data_7HYA
# 
_entry.id   7HYA 
# 
_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   7HYA         pdb_00007hya 10.2210/pdb7hya/pdb 
WWPDB D_1001408082 ?            ?                   
# 
_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                        7HYA 
_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)-1-[(2,1,3-benzoxadiazol-4-yl)acetyl]piperidine-3-carboxamide' 288.302   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    71 ?         ? ? ? 
# 
_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)-1-[(2,1,3-benzoxadiazol-4-yl)acetyl]piperidine-3-carboxamide' A1BPR 
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 
A1BPR non-polymer         . '(3S)-1-[(2,1,3-benzoxadiazol-4-yl)acetyl]piperidine-3-carboxamide' ? 'C14 H16 N4 O3'  288.302 
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        A1BPR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPR 
_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 A1BPR 1  201 201 A1BPR 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 59  HOH   HOH A . 
E 5 HOH   2  302 18  HOH   HOH A . 
E 5 HOH   3  303 9   HOH   HOH A . 
E 5 HOH   4  304 29  HOH   HOH A . 
E 5 HOH   5  305 42  HOH   HOH A . 
E 5 HOH   6  306 27  HOH   HOH A . 
E 5 HOH   7  307 22  HOH   HOH A . 
E 5 HOH   8  308 37  HOH   HOH A . 
E 5 HOH   9  309 36  HOH   HOH A . 
E 5 HOH   10 310 40  HOH   HOH A . 
E 5 HOH   11 311 8   HOH   HOH A . 
E 5 HOH   12 312 23  HOH   HOH A . 
E 5 HOH   13 313 34  HOH   HOH A . 
E 5 HOH   14 314 12  HOH   HOH A . 
E 5 HOH   15 315 16  HOH   HOH A . 
E 5 HOH   16 316 7   HOH   HOH A . 
E 5 HOH   17 317 24  HOH   HOH A . 
E 5 HOH   18 318 35  HOH   HOH A . 
E 5 HOH   19 319 51  HOH   HOH A . 
E 5 HOH   20 320 14  HOH   HOH A . 
E 5 HOH   21 321 54  HOH   HOH A . 
E 5 HOH   22 322 25  HOH   HOH A . 
E 5 HOH   23 323 17  HOH   HOH A . 
E 5 HOH   24 324 60  HOH   HOH A . 
E 5 HOH   25 325 71  HOH   HOH A . 
E 5 HOH   26 326 4   HOH   HOH A . 
E 5 HOH   27 327 65  HOH   HOH A . 
E 5 HOH   28 328 38  HOH   HOH A . 
E 5 HOH   29 329 53  HOH   HOH A . 
E 5 HOH   30 330 67  HOH   HOH A . 
E 5 HOH   31 331 2   HOH   HOH A . 
E 5 HOH   32 332 45  HOH   HOH A . 
E 5 HOH   33 333 48  HOH   HOH A . 
E 5 HOH   34 334 64  HOH   HOH A . 
E 5 HOH   35 335 19  HOH   HOH A . 
E 5 HOH   36 336 21  HOH   HOH A . 
E 5 HOH   37 337 6   HOH   HOH A . 
E 5 HOH   38 338 41  HOH   HOH A . 
E 5 HOH   39 339 10  HOH   HOH A . 
E 5 HOH   40 340 13  HOH   HOH A . 
E 5 HOH   41 341 49  HOH   HOH A . 
E 5 HOH   42 342 66  HOH   HOH A . 
E 5 HOH   43 343 11  HOH   HOH A . 
E 5 HOH   44 344 20  HOH   HOH A . 
E 5 HOH   45 345 68  HOH   HOH A . 
E 5 HOH   46 346 5   HOH   HOH A . 
E 5 HOH   47 347 50  HOH   HOH A . 
E 5 HOH   48 348 74  HOH   HOH A . 
E 5 HOH   49 349 3   HOH   HOH A . 
E 5 HOH   50 350 30  HOH   HOH A . 
E 5 HOH   51 351 15  HOH   HOH A . 
E 5 HOH   52 352 61  HOH   HOH A . 
E 5 HOH   53 353 46  HOH   HOH A . 
E 5 HOH   54 354 26  HOH   HOH A . 
E 5 HOH   55 355 39  HOH   HOH A . 
E 5 HOH   56 356 58  HOH   HOH A . 
E 5 HOH   57 357 31  HOH   HOH A . 
E 5 HOH   58 358 56  HOH   HOH A . 
E 5 HOH   59 359 63  HOH   HOH A . 
E 5 HOH   60 360 70  HOH   HOH A . 
E 5 HOH   61 361 33  HOH   HOH A . 
E 5 HOH   62 362 55  HOH   HOH A . 
E 5 HOH   63 363 28  HOH   HOH A . 
E 5 HOH   64 364 73  HOH   HOH A . 
E 5 HOH   65 365 43  HOH   HOH A . 
E 5 HOH   66 366 32  HOH   HOH A . 
E 5 HOH   67 367 72  HOH   HOH A . 
E 5 HOH   68 368 52  HOH   HOH A . 
E 5 HOH   69 369 69  HOH   HOH A . 
E 5 HOH   70 370 44  HOH   HOH A . 
E 5 HOH   71 371 62  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           7HYA 
_cell.length_a           72.653 
_cell.length_b           61.796 
_cell.length_c           32.699 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.86 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYA 
_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          7HYA 
_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   46.67 
_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   2024-12-02 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.04 
_reflns.d_resolution_high            1.80 
_reflns.number_obs                   13221 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            0.261 
_reflns.pdbx_netI_over_sigmaI        6.1 
_reflns.pdbx_redundancy              6.9 
_reflns.pdbx_Rrim_I_all              0.284 
_reflns.pdbx_Rpim_I_all              0.109 
_reflns.pdbx_CC_half                 0.972 
_reflns.pdbx_number_measured_all     91188 
_reflns.pdbx_chi_squared             0.34 
_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                  1.80 
_reflns_shell.d_res_low                   1.84 
_reflns_shell.number_measured_all         5070 
_reflns_shell.number_unique_obs           740 
_reflns_shell.Rmerge_I_obs                4.046 
_reflns_shell.pdbx_chi_squared            0.09 
_reflns_shell.pdbx_redundancy             6.9 
_reflns_shell.percent_possible_obs        91.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             4.390 
_reflns_shell.pdbx_Rpim_I_all             1.682 
_reflns_shell.pdbx_CC_half                0.177 
_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                                 7HYA 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     13216 
_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                             47.05 
_refine.ls_d_res_high                            1.802 
_refine.ls_percent_reflns_obs                    98.4 
_refine.ls_R_factor_obs                          0.2405 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2388 
_refine.ls_R_factor_R_free                       0.2732 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.910 
_refine.ls_number_reflns_R_free                  649 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.923 
_refine.correlation_coeff_Fo_to_Fc_free          0.906 
_refine.B_iso_mean                               40.78 
_refine.aniso_B[1][1]                            12.47330 
_refine.aniso_B[2][2]                            -12.13910 
_refine.aniso_B[3][3]                            -0.33420 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -4.21150 
_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             0.160 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.147 
_refine.pdbx_overall_SU_R_Blow_DPI               0.161 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.147 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYA 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_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             71 
_refine_hist.number_atoms_total               1171 
_refine_hist.d_res_high                       1.802 
_refine_hist.d_res_low                        47.05 
# 
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                  0.009 ? 2.00  1130 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.96  ? 2.00  1538 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  '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  209  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1130 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.78  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.25 ? ?     ?    '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  882  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   33 
_refine_ls_shell.d_res_high                       1.80 
_refine_ls_shell.d_res_low                        1.82 
_refine_ls_shell.number_reflns_R_work             403 
_refine_ls_shell.R_factor_R_work                  0.4159 
_refine_ls_shell.percent_reflns_obs               83.02 
_refine_ls_shell.R_factor_R_free                  0.4422 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            2.42 
_refine_ls_shell.number_reflns_R_free             10 
_refine_ls_shell.number_reflns_all                413 
_refine_ls_shell.R_factor_all                     0.4165 
# 
_struct.entry_id                  7HYA 
_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-0035416-001 (A71EV2A-x4346)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYA 
_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              7HYA 
_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 ? ? ? ? ? ? ? 2.389 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.415 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
# 
_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_555 107.8 ? 
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_555 105.2 ? 
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_555 112.9 ? 
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_555 107.2 ? 
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_555 101.6 ? 
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_555 121.4 ? 
# 
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 LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
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 THR A 120 ? N THR A 126 O GLY A 127 ? O GLY A 133 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HYA 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -93.84  34.41  
2 1 SER A 125 ? ? -135.86 -30.42 
# 
_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         15.1694 
_pdbx_refine_tls.origin_y         6.6384 
_pdbx_refine_tls.origin_z         14.3025 
_pdbx_refine_tls.T[1][1]          0.2710 
_pdbx_refine_tls.T[2][2]          -0.1563 
_pdbx_refine_tls.T[3][3]          -0.0848 
_pdbx_refine_tls.T[1][2]          0.0192 
_pdbx_refine_tls.T[1][3]          -0.0985 
_pdbx_refine_tls.T[2][3]          -0.0083 
_pdbx_refine_tls.L[1][1]          0.9731 
_pdbx_refine_tls.L[2][2]          9.0330 
_pdbx_refine_tls.L[3][3]          1.3554 
_pdbx_refine_tls.L[1][2]          2.5169 
_pdbx_refine_tls.L[1][3]          -0.9393 
_pdbx_refine_tls.L[2][3]          -2.8888 
_pdbx_refine_tls.S[1][1]          -0.0986 
_pdbx_refine_tls.S[1][2]          0.0603 
_pdbx_refine_tls.S[1][3]          0.0095 
_pdbx_refine_tls.S[2][1]          0.3656 
_pdbx_refine_tls.S[2][2]          0.1321 
_pdbx_refine_tls.S[2][3]          -0.2973 
_pdbx_refine_tls.S[3][1]          -0.0837 
_pdbx_refine_tls.S[3][2]          -0.1729 
_pdbx_refine_tls.S[3][3]          -0.0336 
# 
_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 
A1BPR N1   N  N N 1   
A1BPR N3   N  Y N 2   
A1BPR C4   C  N N 3   
A1BPR C5   C  N N 4   
A1BPR C6   C  N N 5   
A1BPR C7   C  Y N 6   
A1BPR C8   C  Y N 7   
A1BPR C10  C  Y N 8   
A1BPR C13  C  N N 9   
A1BPR O1   O  N N 10  
A1BPR C3   C  N N 11  
A1BPR C2   C  N N 12  
A1BPR C1   C  N S 13  
A1BPR C    C  N N 14  
A1BPR O    O  N N 15  
A1BPR N    N  N N 16  
A1BPR C12  C  Y N 17  
A1BPR O2   O  Y N 18  
A1BPR N2   N  Y N 19  
A1BPR C11  C  Y N 20  
A1BPR C9   C  Y N 21  
A1BPR H8   H  N N 22  
A1BPR H7   H  N N 23  
A1BPR H10  H  N N 24  
A1BPR H9   H  N N 25  
A1BPR H11  H  N N 26  
A1BPR H13  H  N N 27  
A1BPR H15  H  N N 28  
A1BPR H14  H  N N 29  
A1BPR H6   H  N N 30  
A1BPR H5   H  N N 31  
A1BPR H4   H  N N 32  
A1BPR H3   H  N N 33  
A1BPR H    H  N N 34  
A1BPR H1   H  N N 35  
A1BPR H2   H  N N 36  
A1BPR H12  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1BPR N   C    sing N N 1   
A1BPR O   C    doub N N 2   
A1BPR C   C1   sing N N 3   
A1BPR C1  C2   sing N N 4   
A1BPR C2  C3   sing N N 5   
A1BPR C3  C4   sing N N 6   
A1BPR C4  N1   sing N N 7   
A1BPR N1  C5   sing N N 8   
A1BPR C5  O1   doub N N 9   
A1BPR C6  C5   sing N N 10  
A1BPR C7  C6   sing N N 11  
A1BPR C7  C8   doub Y N 12  
A1BPR C8  C9   sing Y N 13  
A1BPR C9  C10  doub Y N 14  
A1BPR C10 C11  sing Y N 15  
A1BPR C11 N2   doub Y N 16  
A1BPR N2  O2   sing Y N 17  
A1BPR O2  N3   sing Y N 18  
A1BPR N3  C12  doub Y N 19  
A1BPR C12 C7   sing Y N 20  
A1BPR C11 C12  sing Y N 21  
A1BPR C13 N1   sing N N 22  
A1BPR C1  C13  sing N N 23  
A1BPR C4  H8   sing N N 24  
A1BPR C4  H7   sing N N 25  
A1BPR C6  H10  sing N N 26  
A1BPR C6  H9   sing N N 27  
A1BPR C8  H11  sing N N 28  
A1BPR C10 H13  sing N N 29  
A1BPR C13 H15  sing N N 30  
A1BPR C13 H14  sing N N 31  
A1BPR C3  H6   sing N N 32  
A1BPR C3  H5   sing N N 33  
A1BPR C2  H4   sing N N 34  
A1BPR C2  H3   sing N N 35  
A1BPR C1  H    sing N N 36  
A1BPR N   H1   sing N N 37  
A1BPR N   H2   sing N N 38  
A1BPR C9  H12  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_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                    7HYA 
_atom_sites.fract_transf_matrix[1][1]   0.013764 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000688 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016182 
_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]   0.030620 
_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   ? 18.987 6.458   24.306 1.00 45.60  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.210 6.461   23.500 1.00 45.91  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.239 5.276   22.497 1.00 44.08  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.550 4.276   22.711 1.00 44.65  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.434 6.415   24.413 1.00 48.25  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.527 5.141   25.035 1.00 52.18  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.043 5.392   21.442 1.00 41.82  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.166 4.340   20.431 1.00 40.95  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.441 4.862   19.027 1.00 38.94  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.019 5.968   18.686 1.00 38.76  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.173 4.086   18.217 1.00 37.21  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.573 4.488   16.869 1.00 37.17  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.581 3.309   15.868 1.00 37.38  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.591 2.146   16.292 1.00 37.32  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.960 5.102   16.930 1.00 37.35  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.582 3.610   14.542 1.00 37.05  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.675 2.601   13.479 1.00 37.52  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.053 2.786   12.843 1.00 39.72  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.421 3.901   12.455 1.00 39.75  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.571 2.753   12.384 1.00 36.43  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.165 2.914   12.973 1.00 35.73  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.625 1.603   11.372 1.00 36.72  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.168 3.402   11.955 1.00 35.71  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.818 1.708   12.736 1.00 41.33  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.150 1.766   12.141 1.00 42.91  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.152 1.012   10.830 1.00 44.81  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.161 -0.220  10.847 1.00 45.43  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.185 1.162   13.108 1.00 42.88  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.352 2.013   14.342 1.00 43.15  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.119 3.174   14.311 1.00 44.69  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.641 1.737   15.498 1.00 43.53  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.218 4.005   15.421 1.00 45.28  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.726 2.562   16.609 1.00 44.81  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.526 3.687   16.570 1.00 46.33  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.628 4.474   17.679 1.00 48.95  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.091 1.729   9.698  1.00 45.39  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.111 1.110   8.368  1.00 46.81  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.276 1.670   7.562  1.00 48.21  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.317 2.869   7.261  1.00 48.54  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.767 1.176   7.594  1.00 47.78  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.188 2.598   7.553  1.00 48.33  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.930 0.613   6.192  1.00 48.30  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.254 0.818   7.270  1.00 48.52  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.455 1.228   6.553  1.00 49.84  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.204 2.317   7.302  1.00 51.07  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.406 2.192   8.514  1.00 52.04  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.522 3.431   6.628  1.00 50.62  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.220 4.528   7.290  1.00 50.71  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.250 5.584   7.831  1.00 48.64  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.581 6.771   7.889  1.00 48.31  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.281 5.137   6.376  1.00 53.87  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.515 4.268   6.235  1.00 60.84  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.749 3.342   7.019  1.00 63.18  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.342 4.555   5.235  1.00 62.85  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.070 5.142   8.290  1.00 46.37  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.070 6.070   8.817  1.00 44.03  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.570 5.668   10.181 1.00 40.90  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.520 4.484   10.518 1.00 40.17  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.859 6.163   7.865  1.00 44.04  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.192 6.747   6.513  1.00 45.18  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.730 8.024   6.398  1.00 46.23  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.952 6.034   5.348  1.00 46.21  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.043 8.563   5.158  1.00 47.31  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.245 6.570   4.102  1.00 47.55  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.798 7.833   4.012  1.00 48.85  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.094 8.367   2.781  1.00 51.81  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.120 6.673   10.936 1.00 38.48  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.466 6.523   12.216 1.00 36.38  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.164 7.336   12.089 1.00 34.59  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.211 8.517   11.753 1.00 34.22  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.371 7.047   13.350 1.00 37.19  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.660 7.281   14.685 1.00 39.60  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.661 7.533   15.798 1.00 42.50  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.240 8.589   16.723 1.00 44.95  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.747 8.366   17.939 1.00 45.34  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.571 7.119   18.377 1.00 43.01  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.419 9.386   18.726 1.00 43.81  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.005 6.690   12.253 1.00 33.33  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.716 7.389   12.185 1.00 32.29  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.231 7.522   13.611 1.00 31.69  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.151 6.520   14.310 1.00 32.57  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.652 6.654   11.339 1.00 32.36  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.448 7.564   11.091 1.00 31.97  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.235 6.132   10.025 1.00 32.20  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.917 8.724   14.053 1.00 30.48  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.445 8.952   15.423 1.00 30.91  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.232 9.895   15.399 1.00 30.57  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.030 10.598  14.398 1.00 30.81  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.570 9.602   16.296 1.00 31.61  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.658 8.608   16.640 1.00 32.55  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.153 10.837  15.623 1.00 31.76  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.496 10.030  16.542 1.00 29.49  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.451 11.057  16.625 1.00 29.47  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.198 12.385  16.648 1.00 30.65  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.195 12.523  17.371 1.00 31.68  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.640 10.973  17.913 1.00 29.78  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.831 9.702   18.071 1.00 31.99  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.301 8.730   18.645 1.00 33.27  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.598 9.700   17.602 1.00 31.22  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.786 13.323  15.810 1.00 30.14  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.430 14.625  15.735 1.00 30.14  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.474 15.318  17.117 1.00 32.18  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.529 15.830  17.477 1.00 33.14  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.757 15.508  14.667 1.00 28.07  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.514 16.790  14.313 1.00 27.60  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.527 17.725  13.630 1.00 28.74  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.081 18.980  13.093 1.00 29.12  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.228 20.098  13.792 1.00 30.47  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.978 20.112  15.098 1.00 28.86  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.616 21.221  13.190 1.00 30.30  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.392 15.226  17.927 1.00 32.89  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.355 15.861  19.262 1.00 34.17  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.317 15.244  20.299 1.00 35.22  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.573 15.843  21.339 1.00 35.45  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.922 15.937  19.821 1.00 35.10  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.369 14.651  20.352 1.00 36.77  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.765 13.719  19.509 1.00 37.56  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.293 14.198  21.631 1.00 37.46  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.366 12.720  20.293 1.00 38.35  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.659 12.955  21.577 1.00 37.95  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.878 14.079  19.999 1.00 36.14  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.832 13.422  20.878 1.00 37.39  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.266 13.406  20.296 1.00 38.69  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.144 12.772  20.885 1.00 39.06  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.364 11.981  21.171 1.00 37.44  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.052 11.818  21.964 1.00 38.86  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.752 10.341  22.241 1.00 38.61  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.081 12.604  23.273 1.00 39.45  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.499 14.042  19.133 1.00 39.15  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.815 14.049  18.497 1.00 40.39  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.888 14.693  19.378 1.00 41.51  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.601 15.637  20.103 1.00 40.96  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.749 14.749  17.141 1.00 40.38  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.112 14.144  19.334 1.00 43.15  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.267 14.609  20.113 1.00 45.15  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.029 15.753  19.395 1.00 47.10  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.685 16.102  18.265 1.00 47.17  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.206 13.400  20.367 1.00 45.87  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.798 13.019  19.125 1.00 46.12  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.505 12.241  21.007 1.00 46.57  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.081 16.321  20.031 1.00 48.92  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.914 17.323  19.377 1.00 50.90  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.657 16.657  18.206 1.00 50.92  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.805 17.272  17.149 1.00 50.93  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.941 17.897  20.360 1.00 53.87  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.364 18.767  21.425 1.00 59.39  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.088 20.101  21.192 1.00 62.21  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.138 18.495  22.735 1.00 62.01  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.664 20.589  22.348 1.00 63.26  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.683 19.662  23.311 1.00 63.57  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.126 15.404  18.405 1.00 50.65  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.817 14.629  17.374 1.00 51.43  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.926 14.373  16.158 1.00 49.86  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.401 14.488  15.031 1.00 50.96  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.336 13.303  17.931 1.00 54.75  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.237 12.587  16.953 1.00 60.97  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.249 13.134  16.509 1.00 63.31  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.885 11.353  16.581 1.00 62.38  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.640 14.052  16.379 1.00 47.16  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.653 13.864  15.301 1.00 44.62  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.554 15.131  14.441 1.00 42.90  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.626 15.041  13.224 1.00 42.85  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.268 13.491  15.875 1.00 43.90  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.159 12.049  16.338 1.00 44.86  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.754 11.179  15.690 1.00 45.01  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.478 11.801  17.358 1.00 44.69  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.456 16.312  15.072 1.00 41.74  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.385 17.603  14.374 1.00 41.45  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.711 17.997  13.673 1.00 43.41  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.690 18.646  12.637 1.00 43.20  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.922 18.720  15.348 1.00 39.73  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.429 18.788  15.510 1.00 37.66  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.687 18.283  16.539 1.00 37.97  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.495 19.312  14.562 1.00 36.35  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.344 18.474  16.291 1.00 37.85  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.202 19.132  15.097 1.00 36.86  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.624 19.915  13.307 1.00 36.34  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.052 19.549  14.427 1.00 36.39  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.481 20.338  12.655 1.00 36.62  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.216 20.134  13.206 1.00 36.23  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.859 17.618  14.252 1.00 45.27  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.184 17.892  13.666 1.00 46.50  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.465 16.950  12.460 1.00 47.14  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.275 17.277  11.592 1.00 48.27  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.271 17.714  14.723 1.00 46.45  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.806 15.784  12.421 1.00 46.03  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.919 14.834  11.320 1.00 45.06  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.567 14.689  10.582 1.00 43.56  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.249 13.610  10.094 1.00 43.31  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.388 13.500  11.857 1.00 46.04  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.824 13.541  12.325 1.00 49.08  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.724 13.963  11.599 1.00 50.69  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.064 13.105  13.545 1.00 48.58  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.762 15.777  10.540 1.00 42.39  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.434 15.840  9.914  1.00 40.69  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.476 15.463  8.445  1.00 40.14  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.331 15.965  7.722  1.00 40.58  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.862 17.262  10.047 1.00 39.93  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.501 17.555  9.356  1.00 39.94  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.379 16.680  9.957  1.00 39.88  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.119 19.047  9.481  1.00 38.95  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.538 14.583  8.006  1.00 38.60  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.338 14.163  6.623  1.00 37.66  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.013 14.821  6.118  1.00 37.02  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.993 15.488  5.087  1.00 37.87  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.271 12.613  6.522  1.00 37.96  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.671 12.168  5.194  1.00 38.58  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.640 11.967  6.759  1.00 38.35  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.929 14.662  6.892  1.00 35.35  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.571 15.116  6.596  1.00 33.43  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.758 15.197  7.908  1.00 31.57  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.954 14.392  8.803  1.00 31.49  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.911 14.072  5.655  1.00 33.01  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.434 14.258  5.420  1.00 33.19  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.841 15.206  4.642  1.00 33.86  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.363 13.502  6.019  1.00 32.54  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.469 15.075  4.698  1.00 34.10  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.150 14.034  5.529  1.00 33.37  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.311 12.462  6.952  1.00 31.92  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.906 13.512  5.891  1.00 33.12  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.081 11.941  7.296  1.00 32.17  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.898 12.451  6.755  1.00 32.47  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.834 16.141  8.006  1.00 30.31  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.943 16.265  9.156  1.00 29.22  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.603 16.862  8.680  1.00 28.23  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.572 17.645  7.735  1.00 27.27  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.568 17.084  10.310 1.00 29.50  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.152 18.439  9.909  1.00 30.50  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.205 19.618  9.721  1.00 33.03  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.569 20.545  8.957  1.00 35.67  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.105 19.616  10.320 1.00 29.02  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.507 16.483  9.329  1.00 27.99  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.190 16.989  8.986  1.00 27.15  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.391 17.119  10.281 1.00 26.02  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.961 16.115  10.847 1.00 25.86  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.505 16.079  7.948  1.00 28.84  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.193 16.600  7.370  1.00 33.27  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.580 17.479  7.987  1.00 31.71  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.783 16.117  6.294  1.00 37.77  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.175 18.372  10.733 1.00 24.93  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.409 18.678  11.945 0.50 25.06  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.435 18.603  11.966 0.50 24.89  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.988 18.138  11.829 1.00 24.96  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.442 17.638  12.797 1.00 24.29  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.339 20.188  12.177 0.50 25.99  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.517 20.067  12.391 0.50 25.34  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.586 20.758  12.528 0.50 27.61  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.957 20.888  11.382 0.50 26.44  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.392 18.253  10.630 1.00 25.32  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.023 17.799  10.408 1.00 26.60  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.865 16.278  10.586 1.00 26.05  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.758 15.825  10.815 1.00 27.09  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.482 18.278  9.061  1.00 29.16  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.896 17.430  8.000  1.00 32.51  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.949 15.505  10.478 1.00 24.63  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.907 14.047  10.668 1.00 24.41  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.574 13.597  11.978 1.00 24.65  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.559 12.401  12.274 1.00 25.65  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.609 13.328  9.495  1.00 24.47  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 12.984 13.596  8.121  1.00 23.71  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.745 12.923  6.980  1.00 26.02  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.761 11.460  7.099  1.00 26.49  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.944 10.621  6.081  1.00 26.92  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.088 11.085  4.846  1.00 24.26  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.946 9.308   6.287  1.00 26.60  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.217 14.524  12.725 1.00 24.63  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.980 14.224  13.934 1.00 24.95  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.121 13.246  13.565 1.00 25.96  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.380 12.312  14.328 1.00 26.49  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.086 13.638  15.070 1.00 25.07  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.830 13.409  16.377 1.00 26.95  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.618 14.290  16.767 1.00 25.30  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.629 12.310  17.012 1.00 28.50  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.770 13.420  12.391 1.00 25.58  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.900 12.541  12.033 1.00 25.78  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.179 13.339  11.809 1.00 26.67  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.156 14.479  11.354 1.00 26.36  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.649 11.683  10.778 1.00 25.33  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.571 10.604  10.870 1.00 27.24  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.383 9.911   9.480  1.00 26.98  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.906 9.578   11.992 1.00 28.13  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.294 12.709  12.114 1.00 27.36  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.609 13.248  11.864 1.00 29.11  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.468 12.040  11.523 1.00 30.26  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.336 10.975  12.122 1.00 30.70  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.171 14.062  13.069 1.00 30.01  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.506 14.773  12.825 1.00 31.23  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.570 16.093  13.559 1.00 32.38  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.692 13.888  13.164 1.00 32.08  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.272 12.176  10.489 1.00 31.75  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.193 11.150  10.042 1.00 33.57  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.591 11.751  10.051 1.00 35.89  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.823 12.836  9.487  1.00 35.10  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.833 10.560  8.661  1.00 34.18  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.898 9.547   8.215  1.00 35.25  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.443 9.914   8.690  1.00 33.92  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.501 11.069  10.745 1.00 38.10  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.897 11.458  10.830 1.00 41.05  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.797 10.345  10.283 1.00 44.78  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.391 9.177   10.205 1.00 43.97  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.270 11.792  12.268 1.00 42.01  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 27.940 10.729  13.147 1.00 43.89  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.023 10.721  9.899  1.00 47.69  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.000 9.782   9.357  1.00 50.99  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.765 9.050   10.472 1.00 54.27  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.926 9.581   11.572 1.00 54.43  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.980 10.524  8.459  1.00 52.22  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.577 11.579  9.193  1.00 54.45  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.202 7.819   10.197 1.00 56.83  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.965 7.015   11.162 1.00 60.17  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.210 6.447   10.498 1.00 64.82  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.210 6.195   9.293  1.00 65.96  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.139 5.859   11.754 1.00 60.17  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.896 4.877   10.751 1.00 61.48  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.843 6.307   12.368 1.00 59.68  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.249 6.188   11.286 1.00 67.36  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.500 5.624   10.770 1.00 69.80  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.438 4.087   10.688 1.00 71.78  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.163 3.470   9.894  1.00 73.29  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.660 6.080   11.660 1.00 71.94  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.500 5.465   12.939 1.00 74.25  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.707 7.596   11.834 1.00 71.79  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.651 3.462   11.568 1.00 71.22  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.508 2.013   11.572 1.00 71.23  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.300 1.607   10.724 1.00 71.14  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.399 2.420   10.482 1.00 71.04  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.358 1.504   12.997 1.00 71.28  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.292 0.358   10.248 1.00 71.12  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.199 -0.131  9.416  1.00 71.41  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.018 -0.593  10.261 1.00 70.60  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.199 -1.193  11.322 1.00 71.14  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.672 -1.274  8.498  1.00 73.66  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.038 -1.256  7.108  1.00 78.76  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.649 -0.180  6.232  1.00 85.91  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.866 -0.130  6.028  1.00 88.89  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.824 0.710   5.686  1.00 86.42  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.821 -0.314  9.766  1.00 68.93  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.563 -0.727  10.377 1.00 67.72  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.955 -1.876  9.595  1.00 65.52  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.172 -1.988  8.383  1.00 65.64  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.178 -2.722  10.260 1.00 63.64  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.626 -3.898  9.584  1.00 62.09  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.110 -4.003  9.616  1.00 59.13  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.578 -5.048  9.218  1.00 59.47  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.278 -5.159  10.127 1.00 63.92  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.039 -5.297  9.743  1.00 71.08  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.410 -2.940  10.062 1.00 55.56  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.960 -2.978  10.099 1.00 53.14  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.420 -2.980  8.688  1.00 50.58  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.896 -2.246  7.825  1.00 51.21  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.370 -1.806  10.922 1.00 54.34  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.513 -1.996  12.418 1.00 57.64  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.578 -3.159  12.860 1.00 59.20  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.571 -0.978  13.148 1.00 58.46  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.464 -3.834  8.444  1.00 47.91  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.809 -3.924  7.156  1.00 46.33  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.568 -3.055  7.237  1.00 43.93  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.787 -3.220  8.170  1.00 44.46  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.450 -5.394  6.875  1.00 47.90  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.641 -6.060  6.460  1.00 50.06  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.387 -5.545  5.793  1.00 47.69  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.382 -2.138  6.292  1.00 41.31  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.186 -1.311  6.259  1.00 39.45  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.159 -2.048  5.410  1.00 39.03  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.497 -2.543  4.326  1.00 39.75  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.471 0.087   5.644  1.00 38.71  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.687 0.781   6.307  1.00 39.31  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.219 0.970   5.648  1.00 38.10  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.558 0.988   7.834  1.00 40.48  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.919 -2.122  5.876  1.00 37.80  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.845 -2.733  5.102  1.00 37.25  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.460 -1.781  3.941  1.00 37.83  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.477 -0.560  4.079  1.00 37.81  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.639 -2.996  5.988  1.00 36.06  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.132 -2.350  2.806  1.00 38.38  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.694 -1.635  1.618  1.00 39.35  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.378 -2.327  1.278  1.00 40.36  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.372 -3.304  0.531  1.00 42.01  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.747 -1.802  0.514  1.00 40.85  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.113 -1.163  0.849  1.00 41.50  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.058 0.314   1.275  1.00 42.16  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.405 0.792   1.586  1.00 41.50  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.685 1.924   2.220  1.00 40.20  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.711 2.729   2.615  1.00 37.00  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.943 2.259   2.465  1.00 40.60  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.273 -1.877  1.896  1.00 39.38  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.994 -2.582  1.821  1.00 39.25  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.830  -1.640  2.223  1.00 40.48  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.054 -0.509  2.647  1.00 39.91  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.072 -3.752  2.806  1.00 39.38  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.161 -3.230  4.557  1.00 39.84  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.587  -2.180  2.234  1.00 41.61  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.407  -1.472  2.735  1.00 42.20  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.757  -2.273  3.897  1.00 41.63  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.534  -2.271  4.039  1.00 42.28  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.396  -1.167  1.612  1.00 44.69  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.522  -2.323  1.167  1.00 54.70  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.892  -3.494  1.433  1.00 55.94  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.455  -2.061  0.571  1.00 60.55  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.578  -2.964  4.713  1.00 39.97  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.131  -3.751  5.866  1.00 38.03  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.347  -2.870  6.833  1.00 35.28  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.734  -1.737  7.062  1.00 34.65  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.336  -4.365  6.579  1.00 38.09  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.959  -5.897  5.845  1.00 37.37  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.263  -3.375  7.382  1.00 33.61  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.513  -2.674  8.426  1.00 32.68  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.435  -3.465  9.723  1.00 31.40  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.560  -3.197  10.531 1.00 31.49  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.110  -2.252  7.968  1.00 33.93  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.059  -0.931  7.194  1.00 36.26  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.645  -0.616  6.764  1.00 38.85  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.298  -0.721  5.589  1.00 41.03  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.787  -0.263  7.717  1.00 37.80  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.307  -4.485  9.902  1.00 30.14  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.459  -5.319  11.098 1.00 29.30  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.960  -5.444  11.347 1.00 26.75  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.769  -5.444  10.406 1.00 26.29  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.799  -6.729  10.975 1.00 31.60  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.573  -7.517  10.068 1.00 32.89  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.331  -6.679  10.502 1.00 32.07  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.315  -5.574  12.604 1.00 25.07  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.710  -5.639  12.995 1.00 24.51  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.870  -5.767  14.496 1.00 24.09  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.888  -5.998  15.203 1.00 24.34  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.120 -5.626  14.979 1.00 23.42  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.540 -5.757  16.378 1.00 23.74  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.432 -4.565  16.759 1.00 24.29  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.346 -4.221  16.009 1.00 24.69  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.259 -7.120  16.628 1.00 24.60  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.735 -7.243  18.071 1.00 25.53  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.335 -8.281  16.303 1.00 26.28  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.142 -3.912  17.883 1.00 24.58  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.934 -2.773  18.326 1.00 25.36  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.495 -2.986  19.763 1.00 26.42  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.848 -3.643  20.583 1.00 26.25  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.121 -1.457  18.236 1.00 24.89  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.170 -1.218  19.395 1.00 26.14  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.932  -1.843  19.443 1.00 26.69  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.491 -0.334  20.417 1.00 27.95  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.030  -1.579  20.463 1.00 27.90  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.603  -0.080  21.464 1.00 28.82  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.380  -0.728  21.493 1.00 29.21  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.470  -0.501  22.490 1.00 30.14  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.663 -2.402  20.057 1.00 27.42  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.230 -2.516  21.382 1.00 30.42  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.739 -1.363  22.289 1.00 30.69  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.810 -0.195  21.903 1.00 28.93  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.758 -2.600  21.343 1.00 32.24  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.342 -2.724  22.730 1.00 34.68  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.104 -3.848  23.504 1.00 35.89  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.078 -1.688  23.293 1.00 36.90  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.622 -3.965  24.784 1.00 37.99  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.591 -1.786  24.583 1.00 38.54  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.351 -2.924  25.329 1.00 40.00  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.816 -3.024  26.616 1.00 43.50  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.207 -1.711  23.480 1.00 32.22  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.696 -0.723  24.447 1.00 33.49  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.615 -0.691  25.676 1.00 35.12  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.497 -1.586  26.519 1.00 34.82  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.261 -1.076  24.830 1.00 34.09  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.546 -0.025  26.117 1.00 36.27  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.569 0.282   25.753 1.00 36.00  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.509 0.351   26.874 1.00 38.45  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.835 0.434   28.224 1.00 39.21  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.279 -0.264  29.130 1.00 40.87  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.519 1.496   26.748 1.00 42.00  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.969 2.619   26.080 1.00 47.66  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.739 1.205   28.346 1.00 38.91  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.976 1.367   29.594 1.00 40.22  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.380 0.051   30.124 1.00 41.25  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.990 -0.013  31.291 1.00 41.72  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.906 2.447   29.458 1.00 40.32  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.859 2.070   28.577 1.00 40.31  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.340 -0.996  29.287 1.00 40.15  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.896 -2.296  29.752 1.00 40.42  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.979 -3.374  29.622 1.00 42.10  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.732 -4.523  30.004 1.00 42.76  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.646 -2.716  28.980 1.00 40.58  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.411  -1.920  29.328 1.00 42.57  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.954  -2.170  30.757 1.00 45.25  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.701  -1.467  31.008 1.00 48.77  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.614  -0.225  31.474 1.00 50.98  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.713  0.454   31.790 1.00 50.27  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.428  0.353   31.618 1.00 51.49  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.155 -3.044  29.017 1.00 42.24  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.221 -4.008  28.698 1.00 41.96  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.632 -5.202  27.902 1.00 40.10  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.962 -6.375  28.157 1.00 39.51  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.981 -4.463  29.956 1.00 43.99  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.945 -3.434  30.544 1.00 50.03  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.771 -4.099  31.628 1.00 57.40  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.200 -3.159  32.663 1.00 64.97  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.427 -3.485  33.933 1.00 69.56  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.243 -4.733  34.350 1.00 69.10  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.815 -2.561  34.802 1.00 71.52  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.690 -4.892  26.975 1.00 38.31  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.960 -5.923  26.215 1.00 36.84  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.710 -5.490  24.759 1.00 34.04  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.500 -4.301  24.490 1.00 34.05  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.560 -6.123  26.838 1.00 38.62  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.340 -7.377  27.658 1.00 43.93  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.875  -7.401  28.122 1.00 49.96  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.492  -8.623  28.927 1.00 55.38  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.596  -8.391  30.407 1.00 57.91  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.615 -6.472  23.869 1.00 31.69  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.236 -6.298  22.467 1.00 30.36  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.742 -6.612  22.383 1.00 29.45  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.241 -7.534  23.071 1.00 30.06  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.986 -7.286  21.576 1.00 30.33  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.453 -7.040  21.499 1.00 30.61  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.010 -6.313  20.461 1.00 31.56  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.439 -7.456  22.320 1.00 31.03  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.310 -6.303  20.690 1.00 31.56  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.614 -6.973  21.798 1.00 31.96  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.028 -5.836  21.590 1.00 27.39  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.591  -6.014  21.438 1.00 27.27  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.186  -6.071  19.958 1.00 26.90  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.610  -5.226  19.182 1.00 25.66  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.837  -4.841  22.086 1.00 27.57  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.886  -4.786  23.593 1.00 29.05  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.172  -5.693  24.366 1.00 30.36  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.581  -3.780  24.248 1.00 30.48  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.191  -5.632  25.760 1.00 31.65  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.584  -3.689  25.640 1.00 31.22  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.876  -4.610  26.389 1.00 32.86  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.886  -4.530  27.756 1.00 36.33  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.320  -7.042  19.574 1.00 27.47  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.793  -7.049  18.190 1.00 27.71  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.726  -5.947  18.027 1.00 28.16  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.954  -5.700  18.969 1.00 28.56  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.165  -8.440  18.044 1.00 28.27  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.795  -8.839  19.459 1.00 28.86  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.728  -8.112  20.417 1.00 27.00  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.713  -5.252  16.872 1.00 27.36  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.756  -4.178  16.610 1.00 28.44  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.239  -4.165  15.175 1.00 29.37  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.921  -4.613  14.251 1.00 29.99  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.357  -2.761  16.917 1.00 28.91  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.528  -2.524  18.409 1.00 29.36  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.655  -2.529  16.155 1.00 29.38  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.051  -3.586  14.979 1.00 29.32  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.502  -3.243  13.674 1.00 30.01  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.700  -1.730  13.673 1.00 30.13  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.499  -1.086  14.716 1.00 30.70  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.007  -3.539  13.573 1.00 32.05  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.813  -4.906  13.262 1.00 36.74  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.197  -1.178  12.577 1.00 29.39  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.450  0.258   12.525 1.00 29.60  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.904  0.886   11.228 1.00 31.96  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.680  0.182   10.238 1.00 32.30  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.933  0.568   12.791 1.00 28.25  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.918  -0.134  11.890 1.00 27.59  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.419  -1.380  12.222 1.00 27.21  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.368  0.473   10.715 1.00 27.99  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.339  -2.022  11.396 1.00 27.83  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.272  -0.173  9.881  1.00 28.41  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.732  -1.430  10.212 1.00 28.26  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.615  2.200   11.256 1.00 32.81  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.056  2.872   10.095 1.00 34.39  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.121  3.207   9.043  1.00 34.70  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.314  3.015   9.285  1.00 33.97  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.301  4.127   10.531 1.00 36.48  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.185  5.054   11.133 1.00 37.57  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.685  3.659   7.864  1.00 35.75  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.565  4.078   6.770  1.00 37.58  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.207  5.429   7.115  1.00 38.29  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.565  6.252   7.765  1.00 38.48  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.742  4.219   5.461  1.00 40.10  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.095  2.903   5.033  1.00 46.20  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.861  2.857   3.518  1.00 52.81  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.831  1.438   3.023  1.00 59.25  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 0.460  1.031   2.599  1.00 64.08  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.455  5.696   6.691  1.00 38.95  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.082  6.993   7.024  1.00 39.81  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.234  8.198   6.617  1.00 40.82  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.779  8.299   5.474  1.00 40.66  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.434  6.935   6.314  1.00 40.60  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.722  5.469   6.188  1.00 41.10  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.374  4.836   5.927  1.00 38.86  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.968  9.082   7.581  1.00 41.68  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.103  10.229  7.344  1.00 43.51  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.462  11.457  8.204  1.00 43.77  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.344  11.370  9.061  1.00 43.22  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.648  9.818   7.565  1.00 46.38  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.377  9.593   8.941  1.00 50.56  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.796  12.614  7.936  1.00 44.20  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.972  13.881  8.655  1.00 45.41  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.031  13.830  9.843  1.00 47.08  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.820  13.849  9.636  1.00 47.59  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.560  15.082  7.763  1.00 45.48  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.648  15.792  6.964  1.00 46.72  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 4.041  16.838  6.068  1.00 47.99  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.622  16.493  7.869  1.00 46.89  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.565  13.789  11.073 1.00 47.71  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.761  13.702  12.287 1.00 49.46  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.125  14.829  13.252 1.00 51.37  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.308  15.062  13.496 1.00 51.12  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.983  12.308  12.957 1.00 50.02  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.431  11.161  12.095 1.00 50.82  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.399  12.246  14.374 1.00 50.34  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.108  9.932   12.332 1.00 52.20  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.114  15.501  13.837 1.00 52.72  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.363  16.566  14.806 1.00 54.46  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.058  16.051  16.085 1.00 55.00  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.664  15.025  16.632 1.00 55.27  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.047  17.273  15.175 1.00 55.17  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.231  18.481  16.056 1.00 55.81  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.710  19.667  15.540 1.00 56.87  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.928  18.428  17.402 1.00 56.83  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.869  20.783  16.353 1.00 57.65  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.074  19.554  18.209 1.00 57.57  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.560  20.714  17.684 1.00 57.11  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.091  16.773  16.550 1.00 55.08  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.858  16.464  17.754 1.00 55.95  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.966  17.733  18.639 1.00 57.70  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.360  18.814  18.162 1.00 57.75  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.265  15.869  17.436 1.00 55.96  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.036  15.570  18.716 1.00 56.26  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.168  14.617  16.576 1.00 56.00  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.623  17.585  19.932 1.00 58.64  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.654  18.653  20.928 1.00 59.86  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.059  19.207  21.196 1.00 59.44  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.052  18.519  20.958 1.00 59.32  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.033  18.152  22.230 1.00 64.11  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.528  18.013  22.162 1.00 71.92  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.847  18.757  23.290 1.00 81.06  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.100  19.976  23.423 1.00 83.44  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.065  18.128  24.040 1.00 84.04  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.137  20.438  21.722 1.00 58.79  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.408  21.107  22.014 1.00 58.90  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.250  20.387  23.071 1.00 58.59  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.707  19.682  23.908 1.00 59.35  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.155  22.544  22.441 1.00 58.97  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.571  20.592  23.042 1.00 57.49  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.540 19.979  23.958 1.00 57.03  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.775 20.907  24.115 1.00 57.15  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.819 21.968  23.472 1.00 56.68  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.955 18.599  23.432 1.00 57.07  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.335 18.605  22.063 1.00 57.62  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.775 20.544  24.974 1.00 57.26  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.980 21.413  25.081 1.00 57.79  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.837 21.397  23.784 1.00 55.37  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.756 22.209  23.641 1.00 55.64  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.839 21.113  26.348 1.00 62.28  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.825 19.959  26.186 1.00 70.29  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 16.477 19.449  27.461 1.00 77.83  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.703 20.271  28.378 1.00 78.52  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 16.770 18.232  27.536 1.00 80.12  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.472 20.511  22.825 1.00 52.86  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.132 20.251  21.558 1.00 50.33  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.414 20.873  20.354 1.00 47.68  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.092 21.327  19.441 1.00 47.78  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.248 18.726  21.343 1.00 49.95  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.778 17.984  22.544 1.00 50.08  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.120 18.046  22.885 1.00 50.83  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.938 17.222  23.341 1.00 51.18  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.614 17.369  23.994 1.00 51.91  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.418 16.538  24.449 1.00 52.08  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.760 16.609  24.772 1.00 53.31  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.240 15.930  25.876 1.00 55.55  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.071 20.828  20.305 1.00 45.22  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.333 21.371  19.159 1.00 43.72  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.099 22.141  19.563 1.00 44.39  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.384 21.708  20.465 1.00 44.55  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.815 20.243  18.235 1.00 41.40  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.865 19.338  17.655 1.00 39.01  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.983 18.019  18.076 1.00 37.89  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.712 19.780  16.646 1.00 38.01  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.925 17.167  17.520 1.00 37.62  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.675 18.943  16.101 1.00 37.60  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.772 17.634  16.534 1.00 37.43  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.748 16.825  16.028 1.00 35.72  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.723 23.178  18.792 1.00 44.50  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.408  23.806  19.029 1.00 44.98  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.289  22.858  18.517 1.00 45.50  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.595  21.907  17.791 1.00 44.87  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.489  25.087  18.193 1.00 45.69  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.402 24.715  17.047 1.00 45.77  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.407 23.739  17.604 1.00 43.87  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.997  23.111  18.846 1.00 45.95  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.910  22.249  18.330 1.00 46.58  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.883  22.319  16.778 1.00 45.85  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.004  23.406  16.220 1.00 45.78  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.571  22.674  18.911 1.00 47.18  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.821  21.158  16.092 1.00 44.97  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.928  21.101  14.624 1.00 44.17  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.423  19.737  14.049 1.00 44.26  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.086  18.827  14.808 1.00 44.51  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.442  21.271  14.263 1.00 43.66  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.255  19.965  14.487 1.00 42.71  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.634  20.101  15.093 1.00 42.15  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.527 19.013  14.661 1.00 40.97  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.551 17.797  15.208 1.00 38.45  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.386 16.873  14.749 1.00 35.04  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.744  17.500  16.222 1.00 36.88  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.470  19.575  12.708 1.00 43.86  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.171  18.307  12.048 1.00 43.83  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.490  17.573  11.785 1.00 40.33  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.411  18.160  11.214 1.00 40.01  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.475  18.550  10.705 1.00 45.89  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.014  18.881  10.869 1.00 49.11  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.089  17.892  11.159 1.00 51.40  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.568  20.192  10.799 1.00 51.16  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.744  18.190  11.333 1.00 53.23  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.228  20.509  10.992 1.00 53.15  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.319  19.503  11.268 1.00 55.19  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.013 19.800  11.452 1.00 58.98  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.601  16.321  12.230 1.00 37.25  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.800  15.530  11.967 1.00 34.65  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.500  14.621  10.785 1.00 33.14  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.505  13.908  10.806 1.00 34.17  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.246  14.701  13.192 1.00 34.43  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.511  13.849  12.908 1.00 33.72  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.205 13.370  14.164 1.00 36.25  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.379 14.129  15.137 1.00 37.17  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.632 12.093  14.164 1.00 33.02  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.316  14.663  9.748  1.00 30.89  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.102  13.839  8.554  1.00 29.92  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.828  12.495  8.665  1.00 29.57  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.730  12.339  9.513  1.00 29.63  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.600  14.578  7.321  1.00 30.49  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.985  14.814  7.460  1.00 32.62  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.424  11.533  7.815  1.00 28.55  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.005  10.196  7.752  1.00 28.44  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.854  9.444   9.091  1.00 28.05  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.687  8.625   9.442  1.00 28.20  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.474 10.281  7.272  1.00 28.72  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.604 10.871  5.891  1.00 30.87  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.622 10.068  4.755  1.00 33.10  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.629 12.171  5.501  1.00 31.77  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.719 10.904  3.726  1.00 33.58  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.712 12.177  4.125  1.00 32.70  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.781  9.736   9.824  1.00 28.37  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.518  9.177   11.148 1.00 28.84  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.482  8.055   11.076 1.00 28.87  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.498  8.175   10.346 1.00 30.02  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.054  10.310  12.102 1.00 28.75  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.820  9.939   13.566 1.00 30.74  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.068  9.349   14.194 1.00 30.98  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.333  11.156  14.380 1.00 32.02  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.716  6.964   11.811 1.00 28.39  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.823  5.802   11.833 1.00 28.93  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.335  5.524   13.245 1.00 30.15  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.160  5.368   14.148 1.00 30.96  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.557  4.564   11.277 1.00 29.31  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.053  4.764   9.849  1.00 30.83  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.158  3.432   9.303  1.00 34.32  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.474  3.607   10.427 1.00 26.88  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.014  5.430   13.455 1.00 30.40  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.510  5.130   14.802 1.00 31.03  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.092  3.660   14.962 1.00 30.90  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.587  3.044   14.024 1.00 29.92  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.356  6.066   15.234 1.00 31.90  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.652  7.574   15.356 1.00 33.94  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.458  8.305   15.955 1.00 35.15  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.828  7.839   16.245 1.00 34.38  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.302  3.131   16.166 1.00 31.62  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.922  1.798   16.623 1.00 33.04  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.325  1.913   18.031 1.00 34.55  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.652  2.829   18.775 1.00 34.75  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.150  0.900   16.686 1.00 32.67  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.465  0.972   18.392 1.00 35.10  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.933  0.827   19.733 1.00 36.57  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.013  0.011   20.468 1.00 37.11  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.416  -1.061  20.025 1.00 36.95  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.437 0.087   19.721 1.00 37.73  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.878 -0.299  21.128 1.00 38.34  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.498 0.937   19.024 1.00 37.71  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.559  0.599   21.506 1.00 37.29  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.637  -0.001  22.271 1.00 37.82  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.179  0.960   23.307 1.00 37.96  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.940  2.173   23.237 1.00 38.87  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.912  0.427   24.278 1.00 36.85  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.498  1.228   25.320 1.00 36.78  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.802  1.953   24.919 1.00 36.16  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.700  1.370   24.323 1.00 35.71  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.703  0.387   26.586 1.00 38.25  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.426  1.126   27.662 1.00 41.30  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.807  2.114   28.384 1.00 44.20  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.725  1.055   28.027 1.00 42.95  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.742  2.613   29.178 1.00 45.40  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.916  2.001   28.986 1.00 45.28  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.912  3.213   25.336 1.00 36.41  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.103  4.028   25.180 1.00 38.54  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.098  5.165   26.222 1.00 41.07  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.042  5.589   26.677 1.00 41.65  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.193  4.605   23.777 1.00 39.15  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.026  5.354   23.495 1.00 41.78  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.282  5.628   26.604 1.00 42.14  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.520  6.700   27.559 1.00 44.61  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.712 7.503   27.070 1.00 46.65  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.561 6.919   26.396 1.00 47.50  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.891  6.121   28.926 1.00 47.83  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.723  5.636   29.751 1.00 54.41  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.182  4.765   30.905 1.00 55.78  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.072 5.204   31.663 1.00 55.95  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.680  3.630   31.028 1.00 55.57  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.885 8.810   27.421 1.00 47.36  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.123 9.510   26.986 1.00 47.60  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.299 8.785   27.653 1.00 47.62  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.230 8.405   28.839 1.00 49.61  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.925 10.962  27.442 1.00 48.26  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.842 10.934  28.463 1.00 48.78  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.024 9.667   28.263 1.00 47.02  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.282 8.470   26.841 1.00 45.22  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.378 7.566   27.173 1.00 43.04  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.367 6.403   26.173 1.00 40.43  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.400 5.786   25.884 1.00 40.29  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.176 6.099   25.611 1.00 38.29  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.009 5.070   24.613 1.00 36.53  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.425 5.485   23.213 1.00 34.24  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.631 4.613   22.387 1.00 33.09  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.588 4.516   24.612 1.00 37.05  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.377 3.615   25.796 1.00 39.31  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.296 2.859   26.125 1.00 38.19  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.310 3.692   26.406 1.00 41.07  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.608 6.787   22.951 1.00 33.51  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.046 7.263   21.618 1.00 33.05  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.360 6.606   21.215 1.00 31.92  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.228 6.476   22.070 1.00 32.91  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.169 8.784   21.623 1.00 33.60  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.575 9.632   21.621 1.00 37.13  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.483 6.156   19.976 1.00 30.59  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.704 5.484   19.544 1.00 30.29  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.558 3.975   19.462 1.00 30.58  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.307 3.314   18.729 1.00 31.68  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.538 3.425   20.126 1.00 28.78  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.226 2.004   20.009 1.00 27.46  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.882 1.629   18.563 1.00 25.86  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.068 2.280   17.912 1.00 24.16  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.520 0.583   18.050 1.00 25.66  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.333 0.134   16.704 1.00 26.48  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.025 -0.628  16.507 1.00 26.75  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.667 -1.492  17.330 1.00 28.01  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.582 -0.703  16.286 1.00 28.59  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.791 0.224   15.988 1.00 29.88  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.293 -1.645  15.095 1.00 29.39  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.086 -0.534  15.869 1.00 30.66  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.360 -0.349  15.367 1.00 25.41  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.188 -1.058  14.870 1.00 25.48  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.702 -1.871  13.642 1.00 26.56  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.413 -1.319  12.793 1.00 25.60  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.093 -0.072  14.439 1.00 25.24  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.933 -0.683  13.605 1.00 26.52  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.111 -1.700  14.435 1.00 27.06  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.007 0.421   13.081 1.00 27.14  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.383 -3.177  13.586 1.00 27.18  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.840 -4.094  12.572 1.00 28.54  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.704 -4.961  12.056 1.00 29.46  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.856 -5.377  12.835 1.00 28.66  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.822 -5.094  13.205 1.00 31.25  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.256 -4.662  13.302 1.00 37.10  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.100 -5.751  13.962 1.00 42.43  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.530 -5.452  13.830 1.00 47.16  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.275 -5.803  12.782 1.00 48.72  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 20.555 -5.447  12.720 1.00 48.46  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 18.738 -6.489  11.775 1.00 47.19  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.783 -5.363  10.786 1.00 30.47  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.879 -6.348  10.204 1.00 32.16  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.820 -7.502  9.732  1.00 34.81  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.026 -7.459  10.018 1.00 34.80  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.113 -5.738  9.031  1.00 32.72  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.183 -5.078  7.738  1.00 31.00  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.292 -8.525  9.018  1.00 36.82  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.140 -9.615  8.499  1.00 39.05  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.204 -9.107  7.491  1.00 40.14  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.164 -9.826  7.190  1.00 41.38  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.266 -10.652 7.774  1.00 41.97  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.581 -10.067 6.536  1.00 47.34  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.562 -11.003 5.968  1.00 54.39  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.359  -10.710 5.965  1.00 56.77  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.030 -12.137 5.447  1.00 54.82  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.997 -7.910  6.921  1.00 39.19  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.901 -7.374  5.906  1.00 38.75  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.039 -6.536  6.463  1.00 36.49  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.942 -6.191  5.699  1.00 37.30  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.131 -6.559  4.843  1.00 40.75  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.051 -7.314  4.133  1.00 46.30  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.743 -6.871  4.142  1.00 48.95  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.118 -8.459  3.408  1.00 48.98  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.054 -7.746  3.426  1.00 49.99  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.835 -8.730  2.973  1.00 50.36  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.975 -6.169  7.745  1.00 33.69  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.994 -5.329  8.346  1.00 31.95  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.442 -4.174  9.167  1.00 29.91  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.310 -4.226  9.654  1.00 29.46  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.263 -3.131  9.344  1.00 28.46  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.942 -1.956  10.130 1.00 28.32  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.919 -1.106  9.406  1.00 27.47  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.122 -0.752  8.247  1.00 28.11  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.230 -1.144  10.473 1.00 29.83  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.872 0.211   11.083 1.00 30.64  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.139 -1.928  11.429 1.00 29.82  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.803 -0.821  10.055 1.00 26.13  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.745 0.011   9.490  1.00 26.67  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.925 1.488   9.940  1.00 26.35  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.732 2.434   9.162  1.00 26.37  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.354 -0.550  9.909  1.00 27.87  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.233 0.427   9.559  1.00 29.19  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.099 -1.921  9.284  1.00 27.98  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.279 1.670   11.203 1.00 25.02  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.479 2.999   11.750 1.00 24.74  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.755 2.988   13.241 1.00 24.58  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.091 1.944   13.810 1.00 23.58  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.669 4.169   13.870 1.00 24.42  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.960 4.288   15.296 1.00 24.27  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.867 5.041   16.049 1.00 23.80  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.300 5.992   15.495 1.00 22.99  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.327 4.996   15.521 1.00 25.92  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.447 6.303   14.702 1.00 26.99  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.520 4.068   15.294 1.00 26.67  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.410 7.240   15.285 1.00 28.41  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.639 4.702   17.369 1.00 23.59  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.659 5.408   18.200 1.00 24.11  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.988 6.903   18.233 1.00 24.59  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.153 7.275   18.366 1.00 23.93  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.555 4.840   19.650 1.00 24.95  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.495 5.597   20.449 1.00 25.34  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.238 3.337   19.639 1.00 26.17  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.975 7.752   18.066 1.00 25.82  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.182 9.188   18.027 1.00 27.24  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.135 9.946   18.862 1.00 30.81  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.404 11.066  19.306 1.00 31.33  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.160 9.658   16.569 1.00 26.69  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.251 11.071  16.477 1.00 27.21  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.910  9.399   18.972 1.00 32.95  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.803  9.987   19.750 1.00 35.94  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.005  8.844   20.446 1.00 37.33  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.232  7.675   20.161 1.00 36.67  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.863  10.935  18.893 1.00 38.41  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.817  10.179  18.282 1.00 40.20  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.580  11.727  17.815 1.00 39.51  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.055  9.199   21.296 1.00 39.27  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.172  8.261   21.970 1.00 42.13  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.255  8.958   22.958 1.00 44.71  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.377  10.164  23.187 1.00 44.63  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.348  8.203   23.553 1.00 46.94  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.417  8.756   24.532 1.00 49.67  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.032  8.145   24.485 1.00 52.05  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.504  7.884   23.407 1.00 53.18  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.448  7.897   25.653 1.00 52.48  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.102  7.355   25.821 1.00 53.12  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.136 5.981   25.176 1.00 51.71  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.225 5.715   24.664 1.00 52.94  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.930 8.355   25.357 1.00 56.09  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.897 9.595   26.202 1.00 62.49  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.997 9.513   27.433 1.00 64.98  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.750 10.760  25.563 1.00 63.36  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.837  5.096   25.296 1.00 48.80  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.712  3.762   24.736 1.00 46.97  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.093  3.690   23.269 1.00 44.80  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.921  2.644   22.647 1.00 45.02  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.642  4.785   22.704 1.00 42.54  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.105  4.820   21.329 1.00 41.24  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.627  5.024   21.324 1.00 39.32  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.175  5.635   22.238 1.00 40.77  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.440  5.989   20.543 1.00 41.79  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.098 5.976   20.506 1.00 44.64  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.658 7.348   20.282 1.00 45.30  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.616 4.990   19.481 1.00 45.97  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.296  4.542   20.277 1.00 35.43  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.713  4.750   20.046 1.00 32.21  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.907  5.168   18.576 1.00 31.10  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.290  4.583   17.682 1.00 30.56  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.567  3.521   20.468 1.00 31.10  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.011  2.210   19.911 1.00 31.37  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.045  3.711   20.126 1.00 30.21  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.739  6.182   18.354 1.00 30.28  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.066  6.712   17.040 1.00 30.26  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.488  6.410   16.603 1.00 30.13  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.432  6.548   17.393 1.00 31.16  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.648  6.000   15.326 1.00 28.46  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.930  5.610   14.723 1.00 27.16  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.295 6.492   13.514 1.00 26.25  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.486  6.698   12.610 1.00 26.31  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.899  4.115   14.288 1.00 26.00  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.440  3.131   15.348 1.00 25.75  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.322 2.652   16.303 1.00 25.48  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.154  2.612   15.327 1.00 26.26  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.906  1.729   17.264 1.00 25.48  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.746  1.675   16.269 1.00 26.23  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.624  1.241   17.239 1.00 25.26  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.516 7.007   13.506 1.00 25.58  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.026 7.784   12.405 1.00 26.00  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.487 6.777   11.330 1.00 26.54  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.412 6.009   11.570 1.00 26.76  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.205 8.627   12.884 1.00 26.39  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.822 6.741   10.182 1.00 27.20  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.168 5.807   9.112  1.00 28.41  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.516 6.124   8.487  1.00 29.09  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.871 7.296   8.380  1.00 29.69  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.059 5.810   8.060  1.00 30.16  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.232 4.807   6.954  1.00 35.13  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.160 3.607   7.235  1.00 34.42  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.445 5.233   5.793  1.00 39.62  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.314 5.093   8.150  1.00 29.11  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.600 5.312   7.448  1.00 29.87  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.663 4.564   6.085  1.00 30.14  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.688 4.647   5.398  1.00 30.25  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.852 4.949   8.286  1.00 30.12  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.949 5.801   9.556  1.00 30.95  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.888 3.450   8.610  1.00 30.37  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.616 3.793   5.728  1.00 29.79  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.602 2.965   4.524  1.00 30.34  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.721 3.729   3.194  1.00 31.12  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.193 3.149   2.227  1.00 31.45  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.370 2.056   4.496  1.00 30.47  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.302 1.077   5.659  1.00 30.32  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.005 0.303   5.569  1.00 30.18  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.888 1.132   6.016  1.00 31.42  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.642  0.699   6.161  1.00 32.55  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.329  -0.557  5.856  1.00 32.34  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.696  1.518   6.608  1.00 29.67  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.309 4.992   3.141  1.00 31.72  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.420 5.798   1.925  1.00 33.11  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.837 6.356   1.715  1.00 34.44  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.148 6.803   0.603  1.00 34.67  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.412 6.952   1.938  1.00 34.09  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.618 7.947   3.070  1.00 36.70  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.778 7.506   4.232  1.00 36.67  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.559 9.164   2.807  1.00 37.94  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.691 6.355   2.772  1.00 34.34  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.060 6.878   2.683  1.00 34.79  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.933 5.849   1.997  1.00 36.24  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.723 5.169   2.656  1.00 36.21  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.615 7.246   4.075  1.00 34.00  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.724 8.196   4.872  1.00 34.84  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.222 8.367   6.309  1.00 35.28  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.602 9.530   4.188  1.00 35.41  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.777 5.729   0.654  1.00 37.03  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.465 4.741   -0.184 1.00 38.28  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.981 4.915   -0.196 1.00 40.11  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.708 3.923   -0.386 1.00 40.75  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.937 4.766   -1.639 1.00 38.09  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.426 4.724   -1.898 1.00 38.82  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.145 4.458   -3.411 1.00 39.16  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.735 3.665   -1.055 1.00 39.67  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.455 6.157   0.025  1.00 40.37  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.873 6.508   0.038  1.00 41.62  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.658 5.928   1.208  1.00 44.70  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.884 5.941   1.167  1.00 45.53  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.080 8.033   -0.044 1.00 40.41  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.327 8.837   0.972  1.00 39.06  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.092 9.400   0.827  1.00 39.34  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.783 9.201   2.274  1.00 38.74  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.751 10.093  1.965  1.00 39.42  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.771 9.982   2.873  1.00 39.23  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 23.942 8.926   3.007  1.00 39.38  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.884 10.479  4.168  1.00 39.72  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.060 9.444   4.283  1.00 40.09  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.045 10.216  4.846  1.00 39.90  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.979 5.444   2.258  1.00 46.47  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.658 4.836   3.398  1.00 48.91  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.429 3.570   2.990  1.00 53.35  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.412 3.222   3.642  1.00 53.69  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.637 4.484   4.495  1.00 47.70  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.037 5.665   5.266  1.00 47.11  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.914 5.197   6.182  1.00 46.74  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.095 6.365   6.092  1.00 47.29  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.965 2.872   1.930  1.00 56.38  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.557 1.646   1.412  1.00 59.92  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.638 1.889   0.390  1.00 63.55  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.538 1.062   0.250  1.00 64.47  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.472 0.800   0.756  1.00 62.16  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.623 0.097   1.770  1.00 67.15  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.179 -0.357  2.788  1.00 67.94  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.399 -0.004  1.548  1.00 69.89  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.514 2.967   -0.389 1.00 65.37  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.485 3.274   -1.421 1.00 67.80  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.376 4.432   -0.989 1.00 69.26  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.374 4.720   -1.656 1.00 70.45  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 25.768 3.596   -2.742 1.00 71.48  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 24.854 4.809   -2.664 1.00 77.35  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.697 4.787   -3.647 1.00 85.06  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.134 5.872   -3.923 1.00 87.09  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.345 3.685   -4.132 1.00 87.46  ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BPR B 2 .   ? 10.155 13.826  22.486 1.00 40.45  ? 201 A1BPR A N1  1 
HETATM 1079 N  N3  . A1BPR B 2 .   ? 10.526 9.680   23.150 1.00 42.23  ? 201 A1BPR A N3  1 
HETATM 1080 C  C4  . A1BPR B 2 .   ? 11.264 14.471  23.203 1.00 40.28  ? 201 A1BPR A C4  1 
HETATM 1081 C  C5  . A1BPR B 2 .   ? 9.410  12.805  22.958 1.00 40.48  ? 201 A1BPR A C5  1 
HETATM 1082 C  C6  . A1BPR B 2 .   ? 9.622  12.399  24.404 1.00 41.73  ? 201 A1BPR A C6  1 
HETATM 1083 C  C7  . A1BPR B 2 .   ? 9.030  11.037  24.692 1.00 41.99  ? 201 A1BPR A C7  1 
HETATM 1084 C  C8  . A1BPR B 2 .   ? 7.972  10.899  25.593 1.00 42.02  ? 201 A1BPR A C8  1 
HETATM 1085 C  C10 . A1BPR B 2 .   ? 7.816  8.536   25.161 1.00 42.19  ? 201 A1BPR A C10 1 
HETATM 1086 C  C13 . A1BPR B 2 .   ? 9.917  14.390  21.152 1.00 40.37  ? 201 A1BPR A C13 1 
HETATM 1087 O  O1  . A1BPR B 2 .   ? 8.588  12.230  22.261 1.00 39.98  ? 201 A1BPR A O1  1 
HETATM 1088 C  C3  . A1BPR B 2 .   ? 12.549 14.371  22.400 1.00 40.37  ? 201 A1BPR A C3  1 
HETATM 1089 C  C2  . A1BPR B 2 .   ? 12.343 14.876  20.964 1.00 40.10  ? 201 A1BPR A C2  1 
HETATM 1090 C  C1  . A1BPR B 2 .   ? 11.158 14.175  20.281 1.00 39.87  ? 201 A1BPR A C1  1 
HETATM 1091 C  C   . A1BPR B 2 .   ? 11.002 14.621  18.837 1.00 39.44  ? 201 A1BPR A C   1 
HETATM 1092 O  O   . A1BPR B 2 .   ? 10.557 15.737  18.558 1.00 39.32  ? 201 A1BPR A O   1 
HETATM 1093 N  N   . A1BPR B 2 .   ? 11.349 13.736  17.918 1.00 39.07  ? 201 A1BPR A N   1 
HETATM 1094 C  C12 . A1BPR B 2 .   ? 9.514  9.892   24.025 1.00 42.05  ? 201 A1BPR A C12 1 
HETATM 1095 O  O2  . A1BPR B 2 .   ? 10.546 8.370   22.867 1.00 42.59  ? 201 A1BPR A O2  1 
HETATM 1096 N  N2  . A1BPR B 2 .   ? 9.576  7.713   23.521 1.00 42.70  ? 201 A1BPR A N2  1 
HETATM 1097 C  C11 . A1BPR B 2 .   ? 8.895  8.632   24.270 1.00 42.19  ? 201 A1BPR A C11 1 
HETATM 1098 C  C9  . A1BPR B 2 .   ? 7.373  9.669   25.825 1.00 42.37  ? 201 A1BPR A C9  1 
HETATM 1099 ZN ZN  . ZN    C 3 .   ? 11.057 -5.367  5.621  1.00 36.94  2 202 ZN    A ZN  1 
HETATM 1100 S  S   . DMS   D 4 .   ? 19.657 -0.774  19.643 1.00 73.00  ? 203 DMS   A S   1 
HETATM 1101 O  O   . DMS   D 4 .   ? 18.188 -1.018  19.813 1.00 72.56  ? 203 DMS   A O   1 
HETATM 1102 C  C1  . DMS   D 4 .   ? 20.543 -2.326  19.984 1.00 72.98  ? 203 DMS   A C1  1 
HETATM 1103 C  C2  . DMS   D 4 .   ? 20.284 0.161   21.067 1.00 72.96  ? 203 DMS   A C2  1 
HETATM 1104 O  O   . HOH   E 5 .   ? 22.956 -2.019  4.520  1.00 49.09  ? 301 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 10.858 7.322   4.713  1.00 43.33  ? 302 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 20.144 8.294   18.882 1.00 24.24  ? 303 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.699 21.409  7.880  1.00 37.86  ? 304 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 30.479 20.131  10.665 1.00 52.40  ? 305 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 9.520  17.873  19.605 1.00 48.60  ? 306 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 8.761  1.727   3.004  1.00 35.72  ? 307 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 19.748 22.000  7.751  1.00 44.96  ? 308 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 8.193  -4.589  0.721  1.00 47.38  ? 309 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 6.947  2.904   32.971 1.00 45.02  ? 310 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 0.429  -0.944  16.450 1.00 33.79  ? 311 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 18.119 18.302  16.921 1.00 27.35  ? 312 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 18.211 1.942   23.098 1.00 35.86  ? 313 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 14.689 2.003   23.242 1.00 33.44  ? 314 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 11.181 10.951  11.359 1.00 26.76  ? 315 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 11.087 1.361   33.501 1.00 32.42  ? 316 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 10.197 3.411   33.772 1.00 39.91  ? 317 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 30.182 10.610  19.109 1.00 47.65  ? 318 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 21.597 18.270  18.272 1.00 47.78  ? 319 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 17.630 20.533  9.446  1.00 37.36  ? 320 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 0.327  0.437   24.326 1.00 49.03  ? 321 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 10.156 4.197   3.464  1.00 34.38  ? 322 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 14.915 11.826  24.105 1.00 37.14  ? 323 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 10.959 -5.902  31.811 1.00 38.37  ? 324 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 4.096  5.100   25.077 1.00 33.90  ? 325 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 5.196  -2.449  24.410 1.00 37.12  ? 326 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 10.993 14.592  2.557  1.00 46.08  ? 327 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 12.832 18.364  26.877 1.00 51.87  ? 328 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 29.982 4.182   3.868  1.00 58.15  ? 329 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 19.258 23.153  15.367 1.00 34.26  ? 330 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 12.803 9.773   9.532  1.00 25.73  ? 331 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 30.768 20.207  16.782 1.00 41.86  ? 332 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 6.463  -6.773  29.058 1.00 54.03  ? 333 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 24.669 6.781   20.626 1.00 49.21  ? 334 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 14.948 -5.123  17.139 1.00 35.73  ? 335 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 4.324  -6.094  6.531  1.00 40.84  ? 336 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 11.537 20.717  12.396 1.00 35.40  ? 337 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 34.984 8.480   7.480  1.00 48.09  ? 338 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 5.653  1.098   7.123  1.00 45.62  ? 339 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 10.719 16.474  5.009  1.00 47.24  ? 340 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 18.246 11.804  1.611  1.00 44.41  ? 341 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 7.233  -5.917  2.767  1.00 51.60  ? 342 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 5.283  7.544   28.310 1.00 38.85  ? 343 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 1.641  -3.014  17.677 1.00 34.75  ? 344 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 4.237  11.702  19.102 1.00 53.42  ? 345 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 22.413 18.501  6.070  1.00 28.17  ? 346 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 14.010 -12.146 4.534  1.00 62.25  ? 347 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 6.586  11.727  5.223  1.00 38.99  ? 348 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 15.837 -5.316  1.886  1.00 33.68  ? 349 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 14.180 14.063  3.712  1.00 42.31  ? 350 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 22.355 8.271   20.734 1.00 36.53  ? 351 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 2.604  2.046   27.615 1.00 38.66  ? 352 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 7.950  25.144  14.202 1.00 59.73  ? 353 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 12.231 -8.640  13.182 1.00 45.48  ? 354 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 8.966  -8.398  9.506  1.00 45.97  ? 355 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? -1.994 0.301   4.734  1.00 113.60 ? 356 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 20.765 21.392  17.617 1.00 50.20  ? 357 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 1.889  12.232  5.194  1.00 54.08  ? 358 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 2.134  14.935  19.956 1.00 41.68  ? 359 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 27.235 20.964  19.611 1.00 44.91  ? 360 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 15.610 23.261  14.642 1.00 69.27  ? 361 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 9.515  20.822  10.510 1.00 47.12  ? 362 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 4.923  -2.265  28.966 1.00 64.97  ? 363 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 19.228 8.248   -1.939 1.00 41.32  ? 364 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? -2.415 -5.120  15.004 1.00 55.52  ? 365 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 3.799  -3.853  22.217 1.00 59.09  ? 366 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? -1.385 14.145  12.236 1.00 38.19  ? 367 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 11.906 23.052  14.124 1.00 42.60  ? 368 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 9.598  -9.392  12.623 1.00 36.65  ? 369 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 8.254  6.211   2.750  1.00 51.77  ? 370 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 9.779  24.070  12.934 1.00 56.84  ? 371 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   ? 1.0735 0.2605 0.3988 -0.0560 -0.2798 0.0214  7   SER   A N   
2    C CA  . SER   A 1   ? 1.0283 0.2670 0.4492 -0.0562 -0.3055 0.0338  7   SER   A CA  
3    C C   . SER   A 1   ? 0.9502 0.2632 0.4616 -0.0411 -0.2874 0.0337  7   SER   A C   
4    O O   . SER   A 1   ? 0.9610 0.2778 0.4577 -0.0368 -0.2724 0.0288  7   SER   A O   
5    C CB  . SER   A 1   ? 1.0761 0.2674 0.4898 -0.0825 -0.3646 0.0555  7   SER   A CB  
6    O OG  . SER   A 1   ? 1.1307 0.3092 0.5425 -0.0912 -0.3834 0.0649  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.8759 0.2390 0.4740 -0.0346 -0.2863 0.0391  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.8210 0.2396 0.4954 -0.0230 -0.2636 0.0385  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.7621 0.2238 0.4937 -0.0124 -0.2380 0.0338  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.7695 0.2304 0.4727 -0.0086 -0.2270 0.0251  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.7036 0.1965 0.5138 -0.0086 -0.2259 0.0402  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.6771 0.1984 0.5370 -0.0014 -0.1977 0.0365  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.6594 0.2017 0.5594 0.0042  -0.1613 0.0324  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.6548 0.1951 0.5680 0.0031  -0.1636 0.0373  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.6579 0.1772 0.5842 -0.0066 -0.2205 0.0548  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.6474 0.2016 0.5586 0.0080  -0.1268 0.0233  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.6447 0.2016 0.5793 0.0092  -0.0868 0.0184  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.6454 0.2014 0.6623 0.0110  -0.0693 0.0298  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.6422 0.1998 0.6685 0.0114  -0.0707 0.0306  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.6527 0.2082 0.5234 0.0065  -0.0595 0.0009  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.6641 0.2250 0.4684 0.0061  -0.0770 -0.0058 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.6604 0.2013 0.5336 0.0020  -0.0196 -0.0048 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.6786 0.2416 0.4366 0.0014  -0.0625 -0.0145 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.6453 0.1975 0.7276 0.0127  -0.0497 0.0403  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.6347 0.1838 0.8120 0.0161  -0.0245 0.0551  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.6684 0.1938 0.8404 0.0164  0.0391  0.0433  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.6740 0.1896 0.8624 0.0171  0.0593  0.0451  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.5984 0.1563 0.8745 0.0171  -0.0517 0.0839  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.6002 0.1653 0.8739 0.0105  -0.1168 0.0985  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.6048 0.1736 0.9195 0.0083  -0.1343 0.1106  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.6273 0.1864 0.8401 0.0042  -0.1582 0.0973  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.6214 0.1843 0.9146 -0.0020 -0.1944 0.1224  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.6563 0.2039 0.8422 -0.0061 -0.2141 0.1081  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.6628 0.2105 0.8869 -0.0103 -0.2333 0.1208  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.7162 0.2411 0.9026 -0.0245 -0.2893 0.1317  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.6928 0.2010 0.8309 0.0135  0.0711  0.0306  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.7338 0.2001 0.8447 0.0083  0.1346  0.0182  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.7362 0.1834 0.9122 0.0115  0.1753  0.0259  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.7439 0.1963 0.9040 0.0102  0.1651  0.0230  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.7953 0.2401 0.7801 -0.0051 0.1406  -0.0050 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.8114 0.2745 0.7502 -0.0074 0.1081  -0.0103 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.8358 0.2198 0.7797 -0.0166 0.2046  -0.0163 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.7201 0.1452 0.9784 0.0168  0.2230  0.0381  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.7168 0.1205 1.0563 0.0217  0.2710  0.0495  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.6875 0.1363 1.1166 0.0290  0.2242  0.0718  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.6663 0.1542 1.1569 0.0328  0.1698  0.0919  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.6875 0.1265 1.1094 0.0276  0.2386  0.0677  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.6496 0.1266 1.1503 0.0320  0.1937  0.0886  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.6463 0.1488 1.0530 0.0262  0.1301  0.0751  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.6324 0.1482 1.0550 0.0260  0.1074  0.0806  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.6757 0.1297 1.2415 0.0354  0.2461  0.0962  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.7207 0.1608 1.4303 0.0449  0.2998  0.1228  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.7184 0.1771 1.5049 0.0496  0.2847  0.1430  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.7428 0.1474 1.4978 0.0480  0.3661  0.1257  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.6458 0.1540 0.9619 0.0219  0.1028  0.0598  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.6387 0.1652 0.8692 0.0179  0.0525  0.0480  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.5970 0.1440 0.8130 0.0173  -0.0002 0.0539  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.5829 0.1282 0.8151 0.0182  0.0048  0.0578  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.6847 0.1901 0.7985 0.0106  0.0752  0.0216  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.7147 0.1890 0.8129 0.0062  0.1209  0.0136  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.7156 0.1994 0.8415 0.0086  0.1107  0.0190  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.7614 0.1883 0.8061 -0.0032 0.1742  0.0001  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.7467 0.1973 0.8536 0.0036  0.1540  0.0115  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.8028 0.1876 0.8161 -0.0111 0.2171  -0.0079 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.8033 0.2018 0.8509 -0.0068 0.2078  -0.0021 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.8672 0.2201 0.8811 -0.0153 0.2517  -0.0099 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.5769 0.1356 0.7495 0.0149  -0.0467 0.0524  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.5631 0.1270 0.6922 0.0118  -0.0931 0.0537  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.5747 0.1370 0.6024 0.0111  -0.0976 0.0332  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.5743 0.1368 0.5891 0.0111  -0.0999 0.0301  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.5551 0.1204 0.7373 0.0064  -0.1442 0.0777  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.6149 0.1669 0.7227 -0.0012 -0.1925 0.0763  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.6400 0.1794 0.7955 -0.0134 -0.2468 0.1041  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.7080 0.2188 0.7811 -0.0240 -0.2865 0.1007  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.7469 0.2253 0.7506 -0.0351 -0.3210 0.1020  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.7157 0.1935 0.7250 -0.0361 -0.3240 0.1064  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.7678 0.2070 0.6899 -0.0462 -0.3490 0.0984  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.5801 0.1416 0.5448 0.0107  -0.0948 0.0212  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.5927 0.1551 0.4788 0.0106  -0.0985 0.0077  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.5992 0.1544 0.4506 0.0103  -0.1331 0.0108  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.6114 0.1625 0.4635 0.0090  -0.1420 0.0144  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.6088 0.1712 0.4496 0.0080  -0.0716 -0.0043 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.6212 0.1884 0.4051 0.0071  -0.0760 -0.0111 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.6037 0.1533 0.4663 0.0035  -0.0326 -0.0074 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.5985 0.1450 0.4146 0.0104  -0.1495 0.0093  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.6287 0.1505 0.3953 0.0076  -0.1756 0.0109  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.6454 0.1618 0.3543 0.0124  -0.1643 0.0013  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.6404 0.1734 0.3568 0.0159  -0.1483 -0.0026 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.6405 0.1375 0.4231 -0.0014 -0.2123 0.0246  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.6313 0.1295 0.4762 -0.0079 -0.2323 0.0413  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.6315 0.1356 0.4397 -0.0005 -0.2102 0.0259  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.6607 0.1469 0.3130 0.0115  -0.1721 -0.0002 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.6785 0.1533 0.2878 0.0173  -0.1568 -0.0054 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.6996 0.1577 0.3074 0.0142  -0.1694 -0.0034 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.7233 0.1529 0.3274 0.0038  -0.1978 0.0030  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.7175 0.1491 0.2648 0.0163  -0.1547 -0.0070 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.7425 0.1858 0.2871 0.0194  -0.1422 -0.0082 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.7633 0.1954 0.3054 0.0129  -0.1578 -0.0060 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.7242 0.1892 0.2729 0.0281  -0.1164 -0.0090 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.6846 0.1606 0.2998 0.0208  -0.1526 -0.0062 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.6896 0.1517 0.3038 0.0186  -0.1618 -0.0050 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.7569 0.1577 0.3080 0.0112  -0.1765 -0.0044 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.7769 0.1542 0.3279 0.0003  -0.2037 0.0010  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.6512 0.1386 0.2765 0.0269  -0.1399 -0.0072 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.6442 0.1257 0.2788 0.0253  -0.1471 -0.0062 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.6557 0.1503 0.2860 0.0335  -0.1260 -0.0065 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.6571 0.1515 0.2979 0.0332  -0.1285 -0.0060 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.6964 0.1551 0.3062 0.0328  -0.1328 -0.0065 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.7092 0.1200 0.2673 0.0301  -0.1354 -0.0081 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.6887 0.1515 0.3110 0.0334  -0.1329 -0.0058 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.7953 0.1631 0.2913 0.0142  -0.1593 -0.0082 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.8644 0.1545 0.2796 0.0043  -0.1653 -0.0095 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.9033 0.1484 0.2864 -0.0158 -0.2054 -0.0035 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.9560 0.1264 0.2646 -0.0318 -0.2214 -0.0023 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.9025 0.1614 0.2697 0.0135  -0.1261 -0.0143 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.9289 0.1844 0.2838 0.0137  -0.1197 -0.0146 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.8967 0.2181 0.3123 0.0248  -0.1073 -0.0129 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.9846 0.1724 0.2665 0.0022  -0.1234 -0.0163 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.9240 0.2230 0.3103 0.0220  -0.1037 -0.0137 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.9723 0.1914 0.2783 0.0089  -0.1123 -0.0158 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.8832 0.1684 0.3214 -0.0175 -0.2231 0.0025  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.9135 0.1652 0.3417 -0.0369 -0.2658 0.0140  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.8897 0.1771 0.4031 -0.0432 -0.2981 0.0286  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.8933 0.1650 0.4257 -0.0588 -0.3368 0.0444  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.9095 0.1724 0.3406 -0.0344 -0.2603 0.0136  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.9691 0.1881 0.3195 -0.0309 -0.2308 0.0033  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.9586 0.1905 0.3181 -0.0304 -0.2310 0.0047  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 1.0461 0.1649 0.2881 -0.0497 -0.2423 0.0029  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.8607 0.1953 0.4316 -0.0315 -0.2810 0.0259  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.8357 0.2037 0.4954 -0.0349 -0.3003 0.0398  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.8687 0.1898 0.5186 -0.0572 -0.3503 0.0576  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.9080 0.1729 0.4754 -0.0676 -0.3604 0.0533  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.8067 0.2191 0.5085 -0.0202 -0.2685 0.0315  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.8549 0.1943 0.5902 -0.0663 -0.3813 0.0799  24  THR   A N   
135  C CA  . THR   A 18  ? 0.8887 0.1893 0.6373 -0.0916 -0.4390 0.1053  24  THR   A CA  
136  C C   . THR   A 18  ? 0.8897 0.2089 0.6911 -0.0905 -0.4407 0.1114  24  THR   A C   
137  O O   . THR   A 18  ? 0.8679 0.2296 0.6946 -0.0697 -0.3954 0.0951  24  THR   A O   
138  C CB  . THR   A 18  ? 0.8615 0.1804 0.7010 -0.1007 -0.4709 0.1328  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.8007 0.1876 0.7639 -0.0822 -0.4393 0.1379  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.8908 0.1946 0.6841 -0.1013 -0.4688 0.1274  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.9186 0.2032 0.7368 -0.1153 -0.4959 0.1369  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.9160 0.2200 0.7979 -0.1157 -0.5012 0.1469  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.8427 0.2209 0.8713 -0.0974 -0.4726 0.1579  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.8177 0.2292 0.8882 -0.0826 -0.4377 0.1494  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.9727 0.2225 0.8514 -0.1505 -0.5741 0.1782  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 1.1239 0.2839 0.8487 -0.1728 -0.5982 0.1675  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 1.1869 0.3260 0.8509 -0.1687 -0.5774 0.1494  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 1.2189 0.2966 0.8407 -0.2022 -0.6421 0.1754  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 1.2782 0.3217 0.8037 -0.1939 -0.6029 0.1451  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 1.3091 0.3083 0.7982 -0.2162 -0.6424 0.1599  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.8084 0.2051 0.9111 -0.0994 -0.4844 0.1773  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.7534 0.2082 0.9925 -0.0824 -0.4494 0.1887  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.7292 0.2178 0.9473 -0.0555 -0.3762 0.1553  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.7071 0.2276 1.0017 -0.0424 -0.3358 0.1553  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.7695 0.2299 1.0808 -0.0900 -0.4745 0.2155  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.7800 0.2898 1.2465 -0.0750 -0.4383 0.2341  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.7719 0.2974 1.3362 -0.0761 -0.4404 0.2553  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.7826 0.3132 1.2744 -0.0605 -0.3992 0.2264  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.7343 0.2101 0.8476 -0.0496 -0.3595 0.1289  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.7043 0.2056 0.7854 -0.0296 -0.3001 0.1002  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.6850 0.1932 0.7519 -0.0230 -0.2777 0.0879  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.6631 0.1965 0.7684 -0.0117 -0.2347 0.0804  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.7365 0.2195 0.7119 -0.0274 -0.2951 0.0799  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.7433 0.2286 0.7326 -0.0286 -0.2998 0.0858  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.7077 0.2209 0.7815 -0.0225 -0.2800 0.0946  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.7770 0.2309 0.6903 -0.0359 -0.3196 0.0815  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.6992 0.1776 0.7092 -0.0325 -0.3068 0.0874  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.6995 0.1810 0.6943 -0.0276 -0.2906 0.0776  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.6832 0.1847 0.7815 -0.0287 -0.2895 0.0955  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.6725 0.1888 0.7800 -0.0197 -0.2576 0.0856  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.7247 0.1592 0.6256 -0.0386 -0.3198 0.0728  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.7346 0.1556 0.5407 -0.0295 -0.2947 0.0502  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.7735 0.1602 0.5091 -0.0347 -0.3043 0.0458  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.7183 0.1611 0.5016 -0.0140 -0.2542 0.0326  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.7897 0.1790 0.4695 -0.0212 -0.2685 0.0273  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.7555 0.1798 0.4651 -0.0093 -0.2412 0.0206  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.6964 0.1692 0.5152 -0.0052 -0.2283 0.0280  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.7530 0.1931 0.4366 0.0038  -0.2074 0.0083  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.7094 0.1929 0.4890 0.0055  -0.1985 0.0141  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.7288 0.1994 0.4486 0.0100  -0.1900 0.0063  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.6805 0.1797 0.8597 -0.0409 -0.3257 0.1246  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.6495 0.1687 0.9485 -0.0420 -0.3243 0.1480  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.6191 0.1711 1.0009 -0.0251 -0.2644 0.1462  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.6016 0.1675 1.0650 -0.0199 -0.2366 0.1554  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.6304 0.1356 0.9990 -0.0630 -0.3873 0.1861  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.6118 0.1689 0.9681 -0.0181 -0.2419 0.1345  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.5773 0.1501 0.9846 -0.0050 -0.1815 0.1288  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.5954 0.1641 0.8954 0.0032  -0.1421 0.0942  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.5929 0.1624 0.8903 0.0085  -0.1074 0.0860  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.5635 0.1425 1.0432 -0.0065 -0.1900 0.1493  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.5547 0.1415 1.1684 -0.0149 -0.2230 0.1904  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.5420 0.1379 1.2461 -0.0106 -0.1975 0.2040  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.5447 0.1251 1.1759 -0.0286 -0.2815 0.2135  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.6119 0.1735 0.8252 0.0026  -0.1509 0.0770  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.6226 0.1818 0.7416 0.0075  -0.1247 0.0509  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.6134 0.1701 0.7418 0.0114  -0.0692 0.0411  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.6036 0.1566 0.7816 0.0120  -0.0472 0.0468  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.6363 0.1888 0.6919 0.0065  -0.1417 0.0419  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.6637 0.2164 0.6374 0.0106  -0.1193 0.0217  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.6801 0.2329 0.6021 0.0118  -0.1252 0.0147  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.6675 0.2135 0.5991 0.0109  -0.1333 0.0176  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.6136 0.1653 0.6875 0.0116  -0.0464 0.0269  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.6165 0.1492 0.6653 0.0089  0.0035  0.0153  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.6417 0.1702 0.5947 0.0043  -0.0006 0.0001  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.6665 0.1789 0.5936 -0.0006 0.0204  -0.0055 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.6207 0.1439 0.6778 0.0081  0.0275  0.0141  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.6623 0.1522 0.6514 -0.0008 0.0712  -0.0014 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.5886 0.1130 0.7556 0.0129  0.0419  0.0329  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.6314 0.1731 0.5387 0.0055  -0.0285 -0.0033 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.6303 0.1737 0.4662 0.0022  -0.0358 -0.0110 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.6081 0.1667 0.4246 0.0084  -0.0680 -0.0091 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.6005 0.1618 0.4343 0.0108  -0.0790 -0.0060 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.6450 0.1711 0.4383 -0.0083 -0.0115 -0.0174 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.6658 0.1964 0.3988 -0.0146 -0.0252 -0.0187 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.6878 0.2128 0.3861 -0.0220 -0.0286 -0.0172 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.6606 0.2038 0.3721 -0.0142 -0.0396 -0.0173 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.6983 0.2339 0.3635 -0.0265 -0.0457 -0.0120 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.6828 0.2294 0.3556 -0.0215 -0.0506 -0.0126 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.6450 0.1970 0.3710 -0.0086 -0.0453 -0.0174 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.6811 0.2406 0.3365 -0.0233 -0.0640 -0.0069 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.6542 0.2159 0.3521 -0.0102 -0.0564 -0.0154 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.6671 0.2331 0.3335 -0.0173 -0.0645 -0.0097 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.6029 0.1662 0.3828 0.0102  -0.0794 -0.0100 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.5961 0.1631 0.3510 0.0161  -0.0981 -0.0087 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.5922 0.1662 0.3144 0.0163  -0.0946 -0.0072 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.5811 0.1554 0.2998 0.0125  -0.0888 -0.0059 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.6017 0.1562 0.3630 0.0199  -0.1197 -0.0055 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.6123 0.1626 0.3837 0.0200  -0.1218 -0.0042 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.6556 0.2049 0.3943 0.0240  -0.1182 -0.0053 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.6852 0.2365 0.4335 0.0230  -0.1130 -0.0050 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.6162 0.1616 0.3249 0.0286  -0.1178 -0.0049 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.5937 0.1719 0.2977 0.0201  -0.0982 -0.0046 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.5838 0.1718 0.2758 0.0211  -0.0960 0.0033  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.5750 0.1562 0.2573 0.0316  -0.0960 0.0061  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.5749 0.1563 0.2514 0.0323  -0.0949 0.0058  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.6048 0.2018 0.2893 0.0087  -0.0930 0.0080  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.6568 0.2658 0.3415 0.0044  -0.0983 0.0235  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.6305 0.2452 0.3290 0.0158  -0.0977 0.0311  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.7189 0.3263 0.3897 -0.0123 -0.1030 0.0302  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.5671 0.1361 0.2439 0.0393  -0.0930 0.0088  36  SER   A N   
241  C CA  A SER   A 30  ? 0.5822 0.1290 0.2408 0.0489  -0.0828 0.0111  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.5802 0.1270 0.2385 0.0486  -0.0832 0.0108  36  SER   A CA  
243  C C   . SER   A 30  ? 0.5690 0.1344 0.2450 0.0522  -0.0712 0.0233  36  SER   A C   
244  O O   . SER   A 30  ? 0.5700 0.1196 0.2331 0.0574  -0.0606 0.0235  36  SER   A O   
245  C CB  A SER   A 30  ? 0.6038 0.1299 0.2540 0.0554  -0.0746 0.0131  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.5992 0.1201 0.2436 0.0548  -0.0763 0.0110  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.6371 0.1414 0.2706 0.0510  -0.0878 0.0043  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.5955 0.1402 0.2689 0.0569  -0.0708 0.0216  36  SER   A OG  
249  N N   . SER   A 31  ? 0.5539 0.1491 0.2589 0.0467  -0.0752 0.0359  37  SER   A N   
250  C CA  . SER   A 31  ? 0.5539 0.1696 0.2874 0.0464  -0.0713 0.0541  37  SER   A CA  
251  C C   . SER   A 31  ? 0.5475 0.1694 0.2729 0.0402  -0.0757 0.0507  37  SER   A C   
252  O O   . SER   A 31  ? 0.5496 0.1823 0.2975 0.0424  -0.0697 0.0646  37  SER   A O   
253  C CB  . SER   A 31  ? 0.5689 0.2082 0.3307 0.0359  -0.0842 0.0725  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.6156 0.2606 0.3591 0.0167  -0.1016 0.0692  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.5399 0.1551 0.2409 0.0330  -0.0841 0.0346  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.5391 0.1569 0.2315 0.0275  -0.0864 0.0302  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.5568 0.1517 0.2280 0.0350  -0.0832 0.0170  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.5713 0.1667 0.2365 0.0320  -0.0845 0.0137  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.5422 0.1629 0.2247 0.0115  -0.0945 0.0244  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.5295 0.1584 0.2131 -0.0041 -0.1032 0.0378  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.5741 0.1856 0.2288 -0.0226 -0.1032 0.0294  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.5870 0.1920 0.2275 -0.0292 -0.0995 0.0238  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.6110 0.1932 0.2185 -0.0494 -0.0965 0.0209  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.5947 0.1541 0.1731 -0.0674 -0.0980 0.0237  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.6133 0.1881 0.2094 -0.0537 -0.0907 0.0155  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.5700 0.1401 0.2258 0.0414  -0.0825 0.0107  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.5942 0.1321 0.2216 0.0421  -0.0887 0.0015  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.5992 0.1469 0.2404 0.0337  -0.1032 -0.0041 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.6134 0.1486 0.2445 0.0317  -0.1098 -0.0066 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.6111 0.1273 0.2142 0.0468  -0.0765 0.0030  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.6654 0.1348 0.2239 0.0427  -0.0871 -0.0045 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.6623 0.1011 0.1979 0.0391  -0.0975 -0.0075 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.6930 0.1530 0.2369 0.0404  -0.0881 -0.0058 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.5803 0.1461 0.2458 0.0287  -0.1044 -0.0049 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.5745 0.1432 0.2618 0.0226  -0.1083 -0.0085 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.5802 0.1426 0.2904 0.0213  -0.1150 -0.0087 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.5768 0.1399 0.2848 0.0226  -0.1130 -0.0082 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.5619 0.1450 0.2557 0.0147  -0.0951 -0.0092 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.5887 0.1790 0.2675 0.0121  -0.0917 -0.0071 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.5879 0.1788 0.2583 -0.0019 -0.0813 -0.0073 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.6021 0.1843 0.2824 0.0156  -0.0972 -0.0096 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.5808 0.1381 0.3206 0.0184  -0.1231 -0.0068 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.5904 0.1449 0.3707 0.0162  -0.1287 -0.0026 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.5870 0.1470 0.4157 0.0136  -0.1190 0.0011  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.5930 0.1517 0.4219 0.0130  -0.1239 0.0028  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.6115 0.1434 0.3853 0.0140  -0.1585 0.0038  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.6109 0.1416 0.4341 0.0102  -0.1692 0.0122  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.6453 0.1502 0.4349 0.0066  -0.1918 0.0143  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.5997 0.1320 0.4873 0.0051  -0.1831 0.0260  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.5921 0.1546 0.4598 0.0123  -0.0989 0.0022  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.5971 0.1580 0.5205 0.0111  -0.0784 0.0073  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.6024 0.1630 0.5981 0.0116  -0.0833 0.0205  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.5930 0.1521 0.5886 0.0116  -0.0775 0.0187  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.6162 0.1667 0.5158 0.0066  -0.0374 -0.0029 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.6136 0.1516 0.5742 0.0064  -0.0058 0.0027  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.6334 0.1854 0.4702 0.0031  -0.0395 -0.0110 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.6075 0.1703 0.6697 0.0112  -0.0979 0.0366  43  SER   A N   
298  C CA  . SER   A 37  ? 0.6139 0.1792 0.7666 0.0102  -0.1065 0.0566  43  SER   A CA  
299  C C   . SER   A 37  ? 0.6318 0.1975 0.8720 0.0134  -0.0707 0.0682  43  SER   A C   
300  O O   . SER   A 37  ? 0.6272 0.1893 0.8543 0.0149  -0.0517 0.0625  43  SER   A O   
301  C CB  . SER   A 37  ? 0.6232 0.1848 0.7882 0.0027  -0.1646 0.0741  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.6534 0.2110 0.8031 -0.0001 -0.1836 0.0776  43  SER   A OG  
303  N N   . SER   A 38  ? 0.6369 0.2044 0.9706 0.0148  -0.0582 0.0857  44  SER   A N   
304  C CA  . SER   A 38  ? 0.6462 0.2098 1.0812 0.0196  -0.0158 0.1009  44  SER   A CA  
305  C C   . SER   A 38  ? 0.6513 0.2291 1.1815 0.0175  -0.0541 0.1319  44  SER   A C   
306  O O   . SER   A 38  ? 0.6499 0.2354 1.1829 0.0089  -0.1170 0.1469  44  SER   A O   
307  C CB  . SER   A 38  ? 0.6410 0.1983 1.1447 0.0225  0.0191  0.1094  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.6487 0.2225 1.1978 0.0180  -0.0325 0.1289  44  SER   A OG  
309  N N   . THR   A 39  ? 0.6615 0.2356 1.2622 0.0229  -0.0169 0.1421  45  THR   A N   
310  C CA  . THR   A 39  ? 0.6644 0.2521 1.3698 0.0208  -0.0499 0.1759  45  THR   A CA  
311  C C   . THR   A 39  ? 0.6742 0.2606 1.5280 0.0294  0.0030  0.2016  45  THR   A C   
312  O O   . THR   A 39  ? 0.6997 0.2629 1.5437 0.0373  0.0777  0.1846  45  THR   A O   
313  C CB  . THR   A 39  ? 0.6846 0.2696 1.3319 0.0198  -0.0602 0.1659  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.7111 0.2788 1.3460 0.0281  0.0108  0.1487  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.7263 0.3081 1.2332 0.0131  -0.1007 0.1413  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.6548 0.2594 1.6450 0.0262  -0.0336 0.2445  46  THR   A N   
317  C CA  . THR   A 40  ? 0.6295 0.2354 1.7873 0.0359  0.0178  0.2766  46  THR   A CA  
318  C C   . THR   A 40  ? 0.6452 0.2422 1.8401 0.0436  0.0574  0.2803  46  THR   A C   
319  O O   . THR   A 40  ? 0.6336 0.2164 1.9348 0.0552  0.1299  0.2940  46  THR   A O   
320  C CB  . THR   A 40  ? 0.5977 0.2294 1.9061 0.0274  -0.0423 0.3285  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.6148 0.2586 1.9480 0.0154  -0.1139 0.3544  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.6111 0.2472 1.8695 0.0168  -0.0897 0.3245  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.6624 0.2643 1.7794 0.0369  0.0115  0.2714  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.6575 0.2509 1.7978 0.0431  0.0438  0.2731  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.7174 0.2804 1.7052 0.0469  0.0997  0.2235  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.7619 0.3187 1.6187 0.0420  0.0891  0.1915  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.6514 0.2627 1.7941 0.0318  -0.0375 0.2936  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.7180 0.2585 1.7256 0.0541  0.1591  0.2197  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.7817 0.2852 1.6464 0.0531  0.2098  0.1768  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.8040 0.3203 1.5582 0.0459  0.1572  0.1593  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.7855 0.3241 1.5932 0.0451  0.1117  0.1815  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.8074 0.2670 1.7242 0.0610  0.3023  0.1778  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.9352 0.3342 1.7231 0.0558  0.3753  0.1387  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 1.0260 0.4082 1.8298 0.0563  0.4068  0.1376  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 1.0123 0.4019 1.9630 0.0659  0.4304  0.1684  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 1.0879 0.4476 1.7479 0.0455  0.4068  0.1050  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.8380 0.3378 1.4431 0.0397  0.1637  0.1224  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.8572 0.3643 1.3515 0.0335  0.1260  0.1031  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.8628 0.3331 1.2935 0.0314  0.1815  0.0823  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.8839 0.3115 1.2987 0.0300  0.2481  0.0709  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.8516 0.3300 1.2364 0.0288  0.1561  0.0769  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.8636 0.3047 1.1909 0.0248  0.2052  0.0596  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.8722 0.3112 1.0633 0.0142  0.1823  0.0340  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.9036 0.3127 1.0433 0.0081  0.2127  0.0218  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.8540 0.2979 1.2769 0.0322  0.2153  0.0811  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.8887 0.3234 1.4886 0.0445  0.2656  0.1148  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.8359 0.3030 0.9722 0.0115  0.1319  0.0276  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.8419 0.3102 0.8670 0.0027  0.1116  0.0086  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.8513 0.2767 0.7936 -0.0106 0.1540  -0.0104 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.8662 0.2706 0.8089 -0.0134 0.1801  -0.0131 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.8558 0.3582 0.8505 0.0041  0.0556  0.0088  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.8767 0.4039 0.9094 0.0096  0.0084  0.0239  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.8891 0.4138 0.9465 0.0107  0.0109  0.0302  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.8824 0.4247 0.9143 0.0107  -0.0312 0.0299  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.8481 0.2545 0.7176 -0.0215 0.1602  -0.0218 52  THR   A N   
356  C CA  . THR   A 46  ? 0.8768 0.2332 0.6505 -0.0413 0.1902  -0.0374 52  THR   A CA  
357  C C   . THR   A 46  ? 0.8604 0.2418 0.5667 -0.0493 0.1452  -0.0420 52  THR   A C   
358  O O   . THR   A 46  ? 0.8565 0.2744 0.5584 -0.0447 0.1075  -0.0390 52  THR   A O   
359  C CB  . THR   A 46  ? 0.9230 0.2404 0.6566 -0.0519 0.2184  -0.0439 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.9445 0.2226 0.7351 -0.0465 0.2761  -0.0402 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.9777 0.2451 0.5893 -0.0794 0.2264  -0.0575 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.8502 0.2105 0.5091 -0.0609 0.1508  -0.0472 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.8375 0.2195 0.4420 -0.0693 0.1107  -0.0474 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.8767 0.2163 0.3900 -0.0958 0.1151  -0.0526 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.9250 0.1981 0.3873 -0.1142 0.1549  -0.0601 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.8308 0.2100 0.4299 -0.0711 0.1095  -0.0473 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.7984 0.2074 0.4876 -0.0491 0.1100  -0.0408 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.8286 0.2334 0.3854 -0.0784 0.0680  -0.0433 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.7776 0.2420 0.5185 -0.0311 0.0673  -0.0321 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.8586 0.2287 0.3489 -0.1000 0.0764  -0.0473 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.8909 0.2247 0.2999 -0.1286 0.0694  -0.0467 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.9292 0.2310 0.2772 -0.1520 0.0602  -0.0436 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.9081 0.2434 0.2851 -0.1417 0.0418  -0.0384 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.8562 0.2373 0.2767 -0.1246 0.0303  -0.0371 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.9898 0.2204 0.2481 -0.1856 0.0725  -0.0462 55  ARG   A N   
376  C CA  . ARG   A 49  ? 1.0433 0.2272 0.2248 -0.2166 0.0596  -0.0409 55  ARG   A CA  
377  C C   . ARG   A 49  ? 1.0841 0.2474 0.2019 -0.2483 0.0244  -0.0288 55  ARG   A C   
378  O O   . ARG   A 49  ? 1.1583 0.2447 0.1932 -0.2772 0.0447  -0.0350 55  ARG   A O   
379  C CB  . ARG   A 49  ? 1.1131 0.2063 0.2326 -0.2330 0.1144  -0.0554 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 1.0875 0.2030 0.2864 -0.2013 0.1508  -0.0634 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 1.0540 0.2364 0.3114 -0.1824 0.1170  -0.0550 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 1.0154 0.2131 0.3482 -0.1558 0.1502  -0.0607 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.9558 0.2137 0.3578 -0.1328 0.1286  -0.0553 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.8983 0.2045 0.3032 -0.1309 0.0803  -0.0456 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.9347 0.2012 0.4066 -0.1126 0.1566  -0.0574 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 1.0348 0.2649 0.1967 -0.2424 -0.0253 -0.0101 56  CYS   A N   
387  C CA  . CYS   A 50  ? 1.0439 0.2716 0.1759 -0.2671 -0.0619 0.0065  56  CYS   A CA  
388  C C   . CYS   A 50  ? 1.0174 0.3129 0.2076 -0.2620 -0.1129 0.0329  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.9752 0.3173 0.2239 -0.2372 -0.1152 0.0346  56  CYS   A O   
390  C CB  . CYS   A 50  ? 1.0245 0.2779 0.1940 -0.2473 -0.0460 -0.0020 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.9542 0.3114 0.2482 -0.1953 -0.0524 -0.0010 56  CYS   A SG  
392  N N   . ASP   A 51  ? 1.0300 0.3346 0.2165 -0.2824 -0.1502 0.0546  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.9899 0.3617 0.2519 -0.2745 -0.1917 0.0837  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.9457 0.3678 0.2683 -0.2548 -0.1939 0.0889  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.9306 0.3829 0.2930 -0.2643 -0.2286 0.1178  57  ASP   A O   
396  C CB  . ASP   A 51  ? 1.0457 0.3859 0.2665 -0.3197 -0.2414 0.1155  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 1.2031 0.5035 0.3716 -0.3598 -0.2710 0.1324  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 1.2385 0.5139 0.3730 -0.3583 -0.2443 0.1126  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 1.2802 0.5743 0.4463 -0.3936 -0.3234 0.1681  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.9188 0.3475 0.2525 -0.2283 -0.1570 0.0635  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.8647 0.3334 0.2467 -0.2083 -0.1536 0.0643  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.7790 0.3140 0.2476 -0.1825 -0.1673 0.0822  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.7542 0.3095 0.2528 -0.1633 -0.1610 0.0794  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.8660 0.3301 0.2513 -0.1828 -0.1138 0.0359  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.9080 0.2991 0.2129 -0.2072 -0.0873 0.0182  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.7354 0.2985 0.2430 -0.1824 -0.1821 0.1008  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.6779 0.2950 0.2689 -0.1553 -0.1822 0.1168  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.6470 0.2824 0.2635 -0.1315 -0.1607 0.1069  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.6173 0.2851 0.2941 -0.1159 -0.1584 0.1237  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.6703 0.3092 0.3097 -0.1739 -0.2172 0.1571  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.6956 0.3361 0.3461 -0.1824 -0.2355 0.1725  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.7004 0.3637 0.4121 -0.2030 -0.2748 0.2190  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.7506 0.3842 0.4243 -0.2432 -0.3143 0.2389  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.6393 0.3498 0.4471 -0.1781 -0.2645 0.2397  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.6544 0.2645 0.2263 -0.1302 -0.1431 0.0821  60  THR   A N   
416  C CA  . THR   A 54  ? 0.6366 0.2557 0.2211 -0.1097 -0.1238 0.0699  60  THR   A CA  
417  C C   . THR   A 54  ? 0.6200 0.2187 0.1776 -0.0963 -0.1020 0.0421  60  THR   A C   
418  O O   . THR   A 54  ? 0.6363 0.2057 0.1568 -0.1095 -0.0975 0.0317  60  THR   A O   
419  C CB  . THR   A 54  ? 0.6744 0.2837 0.2427 -0.1278 -0.1315 0.0765  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.7272 0.2919 0.2305 -0.1487 -0.1270 0.0607  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.6645 0.2903 0.2639 -0.1490 -0.1611 0.1103  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.5889 0.1979 0.1657 -0.0725 -0.0882 0.0327  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.5896 0.1839 0.1579 -0.0597 -0.0741 0.0133  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.5770 0.1773 0.1610 -0.0387 -0.0684 0.0090  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.5736 0.1839 0.1674 -0.0341 -0.0683 0.0178  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.5717 0.1605 0.1577 -0.0283 -0.0643 -0.0023 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.5778 0.1584 0.1660 -0.0143 -0.0655 -0.0057 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.5849 0.1587 0.1794 -0.0052 -0.0715 -0.0083 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.5859 0.1593 0.1929 -0.0079 -0.0713 -0.0118 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.5928 0.1607 0.1814 -0.0164 -0.0627 -0.0113 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.6103 0.1633 0.1963 -0.0067 -0.0717 -0.0113 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.6172 0.1878 0.1937 -0.0267 -0.0571 -0.0091 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.5967 0.1589 0.1785 0.0038  -0.0742 -0.0061 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.6129 0.1600 0.1904 0.0090  -0.0827 -0.0078 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.6471 0.1584 0.1985 0.0104  -0.0951 -0.0083 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.6583 0.1536 0.1853 0.0108  -0.0901 -0.0075 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.6071 0.1579 0.1806 0.0143  -0.0746 -0.0035 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.6394 0.1665 0.1874 0.0211  -0.0616 0.0001  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.6394 0.1779 0.1967 0.0220  -0.0469 0.0074  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.6879 0.1740 0.2001 0.0248  -0.0612 -0.0025 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.6694 0.1814 0.2092 0.0295  -0.0256 0.0120  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.7224 0.1718 0.2010 0.0300  -0.0396 -0.0002 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.7169 0.1801 0.2127 0.0337  -0.0188 0.0069  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.7506 0.1744 0.2201 0.0400  0.0112  0.0105  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.6641 0.1590 0.2185 0.0088  -0.1131 -0.0076 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.7268 0.1794 0.2498 0.0039  -0.1337 -0.0040 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.7638 0.1733 0.2291 0.0040  -0.1309 -0.0053 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.7393 0.1522 0.2075 0.0071  -0.1272 -0.0065 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.7374 0.1887 0.2987 -0.0020 -0.1603 0.0033  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.7964 0.1984 0.3229 -0.0129 -0.1920 0.0123  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.8253 0.2080 0.3304 -0.0176 -0.1979 0.0152  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.8428 0.2104 0.3489 -0.0216 -0.2186 0.0189  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.8840 0.2122 0.3471 -0.0322 -0.2317 0.0255  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.8979 0.2079 0.3585 -0.0382 -0.2544 0.0299  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.9316 0.2202 0.3680 -0.0441 -0.2614 0.0334  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 1.0168 0.2390 0.3969 -0.0647 -0.3004 0.0457  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.8177 0.1804 0.2260 0.0002  -0.1277 -0.0054 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.8770 0.1798 0.2159 -0.0015 -0.1155 -0.0076 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.9421 0.1744 0.2177 -0.0192 -0.1489 -0.0035 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.9630 0.1600 0.1999 -0.0273 -0.1551 -0.0016 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.8960 0.1873 0.2121 0.0061  -0.0778 -0.0096 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.9851 0.1845 0.2086 0.0043  -0.0470 -0.0125 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.9634 0.1744 0.2301 -0.0281 -0.1753 0.0003  66  SER   A N   
464  C CA  . SER   A 60  ? 1.0374 0.1780 0.2454 -0.0508 -0.2177 0.0094  66  SER   A CA  
465  C C   . SER   A 60  ? 1.1179 0.1625 0.2096 -0.0634 -0.2057 0.0053  66  SER   A C   
466  O O   . SER   A 60  ? 1.1709 0.1652 0.2169 -0.0824 -0.2371 0.0135  66  SER   A O   
467  C CB  . SER   A 60  ? 1.0847 0.2128 0.2983 -0.0602 -0.2472 0.0157  66  SER   A CB  
468  O OG  . SER   A 60  ? 1.1491 0.2946 0.3671 -0.0465 -0.2146 0.0058  66  SER   A OG  
469  N N   . SER   A 61  ? 1.1383 0.1549 0.1854 -0.0533 -0.1576 -0.0055 67  SER   A N   
470  C CA  . SER   A 61  ? 1.2275 0.1415 0.1591 -0.0633 -0.1297 -0.0110 67  SER   A CA  
471  C C   . SER   A 61  ? 1.2502 0.1531 0.1640 -0.0638 -0.1180 -0.0111 67  SER   A C   
472  O O   . SER   A 61  ? 1.3246 0.1290 0.1316 -0.0782 -0.1036 -0.0139 67  SER   A O   
473  C CB  . SER   A 61  ? 1.2399 0.1371 0.1549 -0.0475 -0.0711 -0.0194 67  SER   A CB  
474  O OG  . SER   A 61  ? 1.1834 0.1624 0.1860 -0.0222 -0.0317 -0.0202 67  SER   A OG  
475  N N   . ARG   A 62  ? 1.1739 0.1685 0.1832 -0.0505 -0.1232 -0.0084 68  ARG   A N   
476  C CA  . ARG   A 62  ? 1.1833 0.1716 0.1810 -0.0520 -0.1178 -0.0076 68  ARG   A CA  
477  C C   . ARG   A 62  ? 1.1773 0.2003 0.2219 -0.0618 -0.1690 0.0027  68  ARG   A C   
478  O O   . ARG   A 62  ? 1.1891 0.2084 0.2274 -0.0642 -0.1696 0.0045  68  ARG   A O   
479  C CB  . ARG   A 62  ? 1.1410 0.1965 0.2046 -0.0285 -0.0704 -0.0118 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 1.1923 0.2067 0.2186 -0.0185 -0.0135 -0.0163 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 1.2991 0.2057 0.2145 -0.0309 0.0100  -0.0195 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 1.3612 0.2323 0.2594 -0.0175 0.0766  -0.0218 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.4356 0.2326 0.2688 -0.0209 0.1028  -0.0257 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.4653 0.2115 0.2334 -0.0403 0.0626  -0.0283 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.4490 0.2206 0.2869 -0.0053 0.1704  -0.0248 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 1.1465 0.2080 0.2503 -0.0654 -0.2076 0.0109  69  ARG   A N   
487  C CA  . ARG   A 63  ? 1.1041 0.2091 0.2811 -0.0704 -0.2482 0.0241  69  ARG   A CA  
488  C C   . ARG   A 63  ? 1.0337 0.2102 0.2796 -0.0528 -0.2210 0.0191  69  ARG   A C   
489  O O   . ARG   A 63  ? 1.0183 0.1994 0.2835 -0.0581 -0.2386 0.0268  69  ARG   A O   
490  C CB  . ARG   A 63  ? 1.1753 0.2047 0.2912 -0.0979 -0.2975 0.0395  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 1.2894 0.2551 0.3565 -0.1219 -0.3425 0.0516  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.4175 0.3193 0.4442 -0.1523 -0.4016 0.0735  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.5863 0.3811 0.5012 -0.1846 -0.4392 0.0820  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.7130 0.4060 0.5238 -0.2184 -0.4797 0.0950  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.7088 0.3983 0.5185 -0.2217 -0.4861 0.1007  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.8111 0.3974 0.5091 -0.2515 -0.5142 0.1025  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.9844 0.2098 0.2615 -0.0342 -0.1791 0.0077  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.9301 0.2125 0.2573 -0.0218 -0.1535 0.0034  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.8505 0.1998 0.2431 -0.0089 -0.1338 -0.0011 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.8532 0.2015 0.2391 -0.0047 -0.1239 -0.0037 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.9795 0.2330 0.2549 -0.0175 -0.1182 -0.0024 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 1.0667 0.2918 0.3106 -0.0242 -0.1215 -0.0004 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 1.1645 0.3648 0.3690 -0.0172 -0.0772 -0.0053 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 1.2556 0.4244 0.4241 -0.0230 -0.0736 -0.0043 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.3585 0.4237 0.4182 -0.0390 -0.0779 -0.0044 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.7870 0.1851 0.2320 -0.0047 -0.1260 -0.0018 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.7375 0.1873 0.2288 0.0019  -0.1079 -0.0052 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.7255 0.1867 0.2070 0.0061  -0.0820 -0.0060 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.7450 0.1909 0.2063 0.0048  -0.0766 -0.0054 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.7105 0.1903 0.2517 -0.0005 -0.1115 -0.0046 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.7038 0.1801 0.2792 -0.0031 -0.1318 0.0009  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.6971 0.1947 0.3075 -0.0011 -0.1267 -0.0003 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.7131 0.1669 0.2991 -0.0086 -0.1577 0.0108  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.6872 0.1771 0.3348 -0.0037 -0.1463 0.0089  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.7038 0.1688 0.3417 -0.0090 -0.1683 0.0177  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.6847 0.1713 0.1848 0.0102  -0.0677 -0.0047 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.6749 0.1770 0.1842 0.0131  -0.0465 0.0013  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.6417 0.1884 0.1920 0.0080  -0.0471 0.0061  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.6173 0.1765 0.1810 0.0069  -0.0531 0.0055  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.6922 0.1705 0.1847 0.0212  -0.0267 0.0055  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.7520 0.1679 0.1840 0.0222  -0.0181 0.0016  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.7825 0.1772 0.1940 0.0221  -0.0026 0.0033  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.8002 0.1701 0.1876 0.0206  -0.0243 -0.0028 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.8463 0.1695 0.1868 0.0195  0.0075  -0.0005 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.8594 0.1548 0.1721 0.0159  -0.0169 -0.0059 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.8975 0.1671 0.1838 0.0152  0.0005  -0.0050 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.9993 0.1828 0.1981 0.0071  0.0095  -0.0084 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.6382 0.2030 0.2026 0.0021  -0.0425 0.0123  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.6224 0.2174 0.2130 -0.0092 -0.0481 0.0206  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.6128 0.2238 0.2333 -0.0054 -0.0417 0.0366  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.6182 0.2203 0.2467 0.0053  -0.0238 0.0439  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.6274 0.2281 0.2187 -0.0190 -0.0482 0.0246  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.6446 0.2272 0.2247 -0.0078 -0.0349 0.0242  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.6403 0.1930 0.1927 0.0029  -0.0339 0.0139  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.5914 0.2200 0.2283 -0.0139 -0.0531 0.0431  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.5860 0.2325 0.2621 -0.0113 -0.0505 0.0622  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.5840 0.2517 0.2802 -0.0322 -0.0726 0.0786  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.6058 0.2643 0.2696 -0.0483 -0.0863 0.0691  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.5974 0.2330 0.2683 0.0019  -0.0430 0.0556  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.6223 0.2249 0.2683 0.0183  -0.0215 0.0466  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.6131 0.2439 0.2592 -0.0047 -0.0577 0.0406  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.5585 0.2480 0.3075 -0.0337 -0.0751 0.1054  75  SER   A N   
543  C CA  . SER   A 69  ? 0.5539 0.2599 0.3263 -0.0556 -0.1028 0.1277  75  SER   A CA  
544  C C   . SER   A 69  ? 0.5465 0.2579 0.3405 -0.0423 -0.0957 0.1306  75  SER   A C   
545  O O   . SER   A 69  ? 0.5462 0.2560 0.3643 -0.0191 -0.0683 0.1307  75  SER   A O   
546  C CB  . SER   A 69  ? 0.5502 0.2805 0.3870 -0.0652 -0.1131 0.1630  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.6206 0.3437 0.4316 -0.0847 -0.1279 0.1627  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.5449 0.2530 0.3188 -0.0568 -0.1156 0.1295  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.5401 0.2527 0.3318 -0.0450 -0.1100 0.1312  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.5580 0.2828 0.3735 -0.0673 -0.1406 0.1574  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.5731 0.2896 0.3644 -0.0966 -0.1689 0.1666  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.5480 0.2379 0.2875 -0.0338 -0.0980 0.0987  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.5639 0.2343 0.2499 -0.0520 -0.1101 0.0814  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.5743 0.2299 0.2297 -0.0537 -0.1034 0.0654  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.5789 0.2399 0.2447 -0.0673 -0.1234 0.0815  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.6050 0.2361 0.2163 -0.0689 -0.1052 0.0504  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.6115 0.2432 0.2249 -0.0841 -0.1244 0.0654  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.6229 0.2392 0.2117 -0.0845 -0.1132 0.0505  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.5488 0.2879 0.4100 -0.0559 -0.1359 0.1721  77  SER   A N   
560  C CA  . SER   A 71  ? 0.5550 0.3058 0.4459 -0.0772 -0.1680 0.2013  77  SER   A CA  
561  C C   . SER   A 71  ? 0.5904 0.3157 0.4124 -0.0939 -0.1840 0.1830  77  SER   A C   
562  O O   . SER   A 71  ? 0.6066 0.3108 0.3732 -0.0844 -0.1656 0.1489  77  SER   A O   
563  C CB  . SER   A 71  ? 0.5456 0.3206 0.5200 -0.0575 -0.1533 0.2265  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.5722 0.3337 0.5217 -0.0335 -0.1245 0.2007  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.6026 0.3260 0.4296 -0.1211 -0.2188 0.2081  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.6586 0.3503 0.4189 -0.1401 -0.2324 0.1949  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.6586 0.3598 0.4364 -0.1143 -0.2112 0.1829  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.6273 0.3579 0.4769 -0.0935 -0.2009 0.2005  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.6950 0.3753 0.4534 -0.1809 -0.2812 0.2313  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.7905 0.4493 0.5156 -0.2141 -0.3082 0.2438  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.9106 0.5230 0.5730 -0.2649 -0.3562 0.2648  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 1.0404 0.5995 0.6115 -0.2985 -0.3669 0.2542  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 1.0910 0.6524 0.6913 -0.3338 -0.4178 0.2988  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.6968 0.3701 0.4131 -0.1153 -0.2015 0.1548  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.6996 0.3806 0.4322 -0.0924 -0.1840 0.1444  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.6870 0.3887 0.4753 -0.0951 -0.2017 0.1764  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.6915 0.3834 0.4700 -0.1253 -0.2357 0.1991  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.7454 0.3902 0.4071 -0.1022 -0.1775 0.1168  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.7756 0.3959 0.3903 -0.1159 -0.1736 0.1029  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.7380 0.3675 0.3710 -0.1364 -0.2008 0.1319  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.6710 0.3957 0.5170 -0.0655 -0.1788 0.1808  80  SER   A N   
582  C CA  . SER   A 74  ? 0.6638 0.4104 0.5790 -0.0632 -0.1882 0.2138  80  SER   A CA  
583  C C   . SER   A 74  ? 0.6583 0.4075 0.5973 -0.0315 -0.1541 0.2028  80  SER   A C   
584  O O   . SER   A 74  ? 0.6702 0.4026 0.5695 -0.0132 -0.1272 0.1709  80  SER   A O   
585  C CB  . SER   A 74  ? 0.6642 0.4382 0.6597 -0.0669 -0.1984 0.2528  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.7031 0.4850 0.7327 -0.0372 -0.1580 0.2456  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.6372 0.4029 0.6393 -0.0279 -0.1583 0.2316  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.6447 0.4077 0.6729 -0.0006 -0.1255 0.2267  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.6427 0.4123 0.7338 0.0225  -0.0889 0.2409  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.6120 0.4074 0.7889 0.0186  -0.0964 0.2809  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.6242 0.4016 0.7022 -0.0087 -0.1456 0.2570  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.6652 0.4256 0.6844 -0.0181 -0.1597 0.2381  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.6575 0.4329 0.7330 -0.0279 -0.1826 0.2740  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.6863 0.4262 0.6690 0.0076  -0.1232 0.2039  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.6737 0.4148 0.7241 0.0443  -0.0496 0.2113  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.6868 0.4165 0.7759 0.0653  -0.0059 0.2194  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.7324 0.4215 0.7979 0.0882  0.0386  0.2032  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.7653 0.4259 0.7512 0.0885  0.0364  0.1705  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.7146 0.4314 0.7544 0.0631  -0.0021 0.1987  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.7059 0.4556 0.7692 0.0399  -0.0410 0.2170  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.7241 0.4114 0.7771 0.0848  0.0499  0.1988  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.7505 0.4869 0.7458 0.0327  -0.0484 0.1896  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.7294 0.4099 0.8637 0.1064  0.0813  0.2273  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.7800 0.4068 0.8823 0.1263  0.1308  0.2125  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.8421 0.4073 0.8405 0.1311  0.1564  0.1755  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.8491 0.4089 0.8421 0.1308  0.1659  0.1744  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.7561 0.3798 0.9604 0.1449  0.1804  0.2490  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.7959 0.3562 0.9682 0.1636  0.2363  0.2373  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.8084 0.3701 0.9824 0.1646  0.2277  0.2375  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.8454 0.3362 0.9778 0.1781  0.2994  0.2257  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.8517 0.3482 0.9904 0.1801  0.2806  0.2267  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.8934 0.3108 0.9832 0.1919  0.3544  0.2150  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.8856 0.3067 0.9777 0.1927  0.3438  0.2149  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.8868 0.4034 0.8027 0.1329  0.1636  0.1476  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.9563 0.4040 0.7653 0.1321  0.1792  0.1156  84  VAL   A CA  
616  C C   . VAL   A 78  ? 1.0198 0.3916 0.7810 0.1424  0.2252  0.1073  84  VAL   A C   
617  O O   . VAL   A 78  ? 1.0176 0.3929 0.7838 0.1434  0.2177  0.1074  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.9760 0.4332 0.7172 0.1153  0.1275  0.0891  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 1.0389 0.4223 0.6765 0.1111  0.1364  0.0627  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.9446 0.4623 0.7208 0.1041  0.0902  0.0951  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 1.0758 0.3706 0.7814 0.1482  0.2741  0.0993  85  GLU   A N   
622  C CA  . GLU   A 79  ? 1.1453 0.3452 0.7839 0.1545  0.3257  0.0898  85  GLU   A CA  
623  C C   . GLU   A 79  ? 1.1927 0.3436 0.7222 0.1393  0.2947  0.0616  85  GLU   A C   
624  O O   . GLU   A 79  ? 1.1951 0.3707 0.6882 0.1243  0.2402  0.0467  85  GLU   A O   
625  C CB  . GLU   A 79  ? 1.2436 0.3610 0.8313 0.1592  0.3845  0.0863  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 1.2938 0.4397 0.9991 0.1784  0.4356  0.1191  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.4594 0.4960 1.1245 0.1907  0.5252  0.1201  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.5202 0.4993 1.1510 0.1949  0.5570  0.1156  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.5091 0.5112 1.1730 0.1955  0.5674  0.1249  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 1.2250 0.3029 0.7061 0.1427  0.3312  0.0565  86  ALA   A N   
631  C CA  . ALA   A 80  ? 1.2783 0.3014 0.6580 0.1265  0.3033  0.0339  86  ALA   A CA  
632  C C   . ALA   A 80  ? 1.3405 0.2895 0.5961 0.1051  0.2814  0.0116  86  ALA   A C   
633  O O   . ALA   A 80  ? 1.3781 0.2801 0.5968 0.1047  0.3112  0.0100  86  ALA   A O   
634  C CB  . ALA   A 80  ? 1.3162 0.2618 0.6624 0.1337  0.3560  0.0345  86  ALA   A CB  
635  N N   . SER   A 81  ? 1.3508 0.2875 0.5463 0.0863  0.2286  -0.0028 87  SER   A N   
636  C CA  . SER   A 81  ? 1.4031 0.2739 0.4900 0.0614  0.1930  -0.0186 87  SER   A CA  
637  C C   . SER   A 81  ? 1.4427 0.2677 0.4612 0.0423  0.1558  -0.0281 87  SER   A C   
638  O O   . SER   A 81  ? 1.4152 0.2649 0.4735 0.0511  0.1625  -0.0245 87  SER   A O   
639  C CB  . SER   A 81  ? 1.3578 0.3130 0.4974 0.0576  0.1428  -0.0170 87  SER   A CB  
640  O OG  . SER   A 81  ? 1.3019 0.3579 0.5293 0.0615  0.1011  -0.0120 87  SER   A OG  
641  N N   . GLU   A 82  ? 1.5009 0.2562 0.4185 0.0142  0.1144  -0.0375 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.5389 0.2544 0.4024 -0.0068 0.0719  -0.0418 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.4328 0.2662 0.4049 -0.0015 0.0202  -0.0357 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.4461 0.2660 0.4018 -0.0140 -0.0112 -0.0363 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.6785 0.2809 0.4069 -0.0432 0.0344  -0.0474 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.7481 0.4082 0.5145 -0.0568 -0.0344 -0.0414 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.9200 0.4730 0.5644 -0.0916 -0.0685 -0.0416 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 2.0129 0.4410 0.5296 -0.1181 -0.0705 -0.0454 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.9276 0.5168 0.6000 -0.0949 -0.0955 -0.0369 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 1.3296 0.2707 0.4082 0.0160  0.0161  -0.0295 89  TYR   A N   
651  C CA  . TYR   A 83  ? 1.2297 0.2758 0.4067 0.0212  -0.0221 -0.0244 89  TYR   A CA  
652  C C   . TYR   A 83  ? 1.1428 0.2613 0.4074 0.0432  0.0043  -0.0177 89  TYR   A C   
653  O O   . TYR   A 83  ? 1.1122 0.2797 0.4236 0.0432  -0.0202 -0.0158 89  TYR   A O   
654  C CB  . TYR   A 83  ? 1.1926 0.2934 0.4119 0.0207  -0.0446 -0.0221 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 1.2437 0.2755 0.3835 -0.0004 -0.0694 -0.0250 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 1.2719 0.2761 0.3834 -0.0231 -0.1218 -0.0226 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 1.2853 0.2774 0.3818 0.0007  -0.0425 -0.0272 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 1.3323 0.2691 0.3712 -0.0465 -0.1520 -0.0207 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 1.3468 0.2691 0.3628 -0.0214 -0.0679 -0.0288 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 1.3817 0.2759 0.3679 -0.0461 -0.1254 -0.0247 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.4608 0.2822 0.3678 -0.0719 -0.1578 -0.0218 89  TYR   A OH  
662  N N   . TYR   A 84  ? 1.0989 0.2265 0.3929 0.0605  0.0511  -0.0109 90  TYR   A N   
663  C CA  . TYR   A 84  ? 1.0269 0.2230 0.4112 0.0781  0.0693  0.0018  90  TYR   A CA  
664  C C   . TYR   A 84  ? 1.0467 0.2040 0.4358 0.0934  0.1285  0.0109  90  TYR   A C   
665  O O   . TYR   A 84  ? 1.0759 0.1843 0.4324 0.0965  0.1638  0.0111  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.9415 0.2241 0.4075 0.0842  0.0576  0.0120  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.8918 0.2196 0.3707 0.0724  0.0103  0.0056  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.8816 0.2112 0.3469 0.0663  -0.0023 0.0016  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.8553 0.2230 0.3658 0.0683  -0.0169 0.0049  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.8579 0.2272 0.3444 0.0571  -0.0388 -0.0021 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.8323 0.2354 0.3610 0.0588  -0.0504 0.0005  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.8328 0.2370 0.3523 0.0537  -0.0601 -0.0025 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.7935 0.2274 0.3364 0.0455  -0.0872 -0.0053 90  TYR   A OH  
674  N N   . PRO   A 85  ? 1.0188 0.2064 0.4656 0.1049  0.1430  0.0223  91  PRO   A N   
675  C CA  . PRO   A 85  ? 1.0201 0.1853 0.5038 0.1230  0.2032  0.0382  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.9724 0.2062 0.5503 0.1336  0.2112  0.0589  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.9315 0.2319 0.5417 0.1260  0.1673  0.0596  91  PRO   A O   
678  C CB  . PRO   A 85  ? 1.0045 0.1966 0.5349 0.1296  0.2025  0.0473  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.9692 0.2386 0.5314 0.1190  0.1409  0.0442  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.9757 0.2230 0.4680 0.1026  0.1072  0.0246  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.9670 0.1842 0.5948 0.1501  0.2674  0.0783  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.9187 0.2036 0.6477 0.1581  0.2702  0.1035  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.8459 0.2287 0.6675 0.1546  0.2221  0.1229  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.8331 0.2256 0.6805 0.1578  0.2201  0.1301  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.9196 0.1697 0.7032 0.1773  0.3417  0.1262  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.8028 0.2479 0.6579 0.1447  0.1815  0.1286  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.7487 0.2681 0.6616 0.1341  0.1320  0.1430  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.7188 0.2903 0.6726 0.1235  0.1027  0.1562  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.7326 0.2879 0.6707 0.1259  0.1189  0.1515  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.7685 0.2823 0.6082 0.1212  0.0943  0.1145  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.7754 0.2892 0.5583 0.1087  0.0668  0.0923  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.8111 0.2808 0.5096 0.1022  0.0551  0.0634  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.7933 0.2891 0.4741 0.0886  0.0176  0.0509  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.7707 0.2604 0.4297 0.0847  0.0138  0.0439  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.7228 0.2350 0.3735 0.0734  -0.0161 0.0343  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.7660 0.2231 0.4122 0.0923  0.0441  0.0471  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.6836 0.3086 0.6744 0.1083  0.0576  0.1700  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.6644 0.3279 0.6732 0.0922  0.0239  0.1793  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.6492 0.3063 0.5766 0.0779  -0.0054 0.1468  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.6563 0.3106 0.5531 0.0718  -0.0221 0.1342  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.6509 0.3606 0.7322 0.0777  -0.0103 0.2148  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.6495 0.3783 0.8381 0.0882  0.0107  0.2570  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.6573 0.4021 0.8935 0.0872  0.0150  0.2763  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.6550 0.3840 0.9048 0.1006  0.0306  0.2792  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.6359 0.3995 0.9869 0.0977  0.0375  0.3196  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.6362 0.3822 1.0011 0.1124  0.0559  0.3221  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.6381 0.4019 1.0571 0.1112  0.0599  0.3432  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.6364 0.4193 1.1853 0.1232  0.0867  0.3904  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.6215 0.2744 0.5193 0.0738  -0.0081 0.1346  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.6107 0.2590 0.4470 0.0612  -0.0322 0.1084  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.5755 0.2557 0.4279 0.0406  -0.0638 0.1210  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.5709 0.2678 0.4595 0.0372  -0.0653 0.1399  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.6347 0.2518 0.4219 0.0671  -0.0180 0.0867  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.6416 0.2570 0.3826 0.0549  -0.0420 0.0645  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.7025 0.2808 0.3943 0.0595  -0.0343 0.0449  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.7373 0.2758 0.3993 0.0678  -0.0183 0.0382  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.6644 0.2485 0.3416 0.0516  -0.0470 0.0365  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.5559 0.2381 0.3795 0.0250  -0.0871 0.1124  96  SER   A N   
719  C CA  . SER   A 90  ? 0.5419 0.2359 0.3590 0.0000  -0.1155 0.1226  96  SER   A CA  
720  C C   . SER   A 90  ? 0.5577 0.2384 0.3273 -0.0075 -0.1165 0.1003  96  SER   A C   
721  O O   . SER   A 90  ? 0.5720 0.2375 0.3163 0.0052  -0.1014 0.0772  96  SER   A O   
722  C CB  . SER   A 90  ? 0.5566 0.2456 0.3564 -0.0157 -0.1342 0.1249  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.6042 0.2735 0.3618 -0.0098 -0.1234 0.0962  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.5483 0.2305 0.3060 -0.0303 -0.1362 0.1099  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.5666 0.2329 0.2812 -0.0402 -0.1353 0.0921  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.5564 0.2278 0.2816 -0.0224 -0.1183 0.0837  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.5729 0.2303 0.2683 -0.0206 -0.1106 0.0634  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.5932 0.2345 0.2636 -0.0438 -0.1278 0.0676  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.6338 0.2590 0.2801 -0.0650 -0.1414 0.0747  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.6885 0.2835 0.2855 -0.0947 -0.1518 0.0763  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.6396 0.2687 0.2989 -0.0630 -0.1463 0.0823  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.7076 0.2849 0.2834 -0.1105 -0.1627 0.0837  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.6747 0.2761 0.2917 -0.0915 -0.1611 0.0882  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.5399 0.2276 0.3104 -0.0098 -0.1105 0.1014  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.5455 0.2290 0.3212 0.0067  -0.0898 0.0952  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.5338 0.2318 0.3315 -0.0031 -0.0971 0.1118  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.5284 0.2458 0.3666 -0.0158 -0.1142 0.1398  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.5364 0.2144 0.3416 0.0284  -0.0648 0.1022  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.5727 0.2280 0.3672 0.0447  -0.0365 0.0943  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.6052 0.2334 0.3384 0.0447  -0.0389 0.0659  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.5897 0.2242 0.4027 0.0630  -0.0047 0.1015  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.5395 0.2271 0.3123 0.0005  -0.0882 0.0971  99  MET   A N   
743  C CA  . MET   A 93  ? 0.5373 0.2360 0.3261 -0.0085 -0.0938 0.1100  99  MET   A CA  
744  C C   . MET   A 93  ? 0.5505 0.2421 0.3530 0.0111  -0.0660 0.1087  99  MET   A C   
745  O O   . MET   A 93  ? 0.5830 0.2493 0.3442 0.0219  -0.0520 0.0856  99  MET   A O   
746  C CB  . MET   A 93  ? 0.5631 0.2489 0.3016 -0.0257 -0.1067 0.0930  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.5951 0.2715 0.3049 -0.0483 -0.1269 0.0928  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.6710 0.3161 0.3170 -0.0642 -0.1251 0.0682  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.5802 0.2185 0.2225 -0.0386 -0.1029 0.0427  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.5288 0.2375 0.3888 0.0137  -0.0582 0.1353  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.5396 0.2320 0.4073 0.0316  -0.0243 0.1339  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.5368 0.2354 0.4017 0.0229  -0.0301 0.1356  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.5084 0.2315 0.3968 0.0035  -0.0576 0.1526  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.5250 0.2224 0.4645 0.0468  0.0051  0.1612  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.5543 0.2375 0.4977 0.0594  0.0215  0.1599  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.5461 0.2256 0.5639 0.0769  0.0626  0.1873  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.6033 0.2398 0.4632 0.0683  0.0363  0.1253  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.5669 0.2370 0.3976 0.0351  -0.0054 0.1190  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.5876 0.2562 0.4116 0.0315  -0.0026 0.1181  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.6166 0.2534 0.4430 0.0502  0.0408  0.1195  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.6409 0.2408 0.4386 0.0631  0.0659  0.1093  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.6112 0.2632 0.3671 0.0242  -0.0184 0.0897  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.6125 0.2556 0.4656 0.0496  0.0514  0.1316  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.6475 0.2512 0.4909 0.0645  0.0959  0.1305  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.6980 0.2633 0.4486 0.0611  0.0885  0.0989  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.6945 0.2796 0.4301 0.0487  0.0592  0.0914  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.6277 0.2581 0.5479 0.0638  0.1081  0.1598  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.6601 0.2413 0.5556 0.0772  0.1568  0.1543  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.5794 0.2474 0.6059 0.0662  0.1121  0.1979  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.7407 0.2479 0.4281 0.0695  0.1114  0.0820  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.7902 0.2548 0.3920 0.0638  0.0988  0.0571  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.8399 0.2325 0.3698 0.0682  0.1188  0.0437  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.8505 0.2322 0.3944 0.0759  0.1388  0.0495  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.8708 0.2091 0.3201 0.0608  0.1113  0.0275  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.9265 0.1823 0.2888 0.0576  0.1221  0.0155  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.9246 0.1834 0.2658 0.0498  0.0831  0.0062  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.9000 0.1987 0.2582 0.0421  0.0418  0.0020  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.9969 0.1819 0.2744 0.0479  0.1258  0.0061  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 1.1043 0.1913 0.2736 0.0363  0.1256  -0.0052 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 1.1829 0.1939 0.3026 0.0406  0.1757  -0.0055 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 1.1560 0.2109 0.2650 0.0189  0.0788  -0.0136 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 1.2604 0.1883 0.2762 0.0230  0.1560  -0.0162 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 1.2512 0.2064 0.2630 0.0090  0.0939  -0.0194 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.9583 0.1657 0.2593 0.0513  0.1008  0.0033  105 SER   A N   
785  C CA  . SER   A 99  ? 0.9997 0.1939 0.2707 0.0428  0.0684  -0.0044 105 SER   A CA  
786  C C   . SER   A 99  ? 1.0935 0.1895 0.2773 0.0390  0.0964  -0.0098 105 SER   A C   
787  O O   . SER   A 99  ? 1.1166 0.1740 0.2918 0.0491  0.1500  -0.0055 105 SER   A O   
788  C CB  . SER   A 99  ? 0.9533 0.2271 0.3074 0.0501  0.0543  0.0018  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.9676 0.2533 0.3666 0.0641  0.0946  0.0135  105 SER   A OG  
790  N N   . GLU   A 100 ? 1.1435 0.1942 0.2635 0.0230  0.0612  -0.0175 106 GLU   A N   
791  C CA  . GLU   A 100 ? 1.2429 0.1899 0.2623 0.0119  0.0752  -0.0236 106 GLU   A CA  
792  C C   . GLU   A 100 ? 1.2609 0.2248 0.2868 0.0031  0.0302  -0.0250 106 GLU   A C   
793  O O   . GLU   A 100 ? 1.2317 0.2609 0.3121 -0.0006 -0.0160 -0.0223 106 GLU   A O   
794  C CB  . GLU   A 100 ? 1.3575 0.2014 0.2585 -0.0110 0.0635  -0.0293 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.4760 0.2600 0.3315 -0.0062 0.1199  -0.0305 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.5552 0.2570 0.3071 -0.0308 0.0956  -0.0344 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.6215 0.2348 0.2696 -0.0574 0.0622  -0.0376 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.5369 0.2624 0.3121 -0.0257 0.1050  -0.0323 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 1.3100 0.2104 0.2793 -0.0021 0.0426  -0.0285 107 PRO   A N   
800  C CA  . PRO   A 101 ? 1.3049 0.2214 0.2822 -0.0129 -0.0059 -0.0282 107 PRO   A CA  
801  C C   . PRO   A 101 ? 1.3357 0.2134 0.2601 -0.0393 -0.0642 -0.0261 107 PRO   A C   
802  O O   . PRO   A 101 ? 1.4257 0.2100 0.2493 -0.0574 -0.0633 -0.0281 107 PRO   A O   
803  C CB  . PRO   A 101 ? 1.3617 0.2000 0.2719 -0.0152 0.0250  -0.0326 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 1.4259 0.1715 0.2559 -0.0142 0.0846  -0.0367 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 1.3634 0.1672 0.2561 0.0002  0.1029  -0.0323 107 PRO   A CD  
806  N N   . GLY   A 102 ? 1.2545 0.2073 0.2564 -0.0406 -0.1111 -0.0199 108 GLY   A N   
807  C CA  . GLY   A 102 ? 1.2273 0.1781 0.2300 -0.0599 -0.1673 -0.0113 108 GLY   A CA  
808  C C   . GLY   A 102 ? 1.1223 0.1785 0.2355 -0.0436 -0.1707 -0.0083 108 GLY   A C   
809  O O   . GLY   A 102 ? 1.0904 0.1834 0.2571 -0.0508 -0.2120 0.0010  108 GLY   A O   
810  N N   . ASP   A 103 ? 1.0669 0.1696 0.2186 -0.0224 -0.1252 -0.0139 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.9851 0.1765 0.2265 -0.0095 -0.1233 -0.0120 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.9027 0.1700 0.2283 0.0002  -0.1286 -0.0107 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.8476 0.1737 0.2361 0.0044  -0.1352 -0.0088 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.9857 0.1898 0.2322 0.0040  -0.0800 -0.0145 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 1.0555 0.2010 0.2371 -0.0061 -0.0798 -0.0152 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 1.0463 0.1839 0.2210 -0.0196 -0.1188 -0.0116 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 1.1058 0.2094 0.2453 -0.0010 -0.0395 -0.0177 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.8980 0.1566 0.2185 0.0019  -0.1253 -0.0118 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.8466 0.1695 0.2395 0.0093  -0.1300 -0.0106 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.8065 0.1581 0.2480 0.0015  -0.1644 -0.0054 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.8414 0.1520 0.2568 -0.0127 -0.1961 0.0006  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.8701 0.1668 0.2399 0.0097  -0.1253 -0.0120 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.9235 0.2094 0.2779 0.0250  -0.0738 -0.0136 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.7469 0.1597 0.2557 0.0085  -0.1576 -0.0054 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.7171 0.1531 0.2808 0.0034  -0.1786 0.0007  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.7073 0.1619 0.2927 0.0037  -0.1742 0.0014  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.6930 0.1755 0.3353 0.0036  -0.1751 0.0051  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.7043 0.1424 0.2469 0.0052  -0.1630 -0.0021 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.6759 0.1325 0.2351 0.0060  -0.1559 -0.0024 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.6256 0.1299 0.2273 0.0112  -0.1338 -0.0063 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.6002 0.1202 0.1975 0.0154  -0.1176 -0.0090 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.6046 0.1251 0.2454 0.0087  -0.1334 -0.0047 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.5982 0.1452 0.2628 0.0082  -0.1119 -0.0088 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.6065 0.1628 0.2470 0.0071  -0.0980 -0.0117 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.6304 0.1775 0.2563 0.0073  -0.1012 -0.0107 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.6075 0.1565 0.3221 0.0057  -0.1090 -0.0052 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.6105 0.1591 0.3657 0.0064  -0.1157 0.0002  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.6138 0.1707 0.3321 0.0014  -0.0811 -0.0112 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.5984 0.1462 0.4204 0.0058  -0.1127 0.0100  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.5852 0.1573 0.2229 0.0032  -0.0852 -0.0130 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.5874 0.1696 0.2111 -0.0032 -0.0768 -0.0113 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.6019 0.1787 0.2287 -0.0150 -0.0647 -0.0156 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.5892 0.1601 0.2232 -0.0184 -0.0579 -0.0182 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.5816 0.1772 0.2003 -0.0041 -0.0768 -0.0042 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.5958 0.2026 0.2091 -0.0169 -0.0757 0.0040  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.6027 0.2117 0.2138 -0.0146 -0.0737 0.0077  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.5949 0.2168 0.2194 -0.0191 -0.0809 0.0172  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.6146 0.1861 0.2319 -0.0214 -0.0582 -0.0167 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.6411 0.1933 0.2500 -0.0338 -0.0405 -0.0218 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.6660 0.2127 0.2408 -0.0493 -0.0398 -0.0194 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.6509 0.2119 0.2261 -0.0455 -0.0497 -0.0144 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.6691 0.2121 0.3060 -0.0269 -0.0325 -0.0241 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.7296 0.2685 0.4115 -0.0185 -0.0285 -0.0228 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.7859 0.3185 0.5077 -0.0132 -0.0253 -0.0185 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.8275 0.3552 0.6092 -0.0078 -0.0176 -0.0121 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.8463 0.3537 0.6511 -0.0111 0.0181  -0.0141 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.8208 0.3268 0.6937 -0.0046 0.0263  -0.0045 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.8510 0.3331 0.6087 -0.0230 0.0472  -0.0242 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.6994 0.2168 0.2414 -0.0685 -0.0261 -0.0227 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.7408 0.2399 0.2414 -0.0894 -0.0272 -0.0199 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.7937 0.2507 0.2781 -0.0962 0.0042  -0.0312 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.7818 0.2362 0.3042 -0.0812 0.0225  -0.0368 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.7661 0.2505 0.2266 -0.1131 -0.0404 -0.0116 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.7700 0.2095 0.1982 -0.1250 -0.0185 -0.0209 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.8487 0.2693 0.2809 -0.1194 0.0114  -0.0324 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.9011 0.2707 0.3120 -0.1269 0.0495  -0.0433 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.9347 0.2598 0.3307 -0.1326 0.0824  -0.0512 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.9626 0.2469 0.3628 -0.1316 0.1242  -0.0592 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.9769 0.3026 0.3152 -0.1571 0.0494  -0.0430 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 1.0816 0.3694 0.3476 -0.1898 0.0341  -0.0373 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 1.2083 0.4551 0.4033 -0.2236 0.0205  -0.0316 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 1.2314 0.5035 0.4222 -0.2375 -0.0217 -0.0141 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 1.2548 0.4332 0.3949 -0.2391 0.0571  -0.0439 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.9275 0.2554 0.3061 -0.1396 0.0678  -0.0479 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.9452 0.2257 0.3013 -0.1475 0.0997  -0.0551 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.8783 0.1930 0.3151 -0.1191 0.1096  -0.0553 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.9025 0.1787 0.3360 -0.1218 0.1436  -0.0607 118 HIS   A O   
878  C CB  . HIS   A 112 ? 1.0034 0.2566 0.2884 -0.1754 0.0791  -0.0502 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 1.1170 0.3258 0.3166 -0.2113 0.0626  -0.0452 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 1.1421 0.3838 0.3339 -0.2241 0.0120  -0.0278 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 1.2027 0.3336 0.3247 -0.2381 0.0901  -0.0530 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 1.2001 0.3866 0.3126 -0.2598 0.0035  -0.0235 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 1.2460 0.3613 0.3062 -0.2703 0.0496  -0.0400 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.7996 0.1786 0.3018 -0.0950 0.0799  -0.0485 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.7439 0.1527 0.3173 -0.0725 0.0791  -0.0455 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.6948 0.1541 0.2875 -0.0606 0.0384  -0.0386 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.6883 0.1698 0.2614 -0.0625 0.0127  -0.0344 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.6579 0.1313 0.2922 -0.0483 0.0358  -0.0364 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.6385 0.1484 0.2892 -0.0369 0.0039  -0.0310 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.6423 0.1537 0.2477 -0.0486 -0.0077 -0.0297 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.6686 0.1530 0.2464 -0.0618 0.0071  -0.0327 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.6361 0.1537 0.3437 -0.0238 0.0041  -0.0275 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.6383 0.1805 0.3454 -0.0162 -0.0248 -0.0238 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.6149 0.1375 0.3806 -0.0133 0.0021  -0.0208 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.6189 0.1567 0.2172 -0.0452 -0.0321 -0.0233 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.6311 0.1770 0.2053 -0.0549 -0.0471 -0.0155 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.6115 0.1782 0.2114 -0.0405 -0.0578 -0.0124 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.6158 0.1808 0.2054 -0.0475 -0.0619 -0.0084 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.6436 0.2058 0.2096 -0.0590 -0.0624 -0.0058 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.6541 0.2336 0.2214 -0.0648 -0.0809 0.0095  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.6653 0.2013 0.1963 -0.0782 -0.0548 -0.0078 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.5815 0.1612 0.2080 -0.0229 -0.0637 -0.0135 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.5701 0.1588 0.2110 -0.0113 -0.0728 -0.0115 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.5657 0.1525 0.2155 0.0015  -0.0820 -0.0119 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.5538 0.1342 0.2078 0.0021  -0.0825 -0.0137 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.5655 0.1501 0.2121 0.0096  -0.0894 -0.0097 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.5738 0.1391 0.2094 0.0163  -0.0998 -0.0099 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.5796 0.1346 0.1899 0.0229  -0.0944 -0.0066 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.5637 0.1297 0.1801 0.0254  -0.0874 -0.0026 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.5939 0.1464 0.2444 0.0165  -0.1134 -0.0102 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.6022 0.1631 0.2603 0.0176  -0.1093 -0.0105 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.5905 0.1444 0.2784 0.0125  -0.1173 -0.0088 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.6249 0.1680 0.2867 0.0183  -0.1249 -0.0088 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.5968 0.1228 0.1769 0.0253  -0.0956 -0.0071 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.6215 0.1225 0.1721 0.0319  -0.0803 -0.0044 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.6366 0.1206 0.1770 0.0346  -0.0803 -0.0049 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.6353 0.1047 0.1692 0.0295  -0.0998 -0.0082 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.6635 0.1180 0.1664 0.0303  -0.0794 -0.0067 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.6921 0.1095 0.1610 0.0374  -0.0513 -0.0044 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.6693 0.1414 0.1838 0.0280  -0.0794 -0.0062 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.6489 0.1363 0.1960 0.0424  -0.0591 0.0010  125 SER   A N   
922  C CA  . SER   A 119 ? 0.6745 0.1463 0.2142 0.0458  -0.0552 0.0011  125 SER   A CA  
923  C C   . SER   A 119 ? 0.7404 0.1740 0.2561 0.0548  -0.0232 0.0056  125 SER   A C   
924  O O   . SER   A 119 ? 0.7706 0.1652 0.2547 0.0561  -0.0165 0.0026  125 SER   A O   
925  C CB  . SER   A 119 ? 0.6354 0.1553 0.2233 0.0456  -0.0599 0.0065  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.6464 0.1550 0.2323 0.0500  -0.0546 0.0079  125 SER   A OG  
927  N N   . THR   A 120 ? 0.7567 0.2013 0.2940 0.0612  0.0001  0.0148  126 THR   A N   
928  C CA  . THR   A 120 ? 0.8101 0.2170 0.3383 0.0718  0.0414  0.0223  126 THR   A CA  
929  C C   . THR   A 120 ? 0.8334 0.2290 0.3560 0.0734  0.0594  0.0255  126 THR   A C   
930  O O   . THR   A 120 ? 0.8114 0.2374 0.3445 0.0666  0.0370  0.0233  126 THR   A O   
931  C CB  . THR   A 120 ? 0.8061 0.2497 0.4038 0.0820  0.0601  0.0407  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.7895 0.2840 0.4538 0.0832  0.0615  0.0588  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.8027 0.2776 0.4208 0.0782  0.0349  0.0399  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.8774 0.2277 0.3870 0.0827  0.1039  0.0316  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.9187 0.2536 0.4285 0.0861  0.1301  0.0369  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.9812 0.2482 0.4693 0.0973  0.1903  0.0426  127 GLY   A C   
937  O O   . GLY   A 121 ? 1.0009 0.2281 0.4669 0.1015  0.2113  0.0410  127 GLY   A O   
938  N N   . GLY   A 122 ? 1.0151 0.2621 0.5065 0.1017  0.2225  0.0488  128 GLY   A N   
939  C CA  . GLY   A 122 ? 1.0814 0.2537 0.5523 0.1128  0.2911  0.0548  128 GLY   A CA  
940  C C   . GLY   A 122 ? 1.0702 0.2756 0.6321 0.1255  0.3284  0.0789  128 GLY   A C   
941  O O   . GLY   A 122 ? 1.0184 0.3138 0.6883 0.1289  0.3059  0.1002  128 GLY   A O   
942  N N   . ASN   A 123 ? 1.1169 0.2446 0.6324 0.1298  0.3838  0.0772  129 ASN   A N   
943  C CA  . ASN   A 123 ? 1.0914 0.2355 0.6914 0.1428  0.4303  0.1013  129 ASN   A CA  
944  C C   . ASN   A 123 ? 1.0251 0.2526 0.6870 0.1368  0.3869  0.1105  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.9824 0.2681 0.7611 0.1454  0.3998  0.1403  129 ASN   A O   
946  C CB  . ASN   A 123 ? 1.0796 0.2536 0.7980 0.1610  0.4717  0.1321  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 1.2157 0.2896 0.8689 0.1687  0.5328  0.1236  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 1.3162 0.2812 0.8716 0.1677  0.5872  0.1094  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 1.2034 0.3035 0.9004 0.1744  0.5263  0.1317  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 1.0154 0.2399 0.5990 0.1212  0.3394  0.0875  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.9551 0.2473 0.5822 0.1140  0.3006  0.0928  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.8744 0.2600 0.5679 0.1067  0.2414  0.1004  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.8458 0.2864 0.5784 0.0988  0.2100  0.1073  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.8409 0.2374 0.5379 0.1071  0.2262  0.0982  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.7851 0.2545 0.5272 0.0978  0.1735  0.1029  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.7947 0.2437 0.4555 0.0885  0.1392  0.0753  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.8593 0.2426 0.4474 0.0904  0.1560  0.0598  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.7518 0.2561 0.5801 0.1055  0.1828  0.1284  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.7435 0.2736 0.6789 0.1149  0.2153  0.1649  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.7296 0.2593 0.7322 0.1281  0.2463  0.1873  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.7137 0.3154 0.7177 0.1003  0.1708  0.1859  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.7241 0.2238 0.3981 0.0767  0.0927  0.0713  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.7025 0.1946 0.3267 0.0687  0.0609  0.0513  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.6538 0.2010 0.3269 0.0626  0.0332  0.0594  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.6160 0.2075 0.3378 0.0554  0.0195  0.0742  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.7095 0.1880 0.2842 0.0591  0.0384  0.0347  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.6862 0.2073 0.2985 0.0532  0.0279  0.0426  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.7080 0.1855 0.2544 0.0510  0.0055  0.0201  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.6533 0.1903 0.3071 0.0629  0.0243  0.0507  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.6293 0.2054 0.3148 0.0563  0.0009  0.0556  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.6383 0.2152 0.2912 0.0466  -0.0268 0.0376  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.6776 0.2195 0.2869 0.0479  -0.0296 0.0230  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.5989 0.2097 0.2729 0.0345  -0.0470 0.0410  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.5888 0.1998 0.2433 0.0252  -0.0647 0.0268  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.5688 0.1934 0.2353 0.0186  -0.0742 0.0294  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.5558 0.1998 0.2442 0.0104  -0.0797 0.0444  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.5719 0.1927 0.2233 0.0137  -0.0719 0.0250  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.5752 0.1859 0.2172 0.0185  -0.0638 0.0240  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.5892 0.1748 0.2040 0.0221  -0.0653 0.0112  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.5696 0.1952 0.2330 0.0166  -0.0579 0.0385  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.5990 0.1703 0.1986 0.0245  -0.0588 0.0105  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.5762 0.1906 0.2298 0.0206  -0.0482 0.0372  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.5857 0.1713 0.2028 0.0246  -0.0478 0.0219  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.5691 0.1806 0.2221 0.0201  -0.0784 0.0172  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.5699 0.1885 0.2293 0.0137  -0.0844 0.0173  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.5795 0.1987 0.2302 -0.0020 -0.0880 0.0127  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.5876 0.1958 0.2333 -0.0020 -0.0851 0.0021  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.5829 0.1844 0.2353 0.0207  -0.0861 0.0072  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.5870 0.2124 0.2341 -0.0172 -0.0938 0.0228  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.6167 0.2256 0.2372 -0.0365 -0.0930 0.0181  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.6354 0.2242 0.2458 -0.0390 -0.0820 0.0055  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.6384 0.2307 0.2591 -0.0331 -0.0835 0.0059  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.6429 0.2521 0.2509 -0.0579 -0.1083 0.0356  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.7326 0.3088 0.2932 -0.0839 -0.1077 0.0320  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.7293 0.2990 0.2794 -0.0871 -0.1026 0.0275  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.8096 0.3592 0.3366 -0.1028 -0.1106 0.0335  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.6476 0.2141 0.2444 -0.0459 -0.0669 -0.0050 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.6657 0.2079 0.2614 -0.0487 -0.0480 -0.0145 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.7003 0.1985 0.2463 -0.0733 -0.0300 -0.0184 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.7138 0.1813 0.2543 -0.0774 -0.0049 -0.0262 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.6541 0.1987 0.2916 -0.0330 -0.0373 -0.0214 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.6465 0.2157 0.3138 -0.0153 -0.0568 -0.0179 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.6603 0.1964 0.2973 -0.0351 -0.0277 -0.0244 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.7121 0.1999 0.2200 -0.0911 -0.0403 -0.0123 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.7593 0.1913 0.2022 -0.1195 -0.0252 -0.0158 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.8011 0.1897 0.1916 -0.1422 -0.0218 -0.0144 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.8464 0.1711 0.1776 -0.1633 0.0052  -0.0230 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.7713 0.2019 0.1846 -0.1367 -0.0461 -0.0057 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.7479 0.2065 0.1975 -0.1191 -0.0431 -0.0092 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.7547 0.2134 0.1787 -0.1374 -0.0655 0.0034  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.7427 0.2471 0.2041 -0.1311 -0.0966 0.0226  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.7493 0.2697 0.2176 -0.1412 -0.1197 0.0403  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.7683 0.2619 0.1987 -0.1606 -0.1203 0.0400  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.6828 0.2442 0.2004 -0.1319 -0.1399 0.0601  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.7945 0.2095 0.2010 -0.1391 -0.0457 -0.0037 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.8422 0.2165 0.1994 -0.1609 -0.0461 -0.0008 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.8599 0.2167 0.2319 -0.1483 -0.0110 -0.0155 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.8973 0.2037 0.2164 -0.1683 0.0010  -0.0174 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.8351 0.2465 0.2135 -0.1621 -0.0856 0.0197  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.8222 0.2938 0.2785 -0.1269 -0.0887 0.0198  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.7967 0.3004 0.2962 -0.1039 -0.0830 0.0141  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.8312 0.3119 0.2983 -0.1247 -0.0984 0.0266  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.8222 0.2167 0.2657 -0.1175 0.0032  -0.0234 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.8197 0.2049 0.2972 -0.1044 0.0327  -0.0322 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.8663 0.1920 0.3186 -0.1151 0.0798  -0.0430 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.8437 0.1807 0.3514 -0.0982 0.1000  -0.0467 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.7630 0.2041 0.3247 -0.0734 0.0223  -0.0313 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.7517 0.2403 0.3317 -0.0621 -0.0155 -0.0220 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.7255 0.2497 0.3651 -0.0379 -0.0256 -0.0220 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.7648 0.2505 0.3302 -0.0677 -0.0239 -0.0174 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.9293 0.1838 0.2939 -0.1455 0.0981  -0.0464 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.9880 0.1630 0.3035 -0.1618 0.1515  -0.0575 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.9941 0.1567 0.3730 -0.1431 0.2019  -0.0639 141 LEU   A C   
1034 O O   . LEU   A 135 ? 1.0146 0.1335 0.4001 -0.1430 0.2514  -0.0704 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 1.0571 0.1436 0.2464 -0.2038 0.1572  -0.0588 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 1.0884 0.1752 0.2114 -0.2312 0.1022  -0.0456 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 1.1782 0.1501 0.1598 -0.2808 0.1140  -0.0469 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 1.0782 0.2029 0.2261 -0.2246 0.0824  -0.0419 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.9669 0.1675 0.3995 -0.1271 0.1907  -0.0598 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.9593 0.1560 0.4661 -0.1097 0.2313  -0.0608 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.9441 0.1906 0.5637 -0.0821 0.2345  -0.0544 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.9335 0.1704 0.6260 -0.0701 0.2727  -0.0506 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.9286 0.1510 0.4558 -0.1034 0.2122  -0.0567 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.8749 0.1745 0.4347 -0.0893 0.1506  -0.0485 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.8922 0.2055 0.3972 -0.1011 0.1097  -0.0444 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.8179 0.1825 0.4714 -0.0627 0.1262  -0.0415 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.8521 0.2333 0.4122 -0.0806 0.0695  -0.0371 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.8136 0.2222 0.4547 -0.0588 0.0775  -0.0366 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.7882 0.1730 0.5350 -0.0442 0.1392  -0.0359 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.7825 0.2431 0.4835 -0.0386 0.0465  -0.0305 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.7585 0.1985 0.5660 -0.0269 0.0985  -0.0272 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.7560 0.2281 0.5320 -0.0249 0.0550  -0.0265 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.9432 0.2403 0.5822 -0.0732 0.1940  -0.0503 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.9282 0.2662 0.6640 -0.0516 0.1899  -0.0420 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.9921 0.2834 0.7516 -0.0529 0.2467  -0.0433 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.9548 0.2693 0.8159 -0.0356 0.2559  -0.0317 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.8994 0.2853 0.6279 -0.0463 0.1402  -0.0393 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.8732 0.3099 0.6069 -0.0377 0.0889  -0.0344 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.8657 0.3322 0.5780 -0.0357 0.0538  -0.0330 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.8364 0.3043 0.6560 -0.0202 0.0757  -0.0247 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 1.0855 0.3064 0.7503 -0.0755 0.2829  -0.0551 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 1.1504 0.3100 0.8161 -0.0804 0.3454  -0.0590 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 1.2147 0.3084 0.8916 -0.0835 0.4148  -0.0611 144 ASP   A C   
1064 O O   . ASP   A 138 ? 1.2182 0.2781 0.9531 -0.0758 0.4727  -0.0573 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 1.2401 0.3419 0.7796 -0.1084 0.3499  -0.0711 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 1.2836 0.4383 0.8295 -0.1032 0.3024  -0.0677 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 1.2447 0.4488 0.8880 -0.0801 0.2953  -0.0589 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 1.3519 0.4962 0.8073 -0.1239 0.2708  -0.0716 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 1.2668 0.3337 0.8834 -0.0966 0.4145  -0.0667 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 1.3231 0.3178 0.9350 -0.1023 0.4834  -0.0701 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 1.2844 0.3360 1.0113 -0.0793 0.4735  -0.0570 145 GLU   A C   
1072 O O   . GLU   A 139 ? 1.3116 0.3133 1.0518 -0.0808 0.5282  -0.0573 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.4513 0.3609 0.9037 -0.1380 0.4927  -0.0846 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.5205 0.4831 0.9354 -0.1437 0.4190  -0.0821 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.6939 0.5870 0.9509 -0.1834 0.4021  -0.0898 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.7264 0.6333 0.9492 -0.1922 0.3649  -0.0865 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.7777 0.6001 0.9454 -0.2076 0.4233  -0.0970 145 GLU   A OE2 
1078 N N1  . A1BPR B .   ? 1.0264 0.1844 0.3263 0.0640  0.0875  -0.0041 201 A1BPR A N1  
1079 N N3  . A1BPR B .   ? 1.0372 0.2387 0.3286 0.0449  0.0305  -0.0097 201 A1BPR A N3  
1080 C C4  . A1BPR B .   ? 1.0781 0.1633 0.2891 0.0469  0.0647  -0.0154 201 A1BPR A C4  
1081 C C5  . A1BPR B .   ? 1.0289 0.1812 0.3280 0.0668  0.1065  -0.0013 201 A1BPR A C5  
1082 C C6  . A1BPR B .   ? 1.1145 0.1673 0.3036 0.0529  0.1144  -0.0119 201 A1BPR A C6  
1083 C C7  . A1BPR B .   ? 1.1089 0.1763 0.3101 0.0546  0.1216  -0.0093 201 A1BPR A C7  
1084 C C8  . A1BPR B .   ? 1.1417 0.1468 0.3079 0.0607  0.1770  -0.0071 201 A1BPR A C8  
1085 C C10 . A1BPR B .   ? 1.0907 0.1890 0.3234 0.0591  0.1394  -0.0026 201 A1BPR A C10 
1086 C C13 . A1BPR B .   ? 0.9687 0.2057 0.3596 0.0751  0.0835  0.0065  201 A1BPR A C13 
1087 O O1  . A1BPR B .   ? 0.9738 0.1926 0.3527 0.0776  0.1153  0.0105  201 A1BPR A O1  
1088 C C3  . A1BPR B .   ? 1.0489 0.1897 0.2952 0.0378  0.0085  -0.0169 201 A1BPR A C3  
1089 C C2  . A1BPR B .   ? 0.9860 0.2118 0.3257 0.0514  0.0092  -0.0096 201 A1BPR A C2  
1090 C C1  . A1BPR B .   ? 0.9378 0.2262 0.3509 0.0652  0.0310  0.0013  201 A1BPR A C1  
1091 C C   . A1BPR B .   ? 0.8808 0.2437 0.3741 0.0718  0.0226  0.0109  201 A1BPR A C   
1092 O O   . A1BPR B .   ? 0.8731 0.2345 0.3865 0.0800  0.0424  0.0179  201 A1BPR A O   
1093 N N   . A1BPR B .   ? 0.8429 0.2641 0.3774 0.0666  -0.0053 0.0119  201 A1BPR A N   
1094 C C12 . A1BPR B .   ? 1.0684 0.2098 0.3195 0.0507  0.0783  -0.0084 201 A1BPR A C12 
1095 O O2  . A1BPR B .   ? 1.0161 0.2619 0.3402 0.0432  0.0130  -0.0083 201 A1BPR A O2  
1096 N N2  . A1BPR B .   ? 1.0309 0.2525 0.3391 0.0475  0.0437  -0.0059 201 A1BPR A N2  
1097 C C11 . A1BPR B .   ? 1.0612 0.2164 0.3254 0.0528  0.0874  -0.0054 201 A1BPR A C11 
1098 C C9  . A1BPR B .   ? 1.1348 0.1562 0.3187 0.0633  0.1861  -0.0034 201 A1BPR A C9  
# 
