data_7HVK
# 
_entry.id   7HVK 
# 
_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   7HVK         pdb_00007hvk 10.2210/pdb7hvk/pdb 
WWPDB D_1001407985 ?            ?                   
# 
_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                        7HVK 
_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-methyl-2H-indazol-4-yl)acetyl]pyrrolidine-3-carboxamide' 286.329   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                           65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1   ?         ? ? ? 
5 water       nat water                                                                18.015    187 ?         ? ? ? 
# 
_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-methyl-2H-indazol-4-yl)acetyl]pyrrolidine-3-carboxamide' A1BPI 
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 
A1BPI non-polymer         . '(3S)-1-[(2-methyl-2H-indazol-4-yl)acetyl]pyrrolidine-3-carboxamide' ? 'C15 H18 N4 O2'  286.329 
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 140 146 146 GLU GLU 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        A1BPI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPI 
_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 A1BPI 1   201 201 A1BPI LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 3   DMS   DMS A . 
E 5 HOH   1   301 30  HOH   HOH A . 
E 5 HOH   2   302 137 HOH   HOH A . 
E 5 HOH   3   303 256 HOH   HOH A . 
E 5 HOH   4   304 72  HOH   HOH A . 
E 5 HOH   5   305 169 HOH   HOH A . 
E 5 HOH   6   306 263 HOH   HOH A . 
E 5 HOH   7   307 261 HOH   HOH A . 
E 5 HOH   8   308 152 HOH   HOH A . 
E 5 HOH   9   309 103 HOH   HOH A . 
E 5 HOH   10  310 110 HOH   HOH A . 
E 5 HOH   11  311 41  HOH   HOH A . 
E 5 HOH   12  312 75  HOH   HOH A . 
E 5 HOH   13  313 26  HOH   HOH A . 
E 5 HOH   14  314 119 HOH   HOH A . 
E 5 HOH   15  315 36  HOH   HOH A . 
E 5 HOH   16  316 121 HOH   HOH A . 
E 5 HOH   17  317 68  HOH   HOH A . 
E 5 HOH   18  318 234 HOH   HOH A . 
E 5 HOH   19  319 111 HOH   HOH A . 
E 5 HOH   20  320 34  HOH   HOH A . 
E 5 HOH   21  321 42  HOH   HOH A . 
E 5 HOH   22  322 77  HOH   HOH A . 
E 5 HOH   23  323 59  HOH   HOH A . 
E 5 HOH   24  324 55  HOH   HOH A . 
E 5 HOH   25  325 133 HOH   HOH A . 
E 5 HOH   26  326 25  HOH   HOH A . 
E 5 HOH   27  327 29  HOH   HOH A . 
E 5 HOH   28  328 251 HOH   HOH A . 
E 5 HOH   29  329 19  HOH   HOH A . 
E 5 HOH   30  330 107 HOH   HOH A . 
E 5 HOH   31  331 144 HOH   HOH A . 
E 5 HOH   32  332 57  HOH   HOH A . 
E 5 HOH   33  333 170 HOH   HOH A . 
E 5 HOH   34  334 49  HOH   HOH A . 
E 5 HOH   35  335 7   HOH   HOH A . 
E 5 HOH   36  336 252 HOH   HOH A . 
E 5 HOH   37  337 37  HOH   HOH A . 
E 5 HOH   38  338 104 HOH   HOH A . 
E 5 HOH   39  339 9   HOH   HOH A . 
E 5 HOH   40  340 205 HOH   HOH A . 
E 5 HOH   41  341 4   HOH   HOH A . 
E 5 HOH   42  342 2   HOH   HOH A . 
E 5 HOH   43  343 231 HOH   HOH A . 
E 5 HOH   44  344 28  HOH   HOH A . 
E 5 HOH   45  345 15  HOH   HOH A . 
E 5 HOH   46  346 214 HOH   HOH A . 
E 5 HOH   47  347 43  HOH   HOH A . 
E 5 HOH   48  348 21  HOH   HOH A . 
E 5 HOH   49  349 47  HOH   HOH A . 
E 5 HOH   50  350 90  HOH   HOH A . 
E 5 HOH   51  351 174 HOH   HOH A . 
E 5 HOH   52  352 148 HOH   HOH A . 
E 5 HOH   53  353 33  HOH   HOH A . 
E 5 HOH   54  354 211 HOH   HOH A . 
E 5 HOH   55  355 147 HOH   HOH A . 
E 5 HOH   56  356 257 HOH   HOH A . 
E 5 HOH   57  357 70  HOH   HOH A . 
E 5 HOH   58  358 124 HOH   HOH A . 
E 5 HOH   59  359 50  HOH   HOH A . 
E 5 HOH   60  360 259 HOH   HOH A . 
E 5 HOH   61  361 16  HOH   HOH A . 
E 5 HOH   62  362 46  HOH   HOH A . 
E 5 HOH   63  363 105 HOH   HOH A . 
E 5 HOH   64  364 255 HOH   HOH A . 
E 5 HOH   65  365 215 HOH   HOH A . 
E 5 HOH   66  366 18  HOH   HOH A . 
E 5 HOH   67  367 20  HOH   HOH A . 
E 5 HOH   68  368 131 HOH   HOH A . 
E 5 HOH   69  369 167 HOH   HOH A . 
E 5 HOH   70  370 35  HOH   HOH A . 
E 5 HOH   71  371 24  HOH   HOH A . 
E 5 HOH   72  372 14  HOH   HOH A . 
E 5 HOH   73  373 185 HOH   HOH A . 
E 5 HOH   74  374 39  HOH   HOH A . 
E 5 HOH   75  375 11  HOH   HOH A . 
E 5 HOH   76  376 82  HOH   HOH A . 
E 5 HOH   77  377 177 HOH   HOH A . 
E 5 HOH   78  378 220 HOH   HOH A . 
E 5 HOH   79  379 150 HOH   HOH A . 
E 5 HOH   80  380 12  HOH   HOH A . 
E 5 HOH   81  381 100 HOH   HOH A . 
E 5 HOH   82  382 106 HOH   HOH A . 
E 5 HOH   83  383 126 HOH   HOH A . 
E 5 HOH   84  384 52  HOH   HOH A . 
E 5 HOH   85  385 253 HOH   HOH A . 
E 5 HOH   86  386 62  HOH   HOH A . 
E 5 HOH   87  387 27  HOH   HOH A . 
E 5 HOH   88  388 260 HOH   HOH A . 
E 5 HOH   89  389 8   HOH   HOH A . 
E 5 HOH   90  390 146 HOH   HOH A . 
E 5 HOH   91  391 94  HOH   HOH A . 
E 5 HOH   92  392 264 HOH   HOH A . 
E 5 HOH   93  393 269 HOH   HOH A . 
E 5 HOH   94  394 175 HOH   HOH A . 
E 5 HOH   95  395 271 HOH   HOH A . 
E 5 HOH   96  396 89  HOH   HOH A . 
E 5 HOH   97  397 168 HOH   HOH A . 
E 5 HOH   98  398 51  HOH   HOH A . 
E 5 HOH   99  399 84  HOH   HOH A . 
E 5 HOH   100 400 108 HOH   HOH A . 
E 5 HOH   101 401 40  HOH   HOH A . 
E 5 HOH   102 402 132 HOH   HOH A . 
E 5 HOH   103 403 161 HOH   HOH A . 
E 5 HOH   104 404 273 HOH   HOH A . 
E 5 HOH   105 405 176 HOH   HOH A . 
E 5 HOH   106 406 254 HOH   HOH A . 
E 5 HOH   107 407 219 HOH   HOH A . 
E 5 HOH   108 408 17  HOH   HOH A . 
E 5 HOH   109 409 53  HOH   HOH A . 
E 5 HOH   110 410 262 HOH   HOH A . 
E 5 HOH   111 411 95  HOH   HOH A . 
E 5 HOH   112 412 83  HOH   HOH A . 
E 5 HOH   113 413 192 HOH   HOH A . 
E 5 HOH   114 414 23  HOH   HOH A . 
E 5 HOH   115 415 248 HOH   HOH A . 
E 5 HOH   116 416 58  HOH   HOH A . 
E 5 HOH   117 417 156 HOH   HOH A . 
E 5 HOH   118 418 266 HOH   HOH A . 
E 5 HOH   119 419 203 HOH   HOH A . 
E 5 HOH   120 420 71  HOH   HOH A . 
E 5 HOH   121 421 38  HOH   HOH A . 
E 5 HOH   122 422 123 HOH   HOH A . 
E 5 HOH   123 423 80  HOH   HOH A . 
E 5 HOH   124 424 10  HOH   HOH A . 
E 5 HOH   125 425 120 HOH   HOH A . 
E 5 HOH   126 426 182 HOH   HOH A . 
E 5 HOH   127 427 102 HOH   HOH A . 
E 5 HOH   128 428 128 HOH   HOH A . 
E 5 HOH   129 429 96  HOH   HOH A . 
E 5 HOH   130 430 250 HOH   HOH A . 
E 5 HOH   131 431 155 HOH   HOH A . 
E 5 HOH   132 432 76  HOH   HOH A . 
E 5 HOH   133 433 138 HOH   HOH A . 
E 5 HOH   134 434 237 HOH   HOH A . 
E 5 HOH   135 435 69  HOH   HOH A . 
E 5 HOH   136 436 272 HOH   HOH A . 
E 5 HOH   137 437 48  HOH   HOH A . 
E 5 HOH   138 438 233 HOH   HOH A . 
E 5 HOH   139 439 159 HOH   HOH A . 
E 5 HOH   140 440 60  HOH   HOH A . 
E 5 HOH   141 441 201 HOH   HOH A . 
E 5 HOH   142 442 101 HOH   HOH A . 
E 5 HOH   143 443 200 HOH   HOH A . 
E 5 HOH   144 444 65  HOH   HOH A . 
E 5 HOH   145 445 206 HOH   HOH A . 
E 5 HOH   146 446 181 HOH   HOH A . 
E 5 HOH   147 447 204 HOH   HOH A . 
E 5 HOH   148 448 158 HOH   HOH A . 
E 5 HOH   149 449 61  HOH   HOH A . 
E 5 HOH   150 450 268 HOH   HOH A . 
E 5 HOH   151 451 224 HOH   HOH A . 
E 5 HOH   152 452 112 HOH   HOH A . 
E 5 HOH   153 453 154 HOH   HOH A . 
E 5 HOH   154 454 162 HOH   HOH A . 
E 5 HOH   155 455 134 HOH   HOH A . 
E 5 HOH   156 456 99  HOH   HOH A . 
E 5 HOH   157 457 213 HOH   HOH A . 
E 5 HOH   158 458 240 HOH   HOH A . 
E 5 HOH   159 459 184 HOH   HOH A . 
E 5 HOH   160 460 232 HOH   HOH A . 
E 5 HOH   161 461 207 HOH   HOH A . 
E 5 HOH   162 462 241 HOH   HOH A . 
E 5 HOH   163 463 91  HOH   HOH A . 
E 5 HOH   164 464 258 HOH   HOH A . 
E 5 HOH   165 465 270 HOH   HOH A . 
E 5 HOH   166 466 73  HOH   HOH A . 
E 5 HOH   167 467 171 HOH   HOH A . 
E 5 HOH   168 468 127 HOH   HOH A . 
E 5 HOH   169 469 86  HOH   HOH A . 
E 5 HOH   170 470 267 HOH   HOH A . 
E 5 HOH   171 471 221 HOH   HOH A . 
E 5 HOH   172 472 122 HOH   HOH A . 
E 5 HOH   173 473 56  HOH   HOH A . 
E 5 HOH   174 474 208 HOH   HOH A . 
E 5 HOH   175 475 165 HOH   HOH A . 
E 5 HOH   176 476 87  HOH   HOH A . 
E 5 HOH   177 477 125 HOH   HOH A . 
E 5 HOH   178 478 202 HOH   HOH A . 
E 5 HOH   179 479 222 HOH   HOH A . 
E 5 HOH   180 480 118 HOH   HOH A . 
E 5 HOH   181 481 92  HOH   HOH A . 
E 5 HOH   182 482 209 HOH   HOH A . 
E 5 HOH   183 483 229 HOH   HOH A . 
E 5 HOH   184 484 114 HOH   HOH A . 
E 5 HOH   185 485 265 HOH   HOH A . 
E 5 HOH   186 486 238 HOH   HOH A . 
E 5 HOH   187 487 160 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           7HVK 
_cell.length_a           89.175 
_cell.length_b           58.208 
_cell.length_c           32.786 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.41 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVK 
_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          7HVK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.68 
_exptl_crystal.density_percent_sol   54.04 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_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                     7HVK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             44.57 
_reflns.d_resolution_high            1.73 
_reflns.number_obs                   17479 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_netI_over_sigmaI        8.6 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.098 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     95848 
_reflns.pdbx_chi_squared             0.73 
_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                  1.73 
_reflns_shell.d_res_low                   1.83 
_reflns_shell.number_measured_all         13449 
_reflns_shell.number_unique_obs           2547 
_reflns_shell.Rmerge_I_obs                1.605 
_reflns_shell.pdbx_chi_squared            0.57 
_reflns_shell.pdbx_redundancy             5.3 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.787 
_reflns_shell.pdbx_Rpim_I_all             0.771 
_reflns_shell.pdbx_CC_half                0.458 
_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                                 7HVK 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17298 
_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                             44.57 
_refine.ls_d_res_high                            1.734 
_refine.ls_percent_reflns_obs                    98.9 
_refine.ls_R_factor_obs                          0.1968 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1947 
_refine.ls_R_factor_R_free                       0.2364 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.050 
_refine.ls_number_reflns_R_free                  874 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.B_iso_mean                               36.82 
_refine.aniso_B[1][1]                            0.44330 
_refine.aniso_B[2][2]                            0.54190 
_refine.aniso_B[3][3]                            -0.98530 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.96520 
_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             0.111 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.113 
_refine.pdbx_overall_SU_R_Blow_DPI               0.122 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.119 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVK 
_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        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             187 
_refine_hist.number_atoms_total               1296 
_refine_hist.d_res_high                       1.734 
_refine_hist.d_res_low                        44.57 
# 
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  1151 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.91  ? 2.00  1569 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  383  '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  215  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1151 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.56  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.02 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  140  '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  983  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   44 
_refine_ls_shell.d_res_high                       1.73 
_refine_ls_shell.d_res_low                        1.75 
_refine_ls_shell.number_reflns_R_work             380 
_refine_ls_shell.R_factor_R_work                  0.3193 
_refine_ls_shell.percent_reflns_obs               87.14 
_refine_ls_shell.R_factor_R_free                  0.4146 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.71 
_refine_ls_shell.number_reflns_R_free             23 
_refine_ls_shell.number_reflns_all                403 
_refine_ls_shell.R_factor_all                     0.3247 
# 
_struct.entry_id                  7HVK 
_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-0032647-001 (A71EV2A-x3556)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVK 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HVK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 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 ? ? ? ? ? ? ? 2.259 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.372 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
# 
_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_555 110.3 ? 
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_555 115.4 ? 
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_555 112.3 ? 
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 98.9  ? 
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_555 113.8 ? 
# 
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 VAL A 26  ? N VAL A 32  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 LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O 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                   7HVK 
_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_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -138.85 
_pdbx_validate_torsion.psi             -35.87 
# 
_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         15.5855 
_pdbx_refine_tls.origin_y         7.5820 
_pdbx_refine_tls.origin_z         13.5841 
_pdbx_refine_tls.T[1][1]          -0.1042 
_pdbx_refine_tls.T[2][2]          0.0442 
_pdbx_refine_tls.T[3][3]          -0.0192 
_pdbx_refine_tls.T[1][2]          -0.0140 
_pdbx_refine_tls.T[1][3]          -0.0353 
_pdbx_refine_tls.T[2][3]          0.0125 
_pdbx_refine_tls.L[1][1]          1.8383 
_pdbx_refine_tls.L[2][2]          3.3833 
_pdbx_refine_tls.L[3][3]          0.9132 
_pdbx_refine_tls.L[1][2]          1.2584 
_pdbx_refine_tls.L[1][3]          -0.9437 
_pdbx_refine_tls.L[2][3]          -1.0883 
_pdbx_refine_tls.S[1][1]          -0.0392 
_pdbx_refine_tls.S[1][2]          0.0281 
_pdbx_refine_tls.S[1][3]          0.1166 
_pdbx_refine_tls.S[2][1]          0.0817 
_pdbx_refine_tls.S[2][2]          -0.0186 
_pdbx_refine_tls.S[2][3]          -0.1471 
_pdbx_refine_tls.S[3][1]          0.0063 
_pdbx_refine_tls.S[3][2]          -0.0264 
_pdbx_refine_tls.S[3][3]          0.0577 
# 
_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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 486 ? 5.96 . 
2 1 O ? A HOH 487 ? 6.30 . 
# 
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 ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 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 
A1BPI N1   N  N N 1   
A1BPI N3   N  Y N 2   
A1BPI C4   C  N N 3   
A1BPI C5   C  N N 4   
A1BPI C6   C  N N 5   
A1BPI C7   C  N N 6   
A1BPI C8   C  N S 7   
A1BPI C10  C  N N 8   
A1BPI C13  C  Y N 9   
A1BPI O1   O  N N 10  
A1BPI C9   C  N N 11  
A1BPI N2   N  N N 12  
A1BPI O    O  N N 13  
A1BPI C3   C  Y N 14  
A1BPI C11  C  Y N 15  
A1BPI C12  C  Y N 16  
A1BPI C14  C  Y N 17  
A1BPI C2   C  Y N 18  
A1BPI C1   C  Y N 19  
A1BPI N    N  Y N 20  
A1BPI C    C  N N 21  
A1BPI H6   H  N N 22  
A1BPI H5   H  N N 23  
A1BPI H7   H  N N 24  
A1BPI H8   H  N N 25  
A1BPI H9   H  N N 26  
A1BPI H10  H  N N 27  
A1BPI H    H  N N 28  
A1BPI H13  H  N N 29  
A1BPI H14  H  N N 30  
A1BPI H17  H  N N 31  
A1BPI H12  H  N N 32  
A1BPI H11  H  N N 33  
A1BPI H15  H  N N 34  
A1BPI H16  H  N N 35  
A1BPI H4   H  N N 36  
A1BPI H2   H  N N 37  
A1BPI H1   H  N N 38  
A1BPI H3   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1BPI C   N    sing N N 1   
A1BPI N   C1   sing Y N 2   
A1BPI C1  C2   doub Y N 3   
A1BPI C2  C3   sing Y N 4   
A1BPI C3  C4   sing N N 5   
A1BPI C4  C5   sing N N 6   
A1BPI O   C5   doub N N 7   
A1BPI C5  N1   sing N N 8   
A1BPI N1  C6   sing N N 9   
A1BPI C6  C7   sing N N 10  
A1BPI C7  C8   sing N N 11  
A1BPI C8  C9   sing N N 12  
A1BPI N2  C9   sing N N 13  
A1BPI C9  O1   doub N N 14  
A1BPI C10 C8   sing N N 15  
A1BPI N1  C10  sing N N 16  
A1BPI C11 C3   doub Y N 17  
A1BPI C12 C11  sing Y N 18  
A1BPI C13 C12  doub Y N 19  
A1BPI C14 C13  sing Y N 20  
A1BPI C2  C14  sing Y N 21  
A1BPI N3  C14  doub Y N 22  
A1BPI N   N3   sing Y N 23  
A1BPI C4  H6   sing N N 24  
A1BPI C4  H5   sing N N 25  
A1BPI C6  H7   sing N N 26  
A1BPI C6  H8   sing N N 27  
A1BPI C7  H9   sing N N 28  
A1BPI C7  H10  sing N N 29  
A1BPI C8  H    sing N N 30  
A1BPI C10 H13  sing N N 31  
A1BPI C10 H14  sing N N 32  
A1BPI C13 H17  sing N N 33  
A1BPI N2  H12  sing N N 34  
A1BPI N2  H11  sing N N 35  
A1BPI C11 H15  sing N N 36  
A1BPI C12 H16  sing N N 37  
A1BPI C1  H4   sing N N 38  
A1BPI C   H2   sing N N 39  
A1BPI C   H1   sing N N 40  
A1BPI C   H3   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_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                    7HVK 
_atom_sites.fract_transf_matrix[1][1]   0.011214 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000276 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017180 
_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]   0.030510 
_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   ? 19.723 6.929   23.696 1.00 35.31  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.882 7.086   22.815 1.00 35.84  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.958 5.942   21.797 1.00 35.53  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.303 4.906   21.965 1.00 35.86  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.168 7.172   23.637 1.00 37.43  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.425 5.928   24.261 1.00 39.90  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.704 6.159   20.720 1.00 34.27  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.872 5.140   19.699 1.00 33.67  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.150 5.705   18.324 1.00 32.91  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.783 6.845   18.030 1.00 33.15  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.763 4.892   17.465 1.00 31.11  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.091 5.318   16.114 1.00 30.79  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.077 4.157   15.136 1.00 30.62  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.225 3.001   15.546 1.00 31.64  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.481 5.970   16.114 1.00 31.09  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.960 4.457   13.826 1.00 29.59  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.068 3.460   12.763 1.00 29.50  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.469 3.646   12.136 1.00 31.40  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.878 4.790   11.874 1.00 31.50  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.982 3.665   11.675 1.00 28.98  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.552 3.741   12.274 1.00 28.54  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.077 2.559   10.611 1.00 29.88  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.528 4.531   11.319 1.00 27.99  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.206 2.543   11.905 1.00 31.88  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.536 2.619   11.274 1.00 33.68  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.487 1.887   9.955  1.00 34.82  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.467 0.652   9.935  1.00 36.40  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.618 2.014   12.186 1.00 34.39  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.820 2.827   13.440 1.00 35.80  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.605 3.973   13.431 1.00 36.93  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.143 2.515   14.609 1.00 37.29  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.743 4.763   14.564 1.00 37.43  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.274 3.297   15.748 1.00 38.16  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.091 4.412   15.727 1.00 38.13  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.178 5.209   16.840 1.00 38.60  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.388 2.622   8.862  1.00 34.15  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.331 2.038   7.531  1.00 35.34  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.479 2.607   6.701  1.00 37.08  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.591 3.821   6.547  1.00 37.15  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.948 2.242   6.852  1.00 36.24  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.467 3.695   6.962  1.00 36.15  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.967 1.764   5.405  1.00 36.79  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.369 1.735   6.230  1.00 38.02  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.540 2.123   5.452  1.00 38.80  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.410 3.100   6.213  1.00 39.19  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.670 2.895   7.399  1.00 39.77  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.718 4.239   5.590  1.00 38.85  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.463 5.275   6.280  1.00 38.63  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.544 6.375   6.763  1.00 36.63  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.915 7.539   6.704  1.00 36.21  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.621 5.792   5.432  1.00 41.45  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.702 4.755   5.348  1.00 47.79  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.478 4.550   6.290  1.00 49.13  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.726 4.026   4.248  1.00 50.38  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.337 6.010   7.246  1.00 35.27  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.344 6.962   7.766  1.00 34.28  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.867 6.597   9.179  1.00 32.85  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.786 5.415   9.542  1.00 32.21  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.107 7.067   6.838  1.00 33.69  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.400 7.600   5.451  1.00 34.41  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.023 8.829   5.271  1.00 36.04  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.039 6.884   4.320  1.00 34.86  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.305 9.316   3.999  1.00 37.12  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.311 7.362   3.042  1.00 36.14  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.920 8.592   2.886  1.00 38.21  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.204 9.057   1.622  1.00 41.10  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.543 7.621   9.964  1.00 32.12  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.971 7.482   11.302 1.00 31.71  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.663 8.278   11.312 1.00 31.55  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.679 9.494   11.100 1.00 32.04  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.932 8.026   12.368 1.00 32.63  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.328 8.191   13.762 1.00 33.99  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.424 8.556   14.760 1.00 37.56  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.966 9.511   15.770 1.00 40.32  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.452 9.177   16.952 1.00 41.39  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.284 7.899   17.275 1.00 40.46  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.059 10.119  17.802 1.00 39.69  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.531 7.607   11.564 1.00 29.65  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.231 8.289   11.560 1.00 29.06  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.744 8.393   12.983 1.00 28.79  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.597 7.367   13.653 1.00 28.57  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.198 7.543   10.683 1.00 29.21  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.911 8.356   10.538 1.00 28.64  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.782 7.196   9.312  1.00 29.62  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.483 9.617   13.458 1.00 28.15  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.035 9.845   14.839 1.00 28.54  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.838 10.830  14.850 1.00 28.36  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.584 11.486  13.841 1.00 28.37  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.185 10.426  15.721 1.00 30.08  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.378 9.489   15.780 1.00 31.70  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.608 11.819  15.247 1.00 30.62  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.151 10.990  16.017 1.00 27.15  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.129 12.019  16.187 1.00 27.09  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.890 13.352  16.156 1.00 28.48  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.910 13.514  16.856 1.00 28.63  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.431 11.889  17.576 1.00 26.94  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.523 10.672  17.684 1.00 28.27  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.947 9.618   18.141 1.00 29.53  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.288 10.776  17.209 1.00 26.57  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.423 14.314  15.359 1.00 29.50  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.083 15.620  15.256 1.00 30.84  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.270 16.277  16.624 1.00 32.38  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.353 16.793  16.915 1.00 33.09  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.306 16.536  14.305 1.00 31.53  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.079 17.788  13.869 1.00 32.51  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.085 18.713  13.185 1.00 32.23  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.634 19.961  12.655 1.00 34.11  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.665 21.117  13.316 1.00 35.10  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.338 21.165  14.604 1.00 34.18  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.077 22.223  12.711 1.00 32.41  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.252 16.147  17.502 1.00 32.72  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.289 16.725  18.851 1.00 33.20  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.298 16.044  19.796 1.00 33.94  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.636 16.620  20.827 1.00 34.61  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.880 16.819  19.476 1.00 33.47  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.292 15.533  19.976 1.00 34.82  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.562 14.701  19.144 1.00 36.70  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.248 15.034  21.235 1.00 35.12  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.161 13.691  19.903 1.00 36.52  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.526 13.858  21.174 1.00 35.92  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.845 14.886  19.425 1.00 34.14  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.858 14.207  20.239 1.00 35.20  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.259 14.188  19.580 1.00 36.20  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.184 13.598  20.140 1.00 36.51  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.408 12.760  20.568 1.00 35.27  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.094 12.619  21.351 1.00 36.27  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.756 11.162  21.589 1.00 36.43  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.148 13.362  22.670 1.00 37.13  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.416 14.773  18.382 1.00 36.59  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.713 14.779  17.694 1.00 37.86  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.831 15.464  18.516 1.00 39.47  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.553 16.436  19.213 1.00 39.74  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.572 15.442  16.327 1.00 37.59  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.080 14.944  18.441 1.00 40.52  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.262 15.490  19.157 1.00 42.43  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.049 16.511  18.287 1.00 43.56  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.729 16.707  17.109 1.00 43.53  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.188 14.338  19.624 1.00 44.70  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.797 13.740  18.476 1.00 46.39  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.476 13.299  20.492 1.00 45.18  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.081 17.160  18.860 1.00 44.45  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.930 18.101  18.149 1.00 45.98  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.657 17.426  17.000 1.00 44.96  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.725 17.997  15.916 1.00 44.43  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.916 18.718  19.121 1.00 50.36  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.230 19.597  20.106 1.00 57.74  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.504 19.517  21.456 1.00 61.16  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.238 20.497  19.905 1.00 60.13  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 30.701 20.397  22.026 1.00 62.27  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.922 21.011  21.129 1.00 62.03  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.117 16.177  17.200 1.00 44.77  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.769 15.420  16.130 1.00 45.42  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.772 15.206  14.966 1.00 43.43  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.161 15.320  13.807 1.00 44.18  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.275 14.080  16.637 1.00 49.17  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.565 13.645  15.982 1.00 57.47  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.599 14.341  16.045 1.00 59.71  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.538 12.471  15.347 1.00 59.76  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.489 14.941  15.276 1.00 41.03  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.462 14.799  14.257 1.00 38.59  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.288 16.088  13.421 1.00 36.76  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.205 15.997  12.202 1.00 36.30  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.099 14.418  14.886 1.00 37.87  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 28.035 13.024  15.466 1.00 38.84  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.572 12.095  14.832 1.00 38.50  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.424 12.861  16.544 1.00 39.47  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.163 17.259  14.064 1.00 35.89  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.988 18.535  13.342 1.00 36.14  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.243 18.891  12.520 1.00 36.17  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.127 19.400  11.399 1.00 35.50  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.679 19.681  14.313 1.00 35.91  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.268 19.669  14.799 1.00 36.31  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.829 19.339  16.048 1.00 37.34  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.104 19.980  14.028 1.00 36.10  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.453 19.416  16.101 1.00 37.78  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.982 19.809  14.871 1.00 37.13  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.896 20.359  12.694 1.00 36.29  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.680 20.039  14.433 1.00 37.29  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.606 20.606  12.268 1.00 37.07  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.509 20.394  13.116 1.00 37.31  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.426 18.594  13.073 1.00 36.54  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.694 18.826  12.385 1.00 37.47  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.824 17.910  11.162 1.00 37.76  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.466 18.280  10.179 1.00 38.34  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.872 18.586  13.336 1.00 38.02  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.281 16.687  11.246 1.00 37.11  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.363 15.733  10.143 1.00 36.85  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.995 15.542  9.485  1.00 35.03  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.660 14.434  9.087  1.00 34.66  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.923 14.407  10.652 1.00 38.55  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.339 14.574  11.137 1.00 42.97  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.255 14.814  10.354 1.00 45.41  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.548 14.484  12.437 1.00 43.63  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.211 16.630  9.394  1.00 33.37  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.852 16.648  8.877  1.00 32.84  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.779 16.296  7.410  1.00 33.23  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.551 16.809  6.604  1.00 33.23  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.201 18.028  9.123  1.00 31.94  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.774 18.213  8.597  1.00 32.30  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.785 17.281  9.329  1.00 32.05  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.316 19.684  8.707  1.00 31.94  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.851 15.408  7.068  1.00 32.53  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.591 15.015  5.686  1.00 33.08  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.224 15.631  5.274  1.00 32.61  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.112 16.293  4.239  1.00 33.21  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.590 13.459  5.546  1.00 33.83  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.980 13.026  4.215  1.00 34.68  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.996 12.877  5.736  1.00 33.63  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.206 15.462  6.124  1.00 31.17  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.874 15.983  5.849  1.00 31.08  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.061 16.047  7.145  1.00 29.87  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.174 15.157  7.967  1.00 29.62  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.152 15.076  4.810  1.00 31.00  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.684 15.321  4.650  1.00 31.26  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.084 16.221  3.814  1.00 32.04  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.621 14.643  5.346  1.00 30.55  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.709 16.147  3.953  1.00 32.26  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.403 15.173  4.873  1.00 31.33  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.584 13.640  6.326  1.00 30.51  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.162 14.730  5.347  1.00 31.61  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.351 13.185  6.769  1.00 31.05  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.165 13.753  6.308  1.00 31.40  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.218 17.075  7.303  1.00 28.89  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.327 17.173  8.454  1.00 28.93  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.017 17.856  8.068  1.00 29.19  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.988 18.712  7.173  1.00 29.11  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.997 17.874  9.649  1.00 29.76  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.601 19.239  9.302  1.00 32.87  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.686 20.442  9.456  1.00 35.57  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.075 21.546  9.007  1.00 37.43  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.583 20.285  10.030 1.00 35.96  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.947 17.550  8.796  1.00 29.12  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.642 18.157  8.530  1.00 29.13  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.909 18.255  9.852  1.00 28.94  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.467 17.239  10.385 1.00 28.01  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.851 17.286  7.538  1.00 31.18  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.537 17.854  7.033  1.00 36.83  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.890 18.607  7.779  1.00 37.94  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.154 17.535  5.885  1.00 38.02  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.756 19.484  10.355 1.00 28.71  ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 16.085 19.788  11.603 1.00 30.48  ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 14.629 19.285  11.589 1.00 30.49  ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 14.149 18.781  12.606 1.00 31.17  ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 16.067 21.302  11.805 1.00 33.35  ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 15.476 21.609  13.049 1.00 37.10  ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.932 19.419  10.442 1.00 29.29  ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.539 18.994  10.360 1.00 30.50  ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 12.370 17.462  10.390 1.00 29.56  ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 11.277 17.004  10.644 1.00 30.44  ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 11.825 19.629  9.169  1.00 33.74  ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 12.377 19.214  7.931  1.00 37.89  ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.442 16.688  10.208 1.00 28.18  ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 13.424 15.212  10.304 1.00 27.57  ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 14.080 14.702  11.626 1.00 27.18  ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 14.066 13.495  11.899 1.00 26.54  ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 14.177 14.594  9.104  1.00 28.37  ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.459 14.819  7.777  1.00 29.37  ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 14.195 14.191  6.599  1.00 30.13  ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 14.219 12.726  6.688  1.00 29.18  ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 14.262 11.906  5.646  1.00 29.14  ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.298 12.392  4.410  1.00 27.83  ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 14.264 10.593  5.827  1.00 29.20  ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.708 15.600  12.403 1.00 27.48  ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.488 15.269  13.604 1.00 27.28  ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.597 14.256  13.250 1.00 27.37  ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.883 13.362  14.047 1.00 26.95  ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.614 14.746  14.781 1.00 28.17  ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 15.404 14.445  16.065 1.00 29.24  ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 16.260 15.277  16.449 1.00 27.67  ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 15.218 13.340  16.640 1.00 30.01  ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 17.233 14.400  12.057 1.00 27.21  ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 18.323 13.512  11.615 1.00 27.04  ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.610 14.284  11.311 1.00 27.40  ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.563 15.429  10.849 1.00 28.05  ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.942 12.744  10.341 1.00 27.21  ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.886 11.623  10.469 1.00 28.51  ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.679 10.963  9.134  1.00 28.30  ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 17.304 10.598  11.539 1.00 28.52  ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.746 13.614  11.510 1.00 26.11  ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 22.090 14.103  11.211 1.00 26.98  ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.924 12.888  10.817 1.00 27.79  ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.814 11.828  11.440 1.00 28.83  ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.708 14.822  12.407 1.00 27.58  ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 24.107 15.411  12.149 1.00 29.56  ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 24.226 16.791  12.726 1.00 30.26  ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 25.180 14.491  12.660 1.00 31.01  ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.701 13.011  9.746  1.00 27.75  ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.583 11.960  9.273  1.00 28.49  ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.999 12.572  9.241  1.00 30.16  ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 26.195 13.664  8.690  1.00 29.50  ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 24.175 11.420  7.872  1.00 29.56  ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 25.208 10.440  7.337  1.00 30.65  ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.758 10.803  7.876  1.00 29.62  ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.943 11.913  9.893  1.00 31.14  ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 28.351 12.336  9.923  1.00 32.92  ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 29.255 11.236  9.322  1.00 34.43  ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.834 10.080  9.202  1.00 33.80  ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.783 12.680  11.351 1.00 34.37  ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 28.667 11.563  12.217 1.00 37.28  ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.494 11.591  8.919  1.00 35.50  ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.403 10.604  8.331  1.00 37.66  ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 32.184 9.848   9.395  1.00 39.60  ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 32.359 10.341  10.509 1.00 40.10  ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.367 11.268  7.353  1.00 39.93  ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 33.121 12.278  8.002  1.00 42.68  ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.587 8.619   9.084  1.00 40.75  ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 33.379 7.795   10.002 1.00 42.88  ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.634 7.282   9.295  1.00 45.94  ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.652 7.157   8.065  1.00 46.34  ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 32.577 6.583   10.556 1.00 43.18  ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 32.400 5.607   9.532  1.00 43.69  ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 31.256 6.967   11.198 1.00 42.69  ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.663 6.925   10.075 1.00 47.66  ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.880 6.353   9.525  1.00 50.23  ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 36.742 4.819   9.403  1.00 51.10  ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 37.267 4.221   8.461  1.00 51.82  ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 38.085 6.779   10.374 1.00 53.11  ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 37.842 6.389   11.726 1.00 55.36  ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 38.327 8.280   10.319 1.00 53.76  ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 36.029 4.188   10.344 1.00 50.91  ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 35.828 2.743   10.336 1.00 50.73  ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 34.537 2.369   9.613  1.00 50.19  ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 33.579 3.133   9.651  1.00 49.86  ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 35.789 2.221   11.764 1.00 50.87  ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 34.497 1.190   8.972  1.00 49.52  ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 33.288 0.751   8.278  1.00 49.16  ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 32.267 0.183   9.241  1.00 46.81  ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 32.617 -0.568  10.152 1.00 46.79  ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 33.597 -0.295  7.207  1.00 52.91  ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 33.903 0.314   5.850  1.00 60.24  ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 33.461 -0.590  4.733  1.00 66.98  ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 34.247 -0.929  3.837  1.00 69.22  ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 32.190 -1.003  4.767  1.00 67.78  ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 31.010 0.541   9.017  1.00 44.32  ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 29.896 0.051   9.807  1.00 43.06  ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 29.322 -1.216  9.214  1.00 41.68  ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 29.577 -1.534  8.046  1.00 42.15  ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 28.515 -1.932  10.006 1.00 39.81  ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 27.967 -3.222  9.610  1.00 39.15  ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 26.442 -3.273  9.462  1.00 37.28  ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 25.904 -4.363  9.246  1.00 37.28  ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 28.446 -4.295  10.578 1.00 40.98  ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 30.241 -4.441  10.675 1.00 46.47  ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 25.748 -2.139  9.590  1.00 35.74  ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 24.284 -2.128  9.443  1.00 35.11  ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.903 -2.043  7.943  1.00 35.19  ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 24.673 -1.543  7.121  1.00 35.23  ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 23.650 -0.961  10.244 1.00 35.42  ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 23.824 -1.102  11.750 1.00 40.67  ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 23.795 -2.262  12.251 1.00 42.54  ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 23.996 -0.062  12.431 1.00 39.79  ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 22.730 -2.575  7.599  1.00 34.55  ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 22.145 -2.580  6.252  1.00 35.07  ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.848 -1.768  6.353  1.00 33.27  ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 20.084 -1.986  7.288  1.00 32.64  ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.804 -4.046  5.848  1.00 38.91  ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 23.003 -4.704  5.441  1.00 40.54  ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.771 -4.144  4.711  1.00 40.38  ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 20.625 -0.815  5.447  1.00 31.79  ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 19.400 -0.030  5.458  1.00 31.28  ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 18.352 -0.797  4.645  1.00 31.66  ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.646 -1.259  3.535  1.00 32.31  ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.604 1.410   4.908  1.00 30.84  ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.803 2.127   5.596  1.00 31.03  ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 18.299 2.235   5.027  1.00 31.00  ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.676 2.256   7.144  1.00 30.90  ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 17.143 -0.925  5.182  1.00 30.48  ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 16.041 -1.566  4.472  1.00 29.97  ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.616 -0.684  3.283  1.00 29.40  ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.592 0.544   3.390  1.00 27.92  ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.862 -1.733  5.424  1.00 30.02  ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 15.296 -1.295  2.150  1.00 30.48  ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.776 -0.583  0.980  1.00 31.18  ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.447 -1.301  0.703  1.00 32.41  ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.431 -2.318  0.013  1.00 33.26  ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.740 -0.687  -0.212 1.00 31.71  ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 17.124 -0.039  0.020  1.00 34.33  ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 17.109 1.390   0.544  1.00 37.04  ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.461 1.862   0.862  1.00 38.02  ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.735 3.025   1.449  1.00 39.22  ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.757 3.846   1.797  1.00 38.88  ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 19.989 3.370   1.698  1.00 38.93  ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 12.356 -0.832  1.334  1.00 32.80  ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 11.068 -1.531  1.352  1.00 32.80  ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.906  -0.583  1.771  1.00 33.05  ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 10.131 0.604   2.061  1.00 32.59  ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 11.188 -2.680  2.357  1.00 33.36  ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 11.263 -2.129  4.092  1.00 35.86  ? 56  CYS   A SG  1 
ATOM   389  N  N   A ASP   A 1 51  ? 8.674  -1.115  1.831  0.50 33.18  ? 57  ASP   A N   1 
ATOM   390  N  N   B ASP   A 1 51  ? 8.674  -1.155  1.814  0.50 33.59  ? 57  ASP   A N   1 
ATOM   391  C  CA  A ASP   A 1 51  ? 7.538  -0.359  2.337  0.50 33.83  ? 57  ASP   A CA  1 
ATOM   392  C  CA  B ASP   A 1 51  ? 7.409  -0.556  2.233  0.50 34.63  ? 57  ASP   A CA  1 
ATOM   393  C  C   A ASP   A 1 51  ? 6.942  -1.024  3.592  0.50 34.36  ? 57  ASP   A C   1 
ATOM   394  C  C   B ASP   A 1 51  ? 6.844  -1.290  3.474  0.50 34.85  ? 57  ASP   A C   1 
ATOM   395  O  O   A ASP   A 1 51  ? 5.808  -0.691  3.944  0.50 34.52  ? 57  ASP   A O   1 
ATOM   396  O  O   B ASP   A 1 51  ? 5.630  -1.277  3.677  0.50 35.23  ? 57  ASP   A O   1 
ATOM   397  C  CB  A ASP   A 1 51  ? 6.452  -0.119  1.258  0.50 35.39  ? 57  ASP   A CB  1 
ATOM   398  C  CB  B ASP   A 1 51  ? 6.371  -0.673  1.099  0.50 37.03  ? 57  ASP   A CB  1 
ATOM   399  C  CG  A ASP   A 1 51  ? 5.709  -1.335  0.739  0.50 38.74  ? 57  ASP   A CG  1 
ATOM   400  C  CG  B ASP   A 1 51  ? 5.521  0.563   0.926  0.50 43.43  ? 57  ASP   A CG  1 
ATOM   401  O  OD1 A ASP   A 1 51  ? 6.111  -2.462  1.066  0.50 38.59  ? 57  ASP   A OD1 1 
ATOM   402  O  OD1 B ASP   A 1 51  ? 6.032  1.672   1.179  0.50 45.28  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 A ASP   A 1 51  ? 4.736  -1.154  -0.020 0.50 42.21  ? 57  ASP   A OD2 1 
ATOM   404  O  OD2 B ASP   A 1 51  ? 4.363  0.429   0.492  0.50 46.61  ? 57  ASP   A OD2 1 
ATOM   405  N  N   . CYS   A 1 52  ? 7.698  -1.950  4.280  1.00 34.09  ? 58  CYS   A N   1 
ATOM   406  C  CA  . CYS   A 1 52  ? 7.235  -2.674  5.491  1.00 33.53  ? 58  CYS   A CA  1 
ATOM   407  C  C   . CYS   A 1 52  ? 6.525  -1.770  6.473  1.00 32.58  ? 58  CYS   A C   1 
ATOM   408  O  O   . CYS   A 1 52  ? 6.898  -0.611  6.613  1.00 32.97  ? 58  CYS   A O   1 
ATOM   409  C  CB  . CYS   A 1 52  ? 8.371  -3.422  6.195  1.00 33.58  ? 58  CYS   A CB  1 
ATOM   410  S  SG  . CYS   A 1 52  ? 8.972  -4.898  5.328  1.00 35.89  ? 58  CYS   A SG  1 
ATOM   411  N  N   . GLN   A 1 53  ? 5.464  -2.283  7.088  1.00 30.75  ? 59  GLN   A N   1 
ATOM   412  C  CA  . GLN   A 1 53  ? 4.735  -1.572  8.136  1.00 30.40  ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.725  -2.342  9.459  1.00 28.58  ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.915  -2.036  10.341 1.00 27.69  ? 59  GLN   A O   1 
ATOM   415  C  CB  . GLN   A 1 53  ? 3.302  -1.202  7.700  1.00 32.37  ? 59  GLN   A CB  1 
ATOM   416  C  CG  . GLN   A 1 53  ? 3.219  0.143   7.009  1.00 34.91  ? 59  GLN   A CG  1 
ATOM   417  C  CD  . GLN   A 1 53  ? 1.775  0.561   6.835  1.00 37.85  ? 59  GLN   A CD  1 
ATOM   418  O  OE1 . GLN   A 1 53  ? 1.247  0.583   5.715  1.00 37.09  ? 59  GLN   A OE1 1 
ATOM   419  N  NE2 . GLN   A 1 53  ? 1.100  0.891   7.945  1.00 37.61  ? 59  GLN   A NE2 1 
ATOM   420  N  N   . THR   A 1 54  ? 5.566  -3.404  9.573  1.00 27.03  ? 60  THR   A N   1 
ATOM   421  C  CA  . THR   A 1 54  ? 5.725  -4.182  10.785 1.00 26.43  ? 60  THR   A CA  1 
ATOM   422  C  C   . THR   A 1 54  ? 7.222  -4.406  10.975 1.00 24.36  ? 60  THR   A C   1 
ATOM   423  O  O   . THR   A 1 54  ? 7.971  -4.517  10.015 1.00 23.92  ? 60  THR   A O   1 
ATOM   424  C  CB  . THR   A 1 54  ? 4.956  -5.518  10.776 1.00 28.79  ? 60  THR   A CB  1 
ATOM   425  O  OG1 . THR   A 1 54  ? 5.511  -6.348  9.765  1.00 31.60  ? 60  THR   A OG1 1 
ATOM   426  C  CG2 . THR   A 1 54  ? 3.427  -5.358  10.588 1.00 29.04  ? 60  THR   A CG2 1 
ATOM   427  N  N   . GLY   A 1 55  ? 7.642  -4.442  12.218 1.00 22.69  ? 61  GLY   A N   1 
ATOM   428  C  CA  . GLY   A 1 55  ? 9.053  -4.592  12.551 1.00 22.11  ? 61  GLY   A CA  1 
ATOM   429  C  C   . GLY   A 1 55  ? 9.211  -4.708  14.052 1.00 21.85  ? 61  GLY   A C   1 
ATOM   430  O  O   . GLY   A 1 55  ? 8.262  -5.048  14.743 1.00 22.81  ? 61  GLY   A O   1 
ATOM   431  N  N   . VAL   A 1 56  ? 10.422 -4.527  14.535 1.00 20.86  ? 62  VAL   A N   1 
ATOM   432  C  CA  . VAL   A 1 56  ? 10.766 -4.648  15.964 1.00 21.26  ? 62  VAL   A CA  1 
ATOM   433  C  C   . VAL   A 1 56  ? 11.631 -3.444  16.342 1.00 21.85  ? 62  VAL   A C   1 
ATOM   434  O  O   . VAL   A 1 56  ? 12.528 -3.101  15.591 1.00 22.82  ? 62  VAL   A O   1 
ATOM   435  C  CB  . VAL   A 1 56  ? 11.531 -5.985  16.254 1.00 22.61  ? 62  VAL   A CB  1 
ATOM   436  C  CG1 . VAL   A 1 56  ? 11.927 -6.076  17.732 1.00 22.72  ? 62  VAL   A CG1 1 
ATOM   437  C  CG2 . VAL   A 1 56  ? 10.679 -7.203  15.900 1.00 22.94  ? 62  VAL   A CG2 1 
ATOM   438  N  N   . TYR   A 1 57  ? 11.432 -2.833  17.540 1.00 22.05  ? 63  TYR   A N   1 
ATOM   439  C  CA  . TYR   A 1 57  ? 12.284 -1.699  17.932 1.00 20.91  ? 63  TYR   A CA  1 
ATOM   440  C  C   . TYR   A 1 57  ? 12.862 -1.938  19.304 1.00 22.37  ? 63  TYR   A C   1 
ATOM   441  O  O   . TYR   A 1 57  ? 12.239 -2.644  20.073 1.00 22.09  ? 63  TYR   A O   1 
ATOM   442  C  CB  . TYR   A 1 57  ? 11.508 -0.343  17.880 1.00 20.03  ? 63  TYR   A CB  1 
ATOM   443  C  CG  . TYR   A 1 57  ? 10.577 -0.053  19.054 1.00 21.62  ? 63  TYR   A CG  1 
ATOM   444  C  CD1 . TYR   A 1 57  ? 9.289  -0.586  19.100 1.00 22.92  ? 63  TYR   A CD1 1 
ATOM   445  C  CD2 . TYR   A 1 57  ? 10.983 0.765   20.108 1.00 22.99  ? 63  TYR   A CD2 1 
ATOM   446  C  CE1 . TYR   A 1 57  ? 8.428  -0.304  20.160 1.00 24.58  ? 63  TYR   A CE1 1 
ATOM   447  C  CE2 . TYR   A 1 57  ? 10.141 1.018   21.196 1.00 24.18  ? 63  TYR   A CE2 1 
ATOM   448  C  CZ  . TYR   A 1 57  ? 8.861  0.486   21.211 1.00 25.01  ? 63  TYR   A CZ  1 
ATOM   449  O  OH  . TYR   A 1 57  ? 7.997  0.727   22.263 1.00 26.48  ? 63  TYR   A OH  1 
ATOM   450  N  N   . TYR   A 1 58  ? 14.030 -1.374  19.593 1.00 23.11  ? 64  TYR   A N   1 
ATOM   451  C  CA  . TYR   A 1 58  ? 14.619 -1.511  20.923 1.00 23.81  ? 64  TYR   A CA  1 
ATOM   452  C  C   . TYR   A 1 58  ? 14.172 -0.365  21.805 1.00 25.64  ? 64  TYR   A C   1 
ATOM   453  O  O   . TYR   A 1 58  ? 14.346 0.800   21.440 1.00 26.27  ? 64  TYR   A O   1 
ATOM   454  C  CB  . TYR   A 1 58  ? 16.154 -1.558  20.833 1.00 23.72  ? 64  TYR   A CB  1 
ATOM   455  C  CG  . TYR   A 1 58  ? 16.769 -1.656  22.207 1.00 24.55  ? 64  TYR   A CG  1 
ATOM   456  C  CD1 . TYR   A 1 58  ? 16.486 -2.730  23.041 1.00 25.25  ? 64  TYR   A CD1 1 
ATOM   457  C  CD2 . TYR   A 1 58  ? 17.597 -0.653  22.690 1.00 26.10  ? 64  TYR   A CD2 1 
ATOM   458  C  CE1 . TYR   A 1 58  ? 17.051 -2.825  24.313 1.00 26.46  ? 64  TYR   A CE1 1 
ATOM   459  C  CE2 . TYR   A 1 58  ? 18.167 -0.736  23.957 1.00 27.35  ? 64  TYR   A CE2 1 
ATOM   460  C  CZ  . TYR   A 1 58  ? 17.856 -1.803  24.779 1.00 28.25  ? 64  TYR   A CZ  1 
ATOM   461  O  OH  . TYR   A 1 58  ? 18.407 -1.876  26.031 1.00 30.82  ? 64  TYR   A OH  1 
ATOM   462  N  N   . CYS   A 1 59  ? 13.705 -0.683  23.025 1.00 26.52  ? 65  CYS   A N   1 
ATOM   463  C  CA  . CYS   A 1 59  ? 13.280 0.310   23.988 1.00 26.73  ? 65  CYS   A CA  1 
ATOM   464  C  C   . CYS   A 1 59  ? 14.210 0.197   25.200 1.00 26.69  ? 65  CYS   A C   1 
ATOM   465  O  O   . CYS   A 1 59  ? 14.107 -0.754  25.966 1.00 27.12  ? 65  CYS   A O   1 
ATOM   466  C  CB  . CYS   A 1 59  ? 11.818 0.082   24.362 1.00 27.49  ? 65  CYS   A CB  1 
ATOM   467  S  SG  . CYS   A 1 59  ? 11.223 1.103   25.732 1.00 29.80  ? 65  CYS   A SG  1 
ATOM   468  N  N   . SER   A 1 60  ? 15.143 1.145   25.346 1.00 25.98  ? 66  SER   A N   1 
ATOM   469  C  CA  . SER   A 1 60  ? 16.125 1.082   26.426 1.00 26.83  ? 66  SER   A CA  1 
ATOM   470  C  C   . SER   A 1 60  ? 15.521 1.274   27.804 1.00 27.80  ? 66  SER   A C   1 
ATOM   471  O  O   . SER   A 1 60  ? 16.023 0.673   28.751 1.00 28.85  ? 66  SER   A O   1 
ATOM   472  C  CB  . SER   A 1 60  ? 17.281 2.047   26.191 1.00 30.14  ? 66  SER   A CB  1 
ATOM   473  O  OG  . SER   A 1 60  ? 16.911 3.409   26.300 1.00 33.28  ? 66  SER   A OG  1 
ATOM   474  N  N   . SER   A 1 61  ? 14.409 2.046   27.917 1.00 28.49  ? 67  SER   A N   1 
ATOM   475  C  CA  . SER   A 1 61  ? 13.713 2.244   29.206 1.00 28.82  ? 67  SER   A CA  1 
ATOM   476  C  C   . SER   A 1 61  ? 13.016 0.971   29.741 1.00 29.16  ? 67  SER   A C   1 
ATOM   477  O  O   . SER   A 1 61  ? 12.633 0.920   30.928 1.00 30.02  ? 67  SER   A O   1 
ATOM   478  C  CB  . SER   A 1 61  ? 12.734 3.421   29.143 1.00 29.22  ? 67  SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 61  ? 11.650 3.224   28.248 1.00 29.32  ? 67  SER   A OG  1 
ATOM   480  N  N   . ARG   A 1 62  ? 12.939 -0.063  28.927 1.00 27.99  ? 68  ARG   A N   1 
ATOM   481  C  CA  . ARG   A 1 62  ? 12.419 -1.356  29.347 1.00 28.79  ? 68  ARG   A CA  1 
ATOM   482  C  C   . ARG   A 1 62  ? 13.427 -2.488  29.129 1.00 29.49  ? 68  ARG   A C   1 
ATOM   483  O  O   . ARG   A 1 62  ? 13.084 -3.634  29.396 1.00 29.12  ? 68  ARG   A O   1 
ATOM   484  C  CB  . ARG   A 1 62  ? 11.122 -1.684  28.568 1.00 29.58  ? 68  ARG   A CB  1 
ATOM   485  C  CG  . ARG   A 1 62  ? 9.954  -0.752  28.876 1.00 31.63  ? 68  ARG   A CG  1 
ATOM   486  C  CD  . ARG   A 1 62  ? 9.443  -1.015  30.288 1.00 35.42  ? 68  ARG   A CD  1 
ATOM   487  N  NE  . ARG   A 1 62  ? 8.280  -0.180  30.610 1.00 37.80  ? 68  ARG   A NE  1 
ATOM   488  C  CZ  . ARG   A 1 62  ? 8.356  1.029   31.154 1.00 39.35  ? 68  ARG   A CZ  1 
ATOM   489  N  NH1 . ARG   A 1 62  ? 9.538  1.557   31.455 1.00 38.34  ? 68  ARG   A NH1 1 
ATOM   490  N  NH2 . ARG   A 1 62  ? 7.252  1.724   31.397 1.00 40.22  ? 68  ARG   A NH2 1 
ATOM   491  N  N   . ARG   A 1 63  ? 14.615 -2.220  28.519 1.00 30.50  ? 69  ARG   A N   1 
ATOM   492  C  CA  . ARG   A 1 63  ? 15.602 -3.247  28.128 1.00 31.00  ? 69  ARG   A CA  1 
ATOM   493  C  C   . ARG   A 1 63  ? 14.881 -4.356  27.311 1.00 30.80  ? 69  ARG   A C   1 
ATOM   494  O  O   . ARG   A 1 63  ? 15.026 -5.527  27.632 1.00 31.48  ? 69  ARG   A O   1 
ATOM   495  C  CB  . ARG   A 1 63  ? 16.324 -3.836  29.362 1.00 33.01  ? 69  ARG   A CB  1 
ATOM   496  C  CG  . ARG   A 1 63  ? 17.291 -2.885  30.041 1.00 36.73  ? 69  ARG   A CG  1 
ATOM   497  C  CD  . ARG   A 1 63  ? 17.880 -3.508  31.307 1.00 39.30  ? 69  ARG   A CD  1 
ATOM   498  N  NE  . ARG   A 1 63  ? 18.704 -2.562  32.060 1.00 42.23  ? 69  ARG   A NE  1 
ATOM   499  C  CZ  . ARG   A 1 63  ? 18.698 -2.453  33.388 1.00 45.24  ? 69  ARG   A CZ  1 
ATOM   500  N  NH1 . ARG   A 1 63  ? 17.880 -3.202  34.118 1.00 45.75  ? 69  ARG   A NH1 1 
ATOM   501  N  NH2 . ARG   A 1 63  ? 19.479 -1.563  33.993 1.00 45.09  ? 69  ARG   A NH2 1 
ATOM   502  N  N   . LYS   A 1 64  ? 14.018 -3.967  26.332 1.00 29.78  ? 70  LYS   A N   1 
ATOM   503  C  CA  . LYS   A 1 64  ? 13.206 -4.933  25.589 1.00 28.50  ? 70  LYS   A CA  1 
ATOM   504  C  C   . LYS   A 1 64  ? 13.058 -4.558  24.140 1.00 26.08  ? 70  LYS   A C   1 
ATOM   505  O  O   . LYS   A 1 64  ? 13.074 -3.374  23.789 1.00 26.19  ? 70  LYS   A O   1 
ATOM   506  C  CB  . LYS   A 1 64  ? 11.795 -5.045  26.206 1.00 33.47  ? 70  LYS   A CB  1 
ATOM   507  C  CG  . LYS   A 1 64  ? 11.718 -6.038  27.360 1.00 41.72  ? 70  LYS   A CG  1 
ATOM   508  C  CD  . LYS   A 1 64  ? 10.431 -5.892  28.153 1.00 48.84  ? 70  LYS   A CD  1 
ATOM   509  C  CE  . LYS   A 1 64  ? 10.569 -6.456  29.551 1.00 54.31  ? 70  LYS   A CE  1 
ATOM   510  N  NZ  . LYS   A 1 64  ? 11.409 -5.586  30.428 1.00 57.00  ? 70  LYS   A NZ  1 
ATOM   511  N  N   . HIS   A 1 65  ? 12.881 -5.560  23.312 1.00 23.91  ? 71  HIS   A N   1 
ATOM   512  C  CA  . HIS   A 1 65  ? 12.653 -5.377  21.869 1.00 23.38  ? 71  HIS   A CA  1 
ATOM   513  C  C   . HIS   A 1 65  ? 11.163 -5.687  21.603 1.00 24.77  ? 71  HIS   A C   1 
ATOM   514  O  O   . HIS   A 1 65  ? 10.711 -6.831  21.802 1.00 25.82  ? 71  HIS   A O   1 
ATOM   515  C  CB  . HIS   A 1 65  ? 13.565 -6.323  21.081 1.00 24.96  ? 71  HIS   A CB  1 
ATOM   516  C  CG  . HIS   A 1 65  ? 15.030 -6.117  21.355 1.00 25.78  ? 71  HIS   A CG  1 
ATOM   517  N  ND1 . HIS   A 1 65  ? 15.857 -5.501  20.425 1.00 27.24  ? 71  HIS   A ND1 1 
ATOM   518  C  CD2 . HIS   A 1 65  ? 15.753 -6.400  22.468 1.00 25.76  ? 71  HIS   A CD2 1 
ATOM   519  C  CE1 . HIS   A 1 65  ? 17.064 -5.481  20.971 1.00 27.31  ? 71  HIS   A CE1 1 
ATOM   520  N  NE2 . HIS   A 1 65  ? 17.054 -5.997  22.210 1.00 27.29  ? 71  HIS   A NE2 1 
ATOM   521  N  N   . TYR   A 1 66  ? 10.395 -4.678  21.166 1.00 23.47  ? 72  TYR   A N   1 
ATOM   522  C  CA  . TYR   A 1 66  ? 8.951  -4.863  20.978 1.00 23.30  ? 72  TYR   A CA  1 
ATOM   523  C  C   . TYR   A 1 66  ? 8.554  -5.016  19.511 1.00 24.13  ? 72  TYR   A C   1 
ATOM   524  O  O   . TYR   A 1 66  ? 8.886  -4.163  18.704 1.00 23.88  ? 72  TYR   A O   1 
ATOM   525  C  CB  . TYR   A 1 66  ? 8.206  -3.649  21.555 1.00 22.95  ? 72  TYR   A CB  1 
ATOM   526  C  CG  . TYR   A 1 66  ? 8.280  -3.527  23.069 1.00 22.74  ? 72  TYR   A CG  1 
ATOM   527  C  CD1 . TYR   A 1 66  ? 7.471  -4.301  23.884 1.00 24.89  ? 72  TYR   A CD1 1 
ATOM   528  C  CD2 . TYR   A 1 66  ? 9.039  -2.535  23.668 1.00 23.11  ? 72  TYR   A CD2 1 
ATOM   529  C  CE1 . TYR   A 1 66  ? 7.522  -4.188  25.270 1.00 26.31  ? 72  TYR   A CE1 1 
ATOM   530  C  CE2 . TYR   A 1 66  ? 9.047  -2.364  25.054 1.00 24.48  ? 72  TYR   A CE2 1 
ATOM   531  C  CZ  . TYR   A 1 66  ? 8.290  -3.200  25.850 1.00 26.65  ? 72  TYR   A CZ  1 
ATOM   532  O  OH  . TYR   A 1 66  ? 8.305  -3.075  27.229 1.00 28.47  ? 72  TYR   A OH  1 
ATOM   533  N  N   . PRO   A 1 67  ? 7.744  -6.029  19.176 1.00 25.25  ? 73  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 67  ? 7.223  -6.109  17.793 1.00 25.92  ? 73  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 67  ? 6.078  -5.081  17.640 1.00 25.85  ? 73  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 67  ? 5.209  -5.006  18.520 1.00 26.58  ? 73  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 67  ? 6.732  -7.564  17.662 1.00 27.12  ? 73  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 67  ? 6.507  -8.032  19.081 1.00 28.03  ? 73  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 67  ? 7.232  -7.114  20.049 1.00 25.55  ? 73  PRO   A CD  1 
ATOM   540  N  N   . VAL   A 1 68  ? 6.072  -4.305  16.546 1.00 25.01  ? 74  VAL   A N   1 
ATOM   541  C  CA  . VAL   A 1 68  ? 5.064  -3.265  16.333 1.00 25.67  ? 74  VAL   A CA  1 
ATOM   542  C  C   . VAL   A 1 68  ? 4.607  -3.174  14.879 1.00 25.70  ? 74  VAL   A C   1 
ATOM   543  O  O   . VAL   A 1 68  ? 5.332  -3.562  13.955 1.00 25.16  ? 74  VAL   A O   1 
ATOM   544  C  CB  . VAL   A 1 68  ? 5.619  -1.863  16.736 1.00 26.33  ? 74  VAL   A CB  1 
ATOM   545  C  CG1 . VAL   A 1 68  ? 5.658  -1.690  18.261 1.00 27.26  ? 74  VAL   A CG1 1 
ATOM   546  C  CG2 . VAL   A 1 68  ? 6.983  -1.593  16.092 1.00 26.33  ? 74  VAL   A CG2 1 
ATOM   547  N  N   . SER   A 1 69  ? 3.413  -2.574  14.705 1.00 25.50  ? 75  SER   A N   1 
ATOM   548  C  CA  . SER   A 1 69  ? 2.846  -2.135  13.436 1.00 26.67  ? 75  SER   A CA  1 
ATOM   549  C  C   . SER   A 1 69  ? 3.096  -0.614  13.476 1.00 25.94  ? 75  SER   A C   1 
ATOM   550  O  O   . SER   A 1 69  ? 2.908  -0.009  14.531 1.00 26.70  ? 75  SER   A O   1 
ATOM   551  C  CB  . SER   A 1 69  ? 1.333  -2.354  13.429 1.00 29.99  ? 75  SER   A CB  1 
ATOM   552  O  OG  . SER   A 1 69  ? 1.058  -3.653  12.943 1.00 35.65  ? 75  SER   A OG  1 
ATOM   553  N  N   . PHE   A 1 70  ? 3.503  -0.005  12.375 1.00 23.85  ? 76  PHE   A N   1 
ATOM   554  C  CA  . PHE   A 1 70  ? 3.770  1.446   12.361 1.00 24.69  ? 76  PHE   A CA  1 
ATOM   555  C  C   . PHE   A 1 70  ? 3.208  2.102   11.101 1.00 27.03  ? 76  PHE   A C   1 
ATOM   556  O  O   . PHE   A 1 70  ? 3.075  1.442   10.077 1.00 27.57  ? 76  PHE   A O   1 
ATOM   557  C  CB  . PHE   A 1 70  ? 5.293  1.768   12.545 1.00 24.36  ? 76  PHE   A CB  1 
ATOM   558  C  CG  . PHE   A 1 70  ? 6.235  1.013   11.643 1.00 25.26  ? 76  PHE   A CG  1 
ATOM   559  C  CD1 . PHE   A 1 70  ? 6.674  -0.258  11.979 1.00 26.67  ? 76  PHE   A CD1 1 
ATOM   560  C  CD2 . PHE   A 1 70  ? 6.648  1.555   10.436 1.00 26.81  ? 76  PHE   A CD2 1 
ATOM   561  C  CE1 . PHE   A 1 70  ? 7.556  -0.943  11.154 1.00 27.95  ? 76  PHE   A CE1 1 
ATOM   562  C  CE2 . PHE   A 1 70  ? 7.513  0.858   9.598  1.00 27.37  ? 76  PHE   A CE2 1 
ATOM   563  C  CZ  . PHE   A 1 70  ? 7.961  -0.388  9.960  1.00 27.40  ? 76  PHE   A CZ  1 
ATOM   564  N  N   . SER   A 1 71  ? 2.875  3.411   11.169 1.00 28.09  ? 77  SER   A N   1 
ATOM   565  C  CA  . SER   A 1 71  ? 2.317  4.101   10.012 1.00 29.50  ? 77  SER   A CA  1 
ATOM   566  C  C   . SER   A 1 71  ? 3.408  4.468   8.973  1.00 30.70  ? 77  SER   A C   1 
ATOM   567  O  O   . SER   A 1 71  ? 4.588  4.401   9.290  1.00 30.99  ? 77  SER   A O   1 
ATOM   568  C  CB  . SER   A 1 71  ? 1.566  5.353   10.476 1.00 31.41  ? 77  SER   A CB  1 
ATOM   569  O  OG  . SER   A 1 71  ? 2.434  6.192   11.222 1.00 32.77  ? 77  SER   A OG  1 
ATOM   570  N  N   . LYS   A 1 72  ? 3.023  4.830   7.730  1.00 31.58  ? 78  LYS   A N   1 
ATOM   571  C  CA  . LYS   A 1 72  ? 4.002  5.208   6.711  1.00 32.46  ? 78  LYS   A CA  1 
ATOM   572  C  C   . LYS   A 1 72  ? 4.566  6.631   7.003  1.00 32.92  ? 78  LYS   A C   1 
ATOM   573  O  O   . LYS   A 1 72  ? 3.882  7.461   7.616  1.00 33.14  ? 78  LYS   A O   1 
ATOM   574  C  CB  . LYS   A 1 72  ? 3.375  5.113   5.282  1.00 34.68  ? 78  LYS   A CB  1 
ATOM   575  C  CG  . LYS   A 1 72  ? 3.040  3.673   4.861  1.00 38.17  ? 78  LYS   A CG  1 
ATOM   576  C  CD  . LYS   A 1 72  ? 2.575  3.575   3.407  1.00 43.64  ? 78  LYS   A CD  1 
ATOM   577  C  CE  . LYS   A 1 72  ? 2.582  2.138   2.938  1.00 47.65  ? 78  LYS   A CE  1 
ATOM   578  N  NZ  . LYS   A 1 72  ? 1.933  1.982   1.604  1.00 50.55  ? 78  LYS   A NZ  1 
ATOM   579  N  N   . PRO   A 1 73  ? 5.810  6.918   6.592  1.00 32.61  ? 79  PRO   A N   1 
ATOM   580  C  CA  . PRO   A 1 73  ? 6.407  8.234   6.904  1.00 33.06  ? 79  PRO   A CA  1 
ATOM   581  C  C   . PRO   A 1 73  ? 5.548  9.423   6.497  1.00 33.10  ? 79  PRO   A C   1 
ATOM   582  O  O   . PRO   A 1 73  ? 5.116  9.519   5.337  1.00 33.14  ? 79  PRO   A O   1 
ATOM   583  C  CB  . PRO   A 1 73  ? 7.760  8.197   6.197  1.00 34.18  ? 79  PRO   A CB  1 
ATOM   584  C  CG  . PRO   A 1 73  ? 8.074  6.738   6.045  1.00 34.76  ? 79  PRO   A CG  1 
ATOM   585  C  CD  . PRO   A 1 73  ? 6.752  6.047   5.866  1.00 32.77  ? 79  PRO   A CD  1 
ATOM   586  N  N   A SER   A 1 74  ? 5.261  10.314  7.449  0.50 33.15  ? 80  SER   A N   1 
ATOM   587  N  N   B SER   A 1 74  ? 5.236  10.297  7.458  0.50 33.30  ? 80  SER   A N   1 
ATOM   588  C  CA  A SER   A 1 74  ? 4.390  11.459  7.161  0.50 34.14  ? 80  SER   A CA  1 
ATOM   589  C  CA  B SER   A 1 74  ? 4.346  11.432  7.191  0.50 34.44  ? 80  SER   A CA  1 
ATOM   590  C  C   A SER   A 1 74  ? 4.757  12.717  7.963  0.50 34.84  ? 80  SER   A C   1 
ATOM   591  C  C   B SER   A 1 74  ? 4.750  12.706  7.964  0.50 34.98  ? 80  SER   A C   1 
ATOM   592  O  O   A SER   A 1 74  ? 5.642  12.675  8.823  0.50 34.91  ? 80  SER   A O   1 
ATOM   593  O  O   B SER   A 1 74  ? 5.642  12.661  8.817  0.50 35.05  ? 80  SER   A O   1 
ATOM   594  C  CB  A SER   A 1 74  ? 2.925  11.071  7.378  0.50 35.49  ? 80  SER   A CB  1 
ATOM   595  C  CB  B SER   A 1 74  ? 2.902  11.050  7.538  0.50 36.13  ? 80  SER   A CB  1 
ATOM   596  O  OG  A SER   A 1 74  ? 2.676  10.793  8.745  0.50 37.14  ? 80  SER   A OG  1 
ATOM   597  O  OG  B SER   A 1 74  ? 2.509  9.805   6.983  0.50 38.45  ? 80  SER   A OG  1 
ATOM   598  N  N   . LEU   A 1 75  ? 4.086  13.842  7.668  1.00 35.09  ? 81  LEU   A N   1 
ATOM   599  C  CA  . LEU   A 1 75  ? 4.336  15.104  8.357  1.00 36.09  ? 81  LEU   A CA  1 
ATOM   600  C  C   . LEU   A 1 75  ? 3.404  15.117  9.605  1.00 36.12  ? 81  LEU   A C   1 
ATOM   601  O  O   . LEU   A 1 75  ? 2.181  15.074  9.461  1.00 35.70  ? 81  LEU   A O   1 
ATOM   602  C  CB  . LEU   A 1 75  ? 3.999  16.240  7.386  1.00 36.62  ? 81  LEU   A CB  1 
ATOM   603  C  CG  . LEU   A 1 75  ? 4.377  17.636  7.805  1.00 39.56  ? 81  LEU   A CG  1 
ATOM   604  C  CD1 . LEU   A 1 75  ? 5.874  17.773  7.987  1.00 39.16  ? 81  LEU   A CD1 1 
ATOM   605  C  CD2 . LEU   A 1 75  ? 3.851  18.655  6.815  1.00 41.13  ? 81  LEU   A CD2 1 
ATOM   606  N  N   . ILE   A 1 76  ? 3.981  15.119  10.816 1.00 36.44  ? 82  ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 76  ? 3.216  15.012  12.067 1.00 37.32  ? 82  ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 76  ? 3.520  16.153  13.039 1.00 37.38  ? 82  ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 76  ? 4.687  16.489  13.211 1.00 36.52  ? 82  ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 76  ? 3.563  13.646  12.750 1.00 38.64  ? 82  ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 76  ? 3.144  12.430  11.892 1.00 40.45  ? 82  ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 76  ? 3.022  13.532  14.182 1.00 39.09  ? 82  ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 76  ? 1.744  12.270  11.688 1.00 42.75  ? 82  ILE   A CD1 1 
ATOM   614  N  N   . PHE   A 1 77  ? 2.489  16.701  13.733 1.00 37.59  ? 83  PHE   A N   1 
ATOM   615  C  CA  . PHE   A 1 77  ? 2.718  17.752  14.729 1.00 38.28  ? 83  PHE   A CA  1 
ATOM   616  C  C   . PHE   A 1 77  ? 3.379  17.157  15.987 1.00 37.78  ? 83  PHE   A C   1 
ATOM   617  O  O   . PHE   A 1 77  ? 2.890  16.174  16.554 1.00 37.30  ? 83  PHE   A O   1 
ATOM   618  C  CB  . PHE   A 1 77  ? 1.424  18.497  15.118 1.00 39.09  ? 83  PHE   A CB  1 
ATOM   619  C  CG  . PHE   A 1 77  ? 1.765  19.786  15.827 1.00 40.94  ? 83  PHE   A CG  1 
ATOM   620  C  CD1 . PHE   A 1 77  ? 2.389  20.820  15.153 1.00 42.77  ? 83  PHE   A CD1 1 
ATOM   621  C  CD2 . PHE   A 1 77  ? 1.531  19.933  17.183 1.00 42.30  ? 83  PHE   A CD2 1 
ATOM   622  C  CE1 . PHE   A 1 77  ? 2.736  21.991  15.811 1.00 44.21  ? 83  PHE   A CE1 1 
ATOM   623  C  CE2 . PHE   A 1 77  ? 1.856  21.112  17.833 1.00 43.47  ? 83  PHE   A CE2 1 
ATOM   624  C  CZ  . PHE   A 1 77  ? 2.439  22.138  17.144 1.00 43.99  ? 83  PHE   A CZ  1 
ATOM   625  N  N   . VAL   A 1 78  ? 4.511  17.743  16.400 1.00 37.05  ? 84  VAL   A N   1 
ATOM   626  C  CA  . VAL   A 1 78  ? 5.257  17.275  17.558 1.00 37.11  ? 84  VAL   A CA  1 
ATOM   627  C  C   . VAL   A 1 78  ? 5.308  18.365  18.624 1.00 38.03  ? 84  VAL   A C   1 
ATOM   628  O  O   . VAL   A 1 78  ? 5.773  19.464  18.346 1.00 38.51  ? 84  VAL   A O   1 
ATOM   629  C  CB  . VAL   A 1 78  ? 6.679  16.843  17.104 1.00 36.83  ? 84  VAL   A CB  1 
ATOM   630  C  CG1 . VAL   A 1 78  ? 7.567  16.511  18.297 1.00 37.38  ? 84  VAL   A CG1 1 
ATOM   631  C  CG2 . VAL   A 1 78  ? 6.611  15.666  16.139 1.00 36.24  ? 84  VAL   A CG2 1 
ATOM   632  N  N   . GLU   A 1 79  ? 4.856  18.061  19.854 1.00 38.63  ? 85  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 79  ? 4.862  19.022  20.962 1.00 39.37  ? 85  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 79  ? 6.257  19.575  21.294 1.00 39.95  ? 85  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 79  ? 7.257  18.929  20.988 1.00 39.77  ? 85  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 79  ? 4.252  18.375  22.213 1.00 41.47  ? 85  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 79  ? 2.754  18.201  22.119 1.00 47.39  ? 85  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 79  ? 2.036  19.521  21.919 1.00 54.76  ? 85  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 79  ? 2.181  20.412  22.784 1.00 55.15  ? 85  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 79  ? 1.372  19.683  20.870 1.00 57.95  ? 85  GLU   A OE2 1 
ATOM   641  N  N   . ALA   A 1 80  ? 6.326  20.753  21.937 1.00 40.24  ? 86  ALA   A N   1 
ATOM   642  C  CA  . ALA   A 1 80  ? 7.611  21.332  22.313 1.00 41.54  ? 86  ALA   A CA  1 
ATOM   643  C  C   . ALA   A 1 80  ? 8.331  20.481  23.364 1.00 41.83  ? 86  ALA   A C   1 
ATOM   644  O  O   . ALA   A 1 80  ? 7.695  19.776  24.162 1.00 41.99  ? 86  ALA   A O   1 
ATOM   645  C  CB  . ALA   A 1 80  ? 7.434  22.762  22.825 1.00 41.84  ? 86  ALA   A CB  1 
ATOM   646  N  N   . SER   A 1 81  ? 9.664  20.537  23.330 1.00 41.22  ? 87  SER   A N   1 
ATOM   647  C  CA  . SER   A 1 81  ? 10.570 19.850  24.244 1.00 41.23  ? 87  SER   A CA  1 
ATOM   648  C  C   . SER   A 1 81  ? 11.809 20.752  24.501 1.00 42.42  ? 87  SER   A C   1 
ATOM   649  O  O   . SER   A 1 81  ? 11.885 21.850  23.941 1.00 42.81  ? 87  SER   A O   1 
ATOM   650  C  CB  . SER   A 1 81  ? 10.985 18.500  23.661 1.00 41.17  ? 87  SER   A CB  1 
ATOM   651  O  OG  . SER   A 1 81  ? 11.848 18.647  22.544 1.00 42.34  ? 87  SER   A OG  1 
ATOM   652  N  N   . GLU   A 1 82  ? 12.784 20.304  25.325 1.00 42.73  ? 88  GLU   A N   1 
ATOM   653  C  CA  . GLU   A 1 82  ? 13.995 21.103  25.550 1.00 43.53  ? 88  GLU   A CA  1 
ATOM   654  C  C   . GLU   A 1 82  ? 14.871 21.228  24.283 1.00 43.27  ? 88  GLU   A C   1 
ATOM   655  O  O   . GLU   A 1 82  ? 15.755 22.087  24.246 1.00 43.68  ? 88  GLU   A O   1 
ATOM   656  C  CB  . GLU   A 1 82  ? 14.812 20.601  26.759 1.00 46.73  ? 88  GLU   A CB  1 
ATOM   657  C  CG  . GLU   A 1 82  ? 15.659 19.363  26.491 1.00 52.91  ? 88  GLU   A CG  1 
ATOM   658  C  CD  . GLU   A 1 82  ? 16.590 18.944  27.620 1.00 60.36  ? 88  GLU   A CD  1 
ATOM   659  O  OE1 . GLU   A 1 82  ? 16.187 18.075  28.426 1.00 61.46  ? 88  GLU   A OE1 1 
ATOM   660  O  OE2 . GLU   A 1 82  ? 17.721 19.480  27.698 1.00 62.23  ? 88  GLU   A OE2 1 
ATOM   661  N  N   . TYR   A 1 83  ? 14.588 20.432  23.225 1.00 42.33  ? 89  TYR   A N   1 
ATOM   662  C  CA  . TYR   A 1 83  ? 15.382 20.441  21.999 1.00 41.94  ? 89  TYR   A CA  1 
ATOM   663  C  C   . TYR   A 1 83  ? 14.775 21.192  20.815 1.00 40.92  ? 89  TYR   A C   1 
ATOM   664  O  O   . TYR   A 1 83  ? 15.523 21.668  19.963 1.00 41.02  ? 89  TYR   A O   1 
ATOM   665  C  CB  . TYR   A 1 83  ? 15.716 19.008  21.592 1.00 42.35  ? 89  TYR   A CB  1 
ATOM   666  C  CG  . TYR   A 1 83  ? 16.629 18.349  22.596 1.00 43.78  ? 89  TYR   A CG  1 
ATOM   667  C  CD1 . TYR   A 1 83  ? 17.966 18.714  22.692 1.00 44.78  ? 89  TYR   A CD1 1 
ATOM   668  C  CD2 . TYR   A 1 83  ? 16.143 17.406  23.494 1.00 45.21  ? 89  TYR   A CD2 1 
ATOM   669  C  CE1 . TYR   A 1 83  ? 18.812 18.117  23.617 1.00 46.14  ? 89  TYR   A CE1 1 
ATOM   670  C  CE2 . TYR   A 1 83  ? 16.983 16.794  24.419 1.00 46.45  ? 89  TYR   A CE2 1 
ATOM   671  C  CZ  . TYR   A 1 83  ? 18.315 17.163  24.488 1.00 47.74  ? 89  TYR   A CZ  1 
ATOM   672  O  OH  . TYR   A 1 83  ? 19.153 16.579  25.412 1.00 50.10  ? 89  TYR   A OH  1 
ATOM   673  N  N   . TYR   A 1 84  ? 13.449 21.268  20.724 1.00 39.83  ? 90  TYR   A N   1 
ATOM   674  C  CA  . TYR   A 1 84  ? 12.789 21.972  19.621 1.00 39.21  ? 90  TYR   A CA  1 
ATOM   675  C  C   . TYR   A 1 84  ? 11.539 22.663  20.113 1.00 40.95  ? 90  TYR   A C   1 
ATOM   676  O  O   . TYR   A 1 84  ? 10.824 22.097  20.948 1.00 41.45  ? 90  TYR   A O   1 
ATOM   677  C  CB  . TYR   A 1 84  ? 12.301 20.989  18.530 1.00 37.38  ? 90  TYR   A CB  1 
ATOM   678  C  CG  . TYR   A 1 84  ? 13.358 20.150  17.859 1.00 35.44  ? 90  TYR   A CG  1 
ATOM   679  C  CD1 . TYR   A 1 84  ? 14.173 20.682  16.870 1.00 35.00  ? 90  TYR   A CD1 1 
ATOM   680  C  CD2 . TYR   A 1 84  ? 13.543 18.820  18.209 1.00 35.10  ? 90  TYR   A CD2 1 
ATOM   681  C  CE1 . TYR   A 1 84  ? 15.122 19.907  16.229 1.00 34.23  ? 90  TYR   A CE1 1 
ATOM   682  C  CE2 . TYR   A 1 84  ? 14.498 18.039  17.582 1.00 34.75  ? 90  TYR   A CE2 1 
ATOM   683  C  CZ  . TYR   A 1 84  ? 15.276 18.583  16.581 1.00 34.21  ? 90  TYR   A CZ  1 
ATOM   684  O  OH  . TYR   A 1 84  ? 16.249 17.834  15.970 1.00 33.27  ? 90  TYR   A OH  1 
ATOM   685  N  N   . PRO   A 1 85  ? 11.157 23.814  19.519 1.00 41.79  ? 91  PRO   A N   1 
ATOM   686  C  CA  . PRO   A 1 85  ? 9.816  24.358  19.814 1.00 42.01  ? 91  PRO   A CA  1 
ATOM   687  C  C   . PRO   A 1 85  ? 8.754  23.454  19.149 1.00 41.67  ? 91  PRO   A C   1 
ATOM   688  O  O   . PRO   A 1 85  ? 9.108  22.505  18.410 1.00 41.41  ? 91  PRO   A O   1 
ATOM   689  C  CB  . PRO   A 1 85  ? 9.858  25.749  19.162 1.00 42.79  ? 91  PRO   A CB  1 
ATOM   690  C  CG  . PRO   A 1 85  ? 10.755 25.564  17.994 1.00 43.17  ? 91  PRO   A CG  1 
ATOM   691  C  CD  . PRO   A 1 85  ? 11.827 24.583  18.447 1.00 41.77  ? 91  PRO   A CD  1 
ATOM   692  N  N   . ALA   A 1 86  ? 7.454  23.724  19.393 1.00 40.95  ? 92  ALA   A N   1 
ATOM   693  C  CA  . ALA   A 1 86  ? 6.392  22.915  18.787 1.00 41.26  ? 92  ALA   A CA  1 
ATOM   694  C  C   . ALA   A 1 86  ? 6.425  23.107  17.272 1.00 41.38  ? 92  ALA   A C   1 
ATOM   695  O  O   . ALA   A 1 86  ? 6.519  24.235  16.811 1.00 41.66  ? 92  ALA   A O   1 
ATOM   696  C  CB  . ALA   A 1 86  ? 5.044  23.304  19.349 1.00 41.92  ? 92  ALA   A CB  1 
ATOM   697  N  N   . ARG   A 1 87  ? 6.490  22.009  16.504 1.00 40.69  ? 93  ARG   A N   1 
ATOM   698  C  CA  . ARG   A 1 87  ? 6.629  22.107  15.045 1.00 39.88  ? 93  ARG   A CA  1 
ATOM   699  C  C   . ARG   A 1 87  ? 6.089  20.845  14.345 1.00 39.16  ? 93  ARG   A C   1 
ATOM   700  O  O   . ARG   A 1 87  ? 5.757  19.884  15.031 1.00 40.25  ? 93  ARG   A O   1 
ATOM   701  C  CB  . ARG   A 1 87  ? 8.135  22.299  14.708 1.00 39.96  ? 93  ARG   A CB  1 
ATOM   702  C  CG  . ARG   A 1 87  ? 8.943  20.979  14.676 1.00 40.46  ? 93  ARG   A CG  1 
ATOM   703  C  CD  . ARG   A 1 87  ? 10.333 21.055  15.253 1.00 40.33  ? 93  ARG   A CD  1 
ATOM   704  N  NE  . ARG   A 1 87  ? 11.207 19.995  14.733 1.00 39.45  ? 93  ARG   A NE  1 
ATOM   705  C  CZ  . ARG   A 1 87  ? 11.221 18.740  15.183 1.00 38.43  ? 93  ARG   A CZ  1 
ATOM   706  N  NH1 . ARG   A 1 87  ? 10.404 18.369  16.165 1.00 35.78  ? 93  ARG   A NH1 1 
ATOM   707  N  NH2 . ARG   A 1 87  ? 12.052 17.849  14.656 1.00 35.96  ? 93  ARG   A NH2 1 
ATOM   708  N  N   . TYR   A 1 88  ? 6.066  20.814  12.989 1.00 37.04  ? 94  TYR   A N   1 
ATOM   709  C  CA  . TYR   A 1 88  ? 5.740  19.588  12.283 1.00 36.23  ? 94  TYR   A CA  1 
ATOM   710  C  C   . TYR   A 1 88  ? 7.080  18.876  11.965 1.00 34.16  ? 94  TYR   A C   1 
ATOM   711  O  O   . TYR   A 1 88  ? 8.041  19.511  11.507 1.00 34.75  ? 94  TYR   A O   1 
ATOM   712  C  CB  . TYR   A 1 88  ? 4.996  19.866  10.982 1.00 37.06  ? 94  TYR   A CB  1 
ATOM   713  C  CG  . TYR   A 1 88  ? 3.569  20.305  11.200 1.00 38.92  ? 94  TYR   A CG  1 
ATOM   714  C  CD1 . TYR   A 1 88  ? 2.542  19.379  11.275 1.00 40.19  ? 94  TYR   A CD1 1 
ATOM   715  C  CD2 . TYR   A 1 88  ? 3.250  21.647  11.348 1.00 40.26  ? 94  TYR   A CD2 1 
ATOM   716  C  CE1 . TYR   A 1 88  ? 1.227  19.776  11.465 1.00 41.67  ? 94  TYR   A CE1 1 
ATOM   717  C  CE2 . TYR   A 1 88  ? 1.938  22.058  11.540 1.00 41.23  ? 94  TYR   A CE2 1 
ATOM   718  C  CZ  . TYR   A 1 88  ? 0.927  21.119  11.599 1.00 42.76  ? 94  TYR   A CZ  1 
ATOM   719  O  OH  . TYR   A 1 88  ? -0.369 21.516  11.794 1.00 45.04  ? 94  TYR   A OH  1 
ATOM   720  N  N   . GLN   A 1 89  ? 7.146  17.573  12.220 1.00 31.94  ? 95  GLN   A N   1 
ATOM   721  C  CA  . GLN   A 1 89  ? 8.332  16.768  11.905 1.00 30.71  ? 95  GLN   A CA  1 
ATOM   722  C  C   . GLN   A 1 89  ? 7.966  15.898  10.700 1.00 30.34  ? 95  GLN   A C   1 
ATOM   723  O  O   . GLN   A 1 89  ? 6.932  15.214  10.726 1.00 30.13  ? 95  GLN   A O   1 
ATOM   724  C  CB  . GLN   A 1 89  ? 8.774  15.896  13.103 1.00 30.87  ? 95  GLN   A CB  1 
ATOM   725  C  CG  . GLN   A 1 89  ? 10.001 14.991  12.796 1.00 30.54  ? 95  GLN   A CG  1 
ATOM   726  C  CD  . GLN   A 1 89  ? 10.719 14.475  14.031 1.00 29.94  ? 95  GLN   A CD  1 
ATOM   727  O  OE1 . GLN   A 1 89  ? 10.909 15.180  15.009 1.00 29.01  ? 95  GLN   A OE1 1 
ATOM   728  N  NE2 . GLN   A 1 89  ? 11.139 13.210  14.004 1.00 31.06  ? 95  GLN   A NE2 1 
ATOM   729  N  N   . SER   A 1 90  ? 8.773  15.959  9.637  1.00 29.73  ? 96  SER   A N   1 
ATOM   730  C  CA  . SER   A 1 90  ? 8.521  15.197  8.420  1.00 30.13  ? 96  SER   A CA  1 
ATOM   731  C  C   . SER   A 1 90  ? 9.164  13.789  8.487  1.00 29.81  ? 96  SER   A C   1 
ATOM   732  O  O   . SER   A 1 90  ? 10.018 13.523  9.357  1.00 29.61  ? 96  SER   A O   1 
ATOM   733  C  CB  . SER   A 1 90  ? 9.035  15.967  7.203  1.00 31.15  ? 96  SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 90  ? 10.450 16.098  7.253  1.00 33.23  ? 96  SER   A OG  1 
ATOM   735  N  N   . HIS   A 1 91  ? 8.718  12.890  7.579  1.00 29.20  ? 97  HIS   A N   1 
ATOM   736  C  CA  . HIS   A 1 91  ? 9.229  11.513  7.462  1.00 29.33  ? 97  HIS   A CA  1 
ATOM   737  C  C   . HIS   A 1 91  ? 9.137  10.739  8.793  1.00 29.29  ? 97  HIS   A C   1 
ATOM   738  O  O   . HIS   A 1 91  ? 10.025 9.954   9.108  1.00 29.09  ? 97  HIS   A O   1 
ATOM   739  C  CB  . HIS   A 1 91  ? 10.680 11.552  6.934  1.00 29.73  ? 97  HIS   A CB  1 
ATOM   740  C  CG  . HIS   A 1 91  ? 10.799 12.226  5.597  1.00 31.93  ? 97  HIS   A CG  1 
ATOM   741  N  ND1 . HIS   A 1 91  ? 10.737 11.503  4.427  1.00 34.19  ? 97  HIS   A ND1 1 
ATOM   742  C  CD2 . HIS   A 1 91  ? 10.945 13.536  5.289  1.00 32.27  ? 97  HIS   A CD2 1 
ATOM   743  C  CE1 . HIS   A 1 91  ? 10.845 12.388  3.444  1.00 34.07  ? 97  HIS   A CE1 1 
ATOM   744  N  NE2 . HIS   A 1 91  ? 10.956 13.623  3.913  1.00 33.65  ? 97  HIS   A NE2 1 
ATOM   745  N  N   . LEU   A 1 92  ? 8.066  10.961  9.561  1.00 28.88  ? 98  LEU   A N   1 
ATOM   746  C  CA  . LEU   A 1 92  ? 7.887  10.334  10.870 1.00 29.07  ? 98  LEU   A CA  1 
ATOM   747  C  C   . LEU   A 1 92  ? 6.806  9.230   10.826 1.00 28.37  ? 98  LEU   A C   1 
ATOM   748  O  O   . LEU   A 1 92  ? 5.738  9.422   10.213 1.00 28.12  ? 98  LEU   A O   1 
ATOM   749  C  CB  . LEU   A 1 92  ? 7.489  11.414  11.870 1.00 29.84  ? 98  LEU   A CB  1 
ATOM   750  C  CG  . LEU   A 1 92  ? 7.346  11.019  13.343 1.00 31.16  ? 98  LEU   A CG  1 
ATOM   751  C  CD1 . LEU   A 1 92  ? 8.699  10.618  13.940 1.00 30.96  ? 98  LEU   A CD1 1 
ATOM   752  C  CD2 . LEU   A 1 92  ? 6.773  12.190  14.143 1.00 32.62  ? 98  LEU   A CD2 1 
ATOM   753  N  N   . MET   A 1 93  ? 7.087  8.091   11.489 1.00 27.02  ? 99  MET   A N   1 
ATOM   754  C  CA  . MET   A 1 93  ? 6.187  6.919   11.540 1.00 26.75  ? 99  MET   A CA  1 
ATOM   755  C  C   . MET   A 1 93  ? 5.778  6.656   12.988 1.00 26.06  ? 99  MET   A C   1 
ATOM   756  O  O   . MET   A 1 93  ? 6.665  6.638   13.837 1.00 25.95  ? 99  MET   A O   1 
ATOM   757  C  CB  . MET   A 1 93  ? 6.972  5.701   11.041 1.00 27.30  ? 99  MET   A CB  1 
ATOM   758  C  CG  . MET   A 1 93  ? 7.469  5.876   9.603  1.00 28.61  ? 99  MET   A CG  1 
ATOM   759  S  SD  . MET   A 1 93  ? 8.511  4.511   9.051  1.00 33.08  ? 99  MET   A SD  1 
ATOM   760  C  CE  . MET   A 1 93  ? 9.881  4.674   10.143 1.00 30.70  ? 99  MET   A CE  1 
ATOM   761  N  N   . LEU   A 1 94  ? 4.485  6.450   13.291 1.00 26.03  ? 100 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 94  ? 4.064  6.182   14.677 1.00 26.48  ? 100 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 94  ? 3.649  4.724   14.886 1.00 25.83  ? 100 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 94  ? 3.111  4.087   13.974 1.00 25.69  ? 100 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 94  ? 2.871  7.085   15.121 1.00 27.70  ? 100 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 94  ? 3.101  8.593   15.050 1.00 31.12  ? 100 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 94  ? 1.823  9.349   15.412 1.00 33.75  ? 100 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 94  ? 4.267  9.018   15.920 1.00 31.94  ? 100 LEU   A CD2 1 
ATOM   769  N  N   . ALA   A 1 95  ? 3.793  4.261   16.124 1.00 25.21  ? 101 ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 95  ? 3.357  2.946   16.572 1.00 25.35  ? 101 ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 95  ? 2.784  3.073   17.983 1.00 25.77  ? 101 ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 95  ? 3.103  4.030   18.692 1.00 25.68  ? 101 ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 95  ? 4.521  1.957   16.572 1.00 24.68  ? 101 ALA   A CB  1 
ATOM   774  N  N   . VAL   A 1 96  ? 1.928  2.126   18.377 1.00 24.79  ? 102 VAL   A N   1 
ATOM   775  C  CA  . VAL   A 1 96  ? 1.425  2.081   19.738 1.00 25.57  ? 102 VAL   A CA  1 
ATOM   776  C  C   . VAL   A 1 96  ? 2.503  1.332   20.550 1.00 27.47  ? 102 VAL   A C   1 
ATOM   777  O  O   . VAL   A 1 96  ? 2.772  0.145   20.318 1.00 28.01  ? 102 VAL   A O   1 
ATOM   778  C  CB  . VAL   A 1 96  ? 0.020  1.404   19.822 1.00 26.14  ? 102 VAL   A CB  1 
ATOM   779  C  CG1 . VAL   A 1 96  ? -0.432 1.235   21.273 1.00 26.56  ? 102 VAL   A CG1 1 
ATOM   780  C  CG2 . VAL   A 1 96  ? -1.024 2.211   19.035 1.00 26.28  ? 102 VAL   A CG2 1 
ATOM   781  N  N   . GLY   A 1 97  ? 3.158  2.045   21.441 1.00 28.51  ? 103 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 97  ? 4.222  1.469   22.249 1.00 29.59  ? 103 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 97  ? 4.824  2.429   23.247 1.00 29.75  ? 103 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 97  ? 4.593  3.648   23.180 1.00 29.46  ? 103 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 98  ? 5.618  1.877   24.178 1.00 28.85  ? 104 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 98  ? 6.213  2.699   25.216 1.00 29.21  ? 104 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 98  ? 7.503  3.354   24.758 1.00 28.75  ? 104 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 98  ? 8.299  2.737   24.076 1.00 28.54  ? 104 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 98  ? 6.476  1.885   26.499 1.00 30.39  ? 104 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 98  ? 7.149  2.689   27.576 1.00 33.67  ? 104 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 98  ? 6.467  3.665   28.278 1.00 36.17  ? 104 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 98  ? 8.447  2.701   27.963 1.00 35.34  ? 104 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 98  ? 7.357  4.221   29.085 1.00 36.85  ? 104 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 98  ? 8.563  3.676   28.929 1.00 36.57  ? 104 HIS   A NE2 1 
ATOM   795  N  N   . SER   A 1 99  ? 7.701  4.602   25.157 1.00 29.55  ? 105 SER   A N   1 
ATOM   796  C  CA  . SER   A 1 99  ? 8.935  5.329   24.920 1.00 30.52  ? 105 SER   A CA  1 
ATOM   797  C  C   . SER   A 1 99  ? 9.090  6.466   25.924 1.00 31.43  ? 105 SER   A C   1 
ATOM   798  O  O   . SER   A 1 99  ? 8.102  7.005   26.432 1.00 31.52  ? 105 SER   A O   1 
ATOM   799  C  CB  . SER   A 1 99  ? 9.009  5.864   23.495 1.00 31.38  ? 105 SER   A CB  1 
ATOM   800  O  OG  . SER   A 1 99  ? 8.258  7.054   23.362 1.00 33.73  ? 105 SER   A OG  1 
ATOM   801  N  N   . GLU   A 1 100 ? 10.354 6.813   26.218 1.00 30.89  ? 106 GLU   A N   1 
ATOM   802  C  CA  . GLU   A 1 100 ? 10.732 7.919   27.067 1.00 31.20  ? 106 GLU   A CA  1 
ATOM   803  C  C   . GLU   A 1 100 ? 11.806 8.737   26.321 1.00 31.29  ? 106 GLU   A C   1 
ATOM   804  O  O   . GLU   A 1 100 ? 12.455 8.193   25.419 1.00 31.56  ? 106 GLU   A O   1 
ATOM   805  C  CB  . GLU   A 1 100 ? 11.191 7.402   28.456 1.00 33.25  ? 106 GLU   A CB  1 
ATOM   806  C  CG  . GLU   A 1 100 ? 10.056 6.716   29.198 1.00 38.22  ? 106 GLU   A CG  1 
ATOM   807  C  CD  . GLU   A 1 100 ? 10.408 6.142   30.558 1.00 42.90  ? 106 GLU   A CD  1 
ATOM   808  O  OE1 . GLU   A 1 100 ? 11.260 6.744   31.242 1.00 43.01  ? 106 GLU   A OE1 1 
ATOM   809  O  OE2 . GLU   A 1 100 ? 9.840  5.094   30.940 1.00 44.20  ? 106 GLU   A OE2 1 
ATOM   810  N  N   . PRO   A 1 101 ? 12.028 10.035  26.633 1.00 31.24  ? 107 PRO   A N   1 
ATOM   811  C  CA  . PRO   A 1 101 ? 13.012 10.809  25.846 1.00 30.76  ? 107 PRO   A CA  1 
ATOM   812  C  C   . PRO   A 1 101 ? 14.373 10.116  25.605 1.00 30.60  ? 107 PRO   A C   1 
ATOM   813  O  O   . PRO   A 1 101 ? 14.875 10.106  24.473 1.00 30.31  ? 107 PRO   A O   1 
ATOM   814  C  CB  . PRO   A 1 101 ? 13.141 12.126  26.611 1.00 31.55  ? 107 PRO   A CB  1 
ATOM   815  C  CG  . PRO   A 1 101 ? 11.833 12.276  27.356 1.00 32.17  ? 107 PRO   A CG  1 
ATOM   816  C  CD  . PRO   A 1 101 ? 11.342 10.870  27.647 1.00 30.99  ? 107 PRO   A CD  1 
ATOM   817  N  N   . GLY   A 1 102 ? 14.928 9.484   26.634 1.00 30.76  ? 108 GLY   A N   1 
ATOM   818  C  CA  . GLY   A 1 102 ? 16.218 8.796   26.533 1.00 31.28  ? 108 GLY   A CA  1 
ATOM   819  C  C   . GLY   A 1 102 ? 16.245 7.595   25.594 1.00 31.25  ? 108 GLY   A C   1 
ATOM   820  O  O   . GLY   A 1 102 ? 17.324 7.066   25.299 1.00 31.78  ? 108 GLY   A O   1 
ATOM   821  N  N   . ASP   A 1 103 ? 15.065 7.148   25.122 1.00 29.20  ? 109 ASP   A N   1 
ATOM   822  C  CA  . ASP   A 1 103 ? 14.955 6.042   24.169 1.00 28.64  ? 109 ASP   A CA  1 
ATOM   823  C  C   . ASP   A 1 103 ? 15.301 6.403   22.753 1.00 27.21  ? 109 ASP   A C   1 
ATOM   824  O  O   . ASP   A 1 103 ? 15.451 5.495   21.950 1.00 26.77  ? 109 ASP   A O   1 
ATOM   825  C  CB  . ASP   A 1 103 ? 13.573 5.365   24.180 1.00 29.06  ? 109 ASP   A CB  1 
ATOM   826  C  CG  . ASP   A 1 103 ? 13.315 4.668   25.490 1.00 30.97  ? 109 ASP   A CG  1 
ATOM   827  O  OD1 . ASP   A 1 103 ? 14.251 4.097   26.032 1.00 30.05  ? 109 ASP   A OD1 1 
ATOM   828  O  OD2 . ASP   A 1 103 ? 12.150 4.680   25.953 1.00 33.30  ? 109 ASP   A OD2 1 
ATOM   829  N  N   . CYS   A 1 104 ? 15.431 7.712   22.420 1.00 26.88  ? 110 CYS   A N   1 
ATOM   830  C  CA  . CYS   A 1 104 ? 15.800 8.199   21.074 1.00 26.77  ? 110 CYS   A CA  1 
ATOM   831  C  C   . CYS   A 1 104 ? 17.103 7.536   20.645 1.00 26.52  ? 110 CYS   A C   1 
ATOM   832  O  O   . CYS   A 1 104 ? 18.031 7.468   21.441 1.00 27.21  ? 110 CYS   A O   1 
ATOM   833  C  CB  . CYS   A 1 104 ? 15.946 9.723   21.066 1.00 27.82  ? 110 CYS   A CB  1 
ATOM   834  S  SG  . CYS   A 1 104 ? 14.374 10.634  21.158 1.00 31.24  ? 110 CYS   A SG  1 
ATOM   835  N  N   . GLY   A 1 105 ? 17.177 7.074   19.411 1.00 25.19  ? 111 GLY   A N   1 
ATOM   836  C  CA  . GLY   A 1 105 ? 18.362 6.376   18.929 1.00 25.55  ? 111 GLY   A CA  1 
ATOM   837  C  C   . GLY   A 1 105 ? 18.172 4.866   18.857 1.00 25.76  ? 111 GLY   A C   1 
ATOM   838  O  O   . GLY   A 1 105 ? 18.960 4.189   18.184 1.00 26.13  ? 111 GLY   A O   1 
ATOM   839  N  N   . GLY   A 1 106 ? 17.133 4.330   19.529 1.00 24.83  ? 112 GLY   A N   1 
ATOM   840  C  CA  . GLY   A 1 106 ? 16.810 2.899   19.468 1.00 24.20  ? 112 GLY   A CA  1 
ATOM   841  C  C   . GLY   A 1 106 ? 16.417 2.549   18.031 1.00 25.06  ? 112 GLY   A C   1 
ATOM   842  O  O   . GLY   A 1 106 ? 15.703 3.316   17.386 1.00 24.59  ? 112 GLY   A O   1 
ATOM   843  N  N   . ILE   A 1 107 ? 16.916 1.419   17.495 1.00 24.32  ? 113 ILE   A N   1 
ATOM   844  C  CA  . ILE   A 1 107 ? 16.651 1.068   16.112 1.00 24.35  ? 113 ILE   A CA  1 
ATOM   845  C  C   . ILE   A 1 107 ? 15.313 0.340   15.958 1.00 24.00  ? 113 ILE   A C   1 
ATOM   846  O  O   . ILE   A 1 107 ? 14.945 -0.464  16.811 1.00 23.65  ? 113 ILE   A O   1 
ATOM   847  C  CB  . ILE   A 1 107 ? 17.845 0.243   15.520 1.00 25.28  ? 113 ILE   A CB  1 
ATOM   848  C  CG1 . ILE   A 1 107 ? 19.048 1.165   15.226 1.00 27.52  ? 113 ILE   A CG1 1 
ATOM   849  C  CG2 . ILE   A 1 107 ? 17.450 -0.476  14.227 1.00 25.30  ? 113 ILE   A CG2 1 
ATOM   850  C  CD1 . ILE   A 1 107 ? 20.316 0.383   14.967 1.00 29.34  ? 113 ILE   A CD1 1 
ATOM   851  N  N   . LEU   A 1 108 ? 14.604 0.647   14.862 1.00 23.02  ? 114 LEU   A N   1 
ATOM   852  C  CA  . LEU   A 1 108 ? 13.408 -0.023  14.389 1.00 24.30  ? 114 LEU   A CA  1 
ATOM   853  C  C   . LEU   A 1 108 ? 13.894 -0.800  13.151 1.00 25.49  ? 114 LEU   A C   1 
ATOM   854  O  O   . LEU   A 1 108 ? 14.527 -0.214  12.281 1.00 24.99  ? 114 LEU   A O   1 
ATOM   855  C  CB  . LEU   A 1 108 ? 12.341 1.004   13.954 1.00 25.27  ? 114 LEU   A CB  1 
ATOM   856  C  CG  . LEU   A 1 108 ? 11.144 0.407   13.197 1.00 28.24  ? 114 LEU   A CG  1 
ATOM   857  C  CD1 . LEU   A 1 108 ? 10.285 -0.472  14.122 1.00 28.67  ? 114 LEU   A CD1 1 
ATOM   858  C  CD2 . LEU   A 1 108 ? 10.299 1.516   12.540 1.00 29.48  ? 114 LEU   A CD2 1 
ATOM   859  N  N   . ARG   A 1 109 ? 13.681 -2.124  13.119 1.00 26.32  ? 115 ARG   A N   1 
ATOM   860  C  CA  . ARG   A 1 109 ? 14.105 -2.922  11.986 1.00 28.30  ? 115 ARG   A CA  1 
ATOM   861  C  C   . ARG   A 1 109 ? 13.021 -3.868  11.467 1.00 28.77  ? 115 ARG   A C   1 
ATOM   862  O  O   . ARG   A 1 109 ? 12.142 -4.274  12.216 1.00 27.69  ? 115 ARG   A O   1 
ATOM   863  C  CB  . ARG   A 1 109 ? 15.404 -3.673  12.282 1.00 32.22  ? 115 ARG   A CB  1 
ATOM   864  C  CG  . ARG   A 1 109 ? 15.396 -4.542  13.520 1.00 39.00  ? 115 ARG   A CG  1 
ATOM   865  C  CD  . ARG   A 1 109 ? 16.782 -5.199  13.659 1.00 44.81  ? 115 ARG   A CD  1 
ATOM   866  N  NE  . ARG   A 1 109 ? 17.758 -4.335  14.330 1.00 50.13  ? 115 ARG   A NE  1 
ATOM   867  C  CZ  . ARG   A 1 109 ? 18.960 -4.023  13.838 1.00 53.14  ? 115 ARG   A CZ  1 
ATOM   868  N  NH1 . ARG   A 1 109 ? 19.337 -4.479  12.647 1.00 52.25  ? 115 ARG   A NH1 1 
ATOM   869  N  NH2 . ARG   A 1 109 ? 19.789 -3.250  14.532 1.00 52.85  ? 115 ARG   A NH2 1 
ATOM   870  N  N   . CYS   A 1 110 ? 13.075 -4.181  10.174 1.00 29.79  ? 116 CYS   A N   1 
ATOM   871  C  CA  . CYS   A 1 110 ? 12.161 -5.139  9.576  1.00 31.58  ? 116 CYS   A CA  1 
ATOM   872  C  C   . CYS   A 1 110 ? 13.041 -6.307  8.994  1.00 34.17  ? 116 CYS   A C   1 
ATOM   873  O  O   . CYS   A 1 110 ? 14.283 -6.315  9.173  1.00 33.98  ? 116 CYS   A O   1 
ATOM   874  C  CB  . CYS   A 1 110 ? 11.349 -4.448  8.484  1.00 31.30  ? 116 CYS   A CB  1 
ATOM   875  S  SG  . CYS   A 1 110 ? 12.363 -3.897  7.089  1.00 30.63  ? 116 CYS   A SG  1 
ATOM   876  N  N   . GLN   A 1 111 ? 12.429 -7.241  8.228  1.00 35.74  ? 117 GLN   A N   1 
ATOM   877  C  CA  . GLN   A 1 111 ? 13.192 -8.338  7.625  1.00 37.65  ? 117 GLN   A CA  1 
ATOM   878  C  C   . GLN   A 1 111 ? 14.254 -7.868  6.620  1.00 38.15  ? 117 GLN   A C   1 
ATOM   879  O  O   . GLN   A 1 111 ? 15.156 -8.642  6.294  1.00 38.96  ? 117 GLN   A O   1 
ATOM   880  C  CB  . GLN   A 1 111 ? 12.240 -9.336  6.941  1.00 39.95  ? 117 GLN   A CB  1 
ATOM   881  C  CG  . GLN   A 1 111 ? 11.535 -8.743  5.739  1.00 43.50  ? 117 GLN   A CG  1 
ATOM   882  C  CD  . GLN   A 1 111 ? 10.569 -9.689  5.087  1.00 48.24  ? 117 GLN   A CD  1 
ATOM   883  O  OE1 . GLN   A 1 111 ? 9.373  -9.683  5.385  1.00 50.30  ? 117 GLN   A OE1 1 
ATOM   884  N  NE2 . GLN   A 1 111 ? 11.060 -10.498 4.164  1.00 48.13  ? 117 GLN   A NE2 1 
ATOM   885  N  N   . HIS   A 1 112 ? 14.181 -6.605  6.143  1.00 37.28  ? 118 HIS   A N   1 
ATOM   886  C  CA  . HIS   A 1 112 ? 15.149 -6.106  5.169  1.00 37.29  ? 118 HIS   A CA  1 
ATOM   887  C  C   . HIS   A 1 112 ? 16.296 -5.276  5.747  1.00 36.14  ? 118 HIS   A C   1 
ATOM   888  O  O   . HIS   A 1 112 ? 17.181 -4.871  4.997  1.00 36.62  ? 118 HIS   A O   1 
ATOM   889  C  CB  . HIS   A 1 112 ? 14.457 -5.306  4.055  1.00 38.83  ? 118 HIS   A CB  1 
ATOM   890  C  CG  . HIS   A 1 112 ? 13.322 -6.034  3.406  1.00 42.23  ? 118 HIS   A CG  1 
ATOM   891  N  ND1 . HIS   A 1 112 ? 12.013 -5.805  3.784  1.00 44.45  ? 118 HIS   A ND1 1 
ATOM   892  C  CD2 . HIS   A 1 112 ? 13.338 -6.957  2.416  1.00 43.56  ? 118 HIS   A CD2 1 
ATOM   893  C  CE1 . HIS   A 1 112 ? 11.273 -6.594  3.015  1.00 44.80  ? 118 HIS   A CE1 1 
ATOM   894  N  NE2 . HIS   A 1 112 ? 12.030 -7.308  2.179  1.00 44.78  ? 118 HIS   A NE2 1 
ATOM   895  N  N   . GLY   A 1 113 ? 16.280 -5.017  7.045  1.00 34.39  ? 119 GLY   A N   1 
ATOM   896  C  CA  . GLY   A 1 113 ? 17.319 -4.222  7.684  1.00 33.26  ? 119 GLY   A CA  1 
ATOM   897  C  C   . GLY   A 1 113 ? 16.770 -3.079  8.512  1.00 31.53  ? 119 GLY   A C   1 
ATOM   898  O  O   . GLY   A 1 113 ? 15.625 -3.136  8.965  1.00 30.62  ? 119 GLY   A O   1 
ATOM   899  N  N   . VAL   A 1 114 ? 17.597 -2.032  8.732  1.00 29.55  ? 120 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 114 ? 17.210 -0.864  9.536  1.00 28.20  ? 120 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 114 ? 16.184 0.024   8.822  1.00 26.68  ? 120 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 114 ? 16.388 0.403   7.668  1.00 27.57  ? 120 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 114 ? 18.457 -0.045  9.974  1.00 28.84  ? 120 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 114 ? 18.057 1.236   10.691 1.00 28.89  ? 120 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 114 ? 19.401 -0.890  10.836 1.00 28.65  ? 120 VAL   A CG2 1 
ATOM   906  N  N   . VAL   A 1 115 ? 15.089 0.360   9.501  1.00 24.94  ? 121 VAL   A N   1 
ATOM   907  C  CA  . VAL   A 1 115 ? 14.025 1.212   8.943  1.00 24.27  ? 121 VAL   A CA  1 
ATOM   908  C  C   . VAL   A 1 115 ? 14.178 2.675   9.423  1.00 24.48  ? 121 VAL   A C   1 
ATOM   909  O  O   . VAL   A 1 115 ? 13.860 3.619   8.704  1.00 24.93  ? 121 VAL   A O   1 
ATOM   910  C  CB  . VAL   A 1 115 ? 12.651 0.662   9.390  1.00 24.51  ? 121 VAL   A CB  1 
ATOM   911  C  CG1 . VAL   A 1 115 ? 11.508 1.598   8.988  1.00 25.07  ? 121 VAL   A CG1 1 
ATOM   912  C  CG2 . VAL   A 1 115 ? 12.421 -0.751  8.873  1.00 24.28  ? 121 VAL   A CG2 1 
ATOM   913  N  N   . GLY   A 1 116 ? 14.537 2.838   10.694 1.00 23.95  ? 122 GLY   A N   1 
ATOM   914  C  CA  . GLY   A 1 116 ? 14.695 4.164   11.273 1.00 23.66  ? 122 GLY   A CA  1 
ATOM   915  C  C   . GLY   A 1 116 ? 15.085 4.102   12.738 1.00 23.54  ? 122 GLY   A C   1 
ATOM   916  O  O   . GLY   A 1 116 ? 15.485 3.047   13.225 1.00 23.77  ? 122 GLY   A O   1 
ATOM   917  N  N   . ILE   A 1 117 ? 15.063 5.246   13.411 1.00 22.52  ? 123 ILE   A N   1 
ATOM   918  C  CA  . ILE   A 1 117 ? 15.416 5.299   14.839 1.00 23.47  ? 123 ILE   A CA  1 
ATOM   919  C  C   . ILE   A 1 117 ? 14.328 6.018   15.635 1.00 23.62  ? 123 ILE   A C   1 
ATOM   920  O  O   . ILE   A 1 117 ? 13.682 6.920   15.106 1.00 23.73  ? 123 ILE   A O   1 
ATOM   921  C  CB  . ILE   A 1 117 ? 16.774 6.012   15.069 1.00 25.14  ? 123 ILE   A CB  1 
ATOM   922  C  CG1 . ILE   A 1 117 ? 16.810 7.392   14.385 1.00 26.11  ? 123 ILE   A CG1 1 
ATOM   923  C  CG2 . ILE   A 1 117 ? 17.958 5.125   14.677 1.00 26.59  ? 123 ILE   A CG2 1 
ATOM   924  C  CD1 . ILE   A 1 117 ? 18.147 8.212   14.698 1.00 27.65  ? 123 ILE   A CD1 1 
ATOM   925  N  N   . VAL   A 1 118 ? 14.194 5.705   16.948 1.00 23.53  ? 124 VAL   A N   1 
ATOM   926  C  CA  . VAL   A 1 118 ? 13.210 6.370   17.810 1.00 23.08  ? 124 VAL   A CA  1 
ATOM   927  C  C   . VAL   A 1 118 ? 13.550 7.881   17.855 1.00 23.62  ? 124 VAL   A C   1 
ATOM   928  O  O   . VAL   A 1 118 ? 14.730 8.238   17.988 1.00 23.54  ? 124 VAL   A O   1 
ATOM   929  C  CB  . VAL   A 1 118 ? 13.287 5.757   19.234 1.00 23.98  ? 124 VAL   A CB  1 
ATOM   930  C  CG1 . VAL   A 1 118 ? 12.392 6.519   20.166 1.00 24.15  ? 124 VAL   A CG1 1 
ATOM   931  C  CG2 . VAL   A 1 118 ? 12.904 4.263   19.226 1.00 24.89  ? 124 VAL   A CG2 1 
ATOM   932  N  N   . SER   A 1 119 ? 12.539 8.730   17.729 1.00 23.94  ? 125 SER   A N   1 
ATOM   933  C  CA  . SER   A 1 119 ? 12.734 10.176  17.673 1.00 25.24  ? 125 SER   A CA  1 
ATOM   934  C  C   . SER   A 1 119 ? 11.686 10.936  18.481 1.00 27.13  ? 125 SER   A C   1 
ATOM   935  O  O   . SER   A 1 119 ? 12.032 11.953  19.055 1.00 28.35  ? 125 SER   A O   1 
ATOM   936  C  CB  . SER   A 1 119 ? 12.727 10.651  16.214 1.00 26.37  ? 125 SER   A CB  1 
ATOM   937  O  OG  . SER   A 1 119 ? 12.801 12.066  16.101 1.00 28.57  ? 125 SER   A OG  1 
ATOM   938  N  N   . THR   A 1 120 ? 10.410 10.475  18.526 1.00 27.59  ? 126 THR   A N   1 
ATOM   939  C  CA  . THR   A 1 120 ? 9.359  11.174  19.278 1.00 28.76  ? 126 THR   A CA  1 
ATOM   940  C  C   . THR   A 1 120 ? 8.555  10.173  20.172 1.00 29.47  ? 126 THR   A C   1 
ATOM   941  O  O   . THR   A 1 120 ? 8.766  8.948   20.093 1.00 28.04  ? 126 THR   A O   1 
ATOM   942  C  CB  . THR   A 1 120 ? 8.414  11.938  18.281 1.00 29.68  ? 126 THR   A CB  1 
ATOM   943  O  OG1 . THR   A 1 120 ? 7.546  11.001  17.651 1.00 29.66  ? 126 THR   A OG1 1 
ATOM   944  C  CG2 . THR   A 1 120 ? 9.155  12.787  17.247 1.00 29.82  ? 126 THR   A CG2 1 
ATOM   945  N  N   . GLY   A 1 121 ? 7.631  10.687  20.993 1.00 31.13  ? 127 GLY   A N   1 
ATOM   946  C  CA  . GLY   A 1 121 ? 6.801  9.805   21.798 1.00 32.15  ? 127 GLY   A CA  1 
ATOM   947  C  C   . GLY   A 1 121 ? 6.006  10.490  22.874 1.00 32.98  ? 127 GLY   A C   1 
ATOM   948  O  O   . GLY   A 1 121 ? 6.003  11.714  22.981 1.00 32.78  ? 127 GLY   A O   1 
ATOM   949  N  N   . GLY   A 1 122 ? 5.348  9.677   23.670 1.00 33.98  ? 128 GLY   A N   1 
ATOM   950  C  CA  . GLY   A 1 122 ? 4.482  10.151  24.746 1.00 34.97  ? 128 GLY   A CA  1 
ATOM   951  C  C   . GLY   A 1 122 ? 3.059  9.682   24.522 1.00 35.75  ? 128 GLY   A C   1 
ATOM   952  O  O   . GLY   A 1 122 ? 2.669  9.407   23.386 1.00 35.71  ? 128 GLY   A O   1 
ATOM   953  N  N   . ASN   A 1 123 ? 2.285  9.551   25.599 1.00 36.41  ? 129 ASN   A N   1 
ATOM   954  C  CA  . ASN   A 1 123 ? 0.879  9.127   25.546 1.00 37.55  ? 129 ASN   A CA  1 
ATOM   955  C  C   . ASN   A 1 123 ? 0.683  7.728   24.960 1.00 36.68  ? 129 ASN   A C   1 
ATOM   956  O  O   . ASN   A 1 123 ? -0.329 7.471   24.318 1.00 37.67  ? 129 ASN   A O   1 
ATOM   957  C  CB  . ASN   A 1 123 ? 0.017  10.153  24.793 1.00 39.97  ? 129 ASN   A CB  1 
ATOM   958  C  CG  . ASN   A 1 123 ? -0.117 11.473  25.512 1.00 45.36  ? 129 ASN   A CG  1 
ATOM   959  O  OD1 . ASN   A 1 123 ? -0.151 11.533  26.750 1.00 47.05  ? 129 ASN   A OD1 1 
ATOM   960  N  ND2 . ASN   A 1 123 ? -0.235 12.553  24.747 1.00 46.78  ? 129 ASN   A ND2 1 
ATOM   961  N  N   . GLY   A 1 124 ? 1.645  6.835   25.178 1.00 34.53  ? 130 GLY   A N   1 
ATOM   962  C  CA  . GLY   A 1 124 ? 1.553  5.474   24.655 1.00 32.36  ? 130 GLY   A CA  1 
ATOM   963  C  C   . GLY   A 1 124 ? 1.810  5.360   23.164 1.00 30.44  ? 130 GLY   A C   1 
ATOM   964  O  O   . GLY   A 1 124 ? 1.523  4.325   22.575 1.00 30.40  ? 130 GLY   A O   1 
ATOM   965  N  N   . LEU   A 1 125 ? 2.367  6.397   22.536 1.00 28.84  ? 131 LEU   A N   1 
ATOM   966  C  CA  . LEU   A 1 125 ? 2.702  6.354   21.105 1.00 29.18  ? 131 LEU   A CA  1 
ATOM   967  C  C   . LEU   A 1 125 ? 4.178  6.642   20.923 1.00 29.61  ? 131 LEU   A C   1 
ATOM   968  O  O   . LEU   A 1 125 ? 4.664  7.553   21.555 1.00 32.49  ? 131 LEU   A O   1 
ATOM   969  C  CB  . LEU   A 1 125 ? 1.890  7.397   20.342 1.00 30.17  ? 131 LEU   A CB  1 
ATOM   970  C  CG  . LEU   A 1 125 ? 0.390  7.100   20.344 1.00 32.64  ? 131 LEU   A CG  1 
ATOM   971  C  CD1 . LEU   A 1 125 ? -0.411 8.352   20.118 1.00 34.40  ? 131 LEU   A CD1 1 
ATOM   972  C  CD2 . LEU   A 1 125 ? 0.064  6.017   19.342 1.00 33.28  ? 131 LEU   A CD2 1 
ATOM   973  N  N   . VAL   A 1 126 ? 4.888  5.893   20.084 1.00 26.46  ? 132 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 126 ? 6.307  6.092   19.825 1.00 24.59  ? 132 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 126 ? 6.485  6.425   18.339 1.00 25.08  ? 132 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 126 ? 5.795  5.856   17.512 1.00 25.10  ? 132 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 126 ? 7.157  4.865   20.290 1.00 23.98  ? 132 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 126 ? 6.615  3.555   19.735 1.00 24.38  ? 132 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 126 ? 8.658  5.049   19.963 1.00 23.00  ? 132 VAL   A CG2 1 
ATOM   980  N  N   . GLY   A 1 127 ? 7.334  7.406   18.032 1.00 25.17  ? 133 GLY   A N   1 
ATOM   981  C  CA  . GLY   A 1 127 ? 7.602  7.843   16.670 1.00 25.45  ? 133 GLY   A CA  1 
ATOM   982  C  C   . GLY   A 1 127 ? 9.033  7.543   16.280 1.00 24.95  ? 133 GLY   A C   1 
ATOM   983  O  O   . GLY   A 1 127 ? 9.953  7.653   17.103 1.00 24.96  ? 133 GLY   A O   1 
ATOM   984  N  N   . PHE   A 1 128 ? 9.220  7.166   15.014 1.00 24.38  ? 134 PHE   A N   1 
ATOM   985  C  CA  . PHE   A 1 128 ? 10.514 6.762   14.473 1.00 24.82  ? 134 PHE   A CA  1 
ATOM   986  C  C   . PHE   A 1 128 ? 10.799 7.615   13.249 1.00 24.82  ? 134 PHE   A C   1 
ATOM   987  O  O   . PHE   A 1 128 ? 9.895  7.812   12.431 1.00 24.48  ? 134 PHE   A O   1 
ATOM   988  C  CB  . PHE   A 1 128 ? 10.442 5.266   14.026 1.00 24.46  ? 134 PHE   A CB  1 
ATOM   989  C  CG  . PHE   A 1 128 ? 9.885  4.306   15.061 1.00 24.47  ? 134 PHE   A CG  1 
ATOM   990  C  CD1 . PHE   A 1 128 ? 10.706 3.760   16.042 1.00 24.15  ? 134 PHE   A CD1 1 
ATOM   991  C  CD2 . PHE   A 1 128 ? 8.555  3.915   15.028 1.00 24.80  ? 134 PHE   A CD2 1 
ATOM   992  C  CE1 . PHE   A 1 128 ? 10.198 2.875   16.982 1.00 24.74  ? 134 PHE   A CE1 1 
ATOM   993  C  CE2 . PHE   A 1 128 ? 8.045  3.037   15.980 1.00 24.78  ? 134 PHE   A CE2 1 
ATOM   994  C  CZ  . PHE   A 1 128 ? 8.864  2.520   16.950 1.00 24.14  ? 134 PHE   A CZ  1 
ATOM   995  N  N   . ALA   A 1 129 ? 12.037 8.143   13.142 1.00 25.57  ? 135 ALA   A N   1 
ATOM   996  C  CA  . ALA   A 1 129 ? 12.481 8.917   11.989 1.00 25.79  ? 135 ALA   A CA  1 
ATOM   997  C  C   . ALA   A 1 129 ? 12.862 7.896   10.905 1.00 25.45  ? 135 ALA   A C   1 
ATOM   998  O  O   . ALA   A 1 129 ? 13.794 7.114   11.104 1.00 24.95  ? 135 ALA   A O   1 
ATOM   999  C  CB  . ALA   A 1 129 ? 13.708 9.769   12.367 1.00 25.90  ? 135 ALA   A CB  1 
ATOM   1000 N  N   . ASP   A 1 130 ? 12.175 7.915   9.753  1.00 24.85  ? 136 ASP   A N   1 
ATOM   1001 C  CA  . ASP   A 1 130 ? 12.498 6.996   8.668  1.00 25.46  ? 136 ASP   A CA  1 
ATOM   1002 C  C   . ASP   A 1 130 ? 13.867 7.298   8.041  1.00 25.16  ? 136 ASP   A C   1 
ATOM   1003 O  O   . ASP   A 1 130 ? 14.254 8.484   7.943  1.00 24.85  ? 136 ASP   A O   1 
ATOM   1004 C  CB  . ASP   A 1 130 ? 11.410 7.087   7.581  1.00 27.93  ? 136 ASP   A CB  1 
ATOM   1005 C  CG  . ASP   A 1 130 ? 11.602 6.103   6.459  1.00 32.93  ? 136 ASP   A CG  1 
ATOM   1006 O  OD1 . ASP   A 1 130 ? 11.678 4.902   6.738  1.00 33.62  ? 136 ASP   A OD1 1 
ATOM   1007 O  OD2 . ASP   A 1 130 ? 11.682 6.539   5.295  1.00 35.84  ? 136 ASP   A OD2 1 
ATOM   1008 N  N   . VAL   A 1 131 ? 14.622 6.238   7.637  1.00 24.57  ? 137 VAL   A N   1 
ATOM   1009 C  CA  . VAL   A 1 131 ? 15.894 6.440   6.898  1.00 25.80  ? 137 VAL   A CA  1 
ATOM   1010 C  C   . VAL   A 1 131 ? 15.890 5.733   5.499  1.00 27.56  ? 137 VAL   A C   1 
ATOM   1011 O  O   . VAL   A 1 131 ? 16.828 5.898   4.731  1.00 28.25  ? 137 VAL   A O   1 
ATOM   1012 C  CB  . VAL   A 1 131 ? 17.189 6.103   7.682  1.00 25.80  ? 137 VAL   A CB  1 
ATOM   1013 C  CG1 . VAL   A 1 131 ? 17.302 6.966   8.931  1.00 25.67  ? 137 VAL   A CG1 1 
ATOM   1014 C  CG2 . VAL   A 1 131 ? 17.258 4.605   8.027  1.00 25.72  ? 137 VAL   A CG2 1 
ATOM   1015 N  N   . ARG   A 1 132 ? 14.858 4.918   5.198  1.00 27.98  ? 138 ARG   A N   1 
ATOM   1016 C  CA  . ARG   A 1 132 ? 14.762 4.118   3.974  1.00 29.02  ? 138 ARG   A CA  1 
ATOM   1017 C  C   . ARG   A 1 132 ? 14.765 4.912   2.667  1.00 30.86  ? 138 ARG   A C   1 
ATOM   1018 O  O   . ARG   A 1 132 ? 15.101 4.343   1.619  1.00 31.89  ? 138 ARG   A O   1 
ATOM   1019 C  CB  . ARG   A 1 132 ? 13.527 3.202   4.031  1.00 28.36  ? 138 ARG   A CB  1 
ATOM   1020 C  CG  . ARG   A 1 132 ? 13.536 2.191   5.175  1.00 26.03  ? 138 ARG   A CG  1 
ATOM   1021 C  CD  . ARG   A 1 132 ? 12.222 1.408   5.147  1.00 26.13  ? 138 ARG   A CD  1 
ATOM   1022 N  NE  . ARG   A 1 132 ? 11.101 2.227   5.622  1.00 25.93  ? 138 ARG   A NE  1 
ATOM   1023 C  CZ  . ARG   A 1 132 ? 9.863  1.785   5.798  1.00 29.32  ? 138 ARG   A CZ  1 
ATOM   1024 N  NH1 . ARG   A 1 132 ? 9.557  0.520   5.524  1.00 29.27  ? 138 ARG   A NH1 1 
ATOM   1025 N  NH2 . ARG   A 1 132 ? 8.925  2.595   6.287  1.00 28.86  ? 138 ARG   A NH2 1 
ATOM   1026 N  N   . ASP   A 1 133 ? 14.405 6.211   2.699  1.00 30.98  ? 139 ASP   A N   1 
ATOM   1027 C  CA  . ASP   A 1 133 ? 14.436 7.020   1.472  1.00 31.56  ? 139 ASP   A CA  1 
ATOM   1028 C  C   . ASP   A 1 133 ? 15.868 7.562   1.151  1.00 31.84  ? 139 ASP   A C   1 
ATOM   1029 O  O   . ASP   A 1 133 ? 16.144 7.983   0.021  1.00 32.15  ? 139 ASP   A O   1 
ATOM   1030 C  CB  . ASP   A 1 133 ? 13.427 8.169   1.575  1.00 32.90  ? 139 ASP   A CB  1 
ATOM   1031 C  CG  . ASP   A 1 133 ? 13.812 9.243   2.570  1.00 37.85  ? 139 ASP   A CG  1 
ATOM   1032 O  OD1 . ASP   A 1 133 ? 14.112 8.894   3.731  1.00 38.17  ? 139 ASP   A OD1 1 
ATOM   1033 O  OD2 . ASP   A 1 133 ? 13.801 10.433  2.191  1.00 40.07  ? 139 ASP   A OD2 1 
ATOM   1034 N  N   . LEU   A 1 134 ? 16.770 7.563   2.144  1.00 30.85  ? 140 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 134 ? 18.146 8.063   1.997  1.00 30.59  ? 140 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 134 ? 19.040 7.031   1.245  1.00 30.85  ? 140 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 134 ? 19.881 6.362   1.846  1.00 30.52  ? 140 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 134 ? 18.712 8.386   3.404  1.00 30.24  ? 140 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 134 ? 17.863 9.332   4.260  1.00 30.49  ? 140 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 134 ? 18.445 9.486   5.673  1.00 30.57  ? 140 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 134 ? 17.716 10.690  3.599  1.00 30.78  ? 140 LEU   A CD2 1 
ATOM   1042 N  N   . LEU   A 1 135 ? 18.843 6.908   -0.082 1.00 31.36  ? 141 LEU   A N   1 
ATOM   1043 C  CA  . LEU   A 1 135 ? 19.538 5.943   -0.915 1.00 32.88  ? 141 LEU   A CA  1 
ATOM   1044 C  C   . LEU   A 1 135 ? 21.063 6.076   -0.915 1.00 35.13  ? 141 LEU   A C   1 
ATOM   1045 O  O   . LEU   A 1 135 ? 21.771 5.065   -0.991 1.00 35.72  ? 141 LEU   A O   1 
ATOM   1046 C  CB  . LEU   A 1 135 ? 19.005 6.005   -2.358 1.00 33.15  ? 141 LEU   A CB  1 
ATOM   1047 C  CG  . LEU   A 1 135 ? 17.488 5.862   -2.537 1.00 34.83  ? 141 LEU   A CG  1 
ATOM   1048 C  CD1 . LEU   A 1 135 ? 17.132 5.772   -4.031 1.00 35.96  ? 141 LEU   A CD1 1 
ATOM   1049 C  CD2 . LEU   A 1 135 ? 16.939 4.618   -1.854 1.00 35.46  ? 141 LEU   A CD2 1 
ATOM   1050 N  N   . TRP   A 1 136 ? 21.567 7.312   -0.816 1.00 35.50  ? 142 TRP   A N   1 
ATOM   1051 C  CA  . TRP   A 1 136 ? 23.000 7.582   -0.815 1.00 36.98  ? 142 TRP   A CA  1 
ATOM   1052 C  C   . TRP   A 1 136 ? 23.747 6.925   0.359  1.00 39.59  ? 142 TRP   A C   1 
ATOM   1053 O  O   . TRP   A 1 136 ? 24.965 6.817   0.295  1.00 40.22  ? 142 TRP   A O   1 
ATOM   1054 C  CB  . TRP   A 1 136 ? 23.272 9.100   -0.888 1.00 36.10  ? 142 TRP   A CB  1 
ATOM   1055 C  CG  . TRP   A 1 136 ? 22.534 9.907   0.135  1.00 35.27  ? 142 TRP   A CG  1 
ATOM   1056 C  CD1 . TRP   A 1 136 ? 21.327 10.527  -0.016 1.00 35.68  ? 142 TRP   A CD1 1 
ATOM   1057 C  CD2 . TRP   A 1 136 ? 22.987 10.220  1.457  1.00 34.87  ? 142 TRP   A CD2 1 
ATOM   1058 N  NE1 . TRP   A 1 136 ? 20.986 11.182  1.145  1.00 35.55  ? 142 TRP   A NE1 1 
ATOM   1059 C  CE2 . TRP   A 1 136 ? 21.993 11.016  2.064  1.00 35.17  ? 142 TRP   A CE2 1 
ATOM   1060 C  CE3 . TRP   A 1 136 ? 24.149 9.922   2.182  1.00 35.71  ? 142 TRP   A CE3 1 
ATOM   1061 C  CZ2 . TRP   A 1 136 ? 22.104 11.471  3.377  1.00 35.56  ? 142 TRP   A CZ2 1 
ATOM   1062 C  CZ3 . TRP   A 1 136 ? 24.261 10.385  3.483  1.00 36.16  ? 142 TRP   A CZ3 1 
ATOM   1063 C  CH2 . TRP   A 1 136 ? 23.251 11.157  4.060  1.00 35.96  ? 142 TRP   A CH2 1 
ATOM   1064 N  N   . LEU   A 1 137 ? 23.034 6.476   1.414  1.00 40.70  ? 143 LEU   A N   1 
ATOM   1065 C  CA  . LEU   A 1 137 ? 23.662 5.783   2.538  1.00 42.77  ? 143 LEU   A CA  1 
ATOM   1066 C  C   . LEU   A 1 137 ? 24.302 4.449   2.095  1.00 46.05  ? 143 LEU   A C   1 
ATOM   1067 O  O   . LEU   A 1 137 ? 25.209 3.975   2.772  1.00 46.14  ? 143 LEU   A O   1 
ATOM   1068 C  CB  . LEU   A 1 137 ? 22.654 5.508   3.670  1.00 42.14  ? 143 LEU   A CB  1 
ATOM   1069 C  CG  . LEU   A 1 137 ? 22.166 6.703   4.483  1.00 42.28  ? 143 LEU   A CG  1 
ATOM   1070 C  CD1 . LEU   A 1 137 ? 21.039 6.292   5.424  1.00 42.31  ? 143 LEU   A CD1 1 
ATOM   1071 C  CD2 . LEU   A 1 137 ? 23.278 7.297   5.300  1.00 43.09  ? 143 LEU   A CD2 1 
ATOM   1072 N  N   . ASP   A 1 138 ? 23.826 3.842   0.984  1.00 48.74  ? 144 ASP   A N   1 
ATOM   1073 C  CA  . ASP   A 1 138 ? 24.357 2.579   0.437  1.00 52.03  ? 144 ASP   A CA  1 
ATOM   1074 C  C   . ASP   A 1 138 ? 25.527 2.772   -0.518 1.00 55.16  ? 144 ASP   A C   1 
ATOM   1075 O  O   . ASP   A 1 138 ? 25.949 1.781   -1.116 1.00 55.48  ? 144 ASP   A O   1 
ATOM   1076 C  CB  . ASP   A 1 138 ? 23.298 1.830   -0.386 1.00 53.96  ? 144 ASP   A CB  1 
ATOM   1077 C  CG  . ASP   A 1 138 ? 22.057 1.417   0.344  1.00 60.03  ? 144 ASP   A CG  1 
ATOM   1078 O  OD1 . ASP   A 1 138 ? 22.042 1.513   1.591  1.00 61.24  ? 144 ASP   A OD1 1 
ATOM   1079 O  OD2 . ASP   A 1 138 ? 21.083 1.008   -0.330 1.00 62.91  ? 144 ASP   A OD2 1 
ATOM   1080 N  N   . GLU   A 1 139 ? 26.004 4.013   -0.742 1.00 57.35  ? 145 GLU   A N   1 
ATOM   1081 C  CA  . GLU   A 1 139 ? 27.100 4.232   -1.688 1.00 60.20  ? 145 GLU   A CA  1 
ATOM   1082 C  C   . GLU   A 1 139 ? 27.947 5.473   -1.370 1.00 62.37  ? 145 GLU   A C   1 
ATOM   1083 O  O   . GLU   A 1 139 ? 27.491 6.362   -0.646 1.00 62.67  ? 145 GLU   A O   1 
ATOM   1084 C  CB  . GLU   A 1 139 ? 26.549 4.322   -3.124 1.00 63.28  ? 145 GLU   A CB  1 
ATOM   1085 C  CG  . GLU   A 1 139 ? 25.695 5.551   -3.371 1.00 68.93  ? 145 GLU   A CG  1 
ATOM   1086 C  CD  . GLU   A 1 139 ? 24.483 5.277   -4.238 1.00 77.46  ? 145 GLU   A CD  1 
ATOM   1087 O  OE1 . GLU   A 1 139 ? 24.102 6.169   -5.031 1.00 79.32  ? 145 GLU   A OE1 1 
ATOM   1088 O  OE2 . GLU   A 1 139 ? 23.918 4.163   -4.127 1.00 80.38  ? 145 GLU   A OE2 1 
ATOM   1089 N  N   . GLU   A 1 140 ? 29.175 5.528   -1.935 1.00 63.78  ? 146 GLU   A N   1 
ATOM   1090 C  CA  . GLU   A 1 140 ? 30.131 6.638   -1.808 1.00 65.48  ? 146 GLU   A CA  1 
ATOM   1091 C  C   . GLU   A 1 140 ? 30.322 7.091   -0.339 1.00 66.73  ? 146 GLU   A C   1 
ATOM   1092 O  O   . GLU   A 1 140 ? 31.351 6.819   0.277  1.00 67.35  ? 146 GLU   A O   1 
ATOM   1093 C  CB  . GLU   A 1 140 ? 29.729 7.796   -2.762 1.00 67.89  ? 146 GLU   A CB  1 
ATOM   1094 C  CG  . GLU   A 1 140 ? 29.586 9.190   -2.168 1.00 73.37  ? 146 GLU   A CG  1 
ATOM   1095 C  CD  . GLU   A 1 140 ? 30.872 9.987   -2.065 1.00 80.68  ? 146 GLU   A CD  1 
ATOM   1096 O  OE1 . GLU   A 1 140 ? 30.878 11.007  -1.339 1.00 82.01  ? 146 GLU   A OE1 1 
ATOM   1097 O  OE2 . GLU   A 1 140 ? 31.873 9.594   -2.707 1.00 82.96  ? 146 GLU   A OE2 1 
HETATM 1098 N  N1  . A1BPI B 2 .   ? 11.750 14.840  22.251 1.00 32.28  ? 201 A1BPI A N1  1 
HETATM 1099 N  N3  . A1BPI B 2 .   ? 9.594  9.455   24.060 1.00 30.93  ? 201 A1BPI A N3  1 
HETATM 1100 C  C4  . A1BPI B 2 .   ? 9.684  14.272  23.432 1.00 32.57  ? 201 A1BPI A C4  1 
HETATM 1101 C  C5  . A1BPI B 2 .   ? 11.175 14.555  23.438 1.00 32.78  ? 201 A1BPI A C5  1 
HETATM 1102 C  C6  . A1BPI B 2 .   ? 13.166 15.241  22.146 1.00 32.27  ? 201 A1BPI A C6  1 
HETATM 1103 C  C7  . A1BPI B 2 .   ? 13.289 15.711  20.699 1.00 32.20  ? 201 A1BPI A C7  1 
HETATM 1104 C  C8  . A1BPI B 2 .   ? 12.227 14.885  19.954 1.00 31.87  ? 201 A1BPI A C8  1 
HETATM 1105 C  C10 . A1BPI B 2 .   ? 11.067 14.871  20.952 1.00 31.93  ? 201 A1BPI A C10 1 
HETATM 1106 C  C13 . A1BPI B 2 .   ? 8.281  10.852  25.685 1.00 32.00  ? 201 A1BPI A C13 1 
HETATM 1107 O  O1  . A1BPI B 2 .   ? 11.171 16.454  18.469 1.00 31.55  ? 201 A1BPI A O1  1 
HETATM 1108 C  C9  . A1BPI B 2 .   ? 11.832 15.418  18.586 1.00 31.69  ? 201 A1BPI A C9  1 
HETATM 1109 N  N2  . A1BPI B 2 .   ? 12.193 14.676  17.551 1.00 31.22  ? 201 A1BPI A N2  1 
HETATM 1110 O  O   . A1BPI B 2 .   ? 11.810 14.564  24.481 1.00 33.58  ? 201 A1BPI A O   1 
HETATM 1111 C  C3  . A1BPI B 2 .   ? 9.294  13.068  24.263 1.00 32.17  ? 201 A1BPI A C3  1 
HETATM 1112 C  C11 . A1BPI B 2 .   ? 8.478  13.233  25.381 1.00 32.16  ? 201 A1BPI A C11 1 
HETATM 1113 C  C12 . A1BPI B 2 .   ? 7.967  12.144  26.075 1.00 32.36  ? 201 A1BPI A C12 1 
HETATM 1114 C  C14 . A1BPI B 2 .   ? 9.132  10.645  24.586 1.00 31.31  ? 201 A1BPI A C14 1 
HETATM 1115 C  C2  . A1BPI B 2 .   ? 9.637  11.755  23.876 1.00 31.34  ? 201 A1BPI A C2  1 
HETATM 1116 C  C1  . A1BPI B 2 .   ? 10.449 11.187  22.861 1.00 30.90  ? 201 A1BPI A C1  1 
HETATM 1117 N  N   . A1BPI B 2 .   ? 10.390 9.859   23.026 1.00 30.66  ? 201 A1BPI A N   1 
HETATM 1118 C  C   . A1BPI B 2 .   ? 11.177 8.874   22.282 1.00 29.91  ? 201 A1BPI A C   1 
HETATM 1119 ZN ZN  . ZN    C 3 .   ? 11.211 -4.144  5.112  1.00 33.42  2 202 ZN    A ZN  1 
HETATM 1120 S  S   . DMS   D 4 .   ? 1.074  -1.485  23.944 1.00 81.07  ? 203 DMS   A S   1 
HETATM 1121 O  O   . DMS   D 4 .   ? 1.854  -0.259  24.315 1.00 81.15  ? 203 DMS   A O   1 
HETATM 1122 C  C1  . DMS   D 4 .   ? 2.198  -2.905  24.023 1.00 81.08  ? 203 DMS   A C1  1 
HETATM 1123 C  C2  . DMS   D 4 .   ? 0.105  -1.979  25.399 1.00 81.15  ? 203 DMS   A C2  1 
HETATM 1124 O  O   . HOH   E 5 .   ? 3.168  8.338   9.807  1.00 58.82  ? 301 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 13.559 7.525   30.777 1.00 36.54  ? 302 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 5.704  20.307  25.622 1.00 50.18  ? 303 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 3.164  -1.908  3.610  1.00 67.08  ? 304 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 8.275  -3.556  0.246  1.00 48.23  ? 305 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 14.054 15.305  25.495 1.00 52.67  ? 306 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? -0.129 16.199  9.311  1.00 59.97  ? 307 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 6.393  3.031   3.352  1.00 42.55  ? 308 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 27.111 -1.533  6.218  1.00 65.95  ? 309 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 9.760  -4.544  32.162 1.00 64.39  ? 310 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? -1.079 1.115   4.647  1.00 53.61  ? 311 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 4.091  22.170  23.116 1.00 44.14  ? 312 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 29.739 3.493   9.773  1.00 38.15  ? 313 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 22.528 -4.542  11.985 1.00 44.50  ? 314 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 22.542 -0.394  3.348  1.00 41.17  ? 315 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 27.801 3.429   2.594  1.00 52.37  ? 316 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 7.122  -4.912  28.752 1.00 47.30  ? 317 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 24.366 8.823   -4.880 1.00 81.95  ? 318 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 15.270 11.860  0.467  1.00 44.12  ? 319 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 20.081 0.047   26.849 1.00 45.39  ? 320 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 9.020  -8.434  23.125 1.00 30.92  ? 321 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 23.839 0.421   15.139 1.00 32.81  ? 322 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 10.639 8.823   4.294  1.00 34.89  ? 323 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 8.705  19.849  18.364 1.00 36.27  ? 324 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 30.885 11.312  18.076 1.00 52.73  ? 325 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 0.852  2.241   24.306 1.00 34.89  ? 326 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 18.576 2.955   22.670 1.00 27.27  ? 327 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 10.337 18.459  20.315 1.00 38.63  ? 328 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 6.114  1.941   6.190  1.00 38.72  ? 329 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 27.078 4.207   19.098 1.00 54.10  ? 330 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 6.512  8.197   28.272 1.00 41.98  ? 331 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 17.946 -6.081  2.691  1.00 61.22  ? 332 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 7.624  16.349  21.783 1.00 37.02  ? 333 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 21.325 23.864  10.233 1.00 53.14  ? 334 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 9.112  3.088   2.551  1.00 39.10  ? 335 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 24.508 22.781  8.859  1.00 34.95  ? 336 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 1.366  -2.158  19.793 1.00 39.68  ? 337 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 4.670  -4.518  21.177 1.00 29.65  ? 338 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 12.465 2.575   33.138 1.00 33.67  ? 339 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 20.423 -1.158  30.407 1.00 59.39  ? 340 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 20.746 9.371   18.530 1.00 24.49  ? 341 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 15.701 2.865   22.805 1.00 24.87  ? 342 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 8.491  20.751  9.060  1.00 48.42  ? 343 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 11.662 12.183  11.157 1.00 26.78  ? 344 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 16.275 -2.882  17.196 1.00 36.78  ? 345 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 19.223 4.838   25.673 1.00 43.09  ? 346 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 5.583  6.627   24.034 1.00 43.15  ? 347 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 16.107 12.754  23.710 1.00 39.91  ? 348 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 31.625 2.930   11.646 1.00 49.52  ? 349 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 21.007 2.296   17.922 1.00 44.18  ? 350 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 7.801  4.245   32.664 1.00 35.78  ? 351 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 14.066 -6.435  30.153 1.00 74.51  ? 352 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 0.941  0.050   16.533 1.00 24.39  ? 353 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 18.651 0.737   29.738 1.00 46.88  ? 354 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 11.260 17.927  5.279  1.00 66.11  ? 355 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 12.666 21.805  12.953 1.00 39.09  ? 356 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 31.714 9.042   4.450  1.00 42.62  ? 357 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 3.790  4.182   27.530 1.00 43.42  ? 358 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 18.603 19.296  16.595 1.00 32.75  ? 359 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 16.866 17.690  3.633  1.00 55.34  ? 360 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 18.260 21.577  9.011  1.00 34.22  ? 361 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 31.369 11.620  15.106 1.00 85.27  ? 362 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 14.632 15.004  3.305  1.00 42.09  ? 363 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 15.431 -5.216  17.614 1.00 41.10  ? 364 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 19.884 -4.325  26.053 1.00 51.19  ? 365 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 4.896  11.587  18.557 1.00 37.35  ? 366 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 10.946 4.818   33.566 1.00 41.84  ? 367 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 30.925 -3.738  6.810  1.00 55.64  ? 368 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 6.875  13.744  21.151 1.00 31.46  ? 369 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 18.678 20.176  5.068  1.00 47.73  ? 370 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 10.549 5.113   3.064  1.00 31.41  ? 371 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 3.440  13.838  18.147 1.00 42.20  ? 372 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 4.748  13.743  24.614 1.00 39.95  ? 373 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 36.946 -0.337  9.143  1.00 54.52  ? 374 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 5.867  -0.994  23.934 1.00 29.35  ? 375 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 14.438 9.763   29.478 1.00 45.02  ? 376 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 0.365  4.426   6.644  1.00 37.30  ? 377 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 32.082 2.423   2.477  1.00 57.46  ? 378 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 10.651 24.453  24.273 1.00 51.08  ? 379 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 13.389 11.038  9.013  1.00 26.68  ? 380 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 18.998 13.272  1.455  1.00 49.78  ? 381 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 4.228  -4.807  6.328  1.00 38.54  ? 382 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 6.773  -7.480  14.140 1.00 44.69  ? 383 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 27.945 16.480  1.979  1.00 52.75  ? 384 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 7.584  16.980  24.983 1.00 60.19  ? 385 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 13.156 -8.395  23.961 1.00 29.77  ? 386 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 23.487 18.391  18.110 1.00 46.00  ? 387 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 11.903 18.069  27.000 1.00 44.19  ? 388 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 6.873  13.335  5.328  1.00 33.57  ? 389 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 9.714  -6.880  24.572 1.00 124.14 ? 390 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 26.601 10.092  -0.634 1.00 106.86 ? 391 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 10.530 15.783  26.854 1.00 44.88  ? 392 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 18.246 -5.308  17.087 1.00 66.47  ? 393 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 7.430  -4.796  2.366  1.00 47.45  ? 394 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 22.591 -2.249  14.979 1.00 40.14  ? 395 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 24.430 2.820   18.814 1.00 41.79  ? 396 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? -0.178 15.688  12.858 1.00 44.31  ? 397 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 19.220 0.182   18.939 1.00 32.61  ? 398 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 19.847 9.530   25.188 1.00 39.87  ? 399 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 1.219  9.421   4.300  1.00 67.98  ? 400 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 15.014 -4.051  33.805 1.00 55.35  ? 401 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 20.968 3.077   -3.118 1.00 56.90  ? 402 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 5.233  1.002   -2.350 1.00 53.16  ? 403 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 21.860 21.603  5.973  1.00 47.37  ? 404 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 6.484  23.528  11.671 1.00 41.80  ? 405 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 14.791 21.644  8.010  1.00 50.89  ? 406 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 4.442  7.722   2.963  1.00 53.82  ? 407 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 33.241 15.269  19.891 1.00 69.63  ? 408 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 3.317  10.884  20.785 1.00 44.80  ? 409 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 14.933 15.321  27.944 1.00 46.79  ? 410 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 21.279 -4.579  9.413  1.00 41.72  ? 411 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 31.717 0.298   12.956 1.00 61.94  ? 412 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 35.284 6.279   13.429 1.00 60.40  ? 413 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 22.769 19.208  5.152  1.00 36.19  ? 414 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 26.582 -2.283  13.567 1.00 62.57  ? 415 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 4.534  6.881   26.255 1.00 46.02  ? 416 HOH   A O   1 
HETATM 1240 O  O   . HOH   E 5 .   ? 28.920 -1.378  13.014 1.00 48.28  ? 417 HOH   A O   1 
HETATM 1241 O  O   . HOH   E 5 .   ? 10.408 9.696   31.569 1.00 49.75  ? 418 HOH   A O   1 
HETATM 1242 O  O   . HOH   E 5 .   ? 4.268  15.072  20.393 1.00 34.69  ? 419 HOH   A O   1 
HETATM 1243 O  O   . HOH   E 5 .   ? 33.122 14.747  6.130  1.00 70.02  ? 420 HOH   A O   1 
HETATM 1244 O  O   . HOH   E 5 .   ? 4.639  -1.978  21.604 1.00 31.84  ? 421 HOH   A O   1 
HETATM 1245 O  O   . HOH   E 5 .   ? 9.038  -7.207  8.868  1.00 47.08  ? 422 HOH   A O   1 
HETATM 1246 O  O   . HOH   E 5 .   ? 1.717  -2.664  17.332 1.00 32.95  ? 423 HOH   A O   1 
HETATM 1247 O  O   . HOH   E 5 .   ? 22.720 9.112   20.487 1.00 30.01  ? 424 HOH   A O   1 
HETATM 1248 O  O   . HOH   E 5 .   ? 31.069 6.282   17.463 1.00 56.16  ? 425 HOH   A O   1 
HETATM 1249 O  O   . HOH   E 5 .   ? 29.945 4.902   2.570  1.00 44.70  ? 426 HOH   A O   1 
HETATM 1250 O  O   . HOH   E 5 .   ? 29.377 17.291  22.315 1.00 58.72  ? 427 HOH   A O   1 
HETATM 1251 O  O   . HOH   E 5 .   ? 7.272  11.476  3.994  1.00 49.44  ? 428 HOH   A O   1 
HETATM 1252 O  O   . HOH   E 5 .   ? 2.381  13.686  4.947  1.00 50.34  ? 429 HOH   A O   1 
HETATM 1253 O  O   . HOH   E 5 .   ? 28.976 -1.235  4.546  1.00 85.31  ? 430 HOH   A O   1 
HETATM 1254 O  O   . HOH   E 5 .   ? 5.650  -0.869  28.864 1.00 57.06  ? 431 HOH   A O   1 
HETATM 1255 O  O   . HOH   E 5 .   ? 6.605  -3.529  -1.951 1.00 48.52  ? 432 HOH   A O   1 
HETATM 1256 O  O   . HOH   E 5 .   ? 2.457  -6.627  17.782 1.00 55.15  ? 433 HOH   A O   1 
HETATM 1257 O  O   . HOH   E 5 .   ? 36.700 2.323   5.365  1.00 58.37  ? 434 HOH   A O   1 
HETATM 1258 O  O   . HOH   E 5 .   ? 25.166 7.662   19.782 1.00 48.90  ? 435 HOH   A O   1 
HETATM 1259 O  O   . HOH   E 5 .   ? 18.420 23.691  16.547 1.00 62.30  ? 436 HOH   A O   1 
HETATM 1260 O  O   . HOH   E 5 .   ? 4.107  10.185  28.333 1.00 49.87  ? 437 HOH   A O   1 
HETATM 1261 O  O   . HOH   E 5 .   ? 20.914 7.344   -5.318 1.00 43.66  ? 438 HOH   A O   1 
HETATM 1262 O  O   . HOH   E 5 .   ? 18.028 9.744   -2.294 1.00 50.51  ? 439 HOH   A O   1 
HETATM 1263 O  O   . HOH   E 5 .   ? 23.459 -6.686  8.247  1.00 80.14  ? 440 HOH   A O   1 
HETATM 1264 O  O   . HOH   E 5 .   ? 4.713  -4.867  3.155  1.00 61.52  ? 441 HOH   A O   1 
HETATM 1265 O  O   . HOH   E 5 .   ? 35.745 11.046  9.988  1.00 59.83  ? 442 HOH   A O   1 
HETATM 1266 O  O   . HOH   E 5 .   ? 8.845  -10.623 8.731  1.00 55.26  ? 443 HOH   A O   1 
HETATM 1267 O  O   . HOH   E 5 .   ? 2.656  2.330   26.636 1.00 40.61  ? 444 HOH   A O   1 
HETATM 1268 O  O   . HOH   E 5 .   ? 36.725 17.707  15.429 1.00 46.71  ? 445 HOH   A O   1 
HETATM 1269 O  O   . HOH   E 5 .   ? 18.287 -6.250  26.278 1.00 47.73  ? 446 HOH   A O   1 
HETATM 1270 O  O   . HOH   E 5 .   ? 0.968  12.499  21.349 1.00 51.97  ? 447 HOH   A O   1 
HETATM 1271 O  O   . HOH   E 5 .   ? 17.674 11.447  -0.323 1.00 45.46  ? 448 HOH   A O   1 
HETATM 1272 O  O   . HOH   E 5 .   ? 18.880 -2.668  18.008 1.00 39.21  ? 449 HOH   A O   1 
HETATM 1273 O  O   . HOH   E 5 .   ? -0.269 23.772  14.658 1.00 50.34  ? 450 HOH   A O   1 
HETATM 1274 O  O   . HOH   E 5 .   ? 22.492 -2.120  31.870 1.00 73.06  ? 451 HOH   A O   1 
HETATM 1275 O  O   . HOH   E 5 .   ? 37.185 17.107  13.070 1.00 58.94  ? 452 HOH   A O   1 
HETATM 1276 O  O   . HOH   E 5 .   ? 29.867 19.810  4.339  1.00 71.60  ? 453 HOH   A O   1 
HETATM 1277 O  O   . HOH   E 5 .   ? 22.974 -2.854  34.838 1.00 61.74  ? 454 HOH   A O   1 
HETATM 1278 O  O   . HOH   E 5 .   ? 18.253 11.688  25.417 1.00 45.22  ? 455 HOH   A O   1 
HETATM 1279 O  O   . HOH   E 5 .   ? 4.822  -1.662  26.378 1.00 46.66  ? 456 HOH   A O   1 
HETATM 1280 O  O   . HOH   E 5 .   ? 3.599  -6.934  14.807 1.00 50.79  ? 457 HOH   A O   1 
HETATM 1281 O  O   . HOH   E 5 .   ? 20.596 15.304  0.231  1.00 53.15  ? 458 HOH   A O   1 
HETATM 1282 O  O   . HOH   E 5 .   ? 9.281  22.902  26.702 1.00 55.48  ? 459 HOH   A O   1 
HETATM 1283 O  O   . HOH   E 5 .   ? 8.679  20.436  6.708  1.00 57.99  ? 460 HOH   A O   1 
HETATM 1284 O  O   . HOH   E 5 .   ? 19.972 9.725   -3.742 1.00 45.18  ? 461 HOH   A O   1 
HETATM 1285 O  O   . HOH   E 5 .   ? 24.320 13.566  0.636  1.00 53.72  ? 462 HOH   A O   1 
HETATM 1286 O  O   . HOH   E 5 .   ? 21.496 -7.005  15.256 1.00 63.29  ? 463 HOH   A O   1 
HETATM 1287 O  O   . HOH   E 5 .   ? 12.586 24.088  14.833 1.00 54.36  ? 464 HOH   A O   1 
HETATM 1288 O  O   . HOH   E 5 .   ? 31.029 2.127   17.227 1.00 56.70  ? 465 HOH   A O   1 
HETATM 1289 O  O   . HOH   E 5 .   ? 32.537 4.189   13.601 1.00 47.52  ? 466 HOH   A O   1 
HETATM 1290 O  O   . HOH   E 5 .   ? 2.741  14.547  22.495 1.00 43.83  ? 467 HOH   A O   1 
HETATM 1291 O  O   . HOH   E 5 .   ? 16.671 14.481  1.510  1.00 52.84  ? 468 HOH   A O   1 
HETATM 1292 O  O   . HOH   E 5 .   ? 8.689  7.537   2.360  1.00 42.73  ? 469 HOH   A O   1 
HETATM 1293 O  O   . HOH   E 5 .   ? 6.195  7.393   30.813 1.00 47.91  ? 470 HOH   A O   1 
HETATM 1294 O  O   . HOH   E 5 .   ? 6.301  5.875   2.213  1.00 66.18  ? 471 HOH   A O   1 
HETATM 1295 O  O   . HOH   E 5 .   ? 31.871 6.418   14.775 1.00 51.43  ? 472 HOH   A O   1 
HETATM 1296 O  O   . HOH   E 5 .   ? 23.830 10.133  22.976 1.00 52.32  ? 473 HOH   A O   1 
HETATM 1297 O  O   . HOH   E 5 .   ? 4.521  -6.844  22.565 1.00 48.86  ? 474 HOH   A O   1 
HETATM 1298 O  O   . HOH   E 5 .   ? 17.784 -7.511  30.690 1.00 71.57  ? 475 HOH   A O   1 
HETATM 1299 O  O   . HOH   E 5 .   ? 38.254 0.405   6.106  1.00 62.56  ? 476 HOH   A O   1 
HETATM 1300 O  O   . HOH   E 5 .   ? 34.757 20.764  6.473  1.00 56.01  ? 477 HOH   A O   1 
HETATM 1301 O  O   . HOH   E 5 .   ? -0.224 12.860  17.554 1.00 59.74  ? 478 HOH   A O   1 
HETATM 1302 O  O   . HOH   E 5 .   ? 21.200 12.175  -3.421 1.00 57.40  ? 479 HOH   A O   1 
HETATM 1303 O  O   . HOH   E 5 .   ? 14.360 12.335  -2.120 1.00 59.54  ? 480 HOH   A O   1 
HETATM 1304 O  O   . HOH   E 5 .   ? 6.493  -8.037  23.874 1.00 48.00  ? 481 HOH   A O   1 
HETATM 1305 O  O   . HOH   E 5 .   ? 4.151  -5.702  25.136 1.00 53.56  ? 482 HOH   A O   1 
HETATM 1306 O  O   . HOH   E 5 .   ? 24.737 11.726  -2.798 1.00 66.40  ? 483 HOH   A O   1 
HETATM 1307 O  O   . HOH   E 5 .   ? 34.641 11.884  2.647  1.00 67.94  ? 484 HOH   A O   1 
HETATM 1308 O  O   . HOH   E 5 .   ? 8.122  12.835  29.777 1.00 54.32  ? 485 HOH   A O   1 
HETATM 1309 O  O   . HOH   E 5 .   ? 42.440 8.091   8.335  1.00 66.87  ? 486 HOH   A O   1 
HETATM 1310 O  O   . HOH   E 5 .   ? 40.268 -2.029  2.335  1.00 75.31  ? 487 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   ? 0.4192 0.5098 0.4126 -0.0606 -0.1107 0.0233  7   SER   A N   
2    C CA  . SER   A 1   ? 0.4083 0.5150 0.4383 -0.0571 -0.1170 0.0319  7   SER   A CA  
3    C C   . SER   A 1   ? 0.3899 0.5113 0.4488 -0.0454 -0.1083 0.0387  7   SER   A C   
4    O O   . SER   A 1   ? 0.3971 0.5172 0.4481 -0.0418 -0.1022 0.0392  7   SER   A O   
5    C CB  . SER   A 1   ? 0.4265 0.5354 0.4602 -0.0686 -0.1387 0.0434  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4561 0.5692 0.4906 -0.0698 -0.1472 0.0557  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3597 0.4925 0.4498 -0.0401 -0.1054 0.0428  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3407 0.4831 0.4557 -0.0307 -0.0944 0.0479  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3226 0.4705 0.4574 -0.0254 -0.0841 0.0455  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3295 0.4742 0.4556 -0.0265 -0.0823 0.0378  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2890 0.4435 0.4496 -0.0197 -0.0752 0.0520  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2788 0.4360 0.4551 -0.0157 -0.0634 0.0503  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2736 0.4298 0.4599 -0.0103 -0.0463 0.0511  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2841 0.4400 0.4780 -0.0087 -0.0448 0.0567  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2704 0.4344 0.4764 -0.0176 -0.0710 0.0597  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2616 0.4155 0.4473 -0.0085 -0.0329 0.0461  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2604 0.4089 0.4517 -0.0060 -0.0142 0.0453  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2728 0.4231 0.4973 -0.0038 -0.0061 0.0535  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2708 0.4247 0.5013 -0.0049 -0.0104 0.0543  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2651 0.4075 0.4286 -0.0083 -0.0048 0.0349  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2683 0.4111 0.4052 -0.0103 -0.0134 0.0283  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2804 0.4126 0.4422 -0.0089 0.0152  0.0324  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2682 0.4106 0.3849 -0.0134 -0.0115 0.0222  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2718 0.4191 0.5206 -0.0005 0.0071  0.0600  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2820 0.4299 0.5677 0.0023  0.0189  0.0687  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3039 0.4363 0.5828 0.0027  0.0467  0.0622  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3247 0.4492 0.6093 0.0045  0.0597  0.0626  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2734 0.4307 0.6024 0.0055  0.0120  0.0851  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2858 0.4562 0.6184 0.0017  -0.0165 0.0921  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2914 0.4696 0.6422 -0.0007 -0.0258 0.0970  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3108 0.4832 0.6227 -0.0012 -0.0333 0.0919  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2960 0.4826 0.6436 -0.0070 -0.0516 0.1012  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3214 0.5011 0.6275 -0.0075 -0.0580 0.0962  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3129 0.4993 0.6366 -0.0110 -0.0675 0.1006  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3214 0.5114 0.6338 -0.0196 -0.0913 0.1027  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3031 0.4288 0.5656 -0.0002 0.0562  0.0555  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3296 0.4367 0.5766 -0.0031 0.0828  0.0481  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3449 0.4479 0.6159 -0.0018 0.0980  0.0533  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3441 0.4542 0.6133 -0.0029 0.0883  0.0546  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3607 0.4601 0.5563 -0.0107 0.0811  0.0352  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3600 0.4709 0.5427 -0.0123 0.0618  0.0351  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3823 0.4600 0.5554 -0.0173 0.1072  0.0276  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3519 0.4433 0.6496 0.0010  0.1232  0.0572  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3542 0.4397 0.6805 0.0028  0.1427  0.0631  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3379 0.4451 0.7060 0.0073  0.1231  0.0767  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3305 0.4539 0.7268 0.0109  0.1040  0.0867  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3344 0.4420 0.6999 0.0053  0.1241  0.0765  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3134 0.4403 0.7141 0.0074  0.1043  0.0876  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2959 0.4322 0.6635 0.0033  0.0776  0.0814  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2854 0.4283 0.6623 0.0021  0.0696  0.0844  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3397 0.4622 0.7730 0.0090  0.1240  0.0945  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4044 0.5229 0.8883 0.0148  0.1468  0.1053  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3986 0.5346 0.9333 0.0190  0.1337  0.1207  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4500 0.5443 0.9200 0.0142  0.1811  0.0981  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2911 0.4270 0.6222 0.0012  0.0655  0.0729  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2862 0.4291 0.5873 -0.0022 0.0431  0.0668  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2658 0.4181 0.5643 -0.0020 0.0218  0.0677  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2570 0.4074 0.5594 -0.0002 0.0256  0.0691  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2982 0.4302 0.5516 -0.0064 0.0499  0.0553  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3139 0.4351 0.5585 -0.0091 0.0676  0.0543  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3270 0.4536 0.5886 -0.0086 0.0640  0.0596  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3349 0.4387 0.5509 -0.0137 0.0879  0.0478  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3475 0.4631 0.5997 -0.0114 0.0810  0.0597  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3600 0.4512 0.5619 -0.0181 0.1045  0.0471  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3781 0.4757 0.5980 -0.0165 0.1009  0.0536  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4241 0.5083 0.6291 -0.0211 0.1182  0.0539  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2567 0.4167 0.5472 -0.0047 0.0013  0.0666  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2538 0.4189 0.5323 -0.0067 -0.0183 0.0655  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2653 0.4268 0.5067 -0.0093 -0.0243 0.0547  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2716 0.4338 0.5118 -0.0109 -0.0279 0.0533  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2530 0.4281 0.5586 -0.0098 -0.0371 0.0752  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2771 0.4534 0.5611 -0.0151 -0.0579 0.0725  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3107 0.4958 0.6208 -0.0210 -0.0773 0.0839  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3558 0.5369 0.6393 -0.0296 -0.0950 0.0775  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3787 0.5561 0.6380 -0.0351 -0.1083 0.0758  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3663 0.5454 0.6256 -0.0321 -0.1073 0.0810  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3687 0.5381 0.6013 -0.0441 -0.1204 0.0683  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2513 0.4091 0.4663 -0.0093 -0.0244 0.0481  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2542 0.4096 0.4403 -0.0111 -0.0285 0.0399  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2541 0.4101 0.4296 -0.0132 -0.0429 0.0376  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2528 0.4083 0.4245 -0.0130 -0.0451 0.0386  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2653 0.4158 0.4289 -0.0111 -0.0174 0.0344  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2649 0.4158 0.4075 -0.0128 -0.0218 0.0295  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2708 0.4158 0.4390 -0.0114 -0.0007 0.0359  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2485 0.4032 0.4177 -0.0159 -0.0509 0.0345  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2600 0.4103 0.4139 -0.0199 -0.0622 0.0308  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2657 0.4101 0.4019 -0.0202 -0.0595 0.0230  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2635 0.4099 0.4045 -0.0177 -0.0527 0.0232  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2752 0.4260 0.4419 -0.0260 -0.0757 0.0355  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2845 0.4433 0.4767 -0.0255 -0.0795 0.0466  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2785 0.4287 0.4560 -0.0275 -0.0753 0.0347  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2592 0.3955 0.3767 -0.0237 -0.0640 0.0174  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2647 0.3933 0.3714 -0.0240 -0.0592 0.0109  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2799 0.4050 0.3973 -0.0273 -0.0622 0.0108  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2819 0.4043 0.4015 -0.0337 -0.0723 0.0120  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2747 0.3909 0.3579 -0.0285 -0.0608 0.0042  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2943 0.4125 0.3672 -0.0252 -0.0564 0.0038  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3112 0.4310 0.3798 -0.0267 -0.0618 0.0068  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2725 0.3920 0.3450 -0.0209 -0.0471 0.0017  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2900 0.4155 0.4155 -0.0239 -0.0547 0.0107  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3044 0.4257 0.4418 -0.0267 -0.0556 0.0107  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3338 0.4395 0.4571 -0.0355 -0.0608 0.0031  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3411 0.4445 0.4714 -0.0421 -0.0689 0.0039  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3095 0.4322 0.4565 -0.0214 -0.0459 0.0129  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3168 0.4375 0.4808 -0.0227 -0.0452 0.0153  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3107 0.4308 0.4831 -0.0178 -0.0357 0.0183  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3293 0.4472 0.5193 -0.0179 -0.0327 0.0219  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3454 0.4494 0.5389 -0.0214 -0.0293 0.0164  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3442 0.4333 0.5211 -0.0268 -0.0288 0.0059  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3056 0.4083 0.5175 -0.0207 -0.0253 0.0209  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3492 0.4431 0.4510 -0.0372 -0.0564 -0.0042 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3695 0.4431 0.4490 -0.0478 -0.0584 -0.0134 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3838 0.4560 0.4496 -0.0580 -0.0750 -0.0120 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4047 0.4599 0.4506 -0.0704 -0.0807 -0.0183 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3840 0.4428 0.4450 -0.0467 -0.0449 -0.0215 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4060 0.4666 0.4503 -0.0455 -0.0457 -0.0215 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4206 0.4968 0.4771 -0.0356 -0.0412 -0.0158 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4245 0.4709 0.4390 -0.0541 -0.0494 -0.0269 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4259 0.4982 0.4634 -0.0374 -0.0421 -0.0177 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4329 0.4874 0.4446 -0.0481 -0.0465 -0.0239 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3769 0.4658 0.4543 -0.0541 -0.0829 -0.0027 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3911 0.4823 0.4640 -0.0629 -0.0998 0.0030  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3872 0.4945 0.4937 -0.0625 -0.1093 0.0142  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3872 0.5004 0.4998 -0.0688 -0.1243 0.0228  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3940 0.4898 0.4564 -0.0594 -0.1007 0.0065  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4226 0.5025 0.4528 -0.0607 -0.0915 -0.0031 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4248 0.5107 0.4488 -0.0570 -0.0925 0.0018  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4518 0.5091 0.4499 -0.0754 -0.0966 -0.0113 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3817 0.4965 0.5121 -0.0550 -0.1003 0.0159  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3819 0.5105 0.5460 -0.0539 -0.1053 0.0264  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4013 0.5268 0.5717 -0.0672 -0.1220 0.0292  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4170 0.5267 0.5663 -0.0764 -0.1244 0.0199  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3713 0.5042 0.5528 -0.0453 -0.0913 0.0266  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3998 0.5395 0.6001 -0.0689 -0.1329 0.0424  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4193 0.5604 0.6326 -0.0828 -0.1522 0.0488  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4211 0.5673 0.6666 -0.0817 -0.1478 0.0516  24  THR   A C   
137  O O   . THR   A 18  ? 0.4159 0.5650 0.6730 -0.0698 -0.1298 0.0499  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4358 0.5917 0.6709 -0.0857 -0.1680 0.0652  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4376 0.6098 0.7152 -0.0731 -0.1568 0.0761  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4537 0.6046 0.6582 -0.0871 -0.1728 0.0643  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4275 0.5747 0.6868 -0.0952 -0.1648 0.0566  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4340 0.5864 0.7267 -0.0957 -0.1622 0.0605  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3997 0.5710 0.7376 -0.0828 -0.1520 0.0742  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3872 0.5593 0.7417 -0.0749 -0.1360 0.0733  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4879 0.6388 0.7867 -0.1151 -0.1859 0.0648  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6054 0.7316 0.8567 -0.1293 -0.1906 0.0483  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6604 0.7780 0.8854 -0.1490 -0.2136 0.0484  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6506 0.7577 0.8762 -0.1263 -0.1732 0.0321  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6978 0.7887 0.8795 -0.1580 -0.2073 0.0302  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6961 0.7806 0.8801 -0.1439 -0.1825 0.0204  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3870 0.5713 0.7430 -0.0802 -0.1583 0.0867  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3764 0.5748 0.7745 -0.0678 -0.1441 0.0989  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3596 0.5511 0.7394 -0.0537 -0.1180 0.0891  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3603 0.5549 0.7635 -0.0459 -0.1011 0.0926  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4130 0.6236 0.8316 -0.0671 -0.1534 0.1134  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4924 0.7193 0.9720 -0.0617 -0.1477 0.1316  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5064 0.7415 1.0208 -0.0688 -0.1577 0.1409  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5149 0.7454 1.0103 -0.0496 -0.1303 0.1371  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3468 0.5282 0.6840 -0.0518 -0.1153 0.0774  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3242 0.4998 0.6422 -0.0414 -0.0950 0.0691  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3030 0.4730 0.6208 -0.0399 -0.0849 0.0640  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2948 0.4656 0.6189 -0.0321 -0.0681 0.0655  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3320 0.4986 0.6083 -0.0414 -0.0964 0.0585  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3441 0.5149 0.6168 -0.0403 -0.1013 0.0631  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3292 0.5079 0.6259 -0.0339 -0.0928 0.0716  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3635 0.5277 0.6086 -0.0460 -0.1116 0.0581  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2982 0.4601 0.6054 -0.0480 -0.0938 0.0576  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3026 0.4584 0.6122 -0.0466 -0.0842 0.0538  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2871 0.4511 0.6361 -0.0454 -0.0793 0.0641  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2773 0.4398 0.6317 -0.0394 -0.0644 0.0651  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3099 0.4524 0.6021 -0.0567 -0.0932 0.0444  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3311 0.4617 0.5868 -0.0554 -0.0894 0.0334  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3561 0.4778 0.5847 -0.0630 -0.0991 0.0266  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3335 0.4602 0.5780 -0.0464 -0.0742 0.0296  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3735 0.4854 0.5768 -0.0582 -0.0885 0.0179  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3599 0.4760 0.5748 -0.0480 -0.0743 0.0205  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3304 0.4615 0.5870 -0.0379 -0.0610 0.0346  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3670 0.4791 0.5708 -0.0407 -0.0620 0.0171  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3463 0.4735 0.5885 -0.0319 -0.0514 0.0319  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3599 0.4791 0.5788 -0.0327 -0.0520 0.0239  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2791 0.4523 0.6568 -0.0517 -0.0920 0.0732  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2732 0.4555 0.6950 -0.0507 -0.0871 0.0847  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2710 0.4578 0.7061 -0.0389 -0.0661 0.0908  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2698 0.4578 0.7294 -0.0353 -0.0519 0.0966  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2660 0.4594 0.7191 -0.0607 -0.1077 0.0956  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2678 0.4553 0.6869 -0.0341 -0.0630 0.0897  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2621 0.4496 0.6884 -0.0250 -0.0417 0.0935  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2569 0.4343 0.6397 -0.0203 -0.0301 0.0828  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2564 0.4317 0.6289 -0.0159 -0.0195 0.0820  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2736 0.4694 0.7219 -0.0236 -0.0452 0.1023  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3084 0.5167 0.8075 -0.0282 -0.0563 0.1168  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3263 0.5376 0.8617 -0.0254 -0.0429 0.1250  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3130 0.5287 0.8158 -0.0365 -0.0814 0.1212  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2456 0.4169 0.6056 -0.0220 -0.0324 0.0756  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2535 0.4177 0.5768 -0.0190 -0.0257 0.0680  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2620 0.4220 0.5788 -0.0148 -0.0060 0.0705  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2564 0.4150 0.5914 -0.0144 0.0046  0.0762  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2476 0.4069 0.5591 -0.0216 -0.0317 0.0630  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2638 0.4181 0.5454 -0.0185 -0.0262 0.0584  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2686 0.4227 0.5264 -0.0181 -0.0322 0.0521  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2612 0.4102 0.5422 -0.0199 -0.0282 0.0565  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2636 0.4200 0.5525 -0.0132 -0.0007 0.0662  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2788 0.4278 0.5503 -0.0125 0.0168  0.0669  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2840 0.4306 0.5243 -0.0138 0.0129  0.0640  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2956 0.4381 0.5280 -0.0151 0.0205  0.0681  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2921 0.4374 0.5558 -0.0117 0.0261  0.0647  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3174 0.4513 0.5489 -0.0144 0.0417  0.0623  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2761 0.4236 0.5780 -0.0094 0.0338  0.0711  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2695 0.4193 0.4954 -0.0137 0.0009  0.0587  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2756 0.4253 0.4800 -0.0143 -0.0031 0.0580  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2605 0.4131 0.4613 -0.0134 -0.0154 0.0522  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2574 0.4109 0.4571 -0.0134 -0.0195 0.0479  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2850 0.4312 0.4617 -0.0172 0.0043  0.0582  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2936 0.4430 0.4513 -0.0187 -0.0030 0.0592  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3051 0.4555 0.4566 -0.0206 -0.0040 0.0670  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2872 0.4400 0.4334 -0.0186 -0.0103 0.0543  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3097 0.4656 0.4503 -0.0215 -0.0123 0.0683  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2989 0.4559 0.4357 -0.0203 -0.0154 0.0599  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2870 0.4401 0.4321 -0.0172 -0.0130 0.0472  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3036 0.4653 0.4323 -0.0205 -0.0221 0.0580  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2970 0.4532 0.4296 -0.0176 -0.0188 0.0444  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3021 0.4627 0.4282 -0.0191 -0.0230 0.0494  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2487 0.4013 0.4478 -0.0128 -0.0196 0.0527  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2513 0.4030 0.4448 -0.0123 -0.0269 0.0467  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2558 0.4087 0.4447 -0.0107 -0.0262 0.0505  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2520 0.4060 0.4480 -0.0102 -0.0229 0.0584  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2593 0.4061 0.4652 -0.0142 -0.0327 0.0418  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2937 0.4377 0.5175 -0.0148 -0.0303 0.0456  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3291 0.4675 0.5549 -0.0136 -0.0280 0.0452  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3484 0.4843 0.5894 -0.0135 -0.0243 0.0497  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.3385 0.4745 0.5533 -0.0125 -0.0285 0.0412  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2577 0.4106 0.4384 -0.0098 -0.0289 0.0463  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2558 0.4115 0.4395 -0.0077 -0.0280 0.0519  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2555 0.4052 0.4390 -0.0064 -0.0278 0.0441  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2477 0.3980 0.4183 -0.0071 -0.0297 0.0390  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2835 0.4475 0.4539 -0.0096 -0.0296 0.0582  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3501 0.5211 0.5281 -0.0087 -0.0314 0.0688  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3597 0.5286 0.5533 -0.0048 -0.0293 0.0686  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3661 0.5439 0.5347 -0.0128 -0.0347 0.0780  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2508 0.3925 0.4475 -0.0051 -0.0236 0.0430  36  SER   A N   
241  C CA  . SER   A 30  ? 0.2776 0.4080 0.4727 -0.0049 -0.0190 0.0347  36  SER   A CA  
242  C C   . SER   A 30  ? 0.2755 0.4118 0.4710 -0.0017 -0.0165 0.0384  36  SER   A C   
243  O O   . SER   A 30  ? 0.2902 0.4194 0.4748 -0.0025 -0.0140 0.0301  36  SER   A O   
244  C CB  . SER   A 30  ? 0.3116 0.4313 0.5242 -0.0040 -0.0112 0.0350  36  SER   A CB  
245  O OG  . SER   A 30  ? 0.3661 0.4698 0.5736 -0.0053 -0.0034 0.0250  36  SER   A OG  
246  N N   . SER   A 31  ? 0.2518 0.4011 0.4599 0.0008  -0.0178 0.0519  37  SER   A N   
247  C CA  . SER   A 31  ? 0.2623 0.4199 0.4765 0.0028  -0.0173 0.0581  37  SER   A CA  
248  C C   . SER   A 31  ? 0.2556 0.4191 0.4486 -0.0003 -0.0233 0.0538  37  SER   A C   
249  O O   . SER   A 31  ? 0.2641 0.4318 0.4605 0.0006  -0.0223 0.0556  37  SER   A O   
250  C CB  . SER   A 31  ? 0.2919 0.4626 0.5273 0.0045  -0.0198 0.0763  37  SER   A CB  
251  O OG  . SER   A 31  ? 0.3458 0.5255 0.5684 0.0000  -0.0285 0.0834  37  SER   A OG  
252  N N   . ARG   A 32  ? 0.2445 0.4072 0.4189 -0.0037 -0.0279 0.0482  38  ARG   A N   
253  C CA  . ARG   A 32  ? 0.2422 0.4076 0.3977 -0.0066 -0.0314 0.0431  38  ARG   A CA  
254  C C   . ARG   A 32  ? 0.2449 0.3994 0.3885 -0.0070 -0.0305 0.0308  38  ARG   A C   
255  O O   . ARG   A 32  ? 0.2410 0.3962 0.3713 -0.0086 -0.0323 0.0268  38  ARG   A O   
256  C CB  . ARG   A 32  ? 0.2544 0.4247 0.3987 -0.0105 -0.0348 0.0468  38  ARG   A CB  
257  C CG  . ARG   A 32  ? 0.2633 0.4432 0.4093 -0.0136 -0.0383 0.0593  38  ARG   A CG  
258  C CD  . ARG   A 32  ? 0.2792 0.4587 0.4070 -0.0197 -0.0387 0.0610  38  ARG   A CD  
259  N NE  . ARG   A 32  ? 0.2743 0.4512 0.3833 -0.0234 -0.0378 0.0534  38  ARG   A NE  
260  C CZ  . ARG   A 32  ? 0.2810 0.4564 0.3697 -0.0312 -0.0371 0.0545  38  ARG   A CZ  
261  N NH1 . ARG   A 32  ? 0.2668 0.4431 0.3476 -0.0370 -0.0385 0.0634  38  ARG   A NH1 
262  N NH2 . ARG   A 32  ? 0.2881 0.4591 0.3622 -0.0342 -0.0342 0.0468  38  ARG   A NH2 
263  N N   . ASP   A 33  ? 0.2509 0.3949 0.3984 -0.0070 -0.0285 0.0257  39  ASP   A N   
264  C CA  . ASP   A 33  ? 0.2561 0.3897 0.3907 -0.0103 -0.0310 0.0163  39  ASP   A CA  
265  C C   . ASP   A 33  ? 0.2570 0.3963 0.3866 -0.0121 -0.0371 0.0174  39  ASP   A C   
266  O O   . ASP   A 33  ? 0.2563 0.3927 0.3750 -0.0141 -0.0406 0.0133  39  ASP   A O   
267  C CB  . ASP   A 33  ? 0.2747 0.3999 0.3957 -0.0110 -0.0276 0.0094  39  ASP   A CB  
268  C CG  . ASP   A 33  ? 0.2983 0.4113 0.4014 -0.0167 -0.0321 0.0013  39  ASP   A CG  
269  O OD1 . ASP   A 33  ? 0.2810 0.3857 0.3844 -0.0209 -0.0349 -0.0016 39  ASP   A OD1 
270  O OD2 . ASP   A 33  ? 0.3129 0.4253 0.4019 -0.0179 -0.0343 -0.0010 39  ASP   A OD2 
271  N N   . LEU   A 34  ? 0.2496 0.3960 0.3885 -0.0114 -0.0370 0.0237  40  LEU   A N   
272  C CA  . LEU   A 34  ? 0.2462 0.3960 0.3853 -0.0125 -0.0384 0.0254  40  LEU   A CA  
273  C C   . LEU   A 34  ? 0.2459 0.3951 0.4002 -0.0133 -0.0390 0.0285  40  LEU   A C   
274  O O   . LEU   A 34  ? 0.2513 0.4000 0.4145 -0.0127 -0.0369 0.0314  40  LEU   A O   
275  C CB  . LEU   A 34  ? 0.2485 0.4042 0.3812 -0.0126 -0.0340 0.0296  40  LEU   A CB  
276  C CG  . LEU   A 34  ? 0.2690 0.4264 0.3876 -0.0133 -0.0337 0.0272  40  LEU   A CG  
277  C CD1 . LEU   A 34  ? 0.2687 0.4289 0.3778 -0.0166 -0.0299 0.0306  40  LEU   A CD1 
278  C CD2 . LEU   A 34  ? 0.2720 0.4257 0.3861 -0.0132 -0.0355 0.0221  40  LEU   A CD2 
279  N N   . LEU   A 35  ? 0.2269 0.3772 0.3879 -0.0145 -0.0412 0.0294  41  LEU   A N   
280  C CA  . LEU   A 35  ? 0.2310 0.3825 0.4116 -0.0155 -0.0414 0.0338  41  LEU   A CA  
281  C C   . LEU   A 35  ? 0.2374 0.3924 0.4262 -0.0145 -0.0372 0.0376  41  LEU   A C   
282  O O   . LEU   A 35  ? 0.2523 0.4076 0.4355 -0.0145 -0.0398 0.0363  41  LEU   A O   
283  C CB  . LEU   A 35  ? 0.2375 0.3851 0.4253 -0.0199 -0.0514 0.0315  41  LEU   A CB  
284  C CG  . LEU   A 35  ? 0.2534 0.4037 0.4661 -0.0220 -0.0533 0.0372  41  LEU   A CG  
285  C CD1 . LEU   A 35  ? 0.2635 0.4070 0.4792 -0.0268 -0.0584 0.0338  41  LEU   A CD1 
286  C CD2 . LEU   A 35  ? 0.2651 0.4207 0.4926 -0.0241 -0.0599 0.0422  41  LEU   A CD2 
287  N N   . VAL   A 36  ? 0.2322 0.3881 0.4342 -0.0135 -0.0283 0.0427  42  VAL   A N   
288  C CA  . VAL   A 36  ? 0.2373 0.3935 0.4516 -0.0123 -0.0193 0.0467  42  VAL   A CA  
289  C C   . VAL   A 36  ? 0.2469 0.4061 0.4931 -0.0126 -0.0192 0.0535  42  VAL   A C   
290  O O   . VAL   A 36  ? 0.2370 0.3954 0.4886 -0.0131 -0.0168 0.0552  42  VAL   A O   
291  C CB  . VAL   A 36  ? 0.2583 0.4088 0.4560 -0.0124 -0.0039 0.0459  42  VAL   A CB  
292  C CG1 . VAL   A 36  ? 0.2685 0.4149 0.4812 -0.0114 0.0105  0.0492  42  VAL   A CG1 
293  C CG2 . VAL   A 36  ? 0.2692 0.4182 0.4380 -0.0138 -0.0059 0.0403  42  VAL   A CG2 
294  N N   . SER   A 37  ? 0.2500 0.4137 0.5195 -0.0125 -0.0232 0.0588  43  SER   A N   
295  C CA  . SER   A 37  ? 0.2583 0.4273 0.5652 -0.0132 -0.0243 0.0677  43  SER   A CA  
296  C C   . SER   A 37  ? 0.2687 0.4382 0.6014 -0.0094 -0.0087 0.0752  43  SER   A C   
297  O O   . SER   A 37  ? 0.2660 0.4314 0.5870 -0.0071 -0.0007 0.0729  43  SER   A O   
298  C CB  . SER   A 37  ? 0.2706 0.4460 0.5893 -0.0186 -0.0459 0.0706  43  SER   A CB  
299  O OG  . SER   A 37  ? 0.3075 0.4856 0.6232 -0.0189 -0.0536 0.0726  43  SER   A OG  
300  N N   . SER   A 38  ? 0.2687 0.4417 0.6386 -0.0087 -0.0021 0.0842  44  SER   A N   
301  C CA  . SER   A 38  ? 0.2864 0.4578 0.6865 -0.0045 0.0168  0.0920  44  SER   A CA  
302  C C   . SER   A 38  ? 0.2950 0.4779 0.7317 -0.0040 0.0050  0.1035  44  SER   A C   
303  O O   . SER   A 38  ? 0.2955 0.4884 0.7398 -0.0089 -0.0193 0.1075  44  SER   A O   
304  C CB  . SER   A 38  ? 0.3071 0.4761 0.7338 -0.0035 0.0329  0.0977  44  SER   A CB  
305  O OG  . SER   A 38  ? 0.3282 0.5086 0.7847 -0.0067 0.0159  0.1050  44  SER   A OG  
306  N N   . THR   A 39  ? 0.3039 0.4838 0.7604 0.0008  0.0217  0.1089  45  THR   A N   
307  C CA  . THR   A 39  ? 0.3132 0.5048 0.8114 0.0022  0.0123  0.1235  45  THR   A CA  
308  C C   . THR   A 39  ? 0.3339 0.5255 0.8862 0.0077  0.0356  0.1364  45  THR   A C   
309  O O   . THR   A 39  ? 0.3465 0.5230 0.8913 0.0107  0.0645  0.1302  45  THR   A O   
310  C CB  . THR   A 39  ? 0.3254 0.5136 0.8015 0.0038  0.0101  0.1200  45  THR   A CB  
311  O OG1 . THR   A 39  ? 0.3389 0.5122 0.8090 0.0087  0.0399  0.1149  45  THR   A OG1 
312  C CG2 . THR   A 39  ? 0.3375 0.5235 0.7609 -0.0009 -0.0081 0.1070  45  THR   A CG2 
313  N N   . THR   A 40  ? 0.3323 0.5397 0.9391 0.0083  0.0241  0.1552  46  THR   A N   
314  C CA  . THR   A 40  ? 0.3438 0.5527 1.0119 0.0145  0.0469  0.1705  46  THR   A CA  
315  C C   . THR   A 40  ? 0.3551 0.5551 1.0315 0.0211  0.0670  0.1727  46  THR   A C   
316  O O   . THR   A 40  ? 0.3599 0.5472 1.0617 0.0271  0.1010  0.1749  46  THR   A O   
317  C CB  . THR   A 40  ? 0.3521 0.5844 1.0817 0.0112  0.0237  0.1925  46  THR   A CB  
318  O OG1 . THR   A 40  ? 0.3775 0.6227 1.1032 0.0064  -0.0076 0.2001  46  THR   A OG1 
319  C CG2 . THR   A 40  ? 0.3598 0.5974 1.0853 0.0044  0.0098  0.1895  46  THR   A CG2 
320  N N   . ALA   A 41  ? 0.3589 0.5628 1.0125 0.0196  0.0484  0.1716  47  ALA   A N   
321  C CA  . ALA   A 41  ? 0.3573 0.5527 1.0174 0.0253  0.0654  0.1737  47  ALA   A CA  
322  C C   . ALA   A 41  ? 0.3798 0.5527 0.9746 0.0247  0.0827  0.1503  47  ALA   A C   
323  O O   . ALA   A 41  ? 0.3937 0.5646 0.9363 0.0193  0.0685  0.1358  47  ALA   A O   
324  C CB  . ALA   A 41  ? 0.3494 0.5613 1.0222 0.0234  0.0354  0.1874  47  ALA   A CB  
325  N N   . GLN   A 42  ? 0.3756 0.5311 0.9747 0.0294  0.1134  0.1473  48  GLN   A N   
326  C CA  . GLN   A 42  ? 0.3989 0.5326 0.9363 0.0265  0.1288  0.1259  48  GLN   A CA  
327  C C   . GLN   A 42  ? 0.3777 0.5160 0.8851 0.0248  0.1082  0.1219  48  GLN   A C   
328  O O   . GLN   A 42  ? 0.3628 0.5113 0.9035 0.0283  0.0990  0.1362  48  GLN   A O   
329  C CB  . GLN   A 42  ? 0.4514 0.5604 0.9987 0.0296  0.1712  0.1218  48  GLN   A CB  
330  C CG  . GLN   A 42  ? 0.5544 0.6458 1.0884 0.0268  0.1976  0.1129  48  GLN   A CG  
331  C CD  . GLN   A 42  ? 0.6627 0.7212 1.1612 0.0233  0.2342  0.0972  48  GLN   A CD  
332  O OE1 . GLN   A 42  ? 0.6902 0.7293 1.2106 0.0249  0.2702  0.0980  48  GLN   A OE1 
333  N NE2 . GLN   A 42  ? 0.6941 0.7443 1.1368 0.0174  0.2266  0.0823  48  GLN   A NE2 
334  N N   . GLY   A 43  ? 0.3689 0.4997 0.8155 0.0192  0.1015  0.1040  49  GLY   A N   
335  C CA  . GLY   A 43  ? 0.3635 0.4960 0.7766 0.0170  0.0853  0.0978  49  GLY   A CA  
336  C C   . GLY   A 43  ? 0.3590 0.4715 0.7531 0.0170  0.1101  0.0882  49  GLY   A C   
337  O O   . GLY   A 43  ? 0.3721 0.4657 0.7636 0.0163  0.1397  0.0816  49  GLY   A O   
338  N N   . CYS   A 44  ? 0.3405 0.4546 0.7176 0.0166  0.0990  0.0864  50  CYS   A N   
339  C CA  . CYS   A 44  ? 0.3432 0.4390 0.7055 0.0161  0.1205  0.0782  50  CYS   A CA  
340  C C   . CYS   A 44  ? 0.3415 0.4298 0.6453 0.0090  0.1143  0.0608  50  CYS   A C   
341  O O   . CYS   A 44  ? 0.3510 0.4248 0.6408 0.0071  0.1292  0.0538  50  CYS   A O   
342  C CB  . CYS   A 44  ? 0.3507 0.4528 0.7537 0.0225  0.1188  0.0939  50  CYS   A CB  
343  S SG  . CYS   A 44  ? 0.3907 0.5019 0.8730 0.0309  0.1290  0.1180  50  CYS   A SG  
344  N N   . ASP   A 45  ? 0.3288 0.4268 0.6024 0.0049  0.0935  0.0548  51  ASP   A N   
345  C CA  . ASP   A 45  ? 0.3386 0.4320 0.5634 -0.0017 0.0869  0.0408  51  ASP   A CA  
346  C C   . ASP   A 45  ? 0.3563 0.4320 0.5488 -0.0095 0.1059  0.0279  51  ASP   A C   
347  O O   . ASP   A 45  ? 0.3559 0.4259 0.5569 -0.0099 0.1183  0.0290  51  ASP   A O   
348  C CB  . ASP   A 45  ? 0.3422 0.4522 0.5515 -0.0026 0.0587  0.0410  51  ASP   A CB  
349  C CG  . ASP   A 45  ? 0.3983 0.5212 0.6257 0.0013  0.0394  0.0514  51  ASP   A CG  
350  O OD1 . ASP   A 45  ? 0.4198 0.5395 0.6568 0.0036  0.0440  0.0554  51  ASP   A OD1 
351  O OD2 . ASP   A 45  ? 0.3823 0.5171 0.6126 0.0011  0.0201  0.0556  51  ASP   A OD2 
352  N N   . THR   A 46  ? 0.3637 0.4300 0.5191 -0.0169 0.1081  0.0166  52  THR   A N   
353  C CA  . THR   A 46  ? 0.3893 0.4384 0.5050 -0.0281 0.1212  0.0045  52  THR   A CA  
354  C C   . THR   A 46  ? 0.3727 0.4340 0.4574 -0.0335 0.0981  0.0006  52  THR   A C   
355  O O   . THR   A 46  ? 0.3616 0.4331 0.4454 -0.0313 0.0835  0.0011  52  THR   A O   
356  C CB  . THR   A 46  ? 0.4499 0.4773 0.5511 -0.0342 0.1422  -0.0043 52  THR   A CB  
357  O OG1 . THR   A 46  ? 0.4670 0.4781 0.5951 -0.0306 0.1700  -0.0018 52  THR   A OG1 
358  C CG2 . THR   A 46  ? 0.4910 0.5027 0.5405 -0.0499 0.1468  -0.0178 52  THR   A CG2 
359  N N   . ILE   A 47  ? 0.3615 0.4220 0.4245 -0.0399 0.0953  -0.0017 53  ILE   A N   
360  C CA  . ILE   A 47  ? 0.3588 0.4311 0.3984 -0.0447 0.0749  -0.0029 53  ILE   A CA  
361  C C   . ILE   A 47  ? 0.3804 0.4398 0.3826 -0.0583 0.0799  -0.0119 53  ILE   A C   
362  O O   . ILE   A 47  ? 0.4027 0.4415 0.3836 -0.0678 0.0983  -0.0179 53  ILE   A O   
363  C CB  . ILE   A 47  ? 0.3518 0.4312 0.3889 -0.0453 0.0673  0.0016  53  ILE   A CB  
364  C CG1 . ILE   A 47  ? 0.3383 0.4277 0.4131 -0.0341 0.0646  0.0099  53  ILE   A CG1 
365  C CG2 . ILE   A 47  ? 0.3543 0.4477 0.3757 -0.0487 0.0463  0.0030  53  ILE   A CG2 
366  C CD1 . ILE   A 47  ? 0.3240 0.4293 0.4207 -0.0255 0.0471  0.0144  53  ILE   A CD1 
367  N N   . ALA   A 48  ? 0.3650 0.4346 0.3583 -0.0604 0.0645  -0.0129 54  ALA   A N   
368  C CA  . ALA   A 48  ? 0.3726 0.4335 0.3328 -0.0747 0.0645  -0.0198 54  ALA   A CA  
369  C C   . ALA   A 48  ? 0.3746 0.4350 0.3073 -0.0865 0.0577  -0.0182 54  ALA   A C   
370  O O   . ALA   A 48  ? 0.3474 0.4230 0.2906 -0.0813 0.0445  -0.0103 54  ALA   A O   
371  C CB  . ALA   A 48  ? 0.3664 0.4423 0.3318 -0.0725 0.0481  -0.0184 54  ALA   A CB  
372  N N   . ARG   A 49  ? 0.4066 0.4484 0.3029 -0.1033 0.0667  -0.0252 55  ARG   A N   
373  C CA  . ARG   A 49  ? 0.4267 0.4669 0.2909 -0.1181 0.0578  -0.0223 55  ARG   A CA  
374  C C   . ARG   A 49  ? 0.4514 0.4904 0.2896 -0.1339 0.0476  -0.0259 55  ARG   A C   
375  O O   . ARG   A 49  ? 0.4803 0.4956 0.2876 -0.1485 0.0617  -0.0362 55  ARG   A O   
376  C CB  . ARG   A 49  ? 0.4509 0.4648 0.2891 -0.1274 0.0798  -0.0275 55  ARG   A CB  
377  C CG  . ARG   A 49  ? 0.4737 0.4884 0.3423 -0.1122 0.0919  -0.0233 55  ARG   A CG  
378  C CD  . ARG   A 49  ? 0.4906 0.5312 0.3857 -0.1005 0.0720  -0.0113 55  ARG   A CD  
379  N NE  . ARG   A 49  ? 0.4923 0.5333 0.4191 -0.0871 0.0833  -0.0078 55  ARG   A NE  
380  C CZ  . ARG   A 49  ? 0.4918 0.5518 0.4467 -0.0758 0.0703  0.0010  55  ARG   A CZ  
381  N NH1 . ARG   A 49  ? 0.4807 0.5595 0.4371 -0.0749 0.0481  0.0070  55  ARG   A NH1 
382  N NH2 . ARG   A 49  ? 0.4786 0.5382 0.4625 -0.0657 0.0804  0.0042  55  ARG   A NH2 
383  N N   . CYS   A 50  ? 0.4430 0.5064 0.2971 -0.1304 0.0250  -0.0179 56  CYS   A N   
384  C CA  . CYS   A 50  ? 0.4455 0.5129 0.2878 -0.1423 0.0139  -0.0194 56  CYS   A CA  
385  C C   . CYS   A 50  ? 0.4321 0.5285 0.2953 -0.1390 -0.0115 -0.0059 56  CYS   A C   
386  O O   . CYS   A 50  ? 0.4141 0.5251 0.2990 -0.1274 -0.0188 0.0033  56  CYS   A O   
387  C CB  . CYS   A 50  ? 0.4488 0.5108 0.3080 -0.1336 0.0257  -0.0277 56  CYS   A CB  
388  S SG  . CYS   A 50  ? 0.4563 0.5419 0.3642 -0.1086 0.0179  -0.0204 56  CYS   A SG  
389  N N   A ASP   A 51  ? 0.4322 0.5363 0.2923 -0.1489 -0.0233 -0.0045 57  ASP   A N   
390  N N   B ASP   A 51  ? 0.4379 0.5413 0.2970 -0.1494 -0.0230 -0.0049 57  ASP   A N   
391  C CA  A ASP   A 51  ? 0.4223 0.5532 0.3099 -0.1445 -0.0437 0.0086  57  ASP   A CA  
392  C CA  B ASP   A 51  ? 0.4345 0.5638 0.3175 -0.1479 -0.0441 0.0077  57  ASP   A CA  
393  C C   A ASP   A 51  ? 0.4180 0.5566 0.3311 -0.1348 -0.0422 0.0055  57  ASP   A C   
394  C C   B ASP   A 51  ? 0.4269 0.5627 0.3345 -0.1385 -0.0417 0.0038  57  ASP   A C   
395  O O   A ASP   A 51  ? 0.4068 0.5644 0.3406 -0.1347 -0.0564 0.0150  57  ASP   A O   
396  O O   B ASP   A 51  ? 0.4218 0.5735 0.3433 -0.1428 -0.0554 0.0113  57  ASP   A O   
397  C CB  A ASP   A 51  ? 0.4453 0.5846 0.3148 -0.1654 -0.0636 0.0191  57  ASP   A CB  
398  C CB  B ASP   A 51  ? 0.4726 0.6046 0.3299 -0.1720 -0.0609 0.0143  57  ASP   A CB  
399  C CG  A ASP   A 51  ? 0.5003 0.6294 0.3424 -0.1865 -0.0664 0.0127  57  ASP   A CG  
400  C CG  B ASP   A 51  ? 0.5376 0.6956 0.4170 -0.1717 -0.0831 0.0338  57  ASP   A CG  
401  O OD1 A ASP   A 51  ? 0.5078 0.6186 0.3398 -0.1862 -0.0493 -0.0021 57  ASP   A OD1 
402  O OD1 B ASP   A 51  ? 0.5516 0.7178 0.4510 -0.1573 -0.0826 0.0406  57  ASP   A OD1 
403  O OD2 A ASP   A 51  ? 0.5446 0.6836 0.3757 -0.2045 -0.0862 0.0233  57  ASP   A OD2 
404  O OD2 B ASP   A 51  ? 0.5744 0.7442 0.4523 -0.1869 -0.1011 0.0433  57  ASP   A OD2 
405  N N   . CYS   A 52  ? 0.4191 0.5430 0.3333 -0.1265 -0.0245 -0.0062 58  CYS   A N   
406  C CA  . CYS   A 52  ? 0.4039 0.5318 0.3384 -0.1177 -0.0213 -0.0092 58  CYS   A CA  
407  C C   . CYS   A 52  ? 0.3739 0.5235 0.3406 -0.1053 -0.0322 0.0007  58  CYS   A C   
408  O O   . CYS   A 52  ? 0.3720 0.5297 0.3512 -0.0962 -0.0360 0.0069  58  CYS   A O   
409  C CB  . CYS   A 52  ? 0.4082 0.5210 0.3468 -0.1066 -0.0028 -0.0181 58  CYS   A CB  
410  S SG  . CYS   A 52  ? 0.4574 0.5407 0.3656 -0.1202 0.0170  -0.0316 58  CYS   A SG  
411  N N   . GLN   A 53  ? 0.3438 0.5011 0.3235 -0.1061 -0.0359 0.0020  59  GLN   A N   
412  C CA  . GLN   A 53  ? 0.3235 0.4972 0.3342 -0.0943 -0.0411 0.0099  59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.2991 0.4672 0.3196 -0.0844 -0.0304 0.0040  59  GLN   A C   
414  O O   . GLN   A 53  ? 0.2775 0.4552 0.3194 -0.0776 -0.0318 0.0088  59  GLN   A O   
415  C CB  . GLN   A 53  ? 0.3376 0.5294 0.3631 -0.1036 -0.0561 0.0216  59  GLN   A CB  
416  C CG  . GLN   A 53  ? 0.3626 0.5671 0.3966 -0.1043 -0.0679 0.0338  59  GLN   A CG  
417  C CD  . GLN   A 53  ? 0.3839 0.6094 0.4448 -0.1101 -0.0823 0.0490  59  GLN   A CD  
418  O OE1 . GLN   A 53  ? 0.3747 0.6077 0.4269 -0.1265 -0.0972 0.0578  59  GLN   A OE1 
419  N NE2 . GLN   A 53  ? 0.3665 0.6013 0.4613 -0.0977 -0.0779 0.0533  59  GLN   A NE2 
420  N N   . THR   A 54  ? 0.2902 0.4415 0.2954 -0.0844 -0.0185 -0.0057 60  THR   A N   
421  C CA  . THR   A 54  ? 0.2825 0.4270 0.2947 -0.0754 -0.0087 -0.0096 60  THR   A CA  
422  C C   . THR   A 54  ? 0.2627 0.3942 0.2688 -0.0681 0.0011  -0.0140 60  THR   A C   
423  O O   . THR   A 54  ? 0.2644 0.3872 0.2572 -0.0736 0.0052  -0.0173 60  THR   A O   
424  C CB  . THR   A 54  ? 0.3158 0.4546 0.3235 -0.0844 -0.0043 -0.0141 60  THR   A CB  
425  O OG1 . THR   A 54  ? 0.3638 0.4873 0.3496 -0.0956 0.0024  -0.0217 60  THR   A OG1 
426  C CG2 . THR   A 54  ? 0.3100 0.4637 0.3295 -0.0928 -0.0151 -0.0079 60  THR   A CG2 
427  N N   . GLY   A 55  ? 0.2386 0.3687 0.2549 -0.0565 0.0048  -0.0127 61  GLY   A N   
428  C CA  . GLY   A 55  ? 0.2337 0.3550 0.2512 -0.0491 0.0113  -0.0132 61  GLY   A CA  
429  C C   . GLY   A 55  ? 0.2276 0.3486 0.2538 -0.0394 0.0117  -0.0099 61  GLY   A C   
430  O O   . GLY   A 55  ? 0.2388 0.3615 0.2664 -0.0394 0.0118  -0.0096 61  GLY   A O   
431  N N   . VAL   A 56  ? 0.2145 0.3323 0.2459 -0.0326 0.0121  -0.0068 62  VAL   A N   
432  C CA  . VAL   A 56  ? 0.2188 0.3347 0.2542 -0.0257 0.0102  -0.0021 62  VAL   A CA  
433  C C   . VAL   A 56  ? 0.2238 0.3437 0.2627 -0.0212 0.0019  0.0018  62  VAL   A C   
434  O O   . VAL   A 56  ? 0.2339 0.3546 0.2785 -0.0210 0.0020  0.0025  62  VAL   A O   
435  C CB  . VAL   A 56  ? 0.2368 0.3435 0.2785 -0.0238 0.0185  0.0008  62  VAL   A CB  
436  C CG1 . VAL   A 56  ? 0.2381 0.3435 0.2818 -0.0184 0.0133  0.0085  62  VAL   A CG1 
437  C CG2 . VAL   A 56  ? 0.2446 0.3449 0.2823 -0.0291 0.0281  -0.0040 62  VAL   A CG2 
438  N N   . TYR   A 57  ? 0.2280 0.3479 0.2621 -0.0186 -0.0040 0.0039  63  TYR   A N   
439  C CA  . TYR   A 57  ? 0.2127 0.3341 0.2478 -0.0165 -0.0122 0.0066  63  TYR   A CA  
440  C C   . TYR   A 57  ? 0.2350 0.3504 0.2646 -0.0156 -0.0174 0.0121  63  TYR   A C   
441  O O   . TYR   A 57  ? 0.2362 0.3462 0.2570 -0.0161 -0.0143 0.0126  63  TYR   A O   
442  C CB  . TYR   A 57  ? 0.2015 0.3264 0.2330 -0.0170 -0.0148 0.0030  63  TYR   A CB  
443  C CG  . TYR   A 57  ? 0.2273 0.3463 0.2481 -0.0171 -0.0130 0.0012  63  TYR   A CG  
444  C CD1 . TYR   A 57  ? 0.2436 0.3629 0.2643 -0.0180 -0.0061 -0.0008 63  TYR   A CD1 
445  C CD2 . TYR   A 57  ? 0.2507 0.3620 0.2608 -0.0176 -0.0171 0.0012  63  TYR   A CD2 
446  C CE1 . TYR   A 57  ? 0.2698 0.3818 0.2824 -0.0178 -0.0009 -0.0025 63  TYR   A CE1 
447  C CE2 . TYR   A 57  ? 0.2739 0.3750 0.2698 -0.0189 -0.0119 -0.0018 63  TYR   A CE2 
448  C CZ  . TYR   A 57  ? 0.2835 0.3848 0.2819 -0.0183 -0.0026 -0.0035 63  TYR   A CZ  
449  O OH  . TYR   A 57  ? 0.3100 0.3996 0.2964 -0.0193 0.0061  -0.0064 63  TYR   A OH  
450  N N   . TYR   A 58  ? 0.2425 0.3589 0.2768 -0.0153 -0.0260 0.0172  64  TYR   A N   
451  C CA  . TYR   A 58  ? 0.2557 0.3669 0.2821 -0.0172 -0.0348 0.0243  64  TYR   A CA  
452  C C   . TYR   A 58  ? 0.2883 0.3926 0.2935 -0.0212 -0.0396 0.0196  64  TYR   A C   
453  O O   . TYR   A 58  ? 0.2950 0.4012 0.3020 -0.0219 -0.0422 0.0158  64  TYR   A O   
454  C CB  . TYR   A 58  ? 0.2464 0.3628 0.2921 -0.0165 -0.0432 0.0343  64  TYR   A CB  
455  C CG  . TYR   A 58  ? 0.2611 0.3737 0.2981 -0.0210 -0.0564 0.0442  64  TYR   A CG  
456  C CD1 . TYR   A 58  ? 0.2745 0.3817 0.3034 -0.0217 -0.0560 0.0502  64  TYR   A CD1 
457  C CD2 . TYR   A 58  ? 0.2814 0.3947 0.3157 -0.0260 -0.0703 0.0478  64  TYR   A CD2 
458  C CE1 . TYR   A 58  ? 0.2951 0.3981 0.3123 -0.0278 -0.0702 0.0612  64  TYR   A CE1 
459  C CE2 . TYR   A 58  ? 0.3027 0.4116 0.3248 -0.0332 -0.0852 0.0577  64  TYR   A CE2 
460  C CZ  . TYR   A 58  ? 0.3195 0.4230 0.3309 -0.0344 -0.0855 0.0646  64  TYR   A CZ  
461  O OH  . TYR   A 58  ? 0.3589 0.4575 0.3546 -0.0433 -0.1021 0.0760  64  TYR   A OH  
462  N N   . CYS   A 59  ? 0.3100 0.4037 0.2939 -0.0248 -0.0400 0.0204  65  CYS   A N   
463  C CA  . CYS   A 59  ? 0.3254 0.4066 0.2838 -0.0303 -0.0411 0.0148  65  CYS   A CA  
464  C C   . CYS   A 59  ? 0.3335 0.4066 0.2740 -0.0379 -0.0548 0.0231  65  CYS   A C   
465  O O   . CYS   A 59  ? 0.3446 0.4121 0.2737 -0.0400 -0.0557 0.0292  65  CYS   A O   
466  C CB  . CYS   A 59  ? 0.3420 0.4148 0.2875 -0.0297 -0.0273 0.0082  65  CYS   A CB  
467  S SG  . CYS   A 59  ? 0.3906 0.4409 0.3006 -0.0373 -0.0222 0.0008  65  CYS   A SG  
468  N N   . SER   A 60  ? 0.3251 0.3980 0.2640 -0.0431 -0.0667 0.0245  66  SER   A N   
469  C CA  . SER   A 60  ? 0.3428 0.4101 0.2664 -0.0528 -0.0839 0.0344  66  SER   A CA  
470  C C   . SER   A 60  ? 0.3774 0.4226 0.2564 -0.0633 -0.0832 0.0302  66  SER   A C   
471  O O   . SER   A 60  ? 0.3978 0.4379 0.2605 -0.0711 -0.0955 0.0410  66  SER   A O   
472  C CB  . SER   A 60  ? 0.3789 0.4522 0.3142 -0.0572 -0.0977 0.0374  66  SER   A CB  
473  O OG  . SER   A 60  ? 0.4285 0.4904 0.3456 -0.0620 -0.0938 0.0248  66  SER   A OG  
474  N N   . SER   A 61  ? 0.3969 0.4283 0.2572 -0.0637 -0.0675 0.0156  67  SER   A N   
475  C CA  . SER   A 61  ? 0.4246 0.4303 0.2403 -0.0737 -0.0607 0.0094  67  SER   A CA  
476  C C   . SER   A 61  ? 0.4338 0.4349 0.2391 -0.0718 -0.0532 0.0142  67  SER   A C   
477  O O   . SER   A 61  ? 0.4656 0.4445 0.2305 -0.0817 -0.0497 0.0123  67  SER   A O   
478  C CB  . SER   A 61  ? 0.4377 0.4291 0.2434 -0.0734 -0.0422 -0.0064 67  SER   A CB  
479  O OG  . SER   A 61  ? 0.4263 0.4281 0.2595 -0.0608 -0.0252 -0.0108 67  SER   A OG  
480  N N   . ARG   A 62  ? 0.4019 0.4216 0.2401 -0.0610 -0.0511 0.0207  68  ARG   A N   
481  C CA  . ARG   A 62  ? 0.4142 0.4315 0.2482 -0.0589 -0.0452 0.0268  68  ARG   A CA  
482  C C   . ARG   A 62  ? 0.4101 0.4425 0.2679 -0.0558 -0.0586 0.0432  68  ARG   A C   
483  O O   . ARG   A 62  ? 0.4052 0.4368 0.2645 -0.0533 -0.0538 0.0497  68  ARG   A O   
484  C CB  . ARG   A 62  ? 0.4160 0.4386 0.2693 -0.0489 -0.0251 0.0184  68  ARG   A CB  
485  C CG  . ARG   A 62  ? 0.4526 0.4602 0.2891 -0.0505 -0.0082 0.0052  68  ARG   A CG  
486  C CD  . ARG   A 62  ? 0.5223 0.5053 0.3181 -0.0590 -0.0005 0.0046  68  ARG   A CD  
487  N NE  . ARG   A 62  ? 0.5624 0.5283 0.3454 -0.0599 0.0205  -0.0079 68  ARG   A NE  
488  C CZ  . ARG   A 62  ? 0.5969 0.5438 0.3544 -0.0678 0.0243  -0.0166 68  ARG   A CZ  
489  N NH1 . ARG   A 62  ? 0.5913 0.5345 0.3307 -0.0768 0.0061  -0.0143 68  ARG   A NH1 
490  N NH2 . ARG   A 62  ? 0.6150 0.5458 0.3674 -0.0672 0.0474  -0.0272 68  ARG   A NH2 
491  N N   . ARG   A 63  ? 0.4095 0.4567 0.2928 -0.0545 -0.0724 0.0500  69  ARG   A N   
492  C CA  . ARG   A 63  ? 0.3995 0.4621 0.3163 -0.0496 -0.0813 0.0660  69  ARG   A CA  
493  C C   . ARG   A 63  ? 0.3873 0.4560 0.3270 -0.0389 -0.0641 0.0636  69  ARG   A C   
494  O O   . ARG   A 63  ? 0.3931 0.4622 0.3408 -0.0372 -0.0640 0.0749  69  ARG   A O   
495  C CB  . ARG   A 63  ? 0.4317 0.4893 0.3332 -0.0587 -0.0984 0.0838  69  ARG   A CB  
496  C CG  . ARG   A 63  ? 0.4854 0.5401 0.3701 -0.0713 -0.1199 0.0895  69  ARG   A CG  
497  C CD  . ARG   A 63  ? 0.5265 0.5755 0.3914 -0.0828 -0.1388 0.1088  69  ARG   A CD  
498  N NE  . ARG   A 63  ? 0.5736 0.6168 0.4141 -0.0990 -0.1612 0.1135  69  ARG   A NE  
499  C CZ  . ARG   A 63  ? 0.6343 0.6590 0.4257 -0.1161 -0.1740 0.1185  69  ARG   A CZ  
500  N NH1 . ARG   A 63  ? 0.6557 0.6655 0.4171 -0.1180 -0.1649 0.1194  69  ARG   A NH1 
501  N NH2 . ARG   A 63  ? 0.6419 0.6609 0.4105 -0.1329 -0.1954 0.1219  69  ARG   A NH2 
502  N N   . LYS   A 64  ? 0.3707 0.4424 0.3182 -0.0333 -0.0498 0.0492  70  LYS   A N   
503  C CA  . LYS   A 64  ? 0.3481 0.4233 0.3112 -0.0266 -0.0346 0.0453  70  LYS   A CA  
504  C C   . LYS   A 64  ? 0.3069 0.3924 0.2915 -0.0216 -0.0277 0.0365  70  LYS   A C   
505  O O   . LYS   A 64  ? 0.3084 0.3963 0.2905 -0.0226 -0.0305 0.0300  70  LYS   A O   
506  C CB  . LYS   A 64  ? 0.4227 0.4863 0.3627 -0.0284 -0.0228 0.0375  70  LYS   A CB  
507  C CG  . LYS   A 64  ? 0.5362 0.5894 0.4598 -0.0315 -0.0233 0.0471  70  LYS   A CG  
508  C CD  . LYS   A 64  ? 0.6404 0.6788 0.5364 -0.0349 -0.0113 0.0394  70  LYS   A CD  
509  C CE  . LYS   A 64  ? 0.7244 0.7479 0.5912 -0.0416 -0.0155 0.0493  70  LYS   A CE  
510  N NZ  . LYS   A 64  ? 0.7710 0.7855 0.6094 -0.0514 -0.0313 0.0534  70  LYS   A NZ  
511  N N   . HIS   A 65  ? 0.2718 0.3616 0.2750 -0.0175 -0.0183 0.0364  71  HIS   A N   
512  C CA  . HIS   A 65  ? 0.2576 0.3547 0.2759 -0.0153 -0.0110 0.0281  71  HIS   A CA  
513  C C   . HIS   A 65  ? 0.2781 0.3733 0.2897 -0.0163 -0.0003 0.0194  71  HIS   A C   
514  O O   . HIS   A 65  ? 0.2925 0.3833 0.3054 -0.0163 0.0072  0.0209  71  HIS   A O   
515  C CB  . HIS   A 65  ? 0.2689 0.3686 0.3108 -0.0123 -0.0063 0.0336  71  HIS   A CB  
516  C CG  . HIS   A 65  ? 0.2730 0.3766 0.3300 -0.0108 -0.0163 0.0451  71  HIS   A CG  
517  N ND1 . HIS   A 65  ? 0.2841 0.3939 0.3570 -0.0094 -0.0170 0.0444  71  HIS   A ND1 
518  C CD2 . HIS   A 65  ? 0.2725 0.3753 0.3310 -0.0116 -0.0269 0.0586  71  HIS   A CD2 
519  C CE1 . HIS   A 65  ? 0.2785 0.3921 0.3669 -0.0086 -0.0271 0.0576  71  HIS   A CE1 
520  N NE2 . HIS   A 65  ? 0.2821 0.3923 0.3623 -0.0105 -0.0349 0.0672  71  HIS   A NE2 
521  N N   . TYR   A 66  ? 0.2616 0.3607 0.2695 -0.0175 0.0004  0.0118  72  TYR   A N   
522  C CA  . TYR   A 66  ? 0.2596 0.3592 0.2664 -0.0190 0.0086  0.0061  72  TYR   A CA  
523  C C   . TYR   A 66  ? 0.2632 0.3712 0.2822 -0.0213 0.0114  0.0017  72  TYR   A C   
524  O O   . TYR   A 66  ? 0.2565 0.3708 0.2798 -0.0216 0.0068  0.0002  72  TYR   A O   
525  C CB  . TYR   A 66  ? 0.2586 0.3565 0.2568 -0.0193 0.0088  0.0028  72  TYR   A CB  
526  C CG  . TYR   A 66  ? 0.2673 0.3518 0.2448 -0.0203 0.0091  0.0049  72  TYR   A CG  
527  C CD1 . TYR   A 66  ? 0.3004 0.3764 0.2690 -0.0213 0.0177  0.0055  72  TYR   A CD1 
528  C CD2 . TYR   A 66  ? 0.2783 0.3572 0.2427 -0.0219 0.0016  0.0053  72  TYR   A CD2 
529  C CE1 . TYR   A 66  ? 0.3318 0.3925 0.2753 -0.0241 0.0188  0.0074  72  TYR   A CE1 
530  C CE2 . TYR   A 66  ? 0.3096 0.3728 0.2478 -0.0260 0.0018  0.0062  72  TYR   A CE2 
531  C CZ  . TYR   A 66  ? 0.3442 0.3978 0.2705 -0.0272 0.0106  0.0074  72  TYR   A CZ  
532  O OH  . TYR   A 66  ? 0.3839 0.4192 0.2786 -0.0330 0.0116  0.0085  72  TYR   A OH  
533  N N   . PRO   A 67  ? 0.2766 0.3838 0.2990 -0.0244 0.0184  -0.0004 73  PRO   A N   
534  C CA  . PRO   A 67  ? 0.2809 0.3948 0.3093 -0.0301 0.0190  -0.0048 73  PRO   A CA  
535  C C   . PRO   A 67  ? 0.2751 0.3986 0.3086 -0.0317 0.0154  -0.0052 73  PRO   A C   
536  O O   . PRO   A 67  ? 0.2840 0.4065 0.3193 -0.0300 0.0193  -0.0042 73  PRO   A O   
537  C CB  . PRO   A 67  ? 0.2977 0.4056 0.3271 -0.0344 0.0274  -0.0068 73  PRO   A CB  
538  C CG  . PRO   A 67  ? 0.3124 0.4137 0.3388 -0.0300 0.0315  -0.0029 73  PRO   A CG  
539  C CD  . PRO   A 67  ? 0.2840 0.3836 0.3032 -0.0243 0.0254  0.0014  73  PRO   A CD  
540  N N   . VAL   A 68  ? 0.2602 0.3923 0.2977 -0.0348 0.0094  -0.0056 74  VAL   A N   
541  C CA  . VAL   A 68  ? 0.2615 0.4043 0.3098 -0.0356 0.0053  -0.0029 74  VAL   A CA  
542  C C   . VAL   A 68  ? 0.2570 0.4098 0.3096 -0.0445 -0.0014 -0.0016 74  VAL   A C   
543  O O   . VAL   A 68  ? 0.2550 0.4041 0.2968 -0.0495 -0.0027 -0.0045 74  VAL   A O   
544  C CB  . VAL   A 68  ? 0.2694 0.4126 0.3185 -0.0293 0.0021  -0.0013 74  VAL   A CB  
545  C CG1 . VAL   A 68  ? 0.2868 0.4197 0.3292 -0.0238 0.0079  -0.0021 74  VAL   A CG1 
546  C CG2 . VAL   A 68  ? 0.2720 0.4138 0.3146 -0.0289 -0.0026 -0.0021 74  VAL   A CG2 
547  N N   . SER   A 69  ? 0.2450 0.4097 0.3140 -0.0467 -0.0053 0.0038  75  SER   A N   
548  C CA  . SER   A 69  ? 0.2532 0.4307 0.3295 -0.0554 -0.0157 0.0092  75  SER   A CA  
549  C C   . SER   A 69  ? 0.2386 0.4220 0.3252 -0.0484 -0.0191 0.0144  75  SER   A C   
550  O O   . SER   A 69  ? 0.2456 0.4265 0.3422 -0.0396 -0.0126 0.0150  75  SER   A O   
551  C CB  . SER   A 69  ? 0.2843 0.4735 0.3815 -0.0608 -0.0181 0.0156  75  SER   A CB  
552  O OG  . SER   A 69  ? 0.3606 0.5464 0.4474 -0.0717 -0.0186 0.0116  75  SER   A OG  
553  N N   . PHE   A 70  ? 0.2117 0.4004 0.2943 -0.0528 -0.0276 0.0177  76  PHE   A N   
554  C CA  . PHE   A 70  ? 0.2169 0.4104 0.3107 -0.0462 -0.0302 0.0231  76  PHE   A CA  
555  C C   . PHE   A 70  ? 0.2384 0.4464 0.3424 -0.0541 -0.0423 0.0339  76  PHE   A C   
556  O O   . PHE   A 70  ? 0.2490 0.4592 0.3395 -0.0663 -0.0497 0.0346  76  PHE   A O   
557  C CB  . PHE   A 70  ? 0.2218 0.4041 0.2997 -0.0405 -0.0270 0.0167  76  PHE   A CB  
558  C CG  . PHE   A 70  ? 0.2423 0.4178 0.2995 -0.0469 -0.0277 0.0120  76  PHE   A CG  
559  C CD1 . PHE   A 70  ? 0.2680 0.4327 0.3128 -0.0479 -0.0207 0.0048  76  PHE   A CD1 
560  C CD2 . PHE   A 70  ? 0.2632 0.4416 0.3139 -0.0524 -0.0335 0.0152  76  PHE   A CD2 
561  C CE1 . PHE   A 70  ? 0.2925 0.4482 0.3213 -0.0534 -0.0172 0.0002  76  PHE   A CE1 
562  C CE2 . PHE   A 70  ? 0.2805 0.4489 0.3107 -0.0590 -0.0301 0.0099  76  PHE   A CE2 
563  C CZ  . PHE   A 70  ? 0.2880 0.4446 0.3085 -0.0592 -0.0210 0.0021  76  PHE   A CZ  
564  N N   . SER   A 71  ? 0.2412 0.4579 0.3680 -0.0482 -0.0443 0.0429  77  SER   A N   
565  C CA  . SER   A 71  ? 0.2496 0.4817 0.3898 -0.0553 -0.0573 0.0567  77  SER   A CA  
566  C C   . SER   A 71  ? 0.2737 0.5016 0.3910 -0.0598 -0.0630 0.0559  77  SER   A C   
567  O O   . SER   A 71  ? 0.2877 0.5022 0.3875 -0.0546 -0.0554 0.0456  77  SER   A O   
568  C CB  . SER   A 71  ? 0.2579 0.4998 0.4357 -0.0465 -0.0548 0.0681  77  SER   A CB  
569  O OG  . SER   A 71  ? 0.2801 0.5100 0.4552 -0.0354 -0.0444 0.0613  77  SER   A OG  
570  N N   . LYS   A 72  ? 0.2810 0.5201 0.3987 -0.0705 -0.0766 0.0679  78  LYS   A N   
571  C CA  . LYS   A 72  ? 0.3019 0.5353 0.3962 -0.0756 -0.0804 0.0679  78  LYS   A CA  
572  C C   . LYS   A 72  ? 0.3016 0.5358 0.4133 -0.0633 -0.0767 0.0723  78  LYS   A C   
573  O O   . LYS   A 72  ? 0.2906 0.5336 0.4350 -0.0548 -0.0753 0.0804  78  LYS   A O   
574  C CB  . LYS   A 72  ? 0.3305 0.5735 0.4136 -0.0937 -0.0973 0.0801  78  LYS   A CB  
575  C CG  . LYS   A 72  ? 0.3858 0.6223 0.4424 -0.1092 -0.1000 0.0726  78  LYS   A CG  
576  C CD  . LYS   A 72  ? 0.4605 0.7020 0.4958 -0.1308 -0.1174 0.0830  78  LYS   A CD  
577  C CE  . LYS   A 72  ? 0.5285 0.7551 0.5269 -0.1474 -0.1156 0.0705  78  LYS   A CE  
578  N NZ  . LYS   A 72  ? 0.5717 0.8025 0.5466 -0.1722 -0.1348 0.0809  78  LYS   A NZ  
579  N N   . PRO   A 73  ? 0.3078 0.5315 0.3999 -0.0624 -0.0730 0.0669  79  PRO   A N   
580  C CA  . PRO   A 73  ? 0.3083 0.5313 0.4165 -0.0516 -0.0690 0.0698  79  PRO   A CA  
581  C C   . PRO   A 73  ? 0.2941 0.5323 0.4315 -0.0507 -0.0772 0.0878  79  PRO   A C   
582  O O   . PRO   A 73  ? 0.2927 0.5404 0.4259 -0.0617 -0.0898 0.1006  79  PRO   A O   
583  C CB  . PRO   A 73  ? 0.3350 0.5465 0.4172 -0.0547 -0.0659 0.0638  79  PRO   A CB  
584  C CG  . PRO   A 73  ? 0.3549 0.5560 0.4099 -0.0621 -0.0617 0.0525  79  PRO   A CG  
585  C CD  . PRO   A 73  ? 0.3262 0.5363 0.3827 -0.0711 -0.0699 0.0572  79  PRO   A CD  
586  N N   A SER   A 74  ? 0.2843 0.5237 0.4514 -0.0388 -0.0697 0.0898  80  SER   A N   
587  N N   B SER   A 74  ? 0.2862 0.5257 0.4535 -0.0389 -0.0697 0.0898  80  SER   A N   
588  C CA  A SER   A 74  ? 0.2803 0.5336 0.4835 -0.0362 -0.0744 0.1082  80  SER   A CA  
589  C CA  B SER   A 74  ? 0.2838 0.5373 0.4876 -0.0361 -0.0743 0.1081  80  SER   A CA  
590  C C   A SER   A 74  ? 0.2844 0.5300 0.5094 -0.0233 -0.0619 0.1064  80  SER   A C   
591  C C   B SER   A 74  ? 0.2861 0.5318 0.5110 -0.0234 -0.0620 0.1064  80  SER   A C   
592  O O   A SER   A 74  ? 0.2955 0.5253 0.5056 -0.0178 -0.0514 0.0906  80  SER   A O   
593  O O   B SER   A 74  ? 0.2974 0.5272 0.5072 -0.0179 -0.0515 0.0905  80  SER   A O   
594  C CB  A SER   A 74  ? 0.2838 0.5510 0.5137 -0.0383 -0.0784 0.1181  80  SER   A CB  
595  C CB  B SER   A 74  ? 0.2919 0.5580 0.5230 -0.0371 -0.0766 0.1168  80  SER   A CB  
596  O OG  A SER   A 74  ? 0.3047 0.5629 0.5436 -0.0294 -0.0636 0.1066  80  SER   A OG  
597  O OG  B SER   A 74  ? 0.3262 0.5975 0.5372 -0.0498 -0.0870 0.1160  80  SER   A OG  
598  N N   . LEU   A 75  ? 0.2722 0.5283 0.5329 -0.0198 -0.0635 0.1237  81  LEU   A N   
599  C CA  . LEU   A 75  ? 0.2803 0.5272 0.5639 -0.0087 -0.0500 0.1227  81  LEU   A CA  
600  C C   . LEU   A 75  ? 0.2736 0.5159 0.5827 -0.0013 -0.0352 0.1191  81  LEU   A C   
601  O O   . LEU   A 75  ? 0.2528 0.5096 0.5939 -0.0015 -0.0377 0.1337  81  LEU   A O   
602  C CB  . LEU   A 75  ? 0.2729 0.5329 0.5856 -0.0087 -0.0573 0.1449  81  LEU   A CB  
603  C CG  . LEU   A 75  ? 0.3059 0.5559 0.6415 0.0011  -0.0442 0.1458  81  LEU   A CG  
604  C CD1 . LEU   A 75  ? 0.3175 0.5502 0.6203 0.0015  -0.0396 0.1286  81  LEU   A CD1 
605  C CD2 . LEU   A 75  ? 0.3090 0.5747 0.6791 0.0011  -0.0523 0.1716  81  LEU   A CD2 
606  N N   . ILE   A 76  ? 0.2898 0.5115 0.5833 0.0040  -0.0202 0.1002  82  ILE   A N   
607  C CA  . ILE   A 76  ? 0.2999 0.5115 0.6064 0.0092  -0.0037 0.0935  82  ILE   A CA  
608  C C   . ILE   A 76  ? 0.3052 0.4955 0.6195 0.0163  0.0156  0.0849  82  ILE   A C   
609  O O   . ILE   A 76  ? 0.3069 0.4842 0.5966 0.0154  0.0156  0.0739  82  ILE   A O   
610  C CB  . ILE   A 76  ? 0.3319 0.5347 0.6015 0.0053  -0.0038 0.0768  82  ILE   A CB  
611  C CG1 . ILE   A 76  ? 0.3517 0.5718 0.6133 -0.0027 -0.0195 0.0831  82  ILE   A CG1 
612  C CG2 . ILE   A 76  ? 0.3425 0.5287 0.6141 0.0097  0.0150  0.0665  82  ILE   A CG2 
613  C CD1 . ILE   A 76  ? 0.3645 0.6004 0.6595 -0.0035 -0.0213 0.0975  82  ILE   A CD1 
614  N N   . PHE   A 77  ? 0.2988 0.4833 0.6462 0.0223  0.0336  0.0890  83  PHE   A N   
615  C CA  . PHE   A 77  ? 0.3152 0.4737 0.6655 0.0271  0.0556  0.0784  83  PHE   A CA  
616  C C   . PHE   A 77  ? 0.3325 0.4662 0.6369 0.0234  0.0639  0.0550  83  PHE   A C   
617  O O   . PHE   A 77  ? 0.3308 0.4629 0.6236 0.0218  0.0667  0.0498  83  PHE   A O   
618  C CB  . PHE   A 77  ? 0.3098 0.4657 0.7098 0.0345  0.0768  0.0891  83  PHE   A CB  
619  C CG  . PHE   A 77  ? 0.3407 0.4693 0.7455 0.0383  0.0992  0.0801  83  PHE   A CG  
620  C CD1 . PHE   A 77  ? 0.3595 0.4898 0.7756 0.0398  0.0947  0.0867  83  PHE   A CD1 
621  C CD2 . PHE   A 77  ? 0.3723 0.4704 0.7647 0.0388  0.1251  0.0637  83  PHE   A CD2 
622  C CE1 . PHE   A 77  ? 0.3860 0.4890 0.8048 0.0419  0.1158  0.0770  83  PHE   A CE1 
623  C CE2 . PHE   A 77  ? 0.3969 0.4660 0.7889 0.0399  0.1468  0.0536  83  PHE   A CE2 
624  C CZ  . PHE   A 77  ? 0.3975 0.4695 0.8045 0.0416  0.1421  0.0603  83  PHE   A CZ  
625  N N   . VAL   A 78  ? 0.3382 0.4531 0.6166 0.0209  0.0661  0.0421  84  VAL   A N   
626  C CA  . VAL   A 78  ? 0.3615 0.4533 0.5951 0.0151  0.0700  0.0223  84  VAL   A CA  
627  C C   . VAL   A 78  ? 0.3854 0.4456 0.6140 0.0143  0.0925  0.0105  84  VAL   A C   
628  O O   . VAL   A 78  ? 0.3897 0.4440 0.6293 0.0151  0.0954  0.0115  84  VAL   A O   
629  C CB  . VAL   A 78  ? 0.3659 0.4638 0.5697 0.0098  0.0495  0.0178  84  VAL   A CB  
630  C CG1 . VAL   A 78  ? 0.3944 0.4697 0.5560 0.0028  0.0506  0.0005  84  VAL   A CG1 
631  C CG2 . VAL   A 78  ? 0.3504 0.4733 0.5534 0.0090  0.0316  0.0265  84  VAL   A CG2 
632  N N   . GLU   A 79  ? 0.4073 0.4445 0.6160 0.0115  0.1095  -0.0015 85  GLU   A N   
633  C CA  . GLU   A 79  ? 0.4331 0.4342 0.6285 0.0080  0.1338  -0.0153 85  GLU   A CA  
634  C C   . GLU   A 79  ? 0.4581 0.4417 0.6182 -0.0011 0.1259  -0.0280 85  GLU   A C   
635  O O   . GLU   A 79  ? 0.4588 0.4555 0.5968 -0.0054 0.1025  -0.0286 85  GLU   A O   
636  C CB  . GLU   A 79  ? 0.4760 0.4545 0.6451 0.0040  0.1509  -0.0267 85  GLU   A CB  
637  C CG  . GLU   A 79  ? 0.5341 0.5211 0.7453 0.0128  0.1683  -0.0157 85  GLU   A CG  
638  C CD  . GLU   A 79  ? 0.6142 0.5936 0.8730 0.0202  0.1915  -0.0082 85  GLU   A CD  
639  O OE1 . GLU   A 79  ? 0.6364 0.5798 0.8794 0.0161  0.2152  -0.0221 85  GLU   A OE1 
640  O OE2 . GLU   A 79  ? 0.6272 0.6359 0.9385 0.0291  0.1854  0.0121  85  GLU   A OE2 
641  N N   . ALA   A 80  ? 0.4732 0.4264 0.6293 -0.0047 0.1464  -0.0381 86  ALA   A N   
642  C CA  . ALA   A 80  ? 0.5068 0.4417 0.6298 -0.0155 0.1388  -0.0504 86  ALA   A CA  
643  C C   . ALA   A 80  ? 0.5348 0.4541 0.6007 -0.0287 0.1284  -0.0642 86  ALA   A C   
644  O O   . ALA   A 80  ? 0.5474 0.4550 0.5931 -0.0309 0.1383  -0.0694 86  ALA   A O   
645  C CB  . ALA   A 80  ? 0.5196 0.4213 0.6489 -0.0182 0.1656  -0.0595 86  ALA   A CB  
646  N N   . SER   A 81  ? 0.5341 0.4549 0.5771 -0.0374 0.1077  -0.0680 87  SER   A N   
647  C CA  . SER   A 81  ? 0.5548 0.4638 0.5479 -0.0514 0.0926  -0.0775 87  SER   A CA  
648  C C   . SER   A 81  ? 0.5812 0.4748 0.5558 -0.0639 0.0837  -0.0855 87  SER   A C   
649  O O   . SER   A 81  ? 0.5778 0.4698 0.5790 -0.0603 0.0913  -0.0842 87  SER   A O   
650  C CB  . SER   A 81  ? 0.5422 0.4839 0.5380 -0.0470 0.0677  -0.0667 87  SER   A CB  
651  O OG  . SER   A 81  ? 0.5407 0.5076 0.5606 -0.0427 0.0497  -0.0571 87  SER   A OG  
652  N N   . GLU   A 82  ? 0.6029 0.4860 0.5346 -0.0792 0.0665  -0.0923 88  GLU   A N   
653  C CA  . GLU   A 82  ? 0.6221 0.4933 0.5387 -0.0927 0.0547  -0.0982 88  GLU   A CA  
654  C C   . GLU   A 82  ? 0.5948 0.4992 0.5500 -0.0845 0.0358  -0.0852 88  GLU   A C   
655  O O   . GLU   A 82  ? 0.6023 0.4994 0.5579 -0.0927 0.0296  -0.0884 88  GLU   A O   
656  C CB  . GLU   A 82  ? 0.6865 0.5397 0.5494 -0.1130 0.0382  -0.1058 88  GLU   A CB  
657  C CG  . GLU   A 82  ? 0.7537 0.6378 0.6188 -0.1120 0.0084  -0.0929 88  GLU   A CG  
658  C CD  . GLU   A 82  ? 0.8681 0.7383 0.6869 -0.1328 -0.0121 -0.0960 88  GLU   A CD  
659  O OE1 . GLU   A 82  ? 0.8958 0.7567 0.6829 -0.1377 -0.0120 -0.0972 88  GLU   A OE1 
660  O OE2 . GLU   A 82  ? 0.8933 0.7624 0.7086 -0.1449 -0.0291 -0.0958 88  GLU   A OE2 
661  N N   . TYR   A 83  ? 0.5611 0.4992 0.5481 -0.0692 0.0287  -0.0711 89  TYR   A N   
662  C CA  . TYR   A 83  ? 0.5357 0.5029 0.5549 -0.0620 0.0132  -0.0590 89  TYR   A CA  
663  C C   . TYR   A 83  ? 0.5047 0.4845 0.5656 -0.0485 0.0249  -0.0505 89  TYR   A C   
664  O O   . TYR   A 83  ? 0.4946 0.4875 0.5766 -0.0462 0.0168  -0.0438 89  TYR   A O   
665  C CB  . TYR   A 83  ? 0.5316 0.5251 0.5524 -0.0575 -0.0044 -0.0492 89  TYR   A CB  
666  C CG  . TYR   A 83  ? 0.5631 0.5493 0.5512 -0.0709 -0.0211 -0.0527 89  TYR   A CG  
667  C CD1 . TYR   A 83  ? 0.5758 0.5628 0.5626 -0.0808 -0.0376 -0.0516 89  TYR   A CD1 
668  C CD2 . TYR   A 83  ? 0.5936 0.5713 0.5530 -0.0748 -0.0206 -0.0559 89  TYR   A CD2 
669  C CE1 . TYR   A 83  ? 0.6035 0.5859 0.5638 -0.0943 -0.0557 -0.0515 89  TYR   A CE1 
670  C CE2 . TYR   A 83  ? 0.6211 0.5929 0.5509 -0.0880 -0.0379 -0.0563 89  TYR   A CE2 
671  C CZ  . TYR   A 83  ? 0.6361 0.6107 0.5669 -0.0981 -0.0563 -0.0535 89  TYR   A CZ  
672  O OH  . TYR   A 83  ? 0.6761 0.6467 0.5809 -0.1123 -0.0761 -0.0508 89  TYR   A OH  
673  N N   . TYR   A 84  ? 0.4869 0.4645 0.5619 -0.0398 0.0429  -0.0488 90  TYR   A N   
674  C CA  . TYR   A 84  ? 0.4604 0.4516 0.5777 -0.0276 0.0524  -0.0374 90  TYR   A CA  
675  C C   . TYR   A 84  ? 0.4853 0.4565 0.6142 -0.0240 0.0787  -0.0410 90  TYR   A C   
676  O O   . TYR   A 84  ? 0.5017 0.4606 0.6126 -0.0258 0.0886  -0.0476 90  TYR   A O   
677  C CB  . TYR   A 84  ? 0.4196 0.4431 0.5575 -0.0172 0.0424  -0.0225 90  TYR   A CB  
678  C CG  . TYR   A 84  ? 0.3900 0.4345 0.5220 -0.0184 0.0207  -0.0170 90  TYR   A CG  
679  C CD1 . TYR   A 84  ? 0.3746 0.4310 0.5241 -0.0167 0.0128  -0.0095 90  TYR   A CD1 
680  C CD2 . TYR   A 84  ? 0.3907 0.4418 0.5013 -0.0210 0.0103  -0.0188 90  TYR   A CD2 
681  C CE1 . TYR   A 84  ? 0.3602 0.4337 0.5068 -0.0175 -0.0030 -0.0044 90  TYR   A CE1 
682  C CE2 . TYR   A 84  ? 0.3807 0.4492 0.4902 -0.0214 -0.0060 -0.0133 90  TYR   A CE2 
683  C CZ  . TYR   A 84  ? 0.3642 0.4435 0.4920 -0.0195 -0.0117 -0.0064 90  TYR   A CZ  
684  O OH  . TYR   A 84  ? 0.3474 0.4411 0.4757 -0.0200 -0.0240 -0.0013 90  TYR   A OH  
685  N N   . PRO   A 85  ? 0.4845 0.4544 0.6489 -0.0173 0.0919  -0.0343 91  PRO   A N   
686  C CA  . PRO   A 85  ? 0.4840 0.4402 0.6721 -0.0107 0.1186  -0.0331 91  PRO   A CA  
687  C C   . PRO   A 85  ? 0.4615 0.4462 0.6754 0.0001  0.1147  -0.0175 91  PRO   A C   
688  O O   . PRO   A 85  ? 0.4502 0.4624 0.6607 0.0016  0.0922  -0.0092 91  PRO   A O   
689  C CB  . PRO   A 85  ? 0.4825 0.4359 0.7075 -0.0057 0.1289  -0.0257 91  PRO   A CB  
690  C CG  . PRO   A 85  ? 0.4747 0.4571 0.7086 -0.0037 0.1039  -0.0139 91  PRO   A CG  
691  C CD  . PRO   A 85  ? 0.4708 0.4549 0.6615 -0.0138 0.0836  -0.0242 91  PRO   A CD  
692  N N   . ALA   A 86  ? 0.4456 0.4235 0.6868 0.0069  0.1371  -0.0132 92  ALA   A N   
693  C CA  . ALA   A 86  ? 0.4311 0.4363 0.7005 0.0157  0.1327  0.0028  92  ALA   A CA  
694  C C   . ALA   A 86  ? 0.4094 0.4480 0.7150 0.0226  0.1152  0.0241  92  ALA   A C   
695  O O   . ALA   A 86  ? 0.4045 0.4409 0.7374 0.0261  0.1216  0.0314  92  ALA   A O   
696  C CB  . ALA   A 86  ? 0.4342 0.4252 0.7332 0.0217  0.1617  0.0050  92  ALA   A CB  
697  N N   . ARG   A 87  ? 0.3932 0.4599 0.6930 0.0227  0.0926  0.0330  93  ARG   A N   
698  C CA  . ARG   A 87  ? 0.3657 0.4610 0.6885 0.0259  0.0745  0.0519  93  ARG   A CA  
699  C C   . ARG   A 87  ? 0.3477 0.4699 0.6705 0.0257  0.0575  0.0625  93  ARG   A C   
700  O O   . ARG   A 87  ? 0.3690 0.4874 0.6730 0.0235  0.0592  0.0539  93  ARG   A O   
701  C CB  . ARG   A 87  ? 0.3761 0.4691 0.6729 0.0204  0.0611  0.0450  93  ARG   A CB  
702  C CG  . ARG   A 87  ? 0.3925 0.4936 0.6511 0.0144  0.0429  0.0373  93  ARG   A CG  
703  C CD  . ARG   A 87  ? 0.4064 0.4921 0.6336 0.0073  0.0384  0.0223  93  ARG   A CD  
704  N NE  . ARG   A 87  ? 0.3973 0.4976 0.6039 0.0039  0.0199  0.0225  93  ARG   A NE  
705  C CZ  . ARG   A 87  ? 0.3914 0.4938 0.5749 0.0010  0.0139  0.0166  93  ARG   A CZ  
706  N NH1 . ARG   A 87  ? 0.3643 0.4557 0.5396 0.0008  0.0236  0.0099  93  ARG   A NH1 
707  N NH2 . ARG   A 87  ? 0.3609 0.4748 0.5307 -0.0015 0.0000  0.0176  93  ARG   A NH2 
708  N N   . TYR   A 88  ? 0.3072 0.4543 0.6460 0.0262  0.0407  0.0804  94  TYR   A N   
709  C CA  . TYR   A 88  ? 0.2928 0.4617 0.6222 0.0225  0.0232  0.0877  94  TYR   A CA  
710  C C   . TYR   A 88  ? 0.2805 0.4489 0.5685 0.0161  0.0092  0.0772  94  TYR   A C   
711  O O   . TYR   A 88  ? 0.2906 0.4561 0.5737 0.0153  0.0057  0.0772  94  TYR   A O   
712  C CB  . TYR   A 88  ? 0.2838 0.4777 0.6467 0.0232  0.0115  0.1128  94  TYR   A CB  
713  C CG  . TYR   A 88  ? 0.2893 0.4897 0.6999 0.0293  0.0225  0.1274  94  TYR   A CG  
714  C CD1 . TYR   A 88  ? 0.2979 0.5111 0.7182 0.0278  0.0188  0.1331  94  TYR   A CD1 
715  C CD2 . TYR   A 88  ? 0.2956 0.4887 0.7454 0.0366  0.0381  0.1361  94  TYR   A CD2 
716  C CE1 . TYR   A 88  ? 0.2972 0.5181 0.7679 0.0336  0.0295  0.1485  94  TYR   A CE1 
717  C CE2 . TYR   A 88  ? 0.2889 0.4880 0.7896 0.0431  0.0506  0.1514  94  TYR   A CE2 
718  C CZ  . TYR   A 88  ? 0.2994 0.5134 0.8119 0.0417  0.0460  0.1581  94  TYR   A CZ  
719  O OH  . TYR   A 88  ? 0.3071 0.5283 0.8758 0.0484  0.0589  0.1750  94  TYR   A OH  
720  N N   . GLN   A 89  ? 0.2605 0.4309 0.5222 0.0120  0.0029  0.0689  95  GLN   A N   
721  C CA  . GLN   A 89  ? 0.2560 0.4266 0.4844 0.0067  -0.0084 0.0607  95  GLN   A CA  
722  C C   . GLN   A 89  ? 0.2460 0.4359 0.4711 0.0020  -0.0221 0.0717  95  GLN   A C   
723  O O   . GLN   A 89  ? 0.2382 0.4367 0.4700 0.0009  -0.0238 0.0761  95  GLN   A O   
724  C CB  . GLN   A 89  ? 0.2721 0.4285 0.4723 0.0047  -0.0047 0.0437  95  GLN   A CB  
725  C CG  . GLN   A 89  ? 0.2766 0.4343 0.4496 0.0000  -0.0152 0.0375  95  GLN   A CG  
726  C CD  . GLN   A 89  ? 0.2818 0.4245 0.4314 -0.0021 -0.0130 0.0235  95  GLN   A CD  
727  O OE1 . GLN   A 89  ? 0.2763 0.4033 0.4226 -0.0023 -0.0058 0.0160  95  GLN   A OE1 
728  N NE2 . GLN   A 89  ? 0.3008 0.4469 0.4327 -0.0049 -0.0194 0.0202  95  GLN   A NE2 
729  N N   . SER   A 90  ? 0.2401 0.4351 0.4546 -0.0018 -0.0309 0.0762  96  SER   A N   
730  C CA  . SER   A 90  ? 0.2442 0.4528 0.4479 -0.0091 -0.0430 0.0854  96  SER   A CA  
731  C C   . SER   A 90  ? 0.2526 0.4561 0.4239 -0.0143 -0.0452 0.0728  96  SER   A C   
732  O O   . SER   A 90  ? 0.2580 0.4495 0.4174 -0.0116 -0.0394 0.0595  96  SER   A O   
733  C CB  . SER   A 90  ? 0.2550 0.4684 0.4603 -0.0119 -0.0489 0.0969  96  SER   A CB  
734  O OG  . SER   A 90  ? 0.2906 0.4926 0.4795 -0.0114 -0.0450 0.0867  96  SER   A OG  
735  N N   . HIS   A 91  ? 0.2464 0.4584 0.4045 -0.0226 -0.0536 0.0780  97  HIS   A N   
736  C CA  . HIS   A 91  ? 0.2597 0.4659 0.3889 -0.0285 -0.0538 0.0675  97  HIS   A CA  
737  C C   . HIS   A 91  ? 0.2623 0.4615 0.3891 -0.0240 -0.0472 0.0552  97  HIS   A C   
738  O O   . HIS   A 91  ? 0.2685 0.4587 0.3779 -0.0243 -0.0437 0.0449  97  HIS   A O   
739  C CB  . HIS   A 91  ? 0.2735 0.4705 0.3855 -0.0298 -0.0507 0.0623  97  HIS   A CB  
740  C CG  . HIS   A 91  ? 0.3010 0.5024 0.4098 -0.0355 -0.0559 0.0741  97  HIS   A CG  
741  N ND1 . HIS   A 91  ? 0.3381 0.5391 0.4217 -0.0472 -0.0603 0.0770  97  HIS   A ND1 
742  C CD2 . HIS   A 91  ? 0.2987 0.5031 0.4243 -0.0320 -0.0567 0.0837  97  HIS   A CD2 
743  C CE1 . HIS   A 91  ? 0.3356 0.5396 0.4193 -0.0509 -0.0647 0.0889  97  HIS   A CE1 
744  N NE2 . HIS   A 91  ? 0.3201 0.5274 0.4310 -0.0413 -0.0629 0.0940  97  HIS   A NE2 
745  N N   . LEU   A 92  ? 0.2496 0.4524 0.3953 -0.0199 -0.0447 0.0576  98  LEU   A N   
746  C CA  . LEU   A 92  ? 0.2561 0.4505 0.3980 -0.0162 -0.0372 0.0471  98  LEU   A CA  
747  C C   . LEU   A 92  ? 0.2450 0.4464 0.3863 -0.0208 -0.0397 0.0488  98  LEU   A C   
748  O O   . LEU   A 92  ? 0.2316 0.4462 0.3907 -0.0240 -0.0454 0.0608  98  LEU   A O   
749  C CB  . LEU   A 92  ? 0.2613 0.4497 0.4229 -0.0089 -0.0282 0.0468  98  LEU   A CB  
750  C CG  . LEU   A 92  ? 0.2851 0.4601 0.4388 -0.0059 -0.0184 0.0356  98  LEU   A CG  
751  C CD1 . LEU   A 92  ? 0.2952 0.4577 0.4235 -0.0069 -0.0191 0.0243  98  LEU   A CD1 
752  C CD2 . LEU   A 92  ? 0.3000 0.4663 0.4731 -0.0005 -0.0064 0.0360  98  LEU   A CD2 
753  N N   . MET   A 93  ? 0.2366 0.4298 0.3602 -0.0215 -0.0360 0.0384  99  MET   A N   
754  C CA  . MET   A 93  ? 0.2328 0.4301 0.3537 -0.0262 -0.0368 0.0380  99  MET   A CA  
755  C C   . MET   A 93  ? 0.2257 0.4146 0.3498 -0.0205 -0.0268 0.0314  99  MET   A C   
756  O O   . MET   A 93  ? 0.2332 0.4093 0.3435 -0.0169 -0.0220 0.0229  99  MET   A O   
757  C CB  . MET   A 93  ? 0.2501 0.4418 0.3453 -0.0323 -0.0384 0.0310  99  MET   A CB  
758  C CG  . MET   A 93  ? 0.2692 0.4640 0.3538 -0.0397 -0.0451 0.0354  99  MET   A CG  
759  S SD  . MET   A 93  ? 0.3397 0.5221 0.3952 -0.0464 -0.0406 0.0257  99  MET   A SD  
760  C CE  . MET   A 93  ? 0.3123 0.4843 0.3697 -0.0357 -0.0329 0.0185  99  MET   A CE  
761  N N   . LEU   A 94  ? 0.2176 0.4126 0.3590 -0.0205 -0.0239 0.0361  100 LEU   A N   
762  C CA  . LEU   A 94  ? 0.2269 0.4110 0.3684 -0.0158 -0.0118 0.0297  100 LEU   A CA  
763  C C   . LEU   A 94  ? 0.2220 0.4059 0.3535 -0.0201 -0.0112 0.0262  100 LEU   A C   
764  O O   . LEU   A 94  ? 0.2148 0.4104 0.3508 -0.0270 -0.0191 0.0314  100 LEU   A O   
765  C CB  . LEU   A 94  ? 0.2307 0.4179 0.4039 -0.0110 -0.0025 0.0370  100 LEU   A CB  
766  C CG  . LEU   A 94  ? 0.2696 0.4547 0.4581 -0.0060 0.0009  0.0409  100 LEU   A CG  
767  C CD1 . LEU   A 94  ? 0.2895 0.4776 0.5154 -0.0011 0.0127  0.0497  100 LEU   A CD1 
768  C CD2 . LEU   A 94  ? 0.2949 0.4602 0.4586 -0.0035 0.0069  0.0286  100 LEU   A CD2 
769  N N   . ALA   A 95  ? 0.2232 0.3930 0.3416 -0.0169 -0.0016 0.0181  101 ALA   A N   
770  C CA  . ALA   A 95  ? 0.2286 0.3954 0.3391 -0.0195 0.0020  0.0149  101 ALA   A CA  
771  C C   . ALA   A 95  ? 0.2381 0.3920 0.3490 -0.0150 0.0164  0.0116  101 ALA   A C   
772  O O   . ALA   A 95  ? 0.2424 0.3848 0.3487 -0.0111 0.0230  0.0084  101 ALA   A O   
773  C CB  . ALA   A 95  ? 0.2314 0.3904 0.3162 -0.0217 -0.0016 0.0084  101 ALA   A CB  
774  N N   . VAL   A 96  ? 0.2243 0.3782 0.3393 -0.0166 0.0223  0.0119  102 VAL   A N   
775  C CA  . VAL   A 96  ? 0.2410 0.3795 0.3510 -0.0134 0.0381  0.0081  102 VAL   A CA  
776  C C   . VAL   A 96  ? 0.2821 0.4048 0.3568 -0.0144 0.0373  0.0006  102 VAL   A C   
777  O O   . VAL   A 96  ? 0.2909 0.4162 0.3572 -0.0173 0.0322  0.0001  102 VAL   A O   
778  C CB  . VAL   A 96  ? 0.2381 0.3838 0.3712 -0.0147 0.0457  0.0131  102 VAL   A CB  
779  C CG1 . VAL   A 96  ? 0.2534 0.3795 0.3762 -0.0120 0.0646  0.0084  102 VAL   A CG1 
780  C CG2 . VAL   A 96  ? 0.2203 0.3840 0.3943 -0.0141 0.0442  0.0242  102 VAL   A CG2 
781  N N   . GLY   A 97  ? 0.3071 0.4137 0.3625 -0.0130 0.0415  -0.0044 103 GLY   A N   
782  C CA  . GLY   A 97  ? 0.3358 0.4288 0.3596 -0.0152 0.0378  -0.0085 103 GLY   A CA  
783  C C   . GLY   A 97  ? 0.3517 0.4259 0.3529 -0.0165 0.0412  -0.0135 103 GLY   A C   
784  O O   . GLY   A 97  ? 0.3460 0.4172 0.3562 -0.0151 0.0467  -0.0152 103 GLY   A O   
785  N N   . HIS   A 98  ? 0.3546 0.4155 0.3262 -0.0204 0.0375  -0.0151 104 HIS   A N   
786  C CA  . HIS   A 98  ? 0.3754 0.4159 0.3186 -0.0252 0.0387  -0.0200 104 HIS   A CA  
787  C C   . HIS   A 98  ? 0.3680 0.4139 0.3103 -0.0267 0.0234  -0.0194 104 HIS   A C   
788  O O   . HIS   A 98  ? 0.3576 0.4176 0.3091 -0.0253 0.0106  -0.0143 104 HIS   A O   
789  C CB  . HIS   A 98  ? 0.4077 0.4304 0.3164 -0.0312 0.0393  -0.0200 104 HIS   A CB  
790  C CG  . HIS   A 98  ? 0.4688 0.4688 0.3417 -0.0399 0.0376  -0.0248 104 HIS   A CG  
791  N ND1 . HIS   A 98  ? 0.5129 0.4908 0.3707 -0.0432 0.0552  -0.0333 104 HIS   A ND1 
792  C CD2 . HIS   A 98  ? 0.4979 0.4944 0.3503 -0.0466 0.0204  -0.0218 104 HIS   A CD2 
793  C CE1 . HIS   A 98  ? 0.5392 0.4988 0.3620 -0.0534 0.0478  -0.0368 104 HIS   A CE1 
794  N NE2 . HIS   A 98  ? 0.5328 0.5044 0.3524 -0.0560 0.0252  -0.0292 104 HIS   A NE2 
795  N N   . SER   A 99  ? 0.3859 0.4188 0.3181 -0.0298 0.0268  -0.0248 105 SER   A N   
796  C CA  . SER   A 99  ? 0.3987 0.4333 0.3276 -0.0328 0.0132  -0.0247 105 SER   A CA  
797  C C   . SER   A 99  ? 0.4274 0.4370 0.3296 -0.0406 0.0194  -0.0329 105 SER   A C   
798  O O   . SER   A 99  ? 0.4359 0.4292 0.3326 -0.0409 0.0382  -0.0392 105 SER   A O   
799  C CB  . SER   A 99  ? 0.3916 0.4465 0.3540 -0.0262 0.0092  -0.0216 105 SER   A CB  
800  O OG  . SER   A 99  ? 0.4191 0.4688 0.3938 -0.0240 0.0215  -0.0253 105 SER   A OG  
801  N N   . GLU   A 100 ? 0.4275 0.4328 0.3135 -0.0480 0.0042  -0.0325 106 GLU   A N   
802  C CA  . GLU   A 100 ? 0.4485 0.4301 0.3068 -0.0584 0.0061  -0.0406 106 GLU   A CA  
803  C C   . GLU   A 100 ? 0.4399 0.4331 0.3157 -0.0585 -0.0075 -0.0386 106 GLU   A C   
804  O O   . GLU   A 100 ? 0.4273 0.4440 0.3277 -0.0528 -0.0206 -0.0299 106 GLU   A O   
805  C CB  . GLU   A 100 ? 0.4967 0.4575 0.3091 -0.0718 -0.0009 -0.0411 106 GLU   A CB  
806  C CG  . GLU   A 100 ? 0.5705 0.5169 0.3647 -0.0716 0.0164  -0.0438 106 GLU   A CG  
807  C CD  . GLU   A 100 ? 0.6533 0.5780 0.3989 -0.0855 0.0102  -0.0429 106 GLU   A CD  
808  O OE1 . GLU   A 100 ? 0.6704 0.5791 0.3845 -0.0995 -0.0011 -0.0454 106 GLU   A OE1 
809  O OE2 . GLU   A 100 ? 0.6725 0.5961 0.4108 -0.0835 0.0157  -0.0389 106 GLU   A OE2 
810  N N   . PRO   A 101 ? 0.4487 0.4247 0.3135 -0.0652 -0.0032 -0.0466 107 PRO   A N   
811  C CA  . PRO   A 101 ? 0.4316 0.4199 0.3172 -0.0646 -0.0152 -0.0439 107 PRO   A CA  
812  C C   . PRO   A 101 ? 0.4215 0.4275 0.3135 -0.0671 -0.0392 -0.0336 107 PRO   A C   
813  O O   . PRO   A 101 ? 0.3998 0.4275 0.3242 -0.0592 -0.0456 -0.0270 107 PRO   A O   
814  C CB  . PRO   A 101 ? 0.4592 0.4194 0.3203 -0.0759 -0.0079 -0.0552 107 PRO   A CB  
815  C CG  . PRO   A 101 ? 0.4812 0.4173 0.3238 -0.0765 0.0169  -0.0645 107 PRO   A CG  
816  C CD  . PRO   A 101 ? 0.4665 0.4095 0.3015 -0.0733 0.0160  -0.0589 107 PRO   A CD  
817  N N   . GLY   A 102 ? 0.4362 0.4332 0.2993 -0.0777 -0.0513 -0.0307 108 GLY   A N   
818  C CA  . GLY   A 102 ? 0.4338 0.4473 0.3074 -0.0804 -0.0738 -0.0181 108 GLY   A CA  
819  C C   . GLY   A 102 ? 0.4143 0.4527 0.3202 -0.0676 -0.0753 -0.0079 108 GLY   A C   
820  O O   . GLY   A 102 ? 0.4097 0.4633 0.3344 -0.0672 -0.0900 0.0032  108 GLY   A O   
821  N N   . ASP   A 103 ? 0.3846 0.4264 0.2985 -0.0578 -0.0593 -0.0113 109 ASP   A N   
822  C CA  . ASP   A 103 ? 0.3619 0.4236 0.3026 -0.0473 -0.0580 -0.0042 109 ASP   A CA  
823  C C   . ASP   A 103 ? 0.3273 0.4063 0.3004 -0.0396 -0.0577 -0.0021 109 ASP   A C   
824  O O   . ASP   A 103 ? 0.3108 0.4036 0.3029 -0.0335 -0.0575 0.0036  109 ASP   A O   
825  C CB  . ASP   A 103 ? 0.3693 0.4287 0.3063 -0.0419 -0.0430 -0.0078 109 ASP   A CB  
826  C CG  . ASP   A 103 ? 0.4087 0.4527 0.3152 -0.0485 -0.0429 -0.0073 109 ASP   A CG  
827  O OD1 . ASP   A 103 ? 0.3996 0.4441 0.2981 -0.0540 -0.0571 0.0009  109 ASP   A OD1 
828  O OD2 . ASP   A 103 ? 0.4469 0.4787 0.3396 -0.0483 -0.0281 -0.0138 109 ASP   A OD2 
829  N N   . CYS   A 104 ? 0.3222 0.3986 0.3006 -0.0406 -0.0562 -0.0067 110 CYS   A N   
830  C CA  . CYS   A 104 ? 0.3066 0.3975 0.3132 -0.0344 -0.0557 -0.0041 110 CYS   A CA  
831  C C   . CYS   A 104 ? 0.2935 0.3970 0.3173 -0.0338 -0.0667 0.0052  110 CYS   A C   
832  O O   . CYS   A 104 ? 0.3052 0.4054 0.3233 -0.0406 -0.0789 0.0097  110 CYS   A O   
833  C CB  . CYS   A 104 ? 0.3222 0.4054 0.3295 -0.0374 -0.0543 -0.0093 110 CYS   A CB  
834  S SG  . CYS   A 104 ? 0.3710 0.4423 0.3738 -0.0346 -0.0360 -0.0179 110 CYS   A SG  
835  N N   . GLY   A 105 ? 0.2654 0.3818 0.3101 -0.0270 -0.0621 0.0088  111 GLY   A N   
836  C CA  . GLY   A 105 ? 0.2600 0.3861 0.3246 -0.0254 -0.0672 0.0176  111 GLY   A CA  
837  C C   . GLY   A 105 ? 0.2610 0.3902 0.3278 -0.0222 -0.0631 0.0214  111 GLY   A C   
838  O O   . GLY   A 105 ? 0.2565 0.3927 0.3435 -0.0191 -0.0611 0.0278  111 GLY   A O   
839  N N   . GLY   A 106 ? 0.2576 0.3803 0.3054 -0.0228 -0.0595 0.0175  112 GLY   A N   
840  C CA  . GLY   A 106 ? 0.2487 0.3728 0.2979 -0.0200 -0.0541 0.0202  112 GLY   A CA  
841  C C   . GLY   A 106 ? 0.2538 0.3841 0.3144 -0.0158 -0.0432 0.0175  112 GLY   A C   
842  O O   . GLY   A 106 ? 0.2482 0.3801 0.3060 -0.0155 -0.0393 0.0123  112 GLY   A O   
843  N N   . ILE   A 107 ? 0.2394 0.3719 0.3127 -0.0137 -0.0378 0.0218  113 ILE   A N   
844  C CA  . ILE   A 107 ? 0.2376 0.3719 0.3158 -0.0126 -0.0269 0.0182  113 ILE   A CA  
845  C C   . ILE   A 107 ? 0.2385 0.3703 0.3032 -0.0141 -0.0203 0.0126  113 ILE   A C   
846  O O   . ILE   A 107 ? 0.2372 0.3652 0.2964 -0.0139 -0.0200 0.0136  113 ILE   A O   
847  C CB  . ILE   A 107 ? 0.2427 0.3766 0.3411 -0.0106 -0.0201 0.0241  113 ILE   A CB  
848  C CG1 . ILE   A 107 ? 0.2638 0.4022 0.3796 -0.0097 -0.0243 0.0291  113 ILE   A CG1 
849  C CG2 . ILE   A 107 ? 0.2458 0.3750 0.3404 -0.0121 -0.0056 0.0186  113 ILE   A CG2 
850  C CD1 . ILE   A 107 ? 0.2778 0.4162 0.4207 -0.0069 -0.0179 0.0378  113 ILE   A CD1 
851  N N   . LEU   A 108 ? 0.2268 0.3609 0.2869 -0.0164 -0.0160 0.0081  114 LEU   A N   
852  C CA  . LEU   A 108 ? 0.2463 0.3799 0.2971 -0.0200 -0.0108 0.0038  114 LEU   A CA  
853  C C   . LEU   A 108 ? 0.2629 0.3918 0.3138 -0.0235 -0.0015 0.0022  114 LEU   A C   
854  O O   . LEU   A 108 ? 0.2556 0.3849 0.3089 -0.0245 -0.0001 0.0028  114 LEU   A O   
855  C CB  . LEU   A 108 ? 0.2576 0.3978 0.3048 -0.0221 -0.0149 0.0025  114 LEU   A CB  
856  C CG  . LEU   A 108 ? 0.2964 0.4390 0.3374 -0.0282 -0.0123 0.0004  114 LEU   A CG  
857  C CD1 . LEU   A 108 ? 0.3034 0.4437 0.3422 -0.0279 -0.0098 -0.0012 114 LEU   A CD1 
858  C CD2 . LEU   A 108 ? 0.3080 0.4599 0.3521 -0.0307 -0.0182 0.0033  114 LEU   A CD2 
859  N N   . ARG   A 109 ? 0.2767 0.3987 0.3245 -0.0257 0.0068  -0.0001 115 ARG   A N   
860  C CA  . ARG   A 109 ? 0.3061 0.4186 0.3507 -0.0305 0.0192  -0.0036 115 ARG   A CA  
861  C C   . ARG   A 109 ? 0.3191 0.4257 0.3484 -0.0390 0.0248  -0.0099 115 ARG   A C   
862  O O   . ARG   A 109 ? 0.3049 0.4143 0.3331 -0.0386 0.0214  -0.0102 115 ARG   A O   
863  C CB  . ARG   A 109 ? 0.3522 0.4576 0.4144 -0.0252 0.0284  0.0007  115 ARG   A CB  
864  C CG  . ARG   A 109 ? 0.4352 0.5400 0.5066 -0.0205 0.0274  0.0054  115 ARG   A CG  
865  C CD  . ARG   A 109 ? 0.5022 0.6020 0.5982 -0.0152 0.0359  0.0131  115 ARG   A CD  
866  N NE  . ARG   A 109 ? 0.5609 0.6701 0.6739 -0.0100 0.0241  0.0227  115 ARG   A NE  
867  C CZ  . ARG   A 109 ? 0.5919 0.7018 0.7253 -0.0074 0.0285  0.0278  115 ARG   A CZ  
868  N NH1 . ARG   A 109 ? 0.5830 0.6824 0.7200 -0.0093 0.0469  0.0235  115 ARG   A NH1 
869  N NH2 . ARG   A 109 ? 0.5798 0.6992 0.7293 -0.0042 0.0153  0.0371  115 ARG   A NH2 
870  N N   . CYS   A 110 ? 0.3397 0.4369 0.3553 -0.0480 0.0334  -0.0152 116 CYS   A N   
871  C CA  . CYS   A 110 ? 0.3709 0.4597 0.3691 -0.0591 0.0388  -0.0220 116 CYS   A CA  
872  C C   . CYS   A 110 ? 0.4117 0.4796 0.4071 -0.0624 0.0597  -0.0276 116 CYS   A C   
873  O O   . CYS   A 110 ? 0.4049 0.4685 0.4177 -0.0541 0.0684  -0.0238 116 CYS   A O   
874  C CB  . CYS   A 110 ? 0.3723 0.4657 0.3512 -0.0708 0.0301  -0.0234 116 CYS   A CB  
875  S SG  . CYS   A 110 ? 0.3723 0.4549 0.3366 -0.0768 0.0380  -0.0251 116 CYS   A SG  
876  N N   . GLN   A 111 ? 0.4432 0.4970 0.4178 -0.0755 0.0686  -0.0362 117 GLN   A N   
877  C CA  . GLN   A 111 ? 0.4769 0.5065 0.4470 -0.0799 0.0922  -0.0430 117 GLN   A CA  
878  C C   . GLN   A 111 ? 0.4892 0.5073 0.4529 -0.0821 0.1041  -0.0447 117 GLN   A C   
879  O O   . GLN   A 111 ? 0.5041 0.5024 0.4739 -0.0815 0.1269  -0.0481 117 GLN   A O   
880  C CB  . GLN   A 111 ? 0.5203 0.5345 0.4633 -0.0969 0.0988  -0.0537 117 GLN   A CB  
881  C CG  . GLN   A 111 ? 0.5765 0.5900 0.4861 -0.1141 0.0891  -0.0580 117 GLN   A CG  
882  C CD  . GLN   A 111 ? 0.6509 0.6499 0.5322 -0.1336 0.0922  -0.0677 117 GLN   A CD  
883  O OE1 . GLN   A 111 ? 0.6724 0.6857 0.5533 -0.1387 0.0757  -0.0653 117 GLN   A OE1 
884  N NE2 . GLN   A 111 ? 0.6674 0.6367 0.5247 -0.1460 0.1141  -0.0789 117 GLN   A NE2 
885  N N   . HIS   A 112 ? 0.4774 0.5070 0.4319 -0.0839 0.0907  -0.0413 118 HIS   A N   
886  C CA  . HIS   A 112 ? 0.4839 0.5022 0.4309 -0.0865 0.1023  -0.0424 118 HIS   A CA  
887  C C   . HIS   A 112 ? 0.4544 0.4846 0.4343 -0.0708 0.1004  -0.0326 118 HIS   A C   
888  O O   . HIS   A 112 ? 0.4638 0.4849 0.4426 -0.0716 0.1117  -0.0326 118 HIS   A O   
889  C CB  . HIS   A 112 ? 0.5144 0.5336 0.4274 -0.1012 0.0914  -0.0443 118 HIS   A CB  
890  C CG  . HIS   A 112 ? 0.5722 0.5811 0.4514 -0.1199 0.0895  -0.0524 118 HIS   A CG  
891  N ND1 . HIS   A 112 ? 0.5943 0.6222 0.4725 -0.1235 0.0674  -0.0484 118 HIS   A ND1 
892  C CD2 . HIS   A 112 ? 0.6093 0.5900 0.4557 -0.1369 0.1074  -0.0639 118 HIS   A CD2 
893  C CE1 . HIS   A 112 ? 0.6140 0.6273 0.4607 -0.1428 0.0699  -0.0565 118 HIS   A CE1 
894  N NE2 . HIS   A 112 ? 0.6315 0.6149 0.4552 -0.1522 0.0937  -0.0669 118 HIS   A NE2 
895  N N   . GLY   A 113 ? 0.4172 0.4658 0.4236 -0.0582 0.0866  -0.0246 119 GLY   A N   
896  C CA  . GLY   A 113 ? 0.3890 0.4494 0.4251 -0.0456 0.0814  -0.0150 119 GLY   A CA  
897  C C   . GLY   A 113 ? 0.3585 0.4402 0.3991 -0.0405 0.0578  -0.0093 119 GLY   A C   
898  O O   . GLY   A 113 ? 0.3482 0.4369 0.3785 -0.0428 0.0469  -0.0109 119 GLY   A O   
899  N N   . VAL   A 114 ? 0.3248 0.4156 0.3826 -0.0338 0.0514  -0.0026 120 VAL   A N   
900  C CA  . VAL   A 114 ? 0.3006 0.4078 0.3630 -0.0293 0.0320  0.0019  120 VAL   A CA  
901  C C   . VAL   A 114 ? 0.2865 0.3989 0.3284 -0.0359 0.0235  -0.0005 120 VAL   A C   
902  O O   . VAL   A 114 ? 0.3033 0.4105 0.3339 -0.0418 0.0287  -0.0016 120 VAL   A O   
903  C CB  . VAL   A 114 ? 0.2982 0.4118 0.3856 -0.0219 0.0280  0.0096  120 VAL   A CB  
904  C CG1 . VAL   A 114 ? 0.2947 0.4208 0.3824 -0.0194 0.0105  0.0121  120 VAL   A CG1 
905  C CG2 . VAL   A 114 ? 0.2877 0.4003 0.4006 -0.0156 0.0317  0.0161  120 VAL   A CG2 
906  N N   . VAL   A 115 ? 0.2623 0.3845 0.3008 -0.0354 0.0111  0.0000  121 VAL   A N   
907  C CA  . VAL   A 115 ? 0.2549 0.3849 0.2823 -0.0407 0.0018  0.0010  121 VAL   A CA  
908  C C   . VAL   A 115 ? 0.2498 0.3899 0.2905 -0.0343 -0.0079 0.0062  121 VAL   A C   
909  O O   . VAL   A 115 ? 0.2548 0.3998 0.2927 -0.0371 -0.0127 0.0097  121 VAL   A O   
910  C CB  . VAL   A 115 ? 0.2585 0.3927 0.2802 -0.0438 -0.0032 -0.0007 121 VAL   A CB  
911  C CG1 . VAL   A 115 ? 0.2623 0.4080 0.2824 -0.0478 -0.0142 0.0038  121 VAL   A CG1 
912  C CG2 . VAL   A 115 ? 0.2641 0.3872 0.2714 -0.0519 0.0063  -0.0067 121 VAL   A CG2 
913  N N   . GLY   A 116 ? 0.2381 0.3803 0.2916 -0.0269 -0.0114 0.0071  122 GLY   A N   
914  C CA  . GLY   A 116 ? 0.2292 0.3769 0.2927 -0.0223 -0.0191 0.0101  122 GLY   A CA  
915  C C   . GLY   A 116 ? 0.2263 0.3722 0.2959 -0.0177 -0.0230 0.0100  122 GLY   A C   
916  O O   . GLY   A 116 ? 0.2303 0.3723 0.3006 -0.0169 -0.0203 0.0099  122 GLY   A O   
917  N N   . ILE   A 117 ? 0.2116 0.3589 0.2850 -0.0157 -0.0290 0.0106  123 ILE   A N   
918  C CA  . ILE   A 117 ? 0.2256 0.3684 0.2979 -0.0144 -0.0340 0.0101  123 ILE   A CA  
919  C C   . ILE   A 117 ? 0.2310 0.3708 0.2957 -0.0145 -0.0347 0.0067  123 ILE   A C   
920  O O   . ILE   A 117 ? 0.2299 0.3728 0.2991 -0.0139 -0.0331 0.0069  123 ILE   A O   
921  C CB  . ILE   A 117 ? 0.2432 0.3857 0.3263 -0.0143 -0.0396 0.0133  123 ILE   A CB  
922  C CG1 . ILE   A 117 ? 0.2526 0.3975 0.3420 -0.0141 -0.0398 0.0135  123 ILE   A CG1 
923  C CG2 . ILE   A 117 ? 0.2568 0.4008 0.3528 -0.0134 -0.0374 0.0183  123 ILE   A CG2 
924  C CD1 . ILE   A 117 ? 0.2683 0.4125 0.3699 -0.0151 -0.0460 0.0164  123 ILE   A CD1 
925  N N   . VAL   A 118 ? 0.2360 0.3681 0.2898 -0.0155 -0.0363 0.0046  124 VAL   A N   
926  C CA  . VAL   A 118 ? 0.2359 0.3604 0.2806 -0.0161 -0.0329 0.0002  124 VAL   A CA  
927  C C   . VAL   A 118 ? 0.2426 0.3633 0.2915 -0.0168 -0.0342 -0.0012 124 VAL   A C   
928  O O   . VAL   A 118 ? 0.2416 0.3609 0.2919 -0.0190 -0.0412 0.0001  124 VAL   A O   
929  C CB  . VAL   A 118 ? 0.2572 0.3705 0.2836 -0.0192 -0.0345 -0.0016 124 VAL   A CB  
930  C CG1 . VAL   A 118 ? 0.2678 0.3684 0.2813 -0.0210 -0.0277 -0.0074 124 VAL   A CG1 
931  C CG2 . VAL   A 118 ? 0.2684 0.3845 0.2926 -0.0181 -0.0318 0.0004  124 VAL   A CG2 
932  N N   . SER   A 119 ? 0.2454 0.3647 0.2997 -0.0151 -0.0272 -0.0028 125 SER   A N   
933  C CA  . SER   A 119 ? 0.2610 0.3756 0.3225 -0.0152 -0.0257 -0.0039 125 SER   A CA  
934  C C   . SER   A 119 ? 0.2901 0.3920 0.3488 -0.0150 -0.0145 -0.0087 125 SER   A C   
935  O O   . SER   A 119 ? 0.3116 0.4003 0.3652 -0.0180 -0.0119 -0.0134 125 SER   A O   
936  C CB  . SER   A 119 ? 0.2641 0.3924 0.3454 -0.0120 -0.0268 0.0027  125 SER   A CB  
937  O OG  . SER   A 119 ? 0.2898 0.4141 0.3818 -0.0112 -0.0240 0.0031  125 SER   A OG  
938  N N   . THR   A 120 ? 0.2935 0.3978 0.3571 -0.0123 -0.0063 -0.0076 126 THR   A N   
939  C CA  . THR   A 120 ? 0.3119 0.4029 0.3778 -0.0113 0.0083  -0.0113 126 THR   A CA  
940  C C   . THR   A 120 ? 0.3280 0.4117 0.3800 -0.0123 0.0156  -0.0146 126 THR   A C   
941  O O   . THR   A 120 ? 0.3103 0.4014 0.3536 -0.0133 0.0081  -0.0130 126 THR   A O   
942  C CB  . THR   A 120 ? 0.3082 0.4119 0.4077 -0.0055 0.0138  -0.0027 126 THR   A CB  
943  O OG1 . THR   A 120 ? 0.2985 0.4185 0.4101 -0.0037 0.0113  0.0043  126 THR   A OG1 
944  C CG2 . THR   A 120 ? 0.3023 0.4152 0.4157 -0.0045 0.0061  0.0027  126 THR   A CG2 
945  N N   . GLY   A 121 ? 0.3544 0.4224 0.4058 -0.0120 0.0322  -0.0190 127 GLY   A N   
946  C CA  . GLY   A 121 ? 0.3736 0.4339 0.4139 -0.0127 0.0416  -0.0215 127 GLY   A CA  
947  C C   . GLY   A 121 ? 0.3947 0.4304 0.4280 -0.0139 0.0633  -0.0285 127 GLY   A C   
948  O O   . GLY   A 121 ? 0.3939 0.4178 0.4338 -0.0139 0.0729  -0.0317 127 GLY   A O   
949  N N   . GLY   A 122 ? 0.4151 0.4414 0.4346 -0.0154 0.0727  -0.0311 128 GLY   A N   
950  C CA  . GLY   A 122 ? 0.4395 0.4394 0.4500 -0.0170 0.0976  -0.0382 128 GLY   A CA  
951  C C   . GLY   A 122 ? 0.4348 0.4455 0.4780 -0.0102 0.1109  -0.0312 128 GLY   A C   
952  O O   . GLY   A 122 ? 0.4131 0.4519 0.4918 -0.0045 0.1009  -0.0202 128 GLY   A O   
953  N N   . ASN   A 123 ? 0.4552 0.4429 0.4852 -0.0121 0.1330  -0.0370 129 ASN   A N   
954  C CA  . ASN   A 123 ? 0.4561 0.4513 0.5194 -0.0061 0.1489  -0.0302 129 ASN   A CA  
955  C C   . ASN   A 123 ? 0.4333 0.4542 0.5061 -0.0047 0.1325  -0.0221 129 ASN   A C   
956  O O   . ASN   A 123 ? 0.4256 0.4663 0.5395 0.0004  0.1349  -0.0119 129 ASN   A O   
957  C CB  . ASN   A 123 ? 0.4645 0.4719 0.5824 0.0021  0.1598  -0.0209 129 ASN   A CB  
958  C CG  . ASN   A 123 ? 0.5439 0.5209 0.6588 0.0016  0.1853  -0.0292 129 ASN   A CG  
959  O OD1 . ASN   A 123 ? 0.5890 0.5317 0.6670 -0.0046 0.2052  -0.0418 129 ASN   A OD1 
960  N ND2 . ASN   A 123 ? 0.5457 0.5328 0.6989 0.0073  0.1866  -0.0220 129 ASN   A ND2 
961  N N   . GLY   A 124 ? 0.4184 0.4384 0.4552 -0.0100 0.1160  -0.0257 130 GLY   A N   
962  C CA  . GLY   A 124 ? 0.3821 0.4225 0.4251 -0.0095 0.1024  -0.0194 130 GLY   A CA  
963  C C   . GLY   A 124 ? 0.3386 0.4089 0.4090 -0.0069 0.0825  -0.0110 130 GLY   A C   
964  O O   . GLY   A 124 ? 0.3291 0.4160 0.4101 -0.0072 0.0741  -0.0058 130 GLY   A O   
965  N N   . LEU   A 125 ? 0.3136 0.3891 0.3930 -0.0056 0.0756  -0.0099 131 LEU   A N   
966  C CA  . LEU   A 125 ? 0.3029 0.4036 0.4022 -0.0046 0.0573  -0.0020 131 LEU   A CA  
967  C C   . LEU   A 125 ? 0.3169 0.4146 0.3937 -0.0069 0.0440  -0.0062 131 LEU   A C   
968  O O   . LEU   A 125 ? 0.3632 0.4445 0.4268 -0.0078 0.0493  -0.0120 131 LEU   A O   
969  C CB  . LEU   A 125 ? 0.2977 0.4111 0.4375 -0.0003 0.0612  0.0071  131 LEU   A CB  
970  C CG  . LEU   A 125 ? 0.3150 0.4371 0.4881 0.0020  0.0720  0.0152  131 LEU   A CG  
971  C CD1 . LEU   A 125 ? 0.3225 0.4483 0.5361 0.0072  0.0833  0.0238  131 LEU   A CD1 
972  C CD2 . LEU   A 125 ? 0.3115 0.4571 0.4958 -0.0016 0.0560  0.0230  131 LEU   A CD2 
973  N N   . VAL   A 126 ? 0.2737 0.3851 0.3466 -0.0086 0.0284  -0.0035 132 VAL   A N   
974  C CA  . VAL   A 126 ? 0.2553 0.3658 0.3132 -0.0104 0.0166  -0.0057 132 VAL   A CA  
975  C C   . VAL   A 126 ? 0.2487 0.3777 0.3265 -0.0095 0.0068  0.0011  132 VAL   A C   
976  O O   . VAL   A 126 ? 0.2398 0.3827 0.3312 -0.0104 0.0037  0.0066  132 VAL   A O   
977  C CB  . VAL   A 126 ? 0.2569 0.3628 0.2913 -0.0134 0.0099  -0.0082 132 VAL   A CB  
978  C CG1 . VAL   A 126 ? 0.2560 0.3730 0.2974 -0.0138 0.0085  -0.0049 132 VAL   A CG1 
979  C CG2 . VAL   A 126 ? 0.2465 0.3539 0.2735 -0.0148 -0.0022 -0.0080 132 VAL   A CG2 
980  N N   . GLY   A 127 ? 0.2501 0.3780 0.3285 -0.0090 0.0024  0.0009  133 GLY   A N   
981  C CA  . GLY   A 127 ? 0.2438 0.3862 0.3371 -0.0088 -0.0059 0.0076  133 GLY   A CA  
982  C C   . GLY   A 127 ? 0.2418 0.3843 0.3220 -0.0107 -0.0148 0.0058  133 GLY   A C   
983  O O   . GLY   A 127 ? 0.2501 0.3817 0.3166 -0.0114 -0.0158 0.0008  133 GLY   A O   
984  N N   . PHE   A 128 ? 0.2293 0.3834 0.3138 -0.0127 -0.0209 0.0105  134 PHE   A N   
985  C CA  . PHE   A 128 ? 0.2377 0.3916 0.3138 -0.0144 -0.0258 0.0096  134 PHE   A CA  
986  C C   . PHE   A 128 ? 0.2322 0.3935 0.3173 -0.0151 -0.0293 0.0151  134 PHE   A C   
987  O O   . PHE   A 128 ? 0.2221 0.3925 0.3154 -0.0172 -0.0311 0.0212  134 PHE   A O   
988  C CB  . PHE   A 128 ? 0.2352 0.3913 0.3028 -0.0178 -0.0257 0.0087  134 PHE   A CB  
989  C CG  . PHE   A 128 ? 0.2395 0.3902 0.3002 -0.0174 -0.0217 0.0052  134 PHE   A CG  
990  C CD1 . PHE   A 128 ? 0.2416 0.3833 0.2925 -0.0162 -0.0215 0.0024  134 PHE   A CD1 
991  C CD2 . PHE   A 128 ? 0.2405 0.3957 0.3059 -0.0190 -0.0191 0.0065  134 PHE   A CD2 
992  C CE1 . PHE   A 128 ? 0.2538 0.3897 0.2967 -0.0163 -0.0177 0.0004  134 PHE   A CE1 
993  C CE2 . PHE   A 128 ? 0.2443 0.3936 0.3037 -0.0187 -0.0140 0.0036  134 PHE   A CE2 
994  C CZ  . PHE   A 128 ? 0.2439 0.3829 0.2905 -0.0173 -0.0130 0.0003  134 PHE   A CZ  
995  N N   . ALA   A 129 ? 0.2429 0.4007 0.3279 -0.0142 -0.0311 0.0145  135 ALA   A N   
996  C CA  . ALA   A 129 ? 0.2418 0.4047 0.3335 -0.0151 -0.0331 0.0198  135 ALA   A CA  
997  C C   . ALA   A 129 ? 0.2403 0.4049 0.3218 -0.0198 -0.0326 0.0205  135 ALA   A C   
998  O O   . ALA   A 129 ? 0.2374 0.3966 0.3139 -0.0197 -0.0300 0.0169  135 ALA   A O   
999  C CB  . ALA   A 129 ? 0.2434 0.4007 0.3400 -0.0130 -0.0339 0.0183  135 ALA   A CB  
1000 N N   . ASP   A 130 ? 0.2316 0.4026 0.3101 -0.0249 -0.0347 0.0259  136 ASP   A N   
1001 C CA  . ASP   A 130 ? 0.2457 0.4136 0.3081 -0.0320 -0.0324 0.0250  136 ASP   A CA  
1002 C C   . ASP   A 130 ? 0.2444 0.4063 0.3052 -0.0318 -0.0275 0.0250  136 ASP   A C   
1003 O O   . ASP   A 130 ? 0.2360 0.4004 0.3077 -0.0286 -0.0295 0.0294  136 ASP   A O   
1004 C CB  . ASP   A 130 ? 0.2766 0.4520 0.3325 -0.0404 -0.0384 0.0321  136 ASP   A CB  
1005 C CG  . ASP   A 130 ? 0.3505 0.5187 0.3821 -0.0512 -0.0354 0.0295  136 ASP   A CG  
1006 O OD1 . ASP   A 130 ? 0.3648 0.5258 0.3870 -0.0531 -0.0296 0.0220  136 ASP   A OD1 
1007 O OD2 . ASP   A 130 ? 0.3911 0.5591 0.4116 -0.0585 -0.0378 0.0351  136 ASP   A OD2 
1008 N N   . VAL   A 131 ? 0.2435 0.3964 0.2935 -0.0350 -0.0192 0.0204  137 VAL   A N   
1009 C CA  . VAL   A 131 ? 0.2614 0.4072 0.3117 -0.0354 -0.0111 0.0211  137 VAL   A CA  
1010 C C   . VAL   A 131 ? 0.2952 0.4308 0.3211 -0.0461 -0.0024 0.0194  137 VAL   A C   
1011 O O   . VAL   A 131 ? 0.3078 0.4351 0.3305 -0.0479 0.0071  0.0199  137 VAL   A O   
1012 C CB  . VAL   A 131 ? 0.2572 0.3989 0.3243 -0.0287 -0.0054 0.0190  137 VAL   A CB  
1013 C CG1 . VAL   A 131 ? 0.2476 0.3961 0.3318 -0.0219 -0.0150 0.0206  137 VAL   A CG1 
1014 C CG2 . VAL   A 131 ? 0.2597 0.3947 0.3228 -0.0293 0.0017  0.0141  137 VAL   A CG2 
1015 N N   . ARG   A 132 ? 0.3071 0.4415 0.3146 -0.0543 -0.0046 0.0168  138 ARG   A N   
1016 C CA  . ARG   A 132 ? 0.3345 0.4556 0.3125 -0.0675 0.0035  0.0131  138 ARG   A CA  
1017 C C   . ARG   A 132 ? 0.3650 0.4832 0.3243 -0.0769 0.0017  0.0191  138 ARG   A C   
1018 O O   . ARG   A 132 ? 0.3929 0.4943 0.3244 -0.0882 0.0129  0.0148  138 ARG   A O   
1019 C CB  . ARG   A 132 ? 0.3305 0.4528 0.2944 -0.0757 -0.0022 0.0100  138 ARG   A CB  
1020 C CG  . ARG   A 132 ? 0.2972 0.4181 0.2736 -0.0687 0.0026  0.0037  138 ARG   A CG  
1021 C CD  . ARG   A 132 ? 0.3019 0.4251 0.2657 -0.0777 -0.0037 0.0017  138 ARG   A CD  
1022 N NE  . ARG   A 132 ? 0.2883 0.4302 0.2669 -0.0749 -0.0196 0.0097  138 ARG   A NE  
1023 C CZ  . ARG   A 132 ? 0.3288 0.4779 0.3071 -0.0803 -0.0273 0.0110  138 ARG   A CZ  
1024 N NH1 . ARG   A 132 ? 0.3373 0.4765 0.2983 -0.0900 -0.0222 0.0040  138 ARG   A NH1 
1025 N NH2 . ARG   A 132 ? 0.3108 0.4764 0.3093 -0.0759 -0.0387 0.0195  138 ARG   A NH2 
1026 N N   . ASP   A 133 ? 0.3572 0.4897 0.3300 -0.0731 -0.0109 0.0290  139 ASP   A N   
1027 C CA  . ASP   A 133 ? 0.3708 0.5012 0.3273 -0.0817 -0.0135 0.0372  139 ASP   A CA  
1028 C C   . ASP   A 133 ? 0.3755 0.4964 0.3380 -0.0766 -0.0001 0.0368  139 ASP   A C   
1029 O O   . ASP   A 133 ? 0.3888 0.5014 0.3313 -0.0851 0.0037  0.0413  139 ASP   A O   
1030 C CB  . ASP   A 133 ? 0.3760 0.5254 0.3486 -0.0798 -0.0313 0.0502  139 ASP   A CB  
1031 C CG  . ASP   A 133 ? 0.4237 0.5827 0.4316 -0.0643 -0.0327 0.0530  139 ASP   A CG  
1032 O OD1 . ASP   A 133 ? 0.4224 0.5816 0.4463 -0.0548 -0.0289 0.0454  139 ASP   A OD1 
1033 O OD2 . ASP   A 133 ? 0.4465 0.6115 0.4643 -0.0627 -0.0377 0.0632  139 ASP   A OD2 
1034 N N   . LEU   A 134 ? 0.3534 0.4754 0.3435 -0.0637 0.0064  0.0326  140 LEU   A N   
1035 C CA  . LEU   A 134 ? 0.3474 0.4631 0.3518 -0.0580 0.0180  0.0333  140 LEU   A CA  
1036 C C   . LEU   A 134 ? 0.3631 0.4580 0.3511 -0.0639 0.0396  0.0264  140 LEU   A C   
1037 O O   . LEU   A 134 ? 0.3539 0.4444 0.3612 -0.0570 0.0503  0.0218  140 LEU   A O   
1038 C CB  . LEU   A 134 ? 0.3277 0.4532 0.3681 -0.0445 0.0140  0.0327  140 LEU   A CB  
1039 C CG  . LEU   A 134 ? 0.3209 0.4616 0.3761 -0.0390 -0.0024 0.0370  140 LEU   A CG  
1040 C CD1 . LEU   A 134 ? 0.3117 0.4569 0.3929 -0.0293 -0.0055 0.0343  140 LEU   A CD1 
1041 C CD2 . LEU   A 134 ? 0.3221 0.4674 0.3799 -0.0400 -0.0074 0.0461  140 LEU   A CD2 
1042 N N   . LEU   A 135 ? 0.3862 0.4671 0.3382 -0.0777 0.0465  0.0263  141 LEU   A N   
1043 C CA  . LEU   A 135 ? 0.4214 0.4773 0.3504 -0.0861 0.0701  0.0183  141 LEU   A CA  
1044 C C   . LEU   A 135 ? 0.4443 0.4915 0.3991 -0.0775 0.0902  0.0183  141 LEU   A C   
1045 O O   . LEU   A 135 ? 0.4563 0.4870 0.4137 -0.0774 0.1115  0.0113  141 LEU   A O   
1046 C CB  . LEU   A 135 ? 0.4463 0.4872 0.3259 -0.1051 0.0717  0.0192  141 LEU   A CB  
1047 C CG  . LEU   A 135 ? 0.4730 0.5229 0.3273 -0.1169 0.0504  0.0219  141 LEU   A CG  
1048 C CD1 . LEU   A 135 ? 0.5118 0.5428 0.3118 -0.1393 0.0529  0.0229  141 LEU   A CD1 
1049 C CD2 . LEU   A 135 ? 0.4811 0.5303 0.3358 -0.1172 0.0503  0.0125  141 LEU   A CD2 
1050 N N   . TRP   A 136 ? 0.4377 0.4960 0.4152 -0.0702 0.0844  0.0268  142 TRP   A N   
1051 C CA  . TRP   A 136 ? 0.4483 0.5013 0.4554 -0.0624 0.1011  0.0290  142 TRP   A CA  
1052 C C   . TRP   A 136 ? 0.4654 0.5250 0.5140 -0.0504 0.1046  0.0274  142 TRP   A C   
1053 O O   . TRP   A 136 ? 0.4665 0.5198 0.5419 -0.0454 0.1216  0.0294  142 TRP   A O   
1054 C CB  . TRP   A 136 ? 0.4277 0.4927 0.4513 -0.0580 0.0913  0.0389  142 TRP   A CB  
1055 C CG  . TRP   A 136 ? 0.4033 0.4912 0.4456 -0.0508 0.0659  0.0434  142 TRP   A CG  
1056 C CD1 . TRP   A 136 ? 0.4110 0.5082 0.4363 -0.0551 0.0484  0.0479  142 TRP   A CD1 
1057 C CD2 . TRP   A 136 ? 0.3801 0.4824 0.4622 -0.0392 0.0566  0.0444  142 TRP   A CD2 
1058 N NE1 . TRP   A 136 ? 0.3945 0.5091 0.4472 -0.0458 0.0322  0.0502  142 TRP   A NE1 
1059 C CE2 . TRP   A 136 ? 0.3786 0.4954 0.4623 -0.0370 0.0363  0.0474  142 TRP   A CE2 
1060 C CE3 . TRP   A 136 ? 0.3787 0.4826 0.4957 -0.0314 0.0631  0.0444  142 TRP   A CE3 
1061 C CZ2 . TRP   A 136 ? 0.3701 0.4990 0.4819 -0.0287 0.0243  0.0474  142 TRP   A CZ2 
1062 C CZ3 . TRP   A 136 ? 0.3700 0.4888 0.5151 -0.0240 0.0471  0.0463  142 TRP   A CZ3 
1063 C CH2 . TRP   A 136 ? 0.3660 0.4953 0.5051 -0.0233 0.0289  0.0466  142 TRP   A CH2 
1064 N N   . LEU   A 137 ? 0.4730 0.5452 0.5284 -0.0464 0.0888  0.0252  143 LEU   A N   
1065 C CA  . LEU   A 137 ? 0.4855 0.5636 0.5761 -0.0368 0.0899  0.0254  143 LEU   A CA  
1066 C C   . LEU   A 137 ? 0.5333 0.5918 0.6245 -0.0387 0.1159  0.0205  143 LEU   A C   
1067 O O   . LEU   A 137 ? 0.5207 0.5823 0.6499 -0.0303 0.1222  0.0246  143 LEU   A O   
1068 C CB  . LEU   A 137 ? 0.4731 0.5650 0.5628 -0.0340 0.0698  0.0235  143 LEU   A CB  
1069 C CG  . LEU   A 137 ? 0.4657 0.5757 0.5652 -0.0295 0.0471  0.0280  143 LEU   A CG  
1070 C CD1 . LEU   A 137 ? 0.4659 0.5841 0.5575 -0.0288 0.0327  0.0247  143 LEU   A CD1 
1071 C CD2 . LEU   A 137 ? 0.4603 0.5792 0.5976 -0.0215 0.0427  0.0340  143 LEU   A CD2 
1072 N N   . ASP   A 138 ? 0.5882 0.6257 0.6380 -0.0507 0.1309  0.0125  144 ASP   A N   
1073 C CA  . ASP   A 138 ? 0.6400 0.6527 0.6843 -0.0548 0.1602  0.0056  144 ASP   A CA  
1074 C C   . ASP   A 138 ? 0.6836 0.6777 0.7343 -0.0561 0.1878  0.0069  144 ASP   A C   
1075 O O   . ASP   A 138 ? 0.6990 0.6676 0.7413 -0.0609 0.2167  0.0002  144 ASP   A O   
1076 C CB  . ASP   A 138 ? 0.6889 0.6827 0.6789 -0.0707 0.1653  -0.0054 144 ASP   A CB  
1077 C CG  . ASP   A 138 ? 0.7649 0.7719 0.7441 -0.0720 0.1436  -0.0081 144 ASP   A CG  
1078 O OD1 . ASP   A 138 ? 0.7619 0.7898 0.7751 -0.0599 0.1278  -0.0028 144 ASP   A OD1 
1079 O OD2 . ASP   A 138 ? 0.8196 0.8154 0.7552 -0.0865 0.1420  -0.0152 144 ASP   A OD2 
1080 N N   . GLU   A 139 ? 0.7044 0.7076 0.7670 -0.0532 0.1821  0.0147  145 GLU   A N   
1081 C CA  . GLU   A 139 ? 0.7449 0.7293 0.8132 -0.0548 0.2100  0.0163  145 GLU   A CA  
1082 C C   . GLU   A 139 ? 0.7526 0.7552 0.8620 -0.0452 0.2016  0.0280  145 GLU   A C   
1083 O O   . GLU   A 139 ? 0.7454 0.7717 0.8641 -0.0408 0.1728  0.0332  145 GLU   A O   
1084 C CB  . GLU   A 139 ? 0.8132 0.7724 0.8186 -0.0723 0.2220  0.0089  145 GLU   A CB  
1085 C CG  . GLU   A 139 ? 0.8885 0.8626 0.8681 -0.0775 0.1950  0.0143  145 GLU   A CG  
1086 C CD  . GLU   A 139 ? 1.0223 0.9829 0.9381 -0.0958 0.1891  0.0079  145 GLU   A CD  
1087 O OE1 . GLU   A 139 ? 1.0562 1.0157 0.9420 -0.1049 0.1807  0.0131  145 GLU   A OE1 
1088 O OE2 . GLU   A 139 ? 1.0686 1.0199 0.9655 -0.1018 0.1922  -0.0013 145 GLU   A OE2 
1089 N N   . GLU   A 140 ? 0.7668 0.7561 0.9005 -0.0428 0.2287  0.0318  146 GLU   A N   
1090 C CA  . GLU   A 140 ? 0.7703 0.7727 0.9448 -0.0353 0.2262  0.0429  146 GLU   A CA  
1091 C C   . GLU   A 140 ? 0.7591 0.7938 0.9824 -0.0238 0.1967  0.0518  146 GLU   A C   
1092 O O   . GLU   A 140 ? 0.7464 0.7894 1.0234 -0.0153 0.2019  0.0601  146 GLU   A O   
1093 C CB  . GLU   A 140 ? 0.8154 0.8127 0.9513 -0.0438 0.2220  0.0435  146 GLU   A CB  
1094 C CG  . GLU   A 140 ? 0.8698 0.8930 1.0251 -0.0383 0.1933  0.0522  146 GLU   A CG  
1095 C CD  . GLU   A 140 ? 0.9433 0.9737 1.1486 -0.0308 0.2006  0.0622  146 GLU   A CD  
1096 O OE1 . GLU   A 140 ? 0.9450 0.9968 1.1743 -0.0257 0.1770  0.0686  146 GLU   A OE1 
1097 O OE2 . GLU   A 140 ? 0.9725 0.9857 1.1938 -0.0306 0.2311  0.0635  146 GLU   A OE2 
1098 N N1  . A1BPI B .   ? 0.4030 0.4166 0.4070 -0.0361 0.0184  -0.0417 201 A1BPI A N1  
1099 N N3  . A1BPI B .   ? 0.4000 0.4224 0.3529 -0.0338 0.0201  -0.0358 201 A1BPI A N3  
1100 C C4  . A1BPI B .   ? 0.4183 0.4103 0.4088 -0.0339 0.0476  -0.0484 201 A1BPI A C4  
1101 C C5  . A1BPI B .   ? 0.4259 0.4177 0.4018 -0.0417 0.0291  -0.0498 201 A1BPI A C5  
1102 C C6  . A1BPI B .   ? 0.4041 0.4190 0.4029 -0.0426 0.0027  -0.0417 201 A1BPI A C6  
1103 C C7  . A1BPI B .   ? 0.3837 0.4202 0.4194 -0.0333 0.0001  -0.0326 201 A1BPI A C7  
1104 C C8  . A1BPI B .   ? 0.3675 0.4223 0.4213 -0.0237 0.0041  -0.0248 201 A1BPI A C8  
1105 C C10 . A1BPI B .   ? 0.3783 0.4148 0.4201 -0.0245 0.0210  -0.0315 201 A1BPI A C10 
1106 C C13 . A1BPI B .   ? 0.4381 0.4134 0.3643 -0.0405 0.0557  -0.0517 201 A1BPI A C13 
1107 O O1  . A1BPI B .   ? 0.3421 0.4089 0.4476 -0.0122 0.0179  -0.0137 201 A1BPI A O1  
1108 C C9  . A1BPI B .   ? 0.3479 0.4205 0.4356 -0.0154 0.0057  -0.0148 201 A1BPI A C9  
1109 N N2  . A1BPI B .   ? 0.3322 0.4254 0.4286 -0.0126 -0.0056 -0.0068 201 A1BPI A N2  
1110 O O   . A1BPI B .   ? 0.4545 0.4266 0.3949 -0.0537 0.0246  -0.0573 201 A1BPI A O   
1111 C C3  . A1BPI B .   ? 0.4237 0.4096 0.3888 -0.0370 0.0487  -0.0504 201 A1BPI A C3  
1112 C C11 . A1BPI B .   ? 0.4401 0.3984 0.3835 -0.0415 0.0694  -0.0593 201 A1BPI A C11 
1113 C C12 . A1BPI B .   ? 0.4509 0.4039 0.3746 -0.0432 0.0732  -0.0599 201 A1BPI A C12 
1114 C C14 . A1BPI B .   ? 0.4136 0.4153 0.3609 -0.0364 0.0358  -0.0435 201 A1BPI A C14 
1115 C C2  . A1BPI B .   ? 0.4061 0.4129 0.3719 -0.0348 0.0325  -0.0429 201 A1BPI A C2  
1116 C C1  . A1BPI B .   ? 0.3867 0.4187 0.3685 -0.0312 0.0139  -0.0343 201 A1BPI A C1  
1117 N N   . A1BPI B .   ? 0.3841 0.4233 0.3576 -0.0309 0.0082  -0.0310 201 A1BPI A N   
1118 C C   . A1BPI B .   ? 0.3648 0.4241 0.3474 -0.0287 -0.0074 -0.0233 201 A1BPI A C   
# 
