data_7HWA
# 
_entry.id   7HWA 
# 
_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   7HWA         pdb_00007hwa 10.2210/pdb7hwa/pdb 
WWPDB D_1001408010 ?            ?                   
# 
_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                        7HWA 
_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-methoxyphenyl)methyl]-5-oxopyrrolidine-3-carboxamide' 248.278   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    130 ?         ? ? ? 
# 
_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-methoxyphenyl)methyl]-5-oxopyrrolidine-3-carboxamide' A1BTD 
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 
A1BTD non-polymer         . '(3S)-1-[(2-methoxyphenyl)methyl]-5-oxopyrrolidine-3-carboxamide' ? 'C13 H16 N2 O3'  248.278 
ALA   'L-peptide linking' y ALANINE                                                           ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                          ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                        ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                   ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                          ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                              ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                         ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                   ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                           ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                         ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                             ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                            ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                        ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                     ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                           ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                            ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                         ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                        ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                          ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                            ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                        ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BTD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BTD 
_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 A1BTD 1   201 201 A1BTD LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 92  HOH   HOH A . 
E 5 HOH   2   302 108 HOH   HOH A . 
E 5 HOH   3   303 15  HOH   HOH A . 
E 5 HOH   4   304 63  HOH   HOH A . 
E 5 HOH   5   305 83  HOH   HOH A . 
E 5 HOH   6   306 74  HOH   HOH A . 
E 5 HOH   7   307 125 HOH   HOH A . 
E 5 HOH   8   308 77  HOH   HOH A . 
E 5 HOH   9   309 124 HOH   HOH A . 
E 5 HOH   10  310 67  HOH   HOH A . 
E 5 HOH   11  311 57  HOH   HOH A . 
E 5 HOH   12  312 78  HOH   HOH A . 
E 5 HOH   13  313 89  HOH   HOH A . 
E 5 HOH   14  314 11  HOH   HOH A . 
E 5 HOH   15  315 69  HOH   HOH A . 
E 5 HOH   16  316 4   HOH   HOH A . 
E 5 HOH   17  317 96  HOH   HOH A . 
E 5 HOH   18  318 1   HOH   HOH A . 
E 5 HOH   19  319 93  HOH   HOH A . 
E 5 HOH   20  320 71  HOH   HOH A . 
E 5 HOH   21  321 26  HOH   HOH A . 
E 5 HOH   22  322 123 HOH   HOH A . 
E 5 HOH   23  323 29  HOH   HOH A . 
E 5 HOH   24  324 37  HOH   HOH A . 
E 5 HOH   25  325 38  HOH   HOH A . 
E 5 HOH   26  326 31  HOH   HOH A . 
E 5 HOH   27  327 16  HOH   HOH A . 
E 5 HOH   28  328 24  HOH   HOH A . 
E 5 HOH   29  329 102 HOH   HOH A . 
E 5 HOH   30  330 121 HOH   HOH A . 
E 5 HOH   31  331 107 HOH   HOH A . 
E 5 HOH   32  332 10  HOH   HOH A . 
E 5 HOH   33  333 9   HOH   HOH A . 
E 5 HOH   34  334 41  HOH   HOH A . 
E 5 HOH   35  335 91  HOH   HOH A . 
E 5 HOH   36  336 94  HOH   HOH A . 
E 5 HOH   37  337 27  HOH   HOH A . 
E 5 HOH   38  338 45  HOH   HOH A . 
E 5 HOH   39  339 130 HOH   HOH A . 
E 5 HOH   40  340 56  HOH   HOH A . 
E 5 HOH   41  341 14  HOH   HOH A . 
E 5 HOH   42  342 12  HOH   HOH A . 
E 5 HOH   43  343 101 HOH   HOH A . 
E 5 HOH   44  344 66  HOH   HOH A . 
E 5 HOH   45  345 3   HOH   HOH A . 
E 5 HOH   46  346 80  HOH   HOH A . 
E 5 HOH   47  347 18  HOH   HOH A . 
E 5 HOH   48  348 81  HOH   HOH A . 
E 5 HOH   49  349 8   HOH   HOH A . 
E 5 HOH   50  350 55  HOH   HOH A . 
E 5 HOH   51  351 43  HOH   HOH A . 
E 5 HOH   52  352 46  HOH   HOH A . 
E 5 HOH   53  353 40  HOH   HOH A . 
E 5 HOH   54  354 97  HOH   HOH A . 
E 5 HOH   55  355 129 HOH   HOH A . 
E 5 HOH   56  356 53  HOH   HOH A . 
E 5 HOH   57  357 28  HOH   HOH A . 
E 5 HOH   58  358 5   HOH   HOH A . 
E 5 HOH   59  359 100 HOH   HOH A . 
E 5 HOH   60  360 104 HOH   HOH A . 
E 5 HOH   61  361 79  HOH   HOH A . 
E 5 HOH   62  362 17  HOH   HOH A . 
E 5 HOH   63  363 25  HOH   HOH A . 
E 5 HOH   64  364 42  HOH   HOH A . 
E 5 HOH   65  365 105 HOH   HOH A . 
E 5 HOH   66  366 62  HOH   HOH A . 
E 5 HOH   67  367 58  HOH   HOH A . 
E 5 HOH   68  368 59  HOH   HOH A . 
E 5 HOH   69  369 34  HOH   HOH A . 
E 5 HOH   70  370 73  HOH   HOH A . 
E 5 HOH   71  371 39  HOH   HOH A . 
E 5 HOH   72  372 65  HOH   HOH A . 
E 5 HOH   73  373 72  HOH   HOH A . 
E 5 HOH   74  374 13  HOH   HOH A . 
E 5 HOH   75  375 68  HOH   HOH A . 
E 5 HOH   76  376 88  HOH   HOH A . 
E 5 HOH   77  377 6   HOH   HOH A . 
E 5 HOH   78  378 33  HOH   HOH A . 
E 5 HOH   79  379 19  HOH   HOH A . 
E 5 HOH   80  380 64  HOH   HOH A . 
E 5 HOH   81  381 113 HOH   HOH A . 
E 5 HOH   82  382 132 HOH   HOH A . 
E 5 HOH   83  383 106 HOH   HOH A . 
E 5 HOH   84  384 54  HOH   HOH A . 
E 5 HOH   85  385 50  HOH   HOH A . 
E 5 HOH   86  386 60  HOH   HOH A . 
E 5 HOH   87  387 61  HOH   HOH A . 
E 5 HOH   88  388 75  HOH   HOH A . 
E 5 HOH   89  389 44  HOH   HOH A . 
E 5 HOH   90  390 85  HOH   HOH A . 
E 5 HOH   91  391 22  HOH   HOH A . 
E 5 HOH   92  392 76  HOH   HOH A . 
E 5 HOH   93  393 112 HOH   HOH A . 
E 5 HOH   94  394 98  HOH   HOH A . 
E 5 HOH   95  395 48  HOH   HOH A . 
E 5 HOH   96  396 52  HOH   HOH A . 
E 5 HOH   97  397 30  HOH   HOH A . 
E 5 HOH   98  398 111 HOH   HOH A . 
E 5 HOH   99  399 35  HOH   HOH A . 
E 5 HOH   100 400 122 HOH   HOH A . 
E 5 HOH   101 401 87  HOH   HOH A . 
E 5 HOH   102 402 86  HOH   HOH A . 
E 5 HOH   103 403 32  HOH   HOH A . 
E 5 HOH   104 404 119 HOH   HOH A . 
E 5 HOH   105 405 82  HOH   HOH A . 
E 5 HOH   106 406 70  HOH   HOH A . 
E 5 HOH   107 407 118 HOH   HOH A . 
E 5 HOH   108 408 23  HOH   HOH A . 
E 5 HOH   109 409 103 HOH   HOH A . 
E 5 HOH   110 410 90  HOH   HOH A . 
E 5 HOH   111 411 127 HOH   HOH A . 
E 5 HOH   112 412 51  HOH   HOH A . 
E 5 HOH   113 413 133 HOH   HOH A . 
E 5 HOH   114 414 7   HOH   HOH A . 
E 5 HOH   115 415 20  HOH   HOH A . 
E 5 HOH   116 416 99  HOH   HOH A . 
E 5 HOH   117 417 109 HOH   HOH A . 
E 5 HOH   118 418 115 HOH   HOH A . 
E 5 HOH   119 419 128 HOH   HOH A . 
E 5 HOH   120 420 21  HOH   HOH A . 
E 5 HOH   121 421 95  HOH   HOH A . 
E 5 HOH   122 422 2   HOH   HOH A . 
E 5 HOH   123 423 84  HOH   HOH A . 
E 5 HOH   124 424 116 HOH   HOH A . 
E 5 HOH   125 425 47  HOH   HOH A . 
E 5 HOH   126 426 114 HOH   HOH A . 
E 5 HOH   127 427 131 HOH   HOH A . 
E 5 HOH   128 428 117 HOH   HOH A . 
E 5 HOH   129 429 120 HOH   HOH A . 
E 5 HOH   130 430 126 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           7HWA 
_cell.length_a           73.074 
_cell.length_b           60.967 
_cell.length_c           32.571 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.04 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWA 
_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          7HWA 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.28 
_exptl_crystal.density_percent_sol   46.04 
_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   2024-11-22 
_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                     7HWA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             32.53 
_reflns.d_resolution_high            1.38 
_reflns.number_obs                   28863 
_reflns.percent_possible_obs         98.6 
_reflns.pdbx_Rmerge_I_obs            0.099 
_reflns.pdbx_netI_over_sigmaI        8.7 
_reflns.pdbx_redundancy              4.8 
_reflns.pdbx_Rrim_I_all              0.111 
_reflns.pdbx_Rpim_I_all              0.049 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     137710 
_reflns.pdbx_chi_squared             0.89 
_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                  1.38 
_reflns_shell.d_res_low                   1.46 
_reflns_shell.number_measured_all         13655 
_reflns_shell.number_unique_obs           3990 
_reflns_shell.Rmerge_I_obs                1.452 
_reflns_shell.pdbx_chi_squared            0.75 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        93.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             1.701 
_reflns_shell.pdbx_Rpim_I_all             0.869 
_reflns_shell.pdbx_CC_half                0.387 
_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                                 7HWA 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     28618 
_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                             32.52 
_refine.ls_d_res_high                            1.381 
_refine.ls_percent_reflns_obs                    97.6 
_refine.ls_R_factor_obs                          0.1875 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1859 
_refine.ls_R_factor_R_free                       0.2203 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.630 
_refine.ls_number_reflns_R_free                  1324 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               20.39 
_refine.aniso_B[1][1]                            -3.96650 
_refine.aniso_B[2][2]                            2.90320 
_refine.aniso_B[3][3]                            1.06330 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.88160 
_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             0.059 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.063 
_refine.pdbx_overall_SU_R_Blow_DPI               0.061 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.065 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWA 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               1227 
_refine_hist.d_res_high                       1.381 
_refine_hist.d_res_low                        32.52 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  1126 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  1532 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  375  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1126 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.52  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.59 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  970  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.38 
_refine_ls_shell.d_res_low                        1.39 
_refine_ls_shell.number_reflns_R_work             545 
_refine_ls_shell.R_factor_R_work                  0.2927 
_refine_ls_shell.percent_reflns_obs               80.46 
_refine_ls_shell.R_factor_R_free                  0.3798 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.89 
_refine_ls_shell.number_reflns_R_free             28 
_refine_ls_shell.number_reflns_all                573 
_refine_ls_shell.R_factor_all                     0.2965 
# 
_struct.entry_id                  7HWA 
_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-0032721-001 (A71EV2A-x3895)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWA 
_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              7HWA 
_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 ? ? ? ? ? ? ? 2.328 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
# 
_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_555 111.0 ? 
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_555 106.1 ? 
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_555 116.3 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.1 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.1 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 115.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HWA 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 430 ? ? 1_555 O A HOH 430 ? ? 2_656 0.69 
2 1 O A HOH 302 ? ? 1_555 O A HOH 302 ? ? 2_656 0.92 
# 
_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         15.1511 
_pdbx_refine_tls.origin_y         7.0395 
_pdbx_refine_tls.origin_z         14.1546 
_pdbx_refine_tls.T[1][1]          -0.0293 
_pdbx_refine_tls.T[2][2]          -0.0106 
_pdbx_refine_tls.T[3][3]          -0.0164 
_pdbx_refine_tls.T[1][2]          -0.0041 
_pdbx_refine_tls.T[1][3]          -0.0128 
_pdbx_refine_tls.T[2][3]          -0.0045 
_pdbx_refine_tls.L[1][1]          0.8386 
_pdbx_refine_tls.L[2][2]          2.1965 
_pdbx_refine_tls.L[3][3]          0.5625 
_pdbx_refine_tls.L[1][2]          0.7084 
_pdbx_refine_tls.L[1][3]          -0.2812 
_pdbx_refine_tls.L[2][3]          -0.5279 
_pdbx_refine_tls.S[1][1]          -0.0541 
_pdbx_refine_tls.S[1][2]          0.0247 
_pdbx_refine_tls.S[1][3]          0.0687 
_pdbx_refine_tls.S[2][1]          0.0169 
_pdbx_refine_tls.S[2][2]          0.0675 
_pdbx_refine_tls.S[2][3]          -0.0695 
_pdbx_refine_tls.S[3][1]          0.0291 
_pdbx_refine_tls.S[3][2]          -0.0438 
_pdbx_refine_tls.S[3][3]          -0.0134 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BTD N1   N  N N 1   
A1BTD C4   C  Y N 2   
A1BTD C5   C  Y N 3   
A1BTD C6   C  Y N 4   
A1BTD C7   C  N N 5   
A1BTD C8   C  N N 6   
A1BTD C10  C  N N 7   
A1BTD O2   O  N N 8   
A1BTD C12  C  N N 9   
A1BTD C11  C  N N 10  
A1BTD C9   C  N S 11  
A1BTD O1   O  N N 12  
A1BTD N    N  N N 13  
A1BTD C1   C  Y N 14  
A1BTD O    O  N N 15  
A1BTD C    C  N N 16  
A1BTD C3   C  Y N 17  
A1BTD C2   C  Y N 18  
A1BTD H13  H  N N 19  
A1BTD H12  H  N N 20  
A1BTD H6   H  N N 21  
A1BTD H7   H  N N 22  
A1BTD H9   H  N N 23  
A1BTD H8   H  N N 24  
A1BTD H11  H  N N 25  
A1BTD H10  H  N N 26  
A1BTD H14  H  N N 27  
A1BTD H15  H  N N 28  
A1BTD H    H  N N 29  
A1BTD H3   H  N N 30  
A1BTD H2   H  N N 31  
A1BTD H1   H  N N 32  
A1BTD H5   H  N N 33  
A1BTD H4   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
DMS   S    S  N N 122 
DMS   O    O  N N 123 
DMS   C1   C  N N 124 
DMS   C2   C  N N 125 
DMS   H11  H  N N 126 
DMS   H12  H  N N 127 
DMS   H13  H  N N 128 
DMS   H21  H  N N 129 
DMS   H22  H  N N 130 
DMS   H23  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
HIS   N    N  N N 181 
HIS   CA   C  N S 182 
HIS   C    C  N N 183 
HIS   O    O  N N 184 
HIS   CB   C  N N 185 
HIS   CG   C  Y N 186 
HIS   ND1  N  Y N 187 
HIS   CD2  C  Y N 188 
HIS   CE1  C  Y N 189 
HIS   NE2  N  Y N 190 
HIS   OXT  O  N N 191 
HIS   H    H  N N 192 
HIS   H2   H  N N 193 
HIS   HA   H  N N 194 
HIS   HB2  H  N N 195 
HIS   HB3  H  N N 196 
HIS   HD1  H  N N 197 
HIS   HD2  H  N N 198 
HIS   HE1  H  N N 199 
HIS   HE2  H  N N 200 
HIS   HXT  H  N N 201 
HOH   O    O  N N 202 
HOH   H1   H  N N 203 
HOH   H2   H  N N 204 
ILE   N    N  N N 205 
ILE   CA   C  N S 206 
ILE   C    C  N N 207 
ILE   O    O  N N 208 
ILE   CB   C  N S 209 
ILE   CG1  C  N N 210 
ILE   CG2  C  N N 211 
ILE   CD1  C  N N 212 
ILE   OXT  O  N N 213 
ILE   H    H  N N 214 
ILE   H2   H  N N 215 
ILE   HA   H  N N 216 
ILE   HB   H  N N 217 
ILE   HG12 H  N N 218 
ILE   HG13 H  N N 219 
ILE   HG21 H  N N 220 
ILE   HG22 H  N N 221 
ILE   HG23 H  N N 222 
ILE   HD11 H  N N 223 
ILE   HD12 H  N N 224 
ILE   HD13 H  N N 225 
ILE   HXT  H  N N 226 
LEU   N    N  N N 227 
LEU   CA   C  N S 228 
LEU   C    C  N N 229 
LEU   O    O  N N 230 
LEU   CB   C  N N 231 
LEU   CG   C  N N 232 
LEU   CD1  C  N N 233 
LEU   CD2  C  N N 234 
LEU   OXT  O  N N 235 
LEU   H    H  N N 236 
LEU   H2   H  N N 237 
LEU   HA   H  N N 238 
LEU   HB2  H  N N 239 
LEU   HB3  H  N N 240 
LEU   HG   H  N N 241 
LEU   HD11 H  N N 242 
LEU   HD12 H  N N 243 
LEU   HD13 H  N N 244 
LEU   HD21 H  N N 245 
LEU   HD22 H  N N 246 
LEU   HD23 H  N N 247 
LEU   HXT  H  N N 248 
LYS   N    N  N N 249 
LYS   CA   C  N S 250 
LYS   C    C  N N 251 
LYS   O    O  N N 252 
LYS   CB   C  N N 253 
LYS   CG   C  N N 254 
LYS   CD   C  N N 255 
LYS   CE   C  N N 256 
LYS   NZ   N  N N 257 
LYS   OXT  O  N N 258 
LYS   H    H  N N 259 
LYS   H2   H  N N 260 
LYS   HA   H  N N 261 
LYS   HB2  H  N N 262 
LYS   HB3  H  N N 263 
LYS   HG2  H  N N 264 
LYS   HG3  H  N N 265 
LYS   HD2  H  N N 266 
LYS   HD3  H  N N 267 
LYS   HE2  H  N N 268 
LYS   HE3  H  N N 269 
LYS   HZ1  H  N N 270 
LYS   HZ2  H  N N 271 
LYS   HZ3  H  N N 272 
LYS   HXT  H  N N 273 
MET   N    N  N N 274 
MET   CA   C  N S 275 
MET   C    C  N N 276 
MET   O    O  N N 277 
MET   CB   C  N N 278 
MET   CG   C  N N 279 
MET   SD   S  N N 280 
MET   CE   C  N N 281 
MET   OXT  O  N N 282 
MET   H    H  N N 283 
MET   H2   H  N N 284 
MET   HA   H  N N 285 
MET   HB2  H  N N 286 
MET   HB3  H  N N 287 
MET   HG2  H  N N 288 
MET   HG3  H  N N 289 
MET   HE1  H  N N 290 
MET   HE2  H  N N 291 
MET   HE3  H  N N 292 
MET   HXT  H  N N 293 
PHE   N    N  N N 294 
PHE   CA   C  N S 295 
PHE   C    C  N N 296 
PHE   O    O  N N 297 
PHE   CB   C  N N 298 
PHE   CG   C  Y N 299 
PHE   CD1  C  Y N 300 
PHE   CD2  C  Y N 301 
PHE   CE1  C  Y N 302 
PHE   CE2  C  Y N 303 
PHE   CZ   C  Y N 304 
PHE   OXT  O  N N 305 
PHE   H    H  N N 306 
PHE   H2   H  N N 307 
PHE   HA   H  N N 308 
PHE   HB2  H  N N 309 
PHE   HB3  H  N N 310 
PHE   HD1  H  N N 311 
PHE   HD2  H  N N 312 
PHE   HE1  H  N N 313 
PHE   HE2  H  N N 314 
PHE   HZ   H  N N 315 
PHE   HXT  H  N N 316 
PRO   N    N  N N 317 
PRO   CA   C  N S 318 
PRO   C    C  N N 319 
PRO   O    O  N N 320 
PRO   CB   C  N N 321 
PRO   CG   C  N N 322 
PRO   CD   C  N N 323 
PRO   OXT  O  N N 324 
PRO   H    H  N N 325 
PRO   HA   H  N N 326 
PRO   HB2  H  N N 327 
PRO   HB3  H  N N 328 
PRO   HG2  H  N N 329 
PRO   HG3  H  N N 330 
PRO   HD2  H  N N 331 
PRO   HD3  H  N N 332 
PRO   HXT  H  N N 333 
SER   N    N  N N 334 
SER   CA   C  N S 335 
SER   C    C  N N 336 
SER   O    O  N N 337 
SER   CB   C  N N 338 
SER   OG   O  N N 339 
SER   OXT  O  N N 340 
SER   H    H  N N 341 
SER   H2   H  N N 342 
SER   HA   H  N N 343 
SER   HB2  H  N N 344 
SER   HB3  H  N N 345 
SER   HG   H  N N 346 
SER   HXT  H  N N 347 
THR   N    N  N N 348 
THR   CA   C  N S 349 
THR   C    C  N N 350 
THR   O    O  N N 351 
THR   CB   C  N R 352 
THR   OG1  O  N N 353 
THR   CG2  C  N N 354 
THR   OXT  O  N N 355 
THR   H    H  N N 356 
THR   H2   H  N N 357 
THR   HA   H  N N 358 
THR   HB   H  N N 359 
THR   HG1  H  N N 360 
THR   HG21 H  N N 361 
THR   HG22 H  N N 362 
THR   HG23 H  N N 363 
THR   HXT  H  N N 364 
TRP   N    N  N N 365 
TRP   CA   C  N S 366 
TRP   C    C  N N 367 
TRP   O    O  N N 368 
TRP   CB   C  N N 369 
TRP   CG   C  Y N 370 
TRP   CD1  C  Y N 371 
TRP   CD2  C  Y N 372 
TRP   NE1  N  Y N 373 
TRP   CE2  C  Y N 374 
TRP   CE3  C  Y N 375 
TRP   CZ2  C  Y N 376 
TRP   CZ3  C  Y N 377 
TRP   CH2  C  Y N 378 
TRP   OXT  O  N N 379 
TRP   H    H  N N 380 
TRP   H2   H  N N 381 
TRP   HA   H  N N 382 
TRP   HB2  H  N N 383 
TRP   HB3  H  N N 384 
TRP   HD1  H  N N 385 
TRP   HE1  H  N N 386 
TRP   HE3  H  N N 387 
TRP   HZ2  H  N N 388 
TRP   HZ3  H  N N 389 
TRP   HH2  H  N N 390 
TRP   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
ZN    ZN   ZN N N 435 
# 
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 
A1BTD C   O    sing N N 1   
A1BTD O   C1   sing N N 2   
A1BTD C1  C2   doub Y N 3   
A1BTD C2  C3   sing Y N 4   
A1BTD C3  C4   doub Y N 5   
A1BTD C4  C5   sing Y N 6   
A1BTD C5  C6   doub Y N 7   
A1BTD C1  C6   sing Y N 8   
A1BTD C6  C7   sing N N 9   
A1BTD C7  N    sing N N 10  
A1BTD N   C8   sing N N 11  
A1BTD C8  C9   sing N N 12  
A1BTD C10 C9   sing N N 13  
A1BTD N1  C10  sing N N 14  
A1BTD O1  C10  doub N N 15  
A1BTD C9  C11  sing N N 16  
A1BTD C11 C12  sing N N 17  
A1BTD N   C12  sing N N 18  
A1BTD C12 O2   doub N N 19  
A1BTD N1  H13  sing N N 20  
A1BTD N1  H12  sing N N 21  
A1BTD C4  H6   sing N N 22  
A1BTD C5  H7   sing N N 23  
A1BTD C7  H9   sing N N 24  
A1BTD C7  H8   sing N N 25  
A1BTD C8  H11  sing N N 26  
A1BTD C8  H10  sing N N 27  
A1BTD C11 H14  sing N N 28  
A1BTD C11 H15  sing N N 29  
A1BTD C9  H    sing N N 30  
A1BTD C   H3   sing N N 31  
A1BTD C   H2   sing N N 32  
A1BTD C   H1   sing N N 33  
A1BTD C3  H5   sing N N 34  
A1BTD C2  H4   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_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                    7HWA 
_atom_sites.fract_transf_matrix[1][1]   0.013685 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000727 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016402 
_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]   0.030745 
_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   ? 19.029 6.298   24.132 1.00 19.96 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.203 6.429   23.270 1.00 19.30 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.258 5.282   22.265 1.00 19.01 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.499 4.299   22.402 1.00 20.65 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.485 6.464   24.117 1.00 23.51 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.604 5.276   24.874 1.00 28.72 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.077 5.444   21.234 1.00 16.31 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.243 4.406   20.221 1.00 16.18 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.561 4.991   18.855 1.00 16.25 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.190 6.137   18.549 1.00 16.16 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.276 4.213   18.035 1.00 15.69 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.635 4.673   16.702 1.00 15.21 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.593 3.509   15.711 1.00 14.77 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.548 2.347   16.131 1.00 16.05 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.058 5.266   16.742 1.00 17.27 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.580 3.809   14.410 1.00 12.98 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.706 2.832   13.329 1.00 14.30 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.095 3.000   12.730 1.00 15.30 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.504 4.123   12.446 1.00 15.36 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.653 3.059   12.209 1.00 14.28 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.238 3.057   12.767 1.00 14.77 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.789 1.979   11.144 1.00 16.14 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.233 3.670   11.714 1.00 15.24 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.845 1.882   12.508 1.00 16.15 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.163 1.981   11.918 1.00 18.35 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.151 1.244   10.581 1.00 19.38 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.991 0.031   10.570 1.00 20.29 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.209 1.364   12.869 1.00 17.64 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.372 2.132   14.158 1.00 17.95 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.196 3.244   14.224 1.00 18.72 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.631 1.808   15.283 1.00 19.83 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.285 4.010   15.383 1.00 19.80 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.704 2.575   16.445 1.00 20.87 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.551 3.661   16.494 1.00 21.23 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.626 4.424   17.629 1.00 22.27 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.246 1.969   9.465  1.00 19.07 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.210 1.375   8.124  1.00 20.48 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.322 2.010   7.292  1.00 21.93 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.427 3.244   7.186  1.00 22.24 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.812 1.572   7.461  1.00 21.84 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.319 3.019   7.564  1.00 22.36 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.822 1.090   6.019  1.00 23.49 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.217 1.172   6.757  1.00 22.04 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.350 1.671   5.987  1.00 23.19 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.194 2.651   6.789  1.00 23.21 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.444 2.394   7.968  1.00 24.06 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.516 3.807   6.222  1.00 23.61 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.249 4.842   6.964  1.00 24.43 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.306 5.894   7.601  1.00 22.47 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.708 7.024   7.823  1.00 22.87 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.300 5.529   6.098  1.00 28.02 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.403 4.591   5.676  1.00 35.66 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.071 3.945   6.504  1.00 37.74 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.602 4.485   4.377  1.00 38.32 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.070 5.510   7.941  1.00 19.99 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.105 6.438   8.537  1.00 18.32 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.576 5.953   9.874  1.00 17.11 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.465 4.751   10.125 1.00 17.80 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.874 6.613   7.605  1.00 18.36 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.210 7.188   6.251  1.00 19.87 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.888 8.403   6.135  1.00 21.43 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.936 6.482   5.089  1.00 21.49 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.238 8.921   4.892  1.00 23.00 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.267 6.997   3.835  1.00 22.86 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.912 8.221   3.743  1.00 25.02 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.249 8.754   2.515  1.00 28.93 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.206 6.940   10.717 1.00 15.64 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.534 6.760   11.998 1.00 15.29 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.262 7.596   11.953 1.00 15.45 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.339 8.805   11.721 1.00 14.40 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.452 7.216   13.160 1.00 16.10 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.756 7.498   14.507 1.00 18.42 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.765 7.669   15.652 1.00 20.93 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.343 8.688   16.610 1.00 21.56 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.860 8.442   17.822 1.00 21.21 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.743 7.190   18.261 1.00 22.76 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.526 9.448   18.626 1.00 20.55 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.090 6.938   12.142 1.00 15.14 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.803 7.641   12.142 1.00 14.82 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.324 7.763   13.572 1.00 15.24 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.147 6.727   14.234 1.00 14.23 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.765 6.859   11.318 1.00 14.00 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.447 7.671   11.193 1.00 13.67 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.339 6.451   9.953  1.00 14.91 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.025 8.977   14.014 1.00 14.35 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.570 9.220   15.378 1.00 13.67 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.360 10.169  15.382 1.00 11.79 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.121 10.904  14.402 1.00 12.71 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.701 9.824   16.261 1.00 15.70 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.793 8.793   16.483 1.00 19.19 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.268 11.131  15.659 1.00 16.52 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.644 10.248  16.499 1.00 11.28 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.611 11.298  16.671 1.00 11.85 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.350 12.639  16.652 1.00 12.76 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.331 12.818  17.415 1.00 13.10 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.869 11.178  18.021 1.00 13.16 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.011 9.934   18.097 1.00 13.43 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.481 8.862   18.513 1.00 13.60 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.765 10.032  17.606 1.00 12.92 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.851 13.594  15.862 1.00 12.11 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.541 14.907  15.768 1.00 12.34 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.639 15.567  17.144 1.00 12.71 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.682 16.151  17.476 1.00 13.13 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.828 15.813  14.777 1.00 13.97 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.603 17.090  14.454 1.00 13.43 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.645 17.976  13.657 1.00 13.15 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.284 19.208  13.167 1.00 14.13 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.326 20.347  13.844 1.00 16.20 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.839 20.416  15.086 1.00 16.80 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.877 21.442  13.292 1.00 15.67 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.576 15.408  17.999 1.00 12.66 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.609 16.081  19.315 1.00 13.69 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.575 15.443  20.333 1.00 15.29 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.850 16.054  21.379 1.00 16.82 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.181 16.221  19.916 1.00 14.31 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.532 14.944  20.397 1.00 13.57 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.902 14.053  19.525 1.00 14.61 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.518 14.413  21.644 1.00 15.89 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.419 13.079  20.297 1.00 15.62 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.798 13.228  21.574 1.00 16.27 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.098 14.255  20.016 1.00 14.40 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.032 13.557  20.855 1.00 15.12 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.453 13.565  20.245 1.00 16.07 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.366 12.965  20.834 1.00 17.94 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.548 12.106  21.132 1.00 15.89 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.191 12.035  21.858 1.00 16.82 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.770 10.561  22.135 1.00 16.82 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.207 12.831  23.186 1.00 15.63 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.665 14.211  19.056 1.00 14.83 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.995 14.221  18.452 1.00 15.99 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.035 14.834  19.359 1.00 15.88 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.761 15.816  20.043 1.00 17.25 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.951 14.979  17.133 1.00 15.87 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.230 14.263  19.341 1.00 16.67 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.338 14.747  20.171 1.00 18.13 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.198 15.824  19.451 1.00 19.83 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.027 16.048  18.254 1.00 19.39 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.246 13.540  20.545 1.00 20.01 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.945 13.123  19.367 1.00 21.81 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.476 12.408  21.177 1.00 20.58 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.182 16.444  20.162 1.00 21.16 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.108 17.376  19.512 1.00 22.34 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.848 16.700  18.352 1.00 21.45 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.999 17.297  17.300 1.00 23.07 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.162 17.929  20.508 1.00 26.40 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.573 18.640  21.682 1.00 34.34 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.574 19.581  21.527 1.00 37.91 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.878 18.536  23.000 1.00 37.40 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.288 20.011  22.747 1.00 39.14 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.057 19.420  23.667 1.00 39.32 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.303 15.440  18.533 1.00 20.72 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.020 14.710  17.464 1.00 21.23 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.086 14.438  16.268 1.00 19.15 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.524 14.503  15.116 1.00 19.49 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.523 13.397  18.024 1.00 24.67 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.405 12.603  17.072 1.00 33.91 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.543 12.995  16.782 1.00 37.43 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.905 11.472  16.564 1.00 36.28 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.788 14.136  16.522 1.00 18.19 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.839 13.956  15.405 1.00 17.51 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.769 15.255  14.562 1.00 17.14 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.831 15.198  13.338 1.00 17.80 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.411 13.644  15.900 1.00 17.22 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.275 12.231  16.388 1.00 19.40 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.854 11.330  15.747 1.00 20.44 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.603 12.021  17.432 1.00 17.20 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.653 16.427  15.227 1.00 17.28 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.571 17.698  14.509 1.00 17.17 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.927 18.066  13.829 1.00 18.84 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.910 18.676  12.763 1.00 18.91 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.111 18.821  15.468 1.00 15.80 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.622 18.881  15.662 1.00 15.58 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.918 18.417  16.729 1.00 16.29 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.661 19.393  14.726 1.00 15.08 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.562 18.641  16.535 1.00 15.61 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.379 19.228  15.304 1.00 15.40 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.764 20.008  13.464 1.00 16.22 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.213 19.670  14.676 1.00 16.59 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.596 20.408  12.823 1.00 16.79 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.351 20.256  13.434 1.00 16.92 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.066 17.695  14.424 1.00 20.40 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.375 17.964  13.812 1.00 21.13 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.658 17.059  12.579 1.00 21.98 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.578 17.344  11.786 1.00 22.33 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.475 17.756  14.847 1.00 21.08 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.889 15.951  12.443 1.00 20.34 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.012 15.015  11.307 1.00 20.04 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.650 14.919  10.582 1.00 18.90 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.294 13.859  10.077 1.00 18.95 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.459 13.654  11.820 1.00 20.91 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.864 13.730  12.370 1.00 25.44 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.833 13.813  11.606 1.00 26.60 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.971 13.744  13.697 1.00 25.51 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.911 16.039  10.528 1.00 18.58 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.586 16.074  9.923  1.00 18.25 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.611 15.707  8.438  1.00 19.64 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.397 16.277  7.679  1.00 20.91 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.980 17.485  10.106 1.00 17.78 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.618 17.699  9.461  1.00 17.95 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.556 16.844  10.152 1.00 18.49 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.232 19.190  9.470  1.00 18.92 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.692 14.809  8.017  1.00 18.23 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.443 14.453  6.626  1.00 19.21 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.098 15.090  6.169  1.00 19.21 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.023 15.724  5.105  1.00 21.51 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.408 12.918  6.458  1.00 19.01 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.956 12.552  5.045  1.00 19.99 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.783 12.301  6.781  1.00 19.24 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.038 14.939  6.976  1.00 17.60 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.696 15.432  6.650  1.00 16.09 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.875 15.527  7.941  1.00 14.84 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.043 14.704  8.848  1.00 14.94 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.017 14.469  5.650  1.00 16.52 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.548 14.714  5.398  1.00 17.34 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.982 15.622  4.541  1.00 19.14 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.464 13.991  5.994  1.00 16.66 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.596 15.487  4.564  1.00 19.02 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.262 14.506  5.466  1.00 17.82 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.396 12.968  6.948  1.00 17.05 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.020 13.971  5.803  1.00 18.15 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.166 12.461  7.290  1.00 18.02 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.995 12.978  6.735  1.00 18.31 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.034 16.532  8.042  1.00 14.07 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.119 16.642  9.179  1.00 14.98 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.788 17.270  8.688  1.00 14.09 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.767 18.099  7.754  1.00 14.95 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.702 17.398  10.377 1.00 16.16 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.202 18.808  10.048 1.00 15.98 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.184 19.931  9.963  1.00 17.09 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.460 20.906  9.222  1.00 19.81 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.130 19.865  10.632 1.00 16.26 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.675 16.848  9.312  1.00 14.29 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.369 17.376  8.996  1.00 14.47 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.563 17.535  10.264 1.00 14.56 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.160 16.550  10.861 1.00 13.66 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.689 16.535  7.883  1.00 14.75 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.385 17.085  7.398  1.00 19.22 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.747 17.834  8.150  1.00 22.21 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.991 16.767  6.235  1.00 19.53 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.394 18.792  10.736 1.00 14.12 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.668 19.087  11.956 0.50 14.68 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.679 19.043  11.974 0.50 15.37 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.213 18.608  11.873 1.00 14.77 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.662 18.082  12.843 1.00 15.53 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.687 20.589  12.216 0.50 16.08 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.774 20.514  12.366 0.50 18.85 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.043 20.882  13.443 0.50 17.74 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.007 21.321  11.490 0.50 23.68 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.594 18.760  10.691 1.00 14.09 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.203 18.343  10.534 1.00 14.13 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.069 16.835  10.644 1.00 13.92 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.963 16.396  10.917 1.00 15.78 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.625 18.827  9.212  1.00 18.60 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.090 18.074  8.105  1.00 24.49 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.169 16.064  10.504 1.00 12.69 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.123 14.590  10.625 1.00 13.20 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.679 14.082  11.960 1.00 12.89 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.590 12.881  12.237 1.00 12.38 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.908 13.911  9.455  1.00 14.13 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.181 14.078  8.128  1.00 14.56 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.017 13.458  7.001  1.00 16.16 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.988 11.989  7.089  1.00 14.89 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.112 11.171  6.042  1.00 15.20 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.230 11.663  4.809  1.00 16.74 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.061 9.860   6.213  1.00 14.45 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.324 14.955  12.747 1.00 12.31 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.053 14.558  13.960 1.00 11.81 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.163 13.580  13.618 1.00 10.90 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.473 12.726  14.456 1.00 11.15 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.151 14.005  15.083 1.00 12.05 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.886 13.727  16.386 1.00 12.43 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.706 14.593  16.811 1.00 13.62 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.619 12.654  17.009 1.00 12.04 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.832 13.753  12.447 1.00 11.22 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.952 12.870  12.076 1.00 10.89 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.243 13.644  11.875 1.00 11.92 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.234 14.762  11.355 1.00 12.80 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.689 12.081  10.795 1.00 12.02 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.667 10.918  10.937 1.00 12.59 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.540 10.165  9.598  1.00 13.31 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.045 9.919   12.044 1.00 13.51 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.357 12.974  12.182 1.00 11.16 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.681 13.487  11.856 1.00 12.00 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.543 12.288  11.492 1.00 13.84 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.468 11.250  12.159 1.00 14.25 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.302 14.240  13.043 1.00 12.30 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.677 14.878  12.767 1.00 13.27 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.822 16.192  13.553 1.00 14.12 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.826 13.932  13.202 1.00 15.05 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.384 12.437  10.462 1.00 13.87 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.317 11.399  10.028 1.00 13.28 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.734 11.989  10.085 1.00 14.18 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.982 13.101  9.569  1.00 14.96 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.994 10.896  8.597  1.00 14.22 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.020 9.860   8.113  1.00 15.02 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.570 10.319  8.525  1.00 15.27 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.614 11.266  10.769 1.00 13.74 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.021 11.658  10.854 1.00 14.54 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.912 10.599  10.222 1.00 17.39 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.481 9.481   9.990  1.00 18.24 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.421 11.941  12.299 1.00 15.58 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.208 10.803  13.126 1.00 17.42 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.180 10.971  9.929  1.00 17.99 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.096 10.003  9.324  1.00 20.48 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.915 9.276   10.400 1.00 23.17 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.188 9.822   11.482 1.00 23.65 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.989 10.698  8.301  1.00 21.94 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.786 11.659  8.971  1.00 25.10 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.270 8.017   10.119 1.00 24.54 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.053 7.191   11.037 1.00 27.17 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.326 6.695   10.330 1.00 30.66 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.338 6.537   9.102  1.00 31.22 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.249 5.939   11.462 1.00 28.80 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.056 5.108   10.318 1.00 31.27 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.900 6.287   12.055 1.00 27.61 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.333 6.335   11.113 1.00 32.61 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.552 5.741   10.569 1.00 35.01 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.396 4.213   10.455 1.00 36.73 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.970 3.600   9.543  1.00 38.48 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.777 6.144   11.410 1.00 38.07 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.488 5.987   12.803 1.00 39.41 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.217 7.558   11.142 1.00 39.72 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.674 3.585   11.398 1.00 35.71 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.471 2.141   11.354 1.00 36.17 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.250 1.798   10.512 1.00 35.61 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.272 2.552   10.494 1.00 34.57 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.323 1.581   12.758 1.00 36.89 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.303 0.675   9.797  1.00 35.54 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.198 0.256   8.942  1.00 35.51 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.046 -0.393  9.717  1.00 33.64 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.237 -1.347  10.468 1.00 34.46 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.699 -0.689  7.835  1.00 38.95 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.716 -0.820  6.672  1.00 45.13 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.271 -0.165  5.431  1.00 51.40 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.430 -0.378  5.060  1.00 53.51 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.457 0.638   4.752  1.00 52.33 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.850 0.111   9.497  1.00 30.76 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.648 -0.423  10.121 1.00 29.85 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.064 -1.541  9.287  1.00 28.99 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.229 -1.549  8.059  1.00 29.43 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.354 -2.474  9.937  1.00 27.52 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.782 -3.578  9.178  1.00 28.41 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.308 -3.830  9.485  1.00 25.34 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.852 -4.963  9.322  1.00 25.72 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.619 -4.854  9.270  1.00 33.35 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.402 -5.138  10.881 1.00 42.75 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.539 -2.769  9.847  1.00 22.06 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.086 -2.922  9.963  1.00 21.46 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.545 -2.921  8.504  1.00 21.34 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.190 -2.373  7.588  1.00 23.24 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.430 -1.745  10.741 1.00 22.54 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.541 -1.775  12.259 1.00 30.02 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.548 -2.877  12.826 1.00 32.33 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.580 -0.677  12.892 1.00 28.82 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.392 -3.516  8.290  1.00 20.47 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.728 -3.587  6.983  1.00 20.29 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.474 -2.696  7.029  1.00 18.54 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.654 -2.885  7.921  1.00 19.12 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.278 -5.031  6.735  1.00 23.32 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.459 -5.850  6.625  1.00 24.67 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.464 -5.157  5.442  1.00 24.99 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.315 -1.761  6.077  1.00 17.32 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.126 -0.906  6.045  1.00 16.54 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.065 -1.598  5.203  1.00 16.58 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.376 -2.052  4.072  1.00 17.51 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.460 0.477   5.446  1.00 16.08 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.669 1.147   6.138  1.00 17.80 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.244 1.408   5.466  1.00 16.26 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.477 1.349   7.665  1.00 18.28 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.832 -1.654  5.681  1.00 15.69 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.710 -2.208  4.917  1.00 15.59 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.363 -1.279  3.737  1.00 15.94 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.416 -0.041  3.870  1.00 15.48 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.474 -2.308  5.835  1.00 14.94 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 14.981 -1.888  2.581  1.00 16.83 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.550 -1.126  1.398  1.00 17.59 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.221 -1.822  1.063  1.00 18.63 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.183 -2.805  0.312  1.00 19.51 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.582 -1.241  0.282  1.00 18.43 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.979 -0.730  0.712  1.00 18.61 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.020 0.778   1.090  1.00 18.88 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.401 1.172   1.412  1.00 18.70 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.730 2.307   2.029  1.00 20.23 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.789 3.180   2.380  1.00 17.72 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.999 2.574   2.310  1.00 21.09 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.142 -1.268  1.588  1.00 17.71 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.830 -1.955  1.556  1.00 17.29 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.712  -1.009  1.998  1.00 17.61 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.975  0.089   2.474  1.00 18.08 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.881 -3.159  2.518  1.00 17.48 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 10.966 -2.680  4.272  1.00 17.13 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.454  -1.519  2.002  1.00 18.85 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.333  -0.776  2.550  1.00 19.80 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.660  -1.588  3.664  1.00 20.11 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.457  -1.477  3.853  1.00 21.42 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.298  -0.337  1.499  1.00 24.80 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.590  -1.456  0.799  1.00 32.58 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.897  -2.645  1.094  1.00 32.75 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.710  -1.159  -0.055 1.00 38.16 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.436  -2.357  4.450  1.00 18.77 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.869  -3.086  5.602  1.00 16.96 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.133  -2.134  6.556  1.00 16.74 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.539  -0.975  6.748  1.00 16.98 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 7.952  -3.841  6.378  1.00 17.63 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.572  -5.346  5.566  1.00 19.61 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.078  -2.649  7.164  1.00 15.82 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.371  -1.943  8.221  1.00 15.30 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.315  -2.804  9.474  1.00 14.39 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.520  -2.522  10.349 1.00 14.79 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.938  -1.518  7.812  1.00 16.59 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.940  -0.301  6.892  1.00 20.58 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.522  0.192   6.624  1.00 23.66 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.935  -0.053  5.540  1.00 23.58 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.904  0.823   7.640  1.00 21.53 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.158  -3.859  9.592  1.00 14.19 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.278  -4.630  10.826 1.00 14.12 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.781  -4.846  11.077 1.00 13.79 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.577  -4.981  10.146 1.00 15.68 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.565  -6.014  10.775 1.00 17.46 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.186  -6.801  9.762  1.00 21.18 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.062  -5.924  10.476 1.00 18.70 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.141  -4.861  12.356 1.00 12.86 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.536  -5.082  12.737 1.00 13.29 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.648  -5.197  14.245 1.00 11.15 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.649  -5.452  14.925 1.00 12.67 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.876  -5.065  14.742 1.00 10.79 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.180 -5.212  16.181 1.00 11.45 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.085 -4.050  16.585 1.00 11.77 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.058 -3.736  15.873 1.00 12.12 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.915 -6.551  16.410 1.00 12.88 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.399 -6.693  17.873 1.00 14.46 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.984  -7.717  16.040 1.00 13.16 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.765 -3.398  17.725 1.00 10.22 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.661 -2.340  18.219 1.00 10.10 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.190 -2.598  19.591 1.00 11.28 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.582 -3.352  20.366 1.00 11.45 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.012 -0.920  18.173 1.00 10.59 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.057 -0.582  19.308 1.00 10.59 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.790  -1.157  19.375 1.00 11.76 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.446 0.254   20.354 1.00 10.93 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.880  -0.800  20.376 1.00 13.36 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.544  0.621   21.365 1.00 12.56 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.281  0.038   21.405 1.00 12.90 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.387  0.322   22.421 1.00 13.56 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.356 -2.027  19.877 1.00 10.63 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.972 -2.144  21.199 1.00 11.70 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.521 -0.971  22.077 1.00 12.16 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.693 0.189   21.694 1.00 12.09 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.527 -2.249  21.164 1.00 12.35 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.086 -2.393  22.563 1.00 13.26 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.842 -3.535  23.311 1.00 14.49 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.841 -1.383  23.138 1.00 15.07 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.325 -3.663  24.627 1.00 15.79 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.355 -1.506  24.435 1.00 15.55 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.075 -2.635  25.184 1.00 16.57 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.585 -2.733  26.476 1.00 19.77 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.012 -1.291  23.288 1.00 12.00 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.530 -0.297  24.258 1.00 12.60 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.431 -0.349  25.502 1.00 13.13 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.261 -1.237  26.354 1.00 14.05 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.079 -0.602  24.630 1.00 12.93 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.373 0.521   25.883 1.00 15.05 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.374 0.612   25.622 1.00 14.12 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.308 0.569   26.733 1.00 15.03 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.648 0.731   28.111 1.00 15.65 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.114 0.100   29.083 1.00 17.39 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.429 1.580   26.553 1.00 19.86 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.950 2.901   26.672 1.00 24.97 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.527 1.496   28.190 1.00 15.08 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.820 1.670   29.474 1.00 15.05 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.060 0.432   29.935 1.00 14.96 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.539 0.456   31.051 1.00 16.15 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.891 2.888   29.454 1.00 14.88 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.853 2.725   28.496 1.00 16.48 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.043 -0.638  29.125 1.00 14.79 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.475 -1.915  29.543 1.00 14.50 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.518 -3.055  29.392 1.00 16.64 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.210 -4.218  29.723 1.00 17.76 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.229 -2.214  28.689 1.00 15.54 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.079  -1.232  28.917 1.00 17.67 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.379  -1.567  30.222 1.00 19.36 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.231  -0.675  30.426 1.00 20.76 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.291  0.487   31.073 1.00 20.34 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.447  0.920   31.580 1.00 20.36 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.187  1.205   31.264 1.00 21.73 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.757 -2.756  28.888 1.00 16.73 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.795 -3.771  28.527 1.00 17.60 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.140 -4.905  27.715 1.00 17.73 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.405 -6.101  27.941 1.00 20.14 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.525 -4.341  29.752 1.00 19.77 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.501 -3.336  30.361 1.00 23.86 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.288 -4.040  31.458 1.00 28.41 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.978 -3.104  32.347 1.00 31.70 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.763 -3.022  33.661 1.00 33.32 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.863 -3.808  34.246 1.00 32.65 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.414 -2.123  34.393 1.00 32.48 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.279 -4.523  26.751 1.00 15.99 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.559 -5.521  25.963 1.00 16.51 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.395 -5.094  24.532 1.00 14.45 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.378 -3.916  24.233 1.00 14.14 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.124 -5.732  26.514 1.00 20.06 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.047 -6.589  27.782 1.00 26.53 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.603  -6.735  28.256 1.00 32.23 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.501  -7.612  29.489 1.00 39.07 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.521 -7.242  30.513 1.00 43.82 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.204 -6.083  23.654 1.00 12.92 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.833 -5.841  22.276 1.00 12.40 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.334 -6.108  22.165 1.00 13.88 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.797  -7.061  22.765 1.00 16.49 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.599 -6.804  21.336 1.00 13.23 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.075 -6.552  21.290 1.00 14.52 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.677 -5.790  20.283 1.00 17.74 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.036 -6.999  22.125 1.00 14.51 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 15.983 -5.816  20.537 1.00 15.26 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.250 -6.485  21.635 1.00 17.60 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.643  -5.282  21.361 1.00 12.27 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.211  -5.469  21.149 1.00 12.19 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.868  -5.516  19.661 1.00 12.41 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.325  -4.677  18.869 1.00 12.39 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.437  -4.244  21.678 1.00 12.74 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.441  -4.110  23.183 1.00 13.54 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.604  -4.901  23.977 1.00 15.07 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.241  -3.175  23.817 1.00 15.06 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.593  -4.776  25.371 1.00 16.46 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.248  -3.049  25.216 1.00 15.78 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.431  -3.864  25.984 1.00 17.31 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.386  -3.645  27.352 1.00 20.29 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.034  -6.489  19.262 1.00 12.89 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.544  -6.529  17.866 1.00 13.31 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.436  -5.472  17.685 1.00 14.57 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.519  -5.405  18.530 1.00 16.87 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.944  -7.951  17.743 1.00 14.12 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.480  -8.234  19.157 1.00 14.65 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.457  -7.577  20.086 1.00 12.97 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.471  -4.709  16.602 1.00 14.27 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.453  -3.667  16.386 1.00 14.00 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.025  -3.576  14.931 1.00 13.66 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.805  -3.870  14.011 1.00 14.13 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.037  -2.269  16.772 1.00 15.43 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.095  -2.076  18.307 1.00 16.88 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.400  -2.014  16.127 1.00 16.15 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.784  -3.037  14.732 1.00 13.60 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.318  -2.595  13.432 1.00 13.97 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.549  -1.062  13.432 1.00 13.78 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.305  -0.416  14.466 1.00 14.85 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.823  -2.845  13.270 1.00 17.82 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.571  -4.231  13.146 1.00 24.65 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.057  -0.481  12.317 1.00 12.51 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.340  0.954   12.298 1.00 12.92 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.834  1.581   11.014 1.00 13.97 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.714  0.923   9.968  1.00 14.81 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.845  1.243   12.537 1.00 13.26 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.840  0.515   11.644 1.00 12.82 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.320  -0.741  11.986 1.00 13.65 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.265  1.079   10.448 1.00 13.20 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.207  -1.429  11.134 1.00 14.46 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.163  0.419   9.626  1.00 14.07 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.626  -0.845  9.969  1.00 13.74 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.524  2.879   11.106 1.00 13.97 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.029  3.602   9.968  1.00 14.78 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.160  3.921   8.931  1.00 14.80 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.337  3.837   9.255  1.00 15.60 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.323  4.880   10.422 1.00 17.34 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.220  5.767   11.072 1.00 18.56 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.808  4.233   7.646  1.00 16.37 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.830  4.615   6.668  1.00 17.58 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.386  6.007   7.039  1.00 17.94 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.711  6.819   7.677  1.00 18.68 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.298  4.590   5.212  1.00 20.57 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.947  3.185   4.735  1.00 24.77 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.340  3.199   3.318  1.00 30.31 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.088  1.790   2.825  1.00 35.28 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.761  1.767   1.374  1.00 39.80 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.606  6.306   6.599  1.00 16.84 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.222  7.610   6.963  1.00 16.99 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.365  8.791   6.515  1.00 16.79 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.915  8.854   5.339  1.00 17.44 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.579  7.588   6.261  1.00 18.57 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.904  6.110   6.088  1.00 19.20 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.542  5.446   5.856  1.00 17.39 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.120  9.716   7.459  1.00 15.01 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.241  10.826  7.147  1.00 18.03 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.560  12.065  8.021  1.00 18.09 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.487  12.024  8.866  1.00 16.81 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.784  10.369  7.245  1.00 23.27 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.435  10.161  8.595  1.00 29.81 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.861  13.182  7.757  1.00 18.12 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.044  14.442  8.463  1.00 18.93 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.085  14.418  9.656  1.00 19.93 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.848  14.404  9.484  1.00 20.74 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.667  15.590  7.491  1.00 19.47 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.115  16.988  7.856  1.00 22.21 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.590  17.119  7.851  1.00 21.50 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 3.538  18.004  6.871  1.00 23.33 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.652  14.382  10.879 1.00 18.63 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.859  14.247  12.088 1.00 19.98 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.160  15.360  13.077 1.00 20.35 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.333  15.696  13.277 1.00 17.82 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.189  12.870  12.709 1.00 21.25 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.723  11.726  11.782 1.00 23.58 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.626  12.715  14.128 1.00 22.41 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.095  10.412  12.230 1.00 26.37 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.117  15.914  13.735 1.00 21.38 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.343  16.955  14.735 1.00 23.28 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.963  16.374  16.019 1.00 22.70 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.509  15.367  16.545 1.00 24.79 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.036  17.710  15.045 1.00 25.17 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.275  19.066  15.682 1.00 27.70 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.817  20.107  14.949 1.00 30.28 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.045  19.263  17.030 1.00 29.40 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.090  21.333  15.547 1.00 32.10 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.274  20.504  17.615 1.00 30.44 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.768  21.536  16.868 1.00 31.72 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.066  16.962  16.471 1.00 20.44 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.787  16.519  17.645 1.00 19.30 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.773  17.644  18.672 1.00 20.55 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.259  18.757  18.393 1.00 20.79 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.238  16.066  17.271 1.00 18.82 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.027  15.659  18.522 1.00 19.52 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.204  14.916  16.277 1.00 18.83 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.320  17.326  19.879 1.00 20.70 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.256  18.337  20.959 1.00 22.21 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.636  18.888  21.294 1.00 22.71 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.641  18.221  21.066 1.00 22.30 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.684  17.699  22.241 1.00 25.89 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.224  17.328  22.139 1.00 32.43 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.344  18.488  21.741 1.00 44.02 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.661  18.385  20.696 1.00 46.24 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.381  19.527  22.441 1.00 48.42 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.691  20.110  21.844 1.00 22.82 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.945  20.724  22.261 1.00 21.92 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.657  19.875  23.304 1.00 22.35 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.994  19.190  24.117 1.00 23.10 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.675  22.103  22.872 1.00 22.88 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.004  19.948  23.276 1.00 21.78 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.899  19.321  24.247 1.00 23.23 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.004 20.353  24.559 1.00 25.82 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.991 21.476  24.036 1.00 26.98 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.523 18.052  23.642 1.00 23.26 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.387 18.373  22.550 1.00 23.03 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.012 19.961  25.332 1.00 27.15 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.181 20.808  25.580 1.00 28.82 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.024 20.991  24.314 1.00 27.55 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.819 21.921  24.247 1.00 28.49 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.093 20.192  26.666 1.00 34.03 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.975 18.683  26.811 1.00 40.26 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 12.813 18.286  27.704 1.00 50.03 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 11.781 17.818  27.166 1.00 51.63 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 12.921 18.471  28.938 1.00 54.24 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.875 20.092  23.305 1.00 24.92 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.703 20.142  22.100 1.00 23.33 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.080 20.840  20.897 1.00 21.29 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.806 21.297  20.033 1.00 22.23 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.137 18.730  21.700 1.00 22.86 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.747 17.949  22.847 1.00 23.67 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.091 18.085  23.173 1.00 25.64 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.997 17.037  23.562 1.00 24.90 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.658 17.343  24.213 1.00 26.71 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.551 16.279  24.585 1.00 25.92 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.880 16.440  24.915 1.00 28.00 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.403 15.650  25.922 1.00 29.73 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.739 20.939  20.845 1.00 19.42 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.075 21.570  19.724 1.00 19.18 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.790 22.217  20.209 1.00 20.43 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.092 21.644  21.062 1.00 21.30 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.654 20.520  18.657 1.00 17.99 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.742 19.664  18.050 1.00 17.05 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.488 20.115  16.966 1.00 17.40 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.987 18.384  18.522 1.00 15.85 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.467 19.316  16.380 1.00 16.59 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.927 17.555  17.911 1.00 14.57 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.660 18.026  16.837 1.00 15.02 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.636 17.195  16.280 1.00 14.12 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.362 23.305  19.557 1.00 21.66 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.993  23.785  19.803 1.00 21.76 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.988  22.777  19.180 1.00 21.80 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.396  21.850  18.435 1.00 22.95 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.957  25.123  19.059 1.00 22.82 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.966  24.994  17.946 1.00 23.60 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.035 24.048  18.461 1.00 21.70 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.673  22.966  19.399 1.00 21.32 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.664  22.110  18.766 1.00 21.35 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.743  22.325  17.247 1.00 22.00 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.861  23.466  16.773 1.00 23.81 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.264  22.455  19.285 1.00 21.16 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.791  21.232  16.487 1.00 20.74 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.985  21.316  15.057 1.00 20.67 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.526  20.056  14.346 1.00 20.94 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.234  19.041  15.005 1.00 21.67 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.487  21.572  14.800 1.00 19.39 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.314  20.255  14.808 1.00 19.11 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.698  20.403  15.323 1.00 18.23 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.610 19.368  14.816 1.00 17.65 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.733 18.152  15.342 1.00 18.50 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.663 17.315  14.884 1.00 15.85 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.939  17.766  16.344 1.00 19.36 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.497  20.093  13.003 1.00 20.32 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.274  18.869  12.246 1.00 20.31 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.641  18.225  12.001 1.00 18.13 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.557  18.884  11.470 1.00 19.19 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.587  19.158  10.901 1.00 21.50 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.129  19.522  11.055 1.00 24.44 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.153  18.540  11.139 1.00 25.70 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.735  20.843  11.192 1.00 26.91 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.810  18.866  11.300 1.00 28.57 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.394  21.182  11.368 1.00 28.66 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.439  20.186  11.435 1.00 30.34 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.892 20.517  11.572 1.00 34.41 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.754  16.931  12.358 1.00 15.80 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.974  16.148  12.082 1.00 14.25 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.639  15.300  10.851 1.00 15.08 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.587  14.626  10.811 1.00 16.07 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.364  15.277  13.290 1.00 14.35 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.575  14.370  12.973 1.00 13.75 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.258 13.848  14.217 1.00 13.17 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.413 14.568  15.229 1.00 14.80 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.749 12.588  14.138 1.00 13.08 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.529  15.318  9.847  1.00 13.68 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.297  14.563  8.632  1.00 13.40 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.945  13.157  8.709  1.00 13.92 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.799  12.908  9.570  1.00 13.89 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.875  15.331  7.440  1.00 13.91 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.279 15.456  7.570  1.00 15.56 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.508  12.253  7.800  1.00 14.08 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.071  10.893  7.706  1.00 13.67 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.922  10.099  9.021  1.00 13.51 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.770  9.265   9.312  1.00 13.20 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.544 10.948  7.214  1.00 14.23 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.704 11.600  5.865  1.00 14.34 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.696 10.847  4.683  1.00 16.99 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.774 12.919  5.534  1.00 16.37 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.794 11.735  3.691  1.00 18.22 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.853 12.983  4.155  1.00 17.86 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.850  10.368  9.771  1.00 12.86 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.615  9.731   11.064 1.00 13.01 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.548  8.630   10.928 1.00 13.47 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.519  8.790   10.230 1.00 14.60 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.134  10.820  12.056 1.00 13.43 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.984  10.376  13.528 1.00 14.72 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.314  9.956   14.117 1.00 15.89 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.427  11.553  14.358 1.00 17.14 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.786  7.524   11.638 1.00 12.42 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.851  6.369   11.642 1.00 12.06 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.393  6.144   13.070 1.00 13.11 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.239  6.135   13.976 1.00 14.19 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.658  5.133   11.163 1.00 13.33 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.165  5.305   9.689  1.00 16.13 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.244  3.957   9.219  1.00 17.16 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.683  4.267   10.325 1.00 15.85 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.082  5.909   13.290 1.00 13.56 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.630  5.671   14.668 1.00 13.84 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.158  4.237   14.872 1.00 12.31 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.658  3.591   13.950 1.00 13.64 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.416  6.577   15.094 1.00 16.56 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.589  8.070   15.045 1.00 19.96 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.329  8.791   15.595 1.00 21.36 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.861  8.520   15.751 1.00 21.09 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.292  3.797   16.086 1.00 11.41 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.756  2.517   16.532 1.00 12.25 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.230  2.664   17.971 1.00 13.74 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.499  3.649   18.648 1.00 13.79 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.873  1.456   16.513 1.00 12.84 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.406  1.715   18.405 1.00 14.11 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.909  1.660   19.761 1.00 14.17 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.971  0.921   20.576 1.00 15.09 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.299  -0.255  20.307 1.00 15.84 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.463 0.956   19.817 1.00 15.24 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.936 0.795   21.265 1.00 15.96 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.494 1.750   18.998 1.00 15.31 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.561  1.643   21.514 1.00 14.51 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.585  1.023   22.351 1.00 15.84 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.189  1.992   23.321 1.00 16.78 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.867  3.180   23.293 1.00 18.65 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.109  1.494   24.162 1.00 15.92 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.737  2.349   25.160 1.00 15.53 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.002  3.055   24.698 1.00 14.72 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.869  2.407   24.104 1.00 14.25 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.068  1.488   26.399 1.00 15.70 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.556  2.334   27.526 1.00 17.61 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.710  3.227   28.163 1.00 18.94 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.804  2.445   28.057 1.00 18.49 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.462  3.833   29.088 1.00 19.65 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.736  3.405   29.034 1.00 19.83 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.147  4.347   24.987 1.00 14.36 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.321  5.110   24.618 1.00 14.42 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.438  6.288   25.573 1.00 17.20 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.475  7.045   25.717 1.00 20.04 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.119  5.655   23.199 1.00 16.29 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 9.188  6.492   22.772 1.00 20.50 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.611  6.424   26.211 1.00 15.62 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.012 7.549   27.076 1.00 16.31 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.189 8.253   26.397 1.00 17.84 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.809 7.698   25.490 1.00 17.87 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.440 7.005   28.466 1.00 19.10 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.283  6.341   29.192 1.00 22.44 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.619  5.772   30.568 1.00 23.59 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.367 6.434   31.316 1.00 28.71 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.155  4.663   30.891 1.00 24.25 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.516 9.520   26.745 1.00 18.80 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.571 10.241  25.995 1.00 18.18 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.921 9.498   25.834 1.00 17.72 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.533 9.493   24.742 1.00 17.68 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.709 11.561  26.770 1.00 19.95 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.363 11.774  27.341 1.00 20.73 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.850 10.396  27.727 1.00 18.84 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.349 8.790   26.877 1.00 16.94 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.599 8.041   26.829 1.00 16.85 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.550 6.818   25.924 1.00 16.52 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.578 6.182   25.674 1.00 17.30 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.339 6.455   25.469 1.00 14.82 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.206 5.360   24.508 1.00 13.14 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.598 5.779   23.083 1.00 13.00 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.742 4.906   22.194 1.00 13.19 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.777 4.803   24.448 1.00 13.24 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.442 4.049   25.729 1.00 14.93 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.313 3.327   26.220 1.00 15.81 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.309 4.211   26.246 1.00 15.92 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.800 7.110   22.834 1.00 13.34 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.192 7.546   21.485 1.00 13.28 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.496 6.878   21.076 1.00 12.98 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.412 6.751   21.912 1.00 14.14 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.307 9.061   21.415 1.00 12.99 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.715 9.907   21.414 1.00 14.52 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.536 6.396   19.838 1.00 11.12 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.718 5.705   19.365 1.00 11.76 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.539 4.205   19.256 1.00 12.59 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.315 3.538   18.568 1.00 13.43 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.539 3.660   19.933 1.00 12.38 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.243 2.236   19.802 1.00 11.22 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.853 1.889   18.364 1.00 11.76 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.089 2.634   17.734 1.00 12.10 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.388 0.785   17.868 1.00 11.13 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.111 0.405   16.479 1.00 10.69 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.809 -0.322  16.281 1.00 10.11 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.444 -1.188  17.105 1.00 11.40 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.310 -0.406  15.968 1.00 13.46 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.490 0.598   15.703 1.00 15.00 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 16.999 -1.189  14.673 1.00 15.83 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.847 -0.164  15.370 1.00 18.01 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.129 0.018   15.151 1.00 10.38 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 12.949 -0.710  14.648 1.00 10.66 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.465 -1.487  13.419 1.00 11.13 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.115 -0.890  12.541 1.00 11.71 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.874 0.304   14.206 1.00 10.93 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.699 -0.323  13.413 1.00 11.86 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.874  -1.269  14.292 1.00 12.29 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.800  0.740   12.792 1.00 13.51 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.236 -2.824  13.421 1.00 11.34 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.690 -3.712  12.350 1.00 12.83 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.553 -4.544  11.810 1.00 12.88 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.724 -5.032  12.561 1.00 13.04 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.701 -4.693  12.965 1.00 17.23 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.078 -4.169  13.204 1.00 26.56 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.967 -5.290  13.758 1.00 31.94 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.373 -4.871  13.768 1.00 39.22 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.211 -5.028  12.748 1.00 40.89 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.816 -5.650  11.641 1.00 39.60 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.467 -4.620  12.849 1.00 42.42 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.583 -4.767  10.510 1.00 14.47 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.669 -5.717  9.856  1.00 15.59 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.530 -6.902  9.322  1.00 18.25 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.761 -6.964  9.524  1.00 18.02 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 10.891 -5.022  8.738  1.00 15.75 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 11.939 -4.499  7.334  1.00 15.30 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 11.905 -7.821  8.557  1.00 20.68 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.639 -8.943  7.988  1.00 23.58 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.778 -8.508  7.017  1.00 24.00 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.764 -9.249  6.828  1.00 26.57 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.637 -9.878  7.262  1.00 26.94 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 10.803 -9.161  6.180  1.00 31.91 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 9.886  -10.111 5.429  1.00 38.57 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 8.673  -9.868  5.299  1.00 40.34 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.446 -11.213 4.916  1.00 38.55 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.700 -7.285  6.476  1.00 20.83 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.677 -6.759  5.509  1.00 20.08 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.844 -5.993  6.127  1.00 20.35 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.823 -5.695  5.425  1.00 22.87 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 13.957 -5.881  4.481  1.00 19.66 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.785 -6.563  3.815  1.00 20.86 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.466 -6.215  4.095  1.00 20.50 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.777 -7.484  2.817  1.00 23.88 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.709 -6.972  3.318  1.00 24.04 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.447 -7.769  2.550  1.00 25.87 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.725 -5.623  7.409  1.00 17.67 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.802 -4.871  8.039  1.00 16.34 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.286 -3.747  8.922  1.00 13.11 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.126 -3.737  9.315  1.00 14.51 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.126 -2.751  9.159  1.00 12.71 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.773 -1.566  9.981  1.00 12.76 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.815 -0.658  9.216  1.00 12.62 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.094 -0.241  8.061  1.00 13.31 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.050 -0.801  10.318 1.00 14.21 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.719 0.529   11.018 1.00 15.19 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.015 -1.681  11.151 1.00 15.59 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.707 -0.301  9.876  1.00 11.40 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.661 0.558   9.306  1.00 11.93 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.853 1.995   9.782  1.00 11.76 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.679 2.934   9.022  1.00 12.51 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.285 -0.002  9.754  1.00 12.84 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.144 0.920   9.328  1.00 13.38 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.080 -1.411  9.181  1.00 14.15 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.156 2.157   11.068 1.00 11.52 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.287 3.495   11.638 1.00 12.46 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.679 3.444   13.099 1.00 11.62 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.000 2.383   13.625 1.00 11.63 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.577 4.599   13.781 1.00 11.01 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.934 4.665   15.217 1.00 10.81 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.868 5.389   15.978 1.00 11.30 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.220 6.301   15.447 1.00 11.45 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.301 5.376   15.428 1.00 11.40 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.348 6.736   14.718 1.00 13.30 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.459 4.431   15.028 1.00 13.97 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.658 7.495   15.162 1.00 13.96 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.653 5.017   17.258 1.00 10.45 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.686 5.725   18.095 1.00 10.39 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.008 7.225   18.111 1.00 11.30 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.174 7.580   18.333 1.00 10.91 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.691 5.138   19.537 1.00 10.88 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.785 5.974   20.445 1.00 12.42 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.243 3.660   19.534 1.00 12.96 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.983 8.065   17.958 1.00 10.92 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.141 9.505   17.957 1.00 11.40 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.066 10.240  18.768 1.00 13.35 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.352 11.329  19.270 1.00 14.29 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.106 10.001  16.518 1.00 12.67 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.260 11.414  16.400 1.00 12.80 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.857  9.683   18.937 1.00 12.89 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.803  10.353  19.732 1.00 13.37 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.057  9.363   20.632 1.00 14.95 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.268  8.147   20.511 1.00 14.71 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.803  11.068  18.792 1.00 14.97 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.014  10.076  18.137 1.00 16.43 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.463  11.984  17.803 1.00 13.90 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.185  9.886   21.499 1.00 15.54 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.385  9.015   22.339 1.00 16.97 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.429  9.795   23.215 1.00 18.77 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.406  11.024  23.204 1.00 21.09 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.791  9.051   24.086 1.00 21.04 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.776  9.564   24.999 1.00 22.29 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.382  9.109   24.597 1.00 22.84 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.156  8.707   23.450 1.00 22.22 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.436  9.164   25.536 1.00 22.61 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.025  8.779   25.309 1.00 23.45 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.131 7.331   24.807 1.00 21.83 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.095 7.028   24.082 1.00 22.46 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.675 9.730   24.310 1.00 25.56 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -1.001 11.089  24.856 1.00 30.23 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.166 11.261  26.068 1.00 31.15 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.146 12.066  23.956 1.00 31.70 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.837  6.468   25.122 1.00 19.75 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.772  5.097   24.670 1.00 18.10 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.166  4.884   23.209 1.00 15.82 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.848  3.837   22.659 1.00 15.98 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.783  5.877   22.592 1.00 14.94 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.227  5.751   21.213 1.00 14.84 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.771  5.830   21.181 1.00 15.08 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.394  6.390   22.095 1.00 17.60 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.661  6.901   20.355 1.00 16.07 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.110  6.954   20.290 1.00 18.18 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.314 8.301   19.800 1.00 20.81 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.443 5.859   19.399 1.00 18.54 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.374  5.243   20.155 1.00 12.55 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.810  5.351   19.927 1.00 11.84 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.994  5.782   18.464 1.00 11.93 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.305  5.248   17.584 1.00 12.55 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.569  4.048   20.244 1.00 12.56 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.938  2.807   19.597 1.00 14.81 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.057  4.170   19.887 1.00 12.44 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.899  6.745   18.210 1.00 11.34 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.125  7.199   16.848 1.00 11.26 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.553  6.926   16.432 1.00 11.22 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.473  7.036   17.243 1.00 12.62 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.725  6.499   15.181 1.00 10.47 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.049 6.124   14.653 1.00 11.06 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.379 7.002   13.455 1.00 11.18 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.546  7.165   12.549 1.00 11.51 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.055 4.656   14.152 1.00 10.91 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.506  3.690   15.185 1.00 10.20 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.320 3.161   16.159 1.00 10.76 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.161  3.268   15.141 1.00 12.11 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.824  2.241   17.078 1.00 11.17 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.679  2.327   16.035 1.00 12.81 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.496  1.848   17.042 1.00 11.72 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.594 7.552   13.454 1.00 10.50 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.111 8.299   12.296 1.00 10.64 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.576 7.282   11.248 1.00 10.90 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.486 6.475   11.490 1.00 12.26 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.307 9.161   12.733 1.00 10.88 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.926 7.286   10.070 1.00 10.82 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.297 6.376   8.996  1.00 10.82 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.660 6.688   8.424  1.00 11.47 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.007 7.873   8.244  1.00 13.25 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.272 6.515   7.809  1.00 13.50 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.451 5.462   6.715  1.00 14.79 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.473 4.287   7.038  1.00 16.17 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.546 5.849   5.514  1.00 20.20 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.415 5.617   7.995  1.00 11.23 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.679 5.822   7.293  1.00 12.21 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.678 5.041   5.929  1.00 13.00 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.672 5.075   5.202  1.00 13.62 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.903 5.402   8.137  1.00 13.41 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.005 6.244   9.431  1.00 13.36 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.876 3.891   8.439  1.00 13.73 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.582 4.333   5.597  1.00 13.74 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.549 3.500   4.387  1.00 12.78 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.671 4.294   3.088  1.00 15.25 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.052 3.708   2.051  1.00 16.79 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.296 2.593   4.370  1.00 13.57 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.229 1.634   5.537  1.00 13.69 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.918 0.877   5.470  1.00 15.12 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.819 1.755   5.841  1.00 14.86 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.567  1.364   6.013  1.00 16.51 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.200  0.121   5.693  1.00 15.69 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.645  2.231   6.446  1.00 16.79 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.337 5.572   3.119  1.00 13.77 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.434 6.377   1.896  1.00 14.25 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.879 6.913   1.645  1.00 16.44 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.176 7.460   0.556  1.00 17.92 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.414 7.533   1.927  1.00 16.81 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.747 8.551   3.000  1.00 18.66 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.084 8.127   4.139  1.00 18.39 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.717 9.781   2.696  1.00 19.80 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.788 6.782   2.639  1.00 15.80 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.146 7.361   2.514  1.00 16.66 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.040 6.387   1.795  1.00 16.81 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.840 5.663   2.407  1.00 16.94 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.671 7.696   3.925  1.00 16.24 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.779 8.659   4.710  1.00 16.34 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.324 8.868   6.153  1.00 15.94 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.630 10.014  3.983  1.00 17.55 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.827 6.280   0.477  1.00 16.58 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.506 5.258   -0.306 1.00 17.87 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.016 5.421   -0.319 1.00 19.63 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.731 4.426   -0.486 1.00 20.70 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.977 5.202   -1.764 1.00 18.24 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.471 5.235   -1.950 1.00 18.96 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.131 5.041   -3.440 1.00 19.77 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.728 4.140   -1.139 1.00 19.44 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.499 6.661   -0.142 1.00 18.94 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.919 6.941   -0.141 1.00 19.59 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.667 6.351   1.058  1.00 20.73 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.893 6.290   1.016  1.00 21.74 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.133 8.438   -0.220 1.00 19.16 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.402 9.219   0.826  1.00 17.88 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.188 9.839   0.702  1.00 18.01 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.883 9.532   2.152  1.00 17.49 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.885 10.516  1.861  1.00 18.53 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.931 10.381  2.750  1.00 17.78 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.086 9.258   2.842  1.00 17.94 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.077 10.854  4.059  1.00 18.74 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.242 9.753   4.122  1.00 18.63 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.260 10.563  4.705  1.00 18.01 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.962 5.907   2.118  1.00 19.80 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.622 5.302   3.279  1.00 21.15 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.439 4.042   2.888  1.00 25.05 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.391 3.691   3.595  1.00 25.56 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.567 4.902   4.326  1.00 19.96 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.958 6.032   5.140  1.00 19.01 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.881 5.486   6.045  1.00 18.66 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.036 6.740   5.991  1.00 20.20 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.074 3.387   1.759  1.00 27.04 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.702 2.167   1.254  1.00 31.77 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.792 2.325   0.253  1.00 36.52 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.279 1.297   -0.229 1.00 38.11 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.647 1.312   0.576  1.00 34.86 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.813 0.598   1.572  1.00 41.02 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.383 0.091   2.561  1.00 44.08 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.599 0.542   1.377  1.00 43.04 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.099 3.556   -0.162 1.00 38.40 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.133 3.835   -1.153 1.00 41.00 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.084 4.932   -0.664 1.00 42.97 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.838 5.504   -1.467 1.00 44.37 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.485 4.249   -2.478 1.00 44.14 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.721 5.557   -2.401 1.00 48.75 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.437 5.553   -3.205 1.00 56.13 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.050 6.628   -3.721 1.00 57.34 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.816 4.471   -3.313 1.00 57.64 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BTD B 2 .   ? 11.495 13.948  17.848 1.00 14.74 ? 201 A1BTD A N1  1 
HETATM 1079 C  C4  . A1BTD B 2 .   ? 10.373 10.077  23.113 1.00 17.46 ? 201 A1BTD A C4  1 
HETATM 1080 C  C5  . A1BTD B 2 .   ? 10.508 11.447  22.947 1.00 17.81 ? 201 A1BTD A C5  1 
HETATM 1081 C  C6  . A1BTD B 2 .   ? 9.698  12.335  23.661 1.00 18.08 ? 201 A1BTD A C6  1 
HETATM 1082 C  C7  . A1BTD B 2 .   ? 9.810  13.836  23.515 1.00 18.32 ? 201 A1BTD A C7  1 
HETATM 1083 C  C8  . A1BTD B 2 .   ? 10.201 14.144  21.010 1.00 17.14 ? 201 A1BTD A C8  1 
HETATM 1084 C  C10 . A1BTD B 2 .   ? 11.262 14.828  18.817 1.00 16.16 ? 201 A1BTD A C10 1 
HETATM 1085 O  O2  . A1BTD B 2 .   ? 12.429 15.113  23.563 1.00 19.48 ? 201 A1BTD A O2  1 
HETATM 1086 C  C12 . A1BTD B 2 .   ? 11.862 14.866  22.506 1.00 18.07 ? 201 A1BTD A C12 1 
HETATM 1087 C  C11 . A1BTD B 2 .   ? 12.302 15.277  21.127 1.00 18.10 ? 201 A1BTD A C11 1 
HETATM 1088 C  C9  . A1BTD B 2 .   ? 11.509 14.327  20.233 1.00 17.02 ? 201 A1BTD A C9  1 
HETATM 1089 O  O1  . A1BTD B 2 .   ? 10.807 15.961  18.607 1.00 17.05 ? 201 A1BTD A O1  1 
HETATM 1090 N  N   . A1BTD B 2 .   ? 10.663 14.257  22.398 1.00 17.85 ? 201 A1BTD A N   1 
HETATM 1091 C  C1  . A1BTD B 2 .   ? 8.758  11.805  24.546 1.00 18.80 ? 201 A1BTD A C1  1 
HETATM 1092 O  O   . A1BTD B 2 .   ? 8.016  12.737  25.229 1.00 20.34 ? 201 A1BTD A O   1 
HETATM 1093 C  C   . A1BTD B 2 .   ? 6.978  12.256  26.101 1.00 20.67 ? 201 A1BTD A C   1 
HETATM 1094 C  C3  . A1BTD B 2 .   ? 9.440  9.575   23.993 1.00 17.49 ? 201 A1BTD A C3  1 
HETATM 1095 C  C2  . A1BTD B 2 .   ? 8.628  10.434  24.716 1.00 17.73 ? 201 A1BTD A C2  1 
HETATM 1096 ZN ZN  . ZN    C 3 .   ? 10.772 -4.721  5.374  1.00 17.21 2 202 ZN    A ZN  1 
HETATM 1097 S  S   . DMS   D 4 .   ? 19.664 -0.426  19.774 1.00 39.45 ? 203 DMS   A S   1 
HETATM 1098 O  O   . DMS   D 4 .   ? 18.270 -0.768  19.353 1.00 35.12 ? 203 DMS   A O   1 
HETATM 1099 C  C1  . DMS   D 4 .   ? 19.740 0.300   21.426 1.00 39.36 ? 203 DMS   A C1  1 
HETATM 1100 C  C2  . DMS   D 4 .   ? 20.367 0.990   18.844 1.00 39.01 ? 203 DMS   A C2  1 
HETATM 1101 O  O   . HOH   E 5 .   ? 12.745 6.746   30.815 1.00 26.10 ? 301 HOH   A O   1 
HETATM 1102 O  O   . HOH   E 5 .   ? 35.649 15.224  16.722 1.00 35.35 ? 302 HOH   A O   1 
HETATM 1103 O  O   . HOH   E 5 .   ? 2.636  8.011   9.869  1.00 32.87 ? 303 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 22.304 -1.650  4.022  1.00 26.15 ? 304 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 11.110 23.958  23.528 1.00 28.98 ? 305 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? -0.189 15.537  8.450  1.00 45.17 ? 306 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 10.197 -4.925  31.569 1.00 33.95 ? 307 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 12.046 15.450  26.197 1.00 34.61 ? 308 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 23.603 21.568  7.891  1.00 24.00 ? 309 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 8.083  -3.915  0.428  1.00 27.34 ? 310 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 9.859  17.754  20.489 1.00 20.09 ? 311 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 29.345 2.905   10.491 1.00 22.54 ? 312 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 30.713 9.649   13.691 1.00 33.17 ? 313 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 10.594 8.136   4.528  1.00 22.40 ? 314 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 8.153  19.189  18.340 1.00 20.44 ? 315 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 0.515  -0.376  16.457 1.00 14.48 ? 316 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 10.860 17.384  5.782  1.00 47.66 ? 317 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 20.180 8.601   18.954 1.00 15.34 ? 318 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 19.131 -0.687  27.312 1.00 28.97 ? 319 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 6.159  -5.507  28.873 1.00 28.79 ? 320 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 10.371 4.758   3.328  1.00 18.63 ? 321 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 3.190  21.552  22.635 1.00 35.67 ? 322 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 5.935  1.596   6.073  1.00 26.57 ? 323 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 0.958  -2.595  19.898 1.00 25.50 ? 324 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 3.625  -4.747  21.026 1.00 22.23 ? 325 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 30.172 10.689  19.572 1.00 31.65 ? 326 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 17.899 20.893  9.432  1.00 18.60 ? 327 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 8.844  2.563   2.751  1.00 22.03 ? 328 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 15.176 11.275  0.929  1.00 34.27 ? 329 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 26.190 3.554   19.798 1.00 34.91 ? 330 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 16.798 16.890  4.169  1.00 40.01 ? 331 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 17.866 2.190   23.072 1.00 19.81 ? 332 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 23.277 -0.315  16.003 1.00 31.37 ? 333 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 15.669 11.939  24.018 1.00 20.27 ? 334 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 4.464  7.251   3.129  1.00 45.12 ? 335 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 31.073 20.120  10.704 1.00 29.60 ? 336 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 11.485 1.997   33.354 1.00 17.97 ? 337 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 0.142  1.745   24.340 1.00 24.13 ? 338 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 6.362  8.662   27.688 1.00 37.76 ? 339 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 17.778 0.212   29.906 1.00 31.60 ? 340 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 3.038  3.590   27.434 1.00 27.64 ? 341 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 11.326 11.432  11.386 1.00 12.76 ? 342 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 21.743 18.722  17.776 1.00 33.94 ? 343 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 7.118  16.498  24.882 1.00 28.42 ? 344 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 14.924 2.237   23.164 1.00 13.29 ? 345 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 13.749 8.985   29.614 1.00 26.03 ? 346 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 17.943 18.588  17.080 1.00 15.08 ? 347 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 0.248  3.919   6.520  1.00 29.78 ? 348 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 8.324  -7.485  9.093  1.00 33.72 ? 349 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 12.251 21.106  13.140 1.00 23.79 ? 350 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 23.062 17.984  19.416 1.00 35.66 ? 351 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 6.387  13.043  21.486 1.00 21.90 ? 352 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 4.380  5.711   24.841 1.00 22.50 ? 353 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 18.493 4.124   26.026 1.00 33.38 ? 354 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 28.093 3.217   2.875  1.00 40.62 ? 355 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 7.074  15.648  22.186 1.00 22.26 ? 356 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 10.116 4.321   33.544 1.00 23.88 ? 357 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 13.157 10.352  9.355  1.00 12.79 ? 358 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 2.927  12.877  17.862 1.00 37.79 ? 359 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 9.695  20.783  11.522 1.00 45.36 ? 360 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 17.331 20.233  19.155 1.00 29.36 ? 361 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 3.815  -5.103  6.324  1.00 30.04 ? 362 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 6.978  3.591   32.685 1.00 27.45 ? 363 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 19.198 8.742   25.663 1.00 24.64 ? 364 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 20.792 18.774  21.666 1.00 36.15 ? 365 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 11.705 -7.925  12.804 1.00 29.17 ? 366 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 1.950  13.106  5.572  1.00 32.40 ? 367 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 31.140 20.169  16.878 1.00 27.12 ? 368 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 6.688  12.771  5.593  1.00 22.65 ? 369 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 5.304  25.890  18.282 1.00 32.94 ? 370 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 4.028  -2.173  21.670 1.00 22.42 ? 371 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 14.470 20.859  8.654  1.00 31.42 ? 372 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 14.484 14.367  3.693  1.00 26.94 ? 373 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 5.274  -1.452  24.032 1.00 18.11 ? 374 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 14.672 -4.331  17.131 1.00 25.51 ? 375 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 7.373  -8.214  24.045 1.00 34.58 ? 376 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 19.761 23.373  15.551 1.00 22.34 ? 377 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 23.795 2.083   19.456 1.00 28.17 ? 378 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 1.080  -2.986  17.173 1.00 22.35 ? 379 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 3.724  14.466  20.469 1.00 29.98 ? 380 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 31.257 2.216   12.667 1.00 27.08 ? 381 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 2.167  10.124  28.270 1.00 38.49 ? 382 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 21.568 -5.740  10.302 1.00 45.39 ? 383 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 15.634 -4.674  1.667  1.00 24.32 ? 384 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 18.970 12.811  2.177  1.00 40.06 ? 385 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 6.095  22.670  11.572 1.00 26.41 ? 386 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 28.473 -2.366  12.942 1.00 28.29 ? 387 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 0.012  12.151  21.161 1.00 36.43 ? 388 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? -0.609 -4.721  15.909 0.50 28.92 ? 389 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 4.756  -1.529  28.869 1.00 37.11 ? 390 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 22.562 18.727  5.980  1.00 24.35 ? 391 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 31.654 14.215  21.316 1.00 29.30 ? 392 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 17.513 -3.489  18.101 1.00 34.79 ? 393 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 6.323  -3.772  -1.764 1.00 41.25 ? 394 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 4.059  10.253  19.138 1.00 32.08 ? 395 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 26.197 -2.085  14.311 1.00 25.36 ? 396 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 28.539 16.191  23.227 1.00 42.36 ? 397 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 20.205 -6.883  15.367 1.00 49.49 ? 398 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 0.478  -3.152  9.743  1.00 43.68 ? 399 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 18.083 8.845   -1.559 1.00 29.15 ? 400 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 24.367 6.780   20.357 1.00 34.36 ? 401 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 31.599 18.282  8.854  1.00 38.29 ? 402 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 22.074 8.507   21.144 1.00 21.15 ? 403 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 11.272 19.887  5.534  1.00 57.11 ? 404 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 9.083  15.908  26.832 1.00 36.22 ? 405 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 7.076  -5.519  2.621  1.00 30.29 ? 406 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 17.792 10.712  0.278  1.00 35.52 ? 407 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 8.623  21.990  26.667 1.00 39.99 ? 408 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 28.339 0.585   2.655  1.00 50.27 ? 409 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 7.493  -5.358  31.246 1.00 35.62 ? 410 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 6.556  -8.822  13.930 1.00 39.11 ? 411 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 8.870  19.131  6.488  1.00 44.60 ? 412 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 2.005  13.556  22.408 1.00 37.05 ? 413 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 21.115 21.681  17.906 1.00 29.56 ? 414 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 2.018  1.416   26.532 1.00 30.91 ? 415 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 31.853 11.583  21.454 1.00 39.17 ? 416 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 30.400 -0.448  13.793 1.00 39.86 ? 417 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 3.937  -2.057  26.375 1.00 36.08 ? 418 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 14.004 14.656  27.942 1.00 39.02 ? 419 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 0.928  -1.545  23.823 1.00 37.76 ? 420 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 11.846 23.170  15.097 1.00 34.01 ? 421 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 19.427 -4.128  22.653 1.00 57.20 ? 422 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 32.818 21.377  15.034 1.00 34.75 ? 423 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 33.126 21.465  12.351 1.00 35.21 ? 424 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 0.015  11.916  18.427 1.00 60.59 ? 425 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 5.036  -8.384  23.115 1.00 31.18 ? 426 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 7.539  10.276  29.463 1.00 39.67 ? 427 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 9.865  24.612  13.973 1.00 35.80 ? 428 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 2.798  -5.570  25.700 1.00 51.70 ? 429 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 35.540 20.538  16.579 1.00 41.31 ? 430 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   ? 0.2765 0.2444 0.2376 -0.0081 -0.0525 -0.0093 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2581 0.2348 0.2405 -0.0070 -0.0564 -0.0071 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2467 0.2324 0.2434 -0.0038 -0.0520 -0.0046 7   SER   A C   
4    O O   . SER   A 1   ? 0.2702 0.2547 0.2596 -0.0030 -0.0484 -0.0041 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3122 0.2846 0.2966 -0.0107 -0.0692 -0.0038 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3814 0.3498 0.3598 -0.0118 -0.0747 0.0002  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2036 0.1970 0.2191 -0.0023 -0.0508 -0.0036 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1958 0.1951 0.2238 0.0000  -0.0451 -0.0021 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1905 0.1959 0.2310 0.0010  -0.0387 -0.0034 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1903 0.1964 0.2274 0.0004  -0.0369 -0.0056 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1775 0.1862 0.2326 0.0022  -0.0345 -0.0018 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1670 0.1793 0.2317 0.0023  -0.0271 -0.0030 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1607 0.1722 0.2282 0.0028  -0.0180 -0.0033 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1777 0.1870 0.2452 0.0038  -0.0184 -0.0020 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1857 0.2009 0.2698 0.0025  -0.0309 -0.0007 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1377 0.1496 0.2058 0.0016  -0.0097 -0.0051 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1553 0.1637 0.2245 0.0007  0.0005  -0.0063 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1612 0.1702 0.2501 0.0016  0.0061  -0.0054 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1592 0.1711 0.2533 0.0009  0.0055  -0.0052 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1616 0.1674 0.2136 -0.0030 0.0061  -0.0087 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1725 0.1793 0.2093 -0.0038 0.0008  -0.0088 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1886 0.1875 0.2373 -0.0053 0.0167  -0.0107 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1828 0.1894 0.2069 -0.0079 0.0030  -0.0092 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1686 0.1746 0.2705 0.0032  0.0128  -0.0046 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1890 0.1954 0.3129 0.0043  0.0203  -0.0035 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2069 0.2044 0.3249 0.0021  0.0363  -0.0071 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2209 0.2128 0.3372 0.0027  0.0412  -0.0079 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1702 0.1803 0.3198 0.0081  0.0149  0.0016  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1707 0.1871 0.3243 0.0086  -0.0012 0.0053  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1738 0.1956 0.3419 0.0081  -0.0055 0.0072  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1993 0.2150 0.3390 0.0085  -0.0118 0.0063  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1866 0.2117 0.3539 0.0070  -0.0204 0.0098  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2125 0.2308 0.3498 0.0075  -0.0257 0.0087  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2111 0.2337 0.3620 0.0065  -0.0303 0.0103  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2259 0.2487 0.3717 0.0044  -0.0440 0.0121  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2061 0.2006 0.3179 -0.0011 0.0444  -0.0094 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2317 0.2145 0.3319 -0.0050 0.0601  -0.0134 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2459 0.2270 0.3602 -0.0056 0.0708  -0.0134 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2479 0.2342 0.3629 -0.0066 0.0664  -0.0121 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2615 0.2391 0.3292 -0.0110 0.0586  -0.0162 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2677 0.2527 0.3289 -0.0122 0.0488  -0.0144 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2927 0.2559 0.3440 -0.0170 0.0738  -0.0203 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2450 0.2188 0.3736 -0.0045 0.0858  -0.0145 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2547 0.2262 0.4001 -0.0048 0.0985  -0.0143 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2409 0.2265 0.4145 -0.0008 0.0881  -0.0089 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2425 0.2372 0.4344 0.0036  0.0762  -0.0047 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2454 0.2323 0.4192 -0.0033 0.0905  -0.0087 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2434 0.2430 0.4416 -0.0007 0.0797  -0.0039 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2227 0.2285 0.4025 -0.0022 0.0624  -0.0034 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2224 0.2345 0.4119 -0.0025 0.0562  -0.0012 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2839 0.2821 0.4986 -0.0021 0.0925  -0.0031 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3734 0.3669 0.6146 0.0004  0.1098  -0.0025 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3876 0.3879 0.6583 0.0054  0.1059  0.0017  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4147 0.3955 0.6457 -0.0033 0.1298  -0.0065 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2001 0.2040 0.3554 -0.0030 0.0552  -0.0055 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1828 0.1913 0.3219 -0.0040 0.0413  -0.0052 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1667 0.1796 0.3040 -0.0012 0.0284  -0.0041 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1761 0.1864 0.3137 0.0003  0.0303  -0.0043 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1959 0.1975 0.3042 -0.0087 0.0448  -0.0081 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2192 0.2142 0.3216 -0.0130 0.0563  -0.0090 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2333 0.2325 0.3482 -0.0131 0.0555  -0.0069 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2497 0.2328 0.3338 -0.0177 0.0688  -0.0119 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2576 0.2498 0.3666 -0.0175 0.0669  -0.0073 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2729 0.2476 0.3482 -0.0227 0.0800  -0.0127 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2943 0.2739 0.3824 -0.0224 0.0791  -0.0101 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3501 0.3206 0.4286 -0.0277 0.0905  -0.0104 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1476 0.1656 0.2812 -0.0011 0.0159  -0.0030 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1451 0.1651 0.2707 0.0003  0.0037  -0.0024 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1547 0.1738 0.2585 -0.0016 0.0002  -0.0044 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1408 0.1611 0.2452 -0.0028 -0.0011 -0.0043 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1477 0.1727 0.2913 0.0015  -0.0075 0.0010  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1817 0.2063 0.3118 0.0012  -0.0205 0.0009  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2073 0.2344 0.3534 0.0010  -0.0325 0.0049  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2208 0.2453 0.3532 -0.0014 -0.0427 0.0037  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2225 0.2427 0.3406 -0.0024 -0.0518 0.0038  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2429 0.2620 0.3597 -0.0011 -0.0533 0.0059  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2204 0.2358 0.3248 -0.0052 -0.0589 0.0018  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1574 0.1741 0.2439 -0.0018 -0.0007 -0.0057 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1590 0.1755 0.2286 -0.0032 -0.0037 -0.0066 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1655 0.1828 0.2307 -0.0014 -0.0128 -0.0066 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1541 0.1701 0.2165 -0.0004 -0.0147 -0.0064 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1549 0.1682 0.2091 -0.0055 0.0017  -0.0075 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1543 0.1689 0.1961 -0.0070 -0.0016 -0.0068 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1677 0.1764 0.2223 -0.0083 0.0120  -0.0083 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1551 0.1728 0.2176 -0.0016 -0.0173 -0.0069 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1496 0.1650 0.2048 -0.0008 -0.0242 -0.0076 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1295 0.1438 0.1747 -0.0010 -0.0233 -0.0086 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1398 0.1560 0.1870 -0.0017 -0.0197 -0.0078 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1726 0.1870 0.2370 -0.0013 -0.0317 -0.0072 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2120 0.2280 0.2892 -0.0008 -0.0342 -0.0047 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1795 0.1954 0.2529 -0.0024 -0.0307 -0.0072 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1276 0.1381 0.1630 -0.0004 -0.0261 -0.0099 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1374 0.1458 0.1672 0.0000  -0.0242 -0.0107 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1473 0.1540 0.1837 -0.0007 -0.0261 -0.0115 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1522 0.1554 0.1901 -0.0019 -0.0316 -0.0126 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1601 0.1621 0.1779 0.0004  -0.0251 -0.0128 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1651 0.1684 0.1767 0.0009  -0.0228 -0.0118 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1684 0.1707 0.1774 0.0005  -0.0255 -0.0115 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1577 0.1641 0.1692 0.0017  -0.0180 -0.0105 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1373 0.1457 0.1773 -0.0004 -0.0226 -0.0103 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1386 0.1450 0.1854 -0.0012 -0.0239 -0.0108 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1485 0.1460 0.1885 -0.0018 -0.0272 -0.0144 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1534 0.1479 0.1975 -0.0039 -0.0317 -0.0155 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1570 0.1657 0.2080 -0.0007 -0.0198 -0.0081 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1480 0.1549 0.2073 -0.0017 -0.0204 -0.0079 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1431 0.1512 0.2054 -0.0009 -0.0169 -0.0044 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1533 0.1598 0.2238 -0.0020 -0.0167 -0.0033 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1810 0.1809 0.2535 -0.0015 -0.0169 -0.0054 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1933 0.1865 0.2586 -0.0003 -0.0167 -0.0095 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1721 0.1707 0.2527 -0.0027 -0.0165 -0.0039 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1534 0.1456 0.1821 -0.0008 -0.0249 -0.0163 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1741 0.1543 0.1918 -0.0025 -0.0264 -0.0205 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1989 0.1738 0.2084 -0.0058 -0.0346 -0.0219 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2258 0.1891 0.2241 -0.0091 -0.0379 -0.0253 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1871 0.1612 0.1955 -0.0006 -0.0191 -0.0222 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1805 0.1551 0.1799 0.0000  -0.0179 -0.0219 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1878 0.1730 0.1942 0.0020  -0.0157 -0.0181 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2186 0.1836 0.2017 -0.0021 -0.0194 -0.0247 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2052 0.1872 0.2010 0.0018  -0.0148 -0.0189 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2223 0.1922 0.2036 -0.0006 -0.0170 -0.0226 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1833 0.1656 0.1981 -0.0055 -0.0380 -0.0191 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1946 0.1739 0.2061 -0.0083 -0.0467 -0.0184 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1978 0.1845 0.2282 -0.0092 -0.0522 -0.0154 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2206 0.2068 0.2542 -0.0115 -0.0605 -0.0131 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2059 0.1868 0.2109 -0.0070 -0.0462 -0.0169 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2261 0.1994 0.2135 -0.0065 -0.0405 -0.0195 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2275 0.2023 0.2091 -0.0057 -0.0403 -0.0176 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2221 0.1801 0.1915 -0.0105 -0.0432 -0.0234 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1753 0.1686 0.2195 -0.0078 -0.0474 -0.0145 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1815 0.1813 0.2449 -0.0087 -0.0503 -0.0116 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1807 0.1755 0.2471 -0.0129 -0.0604 -0.0115 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2050 0.1907 0.2598 -0.0155 -0.0627 -0.0147 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1751 0.1797 0.2481 -0.0074 -0.0429 -0.0110 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1833 0.1836 0.2666 -0.0140 -0.0662 -0.0075 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2007 0.1978 0.2906 -0.0190 -0.0782 -0.0058 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2146 0.2158 0.3232 -0.0204 -0.0773 -0.0049 24  THR   A C   
137  O O   . THR   A 18  ? 0.2042 0.2111 0.3213 -0.0172 -0.0670 -0.0050 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2180 0.2202 0.3219 -0.0194 -0.0861 -0.0001 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2286 0.2419 0.3584 -0.0160 -0.0791 0.0032  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2320 0.2305 0.3194 -0.0180 -0.0867 -0.0002 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2302 0.2281 0.3455 -0.0259 -0.0887 -0.0034 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2366 0.2392 0.3728 -0.0276 -0.0884 -0.0017 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2118 0.2274 0.3757 -0.0237 -0.0811 0.0030  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2277 0.2470 0.4019 -0.0224 -0.0721 0.0028  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2876 0.2857 0.4298 -0.0351 -0.1039 0.0005  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4033 0.3853 0.5161 -0.0405 -0.1108 -0.0046 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4577 0.4309 0.5520 -0.0393 -0.1017 -0.0110 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4500 0.4220 0.5490 -0.0476 -0.1253 -0.0040 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4866 0.4441 0.5563 -0.0453 -0.1090 -0.0150 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4897 0.4452 0.5591 -0.0511 -0.1237 -0.0111 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1969 0.2180 0.3723 -0.0222 -0.0840 0.0073  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1910 0.2225 0.3931 -0.0184 -0.0749 0.0113  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1682 0.2000 0.3594 -0.0138 -0.0587 0.0077  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1661 0.2023 0.3720 -0.0124 -0.0480 0.0087  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2294 0.2645 0.4434 -0.0173 -0.0811 0.0164  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3330 0.3774 0.5781 -0.0136 -0.0715 0.0208  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3660 0.4165 0.6398 -0.0150 -0.0723 0.0251  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3644 0.4090 0.6050 -0.0092 -0.0613 0.0198  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1667 0.1930 0.3315 -0.0123 -0.0570 0.0038  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1617 0.1881 0.3154 -0.0093 -0.0440 0.0012  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1572 0.1828 0.3113 -0.0105 -0.0383 -0.0001 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1632 0.1911 0.3220 -0.0096 -0.0278 0.0005  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1685 0.1896 0.2963 -0.0081 -0.0443 -0.0021 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1969 0.2185 0.3220 -0.0065 -0.0462 -0.0009 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2036 0.2297 0.3432 -0.0048 -0.0408 0.0014  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1762 0.1927 0.2848 -0.0071 -0.0523 -0.0023 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1627 0.1836 0.3104 -0.0130 -0.0451 -0.0018 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1614 0.1808 0.3101 -0.0141 -0.0404 -0.0025 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1725 0.1971 0.3461 -0.0158 -0.0379 0.0008  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1724 0.1974 0.3486 -0.0159 -0.0295 0.0014  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1511 0.1623 0.2869 -0.0164 -0.0473 -0.0056 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1574 0.1631 0.2716 -0.0142 -0.0440 -0.0087 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1735 0.1739 0.2716 -0.0139 -0.0480 -0.0112 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1529 0.1586 0.2613 -0.0120 -0.0357 -0.0085 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1703 0.1677 0.2551 -0.0114 -0.0418 -0.0130 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1641 0.1653 0.2559 -0.0102 -0.0350 -0.0109 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1639 0.1724 0.2799 -0.0121 -0.0291 -0.0060 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1812 0.1819 0.2671 -0.0080 -0.0289 -0.0101 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1746 0.1819 0.2816 -0.0104 -0.0239 -0.0051 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1816 0.1857 0.2756 -0.0083 -0.0243 -0.0068 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1846 0.2131 0.3772 -0.0174 -0.0452 0.0037  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1826 0.2171 0.4032 -0.0188 -0.0421 0.0076  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1881 0.2271 0.4198 -0.0158 -0.0277 0.0093  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1845 0.2270 0.4369 -0.0166 -0.0202 0.0119  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1742 0.2122 0.4145 -0.0216 -0.0553 0.0114  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1724 0.2102 0.3900 -0.0128 -0.0233 0.0078  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1668 0.2055 0.3889 -0.0107 -0.0090 0.0082  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1640 0.1970 0.3573 -0.0102 -0.0020 0.0047  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1676 0.1988 0.3535 -0.0089 0.0055  0.0038  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1726 0.2146 0.4074 -0.0082 -0.0108 0.0103  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2167 0.2653 0.4845 -0.0091 -0.0175 0.0155  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2222 0.2742 0.5142 -0.0091 -0.0081 0.0182  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2169 0.2667 0.4857 -0.0105 -0.0340 0.0174  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1659 0.1958 0.3444 -0.0117 -0.0048 0.0033  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1711 0.1967 0.3255 -0.0116 -0.0008 0.0016  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1912 0.2139 0.3410 -0.0132 0.0125  0.0023  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2041 0.2260 0.3642 -0.0152 0.0192  0.0039  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1688 0.1918 0.3150 -0.0128 -0.0057 0.0013  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1788 0.1985 0.3049 -0.0129 -0.0028 0.0014  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1902 0.2097 0.3026 -0.0107 -0.0067 -0.0004 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1927 0.2096 0.3168 -0.0138 -0.0056 0.0023  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1804 0.1999 0.3123 -0.0132 0.0161  0.0010  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1991 0.2126 0.3180 -0.0164 0.0274  0.0012  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2074 0.2179 0.3047 -0.0187 0.0239  0.0024  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2407 0.2466 0.3301 -0.0225 0.0289  0.0045  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1990 0.2099 0.3135 -0.0158 0.0335  -0.0008 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2213 0.2228 0.3153 -0.0207 0.0441  -0.0014 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1924 0.2062 0.3325 -0.0134 0.0381  -0.0007 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1891 0.2019 0.2779 -0.0166 0.0154  0.0018  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1756 0.1870 0.2487 -0.0181 0.0116  0.0039  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1585 0.1737 0.2316 -0.0143 0.0028  0.0028  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1582 0.1751 0.2343 -0.0118 0.0004  0.0002  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1887 0.1953 0.2438 -0.0220 0.0164  0.0045  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2037 0.2103 0.2449 -0.0238 0.0106  0.0078  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2296 0.2339 0.2637 -0.0275 0.0090  0.0127  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1962 0.2055 0.2313 -0.0223 0.0056  0.0073  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2302 0.2365 0.2560 -0.0283 0.0026  0.0158  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2136 0.2231 0.2402 -0.0250 0.0010  0.0123  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1997 0.2113 0.2368 -0.0190 0.0043  0.0038  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2187 0.2310 0.2401 -0.0248 -0.0040 0.0137  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2139 0.2274 0.2434 -0.0188 -0.0001 0.0047  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2195 0.2338 0.2424 -0.0215 -0.0039 0.0095  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1496 0.1649 0.2199 -0.0139 -0.0013 0.0050  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1612 0.1781 0.2299 -0.0106 -0.0071 0.0038  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1518 0.1687 0.2148 -0.0113 -0.0086 0.0081  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1630 0.1786 0.2265 -0.0137 -0.0075 0.0122  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1734 0.1895 0.2513 -0.0083 -0.0111 0.0010  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1690 0.1832 0.2550 -0.0093 -0.0108 0.0025  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1842 0.1964 0.2686 -0.0085 -0.0117 0.0051  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2176 0.2284 0.3068 -0.0102 -0.0101 0.0082  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1754 0.1870 0.2553 -0.0062 -0.0133 0.0045  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1552 0.1738 0.2140 -0.0093 -0.0111 0.0081  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1572 0.1772 0.2155 -0.0093 -0.0129 0.0130  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1571 0.1773 0.2188 -0.0051 -0.0140 0.0110  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1470 0.1683 0.2038 -0.0041 -0.0142 0.0088  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1636 0.1849 0.2121 -0.0138 -0.0134 0.0172  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2186 0.2423 0.2692 -0.0149 -0.0171 0.0244  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2526 0.2780 0.3135 -0.0107 -0.0180 0.0254  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2256 0.2488 0.2675 -0.0205 -0.0192 0.0295  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1498 0.1674 0.2193 -0.0027 -0.0137 0.0113  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1571 0.1720 0.2287 0.0010  -0.0124 0.0086  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1660 0.1808 0.2372 0.0010  -0.0124 0.0085  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1564 0.1755 0.2294 0.0020  -0.0119 0.0128  36  SER   A C   
244  O O   . SER   A 30  ? 0.1674 0.1852 0.2375 0.0041  -0.0100 0.0098  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1738 0.1835 0.2538 0.0027  -0.0106 0.0088  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2093 0.2185 0.2884 0.0028  -0.0106 0.0079  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1967 0.2008 0.2766 0.0058  -0.0073 0.0051  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2665 0.2783 0.3550 0.0031  -0.0103 0.0151  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1447 0.1686 0.2219 -0.0002 -0.0141 0.0204  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1420 0.1711 0.2238 0.0000  -0.0152 0.0259  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1421 0.1736 0.2134 -0.0020 -0.0162 0.0235  37  SER   A C   
252  O O   . SER   A 31  ? 0.1630 0.1981 0.2384 -0.0011 -0.0161 0.0262  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1952 0.2284 0.2831 -0.0034 -0.0198 0.0357  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2740 0.3076 0.3488 -0.0095 -0.0233 0.0373  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1311 0.1603 0.1910 -0.0042 -0.0163 0.0187  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1404 0.1706 0.1907 -0.0058 -0.0165 0.0162  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1388 0.1655 0.1854 -0.0026 -0.0143 0.0092  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1346 0.1616 0.1744 -0.0033 -0.0142 0.0072  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1559 0.1847 0.1963 -0.0110 -0.0171 0.0164  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1617 0.1921 0.1995 -0.0163 -0.0205 0.0238  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1881 0.2136 0.2124 -0.0222 -0.0190 0.0228  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1758 0.1996 0.1902 -0.0241 -0.0174 0.0192  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1863 0.2048 0.1863 -0.0307 -0.0163 0.0194  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2101 0.2241 0.2017 -0.0367 -0.0170 0.0234  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1802 0.1964 0.1725 -0.0320 -0.0143 0.0158  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1319 0.1543 0.1815 0.0000  -0.0132 0.0056  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1291 0.1466 0.1731 0.0014  -0.0132 -0.0004 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1184 0.1368 0.1588 -0.0006 -0.0149 -0.0021 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1240 0.1402 0.1594 0.0000  -0.0159 -0.0050 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1346 0.1498 0.1735 0.0032  -0.0113 -0.0023 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1446 0.1527 0.1749 0.0036  -0.0124 -0.0077 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1613 0.1641 0.1918 0.0033  -0.0140 -0.0103 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1426 0.1495 0.1652 0.0036  -0.0124 -0.0089 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1208 0.1410 0.1643 -0.0029 -0.0145 -0.0001 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1169 0.1369 0.1598 -0.0044 -0.0137 -0.0017 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1275 0.1464 0.1788 -0.0048 -0.0135 -0.0025 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1376 0.1563 0.1927 -0.0055 -0.0131 -0.0005 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1329 0.1538 0.1700 -0.0079 -0.0109 0.0006  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1425 0.1642 0.1716 -0.0086 -0.0112 0.0009  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1551 0.1750 0.1756 -0.0137 -0.0086 0.0026  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1548 0.1752 0.1831 -0.0062 -0.0116 -0.0026 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1165 0.1351 0.1723 -0.0046 -0.0138 -0.0044 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1233 0.1421 0.1905 -0.0055 -0.0129 -0.0044 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1447 0.1641 0.2169 -0.0059 -0.0092 -0.0047 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1506 0.1700 0.2209 -0.0045 -0.0110 -0.0056 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1254 0.1427 0.1990 -0.0045 -0.0189 -0.0060 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1325 0.1508 0.2209 -0.0058 -0.0191 -0.0053 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1438 0.1587 0.2340 -0.0064 -0.0244 -0.0065 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1505 0.1709 0.2503 -0.0056 -0.0213 -0.0050 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1428 0.1619 0.2222 -0.0076 -0.0032 -0.0037 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1329 0.1514 0.2203 -0.0078 0.0030  -0.0041 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1368 0.1574 0.2444 -0.0075 0.0036  -0.0030 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1457 0.1662 0.2564 -0.0092 0.0051  -0.0020 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1503 0.1640 0.2262 -0.0113 0.0126  -0.0041 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1584 0.1691 0.2433 -0.0114 0.0220  -0.0052 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1702 0.1823 0.2276 -0.0125 0.0105  -0.0043 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1255 0.1486 0.2481 -0.0056 0.0015  -0.0025 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1265 0.1529 0.2729 -0.0055 0.0015  -0.0004 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1577 0.1838 0.3193 -0.0046 0.0118  0.0005  43  SER   A C   
300  O O   . SER   A 37  ? 0.1724 0.1953 0.3255 -0.0039 0.0168  -0.0009 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1357 0.1652 0.2910 -0.0048 -0.0118 0.0009  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1600 0.1893 0.3126 -0.0030 -0.0166 0.0012  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1563 0.1853 0.3419 -0.0048 0.0158  0.0029  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1821 0.2102 0.3861 -0.0036 0.0278  0.0039  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2057 0.2399 0.4347 -0.0005 0.0199  0.0079  44  SER   A C   
306  O O   . SER   A 38  ? 0.2073 0.2468 0.4447 -0.0007 0.0053  0.0106  44  SER   A O   
307  C CB  . SER   A 38  ? 0.1962 0.2234 0.4140 -0.0055 0.0393  0.0048  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2267 0.2612 0.4656 -0.0057 0.0297  0.0082  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2203 0.2524 0.4597 0.0018  0.0291  0.0084  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2431 0.2806 0.5086 0.0049  0.0223  0.0134  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2757 0.3143 0.5748 0.0069  0.0368  0.0164  45  THR   A C   
312  O O   . THR   A 39  ? 0.2872 0.3185 0.5805 0.0060  0.0550  0.0127  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2702 0.3036 0.5204 0.0068  0.0208  0.0121  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3067 0.3319 0.5496 0.0070  0.0388  0.0083  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2668 0.2981 0.4843 0.0051  0.0100  0.0088  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2866 0.3328 0.6196 0.0092  0.0293  0.0233  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3038 0.3519 0.6747 0.0120  0.0431  0.0273  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3267 0.3690 0.6998 0.0157  0.0526  0.0268  46  THR   A C   
319  O O   . THR   A 40  ? 0.3451 0.3821 0.7348 0.0176  0.0726  0.0260  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3248 0.3850 0.7366 0.0124  0.0299  0.0365  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3421 0.4065 0.7489 0.0119  0.0074  0.0405  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3426 0.4069 0.7598 0.0088  0.0279  0.0366  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3190 0.3611 0.6768 0.0166  0.0393  0.0275  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3265 0.3625 0.6852 0.0198  0.0473  0.0272  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3371 0.3608 0.6551 0.0176  0.0589  0.0180  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3351 0.3575 0.6211 0.0141  0.0523  0.0136  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3327 0.3736 0.6955 0.0213  0.0277  0.0332  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3387 0.3528 0.6587 0.0193  0.0762  0.0153  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3555 0.3565 0.6372 0.0160  0.0872  0.0069  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3404 0.3401 0.5976 0.0158  0.0749  0.0059  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3454 0.3465 0.6173 0.0194  0.0703  0.0099  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4006 0.3888 0.6907 0.0167  0.1118  0.0035  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4981 0.4705 0.7463 0.0107  0.1246  -0.0056 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5802 0.5457 0.8270 0.0071  0.1413  -0.0087 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5960 0.5615 0.8754 0.0100  0.1548  -0.0063 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6061 0.5656 0.8166 0.0007  0.1411  -0.0134 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3171 0.3136 0.5381 0.0116  0.0706  0.0009  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3143 0.3092 0.5106 0.0108  0.0609  -0.0006 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3139 0.2954 0.4920 0.0087  0.0749  -0.0059 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3253 0.2970 0.4959 0.0055  0.0910  -0.0104 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2991 0.2787 0.4677 0.0095  0.0690  -0.0057 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3210 0.2869 0.4718 0.0068  0.0817  -0.0108 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2928 0.2570 0.4131 0.0034  0.0727  -0.0131 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3039 0.2588 0.4146 0.0022  0.0785  -0.0155 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3771 0.3372 0.5527 0.0111  0.0920  -0.0089 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4799 0.4533 0.6910 0.0183  0.0760  0.0013  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2535 0.2257 0.3590 0.0015  0.0600  -0.0126 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2556 0.2262 0.3337 -0.0022 0.0536  -0.0147 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2655 0.2251 0.3202 -0.0092 0.0645  -0.0200 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2901 0.2459 0.3468 -0.0111 0.0735  -0.0216 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2680 0.2493 0.3393 -0.0020 0.0388  -0.0124 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3566 0.3454 0.4388 0.0024  0.0260  -0.0079 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3853 0.3714 0.4718 0.0043  0.0255  -0.0063 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3382 0.3344 0.4224 0.0033  0.0164  -0.0060 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2638 0.2177 0.2962 -0.0138 0.0633  -0.0222 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2740 0.2164 0.2805 -0.0222 0.0704  -0.0265 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2549 0.2048 0.2447 -0.0259 0.0580  -0.0246 52  THR   A C   
358  O O   . THR   A 46  ? 0.2603 0.2169 0.2492 -0.0242 0.0482  -0.0224 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3206 0.2505 0.3152 -0.0256 0.0770  -0.0298 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3343 0.2563 0.3467 -0.0218 0.0904  -0.0313 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3564 0.2731 0.3201 -0.0362 0.0819  -0.0338 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2442 0.1921 0.2218 -0.0311 0.0589  -0.0249 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2363 0.1910 0.2013 -0.0345 0.0475  -0.0220 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2484 0.1931 0.1885 -0.0437 0.0479  -0.0234 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2703 0.2000 0.1950 -0.0504 0.0583  -0.0271 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2294 0.1871 0.1946 -0.0358 0.0468  -0.0202 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2401 0.2059 0.2301 -0.0281 0.0475  -0.0191 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2319 0.1974 0.1885 -0.0385 0.0349  -0.0161 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2371 0.2154 0.2421 -0.0211 0.0363  -0.0164 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2366 0.1879 0.1718 -0.0449 0.0374  -0.0206 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2452 0.1888 0.1584 -0.0545 0.0349  -0.0206 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2561 0.1962 0.1534 -0.0627 0.0321  -0.0183 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2440 0.1939 0.1504 -0.0595 0.0267  -0.0146 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2316 0.1864 0.1495 -0.0529 0.0236  -0.0167 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2809 0.2057 0.1530 -0.0740 0.0352  -0.0203 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2990 0.2180 0.1515 -0.0839 0.0309  -0.0172 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3191 0.2341 0.1546 -0.0936 0.0220  -0.0149 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3437 0.2411 0.1567 -0.1028 0.0279  -0.0193 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3214 0.2219 0.1570 -0.0895 0.0450  -0.0223 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3147 0.2200 0.1724 -0.0792 0.0549  -0.0245 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3074 0.2287 0.1814 -0.0736 0.0461  -0.0188 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2976 0.2215 0.1914 -0.0655 0.0557  -0.0210 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3058 0.2435 0.2194 -0.0584 0.0503  -0.0175 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2693 0.2185 0.1853 -0.0578 0.0369  -0.0121 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3097 0.2494 0.2420 -0.0521 0.0583  -0.0193 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2987 0.2291 0.1451 -0.0921 0.0083  -0.0079 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2956 0.2266 0.1346 -0.0993 -0.0011 -0.0047 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2882 0.2374 0.1436 -0.0973 -0.0153 0.0046  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2846 0.2452 0.1571 -0.0892 -0.0167 0.0074  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2949 0.2263 0.1429 -0.0936 0.0041  -0.0093 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2724 0.2246 0.1537 -0.0776 0.0019  -0.0072 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3034 0.2558 0.1571 -0.1036 -0.0250 0.0091  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3025 0.2728 0.1770 -0.1006 -0.0366 0.0181  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2989 0.2772 0.1881 -0.0957 -0.0369 0.0178  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3083 0.2968 0.2088 -0.0981 -0.0463 0.0251  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3689 0.3391 0.2344 -0.1128 -0.0503 0.0274  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4779 0.4370 0.3230 -0.1264 -0.0556 0.0277  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4858 0.4360 0.3228 -0.1264 -0.0474 0.0200  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5512 0.5100 0.3886 -0.1379 -0.0689 0.0363  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2824 0.2570 0.1738 -0.0884 -0.0266 0.0102  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2526 0.2343 0.1574 -0.0832 -0.0262 0.0101  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2360 0.2351 0.1649 -0.0755 -0.0313 0.0164  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2338 0.2392 0.1723 -0.0694 -0.0311 0.0177  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2626 0.2385 0.1687 -0.0753 -0.0152 0.0024  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3025 0.2572 0.1853 -0.0833 -0.0065 -0.0052 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2188 0.2246 0.1575 -0.0759 -0.0346 0.0198  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.1999 0.2199 0.1616 -0.0681 -0.0360 0.0246  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1865 0.2068 0.1535 -0.0622 -0.0298 0.0211  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1830 0.2127 0.1662 -0.0579 -0.0298 0.0249  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2086 0.2387 0.1829 -0.0740 -0.0461 0.0346  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2578 0.2908 0.2335 -0.0769 -0.0528 0.0401  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.2866 0.3315 0.2810 -0.0814 -0.0633 0.0517  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.2892 0.3316 0.2752 -0.0933 -0.0738 0.0576  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2468 0.3039 0.2673 -0.0727 -0.0606 0.0555  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1919 0.2013 0.1459 -0.0620 -0.0237 0.0143  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1899 0.1985 0.1480 -0.0559 -0.0180 0.0114  60  THR   A CA  
417  C C   . THR   A 54  ? 0.1907 0.1911 0.1423 -0.0504 -0.0114 0.0049  60  THR   A C   
418  O O   . THR   A 54  ? 0.2209 0.2129 0.1618 -0.0538 -0.0094 0.0015  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2357 0.2395 0.1883 -0.0623 -0.0184 0.0115  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2932 0.2836 0.2278 -0.0691 -0.0167 0.0070  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2456 0.2579 0.2070 -0.0690 -0.0259 0.0189  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1759 0.1783 0.1345 -0.0423 -0.0080 0.0036  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1842 0.1803 0.1406 -0.0369 -0.0034 -0.0009 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1546 0.1525 0.1168 -0.0301 -0.0021 -0.0005 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1719 0.1730 0.1365 -0.0303 -0.0026 0.0020  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1505 0.1453 0.1144 -0.0247 -0.0005 -0.0028 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1584 0.1524 0.1243 -0.0193 -0.0006 -0.0023 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1601 0.1565 0.1305 -0.0146 -0.0026 -0.0029 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1638 0.1594 0.1372 -0.0142 -0.0022 -0.0046 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1799 0.1655 0.1439 -0.0187 0.0017  -0.0033 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2003 0.1838 0.1653 -0.0138 -0.0003 -0.0017 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1864 0.1683 0.1451 -0.0239 0.0038  -0.0030 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1399 0.1382 0.1102 -0.0117 -0.0040 -0.0018 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1374 0.1360 0.1101 -0.0081 -0.0065 -0.0026 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1558 0.1488 0.1239 -0.0057 -0.0088 -0.0021 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1614 0.1506 0.1230 -0.0063 -0.0077 -0.0008 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1411 0.1450 0.1165 -0.0075 -0.0064 -0.0024 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1425 0.1454 0.1144 -0.0064 -0.0043 -0.0015 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1567 0.1614 0.1289 -0.0084 -0.0011 0.0005  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1498 0.1483 0.1172 -0.0040 -0.0049 -0.0029 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1779 0.1812 0.1485 -0.0073 0.0032  0.0013  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1734 0.1684 0.1356 -0.0035 -0.0005 -0.0029 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1763 0.1736 0.1405 -0.0048 0.0042  -0.0008 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1874 0.1803 0.1474 -0.0043 0.0107  -0.0008 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1470 0.1387 0.1180 -0.0036 -0.0127 -0.0026 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1645 0.1501 0.1300 -0.0025 -0.0174 -0.0012 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1740 0.1573 0.1309 -0.0025 -0.0179 -0.0024 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1705 0.1570 0.1317 -0.0019 -0.0180 -0.0041 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1699 0.1547 0.1448 -0.0010 -0.0227 0.0001  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1859 0.1639 0.1540 -0.0012 -0.0299 0.0029  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2058 0.1778 0.1668 -0.0020 -0.0310 0.0058  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2096 0.1860 0.1769 -0.0016 -0.0363 0.0030  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2280 0.1922 0.1797 -0.0034 -0.0388 0.0093  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2214 0.1899 0.1795 -0.0034 -0.0447 0.0061  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2394 0.2016 0.1888 -0.0045 -0.0461 0.0094  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2869 0.2397 0.2244 -0.0074 -0.0556 0.0133  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1788 0.1545 0.1225 -0.0036 -0.0176 -0.0016 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1924 0.1620 0.1243 -0.0043 -0.0158 -0.0034 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2071 0.1660 0.1259 -0.0062 -0.0232 -0.0023 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2251 0.1764 0.1323 -0.0080 -0.0242 0.0000  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1993 0.1671 0.1250 -0.0051 -0.0076 -0.0034 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2349 0.1919 0.1450 -0.0061 -0.0013 -0.0062 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2197 0.1772 0.1395 -0.0066 -0.0291 -0.0033 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2385 0.1861 0.1466 -0.0096 -0.0386 -0.0013 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2600 0.1926 0.1421 -0.0135 -0.0365 -0.0025 66  SER   A C   
466  O O   . SER   A 60  ? 0.2898 0.2126 0.1583 -0.0169 -0.0438 0.0010  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2966 0.2458 0.2121 -0.0101 -0.0459 -0.0019 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3649 0.3107 0.2733 -0.0107 -0.0411 -0.0066 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2559 0.1858 0.1313 -0.0131 -0.0257 -0.0068 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2693 0.1831 0.1193 -0.0169 -0.0203 -0.0088 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2721 0.1823 0.1139 -0.0177 -0.0157 -0.0060 67  SER   A C   
472  O O   . SER   A 61  ? 0.3001 0.1951 0.1187 -0.0215 -0.0108 -0.0072 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2686 0.1797 0.1169 -0.0159 -0.0085 -0.0140 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2781 0.2024 0.1456 -0.0115 0.0007  -0.0136 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2606 0.1824 0.1191 -0.0149 -0.0170 -0.0025 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2603 0.1784 0.1121 -0.0160 -0.0143 0.0007  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2843 0.2049 0.1432 -0.0159 -0.0252 0.0061  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.3011 0.2182 0.1556 -0.0168 -0.0244 0.0096  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2650 0.1938 0.1315 -0.0132 -0.0035 0.0000  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2938 0.2203 0.1573 -0.0130 0.0084  -0.0037 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.3278 0.2389 0.1689 -0.0164 0.0158  -0.0037 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3461 0.2548 0.1877 -0.0156 0.0297  -0.0070 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3491 0.2463 0.1775 -0.0169 0.0341  -0.0114 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3580 0.2454 0.1702 -0.0199 0.0242  -0.0128 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3667 0.2609 0.1981 -0.0157 0.0488  -0.0140 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2790 0.2055 0.1510 -0.0146 -0.0347 0.0072  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2837 0.2147 0.1703 -0.0132 -0.0431 0.0124  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2792 0.2170 0.1774 -0.0107 -0.0359 0.0131  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3102 0.2451 0.2101 -0.0108 -0.0390 0.0177  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3197 0.2389 0.1926 -0.0170 -0.0542 0.0184  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3758 0.2893 0.2416 -0.0204 -0.0649 0.0189  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4406 0.3435 0.2955 -0.0249 -0.0783 0.0267  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4910 0.3837 0.3297 -0.0308 -0.0893 0.0273  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5284 0.4028 0.3347 -0.0381 -0.0936 0.0286  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5291 0.3943 0.3171 -0.0397 -0.0869 0.0295  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.5267 0.3906 0.3170 -0.0445 -0.1040 0.0286  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2515 0.1979 0.1579 -0.0089 -0.0270 0.0089  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2535 0.2052 0.1684 -0.0080 -0.0207 0.0092  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2188 0.1814 0.1489 -0.0064 -0.0167 0.0061  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2127 0.1793 0.1452 -0.0057 -0.0161 0.0034  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3038 0.2516 0.2070 -0.0100 -0.0126 0.0086  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3952 0.3310 0.2818 -0.0125 -0.0142 0.0124  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4717 0.4040 0.3488 -0.0143 -0.0041 0.0116  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5689 0.4879 0.4276 -0.0174 -0.0048 0.0155  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6383 0.5459 0.4806 -0.0196 -0.0141 0.0174  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1954 0.1614 0.1341 -0.0064 -0.0138 0.0065  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1828 0.1569 0.1313 -0.0067 -0.0097 0.0039  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2019 0.1781 0.1472 -0.0091 -0.0040 0.0039  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2385 0.2099 0.1780 -0.0105 -0.0021 0.0059  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1903 0.1642 0.1482 -0.0065 -0.0094 0.0040  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2038 0.1774 0.1706 -0.0039 -0.0138 0.0047  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2398 0.2184 0.2157 -0.0031 -0.0129 0.0023  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2044 0.1732 0.1737 -0.0023 -0.0194 0.0083  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2057 0.1830 0.1911 -0.0008 -0.0170 0.0043  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2380 0.2101 0.2207 -0.0002 -0.0219 0.0082  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1773 0.1609 0.1281 -0.0099 -0.0017 0.0025  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1744 0.1619 0.1270 -0.0125 0.0027  0.0037  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1724 0.1664 0.1328 -0.0156 0.0023  0.0035  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1693 0.1672 0.1340 -0.0151 0.0003  0.0023  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1800 0.1704 0.1336 -0.0112 0.0058  0.0038  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1970 0.1787 0.1388 -0.0099 0.0081  0.0037  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2200 0.1969 0.1557 -0.0115 0.0129  0.0055  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2201 0.1969 0.1552 -0.0080 0.0057  0.0017  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2461 0.2123 0.1669 -0.0114 0.0158  0.0053  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2381 0.2039 0.1577 -0.0084 0.0075  0.0014  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2621 0.2222 0.1735 -0.0102 0.0128  0.0031  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3104 0.2574 0.2032 -0.0115 0.0157  0.0025  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1783 0.1725 0.1391 -0.0196 0.0039  0.0049  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1806 0.1794 0.1458 -0.0245 0.0024  0.0052  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1903 0.1985 0.1646 -0.0254 0.0019  0.0083  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2174 0.2278 0.1957 -0.0244 0.0052  0.0106  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1933 0.1880 0.1553 -0.0292 0.0038  0.0062  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2011 0.1938 0.1618 -0.0265 0.0069  0.0081  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1824 0.1717 0.1388 -0.0208 0.0066  0.0067  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1836 0.1967 0.1620 -0.0273 -0.0014 0.0087  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1730 0.1955 0.1633 -0.0278 -0.0025 0.0129  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1665 0.1931 0.1593 -0.0345 -0.0083 0.0158  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1775 0.1988 0.1605 -0.0378 -0.0104 0.0131  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1896 0.2136 0.1830 -0.0221 -0.0016 0.0115  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2103 0.2301 0.2010 -0.0169 0.0038  0.0099  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2022 0.2225 0.1889 -0.0214 -0.0042 0.0080  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1580 0.1939 0.1650 -0.0367 -0.0105 0.0218  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1595 0.2005 0.1709 -0.0430 -0.0179 0.0265  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1522 0.1984 0.1729 -0.0378 -0.0181 0.0280  75  SER   A C   
545  O O   . SER   A 69  ? 0.1615 0.2106 0.1921 -0.0313 -0.0126 0.0281  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2006 0.2499 0.2266 -0.0481 -0.0215 0.0339  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2917 0.3358 0.3090 -0.0540 -0.0222 0.0328  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1381 0.1836 0.1538 -0.0410 -0.0233 0.0286  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1391 0.1886 0.1632 -0.0363 -0.0234 0.0299  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1490 0.2035 0.1782 -0.0426 -0.0319 0.0369  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1644 0.2155 0.1826 -0.0514 -0.0381 0.0385  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1498 0.1919 0.1623 -0.0315 -0.0195 0.0227  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1527 0.1863 0.1481 -0.0361 -0.0206 0.0185  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1690 0.1953 0.1542 -0.0365 -0.0171 0.0137  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1599 0.1918 0.1498 -0.0403 -0.0242 0.0196  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1869 0.2042 0.1583 -0.0406 -0.0160 0.0097  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1796 0.2018 0.1534 -0.0447 -0.0227 0.0152  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1806 0.1955 0.1460 -0.0447 -0.0181 0.0102  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1415 0.2027 0.1866 -0.0385 -0.0324 0.0414  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1476 0.2140 0.1999 -0.0439 -0.0413 0.0496  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1567 0.2153 0.1904 -0.0475 -0.0443 0.0467  77  SER   A C   
562  O O   . SER   A 71  ? 0.1733 0.2247 0.1950 -0.0435 -0.0382 0.0386  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1685 0.2440 0.2463 -0.0378 -0.0398 0.0559  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1857 0.2574 0.2620 -0.0298 -0.0327 0.0500  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1774 0.2366 0.2080 -0.0559 -0.0540 0.0537  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2015 0.2524 0.2142 -0.0596 -0.0554 0.0514  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2012 0.2551 0.2253 -0.0513 -0.0516 0.0512  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2003 0.2629 0.2465 -0.0454 -0.0511 0.0558  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2436 0.2920 0.2461 -0.0722 -0.0671 0.0593  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3048 0.3462 0.2901 -0.0821 -0.0704 0.0579  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3804 0.4179 0.3534 -0.0963 -0.0837 0.0665  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4538 0.4811 0.4055 -0.1072 -0.0863 0.0635  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5210 0.5393 0.4517 -0.1228 -0.0985 0.0699  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1948 0.2407 0.2045 -0.0512 -0.0485 0.0460  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1927 0.2406 0.2124 -0.0438 -0.0448 0.0452  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1819 0.2373 0.2186 -0.0445 -0.0518 0.0557  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.1923 0.2471 0.2233 -0.0534 -0.0609 0.0633  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2222 0.2601 0.2232 -0.0463 -0.0416 0.0395  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2388 0.2688 0.2221 -0.0509 -0.0387 0.0336  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2139 0.2479 0.1989 -0.0572 -0.0460 0.0397  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1507 0.2119 0.2076 -0.0357 -0.0475 0.0564  80  SER   A N   
582  C CA  . SER   A 74  ? 0.1795 0.2482 0.2574 -0.0352 -0.0528 0.0669  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1751 0.2444 0.2680 -0.0255 -0.0452 0.0645  80  SER   A C   
584  O O   . SER   A 74  ? 0.1634 0.2270 0.2482 -0.0202 -0.0371 0.0546  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2372 0.3148 0.3320 -0.0376 -0.0577 0.0752  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3151 0.3954 0.4221 -0.0298 -0.0484 0.0706  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1665 0.2414 0.2804 -0.0240 -0.0485 0.0739  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1720 0.2462 0.3011 -0.0157 -0.0414 0.0725  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1766 0.2550 0.3256 -0.0092 -0.0335 0.0724  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1770 0.2640 0.3473 -0.0102 -0.0370 0.0821  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1728 0.2506 0.3164 -0.0178 -0.0488 0.0841  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2050 0.2793 0.3596 -0.0111 -0.0429 0.0829  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2063 0.2715 0.3392 -0.0110 -0.0393 0.0731  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2119 0.2908 0.3838 -0.0135 -0.0514 0.0966  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1648 0.2364 0.3068 -0.0032 -0.0228 0.0616  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1775 0.2497 0.3321 0.0022  -0.0133 0.0596  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1829 0.2473 0.3430 0.0094  -0.0025 0.0541  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.1591 0.2153 0.3028 0.0101  -0.0012 0.0464  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2014 0.2699 0.3361 0.0006  -0.0109 0.0515  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2302 0.3051 0.3605 -0.0069 -0.0205 0.0570  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2153 0.2804 0.3557 0.0059  0.0008  0.0471  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2731 0.3439 0.3850 -0.0088 -0.0187 0.0499  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1878 0.2537 0.3710 0.0144  0.0061  0.0576  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2143 0.2698 0.4005 0.0206  0.0183  0.0514  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2190 0.2626 0.3810 0.0217  0.0266  0.0388  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2467 0.2913 0.4040 0.0208  0.0295  0.0372  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2262 0.2851 0.4452 0.0256  0.0271  0.0588  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2600 0.3076 0.4850 0.0312  0.0383  0.0545  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2913 0.3382 0.5209 0.0313  0.0329  0.0577  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2866 0.3218 0.5086 0.0354  0.0545  0.0463  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3170 0.3521 0.5506 0.0359  0.0432  0.0529  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3032 0.3254 0.5281 0.0396  0.0653  0.0415  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3168 0.3395 0.5490 0.0400  0.0596  0.0450  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.1995 0.2320 0.3451 0.0226  0.0289  0.0305  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.1973 0.2175 0.3185 0.0224  0.0341  0.0195  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2178 0.2238 0.3391 0.0262  0.0463  0.0137  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2207 0.2229 0.3462 0.0273  0.0458  0.0134  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.1990 0.2178 0.2985 0.0186  0.0242  0.0148  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2199 0.2259 0.2957 0.0179  0.0277  0.0048  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.1959 0.2258 0.2936 0.0146  0.0146  0.0196  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2258 0.2220 0.3388 0.0273  0.0573  0.0084  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2521 0.2310 0.3608 0.0298  0.0711  0.0016  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2703 0.2367 0.3561 0.0272  0.0668  -0.0065 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2695 0.2387 0.3390 0.0236  0.0554  -0.0086 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3069 0.2746 0.4025 0.0297  0.0832  -0.0038 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3779 0.3553 0.4989 0.0327  0.0912  0.0037  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5124 0.4934 0.6668 0.0378  0.0994  0.0103  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5251 0.5241 0.7075 0.0389  0.0923  0.0215  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5741 0.5391 0.7263 0.0401  0.1120  0.0046  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2764 0.2284 0.3622 0.0289  0.0763  -0.0111 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2766 0.2151 0.3412 0.0256  0.0726  -0.0190 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2966 0.2237 0.3289 0.0207  0.0700  -0.0269 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3111 0.2323 0.3342 0.0204  0.0780  -0.0289 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2934 0.2148 0.3612 0.0277  0.0862  -0.0235 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2957 0.2196 0.3124 0.0165  0.0587  -0.0305 87  SER   A N   
636  C CA  . SER   A 81  ? 0.3277 0.2400 0.3148 0.0110  0.0533  -0.0370 87  SER   A CA  
637  C C   . SER   A 81  ? 0.3687 0.2680 0.3442 0.0072  0.0492  -0.0426 87  SER   A C   
638  O O   . SER   A 81  ? 0.3786 0.2779 0.3687 0.0094  0.0520  -0.0416 87  SER   A O   
639  C CB  . SER   A 81  ? 0.3232 0.2509 0.3096 0.0095  0.0397  -0.0329 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.3125 0.2515 0.3110 0.0095  0.0296  -0.0295 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3972 0.2865 0.3481 0.0011  0.0409  -0.0473 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4251 0.3039 0.3659 -0.0037 0.0338  -0.0516 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3964 0.2928 0.3576 -0.0024 0.0228  -0.0462 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4101 0.3008 0.3715 -0.0050 0.0189  -0.0483 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.5050 0.3712 0.4166 -0.0114 0.0244  -0.0558 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5829 0.4577 0.4890 -0.0114 0.0195  -0.0524 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7155 0.5785 0.6071 -0.0110 0.0326  -0.0552 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7259 0.6013 0.6345 -0.0053 0.0401  -0.0510 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7859 0.6262 0.6488 -0.0171 0.0357  -0.0614 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3510 0.2676 0.3282 0.0010  0.0181  -0.0394 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3206 0.2521 0.3139 0.0015  0.0089  -0.0346 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2835 0.2257 0.2998 0.0061  0.0132  -0.0290 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2898 0.2386 0.3163 0.0056  0.0077  -0.0263 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3103 0.2546 0.3038 0.0010  0.0006  -0.0310 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3306 0.2655 0.3034 -0.0034 -0.0051 -0.0347 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3587 0.2896 0.3258 -0.0081 -0.0154 -0.0362 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3514 0.2825 0.3121 -0.0033 -0.0012 -0.0355 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3810 0.3037 0.3301 -0.0128 -0.0226 -0.0379 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3738 0.2962 0.3149 -0.0078 -0.0074 -0.0376 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.4036 0.3216 0.3388 -0.0127 -0.0187 -0.0385 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4343 0.3440 0.3512 -0.0176 -0.0265 -0.0391 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2564 0.1998 0.2817 0.0102  0.0228  -0.0265 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2422 0.1959 0.2906 0.0140  0.0253  -0.0196 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2575 0.2040 0.3147 0.0179  0.0383  -0.0195 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2732 0.2140 0.3222 0.0185  0.0453  -0.0222 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2178 0.1893 0.2763 0.0150  0.0200  -0.0120 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2053 0.1848 0.2576 0.0118  0.0097  -0.0113 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2050 0.1907 0.2653 0.0106  0.0042  -0.0080 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1940 0.1745 0.2337 0.0101  0.0065  -0.0136 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1940 0.1861 0.2503 0.0079  -0.0028 -0.0074 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1761 0.1639 0.2135 0.0078  -0.0013 -0.0125 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1771 0.1705 0.2231 0.0068  -0.0053 -0.0096 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1644 0.1633 0.2087 0.0045  -0.0107 -0.0090 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2658 0.2143 0.3429 0.0210  0.0420  -0.0148 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2624 0.2082 0.3560 0.0258  0.0546  -0.0121 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2526 0.2152 0.3604 0.0278  0.0526  -0.0037 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2642 0.2393 0.3683 0.0252  0.0414  -0.0002 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2691 0.2153 0.3827 0.0282  0.0557  -0.0072 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2754 0.2329 0.3886 0.0252  0.0418  -0.0033 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2604 0.2154 0.3487 0.0205  0.0348  -0.0103 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2402 0.2034 0.3663 0.0321  0.0633  0.0003  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2295 0.2092 0.3726 0.0333  0.0604  0.0094  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2270 0.2220 0.3868 0.0325  0.0482  0.0199  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2462 0.2396 0.4190 0.0341  0.0483  0.0233  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2206 0.1978 0.3854 0.0383  0.0750  0.0126  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2081 0.2159 0.3640 0.0292  0.0374  0.0244  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2007 0.2201 0.3647 0.0265  0.0255  0.0332  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2001 0.2321 0.3634 0.0229  0.0170  0.0391  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2122 0.2441 0.3670 0.0225  0.0199  0.0353  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.1924 0.2064 0.3378 0.0234  0.0197  0.0273  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.1957 0.2116 0.3186 0.0192  0.0134  0.0222  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.1936 0.2003 0.2987 0.0177  0.0126  0.0132  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.1893 0.2006 0.2807 0.0137  0.0048  0.0118  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2042 0.2156 0.2831 0.0124  0.0040  0.0080  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.1731 0.1874 0.2419 0.0093  -0.0018 0.0066  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2170 0.2248 0.2938 0.0144  0.0100  0.0056  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1870 0.2283 0.3568 0.0193  0.0064  0.0482  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.1862 0.2364 0.3489 0.0140  -0.0027 0.0524  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1687 0.2148 0.3052 0.0099  -0.0071 0.0448  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1850 0.2278 0.3162 0.0087  -0.0097 0.0441  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.1928 0.2528 0.3712 0.0104  -0.0127 0.0660  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2176 0.2847 0.4264 0.0137  -0.0101 0.0756  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2284 0.3034 0.4446 0.0120  -0.0118 0.0797  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2416 0.3071 0.4737 0.0189  -0.0048 0.0803  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2516 0.3341 0.4997 0.0152  -0.0089 0.0893  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2508 0.3230 0.5151 0.0227  -0.0010 0.0897  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2662 0.3474 0.5393 0.0209  -0.0029 0.0943  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3031 0.3922 0.6121 0.0245  0.0007  0.1047  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1439 0.1903 0.2661 0.0080  -0.0074 0.0400  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1324 0.1758 0.2331 0.0043  -0.0110 0.0340  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1422 0.1920 0.2388 -0.0020 -0.0191 0.0404  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1509 0.2064 0.2535 -0.0035 -0.0209 0.0449  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1399 0.1779 0.2275 0.0060  -0.0063 0.0250  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1388 0.1747 0.2088 0.0025  -0.0100 0.0201  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1376 0.1666 0.1960 0.0044  -0.0066 0.0118  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1606 0.1828 0.2189 0.0075  -0.0023 0.0077  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1402 0.1694 0.1875 0.0020  -0.0089 0.0094  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1288 0.1767 0.2143 -0.0065 -0.0236 0.0406  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1274 0.1778 0.2040 -0.0139 -0.0306 0.0458  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1413 0.1881 0.1995 -0.0167 -0.0292 0.0387  96  SER   A C   
721  O O   . SER   A 90  ? 0.1441 0.1868 0.1970 -0.0129 -0.0241 0.0306  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1361 0.1840 0.2084 -0.0181 -0.0346 0.0501  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1625 0.2041 0.2246 -0.0169 -0.0301 0.0423  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1462 0.1937 0.1950 -0.0238 -0.0343 0.0424  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1485 0.1910 0.1799 -0.0271 -0.0325 0.0363  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1453 0.1888 0.1790 -0.0221 -0.0278 0.0306  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1467 0.1852 0.1697 -0.0217 -0.0243 0.0239  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1622 0.1973 0.1811 -0.0283 -0.0288 0.0308  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.1667 0.1988 0.1792 -0.0346 -0.0325 0.0362  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2085 0.2343 0.2026 -0.0437 -0.0347 0.0378  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.1893 0.2226 0.2102 -0.0335 -0.0343 0.0410  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2262 0.2493 0.2166 -0.0482 -0.0381 0.0434  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2144 0.2424 0.2216 -0.0420 -0.0381 0.0458  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1306 0.1796 0.1786 -0.0185 -0.0274 0.0338  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1321 0.1808 0.1814 -0.0141 -0.0222 0.0290  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1366 0.1890 0.1863 -0.0181 -0.0247 0.0326  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1456 0.2042 0.2050 -0.0220 -0.0303 0.0409  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1320 0.1820 0.1965 -0.0076 -0.0175 0.0296  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1501 0.1965 0.2128 -0.0031 -0.0105 0.0239  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1727 0.2115 0.2197 -0.0021 -0.0091 0.0158  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1765 0.2218 0.2529 0.0023  -0.0042 0.0245  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1275 0.1765 0.1680 -0.0173 -0.0213 0.0270  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1222 0.1737 0.1622 -0.0210 -0.0228 0.0294  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1336 0.1851 0.1794 -0.0156 -0.0162 0.0268  99  MET   A C   
745  O O   . MET   A 93  ? 0.1519 0.1972 0.1899 -0.0114 -0.0116 0.0203  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1469 0.1915 0.1682 -0.0255 -0.0234 0.0245  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1867 0.2281 0.1981 -0.0321 -0.0280 0.0262  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2101 0.2408 0.2010 -0.0362 -0.0247 0.0192  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.1938 0.2215 0.1871 -0.0272 -0.0181 0.0120  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1330 0.1906 0.1917 -0.0164 -0.0158 0.0322  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1360 0.1916 0.1982 -0.0117 -0.0076 0.0295  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1186 0.1740 0.1751 -0.0152 -0.0076 0.0293  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1338 0.1933 0.1913 -0.0214 -0.0139 0.0337  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1607 0.2225 0.2461 -0.0082 -0.0028 0.0353  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2002 0.2621 0.2960 -0.0041 -0.0011 0.0365  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2081 0.2747 0.3289 -0.0001 0.0063  0.0419  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2232 0.2749 0.3031 -0.0004 0.0030  0.0276  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1114 0.1609 0.1612 -0.0117 -0.0007 0.0245  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1236 0.1721 0.1697 -0.0140 0.0013  0.0245  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1428 0.1875 0.1918 -0.0094 0.0114  0.0229  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1449 0.1852 0.1938 -0.0049 0.0167  0.0202  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1403 0.1810 0.1665 -0.0157 -0.0009 0.0189  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1464 0.1918 0.1977 -0.0113 0.0147  0.0248  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1494 0.1890 0.1998 -0.0081 0.0255  0.0231  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1732 0.2009 0.1991 -0.0076 0.0260  0.0166  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1862 0.2126 0.2031 -0.0109 0.0214  0.0161  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1557 0.2020 0.2215 -0.0107 0.0289  0.0290  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1689 0.2069 0.2308 -0.0079 0.0419  0.0267  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1429 0.2020 0.2368 -0.0113 0.0266  0.0371  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1725 0.1910 0.1879 -0.0041 0.0308  0.0120  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2006 0.2076 0.1936 -0.0042 0.0296  0.0071  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2202 0.2163 0.2012 -0.0016 0.0334  0.0026  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2404 0.2376 0.2306 0.0007  0.0378  0.0023  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2197 0.2048 0.1803 -0.0025 0.0309  -0.0008 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2241 0.1966 0.1693 -0.0018 0.0329  -0.0051 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2140 0.1872 0.1582 -0.0011 0.0242  -0.0073 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2063 0.1838 0.1512 -0.0018 0.0155  -0.0064 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2385 0.1973 0.1608 -0.0043 0.0333  -0.0064 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2745 0.2176 0.1771 -0.0054 0.0356  -0.0107 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2948 0.2299 0.1948 -0.0048 0.0482  -0.0132 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2944 0.2281 0.1801 -0.0075 0.0267  -0.0127 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.3166 0.2357 0.1943 -0.0072 0.0469  -0.0175 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.3218 0.2406 0.1911 -0.0091 0.0329  -0.0169 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2115 0.1797 0.1545 0.0002  0.0272  -0.0101 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2123 0.1806 0.1550 0.0005  0.0196  -0.0121 105 SER   A CA  
786  C C   . SER   A 99  ? 0.2560 0.2109 0.1869 0.0002  0.0246  -0.0166 105 SER   A C   
787  O O   . SER   A 99  ? 0.2903 0.2435 0.2278 0.0019  0.0349  -0.0172 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2241 0.2065 0.1883 0.0024  0.0178  -0.0094 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2768 0.2596 0.2426 0.0028  0.0118  -0.0111 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2446 0.1897 0.1591 -0.0024 0.0172  -0.0193 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2633 0.1935 0.1628 -0.0044 0.0190  -0.0240 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2781 0.2137 0.1860 -0.0042 0.0092  -0.0244 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2703 0.2181 0.1908 -0.0032 0.0013  -0.0212 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3140 0.2268 0.1849 -0.0095 0.0163  -0.0259 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3620 0.2677 0.2229 -0.0101 0.0274  -0.0257 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3934 0.2800 0.2229 -0.0160 0.0251  -0.0269 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.4699 0.3417 0.2794 -0.0206 0.0205  -0.0302 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.4038 0.2898 0.2279 -0.0168 0.0272  -0.0241 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2953 0.2215 0.1975 -0.0053 0.0106  -0.0283 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2816 0.2142 0.1951 -0.0050 0.0022  -0.0282 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2741 0.2113 0.1878 -0.0072 -0.0115 -0.0256 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2634 0.2133 0.1950 -0.0052 -0.0164 -0.0231 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3136 0.2303 0.2142 -0.0075 0.0059  -0.0335 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.3281 0.2363 0.2231 -0.0062 0.0207  -0.0358 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.3064 0.2157 0.1939 -0.0067 0.0218  -0.0333 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2739 0.2008 0.1691 -0.0112 -0.0171 -0.0255 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2704 0.2013 0.1688 -0.0130 -0.0300 -0.0219 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2560 0.2011 0.1705 -0.0095 -0.0307 -0.0176 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2614 0.2116 0.1844 -0.0098 -0.0394 -0.0142 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2311 0.1817 0.1501 -0.0067 -0.0212 -0.0174 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2013 0.1640 0.1341 -0.0043 -0.0211 -0.0140 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1889 0.1637 0.1412 -0.0020 -0.0217 -0.0132 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1853 0.1682 0.1475 -0.0010 -0.0222 -0.0108 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2022 0.1668 0.1341 -0.0031 -0.0120 -0.0134 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2338 0.1868 0.1468 -0.0055 -0.0109 -0.0133 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2486 0.1974 0.1547 -0.0075 -0.0190 -0.0113 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2504 0.1982 0.1562 -0.0056 -0.0017 -0.0146 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1918 0.1666 0.1485 -0.0017 -0.0211 -0.0152 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1821 0.1672 0.1554 -0.0001 -0.0214 -0.0140 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1744 0.1632 0.1555 -0.0006 -0.0279 -0.0122 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1923 0.1757 0.1693 -0.0023 -0.0348 -0.0119 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1782 0.1611 0.1543 0.0000  -0.0204 -0.0161 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1977 0.1796 0.1745 0.0020  -0.0104 -0.0168 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1445 0.1416 0.1365 0.0004  -0.0255 -0.0105 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1485 0.1484 0.1501 0.0004  -0.0287 -0.0089 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1591 0.1595 0.1598 0.0006  -0.0272 -0.0074 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1657 0.1685 0.1761 0.0009  -0.0264 -0.0062 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1613 0.1582 0.1508 0.0002  -0.0257 -0.0074 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1471 0.1439 0.1353 0.0001  -0.0237 -0.0060 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1503 0.1523 0.1441 -0.0006 -0.0182 -0.0062 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1536 0.1591 0.1472 -0.0014 -0.0156 -0.0066 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1411 0.1423 0.1394 -0.0008 -0.0167 -0.0056 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1346 0.1374 0.1342 -0.0029 -0.0112 -0.0064 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1301 0.1325 0.1214 -0.0054 -0.0087 -0.0061 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1489 0.1484 0.1358 -0.0050 -0.0093 -0.0052 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1676 0.1677 0.1761 -0.0023 -0.0086 -0.0065 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1824 0.1851 0.2024 -0.0009 -0.0097 -0.0065 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1999 0.1971 0.2046 -0.0056 -0.0014 -0.0081 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2164 0.2169 0.2510 0.0006  -0.0064 -0.0058 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1333 0.1384 0.1225 -0.0086 -0.0065 -0.0061 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1391 0.1440 0.1219 -0.0126 -0.0049 -0.0053 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1478 0.1475 0.1274 -0.0164 -0.0009 -0.0070 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1550 0.1540 0.1359 -0.0175 0.0008  -0.0079 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1403 0.1512 0.1238 -0.0146 -0.0067 -0.0029 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1533 0.1650 0.1322 -0.0203 -0.0070 -0.0008 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1593 0.1706 0.1369 -0.0202 -0.0064 0.0001  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1707 0.1889 0.1539 -0.0227 -0.0101 0.0031  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1539 0.1483 0.1288 -0.0184 0.0016  -0.0077 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1773 0.1634 0.1470 -0.0224 0.0073  -0.0103 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1827 0.1652 0.1415 -0.0289 0.0075  -0.0101 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1840 0.1687 0.1427 -0.0287 0.0050  -0.0083 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2325 0.2132 0.2090 -0.0183 0.0107  -0.0114 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3461 0.3281 0.3351 -0.0134 0.0113  -0.0114 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.4128 0.3896 0.4113 -0.0100 0.0141  -0.0109 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4994 0.4773 0.5135 -0.0061 0.0153  -0.0102 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.5202 0.4931 0.5403 -0.0069 0.0241  -0.0125 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5108 0.4749 0.5189 -0.0120 0.0325  -0.0161 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5329 0.5083 0.5707 -0.0031 0.0250  -0.0110 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2085 0.1840 0.1574 -0.0355 0.0108  -0.0121 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2292 0.1979 0.1653 -0.0435 0.0111  -0.0126 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2698 0.2241 0.1995 -0.0455 0.0206  -0.0175 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2649 0.2163 0.2035 -0.0399 0.0265  -0.0196 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2342 0.2040 0.1603 -0.0515 0.0064  -0.0104 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2353 0.1952 0.1507 -0.0557 0.0124  -0.0136 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3090 0.2531 0.2237 -0.0541 0.0224  -0.0194 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3536 0.2815 0.2608 -0.0567 0.0331  -0.0247 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3632 0.2824 0.2665 -0.0576 0.0420  -0.0285 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3986 0.3064 0.3047 -0.0557 0.0533  -0.0326 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4062 0.3232 0.2942 -0.0678 0.0325  -0.0262 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4744 0.3915 0.3465 -0.0781 0.0253  -0.0242 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5695 0.4743 0.4215 -0.0906 0.0235  -0.0255 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5907 0.5025 0.4396 -0.0970 0.0125  -0.0204 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5800 0.4656 0.4191 -0.0947 0.0346  -0.0320 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.3222 0.2471 0.2221 -0.0596 0.0376  -0.0265 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.3172 0.2339 0.2118 -0.0614 0.0459  -0.0295 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.3102 0.2360 0.2268 -0.0512 0.0483  -0.0285 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3445 0.2633 0.2611 -0.0515 0.0574  -0.0311 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.3179 0.2341 0.1950 -0.0706 0.0395  -0.0273 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3432 0.2507 0.1987 -0.0822 0.0347  -0.0271 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3343 0.2536 0.1911 -0.0851 0.0210  -0.0210 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3960 0.2834 0.2279 -0.0926 0.0420  -0.0321 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3898 0.2974 0.2260 -0.0969 0.0189  -0.0218 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.4256 0.3130 0.2445 -0.1020 0.0311  -0.0288 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2657 0.2060 0.1996 -0.0431 0.0401  -0.0247 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2396 0.1881 0.1932 -0.0347 0.0404  -0.0233 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1912 0.1546 0.1525 -0.0306 0.0290  -0.0189 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2089 0.1774 0.1650 -0.0323 0.0218  -0.0166 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1799 0.1494 0.1537 -0.0259 0.0281  -0.0178 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1742 0.1556 0.1550 -0.0221 0.0188  -0.0145 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1751 0.1592 0.1452 -0.0273 0.0148  -0.0127 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1879 0.1670 0.1507 -0.0319 0.0185  -0.0135 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1861 0.1712 0.1826 -0.0169 0.0194  -0.0141 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1940 0.1885 0.1948 -0.0142 0.0110  -0.0116 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1994 0.1830 0.2101 -0.0118 0.0212  -0.0140 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1571 0.1487 0.1274 -0.0266 0.0073  -0.0098 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1641 0.1601 0.1291 -0.0307 0.0021  -0.0063 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1558 0.1596 0.1315 -0.0260 -0.0014 -0.0043 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1652 0.1706 0.1394 -0.0287 -0.0033 -0.0019 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1754 0.1748 0.1379 -0.0326 -0.0024 -0.0038 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1796 0.1857 0.1430 -0.0360 -0.0087 0.0014  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1989 0.1891 0.1495 -0.0386 0.0009  -0.0060 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1484 0.1560 0.1334 -0.0196 -0.0028 -0.0049 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1558 0.1687 0.1491 -0.0156 -0.0059 -0.0037 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1431 0.1567 0.1418 -0.0103 -0.0075 -0.0051 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1446 0.1550 0.1421 -0.0093 -0.0066 -0.0063 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1329 0.1493 0.1361 -0.0075 -0.0101 -0.0045 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1308 0.1452 0.1348 -0.0039 -0.0123 -0.0059 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1373 0.1526 0.1395 -0.0026 -0.0126 -0.0052 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1368 0.1556 0.1429 -0.0031 -0.0120 -0.0034 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1363 0.1497 0.1471 -0.0022 -0.0144 -0.0071 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1580 0.1740 0.1734 -0.0027 -0.0140 -0.0065 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1677 0.1794 0.1837 -0.0024 -0.0130 -0.0075 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1643 0.1791 0.1872 -0.0012 -0.0168 -0.0077 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1297 0.1410 0.1263 -0.0012 -0.0131 -0.0063 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1303 0.1401 0.1246 0.0001  -0.0109 -0.0064 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1406 0.1496 0.1391 0.0013  -0.0112 -0.0074 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1367 0.1428 0.1351 0.0014  -0.0146 -0.0091 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1425 0.1447 0.1261 0.0005  -0.0110 -0.0080 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1651 0.1626 0.1443 0.0015  -0.0064 -0.0091 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1699 0.1725 0.1500 -0.0006 -0.0101 -0.0065 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1332 0.1445 0.1370 0.0021  -0.0077 -0.0058 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1381 0.1480 0.1470 0.0035  -0.0069 -0.0065 125 SER   A CA  
923  C C   . SER   A 119 ? 0.1639 0.1697 0.1738 0.0054  -0.0007 -0.0069 125 SER   A C   
924  O O   . SER   A 119 ? 0.1781 0.1776 0.1871 0.0065  0.0010  -0.0095 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1483 0.1655 0.1674 0.0025  -0.0083 -0.0028 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1482 0.1643 0.1738 0.0038  -0.0076 -0.0027 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1563 0.1646 0.1686 0.0058  0.0036  -0.0046 126 THR   A N   
928  C CA  . THR   A 120 ? 0.1628 0.1666 0.1785 0.0080  0.0120  -0.0049 126 THR   A CA  
929  C C   . THR   A 120 ? 0.1866 0.1867 0.1948 0.0076  0.0169  -0.0055 126 THR   A C   
930  O O   . THR   A 120 ? 0.1847 0.1872 0.1868 0.0057  0.0129  -0.0049 126 THR   A O   
931  C CB  . THR   A 120 ? 0.1733 0.1863 0.2093 0.0094  0.0139  0.0012  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.1866 0.2088 0.2290 0.0075  0.0117  0.0062  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1561 0.1727 0.1991 0.0092  0.0089  0.0029  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1959 0.1894 0.2050 0.0094  0.0266  -0.0066 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2175 0.2070 0.2203 0.0090  0.0331  -0.0068 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2421 0.2231 0.2480 0.0112  0.0464  -0.0083 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2704 0.2478 0.2831 0.0132  0.0507  -0.0095 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2756 0.2506 0.2731 0.0103  0.0536  -0.0092 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2940 0.2594 0.2935 0.0121  0.0692  -0.0107 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2889 0.2663 0.3127 0.0137  0.0753  -0.0039 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2697 0.2635 0.3111 0.0134  0.0665  0.0024  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2887 0.2573 0.3132 0.0147  0.0907  -0.0050 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2869 0.2663 0.3376 0.0163  0.0985  0.0019  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2622 0.2533 0.3140 0.0131  0.0889  0.0065  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2565 0.2624 0.3347 0.0133  0.0878  0.0142  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2970 0.2906 0.3835 0.0200  0.0985  0.0091  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3569 0.3399 0.4519 0.0240  0.1130  0.0065  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3798 0.3448 0.4588 0.0242  0.1281  0.0000  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3638 0.3566 0.4839 0.0270  0.1094  0.0117  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2470 0.2314 0.2718 0.0098  0.0809  0.0023  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2234 0.2166 0.2478 0.0068  0.0727  0.0058  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1856 0.1938 0.2216 0.0055  0.0579  0.0100  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.1835 0.1997 0.2241 0.0026  0.0524  0.0138  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1723 0.1828 0.2124 0.0070  0.0527  0.0094  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1648 0.1867 0.2122 0.0051  0.0399  0.0128  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1768 0.1920 0.2044 0.0046  0.0325  0.0072  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2171 0.2207 0.2310 0.0061  0.0362  0.0018  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1692 0.2006 0.2408 0.0070  0.0392  0.0184  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1840 0.2243 0.2824 0.0077  0.0457  0.0259  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2079 0.2536 0.3293 0.0108  0.0473  0.0306  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1821 0.2338 0.2886 0.0028  0.0368  0.0322  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1431 0.1646 0.1693 0.0020  0.0225  0.0086  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1396 0.1571 0.1534 0.0017  0.0158  0.0046  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1341 0.1606 0.1586 0.0002  0.0091  0.0081  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1367 0.1710 0.1692 -0.0028 0.0059  0.0129  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1555 0.1681 0.1538 -0.0003 0.0122  0.0021  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1807 0.1993 0.1827 -0.0035 0.0102  0.0055  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1570 0.1672 0.1484 -0.0004 0.0055  -0.0008 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1277 0.1523 0.1511 0.0016  0.0067  0.0060  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1218 0.1532 0.1529 -0.0003 0.0009  0.0094  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1258 0.1540 0.1464 -0.0016 -0.0037 0.0058  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1485 0.1700 0.1610 0.0003  -0.0031 0.0012  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1150 0.1471 0.1355 -0.0054 -0.0080 0.0082  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1263 0.1550 0.1389 -0.0068 -0.0103 0.0051  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1257 0.1569 0.1421 -0.0088 -0.0128 0.0074  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1271 0.1628 0.1475 -0.0122 -0.0152 0.0125  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1274 0.1549 0.1324 -0.0106 -0.0111 0.0048  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1201 0.1458 0.1218 -0.0096 -0.0089 0.0039  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1313 0.1511 0.1266 -0.0072 -0.0080 0.0003  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1416 0.1713 0.1472 -0.0118 -0.0085 0.0076  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1389 0.1558 0.1295 -0.0068 -0.0061 0.0001  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1525 0.1798 0.1546 -0.0113 -0.0058 0.0070  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1437 0.1641 0.1373 -0.0087 -0.0043 0.0031  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1184 0.1465 0.1339 -0.0072 -0.0127 0.0044  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1194 0.1483 0.1367 -0.0095 -0.0141 0.0062  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1264 0.1526 0.1349 -0.0143 -0.0137 0.0057  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1463 0.1686 0.1511 -0.0136 -0.0114 0.0018  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1222 0.1484 0.1427 -0.0064 -0.0134 0.0030  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1263 0.1535 0.1311 -0.0198 -0.0160 0.0099  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1324 0.1540 0.1249 -0.0258 -0.0146 0.0089  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1431 0.1596 0.1332 -0.0260 -0.0105 0.0060  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1631 0.1813 0.1591 -0.0247 -0.0113 0.0076  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1680 0.1903 0.1547 -0.0333 -0.0196 0.0151  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.1931 0.2066 0.1621 -0.0414 -0.0182 0.0136  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2134 0.2235 0.1773 -0.0418 -0.0154 0.0100  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.2667 0.2754 0.2256 -0.0480 -0.0196 0.0163  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1452 0.1545 0.1270 -0.0285 -0.0052 0.0021  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1599 0.1635 0.1404 -0.0296 0.0007  -0.0003 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1794 0.1725 0.1420 -0.0380 0.0054  -0.0012 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1908 0.1768 0.1499 -0.0400 0.0127  -0.0035 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1718 0.1749 0.1630 -0.0238 0.0050  -0.0045 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1642 0.1747 0.1685 -0.0173 -0.0001 -0.0040 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1785 0.1774 0.1657 -0.0239 0.0081  -0.0072 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1933 0.1845 0.1444 -0.0435 0.0018  0.0005  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1922 0.1707 0.1227 -0.0527 0.0060  -0.0011 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2301 0.2020 0.1475 -0.0601 0.0061  0.0016  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2606 0.2184 0.1589 -0.0677 0.0131  -0.0013 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2055 0.1834 0.1269 -0.0580 0.0004  0.0006  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2027 0.1842 0.1334 -0.0520 0.0018  -0.0024 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2232 0.2049 0.1463 -0.0577 -0.0041 0.0002  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2122 0.2061 0.1461 -0.0564 -0.0136 0.0069  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2311 0.2297 0.1665 -0.0596 -0.0200 0.0110  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2273 0.2184 0.1504 -0.0660 -0.0195 0.0092  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2258 0.2361 0.1761 -0.0569 -0.0267 0.0174  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2057 0.1858 0.1315 -0.0584 -0.0007 0.0071  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2183 0.1919 0.1314 -0.0657 -0.0014 0.0108  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2463 0.2152 0.1631 -0.0628 0.0087  0.0072  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2723 0.2327 0.1758 -0.0694 0.0111  0.0091  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2443 0.2281 0.1662 -0.0656 -0.0132 0.0195  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2560 0.2511 0.2018 -0.0549 -0.0135 0.0197  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2471 0.2469 0.2048 -0.0473 -0.0103 0.0149  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.2676 0.2656 0.2191 -0.0547 -0.0169 0.0247  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2304 0.2045 0.1655 -0.0537 0.0142  0.0025  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2389 0.2110 0.1832 -0.0506 0.0226  0.0002  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2488 0.2073 0.1827 -0.0544 0.0359  -0.0052 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2460 0.2049 0.1926 -0.0489 0.0426  -0.0095 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2214 0.2050 0.1906 -0.0402 0.0204  -0.0012 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2159 0.2104 0.1945 -0.0363 0.0096  0.0031  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2018 0.2042 0.1998 -0.0276 0.0078  0.0008  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2315 0.2264 0.2088 -0.0392 0.0066  0.0081  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2586 0.2036 0.1677 -0.0646 0.0396  -0.0047 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2855 0.2139 0.1795 -0.0698 0.0539  -0.0105 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3034 0.2293 0.2133 -0.0650 0.0678  -0.0141 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3203 0.2363 0.2301 -0.0650 0.0809  -0.0195 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3073 0.2187 0.1668 -0.0836 0.0552  -0.0092 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3206 0.2346 0.1653 -0.0902 0.0395  -0.0035 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3499 0.2437 0.1574 -0.1055 0.0413  -0.0026 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3232 0.2426 0.1727 -0.0876 0.0345  -0.0054 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2868 0.2212 0.2117 -0.0611 0.0652  -0.0107 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2890 0.2228 0.2324 -0.0568 0.0770  -0.0129 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2906 0.2340 0.2630 -0.0470 0.0786  -0.0153 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2981 0.2399 0.2879 -0.0439 0.0898  -0.0171 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2785 0.2192 0.2302 -0.0558 0.0721  -0.0083 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2525 0.2092 0.2176 -0.0501 0.0559  -0.0041 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2568 0.2169 0.2106 -0.0532 0.0439  0.0008  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2339 0.2041 0.2266 -0.0407 0.0508  -0.0044 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2524 0.2264 0.2253 -0.0457 0.0337  0.0029  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2339 0.2133 0.2285 -0.0386 0.0375  -0.0004 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2303 0.2047 0.2468 -0.0345 0.0562  -0.0068 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2355 0.2261 0.2503 -0.0311 0.0302  -0.0003 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2282 0.2147 0.2650 -0.0277 0.0466  -0.0057 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2190 0.2124 0.2529 -0.0264 0.0343  -0.0030 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2736 0.2265 0.2521 -0.0424 0.0677  -0.0148 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2799 0.2407 0.2832 -0.0341 0.0675  -0.0161 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3318 0.2816 0.3383 -0.0343 0.0828  -0.0203 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3279 0.2829 0.3604 -0.0277 0.0858  -0.0203 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2624 0.2313 0.2645 -0.0311 0.0547  -0.0150 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2444 0.2255 0.2525 -0.0279 0.0410  -0.0112 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2396 0.2257 0.2438 -0.0259 0.0319  -0.0107 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2484 0.2378 0.2815 -0.0215 0.0390  -0.0103 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3711 0.3047 0.3516 -0.0424 0.0924  -0.0236 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4365 0.3558 0.4150 -0.0439 0.1090  -0.0286 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5003 0.4073 0.4799 -0.0468 0.1274  -0.0311 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5262 0.4188 0.5030 -0.0485 0.1435  -0.0357 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4912 0.3965 0.4367 -0.0526 0.1098  -0.0316 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5653 0.4789 0.5143 -0.0490 0.0983  -0.0308 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5932 0.5144 0.5674 -0.0407 0.0985  -0.0306 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.5984 0.5109 0.5260 -0.0548 0.0887  -0.0297 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5229 0.4328 0.5033 -0.0484 0.1267  -0.0283 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5597 0.4577 0.5406 -0.0517 0.1449  -0.0302 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5691 0.4816 0.5820 -0.0452 0.1426  -0.0260 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.5890 0.4944 0.6026 -0.0483 0.1549  -0.0261 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6182 0.4999 0.5590 -0.0638 0.1479  -0.0309 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.6753 0.5679 0.6090 -0.0655 0.1303  -0.0249 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.7853 0.6674 0.6799 -0.0763 0.1224  -0.0237 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8045 0.6872 0.6870 -0.0811 0.1149  -0.0189 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8133 0.6865 0.6904 -0.0804 0.1228  -0.0270 145 GLU   A OE2 
1078 N N1  . A1BTD B .   ? 0.1747 0.1786 0.2067 0.0085  0.0016  -0.0059 201 A1BTD A N1  
1079 C C4  . A1BTD B .   ? 0.2426 0.2117 0.2089 0.0045  0.0132  -0.0184 201 A1BTD A C4  
1080 C C5  . A1BTD B .   ? 0.2460 0.2124 0.2182 0.0056  0.0154  -0.0201 201 A1BTD A C5  
1081 C C6  . A1BTD B .   ? 0.2534 0.2098 0.2237 0.0068  0.0261  -0.0227 201 A1BTD A C6  
1082 C C7  . A1BTD B .   ? 0.2556 0.2075 0.2329 0.0081  0.0296  -0.0246 201 A1BTD A C7  
1083 C C8  . A1BTD B .   ? 0.2211 0.1992 0.2309 0.0105  0.0185  -0.0155 201 A1BTD A C8  
1084 C C10 . A1BTD B .   ? 0.1969 0.1910 0.2263 0.0100  0.0072  -0.0094 201 A1BTD A C10 
1085 O O2  . A1BTD B .   ? 0.2778 0.2198 0.2424 0.0029  0.0135  -0.0303 201 A1BTD A O2  
1086 C C12 . A1BTD B .   ? 0.2493 0.2056 0.2318 0.0061  0.0143  -0.0252 201 A1BTD A C12 
1087 C C11 . A1BTD B .   ? 0.2394 0.2085 0.2397 0.0073  0.0090  -0.0209 201 A1BTD A C11 
1088 C C9  . A1BTD B .   ? 0.2176 0.2003 0.2288 0.0088  0.0089  -0.0152 201 A1BTD A C9  
1089 O O1  . A1BTD B .   ? 0.2048 0.1980 0.2450 0.0120  0.0113  -0.0078 201 A1BTD A O1  
1090 N N   . A1BTD B .   ? 0.2424 0.2042 0.2314 0.0083  0.0207  -0.0221 201 A1BTD A N   
1091 C C1  . A1BTD B .   ? 0.2677 0.2171 0.2295 0.0067  0.0351  -0.0237 201 A1BTD A C1  
1092 O O   . A1BTD B .   ? 0.2915 0.2294 0.2521 0.0079  0.0476  -0.0267 201 A1BTD A O   
1093 C C   . A1BTD B .   ? 0.3005 0.2306 0.2542 0.0079  0.0594  -0.0276 201 A1BTD A C   
1094 C C3  . A1BTD B .   ? 0.2481 0.2106 0.2059 0.0043  0.0210  -0.0191 201 A1BTD A C3  
1095 C C2  . A1BTD B .   ? 0.2552 0.2078 0.2105 0.0053  0.0323  -0.0218 201 A1BTD A C2  
# 
