data_7I3U
# 
_entry.id   7I3U 
# 
_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   7I3U         pdb_00007i3u 10.2210/pdb7i3u/pdb 
WWPDB D_1001408281 ?            ?                   
# 
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                        7I3U 
_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   2025-03-12 
_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-[1-(furan-3-yl)cyclobutane-1-carbonyl]piperidine-3-carboxamide' 276.331   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                              65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                    78.133    4   ?         ? ? ? 
5 water       nat water                                                                   18.015    192 ?         ? ? ? 
# 
_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-[1-(furan-3-yl)cyclobutane-1-carbonyl]piperidine-3-carboxamide' A1BPF 
3 'ZINC ION'                                                              ZN    
4 'DIMETHYL SULFOXIDE'                                                    DMS   
5 water                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BPF non-polymer         . '(3S)-1-[1-(furan-3-yl)cyclobutane-1-carbonyl]piperidine-3-carboxamide' ? 'C15 H20 N2 O3'  276.331 
ALA   'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                              ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                         ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                    ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                               ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                         ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                 ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                               ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                   ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                 ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                  ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                              ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                  ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                               ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                              ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                  ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                              ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BPF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPF 
_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 A1BPF 1   201 201 A1BPF LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 -1  DMS   DMS A . 
E 4 DMS   1   204 0   DMS   DMS A . 
F 4 DMS   1   205 1   DMS   DMS A . 
G 4 DMS   1   206 3   DMS   DMS A . 
H 5 HOH   1   301 152 HOH   HOH A . 
H 5 HOH   2   302 103 HOH   HOH A . 
H 5 HOH   3   303 219 HOH   HOH A . 
H 5 HOH   4   304 4   HOH   HOH A . 
H 5 HOH   5   305 151 HOH   HOH A . 
H 5 HOH   6   306 129 HOH   HOH A . 
H 5 HOH   7   307 32  HOH   HOH A . 
H 5 HOH   8   308 272 HOH   HOH A . 
H 5 HOH   9   309 36  HOH   HOH A . 
H 5 HOH   10  310 104 HOH   HOH A . 
H 5 HOH   11  311 71  HOH   HOH A . 
H 5 HOH   12  312 137 HOH   HOH A . 
H 5 HOH   13  313 112 HOH   HOH A . 
H 5 HOH   14  314 29  HOH   HOH A . 
H 5 HOH   15  315 30  HOH   HOH A . 
H 5 HOH   16  316 57  HOH   HOH A . 
H 5 HOH   17  317 81  HOH   HOH A . 
H 5 HOH   18  318 218 HOH   HOH A . 
H 5 HOH   19  319 181 HOH   HOH A . 
H 5 HOH   20  320 33  HOH   HOH A . 
H 5 HOH   21  321 77  HOH   HOH A . 
H 5 HOH   22  322 59  HOH   HOH A . 
H 5 HOH   23  323 52  HOH   HOH A . 
H 5 HOH   24  324 34  HOH   HOH A . 
H 5 HOH   25  325 26  HOH   HOH A . 
H 5 HOH   26  326 68  HOH   HOH A . 
H 5 HOH   27  327 16  HOH   HOH A . 
H 5 HOH   28  328 135 HOH   HOH A . 
H 5 HOH   29  329 205 HOH   HOH A . 
H 5 HOH   30  330 234 HOH   HOH A . 
H 5 HOH   31  331 169 HOH   HOH A . 
H 5 HOH   32  332 24  HOH   HOH A . 
H 5 HOH   33  333 37  HOH   HOH A . 
H 5 HOH   34  334 274 HOH   HOH A . 
H 5 HOH   35  335 186 HOH   HOH A . 
H 5 HOH   36  336 2   HOH   HOH A . 
H 5 HOH   37  337 266 HOH   HOH A . 
H 5 HOH   38  338 277 HOH   HOH A . 
H 5 HOH   39  339 255 HOH   HOH A . 
H 5 HOH   40  340 147 HOH   HOH A . 
H 5 HOH   41  341 25  HOH   HOH A . 
H 5 HOH   42  342 21  HOH   HOH A . 
H 5 HOH   43  343 178 HOH   HOH A . 
H 5 HOH   44  344 28  HOH   HOH A . 
H 5 HOH   45  345 252 HOH   HOH A . 
H 5 HOH   46  346 253 HOH   HOH A . 
H 5 HOH   47  347 211 HOH   HOH A . 
H 5 HOH   48  348 259 HOH   HOH A . 
H 5 HOH   49  349 85  HOH   HOH A . 
H 5 HOH   50  350 43  HOH   HOH A . 
H 5 HOH   51  351 216 HOH   HOH A . 
H 5 HOH   52  352 254 HOH   HOH A . 
H 5 HOH   53  353 124 HOH   HOH A . 
H 5 HOH   54  354 116 HOH   HOH A . 
H 5 HOH   55  355 198 HOH   HOH A . 
H 5 HOH   56  356 50  HOH   HOH A . 
H 5 HOH   57  357 15  HOH   HOH A . 
H 5 HOH   58  358 107 HOH   HOH A . 
H 5 HOH   59  359 9   HOH   HOH A . 
H 5 HOH   60  360 269 HOH   HOH A . 
H 5 HOH   61  361 213 HOH   HOH A . 
H 5 HOH   62  362 13  HOH   HOH A . 
H 5 HOH   63  363 174 HOH   HOH A . 
H 5 HOH   64  364 12  HOH   HOH A . 
H 5 HOH   65  365 39  HOH   HOH A . 
H 5 HOH   66  366 18  HOH   HOH A . 
H 5 HOH   67  367 131 HOH   HOH A . 
H 5 HOH   68  368 47  HOH   HOH A . 
H 5 HOH   69  369 19  HOH   HOH A . 
H 5 HOH   70  370 79  HOH   HOH A . 
H 5 HOH   71  371 197 HOH   HOH A . 
H 5 HOH   72  372 231 HOH   HOH A . 
H 5 HOH   73  373 111 HOH   HOH A . 
H 5 HOH   74  374 220 HOH   HOH A . 
H 5 HOH   75  375 109 HOH   HOH A . 
H 5 HOH   76  376 7   HOH   HOH A . 
H 5 HOH   77  377 49  HOH   HOH A . 
H 5 HOH   78  378 273 HOH   HOH A . 
H 5 HOH   79  379 83  HOH   HOH A . 
H 5 HOH   80  380 105 HOH   HOH A . 
H 5 HOH   81  381 146 HOH   HOH A . 
H 5 HOH   82  382 20  HOH   HOH A . 
H 5 HOH   83  383 144 HOH   HOH A . 
H 5 HOH   84  384 214 HOH   HOH A . 
H 5 HOH   85  385 27  HOH   HOH A . 
H 5 HOH   86  386 250 HOH   HOH A . 
H 5 HOH   87  387 100 HOH   HOH A . 
H 5 HOH   88  388 177 HOH   HOH A . 
H 5 HOH   89  389 42  HOH   HOH A . 
H 5 HOH   90  390 5   HOH   HOH A . 
H 5 HOH   91  391 8   HOH   HOH A . 
H 5 HOH   92  392 182 HOH   HOH A . 
H 5 HOH   93  393 168 HOH   HOH A . 
H 5 HOH   94  394 156 HOH   HOH A . 
H 5 HOH   95  395 62  HOH   HOH A . 
H 5 HOH   96  396 225 HOH   HOH A . 
H 5 HOH   97  397 90  HOH   HOH A . 
H 5 HOH   98  398 258 HOH   HOH A . 
H 5 HOH   99  399 11  HOH   HOH A . 
H 5 HOH   100 400 261 HOH   HOH A . 
H 5 HOH   101 401 260 HOH   HOH A . 
H 5 HOH   102 402 84  HOH   HOH A . 
H 5 HOH   103 403 257 HOH   HOH A . 
H 5 HOH   104 404 106 HOH   HOH A . 
H 5 HOH   105 405 256 HOH   HOH A . 
H 5 HOH   106 406 161 HOH   HOH A . 
H 5 HOH   107 407 191 HOH   HOH A . 
H 5 HOH   108 408 263 HOH   HOH A . 
H 5 HOH   109 409 248 HOH   HOH A . 
H 5 HOH   110 410 133 HOH   HOH A . 
H 5 HOH   111 411 40  HOH   HOH A . 
H 5 HOH   112 412 215 HOH   HOH A . 
H 5 HOH   113 413 89  HOH   HOH A . 
H 5 HOH   114 414 80  HOH   HOH A . 
H 5 HOH   115 415 264 HOH   HOH A . 
H 5 HOH   116 416 138 HOH   HOH A . 
H 5 HOH   117 417 203 HOH   HOH A . 
H 5 HOH   118 418 201 HOH   HOH A . 
H 5 HOH   119 419 38  HOH   HOH A . 
H 5 HOH   120 420 123 HOH   HOH A . 
H 5 HOH   121 421 10  HOH   HOH A . 
H 5 HOH   122 422 78  HOH   HOH A . 
H 5 HOH   123 423 148 HOH   HOH A . 
H 5 HOH   124 424 262 HOH   HOH A . 
H 5 HOH   125 425 46  HOH   HOH A . 
H 5 HOH   126 426 76  HOH   HOH A . 
H 5 HOH   127 427 95  HOH   HOH A . 
H 5 HOH   128 428 51  HOH   HOH A . 
H 5 HOH   129 429 87  HOH   HOH A . 
H 5 HOH   130 430 120 HOH   HOH A . 
H 5 HOH   131 431 58  HOH   HOH A . 
H 5 HOH   132 432 23  HOH   HOH A . 
H 5 HOH   133 433 61  HOH   HOH A . 
H 5 HOH   134 434 96  HOH   HOH A . 
H 5 HOH   135 435 157 HOH   HOH A . 
H 5 HOH   136 436 48  HOH   HOH A . 
H 5 HOH   137 437 171 HOH   HOH A . 
H 5 HOH   138 438 101 HOH   HOH A . 
H 5 HOH   139 439 212 HOH   HOH A . 
H 5 HOH   140 440 159 HOH   HOH A . 
H 5 HOH   141 441 175 HOH   HOH A . 
H 5 HOH   142 442 270 HOH   HOH A . 
H 5 HOH   143 443 65  HOH   HOH A . 
H 5 HOH   144 444 69  HOH   HOH A . 
H 5 HOH   145 445 91  HOH   HOH A . 
H 5 HOH   146 446 119 HOH   HOH A . 
H 5 HOH   147 447 224 HOH   HOH A . 
H 5 HOH   148 448 128 HOH   HOH A . 
H 5 HOH   149 449 155 HOH   HOH A . 
H 5 HOH   150 450 210 HOH   HOH A . 
H 5 HOH   151 451 140 HOH   HOH A . 
H 5 HOH   152 452 17  HOH   HOH A . 
H 5 HOH   153 453 102 HOH   HOH A . 
H 5 HOH   154 454 247 HOH   HOH A . 
H 5 HOH   155 455 99  HOH   HOH A . 
H 5 HOH   156 456 14  HOH   HOH A . 
H 5 HOH   157 457 267 HOH   HOH A . 
H 5 HOH   158 458 154 HOH   HOH A . 
H 5 HOH   159 459 176 HOH   HOH A . 
H 5 HOH   160 460 56  HOH   HOH A . 
H 5 HOH   161 461 117 HOH   HOH A . 
H 5 HOH   162 462 204 HOH   HOH A . 
H 5 HOH   163 463 189 HOH   HOH A . 
H 5 HOH   164 464 158 HOH   HOH A . 
H 5 HOH   165 465 206 HOH   HOH A . 
H 5 HOH   166 466 122 HOH   HOH A . 
H 5 HOH   167 467 276 HOH   HOH A . 
H 5 HOH   168 468 60  HOH   HOH A . 
H 5 HOH   169 469 240 HOH   HOH A . 
H 5 HOH   170 470 127 HOH   HOH A . 
H 5 HOH   171 471 209 HOH   HOH A . 
H 5 HOH   172 472 86  HOH   HOH A . 
H 5 HOH   173 473 163 HOH   HOH A . 
H 5 HOH   174 474 268 HOH   HOH A . 
H 5 HOH   175 475 73  HOH   HOH A . 
H 5 HOH   176 476 125 HOH   HOH A . 
H 5 HOH   177 477 187 HOH   HOH A . 
H 5 HOH   178 478 232 HOH   HOH A . 
H 5 HOH   179 479 236 HOH   HOH A . 
H 5 HOH   180 480 208 HOH   HOH A . 
H 5 HOH   181 481 223 HOH   HOH A . 
H 5 HOH   182 482 202 HOH   HOH A . 
H 5 HOH   183 483 207 HOH   HOH A . 
H 5 HOH   184 484 226 HOH   HOH A . 
H 5 HOH   185 485 271 HOH   HOH A . 
H 5 HOH   186 486 275 HOH   HOH A . 
H 5 HOH   187 487 265 HOH   HOH A . 
H 5 HOH   188 488 229 HOH   HOH A . 
H 5 HOH   189 489 92  HOH   HOH A . 
H 5 HOH   190 490 222 HOH   HOH A . 
H 5 HOH   191 491 241 HOH   HOH A . 
H 5 HOH   192 492 278 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           7I3U 
_cell.length_a           87.331 
_cell.length_b           58.279 
_cell.length_c           32.719 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.10 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I3U 
_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          7I3U 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.62 
_exptl_crystal.density_percent_sol   52.98 
_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   2025-01-17 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I3U 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.45 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   15590 
_reflns.percent_possible_obs         98.8 
_reflns.pdbx_Rmerge_I_obs            0.245 
_reflns.pdbx_netI_over_sigmaI        12.1 
_reflns.pdbx_redundancy              7.0 
_reflns.pdbx_Rrim_I_all              0.264 
_reflns.pdbx_Rpim_I_all              0.099 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_number_measured_all     109263 
_reflns.pdbx_chi_squared             0.67 
_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                  1.78 
_reflns_shell.d_res_low                   1.82 
_reflns_shell.number_measured_all         5822 
_reflns_shell.number_unique_obs           877 
_reflns_shell.Rmerge_I_obs                3.877 
_reflns_shell.pdbx_chi_squared            0.23 
_reflns_shell.pdbx_redundancy             6.6 
_reflns_shell.percent_possible_obs        95.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             4.200 
_reflns_shell.pdbx_Rpim_I_all             1.602 
_reflns_shell.pdbx_CC_half                0.314 
_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                                 7I3U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15528 
_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                             48.45 
_refine.ls_d_res_high                            1.780 
_refine.ls_percent_reflns_obs                    98.2 
_refine.ls_R_factor_obs                          0.1913 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1888 
_refine.ls_R_factor_R_free                       0.2385 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_number_reflns_R_free                  772 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_refine.B_iso_mean                               36.18 
_refine.aniso_B[1][1]                            -6.56940 
_refine.aniso_B[2][2]                            2.52000 
_refine.aniso_B[3][3]                            4.04930 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -3.93030 
_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             0.121 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.124 
_refine.pdbx_overall_SU_R_Blow_DPI               0.134 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.132 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I3U 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             193 
_refine_hist.number_atoms_total               1313 
_refine_hist.d_res_high                       1.780 
_refine_hist.d_res_low                        48.45 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.009 ? 2.00  1156 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.94  ? 2.00  1573 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  388  '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  206  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1156 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.66  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.16 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  140  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1055 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   39 
_refine_ls_shell.d_res_high                       1.78 
_refine_ls_shell.d_res_low                        1.80 
_refine_ls_shell.number_reflns_R_work             383 
_refine_ls_shell.R_factor_R_work                  0.3023 
_refine_ls_shell.percent_reflns_obs               85.39 
_refine_ls_shell.R_factor_R_free                  0.4671 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.36 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.number_reflns_all                409 
_refine_ls_shell.R_factor_all                     0.3117 
# 
_struct.entry_id                  7I3U 
_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-0036390-001 (A71EV2A-x4575)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I3U 
_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 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I3U 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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  ? ALA A 23  ? THR A 24  ALA A 29  1 ? 6 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? 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 ? ? ? ? ? ? ? 2.325 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.194 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 111.2 ? 
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_555 107.5 ? 
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_555 117.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.4 ? 
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 96.5  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.8 ? 
# 
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 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I3U 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -104.86 
_pdbx_validate_torsion.psi             41.12 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     415 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_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         15.0555 
_pdbx_refine_tls.origin_y         7.6716 
_pdbx_refine_tls.origin_z         14.1923 
_pdbx_refine_tls.T[1][1]          -0.0149 
_pdbx_refine_tls.T[2][2]          -0.0568 
_pdbx_refine_tls.T[3][3]          -0.0061 
_pdbx_refine_tls.T[1][2]          0.0073 
_pdbx_refine_tls.T[1][3]          0.0558 
_pdbx_refine_tls.T[2][3]          -0.0047 
_pdbx_refine_tls.L[1][1]          1.3138 
_pdbx_refine_tls.L[2][2]          3.0521 
_pdbx_refine_tls.L[3][3]          0.5522 
_pdbx_refine_tls.L[1][2]          -0.1676 
_pdbx_refine_tls.L[1][3]          -0.4166 
_pdbx_refine_tls.L[2][3]          0.6713 
_pdbx_refine_tls.S[1][1]          -0.0273 
_pdbx_refine_tls.S[1][2]          0.0196 
_pdbx_refine_tls.S[1][3]          0.1478 
_pdbx_refine_tls.S[2][1]          0.0078 
_pdbx_refine_tls.S[2][2]          0.1298 
_pdbx_refine_tls.S[2][3]          -0.2118 
_pdbx_refine_tls.S[3][1]          0.0127 
_pdbx_refine_tls.S[3][2]          -0.0344 
_pdbx_refine_tls.S[3][3]          -0.1025 
# 
_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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       492 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.19 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BPF N1   N  N N 1   
A1BPF C4   C  N N 2   
A1BPF C5   C  N N 3   
A1BPF C6   C  N N 4   
A1BPF C7   C  Y N 5   
A1BPF C8   C  Y N 6   
A1BPF C10  C  Y N 7   
A1BPF C13  C  N N 8   
A1BPF O1   O  N N 9   
A1BPF C3   C  N N 10  
A1BPF C2   C  N N 11  
A1BPF C14  C  N N 12  
A1BPF C1   C  N S 13  
A1BPF C    C  N N 14  
A1BPF O    O  N N 15  
A1BPF N    N  N N 16  
A1BPF C12  C  N N 17  
A1BPF C11  C  N N 18  
A1BPF O2   O  Y N 19  
A1BPF C9   C  Y N 20  
A1BPF H8   H  N N 21  
A1BPF H7   H  N N 22  
A1BPF H9   H  N N 23  
A1BPF H11  H  N N 24  
A1BPF H17  H  N N 25  
A1BPF H16  H  N N 26  
A1BPF H6   H  N N 27  
A1BPF H5   H  N N 28  
A1BPF H4   H  N N 29  
A1BPF H3   H  N N 30  
A1BPF H19  H  N N 31  
A1BPF H18  H  N N 32  
A1BPF H    H  N N 33  
A1BPF H1   H  N N 34  
A1BPF H2   H  N N 35  
A1BPF H14  H  N N 36  
A1BPF H15  H  N N 37  
A1BPF H13  H  N N 38  
A1BPF H12  H  N N 39  
A1BPF H10  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
ZN    ZN   ZN N N 441 
# 
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 
A1BPF N   C    sing N N 1   
A1BPF O   C    doub N N 2   
A1BPF C   C1   sing N N 3   
A1BPF C1  C2   sing N N 4   
A1BPF C2  C3   sing N N 5   
A1BPF C3  C4   sing N N 6   
A1BPF C4  N1   sing N N 7   
A1BPF N1  C5   sing N N 8   
A1BPF C5  O1   doub N N 9   
A1BPF C6  C5   sing N N 10  
A1BPF C7  C6   sing N N 11  
A1BPF C7  C8   sing Y N 12  
A1BPF C8  C9   doub Y N 13  
A1BPF C9  O2   sing Y N 14  
A1BPF O2  C10  sing Y N 15  
A1BPF C10 C7   doub Y N 16  
A1BPF C6  C11  sing N N 17  
A1BPF C11 C12  sing N N 18  
A1BPF C12 C13  sing N N 19  
A1BPF C13 C6   sing N N 20  
A1BPF C14 N1   sing N N 21  
A1BPF C1  C14  sing N N 22  
A1BPF C4  H8   sing N N 23  
A1BPF C4  H7   sing N N 24  
A1BPF C8  H9   sing N N 25  
A1BPF C10 H11  sing N N 26  
A1BPF C13 H17  sing N N 27  
A1BPF C13 H16  sing N N 28  
A1BPF C3  H6   sing N N 29  
A1BPF C3  H5   sing N N 30  
A1BPF C2  H4   sing N N 31  
A1BPF C2  H3   sing N N 32  
A1BPF C14 H19  sing N N 33  
A1BPF C14 H18  sing N N 34  
A1BPF C1  H    sing N N 35  
A1BPF N   H1   sing N N 36  
A1BPF N   H2   sing N N 37  
A1BPF C12 H14  sing N N 38  
A1BPF C12 H15  sing N N 39  
A1BPF C11 H13  sing N N 40  
A1BPF C11 H12  sing N N 41  
A1BPF C9  H10  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7I3U 
_atom_sites.fract_transf_matrix[1][1]   0.011451 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000620 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017159 
_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]   0.030608 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.680 6.921   24.417 1.00 37.28  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.869 7.107   23.576 1.00 37.72  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.017 5.969   22.554 1.00 36.18  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.375 4.926   22.698 1.00 36.40  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.126 7.240   24.437 1.00 40.49  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.238 6.145   25.332 1.00 43.60  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.823 6.194   21.516 1.00 34.13  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.048 5.184   20.491 1.00 33.14  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.353 5.765   19.127 1.00 31.79  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.964 6.895   18.829 1.00 31.98  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.003 4.973   18.265 1.00 30.77  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.368 5.436   16.936 1.00 30.23  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.398 4.297   15.930 1.00 30.14  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.528 3.134   16.320 1.00 31.23  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.766 6.078   17.002 1.00 30.21  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.329 4.616   14.625 1.00 29.43  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.503 3.634   13.546 1.00 29.39  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.921 3.811   13.007 1.00 31.02  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.336 4.945   12.760 1.00 31.03  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.504 3.868   12.406 1.00 28.82  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.054 4.034   12.924 1.00 28.46  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.612 2.778   11.314 1.00 29.07  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.110 4.541   11.820 1.00 28.23  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.661 2.700   12.791 1.00 31.81  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.017 2.741   12.258 1.00 32.90  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.045 2.022   10.912 1.00 33.59  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.036 0.799   10.883 1.00 33.98  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.016 2.106   13.247 1.00 33.12  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.184 2.933   14.504 1.00 34.42  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.964 4.083   14.506 1.00 35.22  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.516 2.600   15.673 1.00 35.66  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.057 4.890   15.632 1.00 36.32  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.623 3.385   16.814 1.00 36.69  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.413 4.521   16.795 1.00 37.38  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.500 5.317   17.910 1.00 38.87  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.042 2.776   9.794  1.00 33.38  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.023 2.211   8.447  1.00 33.41  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.154 2.825   7.631  1.00 34.60  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.305 4.047   7.614  1.00 34.09  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.641 2.393   7.771  1.00 34.21  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.193 3.860   7.778  1.00 34.64  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.620 1.800   6.362  1.00 34.95  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.025 1.988   7.034  1.00 35.08  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.187 2.491   6.306  1.00 36.26  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.038 3.401   7.178  1.00 37.13  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.253 3.079   8.347  1.00 37.72  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.354 4.615   6.694  1.00 36.66  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.093 5.568   7.493  1.00 37.05  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.153 6.685   8.015  1.00 36.33  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.532 7.860   8.065  1.00 36.56  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.292 6.108   6.712  1.00 39.86  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.321 5.035   6.433  1.00 46.86  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.061 4.592   7.324  1.00 49.47  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.375 4.563   5.198  1.00 48.27  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.940 6.294   8.445  1.00 34.67  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.922 7.202   8.979  1.00 33.68  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.403 6.762   10.355 1.00 32.78  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.351 5.569   10.647 1.00 33.16  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.732 7.303   8.004  1.00 33.66  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.096 7.823   6.632  1.00 34.69  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.736 9.045   6.479  1.00 35.60  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.769 7.110   5.483  1.00 35.70  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.029 9.552   5.224  1.00 37.20  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.070 7.606   4.216  1.00 37.27  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.701 8.832   4.093  1.00 38.63  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.042 9.359   2.865  1.00 41.92  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.054 7.741   11.201 1.00 31.80  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.407 7.582   12.503 1.00 31.05  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.121 8.416   12.395 1.00 30.01  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.207 9.612   12.147 1.00 30.09  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.298 8.140   13.629 1.00 32.33  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.586 8.369   14.972 1.00 34.84  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.595 8.656   16.070 1.00 36.74  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.125 9.657   17.031 1.00 38.52  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.682 9.383   18.253 1.00 38.79  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.607 8.126   18.675 1.00 37.71  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.288 10.362  19.057 1.00 37.92  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.941 7.791   12.512 1.00 28.66  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.669 8.504   12.442 1.00 27.95  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.137 8.584   13.867 1.00 28.55  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.941 7.541   14.502 1.00 29.31  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.665 7.742   11.533 1.00 27.77  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.362 8.527   11.356 1.00 27.42  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.295 7.401   10.179 1.00 26.78  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.876 9.788   14.360 1.00 27.82  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.331 10.002  15.708 1.00 28.74  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.120 10.955  15.626 1.00 27.92  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.917 11.630  14.603 1.00 28.25  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.410 10.621  16.653 1.00 30.56  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.509 9.622   16.967 1.00 32.26  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.002 11.897  16.044 1.00 31.65  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.368 11.083  16.731 1.00 27.09  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.324 12.088  16.862 1.00 26.90  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.075 13.437  16.909 1.00 27.90  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.084 13.565  17.621 1.00 28.17  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.573 11.918  18.190 1.00 26.85  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.781 10.637  18.266 1.00 27.73  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.264 9.631   18.765 1.00 28.24  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.554 10.653  17.777 1.00 27.73  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.656 14.393  16.098 1.00 27.83  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.319 15.707  16.052 1.00 29.07  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.336 16.378  17.441 1.00 30.37  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.376 16.911  17.833 1.00 30.86  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.646 16.605  15.009 1.00 28.82  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.368 17.921  14.776 1.00 29.48  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.468 18.874  14.043 1.00 31.23  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.148 20.110  13.650 1.00 33.88  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.155 21.229  14.371 1.00 35.84  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.557 21.269  15.557 1.00 35.00  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.745 22.321  13.905 1.00 35.55  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.236 16.231  18.228 1.00 30.01  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.151 16.810  19.577 1.00 30.37  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.080 16.146  20.603 1.00 32.46  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.309 16.714  21.676 1.00 32.77  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.699 16.866  20.085 1.00 30.37  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.117 15.571  20.584 1.00 29.76  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.548 14.653  19.714 1.00 31.09  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.944 15.134  21.854 1.00 30.51  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.073 13.682  20.477 1.00 31.59  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.275 13.932  21.771 1.00 31.05  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.624 14.957  20.288 1.00 33.18  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.572 14.279  21.181 1.00 34.42  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.013 14.282  20.611 1.00 35.58  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.881 13.662  21.215 1.00 36.20  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.149 12.825  21.464 1.00 34.27  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.824 12.635  22.198 1.00 36.19  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.488 11.159  22.347 1.00 36.78  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.837 13.317  23.548 1.00 36.19  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.265 14.930  19.460 1.00 35.99  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.603 14.937  18.864 1.00 37.46  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.630 15.586  19.802 1.00 39.46  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.316 16.582  20.455 1.00 39.44  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.576 15.655  17.527 1.00 37.51  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.817 14.963  19.937 1.00 40.96  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.879 15.450  20.826 1.00 43.15  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.702 16.566  20.150 1.00 45.03  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.559 16.810  18.946 1.00 45.47  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.808 14.274  21.271 1.00 44.30  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.626 13.865  20.170 1.00 45.45  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.057 13.092  21.854 1.00 45.10  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.619 17.214  20.907 1.00 45.37  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.527 18.193  20.338 1.00 45.92  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.397 17.513  19.225 1.00 45.16  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.658 18.128  18.199 1.00 45.25  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.411 18.797  21.456 1.00 47.51  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.602 19.534  20.938 1.00 51.85  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.493 20.824  20.457 1.00 54.28  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.877 19.109  20.776 1.00 53.74  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 32.704 21.157  20.043 1.00 55.01  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.571 20.156  20.207 1.00 55.48  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.808 16.255  19.424 1.00 44.76  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.623 15.541  18.425 1.00 44.79  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.861 15.318  17.099 1.00 43.60  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.472 15.398  16.034 1.00 43.89  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.157 14.219  18.993 1.00 47.41  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.271 13.588  18.184 1.00 52.48  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.439 14.015  18.241 1.00 53.96  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.938 12.553  17.403 1.00 53.52  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.523 15.070  17.159 1.00 41.52  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.672 14.897  15.968 1.00 39.99  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.654 16.176  15.122 1.00 39.38  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.794 16.117  13.901 1.00 38.40  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.228 14.569  16.387 1.00 39.32  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.077 13.163  16.868 1.00 39.49  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.703 12.268  16.266 1.00 37.58  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.326 12.952  17.853 1.00 41.23  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.477 17.329  15.777 1.00 39.49  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.474 18.616  15.091 1.00 40.36  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.846 18.948  14.499 1.00 41.41  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.913 19.570  13.436 1.00 41.28  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.010 19.729  16.040 1.00 40.28  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.528 19.731  16.251 1.00 40.29  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.853 19.251  17.333 1.00 41.23  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.536 20.205  15.334 1.00 40.40  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.494 19.425  17.160 1.00 41.19  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.273 20.012  15.940 1.00 40.75  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.588 20.771  14.055 1.00 40.92  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.081 20.368  15.312 1.00 40.93  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.406 21.160  13.452 1.00 41.62  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.167 20.917  14.063 1.00 41.27  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.933 18.504  15.167 1.00 41.89  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.307 18.727  14.699 1.00 43.11  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.707 17.815  13.544 1.00 43.88  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.798 17.989  12.999 1.00 44.74  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.291 18.552  15.846 1.00 43.59  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.846 16.821  13.189 1.00 43.03  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.053 15.859  12.106 1.00 42.70  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.731 15.686  11.318 1.00 41.57  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.415 14.585  10.881 1.00 41.77  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.484 14.512  12.704 1.00 44.93  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.821 14.570  13.404 1.00 49.52  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.855 14.732  12.768 1.00 51.71  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.839 14.471  14.732 1.00 49.81  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.960 16.776  11.148 1.00 40.21  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.660 16.783  10.471 1.00 39.46  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.652 16.387  8.970  1.00 38.96  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.496 16.853  8.215  1.00 38.86  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.050 18.172  10.632 1.00 39.37  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.601 18.350  10.192 1.00 40.47  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.673 17.414  10.942 1.00 40.44  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.148 19.777  10.401 1.00 40.53  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.654 15.564  8.540  1.00 37.79  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.430 15.169  7.147  1.00 37.00  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.104 15.830  6.643  1.00 36.49  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.070 16.478  5.582  1.00 36.63  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.395 13.620  6.970  1.00 38.28  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.975 13.229  5.555  1.00 39.08  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.741 12.982  7.307  1.00 38.68  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.019 15.663  7.421  1.00 35.20  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.692 16.162  7.075  1.00 34.52  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.801 16.228  8.334  1.00 34.37  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.944 15.418  9.250  1.00 33.70  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.067 15.236  6.004  1.00 34.55  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.597 15.416  5.740  1.00 35.09  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.026 16.244  4.819  1.00 36.59  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.515 14.702  6.365  1.00 34.37  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.654 16.131  4.870  1.00 36.70  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.315 15.180  5.799  1.00 35.38  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.446 13.712  7.353  1.00 33.88  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.068 14.670  6.155  1.00 35.43  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.206 13.230  7.731  1.00 34.48  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.034 13.710  7.143  1.00 35.01  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.897 17.213  8.383  1.00 33.48  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.966 17.334  9.496  1.00 32.77  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.693 18.002  9.006  1.00 32.63  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.733 18.866  8.118  1.00 33.29  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.589 18.050  10.724 1.00 34.63  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.169 19.451  10.490 1.00 37.18  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.183 20.607  10.410 1.00 39.75  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.479 21.576  9.670  1.00 39.96  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.103 20.538  11.046 1.00 37.36  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.568 17.612  9.580  1.00 31.64  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.286 18.186  9.226  1.00 30.65  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.453 18.301  10.510 1.00 30.56  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.997 17.294  11.057 1.00 30.33  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.625 17.333  8.137  1.00 31.70  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.334 17.893  7.587  1.00 36.31  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.718 18.728  8.263  1.00 36.86  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.926 17.472  6.486  1.00 39.00  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.266 19.537  10.996 1.00 29.67  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.497 19.822  12.192 0.50 29.55  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.499 19.757  12.219 0.50 29.74  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.057 19.307  12.055 1.00 29.21  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.509 18.737  12.995 1.00 29.53  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.484 21.329  12.437 0.50 30.35  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.554 21.216  12.671 0.50 31.13  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.109 21.613  13.766 0.50 30.96  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.856 22.059  11.771 0.50 32.98  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.444 19.515  10.876 1.00 28.53  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.058 19.073  10.676 1.00 28.79  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.878 17.517  10.805 1.00 27.26  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.764 17.073  11.021 1.00 26.97  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.518 19.579  9.343  1.00 31.45  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.096 18.800  8.307  1.00 36.63  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.966 16.708  10.662 1.00 26.62  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.916 15.246  10.795 1.00 26.61  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.526 14.718  12.099 1.00 26.70  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.473 13.502  12.332 1.00 26.66  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.657 14.554  9.626  1.00 27.50  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.088 14.866  8.261  1.00 29.70  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.916 14.204  7.156  1.00 30.23  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.871 12.739  7.230  1.00 28.97  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.918 11.935  6.167  1.00 29.22  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.069 12.444  4.944  1.00 26.46  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.864 10.619  6.322  1.00 27.75  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.121 15.611  12.930 1.00 25.75  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.842 15.266  14.143 1.00 25.71  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.989 14.302  13.808 1.00 26.54  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.272 13.412  14.599 1.00 26.97  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.902 14.687  15.235 1.00 26.13  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.580 14.398  16.558 1.00 26.80  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.455 15.217  16.978 1.00 25.31  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.290 13.318  17.154 1.00 27.85  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.652 14.461  12.638 1.00 25.87  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.778 13.591  12.281 1.00 26.08  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.091 14.358  12.091 1.00 26.52  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.088 15.505  11.641 1.00 26.28  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.508 12.801  10.998 1.00 26.54  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.492 11.649  11.106 1.00 28.16  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.334 10.975  9.752  1.00 28.53  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.941 10.629  12.160 1.00 28.06  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.200 13.698  12.404 1.00 26.54  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.545 14.230  12.195 1.00 28.09  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.437 13.037  11.874 1.00 28.87  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.316 11.986  12.496 1.00 28.74  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.065 15.015  13.413 1.00 28.35  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.414 15.757  13.231 1.00 30.65  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.422 17.072  13.991 1.00 31.36  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.598 14.898  13.695 1.00 30.83  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.301 13.187  10.879 1.00 29.70  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.246 12.161  10.463 1.00 30.92  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.636 12.761  10.573 1.00 32.94  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.872 13.877  10.085 1.00 33.30  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.966 11.651  9.024  1.00 31.18  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.106 10.769  8.516  1.00 31.89  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.624 10.899  8.956  1.00 31.67  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.550 12.046  11.233 1.00 33.87  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.953 12.478  11.323 1.00 35.28  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.869 11.384  10.756 1.00 37.33  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.465 10.226  10.688 1.00 36.67  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.334 12.822  12.759 1.00 36.01  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.111 11.750  13.661 1.00 37.63  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.098 11.745  10.315 1.00 39.19  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.035 10.777  9.726  1.00 41.48  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.781 9.981   10.793 1.00 43.54  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.994 10.475  11.903 1.00 44.28  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.061 11.487  8.844  1.00 44.24  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.679 12.523  9.587  1.00 47.47  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.184 8.749   10.459 1.00 44.34  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.905 7.888   11.395 1.00 46.01  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.210 7.373   10.784 1.00 48.16  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.328 7.266   9.555  1.00 48.24  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.012 6.701   11.876 1.00 47.03  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.924 5.700   10.857 1.00 47.89  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.618 7.136   12.309 1.00 47.01  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.165 6.987   11.637 1.00 49.64  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.431 6.451   11.134 1.00 51.45  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.268 4.992   10.739 1.00 51.59  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.701 4.588   9.661  1.00 52.10  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.570 6.678   12.138 1.00 54.11  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.370 5.835   13.279 1.00 55.93  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.667 8.127   12.572 1.00 54.78  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.622 4.203   11.603 1.00 50.71  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.426 2.785   11.339 1.00 50.30  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.103 2.523   10.618 1.00 49.34  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.154 3.288   10.764 1.00 49.11  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.475 2.001   12.646 1.00 50.58  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.040 1.432   9.859  1.00 48.33  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.835 1.064   9.126  1.00 47.95  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.829 0.359   10.010 1.00 45.37  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.206 -0.503  10.796 1.00 45.48  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.179 0.172   7.931  1.00 51.55  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.007 0.884   6.603  1.00 58.57  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.573 -0.079  5.539  1.00 65.66  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.341 -0.418  4.635  1.00 68.81  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.337 -0.557  5.638  1.00 66.50  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.563 0.743   9.859  1.00 42.92  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.419 0.202   10.578 1.00 41.19  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.801 -0.975  9.845  1.00 39.25  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.064 -1.178  8.655  1.00 39.38  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.988 -1.773  10.549 1.00 37.40  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.428 -2.979  9.947  1.00 37.35  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.910 -3.033  9.896  1.00 36.00  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.389 -4.051  9.443  1.00 37.22  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.998 -4.222  10.615 1.00 38.45  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.803 -4.265  10.625 1.00 41.63  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.210 -1.970  10.302 1.00 33.78  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.752 -1.955  10.196 1.00 33.29  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.367 -1.895  8.714  1.00 33.11  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.088 -1.287  7.908  1.00 33.68  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.148 -0.751  10.962 1.00 33.78  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.322 -0.873  12.466 1.00 36.74  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.404 -2.018  12.963 1.00 37.91  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.376 0.177   13.151 1.00 36.76  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.303 -2.594  8.336  1.00 31.92  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.777 -2.540  6.973  1.00 32.20  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.481 -1.732  7.045  1.00 30.80  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.668 -2.011  7.909  1.00 29.92  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.464 -3.954  6.465  1.00 35.60  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.703 -4.622  6.229  1.00 37.05  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.660 -3.941  5.151  1.00 37.01  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.291 -0.751  6.162  1.00 30.09  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.074 0.048   6.136  1.00 29.58  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.028 -0.686  5.295  1.00 28.82  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.352 -1.180  4.217  1.00 29.01  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.341 1.480   5.581  1.00 30.50  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.538 2.138   6.305  1.00 31.43  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.061 2.363   5.709  1.00 30.55  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.315 2.317   7.816  1.00 31.92  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.793 -0.788  5.797  1.00 27.55  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.721 -1.433  5.050  1.00 27.00  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.378 -0.559  3.832  1.00 26.42  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.345 0.673   3.949  1.00 26.15  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.487 -1.562  5.940  1.00 27.03  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.060 -1.182  2.696  1.00 25.44  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.611 -0.436  1.512  1.00 25.68  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.316 -1.145  1.118  1.00 25.60  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.342 -2.124  0.381  1.00 25.73  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.660 -0.420  0.387  1.00 27.49  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.008 0.161   0.811  1.00 29.89  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.989 1.618   1.226  1.00 32.45  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.341 2.071   1.592  1.00 33.20  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.601 3.188   2.266  1.00 34.16  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.616 4.005   2.617  1.00 32.30  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.850 3.505   2.579  1.00 35.26  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.193 -0.679  1.682  1.00 25.63  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.915 -1.393  1.608  1.00 25.46  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.730  -0.468  2.044  1.00 25.86  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.954  0.661   2.470  1.00 24.93  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.030 -2.567  2.590  1.00 24.56  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.011 -2.041  4.327  1.00 25.35  ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.489  -1.002  2.049  0.50 25.96  ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.504  -1.051  2.035  0.50 26.81  ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.322  -0.286  2.558  0.50 26.21  ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.212  -0.491  2.418  0.50 27.93  ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.674  -1.032  3.736  0.50 26.68  ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.610  -1.266  3.617  0.50 27.49  ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.488  -0.804  4.017  0.50 26.49  ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.385  -1.294  3.763  0.50 27.56  ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.279  -0.023  1.454  0.50 28.00  ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.251  -0.660  1.231  0.50 31.77  ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.661  -1.256  0.805  0.50 31.74  ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.327  0.505   0.999  0.50 39.49  ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 6.074  -2.381  1.147  0.50 32.06  ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.656  1.618   1.450  0.50 41.30  ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.779  -1.089  -0.058 0.50 34.05  ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.281  0.310   0.337  0.50 42.06  ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.447  -1.897  4.462  1.00 26.37  ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 6.937  -2.644  5.642  1.00 25.89  ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.213  -1.691  6.613  1.00 25.75  ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.652  -0.547  6.802  1.00 24.79  ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.076  -3.357  6.375  1.00 25.58  ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.714  -4.849  5.561  1.00 28.62  ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.108  -2.155  7.218  1.00 24.95  ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.433  -1.380  8.258  1.00 26.36  ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.343  -2.206  9.573  1.00 26.56  ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.496  -1.917  10.421 1.00 27.32  ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.033  -0.943  7.813  1.00 28.51  ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.003  0.292   6.934  1.00 32.70  ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.552  0.687   6.703  1.00 37.62  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 1.011  0.485   5.617  1.00 38.23  ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 0.880  1.240   7.731  1.00 35.92  ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.178  -3.273  9.715  1.00 25.74  ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.259  -4.107  10.927 1.00 25.70  ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 6.761  -4.332  11.167 1.00 25.43  ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.562  -4.434  10.228 1.00 25.10  ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.462  -5.429  10.832 1.00 27.51  ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.025  -6.249  9.814  1.00 30.44  ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 2.960  -5.222  10.548 1.00 28.48  ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.141  -4.293  12.425 1.00 24.62  ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.534  -4.421  12.807 1.00 24.48  ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 8.663  -4.619  14.298 1.00 24.27  ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 7.679  -4.940  14.960 1.00 23.76  ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 9.891  -4.478  14.819 1.00 24.20  ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.206 -4.657  16.245 1.00 24.62  ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.075 -3.484  16.685 1.00 24.47  ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.030 -3.165  15.986 1.00 25.36  ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 10.959 -6.003  16.488 1.00 26.09  ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.493 -6.081  17.938 1.00 26.91  ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.066 -7.213  16.171 1.00 25.91  ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 10.757 -2.825  17.830 1.00 23.62  ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 11.596 -1.712  18.284 1.00 23.82  ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.171 -1.945  19.666 1.00 24.98  ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 11.552 -2.629  20.480 1.00 24.99  ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 10.845 -0.358  18.223 1.00 23.27  ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 9.944  -0.047  19.408 1.00 24.46  ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 8.657  -0.575  19.491 1.00 25.31  ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 10.348 0.831   20.403 1.00 25.46  ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 7.813  -0.256  20.550 1.00 26.77  ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 9.504  1.168   21.462 1.00 26.75  ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.241  0.614   21.535 1.00 27.62  ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 7.405  0.930   22.575 1.00 29.17  ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.298 -1.286  19.971 1.00 25.28  ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 13.869 -1.393  21.295 1.00 25.74  ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 13.374 -0.247  22.199 1.00 24.90  ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 13.508 0.925   21.850 1.00 23.91  ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 15.397 -1.498  21.272 1.00 26.20  ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 15.952 -1.659  22.669 1.00 27.87  ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 15.662 -2.788  23.431 1.00 29.32  ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 16.720 -0.661  23.253 1.00 28.79  ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 16.116 -2.913  24.742 1.00 30.39  ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 17.194 -0.783  24.553 1.00 30.04  ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 16.889 -1.909  25.297 1.00 31.75  ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 17.376 -2.030  26.580 1.00 34.72  ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 12.836 -0.601  23.375 1.00 25.01  ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 12.347 0.365   24.360 1.00 25.96  ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 13.266 0.319   25.588 1.00 27.54  ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 13.167 -0.613  26.415 1.00 28.49  ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 10.893 0.070   24.738 1.00 26.60  ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 10.245 1.106   26.082 1.00 29.35  ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 14.197 1.272   25.687 1.00 27.36  ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 15.153 1.276   26.789 1.00 28.81  ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 14.527 1.396   28.185 1.00 28.48  ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.029 0.763   29.121 1.00 27.93  ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 16.220 2.351   26.600 1.00 33.36  ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 15.645 3.644   26.657 1.00 39.44  ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 13.404 2.142   28.321 1.00 27.49  ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 12.718 2.292   29.623 1.00 27.85  ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 12.010 1.022   30.122 1.00 28.60  ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 11.514 0.984   31.258 1.00 29.47  ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 11.746 3.466   29.592 1.00 28.14  ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 10.727 3.239   28.635 1.00 27.39  ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 11.945 -0.009  29.284 1.00 28.76  ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 11.409 -1.306  29.701 1.00 29.29  ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 12.439 -2.429  29.531 1.00 30.38  ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 12.117 -3.567  29.843 1.00 30.95  ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 10.175 -1.648  28.868 1.00 29.97  ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.026  -0.674  29.075 1.00 30.66  ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 8.348  -0.982  30.390 1.00 31.18  ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 7.230  -0.080  30.650 1.00 33.38  ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 7.325  1.066   31.319 1.00 35.08  ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 8.504  1.486   31.769 1.00 33.08  ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 6.245  1.803   31.540 1.00 34.45  ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 13.646 -2.145  28.983 1.00 30.68  ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 14.688 -3.124  28.637 1.00 31.80  ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.053 -4.258  27.787 1.00 32.32  ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.265 -5.434  28.083 1.00 33.16  ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 15.384 -3.697  29.898 1.00 33.69  ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 16.242 -2.680  30.657 1.00 37.25  ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.001 -3.346  31.790 1.00 40.23  ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 17.720 -2.378  32.622 1.00 42.96  ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 17.589 -2.268  33.939 1.00 44.20  ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 16.732 -3.043  34.596 1.00 44.24  ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 18.284 -1.355  34.607 1.00 43.74  ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.179 -3.888  26.827 1.00 31.25  ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 12.410 -4.842  26.036 1.00 31.58  ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.248 -4.435  24.587 1.00 30.21  ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.042 -3.257  24.286 1.00 30.45  ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 10.976 -4.956  26.594 1.00 34.98  ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 10.836 -5.784  27.873 1.00 43.71  ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 9.575  -6.659  27.824 1.00 50.71  ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 9.327  -7.380  29.128 1.00 56.51  ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 8.878  -6.451  30.199 1.00 59.85  ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.227 -5.433  23.705 1.00 28.76  ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 11.963 -5.255  22.292 1.00 28.06  ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 10.471 -5.564  22.102 1.00 28.59  ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 9.979  -6.571  22.638 1.00 30.31  ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 12.842 -6.201  21.435 1.00 26.89  ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.312 -5.943  21.557 1.00 26.81  ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.004 -5.225  20.592 1.00 28.72  ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.165 -6.267  22.553 1.00 28.20  ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.259 -5.182  21.009 1.00 29.11  ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.391 -5.763  22.209 1.00 30.08  ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 9.732  -4.683  21.421 1.00 27.74  ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.294  -4.898  21.212 1.00 27.80  ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 7.951  -5.034  19.731 1.00 27.77  ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.318  -4.174  18.943 1.00 26.53  ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 7.484  -3.705  21.731 1.00 28.12  ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 7.475  -3.584  23.238 1.00 28.61  ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 6.677  -4.412  24.016 1.00 30.27  ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.246  -2.629  23.882 1.00 29.69  ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 6.641  -4.285  25.403 1.00 31.28  ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.220  -2.493  25.270 1.00 30.59  ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 7.424  -3.329  26.027 1.00 31.96  ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 7.411  -3.221  27.403 1.00 34.19  ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.121  -6.022  19.375 1.00 27.84  ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 6.632  -6.085  17.988 1.00 28.21  ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 5.502  -5.036  17.820 1.00 27.94  ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 4.640  -4.923  18.697 1.00 28.65  ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.127  -7.526  17.849 1.00 29.10  ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 5.810  -7.968  19.240 1.00 29.34  ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 6.561  -7.098  20.226 1.00 27.38  ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 5.539  -4.229  16.750 1.00 26.82  ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 4.529  -3.186  16.541 1.00 27.08  ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.088  -3.094  15.071 1.00 26.25  ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 4.818  -3.508  14.153 1.00 26.07  ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.058  -1.775  16.982 1.00 28.58  ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.113  -1.629  18.494 1.00 30.07  ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.412  -1.451  16.340 1.00 29.03  ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 2.890  -2.522  14.865 1.00 25.39  ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.411  -2.111  13.552 1.00 27.02  ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 2.623  -0.586  13.577 1.00 26.01  ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.307  0.051   14.575 1.00 26.02  ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 0.924  -2.390  13.381 1.00 30.99  ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.676  -3.777  13.481 1.00 37.25  ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.114  0.005   12.492 1.00 25.16  ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.373  1.442   12.456 1.00 24.38  ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 2.851  2.075   11.185 1.00 24.93  ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 2.765  1.410   10.149 1.00 25.70  ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 4.865  1.768   12.703 1.00 24.06  ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 5.837  1.036   11.805 1.00 24.62  ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.280  -0.234  12.126 1.00 25.09  ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.274  1.604   10.617 1.00 26.08  ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.195  -0.895  11.307 1.00 25.64  ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.183  0.936   9.797  1.00 26.24  ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.629  -0.307  10.140 1.00 25.28  ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.504  3.359   11.256 1.00 24.76  ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 1.945  4.068   10.119 1.00 25.17  ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.011  4.470   9.095  1.00 25.05  ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.209  4.380   9.368  1.00 24.24  ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.152  5.291   10.600 1.00 26.22  ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 1.965  6.208   11.314 1.00 27.31  ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.582  4.876   7.912  1.00 26.15  ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.498  5.332   6.870  1.00 27.70  ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.132  6.692   7.215  1.00 27.62  ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.518  7.485   7.916  1.00 28.16  ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 2.780  5.361   5.503  1.00 31.71  ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 2.996  4.052   4.756  1.00 39.26  ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.236  3.961   3.438  1.00 45.95  ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.638  2.686   2.720  1.00 50.96  ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.786  2.411   1.537  1.00 54.09  ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.383  6.969   6.783  1.00 27.94  ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.018  8.260   7.131  1.00 27.74  ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.154  9.437   6.686  1.00 27.41  ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 4.670  9.478   5.549  1.00 27.33  ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.357  8.220   6.379  1.00 29.27  ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 7.616  6.750   6.120  1.00 30.12  ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.248  6.153   5.903  1.00 27.88  ? 79  PRO   A CD  1 
ATOM   589  N  N   . SER   A 1 74  ? 4.903  10.350  7.615  1.00 27.09  ? 80  SER   A N   1 
ATOM   590  C  CA  . SER   A 1 74  ? 3.981  11.462  7.402  1.00 28.28  ? 80  SER   A CA  1 
ATOM   591  C  C   . SER   A 1 74  ? 4.421  12.731  8.171  1.00 27.54  ? 80  SER   A C   1 
ATOM   592  O  O   . SER   A 1 74  ? 5.343  12.692  8.992  1.00 27.11  ? 80  SER   A O   1 
ATOM   593  C  CB  . SER   A 1 74  ? 2.585  11.044  7.899  1.00 31.83  ? 80  SER   A CB  1 
ATOM   594  O  OG  . SER   A 1 74  ? 2.079  9.911   7.219  1.00 36.17  ? 80  SER   A OG  1 
ATOM   595  N  N   . LEU   A 1 75  ? 3.721  13.843  7.928  1.00 28.15  ? 81  LEU   A N   1 
ATOM   596  C  CA  . LEU   A 1 75  ? 3.923  15.139  8.575  1.00 28.90  ? 81  LEU   A CA  1 
ATOM   597  C  C   . LEU   A 1 75  ? 2.958  15.141  9.768  1.00 29.39  ? 81  LEU   A C   1 
ATOM   598  O  O   . LEU   A 1 75  ? 1.748  15.232  9.570  1.00 29.33  ? 81  LEU   A O   1 
ATOM   599  C  CB  . LEU   A 1 75  ? 3.547  16.217  7.538  1.00 30.25  ? 81  LEU   A CB  1 
ATOM   600  C  CG  . LEU   A 1 75  ? 4.036  17.662  7.762  1.00 32.81  ? 81  LEU   A CG  1 
ATOM   601  C  CD1 . LEU   A 1 75  ? 5.522  17.729  7.829  1.00 32.45  ? 81  LEU   A CD1 1 
ATOM   602  C  CD2 . LEU   A 1 75  ? 3.523  18.608  6.627  1.00 33.61  ? 81  LEU   A CD2 1 
ATOM   603  N  N   . ILE   A 1 76  ? 3.476  14.926  10.990 1.00 28.81  ? 82  ILE   A N   1 
ATOM   604  C  CA  . ILE   A 1 76  ? 2.675  14.791  12.210 1.00 29.46  ? 82  ILE   A CA  1 
ATOM   605  C  C   . ILE   A 1 76  ? 2.989  15.938  13.196 1.00 30.41  ? 82  ILE   A C   1 
ATOM   606  O  O   . ILE   A 1 76  ? 4.161  16.299  13.363 1.00 29.18  ? 82  ILE   A O   1 
ATOM   607  C  CB  . ILE   A 1 76  ? 3.043  13.431  12.862 1.00 30.15  ? 82  ILE   A CB  1 
ATOM   608  C  CG1 . ILE   A 1 76  ? 2.888  12.224  11.877 1.00 31.58  ? 82  ILE   A CG1 1 
ATOM   609  C  CG2 . ILE   A 1 76  ? 2.301  13.192  14.192 1.00 30.65  ? 82  ILE   A CG2 1 
ATOM   610  C  CD1 . ILE   A 1 76  ? 1.537  11.773  11.620 1.00 33.84  ? 82  ILE   A CD1 1 
ATOM   611  N  N   . PHE   A 1 77  ? 1.956  16.520  13.833 1.00 31.77  ? 83  PHE   A N   1 
ATOM   612  C  CA  . PHE   A 1 77  ? 2.170  17.601  14.797 1.00 33.62  ? 83  PHE   A CA  1 
ATOM   613  C  C   . PHE   A 1 77  ? 2.745  17.015  16.057 1.00 33.82  ? 83  PHE   A C   1 
ATOM   614  O  O   . PHE   A 1 77  ? 2.235  16.015  16.584 1.00 34.64  ? 83  PHE   A O   1 
ATOM   615  C  CB  . PHE   A 1 77  ? 0.859  18.366  15.123 1.00 35.32  ? 83  PHE   A CB  1 
ATOM   616  C  CG  . PHE   A 1 77  ? 0.939  19.297  16.328 1.00 37.63  ? 83  PHE   A CG  1 
ATOM   617  C  CD1 . PHE   A 1 77  ? 1.199  20.645  16.165 1.00 38.51  ? 83  PHE   A CD1 1 
ATOM   618  C  CD2 . PHE   A 1 77  ? 0.766  18.811  17.621 1.00 39.34  ? 83  PHE   A CD2 1 
ATOM   619  C  CE1 . PHE   A 1 77  ? 1.279  21.496  17.265 1.00 39.02  ? 83  PHE   A CE1 1 
ATOM   620  C  CE2 . PHE   A 1 77  ? 0.863  19.664  18.723 1.00 40.35  ? 83  PHE   A CE2 1 
ATOM   621  C  CZ  . PHE   A 1 77  ? 1.147  20.998  18.533 1.00 39.34  ? 83  PHE   A CZ  1 
ATOM   622  N  N   . VAL   A 1 78  ? 3.840  17.625  16.530 1.00 32.54  ? 84  VAL   A N   1 
ATOM   623  C  CA  . VAL   A 1 78  ? 4.513  17.225  17.748 1.00 31.74  ? 84  VAL   A CA  1 
ATOM   624  C  C   . VAL   A 1 78  ? 4.496  18.428  18.705 1.00 30.83  ? 84  VAL   A C   1 
ATOM   625  O  O   . VAL   A 1 78  ? 4.932  19.532  18.340 1.00 30.06  ? 84  VAL   A O   1 
ATOM   626  C  CB  . VAL   A 1 78  ? 5.958  16.767  17.452 1.00 32.15  ? 84  VAL   A CB  1 
ATOM   627  C  CG1 . VAL   A 1 78  ? 6.669  16.406  18.747 1.00 33.02  ? 84  VAL   A CG1 1 
ATOM   628  C  CG2 . VAL   A 1 78  ? 5.967  15.594  16.466 1.00 32.50  ? 84  VAL   A CG2 1 
ATOM   629  N  N   . GLU   A 1 79  ? 4.029  18.199  19.922 1.00 30.62  ? 85  GLU   A N   1 
ATOM   630  C  CA  . GLU   A 1 79  ? 3.912  19.236  20.951 1.00 31.68  ? 85  GLU   A CA  1 
ATOM   631  C  C   . GLU   A 1 79  ? 5.241  19.861  21.322 1.00 31.55  ? 85  GLU   A C   1 
ATOM   632  O  O   . GLU   A 1 79  ? 6.293  19.229  21.185 1.00 31.28  ? 85  GLU   A O   1 
ATOM   633  C  CB  . GLU   A 1 79  ? 3.270  18.650  22.205 1.00 35.28  ? 85  GLU   A CB  1 
ATOM   634  C  CG  . GLU   A 1 79  ? 1.827  18.283  22.001 1.00 46.61  ? 85  GLU   A CG  1 
ATOM   635  C  CD  . GLU   A 1 79  ? 0.891  19.154  22.810 1.00 60.50  ? 85  GLU   A CD  1 
ATOM   636  O  OE1 . GLU   A 1 79  ? -0.021 18.599  23.466 1.00 65.57  ? 85  GLU   A OE1 1 
ATOM   637  O  OE2 . GLU   A 1 79  ? 1.073  20.393  22.793 1.00 62.19  ? 85  GLU   A OE2 1 
ATOM   638  N  N   . ALA   A 1 80  ? 5.197  21.097  21.843 1.00 32.02  ? 86  ALA   A N   1 
ATOM   639  C  CA  . ALA   A 1 80  ? 6.407  21.788  22.276 1.00 32.74  ? 86  ALA   A CA  1 
ATOM   640  C  C   . ALA   A 1 80  ? 7.108  21.001  23.376 1.00 33.44  ? 86  ALA   A C   1 
ATOM   641  O  O   . ALA   A 1 80  ? 6.446  20.455  24.253 1.00 34.14  ? 86  ALA   A O   1 
ATOM   642  C  CB  . ALA   A 1 80  ? 6.074  23.185  22.777 1.00 32.38  ? 86  ALA   A CB  1 
ATOM   643  N  N   . SER   A 1 81  ? 8.427  20.925  23.302 1.00 33.15  ? 87  SER   A N   1 
ATOM   644  C  CA  . SER   A 1 81  ? 9.267  20.243  24.281 1.00 34.21  ? 87  SER   A CA  1 
ATOM   645  C  C   . SER   A 1 81  ? 10.451 21.191  24.647 1.00 35.08  ? 87  SER   A C   1 
ATOM   646  O  O   . SER   A 1 81  ? 10.473 22.343  24.184 1.00 35.74  ? 87  SER   A O   1 
ATOM   647  C  CB  . SER   A 1 81  ? 9.789  18.936  23.675 1.00 35.03  ? 87  SER   A CB  1 
ATOM   648  O  OG  . SER   A 1 81  ? 10.778 19.191  22.684 1.00 35.94  ? 87  SER   A OG  1 
ATOM   649  N  N   . GLU   A 1 82  ? 11.444 20.721  25.435 1.00 35.23  ? 88  GLU   A N   1 
ATOM   650  C  CA  . GLU   A 1 82  ? 12.626 21.559  25.697 1.00 36.08  ? 88  GLU   A CA  1 
ATOM   651  C  C   . GLU   A 1 82  ? 13.572 21.633  24.464 1.00 34.74  ? 88  GLU   A C   1 
ATOM   652  O  O   . GLU   A 1 82  ? 14.459 22.498  24.424 1.00 34.80  ? 88  GLU   A O   1 
ATOM   653  C  CB  . GLU   A 1 82  ? 13.381 21.108  26.958 1.00 41.14  ? 88  GLU   A CB  1 
ATOM   654  C  CG  . GLU   A 1 82  ? 13.830 19.665  26.931 1.00 50.91  ? 88  GLU   A CG  1 
ATOM   655  C  CD  . GLU   A 1 82  ? 14.273 19.087  28.263 1.00 62.30  ? 88  GLU   A CD  1 
ATOM   656  O  OE1 . GLU   A 1 82  ? 13.411 18.547  28.996 1.00 64.09  ? 88  GLU   A OE1 1 
ATOM   657  O  OE2 . GLU   A 1 82  ? 15.487 19.163  28.565 1.00 66.29  ? 88  GLU   A OE2 1 
ATOM   658  N  N   . TYR   A 1 83  ? 13.343 20.775  23.438 1.00 33.33  ? 89  TYR   A N   1 
ATOM   659  C  CA  . TYR   A 1 83  ? 14.181 20.672  22.248 1.00 33.06  ? 89  TYR   A CA  1 
ATOM   660  C  C   . TYR   A 1 83  ? 13.638 21.393  21.022 1.00 32.50  ? 89  TYR   A C   1 
ATOM   661  O  O   . TYR   A 1 83  ? 14.428 21.889  20.212 1.00 32.37  ? 89  TYR   A O   1 
ATOM   662  C  CB  . TYR   A 1 83  ? 14.458 19.194  21.923 1.00 33.05  ? 89  TYR   A CB  1 
ATOM   663  C  CG  . TYR   A 1 83  ? 15.091 18.460  23.080 1.00 33.63  ? 89  TYR   A CG  1 
ATOM   664  C  CD1 . TYR   A 1 83  ? 16.444 18.593  23.357 1.00 34.63  ? 89  TYR   A CD1 1 
ATOM   665  C  CD2 . TYR   A 1 83  ? 14.328 17.662  23.924 1.00 35.20  ? 89  TYR   A CD2 1 
ATOM   666  C  CE1 . TYR   A 1 83  ? 17.027 17.941  24.439 1.00 35.93  ? 89  TYR   A CE1 1 
ATOM   667  C  CE2 . TYR   A 1 83  ? 14.895 17.014  25.012 1.00 36.34  ? 89  TYR   A CE2 1 
ATOM   668  C  CZ  . TYR   A 1 83  ? 16.245 17.154  25.266 1.00 37.82  ? 89  TYR   A CZ  1 
ATOM   669  O  OH  . TYR   A 1 83  ? 16.802 16.502  26.336 1.00 41.19  ? 89  TYR   A OH  1 
ATOM   670  N  N   . TYR   A 1 84  ? 12.301 21.452  20.877 1.00 31.88  ? 90  TYR   A N   1 
ATOM   671  C  CA  . TYR   A 1 84  ? 11.703 22.107  19.720 1.00 31.63  ? 90  TYR   A CA  1 
ATOM   672  C  C   . TYR   A 1 84  ? 10.422 22.826  20.108 1.00 32.23  ? 90  TYR   A C   1 
ATOM   673  O  O   . TYR   A 1 84  ? 9.679  22.345  20.969 1.00 32.68  ? 90  TYR   A O   1 
ATOM   674  C  CB  . TYR   A 1 84  ? 11.318 21.062  18.652 1.00 30.38  ? 90  TYR   A CB  1 
ATOM   675  C  CG  . TYR   A 1 84  ? 12.441 20.225  18.091 1.00 29.36  ? 90  TYR   A CG  1 
ATOM   676  C  CD1 . TYR   A 1 84  ? 13.248 20.705  17.070 1.00 29.85  ? 90  TYR   A CD1 1 
ATOM   677  C  CD2 . TYR   A 1 84  ? 12.638 18.917  18.514 1.00 29.09  ? 90  TYR   A CD2 1 
ATOM   678  C  CE1 . TYR   A 1 84  ? 14.238 19.916  16.504 1.00 29.51  ? 90  TYR   A CE1 1 
ATOM   679  C  CE2 . TYR   A 1 84  ? 13.628 18.121  17.961 1.00 29.05  ? 90  TYR   A CE2 1 
ATOM   680  C  CZ  . TYR   A 1 84  ? 14.413 18.616  16.939 1.00 29.14  ? 90  TYR   A CZ  1 
ATOM   681  O  OH  . TYR   A 1 84  ? 15.432 17.858  16.411 1.00 28.11  ? 90  TYR   A OH  1 
ATOM   682  N  N   . PRO   A 1 85  ? 10.073 23.913  19.395 1.00 32.26  ? 91  PRO   A N   1 
ATOM   683  C  CA  . PRO   A 1 85  ? 8.743  24.516  19.608 1.00 32.36  ? 91  PRO   A CA  1 
ATOM   684  C  C   . PRO   A 1 85  ? 7.666  23.607  18.966 1.00 32.63  ? 91  PRO   A C   1 
ATOM   685  O  O   . PRO   A 1 85  ? 8.007  22.654  18.238 1.00 32.67  ? 91  PRO   A O   1 
ATOM   686  C  CB  . PRO   A 1 85  ? 8.850  25.865  18.883 1.00 33.07  ? 91  PRO   A CB  1 
ATOM   687  C  CG  . PRO   A 1 85  ? 9.858  25.638  17.798 1.00 33.81  ? 91  PRO   A CG  1 
ATOM   688  C  CD  . PRO   A 1 85  ? 10.814 24.571  18.295 1.00 31.86  ? 91  PRO   A CD  1 
ATOM   689  N  N   . ALA   A 1 86  ? 6.367  23.893  19.191 1.00 32.60  ? 92  ALA   A N   1 
ATOM   690  C  CA  . ALA   A 1 86  ? 5.295  23.075  18.606 1.00 33.20  ? 92  ALA   A CA  1 
ATOM   691  C  C   . ALA   A 1 86  ? 5.388  23.171  17.081 1.00 33.17  ? 92  ALA   A C   1 
ATOM   692  O  O   . ALA   A 1 86  ? 5.592  24.272  16.559 1.00 33.16  ? 92  ALA   A O   1 
ATOM   693  C  CB  . ALA   A 1 86  ? 3.932  23.542  19.108 1.00 33.84  ? 92  ALA   A CB  1 
ATOM   694  N  N   . ARG   A 1 87  ? 5.467  22.017  16.395 1.00 32.55  ? 93  ARG   A N   1 
ATOM   695  C  CA  . ARG   A 1 87  ? 5.700  22.017  14.950 1.00 32.37  ? 93  ARG   A CA  1 
ATOM   696  C  C   . ARG   A 1 87  ? 5.239  20.699  14.268 1.00 32.34  ? 93  ARG   A C   1 
ATOM   697  O  O   . ARG   A 1 87  ? 4.893  19.737  14.940 1.00 32.65  ? 93  ARG   A O   1 
ATOM   698  C  CB  . ARG   A 1 87  ? 7.227  22.210  14.703 1.00 32.89  ? 93  ARG   A CB  1 
ATOM   699  C  CG  . ARG   A 1 87  ? 8.033  20.910  14.854 1.00 32.16  ? 93  ARG   A CG  1 
ATOM   700  C  CD  . ARG   A 1 87  ? 9.435  21.074  15.389 1.00 31.16  ? 93  ARG   A CD  1 
ATOM   701  N  NE  . ARG   A 1 87  ? 10.353 20.036  14.900 1.00 29.82  ? 93  ARG   A NE  1 
ATOM   702  C  CZ  . ARG   A 1 87  ? 10.423 18.801  15.396 1.00 31.07  ? 93  ARG   A CZ  1 
ATOM   703  N  NH1 . ARG   A 1 87  ? 9.594  18.416  16.380 1.00 29.29  ? 93  ARG   A NH1 1 
ATOM   704  N  NH2 . ARG   A 1 87  ? 11.330 17.945  14.933 1.00 29.13  ? 93  ARG   A NH2 1 
ATOM   705  N  N   . TYR   A 1 88  ? 5.280  20.659  12.930 1.00 32.33  ? 94  TYR   A N   1 
ATOM   706  C  CA  . TYR   A 1 88  ? 5.001  19.435  12.196 1.00 32.96  ? 94  TYR   A CA  1 
ATOM   707  C  C   . TYR   A 1 88  ? 6.353  18.776  11.973 1.00 30.18  ? 94  TYR   A C   1 
ATOM   708  O  O   . TYR   A 1 88  ? 7.263  19.420  11.448 1.00 30.96  ? 94  TYR   A O   1 
ATOM   709  C  CB  . TYR   A 1 88  ? 4.428  19.740  10.815 1.00 34.93  ? 94  TYR   A CB  1 
ATOM   710  C  CG  . TYR   A 1 88  ? 3.026  20.291  10.838 1.00 37.84  ? 94  TYR   A CG  1 
ATOM   711  C  CD1 . TYR   A 1 88  ? 1.946  19.482  11.150 1.00 39.41  ? 94  TYR   A CD1 1 
ATOM   712  C  CD2 . TYR   A 1 88  ? 2.772  21.608  10.476 1.00 39.86  ? 94  TYR   A CD2 1 
ATOM   713  C  CE1 . TYR   A 1 88  ? 0.645  19.986  11.156 1.00 41.24  ? 94  TYR   A CE1 1 
ATOM   714  C  CE2 . TYR   A 1 88  ? 1.483  22.125  10.487 1.00 41.26  ? 94  TYR   A CE2 1 
ATOM   715  C  CZ  . TYR   A 1 88  ? 0.419  21.308  10.816 1.00 42.49  ? 94  TYR   A CZ  1 
ATOM   716  O  OH  . TYR   A 1 88  ? -0.852 21.833  10.794 1.00 44.59  ? 94  TYR   A OH  1 
ATOM   717  N  N   . GLN   A 1 89  ? 6.517  17.556  12.437 1.00 27.76  ? 95  GLN   A N   1 
ATOM   718  C  CA  . GLN   A 1 89  ? 7.748  16.800  12.183 1.00 26.69  ? 95  GLN   A CA  1 
ATOM   719  C  C   . GLN   A 1 89  ? 7.444  15.937  10.959 1.00 26.46  ? 95  GLN   A C   1 
ATOM   720  O  O   . GLN   A 1 89  ? 6.417  15.253  10.934 1.00 26.64  ? 95  GLN   A O   1 
ATOM   721  C  CB  . GLN   A 1 89  ? 8.149  15.926  13.387 1.00 26.85  ? 95  GLN   A CB  1 
ATOM   722  C  CG  . GLN   A 1 89  ? 9.458  15.154  13.117 1.00 28.89  ? 95  GLN   A CG  1 
ATOM   723  C  CD  . GLN   A 1 89  ? 10.121 14.589  14.354 1.00 29.31  ? 95  GLN   A CD  1 
ATOM   724  O  OE1 . GLN   A 1 89  ? 10.267 15.260  15.394 1.00 27.91  ? 95  GLN   A OE1 1 
ATOM   725  N  NE2 . GLN   A 1 89  ? 10.571 13.348  14.249 1.00 27.04  ? 95  GLN   A NE2 1 
ATOM   726  N  N   . SER   A 1 90  ? 8.298  15.984  9.936  1.00 25.88  ? 96  SER   A N   1 
ATOM   727  C  CA  . SER   A 1 90  ? 8.078  15.178  8.719  1.00 25.48  ? 96  SER   A CA  1 
ATOM   728  C  C   . SER   A 1 90  ? 8.753  13.778  8.800  1.00 24.57  ? 96  SER   A C   1 
ATOM   729  O  O   . SER   A 1 90  ? 9.590  13.556  9.679  1.00 24.50  ? 96  SER   A O   1 
ATOM   730  C  CB  . SER   A 1 90  ? 8.572  15.936  7.488  1.00 26.35  ? 96  SER   A CB  1 
ATOM   731  O  OG  . SER   A 1 90  ? 9.972  16.135  7.569  1.00 28.43  ? 96  SER   A OG  1 
ATOM   732  N  N   . HIS   A 1 91  ? 8.375  12.857  7.884  1.00 23.53  ? 97  HIS   A N   1 
ATOM   733  C  CA  . HIS   A 1 91  ? 8.880  11.480  7.781  1.00 23.91  ? 97  HIS   A CA  1 
ATOM   734  C  C   . HIS   A 1 91  ? 8.732  10.694  9.136  1.00 24.37  ? 97  HIS   A C   1 
ATOM   735  O  O   . HIS   A 1 91  ? 9.582  9.873   9.483  1.00 25.28  ? 97  HIS   A O   1 
ATOM   736  C  CB  . HIS   A 1 91  ? 10.328 11.475  7.244  1.00 24.40  ? 97  HIS   A CB  1 
ATOM   737  C  CG  . HIS   A 1 91  ? 10.501 12.156  5.908  1.00 27.39  ? 97  HIS   A CG  1 
ATOM   738  N  ND1 . HIS   A 1 91  ? 10.555 11.426  4.733  1.00 29.82  ? 97  HIS   A ND1 1 
ATOM   739  C  CD2 . HIS   A 1 91  ? 10.627 13.475  5.609  1.00 28.27  ? 97  HIS   A CD2 1 
ATOM   740  C  CE1 . HIS   A 1 91  ? 10.716 12.314  3.757  1.00 30.44  ? 97  HIS   A CE1 1 
ATOM   741  N  NE2 . HIS   A 1 91  ? 10.739 13.564  4.237  1.00 29.94  ? 97  HIS   A NE2 1 
ATOM   742  N  N   . LEU   A 1 92  ? 7.660  10.976  9.886  1.00 23.42  ? 98  LEU   A N   1 
ATOM   743  C  CA  . LEU   A 1 92  ? 7.431  10.377  11.198 1.00 23.57  ? 98  LEU   A CA  1 
ATOM   744  C  C   . LEU   A 1 92  ? 6.374  9.289   11.062 1.00 23.76  ? 98  LEU   A C   1 
ATOM   745  O  O   . LEU   A 1 92  ? 5.379  9.467   10.350 1.00 24.97  ? 98  LEU   A O   1 
ATOM   746  C  CB  . LEU   A 1 92  ? 6.966  11.451  12.222 1.00 23.40  ? 98  LEU   A CB  1 
ATOM   747  C  CG  . LEU   A 1 92  ? 6.799  11.011  13.698 1.00 24.18  ? 98  LEU   A CG  1 
ATOM   748  C  CD1 . LEU   A 1 92  ? 8.121  10.542  14.283 1.00 24.76  ? 98  LEU   A CD1 1 
ATOM   749  C  CD2 . LEU   A 1 92  ? 6.236  12.139  14.550 1.00 25.66  ? 98  LEU   A CD2 1 
ATOM   750  N  N   . MET   A 1 93  ? 6.571  8.189   11.798 1.00 23.20  ? 99  MET   A N   1 
ATOM   751  C  CA  . MET   A 1 93  ? 5.662  7.048   11.796 1.00 22.78  ? 99  MET   A CA  1 
ATOM   752  C  C   . MET   A 1 93  ? 5.234  6.772   13.231 1.00 23.29  ? 99  MET   A C   1 
ATOM   753  O  O   . MET   A 1 93  ? 6.087  6.789   14.111 1.00 23.27  ? 99  MET   A O   1 
ATOM   754  C  CB  . MET   A 1 93  ? 6.433  5.832   11.265 1.00 23.65  ? 99  MET   A CB  1 
ATOM   755  C  CG  . MET   A 1 93  ? 6.924  6.040   9.827  1.00 24.69  ? 99  MET   A CG  1 
ATOM   756  S  SD  . MET   A 1 93  ? 7.930  4.653   9.272  1.00 26.36  ? 99  MET   A SD  1 
ATOM   757  C  CE  . MET   A 1 93  ? 9.363  4.844   10.232 1.00 22.75  ? 99  MET   A CE  1 
ATOM   758  N  N   . LEU   A 1 94  ? 3.939  6.533   13.479 1.00 22.95  ? 100 LEU   A N   1 
ATOM   759  C  CA  . LEU   A 1 94  ? 3.484  6.226   14.852 1.00 23.64  ? 100 LEU   A CA  1 
ATOM   760  C  C   . LEU   A 1 94  ? 3.083  4.762   15.012 1.00 23.07  ? 100 LEU   A C   1 
ATOM   761  O  O   . LEU   A 1 94  ? 2.588  4.134   14.076 1.00 22.69  ? 100 LEU   A O   1 
ATOM   762  C  CB  . LEU   A 1 94  ? 2.263  7.093   15.273 1.00 24.76  ? 100 LEU   A CB  1 
ATOM   763  C  CG  . LEU   A 1 94  ? 2.399  8.612   15.212 1.00 27.58  ? 100 LEU   A CG  1 
ATOM   764  C  CD1 . LEU   A 1 94  ? 1.138  9.282   15.789 1.00 29.15  ? 100 LEU   A CD1 1 
ATOM   765  C  CD2 . LEU   A 1 94  ? 3.649  9.093   15.963 1.00 28.51  ? 100 LEU   A CD2 1 
ATOM   766  N  N   . ALA   A 1 95  ? 3.194  4.273   16.239 1.00 22.54  ? 101 ALA   A N   1 
ATOM   767  C  CA  . ALA   A 1 95  ? 2.761  2.950   16.682 1.00 22.66  ? 101 ALA   A CA  1 
ATOM   768  C  C   . ALA   A 1 95  ? 2.152  3.132   18.076 1.00 23.74  ? 101 ALA   A C   1 
ATOM   769  O  O   . ALA   A 1 95  ? 2.450  4.114   18.757 1.00 23.81  ? 101 ALA   A O   1 
ATOM   770  C  CB  . ALA   A 1 95  ? 3.952  1.993   16.778 1.00 21.90  ? 101 ALA   A CB  1 
ATOM   771  N  N   . VAL   A 1 96  ? 1.332  2.176   18.496 1.00 24.86  ? 102 VAL   A N   1 
ATOM   772  C  CA  . VAL   A 1 96  ? 0.789  2.126   19.841 1.00 26.61  ? 102 VAL   A CA  1 
ATOM   773  C  C   . VAL   A 1 96  ? 1.873  1.381   20.642 1.00 28.53  ? 102 VAL   A C   1 
ATOM   774  O  O   . VAL   A 1 96  ? 2.191  0.225   20.356 1.00 27.70  ? 102 VAL   A O   1 
ATOM   775  C  CB  . VAL   A 1 96  ? -0.556 1.376   19.847 1.00 27.67  ? 102 VAL   A CB  1 
ATOM   776  C  CG1 . VAL   A 1 96  ? -1.059 1.148   21.281 1.00 27.94  ? 102 VAL   A CG1 1 
ATOM   777  C  CG2 . VAL   A 1 96  ? -1.591 2.136   19.023 1.00 28.64  ? 102 VAL   A CG2 1 
ATOM   778  N  N   . GLY   A 1 97  ? 2.477  2.072   21.595 1.00 30.20  ? 103 GLY   A N   1 
ATOM   779  C  CA  . GLY   A 1 97  ? 3.534  1.488   22.413 1.00 30.57  ? 103 GLY   A CA  1 
ATOM   780  C  C   . GLY   A 1 97  ? 4.089  2.458   23.434 1.00 30.66  ? 103 GLY   A C   1 
ATOM   781  O  O   . GLY   A 1 97  ? 3.671  3.624   23.488 1.00 30.43  ? 103 GLY   A O   1 
ATOM   782  N  N   . HIS   A 1 98  ? 5.029  1.984   24.260 1.00 29.41  ? 104 HIS   A N   1 
ATOM   783  C  CA  . HIS   A 1 98  ? 5.630  2.807   25.297 1.00 28.82  ? 104 HIS   A CA  1 
ATOM   784  C  C   . HIS   A 1 98  ? 6.883  3.567   24.830 1.00 28.12  ? 104 HIS   A C   1 
ATOM   785  O  O   . HIS   A 1 98  ? 7.815  2.978   24.287 1.00 28.34  ? 104 HIS   A O   1 
ATOM   786  C  CB  . HIS   A 1 98  ? 5.953  1.984   26.561 1.00 28.77  ? 104 HIS   A CB  1 
ATOM   787  C  CG  . HIS   A 1 98  ? 6.433  2.865   27.673 1.00 30.86  ? 104 HIS   A CG  1 
ATOM   788  N  ND1 . HIS   A 1 98  ? 5.580  3.777   28.291 1.00 32.22  ? 104 HIS   A ND1 1 
ATOM   789  C  CD2 . HIS   A 1 98  ? 7.673  3.017   28.184 1.00 31.53  ? 104 HIS   A CD2 1 
ATOM   790  C  CE1 . HIS   A 1 98  ? 6.324  4.431   29.163 1.00 32.80  ? 104 HIS   A CE1 1 
ATOM   791  N  NE2 . HIS   A 1 98  ? 7.584  4.003   29.148 1.00 32.66  ? 104 HIS   A NE2 1 
ATOM   792  N  N   . SER   A 1 99  ? 6.931  4.868   25.127 1.00 27.44  ? 105 SER   A N   1 
ATOM   793  C  CA  . SER   A 1 99  ? 8.087  5.681   24.790 1.00 27.65  ? 105 SER   A CA  1 
ATOM   794  C  C   . SER   A 1 99  ? 8.089  6.844   25.767 1.00 29.90  ? 105 SER   A C   1 
ATOM   795  O  O   . SER   A 1 99  ? 7.088  7.551   25.888 1.00 30.65  ? 105 SER   A O   1 
ATOM   796  C  CB  . SER   A 1 99  ? 7.992  6.165   23.342 1.00 27.73  ? 105 SER   A CB  1 
ATOM   797  O  OG  . SER   A 1 99  ? 9.023  7.075   23.003 1.00 28.99  ? 105 SER   A OG  1 
ATOM   798  N  N   . GLU   A 1 100 ? 9.171  6.999   26.511 1.00 30.18  ? 106 GLU   A N   1 
ATOM   799  C  CA  . GLU   A 1 100 ? 9.287  8.095   27.469 1.00 30.97  ? 106 GLU   A CA  1 
ATOM   800  C  C   . GLU   A 1 100 ? 10.656 8.759   27.320 1.00 32.89  ? 106 GLU   A C   1 
ATOM   801  O  O   . GLU   A 1 100 ? 11.528 8.184   26.669 1.00 34.14  ? 106 GLU   A O   1 
ATOM   802  C  CB  . GLU   A 1 100 ? 9.025  7.595   28.922 1.00 31.18  ? 106 GLU   A CB  1 
ATOM   803  C  CG  . GLU   A 1 100 ? 10.063 6.621   29.432 1.00 34.61  ? 106 GLU   A CG  1 
ATOM   804  C  CD  . GLU   A 1 100 ? 9.781  6.206   30.870 1.00 38.02  ? 106 GLU   A CD  1 
ATOM   805  O  OE1 . GLU   A 1 100 ? 10.180 6.953   31.785 1.00 41.08  ? 106 GLU   A OE1 1 
ATOM   806  O  OE2 . GLU   A 1 100 ? 9.125  5.163   31.081 1.00 36.87  ? 106 GLU   A OE2 1 
ATOM   807  N  N   . PRO   A 1 101 ? 10.872 9.984   27.851 1.00 34.03  ? 107 PRO   A N   1 
ATOM   808  C  CA  . PRO   A 1 101 ? 12.208 10.611  27.739 1.00 34.37  ? 107 PRO   A CA  1 
ATOM   809  C  C   . PRO   A 1 101 ? 13.340 9.682   28.179 1.00 33.88  ? 107 PRO   A C   1 
ATOM   810  O  O   . PRO   A 1 101 ? 13.347 9.185   29.316 1.00 34.62  ? 107 PRO   A O   1 
ATOM   811  C  CB  . PRO   A 1 101 ? 12.106 11.828  28.659 1.00 35.17  ? 107 PRO   A CB  1 
ATOM   812  C  CG  . PRO   A 1 101 ? 10.666 12.153  28.704 1.00 35.73  ? 107 PRO   A CG  1 
ATOM   813  C  CD  . PRO   A 1 101 ? 9.943  10.837  28.629 1.00 33.51  ? 107 PRO   A CD  1 
ATOM   814  N  N   . GLY   A 1 102 ? 14.232 9.404   27.236 1.00 31.67  ? 108 GLY   A N   1 
ATOM   815  C  CA  . GLY   A 1 102 ? 15.339 8.467   27.379 1.00 30.08  ? 108 GLY   A CA  1 
ATOM   816  C  C   . GLY   A 1 102 ? 15.267 7.356   26.333 1.00 28.33  ? 108 GLY   A C   1 
ATOM   817  O  O   . GLY   A 1 102 ? 16.280 6.722   26.029 1.00 28.21  ? 108 GLY   A O   1 
ATOM   818  N  N   . ASP   A 1 103 ? 14.059 7.124   25.736 1.00 25.81  ? 109 ASP   A N   1 
ATOM   819  C  CA  . ASP   A 1 103 ? 13.860 6.094   24.725 1.00 24.78  ? 109 ASP   A CA  1 
ATOM   820  C  C   . ASP   A 1 103 ? 14.272 6.494   23.316 1.00 23.93  ? 109 ASP   A C   1 
ATOM   821  O  O   . ASP   A 1 103 ? 14.495 5.601   22.481 1.00 23.89  ? 109 ASP   A O   1 
ATOM   822  C  CB  . ASP   A 1 103 ? 12.409 5.595   24.726 1.00 25.05  ? 109 ASP   A CB  1 
ATOM   823  C  CG  . ASP   A 1 103 ? 12.143 4.728   25.943 1.00 27.34  ? 109 ASP   A CG  1 
ATOM   824  O  OD1 . ASP   A 1 103 ? 13.065 3.998   26.357 1.00 27.96  ? 109 ASP   A OD1 1 
ATOM   825  O  OD2 . ASP   A 1 103 ? 11.022 4.776   26.471 1.00 27.36  ? 109 ASP   A OD2 1 
ATOM   826  N  N   . CYS   A 1 104 ? 14.444 7.803   23.046 1.00 23.78  ? 110 CYS   A N   1 
ATOM   827  C  CA  . CYS   A 1 104 ? 14.881 8.220   21.696 1.00 25.11  ? 110 CYS   A CA  1 
ATOM   828  C  C   . CYS   A 1 104 ? 16.197 7.546   21.285 1.00 26.58  ? 110 CYS   A C   1 
ATOM   829  O  O   . CYS   A 1 104 ? 17.067 7.354   22.119 1.00 27.97  ? 110 CYS   A O   1 
ATOM   830  C  CB  . CYS   A 1 104 ? 14.946 9.743   21.561 1.00 26.35  ? 110 CYS   A CB  1 
ATOM   831  S  SG  . CYS   A 1 104 ? 13.327 10.561  21.675 1.00 29.51  ? 110 CYS   A SG  1 
ATOM   832  N  N   . GLY   A 1 105 ? 16.293 7.114   20.043 1.00 25.81  ? 111 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 105 ? 17.491 6.435   19.567 1.00 25.83  ? 111 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 105 ? 17.320 4.937   19.417 1.00 25.80  ? 111 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 105 ? 18.112 4.311   18.710 1.00 25.94  ? 111 GLY   A O   1 
ATOM   836  N  N   . GLY   A 1 106 ? 16.279 4.356   20.065 1.00 24.70  ? 112 GLY   A N   1 
ATOM   837  C  CA  . GLY   A 1 106 ? 15.965 2.939   19.951 1.00 23.95  ? 112 GLY   A CA  1 
ATOM   838  C  C   . GLY   A 1 106 ? 15.684 2.561   18.505 1.00 24.03  ? 112 GLY   A C   1 
ATOM   839  O  O   . GLY   A 1 106 ? 14.948 3.268   17.810 1.00 24.23  ? 112 GLY   A O   1 
ATOM   840  N  N   . ILE   A 1 107 ? 16.276 1.468   18.032 1.00 22.78  ? 113 ILE   A N   1 
ATOM   841  C  CA  . ILE   A 1 107 ? 16.096 1.051   16.645 1.00 23.53  ? 113 ILE   A CA  1 
ATOM   842  C  C   . ILE   A 1 107 ? 14.755 0.374   16.394 1.00 22.43  ? 113 ILE   A C   1 
ATOM   843  O  O   . ILE   A 1 107 ? 14.305 -0.422  17.219 1.00 22.40  ? 113 ILE   A O   1 
ATOM   844  C  CB  . ILE   A 1 107 ? 17.318 0.175   16.222 1.00 25.16  ? 113 ILE   A CB  1 
ATOM   845  C  CG1 . ILE   A 1 107 ? 18.499 1.106   15.840 1.00 27.14  ? 113 ILE   A CG1 1 
ATOM   846  C  CG2 . ILE   A 1 107 ? 16.995 -0.773  15.047 1.00 25.60  ? 113 ILE   A CG2 1 
ATOM   847  C  CD1 . ILE   A 1 107 ? 19.780 0.397   15.530 1.00 28.62  ? 113 ILE   A CD1 1 
ATOM   848  N  N   . LEU   A 1 108 ? 14.131 0.686   15.252 1.00 21.44  ? 114 LEU   A N   1 
ATOM   849  C  CA  . LEU   A 1 108 ? 12.943 -0.003  14.768 1.00 21.78  ? 114 LEU   A CA  1 
ATOM   850  C  C   . LEU   A 1 108 ? 13.456 -0.847  13.549 1.00 22.42  ? 114 LEU   A C   1 
ATOM   851  O  O   . LEU   A 1 108 ? 14.033 -0.279  12.619 1.00 21.38  ? 114 LEU   A O   1 
ATOM   852  C  CB  . LEU   A 1 108 ? 11.867 0.986   14.292 1.00 21.42  ? 114 LEU   A CB  1 
ATOM   853  C  CG  . LEU   A 1 108 ? 10.716 0.360   13.482 1.00 22.05  ? 114 LEU   A CG  1 
ATOM   854  C  CD1 . LEU   A 1 108 ? 9.903  -0.678  14.352 1.00 22.35  ? 114 LEU   A CD1 1 
ATOM   855  C  CD2 . LEU   A 1 108 ? 9.799  1.457   12.903 1.00 23.31  ? 114 LEU   A CD2 1 
ATOM   856  N  N   . ARG   A 1 109 ? 13.226 -2.173  13.557 1.00 22.82  ? 115 ARG   A N   1 
ATOM   857  C  CA  . ARG   A 1 109 ? 13.697 -3.034  12.457 1.00 24.71  ? 115 ARG   A CA  1 
ATOM   858  C  C   . ARG   A 1 109 ? 12.589 -3.910  11.884 1.00 24.67  ? 115 ARG   A C   1 
ATOM   859  O  O   . ARG   A 1 109 ? 11.692 -4.299  12.602 1.00 24.64  ? 115 ARG   A O   1 
ATOM   860  C  CB  . ARG   A 1 109 ? 14.891 -3.902  12.929 1.00 27.82  ? 115 ARG   A CB  1 
ATOM   861  C  CG  . ARG   A 1 109 ? 14.572 -4.835  14.119 1.00 36.81  ? 115 ARG   A CG  1 
ATOM   862  C  CD  . ARG   A 1 109 ? 15.720 -5.789  14.490 1.00 44.57  ? 115 ARG   A CD  1 
ATOM   863  N  NE  . ARG   A 1 109 ? 16.977 -5.075  14.745 1.00 51.41  ? 115 ARG   A NE  1 
ATOM   864  C  CZ  . ARG   A 1 109 ? 17.487 -4.847  15.952 1.00 55.80  ? 115 ARG   A CZ  1 
ATOM   865  N  NH1 . ARG   A 1 109 ? 16.876 -5.307  17.034 1.00 56.60  ? 115 ARG   A NH1 1 
ATOM   866  N  NH2 . ARG   A 1 109 ? 18.622 -4.168  16.085 1.00 56.58  ? 115 ARG   A NH2 1 
ATOM   867  N  N   . CYS   A 1 110 ? 12.653 -4.214  10.586 1.00 25.08  ? 116 CYS   A N   1 
ATOM   868  C  CA  . CYS   A 1 110 ? 11.733 -5.129  9.931  1.00 25.68  ? 116 CYS   A CA  1 
ATOM   869  C  C   . CYS   A 1 110 ? 12.628 -6.285  9.364  1.00 26.47  ? 116 CYS   A C   1 
ATOM   870  O  O   . CYS   A 1 110 ? 13.850 -6.267  9.544  1.00 26.04  ? 116 CYS   A O   1 
ATOM   871  C  CB  . CYS   A 1 110 ? 11.003 -4.387  8.814  1.00 25.71  ? 116 CYS   A CB  1 
ATOM   872  S  SG  . CYS   A 1 110 ? 12.106 -3.846  7.476  1.00 25.93  ? 116 CYS   A SG  1 
ATOM   873  N  N   . GLN   A 1 111 ? 12.056 -7.224  8.614  1.00 28.05  ? 117 GLN   A N   1 
ATOM   874  C  CA  . GLN   A 1 111 ? 12.862 -8.299  7.989  1.00 29.72  ? 117 GLN   A CA  1 
ATOM   875  C  C   . GLN   A 1 111 ? 13.963 -7.768  7.076  1.00 30.02  ? 117 GLN   A C   1 
ATOM   876  O  O   . GLN   A 1 111 ? 14.968 -8.460  6.888  1.00 31.98  ? 117 GLN   A O   1 
ATOM   877  C  CB  . GLN   A 1 111 ? 11.956 -9.263  7.211  1.00 32.26  ? 117 GLN   A CB  1 
ATOM   878  C  CG  . GLN   A 1 111 ? 11.366 -8.683  5.955  1.00 36.11  ? 117 GLN   A CG  1 
ATOM   879  C  CD  . GLN   A 1 111 ? 10.431 -9.652  5.315  1.00 43.49  ? 117 GLN   A CD  1 
ATOM   880  O  OE1 . GLN   A 1 111 ? 9.205  -9.550  5.459  1.00 46.45  ? 117 GLN   A OE1 1 
ATOM   881  N  NE2 . GLN   A 1 111 ? 10.999 -10.618 4.596  1.00 44.03  ? 117 GLN   A NE2 1 
ATOM   882  N  N   . HIS   A 1 112 ? 13.802 -6.550  6.505  1.00 28.73  ? 118 HIS   A N   1 
ATOM   883  C  CA  . HIS   A 1 112 ? 14.765 -5.981  5.554  1.00 28.72  ? 118 HIS   A CA  1 
ATOM   884  C  C   . HIS   A 1 112 ? 15.952 -5.227  6.176  1.00 28.87  ? 118 HIS   A C   1 
ATOM   885  O  O   . HIS   A 1 112 ? 16.928 -4.946  5.467  1.00 29.91  ? 118 HIS   A O   1 
ATOM   886  C  CB  . HIS   A 1 112 ? 14.048 -5.078  4.541  1.00 28.37  ? 118 HIS   A CB  1 
ATOM   887  C  CG  . HIS   A 1 112 ? 12.982 -5.800  3.786  1.00 28.75  ? 118 HIS   A CG  1 
ATOM   888  N  ND1 . HIS   A 1 112 ? 11.646 -5.644  4.102  1.00 29.27  ? 118 HIS   A ND1 1 
ATOM   889  C  CD2 . HIS   A 1 112 ? 13.094 -6.697  2.774  1.00 29.43  ? 118 HIS   A CD2 1 
ATOM   890  C  CE1 . HIS   A 1 112 ? 10.981 -6.444  3.284  1.00 29.60  ? 118 HIS   A CE1 1 
ATOM   891  N  NE2 . HIS   A 1 112 ? 11.811 -7.113  2.475  1.00 30.17  ? 118 HIS   A NE2 1 
ATOM   892  N  N   . GLY   A 1 113 ? 15.840 -4.871  7.455  1.00 27.13  ? 119 GLY   A N   1 
ATOM   893  C  CA  . GLY   A 1 113 ? 16.885 -4.150  8.167  1.00 26.07  ? 119 GLY   A CA  1 
ATOM   894  C  C   . GLY   A 1 113 ? 16.347 -3.028  9.038  1.00 24.84  ? 119 GLY   A C   1 
ATOM   895  O  O   . GLY   A 1 113 ? 15.206 -3.084  9.490  1.00 23.64  ? 119 GLY   A O   1 
ATOM   896  N  N   . VAL   A 1 114 ? 17.139 -1.966  9.212  1.00 24.48  ? 120 VAL   A N   1 
ATOM   897  C  CA  . VAL   A 1 114 ? 16.754 -0.809  10.035 1.00 23.90  ? 120 VAL   A CA  1 
ATOM   898  C  C   . VAL   A 1 114 ? 15.786 0.079   9.308  1.00 23.24  ? 120 VAL   A C   1 
ATOM   899  O  O   . VAL   A 1 114 ? 16.055 0.507   8.190  1.00 24.50  ? 120 VAL   A O   1 
ATOM   900  C  CB  . VAL   A 1 114 ? 17.994 0.005   10.512 1.00 24.39  ? 120 VAL   A CB  1 
ATOM   901  C  CG1 . VAL   A 1 114 ? 17.559 1.265   11.278 1.00 25.33  ? 120 VAL   A CG1 1 
ATOM   902  C  CG2 . VAL   A 1 114 ? 18.913 -0.867  11.374 1.00 25.00  ? 120 VAL   A CG2 1 
ATOM   903  N  N   . VAL   A 1 115 ? 14.650 0.383   9.952  1.00 22.47  ? 121 VAL   A N   1 
ATOM   904  C  CA  . VAL   A 1 115 ? 13.601 1.229   9.388  1.00 21.96  ? 121 VAL   A CA  1 
ATOM   905  C  C   . VAL   A 1 115 ? 13.781 2.682   9.877  1.00 22.33  ? 121 VAL   A C   1 
ATOM   906  O  O   . VAL   A 1 115 ? 13.617 3.637   9.118  1.00 22.23  ? 121 VAL   A O   1 
ATOM   907  C  CB  . VAL   A 1 115 ? 12.214 0.666   9.813  1.00 22.28  ? 121 VAL   A CB  1 
ATOM   908  C  CG1 . VAL   A 1 115 ? 11.081 1.624   9.422  1.00 22.50  ? 121 VAL   A CG1 1 
ATOM   909  C  CG2 . VAL   A 1 115 ? 11.986 -0.729  9.230  1.00 22.30  ? 121 VAL   A CG2 1 
ATOM   910  N  N   . GLY   A 1 116 ? 14.061 2.840   11.162 1.00 22.78  ? 122 GLY   A N   1 
ATOM   911  C  CA  . GLY   A 1 116 ? 14.238 4.157   11.756 1.00 23.31  ? 122 GLY   A CA  1 
ATOM   912  C  C   . GLY   A 1 116 ? 14.554 4.084   13.239 1.00 23.04  ? 122 GLY   A C   1 
ATOM   913  O  O   . GLY   A 1 116 ? 14.914 3.008   13.747 1.00 22.95  ? 122 GLY   A O   1 
ATOM   914  N  N   . ILE   A 1 117 ? 14.461 5.227   13.923 1.00 22.59  ? 123 ILE   A N   1 
ATOM   915  C  CA  . ILE   A 1 117 ? 14.780 5.311   15.355 1.00 23.25  ? 123 ILE   A CA  1 
ATOM   916  C  C   . ILE   A 1 117 ? 13.693 6.052   16.106 1.00 23.00  ? 123 ILE   A C   1 
ATOM   917  O  O   . ILE   A 1 117 ? 13.085 6.982   15.571 1.00 23.15  ? 123 ILE   A O   1 
ATOM   918  C  CB  . ILE   A 1 117 ? 16.156 5.995   15.622 1.00 24.56  ? 123 ILE   A CB  1 
ATOM   919  C  CG1 . ILE   A 1 117 ? 16.226 7.387   14.938 1.00 26.51  ? 123 ILE   A CG1 1 
ATOM   920  C  CG2 . ILE   A 1 117 ? 17.338 5.095   15.229 1.00 26.07  ? 123 ILE   A CG2 1 
ATOM   921  C  CD1 . ILE   A 1 117 ? 17.526 8.191   15.221 1.00 29.09  ? 123 ILE   A CD1 1 
ATOM   922  N  N   . VAL   A 1 118 ? 13.477 5.695   17.386 1.00 22.15  ? 124 VAL   A N   1 
ATOM   923  C  CA  . VAL   A 1 118 ? 12.490 6.401   18.224 1.00 22.09  ? 124 VAL   A CA  1 
ATOM   924  C  C   . VAL   A 1 118 ? 12.809 7.899   18.283 1.00 22.20  ? 124 VAL   A C   1 
ATOM   925  O  O   . VAL   A 1 118 ? 13.974 8.277   18.433 1.00 22.01  ? 124 VAL   A O   1 
ATOM   926  C  CB  . VAL   A 1 118 ? 12.441 5.797   19.644 1.00 22.71  ? 124 VAL   A CB  1 
ATOM   927  C  CG1 . VAL   A 1 118 ? 11.547 6.627   20.563 1.00 23.20  ? 124 VAL   A CG1 1 
ATOM   928  C  CG2 . VAL   A 1 118 ? 12.005 4.334   19.609 1.00 23.00  ? 124 VAL   A CG2 1 
ATOM   929  N  N   . SER   A 1 119 ? 11.800 8.733   18.053 1.00 22.44  ? 125 SER   A N   1 
ATOM   930  C  CA  . SER   A 1 119 ? 11.953 10.172  18.044 1.00 23.97  ? 125 SER   A CA  1 
ATOM   931  C  C   . SER   A 1 119 ? 10.901 10.875  18.901 1.00 25.07  ? 125 SER   A C   1 
ATOM   932  O  O   . SER   A 1 119 ? 11.197 11.954  19.400 1.00 25.90  ? 125 SER   A O   1 
ATOM   933  C  CB  . SER   A 1 119 ? 11.917 10.696  16.604 1.00 25.64  ? 125 SER   A CB  1 
ATOM   934  O  OG  . SER   A 1 119 ? 12.026 12.113  16.536 1.00 26.67  ? 125 SER   A OG  1 
ATOM   935  N  N   . THR   A 1 120 ? 9.683  10.284  19.081 1.00 25.39  ? 126 THR   A N   1 
ATOM   936  C  CA  . THR   A 1 120 ? 8.605  10.861  19.925 1.00 25.37  ? 126 THR   A CA  1 
ATOM   937  C  C   . THR   A 1 120 ? 7.991  9.810   20.919 1.00 26.33  ? 126 THR   A C   1 
ATOM   938  O  O   . THR   A 1 120 ? 8.242  8.603   20.804 1.00 26.28  ? 126 THR   A O   1 
ATOM   939  C  CB  . THR   A 1 120 ? 7.499  11.586  19.082 1.00 26.07  ? 126 THR   A CB  1 
ATOM   940  O  OG1 . THR   A 1 120 ? 6.566  10.647  18.538 1.00 27.84  ? 126 THR   A OG1 1 
ATOM   941  C  CG2 . THR   A 1 120 ? 8.038  12.514  17.996 1.00 25.89  ? 126 THR   A CG2 1 
ATOM   942  N  N   . GLY   A 1 121 ? 7.210  10.282  21.893 1.00 26.69  ? 127 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 121 ? 6.546  9.398   22.842 1.00 27.60  ? 127 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 121 ? 5.356  10.049  23.516 1.00 28.67  ? 127 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 121 ? 4.792  11.010  22.983 1.00 28.33  ? 127 GLY   A O   1 
ATOM   946  N  N   . GLY   A 1 122 ? 4.969  9.501   24.676 1.00 29.45  ? 128 GLY   A N   1 
ATOM   947  C  CA  . GLY   A 1 122 ? 3.836  10.000  25.457 1.00 30.82  ? 128 GLY   A CA  1 
ATOM   948  C  C   . GLY   A 1 122 ? 2.494  9.520   24.940 1.00 32.45  ? 128 GLY   A C   1 
ATOM   949  O  O   . GLY   A 1 122 ? 2.404  9.017   23.815 1.00 32.87  ? 128 GLY   A O   1 
ATOM   950  N  N   . ASN   A 1 123 ? 1.439  9.666   25.763 1.00 33.67  ? 129 ASN   A N   1 
ATOM   951  C  CA  . ASN   A 1 123 ? 0.064  9.281   25.426 1.00 34.92  ? 129 ASN   A CA  1 
ATOM   952  C  C   . ASN   A 1 123 ? -0.101 7.828   24.903 1.00 33.86  ? 129 ASN   A C   1 
ATOM   953  O  O   . ASN   A 1 123 ? -1.027 7.556   24.135 1.00 34.35  ? 129 ASN   A O   1 
ATOM   954  C  CB  . ASN   A 1 123 ? -0.513 10.272  24.407 1.00 37.81  ? 129 ASN   A CB  1 
ATOM   955  C  CG  . ASN   A 1 123 ? -0.790 11.649  24.972 1.00 43.87  ? 129 ASN   A CG  1 
ATOM   956  O  OD1 . ASN   A 1 123 ? -0.852 11.855  26.196 1.00 45.51  ? 129 ASN   A OD1 1 
ATOM   957  N  ND2 . ASN   A 1 123 ? -1.020 12.613  24.078 1.00 44.78  ? 129 ASN   A ND2 1 
ATOM   958  N  N   . GLY   A 1 124 ? 0.768  6.917   25.330 1.00 31.96  ? 130 GLY   A N   1 
ATOM   959  C  CA  . GLY   A 1 124 ? 0.710  5.531   24.887 1.00 31.15  ? 130 GLY   A CA  1 
ATOM   960  C  C   . GLY   A 1 124 ? 1.054  5.332   23.418 1.00 29.86  ? 130 GLY   A C   1 
ATOM   961  O  O   . GLY   A 1 124 ? 0.700  4.309   22.830 1.00 30.14  ? 130 GLY   A O   1 
ATOM   962  N  N   . LEU   A 1 125 ? 1.781  6.287   22.832 1.00 28.47  ? 131 LEU   A N   1 
ATOM   963  C  CA  . LEU   A 1 125 ? 2.233  6.221   21.438 1.00 27.89  ? 131 LEU   A CA  1 
ATOM   964  C  C   . LEU   A 1 125 ? 3.755  6.358   21.346 1.00 27.52  ? 131 LEU   A C   1 
ATOM   965  O  O   . LEU   A 1 125 ? 4.382  6.967   22.207 1.00 28.32  ? 131 LEU   A O   1 
ATOM   966  C  CB  . LEU   A 1 125 ? 1.611  7.360   20.626 1.00 28.18  ? 131 LEU   A CB  1 
ATOM   967  C  CG  . LEU   A 1 125 ? 0.090  7.314   20.485 1.00 29.97  ? 131 LEU   A CG  1 
ATOM   968  C  CD1 . LEU   A 1 125 ? -0.449 8.702   20.223 1.00 31.26  ? 131 LEU   A CD1 1 
ATOM   969  C  CD2 . LEU   A 1 125 ? -0.331 6.337   19.363 1.00 30.31  ? 131 LEU   A CD2 1 
ATOM   970  N  N   . VAL   A 1 126 ? 4.342  5.807   20.285 1.00 25.80  ? 132 VAL   A N   1 
ATOM   971  C  CA  . VAL   A 1 126 ? 5.759  5.955   20.026 1.00 25.52  ? 132 VAL   A CA  1 
ATOM   972  C  C   . VAL   A 1 126 ? 5.899  6.393   18.557 1.00 24.05  ? 132 VAL   A C   1 
ATOM   973  O  O   . VAL   A 1 126 ? 5.270  5.816   17.673 1.00 23.92  ? 132 VAL   A O   1 
ATOM   974  C  CB  . VAL   A 1 126 ? 6.566  4.662   20.337 1.00 26.48  ? 132 VAL   A CB  1 
ATOM   975  C  CG1 . VAL   A 1 126 ? 5.930  3.429   19.713 1.00 28.82  ? 132 VAL   A CG1 1 
ATOM   976  C  CG2 . VAL   A 1 126 ? 8.038  4.789   19.946 1.00 25.51  ? 132 VAL   A CG2 1 
ATOM   977  N  N   . GLY   A 1 127 ? 6.708  7.405   18.319 1.00 23.21  ? 133 GLY   A N   1 
ATOM   978  C  CA  . GLY   A 1 127 ? 6.966  7.886   16.970 1.00 23.43  ? 133 GLY   A CA  1 
ATOM   979  C  C   . GLY   A 1 127 ? 8.397  7.572   16.574 1.00 23.51  ? 133 GLY   A C   1 
ATOM   980  O  O   . GLY   A 1 127 ? 9.297  7.688   17.402 1.00 23.04  ? 133 GLY   A O   1 
ATOM   981  N  N   . PHE   A 1 128 ? 8.614  7.177   15.300 1.00 22.41  ? 134 PHE   A N   1 
ATOM   982  C  CA  . PHE   A 1 128 ? 9.922  6.789   14.782 1.00 21.78  ? 134 PHE   A CA  1 
ATOM   983  C  C   . PHE   A 1 128 ? 10.283 7.668   13.582 1.00 21.98  ? 134 PHE   A C   1 
ATOM   984  O  O   . PHE   A 1 128 ? 9.465  7.851   12.684 1.00 21.15  ? 134 PHE   A O   1 
ATOM   985  C  CB  . PHE   A 1 128 ? 9.893  5.324   14.302 1.00 21.59  ? 134 PHE   A CB  1 
ATOM   986  C  CG  . PHE   A 1 128 ? 9.349  4.323   15.304 1.00 21.97  ? 134 PHE   A CG  1 
ATOM   987  C  CD1 . PHE   A 1 128 ? 10.175 3.753   16.255 1.00 22.24  ? 134 PHE   A CD1 1 
ATOM   988  C  CD2 . PHE   A 1 128 ? 8.020  3.930   15.265 1.00 22.56  ? 134 PHE   A CD2 1 
ATOM   989  C  CE1 . PHE   A 1 128 ? 9.684  2.824   17.163 1.00 22.50  ? 134 PHE   A CE1 1 
ATOM   990  C  CE2 . PHE   A 1 128 ? 7.524  3.000   16.183 1.00 23.66  ? 134 PHE   A CE2 1 
ATOM   991  C  CZ  . PHE   A 1 128 ? 8.364  2.449   17.126 1.00 23.26  ? 134 PHE   A CZ  1 
ATOM   992  N  N   . ALA   A 1 129 ? 11.501 8.213   13.579 1.00 21.73  ? 135 ALA   A N   1 
ATOM   993  C  CA  . ALA   A 1 129 ? 11.995 8.996   12.462 1.00 22.45  ? 135 ALA   A CA  1 
ATOM   994  C  C   . ALA   A 1 129 ? 12.418 7.976   11.386 1.00 23.45  ? 135 ALA   A C   1 
ATOM   995  O  O   . ALA   A 1 129 ? 13.376 7.232   11.610 1.00 23.72  ? 135 ALA   A O   1 
ATOM   996  C  CB  . ALA   A 1 129 ? 13.228 9.805   12.894 1.00 23.33  ? 135 ALA   A CB  1 
ATOM   997  N  N   . ASP   A 1 130 ? 11.735 7.951   10.231 1.00 23.34  ? 136 ASP   A N   1 
ATOM   998  C  CA  . ASP   A 1 130 ? 12.080 7.030   9.126  1.00 24.80  ? 136 ASP   A CA  1 
ATOM   999  C  C   . ASP   A 1 130 ? 13.431 7.385   8.483  1.00 25.24  ? 136 ASP   A C   1 
ATOM   1000 O  O   . ASP   A 1 130 ? 13.737 8.571   8.310  1.00 25.39  ? 136 ASP   A O   1 
ATOM   1001 C  CB  . ASP   A 1 130 ? 11.013 7.098   8.024  1.00 25.41  ? 136 ASP   A CB  1 
ATOM   1002 C  CG  . ASP   A 1 130 ? 11.164 6.049   6.932  1.00 28.34  ? 136 ASP   A CG  1 
ATOM   1003 O  OD1 . ASP   A 1 130 ? 11.181 4.854   7.256  1.00 28.73  ? 136 ASP   A OD1 1 
ATOM   1004 O  OD2 . ASP   A 1 130 ? 11.275 6.428   5.755  1.00 30.69  ? 136 ASP   A OD2 1 
ATOM   1005 N  N   . VAL   A 1 131 ? 14.238 6.361   8.114  1.00 24.60  ? 137 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 131 ? 15.511 6.595   7.409  1.00 25.11  ? 137 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 131 ? 15.550 5.831   6.042  1.00 25.50  ? 137 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 131 ? 16.572 5.876   5.363  1.00 25.05  ? 137 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 131 ? 16.746 6.199   8.270  1.00 25.10  ? 137 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 131 ? 16.786 6.962   9.599  1.00 25.51  ? 137 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 131 ? 16.825 4.699   8.497  1.00 24.88  ? 137 VAL   A CG2 1 
ATOM   1012 N  N   . ARG   A 1 132 ? 14.472 5.084   5.680  1.00 25.01  ? 138 ARG   A N   1 
ATOM   1013 C  CA  . ARG   A 1 132 ? 14.421 4.249   4.459  1.00 25.65  ? 138 ARG   A CA  1 
ATOM   1014 C  C   . ARG   A 1 132 ? 14.509 5.034   3.151  1.00 26.85  ? 138 ARG   A C   1 
ATOM   1015 O  O   . ARG   A 1 132 ? 14.869 4.455   2.128  1.00 27.42  ? 138 ARG   A O   1 
ATOM   1016 C  CB  . ARG   A 1 132 ? 13.164 3.378   4.449  1.00 24.57  ? 138 ARG   A CB  1 
ATOM   1017 C  CG  . ARG   A 1 132 ? 13.122 2.326   5.570  1.00 24.53  ? 138 ARG   A CG  1 
ATOM   1018 C  CD  . ARG   A 1 132 ? 11.805 1.527   5.487  1.00 23.52  ? 138 ARG   A CD  1 
ATOM   1019 N  NE  . ARG   A 1 132 ? 10.681 2.357   5.909  1.00 24.75  ? 138 ARG   A NE  1 
ATOM   1020 C  CZ  . ARG   A 1 132 ? 9.421  1.926   6.020  1.00 24.50  ? 138 ARG   A CZ  1 
ATOM   1021 N  NH1 . ARG   A 1 132 ? 9.102  0.682   5.669  1.00 20.65  ? 138 ARG   A NH1 1 
ATOM   1022 N  NH2 . ARG   A 1 132 ? 8.479  2.728   6.511  1.00 23.46  ? 138 ARG   A NH2 1 
ATOM   1023 N  N   . ASP   A 1 133 ? 14.194 6.325   3.164  1.00 27.61  ? 139 ASP   A N   1 
ATOM   1024 C  CA  . ASP   A 1 133 ? 14.322 7.147   1.943  1.00 28.91  ? 139 ASP   A CA  1 
ATOM   1025 C  C   . ASP   A 1 133 ? 15.747 7.689   1.731  1.00 29.20  ? 139 ASP   A C   1 
ATOM   1026 O  O   . ASP   A 1 133 ? 16.040 8.212   0.658  1.00 30.05  ? 139 ASP   A O   1 
ATOM   1027 C  CB  . ASP   A 1 133 ? 13.329 8.316   1.979  1.00 31.11  ? 139 ASP   A CB  1 
ATOM   1028 C  CG  . ASP   A 1 133 ? 13.620 9.342   3.076  1.00 33.55  ? 139 ASP   A CG  1 
ATOM   1029 O  OD1 . ASP   A 1 133 ? 13.963 8.925   4.206  1.00 32.60  ? 139 ASP   A OD1 1 
ATOM   1030 O  OD2 . ASP   A 1 133 ? 13.492 10.548  2.805  1.00 35.42  ? 139 ASP   A OD2 1 
ATOM   1031 N  N   . LEU   A 1 134 ? 16.613 7.608   2.748  1.00 28.88  ? 140 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 134 ? 17.978 8.145   2.691  1.00 29.66  ? 140 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 134 ? 18.891 7.147   2.001  1.00 31.39  ? 140 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 134 ? 19.730 6.506   2.640  1.00 31.32  ? 140 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 134 ? 18.483 8.462   4.111  1.00 29.97  ? 140 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 134 ? 17.583 9.389   4.928  1.00 30.74  ? 140 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 134 ? 18.080 9.508   6.350  1.00 31.58  ? 140 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 134 ? 17.505 10.773  4.285  1.00 31.75  ? 140 LEU   A CD2 1 
ATOM   1039 N  N   . LEU   A 1 135 ? 18.715 7.008   0.673  1.00 32.20  ? 141 LEU   A N   1 
ATOM   1040 C  CA  . LEU   A 1 135 ? 19.452 6.030   -0.108 1.00 33.77  ? 141 LEU   A CA  1 
ATOM   1041 C  C   . LEU   A 1 135 ? 20.960 6.243   -0.086 1.00 34.92  ? 141 LEU   A C   1 
ATOM   1042 O  O   . LEU   A 1 135 ? 21.722 5.271   -0.198 1.00 34.80  ? 141 LEU   A O   1 
ATOM   1043 C  CB  . LEU   A 1 135 ? 18.929 5.953   -1.567 1.00 34.60  ? 141 LEU   A CB  1 
ATOM   1044 C  CG  . LEU   A 1 135 ? 17.410 5.819   -1.774 1.00 36.83  ? 141 LEU   A CG  1 
ATOM   1045 C  CD1 . LEU   A 1 135 ? 17.096 5.430   -3.187 1.00 37.98  ? 141 LEU   A CD1 1 
ATOM   1046 C  CD2 . LEU   A 1 135 ? 16.770 4.796   -0.846 1.00 37.75  ? 141 LEU   A CD2 1 
ATOM   1047 N  N   . TRP   A 1 136 ? 21.384 7.508   0.077  1.00 35.47  ? 142 TRP   A N   1 
ATOM   1048 C  CA  . TRP   A 1 136 ? 22.798 7.868   0.114  1.00 36.05  ? 142 TRP   A CA  1 
ATOM   1049 C  C   . TRP   A 1 136 ? 23.536 7.221   1.283  1.00 36.34  ? 142 TRP   A C   1 
ATOM   1050 O  O   . TRP   A 1 136 ? 24.748 7.092   1.209  1.00 36.94  ? 142 TRP   A O   1 
ATOM   1051 C  CB  . TRP   A 1 136 ? 22.989 9.401   0.086  1.00 35.88  ? 142 TRP   A CB  1 
ATOM   1052 C  CG  . TRP   A 1 136 ? 22.296 10.150  1.195  1.00 35.85  ? 142 TRP   A CG  1 
ATOM   1053 C  CD1 . TRP   A 1 136 ? 21.070 10.744  1.146  1.00 35.94  ? 142 TRP   A CD1 1 
ATOM   1054 C  CD2 . TRP   A 1 136 ? 22.805 10.387  2.518  1.00 35.73  ? 142 TRP   A CD2 1 
ATOM   1055 N  NE1 . TRP   A 1 136 ? 20.788 11.345  2.353  1.00 36.28  ? 142 TRP   A NE1 1 
ATOM   1056 C  CE2 . TRP   A 1 136 ? 21.837 11.142  3.211  1.00 35.86  ? 142 TRP   A CE2 1 
ATOM   1057 C  CE3 . TRP   A 1 136 ? 24.009 10.079  3.167  1.00 36.04  ? 142 TRP   A CE3 1 
ATOM   1058 C  CZ2 . TRP   A 1 136 ? 22.040 11.599  4.508  1.00 35.85  ? 142 TRP   A CZ2 1 
ATOM   1059 C  CZ3 . TRP   A 1 136 ? 24.193 10.512  4.464  1.00 36.15  ? 142 TRP   A CZ3 1 
ATOM   1060 C  CH2 . TRP   A 1 136 ? 23.219 11.266  5.118  1.00 35.81  ? 142 TRP   A CH2 1 
ATOM   1061 N  N   . LEU   A 1 137 ? 22.815 6.751   2.332  1.00 35.96  ? 143 LEU   A N   1 
ATOM   1062 C  CA  . LEU   A 1 137 ? 23.440 6.075   3.458  1.00 37.51  ? 143 LEU   A CA  1 
ATOM   1063 C  C   . LEU   A 1 137 ? 24.203 4.804   3.045  1.00 40.31  ? 143 LEU   A C   1 
ATOM   1064 O  O   . LEU   A 1 137 ? 25.129 4.409   3.749  1.00 40.01  ? 143 LEU   A O   1 
ATOM   1065 C  CB  . LEU   A 1 137 ? 22.403 5.729   4.533  1.00 36.67  ? 143 LEU   A CB  1 
ATOM   1066 C  CG  . LEU   A 1 137 ? 21.960 6.891   5.415  1.00 37.89  ? 143 LEU   A CG  1 
ATOM   1067 C  CD1 . LEU   A 1 137 ? 20.837 6.465   6.381  1.00 37.95  ? 143 LEU   A CD1 1 
ATOM   1068 C  CD2 . LEU   A 1 137 ? 23.143 7.489   6.189  1.00 38.37  ? 143 LEU   A CD2 1 
ATOM   1069 N  N   . ASP   A 1 138 ? 23.796 4.172   1.919  1.00 42.84  ? 144 ASP   A N   1 
ATOM   1070 C  CA  . ASP   A 1 138 ? 24.385 2.949   1.366  1.00 46.36  ? 144 ASP   A CA  1 
ATOM   1071 C  C   . ASP   A 1 138 ? 25.568 3.200   0.437  1.00 49.68  ? 144 ASP   A C   1 
ATOM   1072 O  O   . ASP   A 1 138 ? 26.000 2.242   -0.205 1.00 50.10  ? 144 ASP   A O   1 
ATOM   1073 C  CB  . ASP   A 1 138 ? 23.351 2.190   0.521  1.00 47.86  ? 144 ASP   A CB  1 
ATOM   1074 C  CG  . ASP   A 1 138 ? 22.112 1.745   1.244  1.00 52.12  ? 144 ASP   A CG  1 
ATOM   1075 O  OD1 . ASP   A 1 138 ? 22.150 1.666   2.489  1.00 53.13  ? 144 ASP   A OD1 1 
ATOM   1076 O  OD2 . ASP   A 1 138 ? 21.092 1.484   0.564  1.00 53.81  ? 144 ASP   A OD2 1 
ATOM   1077 N  N   . GLU   A 1 139 ? 26.058 4.448   0.302  1.00 52.26  ? 145 GLU   A N   1 
ATOM   1078 C  CA  . GLU   A 1 139 ? 27.150 4.715   -0.640 1.00 55.71  ? 145 GLU   A CA  1 
ATOM   1079 C  C   . GLU   A 1 139 ? 27.990 5.955   -0.316 1.00 58.55  ? 145 GLU   A C   1 
ATOM   1080 O  O   . GLU   A 1 139 ? 27.551 6.816   0.456  1.00 59.44  ? 145 GLU   A O   1 
ATOM   1081 C  CB  . GLU   A 1 139 ? 26.581 4.825   -2.070 1.00 58.85  ? 145 GLU   A CB  1 
ATOM   1082 C  CG  . GLU   A 1 139 ? 25.649 6.011   -2.249 1.00 65.58  ? 145 GLU   A CG  1 
ATOM   1083 C  CD  . GLU   A 1 139 ? 24.522 5.773   -3.234 1.00 75.50  ? 145 GLU   A CD  1 
ATOM   1084 O  OE1 . GLU   A 1 139 ? 24.321 6.632   -4.125 1.00 77.72  ? 145 GLU   A OE1 1 
ATOM   1085 O  OE2 . GLU   A 1 139 ? 23.840 4.728   -3.118 1.00 78.50  ? 145 GLU   A OE2 1 
ATOM   1086 N  N   . GLU   A 1 140 ? 29.193 6.048   -0.934 1.00 60.05  ? 146 GLU   A N   1 
ATOM   1087 C  CA  . GLU   A 1 140 ? 30.124 7.178   -0.812 1.00 62.13  ? 146 GLU   A CA  1 
ATOM   1088 C  C   . GLU   A 1 140 ? 30.498 7.483   0.656  1.00 63.37  ? 146 GLU   A C   1 
ATOM   1089 O  O   . GLU   A 1 140 ? 31.420 6.873   1.197  1.00 64.10  ? 146 GLU   A O   1 
ATOM   1090 C  CB  . GLU   A 1 140 ? 29.565 8.416   -1.570 1.00 65.06  ? 146 GLU   A CB  1 
ATOM   1091 C  CG  . GLU   A 1 140 ? 29.464 9.729   -0.799 1.00 70.49  ? 146 GLU   A CG  1 
ATOM   1092 C  CD  . GLU   A 1 140 ? 30.699 10.607  -0.860 1.00 76.96  ? 146 GLU   A CD  1 
ATOM   1093 O  OE1 . GLU   A 1 140 ? 30.757 11.598  -0.095 1.00 78.37  ? 146 GLU   A OE1 1 
ATOM   1094 O  OE2 . GLU   A 1 140 ? 31.607 10.311  -1.672 1.00 78.41  ? 146 GLU   A OE2 1 
HETATM 1095 N  N1  . A1BPF B 2 .   ? 9.515  14.624  22.509 1.00 30.62  ? 201 A1BPF A N1  1 
HETATM 1096 C  C4  . A1BPF B 2 .   ? 10.659 15.089  23.315 1.00 30.62  ? 201 A1BPF A C4  1 
HETATM 1097 C  C5  . A1BPF B 2 .   ? 8.558  13.760  22.916 1.00 31.46  ? 201 A1BPF A C5  1 
HETATM 1098 C  C6  . A1BPF B 2 .   ? 8.418  13.362  24.407 1.00 33.28  ? 201 A1BPF A C6  1 
HETATM 1099 C  C7  . A1BPF B 2 .   ? 9.125  12.027  24.540 1.00 34.84  ? 201 A1BPF A C7  1 
HETATM 1100 C  C8  . A1BPF B 2 .   ? 8.533  10.876  25.171 1.00 35.45  ? 201 A1BPF A C8  1 
HETATM 1101 C  C10 . A1BPF B 2 .   ? 10.311 11.578  24.004 1.00 36.16  ? 201 A1BPF A C10 1 
HETATM 1102 C  C13 . A1BPF B 2 .   ? 8.750  14.377  25.544 1.00 33.41  ? 201 A1BPF A C13 1 
HETATM 1103 O  O1  . A1BPF B 2 .   ? 7.728  13.301  22.151 1.00 30.63  ? 201 A1BPF A O1  1 
HETATM 1104 C  C3  . A1BPF B 2 .   ? 11.977 15.049  22.550 1.00 30.51  ? 201 A1BPF A C3  1 
HETATM 1105 C  C2  . A1BPF B 2 .   ? 11.831 15.698  21.174 1.00 30.70  ? 201 A1BPF A C2  1 
HETATM 1106 C  C14 . A1BPF B 2 .   ? 9.403  15.246  21.185 1.00 30.47  ? 201 A1BPF A C14 1 
HETATM 1107 C  C1  . A1BPF B 2 .   ? 10.694 15.034  20.387 1.00 30.65  ? 201 A1BPF A C1  1 
HETATM 1108 C  C   . A1BPF B 2 .   ? 10.644 15.540  18.956 1.00 30.28  ? 201 A1BPF A C   1 
HETATM 1109 O  O   . A1BPF B 2 .   ? 10.185 16.654  18.690 1.00 30.74  ? 201 A1BPF A O   1 
HETATM 1110 N  N   . A1BPF B 2 .   ? 11.119 14.712  18.033 1.00 29.17  ? 201 A1BPF A N   1 
HETATM 1111 C  C12 . A1BPF B 2 .   ? 7.400  14.065  26.204 1.00 33.79  ? 201 A1BPF A C12 1 
HETATM 1112 C  C11 . A1BPF B 2 .   ? 6.948  13.345  24.926 1.00 33.62  ? 201 A1BPF A C11 1 
HETATM 1113 O  O2  . A1BPF B 2 .   ? 10.465 10.239  24.231 1.00 36.50  ? 201 A1BPF A O2  1 
HETATM 1114 C  C9  . A1BPF B 2 .   ? 9.355  9.843   24.949 1.00 35.58  ? 201 A1BPF A C9  1 
HETATM 1115 ZN ZN  . ZN    C 3 .   ? 10.899 -4.077  5.444  1.00 25.56  2 202 ZN    A ZN  1 
HETATM 1116 S  S   . DMS   D 4 .   ? 18.843 -7.468  7.195  1.00 97.59  ? 203 DMS   A S   1 
HETATM 1117 O  O   . DMS   D 4 .   ? 19.901 -7.399  6.132  1.00 97.57  ? 203 DMS   A O   1 
HETATM 1118 C  C1  . DMS   D 4 .   ? 18.369 -9.211  7.386  1.00 97.58  ? 203 DMS   A C1  1 
HETATM 1119 C  C2  . DMS   D 4 .   ? 19.661 -7.334  8.802  1.00 97.52  ? 203 DMS   A C2  1 
HETATM 1120 S  S   . DMS   E 4 .   ? 14.824 21.511  7.978  1.00 90.25  ? 204 DMS   A S   1 
HETATM 1121 O  O   . DMS   E 4 .   ? 14.467 22.243  9.240  1.00 90.22  ? 204 DMS   A O   1 
HETATM 1122 C  C1  . DMS   E 4 .   ? 13.443 21.683  6.814  1.00 90.18  ? 204 DMS   A C1  1 
HETATM 1123 C  C2  . DMS   E 4 .   ? 16.010 22.526  7.055  1.00 90.31  ? 204 DMS   A C2  1 
HETATM 1124 S  S   . DMS   F 4 .   ? 20.802 -2.696  23.230 1.00 116.92 ? 205 DMS   A S   1 
HETATM 1125 O  O   . DMS   F 4 .   ? 20.784 -1.490  24.122 1.00 116.87 ? 205 DMS   A O   1 
HETATM 1126 C  C1  . DMS   F 4 .   ? 22.313 -3.624  23.619 1.00 116.97 ? 205 DMS   A C1  1 
HETATM 1127 C  C2  . DMS   F 4 .   ? 19.670 -3.915  23.944 1.00 116.89 ? 205 DMS   A C2  1 
HETATM 1128 S  S   . DMS   G 4 .   ? 0.492  -1.791  23.706 1.00 105.96 ? 206 DMS   A S   1 
HETATM 1129 O  O   . DMS   G 4 .   ? 0.614  -0.547  24.538 1.00 105.95 ? 206 DMS   A O   1 
HETATM 1130 C  C1  . DMS   G 4 .   ? 0.757  -3.207  24.808 1.00 105.95 ? 206 DMS   A C1  1 
HETATM 1131 C  C2  . DMS   G 4 .   ? -1.275 -2.110  23.421 1.00 105.88 ? 206 DMS   A C2  1 
HETATM 1132 O  O   . HOH   H 5 .   ? 6.135  3.301   3.178  1.00 46.14  ? 301 HOH   A O   1 
HETATM 1133 O  O   . HOH   H 5 .   ? 25.858 -1.957  6.289  1.00 52.79  ? 302 HOH   A O   1 
HETATM 1134 O  O   . HOH   H 5 .   ? 4.595  8.177   3.423  1.00 55.50  ? 303 HOH   A O   1 
HETATM 1135 O  O   . HOH   H 5 .   ? 19.728 9.229   19.054 1.00 26.61  ? 304 HOH   A O   1 
HETATM 1136 O  O   . HOH   H 5 .   ? 20.683 -7.608  3.701  1.00 70.38  ? 305 HOH   A O   1 
HETATM 1137 O  O   . HOH   H 5 .   ? 11.867 -4.948  32.000 1.00 66.88  ? 306 HOH   A O   1 
HETATM 1138 O  O   . HOH   H 5 .   ? 0.148  12.732  21.764 1.00 49.16  ? 307 HOH   A O   1 
HETATM 1139 O  O   . HOH   H 5 .   ? 2.668  22.408  22.417 1.00 44.19  ? 308 HOH   A O   1 
HETATM 1140 O  O   . HOH   H 5 .   ? 22.281 -0.367  4.105  1.00 33.11  ? 309 HOH   A O   1 
HETATM 1141 O  O   . HOH   H 5 .   ? 4.009  -4.631  21.208 1.00 38.21  ? 310 HOH   A O   1 
HETATM 1142 O  O   . HOH   H 5 .   ? 34.506 18.673  10.585 1.00 51.26  ? 311 HOH   A O   1 
HETATM 1143 O  O   . HOH   H 5 .   ? 11.617 9.210   31.279 1.00 41.63  ? 312 HOH   A O   1 
HETATM 1144 O  O   . HOH   H 5 .   ? 36.322 17.368  13.306 1.00 48.82  ? 313 HOH   A O   1 
HETATM 1145 O  O   . HOH   H 5 .   ? 17.661 2.997   23.145 1.00 30.41  ? 314 HOH   A O   1 
HETATM 1146 O  O   . HOH   H 5 .   ? 1.764  8.501   10.061 1.00 42.16  ? 315 HOH   A O   1 
HETATM 1147 O  O   . HOH   H 5 .   ? 17.782 -6.410  3.460  1.00 42.92  ? 316 HOH   A O   1 
HETATM 1148 O  O   . HOH   H 5 .   ? 31.456 19.692  11.313 1.00 64.15  ? 317 HOH   A O   1 
HETATM 1149 O  O   . HOH   H 5 .   ? -0.042 16.583  8.198  1.00 53.73  ? 318 HOH   A O   1 
HETATM 1150 O  O   . HOH   H 5 .   ? 23.463 22.018  7.957  1.00 51.94  ? 319 HOH   A O   1 
HETATM 1151 O  O   . HOH   H 5 .   ? 0.536  0.151   16.562 1.00 22.28  ? 320 HOH   A O   1 
HETATM 1152 O  O   . HOH   H 5 .   ? 23.278 0.344   15.810 1.00 41.80  ? 321 HOH   A O   1 
HETATM 1153 O  O   . HOH   H 5 .   ? 10.459 8.751   4.732  1.00 31.54  ? 322 HOH   A O   1 
HETATM 1154 O  O   . HOH   H 5 .   ? 28.018 16.588  3.758  1.00 48.83  ? 323 HOH   A O   1 
HETATM 1155 O  O   . HOH   H 5 .   ? 18.949 -0.066  27.481 1.00 45.72  ? 324 HOH   A O   1 
HETATM 1156 O  O   . HOH   H 5 .   ? 29.228 3.684   10.923 1.00 39.86  ? 325 HOH   A O   1 
HETATM 1157 O  O   . HOH   H 5 .   ? 5.818  -4.818  28.842 1.00 46.64  ? 326 HOH   A O   1 
HETATM 1158 O  O   . HOH   H 5 .   ? 17.925 21.647  9.955  1.00 37.23  ? 327 HOH   A O   1 
HETATM 1159 O  O   . HOH   H 5 .   ? 24.486 18.000  4.052  1.00 71.51  ? 328 HOH   A O   1 
HETATM 1160 O  O   . HOH   H 5 .   ? 20.983 -0.439  -1.305 1.00 57.75  ? 329 HOH   A O   1 
HETATM 1161 O  O   . HOH   H 5 .   ? 24.358 9.207   -3.367 1.00 61.50  ? 330 HOH   A O   1 
HETATM 1162 O  O   . HOH   H 5 .   ? 8.397  -3.490  0.377  1.00 39.74  ? 331 HOH   A O   1 
HETATM 1163 O  O   . HOH   H 5 .   ? 10.092 5.400   3.564  1.00 30.78  ? 332 HOH   A O   1 
HETATM 1164 O  O   . HOH   H 5 .   ? 0.854  -2.083  19.928 1.00 38.85  ? 333 HOH   A O   1 
HETATM 1165 O  O   . HOH   H 5 .   ? 16.756 17.484  30.261 1.00 72.07  ? 334 HOH   A O   1 
HETATM 1166 O  O   . HOH   H 5 .   ? 16.043 23.903  14.858 1.00 66.27  ? 335 HOH   A O   1 
HETATM 1167 O  O   . HOH   H 5 .   ? 14.632 3.001   23.223 1.00 23.26  ? 336 HOH   A O   1 
HETATM 1168 O  O   . HOH   H 5 .   ? 9.144  24.697  23.998 1.00 44.03  ? 337 HOH   A O   1 
HETATM 1169 O  O   . HOH   H 5 .   ? 14.903 23.713  18.256 1.00 36.81  ? 338 HOH   A O   1 
HETATM 1170 O  O   . HOH   H 5 .   ? 6.450  17.868  25.110 1.00 34.98  ? 339 HOH   A O   1 
HETATM 1171 O  O   . HOH   H 5 .   ? 10.489 18.261  5.944  1.00 47.01  ? 340 HOH   A O   1 
HETATM 1172 O  O   . HOH   H 5 .   ? 0.155  2.147   24.423 1.00 35.99  ? 341 HOH   A O   1 
HETATM 1173 O  O   . HOH   H 5 .   ? 14.630 12.844  24.207 1.00 39.14  ? 342 HOH   A O   1 
HETATM 1174 O  O   . HOH   H 5 .   ? 30.011 11.521  20.545 1.00 52.33  ? 343 HOH   A O   1 
HETATM 1175 O  O   . HOH   H 5 .   ? 11.132 12.147  11.473 1.00 25.55  ? 344 HOH   A O   1 
HETATM 1176 O  O   . HOH   H 5 .   ? 9.272  18.708  20.281 1.00 31.22  ? 345 HOH   A O   1 
HETATM 1177 O  O   . HOH   H 5 .   ? 5.331  14.671  22.102 1.00 34.98  ? 346 HOH   A O   1 
HETATM 1178 O  O   . HOH   H 5 .   ? 17.696 0.744   29.850 1.00 40.78  ? 347 HOH   A O   1 
HETATM 1179 O  O   . HOH   H 5 .   ? 15.122 10.233  24.745 1.00 29.70  ? 348 HOH   A O   1 
HETATM 1180 O  O   . HOH   H 5 .   ? 16.880 20.666  19.767 1.00 34.47  ? 349 HOH   A O   1 
HETATM 1181 O  O   . HOH   H 5 .   ? 4.251  6.122   24.860 1.00 25.93  ? 350 HOH   A O   1 
HETATM 1182 O  O   . HOH   H 5 .   ? 12.465 11.266  0.315  1.00 49.22  ? 351 HOH   A O   1 
HETATM 1183 O  O   . HOH   H 5 .   ? 7.725  19.879  18.324 1.00 28.26  ? 352 HOH   A O   1 
HETATM 1184 O  O   . HOH   H 5 .   ? 2.911  3.916   27.485 1.00 35.81  ? 353 HOH   A O   1 
HETATM 1185 O  O   . HOH   H 5 .   ? 22.471 18.456  21.392 1.00 59.06  ? 354 HOH   A O   1 
HETATM 1186 O  O   . HOH   H 5 .   ? 10.842 -9.137  0.811  1.00 49.75  ? 355 HOH   A O   1 
HETATM 1187 O  O   . HOH   H 5 .   ? 17.707 19.306  17.358 1.00 28.83  ? 356 HOH   A O   1 
HETATM 1188 O  O   . HOH   H 5 .   ? 14.806 -3.466  17.416 1.00 35.79  ? 357 HOH   A O   1 
HETATM 1189 O  O   . HOH   H 5 .   ? 25.977 4.453   20.100 1.00 55.75  ? 358 HOH   A O   1 
HETATM 1190 O  O   . HOH   H 5 .   ? 11.289 2.594   33.544 1.00 26.05  ? 359 HOH   A O   1 
HETATM 1191 O  O   . HOH   H 5 .   ? 14.711 24.549  26.338 1.00 44.94  ? 360 HOH   A O   1 
HETATM 1192 O  O   . HOH   H 5 .   ? 1.861  -6.046  14.670 1.00 50.36  ? 361 HOH   A O   1 
HETATM 1193 O  O   . HOH   H 5 .   ? 0.089  14.322  17.295 1.00 35.50  ? 362 HOH   A O   1 
HETATM 1194 O  O   . HOH   H 5 .   ? 7.471  3.963   33.036 1.00 34.73  ? 363 HOH   A O   1 
HETATM 1195 O  O   . HOH   H 5 .   ? 12.931 11.015  9.496  1.00 25.33  ? 364 HOH   A O   1 
HETATM 1196 O  O   . HOH   H 5 .   ? 34.034 -2.566  10.128 1.00 52.39  ? 365 HOH   A O   1 
HETATM 1197 O  O   . HOH   H 5 .   ? 4.227  10.911  20.203 1.00 40.53  ? 366 HOH   A O   1 
HETATM 1198 O  O   . HOH   H 5 .   ? 30.376 -3.064  6.985  1.00 56.80  ? 367 HOH   A O   1 
HETATM 1199 O  O   . HOH   H 5 .   ? 31.129 3.270   12.759 1.00 55.99  ? 368 HOH   A O   1 
HETATM 1200 O  O   . HOH   H 5 .   ? 5.668  2.305   6.344  1.00 45.49  ? 369 HOH   A O   1 
HETATM 1201 O  O   . HOH   H 5 .   ? 9.311  -4.367  32.099 1.00 53.14  ? 370 HOH   A O   1 
HETATM 1202 O  O   . HOH   H 5 .   ? 18.278 19.495  28.075 1.00 66.88  ? 371 HOH   A O   1 
HETATM 1203 O  O   . HOH   H 5 .   ? 7.766  20.689  8.940  1.00 52.86  ? 372 HOH   A O   1 
HETATM 1204 O  O   . HOH   H 5 .   ? 14.707 11.963  0.641  1.00 48.82  ? 373 HOH   A O   1 
HETATM 1205 O  O   . HOH   H 5 .   ? 31.700 2.964   3.509  1.00 51.63  ? 374 HOH   A O   1 
HETATM 1206 O  O   . HOH   H 5 .   ? 23.802 -6.203  8.404  1.00 62.44  ? 375 HOH   A O   1 
HETATM 1207 O  O   . HOH   H 5 .   ? 8.671  3.213   2.785  1.00 32.87  ? 376 HOH   A O   1 
HETATM 1208 O  O   . HOH   H 5 .   ? 21.024 23.794  11.794 1.00 56.60  ? 377 HOH   A O   1 
HETATM 1209 O  O   . HOH   H 5 .   ? 19.667 16.556  26.570 1.00 52.42  ? 378 HOH   A O   1 
HETATM 1210 O  O   . HOH   H 5 .   ? 31.578 0.152   13.528 1.00 48.87  ? 379 HOH   A O   1 
HETATM 1211 O  O   . HOH   H 5 .   ? 14.298 15.068  3.778  1.00 33.28  ? 380 HOH   A O   1 
HETATM 1212 O  O   . HOH   H 5 .   ? 30.915 19.322  8.665  1.00 44.06  ? 381 HOH   A O   1 
HETATM 1213 O  O   . HOH   H 5 .   ? 9.494  4.944   33.933 1.00 38.36  ? 382 HOH   A O   1 
HETATM 1214 O  O   . HOH   H 5 .   ? 5.467  8.323   28.148 1.00 42.62  ? 383 HOH   A O   1 
HETATM 1215 O  O   . HOH   H 5 .   ? 18.477 5.133   27.027 1.00 54.11  ? 384 HOH   A O   1 
HETATM 1216 O  O   . HOH   H 5 .   ? 21.366 19.605  18.244 1.00 48.04  ? 385 HOH   A O   1 
HETATM 1217 O  O   . HOH   H 5 .   ? 27.780 -0.531  5.610  1.00 56.39  ? 386 HOH   A O   1 
HETATM 1218 O  O   . HOH   H 5 .   ? 18.808 13.471  2.133  1.00 44.43  ? 387 HOH   A O   1 
HETATM 1219 O  O   . HOH   H 5 .   ? -0.003 3.770   6.584  1.00 57.12  ? 388 HOH   A O   1 
HETATM 1220 O  O   . HOH   H 5 .   ? 7.676  -8.183  23.411 1.00 46.29  ? 389 HOH   A O   1 
HETATM 1221 O  O   . HOH   H 5 .   ? 34.544 5.127   14.152 1.00 64.16  ? 390 HOH   A O   1 
HETATM 1222 O  O   . HOH   H 5 .   ? 6.566  13.294  5.636  1.00 37.97  ? 391 HOH   A O   1 
HETATM 1223 O  O   . HOH   H 5 .   ? 29.973 5.102   3.839  1.00 44.53  ? 392 HOH   A O   1 
HETATM 1224 O  O   . HOH   H 5 .   ? -0.736 15.543  13.255 1.00 28.54  ? 393 HOH   A O   1 
HETATM 1225 O  O   . HOH   H 5 .   ? 28.194 -1.590  13.459 1.00 50.51  ? 394 HOH   A O   1 
HETATM 1226 O  O   . HOH   H 5 .   ? 12.777 -8.171  24.591 1.00 35.36  ? 395 HOH   A O   1 
HETATM 1227 O  O   . HOH   H 5 .   ? 3.818  26.589  16.873 1.00 58.00  ? 396 HOH   A O   1 
HETATM 1228 O  O   . HOH   H 5 .   ? 20.346 2.418   18.446 1.00 44.00  ? 397 HOH   A O   1 
HETATM 1229 O  O   . HOH   H 5 .   ? 6.834  16.777  22.716 1.00 33.23  ? 398 HOH   A O   1 
HETATM 1230 O  O   . HOH   H 5 .   ? 5.303  -0.946  24.169 1.00 31.20  ? 399 HOH   A O   1 
HETATM 1231 O  O   . HOH   H 5 .   ? 12.019 21.759  13.188 1.00 35.03  ? 400 HOH   A O   1 
HETATM 1232 O  O   . HOH   H 5 .   ? 7.812  8.454   32.730 1.00 54.66  ? 401 HOH   A O   1 
HETATM 1233 O  O   . HOH   H 5 .   ? 18.402 9.629   25.585 1.00 46.35  ? 402 HOH   A O   1 
HETATM 1234 O  O   . HOH   H 5 .   ? 18.340 19.956  5.719  1.00 58.88  ? 403 HOH   A O   1 
HETATM 1235 O  O   . HOH   H 5 .   ? 4.003  -4.788  6.363  1.00 39.03  ? 404 HOH   A O   1 
HETATM 1236 O  O   . HOH   H 5 .   ? 5.780  26.242  20.932 1.00 37.78  ? 405 HOH   A O   1 
HETATM 1237 O  O   . HOH   H 5 .   ? 3.637  1.060   30.295 1.00 44.30  ? 406 HOH   A O   1 
HETATM 1238 O  O   . HOH   H 5 .   ? 24.151 13.070  23.858 1.00 62.67  ? 407 HOH   A O   1 
HETATM 1239 O  O   . HOH   H 5 .   ? 10.978 18.101  26.804 1.00 49.52  ? 408 HOH   A O   1 
HETATM 1240 O  O   . HOH   H 5 .   ? 25.907 -1.991  14.607 1.00 52.02  ? 409 HOH   A O   1 
HETATM 1241 O  O   . HOH   H 5 .   ? 30.112 11.335  17.801 1.00 57.95  ? 410 HOH   A O   1 
HETATM 1242 O  O   . HOH   H 5 .   ? 15.513 -3.911  1.510  1.00 29.54  ? 411 HOH   A O   1 
HETATM 1243 O  O   . HOH   H 5 .   ? 18.187 -4.823  27.365 1.00 63.21  ? 412 HOH   A O   1 
HETATM 1244 O  O   . HOH   H 5 .   ? 23.466 2.693   19.612 1.00 43.12  ? 413 HOH   A O   1 
HETATM 1245 O  O   . HOH   H 5 .   ? 1.241  -2.350  17.396 1.00 31.22  ? 414 HOH   A O   1 
HETATM 1246 O  O   . HOH   H 5 .   ? 0.000  0.499   -0.000 0.50 102.30 ? 415 HOH   A O   1 
HETATM 1247 O  O   . HOH   H 5 .   ? 1.694  -5.425  18.170 1.00 60.60  ? 416 HOH   A O   1 
HETATM 1248 O  O   . HOH   H 5 .   ? 3.210  15.347  20.598 1.00 33.25  ? 417 HOH   A O   1 
HETATM 1249 O  O   . HOH   H 5 .   ? 3.474  -3.689  3.651  1.00 54.54  ? 418 HOH   A O   1 
HETATM 1250 O  O   . HOH   H 5 .   ? 3.821  -1.935  21.804 1.00 35.14  ? 419 HOH   A O   1 
HETATM 1251 O  O   . HOH   H 5 .   ? 9.044  -7.276  8.014  1.00 43.42  ? 420 HOH   A O   1 
HETATM 1252 O  O   . HOH   H 5 .   ? 21.628 9.155   21.352 1.00 39.03  ? 421 HOH   A O   1 
HETATM 1253 O  O   . HOH   H 5 .   ? 14.489 -8.155  11.885 1.00 46.93  ? 422 HOH   A O   1 
HETATM 1254 O  O   . HOH   H 5 .   ? 13.382 -6.806  30.691 1.00 69.03  ? 423 HOH   A O   1 
HETATM 1255 O  O   . HOH   H 5 .   ? 21.039 16.882  24.226 1.00 62.76  ? 424 HOH   A O   1 
HETATM 1256 O  O   . HOH   H 5 .   ? 31.199 9.847   14.829 1.00 67.08  ? 425 HOH   A O   1 
HETATM 1257 O  O   . HOH   H 5 .   ? 6.667  -3.402  -1.731 1.00 52.00  ? 426 HOH   A O   1 
HETATM 1258 O  O   . HOH   H 5 .   ? 20.891 -4.512  10.380 1.00 41.38  ? 427 HOH   A O   1 
HETATM 1259 O  O   . HOH   H 5 .   ? 18.379 -0.013  19.838 1.00 38.07  ? 428 HOH   A O   1 
HETATM 1260 O  O   . HOH   H 5 .   ? 36.780 0.130   9.016  1.00 56.11  ? 429 HOH   A O   1 
HETATM 1261 O  O   . HOH   H 5 .   ? 30.209 6.552   18.962 1.00 58.56  ? 430 HOH   A O   1 
HETATM 1262 O  O   . HOH   H 5 .   ? 3.206  7.073   27.332 1.00 51.31  ? 431 HOH   A O   1 
HETATM 1263 O  O   . HOH   H 5 .   ? 22.474 19.392  6.163  1.00 35.39  ? 432 HOH   A O   1 
HETATM 1264 O  O   . HOH   H 5 .   ? 17.842 -2.933  18.934 1.00 65.76  ? 433 HOH   A O   1 
HETATM 1265 O  O   . HOH   H 5 .   ? 1.524  13.758  5.604  1.00 39.06  ? 434 HOH   A O   1 
HETATM 1266 O  O   . HOH   H 5 .   ? 23.665 15.561  23.676 1.00 62.44  ? 435 HOH   A O   1 
HETATM 1267 O  O   . HOH   H 5 .   ? 2.338  10.878  28.597 1.00 45.08  ? 436 HOH   A O   1 
HETATM 1268 O  O   . HOH   H 5 .   ? 3.487  13.909  23.609 1.00 50.61  ? 437 HOH   A O   1 
HETATM 1269 O  O   . HOH   H 5 .   ? 35.235 10.774  11.603 1.00 57.46  ? 438 HOH   A O   1 
HETATM 1270 O  O   . HOH   H 5 .   ? 18.412 -5.338  11.818 1.00 59.82  ? 439 HOH   A O   1 
HETATM 1271 O  O   . HOH   H 5 .   ? 17.961 9.658   -1.582 1.00 51.64  ? 440 HOH   A O   1 
HETATM 1272 O  O   . HOH   H 5 .   ? 7.326  -4.988  2.721  1.00 47.69  ? 441 HOH   A O   1 
HETATM 1273 O  O   . HOH   H 5 .   ? 16.621 -7.585  29.070 1.00 64.41  ? 442 HOH   A O   1 
HETATM 1274 O  O   . HOH   H 5 .   ? 1.878  2.005   26.311 1.00 43.51  ? 443 HOH   A O   1 
HETATM 1275 O  O   . HOH   H 5 .   ? 23.915 7.459   21.151 1.00 56.75  ? 444 HOH   A O   1 
HETATM 1276 O  O   . HOH   H 5 .   ? 21.623 -2.634  15.794 1.00 61.06  ? 445 HOH   A O   1 
HETATM 1277 O  O   . HOH   H 5 .   ? 18.487 23.491  18.161 1.00 66.83  ? 446 HOH   A O   1 
HETATM 1278 O  O   . HOH   H 5 .   ? 21.466 -2.441  33.847 1.00 73.00  ? 447 HOH   A O   1 
HETATM 1279 O  O   . HOH   H 5 .   ? 6.765  11.671  3.890  1.00 47.95  ? 448 HOH   A O   1 
HETATM 1280 O  O   . HOH   H 5 .   ? 4.461  -0.857  28.706 1.00 56.72  ? 449 HOH   A O   1 
HETATM 1281 O  O   . HOH   H 5 .   ? 16.586 13.043  26.775 1.00 60.51  ? 450 HOH   A O   1 
HETATM 1282 O  O   . HOH   H 5 .   ? 24.336 -7.776  6.441  1.00 55.58  ? 451 HOH   A O   1 
HETATM 1283 O  O   . HOH   H 5 .   ? 31.264 14.574  22.527 1.00 63.48  ? 452 HOH   A O   1 
HETATM 1284 O  O   . HOH   H 5 .   ? 28.906 16.218  24.328 1.00 67.91  ? 453 HOH   A O   1 
HETATM 1285 O  O   . HOH   H 5 .   ? 24.304 -2.175  4.129  1.00 69.22  ? 454 HOH   A O   1 
HETATM 1286 O  O   . HOH   H 5 .   ? 3.535  -1.520  26.421 1.00 52.49  ? 455 HOH   A O   1 
HETATM 1287 O  O   . HOH   H 5 .   ? 3.375  12.959  18.335 1.00 36.82  ? 456 HOH   A O   1 
HETATM 1288 O  O   . HOH   H 5 .   ? -1.235 24.114  13.688 1.00 56.85  ? 457 HOH   A O   1 
HETATM 1289 O  O   . HOH   H 5 .   ? 14.417 -8.675  26.260 1.00 63.82  ? 458 HOH   A O   1 
HETATM 1290 O  O   . HOH   H 5 .   ? 4.898  22.398  9.576  1.00 54.65  ? 459 HOH   A O   1 
HETATM 1291 O  O   . HOH   H 5 .   ? 23.066 10.631  23.496 1.00 64.91  ? 460 HOH   A O   1 
HETATM 1292 O  O   . HOH   H 5 .   ? 11.611 23.750  14.950 1.00 42.88  ? 461 HOH   A O   1 
HETATM 1293 O  O   . HOH   H 5 .   ? 0.860  15.170  21.725 1.00 43.06  ? 462 HOH   A O   1 
HETATM 1294 O  O   . HOH   H 5 .   ? 8.077  -7.315  1.187  1.00 59.32  ? 463 HOH   A O   1 
HETATM 1295 O  O   . HOH   H 5 .   ? 17.228 11.957  0.197  1.00 58.44  ? 464 HOH   A O   1 
HETATM 1296 O  O   . HOH   H 5 .   ? 36.814 18.357  15.533 1.00 62.15  ? 465 HOH   A O   1 
HETATM 1297 O  O   . HOH   H 5 .   ? 30.946 6.784   16.608 1.00 47.19  ? 466 HOH   A O   1 
HETATM 1298 O  O   . HOH   H 5 .   ? 13.256 14.524  1.322  1.00 67.53  ? 467 HOH   A O   1 
HETATM 1299 O  O   . HOH   H 5 .   ? 22.853 -6.860  10.851 1.00 77.04  ? 468 HOH   A O   1 
HETATM 1300 O  O   . HOH   H 5 .   ? 20.414 15.146  0.749  1.00 57.75  ? 469 HOH   A O   1 
HETATM 1301 O  O   . HOH   H 5 .   ? 16.774 14.677  2.138  1.00 58.71  ? 470 HOH   A O   1 
HETATM 1302 O  O   . HOH   H 5 .   ? 3.228  -4.032  27.252 1.00 85.19  ? 471 HOH   A O   1 
HETATM 1303 O  O   . HOH   H 5 .   ? 8.639  7.770   2.675  1.00 42.94  ? 472 HOH   A O   1 
HETATM 1304 O  O   . HOH   H 5 .   ? 6.366  11.060  28.443 1.00 48.64  ? 473 HOH   A O   1 
HETATM 1305 O  O   . HOH   H 5 .   ? 8.313  17.620  26.916 1.00 48.96  ? 474 HOH   A O   1 
HETATM 1306 O  O   . HOH   H 5 .   ? 31.813 4.737   15.088 1.00 53.35  ? 475 HOH   A O   1 
HETATM 1307 O  O   . HOH   H 5 .   ? 4.908  -6.888  27.377 1.00 73.66  ? 476 HOH   A O   1 
HETATM 1308 O  O   . HOH   H 5 .   ? 4.302  12.854  27.552 1.00 65.28  ? 477 HOH   A O   1 
HETATM 1309 O  O   . HOH   H 5 .   ? 8.148  20.054  6.398  1.00 56.37  ? 478 HOH   A O   1 
HETATM 1310 O  O   . HOH   H 5 .   ? 1.171  21.517  27.129 1.00 63.82  ? 479 HOH   A O   1 
HETATM 1311 O  O   . HOH   H 5 .   ? 3.460  -6.531  22.791 1.00 41.22  ? 480 HOH   A O   1 
HETATM 1312 O  O   . HOH   H 5 .   ? 18.653 15.489  30.387 1.00 70.28  ? 481 HOH   A O   1 
HETATM 1313 O  O   . HOH   H 5 .   ? 0.918  12.472  19.171 1.00 70.37  ? 482 HOH   A O   1 
HETATM 1314 O  O   . HOH   H 5 .   ? 18.002 10.940  29.486 1.00 59.31  ? 483 HOH   A O   1 
HETATM 1315 O  O   . HOH   H 5 .   ? 3.372  25.843  22.245 1.00 47.78  ? 484 HOH   A O   1 
HETATM 1316 O  O   . HOH   H 5 .   ? 9.435  25.266  14.022 1.00 54.82  ? 485 HOH   A O   1 
HETATM 1317 O  O   . HOH   H 5 .   ? 13.077 18.373  33.729 1.00 62.72  ? 486 HOH   A O   1 
HETATM 1318 O  O   . HOH   H 5 .   ? 4.255  16.831  26.423 1.00 56.53  ? 487 HOH   A O   1 
HETATM 1319 O  O   . HOH   H 5 .   ? 25.791 11.631  -0.674 1.00 65.41  ? 488 HOH   A O   1 
HETATM 1320 O  O   . HOH   H 5 .   ? 5.342  -7.804  23.725 1.00 46.02  ? 489 HOH   A O   1 
HETATM 1321 O  O   . HOH   H 5 .   ? 21.172 12.918  -2.445 1.00 60.25  ? 490 HOH   A O   1 
HETATM 1322 O  O   . HOH   H 5 .   ? 23.349 11.529  -2.733 1.00 73.80  ? 491 HOH   A O   1 
HETATM 1323 O  O   . HOH   H 5 .   ? 7.859  15.857  29.515 1.00 30.00  ? 492 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   ? 0.5265 0.4232 0.4668 0.0500  -0.0181 -0.0472 7   SER   A N   
2    C CA  . SER   A 1   ? 0.5159 0.4255 0.4918 0.0486  -0.0226 -0.0532 7   SER   A CA  
3    C C   . SER   A 1   ? 0.4915 0.4063 0.4770 0.0456  -0.0173 -0.0474 7   SER   A C   
4    O O   . SER   A 1   ? 0.5041 0.4110 0.4681 0.0461  -0.0143 -0.0400 7   SER   A O   
5    C CB  . SER   A 1   ? 0.5500 0.4554 0.5331 0.0556  -0.0416 -0.0645 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6035 0.4937 0.5592 0.0625  -0.0531 -0.0624 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4509 0.3776 0.4683 0.0420  -0.0142 -0.0511 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4335 0.3645 0.4610 0.0387  -0.0082 -0.0472 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4041 0.3463 0.4574 0.0319  0.0037  -0.0480 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4038 0.3499 0.4613 0.0288  0.0106  -0.0474 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3850 0.3304 0.4536 0.0296  0.0075  -0.0489 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3690 0.3214 0.4582 0.0231  0.0206  -0.0496 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3680 0.3205 0.4567 0.0194  0.0287  -0.0463 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3850 0.3337 0.4681 0.0225  0.0223  -0.0461 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3557 0.3125 0.4797 0.0243  0.0170  -0.0610 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3565 0.3116 0.4502 0.0128  0.0429  -0.0440 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3560 0.3102 0.4503 0.0085  0.0521  -0.0429 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3653 0.3214 0.4919 0.0068  0.0583  -0.0519 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3600 0.3175 0.5014 0.0050  0.0641  -0.0549 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3557 0.3088 0.4306 0.0026  0.0637  -0.0351 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3592 0.3123 0.4097 0.0040  0.0586  -0.0273 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3609 0.3116 0.4319 -0.0019 0.0724  -0.0349 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3613 0.3141 0.3972 -0.0007 0.0671  -0.0203 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3711 0.3266 0.5111 0.0071  0.0586  -0.0567 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3727 0.3299 0.5476 0.0052  0.0662  -0.0663 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3842 0.3375 0.5544 -0.0014 0.0829  -0.0651 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3909 0.3426 0.5577 -0.0005 0.0807  -0.0654 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3659 0.3258 0.5669 0.0123  0.0509  -0.0750 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3794 0.3419 0.5867 0.0186  0.0344  -0.0787 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3782 0.3453 0.6148 0.0176  0.0366  -0.0870 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.4049 0.3634 0.5866 0.0252  0.0180  -0.0741 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3900 0.3591 0.6307 0.0230  0.0214  -0.0914 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.4177 0.3764 0.5999 0.0308  0.0034  -0.0780 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.4145 0.3791 0.6269 0.0298  0.0041  -0.0873 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4333 0.3978 0.6457 0.0351  -0.0107 -0.0924 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3839 0.3334 0.5508 -0.0078 0.0999  -0.0636 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3904 0.3330 0.5460 -0.0144 0.1168  -0.0626 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3982 0.3367 0.5796 -0.0191 0.1352  -0.0697 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3897 0.3273 0.5781 -0.0200 0.1399  -0.0691 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4160 0.3536 0.5301 -0.0176 0.1199  -0.0516 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4245 0.3611 0.5305 -0.0177 0.1212  -0.0460 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4339 0.3624 0.5317 -0.0241 0.1359  -0.0514 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3990 0.3347 0.5991 -0.0220 0.1462  -0.0774 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4057 0.3367 0.6354 -0.0268 0.1661  -0.0856 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.4004 0.3396 0.6709 -0.0232 0.1594  -0.0932 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3984 0.3475 0.6872 -0.0162 0.1389  -0.0974 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3934 0.3273 0.6723 -0.0273 0.1745  -0.0937 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3827 0.3243 0.7009 -0.0245 0.1684  -0.1016 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3813 0.3236 0.6755 -0.0223 0.1587  -0.0927 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3781 0.3195 0.6917 -0.0238 0.1654  -0.0956 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4074 0.3433 0.7638 -0.0308 0.1931  -0.1113 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4840 0.4220 0.8745 -0.0319 0.2002  -0.1227 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4996 0.4498 0.9304 -0.0263 0.1840  -0.1333 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5117 0.4367 0.8857 -0.0387 0.2238  -0.1210 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3726 0.3165 0.6281 -0.0186 0.1434  -0.0827 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3676 0.3125 0.5994 -0.0160 0.1337  -0.0742 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3557 0.3094 0.5803 -0.0085 0.1087  -0.0739 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3617 0.3175 0.5809 -0.0058 0.0998  -0.0745 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3858 0.3210 0.5723 -0.0197 0.1427  -0.0608 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4048 0.3263 0.5869 -0.0265 0.1673  -0.0587 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4105 0.3274 0.6149 -0.0287 0.1796  -0.0616 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4308 0.3419 0.5839 -0.0308 0.1789  -0.0539 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4390 0.3397 0.6348 -0.0349 0.2041  -0.0584 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4599 0.3545 0.6017 -0.0368 0.2022  -0.0513 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4722 0.3608 0.6346 -0.0388 0.2154  -0.0529 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5247 0.3936 0.6746 -0.0446 0.2406  -0.0497 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3424 0.2993 0.5667 -0.0052 0.0988  -0.0733 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3362 0.2976 0.5460 0.0015  0.0779  -0.0717 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.3342 0.2924 0.5136 0.0004  0.0805  -0.0608 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.3328 0.2891 0.5213 -0.0017 0.0885  -0.0609 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3399 0.3072 0.5815 0.0064  0.0644  -0.0836 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3779 0.3462 0.5998 0.0129  0.0455  -0.0821 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3905 0.3633 0.6421 0.0185  0.0291  -0.0957 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.4164 0.3887 0.6584 0.0216  0.0195  -0.0971 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4285 0.3978 0.6476 0.0283  0.0016  -0.0971 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4215 0.3875 0.6239 0.0329  -0.0089 -0.0944 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4206 0.3885 0.6316 0.0304  -0.0046 -0.0996 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.3285 0.2855 0.4749 0.0017  0.0750  -0.0518 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.3285 0.2835 0.4499 0.0013  0.0761  -0.0422 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.3377 0.2956 0.4513 0.0070  0.0608  -0.0431 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3510 0.3090 0.4538 0.0102  0.0513  -0.0432 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.3369 0.2887 0.4297 -0.0018 0.0812  -0.0326 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3398 0.2902 0.4117 -0.0019 0.0818  -0.0232 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3251 0.2716 0.4210 -0.0072 0.0958  -0.0332 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.3272 0.2855 0.4442 0.0083  0.0594  -0.0436 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3424 0.3009 0.4489 0.0134  0.0470  -0.0451 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3370 0.2943 0.4293 0.0125  0.0519  -0.0374 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3408 0.2969 0.4357 0.0089  0.0628  -0.0322 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3567 0.3169 0.4876 0.0169  0.0379  -0.0575 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3729 0.3345 0.5184 0.0197  0.0287  -0.0656 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3614 0.3228 0.5184 0.0132  0.0484  -0.0613 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3317 0.2878 0.4098 0.0163  0.0441  -0.0373 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3318 0.2872 0.4029 0.0162  0.0479  -0.0325 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3365 0.2922 0.4313 0.0158  0.0507  -0.0391 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3347 0.2909 0.4447 0.0179  0.0435  -0.0498 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3383 0.2905 0.3916 0.0203  0.0405  -0.0337 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3570 0.3075 0.3889 0.0205  0.0394  -0.0277 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3670 0.3143 0.3919 0.0228  0.0326  -0.0304 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3595 0.3115 0.3825 0.0185  0.0456  -0.0196 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3345 0.2891 0.4339 0.0133  0.0607  -0.0331 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3427 0.2960 0.4658 0.0123  0.0659  -0.0385 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3573 0.3108 0.4858 0.0159  0.0575  -0.0480 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3556 0.3100 0.5070 0.0161  0.0549  -0.0590 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3416 0.2907 0.4629 0.0100  0.0776  -0.0281 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3428 0.2881 0.4891 0.0084  0.0862  -0.0321 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3691 0.3083 0.5091 0.0081  0.0949  -0.0209 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3975 0.3300 0.5600 0.0061  0.1060  -0.0227 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.4165 0.3487 0.5965 0.0073  0.1062  -0.0287 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4057 0.3431 0.5812 0.0107  0.0959  -0.0340 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4082 0.3330 0.6093 0.0051  0.1182  -0.0294 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3602 0.3126 0.4675 0.0187  0.0528  -0.0451 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3661 0.3160 0.4719 0.0221  0.0458  -0.0541 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3938 0.3423 0.4972 0.0256  0.0319  -0.0654 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3985 0.3438 0.5027 0.0285  0.0246  -0.0755 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3742 0.3213 0.4586 0.0237  0.0479  -0.0481 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3760 0.3207 0.4342 0.0255  0.0431  -0.0447 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3948 0.3423 0.4441 0.0234  0.0468  -0.0346 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3944 0.3322 0.4326 0.0290  0.0363  -0.0498 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4097 0.3530 0.4377 0.0254  0.0430  -0.0341 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4083 0.3445 0.4270 0.0289  0.0372  -0.0423 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4033 0.3535 0.5038 0.0258  0.0275  -0.0642 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4197 0.3681 0.5200 0.0301  0.0126  -0.0742 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4211 0.3753 0.5555 0.0285  0.0110  -0.0822 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.4273 0.3812 0.5670 0.0324  -0.0025 -0.0906 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4285 0.3725 0.5010 0.0326  0.0073  -0.0679 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4663 0.4027 0.5060 0.0343  0.0090  -0.0617 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4833 0.4145 0.4996 0.0360  0.0062  -0.0552 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4725 0.4009 0.5014 0.0386  0.0009  -0.0708 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4175 0.3756 0.5745 0.0232  0.0250  -0.0796 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4231 0.3856 0.6146 0.0209  0.0274  -0.0874 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4386 0.4034 0.6574 0.0238  0.0153  -0.1042 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4391 0.4019 0.6575 0.0248  0.0132  -0.1087 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.4193 0.3812 0.6247 0.0147  0.0470  -0.0807 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4485 0.4173 0.6906 0.0256  0.0058  -0.1142 24  THR   A N   
135  C CA  . THR   A 18  ? 0.4653 0.4374 0.7369 0.0291  -0.0092 -0.1320 24  THR   A CA  
136  C C   . THR   A 18  ? 0.4721 0.4489 0.7898 0.0234  0.0040  -0.1404 24  THR   A C   
137  O O   . THR   A 18  ? 0.4759 0.4516 0.8002 0.0172  0.0249  -0.1314 24  THR   A O   
138  C CB  . THR   A 18  ? 0.4761 0.4506 0.7567 0.0344  -0.0271 -0.1397 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4779 0.4581 0.7907 0.0300  -0.0153 -0.1403 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5036 0.4709 0.7392 0.0398  -0.0377 -0.1303 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4642 0.4449 0.8146 0.0255  -0.0083 -0.1581 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4531 0.4383 0.8534 0.0200  0.0041  -0.1682 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4325 0.4215 0.8619 0.0158  0.0168  -0.1676 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4266 0.4138 0.8788 0.0089  0.0395  -0.1652 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4610 0.4509 0.8931 0.0238  -0.0158 -0.1899 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4934 0.4898 0.9868 0.0186  -0.0057 -0.2038 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5186 0.5122 1.0315 0.0123  0.0138  -0.2039 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4992 0.5037 1.0390 0.0185  -0.0107 -0.2170 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5069 0.5064 1.0767 0.0082  0.0211  -0.2175 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5038 0.5107 1.0934 0.0116  0.0071  -0.2262 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4274 0.4195 0.8538 0.0201  0.0036  -0.1692 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4174 0.4128 0.8715 0.0164  0.0158  -0.1697 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4138 0.4020 0.8409 0.0101  0.0412  -0.1513 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.4092 0.3963 0.8622 0.0039  0.0615  -0.1518 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4489 0.4483 0.9042 0.0233  -0.0053 -0.1750 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4972 0.5018 0.9952 0.0204  0.0040  -0.1815 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4950 0.5070 1.0480 0.0195  0.0024  -0.1983 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5188 0.5198 0.9949 0.0186  0.0145  -0.1695 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4066 0.3890 0.7821 0.0115  0.0403  -0.1359 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3992 0.3746 0.7456 0.0065  0.0604  -0.1188 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3890 0.3586 0.7487 0.0002  0.0823  -0.1156 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3784 0.3418 0.7390 -0.0054 0.1027  -0.1089 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4087 0.3805 0.7046 0.0098  0.0526  -0.1058 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4174 0.3906 0.6926 0.0146  0.0381  -0.1039 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3888 0.3634 0.6757 0.0132  0.0421  -0.1050 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4495 0.4208 0.6963 0.0197  0.0240  -0.1014 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3876 0.3573 0.7556 0.0012  0.0785  -0.1204 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3960 0.3588 0.7786 -0.0041 0.0985  -0.1177 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3926 0.3556 0.8251 -0.0094 0.1132  -0.1291 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3928 0.3455 0.8302 -0.0152 0.1372  -0.1223 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3946 0.3579 0.7778 -0.0015 0.0900  -0.1222 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4114 0.3707 0.7485 0.0014  0.0859  -0.1080 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.4311 0.3937 0.7417 0.0071  0.0671  -0.1086 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.4240 0.3743 0.7369 -0.0011 0.1015  -0.0913 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4439 0.4015 0.7198 0.0077  0.0713  -0.0943 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.4399 0.3908 0.7175 0.0031  0.0907  -0.0836 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.4328 0.3729 0.7492 -0.0061 0.1235  -0.0820 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4532 0.3974 0.7045 0.0027  0.0994  -0.0681 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.4548 0.3864 0.7403 -0.0059 0.1307  -0.0656 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4594 0.3943 0.7145 -0.0014 0.1178  -0.0591 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3831 0.3564 0.8523 -0.0070 0.0993  -0.1463 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3792 0.3549 0.9039 -0.0118 0.1121  -0.1599 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3903 0.3617 0.9154 -0.0161 0.1297  -0.1544 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3862 0.3573 0.9564 -0.0211 0.1456  -0.1644 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3672 0.3562 0.9330 -0.0069 0.0881  -0.1811 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3967 0.3645 0.8737 -0.0143 0.1274  -0.1397 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3972 0.3596 0.8654 -0.0180 0.1427  -0.1335 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.4064 0.3573 0.8159 -0.0193 0.1517  -0.1128 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.4180 0.3675 0.8017 -0.0190 0.1512  -0.1060 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.4195 0.3924 0.8951 -0.0127 0.1228  -0.1410 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.4540 0.4383 0.9892 -0.0106 0.1117  -0.1619 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.4670 0.4511 1.0465 -0.0159 0.1292  -0.1713 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4534 0.4470 0.9921 -0.0028 0.0825  -0.1703 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.3982 0.3410 0.7887 -0.0204 0.1588  -0.1034 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.4093 0.3418 0.7480 -0.0206 0.1643  -0.0846 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4151 0.3330 0.7323 -0.0260 0.1869  -0.0744 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.4094 0.3176 0.7493 -0.0315 0.2088  -0.0778 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.4117 0.3384 0.7458 -0.0203 0.1678  -0.0791 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4446 0.3630 0.7303 -0.0186 0.1678  -0.0610 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4502 0.3787 0.7076 -0.0133 0.1460  -0.0578 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.4458 0.3587 0.7355 -0.0180 0.1716  -0.0575 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.4163 0.3312 0.6882 -0.0246 0.1820  -0.0621 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4217 0.3213 0.6630 -0.0290 0.1998  -0.0516 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4332 0.3217 0.6314 -0.0275 0.2004  -0.0347 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4463 0.3164 0.6290 -0.0309 0.2194  -0.0261 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4410 0.3458 0.6676 -0.0286 0.1931  -0.0528 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4698 0.3578 0.6572 -0.0327 0.2090  -0.0418 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.4286 0.3420 0.6993 -0.0298 0.1942  -0.0687 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4197 0.3183 0.5993 -0.0222 0.1798  -0.0302 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4253 0.3169 0.5692 -0.0198 0.1764  -0.0157 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4191 0.3249 0.5618 -0.0142 0.1552  -0.0164 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.4034 0.3222 0.5550 -0.0120 0.1414  -0.0245 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4418 0.3252 0.5459 -0.0211 0.1787  -0.0062 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.4615 0.3417 0.5300 -0.0176 0.1690  0.0071  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.4941 0.3579 0.5385 -0.0173 0.1768  0.0194  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4529 0.3460 0.5072 -0.0138 0.1498  0.0090  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5023 0.3700 0.5222 -0.0130 0.1616  0.0281  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.4773 0.3631 0.5039 -0.0113 0.1462  0.0215  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4386 0.3472 0.5014 -0.0120 0.1359  0.0015  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.4798 0.3751 0.4912 -0.0079 0.1302  0.0254  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4499 0.3658 0.4943 -0.0088 0.1218  0.0063  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.4661 0.3764 0.4876 -0.0071 0.1193  0.0175  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4129 0.3145 0.5446 -0.0117 0.1535  -0.0078 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.4012 0.3139 0.5300 -0.0068 0.1366  -0.0081 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4097 0.3152 0.5148 -0.0045 0.1363  0.0056  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4243 0.3157 0.5248 -0.0057 0.1488  0.0134  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.4112 0.3316 0.5731 -0.0054 0.1318  -0.0205 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4384 0.3502 0.6241 -0.0074 0.1454  -0.0222 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4765 0.3813 0.6526 -0.0051 0.1474  -0.0123 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4812 0.3727 0.6643 -0.0072 0.1629  -0.0075 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4487 0.3601 0.6107 -0.0010 0.1347  -0.0091 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3989 0.3130 0.4901 -0.0009 0.1225  0.0086  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3936 0.3034 0.4675 0.0022  0.1194  0.0201  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3863 0.3078 0.4669 0.0060  0.1073  0.0164  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3833 0.3138 0.4555 0.0069  0.0977  0.0137  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4185 0.3238 0.4622 0.0017  0.1174  0.0293  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4844 0.3843 0.5108 0.0053  0.1126  0.0414  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.4862 0.3898 0.5246 0.0088  0.1085  0.0423  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5297 0.4215 0.5306 0.0051  0.1120  0.0494  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3707 0.2904 0.4663 0.0081  0.1093  0.0159  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3643 0.2921 0.4663 0.0114  0.1009  0.0119  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3667 0.2949 0.4682 0.0114  0.1005  0.0116  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3647 0.2966 0.4486 0.0140  0.0932  0.0199  36  SER   A C   
244  O O   . SER   A 30  ? 0.3667 0.3068 0.4485 0.0153  0.0859  0.0153  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3702 0.2925 0.4905 0.0129  0.1069  0.0116  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3790 0.3033 0.5006 0.0128  0.1055  0.0092  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3723 0.3018 0.5023 0.0152  0.1008  0.0032  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4072 0.3222 0.5238 0.0146  0.1106  0.0215  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3627 0.2875 0.4336 0.0148  0.0947  0.0318  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3686 0.2982 0.4272 0.0175  0.0859  0.0384  37  SER   A CA  
251  C C   . SER   A 31  ? 0.3506 0.2886 0.3964 0.0155  0.0792  0.0350  37  SER   A C   
252  O O   . SER   A 31  ? 0.3459 0.2905 0.3884 0.0172  0.0723  0.0367  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4102 0.3291 0.4556 0.0195  0.0862  0.0512  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4848 0.3970 0.5102 0.0164  0.0887  0.0540  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3443 0.2815 0.3856 0.0120  0.0822  0.0299  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3455 0.2891 0.3765 0.0101  0.0771  0.0264  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.3417 0.2913 0.3817 0.0100  0.0748  0.0159  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.3425 0.2961 0.3744 0.0091  0.0707  0.0133  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3632 0.3005 0.3810 0.0066  0.0816  0.0282  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.4001 0.3282 0.4002 0.0069  0.0824  0.0385  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.4150 0.3342 0.3994 0.0029  0.0893  0.0390  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3990 0.3254 0.3764 0.0007  0.0845  0.0340  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.4107 0.3312 0.3682 -0.0021 0.0858  0.0356  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3869 0.2925 0.3258 -0.0028 0.0921  0.0424  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3908 0.3181 0.3454 -0.0041 0.0817  0.0304  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.3246 0.2734 0.3803 0.0113  0.0769  0.0098  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.3207 0.2727 0.3836 0.0120  0.0729  -0.0008 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.3311 0.2829 0.3945 0.0097  0.0731  -0.0052 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.3367 0.2912 0.3970 0.0108  0.0666  -0.0109 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.3280 0.2837 0.3811 0.0144  0.0666  -0.0024 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3364 0.2915 0.3904 0.0163  0.0612  -0.0125 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3133 0.2669 0.3816 0.0170  0.0610  -0.0198 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3544 0.3094 0.3945 0.0172  0.0567  -0.0135 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.3230 0.2702 0.3897 0.0066  0.0811  -0.0024 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.3243 0.2711 0.3956 0.0041  0.0834  -0.0076 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.3231 0.2664 0.4182 0.0022  0.0915  -0.0141 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3199 0.2573 0.4214 0.0014  0.0998  -0.0106 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.3374 0.2804 0.3907 0.0011  0.0880  -0.0005 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.3625 0.3102 0.3974 0.0017  0.0801  0.0028  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3743 0.3172 0.3924 -0.0016 0.0846  0.0080  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3580 0.3106 0.3974 0.0032  0.0730  -0.0049 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.3175 0.2637 0.4274 0.0016  0.0896  -0.0235 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3282 0.2724 0.4667 -0.0007 0.0978  -0.0317 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3352 0.2811 0.4806 -0.0025 0.0987  -0.0371 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3344 0.2854 0.4723 0.0002  0.0873  -0.0395 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.3220 0.2708 0.4845 0.0021  0.0900  -0.0426 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3392 0.2869 0.5384 -0.0006 0.0988  -0.0527 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3424 0.2905 0.5586 0.0009  0.0967  -0.0584 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3318 0.2859 0.5539 0.0003  0.0911  -0.0653 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3432 0.2832 0.5020 -0.0070 0.1136  -0.0387 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3546 0.2951 0.5251 -0.0093 0.1179  -0.0449 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3659 0.3074 0.5783 -0.0111 0.1252  -0.0569 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3692 0.3036 0.5923 -0.0141 0.1388  -0.0558 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3692 0.2998 0.5155 -0.0139 0.1320  -0.0363 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3727 0.3022 0.5369 -0.0172 0.1410  -0.0444 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3871 0.3190 0.4971 -0.0121 0.1223  -0.0268 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.3664 0.3160 0.6045 -0.0089 0.1159  -0.0687 43  SER   A N   
298  C CA  . SER   A 37  ? 0.3678 0.3200 0.6527 -0.0106 0.1216  -0.0824 43  SER   A CA  
299  C C   . SER   A 37  ? 0.3877 0.3405 0.6900 -0.0129 0.1285  -0.0886 43  SER   A C   
300  O O   . SER   A 37  ? 0.3864 0.3400 0.6667 -0.0114 0.1222  -0.0843 43  SER   A O   
301  C CB  . SER   A 37  ? 0.3659 0.3280 0.6742 -0.0049 0.1014  -0.0939 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3890 0.3569 0.6839 0.0011  0.0809  -0.0953 43  SER   A OG  
303  N N   . SER   A 38  ? 0.3978 0.3494 0.7417 -0.0170 0.1431  -0.0991 44  SER   A N   
304  C CA  . SER   A 38  ? 0.4195 0.3711 0.7856 -0.0197 0.1526  -0.1062 44  SER   A CA  
305  C C   . SER   A 38  ? 0.4306 0.3954 0.8282 -0.0134 0.1309  -0.1190 44  SER   A C   
306  O O   . SER   A 38  ? 0.4310 0.4040 0.8473 -0.0084 0.1127  -0.1267 44  SER   A O   
307  C CB  . SER   A 38  ? 0.4452 0.3893 0.8465 -0.0268 0.1789  -0.1131 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4704 0.4213 0.9121 -0.0256 0.1738  -0.1239 44  SER   A OG  
309  N N   . THR   A 39  ? 0.4388 0.4043 0.8416 -0.0134 0.1322  -0.1216 45  THR   A N   
310  C CA  . THR   A 39  ? 0.4468 0.4227 0.8786 -0.0066 0.1112  -0.1326 45  THR   A CA  
311  C C   . THR   A 39  ? 0.4574 0.4351 0.9373 -0.0099 0.1248  -0.1451 45  THR   A C   
312  O O   . THR   A 39  ? 0.4630 0.4314 0.9386 -0.0175 0.1511  -0.1422 45  THR   A O   
313  C CB  . THR   A 39  ? 0.4733 0.4492 0.8644 -0.0011 0.0939  -0.1234 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4907 0.4606 0.8684 -0.0055 0.1089  -0.1189 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4902 0.4630 0.8331 0.0007  0.0854  -0.1105 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4580 0.4463 0.9817 -0.0037 0.1065  -0.1589 46  THR   A N   
317  C CA  . THR   A 40  ? 0.4625 0.4539 1.0386 -0.0060 0.1180  -0.1722 46  THR   A CA  
318  C C   . THR   A 40  ? 0.4713 0.4594 1.0297 -0.0050 0.1190  -0.1675 46  THR   A C   
319  O O   . THR   A 40  ? 0.4756 0.4578 1.0460 -0.0117 0.1435  -0.1698 46  THR   A O   
320  C CB  . THR   A 40  ? 0.4716 0.4762 1.1080 0.0003  0.0974  -0.1903 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4975 0.5071 1.1207 0.0112  0.0646  -0.1897 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4737 0.4814 1.1264 -0.0008 0.0955  -0.1957 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4695 0.4596 0.9978 0.0030  0.0939  -0.1609 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4709 0.4575 0.9830 0.0046  0.0931  -0.1564 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4825 0.4589 0.9333 -0.0005 0.1053  -0.1401 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4923 0.4661 0.9074 -0.0014 0.1033  -0.1305 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4724 0.4640 0.9855 0.0162  0.0605  -0.1579 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4748 0.4458 0.9158 -0.0035 0.1168  -0.1379 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4912 0.4529 0.8776 -0.0082 0.1269  -0.1245 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4702 0.4327 0.8209 -0.0015 0.1047  -0.1151 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4654 0.4312 0.8314 0.0056  0.0878  -0.1188 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5381 0.4926 0.9279 -0.0146 0.1490  -0.1275 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6371 0.5804 1.0081 -0.0245 0.1774  -0.1244 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7405 0.6732 1.0810 -0.0300 0.1925  -0.1207 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7765 0.7024 1.1355 -0.0357 0.2146  -0.1286 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7670 0.6980 1.0617 -0.0286 0.1814  -0.1097 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4561 0.4143 0.7605 -0.0038 0.1056  -0.1029 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4469 0.4042 0.7138 0.0008  0.0894  -0.0929 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4327 0.3840 0.6745 -0.0028 0.0974  -0.0877 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4353 0.3820 0.6791 -0.0097 0.1169  -0.0903 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4177 0.3678 0.6356 0.0017  0.0835  -0.0810 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4251 0.3700 0.6238 -0.0014 0.0898  -0.0776 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4232 0.3654 0.5793 -0.0034 0.0879  -0.0667 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4448 0.3831 0.5862 -0.0060 0.0920  -0.0646 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4333 0.3773 0.6505 0.0049  0.0789  -0.0814 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4528 0.4013 0.7276 0.0077  0.0801  -0.0959 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3998 0.3442 0.5394 -0.0025 0.0827  -0.0608 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4059 0.3487 0.5103 -0.0046 0.0817  -0.0514 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4098 0.3492 0.4988 -0.0127 0.0973  -0.0502 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4143 0.3516 0.5139 -0.0164 0.1095  -0.0542 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4146 0.3604 0.5087 -0.0016 0.0735  -0.0464 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4503 0.3964 0.5493 0.0065  0.0571  -0.0469 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4666 0.4090 0.5649 0.0101  0.0507  -0.0469 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4489 0.3973 0.5507 0.0096  0.0507  -0.0473 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4036 0.3409 0.4684 -0.0153 0.0975  -0.0457 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4156 0.3483 0.4597 -0.0222 0.1087  -0.0444 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4048 0.3397 0.4256 -0.0220 0.1025  -0.0359 52  THR   A C   
358  O O   . THR   A 46  ? 0.3942 0.3330 0.4097 -0.0188 0.0923  -0.0321 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4623 0.3917 0.4985 -0.0254 0.1116  -0.0471 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4739 0.4004 0.5334 -0.0260 0.1196  -0.0555 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4911 0.4154 0.4995 -0.0318 0.1187  -0.0457 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4015 0.3328 0.4091 -0.0251 0.1093  -0.0330 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4009 0.3340 0.3890 -0.0244 0.1031  -0.0252 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3997 0.3306 0.3648 -0.0281 0.1018  -0.0237 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4079 0.3314 0.3630 -0.0326 0.1106  -0.0275 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4154 0.3437 0.3997 -0.0251 0.1099  -0.0218 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4171 0.3476 0.4296 -0.0225 0.1126  -0.0260 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4205 0.3514 0.3889 -0.0230 0.1015  -0.0134 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4162 0.3555 0.4412 -0.0166 0.0989  -0.0255 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3840 0.3208 0.3419 -0.0263 0.0915  -0.0194 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3830 0.3194 0.3235 -0.0296 0.0882  -0.0193 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3852 0.3150 0.3037 -0.0315 0.0900  -0.0157 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3823 0.3116 0.2998 -0.0289 0.0893  -0.0101 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3796 0.3242 0.3231 -0.0271 0.0779  -0.0157 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3812 0.3048 0.2805 -0.0357 0.0914  -0.0188 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3964 0.3109 0.2683 -0.0367 0.0906  -0.0149 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3978 0.3164 0.2585 -0.0380 0.0787  -0.0168 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4048 0.3185 0.2545 -0.0422 0.0809  -0.0236 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.4302 0.3289 0.2853 -0.0406 0.1055  -0.0180 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.4550 0.3511 0.3295 -0.0399 0.1184  -0.0185 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.4857 0.3824 0.3650 -0.0360 0.1170  -0.0106 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4884 0.3830 0.3902 -0.0361 0.1296  -0.0134 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4942 0.3921 0.4117 -0.0328 0.1294  -0.0096 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4713 0.3735 0.3826 -0.0291 0.1186  -0.0021 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5003 0.3972 0.4421 -0.0332 0.1400  -0.0143 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3925 0.3209 0.2602 -0.0346 0.0666  -0.0120 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3874 0.3236 0.2564 -0.0356 0.0548  -0.0151 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3870 0.3319 0.2636 -0.0311 0.0428  -0.0087 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3742 0.3187 0.2543 -0.0274 0.0443  -0.0020 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3659 0.3097 0.2577 -0.0371 0.0580  -0.0204 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3645 0.3173 0.2814 -0.0321 0.0581  -0.0149 56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.3828 0.3364 0.2670 -0.0318 0.0318  -0.0120 57  ASP   A N   
393  N N   B ASP   A 51  ? 0.3937 0.3472 0.2778 -0.0319 0.0320  -0.0123 57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.3778 0.3413 0.2766 -0.0279 0.0216  -0.0077 57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.3999 0.3636 0.2978 -0.0286 0.0204  -0.0092 57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.3706 0.3456 0.2974 -0.0288 0.0225  -0.0113 57  ASP   A C   
397  C C   B ASP   A 51  ? 0.3810 0.3561 0.3074 -0.0296 0.0220  -0.0128 57  ASP   A C   
398  O O   A ASP   A 51  ? 0.3600 0.3441 0.3024 -0.0272 0.0144  -0.0111 57  ASP   A O   
399  O O   B ASP   A 51  ? 0.3738 0.3580 0.3152 -0.0291 0.0133  -0.0144 57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.4051 0.3681 0.2908 -0.0268 0.0063  -0.0082 57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.4533 0.4163 0.3375 -0.0293 0.0061  -0.0126 57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.4520 0.4176 0.3363 -0.0312 -0.0009 -0.0181 57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.5502 0.5159 0.4344 -0.0239 -0.0069 -0.0063 57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.4529 0.4197 0.3456 -0.0357 0.0077  -0.0245 57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.5732 0.5368 0.4591 -0.0199 -0.0028 0.0019  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.4844 0.4502 0.3594 -0.0300 -0.0160 -0.0197 57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.5817 0.5511 0.4652 -0.0234 -0.0221 -0.0100 57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.3648 0.3382 0.2989 -0.0309 0.0331  -0.0142 58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.3494 0.3291 0.3053 -0.0315 0.0365  -0.0162 58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.3408 0.3266 0.3108 -0.0273 0.0348  -0.0108 58  CYS   A C   
411  O O   . CYS   A 52  ? 0.3311 0.3149 0.2961 -0.0236 0.0353  -0.0051 58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.3470 0.3206 0.3043 -0.0319 0.0472  -0.0170 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.3897 0.3572 0.3406 -0.0373 0.0518  -0.0254 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.3220 0.3147 0.3113 -0.0284 0.0342  -0.0134 59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.3335 0.3306 0.3376 -0.0250 0.0360  -0.0094 59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.3336 0.3275 0.3480 -0.0260 0.0470  -0.0104 59  GLN   A C   
417  O O   . GLN   A 53  ? 0.3375 0.3342 0.3665 -0.0249 0.0506  -0.0095 59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.3519 0.3590 0.3721 -0.0246 0.0262  -0.0111 59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.4083 0.4161 0.4183 -0.0209 0.0156  -0.0065 59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.4599 0.4782 0.4914 -0.0194 0.0049  -0.0084 59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.4672 0.4886 0.4967 -0.0200 -0.0080 -0.0121 59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.4293 0.4528 0.4829 -0.0172 0.0098  -0.0067 59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.3284 0.3147 0.3349 -0.0281 0.0530  -0.0124 60  THR   A N   
424  C CA  . THR   A 54  ? 0.3291 0.3079 0.3393 -0.0281 0.0632  -0.0119 60  THR   A CA  
425  C C   . THR   A 54  ? 0.3340 0.3034 0.3289 -0.0258 0.0658  -0.0099 60  THR   A C   
426  O O   . THR   A 54  ? 0.3325 0.3017 0.3196 -0.0270 0.0626  -0.0120 60  THR   A O   
427  C CB  . THR   A 54  ? 0.3473 0.3267 0.3711 -0.0332 0.0672  -0.0176 60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.3869 0.3653 0.4045 -0.0365 0.0643  -0.0224 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.3487 0.3392 0.3941 -0.0356 0.0636  -0.0214 60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.3280 0.2890 0.3185 -0.0221 0.0711  -0.0062 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.3326 0.2852 0.3123 -0.0186 0.0713  -0.0047 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.3360 0.2770 0.3091 -0.0144 0.0760  -0.0010 61  GLY   A C   
433  O O   . GLY   A 55  ? 0.3299 0.2673 0.3057 -0.0153 0.0823  0.0001  61  GLY   A O   
434  N N   . VAL   A 56  ? 0.3405 0.2743 0.3048 -0.0096 0.0732  0.0002  62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.3545 0.2743 0.3067 -0.0042 0.0747  0.0037  62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.3542 0.2743 0.3014 0.0009  0.0680  0.0039  62  VAL   A C   
437  O O   . VAL   A 56  ? 0.3614 0.2874 0.3147 0.0011  0.0630  0.0012  62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.3783 0.2865 0.3265 -0.0026 0.0754  0.0038  62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.4001 0.2912 0.3310 0.0048  0.0734  0.0078  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.3747 0.2806 0.3291 -0.0079 0.0836  0.0031  62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.3492 0.2623 0.2858 0.0048  0.0688  0.0063  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.3529 0.2661 0.2860 0.0095  0.0617  0.0051  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.3793 0.2758 0.2940 0.0162  0.0581  0.0062  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.3889 0.2719 0.2888 0.0173  0.0641  0.0097  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.3414 0.2632 0.2795 0.0084  0.0634  0.0051  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.3634 0.2760 0.2900 0.0103  0.0695  0.0070  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.3739 0.2851 0.3029 0.0066  0.0794  0.0089  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.3822 0.2877 0.2977 0.0152  0.0663  0.0059  63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.3985 0.3003 0.3186 0.0078  0.0879  0.0100  63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.4059 0.3014 0.3089 0.0165  0.0738  0.0069  63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.4171 0.3102 0.3222 0.0127  0.0856  0.0092  63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.4442 0.3260 0.3381 0.0135  0.0958  0.0097  63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.3831 0.2794 0.2979 0.0209  0.0484  0.0030  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.4008 0.2808 0.2963 0.0283  0.0415  0.0032  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.3959 0.2715 0.2787 0.0305  0.0424  0.0025  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.3752 0.2625 0.2709 0.0293  0.0404  -0.0010 64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.4036 0.2839 0.3078 0.0331  0.0286  -0.0013 64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.4384 0.3002 0.3201 0.0418  0.0183  -0.0013 64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.4712 0.3135 0.3295 0.0453  0.0201  0.0045  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.4499 0.3119 0.3319 0.0467  0.0069  -0.0071 64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.5006 0.3223 0.3318 0.0541  0.0099  0.0055  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.4800 0.3236 0.3377 0.0553  -0.0047 -0.0077 64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.5179 0.3404 0.3480 0.0593  -0.0036 -0.0010 64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.5725 0.3736 0.3733 0.0687  -0.0164 -0.0010 64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.4124 0.2691 0.2687 0.0337  0.0465  0.0059  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.4327 0.2813 0.2725 0.0359  0.0492  0.0047  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.4680 0.2974 0.2811 0.0446  0.0370  0.0029  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.4964 0.3041 0.2819 0.0486  0.0385  0.0076  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.4472 0.2873 0.2763 0.0323  0.0661  0.0091  65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.4952 0.3202 0.2998 0.0350  0.0729  0.0073  65  CYS   A SG  
471  N N   . SER   A 60  ? 0.4608 0.2968 0.2820 0.0479  0.0242  -0.0040 66  SER   A N   
472  C CA  . SER   A 60  ? 0.4920 0.3116 0.2912 0.0567  0.0088  -0.0075 66  SER   A CA  
473  C C   . SER   A 60  ? 0.5100 0.3045 0.2676 0.0609  0.0129  -0.0058 66  SER   A C   
474  O O   . SER   A 60  ? 0.5204 0.2929 0.2479 0.0684  0.0032  -0.0042 66  SER   A O   
475  C CB  . SER   A 60  ? 0.5378 0.3709 0.3590 0.0586  -0.0050 -0.0171 66  SER   A CB  
476  O OG  . SER   A 60  ? 0.6108 0.4509 0.4369 0.0554  0.0016  -0.0207 66  SER   A OG  
477  N N   . SER   A 61  ? 0.4979 0.2938 0.2527 0.0562  0.0279  -0.0056 67  SER   A N   
478  C CA  . SER   A 61  ? 0.5242 0.2948 0.2391 0.0591  0.0360  -0.0045 67  SER   A CA  
479  C C   . SER   A 61  ? 0.5509 0.2986 0.2373 0.0594  0.0488  0.0047  67  SER   A C   
480  O O   . SER   A 61  ? 0.5836 0.3051 0.2311 0.0623  0.0569  0.0065  67  SER   A O   
481  C CB  . SER   A 61  ? 0.5215 0.3009 0.2468 0.0538  0.0495  -0.0080 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.4981 0.2929 0.2499 0.0460  0.0649  -0.0034 67  SER   A OG  
483  N N   . ARG   A 62  ? 0.5442 0.3000 0.2488 0.0561  0.0522  0.0101  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.5661 0.2998 0.2472 0.0565  0.0637  0.0187  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.5823 0.3103 0.2616 0.0617  0.0497  0.0222  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.6022 0.3108 0.2630 0.0627  0.0581  0.0298  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.5614 0.3085 0.2687 0.0469  0.0838  0.0218  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.5674 0.3184 0.2792 0.0420  0.0995  0.0189  68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.5989 0.3169 0.2691 0.0442  0.1150  0.0228  68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.6240 0.3442 0.3000 0.0395  0.1321  0.0193  68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.6519 0.3675 0.3137 0.0423  0.1297  0.0135  68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.6349 0.3448 0.2770 0.0495  0.1093  0.0098  68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.6406 0.3576 0.3106 0.0377  0.1474  0.0103  68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.5728 0.3177 0.2749 0.0647  0.0302  0.0165  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.5840 0.3288 0.2954 0.0690  0.0167  0.0180  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.5835 0.3331 0.3113 0.0624  0.0314  0.0241  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.6050 0.3367 0.3183 0.0663  0.0307  0.0301  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.6320 0.3456 0.3025 0.0806  0.0027  0.0212  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.6823 0.3925 0.3405 0.0880  -0.0173 0.0129  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.7433 0.4230 0.3622 0.1004  -0.0350 0.0160  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.7851 0.4590 0.3880 0.1078  -0.0548 0.0071  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 0.8291 0.4713 0.3790 0.1153  -0.0597 0.0085  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 0.8542 0.4660 0.3607 0.1162  -0.0437 0.0196  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 0.8278 0.4672 0.3670 0.1216  -0.0795 -0.0016 69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.5538 0.3248 0.3088 0.0528  0.0450  0.0225  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.5509 0.3273 0.3219 0.0457  0.0592  0.0264  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.5103 0.3170 0.3205 0.0377  0.0609  0.0216  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.5043 0.3262 0.3264 0.0352  0.0603  0.0174  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.6035 0.3667 0.3587 0.0415  0.0797  0.0308  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.7398 0.4675 0.4533 0.0474  0.0857  0.0383  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.8311 0.5496 0.5462 0.0406  0.1088  0.0433  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 0.9324 0.6120 0.6029 0.0459  0.1190  0.0515  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 0.9903 0.6539 0.6299 0.0482  0.1254  0.0508  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.4839 0.2972 0.3116 0.0336  0.0645  0.0226  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.4564 0.2943 0.3155 0.0259  0.0673  0.0187  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.4611 0.3002 0.3250 0.0189  0.0835  0.0207  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.4925 0.3147 0.3445 0.0188  0.0930  0.0251  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.4345 0.2777 0.3096 0.0253  0.0618  0.0170  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.4323 0.2760 0.3103 0.0318  0.0466  0.0136  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.4424 0.3053 0.3436 0.0295  0.0409  0.0075  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.4611 0.2878 0.3226 0.0407  0.0360  0.0153  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.4483 0.3068 0.3511 0.0363  0.0282  0.0047  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.4754 0.3129 0.3545 0.0437  0.0231  0.0091  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.4383 0.2956 0.3199 0.0136  0.0867  0.0176  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.4344 0.2952 0.3267 0.0072  0.1003  0.0179  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.4177 0.2998 0.3375 0.0006  0.0987  0.0138  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.3935 0.2908 0.3237 0.0001  0.0903  0.0110  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.4380 0.3012 0.3292 0.0071  0.1055  0.0172  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.4621 0.3017 0.3231 0.0124  0.1111  0.0205  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.4942 0.3143 0.3418 0.0113  0.1265  0.0243  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.4827 0.3178 0.3275 0.0184  0.1016  0.0193  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.5266 0.3213 0.3407 0.0162  0.1330  0.0276  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.5127 0.3242 0.3253 0.0234  0.1058  0.0215  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.5431 0.3333 0.3379 0.0225  0.1217  0.0261  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.5932 0.3560 0.3500 0.0278  0.1270  0.0287  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.4149 0.2969 0.3459 -0.0048 0.1076  0.0132  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.4050 0.3065 0.3603 -0.0111 0.1049  0.0082  73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.3926 0.3067 0.3622 -0.0135 0.1069  0.0065  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.4045 0.3109 0.3734 -0.0136 0.1175  0.0078  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.4159 0.3110 0.3789 -0.0155 0.1138  0.0072  73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.4318 0.3048 0.3781 -0.0128 0.1258  0.0125  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.4186 0.2813 0.3403 -0.0053 0.1208  0.0167  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.3690 0.3001 0.3500 -0.0148 0.0973  0.0037  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.3633 0.3062 0.3592 -0.0159 0.0969  0.0025  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.3415 0.3012 0.3548 -0.0198 0.0882  -0.0015 74  VAL   A C   
546  O O   . VAL   A 68  ? 0.3398 0.3021 0.3485 -0.0210 0.0815  -0.0031 74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.3854 0.3285 0.3718 -0.0108 0.0923  0.0049  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.4153 0.3422 0.3851 -0.0070 0.1007  0.0076  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.3932 0.3390 0.3708 -0.0085 0.0820  0.0052  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.3207 0.2906 0.3534 -0.0213 0.0880  -0.0035 75  SER   A N   
551  C CA  . SER   A 69  ? 0.3318 0.3166 0.3781 -0.0230 0.0766  -0.0065 75  SER   A CA  
552  C C   . SER   A 69  ? 0.3191 0.3075 0.3616 -0.0184 0.0712  -0.0026 75  SER   A C   
553  O O   . SER   A 69  ? 0.3197 0.3044 0.3645 -0.0160 0.0780  -0.0008 75  SER   A O   
554  C CB  . SER   A 69  ? 0.3697 0.3635 0.4442 -0.0267 0.0783  -0.0115 75  SER   A CB  
555  O OG  . SER   A 69  ? 0.4484 0.4378 0.5292 -0.0313 0.0857  -0.0155 75  SER   A OG  
556  N N   . PHE   A 70  ? 0.3087 0.3025 0.3449 -0.0174 0.0602  -0.0016 76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.2993 0.2947 0.3322 -0.0131 0.0560  0.0025  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.3012 0.3056 0.3404 -0.0127 0.0442  0.0029  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.3110 0.3181 0.3474 -0.0154 0.0374  0.0001  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.3046 0.2917 0.3177 -0.0106 0.0571  0.0053  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.3168 0.3013 0.3175 -0.0128 0.0540  0.0039  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.3263 0.3049 0.3223 -0.0149 0.0586  0.0015  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.3370 0.3233 0.3305 -0.0127 0.0475  0.0052  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.3370 0.3130 0.3241 -0.0169 0.0570  -0.0006 76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.3443 0.3266 0.3260 -0.0151 0.0472  0.0032  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.3340 0.3122 0.3143 -0.0173 0.0518  -0.0002 76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.2957 0.3032 0.3418 -0.0088 0.0412  0.0062  77  SER   A N   
568  C CA  . SER   A 71  ? 0.2972 0.3109 0.3481 -0.0070 0.0288  0.0080  77  SER   A CA  
569  C C   . SER   A 71  ? 0.3059 0.3132 0.3328 -0.0059 0.0233  0.0119  77  SER   A C   
570  O O   . SER   A 71  ? 0.3031 0.3029 0.3150 -0.0064 0.0300  0.0130  77  SER   A O   
571  C CB  . SER   A 71  ? 0.3029 0.3210 0.3724 -0.0028 0.0284  0.0104  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.3219 0.3333 0.3823 0.0000  0.0352  0.0142  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.3205 0.3294 0.3436 -0.0044 0.0114  0.0138  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.3518 0.3514 0.3493 -0.0034 0.0080  0.0183  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.3538 0.3476 0.3480 0.0006  0.0129  0.0249  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.3532 0.3515 0.3652 0.0037  0.0134  0.0265  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.4051 0.4050 0.3947 -0.0023 -0.0072 0.0188  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.5060 0.5040 0.4818 -0.0073 -0.0094 0.0125  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.5942 0.5918 0.5599 -0.0062 -0.0263 0.0111  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.6648 0.6582 0.6134 -0.0117 -0.0262 0.0040  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.7070 0.7009 0.6472 -0.0112 -0.0443 -0.0001 78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.3680 0.3514 0.3422 0.0001  0.0181  0.0276  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.3672 0.3450 0.3418 0.0033  0.0237  0.0327  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.3614 0.3390 0.3412 0.0083  0.0156  0.0391  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.3655 0.3396 0.3333 0.0097  0.0054  0.0423  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.3975 0.3637 0.3508 0.0012  0.0299  0.0339  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.4105 0.3778 0.3561 -0.0035 0.0307  0.0277  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.3769 0.3528 0.3295 -0.0037 0.0201  0.0255  79  PRO   A CD  
589  N N   . SER   A 74  ? 0.3503 0.3311 0.3481 0.0113  0.0191  0.0403  80  SER   A N   
590  C CA  . SER   A 74  ? 0.3610 0.3430 0.3707 0.0166  0.0120  0.0457  80  SER   A CA  
591  C C   . SER   A 74  ? 0.3496 0.3278 0.3691 0.0194  0.0204  0.0483  80  SER   A C   
592  O O   . SER   A 74  ? 0.3448 0.3213 0.3641 0.0171  0.0305  0.0446  80  SER   A O   
593  C CB  . SER   A 74  ? 0.3932 0.3884 0.4278 0.0172  0.0061  0.0413  80  SER   A CB  
594  O OG  . SER   A 74  ? 0.4481 0.4478 0.4785 0.0145  -0.0024 0.0375  80  SER   A OG  
595  N N   . LEU   A 75  ? 0.3541 0.3312 0.3842 0.0245  0.0151  0.0540  81  LEU   A N   
596  C CA  . LEU   A 75  ? 0.3604 0.3341 0.4034 0.0276  0.0219  0.0563  81  LEU   A CA  
597  C C   . LEU   A 75  ? 0.3536 0.3388 0.4241 0.0283  0.0241  0.0503  81  LEU   A C   
598  O O   . LEU   A 75  ? 0.3450 0.3370 0.4324 0.0313  0.0159  0.0512  81  LEU   A O   
599  C CB  . LEU   A 75  ? 0.3818 0.3467 0.4208 0.0333  0.0140  0.0663  81  LEU   A CB  
600  C CG  . LEU   A 75  ? 0.4153 0.3707 0.4604 0.0365  0.0217  0.0712  81  LEU   A CG  
601  C CD1 . LEU   A 75  ? 0.4186 0.3648 0.4493 0.0325  0.0339  0.0699  81  LEU   A CD1 
602  C CD2 . LEU   A 75  ? 0.4315 0.3758 0.4698 0.0431  0.0122  0.0828  81  LEU   A CD2 
603  N N   . ILE   A 76  ? 0.3447 0.3312 0.4186 0.0255  0.0349  0.0436  82  ILE   A N   
604  C CA  . ILE   A 76  ? 0.3441 0.3377 0.4375 0.0252  0.0404  0.0373  82  ILE   A CA  
605  C C   . ILE   A 76  ? 0.3544 0.3438 0.4572 0.0272  0.0495  0.0352  82  ILE   A C   
606  O O   . ILE   A 76  ? 0.3451 0.3273 0.4363 0.0264  0.0538  0.0346  82  ILE   A O   
607  C CB  . ILE   A 76  ? 0.3559 0.3510 0.4385 0.0204  0.0455  0.0309  82  ILE   A CB  
608  C CG1 . ILE   A 76  ? 0.3763 0.3747 0.4488 0.0177  0.0376  0.0317  82  ILE   A CG1 
609  C CG2 . ILE   A 76  ? 0.3566 0.3548 0.4532 0.0196  0.0542  0.0246  82  ILE   A CG2 
610  C CD1 . ILE   A 76  ? 0.3960 0.4036 0.4862 0.0178  0.0315  0.0302  82  ILE   A CD1 
611  N N   . PHE   A 77  ? 0.3625 0.3561 0.4885 0.0296  0.0525  0.0330  83  PHE   A N   
612  C CA  . PHE   A 77  ? 0.3844 0.3735 0.5197 0.0313  0.0616  0.0296  83  PHE   A CA  
613  C C   . PHE   A 77  ? 0.3922 0.3778 0.5151 0.0279  0.0708  0.0214  83  PHE   A C   
614  O O   . PHE   A 77  ? 0.4023 0.3906 0.5233 0.0255  0.0741  0.0175  83  PHE   A O   
615  C CB  . PHE   A 77  ? 0.3942 0.3882 0.5594 0.0348  0.0635  0.0288  83  PHE   A CB  
616  C CG  . PHE   A 77  ? 0.4220 0.4110 0.5967 0.0355  0.0754  0.0227  83  PHE   A CG  
617  C CD1 . PHE   A 77  ? 0.4315 0.4156 0.6160 0.0390  0.0761  0.0255  83  PHE   A CD1 
618  C CD2 . PHE   A 77  ? 0.4452 0.4326 0.6168 0.0327  0.0865  0.0138  83  PHE   A CD2 
619  C CE1 . PHE   A 77  ? 0.4366 0.4158 0.6300 0.0395  0.0869  0.0185  83  PHE   A CE1 
620  C CE2 . PHE   A 77  ? 0.4587 0.4395 0.6348 0.0334  0.0971  0.0072  83  PHE   A CE2 
621  C CZ  . PHE   A 77  ? 0.4431 0.4207 0.6308 0.0366  0.0969  0.0089  83  PHE   A CZ  
622  N N   . VAL   A 78  ? 0.3814 0.3597 0.4954 0.0280  0.0746  0.0186  84  VAL   A N   
623  C CA  . VAL   A 78  ? 0.3779 0.3506 0.4776 0.0261  0.0807  0.0105  84  VAL   A CA  
624  C C   . VAL   A 78  ? 0.3648 0.3323 0.4743 0.0280  0.0879  0.0048  84  VAL   A C   
625  O O   . VAL   A 78  ? 0.3525 0.3180 0.4715 0.0298  0.0872  0.0064  84  VAL   A O   
626  C CB  . VAL   A 78  ? 0.3903 0.3593 0.4718 0.0243  0.0765  0.0101  84  VAL   A CB  
627  C CG1 . VAL   A 78  ? 0.4084 0.3707 0.4754 0.0237  0.0797  0.0015  84  VAL   A CG1 
628  C CG2 . VAL   A 78  ? 0.3966 0.3697 0.4685 0.0222  0.0705  0.0151  84  VAL   A CG2 
629  N N   . GLU   A 79  ? 0.3647 0.3283 0.4704 0.0275  0.0959  -0.0022 85  GLU   A N   
630  C CA  . GLU   A 79  ? 0.3781 0.3353 0.4902 0.0290  0.1041  -0.0095 85  GLU   A CA  
631  C C   . GLU   A 79  ? 0.3818 0.3324 0.4844 0.0294  0.1018  -0.0149 85  GLU   A C   
632  O O   . GLU   A 79  ? 0.3844 0.3335 0.4708 0.0282  0.0954  -0.0153 85  GLU   A O   
633  C CB  . GLU   A 79  ? 0.4297 0.3802 0.5308 0.0278  0.1143  -0.0162 85  GLU   A CB  
634  C CG  . GLU   A 79  ? 0.5646 0.5217 0.6846 0.0272  0.1200  -0.0135 85  GLU   A CG  
635  C CD  . GLU   A 79  ? 0.7357 0.6894 0.8737 0.0283  0.1328  -0.0194 85  GLU   A CD  
636  O OE1 . GLU   A 79  ? 0.8003 0.7510 0.9399 0.0266  0.1442  -0.0228 85  GLU   A OE1 
637  O OE2 . GLU   A 79  ? 0.7528 0.7059 0.9043 0.0307  0.1329  -0.0209 85  GLU   A OE2 
638  N N   . ALA   A 80  ? 0.3849 0.3314 0.5002 0.0310  0.1071  -0.0202 86  ALA   A N   
639  C CA  . ALA   A 80  ? 0.3975 0.3380 0.5085 0.0311  0.1051  -0.0276 86  ALA   A CA  
640  C C   . ALA   A 80  ? 0.4184 0.3508 0.5014 0.0304  0.1029  -0.0364 86  ALA   A C   
641  O O   . ALA   A 80  ? 0.4342 0.3607 0.5023 0.0303  0.1087  -0.0396 86  ALA   A O   
642  C CB  . ALA   A 80  ? 0.3881 0.3247 0.5176 0.0327  0.1126  -0.0333 86  ALA   A CB  
643  N N   . SER   A 81  ? 0.4173 0.3485 0.4937 0.0301  0.0947  -0.0399 87  SER   A N   
644  C CA  . SER   A 81  ? 0.4417 0.3649 0.4930 0.0306  0.0887  -0.0484 87  SER   A CA  
645  C C   . SER   A 81  ? 0.4511 0.3713 0.5107 0.0313  0.0835  -0.0589 87  SER   A C   
646  O O   . SER   A 81  ? 0.4502 0.3735 0.5343 0.0309  0.0874  -0.0590 87  SER   A O   
647  C CB  . SER   A 81  ? 0.4548 0.3819 0.4944 0.0297  0.0812  -0.0423 87  SER   A CB  
648  O OG  . SER   A 81  ? 0.4590 0.3926 0.5141 0.0287  0.0756  -0.0401 87  SER   A OG  
649  N N   . GLU   A 82  ? 0.4612 0.3750 0.5026 0.0326  0.0741  -0.0680 88  GLU   A N   
650  C CA  . GLU   A 82  ? 0.4678 0.3807 0.5223 0.0331  0.0672  -0.0792 88  GLU   A CA  
651  C C   . GLU   A 82  ? 0.4394 0.3622 0.5183 0.0311  0.0637  -0.0749 88  GLU   A C   
652  O O   . GLU   A 82  ? 0.4329 0.3567 0.5327 0.0305  0.0615  -0.0830 88  GLU   A O   
653  C CB  . GLU   A 82  ? 0.5439 0.4464 0.5730 0.0360  0.0559  -0.0915 88  GLU   A CB  
654  C CG  . GLU   A 82  ? 0.6749 0.5763 0.6832 0.0373  0.0465  -0.0873 88  GLU   A CG  
655  C CD  . GLU   A 82  ? 0.8352 0.7221 0.8098 0.0415  0.0356  -0.0967 88  GLU   A CD  
656  O OE1 . GLU   A 82  ? 0.8721 0.7471 0.8159 0.0428  0.0413  -0.0940 88  GLU   A OE1 
657  O OE2 . GLU   A 82  ? 0.8843 0.7708 0.8635 0.0437  0.0212  -0.1067 88  GLU   A OE2 
658  N N   . TYR   A 83  ? 0.4201 0.3491 0.4974 0.0297  0.0647  -0.0626 89  TYR   A N   
659  C CA  . TYR   A 83  ? 0.4088 0.3444 0.5030 0.0275  0.0635  -0.0578 89  TYR   A CA  
660  C C   . TYR   A 83  ? 0.3946 0.3338 0.5064 0.0257  0.0728  -0.0469 89  TYR   A C   
661  O O   . TYR   A 83  ? 0.3866 0.3269 0.5164 0.0239  0.0752  -0.0458 89  TYR   A O   
662  C CB  . TYR   A 83  ? 0.4133 0.3511 0.4914 0.0273  0.0576  -0.0529 89  TYR   A CB  
663  C CG  . TYR   A 83  ? 0.4285 0.3608 0.4884 0.0300  0.0467  -0.0625 89  TYR   A CG  
664  C CD1 . TYR   A 83  ? 0.4372 0.3697 0.5088 0.0309  0.0373  -0.0733 89  TYR   A CD1 
665  C CD2 . TYR   A 83  ? 0.4603 0.3855 0.4916 0.0321  0.0458  -0.0612 89  TYR   A CD2 
666  C CE1 . TYR   A 83  ? 0.4618 0.3878 0.5155 0.0347  0.0245  -0.0821 89  TYR   A CE1 
667  C CE2 . TYR   A 83  ? 0.4849 0.4012 0.4945 0.0356  0.0353  -0.0690 89  TYR   A CE2 
668  C CZ  . TYR   A 83  ? 0.5001 0.4169 0.5201 0.0374  0.0232  -0.0793 89  TYR   A CZ  
669  O OH  . TYR   A 83  ? 0.5537 0.4605 0.5508 0.0420  0.0101  -0.0867 89  TYR   A OH  
670  N N   . TYR   A 84  ? 0.3881 0.3279 0.4952 0.0265  0.0783  -0.0387 90  TYR   A N   
671  C CA  . TYR   A 84  ? 0.3795 0.3213 0.5009 0.0262  0.0844  -0.0276 90  TYR   A CA  
672  C C   . TYR   A 84  ? 0.3852 0.3261 0.5132 0.0282  0.0901  -0.0260 90  TYR   A C   
673  O O   . TYR   A 84  ? 0.3950 0.3354 0.5111 0.0291  0.0907  -0.0292 90  TYR   A O   
674  C CB  . TYR   A 84  ? 0.3660 0.3121 0.4763 0.0252  0.0823  -0.0160 90  TYR   A CB  
675  C CG  . TYR   A 84  ? 0.3548 0.3019 0.4590 0.0230  0.0784  -0.0162 90  TYR   A CG  
676  C CD1 . TYR   A 84  ? 0.3580 0.3030 0.4734 0.0212  0.0821  -0.0128 90  TYR   A CD1 
677  C CD2 . TYR   A 84  ? 0.3564 0.3054 0.4437 0.0226  0.0726  -0.0189 90  TYR   A CD2 
678  C CE1 . TYR   A 84  ? 0.3547 0.3001 0.4664 0.0188  0.0807  -0.0133 90  TYR   A CE1 
679  C CE2 . TYR   A 84  ? 0.3565 0.3066 0.4409 0.0207  0.0695  -0.0191 90  TYR   A CE2 
680  C CZ  . TYR   A 84  ? 0.3537 0.3026 0.4510 0.0187  0.0739  -0.0166 90  TYR   A CZ  
681  O OH  . TYR   A 84  ? 0.3404 0.2899 0.4377 0.0165  0.0729  -0.0181 90  TYR   A OH  
682  N N   . PRO   A 85  ? 0.3797 0.3194 0.5266 0.0292  0.0952  -0.0197 91  PRO   A N   
683  C CA  . PRO   A 85  ? 0.3775 0.3176 0.5346 0.0317  0.1001  -0.0168 91  PRO   A CA  
684  C C   . PRO   A 85  ? 0.3813 0.3274 0.5310 0.0324  0.0971  -0.0065 91  PRO   A C   
685  O O   . PRO   A 85  ? 0.3853 0.3342 0.5219 0.0309  0.0917  -0.0010 91  PRO   A O   
686  C CB  . PRO   A 85  ? 0.3806 0.3164 0.5597 0.0331  0.1048  -0.0116 91  PRO   A CB  
687  C CG  . PRO   A 85  ? 0.3920 0.3259 0.5669 0.0312  0.1027  -0.0054 91  PRO   A CG  
688  C CD  . PRO   A 85  ? 0.3714 0.3082 0.5308 0.0283  0.0976  -0.0138 91  PRO   A CD  
689  N N   . ALA   A 86  ? 0.3765 0.3248 0.5373 0.0346  0.1006  -0.0046 92  ALA   A N   
690  C CA  . ALA   A 86  ? 0.3823 0.3374 0.5419 0.0353  0.0969  0.0033  92  ALA   A CA  
691  C C   . ALA   A 86  ? 0.3810 0.3370 0.5422 0.0366  0.0903  0.0157  92  ALA   A C   
692  O O   . ALA   A 86  ? 0.3786 0.3293 0.5518 0.0388  0.0918  0.0203  92  ALA   A O   
693  C CB  . ALA   A 86  ? 0.3831 0.3406 0.5621 0.0377  0.1027  0.0018  92  ALA   A CB  
694  N N   . ARG   A 87  ? 0.3772 0.3370 0.5225 0.0349  0.0838  0.0205  93  ARG   A N   
695  C CA  . ARG   A 87  ? 0.3778 0.3352 0.5169 0.0357  0.0778  0.0313  93  ARG   A CA  
696  C C   . ARG   A 87  ? 0.3800 0.3435 0.5054 0.0344  0.0700  0.0355  93  ARG   A C   
697  O O   . ARG   A 87  ? 0.3832 0.3525 0.5047 0.0323  0.0702  0.0299  93  ARG   A O   
698  C CB  . ARG   A 87  ? 0.3901 0.3402 0.5195 0.0331  0.0809  0.0298  93  ARG   A CB  
699  C CG  . ARG   A 87  ? 0.3860 0.3388 0.4970 0.0291  0.0788  0.0250  93  ARG   A CG  
700  C CD  . ARG   A 87  ? 0.3749 0.3238 0.4855 0.0267  0.0825  0.0166  93  ARG   A CD  
701  N NE  . ARG   A 87  ? 0.3626 0.3117 0.4589 0.0237  0.0802  0.0163  93  ARG   A NE  
702  C CZ  . ARG   A 87  ? 0.3810 0.3345 0.4651 0.0222  0.0762  0.0118  93  ARG   A CZ  
703  N NH1 . ARG   A 87  ? 0.3581 0.3151 0.4398 0.0232  0.0751  0.0080  93  ARG   A NH1 
704  N NH2 . ARG   A 87  ? 0.3596 0.3128 0.4343 0.0196  0.0748  0.0111  93  ARG   A NH2 
705  N N   . TYR   A 88  ? 0.3839 0.3441 0.5004 0.0355  0.0636  0.0451  94  TYR   A N   
706  C CA  . TYR   A 88  ? 0.3954 0.3599 0.4970 0.0339  0.0559  0.0479  94  TYR   A CA  
707  C C   . TYR   A 88  ? 0.3684 0.3282 0.4501 0.0296  0.0589  0.0458  94  TYR   A C   
708  O O   . TYR   A 88  ? 0.3830 0.3336 0.4597 0.0294  0.0630  0.0490  94  TYR   A O   
709  C CB  . TYR   A 88  ? 0.4232 0.3836 0.5204 0.0376  0.0465  0.0589  94  TYR   A CB  
710  C CG  . TYR   A 88  ? 0.4507 0.4166 0.5703 0.0428  0.0402  0.0616  94  TYR   A CG  
711  C CD1 . TYR   A 88  ? 0.4624 0.4404 0.5943 0.0424  0.0351  0.0572  94  TYR   A CD1 
712  C CD2 . TYR   A 88  ? 0.4750 0.4334 0.6059 0.0482  0.0393  0.0687  94  TYR   A CD2 
713  C CE1 . TYR   A 88  ? 0.4748 0.4590 0.6332 0.0472  0.0293  0.0585  94  TYR   A CE1 
714  C CE2 . TYR   A 88  ? 0.4827 0.4466 0.6382 0.0536  0.0327  0.0709  94  TYR   A CE2 
715  C CZ  . TYR   A 88  ? 0.4889 0.4664 0.6593 0.0531  0.0273  0.0654  94  TYR   A CZ  
716  O OH  . TYR   A 88  ? 0.5037 0.4872 0.7035 0.0586  0.0207  0.0667  94  TYR   A OH  
717  N N   . GLN   A 89  ? 0.3387 0.3040 0.4121 0.0262  0.0585  0.0398  95  GLN   A N   
718  C CA  . GLN   A 89  ? 0.3315 0.2935 0.3889 0.0224  0.0604  0.0374  95  GLN   A CA  
719  C C   . GLN   A 89  ? 0.3337 0.2958 0.3760 0.0213  0.0539  0.0429  95  GLN   A C   
720  O O   . GLN   A 89  ? 0.3329 0.3022 0.3772 0.0215  0.0479  0.0428  95  GLN   A O   
721  C CB  . GLN   A 89  ? 0.3331 0.2989 0.3883 0.0201  0.0627  0.0280  95  GLN   A CB  
722  C CG  . GLN   A 89  ? 0.3640 0.3266 0.4070 0.0170  0.0637  0.0251  95  GLN   A CG  
723  C CD  . GLN   A 89  ? 0.3695 0.3328 0.4112 0.0163  0.0647  0.0162  95  GLN   A CD  
724  O OE1 . GLN   A 89  ? 0.3499 0.3116 0.3988 0.0180  0.0667  0.0108  95  GLN   A OE1 
725  N NE2 . GLN   A 89  ? 0.3441 0.3081 0.3752 0.0141  0.0627  0.0143  95  GLN   A NE2 
726  N N   . SER   A 90  ? 0.3341 0.2874 0.3620 0.0199  0.0557  0.0470  96  SER   A N   
727  C CA  . SER   A 90  ? 0.3360 0.2868 0.3451 0.0186  0.0498  0.0514  96  SER   A CA  
728  C C   . SER   A 90  ? 0.3269 0.2806 0.3259 0.0139  0.0515  0.0450  96  SER   A C   
729  O O   . SER   A 90  ? 0.3233 0.2788 0.3286 0.0121  0.0572  0.0384  96  SER   A O   
730  C CB  . SER   A 90  ? 0.3570 0.2931 0.3509 0.0197  0.0524  0.0599  96  SER   A CB  
731  O OG  . SER   A 90  ? 0.3860 0.3150 0.3790 0.0166  0.0639  0.0568  96  SER   A OG  
732  N N   . HIS   A 91  ? 0.3188 0.2725 0.3027 0.0123  0.0456  0.0466  97  HIS   A N   
733  C CA  . HIS   A 91  ? 0.3261 0.2817 0.3005 0.0079  0.0468  0.0411  97  HIS   A CA  
734  C C   . HIS   A 91  ? 0.3243 0.2898 0.3120 0.0069  0.0476  0.0337  97  HIS   A C   
735  O O   . HIS   A 91  ? 0.3370 0.3019 0.3218 0.0043  0.0515  0.0286  97  HIS   A O   
736  C CB  . HIS   A 91  ? 0.3393 0.2847 0.3029 0.0051  0.0561  0.0403  97  HIS   A CB  
737  C CG  . HIS   A 91  ? 0.3879 0.3196 0.3333 0.0057  0.0581  0.0480  97  HIS   A CG  
738  N ND1 . HIS   A 91  ? 0.4291 0.3533 0.3509 0.0033  0.0568  0.0493  97  HIS   A ND1 
739  C CD2 . HIS   A 91  ? 0.4021 0.3243 0.3476 0.0085  0.0619  0.0546  97  HIS   A CD2 
740  C CE1 . HIS   A 91  ? 0.4476 0.3565 0.3525 0.0049  0.0600  0.0572  97  HIS   A CE1 
741  N NE2 . HIS   A 91  ? 0.4370 0.3442 0.3563 0.0082  0.0631  0.0612  97  HIS   A NE2 
742  N N   . LEU   A 92  ? 0.3053 0.2777 0.3069 0.0092  0.0445  0.0335  98  LEU   A N   
743  C CA  . LEU   A 92  ? 0.3026 0.2802 0.3129 0.0087  0.0473  0.0277  98  LEU   A CA  
744  C C   . LEU   A 92  ? 0.3020 0.2861 0.3145 0.0068  0.0431  0.0261  98  LEU   A C   
745  O O   . LEU   A 92  ? 0.3142 0.3025 0.3320 0.0079  0.0363  0.0290  98  LEU   A O   
746  C CB  . LEU   A 92  ? 0.2950 0.2739 0.3200 0.0119  0.0502  0.0271  98  LEU   A CB  
747  C CG  . LEU   A 92  ? 0.3034 0.2833 0.3322 0.0118  0.0552  0.0212  98  LEU   A CG  
748  C CD1 . LEU   A 92  ? 0.3160 0.2903 0.3343 0.0109  0.0577  0.0168  98  LEU   A CD1 
749  C CD2 . LEU   A 92  ? 0.3177 0.2975 0.3596 0.0148  0.0588  0.0203  98  LEU   A CD2 
750  N N   . MET   A 93  ? 0.2955 0.2800 0.3058 0.0045  0.0468  0.0213  99  MET   A N   
751  C CA  . MET   A 93  ? 0.2872 0.2767 0.3017 0.0020  0.0453  0.0188  99  MET   A CA  
752  C C   . MET   A 93  ? 0.2916 0.2804 0.3132 0.0023  0.0526  0.0156  99  MET   A C   
753  O O   . MET   A 93  ? 0.2962 0.2784 0.3096 0.0034  0.0572  0.0140  99  MET   A O   
754  C CB  . MET   A 93  ? 0.3036 0.2900 0.3048 -0.0015 0.0453  0.0165  99  MET   A CB  
755  C CG  . MET   A 93  ? 0.3216 0.3054 0.3109 -0.0023 0.0406  0.0191  99  MET   A CG  
756  S SD  . MET   A 93  ? 0.3490 0.3282 0.3246 -0.0067 0.0432  0.0150  99  MET   A SD  
757  C CE  . MET   A 93  ? 0.3051 0.2787 0.2806 -0.0052 0.0502  0.0133  99  MET   A CE  
758  N N   . LEU   A 94  ? 0.2804 0.2747 0.3171 0.0016  0.0538  0.0142  100 LEU   A N   
759  C CA  . LEU   A 94  ? 0.2890 0.2793 0.3298 0.0015  0.0638  0.0113  100 LEU   A CA  
760  C C   . LEU   A 94  ? 0.2821 0.2714 0.3230 -0.0024 0.0680  0.0084  100 LEU   A C   
761  O O   . LEU   A 94  ? 0.2723 0.2685 0.3212 -0.0051 0.0625  0.0073  100 LEU   A O   
762  C CB  . LEU   A 94  ? 0.2943 0.2896 0.3566 0.0032  0.0672  0.0107  100 LEU   A CB  
763  C CG  . LEU   A 94  ? 0.3281 0.3243 0.3956 0.0072  0.0646  0.0133  100 LEU   A CG  
764  C CD1 . LEU   A 94  ? 0.3386 0.3389 0.4301 0.0086  0.0701  0.0115  100 LEU   A CD1 
765  C CD2 . LEU   A 94  ? 0.3490 0.3355 0.3988 0.0089  0.0682  0.0129  100 LEU   A CD2 
766  N N   . ALA   A 95  ? 0.2816 0.2610 0.3139 -0.0024 0.0780  0.0071  101 ALA   A N   
767  C CA  . ALA   A 95  ? 0.2850 0.2592 0.3168 -0.0056 0.0858  0.0051  101 ALA   A CA  
768  C C   . ALA   A 95  ? 0.3021 0.2666 0.3333 -0.0047 0.0993  0.0042  101 ALA   A C   
769  O O   . ALA   A 95  ? 0.3071 0.2668 0.3307 -0.0013 0.1010  0.0046  101 ALA   A O   
770  C CB  . ALA   A 95  ? 0.2856 0.2505 0.2960 -0.0057 0.0847  0.0058  101 ALA   A CB  
771  N N   . VAL   A 96  ? 0.3154 0.2756 0.3537 -0.0080 0.1099  0.0023  102 VAL   A N   
772  C CA  . VAL   A 96  ? 0.3440 0.2903 0.3766 -0.0079 0.1262  0.0016  102 VAL   A CA  
773  C C   . VAL   A 96  ? 0.3861 0.3135 0.3843 -0.0058 0.1285  0.0045  102 VAL   A C   
774  O O   . VAL   A 96  ? 0.3786 0.3025 0.3713 -0.0077 0.1276  0.0054  102 VAL   A O   
775  C CB  . VAL   A 96  ? 0.3481 0.2972 0.4061 -0.0129 0.1377  -0.0017 102 VAL   A CB  
776  C CG1 . VAL   A 96  ? 0.3614 0.2912 0.4089 -0.0134 0.1586  -0.0020 102 VAL   A CG1 
777  C CG2 . VAL   A 96  ? 0.3416 0.3104 0.4364 -0.0138 0.1318  -0.0051 102 VAL   A CG2 
778  N N   . GLY   A 97  ? 0.4187 0.3341 0.3947 -0.0014 0.1298  0.0053  103 GLY   A N   
779  C CA  . GLY   A 97  ? 0.4408 0.3374 0.3834 0.0021  0.1289  0.0077  103 GLY   A CA  
780  C C   . GLY   A 97  ? 0.4530 0.3381 0.3737 0.0072  0.1281  0.0067  103 GLY   A C   
781  O O   . GLY   A 97  ? 0.4438 0.3360 0.3765 0.0076  0.1294  0.0042  103 GLY   A O   
782  N N   . HIS   A 98  ? 0.4538 0.3206 0.3430 0.0115  0.1250  0.0083  104 HIS   A N   
783  C CA  . HIS   A 98  ? 0.4589 0.3126 0.3237 0.0168  0.1220  0.0062  104 HIS   A CA  
784  C C   . HIS   A 98  ? 0.4450 0.3095 0.3138 0.0201  0.1042  0.0036  104 HIS   A C   
785  O O   . HIS   A 98  ? 0.4463 0.3146 0.3157 0.0211  0.0934  0.0046  104 HIS   A O   
786  C CB  . HIS   A 98  ? 0.4811 0.3059 0.3061 0.0208  0.1268  0.0087  104 HIS   A CB  
787  C CG  . HIS   A 98  ? 0.5217 0.3315 0.3193 0.0262  0.1236  0.0052  104 HIS   A CG  
788  N ND1 . HIS   A 98  ? 0.5407 0.3460 0.3373 0.0251  0.1363  0.0017  104 HIS   A ND1 
789  C CD2 . HIS   A 98  ? 0.5409 0.3414 0.3157 0.0326  0.1080  0.0034  104 HIS   A CD2 
790  C CE1 . HIS   A 98  ? 0.5614 0.3536 0.3313 0.0306  0.1285  -0.0021 104 HIS   A CE1 
791  N NE2 . HIS   A 98  ? 0.5652 0.3542 0.3215 0.0354  0.1107  -0.0015 104 HIS   A NE2 
792  N N   . SER   A 99  ? 0.4345 0.3020 0.3063 0.0218  0.1026  -0.0005 105 SER   A N   
793  C CA  . SER   A 99  ? 0.4322 0.3084 0.3098 0.0246  0.0880  -0.0040 105 SER   A CA  
794  C C   . SER   A 99  ? 0.4672 0.3349 0.3340 0.0276  0.0895  -0.0093 105 SER   A C   
795  O O   . SER   A 99  ? 0.4723 0.3427 0.3496 0.0255  0.1003  -0.0104 105 SER   A O   
796  C CB  . SER   A 99  ? 0.4149 0.3137 0.3250 0.0209  0.0842  -0.0029 105 SER   A CB  
797  O OG  . SER   A 99  ? 0.4257 0.3317 0.3441 0.0229  0.0737  -0.0063 105 SER   A OG  
798  N N   . GLU   A 100 ? 0.4812 0.3379 0.3275 0.0327  0.0788  -0.0134 106 GLU   A N   
799  C CA  . GLU   A 100 ? 0.4984 0.3460 0.3324 0.0357  0.0784  -0.0203 106 GLU   A CA  
800  C C   . GLU   A 100 ? 0.5177 0.3721 0.3599 0.0390  0.0614  -0.0265 106 GLU   A C   
801  O O   . GLU   A 100 ? 0.5280 0.3897 0.3795 0.0395  0.0510  -0.0251 106 GLU   A O   
802  C CB  . GLU   A 100 ? 0.5247 0.3441 0.3160 0.0393  0.0847  -0.0208 106 GLU   A CB  
803  C CG  . GLU   A 100 ? 0.5825 0.3867 0.3458 0.0448  0.0715  -0.0196 106 GLU   A CG  
804  C CD  . GLU   A 100 ? 0.6522 0.4248 0.3678 0.0490  0.0778  -0.0193 106 GLU   A CD  
805  O OE1 . GLU   A 100 ? 0.7024 0.4624 0.3960 0.0533  0.0716  -0.0265 106 GLU   A OE1 
806  O OE2 . GLU   A 100 ? 0.6475 0.4066 0.3469 0.0477  0.0899  -0.0121 106 GLU   A OE2 
807  N N   . PRO   A 101 ? 0.5324 0.3852 0.3755 0.0407  0.0591  -0.0343 107 PRO   A N   
808  C CA  . PRO   A 101 ? 0.5307 0.3898 0.3856 0.0434  0.0431  -0.0417 107 PRO   A CA  
809  C C   . PRO   A 101 ? 0.5338 0.3832 0.3703 0.0486  0.0276  -0.0434 107 PRO   A C   
810  O O   . PRO   A 101 ? 0.5624 0.3905 0.3625 0.0532  0.0247  -0.0444 107 PRO   A O   
811  C CB  . PRO   A 101 ? 0.5460 0.3971 0.3931 0.0452  0.0444  -0.0508 107 PRO   A CB  
812  C CG  . PRO   A 101 ? 0.5529 0.4031 0.4017 0.0416  0.0630  -0.0470 107 PRO   A CG  
813  C CD  . PRO   A 101 ? 0.5314 0.3756 0.3661 0.0401  0.0715  -0.0380 107 PRO   A CD  
814  N N   . GLY   A 102 ? 0.4930 0.3564 0.3541 0.0478  0.0188  -0.0429 108 GLY   A N   
815  C CA  . GLY   A 102 ? 0.4765 0.3351 0.3311 0.0523  0.0041  -0.0441 108 GLY   A CA  
816  C C   . GLY   A 102 ? 0.4476 0.3147 0.3143 0.0490  0.0082  -0.0356 108 GLY   A C   
817  O O   . GLY   A 102 ? 0.4421 0.3120 0.3180 0.0512  -0.0025 -0.0369 108 GLY   A O   
818  N N   . ASP   A 103 ? 0.4130 0.2850 0.2827 0.0436  0.0237  -0.0278 109 ASP   A N   
819  C CA  . ASP   A 103 ? 0.3938 0.2737 0.2742 0.0399  0.0282  -0.0208 109 ASP   A CA  
820  C C   . ASP   A 103 ? 0.3655 0.2649 0.2786 0.0354  0.0281  -0.0211 109 ASP   A C   
821  O O   . ASP   A 103 ? 0.3606 0.2653 0.2819 0.0332  0.0284  -0.0176 109 ASP   A O   
822  C CB  . ASP   A 103 ? 0.4018 0.2777 0.2724 0.0362  0.0431  -0.0138 109 ASP   A CB  
823  C CG  . ASP   A 103 ? 0.4499 0.3030 0.2857 0.0401  0.0453  -0.0115 109 ASP   A CG  
824  O OD1 . ASP   A 103 ? 0.4659 0.3088 0.2878 0.0451  0.0342  -0.0119 109 ASP   A OD1 
825  O OD2 . ASP   A 103 ? 0.4574 0.3017 0.2803 0.0385  0.0584  -0.0091 109 ASP   A OD2 
826  N N   . CYS   A 104 ? 0.3550 0.2630 0.2854 0.0343  0.0282  -0.0253 110 CYS   A N   
827  C CA  . CYS   A 104 ? 0.3578 0.2806 0.3157 0.0303  0.0298  -0.0248 110 CYS   A CA  
828  C C   . CYS   A 104 ? 0.3721 0.2972 0.3407 0.0313  0.0217  -0.0280 110 CYS   A C   
829  O O   . CYS   A 104 ? 0.3935 0.3119 0.3575 0.0362  0.0109  -0.0340 110 CYS   A O   
830  C CB  . CYS   A 104 ? 0.3661 0.2948 0.3404 0.0294  0.0317  -0.0286 110 CYS   A CB  
831  S SG  . CYS   A 104 ? 0.4069 0.3363 0.3781 0.0275  0.0431  -0.0240 110 CYS   A SG  
832  N N   . GLY   A 105 ? 0.3552 0.2886 0.3367 0.0271  0.0266  -0.0243 111 GLY   A N   
833  C CA  . GLY   A 105 ? 0.3505 0.2861 0.3449 0.0273  0.0217  -0.0277 111 GLY   A CA  
834  C C   . GLY   A 105 ? 0.3551 0.2866 0.3385 0.0272  0.0219  -0.0235 111 GLY   A C   
835  O O   . GLY   A 105 ? 0.3515 0.2863 0.3478 0.0259  0.0215  -0.0251 111 GLY   A O   
836  N N   . GLY   A 106 ? 0.3513 0.2749 0.3125 0.0281  0.0244  -0.0183 112 GLY   A N   
837  C CA  . GLY   A 106 ? 0.3469 0.2653 0.2979 0.0274  0.0266  -0.0139 112 GLY   A CA  
838  C C   . GLY   A 106 ? 0.3403 0.2688 0.3037 0.0210  0.0343  -0.0111 112 GLY   A C   
839  O O   . GLY   A 106 ? 0.3388 0.2749 0.3070 0.0171  0.0403  -0.0088 112 GLY   A O   
840  N N   . ILE   A 107 ? 0.3233 0.2509 0.2913 0.0204  0.0334  -0.0117 113 ILE   A N   
841  C CA  . ILE   A 107 ? 0.3273 0.2625 0.3042 0.0143  0.0405  -0.0105 113 ILE   A CA  
842  C C   . ILE   A 107 ? 0.3169 0.2518 0.2835 0.0107  0.0467  -0.0055 113 ILE   A C   
843  O O   . ILE   A 107 ? 0.3233 0.2495 0.2782 0.0127  0.0470  -0.0032 113 ILE   A O   
844  C CB  . ILE   A 107 ? 0.3442 0.2785 0.3332 0.0148  0.0383  -0.0147 113 ILE   A CB  
845  C CG1 . ILE   A 107 ? 0.3609 0.3007 0.3697 0.0151  0.0367  -0.0207 113 ILE   A CG1 
846  C CG2 . ILE   A 107 ? 0.3485 0.2854 0.3388 0.0091  0.0458  -0.0136 113 ILE   A CG2 
847  C CD1 . ILE   A 107 ? 0.3738 0.3133 0.4002 0.0161  0.0349  -0.0264 113 ILE   A CD1 
848  N N   . LEU   A 108 ? 0.3000 0.2432 0.2712 0.0055  0.0516  -0.0041 114 LEU   A N   
849  C CA  . LEU   A 108 ? 0.3050 0.2503 0.2723 0.0014  0.0560  -0.0014 114 LEU   A CA  
850  C C   . LEU   A 108 ? 0.3108 0.2582 0.2827 -0.0027 0.0579  -0.0040 114 LEU   A C   
851  O O   . LEU   A 108 ? 0.2950 0.2461 0.2713 -0.0045 0.0588  -0.0056 114 LEU   A O   
852  C CB  . LEU   A 108 ? 0.2972 0.2499 0.2666 -0.0007 0.0574  0.0012  114 LEU   A CB  
853  C CG  . LEU   A 108 ? 0.3031 0.2607 0.2738 -0.0053 0.0595  0.0021  114 LEU   A CG  
854  C CD1 . LEU   A 108 ? 0.3094 0.2618 0.2779 -0.0056 0.0634  0.0026  114 LEU   A CD1 
855  C CD2 . LEU   A 108 ? 0.3152 0.2804 0.2903 -0.0062 0.0580  0.0044  114 LEU   A CD2 
856  N N   . ARG   A 109 ? 0.3179 0.2614 0.2878 -0.0043 0.0600  -0.0046 115 ARG   A N   
857  C CA  . ARG   A 109 ? 0.3403 0.2846 0.3141 -0.0083 0.0627  -0.0082 115 ARG   A CA  
858  C C   . ARG   A 109 ? 0.3398 0.2860 0.3117 -0.0133 0.0656  -0.0086 115 ARG   A C   
859  O O   . ARG   A 109 ? 0.3405 0.2845 0.3111 -0.0129 0.0669  -0.0064 115 ARG   A O   
860  C CB  . ARG   A 109 ? 0.3804 0.3175 0.3592 -0.0052 0.0617  -0.0109 115 ARG   A CB  
861  C CG  . ARG   A 109 ? 0.4995 0.4269 0.4722 -0.0016 0.0607  -0.0080 115 ARG   A CG  
862  C CD  . ARG   A 109 ? 0.5988 0.5178 0.5768 0.0023  0.0581  -0.0101 115 ARG   A CD  
863  N NE  . ARG   A 109 ? 0.6821 0.6022 0.6689 0.0068  0.0517  -0.0132 115 ARG   A NE  
864  C CZ  . ARG   A 109 ? 0.7413 0.6544 0.7243 0.0141  0.0433  -0.0121 115 ARG   A CZ  
865  N NH1 . ARG   A 109 ? 0.7610 0.6626 0.7269 0.0178  0.0416  -0.0071 115 ARG   A NH1 
866  N NH2 . ARG   A 109 ? 0.7460 0.6620 0.7419 0.0177  0.0367  -0.0167 115 ARG   A NH2 
867  N N   . CYS   A 110 ? 0.3440 0.2932 0.3158 -0.0180 0.0673  -0.0121 116 CYS   A N   
868  C CA  . CYS   A 110 ? 0.3509 0.3020 0.3226 -0.0230 0.0687  -0.0148 116 CYS   A CA  
869  C C   . CYS   A 110 ? 0.3620 0.3079 0.3359 -0.0255 0.0729  -0.0203 116 CYS   A C   
870  O O   . CYS   A 110 ? 0.3567 0.2986 0.3343 -0.0229 0.0744  -0.0212 116 CYS   A O   
871  C CB  . CYS   A 110 ? 0.3508 0.3087 0.3172 -0.0261 0.0652  -0.0152 116 CYS   A CB  
872  S SG  . CYS   A 110 ? 0.3580 0.3129 0.3143 -0.0278 0.0673  -0.0174 116 CYS   A SG  
873  N N   . GLN   A 111 ? 0.3818 0.3282 0.3559 -0.0306 0.0747  -0.0249 117 GLN   A N   
874  C CA  . GLN   A 111 ? 0.4039 0.3450 0.3806 -0.0335 0.0798  -0.0311 117 GLN   A CA  
875  C C   . GLN   A 111 ? 0.4097 0.3493 0.3818 -0.0343 0.0828  -0.0340 117 GLN   A C   
876  O O   . GLN   A 111 ? 0.4340 0.3684 0.4128 -0.0348 0.0883  -0.0384 117 GLN   A O   
877  C CB  . GLN   A 111 ? 0.4355 0.3779 0.4122 -0.0396 0.0807  -0.0370 117 GLN   A CB  
878  C CG  . GLN   A 111 ? 0.4865 0.4339 0.4515 -0.0435 0.0764  -0.0400 117 GLN   A CG  
879  C CD  . GLN   A 111 ? 0.5787 0.5279 0.5459 -0.0490 0.0749  -0.0472 117 GLN   A CD  
880  O OE1 . GLN   A 111 ? 0.6121 0.5679 0.5850 -0.0500 0.0693  -0.0469 117 GLN   A OE1 
881  N NE2 . GLN   A 111 ? 0.5879 0.5314 0.5535 -0.0530 0.0802  -0.0548 117 GLN   A NE2 
882  N N   . HIS   A 112 ? 0.3956 0.3384 0.3575 -0.0345 0.0805  -0.0315 118 HIS   A N   
883  C CA  . HIS   A 112 ? 0.3991 0.3378 0.3542 -0.0359 0.0859  -0.0338 118 HIS   A CA  
884  C C   . HIS   A 112 ? 0.3978 0.3354 0.3638 -0.0316 0.0885  -0.0318 118 HIS   A C   
885  O O   . HIS   A 112 ? 0.4124 0.3454 0.3787 -0.0332 0.0961  -0.0351 118 HIS   A O   
886  C CB  . HIS   A 112 ? 0.4008 0.3401 0.3370 -0.0381 0.0828  -0.0317 118 HIS   A CB  
887  C CG  . HIS   A 112 ? 0.4086 0.3489 0.3350 -0.0423 0.0784  -0.0357 118 HIS   A CG  
888  N ND1 . HIS   A 112 ? 0.4119 0.3598 0.3405 -0.0416 0.0690  -0.0331 118 HIS   A ND1 
889  C CD2 . HIS   A 112 ? 0.4222 0.3569 0.3393 -0.0474 0.0821  -0.0434 118 HIS   A CD2 
890  C CE1 . HIS   A 112 ? 0.4181 0.3659 0.3405 -0.0460 0.0660  -0.0395 118 HIS   A CE1 
891  N NE2 . HIS   A 112 ? 0.4310 0.3705 0.3447 -0.0497 0.0735  -0.0459 118 HIS   A NE2 
892  N N   . GLY   A 113 ? 0.3718 0.3127 0.3464 -0.0263 0.0826  -0.0272 119 GLY   A N   
893  C CA  . GLY   A 113 ? 0.3545 0.2951 0.3409 -0.0217 0.0822  -0.0265 119 GLY   A CA  
894  C C   . GLY   A 113 ? 0.3383 0.2828 0.3226 -0.0176 0.0757  -0.0206 119 GLY   A C   
895  O O   . GLY   A 113 ? 0.3245 0.2716 0.3023 -0.0172 0.0714  -0.0169 119 GLY   A O   
896  N N   . VAL   A 114 ? 0.3311 0.2762 0.3228 -0.0152 0.0761  -0.0206 120 VAL   A N   
897  C CA  . VAL   A 114 ? 0.3229 0.2711 0.3141 -0.0114 0.0707  -0.0163 120 VAL   A CA  
898  C C   . VAL   A 114 ? 0.3178 0.2684 0.2970 -0.0138 0.0713  -0.0117 120 VAL   A C   
899  O O   . VAL   A 114 ? 0.3363 0.2843 0.3101 -0.0169 0.0768  -0.0119 120 VAL   A O   
900  C CB  . VAL   A 114 ? 0.3240 0.2719 0.3309 -0.0080 0.0704  -0.0194 120 VAL   A CB  
901  C CG1 . VAL   A 114 ? 0.3354 0.2859 0.3410 -0.0047 0.0655  -0.0159 120 VAL   A CG1 
902  C CG2 . VAL   A 114 ? 0.3281 0.2736 0.3481 -0.0040 0.0658  -0.0239 120 VAL   A CG2 
903  N N   . VAL   A 115 ? 0.3083 0.2623 0.2830 -0.0119 0.0661  -0.0075 121 VAL   A N   
904  C CA  . VAL   A 115 ? 0.3034 0.2606 0.2703 -0.0129 0.0644  -0.0030 121 VAL   A CA  
905  C C   . VAL   A 115 ? 0.3061 0.2641 0.2781 -0.0095 0.0636  -0.0002 121 VAL   A C   
906  O O   . VAL   A 115 ? 0.3066 0.2637 0.2742 -0.0101 0.0648  0.0031  121 VAL   A O   
907  C CB  . VAL   A 115 ? 0.3066 0.2679 0.2720 -0.0132 0.0603  -0.0014 121 VAL   A CB  
908  C CG1 . VAL   A 115 ? 0.3086 0.2745 0.2717 -0.0129 0.0565  0.0028  121 VAL   A CG1 
909  C CG2 . VAL   A 115 ? 0.3082 0.2686 0.2705 -0.0173 0.0614  -0.0050 121 VAL   A CG2 
910  N N   . GLY   A 116 ? 0.3093 0.2675 0.2888 -0.0057 0.0611  -0.0013 122 GLY   A N   
911  C CA  . GLY   A 116 ? 0.3138 0.2725 0.2992 -0.0025 0.0601  -0.0003 122 GLY   A CA  
912  C C   . GLY   A 116 ? 0.3098 0.2668 0.2990 0.0018  0.0560  -0.0031 122 GLY   A C   
913  O O   . GLY   A 116 ? 0.3102 0.2639 0.2977 0.0029  0.0540  -0.0055 122 GLY   A O   
914  N N   . ILE   A 117 ? 0.3027 0.2600 0.2955 0.0047  0.0545  -0.0030 123 ILE   A N   
915  C CA  . ILE   A 117 ? 0.3125 0.2660 0.3048 0.0093  0.0497  -0.0064 123 ILE   A CA  
916  C C   . ILE   A 117 ? 0.3112 0.2644 0.2982 0.0110  0.0501  -0.0040 123 ILE   A C   
917  O O   . ILE   A 117 ? 0.3101 0.2675 0.3018 0.0097  0.0529  -0.0010 123 ILE   A O   
918  C CB  . ILE   A 117 ? 0.3249 0.2776 0.3307 0.0115  0.0468  -0.0126 123 ILE   A CB  
919  C CG1 . ILE   A 117 ? 0.3451 0.3010 0.3613 0.0097  0.0516  -0.0117 123 ILE   A CG1 
920  C CG2 . ILE   A 117 ? 0.3413 0.2932 0.3559 0.0110  0.0458  -0.0169 123 ILE   A CG2 
921  C CD1 . ILE   A 117 ? 0.3717 0.3274 0.4064 0.0113  0.0502  -0.0190 123 ILE   A CD1 
922  N N   . VAL   A 118 ? 0.3061 0.2527 0.2827 0.0143  0.0477  -0.0054 124 VAL   A N   
923  C CA  . VAL   A 118 ? 0.3079 0.2522 0.2791 0.0159  0.0503  -0.0043 124 VAL   A CA  
924  C C   . VAL   A 118 ? 0.3048 0.2519 0.2866 0.0171  0.0496  -0.0070 124 VAL   A C   
925  O O   . VAL   A 118 ? 0.3005 0.2467 0.2890 0.0188  0.0451  -0.0120 124 VAL   A O   
926  C CB  . VAL   A 118 ? 0.3258 0.2581 0.2791 0.0196  0.0487  -0.0060 124 VAL   A CB  
927  C CG1 . VAL   A 118 ? 0.3356 0.2634 0.2825 0.0211  0.0533  -0.0065 124 VAL   A CG1 
928  C CG2 . VAL   A 118 ? 0.3341 0.2618 0.2778 0.0182  0.0515  -0.0026 124 VAL   A CG2 
929  N N   . SER   A 119 ? 0.3048 0.2558 0.2919 0.0161  0.0542  -0.0038 125 SER   A N   
930  C CA  . SER   A 119 ? 0.3198 0.2727 0.3183 0.0171  0.0550  -0.0054 125 SER   A CA  
931  C C   . SER   A 119 ? 0.3349 0.2855 0.3322 0.0187  0.0591  -0.0058 125 SER   A C   
932  O O   . SER   A 119 ? 0.3440 0.2928 0.3472 0.0205  0.0591  -0.0099 125 SER   A O   
933  C CB  . SER   A 119 ? 0.3351 0.2942 0.3449 0.0145  0.0571  -0.0005 125 SER   A CB  
934  O OG  . SER   A 119 ? 0.3442 0.3034 0.3657 0.0155  0.0592  -0.0009 125 SER   A OG  
935  N N   . THR   A 120 ? 0.3406 0.2913 0.3330 0.0177  0.0636  -0.0025 126 THR   A N   
936  C CA  . THR   A 120 ? 0.3409 0.2887 0.3342 0.0188  0.0702  -0.0036 126 THR   A CA  
937  C C   . THR   A 120 ? 0.3617 0.3004 0.3381 0.0188  0.0756  -0.0043 126 THR   A C   
938  O O   . THR   A 120 ? 0.3654 0.3014 0.3318 0.0178  0.0738  -0.0027 126 THR   A O   
939  C CB  . THR   A 120 ? 0.3403 0.2974 0.3530 0.0176  0.0731  0.0009  126 THR   A CB  
940  O OG1 . THR   A 120 ? 0.3601 0.3221 0.3758 0.0152  0.0744  0.0047  126 THR   A OG1 
941  C CG2 . THR   A 120 ? 0.3321 0.2946 0.3569 0.0178  0.0689  0.0038  126 THR   A CG2 
942  N N   . GLY   A 121 ? 0.3697 0.3017 0.3427 0.0198  0.0836  -0.0068 127 GLY   A N   
943  C CA  . GLY   A 121 ? 0.3907 0.3110 0.3469 0.0195  0.0923  -0.0071 127 GLY   A CA  
944  C C   . GLY   A 121 ? 0.4033 0.3202 0.3658 0.0192  0.1047  -0.0092 127 GLY   A C   
945  O O   . GLY   A 121 ? 0.3875 0.3151 0.3739 0.0187  0.1058  -0.0090 127 GLY   A O   
946  N N   . GLY   A 122 ? 0.4260 0.3264 0.3667 0.0196  0.1148  -0.0110 128 GLY   A N   
947  C CA  . GLY   A 122 ? 0.4445 0.3381 0.3886 0.0188  0.1302  -0.0140 128 GLY   A CA  
948  C C   . GLY   A 122 ? 0.4538 0.3562 0.4229 0.0148  0.1403  -0.0113 128 GLY   A C   
949  O O   . GLY   A 122 ? 0.4485 0.3652 0.4353 0.0128  0.1330  -0.0073 128 GLY   A O   
950  N N   . ASN   A 123 ? 0.4715 0.3648 0.4431 0.0135  0.1577  -0.0143 129 ASN   A N   
951  C CA  . ASN   A 123 ? 0.4749 0.3762 0.4759 0.0095  0.1694  -0.0139 129 ASN   A CA  
952  C C   . ASN   A 123 ? 0.4604 0.3639 0.4624 0.0063  0.1688  -0.0099 129 ASN   A C   
953  O O   . ASN   A 123 ? 0.4509 0.3688 0.4856 0.0031  0.1701  -0.0097 129 ASN   A O   
954  C CB  . ASN   A 123 ? 0.4905 0.4135 0.5325 0.0097  0.1626  -0.0140 129 ASN   A CB  
955  C CG  . ASN   A 123 ? 0.5650 0.4858 0.6161 0.0119  0.1690  -0.0187 129 ASN   A CG  
956  O OD1 . ASN   A 123 ? 0.5986 0.5016 0.6290 0.0123  0.1826  -0.0234 129 ASN   A OD1 
957  N ND2 . ASN   A 123 ? 0.5608 0.4982 0.6426 0.0135  0.1600  -0.0176 129 ASN   A ND2 
958  N N   . GLY   A 124 ? 0.4524 0.3414 0.4205 0.0073  0.1662  -0.0074 130 GLY   A N   
959  C CA  . GLY   A 124 ? 0.4423 0.3314 0.4099 0.0044  0.1660  -0.0039 130 GLY   A CA  
960  C C   . GLY   A 124 ? 0.4118 0.3223 0.4003 0.0033  0.1491  -0.0016 130 GLY   A C   
961  O O   . GLY   A 124 ? 0.4102 0.3257 0.4095 -0.0002 0.1494  -0.0003 130 GLY   A O   
962  N N   . LEU   A 125 ? 0.3894 0.3104 0.3818 0.0060  0.1350  -0.0014 131 LEU   A N   
963  C CA  . LEU   A 125 ? 0.3720 0.3096 0.3780 0.0054  0.1198  0.0010  131 LEU   A CA  
964  C C   . LEU   A 125 ? 0.3755 0.3095 0.3606 0.0084  0.1080  0.0021  131 LEU   A C   
965  O O   . LEU   A 125 ? 0.3945 0.3185 0.3629 0.0117  0.1081  0.0000  131 LEU   A O   
966  C CB  . LEU   A 125 ? 0.3607 0.3143 0.3957 0.0058  0.1148  0.0008  131 LEU   A CB  
967  C CG  . LEU   A 125 ? 0.3705 0.3323 0.4360 0.0032  0.1228  -0.0012 131 LEU   A CG  
968  C CD1 . LEU   A 125 ? 0.3758 0.3470 0.4648 0.0057  0.1204  -0.0019 131 LEU   A CD1 
969  C CD2 . LEU   A 125 ? 0.3657 0.3392 0.4468 -0.0002 0.1157  -0.0003 131 LEU   A CD2 
970  N N   . VAL   A 126 ? 0.3501 0.2923 0.3379 0.0072  0.0980  0.0042  132 VAL   A N   
971  C CA  . VAL   A 126 ? 0.3509 0.2920 0.3266 0.0094  0.0878  0.0044  132 VAL   A CA  
972  C C   . VAL   A 126 ? 0.3219 0.2776 0.3141 0.0080  0.0792  0.0064  132 VAL   A C   
973  O O   . VAL   A 126 ? 0.3141 0.2777 0.3170 0.0050  0.0779  0.0078  132 VAL   A O   
974  C CB  . VAL   A 126 ? 0.3729 0.3038 0.3294 0.0098  0.0861  0.0049  132 VAL   A CB  
975  C CG1 . VAL   A 126 ? 0.3991 0.3335 0.3627 0.0056  0.0893  0.0066  132 VAL   A CG1 
976  C CG2 . VAL   A 126 ? 0.3619 0.2940 0.3133 0.0119  0.0752  0.0040  132 VAL   A CG2 
977  N N   . GLY   A 127 ? 0.3104 0.2680 0.3035 0.0102  0.0738  0.0061  133 GLY   A N   
978  C CA  . GLY   A 127 ? 0.3068 0.2736 0.3099 0.0093  0.0674  0.0087  133 GLY   A CA  
979  C C   . GLY   A 127 ? 0.3116 0.2757 0.3058 0.0093  0.0626  0.0079  133 GLY   A C   
980  O O   . GLY   A 127 ? 0.3104 0.2678 0.2971 0.0116  0.0619  0.0045  133 GLY   A O   
981  N N   . PHE   A 128 ? 0.2956 0.2644 0.2913 0.0068  0.0592  0.0101  134 PHE   A N   
982  C CA  . PHE   A 128 ? 0.2902 0.2567 0.2805 0.0060  0.0570  0.0087  134 PHE   A CA  
983  C C   . PHE   A 128 ? 0.2907 0.2595 0.2851 0.0052  0.0560  0.0114  134 PHE   A C   
984  O O   . PHE   A 128 ? 0.2785 0.2510 0.2741 0.0041  0.0543  0.0153  134 PHE   A O   
985  C CB  . PHE   A 128 ? 0.2898 0.2562 0.2743 0.0029  0.0567  0.0083  134 PHE   A CB  
986  C CG  . PHE   A 128 ? 0.2976 0.2598 0.2772 0.0031  0.0594  0.0071  134 PHE   A CG  
987  C CD1 . PHE   A 128 ? 0.3070 0.2606 0.2775 0.0055  0.0593  0.0049  134 PHE   A CD1 
988  C CD2 . PHE   A 128 ? 0.3023 0.2680 0.2870 0.0010  0.0622  0.0083  134 PHE   A CD2 
989  C CE1 . PHE   A 128 ? 0.3157 0.2616 0.2776 0.0060  0.0630  0.0051  134 PHE   A CE1 
990  C CE2 . PHE   A 128 ? 0.3197 0.2791 0.3000 0.0007  0.0677  0.0075  134 PHE   A CE2 
991  C CZ  . PHE   A 128 ? 0.3231 0.2713 0.2895 0.0032  0.0686  0.0066  134 PHE   A CZ  
992  N N   . ALA   A 129 ? 0.2877 0.2532 0.2845 0.0060  0.0569  0.0091  135 ALA   A N   
993  C CA  . ALA   A 129 ? 0.2966 0.2608 0.2956 0.0049  0.0589  0.0119  135 ALA   A CA  
994  C C   . ALA   A 129 ? 0.3127 0.2753 0.3031 0.0014  0.0599  0.0120  135 ALA   A C   
995  O O   . ALA   A 129 ? 0.3163 0.2772 0.3079 0.0006  0.0610  0.0073  135 ALA   A O   
996  C CB  . ALA   A 129 ? 0.3057 0.2666 0.3143 0.0062  0.0613  0.0076  135 ALA   A CB  
997  N N   . ASP   A 130 ? 0.3141 0.2766 0.2961 -0.0003 0.0589  0.0167  136 ASP   A N   
998  C CA  . ASP   A 130 ? 0.3375 0.2967 0.3080 -0.0040 0.0603  0.0161  136 ASP   A CA  
999  C C   . ASP   A 130 ? 0.3459 0.2975 0.3155 -0.0056 0.0681  0.0148  136 ASP   A C   
1000 O O   . ASP   A 130 ? 0.3481 0.2955 0.3211 -0.0043 0.0718  0.0176  136 ASP   A O   
1001 C CB  . ASP   A 130 ? 0.3492 0.3082 0.3081 -0.0046 0.0555  0.0211  136 ASP   A CB  
1002 C CG  . ASP   A 130 ? 0.3925 0.3477 0.3365 -0.0085 0.0558  0.0192  136 ASP   A CG  
1003 O OD1 . ASP   A 130 ? 0.3955 0.3542 0.3419 -0.0106 0.0555  0.0143  136 ASP   A OD1 
1004 O OD2 . ASP   A 130 ? 0.4302 0.3772 0.3586 -0.0094 0.0568  0.0226  136 ASP   A OD2 
1005 N N   . VAL   A 131 ? 0.3395 0.2886 0.3065 -0.0086 0.0720  0.0101  137 VAL   A N   
1006 C CA  . VAL   A 131 ? 0.3480 0.2893 0.3166 -0.0110 0.0819  0.0078  137 VAL   A CA  
1007 C C   . VAL   A 131 ? 0.3618 0.2957 0.3115 -0.0152 0.0866  0.0079  137 VAL   A C   
1008 O O   . VAL   A 131 ? 0.3590 0.2846 0.3080 -0.0179 0.0973  0.0055  137 VAL   A O   
1009 C CB  . VAL   A 131 ? 0.3405 0.2842 0.3290 -0.0104 0.0841  0.0000  137 VAL   A CB  
1010 C CG1 . VAL   A 131 ? 0.3390 0.2877 0.3424 -0.0061 0.0786  -0.0015 137 VAL   A CG1 
1011 C CG2 . VAL   A 131 ? 0.3370 0.2834 0.3250 -0.0114 0.0812  -0.0044 137 VAL   A CG2 
1012 N N   . ARG   A 132 ? 0.3592 0.2959 0.2952 -0.0160 0.0793  0.0094  138 ARG   A N   
1013 C CA  . ARG   A 132 ? 0.3761 0.3059 0.2925 -0.0201 0.0818  0.0078  138 ARG   A CA  
1014 C C   . ARG   A 132 ? 0.4035 0.3195 0.2971 -0.0211 0.0873  0.0129  138 ARG   A C   
1015 O O   . ARG   A 132 ? 0.4201 0.3262 0.2958 -0.0249 0.0935  0.0103  138 ARG   A O   
1016 C CB  . ARG   A 132 ? 0.3620 0.2988 0.2727 -0.0205 0.0711  0.0072  138 ARG   A CB  
1017 C CG  . ARG   A 132 ? 0.3528 0.2987 0.2805 -0.0203 0.0688  0.0022  138 ARG   A CG  
1018 C CD  . ARG   A 132 ? 0.3389 0.2909 0.2636 -0.0215 0.0602  0.0013  138 ARG   A CD  
1019 N NE  . ARG   A 132 ? 0.3507 0.3090 0.2805 -0.0181 0.0524  0.0062  138 ARG   A NE  
1020 C CZ  . ARG   A 132 ? 0.3436 0.3091 0.2784 -0.0184 0.0448  0.0055  138 ARG   A CZ  
1021 N NH1 . ARG   A 132 ? 0.2948 0.2617 0.2281 -0.0220 0.0434  0.0001  138 ARG   A NH1 
1022 N NH2 . ARG   A 132 ? 0.3251 0.2966 0.2695 -0.0151 0.0394  0.0093  138 ARG   A NH2 
1023 N N   . ASP   A 133 ? 0.4147 0.3277 0.3067 -0.0178 0.0858  0.0200  139 ASP   A N   
1024 C CA  . ASP   A 133 ? 0.4449 0.3410 0.3124 -0.0181 0.0919  0.0265  139 ASP   A CA  
1025 C C   . ASP   A 133 ? 0.4504 0.3352 0.3238 -0.0205 0.1098  0.0251  139 ASP   A C   
1026 O O   . ASP   A 133 ? 0.4748 0.3417 0.3254 -0.0218 0.1193  0.0297  139 ASP   A O   
1027 C CB  . ASP   A 133 ? 0.4741 0.3699 0.3379 -0.0130 0.0826  0.0356  139 ASP   A CB  
1028 C CG  . ASP   A 133 ? 0.4940 0.3962 0.3844 -0.0101 0.0852  0.0369  139 ASP   A CG  
1029 O OD1 . ASP   A 133 ? 0.4701 0.3845 0.3841 -0.0104 0.0849  0.0303  139 ASP   A OD1 
1030 O OD2 . ASP   A 133 ? 0.5220 0.4156 0.4082 -0.0073 0.0871  0.0443  139 ASP   A OD2 
1031 N N   . LEU   A 134 ? 0.4331 0.3271 0.3369 -0.0208 0.1143  0.0186  140 LEU   A N   
1032 C CA  . LEU   A 134 ? 0.4404 0.3269 0.3595 -0.0229 0.1303  0.0152  140 LEU   A CA  
1033 C C   . LEU   A 134 ? 0.4659 0.3454 0.3814 -0.0280 0.1424  0.0081  140 LEU   A C   
1034 O O   . LEU   A 134 ? 0.4536 0.3413 0.3951 -0.0290 0.1449  -0.0007 140 LEU   A O   
1035 C CB  . LEU   A 134 ? 0.4279 0.3280 0.3829 -0.0204 0.1268  0.0099  140 LEU   A CB  
1036 C CG  . LEU   A 134 ? 0.4334 0.3408 0.3938 -0.0156 0.1158  0.0152  140 LEU   A CG  
1037 C CD1 . LEU   A 134 ? 0.4301 0.3494 0.4205 -0.0132 0.1111  0.0083  140 LEU   A CD1 
1038 C CD2 . LEU   A 134 ? 0.4534 0.3481 0.4051 -0.0148 0.1230  0.0233  140 LEU   A CD2 
1039 N N   . LEU   A 135 ? 0.4929 0.3558 0.3748 -0.0308 0.1495  0.0116  141 LEU   A N   
1040 C CA  . LEU   A 135 ? 0.5186 0.3726 0.3920 -0.0361 0.1620  0.0046  141 LEU   A CA  
1041 C C   . LEU   A 135 ? 0.5264 0.3750 0.4255 -0.0394 0.1817  -0.0022 141 LEU   A C   
1042 O O   . LEU   A 135 ? 0.5205 0.3700 0.4317 -0.0428 0.1898  -0.0114 141 LEU   A O   
1043 C CB  . LEU   A 135 ? 0.5515 0.3854 0.3777 -0.0382 0.1656  0.0097  141 LEU   A CB  
1044 C CG  . LEU   A 135 ? 0.5870 0.4247 0.3878 -0.0347 0.1450  0.0158  141 LEU   A CG  
1045 C CD1 . LEU   A 135 ? 0.6230 0.4412 0.3788 -0.0372 0.1475  0.0170  141 LEU   A CD1 
1046 C CD2 . LEU   A 135 ? 0.5845 0.4442 0.4055 -0.0336 0.1292  0.0102  141 LEU   A CD2 
1047 N N   . TRP   A 136 ? 0.5310 0.3744 0.4423 -0.0383 0.1896  0.0016  142 TRP   A N   
1048 C CA  . TRP   A 136 ? 0.5298 0.3686 0.4713 -0.0415 0.2088  -0.0055 142 TRP   A CA  
1049 C C   . TRP   A 136 ? 0.5119 0.3704 0.4983 -0.0404 0.2025  -0.0169 142 TRP   A C   
1050 O O   . TRP   A 136 ? 0.5111 0.3674 0.5250 -0.0436 0.2172  -0.0258 142 TRP   A O   
1051 C CB  . TRP   A 136 ? 0.5292 0.3584 0.4758 -0.0405 0.2176  0.0010  142 TRP   A CB  
1052 C CG  . TRP   A 136 ? 0.5188 0.3631 0.4803 -0.0348 0.1997  0.0050  142 TRP   A CG  
1053 C CD1 . TRP   A 136 ? 0.5286 0.3714 0.4657 -0.0306 0.1872  0.0159  142 TRP   A CD1 
1054 C CD2 . TRP   A 136 ? 0.4970 0.3590 0.5016 -0.0324 0.1924  -0.0027 142 TRP   A CD2 
1055 N NE1 . TRP   A 136 ? 0.5192 0.3775 0.4819 -0.0264 0.1749  0.0153  142 TRP   A NE1 
1056 C CE2 . TRP   A 136 ? 0.4972 0.3666 0.4988 -0.0274 0.1775  0.0040  142 TRP   A CE2 
1057 C CE3 . TRP   A 136 ? 0.4841 0.3553 0.5298 -0.0337 0.1967  -0.0152 142 TRP   A CE3 
1058 C CZ2 . TRP   A 136 ? 0.4813 0.3653 0.5154 -0.0242 0.1682  -0.0015 142 TRP   A CZ2 
1059 C CZ3 . TRP   A 136 ? 0.4697 0.3561 0.5475 -0.0298 0.1846  -0.0205 142 TRP   A CZ3 
1060 C CH2 . TRP   A 136 ? 0.4664 0.3583 0.5362 -0.0253 0.1711  -0.0137 142 TRP   A CH2 
1061 N N   . LEU   A 137 ? 0.4988 0.3752 0.4922 -0.0358 0.1810  -0.0170 143 LEU   A N   
1062 C CA  . LEU   A 137 ? 0.5012 0.3934 0.5305 -0.0337 0.1726  -0.0265 143 LEU   A CA  
1063 C C   . LEU   A 137 ? 0.5343 0.4250 0.5723 -0.0371 0.1808  -0.0354 143 LEU   A C   
1064 O O   . LEU   A 137 ? 0.5156 0.4150 0.5895 -0.0358 0.1794  -0.0446 143 LEU   A O   
1065 C CB  . LEU   A 137 ? 0.4872 0.3936 0.5126 -0.0284 0.1505  -0.0234 143 LEU   A CB  
1066 C CG  . LEU   A 137 ? 0.4981 0.4105 0.5310 -0.0241 0.1412  -0.0190 143 LEU   A CG  
1067 C CD1 . LEU   A 137 ? 0.4979 0.4215 0.5226 -0.0197 0.1225  -0.0158 143 LEU   A CD1 
1068 C CD2 . LEU   A 137 ? 0.4897 0.4069 0.5611 -0.0228 0.1438  -0.0274 143 LEU   A CD2 
1069 N N   . ASP   A 138 ? 0.5810 0.4602 0.5864 -0.0410 0.1882  -0.0331 144 ASP   A N   
1070 C CA  . ASP   A 138 ? 0.6260 0.5013 0.6342 -0.0450 0.1977  -0.0414 144 ASP   A CA  
1071 C C   . ASP   A 138 ? 0.6701 0.5303 0.6871 -0.0506 0.2235  -0.0472 144 ASP   A C   
1072 O O   . ASP   A 138 ? 0.6784 0.5322 0.6930 -0.0546 0.2345  -0.0540 144 ASP   A O   
1073 C CB  . ASP   A 138 ? 0.6613 0.5295 0.6276 -0.0471 0.1941  -0.0375 144 ASP   A CB  
1074 C CG  . ASP   A 138 ? 0.7140 0.5953 0.6710 -0.0430 0.1718  -0.0329 144 ASP   A CG  
1075 O OD1 . ASP   A 138 ? 0.7134 0.6090 0.6963 -0.0385 0.1596  -0.0341 144 ASP   A OD1 
1076 O OD2 . ASP   A 138 ? 0.7483 0.6245 0.6716 -0.0442 0.1666  -0.0284 144 ASP   A OD2 
1077 N N   . GLU   A 139 ? 0.7022 0.5550 0.7284 -0.0514 0.2352  -0.0450 145 GLU   A N   
1078 C CA  . GLU   A 139 ? 0.7492 0.5848 0.7827 -0.0574 0.2634  -0.0503 145 GLU   A CA  
1079 C C   . GLU   A 139 ? 0.7744 0.6088 0.8416 -0.0577 0.2744  -0.0521 145 GLU   A C   
1080 O O   . GLU   A 139 ? 0.7804 0.6238 0.8542 -0.0532 0.2606  -0.0467 145 GLU   A O   
1081 C CB  . GLU   A 139 ? 0.8159 0.6268 0.7935 -0.0616 0.2768  -0.0424 145 GLU   A CB  
1082 C CG  . GLU   A 139 ? 0.9145 0.7172 0.8599 -0.0587 0.2702  -0.0286 145 GLU   A CG  
1083 C CD  . GLU   A 139 ? 1.0648 0.8527 0.9512 -0.0589 0.2649  -0.0196 145 GLU   A CD  
1084 O OE1 . GLU   A 139 ? 1.1120 0.8775 0.9635 -0.0598 0.2758  -0.0107 145 GLU   A OE1 
1085 O OE2 . GLU   A 139 ? 1.1031 0.9011 0.9785 -0.0579 0.2493  -0.0218 145 GLU   A OE2 
1086 N N   . GLU   A 140 ? 0.7897 0.6124 0.8795 -0.0633 0.3008  -0.0604 146 GLU   A N   
1087 C CA  . GLU   A 140 ? 0.8054 0.6242 0.9311 -0.0652 0.3169  -0.0642 146 GLU   A CA  
1088 C C   . GLU   A 140 ? 0.7955 0.6390 0.9733 -0.0597 0.2971  -0.0712 146 GLU   A C   
1089 O O   . GLU   A 140 ? 0.7851 0.6415 1.0090 -0.0591 0.2951  -0.0842 146 GLU   A O   
1090 C CB  . GLU   A 140 ? 0.8630 0.6601 0.9487 -0.0666 0.3285  -0.0507 146 GLU   A CB  
1091 C CG  . GLU   A 140 ? 0.9227 0.7266 1.0292 -0.0631 0.3209  -0.0466 146 GLU   A CG  
1092 C CD  . GLU   A 140 ? 0.9922 0.7892 1.1427 -0.0674 0.3448  -0.0545 146 GLU   A CD  
1093 O OE1 . GLU   A 140 ? 0.9983 0.8039 1.1754 -0.0647 0.3376  -0.0545 146 GLU   A OE1 
1094 O OE2 . GLU   A 140 ? 1.0122 0.7947 1.1722 -0.0738 0.3717  -0.0614 146 GLU   A OE2 
1095 N N1  . A1BPF B .   ? 0.4105 0.3428 0.4102 0.0263  0.0730  -0.0235 201 A1BPF A N1  
1096 C C4  . A1BPF B .   ? 0.4150 0.3404 0.4080 0.0287  0.0665  -0.0327 201 A1BPF A C4  
1097 C C5  . A1BPF B .   ? 0.4267 0.3549 0.4139 0.0257  0.0790  -0.0208 201 A1BPF A C5  
1098 C C6  . A1BPF B .   ? 0.4641 0.3762 0.4243 0.0277  0.0828  -0.0262 201 A1BPF A C6  
1099 C C7  . A1BPF B .   ? 0.4926 0.3987 0.4324 0.0285  0.0759  -0.0247 201 A1BPF A C7  
1100 C C8  . A1BPF B .   ? 0.5116 0.4063 0.4292 0.0285  0.0821  -0.0220 201 A1BPF A C8  
1101 C C10 . A1BPF B .   ? 0.5073 0.4176 0.4489 0.0292  0.0647  -0.0247 201 A1BPF A C10 
1102 C C13 . A1BPF B .   ? 0.4723 0.3740 0.4233 0.0305  0.0832  -0.0357 201 A1BPF A C13 
1103 O O1  . A1BPF B .   ? 0.4107 0.3461 0.4071 0.0234  0.0822  -0.0143 201 A1BPF A O1  
1104 C C3  . A1BPF B .   ? 0.4078 0.3391 0.4123 0.0283  0.0580  -0.0337 201 A1BPF A C3  
1105 C C2  . A1BPF B .   ? 0.3993 0.3404 0.4268 0.0257  0.0619  -0.0270 201 A1BPF A C2  
1106 C C14 . A1BPF B .   ? 0.3975 0.3405 0.4198 0.0247  0.0732  -0.0175 201 A1BPF A C14 
1107 C C1  . A1BPF B .   ? 0.3974 0.3437 0.4234 0.0238  0.0662  -0.0172 201 A1BPF A C1  
1108 C C   . A1BPF B .   ? 0.3851 0.3383 0.4272 0.0221  0.0675  -0.0099 201 A1BPF A C   
1109 O O   . A1BPF B .   ? 0.3859 0.3402 0.4418 0.0227  0.0712  -0.0078 201 A1BPF A O   
1110 N N   . A1BPF B .   ? 0.3713 0.3273 0.4098 0.0201  0.0646  -0.0060 201 A1BPF A N   
1111 C C12 . A1BPF B .   ? 0.4832 0.3765 0.4241 0.0294  0.0975  -0.0343 201 A1BPF A C12 
1112 C C11 . A1BPF B .   ? 0.4702 0.3777 0.4295 0.0264  0.0971  -0.0251 201 A1BPF A C11 
1113 O O2  . A1BPF B .   ? 0.5202 0.4233 0.4434 0.0298  0.0626  -0.0219 201 A1BPF A O2  
1114 C C9  . A1BPF B .   ? 0.5170 0.4100 0.4249 0.0293  0.0735  -0.0199 201 A1BPF A C9  
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