data_7HWU
# 
_entry.id   7HWU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HWU         pdb_00007hwu 10.2210/pdb7hwu/pdb 
WWPDB D_1001408030 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HWU 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                      15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S,4R)-1-[(2-methoxyphenyl)acetyl]-4-(trifluoromethyl)pyrrolidine-3-carboxamide' 330.302   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                         65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                               78.133    1  ?         ? ? ? 
5 water       nat water                                                                              18.015    91 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S,4R)-1-[(2-methoxyphenyl)acetyl]-4-(trifluoromethyl)pyrrolidine-3-carboxamide' A1BPU 
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 
A1BPU non-polymer         . '(3S,4R)-1-[(2-methoxyphenyl)acetyl]-4-(trifluoromethyl)pyrrolidine-3-carboxamide' ? 
'C15 H17 F3 N2 O3' 330.302 
ALA   'L-peptide linking' y ALANINE                                                                            ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                           ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                         ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                    ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                           ? 'C3 H7 N O2 S' 
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                               ? 'C2 H6 O S' 
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                          ? 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                    ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                            ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                          ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                              ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                         ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                            ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                             ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                         ? 'C5 H11 N O2 S' 
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                      ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                            ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                             ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                          ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                         ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                           ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                             ? 'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                         ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BPU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPU 
_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 A1BPU 1  201 201 A1BPU LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 74  HOH   HOH A . 
E 5 HOH   2  302 9   HOH   HOH A . 
E 5 HOH   3  303 15  HOH   HOH A . 
E 5 HOH   4  304 88  HOH   HOH A . 
E 5 HOH   5  305 53  HOH   HOH A . 
E 5 HOH   6  306 86  HOH   HOH A . 
E 5 HOH   7  307 24  HOH   HOH A . 
E 5 HOH   8  308 78  HOH   HOH A . 
E 5 HOH   9  309 38  HOH   HOH A . 
E 5 HOH   10 310 1   HOH   HOH A . 
E 5 HOH   11 311 90  HOH   HOH A . 
E 5 HOH   12 312 37  HOH   HOH A . 
E 5 HOH   13 313 80  HOH   HOH A . 
E 5 HOH   14 314 4   HOH   HOH A . 
E 5 HOH   15 315 54  HOH   HOH A . 
E 5 HOH   16 316 75  HOH   HOH A . 
E 5 HOH   17 317 11  HOH   HOH A . 
E 5 HOH   18 318 69  HOH   HOH A . 
E 5 HOH   19 319 73  HOH   HOH A . 
E 5 HOH   20 320 40  HOH   HOH A . 
E 5 HOH   21 321 70  HOH   HOH A . 
E 5 HOH   22 322 62  HOH   HOH A . 
E 5 HOH   23 323 55  HOH   HOH A . 
E 5 HOH   24 324 16  HOH   HOH A . 
E 5 HOH   25 325 27  HOH   HOH A . 
E 5 HOH   26 326 31  HOH   HOH A . 
E 5 HOH   27 327 12  HOH   HOH A . 
E 5 HOH   28 328 10  HOH   HOH A . 
E 5 HOH   29 329 84  HOH   HOH A . 
E 5 HOH   30 330 26  HOH   HOH A . 
E 5 HOH   31 331 79  HOH   HOH A . 
E 5 HOH   32 332 3   HOH   HOH A . 
E 5 HOH   33 333 81  HOH   HOH A . 
E 5 HOH   34 334 71  HOH   HOH A . 
E 5 HOH   35 335 68  HOH   HOH A . 
E 5 HOH   36 336 41  HOH   HOH A . 
E 5 HOH   37 337 66  HOH   HOH A . 
E 5 HOH   38 338 18  HOH   HOH A . 
E 5 HOH   39 339 28  HOH   HOH A . 
E 5 HOH   40 340 14  HOH   HOH A . 
E 5 HOH   41 341 13  HOH   HOH A . 
E 5 HOH   42 342 5   HOH   HOH A . 
E 5 HOH   43 343 25  HOH   HOH A . 
E 5 HOH   44 344 59  HOH   HOH A . 
E 5 HOH   45 345 43  HOH   HOH A . 
E 5 HOH   46 346 17  HOH   HOH A . 
E 5 HOH   47 347 42  HOH   HOH A . 
E 5 HOH   48 348 50  HOH   HOH A . 
E 5 HOH   49 349 72  HOH   HOH A . 
E 5 HOH   50 350 34  HOH   HOH A . 
E 5 HOH   51 351 65  HOH   HOH A . 
E 5 HOH   52 352 52  HOH   HOH A . 
E 5 HOH   53 353 85  HOH   HOH A . 
E 5 HOH   54 354 45  HOH   HOH A . 
E 5 HOH   55 355 6   HOH   HOH A . 
E 5 HOH   56 356 44  HOH   HOH A . 
E 5 HOH   57 357 61  HOH   HOH A . 
E 5 HOH   58 358 48  HOH   HOH A . 
E 5 HOH   59 359 29  HOH   HOH A . 
E 5 HOH   60 360 82  HOH   HOH A . 
E 5 HOH   61 361 67  HOH   HOH A . 
E 5 HOH   62 362 19  HOH   HOH A . 
E 5 HOH   63 363 22  HOH   HOH A . 
E 5 HOH   64 364 39  HOH   HOH A . 
E 5 HOH   65 365 93  HOH   HOH A . 
E 5 HOH   66 366 32  HOH   HOH A . 
E 5 HOH   67 367 96  HOH   HOH A . 
E 5 HOH   68 368 57  HOH   HOH A . 
E 5 HOH   69 369 8   HOH   HOH A . 
E 5 HOH   70 370 33  HOH   HOH A . 
E 5 HOH   71 371 91  HOH   HOH A . 
E 5 HOH   72 372 64  HOH   HOH A . 
E 5 HOH   73 373 56  HOH   HOH A . 
E 5 HOH   74 374 58  HOH   HOH A . 
E 5 HOH   75 375 30  HOH   HOH A . 
E 5 HOH   76 376 87  HOH   HOH A . 
E 5 HOH   77 377 76  HOH   HOH A . 
E 5 HOH   78 378 94  HOH   HOH A . 
E 5 HOH   79 379 92  HOH   HOH A . 
E 5 HOH   80 380 77  HOH   HOH A . 
E 5 HOH   81 381 35  HOH   HOH A . 
E 5 HOH   82 382 51  HOH   HOH A . 
E 5 HOH   83 383 63  HOH   HOH A . 
E 5 HOH   84 384 20  HOH   HOH A . 
E 5 HOH   85 385 7   HOH   HOH A . 
E 5 HOH   86 386 89  HOH   HOH A . 
E 5 HOH   87 387 21  HOH   HOH A . 
E 5 HOH   88 388 23  HOH   HOH A . 
E 5 HOH   89 389 95  HOH   HOH A . 
E 5 HOH   90 390 47  HOH   HOH A . 
E 5 HOH   91 391 2   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           7HWU 
_cell.length_a           72.798 
_cell.length_b           61.422 
_cell.length_c           32.683 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.88 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWU 
_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          7HWU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.43 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HWU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.35 
_reflns.d_resolution_high            1.52 
_reflns.number_obs                   22147 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.095 
_reflns.pdbx_netI_over_sigmaI        9.5 
_reflns.pdbx_redundancy              6.8 
_reflns.pdbx_Rrim_I_all              0.103 
_reflns.pdbx_Rpim_I_all              0.039 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     149798 
_reflns.pdbx_chi_squared             0.80 
_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                  1.52 
_reflns_shell.d_res_low                   1.60 
_reflns_shell.number_measured_all         18339 
_reflns_shell.number_unique_obs           3216 
_reflns_shell.Rmerge_I_obs                1.645 
_reflns_shell.pdbx_chi_squared            0.67 
_reflns_shell.pdbx_redundancy             5.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.815 
_reflns_shell.pdbx_Rpim_I_all             0.755 
_reflns_shell.pdbx_CC_half                0.419 
_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                                 7HWU 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     22046 
_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                             16.32 
_refine.ls_d_res_high                            1.521 
_refine.ls_percent_reflns_obs                    99.6 
_refine.ls_R_factor_obs                          0.2073 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2054 
_refine.ls_R_factor_R_free                       0.2469 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.500 
_refine.ls_number_reflns_R_free                  992 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.B_iso_mean                               32.16 
_refine.aniso_B[1][1]                            -0.56930 
_refine.aniso_B[2][2]                            0.45820 
_refine.aniso_B[3][3]                            0.11110 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.04330 
_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             0.082 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.087 
_refine.pdbx_overall_SU_R_Blow_DPI               0.083 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.088 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWU 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             91 
_refine_hist.number_atoms_total               1193 
_refine_hist.d_res_high                       1.521 
_refine_hist.d_res_low                        16.32 
# 
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                  0.011 ? 2.00  1131 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.97  ? 2.00  1541 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1131 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.06  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.59 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  954  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   50 
_refine_ls_shell.d_res_high                       1.52 
_refine_ls_shell.d_res_low                        1.53 
_refine_ls_shell.number_reflns_R_work             433 
_refine_ls_shell.R_factor_R_work                  0.3274 
_refine_ls_shell.percent_reflns_obs               91.84 
_refine_ls_shell.R_factor_R_free                  0.2412 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.78 
_refine_ls_shell.number_reflns_R_free             17 
_refine_ls_shell.number_reflns_all                450 
_refine_ls_shell.R_factor_all                     0.3240 
# 
_struct.entry_id                  7HWU 
_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-0034420-001 (A71EV2A-x3990)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWU 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HWU 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.155 ? ? 
# 
_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_555 112.1 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.9 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.9 ? 
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_555 108.0 ? 
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_555 101.5 ? 
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_555 112.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7HWU 
_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             -93.69 
_pdbx_validate_torsion.psi             30.98 
# 
_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         15.1477 
_pdbx_refine_tls.origin_y         7.1417 
_pdbx_refine_tls.origin_z         14.2338 
_pdbx_refine_tls.T[1][1]          -0.0408 
_pdbx_refine_tls.T[2][2]          -0.0334 
_pdbx_refine_tls.T[3][3]          -0.0273 
_pdbx_refine_tls.T[1][2]          -0.0004 
_pdbx_refine_tls.T[1][3]          -0.0178 
_pdbx_refine_tls.T[2][3]          -0.0117 
_pdbx_refine_tls.L[1][1]          1.5105 
_pdbx_refine_tls.L[2][2]          7.0359 
_pdbx_refine_tls.L[3][3]          0.9617 
_pdbx_refine_tls.L[1][2]          2.4908 
_pdbx_refine_tls.L[1][3]          -0.6722 
_pdbx_refine_tls.L[2][3]          -2.2184 
_pdbx_refine_tls.S[1][1]          -0.0893 
_pdbx_refine_tls.S[1][2]          0.0503 
_pdbx_refine_tls.S[1][3]          0.0592 
_pdbx_refine_tls.S[2][1]          0.2823 
_pdbx_refine_tls.S[2][2]          0.1273 
_pdbx_refine_tls.S[2][3]          -0.1728 
_pdbx_refine_tls.S[3][1]          -0.0585 
_pdbx_refine_tls.S[3][2]          -0.0959 
_pdbx_refine_tls.S[3][3]          -0.0379 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BPU N1   N  N N 1   
A1BPU C4   C  Y N 2   
A1BPU C5   C  Y N 3   
A1BPU C6   C  Y N 4   
A1BPU C7   C  N N 5   
A1BPU C8   C  N N 6   
A1BPU C10  C  N R 7   
A1BPU C13  C  N N 8   
A1BPU F2   F  N N 9   
A1BPU F    F  N N 10  
A1BPU F1   F  N N 11  
A1BPU C12  C  N R 12  
A1BPU C11  C  N N 13  
A1BPU O2   O  N N 14  
A1BPU C9   C  N N 15  
A1BPU C14  C  N N 16  
A1BPU N    N  N N 17  
A1BPU O1   O  N N 18  
A1BPU C1   C  Y N 19  
A1BPU O    O  N N 20  
A1BPU C    C  N N 21  
A1BPU C3   C  Y N 22  
A1BPU C2   C  Y N 23  
A1BPU H14  H  N N 24  
A1BPU H13  H  N N 25  
A1BPU H7   H  N N 26  
A1BPU H8   H  N N 27  
A1BPU H9   H  N N 28  
A1BPU H10  H  N N 29  
A1BPU H    H  N N 30  
A1BPU H1   H  N N 31  
A1BPU H12  H  N N 32  
A1BPU H11  H  N N 33  
A1BPU H16  H  N N 34  
A1BPU H15  H  N N 35  
A1BPU H3   H  N N 36  
A1BPU H2   H  N N 37  
A1BPU H4   H  N N 38  
A1BPU H6   H  N N 39  
A1BPU H5   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 
A1BPU C   O    sing N N 1   
A1BPU O   C1   sing N N 2   
A1BPU C1  C2   doub Y N 3   
A1BPU C2  C3   sing Y N 4   
A1BPU C3  C4   doub Y N 5   
A1BPU C4  C5   sing Y N 6   
A1BPU C5  C6   doub Y N 7   
A1BPU C1  C6   sing Y N 8   
A1BPU C6  C7   sing N N 9   
A1BPU C7  C8   sing N N 10  
A1BPU O1  C8   doub N N 11  
A1BPU C8  N    sing N N 12  
A1BPU N   C9   sing N N 13  
A1BPU C9  C10  sing N N 14  
A1BPU C11 C10  sing N N 15  
A1BPU N1  C11  sing N N 16  
A1BPU O2  C11  doub N N 17  
A1BPU C10 C12  sing N N 18  
A1BPU C12 C13  sing N N 19  
A1BPU F   C13  sing N N 20  
A1BPU F1  C13  sing N N 21  
A1BPU C13 F2   sing N N 22  
A1BPU C14 C12  sing N N 23  
A1BPU N   C14  sing N N 24  
A1BPU N1  H14  sing N N 25  
A1BPU N1  H13  sing N N 26  
A1BPU C4  H7   sing N N 27  
A1BPU C5  H8   sing N N 28  
A1BPU C7  H9   sing N N 29  
A1BPU C7  H10  sing N N 30  
A1BPU C10 H    sing N N 31  
A1BPU C12 H1   sing N N 32  
A1BPU C9  H12  sing N N 33  
A1BPU C9  H11  sing N N 34  
A1BPU C14 H16  sing N N 35  
A1BPU C14 H15  sing N N 36  
A1BPU C   H3   sing N N 37  
A1BPU C   H2   sing N N 38  
A1BPU C   H4   sing N N 39  
A1BPU C3  H6   sing N N 40  
A1BPU C2  H5   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HWU 
_atom_sites.fract_transf_matrix[1][1]   0.013737 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000691 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016281 
_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]   0.030636 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.956 6.515   24.215 1.00 35.99 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.137 6.613   23.359 1.00 36.26 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.193 5.464   22.346 1.00 34.21 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.498 4.456   22.516 1.00 34.24 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.403 6.640   24.218 1.00 40.40 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.592 5.362   24.804 1.00 45.63 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.003 5.636   21.305 1.00 31.99 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.195 4.629   20.272 1.00 30.88 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.564 5.190   18.911 1.00 29.90 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.203 6.326   18.589 1.00 30.72 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.270 4.399   18.095 1.00 28.56 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.688 4.816   16.757 1.00 28.18 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.679 3.639   15.761 1.00 27.50 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.748 2.483   16.180 1.00 28.36 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.105 5.403   16.833 1.00 28.54 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.654 3.943   14.450 1.00 25.73 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.780 2.974   13.363 1.00 25.39 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.157 3.186   12.722 1.00 28.46 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.527 4.308   12.402 1.00 28.52 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.692 3.206   12.281 1.00 23.90 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.281 3.163   12.906 1.00 21.49 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.848 2.184   11.130 1.00 24.95 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.235 3.769   11.938 1.00 21.62 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.926 2.102   12.549 1.00 30.61 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.246 2.189   11.939 1.00 32.35 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.198 1.445   10.621 1.00 34.00 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.020 0.232   10.605 1.00 35.33 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.302 1.584   12.881 1.00 32.99 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.435 2.354   14.173 1.00 33.60 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.250 3.474   14.257 1.00 34.74 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.689 2.010   15.288 1.00 34.11 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.361 4.202   15.435 1.00 35.41 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.749 2.763   16.455 1.00 34.87 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.613 3.836   16.534 1.00 35.64 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.698 4.560   17.692 1.00 35.93 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.299 2.162   9.522  1.00 34.80 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.212 1.577   8.186  1.00 36.15 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.302 2.188   7.299  1.00 37.65 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.339 3.401   7.075  1.00 38.24 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.782 1.768   7.592  1.00 37.24 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.325 3.229   7.709  1.00 36.64 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.733 1.305   6.146  1.00 38.67 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.234 1.356   6.839  1.00 38.25 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.362 1.830   6.045  1.00 39.94 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.186 2.872   6.792  1.00 42.69 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.439 2.697   7.985  1.00 44.83 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.498 4.005   6.160  1.00 42.00 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.261 5.065   6.842  1.00 42.54 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.314 6.115   7.481  1.00 39.79 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.692 7.280   7.640  1.00 39.66 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.260 5.699   5.900  1.00 46.43 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.453 4.807   5.639  1.00 53.91 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.817 3.954   6.458  1.00 55.51 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.110 4.990   4.501  1.00 56.71 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.113 5.676   7.910  1.00 37.43 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.121 6.577   8.507  1.00 35.19 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.602 6.131   9.876  1.00 32.53 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.473 4.930   10.167 1.00 31.86 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.897 6.719   7.572  1.00 34.58 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.217 7.315   6.223  1.00 35.75 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.801 8.571   6.116  1.00 37.26 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.919 6.633   5.051  1.00 36.68 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.130 9.112   4.879  1.00 38.41 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.214 7.176   3.805  1.00 38.18 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.805 8.426   3.723  1.00 39.74 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.078 8.985   2.496  1.00 42.45 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.216 7.130   10.686 1.00 29.90 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.586 6.918   11.976 1.00 27.84 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.287 7.746   11.933 1.00 25.18 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.328 8.938   11.682 1.00 25.04 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.501 7.361   13.118 1.00 29.12 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.832 7.560   14.477 1.00 30.64 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.894 7.854   15.539 1.00 33.72 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.482 8.885   16.489 1.00 35.04 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.969 8.642   17.691 1.00 37.45 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.819 7.394   18.119 1.00 37.61 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.632 9.647   18.491 1.00 36.42 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.131 7.092   12.124 1.00 22.97 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.815 7.762   12.113 1.00 22.29 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.333 7.888   13.548 1.00 21.36 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.206 6.867   14.223 1.00 22.20 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.764 6.979   11.311 1.00 23.11 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.477 7.816   11.169 1.00 22.38 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.310 6.528   9.957  1.00 23.21 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.990 9.106   14.008 1.00 19.57 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.537 9.283   15.392 1.00 19.98 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.334 10.262  15.394 1.00 19.20 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.117 10.990  14.418 1.00 19.42 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.683 9.872   16.289 1.00 22.42 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.794 8.846   16.514 1.00 25.05 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.225 11.168  15.690 1.00 22.14 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.589 10.341  16.524 1.00 18.61 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.564 11.379  16.688 1.00 18.26 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.311 12.717  16.682 1.00 19.24 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.343 12.860  17.381 1.00 20.43 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.857 11.281  18.048 1.00 18.70 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.995 10.059  18.124 1.00 20.00 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.479 8.998   18.523 1.00 22.12 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.718 10.162  17.711 1.00 19.46 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.833 13.658  15.884 1.00 18.58 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.491 14.977  15.818 1.00 18.52 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.583 15.637  17.210 1.00 20.70 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.617 16.242  17.517 1.00 22.20 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.749 15.868  14.813 1.00 18.83 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.487 17.169  14.453 1.00 18.74 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.520 18.058  13.656 1.00 18.91 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.154 19.285  13.122 1.00 19.14 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.238 20.422  13.798 1.00 23.07 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.857 20.479  15.073 1.00 22.78 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.731 21.513  13.214 1.00 24.13 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.539 15.502  18.054 1.00 21.31 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.570 16.136  19.387 1.00 23.64 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.587 15.504  20.380 1.00 26.15 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.940 16.121  21.400 1.00 28.08 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.174 16.223  20.013 1.00 24.69 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.622 14.921  20.495 1.00 25.97 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.944 14.067  19.640 1.00 27.36 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.607 14.394  21.745 1.00 26.89 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.552 13.041  20.392 1.00 28.26 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.940 13.186  21.663 1.00 28.35 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.090 14.320  20.042 1.00 25.96 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.055 13.591  20.852 1.00 27.02 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.482 13.605  20.247 1.00 28.01 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.389 13.010  20.844 1.00 29.32 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.525 12.138  21.107 1.00 27.36 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.199 12.073  21.908 1.00 29.63 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.749 10.608  22.172 1.00 30.79 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.306 12.826  23.245 1.00 30.80 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.684 14.249  19.047 1.00 26.94 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.991 14.284  18.396 1.00 27.56 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.024 14.956  19.310 1.00 29.19 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.680 15.907  19.986 1.00 29.81 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.920 15.042  17.081 1.00 26.90 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.259 14.469  19.311 1.00 30.83 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.357 14.995  20.153 1.00 32.66 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.209 16.078  19.419 1.00 33.60 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.023 16.280  18.226 1.00 32.05 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.260 13.819  20.536 1.00 35.35 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.894 13.350  19.348 1.00 37.02 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.521 12.711  21.233 1.00 36.55 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.234 16.708  20.100 1.00 35.86 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.100 17.667  19.401 1.00 38.19 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.821 16.998  18.226 1.00 37.62 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.946 17.595  17.159 1.00 37.64 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.137 18.298  20.355 1.00 41.92 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.529 19.098  21.457 1.00 48.91 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.789 20.233  21.197 1.00 52.17 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.636 18.941  22.801 1.00 52.12 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.447 20.719  22.381 1.00 53.81 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.941 19.981  23.378 1.00 53.88 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.241 15.733  18.423 1.00 37.21 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.933 14.923  17.430 1.00 37.21 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.030 14.698  16.223 1.00 34.49 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.454 14.888  15.084 1.00 34.81 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.342 13.588  18.052 1.00 40.62 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.993 13.748  19.399 1.00 51.05 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.183 13.547  19.539 1.00 54.90 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.216 14.094  20.430 1.00 53.22 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.747 14.362  16.457 1.00 32.10 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.783 14.231  15.361 1.00 30.08 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.700 15.497  14.524 1.00 28.65 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.833 15.421  13.309 1.00 29.28 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.390 13.859  15.883 1.00 29.67 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.273 12.416  16.329 1.00 31.08 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.840 11.540  15.652 1.00 33.38 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.633 12.168  17.372 1.00 31.51 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.538 16.672  15.167 1.00 27.91 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.413 17.945  14.443 1.00 28.54 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.737 18.360  13.727 1.00 31.23 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.686 18.966  12.659 1.00 31.45 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.959 19.041  15.424 1.00 27.97 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.482 19.074  15.613 1.00 26.97 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.772 18.543  16.647 1.00 27.91 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.523 19.592  14.686 1.00 26.15 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.430 18.807  16.476 1.00 27.42 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.242 19.354  15.230 1.00 26.69 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.621 20.175  13.416 1.00 26.31 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.067 19.790  14.594 1.00 25.76 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.456 20.578  12.773 1.00 26.22 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.197 20.366  13.358 1.00 25.29 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.898 17.977  14.284 1.00 32.73 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.198 18.289  13.655 1.00 34.46 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.497 17.385  12.445 1.00 35.83 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.400 17.685  11.668 1.00 37.45 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.335 18.171  14.673 1.00 34.99 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.781 16.243  12.315 1.00 34.01 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.924 15.314  11.186 1.00 33.04 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.558 15.169  10.475 1.00 30.86 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.197 14.081  10.019 1.00 29.45 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.402 13.952  11.699 1.00 34.67 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.813 14.056  12.227 1.00 40.21 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.730 14.370  11.471 1.00 42.20 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.006 13.793  13.522 1.00 40.97 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.808 16.263  10.423 1.00 30.14 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.480 16.275  9.846  1.00 28.47 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.479 15.923  8.358  1.00 29.59 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.249 16.500  7.590  1.00 31.61 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.888 17.673  10.049 1.00 27.29 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.491 17.894  9.437  1.00 26.04 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.433 17.036  10.157 1.00 25.52 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.098 19.383  9.535  1.00 25.08 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.556 15.021  7.942  1.00 27.51 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.327 14.656  6.544  1.00 27.51 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.959 15.256  6.080  1.00 26.65 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.831 15.828  4.982  1.00 27.33 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.327 13.111  6.420  1.00 29.07 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.823 12.660  5.053  1.00 29.63 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.729 12.563  6.697  1.00 29.76 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.940 15.142  6.949  1.00 24.01 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.588 15.603  6.634  1.00 22.67 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.758 15.644  7.922  1.00 21.21 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.889 14.766  8.779  1.00 20.84 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.939 14.599  5.647  1.00 23.27 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.465 14.787  5.383  1.00 23.78 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.881 15.613  4.466  1.00 25.40 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.402 14.057  6.003  1.00 22.99 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.507 15.437  4.479  1.00 25.20 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.189 14.504  5.432  1.00 23.83 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.361 13.081  7.005  1.00 23.12 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.953 13.982  5.807  1.00 23.30 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.130 12.565  7.377  1.00 23.07 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.945 13.028  6.791  1.00 22.52 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.876 16.617  8.018  1.00 20.10 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.936 16.668  9.145  1.00 20.09 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.621 17.268  8.662  1.00 20.22 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.600 18.097  7.736  1.00 20.18 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.482 17.474  10.324 1.00 21.30 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.049 18.841  9.933  1.00 21.26 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.041 19.974  9.845  1.00 23.97 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.304 20.961  9.117  1.00 28.21 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.986 19.888  10.508 1.00 22.31 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.533 16.849  9.297  1.00 19.44 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.233 17.391  8.968  1.00 19.46 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.444 17.567  10.280 1.00 19.29 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.017 16.592  10.888 1.00 19.54 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.537 16.511  7.918  1.00 21.40 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.207 17.060  7.426  1.00 25.63 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.532 17.752  8.203  1.00 26.79 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.814 16.746  6.262  1.00 26.36 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.290 18.823  10.721 1.00 19.54 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.583 19.118  11.947 0.50 21.03 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.575 19.113  11.957 0.50 21.08 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.118 18.623  11.881 1.00 22.22 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.578 18.162  12.879 1.00 23.44 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.616 20.618  12.213 0.50 23.23 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.596 20.610  12.260 0.50 23.40 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.838 20.919  13.352 0.50 25.15 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.068 21.348  11.170 0.50 25.64 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.481 18.731  10.700 1.00 21.58 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.092 18.297  10.562 1.00 22.99 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.947 16.775  10.726 1.00 21.98 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.858 16.323  11.048 1.00 23.87 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.496 18.751  9.237  1.00 27.37 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.949 17.940  8.167  1.00 30.79 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.040 16.004  10.548 1.00 18.66 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.985 14.530  10.721 1.00 18.30 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.597 14.065  12.048 1.00 17.35 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.506 12.876  12.385 1.00 17.39 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.745 13.840  9.558  1.00 18.02 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.073 14.104  8.210  1.00 17.80 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.864 13.444  7.072  1.00 19.76 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.836 11.974  7.170  1.00 19.21 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.015 11.149  6.132  1.00 20.36 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.143 11.636  4.901  1.00 21.62 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.968 9.823   6.309  1.00 19.92 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.244 14.966  12.791 1.00 17.51 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.000 14.635  14.005 1.00 16.75 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.112 13.640  13.671 1.00 16.17 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.429 12.795  14.502 1.00 16.98 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.112 14.120  15.164 1.00 17.45 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.869 13.837  16.468 1.00 19.47 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.746 14.645  16.832 1.00 20.04 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.616 12.754  17.103 1.00 20.84 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.761 13.764  12.464 1.00 15.42 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.894 12.872  12.124 1.00 15.18 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.180 13.679  11.887 1.00 16.69 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.133 14.775  11.336 1.00 18.29 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.639 12.115  10.813 1.00 14.90 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.562 10.994  10.936 1.00 16.43 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.411 10.263  9.572  1.00 17.60 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.949 9.942   11.982 1.00 17.30 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.314 13.031  12.148 1.00 15.67 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.614 13.602  11.828 1.00 17.90 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.504 12.403  11.472 1.00 19.30 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.441 11.354  12.132 1.00 20.78 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.207 14.363  13.012 1.00 18.91 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.597 14.998  12.756 1.00 20.68 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.716 16.305  13.496 1.00 22.15 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.741 14.103  13.228 1.00 23.20 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.321 12.541  10.408 1.00 19.58 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.248 11.503  9.974  1.00 21.17 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.656 12.129  10.019 1.00 23.21 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.866 13.264  9.530  1.00 24.16 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.949 10.973  8.561  1.00 22.39 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.021 9.963   8.110  1.00 23.34 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.565 10.326  8.532  1.00 21.52 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.549 11.435  10.700 1.00 24.26 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.953 11.861  10.798 1.00 26.56 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.852 10.792  10.174 1.00 29.58 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.455 9.631   10.030 1.00 28.42 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.358 12.155  12.241 1.00 27.11 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.211 11.026  13.095 1.00 29.04 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.097 11.178  9.818  1.00 32.38 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.022 10.212  9.229  1.00 36.23 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.838 9.483   10.303 1.00 40.84 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.073 10.015  11.388 1.00 41.63 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.936 10.898  8.224  1.00 38.01 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.679 11.906  8.888  1.00 42.83 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.241 8.245   10.010 1.00 43.47 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.026 7.419   10.920 1.00 47.47 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.276 6.948   10.184 1.00 52.26 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.289 6.892   8.952  1.00 52.96 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.220 6.186   11.392 1.00 48.57 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.086 5.246   10.320 1.00 50.11 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.851 6.545   11.947 1.00 47.92 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.316 6.585   10.932 1.00 55.36 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.542 6.050   10.338 1.00 58.98 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.435 4.526   10.142 1.00 61.27 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.085 3.976   9.247  1.00 63.36 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.776 6.448   11.179 1.00 61.43 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.504 6.145   12.550 1.00 63.78 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.103 7.907   11.061 1.00 62.22 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.668 3.837   11.006 1.00 60.80 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.475 2.390   10.938 1.00 61.39 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.261 2.062   10.063 1.00 61.42 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.340 2.873   9.951  1.00 60.90 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.263 1.832   12.338 1.00 61.79 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.250 0.869   9.454  1.00 61.62 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.146 0.470   8.582  1.00 61.92 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.036 -0.244  9.355  1.00 60.10 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.263 -1.309  9.923  1.00 60.70 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.666 -0.419  7.438  1.00 65.58 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.832 -0.326  6.162  1.00 71.67 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.337 0.756   5.235  1.00 78.11 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.533 1.095   5.221  1.00 81.34 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.442 1.325   4.432  1.00 77.86 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.849 0.351   9.353  1.00 57.68 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.649 -0.164  10.002 1.00 56.28 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.074 -1.362  9.273  1.00 54.06 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.221 -1.481  8.051  1.00 54.04 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.406 -2.241  10.008 1.00 51.86 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.891 -3.457  9.403  1.00 50.84 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.371 -3.623  9.529  1.00 46.98 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.879 -4.736  9.316  1.00 47.84 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.650 -4.674  9.926  1.00 55.04 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.805 -4.741  11.736 1.00 66.49 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.615 -2.528  9.816  1.00 42.78 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.149 -2.630  9.875  1.00 40.40 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.620 -2.619  8.446  1.00 38.22 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.188 -1.963  7.560  1.00 39.05 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.498 -1.435  10.622 1.00 41.65 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.360 -1.542  12.128 1.00 45.99 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.750 -2.532  12.606 1.00 47.75 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.798 -0.602  12.834 1.00 45.57 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.549 -3.330  8.219  1.00 35.27 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.897 -3.384  6.920  1.00 34.69 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.634 -2.540  6.999  1.00 31.44 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.818 -2.792  7.877  1.00 31.43 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.524 -4.849  6.638  1.00 38.87 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.718 -5.486  6.196  1.00 41.54 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.456 -5.002  5.559  1.00 39.09 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.445 -1.589  6.071  1.00 29.09 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.228 -0.793  6.061  1.00 27.29 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.178 -1.513  5.222  1.00 26.90 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.488 -2.004  4.108  1.00 27.83 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.481 0.628   5.528  1.00 27.00 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.618 1.336   6.320  1.00 27.59 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.171 1.455   5.543  1.00 26.01 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.281 1.581   7.825  1.00 27.85 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.969 -1.636  5.762  1.00 24.73 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.851 -2.243  5.040  1.00 23.46 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.449 -1.326  3.865  1.00 24.06 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.414 -0.108  4.031  1.00 23.02 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.644 -2.422  5.989  1.00 22.42 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.085 -1.936  2.698  1.00 25.30 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.594 -1.182  1.527  1.00 27.66 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.276 -1.880  1.192  1.00 29.33 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.289 -2.877  0.455  1.00 31.25 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.594 -1.258  0.367  1.00 29.57 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.986 -0.689  0.733  1.00 30.56 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.049 0.810   1.134  1.00 31.37 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.424 1.230   1.462  1.00 31.26 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.738 2.352   2.112  1.00 32.16 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.794 3.212   2.463  1.00 29.38 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.005 2.635   2.386  1.00 31.47 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.160 -1.397  1.783  1.00 28.94 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.866 -2.069  1.754  1.00 29.13 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.709  -1.125  2.205  1.00 30.58 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.944  0.030   2.570  1.00 29.94 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.956 -3.262  2.697  1.00 28.12 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.117 -2.778  4.446  1.00 25.98 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.459  -1.656  2.201  1.00 30.99 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.288  -0.962  2.725  1.00 31.88 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.667  -1.772  3.871  1.00 30.77 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.462  -1.708  4.095  1.00 31.52 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.234  -0.614  1.630  1.00 35.76 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.558  -1.785  0.981  1.00 42.99 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.899  -2.937  1.324  1.00 43.59 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.673  -1.558  0.113  1.00 49.05 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.487  -2.532  4.642  1.00 28.26 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.991  -3.269  5.806  1.00 26.42 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.264  -2.317  6.766  1.00 25.04 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.665  -1.153  6.935  1.00 24.05 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.142  -3.965  6.541  1.00 25.80 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.728  -5.505  5.784  1.00 28.72 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.209  -2.811  7.377  1.00 23.76 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.505  -2.104  8.429  1.00 23.06 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.453  -2.925  9.698  1.00 21.18 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.637  -2.657  10.573 1.00 21.31 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.102  -1.638  7.998  1.00 25.46 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.114  -0.413  7.084  1.00 30.00 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.681  0.019   6.780  1.00 34.69 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.175  -0.139  5.658  1.00 38.75 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.968  0.489   7.803  1.00 33.45 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.314  -3.974  9.805  1.00 19.69 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.453  -4.749  11.027 1.00 19.10 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.945  -4.948  11.278 1.00 17.80 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.769  -5.001  10.336 1.00 18.02 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.720  -6.104  11.008 1.00 23.43 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.370  -6.997  10.103 1.00 25.32 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.240  -5.975  10.643 1.00 24.69 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.295  -4.968  12.556 1.00 16.66 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.691  -5.149  12.933 1.00 16.38 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.847  -5.240  14.441 1.00 14.78 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.869  -5.477  15.153 1.00 15.54 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.079 -5.144  14.913 1.00 14.62 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.387 -5.246  16.352 1.00 14.85 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.271 -4.071  16.733 1.00 15.13 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.253 -3.794  16.038 1.00 14.97 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.117 -6.597  16.597 1.00 16.07 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.599 -6.723  18.055 1.00 17.76 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.181 -7.745  16.246 1.00 16.45 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.969 -3.432  17.877 1.00 14.80 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.857 -2.353  18.364 1.00 14.08 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.396 -2.628  19.744 1.00 15.72 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.797 -3.379  20.508 1.00 16.08 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.179 -0.955  18.317 1.00 14.17 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.199 -0.684  19.435 1.00 15.35 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.942  -1.281  19.449 1.00 16.98 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.525 0.172   20.482 1.00 16.92 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.996  -0.948  20.423 1.00 18.08 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.612  0.448   21.507 1.00 18.97 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.352  -0.131  21.485 1.00 19.43 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.435  0.139   22.480 1.00 21.87 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.540 -2.022  20.066 1.00 15.09 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.131 -2.179  21.393 1.00 16.89 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.659 -1.027  22.254 1.00 17.62 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.793 0.158   21.843 1.00 17.53 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.672 -2.153  21.337 1.00 17.81 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.250 -2.326  22.727 1.00 19.70 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.020 -3.484  23.452 1.00 21.20 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.902 -1.280  23.368 1.00 22.50 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.535 -3.656  24.742 1.00 24.31 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.430 -1.436  24.648 1.00 24.78 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.223 -2.616  25.341 1.00 26.66 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.705 -2.726  26.629 1.00 30.85 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.144 -1.353  23.456 1.00 18.84 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.640 -0.326  24.387 1.00 20.62 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.523 -0.319  25.645 1.00 23.37 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.391 -1.200  26.511 1.00 24.26 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.179 -0.625  24.713 1.00 22.77 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.477 0.375   26.055 1.00 25.04 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.462 0.642   25.723 1.00 23.65 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.397 0.672   26.845 1.00 25.57 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.728 0.802   28.199 1.00 26.21 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.218 0.200   29.165 1.00 28.47 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.457 1.755   26.679 1.00 30.66 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.853 3.027   26.590 1.00 37.31 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.612 1.553   28.285 1.00 25.14 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.889 1.723   29.578 1.00 26.49 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.219 0.433   30.104 1.00 28.19 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.706 0.432   31.230 1.00 31.26 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.859 2.839   29.479 1.00 27.70 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.815 2.485   28.589 1.00 27.89 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.227 -0.636  29.302 1.00 27.58 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.718 -1.919  29.751 1.00 27.84 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.783 -3.023  29.570 1.00 29.40 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.474 -4.184  29.862 1.00 31.40 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.453 -2.298  28.938 1.00 28.39 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.234  -1.405  29.189 1.00 30.32 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.597  -1.716  30.530 1.00 31.00 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.390  -0.925  30.763 1.00 35.16 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.377  0.265   31.362 1.00 38.30 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.512  0.828   31.766 1.00 37.33 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.232  0.909   31.543 1.00 38.76 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.997 -2.705  29.014 1.00 28.70 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.046 -3.685  28.660 1.00 30.24 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.449 -4.873  27.878 1.00 29.18 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.720 -6.060  28.165 1.00 29.97 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.836 -4.167  29.893 1.00 32.94 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.811 -3.142  30.458 1.00 38.62 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.623 -3.781  31.579 1.00 45.15 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.224 -2.788  32.461 1.00 52.61 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.028 -2.738  33.775 1.00 57.63 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.237 -3.627  34.373 1.00 58.50 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.599 -1.784  34.501 1.00 59.34 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.578 -4.550  26.901 1.00 26.32 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.878 -5.589  26.151 1.00 25.91 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.655 -5.161  24.716 1.00 23.27 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.555 -3.956  24.423 1.00 23.34 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.465 -5.806  26.749 1.00 28.37 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.351 -6.776  27.918 1.00 35.73 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.893  -6.816  28.399 1.00 43.02 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.637  -7.915  29.421 1.00 48.51 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.043  -7.403  30.688 1.00 51.43 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.469 -6.142  23.840 1.00 20.32 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.087 -5.849  22.454 1.00 18.78 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.585 -6.117  22.341 1.00 19.97 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.030 -7.069  22.960 1.00 22.12 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.834 -6.766  21.465 1.00 19.50 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.329 -6.607  21.472 1.00 20.20 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.994 -5.889  20.479 1.00 22.75 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.248 -7.125  22.312 1.00 21.57 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.278 -5.961  20.780 1.00 21.71 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.485 -6.674  21.869 1.00 24.07 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.895  -5.299  21.541 1.00 17.45 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.455  -5.483  21.349 1.00 17.35 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.125  -5.566  19.863 1.00 16.15 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.619  -4.769  19.065 1.00 15.80 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.655  -4.282  21.919 1.00 17.70 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.649  -4.208  23.432 1.00 20.37 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.871  -5.081  24.195 1.00 22.38 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.361  -3.227  24.101 1.00 22.47 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.828  -4.984  25.594 1.00 24.93 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.378  -3.166  25.497 1.00 23.64 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.610  -4.042  26.239 1.00 25.93 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.582  -3.902  27.627 1.00 29.16 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.247  -6.505  19.484 1.00 16.54 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.753  -6.542  18.091 1.00 17.67 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.668  -5.438  17.948 1.00 19.14 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.861  -5.246  18.867 1.00 21.26 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.102  -7.935  17.982 1.00 19.38 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.690  -8.273  19.386 1.00 19.78 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.620  -7.551  20.341 1.00 18.00 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.635  -4.760  16.809 1.00 18.80 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.684  -3.671  16.559 1.00 20.37 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.200  -3.638  15.122 1.00 19.60 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.949  -3.987  14.205 1.00 20.56 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.329  -2.272  16.836 1.00 22.55 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.405  -1.941  18.320 1.00 24.72 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.673  -2.103  16.135 1.00 22.37 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.988  -3.100  14.922 1.00 18.98 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.461  -2.700  13.626 1.00 20.66 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.634  -1.172  13.619 1.00 21.40 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.462  -0.550  14.676 1.00 23.56 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.973  -3.013  13.504 1.00 24.15 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.799  -4.418  13.547 1.00 30.29 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.146  -0.611  12.526 1.00 19.71 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.415  0.835   12.494 1.00 19.23 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.900  1.459   11.243 1.00 21.58 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.716  0.782   10.209 1.00 23.79 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.916  1.159   12.746 1.00 18.63 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.893  0.429   11.841 1.00 17.54 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.402  -0.807  12.202 1.00 17.54 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.309  0.992   10.634 1.00 18.61 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.332  -1.467  11.389 1.00 18.08 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.243  0.332   9.823  1.00 19.01 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.726  -0.912  10.197 1.00 19.06 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.624  2.785   11.300 1.00 22.00 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.053  3.468   10.160 1.00 23.14 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.112  3.793   9.060  1.00 24.22 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.306  3.639   9.284  1.00 23.53 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.337  4.734   10.641 1.00 25.25 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.315  5.641   11.136 1.00 26.78 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.671  4.202   7.847  1.00 25.91 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.617  4.600   6.792  1.00 27.57 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.241  5.934   7.173  1.00 27.63 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.598  6.729   7.843  1.00 28.89 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.900  4.724   5.417  1.00 32.63 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.560  3.344   4.838  1.00 40.11 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.814  3.455   3.516  1.00 48.58 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.262  2.351   2.592  1.00 54.55 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 3.738  2.410   2.408  1.00 57.60 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.471  6.225   6.712  1.00 25.99 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.102  7.515   7.076  1.00 27.28 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.258  8.708   6.643  1.00 28.58 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.782  8.762   5.488  1.00 28.75 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.430  7.522   6.312  1.00 28.54 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.669  6.144   5.873  1.00 29.49 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.348  5.386   5.878  1.00 26.00 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.018  9.637   7.578  1.00 29.33 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.175  10.789  7.261  1.00 31.25 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.488  12.012  8.164  1.00 30.37 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.360  11.932  9.044  1.00 28.56 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.699  10.379  7.320  1.00 35.64 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.301  10.021  8.628  1.00 41.39 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.815  13.164  7.897  1.00 30.92 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.959  14.395  8.668  1.00 32.78 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.017  14.289  9.840  1.00 34.86 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.783  14.221  9.640  1.00 36.97 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.498  15.616  7.831  1.00 34.12 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.492  16.215  6.892  1.00 38.08 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.795  17.145  5.903  1.00 40.33 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.559  16.992  7.659  1.00 38.80 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.558  14.331  11.054 1.00 34.40 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.788  14.205  12.274 1.00 36.55 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.090  15.354  13.248 1.00 38.64 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.253  15.717  13.434 1.00 37.50 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.092  12.817  12.888 1.00 37.64 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.538  11.691  11.986 1.00 39.06 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.577  12.707  14.308 1.00 38.96 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.010  10.381  12.276 1.00 40.40 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.035  15.949  13.862 1.00 41.16 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.261  17.014  14.836 1.00 44.76 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.973  16.493  16.101 1.00 46.33 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.639  15.433  16.622 1.00 46.34 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.950  17.732  15.204 1.00 46.39 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.185  19.028  15.935 1.00 48.47 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.621  20.147  15.265 1.00 50.23 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.971  19.122  17.297 1.00 50.13 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.838  21.345  15.941 1.00 51.50 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.154  20.330  17.965 1.00 50.98 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.604  21.426  17.287 1.00 51.16 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.999  17.221  16.545 1.00 47.42 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.795  16.891  17.722 1.00 48.78 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.952  18.157  18.593 1.00 50.70 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.314  19.232  18.090 1.00 50.57 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.183  16.290  17.345 1.00 48.40 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.994  15.985  18.595 1.00 48.92 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.041  15.034  16.491 1.00 48.17 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.695  18.009  19.898 1.00 52.04 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.737  19.069  20.917 1.00 53.93 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.130  19.698  21.146 1.00 54.57 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.142  19.117  20.758 1.00 54.66 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.216  18.489  22.234 1.00 57.17 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.734  18.175  22.210 1.00 64.79 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.911  19.033  23.154 1.00 73.56 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.398  20.114  23.560 1.00 75.06 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.770  18.630  23.477 1.00 76.82 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.184  20.860  21.824 1.00 54.28 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.445  21.547  22.123 1.00 55.30 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.393  20.744  23.049 1.00 56.25 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.948  19.855  23.775 1.00 56.91 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.159  22.925  22.725 1.00 55.71 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.697  21.076  23.024 1.00 56.05 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.738 20.441  23.832 1.00 56.37 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.947 21.404  24.027 1.00 56.84 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.997 22.482  23.419 1.00 57.34 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.194 19.138  23.164 1.00 57.41 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 12.015 19.383  22.034 1.00 58.74 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.934 21.010  24.856 1.00 56.34 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 14.158 21.806  25.018 1.00 56.58 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.986 21.884  23.711 1.00 54.83 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.951 22.644  23.636 1.00 55.07 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 15.035 21.206  26.133 1.00 61.00 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.500 21.430  27.540 1.00 68.89 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.265 22.459  28.349 1.00 80.68 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.417 22.772  27.973 1.00 84.45 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 14.708 22.969  29.350 1.00 83.73 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.610 21.086  22.689 1.00 53.06 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.302 20.985  21.417 1.00 51.55 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.460 21.540  20.245 1.00 48.03 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.030 22.099  19.311 1.00 47.89 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.727 19.524  21.140 1.00 52.40 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.995 18.658  22.362 1.00 53.95 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.272 18.545  22.896 1.00 55.28 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.984 17.899  22.935 1.00 55.04 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.532 17.708  23.978 1.00 56.35 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.230 17.067  24.018 1.00 56.40 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.506 16.971  24.537 1.00 57.89 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.736 16.133  25.611 1.00 60.88 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.123 21.395  20.282 1.00 45.25 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.273 21.896  19.185 1.00 43.18 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.022 22.656  19.611 1.00 44.77 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.381 22.268  20.584 1.00 45.27 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.756 20.724  18.334 1.00 39.60 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.813 19.801  17.800 1.00 35.19 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.656 20.199  16.771 1.00 34.11 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.917 18.497  18.262 1.00 34.07 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.614 19.341  16.255 1.00 32.47 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.844 17.615  17.726 1.00 32.10 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.682 18.034  16.714 1.00 31.45 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.665 17.199  16.244 1.00 26.28 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.547 23.628  18.800 1.00 45.32 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.211  24.204  19.077 1.00 46.07 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.106  23.246  18.546 1.00 47.23 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.421  22.244  17.877 1.00 47.55 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.237  25.529  18.311 1.00 46.67 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.217 25.299  17.171 1.00 46.74 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.136 24.154  17.547 1.00 44.87 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.817  23.548  18.793 1.00 47.58 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.720  22.726  18.273 1.00 47.59 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.768  22.715  16.732 1.00 46.03 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.862  23.777  16.129 1.00 46.62 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.388  23.279  18.752 1.00 48.34 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.849  21.519  16.109 1.00 43.82 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.980  21.453  14.650 1.00 41.98 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.456  20.127  14.065 1.00 40.62 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.088  19.224  14.807 1.00 41.06 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.471  21.668  14.258 1.00 41.20 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.325  20.375  14.388 1.00 40.10 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.715  20.578  14.931 1.00 38.53 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.619 19.467  14.578 1.00 38.01 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.649 18.294  15.205 1.00 37.01 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.515 17.356  14.833 1.00 31.66 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.815  18.048  16.209 1.00 38.56 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.443  20.019  12.733 1.00 39.29 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.162  18.760  12.084 1.00 38.43 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.515  18.093  11.895 1.00 34.05 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.447  18.706  11.352 1.00 33.59 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.534  18.950  10.709 1.00 40.84 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.097  19.409  10.775 1.00 44.60 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.054  18.496  10.789 1.00 46.92 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.782  20.758  10.807 1.00 47.03 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.728  18.918  10.831 1.00 49.40 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.466  21.192  10.852 1.00 48.87 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.441  20.269  10.865 1.00 50.71 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.864 20.705  10.900 1.00 54.40 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.641  16.868  12.390 1.00 30.17 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.855  16.088  12.148 1.00 26.58 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.535  15.222  10.920 1.00 24.86 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.482  14.577  10.866 1.00 26.46 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.238  15.236  13.373 1.00 26.13 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.415  14.258  13.070 1.00 24.87 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.150 13.816  14.324 1.00 24.69 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.304 14.568  15.288 1.00 24.72 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.632 12.590  14.333 1.00 22.43 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.410  15.219  9.923  1.00 22.43 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.183  14.449  8.698  1.00 22.01 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.857  13.069  8.787  1.00 21.73 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.706  12.829  9.662  1.00 21.35 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.738  15.212  7.490  1.00 22.90 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.134 15.407  7.604  1.00 24.26 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.421  12.162  7.900  1.00 21.53 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.955  10.813  7.793  1.00 20.90 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.844  10.034  9.112  1.00 20.31 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.737  9.261   9.445  1.00 20.19 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.403 10.876  7.309  1.00 20.53 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.550 11.525  5.950  1.00 24.52 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.523 10.768  4.786  1.00 27.45 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.690 12.831  5.614  1.00 27.13 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.688 11.626  3.785  1.00 28.66 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.794 12.879  4.233  1.00 28.73 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.789  10.283  9.864  1.00 20.78 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.579  9.634   11.157 1.00 20.67 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.512  8.512   11.049 1.00 20.04 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.504  8.674   10.359 1.00 21.14 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.108  10.711  12.158 1.00 22.07 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.956  10.305  13.623 1.00 23.65 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.322  9.977   14.214 1.00 23.08 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.300  11.474  14.435 1.00 26.52 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.752  7.406   11.771 1.00 18.85 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.811  6.250   11.750 1.00 19.17 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.377  6.003   13.163 1.00 19.94 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.248  5.897   14.030 1.00 19.71 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.582  5.010   11.254 1.00 18.57 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.070  5.212   9.822  1.00 22.42 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.184  3.960   9.228  1.00 25.29 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.593  4.128   10.411 1.00 21.67 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.065  5.878   13.419 1.00 20.29 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.592  5.640   14.781 1.00 21.51 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.179  4.189   14.979 1.00 21.49 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.679  3.540   14.063 1.00 22.24 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.336  6.538   15.114 1.00 23.95 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.615  8.026   15.239 1.00 28.05 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.334  8.758   15.707 1.00 28.83 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.704  8.290   16.270 1.00 29.15 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.291  3.737   16.205 1.00 20.40 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.848  2.396   16.595 1.00 20.85 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.277  2.503   18.009 1.00 22.28 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.584  3.452   18.732 1.00 22.70 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.051  1.449   16.606 1.00 21.20 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.445  1.541   18.399 1.00 22.01 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.966  1.449   19.761 1.00 24.16 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.036  0.674   20.562 1.00 26.66 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.337  -0.498  20.275 1.00 27.12 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.403 0.741   19.843 1.00 26.49 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.839 0.621   21.289 1.00 28.02 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.441 1.524   19.057 1.00 26.42 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.614  1.348   21.533 1.00 27.55 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.660  0.745   22.340 1.00 28.45 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.240  1.703   23.343 1.00 28.32 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.047  2.918   23.251 1.00 29.16 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.981  1.148   24.291 1.00 26.70 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.613  1.932   25.313 1.00 27.01 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.863  2.657   24.865 1.00 26.95 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.753  2.082   24.240 1.00 26.20 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.937  1.061   26.536 1.00 27.81 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.435  1.868   27.687 1.00 31.25 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.615  2.770   28.334 1.00 34.10 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.687  1.983   28.184 1.00 33.13 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.379  3.367   29.244 1.00 35.48 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.634  2.916   29.192 1.00 35.23 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.968  3.906   25.273 1.00 28.25 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.158  4.699   25.057 1.00 29.90 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.218  5.800   26.112 1.00 33.06 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.185  6.206   26.661 1.00 35.33 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.221  5.265   23.644 1.00 30.68 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.143  6.153   23.420 1.00 34.25 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.442  6.189   26.465 1.00 32.94 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.817  7.259   27.385 1.00 33.47 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.934 8.070   26.691 1.00 33.55 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.557 7.568   25.750 1.00 32.27 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.238 6.688   28.744 1.00 35.69 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.037  6.151   29.504 1.00 41.11 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.310  5.389   30.791 1.00 45.24 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.091 5.894   31.624 1.00 46.89 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.742  4.287   30.967 1.00 45.33 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.180 9.343   27.066 1.00 34.72 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.178 10.151  26.314 1.00 34.26 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.552 9.485   26.110 1.00 33.66 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.116 9.527   24.996 1.00 33.63 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.265 11.445  27.126 1.00 35.33 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.918 11.556  27.778 1.00 36.26 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.492 10.135  28.100 1.00 34.77 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.062 8.828   27.155 1.00 32.67 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.331 8.103   27.081 1.00 31.77 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.336 6.922   26.110 1.00 28.95 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.383 6.306   25.861 1.00 28.85 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.146 6.523   25.623 1.00 26.56 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.049 5.455   24.640 1.00 24.31 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.462 5.890   23.242 1.00 22.27 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.631 5.021   22.381 1.00 20.56 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.654 4.822   24.567 1.00 24.42 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.364 4.008   25.797 1.00 26.94 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.294 3.384   26.311 1.00 26.61 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.217 4.060   26.284 1.00 29.18 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.632 7.210   22.990 1.00 22.67 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.070 7.658   21.645 1.00 21.98 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.377 6.997   21.249 1.00 21.63 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.273 6.834   22.097 1.00 22.20 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.192 9.175   21.590 1.00 23.16 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.610 10.034  21.586 1.00 26.44 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.454 6.564   20.009 1.00 19.97 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.644 5.874   19.531 1.00 20.79 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.467 4.362   19.458 1.00 20.36 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.251 3.671   18.793 1.00 20.63 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.445 3.816   20.134 1.00 18.93 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.156 2.382   20.013 1.00 17.68 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.828 2.028   18.565 1.00 17.20 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.090 2.758   17.903 1.00 17.17 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.410 0.939   18.065 1.00 16.52 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.228 0.576   16.668 1.00 15.89 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.948 -0.212  16.430 1.00 16.17 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.598 -1.114  17.231 1.00 17.03 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.491 -0.203  16.179 1.00 18.47 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.669 0.785   15.999 1.00 20.57 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.234 -1.012  14.899 1.00 20.72 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.021 0.050   15.787 1.00 22.80 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.284 0.103   15.294 1.00 14.76 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.119 -0.676  14.813 1.00 13.88 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.642 -1.493  13.605 1.00 14.73 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.307 -0.925  12.721 1.00 15.55 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.044 0.299   14.282 1.00 14.45 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.860 -0.355  13.540 1.00 15.47 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.066 -1.285  14.491 1.00 16.70 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.929  0.789   12.966 1.00 16.67 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.397 -2.807  13.589 1.00 15.70 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.867 -3.651  12.506 1.00 17.18 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.741 -4.502  11.997 1.00 17.43 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.884 -4.932  12.746 1.00 17.18 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.917 -4.645  13.055 1.00 19.26 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.152 -4.033  13.669 1.00 25.85 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.038 -5.173  14.206 1.00 30.18 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.702 -5.772  13.057 1.00 37.30 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.883 -5.377  12.593 1.00 38.95 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.609 -4.491  13.268 1.00 38.00 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.363 -5.892  11.478 1.00 39.09 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.827 -4.848  10.717 1.00 17.93 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.921 -5.834  10.097 1.00 20.06 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.834 -6.967  9.544  1.00 22.96 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.048 -6.928  9.760  1.00 24.23 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.105 -5.168  8.992  1.00 20.32 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.115 -4.592  7.584  1.00 21.25 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.269 -7.976  8.838  1.00 25.47 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.086 -9.075  8.305  1.00 28.11 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.177 -8.606  7.303  1.00 29.71 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.144 -9.351  7.040  1.00 32.76 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.171 -10.122 7.626  1.00 32.09 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.492 -9.562  6.360  1.00 37.76 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.460 -10.509 5.769  1.00 45.92 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.243  -10.240 5.790  1.00 48.39 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.931 -11.628 5.218  1.00 46.08 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.026 -7.404  6.739  1.00 28.04 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.969 -6.874  5.748  1.00 28.12 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.131 -6.066  6.344  1.00 27.33 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.089 -5.734  5.629  1.00 29.18 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.225 -6.046  4.672  1.00 29.49 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.045 -6.762  4.061  1.00 32.21 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.749 -6.363  4.321  1.00 33.94 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.013 -7.755  3.130  1.00 34.61 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.962 -7.191  3.646  1.00 36.38 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.677 -8.049  2.909  1.00 36.40 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.024 -5.702  7.633  1.00 24.56 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.065 -4.902  8.256  1.00 22.77 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.517 -3.743  9.071  1.00 20.18 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.383 -3.783  9.534  1.00 19.93 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.318 -2.708  9.233  1.00 19.64 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.967 -1.543  10.036 1.00 19.09 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.950 -0.680  9.324  1.00 18.39 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.219 -0.235  8.191  1.00 19.38 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.240 -0.724  10.395 1.00 20.18 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.848 0.565   11.088 1.00 18.74 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.184 -1.542  11.287 1.00 20.85 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.830 -0.360  10.013 1.00 16.73 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.795 0.510   9.455  1.00 16.40 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.926 1.981   9.931  1.00 17.17 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.710 2.913   9.162  1.00 17.51 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.403 -0.057  9.869  1.00 17.41 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.288 0.895   9.450  1.00 19.07 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.178 -1.445  9.270  1.00 17.93 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.156 2.152   11.233 1.00 15.60 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.243 3.508   11.792 1.00 16.03 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.662 3.517   13.243 1.00 15.11 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.069 2.479   13.769 1.00 15.10 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.530 4.671   13.897 1.00 14.63 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.903 4.752   15.302 1.00 14.85 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.852 5.502   16.087 1.00 15.87 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.185 6.367   15.544 1.00 15.60 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.263 5.464   15.487 1.00 16.52 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.289 6.804   14.779 1.00 18.07 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.430 4.582   15.114 1.00 19.14 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.593 7.658   15.231 1.00 21.13 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.651 5.115   17.367 1.00 15.03 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.667 5.814   18.183 1.00 15.14 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.978 7.336   18.230 1.00 15.88 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.125 7.719   18.486 1.00 16.76 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.608 5.239   19.619 1.00 16.38 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.642 6.063   20.455 1.00 17.62 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.182 3.760   19.623 1.00 17.50 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.954 8.174   18.028 1.00 16.03 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.122 9.612   18.040 1.00 18.14 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.047 10.328  18.866 1.00 20.97 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.311 11.430  19.389 1.00 22.77 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.133 10.146  16.610 1.00 20.35 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.232 11.563  16.597 1.00 21.03 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.841  9.737   18.964 1.00 22.05 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.745  10.373  19.736 1.00 24.08 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.977  9.330   20.579 1.00 26.52 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.147  8.126   20.395 1.00 24.99 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.772  11.147  18.785 1.00 25.74 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.866  10.231  18.166 1.00 27.11 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.477  12.031  17.737 1.00 25.06 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.076  9.795   21.452 1.00 28.78 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.220  8.890   22.198 1.00 32.22 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.219  9.601   23.075 1.00 35.55 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.976  10.787  22.896 1.00 36.83 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.696  8.867   24.038 1.00 37.41 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.725  9.352   25.011 1.00 40.36 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.343  8.817   24.708 1.00 43.00 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.028  8.576   23.546 1.00 43.60 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.486  8.684   25.738 1.00 44.17 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.102  8.235   25.567 1.00 45.35 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.056 6.782   25.055 1.00 42.85 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.130 6.412   24.565 1.00 43.98 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.674 9.228   24.671 1.00 49.02 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.763 10.630  25.230 1.00 55.29 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.941 10.835  26.438 1.00 57.91 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.683 11.633  24.360 1.00 55.96 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.945  5.933   25.281 1.00 39.43 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.888  4.555   24.820 1.00 36.72 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.208  4.429   23.337 1.00 33.80 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.875  3.420   22.715 1.00 34.55 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.874  5.438   22.777 1.00 31.02 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.305  5.467   21.385 1.00 28.40 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.830  5.570   21.340 1.00 26.44 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.441  6.139   22.244 1.00 28.18 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.715  6.696   20.668 1.00 29.25 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.178  6.749   20.549 1.00 32.81 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.281 8.156   20.142 1.00 34.84 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.330 5.702   19.542 1.00 33.48 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.416  5.117   20.237 1.00 22.40 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.835  5.264   20.005 1.00 20.09 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.997  5.654   18.526 1.00 19.52 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.314  5.086   17.669 1.00 20.58 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.663  4.001   20.386 1.00 20.32 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.177  2.734   19.676 1.00 21.03 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.146  4.220   20.088 1.00 19.62 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.811  6.664   18.274 1.00 18.56 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.071  7.161   16.928 1.00 17.20 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.504  6.921   16.490 1.00 17.48 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.443  7.097   17.270 1.00 18.21 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.682  6.479   15.242 1.00 16.24 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.004 6.112   14.715 1.00 15.72 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.329 6.984   13.514 1.00 15.99 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.510  7.143   12.608 1.00 16.76 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.012 4.653   14.185 1.00 14.92 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.526  3.675   15.233 1.00 15.39 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.408 3.139   16.171 1.00 15.81 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.213  3.196   15.214 1.00 16.05 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.957  2.250   17.144 1.00 15.91 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.771  2.300   16.182 1.00 16.38 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.656  1.801   17.123 1.00 16.15 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.519 7.553   13.524 1.00 15.20 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.024 8.281   12.376 1.00 14.62 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.498 7.255   11.321 1.00 13.72 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.415 6.448   11.578 1.00 14.41 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.203 9.142   12.808 1.00 14.02 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.851 7.266   10.139 1.00 14.08 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.210 6.317   9.089  1.00 15.09 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.586 6.638   8.489  1.00 17.46 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.975 7.818   8.375  1.00 18.19 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.163 6.427   7.954  1.00 18.80 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.358 5.412   6.853  1.00 25.56 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.511 4.233   7.169  1.00 23.23 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.449 5.827   5.663  1.00 29.08 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.336 5.576   8.086  1.00 16.47 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.606 5.808   7.373  1.00 17.27 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.638 5.046   6.043  1.00 19.33 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.654 5.105   5.358  1.00 20.77 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.877 5.471   8.206  1.00 17.82 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.939 6.294   9.500  1.00 17.82 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.924 3.966   8.534  1.00 18.14 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.558 4.294   5.691  1.00 18.72 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.544 3.465   4.482  1.00 18.44 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.631 4.241   3.170  1.00 22.95 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.024 3.662   2.147  1.00 26.21 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.301 2.558   4.466  1.00 19.25 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.243 1.627   5.642  1.00 22.02 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.927 0.905   5.611  1.00 21.30 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.793 1.754   5.998  1.00 21.96 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.554  1.312   6.173  1.00 23.70 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.241  0.061   5.864  1.00 22.42 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.610  2.126   6.629  1.00 23.67 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.242 5.526   3.192  1.00 22.87 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.302 6.327   1.969  1.00 24.87 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.715 6.893   1.723  1.00 24.76 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 15.961 7.421   0.617  1.00 26.51 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.268 7.474   2.017  1.00 27.37 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.572 8.503   3.089  1.00 31.32 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.929 8.098   4.211  1.00 31.30 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.449 9.712   2.802  1.00 30.97 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.655 6.813   2.717  1.00 23.61 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.030 7.362   2.586  1.00 24.10 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.950 6.399   1.829  1.00 26.26 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.786 5.700   2.421  1.00 26.31 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.601 7.733   3.978  1.00 23.48 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.696 8.704   4.802  1.00 22.51 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.217 8.892   6.239  1.00 22.11 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.463 10.044  4.066  1.00 23.00 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.712 6.290   0.514  1.00 27.26 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.409 5.297   -0.294 1.00 30.02 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.922 5.492   -0.314 1.00 32.55 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.673 4.513   -0.435 1.00 33.80 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.850 5.252   -1.735 1.00 31.23 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.342 5.185   -1.934 1.00 33.77 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.012 5.003   -3.431 1.00 36.13 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.679 4.063   -1.051 1.00 33.75 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.380 6.757   -0.155 1.00 32.97 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.798 7.065   -0.150 1.00 32.51 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.549 6.454   1.034  1.00 34.08 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.764 6.359   0.975  1.00 35.49 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.020 8.574   -0.247 1.00 30.80 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.280 9.356   0.809  1.00 28.85 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.042 9.918   0.705  1.00 28.91 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.756 9.671   2.125  1.00 27.75 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.725 10.577  1.876  1.00 28.56 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.770 10.454  2.754  1.00 27.91 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 23.947 9.409   2.814  1.00 28.51 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.939 10.973  4.035  1.00 28.39 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.116 9.939   4.076  1.00 29.26 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.113 10.693  4.681  1.00 28.49 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.849 5.987   2.090  1.00 33.80 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.517 5.340   3.219  1.00 35.35 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.284 4.077   2.792  1.00 41.25 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.204 3.687   3.504  1.00 42.43 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.502 4.960   4.313  1.00 33.02 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.904 6.112   5.093  1.00 30.71 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.865 5.583   6.089  1.00 30.63 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.992 6.900   5.844  1.00 30.65 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.881 3.432   1.670  1.00 44.64 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.478 2.193   1.147  1.00 49.20 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.592 2.384   0.153  1.00 52.97 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.079 1.375   -0.360 1.00 54.16 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.433 1.381   0.380  1.00 51.35 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.290 0.874   1.186  1.00 55.95 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.462 0.694   2.406  1.00 57.64 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.213 0.654   0.601  1.00 58.63 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.907 3.622   -0.246 1.00 55.00 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.936 3.847   -1.263 1.00 57.66 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.930 4.941   -0.880 1.00 59.05 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.774 5.320   -1.706 1.00 60.07 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.284 4.180   -2.611 1.00 61.16 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.321 5.353   -2.533 1.00 67.22 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.184 5.271   -3.532 1.00 75.52 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.053 6.198   -4.363 1.00 77.62 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.438 4.265   -3.497 1.00 77.92 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BPU B 2 .   ? 11.225 14.255  18.142 1.00 41.89 ? 201 A1BPU A N1  1 
HETATM 1079 C  C4  . A1BPU B 2 .   ? 7.012  10.607  26.403 1.00 44.14 ? 201 A1BPU A C4  1 
HETATM 1080 C  C5  . A1BPU B 2 .   ? 7.639  11.697  25.830 1.00 44.57 ? 201 A1BPU A C5  1 
HETATM 1081 C  C6  . A1BPU B 2 .   ? 8.535  11.535  24.777 1.00 43.87 ? 201 A1BPU A C6  1 
HETATM 1082 C  C7  . A1BPU B 2 .   ? 9.224  12.735  24.167 1.00 43.82 ? 201 A1BPU A C7  1 
HETATM 1083 C  C8  . A1BPU B 2 .   ? 8.849  12.960  22.713 1.00 43.48 ? 201 A1BPU A C8  1 
HETATM 1084 C  C10 . A1BPU B 2 .   ? 10.574 15.070  20.330 1.00 45.00 ? 201 A1BPU A C10 1 
HETATM 1085 C  C13 . A1BPU B 2 .   ? 12.805 15.475  21.459 1.00 48.41 ? 201 A1BPU A C13 1 
HETATM 1086 F  F2  . A1BPU B 2 .   ? 12.291 16.437  22.231 1.00 48.73 ? 201 A1BPU A F2  1 
HETATM 1087 F  F   . A1BPU B 2 .   ? 13.348 16.087  20.394 1.00 48.42 ? 201 A1BPU A F   1 
HETATM 1088 F  F1  . A1BPU B 2 .   ? 13.812 14.939  22.150 1.00 49.56 ? 201 A1BPU A F1  1 
HETATM 1089 C  C12 . A1BPU B 2 .   ? 11.781 14.449  21.068 1.00 46.47 ? 201 A1BPU A C12 1 
HETATM 1090 C  C11 . A1BPU B 2 .   ? 10.742 15.280  18.840 1.00 44.01 ? 201 A1BPU A C11 1 
HETATM 1091 O  O2  . A1BPU B 2 .   ? 10.430 16.355  18.323 1.00 44.13 ? 201 A1BPU A O2  1 
HETATM 1092 C  C9  . A1BPU B 2 .   ? 9.445  14.087  20.633 1.00 44.87 ? 201 A1BPU A C9  1 
HETATM 1093 C  C14 . A1BPU B 2 .   ? 11.169 13.836  22.327 1.00 46.01 ? 201 A1BPU A C14 1 
HETATM 1094 N  N   . A1BPU B 2 .   ? 9.773  13.593  21.966 1.00 45.00 ? 201 A1BPU A N   1 
HETATM 1095 O  O1  . A1BPU B 2 .   ? 7.779  12.603  22.253 1.00 42.28 ? 201 A1BPU A O1  1 
HETATM 1096 C  C1  . A1BPU B 2 .   ? 8.793  10.239  24.319 1.00 43.01 ? 201 A1BPU A C1  1 
HETATM 1097 O  O   . A1BPU B 2 .   ? 9.691  10.155  23.289 1.00 41.83 ? 201 A1BPU A O   1 
HETATM 1098 C  C   . A1BPU B 2 .   ? 10.365 8.910   23.075 1.00 40.93 ? 201 A1BPU A C   1 
HETATM 1099 C  C3  . A1BPU B 2 .   ? 7.264  9.345   25.938 1.00 43.67 ? 201 A1BPU A C3  1 
HETATM 1100 C  C2  . A1BPU B 2 .   ? 8.158  9.147   24.895 1.00 43.26 ? 201 A1BPU A C2  1 
HETATM 1101 ZN ZN  . ZN    C 3 .   ? 10.931 -4.819  5.583  1.00 25.88 2 202 ZN    A ZN  1 
HETATM 1102 S  S   . DMS   D 4 .   ? 19.645 -0.368  19.989 1.00 46.84 ? 203 DMS   A S   1 
HETATM 1103 O  O   . DMS   D 4 .   ? 18.234 -0.614  19.573 1.00 44.41 ? 203 DMS   A O   1 
HETATM 1104 C  C1  . DMS   D 4 .   ? 19.814 -0.034  21.761 1.00 46.85 ? 203 DMS   A C1  1 
HETATM 1105 C  C2  . DMS   D 4 .   ? 20.346 1.203   19.388 1.00 46.69 ? 203 DMS   A C2  1 
HETATM 1106 O  O   . HOH   E 5 .   ? 3.775  7.691   3.565  1.00 39.33 ? 301 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.758 -0.145  15.228 1.00 42.51 ? 302 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 2.959  7.828   9.925  1.00 55.98 ? 303 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 9.317  18.341  19.794 1.00 46.34 ? 304 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 8.078  -3.964  0.546  1.00 29.51 ? 305 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 14.849 23.521  17.219 1.00 50.74 ? 306 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 8.888  2.314   2.896  1.00 32.62 ? 307 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 27.251 16.066  2.887  1.00 40.78 ? 308 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 3.754  -4.991  21.188 1.00 37.49 ? 309 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 20.179 8.686   18.870 1.00 23.73 ? 310 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 8.173  19.664  17.884 1.00 49.75 ? 311 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 0.979  -2.710  20.231 1.00 43.04 ? 312 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 22.503 -1.312  4.068  1.00 36.69 ? 313 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 0.523  -0.473  16.435 1.00 23.11 ? 314 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 23.519 21.724  7.930  1.00 30.29 ? 315 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 12.510 6.826   31.174 1.00 38.47 ? 316 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 10.427 8.119   4.712  1.00 36.02 ? 317 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 18.270 18.953  5.602  1.00 52.78 ? 318 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 31.125 20.239  16.865 1.00 36.44 ? 319 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 4.304  5.627   24.874 1.00 37.82 ? 320 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 30.742 20.401  10.651 1.00 38.47 ? 321 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 11.328 16.850  5.643  1.00 53.12 ? 322 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 14.351 20.755  8.604  1.00 43.45 ? 323 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 17.719 20.992  9.427  1.00 23.05 ? 324 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 11.439 1.994   33.472 1.00 27.50 ? 325 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 30.037 10.846  19.476 1.00 45.47 ? 326 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 11.202 11.427  11.503 1.00 19.04 ? 327 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 17.823 2.380   23.222 1.00 31.29 ? 328 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 6.642  -5.988  29.170 1.00 41.67 ? 329 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 10.264 4.571   3.505  1.00 27.54 ? 330 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 10.107 -5.113  31.819 1.00 45.47 ? 331 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 14.819 2.374   23.227 1.00 20.84 ? 332 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 16.027 -11.185 5.136  1.00 52.73 ? 333 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 5.317  7.310   28.444 1.00 54.39 ? 334 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 21.900 -5.747  10.279 1.00 44.50 ? 335 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 14.954 12.089  24.156 1.00 35.66 ? 336 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 17.977 23.320  21.782 1.00 32.87 ? 337 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 17.969 18.684  17.077 1.00 24.74 ? 338 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 9.854  4.142   33.840 1.00 41.63 ? 339 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 2.912  3.164   27.561 1.00 38.67 ? 340 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 5.368  -1.672  24.273 1.00 32.52 ? 341 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 13.029 10.306  9.388  1.00 17.08 ? 342 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 6.955  3.466   33.030 1.00 37.80 ? 343 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 14.781 -4.518  17.155 1.00 28.50 ? 344 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 22.856 17.903  19.041 1.00 41.61 ? 345 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 4.023  -5.304  6.534  1.00 36.83 ? 346 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 18.904 9.009   25.669 1.00 54.23 ? 347 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 18.595 12.523  1.735  1.00 45.72 ? 348 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 13.230 9.048   29.943 1.00 44.78 ? 349 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 6.677  12.629  5.581  1.00 31.74 ? 350 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 1.783  13.243  5.774  1.00 39.17 ? 351 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 15.593 -4.670  1.743  1.00 34.96 ? 352 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 19.022 -5.218  27.489 1.00 52.96 ? 353 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 0.630  0.957   24.353 1.00 40.81 ? 354 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 19.460 23.549  15.358 1.00 28.62 ? 355 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? -1.554 -4.546  15.363 0.50 36.18 ? 356 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 14.400 14.411  3.737  1.00 34.20 ? 357 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 4.178  11.178  19.223 1.00 47.32 ? 358 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 5.571  1.832   7.171  1.00 33.40 ? 359 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 0.089  3.149   6.562  1.00 48.51 ? 360 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 30.876 10.526  14.562 1.00 46.31 ? 361 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 1.546  -2.733  17.634 1.00 28.72 ? 362 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 22.239 18.766  5.822  1.00 31.70 ? 363 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 4.219  -2.562  21.608 1.00 49.94 ? 364 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 6.587  17.166  24.608 1.00 52.29 ? 365 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 21.976 8.624   21.042 1.00 34.67 ? 366 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 11.889 21.356  12.277 1.00 39.80 ? 367 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 2.404  -6.801  14.895 1.00 51.79 ? 368 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 8.791  -7.902  9.553  1.00 45.94 ? 369 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 23.889 1.986   19.394 1.00 50.65 ? 370 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 6.947  16.237  22.149 1.00 98.48 ? 371 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 4.715  -1.765  29.126 1.00 51.75 ? 372 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 7.137  -5.492  2.925  1.00 36.39 ? 373 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 16.161 23.681  14.505 1.00 53.83 ? 374 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 28.184 16.736  23.309 1.00 53.95 ? 375 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 9.195  17.013  25.133 1.00 73.97 ? 376 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 17.156 -3.407  17.974 1.00 42.21 ? 377 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 7.154  10.897  4.132  1.00 42.86 ? 378 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 3.015  9.999   28.567 1.00 65.02 ? 379 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 12.038 19.793  5.201  1.00 67.72 ? 380 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 0.385  -3.684  9.743  1.00 48.06 ? 381 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 9.108  19.352  6.656  1.00 64.08 ? 382 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 26.490 -1.956  14.683 1.00 41.87 ? 383 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 2.046  0.902   26.542 1.00 39.14 ? 384 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 20.802 21.788  17.953 1.00 35.44 ? 385 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 11.094 17.990  26.482 1.00 50.05 ? 386 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 0.927  -2.026  23.622 1.00 42.21 ? 387 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 8.840  22.519  26.666 1.00 49.33 ? 388 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 9.297  -8.752  12.549 1.00 37.20 ? 389 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 0.753  11.372  17.926 1.00 55.11 ? 390 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 20.198 -3.924  22.617 1.00 63.74 ? 391 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.6197 0.3602 0.3875 -0.0669 -0.1506 0.0085  7   SER   A N   
2    C CA  . SER   A 1   ? 0.5869 0.3650 0.4261 -0.0640 -0.1687 0.0182  7   SER   A CA  
3    C C   . SER   A 1   ? 0.5200 0.3507 0.4291 -0.0500 -0.1573 0.0202  7   SER   A C   
4    O O   . SER   A 1   ? 0.5219 0.3567 0.4223 -0.0464 -0.1465 0.0176  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6508 0.3984 0.4856 -0.0857 -0.2137 0.0363  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.7164 0.4597 0.5575 -0.0935 -0.2316 0.0480  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4589 0.3242 0.4325 -0.0433 -0.1570 0.0241  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4110 0.3161 0.4463 -0.0327 -0.1418 0.0250  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3742 0.3084 0.4534 -0.0239 -0.1238 0.0207  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3925 0.3248 0.4497 -0.0215 -0.1158 0.0131  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3292 0.2866 0.4694 -0.0196 -0.1143 0.0254  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3052 0.2828 0.4828 -0.0138 -0.0927 0.0211  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2809 0.2735 0.4905 -0.0089 -0.0647 0.0169  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2870 0.2783 0.5122 -0.0092 -0.0672 0.0220  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2924 0.2700 0.5220 -0.0180 -0.1104 0.0355  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2534 0.2547 0.4696 -0.0065 -0.0383 0.0082  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2412 0.2447 0.4786 -0.0059 -0.0070 0.0028  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2588 0.2633 0.5591 -0.0052 0.0069  0.0095  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2576 0.2643 0.5616 -0.0058 0.0045  0.0102  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2397 0.2418 0.4267 -0.0093 0.0132  -0.0110 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2253 0.2292 0.3619 -0.0091 0.0001  -0.0142 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2543 0.2458 0.4480 -0.0139 0.0467  -0.0178 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2395 0.2451 0.3370 -0.0141 0.0097  -0.0206 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2685 0.2706 0.6238 -0.0035 0.0238  0.0158  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2667 0.2679 0.6944 -0.0017 0.0442  0.0243  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2951 0.2792 0.7175 -0.0035 0.0941  0.0109  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3129 0.2886 0.7407 -0.0032 0.1098  0.0085  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2451 0.2530 0.7553 0.0008  0.0243  0.0476  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2530 0.2665 0.7573 -0.0035 -0.0276 0.0622  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2558 0.2731 0.7912 -0.0059 -0.0446 0.0735  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2767 0.2853 0.7339 -0.0074 -0.0580 0.0633  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2717 0.2844 0.7893 -0.0140 -0.0925 0.0860  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2971 0.2980 0.7299 -0.0154 -0.1021 0.0741  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2970 0.2981 0.7592 -0.0197 -0.1203 0.0858  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3173 0.3016 0.7465 -0.0315 -0.1642 0.0964  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3153 0.2888 0.7181 -0.0078 0.1189  0.0015  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3508 0.2951 0.7277 -0.0152 0.1677  -0.0131 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3604 0.2919 0.7782 -0.0162 0.2001  -0.0114 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3709 0.3094 0.7724 -0.0182 0.1883  -0.0115 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4016 0.3350 0.6782 -0.0267 0.1646  -0.0289 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3990 0.3490 0.6441 -0.0274 0.1352  -0.0276 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4475 0.3400 0.6819 -0.0410 0.2112  -0.0430 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3545 0.2666 0.8323 -0.0140 0.2431  -0.0086 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3636 0.2609 0.8932 -0.0137 0.2809  -0.0052 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3633 0.2944 0.9643 -0.0051 0.2455  0.0154  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3640 0.3221 1.0174 0.0021  0.2055  0.0335  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3590 0.2865 0.9503 -0.0086 0.2532  0.0131  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3354 0.2921 0.9889 -0.0026 0.2174  0.0326  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3182 0.2944 0.8994 -0.0053 0.1642  0.0285  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3077 0.2963 0.9027 -0.0051 0.1427  0.0360  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3739 0.3173 1.0728 -0.0033 0.2561  0.0355  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4369 0.3681 1.2434 0.0032  0.3026  0.0489  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4285 0.3743 1.3064 0.0104  0.2892  0.0657  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4760 0.3778 1.3009 0.0003  0.3600  0.0434  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3112 0.2887 0.8223 -0.0076 0.1444  0.0180  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3003 0.2910 0.7456 -0.0094 0.1028  0.0137  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2653 0.2687 0.7019 -0.0062 0.0632  0.0203  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2540 0.2544 0.7021 -0.0046 0.0694  0.0212  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3278 0.3038 0.6822 -0.0182 0.1181  -0.0054 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3544 0.3109 0.6929 -0.0264 0.1515  -0.0127 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3634 0.3287 0.7237 -0.0251 0.1426  -0.0066 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3921 0.3157 0.6861 -0.0381 0.1917  -0.0258 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3902 0.3347 0.7347 -0.0337 0.1746  -0.0127 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4287 0.3252 0.6966 -0.0496 0.2234  -0.0326 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4357 0.3444 0.7297 -0.0468 0.2146  -0.0259 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4897 0.3695 0.7536 -0.0594 0.2457  -0.0323 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2392 0.2512 0.6456 -0.0067 0.0253  0.0231  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2221 0.2363 0.5995 -0.0067 -0.0096 0.0266  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2152 0.2275 0.5141 -0.0082 -0.0164 0.0132  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2169 0.2302 0.5042 -0.0092 -0.0213 0.0119  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2237 0.2395 0.6433 -0.0092 -0.0479 0.0463  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2642 0.2696 0.6305 -0.0141 -0.0857 0.0481  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2920 0.2902 0.6989 -0.0226 -0.1261 0.0710  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3369 0.3144 0.6801 -0.0313 -0.1574 0.0696  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3926 0.3470 0.6834 -0.0398 -0.1829 0.0714  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3919 0.3462 0.6911 -0.0403 -0.1856 0.0763  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4100 0.3362 0.6375 -0.0492 -0.2042 0.0684  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2035 0.2136 0.4559 -0.0081 -0.0146 0.0048  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2152 0.2249 0.4068 -0.0087 -0.0190 -0.0040 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2143 0.2169 0.3802 -0.0075 -0.0451 -0.0007 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2263 0.2252 0.3921 -0.0075 -0.0508 0.0018  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2367 0.2460 0.3954 -0.0116 0.0011  -0.0129 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2414 0.2536 0.3554 -0.0130 -0.0044 -0.0162 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2356 0.2380 0.4084 -0.0173 0.0310  -0.0173 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2034 0.1989 0.3414 -0.0078 -0.0579 -0.0015 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2270 0.2032 0.3289 -0.0095 -0.0770 -0.0001 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2329 0.2033 0.2932 -0.0066 -0.0687 -0.0073 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2293 0.2122 0.2963 -0.0047 -0.0576 -0.0097 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2598 0.2185 0.3735 -0.0166 -0.1049 0.0102  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2743 0.2379 0.4395 -0.0201 -0.1174 0.0232  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2500 0.2127 0.3785 -0.0167 -0.1050 0.0107  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2468 0.1944 0.2658 -0.0074 -0.0732 -0.0093 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2563 0.1924 0.2453 -0.0041 -0.0620 -0.0138 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2719 0.1970 0.2622 -0.0071 -0.0715 -0.0129 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2946 0.2003 0.2812 -0.0152 -0.0928 -0.0086 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2894 0.1904 0.2307 -0.0063 -0.0606 -0.0165 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3034 0.2140 0.2425 -0.0029 -0.0499 -0.0170 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3303 0.2392 0.2711 -0.0070 -0.0615 -0.0145 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2915 0.2141 0.2338 0.0041  -0.0293 -0.0177 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2564 0.1939 0.2554 -0.0024 -0.0591 -0.0143 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2582 0.1860 0.2594 -0.0048 -0.0667 -0.0136 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3167 0.1982 0.2716 -0.0113 -0.0760 -0.0161 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3415 0.2072 0.2947 -0.0193 -0.0952 -0.0129 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2517 0.1973 0.2666 0.0009  -0.0514 -0.0134 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2477 0.1908 0.2734 -0.0011 -0.0580 -0.0121 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2421 0.1982 0.2781 0.0039  -0.0435 -0.0096 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2399 0.1978 0.2896 0.0023  -0.0484 -0.0077 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3039 0.2355 0.3370 0.0024  -0.0497 -0.0098 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3252 0.2199 0.3205 0.0019  -0.0457 -0.0151 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3107 0.2469 0.3593 0.0012  -0.0535 -0.0073 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3464 0.2014 0.2617 -0.0101 -0.0618 -0.0209 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4150 0.2122 0.2708 -0.0199 -0.0651 -0.0253 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4664 0.2337 0.2933 -0.0362 -0.0959 -0.0207 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5271 0.2405 0.2993 -0.0511 -0.1084 -0.0218 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4492 0.2187 0.2701 -0.0148 -0.0341 -0.0318 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4700 0.2386 0.2782 -0.0145 -0.0291 -0.0318 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4569 0.2727 0.3098 -0.0035 -0.0189 -0.0281 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5164 0.2378 0.2674 -0.0258 -0.0326 -0.0347 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4820 0.2823 0.3095 -0.0062 -0.0158 -0.0292 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5222 0.2665 0.2885 -0.0194 -0.0237 -0.0331 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4408 0.2401 0.3054 -0.0354 -0.1094 -0.0138 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4634 0.2436 0.3198 -0.0501 -0.1412 -0.0041 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4458 0.2537 0.3646 -0.0534 -0.1664 0.0089  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.4624 0.2593 0.3922 -0.0661 -0.1966 0.0224  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4646 0.2544 0.3207 -0.0472 -0.1356 -0.0036 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5257 0.2804 0.3196 -0.0465 -0.1117 -0.0138 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5365 0.3013 0.3321 -0.0446 -0.1089 -0.0120 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5917 0.2739 0.3049 -0.0655 -0.1215 -0.0162 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4052 0.2484 0.3699 -0.0427 -0.1534 0.0071  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3832 0.2518 0.4122 -0.0443 -0.1688 0.0190  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4196 0.2533 0.4362 -0.0623 -0.2058 0.0314  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4609 0.2544 0.4172 -0.0707 -0.2100 0.0253  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3540 0.2532 0.4149 -0.0333 -0.1472 0.0135  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4167 0.2629 0.4919 -0.0694 -0.2311 0.0500  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4502 0.2653 0.5256 -0.0903 -0.2746 0.0685  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4408 0.2723 0.5636 -0.0890 -0.2783 0.0746  24  THR   A C   
137  O O   . THR   A 18  ? 0.3969 0.2650 0.5559 -0.0719 -0.2464 0.0653  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4623 0.2865 0.5942 -0.0990 -0.3026 0.0915  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4340 0.3093 0.6633 -0.0835 -0.2828 0.0978  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4962 0.3056 0.5868 -0.1011 -0.3012 0.0875  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4772 0.2810 0.6043 -0.1095 -0.3204 0.0934  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4828 0.3047 0.6637 -0.1082 -0.3245 0.1016  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4209 0.2982 0.7104 -0.0925 -0.3047 0.1114  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4013 0.3046 0.7241 -0.0803 -0.2789 0.1048  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5449 0.3279 0.7201 -0.1357 -0.3781 0.1248  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6947 0.4105 0.7533 -0.1550 -0.3937 0.1138  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7595 0.4598 0.7632 -0.1476 -0.3665 0.0915  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7788 0.4342 0.7675 -0.1837 -0.4332 0.1241  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.8375 0.4670 0.7400 -0.1701 -0.3843 0.0866  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.8556 0.4527 0.7390 -0.1940 -0.4253 0.1052  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3941 0.2849 0.7347 -0.0934 -0.3130 0.1265  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3454 0.2794 0.7889 -0.0798 -0.2891 0.1364  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3076 0.2663 0.7366 -0.0590 -0.2346 0.1101  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2861 0.2690 0.7674 -0.0491 -0.2055 0.1086  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3735 0.3092 0.8609 -0.0857 -0.3083 0.1560  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5202 0.4215 0.9980 -0.1121 -0.3696 0.1826  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5355 0.4466 1.1037 -0.1213 -0.3979 0.2144  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5997 0.4553 0.9671 -0.1270 -0.3912 0.1719  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3061 0.2544 0.6592 -0.0546 -0.2209 0.0900  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2814 0.2486 0.6128 -0.0395 -0.1767 0.0679  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2643 0.2374 0.5869 -0.0355 -0.1618 0.0591  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2546 0.2484 0.6094 -0.0277 -0.1311 0.0544  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3067 0.2596 0.5611 -0.0375 -0.1703 0.0519  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3207 0.2753 0.5850 -0.0375 -0.1721 0.0563  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3215 0.2980 0.6487 -0.0319 -0.1562 0.0624  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3527 0.2830 0.5614 -0.0438 -0.1874 0.0538  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2779 0.2276 0.5550 -0.0429 -0.1828 0.0576  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2876 0.2414 0.5553 -0.0394 -0.1706 0.0500  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2909 0.2621 0.6336 -0.0404 -0.1715 0.0640  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2857 0.2711 0.6381 -0.0343 -0.1478 0.0573  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3146 0.2322 0.5158 -0.0480 -0.1911 0.0454  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3276 0.2335 0.4637 -0.0417 -0.1718 0.0281  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3658 0.2448 0.4501 -0.0459 -0.1769 0.0235  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3157 0.2377 0.4401 -0.0307 -0.1428 0.0162  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3736 0.2500 0.4182 -0.0368 -0.1508 0.0093  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3445 0.2511 0.4185 -0.0273 -0.1312 0.0062  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2994 0.2467 0.4538 -0.0249 -0.1258 0.0150  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3336 0.2507 0.3943 -0.0182 -0.1068 -0.0018 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3028 0.2584 0.4352 -0.0179 -0.1046 0.0065  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3088 0.2516 0.4004 -0.0144 -0.0964 -0.0004 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2913 0.2611 0.6912 -0.0488 -0.1978 0.0854  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2789 0.2660 0.7646 -0.0492 -0.1968 0.1026  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2671 0.2803 0.8140 -0.0375 -0.1531 0.1011  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2616 0.2875 0.8739 -0.0352 -0.1368 0.1103  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2720 0.2484 0.8090 -0.0641 -0.2427 0.1314  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2500 0.2665 0.7758 -0.0314 -0.1323 0.0902  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2201 0.2500 0.7852 -0.0229 -0.0869 0.0851  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2198 0.2467 0.7060 -0.0185 -0.0588 0.0600  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2030 0.2306 0.6853 -0.0153 -0.0324 0.0524  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2215 0.2548 0.8412 -0.0224 -0.0907 0.0991  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2580 0.2967 0.9729 -0.0282 -0.1178 0.1297  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2567 0.3048 1.0420 -0.0254 -0.0969 0.1395  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2693 0.2994 0.9881 -0.0383 -0.1653 0.1472  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2319 0.2540 0.6591 -0.0198 -0.0668 0.0495  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2337 0.2541 0.5941 -0.0178 -0.0488 0.0317  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2461 0.2681 0.6100 -0.0185 -0.0083 0.0242  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2616 0.2837 0.6558 -0.0203 0.0066  0.0277  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2350 0.2501 0.5518 -0.0191 -0.0646 0.0273  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2379 0.2535 0.4978 -0.0179 -0.0502 0.0145  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2448 0.2564 0.4684 -0.0155 -0.0546 0.0090  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2356 0.2465 0.4708 -0.0183 -0.0619 0.0134  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2341 0.2522 0.5588 -0.0194 0.0093  0.0136  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2449 0.2526 0.5476 -0.0258 0.0452  0.0048  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2574 0.2631 0.4919 -0.0317 0.0392  -0.0027 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2771 0.2737 0.4878 -0.0406 0.0532  -0.0052 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2652 0.2646 0.5749 -0.0261 0.0672  0.0011  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2956 0.2728 0.5573 -0.0378 0.1015  -0.0101 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2459 0.2473 0.6375 -0.0208 0.0778  0.0124  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2310 0.2434 0.4379 -0.0276 0.0176  -0.0039 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2297 0.2431 0.3885 -0.0318 0.0110  -0.0063 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2131 0.2325 0.3601 -0.0235 -0.0106 -0.0055 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2061 0.2246 0.3612 -0.0189 -0.0154 -0.0061 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2522 0.2545 0.3773 -0.0429 0.0299  -0.0109 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2715 0.2761 0.3560 -0.0494 0.0188  -0.0082 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3011 0.3023 0.3617 -0.0608 0.0150  -0.0028 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2643 0.2747 0.3345 -0.0464 0.0097  -0.0076 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3041 0.3104 0.3430 -0.0653 0.0021  0.0036  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2826 0.2951 0.3278 -0.0556 0.0003  0.0000  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2616 0.2756 0.3412 -0.0375 0.0075  -0.0108 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2771 0.2962 0.3120 -0.0554 -0.0088 0.0050  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2657 0.2843 0.3266 -0.0372 0.0001  -0.0086 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2639 0.2859 0.3059 -0.0453 -0.0071 -0.0006 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2047 0.2267 0.3323 -0.0225 -0.0204 -0.0034 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2102 0.2309 0.3223 -0.0155 -0.0318 -0.0034 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2152 0.2412 0.3118 -0.0175 -0.0311 0.0014  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2128 0.2423 0.3117 -0.0233 -0.0303 0.0061  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2276 0.2372 0.3444 -0.0101 -0.0464 -0.0033 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2235 0.2323 0.3520 -0.0114 -0.0504 -0.0005 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2629 0.2703 0.3776 -0.0092 -0.0498 0.0014  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3118 0.3235 0.4367 -0.0119 -0.0496 0.0048  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2495 0.2506 0.3474 -0.0047 -0.0476 0.0008  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2089 0.2350 0.2946 -0.0132 -0.0317 0.0026  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2068 0.2396 0.2929 -0.0141 -0.0317 0.0118  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2084 0.2320 0.2924 -0.0031 -0.0287 0.0113  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2156 0.2364 0.2904 -0.0005 -0.0255 0.0088  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2313 0.2723 0.3092 -0.0260 -0.0309 0.0183  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2783 0.3285 0.3670 -0.0308 -0.0370 0.0346  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2863 0.3379 0.3938 -0.0198 -0.0351 0.0395  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2905 0.3425 0.3686 -0.0475 -0.0434 0.0440  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2130 0.2269 0.3026 0.0026  -0.0269 0.0129  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2414 0.2352 0.3226 0.0114  -0.0165 0.0109  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2421 0.2357 0.3232 0.0114  -0.0164 0.0108  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2473 0.2519 0.3449 0.0142  -0.0066 0.0212  36  SER   A C   
244  O O   . SER   A 30  ? 0.2720 0.2610 0.3578 0.0199  0.0048  0.0176  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2729 0.2510 0.3587 0.0154  -0.0117 0.0116  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2757 0.2527 0.3607 0.0156  -0.0113 0.0113  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3105 0.2607 0.3845 0.0227  0.0061  0.0091  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2862 0.2843 0.4039 0.0139  -0.0122 0.0246  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2222 0.2507 0.3470 0.0080  -0.0124 0.0361  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2273 0.2683 0.3778 0.0081  -0.0082 0.0514  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2194 0.2639 0.3520 0.0048  -0.0099 0.0470  37  SER   A C   
252  O O   . SER   A 31  ? 0.2360 0.2846 0.3863 0.0080  -0.0028 0.0564  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2655 0.3276 0.4468 -0.0031 -0.0220 0.0725  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3141 0.3840 0.4718 -0.0195 -0.0375 0.0721  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1879 0.2297 0.2913 -0.0007 -0.0169 0.0338  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1883 0.2314 0.2756 -0.0036 -0.0171 0.0288  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1899 0.2141 0.2554 0.0049  -0.0114 0.0145  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1943 0.2178 0.2488 0.0042  -0.0107 0.0110  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1879 0.2362 0.2606 -0.0172 -0.0250 0.0257  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1800 0.2378 0.2586 -0.0325 -0.0345 0.0413  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2172 0.2664 0.2672 -0.0491 -0.0358 0.0355  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2182 0.2617 0.2499 -0.0529 -0.0310 0.0289  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2472 0.2771 0.2494 -0.0712 -0.0293 0.0272  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2737 0.2919 0.2557 -0.0896 -0.0334 0.0328  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2488 0.2718 0.2364 -0.0733 -0.0230 0.0208  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2012 0.2069 0.2571 0.0101  -0.0100 0.0075  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2091 0.1900 0.2374 0.0121  -0.0122 -0.0034 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1988 0.1882 0.2276 0.0064  -0.0238 -0.0075 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2178 0.1953 0.2321 0.0061  -0.0279 -0.0115 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2309 0.1921 0.2399 0.0167  0.0001  -0.0050 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2812 0.2078 0.2507 0.0137  -0.0060 -0.0142 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3003 0.2066 0.2544 0.0099  -0.0153 -0.0179 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3066 0.2255 0.2596 0.0128  -0.0048 -0.0159 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1776 0.1839 0.2242 0.0012  -0.0273 -0.0059 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1704 0.1804 0.2260 -0.0031 -0.0307 -0.0093 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1848 0.1924 0.2569 -0.0048 -0.0369 -0.0096 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2029 0.2136 0.2787 -0.0056 -0.0362 -0.0075 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1615 0.1844 0.2204 -0.0108 -0.0221 -0.0079 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1836 0.2099 0.2306 -0.0119 -0.0185 -0.0064 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2000 0.2292 0.2393 -0.0247 -0.0118 -0.0052 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1979 0.2166 0.2427 -0.0073 -0.0203 -0.0111 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1671 0.1718 0.2565 -0.0061 -0.0419 -0.0099 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1855 0.1909 0.3037 -0.0082 -0.0463 -0.0071 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1909 0.2012 0.3412 -0.0099 -0.0384 -0.0055 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2104 0.2177 0.3614 -0.0089 -0.0421 -0.0047 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2050 0.1933 0.3201 -0.0085 -0.0673 -0.0037 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2143 0.2042 0.3671 -0.0117 -0.0763 0.0029  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2459 0.2169 0.3787 -0.0143 -0.0935 0.0043  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2332 0.2225 0.4260 -0.0147 -0.0881 0.0123  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1836 0.1984 0.3618 -0.0128 -0.0239 -0.0046 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1908 0.2056 0.4079 -0.0138 -0.0077 -0.0027 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1984 0.2148 0.4686 -0.0133 -0.0127 0.0068  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2105 0.2278 0.4795 -0.0149 -0.0124 0.0069  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2138 0.2229 0.4141 -0.0205 0.0232  -0.0102 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2136 0.2149 0.4582 -0.0210 0.0487  -0.0090 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2188 0.2267 0.3720 -0.0234 0.0229  -0.0157 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1955 0.2126 0.5137 -0.0117 -0.0217 0.0171  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2015 0.2217 0.5861 -0.0121 -0.0291 0.0316  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2174 0.2392 0.6671 -0.0101 0.0006  0.0375  43  SER   A C   
300  O O   . SER   A 37  ? 0.2066 0.2247 0.6484 -0.0088 0.0179  0.0318  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2062 0.2220 0.6018 -0.0156 -0.0721 0.0457  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2311 0.2433 0.6291 -0.0164 -0.0850 0.0510  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2285 0.2538 0.7481 -0.0098 0.0087  0.0501  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2534 0.2765 0.8466 -0.0068 0.0439  0.0575  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2830 0.3149 0.9538 -0.0053 0.0180  0.0810  44  SER   A C   
306  O O   . SER   A 38  ? 0.2887 0.3258 0.9673 -0.0098 -0.0294 0.0958  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2620 0.2821 0.8999 -0.0070 0.0736  0.0609  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3048 0.3372 0.9854 -0.0081 0.0372  0.0787  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2996 0.3284 1.0238 -0.0013 0.0484  0.0854  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3189 0.3564 1.1283 -0.0002 0.0268  0.1110  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3419 0.3794 1.2645 0.0053  0.0695  0.1261  45  THR   A C   
312  O O   . THR   A 39  ? 0.3594 0.3816 1.2712 0.0080  0.1250  0.1096  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3463 0.3794 1.1197 0.0008  0.0249  0.1035  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3694 0.3893 1.1452 0.0055  0.0827  0.0886  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3768 0.4062 1.0376 -0.0033 -0.0032 0.0856  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3407 0.3910 1.3717 0.0053  0.0452  0.1590  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3431 0.3947 1.5030 0.0120  0.0875  0.1788  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3659 0.4072 1.5550 0.0183  0.1260  0.1756  46  THR   A C   
319  O O   . THR   A 40  ? 0.3732 0.4015 1.6326 0.0253  0.1875  0.1768  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3278 0.3993 1.6069 0.0076  0.0409  0.2217  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3612 0.4389 1.6232 -0.0017 -0.0247 0.2378  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3398 0.4164 1.6079 0.0023  0.0198  0.2248  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3757 0.4196 1.5149 0.0155  0.0922  0.1728  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3794 0.4141 1.5389 0.0206  0.1218  0.1698  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4284 0.4393 1.4661 0.0206  0.1632  0.1294  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4579 0.4669 1.3889 0.0154  0.1463  0.1085  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3783 0.4260 1.5435 0.0153  0.0611  0.1891  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4316 0.4221 1.4874 0.0249  0.2160  0.1205  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4834 0.4450 1.4244 0.0206  0.2538  0.0851  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4811 0.4485 1.3537 0.0183  0.2201  0.0772  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4689 0.4400 1.3975 0.0224  0.2175  0.0905  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5293 0.4537 1.5088 0.0228  0.3335  0.0763  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6611 0.5436 1.5187 0.0118  0.3788  0.0412  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7495 0.6174 1.6009 0.0077  0.4064  0.0362  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7514 0.6286 1.7107 0.0152  0.4210  0.0567  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7947 0.6394 1.5241 -0.0055 0.4130  0.0112  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4886 0.4564 1.2464 0.0119  0.1965  0.0571  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4947 0.4665 1.1773 0.0092  0.1676  0.0475  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4884 0.4331 1.1324 0.0065  0.2111  0.0294  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5043 0.4181 1.1309 0.0019  0.2635  0.0148  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4658 0.4161 1.0887 0.0070  0.1903  0.0297  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4727 0.3961 1.0629 0.0036  0.2286  0.0144  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4597 0.3817 0.9437 -0.0037 0.2078  -0.0021 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4850 0.3886 0.9439 -0.0072 0.2276  -0.0111 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4939 0.4188 1.1785 0.0113  0.2390  0.0318  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.6086 0.5722 1.3456 0.0162  0.1675  0.0610  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4208 0.3594 0.8452 -0.0066 0.1716  -0.0057 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4206 0.3586 0.7559 -0.0132 0.1551  -0.0183 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4257 0.3321 0.6943 -0.0268 0.1900  -0.0364 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4409 0.3320 0.7110 -0.0314 0.2140  -0.0404 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4405 0.4020 0.7400 -0.0118 0.1112  -0.0149 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4841 0.4645 0.7986 -0.0058 0.0704  -0.0021 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5121 0.4914 0.8108 -0.0058 0.0655  -0.0030 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4690 0.4609 0.8017 -0.0033 0.0425  0.0082  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4129 0.3064 0.6209 -0.0357 0.1913  -0.0458 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4430 0.3008 0.5744 -0.0547 0.2154  -0.0603 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4159 0.2911 0.4877 -0.0611 0.1790  -0.0596 52  THR   A C   
358  O O   . THR   A 46  ? 0.4102 0.3079 0.4761 -0.0557 0.1504  -0.0546 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5137 0.3423 0.6208 -0.0629 0.2384  -0.0682 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5405 0.3408 0.6973 -0.0603 0.2852  -0.0708 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5609 0.3533 0.5709 -0.0875 0.2454  -0.0798 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4046 0.2666 0.4343 -0.0736 0.1822  -0.0633 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3922 0.2697 0.3752 -0.0806 0.1493  -0.0592 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4208 0.2678 0.3337 -0.1035 0.1530  -0.0637 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4618 0.2614 0.3343 -0.1223 0.1851  -0.0733 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3896 0.2702 0.3660 -0.0839 0.1446  -0.0571 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3652 0.2718 0.4114 -0.0639 0.1402  -0.0516 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3835 0.2818 0.3231 -0.0905 0.1107  -0.0494 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3459 0.2900 0.4221 -0.0469 0.1042  -0.0424 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3912 0.2596 0.2889 -0.1035 0.1228  -0.0563 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4037 0.2475 0.2399 -0.1270 0.1167  -0.0553 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4359 0.2581 0.2202 -0.1507 0.1093  -0.0514 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4074 0.2555 0.2117 -0.1430 0.0922  -0.0439 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3753 0.2536 0.2230 -0.1190 0.0845  -0.0440 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4926 0.2634 0.2054 -0.1822 0.1198  -0.0552 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.5526 0.2943 0.2040 -0.2120 0.1070  -0.0483 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5955 0.3208 0.1980 -0.2374 0.0811  -0.0374 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.6590 0.3291 0.1994 -0.2624 0.0998  -0.0464 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.6142 0.2940 0.2153 -0.2317 0.1481  -0.0634 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.6002 0.2975 0.2637 -0.2052 0.1766  -0.0721 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5804 0.3245 0.2871 -0.1892 0.1508  -0.0613 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5554 0.3113 0.3210 -0.1672 0.1771  -0.0684 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5346 0.3340 0.3533 -0.1468 0.1590  -0.0612 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4883 0.3205 0.3075 -0.1447 0.1203  -0.0486 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5051 0.3119 0.3787 -0.1298 0.1809  -0.0652 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.5646 0.3359 0.1992 -0.2307 0.0408  -0.0175 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.5738 0.3442 0.1888 -0.2480 0.0126  -0.0025 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5604 0.3801 0.2216 -0.2416 -0.0285 0.0239  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.5275 0.3792 0.2311 -0.2231 -0.0324 0.0278  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.5470 0.3306 0.1908 -0.2281 0.0271  -0.0123 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4644 0.3188 0.2038 -0.1808 0.0227  -0.0105 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5652 0.3893 0.2229 -0.2569 -0.0568 0.0429  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.5415 0.4123 0.2576 -0.2488 -0.0898 0.0703  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5015 0.4040 0.2635 -0.2277 -0.0898 0.0730  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4914 0.4175 0.2887 -0.2314 -0.1157 0.0980  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.6068 0.4584 0.2934 -0.2887 -0.1299 0.1001  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.7305 0.5421 0.3606 -0.3240 -0.1465 0.1083  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.7496 0.5463 0.3603 -0.3174 -0.1233 0.0887  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.8221 0.6148 0.4269 -0.3608 -0.1854 0.1364  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4673 0.3710 0.2353 -0.2052 -0.0604 0.0494  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4214 0.3529 0.2295 -0.1845 -0.0588 0.0508  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3662 0.3440 0.2411 -0.1616 -0.0700 0.0673  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3416 0.3338 0.2385 -0.1485 -0.0667 0.0664  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4133 0.3413 0.2255 -0.1625 -0.0281 0.0255  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4879 0.3634 0.2400 -0.1834 -0.0065 0.0077  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3332 0.3303 0.2393 -0.1574 -0.0800 0.0821  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2912 0.3246 0.2604 -0.1340 -0.0801 0.0954  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2583 0.3020 0.2446 -0.1127 -0.0637 0.0861  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2376 0.3029 0.2691 -0.0979 -0.0609 0.0986  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3033 0.3526 0.3115 -0.1487 -0.1068 0.1299  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3604 0.4084 0.3710 -0.1623 -0.1232 0.1434  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3949 0.4624 0.4610 -0.1757 -0.1518 0.1832  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4591 0.5100 0.5031 -0.2102 -0.1838 0.2043  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3441 0.4430 0.4839 -0.1508 -0.1403 0.1961  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2575 0.2823 0.2085 -0.1121 -0.0505 0.0648  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2439 0.2752 0.2068 -0.0929 -0.0363 0.0551  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2383 0.2559 0.1823 -0.0828 -0.0195 0.0316  60  THR   A C   
418  O O   . THR   A 54  ? 0.2572 0.2544 0.1732 -0.0948 -0.0148 0.0215  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3032 0.3289 0.2580 -0.1039 -0.0418 0.0612  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3530 0.3482 0.2609 -0.1224 -0.0392 0.0485  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3059 0.3450 0.2871 -0.1177 -0.0627 0.0895  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2152 0.2414 0.1765 -0.0620 -0.0102 0.0249  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2167 0.2328 0.1727 -0.0528 0.0005  0.0084  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1905 0.2115 0.1594 -0.0354 0.0033  0.0065  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1962 0.2234 0.1710 -0.0312 0.0027  0.0146  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1898 0.2038 0.1618 -0.0277 0.0061  -0.0027 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1935 0.2029 0.1677 -0.0167 0.0037  -0.0033 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1976 0.2027 0.1745 -0.0109 -0.0003 -0.0061 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1921 0.1970 0.1797 -0.0131 0.0002  -0.0105 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2098 0.2113 0.1896 -0.0177 0.0043  -0.0072 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2346 0.2266 0.2135 -0.0110 -0.0044 -0.0050 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2164 0.2193 0.1892 -0.0244 0.0081  -0.0048 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2003 0.1968 0.1651 -0.0049 -0.0022 -0.0037 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1966 0.1819 0.1566 -0.0022 -0.0088 -0.0061 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2312 0.1934 0.1726 -0.0027 -0.0190 -0.0051 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2444 0.1968 0.1695 -0.0033 -0.0169 -0.0029 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1997 0.1848 0.1537 0.0012  -0.0019 -0.0046 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2275 0.1952 0.1607 0.0051  0.0086  -0.0018 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2430 0.2186 0.1836 0.0065  0.0199  0.0044  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2670 0.2049 0.1711 0.0057  0.0095  -0.0049 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2675 0.2243 0.1950 0.0109  0.0373  0.0076  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3107 0.2219 0.1883 0.0078  0.0271  -0.0041 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3082 0.2296 0.2005 0.0115  0.0434  0.0020  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3557 0.2481 0.2273 0.0144  0.0678  0.0034  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2265 0.1776 0.1691 -0.0049 -0.0324 -0.0049 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2668 0.1892 0.1859 -0.0110 -0.0496 -0.0004 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3013 0.1936 0.1746 -0.0131 -0.0459 -0.0027 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2987 0.1929 0.1743 -0.0108 -0.0424 -0.0058 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2681 0.1908 0.2180 -0.0155 -0.0705 0.0057  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3117 0.2013 0.2354 -0.0268 -0.0960 0.0151  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3380 0.2170 0.2506 -0.0313 -0.1025 0.0206  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3641 0.2269 0.2640 -0.0358 -0.1146 0.0191  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4000 0.2426 0.2810 -0.0462 -0.1299 0.0316  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4171 0.2413 0.2830 -0.0520 -0.1431 0.0301  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4486 0.2616 0.3028 -0.0579 -0.1512 0.0367  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5310 0.2991 0.3421 -0.0782 -0.1826 0.0494  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3425 0.2020 0.1712 -0.0187 -0.0446 -0.0016 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3975 0.2146 0.1714 -0.0229 -0.0335 -0.0055 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.4655 0.2337 0.1889 -0.0405 -0.0591 -0.0009 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.4951 0.2390 0.1879 -0.0492 -0.0657 0.0032  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4326 0.2424 0.1903 -0.0173 -0.0039 -0.0076 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5083 0.2511 0.1919 -0.0238 0.0214  -0.0132 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.4769 0.2296 0.1920 -0.0480 -0.0773 0.0005  66  SER   A N   
464  C CA  . SER   A 60  ? 0.5325 0.2373 0.2019 -0.0694 -0.1102 0.0092  66  SER   A CA  
465  C C   . SER   A 60  ? 0.5938 0.2305 0.1716 -0.0844 -0.1002 0.0054  66  SER   A C   
466  O O   . SER   A 60  ? 0.6484 0.2475 0.1860 -0.1041 -0.1275 0.0152  66  SER   A O   
467  C CB  . SER   A 60  ? 0.5968 0.2948 0.2732 -0.0764 -0.1320 0.0128  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.6973 0.3776 0.3428 -0.0717 -0.1065 0.0008  66  SER   A OG  
469  N N   . SER   A 61  ? 0.5974 0.2147 0.1433 -0.0766 -0.0602 -0.0071 67  SER   A N   
470  C CA  . SER   A 61  ? 0.6701 0.2127 0.1236 -0.0909 -0.0390 -0.0129 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6983 0.2351 0.1377 -0.0922 -0.0303 -0.0100 67  SER   A C   
472  O O   . SER   A 61  ? 0.7867 0.2562 0.1447 -0.1069 -0.0135 -0.0138 67  SER   A O   
473  C CB  . SER   A 61  ? 0.6963 0.2211 0.1349 -0.0797 0.0084  -0.0252 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6566 0.2386 0.1644 -0.0560 0.0380  -0.0260 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.6447 0.2458 0.1576 -0.0786 -0.0394 -0.0040 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.6511 0.2505 0.1563 -0.0804 -0.0363 0.0001  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.6470 0.2762 0.1941 -0.0861 -0.0789 0.0135  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6700 0.3035 0.2196 -0.0872 -0.0805 0.0183  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.6241 0.2714 0.1831 -0.0578 0.0004  -0.0043 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6660 0.2859 0.2001 -0.0507 0.0473  -0.0126 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.7233 0.2754 0.1793 -0.0637 0.0694  -0.0148 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.7895 0.3138 0.2327 -0.0551 0.1226  -0.0215 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.8692 0.3324 0.2535 -0.0634 0.1445  -0.0299 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.8884 0.3131 0.2171 -0.0821 0.1129  -0.0323 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.8828 0.3219 0.2679 -0.0535 0.1989  -0.0344 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.6153 0.2689 0.2061 -0.0876 -0.1096 0.0204  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6025 0.2906 0.2558 -0.0891 -0.1431 0.0347  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5539 0.2918 0.2632 -0.0719 -0.1247 0.0325  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5565 0.2989 0.2833 -0.0766 -0.1407 0.0426  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6668 0.3068 0.2778 -0.1156 -0.1842 0.0518  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.7650 0.3629 0.3396 -0.1367 -0.2169 0.0604  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.8730 0.4270 0.4155 -0.1662 -0.2656 0.0831  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.0144 0.5024 0.4823 -0.1952 -0.2956 0.0904  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.1420 0.5481 0.4998 -0.2259 -0.3099 0.0941  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.1751 0.5586 0.4891 -0.2296 -0.2949 0.0913  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.2100 0.5506 0.4940 -0.2551 -0.3379 0.1003  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4976 0.2696 0.2329 -0.0538 -0.0918 0.0205  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4653 0.2768 0.2422 -0.0412 -0.0745 0.0182  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4011 0.2563 0.2267 -0.0271 -0.0576 0.0113  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4049 0.2583 0.2235 -0.0240 -0.0491 0.0062  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5168 0.3089 0.2524 -0.0395 -0.0477 0.0136  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6349 0.3931 0.3296 -0.0515 -0.0570 0.0201  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7452 0.4844 0.4049 -0.0477 -0.0222 0.0148  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8371 0.5466 0.4594 -0.0584 -0.0267 0.0206  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9246 0.5669 0.4627 -0.0708 -0.0074 0.0171  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3384 0.2273 0.2062 -0.0205 -0.0512 0.0112  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2967 0.2190 0.1978 -0.0120 -0.0352 0.0055  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3123 0.2419 0.2046 -0.0078 -0.0150 0.0046  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3462 0.2680 0.2263 -0.0095 -0.0122 0.0076  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2829 0.2284 0.2296 -0.0112 -0.0383 0.0059  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2832 0.2260 0.2582 -0.0138 -0.0549 0.0106  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3020 0.2581 0.3044 -0.0113 -0.0504 0.0072  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3015 0.2305 0.2877 -0.0199 -0.0763 0.0211  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2800 0.2313 0.3135 -0.0143 -0.0671 0.0158  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3172 0.2529 0.3445 -0.0201 -0.0853 0.0257  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2713 0.2168 0.1750 -0.0033 -0.0019 0.0030  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2644 0.2205 0.1744 -0.0004 0.0146  0.0074  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2288 0.2145 0.1702 -0.0020 0.0145  0.0096  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2185 0.2124 0.1695 -0.0028 0.0110  0.0071  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2785 0.2189 0.1751 0.0042  0.0319  0.0091  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3420 0.2400 0.1919 0.0019  0.0391  0.0068  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3769 0.2614 0.2122 0.0010  0.0505  0.0102  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3911 0.2568 0.2057 -0.0018 0.0356  0.0016  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4438 0.2793 0.2243 -0.0046 0.0599  0.0077  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4423 0.2571 0.1988 -0.0095 0.0408  -0.0006 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4835 0.2813 0.2202 -0.0114 0.0540  0.0021  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5678 0.3050 0.2350 -0.0223 0.0626  -0.0006 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2259 0.2238 0.1787 -0.0051 0.0174  0.0153  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2273 0.2448 0.1993 -0.0124 0.0143  0.0204  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2364 0.2635 0.2275 -0.0097 0.0209  0.0319  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2634 0.2847 0.2595 -0.0027 0.0340  0.0380  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2470 0.2681 0.2213 -0.0183 0.0132  0.0250  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2586 0.2685 0.2245 -0.0107 0.0215  0.0270  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2497 0.2400 0.1944 -0.0046 0.0221  0.0190  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2240 0.2628 0.2275 -0.0162 0.0138  0.0362  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2305 0.2807 0.2626 -0.0147 0.0171  0.0506  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2111 0.2755 0.2581 -0.0305 0.0008  0.0634  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2333 0.2917 0.2563 -0.0422 -0.0092 0.0552  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2619 0.3047 0.2901 -0.0062 0.0230  0.0438  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3023 0.3229 0.3141 0.0057  0.0404  0.0372  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2672 0.3068 0.2759 -0.0112 0.0123  0.0311  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1850 0.2639 0.2722 -0.0322 -0.0008 0.0851  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1964 0.2866 0.3019 -0.0495 -0.0211 0.1032  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1976 0.2922 0.3231 -0.0408 -0.0155 0.1058  75  SER   A C   
545  O O   . SER   A 69  ? 0.2198 0.3120 0.3632 -0.0228 0.0060  0.1038  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2194 0.3254 0.3727 -0.0567 -0.0293 0.1318  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3055 0.4062 0.4391 -0.0650 -0.0345 0.1293  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1814 0.2748 0.2926 -0.0536 -0.0310 0.1057  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1687 0.2655 0.2965 -0.0455 -0.0263 0.1068  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1885 0.2946 0.3367 -0.0640 -0.0493 0.1289  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2254 0.3262 0.3522 -0.0880 -0.0716 0.1372  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1797 0.2615 0.2668 -0.0373 -0.0174 0.0798  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1843 0.2537 0.2282 -0.0520 -0.0269 0.0662  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1963 0.2551 0.2152 -0.0512 -0.0213 0.0522  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2045 0.2689 0.2336 -0.0671 -0.0382 0.0678  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2198 0.2625 0.2048 -0.0634 -0.0223 0.0394  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2303 0.2749 0.2171 -0.0806 -0.0382 0.0536  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2410 0.2745 0.2086 -0.0783 -0.0285 0.0396  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1774 0.2933 0.3650 -0.0559 -0.0453 0.1405  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1793 0.3052 0.3949 -0.0743 -0.0703 0.1667  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2157 0.3265 0.3780 -0.0909 -0.0851 0.1544  77  SER   A C   
562  O O   . SER   A 71  ? 0.2267 0.3232 0.3440 -0.0834 -0.0713 0.1261  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1775 0.3188 0.4631 -0.0586 -0.0577 0.1855  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2077 0.3385 0.4715 -0.0422 -0.0381 0.1626  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2352 0.3462 0.4029 -0.1161 -0.1140 0.1779  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2807 0.3717 0.3952 -0.1334 -0.1242 0.1673  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2722 0.3711 0.4063 -0.1134 -0.1088 0.1582  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2618 0.3798 0.4562 -0.0963 -0.1006 0.1719  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3498 0.4321 0.4581 -0.1703 -0.1627 0.1980  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4672 0.5274 0.5295 -0.1976 -0.1798 0.2017  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5847 0.6286 0.6326 -0.2396 -0.2232 0.2350  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7088 0.7043 0.6597 -0.2729 -0.2311 0.2211  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7777 0.7462 0.6645 -0.2658 -0.2002 0.1828  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2734 0.3548 0.3594 -0.1166 -0.1032 0.1367  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2816 0.3695 0.3855 -0.0986 -0.0904 0.1285  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2760 0.3791 0.4308 -0.1038 -0.1065 0.1578  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2817 0.3803 0.4304 -0.1316 -0.1350 0.1801  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3241 0.3894 0.3709 -0.1091 -0.0874 0.1077  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3593 0.4036 0.3577 -0.1253 -0.0874 0.0976  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3066 0.3586 0.3229 -0.1361 -0.1039 0.1191  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2641 0.3813 0.4690 -0.0794 -0.0888 0.1600  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2623 0.3952 0.5297 -0.0811 -0.0995 0.1897  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2410 0.3754 0.5374 -0.0547 -0.0724 0.1797  80  SER   A C   
584  O O   . SER   A 74  ? 0.2341 0.3551 0.4959 -0.0379 -0.0495 0.1504  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2915 0.4416 0.6210 -0.0865 -0.1106 0.2229  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3538 0.5078 0.7109 -0.0621 -0.0802 0.2150  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2232 0.3702 0.5815 -0.0538 -0.0774 0.2057  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2374 0.3812 0.6269 -0.0313 -0.0507 0.1997  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2467 0.3909 0.6871 -0.0113 -0.0200 0.2061  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2435 0.4056 0.7555 -0.0152 -0.0263 0.2394  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2315 0.3885 0.6762 -0.0398 -0.0680 0.2293  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2989 0.4491 0.6989 -0.0538 -0.0872 0.2211  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3037 0.4683 0.7603 -0.0696 -0.1142 0.2588  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3226 0.4573 0.6943 -0.0335 -0.0602 0.1904  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2594 0.3809 0.6667 0.0081  0.0132  0.1776  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2808 0.3901 0.7179 0.0259  0.0497  0.1779  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3188 0.3981 0.7513 0.0439  0.0865  0.1625  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3308 0.3912 0.7028 0.0446  0.0851  0.1371  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3167 0.4155 0.6980 0.0256  0.0529  0.1575  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3222 0.4460 0.7160 0.0075  0.0214  0.1764  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3400 0.4135 0.7267 0.0431  0.0949  0.1497  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3605 0.4767 0.6978 0.0038  0.0177  0.1569  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3312 0.4026 0.8303 0.0575  0.1211  0.1793  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3942 0.4257 0.8808 0.0727  0.1622  0.1632  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4594 0.4456 0.8553 0.0773  0.1851  0.1279  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4664 0.4479 0.8463 0.0775  0.1926  0.1244  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3846 0.4117 0.9663 0.0861  0.2017  0.1894  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4284 0.4123 1.0010 0.0986  0.2426  0.1757  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4427 0.4351 1.0308 0.0964  0.2275  0.1803  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4784 0.4068 1.0194 0.1102  0.2972  0.1574  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4771 0.4258 1.0539 0.1069  0.2658  0.1671  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5108 0.3899 1.0362 0.1188  0.3377  0.1443  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5034 0.3938 1.0467 0.1175  0.3210  0.1487  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5048 0.4576 0.8394 0.0782  0.1909  0.1036  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5688 0.4725 0.8123 0.0775  0.2050  0.0732  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6204 0.4684 0.8375 0.0837  0.2420  0.0603  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.6119 0.4643 0.8452 0.0841  0.2352  0.0626  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5812 0.4964 0.7615 0.0656  0.1629  0.0558  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6340 0.4975 0.7275 0.0621  0.1719  0.0300  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5571 0.5174 0.7557 0.0581  0.1322  0.0661  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6726 0.4627 0.8419 0.0863  0.2817  0.0460  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.7348 0.4535 0.8610 0.0887  0.3255  0.0311  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.7812 0.4671 0.8252 0.0773  0.3029  0.0091  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.7844 0.4966 0.7958 0.0676  0.2567  0.0026  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.8130 0.4716 0.8878 0.0883  0.3685  0.0195  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8740 0.5506 1.0372 0.1016  0.4059  0.0420  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.0055 0.6137 1.1757 0.1106  0.4787  0.0400  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0579 0.6129 1.1812 0.1078  0.4986  0.0248  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.0296 0.6347 1.2545 0.1201  0.5186  0.0541  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.8094 0.4331 0.8200 0.0774  0.3377  -0.0018 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.8612 0.4463 0.7936 0.0645  0.3175  -0.0206 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.9235 0.4651 0.7488 0.0462  0.2951  -0.0401 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.9504 0.4677 0.7441 0.0435  0.3112  -0.0439 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.8943 0.4124 0.8099 0.0669  0.3654  -0.0279 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.9415 0.4727 0.7156 0.0326  0.2568  -0.0500 87  SER   A N   
636  C CA  . SER   A 81  ? 0.9890 0.4812 0.6717 0.0124  0.2265  -0.0629 87  SER   A CA  
637  C C   . SER   A 81  ? 1.0253 0.4806 0.6537 -0.0031 0.2012  -0.0719 87  SER   A C   
638  O O   . SER   A 81  ? 1.0145 0.4835 0.6807 0.0039  0.2059  -0.0689 87  SER   A O   
639  C CB  . SER   A 81  ? 0.9679 0.5293 0.6839 0.0129  0.1826  -0.0547 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.9500 0.5694 0.7124 0.0148  0.1445  -0.0480 87  SER   A OG  
641  N N   . GLU   A 82  ? 1.0623 0.4719 0.6062 -0.0257 0.1708  -0.0801 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.0909 0.4698 0.5892 -0.0433 0.1378  -0.0843 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.0140 0.4774 0.5920 -0.0348 0.0966  -0.0730 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.0265 0.4773 0.5886 -0.0454 0.0713  -0.0735 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.1991 0.5175 0.6010 -0.0721 0.1053  -0.0889 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.3726 0.5806 0.6641 -0.0903 0.1429  -0.1028 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.5849 0.7019 0.7786 -0.1184 0.1325  -0.1116 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.6203 0.7612 0.8272 -0.1280 0.0826  -0.1042 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.6868 0.7047 0.7897 -0.1320 0.1760  -0.1256 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.9376 0.4817 0.5967 -0.0176 0.0909  -0.0626 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.8709 0.4891 0.5987 -0.0111 0.0583  -0.0527 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.7826 0.4529 0.5893 0.0077  0.0783  -0.0439 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.7560 0.4624 0.6013 0.0098  0.0600  -0.0385 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.8611 0.5220 0.6080 -0.0126 0.0303  -0.0471 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.9191 0.5322 0.5987 -0.0280 0.0200  -0.0517 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.9572 0.5445 0.5987 -0.0474 -0.0189 -0.0501 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.9448 0.5413 0.6051 -0.0244 0.0461  -0.0545 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 1.0050 0.5491 0.5871 -0.0645 -0.0343 -0.0504 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.9979 0.5503 0.5946 -0.0402 0.0349  -0.0575 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 1.0394 0.5649 0.5952 -0.0610 -0.0068 -0.0550 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.1135 0.5935 0.6063 -0.0795 -0.0223 -0.0547 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.7374 0.4108 0.5711 0.0198  0.1140  -0.0398 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.6678 0.3900 0.5828 0.0345  0.1274  -0.0257 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.6916 0.3827 0.6268 0.0449  0.1758  -0.0223 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.7230 0.3713 0.6257 0.0452  0.2064  -0.0282 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5847 0.3682 0.5518 0.0401  0.1154  -0.0132 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.5202 0.3369 0.4798 0.0321  0.0765  -0.0148 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4874 0.3372 0.4715 0.0292  0.0515  -0.0111 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.5147 0.3304 0.4494 0.0280  0.0684  -0.0187 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4578 0.3343 0.4417 0.0227  0.0237  -0.0121 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4783 0.3246 0.4169 0.0220  0.0379  -0.0186 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4515 0.3273 0.4163 0.0198  0.0180  -0.0154 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3765 0.2750 0.3471 0.0141  -0.0051 -0.0158 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.6680 0.3852 0.6686 0.0544  0.1854  -0.0094 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.6686 0.3668 0.7149 0.0669  0.2340  0.0001  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.6428 0.3919 0.7598 0.0755  0.2369  0.0201  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6287 0.4254 0.7528 0.0705  0.2002  0.0248  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.6540 0.3680 0.7512 0.0720  0.2339  0.0103  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.6328 0.4031 0.7402 0.0647  0.1810  0.0146  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.6311 0.3986 0.6750 0.0538  0.1534  0.0003  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.6317 0.3703 0.8056 0.0874  0.2804  0.0336  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5900 0.3771 0.8409 0.0941  0.2807  0.0572  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.5239 0.3840 0.8412 0.0906  0.2349  0.0801  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.5155 0.3863 0.8697 0.0921  0.2300  0.0897  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5856 0.3485 0.9024 0.1079  0.3371  0.0721  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4815 0.3842 0.7994 0.0830  0.1998  0.0860  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.4255 0.3843 0.7850 0.0742  0.1565  0.1049  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3886 0.3856 0.7691 0.0668  0.1332  0.1194  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.4040 0.3885 0.7675 0.0701  0.1489  0.1132  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4366 0.3948 0.7342 0.0646  0.1260  0.0856  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4431 0.4033 0.6772 0.0561  0.1044  0.0676  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.4562 0.3869 0.6208 0.0520  0.0964  0.0428  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4549 0.4032 0.5860 0.0426  0.0678  0.0340  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4552 0.3950 0.5559 0.0413  0.0684  0.0257  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3896 0.3448 0.4685 0.0335  0.0449  0.0192  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4859 0.3994 0.5797 0.0476  0.0954  0.0245  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3479 0.3862 0.7586 0.0544  0.0955  0.1384  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.3275 0.3940 0.7385 0.0422  0.0686  0.1485  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.3005 0.3619 0.6314 0.0331  0.0478  0.1221  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.3025 0.3637 0.6100 0.0276  0.0333  0.1141  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3267 0.4292 0.7958 0.0274  0.0360  0.1823  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3371 0.4526 0.9047 0.0342  0.0503  0.2170  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3469 0.4784 0.9576 0.0313  0.0481  0.2379  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3498 0.4619 0.9751 0.0433  0.0665  0.2311  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3384 0.4841 1.0544 0.0376  0.0613  0.2744  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3339 0.4587 1.0643 0.0503  0.0821  0.2665  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3351 0.4776 1.1141 0.0476  0.0794  0.2892  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3376 0.4947 1.2346 0.0547  0.0952  0.3286  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2656 0.3213 0.5596 0.0324  0.0491  0.1093  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2411 0.2950 0.4737 0.0235  0.0302  0.0888  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2074 0.2881 0.4490 0.0066  0.0031  0.1040  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2135 0.3063 0.4856 0.0039  0.0018  0.1209  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2589 0.2883 0.4455 0.0302  0.0448  0.0677  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2577 0.2898 0.3975 0.0211  0.0250  0.0518  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2806 0.2833 0.3740 0.0262  0.0337  0.0316  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2972 0.2696 0.3725 0.0325  0.0487  0.0235  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2583 0.2649 0.3290 0.0211  0.0234  0.0243  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1844 0.2697 0.3979 -0.0069 -0.0173 0.0992  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1778 0.2753 0.3832 -0.0280 -0.0413 0.1116  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1935 0.2821 0.3502 -0.0327 -0.0412 0.0925  96  SER   A C   
721  O O   . SER   A 90  ? 0.2009 0.2773 0.3330 -0.0208 -0.0277 0.0709  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1922 0.2905 0.3873 -0.0432 -0.0587 0.1171  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2266 0.3119 0.3834 -0.0389 -0.0513 0.0928  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1937 0.2857 0.3386 -0.0519 -0.0575 0.1031  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2037 0.2849 0.3055 -0.0592 -0.0564 0.0878  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1957 0.2761 0.2998 -0.0418 -0.0402 0.0762  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2079 0.2776 0.2815 -0.0388 -0.0331 0.0572  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2170 0.2832 0.2799 -0.0635 -0.0520 0.0681  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2745 0.3342 0.3231 -0.0841 -0.0657 0.0780  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3314 0.3729 0.3387 -0.1106 -0.0753 0.0814  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3006 0.3646 0.3658 -0.0837 -0.0707 0.0854  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3536 0.3866 0.3489 -0.1267 -0.0861 0.0904  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3365 0.3857 0.3696 -0.1104 -0.0845 0.0936  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1860 0.2748 0.3286 -0.0308 -0.0328 0.0889  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1875 0.2697 0.3282 -0.0159 -0.0151 0.0793  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1715 0.2634 0.3266 -0.0232 -0.0207 0.0934  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1685 0.2746 0.3601 -0.0337 -0.0341 0.1185  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1974 0.2733 0.3679 0.0013  0.0055  0.0824  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2285 0.2847 0.3853 0.0153  0.0290  0.0707  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2458 0.2819 0.3491 0.0169  0.0278  0.0461  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2601 0.3014 0.4463 0.0289  0.0555  0.0765  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1678 0.2511 0.2972 -0.0184 -0.0125 0.0794  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1660 0.2567 0.3058 -0.0249 -0.0169 0.0908  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1751 0.2582 0.3241 -0.0078 0.0059  0.0862  99  MET   A C   
745  O O   . MET   A 93  ? 0.1897 0.2548 0.3042 0.0013  0.0170  0.0656  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1766 0.2587 0.2704 -0.0371 -0.0259 0.0765  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2341 0.3120 0.3059 -0.0572 -0.0426 0.0785  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2955 0.3526 0.3130 -0.0698 -0.0410 0.0581  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2530 0.3044 0.2660 -0.0469 -0.0224 0.0339  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1613 0.2545 0.3554 -0.0052 0.0127  0.1065  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1796 0.2588 0.3787 0.0101  0.0406  0.1020  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1812 0.2638 0.3717 0.0054  0.0370  0.1033  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1795 0.2797 0.3858 -0.0090 0.0157  0.1185  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1863 0.2704 0.4531 0.0199  0.0619  0.1249  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2379 0.3116 0.5163 0.0284  0.0753  0.1228  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2236 0.2969 0.5749 0.0401  0.1053  0.1452  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2853 0.3234 0.4988 0.0369  0.0922  0.0928  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1826 0.2445 0.3479 0.0159  0.0579  0.0896  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1904 0.2528 0.3491 0.0138  0.0589  0.0907  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2162 0.2543 0.3760 0.0274  0.0934  0.0884  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2358 0.2481 0.3785 0.0360  0.1139  0.0786  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2164 0.2697 0.3193 0.0081  0.0450  0.0695  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2067 0.2478 0.3820 0.0277  0.1014  0.0972  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2477 0.2584 0.4120 0.0381  0.1368  0.0929  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3140 0.2970 0.4021 0.0353  0.1316  0.0686  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3204 0.3162 0.3939 0.0282  0.1107  0.0657  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2537 0.2797 0.4732 0.0393  0.1486  0.1151  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2928 0.2796 0.4924 0.0491  0.1908  0.1084  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2144 0.2688 0.5205 0.0401  0.1489  0.1449  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3544 0.2970 0.3953 0.0391  0.1491  0.0532  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3989 0.3116 0.3705 0.0335  0.1392  0.0348  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4324 0.2944 0.3492 0.0331  0.1548  0.0213  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.4414 0.2943 0.3721 0.0380  0.1712  0.0226  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.4453 0.2713 0.2980 0.0249  0.1470  0.0095  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4908 0.2589 0.2764 0.0181  0.1551  -0.0025 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4919 0.2651 0.2669 0.0134  0.1266  -0.0088 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.4675 0.2719 0.2562 0.0100  0.0932  -0.0087 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.5394 0.2613 0.2558 0.0060  0.1517  -0.0088 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.6350 0.2835 0.2689 -0.0065 0.1613  -0.0195 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.6959 0.2950 0.3047 -0.0043 0.2076  -0.0233 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.6885 0.3051 0.2650 -0.0225 0.1294  -0.0252 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.7643 0.2963 0.2876 -0.0211 0.2032  -0.0338 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.7649 0.3066 0.2673 -0.0334 0.1530  -0.0337 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5301 0.2660 0.2774 0.0124  0.1428  -0.0146 105 SER   A N   
785  C CA  . SER   A 99  ? 0.5590 0.2891 0.2879 0.0062  0.1180  -0.0206 105 SER   A CA  
786  C C   . SER   A 99  ? 0.6448 0.3040 0.3075 -0.0015 0.1402  -0.0297 105 SER   A C   
787  O O   . SER   A 99  ? 0.6883 0.3134 0.3406 0.0030  0.1832  -0.0308 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5277 0.3139 0.3242 0.0158  0.1079  -0.0147 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5606 0.3487 0.3921 0.0261  0.1404  -0.0089 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.6684 0.2994 0.2837 -0.0155 0.1116  -0.0354 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.7241 0.2828 0.2649 -0.0290 0.1206  -0.0443 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.7107 0.2922 0.2719 -0.0309 0.0887  -0.0439 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.6557 0.2974 0.2731 -0.0257 0.0582  -0.0374 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.8069 0.2955 0.2538 -0.0522 0.1093  -0.0481 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.8972 0.3501 0.3149 -0.0506 0.1518  -0.0505 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.0029 0.3884 0.3276 -0.0745 0.1415  -0.0525 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.0759 0.3918 0.3138 -0.0990 0.1240  -0.0569 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.9957 0.3952 0.3316 -0.0710 0.1485  -0.0483 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.7552 0.2893 0.2749 -0.0379 0.0985  -0.0507 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.7306 0.2919 0.2792 -0.0380 0.0700  -0.0491 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.7112 0.2975 0.2701 -0.0488 0.0174  -0.0420 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.6690 0.3144 0.2943 -0.0396 -0.0013 -0.0367 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.7931 0.2786 0.2706 -0.0503 0.0875  -0.0584 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.8283 0.2703 0.2791 -0.0447 0.1430  -0.0646 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.8060 0.2594 0.2558 -0.0449 0.1418  -0.0605 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.7343 0.2749 0.2322 -0.0688 -0.0046 -0.0399 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.7093 0.2710 0.2267 -0.0798 -0.0540 -0.0285 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.6216 0.2579 0.2205 -0.0640 -0.0611 -0.0217 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6000 0.2615 0.2346 -0.0691 -0.0955 -0.0113 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.5716 0.2379 0.1994 -0.0468 -0.0279 -0.0259 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.4993 0.2292 0.1953 -0.0341 -0.0317 -0.0209 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4337 0.2170 0.1954 -0.0231 -0.0360 -0.0194 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.3811 0.2085 0.1918 -0.0169 -0.0417 -0.0157 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.4932 0.2360 0.1987 -0.0230 -0.0003 -0.0227 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.5582 0.2572 0.2083 -0.0339 0.0016  -0.0226 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.5653 0.2497 0.1962 -0.0474 -0.0299 -0.0173 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6025 0.2775 0.2287 -0.0301 0.0352  -0.0264 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.4422 0.2177 0.2016 -0.0219 -0.0315 -0.0227 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3985 0.2210 0.2156 -0.0135 -0.0360 -0.0208 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3754 0.2199 0.2265 -0.0182 -0.0639 -0.0145 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3988 0.2157 0.2290 -0.0309 -0.0889 -0.0092 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4230 0.2283 0.2287 -0.0136 -0.0305 -0.0242 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.4697 0.2648 0.2701 -0.0026 0.0101  -0.0281 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3226 0.2115 0.2248 -0.0103 -0.0592 -0.0133 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3126 0.2212 0.2561 -0.0129 -0.0758 -0.0075 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2972 0.2197 0.2567 -0.0117 -0.0735 -0.0054 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2795 0.2220 0.2824 -0.0111 -0.0763 -0.0016 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2943 0.2039 0.2212 -0.0113 -0.0650 -0.0076 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2689 0.1925 0.2102 -0.0098 -0.0614 -0.0060 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2403 0.1976 0.2154 -0.0039 -0.0450 -0.0091 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2375 0.2048 0.2101 -0.0006 -0.0326 -0.0119 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2174 0.1873 0.2230 -0.0048 -0.0452 -0.0074 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1965 0.1858 0.2216 -0.0042 -0.0287 -0.0115 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2035 0.1987 0.2122 -0.0046 -0.0180 -0.0130 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2195 0.2085 0.2192 -0.0043 -0.0210 -0.0110 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2144 0.2069 0.2807 -0.0057 -0.0265 -0.0096 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2321 0.2244 0.3250 -0.0056 -0.0331 -0.0064 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2391 0.2373 0.3110 -0.0088 -0.0047 -0.0155 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2413 0.2349 0.3901 -0.0059 -0.0311 0.0004  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1830 0.1888 0.1890 -0.0077 -0.0081 -0.0144 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1733 0.1850 0.1690 -0.0124 -0.0016 -0.0125 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1838 0.1923 0.1835 -0.0215 0.0079  -0.0171 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1938 0.1993 0.1976 -0.0258 0.0134  -0.0203 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1792 0.1998 0.1700 -0.0145 -0.0012 -0.0066 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1913 0.2187 0.1776 -0.0240 -0.0005 0.0006  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2072 0.2348 0.1923 -0.0196 0.0008  0.0040  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2002 0.2380 0.1951 -0.0275 -0.0047 0.0121  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1988 0.2028 0.1950 -0.0252 0.0127  -0.0183 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2230 0.2138 0.2159 -0.0353 0.0274  -0.0243 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2363 0.2221 0.2037 -0.0468 0.0283  -0.0223 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2305 0.2251 0.1971 -0.0430 0.0201  -0.0168 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2423 0.2265 0.2632 -0.0292 0.0341  -0.0268 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3128 0.3006 0.3685 -0.0201 0.0282  -0.0241 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3571 0.3398 0.4498 -0.0162 0.0312  -0.0209 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4470 0.4148 0.5556 -0.0215 0.0592  -0.0272 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4572 0.4200 0.6026 -0.0198 0.0724  -0.0268 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4307 0.4058 0.6072 -0.0129 0.0541  -0.0181 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4644 0.4056 0.6151 -0.0261 0.1056  -0.0345 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2573 0.2228 0.2011 -0.0630 0.0402  -0.0271 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2999 0.2504 0.2121 -0.0797 0.0406  -0.0256 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3496 0.2692 0.2536 -0.0865 0.0661  -0.0378 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3561 0.2735 0.2910 -0.0756 0.0811  -0.0438 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3167 0.2593 0.1960 -0.0996 0.0299  -0.0181 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3497 0.2591 0.1986 -0.1156 0.0479  -0.0280 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4028 0.2959 0.2690 -0.1051 0.0722  -0.0401 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4518 0.3082 0.3081 -0.1122 0.1029  -0.0528 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4860 0.3113 0.3315 -0.1197 0.1309  -0.0631 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5297 0.3271 0.3879 -0.1187 0.1644  -0.0733 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5302 0.3553 0.3337 -0.1359 0.1031  -0.0535 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6322 0.4294 0.3730 -0.1656 0.0929  -0.0498 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7640 0.5304 0.4505 -0.1930 0.0829  -0.0456 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7917 0.5761 0.4707 -0.2033 0.0494  -0.0283 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7944 0.5111 0.4452 -0.2066 0.1127  -0.0599 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4706 0.2984 0.2965 -0.1272 0.1204  -0.0597 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4875 0.2838 0.2973 -0.1364 0.1468  -0.0687 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4472 0.2703 0.3209 -0.1128 0.1532  -0.0684 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4785 0.2769 0.3535 -0.1167 0.1808  -0.0756 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5319 0.3088 0.2797 -0.1624 0.1316  -0.0639 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5965 0.3455 0.2817 -0.1905 0.1171  -0.0591 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.6088 0.3876 0.2931 -0.1952 0.0767  -0.0411 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.6687 0.3574 0.2891 -0.2179 0.1383  -0.0687 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.6705 0.4134 0.2983 -0.2238 0.0694  -0.0379 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.7058 0.3909 0.2866 -0.2396 0.1051  -0.0553 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3807 0.2497 0.3026 -0.0909 0.1274  -0.0592 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3323 0.2237 0.3093 -0.0724 0.1261  -0.0562 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2846 0.2117 0.2703 -0.0621 0.0929  -0.0467 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2825 0.2240 0.2507 -0.0624 0.0726  -0.0410 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2647 0.2028 0.2788 -0.0534 0.0904  -0.0447 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2461 0.2108 0.2684 -0.0437 0.0638  -0.0373 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2496 0.2155 0.2337 -0.0545 0.0544  -0.0347 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2743 0.2234 0.2387 -0.0668 0.0660  -0.0380 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2433 0.2151 0.3084 -0.0334 0.0631  -0.0350 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2205 0.2101 0.2817 -0.0268 0.0391  -0.0294 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2346 0.2091 0.3487 -0.0237 0.0630  -0.0305 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2245 0.2086 0.2025 -0.0501 0.0343  -0.0269 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2250 0.2150 0.1832 -0.0589 0.0224  -0.0189 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2234 0.2290 0.2002 -0.0480 0.0126  -0.0147 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2302 0.2360 0.1991 -0.0557 0.0086  -0.0102 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2369 0.2363 0.1882 -0.0609 0.0108  -0.0099 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2549 0.2651 0.2046 -0.0680 -0.0039 0.0043  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2582 0.2386 0.1846 -0.0753 0.0182  -0.0132 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1940 0.2086 0.1902 -0.0324 0.0074  -0.0151 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1938 0.2152 0.2000 -0.0235 -0.0002 -0.0122 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1811 0.1989 0.1944 -0.0120 -0.0059 -0.0139 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1813 0.1942 0.1984 -0.0106 -0.0060 -0.0161 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1764 0.1919 0.1876 -0.0060 -0.0111 -0.0120 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1871 0.1875 0.1897 -0.0004 -0.0182 -0.0133 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2092 0.1998 0.1941 0.0042  -0.0135 -0.0110 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2005 0.1992 0.1929 0.0055  -0.0075 -0.0072 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2072 0.2000 0.2205 -0.0007 -0.0283 -0.0144 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2235 0.2217 0.2414 -0.0005 -0.0259 -0.0143 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2298 0.2267 0.2708 -0.0034 -0.0301 -0.0141 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2632 0.2499 0.2897 -0.0011 -0.0390 -0.0139 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2132 0.1829 0.1751 0.0057  -0.0140 -0.0121 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2277 0.1783 0.1694 0.0098  -0.0011 -0.0113 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2430 0.1808 0.1795 0.0110  0.0002  -0.0130 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2618 0.1867 0.1884 0.0066  -0.0144 -0.0162 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2670 0.1845 0.1708 0.0073  -0.0007 -0.0139 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3014 0.1887 0.1793 0.0106  0.0211  -0.0148 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2748 0.2048 0.1851 0.0069  -0.0004 -0.0115 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2404 0.1804 0.1881 0.0164  0.0170  -0.0089 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2720 0.1993 0.2180 0.0183  0.0216  -0.0100 125 SER   A CA  
923  C C   . SER   A 119 ? 0.3210 0.2199 0.2558 0.0240  0.0485  -0.0090 125 SER   A C   
924  O O   . SER   A 119 ? 0.3616 0.2295 0.2741 0.0237  0.0558  -0.0140 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2756 0.2372 0.2605 0.0185  0.0160  -0.0035 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2867 0.2378 0.2744 0.0210  0.0209  -0.0034 125 SER   A OG  
927  N N   . THR   A 120 ? 0.3262 0.2328 0.2789 0.0288  0.0656  -0.0018 126 THR   A N   
928  C CA  . THR   A 120 ? 0.3615 0.2392 0.3141 0.0356  0.0995  0.0009  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4028 0.2644 0.3402 0.0366  0.1161  0.0014  126 THR   A C   
930  O O   . THR   A 120 ? 0.3771 0.2587 0.3138 0.0329  0.0992  0.0021  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3500 0.2588 0.3691 0.0430  0.1103  0.0173  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3410 0.2856 0.4036 0.0434  0.1067  0.0321  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3275 0.2590 0.3656 0.0404  0.0903  0.0193  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.4465 0.2711 0.3759 0.0418  0.1532  0.0019  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.4979 0.3069 0.4194 0.0434  0.1748  0.0041  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5561 0.3193 0.4753 0.0500  0.2247  0.0050  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.5668 0.3218 0.5108 0.0559  0.2436  0.0081  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.6017 0.3310 0.4886 0.0484  0.2480  0.0018  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.6610 0.3355 0.5370 0.0533  0.3041  0.0010  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.6555 0.3644 0.6140 0.0652  0.3282  0.0212  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6148 0.3907 0.6512 0.0702  0.3027  0.0391  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.6923 0.3513 0.6347 0.0680  0.3788  0.0202  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.6688 0.3558 0.6983 0.0797  0.4076  0.0422  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.6099 0.3518 0.6666 0.0770  0.3709  0.0528  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5813 0.3638 0.7262 0.0848  0.3788  0.0764  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.6655 0.3919 0.8052 0.0929  0.4206  0.0656  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.7679 0.4373 0.8955 0.0982  0.4687  0.0580  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.8481 0.4399 0.9124 0.0964  0.5198  0.0429  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.7463 0.4478 0.9320 0.1037  0.4559  0.0689  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.5932 0.3295 0.5753 0.0650  0.3348  0.0367  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.5375 0.3193 0.5385 0.0617  0.3021  0.0442  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4592 0.3099 0.5151 0.0606  0.2551  0.0554  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4433 0.3353 0.5342 0.0582  0.2328  0.0670  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4217 0.2790 0.4779 0.0602  0.2407  0.0514  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3582 0.2690 0.4517 0.0564  0.1992  0.0594  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.3583 0.2582 0.3882 0.0485  0.1704  0.0393  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4148 0.2680 0.3877 0.0470  0.1825  0.0240  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3397 0.2699 0.5016 0.0627  0.2085  0.0765  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3493 0.2975 0.5997 0.0705  0.2340  0.1043  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3522 0.3060 0.6658 0.0779  0.2501  0.1198  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3249 0.3244 0.6228 0.0622  0.1993  0.1248  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.2894 0.2290 0.3327 0.0422  0.1339  0.0414  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2745 0.2108 0.2781 0.0360  0.1083  0.0268  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2403 0.2169 0.2846 0.0326  0.0863  0.0359  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2308 0.2384 0.3127 0.0286  0.0764  0.0502  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.2933 0.2233 0.2554 0.0290  0.0896  0.0162  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2817 0.2453 0.2720 0.0258  0.0777  0.0250  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2925 0.2218 0.2311 0.0232  0.0645  0.0056  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2334 0.2044 0.2674 0.0322  0.0796  0.0293  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1966 0.1977 0.2594 0.0273  0.0607  0.0365  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2094 0.2122 0.2428 0.0205  0.0392  0.0234  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2381 0.2165 0.2371 0.0215  0.0381  0.0105  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1811 0.2084 0.2275 0.0115  0.0223  0.0281  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1809 0.2087 0.2076 0.0050  0.0087  0.0169  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1764 0.2157 0.2153 -0.0014 0.0004  0.0210  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1751 0.2288 0.2330 -0.0090 -0.0047 0.0347  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1699 0.2060 0.1909 -0.0034 0.0021  0.0164  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1814 0.2095 0.1937 0.0014  0.0087  0.0152  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1998 0.2110 0.1900 0.0045  0.0076  0.0044  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1810 0.2186 0.2103 0.0005  0.0133  0.0274  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2088 0.2094 0.1865 0.0070  0.0127  0.0041  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1910 0.2199 0.2117 0.0047  0.0214  0.0263  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2043 0.2139 0.1955 0.0076  0.0212  0.0136  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1726 0.2039 0.2011 -0.0003 -0.0028 0.0112  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1605 0.1995 0.1955 -0.0073 -0.0092 0.0130  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1521 0.1932 0.1760 -0.0200 -0.0126 0.0099  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1659 0.1995 0.1822 -0.0190 -0.0098 -0.0001 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1583 0.1861 0.1883 -0.0021 -0.0103 0.0040  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1552 0.2020 0.1778 -0.0339 -0.0183 0.0201  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1792 0.2160 0.1781 -0.0501 -0.0177 0.0163  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2160 0.2412 0.2061 -0.0532 -0.0098 0.0053  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2208 0.2494 0.2210 -0.0498 -0.0120 0.0065  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2288 0.2662 0.2193 -0.0698 -0.0306 0.0328  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3351 0.3502 0.2858 -0.0921 -0.0294 0.0291  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3117 0.3193 0.2518 -0.0907 -0.0208 0.0204  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3934 0.3930 0.3186 -0.1121 -0.0348 0.0338  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2138 0.2233 0.1888 -0.0598 0.0024  -0.0048 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2297 0.2246 0.2019 -0.0643 0.0163  -0.0134 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2785 0.2446 0.2114 -0.0867 0.0296  -0.0170 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3053 0.2517 0.2322 -0.0924 0.0487  -0.0249 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2260 0.2219 0.2290 -0.0495 0.0259  -0.0218 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2127 0.2249 0.2395 -0.0332 0.0108  -0.0185 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2325 0.2212 0.2357 -0.0489 0.0348  -0.0264 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2828 0.2413 0.1871 -0.1011 0.0216  -0.0111 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3090 0.2292 0.1624 -0.1269 0.0338  -0.0153 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3882 0.2822 0.2015 -0.1502 0.0336  -0.0119 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4610 0.3106 0.2243 -0.1723 0.0534  -0.0202 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3275 0.2449 0.1590 -0.1393 0.0188  -0.0066 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3467 0.2820 0.2079 -0.1200 0.0225  -0.0112 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3426 0.2788 0.1878 -0.1322 0.0054  0.0003  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3318 0.2980 0.2046 -0.1277 -0.0197 0.0195  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3482 0.3246 0.2277 -0.1338 -0.0367 0.0347  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3486 0.3052 0.1982 -0.1488 -0.0361 0.0331  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3252 0.3296 0.2446 -0.1257 -0.0527 0.0530  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3738 0.2900 0.2052 -0.1472 0.0131  0.0006  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4198 0.3116 0.2137 -0.1706 0.0092  0.0063  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4196 0.3003 0.2210 -0.1632 0.0351  -0.0072 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4650 0.3159 0.2265 -0.1847 0.0398  -0.0060 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4346 0.3541 0.2513 -0.1718 -0.0238 0.0285  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4516 0.4097 0.3287 -0.1410 -0.0249 0.0280  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4355 0.4105 0.3433 -0.1176 -0.0149 0.0180  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4401 0.4072 0.3296 -0.1425 -0.0368 0.0384  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3810 0.2829 0.2334 -0.1355 0.0503  -0.0177 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3814 0.2777 0.2567 -0.1269 0.0726  -0.0265 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.4308 0.2843 0.2827 -0.1383 0.1117  -0.0401 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4166 0.2740 0.3091 -0.1225 0.1316  -0.0476 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3392 0.2729 0.2800 -0.0969 0.0656  -0.0269 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3098 0.2765 0.2692 -0.0854 0.0349  -0.0158 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2817 0.2712 0.2871 -0.0614 0.0286  -0.0176 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3193 0.2864 0.2681 -0.0947 0.0241  -0.0073 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4818 0.2892 0.2648 -0.1685 0.1227  -0.0418 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.5474 0.3006 0.2927 -0.1841 0.1657  -0.0560 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.5660 0.3124 0.3582 -0.1699 0.2043  -0.0650 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.5878 0.3060 0.3905 -0.1683 0.2441  -0.0757 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.6156 0.3087 0.2622 -0.2252 0.1690  -0.0556 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.6626 0.3573 0.2631 -0.2466 0.1258  -0.0404 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.7532 0.3734 0.2463 -0.2937 0.1316  -0.0401 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.6473 0.3651 0.2702 -0.2345 0.1143  -0.0397 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.5503 0.3234 0.3791 -0.1586 0.1933  -0.0589 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.5270 0.2983 0.4099 -0.1453 0.2251  -0.0632 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5075 0.3111 0.4763 -0.1174 0.2298  -0.0623 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5105 0.3060 0.5317 -0.1087 0.2619  -0.0638 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4932 0.2853 0.3915 -0.1419 0.2072  -0.0555 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4406 0.2865 0.3692 -0.1253 0.1586  -0.0442 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4499 0.3069 0.3417 -0.1350 0.1244  -0.0353 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3878 0.2770 0.3896 -0.0981 0.1415  -0.0395 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.4145 0.3174 0.3531 -0.1132 0.0939  -0.0276 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3808 0.3006 0.3789 -0.0922 0.1028  -0.0310 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3703 0.2716 0.4415 -0.0803 0.1546  -0.0393 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3594 0.3132 0.4062 -0.0712 0.0803  -0.0261 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3509 0.2892 0.4716 -0.0615 0.1246  -0.0314 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3402 0.3006 0.4415 -0.0578 0.0894  -0.0267 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4874 0.3239 0.4730 -0.1050 0.1993  -0.0578 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4739 0.3357 0.5334 -0.0829 0.1993  -0.0546 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.5546 0.3817 0.6312 -0.0857 0.2460  -0.0621 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5380 0.3815 0.6928 -0.0687 0.2534  -0.0560 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4352 0.3274 0.4921 -0.0740 0.1625  -0.0500 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3926 0.3201 0.4540 -0.0650 0.1219  -0.0415 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3880 0.3350 0.4410 -0.0584 0.0959  -0.0383 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3635 0.3124 0.4886 -0.0492 0.1130  -0.0347 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.6386 0.4150 0.6425 -0.1086 0.2757  -0.0736 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7113 0.4419 0.7162 -0.1148 0.3273  -0.0835 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.7714 0.4576 0.7838 -0.1225 0.3819  -0.0899 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8031 0.4423 0.8124 -0.1292 0.4329  -0.0994 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.7869 0.4716 0.6928 -0.1412 0.3340  -0.0939 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8388 0.5548 0.7323 -0.1373 0.2921  -0.0890 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8210 0.5839 0.7852 -0.1128 0.2713  -0.0811 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9082 0.5992 0.7202 -0.1607 0.2787  -0.0912 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.7959 0.4874 0.8066 -0.1250 0.3767  -0.0864 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.8448 0.4890 0.8572 -0.1343 0.4326  -0.0927 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.8207 0.5033 0.9196 -0.1155 0.4260  -0.0805 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.8428 0.4912 0.9482 -0.1222 0.4696  -0.0836 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.9504 0.5342 0.8390 -0.1694 0.4447  -0.1036 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.0298 0.6473 0.8768 -0.1760 0.3856  -0.0948 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.1927 0.7609 0.9157 -0.2127 0.3744  -0.0994 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.2453 0.7901 0.9136 -0.2330 0.3693  -0.0973 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.2431 0.7940 0.9236 -0.2233 0.3690  -0.1034 145 GLU   A OE2 
1078 N N1  . A1BPU B .   ? 0.5819 0.4627 0.5469 0.0316  0.0665  -0.0065 201 A1BPU A N1  
1079 C C4  . A1BPU B .   ? 0.8216 0.3769 0.4785 0.0139  0.2483  -0.0418 201 A1BPU A C4  
1080 C C5  . A1BPU B .   ? 0.8191 0.3847 0.4897 0.0148  0.2342  -0.0433 201 A1BPU A C5  
1081 C C6  . A1BPU B .   ? 0.7766 0.4036 0.4866 0.0154  0.1872  -0.0383 201 A1BPU A C6  
1082 C C7  . A1BPU B .   ? 0.7682 0.4045 0.4924 0.0158  0.1735  -0.0396 201 A1BPU A C7  
1083 C C8  . A1BPU B .   ? 0.7081 0.4184 0.5257 0.0300  0.1661  -0.0261 201 A1BPU A C8  
1084 C C10 . A1BPU B .   ? 0.6781 0.4622 0.5695 0.0320  0.1131  -0.0196 201 A1BPU A C10 
1085 C C13 . A1BPU B .   ? 0.7773 0.4967 0.5654 0.0085  0.0739  -0.0379 201 A1BPU A C13 
1086 F F2  . A1BPU B .   ? 0.8114 0.4761 0.5638 0.0078  0.1048  -0.0441 201 A1BPU A F2  
1087 F F   . A1BPU B .   ? 0.7502 0.5084 0.5813 0.0119  0.0573  -0.0333 201 A1BPU A F   
1088 F F1  . A1BPU B .   ? 0.8166 0.5101 0.5563 -0.0060 0.0469  -0.0422 201 A1BPU A F1  
1089 C C12 . A1BPU B .   ? 0.7267 0.4832 0.5556 0.0182  0.0864  -0.0303 201 A1BPU A C12 
1090 C C11 . A1BPU B .   ? 0.6253 0.4690 0.5780 0.0356  0.0925  -0.0088 201 A1BPU A C11 
1091 O O2  . A1BPU B .   ? 0.6130 0.4645 0.5991 0.0407  0.1016  -0.0022 201 A1BPU A O2  
1092 C C9  . A1BPU B .   ? 0.6698 0.4592 0.5760 0.0374  0.1334  -0.0138 201 A1BPU A C9  
1093 C C14 . A1BPU B .   ? 0.7541 0.4620 0.5322 0.0143  0.1087  -0.0359 201 A1BPU A C14 
1094 N N   . A1BPU B .   ? 0.7151 0.4487 0.5461 0.0278  0.1385  -0.0264 201 A1BPU A N   
1095 O O1  . A1BPU B .   ? 0.6625 0.4059 0.5381 0.0406  0.1825  -0.0139 201 A1BPU A O1  
1096 C C1  . A1BPU B .   ? 0.7420 0.4166 0.4757 0.0149  0.1567  -0.0327 201 A1BPU A C1  
1097 O O   . A1BPU B .   ? 0.6983 0.4236 0.4674 0.0149  0.1187  -0.0292 201 A1BPU A O   
1098 C C   . A1BPU B .   ? 0.6769 0.4299 0.4483 0.0095  0.0864  -0.0275 201 A1BPU A C   
1099 C C3  . A1BPU B .   ? 0.7899 0.3968 0.4725 0.0138  0.2139  -0.0354 201 A1BPU A C3  
1100 C C2  . A1BPU B .   ? 0.7527 0.4179 0.4731 0.0143  0.1690  -0.0313 201 A1BPU A C2  
# 
