data_7I8X
# 
_entry.id   7I8X 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I8X         pdb_00007i8x 10.2210/pdb7i8x/pdb 
WWPDB D_1001408464 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I8X 
_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   2025-03-18 
_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-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' 323.747   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                     65.409    1  ?         ? ? ? 
4 water       nat water                                                                          18.015    85 ?         ? ? ? 
# 
_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-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' A1BN7 
3 'ZINC ION'                                                                     ZN    
4 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 
A1BN7 non-polymer         . '(3S)-1-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' ? 
'C11 H12 Cl F2 N3 O2 S' 323.747 
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 
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        A1BN7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN7 
_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 A1BN7 1  201 201 A1BN7 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 HOH   1  301 37  HOH   HOH A . 
D 4 HOH   2  302 14  HOH   HOH A . 
D 4 HOH   3  303 2   HOH   HOH A . 
D 4 HOH   4  304 27  HOH   HOH A . 
D 4 HOH   5  305 18  HOH   HOH A . 
D 4 HOH   6  306 42  HOH   HOH A . 
D 4 HOH   7  307 34  HOH   HOH A . 
D 4 HOH   8  308 75  HOH   HOH A . 
D 4 HOH   9  309 29  HOH   HOH A . 
D 4 HOH   10 310 36  HOH   HOH A . 
D 4 HOH   11 311 24  HOH   HOH A . 
D 4 HOH   12 312 9   HOH   HOH A . 
D 4 HOH   13 313 35  HOH   HOH A . 
D 4 HOH   14 314 59  HOH   HOH A . 
D 4 HOH   15 315 25  HOH   HOH A . 
D 4 HOH   16 316 13  HOH   HOH A . 
D 4 HOH   17 317 60  HOH   HOH A . 
D 4 HOH   18 318 12  HOH   HOH A . 
D 4 HOH   19 319 23  HOH   HOH A . 
D 4 HOH   20 320 85  HOH   HOH A . 
D 4 HOH   21 321 47  HOH   HOH A . 
D 4 HOH   22 322 22  HOH   HOH A . 
D 4 HOH   23 323 8   HOH   HOH A . 
D 4 HOH   24 324 53  HOH   HOH A . 
D 4 HOH   25 325 7   HOH   HOH A . 
D 4 HOH   26 326 19  HOH   HOH A . 
D 4 HOH   27 327 84  HOH   HOH A . 
D 4 HOH   28 328 10  HOH   HOH A . 
D 4 HOH   29 329 16  HOH   HOH A . 
D 4 HOH   30 330 73  HOH   HOH A . 
D 4 HOH   31 331 4   HOH   HOH A . 
D 4 HOH   32 332 81  HOH   HOH A . 
D 4 HOH   33 333 54  HOH   HOH A . 
D 4 HOH   34 334 58  HOH   HOH A . 
D 4 HOH   35 335 17  HOH   HOH A . 
D 4 HOH   36 336 30  HOH   HOH A . 
D 4 HOH   37 337 82  HOH   HOH A . 
D 4 HOH   38 338 6   HOH   HOH A . 
D 4 HOH   39 339 79  HOH   HOH A . 
D 4 HOH   40 340 49  HOH   HOH A . 
D 4 HOH   41 341 21  HOH   HOH A . 
D 4 HOH   42 342 45  HOH   HOH A . 
D 4 HOH   43 343 33  HOH   HOH A . 
D 4 HOH   44 344 50  HOH   HOH A . 
D 4 HOH   45 345 70  HOH   HOH A . 
D 4 HOH   46 346 11  HOH   HOH A . 
D 4 HOH   47 347 48  HOH   HOH A . 
D 4 HOH   48 348 55  HOH   HOH A . 
D 4 HOH   49 349 32  HOH   HOH A . 
D 4 HOH   50 350 28  HOH   HOH A . 
D 4 HOH   51 351 67  HOH   HOH A . 
D 4 HOH   52 352 5   HOH   HOH A . 
D 4 HOH   53 353 56  HOH   HOH A . 
D 4 HOH   54 354 26  HOH   HOH A . 
D 4 HOH   55 355 78  HOH   HOH A . 
D 4 HOH   56 356 65  HOH   HOH A . 
D 4 HOH   57 357 68  HOH   HOH A . 
D 4 HOH   58 358 41  HOH   HOH A . 
D 4 HOH   59 359 80  HOH   HOH A . 
D 4 HOH   60 360 20  HOH   HOH A . 
D 4 HOH   61 361 40  HOH   HOH A . 
D 4 HOH   62 362 51  HOH   HOH A . 
D 4 HOH   63 363 46  HOH   HOH A . 
D 4 HOH   64 364 39  HOH   HOH A . 
D 4 HOH   65 365 3   HOH   HOH A . 
D 4 HOH   66 366 44  HOH   HOH A . 
D 4 HOH   67 367 74  HOH   HOH A . 
D 4 HOH   68 368 43  HOH   HOH A . 
D 4 HOH   69 369 15  HOH   HOH A . 
D 4 HOH   70 370 63  HOH   HOH A . 
D 4 HOH   71 371 72  HOH   HOH A . 
D 4 HOH   72 372 64  HOH   HOH A . 
D 4 HOH   73 373 66  HOH   HOH A . 
D 4 HOH   74 374 57  HOH   HOH A . 
D 4 HOH   75 375 31  HOH   HOH A . 
D 4 HOH   76 376 77  HOH   HOH A . 
D 4 HOH   77 377 76  HOH   HOH A . 
D 4 HOH   78 378 83  HOH   HOH A . 
D 4 HOH   79 379 61  HOH   HOH A . 
D 4 HOH   80 380 71  HOH   HOH A . 
D 4 HOH   81 381 38  HOH   HOH A . 
D 4 HOH   82 382 52  HOH   HOH A . 
D 4 HOH   83 383 86  HOH   HOH A . 
D 4 HOH   84 384 69  HOH   HOH A . 
D 4 HOH   85 385 62  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I8X 
_cell.length_a           73.216 
_cell.length_b           62.401 
_cell.length_c           33.133 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.81 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I8X 
_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          7I8X 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.38 
_exptl_crystal.density_percent_sol   48.28 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_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                     7I8X 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.57 
_reflns.d_resolution_high            1.67 
_reflns.number_obs                   17087 
_reflns.percent_possible_obs         98.9 
_reflns.pdbx_Rmerge_I_obs            0.276 
_reflns.pdbx_netI_over_sigmaI        3.9 
_reflns.pdbx_redundancy              6.6 
_reflns.pdbx_Rrim_I_all              0.300 
_reflns.pdbx_Rpim_I_all              0.116 
_reflns.pdbx_CC_half                 0.985 
_reflns.pdbx_number_measured_all     112594 
_reflns.pdbx_chi_squared             0.47 
_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                  1.67 
_reflns_shell.d_res_low                   1.70 
_reflns_shell.number_measured_all         5855 
_reflns_shell.number_unique_obs           844 
_reflns_shell.Rmerge_I_obs                5.211 
_reflns_shell.pdbx_chi_squared            0.17 
_reflns_shell.pdbx_redundancy             6.9 
_reflns_shell.percent_possible_obs        91.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             5.640 
_reflns_shell.pdbx_Rpim_I_all             2.133 
_reflns_shell.pdbx_CC_half                0.481 
_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                                 7I8X 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     13025 
_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                             19.00 
_refine.ls_d_res_high                            1.673 
_refine.ls_percent_reflns_obs                    75.5 
_refine.ls_R_factor_obs                          0.2770 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2744 
_refine.ls_R_factor_R_free                       0.3245 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.990 
_refine.ls_number_reflns_R_free                  650 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.921 
_refine.correlation_coeff_Fo_to_Fc_free          0.879 
_refine.B_iso_mean                               40.81 
_refine.aniso_B[1][1]                            0.46460 
_refine.aniso_B[2][2]                            -9.95570 
_refine.aniso_B[3][3]                            9.49100 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            4.13270 
_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             0.189 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.179 
_refine.pdbx_overall_SU_R_Blow_DPI               0.192 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.180 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I8X 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_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         21 
_refine_hist.number_atoms_solvent             85 
_refine_hist.number_atoms_total               1180 
_refine_hist.d_res_high                       1.673 
_refine_hist.d_res_low                        19.00 
# 
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                  0.010 ? 2.00  1121 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.09  ? 2.00  1527 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  373  '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  200  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1121 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.78  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           18.08 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  137  '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  812  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   33 
_refine_ls_shell.d_res_high                       1.67 
_refine_ls_shell.d_res_low                        1.75 
_refine_ls_shell.number_reflns_R_work             387 
_refine_ls_shell.R_factor_R_work                  0.4771 
_refine_ls_shell.percent_reflns_obs               19.22 
_refine_ls_shell.R_factor_R_free                  0.4762 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.15 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                408 
_refine_ls_shell.R_factor_all                     0.4771 
# 
_struct.entry_id                  7I8X 
_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-0036379-001 (A71EV2A-x4516)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I8X 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
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 ? 
# 
_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              7I8X 
_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 
# 
_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 ? ? ? ? ? ? ? 2.384 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.515 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
# 
_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 99.8  ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 110.5 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 119.7 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.7 ? 
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 97.2  ? 
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_555 118.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O TYR A 66  ? O TYR A 72  N TYR A 57  ? N TYR A 63  
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 GLY A 116 ? O GLY A 122 
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                   7I8X 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    360 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    368 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -93.05  33.80  
2 1 SER A 125 ? ? -140.51 -25.26 
# 
_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         15.2508 
_pdbx_refine_tls.origin_y         6.6306 
_pdbx_refine_tls.origin_z         14.4413 
_pdbx_refine_tls.T[1][1]          0.0248 
_pdbx_refine_tls.T[2][2]          -0.1265 
_pdbx_refine_tls.T[3][3]          0.1140 
_pdbx_refine_tls.T[1][2]          0.0791 
_pdbx_refine_tls.T[1][3]          0.0988 
_pdbx_refine_tls.T[2][3]          -0.0117 
_pdbx_refine_tls.L[1][1]          1.6272 
_pdbx_refine_tls.L[2][2]          9.5484 
_pdbx_refine_tls.L[3][3]          0.9323 
_pdbx_refine_tls.L[1][2]          2.4957 
_pdbx_refine_tls.L[1][3]          -0.9665 
_pdbx_refine_tls.L[2][3]          -2.1150 
_pdbx_refine_tls.S[1][1]          -0.1113 
_pdbx_refine_tls.S[1][2]          -0.0034 
_pdbx_refine_tls.S[1][3]          0.0952 
_pdbx_refine_tls.S[2][1]          0.2722 
_pdbx_refine_tls.S[2][2]          0.1215 
_pdbx_refine_tls.S[2][3]          -0.4630 
_pdbx_refine_tls.S[3][1]          0.1335 
_pdbx_refine_tls.S[3][2]          -0.2494 
_pdbx_refine_tls.S[3][3]          -0.0102 
# 
_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 
A1BN7 N1   N  N N 1   
A1BN7 C4   C  N N 2   
A1BN7 C5   C  N N 3   
A1BN7 C6   C  N N 4   
A1BN7 C7   C  Y N 5   
A1BN7 C8   C  Y N 6   
A1BN7 C10  C  N N 7   
A1BN7 CL   CL N N 8   
A1BN7 C9   C  Y N 9   
A1BN7 S    S  Y N 10  
A1BN7 N2   N  Y N 11  
A1BN7 F    F  N N 12  
A1BN7 F1   F  N N 13  
A1BN7 O1   O  N N 14  
A1BN7 C3   C  N N 15  
A1BN7 C2   C  N N 16  
A1BN7 C1   C  N S 17  
A1BN7 C    C  N N 18  
A1BN7 O    O  N N 19  
A1BN7 N    N  N N 20  
A1BN7 H8   H  N N 21  
A1BN7 H7   H  N N 22  
A1BN7 H9   H  N N 23  
A1BN7 H11  H  N N 24  
A1BN7 H10  H  N N 25  
A1BN7 H6   H  N N 26  
A1BN7 H5   H  N N 27  
A1BN7 H4   H  N N 28  
A1BN7 H3   H  N N 29  
A1BN7 H    H  N N 30  
A1BN7 H2   H  N N 31  
A1BN7 H1   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
THR   N    N  N N 336 
THR   CA   C  N S 337 
THR   C    C  N N 338 
THR   O    O  N N 339 
THR   CB   C  N R 340 
THR   OG1  O  N N 341 
THR   CG2  C  N N 342 
THR   OXT  O  N N 343 
THR   H    H  N N 344 
THR   H2   H  N N 345 
THR   HA   H  N N 346 
THR   HB   H  N N 347 
THR   HG1  H  N N 348 
THR   HG21 H  N N 349 
THR   HG22 H  N N 350 
THR   HG23 H  N N 351 
THR   HXT  H  N N 352 
TRP   N    N  N N 353 
TRP   CA   C  N S 354 
TRP   C    C  N N 355 
TRP   O    O  N N 356 
TRP   CB   C  N N 357 
TRP   CG   C  Y N 358 
TRP   CD1  C  Y N 359 
TRP   CD2  C  Y N 360 
TRP   NE1  N  Y N 361 
TRP   CE2  C  Y N 362 
TRP   CE3  C  Y N 363 
TRP   CZ2  C  Y N 364 
TRP   CZ3  C  Y N 365 
TRP   CH2  C  Y N 366 
TRP   OXT  O  N N 367 
TRP   H    H  N N 368 
TRP   H2   H  N N 369 
TRP   HA   H  N N 370 
TRP   HB2  H  N N 371 
TRP   HB3  H  N N 372 
TRP   HD1  H  N N 373 
TRP   HE1  H  N N 374 
TRP   HE3  H  N N 375 
TRP   HZ2  H  N N 376 
TRP   HZ3  H  N N 377 
TRP   HH2  H  N N 378 
TRP   HXT  H  N N 379 
TYR   N    N  N N 380 
TYR   CA   C  N S 381 
TYR   C    C  N N 382 
TYR   O    O  N N 383 
TYR   CB   C  N N 384 
TYR   CG   C  Y N 385 
TYR   CD1  C  Y N 386 
TYR   CD2  C  Y N 387 
TYR   CE1  C  Y N 388 
TYR   CE2  C  Y N 389 
TYR   CZ   C  Y N 390 
TYR   OH   O  N N 391 
TYR   OXT  O  N N 392 
TYR   H    H  N N 393 
TYR   H2   H  N N 394 
TYR   HA   H  N N 395 
TYR   HB2  H  N N 396 
TYR   HB3  H  N N 397 
TYR   HD1  H  N N 398 
TYR   HD2  H  N N 399 
TYR   HE1  H  N N 400 
TYR   HE2  H  N N 401 
TYR   HH   H  N N 402 
TYR   HXT  H  N N 403 
VAL   N    N  N N 404 
VAL   CA   C  N S 405 
VAL   C    C  N N 406 
VAL   O    O  N N 407 
VAL   CB   C  N N 408 
VAL   CG1  C  N N 409 
VAL   CG2  C  N N 410 
VAL   OXT  O  N N 411 
VAL   H    H  N N 412 
VAL   H2   H  N N 413 
VAL   HA   H  N N 414 
VAL   HB   H  N N 415 
VAL   HG11 H  N N 416 
VAL   HG12 H  N N 417 
VAL   HG13 H  N N 418 
VAL   HG21 H  N N 419 
VAL   HG22 H  N N 420 
VAL   HG23 H  N N 421 
VAL   HXT  H  N N 422 
ZN    ZN   ZN N N 423 
# 
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 
A1BN7 N   C    sing N N 1   
A1BN7 O   C    doub N N 2   
A1BN7 C   C1   sing N N 3   
A1BN7 C1  C2   sing N N 4   
A1BN7 C2  C3   sing N N 5   
A1BN7 C3  C4   sing N N 6   
A1BN7 C4  N1   sing N N 7   
A1BN7 N1  C5   sing N N 8   
A1BN7 O1  C5   doub N N 9   
A1BN7 C5  C6   sing N N 10  
A1BN7 F   C6   sing N N 11  
A1BN7 F1  C6   sing N N 12  
A1BN7 C6  C7   sing N N 13  
A1BN7 C7  C8   sing Y N 14  
A1BN7 C8  N2   doub Y N 15  
A1BN7 N2  S    sing Y N 16  
A1BN7 S   C9   sing Y N 17  
A1BN7 C7  C9   doub Y N 18  
A1BN7 C9  CL   sing N N 19  
A1BN7 C10 N1   sing N N 20  
A1BN7 C1  C10  sing N N 21  
A1BN7 C4  H8   sing N N 22  
A1BN7 C4  H7   sing N N 23  
A1BN7 C8  H9   sing N N 24  
A1BN7 C10 H11  sing N N 25  
A1BN7 C10 H10  sing N N 26  
A1BN7 C3  H6   sing N N 27  
A1BN7 C3  H5   sing N N 28  
A1BN7 C2  H4   sing N N 29  
A1BN7 C2  H3   sing N N 30  
A1BN7 C1  H    sing N N 31  
A1BN7 N   H2   sing N N 32  
A1BN7 N   H1   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
GLN   N   CA   sing N N 116 
GLN   N   H    sing N N 117 
GLN   N   H2   sing N N 118 
GLN   CA  C    sing N N 119 
GLN   CA  CB   sing N N 120 
GLN   CA  HA   sing N N 121 
GLN   C   O    doub N N 122 
GLN   C   OXT  sing N N 123 
GLN   CB  CG   sing N N 124 
GLN   CB  HB2  sing N N 125 
GLN   CB  HB3  sing N N 126 
GLN   CG  CD   sing N N 127 
GLN   CG  HG2  sing N N 128 
GLN   CG  HG3  sing N N 129 
GLN   CD  OE1  doub N N 130 
GLN   CD  NE2  sing N N 131 
GLN   NE2 HE21 sing N N 132 
GLN   NE2 HE22 sing N N 133 
GLN   OXT HXT  sing N N 134 
GLU   N   CA   sing N N 135 
GLU   N   H    sing N N 136 
GLU   N   H2   sing N N 137 
GLU   CA  C    sing N N 138 
GLU   CA  CB   sing N N 139 
GLU   CA  HA   sing N N 140 
GLU   C   O    doub N N 141 
GLU   C   OXT  sing N N 142 
GLU   CB  CG   sing N N 143 
GLU   CB  HB2  sing N N 144 
GLU   CB  HB3  sing N N 145 
GLU   CG  CD   sing N N 146 
GLU   CG  HG2  sing N N 147 
GLU   CG  HG3  sing N N 148 
GLU   CD  OE1  doub N N 149 
GLU   CD  OE2  sing N N 150 
GLU   OE2 HE2  sing N N 151 
GLU   OXT HXT  sing N N 152 
GLY   N   CA   sing N N 153 
GLY   N   H    sing N N 154 
GLY   N   H2   sing N N 155 
GLY   CA  C    sing N N 156 
GLY   CA  HA2  sing N N 157 
GLY   CA  HA3  sing N N 158 
GLY   C   O    doub N N 159 
GLY   C   OXT  sing N N 160 
GLY   OXT HXT  sing N N 161 
HIS   N   CA   sing N N 162 
HIS   N   H    sing N N 163 
HIS   N   H2   sing N N 164 
HIS   CA  C    sing N N 165 
HIS   CA  CB   sing N N 166 
HIS   CA  HA   sing N N 167 
HIS   C   O    doub N N 168 
HIS   C   OXT  sing N N 169 
HIS   CB  CG   sing N N 170 
HIS   CB  HB2  sing N N 171 
HIS   CB  HB3  sing N N 172 
HIS   CG  ND1  sing Y N 173 
HIS   CG  CD2  doub Y N 174 
HIS   ND1 CE1  doub Y N 175 
HIS   ND1 HD1  sing N N 176 
HIS   CD2 NE2  sing Y N 177 
HIS   CD2 HD2  sing N N 178 
HIS   CE1 NE2  sing Y N 179 
HIS   CE1 HE1  sing N N 180 
HIS   NE2 HE2  sing N N 181 
HIS   OXT HXT  sing N N 182 
HOH   O   H1   sing N N 183 
HOH   O   H2   sing N N 184 
ILE   N   CA   sing N N 185 
ILE   N   H    sing N N 186 
ILE   N   H2   sing N N 187 
ILE   CA  C    sing N N 188 
ILE   CA  CB   sing N N 189 
ILE   CA  HA   sing N N 190 
ILE   C   O    doub N N 191 
ILE   C   OXT  sing N N 192 
ILE   CB  CG1  sing N N 193 
ILE   CB  CG2  sing N N 194 
ILE   CB  HB   sing N N 195 
ILE   CG1 CD1  sing N N 196 
ILE   CG1 HG12 sing N N 197 
ILE   CG1 HG13 sing N N 198 
ILE   CG2 HG21 sing N N 199 
ILE   CG2 HG22 sing N N 200 
ILE   CG2 HG23 sing N N 201 
ILE   CD1 HD11 sing N N 202 
ILE   CD1 HD12 sing N N 203 
ILE   CD1 HD13 sing N N 204 
ILE   OXT HXT  sing N N 205 
LEU   N   CA   sing N N 206 
LEU   N   H    sing N N 207 
LEU   N   H2   sing N N 208 
LEU   CA  C    sing N N 209 
LEU   CA  CB   sing N N 210 
LEU   CA  HA   sing N N 211 
LEU   C   O    doub N N 212 
LEU   C   OXT  sing N N 213 
LEU   CB  CG   sing N N 214 
LEU   CB  HB2  sing N N 215 
LEU   CB  HB3  sing N N 216 
LEU   CG  CD1  sing N N 217 
LEU   CG  CD2  sing N N 218 
LEU   CG  HG   sing N N 219 
LEU   CD1 HD11 sing N N 220 
LEU   CD1 HD12 sing N N 221 
LEU   CD1 HD13 sing N N 222 
LEU   CD2 HD21 sing N N 223 
LEU   CD2 HD22 sing N N 224 
LEU   CD2 HD23 sing N N 225 
LEU   OXT HXT  sing N N 226 
LYS   N   CA   sing N N 227 
LYS   N   H    sing N N 228 
LYS   N   H2   sing N N 229 
LYS   CA  C    sing N N 230 
LYS   CA  CB   sing N N 231 
LYS   CA  HA   sing N N 232 
LYS   C   O    doub N N 233 
LYS   C   OXT  sing N N 234 
LYS   CB  CG   sing N N 235 
LYS   CB  HB2  sing N N 236 
LYS   CB  HB3  sing N N 237 
LYS   CG  CD   sing N N 238 
LYS   CG  HG2  sing N N 239 
LYS   CG  HG3  sing N N 240 
LYS   CD  CE   sing N N 241 
LYS   CD  HD2  sing N N 242 
LYS   CD  HD3  sing N N 243 
LYS   CE  NZ   sing N N 244 
LYS   CE  HE2  sing N N 245 
LYS   CE  HE3  sing N N 246 
LYS   NZ  HZ1  sing N N 247 
LYS   NZ  HZ2  sing N N 248 
LYS   NZ  HZ3  sing N N 249 
LYS   OXT HXT  sing N N 250 
MET   N   CA   sing N N 251 
MET   N   H    sing N N 252 
MET   N   H2   sing N N 253 
MET   CA  C    sing N N 254 
MET   CA  CB   sing N N 255 
MET   CA  HA   sing N N 256 
MET   C   O    doub N N 257 
MET   C   OXT  sing N N 258 
MET   CB  CG   sing N N 259 
MET   CB  HB2  sing N N 260 
MET   CB  HB3  sing N N 261 
MET   CG  SD   sing N N 262 
MET   CG  HG2  sing N N 263 
MET   CG  HG3  sing N N 264 
MET   SD  CE   sing N N 265 
MET   CE  HE1  sing N N 266 
MET   CE  HE2  sing N N 267 
MET   CE  HE3  sing N N 268 
MET   OXT HXT  sing N N 269 
PHE   N   CA   sing N N 270 
PHE   N   H    sing N N 271 
PHE   N   H2   sing N N 272 
PHE   CA  C    sing N N 273 
PHE   CA  CB   sing N N 274 
PHE   CA  HA   sing N N 275 
PHE   C   O    doub N N 276 
PHE   C   OXT  sing N N 277 
PHE   CB  CG   sing N N 278 
PHE   CB  HB2  sing N N 279 
PHE   CB  HB3  sing N N 280 
PHE   CG  CD1  doub Y N 281 
PHE   CG  CD2  sing Y N 282 
PHE   CD1 CE1  sing Y N 283 
PHE   CD1 HD1  sing N N 284 
PHE   CD2 CE2  doub Y N 285 
PHE   CD2 HD2  sing N N 286 
PHE   CE1 CZ   doub Y N 287 
PHE   CE1 HE1  sing N N 288 
PHE   CE2 CZ   sing Y N 289 
PHE   CE2 HE2  sing N N 290 
PHE   CZ  HZ   sing N N 291 
PHE   OXT HXT  sing N N 292 
PRO   N   CA   sing N N 293 
PRO   N   CD   sing N N 294 
PRO   N   H    sing N N 295 
PRO   CA  C    sing N N 296 
PRO   CA  CB   sing N N 297 
PRO   CA  HA   sing N N 298 
PRO   C   O    doub N N 299 
PRO   C   OXT  sing N N 300 
PRO   CB  CG   sing N N 301 
PRO   CB  HB2  sing N N 302 
PRO   CB  HB3  sing N N 303 
PRO   CG  CD   sing N N 304 
PRO   CG  HG2  sing N N 305 
PRO   CG  HG3  sing N N 306 
PRO   CD  HD2  sing N N 307 
PRO   CD  HD3  sing N N 308 
PRO   OXT HXT  sing N N 309 
SER   N   CA   sing N N 310 
SER   N   H    sing N N 311 
SER   N   H2   sing N N 312 
SER   CA  C    sing N N 313 
SER   CA  CB   sing N N 314 
SER   CA  HA   sing N N 315 
SER   C   O    doub N N 316 
SER   C   OXT  sing N N 317 
SER   CB  OG   sing N N 318 
SER   CB  HB2  sing N N 319 
SER   CB  HB3  sing N N 320 
SER   OG  HG   sing N N 321 
SER   OXT HXT  sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TRP   N   CA   sing N N 339 
TRP   N   H    sing N N 340 
TRP   N   H2   sing N N 341 
TRP   CA  C    sing N N 342 
TRP   CA  CB   sing N N 343 
TRP   CA  HA   sing N N 344 
TRP   C   O    doub N N 345 
TRP   C   OXT  sing N N 346 
TRP   CB  CG   sing N N 347 
TRP   CB  HB2  sing N N 348 
TRP   CB  HB3  sing N N 349 
TRP   CG  CD1  doub Y N 350 
TRP   CG  CD2  sing Y N 351 
TRP   CD1 NE1  sing Y N 352 
TRP   CD1 HD1  sing N N 353 
TRP   CD2 CE2  doub Y N 354 
TRP   CD2 CE3  sing Y N 355 
TRP   NE1 CE2  sing Y N 356 
TRP   NE1 HE1  sing N N 357 
TRP   CE2 CZ2  sing Y N 358 
TRP   CE3 CZ3  doub Y N 359 
TRP   CE3 HE3  sing N N 360 
TRP   CZ2 CH2  doub Y N 361 
TRP   CZ2 HZ2  sing N N 362 
TRP   CZ3 CH2  sing Y N 363 
TRP   CZ3 HZ3  sing N N 364 
TRP   CH2 HH2  sing N N 365 
TRP   OXT HXT  sing N N 366 
TYR   N   CA   sing N N 367 
TYR   N   H    sing N N 368 
TYR   N   H2   sing N N 369 
TYR   CA  C    sing N N 370 
TYR   CA  CB   sing N N 371 
TYR   CA  HA   sing N N 372 
TYR   C   O    doub N N 373 
TYR   C   OXT  sing N N 374 
TYR   CB  CG   sing N N 375 
TYR   CB  HB2  sing N N 376 
TYR   CB  HB3  sing N N 377 
TYR   CG  CD1  doub Y N 378 
TYR   CG  CD2  sing Y N 379 
TYR   CD1 CE1  sing Y N 380 
TYR   CD1 HD1  sing N N 381 
TYR   CD2 CE2  doub Y N 382 
TYR   CD2 HD2  sing N N 383 
TYR   CE1 CZ   doub Y N 384 
TYR   CE1 HE1  sing N N 385 
TYR   CE2 CZ   sing Y N 386 
TYR   CE2 HE2  sing N N 387 
TYR   CZ  OH   sing N N 388 
TYR   OH  HH   sing N N 389 
TYR   OXT HXT  sing N N 390 
VAL   N   CA   sing N N 391 
VAL   N   H    sing N N 392 
VAL   N   H2   sing N N 393 
VAL   CA  C    sing N N 394 
VAL   CA  CB   sing N N 395 
VAL   CA  HA   sing N N 396 
VAL   C   O    doub N N 397 
VAL   C   OXT  sing N N 398 
VAL   CB  CG1  sing N N 399 
VAL   CB  CG2  sing N N 400 
VAL   CB  HB   sing N N 401 
VAL   CG1 HG11 sing N N 402 
VAL   CG1 HG12 sing N N 403 
VAL   CG1 HG13 sing N N 404 
VAL   CG2 HG21 sing N N 405 
VAL   CG2 HG22 sing N N 406 
VAL   CG2 HG23 sing N N 407 
VAL   OXT HXT  sing N N 408 
# 
_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_1002344 
_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                    7I8X 
_atom_sites.fract_transf_matrix[1][1]   0.013658 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000670 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016025 
_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]   0.030218 
_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  
CL 
F  
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   ? 19.355 6.725   24.235 1.00 46.54  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.580 5.984   23.970 1.00 46.79  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.387 5.107   22.735 1.00 46.09  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.346 4.467   22.625 1.00 46.15  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.916 5.106   25.173 1.00 48.99  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 19.937 4.092   25.378 1.00 52.70  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.362 5.083   21.823 1.00 45.03  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.278 4.212   20.652 1.00 44.88  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.562 4.776   19.267 1.00 43.99  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.020 5.819   18.895 1.00 44.59  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.348 4.040   18.451 1.00 42.28  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.671 4.489   17.090 1.00 41.65  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.759 3.329   16.059 1.00 40.72  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.819 2.161   16.450 1.00 39.24  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.984 5.257   17.128 1.00 42.15  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.731 3.648   14.741 1.00 40.93  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.876 2.618   13.693 1.00 41.26  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.250 2.819   13.061 1.00 41.39  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.668 3.947   12.796 1.00 40.15  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.775 2.695   12.601 1.00 41.51  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.354 2.881   13.186 1.00 40.91  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.852 1.487   11.670 1.00 41.93  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.383 3.323   12.195 1.00 40.72  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.954 1.744   12.837 1.00 43.39  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.293 1.807   12.279 1.00 45.31  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.323 1.065   10.956 1.00 46.42  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.295 -0.165  10.956 1.00 45.89  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.270 1.198   13.289 1.00 45.91  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.385 2.030   14.550 1.00 46.66  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.156 3.184   14.578 1.00 47.40  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.761 1.638   15.726 1.00 47.38  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.288 3.938   15.739 1.00 47.88  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.886 2.386   16.893 1.00 48.09  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.657 3.533   16.894 1.00 48.59  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.813 4.263   18.039 1.00 49.75  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.332 1.807   9.826  1.00 46.64  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.367 1.176   8.495  1.00 47.32  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.514 1.737   7.663  1.00 48.33  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.541 2.933   7.357  1.00 47.78  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.999 1.241   7.759  1.00 47.28  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.386 2.641   7.807  1.00 47.13  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.121 0.745   6.330  1.00 47.14  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.502 0.888   7.331  1.00 49.14  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.656 1.351   6.576  1.00 51.12  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.405 2.437   7.329  1.00 52.40  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.557 2.325   8.551  1.00 52.92  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.763 3.540   6.658  1.00 52.82  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.449 4.637   7.350  1.00 53.67  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.469 5.714   7.870  1.00 49.99  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.795 6.902   7.955  1.00 49.40  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.561 5.204   6.492  1.00 57.73  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.675 4.202   6.293  1.00 65.10  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.880 3.273   7.101  1.00 67.11  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.410 4.345   5.200  1.00 67.87  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.277 5.266   8.273  1.00 47.36  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.232 6.150   8.786  1.00 44.37  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.729 5.718   10.162 1.00 41.11  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.788 4.538   10.531 1.00 40.35  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.050 6.207   7.798  1.00 43.72  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.423 6.865   6.492  1.00 43.96  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.032 8.111   6.473  1.00 44.87  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.145 6.256   5.277  1.00 44.87  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.397 8.717   5.282  1.00 46.26  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.498 6.859   4.072  1.00 46.47  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.108 8.101   4.081  1.00 48.10  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.489 8.727   2.911  1.00 51.18  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.220 6.693   10.913 1.00 37.67  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.629 6.469   12.217 1.00 35.94  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.346 7.342   12.232 1.00 33.81  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.470 8.530   12.049 1.00 33.08  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.612 6.897   13.330 1.00 37.66  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.953 7.099   14.711 1.00 40.86  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.950 7.536   15.780 1.00 43.91  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.422 8.566   16.679 1.00 46.41  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.078 8.356   17.946 1.00 48.57  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.165 7.134   18.475 1.00 48.54  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.630 9.359   18.693 1.00 47.68  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.150 6.761   12.376 1.00 32.92  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.908 7.533   12.418 1.00 33.67  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.464 7.651   13.868 1.00 33.91  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.473 6.654   14.575 1.00 35.03  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.800 6.844   11.597 1.00 35.12  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.513 7.680   11.597 1.00 35.79  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.280 6.540   10.181 1.00 35.97  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.045 8.823   14.306 1.00 32.75  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.579 9.035   15.679 1.00 32.90  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.338 9.960   15.682 1.00 31.48  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.054 10.600  14.666 1.00 30.43  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.686 9.703   16.552 1.00 34.16  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.628 8.702   17.147 1.00 35.32  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.411 10.827  15.815 1.00 35.13  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.678 10.149  16.855 1.00 31.34  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.636 11.187  16.969 1.00 31.55  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.409 12.502  16.953 1.00 33.91  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.431 12.597  17.624 1.00 34.98  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.846 11.075  18.286 1.00 30.03  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.152 9.730   18.467 1.00 29.88  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.727 8.797   19.039 1.00 29.97  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.913 9.600   17.980 1.00 27.68  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.004 13.462  16.126 1.00 35.28  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.663 14.767  16.039 1.00 36.39  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.601 15.487  17.403 1.00 38.76  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.568 16.157  17.758 1.00 40.73  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.023 15.630  14.938 1.00 35.78  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.744 16.940  14.613 1.00 36.04  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.786 17.820  13.839 1.00 38.79  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.365 19.052  13.304 1.00 40.54  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.377 20.223  13.940 1.00 41.59  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.928 20.315  15.184 1.00 40.87  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.853 21.306  13.339 1.00 39.23  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.507 15.327  18.194 1.00 38.52  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.449 15.972  19.527 1.00 38.53  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.419 15.345  20.570 1.00 39.16  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.689 15.935  21.611 1.00 38.60  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.013 16.059  20.067 1.00 38.58  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.414 14.774  20.528 1.00 40.51  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.595 14.028  19.703 1.00 41.87  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.474 14.176  21.742 1.00 42.01  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.217 12.983  20.418 1.00 42.65  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.725 13.021  21.650 1.00 42.70  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.961 14.177  20.270 1.00 39.89  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.905 13.504  21.144 1.00 41.27  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.352 13.486  20.578 1.00 43.30  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.239 12.877  21.194 1.00 44.16  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.396 12.080  21.434 1.00 41.16  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.189 12.010  22.376 1.00 42.59  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.668 10.575  22.501 1.00 43.25  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.549 12.537  23.763 1.00 43.09  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.586 14.140  19.413 1.00 44.04  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.882 14.212  18.739 1.00 45.04  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.938 14.856  19.635 1.00 46.48  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.630 15.806  20.349 1.00 46.14  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.744 14.999  17.447 1.00 44.77  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.167 14.321  19.603 1.00 47.94  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.310 14.776  20.416 1.00 50.22  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.167 15.875  19.691 1.00 52.77  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.797 16.315  18.605 1.00 53.26  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.165 13.538  20.820 1.00 51.20  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.916 13.104  19.691 1.00 51.72  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.341 12.401  21.392 1.00 51.98  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.283 16.339  20.301 1.00 54.02  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.165 17.298  19.654 1.00 55.85  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.934 16.632  18.508 1.00 56.21  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.234 17.303  17.521 1.00 56.93  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.163 17.876  20.655 1.00 58.21  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.672 19.101  21.346 1.00 62.91  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.841 20.008  20.706 1.00 65.74  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.948 19.557  22.590 1.00 64.74  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.619 20.969  21.587 1.00 66.54  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.277 20.749  22.731 1.00 66.27  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.272 15.340  18.638 1.00 55.41  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.975 14.628  17.575 1.00 55.59  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.089 14.456  16.349 1.00 54.17  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.561 14.621  15.227 1.00 54.71  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.499 13.254  18.026 1.00 58.18  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.620 12.761  17.132 1.00 64.20  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.282 13.555  16.435 1.00 67.40  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.886 11.456  17.137 1.00 64.42  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.794 14.154  16.554 1.00 51.97  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.847 14.018  15.443 1.00 48.88  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.768 15.326  14.626 1.00 46.16  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.803 15.265  13.408 1.00 44.90  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.450 13.567  15.926 1.00 48.30  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.392 12.221  16.645 1.00 49.73  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.060 11.269  16.187 1.00 48.30  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.669 12.121  17.657 1.00 51.77  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.708 16.499  15.286 1.00 45.55  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.645 17.790  14.592 1.00 45.00  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.955 18.219  13.880 1.00 45.83  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.896 19.023  12.941 1.00 46.09  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.177 18.911  15.545 1.00 44.14  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.695 18.966  15.742 1.00 42.94  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.997 18.516  16.822 1.00 43.50  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.724 19.434  14.805 1.00 43.00  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.650 18.718  16.634 1.00 43.74  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.455 19.284  15.403 1.00 43.49  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.800 19.983  13.523 1.00 43.60  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.279 19.652  14.757 1.00 43.96  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.634 20.394  12.907 1.00 43.90  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.392 20.214  13.516 1.00 43.97  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.112 17.760  14.384 1.00 45.83  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.445 18.043  13.843 1.00 48.04  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.820 17.111  12.657 1.00 49.59  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.861 17.333  12.034 1.00 51.43  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.509 17.893  14.938 1.00 48.91  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.044 16.024  12.432 1.00 48.40  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.148 15.066  11.328 1.00 47.66  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.767 14.835  10.718 1.00 45.33  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.382 13.706  10.471 1.00 44.94  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.769 13.735  11.813 1.00 49.83  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.121 13.991  12.369 1.00 53.93  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.889 14.752  11.780 1.00 57.22  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.386 13.486  13.548 1.00 54.30  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.991 15.918  10.544 1.00 44.40  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.624 15.879  10.044 1.00 42.59  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.537 15.498  8.571  1.00 41.96  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.231 16.103  7.764  1.00 42.69  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.001 17.286  10.258 1.00 41.41  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.625 17.603  9.630  1.00 41.31  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.482 17.098  10.497 1.00 41.51  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.436 19.105  9.442  1.00 38.91  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.628 14.567  8.199  1.00 40.12  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.385 14.285  6.786  1.00 38.91  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.064 14.987  6.344  1.00 37.10  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.045 15.730  5.357  1.00 37.98  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.314 12.781  6.502  1.00 40.63  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.903 12.536  5.056  1.00 41.87  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.644 12.087  6.823  1.00 41.09  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.978 14.784  7.105  1.00 34.42  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.644 15.318  6.786  1.00 31.73  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.792 15.383  8.074  1.00 29.68  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.907 14.517  8.932  1.00 29.77  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.997 14.361  5.745  1.00 31.19  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.510 14.465  5.566  1.00 30.84  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.829 15.419  4.864  1.00 31.70  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.513 13.623  6.169  1.00 29.66  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.471 15.198  4.959  1.00 31.49  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.249 14.111  5.762  1.00 30.43  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.561 12.570  7.086  1.00 28.92  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.052 13.521  6.173  1.00 30.22  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.379 11.955  7.447  1.00 29.84  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.139 12.448  7.017  1.00 29.76  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.938 16.420  8.209  1.00 28.37  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.065 16.521  9.353  1.00 27.05  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.709 17.116  8.903  1.00 27.90  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.656 17.920  7.949  1.00 27.42  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.755 17.249  10.523 1.00 26.11  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.440 18.560  10.117 1.00 27.57  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.484 19.737  10.073 1.00 28.18  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.636 20.632  9.202  1.00 27.54  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.539 19.729  10.890 1.00 27.40  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.626 16.631  9.509  1.00 26.83  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.306 17.112  9.162  1.00 27.64  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.449 17.278  10.408 1.00 27.26  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.786 16.344  10.873 1.00 27.22  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.661 16.198  8.101  1.00 29.26  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.417 16.742  7.432  1.00 32.28  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.669 17.511  8.084  1.00 30.94  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.172 16.379  6.257  1.00 35.25  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.404 18.504  10.916 1.00 26.84  ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 15.538 18.907  12.011 1.00 27.50  ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 14.097 18.350  11.911 1.00 26.58  ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 13.597 17.827  12.890 1.00 25.31  ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 15.460 20.432  12.065 1.00 30.16  ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 16.046 20.896  13.264 1.00 33.37  ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.453 18.436  10.726 1.00 26.64  ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.078 17.946  10.593 1.00 27.42  ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 11.969 16.431  10.720 1.00 26.38  ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 10.881 15.975  10.932 1.00 26.57  ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 11.383 18.457  9.328  1.00 29.68  ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 11.725 17.684  8.191  1.00 32.83  ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.060 15.672  10.616 1.00 25.84  ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 13.085 14.193  10.770 1.00 25.99  ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 13.735 13.716  12.092 1.00 26.61  ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 13.726 12.522  12.370 1.00 27.03  ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 13.851 13.522  9.604  1.00 25.35  ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.201 13.717  8.238  1.00 26.14  ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 13.945 13.015  7.126  1.00 27.87  ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 13.929 11.555  7.255  1.00 29.37  ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 14.125 10.710  6.241  1.00 31.58  ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.308 11.171  5.006  1.00 29.95  ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 14.115 9.401   6.450  1.00 31.20  ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.333 14.640  12.865 1.00 26.98  ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.059 14.363  14.108 1.00 27.04  ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.218 13.423  13.793 1.00 26.64  ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.517 12.525  14.597 1.00 26.66  ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.128 13.809  15.216 1.00 28.28  ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 14.827 13.488  16.526 1.00 32.16  ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 15.705 14.270  16.939 1.00 32.13  ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 14.553 12.414  17.100 1.00 35.71  ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 16.890 13.603  12.607 1.00 25.58  ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 18.030 12.716  12.251 1.00 24.35  ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.392 13.441  12.022 1.00 24.37  ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.454 14.571  11.569 1.00 23.96  ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.728 11.883  10.993 1.00 24.44  ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.760 10.688  11.054 1.00 25.54  ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.759 9.965   9.673  1.00 24.33  ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 17.129 9.712   12.184 1.00 25.40  ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.490 12.727  12.252 1.00 24.56  ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 21.814 13.262  11.992 1.00 25.56  ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.710 12.072  11.722 1.00 26.97  ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.689 11.112  12.492 1.00 26.38  ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.328 14.145  13.174 1.00 26.23  ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 23.579 14.980  12.869 1.00 28.89  ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 23.729 16.146  13.787 1.00 29.68  ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 24.864 14.134  12.953 1.00 30.29  ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.453 12.104  10.596 1.00 29.03  ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.467 11.059  10.268 1.00 30.57  ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.889 11.648  10.421 1.00 33.14  ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 26.132 12.771  9.996  1.00 33.64  ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 24.263 10.433  8.868  1.00 31.11  ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 25.279 9.311   8.598  1.00 32.77  ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.842 9.928   8.702  1.00 31.40  ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.858 10.846  10.935 1.00 35.32  ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 28.223 11.321  11.086 1.00 38.44  ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 29.242 10.204  10.751 1.00 42.49  ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.930 9.016   10.860 1.00 41.18  ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.449 11.855  12.494 1.00 38.33  ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 28.032 10.878  13.439 1.00 39.48  ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.465 10.648  10.379 1.00 46.45  ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.621 9.898   9.907  1.00 51.84  ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 32.311 9.052   10.948 1.00 56.70  ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 32.627 9.517   12.039 1.00 57.64  ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.657 10.831  9.265  1.00 52.88  ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 32.196 12.167  9.122  1.00 52.55  ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.614 7.830   10.585 1.00 60.26  ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 33.334 6.904   11.472 1.00 63.81  ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.565 6.394   10.730 1.00 67.63  ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.553 6.384   9.501  1.00 68.41  ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 32.427 5.736   11.986 1.00 64.70  ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 32.615 4.562   11.198 1.00 66.59  ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 30.939 6.089   12.079 1.00 64.81  ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.593 5.908   11.449 1.00 69.96  ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.776 5.351   10.797 1.00 72.55  ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 36.652 3.819   10.713 1.00 73.73  ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 37.011 3.194   9.706  1.00 74.44  ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 38.067 5.825   11.497 1.00 75.35  ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 38.114 5.260   12.810 1.00 77.22  ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 38.149 7.331   11.591 1.00 75.92  ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 36.157 3.211   11.786 1.00 73.42  ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 35.862 1.806   11.806 1.00 72.85  ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 34.609 1.597   10.939 1.00 73.28  ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 33.703 2.444   10.914 1.00 73.31  ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 35.592 1.371   13.231 1.00 72.84  ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 34.575 0.481   10.209 1.00 73.71  ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 33.466 0.075   9.335  1.00 74.40  ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 32.273 -0.566  10.128 1.00 73.10  ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 32.490 -1.487  10.907 1.00 73.94  ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 34.018 -0.878  8.241  1.00 76.88  ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 33.022 -1.829  7.579  1.00 83.07  ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 32.188 -1.182  6.505  1.00 91.65  ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 32.520 -0.099  5.966  1.00 94.34  ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 31.067 -1.839  6.192  1.00 92.89  ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 31.050 -0.083  9.889  1.00 70.77  ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 29.810 -0.574  10.502 1.00 68.93  ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 29.258 -1.824  9.839  1.00 65.97  ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 29.536 -2.069  8.663  1.00 66.23  ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 28.457 -2.611  10.561 1.00 63.68  ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 28.021 -3.906  10.020 1.00 62.26  ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 26.512 -4.147  9.978  1.00 59.10  ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 26.103 -5.248  9.586  1.00 59.06  ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 28.728 -5.035  10.758 1.00 64.29  ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 30.302 -5.533  10.012 1.00 73.47  ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 25.690 -3.142  10.335 1.00 55.76  ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 24.237 -3.299  10.303 1.00 53.18  ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.691 -3.263  8.879  1.00 49.75  ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 24.114 -2.450  8.067  1.00 49.86  ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 23.529 -2.210  11.157 1.00 55.79  ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 23.954 -2.171  12.612 1.00 61.17  ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 24.672 -3.106  13.046 1.00 64.09  ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 23.576 -1.205  13.318 1.00 61.65  ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 22.709 -4.104  8.598  1.00 47.40  ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 22.043 -4.141  7.299  1.00 45.86  ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.789 -3.246  7.389  1.00 44.05  ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 20.037 -3.366  8.356  1.00 44.75  ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.686 -5.620  6.937  1.00 46.73  ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 22.859 -6.306  6.455  1.00 46.75  ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.595 -5.723  5.886  1.00 47.22  ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 20.551 -2.377  6.411  1.00 41.95  ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 19.352 -1.527  6.408  1.00 41.33  ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 18.306 -2.189  5.500  1.00 40.44  ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.660 -2.720  4.450  1.00 40.32  ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.701 -0.088  5.915  1.00 41.58  ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.896 0.499   6.683  1.00 42.50  ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 18.482 0.844   5.925  1.00 41.33  ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.615 0.773   8.158  1.00 44.01  ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 17.036 -2.177  5.895  1.00 39.80  ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 15.972 -2.774  5.085  1.00 39.50  ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.602 -1.857  3.918  1.00 40.32  ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.547 -0.635  4.073  1.00 40.43  ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.743 -3.042  5.938  1.00 38.04  ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 15.309 -2.455  2.770  1.00 41.16  ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.826 -1.775  1.561  1.00 42.05  ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.492 -2.485  1.214  1.00 43.13  ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.475 -3.424  0.410  1.00 43.68  ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.860 -1.880  0.449  1.00 43.13  ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 17.217 -1.240  0.774  1.00 45.28  ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 17.180 0.188   1.338  1.00 46.50  ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.541 0.695   1.526  1.00 46.14  ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.852 1.801   2.193  1.00 46.31  ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.898 2.565   2.708  1.00 42.46  ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 20.122 2.174   2.313  1.00 46.59  ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 12.393 -2.059  1.893  1.00 42.80  ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 11.072 -2.698  1.885  1.00 43.51  ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.957  -1.715  2.344  1.00 44.38  ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 10.253 -0.606  2.791  1.00 44.38  ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 11.140 -3.870  2.862  1.00 43.42  ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 11.099 -3.361  4.617  1.00 48.46  ? 56  CYS   A SG  1 
ATOM   389  N  N   . ASP   A 1 51  ? 8.696  -2.207  2.408  1.00 44.39  ? 57  ASP   A N   1 
ATOM   390  C  CA  . ASP   A 1 51  ? 7.591  -1.450  2.980  1.00 44.53  ? 57  ASP   A CA  1 
ATOM   391  C  C   . ASP   A 1 51  ? 6.801  -2.292  3.979  1.00 43.23  ? 57  ASP   A C   1 
ATOM   392  O  O   . ASP   A 1 51  ? 5.577  -2.299  3.939  1.00 43.58  ? 57  ASP   A O   1 
ATOM   393  C  CB  . ASP   A 1 51  ? 6.689  -0.761  1.944  1.00 47.80  ? 57  ASP   A CB  1 
ATOM   394  C  CG  . ASP   A 1 51  ? 5.726  -1.608  1.134  1.00 55.42  ? 57  ASP   A CG  1 
ATOM   395  O  OD1 . ASP   A 1 51  ? 5.924  -2.850  1.065  1.00 57.22  ? 57  ASP   A OD1 1 
ATOM   396  O  OD2 . ASP   A 1 51  ? 4.772  -1.031  0.565  1.00 58.99  ? 57  ASP   A OD2 1 
ATOM   397  N  N   . CYS   A 1 52  ? 7.510  -2.992  4.888  1.00 41.50  ? 58  CYS   A N   1 
ATOM   398  C  CA  . CYS   A 1 52  ? 6.880  -3.786  5.941  1.00 39.68  ? 58  CYS   A CA  1 
ATOM   399  C  C   . CYS   A 1 52  ? 6.138  -2.889  6.913  1.00 37.55  ? 58  CYS   A C   1 
ATOM   400  O  O   . CYS   A 1 52  ? 6.451  -1.716  7.042  1.00 38.71  ? 58  CYS   A O   1 
ATOM   401  C  CB  . CYS   A 1 52  ? 7.906  -4.634  6.689  1.00 40.02  ? 58  CYS   A CB  1 
ATOM   402  S  SG  . CYS   A 1 52  ? 8.638  -5.963  5.720  1.00 43.14  ? 58  CYS   A SG  1 
ATOM   403  N  N   . GLN   A 1 53  ? 5.179  -3.440  7.605  1.00 34.96  ? 59  GLN   A N   1 
ATOM   404  C  CA  . GLN   A 1 53  ? 4.452  -2.725  8.651  1.00 33.85  ? 59  GLN   A CA  1 
ATOM   405  C  C   . GLN   A 1 53  ? 4.346  -3.534  9.943  1.00 32.58  ? 59  GLN   A C   1 
ATOM   406  O  O   . GLN   A 1 53  ? 3.409  -3.340  10.714 1.00 31.63  ? 59  GLN   A O   1 
ATOM   407  C  CB  . GLN   A 1 53  ? 3.081  -2.254  8.150  1.00 35.10  ? 59  GLN   A CB  1 
ATOM   408  C  CG  . GLN   A 1 53  ? 3.126  -0.964  7.335  1.00 37.65  ? 59  GLN   A CG  1 
ATOM   409  C  CD  . GLN   A 1 53  ? 1.738  -0.568  6.908  1.00 41.61  ? 59  GLN   A CD  1 
ATOM   410  O  OE1 . GLN   A 1 53  ? 1.349  -0.736  5.751  1.00 44.05  ? 59  GLN   A OE1 1 
ATOM   411  N  NE2 . GLN   A 1 53  ? 0.942  -0.082  7.852  1.00 41.71  ? 59  GLN   A NE2 1 
ATOM   412  N  N   . THR   A 1 54  ? 5.269  -4.502  10.140 1.00 32.06  ? 60  THR   A N   1 
ATOM   413  C  CA  . THR   A 1 54  ? 5.435  -5.341  11.334 1.00 31.24  ? 60  THR   A CA  1 
ATOM   414  C  C   . THR   A 1 54  ? 6.928  -5.489  11.534 1.00 28.71  ? 60  THR   A C   1 
ATOM   415  O  O   . THR   A 1 54  ? 7.687  -5.608  10.568 1.00 27.87  ? 60  THR   A O   1 
ATOM   416  C  CB  . THR   A 1 54  ? 4.791  -6.740  11.238 1.00 33.46  ? 60  THR   A CB  1 
ATOM   417  O  OG1 . THR   A 1 54  ? 5.472  -7.513  10.257 1.00 35.28  ? 60  THR   A OG1 1 
ATOM   418  C  CG2 . THR   A 1 54  ? 3.277  -6.709  11.015 1.00 33.84  ? 60  THR   A CG2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 7.339  -5.500  12.780 1.00 27.56  ? 61  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 8.746  -5.597  13.131 1.00 27.81  ? 61  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 8.938  -5.816  14.619 1.00 28.09  ? 61  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 7.985  -6.227  15.299 1.00 29.08  ? 61  GLY   A O   1 
ATOM   423  N  N   . VAL   A 1 56  ? 10.175 -5.562  15.128 1.00 26.35  ? 62  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 56  ? 10.588 -5.700  16.529 1.00 26.11  ? 62  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 56  ? 11.454 -4.505  16.963 1.00 26.60  ? 62  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 56  ? 12.452 -4.189  16.303 1.00 26.41  ? 62  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 56  ? 11.317 -7.054  16.832 1.00 26.74  ? 62  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 56  ? 11.892 -7.091  18.261 1.00 26.98  ? 62  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 56  ? 10.387 -8.236  16.620 1.00 27.61  ? 62  VAL   A CG2 1 
ATOM   430  N  N   . TYR   A 1 57  ? 11.102 -3.872  18.103 1.00 26.77  ? 63  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 57  ? 11.890 -2.756  18.636 1.00 26.00  ? 63  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 57  ? 12.472 -3.054  20.034 1.00 25.58  ? 63  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 57  ? 11.910 -3.830  20.790 1.00 23.72  ? 63  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 57  ? 11.078 -1.438  18.621 1.00 26.12  ? 63  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 57  ? 10.111 -1.228  19.778 1.00 27.34  ? 63  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 57  ? 8.818  -1.745  19.733 1.00 27.67  ? 63  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 57  ? 10.433 -0.386  20.838 1.00 28.22  ? 63  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 57  ? 7.900  -1.483  20.740 1.00 29.08  ? 63  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 57  ? 9.540  -0.171  21.890 1.00 29.46  ? 63  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 57  ? 8.270  -0.722  21.835 1.00 30.49  ? 63  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 57  ? 7.360  -0.503  22.838 1.00 32.40  ? 63  TYR   A OH  1 
ATOM   442  N  N   . TYR   A 1 58  ? 13.602 -2.430  20.361 1.00 26.54  ? 64  TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 14.226 -2.608  21.662 1.00 27.51  ? 64  TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 13.809 -1.475  22.602 1.00 28.36  ? 64  TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 13.844 -0.316  22.219 1.00 26.93  ? 64  TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 15.749 -2.765  21.568 1.00 27.41  ? 64  TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 16.364 -2.815  22.950 1.00 28.94  ? 64  TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 16.164 -3.913  23.780 1.00 30.60  ? 64  TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 17.007 -1.707  23.482 1.00 29.94  ? 64  TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 16.673 -3.942  25.071 1.00 32.15  ? 64  TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 17.496 -1.712  24.778 1.00 31.21  ? 64  TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 17.330 -2.834  25.571 1.00 33.38  ? 64  TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 17.818 -2.840  26.862 1.00 36.02  ? 64  TYR   A OH  1 
ATOM   454  N  N   . CYS   A 1 59  ? 13.449 -1.809  23.853 1.00 30.68  ? 65  CYS   A N   1 
ATOM   455  C  CA  . CYS   A 1 59  ? 12.984 -0.829  24.828 1.00 31.98  ? 65  CYS   A CA  1 
ATOM   456  C  C   . CYS   A 1 59  ? 13.900 -0.755  26.052 1.00 34.16  ? 65  CYS   A C   1 
ATOM   457  O  O   . CYS   A 1 59  ? 13.730 -1.598  26.927 1.00 35.38  ? 65  CYS   A O   1 
ATOM   458  C  CB  . CYS   A 1 59  ? 11.552 -1.180  25.225 1.00 32.30  ? 65  CYS   A CB  1 
ATOM   459  S  SG  . CYS   A 1 59  ? 10.796 -0.029  26.394 1.00 36.03  ? 65  CYS   A SG  1 
ATOM   460  N  N   . SER   A 1 60  ? 14.852 0.232   26.130 1.00 34.10  ? 66  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 60  ? 15.799 0.385   27.252 1.00 35.51  ? 66  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 60  ? 15.126 0.399   28.618 1.00 37.08  ? 66  SER   A C   1 
ATOM   463  O  O   . SER   A 1 60  ? 15.647 -0.219  29.543 1.00 38.02  ? 66  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 60  ? 16.665 1.652   27.149 1.00 36.34  ? 66  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 60  ? 16.770 2.221   25.855 1.00 39.81  ? 66  SER   A OG  1 
ATOM   466  N  N   . SER   A 1 61  ? 13.997 1.148   28.753 1.00 37.45  ? 67  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 61  ? 13.242 1.317   30.009 1.00 37.84  ? 67  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 61  ? 12.606 0.029   30.547 1.00 37.45  ? 67  SER   A C   1 
ATOM   469  O  O   . SER   A 1 61  ? 12.271 -0.043  31.749 1.00 37.38  ? 67  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 61  ? 12.197 2.420   29.867 1.00 39.80  ? 67  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 61  ? 11.065 1.998   29.130 1.00 42.17  ? 67  SER   A OG  1 
ATOM   472  N  N   . ARG   A 1 62  ? 12.524 -1.006  29.714 1.00 36.34  ? 68  ARG   A N   1 
ATOM   473  C  CA  . ARG   A 1 62  ? 12.037 -2.321  30.131 1.00 36.51  ? 68  ARG   A CA  1 
ATOM   474  C  C   . ARG   A 1 62  ? 13.028 -3.452  29.844 1.00 38.66  ? 68  ARG   A C   1 
ATOM   475  O  O   . ARG   A 1 62  ? 12.666 -4.612  30.024 1.00 38.08  ? 68  ARG   A O   1 
ATOM   476  C  CB  . ARG   A 1 62  ? 10.735 -2.664  29.416 1.00 36.05  ? 68  ARG   A CB  1 
ATOM   477  C  CG  . ARG   A 1 62  ? 9.521  -1.899  29.908 1.00 38.19  ? 68  ARG   A CG  1 
ATOM   478  C  CD  . ARG   A 1 62  ? 9.105  -2.134  31.369 1.00 40.70  ? 68  ARG   A CD  1 
ATOM   479  N  NE  . ARG   A 1 62  ? 7.801  -1.499  31.593 1.00 41.70  ? 68  ARG   A NE  1 
ATOM   480  C  CZ  . ARG   A 1 62  ? 7.635  -0.214  31.878 1.00 44.27  ? 68  ARG   A CZ  1 
ATOM   481  N  NH1 . ARG   A 1 62  ? 8.688  0.571   32.084 1.00 44.83  ? 68  ARG   A NH1 1 
ATOM   482  N  NH2 . ARG   A 1 62  ? 6.415  0.300   31.957 1.00 45.97  ? 68  ARG   A NH2 1 
ATOM   483  N  N   . ARG   A 1 63  ? 14.224 -3.157  29.294 1.00 40.67  ? 69  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 63  ? 15.229 -4.178  28.927 1.00 41.40  ? 69  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 63  ? 14.641 -5.393  28.181 1.00 41.13  ? 69  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 63  ? 15.026 -6.556  28.432 1.00 41.30  ? 69  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 63  ? 16.000 -4.622  30.174 1.00 43.37  ? 69  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 63  ? 17.023 -3.607  30.631 1.00 48.82  ? 69  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 63  ? 17.910 -4.230  31.671 1.00 54.71  ? 69  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 63  ? 18.343 -3.245  32.652 1.00 61.55  ? 69  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 63  ? 18.341 -3.440  33.969 1.00 66.19  ? 69  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 63  ? 17.913 -4.592  34.479 1.00 66.03  ? 69  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 63  ? 18.746 -2.476  34.788 1.00 67.38  ? 69  ARG   A NH2 1 
ATOM   494  N  N   . LYS   A 1 64  ? 13.649 -5.116  27.307 1.00 39.60  ? 70  LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 64  ? 12.907 -6.149  26.576 1.00 38.08  ? 70  LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 64  ? 12.671 -5.688  25.136 1.00 35.92  ? 70  LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 64  ? 12.371 -4.500  24.917 1.00 36.00  ? 70  LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 64  ? 11.513 -6.377  27.246 1.00 38.83  ? 70  LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 64  ? 11.478 -7.407  28.379 1.00 41.30  ? 70  LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 64  ? 10.511 -6.998  29.545 1.00 44.86  ? 70  LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 64  ? 11.045 -7.269  30.967 1.00 48.09  ? 70  LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 64  ? 11.049 -6.046  31.857 1.00 47.71  ? 70  LYS   A NZ  1 
ATOM   503  N  N   . HIS   A 1 65  ? 12.759 -6.632  24.175 1.00 33.60  ? 71  HIS   A N   1 
ATOM   504  C  CA  . HIS   A 1 65  ? 12.437 -6.435  22.753 1.00 31.53  ? 71  HIS   A CA  1 
ATOM   505  C  C   . HIS   A 1 65  ? 10.931 -6.741  22.609 1.00 31.97  ? 71  HIS   A C   1 
ATOM   506  O  O   . HIS   A 1 65  ? 10.422 -7.671  23.263 1.00 32.13  ? 71  HIS   A O   1 
ATOM   507  C  CB  . HIS   A 1 65  ? 13.242 -7.389  21.845 1.00 30.37  ? 71  HIS   A CB  1 
ATOM   508  C  CG  . HIS   A 1 65  ? 14.739 -7.238  21.916 1.00 29.53  ? 71  HIS   A CG  1 
ATOM   509  N  ND1 . HIS   A 1 65  ? 15.446 -6.558  20.938 1.00 31.26  ? 71  HIS   A ND1 1 
ATOM   510  C  CD2 . HIS   A 1 65  ? 15.606 -7.653  22.868 1.00 30.71  ? 71  HIS   A CD2 1 
ATOM   511  C  CE1 . HIS   A 1 65  ? 16.712 -6.616  21.307 1.00 31.95  ? 71  HIS   A CE1 1 
ATOM   512  N  NE2 . HIS   A 1 65  ? 16.857 -7.255  22.473 1.00 32.00  ? 71  HIS   A NE2 1 
ATOM   513  N  N   . TYR   A 1 66  ? 10.210 -5.957  21.784 1.00 31.81  ? 72  TYR   A N   1 
ATOM   514  C  CA  . TYR   A 1 66  ? 8.761  -6.104  21.590 1.00 32.25  ? 72  TYR   A CA  1 
ATOM   515  C  C   . TYR   A 1 66  ? 8.353  -6.151  20.123 1.00 32.51  ? 72  TYR   A C   1 
ATOM   516  O  O   . TYR   A 1 66  ? 8.781  -5.321  19.328 1.00 32.49  ? 72  TYR   A O   1 
ATOM   517  C  CB  . TYR   A 1 66  ? 7.985  -4.900  22.201 1.00 32.46  ? 72  TYR   A CB  1 
ATOM   518  C  CG  . TYR   A 1 66  ? 7.981  -4.800  23.707 1.00 33.49  ? 72  TYR   A CG  1 
ATOM   519  C  CD1 . TYR   A 1 66  ? 7.218  -5.665  24.480 1.00 35.12  ? 72  TYR   A CD1 1 
ATOM   520  C  CD2 . TYR   A 1 66  ? 8.631  -3.762  24.354 1.00 34.98  ? 72  TYR   A CD2 1 
ATOM   521  C  CE1 . TYR   A 1 66  ? 7.199  -5.568  25.868 1.00 36.32  ? 72  TYR   A CE1 1 
ATOM   522  C  CE2 . TYR   A 1 66  ? 8.576  -3.624  25.737 1.00 36.28  ? 72  TYR   A CE2 1 
ATOM   523  C  CZ  . TYR   A 1 66  ? 7.882  -4.545  26.491 1.00 37.41  ? 72  TYR   A CZ  1 
ATOM   524  O  OH  . TYR   A 1 66  ? 7.845  -4.424  27.851 1.00 40.04  ? 72  TYR   A OH  1 
ATOM   525  N  N   . PRO   A 1 67  ? 7.410  -7.043  19.774 1.00 33.06  ? 73  PRO   A N   1 
ATOM   526  C  CA  . PRO   A 1 67  ? 6.857  -7.029  18.400 1.00 32.89  ? 73  PRO   A CA  1 
ATOM   527  C  C   . PRO   A 1 67  ? 5.765  -5.941  18.248 1.00 32.61  ? 73  PRO   A C   1 
ATOM   528  O  O   . PRO   A 1 67  ? 5.011  -5.698  19.201 1.00 33.60  ? 73  PRO   A O   1 
ATOM   529  C  CB  . PRO   A 1 67  ? 6.269  -8.441  18.227 1.00 33.66  ? 73  PRO   A CB  1 
ATOM   530  C  CG  . PRO   A 1 67  ? 6.336  -9.104  19.594 1.00 34.69  ? 73  PRO   A CG  1 
ATOM   531  C  CD  . PRO   A 1 67  ? 6.788  -8.091  20.612 1.00 33.20  ? 73  PRO   A CD  1 
ATOM   532  N  N   . VAL   A 1 68  ? 5.674  -5.276  17.067 1.00 31.41  ? 74  VAL   A N   1 
ATOM   533  C  CA  . VAL   A 1 68  ? 4.700  -4.181  16.801 1.00 30.08  ? 74  VAL   A CA  1 
ATOM   534  C  C   . VAL   A 1 68  ? 4.243  -4.115  15.340 1.00 29.44  ? 74  VAL   A C   1 
ATOM   535  O  O   . VAL   A 1 68  ? 5.006  -4.469  14.435 1.00 29.06  ? 74  VAL   A O   1 
ATOM   536  C  CB  . VAL   A 1 68  ? 5.266  -2.760  17.159 1.00 29.88  ? 74  VAL   A CB  1 
ATOM   537  C  CG1 . VAL   A 1 68  ? 5.405  -2.556  18.654 1.00 29.76  ? 74  VAL   A CG1 1 
ATOM   538  C  CG2 . VAL   A 1 68  ? 6.586  -2.480  16.453 1.00 29.63  ? 74  VAL   A CG2 1 
ATOM   539  N  N   . SER   A 1 69  ? 3.008  -3.614  15.126 1.00 27.89  ? 75  SER   A N   1 
ATOM   540  C  CA  . SER   A 1 69  ? 2.440  -3.256  13.844 1.00 27.70  ? 75  SER   A CA  1 
ATOM   541  C  C   . SER   A 1 69  ? 2.711  -1.754  13.821 1.00 27.78  ? 75  SER   A C   1 
ATOM   542  O  O   . SER   A 1 69  ? 2.534  -1.081  14.847 1.00 26.96  ? 75  SER   A O   1 
ATOM   543  C  CB  . SER   A 1 69  ? 0.929  -3.460  13.833 1.00 30.39  ? 75  SER   A CB  1 
ATOM   544  O  OG  . SER   A 1 69  ? 0.539  -4.750  13.395 1.00 33.41  ? 75  SER   A OG  1 
ATOM   545  N  N   . PHE   A 1 70  ? 3.144  -1.216  12.679 1.00 28.19  ? 76  PHE   A N   1 
ATOM   546  C  CA  . PHE   A 1 70  ? 3.460  0.200   12.612 1.00 29.45  ? 76  PHE   A CA  1 
ATOM   547  C  C   . PHE   A 1 70  ? 2.914  0.838   11.356 1.00 31.17  ? 76  PHE   A C   1 
ATOM   548  O  O   . PHE   A 1 70  ? 2.631  0.161   10.373 1.00 32.48  ? 76  PHE   A O   1 
ATOM   549  C  CB  . PHE   A 1 70  ? 4.961  0.463   12.831 1.00 29.62  ? 76  PHE   A CB  1 
ATOM   550  C  CG  . PHE   A 1 70  ? 5.928  -0.206  11.868 1.00 30.78  ? 76  PHE   A CG  1 
ATOM   551  C  CD1 . PHE   A 1 70  ? 6.489  -1.436  12.165 1.00 31.63  ? 76  PHE   A CD1 1 
ATOM   552  C  CD2 . PHE   A 1 70  ? 6.330  0.436   10.702 1.00 31.69  ? 76  PHE   A CD2 1 
ATOM   553  C  CE1 . PHE   A 1 70  ? 7.384  -2.037  11.280 1.00 32.64  ? 76  PHE   A CE1 1 
ATOM   554  C  CE2 . PHE   A 1 70  ? 7.232  -0.162  9.826  1.00 32.14  ? 76  PHE   A CE2 1 
ATOM   555  C  CZ  . PHE   A 1 70  ? 7.761  -1.389  10.122 1.00 31.96  ? 76  PHE   A CZ  1 
ATOM   556  N  N   . SER   A 1 71  ? 2.666  2.136   11.423 1.00 31.36  ? 77  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 71  ? 2.111  2.884   10.306 1.00 32.39  ? 77  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 71  ? 3.161  3.184   9.227  1.00 32.92  ? 77  SER   A C   1 
ATOM   559  O  O   . SER   A 1 71  ? 4.353  2.969   9.448  1.00 31.75  ? 77  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 71  ? 1.498  4.183   10.819 1.00 34.31  ? 77  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 71  ? 2.509  5.108   11.194 1.00 36.63  ? 77  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 72  ? 2.703  3.700   8.068  1.00 34.36  ? 78  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 72  ? 3.553  4.084   6.946  1.00 36.71  ? 78  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 72  ? 4.214  5.439   7.221  1.00 37.75  ? 78  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 72  ? 3.566  6.315   7.794  1.00 38.45  ? 78  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 72  ? 2.704  4.207   5.670  1.00 39.53  ? 78  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 72  ? 1.838  2.994   5.387  1.00 44.77  ? 78  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 72  ? 2.027  2.534   3.950  1.00 49.83  ? 78  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 72  ? 3.260  1.673   3.816  1.00 54.05  ? 78  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 72  ? 3.598  1.448   2.387  1.00 56.78  ? 78  LYS   A NZ  1 
ATOM   571  N  N   . PRO   A 1 73  ? 5.463  5.665   6.767  1.00 37.45  ? 79  PRO   A N   1 
ATOM   572  C  CA  . PRO   A 1 73  ? 6.109  6.967   7.016  1.00 37.75  ? 79  PRO   A CA  1 
ATOM   573  C  C   . PRO   A 1 73  ? 5.288  8.168   6.552  1.00 37.77  ? 79  PRO   A C   1 
ATOM   574  O  O   . PRO   A 1 73  ? 4.889  8.241   5.387  1.00 37.93  ? 79  PRO   A O   1 
ATOM   575  C  CB  . PRO   A 1 73  ? 7.440  6.853   6.269  1.00 38.37  ? 79  PRO   A CB  1 
ATOM   576  C  CG  . PRO   A 1 73  ? 7.725  5.371   6.219  1.00 38.67  ? 79  PRO   A CG  1 
ATOM   577  C  CD  . PRO   A 1 73  ? 6.362  4.739   6.049  1.00 37.03  ? 79  PRO   A CD  1 
ATOM   578  N  N   . SER   A 1 74  ? 5.032  9.107   7.475  1.00 37.87  ? 80  SER   A N   1 
ATOM   579  C  CA  . SER   A 1 74  ? 4.204  10.281  7.189  1.00 38.92  ? 80  SER   A CA  1 
ATOM   580  C  C   . SER   A 1 74  ? 4.460  11.496  8.130  1.00 38.90  ? 80  SER   A C   1 
ATOM   581  O  O   . SER   A 1 74  ? 5.280  11.412  9.046  1.00 38.63  ? 80  SER   A O   1 
ATOM   582  C  CB  . SER   A 1 74  ? 2.742  9.864   7.285  1.00 41.68  ? 80  SER   A CB  1 
ATOM   583  O  OG  . SER   A 1 74  ? 2.487  9.366   8.589  1.00 45.63  ? 80  SER   A OG  1 
ATOM   584  N  N   . LEU   A 1 75  ? 3.723  12.620  7.913  1.00 39.03  ? 81  LEU   A N   1 
ATOM   585  C  CA  . LEU   A 1 75  ? 3.797  13.837  8.728  1.00 39.77  ? 81  LEU   A CA  1 
ATOM   586  C  C   . LEU   A 1 75  ? 2.852  13.764  9.944  1.00 40.70  ? 81  LEU   A C   1 
ATOM   587  O  O   . LEU   A 1 75  ? 1.625  13.842  9.784  1.00 41.17  ? 81  LEU   A O   1 
ATOM   588  C  CB  . LEU   A 1 75  ? 3.407  15.065  7.898  1.00 39.82  ? 81  LEU   A CB  1 
ATOM   589  C  CG  . LEU   A 1 75  ? 4.520  15.739  7.107  1.00 41.32  ? 81  LEU   A CG  1 
ATOM   590  C  CD1 . LEU   A 1 75  ? 3.953  16.736  6.151  1.00 41.95  ? 81  LEU   A CD1 1 
ATOM   591  C  CD2 . LEU   A 1 75  ? 5.477  16.458  8.013  1.00 42.17  ? 81  LEU   A CD2 1 
ATOM   592  N  N   . ILE   A 1 76  ? 3.431  13.699  11.148 1.00 40.41  ? 82  ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 76  ? 2.715  13.660  12.409 1.00 41.38  ? 82  ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 76  ? 3.143  14.830  13.322 1.00 43.61  ? 82  ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 76  ? 4.337  15.118  13.426 1.00 43.77  ? 82  ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 76  ? 2.966  12.292  13.071 1.00 41.25  ? 82  ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 76  ? 2.314  11.145  12.256 1.00 41.70  ? 82  ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 76  ? 2.530  12.266  14.544 1.00 41.21  ? 82  ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 76  ? 3.028  9.882   12.386 1.00 42.62  ? 82  ILE   A CD1 1 
ATOM   600  N  N   . PHE   A 1 77  ? 2.170  15.500  13.975 1.00 44.65  ? 83  PHE   A N   1 
ATOM   601  C  CA  . PHE   A 1 77  ? 2.411  16.600  14.906 1.00 46.67  ? 83  PHE   A CA  1 
ATOM   602  C  C   . PHE   A 1 77  ? 3.049  16.137  16.237 1.00 46.70  ? 83  PHE   A C   1 
ATOM   603  O  O   . PHE   A 1 77  ? 2.532  15.238  16.909 1.00 46.61  ? 83  PHE   A O   1 
ATOM   604  C  CB  . PHE   A 1 77  ? 1.089  17.325  15.188 1.00 48.87  ? 83  PHE   A CB  1 
ATOM   605  C  CG  . PHE   A 1 77  ? 1.188  18.503  16.122 1.00 51.16  ? 83  PHE   A CG  1 
ATOM   606  C  CD1 . PHE   A 1 77  ? 1.589  19.743  15.658 1.00 52.88  ? 83  PHE   A CD1 1 
ATOM   607  C  CD2 . PHE   A 1 77  ? 0.851  18.377  17.457 1.00 52.84  ? 83  PHE   A CD2 1 
ATOM   608  C  CE1 . PHE   A 1 77  ? 1.610  20.846  16.510 1.00 54.28  ? 83  PHE   A CE1 1 
ATOM   609  C  CE2 . PHE   A 1 77  ? 0.843  19.491  18.299 1.00 54.20  ? 83  PHE   A CE2 1 
ATOM   610  C  CZ  . PHE   A 1 77  ? 1.242  20.710  17.825 1.00 53.85  ? 83  PHE   A CZ  1 
ATOM   611  N  N   . VAL   A 1 78  ? 4.164  16.772  16.623 1.00 46.61  ? 84  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 78  ? 4.907  16.460  17.841 1.00 46.99  ? 84  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 78  ? 4.913  17.681  18.773 1.00 48.60  ? 84  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 78  ? 5.215  18.806  18.342 1.00 48.50  ? 84  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 78  ? 6.344  15.927  17.521 1.00 46.30  ? 84  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 78  ? 7.111  15.569  18.784 1.00 46.37  ? 84  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 78  ? 6.283  14.726  16.597 1.00 46.22  ? 84  VAL   A CG2 1 
ATOM   618  N  N   . GLU   A 1 79  ? 4.542  17.442  20.049 1.00 49.72  ? 85  GLU   A N   1 
ATOM   619  C  CA  . GLU   A 1 79  ? 4.466  18.430  21.131 1.00 50.76  ? 85  GLU   A CA  1 
ATOM   620  C  C   . GLU   A 1 79  ? 5.785  19.158  21.339 1.00 50.71  ? 85  GLU   A C   1 
ATOM   621  O  O   . GLU   A 1 79  ? 6.855  18.586  21.103 1.00 50.48  ? 85  GLU   A O   1 
ATOM   622  C  CB  . GLU   A 1 79  ? 4.081  17.740  22.441 1.00 53.98  ? 85  GLU   A CB  1 
ATOM   623  C  CG  . GLU   A 1 79  ? 2.594  17.505  22.575 1.00 61.44  ? 85  GLU   A CG  1 
ATOM   624  C  CD  . GLU   A 1 79  ? 1.920  18.333  23.649 1.00 70.48  ? 85  GLU   A CD  1 
ATOM   625  O  OE1 . GLU   A 1 79  ? 2.228  19.543  23.777 1.00 71.31  ? 85  GLU   A OE1 1 
ATOM   626  O  OE2 . GLU   A 1 79  ? 1.059  17.766  24.358 1.00 75.19  ? 85  GLU   A OE2 1 
ATOM   627  N  N   . ALA   A 1 80  ? 5.712  20.396  21.831 1.00 50.87  ? 86  ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 80  ? 6.914  21.188  22.094 1.00 51.60  ? 86  ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 80  ? 7.758  20.514  23.181 1.00 52.30  ? 86  ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 80  ? 7.211  20.028  24.159 1.00 52.97  ? 86  ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 80  ? 6.531  22.596  22.530 1.00 51.40  ? 86  ALA   A CB  1 
ATOM   632  N  N   . SER   A 1 81  ? 9.067  20.420  22.961 1.00 52.27  ? 87  SER   A N   1 
ATOM   633  C  CA  . SER   A 1 81  ? 10.043 19.845  23.882 1.00 52.11  ? 87  SER   A CA  1 
ATOM   634  C  C   . SER   A 1 81  ? 11.182 20.871  24.120 1.00 52.45  ? 87  SER   A C   1 
ATOM   635  O  O   . SER   A 1 81  ? 11.220 21.929  23.478 1.00 52.80  ? 87  SER   A O   1 
ATOM   636  C  CB  . SER   A 1 81  ? 10.614 18.557  23.286 1.00 52.73  ? 87  SER   A CB  1 
ATOM   637  O  OG  . SER   A 1 81  ? 11.429 18.802  22.149 1.00 53.89  ? 87  SER   A OG  1 
ATOM   638  N  N   . GLU   A 1 82  ? 12.121 20.558  25.017 1.00 52.14  ? 88  GLU   A N   1 
ATOM   639  C  CA  . GLU   A 1 82  ? 13.280 21.419  25.250 1.00 52.55  ? 88  GLU   A CA  1 
ATOM   640  C  C   . GLU   A 1 82  ? 14.219 21.483  24.033 1.00 51.50  ? 88  GLU   A C   1 
ATOM   641  O  O   . GLU   A 1 82  ? 15.101 22.341  24.009 1.00 51.96  ? 88  GLU   A O   1 
ATOM   642  C  CB  . GLU   A 1 82  ? 14.065 20.934  26.477 1.00 56.64  ? 88  GLU   A CB  1 
ATOM   643  C  CG  . GLU   A 1 82  ? 14.384 19.448  26.423 1.00 64.08  ? 88  GLU   A CG  1 
ATOM   644  C  CD  . GLU   A 1 82  ? 14.370 18.740  27.762 1.00 73.61  ? 88  GLU   A CD  1 
ATOM   645  O  OE1 . GLU   A 1 82  ? 13.577 19.145  28.644 1.00 76.21  ? 88  GLU   A OE1 1 
ATOM   646  O  OE2 . GLU   A 1 82  ? 15.159 17.781  27.931 1.00 76.48  ? 88  GLU   A OE2 1 
ATOM   647  N  N   . TYR   A 1 83  ? 14.049 20.571  23.035 1.00 49.94  ? 89  TYR   A N   1 
ATOM   648  C  CA  . TYR   A 1 83  ? 14.876 20.505  21.829 1.00 48.10  ? 89  TYR   A CA  1 
ATOM   649  C  C   . TYR   A 1 83  ? 14.186 21.174  20.639 1.00 45.69  ? 89  TYR   A C   1 
ATOM   650  O  O   . TYR   A 1 83  ? 14.862 21.782  19.826 1.00 45.79  ? 89  TYR   A O   1 
ATOM   651  C  CB  . TYR   A 1 83  ? 15.237 19.040  21.463 1.00 48.00  ? 89  TYR   A CB  1 
ATOM   652  C  CG  . TYR   A 1 83  ? 15.710 18.219  22.638 1.00 48.87  ? 89  TYR   A CG  1 
ATOM   653  C  CD1 . TYR   A 1 83  ? 17.018 18.306  23.090 1.00 49.94  ? 89  TYR   A CD1 1 
ATOM   654  C  CD2 . TYR   A 1 83  ? 14.838 17.389  23.327 1.00 49.91  ? 89  TYR   A CD2 1 
ATOM   655  C  CE1 . TYR   A 1 83  ? 17.448 17.588  24.205 1.00 50.99  ? 89  TYR   A CE1 1 
ATOM   656  C  CE2 . TYR   A 1 83  ? 15.261 16.647  24.423 1.00 50.91  ? 89  TYR   A CE2 1 
ATOM   657  C  CZ  . TYR   A 1 83  ? 16.562 16.760  24.871 1.00 52.08  ? 89  TYR   A CZ  1 
ATOM   658  O  OH  . TYR   A 1 83  ? 16.971 16.020  25.961 1.00 53.94  ? 89  TYR   A OH  1 
ATOM   659  N  N   . TYR   A 1 84  ? 12.865 21.024  20.504 1.00 43.92  ? 90  TYR   A N   1 
ATOM   660  C  CA  . TYR   A 1 84  ? 12.148 21.605  19.370 1.00 43.18  ? 90  TYR   A CA  1 
ATOM   661  C  C   . TYR   A 1 84  ? 10.862 22.298  19.789 1.00 44.00  ? 90  TYR   A C   1 
ATOM   662  O  O   . TYR   A 1 84  ? 10.190 21.832  20.701 1.00 43.45  ? 90  TYR   A O   1 
ATOM   663  C  CB  . TYR   A 1 84  ? 11.727 20.498  18.381 1.00 41.85  ? 90  TYR   A CB  1 
ATOM   664  C  CG  . TYR   A 1 84  ? 12.817 19.586  17.870 1.00 40.30  ? 90  TYR   A CG  1 
ATOM   665  C  CD1 . TYR   A 1 84  ? 12.929 18.279  18.330 1.00 39.77  ? 90  TYR   A CD1 1 
ATOM   666  C  CD2 . TYR   A 1 84  ? 13.672 19.992  16.853 1.00 39.89  ? 90  TYR   A CD2 1 
ATOM   667  C  CE1 . TYR   A 1 84  ? 13.893 17.419  17.832 1.00 39.85  ? 90  TYR   A CE1 1 
ATOM   668  C  CE2 . TYR   A 1 84  ? 14.638 19.136  16.343 1.00 39.63  ? 90  TYR   A CE2 1 
ATOM   669  C  CZ  . TYR   A 1 84  ? 14.742 17.846  16.830 1.00 39.92  ? 90  TYR   A CZ  1 
ATOM   670  O  OH  . TYR   A 1 84  ? 15.712 16.999  16.344 1.00 39.54  ? 90  TYR   A OH  1 
ATOM   671  N  N   . PRO   A 1 85  ? 10.428 23.332  19.044 1.00 45.05  ? 91  PRO   A N   1 
ATOM   672  C  CA  . PRO   A 1 85  ? 9.079  23.883  19.294 1.00 45.62  ? 91  PRO   A CA  1 
ATOM   673  C  C   . PRO   A 1 85  ? 8.003  22.930  18.709 1.00 44.82  ? 91  PRO   A C   1 
ATOM   674  O  O   . PRO   A 1 85  ? 8.337  21.988  17.984 1.00 43.33  ? 91  PRO   A O   1 
ATOM   675  C  CB  . PRO   A 1 85  ? 9.106  25.226  18.555 1.00 47.03  ? 91  PRO   A CB  1 
ATOM   676  C  CG  . PRO   A 1 85  ? 10.115 25.017  17.438 1.00 46.90  ? 91  PRO   A CG  1 
ATOM   677  C  CD  . PRO   A 1 85  ? 11.093 23.962  17.877 1.00 44.96  ? 91  PRO   A CD  1 
ATOM   678  N  N   . ALA   A 1 86  ? 6.709  23.172  18.999 1.00 44.91  ? 92  ALA   A N   1 
ATOM   679  C  CA  . ALA   A 1 86  ? 5.637  22.316  18.462 1.00 45.02  ? 92  ALA   A CA  1 
ATOM   680  C  C   . ALA   A 1 86  ? 5.652  22.347  16.910 1.00 44.40  ? 92  ALA   A C   1 
ATOM   681  O  O   . ALA   A 1 86  ? 5.690  23.420  16.300 1.00 43.95  ? 92  ALA   A O   1 
ATOM   682  C  CB  . ALA   A 1 86  ? 4.295  22.733  19.014 1.00 45.81  ? 92  ALA   A CB  1 
ATOM   683  N  N   . ARG   A 1 87  ? 5.812  21.156  16.289 1.00 43.26  ? 93  ARG   A N   1 
ATOM   684  C  CA  . ARG   A 1 87  ? 5.965  21.085  14.836 1.00 41.34  ? 93  ARG   A CA  1 
ATOM   685  C  C   . ARG   A 1 87  ? 5.445  19.774  14.228 1.00 40.54  ? 93  ARG   A C   1 
ATOM   686  O  O   . ARG   A 1 87  ? 5.066  18.867  14.964 1.00 41.05  ? 93  ARG   A O   1 
ATOM   687  C  CB  . ARG   A 1 87  ? 7.452  21.290  14.510 1.00 40.36  ? 93  ARG   A CB  1 
ATOM   688  C  CG  . ARG   A 1 87  ? 8.297  19.997  14.608 1.00 38.71  ? 93  ARG   A CG  1 
ATOM   689  C  CD  . ARG   A 1 87  ? 9.647  20.166  15.235 1.00 37.54  ? 93  ARG   A CD  1 
ATOM   690  N  NE  . ARG   A 1 87  ? 10.577 19.102  14.810 1.00 35.68  ? 93  ARG   A NE  1 
ATOM   691  C  CZ  . ARG   A 1 87  ? 10.673 17.911  15.391 1.00 35.30  ? 93  ARG   A CZ  1 
ATOM   692  N  NH1 . ARG   A 1 87  ? 11.546 17.014  14.944 1.00 33.61  ? 93  ARG   A NH1 1 
ATOM   693  N  NH2 . ARG   A 1 87  ? 9.915  17.612  16.438 1.00 33.13  ? 93  ARG   A NH2 1 
ATOM   694  N  N   . TYR   A 1 88  ? 5.418  19.671  12.893 1.00 39.79  ? 94  TYR   A N   1 
ATOM   695  C  CA  . TYR   A 1 88  ? 5.113  18.406  12.231 1.00 39.54  ? 94  TYR   A CA  1 
ATOM   696  C  C   . TYR   A 1 88  ? 6.453  17.755  11.994 1.00 35.73  ? 94  TYR   A C   1 
ATOM   697  O  O   . TYR   A 1 88  ? 7.320  18.373  11.376 1.00 35.15  ? 94  TYR   A O   1 
ATOM   698  C  CB  . TYR   A 1 88  ? 4.530  18.595  10.834 1.00 41.41  ? 94  TYR   A CB  1 
ATOM   699  C  CG  . TYR   A 1 88  ? 3.080  19.016  10.778 1.00 44.89  ? 94  TYR   A CG  1 
ATOM   700  C  CD1 . TYR   A 1 88  ? 2.067  18.140  11.145 1.00 46.45  ? 94  TYR   A CD1 1 
ATOM   701  C  CD2 . TYR   A 1 88  ? 2.715  20.232  10.216 1.00 46.88  ? 94  TYR   A CD2 1 
ATOM   702  C  CE1 . TYR   A 1 88  ? 0.725  18.495  11.015 1.00 48.38  ? 94  TYR   A CE1 1 
ATOM   703  C  CE2 . TYR   A 1 88  ? 1.386  20.597  10.083 1.00 48.48  ? 94  TYR   A CE2 1 
ATOM   704  C  CZ  . TYR   A 1 88  ? 0.390  19.728  10.484 1.00 49.70  ? 94  TYR   A CZ  1 
ATOM   705  O  OH  . TYR   A 1 88  ? -0.919 20.135  10.353 1.00 52.11  ? 94  TYR   A OH  1 
ATOM   706  N  N   . GLN   A 1 89  ? 6.612  16.507  12.401 1.00 33.39  ? 95  GLN   A N   1 
ATOM   707  C  CA  . GLN   A 1 89  ? 7.846  15.767  12.095 1.00 31.38  ? 95  GLN   A CA  1 
ATOM   708  C  C   . GLN   A 1 89  ? 7.543  14.829  10.924 1.00 31.12  ? 95  GLN   A C   1 
ATOM   709  O  O   . GLN   A 1 89  ? 6.544  14.088  10.945 1.00 31.19  ? 95  GLN   A O   1 
ATOM   710  C  CB  . GLN   A 1 89  ? 8.398  15.010  13.308 1.00 30.79  ? 95  GLN   A CB  1 
ATOM   711  C  CG  . GLN   A 1 89  ? 9.637  14.134  12.971 1.00 29.75  ? 95  GLN   A CG  1 
ATOM   712  C  CD  . GLN   A 1 89  ? 10.291 13.613  14.220 1.00 31.55  ? 95  GLN   A CD  1 
ATOM   713  O  OE1 . GLN   A 1 89  ? 10.383 14.316  15.236 1.00 32.09  ? 95  GLN   A OE1 1 
ATOM   714  N  NE2 . GLN   A 1 89  ? 10.757 12.359  14.179 1.00 31.99  ? 95  GLN   A NE2 1 
ATOM   715  N  N   . SER   A 1 90  ? 8.366  14.902  9.875  1.00 30.15  ? 96  SER   A N   1 
ATOM   716  C  CA  . SER   A 1 90  ? 8.177  14.093  8.664  1.00 30.15  ? 96  SER   A CA  1 
ATOM   717  C  C   . SER   A 1 90  ? 8.881  12.730  8.758  1.00 30.45  ? 96  SER   A C   1 
ATOM   718  O  O   . SER   A 1 90  ? 9.834  12.587  9.539  1.00 30.92  ? 96  SER   A O   1 
ATOM   719  C  CB  . SER   A 1 90  ? 8.701  14.849  7.450  1.00 31.03  ? 96  SER   A CB  1 
ATOM   720  O  OG  . SER   A 1 90  ? 10.115 14.981  7.506  1.00 33.49  ? 96  SER   A OG  1 
ATOM   721  N  N   . HIS   A 1 91  ? 8.437  11.749  7.934  1.00 29.22  ? 97  HIS   A N   1 
ATOM   722  C  CA  . HIS   A 1 91  ? 9.017  10.402  7.869  1.00 28.77  ? 97  HIS   A CA  1 
ATOM   723  C  C   . HIS   A 1 91  ? 8.890  9.672   9.222  1.00 28.62  ? 97  HIS   A C   1 
ATOM   724  O  O   . HIS   A 1 91  ? 9.767  8.926   9.601  1.00 28.11  ? 97  HIS   A O   1 
ATOM   725  C  CB  . HIS   A 1 91  ? 10.474 10.413  7.354  1.00 29.15  ? 97  HIS   A CB  1 
ATOM   726  C  CG  . HIS   A 1 91  ? 10.663 11.043  5.994  1.00 31.17  ? 97  HIS   A CG  1 
ATOM   727  N  ND1 . HIS   A 1 91  ? 10.911 10.273  4.864  1.00 33.01  ? 97  HIS   A ND1 1 
ATOM   728  C  CD2 . HIS   A 1 91  ? 10.603 12.346  5.617  1.00 31.33  ? 97  HIS   A CD2 1 
ATOM   729  C  CE1 . HIS   A 1 91  ? 11.026 11.132  3.856  1.00 32.34  ? 97  HIS   A CE1 1 
ATOM   730  N  NE2 . HIS   A 1 91  ? 10.823 12.382  4.256  1.00 32.04  ? 97  HIS   A NE2 1 
ATOM   731  N  N   . LEU   A 1 92  ? 7.795  9.909   9.945  1.00 29.24  ? 98  LEU   A N   1 
ATOM   732  C  CA  . LEU   A 1 92  ? 7.580  9.280   11.255 1.00 29.70  ? 98  LEU   A CA  1 
ATOM   733  C  C   . LEU   A 1 92  ? 6.611  8.124   11.171 1.00 29.12  ? 98  LEU   A C   1 
ATOM   734  O  O   . LEU   A 1 92  ? 5.544  8.301   10.584 1.00 29.88  ? 98  LEU   A O   1 
ATOM   735  C  CB  . LEU   A 1 92  ? 7.021  10.333  12.226 1.00 29.54  ? 98  LEU   A CB  1 
ATOM   736  C  CG  . LEU   A 1 92  ? 6.924  9.921   13.694 1.00 30.60  ? 98  LEU   A CG  1 
ATOM   737  C  CD1 . LEU   A 1 92  ? 8.283  9.617   14.254 1.00 30.85  ? 98  LEU   A CD1 1 
ATOM   738  C  CD2 . LEU   A 1 92  ? 6.195  11.032  14.546 1.00 31.58  ? 98  LEU   A CD2 1 
ATOM   739  N  N   . MET   A 1 93  ? 6.931  6.970   11.820 1.00 28.22  ? 99  MET   A N   1 
ATOM   740  C  CA  . MET   A 1 93  ? 6.040  5.787   11.894 1.00 27.26  ? 99  MET   A CA  1 
ATOM   741  C  C   . MET   A 1 93  ? 5.508  5.528   13.333 1.00 28.17  ? 99  MET   A C   1 
ATOM   742  O  O   . MET   A 1 93  ? 6.311  5.424   14.259 1.00 28.94  ? 99  MET   A O   1 
ATOM   743  C  CB  . MET   A 1 93  ? 6.750  4.529   11.349 1.00 26.09  ? 99  MET   A CB  1 
ATOM   744  C  CG  . MET   A 1 93  ? 7.280  4.712   9.930  1.00 26.36  ? 99  MET   A CG  1 
ATOM   745  S  SD  . MET   A 1 93  ? 8.410  3.404   9.352  1.00 32.34  ? 99  MET   A SD  1 
ATOM   746  C  CE  . MET   A 1 93  ? 9.724  3.530   10.528 1.00 33.38  ? 99  MET   A CE  1 
ATOM   747  N  N   . LEU   A 1 94  ? 4.175  5.370   13.527 1.00 27.41  ? 100 LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 94  ? 3.627  5.111   14.862 1.00 27.41  ? 100 LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 94  ? 3.173  3.649   15.119 1.00 27.60  ? 100 LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 94  ? 2.700  2.971   14.209 1.00 25.58  ? 100 LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 94  ? 2.470  6.069   15.237 1.00 27.62  ? 100 LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 94  ? 2.731  7.603   15.306 1.00 29.23  ? 100 LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 94  ? 1.622  8.293   16.123 1.00 30.76  ? 100 LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 94  ? 4.013  7.933   16.005 1.00 28.91  ? 100 LEU   A CD2 1 
ATOM   755  N  N   . ALA   A 1 95  ? 3.273  3.212   16.396 1.00 29.27  ? 101 ALA   A N   1 
ATOM   756  C  CA  . ALA   A 1 95  ? 2.873  1.891   16.891 1.00 31.57  ? 101 ALA   A CA  1 
ATOM   757  C  C   . ALA   A 1 95  ? 2.370  1.956   18.345 1.00 34.07  ? 101 ALA   A C   1 
ATOM   758  O  O   . ALA   A 1 95  ? 2.743  2.860   19.100 1.00 34.69  ? 101 ALA   A O   1 
ATOM   759  C  CB  . ALA   A 1 95  ? 4.070  0.950   16.836 1.00 31.93  ? 101 ALA   A CB  1 
ATOM   760  N  N   . VAL   A 1 96  ? 1.521  0.992   18.738 1.00 35.11  ? 102 VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 96  ? 1.064  0.811   20.112 1.00 36.44  ? 102 VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 96  ? 2.225  0.077   20.820 1.00 37.50  ? 102 VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 96  ? 2.744  -0.934  20.320 1.00 37.70  ? 102 VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 96  ? -0.260 -0.019  20.200 1.00 37.47  ? 102 VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 96  ? -0.636 -0.319  21.651 1.00 38.34  ? 102 VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 96  ? -1.417 0.679   19.483 1.00 37.62  ? 102 VAL   A CG2 1 
ATOM   767  N  N   . GLY   A 1 97  ? 2.678  0.641   21.922 1.00 38.26  ? 103 GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 97  ? 3.801  0.088   22.657 1.00 39.34  ? 103 GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 97  ? 4.457  1.103   23.565 1.00 39.95  ? 103 GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 97  ? 4.471  2.298   23.274 1.00 40.75  ? 103 GLY   A O   1 
ATOM   771  N  N   . HIS   A 1 98  ? 5.000  0.622   24.672 1.00 39.53  ? 104 HIS   A N   1 
ATOM   772  C  CA  . HIS   A 1 98  ? 5.644  1.442   25.667 1.00 40.66  ? 104 HIS   A CA  1 
ATOM   773  C  C   . HIS   A 1 98  ? 6.956  2.146   25.224 1.00 40.32  ? 104 HIS   A C   1 
ATOM   774  O  O   . HIS   A 1 98  ? 7.865  1.521   24.713 1.00 40.22  ? 104 HIS   A O   1 
ATOM   775  C  CB  . HIS   A 1 98  ? 5.886  0.604   26.936 1.00 42.09  ? 104 HIS   A CB  1 
ATOM   776  C  CG  . HIS   A 1 98  ? 6.621  1.331   28.019 1.00 46.18  ? 104 HIS   A CG  1 
ATOM   777  N  ND1 . HIS   A 1 98  ? 6.050  2.388   28.695 1.00 48.70  ? 104 HIS   A ND1 1 
ATOM   778  C  CD2 . HIS   A 1 98  ? 7.857  1.108   28.522 1.00 47.90  ? 104 HIS   A CD2 1 
ATOM   779  C  CE1 . HIS   A 1 98  ? 6.956  2.786   29.573 1.00 48.84  ? 104 HIS   A CE1 1 
ATOM   780  N  NE2 . HIS   A 1 98  ? 8.062  2.048   29.500 1.00 48.60  ? 104 HIS   A NE2 1 
ATOM   781  N  N   . SER   A 1 99  ? 7.065  3.437   25.546 1.00 40.44  ? 105 SER   A N   1 
ATOM   782  C  CA  . SER   A 1 99  ? 8.270  4.236   25.381 1.00 41.05  ? 105 SER   A CA  1 
ATOM   783  C  C   . SER   A 1 99  ? 8.324  5.367   26.420 1.00 41.86  ? 105 SER   A C   1 
ATOM   784  O  O   . SER   A 1 99  ? 7.296  5.924   26.806 1.00 41.37  ? 105 SER   A O   1 
ATOM   785  C  CB  . SER   A 1 99  ? 8.429  4.774   23.964 1.00 41.64  ? 105 SER   A CB  1 
ATOM   786  O  OG  . SER   A 1 99  ? 7.231  5.288   23.417 1.00 43.82  ? 105 SER   A OG  1 
ATOM   787  N  N   . GLU   A 1 100 ? 9.539  5.668   26.875 1.00 42.28  ? 106 GLU   A N   1 
ATOM   788  C  CA  . GLU   A 1 100 ? 9.910  6.736   27.803 1.00 42.92  ? 106 GLU   A CA  1 
ATOM   789  C  C   . GLU   A 1 100 ? 11.026 7.562   27.122 1.00 43.76  ? 106 GLU   A C   1 
ATOM   790  O  O   . GLU   A 1 100 ? 11.684 7.040   26.219 1.00 45.04  ? 106 GLU   A O   1 
ATOM   791  C  CB  . GLU   A 1 100 ? 10.396 6.148   29.141 1.00 45.32  ? 106 GLU   A CB  1 
ATOM   792  C  CG  . GLU   A 1 100 ? 9.277  5.515   29.948 1.00 49.22  ? 106 GLU   A CG  1 
ATOM   793  C  CD  . GLU   A 1 100 ? 9.658  4.942   31.301 1.00 52.28  ? 106 GLU   A CD  1 
ATOM   794  O  OE1 . GLU   A 1 100 ? 10.551 5.511   31.965 1.00 51.49  ? 106 GLU   A OE1 1 
ATOM   795  O  OE2 . GLU   A 1 100 ? 9.068  3.912   31.692 1.00 52.90  ? 106 GLU   A OE2 1 
ATOM   796  N  N   . PRO   A 1 101 ? 11.254 8.849   27.481 1.00 43.28  ? 107 PRO   A N   1 
ATOM   797  C  CA  . PRO   A 1 101 ? 12.270 9.651   26.769 1.00 42.47  ? 107 PRO   A CA  1 
ATOM   798  C  C   . PRO   A 1 101 ? 13.644 9.019   26.564 1.00 41.91  ? 107 PRO   A C   1 
ATOM   799  O  O   . PRO   A 1 101 ? 14.195 9.159   25.482 1.00 42.10  ? 107 PRO   A O   1 
ATOM   800  C  CB  . PRO   A 1 101 ? 12.363 10.909  27.616 1.00 42.94  ? 107 PRO   A CB  1 
ATOM   801  C  CG  . PRO   A 1 101 ? 10.993 11.086  28.124 1.00 43.83  ? 107 PRO   A CG  1 
ATOM   802  C  CD  . PRO   A 1 101 ? 10.531 9.680   28.463 1.00 42.69  ? 107 PRO   A CD  1 
ATOM   803  N  N   . GLY   A 1 102 ? 14.168 8.304   27.568 1.00 41.04  ? 108 GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 102 ? 15.450 7.596   27.466 1.00 39.49  ? 108 GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 102 ? 15.495 6.446   26.463 1.00 36.80  ? 108 GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 102 ? 16.555 5.866   26.216 1.00 37.39  ? 108 GLY   A O   1 
ATOM   807  N  N   . ASP   A 1 103 ? 14.351 6.100   25.874 1.00 33.90  ? 109 ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 103 ? 14.256 5.030   24.895 1.00 31.60  ? 109 ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 103 ? 14.576 5.458   23.471 1.00 29.42  ? 109 ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 103 ? 14.654 4.585   22.607 1.00 28.73  ? 109 ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 103 ? 12.853 4.444   24.885 1.00 32.12  ? 109 ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 103 ? 12.567 3.564   26.066 1.00 33.17  ? 109 ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 103 ? 13.471 2.835   26.490 1.00 29.70  ? 109 ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 103 ? 11.443 3.622   26.577 1.00 37.40  ? 109 ASP   A OD2 1 
ATOM   815  N  N   . CYS   A 1 104 ? 14.713 6.783   23.189 1.00 28.08  ? 110 CYS   A N   1 
ATOM   816  C  CA  . CYS   A 1 104 ? 15.063 7.273   21.818 1.00 27.49  ? 110 CYS   A CA  1 
ATOM   817  C  C   . CYS   A 1 104 ? 16.384 6.642   21.376 1.00 27.10  ? 110 CYS   A C   1 
ATOM   818  O  O   . CYS   A 1 104 ? 17.321 6.685   22.157 1.00 28.56  ? 110 CYS   A O   1 
ATOM   819  C  CB  . CYS   A 1 104 ? 15.169 8.795   21.790 1.00 28.11  ? 110 CYS   A CB  1 
ATOM   820  S  SG  . CYS   A 1 104 ? 13.583 9.653   21.820 1.00 33.82  ? 110 CYS   A SG  1 
ATOM   821  N  N   . GLY   A 1 105 ? 16.461 6.071   20.176 1.00 25.92  ? 111 GLY   A N   1 
ATOM   822  C  CA  . GLY   A 1 105 ? 17.704 5.441   19.726 1.00 25.86  ? 111 GLY   A CA  1 
ATOM   823  C  C   . GLY   A 1 105 ? 17.639 3.927   19.616 1.00 25.92  ? 111 GLY   A C   1 
ATOM   824  O  O   . GLY   A 1 105 ? 18.438 3.318   18.907 1.00 28.03  ? 111 GLY   A O   1 
ATOM   825  N  N   . GLY   A 1 106 ? 16.674 3.301   20.277 1.00 23.97  ? 112 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 106 ? 16.445 1.868   20.153 1.00 23.59  ? 112 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 106 ? 16.011 1.542   18.738 1.00 22.49  ? 112 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 106 ? 15.251 2.292   18.140 1.00 20.62  ? 112 GLY   A O   1 
ATOM   829  N  N   . ILE   A 1 107 ? 16.554 0.461   18.166 1.00 22.84  ? 113 ILE   A N   1 
ATOM   830  C  CA  . ILE   A 1 107 ? 16.306 0.078   16.782 1.00 23.99  ? 113 ILE   A CA  1 
ATOM   831  C  C   . ILE   A 1 107 ? 15.010 -0.699  16.579 1.00 23.22  ? 113 ILE   A C   1 
ATOM   832  O  O   . ILE   A 1 107 ? 14.663 -1.552  17.411 1.00 23.90  ? 113 ILE   A O   1 
ATOM   833  C  CB  . ILE   A 1 107 ? 17.548 -0.750  16.316 1.00 26.12  ? 113 ILE   A CB  1 
ATOM   834  C  CG1 . ILE   A 1 107 ? 18.789 0.153   16.127 1.00 28.54  ? 113 ILE   A CG1 1 
ATOM   835  C  CG2 . ILE   A 1 107 ? 17.272 -1.612  15.092 1.00 26.96  ? 113 ILE   A CG2 1 
ATOM   836  C  CD1 . ILE   A 1 107 ? 20.083 -0.566  15.848 1.00 30.16  ? 113 ILE   A CD1 1 
ATOM   837  N  N   . LEU   A 1 108 ? 14.356 -0.453  15.427 1.00 22.16  ? 114 LEU   A N   1 
ATOM   838  C  CA  . LEU   A 1 108 ? 13.212 -1.174  14.889 1.00 23.07  ? 114 LEU   A CA  1 
ATOM   839  C  C   . LEU   A 1 108 ? 13.735 -2.009  13.696 1.00 24.34  ? 114 LEU   A C   1 
ATOM   840  O  O   . LEU   A 1 108 ? 14.484 -1.519  12.857 1.00 21.74  ? 114 LEU   A O   1 
ATOM   841  C  CB  . LEU   A 1 108 ? 12.118 -0.224  14.412 1.00 22.95  ? 114 LEU   A CB  1 
ATOM   842  C  CG  . LEU   A 1 108 ? 10.925 -0.898  13.699 1.00 24.34  ? 114 LEU   A CG  1 
ATOM   843  C  CD1 . LEU   A 1 108 ? 10.137 -1.731  14.643 1.00 24.32  ? 114 LEU   A CD1 1 
ATOM   844  C  CD2 . LEU   A 1 108 ? 9.984  0.177   13.094 1.00 25.70  ? 114 LEU   A CD2 1 
ATOM   845  N  N   . ARG   A 1 109 ? 13.381 -3.300  13.661 1.00 26.49  ? 115 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 109 ? 13.839 -4.213  12.632 1.00 27.37  ? 115 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 109 ? 12.703 -5.065  12.130 1.00 29.04  ? 115 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 109 ? 11.873 -5.467  12.912 1.00 29.17  ? 115 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 109 ? 14.832 -5.221  13.234 1.00 29.59  ? 115 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 109 ? 16.156 -4.663  13.674 1.00 35.20  ? 115 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 109 ? 17.028 -5.766  14.232 1.00 39.28  ? 115 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 109 ? 17.589 -6.532  13.129 1.00 41.88  ? 115 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 109 ? 18.822 -6.383  12.660 1.00 45.31  ? 115 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 109 ? 19.232 -7.099  11.624 1.00 45.40  ? 115 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 109 ? 19.674 -5.562  13.261 1.00 46.01  ? 115 ARG   A NH2 1 
ATOM   856  N  N   . CYS   A 1 110 ? 12.758 -5.470  10.861 1.00 30.37  ? 116 CYS   A N   1 
ATOM   857  C  CA  . CYS   A 1 110 ? 11.877 -6.453  10.239 1.00 31.83  ? 116 CYS   A CA  1 
ATOM   858  C  C   . CYS   A 1 110 ? 12.810 -7.601  9.747  1.00 33.55  ? 116 CYS   A C   1 
ATOM   859  O  O   . CYS   A 1 110 ? 14.017 -7.556  10.011 1.00 32.85  ? 116 CYS   A O   1 
ATOM   860  C  CB  . CYS   A 1 110 ? 11.102 -5.819  9.085  1.00 32.85  ? 116 CYS   A CB  1 
ATOM   861  S  SG  . CYS   A 1 110 ? 12.139 -5.254  7.717  1.00 36.09  ? 116 CYS   A SG  1 
ATOM   862  N  N   . GLN   A 1 111 ? 12.286 -8.620  9.046  1.00 35.67  ? 117 GLN   A N   1 
ATOM   863  C  CA  . GLN   A 1 111 ? 13.141 -9.699  8.500  1.00 37.83  ? 117 GLN   A CA  1 
ATOM   864  C  C   . GLN   A 1 111 ? 14.137 -9.212  7.421  1.00 39.34  ? 117 GLN   A C   1 
ATOM   865  O  O   . GLN   A 1 111 ? 14.967 -9.999  6.965  1.00 39.93  ? 117 GLN   A O   1 
ATOM   866  C  CB  . GLN   A 1 111 ? 12.267 -10.784 7.879  1.00 39.64  ? 117 GLN   A CB  1 
ATOM   867  C  CG  . GLN   A 1 111 ? 11.432 -10.258 6.727  1.00 44.91  ? 117 GLN   A CG  1 
ATOM   868  C  CD  . GLN   A 1 111 ? 10.725 -11.382 6.034  1.00 52.20  ? 117 GLN   A CD  1 
ATOM   869  O  OE1 . GLN   A 1 111 ? 9.501  -11.518 6.135  1.00 55.72  ? 117 GLN   A OE1 1 
ATOM   870  N  NE2 . GLN   A 1 111 ? 11.479 -12.217 5.317  1.00 51.77  ? 117 GLN   A NE2 1 
ATOM   871  N  N   . HIS   A 1 112 ? 14.016 -7.955  6.953  1.00 39.69  ? 118 HIS   A N   1 
ATOM   872  C  CA  . HIS   A 1 112 ? 14.922 -7.436  5.916  1.00 39.74  ? 118 HIS   A CA  1 
ATOM   873  C  C   . HIS   A 1 112 ? 16.082 -6.582  6.463  1.00 37.02  ? 118 HIS   A C   1 
ATOM   874  O  O   . HIS   A 1 112 ? 16.988 -6.223  5.706  1.00 36.84  ? 118 HIS   A O   1 
ATOM   875  C  CB  . HIS   A 1 112 ? 14.156 -6.623  4.851  1.00 43.00  ? 118 HIS   A CB  1 
ATOM   876  C  CG  . HIS   A 1 112 ? 12.957 -7.315  4.272  1.00 48.12  ? 118 HIS   A CG  1 
ATOM   877  N  ND1 . HIS   A 1 112 ? 11.675 -6.862  4.522  1.00 50.56  ? 118 HIS   A ND1 1 
ATOM   878  C  CD2 . HIS   A 1 112 ? 12.886 -8.394  3.458  1.00 50.65  ? 118 HIS   A CD2 1 
ATOM   879  C  CE1 . HIS   A 1 112 ? 10.866 -7.669  3.847  1.00 51.55  ? 118 HIS   A CE1 1 
ATOM   880  N  NE2 . HIS   A 1 112 ? 11.545 -8.625  3.216  1.00 52.02  ? 118 HIS   A NE2 1 
ATOM   881  N  N   . GLY   A 1 113 ? 16.037 -6.238  7.744  1.00 34.40  ? 119 GLY   A N   1 
ATOM   882  C  CA  . GLY   A 1 113 ? 17.057 -5.394  8.352  1.00 32.34  ? 119 GLY   A CA  1 
ATOM   883  C  C   . GLY   A 1 113 ? 16.517 -4.308  9.268  1.00 29.65  ? 119 GLY   A C   1 
ATOM   884  O  O   . GLY   A 1 113 ? 15.421 -4.433  9.826  1.00 28.66  ? 119 GLY   A O   1 
ATOM   885  N  N   . VAL   A 1 114 ? 17.320 -3.249  9.429  1.00 28.62  ? 120 VAL   A N   1 
ATOM   886  C  CA  . VAL   A 1 114 ? 17.070 -2.070  10.218 1.00 29.17  ? 120 VAL   A CA  1 
ATOM   887  C  C   . VAL   A 1 114 ? 16.095 -1.159  9.468  1.00 28.61  ? 120 VAL   A C   1 
ATOM   888  O  O   . VAL   A 1 114 ? 16.339 -0.803  8.316  1.00 29.15  ? 120 VAL   A O   1 
ATOM   889  C  CB  . VAL   A 1 114 ? 18.388 -1.333  10.518 1.00 30.65  ? 120 VAL   A CB  1 
ATOM   890  C  CG1 . VAL   A 1 114 ? 18.094 0.032   11.161 1.00 32.25  ? 120 VAL   A CG1 1 
ATOM   891  C  CG2 . VAL   A 1 114 ? 19.285 -2.180  11.418 1.00 30.66  ? 120 VAL   A CG2 1 
ATOM   892  N  N   . VAL   A 1 115 ? 14.994 -0.814  10.115 1.00 27.24  ? 121 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 115 ? 13.925 0.009   9.559  1.00 26.66  ? 121 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 115 ? 14.050 1.479   10.011 1.00 26.78  ? 121 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 115 ? 13.770 2.416   9.263  1.00 26.71  ? 121 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 115 ? 12.568 -0.598  10.046 1.00 26.61  ? 121 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 115 ? 11.377 0.220   9.569  1.00 26.46  ? 121 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 115 ? 12.438 -2.067  9.653  1.00 26.19  ? 121 VAL   A CG2 1 
ATOM   899  N  N   . GLY   A 1 116 ? 14.374 1.657   11.280 1.00 26.33  ? 122 GLY   A N   1 
ATOM   900  C  CA  . GLY   A 1 116 ? 14.465 2.974   11.872 1.00 25.84  ? 122 GLY   A CA  1 
ATOM   901  C  C   . GLY   A 1 116 ? 14.773 2.917   13.352 1.00 25.07  ? 122 GLY   A C   1 
ATOM   902  O  O   . GLY   A 1 116 ? 15.104 1.840   13.888 1.00 24.49  ? 122 GLY   A O   1 
ATOM   903  N  N   . ILE   A 1 117 ? 14.743 4.117   14.004 1.00 23.36  ? 123 ILE   A N   1 
ATOM   904  C  CA  . ILE   A 1 117 ? 15.045 4.247   15.429 1.00 23.27  ? 123 ILE   A CA  1 
ATOM   905  C  C   . ILE   A 1 117 ? 13.957 4.963   16.235 1.00 24.58  ? 123 ILE   A C   1 
ATOM   906  O  O   . ILE   A 1 117 ? 13.321 5.882   15.717 1.00 26.18  ? 123 ILE   A O   1 
ATOM   907  C  CB  . ILE   A 1 117 ? 16.424 4.920   15.632 1.00 23.08  ? 123 ILE   A CB  1 
ATOM   908  C  CG1 . ILE   A 1 117 ? 16.605 6.193   14.780 1.00 23.14  ? 123 ILE   A CG1 1 
ATOM   909  C  CG2 . ILE   A 1 117 ? 17.597 3.932   15.409 1.00 23.58  ? 123 ILE   A CG2 1 
ATOM   910  C  CD1 . ILE   A 1 117 ? 17.528 7.128   15.409 1.00 23.23  ? 123 ILE   A CD1 1 
ATOM   911  N  N   . VAL   A 1 118 ? 13.795 4.623   17.567 1.00 23.90  ? 124 VAL   A N   1 
ATOM   912  C  CA  . VAL   A 1 118 ? 12.787 5.249   18.417 1.00 23.78  ? 124 VAL   A CA  1 
ATOM   913  C  C   . VAL   A 1 118 ? 13.043 6.767   18.437 1.00 23.91  ? 124 VAL   A C   1 
ATOM   914  O  O   . VAL   A 1 118 ? 14.204 7.174   18.473 1.00 23.19  ? 124 VAL   A O   1 
ATOM   915  C  CB  . VAL   A 1 118 ? 12.790 4.665   19.860 1.00 25.18  ? 124 VAL   A CB  1 
ATOM   916  C  CG1 . VAL   A 1 118 ? 11.739 5.359   20.706 1.00 25.84  ? 124 VAL   A CG1 1 
ATOM   917  C  CG2 . VAL   A 1 118 ? 12.555 3.142   19.862 1.00 26.07  ? 124 VAL   A CG2 1 
ATOM   918  N  N   . SER   A 1 119 ? 11.991 7.591   18.315 1.00 24.94  ? 125 SER   A N   1 
ATOM   919  C  CA  . SER   A 1 119 ? 12.175 9.036   18.221 1.00 25.39  ? 125 SER   A CA  1 
ATOM   920  C  C   . SER   A 1 119 ? 11.161 9.847   18.973 1.00 27.40  ? 125 SER   A C   1 
ATOM   921  O  O   . SER   A 1 119 ? 11.487 10.985  19.335 1.00 26.79  ? 125 SER   A O   1 
ATOM   922  C  CB  . SER   A 1 119 ? 12.184 9.461   16.760 1.00 27.36  ? 125 SER   A CB  1 
ATOM   923  O  OG  . SER   A 1 119 ? 12.518 10.831  16.606 1.00 32.44  ? 125 SER   A OG  1 
ATOM   924  N  N   . THR   A 1 120 ? 9.928  9.297   19.213 1.00 29.15  ? 126 THR   A N   1 
ATOM   925  C  CA  . THR   A 1 120 ? 8.825  9.934   19.991 1.00 31.83  ? 126 THR   A CA  1 
ATOM   926  C  C   . THR   A 1 120 ? 8.023  8.850   20.792 1.00 35.44  ? 126 THR   A C   1 
ATOM   927  O  O   . THR   A 1 120 ? 8.249  7.648   20.583 1.00 36.11  ? 126 THR   A O   1 
ATOM   928  C  CB  . THR   A 1 120 ? 7.895  10.792  19.098 1.00 31.85  ? 126 THR   A CB  1 
ATOM   929  O  OG1 . THR   A 1 120 ? 7.110  9.934   18.281 1.00 33.72  ? 126 THR   A OG1 1 
ATOM   930  C  CG2 . THR   A 1 120 ? 8.618  11.837  18.252 1.00 30.41  ? 126 THR   A CG2 1 
ATOM   931  N  N   . GLY   A 1 121 ? 7.119  9.267   21.681 1.00 37.68  ? 127 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 121 ? 6.301  8.366   22.495 1.00 40.56  ? 127 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 121 ? 5.296  9.065   23.397 1.00 42.87  ? 127 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 121 ? 5.179  10.285  23.344 1.00 42.70  ? 127 GLY   A O   1 
ATOM   935  N  N   . GLY   A 1 122 ? 4.582  8.297   24.228 1.00 44.82  ? 128 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 122 ? 3.592  8.815   25.177 1.00 47.54  ? 128 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 122 ? 2.173  8.311   24.962 1.00 49.50  ? 128 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 122 ? 1.766  8.067   23.829 1.00 50.28  ? 128 GLY   A O   1 
ATOM   939  N  N   . ASN   A 1 123 ? 1.423  8.127   26.043 1.00 50.48  ? 129 ASN   A N   1 
ATOM   940  C  CA  . ASN   A 1 123 ? 0.026  7.642   26.050 1.00 51.19  ? 129 ASN   A CA  1 
ATOM   941  C  C   . ASN   A 1 123 ? -0.122 6.223   25.479 1.00 50.36  ? 129 ASN   A C   1 
ATOM   942  O  O   . ASN   A 1 123 ? -1.195 5.862   24.985 1.00 51.64  ? 129 ASN   A O   1 
ATOM   943  C  CB  . ASN   A 1 123 ? -0.934 8.619   25.356 1.00 53.36  ? 129 ASN   A CB  1 
ATOM   944  C  CG  . ASN   A 1 123 ? -0.846 10.053  25.851 1.00 57.79  ? 129 ASN   A CG  1 
ATOM   945  O  OD1 . ASN   A 1 123 ? -0.868 10.305  27.060 1.00 59.17  ? 129 ASN   A OD1 1 
ATOM   946  N  ND2 . ASN   A 1 123 ? -0.771 11.029  24.923 1.00 57.84  ? 129 ASN   A ND2 1 
ATOM   947  N  N   . GLY   A 1 124 ? 0.925  5.419   25.608 1.00 47.60  ? 130 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 124 ? 0.896  4.063   25.099 1.00 45.86  ? 130 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 124 ? 1.213  3.970   23.623 1.00 44.01  ? 130 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 124 ? 0.921  2.948   22.999 1.00 44.81  ? 130 GLY   A O   1 
ATOM   951  N  N   . LEU   A 1 125 ? 1.829  5.026   23.047 1.00 41.20  ? 131 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 125 ? 2.261  5.037   21.662 1.00 39.16  ? 131 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 125 ? 3.804  5.172   21.617 1.00 37.04  ? 131 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 125 ? 4.408  5.683   22.568 1.00 37.14  ? 131 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 125 ? 1.674  6.236   20.903 1.00 40.06  ? 131 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 125 ? 0.163  6.485   20.914 1.00 42.58  ? 131 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 125 ? -0.167 7.592   19.957 1.00 43.45  ? 131 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 125 ? -0.591 5.275   20.455 1.00 43.49  ? 131 LEU   A CD2 1 
ATOM   959  N  N   . VAL   A 1 126 ? 4.425  4.739   20.487 1.00 34.20  ? 132 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 126 ? 5.857  4.825   20.213 1.00 32.14  ? 132 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 126 ? 6.063  5.216   18.724 1.00 31.98  ? 132 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 126 ? 5.457  4.610   17.839 1.00 31.86  ? 132 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 126 ? 6.626  3.534   20.629 1.00 31.22  ? 132 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 126 ? 6.009  2.274   20.044 1.00 31.30  ? 132 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 126 ? 8.120  3.625   20.322 1.00 31.00  ? 132 VAL   A CG2 1 
ATOM   966  N  N   . GLY   A 1 127 ? 6.907  6.231   18.483 1.00 31.40  ? 133 GLY   A N   1 
ATOM   967  C  CA  . GLY   A 1 127 ? 7.225  6.764   17.165 1.00 30.52  ? 133 GLY   A CA  1 
ATOM   968  C  C   . GLY   A 1 127 ? 8.643  6.464   16.748 1.00 29.87  ? 133 GLY   A C   1 
ATOM   969  O  O   . GLY   A 1 127 ? 9.561  6.591   17.559 1.00 29.78  ? 133 GLY   A O   1 
ATOM   970  N  N   . PHE   A 1 128 ? 8.826  6.022   15.473 1.00 28.57  ? 134 PHE   A N   1 
ATOM   971  C  CA  . PHE   A 1 128 ? 10.110 5.614   14.895 1.00 27.43  ? 134 PHE   A CA  1 
ATOM   972  C  C   . PHE   A 1 128 ? 10.416 6.494   13.698 1.00 27.37  ? 134 PHE   A C   1 
ATOM   973  O  O   . PHE   A 1 128 ? 9.558  6.712   12.833 1.00 26.73  ? 134 PHE   A O   1 
ATOM   974  C  CB  . PHE   A 1 128 ? 10.112 4.117   14.444 1.00 26.60  ? 134 PHE   A CB  1 
ATOM   975  C  CG  . PHE   A 1 128 ? 9.608  3.090   15.436 1.00 26.79  ? 134 PHE   A CG  1 
ATOM   976  C  CD1 . PHE   A 1 128 ? 10.411 2.649   16.481 1.00 27.17  ? 134 PHE   A CD1 1 
ATOM   977  C  CD2 . PHE   A 1 128 ? 8.317  2.581   15.342 1.00 27.30  ? 134 PHE   A CD2 1 
ATOM   978  C  CE1 . PHE   A 1 128 ? 9.928  1.720   17.410 1.00 27.82  ? 134 PHE   A CE1 1 
ATOM   979  C  CE2 . PHE   A 1 128 ? 7.842  1.636   16.264 1.00 27.53  ? 134 PHE   A CE2 1 
ATOM   980  C  CZ  . PHE   A 1 128 ? 8.644  1.215   17.297 1.00 27.05  ? 134 PHE   A CZ  1 
ATOM   981  N  N   . ALA   A 1 129 ? 11.648 6.992   13.646 1.00 26.96  ? 135 ALA   A N   1 
ATOM   982  C  CA  . ALA   A 1 129 ? 12.126 7.811   12.556 1.00 27.14  ? 135 ALA   A CA  1 
ATOM   983  C  C   . ALA   A 1 129 ? 12.596 6.862   11.449 1.00 27.89  ? 135 ALA   A C   1 
ATOM   984  O  O   . ALA   A 1 129 ? 13.539 6.112   11.673 1.00 27.02  ? 135 ALA   A O   1 
ATOM   985  C  CB  . ALA   A 1 129 ? 13.289 8.662   13.040 1.00 27.67  ? 135 ALA   A CB  1 
ATOM   986  N  N   . ASP   A 1 130 ? 11.907 6.831   10.295 1.00 29.23  ? 136 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 130 ? 12.259 5.928   9.192  1.00 31.30  ? 136 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 130 ? 13.620 6.242   8.593  1.00 31.48  ? 136 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 130 ? 13.956 7.431   8.499  1.00 31.55  ? 136 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 130 ? 11.190 6.023   8.092  1.00 33.30  ? 136 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 130 ? 11.336 4.994   6.995  1.00 36.51  ? 136 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 130 ? 11.286 3.790   7.307  1.00 36.97  ? 136 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 130 ? 11.458 5.397   5.816  1.00 38.47  ? 136 ASP   A OD2 1 
ATOM   994  N  N   . VAL   A 1 131 ? 14.395 5.189   8.178  1.00 31.06  ? 137 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 131 ? 15.709 5.327   7.500  1.00 30.77  ? 137 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 131 ? 15.798 4.519   6.140  1.00 31.92  ? 137 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 131 ? 16.839 4.575   5.451  1.00 31.77  ? 137 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 131 ? 16.894 4.919   8.398  1.00 29.76  ? 137 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 131 ? 16.871 5.633   9.746  1.00 29.80  ? 137 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 131 ? 16.987 3.386   8.544  1.00 29.62  ? 137 VAL   A CG2 1 
ATOM   1001 N  N   . ARG   A 1 132 ? 14.745 3.739   5.782  1.00 31.98  ? 138 ARG   A N   1 
ATOM   1002 C  CA  . ARG   A 1 132 ? 14.778 2.913   4.558  1.00 32.69  ? 138 ARG   A CA  1 
ATOM   1003 C  C   . ARG   A 1 132 ? 14.911 3.690   3.219  1.00 35.17  ? 138 ARG   A C   1 
ATOM   1004 O  O   . ARG   A 1 132 ? 15.295 3.100   2.196  1.00 36.08  ? 138 ARG   A O   1 
ATOM   1005 C  CB  . ARG   A 1 132 ? 13.550 2.005   4.486  1.00 31.50  ? 138 ARG   A CB  1 
ATOM   1006 C  CG  . ARG   A 1 132 ? 13.283 1.231   5.774  1.00 30.18  ? 138 ARG   A CG  1 
ATOM   1007 C  CD  . ARG   A 1 132 ? 11.981 0.471   5.656  1.00 30.10  ? 138 ARG   A CD  1 
ATOM   1008 N  NE  . ARG   A 1 132 ? 10.840 1.275   6.091  1.00 32.60  ? 138 ARG   A NE  1 
ATOM   1009 C  CZ  . ARG   A 1 132 ? 9.606  0.799   6.230  1.00 36.01  ? 138 ARG   A CZ  1 
ATOM   1010 N  NH1 . ARG   A 1 132 ? 9.343  -0.472  5.957  1.00 37.88  ? 138 ARG   A NH1 1 
ATOM   1011 N  NH2 . ARG   A 1 132 ? 8.626  1.590   6.645  1.00 34.94  ? 138 ARG   A NH2 1 
ATOM   1012 N  N   . ASP   A 1 133 ? 14.597 4.995   3.217  1.00 35.58  ? 139 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 133 ? 14.667 5.783   1.981  1.00 36.29  ? 139 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 133 ? 16.049 6.386   1.702  1.00 37.23  ? 139 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 133 ? 16.336 6.786   0.558  1.00 37.19  ? 139 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 133 ? 13.584 6.866   1.965  1.00 37.38  ? 139 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 133 ? 13.777 7.932   3.028  1.00 40.61  ? 139 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 133 ? 14.066 7.571   4.181  1.00 39.49  ? 139 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 133 ? 13.642 9.134   2.699  1.00 43.74  ? 139 ASP   A OD2 1 
ATOM   1020 N  N   . LEU   A 1 134 ? 16.916 6.422   2.736  1.00 37.19  ? 140 LEU   A N   1 
ATOM   1021 C  CA  . LEU   A 1 134 ? 18.269 6.962   2.659  1.00 37.08  ? 140 LEU   A CA  1 
ATOM   1022 C  C   . LEU   A 1 134 ? 19.150 5.916   2.015  1.00 39.09  ? 140 LEU   A C   1 
ATOM   1023 O  O   . LEU   A 1 134 ? 19.924 5.230   2.692  1.00 39.32  ? 140 LEU   A O   1 
ATOM   1024 C  CB  . LEU   A 1 134 ? 18.782 7.328   4.064  1.00 35.95  ? 140 LEU   A CB  1 
ATOM   1025 C  CG  . LEU   A 1 134 ? 17.849 8.212   4.896  1.00 36.16  ? 140 LEU   A CG  1 
ATOM   1026 C  CD1 . LEU   A 1 134 ? 18.402 8.442   6.273  1.00 36.22  ? 140 LEU   A CD1 1 
ATOM   1027 C  CD2 . LEU   A 1 134 ? 17.537 9.546   4.188  1.00 36.29  ? 140 LEU   A CD2 1 
ATOM   1028 N  N   . LEU   A 1 135 ? 19.047 5.824   0.679  1.00 40.32  ? 141 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 135 ? 19.735 4.827   -0.133 1.00 41.63  ? 141 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 135 ? 21.251 4.953   -0.136 1.00 43.85  ? 141 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 135 ? 21.941 3.944   -0.370 1.00 43.93  ? 141 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 135 ? 19.201 4.855   -1.569 1.00 41.51  ? 141 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 135 ? 17.701 4.784   -1.792 1.00 42.41  ? 141 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 135 ? 17.407 4.622   -3.284 1.00 43.30  ? 141 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 135 ? 17.085 3.619   -1.037 1.00 42.50  ? 141 LEU   A CD2 1 
ATOM   1036 N  N   . TRP   A 1 136 ? 21.768 6.197   0.108  1.00 45.14  ? 142 TRP   A N   1 
ATOM   1037 C  CA  . TRP   A 1 136 ? 23.198 6.538   0.137  1.00 46.45  ? 142 TRP   A CA  1 
ATOM   1038 C  C   . TRP   A 1 136 ? 23.959 5.975   1.333  1.00 48.47  ? 142 TRP   A C   1 
ATOM   1039 O  O   . TRP   A 1 136 ? 25.188 6.003   1.341  1.00 48.82  ? 142 TRP   A O   1 
ATOM   1040 C  CB  . TRP   A 1 136 ? 23.420 8.053   0.038  1.00 46.18  ? 142 TRP   A CB  1 
ATOM   1041 C  CG  . TRP   A 1 136 ? 22.655 8.869   1.039  1.00 46.86  ? 142 TRP   A CG  1 
ATOM   1042 C  CD1 . TRP   A 1 136 ? 21.427 9.440   0.865  1.00 47.60  ? 142 TRP   A CD1 1 
ATOM   1043 C  CD2 . TRP   A 1 136 ? 23.092 9.252   2.352  1.00 47.08  ? 142 TRP   A CD2 1 
ATOM   1044 N  NE1 . TRP   A 1 136 ? 21.070 10.145  1.989  1.00 48.00  ? 142 TRP   A NE1 1 
ATOM   1045 C  CE2 . TRP   A 1 136 ? 22.059 10.016  2.932  1.00 47.84  ? 142 TRP   A CE2 1 
ATOM   1046 C  CE3 . TRP   A 1 136 ? 24.234 8.983   3.114  1.00 47.97  ? 142 TRP   A CE3 1 
ATOM   1047 C  CZ2 . TRP   A 1 136 ? 22.150 10.539  4.223  1.00 48.40  ? 142 TRP   A CZ2 1 
ATOM   1048 C  CZ3 . TRP   A 1 136 ? 24.323 9.508   4.392  1.00 48.76  ? 142 TRP   A CZ3 1 
ATOM   1049 C  CH2 . TRP   A 1 136 ? 23.295 10.278  4.930  1.00 48.39  ? 142 TRP   A CH2 1 
ATOM   1050 N  N   . LEU   A 1 137 ? 23.245 5.474   2.353  1.00 49.35  ? 143 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 137 ? 23.880 4.846   3.510  1.00 51.27  ? 143 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 137 ? 24.669 3.580   3.119  1.00 55.34  ? 143 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 137 ? 25.583 3.177   3.839  1.00 55.79  ? 143 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 137 ? 22.793 4.476   4.540  1.00 50.12  ? 143 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 137 ? 22.197 5.650   5.310  1.00 49.40  ? 143 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 137 ? 21.042 5.187   6.198  1.00 49.32  ? 143 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 137 ? 23.256 6.341   6.147  1.00 49.00  ? 143 LEU   A CD2 1 
ATOM   1058 N  N   . ASP   A 1 138 ? 24.297 2.950   1.987  1.00 58.13  ? 144 ASP   A N   1 
ATOM   1059 C  CA  . ASP   A 1 138 ? 24.893 1.741   1.435  1.00 61.55  ? 144 ASP   A CA  1 
ATOM   1060 C  C   . ASP   A 1 138 ? 25.948 1.981   0.364  1.00 65.29  ? 144 ASP   A C   1 
ATOM   1061 O  O   . ASP   A 1 138 ? 26.538 1.017   -0.101 1.00 66.15  ? 144 ASP   A O   1 
ATOM   1062 C  CB  . ASP   A 1 138 ? 23.785 0.932   0.772  1.00 63.27  ? 144 ASP   A CB  1 
ATOM   1063 C  CG  . ASP   A 1 138 ? 22.968 0.152   1.751  1.00 67.63  ? 144 ASP   A CG  1 
ATOM   1064 O  OD1 . ASP   A 1 138 ? 23.566 -0.531  2.607  1.00 68.55  ? 144 ASP   A OD1 1 
ATOM   1065 O  OD2 . ASP   A 1 138 ? 21.730 0.212   1.661  1.00 69.94  ? 144 ASP   A OD2 1 
ATOM   1066 N  N   . GLU   A 1 139 ? 26.126 3.230   -0.089 1.00 67.61  ? 145 GLU   A N   1 
ATOM   1067 C  CA  . GLU   A 1 139 ? 27.025 3.588   -1.178 1.00 70.41  ? 145 GLU   A CA  1 
ATOM   1068 C  C   . GLU   A 1 139 ? 27.750 4.914   -0.886 1.00 72.39  ? 145 GLU   A C   1 
ATOM   1069 O  O   . GLU   A 1 139 ? 28.455 5.466   -1.754 1.00 73.50  ? 145 GLU   A O   1 
ATOM   1070 C  CB  . GLU   A 1 139 ? 26.191 3.735   -2.460 1.00 74.11  ? 145 GLU   A CB  1 
ATOM   1071 C  CG  . GLU   A 1 139 ? 25.093 4.786   -2.324 1.00 80.40  ? 145 GLU   A CG  1 
ATOM   1072 C  CD  . GLU   A 1 139 ? 24.157 4.940   -3.508 1.00 88.30  ? 145 GLU   A CD  1 
ATOM   1073 O  OE1 . GLU   A 1 139 ? 23.710 6.083   -3.768 1.00 89.53  ? 145 GLU   A OE1 1 
ATOM   1074 O  OE2 . GLU   A 1 139 ? 23.871 3.920   -4.177 1.00 91.55  ? 145 GLU   A OE2 1 
HETATM 1075 N  N1  . A1BN7 B 2 .   ? 10.238 13.666  22.538 1.00 45.45  ? 201 A1BN7 A N1  1 
HETATM 1076 C  C4  . A1BN7 B 2 .   ? 11.175 14.552  23.248 1.00 45.15  ? 201 A1BN7 A C4  1 
HETATM 1077 C  C5  . A1BN7 B 2 .   ? 9.547  12.668  23.133 1.00 45.28  ? 201 A1BN7 A C5  1 
HETATM 1078 C  C6  . A1BN7 B 2 .   ? 9.802  12.254  24.608 1.00 46.34  ? 201 A1BN7 A C6  1 
HETATM 1079 C  C7  . A1BN7 B 2 .   ? 9.066  10.970  24.956 1.00 47.27  ? 201 A1BN7 A C7  1 
HETATM 1080 C  C8  . A1BN7 B 2 .   ? 8.115  10.910  25.985 1.00 47.70  ? 201 A1BN7 A C8  1 
HETATM 1081 C  C10 . A1BN7 B 2 .   ? 9.989  14.050  21.142 1.00 45.40  ? 201 A1BN7 A C10 1 
HETATM 1082 CL CL  . A1BN7 B 2 .   ? 10.298 9.282   23.127 1.00 47.33  ? 201 A1BN7 A CL  1 
HETATM 1083 C  C9  . A1BN7 B 2 .   ? 9.251  9.735   24.399 1.00 47.57  ? 201 A1BN7 A C9  1 
HETATM 1084 S  S   . A1BN7 B 2 .   ? 8.259  8.590   25.178 1.00 48.20  ? 201 A1BN7 A S   1 
HETATM 1085 N  N2  . A1BN7 B 2 .   ? 7.599  9.707   26.227 1.00 47.80  ? 201 A1BN7 A N2  1 
HETATM 1086 F  F   . A1BN7 B 2 .   ? 9.418  13.263  25.454 1.00 45.54  ? 201 A1BN7 A F   1 
HETATM 1087 F  F1  . A1BN7 B 2 .   ? 11.146 12.091  24.811 1.00 46.73  ? 201 A1BN7 A F1  1 
HETATM 1088 O  O1  . A1BN7 B 2 .   ? 8.638  12.100  22.553 1.00 44.09  ? 201 A1BN7 A O1  1 
HETATM 1089 C  C3  . A1BN7 B 2 .   ? 12.492 14.648  22.514 1.00 45.32  ? 201 A1BN7 A C3  1 
HETATM 1090 C  C2  . A1BN7 B 2 .   ? 12.270 15.082  21.065 1.00 45.23  ? 201 A1BN7 A C2  1 
HETATM 1091 C  C1  . A1BN7 B 2 .   ? 11.291 14.149  20.335 1.00 44.95  ? 201 A1BN7 A C1  1 
HETATM 1092 C  C   . A1BN7 B 2 .   ? 11.087 14.607  18.899 1.00 44.59  ? 201 A1BN7 A C   1 
HETATM 1093 O  O   . A1BN7 B 2 .   ? 10.758 15.767  18.639 1.00 44.50  ? 201 A1BN7 A O   1 
HETATM 1094 N  N   . A1BN7 B 2 .   ? 11.343 13.714  17.960 1.00 44.34  ? 201 A1BN7 A N   1 
HETATM 1095 ZN ZN  . ZN    C 3 .   ? 11.099 -5.446  5.772  1.00 39.86  2 202 ZN    A ZN  1 
HETATM 1096 O  O   . HOH   D 4 .   ? 20.171 22.085  8.066  1.00 29.62  ? 301 HOH   A O   1 
HETATM 1097 O  O   . HOH   D 4 .   ? 18.385 20.469  10.045 1.00 33.07  ? 302 HOH   A O   1 
HETATM 1098 O  O   . HOH   D 4 .   ? 13.429 9.659   9.626  1.00 16.99  ? 303 HOH   A O   1 
HETATM 1099 O  O   . HOH   D 4 .   ? 9.642  17.734  19.971 1.00 35.67  ? 304 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 10.431 7.397   4.459  1.00 53.89  ? 305 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 30.347 20.481  10.796 1.00 42.88  ? 306 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 17.318 2.433   23.278 1.00 29.24  ? 307 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 4.623  4.855   25.071 1.00 36.16  ? 308 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 23.614 21.793  7.847  1.00 42.66  ? 309 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 7.881  -4.635  0.690  1.00 30.62  ? 310 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 10.261 3.777   34.130 1.00 37.51  ? 311 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 20.361 8.400   19.578 1.00 28.14  ? 312 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 30.093 10.635  19.471 1.00 37.36  ? 313 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 20.314 -2.297  37.033 1.00 33.61  ? 314 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 10.578 4.186   3.512  1.00 30.77  ? 315 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 11.822 15.993  5.601  1.00 37.00  ? 316 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 9.969  -2.527  7.695  1.00 300.00 ? 317 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 15.162 1.848   23.354 1.00 36.30  ? 318 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 18.002 18.411  17.071 1.00 30.11  ? 319 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 30.382 10.760  3.216  1.00 33.48  ? 320 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 8.684  19.240  18.513 1.00 34.01  ? 321 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 8.881  1.860   2.966  1.00 30.58  ? 322 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 0.536  -1.124  16.852 1.00 36.90  ? 323 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 30.448 4.051   3.871  1.00 46.91  ? 324 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 11.309 1.400   34.022 1.00 30.18  ? 325 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 15.035 -4.995  17.261 1.00 27.63  ? 326 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 14.102 -12.146 4.105  1.00 28.38  ? 327 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 5.798  1.053   6.346  1.00 40.27  ? 328 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 11.466 10.923  11.513 1.00 26.90  ? 329 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 13.104 8.523   30.256 1.00 42.41  ? 330 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 5.532  -2.239  24.763 1.00 35.84  ? 331 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 18.680 -0.993  19.541 1.00 33.06  ? 332 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 0.694  0.637   24.803 1.00 48.11  ? 333 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? -1.237 -0.980  4.361  1.00 60.84  ? 334 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 14.776 11.871  24.209 1.00 30.84  ? 335 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 14.523 13.904  3.871  1.00 40.44  ? 336 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 19.655 -0.607  27.566 1.00 41.12  ? 337 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 11.928 20.719  12.701 1.00 29.02  ? 338 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 22.033 -6.349  10.809 1.00 33.46  ? 339 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 18.505 11.640  1.478  1.00 58.23  ? 340 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 4.546  -6.320  6.972  1.00 41.52  ? 341 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 31.313 20.335  17.428 1.00 34.85  ? 342 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 17.566 22.049  17.277 1.00 33.89  ? 343 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 16.539 -11.958 5.245  1.00 42.00  ? 344 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 28.683 21.983  18.657 1.00 39.64  ? 345 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 6.668  7.663   29.305 1.00 51.91  ? 346 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 6.218  -6.456  29.557 1.00 56.68  ? 347 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 9.155  20.947  10.775 1.00 48.62  ? 348 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 3.941  -3.427  22.032 1.00 52.14  ? 349 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 5.193  -1.988  29.699 1.00 48.44  ? 350 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 19.626 23.668  15.577 1.00 26.34  ? 351 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 22.626 18.703  5.943  1.00 29.91  ? 352 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 1.866  13.071  5.234  1.00 49.35  ? 353 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 12.425 -8.669  13.455 1.00 30.78  ? 354 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? -0.638 14.624  7.519  1.00 38.27  ? 355 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 11.584 13.763  1.353  1.00 45.39  ? 356 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 4.240  11.086  19.496 1.00 34.95  ? 357 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 36.469 6.500   6.781  1.00 47.39  ? 358 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 14.355 20.798  8.527  1.00 39.24  ? 359 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 1.701  -3.306  18.214 1.00 39.05  ? 360 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 6.193  3.315   33.376 1.00 36.81  ? 361 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 22.435 18.309  19.937 1.00 28.39  ? 362 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 7.128  25.467  14.065 1.00 36.28  ? 363 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 8.655  -8.358  8.887  1.00 48.24  ? 364 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 16.258 -5.613  1.922  1.00 38.18  ? 365 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 8.119  6.709   34.101 1.00 45.85  ? 366 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 5.052  5.562   29.716 1.00 48.11  ? 367 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 0.383  -4.623  17.189 1.00 48.13  ? 368 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 22.245 8.353   20.977 1.00 36.61  ? 369 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 1.470  14.447  23.287 1.00 40.84  ? 370 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 19.437 8.266   -1.936 1.00 49.49  ? 371 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 24.614 6.696   21.418 1.00 37.02  ? 372 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 7.403  -5.923  2.613  1.00 66.43  ? 373 HOH   A O   1 
HETATM 1169 O  O   . HOH   D 4 .   ? 5.420  13.946  22.050 1.00 50.62  ? 374 HOH   A O   1 
HETATM 1170 O  O   . HOH   D 4 .   ? 21.057 21.614  17.997 1.00 38.59  ? 375 HOH   A O   1 
HETATM 1171 O  O   . HOH   D 4 .   ? 2.998  23.024  22.208 1.00 47.25  ? 376 HOH   A O   1 
HETATM 1172 O  O   . HOH   D 4 .   ? 8.718  16.979  25.883 1.00 40.14  ? 377 HOH   A O   1 
HETATM 1173 O  O   . HOH   D 4 .   ? 22.837 15.759  23.989 1.00 38.27  ? 378 HOH   A O   1 
HETATM 1174 O  O   . HOH   D 4 .   ? 2.241  1.999   27.629 1.00 49.90  ? 379 HOH   A O   1 
HETATM 1175 O  O   . HOH   D 4 .   ? 13.975 13.361  25.963 1.00 35.06  ? 380 HOH   A O   1 
HETATM 1176 O  O   . HOH   D 4 .   ? 10.758 16.589  27.215 1.00 44.87  ? 381 HOH   A O   1 
HETATM 1177 O  O   . HOH   D 4 .   ? 11.262 23.169  14.447 1.00 35.45  ? 382 HOH   A O   1 
HETATM 1178 O  O   . HOH   D 4 .   ? 25.668 6.640   -7.701 1.00 47.26  ? 383 HOH   A O   1 
HETATM 1179 O  O   . HOH   D 4 .   ? 9.445  -9.540  12.732 1.00 27.91  ? 384 HOH   A O   1 
HETATM 1180 O  O   . HOH   D 4 .   ? 9.452  24.357  13.079 1.00 50.53  ? 385 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   ? 0.8060 0.3240 0.6383 0.0298  -0.1162 0.0034  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.7734 0.3136 0.6907 0.0294  -0.1514 0.0208  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.7191 0.3224 0.7097 0.0448  -0.1174 0.0207  7   SER   A C   
4    O  O   . SER   A 1   ? 0.7291 0.3406 0.6836 0.0479  -0.0873 0.0132  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.8351 0.3179 0.7085 0.0103  -0.1992 0.0362  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.8998 0.3759 0.7268 0.0101  -0.1778 0.0331  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.6605 0.3007 0.7497 0.0525  -0.1202 0.0291  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.6244 0.3085 0.7725 0.0630  -0.0856 0.0284  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.5788 0.3027 0.7899 0.0740  -0.0537 0.0229  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.5912 0.3255 0.7775 0.0778  -0.0376 0.0121  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.5251 0.2664 0.8151 0.0785  -0.0394 0.0303  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.4922 0.2580 0.8323 0.0861  -0.0035 0.0249  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.4670 0.2406 0.8394 0.0876  0.0364  0.0239  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.4492 0.2140 0.8279 0.0848  0.0320  0.0304  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.4727 0.2364 0.8924 0.0884  -0.0240 0.0362  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.4632 0.2458 0.8462 0.0898  0.0765  0.0154  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.4642 0.2382 0.8652 0.0874  0.1196  0.0127  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.4371 0.2027 0.9329 0.0926  0.1412  0.0202  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.4115 0.1827 0.9315 0.0964  0.1398  0.0200  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.4920 0.2659 0.8192 0.0799  0.1516  -0.0013 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.5052 0.2935 0.7558 0.0765  0.1301  -0.0060 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.5064 0.2567 0.8302 0.0721  0.1928  -0.0050 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.5185 0.3114 0.7174 0.0689  0.1479  -0.0130 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.4473 0.1981 1.0033 0.0931  0.1636  0.0278  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.4395 0.1789 1.1033 0.0989  0.1914  0.0377  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.4674 0.1752 1.1211 0.0939  0.2604  0.0271  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.4637 0.1562 1.1237 0.0910  0.2786  0.0288  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.4120 0.1547 1.1776 0.1034  0.1569  0.0615  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.4161 0.1739 1.1830 0.1030  0.0870  0.0730  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.4039 0.1684 1.2288 0.1064  0.0700  0.0805  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.4456 0.2024 1.1522 0.0969  0.0394  0.0769  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.4119 0.1791 1.2282 0.1020  0.0049  0.0907  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.4608 0.2146 1.1520 0.0919  -0.0223 0.0866  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.4481 0.2057 1.1923 0.0936  -0.0406 0.0934  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.4751 0.2196 1.1954 0.0848  -0.1023 0.1027  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.4853 0.1762 1.1108 0.0904  0.2992  0.0155  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.5205 0.1632 1.1144 0.0803  0.3686  0.0039  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.5172 0.1331 1.1861 0.0846  0.4167  0.0064  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.5115 0.1354 1.1687 0.0860  0.4104  0.0036  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.5723 0.1996 1.0245 0.0633  0.3755  -0.0136 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.5762 0.2319 0.9827 0.0640  0.3410  -0.0163 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.6086 0.1700 1.0124 0.0473  0.4450  -0.0254 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.5088 0.0923 1.2658 0.0877  0.4673  0.0134  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.5146 0.0683 1.3596 0.0928  0.5216  0.0178  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.4807 0.0803 1.4298 0.1072  0.4746  0.0352  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.4538 0.0961 1.4610 0.1148  0.4107  0.0519  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.4881 0.0763 1.4424 0.1080  0.4984  0.0307  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.4537 0.0829 1.5024 0.1198  0.4523  0.0465  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.4275 0.0944 1.3777 0.1174  0.3878  0.0382  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.4045 0.0888 1.3836 0.1222  0.3680  0.0416  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.4852 0.0845 1.6237 0.1246  0.5126  0.0507  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.5414 0.1122 1.8200 0.1309  0.5683  0.0663  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.5386 0.1268 1.8845 0.1351  0.5424  0.0820  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.5768 0.0980 1.9038 0.1314  0.6502  0.0635  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.4261 0.1050 1.2686 0.1103  0.3567  0.0285  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.4080 0.1179 1.1599 0.1081  0.3041  0.0210  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.3623 0.1013 1.0984 0.1093  0.2420  0.0278  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.3480 0.0817 1.1034 0.1083  0.2414  0.0338  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.4505 0.1401 1.0704 0.0952  0.3305  0.0023  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.4695 0.1230 1.0779 0.0902  0.3829  -0.0045 15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.4593 0.1263 1.1194 0.0983  0.3754  0.0001  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.5238 0.1221 1.0591 0.0746  0.4396  -0.0159 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.4937 0.1229 1.1409 0.0931  0.4258  -0.0057 15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.5678 0.1195 1.0785 0.0665  0.4902  -0.0222 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.5637 0.1330 1.1310 0.0767  0.4833  -0.0169 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.6274 0.1476 1.1697 0.0686  0.5346  -0.0225 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.3238 0.0875 1.0199 0.1104  0.1931  0.0266  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.3098 0.0889 0.9670 0.1088  0.1385  0.0302  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.3139 0.1046 0.8660 0.1058  0.1271  0.0159  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.3012 0.0984 0.8572 0.1086  0.1234  0.0137  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.3026 0.0881 1.0403 0.1116  0.0867  0.0487  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.3656 0.1525 1.0345 0.1058  0.0282  0.0497  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.3851 0.1646 1.1186 0.1021  -0.0293 0.0695  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.4459 0.2161 1.1015 0.0956  -0.0702 0.0635  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.5016 0.2484 1.0956 0.0848  -0.1169 0.0679  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.5020 0.2381 1.1042 0.0797  -0.1335 0.0796  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.5221 0.2492 1.0405 0.0776  -0.1442 0.0603  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.3294 0.1223 0.7993 0.1003  0.1254  0.0080  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.3614 0.1665 0.7514 0.0981  0.1166  -0.0012 17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.3737 0.1818 0.7330 0.0985  0.0745  0.0011  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.3918 0.1919 0.7474 0.0958  0.0607  0.0056  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.4031 0.2050 0.7265 0.0893  0.1433  -0.0088 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.4264 0.2440 0.6893 0.0872  0.1334  -0.0129 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.4178 0.1969 0.7522 0.0834  0.1879  -0.0117 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.3669 0.1794 0.6978 0.1003  0.0577  -0.0024 18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.3885 0.1884 0.6734 0.0979  0.0257  -0.0027 18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.3870 0.1941 0.6151 0.0992  0.0358  -0.0112 18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.3649 0.1894 0.6018 0.1021  0.0567  -0.0137 18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.3989 0.1804 0.7186 0.0964  -0.0118 0.0050  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.4030 0.1703 0.7689 0.0919  -0.0380 0.0189  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.3902 0.1828 0.7617 0.1018  -0.0038 0.0052  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.4100 0.1973 0.5835 0.0962  0.0213  -0.0142 19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.4244 0.2134 0.5611 0.0989  0.0346  -0.0203 19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.4477 0.2312 0.6097 0.1017  0.0239  -0.0213 19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.4651 0.2250 0.6391 0.0973  -0.0047 -0.0181 19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.4381 0.1935 0.5093 0.0941  0.0301  -0.0243 19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.4443 0.2005 0.4907 0.0907  0.0380  -0.0227 19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.4541 0.1912 0.4932 0.0850  0.0183  -0.0191 19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.4114 0.1896 0.4506 0.0931  0.0642  -0.0231 19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.4527 0.2579 0.6298 0.1075  0.0432  -0.0229 20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.4597 0.2612 0.6617 0.1107  0.0365  -0.0241 20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.5189 0.2792 0.6747 0.1062  0.0195  -0.0295 20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.5450 0.2862 0.7164 0.1029  -0.0034 -0.0289 20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.4375 0.2667 0.6553 0.1167  0.0610  -0.0233 20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.4296 0.2594 0.6804 0.1209  0.0585  -0.0239 20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.4573 0.3076 0.7090 0.1254  0.0796  -0.0214 20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.4671 0.3218 0.7514 0.1298  0.0819  -0.0207 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.4865 0.3266 0.7671 0.1330  0.0783  -0.0249 20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.5011 0.3123 0.7397 0.1307  0.0736  -0.0313 20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.4435 0.2905 0.7566 0.1371  0.0822  -0.0234 20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.5429 0.2815 0.6392 0.1035  0.0312  -0.0343 21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.5831 0.2641 0.6166 0.0952  0.0214  -0.0414 21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.6172 0.2522 0.6186 0.0806  -0.0205 -0.0385 21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.6487 0.2250 0.5930 0.0681  -0.0394 -0.0427 21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.6077 0.2691 0.5892 0.0963  0.0554  -0.0473 21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.6471 0.2985 0.5935 0.0919  0.0604  -0.0462 21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.6371 0.3361 0.6176 0.0989  0.0801  -0.0403 21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.7094 0.3028 0.5839 0.0792  0.0482  -0.0496 21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.6695 0.3443 0.6067 0.0926  0.0809  -0.0410 21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.7134 0.3242 0.5848 0.0810  0.0629  -0.0464 21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.6070 0.2636 0.6450 0.0801  -0.0364 -0.0297 22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.6406 0.2603 0.6670 0.0664  -0.0804 -0.0210 22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.6275 0.2707 0.7472 0.0675  -0.1088 -0.0081 22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.6412 0.2604 0.7763 0.0562  -0.1504 0.0049  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.6485 0.2667 0.6487 0.0639  -0.0763 -0.0181 22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.7143 0.2875 0.6163 0.0573  -0.0576 -0.0276 22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.7256 0.3052 0.6127 0.0565  -0.0502 -0.0241 22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.7763 0.2668 0.5940 0.0373  -0.0894 -0.0293 22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.6003 0.2869 0.7860 0.0802  -0.0859 -0.0095 23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.5734 0.2821 0.8559 0.0835  -0.0989 0.0018  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.6003 0.2709 0.8947 0.0703  -0.1492 0.0110  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.6301 0.2641 0.8589 0.0622  -0.1601 0.0028  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.5434 0.2906 0.8671 0.0966  -0.0610 -0.0040 23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.5886 0.2639 0.9691 0.0667  -0.1793 0.0294  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.6181 0.2591 1.0310 0.0509  -0.2380 0.0455  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.6132 0.2772 1.1146 0.0579  -0.2336 0.0492  24  THR   A C   
137  O  O   . THR   A 18  ? 0.6006 0.3014 1.1216 0.0742  -0.1834 0.0374  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.6120 0.2466 1.0869 0.0423  -0.2771 0.0695  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.5597 0.2422 1.1631 0.0576  -0.2488 0.0798  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.6545 0.2707 1.0499 0.0373  -0.2759 0.0662  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.6209 0.2594 1.1724 0.0434  -0.2883 0.0669  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.6051 0.2651 1.2517 0.0494  -0.2852 0.0728  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.5482 0.2561 1.3314 0.0657  -0.2517 0.0855  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.5283 0.2633 1.3715 0.0785  -0.2146 0.0814  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.6420 0.2587 1.3110 0.0264  -0.3582 0.0916  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.7550 0.3240 1.3114 0.0130  -0.3735 0.0753  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.8007 0.3873 1.3100 0.0283  -0.3186 0.0507  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.8251 0.3242 1.3105 -0.0160 -0.4369 0.0818  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.8609 0.3902 1.2770 0.0107  -0.3439 0.0416  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.8853 0.3562 1.2764 -0.0175 -0.4145 0.0584  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.5207 0.2329 1.3515 0.0644  -0.2614 0.1012  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.4693 0.2167 1.4261 0.0791  -0.2202 0.1124  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.4570 0.2302 1.3710 0.0961  -0.1434 0.0889  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.4328 0.2248 1.4210 0.1075  -0.0963 0.0885  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.4828 0.2255 1.5023 0.0737  -0.2460 0.1355  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.4951 0.2625 1.6816 0.0850  -0.2150 0.1554  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.5042 0.2851 1.7715 0.0928  -0.1902 0.1574  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.4768 0.2468 1.7240 0.0863  -0.2120 0.1714  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.4714 0.2398 1.2632 0.0954  -0.1312 0.0704  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.4422 0.2308 1.1844 0.1068  -0.0691 0.0510  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.4039 0.2036 1.1462 0.1137  -0.0413 0.0406  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.3750 0.1874 1.1437 0.1217  0.0084  0.0361  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.4774 0.2590 1.0990 0.1033  -0.0685 0.0368  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.5038 0.2730 1.1129 0.0967  -0.0900 0.0453  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.4572 0.2350 1.1429 0.1000  -0.0760 0.0566  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.5662 0.3126 1.0883 0.0879  -0.1166 0.0408  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.4110 0.1988 1.1208 0.1089  -0.0724 0.0373  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.4003 0.1978 1.1119 0.1153  -0.0494 0.0287  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.3684 0.1746 1.1982 0.1202  -0.0377 0.0406  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.3664 0.1823 1.2025 0.1274  -0.0023 0.0335  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.4203 0.1961 1.0606 0.1080  -0.0817 0.0209  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.4422 0.2148 0.9745 0.1091  -0.0646 0.0051  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.4846 0.2306 0.9377 0.1002  -0.0857 0.0011  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.4466 0.2410 0.9462 0.1187  -0.0219 -0.0055 28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.5088 0.2614 0.8918 0.1055  -0.0547 -0.0118 28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.4848 0.2692 0.8984 0.1164  -0.0192 -0.0143 28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.4351 0.2519 0.9694 0.1272  0.0132  -0.0065 28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.4968 0.2993 0.8744 0.1231  0.0135  -0.0209 28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.4513 0.2811 0.9355 0.1316  0.0408  -0.0135 28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.4769 0.3027 0.8912 0.1299  0.0390  -0.0192 28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.3390 0.1388 1.2637 0.1151  -0.0698 0.0607  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.3196 0.1265 1.3791 0.1192  -0.0603 0.0769  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.3131 0.1289 1.4422 0.1295  0.0029  0.0801  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2978 0.1156 1.5408 0.1348  0.0279  0.0919  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.3068 0.1009 1.4506 0.1069  -0.1277 0.1026  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.3192 0.1341 1.3858 0.1304  0.0274  0.0714  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.3020 0.1124 1.3963 0.1363  0.0915  0.0691  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.3179 0.1259 1.2786 0.1353  0.1233  0.0472  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.3249 0.1258 1.2566 0.1335  0.1451  0.0439  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.3043 0.1114 1.4777 0.1348  0.0795  0.0873  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.3076 0.1178 1.6237 0.1336  0.0410  0.1144  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.3220 0.1336 1.7187 0.1385  0.0626  0.1198  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.3038 0.1127 1.6467 0.1248  -0.0223 0.1327  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.3303 0.1439 1.2130 0.1352  0.1204  0.0342  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.3456 0.1600 1.1124 0.1326  0.1394  0.0186  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.3504 0.1459 1.0980 0.1307  0.2013  0.0125  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.3491 0.1324 1.1404 0.1330  0.2332  0.0139  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.3444 0.1689 1.0600 0.1336  0.1191  0.0116  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.3742 0.2027 0.9929 0.1315  0.1379  0.0006  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.3980 0.2340 0.9452 0.1283  0.1132  -0.0037 31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.3446 0.1795 0.9545 0.1349  0.1348  -0.0019 31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.3554 0.1421 1.0270 0.1239  0.2184  0.0053  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.3665 0.1219 0.9900 0.1158  0.2722  -0.0014 32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.3757 0.1364 0.8975 0.1086  0.2633  -0.0079 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.4014 0.1436 0.8981 0.1040  0.2877  -0.0094 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.4017 0.1337 1.0082 0.1088  0.2995  -0.0034 32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.4596 0.1459 0.9855 0.0940  0.3503  -0.0118 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.3711 0.0959 1.0941 0.1161  0.3143  0.0068  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.3512 0.1353 0.8214 0.1076  0.2279  -0.0094 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.3402 0.1334 0.7322 0.1011  0.2168  -0.0108 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.3092 0.1330 0.6857 0.1067  0.1761  -0.0107 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.3051 0.1326 0.6933 0.1087  0.1619  -0.0112 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.3666 0.1304 0.6882 0.0842  0.2421  -0.0124 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.3823 0.1570 0.6325 0.0742  0.2220  -0.0088 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.4053 0.1789 0.6201 0.0670  0.2168  -0.0025 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.3723 0.1633 0.5912 0.0707  0.2015  -0.0079 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.4119 0.2012 0.5836 0.0588  0.1932  0.0045  33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.3942 0.1946 0.5676 0.0614  0.1854  0.0004  33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.3555 0.1556 0.5877 0.0752  0.1928  -0.0112 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.3950 0.2125 0.5407 0.0561  0.1657  0.0053  33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.3763 0.1894 0.5681 0.0694  0.1760  -0.0088 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.3848 0.2079 0.5381 0.0606  0.1634  -0.0007 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2955 0.1360 0.6464 0.1086  0.1608  -0.0092 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2792 0.1379 0.6106 0.1129  0.1342  -0.0099 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.2984 0.1700 0.5916 0.1091  0.1336  -0.0044 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.2934 0.1628 0.5857 0.1061  0.1431  0.0007  34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2547 0.1173 0.6200 0.1192  0.1115  -0.0120 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2613 0.1224 0.6639 0.1252  0.1162  -0.0115 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2736 0.1441 0.6529 0.1295  0.1151  -0.0109 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2606 0.1326 0.6530 0.1304  0.1280  -0.0076 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.2725 0.1473 0.6211 0.1305  0.1044  -0.0123 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.2904 0.1726 0.5565 0.1076  0.1235  -0.0027 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.3011 0.1982 0.5507 0.1041  0.1211  0.0073  35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.2932 0.2004 0.5421 0.1117  0.1135  0.0063  35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.2985 0.2074 0.5284 0.1084  0.1116  0.0067  35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.3352 0.2266 0.5501 0.0876  0.1244  0.0157  35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.3717 0.2756 0.5792 0.0790  0.1151  0.0329  35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.3385 0.2634 0.5735 0.0885  0.1092  0.0389  35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.4262 0.3133 0.5997 0.0606  0.1136  0.0420  35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.2812 0.1903 0.5481 0.1208  0.1136  0.0053  36  SER   A N   
241  C  CA  . SER   A 30  ? 0.2916 0.1989 0.5545 0.1271  0.1170  0.0043  36  SER   A CA  
242  C  C   . SER   A 30  ? 0.2753 0.1983 0.5363 0.1229  0.1222  0.0162  36  SER   A C   
243  O  O   . SER   A 30  ? 0.2681 0.1813 0.5123 0.1244  0.1275  0.0118  36  SER   A O   
244  C  CB  . SER   A 30  ? 0.3170 0.2249 0.6041 0.1349  0.1238  0.0062  36  SER   A CB  
245  O  OG  . SER   A 30  ? 0.3712 0.2514 0.6455 0.1394  0.1211  -0.0078 36  SER   A OG  
246  N  N   . SER   A 31  ? 0.2642 0.2069 0.5413 0.1153  0.1185  0.0330  37  SER   A N   
247  C  CA  . SER   A 31  ? 0.2646 0.2239 0.5533 0.1090  0.1171  0.0493  37  SER   A CA  
248  C  C   . SER   A 31  ? 0.2637 0.2182 0.5206 0.1003  0.1128  0.0453  37  SER   A C   
249  O  O   . SER   A 31  ? 0.2584 0.2239 0.5274 0.0972  0.1138  0.0559  37  SER   A O   
250  C  CB  . SER   A 31  ? 0.2792 0.2555 0.5928 0.0987  0.1046  0.0731  37  SER   A CB  
251  O  OG  . SER   A 31  ? 0.3355 0.3010 0.6110 0.0810  0.0911  0.0762  37  SER   A OG  
252  N  N   . ARG   A 32  ? 0.2727 0.2109 0.4983 0.0970  0.1103  0.0316  38  ARG   A N   
253  C  CA  . ARG   A 32  ? 0.2868 0.2171 0.4834 0.0894  0.1085  0.0266  38  ARG   A CA  
254  C  C   . ARG   A 32  ? 0.3050 0.2186 0.4874 0.0982  0.1112  0.0109  38  ARG   A C   
255  O  O   . ARG   A 32  ? 0.3193 0.2263 0.4815 0.0935  0.1099  0.0075  38  ARG   A O   
256  C  CB  . ARG   A 32  ? 0.2914 0.2074 0.4642 0.0765  0.1075  0.0249  38  ARG   A CB  
257  C  CG  . ARG   A 32  ? 0.3053 0.2213 0.4665 0.0595  0.0999  0.0413  38  ARG   A CG  
258  C  CD  . ARG   A 32  ? 0.3519 0.2360 0.4712 0.0433  0.1069  0.0371  38  ARG   A CD  
259  N  NE  . ARG   A 32  ? 0.3847 0.2555 0.4756 0.0351  0.1113  0.0308  38  ARG   A NE  
260  C  CZ  . ARG   A 32  ? 0.4401 0.2766 0.4834 0.0150  0.1188  0.0300  38  ARG   A CZ  
261  N  NH1 . ARG   A 32  ? 0.4407 0.2472 0.4502 -0.0013 0.1219  0.0356  38  ARG   A NH1 
262  N  NH2 . ARG   A 32  ? 0.4464 0.2709 0.4683 0.0090  0.1249  0.0236  38  ARG   A NH2 
263  N  N   . ASP   A 33  ? 0.3113 0.2133 0.5006 0.1083  0.1116  0.0026  39  ASP   A N   
264  C  CA  . ASP   A 33  ? 0.3276 0.2033 0.4963 0.1119  0.1052  -0.0094 39  ASP   A CA  
265  C  C   . ASP   A 33  ? 0.3236 0.1931 0.4956 0.1077  0.0953  -0.0129 39  ASP   A C   
266  O  O   . ASP   A 33  ? 0.3350 0.1882 0.4897 0.1057  0.0867  -0.0167 39  ASP   A O   
267  C  CB  . ASP   A 33  ? 0.3583 0.2195 0.4967 0.1115  0.1123  -0.0111 39  ASP   A CB  
268  C  CG  . ASP   A 33  ? 0.4331 0.2550 0.5338 0.1102  0.1011  -0.0214 39  ASP   A CG  
269  O  OD1 . ASP   A 33  ? 0.4403 0.2417 0.5387 0.1114  0.0894  -0.0268 39  ASP   A OD1 
270  O  OD2 . ASP   A 33  ? 0.4919 0.3008 0.5642 0.1058  0.1000  -0.0225 39  ASP   A OD2 
271  N  N   . LEU   A 34  ? 0.2993 0.1770 0.4954 0.1057  0.0995  -0.0104 40  LEU   A N   
272  C  CA  . LEU   A 34  ? 0.2823 0.1494 0.4935 0.1025  0.1001  -0.0129 40  LEU   A CA  
273  C  C   . LEU   A 34  ? 0.2706 0.1306 0.5250 0.1074  0.0987  -0.0143 40  LEU   A C   
274  O  O   . LEU   A 34  ? 0.2592 0.1248 0.5264 0.1106  0.1027  -0.0134 40  LEU   A O   
275  C  CB  . LEU   A 34  ? 0.2882 0.1557 0.4848 0.0918  0.1165  -0.0094 40  LEU   A CB  
276  C  CG  . LEU   A 34  ? 0.3126 0.1818 0.4758 0.0833  0.1172  -0.0072 40  LEU   A CG  
277  C  CD1 . LEU   A 34  ? 0.3097 0.1643 0.4506 0.0682  0.1332  -0.0051 40  LEU   A CD1 
278  C  CD2 . LEU   A 34  ? 0.3138 0.1740 0.4772 0.0868  0.1090  -0.0117 40  LEU   A CD2 
279  N  N   . LEU   A 35  ? 0.2665 0.1146 0.5521 0.1075  0.0943  -0.0143 41  LEU   A N   
280  C  CA  . LEU   A 35  ? 0.2619 0.1042 0.6051 0.1115  0.0948  -0.0124 41  LEU   A CA  
281  C  C   . LEU   A 35  ? 0.2702 0.1016 0.6530 0.1093  0.1060  -0.0089 41  LEU   A C   
282  O  O   . LEU   A 35  ? 0.2654 0.0945 0.6425 0.1059  0.0911  -0.0065 41  LEU   A O   
283  C  CB  . LEU   A 35  ? 0.2672 0.1025 0.6270 0.1154  0.0631  -0.0118 41  LEU   A CB  
284  C  CG  . LEU   A 35  ? 0.2799 0.1129 0.7051 0.1191  0.0609  -0.0081 41  LEU   A CG  
285  C  CD1 . LEU   A 35  ? 0.2947 0.1179 0.7152 0.1196  0.0321  -0.0092 41  LEU   A CD1 
286  C  CD2 . LEU   A 35  ? 0.2760 0.1012 0.7737 0.1185  0.0564  0.0010  41  LEU   A CD2 
287  N  N   . VAL   A 36  ? 0.2871 0.1095 0.7063 0.1088  0.1371  -0.0080 42  VAL   A N   
288  C  CA  . VAL   A 36  ? 0.2938 0.0996 0.7682 0.1081  0.1588  -0.0037 42  VAL   A CA  
289  C  C   . VAL   A 36  ? 0.2949 0.0988 0.8656 0.1153  0.1545  0.0047  42  VAL   A C   
290  O  O   . VAL   A 36  ? 0.2961 0.1022 0.8800 0.1182  0.1606  0.0035  42  VAL   A O   
291  C  CB  . VAL   A 36  ? 0.3199 0.1016 0.7607 0.0990  0.2070  -0.0090 42  VAL   A CB  
292  C  CG1 . VAL   A 36  ? 0.3290 0.0871 0.8291 0.0989  0.2377  -0.0054 42  VAL   A CG1 
293  C  CG2 . VAL   A 36  ? 0.3524 0.1365 0.7041 0.0890  0.2032  -0.0139 42  VAL   A CG2 
294  N  N   . SER   A 37  ? 0.2988 0.0974 0.9460 0.1175  0.1463  0.0157  43  SER   A N   
295  C  CA  . SER   A 37  ? 0.3020 0.0999 1.0585 0.1229  0.1391  0.0287  43  SER   A CA  
296  C  C   . SER   A 37  ? 0.3265 0.1100 1.1779 0.1248  0.1686  0.0405  43  SER   A C   
297  O  O   . SER   A 37  ? 0.3185 0.0954 1.1505 0.1218  0.1758  0.0404  43  SER   A O   
298  C  CB  . SER   A 37  ? 0.2926 0.0995 1.0644 0.1218  0.0745  0.0380  43  SER   A CB  
299  O  OG  . SER   A 37  ? 0.3194 0.1229 1.0577 0.1167  0.0439  0.0418  43  SER   A OG  
300  N  N   . SER   A 38  ? 0.3415 0.1201 1.3032 0.1302  0.1863  0.0518  44  SER   A N   
301  C  CA  . SER   A 38  ? 0.3750 0.1373 1.4573 0.1343  0.2263  0.0657  44  SER   A CA  
302  C  C   . SER   A 38  ? 0.4015 0.1732 1.5799 0.1350  0.1834  0.0891  44  SER   A C   
303  O  O   . SER   A 38  ? 0.3972 0.1846 1.6082 0.1327  0.1167  0.1034  44  SER   A O   
304  C  CB  . SER   A 38  ? 0.3592 0.1150 1.5350 0.1401  0.2562  0.0722  44  SER   A CB  
305  O  OG  . SER   A 38  ? 0.3728 0.1386 1.4853 0.1396  0.2413  0.0612  44  SER   A OG  
306  N  N   . THR   A 39  ? 0.4357 0.1915 1.6626 0.1364  0.2216  0.0949  45  THR   A N   
307  C  CA  . THR   A 39  ? 0.4424 0.2050 1.7769 0.1370  0.1847  0.1216  45  THR   A CA  
308  C  C   . THR   A 39  ? 0.4446 0.1899 1.9350 0.1446  0.2443  0.1385  45  THR   A C   
309  O  O   . THR   A 39  ? 0.4701 0.1873 1.9419 0.1469  0.3239  0.1224  45  THR   A O   
310  C  CB  . THR   A 39  ? 0.4830 0.2430 1.7322 0.1316  0.1707  0.1155  45  THR   A CB  
311  O  OG1 . THR   A 39  ? 0.5135 0.2479 1.7687 0.1334  0.2448  0.1074  45  THR   A OG1 
312  C  CG2 . THR   A 39  ? 0.5370 0.3054 1.6200 0.1251  0.1427  0.0927  45  THR   A CG2 
313  N  N   . THR   A 40  ? 0.4209 0.1759 2.0613 0.1467  0.2098  0.1718  46  THR   A N   
314  C  CA  . THR   A 40  ? 0.4025 0.1411 2.2130 0.1554  0.2709  0.1917  46  THR   A CA  
315  C  C   . THR   A 40  ? 0.4201 0.1399 2.2416 0.1561  0.3079  0.1939  46  THR   A C   
316  O  O   . THR   A 40  ? 0.4238 0.1092 2.2952 0.1614  0.3980  0.1890  46  THR   A O   
317  C  CB  . THR   A 40  ? 0.3686 0.1288 2.3656 0.1572  0.2156  0.2320  46  THR   A CB  
318  O  OG1 . THR   A 40  ? 0.3806 0.1573 2.3960 0.1487  0.1264  0.2565  46  THR   A OG1 
319  C  CG2 . THR   A 40  ? 0.3763 0.1506 2.3578 0.1553  0.1823  0.2283  46  THR   A CG2 
320  N  N   . ALA   A 41  ? 0.4267 0.1626 2.2003 0.1498  0.2411  0.2014  47  ALA   A N   
321  C  CA  . ALA   A 41  ? 0.4279 0.1485 2.1914 0.1494  0.2680  0.2013  47  ALA   A CA  
322  C  C   . ALA   A 41  ? 0.5017 0.1975 2.0851 0.1450  0.3264  0.1602  47  ALA   A C   
323  O  O   . ALA   A 41  ? 0.5447 0.2489 1.9918 0.1398  0.3070  0.1372  47  ALA   A O   
324  C  CB  . ALA   A 41  ? 0.4278 0.1691 2.1708 0.1417  0.1750  0.2197  47  ALA   A CB  
325  N  N   . GLN   A 42  ? 0.5172 0.1789 2.1045 0.1454  0.3976  0.1529  48  GLN   A N   
326  C  CA  . GLN   A 42  ? 0.5920 0.2200 2.0148 0.1366  0.4519  0.1179  48  GLN   A CA  
327  C  C   . GLN   A 42  ? 0.6107 0.2572 1.9095 0.1289  0.3976  0.1091  48  GLN   A C   
328  O  O   . GLN   A 42  ? 0.5990 0.2541 1.9564 0.1307  0.3712  0.1274  48  GLN   A O   
329  C  CB  . GLN   A 42  ? 0.6245 0.1952 2.1015 0.1373  0.5551  0.1140  48  GLN   A CB  
330  C  CG  . GLN   A 42  ? 0.7662 0.2940 2.0961 0.1244  0.6021  0.0866  48  GLN   A CG  
331  C  CD  . GLN   A 42  ? 0.9415 0.4348 2.1059 0.1105  0.6363  0.0546  48  GLN   A CD  
332  O  OE1 . GLN   A 42  ? 0.9769 0.4648 2.1430 0.1116  0.6504  0.0504  48  GLN   A OE1 
333  N  NE2 . GLN   A 42  ? 1.0141 0.4824 2.0327 0.0956  0.6458  0.0337  48  GLN   A NE2 
334  N  N   . GLY   A 43  ? 0.6335 0.2838 1.7716 0.1203  0.3842  0.0835  49  GLY   A N   
335  C  CA  . GLY   A 43  ? 0.6466 0.3111 1.6614 0.1126  0.3429  0.0727  49  GLY   A CA  
336  C  C   . GLY   A 43  ? 0.6422 0.2706 1.5936 0.1044  0.3964  0.0583  49  GLY   A C   
337  O  O   . GLY   A 43  ? 0.6602 0.2428 1.6134 0.1004  0.4715  0.0479  49  GLY   A O   
338  N  N   . CYS   A 44  ? 0.6303 0.2712 1.5182 0.0998  0.3619  0.0569  50  CYS   A N   
339  C  CA  . CYS   A 44  ? 0.6399 0.2452 1.4805 0.0913  0.4102  0.0459  50  CYS   A CA  
340  C  C   . CYS   A 44  ? 0.6505 0.2570 1.3380 0.0781  0.3947  0.0261  50  CYS   A C   
341  O  O   . CYS   A 44  ? 0.6744 0.2508 1.3189 0.0690  0.4284  0.0177  50  CYS   A O   
342  C  CB  . CYS   A 44  ? 0.6277 0.2353 1.5798 0.0986  0.4032  0.0686  50  CYS   A CB  
343  S  SG  . CYS   A 44  ? 0.7029 0.2698 1.8189 0.1070  0.4839  0.0831  50  CYS   A SG  
344  N  N   . ASP   A 45  ? 0.6234 0.2608 1.2343 0.0763  0.3482  0.0195  51  ASP   A N   
345  C  CA  . ASP   A 45  ? 0.6317 0.2737 1.1152 0.0642  0.3329  0.0047  51  ASP   A CA  
346  C  C   . ASP   A 45  ? 0.6319 0.2324 1.0260 0.0474  0.3823  -0.0138 51  ASP   A C   
347  O  O   . ASP   A 45  ? 0.6387 0.2210 1.0347 0.0457  0.4085  -0.0183 51  ASP   A O   
348  C  CB  . ASP   A 45  ? 0.6648 0.3489 1.1061 0.0680  0.2730  0.0057  51  ASP   A CB  
349  C  CG  . ASP   A 45  ? 0.7061 0.4167 1.2016 0.0780  0.2182  0.0226  51  ASP   A CG  
350  O  OD1 . ASP   A 45  ? 0.7226 0.4257 1.2868 0.0815  0.2172  0.0361  51  ASP   A OD1 
351  O  OD2 . ASP   A 45  ? 0.7143 0.4471 1.1811 0.0805  0.1761  0.0233  51  ASP   A OD2 
352  N  N   . THR   A 46  ? 0.6367 0.2192 0.9452 0.0325  0.3900  -0.0233 52  THR   A N   
353  C  CA  . THR   A 46  ? 0.6676 0.2029 0.8720 0.0097  0.4248  -0.0386 52  THR   A CA  
354  C  C   . THR   A 46  ? 0.6594 0.2281 0.7863 0.0029  0.3779  -0.0405 52  THR   A C   
355  O  O   . THR   A 46  ? 0.6561 0.2670 0.7771 0.0087  0.3343  -0.0354 52  THR   A O   
356  C  CB  . THR   A 46  ? 0.7091 0.2007 0.8656 -0.0062 0.4566  -0.0459 52  THR   A CB  
357  O  OG1 . THR   A 46  ? 0.7038 0.1473 0.9252 -0.0035 0.5181  -0.0462 52  THR   A OG1 
358  C  CG2 . THR   A 46  ? 0.7739 0.2215 0.7987 -0.0359 0.4674  -0.0587 52  THR   A CG2 
359  N  N   . ILE   A 47  ? 0.6589 0.2055 0.7297 -0.0097 0.3884  -0.0461 53  ILE   A N   
360  C  CA  . ILE   A 47  ? 0.6617 0.2379 0.6707 -0.0171 0.3460  -0.0442 53  ILE   A CA  
361  C  C   . ILE   A 47  ? 0.6991 0.2339 0.6035 -0.0471 0.3521  -0.0493 53  ILE   A C   
362  O  O   . ILE   A 47  ? 0.7368 0.2030 0.5922 -0.0665 0.3966  -0.0578 53  ILE   A O   
363  C  CB  . ILE   A 47  ? 0.6619 0.2407 0.6774 -0.0139 0.3457  -0.0432 53  ILE   A CB  
364  C  CG1 . ILE   A 47  ? 0.6285 0.2363 0.7501 0.0119  0.3442  -0.0378 53  ILE   A CG1 
365  C  CG2 . ILE   A 47  ? 0.6634 0.2754 0.6314 -0.0197 0.3022  -0.0379 53  ILE   A CG2 
366  C  CD1 . ILE   A 47  ? 0.6128 0.2796 0.7796 0.0300  0.2936  -0.0296 53  ILE   A CD1 
367  N  N   . ALA   A 48  ? 0.6910 0.2601 0.5610 -0.0529 0.3097  -0.0434 54  ALA   A N   
368  C  CA  . ALA   A 48  ? 0.7298 0.2630 0.5081 -0.0840 0.3047  -0.0438 54  ALA   A CA  
369  C  C   . ALA   A 48  ? 0.7735 0.2739 0.4844 -0.1068 0.2990  -0.0407 54  ALA   A C   
370  O  O   . ALA   A 48  ? 0.7531 0.2898 0.4933 -0.0950 0.2772  -0.0338 54  ALA   A O   
371  C  CB  . ALA   A 48  ? 0.6929 0.2768 0.4755 -0.0817 0.2615  -0.0347 54  ALA   A CB  
372  N  N   . ARG   A 49  ? 0.8408 0.2676 0.4556 -0.1417 0.3161  -0.0449 55  ARG   A N   
373  C  CA  . ARG   A 49  ? 0.8975 0.2759 0.4244 -0.1729 0.3046  -0.0393 55  ARG   A CA  
374  C  C   . ARG   A 49  ? 0.9420 0.3020 0.3947 -0.2061 0.2681  -0.0299 55  ARG   A C   
375  O  O   . ARG   A 49  ? 1.0054 0.2854 0.3689 -0.2379 0.2909  -0.0378 55  ARG   A O   
376  C  CB  . ARG   A 49  ? 0.9625 0.2471 0.4291 -0.1900 0.3638  -0.0531 55  ARG   A CB  
377  C  CG  . ARG   A 49  ? 0.9542 0.2567 0.5094 -0.1577 0.4017  -0.0598 55  ARG   A CG  
378  C  CD  . ARG   A 49  ? 0.9223 0.2984 0.5461 -0.1333 0.3648  -0.0490 55  ARG   A CD  
379  N  NE  . ARG   A 49  ? 0.8900 0.2705 0.5925 -0.1080 0.4028  -0.0551 55  ARG   A NE  
380  C  CZ  . ARG   A 49  ? 0.8450 0.2877 0.6267 -0.0815 0.3805  -0.0488 55  ARG   A CZ  
381  N  NH1 . ARG   A 49  ? 0.7740 0.2761 0.5633 -0.0758 0.3266  -0.0377 55  ARG   A NH1 
382  N  NH2 . ARG   A 49  ? 0.8242 0.2655 0.6806 -0.0617 0.4141  -0.0525 55  ARG   A NH2 
383  N  N   . CYS   A 50  ? 0.8987 0.3317 0.3960 -0.1979 0.2139  -0.0126 56  CYS   A N   
384  C  CA  . CYS   A 50  ? 0.9155 0.3548 0.3828 -0.2213 0.1736  0.0009  56  CYS   A CA  
385  C  C   . CYS   A 50  ? 0.8827 0.3951 0.4086 -0.2132 0.1192  0.0246  56  CYS   A C   
386  O  O   . CYS   A 50  ? 0.8469 0.4053 0.4340 -0.1869 0.1164  0.0274  56  CYS   A O   
387  C  CB  . CYS   A 50  ? 0.8922 0.3570 0.4006 -0.2041 0.1892  -0.0084 56  CYS   A CB  
388  S  SG  . CYS   A 50  ? 0.8781 0.4492 0.5140 -0.1547 0.1742  -0.0040 56  CYS   A SG  
389  N  N   . ASP   A 51  ? 0.8786 0.4065 0.4015 -0.2318 0.0803  0.0415  57  ASP   A N   
390  C  CA  . ASP   A 51  ? 0.8316 0.4301 0.4300 -0.2219 0.0365  0.0658  57  ASP   A CA  
391  C  C   . ASP   A 51  ? 0.7825 0.4261 0.4339 -0.2111 0.0282  0.0701  57  ASP   A C   
392  O  O   . ASP   A 51  ? 0.7714 0.4370 0.4474 -0.2268 -0.0106 0.0937  57  ASP   A O   
393  C  CB  . ASP   A 51  ? 0.8921 0.4687 0.4554 -0.2576 -0.0121 0.0931  57  ASP   A CB  
394  C  CG  . ASP   A 51  ? 1.0261 0.5561 0.5236 -0.3042 -0.0492 0.1096  57  ASP   A CG  
395  O  OD1 . ASP   A 51  ? 1.0802 0.5694 0.5245 -0.3166 -0.0278 0.0937  57  ASP   A OD1 
396  O  OD2 . ASP   A 51  ? 1.0687 0.6013 0.5713 -0.3297 -0.1020 0.1404  57  ASP   A OD2 
397  N  N   . CYS   A 52  ? 0.7489 0.4049 0.4231 -0.1849 0.0642  0.0496  58  CYS   A N   
398  C  CA  . CYS   A 52  ? 0.6974 0.3921 0.4181 -0.1720 0.0621  0.0517  58  CYS   A CA  
399  C  C   . CYS   A 52  ? 0.6186 0.3814 0.4268 -0.1474 0.0457  0.0666  58  CYS   A C   
400  O  O   . CYS   A 52  ? 0.6159 0.3999 0.4550 -0.1306 0.0462  0.0682  58  CYS   A O   
401  C  CB  . CYS   A 52  ? 0.7028 0.3905 0.4272 -0.1501 0.1014  0.0289  58  CYS   A CB  
402  S  SG  . CYS   A 52  ? 0.7993 0.4047 0.4352 -0.1775 0.1320  0.0116  58  CYS   A SG  
403  N  N   . GLN   A 53  ? 0.5629 0.3549 0.4106 -0.1451 0.0365  0.0768  59  GLN   A N   
404  C  CA  . GLN   A 53  ? 0.5027 0.3499 0.4335 -0.1208 0.0336  0.0890  59  GLN   A CA  
405  C  C   . GLN   A 53  ? 0.4729 0.3366 0.4283 -0.1008 0.0561  0.0798  59  GLN   A C   
406  O  O   . GLN   A 53  ? 0.4304 0.3266 0.4446 -0.0905 0.0558  0.0928  59  GLN   A O   
407  C  CB  . GLN   A 53  ? 0.4961 0.3651 0.4724 -0.1400 -0.0032 0.1210  59  GLN   A CB  
408  C  CG  . GLN   A 53  ? 0.5263 0.3958 0.5083 -0.1469 -0.0242 0.1342  59  GLN   A CG  
409  C  CD  . GLN   A 53  ? 0.5501 0.4414 0.5896 -0.1677 -0.0660 0.1711  59  GLN   A CD  
410  O  OE1 . GLN   A 53  ? 0.6063 0.4651 0.6025 -0.2050 -0.1042 0.1880  59  GLN   A OE1 
411  N  NE2 . GLN   A 53  ? 0.5017 0.4425 0.6406 -0.1463 -0.0593 0.1863  59  GLN   A NE2 
412  N  N   . THR   A 54  ? 0.4904 0.3262 0.4014 -0.0976 0.0771  0.0593  60  THR   A N   
413  C  CA  . THR   A 54  ? 0.4753 0.3161 0.3956 -0.0798 0.0978  0.0489  60  THR   A CA  
414  C  C   . THR   A 54  ? 0.4592 0.2776 0.3540 -0.0658 0.1179  0.0287  60  THR   A C   
415  O  O   . THR   A 54  ? 0.4708 0.2584 0.3297 -0.0779 0.1230  0.0211  60  THR   A O   
416  C  CB  . THR   A 54  ? 0.5137 0.3414 0.4161 -0.0979 0.0958  0.0519  60  THR   A CB  
417  O  OG1 . THR   A 54  ? 0.5719 0.3552 0.4134 -0.1177 0.1007  0.0407  60  THR   A OG1 
418  C  CG2 . THR   A 54  ? 0.4990 0.3484 0.4385 -0.1153 0.0716  0.0761  60  THR   A CG2 
419  N  N   . GLY   A 55  ? 0.4353 0.2630 0.3488 -0.0426 0.1298  0.0220  61  GLY   A N   
420  C  CA  . GLY   A 55  ? 0.4464 0.2568 0.3535 -0.0286 0.1420  0.0085  61  GLY   A CA  
421  C  C   . GLY   A 55  ? 0.4452 0.2587 0.3634 -0.0100 0.1459  0.0060  61  GLY   A C   
422  O  O   . GLY   A 55  ? 0.4548 0.2757 0.3745 -0.0101 0.1473  0.0116  61  GLY   A O   
423  N  N   . VAL   A 56  ? 0.4246 0.2270 0.3497 0.0038  0.1465  -0.0006 62  VAL   A N   
424  C  CA  . VAL   A 56  ? 0.4254 0.2175 0.3494 0.0173  0.1422  -0.0013 62  VAL   A CA  
425  C  C   . VAL   A 56  ? 0.4280 0.2181 0.3645 0.0297  0.1318  -0.0031 62  VAL   A C   
426  O  O   . VAL   A 56  ? 0.4192 0.2076 0.3765 0.0312  0.1308  -0.0056 62  VAL   A O   
427  C  CB  . VAL   A 56  ? 0.4411 0.2119 0.3630 0.0162  0.1452  -0.0026 62  VAL   A CB  
428  C  CG1 . VAL   A 56  ? 0.4521 0.2046 0.3685 0.0266  0.1312  0.0004  62  VAL   A CG1 
429  C  CG2 . VAL   A 56  ? 0.4583 0.2278 0.3629 0.0042  0.1551  -0.0013 62  VAL   A CG2 
430  N  N   . TYR   A 57  ? 0.4375 0.2209 0.3588 0.0371  0.1268  -0.0019 63  TYR   A N   
431  C  CA  . TYR   A 57  ? 0.4304 0.2036 0.3538 0.0457  0.1141  -0.0036 63  TYR   A CA  
432  C  C   . TYR   A 57  ? 0.4471 0.1833 0.3414 0.0477  0.0983  -0.0020 63  TYR   A C   
433  O  O   . TYR   A 57  ? 0.4404 0.1580 0.3028 0.0442  0.1028  -0.0003 63  TYR   A O   
434  C  CB  . TYR   A 57  ? 0.4277 0.2135 0.3514 0.0495  0.1216  -0.0038 63  TYR   A CB  
435  C  CG  . TYR   A 57  ? 0.4601 0.2261 0.3527 0.0515  0.1339  -0.0033 63  TYR   A CG  
436  C  CD1 . TYR   A 57  ? 0.4591 0.2363 0.3560 0.0475  0.1525  0.0016  63  TYR   A CD1 
437  C  CD2 . TYR   A 57  ? 0.4933 0.2251 0.3537 0.0557  0.1304  -0.0071 63  TYR   A CD2 
438  C  CE1 . TYR   A 57  ? 0.4910 0.2462 0.3676 0.0501  0.1737  0.0025  63  TYR   A CE1 
439  C  CE2 . TYR   A 57  ? 0.5327 0.2322 0.3543 0.0556  0.1512  -0.0083 63  TYR   A CE2 
440  C  CZ  . TYR   A 57  ? 0.5377 0.2497 0.3713 0.0540  0.1765  -0.0036 63  TYR   A CZ  
441  O  OH  . TYR   A 57  ? 0.5839 0.2603 0.3870 0.0546  0.2065  -0.0044 63  TYR   A OH  
442  N  N   . TYR   A 58  ? 0.4610 0.1827 0.3648 0.0510  0.0770  -0.0007 64  TYR   A N   
443  C  CA  . TYR   A 58  ? 0.4983 0.1771 0.3697 0.0479  0.0516  0.0045  64  TYR   A CA  
444  C  C   . TYR   A 58  ? 0.5379 0.1845 0.3553 0.0467  0.0499  0.0002  64  TYR   A C   
445  O  O   . TYR   A 58  ? 0.5105 0.1702 0.3424 0.0513  0.0535  -0.0041 64  TYR   A O   
446  C  CB  . TYR   A 58  ? 0.4825 0.1570 0.4019 0.0484  0.0233  0.0132  64  TYR   A CB  
447  C  CG  . TYR   A 58  ? 0.5309 0.1555 0.4131 0.0406  -0.0141 0.0230  64  TYR   A CG  
448  C  CD1 . TYR   A 58  ? 0.5746 0.1687 0.4193 0.0332  -0.0231 0.0299  64  TYR   A CD1 
449  C  CD2 . TYR   A 58  ? 0.5557 0.1559 0.4259 0.0376  -0.0413 0.0254  64  TYR   A CD2 
450  C  CE1 . TYR   A 58  ? 0.6297 0.1668 0.4250 0.0212  -0.0621 0.0409  64  TYR   A CE1 
451  C  CE2 . TYR   A 58  ? 0.6084 0.1503 0.4270 0.0245  -0.0810 0.0355  64  TYR   A CE2 
452  C  CZ  . TYR   A 58  ? 0.6605 0.1688 0.4388 0.0155  -0.0926 0.0439  64  TYR   A CZ  
453  O  OH  . TYR   A 58  ? 0.7379 0.1779 0.4527 -0.0020 -0.1372 0.0562  64  TYR   A OH  
454  N  N   . CYS   A 59  ? 0.6067 0.2029 0.3560 0.0390  0.0466  0.0013  65  CYS   A N   
455  C  CA  . CYS   A 59  ? 0.6621 0.2097 0.3434 0.0347  0.0540  -0.0045 65  CYS   A CA  
456  C  C   . CYS   A 59  ? 0.7340 0.2121 0.3520 0.0210  0.0147  0.0013  65  CYS   A C   
457  O  O   . CYS   A 59  ? 0.7835 0.2163 0.3444 0.0108  0.0088  0.0058  65  CYS   A O   
458  C  CB  . CYS   A 59  ? 0.6831 0.2175 0.3268 0.0342  0.0947  -0.0090 65  CYS   A CB  
459  S  SG  . CYS   A 59  ? 0.7819 0.2457 0.3414 0.0290  0.1235  -0.0180 65  CYS   A SG  
460  N  N   . SER   A 60  ? 0.7353 0.2004 0.3600 0.0182  -0.0151 0.0030  66  SER   A N   
461  C  CA  . SER   A 60  ? 0.7960 0.1910 0.3625 0.0005  -0.0636 0.0123  66  SER   A CA  
462  C  C   . SER   A 60  ? 0.8881 0.1931 0.3275 -0.0165 -0.0550 0.0076  66  SER   A C   
463  O  O   . SER   A 60  ? 0.9391 0.1844 0.3213 -0.0343 -0.0931 0.0194  66  SER   A O   
464  C  CB  . SER   A 60  ? 0.8019 0.1919 0.3868 -0.0014 -0.0899 0.0125  66  SER   A CB  
465  O  OG  . SER   A 60  ? 0.7906 0.2546 0.4675 0.0164  -0.0710 0.0076  66  SER   A OG  
466  N  N   . SER   A 61  ? 0.9132 0.2013 0.3084 -0.0126 -0.0043 -0.0080 67  SER   A N   
467  C  CA  . SER   A 61  ? 0.9920 0.1839 0.2617 -0.0283 0.0212  -0.0159 67  SER   A CA  
468  C  C   . SER   A 61  ? 1.0103 0.1759 0.2367 -0.0338 0.0373  -0.0123 67  SER   A C   
469  O  O   . SER   A 61  ? 1.0828 0.1492 0.1885 -0.0529 0.0468  -0.0152 67  SER   A O   
470  C  CB  . SER   A 61  ? 1.0200 0.2100 0.2823 -0.0189 0.0803  -0.0314 67  SER   A CB  
471  O  OG  . SER   A 61  ? 1.0054 0.2606 0.3363 -0.0011 0.1289  -0.0337 67  SER   A OG  
472  N  N   . ARG   A 62  ? 0.9417 0.1839 0.2551 -0.0206 0.0378  -0.0055 68  ARG   A N   
473  C  CA  . ARG   A 62  ? 0.9589 0.1843 0.2441 -0.0251 0.0479  -0.0003 68  ARG   A CA  
474  C  C   . ARG   A 62  ? 0.9579 0.2146 0.2965 -0.0264 -0.0004 0.0160  68  ARG   A C   
475  O  O   . ARG   A 62  ? 0.9537 0.2084 0.2849 -0.0279 0.0073  0.0211  68  ARG   A O   
476  C  CB  . ARG   A 62  ? 0.9149 0.1990 0.2557 -0.0089 0.1049  -0.0073 68  ARG   A CB  
477  C  CG  . ARG   A 62  ? 0.9720 0.2149 0.2643 -0.0084 0.1635  -0.0190 68  ARG   A CG  
478  C  CD  . ARG   A 62  ? 1.0851 0.2150 0.2461 -0.0271 0.1844  -0.0223 68  ARG   A CD  
479  N  NE  . ARG   A 62  ? 1.1098 0.2162 0.2582 -0.0214 0.2560  -0.0327 68  ARG   A NE  
480  C  CZ  . ARG   A 62  ? 1.1676 0.2323 0.2823 -0.0229 0.2819  -0.0426 68  ARG   A CZ  
481  N  NH1 . ARG   A 62  ? 1.1999 0.2318 0.2715 -0.0328 0.2389  -0.0446 68  ARG   A NH1 
482  N  NH2 . ARG   A 62  ? 1.1872 0.2414 0.3179 -0.0146 0.3521  -0.0490 68  ARG   A NH2 
483  N  N   . ARG   A 63  ? 0.9486 0.2406 0.3560 -0.0235 -0.0436 0.0248  69  ARG   A N   
484  C  CA  . ARG   A 63  ? 0.9224 0.2472 0.4034 -0.0225 -0.0830 0.0423  69  ARG   A CA  
485  C  C   . ARG   A 63  ? 0.8819 0.2622 0.4186 -0.0105 -0.0514 0.0412  69  ARG   A C   
486  O  O   . ARG   A 63  ? 0.8836 0.2550 0.4305 -0.0155 -0.0715 0.0546  69  ARG   A O   
487  C  CB  . ARG   A 63  ? 0.9972 0.2416 0.4092 -0.0455 -0.1385 0.0608  69  ARG   A CB  
488  C  CG  . ARG   A 63  ? 1.0860 0.2894 0.4796 -0.0593 -0.1896 0.0694  69  ARG   A CG  
489  C  CD  . ARG   A 63  ? 1.1984 0.3322 0.5480 -0.0839 -0.2564 0.0950  69  ARG   A CD  
490  N  NE  . ARG   A 63  ? 1.3482 0.3928 0.5976 -0.1095 -0.2978 0.0986  69  ARG   A NE  
491  C  CZ  . ARG   A 63  ? 1.4888 0.4232 0.6028 -0.1403 -0.3310 0.1080  69  ARG   A CZ  
492  N  NH1 . ARG   A 63  ? 1.5125 0.4165 0.5797 -0.1471 -0.3259 0.1150  69  ARG   A NH1 
493  N  NH2 . ARG   A 63  ? 1.5663 0.4126 0.5814 -0.1667 -0.3686 0.1100  69  ARG   A NH2 
494  N  N   . LYS   A 64  ? 0.8348 0.2667 0.4033 0.0030  -0.0032 0.0266  70  LYS   A N   
495  C  CA  . LYS   A 64  ? 0.7860 0.2647 0.3961 0.0108  0.0286  0.0241  70  LYS   A CA  
496  C  C   . LYS   A 64  ? 0.7092 0.2589 0.3968 0.0235  0.0509  0.0163  70  LYS   A C   
497  O  O   . LYS   A 64  ? 0.7075 0.2659 0.3943 0.0277  0.0624  0.0089  70  LYS   A O   
498  C  CB  . LYS   A 64  ? 0.8281 0.2757 0.3716 0.0073  0.0680  0.0169  70  LYS   A CB  
499  C  CG  . LYS   A 64  ? 0.9018 0.2902 0.3771 -0.0049 0.0596  0.0246  70  LYS   A CG  
500  C  CD  . LYS   A 64  ? 1.0064 0.3204 0.3777 -0.0143 0.0908  0.0174  70  LYS   A CD  
501  C  CE  . LYS   A 64  ? 1.1168 0.3319 0.3783 -0.0350 0.0596  0.0259  70  LYS   A CE  
502  N  NZ  . LYS   A 64  ? 1.1721 0.3060 0.3345 -0.0477 0.0643  0.0182  70  LYS   A NZ  
503  N  N   . HIS   A 65  ? 0.6460 0.2386 0.3921 0.0273  0.0586  0.0183  71  HIS   A N   
504  C  CA  . HIS   A 65  ? 0.5826 0.2303 0.3852 0.0335  0.0803  0.0119  71  HIS   A CA  
505  C  C   . HIS   A 65  ? 0.5893 0.2503 0.3752 0.0318  0.1121  0.0077  71  HIS   A C   
506  O  O   . HIS   A 65  ? 0.6088 0.2482 0.3638 0.0273  0.1196  0.0103  71  HIS   A O   
507  C  CB  . HIS   A 65  ? 0.5419 0.2114 0.4008 0.0339  0.0776  0.0158  71  HIS   A CB  
508  C  CG  . HIS   A 65  ? 0.5205 0.1808 0.4208 0.0363  0.0498  0.0243  71  HIS   A CG  
509  N  ND1 . HIS   A 65  ? 0.5167 0.2010 0.4700 0.0415  0.0527  0.0220  71  HIS   A ND1 
510  C  CD2 . HIS   A 65  ? 0.5467 0.1741 0.4463 0.0328  0.0176  0.0377  71  HIS   A CD2 
511  C  CE1 . HIS   A 65  ? 0.5168 0.1864 0.5108 0.0426  0.0255  0.0341  71  HIS   A CE1 
512  N  NE2 . HIS   A 65  ? 0.5383 0.1741 0.5033 0.0367  -0.0004 0.0453  71  HIS   A NE2 
513  N  N   . TYR   A 66  ? 0.5676 0.2624 0.3787 0.0344  0.1289  0.0038  72  TYR   A N   
514  C  CA  . TYR   A 66  ? 0.5664 0.2778 0.3810 0.0319  0.1546  0.0047  72  TYR   A CA  
515  C  C   . TYR   A 66  ? 0.5397 0.2953 0.4001 0.0275  0.1583  0.0063  72  TYR   A C   
516  O  O   . TYR   A 66  ? 0.5259 0.2995 0.4088 0.0293  0.1507  0.0048  72  TYR   A O   
517  C  CB  . TYR   A 66  ? 0.5778 0.2772 0.3782 0.0366  0.1720  0.0036  72  TYR   A CB  
518  C  CG  . TYR   A 66  ? 0.6331 0.2723 0.3672 0.0357  0.1789  0.0011  72  TYR   A CG  
519  C  CD1 . TYR   A 66  ? 0.6740 0.2850 0.3753 0.0312  0.1991  0.0032  72  TYR   A CD1 
520  C  CD2 . TYR   A 66  ? 0.6760 0.2796 0.3737 0.0370  0.1684  -0.0032 72  TYR   A CD2 
521  C  CE1 . TYR   A 66  ? 0.7383 0.2797 0.3621 0.0268  0.2084  0.0005  72  TYR   A CE1 
522  C  CE2 . TYR   A 66  ? 0.7427 0.2754 0.3606 0.0310  0.1753  -0.0059 72  TYR   A CE2 
523  C  CZ  . TYR   A 66  ? 0.7821 0.2806 0.3588 0.0253  0.1958  -0.0042 72  TYR   A CZ  
524  O  OH  . TYR   A 66  ? 0.8745 0.2898 0.3572 0.0158  0.2047  -0.0071 72  TYR   A OH  
525  N  N   . PRO   A 67  ? 0.5394 0.3079 0.4089 0.0193  0.1693  0.0107  73  PRO   A N   
526  C  CA  . PRO   A 67  ? 0.5160 0.3164 0.4172 0.0089  0.1673  0.0150  73  PRO   A CA  
527  C  C   . PRO   A 67  ? 0.4943 0.3176 0.4272 0.0100  0.1735  0.0237  73  PRO   A C   
528  O  O   . PRO   A 67  ? 0.5087 0.3238 0.4442 0.0162  0.1911  0.0272  73  PRO   A O   
529  C  CB  . PRO   A 67  ? 0.5279 0.3265 0.4245 -0.0028 0.1727  0.0181  73  PRO   A CB  
530  C  CG  . PRO   A 67  ? 0.5597 0.3303 0.4282 0.0042  0.1819  0.0164  73  PRO   A CG  
531  C  CD  . PRO   A 67  ? 0.5548 0.3042 0.4025 0.0164  0.1817  0.0132  73  PRO   A CD  
532  N  N   . VAL   A 68  ? 0.4629 0.3095 0.4209 0.0033  0.1616  0.0285  74  VAL   A N   
533  C  CA  . VAL   A 68  ? 0.4234 0.2946 0.4250 0.0038  0.1628  0.0411  74  VAL   A CA  
534  C  C   . VAL   A 68  ? 0.4008 0.2930 0.4247 -0.0148 0.1419  0.0532  74  VAL   A C   
535  O  O   . VAL   A 68  ? 0.4100 0.2908 0.4031 -0.0257 0.1300  0.0466  74  VAL   A O   
536  C  CB  . VAL   A 68  ? 0.4206 0.2894 0.4252 0.0186  0.1659  0.0360  74  VAL   A CB  
537  C  CG1 . VAL   A 68  ? 0.4383 0.2767 0.4156 0.0321  0.1854  0.0279  74  VAL   A CG1 
538  C  CG2 . VAL   A 68  ? 0.4253 0.2897 0.4107 0.0184  0.1501  0.0265  74  VAL   A CG2 
539  N  N   . SER   A 69  ? 0.3550 0.2717 0.4329 -0.0199 0.1386  0.0726  75  SER   A N   
540  C  CA  . SER   A 69  ? 0.3376 0.2721 0.4430 -0.0393 0.1113  0.0906  75  SER   A CA  
541  C  C   . SER   A 69  ? 0.3265 0.2727 0.4564 -0.0260 0.1124  0.0923  75  SER   A C   
542  O  O   . SER   A 69  ? 0.3065 0.2558 0.4622 -0.0063 0.1364  0.0903  75  SER   A O   
543  C  CB  . SER   A 69  ? 0.3419 0.2993 0.5136 -0.0496 0.1056  0.1159  75  SER   A CB  
544  O  OG  . SER   A 69  ? 0.3890 0.3379 0.5423 -0.0709 0.0918  0.1201  75  SER   A OG  
545  N  N   . PHE   A 70  ? 0.3368 0.2822 0.4523 -0.0377 0.0897  0.0953  76  PHE   A N   
546  C  CA  . PHE   A 70  ? 0.3419 0.2977 0.4795 -0.0253 0.0905  0.0966  76  PHE   A CA  
547  C  C   . PHE   A 70  ? 0.3510 0.3192 0.5143 -0.0447 0.0593  0.1191  76  PHE   A C   
548  O  O   . PHE   A 70  ? 0.3803 0.3362 0.5176 -0.0715 0.0336  0.1287  76  PHE   A O   
549  C  CB  . PHE   A 70  ? 0.3676 0.3022 0.4557 -0.0120 0.1012  0.0722  76  PHE   A CB  
550  C  CG  . PHE   A 70  ? 0.4095 0.3185 0.4417 -0.0268 0.0922  0.0612  76  PHE   A CG  
551  C  CD1 . PHE   A 70  ? 0.4395 0.3271 0.4351 -0.0281 0.1026  0.0474  76  PHE   A CD1 
552  C  CD2 . PHE   A 70  ? 0.4293 0.3296 0.4454 -0.0386 0.0786  0.0642  76  PHE   A CD2 
553  C  CE1 . PHE   A 70  ? 0.4772 0.3350 0.4278 -0.0410 0.1037  0.0373  76  PHE   A CE1 
554  C  CE2 . PHE   A 70  ? 0.4650 0.3303 0.4258 -0.0527 0.0808  0.0528  76  PHE   A CE2 
555  C  CZ  . PHE   A 70  ? 0.4795 0.3237 0.4112 -0.0532 0.0959  0.0390  76  PHE   A CZ  
556  N  N   . SER   A 71  ? 0.3300 0.3179 0.5438 -0.0335 0.0603  0.1300  77  SER   A N   
557  C  CA  . SER   A 71  ? 0.3279 0.3282 0.5747 -0.0512 0.0274  0.1559  77  SER   A CA  
558  C  C   . SER   A 71  ? 0.3665 0.3398 0.5443 -0.0636 0.0116  0.1457  77  SER   A C   
559  O  O   . SER   A 71  ? 0.3772 0.3289 0.5001 -0.0531 0.0314  0.1188  77  SER   A O   
560  C  CB  . SER   A 71  ? 0.3138 0.3432 0.6467 -0.0327 0.0395  0.1717  77  SER   A CB  
561  O  OG  . SER   A 71  ? 0.3538 0.3751 0.6629 -0.0124 0.0594  0.1514  77  SER   A OG  
562  N  N   . LYS   A 72  ? 0.3830 0.3543 0.5681 -0.0871 -0.0243 0.1699  78  LYS   A N   
563  C  CA  . LYS   A 72  ? 0.4465 0.3842 0.5640 -0.1029 -0.0383 0.1644  78  LYS   A CA  
564  C  C   . LYS   A 72  ? 0.4468 0.3984 0.5892 -0.0782 -0.0214 0.1566  78  LYS   A C   
565  O  O   . LYS   A 72  ? 0.4174 0.4042 0.6392 -0.0614 -0.0174 0.1708  78  LYS   A O   
566  C  CB  . LYS   A 72  ? 0.4877 0.4124 0.6019 -0.1402 -0.0882 0.1978  78  LYS   A CB  
567  C  CG  . LYS   A 72  ? 0.5608 0.4748 0.6654 -0.1683 -0.1140 0.2129  78  LYS   A CG  
568  C  CD  . LYS   A 72  ? 0.6805 0.5314 0.6812 -0.2125 -0.1473 0.2179  78  LYS   A CD  
569  C  CE  . LYS   A 72  ? 0.7849 0.5858 0.6828 -0.2124 -0.1109 0.1800  78  LYS   A CE  
570  N  NZ  . LYS   A 72  ? 0.8828 0.6075 0.6672 -0.2542 -0.1308 0.1811  78  LYS   A NZ  
571  N  N   . PRO   A 73  ? 0.4738 0.3950 0.5541 -0.0771 -0.0097 0.1361  79  PRO   A N   
572  C  CA  . PRO   A 73  ? 0.4650 0.3986 0.5707 -0.0549 0.0043  0.1293  79  PRO   A CA  
573  C  C   . PRO   A 73  ? 0.4387 0.3948 0.6017 -0.0595 -0.0201 0.1585  79  PRO   A C   
574  O  O   . PRO   A 73  ? 0.4546 0.3922 0.5942 -0.0885 -0.0541 0.1797  79  PRO   A O   
575  C  CB  . PRO   A 73  ? 0.5122 0.4028 0.5430 -0.0623 0.0155  0.1092  79  PRO   A CB  
576  C  CG  . PRO   A 73  ? 0.5441 0.4050 0.5202 -0.0747 0.0251  0.0952  79  PRO   A CG  
577  C  CD  . PRO   A 73  ? 0.5153 0.3864 0.5054 -0.0954 -0.0030 0.1180  79  PRO   A CD  
578  N  N   . SER   A 74  ? 0.4046 0.3944 0.6398 -0.0327 -0.0028 0.1607  80  SER   A N   
579  C  CA  . SER   A 74  ? 0.3847 0.4000 0.6939 -0.0326 -0.0199 0.1902  80  SER   A CA  
580  C  C   . SER   A 74  ? 0.3608 0.3953 0.7219 -0.0008 0.0117  0.1809  80  SER   A C   
581  O  O   . SER   A 74  ? 0.3699 0.3949 0.7030 0.0190  0.0426  0.1519  80  SER   A O   
582  C  CB  . SER   A 74  ? 0.3874 0.4278 0.7684 -0.0435 -0.0388 0.2213  80  SER   A CB  
583  O  OG  . SER   A 74  ? 0.4225 0.4768 0.8346 -0.0218 -0.0029 0.2078  80  SER   A OG  
584  N  N   . LEU   A 75  ? 0.3291 0.3867 0.7674 0.0020  0.0021  0.2079  81  LEU   A N   
585  C  CA  . LEU   A 75  ? 0.3161 0.3870 0.8080 0.0292  0.0336  0.2025  81  LEU   A CA  
586  C  C   . LEU   A 75  ? 0.2989 0.3855 0.8619 0.0463  0.0669  0.2070  81  LEU   A C   
587  O  O   . LEU   A 75  ? 0.2677 0.3784 0.9183 0.0401  0.0569  0.2401  81  LEU   A O   
588  C  CB  . LEU   A 75  ? 0.2930 0.3785 0.8417 0.0240  0.0113  0.2317  81  LEU   A CB  
589  C  CG  . LEU   A 75  ? 0.3386 0.4038 0.8278 0.0203  0.0013  0.2201  81  LEU   A CG  
590  C  CD1 . LEU   A 75  ? 0.3261 0.4022 0.8657 0.0074  -0.0310 0.2559  81  LEU   A CD1 
591  C  CD2 . LEU   A 75  ? 0.3548 0.4137 0.8338 0.0477  0.0401  0.1900  81  LEU   A CD2 
592  N  N   . ILE   A 76  ? 0.3132 0.3808 0.8415 0.0663  0.1070  0.1761  82  ILE   A N   
593  C  CA  . ILE   A 76  ? 0.3130 0.3766 0.8828 0.0820  0.1490  0.1735  82  ILE   A CA  
594  C  C   . ILE   A 76  ? 0.3486 0.3906 0.9178 0.1033  0.1885  0.1558  82  ILE   A C   
595  O  O   . ILE   A 76  ? 0.3807 0.4015 0.8810 0.1076  0.1865  0.1309  82  ILE   A O   
596  C  CB  . ILE   A 76  ? 0.3396 0.3834 0.8442 0.0794  0.1578  0.1526  82  ILE   A CB  
597  C  CG1 . ILE   A 76  ? 0.3352 0.3977 0.8516 0.0576  0.1244  0.1728  82  ILE   A CG1 
598  C  CG2 . ILE   A 76  ? 0.3448 0.3642 0.8566 0.0956  0.2086  0.1405  82  ILE   A CG2 
599  C  CD1 . ILE   A 76  ? 0.3821 0.4244 0.8130 0.0502  0.1180  0.1501  82  ILE   A CD1 
600  N  N   . PHE   A 77  ? 0.3350 0.3779 0.9835 0.1155  0.2262  0.1696  83  PHE   A N   
601  C  CA  . PHE   A 77  ? 0.3721 0.3833 1.0177 0.1332  0.2711  0.1535  83  PHE   A CA  
602  C  C   . PHE   A 77  ? 0.4234 0.3795 0.9717 0.1390  0.3038  0.1177  83  PHE   A C   
603  O  O   . PHE   A 77  ? 0.4312 0.3719 0.9680 0.1374  0.3240  0.1150  83  PHE   A O   
604  C  CB  . PHE   A 77  ? 0.3566 0.3785 1.1217 0.1427  0.3088  0.1810  83  PHE   A CB  
605  C  CG  . PHE   A 77  ? 0.3994 0.3795 1.1650 0.1595  0.3644  0.1657  83  PHE   A CG  
606  C  CD1 . PHE   A 77  ? 0.4119 0.3980 1.1994 0.1653  0.3589  0.1688  83  PHE   A CD1 
607  C  CD2 . PHE   A 77  ? 0.4474 0.3745 1.1858 0.1674  0.4248  0.1485  83  PHE   A CD2 
608  C  CE1 . PHE   A 77  ? 0.4435 0.3860 1.2329 0.1792  0.4132  0.1554  83  PHE   A CE1 
609  C  CE2 . PHE   A 77  ? 0.4832 0.3595 1.2168 0.1794  0.4814  0.1352  83  PHE   A CE2 
610  C  CZ  . PHE   A 77  ? 0.4677 0.3523 1.2261 0.1853  0.4747  0.1380  83  PHE   A CZ  
611  N  N   . VAL   A 78  ? 0.4565 0.3796 0.9348 0.1438  0.3064  0.0924  84  VAL   A N   
612  C  CA  . VAL   A 78  ? 0.5148 0.3781 0.8926 0.1446  0.3255  0.0613  84  VAL   A CA  
613  C  C   . VAL   A 78  ? 0.5574 0.3684 0.9206 0.1538  0.3703  0.0487  84  VAL   A C   
614  O  O   . VAL   A 78  ? 0.5436 0.3645 0.9349 0.1590  0.3662  0.0514  84  VAL   A O   
615  C  CB  . VAL   A 78  ? 0.5321 0.3943 0.8327 0.1369  0.2807  0.0434  84  VAL   A CB  
616  C  CG1 . VAL   A 78  ? 0.5863 0.3863 0.7892 0.1343  0.2897  0.0172  84  VAL   A CG1 
617  C  CG2 . VAL   A 78  ? 0.5135 0.4172 0.8253 0.1267  0.2455  0.0549  84  VAL   A CG2 
618  N  N   . GLU   A 79  ? 0.6090 0.3574 0.9227 0.1540  0.4162  0.0350  85  GLU   A N   
619  C  CA  . GLU   A 79  ? 0.6603 0.3344 0.9341 0.1579  0.4692  0.0192  85  GLU   A CA  
620  C  C   . GLU   A 79  ? 0.6977 0.3373 0.8917 0.1537  0.4448  -0.0024 85  GLU   A C   
621  O  O   . GLU   A 79  ? 0.7086 0.3595 0.8501 0.1460  0.3942  -0.0114 85  GLU   A O   
622  C  CB  . GLU   A 79  ? 0.7523 0.3514 0.9475 0.1517  0.5117  0.0041  85  GLU   A CB  
623  C  CG  . GLU   A 79  ? 0.8147 0.4232 1.0966 0.1585  0.5634  0.0237  85  GLU   A CG  
624  C  CD  . GLU   A 79  ? 0.9542 0.4866 1.2372 0.1640  0.6461  0.0178  85  GLU   A CD  
625  O  OE1 . GLU   A 79  ? 0.9819 0.4803 1.2472 0.1669  0.6629  0.0079  85  GLU   A OE1 
626  O  OE2 . GLU   A 79  ? 1.0164 0.5198 1.3206 0.1652  0.6986  0.0233  85  GLU   A OE2 
627  N  N   . ALA   A 80  ? 0.7181 0.3100 0.9047 0.1579  0.4834  -0.0103 86  ALA   A N   
628  C  CA  . ALA   A 80  ? 0.7652 0.3176 0.8776 0.1520  0.4614  -0.0300 86  ALA   A CA  
629  C  C   . ALA   A 80  ? 0.8446 0.3213 0.8212 0.1351  0.4453  -0.0535 86  ALA   A C   
630  O  O   . ALA   A 80  ? 0.8932 0.3074 0.8119 0.1286  0.4829  -0.0612 86  ALA   A O   
631  C  CB  . ALA   A 80  ? 0.7742 0.2791 0.8996 0.1579  0.5135  -0.0346 86  ALA   A CB  
632  N  N   . SER   A 81  ? 0.8562 0.3400 0.7897 0.1272  0.3880  -0.0616 87  SER   A N   
633  C  CA  . SER   A 81  ? 0.9147 0.3327 0.7325 0.1090  0.3568  -0.0782 87  SER   A CA  
634  C  C   . SER   A 81  ? 0.9479 0.3258 0.7191 0.1004  0.3302  -0.0902 87  SER   A C   
635  O  O   . SER   A 81  ? 0.9209 0.3314 0.7537 0.1107  0.3367  -0.0863 87  SER   A O   
636  C  CB  . SER   A 81  ? 0.8970 0.3736 0.7328 0.1072  0.3045  -0.0702 87  SER   A CB  
637  O  OG  . SER   A 81  ? 0.8664 0.4128 0.7683 0.1138  0.2641  -0.0623 87  SER   A OG  
638  N  N   . GLU   A 82  ? 1.0020 0.3100 0.6689 0.0800  0.2957  -0.1023 88  GLU   A N   
639  C  CA  . GLU   A 82  ? 1.0327 0.3037 0.6603 0.0685  0.2601  -0.1105 88  GLU   A CA  
640  C  C   . GLU   A 82  ? 0.9574 0.3204 0.6788 0.0789  0.2107  -0.0991 88  GLU   A C   
641  O  O   . GLU   A 82  ? 0.9697 0.3178 0.6866 0.0733  0.1850  -0.1030 88  GLU   A O   
642  C  CB  . GLU   A 82  ? 1.1602 0.3335 0.6583 0.0401  0.2243  -0.1204 88  GLU   A CB  
643  C  CG  . GLU   A 82  ? 1.2430 0.4481 0.7438 0.0359  0.1809  -0.1108 88  GLU   A CG  
644  C  CD  . GLU   A 82  ? 1.4374 0.5457 0.8139 0.0137  0.1838  -0.1175 88  GLU   A CD  
645  O  OE1 . GLU   A 82  ? 1.5178 0.5523 0.8254 0.0088  0.2430  -0.1287 88  GLU   A OE1 
646  O  OE2 . GLU   A 82  ? 1.4845 0.5871 0.8343 0.0006  0.1293  -0.1104 88  GLU   A OE2 
647  N  N   . TYR   A 83  ? 0.8822 0.3322 0.6833 0.0918  0.1995  -0.0855 89  TYR   A N   
648  C  CA  . TYR   A 83  ? 0.8059 0.3335 0.6882 0.1002  0.1624  -0.0752 89  TYR   A CA  
649  C  C   . TYR   A 83  ? 0.7226 0.3178 0.6956 0.1180  0.1882  -0.0648 89  TYR   A C   
650  O  O   . TYR   A 83  ? 0.6958 0.3266 0.7172 0.1230  0.1700  -0.0608 89  TYR   A O   
651  C  CB  . TYR   A 83  ? 0.7862 0.3523 0.6852 0.0987  0.1324  -0.0673 89  TYR   A CB  
652  C  CG  . TYR   A 83  ? 0.8466 0.3486 0.6617 0.0810  0.1074  -0.0727 89  TYR   A CG  
653  C  CD1 . TYR   A 83  ? 0.8805 0.3481 0.6688 0.0670  0.0593  -0.0734 89  TYR   A CD1 
654  C  CD2 . TYR   A 83  ? 0.8871 0.3584 0.6510 0.0766  0.1301  -0.0748 89  TYR   A CD2 
655  C  CE1 . TYR   A 83  ? 0.9425 0.3442 0.6505 0.0471  0.0291  -0.0743 89  TYR   A CE1 
656  C  CE2 . TYR   A 83  ? 0.9504 0.3555 0.6286 0.0581  0.1053  -0.0783 89  TYR   A CE2 
657  C  CZ  . TYR   A 83  ? 0.9874 0.3561 0.6351 0.0424  0.0524  -0.0773 89  TYR   A CZ  
658  O  OH  . TYR   A 83  ? 1.0630 0.3617 0.6247 0.0209  0.0206  -0.0766 89  TYR   A OH  
659  N  N   . TYR   A 84  ? 0.6849 0.2976 0.6861 0.1262  0.2274  -0.0576 90  TYR   A N   
660  C  CA  . TYR   A 84  ? 0.6244 0.2999 0.7164 0.1399  0.2439  -0.0420 90  TYR   A CA  
661  C  C   . TYR   A 84  ? 0.6343 0.2892 0.7484 0.1470  0.2974  -0.0381 90  TYR   A C   
662  O  O   . TYR   A 84  ? 0.6555 0.2665 0.7291 0.1434  0.3277  -0.0434 90  TYR   A O   
663  C  CB  . TYR   A 84  ? 0.5697 0.3096 0.7108 0.1421  0.2292  -0.0262 90  TYR   A CB  
664  C  CG  . TYR   A 84  ? 0.5467 0.3082 0.6765 0.1360  0.1876  -0.0279 90  TYR   A CG  
665  C  CD1 . TYR   A 84  ? 0.5569 0.3064 0.6477 0.1288  0.1760  -0.0314 90  TYR   A CD1 
666  C  CD2 . TYR   A 84  ? 0.5184 0.3128 0.6845 0.1379  0.1650  -0.0239 90  TYR   A CD2 
667  C  CE1 . TYR   A 84  ? 0.5507 0.3198 0.6437 0.1243  0.1438  -0.0309 90  TYR   A CE1 
668  C  CE2 . TYR   A 84  ? 0.5099 0.3203 0.6757 0.1330  0.1368  -0.0243 90  TYR   A CE2 
669  C  CZ  . TYR   A 84  ? 0.5283 0.3270 0.6613 0.1266  0.1269  -0.0274 90  TYR   A CZ  
670  O  OH  . TYR   A 84  ? 0.5164 0.3279 0.6581 0.1225  0.1042  -0.0268 90  TYR   A OH  
671  N  N   . PRO   A 85  ? 0.6109 0.3005 0.8003 0.1577  0.3120  -0.0255 91  PRO   A N   
672  C  CA  . PRO   A 85  ? 0.6037 0.2852 0.8444 0.1665  0.3653  -0.0150 91  PRO   A CA  
673  C  C   . PRO   A 85  ? 0.5533 0.2886 0.8611 0.1697  0.3672  0.0075  91  PRO   A C   
674  O  O   . PRO   A 85  ? 0.5188 0.2981 0.8296 0.1646  0.3264  0.0139  91  PRO   A O   
675  C  CB  . PRO   A 85  ? 0.5895 0.2990 0.8984 0.1758  0.3683  -0.0045 91  PRO   A CB  
676  C  CG  . PRO   A 85  ? 0.5662 0.3289 0.8869 0.1730  0.3128  0.0004  91  PRO   A CG  
677  C  CD  . PRO   A 85  ? 0.5764 0.3157 0.8162 0.1619  0.2817  -0.0170 91  PRO   A CD  
678  N  N   . ALA   A 86  ? 0.5362 0.2664 0.9037 0.1770  0.4155  0.0210  92  ALA   A N   
679  C  CA  . ALA   A 86  ? 0.4955 0.2765 0.9385 0.1782  0.4144  0.0461  92  ALA   A CA  
680  C  C   . ALA   A 86  ? 0.4365 0.2961 0.9544 0.1772  0.3651  0.0717  92  ALA   A C   
681  O  O   . ALA   A 86  ? 0.4066 0.2863 0.9770 0.1826  0.3612  0.0833  92  ALA   A O   
682  C  CB  . ALA   A 86  ? 0.4881 0.2500 1.0026 0.1871  0.4773  0.0597  92  ALA   A CB  
683  N  N   . ARG   A 87  ? 0.4162 0.3092 0.9181 0.1675  0.3247  0.0769  93  ARG   A N   
684  C  CA  . ARG   A 87  ? 0.3605 0.3085 0.9016 0.1607  0.2773  0.0972  93  ARG   A CA  
685  C  C   . ARG   A 87  ? 0.3360 0.3158 0.8886 0.1487  0.2499  0.1129  93  ARG   A C   
686  O  O   . ARG   A 87  ? 0.3551 0.3189 0.8855 0.1475  0.2664  0.1061  93  ARG   A O   
687  C  CB  . ARG   A 87  ? 0.3738 0.3123 0.8476 0.1575  0.2488  0.0769  93  ARG   A CB  
688  C  CG  . ARG   A 87  ? 0.3810 0.3104 0.7796 0.1482  0.2243  0.0597  93  ARG   A CG  
689  C  CD  . ARG   A 87  ? 0.4018 0.2938 0.7306 0.1489  0.2190  0.0329  93  ARG   A CD  
690  N  NE  . ARG   A 87  ? 0.3894 0.2882 0.6779 0.1402  0.1879  0.0253  93  ARG   A NE  
691  C  CZ  . ARG   A 87  ? 0.4038 0.2873 0.6500 0.1350  0.1845  0.0166  93  ARG   A CZ  
692  N  NH1 . ARG   A 87  ? 0.3889 0.2783 0.6100 0.1281  0.1599  0.0115  93  ARG   A NH1 
693  N  NH2 . ARG   A 87  ? 0.3908 0.2481 0.6200 0.1366  0.2096  0.0132  93  ARG   A NH2 
694  N  N   . TYR   A 88  ? 0.3048 0.3223 0.8848 0.1375  0.2085  0.1340  94  TYR   A N   
695  C  CA  . TYR   A 88  ? 0.2985 0.3357 0.8682 0.1213  0.1772  0.1457  94  TYR   A CA  
696  C  C   . TYR   A 88  ? 0.2869 0.3070 0.7638 0.1146  0.1573  0.1203  94  TYR   A C   
697  O  O   . TYR   A 88  ? 0.2871 0.3047 0.7436 0.1137  0.1435  0.1149  94  TYR   A O   
698  C  CB  . TYR   A 88  ? 0.2932 0.3636 0.9167 0.1062  0.1378  0.1806  94  TYR   A CB  
699  C  CG  . TYR   A 88  ? 0.2900 0.3874 1.0283 0.1073  0.1430  0.2176  94  TYR   A CG  
700  C  CD1 . TYR   A 88  ? 0.2922 0.3999 1.0729 0.1034  0.1501  0.2315  94  TYR   A CD1 
701  C  CD2 . TYR   A 88  ? 0.2842 0.3994 1.0977 0.1096  0.1352  0.2436  94  TYR   A CD2 
702  C  CE1 . TYR   A 88  ? 0.2658 0.4014 1.1710 0.1031  0.1520  0.2710  94  TYR   A CE1 
703  C  CE2 . TYR   A 88  ? 0.2542 0.3971 1.1907 0.1094  0.1354  0.2837  94  TYR   A CE2 
704  C  CZ  . TYR   A 88  ? 0.2493 0.4031 1.2362 0.1061  0.1438  0.2982  94  TYR   A CZ  
705  O  OH  . TYR   A 88  ? 0.2230 0.4059 1.3509 0.1064  0.1448  0.3418  94  TYR   A OH  
706  N  N   . GLN   A 89  ? 0.2769 0.2857 0.7060 0.1094  0.1562  0.1075  95  GLN   A N   
707  C  CA  . GLN   A 89  ? 0.2806 0.2746 0.6369 0.1023  0.1383  0.0876  95  GLN   A CA  
708  C  C   . GLN   A 89  ? 0.2756 0.2836 0.6233 0.0822  0.1093  0.1030  95  GLN   A C   
709  O  O   . GLN   A 89  ? 0.2652 0.2848 0.6351 0.0744  0.1053  0.1174  95  GLN   A O   
710  C  CB  . GLN   A 89  ? 0.3006 0.2655 0.6037 0.1082  0.1537  0.0630  95  GLN   A CB  
711  C  CG  . GLN   A 89  ? 0.3098 0.2629 0.5577 0.1010  0.1354  0.0475  95  GLN   A CG  
712  C  CD  . GLN   A 89  ? 0.3578 0.2800 0.5610 0.1065  0.1441  0.0273  95  GLN   A CD  
713  O  OE1 . GLN   A 89  ? 0.3763 0.2740 0.5691 0.1152  0.1592  0.0180  95  GLN   A OE1 
714  N  NE2 . GLN   A 89  ? 0.3759 0.2920 0.5475 0.0993  0.1338  0.0211  95  GLN   A NE2 
715  N  N   . SER   A 90  ? 0.2768 0.2777 0.5910 0.0718  0.0907  0.1009  96  SER   A N   
716  C  CA  . SER   A 90  ? 0.2879 0.2846 0.5733 0.0477  0.0649  0.1138  96  SER   A CA  
717  C  C   . SER   A 90  ? 0.3191 0.2940 0.5438 0.0412  0.0687  0.0942  96  SER   A C   
718  O  O   . SER   A 90  ? 0.3354 0.2985 0.5408 0.0550  0.0855  0.0714  96  SER   A O   
719  C  CB  . SER   A 90  ? 0.3084 0.2940 0.5765 0.0368  0.0497  0.1211  96  SER   A CB  
720  O  OG  . SER   A 90  ? 0.3594 0.3239 0.5893 0.0450  0.0652  0.0963  96  SER   A OG  
721  N  N   . HIS   A 91  ? 0.3164 0.2821 0.5119 0.0182  0.0508  0.1048  97  HIS   A N   
722  C  CA  . HIS   A 91  ? 0.3375 0.2787 0.4769 0.0090  0.0561  0.0888  97  HIS   A CA  
723  C  C   . HIS   A 91  ? 0.3287 0.2792 0.4795 0.0244  0.0724  0.0763  97  HIS   A C   
724  O  O   . HIS   A 91  ? 0.3387 0.2717 0.4575 0.0285  0.0839  0.0576  97  HIS   A O   
725  C  CB  . HIS   A 91  ? 0.3675 0.2777 0.4623 0.0084  0.0689  0.0700  97  HIS   A CB  
726  C  CG  . HIS   A 91  ? 0.4099 0.2975 0.4768 -0.0095 0.0586  0.0802  97  HIS   A CG  
727  N  ND1 . HIS   A 91  ? 0.4708 0.3139 0.4694 -0.0363 0.0565  0.0800  97  HIS   A ND1 
728  C  CD2 . HIS   A 91  ? 0.4008 0.2972 0.4925 -0.0060 0.0514  0.0910  97  HIS   A CD2 
729  C  CE1 . HIS   A 91  ? 0.4763 0.2987 0.4539 -0.0492 0.0480  0.0903  97  HIS   A CE1 
730  N  NE2 . HIS   A 91  ? 0.4413 0.2985 0.4775 -0.0312 0.0425  0.0984  97  HIS   A NE2 
731  N  N   . LEU   A 92  ? 0.3126 0.2865 0.5118 0.0321  0.0751  0.0885  98  LEU   A N   
732  C  CA  . LEU   A 92  ? 0.3178 0.2910 0.5195 0.0447  0.0941  0.0777  98  LEU   A CA  
733  C  C   . LEU   A 92  ? 0.3072 0.2866 0.5125 0.0309  0.0867  0.0894  98  LEU   A C   
734  O  O   . LEU   A 92  ? 0.2970 0.2946 0.5436 0.0189  0.0703  0.1142  98  LEU   A O   
735  C  CB  . LEU   A 92  ? 0.2968 0.2798 0.5460 0.0628  0.1140  0.0810  98  LEU   A CB  
736  C  CG  . LEU   A 92  ? 0.3211 0.2862 0.5554 0.0752  0.1397  0.0667  98  LEU   A CG  
737  C  CD1 . LEU   A 92  ? 0.3526 0.2899 0.5296 0.0804  0.1400  0.0428  98  LEU   A CD1 
738  C  CD2 . LEU   A 92  ? 0.3196 0.2825 0.5979 0.0895  0.1680  0.0718  98  LEU   A CD2 
739  N  N   . MET   A 93  ? 0.3126 0.2772 0.4824 0.0323  0.0967  0.0744  99  MET   A N   
740  C  CA  . MET   A 93  ? 0.2985 0.2669 0.4703 0.0205  0.0931  0.0832  99  MET   A CA  
741  C  C   . MET   A 93  ? 0.3047 0.2722 0.4937 0.0356  0.1189  0.0785  99  MET   A C   
742  O  O   . MET   A 93  ? 0.3334 0.2792 0.4870 0.0480  0.1338  0.0589  99  MET   A O   
743  C  CB  . MET   A 93  ? 0.3111 0.2565 0.4236 0.0063  0.0861  0.0713  99  MET   A CB  
744  C  CG  . MET   A 93  ? 0.3308 0.2602 0.4107 -0.0117 0.0698  0.0736  99  MET   A CG  
745  S  SD  . MET   A 93  ? 0.4437 0.3318 0.4532 -0.0248 0.0782  0.0546  99  MET   A SD  
746  C  CE  . MET   A 93  ? 0.4554 0.3405 0.4724 0.0029  0.1003  0.0326  99  MET   A CE  
747  N  N   . LEU   A 94  ? 0.2718 0.2567 0.5132 0.0324  0.1238  0.0977  100 LEU   A N   
748  C  CA  . LEU   A 94  ? 0.2716 0.2458 0.5242 0.0452  0.1563  0.0930  100 LEU   A CA  
749  C  C   . LEU   A 94  ? 0.2810 0.2501 0.5175 0.0360  0.1578  0.0933  100 LEU   A C   
750  O  O   . LEU   A 94  ? 0.2462 0.2306 0.4953 0.0178  0.1334  0.1074  100 LEU   A O   
751  C  CB  . LEU   A 94  ? 0.2420 0.2314 0.5760 0.0542  0.1787  0.1122  100 LEU   A CB  
752  C  CG  . LEU   A 94  ? 0.2541 0.2438 0.6127 0.0670  0.1893  0.1119  100 LEU   A CG  
753  C  CD1 . LEU   A 94  ? 0.2499 0.2381 0.6807 0.0794  0.2305  0.1247  100 LEU   A CD1 
754  C  CD2 . LEU   A 94  ? 0.2863 0.2415 0.5708 0.0778  0.1994  0.0832  100 LEU   A CD2 
755  N  N   . ALA   A 95  ? 0.3219 0.2635 0.5268 0.0468  0.1862  0.0787  101 ALA   A N   
756  C  CA  . ALA   A 95  ? 0.3605 0.2916 0.5475 0.0414  0.1947  0.0771  101 ALA   A CA  
757  C  C   . ALA   A 95  ? 0.4043 0.3045 0.5856 0.0537  0.2370  0.0716  101 ALA   A C   
758  O  O   . ALA   A 95  ? 0.4294 0.3016 0.5873 0.0653  0.2573  0.0607  101 ALA   A O   
759  C  CB  . ALA   A 95  ? 0.3953 0.3068 0.5109 0.0368  0.1788  0.0587  101 ALA   A CB  
760  N  N   . VAL   A 96  ? 0.4131 0.3111 0.6099 0.0492  0.2523  0.0789  102 VAL   A N   
761  C  CA  . VAL   A 96  ? 0.4504 0.3074 0.6266 0.0574  0.2967  0.0725  102 VAL   A CA  
762  C  C   . VAL   A 96  ? 0.5117 0.3264 0.5866 0.0568  0.2885  0.0499  102 VAL   A C   
763  O  O   . VAL   A 96  ? 0.5181 0.3444 0.5699 0.0482  0.2602  0.0470  102 VAL   A O   
764  C  CB  . VAL   A 96  ? 0.4388 0.3098 0.6749 0.0518  0.3153  0.0905  102 VAL   A CB  
765  C  CG1 . VAL   A 96  ? 0.4806 0.2970 0.6794 0.0589  0.3670  0.0812  102 VAL   A CG1 
766  C  CG2 . VAL   A 96  ? 0.3866 0.3022 0.7408 0.0502  0.3158  0.1195  102 VAL   A CG2 
767  N  N   . GLY   A 97  ? 0.5588 0.3209 0.5742 0.0640  0.3105  0.0356  103 GLY   A N   
768  C  CA  . GLY   A 97  ? 0.6179 0.3350 0.5417 0.0611  0.2957  0.0190  103 GLY   A CA  
769  C  C   . GLY   A 97  ? 0.6647 0.3267 0.5265 0.0650  0.3049  0.0060  103 GLY   A C   
770  O  O   . GLY   A 97  ? 0.6620 0.3340 0.5522 0.0710  0.3101  0.0064  103 GLY   A O   
771  N  N   . HIS   A 98  ? 0.7100 0.3089 0.4830 0.0592  0.3043  -0.0045 104 HIS   A N   
772  C  CA  . HIS   A 98  ? 0.7741 0.3034 0.4673 0.0564  0.3078  -0.0163 104 HIS   A CA  
773  C  C   . HIS   A 98  ? 0.7670 0.3091 0.4560 0.0569  0.2640  -0.0210 104 HIS   A C   
774  O  O   . HIS   A 98  ? 0.7529 0.3228 0.4525 0.0548  0.2237  -0.0191 104 HIS   A O   
775  C  CB  . HIS   A 98  ? 0.8524 0.3033 0.4435 0.0447  0.3106  -0.0224 104 HIS   A CB  
776  C  CG  . HIS   A 98  ? 0.9675 0.3313 0.4557 0.0347  0.3046  -0.0331 104 HIS   A CG  
777  N  ND1 . HIS   A 98  ? 1.0326 0.3366 0.4810 0.0338  0.3511  -0.0407 104 HIS   A ND1 
778  C  CD2 . HIS   A 98  ? 1.0257 0.3488 0.4453 0.0228  0.2564  -0.0352 104 HIS   A CD2 
779  C  CE1 . HIS   A 98  ? 1.0958 0.3201 0.4398 0.0193  0.3280  -0.0493 104 HIS   A CE1 
780  N  NE2 . HIS   A 98  ? 1.0944 0.3299 0.4222 0.0120  0.2670  -0.0445 104 HIS   A NE2 
781  N  N   . SER   A 99  ? 0.7853 0.2964 0.4547 0.0589  0.2769  -0.0273 105 SER   A N   
782  C  CA  . SER   A 99  ? 0.7995 0.3060 0.4544 0.0578  0.2408  -0.0324 105 SER   A CA  
783  C  C   . SER   A 99  ? 0.8608 0.2880 0.4416 0.0523  0.2618  -0.0430 105 SER   A C   
784  O  O   . SER   A 99  ? 0.8640 0.2645 0.4433 0.0558  0.3139  -0.0453 105 SER   A O   
785  C  CB  . SER   A 99  ? 0.7492 0.3359 0.4969 0.0681  0.2253  -0.0263 105 SER   A CB  
786  O  OG  . SER   A 99  ? 0.7423 0.3661 0.5567 0.0765  0.2598  -0.0188 105 SER   A OG  
787  N  N   . GLU   A 100 ? 0.8997 0.2852 0.4217 0.0421  0.2214  -0.0480 106 GLU   A N   
788  C  CA  . GLU   A 100 ? 0.9631 0.2661 0.4017 0.0312  0.2251  -0.0582 106 GLU   A CA  
789  C  C   . GLU   A 100 ? 0.9462 0.2871 0.4293 0.0348  0.1828  -0.0571 106 GLU   A C   
790  O  O   . GLU   A 100 ? 0.9159 0.3259 0.4696 0.0413  0.1477  -0.0489 106 GLU   A O   
791  C  CB  . GLU   A 100 ? 1.0694 0.2714 0.3811 0.0083  0.2044  -0.0613 106 GLU   A CB  
792  C  CG  . GLU   A 100 ? 1.1558 0.3045 0.4097 0.0033  0.2543  -0.0642 106 GLU   A CG  
793  C  CD  . GLU   A 100 ? 1.2797 0.3148 0.3919 -0.0226 0.2381  -0.0668 106 GLU   A CD  
794  O  OE1 . GLU   A 100 ? 1.3227 0.2845 0.3490 -0.0418 0.2022  -0.0700 106 GLU   A OE1 
795  O  OE2 . GLU   A 100 ? 1.3031 0.3190 0.3878 -0.0259 0.2581  -0.0640 106 GLU   A OE2 
796  N  N   . PRO   A 101 ? 0.9671 0.2631 0.4143 0.0307  0.1894  -0.0654 107 PRO   A N   
797  C  CA  . PRO   A 101 ? 0.9257 0.2626 0.4255 0.0352  0.1521  -0.0636 107 PRO   A CA  
798  C  C   . PRO   A 101 ? 0.9065 0.2624 0.4235 0.0284  0.0876  -0.0547 107 PRO   A C   
799  O  O   . PRO   A 101 ? 0.8556 0.2830 0.4609 0.0398  0.0691  -0.0491 107 PRO   A O   
800  C  CB  . PRO   A 101 ? 0.9851 0.2393 0.4071 0.0242  0.1659  -0.0751 107 PRO   A CB  
801  C  CG  . PRO   A 101 ? 1.0213 0.2343 0.4100 0.0268  0.2348  -0.0822 107 PRO   A CG  
802  C  CD  . PRO   A 101 ? 1.0172 0.2234 0.3812 0.0226  0.2391  -0.0774 107 PRO   A CD  
803  N  N   . GLY   A 102 ? 0.9438 0.2340 0.3816 0.0096  0.0558  -0.0516 108 GLY   A N   
804  C  CA  . GLY   A 102 ? 0.9097 0.2146 0.3760 0.0024  -0.0060 -0.0383 108 GLY   A CA  
805  C  C   . GLY   A 102 ? 0.8165 0.2054 0.3763 0.0167  -0.0084 -0.0290 108 GLY   A C   
806  O  O   . GLY   A 102 ? 0.8013 0.2112 0.4080 0.0144  -0.0509 -0.0169 108 GLY   A O   
807  N  N   . ASP   A 103 ? 0.7545 0.1881 0.3456 0.0302  0.0376  -0.0332 109 ASP   A N   
808  C  CA  . ASP   A 103 ? 0.6773 0.1806 0.3428 0.0404  0.0398  -0.0262 109 ASP   A CA  
809  C  C   . ASP   A 103 ? 0.5933 0.1711 0.3535 0.0540  0.0410  -0.0244 109 ASP   A C   
810  O  O   . ASP   A 103 ? 0.5511 0.1757 0.3647 0.0589  0.0409  -0.0193 109 ASP   A O   
811  C  CB  . ASP   A 103 ? 0.6839 0.1971 0.3394 0.0449  0.0838  -0.0290 109 ASP   A CB  
812  C  CG  . ASP   A 103 ? 0.7456 0.1950 0.3195 0.0322  0.0845  -0.0285 109 ASP   A CG  
813  O  OD1 . ASP   A 103 ? 0.7156 0.1425 0.2704 0.0225  0.0444  -0.0210 109 ASP   A OD1 
814  O  OD2 . ASP   A 103 ? 0.8234 0.2421 0.3556 0.0315  0.1262  -0.0341 109 ASP   A OD2 
815  N  N   . CYS   A 104 ? 0.5693 0.1527 0.3447 0.0586  0.0459  -0.0291 110 CYS   A N   
816  C  CA  . CYS   A 104 ? 0.5138 0.1598 0.3708 0.0696  0.0473  -0.0270 110 CYS   A CA  
817  C  C   . CYS   A 104 ? 0.4873 0.1500 0.3923 0.0683  0.0150  -0.0192 110 CYS   A C   
818  O  O   . CYS   A 104 ? 0.5240 0.1491 0.4120 0.0599  -0.0192 -0.0148 110 CYS   A O   
819  C  CB  . CYS   A 104 ? 0.5239 0.1617 0.3822 0.0729  0.0520  -0.0323 110 CYS   A CB  
820  S  SG  . CYS   A 104 ? 0.5994 0.2389 0.4466 0.0799  0.1013  -0.0374 110 CYS   A SG  
821  N  N   . GLY   A 105 ? 0.4369 0.1478 0.4000 0.0744  0.0260  -0.0161 111 GLY   A N   
822  C  CA  . GLY   A 105 ? 0.4144 0.1363 0.4319 0.0742  0.0067  -0.0085 111 GLY   A CA  
823  C  C   . GLY   A 105 ? 0.4113 0.1379 0.4355 0.0715  0.0101  -0.0038 111 GLY   A C   
824  O  O   . GLY   A 105 ? 0.4144 0.1561 0.4944 0.0731  0.0099  0.0017  111 GLY   A O   
825  N  N   . GLY   A 106 ? 0.4095 0.1208 0.3805 0.0674  0.0185  -0.0060 112 GLY   A N   
826  C  CA  . GLY   A 106 ? 0.4020 0.1188 0.3756 0.0647  0.0253  -0.0025 112 GLY   A CA  
827  C  C   . GLY   A 106 ? 0.3636 0.1200 0.3709 0.0675  0.0535  -0.0055 112 GLY   A C   
828  O  O   . GLY   A 106 ? 0.3344 0.1105 0.3383 0.0695  0.0700  -0.0097 112 GLY   A O   
829  N  N   . ILE   A 107 ? 0.3551 0.1175 0.3953 0.0658  0.0582  -0.0020 113 ILE   A N   
830  C  CA  . ILE   A 107 ? 0.3566 0.1396 0.4151 0.0633  0.0846  -0.0054 113 ILE   A CA  
831  C  C   . ILE   A 107 ? 0.3566 0.1466 0.3790 0.0563  0.0998  -0.0074 113 ILE   A C   
832  O  O   . ILE   A 107 ? 0.3769 0.1545 0.3768 0.0544  0.0951  -0.0053 113 ILE   A O   
833  C  CB  . ILE   A 107 ? 0.3692 0.1437 0.4794 0.0634  0.0895  -0.0011 113 ILE   A CB  
834  C  CG1 . ILE   A 107 ? 0.3817 0.1558 0.5468 0.0698  0.0808  0.0026  113 ILE   A CG1 
835  C  CG2 . ILE   A 107 ? 0.3805 0.1555 0.4884 0.0558  0.1211  -0.0057 113 ILE   A CG2 
836  C  CD1 . ILE   A 107 ? 0.3817 0.1456 0.6186 0.0718  0.0867  0.0110  113 ILE   A CD1 
837  N  N   . LEU   A 108 ? 0.3391 0.1454 0.3574 0.0503  0.1154  -0.0094 114 LEU   A N   
838  C  CA  . LEU   A 108 ? 0.3564 0.1695 0.3507 0.0392  0.1262  -0.0083 114 LEU   A CA  
839  C  C   . LEU   A 108 ? 0.3768 0.1758 0.3722 0.0282  0.1423  -0.0112 114 LEU   A C   
840  O  O   . LEU   A 108 ? 0.3418 0.1334 0.3509 0.0271  0.1514  -0.0138 114 LEU   A O   
841  C  CB  . LEU   A 108 ? 0.3497 0.1831 0.3394 0.0357  0.1259  -0.0041 114 LEU   A CB  
842  C  CG  . LEU   A 108 ? 0.3699 0.2107 0.3443 0.0199  0.1292  0.0020  114 LEU   A CG  
843  C  CD1 . LEU   A 108 ? 0.3724 0.2136 0.3381 0.0206  0.1310  0.0044  114 LEU   A CD1 
844  C  CD2 . LEU   A 108 ? 0.3759 0.2377 0.3628 0.0153  0.1225  0.0119  114 LEU   A CD2 
845  N  N   . ARG   A 109 ? 0.4133 0.2017 0.3914 0.0194  0.1502  -0.0115 115 ARG   A N   
846  C  CA  . ARG   A 109 ? 0.4358 0.1988 0.4054 0.0070  0.1714  -0.0158 115 ARG   A CA  
847  C  C   . ARG   A 109 ? 0.4726 0.2295 0.4014 -0.0114 0.1746  -0.0148 115 ARG   A C   
848  O  O   . ARG   A 109 ? 0.4710 0.2424 0.3949 -0.0098 0.1643  -0.0106 115 ARG   A O   
849  C  CB  . ARG   A 109 ? 0.4594 0.2062 0.4587 0.0145  0.1790  -0.0161 115 ARG   A CB  
850  C  CG  . ARG   A 109 ? 0.5126 0.2591 0.5656 0.0293  0.1732  -0.0131 115 ARG   A CG  
851  C  CD  . ARG   A 109 ? 0.5562 0.2872 0.6490 0.0341  0.1764  -0.0078 115 ARG   A CD  
852  N  NE  . ARG   A 109 ? 0.5937 0.2972 0.7003 0.0262  0.2144  -0.0125 115 ARG   A NE  
853  C  CZ  . ARG   A 109 ? 0.6230 0.3109 0.7876 0.0316  0.2351  -0.0106 115 ARG   A CZ  
854  N  NH1 . ARG   A 109 ? 0.6355 0.2873 0.8023 0.0225  0.2797  -0.0168 115 ARG   A NH1 
855  N  NH2 . ARG   A 109 ? 0.6076 0.3104 0.8302 0.0449  0.2135  -0.0018 115 ARG   A NH2 
856  N  N   . CYS   A 110 ? 0.5102 0.2366 0.4069 -0.0306 0.1916  -0.0189 116 CYS   A N   
857  C  CA  . CYS   A 110 ? 0.5510 0.2570 0.4015 -0.0540 0.1945  -0.0184 116 CYS   A CA  
858  C  C   . CYS   A 110 ? 0.5923 0.2517 0.4308 -0.0611 0.2283  -0.0283 116 CYS   A C   
859  O  O   . CYS   A 110 ? 0.5714 0.2244 0.4524 -0.0453 0.2455  -0.0319 116 CYS   A O   
860  C  CB  . CYS   A 110 ? 0.5812 0.2769 0.3900 -0.0768 0.1824  -0.0129 116 CYS   A CB  
861  S  SG  . CYS   A 110 ? 0.6500 0.2960 0.4254 -0.0890 0.2070  -0.0212 116 CYS   A SG  
862  N  N   . GLN   A 111 ? 0.6482 0.2721 0.4351 -0.0853 0.2389  -0.0314 117 GLN   A N   
863  C  CA  . GLN   A 111 ? 0.6988 0.2685 0.4699 -0.0941 0.2793  -0.0419 117 GLN   A CA  
864  C  C   . GLN   A 111 ? 0.7388 0.2613 0.4948 -0.1008 0.3131  -0.0501 117 GLN   A C   
865  O  O   . GLN   A 111 ? 0.7632 0.2360 0.5179 -0.1051 0.3566  -0.0589 117 GLN   A O   
866  C  CB  . GLN   A 111 ? 0.7571 0.2890 0.4600 -0.1241 0.2824  -0.0443 117 GLN   A CB  
867  C  CG  . GLN   A 111 ? 0.8570 0.3621 0.4871 -0.1554 0.2647  -0.0409 117 GLN   A CG  
868  C  CD  . GLN   A 111 ? 0.9906 0.4458 0.5469 -0.1900 0.2659  -0.0427 117 GLN   A CD  
869  O  OE1 . GLN   A 111 ? 1.0322 0.5098 0.5753 -0.2044 0.2282  -0.0306 117 GLN   A OE1 
870  N  NE2 . GLN   A 111 ? 1.0248 0.4075 0.5348 -0.2051 0.3110  -0.0571 117 GLN   A NE2 
871  N  N   . HIS   A 112 ? 0.7448 0.2761 0.4872 -0.1035 0.2980  -0.0470 118 HIS   A N   
872  C  CA  . HIS   A 112 ? 0.7688 0.2504 0.4909 -0.1112 0.3325  -0.0546 118 HIS   A CA  
873  C  C   . HIS   A 112 ? 0.6956 0.2075 0.5034 -0.0809 0.3407  -0.0533 118 HIS   A C   
874  O  O   . HIS   A 112 ? 0.7064 0.1782 0.5151 -0.0833 0.3764  -0.0591 118 HIS   A O   
875  C  CB  . HIS   A 112 ? 0.8442 0.3012 0.4883 -0.1384 0.3137  -0.0511 118 HIS   A CB  
876  C  CG  . HIS   A 112 ? 0.9468 0.3733 0.5085 -0.1728 0.2934  -0.0474 118 HIS   A CG  
877  N  ND1 . HIS   A 112 ? 0.9620 0.4351 0.5241 -0.1789 0.2411  -0.0317 118 HIS   A ND1 
878  C  CD2 . HIS   A 112 ? 1.0307 0.3816 0.5122 -0.2037 0.3190  -0.0562 118 HIS   A CD2 
879  C  CE1 . HIS   A 112 ? 1.0142 0.4428 0.5018 -0.2138 0.2306  -0.0292 118 HIS   A CE1 
880  N  NE2 . HIS   A 112 ? 1.0644 0.4172 0.4948 -0.2306 0.2755  -0.0448 118 HIS   A NE2 
881  N  N   . GLY   A 113 ? 0.6193 0.1946 0.4931 -0.0555 0.3082  -0.0450 119 GLY   A N   
882  C  CA  . GLY   A 113 ? 0.5579 0.1615 0.5093 -0.0302 0.3049  -0.0412 119 GLY   A CA  
883  C  C   . GLY   A 113 ? 0.4982 0.1584 0.4699 -0.0155 0.2602  -0.0333 119 GLY   A C   
884  O  O   . GLY   A 113 ? 0.4847 0.1711 0.4330 -0.0178 0.2333  -0.0292 119 GLY   A O   
885  N  N   . VAL   A 114 ? 0.4647 0.1393 0.4835 -0.0007 0.2567  -0.0312 120 VAL   A N   
886  C  CA  . VAL   A 114 ? 0.4508 0.1671 0.4904 0.0133  0.2225  -0.0257 120 VAL   A CA  
887  C  C   . VAL   A 114 ? 0.4579 0.1803 0.4488 0.0012  0.2126  -0.0250 120 VAL   A C   
888  O  O   . VAL   A 114 ? 0.4830 0.1764 0.4482 -0.0110 0.2318  -0.0281 120 VAL   A O   
889  C  CB  . VAL   A 114 ? 0.4449 0.1662 0.5536 0.0299  0.2239  -0.0231 120 VAL   A CB  
890  C  CG1 . VAL   A 114 ? 0.4516 0.2064 0.5672 0.0405  0.1917  -0.0195 120 VAL   A CG1 
891  C  CG2 . VAL   A 114 ? 0.4251 0.1451 0.5948 0.0410  0.2209  -0.0170 120 VAL   A CG2 
892  N  N   . VAL   A 115 ? 0.4334 0.1884 0.4131 0.0035  0.1845  -0.0192 121 VAL   A N   
893  C  CA  . VAL   A 115 ? 0.4312 0.1991 0.3825 -0.0070 0.1692  -0.0127 121 VAL   A CA  
894  C  C   . VAL   A 115 ? 0.4124 0.2083 0.3970 0.0090  0.1551  -0.0095 121 VAL   A C   
895  O  O   . VAL   A 115 ? 0.4140 0.2118 0.3892 0.0026  0.1506  -0.0049 121 VAL   A O   
896  C  CB  . VAL   A 115 ? 0.4298 0.2161 0.3652 -0.0136 0.1525  -0.0057 121 VAL   A CB  
897  C  CG1 . VAL   A 115 ? 0.4244 0.2292 0.3518 -0.0239 0.1328  0.0069  121 VAL   A CG1 
898  C  CG2 . VAL   A 115 ? 0.4455 0.2029 0.3468 -0.0301 0.1651  -0.0093 121 VAL   A CG2 
899  N  N   . GLY   A 116 ? 0.3901 0.2033 0.4069 0.0272  0.1457  -0.0106 122 GLY   A N   
900  C  CA  . GLY   A 116 ? 0.3697 0.2018 0.4103 0.0409  0.1331  -0.0090 122 GLY   A CA  
901  C  C   . GLY   A 116 ? 0.3546 0.1889 0.4089 0.0544  0.1209  -0.0106 122 GLY   A C   
902  O  O   . GLY   A 116 ? 0.3517 0.1742 0.4047 0.0543  0.1205  -0.0116 122 GLY   A O   
903  N  N   . ILE   A 117 ? 0.3275 0.1696 0.3907 0.0641  0.1105  -0.0103 123 ILE   A N   
904  C  CA  . ILE   A 117 ? 0.3323 0.1615 0.3903 0.0721  0.0963  -0.0118 123 ILE   A CA  
905  C  C   . ILE   A 117 ? 0.3565 0.1864 0.3910 0.0754  0.0974  -0.0115 123 ILE   A C   
906  O  O   . ILE   A 117 ? 0.3676 0.2145 0.4127 0.0767  0.1047  -0.0088 123 ILE   A O   
907  C  CB  . ILE   A 117 ? 0.3230 0.1419 0.4120 0.0783  0.0832  -0.0128 123 ILE   A CB  
908  C  CG1 . ILE   A 117 ? 0.3122 0.1444 0.4225 0.0815  0.0893  -0.0136 123 ILE   A CG1 
909  C  CG2 . ILE   A 117 ? 0.3212 0.1297 0.4448 0.0770  0.0822  -0.0101 123 ILE   A CG2 
910  C  CD1 . ILE   A 117 ? 0.3102 0.1317 0.4407 0.0878  0.0722  -0.0141 123 ILE   A CD1 
911  N  N   . VAL   A 118 ? 0.3673 0.1714 0.3694 0.0761  0.0919  -0.0133 124 VAL   A N   
912  C  CA  . VAL   A 118 ? 0.3794 0.1702 0.3539 0.0784  0.1036  -0.0144 124 VAL   A CA  
913  C  C   . VAL   A 118 ? 0.3788 0.1669 0.3629 0.0842  0.1031  -0.0170 124 VAL   A C   
914  O  O   . VAL   A 118 ? 0.3704 0.1484 0.3624 0.0852  0.0846  -0.0195 124 VAL   A O   
915  C  CB  . VAL   A 118 ? 0.4299 0.1755 0.3514 0.0748  0.0989  -0.0174 124 VAL   A CB  
916  C  CG1 . VAL   A 118 ? 0.4579 0.1779 0.3460 0.0762  0.1226  -0.0202 124 VAL   A CG1 
917  C  CG2 . VAL   A 118 ? 0.4428 0.1908 0.3569 0.0696  0.0995  -0.0142 124 VAL   A CG2 
918  N  N   . SER   A 119 ? 0.3844 0.1840 0.3794 0.0879  0.1231  -0.0144 125 SER   A N   
919  C  CA  . SER   A 119 ? 0.3854 0.1846 0.3949 0.0938  0.1258  -0.0162 125 SER   A CA  
920  C  C   . SER   A 119 ? 0.4213 0.2005 0.4192 0.0977  0.1523  -0.0167 125 SER   A C   
921  O  O   . SER   A 119 ? 0.4235 0.1816 0.4128 0.1011  0.1554  -0.0221 125 SER   A O   
922  C  CB  . SER   A 119 ? 0.3799 0.2215 0.4383 0.0947  0.1233  -0.0088 125 SER   A CB  
923  O  OG  . SER   A 119 ? 0.4381 0.2805 0.5138 0.1007  0.1242  -0.0100 125 SER   A OG  
924  N  N   . THR   A 120 ? 0.4408 0.2236 0.4431 0.0970  0.1754  -0.0107 126 THR   A N   
925  C  CA  . THR   A 120 ? 0.4837 0.2415 0.4842 0.1012  0.2129  -0.0097 126 THR   A CA  
926  C  C   . THR   A 120 ? 0.5471 0.2806 0.5187 0.0970  0.2335  -0.0093 126 THR   A C   
927  O  O   . THR   A 120 ? 0.5546 0.3010 0.5166 0.0913  0.2150  -0.0080 126 THR   A O   
928  C  CB  . THR   A 120 ? 0.4433 0.2447 0.5221 0.1075  0.2279  0.0054  126 THR   A CB  
929  O  OG1 . THR   A 120 ? 0.4376 0.2819 0.5619 0.1029  0.2217  0.0210  126 THR   A OG1 
930  C  CG2 . THR   A 120 ? 0.4086 0.2326 0.5142 0.1110  0.2092  0.0063  126 THR   A CG2 
931  N  N   . GLY   A 121 ? 0.5928 0.2875 0.5515 0.0995  0.2754  -0.0107 127 GLY   A N   
932  C  CA  . GLY   A 121 ? 0.6486 0.3125 0.5803 0.0958  0.3038  -0.0103 127 GLY   A CA  
933  C  C   . GLY   A 121 ? 0.6952 0.3108 0.6230 0.0997  0.3621  -0.0114 127 GLY   A C   
934  O  O   . GLY   A 121 ? 0.6860 0.2963 0.6400 0.1061  0.3811  -0.0114 127 GLY   A O   
935  N  N   . GLY   A 122 ? 0.7437 0.3195 0.6396 0.0958  0.3951  -0.0124 128 GLY   A N   
936  C  CA  . GLY   A 122 ? 0.8012 0.3172 0.6878 0.0984  0.4626  -0.0144 128 GLY   A CA  
937  C  C   . GLY   A 122 ? 0.7842 0.3339 0.7628 0.1041  0.5007  0.0042  128 GLY   A C   
938  O  O   . GLY   A 122 ? 0.7332 0.3653 0.8119 0.1080  0.4751  0.0237  128 GLY   A O   
939  N  N   . ASN   A 123 ? 0.8318 0.3121 0.7742 0.1023  0.5613  -0.0004 129 ASN   A N   
940  C  CA  . ASN   A 123 ? 0.8046 0.3036 0.8366 0.1074  0.6082  0.0177  129 ASN   A CA  
941  C  C   . ASN   A 123 ? 0.7647 0.3215 0.8273 0.1025  0.5690  0.0291  129 ASN   A C   
942  O  O   . ASN   A 123 ? 0.7276 0.3346 0.9001 0.1062  0.5827  0.0515  129 ASN   A O   
943  C  CB  . ASN   A 123 ? 0.7662 0.3174 0.9438 0.1203  0.6356  0.0406  129 ASN   A CB  
944  C  CG  . ASN   A 123 ? 0.8461 0.3429 1.0067 0.1263  0.6794  0.0307  129 ASN   A CG  
945  O  OD1 . ASN   A 123 ? 0.9286 0.3241 0.9952 0.1221  0.7360  0.0119  129 ASN   A OD1 
946  N  ND2 . ASN   A 123 ? 0.7983 0.3544 1.0452 0.1346  0.6565  0.0436  129 ASN   A ND2 
947  N  N   . GLY   A 124 ? 0.7653 0.3096 0.7338 0.0931  0.5224  0.0152  130 GLY   A N   
948  C  CA  . GLY   A 124 ? 0.7217 0.3125 0.7083 0.0875  0.4872  0.0232  130 GLY   A CA  
949  C  C   . GLY   A 124 ? 0.6441 0.3241 0.7041 0.0876  0.4299  0.0360  130 GLY   A C   
950  O  O   . GLY   A 124 ? 0.6273 0.3510 0.7240 0.0820  0.4066  0.0469  130 GLY   A O   
951  N  N   . LEU   A 125 ? 0.5971 0.2974 0.6709 0.0918  0.4078  0.0341  131 LEU   A N   
952  C  CA  . LEU   A 125 ? 0.5319 0.3009 0.6549 0.0894  0.3562  0.0438  131 LEU   A CA  
953  C  C   . LEU   A 125 ? 0.5362 0.2890 0.5822 0.0873  0.3186  0.0254  131 LEU   A C   
954  O  O   . LEU   A 125 ? 0.5802 0.2754 0.5556 0.0887  0.3308  0.0097  131 LEU   A O   
955  C  CB  . LEU   A 125 ? 0.4983 0.3075 0.7162 0.0958  0.3615  0.0613  131 LEU   A CB  
956  C  CG  . LEU   A 125 ? 0.4897 0.3158 0.8123 0.1003  0.4012  0.0849  131 LEU   A CG  
957  C  CD1 . LEU   A 125 ? 0.4550 0.3253 0.8705 0.1046  0.3906  0.1048  131 LEU   A CD1 
958  C  CD2 . LEU   A 125 ? 0.4721 0.3357 0.8445 0.0908  0.3853  0.1028  131 LEU   A CD2 
959  N  N   . VAL   A 126 ? 0.4799 0.2782 0.5414 0.0821  0.2741  0.0288  132 VAL   A N   
960  C  CA  . VAL   A 126 ? 0.4703 0.2637 0.4870 0.0806  0.2399  0.0163  132 VAL   A CA  
961  C  C   . VAL   A 126 ? 0.4330 0.2790 0.5029 0.0784  0.2124  0.0261  132 VAL   A C   
962  O  O   . VAL   A 126 ? 0.4074 0.2878 0.5152 0.0703  0.2013  0.0394  132 VAL   A O   
963  C  CB  . VAL   A 126 ? 0.4859 0.2567 0.4437 0.0740  0.2215  0.0070  132 VAL   A CB  
964  C  CG1 . VAL   A 126 ? 0.4685 0.2689 0.4519 0.0666  0.2169  0.0164  132 VAL   A CG1 
965  C  CG2 . VAL   A 126 ? 0.4919 0.2603 0.4257 0.0731  0.1878  -0.0015 132 VAL   A CG2 
966  N  N   . GLY   A 127 ? 0.4279 0.2722 0.4931 0.0832  0.2013  0.0199  133 GLY   A N   
967  C  CA  . GLY   A 127 ? 0.3923 0.2731 0.4942 0.0807  0.1792  0.0272  133 GLY   A CA  
968  C  C   . GLY   A 127 ? 0.3967 0.2717 0.4664 0.0779  0.1552  0.0161  133 GLY   A C   
969  O  O   . GLY   A 127 ? 0.4180 0.2623 0.4512 0.0823  0.1521  0.0036  133 GLY   A O   
970  N  N   . PHE   A 128 ? 0.3682 0.2664 0.4509 0.0681  0.1385  0.0221  134 PHE   A N   
971  C  CA  . PHE   A 128 ? 0.3630 0.2534 0.4257 0.0645  0.1248  0.0134  134 PHE   A CA  
972  C  C   . PHE   A 128 ? 0.3510 0.2555 0.4333 0.0612  0.1172  0.0182  134 PHE   A C   
973  O  O   . PHE   A 128 ? 0.3308 0.2531 0.4316 0.0519  0.1123  0.0321  134 PHE   A O   
974  C  CB  . PHE   A 128 ? 0.3596 0.2469 0.4040 0.0525  0.1213  0.0134  134 PHE   A CB  
975  C  CG  . PHE   A 128 ? 0.3718 0.2478 0.3982 0.0528  0.1284  0.0118  134 PHE   A CG  
976  C  CD1 . PHE   A 128 ? 0.3943 0.2438 0.3942 0.0590  0.1271  0.0021  134 PHE   A CD1 
977  C  CD2 . PHE   A 128 ? 0.3699 0.2591 0.4084 0.0455  0.1339  0.0225  134 PHE   A CD2 
978  C  CE1 . PHE   A 128 ? 0.4160 0.2490 0.3920 0.0578  0.1339  0.0015  134 PHE   A CE1 
979  C  CE2 . PHE   A 128 ? 0.3826 0.2589 0.4046 0.0459  0.1441  0.0210  134 PHE   A CE2 
980  C  CZ  . PHE   A 128 ? 0.3984 0.2449 0.3844 0.0522  0.1454  0.0097  134 PHE   A CZ  
981  N  N   . ALA   A 129 ? 0.3505 0.2439 0.4301 0.0671  0.1140  0.0090  135 ALA   A N   
982  C  CA  . ALA   A 129 ? 0.3464 0.2457 0.4391 0.0644  0.1108  0.0115  135 ALA   A CA  
983  C  C   . ALA   A 129 ? 0.3667 0.2536 0.4394 0.0501  0.1120  0.0105  135 ALA   A C   
984  O  O   . ALA   A 129 ? 0.3632 0.2335 0.4297 0.0520  0.1170  0.0014  135 ALA   A O   
985  C  CB  . ALA   A 129 ? 0.3532 0.2421 0.4562 0.0763  0.1095  0.0022  135 ALA   A CB  
986  N  N   . ASP   A 130 ? 0.3872 0.2757 0.4478 0.0337  0.1073  0.0212  136 ASP   A N   
987  C  CA  . ASP   A 130 ? 0.4350 0.2960 0.4581 0.0150  0.1127  0.0191  136 ASP   A CA  
988  C  C   . ASP   A 130 ? 0.4464 0.2832 0.4663 0.0169  0.1282  0.0093  136 ASP   A C   
989  O  O   . ASP   A 130 ? 0.4374 0.2827 0.4788 0.0254  0.1265  0.0106  136 ASP   A O   
990  C  CB  . ASP   A 130 ? 0.4689 0.3268 0.4696 -0.0080 0.0971  0.0356  136 ASP   A CB  
991  C  CG  . ASP   A 130 ? 0.5432 0.3592 0.4849 -0.0338 0.1018  0.0337  136 ASP   A CG  
992  O  OD1 . ASP   A 130 ? 0.5572 0.3639 0.4835 -0.0375 0.1087  0.0275  136 ASP   A OD1 
993  O  OD2 . ASP   A 130 ? 0.5903 0.3765 0.4948 -0.0524 0.0992  0.0388  136 ASP   A OD2 
994  N  N   . VAL   A 131 ? 0.4590 0.2636 0.4575 0.0091  0.1472  0.0004  137 VAL   A N   
995  C  CA  . VAL   A 131 ? 0.4644 0.2379 0.4669 0.0093  0.1721  -0.0078 137 VAL   A CA  
996  C  C   . VAL   A 131 ? 0.5174 0.2368 0.4585 -0.0167 0.1957  -0.0108 137 VAL   A C   
997  O  O   . VAL   A 131 ? 0.5288 0.2108 0.4677 -0.0192 0.2267  -0.0179 137 VAL   A O   
998  C  CB  . VAL   A 131 ? 0.4339 0.2098 0.4870 0.0274  0.1822  -0.0155 137 VAL   A CB  
999  C  CG1 . VAL   A 131 ? 0.4096 0.2205 0.5021 0.0467  0.1578  -0.0135 137 VAL   A CG1 
1000 C  CG2 . VAL   A 131 ? 0.4421 0.1997 0.4837 0.0214  0.1946  -0.0194 137 VAL   A CG2 
1001 N  N   . ARG   A 132 ? 0.5387 0.2469 0.4293 -0.0373 0.1841  -0.0054 138 ARG   A N   
1002 C  CA  . ARG   A 132 ? 0.5940 0.2383 0.4099 -0.0667 0.2049  -0.0091 138 ARG   A CA  
1003 C  C   . ARG   A 132 ? 0.6601 0.2569 0.4193 -0.0881 0.2124  -0.0059 138 ARG   A C   
1004 O  O   . ARG   A 132 ? 0.7183 0.2439 0.4085 -0.1118 0.2426  -0.0133 138 ARG   A O   
1005 C  CB  . ARG   A 132 ? 0.5940 0.2356 0.3672 -0.0873 0.1828  -0.0016 138 ARG   A CB  
1006 C  CG  . ARG   A 132 ? 0.5477 0.2315 0.3674 -0.0689 0.1753  -0.0033 138 ARG   A CG  
1007 C  CD  . ARG   A 132 ? 0.5581 0.2424 0.3432 -0.0898 0.1518  0.0068  138 ARG   A CD  
1008 N  NE  . ARG   A 132 ? 0.5612 0.2952 0.3824 -0.0849 0.1167  0.0240  138 ARG   A NE  
1009 C  CZ  . ARG   A 132 ? 0.5986 0.3490 0.4206 -0.0972 0.0926  0.0376  138 ARG   A CZ  
1010 N  NH1 . ARG   A 132 ? 0.6462 0.3671 0.4259 -0.1165 0.0957  0.0348  138 ARG   A NH1 
1011 N  NH2 . ARG   A 132 ? 0.5538 0.3487 0.4252 -0.0902 0.0678  0.0550  138 ARG   A NH2 
1012 N  N   . ASP   A 133 ? 0.6470 0.2753 0.4296 -0.0813 0.1883  0.0049  139 ASP   A N   
1013 C  CA  . ASP   A 133 ? 0.6897 0.2726 0.4166 -0.1025 0.1905  0.0107  139 ASP   A CA  
1014 C  C   . ASP   A 133 ? 0.7029 0.2614 0.4502 -0.0896 0.2308  -0.0013 139 ASP   A C   
1015 O  O   . ASP   A 133 ? 0.7432 0.2419 0.4280 -0.1105 0.2482  -0.0011 139 ASP   A O   
1016 C  CB  . ASP   A 133 ? 0.6843 0.3078 0.4283 -0.1045 0.1450  0.0318  139 ASP   A CB  
1017 C  CG  . ASP   A 133 ? 0.6724 0.3625 0.5082 -0.0691 0.1382  0.0321  139 ASP   A CG  
1018 O  OD1 . ASP   A 133 ? 0.6288 0.3546 0.5171 -0.0454 0.1445  0.0229  139 ASP   A OD1 
1019 O  OD2 . ASP   A 133 ? 0.7043 0.4044 0.5530 -0.0673 0.1258  0.0421  139 ASP   A OD2 
1020 N  N   . LEU   A 134 ? 0.6605 0.2593 0.4933 -0.0577 0.2446  -0.0103 140 LEU   A N   
1021 C  CA  . LEU   A 134 ? 0.6479 0.2341 0.5269 -0.0420 0.2790  -0.0187 140 LEU   A CA  
1022 C  C   . LEU   A 134 ? 0.7043 0.2239 0.5571 -0.0534 0.3317  -0.0307 140 LEU   A C   
1023 O  O   . LEU   A 134 ? 0.6822 0.2131 0.5986 -0.0364 0.3510  -0.0368 140 LEU   A O   
1024 C  CB  . LEU   A 134 ? 0.5788 0.2288 0.5582 -0.0086 0.2643  -0.0197 140 LEU   A CB  
1025 C  CG  . LEU   A 134 ? 0.5539 0.2632 0.5568 0.0032  0.2195  -0.0102 140 LEU   A CG  
1026 C  CD1 . LEU   A 134 ? 0.5155 0.2668 0.5938 0.0298  0.2075  -0.0131 140 LEU   A CD1 
1027 C  CD2 . LEU   A 134 ? 0.5612 0.2701 0.5477 -0.0024 0.2092  -0.0018 140 LEU   A CD2 
1028 N  N   . LEU   A 135 ? 0.7774 0.2202 0.5342 -0.0841 0.3563  -0.0327 141 LEU   A N   
1029 C  CA  . LEU   A 135 ? 0.8393 0.1972 0.5454 -0.1022 0.4151  -0.0452 141 LEU   A CA  
1030 C  C   . LEU   A 135 ? 0.8480 0.1871 0.6312 -0.0828 0.4718  -0.0537 141 LEU   A C   
1031 O  O   . LEU   A 135 ? 0.8640 0.1530 0.6520 -0.0863 0.5241  -0.0633 141 LEU   A O   
1032 C  CB  . LEU   A 135 ? 0.9145 0.1821 0.4806 -0.1448 0.4238  -0.0442 141 LEU   A CB  
1033 C  CG  . LEU   A 135 ? 0.9491 0.2238 0.4384 -0.1711 0.3638  -0.0301 141 LEU   A CG  
1034 C  CD1 . LEU   A 135 ? 1.0482 0.2100 0.3870 -0.2198 0.3769  -0.0293 141 LEU   A CD1 
1035 C  CD2 . LEU   A 135 ? 0.9336 0.2421 0.4393 -0.1685 0.3439  -0.0307 141 LEU   A CD2 
1036 N  N   . TRP   A 136 ? 0.8292 0.2068 0.6791 -0.0628 0.4630  -0.0488 142 TRP   A N   
1037 C  CA  . TRP   A 136 ? 0.8184 0.1871 0.7594 -0.0434 0.5092  -0.0524 142 TRP   A CA  
1038 C  C   . TRP   A 136 ? 0.7842 0.2053 0.8520 -0.0148 0.5072  -0.0505 142 TRP   A C   
1039 O  O   . TRP   A 136 ? 0.7640 0.1716 0.9196 -0.0012 0.5485  -0.0505 142 TRP   A O   
1040 C  CB  . TRP   A 136 ? 0.7969 0.1914 0.7665 -0.0333 0.4936  -0.0464 142 TRP   A CB  
1041 C  CG  . TRP   A 136 ? 0.7642 0.2460 0.7701 -0.0168 0.4244  -0.0367 142 TRP   A CG  
1042 C  CD1 . TRP   A 136 ? 0.7898 0.2893 0.7296 -0.0292 0.3799  -0.0289 142 TRP   A CD1 
1043 C  CD2 . TRP   A 136 ? 0.7060 0.2602 0.8228 0.0132  0.3949  -0.0326 142 TRP   A CD2 
1044 N  NE1 . TRP   A 136 ? 0.7471 0.3245 0.7522 -0.0067 0.3332  -0.0223 142 TRP   A NE1 
1045 C  CE2 . TRP   A 136 ? 0.7023 0.3101 0.8053 0.0177  0.3402  -0.0256 142 TRP   A CE2 
1046 C  CE3 . TRP   A 136 ? 0.6741 0.2482 0.9003 0.0342  0.4072  -0.0321 142 TRP   A CE3 
1047 C  CZ2 . TRP   A 136 ? 0.6637 0.3338 0.8413 0.0408  0.3034  -0.0219 142 TRP   A CZ2 
1048 C  CZ3 . TRP   A 136 ? 0.6382 0.2767 0.9379 0.0551  0.3606  -0.0257 142 TRP   A CZ3 
1049 C  CH2 . TRP   A 136 ? 0.6301 0.3112 0.8972 0.0575  0.3121  -0.0225 142 TRP   A CH2 
1050 N  N   . LEU   A 137 ? 0.7716 0.2495 0.8538 -0.0065 0.4585  -0.0464 143 LEU   A N   
1051 C  CA  . LEU   A 137 ? 0.7469 0.2663 0.9349 0.0159  0.4495  -0.0421 143 LEU   A CA  
1052 C  C   . LEU   A 137 ? 0.8085 0.2736 1.0205 0.0112  0.5085  -0.0469 143 LEU   A C   
1053 O  O   . LEU   A 137 ? 0.7701 0.2567 1.0931 0.0296  0.5140  -0.0397 143 LEU   A O   
1054 C  CB  . LEU   A 137 ? 0.7201 0.2941 0.8902 0.0198  0.3917  -0.0382 143 LEU   A CB  
1055 C  CG  . LEU   A 137 ? 0.6869 0.3206 0.8694 0.0317  0.3375  -0.0318 143 LEU   A CG  
1056 C  CD1 . LEU   A 137 ? 0.6843 0.3555 0.8343 0.0314  0.2942  -0.0292 143 LEU   A CD1 
1057 C  CD2 . LEU   A 137 ? 0.6357 0.3021 0.9239 0.0543  0.3248  -0.0257 143 LEU   A CD2 
1058 N  N   . ASP   A 138 ? 0.9040 0.2939 1.0110 -0.0156 0.5509  -0.0574 144 ASP   A N   
1059 C  CA  . ASP   A 138 ? 0.9715 0.2917 1.0753 -0.0255 0.6171  -0.0650 144 ASP   A CA  
1060 C  C   . ASP   A 138 ? 1.0440 0.2845 1.1523 -0.0327 0.6959  -0.0714 144 ASP   A C   
1061 O  O   . ASP   A 138 ? 1.0797 0.2505 1.1832 -0.0421 0.7622  -0.0787 144 ASP   A O   
1062 C  CB  . ASP   A 138 ? 1.0570 0.3270 1.0198 -0.0567 0.6169  -0.0741 144 ASP   A CB  
1063 C  CG  . ASP   A 138 ? 1.0900 0.4161 1.0636 -0.0504 0.5678  -0.0697 144 ASP   A CG  
1064 O  OD1 . ASP   A 138 ? 1.0583 0.4140 1.1322 -0.0301 0.5728  -0.0650 144 ASP   A OD1 
1065 O  OD2 . ASP   A 138 ? 1.1442 0.4828 1.0305 -0.0666 0.5239  -0.0689 144 ASP   A OD2 
1066 N  N   . GLU   A 139 ? 1.0731 0.3148 1.1811 -0.0307 0.6945  -0.0694 145 GLU   A N   
1067 C  CA  . GLU   A 139 ? 1.1394 0.2987 1.2371 -0.0399 0.7710  -0.0758 145 GLU   A CA  
1068 C  C   . GLU   A 139 ? 1.1150 0.3211 1.3145 -0.0174 0.7598  -0.0663 145 GLU   A C   
1069 O  O   . GLU   A 139 ? 1.1477 0.2936 1.3516 -0.0220 0.8206  -0.0698 145 GLU   A O   
1070 C  CB  . GLU   A 139 ? 1.2773 0.3489 1.1896 -0.0791 0.7858  -0.0867 145 GLU   A CB  
1071 C  CG  . GLU   A 139 ? 1.3605 0.4858 1.2083 -0.0849 0.7057  -0.0793 145 GLU   A CG  
1072 C  CD  . GLU   A 139 ? 1.5470 0.5904 1.2175 -0.1266 0.7037  -0.0834 145 GLU   A CD  
1073 O  OE1 . GLU   A 139 ? 1.5684 0.6313 1.2018 -0.1317 0.6630  -0.0753 145 GLU   A OE1 
1074 O  OE2 . GLU   A 139 ? 1.6523 0.6071 1.2191 -0.1562 0.7411  -0.0933 145 GLU   A OE2 
1075 N  N1  . A1BN7 B .   ? 0.7599 0.3466 0.6203 0.1004  0.2432  -0.0466 201 A1BN7 A N1  
1076 C  C4  . A1BN7 B .   ? 0.7971 0.3240 0.5945 0.0925  0.2293  -0.0592 201 A1BN7 A C4  
1077 C  C5  . A1BN7 B .   ? 0.7752 0.3399 0.6052 0.0962  0.2621  -0.0460 201 A1BN7 A C5  
1078 C  C6  . A1BN7 B .   ? 0.8584 0.3290 0.5733 0.0812  0.2668  -0.0587 201 A1BN7 A C6  
1079 C  C7  . A1BN7 B .   ? 0.8766 0.3427 0.5768 0.0784  0.2826  -0.0547 201 A1BN7 A C7  
1080 C  C8  . A1BN7 B .   ? 0.9224 0.3210 0.5689 0.0740  0.3345  -0.0599 201 A1BN7 A C8  
1081 C  C10 . A1BN7 B .   ? 0.7012 0.3663 0.6575 0.1113  0.2380  -0.0334 201 A1BN7 A C10 
1082 CL CL  . A1BN7 B .   ? 0.8053 0.3961 0.5971 0.0817  0.2008  -0.0393 201 A1BN7 A CL  
1083 C  C9  . A1BN7 B .   ? 0.8541 0.3696 0.5837 0.0784  0.2536  -0.0467 201 A1BN7 A C9  
1084 S  S   . A1BN7 B .   ? 0.8857 0.3677 0.5778 0.0734  0.2862  -0.0455 201 A1BN7 A S   
1085 N  N2  . A1BN7 B .   ? 0.9268 0.3257 0.5635 0.0712  0.3426  -0.0556 201 A1BN7 A N2  
1086 F  F   . A1BN7 B .   ? 0.8889 0.2887 0.5528 0.0779  0.3068  -0.0687 201 A1BN7 A F   
1087 F  F1  . A1BN7 B .   ? 0.8846 0.3353 0.5556 0.0707  0.2155  -0.0629 201 A1BN7 A F1  
1088 O  O1  . A1BN7 B .   ? 0.7245 0.3370 0.6137 0.1022  0.2765  -0.0342 201 A1BN7 A O1  
1089 C  C3  . A1BN7 B .   ? 0.7767 0.3409 0.6044 0.0922  0.1792  -0.0569 201 A1BN7 A C3  
1090 C  C2  . A1BN7 B .   ? 0.7166 0.3607 0.6411 0.1057  0.1815  -0.0461 201 A1BN7 A C2  
1091 C  C1  . A1BN7 B .   ? 0.6794 0.3758 0.6527 0.1104  0.1937  -0.0338 201 A1BN7 A C1  
1092 C  C   . A1BN7 B .   ? 0.6262 0.3884 0.6794 0.1179  0.1890  -0.0210 201 A1BN7 A C   
1093 O  O   . A1BN7 B .   ? 0.6109 0.3812 0.6986 0.1244  0.2049  -0.0171 201 A1BN7 A O   
1094 N  N   . A1BN7 B .   ? 0.6021 0.4040 0.6788 0.1149  0.1669  -0.0143 201 A1BN7 A N   
# 
