data_7HYG
# 
_entry.id   7HYG 
# 
_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   7HYG         pdb_00007hyg 10.2210/pdb7hyg/pdb 
WWPDB D_1001408088 ?            ?                   
# 
_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                        7HYG 
_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-hydroxypyridin-3-yl)acetyl]piperidine-3-carboxamide' 263.292   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                       65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                             78.133    2  ?         ? ? ? 
5 water       nat water                                                            18.015    91 ?         ? ? ? 
# 
_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-hydroxypyridin-3-yl)acetyl]piperidine-3-carboxamide' A1BN4 
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 
A1BN4 non-polymer         . '(3S)-1-[(2-hydroxypyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C13 H17 N3 O3'  263.292 
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        A1BN4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN4 
_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 A1BN4 1  201 201 A1BN4 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 1   DMS   DMS A . 
E 4 DMS   1  204 6   DMS   DMS A . 
F 5 HOH   1  301 91  HOH   HOH A . 
F 5 HOH   2  302 59  HOH   HOH A . 
F 5 HOH   3  303 22  HOH   HOH A . 
F 5 HOH   4  304 50  HOH   HOH A . 
F 5 HOH   5  305 9   HOH   HOH A . 
F 5 HOH   6  306 36  HOH   HOH A . 
F 5 HOH   7  307 79  HOH   HOH A . 
F 5 HOH   8  308 13  HOH   HOH A . 
F 5 HOH   9  309 29  HOH   HOH A . 
F 5 HOH   10 310 14  HOH   HOH A . 
F 5 HOH   11 311 42  HOH   HOH A . 
F 5 HOH   12 312 47  HOH   HOH A . 
F 5 HOH   13 313 18  HOH   HOH A . 
F 5 HOH   14 314 32  HOH   HOH A . 
F 5 HOH   15 315 54  HOH   HOH A . 
F 5 HOH   16 316 7   HOH   HOH A . 
F 5 HOH   17 317 27  HOH   HOH A . 
F 5 HOH   18 318 12  HOH   HOH A . 
F 5 HOH   19 319 8   HOH   HOH A . 
F 5 HOH   20 320 51  HOH   HOH A . 
F 5 HOH   21 321 55  HOH   HOH A . 
F 5 HOH   22 322 19  HOH   HOH A . 
F 5 HOH   23 323 17  HOH   HOH A . 
F 5 HOH   24 324 93  HOH   HOH A . 
F 5 HOH   25 325 24  HOH   HOH A . 
F 5 HOH   26 326 16  HOH   HOH A . 
F 5 HOH   27 327 57  HOH   HOH A . 
F 5 HOH   28 328 40  HOH   HOH A . 
F 5 HOH   29 329 82  HOH   HOH A . 
F 5 HOH   30 330 89  HOH   HOH A . 
F 5 HOH   31 331 37  HOH   HOH A . 
F 5 HOH   32 332 2   HOH   HOH A . 
F 5 HOH   33 333 23  HOH   HOH A . 
F 5 HOH   34 334 34  HOH   HOH A . 
F 5 HOH   35 335 78  HOH   HOH A . 
F 5 HOH   36 336 11  HOH   HOH A . 
F 5 HOH   37 337 75  HOH   HOH A . 
F 5 HOH   38 338 21  HOH   HOH A . 
F 5 HOH   39 339 73  HOH   HOH A . 
F 5 HOH   40 340 25  HOH   HOH A . 
F 5 HOH   41 341 72  HOH   HOH A . 
F 5 HOH   42 342 10  HOH   HOH A . 
F 5 HOH   43 343 88  HOH   HOH A . 
F 5 HOH   44 344 86  HOH   HOH A . 
F 5 HOH   45 345 58  HOH   HOH A . 
F 5 HOH   46 346 35  HOH   HOH A . 
F 5 HOH   47 347 87  HOH   HOH A . 
F 5 HOH   48 348 49  HOH   HOH A . 
F 5 HOH   49 349 80  HOH   HOH A . 
F 5 HOH   50 350 53  HOH   HOH A . 
F 5 HOH   51 351 48  HOH   HOH A . 
F 5 HOH   52 352 76  HOH   HOH A . 
F 5 HOH   53 353 39  HOH   HOH A . 
F 5 HOH   54 354 4   HOH   HOH A . 
F 5 HOH   55 355 77  HOH   HOH A . 
F 5 HOH   56 356 20  HOH   HOH A . 
F 5 HOH   57 357 74  HOH   HOH A . 
F 5 HOH   58 358 6   HOH   HOH A . 
F 5 HOH   59 359 71  HOH   HOH A . 
F 5 HOH   60 360 70  HOH   HOH A . 
F 5 HOH   61 361 56  HOH   HOH A . 
F 5 HOH   62 362 85  HOH   HOH A . 
F 5 HOH   63 363 67  HOH   HOH A . 
F 5 HOH   64 364 3   HOH   HOH A . 
F 5 HOH   65 365 30  HOH   HOH A . 
F 5 HOH   66 366 5   HOH   HOH A . 
F 5 HOH   67 367 84  HOH   HOH A . 
F 5 HOH   68 368 60  HOH   HOH A . 
F 5 HOH   69 369 38  HOH   HOH A . 
F 5 HOH   70 370 33  HOH   HOH A . 
F 5 HOH   71 371 15  HOH   HOH A . 
F 5 HOH   72 372 81  HOH   HOH A . 
F 5 HOH   73 373 45  HOH   HOH A . 
F 5 HOH   74 374 63  HOH   HOH A . 
F 5 HOH   75 375 92  HOH   HOH A . 
F 5 HOH   76 376 31  HOH   HOH A . 
F 5 HOH   77 377 64  HOH   HOH A . 
F 5 HOH   78 378 41  HOH   HOH A . 
F 5 HOH   79 379 28  HOH   HOH A . 
F 5 HOH   80 380 69  HOH   HOH A . 
F 5 HOH   81 381 43  HOH   HOH A . 
F 5 HOH   82 382 66  HOH   HOH A . 
F 5 HOH   83 383 68  HOH   HOH A . 
F 5 HOH   84 384 94  HOH   HOH A . 
F 5 HOH   85 385 65  HOH   HOH A . 
F 5 HOH   86 386 61  HOH   HOH A . 
F 5 HOH   87 387 52  HOH   HOH A . 
F 5 HOH   88 388 26  HOH   HOH A . 
F 5 HOH   89 389 90  HOH   HOH A . 
F 5 HOH   90 390 44  HOH   HOH A . 
F 5 HOH   91 391 83  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           7HYG 
_cell.length_a           73.019 
_cell.length_b           61.436 
_cell.length_c           32.729 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.46 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYG 
_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          7HYG 
_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   46.65 
_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                     7HYG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.97 
_reflns.d_resolution_high            1.75 
_reflns.number_obs                   14727 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.309 
_reflns.pdbx_netI_over_sigmaI        3.6 
_reflns.pdbx_redundancy              4.9 
_reflns.pdbx_Rrim_I_all              0.345 
_reflns.pdbx_Rpim_I_all              0.151 
_reflns.pdbx_CC_half                 0.973 
_reflns.pdbx_number_measured_all     72641 
_reflns.pdbx_chi_squared             0.87 
_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                  1.75 
_reflns_shell.d_res_low                   1.84 
_reflns_shell.number_measured_all         9901 
_reflns_shell.number_unique_obs           2151 
_reflns_shell.Rmerge_I_obs                1.893 
_reflns_shell.pdbx_chi_squared            0.86 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             2.133 
_reflns_shell.pdbx_Rpim_I_all             0.969 
_reflns_shell.pdbx_CC_half                0.433 
_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                                 7HYG 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14570 
_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                             15.36 
_refine.ls_d_res_high                            1.746 
_refine.ls_percent_reflns_obs                    99.1 
_refine.ls_R_factor_obs                          0.2100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2087 
_refine.ls_R_factor_R_free                       0.2343 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.950 
_refine.ls_number_reflns_R_free                  721 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.922 
_refine.B_iso_mean                               23.00 
_refine.aniso_B[1][1]                            -3.55100 
_refine.aniso_B[2][2]                            1.02980 
_refine.aniso_B[3][3]                            2.52120 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.35730 
_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             0.127 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.117 
_refine.pdbx_overall_SU_R_Blow_DPI               0.130 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.118 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYG 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_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         28 
_refine_hist.number_atoms_solvent             91 
_refine_hist.number_atoms_total               1193 
_refine_hist.d_res_high                       1.746 
_refine_hist.d_res_low                        15.36 
# 
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  1134 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.92  ? 2.00  1543 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  379  '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  205  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1134 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.65  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.79 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  '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  893  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   37 
_refine_ls_shell.d_res_high                       1.75 
_refine_ls_shell.d_res_low                        1.76 
_refine_ls_shell.number_reflns_R_work             380 
_refine_ls_shell.R_factor_R_work                  0.3063 
_refine_ls_shell.percent_reflns_obs               87.14 
_refine_ls_shell.R_factor_R_free                  0.3940 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.17 
_refine_ls_shell.number_reflns_R_free             25 
_refine_ls_shell.number_reflns_all                405 
_refine_ls_shell.R_factor_all                     0.3121 
# 
_struct.entry_id                  7HYG 
_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-0035287-001 (A71EV2A-x4372)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYG 
_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 4 ? 
F 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              7HYG 
_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,F 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_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 ? ? ? ? ? ? ? 2.294 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
# 
_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_555 109.3 ? 
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_555 106.3 ? 
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_555 117.0 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.3 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.5 ? 
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_555 115.2 ? 
# 
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 SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HYG 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     376 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     388 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_556 
_pdbx_validate_symm_contact.dist              2.16 
# 
_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         15.0771 
_pdbx_refine_tls.origin_y         6.5884 
_pdbx_refine_tls.origin_z         14.3502 
_pdbx_refine_tls.T[1][1]          -0.0562 
_pdbx_refine_tls.T[2][2]          -0.0281 
_pdbx_refine_tls.T[3][3]          -0.0009 
_pdbx_refine_tls.T[1][2]          0.0004 
_pdbx_refine_tls.T[1][3]          -0.0128 
_pdbx_refine_tls.T[2][3]          -0.0051 
_pdbx_refine_tls.L[1][1]          1.4040 
_pdbx_refine_tls.L[2][2]          2.8753 
_pdbx_refine_tls.L[3][3]          0.5872 
_pdbx_refine_tls.L[1][2]          0.8822 
_pdbx_refine_tls.L[1][3]          -0.1341 
_pdbx_refine_tls.L[2][3]          -0.3334 
_pdbx_refine_tls.S[1][1]          -0.0982 
_pdbx_refine_tls.S[1][2]          0.0029 
_pdbx_refine_tls.S[1][3]          0.0872 
_pdbx_refine_tls.S[2][1]          0.0251 
_pdbx_refine_tls.S[2][2]          0.0718 
_pdbx_refine_tls.S[2][3]          -0.1146 
_pdbx_refine_tls.S[3][1]          -0.0007 
_pdbx_refine_tls.S[3][2]          -0.0786 
_pdbx_refine_tls.S[3][3]          0.0264 
# 
_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 
A1BN4 N1   N  N N 1   
A1BN4 C4   C  N N 2   
A1BN4 C5   C  N N 3   
A1BN4 C6   C  N N 4   
A1BN4 C7   C  Y N 5   
A1BN4 C8   C  Y N 6   
A1BN4 C10  C  Y N 7   
A1BN4 O1   O  N N 8   
A1BN4 C3   C  N N 9   
A1BN4 C2   C  N N 10  
A1BN4 C12  C  N N 11  
A1BN4 C1   C  N S 12  
A1BN4 C    C  N N 13  
A1BN4 O    O  N N 14  
A1BN4 N    N  N N 15  
A1BN4 C11  C  Y N 16  
A1BN4 O2   O  N N 17  
A1BN4 N2   N  Y N 18  
A1BN4 C9   C  Y N 19  
A1BN4 H8   H  N N 20  
A1BN4 H7   H  N N 21  
A1BN4 H10  H  N N 22  
A1BN4 H9   H  N N 23  
A1BN4 H11  H  N N 24  
A1BN4 H13  H  N N 25  
A1BN4 H6   H  N N 26  
A1BN4 H5   H  N N 27  
A1BN4 H4   H  N N 28  
A1BN4 H3   H  N N 29  
A1BN4 H16  H  N N 30  
A1BN4 H15  H  N N 31  
A1BN4 H    H  N N 32  
A1BN4 H1   H  N N 33  
A1BN4 H2   H  N N 34  
A1BN4 H14  H  N N 35  
A1BN4 H12  H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
THR   N    N  N N 350 
THR   CA   C  N S 351 
THR   C    C  N N 352 
THR   O    O  N N 353 
THR   CB   C  N R 354 
THR   OG1  O  N N 355 
THR   CG2  C  N N 356 
THR   OXT  O  N N 357 
THR   H    H  N N 358 
THR   H2   H  N N 359 
THR   HA   H  N N 360 
THR   HB   H  N N 361 
THR   HG1  H  N N 362 
THR   HG21 H  N N 363 
THR   HG22 H  N N 364 
THR   HG23 H  N N 365 
THR   HXT  H  N N 366 
TRP   N    N  N N 367 
TRP   CA   C  N S 368 
TRP   C    C  N N 369 
TRP   O    O  N N 370 
TRP   CB   C  N N 371 
TRP   CG   C  Y N 372 
TRP   CD1  C  Y N 373 
TRP   CD2  C  Y N 374 
TRP   NE1  N  Y N 375 
TRP   CE2  C  Y N 376 
TRP   CE3  C  Y N 377 
TRP   CZ2  C  Y N 378 
TRP   CZ3  C  Y N 379 
TRP   CH2  C  Y N 380 
TRP   OXT  O  N N 381 
TRP   H    H  N N 382 
TRP   H2   H  N N 383 
TRP   HA   H  N N 384 
TRP   HB2  H  N N 385 
TRP   HB3  H  N N 386 
TRP   HD1  H  N N 387 
TRP   HE1  H  N N 388 
TRP   HE3  H  N N 389 
TRP   HZ2  H  N N 390 
TRP   HZ3  H  N N 391 
TRP   HH2  H  N N 392 
TRP   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
ZN    ZN   ZN N N 437 
# 
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 
A1BN4 N   C    sing N N 1   
A1BN4 O   C    doub N N 2   
A1BN4 C   C1   sing N N 3   
A1BN4 C1  C2   sing N N 4   
A1BN4 C2  C3   sing N N 5   
A1BN4 C3  C4   sing N N 6   
A1BN4 C4  N1   sing N N 7   
A1BN4 N1  C5   sing N N 8   
A1BN4 C5  O1   doub N N 9   
A1BN4 C6  C5   sing N N 10  
A1BN4 C7  C6   sing N N 11  
A1BN4 C7  C8   doub Y N 12  
A1BN4 C8  C9   sing Y N 13  
A1BN4 C9  C10  doub Y N 14  
A1BN4 C10 N2   sing Y N 15  
A1BN4 N2  C11  doub Y N 16  
A1BN4 C11 C7   sing Y N 17  
A1BN4 O2  C11  sing N N 18  
A1BN4 C12 N1   sing N N 19  
A1BN4 C1  C12  sing N N 20  
A1BN4 C4  H8   sing N N 21  
A1BN4 C4  H7   sing N N 22  
A1BN4 C6  H10  sing N N 23  
A1BN4 C6  H9   sing N N 24  
A1BN4 C8  H11  sing N N 25  
A1BN4 C10 H13  sing N N 26  
A1BN4 C3  H6   sing N N 27  
A1BN4 C3  H5   sing N N 28  
A1BN4 C2  H4   sing N N 29  
A1BN4 C2  H3   sing N N 30  
A1BN4 C12 H16  sing N N 31  
A1BN4 C12 H15  sing N N 32  
A1BN4 C1  H    sing N N 33  
A1BN4 N   H1   sing N N 34  
A1BN4 N   H2   sing N N 35  
A1BN4 O2  H14  sing N N 36  
A1BN4 C9  H12  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7HYG 
_atom_sites.fract_transf_matrix[1][1]   0.013695 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000828 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016277 
_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]   0.030610 
_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   ? 18.761 5.959   24.394 1.00 23.80  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.932 6.089   23.529 1.00 24.61  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.033 4.929   22.504 1.00 24.19  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.300 3.947   22.623 1.00 24.73  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.199 6.209   24.374 1.00 26.69  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.233 5.106   25.265 1.00 29.68  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.899 5.087   21.491 1.00 23.06  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.117 4.093   20.447 1.00 22.43  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.435 4.662   19.070 1.00 22.10  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.004 5.770   18.722 1.00 22.24  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.175 3.892   18.263 1.00 20.98  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.574 4.313   16.925 1.00 20.56  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.525 3.151   15.904 1.00 20.05  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.482 1.989   16.299 1.00 19.89  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.992 4.886   16.982 1.00 19.89  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.554 3.465   14.601 1.00 19.08  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.638 2.469   13.543 1.00 19.44  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.012 2.659   12.901 1.00 19.93  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.404 3.784   12.618 1.00 19.60  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.527 2.644   12.477 1.00 19.94  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.120 2.683   13.097 1.00 19.40  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.656 1.554   11.400 1.00 21.06  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.106 3.337   12.163 1.00 20.77  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.746 1.577   12.679 1.00 20.71  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.070 1.647   12.095 1.00 21.82  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.084 0.901   10.777 1.00 23.31  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.017 -0.324  10.760 1.00 23.61  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.093 1.069   13.070 1.00 21.89  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.184 1.846   14.365 1.00 22.15  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.966 2.992   14.462 1.00 23.11  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.476 1.448   15.488 1.00 22.57  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.066 3.699   15.653 1.00 23.38  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.568 2.146   16.684 1.00 23.32  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.368 3.269   16.762 1.00 23.99  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.418 3.964   17.933 1.00 25.26  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.162 1.635   9.673  1.00 23.71  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.160 1.047   8.340  1.00 24.41  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.292 1.693   7.522  1.00 25.09  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.382 2.922   7.439  1.00 24.83  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.745 1.207   7.693  1.00 25.27  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.277 2.663   7.715  1.00 26.09  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.688 0.619   6.290  1.00 25.91  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.215 0.872   7.002  1.00 25.26  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.362 1.386   6.251  1.00 26.21  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.193 2.359   7.069  1.00 27.16  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.511 2.071   8.227  1.00 27.48  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.450 3.558   6.535  1.00 27.33  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.168 4.587   7.296  1.00 27.76  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.220 5.632   7.888  1.00 26.03  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.582 6.803   8.024  1.00 26.96  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.275 5.215   6.479  1.00 30.50  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.446 4.274   6.380  1.00 36.66  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.987 3.816   7.395  1.00 38.47  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.832 3.927   5.164  1.00 38.47  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.025 5.196   8.294  1.00 23.94  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.025 6.104   8.862  1.00 21.81  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.514 5.656   10.224 1.00 19.38  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.422 4.463   10.507 1.00 19.04  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.820 6.256   7.901  1.00 22.30  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.174 6.825   6.539  1.00 24.40  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.825 8.050   6.420  1.00 25.87  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.818 6.163   5.374  1.00 25.69  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.164 8.569   5.172  1.00 27.07  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.127 6.685   4.121  1.00 27.16  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.796 7.890   4.023  1.00 28.49  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.110 8.392   2.779  1.00 31.17  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.115 6.626   11.046 1.00 17.59  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.478 6.392   12.333 1.00 16.53  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.166 7.203   12.265 1.00 15.73  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.213 8.389   11.980 1.00 15.55  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.400 6.879   13.482 1.00 17.65  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.703 7.265   14.788 1.00 19.63  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.708 7.448   15.918 1.00 22.79  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.218 8.408   16.903 1.00 24.21  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.683 8.089   18.074 1.00 25.91  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.591 6.819   18.445 1.00 24.47  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.248 9.040   18.894 1.00 26.31  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.006 6.561   12.443 1.00 14.97  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.720 7.271   12.382 1.00 14.91  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.175 7.387   13.800 1.00 14.66  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.015 6.370   14.453 1.00 15.44  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.725 6.501   11.474 1.00 15.09  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.392 7.272   11.324 1.00 14.97  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.350 6.210   10.109 1.00 14.64  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.884 8.589   14.271 1.00 13.49  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.380 8.794   15.625 1.00 14.07  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.210 9.753   15.606 1.00 13.62  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.041 10.482  14.621 1.00 14.72  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.487 9.368   16.567 1.00 15.63  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.506 8.308   16.906 1.00 16.88  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.140 10.630  15.974 1.00 16.29  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.439 9.854   16.727 1.00 12.08  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.416 10.894  16.834 1.00 12.48  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.160 12.244  16.824 1.00 14.07  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.204 12.370  17.471 1.00 14.93  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.655 10.784  18.178 1.00 12.56  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.824 9.516   18.299 1.00 12.72  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.307 8.475   18.746 1.00 14.72  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.567 9.574   17.914 1.00 11.88  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.702 13.195  16.013 1.00 14.14  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.344 14.519  15.945 1.00 14.27  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.393 15.209  17.319 1.00 15.78  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.426 15.791  17.654 1.00 16.98  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.637 15.420  14.926 1.00 13.01  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.407 16.685  14.492 1.00 14.26  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.405 17.613  13.793 1.00 16.87  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.991 18.847  13.239 1.00 19.15  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.130 19.985  13.905 1.00 20.00  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.810 20.050  15.192 1.00 18.33  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.614 21.063  13.296 1.00 19.90  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.351 15.045  18.154 1.00 15.57  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.329 15.685  19.486 1.00 16.87  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.299 15.041  20.505 1.00 18.14  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.628 15.670  21.499 1.00 19.68  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.898 15.787  20.058 1.00 17.66  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.329 14.490  20.565 1.00 20.07  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.690 13.600  19.708 1.00 20.93  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.297 13.987  21.831 1.00 21.15  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.309 12.576  20.466 1.00 22.12  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.644 12.761  21.757 1.00 22.31  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.777 13.838  20.239 1.00 18.13  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.749 13.164  21.105 1.00 18.88  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.173 13.194  20.530 1.00 18.87  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.059 12.572  21.117 1.00 19.48  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.326 11.709  21.402 1.00 18.90  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.941 11.560  22.082 1.00 20.50  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.560 10.090  22.255 1.00 21.02  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.895 12.298  23.434 1.00 20.17  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.396 13.838  19.357 1.00 18.36  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.732 13.873  18.754 1.00 18.45  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.726 14.563  19.660 1.00 19.18  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.407 15.574  20.274 1.00 19.65  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.704 14.553  17.392 1.00 18.23  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.928 14.010  19.731 1.00 20.13  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.013 14.497  20.596 1.00 21.37  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.847 15.600  19.899 1.00 22.78  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.716 15.795  18.683 1.00 22.53  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.921 13.284  20.946 1.00 21.53  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.619 12.885  19.763 1.00 21.66  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.148 12.114  21.529 1.00 21.72  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.816 16.217  20.627 1.00 23.59  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.750 17.168  20.030 1.00 25.63  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.521 16.485  18.884 1.00 25.34  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.638 17.048  17.807 1.00 25.61  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.760 17.663  21.089 1.00 28.93  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.251 18.792  21.919 1.00 35.23  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.816 19.974  21.339 1.00 38.04  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.172 18.912  23.268 1.00 37.33  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.450 20.756  22.343 1.00 38.36  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.671 20.174  23.523 1.00 38.92  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.965 15.241  19.105 1.00 25.06  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.700 14.478  18.092 1.00 25.28  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.858 14.167  16.841 1.00 23.74  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.385 14.148  15.731 1.00 23.95  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.258 13.193  18.697 1.00 28.29  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.203 12.532  17.745 1.00 34.05  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.248 13.099  17.414 1.00 36.51  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.812 11.374  17.214 1.00 35.00  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.558 13.939  17.013 1.00 22.05  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.654 13.692  15.880 1.00 20.90  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.581 14.968  15.019 1.00 20.69  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.763 14.895  13.809 1.00 20.61  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.251 13.307  16.379 1.00 20.04  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.121 11.856  16.806 1.00 20.31  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.721 10.977  16.132 1.00 19.75  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.431 11.598  17.813 1.00 20.46  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.390 16.134  15.652 1.00 20.20  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.354 17.413  14.940 1.00 20.60  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.717 17.756  14.297 1.00 22.29  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.749 18.252  13.177 1.00 22.31  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.873 18.547  15.870 1.00 19.33  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.396 18.499  16.139 1.00 18.43  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.773 18.051  17.269 1.00 18.94  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.359 18.944  15.255 1.00 17.69  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.404 18.230  17.156 1.00 19.16  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.123 18.728  15.908 1.00 18.46  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.358 19.525  13.980 1.00 18.39  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.895 19.094  15.330 1.00 18.73  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.140 19.863  13.397 1.00 18.97  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.926 19.637  14.067 1.00 18.90  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.834 17.439  14.974 1.00 23.43  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.175 17.694  14.420 1.00 25.22  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.490 16.794  13.186 1.00 26.81  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.426 17.090  12.437 1.00 28.24  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.230 17.468  15.490 1.00 25.67  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.749 15.672  13.025 1.00 25.74  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.872 14.728  11.905 1.00 24.85  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.542 14.650  11.103 1.00 22.94  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.256 13.632  10.490 1.00 21.87  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.250 13.334  12.432 1.00 26.38  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.658 13.251  12.981 1.00 29.50  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.628 13.114  12.228 1.00 33.13  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.807 13.304  14.298 1.00 27.82  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.742 15.729  11.105 1.00 22.00  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.439 15.794  10.427 1.00 20.81  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.483 15.489  8.913  1.00 21.46  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.235 16.130  8.178  1.00 22.57  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.823 17.199  10.656 1.00 20.56  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.511 17.493  9.907  1.00 22.05  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.369 16.619  10.444 1.00 21.78  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.156 18.984  9.952  1.00 22.12  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.642 14.541  8.452  1.00 21.03  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.453 14.214  7.043  1.00 20.93  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.089 14.842  6.589  1.00 20.72  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.017 15.617  5.626  1.00 20.40  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.474 12.671  6.821  1.00 21.84  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.070 12.316  5.398  1.00 22.34  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.844 12.092  7.148  1.00 22.20  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.018 14.543  7.344  1.00 19.87  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.686 15.005  7.006  1.00 19.46  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.851 15.131  8.272  1.00 18.89  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.029 14.350  9.195  1.00 18.76  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.047 13.974  6.056  1.00 19.46  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.612 14.228  5.697  1.00 20.17  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.139 15.132  4.796  1.00 21.08  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.464 13.585  6.261  1.00 19.75  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.770 15.034  4.706  1.00 21.41  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.329 14.106  5.611  1.00 20.42  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.291 12.555  7.194  1.00 20.13  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.040 13.657  5.890  1.00 20.80  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.011 12.139  7.487  1.00 20.83  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.905 12.684  6.836  1.00 20.57  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.944 16.092  8.309  1.00 17.61  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.022 16.238  9.438  1.00 17.06  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.695 16.813  8.933  1.00 15.88  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.678 17.631  7.990  1.00 14.77  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.634 17.048  10.600 1.00 19.18  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.111 18.459  10.241 1.00 22.31  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.041 19.526  10.073 1.00 23.43  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.281 20.476  9.294  1.00 24.11  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.958 19.405  10.690 1.00 19.79  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.579 16.394  9.554  1.00 14.52  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.265 16.923  9.160  1.00 14.20  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.458 17.080  10.438 1.00 14.11  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.063 16.080  11.029 1.00 14.09  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.572 16.018  8.145  1.00 14.94  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.286 16.592  7.540  1.00 20.37  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.555 17.283  8.254  1.00 20.68  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.995 16.299  6.358  1.00 23.37  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.224 18.331  10.865 1.00 14.64  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.483 18.629  12.091 0.50 15.41  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.489 18.604  12.098 0.50 15.63  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.043 18.129  11.999 1.00 15.52  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.506 17.617  12.975 1.00 16.09  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.509 20.129  12.380 0.50 17.19  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.536 20.090  12.432 0.50 18.06  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.836 20.450  13.587 0.50 18.56  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.854 20.826  11.432 0.50 20.59  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.425 18.246  10.811 1.00 15.06  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.049 17.795  10.644 1.00 15.19  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.902 16.278  10.803 1.00 14.49  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.808 15.811  11.089 1.00 14.33  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.478 18.277  9.318  1.00 18.16  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.964 17.461  8.264  1.00 22.95  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.980 15.513  10.612 1.00 13.30  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.944 14.049  10.761 1.00 12.93  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.526 13.577  12.102 1.00 13.02  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.466 12.380  12.399 1.00 13.97  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.719 13.382  9.603  1.00 13.34  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.151 13.680  8.216  1.00 14.21  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.926 13.024  7.078  1.00 15.45  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.897 11.572  7.178  1.00 14.32  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.991 10.733  6.150  1.00 14.73  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.154 11.200  4.909  1.00 12.36  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.947 9.422   6.353  1.00 15.69  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.207 14.483  12.861 1.00 13.09  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.910 14.144  14.100 1.00 12.61  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.045 13.148  13.799 1.00 13.25  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.304 12.251  14.590 1.00 13.83  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.958 13.648  15.202 1.00 12.95  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.673 13.371  16.503 1.00 15.34  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.458 14.229  16.929 1.00 14.25  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.529 12.234  17.042 1.00 16.90  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.702 13.278  12.623 1.00 12.50  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.822 12.428  12.226 1.00 12.03  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.147 13.203  12.081 1.00 13.64  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.184 14.338  11.606 1.00 14.56  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.551 11.680  10.891 1.00 11.48  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.532 10.523  10.946 1.00 12.51  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.439 9.797   9.610  1.00 12.57  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.858 9.532   12.069 1.00 12.78  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.229 12.558  12.460 1.00 14.04  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.578 13.075  12.214 1.00 15.12  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.426 11.895  11.783 1.00 15.21  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.338 10.841  12.379 1.00 15.92  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.214 13.753  13.453 1.00 16.02  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.579 14.459  13.167 1.00 18.28  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.652 15.851  13.795 1.00 18.21  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.772 13.602  13.632 1.00 20.08  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.275 12.068  10.780 1.00 14.84  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.217 11.049  10.361 1.00 15.19  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.627 11.671  10.481 1.00 16.80  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.853 12.803  10.020 1.00 16.62  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.954 10.522  8.927  1.00 15.68  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.101 9.636   8.452  1.00 15.81  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.621 9.780   8.851  1.00 15.57  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.543 10.961  11.156 1.00 17.23  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.933 11.381  11.257 1.00 18.69  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.814 10.304  10.600 1.00 20.90  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.383 9.145   10.430 1.00 19.67  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.341 11.589  12.714 1.00 19.66  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.093 10.441  13.509 1.00 21.65  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.065 10.674  10.265 1.00 22.72  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 30.982 9.725   9.664  1.00 25.19  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.803 9.004   10.729 1.00 28.25  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.087 9.575   11.782 1.00 28.89  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.902 10.425  8.676  1.00 26.60  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.561 11.490  9.339  1.00 29.63  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.174 7.739   10.461 1.00 29.53  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.947 6.925   11.390 1.00 31.50  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.243 6.422   10.760 1.00 34.83  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.314 6.196   9.546  1.00 35.38  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.132 5.702   11.829 1.00 32.20  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.903 4.890   10.687 1.00 33.39  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.802 6.071   12.450 1.00 32.10  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.246 6.178   11.597 1.00 36.73  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.514 5.637   11.125 1.00 38.91  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.350 4.125   10.870 1.00 39.62  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.878 3.603   9.877  1.00 40.32  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.614 5.930   12.155 1.00 41.51  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.202 5.420   13.428 1.00 43.07  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.908 7.422   12.280 1.00 42.37  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.616 3.427   11.764 1.00 38.75  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.392 1.988   11.657 1.00 38.82  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.166 1.664   10.820 1.00 38.78  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.228 2.453   10.742 1.00 38.73  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.262 1.365   13.042 1.00 38.73  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.180 0.487   10.207 1.00 38.96  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.115 -0.033  9.357  1.00 39.27  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.927 -0.585  10.178 1.00 38.37  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.130 -1.313  11.146 1.00 39.18  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.705 -1.137  8.464  1.00 41.51  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.724 -1.735  7.470  1.00 47.44  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.724 -1.031  6.135  1.00 54.38  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.576 -0.177  5.838  1.00 56.59  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.760 -1.390  5.293  1.00 55.35  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.707 -0.241  9.761  1.00 36.61  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.456 -0.704  10.354 1.00 35.65  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.899 -1.874  9.566  1.00 33.76  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.069 -1.929  8.345  1.00 34.25  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.230 -2.818  10.239 1.00 31.74  ? 50  CYS   A N   1 
ATOM   342  C  CA  A CYS   A 1 44  ? 27.729 -4.007  9.546  0.50 31.45  ? 50  CYS   A CA  1 
ATOM   343  C  CA  B CYS   A 1 44  ? 27.730 -4.018  9.571  0.50 31.42  ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 26.219 -4.227  9.686  1.00 30.39  ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 25.741 -5.335  9.412  1.00 29.96  ? 50  CYS   A O   1 
ATOM   346  C  CB  A CYS   A 1 44  ? 28.518 -5.250  9.948  0.50 32.54  ? 50  CYS   A CB  1 
ATOM   347  C  CB  B CYS   A 1 44  ? 28.492 -5.245  10.055 0.50 32.42  ? 50  CYS   A CB  1 
ATOM   348  S  SG  A CYS   A 1 44  ? 28.872 -5.372  11.721 0.50 36.70  ? 50  CYS   A SG  1 
ATOM   349  S  SG  B CYS   A 1 44  ? 30.290 -5.084  9.952  0.50 36.24  ? 50  CYS   A SG  1 
ATOM   350  N  N   . ASP   A 1 45  ? 25.469 -3.183  10.086 1.00 28.32  ? 51  ASP   A N   1 
ATOM   351  C  CA  . ASP   A 1 45  ? 24.011 -3.287  10.164 1.00 27.43  ? 51  ASP   A CA  1 
ATOM   352  C  C   . ASP   A 1 45  ? 23.485 -3.269  8.722  1.00 25.46  ? 51  ASP   A C   1 
ATOM   353  O  O   . ASP   A 1 45  ? 24.097 -2.660  7.846  1.00 25.12  ? 51  ASP   A O   1 
ATOM   354  C  CB  . ASP   A 1 45  ? 23.383 -2.101  10.938 1.00 30.07  ? 51  ASP   A CB  1 
ATOM   355  C  CG  . ASP   A 1 45  ? 23.601 -2.144  12.431 1.00 35.94  ? 51  ASP   A CG  1 
ATOM   356  O  OD1 . ASP   A 1 45  ? 23.839 -3.244  12.957 1.00 38.09  ? 51  ASP   A OD1 1 
ATOM   357  O  OD2 . ASP   A 1 45  ? 23.552 -1.063  13.077 1.00 36.61  ? 51  ASP   A OD2 1 
ATOM   358  N  N   . THR   A 1 46  ? 22.366 -3.936  8.475  1.00 24.32  ? 52  THR   A N   1 
ATOM   359  C  CA  . THR   A 1 46  ? 21.769 -3.983  7.139  1.00 23.99  ? 52  THR   A CA  1 
ATOM   360  C  C   . THR   A 1 46  ? 20.512 -3.124  7.155  1.00 22.05  ? 52  THR   A C   1 
ATOM   361  O  O   . THR   A 1 46  ? 19.668 -3.314  8.036  1.00 21.57  ? 52  THR   A O   1 
ATOM   362  C  CB  . THR   A 1 46  ? 21.382 -5.424  6.788  1.00 26.30  ? 52  THR   A CB  1 
ATOM   363  O  OG1 . THR   A 1 46  ? 22.580 -6.188  6.636  1.00 28.57  ? 52  THR   A OG1 1 
ATOM   364  C  CG2 . THR   A 1 46  ? 20.572 -5.511  5.497  1.00 26.57  ? 52  THR   A CG2 1 
ATOM   365  N  N   . ILE   A 1 47  ? 20.394 -2.161  6.226  1.00 20.30  ? 53  ILE   A N   1 
ATOM   366  C  CA  . ILE   A 1 47  ? 19.194 -1.332  6.166  1.00 19.06  ? 53  ILE   A CA  1 
ATOM   367  C  C   . ILE   A 1 47  ? 18.128 -2.035  5.315  1.00 17.96  ? 53  ILE   A C   1 
ATOM   368  O  O   . ILE   A 1 47  ? 18.432 -2.553  4.230  1.00 17.66  ? 53  ILE   A O   1 
ATOM   369  C  CB  . ILE   A 1 47  ? 19.495 0.097   5.644  1.00 19.60  ? 53  ILE   A CB  1 
ATOM   370  C  CG1 . ILE   A 1 47  ? 20.667 0.744   6.414  1.00 20.83  ? 53  ILE   A CG1 1 
ATOM   371  C  CG2 . ILE   A 1 47  ? 18.239 0.976   5.706  1.00 20.13  ? 53  ILE   A CG2 1 
ATOM   372  C  CD1 . ILE   A 1 47  ? 20.378 0.952   7.956  1.00 21.52  ? 53  ILE   A CD1 1 
ATOM   373  N  N   . ALA   A 1 48  ? 16.891 -2.074  5.801  1.00 16.64  ? 54  ALA   A N   1 
ATOM   374  C  CA  . ALA   A 1 48  ? 15.789 -2.707  5.073  1.00 16.78  ? 54  ALA   A CA  1 
ATOM   375  C  C   . ALA   A 1 48  ? 15.377 -1.823  3.897  1.00 16.86  ? 54  ALA   A C   1 
ATOM   376  O  O   . ALA   A 1 48  ? 15.290 -0.621  4.056  1.00 16.05  ? 54  ALA   A O   1 
ATOM   377  C  CB  . ALA   A 1 48  ? 14.594 -2.882  6.005  1.00 16.59  ? 54  ALA   A CB  1 
ATOM   378  N  N   . ARG   A 1 49  ? 15.098 -2.417  2.738  1.00 17.16  ? 55  ARG   A N   1 
ATOM   379  C  CA  . ARG   A 1 49  ? 14.615 -1.704  1.554  1.00 17.88  ? 55  ARG   A CA  1 
ATOM   380  C  C   . ARG   A 1 49  ? 13.284 -2.357  1.183  1.00 18.64  ? 55  ARG   A C   1 
ATOM   381  O  O   . ARG   A 1 49  ? 13.236 -3.289  0.369  1.00 19.14  ? 55  ARG   A O   1 
ATOM   382  C  CB  . ARG   A 1 49  ? 15.631 -1.807  0.425  1.00 18.47  ? 55  ARG   A CB  1 
ATOM   383  C  CG  . ARG   A 1 49  ? 17.004 -1.287  0.824  1.00 20.80  ? 55  ARG   A CG  1 
ATOM   384  C  CD  . ARG   A 1 49  ? 17.017 0.193   1.244  1.00 23.03  ? 55  ARG   A CD  1 
ATOM   385  N  NE  . ARG   A 1 49  ? 18.385 0.644   1.507  1.00 24.10  ? 55  ARG   A NE  1 
ATOM   386  C  CZ  . ARG   A 1 49  ? 18.698 1.774   2.132  1.00 25.95  ? 55  ARG   A CZ  1 
ATOM   387  N  NH1 . ARG   A 1 49  ? 17.746 2.607   2.529  1.00 24.93  ? 55  ARG   A NH1 1 
ATOM   388  N  NH2 . ARG   A 1 49  ? 19.965 2.094   2.340  1.00 25.36  ? 55  ARG   A NH2 1 
ATOM   389  N  N   . CYS   A 1 50  ? 12.215 -1.891  1.809  1.00 18.96  ? 56  CYS   A N   1 
ATOM   390  C  CA  . CYS   A 1 50  ? 10.906 -2.535  1.736  1.00 19.45  ? 56  CYS   A CA  1 
ATOM   391  C  C   . CYS   A 1 50  ? 9.780  -1.589  2.140  1.00 19.84  ? 56  CYS   A C   1 
ATOM   392  O  O   . CYS   A 1 50  ? 10.030 -0.474  2.578  1.00 19.85  ? 56  CYS   A O   1 
ATOM   393  C  CB  . CYS   A 1 50  ? 10.929 -3.738  2.681  1.00 19.84  ? 56  CYS   A CB  1 
ATOM   394  S  SG  . CYS   A 1 50  ? 11.060 -3.280  4.439  1.00 20.37  ? 56  CYS   A SG  1 
ATOM   395  N  N   . ASP   A 1 51  ? 8.520  -2.105  2.119  1.00 20.51  ? 57  ASP   A N   1 
ATOM   396  C  CA  . ASP   A 1 51  ? 7.384  -1.346  2.619  1.00 21.35  ? 57  ASP   A CA  1 
ATOM   397  C  C   . ASP   A 1 51  ? 6.689  -2.077  3.770  1.00 21.34  ? 57  ASP   A C   1 
ATOM   398  O  O   . ASP   A 1 51  ? 5.479  -1.913  3.948  1.00 21.99  ? 57  ASP   A O   1 
ATOM   399  C  CB  . ASP   A 1 51  ? 6.400  -0.929  1.502  1.00 24.09  ? 57  ASP   A CB  1 
ATOM   400  C  CG  . ASP   A 1 51  ? 5.656  -2.046  0.803  1.00 32.14  ? 57  ASP   A CG  1 
ATOM   401  O  OD1 . ASP   A 1 51  ? 5.929  -3.227  1.106  1.00 33.23  ? 57  ASP   A OD1 1 
ATOM   402  O  OD2 . ASP   A 1 51  ? 4.789  -1.739  -0.053 1.00 36.83  ? 57  ASP   A OD2 1 
ATOM   403  N  N   . CYS   A 1 52  ? 7.443  -2.907  4.554  1.00 20.09  ? 58  CYS   A N   1 
ATOM   404  C  CA  . CYS   A 1 52  ? 6.910  -3.643  5.723  1.00 18.56  ? 58  CYS   A CA  1 
ATOM   405  C  C   . CYS   A 1 52  ? 6.175  -2.700  6.660  1.00 17.45  ? 58  CYS   A C   1 
ATOM   406  O  O   . CYS   A 1 52  ? 6.597  -1.562  6.834  1.00 18.01  ? 58  CYS   A O   1 
ATOM   407  C  CB  . CYS   A 1 52  ? 8.040  -4.346  6.485  1.00 18.50  ? 58  CYS   A CB  1 
ATOM   408  S  SG  . CYS   A 1 52  ? 8.641  -5.880  5.728  1.00 19.79  ? 58  CYS   A SG  1 
ATOM   409  N  N   . GLN   A 1 53  ? 5.124  -3.183  7.289  1.00 15.46  ? 59  GLN   A N   1 
ATOM   410  C  CA  . GLN   A 1 53  ? 4.416  -2.455  8.329  1.00 15.28  ? 59  GLN   A CA  1 
ATOM   411  C  C   . GLN   A 1 53  ? 4.350  -3.289  9.622  1.00 14.67  ? 59  GLN   A C   1 
ATOM   412  O  O   . GLN   A 1 53  ? 3.476  -3.051  10.455 1.00 14.86  ? 59  GLN   A O   1 
ATOM   413  C  CB  . GLN   A 1 53  ? 2.990  -2.040  7.887  1.00 17.66  ? 59  GLN   A CB  1 
ATOM   414  C  CG  . GLN   A 1 53  ? 2.937  -0.853  6.907  1.00 20.83  ? 59  GLN   A CG  1 
ATOM   415  C  CD  . GLN   A 1 53  ? 1.496  -0.394  6.702  1.00 24.89  ? 59  GLN   A CD  1 
ATOM   416  O  OE1 . GLN   A 1 53  ? 0.948  -0.444  5.593  1.00 24.99  ? 59  GLN   A OE1 1 
ATOM   417  N  NE2 . GLN   A 1 53  ? 0.830  0.022   7.789  1.00 25.20  ? 59  GLN   A NE2 1 
ATOM   418  N  N   . THR   A 1 54  ? 5.183  -4.334  9.752  1.00 13.00  ? 60  THR   A N   1 
ATOM   419  C  CA  . THR   A 1 54  ? 5.297  -5.155  10.949 1.00 13.16  ? 60  THR   A CA  1 
ATOM   420  C  C   . THR   A 1 54  ? 6.807  -5.312  11.236 1.00 12.00  ? 60  THR   A C   1 
ATOM   421  O  O   . THR   A 1 54  ? 7.634  -5.394  10.318 1.00 11.98  ? 60  THR   A O   1 
ATOM   422  C  CB  . THR   A 1 54  ? 4.582  -6.523  10.847 1.00 15.46  ? 60  THR   A CB  1 
ATOM   423  O  OG1 . THR   A 1 54  ? 5.254  -7.304  9.876  1.00 16.04  ? 60  THR   A OG1 1 
ATOM   424  C  CG2 . THR   A 1 54  ? 3.079  -6.414  10.503 1.00 15.55  ? 60  THR   A CG2 1 
ATOM   425  N  N   . GLY   A 1 55  ? 7.144  -5.293  12.508 1.00 10.36  ? 61  GLY   A N   1 
ATOM   426  C  CA  . GLY   A 1 55  ? 8.530  -5.444  12.918 1.00 10.92  ? 61  GLY   A CA  1 
ATOM   427  C  C   . GLY   A 1 55  ? 8.640  -5.644  14.406 1.00 10.89  ? 61  GLY   A C   1 
ATOM   428  O  O   . GLY   A 1 55  ? 7.640  -5.909  15.054 1.00 11.86  ? 61  GLY   A O   1 
ATOM   429  N  N   . VAL   A 1 56  ? 9.863  -5.565  14.933 1.00 10.69  ? 62  VAL   A N   1 
ATOM   430  C  CA  . VAL   A 1 56  ? 10.186 -5.712  16.361 1.00 10.79  ? 62  VAL   A CA  1 
ATOM   431  C  C   . VAL   A 1 56  ? 11.082 -4.543  16.765 1.00 10.80  ? 62  VAL   A C   1 
ATOM   432  O  O   . VAL   A 1 56  ? 12.106 -4.311  16.099 1.00 10.99  ? 62  VAL   A O   1 
ATOM   433  C  CB  . VAL   A 1 56  ? 10.945 -7.036  16.608 1.00 11.93  ? 62  VAL   A CB  1 
ATOM   434  C  CG1 . VAL   A 1 56  ? 11.404 -7.138  18.066 1.00 13.82  ? 62  VAL   A CG1 1 
ATOM   435  C  CG2 . VAL   A 1 56  ? 10.095 -8.258  16.216 1.00 11.73  ? 62  VAL   A CG2 1 
ATOM   436  N  N   . TYR   A 1 57  ? 10.758 -3.842  17.866 1.00 10.55  ? 63  TYR   A N   1 
ATOM   437  C  CA  . TYR   A 1 57  ? 11.620 -2.754  18.324 1.00 10.12  ? 63  TYR   A CA  1 
ATOM   438  C  C   . TYR   A 1 57  ? 12.182 -3.006  19.711 1.00 10.85  ? 63  TYR   A C   1 
ATOM   439  O  O   . TYR   A 1 57  ? 11.541 -3.695  20.496 1.00 10.75  ? 63  TYR   A O   1 
ATOM   440  C  CB  . TYR   A 1 57  ? 10.893 -1.393  18.260 1.00 9.83   ? 63  TYR   A CB  1 
ATOM   441  C  CG  . TYR   A 1 57  ? 9.939  -1.124  19.418 1.00 10.87  ? 63  TYR   A CG  1 
ATOM   442  C  CD1 . TYR   A 1 57  ? 8.639  -1.623  19.407 1.00 12.02  ? 63  TYR   A CD1 1 
ATOM   443  C  CD2 . TYR   A 1 57  ? 10.310 -0.305  20.475 1.00 12.61  ? 63  TYR   A CD2 1 
ATOM   444  C  CE1 . TYR   A 1 57  ? 7.744  -1.340  20.446 1.00 13.74  ? 63  TYR   A CE1 1 
ATOM   445  C  CE2 . TYR   A 1 57  ? 9.411  0.013   21.500 1.00 14.06  ? 63  TYR   A CE2 1 
ATOM   446  C  CZ  . TYR   A 1 57  ? 8.150  -0.560  21.510 1.00 14.69  ? 63  TYR   A CZ  1 
ATOM   447  O  OH  . TYR   A 1 57  ? 7.249  -0.299  22.525 1.00 16.27  ? 63  TYR   A OH  1 
ATOM   448  N  N   . TYR   A 1 58  ? 13.394 -2.480  20.014 1.00 11.16  ? 64  TYR   A N   1 
ATOM   449  C  CA  . TYR   A 1 58  ? 13.965 -2.624  21.358 1.00 12.52  ? 64  TYR   A CA  1 
ATOM   450  C  C   . TYR   A 1 58  ? 13.474 -1.460  22.256 1.00 12.50  ? 64  TYR   A C   1 
ATOM   451  O  O   . TYR   A 1 58  ? 13.565 -0.308  21.834 1.00 11.82  ? 64  TYR   A O   1 
ATOM   452  C  CB  . TYR   A 1 58  ? 15.494 -2.643  21.346 1.00 13.12  ? 64  TYR   A CB  1 
ATOM   453  C  CG  . TYR   A 1 58  ? 16.047 -2.832  22.745 1.00 14.20  ? 64  TYR   A CG  1 
ATOM   454  C  CD1 . TYR   A 1 58  ? 15.763 -3.977  23.478 1.00 14.94  ? 64  TYR   A CD1 1 
ATOM   455  C  CD2 . TYR   A 1 58  ? 16.779 -1.829  23.366 1.00 15.07  ? 64  TYR   A CD2 1 
ATOM   456  C  CE1 . TYR   A 1 58  ? 16.249 -4.149  24.768 1.00 16.55  ? 64  TYR   A CE1 1 
ATOM   457  C  CE2 . TYR   A 1 58  ? 17.291 -1.998  24.645 1.00 16.18  ? 64  TYR   A CE2 1 
ATOM   458  C  CZ  . TYR   A 1 58  ? 17.004 -3.150  25.353 1.00 18.00  ? 64  TYR   A CZ  1 
ATOM   459  O  OH  . TYR   A 1 58  ? 17.496 -3.312  26.624 1.00 20.02  ? 64  TYR   A OH  1 
ATOM   460  N  N   . CYS   A 1 59  ? 12.983 -1.776  23.494 1.00 12.46  ? 65  CYS   A N   1 
ATOM   461  C  CA  . CYS   A 1 59  ? 12.468 -0.833  24.495 1.00 13.53  ? 65  CYS   A CA  1 
ATOM   462  C  C   . CYS   A 1 59  ? 13.390 -0.878  25.725 1.00 15.02  ? 65  CYS   A C   1 
ATOM   463  O  O   . CYS   A 1 59  ? 13.264 -1.799  26.547 1.00 15.05  ? 65  CYS   A O   1 
ATOM   464  C  CB  . CYS   A 1 59  ? 11.029 -1.183  24.879 1.00 13.97  ? 65  CYS   A CB  1 
ATOM   465  S  SG  . CYS   A 1 59  ? 10.301 -0.070  26.113 1.00 16.08  ? 65  CYS   A SG  1 
ATOM   466  N  N   . SER   A 1 60  ? 14.314 0.098   25.849 1.00 14.91  ? 66  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 60  ? 15.258 0.079   26.949 1.00 16.44  ? 66  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 60  ? 14.591 0.217   28.306 1.00 16.29  ? 66  SER   A C   1 
ATOM   469  O  O   . SER   A 1 60  ? 14.978 -0.531  29.213 1.00 17.01  ? 66  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 60  ? 16.398 1.083   26.757 1.00 19.79  ? 66  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 60  ? 15.998 2.439   26.719 1.00 25.30  ? 66  SER   A OG  1 
ATOM   472  N  N   . SER   A 1 61  ? 13.506 1.038   28.425 1.00 15.48  ? 67  SER   A N   1 
ATOM   473  C  CA  . SER   A 1 61  ? 12.737 1.208   29.675 1.00 15.41  ? 67  SER   A CA  1 
ATOM   474  C  C   . SER   A 1 61  ? 12.055 -0.074  30.178 1.00 16.53  ? 67  SER   A C   1 
ATOM   475  O  O   . SER   A 1 61  ? 11.525 -0.086  31.296 1.00 17.30  ? 67  SER   A O   1 
ATOM   476  C  CB  . SER   A 1 61  ? 11.724 2.344   29.565 1.00 15.24  ? 67  SER   A CB  1 
ATOM   477  O  OG  . SER   A 1 61  ? 10.692 2.091   28.622 1.00 16.93  ? 67  SER   A OG  1 
ATOM   478  N  N   . ARG   A 1 62  ? 12.063 -1.143  29.372 1.00 15.58  ? 68  ARG   A N   1 
ATOM   479  C  CA  . ARG   A 1 62  ? 11.517 -2.439  29.770 1.00 16.30  ? 68  ARG   A CA  1 
ATOM   480  C  C   . ARG   A 1 62  ? 12.552 -3.588  29.571 1.00 18.55  ? 68  ARG   A C   1 
ATOM   481  O  O   . ARG   A 1 62  ? 12.247 -4.735  29.885 1.00 18.53  ? 68  ARG   A O   1 
ATOM   482  C  CB  . ARG   A 1 62  ? 10.275 -2.753  28.909 1.00 16.72  ? 68  ARG   A CB  1 
ATOM   483  C  CG  . ARG   A 1 62  ? 9.114  -1.813  29.140 1.00 19.51  ? 68  ARG   A CG  1 
ATOM   484  C  CD  . ARG   A 1 62  ? 8.433  -2.068  30.463 1.00 21.76  ? 68  ARG   A CD  1 
ATOM   485  N  NE  . ARG   A 1 62  ? 7.274  -1.199  30.629 1.00 23.34  ? 68  ARG   A NE  1 
ATOM   486  C  CZ  . ARG   A 1 62  ? 7.273  -0.073  31.343 1.00 24.54  ? 68  ARG   A CZ  1 
ATOM   487  N  NH1 . ARG   A 1 62  ? 8.388  0.349   31.933 1.00 23.14  ? 68  ARG   A NH1 1 
ATOM   488  N  NH2 . ARG   A 1 62  ? 6.162  0.650   31.455 1.00 21.68  ? 68  ARG   A NH2 1 
ATOM   489  N  N   . ARG   A 1 63  ? 13.742 -3.306  29.003 1.00 19.57  ? 69  ARG   A N   1 
ATOM   490  C  CA  . ARG   A 1 63  ? 14.767 -4.306  28.648 1.00 20.58  ? 69  ARG   A CA  1 
ATOM   491  C  C   . ARG   A 1 63  ? 14.137 -5.443  27.845 1.00 21.19  ? 69  ARG   A C   1 
ATOM   492  O  O   . ARG   A 1 63  ? 14.384 -6.616  28.122 1.00 21.82  ? 69  ARG   A O   1 
ATOM   493  C  CB  . ARG   A 1 63  ? 15.519 -4.843  29.882 1.00 22.25  ? 69  ARG   A CB  1 
ATOM   494  C  CG  . ARG   A 1 63  ? 16.354 -3.794  30.602 1.00 27.11  ? 69  ARG   A CG  1 
ATOM   495  C  CD  . ARG   A 1 63  ? 17.063 -4.458  31.772 1.00 30.97  ? 69  ARG   A CD  1 
ATOM   496  N  NE  . ARG   A 1 63  ? 17.688 -3.485  32.665 1.00 35.83  ? 69  ARG   A NE  1 
ATOM   497  C  CZ  . ARG   A 1 63  ? 17.680 -3.574  33.995 1.00 37.23  ? 69  ARG   A CZ  1 
ATOM   498  N  NH1 . ARG   A 1 63  ? 17.053 -4.581  34.598 1.00 35.21  ? 69  ARG   A NH1 1 
ATOM   499  N  NH2 . ARG   A 1 63  ? 18.261 -2.634  34.732 1.00 37.35  ? 69  ARG   A NH2 1 
ATOM   500  N  N   . LYS   A 1 64  ? 13.239 -5.086  26.912 1.00 20.05  ? 70  LYS   A N   1 
ATOM   501  C  CA  . LYS   A 1 64  ? 12.485 -6.075  26.138 1.00 19.72  ? 70  LYS   A CA  1 
ATOM   502  C  C   . LYS   A 1 64  ? 12.336 -5.651  24.689 1.00 17.36  ? 70  LYS   A C   1 
ATOM   503  O  O   . LYS   A 1 64  ? 12.279 -4.452  24.393 1.00 16.95  ? 70  LYS   A O   1 
ATOM   504  C  CB  . LYS   A 1 64  ? 11.039 -6.178  26.676 1.00 23.03  ? 70  LYS   A CB  1 
ATOM   505  C  CG  . LYS   A 1 64  ? 10.834 -7.165  27.808 1.00 29.84  ? 70  LYS   A CG  1 
ATOM   506  C  CD  . LYS   A 1 64  ? 9.355  -7.289  28.087 1.00 36.26  ? 70  LYS   A CD  1 
ATOM   507  C  CE  . LYS   A 1 64  ? 9.064  -8.380  29.093 1.00 42.57  ? 70  LYS   A CE  1 
ATOM   508  N  NZ  . LYS   A 1 64  ? 9.645  -8.063  30.424 1.00 46.28  ? 70  LYS   A NZ  1 
ATOM   509  N  N   . HIS   A 1 65  ? 12.182 -6.631  23.801 1.00 15.55  ? 71  HIS   A N   1 
ATOM   510  C  CA  . HIS   A 1 65  ? 11.847 -6.350  22.404 1.00 14.13  ? 71  HIS   A CA  1 
ATOM   511  C  C   . HIS   A 1 65  ? 10.333 -6.630  22.270 1.00 14.72  ? 71  HIS   A C   1 
ATOM   512  O  O   . HIS   A 1 65  ? 9.795  -7.552  22.931 1.00 15.90  ? 71  HIS   A O   1 
ATOM   513  C  CB  . HIS   A 1 65  ? 12.620 -7.230  21.397 1.00 13.74  ? 71  HIS   A CB  1 
ATOM   514  C  CG  . HIS   A 1 65  ? 14.111 -7.088  21.438 1.00 14.76  ? 71  HIS   A CG  1 
ATOM   515  N  ND1 . HIS   A 1 65  ? 14.797 -6.319  20.501 1.00 16.94  ? 71  HIS   A ND1 1 
ATOM   516  C  CD2 . HIS   A 1 65  ? 15.000 -7.592  22.317 1.00 15.20  ? 71  HIS   A CD2 1 
ATOM   517  C  CE1 . HIS   A 1 65  ? 16.076 -6.405  20.832 1.00 15.83  ? 71  HIS   A CE1 1 
ATOM   518  N  NE2 . HIS   A 1 65  ? 16.247 -7.131  21.928 1.00 16.65  ? 71  HIS   A NE2 1 
ATOM   519  N  N   . TYR   A 1 66  ? 9.648  -5.814  21.458 1.00 13.56  ? 72  TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 66  ? 8.216  -5.951  21.210 1.00 13.88  ? 72  TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 66  ? 7.866  -6.037  19.727 1.00 13.17  ? 72  TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 66  ? 8.269  -5.169  18.941 1.00 13.00  ? 72  TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 66  ? 7.401  -4.780  21.804 1.00 14.06  ? 72  TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 66  ? 7.448  -4.662  23.316 1.00 15.52  ? 72  TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 66  ? 6.687  -5.502  24.127 1.00 16.88  ? 72  TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 66  ? 8.231  -3.699  23.934 1.00 16.38  ? 72  TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 66  ? 6.708  -5.382  25.518 1.00 18.34  ? 72  TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 66  ? 8.224  -3.541  25.322 1.00 17.78  ? 72  TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 66  ? 7.500  -4.418  26.112 1.00 19.19  ? 72  TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 66  ? 7.510  -4.292  27.484 1.00 20.97  ? 72  TYR   A OH  1 
ATOM   531  N  N   . PRO   A 1 67  ? 7.032  -7.029  19.356 1.00 12.48  ? 73  PRO   A N   1 
ATOM   532  C  CA  . PRO   A 1 67  ? 6.528  -7.096  17.960 1.00 12.71  ? 73  PRO   A CA  1 
ATOM   533  C  C   . PRO   A 1 67  ? 5.407  -6.038  17.779 1.00 13.36  ? 73  PRO   A C   1 
ATOM   534  O  O   . PRO   A 1 67  ? 4.516  -5.958  18.635 1.00 13.65  ? 73  PRO   A O   1 
ATOM   535  C  CB  . PRO   A 1 67  ? 5.954  -8.517  17.867 1.00 13.22  ? 73  PRO   A CB  1 
ATOM   536  C  CG  . PRO   A 1 67  ? 5.535  -8.846  19.283 1.00 13.36  ? 73  PRO   A CG  1 
ATOM   537  C  CD  . PRO   A 1 67  ? 6.490  -8.120  20.206 1.00 11.83  ? 73  PRO   A CD  1 
ATOM   538  N  N   . VAL   A 1 68  ? 5.489  -5.178  16.751 1.00 13.73  ? 74  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 68  ? 4.491  -4.114  16.512 1.00 13.77  ? 74  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 68  ? 4.041  -4.033  15.068 1.00 13.61  ? 74  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 68  ? 4.802  -4.346  14.158 1.00 12.71  ? 74  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 68  ? 5.008  -2.685  16.924 1.00 14.22  ? 74  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 68  ? 4.948  -2.474  18.433 1.00 15.53  ? 74  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 68  ? 6.411  -2.419  16.395 1.00 13.25  ? 74  VAL   A CG2 1 
ATOM   545  N  N   . SER   A 1 69  ? 2.808  -3.554  14.867 1.00 13.93  ? 75  SER   A N   1 
ATOM   546  C  CA  . SER   A 1 69  ? 2.271  -3.166  13.565 1.00 15.01  ? 75  SER   A CA  1 
ATOM   547  C  C   . SER   A 1 69  ? 2.476  -1.624  13.563 1.00 14.03  ? 75  SER   A C   1 
ATOM   548  O  O   . SER   A 1 69  ? 2.264  -0.990  14.599 1.00 13.86  ? 75  SER   A O   1 
ATOM   549  C  CB  . SER   A 1 69  ? 0.784  -3.480  13.462 1.00 16.56  ? 75  SER   A CB  1 
ATOM   550  O  OG  . SER   A 1 69  ? 0.610  -4.853  13.171 1.00 21.90  ? 75  SER   A OG  1 
ATOM   551  N  N   . PHE   A 1 70  ? 2.980  -1.044  12.466 1.00 13.86  ? 76  PHE   A N   1 
ATOM   552  C  CA  . PHE   A 1 70  ? 3.254  0.407   12.437 1.00 13.67  ? 76  PHE   A CA  1 
ATOM   553  C  C   . PHE   A 1 70  ? 2.773  1.046   11.150 1.00 15.30  ? 76  PHE   A C   1 
ATOM   554  O  O   . PHE   A 1 70  ? 2.722  0.383   10.115 1.00 15.84  ? 76  PHE   A O   1 
ATOM   555  C  CB  . PHE   A 1 70  ? 4.743  0.743   12.731 1.00 13.23  ? 76  PHE   A CB  1 
ATOM   556  C  CG  . PHE   A 1 70  ? 5.738  0.049   11.824 1.00 13.52  ? 76  PHE   A CG  1 
ATOM   557  C  CD1 . PHE   A 1 70  ? 6.235  -1.203  12.143 1.00 14.15  ? 76  PHE   A CD1 1 
ATOM   558  C  CD2 . PHE   A 1 70  ? 6.130  0.628   10.620 1.00 14.40  ? 76  PHE   A CD2 1 
ATOM   559  C  CE1 . PHE   A 1 70  ? 7.144  -1.849  11.291 1.00 15.21  ? 76  PHE   A CE1 1 
ATOM   560  C  CE2 . PHE   A 1 70  ? 7.030  -0.016  9.775  1.00 14.84  ? 76  PHE   A CE2 1 
ATOM   561  C  CZ  . PHE   A 1 70  ? 7.528  -1.252  10.115 1.00 14.76  ? 76  PHE   A CZ  1 
ATOM   562  N  N   . SER   A 1 71  ? 2.376  2.341   11.213 1.00 15.47  ? 77  SER   A N   1 
ATOM   563  C  CA  . SER   A 1 71  ? 1.862  3.041   10.040 1.00 16.09  ? 77  SER   A CA  1 
ATOM   564  C  C   . SER   A 1 71  ? 2.996  3.384   9.036  1.00 16.56  ? 77  SER   A C   1 
ATOM   565  O  O   . SER   A 1 71  ? 4.164  3.334   9.395  1.00 16.71  ? 77  SER   A O   1 
ATOM   566  C  CB  . SER   A 1 71  ? 1.127  4.308   10.476 1.00 17.47  ? 77  SER   A CB  1 
ATOM   567  O  OG  . SER   A 1 71  ? 2.015  5.250   11.047 1.00 19.35  ? 77  SER   A OG  1 
ATOM   568  N  N   . LYS   A 1 72  ? 2.657  3.698   7.783  1.00 17.07  ? 78  LYS   A N   1 
ATOM   569  C  CA  . LYS   A 1 72  ? 3.670  4.094   6.788  1.00 18.26  ? 78  LYS   A CA  1 
ATOM   570  C  C   . LYS   A 1 72  ? 4.226  5.477   7.139  1.00 18.10  ? 78  LYS   A C   1 
ATOM   571  O  O   . LYS   A 1 72  ? 3.541  6.264   7.797  1.00 18.48  ? 78  LYS   A O   1 
ATOM   572  C  CB  . LYS   A 1 72  ? 3.075  4.067   5.349  1.00 21.63  ? 78  LYS   A CB  1 
ATOM   573  C  CG  . LYS   A 1 72  ? 2.793  2.640   4.854  1.00 25.69  ? 78  LYS   A CG  1 
ATOM   574  C  CD  . LYS   A 1 72  ? 2.418  2.590   3.359  1.00 30.28  ? 78  LYS   A CD  1 
ATOM   575  C  CE  . LYS   A 1 72  ? 2.190  1.163   2.894  1.00 35.35  ? 78  LYS   A CE  1 
ATOM   576  N  NZ  . LYS   A 1 72  ? 1.587  1.093   1.528  1.00 39.10  ? 78  LYS   A NZ  1 
ATOM   577  N  N   . PRO   A 1 73  ? 5.486  5.775   6.767  1.00 17.83  ? 79  PRO   A N   1 
ATOM   578  C  CA  . PRO   A 1 73  ? 6.067  7.083   7.112  1.00 18.12  ? 79  PRO   A CA  1 
ATOM   579  C  C   . PRO   A 1 73  ? 5.244  8.266   6.618  1.00 18.50  ? 79  PRO   A C   1 
ATOM   580  O  O   . PRO   A 1 73  ? 4.869  8.325   5.445  1.00 17.61  ? 79  PRO   A O   1 
ATOM   581  C  CB  . PRO   A 1 73  ? 7.431  7.065   6.412  1.00 18.85  ? 79  PRO   A CB  1 
ATOM   582  C  CG  . PRO   A 1 73  ? 7.759  5.611   6.224  1.00 19.69  ? 79  PRO   A CG  1 
ATOM   583  C  CD  . PRO   A 1 73  ? 6.433  4.944   5.997  1.00 18.24  ? 79  PRO   A CD  1 
ATOM   584  N  N   . SER   A 1 74  ? 4.981  9.218   7.512  1.00 19.21  ? 80  SER   A N   1 
ATOM   585  C  CA  . SER   A 1 74  ? 4.156  10.361  7.177  1.00 20.99  ? 80  SER   A CA  1 
ATOM   586  C  C   . SER   A 1 74  ? 4.480  11.603  8.046  1.00 21.17  ? 80  SER   A C   1 
ATOM   587  O  O   . SER   A 1 74  ? 5.333  11.528  8.939  1.00 20.42  ? 80  SER   A O   1 
ATOM   588  C  CB  . SER   A 1 74  ? 2.687  9.960   7.308  1.00 24.94  ? 80  SER   A CB  1 
ATOM   589  O  OG  . SER   A 1 74  ? 2.360  9.507   8.611  1.00 29.60  ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 3.800  12.749  7.764  1.00 20.96  ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 3.930  14.008  8.508  1.00 21.74  ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 2.963  13.911  9.691  1.00 22.76  ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 1.744  13.850  9.490  1.00 22.56  ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 3.473  15.195  7.637  1.00 22.17  ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 4.494  16.169  7.062  1.00 24.60  ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 3.772  17.413  6.515  1.00 26.35  ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 5.531  16.585  8.079  1.00 24.88  ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 3.494  13.873  10.912 1.00 23.13  ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 2.664  13.738  12.096 1.00 24.78  ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 2.982  14.844  13.080 1.00 25.64  ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 4.163  15.148  13.296 1.00 24.90  ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 2.917  12.332  12.710 1.00 26.00  ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 2.366  11.227  11.796 1.00 27.22  ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 2.374  12.211  14.144 1.00 26.46  ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 2.923  9.981   12.040 1.00 29.32  ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 1.940  15.418  13.716 1.00 26.40  ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 2.160  16.457  14.717 1.00 28.29  ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 2.821  15.888  15.994 1.00 28.06  ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 2.405  14.854  16.508 1.00 28.24  ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 0.835  17.158  15.068 1.00 29.50  ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 1.008  18.374  15.946 1.00 31.55  ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 1.455  19.568  15.419 1.00 32.76  ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 0.666  18.335  17.287 1.00 33.03  ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 1.579  20.695  16.219 1.00 33.65  ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 0.800  19.461  18.086 1.00 33.57  ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 1.271  20.627  17.552 1.00 33.36  ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 3.838  16.579  16.501 1.00 27.86  ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 4.534  16.161  17.709 1.00 28.88  ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 4.520  17.320  18.709 1.00 30.54  ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 4.961  18.426  18.383 1.00 30.26  ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 5.986  15.668  17.409 1.00 28.61  ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 6.790  15.496  18.692 1.00 28.69  ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 5.980  14.378  16.600 1.00 28.41  ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 4.026  17.051  19.926 1.00 32.04  ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 3.954  18.018  21.020 1.00 34.37  ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 5.316  18.647  21.336 1.00 35.58  ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 6.350  18.018  21.116 1.00 35.81  ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 3.423  17.317  22.277 1.00 37.83  ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 1.929  17.468  22.481 1.00 45.35  ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 1.496  18.744  23.180 1.00 53.56  ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 2.369  19.464  23.717 1.00 54.78  ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 0.275  19.020  23.196 1.00 57.10  ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 5.320  19.868  21.887 1.00 36.23  ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 6.569  20.529  22.263 1.00 37.48  ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 7.307  19.765  23.361 1.00 38.13  ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 6.684  19.120  24.213 1.00 38.59  ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 6.292  21.946  22.735 1.00 38.07  ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 8.638  19.827  23.303 1.00 37.85  ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 9.608  19.234  24.229 1.00 38.07  ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 10.752 20.256  24.435 1.00 38.97  ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 10.783 21.288  23.753 1.00 39.77  ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 10.180 17.942  23.633 1.00 38.34  ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 11.062 18.186  22.543 1.00 38.07  ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 11.719 19.958  25.321 1.00 38.97  ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 12.864 20.849  25.512 1.00 39.54  ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 13.842 20.863  24.313 1.00 38.70  ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 14.751 21.693  24.286 1.00 39.22  ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 13.598 20.550  26.831 1.00 43.33  ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 14.314 19.208  26.864 1.00 50.99  ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 15.017 18.945  28.185 1.00 60.77  ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 16.121 18.352  28.167 1.00 62.35  ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 14.469 19.347  29.240 1.00 63.32  ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 13.647 19.965  23.323 1.00 37.44  ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 14.491 19.854  22.128 1.00 36.00  ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 13.874 20.548  20.899 1.00 34.46  ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 14.600 21.063  20.048 1.00 34.96  ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 14.772 18.375  21.807 1.00 35.76  ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 15.403 17.609  22.951 1.00 36.13  ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 16.737 17.795  23.287 1.00 36.92  ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 14.675 16.674  23.673 1.00 36.86  ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 17.327 17.085  24.327 1.00 37.73  ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 15.248 15.969  24.723 1.00 37.84  ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 16.579 16.169  25.041 1.00 39.23  ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 17.160 15.446  26.061 1.00 41.88  ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 12.543 20.559  20.801 1.00 32.74  ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 11.860 21.172  19.661 1.00 31.97  ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 10.577 21.874  20.070 1.00 33.40  ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 9.842  21.345  20.910 1.00 33.81  ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 11.419 20.083  18.660 1.00 30.27  ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 12.520 19.222  18.077 1.00 28.70  ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 12.805 17.971  18.607 1.00 28.30  ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 13.227 19.629  16.955 1.00 28.39  ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 13.743 17.134  18.016 1.00 27.98  ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 14.215 18.829  16.398 1.00 27.96  ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 14.452 17.570  16.916 1.00 27.68  ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 15.441 16.785  16.379 1.00 26.78  ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 10.195 22.966  19.378 1.00 34.10  ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 8.841  23.503  19.600 1.00 34.35  ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 7.818  22.556  18.936 1.00 34.43  ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 8.193  21.627  18.188 1.00 34.87  ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 8.873  24.875  18.912 1.00 35.30  ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 9.919  24.750  17.846 1.00 35.89  ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 10.905 23.668  18.281 1.00 33.97  ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 6.523  22.772  19.186 1.00 33.62  ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 5.451  21.974  18.575 1.00 33.27  ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 5.542  22.097  17.046 1.00 33.14  ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 5.583  23.211  16.515 1.00 33.81  ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 4.095  22.478  19.057 1.00 33.35  ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 5.671  20.966  16.355 1.00 32.28  ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 5.872  20.975  14.907 1.00 31.34  ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 5.373  19.663  14.252 1.00 30.86  ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 5.047  18.700  14.952 1.00 31.10  ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 7.389  21.132  14.649 1.00 31.36  ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 8.183  19.806  14.797 1.00 31.59  ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 9.601  19.952  15.276 1.00 31.47  ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 10.483 18.876  14.795 1.00 29.72  ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 10.549 17.660  15.333 1.00 27.69  ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 11.407 16.768  14.863 1.00 25.57  ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 9.752  17.327  16.344 1.00 25.82  ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 5.382  19.613  12.908 1.00 29.83  ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 5.098  18.375  12.214 1.00 29.73  ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 6.454  17.711  11.962 1.00 27.20  ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 7.379  18.364  11.465 1.00 28.10  ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 4.378  18.624  10.893 1.00 31.22  ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 2.933  19.019  11.082 1.00 33.96  ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 1.957  18.063  11.317 1.00 35.74  ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 2.551  20.352  11.079 1.00 35.68  ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 0.624  18.421  11.494 1.00 37.26  ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 1.224  20.723  11.250 1.00 37.15  ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 0.263  19.755  11.468 1.00 38.75  ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? -1.055 20.124  11.638 1.00 41.73  ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 6.594  16.447  12.372 1.00 23.90  ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 7.798  15.655  12.122 1.00 20.36  ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 7.477  14.792  10.888 1.00 17.74  ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 6.399  14.190  10.824 1.00 16.97  ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 8.173  14.787  13.349 1.00 20.80  ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 9.344  13.793  13.081 1.00 21.68  ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 10.068 13.350  14.343 1.00 22.30  ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 10.179 14.098  15.320 1.00 22.63  ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 10.613 12.140  14.330 1.00 20.47  ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 8.373  14.782  9.887  1.00 15.26  ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 8.180  13.988  8.679  1.00 14.44  ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 8.874  12.612  8.768  1.00 13.65  ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 9.772  12.404  9.621  1.00 13.18  ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 8.703  14.740  7.457  1.00 16.68  ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 10.097 14.970  7.599  1.00 19.81  ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 8.432  11.685  7.890  1.00 12.87  ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 8.945  10.327  7.765  1.00 12.73  ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 8.779  9.571   9.117  1.00 12.94  ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 9.639  8.773   9.481  1.00 12.74  ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 10.425 10.374  7.324  1.00 12.90  ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 10.623 11.020  5.986  1.00 16.38  ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 10.651 10.270  4.822  1.00 17.52  ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 10.678 12.332  5.654  1.00 16.58  ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 10.789 11.142  3.833  1.00 17.38  ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 10.785 12.389  4.280  1.00 17.44  ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 7.700  9.846   9.858  1.00 12.26  ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 7.500  9.255   11.181 1.00 13.62  ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 6.456  8.129   11.093 1.00 13.76  ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 5.475  8.304   10.376 1.00 14.83  ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 7.020  10.372  12.157 1.00 13.48  ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 6.813  9.971   13.622 1.00 15.43  ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 8.116  9.545   14.277 1.00 15.76  ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 6.137  11.111  14.418 1.00 17.15  ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 6.677  6.981   11.790 1.00 12.49  ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 5.760  5.819   11.772 1.00 12.51  ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 5.263  5.548   13.174 1.00 12.66  ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 6.075  5.521   14.081 1.00 14.42  ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 6.462  4.555   11.217 1.00 12.21  ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 7.109  4.797   9.864  1.00 14.38  ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 8.161  3.441   9.343  1.00 19.04  ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 9.574  3.646   10.411 1.00 19.18  ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 3.942  5.395   13.383 1.00 11.98  ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 3.432  5.171   14.732 1.00 12.31  ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 2.976  3.732   14.907 1.00 12.71  ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 2.422  3.123   13.983 1.00 11.53  ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 2.237  6.115   15.086 1.00 12.90  ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 2.499  7.632   15.201 1.00 16.39  ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 1.268  8.345   15.728 1.00 18.17  ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 3.673  7.913   16.125 1.00 17.36  ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 3.098  3.252   16.151 1.00 12.60  ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 2.671  1.938   16.615 1.00 12.44  ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 2.111  2.080   18.033 1.00 12.85  ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 2.429  3.041   18.738 1.00 13.24  ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 3.861  0.998   16.637 1.00 12.48  ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 1.286  1.137   18.447 1.00 13.02  ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 0.770  1.120   19.803 1.00 13.98  ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 1.855  0.406   20.599 1.00 14.92  ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 2.215  -0.728  20.270 1.00 15.86  ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? -0.573 0.362   19.864 1.00 14.87  ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? -1.064 0.227   21.310 1.00 15.46  ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? -1.617 1.092   19.015 1.00 15.55  ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 2.377  1.065   21.611 1.00 15.21  ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 3.419  0.472   22.433 1.00 16.05  ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 4.058  1.426   23.416 1.00 16.56  ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 3.829  2.639   23.359 1.00 16.60  ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 4.868  0.861   24.325 1.00 17.06  ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 5.557  1.616   25.360 1.00 17.76  ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 6.813  2.331   24.877 1.00 17.63  ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 7.668  1.735   24.232 1.00 16.29  ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 5.860  0.738   26.576 1.00 18.31  ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 6.384  1.532   27.725 1.00 21.03  ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 5.594  2.466   28.380 1.00 22.70  ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 7.625  1.557   28.265 1.00 22.67  ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 6.366  3.001   29.312 1.00 23.39  ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 7.595  2.491   29.280 1.00 23.85  ? 104 HIS   A NE2 1 
ATOM   787  N  N   . SER   A 1 99  ? 6.930  3.620   25.229 1.00 18.83  ? 105 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 99  ? 8.060  4.474   24.860 1.00 19.89  ? 105 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 99  ? 8.163  5.596   25.903 1.00 22.01  ? 105 SER   A C   1 
ATOM   790  O  O   . SER   A 1 99  ? 7.153  6.193   26.260 1.00 23.67  ? 105 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 99  ? 7.844  5.081   23.481 1.00 20.95  ? 105 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 99  ? 8.928  5.907   23.045 1.00 25.65  ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 9.363  5.805   26.444 1.00 21.55  ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 9.741  6.845   27.388 1.00 22.29  ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 10.911 7.631   26.749 1.00 23.04  ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 11.556 7.095   25.851 1.00 23.36  ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 10.136 6.228   28.739 1.00 24.40  ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 8.930  5.744   29.526 1.00 28.82  ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 9.288  5.008   30.801 1.00 34.94  ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 10.265 5.419   31.467 1.00 37.81  ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 8.586  4.032   31.150 1.00 36.34  ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 11.200 8.899   27.147 1.00 23.39  ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 12.257 9.667   26.455 1.00 23.44  ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 13.588 8.942   26.214 1.00 22.83  ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 14.146 9.017   25.111 1.00 23.98  ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 12.443 10.901  27.343 1.00 24.57  ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 11.153 11.072  28.038 1.00 25.20  ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 10.520 9.710   28.171 1.00 23.37  ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 14.059 8.211   27.218 1.00 21.32  ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 15.303 7.452   27.146 1.00 20.65  ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 15.285 6.274   26.195 1.00 19.84  ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 16.326 5.686   25.916 1.00 20.27  ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 14.095 5.920   25.681 1.00 18.30  ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 13.922 4.871   24.699 1.00 16.49  ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 14.335 5.336   23.298 1.00 14.74  ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 14.562 4.488   22.455 1.00 13.68  ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 12.475 4.332   24.681 1.00 17.02  ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 12.172 3.490   25.902 1.00 18.19  ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 13.092 2.830   26.402 1.00 18.08  ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 11.024 3.543   26.390 1.00 18.35  ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 14.486 6.664   23.040 1.00 14.63  ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 14.924 7.120   21.689 1.00 14.47  ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 16.242 6.460   21.290 1.00 13.45  ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 17.108 6.299   22.144 1.00 14.29  ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 15.017 8.645   21.600 1.00 14.88  ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 13.417 9.495   21.668 1.00 18.06  ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 16.343 5.990   20.049 1.00 12.27  ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.538 5.308   19.586 1.00 13.29  ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.388 3.792   19.535 1.00 14.30  ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 18.210 3.103   18.934 1.00 15.29  ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 16.343 3.250   20.167 1.00 13.72  ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 16.051 1.821   20.064 1.00 12.77  ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 15.718 1.487   18.610 1.00 12.47  ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 14.955 2.221   17.955 1.00 11.59  ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 16.336 0.436   18.074 1.00 11.77  ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 16.122 0.071   16.678 1.00 12.54  ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 14.816 -0.701  16.446 1.00 12.22  ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 14.432 -1.549  17.262 1.00 12.25  ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.378 -0.697  16.186 1.00 13.90  ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 18.555 0.275   16.013 1.00 14.98  ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 17.105 -1.510  14.917 1.00 15.24  ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 19.916 -0.359  15.670 1.00 16.36  ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 14.135 -0.388  15.323 1.00 11.88  ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 12.949 -1.093  14.837 1.00 11.78  ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 13.476 -1.957  13.655 1.00 13.06  ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 14.144 -1.434  12.751 1.00 12.67  ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 11.881 -0.088  14.321 1.00 11.70  ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 10.674 -0.704  13.589 1.00 13.49  ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 9.901  -1.666  14.497 1.00 14.12  ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 9.732  0.416   13.039 1.00 15.29  ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 13.239 -3.270  13.703 1.00 13.57  ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 13.716 -4.211  12.685 1.00 15.92  ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 12.571 -5.017  12.059 1.00 17.13  ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 11.643 -5.415  12.753 1.00 17.32  ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 14.632 -5.253  13.326 1.00 18.29  ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 15.944 -4.738  13.824 1.00 23.76  ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 16.832 -5.906  14.200 1.00 26.50  ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 17.368 -6.509  12.987 1.00 30.58  ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 18.516 -6.155  12.417 1.00 32.73  ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 18.910 -6.735  11.290 1.00 31.52  ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 19.286 -5.226  12.977 1.00 33.61  ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 12.691 -5.338  10.779 1.00 17.49  ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 11.740 -6.228  10.098 1.00 18.42  ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 12.546 -7.435  9.563  1.00 19.51  ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 13.764 -7.521  9.801  1.00 19.33  ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 11.012 -5.482  8.973  1.00 18.76  ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 12.084 -4.997  7.592  1.00 17.29  ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 11.904 -8.351  8.818  1.00 21.34  ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 12.628 -9.491  8.235  1.00 22.95  ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 13.781 -9.043  7.279  1.00 23.41  ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 14.771 -9.762  7.122  1.00 24.32  ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 11.644 -10.419 7.513  1.00 26.01  ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 11.013 -9.800  6.269  1.00 29.92  ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 9.996  -10.725 5.641  1.00 34.73  ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 8.780  -10.509 5.747  1.00 36.35  ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 10.474 -11.780 4.978  1.00 33.99  ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 13.696 -7.832  6.716  1.00 21.84  ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 14.712 -7.339  5.786  1.00 20.77  ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 15.855 -6.558  6.413  1.00 19.83  ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 16.848 -6.314  5.737  1.00 20.67  ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 14.071 -6.495  4.678  1.00 20.81  ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 12.912 -7.157  4.001  1.00 22.76  ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 11.610 -6.805  4.301  1.00 23.44  ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 12.898 -8.128  3.054  1.00 24.39  ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 10.843 -7.547  3.521  1.00 24.51  ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 11.569 -8.377  2.764  1.00 25.23  ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 15.721 -6.139  7.672  1.00 17.82  ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 16.773 -5.351  8.315  1.00 16.23  ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 16.253 -4.170  9.134  1.00 13.75  ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 15.123 -4.180  9.618  1.00 13.70  ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.087 -3.169  9.317  1.00 12.63  ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 16.767 -1.970  10.088 1.00 12.42  ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 15.776 -1.071  9.363  1.00 12.34  ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 16.037 -0.631  8.238  1.00 13.37  ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 18.056 -1.191  10.465 1.00 13.26  ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 17.707 0.119   11.190 1.00 13.50  ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 18.980 -2.057  11.341 1.00 14.06  ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 14.650 -0.798  10.001 1.00 11.06  ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 13.619 0.070   9.459  1.00 10.90  ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 13.809 1.540   9.936  1.00 10.82  ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 13.617 2.495   9.167  1.00 10.12  ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 12.233 -0.480  9.888  1.00 11.23  ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 11.100 0.422   9.420  1.00 12.20  ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 12.041 -1.887  9.366  1.00 12.03  ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 14.116 1.708   11.228 1.00 10.26  ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 14.258 3.045   11.796 1.00 10.72  ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 14.602 3.006   13.277 1.00 10.65  ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 14.960 1.947   13.809 1.00 10.10  ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 14.493 4.157   13.954 1.00 9.90   ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 14.824 4.219   15.386 1.00 10.01  ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 13.709 4.917   16.141 1.00 9.46   ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 13.048 5.809   15.587 1.00 8.57   ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 16.178 4.961   15.630 1.00 11.32  ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 16.274 6.256   14.818 1.00 14.18  ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.395 4.058   15.374 1.00 12.04  ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.499 7.188   15.255 1.00 15.97  ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 13.526 4.592   17.422 1.00 9.35   ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 12.518 5.276   18.246 1.00 9.42   ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 12.836 6.805   18.280 1.00 10.74  ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 14.006 7.189   18.459 1.00 10.77  ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 12.482 4.690   19.678 1.00 10.30  ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 11.545 5.502   20.559 1.00 11.21  ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 12.040 3.205   19.659 1.00 11.29  ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 11.826 7.642   18.055 1.00 11.01  ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 12.023 9.082   18.030 1.00 12.61  ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 10.985 9.837   18.854 1.00 14.42  ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 11.275 10.940  19.331 1.00 15.79  ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 12.097 9.584   16.584 1.00 15.06  ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 12.046 11.003  16.516 1.00 17.20  ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 9.785  9.271   19.048 1.00 14.08  ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 8.759  9.951   19.872 1.00 14.94  ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 8.059  8.913   20.763 1.00 16.11  ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 8.108  7.717   20.464 1.00 14.22  ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 7.718  10.692  18.979 1.00 16.34  ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 6.865  9.740   18.379 1.00 18.53  ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 8.334  11.523  17.891 1.00 16.75  ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 7.325  9.383   21.772 1.00 17.98  ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 6.579  8.493   22.652 1.00 19.75  ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 5.473  9.195   23.411 1.00 21.62  ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 5.316  10.395  23.274 1.00 22.65  ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 4.727  8.469   24.230 1.00 23.12  ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 3.657  9.073   25.033 1.00 24.48  ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 2.250  8.734   24.580 1.00 25.00  ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 2.039  8.409   23.413 1.00 24.96  ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 1.274  8.803   25.503 1.00 24.67  ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? -0.134 8.448   25.228 1.00 25.24  ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? -0.258 6.967   24.769 1.00 23.79  ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? -1.183 6.651   24.030 1.00 24.56  ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? -0.774 9.370   24.157 1.00 27.56  ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? -1.211 10.751  24.630 1.00 33.40  ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? -1.498 10.980  25.811 1.00 35.03  ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? -1.325 11.695  23.694 1.00 34.12  ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 0.674  6.098   25.182 1.00 21.10  ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 0.667  4.699   24.782 1.00 19.44  ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 0.993  4.472   23.312 1.00 17.74  ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 0.635  3.437   22.748 1.00 17.44  ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 1.709  5.402   22.693 1.00 16.94  ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 2.122  5.271   21.296 1.00 16.72  ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 3.643  5.409   21.202 1.00 17.19  ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 4.243  6.121   22.000 1.00 19.45  ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 1.486  6.389   20.441 1.00 16.83  ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? -0.033 6.384   20.323 1.00 18.02  ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? -0.518 7.667   19.621 1.00 17.98  ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? -0.498 5.112   19.566 1.00 18.67  ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 4.265  4.761   20.213 1.00 14.97  ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 5.692  4.886   19.986 1.00 13.55  ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 5.881  5.300   18.526 1.00 12.60  ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 5.246  4.730   17.631 1.00 12.13  ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 6.480  3.593   20.363 1.00 14.07  ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 5.930  2.351   19.665 1.00 13.94  ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 7.988  3.740   20.102 1.00 14.37  ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 6.701  6.330   18.297 1.00 11.90  ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 6.967  6.785   16.947 1.00 11.84  ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 8.400  6.478   16.561 1.00 11.88  ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 9.291  6.584   17.407 1.00 12.46  ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 8.611  6.077   15.292 1.00 11.19  ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 9.906  5.664   14.742 1.00 10.69  ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 10.290 6.533   13.562 1.00 11.33  ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 9.476  6.744   12.670 1.00 11.08  ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 9.874  4.215   14.251 1.00 9.77   ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 9.373  3.219   15.267 1.00 10.16  ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 10.211 2.733   16.259 1.00 10.07  ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 8.063  2.759   15.223 1.00 10.79  ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 9.751  1.789   17.187 1.00 10.34  ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 7.613  1.803   16.140 1.00 10.49  ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 8.448  1.363   17.141 1.00 9.98   ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 11.541 7.021   13.549 1.00 10.64  ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 12.028 7.822   12.430 1.00 11.68  ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 12.475 6.833   11.365 1.00 12.71  ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 13.359 6.021   11.622 1.00 11.55  ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 13.208 8.689   12.874 1.00 12.40  ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 11.818 6.838   10.199 1.00 13.62  ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 12.159 5.912   9.135  1.00 13.68  ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 13.533 6.193   8.557  1.00 13.82  ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 13.917 7.358   8.468  1.00 14.44  ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 11.108 5.982   8.013  1.00 15.78  ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 11.350 4.957   6.899  1.00 20.31  ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 11.466 3.760   7.210  1.00 19.70  ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 11.470 5.368   5.732  1.00 23.90  ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 14.290 5.134   8.162  1.00 12.36  ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 15.569 5.343   7.475  1.00 12.83  ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 15.625 4.589   6.106  1.00 13.73  ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 16.633 4.696   5.414  1.00 14.45  ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 16.826 5.027   8.330  1.00 12.80  ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 16.886 5.869   9.613  1.00 13.46  ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 16.922 3.518   8.634  1.00 12.10  ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 14.581 3.801   5.734  1.00 13.56  ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 14.566 2.973   4.516  1.00 14.74  ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 14.715 3.739   3.202  1.00 16.30  ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 15.182 3.156   2.227  1.00 17.05  ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 13.313 2.104   4.467  1.00 15.23  ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 13.254 1.093   5.600  1.00 15.23  ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 11.944 0.348   5.540  1.00 15.90  ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 10.844 1.215   5.955  1.00 14.65  ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 9.585  0.805   6.083  1.00 15.45  ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 9.250  -0.446  5.776  1.00 14.25  ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 8.651  1.639   6.521  1.00 15.63  ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 14.301 5.012   3.156  1.00 16.02  ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 14.434 5.830   1.945  1.00 16.73  ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 15.852 6.405   1.745  1.00 16.99  ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 16.148 6.920   0.656  1.00 16.71  ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 13.428 6.987   1.971  1.00 18.87  ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 13.675 7.974   3.105  1.00 23.60  ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 13.847 7.517   4.274  1.00 22.38  ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 13.678 9.197   2.836  1.00 25.85  ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 16.717 6.350   2.781  1.00 16.59  ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 18.080 6.929   2.687  1.00 17.00  ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 18.978 5.932   1.979  1.00 17.14  ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 19.822 5.304   2.615  1.00 17.69  ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 18.635 7.276   4.102  1.00 16.49  ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 17.744 8.176   4.974  1.00 17.21  ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 18.350 8.399   6.364  1.00 16.73  ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 17.473 9.511   4.295  1.00 18.28  ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 18.789 5.752   0.656  1.00 17.57  ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 19.543 4.749   -0.083 1.00 19.00  ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 21.056 4.993   -0.077 1.00 20.81  ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 21.829 4.023   -0.200 1.00 21.49  ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 19.033 4.570   -1.532 1.00 19.85  ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 17.540 4.677   -1.792 1.00 20.58  ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 17.250 4.540   -3.292 1.00 20.94  ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 16.771 3.630   -1.010 1.00 21.34  ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 21.479 6.283   0.068  1.00 20.73  ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 22.894 6.675   0.103  1.00 22.04  ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 23.662 6.050   1.286  1.00 23.20  ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 24.875 5.851   1.187  1.00 22.96  ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 23.075 8.210   0.046  1.00 21.56  ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 22.352 8.986   1.119  1.00 20.94  ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 21.116 9.558   1.033  1.00 21.30  ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 22.845 9.286   2.428  1.00 20.41  ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 20.815 10.212  2.213  1.00 21.41  ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 21.880 10.090  3.070  1.00 20.98  ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 24.037 8.993   3.106  1.00 20.95  ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 22.046 10.548  4.371  1.00 21.86  ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 24.204 9.467   4.392  1.00 21.72  ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 23.221 10.243  5.006  1.00 21.83  ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 22.950 5.660   2.363  1.00 23.61  ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 23.558 5.010   3.530  1.00 25.36  ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 24.403 3.767   3.168  1.00 29.07  ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 25.362 3.461   3.880  1.00 29.00  ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 22.485 4.632   4.567  1.00 24.35  ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 21.928 5.752   5.426  1.00 24.80  ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 20.850 5.229   6.380  1.00 24.88  ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 23.044 6.447   6.223  1.00 25.58  ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 24.071 3.088   2.046  1.00 31.97  ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 24.761 1.897   1.543  1.00 35.55  ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 25.891 2.172   0.552  1.00 39.15  ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 26.340 1.217   -0.083 1.00 40.27  ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 23.769 0.976   0.833  1.00 37.84  ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 22.824 0.280   1.760  1.00 43.56  ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 23.268 -0.131  2.859  1.00 45.63  ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 21.644 0.135   1.393  1.00 45.29  ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 26.317 3.431   0.355  1.00 40.86  ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 27.411 3.716   -0.584 1.00 42.81  ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 28.306 4.864   -0.136 1.00 44.09  ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 29.169 5.315   -0.906 1.00 44.87  ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 26.903 3.935   -2.022 1.00 45.90  ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 25.817 4.985   -2.173 1.00 51.56  ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 24.606 4.468   -2.924 1.00 57.92  ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 23.968 5.256   -3.659 1.00 58.58  ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 24.300 3.263   -2.780 1.00 60.85  ? 145 GLU   A OE2 1 
HETATM 1081 N  N1  . A1BN4 B 2 .   ? 10.049 13.501  22.486 1.00 31.46  ? 201 A1BN4 A N1  1 
HETATM 1082 C  C4  . A1BN4 B 2 .   ? 11.173 14.083  23.239 1.00 31.19  ? 201 A1BN4 A C4  1 
HETATM 1083 C  C5  . A1BN4 B 2 .   ? 9.278  12.472  22.893 1.00 32.27  ? 201 A1BN4 A C5  1 
HETATM 1084 C  C6  . A1BN4 B 2 .   ? 9.771  11.689  24.096 1.00 34.18  ? 201 A1BN4 A C6  1 
HETATM 1085 C  C7  . A1BN4 B 2 .   ? 8.672  11.462  25.108 1.00 35.91  ? 201 A1BN4 A C7  1 
HETATM 1086 C  C8  . A1BN4 B 2 .   ? 8.270  10.171  25.437 1.00 36.35  ? 201 A1BN4 A C8  1 
HETATM 1087 C  C10 . A1BN4 B 2 .   ? 6.549  11.044  26.837 1.00 37.27  ? 201 A1BN4 A C10 1 
HETATM 1088 O  O1  . A1BN4 B 2 .   ? 8.248  12.166  22.313 1.00 31.16  ? 201 A1BN4 A O1  1 
HETATM 1089 C  C3  . A1BN4 B 2 .   ? 12.460 14.043  22.416 1.00 30.63  ? 201 A1BN4 A C3  1 
HETATM 1090 C  C2  . A1BN4 B 2 .   ? 12.240 14.618  21.014 1.00 30.24  ? 201 A1BN4 A C2  1 
HETATM 1091 C  C12 . A1BN4 B 2 .   ? 9.818  14.126  21.182 1.00 30.61  ? 201 A1BN4 A C12 1 
HETATM 1092 C  C1  . A1BN4 B 2 .   ? 11.058 13.932  20.313 1.00 30.10  ? 201 A1BN4 A C1  1 
HETATM 1093 C  C   . A1BN4 B 2 .   ? 10.861 14.441  18.895 1.00 29.50  ? 201 A1BN4 A C   1 
HETATM 1094 O  O   . A1BN4 B 2 .   ? 10.470 15.589  18.679 1.00 29.51  ? 201 A1BN4 A O   1 
HETATM 1095 N  N   . A1BN4 B 2 .   ? 11.110 13.572  17.932 1.00 28.70  ? 201 A1BN4 A N   1 
HETATM 1096 C  C11 . A1BN4 B 2 .   ? 7.971  12.509  25.719 1.00 37.29  ? 201 A1BN4 A C11 1 
HETATM 1097 O  O2  . A1BN4 B 2 .   ? 8.278  13.785  25.626 1.00 37.67  ? 201 A1BN4 A O2  1 
HETATM 1098 N  N2  . A1BN4 B 2 .   ? 6.880  12.318  26.579 1.00 37.67  ? 201 A1BN4 A N2  1 
HETATM 1099 C  C9  . A1BN4 B 2 .   ? 7.215  9.956   26.309 1.00 36.65  ? 201 A1BN4 A C9  1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 10.892 -5.274  5.561  1.00 19.76  2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 15.958 -8.943  10.999 1.00 100.97 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 17.184 -8.759  10.156 1.00 100.96 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 15.315 -10.610 10.688 1.00 100.93 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 16.495 -9.317  12.689 1.00 101.02 ? 203 DMS   A C2  1 
HETATM 1105 S  S   . DMS   E 4 .   ? 18.955 -2.709  19.356 1.00 60.56  ? 204 DMS   A S   1 
HETATM 1106 O  O   . DMS   E 4 .   ? 18.338 -1.380  19.746 1.00 59.86  ? 204 DMS   A O   1 
HETATM 1107 C  C1  . DMS   E 4 .   ? 17.684 -3.712  18.517 1.00 60.46  ? 204 DMS   A C1  1 
HETATM 1108 C  C2  . DMS   E 4 .   ? 19.075 -3.757  20.840 1.00 60.68  ? 204 DMS   A C2  1 
HETATM 1109 O  O   . HOH   F 5 .   ? 23.892 -6.944  9.230  1.00 36.46  ? 301 HOH   A O   1 
HETATM 1110 O  O   . HOH   F 5 .   ? 22.302 -2.136  4.079  1.00 26.17  ? 302 HOH   A O   1 
HETATM 1111 O  O   . HOH   F 5 .   ? 8.954  1.838   2.975  1.00 19.05  ? 303 HOH   A O   1 
HETATM 1112 O  O   . HOH   F 5 .   ? 18.513 19.006  27.419 1.00 51.76  ? 304 HOH   A O   1 
HETATM 1113 O  O   . HOH   F 5 .   ? 19.858 8.182   19.159 1.00 14.00  ? 305 HOH   A O   1 
HETATM 1114 O  O   . HOH   F 5 .   ? 8.015  -4.737  0.686  1.00 23.12  ? 306 HOH   A O   1 
HETATM 1115 O  O   . HOH   F 5 .   ? 29.468 2.630   10.567 1.00 32.05  ? 307 HOH   A O   1 
HETATM 1116 O  O   . HOH   F 5 .   ? 11.157 16.716  5.878  1.00 45.91  ? 308 HOH   A O   1 
HETATM 1117 O  O   . HOH   F 5 .   ? 23.548 21.283  8.230  1.00 30.38  ? 309 HOH   A O   1 
HETATM 1118 O  O   . HOH   F 5 .   ? 17.758 20.438  9.666  1.00 18.64  ? 310 HOH   A O   1 
HETATM 1119 O  O   . HOH   F 5 .   ? 30.979 19.621  11.282 1.00 29.60  ? 311 HOH   A O   1 
HETATM 1120 O  O   . HOH   F 5 .   ? 7.704  19.034  18.358 1.00 37.95  ? 312 HOH   A O   1 
HETATM 1121 O  O   . HOH   F 5 .   ? 10.553 7.583   4.606  1.00 20.36  ? 313 HOH   A O   1 
HETATM 1122 O  O   . HOH   F 5 .   ? 3.774  -5.674  21.162 1.00 20.40  ? 314 HOH   A O   1 
HETATM 1123 O  O   . HOH   F 5 .   ? -0.175 1.544   24.457 1.00 22.37  ? 315 HOH   A O   1 
HETATM 1124 O  O   . HOH   F 5 .   ? 11.338 1.495   33.458 1.00 22.13  ? 316 HOH   A O   1 
HETATM 1125 O  O   . HOH   F 5 .   ? 9.570  17.485  20.366 1.00 25.43  ? 317 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 14.656 1.732   23.255 1.00 15.48  ? 318 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 0.372  -0.890  16.569 1.00 10.48  ? 319 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 22.499 17.345  19.404 1.00 15.93  ? 320 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 8.880  20.545  10.717 1.00 41.97  ? 321 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 14.594 -4.903  17.133 1.00 21.73  ? 322 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 14.899 11.609  24.173 1.00 17.87  ? 323 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 5.779  13.304  21.731 1.00 35.76  ? 324 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 9.611  3.957   33.746 1.00 27.89  ? 325 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 11.165 10.978  11.573 1.00 15.43  ? 326 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 4.437  9.858   19.750 1.00 39.61  ? 327 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 6.612  3.068   32.886 1.00 42.18  ? 328 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 0.748  -3.060  19.756 1.00 27.02  ? 329 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 21.452 -5.856  10.461 1.00 38.34  ? 330 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 19.883 21.999  7.381  1.00 44.38  ? 331 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 12.945 9.795   9.500  1.00 14.22  ? 332 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 17.729 18.279  17.106 1.00 17.61  ? 333 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 17.699 1.693   23.200 1.00 16.82  ? 334 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 18.834 -0.988  27.512 1.00 24.20  ? 335 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 5.805  7.535   28.354 1.00 46.07  ? 336 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 13.671 8.372   30.016 1.00 23.63  ? 337 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 4.810  -6.480  7.205  1.00 28.58  ? 338 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 4.406  5.097   24.641 1.00 24.58  ? 339 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 10.306 4.276   3.387  1.00 17.84  ? 340 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 10.243 -5.694  31.887 1.00 28.75  ? 341 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 5.876  1.204   6.034  1.00 23.78  ? 342 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 26.923 7.780   0.256  1.00 40.78  ? 343 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 30.192 10.173  17.332 1.00 27.28  ? 344 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 0.035  2.996   6.844  1.00 33.16  ? 345 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 29.892 10.286  19.939 1.00 21.65  ? 346 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 10.391 8.392   23.366 1.00 38.81  ? 347 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 18.639 12.139  2.140  1.00 35.54  ? 348 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 31.082 18.223  9.006  1.00 29.49  ? 349 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 30.008 4.221   3.732  1.00 40.72  ? 350 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 6.179  -6.334  29.093 1.00 28.71  ? 351 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 23.456 1.652   19.645 1.00 30.72  ? 352 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 8.556  -7.922  9.160  1.00 26.36  ? 353 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 5.153  -2.058  24.075 1.00 19.14  ? 354 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 31.278 1.784   12.879 1.00 31.51  ? 355 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 1.274  -3.151  17.395 1.00 23.04  ? 356 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 28.151 -2.751  13.227 1.00 36.66  ? 357 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 11.961 20.721  12.767 1.00 36.29  ? 358 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 14.283 20.407  8.506  1.00 35.65  ? 359 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 28.547 20.770  18.726 1.00 26.72  ? 360 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? -3.730 12.492  27.165 1.00 35.02  ? 361 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 18.455 18.296  5.293  1.00 32.75  ? 362 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 18.936 23.281  15.263 1.00 23.48  ? 363 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 15.625 -5.297  1.856  1.00 23.70  ? 364 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 14.719 13.989  3.739  1.00 30.17  ? 365 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 22.392 18.297  6.210  1.00 24.57  ? 366 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 3.843  -2.920  21.779 1.00 25.95  ? 367 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 9.958  -10.913 1.908  1.00 65.12  ? 368 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 11.338 17.228  26.801 1.00 26.61  ? 369 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 15.829 23.310  14.501 1.00 26.30  ? 370 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 21.745 8.174   21.297 1.00 21.21  ? 371 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 3.043  -3.943  3.465  1.00 33.99  ? 372 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 30.900 20.261  17.497 1.00 33.77  ? 373 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 2.360  14.173  19.781 1.00 48.97  ? 374 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 6.403  22.273  11.099 1.00 40.80  ? 375 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 20.757 21.304  17.701 1.00 25.56  ? 376 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 23.966 6.605   21.166 1.00 47.32  ? 377 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 35.541 9.882   10.005 1.00 70.19  ? 378 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 4.186  -1.707  29.003 1.00 39.20  ? 379 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 26.636 21.159  20.187 1.00 45.22  ? 380 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 0.195  -5.197  16.792 1.00 56.28  ? 381 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 7.386  -6.261  2.824  1.00 26.77  ? 382 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 3.596  11.623  18.104 1.00 35.74  ? 383 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 8.447  21.612  26.719 1.00 43.53  ? 384 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 11.330 12.880  0.499  1.00 45.72  ? 385 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 1.831  1.334   26.825 1.00 34.00  ? 386 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 11.594 22.798  14.529 1.00 42.55  ? 387 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 12.481 -9.553  13.244 1.00 34.86  ? 388 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 26.335 10.504  -0.487 1.00 37.37  ? 389 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 8.723  6.547   2.619  1.00 41.02  ? 390 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 31.865 3.472   15.271 1.00 31.85  ? 391 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.3164 0.2860 0.3020 -0.0008 -0.0670 -0.0092 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3146 0.2914 0.3290 0.0004  -0.0722 -0.0065 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2994 0.2861 0.3336 0.0024  -0.0657 -0.0020 7   SER   A C   
4    O O   . SER   A 1   ? 0.3093 0.2963 0.3341 0.0023  -0.0605 -0.0001 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3427 0.3117 0.3596 -0.0030 -0.0892 -0.0032 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3872 0.3495 0.3908 -0.0058 -0.0962 0.0026  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2741 0.2676 0.3344 0.0036  -0.0646 -0.0011 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2577 0.2582 0.3365 0.0046  -0.0567 0.0015  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2455 0.2524 0.3416 0.0053  -0.0481 -0.0008 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2490 0.2569 0.3392 0.0055  -0.0455 -0.0042 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2234 0.2334 0.3405 0.0052  -0.0428 0.0011  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2120 0.2259 0.3432 0.0044  -0.0328 -0.0009 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2031 0.2180 0.3406 0.0032  -0.0202 -0.0014 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2011 0.2143 0.3404 0.0038  -0.0206 0.0005  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1949 0.2093 0.3517 0.0045  -0.0383 0.0007  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1898 0.2057 0.3294 0.0008  -0.0088 -0.0041 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1936 0.2076 0.3373 -0.0018 0.0046  -0.0060 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1913 0.2047 0.3614 -0.0026 0.0118  -0.0065 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1853 0.2000 0.3595 -0.0034 0.0112  -0.0065 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2081 0.2210 0.3284 -0.0061 0.0125  -0.0087 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2076 0.2227 0.3067 -0.0052 0.0055  -0.0078 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2240 0.2317 0.3445 -0.0103 0.0266  -0.0119 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2305 0.2463 0.3122 -0.0089 0.0084  -0.0083 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1951 0.2063 0.3855 -0.0023 0.0195  -0.0069 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1992 0.2100 0.4199 -0.0027 0.0289  -0.0075 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2211 0.2254 0.4390 -0.0071 0.0494  -0.0130 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2246 0.2252 0.4472 -0.0067 0.0552  -0.0145 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1879 0.2014 0.4426 0.0016  0.0199  -0.0027 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1900 0.2072 0.4443 0.0041  -0.0012 0.0024  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1961 0.2163 0.4657 0.0038  -0.0070 0.0037  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2018 0.2178 0.4381 0.0057  -0.0148 0.0055  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2002 0.2214 0.4668 0.0049  -0.0265 0.0073  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2130 0.2292 0.4440 0.0065  -0.0331 0.0092  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2157 0.2342 0.4615 0.0059  -0.0393 0.0097  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2356 0.2521 0.4723 0.0056  -0.0573 0.0122  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2304 0.2316 0.4387 -0.0121 0.0607  -0.0161 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2458 0.2376 0.4440 -0.0184 0.0812  -0.0222 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2491 0.2383 0.4658 -0.0214 0.0953  -0.0237 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2462 0.2385 0.4589 -0.0224 0.0901  -0.0210 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2728 0.2601 0.4275 -0.0243 0.0805  -0.0239 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2867 0.2785 0.4263 -0.0249 0.0697  -0.0199 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2910 0.2657 0.4279 -0.0331 0.1002  -0.0304 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2450 0.2287 0.4860 -0.0223 0.1134  -0.0279 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2505 0.2317 0.5137 -0.0252 0.1298  -0.0297 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2480 0.2405 0.5435 -0.0201 0.1163  -0.0231 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2408 0.2414 0.5621 -0.0133 0.1006  -0.0184 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2520 0.2441 0.5423 -0.0240 0.1195  -0.0221 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2448 0.2467 0.5630 -0.0202 0.1054  -0.0162 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2312 0.2369 0.5207 -0.0192 0.0846  -0.0124 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2393 0.2483 0.5367 -0.0196 0.0778  -0.0092 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2722 0.2722 0.6143 -0.0242 0.1226  -0.0169 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3346 0.3351 0.7231 -0.0221 0.1382  -0.0190 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3424 0.3515 0.7676 -0.0154 0.1254  -0.0149 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3615 0.3516 0.7486 -0.0281 0.1663  -0.0252 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2149 0.2200 0.4745 -0.0178 0.0746  -0.0128 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1956 0.2036 0.4294 -0.0165 0.0572  -0.0100 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1638 0.1767 0.3959 -0.0107 0.0392  -0.0079 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1584 0.1707 0.3942 -0.0088 0.0406  -0.0088 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2176 0.2191 0.4105 -0.0222 0.0630  -0.0117 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2495 0.2435 0.4343 -0.0298 0.0790  -0.0126 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2633 0.2587 0.4611 -0.0307 0.0780  -0.0095 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2771 0.2609 0.4381 -0.0371 0.0948  -0.0165 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2843 0.2714 0.4730 -0.0386 0.0934  -0.0096 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3033 0.2775 0.4512 -0.0457 0.1098  -0.0171 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3150 0.2910 0.4767 -0.0463 0.1093  -0.0132 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3573 0.3226 0.5043 -0.0556 0.1250  -0.0130 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1428 0.1589 0.3665 -0.0084 0.0232  -0.0055 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1321 0.1503 0.3457 -0.0043 0.0072  -0.0041 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1329 0.1501 0.3147 -0.0051 0.0031  -0.0049 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1313 0.1479 0.3115 -0.0064 0.0018  -0.0044 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1376 0.1586 0.3743 -0.0016 -0.0081 -0.0010 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1694 0.1895 0.3869 0.0005  -0.0254 -0.0003 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2022 0.2227 0.4409 0.0015  -0.0414 0.0031  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2282 0.2448 0.4467 0.0013  -0.0552 0.0019  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2577 0.2701 0.4566 0.0020  -0.0666 0.0023  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2398 0.2521 0.4381 0.0030  -0.0678 0.0052  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2713 0.2780 0.4504 0.0011  -0.0761 -0.0003 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1309 0.1475 0.2903 -0.0046 0.0021  -0.0057 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1382 0.1549 0.2733 -0.0049 -0.0014 -0.0058 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1372 0.1548 0.2649 -0.0009 -0.0138 -0.0058 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1480 0.1655 0.2732 0.0006  -0.0160 -0.0056 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1474 0.1626 0.2634 -0.0085 0.0071  -0.0067 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1520 0.1683 0.2486 -0.0090 0.0026  -0.0054 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1422 0.1530 0.2610 -0.0140 0.0211  -0.0079 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1243 0.1412 0.2471 0.0005  -0.0207 -0.0062 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1357 0.1507 0.2482 0.0033  -0.0304 -0.0075 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1347 0.1492 0.2336 0.0043  -0.0303 -0.0088 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1474 0.1630 0.2487 0.0029  -0.0262 -0.0076 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1525 0.1642 0.2772 0.0038  -0.0410 -0.0077 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1627 0.1752 0.3033 0.0036  -0.0444 -0.0050 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1564 0.1679 0.2945 0.0026  -0.0407 -0.0077 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1205 0.1324 0.2061 0.0065  -0.0346 -0.0112 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1283 0.1390 0.2068 0.0082  -0.0337 -0.0131 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1465 0.1533 0.2349 0.0081  -0.0379 -0.0143 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1569 0.1597 0.2506 0.0073  -0.0446 -0.0155 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1360 0.1421 0.1991 0.0100  -0.0354 -0.0167 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1400 0.1496 0.1937 0.0099  -0.0309 -0.0153 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1668 0.1751 0.2173 0.0088  -0.0332 -0.0140 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1287 0.1425 0.1801 0.0108  -0.0250 -0.0148 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1455 0.1534 0.2386 0.0083  -0.0350 -0.0129 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1451 0.1485 0.2486 0.0081  -0.0385 -0.0136 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1689 0.1639 0.2667 0.0097  -0.0444 -0.0197 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1832 0.1734 0.2886 0.0080  -0.0506 -0.0212 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1272 0.1320 0.2351 0.0081  -0.0351 -0.0099 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1401 0.1407 0.2610 0.0067  -0.0373 -0.0085 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1723 0.1727 0.2959 0.0077  -0.0359 -0.0045 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1987 0.1945 0.3343 0.0060  -0.0375 -0.0016 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2093 0.1981 0.3525 0.0081  -0.0410 -0.0054 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1915 0.1759 0.3290 0.0114  -0.0428 -0.0133 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2055 0.1901 0.3605 0.0062  -0.0421 -0.0017 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1719 0.1641 0.2555 0.0119  -0.0424 -0.0235 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1958 0.1768 0.2685 0.0122  -0.0459 -0.0306 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2170 0.1922 0.2798 0.0089  -0.0548 -0.0323 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2436 0.2074 0.2968 0.0070  -0.0607 -0.0377 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2106 0.1888 0.2717 0.0150  -0.0382 -0.0347 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2451 0.2259 0.2916 0.0148  -0.0350 -0.0343 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2505 0.2425 0.3023 0.0156  -0.0302 -0.0287 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2686 0.2407 0.2944 0.0130  -0.0361 -0.0385 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2709 0.2617 0.3079 0.0149  -0.0282 -0.0296 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2828 0.2616 0.3031 0.0132  -0.0314 -0.0350 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2138 0.1955 0.2796 0.0078  -0.0564 -0.0274 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2262 0.2035 0.2879 0.0048  -0.0667 -0.0265 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2164 0.1980 0.3025 0.0030  -0.0730 -0.0223 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2234 0.2034 0.3134 0.0007  -0.0826 -0.0197 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2290 0.2093 0.2799 0.0049  -0.0647 -0.0235 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2585 0.2343 0.2862 0.0061  -0.0575 -0.0273 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2665 0.2459 0.2863 0.0058  -0.0551 -0.0234 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2665 0.2271 0.2727 0.0035  -0.0623 -0.0339 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2020 0.1894 0.3061 0.0037  -0.0674 -0.0206 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1933 0.1849 0.3227 0.0017  -0.0702 -0.0167 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2028 0.1871 0.3387 -0.0012 -0.0837 -0.0184 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2157 0.1912 0.3398 -0.0020 -0.0876 -0.0235 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1848 0.1810 0.3269 0.0019  -0.0608 -0.0147 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2069 0.1946 0.3634 -0.0033 -0.0907 -0.0142 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2210 0.2029 0.3880 -0.0073 -0.1067 -0.0141 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2297 0.2135 0.4225 -0.0090 -0.1060 -0.0137 24  THR   A C   
137  O O   . THR   A 18  ? 0.2206 0.2109 0.4244 -0.0073 -0.0925 -0.0121 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2161 0.2022 0.3996 -0.0084 -0.1153 -0.0078 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2033 0.2004 0.4191 -0.0070 -0.1053 -0.0034 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2269 0.2112 0.3871 -0.0070 -0.1152 -0.0069 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2379 0.2161 0.4422 -0.0134 -0.1212 -0.0139 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2532 0.2338 0.4868 -0.0157 -0.1216 -0.0126 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2341 0.2276 0.5011 -0.0145 -0.1109 -0.0061 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2320 0.2291 0.5119 -0.0144 -0.0986 -0.0052 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2943 0.2676 0.5375 -0.0216 -0.1424 -0.0128 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3879 0.3461 0.6046 -0.0245 -0.1497 -0.0208 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4250 0.3797 0.6408 -0.0234 -0.1402 -0.0250 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4277 0.3719 0.6186 -0.0293 -0.1653 -0.0252 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4422 0.3815 0.6337 -0.0265 -0.1487 -0.0327 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4577 0.3893 0.6317 -0.0307 -0.1636 -0.0336 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2249 0.2239 0.5035 -0.0138 -0.1141 -0.0018 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2133 0.2230 0.5244 -0.0126 -0.1020 0.0032  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1970 0.2099 0.4950 -0.0098 -0.0803 0.0019  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1909 0.2089 0.5102 -0.0106 -0.0662 0.0038  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2452 0.2584 0.5714 -0.0120 -0.1109 0.0081  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3013 0.3243 0.6684 -0.0110 -0.0985 0.0125  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3194 0.3464 0.7216 -0.0134 -0.0987 0.0149  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3135 0.3397 0.6768 -0.0078 -0.0851 0.0129  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1886 0.1979 0.4514 -0.0074 -0.0776 -0.0013 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1784 0.1899 0.4260 -0.0059 -0.0602 -0.0021 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1759 0.1855 0.4248 -0.0077 -0.0533 -0.0024 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1715 0.1837 0.4279 -0.0094 -0.0392 -0.0004 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1800 0.1883 0.3932 -0.0033 -0.0612 -0.0049 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1841 0.1946 0.3932 -0.0017 -0.0622 -0.0035 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1689 0.1843 0.3971 -0.0018 -0.0539 -0.0009 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1946 0.2009 0.3820 -0.0006 -0.0701 -0.0052 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1740 0.1775 0.4159 -0.0082 -0.0630 -0.0050 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1790 0.1795 0.4242 -0.0100 -0.0583 -0.0045 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1882 0.1919 0.4667 -0.0137 -0.0544 -0.0009 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1874 0.1909 0.4695 -0.0159 -0.0427 0.0018  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1702 0.1619 0.4025 -0.0095 -0.0693 -0.0091 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1697 0.1581 0.3726 -0.0059 -0.0671 -0.0123 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1841 0.1686 0.3670 -0.0041 -0.0737 -0.0167 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1638 0.1522 0.3560 -0.0044 -0.0578 -0.0107 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1940 0.1767 0.3573 -0.0009 -0.0674 -0.0187 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1818 0.1677 0.3519 -0.0009 -0.0586 -0.0145 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1700 0.1594 0.3694 -0.0063 -0.0493 -0.0057 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1885 0.1744 0.3485 0.0014  -0.0523 -0.0131 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1824 0.1707 0.3677 -0.0047 -0.0446 -0.0036 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1875 0.1750 0.3558 -0.0006 -0.0465 -0.0071 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1933 0.1998 0.4969 -0.0150 -0.0639 0.0000  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2019 0.2128 0.5435 -0.0185 -0.0597 0.0037  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2160 0.2328 0.5700 -0.0188 -0.0396 0.0066  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2239 0.2432 0.6058 -0.0221 -0.0297 0.0093  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1981 0.2112 0.5660 -0.0198 -0.0768 0.0050  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2087 0.2268 0.5427 -0.0161 -0.0332 0.0054  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1952 0.2159 0.5331 -0.0169 -0.0136 0.0063  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1855 0.2017 0.4845 -0.0173 -0.0037 0.0049  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1750 0.1913 0.4647 -0.0176 0.0081  0.0040  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2081 0.2336 0.5608 -0.0140 -0.0158 0.0065  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2306 0.2616 0.6285 -0.0144 -0.0237 0.0097  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2647 0.2991 0.6951 -0.0164 -0.0100 0.0114  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2081 0.2393 0.6096 -0.0131 -0.0457 0.0109  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1820 0.1937 0.4602 -0.0176 -0.0092 0.0050  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1793 0.1872 0.4244 -0.0180 -0.0037 0.0052  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1910 0.1960 0.4285 -0.0235 0.0148  0.0075  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2016 0.2040 0.4520 -0.0280 0.0233  0.0101  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1809 0.1842 0.4161 -0.0176 -0.0125 0.0061  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2102 0.2099 0.4177 -0.0184 -0.0089 0.0085  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2128 0.2150 0.3998 -0.0145 -0.0128 0.0058  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2130 0.2075 0.4198 -0.0183 -0.0154 0.0106  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1937 0.1976 0.4077 -0.0241 0.0209  0.0064  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2002 0.1983 0.3968 -0.0307 0.0368  0.0078  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2093 0.2031 0.3749 -0.0325 0.0311  0.0114  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2109 0.1982 0.3662 -0.0384 0.0360  0.0161  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2129 0.2113 0.4056 -0.0311 0.0470  0.0039  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2312 0.2205 0.3970 -0.0393 0.0621  0.0042  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2043 0.2066 0.4328 -0.0294 0.0534  0.0017  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2014 0.1989 0.3548 -0.0275 0.0201  0.0100  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2046 0.1998 0.3350 -0.0284 0.0141  0.0137  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1954 0.1958 0.3265 -0.0209 0.0011  0.0114  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1904 0.1948 0.3274 -0.0167 -0.0015 0.0069  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2137 0.2056 0.3202 -0.0339 0.0219  0.0141  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2302 0.2210 0.3152 -0.0354 0.0141  0.0187  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2477 0.2327 0.3206 -0.0408 0.0116  0.0261  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2259 0.2220 0.3025 -0.0316 0.0069  0.0172  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2560 0.2427 0.3148 -0.0408 0.0027  0.0296  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2401 0.2340 0.3019 -0.0350 0.0004  0.0239  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2277 0.2294 0.3079 -0.0264 0.0057  0.0117  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2458 0.2445 0.3000 -0.0330 -0.0067 0.0247  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2387 0.2442 0.3085 -0.0246 -0.0004 0.0123  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2396 0.2441 0.2980 -0.0278 -0.0062 0.0184  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1816 0.1806 0.3067 -0.0194 -0.0064 0.0147  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1739 0.1763 0.2982 -0.0128 -0.0157 0.0119  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1625 0.1641 0.2768 -0.0132 -0.0197 0.0172  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1503 0.1474 0.2634 -0.0174 -0.0195 0.0238  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1959 0.1971 0.3359 -0.0083 -0.0224 0.0077  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2334 0.2295 0.3850 -0.0100 -0.0240 0.0109  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2496 0.2425 0.3981 -0.0084 -0.0285 0.0146  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2580 0.2462 0.4118 -0.0118 -0.0279 0.0204  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2048 0.1996 0.3474 -0.0040 -0.0321 0.0124  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1458 0.1515 0.2545 -0.0091 -0.0235 0.0154  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1425 0.1490 0.2482 -0.0087 -0.0282 0.0211  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1382 0.1477 0.2503 -0.0012 -0.0317 0.0160  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1387 0.1523 0.2445 0.0006  -0.0301 0.0120  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1565 0.1647 0.2464 -0.0146 -0.0269 0.0259  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2252 0.2341 0.3146 -0.0159 -0.0342 0.0343  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2236 0.2352 0.3269 -0.0096 -0.0387 0.0342  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2688 0.2750 0.3439 -0.0238 -0.0354 0.0410  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1420 0.1481 0.2663 0.0026  -0.0351 0.0159  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1498 0.1559 0.2797 0.0092  -0.0357 0.0099  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1526 0.1588 0.2823 0.0092  -0.0357 0.0098  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1493 0.1618 0.2785 0.0108  -0.0355 0.0128  36  SER   A C   
244  O O   . SER   A 30  ? 0.1568 0.1713 0.2834 0.0145  -0.0326 0.0069  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1699 0.1692 0.3142 0.0123  -0.0380 0.0093  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1809 0.1803 0.3249 0.0123  -0.0379 0.0089  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1868 0.1835 0.3349 0.0181  -0.0361 0.0017  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2098 0.2095 0.3629 0.0113  -0.0410 0.0185  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1420 0.1572 0.2730 0.0071  -0.0390 0.0225  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1402 0.1623 0.2744 0.0078  -0.0408 0.0267  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1346 0.1619 0.2543 0.0056  -0.0375 0.0234  37  SER   A C   
252  O O   . SER   A 31  ? 0.1290 0.1623 0.2531 0.0075  -0.0372 0.0238  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1764 0.1989 0.3146 0.0028  -0.0484 0.0392  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2443 0.2655 0.3622 -0.0059 -0.0490 0.0430  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1250 0.1500 0.2304 0.0018  -0.0345 0.0203  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1233 0.1516 0.2163 -0.0002 -0.0309 0.0171  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1254 0.1526 0.2164 0.0043  -0.0270 0.0083  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1396 0.1691 0.2222 0.0034  -0.0242 0.0058  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1340 0.1593 0.2134 -0.0080 -0.0290 0.0197  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1476 0.1713 0.2210 -0.0151 -0.0337 0.0289  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1714 0.1889 0.2266 -0.0241 -0.0292 0.0300  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1602 0.1791 0.2049 -0.0262 -0.0242 0.0250  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1733 0.1868 0.1997 -0.0350 -0.0207 0.0257  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1504 0.1560 0.1633 -0.0435 -0.0215 0.0315  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1874 0.2017 0.2071 -0.0360 -0.0158 0.0205  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1259 0.1481 0.2232 0.0079  -0.0276 0.0040  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1225 0.1412 0.2154 0.0104  -0.0267 -0.0033 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1322 0.1509 0.2202 0.0068  -0.0258 -0.0034 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1415 0.1600 0.2238 0.0076  -0.0254 -0.0068 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1284 0.1481 0.2156 0.0137  -0.0240 -0.0075 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1637 0.1773 0.2420 0.0149  -0.0248 -0.0140 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1512 0.1581 0.2320 0.0154  -0.0282 -0.0172 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1864 0.2010 0.2546 0.0143  -0.0232 -0.0152 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1219 0.1403 0.2128 0.0025  -0.0245 0.0006  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1162 0.1339 0.2070 -0.0009 -0.0209 0.0001  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1338 0.1478 0.2368 -0.0019 -0.0213 0.0000  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1446 0.1561 0.2524 -0.0028 -0.0226 0.0027  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1120 0.1305 0.1937 -0.0067 -0.0155 0.0038  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1273 0.1494 0.1985 -0.0074 -0.0144 0.0035  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1326 0.1525 0.1925 -0.0148 -0.0093 0.0060  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1302 0.1532 0.2024 -0.0040 -0.0138 -0.0010 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1364 0.1502 0.2467 -0.0021 -0.0204 -0.0023 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1455 0.1573 0.2719 -0.0039 -0.0196 -0.0019 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1439 0.1570 0.2772 -0.0063 -0.0123 -0.0021 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1529 0.1678 0.2841 -0.0044 -0.0134 -0.0038 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1541 0.1636 0.2909 -0.0009 -0.0289 -0.0049 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1764 0.1844 0.3339 -0.0033 -0.0292 -0.0037 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1756 0.1787 0.3374 -0.0022 -0.0374 -0.0054 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1928 0.2030 0.3673 -0.0036 -0.0309 -0.0042 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1365 0.1479 0.2793 -0.0104 -0.0041 -0.0004 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1370 0.1486 0.2916 -0.0125 0.0053  -0.0014 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1480 0.1600 0.3302 -0.0129 0.0054  -0.0007 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1456 0.1552 0.3308 -0.0152 0.0062  0.0013  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1495 0.1569 0.2895 -0.0187 0.0191  -0.0009 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1460 0.1518 0.3029 -0.0211 0.0322  -0.0031 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1558 0.1634 0.2722 -0.0191 0.0176  -0.0014 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1452 0.1602 0.3492 -0.0106 0.0030  -0.0016 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1526 0.1692 0.3884 -0.0113 0.0028  -0.0004 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1734 0.1909 0.4299 -0.0129 0.0173  -0.0009 43  SER   A C   
300  O O   . SER   A 37  ? 0.1614 0.1781 0.4080 -0.0124 0.0235  -0.0027 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1598 0.1786 0.4087 -0.0078 -0.0151 0.0000  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1859 0.2060 0.4309 -0.0048 -0.0210 -0.0003 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1854 0.2043 0.4733 -0.0148 0.0235  0.0005  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2082 0.2276 0.5214 -0.0160 0.0395  -0.0005 44  SER   A CA  
305  C C   . SER   A 38  ? 0.2335 0.2590 0.5810 -0.0115 0.0289  0.0015  44  SER   A C   
306  O O   . SER   A 38  ? 0.2367 0.2656 0.5955 -0.0094 0.0100  0.0043  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2202 0.2378 0.5525 -0.0210 0.0546  0.0002  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2495 0.2714 0.6049 -0.0200 0.0412  0.0035  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2442 0.2698 0.6080 -0.0104 0.0403  0.0002  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2555 0.2864 0.6547 -0.0061 0.0302  0.0036  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2812 0.3143 0.7278 -0.0066 0.0471  0.0039  45  THR   A C   
312  O O   . THR   A 39  ? 0.2910 0.3189 0.7344 -0.0101 0.0715  -0.0008 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2717 0.3004 0.6515 -0.0032 0.0267  0.0028  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2912 0.3144 0.6630 -0.0055 0.0498  -0.0023 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2858 0.3124 0.6214 -0.0027 0.0128  0.0022  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2882 0.3282 0.7790 -0.0035 0.0343  0.0094  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2967 0.3403 0.8416 -0.0029 0.0493  0.0105  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3052 0.3451 0.8550 -0.0002 0.0625  0.0079  46  THR   A C   
319  O O   . THR   A 40  ? 0.3082 0.3448 0.8792 -0.0015 0.0886  0.0034  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3104 0.3631 0.9036 -0.0009 0.0275  0.0188  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3337 0.3869 0.9157 0.0023  0.0022  0.0236  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3207 0.3757 0.9133 -0.0044 0.0172  0.0204  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3012 0.3402 0.8308 0.0031  0.0457  0.0102  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3023 0.3371 0.8357 0.0057  0.0551  0.0085  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3222 0.3477 0.8037 0.0026  0.0707  0.0003  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3368 0.3604 0.7745 -0.0002 0.0651  -0.0016 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2982 0.3360 0.8375 0.0100  0.0290  0.0164  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3241 0.3433 0.8127 0.0028  0.0898  -0.0044 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3465 0.3553 0.7901 -0.0012 0.1053  -0.0125 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3466 0.3547 0.7565 0.0009  0.0876  -0.0103 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3487 0.3601 0.7797 0.0058  0.0737  -0.0044 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3694 0.3700 0.8377 -0.0021 0.1328  -0.0190 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4643 0.4514 0.8868 -0.0082 0.1511  -0.0286 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5631 0.5419 0.9612 -0.0166 0.1719  -0.0353 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5823 0.5649 1.0028 -0.0176 0.1775  -0.0336 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5954 0.5617 0.9461 -0.0236 0.1832  -0.0425 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3426 0.3461 0.7021 -0.0033 0.0884  -0.0143 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3424 0.3447 0.6673 -0.0025 0.0757  -0.0134 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3271 0.3196 0.6361 -0.0057 0.0927  -0.0201 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3380 0.3224 0.6409 -0.0111 0.1141  -0.0271 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3047 0.2962 0.6051 -0.0033 0.0840  -0.0181 50  CYS   A N   
342  C CA  A CYS   A 44  ? 0.3087 0.2900 0.5965 -0.0066 0.0993  -0.0246 50  CYS   A CA  
343  C CA  B CYS   A 44  ? 0.3082 0.2896 0.5962 -0.0065 0.0991  -0.0245 50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.3102 0.2896 0.5549 -0.0094 0.0912  -0.0253 50  CYS   A C   
345  O O   . CYS   A 44  ? 0.3100 0.2817 0.5467 -0.0115 0.0989  -0.0291 50  CYS   A O   
346  C CB  A CYS   A 44  ? 0.3096 0.2886 0.6380 -0.0018 0.1033  -0.0229 50  CYS   A CB  
347  C CB  B CYS   A 44  ? 0.3079 0.2875 0.6363 -0.0015 0.1018  -0.0223 50  CYS   A CB  
348  S SG  A CYS   A 44  ? 0.3502 0.3394 0.7048 0.0061  0.0749  -0.0096 50  CYS   A SG  
349  S SG  B CYS   A 44  ? 0.3346 0.3182 0.7240 0.0024  0.1105  -0.0201 50  CYS   A SG  
350  N N   . ASP   A 45  ? 0.2902 0.2762 0.5098 -0.0096 0.0766  -0.0219 51  ASP   A N   
351  C CA  . ASP   A 45  ? 0.2913 0.2767 0.4741 -0.0124 0.0698  -0.0222 51  ASP   A CA  
352  C C   . ASP   A 45  ? 0.2783 0.2550 0.4341 -0.0210 0.0848  -0.0295 51  ASP   A C   
353  O O   . ASP   A 45  ? 0.2746 0.2478 0.4320 -0.0245 0.0958  -0.0326 51  ASP   A O   
354  C CB  . ASP   A 45  ? 0.3271 0.3212 0.4943 -0.0102 0.0524  -0.0172 51  ASP   A CB  
355  C CG  . ASP   A 45  ? 0.3950 0.3947 0.5758 -0.0040 0.0357  -0.0104 51  ASP   A CG  
356  O OD1 . ASP   A 45  ? 0.4183 0.4157 0.6131 -0.0017 0.0345  -0.0082 51  ASP   A OD1 
357  O OD2 . ASP   A 45  ? 0.4031 0.4081 0.5796 -0.0020 0.0236  -0.0073 51  ASP   A OD2 
358  N N   . THR   A 46  ? 0.2738 0.2461 0.4042 -0.0252 0.0850  -0.0318 52  THR   A N   
359  C CA  . THR   A 46  ? 0.2829 0.2452 0.3834 -0.0350 0.0961  -0.0380 52  THR   A CA  
360  C C   . THR   A 46  ? 0.2658 0.2341 0.3380 -0.0376 0.0825  -0.0341 52  THR   A C   
361  O O   . THR   A 46  ? 0.2584 0.2337 0.3275 -0.0341 0.0701  -0.0301 52  THR   A O   
362  C CB  . THR   A 46  ? 0.3180 0.2698 0.4117 -0.0392 0.1054  -0.0437 52  THR   A CB  
363  O OG1 . THR   A 46  ? 0.3393 0.2841 0.4620 -0.0370 0.1206  -0.0479 52  THR   A OG1 
364  C CG2 . THR   A 46  ? 0.3374 0.2777 0.3942 -0.0511 0.1129  -0.0497 52  THR   A CG2 
365  N N   . ILE   A 47  ? 0.2507 0.2161 0.3045 -0.0437 0.0850  -0.0346 53  ILE   A N   
366  C CA  . ILE   A 47  ? 0.2407 0.2115 0.2718 -0.0462 0.0718  -0.0300 53  ILE   A CA  
367  C C   . ILE   A 47  ? 0.2391 0.2015 0.2419 -0.0559 0.0735  -0.0329 53  ILE   A C   
368  O O   . ILE   A 47  ? 0.2446 0.1932 0.2332 -0.0646 0.0870  -0.0391 53  ILE   A O   
369  C CB  . ILE   A 47  ? 0.2490 0.2209 0.2750 -0.0480 0.0703  -0.0270 53  ILE   A CB  
370  C CG1 . ILE   A 47  ? 0.2523 0.2311 0.3080 -0.0397 0.0694  -0.0250 53  ILE   A CG1 
371  C CG2 . ILE   A 47  ? 0.2590 0.2376 0.2684 -0.0490 0.0554  -0.0211 53  ILE   A CG2 
372  C CD1 . ILE   A 47  ? 0.2521 0.2429 0.3226 -0.0300 0.0536  -0.0203 53  ILE   A CD1 
373  N N   . ALA   A 48  ? 0.2226 0.1923 0.2174 -0.0551 0.0605  -0.0288 54  ALA   A N   
374  C CA  . ALA   A 48  ? 0.2345 0.1979 0.2053 -0.0646 0.0589  -0.0303 54  ALA   A CA  
375  C C   . ALA   A 48  ? 0.2455 0.2035 0.1914 -0.0743 0.0558  -0.0282 54  ALA   A C   
376  O O   . ALA   A 48  ? 0.2316 0.1973 0.1810 -0.0710 0.0476  -0.0222 54  ALA   A O   
377  C CB  . ALA   A 48  ? 0.2268 0.2016 0.2019 -0.0605 0.0457  -0.0254 54  ALA   A CB  
378  N N   . ARG   A 49  ? 0.2631 0.2065 0.1824 -0.0868 0.0616  -0.0326 55  ARG   A N   
379  C CA  . ARG   A 49  ? 0.2846 0.2200 0.1746 -0.0985 0.0567  -0.0295 55  ARG   A CA  
380  C C   . ARG   A 49  ? 0.3015 0.2342 0.1726 -0.1075 0.0464  -0.0284 55  ARG   A C   
381  O O   . ARG   A 49  ? 0.3207 0.2373 0.1693 -0.1186 0.0542  -0.0354 55  ARG   A O   
382  C CB  . ARG   A 49  ? 0.3046 0.2212 0.1759 -0.1076 0.0746  -0.0366 55  ARG   A CB  
383  C CG  . ARG   A 49  ? 0.3247 0.2448 0.2210 -0.0986 0.0860  -0.0380 55  ARG   A CG  
384  C CD  . ARG   A 49  ? 0.3447 0.2777 0.2526 -0.0920 0.0742  -0.0288 55  ARG   A CD  
385  N NE  . ARG   A 49  ? 0.3502 0.2846 0.2810 -0.0855 0.0856  -0.0306 55  ARG   A NE  
386  C CZ  . ARG   A 49  ? 0.3634 0.3094 0.3133 -0.0774 0.0778  -0.0246 55  ARG   A CZ  
387  N NH1 . ARG   A 49  ? 0.3475 0.3036 0.2959 -0.0745 0.0603  -0.0169 55  ARG   A NH1 
388  N NH2 . ARG   A 49  ? 0.3482 0.2949 0.3205 -0.0725 0.0879  -0.0264 55  ARG   A NH2 
389  N N   . CYS   A 50  ? 0.2969 0.2448 0.1788 -0.1030 0.0296  -0.0201 56  CYS   A N   
390  C CA  . CYS   A 50  ? 0.3048 0.2546 0.1797 -0.1091 0.0185  -0.0179 56  CYS   A CA  
391  C C   . CYS   A 50  ? 0.3002 0.2661 0.1873 -0.1055 0.0003  -0.0070 56  CYS   A C   
392  O O   . CYS   A 50  ? 0.2926 0.2676 0.1940 -0.0972 -0.0029 -0.0020 56  CYS   A O   
393  C CB  . CYS   A 50  ? 0.3025 0.2561 0.1952 -0.1023 0.0249  -0.0231 56  CYS   A CB  
394  S SG  . CYS   A 50  ? 0.2902 0.2641 0.2196 -0.0840 0.0216  -0.0184 56  CYS   A SG  
395  N N   . ASP   A 51  ? 0.3075 0.2778 0.1942 -0.1106 -0.0109 -0.0036 57  ASP   A N   
396  C CA  . ASP   A 51  ? 0.3061 0.2929 0.2121 -0.1061 -0.0263 0.0064  57  ASP   A CA  
397  C C   . ASP   A 51  ? 0.2941 0.2933 0.2235 -0.0986 -0.0265 0.0060  57  ASP   A C   
398  O O   . ASP   A 51  ? 0.2944 0.3044 0.2367 -0.0995 -0.0383 0.0129  57  ASP   A O   
399  C CB  . ASP   A 51  ? 0.3473 0.3308 0.2372 -0.1192 -0.0429 0.0146  57  ASP   A CB  
400  C CG  . ASP   A 51  ? 0.4584 0.4328 0.3301 -0.1330 -0.0484 0.0126  57  ASP   A CG  
401  O OD1 . ASP   A 51  ? 0.4745 0.4437 0.3445 -0.1330 -0.0374 0.0037  57  ASP   A OD1 
402  O OD2 . ASP   A 51  ? 0.5225 0.4946 0.3824 -0.1445 -0.0648 0.0204  57  ASP   A OD2 
403  N N   . CYS   A 52  ? 0.2766 0.2739 0.2129 -0.0917 -0.0133 -0.0013 58  CYS   A N   
404  C CA  . CYS   A 52  ? 0.2475 0.2544 0.2033 -0.0848 -0.0119 -0.0014 58  CYS   A CA  
405  C C   . CYS   A 52  ? 0.2202 0.2438 0.1988 -0.0756 -0.0190 0.0058  58  CYS   A C   
406  O O   . CYS   A 52  ? 0.2244 0.2517 0.2083 -0.0695 -0.0200 0.0081  58  CYS   A O   
407  C CB  . CYS   A 52  ? 0.2464 0.2486 0.2077 -0.0773 0.0015  -0.0081 58  CYS   A CB  
408  S SG  . CYS   A 52  ? 0.2747 0.2581 0.2191 -0.0865 0.0129  -0.0176 58  CYS   A SG  
409  N N   . GLN   A 53  ? 0.1873 0.2199 0.1802 -0.0745 -0.0220 0.0086  59  GLN   A N   
410  C CA  . GLN   A 53  ? 0.1725 0.2196 0.1885 -0.0654 -0.0244 0.0137  59  GLN   A CA  
411  C C   . GLN   A 53  ? 0.1605 0.2106 0.1863 -0.0590 -0.0158 0.0112  59  GLN   A C   
412  O O   . GLN   A 53  ? 0.1535 0.2142 0.1968 -0.0544 -0.0160 0.0148  59  GLN   A O   
413  C CB  . GLN   A 53  ? 0.1950 0.2520 0.2242 -0.0705 -0.0368 0.0217  59  GLN   A CB  
414  C CG  . GLN   A 53  ? 0.2364 0.2930 0.2619 -0.0741 -0.0475 0.0274  59  GLN   A CG  
415  C CD  . GLN   A 53  ? 0.2766 0.3453 0.3239 -0.0770 -0.0605 0.0369  59  GLN   A CD  
416  O OE1 . GLN   A 53  ? 0.2815 0.3472 0.3209 -0.0884 -0.0736 0.0422  59  GLN   A OE1 
417  N NE2 . GLN   A 53  ? 0.2664 0.3484 0.3426 -0.0673 -0.0571 0.0394  59  GLN   A NE2 
418  N N   . THR   A 54  ? 0.1461 0.1863 0.1615 -0.0597 -0.0079 0.0055  60  THR   A N   
419  C CA  . THR   A 54  ? 0.1460 0.1863 0.1678 -0.0543 -0.0006 0.0042  60  THR   A CA  
420  C C   . THR   A 54  ? 0.1364 0.1677 0.1517 -0.0493 0.0062  -0.0004 60  THR   A C   
421  O O   . THR   A 54  ? 0.1425 0.1648 0.1477 -0.0532 0.0081  -0.0042 60  THR   A O   
422  C CB  . THR   A 54  ? 0.1759 0.2137 0.1980 -0.0613 0.0005  0.0037  60  THR   A CB  
423  O OG1 . THR   A 54  ? 0.1926 0.2170 0.1997 -0.0685 0.0030  -0.0017 60  THR   A OG1 
424  C CG2 . THR   A 54  ? 0.1703 0.2178 0.2028 -0.0674 -0.0075 0.0089  60  THR   A CG2 
425  N N   . GLY   A 55  ? 0.1130 0.1462 0.1346 -0.0413 0.0095  0.0006  61  GLY   A N   
426  C CA  . GLY   A 55  ? 0.1230 0.1489 0.1430 -0.0365 0.0134  -0.0020 61  GLY   A CA  
427  C C   . GLY   A 55  ? 0.1211 0.1478 0.1450 -0.0301 0.0148  0.0005  61  GLY   A C   
428  O O   . GLY   A 55  ? 0.1312 0.1624 0.1572 -0.0304 0.0154  0.0033  61  GLY   A O   
429  N N   . VAL   A 56  ? 0.1199 0.1415 0.1448 -0.0253 0.0151  0.0000  62  VAL   A N   
430  C CA  . VAL   A 56  ? 0.1219 0.1414 0.1465 -0.0202 0.0141  0.0031  62  VAL   A CA  
431  C C   . VAL   A 56  ? 0.1219 0.1416 0.1468 -0.0150 0.0101  0.0026  62  VAL   A C   
432  O O   . VAL   A 56  ? 0.1235 0.1406 0.1535 -0.0146 0.0097  0.0004  62  VAL   A O   
433  C CB  . VAL   A 56  ? 0.1381 0.1487 0.1664 -0.0207 0.0159  0.0042  62  VAL   A CB  
434  C CG1 . VAL   A 56  ? 0.1642 0.1708 0.1900 -0.0166 0.0121  0.0090  62  VAL   A CG1 
435  C CG2 . VAL   A 56  ? 0.1363 0.1449 0.1646 -0.0264 0.0201  0.0042  62  VAL   A CG2 
436  N N   . TYR   A 57  ? 0.1201 0.1414 0.1394 -0.0117 0.0081  0.0041  63  TYR   A N   
437  C CA  . TYR   A 57  ? 0.1155 0.1352 0.1338 -0.0076 0.0035  0.0032  63  TYR   A CA  
438  C C   . TYR   A 57  ? 0.1298 0.1421 0.1405 -0.0058 -0.0007 0.0061  63  TYR   A C   
439  O O   . TYR   A 57  ? 0.1323 0.1417 0.1345 -0.0072 0.0015  0.0088  63  TYR   A O   
440  C CB  . TYR   A 57  ? 0.1101 0.1359 0.1274 -0.0060 0.0038  0.0013  63  TYR   A CB  
441  C CG  . TYR   A 57  ? 0.1260 0.1518 0.1351 -0.0048 0.0068  0.0017  63  TYR   A CG  
442  C CD1 . TYR   A 57  ? 0.1383 0.1689 0.1493 -0.0071 0.0125  0.0030  63  TYR   A CD1 
443  C CD2 . TYR   A 57  ? 0.1531 0.1733 0.1529 -0.0020 0.0049  0.0002  63  TYR   A CD2 
444  C CE1 . TYR   A 57  ? 0.1621 0.1924 0.1676 -0.0061 0.0183  0.0028  63  TYR   A CE1 
445  C CE2 . TYR   A 57  ? 0.1753 0.1934 0.1655 -0.0017 0.0106  -0.0008 63  TYR   A CE2 
446  C CZ  . TYR   A 57  ? 0.1806 0.2036 0.1739 -0.0035 0.0183  0.0006  63  TYR   A CZ  
447  O OH  . TYR   A 57  ? 0.2042 0.2246 0.1896 -0.0035 0.0267  -0.0007 63  TYR   A OH  
448  N N   . TYR   A 58  ? 0.1341 0.1425 0.1474 -0.0034 -0.0073 0.0063  64  TYR   A N   
449  C CA  . TYR   A 58  ? 0.1574 0.1573 0.1611 -0.0030 -0.0144 0.0099  64  TYR   A CA  
450  C C   . TYR   A 58  ? 0.1633 0.1610 0.1506 -0.0023 -0.0150 0.0073  64  TYR   A C   
451  O O   . TYR   A 58  ? 0.1521 0.1535 0.1436 -0.0004 -0.0151 0.0032  64  TYR   A O   
452  C CB  . TYR   A 58  ? 0.1618 0.1583 0.1785 -0.0016 -0.0229 0.0121  64  TYR   A CB  
453  C CG  . TYR   A 58  ? 0.1824 0.1692 0.1879 -0.0025 -0.0333 0.0174  64  TYR   A CG  
454  C CD1 . TYR   A 58  ? 0.1969 0.1772 0.1937 -0.0048 -0.0345 0.0233  64  TYR   A CD1 
455  C CD2 . TYR   A 58  ? 0.1963 0.1792 0.1972 -0.0021 -0.0427 0.0169  64  TYR   A CD2 
456  C CE1 . TYR   A 58  ? 0.2255 0.1951 0.2083 -0.0070 -0.0455 0.0294  64  TYR   A CE1 
457  C CE2 . TYR   A 58  ? 0.2184 0.1905 0.2056 -0.0046 -0.0544 0.0223  64  TYR   A CE2 
458  C CZ  . TYR   A 58  ? 0.2473 0.2125 0.2240 -0.0072 -0.0560 0.0289  64  TYR   A CZ  
459  O OH  . TYR   A 58  ? 0.2828 0.2356 0.2422 -0.0110 -0.0691 0.0354  64  TYR   A OH  
460  N N   . CYS   A 59  ? 0.1719 0.1617 0.1397 -0.0044 -0.0146 0.0096  65  CYS   A N   
461  C CA  . CYS   A 59  ? 0.1942 0.1780 0.1421 -0.0050 -0.0125 0.0062  65  CYS   A CA  
462  C C   . CYS   A 59  ? 0.2237 0.1936 0.1532 -0.0076 -0.0235 0.0095  65  CYS   A C   
463  O O   . CYS   A 59  ? 0.2318 0.1934 0.1465 -0.0111 -0.0249 0.0149  65  CYS   A O   
464  C CB  . CYS   A 59  ? 0.2026 0.1873 0.1410 -0.0067 -0.0005 0.0056  65  CYS   A CB  
465  S SG  . CYS   A 59  ? 0.2405 0.2157 0.1549 -0.0077 0.0070  -0.0001 65  CYS   A SG  
466  N N   . SER   A 60  ? 0.2232 0.1900 0.1534 -0.0068 -0.0324 0.0071  66  SER   A N   
467  C CA  . SER   A 60  ? 0.2523 0.2058 0.1664 -0.0104 -0.0460 0.0110  66  SER   A CA  
468  C C   . SER   A 60  ? 0.2673 0.2062 0.1453 -0.0154 -0.0432 0.0099  66  SER   A C   
469  O O   . SER   A 60  ? 0.2861 0.2134 0.1467 -0.0202 -0.0520 0.0169  66  SER   A O   
470  C CB  . SER   A 60  ? 0.2912 0.2447 0.2162 -0.0092 -0.0569 0.0088  66  SER   A CB  
471  O OG  . SER   A 60  ? 0.3632 0.3163 0.2818 -0.0081 -0.0515 0.0004  66  SER   A OG  
472  N N   . SER   A 61  ? 0.2606 0.1995 0.1279 -0.0147 -0.0293 0.0018  67  SER   A N   
473  C CA  . SER   A 61  ? 0.2764 0.2003 0.1088 -0.0198 -0.0215 -0.0011 67  SER   A CA  
474  C C   . SER   A 61  ? 0.2962 0.2162 0.1156 -0.0235 -0.0153 0.0053  67  SER   A C   
475  O O   . SER   A 61  ? 0.3218 0.2268 0.1087 -0.0291 -0.0089 0.0042  67  SER   A O   
476  C CB  . SER   A 61  ? 0.2733 0.1997 0.1059 -0.0171 -0.0058 -0.0113 67  SER   A CB  
477  O OG  . SER   A 61  ? 0.2810 0.2237 0.1387 -0.0126 0.0068  -0.0118 67  SER   A OG  
478  N N   . ARG   A 62  ? 0.2724 0.2040 0.1154 -0.0210 -0.0161 0.0116  68  ARG   A N   
479  C CA  . ARG   A 62  ? 0.2857 0.2136 0.1201 -0.0245 -0.0116 0.0186  68  ARG   A CA  
480  C C   . ARG   A 62  ? 0.3100 0.2375 0.1572 -0.0249 -0.0263 0.0288  68  ARG   A C   
481  O O   . ARG   A 62  ? 0.3128 0.2361 0.1550 -0.0279 -0.0247 0.0359  68  ARG   A O   
482  C CB  . ARG   A 62  ? 0.2792 0.2219 0.1341 -0.0214 0.0042  0.0160  68  ARG   A CB  
483  C CG  . ARG   A 62  ? 0.3163 0.2602 0.1649 -0.0208 0.0202  0.0078  68  ARG   A CG  
484  C CD  . ARG   A 62  ? 0.3608 0.2893 0.1766 -0.0270 0.0303  0.0083  68  ARG   A CD  
485  N NE  . ARG   A 62  ? 0.3802 0.3106 0.1959 -0.0258 0.0485  -0.0003 68  ARG   A NE  
486  C CZ  . ARG   A 62  ? 0.4061 0.3248 0.2017 -0.0270 0.0534  -0.0082 68  ARG   A CZ  
487  N NH1 . ARG   A 62  ? 0.4009 0.3054 0.1731 -0.0300 0.0394  -0.0087 68  ARG   A NH1 
488  N NH2 . ARG   A 62  ? 0.3673 0.2882 0.1683 -0.0253 0.0722  -0.0159 68  ARG   A NH2 
489  N N   . ARG   A 63  ? 0.3146 0.2467 0.1821 -0.0218 -0.0391 0.0296  69  ARG   A N   
490  C CA  . ARG   A 63  ? 0.3197 0.2533 0.2087 -0.0208 -0.0510 0.0382  69  ARG   A CA  
491  C C   . ARG   A 63  ? 0.3184 0.2607 0.2259 -0.0191 -0.0409 0.0402  69  ARG   A C   
492  O O   . ARG   A 63  ? 0.3274 0.2642 0.2375 -0.0210 -0.0455 0.0488  69  ARG   A O   
493  C CB  . ARG   A 63  ? 0.3531 0.2702 0.2221 -0.0265 -0.0670 0.0484  69  ARG   A CB  
494  C CG  . ARG   A 63  ? 0.4232 0.3306 0.2761 -0.0294 -0.0809 0.0471  69  ARG   A CG  
495  C CD  . ARG   A 63  ? 0.4841 0.3747 0.3176 -0.0363 -0.0993 0.0592  69  ARG   A CD  
496  N NE  . ARG   A 63  ? 0.5586 0.4359 0.3668 -0.0418 -0.1133 0.0580  69  ARG   A NE  
497  C CZ  . ARG   A 63  ? 0.5973 0.4537 0.3635 -0.0512 -0.1226 0.0634  69  ARG   A CZ  
498  N NH1 . ARG   A 63  ? 0.5820 0.4289 0.3269 -0.0559 -0.1183 0.0708  69  ARG   A NH1 
499  N NH2 . ARG   A 63  ? 0.6111 0.4546 0.3535 -0.0571 -0.1357 0.0610  69  ARG   A NH2 
500  N N   . LYS   A 64  ? 0.2962 0.2507 0.2149 -0.0162 -0.0275 0.0327  70  LYS   A N   
501  C CA  . LYS   A 64  ? 0.2847 0.2467 0.2178 -0.0159 -0.0178 0.0334  70  LYS   A CA  
502  C C   . LYS   A 64  ? 0.2425 0.2183 0.1987 -0.0123 -0.0121 0.0266  70  LYS   A C   
503  O O   . LYS   A 64  ? 0.2355 0.2163 0.1922 -0.0101 -0.0109 0.0207  70  LYS   A O   
504  C CB  . LYS   A 64  ? 0.3328 0.2938 0.2486 -0.0190 -0.0051 0.0322  70  LYS   A CB  
505  C CG  . LYS   A 64  ? 0.4299 0.3781 0.3256 -0.0242 -0.0057 0.0403  70  LYS   A CG  
506  C CD  . LYS   A 64  ? 0.5137 0.4638 0.4002 -0.0268 0.0101  0.0383  70  LYS   A CD  
507  C CE  . LYS   A 64  ? 0.6044 0.5417 0.4714 -0.0327 0.0115  0.0469  70  LYS   A CE  
508  N NZ  . LYS   A 64  ? 0.6686 0.5884 0.5016 -0.0370 0.0043  0.0504  70  LYS   A NZ  
509  N N   . HIS   A 65  ? 0.2125 0.1929 0.1854 -0.0126 -0.0080 0.0275  71  HIS   A N   
510  C CA  . HIS   A 65  ? 0.1855 0.1768 0.1744 -0.0114 -0.0019 0.0215  71  HIS   A CA  
511  C C   . HIS   A 65  ? 0.1925 0.1890 0.1778 -0.0141 0.0078  0.0204  71  HIS   A C   
512  O O   . HIS   A 65  ? 0.2114 0.2030 0.1895 -0.0170 0.0108  0.0249  71  HIS   A O   
513  C CB  . HIS   A 65  ? 0.1741 0.1654 0.1825 -0.0112 -0.0024 0.0217  71  HIS   A CB  
514  C CG  . HIS   A 65  ? 0.1845 0.1719 0.2043 -0.0085 -0.0105 0.0234  71  HIS   A CG  
515  N ND1 . HIS   A 65  ? 0.2062 0.1986 0.2387 -0.0064 -0.0103 0.0185  71  HIS   A ND1 
516  C CD2 . HIS   A 65  ? 0.1921 0.1714 0.2140 -0.0079 -0.0196 0.0303  71  HIS   A CD2 
517  C CE1 . HIS   A 65  ? 0.1896 0.1776 0.2342 -0.0043 -0.0180 0.0220  71  HIS   A CE1 
518  N NE2 . HIS   A 65  ? 0.2042 0.1847 0.2436 -0.0051 -0.0250 0.0294  71  HIS   A NE2 
519  N N   . TYR   A 66  ? 0.1726 0.1787 0.1640 -0.0135 0.0119  0.0154  72  TYR   A N   
520  C CA  . TYR   A 66  ? 0.1732 0.1865 0.1676 -0.0161 0.0196  0.0147  72  TYR   A CA  
521  C C   . TYR   A 66  ? 0.1569 0.1783 0.1653 -0.0182 0.0201  0.0120  72  TYR   A C   
522  O O   . TYR   A 66  ? 0.1520 0.1770 0.1650 -0.0166 0.0170  0.0089  72  TYR   A O   
523  C CB  . TYR   A 66  ? 0.1759 0.1931 0.1651 -0.0142 0.0242  0.0124  72  TYR   A CB  
524  C CG  . TYR   A 66  ? 0.2044 0.2116 0.1738 -0.0142 0.0264  0.0140  72  TYR   A CG  
525  C CD1 . TYR   A 66  ? 0.2261 0.2288 0.1866 -0.0177 0.0334  0.0176  72  TYR   A CD1 
526  C CD2 . TYR   A 66  ? 0.2213 0.2220 0.1789 -0.0117 0.0216  0.0117  72  TYR   A CD2 
527  C CE1 . TYR   A 66  ? 0.2563 0.2472 0.1932 -0.0192 0.0362  0.0191  72  TYR   A CE1 
528  C CE2 . TYR   A 66  ? 0.2508 0.2397 0.1850 -0.0134 0.0235  0.0124  72  TYR   A CE2 
529  C CZ  . TYR   A 66  ? 0.2746 0.2578 0.1968 -0.0174 0.0307  0.0163  72  TYR   A CZ  
530  O OH  . TYR   A 66  ? 0.3113 0.2802 0.2053 -0.0206 0.0330  0.0173  72  TYR   A OH  
531  N N   . PRO   A 67  ? 0.1458 0.1691 0.1593 -0.0227 0.0238  0.0134  73  PRO   A N   
532  C CA  . PRO   A 67  ? 0.1434 0.1730 0.1665 -0.0268 0.0230  0.0110  73  PRO   A CA  
533  C C   . PRO   A 67  ? 0.1457 0.1863 0.1757 -0.0264 0.0236  0.0109  73  PRO   A C   
534  O O   . PRO   A 67  ? 0.1475 0.1915 0.1795 -0.0258 0.0287  0.0129  73  PRO   A O   
535  C CB  . PRO   A 67  ? 0.1499 0.1767 0.1757 -0.0323 0.0262  0.0130  73  PRO   A CB  
536  C CG  . PRO   A 67  ? 0.1544 0.1786 0.1746 -0.0310 0.0307  0.0174  73  PRO   A CG  
537  C CD  . PRO   A 67  ? 0.1404 0.1591 0.1498 -0.0254 0.0282  0.0178  73  PRO   A CD  
538  N N   . VAL   A 68  ? 0.1473 0.1926 0.1817 -0.0267 0.0190  0.0089  74  VAL   A N   
539  C CA  . VAL   A 68  ? 0.1409 0.1964 0.1860 -0.0259 0.0178  0.0100  74  VAL   A CA  
540  C C   . VAL   A 68  ? 0.1352 0.1954 0.1865 -0.0318 0.0113  0.0108  74  VAL   A C   
541  O O   . VAL   A 68  ? 0.1287 0.1826 0.1715 -0.0354 0.0082  0.0086  74  VAL   A O   
542  C CB  . VAL   A 68  ? 0.1468 0.2027 0.1906 -0.0194 0.0170  0.0083  74  VAL   A CB  
543  C CG1 . VAL   A 68  ? 0.1666 0.2190 0.2043 -0.0149 0.0235  0.0077  74  VAL   A CG1 
544  C CG2 . VAL   A 68  ? 0.1395 0.1889 0.1752 -0.0183 0.0125  0.0058  74  VAL   A CG2 
545  N N   . SER   A 69  ? 0.1308 0.2012 0.1973 -0.0332 0.0094  0.0141  75  SER   A N   
546  C CA  . SER   A 69  ? 0.1405 0.2160 0.2139 -0.0389 0.0001  0.0168  75  SER   A CA  
547  C C   . SER   A 69  ? 0.1249 0.2041 0.2041 -0.0329 -0.0025 0.0175  75  SER   A C   
548  O O   . SER   A 69  ? 0.1190 0.2013 0.2062 -0.0260 0.0036  0.0170  75  SER   A O   
549  C CB  . SER   A 69  ? 0.1503 0.2359 0.2431 -0.0435 -0.0020 0.0216  75  SER   A CB  
550  O OG  . SER   A 69  ? 0.2213 0.3025 0.3081 -0.0509 -0.0021 0.0209  75  SER   A OG  
551  N N   . PHE   A 70  ? 0.1258 0.2022 0.1984 -0.0358 -0.0102 0.0181  76  PHE   A N   
552  C CA  . PHE   A 70  ? 0.1209 0.1994 0.1991 -0.0304 -0.0128 0.0192  76  PHE   A CA  
553  C C   . PHE   A 70  ? 0.1388 0.2205 0.2221 -0.0361 -0.0243 0.0249  76  PHE   A C   
554  O O   . PHE   A 70  ? 0.1508 0.2283 0.2226 -0.0454 -0.0303 0.0260  76  PHE   A O   
555  C CB  . PHE   A 70  ? 0.1234 0.1928 0.1866 -0.0258 -0.0091 0.0141  76  PHE   A CB  
556  C CG  . PHE   A 70  ? 0.1360 0.1960 0.1817 -0.0316 -0.0101 0.0115  76  PHE   A CG  
557  C CD1 . PHE   A 70  ? 0.1489 0.2026 0.1861 -0.0330 -0.0045 0.0079  76  PHE   A CD1 
558  C CD2 . PHE   A 70  ? 0.1508 0.2072 0.1893 -0.0362 -0.0156 0.0128  76  PHE   A CD2 
559  C CE1 . PHE   A 70  ? 0.1699 0.2140 0.1941 -0.0381 -0.0031 0.0046  76  PHE   A CE1 
560  C CE2 . PHE   A 70  ? 0.1654 0.2114 0.1871 -0.0422 -0.0135 0.0093  76  PHE   A CE2 
561  C CZ  . PHE   A 70  ? 0.1682 0.2083 0.1843 -0.0428 -0.0065 0.0048  76  PHE   A CZ  
562  N N   . SER   A 71  ? 0.1332 0.2211 0.2332 -0.0314 -0.0278 0.0288  77  SER   A N   
563  C CA  . SER   A 71  ? 0.1378 0.2286 0.2449 -0.0368 -0.0407 0.0364  77  SER   A CA  
564  C C   . SER   A 71  ? 0.1553 0.2352 0.2387 -0.0413 -0.0451 0.0357  77  SER   A C   
565  O O   . SER   A 71  ? 0.1643 0.2368 0.2336 -0.0377 -0.0372 0.0293  77  SER   A O   
566  C CB  . SER   A 71  ? 0.1427 0.2427 0.2785 -0.0296 -0.0419 0.0410  77  SER   A CB  
567  O OG  . SER   A 71  ? 0.1693 0.2644 0.3013 -0.0217 -0.0359 0.0366  77  SER   A OG  
568  N N   . LYS   A 72  ? 0.1637 0.2420 0.2427 -0.0499 -0.0576 0.0427  78  LYS   A N   
569  C CA  . LYS   A 72  ? 0.1907 0.2573 0.2459 -0.0553 -0.0604 0.0426  78  LYS   A CA  
570  C C   . LYS   A 72  ? 0.1852 0.2524 0.2499 -0.0467 -0.0587 0.0435  78  LYS   A C   
571  O O   . LYS   A 72  ? 0.1784 0.2548 0.2689 -0.0392 -0.0598 0.0468  78  LYS   A O   
572  C CB  . LYS   A 72  ? 0.2387 0.3011 0.2822 -0.0686 -0.0754 0.0508  78  LYS   A CB  
573  C CG  . LYS   A 72  ? 0.2978 0.3546 0.3237 -0.0793 -0.0762 0.0476  78  LYS   A CG  
574  C CD  . LYS   A 72  ? 0.3662 0.4138 0.3705 -0.0950 -0.0910 0.0542  78  LYS   A CD  
575  C CE  . LYS   A 72  ? 0.4398 0.4793 0.4242 -0.1062 -0.0908 0.0493  78  LYS   A CE  
576  N NZ  . LYS   A 72  ? 0.4966 0.5277 0.4615 -0.1228 -0.1082 0.0568  78  LYS   A NZ  
577  N N   . PRO   A 73  ? 0.1914 0.2485 0.2376 -0.0475 -0.0545 0.0400  79  PRO   A N   
578  C CA  . PRO   A 73  ? 0.1920 0.2489 0.2476 -0.0400 -0.0530 0.0406  79  PRO   A CA  
579  C C   . PRO   A 73  ? 0.1897 0.2511 0.2620 -0.0404 -0.0649 0.0510  79  PRO   A C   
580  O O   . PRO   A 73  ? 0.1829 0.2407 0.2456 -0.0502 -0.0761 0.0590  79  PRO   A O   
581  C CB  . PRO   A 73  ? 0.2132 0.2579 0.2452 -0.0446 -0.0484 0.0371  79  PRO   A CB  
582  C CG  . PRO   A 73  ? 0.2316 0.2708 0.2457 -0.0503 -0.0419 0.0308  79  PRO   A CG  
583  C CD  . PRO   A 73  ? 0.2103 0.2550 0.2280 -0.0557 -0.0497 0.0350  79  PRO   A CD  
584  N N   . SER   A 74  ? 0.1885 0.2562 0.2853 -0.0302 -0.0627 0.0511  80  SER   A N   
585  C CA  . SER   A 74  ? 0.2017 0.2742 0.3215 -0.0288 -0.0730 0.0611  80  SER   A CA  
586  C C   . SER   A 74  ? 0.1978 0.2706 0.3361 -0.0179 -0.0670 0.0582  80  SER   A C   
587  O O   . SER   A 74  ? 0.1919 0.2611 0.3228 -0.0122 -0.0559 0.0483  80  SER   A O   
588  C CB  . SER   A 74  ? 0.2401 0.3241 0.3832 -0.0294 -0.0787 0.0666  80  SER   A CB  
589  O OG  . SER   A 74  ? 0.2927 0.3831 0.4491 -0.0214 -0.0664 0.0586  80  SER   A OG  
590  N N   . LEU   A 75  ? 0.1857 0.2618 0.3487 -0.0156 -0.0754 0.0673  81  LEU   A N   
591  C CA  . LEU   A 75  ? 0.1888 0.2641 0.3729 -0.0058 -0.0704 0.0651  81  LEU   A CA  
592  C C   . LEU   A 75  ? 0.1900 0.2741 0.4005 0.0025  -0.0615 0.0603  81  LEU   A C   
593  O O   . LEU   A 75  ? 0.1761 0.2695 0.4116 0.0020  -0.0673 0.0678  81  LEU   A O   
594  C CB  . LEU   A 75  ? 0.1881 0.2630 0.3911 -0.0073 -0.0835 0.0782  81  LEU   A CB  
595  C CG  . LEU   A 75  ? 0.2265 0.2907 0.4175 -0.0091 -0.0867 0.0810  81  LEU   A CG  
596  C CD1 . LEU   A 75  ? 0.2390 0.3041 0.4582 -0.0081 -0.0989 0.0945  81  LEU   A CD1 
597  C CD2 . LEU   A 75  ? 0.2334 0.2919 0.4201 -0.0014 -0.0733 0.0686  81  LEU   A CD2 
598  N N   . ILE   A 76  ? 0.1979 0.2784 0.4027 0.0093  -0.0475 0.0482  82  ILE   A N   
599  C CA  . ILE   A 76  ? 0.2107 0.2966 0.4342 0.0161  -0.0361 0.0423  82  ILE   A CA  
600  C C   . ILE   A 76  ? 0.2210 0.2999 0.4534 0.0245  -0.0262 0.0344  82  ILE   A C   
601  O O   . ILE   A 76  ? 0.2216 0.2909 0.4336 0.0248  -0.0244 0.0284  82  ILE   A O   
602  C CB  . ILE   A 76  ? 0.2340 0.3197 0.4342 0.0137  -0.0282 0.0346  82  ILE   A CB  
603  C CG1 . ILE   A 76  ? 0.2486 0.3410 0.4444 0.0053  -0.0370 0.0418  82  ILE   A CG1 
604  C CG2 . ILE   A 76  ? 0.2366 0.3231 0.4458 0.0202  -0.0131 0.0261  82  ILE   A CG2 
605  C CD1 . ILE   A 76  ? 0.2848 0.3742 0.4550 0.0018  -0.0323 0.0359  82  ILE   A CD1 
606  N N   . PHE   A 77  ? 0.2188 0.3018 0.4825 0.0309  -0.0188 0.0337  83  PHE   A N   
607  C CA  . PHE   A 77  ? 0.2432 0.3174 0.5144 0.0383  -0.0073 0.0245  83  PHE   A CA  
608  C C   . PHE   A 77  ? 0.2530 0.3183 0.4947 0.0393  0.0059  0.0106  83  PHE   A C   
609  O O   . PHE   A 77  ? 0.2566 0.3257 0.4905 0.0379  0.0126  0.0078  83  PHE   A O   
610  C CB  . PHE   A 77  ? 0.2424 0.3222 0.5564 0.0448  -0.0001 0.0264  83  PHE   A CB  
611  C CG  . PHE   A 77  ? 0.2687 0.3372 0.5928 0.0520  0.0118  0.0171  83  PHE   A CG  
612  C CD1 . PHE   A 77  ? 0.2825 0.3451 0.6171 0.0538  0.0042  0.0210  83  PHE   A CD1 
613  C CD2 . PHE   A 77  ? 0.2898 0.3523 0.6129 0.0563  0.0313  0.0044  83  PHE   A CD2 
614  C CE1 . PHE   A 77  ? 0.2943 0.3451 0.6393 0.0601  0.0154  0.0117  83  PHE   A CE1 
615  C CE2 . PHE   A 77  ? 0.2985 0.3481 0.6287 0.0619  0.0431  -0.0055 83  PHE   A CE2 
616  C CZ  . PHE   A 77  ? 0.2940 0.3379 0.6355 0.0639  0.0349  -0.0022 83  PHE   A CZ  
617  N N   . VAL   A 78  ? 0.2599 0.3128 0.4859 0.0411  0.0086  0.0028  84  VAL   A N   
618  C CA  . VAL   A 78  ? 0.2860 0.3285 0.4830 0.0410  0.0180  -0.0092 84  VAL   A CA  
619  C C   . VAL   A 78  ? 0.3093 0.3393 0.5118 0.0461  0.0290  -0.0192 84  VAL   A C   
620  O O   . VAL   A 78  ? 0.3045 0.3290 0.5163 0.0480  0.0244  -0.0187 84  VAL   A O   
621  C CB  . VAL   A 78  ? 0.2942 0.3319 0.4611 0.0360  0.0089  -0.0096 84  VAL   A CB  
622  C CG1 . VAL   A 78  ? 0.3082 0.3334 0.4485 0.0359  0.0155  -0.0209 84  VAL   A CG1 
623  C CG2 . VAL   A 78  ? 0.2914 0.3385 0.4494 0.0306  0.0021  -0.0026 84  VAL   A CG2 
624  N N   . GLU   A 79  ? 0.3328 0.3570 0.5276 0.0476  0.0441  -0.0287 85  GLU   A N   
625  C CA  . GLU   A 79  ? 0.3677 0.3767 0.5615 0.0512  0.0577  -0.0406 85  GLU   A CA  
626  C C   . GLU   A 79  ? 0.3960 0.3902 0.5656 0.0493  0.0516  -0.0472 85  GLU   A C   
627  O O   . GLU   A 79  ? 0.4068 0.4011 0.5529 0.0447  0.0406  -0.0449 85  GLU   A O   
628  C CB  . GLU   A 79  ? 0.4197 0.4223 0.5953 0.0501  0.0742  -0.0497 85  GLU   A CB  
629  C CG  . GLU   A 79  ? 0.5017 0.5110 0.7105 0.0545  0.0898  -0.0496 85  GLU   A CG  
630  C CD  . GLU   A 79  ? 0.6035 0.6007 0.8307 0.0598  0.1053  -0.0593 85  GLU   A CD  
631  O OE1 . GLU   A 79  ? 0.6323 0.6120 0.8371 0.0589  0.1061  -0.0688 85  GLU   A OE1 
632  O OE2 . GLU   A 79  ? 0.6330 0.6376 0.8988 0.0646  0.1168  -0.0574 85  GLU   A OE2 
633  N N   . ALA   A 80  ? 0.4064 0.3873 0.5831 0.0525  0.0594  -0.0557 86  ALA   A N   
634  C CA  . ALA   A 80  ? 0.4345 0.4001 0.5895 0.0500  0.0536  -0.0627 86  ALA   A CA  
635  C C   . ALA   A 80  ? 0.4610 0.4147 0.5731 0.0442  0.0547  -0.0712 86  ALA   A C   
636  O O   . ALA   A 80  ? 0.4727 0.4230 0.5706 0.0430  0.0667  -0.0764 86  ALA   A O   
637  C CB  . ALA   A 80  ? 0.4414 0.3930 0.6121 0.0541  0.0638  -0.0717 86  ALA   A CB  
638  N N   . SER   A 81  ? 0.4656 0.4135 0.5590 0.0400  0.0416  -0.0714 87  SER   A N   
639  C CA  . SER   A 81  ? 0.4849 0.4212 0.5405 0.0338  0.0368  -0.0772 87  SER   A CA  
640  C C   . SER   A 81  ? 0.5033 0.4258 0.5514 0.0313  0.0280  -0.0826 87  SER   A C   
641  O O   . SER   A 81  ? 0.5048 0.4289 0.5775 0.0345  0.0258  -0.0805 87  SER   A O   
642  C CB  . SER   A 81  ? 0.4863 0.4360 0.5345 0.0308  0.0252  -0.0673 87  SER   A CB  
643  O OG  . SER   A 81  ? 0.4758 0.4333 0.5375 0.0305  0.0119  -0.0597 87  SER   A OG  
644  N N   . GLU   A 82  ? 0.5184 0.4279 0.5344 0.0249  0.0213  -0.0881 88  GLU   A N   
645  C CA  . GLU   A 82  ? 0.5318 0.4289 0.5417 0.0213  0.0108  -0.0925 88  GLU   A CA  
646  C C   . GLU   A 82  ? 0.5098 0.4205 0.5400 0.0215  -0.0041 -0.0818 88  GLU   A C   
647  O O   . GLU   A 82  ? 0.5180 0.4210 0.5512 0.0192  -0.0124 -0.0840 88  GLU   A O   
648  C CB  . GLU   A 82  ? 0.5993 0.4777 0.5693 0.0132  0.0056  -0.1005 88  GLU   A CB  
649  C CG  . GLU   A 82  ? 0.6987 0.5850 0.6538 0.0091  -0.0062 -0.0925 88  GLU   A CG  
650  C CD  . GLU   A 82  ? 0.8422 0.7089 0.7578 0.0004  -0.0135 -0.0987 88  GLU   A CD  
651  O OE1 . GLU   A 82  ? 0.8631 0.7327 0.7734 -0.0039 -0.0301 -0.0923 88  GLU   A OE1 
652  O OE2 . GLU   A 82  ? 0.8895 0.7369 0.7795 -0.0027 -0.0026 -0.1098 88  GLU   A OE2 
653  N N   . TYR   A 83  ? 0.4831 0.4127 0.5268 0.0236  -0.0064 -0.0707 89  TYR   A N   
654  C CA  . TYR   A 83  ? 0.4552 0.3970 0.5156 0.0231  -0.0172 -0.0608 89  TYR   A CA  
655  C C   . TYR   A 83  ? 0.4228 0.3743 0.5122 0.0276  -0.0146 -0.0538 89  TYR   A C   
656  O O   . TYR   A 83  ? 0.4237 0.3781 0.5265 0.0266  -0.0216 -0.0484 89  TYR   A O   
657  C CB  . TYR   A 83  ? 0.4507 0.4042 0.5038 0.0211  -0.0215 -0.0536 89  TYR   A CB  
658  C CG  . TYR   A 83  ? 0.4672 0.4118 0.4938 0.0164  -0.0264 -0.0578 89  TYR   A CG  
659  C CD1 . TYR   A 83  ? 0.4813 0.4188 0.5025 0.0119  -0.0385 -0.0588 89  TYR   A CD1 
660  C CD2 . TYR   A 83  ? 0.4830 0.4262 0.4913 0.0159  -0.0200 -0.0595 89  TYR   A CD2 
661  C CE1 . TYR   A 83  ? 0.5023 0.4312 0.5002 0.0069  -0.0459 -0.0607 89  TYR   A CE1 
662  C CE2 . TYR   A 83  ? 0.5074 0.4409 0.4896 0.0107  -0.0259 -0.0617 89  TYR   A CE2 
663  C CZ  . TYR   A 83  ? 0.5291 0.4555 0.5061 0.0062  -0.0399 -0.0619 89  TYR   A CZ  
664  O OH  . TYR   A 83  ? 0.5740 0.4908 0.5263 0.0005  -0.0485 -0.0622 89  TYR   A OH  
665  N N   . TYR   A 84  ? 0.3958 0.3521 0.4959 0.0319  -0.0048 -0.0530 90  TYR   A N   
666  C CA  . TYR   A 84  ? 0.3737 0.3390 0.5022 0.0356  -0.0045 -0.0446 90  TYR   A CA  
667  C C   . TYR   A 84  ? 0.3875 0.3492 0.5323 0.0410  0.0071  -0.0489 90  TYR   A C   
668  O O   . TYR   A 84  ? 0.3964 0.3562 0.5319 0.0420  0.0172  -0.0549 90  TYR   A O   
669  C CB  . TYR   A 84  ? 0.3450 0.3269 0.4781 0.0349  -0.0072 -0.0338 90  TYR   A CB  
670  C CG  . TYR   A 84  ? 0.3275 0.3146 0.4485 0.0300  -0.0158 -0.0288 90  TYR   A CG  
671  C CD1 . TYR   A 84  ? 0.3282 0.3170 0.4300 0.0275  -0.0156 -0.0309 90  TYR   A CD1 
672  C CD2 . TYR   A 84  ? 0.3194 0.3095 0.4498 0.0277  -0.0228 -0.0214 90  TYR   A CD2 
673  C CE1 . TYR   A 84  ? 0.3245 0.3185 0.4202 0.0236  -0.0218 -0.0261 90  TYR   A CE1 
674  C CE2 . TYR   A 84  ? 0.3155 0.3098 0.4373 0.0233  -0.0276 -0.0176 90  TYR   A CE2 
675  C CZ  . TYR   A 84  ? 0.3163 0.3130 0.4226 0.0216  -0.0269 -0.0201 90  TYR   A CZ  
676  O OH  . TYR   A 84  ? 0.3052 0.3054 0.4071 0.0178  -0.0304 -0.0167 90  TYR   A OH  
677  N N   . PRO   A 85  ? 0.3869 0.3493 0.5594 0.0445  0.0064  -0.0441 91  PRO   A N   
678  C CA  . PRO   A 85  ? 0.3821 0.3444 0.5787 0.0505  0.0176  -0.0457 91  PRO   A CA  
679  C C   . PRO   A 85  ? 0.3731 0.3530 0.5822 0.0515  0.0175  -0.0356 91  PRO   A C   
680  O O   . PRO   A 85  ? 0.3786 0.3690 0.5772 0.0474  0.0082  -0.0274 91  PRO   A O   
681  C CB  . PRO   A 85  ? 0.3860 0.3446 0.6104 0.0533  0.0134  -0.0409 91  PRO   A CB  
682  C CG  . PRO   A 85  ? 0.3936 0.3579 0.6122 0.0485  -0.0012 -0.0308 91  PRO   A CG  
683  C CD  . PRO   A 85  ? 0.3803 0.3446 0.5660 0.0431  -0.0044 -0.0352 91  PRO   A CD  
684  N N   . ALA   A 86  ? 0.3539 0.3368 0.5869 0.0566  0.0281  -0.0363 92  ALA   A N   
685  C CA  . ALA   A 86  ? 0.3380 0.3376 0.5885 0.0574  0.0273  -0.0263 92  ALA   A CA  
686  C C   . ALA   A 86  ? 0.3276 0.3382 0.5934 0.0553  0.0109  -0.0103 92  ALA   A C   
687  O O   . ALA   A 86  ? 0.3301 0.3374 0.6171 0.0574  0.0059  -0.0052 92  ALA   A O   
688  C CB  . ALA   A 86  ? 0.3279 0.3281 0.6111 0.0639  0.0414  -0.0292 92  ALA   A CB  
689  N N   . ARG   A 87  ? 0.3180 0.3391 0.5695 0.0501  0.0025  -0.0028 93  ARG   A N   
690  C CA  . ARG   A 87  ? 0.3020 0.3304 0.5583 0.0457  -0.0126 0.0113  93  ARG   A CA  
691  C C   . ARG   A 87  ? 0.2940 0.3350 0.5434 0.0409  -0.0181 0.0190  93  ARG   A C   
692  O O   . ARG   A 87  ? 0.2993 0.3436 0.5387 0.0409  -0.0103 0.0131  93  ARG   A O   
693  C CB  . ARG   A 87  ? 0.3133 0.3334 0.5449 0.0414  -0.0185 0.0094  93  ARG   A CB  
694  C CG  . ARG   A 87  ? 0.3262 0.3481 0.5261 0.0363  -0.0186 0.0055  93  ARG   A CG  
695  C CD  . ARG   A 87  ? 0.3347 0.3467 0.5144 0.0345  -0.0188 -0.0021 93  ARG   A CD  
696  N NE  . ARG   A 87  ? 0.3184 0.3337 0.4771 0.0287  -0.0232 0.0001  93  ARG   A NE  
697  C CZ  . ARG   A 87  ? 0.2973 0.3153 0.4394 0.0273  -0.0199 -0.0041 93  ARG   A CZ  
698  N NH1 . ARG   A 87  ? 0.2748 0.2947 0.4020 0.0226  -0.0232 -0.0023 93  ARG   A NH1 
699  N NH2 . ARG   A 87  ? 0.2740 0.2919 0.4151 0.0305  -0.0122 -0.0101 93  ARG   A NH2 
700  N N   . TYR   A 88  ? 0.2785 0.3248 0.5300 0.0355  -0.0315 0.0320  94  TYR   A N   
701  C CA  . TYR   A 88  ? 0.2785 0.3335 0.5175 0.0291  -0.0376 0.0381  94  TYR   A CA  
702  C C   . TYR   A 88  ? 0.2599 0.3094 0.4642 0.0234  -0.0388 0.0343  94  TYR   A C   
703  O O   . TYR   A 88  ? 0.2759 0.3184 0.4732 0.0213  -0.0429 0.0362  94  TYR   A O   
704  C CB  . TYR   A 88  ? 0.2899 0.3511 0.5453 0.0246  -0.0520 0.0539  94  TYR   A CB  
705  C CG  . TYR   A 88  ? 0.3087 0.3784 0.6034 0.0297  -0.0521 0.0594  94  TYR   A CG  
706  C CD1 . TYR   A 88  ? 0.3248 0.4050 0.6283 0.0291  -0.0496 0.0599  94  TYR   A CD1 
707  C CD2 . TYR   A 88  ? 0.3207 0.3878 0.6472 0.0354  -0.0534 0.0638  94  TYR   A CD2 
708  C CE1 . TYR   A 88  ? 0.3272 0.4163 0.6723 0.0339  -0.0488 0.0653  94  TYR   A CE1 
709  C CE2 . TYR   A 88  ? 0.3225 0.3979 0.6912 0.0407  -0.0526 0.0691  94  TYR   A CE2 
710  C CZ  . TYR   A 88  ? 0.3355 0.4224 0.7144 0.0400  -0.0500 0.0698  94  TYR   A CZ  
711  O OH  . TYR   A 88  ? 0.3545 0.4507 0.7804 0.0453  -0.0484 0.0754  94  TYR   A OH  
712  N N   . GLN   A 89  ? 0.2235 0.2756 0.4091 0.0212  -0.0340 0.0288  95  GLN   A N   
713  C CA  . GLN   A 89  ? 0.1893 0.2372 0.3469 0.0160  -0.0344 0.0257  95  GLN   A CA  
714  C C   . GLN   A 89  ? 0.1575 0.2104 0.3063 0.0080  -0.0420 0.0343  95  GLN   A C   
715  O O   . GLN   A 89  ? 0.1424 0.2030 0.2995 0.0070  -0.0434 0.0376  95  GLN   A O   
716  C CB  . GLN   A 89  ? 0.2005 0.2465 0.3435 0.0183  -0.0253 0.0149  95  GLN   A CB  
717  C CG  . GLN   A 89  ? 0.2203 0.2634 0.3399 0.0132  -0.0259 0.0127  95  GLN   A CG  
718  C CD  . GLN   A 89  ? 0.2341 0.2720 0.3413 0.0158  -0.0200 0.0032  95  GLN   A CD  
719  O OE1 . GLN   A 89  ? 0.2392 0.2714 0.3492 0.0202  -0.0167 -0.0027 95  GLN   A OE1 
720  N NE2 . GLN   A 89  ? 0.2156 0.2538 0.3082 0.0125  -0.0192 0.0019  95  GLN   A NE2 
721  N N   . SER   A 90  ? 0.1332 0.1808 0.2659 0.0015  -0.0464 0.0379  96  SER   A N   
722  C CA  . SER   A 90  ? 0.1274 0.1757 0.2455 -0.0079 -0.0526 0.0448  96  SER   A CA  
723  C C   . SER   A 90  ? 0.1254 0.1719 0.2214 -0.0116 -0.0461 0.0378  96  SER   A C   
724  O O   . SER   A 90  ? 0.1219 0.1655 0.2133 -0.0075 -0.0385 0.0293  96  SER   A O   
725  C CB  . SER   A 90  ? 0.1607 0.2019 0.2711 -0.0144 -0.0595 0.0530  96  SER   A CB  
726  O OG  . SER   A 90  ? 0.2063 0.2401 0.3062 -0.0139 -0.0529 0.0470  96  SER   A OG  
727  N N   . HIS   A 91  ? 0.1195 0.1668 0.2029 -0.0198 -0.0500 0.0418  97  HIS   A N   
728  C CA  . HIS   A 91  ? 0.1253 0.1696 0.1889 -0.0245 -0.0441 0.0361  97  HIS   A CA  
729  C C   . HIS   A 91  ? 0.1241 0.1736 0.1941 -0.0176 -0.0368 0.0284  97  HIS   A C   
730  O O   . HIS   A 91  ? 0.1264 0.1722 0.1857 -0.0174 -0.0300 0.0219  97  HIS   A O   
731  C CB  . HIS   A 91  ? 0.1356 0.1704 0.1841 -0.0275 -0.0383 0.0326  97  HIS   A CB  
732  C CG  . HIS   A 91  ? 0.1858 0.2134 0.2232 -0.0357 -0.0435 0.0401  97  HIS   A CG  
733  N ND1 . HIS   A 91  ? 0.2104 0.2308 0.2244 -0.0470 -0.0440 0.0421  97  HIS   A ND1 
734  C CD2 . HIS   A 91  ? 0.1864 0.2119 0.2318 -0.0351 -0.0490 0.0466  97  HIS   A CD2 
735  C CE1 . HIS   A 91  ? 0.2137 0.2271 0.2195 -0.0533 -0.0493 0.0499  97  HIS   A CE1 
736  N NE2 . HIS   A 91  ? 0.2068 0.2235 0.2322 -0.0462 -0.0531 0.0535  97  HIS   A NE2 
737  N N   . LEU   A 92  ? 0.1069 0.1640 0.1950 -0.0122 -0.0377 0.0295  98  LEU   A N   
738  C CA  . LEU   A 92  ? 0.1219 0.1820 0.2136 -0.0064 -0.0299 0.0226  98  LEU   A CA  
739  C C   . LEU   A 92  ? 0.1212 0.1875 0.2141 -0.0101 -0.0303 0.0246  98  LEU   A C   
740  O O   . LEU   A 92  ? 0.1294 0.2010 0.2329 -0.0137 -0.0378 0.0319  98  LEU   A O   
741  C CB  . LEU   A 92  ? 0.1131 0.1753 0.2238 0.0020  -0.0271 0.0210  98  LEU   A CB  
742  C CG  . LEU   A 92  ? 0.1377 0.1999 0.2486 0.0074  -0.0177 0.0135  98  LEU   A CG  
743  C CD1 . LEU   A 92  ? 0.1508 0.2051 0.2430 0.0080  -0.0140 0.0067  98  LEU   A CD1 
744  C CD2 . LEU   A 92  ? 0.1529 0.2157 0.2828 0.0143  -0.0133 0.0116  98  LEU   A CD2 
745  N N   . MET   A 93  ? 0.1087 0.1739 0.1920 -0.0098 -0.0236 0.0190  99  MET   A N   
746  C CA  . MET   A 93  ? 0.1070 0.1772 0.1911 -0.0137 -0.0231 0.0203  99  MET   A CA  
747  C C   . MET   A 93  ? 0.1054 0.1787 0.1970 -0.0078 -0.0146 0.0164  99  MET   A C   
748  O O   . MET   A 93  ? 0.1327 0.2002 0.2150 -0.0037 -0.0089 0.0108  99  MET   A O   
749  C CB  . MET   A 93  ? 0.1119 0.1758 0.1761 -0.0203 -0.0218 0.0178  99  MET   A CB  
750  C CG  . MET   A 93  ? 0.1458 0.2032 0.1972 -0.0271 -0.0269 0.0200  99  MET   A CG  
751  S SD  . MET   A 93  ? 0.2154 0.2626 0.2454 -0.0334 -0.0208 0.0144  99  MET   A SD  
752  C CE  . MET   A 93  ? 0.2178 0.2612 0.2496 -0.0250 -0.0133 0.0084  99  MET   A CE  
753  N N   . LEU   A 94  ? 0.0882 0.1699 0.1969 -0.0077 -0.0137 0.0196  100 LEU   A N   
754  C CA  . LEU   A 94  ? 0.0900 0.1733 0.2045 -0.0027 -0.0032 0.0157  100 LEU   A CA  
755  C C   . LEU   A 94  ? 0.0961 0.1813 0.2057 -0.0072 -0.0001 0.0159  100 LEU   A C   
756  O O   . LEU   A 94  ? 0.0782 0.1679 0.1920 -0.0137 -0.0066 0.0205  100 LEU   A O   
757  C CB  . LEU   A 94  ? 0.0854 0.1765 0.2281 0.0019  0.0000  0.0181  100 LEU   A CB  
758  C CG  . LEU   A 94  ? 0.1272 0.2157 0.2798 0.0078  -0.0002 0.0170  100 LEU   A CG  
759  C CD1 . LEU   A 94  ? 0.1375 0.2327 0.3203 0.0128  0.0068  0.0180  100 LEU   A CD1 
760  C CD2 . LEU   A 94  ? 0.1504 0.2274 0.2818 0.0115  0.0056  0.0088  100 LEU   A CD2 
761  N N   . ALA   A 95  ? 0.0989 0.1799 0.2001 -0.0042 0.0098  0.0113  101 ALA   A N   
762  C CA  . ALA   A 95  ? 0.0982 0.1795 0.1949 -0.0075 0.0151  0.0114  101 ALA   A CA  
763  C C   . ALA   A 95  ? 0.1030 0.1830 0.2021 -0.0032 0.0276  0.0084  101 ALA   A C   
764  O O   . ALA   A 95  ? 0.1108 0.1858 0.2065 0.0018  0.0321  0.0043  101 ALA   A O   
765  C CB  . ALA   A 95  ? 0.1094 0.1813 0.1834 -0.0098 0.0137  0.0089  101 ALA   A CB  
766  N N   . VAL   A 96  ? 0.1027 0.1858 0.2063 -0.0060 0.0340  0.0100  102 VAL   A N   
767  C CA  . VAL   A 96  ? 0.1167 0.1964 0.2182 -0.0035 0.0481  0.0071  102 VAL   A CA  
768  C C   . VAL   A 96  ? 0.1433 0.2097 0.2139 -0.0045 0.0492  0.0043  102 VAL   A C   
769  O O   . VAL   A 96  ? 0.1585 0.2232 0.2209 -0.0086 0.0446  0.0068  102 VAL   A O   
770  C CB  . VAL   A 96  ? 0.1183 0.2072 0.2395 -0.0070 0.0547  0.0110  102 VAL   A CB  
771  C CG1 . VAL   A 96  ? 0.1297 0.2129 0.2448 -0.0056 0.0720  0.0078  102 VAL   A CG1 
772  C CG2 . VAL   A 96  ? 0.1105 0.2135 0.2668 -0.0064 0.0504  0.0154  102 VAL   A CG2 
773  N N   . GLY   A 97  ? 0.1557 0.2120 0.2103 -0.0011 0.0544  -0.0004 103 GLY   A N   
774  C CA  . GLY   A 97  ? 0.1802 0.2232 0.2062 -0.0025 0.0531  -0.0017 103 GLY   A CA  
775  C C   . GLY   A 97  ? 0.1969 0.2279 0.2045 0.0002  0.0554  -0.0072 103 GLY   A C   
776  O O   . GLY   A 97  ? 0.1936 0.2262 0.2110 0.0039  0.0580  -0.0110 103 GLY   A O   
777  N N   . HIS   A 98  ? 0.2165 0.2344 0.1974 -0.0022 0.0535  -0.0072 104 HIS   A N   
778  C CA  . HIS   A 98  ? 0.2379 0.2415 0.1955 -0.0018 0.0535  -0.0120 104 HIS   A CA  
779  C C   . HIS   A 98  ? 0.2367 0.2386 0.1944 0.0005  0.0404  -0.0134 104 HIS   A C   
780  O O   . HIS   A 98  ? 0.2177 0.2222 0.1790 -0.0001 0.0298  -0.0095 104 HIS   A O   
781  C CB  . HIS   A 98  ? 0.2598 0.2487 0.1874 -0.0066 0.0549  -0.0099 104 HIS   A CB  
782  C CG  . HIS   A 98  ? 0.3092 0.2811 0.2087 -0.0081 0.0555  -0.0152 104 HIS   A CG  
783  N ND1 . HIS   A 98  ? 0.3342 0.3003 0.2281 -0.0075 0.0700  -0.0225 104 HIS   A ND1 
784  C CD2 . HIS   A 98  ? 0.3415 0.3009 0.2190 -0.0104 0.0428  -0.0143 104 HIS   A CD2 
785  C CE1 . HIS   A 98  ? 0.3587 0.3072 0.2227 -0.0103 0.0660  -0.0267 104 HIS   A CE1 
786  N NE2 . HIS   A 98  ? 0.3693 0.3137 0.2230 -0.0123 0.0485  -0.0214 104 HIS   A NE2 
787  N N   . SER   A 99  ? 0.2550 0.2513 0.2092 0.0029  0.0423  -0.0195 105 SER   A N   
788  C CA  . SER   A 99  ? 0.2688 0.2628 0.2243 0.0049  0.0311  -0.0215 105 SER   A CA  
789  C C   . SER   A 99  ? 0.3060 0.2861 0.2443 0.0049  0.0355  -0.0292 105 SER   A C   
790  O O   . SER   A 99  ? 0.3262 0.3052 0.2681 0.0064  0.0487  -0.0340 105 SER   A O   
791  C CB  . SER   A 99  ? 0.2681 0.2760 0.2521 0.0085  0.0285  -0.0203 105 SER   A CB  
792  O OG  . SER   A 99  ? 0.3271 0.3332 0.3141 0.0100  0.0188  -0.0216 105 SER   A OG  
793  N N   . GLU   A 100 ? 0.3104 0.2787 0.2299 0.0026  0.0247  -0.0303 106 GLU   A N   
794  C CA  . GLU   A 100 ? 0.3317 0.2841 0.2311 0.0010  0.0249  -0.0378 106 GLU   A CA  
795  C C   . GLU   A 100 ? 0.3365 0.2909 0.2479 0.0029  0.0112  -0.0380 106 GLU   A C   
796  O O   . GLU   A 100 ? 0.3318 0.2966 0.2593 0.0040  0.0018  -0.0318 106 GLU   A O   
797  C CB  . GLU   A 100 ? 0.3770 0.3113 0.2389 -0.0058 0.0221  -0.0376 106 GLU   A CB  
798  C CG  . GLU   A 100 ? 0.4402 0.3686 0.2864 -0.0084 0.0392  -0.0393 106 GLU   A CG  
799  C CD  . GLU   A 100 ? 0.5372 0.4468 0.3434 -0.0165 0.0360  -0.0371 106 GLU   A CD  
800  O OE1 . GLU   A 100 ? 0.5865 0.4809 0.3691 -0.0208 0.0239  -0.0388 106 GLU   A OE1 
801  O OE2 . GLU   A 100 ? 0.5580 0.4670 0.3558 -0.0191 0.0447  -0.0330 106 GLU   A OE2 
802  N N   . PRO   A 101 ? 0.3463 0.2907 0.2517 0.0031  0.0109  -0.0454 107 PRO   A N   
803  C CA  . PRO   A 101 ? 0.3408 0.2883 0.2614 0.0047  -0.0013 -0.0451 107 PRO   A CA  
804  C C   . PRO   A 101 ? 0.3319 0.2815 0.2541 0.0023  -0.0174 -0.0382 107 PRO   A C   
805  O O   . PRO   A 101 ? 0.3348 0.2957 0.2808 0.0049  -0.0229 -0.0343 107 PRO   A O   
806  C CB  . PRO   A 101 ? 0.3666 0.2969 0.2702 0.0028  -0.0001 -0.0546 107 PRO   A CB  
807  C CG  . PRO   A 101 ? 0.3809 0.3041 0.2725 0.0028  0.0179  -0.0610 107 PRO   A CG  
808  C CD  . PRO   A 101 ? 0.3574 0.2868 0.2439 0.0017  0.0235  -0.0550 107 PRO   A CD  
809  N N   . GLY   A 102 ? 0.3246 0.2630 0.2226 -0.0029 -0.0242 -0.0360 108 GLY   A N   
810  C CA  . GLY   A 102 ? 0.3145 0.2538 0.2164 -0.0052 -0.0399 -0.0286 108 GLY   A CA  
811  C C   . GLY   A 102 ? 0.2924 0.2463 0.2150 -0.0026 -0.0390 -0.0210 108 GLY   A C   
812  O O   . GLY   A 102 ? 0.2930 0.2497 0.2275 -0.0033 -0.0498 -0.0151 108 GLY   A O   
813  N N   . ASP   A 103 ? 0.2678 0.2306 0.1968 0.0000  -0.0259 -0.0212 109 ASP   A N   
814  C CA  . ASP   A 103 ? 0.2347 0.2101 0.1817 0.0016  -0.0236 -0.0155 109 ASP   A CA  
815  C C   . ASP   A 103 ? 0.2000 0.1869 0.1731 0.0047  -0.0249 -0.0151 109 ASP   A C   
816  O O   . ASP   A 103 ? 0.1796 0.1741 0.1660 0.0049  -0.0250 -0.0109 109 ASP   A O   
817  C CB  . ASP   A 103 ? 0.2407 0.2208 0.1850 0.0020  -0.0105 -0.0156 109 ASP   A CB  
818  C CG  . ASP   A 103 ? 0.2674 0.2367 0.1869 -0.0021 -0.0086 -0.0137 109 ASP   A CG  
819  O OD1 . ASP   A 103 ? 0.2715 0.2336 0.1818 -0.0050 -0.0192 -0.0090 109 ASP   A OD1 
820  O OD2 . ASP   A 103 ? 0.2734 0.2407 0.1833 -0.0027 0.0036  -0.0165 109 ASP   A OD2 
821  N N   . CYS   A 104 ? 0.1966 0.1833 0.1761 0.0065  -0.0254 -0.0194 110 CYS   A N   
822  C CA  . CYS   A 104 ? 0.1838 0.1800 0.1858 0.0085  -0.0265 -0.0180 110 CYS   A CA  
823  C C   . CYS   A 104 ? 0.1670 0.1645 0.1797 0.0072  -0.0342 -0.0139 110 CYS   A C   
824  O O   . CYS   A 104 ? 0.1820 0.1721 0.1889 0.0054  -0.0430 -0.0129 110 CYS   A O   
825  C CB  . CYS   A 104 ? 0.1883 0.1820 0.1952 0.0101  -0.0271 -0.0224 110 CYS   A CB  
826  S SG  . CYS   A 104 ? 0.2282 0.2232 0.2350 0.0130  -0.0158 -0.0266 110 CYS   A SG  
827  N N   . GLY   A 105 ? 0.1442 0.1501 0.1718 0.0073  -0.0305 -0.0112 111 GLY   A N   
828  C CA  . GLY   A 105 ? 0.1522 0.1593 0.1936 0.0064  -0.0342 -0.0080 111 GLY   A CA  
829  C C   . GLY   A 105 ? 0.1647 0.1728 0.2056 0.0053  -0.0315 -0.0047 111 GLY   A C   
830  O O   . GLY   A 105 ? 0.1720 0.1816 0.2275 0.0047  -0.0310 -0.0026 111 GLY   A O   
831  N N   . GLY   A 106 ? 0.1629 0.1695 0.1888 0.0048  -0.0285 -0.0045 112 GLY   A N   
832  C CA  . GLY   A 106 ? 0.1507 0.1581 0.1764 0.0035  -0.0251 -0.0013 112 GLY   A CA  
833  C C   . GLY   A 106 ? 0.1413 0.1554 0.1771 0.0024  -0.0173 -0.0021 112 GLY   A C   
834  O O   . GLY   A 106 ? 0.1289 0.1478 0.1637 0.0023  -0.0136 -0.0041 112 GLY   A O   
835  N N   . ILE   A 107 ? 0.1293 0.1427 0.1752 0.0012  -0.0153 -0.0005 113 ILE   A N   
836  C CA  . ILE   A 107 ? 0.1362 0.1527 0.1875 -0.0015 -0.0075 -0.0022 113 ILE   A CA  
837  C C   . ILE   A 107 ? 0.1346 0.1531 0.1765 -0.0042 -0.0027 -0.0021 113 ILE   A C   
838  O O   . ILE   A 107 ? 0.1374 0.1537 0.1744 -0.0041 -0.0032 0.0001  113 ILE   A O   
839  C CB  . ILE   A 107 ? 0.1491 0.1622 0.2166 -0.0019 -0.0051 -0.0020 113 ILE   A CB  
840  C CG1 . ILE   A 107 ? 0.1584 0.1718 0.2391 -0.0003 -0.0079 -0.0025 113 ILE   A CG1 
841  C CG2 . ILE   A 107 ? 0.1664 0.1784 0.2343 -0.0061 0.0049  -0.0045 113 ILE   A CG2 
842  C CD1 . ILE   A 107 ? 0.1690 0.1798 0.2726 0.0001  -0.0051 -0.0019 113 ILE   A CD1 
843  N N   . LEU   A 108 ? 0.1299 0.1521 0.1694 -0.0073 0.0012  -0.0037 114 LEU   A N   
844  C CA  . LEU   A 108 ? 0.1299 0.1543 0.1635 -0.0113 0.0045  -0.0034 114 LEU   A CA  
845  C C   . LEU   A 108 ? 0.1473 0.1667 0.1824 -0.0163 0.0101  -0.0057 114 LEU   A C   
846  O O   . LEU   A 108 ? 0.1425 0.1599 0.1791 -0.0180 0.0123  -0.0076 114 LEU   A O   
847  C CB  . LEU   A 108 ? 0.1276 0.1584 0.1585 -0.0126 0.0028  -0.0027 114 LEU   A CB  
848  C CG  . LEU   A 108 ? 0.1504 0.1842 0.1780 -0.0182 0.0040  -0.0016 114 LEU   A CG  
849  C CD1 . LEU   A 108 ? 0.1581 0.1932 0.1854 -0.0179 0.0059  -0.0003 114 LEU   A CD1 
850  C CD2 . LEU   A 108 ? 0.1701 0.2107 0.2001 -0.0193 -0.0001 0.0008  114 LEU   A CD2 
851  N N   . ARG   A 109 ? 0.1550 0.1708 0.1896 -0.0187 0.0136  -0.0059 115 ARG   A N   
852  C CA  . ARG   A 109 ? 0.1870 0.1954 0.2224 -0.0236 0.0208  -0.0095 115 ARG   A CA  
853  C C   . ARG   A 109 ? 0.2059 0.2131 0.2316 -0.0305 0.0228  -0.0106 115 ARG   A C   
854  O O   . ARG   A 109 ? 0.2075 0.2185 0.2321 -0.0301 0.0201  -0.0077 115 ARG   A O   
855  C CB  . ARG   A 109 ? 0.2149 0.2176 0.2625 -0.0206 0.0233  -0.0090 115 ARG   A CB  
856  C CG  . ARG   A 109 ? 0.2796 0.2819 0.3411 -0.0152 0.0208  -0.0077 115 ARG   A CG  
857  C CD  . ARG   A 109 ? 0.3111 0.3070 0.3888 -0.0133 0.0233  -0.0065 115 ARG   A CD  
858  N NE  . ARG   A 109 ? 0.3628 0.3518 0.4471 -0.0171 0.0350  -0.0122 115 ARG   A NE  
859  C CZ  . ARG   A 109 ? 0.3861 0.3728 0.4845 -0.0163 0.0408  -0.0148 115 ARG   A CZ  
860  N NH1 . ARG   A 109 ? 0.3728 0.3511 0.4738 -0.0208 0.0543  -0.0211 115 ARG   A NH1 
861  N NH2 . ARG   A 109 ? 0.3918 0.3836 0.5015 -0.0116 0.0340  -0.0116 115 ARG   A NH2 
862  N N   . CYS   A 110 ? 0.2154 0.2157 0.2336 -0.0376 0.0283  -0.0149 116 CYS   A N   
863  C CA  . CYS   A 110 ? 0.2320 0.2282 0.2397 -0.0459 0.0297  -0.0167 116 CYS   A CA  
864  C C   . CYS   A 110 ? 0.2498 0.2329 0.2587 -0.0494 0.0403  -0.0227 116 CYS   A C   
865  O O   . CYS   A 110 ? 0.2446 0.2239 0.2660 -0.0445 0.0459  -0.0243 116 CYS   A O   
866  C CB  . CYS   A 110 ? 0.2408 0.2381 0.2340 -0.0534 0.0253  -0.0165 116 CYS   A CB  
867  S SG  . CYS   A 110 ? 0.2299 0.2160 0.2109 -0.0592 0.0325  -0.0215 116 CYS   A SG  
868  N N   . GLN   A 111 ? 0.2792 0.2545 0.2769 -0.0583 0.0433  -0.0264 117 GLN   A N   
869  C CA  . GLN   A 111 ? 0.3045 0.2650 0.3027 -0.0623 0.0554  -0.0337 117 GLN   A CA  
870  C C   . GLN   A 111 ? 0.3146 0.2660 0.3090 -0.0644 0.0656  -0.0395 117 GLN   A C   
871  O O   . GLN   A 111 ? 0.3258 0.2671 0.3312 -0.0634 0.0776  -0.0448 117 GLN   A O   
872  C CB  . GLN   A 111 ? 0.3511 0.3033 0.3338 -0.0732 0.0560  -0.0374 117 GLN   A CB  
873  C CG  . GLN   A 111 ? 0.4098 0.3590 0.3681 -0.0841 0.0516  -0.0391 117 GLN   A CG  
874  C CD  . GLN   A 111 ? 0.4784 0.4196 0.4217 -0.0958 0.0494  -0.0421 117 GLN   A CD  
875  O OE1 . GLN   A 111 ? 0.4965 0.4471 0.4375 -0.0991 0.0373  -0.0365 117 GLN   A OE1 
876  N NE2 . GLN   A 111 ? 0.4777 0.4009 0.4128 -0.1025 0.0614  -0.0513 117 GLN   A NE2 
877  N N   . HIS   A 112 ? 0.2975 0.2527 0.2798 -0.0668 0.0613  -0.0380 118 HIS   A N   
878  C CA  . HIS   A 112 ? 0.2888 0.2350 0.2653 -0.0699 0.0715  -0.0428 118 HIS   A CA  
879  C C   . HIS   A 112 ? 0.2673 0.2206 0.2656 -0.0599 0.0729  -0.0401 118 HIS   A C   
880  O O   . HIS   A 112 ? 0.2800 0.2257 0.2798 -0.0617 0.0840  -0.0444 118 HIS   A O   
881  C CB  . HIS   A 112 ? 0.2994 0.2427 0.2485 -0.0799 0.0666  -0.0422 118 HIS   A CB  
882  C CG  . HIS   A 112 ? 0.3339 0.2703 0.2606 -0.0913 0.0621  -0.0439 118 HIS   A CG  
883  N ND1 . HIS   A 112 ? 0.3395 0.2874 0.2636 -0.0922 0.0463  -0.0366 118 HIS   A ND1 
884  C CD2 . HIS   A 112 ? 0.3669 0.2854 0.2743 -0.1025 0.0715  -0.0522 118 HIS   A CD2 
885  C CE1 . HIS   A 112 ? 0.3629 0.3009 0.2675 -0.1042 0.0446  -0.0398 118 HIS   A CE1 
886  N NE2 . HIS   A 112 ? 0.3825 0.3019 0.2743 -0.1111 0.0594  -0.0496 118 HIS   A NE2 
887  N N   . GLY   A 113 ? 0.2321 0.1988 0.2462 -0.0504 0.0620  -0.0332 119 GLY   A N   
888  C CA  . GLY   A 113 ? 0.2034 0.1762 0.2370 -0.0419 0.0607  -0.0303 119 GLY   A CA  
889  C C   . GLY   A 113 ? 0.1677 0.1533 0.2013 -0.0365 0.0470  -0.0236 119 GLY   A C   
890  O O   . GLY   A 113 ? 0.1676 0.1593 0.1938 -0.0364 0.0387  -0.0203 119 GLY   A O   
891  N N   . VAL   A 114 ? 0.1489 0.1381 0.1928 -0.0322 0.0455  -0.0220 120 VAL   A N   
892  C CA  . VAL   A 114 ? 0.1426 0.1417 0.1877 -0.0270 0.0342  -0.0170 120 VAL   A CA  
893  C C   . VAL   A 114 ? 0.1466 0.1482 0.1743 -0.0318 0.0298  -0.0154 120 VAL   A C   
894  O O   . VAL   A 114 ? 0.1644 0.1606 0.1829 -0.0376 0.0346  -0.0170 120 VAL   A O   
895  C CB  . VAL   A 114 ? 0.1467 0.1475 0.2097 -0.0218 0.0337  -0.0161 120 VAL   A CB  
896  C CG1 . VAL   A 114 ? 0.1475 0.1561 0.2093 -0.0175 0.0226  -0.0122 120 VAL   A CG1 
897  C CG2 . VAL   A 114 ? 0.1502 0.1497 0.2344 -0.0166 0.0340  -0.0153 120 VAL   A CG2 
898  N N   . VAL   A 115 ? 0.1290 0.1381 0.1531 -0.0297 0.0211  -0.0118 121 VAL   A N   
899  C CA  . VAL   A 115 ? 0.1291 0.1422 0.1430 -0.0332 0.0149  -0.0087 121 VAL   A CA  
900  C C   . VAL   A 115 ? 0.1235 0.1424 0.1451 -0.0274 0.0091  -0.0057 121 VAL   A C   
901  O O   . VAL   A 115 ? 0.1163 0.1352 0.1329 -0.0305 0.0063  -0.0033 121 VAL   A O   
902  C CB  . VAL   A 115 ? 0.1322 0.1508 0.1436 -0.0340 0.0101  -0.0064 121 VAL   A CB  
903  C CG1 . VAL   A 115 ? 0.1437 0.1683 0.1515 -0.0367 0.0023  -0.0018 121 VAL   A CG1 
904  C CG2 . VAL   A 115 ? 0.1471 0.1589 0.1508 -0.0405 0.0153  -0.0096 121 VAL   A CG2 
905  N N   . GLY   A 116 ? 0.1117 0.1342 0.1437 -0.0199 0.0065  -0.0056 122 GLY   A N   
906  C CA  . GLY   A 116 ? 0.1143 0.1405 0.1525 -0.0148 0.0012  -0.0041 122 GLY   A CA  
907  C C   . GLY   A 116 ? 0.1112 0.1382 0.1554 -0.0085 -0.0017 -0.0048 122 GLY   A C   
908  O O   . GLY   A 116 ? 0.1046 0.1291 0.1502 -0.0078 -0.0001 -0.0055 122 GLY   A O   
909  N N   . ILE   A 117 ? 0.1002 0.1290 0.1468 -0.0044 -0.0063 -0.0045 123 ILE   A N   
910  C CA  . ILE   A 117 ? 0.1023 0.1290 0.1492 0.0000  -0.0098 -0.0056 123 ILE   A CA  
911  C C   . ILE   A 117 ? 0.0961 0.1250 0.1382 0.0026  -0.0109 -0.0061 123 ILE   A C   
912  O O   . ILE   A 117 ? 0.0826 0.1149 0.1281 0.0027  -0.0109 -0.0053 123 ILE   A O   
913  C CB  . ILE   A 117 ? 0.1172 0.1405 0.1725 0.0018  -0.0138 -0.0065 123 ILE   A CB  
914  C CG1 . ILE   A 117 ? 0.1514 0.1759 0.2113 0.0013  -0.0140 -0.0064 123 ILE   A CG1 
915  C CG2 . ILE   A 117 ? 0.1239 0.1447 0.1889 0.0006  -0.0123 -0.0061 123 ILE   A CG2 
916  C CD1 . ILE   A 117 ? 0.1720 0.1932 0.2417 0.0032  -0.0188 -0.0074 123 ILE   A CD1 
917  N N   . VAL   A 118 ? 0.0983 0.1240 0.1331 0.0045  -0.0115 -0.0071 124 VAL   A N   
918  C CA  . VAL   A 118 ? 0.1008 0.1264 0.1306 0.0068  -0.0095 -0.0090 124 VAL   A CA  
919  C C   . VAL   A 118 ? 0.1167 0.1401 0.1512 0.0092  -0.0121 -0.0115 124 VAL   A C   
920  O O   . VAL   A 118 ? 0.1184 0.1371 0.1537 0.0094  -0.0172 -0.0125 124 VAL   A O   
921  C CB  . VAL   A 118 ? 0.1189 0.1377 0.1348 0.0070  -0.0091 -0.0101 124 VAL   A CB  
922  C CG1 . VAL   A 118 ? 0.1335 0.1496 0.1428 0.0089  -0.0042 -0.0137 124 VAL   A CG1 
923  C CG2 . VAL   A 118 ? 0.1319 0.1525 0.1446 0.0046  -0.0059 -0.0070 124 VAL   A CG2 
924  N N   . SER   A 119 ? 0.1168 0.1439 0.1576 0.0109  -0.0090 -0.0118 125 SER   A N   
925  C CA  . SER   A 119 ? 0.1357 0.1601 0.1831 0.0133  -0.0109 -0.0138 125 SER   A CA  
926  C C   . SER   A 119 ? 0.1590 0.1813 0.2075 0.0165  -0.0052 -0.0175 125 SER   A C   
927  O O   . SER   A 119 ? 0.1784 0.1940 0.2274 0.0186  -0.0056 -0.0216 125 SER   A O   
928  C CB  . SER   A 119 ? 0.1609 0.1907 0.2205 0.0119  -0.0135 -0.0093 125 SER   A CB  
929  O OG  . SER   A 119 ? 0.1858 0.2134 0.2544 0.0144  -0.0149 -0.0101 125 SER   A OG  
930  N N   . THR   A 120 ? 0.1526 0.1797 0.2027 0.0168  0.0012  -0.0165 126 THR   A N   
931  C CA  . THR   A 120 ? 0.1629 0.1877 0.2170 0.0199  0.0098  -0.0207 126 THR   A CA  
932  C C   . THR   A 120 ? 0.1819 0.2055 0.2247 0.0186  0.0177  -0.0219 126 THR   A C   
933  O O   . THR   A 120 ? 0.1580 0.1860 0.1965 0.0156  0.0156  -0.0179 126 THR   A O   
934  C CB  . THR   A 120 ? 0.1691 0.2032 0.2486 0.0222  0.0110  -0.0166 126 THR   A CB  
935  O OG1 . THR   A 120 ? 0.1910 0.2353 0.2780 0.0199  0.0113  -0.0109 126 THR   A OG1 
936  C CG2 . THR   A 120 ? 0.1705 0.2061 0.2599 0.0221  0.0024  -0.0128 126 THR   A CG2 
937  N N   . GLY   A 121 ? 0.2084 0.2262 0.2484 0.0205  0.0282  -0.0274 127 GLY   A N   
938  C CA  . GLY   A 121 ? 0.2352 0.2509 0.2643 0.0187  0.0381  -0.0286 127 GLY   A CA  
939  C C   . GLY   A 121 ? 0.2578 0.2699 0.2938 0.0213  0.0530  -0.0342 127 GLY   A C   
940  O O   . GLY   A 121 ? 0.2665 0.2773 0.3169 0.0250  0.0552  -0.0374 127 GLY   A O   
941  N N   . GLY   A 122 ? 0.2808 0.2902 0.3076 0.0194  0.0646  -0.0355 128 GLY   A N   
942  C CA  . GLY   A 122 ? 0.2974 0.3020 0.3308 0.0214  0.0826  -0.0418 128 GLY   A CA  
943  C C   . GLY   A 122 ? 0.2882 0.3079 0.3536 0.0231  0.0916  -0.0372 128 GLY   A C   
944  O O   . GLY   A 122 ? 0.2752 0.3101 0.3632 0.0235  0.0814  -0.0290 128 GLY   A O   
945  N N   . ASN   A 123 ? 0.2851 0.2998 0.3524 0.0234  0.1109  -0.0423 129 ASN   A N   
946  C CA  . ASN   A 123 ? 0.2763 0.3054 0.3775 0.0247  0.1216  -0.0380 129 ASN   A CA  
947  C C   . ASN   A 123 ? 0.2552 0.2946 0.3542 0.0200  0.1139  -0.0293 129 ASN   A C   
948  O O   . ASN   A 123 ? 0.2487 0.3042 0.3804 0.0204  0.1130  -0.0226 129 ASN   A O   
949  C CB  . ASN   A 123 ? 0.2853 0.3292 0.4326 0.0303  0.1170  -0.0335 129 ASN   A CB  
950  C CG  . ASN   A 123 ? 0.3556 0.3926 0.5209 0.0358  0.1308  -0.0413 129 ASN   A CG  
951  O OD1 . ASN   A 123 ? 0.3854 0.4086 0.5368 0.0356  0.1505  -0.0509 129 ASN   A OD1 
952  N ND2 . ASN   A 123 ? 0.3511 0.3967 0.5485 0.0405  0.1215  -0.0371 129 ASN   A ND2 
953  N N   . GLY   A 124 ? 0.2364 0.2662 0.2992 0.0153  0.1074  -0.0290 130 GLY   A N   
954  C CA  . GLY   A 124 ? 0.2141 0.2510 0.2736 0.0109  0.1005  -0.0216 130 GLY   A CA  
955  C C   . GLY   A 124 ? 0.1822 0.2324 0.2593 0.0110  0.0827  -0.0145 130 GLY   A C   
956  O O   . GLY   A 124 ? 0.1729 0.2319 0.2580 0.0075  0.0785  -0.0085 130 GLY   A O   
957  N N   . LEU   A 125 ? 0.1711 0.2211 0.2515 0.0139  0.0725  -0.0154 131 LEU   A N   
958  C CA  . LEU   A 125 ? 0.1615 0.2210 0.2529 0.0129  0.0566  -0.0093 131 LEU   A CA  
959  C C   . LEU   A 125 ? 0.1782 0.2284 0.2465 0.0126  0.0462  -0.0113 131 LEU   A C   
960  O O   . LEU   A 125 ? 0.2153 0.2544 0.2691 0.0146  0.0488  -0.0171 131 LEU   A O   
961  C CB  . LEU   A 125 ? 0.1490 0.2183 0.2722 0.0164  0.0534  -0.0066 131 LEU   A CB  
962  C CG  . LEU   A 125 ? 0.1490 0.2304 0.3054 0.0172  0.0608  -0.0028 131 LEU   A CG  
963  C CD1 . LEU   A 125 ? 0.1354 0.2240 0.3238 0.0214  0.0566  0.0002  131 LEU   A CD1 
964  C CD2 . LEU   A 125 ? 0.1518 0.2433 0.3143 0.0112  0.0537  0.0045  131 LEU   A CD2 
965  N N   . VAL   A 126 ? 0.1496 0.2036 0.2158 0.0096  0.0350  -0.0069 132 VAL   A N   
966  C CA  . VAL   A 126 ? 0.1389 0.1858 0.1900 0.0093  0.0260  -0.0081 132 VAL   A CA  
967  C C   . VAL   A 126 ? 0.1199 0.1741 0.1848 0.0085  0.0168  -0.0041 132 VAL   A C   
968  O O   . VAL   A 126 ? 0.1078 0.1701 0.1828 0.0051  0.0139  0.0007  132 VAL   A O   
969  C CB  . VAL   A 126 ? 0.1541 0.1947 0.1858 0.0060  0.0237  -0.0073 132 VAL   A CB  
970  C CG1 . VAL   A 126 ? 0.1480 0.1957 0.1860 0.0019  0.0231  -0.0026 132 VAL   A CG1 
971  C CG2 . VAL   A 126 ? 0.1628 0.1975 0.1857 0.0060  0.0146  -0.0080 132 VAL   A CG2 
972  N N   . GLY   A 127 ? 0.1124 0.1627 0.1768 0.0107  0.0120  -0.0058 133 GLY   A N   
973  C CA  . GLY   A 127 ? 0.1072 0.1619 0.1808 0.0091  0.0039  -0.0017 133 GLY   A CA  
974  C C   . GLY   A 127 ? 0.1140 0.1628 0.1747 0.0070  -0.0012 -0.0025 133 GLY   A C   
975  O O   . GLY   A 127 ? 0.1272 0.1685 0.1778 0.0089  -0.0009 -0.0065 133 GLY   A O   
976  N N   . PHE   A 128 ? 0.1041 0.1557 0.1654 0.0024  -0.0058 0.0013  134 PHE   A N   
977  C CA  . PHE   A 128 ? 0.1025 0.1488 0.1550 -0.0003 -0.0080 0.0005  134 PHE   A CA  
978  C C   . PHE   A 128 ? 0.1095 0.1555 0.1655 -0.0025 -0.0123 0.0032  134 PHE   A C   
979  O O   . PHE   A 128 ? 0.1035 0.1537 0.1639 -0.0058 -0.0155 0.0078  134 PHE   A O   
980  C CB  . PHE   A 128 ? 0.0930 0.1393 0.1389 -0.0053 -0.0065 0.0014  134 PHE   A CB  
981  C CG  . PHE   A 128 ? 0.0990 0.1455 0.1414 -0.0044 -0.0025 0.0003  134 PHE   A CG  
982  C CD1 . PHE   A 128 ? 0.1024 0.1427 0.1376 -0.0022 -0.0012 -0.0020 134 PHE   A CD1 
983  C CD2 . PHE   A 128 ? 0.1034 0.1560 0.1507 -0.0064 -0.0008 0.0027  134 PHE   A CD2 
984  C CE1 . PHE   A 128 ? 0.1081 0.1470 0.1377 -0.0023 0.0023  -0.0018 134 PHE   A CE1 
985  C CE2 . PHE   A 128 ? 0.1009 0.1529 0.1446 -0.0062 0.0040  0.0022  134 PHE   A CE2 
986  C CZ  . PHE   A 128 ? 0.1004 0.1450 0.1338 -0.0042 0.0058  0.0000  134 PHE   A CZ  
987  N N   . ALA   A 129 ? 0.1030 0.1437 0.1575 -0.0015 -0.0130 0.0012  135 ALA   A N   
988  C CA  . ALA   A 129 ? 0.1162 0.1552 0.1725 -0.0043 -0.0156 0.0040  135 ALA   A CA  
989  C C   . ALA   A 129 ? 0.1333 0.1694 0.1802 -0.0111 -0.0131 0.0047  135 ALA   A C   
990  O O   . ALA   A 129 ? 0.1206 0.1532 0.1650 -0.0111 -0.0091 0.0013  135 ALA   A O   
991  C CB  . ALA   A 129 ? 0.1255 0.1598 0.1859 -0.0011 -0.0162 0.0013  135 ALA   A CB  
992  N N   . ASP   A 130 ? 0.1465 0.1830 0.1880 -0.0173 -0.0156 0.0090  136 ASP   A N   
993  C CA  . ASP   A 130 ? 0.1535 0.1845 0.1817 -0.0253 -0.0121 0.0085  136 ASP   A CA  
994  C C   . ASP   A 130 ? 0.1589 0.1825 0.1839 -0.0274 -0.0069 0.0066  136 ASP   A C   
995  O O   . ASP   A 130 ? 0.1650 0.1881 0.1956 -0.0256 -0.0092 0.0088  136 ASP   A O   
996  C CB  . ASP   A 130 ? 0.1829 0.2141 0.2027 -0.0331 -0.0182 0.0143  136 ASP   A CB  
997  C CG  . ASP   A 130 ? 0.2495 0.2720 0.2500 -0.0432 -0.0142 0.0126  136 ASP   A CG  
998  O OD1 . ASP   A 130 ? 0.2433 0.2643 0.2411 -0.0435 -0.0086 0.0077  136 ASP   A OD1 
999  O OD2 . ASP   A 130 ? 0.3019 0.3175 0.2889 -0.0511 -0.0161 0.0158  136 ASP   A OD2 
1000 N N   . VAL   A 131 ? 0.1447 0.1621 0.1630 -0.0312 0.0012  0.0024  137 VAL   A N   
1001 C CA  . VAL   A 131 ? 0.1534 0.1634 0.1708 -0.0343 0.0089  0.0004  137 VAL   A CA  
1002 C C   . VAL   A 131 ? 0.1747 0.1746 0.1724 -0.0450 0.0165  -0.0012 137 VAL   A C   
1003 O O   . VAL   A 131 ? 0.1874 0.1794 0.1822 -0.0489 0.0257  -0.0034 137 VAL   A O   
1004 C CB  . VAL   A 131 ? 0.1473 0.1576 0.1813 -0.0282 0.0141  -0.0038 137 VAL   A CB  
1005 C CG1 . VAL   A 131 ? 0.1489 0.1657 0.1969 -0.0197 0.0061  -0.0027 137 VAL   A CG1 
1006 C CG2 . VAL   A 131 ? 0.1389 0.1474 0.1735 -0.0282 0.0194  -0.0078 137 VAL   A CG2 
1007 N N   . ARG   A 132 ? 0.1775 0.1763 0.1615 -0.0505 0.0136  -0.0009 138 ARG   A N   
1008 C CA  . ARG   A 132 ? 0.2040 0.1907 0.1655 -0.0620 0.0205  -0.0038 138 ARG   A CA  
1009 C C   . ARG   A 132 ? 0.2337 0.2105 0.1751 -0.0718 0.0211  -0.0005 138 ARG   A C   
1010 O O   . ARG   A 132 ? 0.2542 0.2174 0.1762 -0.0812 0.0317  -0.0050 138 ARG   A O   
1011 C CB  . ARG   A 132 ? 0.2127 0.2009 0.1650 -0.0663 0.0142  -0.0032 138 ARG   A CB  
1012 C CG  . ARG   A 132 ? 0.2057 0.1999 0.1731 -0.0589 0.0166  -0.0069 138 ARG   A CG  
1013 C CD  . ARG   A 132 ? 0.2157 0.2123 0.1761 -0.0636 0.0100  -0.0054 138 ARG   A CD  
1014 N NE  . ARG   A 132 ? 0.1930 0.2012 0.1623 -0.0603 -0.0026 0.0019  138 ARG   A NE  
1015 C CZ  . ARG   A 132 ? 0.2006 0.2147 0.1718 -0.0626 -0.0100 0.0051  138 ARG   A CZ  
1016 N NH1 . ARG   A 132 ? 0.1903 0.1990 0.1520 -0.0692 -0.0075 0.0017  138 ARG   A NH1 
1017 N NH2 . ARG   A 132 ? 0.1945 0.2197 0.1796 -0.0584 -0.0194 0.0115  138 ARG   A NH2 
1018 N N   . ASP   A 133 ? 0.2275 0.2093 0.1719 -0.0704 0.0105  0.0073  139 ASP   A N   
1019 C CA  . ASP   A 133 ? 0.2464 0.2181 0.1712 -0.0800 0.0095  0.0124  139 ASP   A CA  
1020 C C   . ASP   A 133 ? 0.2500 0.2158 0.1799 -0.0790 0.0217  0.0099  139 ASP   A C   
1021 O O   . ASP   A 133 ? 0.2569 0.2112 0.1670 -0.0885 0.0251  0.0130  139 ASP   A O   
1022 C CB  . ASP   A 133 ? 0.2692 0.2483 0.1996 -0.0786 -0.0072 0.0230  139 ASP   A CB  
1023 C CG  . ASP   A 133 ? 0.3155 0.3062 0.2749 -0.0656 -0.0104 0.0244  139 ASP   A CG  
1024 O OD1 . ASP   A 133 ? 0.2915 0.2903 0.2686 -0.0561 -0.0073 0.0188  139 ASP   A OD1 
1025 O OD2 . ASP   A 133 ? 0.3429 0.3332 0.3060 -0.0655 -0.0163 0.0312  139 ASP   A OD2 
1026 N N   . LEU   A 134 ? 0.2337 0.2069 0.1898 -0.0683 0.0276  0.0052  140 LEU   A N   
1027 C CA  . LEU   A 134 ? 0.2361 0.2059 0.2038 -0.0667 0.0380  0.0035  140 LEU   A CA  
1028 C C   . LEU   A 134 ? 0.2447 0.2027 0.2037 -0.0733 0.0564  -0.0042 140 LEU   A C   
1029 O O   . LEU   A 134 ? 0.2436 0.2046 0.2241 -0.0671 0.0649  -0.0099 140 LEU   A O   
1030 C CB  . LEU   A 134 ? 0.2149 0.1968 0.2149 -0.0537 0.0345  0.0021  140 LEU   A CB  
1031 C CG  . LEU   A 134 ? 0.2173 0.2096 0.2269 -0.0464 0.0189  0.0073  140 LEU   A CG  
1032 C CD1 . LEU   A 134 ? 0.2001 0.2005 0.2351 -0.0357 0.0164  0.0046  140 LEU   A CD1 
1033 C CD2 . LEU   A 134 ? 0.2340 0.2235 0.2373 -0.0501 0.0127  0.0149  140 LEU   A CD2 
1034 N N   . LEU   A 135 ? 0.2658 0.2090 0.1929 -0.0865 0.0627  -0.0042 141 LEU   A N   
1035 C CA  . LEU   A 135 ? 0.2926 0.2215 0.2077 -0.0940 0.0826  -0.0130 141 LEU   A CA  
1036 C C   . LEU   A 135 ? 0.3090 0.2358 0.2461 -0.0911 0.0997  -0.0169 141 LEU   A C   
1037 O O   . LEU   A 135 ? 0.3171 0.2373 0.2620 -0.0917 0.1170  -0.0254 141 LEU   A O   
1038 C CB  . LEU   A 135 ? 0.3245 0.2347 0.1951 -0.1108 0.0862  -0.0128 141 LEU   A CB  
1039 C CG  . LEU   A 135 ? 0.3409 0.2522 0.1888 -0.1165 0.0663  -0.0056 141 LEU   A CG  
1040 C CD1 . LEU   A 135 ? 0.3683 0.2579 0.1694 -0.1351 0.0699  -0.0051 141 LEU   A CD1 
1041 C CD2 . LEU   A 135 ? 0.3440 0.2644 0.2023 -0.1109 0.0596  -0.0092 141 LEU   A CD2 
1042 N N   . TRP   A 136 ? 0.3019 0.2339 0.2518 -0.0878 0.0951  -0.0106 142 TRP   A N   
1043 C CA  . TRP   A 136 ? 0.3103 0.2419 0.2852 -0.0851 0.1092  -0.0128 142 TRP   A CA  
1044 C C   . TRP   A 136 ? 0.3075 0.2508 0.3231 -0.0731 0.1114  -0.0175 142 TRP   A C   
1045 O O   . TRP   A 136 ? 0.2977 0.2387 0.3360 -0.0723 0.1271  -0.0216 142 TRP   A O   
1046 C CB  . TRP   A 136 ? 0.3015 0.2362 0.2815 -0.0846 0.1016  -0.0044 142 TRP   A CB  
1047 C CG  . TRP   A 136 ? 0.2838 0.2333 0.2786 -0.0747 0.0795  0.0018  142 TRP   A CG  
1048 C CD1 . TRP   A 136 ? 0.2936 0.2449 0.2708 -0.0762 0.0631  0.0088  142 TRP   A CD1 
1049 C CD2 . TRP   A 136 ? 0.2607 0.2238 0.2911 -0.0626 0.0725  0.0012  142 TRP   A CD2 
1050 N NE1 . TRP   A 136 ? 0.2827 0.2475 0.2833 -0.0651 0.0487  0.0116  142 TRP   A NE1 
1051 C CE2 . TRP   A 136 ? 0.2653 0.2364 0.2956 -0.0574 0.0539  0.0069  142 TRP   A CE2 
1052 C CE3 . TRP   A 136 ? 0.2548 0.2231 0.3180 -0.0562 0.0796  -0.0032 142 TRP   A CE3 
1053 C CZ2 . TRP   A 136 ? 0.2640 0.2462 0.3203 -0.0468 0.0436  0.0068  142 TRP   A CZ2 
1054 C CZ3 . TRP   A 136 ? 0.2521 0.2321 0.3411 -0.0462 0.0664  -0.0018 142 TRP   A CZ3 
1055 C CH2 . TRP   A 136 ? 0.2536 0.2394 0.3365 -0.0420 0.0494  0.0026  142 TRP   A CH2 
1056 N N   . LEU   A 137 ? 0.3059 0.2606 0.3306 -0.0647 0.0962  -0.0167 143 LEU   A N   
1057 C CA  . LEU   A 137 ? 0.3135 0.2779 0.3722 -0.0544 0.0950  -0.0195 143 LEU   A CA  
1058 C C   . LEU   A 137 ? 0.3593 0.3159 0.4295 -0.0563 0.1145  -0.0272 143 LEU   A C   
1059 O O   . LEU   A 137 ? 0.3444 0.3071 0.4502 -0.0492 0.1172  -0.0284 143 LEU   A O   
1060 C CB  . LEU   A 137 ? 0.2982 0.2720 0.3549 -0.0479 0.0780  -0.0176 143 LEU   A CB  
1061 C CG  . LEU   A 137 ? 0.2990 0.2831 0.3603 -0.0417 0.0600  -0.0116 143 LEU   A CG  
1062 C CD1 . LEU   A 137 ? 0.2989 0.2901 0.3563 -0.0365 0.0476  -0.0108 143 LEU   A CD1 
1063 C CD2 . LEU   A 137 ? 0.2964 0.2868 0.3886 -0.0350 0.0575  -0.0104 143 LEU   A CD2 
1064 N N   . ASP   A 138 ? 0.4105 0.3526 0.4514 -0.0666 0.1278  -0.0324 144 ASP   A N   
1065 C CA  . ASP   A 138 ? 0.4574 0.3885 0.5048 -0.0699 0.1491  -0.0412 144 ASP   A CA  
1066 C C   . ASP   A 138 ? 0.5057 0.4251 0.5567 -0.0767 0.1725  -0.0453 144 ASP   A C   
1067 O O   . ASP   A 138 ? 0.5250 0.4313 0.5738 -0.0819 0.1934  -0.0539 144 ASP   A O   
1068 C CB  . ASP   A 138 ? 0.5031 0.4216 0.5130 -0.0790 0.1522  -0.0461 144 ASP   A CB  
1069 C CG  . ASP   A 138 ? 0.5717 0.4995 0.5837 -0.0729 0.1360  -0.0445 144 ASP   A CG  
1070 O OD1 . ASP   A 138 ? 0.5830 0.5216 0.6290 -0.0621 0.1315  -0.0436 144 ASP   A OD1 
1071 O OD2 . ASP   A 138 ? 0.6056 0.5295 0.5858 -0.0793 0.1274  -0.0434 144 ASP   A OD2 
1072 N N   . GLU   A 139 ? 0.5252 0.4473 0.5799 -0.0777 0.1709  -0.0398 145 GLU   A N   
1073 C CA  . GLU   A 139 ? 0.5521 0.4629 0.6114 -0.0846 0.1948  -0.0433 145 GLU   A CA  
1074 C C   . GLU   A 139 ? 0.5536 0.4754 0.6462 -0.0790 0.1911  -0.0371 145 GLU   A C   
1075 O O   . GLU   A 139 ? 0.5649 0.4785 0.6616 -0.0852 0.2097  -0.0382 145 GLU   A O   
1076 C CB  . GLU   A 139 ? 0.6157 0.5063 0.6220 -0.1005 0.2053  -0.0449 145 GLU   A CB  
1077 C CG  . GLU   A 139 ? 0.6974 0.5901 0.6717 -0.1043 0.1835  -0.0352 145 GLU   A CG  
1078 C CD  . GLU   A 139 ? 0.7988 0.6785 0.7236 -0.1152 0.1784  -0.0363 145 GLU   A CD  
1079 O OE1 . GLU   A 139 ? 0.8214 0.6933 0.7112 -0.1247 0.1701  -0.0295 145 GLU   A OE1 
1080 O OE2 . GLU   A 139 ? 0.8379 0.7145 0.7597 -0.1149 0.1820  -0.0434 145 GLU   A OE2 
1081 N N1  . A1BN4 B .   ? 0.3927 0.3779 0.4249 0.0244  0.0146  -0.0442 201 A1BN4 A N1  
1082 C C4  . A1BN4 B .   ? 0.3999 0.3706 0.4147 0.0220  0.0084  -0.0502 201 A1BN4 A C4  
1083 C C5  . A1BN4 B .   ? 0.4044 0.3927 0.4290 0.0234  0.0217  -0.0432 201 A1BN4 A C5  
1084 C C6  . A1BN4 B .   ? 0.4431 0.4195 0.4363 0.0190  0.0214  -0.0466 201 A1BN4 A C6  
1085 C C7  . A1BN4 B .   ? 0.4710 0.4409 0.4526 0.0185  0.0365  -0.0516 201 A1BN4 A C7  
1086 C C8  . A1BN4 B .   ? 0.4795 0.4519 0.4498 0.0157  0.0400  -0.0479 201 A1BN4 A C8  
1087 C C10 . A1BN4 B .   ? 0.4975 0.4562 0.4624 0.0172  0.0692  -0.0605 201 A1BN4 A C10 
1088 O O1  . A1BN4 B .   ? 0.3807 0.3804 0.4230 0.0253  0.0269  -0.0388 201 A1BN4 A O1  
1089 C C3  . A1BN4 B .   ? 0.3890 0.3644 0.4104 0.0204  -0.0050 -0.0448 201 A1BN4 A C3  
1090 C C2  . A1BN4 B .   ? 0.3715 0.3582 0.4194 0.0232  -0.0064 -0.0388 201 A1BN4 A C2  
1091 C C12 . A1BN4 B .   ? 0.3692 0.3653 0.4285 0.0272  0.0112  -0.0382 201 A1BN4 A C12 
1092 C C1  . A1BN4 B .   ? 0.3616 0.3611 0.4212 0.0247  -0.0009 -0.0329 201 A1BN4 A C1  
1093 C C   . A1BN4 B .   ? 0.3434 0.3525 0.4249 0.0256  -0.0049 -0.0255 201 A1BN4 A C   
1094 O O   . A1BN4 B .   ? 0.3390 0.3466 0.4359 0.0285  -0.0036 -0.0257 201 A1BN4 A O   
1095 N N   . A1BN4 B .   ? 0.3304 0.3478 0.4122 0.0226  -0.0094 -0.0188 201 A1BN4 A N   
1096 C C11 . A1BN4 B .   ? 0.4909 0.4517 0.4743 0.0206  0.0493  -0.0601 201 A1BN4 A C11 
1097 O O2  . A1BN4 B .   ? 0.4950 0.4497 0.4866 0.0229  0.0480  -0.0651 201 A1BN4 A O2  
1098 N N2  . A1BN4 B .   ? 0.5000 0.4551 0.4761 0.0202  0.0666  -0.0650 201 A1BN4 A N2  
1099 C C9  . A1BN4 B .   ? 0.4881 0.4551 0.4495 0.0149  0.0558  -0.0520 201 A1BN4 A C9  
# 
