.0080  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.8637 0.2850 0.4164 0.0469  0.1735  0.0052  87  SER   A OG  
641  N N   . GLU   A 82  ? 1.0473 0.2138 0.3556 0.0214  0.2055  -0.0094 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.0834 0.2078 0.3347 0.0053  0.1623  -0.0152 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.9930 0.2273 0.3423 0.0094  0.1110  -0.0126 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.0176 0.2399 0.3535 0.0019  0.0841  -0.0140 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.2299 0.2436 0.3550 -0.0201 0.1282  -0.0217 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.3166 0.3481 0.4489 -0.0221 0.1106  -0.0213 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.5566 0.4782 0.5670 -0.0494 0.0723  -0.0246 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.6530 0.4598 0.5513 -0.0591 0.1101  -0.0287 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.5998 0.5474 0.6298 -0.0620 0.0050  -0.0211 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8874 0.2243 0.3340 0.0207  0.1008  -0.0085 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7907 0.2216 0.3239 0.0237  0.0608  -0.0068 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6917 0.2056 0.3154 0.0395  0.0859  0.0002  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6643 0.2341 0.3402 0.0405  0.0609  0.0008  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7526 0.2329 0.3251 0.0215  0.0299  -0.0072 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.8200 0.2218 0.3108 0.0059  0.0066  -0.0107 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.8577 0.2226 0.3173 -0.0111 -0.0454 -0.0105 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.8591 0.2228 0.3086 0.0068  0.0341  -0.0116 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.9234 0.2117 0.3070 -0.0290 -0.0734 -0.0101 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.9408 0.2228 0.3047 -0.0098 0.0127  -0.0142 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.9835 0.2267 0.3119 -0.0288 -0.0435 -0.0129 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.0753 0.2335 0.3175 -0.0486 -0.0707 -0.0122 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6568 0.1790 0.3052 0.0508  0.1334  0.0080  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5765 0.1761 0.3163 0.0628  0.1511  0.0197  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.6185 0.1855 0.3642 0.0724  0.2088  0.0306  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6705 0.1776 0.3726 0.0731  0.2411  0.0305  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.4905 0.1727 0.3053 0.0661  0.1394  0.0267  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4370 0.1567 0.2617 0.0583  0.0941  0.0181  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3951 0.1642 0.2598 0.0561  0.0678  0.0164  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4359 0.1430 0.2379 0.0539  0.0827  0.0130  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3694 0.1684 0.2512 0.0498  0.0356  0.0099  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3975 0.1410 0.2211 0.0477  0.0474  0.0073  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3689 0.1565 0.2336 0.0458  0.0261  0.0059  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3276 0.1427 0.2173 0.0400  -0.0015 0.0007  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.5895 0.1980 0.3994 0.0803  0.2252  0.0424  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.5972 0.1893 0.4448 0.0911  0.2826  0.0590  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5706 0.2223 0.4986 0.0965  0.2888  0.0757  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5383 0.2439 0.4858 0.0911  0.2483  0.0725  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.5713 0.2000 0.4736 0.0959  0.2870  0.0689  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5393 0.2360 0.4635 0.0892  0.2293  0.0619  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5462 0.2248 0.4109 0.0798  0.1931  0.0444  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5802 0.2207 0.5595 0.1064  0.3397  0.0953  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5418 0.2362 0.6067 0.1103  0.3440  0.1158  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4536 0.2451 0.6047 0.1058  0.3005  0.1304  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4476 0.2594 0.6253 0.1062  0.2958  0.1359  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5563 0.2166 0.6737 0.1220  0.4101  0.1381  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3939 0.2368 0.5697 0.0986  0.2644  0.1326  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3349 0.2521 0.5633 0.0890  0.2198  0.1421  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2933 0.2515 0.5547 0.0807  0.1948  0.1513  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3150 0.2477 0.5531 0.0838  0.2085  0.1459  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3559 0.2729 0.5196 0.0822  0.1851  0.1159  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3688 0.2794 0.4768 0.0755  0.1583  0.0946  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3936 0.2730 0.4325 0.0728  0.1400  0.0701  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3723 0.2711 0.3930 0.0642  0.1057  0.0564  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3689 0.2472 0.3584 0.0625  0.1021  0.0481  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3171 0.2132 0.2984 0.0550  0.0735  0.0369  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3971 0.2324 0.3637 0.0681  0.1303  0.0512  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2560 0.2701 0.5607 0.0681  0.1571  0.1640  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2501 0.2940 0.5651 0.0558  0.1278  0.1683  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2066 0.2470 0.4483 0.0484  0.1006  0.1379  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1874 0.2324 0.4051 0.0448  0.0859  0.1261  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2557 0.3470 0.6394 0.0406  0.0981  0.1978  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2797 0.3830 0.7607 0.0451  0.1179  0.2361  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2932 0.4097 0.8298 0.0409  0.1153  0.2596  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2973 0.4033 0.8262 0.0515  0.1350  0.2526  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2827 0.4132 0.9274 0.0441  0.1315  0.3003  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2860 0.4055 0.9209 0.0551  0.1532  0.2923  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2891 0.4210 0.9861 0.0516  0.1518  0.3172  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2948 0.4414 1.1133 0.0549  0.1694  0.3611  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1774 0.2067 0.3881 0.0474  0.0976  0.1260  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1722 0.2000 0.3286 0.0399  0.0736  0.1010  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1539 0.2155 0.3295 0.0229  0.0468  0.1100  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1533 0.2262 0.3633 0.0195  0.0471  0.1278  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1843 0.1728 0.2891 0.0473  0.0845  0.0817  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1995 0.1906 0.2674 0.0392  0.0595  0.0610  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2393 0.1878 0.2577 0.0447  0.0634  0.0444  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2593 0.1662 0.2460 0.0516  0.0766  0.0402  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2112 0.1631 0.2163 0.0392  0.0493  0.0346  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1269 0.1994 0.2808 0.0106  0.0251  0.0999  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1258 0.2148 0.2795 -0.0098 0.0014  0.1069  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1572 0.2343 0.2710 -0.0140 -0.0020 0.0865  96  SER   A C   
721  O O   . SER   A 90  ? 0.1683 0.2280 0.2580 -0.0018 0.0088  0.0670  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1439 0.2395 0.2888 -0.0233 -0.0142 0.1082  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1739 0.2552 0.2820 -0.0181 -0.0085 0.0826  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1542 0.2372 0.2636 -0.0325 -0.0183 0.0942  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1596 0.2306 0.2342 -0.0392 -0.0200 0.0770  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1525 0.2178 0.2303 -0.0234 -0.0062 0.0698  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1530 0.2057 0.2044 -0.0214 -0.0027 0.0505  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1712 0.2277 0.2120 -0.0418 -0.0162 0.0547  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2144 0.2667 0.2400 -0.0604 -0.0266 0.0603  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2741 0.3066 0.2613 -0.0848 -0.0345 0.0586  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2366 0.2953 0.2740 -0.0597 -0.0296 0.0682  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2906 0.3143 0.2625 -0.0994 -0.0430 0.0658  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2730 0.3160 0.2784 -0.0842 -0.0413 0.0720  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1573 0.2276 0.2692 -0.0124 0.0038  0.0864  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1577 0.2125 0.2656 0.0025  0.0216  0.0807  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1438 0.2089 0.2732 -0.0043 0.0173  0.0944  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1343 0.2178 0.3046 -0.0140 0.0069  0.1189  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1743 0.2149 0.3008 0.0195  0.0457  0.0894  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2118 0.2172 0.3152 0.0339  0.0697  0.0814  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2365 0.2159 0.2828 0.0350  0.0618  0.0555  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2498 0.2288 0.3648 0.0477  0.1009  0.0913  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1501 0.2024 0.2566 0.0001  0.0231  0.0812  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1473 0.2081 0.2733 -0.0055 0.0199  0.0929  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1726 0.2128 0.3007 0.0123  0.0458  0.0920  99  MET   A C   
745  O O   . MET   A 93  ? 0.2045 0.2181 0.2900 0.0213  0.0546  0.0717  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1481 0.2063 0.2364 -0.0179 0.0062  0.0750  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1681 0.2315 0.2396 -0.0384 -0.0129 0.0740  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2315 0.2795 0.2575 -0.0517 -0.0159 0.0512  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2278 0.2632 0.2430 -0.0312 -0.0001 0.0279  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1475 0.1937 0.3240 0.0163  0.0581  0.1149  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1720 0.1882 0.3443 0.0328  0.0900  0.1136  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1730 0.1920 0.3460 0.0300  0.0873  0.1133  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1510 0.1991 0.3558 0.0162  0.0653  0.1268  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1923 0.2027 0.4254 0.0441  0.1208  0.1401  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2373 0.2359 0.4713 0.0507  0.1344  0.1415  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2559 0.2420 0.5551 0.0631  0.1738  0.1680  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2905 0.2457 0.4435 0.0576  0.1437  0.1125  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1908 0.1733 0.3273 0.0418  0.1100  0.1004  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2034 0.1823 0.3395 0.0423  0.1140  0.1000  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2517 0.1832 0.3765 0.0584  0.1556  0.1023  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2799 0.1716 0.3729 0.0668  0.1780  0.0967  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2321 0.2062 0.3131 0.0358  0.0935  0.0748  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2541 0.1840 0.4025 0.0615  0.1687  0.1116  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3127 0.1874 0.4385 0.0753  0.2123  0.1113  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3688 0.2081 0.4089 0.0729  0.2020  0.0844  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3645 0.2292 0.4023 0.0657  0.1772  0.0774  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.3196 0.2070 0.5164 0.0802  0.2331  0.1353  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3695 0.1890 0.5300 0.0937  0.2835  0.1316  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2903 0.2116 0.5859 0.0809  0.2395  0.1681  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4184 0.1958 0.3886 0.0771  0.2192  0.0711  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4821 0.2183 0.3702 0.0717  0.2029  0.0494  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.5370 0.1954 0.3444 0.0721  0.2183  0.0394  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5403 0.1846 0.3549 0.0766  0.2387  0.0456  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5807 0.1834 0.3082 0.0654  0.2067  0.0251  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.6489 0.1649 0.2830 0.0598  0.2122  0.0159  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.6437 0.1749 0.2677 0.0516  0.1733  0.0085  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.6068 0.1924 0.2630 0.0457  0.1322  0.0039  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.7144 0.1570 0.2612 0.0509  0.2059  0.0066  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.8246 0.1593 0.2598 0.0408  0.2124  -0.0004 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.9093 0.1720 0.3035 0.0464  0.2682  0.0033  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.8864 0.1754 0.2505 0.0239  0.1685  -0.0086 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.9844 0.1541 0.2702 0.0313  0.2565  -0.0052 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.9886 0.1705 0.2532 0.0165  0.1934  -0.0113 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.6953 0.1702 0.2708 0.0505  0.1890  0.0073  105 SER   A N   
785  C CA  . SER   A 99  ? 0.7138 0.1901 0.2720 0.0423  0.1545  0.0012  105 SER   A CA  
786  C C   . SER   A 99  ? 0.8177 0.1997 0.2923 0.0387  0.1796  -0.0011 105 SER   A C   
787  O O   . SER   A 99  ? 0.8638 0.2139 0.3369 0.0482  0.2321  0.0054  105 SER   A O   
788  C CB  . SER   A 99  ? 0.6655 0.2347 0.3162 0.0483  0.1432  0.0067  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.6960 0.2706 0.3819 0.0591  0.1843  0.0179  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.8667 0.1949 0.2692 0.0234  0.1438  -0.0086 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.9662 0.1940 0.2739 0.0151  0.1608  -0.0117 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.9930 0.2296 0.2944 0.0034  0.1093  -0.0147 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.9448 0.2539 0.3089 0.0013  0.0638  -0.0143 106 GLU   A O   
794  C CB  . GLU   A 100 ? 1.0808 0.1828 0.2635 0.0020  0.1785  -0.0160 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.1412 0.2338 0.2951 -0.0120 0.1302  -0.0183 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.2648 0.2309 0.2925 -0.0259 0.1496  -0.0214 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.4013 0.2575 0.3115 -0.0478 0.1319  -0.0243 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.2343 0.2048 0.2755 -0.0167 0.1823  -0.0203 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 1.0657 0.2323 0.3014 -0.0034 0.1190  -0.0166 107 PRO   A N   
800  C CA  . PRO   A 101 ? 1.0751 0.2505 0.3106 -0.0150 0.0674  -0.0175 107 PRO   A CA  
801  C C   . PRO   A 101 ? 1.0784 0.2231 0.2755 -0.0354 0.0059  -0.0168 107 PRO   A C   
802  O O   . PRO   A 101 ? 1.1737 0.2265 0.2753 -0.0502 0.0028  -0.0177 107 PRO   A O   
803  C CB  . PRO   A 101 ? 1.1514 0.2399 0.3074 -0.0201 0.0952  -0.0196 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 1.2122 0.2088 0.2880 -0.0195 0.1527  -0.0215 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 1.1314 0.1990 0.2861 -0.0027 0.1777  -0.0177 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.9738 0.2015 0.2575 -0.0349 -0.0385 -0.0136 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.9370 0.1707 0.2359 -0.0497 -0.0977 -0.0083 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.8243 0.1649 0.2331 -0.0362 -0.0986 -0.0079 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.8020 0.1766 0.2635 -0.0431 -0.1408 -0.0025 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.7592 0.1493 0.2056 -0.0180 -0.0510 -0.0119 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.6662 0.1475 0.2034 -0.0077 -0.0491 -0.0119 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.5819 0.1507 0.2110 0.0001  -0.0545 -0.0117 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.5322 0.1657 0.2289 0.0036  -0.0598 -0.0121 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.6699 0.1631 0.2099 0.0048  -0.0031 -0.0128 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.7419 0.1654 0.2104 -0.0029 -0.0012 -0.0135 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.7361 0.1377 0.1868 -0.0164 -0.0422 -0.0122 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.7571 0.1471 0.1928 0.0044  0.0427  -0.0135 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.5708 0.1364 0.1981 0.0017  -0.0512 -0.0115 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4928 0.1337 0.1994 0.0080  -0.0541 -0.0114 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4639 0.1340 0.2225 0.0007  -0.0909 -0.0100 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5053 0.1292 0.2384 -0.0115 -0.1256 -0.0056 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.5011 0.1266 0.1928 0.0097  -0.0477 -0.0109 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.5474 0.1665 0.2227 0.0225  0.0056  -0.0089 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3913 0.1309 0.2213 0.0063  -0.0823 -0.0118 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3583 0.1238 0.2473 0.0009  -0.1058 -0.0099 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3573 0.1425 0.2703 0.0001  -0.1033 -0.0110 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3398 0.1550 0.3137 -0.0022 -0.1096 -0.0100 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3566 0.1209 0.2242 0.0018  -0.0914 -0.0125 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3083 0.0929 0.1968 0.0016  -0.0866 -0.0140 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2569 0.1020 0.1970 0.0058  -0.0637 -0.0184 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2778 0.1428 0.2159 0.0103  -0.0451 -0.0192 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2266 0.0943 0.2102 0.0023  -0.0656 -0.0199 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2064 0.1159 0.2245 0.0017  -0.0435 -0.0248 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2002 0.1235 0.1989 0.0028  -0.0264 -0.0263 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2192 0.1296 0.2026 0.0037  -0.0293 -0.0255 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2217 0.1410 0.2970 -0.0035 -0.0456 -0.0256 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2462 0.1626 0.3584 -0.0044 -0.0548 -0.0221 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2357 0.1787 0.3276 -0.0078 -0.0197 -0.0322 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2533 0.1735 0.4377 -0.0084 -0.0544 -0.0183 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1640 0.1135 0.1682 0.0002  -0.0105 -0.0270 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1636 0.1289 0.1601 -0.0029 0.0012  -0.0252 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1668 0.1442 0.1816 -0.0141 0.0100  -0.0315 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1757 0.1552 0.2001 -0.0195 0.0154  -0.0344 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1782 0.1557 0.1667 -0.0023 0.0073  -0.0168 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1676 0.1640 0.1590 -0.0107 0.0128  -0.0095 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1685 0.1601 0.1561 -0.0051 0.0162  -0.0059 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1934 0.2025 0.1918 -0.0119 0.0132  0.0044  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1768 0.1557 0.1925 -0.0183 0.0148  -0.0340 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1868 0.1652 0.2113 -0.0302 0.0287  -0.0410 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2038 0.1869 0.2066 -0.0400 0.0334  -0.0391 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2003 0.1894 0.1986 -0.0344 0.0270  -0.0338 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2136 0.1833 0.2694 -0.0273 0.0302  -0.0454 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2903 0.2519 0.3799 -0.0206 0.0191  -0.0433 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3236 0.2781 0.4553 -0.0207 0.0179  -0.0426 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3548 0.3068 0.5121 -0.0291 0.0474  -0.0490 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3552 0.2997 0.5590 -0.0302 0.0604  -0.0485 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3790 0.3229 0.6195 -0.0238 0.0391  -0.0397 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3516 0.2831 0.5645 -0.0391 0.0961  -0.0558 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2170 0.1901 0.2036 -0.0565 0.0455  -0.0433 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2601 0.2277 0.2200 -0.0717 0.0473  -0.0415 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2979 0.2422 0.2570 -0.0811 0.0701  -0.0541 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2869 0.2260 0.2782 -0.0733 0.0825  -0.0606 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2875 0.2491 0.2150 -0.0890 0.0391  -0.0328 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3110 0.2396 0.2102 -0.1056 0.0569  -0.0423 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3432 0.2703 0.2702 -0.0984 0.0766  -0.0559 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3887 0.2865 0.3124 -0.1077 0.1051  -0.0683 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4241 0.2865 0.3363 -0.1182 0.1336  -0.0774 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.4461 0.2821 0.3734 -0.1213 0.1663  -0.0871 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4504 0.3272 0.3278 -0.1282 0.1056  -0.0682 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.5291 0.3792 0.3443 -0.1537 0.0943  -0.0619 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.6360 0.4642 0.4072 -0.1755 0.0861  -0.0582 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6437 0.5001 0.4270 -0.1730 0.0578  -0.0438 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.6849 0.4589 0.4074 -0.1969 0.1135  -0.0705 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4251 0.2847 0.3155 -0.1231 0.1249  -0.0732 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4297 0.2526 0.3041 -0.1332 0.1525  -0.0810 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.3861 0.2293 0.3272 -0.1118 0.1587  -0.0815 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4188 0.2328 0.3647 -0.1165 0.1878  -0.0876 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.4683 0.2718 0.2793 -0.1532 0.1377  -0.0748 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5352 0.3121 0.2800 -0.1795 0.1235  -0.0696 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5437 0.3493 0.2827 -0.1826 0.0827  -0.0521 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.6068 0.3256 0.2895 -0.2055 0.1448  -0.0778 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.6053 0.3759 0.2877 -0.2094 0.0746  -0.0484 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6435 0.3584 0.2826 -0.2251 0.1105  -0.0647 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3246 0.2108 0.3114 -0.0906 0.1309  -0.0738 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2730 0.1739 0.3169 -0.0739 0.1275  -0.0713 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2346 0.1646 0.2792 -0.0614 0.0944  -0.0624 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2335 0.1785 0.2514 -0.0605 0.0753  -0.0568 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2096 0.1434 0.2858 -0.0526 0.0910  -0.0602 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2046 0.1574 0.2790 -0.0413 0.0639  -0.0527 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2030 0.1598 0.2339 -0.0486 0.0599  -0.0497 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2370 0.1786 0.2520 -0.0597 0.0751  -0.0531 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2031 0.1549 0.3246 -0.0319 0.0582  -0.0500 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2037 0.1657 0.3098 -0.0229 0.0333  -0.0436 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2022 0.1508 0.3762 -0.0260 0.0510  -0.0464 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1862 0.1593 0.2009 -0.0429 0.0410  -0.0415 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1882 0.1689 0.1770 -0.0493 0.0336  -0.0330 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1650 0.1548 0.1655 -0.0373 0.0241  -0.0279 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1772 0.1687 0.1684 -0.0431 0.0235  -0.0238 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2014 0.1937 0.1796 -0.0499 0.0233  -0.0234 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2200 0.2238 0.1916 -0.0544 0.0121  -0.0083 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2274 0.2089 0.1886 -0.0641 0.0299  -0.0273 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1450 0.1347 0.1597 -0.0226 0.0159  -0.0277 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1572 0.1465 0.1736 -0.0127 0.0080  -0.0233 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1673 0.1400 0.1831 -0.0019 -0.0028 -0.0236 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1657 0.1300 0.1880 -0.0020 -0.0066 -0.0269 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1694 0.1312 0.1729 0.0054  -0.0084 -0.0196 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1888 0.1188 0.1733 0.0111  -0.0209 -0.0193 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2131 0.1252 0.1639 0.0179  -0.0121 -0.0134 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2009 0.1277 0.1570 0.0201  -0.0009 -0.0080 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2230 0.1380 0.2211 0.0105  -0.0374 -0.0203 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2551 0.1836 0.2616 0.0118  -0.0315 -0.0194 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2213 0.1407 0.2617 0.0055  -0.0459 -0.0224 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2948 0.1996 0.3073 0.0122  -0.0512 -0.0179 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2443 0.1181 0.1594 0.0204  -0.0148 -0.0132 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2595 0.1010 0.1372 0.0267  0.0021  -0.0082 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2749 0.1006 0.1409 0.0287  0.0024  -0.0070 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.3008 0.1102 0.1603 0.0241  -0.0191 -0.0106 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3075 0.0927 0.1327 0.0254  -0.0015 -0.0100 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3565 0.0924 0.1339 0.0310  0.0246  -0.0061 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3027 0.1031 0.1395 0.0247  0.0009  -0.0107 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2794 0.1099 0.1496 0.0350  0.0261  0.0002  125 SER   A N   
922  C CA  . SER   A 119 ? 0.3008 0.1195 0.1644 0.0377  0.0309  0.0022  125 SER   A CA  
923  C C   . SER   A 119 ? 0.3718 0.1491 0.2063 0.0449  0.0625  0.0089  125 SER   A C   
924  O O   . SER   A 119 ? 0.4039 0.1440 0.2074 0.0458  0.0676  0.0077  125 SER   A O   
925  C CB  . SER   A 119 ? 0.2636 0.1401 0.1808 0.0369  0.0298  0.0070  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2943 0.1630 0.2097 0.0400  0.0347  0.0095  125 SER   A OG  
927  N N   . THR   A 120 ? 0.3929 0.1746 0.2424 0.0502  0.0876  0.0173  126 THR   A N   
928  C CA  . THR   A 120 ? 0.4480 0.1856 0.2809 0.0586  0.1286  0.0261  126 THR   A CA  
929  C C   . THR   A 120 ? 0.5063 0.2100 0.3161 0.0612  0.1497  0.0275  126 THR   A C   
930  O O   . THR   A 120 ? 0.4742 0.2014 0.2922 0.0573  0.1311  0.0238  126 THR   A O   
931  C CB  . THR   A 120 ? 0.4235 0.2072 0.3285 0.0650  0.1479  0.0437  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4127 0.2470 0.3774 0.0646  0.1464  0.0562  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4119 0.2299 0.3400 0.0620  0.1281  0.0432  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5772 0.2220 0.3584 0.0679  0.1927  0.0330  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.6361 0.2432 0.3966 0.0712  0.2200  0.0354  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.7072 0.2496 0.4510 0.0802  0.2794  0.0445  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.7161 0.2464 0.4699 0.0842  0.3000  0.0499  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.7670 0.2664 0.4878 0.0833  0.3096  0.0464  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.8445 0.2679 0.5447 0.0919  0.3765  0.0547  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.8226 0.2903 0.6257 0.1044  0.4103  0.0771  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.7534 0.3157 0.6547 0.1060  0.3821  0.0907  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.8699 0.2627 0.6509 0.1118  0.4724  0.0831  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.8423 0.2644 0.7264 0.1245  0.5125  0.1078  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.7827 0.2665 0.7084 0.1224  0.4782  0.1106  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.7538 0.2885 0.7877 0.1302  0.4918  0.1350  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.8201 0.3081 0.8300 0.1329  0.5226  0.1346  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.9212 0.3393 0.9022 0.1382  0.5741  0.1357  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 1.0122 0.3207 0.9099 0.1406  0.6327  0.1272  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.8839 0.3561 0.9297 0.1391  0.5576  0.1469  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.7750 0.2463 0.6169 0.1115  0.4370  0.0880  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.7028 0.2309 0.5786 0.1086  0.4036  0.0884  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5968 0.2308 0.5473 0.1024  0.3461  0.0934  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5644 0.2547 0.5651 0.0997  0.3221  0.0996  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.5513 0.2039 0.4969 0.0981  0.3235  0.0887  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4705 0.2072 0.4707 0.0904  0.2744  0.0917  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4722 0.2016 0.4012 0.0806  0.2346  0.0677  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5627 0.2298 0.4204 0.0802  0.2447  0.0560  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4388 0.2048 0.5122 0.0948  0.2875  0.1124  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4214 0.2040 0.5944 0.1036  0.3231  0.1442  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4269 0.2173 0.6627 0.1092  0.3452  0.1647  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3777 0.2314 0.6215 0.0952  0.2861  0.1592  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3702 0.1624 0.3267 0.0716  0.1907  0.0637  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3596 0.1539 0.2734 0.0632  0.1553  0.0455  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3008 0.1604 0.2695 0.0571  0.1302  0.0514  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2747 0.1809 0.2964 0.0528  0.1217  0.0635  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3783 0.1656 0.2549 0.0564  0.1307  0.0309  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3632 0.2006 0.2884 0.0536  0.1221  0.0370  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3950 0.1884 0.2490 0.0480  0.0952  0.0170  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2869 0.1423 0.2389 0.0554  0.1195  0.0447  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2477 0.1544 0.2408 0.0487  0.0986  0.0492  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2522 0.1688 0.2227 0.0403  0.0687  0.0322  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2872 0.1676 0.2144 0.0411  0.0623  0.0197  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1967 0.1568 0.1967 0.0300  0.0506  0.0334  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1832 0.1508 0.1718 0.0222  0.0307  0.0187  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1708 0.1616 0.1772 0.0156  0.0232  0.0211  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1619 0.1767 0.1921 0.0084  0.0217  0.0340  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1661 0.1497 0.1605 0.0135  0.0230  0.0146  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1803 0.1471 0.1626 0.0186  0.0302  0.0143  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2097 0.1473 0.1639 0.0215  0.0246  0.0029  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1963 0.1738 0.1985 0.0196  0.0407  0.0279  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2189 0.1364 0.1561 0.0250  0.0310  0.0028  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2114 0.1715 0.2025 0.0248  0.0501  0.0274  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2198 0.1483 0.1736 0.0276  0.0463  0.0137  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1685 0.1500 0.1643 0.0157  0.0152  0.0100  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1469 0.1459 0.1559 0.0091  0.0102  0.0101  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1402 0.1504 0.1516 -0.0041 0.0060  0.0036  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1450 0.1452 0.1548 -0.0044 0.0045  -0.0074 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1530 0.1350 0.1551 0.0143  0.0049  0.0016  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1468 0.1713 0.1605 -0.0173 0.0041  0.0117  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1624 0.1828 0.1626 -0.0337 0.0043  0.0052  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1768 0.1854 0.1745 -0.0366 0.0115  -0.0073 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1833 0.1941 0.1873 -0.0330 0.0107  -0.0058 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1772 0.2039 0.1691 -0.0517 -0.0051 0.0206  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2748 0.2826 0.2346 -0.0732 -0.0042 0.0146  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2569 0.2588 0.2117 -0.0731 0.0013  0.0069  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3480 0.3401 0.2819 -0.0909 -0.0065 0.0161  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1729 0.1668 0.1654 -0.0439 0.0221  -0.0187 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1898 0.1676 0.1882 -0.0479 0.0368  -0.0287 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2312 0.1826 0.1954 -0.0695 0.0533  -0.0339 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2739 0.2026 0.2402 -0.0743 0.0747  -0.0427 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1894 0.1631 0.2264 -0.0354 0.0411  -0.0363 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1889 0.1724 0.2420 -0.0192 0.0219  -0.0311 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1903 0.1573 0.2327 -0.0377 0.0475  -0.0410 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2413 0.1889 0.1735 -0.0835 0.0454  -0.0280 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2774 0.1875 0.1626 -0.1077 0.0593  -0.0332 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3510 0.2297 0.1928 -0.1275 0.0649  -0.0321 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4186 0.2489 0.2149 -0.1472 0.0881  -0.0414 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2795 0.1916 0.1413 -0.1197 0.0427  -0.0242 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2608 0.1939 0.1556 -0.1033 0.0425  -0.0273 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2613 0.1991 0.1382 -0.1149 0.0244  -0.0153 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2584 0.2247 0.1557 -0.1099 0.0005  0.0044  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2931 0.2720 0.1981 -0.1150 -0.0171 0.0205  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3031 0.2670 0.1859 -0.1286 -0.0182 0.0188  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2935 0.2983 0.2337 -0.1065 -0.0314 0.0398  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3478 0.2464 0.1984 -0.1238 0.0468  -0.0209 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.3900 0.2572 0.1976 -0.1434 0.0495  -0.0186 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.3866 0.2383 0.2101 -0.1342 0.0796  -0.0327 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4265 0.2405 0.2076 -0.1513 0.0915  -0.0345 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.3953 0.2892 0.2113 -0.1452 0.0177  0.0020  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3858 0.3236 0.2623 -0.1160 0.0144  0.0040  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3468 0.3059 0.2609 -0.0946 0.0197  -0.0027 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3854 0.3315 0.2674 -0.1162 0.0054  0.0130  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3523 0.2274 0.2363 -0.1094 0.0911  -0.0408 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3380 0.2036 0.2560 -0.0993 0.1155  -0.0494 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3898 0.2079 0.2964 -0.1100 0.1565  -0.0620 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3777 0.2008 0.3376 -0.0971 0.1720  -0.0671 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2807 0.1857 0.2690 -0.0724 0.1026  -0.0477 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2585 0.2005 0.2529 -0.0613 0.0697  -0.0364 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2338 0.1959 0.2783 -0.0399 0.0582  -0.0362 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2713 0.2150 0.2487 -0.0663 0.0638  -0.0299 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4541 0.2186 0.2871 -0.1363 0.1749  -0.0655 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.5160 0.2178 0.3162 -0.1521 0.2210  -0.0781 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.5304 0.2189 0.3949 -0.1375 0.2636  -0.0858 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.5415 0.2014 0.4290 -0.1374 0.3017  -0.0935 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.5863 0.2179 0.2749 -0.1883 0.2296  -0.0795 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.6352 0.2723 0.2629 -0.2086 0.1827  -0.0661 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.7437 0.2931 0.2538 -0.2500 0.1923  -0.0671 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.6287 0.2976 0.2797 -0.2018 0.1650  -0.0637 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.5177 0.2317 0.4246 -0.1234 0.2560  -0.0813 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4957 0.2032 0.4786 -0.1086 0.2902  -0.0840 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.4679 0.2134 0.5531 -0.0861 0.2852  -0.0798 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.4735 0.2068 0.6331 -0.0769 0.3172  -0.0789 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4660 0.1936 0.4664 -0.1003 0.2763  -0.0787 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4170 0.2087 0.4365 -0.0858 0.2204  -0.0683 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4200 0.2271 0.3828 -0.0946 0.1870  -0.0621 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3696 0.2096 0.4699 -0.0620 0.1941  -0.0615 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3888 0.2492 0.3939 -0.0754 0.1501  -0.0535 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3588 0.2359 0.4384 -0.0568 0.1523  -0.0541 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3453 0.1945 0.5348 -0.0466 0.2014  -0.0585 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3425 0.2565 0.4706 -0.0382 0.1217  -0.0472 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3257 0.2144 0.5642 -0.0300 0.1617  -0.0493 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3229 0.2393 0.5224 -0.0266 0.1242  -0.0455 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4340 0.2213 0.5274 -0.0784 0.2456  -0.0750 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4066 0.2226 0.5874 -0.0609 0.2353  -0.0691 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.4746 0.2549 0.6973 -0.0643 0.2828  -0.0731 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.4427 0.2395 0.7595 -0.0507 0.2814  -0.0645 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.3710 0.2246 0.5360 -0.0555 0.1911  -0.0648 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3400 0.2300 0.4918 -0.0465 0.1478  -0.0577 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3315 0.2461 0.4636 -0.0425 0.1160  -0.0541 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3024 0.2096 0.5256 -0.0308 0.1323  -0.0499 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.5670 0.2932 0.7192 -0.0842 0.3239  -0.0844 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.6374 0.3176 0.8199 -0.0893 0.3799  -0.0897 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.7220 0.3520 0.9300 -0.0921 0.4378  -0.0927 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.7345 0.3478 1.0320 -0.0842 0.4792  -0.0887 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.7024 0.3356 0.7826 -0.1126 0.3986  -0.1013 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.7271 0.4028 0.7770 -0.1120 0.3477  -0.0983 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.7088 0.4248 0.8305 -0.0959 0.3291  -0.0919 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7846 0.4491 0.7402 -0.1293 0.3267  -0.1007 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.7867 0.3847 0.9158 -0.1055 0.4465  -0.0988 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.8448 0.3832 0.9845 -0.1104 0.5088  -0.1031 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.8275 0.4051 1.0628 -0.0900 0.4970  -0.0918 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.8517 0.3853 1.1195 -0.0901 0.5508  -0.0928 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.9630 0.4269 0.9580 -0.1403 0.5324  -0.1158 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.0463 0.5467 0.9709 -0.1465 0.4695  -0.1118 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.1785 0.6447 0.9738 -0.1753 0.4485  -0.1164 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.2077 0.6821 0.9376 -0.1870 0.4089  -0.1114 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.2330 0.6636 0.9968 -0.1871 0.4700  -0.1230 145 GLU   A OE2 
1078 N N1  . A1BPV B .   ? 0.7243 0.2271 0.3419 0.0518  0.1666  0.0096  201 A1BPV A N1  
1079 C C4  . A1BPV B .   ? 0.9688 0.2576 0.4163 0.0531  0.2800  0.0095  201 A1BPV A C4  
1080 C C5  . A1BPV B .   ? 0.9837 0.2376 0.4271 0.0590  0.3214  0.0144  201 A1BPV A C5  
1081 C C6  . A1BPV B .   ? 0.9557 0.2475 0.4263 0.0581  0.2979  0.0140  201 A1BPV A C6  
1082 C C7  . A1BPV B .   ? 0.9074 0.2683 0.4083 0.0513  0.2348  0.0086  201 A1BPV A C7  
1083 C C8  . A1BPV B .   ? 0.7453 0.2365 0.3627 0.0558  0.1911  0.0133  201 A1BPV A C8  
1084 C C10 . A1BPV B .   ? 0.7247 0.1934 0.2804 0.0327  0.0977  -0.0037 201 A1BPV A C10 
1085 C C13 . A1BPV B .   ? 0.4858 0.2051 0.2958 0.0556  0.1027  0.0177  201 A1BPV A C13 
1086 O O2  . A1BPV B .   ? 0.4765 0.1996 0.3053 0.0607  0.1209  0.0246  201 A1BPV A O2  
1087 N N2  . A1BPV B .   ? 0.4198 0.1979 0.2739 0.0522  0.0791  0.0170  201 A1BPV A N2  
1088 C C12 . A1BPV B .   ? 0.5809 0.2185 0.3087 0.0509  0.1079  0.0101  201 A1BPV A C12 
1089 C C11 . A1BPV B .   ? 0.6438 0.2180 0.3023 0.0411  0.0863  0.0013  201 A1BPV A C11 
1090 C C9  . A1BPV B .   ? 0.7500 0.2111 0.3021 0.0367  0.1213  -0.0015 201 A1BPV A C9  
1091 C C14 . A1BPV B .   ? 0.6349 0.2269 0.3444 0.0587  0.1591  0.0177  201 A1BPV A C14 
1092 O O1  . A1BPV B .   ? 0.6692 0.2279 0.3656 0.0641  0.1999  0.0235  201 A1BPV A O1  
1093 N N   . A1BPV B .   ? 0.8645 0.2556 0.3849 0.0492  0.2096  0.0070  201 A1BPV A N   
1094 C C3  . A1BPV B .   ? 0.9299 0.2897 0.4129 0.0468  0.2189  0.0048  201 A1BPV A C3  
1095 C C2  . A1BPV B .   ? 0.8971 0.2923 0.4074 0.0458  0.1969  0.0043  201 A1BPV A C2  
1096 C C1  . A1BPV B .   ? 0.8567 0.3223 0.4092 0.0394  0.1385  -0.0001 201 A1BPV A C1  
1097 O O   . A1BPV B .   ? 0.8498 0.3255 0.3990 0.0341  0.1143  -0.0035 201 A1BPV A O   
1098 C C   . A1BPV B .   ? 0.7886 0.3580 0.4213 0.0364  0.0871  -0.0023 201 A1BPV A C   
# 
