data_7I53
# 
_entry.id   7I53 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I53         pdb_00007i53 10.2210/pdb7i53/pdb 
WWPDB D_1001408326 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I53 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                      15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' 362.367   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                         65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                               78.133    4  ?         ? ? ? 
5 water       nat water                                                                              18.015    89 ?         ? ? ? 
# 
_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 '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' A1B3K 
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 
A1B3K non-polymer         . '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' ? 
'C15 H17 F3 N2 O3 S' 362.367 
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        A1B3K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3K 
_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 A1B3K 1  201 201 A1B3K LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 1   DMS   DMS A . 
E 4 DMS   1  204 2   DMS   DMS A . 
F 4 DMS   1  205 6   DMS   DMS A . 
G 4 DMS   1  206 7   DMS   DMS A . 
H 5 HOH   1  301 47  HOH   HOH A . 
H 5 HOH   2  302 27  HOH   HOH A . 
H 5 HOH   3  303 37  HOH   HOH A . 
H 5 HOH   4  304 32  HOH   HOH A . 
H 5 HOH   5  305 38  HOH   HOH A . 
H 5 HOH   6  306 22  HOH   HOH A . 
H 5 HOH   7  307 63  HOH   HOH A . 
H 5 HOH   8  308 73  HOH   HOH A . 
H 5 HOH   9  309 29  HOH   HOH A . 
H 5 HOH   10 310 50  HOH   HOH A . 
H 5 HOH   11 311 59  HOH   HOH A . 
H 5 HOH   12 312 18  HOH   HOH A . 
H 5 HOH   13 313 72  HOH   HOH A . 
H 5 HOH   14 314 36  HOH   HOH A . 
H 5 HOH   15 315 60  HOH   HOH A . 
H 5 HOH   16 316 74  HOH   HOH A . 
H 5 HOH   17 317 9   HOH   HOH A . 
H 5 HOH   18 318 8   HOH   HOH A . 
H 5 HOH   19 319 84  HOH   HOH A . 
H 5 HOH   20 320 14  HOH   HOH A . 
H 5 HOH   21 321 48  HOH   HOH A . 
H 5 HOH   22 322 23  HOH   HOH A . 
H 5 HOH   23 323 24  HOH   HOH A . 
H 5 HOH   24 324 51  HOH   HOH A . 
H 5 HOH   25 325 75  HOH   HOH A . 
H 5 HOH   26 326 25  HOH   HOH A . 
H 5 HOH   27 327 12  HOH   HOH A . 
H 5 HOH   28 328 16  HOH   HOH A . 
H 5 HOH   29 329 82  HOH   HOH A . 
H 5 HOH   30 330 76  HOH   HOH A . 
H 5 HOH   31 331 35  HOH   HOH A . 
H 5 HOH   32 332 19  HOH   HOH A . 
H 5 HOH   33 333 2   HOH   HOH A . 
H 5 HOH   34 334 40  HOH   HOH A . 
H 5 HOH   35 335 34  HOH   HOH A . 
H 5 HOH   36 336 4   HOH   HOH A . 
H 5 HOH   37 337 17  HOH   HOH A . 
H 5 HOH   38 338 7   HOH   HOH A . 
H 5 HOH   39 339 21  HOH   HOH A . 
H 5 HOH   40 340 30  HOH   HOH A . 
H 5 HOH   41 341 13  HOH   HOH A . 
H 5 HOH   42 342 54  HOH   HOH A . 
H 5 HOH   43 343 71  HOH   HOH A . 
H 5 HOH   44 344 77  HOH   HOH A . 
H 5 HOH   45 345 45  HOH   HOH A . 
H 5 HOH   46 346 78  HOH   HOH A . 
H 5 HOH   47 347 53  HOH   HOH A . 
H 5 HOH   48 348 42  HOH   HOH A . 
H 5 HOH   49 349 90  HOH   HOH A . 
H 5 HOH   50 350 33  HOH   HOH A . 
H 5 HOH   51 351 87  HOH   HOH A . 
H 5 HOH   52 352 79  HOH   HOH A . 
H 5 HOH   53 353 11  HOH   HOH A . 
H 5 HOH   54 354 26  HOH   HOH A . 
H 5 HOH   55 355 67  HOH   HOH A . 
H 5 HOH   56 356 55  HOH   HOH A . 
H 5 HOH   57 357 92  HOH   HOH A . 
H 5 HOH   58 358 20  HOH   HOH A . 
H 5 HOH   59 359 80  HOH   HOH A . 
H 5 HOH   60 360 49  HOH   HOH A . 
H 5 HOH   61 361 39  HOH   HOH A . 
H 5 HOH   62 362 10  HOH   HOH A . 
H 5 HOH   63 363 83  HOH   HOH A . 
H 5 HOH   64 364 81  HOH   HOH A . 
H 5 HOH   65 365 15  HOH   HOH A . 
H 5 HOH   66 366 5   HOH   HOH A . 
H 5 HOH   67 367 64  HOH   HOH A . 
H 5 HOH   68 368 6   HOH   HOH A . 
H 5 HOH   69 369 66  HOH   HOH A . 
H 5 HOH   70 370 88  HOH   HOH A . 
H 5 HOH   71 371 43  HOH   HOH A . 
H 5 HOH   72 372 3   HOH   HOH A . 
H 5 HOH   73 373 91  HOH   HOH A . 
H 5 HOH   74 374 56  HOH   HOH A . 
H 5 HOH   75 375 70  HOH   HOH A . 
H 5 HOH   76 376 85  HOH   HOH A . 
H 5 HOH   77 377 89  HOH   HOH A . 
H 5 HOH   78 378 46  HOH   HOH A . 
H 5 HOH   79 379 31  HOH   HOH A . 
H 5 HOH   80 380 28  HOH   HOH A . 
H 5 HOH   81 381 41  HOH   HOH A . 
H 5 HOH   82 382 86  HOH   HOH A . 
H 5 HOH   83 383 61  HOH   HOH A . 
H 5 HOH   84 384 65  HOH   HOH A . 
H 5 HOH   85 385 52  HOH   HOH A . 
H 5 HOH   86 386 58  HOH   HOH A . 
H 5 HOH   87 387 69  HOH   HOH A . 
H 5 HOH   88 388 44  HOH   HOH A . 
H 5 HOH   89 389 62  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I53 
_cell.length_a           72.848 
_cell.length_b           61.666 
_cell.length_c           32.812 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.48 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I53 
_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          7I53 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.90 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-16 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I53 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.05 
_reflns.d_resolution_high            1.54 
_reflns.number_obs                   21443 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.108 
_reflns.pdbx_netI_over_sigmaI        6.1 
_reflns.pdbx_redundancy              4.6 
_reflns.pdbx_Rrim_I_all              0.122 
_reflns.pdbx_Rpim_I_all              0.055 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     99271 
_reflns.pdbx_chi_squared             0.69 
_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                  1.54 
_reflns_shell.d_res_low                   1.62 
_reflns_shell.number_measured_all         10366 
_reflns_shell.number_unique_obs           3039 
_reflns_shell.Rmerge_I_obs                1.167 
_reflns_shell.pdbx_chi_squared            0.49 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        97.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.372 
_reflns_shell.pdbx_Rpim_I_all             0.708 
_reflns_shell.pdbx_CC_half                0.454 
_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                                 7I53 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21306 
_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                             36.39 
_refine.ls_d_res_high                            1.538 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_R_factor_obs                          0.2303 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2286 
_refine.ls_R_factor_R_free                       0.2634 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.830 
_refine.ls_number_reflns_R_free                  1030 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.934 
_refine.B_iso_mean                               30.51 
_refine.aniso_B[1][1]                            -1.85820 
_refine.aniso_B[2][2]                            -0.48840 
_refine.aniso_B[3][3]                            2.34670 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.21050 
_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             0.095 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.096 
_refine.pdbx_overall_SU_R_Blow_DPI               0.096 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.097 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I53 
_refine_analyze.Luzzati_coordinate_error_obs    0.25 
_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         25 
_refine_hist.number_atoms_solvent             84 
_refine_hist.number_atoms_total               1183 
_refine_hist.d_res_high                       1.538 
_refine_hist.d_res_low                        36.39 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1138 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  1548 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  '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  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1129 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.95  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.42 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  914  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.54 
_refine_ls_shell.d_res_low                        1.55 
_refine_ls_shell.number_reflns_R_work             402 
_refine_ls_shell.R_factor_R_work                  0.3363 
_refine_ls_shell.percent_reflns_obs               88.54 
_refine_ls_shell.R_factor_R_free                  0.2418 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.85 
_refine_ls_shell.number_reflns_R_free             25 
_refine_ls_shell.number_reflns_all                427 
_refine_ls_shell.R_factor_all                     0.3306 
# 
_struct.entry_id                  7I53 
_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-0036726-001 (A71EV2A-x4778)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I53 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I53 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? 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 ? ? ? ? ? ? ? 2.312 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
# 
_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_555 112.8 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.2 ? 
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_555 114.5 ? 
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_555 109.2 ? 
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 99.2  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 112.6 ? 
# 
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 THR A 120 ? N THR A 126 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                   7I53 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 313 ? ? 1_555 O  A HOH 313 ? ? 2_656 1.27 
2 1 OE2 A GLU 85  ? ? 1_555 OH A TYR 94  ? ? 2_556 2.02 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 89 ? ? -133.28 -34.67 
2 1 ALA A 92 ? ? -29.89  122.38 
# 
_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         15.2188 
_pdbx_refine_tls.origin_y         6.6197 
_pdbx_refine_tls.origin_z         14.3566 
_pdbx_refine_tls.T[1][1]          -0.0227 
_pdbx_refine_tls.T[2][2]          -0.0162 
_pdbx_refine_tls.T[3][3]          -0.0261 
_pdbx_refine_tls.T[1][2]          0.0076 
_pdbx_refine_tls.T[1][3]          -0.0063 
_pdbx_refine_tls.T[2][3]          -0.0204 
_pdbx_refine_tls.L[1][1]          1.0529 
_pdbx_refine_tls.L[2][2]          9.2749 
_pdbx_refine_tls.L[3][3]          0.6545 
_pdbx_refine_tls.L[1][2]          2.5994 
_pdbx_refine_tls.L[1][3]          -0.7435 
_pdbx_refine_tls.L[2][3]          -2.5720 
_pdbx_refine_tls.S[1][1]          -0.1265 
_pdbx_refine_tls.S[1][2]          0.0269 
_pdbx_refine_tls.S[1][3]          -0.0103 
_pdbx_refine_tls.S[2][1]          0.2126 
_pdbx_refine_tls.S[2][2]          0.1505 
_pdbx_refine_tls.S[2][3]          -0.3683 
_pdbx_refine_tls.S[3][1]          -0.0335 
_pdbx_refine_tls.S[3][2]          -0.1784 
_pdbx_refine_tls.S[3][3]          -0.0239 
# 
_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 
6 1 N 0 A DMS 203 ? D DMS ?   
7 1 N 0 A DMS 204 ? E DMS ?   
8 1 N 0 A DMS 205 ? F DMS ?   
# 
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 
A1B3K N1   N  N N 1   
A1B3K C4   C  Y N 2   
A1B3K C5   C  N N 3   
A1B3K C6   C  Y N 4   
A1B3K C7   C  Y N 5   
A1B3K C8   C  N N 6   
A1B3K C10  C  N N 7   
A1B3K C13  C  N N 8   
A1B3K O2   O  N N 9   
A1B3K C12  C  N S 10  
A1B3K S    S  N N 11  
A1B3K C11  C  N N 12  
A1B3K C14  C  N N 13  
A1B3K N    N  N N 14  
A1B3K C9   C  N N 15  
A1B3K O1   O  N N 16  
A1B3K C1   C  Y N 17  
A1B3K O    O  N N 18  
A1B3K C    C  N N 19  
A1B3K F2   F  N N 20  
A1B3K F1   F  N N 21  
A1B3K F    F  N N 22  
A1B3K C3   C  Y N 23  
A1B3K C2   C  Y N 24  
A1B3K H14  H  N N 25  
A1B3K H13  H  N N 26  
A1B3K H6   H  N N 27  
A1B3K H7   H  N N 28  
A1B3K H8   H  N N 29  
A1B3K H10  H  N N 30  
A1B3K H9   H  N N 31  
A1B3K H    H  N N 32  
A1B3K H11  H  N N 33  
A1B3K H12  H  N N 34  
A1B3K H15  H  N N 35  
A1B3K H16  H  N N 36  
A1B3K H2   H  N N 37  
A1B3K H1   H  N N 38  
A1B3K H3   H  N N 39  
A1B3K H5   H  N N 40  
A1B3K H4   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
DMS   S    S  N N 129 
DMS   O    O  N N 130 
DMS   C1   C  N N 131 
DMS   C2   C  N N 132 
DMS   H11  H  N N 133 
DMS   H12  H  N N 134 
DMS   H13  H  N N 135 
DMS   H21  H  N N 136 
DMS   H22  H  N N 137 
DMS   H23  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
ZN    ZN   ZN N N 442 
# 
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 
A1B3K C   O    sing N N 1   
A1B3K O   C1   sing N N 2   
A1B3K C1  C2   doub Y N 3   
A1B3K C2  C3   sing Y N 4   
A1B3K C3  C4   doub Y N 5   
A1B3K C5  C4   sing N N 6   
A1B3K F   C5   sing N N 7   
A1B3K F1  C5   sing N N 8   
A1B3K F2  C5   sing N N 9   
A1B3K C4  C6   sing Y N 10  
A1B3K C6  C7   doub Y N 11  
A1B3K C1  C7   sing Y N 12  
A1B3K C7  C8   sing N N 13  
A1B3K C8  C9   sing N N 14  
A1B3K O1  C9   doub N N 15  
A1B3K C9  N    sing N N 16  
A1B3K N   C10  sing N N 17  
A1B3K C10 C11  sing N N 18  
A1B3K C11 S    sing N N 19  
A1B3K S   C12  sing N N 20  
A1B3K C12 C13  sing N N 21  
A1B3K N1  C13  sing N N 22  
A1B3K C13 O2   doub N N 23  
A1B3K C14 C12  sing N N 24  
A1B3K N   C14  sing N N 25  
A1B3K N1  H14  sing N N 26  
A1B3K N1  H13  sing N N 27  
A1B3K C6  H6   sing N N 28  
A1B3K C8  H7   sing N N 29  
A1B3K C8  H8   sing N N 30  
A1B3K C10 H10  sing N N 31  
A1B3K C10 H9   sing N N 32  
A1B3K C12 H    sing N N 33  
A1B3K C11 H11  sing N N 34  
A1B3K C11 H12  sing N N 35  
A1B3K C14 H15  sing N N 36  
A1B3K C14 H16  sing N N 37  
A1B3K C   H2   sing N N 38  
A1B3K C   H1   sing N N 39  
A1B3K C   H3   sing N N 40  
A1B3K C3  H5   sing N N 41  
A1B3K C2  H4   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I53 
_atom_sites.fract_transf_matrix[1][1]   0.013727 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000595 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016216 
_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]   0.030505 
_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   ? 19.074 6.231   24.320 1.00 31.87 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.266 6.307   23.465 1.00 32.98 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.328 5.130   22.472 1.00 32.31 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.643 4.116   22.680 1.00 32.37 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.527 6.318   24.327 1.00 35.79 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.585 5.083   25.015 1.00 39.71 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.167 5.265   21.437 1.00 30.36 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.370 4.222   20.427 1.00 28.85 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.643 4.759   19.033 1.00 27.42 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.175 5.841   18.671 1.00 26.37 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.378 4.001   18.226 1.00 25.98 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.715 4.415   16.858 1.00 25.48 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.706 3.217   15.880 1.00 24.89 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.700 2.068   16.332 1.00 24.58 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.114 5.041   16.862 1.00 25.77 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.689 3.496   14.554 1.00 24.27 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.806 2.526   13.472 1.00 25.46 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.207 2.752   12.851 1.00 27.73 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.548 3.870   12.488 1.00 27.01 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.720 2.746   12.385 1.00 25.85 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.322 2.783   12.990 1.00 24.60 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.815 1.658   11.291 1.00 26.80 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.288 3.365   12.033 1.00 24.47 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.980 1.683   12.706 1.00 30.60 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.326 1.696   12.137 1.00 33.30 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.321 0.922   10.811 1.00 35.28 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.152 -0.290  10.830 1.00 36.00 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.289 1.020   13.133 1.00 33.83 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.433 1.838   14.395 1.00 34.18 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.224 2.979   14.421 1.00 35.08 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.701 1.530   15.532 1.00 34.89 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.321 3.765   15.562 1.00 36.14 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.792 2.306   16.679 1.00 35.84 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.590 3.435   16.683 1.00 36.82 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.695 4.201   17.811 1.00 38.13 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.442 1.621   9.676  1.00 36.14 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.397 1.036   8.328  1.00 37.71 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.492 1.659   7.457  1.00 39.20 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.476 2.865   7.199  1.00 39.66 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.992 1.180   7.676  1.00 39.19 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.429 2.592   7.848  1.00 38.96 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.026 0.789   6.207  1.00 40.98 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.467 0.848   7.027  1.00 39.57 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.586 1.338   6.244  1.00 41.67 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.392 2.331   7.057  1.00 44.02 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.593 2.103   8.254  1.00 45.37 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.724 3.485   6.478  1.00 44.30 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.438 4.507   7.240  1.00 44.46 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.447 5.529   7.856  1.00 41.17 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.826 6.660   8.103  1.00 40.18 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.521 5.161   6.396  1.00 49.41 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.575 4.155   5.978  1.00 57.61 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.129 3.411   6.798  1.00 59.00 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.874 4.076   4.690  1.00 61.79 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.205 5.104   8.167  1.00 38.82 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.201 6.027   8.715  1.00 37.11 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.662 5.630   10.087 1.00 34.13 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.536 4.455   10.376 1.00 33.68 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.005 6.152   7.753  1.00 37.12 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.355 6.741   6.409  1.00 39.24 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.977 7.977   6.312  1.00 40.42 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.011 6.091   5.233  1.00 40.78 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.306 8.523   5.079  1.00 42.45 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.298 6.644   3.994  1.00 42.59 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.973 7.847   3.919  1.00 44.27 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.285 8.399   2.695  1.00 47.34 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.302 6.634   10.903 1.00 32.08 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.653 6.484   12.199 1.00 30.08 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.364 7.316   12.121 1.00 27.71 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.405 8.487   11.785 1.00 27.33 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.565 6.947   13.349 1.00 30.21 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.864 7.190   14.700 1.00 32.26 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.892 7.607   15.751 1.00 36.30 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.400 8.599   16.711 1.00 36.71 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.864 8.302   17.892 1.00 37.35 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.699 7.032   18.257 1.00 35.05 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.472 9.271   18.712 1.00 36.59 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.210 6.687   12.354 1.00 25.03 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.902 7.342   12.311 1.00 24.06 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.408 7.470   13.724 1.00 22.34 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.251 6.460   14.397 1.00 22.99 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.870 6.543   11.485 1.00 23.96 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.616 7.396   11.228 1.00 23.89 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.466 6.007   10.175 1.00 23.33 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.096 8.678   14.161 1.00 20.67 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.595 8.906   15.519 1.00 20.52 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.383 9.848   15.484 1.00 18.25 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.227 10.606  14.518 1.00 17.04 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.682 9.548   16.421 1.00 22.82 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.671 8.513   16.900 1.00 24.95 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.355 10.740  15.725 1.00 22.84 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.615 9.945   16.608 1.00 17.85 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.595 11.002  16.722 1.00 17.65 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.380 12.335  16.733 1.00 17.86 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.404 12.449  17.440 1.00 19.37 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.831 10.914  18.073 1.00 18.76 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.030 9.645   18.196 1.00 20.19 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.535 8.619   18.678 1.00 23.22 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.791 9.669   17.753 1.00 18.57 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.918 13.305  15.968 1.00 17.32 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.574 14.618  15.864 1.00 16.80 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.623 15.301  17.231 1.00 19.35 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.644 15.908  17.579 1.00 20.57 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.831 15.483  14.827 1.00 16.10 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.611 16.757  14.440 1.00 17.11 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.668 17.672  13.677 1.00 18.26 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.287 18.902  13.144 1.00 20.51 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.391 20.040  13.824 1.00 22.59 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.031 20.096  15.106 1.00 20.24 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.884 21.130  13.238 1.00 24.23 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.538 15.173  18.036 1.00 19.86 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.500 15.786  19.387 1.00 22.15 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.500 15.164  20.386 1.00 24.98 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.771 15.738  21.447 1.00 26.41 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.068 15.814  19.959 1.00 22.09 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.534 14.500  20.453 1.00 23.04 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.909 13.606  19.599 1.00 23.20 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.482 14.005  21.722 1.00 23.10 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.503 12.592  20.363 1.00 24.12 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.843 12.772  21.645 1.00 24.22 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.072 13.985  20.034 1.00 24.89 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.046 13.348  20.903 1.00 26.37 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.484 13.364  20.327 1.00 27.80 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.371 12.731  20.908 1.00 29.24 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.571 11.911  21.194 1.00 25.85 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.236 11.833  21.962 1.00 26.96 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.792 10.388  22.164 1.00 27.56 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.358 12.483  23.344 1.00 27.45 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.696 13.986  19.144 1.00 27.60 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.010 14.034  18.512 1.00 28.77 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.044 14.694  19.424 1.00 30.71 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.711 15.632  20.143 1.00 30.59 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.936 14.782  17.185 1.00 28.30 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.275 14.175  19.407 1.00 32.52 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.409 14.639  20.223 1.00 35.16 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.244 15.725  19.473 1.00 36.66 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.013 15.961  18.292 1.00 35.57 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.314 13.415  20.532 1.00 37.66 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.973 13.012  19.330 1.00 39.72 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.565 12.251  21.136 1.00 38.55 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.288 16.303  20.123 1.00 39.04 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.159 17.266  19.444 1.00 41.49 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.890 16.556  18.289 1.00 41.50 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.024 17.129  17.211 1.00 41.43 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.208 17.838  20.414 1.00 45.20 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.651 18.665  21.530 1.00 51.06 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.089 19.902  21.297 1.00 54.37 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.684 18.440  22.868 1.00 53.51 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.764 20.380  22.489 1.00 55.32 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.108 19.534  23.467 1.00 55.00 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.373 15.311  18.519 1.00 41.52 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.052 14.535  17.470 1.00 42.39 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.140 14.337  16.264 1.00 39.57 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.572 14.607  15.144 1.00 40.24 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.529 13.171  17.965 1.00 46.43 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.324 12.440  16.913 1.00 53.30 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.377 12.926  16.464 1.00 55.36 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.798 11.299  16.450 1.00 54.19 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.861 13.949  16.485 1.00 36.24 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.879 13.811  15.399 1.00 33.18 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.792 15.077  14.564 1.00 30.60 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.877 15.005  13.344 1.00 30.78 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.488 13.482  15.956 1.00 32.38 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.364 12.079  16.492 1.00 34.42 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.930 11.150  15.865 1.00 33.94 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.732 11.908  17.549 1.00 35.58 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.666 16.242  15.215 1.00 28.80 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.555 17.497  14.474 1.00 28.66 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.884 17.875  13.753 1.00 31.95 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.837 18.524  12.708 1.00 32.79 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.064 18.614  15.419 1.00 27.31 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.566 18.664  15.577 1.00 25.67 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.827 18.177  16.619 1.00 26.18 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.629 19.240  14.651 1.00 23.99 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.480 18.442  16.405 1.00 25.89 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.332 19.037  15.179 1.00 24.65 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.750 19.813  13.383 1.00 23.74 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.183 19.523  14.542 1.00 23.97 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.614 20.278  12.748 1.00 23.34 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.343 20.098  13.308 1.00 23.44 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.050 17.493  14.315 1.00 33.92 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.366 17.783  13.713 1.00 37.41 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.646 16.878  12.488 1.00 39.39 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.532 17.195  11.679 1.00 41.08 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.490 17.589  14.744 1.00 38.12 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.968 15.719  12.413 1.00 37.59 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.073 14.791  11.301 1.00 37.30 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.687 14.661  10.600 1.00 34.44 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.326 13.597  10.145 1.00 33.58 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.583 13.454  11.800 1.00 40.75 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.016 13.514  12.274 1.00 48.18 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.938 13.776  11.492 1.00 52.92 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.242 13.250  13.553 1.00 47.83 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.946 15.768  10.507 1.00 33.41 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.614 15.792  9.894  1.00 30.85 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.624 15.376  8.411  1.00 31.90 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.443 15.880  7.642  1.00 33.12 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.022 17.196  10.024 1.00 29.00 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.638 17.412  9.407  1.00 27.48 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.558 16.533  10.117 1.00 28.47 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.261 18.874  9.434  1.00 25.31 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.678 14.480  8.007  1.00 29.95 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.466 14.083  6.620  1.00 29.43 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.133 14.715  6.148  1.00 28.52 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.076 15.398  5.117  1.00 30.07 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.406 12.546  6.496  1.00 31.33 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.959 12.148  5.097  1.00 32.74 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.765 11.908  6.838  1.00 32.57 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.083 14.569  6.971  1.00 26.09 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.752 15.078  6.696  1.00 24.20 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.925 15.124  8.007  1.00 21.87 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.140 14.325  8.902  1.00 21.72 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.080 14.139  5.672  1.00 24.03 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.605 14.337  5.452  1.00 24.43 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.008 15.255  4.636  1.00 25.54 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.543 13.570  6.040  1.00 24.07 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.637 15.102  4.675  1.00 25.79 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.325 14.092  5.550  1.00 24.74 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.502 12.521  6.970  1.00 23.81 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.083 13.539  5.892  1.00 23.72 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.270 11.996  7.327  1.00 23.19 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.082 12.500  6.789  1.00 22.96 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.044 16.098  8.120  1.00 19.62 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.133 16.218  9.251  1.00 18.96 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.807 16.831  8.748  1.00 19.28 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.802 17.623  7.792  1.00 19.02 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.751 17.015  10.409 1.00 19.16 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.345 18.378  10.035 1.00 19.32 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.345 19.511  9.888  1.00 23.82 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.625 20.455  9.112  1.00 25.53 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.279 19.463  10.545 1.00 24.08 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.703 16.452  9.389  1.00 17.85 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.396 16.954  9.027  1.00 17.51 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.584 17.096  10.300 1.00 16.56 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.152 16.118  10.901 1.00 16.96 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.735 16.063  7.987  1.00 19.49 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.478 16.654  7.395  1.00 23.91 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.833 17.492  8.070  1.00 23.43 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.123 16.267  6.255  1.00 25.41 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.395 18.346  10.724 1.00 15.39 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.670 18.639  11.943 0.50 15.66 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.664 18.605  11.970 0.50 15.72 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.216 18.149  11.836 1.00 15.89 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.632 17.730  12.809 1.00 17.25 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.729 20.145  12.201 0.50 17.31 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.719 20.087  12.344 0.50 17.67 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.943 20.506  13.313 0.50 20.42 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.997 20.817  11.372 0.50 21.30 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.627 18.246  10.622 1.00 15.51 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.238 17.834  10.448 1.00 15.86 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.062 16.320  10.635 1.00 16.16 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.930 15.896  10.839 1.00 17.70 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.697 18.300  9.102  1.00 19.20 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.169 17.481  8.049  1.00 23.21 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.142 15.529  10.490 1.00 14.87 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.144 14.036  10.648 1.00 14.89 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.740 13.564  11.987 1.00 15.87 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.678 12.387  12.288 1.00 16.44 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.889 13.336  9.495  1.00 16.40 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.226 13.569  8.151  1.00 16.97 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.002 12.923  7.013  1.00 19.60 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.020 11.457  7.125  1.00 19.78 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.141 10.639  6.072  1.00 19.69 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.266 11.135  4.843  1.00 20.17 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.134 9.318   6.244  1.00 20.37 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.342 14.487  12.767 1.00 16.55 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.078 14.198  14.002 1.00 14.99 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.238 13.236  13.688 1.00 14.43 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.518 12.362  14.498 1.00 14.61 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.171 13.627  15.115 1.00 14.63 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.900 13.381  16.428 1.00 18.10 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.696 14.241  16.829 1.00 18.20 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.683 12.310  17.044 1.00 18.37 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.870 13.355  12.491 1.00 13.98 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.016 12.498  12.131 1.00 13.27 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.302 13.274  11.891 1.00 15.77 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.295 14.372  11.354 1.00 17.14 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.761 11.679  10.828 1.00 13.54 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.694 10.539  10.918 1.00 16.36 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.591 9.798   9.558  1.00 15.67 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.990 9.550   12.053 1.00 18.07 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.415 12.652  12.225 1.00 16.05 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.745 13.176  11.957 1.00 17.45 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.593 11.975  11.618 1.00 18.57 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.458 10.921  12.259 1.00 19.08 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.338 13.969  13.153 1.00 18.59 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.720 14.605  12.897 1.00 21.37 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.835 15.903  13.585 1.00 22.55 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.891 13.677  13.333 1.00 23.16 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.412 12.097  10.569 1.00 19.93 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.348 11.038  10.144 1.00 21.19 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.763 11.642  10.199 1.00 23.70 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.001 12.747  9.680  1.00 23.65 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.055 10.431  8.742  1.00 22.05 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.122 9.376   8.339  1.00 23.94 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.662 9.792   8.706  1.00 22.29 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.667 10.937  10.882 1.00 25.17 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.062 11.344  10.945 1.00 27.95 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.946 10.248  10.376 1.00 31.76 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.547 9.083   10.310 1.00 29.15 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.472 11.705  12.368 1.00 28.21 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.292 10.615  13.258 1.00 29.52 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.187 10.629  9.991  1.00 35.59 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.130 9.654   9.444  1.00 40.14 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.945 8.941   10.540 1.00 45.22 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.164 9.488   11.621 1.00 46.37 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.071 10.351  8.475  1.00 41.35 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.740 11.378  9.180  1.00 43.65 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.402 7.726   10.260 1.00 48.26 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.170 6.935   11.224 1.00 53.16 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.422 6.376   10.565 1.00 58.44 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.409 6.088   9.368  1.00 59.13 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.354 5.728   11.728 1.00 54.03 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.164 4.812   10.653 1.00 55.67 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.012 6.110   12.324 1.00 53.56 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.447 6.103   11.365 1.00 62.02 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.694 5.512   10.885 1.00 65.37 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.546 3.981   10.766 1.00 67.08 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.162 3.351   9.896  1.00 69.41 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.844 5.912   11.833 1.00 67.84 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.463 5.545   13.164 1.00 70.35 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.156 7.405   11.787 1.00 68.13 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.765 3.364   11.664 1.00 66.06 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.550 1.925   11.636 1.00 65.66 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.358 1.589   10.746 1.00 65.01 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.438 2.398   10.599 1.00 64.78 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.324 1.411   13.043 1.00 66.11 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.376 0.396   10.150 1.00 64.73 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.335 -0.095  9.244  1.00 64.41 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.121 -0.726  9.976  1.00 62.95 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.285 -1.634  10.788 1.00 64.08 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.979 -1.062  8.221  1.00 67.16 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.016 -1.971  7.452  1.00 73.55 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.478 -1.356  6.181  1.00 81.32 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.736 -0.182  5.851  1.00 84.07 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.711 -2.152  5.438  1.00 82.20 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.919 -0.271  9.622  1.00 60.03 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.639 -0.730  10.160 1.00 58.21 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.007 -1.881  9.395  1.00 55.45 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.079 -1.939  8.163  1.00 55.73 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.337 -2.770  10.110 1.00 52.50 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.780 -3.974  9.501  1.00 50.92 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.269 -4.103  9.562  1.00 47.64 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.754 -5.195  9.248  1.00 47.83 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.450 -5.200  10.099 1.00 53.61 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.182 -5.380  9.628  1.00 62.64 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.557 -3.026  9.967  1.00 43.58 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.099 -3.070  10.008 1.00 42.00 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.553 -3.090  8.597  1.00 40.45 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.049 -2.402  7.702  1.00 41.18 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.451 -1.904  10.817 1.00 43.46 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.621 -1.961  12.326 1.00 47.57 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.804 -3.058  12.856 1.00 49.05 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.574 -0.892  12.975 1.00 49.08 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.543 -3.876  8.402  1.00 39.39 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.876 -3.991  7.118  1.00 39.55 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.659 -3.097  7.175  1.00 37.31 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.889 -3.206  8.120  1.00 37.29 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.471 -5.456  6.863  1.00 41.96 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.645 -6.219  6.533  1.00 45.57 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.446 -5.593  5.752  1.00 42.05 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.495 -2.207  6.201  1.00 35.03 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.307 -1.377  6.147  1.00 32.76 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.280 -2.101  5.279  1.00 32.26 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.619 -2.576  4.169  1.00 33.08 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.608 0.033   5.601  1.00 32.09 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.793 0.693   6.340  1.00 32.18 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.347 0.895   5.650  1.00 31.94 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.564 0.948   7.840  1.00 32.84 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.047 -2.209  5.781  1.00 30.13 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.929 -2.804  5.048  1.00 28.81 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.533 -1.856  3.893  1.00 29.28 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.568 -0.629  4.055  1.00 28.73 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.734 -2.987  5.995  1.00 27.15 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.165 -2.429  2.724  1.00 30.32 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.690 -1.656  1.570  1.00 32.29 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.375 -2.344  1.239  1.00 34.81 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.382 -3.341  0.505  1.00 37.35 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.690 -1.755  0.408  1.00 33.64 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.089 -1.255  0.738  1.00 35.22 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.145 0.222   1.160  1.00 36.76 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.518 0.634   1.470  1.00 36.20 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.844 1.756   2.106  1.00 35.80 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.902 2.593   2.515  1.00 32.10 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.115 2.034   2.363  1.00 35.04 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.266 -1.889  1.872  1.00 34.50 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.975 -2.580  1.841  1.00 34.10 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.815  -1.666  2.315  1.00 34.14 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.039 -0.532  2.730  1.00 32.84 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.082 -3.788  2.764  1.00 33.69 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.157 -3.324  4.525  1.00 30.18 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.573  -2.213  2.324  1.00 34.79 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.422  -1.473  2.835  1.00 35.47 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.748  -2.247  3.973  1.00 34.23 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.543  -2.133  4.162  1.00 35.19 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.428  -1.068  1.709  1.00 39.50 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.460  -2.140  1.231  1.00 46.40 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.690  -3.336  1.535  1.00 47.31 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.455  -1.783  0.579  1.00 50.60 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.526  -3.026  4.760  1.00 32.00 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.030  -3.768  5.929  1.00 28.94 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.305  -2.837  6.879  1.00 27.06 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.739  -1.711  7.089  1.00 28.07 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.191  -4.435  6.666  1.00 28.62 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.755  -5.996  5.950  1.00 29.60 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.241  -3.303  7.458  1.00 25.42 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.532  -2.607  8.509  1.00 25.08 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.527  -3.442  9.792  1.00 22.93 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.670  -3.220  10.643 1.00 23.26 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.101  -2.217  8.083  1.00 27.50 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.015  -0.850  7.373  1.00 30.61 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.572  -0.483  7.069  1.00 34.75 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.088  -0.613  5.936  1.00 35.58 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.835  -0.075  8.099  1.00 34.78 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.411  -4.474  9.906  1.00 20.71 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.564  -5.309  11.119 1.00 19.32 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.076  -5.440  11.405 1.00 16.65 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.902  -5.522  10.487 1.00 17.36 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.882  -6.726  11.041 1.00 23.88 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.552  -7.540  10.074 1.00 26.56 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.373  -6.676  10.734 1.00 24.39 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.415  -5.467  12.681 1.00 15.93 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.814  -5.575  13.075 1.00 14.62 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.957  -5.753  14.577 1.00 14.41 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.984  -6.008  15.277 1.00 15.79 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.179 -5.594  15.053 1.00 13.76 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.490 -5.734  16.489 1.00 14.61 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.357 -4.548  16.880 1.00 15.14 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.344 -4.277  16.197 1.00 14.91 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.224 -7.070  16.766 1.00 16.69 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.715 -7.139  18.225 1.00 17.81 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.331 -8.265  16.434 1.00 17.91 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.037 -3.871  18.006 1.00 14.84 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.916 -2.780  18.457 1.00 13.72 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.520 -3.062  19.833 1.00 14.69 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.949 -3.792  20.617 1.00 15.68 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.206 -1.389  18.434 1.00 13.20 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.242 -1.145  19.592 1.00 14.80 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.966  -1.708  19.595 1.00 15.92 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.559 -0.255  20.619 1.00 16.55 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.042  -1.407  20.592 1.00 17.80 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.651  0.016   21.654 1.00 17.90 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.398  -0.582  21.645 1.00 18.65 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.466  -0.353  22.635 1.00 19.90 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.658 -2.460  20.114 1.00 14.16 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.290 -2.576  21.425 1.00 16.47 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.842 -1.425  22.310 1.00 17.95 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.920 -0.244  21.922 1.00 16.47 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.804 -2.639  21.329 1.00 17.12 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.405 -2.783  22.713 1.00 19.89 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.218 -3.941  23.451 1.00 21.57 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.118 -1.742  23.294 1.00 21.38 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.769 -4.088  24.720 1.00 23.38 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.660 -1.863  24.572 1.00 23.18 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.492 -3.046  25.275 1.00 25.20 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.986 -3.140  26.556 1.00 28.56 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.363 -1.776  23.521 1.00 19.36 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.887 -0.777  24.479 1.00 21.41 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.775 -0.813  25.713 1.00 24.31 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.573 -1.681  26.561 1.00 25.06 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.424 -1.027  24.836 1.00 22.21 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.804 0.004   26.202 1.00 25.30 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.717 0.168   25.835 1.00 25.54 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.671 0.245   26.918 1.00 27.76 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.024 0.393   28.279 1.00 29.51 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.532 -0.198  29.241 1.00 32.06 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.696 1.355   26.692 1.00 32.76 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.112 2.647   26.674 1.00 37.92 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.893 1.132   28.377 1.00 28.95 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.181 1.322   29.673 1.00 29.83 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.544 0.029   30.219 1.00 30.99 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.018 0.023   31.348 1.00 33.98 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.127 2.422   29.572 1.00 29.32 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.075 2.028   28.704 1.00 30.21 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.567 -1.059  29.424 1.00 29.69 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.070 -2.353  29.886 1.00 29.79 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.107 -3.472  29.696 1.00 31.61 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.806 -4.615  30.038 1.00 33.12 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.790 -2.742  29.139 1.00 29.75 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.583  -1.881  29.457 1.00 32.17 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.996  -2.217  30.817 1.00 34.32 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.742  -1.490  31.017 1.00 37.49 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.657  -0.270  31.538 1.00 38.81 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.748  0.352   31.979 1.00 38.71 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.474  0.319   31.671 1.00 39.11 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.293 -3.179  29.081 1.00 31.19 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.334 -4.160  28.734 1.00 31.15 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.696 -5.319  27.950 1.00 29.67 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.922 -6.496  28.239 1.00 29.31 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.093 -4.640  29.985 1.00 34.19 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.203 -3.695  30.391 1.00 40.06 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 18.029 -4.276  31.526 1.00 47.58 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.603 -3.219  32.350 1.00 55.52 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.517 -3.170  33.677 1.00 60.93 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.888 -4.133  34.346 1.00 62.27 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 19.039 -2.147  34.344 1.00 62.41 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.822 -4.965  26.983 1.00 27.26 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 13.070 -5.978  26.242 1.00 25.53 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.829 -5.550  24.815 1.00 22.72 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.734 -4.344  24.524 1.00 21.36 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.647 -6.113  26.829 1.00 28.28 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.433 -7.094  27.940 1.00 34.99 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.946  -7.100  28.280 1.00 39.80 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.521  -8.325  29.060 1.00 45.04 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.826  -8.199  30.515 1.00 46.36 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.653 -6.544  23.945 1.00 20.13 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.255 -6.283  22.574 1.00 18.87 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.719 -6.548  22.484 1.00 19.88 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.178 -7.448  23.150 1.00 20.71 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.014 -7.192  21.595 1.00 19.02 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.499 -7.012  21.576 1.00 19.38 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.139 -6.335  20.538 1.00 22.13 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.434 -7.490  22.415 1.00 20.36 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.433 -6.411  20.805 1.00 21.04 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.657 -7.047  21.943 1.00 22.58 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.013 -5.764  21.670 1.00 18.32 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.562  -5.927  21.514 1.00 17.43 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.188  -6.026  20.046 1.00 16.81 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.656  -5.231  19.242 1.00 16.16 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.835  -4.707  22.115 1.00 18.34 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.922  -4.633  23.619 1.00 20.45 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.208  -5.512  24.420 1.00 22.46 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.651  -3.632  24.245 1.00 23.04 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.239  -5.416  25.812 1.00 24.20 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.701  -3.535  25.638 1.00 24.53 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 8.002  -4.439  26.414 1.00 25.58 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.983  -4.343  27.794 1.00 28.56 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.335  -6.980  19.674 1.00 16.31 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.860  -7.039  18.268 1.00 17.08 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.733  -5.984  18.082 1.00 18.49 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.867  -5.836  18.988 1.00 20.11 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.297  -8.464  18.156 1.00 17.66 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.820  -8.778  19.564 1.00 18.34 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.718  -8.021  20.534 1.00 17.10 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.715  -5.290  16.937 1.00 18.10 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.723  -4.250  16.704 1.00 19.65 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.294  -4.165  15.254 1.00 19.39 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.052  -4.504  14.331 1.00 17.89 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.271  -2.826  17.086 1.00 20.39 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.294  -2.564  18.594 1.00 22.74 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.613  -2.553  16.424 1.00 19.12 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.064  -3.643  15.050 1.00 19.21 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.588  -3.220  13.729 1.00 20.49 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.824  -1.719  13.736 1.00 20.83 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.692  -1.089  14.801 1.00 22.25 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.093  -3.462  13.549 1.00 23.68 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.796  -4.843  13.583 1.00 30.26 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.264  -1.155  12.615 1.00 19.30 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.567  0.270   12.589 1.00 19.35 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.055  0.925   11.321 1.00 21.66 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.841  0.243   10.317 1.00 23.73 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.060  0.538   12.869 1.00 18.58 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.039  -0.156  11.942 1.00 17.64 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.565  -1.395  12.268 1.00 16.77 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.463  0.456   10.769 1.00 18.58 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.464  -2.033  11.403 1.00 17.66 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.369  -0.172  9.913  1.00 18.44 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.863  -1.417  10.236 1.00 17.65 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.786  2.247   11.375 1.00 20.87 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.172  2.918   10.241 1.00 22.90 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.198  3.276   9.118  1.00 22.55 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.399  3.095   9.309  1.00 21.87 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.428  4.162   10.728 1.00 25.66 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.370  5.125   11.186 1.00 25.15 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.734  3.716   7.929  1.00 24.43 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.663  4.108   6.859  1.00 26.46 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.325  5.452   7.213  1.00 26.86 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.691  6.268   7.876  1.00 27.72 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.940  4.180   5.494  1.00 30.74 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.497  2.790   5.025  1.00 35.75 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.327  2.664   3.488  1.00 42.30 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.116  1.199   3.169  1.00 48.92 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.285  0.889   1.722  1.00 54.34 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.584  5.721   6.781  1.00 26.00 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.206  7.016   7.121  1.00 26.67 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.383  8.204   6.654  1.00 28.02 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.950  8.258   5.490  1.00 27.63 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.587  6.985   6.450  1.00 27.73 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.698  5.685   5.740  1.00 28.24 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.459  4.864   5.963  1.00 25.70 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.100  9.123   7.576  1.00 28.89 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.251  10.273  7.246  1.00 30.28 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.573  11.502  8.144  1.00 29.83 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.436  11.416  9.035  1.00 28.26 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.776  9.851   7.336  1.00 34.29 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.370  9.634   8.678  1.00 39.54 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.905  12.647  7.892  1.00 30.08 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.063  13.875  8.681  1.00 31.02 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.129  13.753  9.886  1.00 31.84 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.907  13.602  9.711  1.00 33.54 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.621  15.115  7.859  1.00 31.44 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.615  15.744  6.904  1.00 32.98 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.913  16.797  5.998  1.00 34.70 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.719  16.462  7.652  1.00 33.69 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.725  13.850  11.106 1.00 30.85 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.987  13.688  12.421 1.00 32.00 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.404  14.710  13.532 1.00 33.76 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.611  14.985  13.619 1.00 32.97 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.103  12.230  12.965 1.00 32.54 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.303  11.222  12.135 1.00 33.49 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.731  12.150  14.434 1.00 33.51 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.958  9.875   11.990 1.00 35.32 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.478  15.228  14.383 1.00 34.87 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.717  16.231  15.483 1.00 37.76 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.594  15.823  16.695 1.00 36.97 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 3.315  14.816  17.305 1.00 37.15 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.368  16.625  16.109 1.00 40.74 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.368  17.884  16.938 1.00 43.83 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.323  19.133  16.343 1.00 46.24 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.419  17.812  18.319 1.00 45.65 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.332  20.282  17.117 1.00 47.90 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.424  18.961  19.093 1.00 46.88 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.379  20.194  18.489 1.00 47.41 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.501  16.708  17.070 1.00 35.95 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.442  16.406  18.180 1.00 36.32 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.553  17.629  19.068 1.00 38.32 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.935  18.693  18.584 1.00 38.69 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.810  15.898  17.690 1.00 35.31 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.682  15.518  18.867 1.00 34.95 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.642  14.716  16.752 1.00 35.59 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 5.351  17.381  20.345 1.00 39.72 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 5.312  18.455  21.308 1.00 41.29 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.717  18.966  21.595 1.00 41.20 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.677  18.435  21.082 1.00 40.63 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.523  17.846  22.456 1.00 45.41 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 3.082  17.526  22.085 1.00 54.35 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 2.014  18.077  23.025 1.00 63.74 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.365  18.794  23.973 1.00 66.83 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.828  17.806  22.791 1.00 66.79 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.798  19.807  22.588 1.00 41.41 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 8.085  20.506  22.789 1.00 41.80 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 9.055  19.675  23.615 1.00 42.38 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 8.572  18.932  24.438 1.00 43.42 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.833  21.844  23.442 1.00 41.75 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 10.359 19.814  23.412 1.00 41.43 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 11.404 19.209  24.239 1.00 41.03 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 12.516 20.213  24.419 1.00 41.19 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 12.345 21.378  24.011 1.00 40.78 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.971 18.085  23.481 1.00 41.85 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 12.337 18.484  22.183 1.00 42.68 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 13.630 19.758  24.991 1.00 41.30 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 14.768 20.701  24.957 1.00 41.25 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 15.366 20.455  23.574 1.00 38.45 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 16.539 20.821  23.363 1.00 38.48 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 15.768 20.504  26.096 1.00 46.79 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.101 20.128  27.398 1.00 54.50 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.595 18.705  27.332 1.00 65.87 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 15.439 17.804  27.389 1.00 68.42 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.370 18.519  27.157 1.00 69.54 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.582 19.843  22.668 1.00 35.31 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.212 19.538  21.374 1.00 32.50 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.263 19.975  20.264 1.00 29.87 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.780 20.429  19.225 1.00 29.88 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.695 18.101  21.380 1.00 32.01 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.995 17.501  22.724 1.00 31.94 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.267 17.545  23.255 1.00 32.91 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.024 16.807  23.414 1.00 32.77 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.557 16.938  24.461 1.00 34.55 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.290 16.210  24.630 1.00 34.34 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.561 16.280  25.157 1.00 35.94 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.836 15.682  26.350 1.00 39.36 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.945 19.861  20.453 1.00 28.32 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.040 20.526  19.465 1.00 26.81 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.690 20.900  20.076 1.00 29.16 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.261 20.222  21.000 1.00 29.42 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.733 19.709  18.216 1.00 23.96 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.874 18.945  17.642 1.00 20.57 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.208 17.713  18.165 1.00 19.84 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.590 19.446  16.574 1.00 19.74 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.253 16.988  17.642 1.00 17.70 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.637 18.726  16.036 1.00 18.81 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.952 17.488  16.562 1.00 18.35 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.976 16.747  16.070 1.00 18.14 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.004 21.957  19.585 1.00 30.01 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.665  22.308  20.060 1.00 31.32 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.563  21.862  19.089 1.00 32.12 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.892  21.457  17.989 1.00 32.13 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.760  23.835  20.035 1.00 32.42 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.571  24.121  18.784 1.00 31.83 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.501 22.934  18.615 1.00 30.01 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.295  21.964  19.504 1.00 33.42 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.152  21.575  18.641 1.00 34.10 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.499  21.785  17.162 1.00 33.02 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.816  22.933  16.790 1.00 33.38 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.930  22.367  19.033 1.00 34.72 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.418  20.723  16.351 1.00 31.28 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.785  20.819  14.913 1.00 29.82 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.414  19.528  14.187 1.00 29.08 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.149  18.578  14.864 1.00 29.20 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.302  20.998  14.769 1.00 29.37 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.091  19.705  14.565 1.00 29.73 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.530  19.771  15.037 1.00 27.36 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.461 18.768  14.558 1.00 26.21 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.634 17.603  15.152 1.00 23.63 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.509 16.736  14.680 1.00 20.14 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.937  17.320  16.235 1.00 23.34 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.384  19.531  12.860 1.00 29.06 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.228  18.258  12.086 1.00 29.56 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.612  17.591  11.952 1.00 26.58 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.547  18.325  11.803 1.00 25.96 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.532  18.503  10.746 1.00 32.43 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.110  18.009  10.743 1.00 36.73 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.414  17.872  11.931 1.00 40.08 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.466  17.666  9.567  1.00 38.94 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.109  17.414  11.949 1.00 42.53 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.162  17.204  9.569  1.00 41.10 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.480  17.077  10.765 1.00 43.83 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.808 16.625  10.778 1.00 47.90 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.750  16.308  12.258 1.00 23.48 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.972  15.544  12.010 1.00 20.83 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.658  14.628  10.826 1.00 20.58 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.606  13.957  10.814 1.00 20.84 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.375  14.713  13.234 1.00 19.56 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.663  13.859  12.953 1.00 17.01 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.291 13.342  14.229 1.00 19.85 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.411 14.069  15.245 1.00 18.89 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.803 12.109  14.177 1.00 17.29 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.480  14.675  9.799  1.00 18.91 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.267  13.877  8.602  1.00 19.30 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.968  12.524  8.709  1.00 19.80 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.855  12.343  9.576  1.00 19.68 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.785  14.637  7.392  1.00 20.60 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.189 14.805  7.484  1.00 22.23 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.527  11.574  7.868  1.00 19.98 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.087  10.240  7.797  1.00 19.44 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.927  9.497   9.127  1.00 19.02 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.756  8.653   9.430  1.00 18.87 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.549 10.319  7.359  1.00 19.50 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.680 10.944  5.992  1.00 22.31 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.706 10.171  4.843  1.00 26.37 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.707 12.251  5.631  1.00 23.96 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.764 11.027  3.828  1.00 26.72 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.740 12.287  4.251  1.00 25.50 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.856  9.789   9.899  1.00 19.27 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.640  9.162   11.223 1.00 19.22 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.596  8.030   11.104 1.00 18.47 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.590  8.192   10.409 1.00 20.08 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.109  10.252  12.204 1.00 18.98 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.031  9.923   13.708 1.00 19.89 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.408  9.481   14.252 1.00 19.80 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.440  11.143  14.516 1.00 22.29 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.802  6.917   11.840 1.00 17.03 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.882  5.753   11.810 1.00 17.82 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.442  5.448   13.248 1.00 19.51 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.305  5.346   14.123 1.00 20.66 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.635  4.535   11.226 1.00 17.67 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.131  4.764   9.766  1.00 20.55 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.237  3.431   9.266  1.00 22.84 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.609  3.671   10.376 1.00 23.45 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.128  5.327   13.509 1.00 18.83 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.648  5.061   14.860 1.00 19.82 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.251  3.603   15.077 1.00 19.93 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.739  2.948   14.179 1.00 20.43 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.450  5.974   15.232 1.00 20.95 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.727  7.482   15.246 1.00 24.39 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.552  8.251   15.801 1.00 26.82 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.927  7.825   16.067 1.00 24.89 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.421  3.143   16.304 1.00 20.00 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.056  1.802   16.755 1.00 20.71 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.483  1.920   18.161 1.00 21.83 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.803  2.868   18.899 1.00 21.89 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.294  0.943   16.830 1.00 21.24 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.607  0.982   18.532 1.00 21.98 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.085  0.927   19.897 1.00 24.02 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.159  0.180   20.722 1.00 26.27 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.475  -0.979  20.428 1.00 27.74 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.276 0.190   19.967 1.00 26.00 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.720 -0.005  21.408 1.00 27.75 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.350 0.938   19.181 1.00 25.62 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.757  0.860   21.687 1.00 26.70 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.808  0.258   22.493 1.00 27.62 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.381  1.195   23.528 1.00 27.82 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.153  2.413   23.488 1.00 29.51 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.115  0.626   24.476 1.00 25.82 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.733  1.389   25.518 1.00 25.13 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.006  2.109   25.071 1.00 23.87 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.886  1.520   24.463 1.00 22.62 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.028  0.498   26.730 1.00 25.39 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.606  1.272   27.865 1.00 29.20 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.828  2.124   28.607 1.00 33.71 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.898  1.437   28.224 1.00 30.50 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.659  2.735   29.442 1.00 34.02 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.916  2.343   29.241 1.00 32.81 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.151  3.348   25.520 1.00 23.41 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.377  4.097   25.340 1.00 25.39 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.449  5.241   26.372 1.00 28.29 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.428  5.705   26.850 1.00 30.30 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.506  4.656   23.929 1.00 25.58 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.570  5.700   23.716 1.00 28.40 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.665  5.622   26.750 1.00 29.16 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.005 6.748   27.619 1.00 30.54 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.087 7.579   26.892 1.00 31.73 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.654 7.074   25.907 1.00 32.04 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.437 6.276   29.018 1.00 33.78 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.342  5.449   29.668 1.00 38.61 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.676  4.738   30.962 1.00 44.73 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.502 5.259   31.740 1.00 44.40 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.100  3.654   31.198 1.00 46.00 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.336 8.869   27.251 1.00 32.37 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.279 9.680   26.438 1.00 31.70 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.649 9.043   26.169 1.00 30.62 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.161 9.127   25.043 1.00 30.58 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.397 10.993  27.219 1.00 32.62 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.110 11.110  27.965 1.00 33.47 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.698 9.671   28.314 1.00 32.20 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.212 8.391   27.179 1.00 30.20 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.487 7.685   27.086 1.00 29.54 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.485 6.503   26.121 1.00 27.79 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.545 5.947   25.807 1.00 28.45 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.292 6.078   25.646 1.00 25.57 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.193 4.999   24.665 1.00 23.14 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.600 5.421   23.272 1.00 21.43 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.787 4.553   22.397 1.00 21.82 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.796 4.363   24.621 1.00 23.15 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.551 3.500   25.844 1.00 25.52 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.510 2.904   26.342 1.00 25.10 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.417 3.497   26.347 1.00 27.09 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.726 6.752   23.021 1.00 20.85 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.135 7.246   21.683 1.00 20.01 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.452 6.582   21.275 1.00 19.93 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.343 6.430   22.120 1.00 20.49 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.255 8.766   21.682 1.00 20.60 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.663 9.644   21.637 1.00 22.69 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.543 6.132   20.032 1.00 19.47 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.755 5.450   19.571 1.00 19.51 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.616 3.934   19.495 1.00 19.94 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.454 3.266   18.877 1.00 20.52 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.577 3.369   20.119 1.00 18.20 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.331 1.922   20.015 1.00 16.81 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.995 1.556   18.565 1.00 15.36 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.239 2.260   17.895 1.00 14.84 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.582 0.479   18.079 1.00 14.93 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.346 0.052   16.710 1.00 15.31 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.040 -0.701  16.542 1.00 15.00 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.689 -1.581  17.367 1.00 16.13 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.591 -0.766  16.236 1.00 18.87 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.747 0.171   15.827 1.00 21.36 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.277 -1.808  15.157 1.00 19.96 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.185 -0.602  15.754 1.00 23.63 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.368 -0.409  15.409 1.00 14.74 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.196 -1.132  14.920 1.00 14.75 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.709 -1.979  13.708 1.00 15.70 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.381 -1.432  12.800 1.00 14.85 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.135 -0.137  14.392 1.00 15.81 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.932 -0.801  13.675 1.00 16.48 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.159 -1.800  14.635 1.00 16.34 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.952  0.289   13.168 1.00 17.19 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.449 -3.297  13.715 1.00 16.35 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.944 -4.160  12.646 1.00 17.91 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.818 -5.033  12.135 1.00 18.66 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.995 -5.466  12.908 1.00 18.13 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.963 -5.185  13.192 1.00 21.45 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.204 -4.704  13.875 1.00 29.71 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.053 -5.901  14.314 1.00 32.62 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.539 -6.558  13.108 1.00 34.70 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.686 -6.267  12.510 1.00 35.93 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.988 -6.817  11.350 1.00 35.71 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.560 -5.453  13.091 1.00 37.15 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.867 -5.378  10.855 1.00 19.14 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.965 -6.352  10.232 1.00 21.52 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.886 -7.497  9.700  1.00 24.23 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.103 -7.452  9.913  1.00 24.53 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.159 -5.690  9.108  1.00 21.60 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.175 -5.110  7.711  1.00 22.25 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.330 -8.539  9.046  1.00 26.66 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.157 -9.623  8.487  1.00 29.90 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.205 -9.136  7.458  1.00 31.60 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.187 -9.853  7.170  1.00 32.73 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.250 -10.652 7.811  1.00 33.39 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.426 -10.066 6.665  1.00 37.42 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.559 -11.152 6.096  1.00 43.66 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.360  -11.243 6.397  1.00 47.26 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.169 -12.040 5.324  1.00 42.54 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.973 -7.949  6.858  1.00 30.50 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.897 -7.410  5.836  1.00 30.36 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.063 -6.622  6.444  1.00 29.11 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.025 -6.323  5.740  1.00 30.70 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.149 -6.562  4.781  1.00 31.96 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.997 -7.259  4.125  1.00 36.70 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.687 -6.944  4.440  1.00 38.89 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.993 -8.238  3.184  1.00 38.95 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.929 -7.766  3.734  1.00 40.08 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.668 -8.567  2.958  1.00 40.39 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.971 -6.260  7.736  1.00 26.36 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.026 -5.495  8.377  1.00 23.95 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.516 -4.305  9.196  1.00 21.37 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.379 -4.301  9.655  1.00 21.14 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.367 -3.291  9.366  1.00 20.99 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.058 -2.084  10.143 1.00 20.48 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.059 -1.172  9.428  1.00 19.83 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.296 -0.769  8.282  1.00 20.87 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.344 -1.302  10.531 1.00 22.28 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.993 0.006   11.251 1.00 22.83 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.243 -2.160  11.414 1.00 23.35 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.937 -0.878  10.082 1.00 18.72 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.896 -0.017  9.521  1.00 17.62 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.041 1.443   9.976  1.00 17.02 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.832 2.384   9.212  1.00 17.50 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.499 -0.580  9.918  1.00 18.09 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.369 0.336   9.480  1.00 18.72 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.296 -2.003  9.410  1.00 18.60 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.330 1.614   11.262 1.00 15.10 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.466 2.962   11.820 1.00 15.53 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.834 2.976   13.279 1.00 15.41 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.235 1.952   13.812 1.00 15.67 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.735 4.152   13.911 1.00 14.35 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.069 4.242   15.341 1.00 13.76 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.945 4.932   16.119 1.00 13.43 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.266 5.785   15.571 1.00 12.97 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.418 5.004   15.552 1.00 15.32 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.463 6.339   14.780 1.00 16.93 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.652 4.123   15.242 1.00 16.67 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.673 7.240   15.250 1.00 18.44 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.757 4.603   17.419 1.00 13.04 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.764 5.312   18.243 1.00 12.94 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.078 6.821   18.244 1.00 13.43 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.215 7.202   18.429 1.00 13.85 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.709 4.801   19.695 1.00 14.64 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.679 5.582   20.500 1.00 15.81 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.379 3.308   19.728 1.00 15.63 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.084 7.702   18.092 1.00 13.99 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.317 9.179   17.974 1.00 14.55 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.257 9.968   18.772 1.00 17.03 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.525 11.107  19.139 1.00 17.44 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.372 9.637   16.498 1.00 15.43 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.451 11.042  16.377 1.00 18.24 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.098 9.333   18.982 1.00 18.49 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.049  9.935   19.822 1.00 20.95 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.204  8.844   20.456 1.00 22.49 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.352  7.690   20.164 1.00 20.94 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.084  10.864  19.064 1.00 22.45 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.158  10.110  18.275 1.00 24.54 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.768  11.886  18.178 1.00 22.42 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.282  9.301   21.283 1.00 25.44 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.307  8.383   21.857 1.00 28.46 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.488  9.166   22.855 1.00 32.30 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.841  10.310  23.227 1.00 33.21 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.448  8.554   23.311 1.00 34.84 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.679  9.246   24.349 1.00 38.32 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.306  8.683   24.301 1.00 40.49 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.870  8.431   23.216 1.00 40.15 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.665  8.569   25.467 1.00 42.04 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.286  8.008   25.579 1.00 44.19 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 0.137  6.521   25.197 1.00 42.49 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.954 6.161   24.740 1.00 44.10 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.690 8.864   24.787 1.00 48.33 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.779 10.296  25.277 1.00 55.32 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.879 10.538  26.476 1.00 58.99 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.726 11.251  24.362 1.00 54.98 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 1.198  5.689   25.340 1.00 39.26 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 1.088  4.286   24.909 1.00 37.05 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.416  4.126   23.428 1.00 34.54 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.116  3.070   22.878 1.00 35.59 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.964  5.167   22.820 1.00 31.47 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.367  5.117   21.395 1.00 29.08 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.870  5.326   21.309 1.00 26.80 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.387  6.097   22.080 1.00 28.59 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.644  6.220   20.612 1.00 29.69 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.128  6.041   20.528 1.00 33.32 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.556 7.386   20.380 1.00 35.10 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.245 5.106   19.384 1.00 34.21 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.460  4.745   20.266 1.00 21.90 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.909  4.891   20.061 1.00 19.45 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.106  5.319   18.602 1.00 19.03 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.448  4.778   17.738 1.00 19.97 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.667  3.604   20.438 1.00 19.66 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.210  2.373   19.680 1.00 19.88 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.175  3.800   20.345 1.00 19.98 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.942  6.334   18.426 1.00 16.58 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.193  6.818   17.060 1.00 15.78 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.608  6.478   16.604 1.00 17.00 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.527  6.655   17.366 1.00 18.06 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.722  6.020   15.358 1.00 15.72 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.048 5.634   14.794 1.00 14.14 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.430 6.546   13.596 1.00 14.69 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.582  6.742   12.737 1.00 15.06 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.041 4.156   14.380 1.00 14.02 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.546  3.173   15.411 1.00 14.90 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.400 2.660   16.372 1.00 15.44 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.221  2.768   15.424 1.00 15.40 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.937  1.760   17.317 1.00 15.39 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.762  1.859   16.363 1.00 16.04 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.622  1.357   17.310 1.00 15.75 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.678 7.033   13.548 1.00 13.84 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.125 7.818   12.400 1.00 13.59 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.577 6.774   11.358 1.00 14.81 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.487 5.967   11.626 1.00 13.93 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.298 8.714   12.824 1.00 13.96 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.911 6.740   10.193 1.00 15.37 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.270 5.780   9.142  1.00 16.79 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.650 6.099   8.524  1.00 16.83 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.000 7.275   8.379  1.00 17.57 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.196 5.845   8.034  1.00 20.15 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.404 4.831   6.943  1.00 24.56 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.600 3.656   7.273  1.00 24.30 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.393 5.231   5.734  1.00 27.10 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.421 5.056   8.125  1.00 15.78 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.707 5.308   7.429  1.00 17.74 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.782 4.541   6.075  1.00 20.51 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.794 4.621   5.379  1.00 22.44 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.949 4.976   8.296  1.00 17.93 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.971 5.803   9.590  1.00 17.11 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.002 3.468   8.587  1.00 17.94 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.747 3.751   5.742  1.00 20.69 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.731 2.886   4.566  1.00 21.99 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.862 3.613   3.236  1.00 25.47 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.361 3.034   2.274  1.00 26.91 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.472 2.033   4.569  1.00 22.20 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.345 1.160   5.807  1.00 21.67 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.036 0.395   5.725  1.00 20.64 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.889 1.233   6.092  1.00 21.79 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.653  0.774   6.242  1.00 22.50 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.367  -0.490  5.954  1.00 23.15 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.683  1.584   6.654  1.00 21.75 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.468 4.887   3.189  1.00 25.89 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.543 5.656   1.957  1.00 26.40 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.962 6.194   1.674  1.00 26.84 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.238 6.671   0.553  1.00 27.93 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.530 6.816   1.999  1.00 27.34 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.811 7.849   3.076  1.00 28.57 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.115 7.445   4.228  1.00 25.83 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.729 9.077   2.770  1.00 28.28 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.835 6.242   2.702  1.00 26.39 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.189 6.817   2.580  1.00 26.01 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.085 5.845   1.886  1.00 29.15 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.889 5.138   2.511  1.00 29.14 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.741 7.177   3.969  1.00 24.95 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.831 8.048   4.829  1.00 23.80 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.424 8.252   6.207  1.00 22.33 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.545 9.394   4.149  1.00 24.59 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.897 5.756   0.567  1.00 31.74 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.585 4.757   -0.239 1.00 34.91 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.106 4.941   -0.205 1.00 37.16 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.829 3.946   -0.262 1.00 37.99 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.029 4.738   -1.683 1.00 36.42 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.500 4.673   -1.857 1.00 38.22 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.113 4.566   -3.351 1.00 40.27 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.870 3.530   -1.047 1.00 38.85 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.587 6.198   0.011  1.00 37.35 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.010 6.533   0.039  1.00 37.52 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.775 5.948   1.229  1.00 39.81 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.007 5.891   1.179  1.00 40.96 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.238 8.046   -0.067 1.00 36.14 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.512 8.836   0.977  1.00 34.81 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.263 9.375   0.882  1.00 34.83 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.994 9.165   2.284  1.00 34.11 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.955 10.053  2.037  1.00 34.67 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.009 9.954   2.908  1.00 34.39 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.211 8.958   2.951  1.00 34.45 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.149 10.426  4.211  1.00 34.57 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.364 9.467   4.227  1.00 34.81 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.340 10.191  4.842  1.00 34.60 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.071 5.450   2.265  1.00 40.05 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.734 4.825   3.408  1.00 41.37 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.593 3.612   3.003  1.00 46.91 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.532 3.270   3.722  1.00 47.11 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.687 4.405   4.457  1.00 39.51 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.954 5.551   5.144  1.00 37.73 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.898 5.007   6.127  1.00 36.82 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.930 6.479   5.877  1.00 37.53 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.268 2.969   1.854  1.00 51.02 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.967 1.806   1.304  1.00 55.84 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.025 2.128   0.252  1.00 61.05 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.598 1.189   -0.307 1.00 63.21 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.955 0.892   0.631  1.00 58.21 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.065 0.186   1.603  1.00 62.64 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.593 -0.373  2.588  1.00 64.16 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.839 0.180   1.381  1.00 64.31 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.238 3.404   -0.088 1.00 63.44 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.215 3.758   -1.127 1.00 65.89 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.994 5.030   -0.802 1.00 67.65 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.786 5.506   -1.631 1.00 68.61 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.522 3.889   -2.491 1.00 68.83 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.407 4.925   -2.498 1.00 74.51 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.191 4.557   -3.327 1.00 81.98 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.438 5.479   -3.720 1.00 83.58 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.989 3.347   -3.583 1.00 84.34 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B3K B 2 .   ? 11.658 13.613  17.996 1.00 20.22 ? 201 A1B3K A N1  1 
HETATM 1079 C  C4  . A1B3K B 2 .   ? 7.369  10.292  26.352 1.00 35.03 ? 201 A1B3K A C4  1 
HETATM 1080 C  C5  . A1B3K B 2 .   ? 6.256  10.657  27.283 1.00 40.07 ? 201 A1B3K A C5  1 
HETATM 1081 C  C6  . A1B3K B 2 .   ? 8.293  11.254  25.970 1.00 33.02 ? 201 A1B3K A C6  1 
HETATM 1082 C  C7  . A1B3K B 2 .   ? 9.279  10.992  25.032 1.00 30.10 ? 201 A1B3K A C7  1 
HETATM 1083 C  C8  . A1B3K B 2 .   ? 10.185 12.091  24.528 1.00 28.45 ? 201 A1B3K A C8  1 
HETATM 1084 C  C10 . A1B3K B 2 .   ? 11.577 14.271  23.341 1.00 25.02 ? 201 A1B3K A C10 1 
HETATM 1085 C  C13 . A1B3K B 2 .   ? 11.215 14.451  18.919 1.00 22.03 ? 201 A1B3K A C13 1 
HETATM 1086 O  O2  . A1B3K B 2 .   ? 10.792 15.577  18.651 1.00 22.22 ? 201 A1B3K A O2  1 
HETATM 1087 C  C12 . A1B3K B 2 .   ? 11.337 13.952  20.352 1.00 23.89 ? 201 A1B3K A C12 1 
HETATM 1088 S  S   . A1B3K B 2 .   ? 12.725 14.962  20.931 1.00 25.34 ? 201 A1B3K A S   1 
HETATM 1089 C  C11 . A1B3K B 2 .   ? 12.856 14.167  22.550 1.00 24.86 ? 201 A1B3K A C11 1 
HETATM 1090 C  C14 . A1B3K B 2 .   ? 10.171 14.151  21.314 1.00 24.54 ? 201 A1B3K A C14 1 
HETATM 1091 N  N   . A1B3K B 2 .   ? 10.467 13.618  22.648 1.00 25.28 ? 201 A1B3K A N   1 
HETATM 1092 C  C9  . A1B3K B 2 .   ? 9.776  12.580  23.150 1.00 26.12 ? 201 A1B3K A C9  1 
HETATM 1093 O  O1  . A1B3K B 2 .   ? 8.881  12.048  22.534 1.00 24.73 ? 201 A1B3K A O1  1 
HETATM 1094 C  C1  . A1B3K B 2 .   ? 9.360  9.704   24.505 1.00 29.15 ? 201 A1B3K A C1  1 
HETATM 1095 O  O   . A1B3K B 2 .   ? 10.331 9.527   23.569 1.00 27.62 ? 201 A1B3K A O   1 
HETATM 1096 C  C   . A1B3K B 2 .   ? 10.291 8.324   22.818 1.00 27.48 ? 201 A1B3K A C   1 
HETATM 1097 F  F2  . A1B3K B 2 .   ? 5.557  11.654  26.882 1.00 41.82 ? 201 A1B3K A F2  1 
HETATM 1098 F  F1  . A1B3K B 2 .   ? 6.704  11.001  28.457 1.00 42.10 ? 201 A1B3K A F1  1 
HETATM 1099 F  F   . A1B3K B 2 .   ? 5.358  9.722   27.402 1.00 42.19 ? 201 A1B3K A F   1 
HETATM 1100 C  C3  . A1B3K B 2 .   ? 7.477  9.013   25.818 1.00 32.69 ? 201 A1B3K A C3  1 
HETATM 1101 C  C2  . A1B3K B 2 .   ? 8.473  8.710   24.904 1.00 30.27 ? 201 A1B3K A C2  1 
HETATM 1102 ZN ZN  . ZN    C 3 .   ? 10.964 -5.314  5.687  1.00 27.33 2 202 ZN    A ZN  1 
HETATM 1103 S  S   . DMS   D 4 .   ? 23.416 -6.230  10.478 0.00 36.16 ? 203 DMS   A S   1 
HETATM 1104 O  O   . DMS   D 4 .   ? 24.353 -7.386  10.582 0.00 42.36 ? 203 DMS   A O   1 
HETATM 1105 C  C1  . DMS   D 4 .   ? 21.791 -6.808  10.060 0.00 33.83 ? 203 DMS   A C1  1 
HETATM 1106 C  C2  . DMS   D 4 .   ? 22.784 -5.788  12.099 0.00 31.27 ? 203 DMS   A C2  1 
HETATM 1107 S  S   . DMS   E 4 .   ? 14.951 20.507  7.596  0.00 39.62 ? 204 DMS   A S   1 
HETATM 1108 O  O   . DMS   E 4 .   ? 14.304 20.679  8.938  0.00 31.45 ? 204 DMS   A O   1 
HETATM 1109 C  C1  . DMS   E 4 .   ? 13.637 20.541  6.348  0.00 36.15 ? 204 DMS   A C1  1 
HETATM 1110 C  C2  . DMS   E 4 .   ? 15.683 22.100  7.135  0.00 36.09 ? 204 DMS   A C2  1 
HETATM 1111 S  S   . DMS   F 4 .   ? 20.151 -1.064  20.087 0.00 36.66 ? 205 DMS   A S   1 
HETATM 1112 O  O   . DMS   F 4 .   ? 18.679 -0.888  19.865 0.00 21.41 ? 205 DMS   A O   1 
HETATM 1113 C  C1  . DMS   F 4 .   ? 20.472 -0.800  21.852 0.00 35.52 ? 205 DMS   A C1  1 
HETATM 1114 C  C2  . DMS   F 4 .   ? 20.973 0.451   19.523 0.00 35.92 ? 205 DMS   A C2  1 
HETATM 1115 S  S   . DMS   G 4 .   ? 3.272  10.603  18.488 1.00 20.00 ? 206 DMS   A S   1 
HETATM 1116 O  O   . DMS   G 4 .   ? 4.135  11.457  19.345 1.00 20.00 ? 206 DMS   A O   1 
HETATM 1117 C  C1  . DMS   G 4 .   ? 1.733  11.464  18.281 1.00 20.00 ? 206 DMS   A C1  1 
HETATM 1118 C  C2  . DMS   G 4 .   ? 2.653  9.314   19.531 1.00 20.00 ? 206 DMS   A C2  1 
HETATM 1119 O  O   . HOH   H 5 .   ? 8.262  19.077  18.197 1.00 28.89 ? 301 HOH   A O   1 
HETATM 1120 O  O   . HOH   H 5 .   ? 9.730  17.709  20.056 1.00 27.09 ? 302 HOH   A O   1 
HETATM 1121 O  O   . HOH   H 5 .   ? 20.246 21.960  7.829  1.00 31.49 ? 303 HOH   A O   1 
HETATM 1122 O  O   . HOH   H 5 .   ? 3.871  -5.416  21.204 1.00 42.09 ? 304 HOH   A O   1 
HETATM 1123 O  O   . HOH   H 5 .   ? 11.281 17.251  26.663 1.00 38.05 ? 305 HOH   A O   1 
HETATM 1124 O  O   . HOH   H 5 .   ? 8.942  1.701   2.985  1.00 28.07 ? 306 HOH   A O   1 
HETATM 1125 O  O   . HOH   H 5 .   ? 2.894  14.299  19.740 1.00 40.73 ? 307 HOH   A O   1 
HETATM 1126 O  O   . HOH   H 5 .   ? 5.036  5.070   24.301 1.00 32.12 ? 308 HOH   A O   1 
HETATM 1127 O  O   . HOH   H 5 .   ? 23.743 21.418  8.021  1.00 28.19 ? 309 HOH   A O   1 
HETATM 1128 O  O   . HOH   H 5 .   ? 15.979 -11.694 5.509  1.00 46.13 ? 310 HOH   A O   1 
HETATM 1129 O  O   . HOH   H 5 .   ? 22.883 -2.092  4.413  1.00 38.14 ? 311 HOH   A O   1 
HETATM 1130 O  O   . HOH   H 5 .   ? 10.608 7.486   4.649  1.00 30.22 ? 312 HOH   A O   1 
HETATM 1131 O  O   . HOH   H 5 .   ? 35.704 15.135  17.024 1.00 39.72 ? 313 HOH   A O   1 
HETATM 1132 O  O   . HOH   H 5 .   ? 7.896  -4.569  0.770  1.00 28.76 ? 314 HOH   A O   1 
HETATM 1133 O  O   . HOH   H 5 .   ? 11.197 -5.649  31.860 1.00 33.08 ? 315 HOH   A O   1 
HETATM 1134 O  O   . HOH   H 5 .   ? 21.502 18.416  17.711 1.00 37.12 ? 316 HOH   A O   1 
HETATM 1135 O  O   . HOH   H 5 .   ? 20.186 8.346   19.075 1.00 23.18 ? 317 HOH   A O   1 
HETATM 1136 O  O   . HOH   H 5 .   ? 0.593  -0.858  16.484 1.00 22.44 ? 318 HOH   A O   1 
HETATM 1137 O  O   . HOH   H 5 .   ? 36.843 15.398  12.543 1.00 44.23 ? 319 HOH   A O   1 
HETATM 1138 O  O   . HOH   H 5 .   ? 17.972 20.595  9.669  1.00 23.75 ? 320 HOH   A O   1 
HETATM 1139 O  O   . HOH   H 5 .   ? 6.812  -6.230  29.359 1.00 36.40 ? 321 HOH   A O   1 
HETATM 1140 O  O   . HOH   H 5 .   ? 18.048 18.220  17.079 1.00 18.87 ? 322 HOH   A O   1 
HETATM 1141 O  O   . HOH   H 5 .   ? 10.068 3.793   34.014 1.00 30.04 ? 323 HOH   A O   1 
HETATM 1142 O  O   . HOH   H 5 .   ? 23.180 17.790  19.405 1.00 40.46 ? 324 HOH   A O   1 
HETATM 1143 O  O   . HOH   H 5 .   ? 18.165 0.126   29.963 1.00 44.57 ? 325 HOH   A O   1 
HETATM 1144 O  O   . HOH   H 5 .   ? 10.228 4.156   3.481  1.00 25.17 ? 326 HOH   A O   1 
HETATM 1145 O  O   . HOH   H 5 .   ? 14.935 1.927   23.287 1.00 22.30 ? 327 HOH   A O   1 
HETATM 1146 O  O   . HOH   H 5 .   ? 11.457 10.911  11.307 1.00 14.97 ? 328 HOH   A O   1 
HETATM 1147 O  O   . HOH   H 5 .   ? 1.025  -3.367  20.206 1.00 36.88 ? 329 HOH   A O   1 
HETATM 1148 O  O   . HOH   H 5 .   ? 18.158 18.625  5.739  1.00 33.76 ? 330 HOH   A O   1 
HETATM 1149 O  O   . HOH   H 5 .   ? 30.136 10.444  19.520 1.00 33.04 ? 331 HOH   A O   1 
HETATM 1150 O  O   . HOH   H 5 .   ? 14.864 -5.072  17.211 1.00 26.89 ? 332 HOH   A O   1 
HETATM 1151 O  O   . HOH   H 5 .   ? 13.199 9.790   9.418  1.00 15.18 ? 333 HOH   A O   1 
HETATM 1152 O  O   . HOH   H 5 .   ? 7.206  2.787   33.131 1.00 36.07 ? 334 HOH   A O   1 
HETATM 1153 O  O   . HOH   H 5 .   ? 17.999 1.844   23.204 1.00 25.43 ? 335 HOH   A O   1 
HETATM 1154 O  O   . HOH   H 5 .   ? 5.498  -2.202  24.546 1.00 22.89 ? 336 HOH   A O   1 
HETATM 1155 O  O   . HOH   H 5 .   ? 15.263 11.656  24.223 1.00 25.51 ? 337 HOH   A O   1 
HETATM 1156 O  O   . HOH   H 5 .   ? 11.394 1.570   33.703 1.00 25.14 ? 338 HOH   A O   1 
HETATM 1157 O  O   . HOH   H 5 .   ? 4.233  -5.857  6.566  1.00 41.23 ? 339 HOH   A O   1 
HETATM 1158 O  O   . HOH   H 5 .   ? 14.543 13.684  3.507  1.00 30.71 ? 340 HOH   A O   1 
HETATM 1159 O  O   . HOH   H 5 .   ? 10.548 16.496  5.156  1.00 47.75 ? 341 HOH   A O   1 
HETATM 1160 O  O   . HOH   H 5 .   ? 0.817  0.674   24.504 1.00 41.39 ? 342 HOH   A O   1 
HETATM 1161 O  O   . HOH   H 5 .   ? 13.390 8.516   29.973 1.00 34.90 ? 343 HOH   A O   1 
HETATM 1162 O  O   . HOH   H 5 .   ? 26.146 3.524   20.188 1.00 42.48 ? 344 HOH   A O   1 
HETATM 1163 O  O   . HOH   H 5 .   ? 31.182 20.020  16.789 1.00 34.89 ? 345 HOH   A O   1 
HETATM 1164 O  O   . HOH   H 5 .   ? 30.899 9.801   14.798 1.00 42.96 ? 346 HOH   A O   1 
HETATM 1165 O  O   . HOH   H 5 .   ? 28.430 3.255   3.192  1.00 63.18 ? 347 HOH   A O   1 
HETATM 1166 O  O   . HOH   H 5 .   ? 30.847 20.310  10.591 1.00 43.70 ? 348 HOH   A O   1 
HETATM 1167 O  O   . HOH   H 5 .   ? 8.222  16.256  23.219 1.00 30.00 ? 349 HOH   A O   1 
HETATM 1168 O  O   . HOH   H 5 .   ? 16.043 23.011  14.488 1.00 50.47 ? 350 HOH   A O   1 
HETATM 1169 O  O   . HOH   H 5 .   ? -0.695 14.105  12.367 1.00 30.00 ? 351 HOH   A O   1 
HETATM 1170 O  O   . HOH   H 5 .   ? 30.300 10.607  2.751  1.00 51.20 ? 352 HOH   A O   1 
HETATM 1171 O  O   . HOH   H 5 .   ? 5.327  6.540   28.811 1.00 40.23 ? 353 HOH   A O   1 
HETATM 1172 O  O   . HOH   H 5 .   ? 12.147 -8.444  13.276 1.00 33.71 ? 354 HOH   A O   1 
HETATM 1173 O  O   . HOH   H 5 .   ? 19.791 23.125  15.488 1.00 27.85 ? 355 HOH   A O   1 
HETATM 1174 O  O   . HOH   H 5 .   ? 9.408  20.541  10.915 1.00 33.18 ? 356 HOH   A O   1 
HETATM 1175 O  O   . HOH   H 5 .   ? 6.950  14.357  22.877 1.00 30.00 ? 357 HOH   A O   1 
HETATM 1176 O  O   . HOH   H 5 .   ? 1.595  -3.197  17.685 1.00 26.38 ? 358 HOH   A O   1 
HETATM 1177 O  O   . HOH   H 5 .   ? -0.235 14.592  7.768  1.00 50.31 ? 359 HOH   A O   1 
HETATM 1178 O  O   . HOH   H 5 .   ? 18.653 12.078  2.147  1.00 35.13 ? 360 HOH   A O   1 
HETATM 1179 O  O   . HOH   H 5 .   ? 8.836  -8.189  9.289  1.00 39.99 ? 361 HOH   A O   1 
HETATM 1180 O  O   . HOH   H 5 .   ? 5.571  1.191   7.154  1.00 34.81 ? 362 HOH   A O   1 
HETATM 1181 O  O   . HOH   H 5 .   ? 30.893 14.963  22.420 1.00 41.16 ? 363 HOH   A O   1 
HETATM 1182 O  O   . HOH   H 5 .   ? 32.642 13.663  20.852 1.00 40.24 ? 364 HOH   A O   1 
HETATM 1183 O  O   . HOH   H 5 .   ? 22.190 8.200   21.054 1.00 31.73 ? 365 HOH   A O   1 
HETATM 1184 O  O   . HOH   H 5 .   ? 22.426 18.365  5.993  1.00 31.22 ? 366 HOH   A O   1 
HETATM 1185 O  O   . HOH   H 5 .   ? 24.487 6.941   20.474 1.00 37.98 ? 367 HOH   A O   1 
HETATM 1186 O  O   . HOH   H 5 .   ? 11.952 20.642  12.382 1.00 25.71 ? 368 HOH   A O   1 
HETATM 1187 O  O   . HOH   H 5 .   ? 7.013  -5.836  2.913  1.00 34.14 ? 369 HOH   A O   1 
HETATM 1188 O  O   . HOH   H 5 .   ? 4.071  6.590   26.275 1.00 30.00 ? 370 HOH   A O   1 
HETATM 1189 O  O   . HOH   H 5 .   ? -1.659 -4.928  15.579 1.00 51.48 ? 371 HOH   A O   1 
HETATM 1190 O  O   . HOH   H 5 .   ? 15.905 -5.430  1.930  1.00 31.40 ? 372 HOH   A O   1 
HETATM 1191 O  O   . HOH   H 5 .   ? 14.731 13.123  26.454 1.00 30.00 ? 373 HOH   A O   1 
HETATM 1192 O  O   . HOH   H 5 .   ? -3.451 12.261  27.677 1.00 44.91 ? 374 HOH   A O   1 
HETATM 1193 O  O   . HOH   H 5 .   ? 6.353  -8.776  14.394 1.00 34.47 ? 375 HOH   A O   1 
HETATM 1194 O  O   . HOH   H 5 .   ? 5.177  13.960  21.302 1.00 36.41 ? 376 HOH   A O   1 
HETATM 1195 O  O   . HOH   H 5 .   ? -1.379 6.139   28.066 1.00 30.00 ? 377 HOH   A O   1 
HETATM 1196 O  O   . HOH   H 5 .   ? 7.038  25.066  14.329 1.00 41.29 ? 378 HOH   A O   1 
HETATM 1197 O  O   . HOH   H 5 .   ? 21.092 21.509  17.776 1.00 31.85 ? 379 HOH   A O   1 
HETATM 1198 O  O   . HOH   H 5 .   ? 4.614  -2.035  29.109 1.00 49.73 ? 380 HOH   A O   1 
HETATM 1199 O  O   . HOH   H 5 .   ? 37.138 5.996   6.779  1.00 53.06 ? 381 HOH   A O   1 
HETATM 1200 O  O   . HOH   H 5 .   ? -3.417 13.847  10.286 1.00 30.00 ? 382 HOH   A O   1 
HETATM 1201 O  O   . HOH   H 5 .   ? 2.248  1.634   27.299 1.00 33.60 ? 383 HOH   A O   1 
HETATM 1202 O  O   . HOH   H 5 .   ? 13.409 13.200  1.444  1.00 51.16 ? 384 HOH   A O   1 
HETATM 1203 O  O   . HOH   H 5 .   ? 11.778 22.748  14.285 1.00 29.83 ? 385 HOH   A O   1 
HETATM 1204 O  O   . HOH   H 5 .   ? -1.040 2.740   4.469  1.00 43.81 ? 386 HOH   A O   1 
HETATM 1205 O  O   . HOH   H 5 .   ? 9.205  -9.420  12.808 1.00 41.73 ? 387 HOH   A O   1 
HETATM 1206 O  O   . HOH   H 5 .   ? 9.070  6.625   2.340  1.00 42.22 ? 388 HOH   A O   1 
HETATM 1207 O  O   . HOH   H 5 .   ? 9.782  24.263  13.468 1.00 50.04 ? 389 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   ? 0.5968 0.2744 0.3397 -0.0552 -0.1943 0.0131  7   SER   A N   
2    C CA  . SER   A 1   ? 0.5640 0.2859 0.4030 -0.0531 -0.2139 0.0234  7   SER   A CA  
3    C C   . SER   A 1   ? 0.5061 0.2922 0.4295 -0.0412 -0.1951 0.0237  7   SER   A C   
4    O O   . SER   A 1   ? 0.5110 0.3017 0.4172 -0.0394 -0.1824 0.0203  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6133 0.2897 0.4568 -0.0758 -0.2719 0.0444  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6709 0.3300 0.5078 -0.0869 -0.2923 0.0544  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4391 0.2662 0.4481 -0.0348 -0.1914 0.0281  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3793 0.2534 0.4635 -0.0264 -0.1682 0.0281  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3324 0.2419 0.4676 -0.0159 -0.1386 0.0217  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3293 0.2407 0.4320 -0.0107 -0.1264 0.0122  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2806 0.2131 0.4934 -0.0136 -0.1230 0.0268  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2535 0.2068 0.5078 -0.0067 -0.0895 0.0206  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2300 0.1975 0.5184 -0.0045 -0.0515 0.0159  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2214 0.1882 0.5241 -0.0073 -0.0560 0.0212  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2340 0.1819 0.5633 -0.0091 -0.1071 0.0363  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2189 0.1917 0.5115 -0.0020 -0.0138 0.0058  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2285 0.1974 0.5413 -0.0039 0.0285  0.0001  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2317 0.1915 0.6304 -0.0026 0.0504  0.0087  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2212 0.1797 0.6254 -0.0006 0.0509  0.0082  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2595 0.2245 0.4983 -0.0076 0.0545  -0.0161 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2622 0.2391 0.4333 -0.0073 0.0329  -0.0203 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2784 0.2225 0.5175 -0.0151 0.0982  -0.0228 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2802 0.2562 0.3934 -0.0121 0.0447  -0.0286 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2468 0.1993 0.7165 -0.0033 0.0722  0.0174  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2515 0.1923 0.8217 -0.0011 0.1022  0.0291  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2900 0.2009 0.8494 -0.0049 0.1695  0.0157  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3002 0.2038 0.8639 -0.0075 0.1863  0.0149  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2196 0.1694 0.8963 -0.0005 0.0739  0.0555  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2198 0.1812 0.8974 -0.0029 0.0062  0.0707  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2162 0.1773 0.9396 -0.0022 -0.0108 0.0822  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2482 0.2125 0.8650 -0.0080 -0.0386 0.0716  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2354 0.1951 0.9424 -0.0084 -0.0736 0.0951  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2698 0.2272 0.8647 -0.0145 -0.0970 0.0835  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2700 0.2233 0.9056 -0.0156 -0.1155 0.0949  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3034 0.2388 0.9065 -0.0259 -0.1739 0.1068  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3182 0.2046 0.8504 -0.0075 0.2076  0.0045  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3669 0.2052 0.8608 -0.0166 0.2739  -0.0102 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3772 0.1848 0.9274 -0.0153 0.3209  -0.0075 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3900 0.2014 0.9153 -0.0146 0.3093  -0.0107 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4371 0.2598 0.7920 -0.0292 0.2717  -0.0304 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4412 0.2888 0.7502 -0.0270 0.2315  -0.0325 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5016 0.2573 0.7983 -0.0450 0.3362  -0.0446 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3649 0.1406 0.9980 -0.0144 0.3772  -0.0004 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3793 0.1212 1.0825 -0.0119 0.4310  0.0048  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3588 0.1464 1.1673 0.0005  0.3849  0.0275  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3381 0.1693 1.2164 0.0066  0.3299  0.0474  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3683 0.1444 1.1706 0.0013  0.3972  0.0242  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3268 0.1433 1.2192 0.0109  0.3488  0.0456  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3064 0.1580 1.0997 0.0097  0.2793  0.0364  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2791 0.1476 1.0999 0.0138  0.2508  0.0445  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3738 0.1608 1.3426 0.0146  0.4019  0.0522  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4481 0.2012 1.5398 0.0179  0.4717  0.0668  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4182 0.1971 1.6263 0.0233  0.4510  0.0919  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5307 0.2184 1.5988 0.0132  0.5589  0.0525  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3083 0.1701 0.9966 0.0044  0.2533  0.0217  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3072 0.1962 0.9066 0.0038  0.1984  0.0135  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2627 0.1830 0.8513 0.0053  0.1400  0.0212  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2531 0.1726 0.8538 0.0036  0.1448  0.0237  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3574 0.2247 0.8284 -0.0058 0.2199  -0.0102 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4054 0.2317 0.8537 -0.0121 0.2701  -0.0197 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4058 0.2392 0.8909 -0.0064 0.2638  -0.0142 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4666 0.2395 0.8435 -0.0265 0.3222  -0.0345 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4540 0.2449 0.9141 -0.0130 0.3117  -0.0229 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5196 0.2414 0.8571 -0.0365 0.3686  -0.0438 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5221 0.2541 0.9056 -0.0287 0.3653  -0.0379 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5930 0.2699 0.9357 -0.0391 0.4136  -0.0469 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2408 0.1814 0.7967 0.0071  0.0887  0.0235  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2229 0.1792 0.7408 0.0059  0.0365  0.0275  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2271 0.1884 0.6376 0.0058  0.0265  0.0102  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2269 0.1884 0.6230 0.0076  0.0252  0.0068  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2011 0.1615 0.7853 0.0047  -0.0145 0.0508  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2508 0.2094 0.7657 -0.0004 -0.0691 0.0524  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2858 0.2333 0.8600 -0.0082 -0.1225 0.0783  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3248 0.2541 0.8160 -0.0147 -0.1656 0.0759  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3623 0.2693 0.7876 -0.0243 -0.2016 0.0781  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3299 0.2378 0.7639 -0.0274 -0.2036 0.0827  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3894 0.2668 0.7339 -0.0317 -0.2319 0.0749  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2142 0.1795 0.5574 0.0037  0.0233  0.0009  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2283 0.1996 0.4862 0.0037  0.0160  -0.0108 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2154 0.1894 0.4439 0.0051  -0.0227 -0.0063 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2242 0.1968 0.4525 0.0032  -0.0323 -0.0027 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2454 0.2138 0.4510 -0.0019 0.0420  -0.0216 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2641 0.2396 0.4040 -0.0031 0.0350  -0.0277 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2389 0.1849 0.4627 -0.0086 0.0859  -0.0261 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2061 0.1775 0.4017 0.0073  -0.0410 -0.0075 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2238 0.1811 0.3746 0.0062  -0.0707 -0.0049 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2149 0.1730 0.3054 0.0103  -0.0628 -0.0138 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1944 0.1648 0.2881 0.0131  -0.0469 -0.0182 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2521 0.1877 0.4271 0.0011  -0.1065 0.0076  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2611 0.1911 0.4956 -0.0054 -0.1260 0.0230  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2401 0.1810 0.4467 0.0041  -0.1021 0.0083  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2341 0.1722 0.2721 0.0099  -0.0741 -0.0145 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2479 0.1803 0.2426 0.0147  -0.0635 -0.0196 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2524 0.1724 0.2539 0.0144  -0.0757 -0.0183 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2774 0.1728 0.2858 0.0074  -0.1028 -0.0118 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2935 0.1901 0.2292 0.0130  -0.0670 -0.0203 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3108 0.2172 0.2393 0.0137  -0.0558 -0.0207 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3503 0.2485 0.2835 0.0078  -0.0704 -0.0174 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2854 0.2103 0.2099 0.0198  -0.0323 -0.0220 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2400 0.1754 0.2427 0.0199  -0.0600 -0.0218 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2338 0.1606 0.2438 0.0206  -0.0683 -0.0213 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2987 0.1783 0.2581 0.0162  -0.0855 -0.0206 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3191 0.1777 0.2847 0.0102  -0.1094 -0.0161 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2156 0.1660 0.2301 0.0265  -0.0474 -0.0241 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2231 0.1718 0.2551 0.0276  -0.0533 -0.0239 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2336 0.1990 0.2613 0.0322  -0.0361 -0.0246 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2558 0.2234 0.3001 0.0337  -0.0385 -0.0247 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2952 0.2416 0.3216 0.0363  -0.0449 -0.0254 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2912 0.2027 0.2750 0.0357  -0.0486 -0.0267 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3080 0.2602 0.3524 0.0379  -0.0459 -0.0252 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3311 0.1861 0.2374 0.0170  -0.0728 -0.0240 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4048 0.1954 0.2414 0.0091  -0.0818 -0.0253 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4625 0.2110 0.2755 -0.0071 -0.1204 -0.0183 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5242 0.2073 0.2720 -0.0204 -0.1386 -0.0171 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4281 0.1947 0.2164 0.0142  -0.0483 -0.0302 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4474 0.2087 0.2192 0.0122  -0.0431 -0.0296 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4150 0.2310 0.2354 0.0204  -0.0289 -0.0279 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4907 0.1917 0.1954 0.0010  -0.0497 -0.0304 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4439 0.2386 0.2341 0.0167  -0.0262 -0.0278 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4913 0.2171 0.2117 0.0051  -0.0382 -0.0294 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4334 0.2137 0.2988 -0.0086 -0.1344 -0.0119 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4646 0.2109 0.3264 -0.0248 -0.1754 0.0000  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4452 0.2173 0.3936 -0.0279 -0.2025 0.0134  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.4616 0.2151 0.4342 -0.0413 -0.2394 0.0291  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4573 0.2100 0.3146 -0.0256 -0.1703 0.0005  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5113 0.2277 0.2853 -0.0247 -0.1447 -0.0094 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5141 0.2421 0.2911 -0.0246 -0.1397 -0.0084 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5794 0.2067 0.2569 -0.0430 -0.1646 -0.0081 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4101 0.2252 0.4132 -0.0159 -0.1821 0.0095  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3879 0.2255 0.4797 -0.0167 -0.1964 0.0219  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4274 0.2212 0.5184 -0.0330 -0.2455 0.0384  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4662 0.2156 0.4805 -0.0404 -0.2574 0.0340  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3577 0.2335 0.4841 -0.0035 -0.1636 0.0130  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4190 0.2202 0.5966 -0.0402 -0.2734 0.0592  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4585 0.2199 0.6576 -0.0596 -0.3304 0.0831  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4486 0.2294 0.7150 -0.0541 -0.3293 0.0890  24  THR   A C   
137  O O   . THR   A 18  ? 0.4091 0.2337 0.7088 -0.0356 -0.2828 0.0750  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4604 0.2260 0.7445 -0.0699 -0.3613 0.1088  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4272 0.2477 0.8344 -0.0545 -0.3287 0.1140  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4933 0.2468 0.7244 -0.0738 -0.3592 0.1035  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4814 0.2275 0.7744 -0.0723 -0.3834 0.1129  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4809 0.2459 0.8496 -0.0674 -0.3843 0.1217  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4159 0.2375 0.9235 -0.0520 -0.3503 0.1306  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3910 0.2438 0.9395 -0.0369 -0.3110 0.1211  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5400 0.2544 0.9231 -0.0937 -0.4566 0.1518  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6870 0.3277 0.9255 -0.1134 -0.4885 0.1440  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7555 0.3863 0.9239 -0.1055 -0.4632 0.1224  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7709 0.3363 0.9259 -0.1433 -0.5436 0.1576  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.8365 0.3853 0.8799 -0.1291 -0.4967 0.1214  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.8545 0.3570 0.8782 -0.1539 -0.5463 0.1418  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3904 0.2186 0.9684 -0.0573 -0.3628 0.1495  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3437 0.2149 1.0522 -0.0435 -0.3218 0.1580  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3101 0.2128 0.9808 -0.0230 -0.2484 0.1252  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2904 0.2142 1.0242 -0.0113 -0.2056 0.1219  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3711 0.2416 1.1513 -0.0520 -0.3427 0.1816  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3992 0.3045 1.3216 -0.0384 -0.2945 0.1925  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3852 0.2989 1.4195 -0.0361 -0.2916 0.2125  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4069 0.3283 1.3236 -0.0291 -0.2496 0.1782  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3051 0.2043 0.8676 -0.0208 -0.2352 0.1022  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2737 0.1969 0.7902 -0.0063 -0.1762 0.0744  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2433 0.1746 0.7445 0.0015  -0.1534 0.0623  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2301 0.1779 0.7616 0.0099  -0.1070 0.0538  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3035 0.2181 0.7086 -0.0072 -0.1766 0.0567  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3276 0.2398 0.7405 -0.0120 -0.1843 0.0630  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2890 0.2189 0.7816 -0.0083 -0.1605 0.0699  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3750 0.2623 0.7144 -0.0202 -0.2112 0.0615  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2437 0.1562 0.6943 -0.0034 -0.1853 0.0622  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2443 0.1647 0.6799 0.0038  -0.1662 0.0514  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2465 0.1771 0.7903 0.0064  -0.1579 0.0664  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2520 0.1948 0.7990 0.0146  -0.1229 0.0556  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2648 0.1561 0.6169 -0.0026 -0.1988 0.0475  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2782 0.1661 0.5309 0.0017  -0.1796 0.0271  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3169 0.1779 0.5001 -0.0049 -0.1939 0.0242  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2604 0.1701 0.4808 0.0127  -0.1420 0.0103  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3326 0.1999 0.4511 0.0034  -0.1636 0.0070  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2972 0.1971 0.4421 0.0136  -0.1345 0.0000  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2389 0.1731 0.4898 0.0203  -0.1134 0.0050  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2945 0.2110 0.4052 0.0218  -0.1053 -0.0117 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2452 0.1922 0.4496 0.0260  -0.0883 -0.0077 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2689 0.2103 0.4113 0.0269  -0.0857 -0.0143 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2441 0.1665 0.8784 -0.0017 -0.1907 0.0935  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2443 0.1754 1.0018 0.0010  -0.1820 0.1131  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2407 0.1885 1.0675 0.0118  -0.1167 0.1089  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2317 0.1830 1.1461 0.0174  -0.0861 0.1175  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2292 0.1447 1.0744 -0.0136 -0.2426 0.1496  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2288 0.1796 1.0198 0.0129  -0.0949 0.0978  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2116 0.1649 1.0406 0.0196  -0.0309 0.0902  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2168 0.1695 0.9222 0.0218  0.0034  0.0586  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2123 0.1605 0.9033 0.0215  0.0369  0.0501  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2293 0.1828 1.1363 0.0163  -0.0374 0.1093  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2749 0.2287 1.3271 0.0126  -0.0669 0.1464  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3024 0.2551 1.4531 0.0187  -0.0300 0.1571  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2652 0.2154 1.3366 0.0007  -0.1338 0.1693  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2302 0.1854 0.8538 0.0227  -0.0069 0.0442  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2325 0.1885 0.7511 0.0226  0.0155  0.0209  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2532 0.1932 0.7656 0.0211  0.0758  0.0096  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2574 0.1851 0.8160 0.0226  0.1044  0.0125  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2277 0.1884 0.6859 0.0241  -0.0055 0.0134  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2382 0.2020 0.6037 0.0230  0.0107  -0.0043 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2668 0.2355 0.5794 0.0211  -0.0029 -0.0086 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2208 0.1891 0.5516 0.0256  -0.0044 -0.0078 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2526 0.1855 0.6998 0.0159  0.0954  -0.0029 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2694 0.1721 0.6766 0.0080  0.1476  -0.0152 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2922 0.1954 0.5960 0.0010  0.1376  -0.0276 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3307 0.2126 0.5994 -0.0057 0.1590  -0.0336 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2976 0.1846 0.7082 0.0032  0.1735  -0.0170 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3552 0.1972 0.6916 -0.0109 0.2225  -0.0315 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2745 0.1590 0.8040 0.0095  0.1886  -0.0008 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2675 0.1942 0.5298 0.0024  0.1026  -0.0284 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2669 0.1997 0.4530 -0.0031 0.0891  -0.0340 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2324 0.1930 0.4057 0.0044  0.0511  -0.0307 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2207 0.1870 0.4176 0.0082  0.0399  -0.0272 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2934 0.1984 0.4211 -0.0188 0.1145  -0.0404 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.3185 0.2303 0.3796 -0.0277 0.0945  -0.0400 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3494 0.2523 0.3685 -0.0376 0.0895  -0.0384 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.3159 0.2441 0.3546 -0.0285 0.0762  -0.0375 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3617 0.2759 0.3424 -0.0450 0.0671  -0.0323 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3388 0.2694 0.3319 -0.0385 0.0604  -0.0322 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.3018 0.2429 0.3600 -0.0218 0.0702  -0.0371 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3280 0.2728 0.3006 -0.0419 0.0425  -0.0258 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2999 0.2537 0.3275 -0.0246 0.0542  -0.0340 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3090 0.2653 0.2982 -0.0340 0.0418  -0.0280 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2113 0.1837 0.3503 0.0060  0.0346  -0.0307 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2046 0.1922 0.3237 0.0121  0.0103  -0.0284 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2189 0.2145 0.2993 0.0084  0.0087  -0.0267 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2193 0.2110 0.2924 0.0032  0.0149  -0.0260 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2001 0.1874 0.3405 0.0207  -0.0122 -0.0253 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1971 0.1832 0.3539 0.0233  -0.0136 -0.0246 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2628 0.2557 0.3866 0.0255  -0.0159 -0.0255 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2815 0.2755 0.4131 0.0249  -0.0098 -0.0256 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2747 0.2704 0.3701 0.0279  -0.0214 -0.0247 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2039 0.2088 0.2657 0.0104  0.0004  -0.0235 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2018 0.2168 0.2469 0.0073  -0.0029 -0.0160 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1880 0.2090 0.2322 0.0179  -0.0084 -0.0129 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1956 0.2163 0.2324 0.0186  -0.0080 -0.0127 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2357 0.2460 0.2589 -0.0085 0.0007  -0.0115 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2910 0.3096 0.3081 -0.0166 -0.0099 0.0027  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2724 0.3069 0.3110 -0.0056 -0.0149 0.0097  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3238 0.3273 0.3144 -0.0362 -0.0134 0.0089  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1717 0.1922 0.2207 0.0256  -0.0097 -0.0109 36  SER   A N   
241  C CA  A SER   A 30  ? 0.1811 0.1926 0.2215 0.0348  -0.0054 -0.0092 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1821 0.1933 0.2221 0.0348  -0.0054 -0.0092 36  SER   A CA  
243  C C   . SER   A 30  ? 0.1764 0.2013 0.2261 0.0337  0.0020  0.0024  36  SER   A C   
244  O O   . SER   A 30  ? 0.2000 0.2144 0.2409 0.0392  0.0108  0.0028  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2040 0.2067 0.2470 0.0414  -0.0025 -0.0088 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2102 0.2105 0.2507 0.0419  -0.0021 -0.0093 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2548 0.2373 0.2837 0.0489  0.0109  -0.0074 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2412 0.2618 0.3063 0.0401  0.0010  0.0014  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1594 0.2029 0.2270 0.0245  -0.0033 0.0141  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1522 0.2092 0.2412 0.0207  -0.0032 0.0311  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1611 0.2175 0.2354 0.0157  -0.0045 0.0287  37  SER   A C   
252  O O   . SER   A 31  ? 0.1707 0.2360 0.2657 0.0157  -0.0022 0.0422  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1842 0.2537 0.2917 0.0063  -0.0181 0.0483  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2486 0.3090 0.3243 -0.0118 -0.0298 0.0449  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1569 0.2034 0.2047 0.0112  -0.0072 0.0144  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1628 0.2066 0.1964 0.0064  -0.0071 0.0105  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1829 0.2145 0.2057 0.0172  -0.0020 -0.0009 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1933 0.2233 0.2081 0.0150  -0.0016 -0.0031 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1917 0.2256 0.2060 -0.0088 -0.0091 0.0050  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2033 0.2340 0.2076 -0.0272 -0.0188 0.0177  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2585 0.2606 0.2256 -0.0453 -0.0128 0.0098  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2696 0.2618 0.2202 -0.0508 -0.0064 0.0048  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2935 0.2527 0.2020 -0.0723 -0.0008 0.0030  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3224 0.2501 0.1939 -0.0920 -0.0014 0.0056  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3093 0.2594 0.2052 -0.0761 0.0068  -0.0017 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1976 0.2154 0.2158 0.0260  -0.0014 -0.0070 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1924 0.1864 0.1908 0.0302  -0.0055 -0.0153 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1819 0.1769 0.1896 0.0242  -0.0146 -0.0203 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1910 0.1740 0.1900 0.0235  -0.0206 -0.0221 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1999 0.1787 0.1774 0.0341  0.0035  -0.0136 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2683 0.2094 0.2102 0.0332  -0.0056 -0.0203 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2819 0.1999 0.2096 0.0322  -0.0157 -0.0236 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2801 0.2117 0.2063 0.0311  -0.0059 -0.0207 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1664 0.1714 0.1932 0.0189  -0.0122 -0.0214 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1522 0.1529 0.1990 0.0141  -0.0108 -0.0249 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1765 0.1709 0.2517 0.0154  -0.0134 -0.0259 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1933 0.1902 0.2678 0.0163  -0.0111 -0.0260 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1565 0.1598 0.1980 0.0034  0.0048  -0.0256 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1973 0.2054 0.2189 -0.0012 0.0059  -0.0229 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1986 0.1947 0.2021 -0.0170 0.0191  -0.0238 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2172 0.2229 0.2465 0.0040  0.0007  -0.0246 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1715 0.1584 0.2799 0.0148  -0.0180 -0.0243 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1757 0.1571 0.3301 0.0153  -0.0189 -0.0213 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1760 0.1534 0.3760 0.0120  -0.0047 -0.0184 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1822 0.1591 0.3835 0.0108  -0.0118 -0.0159 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1916 0.1609 0.3540 0.0176  -0.0498 -0.0149 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2086 0.1740 0.4296 0.0176  -0.0558 -0.0076 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2342 0.1868 0.4359 0.0181  -0.0803 -0.0053 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2107 0.1703 0.4991 0.0139  -0.0680 0.0056  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1835 0.1543 0.4194 0.0102  0.0206  -0.0189 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1846 0.1444 0.4761 0.0079  0.0456  -0.0152 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1904 0.1469 0.5629 0.0118  0.0437  -0.0038 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1908 0.1451 0.5628 0.0132  0.0493  -0.0058 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2131 0.1520 0.4727 -0.0008 0.0901  -0.0254 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2228 0.1411 0.5455 -0.0024 0.1261  -0.0215 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2391 0.1810 0.4267 -0.0072 0.0850  -0.0321 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1842 0.1411 0.6309 0.0127  0.0318  0.0110  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1877 0.1419 0.7325 0.0150  0.0280  0.0281  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2111 0.1544 0.8412 0.0152  0.0686  0.0366  43  SER   A C   
300  O O   . SER   A 37  ? 0.1847 0.1237 0.7990 0.0129  0.0858  0.0317  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1806 0.1392 0.7519 0.0124  -0.0324 0.0460  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1971 0.1550 0.7693 0.0079  -0.0552 0.0536  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2289 0.1656 0.9577 0.0183  0.0863  0.0510  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2587 0.1799 1.0867 0.0199  0.1340  0.0620  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2816 0.2165 1.2202 0.0193  0.0959  0.0918  44  SER   A C   
306  O O   . SER   A 38  ? 0.2855 0.2342 1.2421 0.0159  0.0317  0.1086  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2586 0.1618 1.1508 0.0236  0.1787  0.0658  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2608 0.1830 1.2146 0.0259  0.1299  0.0853  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2998 0.2242 1.3097 0.0203  0.1346  0.0998  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3193 0.2558 1.4445 0.0183  0.0998  0.1316  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3397 0.2620 1.6189 0.0236  0.1567  0.1525  45  THR   A C   
312  O O   . THR   A 39  ? 0.3632 0.2564 1.6270 0.0273  0.2354  0.1344  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3481 0.2881 1.4167 0.0144  0.0893  0.1238  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3804 0.2981 1.4367 0.0170  0.1645  0.1069  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3888 0.3378 1.3084 0.0101  0.0465  0.1025  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3321 0.2678 1.7567 0.0217  0.1185  0.1919  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3193 0.2444 1.9200 0.0275  0.1703  0.2196  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3364 0.2508 1.9617 0.0284  0.2116  0.2183  46  THR   A C   
319  O O   . THR   A 40  ? 0.3449 0.2330 2.0593 0.0349  0.2928  0.2222  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2916 0.2366 2.0496 0.0224  0.1022  0.2689  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3299 0.2900 2.0531 0.0095  0.0153  0.2830  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2961 0.2451 2.0475 0.0220  0.0744  0.2717  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3432 0.2732 1.8938 0.0214  0.1586  0.2142  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3356 0.2582 1.9008 0.0215  0.1902  0.2124  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3899 0.2886 1.7918 0.0222  0.2461  0.1664  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4330 0.3333 1.6951 0.0199  0.2294  0.1394  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3333 0.2798 1.8989 0.0119  0.1050  0.2324  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3877 0.2611 1.8107 0.0236  0.3112  0.1600  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4441 0.2837 1.7196 0.0197  0.3656  0.1208  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4560 0.3167 1.6192 0.0139  0.3162  0.1069  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4430 0.3217 1.6700 0.0137  0.2888  0.1256  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4728 0.2611 1.8180 0.0215  0.4658  0.1201  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6143 0.3582 1.8220 0.0126  0.5179  0.0866  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7771 0.4672 1.8456 0.0035  0.5689  0.0539  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8136 0.5031 1.8777 0.0053  0.5660  0.0529  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8455 0.4848 1.7928 -0.0091 0.6134  0.0279  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4743 0.3294 1.4774 0.0087  0.3096  0.0760  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4841 0.3554 1.3723 0.0036  0.2710  0.0606  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4835 0.3204 1.3030 -0.0030 0.3245  0.0405  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5158 0.3035 1.2981 -0.0086 0.3915  0.0247  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4500 0.3052 1.2395 -0.0050 0.2945  0.0403  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4596 0.2826 1.1926 -0.0122 0.3400  0.0245  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4629 0.2927 1.0546 -0.0201 0.3118  0.0042  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4873 0.2950 1.0350 -0.0274 0.3372  -0.0057 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4537 0.2844 1.2990 -0.0080 0.3464  0.0448  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5168 0.3223 1.5408 -0.0008 0.4087  0.0692  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4237 0.2814 0.9508 -0.0191 0.2618  -0.0004 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4407 0.3058 0.8494 -0.0259 0.2371  -0.0156 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4683 0.2850 0.7838 -0.0406 0.2817  -0.0346 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4897 0.2752 0.7998 -0.0446 0.3141  -0.0394 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4596 0.3617 0.8301 -0.0208 0.1787  -0.0138 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4852 0.4205 0.9017 -0.0133 0.1260  0.0022  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4897 0.4283 0.9456 -0.0132 0.1231  0.0105  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5024 0.4537 0.9089 -0.0097 0.0876  0.0067  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4841 0.2893 0.7233 -0.0509 0.2814  -0.0439 52  THR   A N   
356  C CA  . THR   A 46  ? 0.5392 0.2902 0.6733 -0.0714 0.3122  -0.0590 52  THR   A CA  
357  C C   . THR   A 46  ? 0.5282 0.3031 0.5863 -0.0761 0.2654  -0.0610 52  THR   A C   
358  O O   . THR   A 46  ? 0.5133 0.3327 0.5708 -0.0687 0.2227  -0.0556 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5925 0.3119 0.6899 -0.0832 0.3362  -0.0649 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6283 0.3100 0.7932 -0.0814 0.3949  -0.0640 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6547 0.3202 0.6227 -0.1097 0.3452  -0.0771 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5294 0.2728 0.5289 -0.0884 0.2749  -0.0669 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.5153 0.2782 0.4511 -0.0948 0.2324  -0.0652 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5568 0.2742 0.3946 -0.1213 0.2355  -0.0694 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.6101 0.2545 0.3924 -0.1423 0.2786  -0.0782 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.5125 0.2680 0.4390 -0.0957 0.2321  -0.0657 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4695 0.2585 0.4945 -0.0730 0.2331  -0.0604 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.5179 0.2998 0.3961 -0.1005 0.1861  -0.0600 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4390 0.2923 0.5163 -0.0534 0.1849  -0.0507 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.5257 0.2781 0.3411 -0.1223 0.1924  -0.0621 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.5496 0.2655 0.2795 -0.1491 0.1813  -0.0601 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5943 0.2675 0.2508 -0.1732 0.1729  -0.0576 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.5682 0.2724 0.2510 -0.1625 0.1548  -0.0529 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.5034 0.2766 0.2516 -0.1401 0.1359  -0.0484 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.6663 0.2612 0.2244 -0.2083 0.1846  -0.0600 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.7381 0.2788 0.2101 -0.2392 0.1695  -0.0544 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.7990 0.3176 0.2059 -0.2677 0.1310  -0.0410 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.8841 0.3253 0.2097 -0.2960 0.1530  -0.0476 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.8111 0.2540 0.2129 -0.2607 0.2267  -0.0699 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.7978 0.2601 0.2804 -0.2321 0.2708  -0.0807 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.7772 0.3023 0.3171 -0.2119 0.2404  -0.0731 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.7386 0.2783 0.3587 -0.1870 0.2798  -0.0810 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6891 0.2898 0.3813 -0.1629 0.2595  -0.0759 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.6249 0.2763 0.3186 -0.1585 0.2067  -0.0649 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.6511 0.2604 0.4199 -0.1434 0.2926  -0.0799 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.7577 0.3442 0.2089 -0.2589 0.0769  -0.0214 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.7612 0.3477 0.1867 -0.2785 0.0361  -0.0037 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.7204 0.3731 0.2035 -0.2706 -0.0184 0.0222  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6705 0.3685 0.2089 -0.2483 -0.0213 0.0236  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.7302 0.3496 0.2003 -0.2583 0.0530  -0.0119 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.6045 0.3367 0.2055 -0.2066 0.0449  -0.0104 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.7278 0.3869 0.2074 -0.2873 -0.0586 0.0441  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.6910 0.4129 0.2437 -0.2780 -0.1035 0.0720  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.6324 0.4131 0.2552 -0.2554 -0.1090 0.0787  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.6199 0.4300 0.2873 -0.2600 -0.1463 0.1068  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.7735 0.4504 0.2768 -0.3217 -0.1554 0.1026  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.8891 0.5265 0.3472 -0.3573 -0.1905 0.1226  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.9109 0.5375 0.3492 -0.3536 -0.1667 0.1071  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.9521 0.5700 0.4004 -0.3896 -0.2450 0.1566  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5932 0.3902 0.2327 -0.2309 -0.0712 0.0551  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.5171 0.3655 0.2171 -0.2078 -0.0712 0.0581  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4432 0.3563 0.2285 -0.1821 -0.0865 0.0743  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4418 0.3730 0.2519 -0.1665 -0.0792 0.0701  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5066 0.3629 0.2180 -0.1838 -0.0297 0.0311  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.5657 0.3557 0.2034 -0.2074 -0.0033 0.0152  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3977 0.3407 0.2273 -0.1776 -0.1027 0.0922  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3479 0.3447 0.2605 -0.1510 -0.1043 0.1061  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.3017 0.3254 0.2443 -0.1261 -0.0822 0.0957  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2749 0.3308 0.2781 -0.1097 -0.0814 0.1105  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3598 0.3675 0.3177 -0.1677 -0.1422 0.1444  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3979 0.4008 0.3644 -0.1777 -0.1611 0.1588  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4227 0.4414 0.4563 -0.1928 -0.2007 0.2026  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4556 0.4392 0.4569 -0.2310 -0.2430 0.2257  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3755 0.4411 0.5050 -0.1653 -0.1872 0.2172  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2934 0.2986 0.1950 -0.1255 -0.0631 0.0729  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2620 0.2872 0.1848 -0.1041 -0.0441 0.0621  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2392 0.2527 0.1406 -0.0929 -0.0193 0.0356  60  THR   A C   
418  O O   . THR   A 54  ? 0.2718 0.2535 0.1343 -0.1070 -0.0116 0.0247  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3252 0.3438 0.2384 -0.1171 -0.0523 0.0696  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3944 0.3699 0.2449 -0.1396 -0.0484 0.0572  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3164 0.3463 0.2638 -0.1308 -0.0818 0.1016  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2146 0.2481 0.1426 -0.0695 -0.0067 0.0276  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2023 0.2273 0.1259 -0.0597 0.0091  0.0091  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1882 0.2271 0.1324 -0.0400 0.0133  0.0059  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1983 0.2487 0.1528 -0.0341 0.0113  0.0146  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1803 0.2125 0.1299 -0.0321 0.0185  -0.0048 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1889 0.2208 0.1454 -0.0192 0.0160  -0.0067 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1969 0.2213 0.1573 -0.0124 0.0114  -0.0102 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1912 0.2115 0.1639 -0.0160 0.0134  -0.0148 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2145 0.2403 0.1793 -0.0216 0.0182  -0.0112 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2312 0.2478 0.1975 -0.0133 0.0077  -0.0105 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2312 0.2618 0.1877 -0.0288 0.0225  -0.0080 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2003 0.2159 0.1477 -0.0037 0.0079  -0.0080 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1925 0.1930 0.1358 -0.0001 -0.0002 -0.0108 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2202 0.1930 0.1451 0.0001  -0.0137 -0.0106 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2430 0.2049 0.1478 0.0003  -0.0117 -0.0088 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1896 0.1889 0.1231 0.0053  0.0064  -0.0083 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2252 0.2041 0.1331 0.0118  0.0172  -0.0049 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2324 0.2226 0.1498 0.0141  0.0310  0.0026  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2710 0.2131 0.1447 0.0143  0.0170  -0.0078 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2695 0.2362 0.1705 0.0211  0.0509  0.0067  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3102 0.2193 0.1508 0.0188  0.0369  -0.0060 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3095 0.2316 0.1674 0.0233  0.0572  0.0011  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3457 0.2315 0.1788 0.0287  0.0860  0.0040  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2167 0.1743 0.1471 -0.0021 -0.0297 -0.0105 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2663 0.1873 0.1724 -0.0077 -0.0523 -0.0062 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3167 0.1991 0.1661 -0.0074 -0.0517 -0.0077 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2972 0.1811 0.1475 -0.0041 -0.0475 -0.0101 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2602 0.1798 0.2104 -0.0139 -0.0758 0.0002  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3192 0.1948 0.2416 -0.0250 -0.1091 0.0098  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3498 0.2118 0.2578 -0.0307 -0.1178 0.0144  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3561 0.1974 0.2589 -0.0328 -0.1347 0.0153  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4009 0.2134 0.2743 -0.0458 -0.1538 0.0257  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4093 0.1977 0.2738 -0.0493 -0.1725 0.0270  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4452 0.2181 0.2942 -0.0566 -0.1830 0.0327  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5255 0.2358 0.3240 -0.0774 -0.2245 0.0458  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3670 0.2073 0.1613 -0.0121 -0.0525 -0.0066 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4344 0.2195 0.1596 -0.0143 -0.0433 -0.0093 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5116 0.2320 0.1801 -0.0321 -0.0771 -0.0041 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5448 0.2326 0.1746 -0.0403 -0.0824 -0.0015 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4567 0.2318 0.1555 -0.0068 -0.0065 -0.0116 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5577 0.2432 0.1602 -0.0114 0.0185  -0.0155 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5383 0.2346 0.1974 -0.0404 -0.1022 -0.0012 66  SER   A N   
464  C CA  . SER   A 60  ? 0.6052 0.2360 0.2137 -0.0625 -0.1453 0.0085  66  SER   A CA  
465  C C   . SER   A 60  ? 0.6968 0.2366 0.1880 -0.0764 -0.1371 0.0052  66  SER   A C   
466  O O   . SER   A 60  ? 0.7635 0.2485 0.2063 -0.0976 -0.1723 0.0149  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6648 0.2891 0.2908 -0.0685 -0.1722 0.0136  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.7534 0.3541 0.3333 -0.0629 -0.1453 0.0031  66  SER   A OG  
469  N N   . SER   A 61  ? 0.7120 0.2300 0.1581 -0.0661 -0.0890 -0.0067 67  SER   A N   
470  C CA  . SER   A 61  ? 0.7962 0.2140 0.1232 -0.0788 -0.0659 -0.0118 67  SER   A CA  
471  C C   . SER   A 61  ? 0.8223 0.2277 0.1274 -0.0805 -0.0534 -0.0109 67  SER   A C   
472  O O   . SER   A 61  ? 0.9257 0.2392 0.1260 -0.0937 -0.0335 -0.0146 67  SER   A O   
473  C CB  . SER   A 61  ? 0.8030 0.2035 0.1076 -0.0648 -0.0090 -0.0224 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.7613 0.2388 0.1476 -0.0403 0.0307  -0.0241 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.7468 0.2372 0.1440 -0.0682 -0.0609 -0.0068 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.7540 0.2390 0.1387 -0.0701 -0.0545 -0.0049 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.7463 0.2686 0.1862 -0.0786 -0.1037 0.0067  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.7663 0.2890 0.2029 -0.0807 -0.1033 0.0095  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.7127 0.2606 0.1570 -0.0462 -0.0054 -0.0101 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.7695 0.2783 0.1742 -0.0369 0.0504  -0.0167 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.8630 0.2759 0.1650 -0.0490 0.0757  -0.0192 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.9190 0.3001 0.2054 -0.0365 0.1412  -0.0237 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.9830 0.2902 0.2016 -0.0419 0.1669  -0.0294 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.0243 0.2754 0.1712 -0.0626 0.1274  -0.0317 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.9936 0.2760 0.2165 -0.0283 0.2333  -0.0311 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.7075 0.2662 0.2113 -0.0813 -0.1411 0.0146  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6666 0.2676 0.2495 -0.0862 -0.1800 0.0281  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.6032 0.2732 0.2509 -0.0688 -0.1514 0.0233  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5912 0.2654 0.2569 -0.0749 -0.1677 0.0312  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.7476 0.2761 0.2754 -0.1147 -0.2314 0.0446  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.8443 0.3256 0.3523 -0.1352 -0.2790 0.0576  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.9758 0.3886 0.4433 -0.1677 -0.3412 0.0804  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.1350 0.4585 0.5160 -0.1954 -0.3812 0.0895  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.2866 0.4959 0.5325 -0.2276 -0.4080 0.0954  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.3351 0.5091 0.5217 -0.2346 -0.3977 0.0933  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.3630 0.4851 0.5233 -0.2551 -0.4441 0.1031  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5465 0.2652 0.2241 -0.0492 -0.1099 0.0115  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4904 0.2642 0.2154 -0.0363 -0.0839 0.0077  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4147 0.2486 0.2000 -0.0224 -0.0623 0.0020  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4010 0.2323 0.1783 -0.0182 -0.0539 -0.0017 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5517 0.3004 0.2224 -0.0311 -0.0493 0.0021  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6688 0.3726 0.2880 -0.0414 -0.0556 0.0057  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7471 0.4340 0.3313 -0.0320 -0.0098 0.0003  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8319 0.4942 0.3854 -0.0375 -0.0066 0.0029  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9160 0.4809 0.3645 -0.0577 -0.0201 0.0044  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3492 0.2300 0.1858 -0.0172 -0.0525 0.0015  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3047 0.2306 0.1817 -0.0091 -0.0324 -0.0030 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3181 0.2552 0.1821 -0.0027 -0.0069 -0.0036 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3378 0.2643 0.1846 -0.0034 -0.0024 -0.0016 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2776 0.2346 0.2105 -0.0116 -0.0347 -0.0025 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2718 0.2228 0.2419 -0.0164 -0.0545 0.0023  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2895 0.2561 0.2953 -0.0148 -0.0474 -0.0001 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2860 0.2169 0.2708 -0.0239 -0.0811 0.0123  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2645 0.2223 0.3128 -0.0194 -0.0668 0.0088  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2941 0.2306 0.3332 -0.0259 -0.0912 0.0181  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2867 0.2445 0.1649 0.0026  0.0082  -0.0035 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2687 0.2398 0.1539 0.0075  0.0285  0.0022  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2356 0.2446 0.1584 0.0041  0.0284  0.0061  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2213 0.2387 0.1542 0.0020  0.0235  0.0042  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2945 0.2416 0.1607 0.0146  0.0473  0.0048  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3594 0.2503 0.1674 0.0138  0.0541  0.0012  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3981 0.2692 0.1861 0.0144  0.0687  0.0037  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.4205 0.2694 0.1855 0.0103  0.0471  -0.0038 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4658 0.2700 0.1838 0.0099  0.0778  0.0003  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4866 0.2666 0.1789 0.0039  0.0520  -0.0065 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.5173 0.2722 0.1823 0.0030  0.0682  -0.0048 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6114 0.2844 0.1895 -0.0066 0.0769  -0.0078 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2184 0.2445 0.1567 0.0010  0.0322  0.0126  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2131 0.2622 0.1738 -0.0083 0.0269  0.0195  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2198 0.2780 0.2046 -0.0046 0.0324  0.0337  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2388 0.2911 0.2343 0.0052  0.0485  0.0414  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2164 0.2731 0.1815 -0.0145 0.0258  0.0238  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2309 0.2762 0.1897 -0.0035 0.0377  0.0253  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2333 0.2522 0.1641 0.0034  0.0395  0.0156  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2078 0.2760 0.2038 -0.0132 0.0220  0.0390  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2127 0.2911 0.2429 -0.0108 0.0238  0.0560  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2014 0.2904 0.2451 -0.0295 0.0018  0.0702  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1968 0.2755 0.2075 -0.0440 -0.0096 0.0609  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2276 0.2957 0.2515 -0.0004 0.0328  0.0490  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2715 0.3149 0.2775 0.0146  0.0554  0.0420  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2224 0.2849 0.2191 -0.0069 0.0212  0.0340  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1778 0.2808 0.2712 -0.0309 -0.0030 0.0951  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1874 0.2948 0.2963 -0.0514 -0.0307 0.1145  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1857 0.2955 0.3100 -0.0422 -0.0243 0.1147  75  SER   A C   
545  O O   . SER   A 69  ? 0.1957 0.3074 0.3424 -0.0212 0.0019  0.1120  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2012 0.3246 0.3738 -0.0591 -0.0449 0.1483  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2891 0.4103 0.4503 -0.0674 -0.0513 0.1496  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1766 0.2783 0.2785 -0.0584 -0.0441 0.1151  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1721 0.2764 0.2867 -0.0498 -0.0385 0.1141  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1962 0.3001 0.3268 -0.0717 -0.0690 0.1374  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2365 0.3252 0.3400 -0.0982 -0.0965 0.1470  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1841 0.2737 0.2482 -0.0406 -0.0238 0.0834  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1970 0.2662 0.2069 -0.0579 -0.0326 0.0682  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1976 0.2580 0.1817 -0.0576 -0.0240 0.0537  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2227 0.2760 0.2075 -0.0744 -0.0447 0.0683  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2320 0.2671 0.1721 -0.0731 -0.0232 0.0405  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2489 0.2716 0.1802 -0.0909 -0.0425 0.0537  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2484 0.2618 0.1606 -0.0896 -0.0293 0.0399  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1683 0.2834 0.3412 -0.0631 -0.0659 0.1488  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1850 0.3007 0.3844 -0.0848 -0.0992 0.1769  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2139 0.3019 0.3410 -0.1042 -0.1150 0.1621  77  SER   A C   
562  O O   . SER   A 71  ? 0.2281 0.3023 0.3006 -0.0960 -0.0947 0.1306  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1846 0.3226 0.4677 -0.0679 -0.0869 0.1978  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1884 0.3215 0.4459 -0.0497 -0.0616 0.1732  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2426 0.3170 0.3688 -0.1323 -0.1520 0.1866  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3052 0.3436 0.3565 -0.1522 -0.1620 0.1729  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2994 0.3525 0.3687 -0.1301 -0.1409 0.1600  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2750 0.3594 0.4189 -0.1113 -0.1338 0.1751  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3763 0.3837 0.4079 -0.1941 -0.2119 0.2048  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4643 0.4417 0.4525 -0.2217 -0.2342 0.2132  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5955 0.5083 0.5033 -0.2729 -0.2800 0.2311  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7122 0.5868 0.5598 -0.2976 -0.2914 0.2302  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8493 0.6368 0.5785 -0.3496 -0.3228 0.2353  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3179 0.3458 0.3241 -0.1321 -0.1277 0.1336  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3153 0.3571 0.3409 -0.1121 -0.1108 0.1230  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3119 0.3659 0.3867 -0.1195 -0.1342 0.1522  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3220 0.3523 0.3755 -0.1512 -0.1692 0.1733  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3646 0.3711 0.3180 -0.1207 -0.0985 0.0966  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4042 0.3727 0.2960 -0.1451 -0.1031 0.0917  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3584 0.3402 0.2780 -0.1531 -0.1241 0.1140  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2910 0.3760 0.4308 -0.0928 -0.1158 0.1561  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2814 0.3821 0.4870 -0.0963 -0.1330 0.1869  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2579 0.3756 0.5001 -0.0662 -0.1004 0.1759  80  SER   A C   
584  O O   . SER   A 74  ? 0.2499 0.3634 0.4604 -0.0456 -0.0698 0.1457  80  SER   A O   
585  C CB  . SER   A 74  ? 0.3003 0.4197 0.5828 -0.1034 -0.1518 0.2247  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3425 0.4833 0.6766 -0.0741 -0.1149 0.2208  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2348 0.3665 0.5417 -0.0663 -0.1095 0.2019  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2310 0.3728 0.5749 -0.0405 -0.0777 0.1952  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2142 0.3685 0.6269 -0.0186 -0.0445 0.2061  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2036 0.3741 0.6966 -0.0252 -0.0564 0.2420  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2164 0.3669 0.6111 -0.0510 -0.0999 0.2229  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2625 0.3958 0.5947 -0.0652 -0.1180 0.2093  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2627 0.4036 0.6522 -0.0818 -0.1497 0.2457  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2839 0.4124 0.5839 -0.0407 -0.0828 0.1754  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2166 0.3573 0.5984 0.0047  -0.0038 0.1780  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2183 0.3543 0.6433 0.0242  0.0364  0.1830  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2514 0.3641 0.6671 0.0450  0.0780  0.1670  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2721 0.3666 0.6143 0.0474  0.0782  0.1379  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2456 0.3704 0.6206 0.0261  0.0443  0.1648  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2464 0.3896 0.6366 0.0047  0.0063  0.1844  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2561 0.3617 0.6555 0.0465  0.0936  0.1644  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2944 0.4276 0.6201 0.0015  0.0040  0.1625  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2410 0.3497 0.7342 0.0586  0.1145  0.1878  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2935 0.3674 0.7738 0.0765  0.1614  0.1740  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3315 0.3570 0.7161 0.0853  0.1918  0.1399  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3399 0.3566 0.7149 0.0866  0.2032  0.1387  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2940 0.3676 0.8864 0.0886  0.2022  0.2065  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.3489 0.3835 0.9329 0.1037  0.2498  0.1959  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3712 0.4191 0.9665 0.1009  0.2317  0.1983  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4023 0.3779 0.9543 0.1184  0.3138  0.1816  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4071 0.4163 0.9966 0.1142  0.2771  0.1896  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4398 0.3671 0.9743 0.1294  0.3610  0.1718  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4327 0.3794 0.9891 0.1278  0.3421  0.1760  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3542 0.3461 0.6656 0.0887  0.1997  0.1139  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4097 0.3477 0.6225 0.0912  0.2175  0.0845  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.4667 0.3448 0.6444 0.0999  0.2610  0.0740  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.4714 0.3518 0.6467 0.0998  0.2520  0.0705  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4176 0.3646 0.5593 0.0800  0.1718  0.0623  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.4644 0.3529 0.5107 0.0790  0.1817  0.0375  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.3976 0.3918 0.5627 0.0695  0.1354  0.0704  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.5173 0.3340 0.6577 0.1056  0.3094  0.0678  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.5841 0.3184 0.6665 0.1104  0.3610  0.0554  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.6246 0.3259 0.6147 0.1015  0.3347  0.0318  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.6297 0.3453 0.5689 0.0910  0.2862  0.0185  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.6849 0.3455 0.6949 0.1092  0.4012  0.0442  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.7689 0.4317 0.8645 0.1209  0.4529  0.0668  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9003 0.5002 1.0213 0.1321  0.5302  0.0744  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.9687 0.5274 1.0430 0.1307  0.5417  0.0625  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.9176 0.5083 1.1118 0.1424  0.5821  0.0937  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.6525 0.3011 0.6199 0.1050  0.3702  0.0273  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.7017 0.3086 0.5778 0.0948  0.3462  0.0066  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.7751 0.3098 0.5253 0.0793  0.3328  -0.0141 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.8191 0.3011 0.5297 0.0779  0.3679  -0.0161 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.7251 0.2724 0.5890 0.1000  0.3958  0.0053  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.7829 0.3146 0.4769 0.0666  0.2811  -0.0263 87  SER   A N   
636  C CA  . SER   A 81  ? 0.8368 0.3021 0.4200 0.0479  0.2548  -0.0406 87  SER   A CA  
637  C C   . SER   A 81  ? 0.8752 0.2970 0.3929 0.0343  0.2239  -0.0504 87  SER   A C   
638  O O   . SER   A 81  ? 0.8482 0.2942 0.4072 0.0420  0.2292  -0.0479 87  SER   A O   
639  C CB  . SER   A 81  ? 0.8139 0.3460 0.4302 0.0449  0.2064  -0.0375 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.7855 0.3858 0.4504 0.0444  0.1573  -0.0357 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.9299 0.2884 0.3508 0.0128  0.1874  -0.0588 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.9588 0.2808 0.3276 -0.0031 0.1461  -0.0634 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.8581 0.2815 0.3212 0.0036  0.0957  -0.0568 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.8672 0.2783 0.3166 -0.0047 0.0660  -0.0578 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.1023 0.3267 0.3488 -0.0324 0.1115  -0.0680 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.1884 0.4381 0.4442 -0.0364 0.0875  -0.0636 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.3896 0.5630 0.5503 -0.0674 0.0332  -0.0618 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.4692 0.5722 0.5582 -0.0884 0.0041  -0.0621 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.4336 0.6157 0.5929 -0.0725 0.0166  -0.0579 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.7555 0.2735 0.3125 0.0175  0.0898  -0.0497 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.6651 0.2674 0.3024 0.0223  0.0517  -0.0444 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.5803 0.2518 0.3029 0.0396  0.0737  -0.0385 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.5503 0.2671 0.3179 0.0412  0.0500  -0.0364 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.6337 0.2800 0.3025 0.0199  0.0249  -0.0407 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.6809 0.2606 0.2722 0.0028  0.0061  -0.0429 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.7175 0.2598 0.2733 -0.0154 -0.0411 -0.0405 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7122 0.2639 0.2689 0.0030  0.0328  -0.0444 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.7836 0.2611 0.2683 -0.0352 -0.0662 -0.0384 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.7801 0.2655 0.2591 -0.0151 0.0136  -0.0455 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.8264 0.2727 0.2663 -0.0355 -0.0381 -0.0420 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.9223 0.2937 0.2793 -0.0580 -0.0629 -0.0397 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.5496 0.2274 0.2991 0.0510  0.1173  -0.0330 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.4793 0.2223 0.3172 0.0638  0.1304  -0.0214 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.5126 0.2281 0.3674 0.0740  0.1838  -0.0142 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.5448 0.2103 0.3626 0.0742  0.2168  -0.0162 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3984 0.2108 0.3012 0.0668  0.1184  -0.0109 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.3443 0.1894 0.2481 0.0587  0.0768  -0.0154 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3462 0.1829 0.2246 0.0531  0.0664  -0.0190 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3104 0.1934 0.2461 0.0567  0.0524  -0.0149 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3066 0.1705 0.1956 0.0465  0.0341  -0.0216 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2880 0.1949 0.2316 0.0499  0.0243  -0.0182 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2905 0.1905 0.2163 0.0454  0.0166  -0.0208 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2766 0.1954 0.2172 0.0393  -0.0061 -0.0229 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.4913 0.2390 0.4100 0.0827  0.1960  -0.0037 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.4979 0.2296 0.4625 0.0941  0.2502  0.0096  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.4631 0.2499 0.5074 0.0991  0.2528  0.0289  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.4435 0.2785 0.4987 0.0927  0.2122  0.0299  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.4837 0.2444 0.5037 0.0996  0.2494  0.0184  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.4498 0.2731 0.4865 0.0925  0.1917  0.0172  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.4574 0.2615 0.4215 0.0822  0.1621  0.0003  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.4612 0.2406 0.5681 0.1095  0.3002  0.0466  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.4237 0.2540 0.6179 0.1128  0.3003  0.0701  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3583 0.2699 0.6265 0.1070  0.2490  0.0881  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3486 0.2745 0.6454 0.1079  0.2419  0.0937  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.4163 0.2213 0.6818 0.1256  0.3637  0.0902  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3190 0.2731 0.5963 0.0978  0.2104  0.0929  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2670 0.2788 0.5871 0.0865  0.1620  0.1071  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2371 0.2834 0.5843 0.0761  0.1348  0.1214  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2497 0.2803 0.5797 0.0796  0.1516  0.1166  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2868 0.2951 0.5341 0.0794  0.1313  0.0823  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3136 0.3186 0.4975 0.0716  0.1090  0.0635  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3204 0.2908 0.4283 0.0714  0.1040  0.0373  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3118 0.2955 0.3887 0.0619  0.0735  0.0262  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2912 0.2654 0.3413 0.0596  0.0721  0.0201  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2492 0.2351 0.2808 0.0514  0.0477  0.0115  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2984 0.2471 0.3412 0.0656  0.0990  0.0227  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2142 0.2992 0.5906 0.0608  0.0918  0.1372  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2144 0.3201 0.5887 0.0456  0.0606  0.1454  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2092 0.3053 0.4953 0.0378  0.0407  0.1157  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2123 0.3057 0.4684 0.0341  0.0284  0.1040  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2219 0.3576 0.6527 0.0263  0.0210  0.1776  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2335 0.3860 0.7759 0.0302  0.0315  0.2167  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2544 0.4177 0.8509 0.0280  0.0323  0.2392  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2390 0.3974 0.8430 0.0362  0.0410  0.2337  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2389 0.4194 0.9575 0.0313  0.0418  0.2807  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2207 0.3956 0.9453 0.0399  0.0520  0.2743  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2312 0.4170 1.0173 0.0380  0.0539  0.2985  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2310 0.4344 1.1547 0.0419  0.0655  0.3435  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1834 0.2734 0.4354 0.0361  0.0405  0.1050  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1748 0.2569 0.3597 0.0282  0.0238  0.0814  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1655 0.2631 0.3531 0.0075  -0.0058 0.0945  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1537 0.2621 0.3761 0.0030  -0.0098 0.1136  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1800 0.2399 0.3233 0.0375  0.0412  0.0623  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1665 0.2211 0.2587 0.0293  0.0237  0.0424  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2249 0.2526 0.2766 0.0371  0.0345  0.0250  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2285 0.2279 0.2614 0.0463  0.0505  0.0186  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1989 0.2277 0.2302 0.0308  0.0242  0.0173  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1578 0.2505 0.3102 -0.0068 -0.0251 0.0871  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1702 0.2594 0.3037 -0.0317 -0.0512 0.0975  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1976 0.2726 0.2819 -0.0357 -0.0467 0.0780  96  SER   A C   
721  O O   . SER   A 90  ? 0.2038 0.2735 0.2704 -0.0204 -0.0286 0.0564  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1985 0.2756 0.3086 -0.0480 -0.0679 0.0992  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2373 0.3002 0.3071 -0.0408 -0.0529 0.0721  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2098 0.2750 0.2743 -0.0579 -0.0653 0.0884  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2238 0.2716 0.2433 -0.0651 -0.0600 0.0728  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2075 0.2698 0.2455 -0.0455 -0.0433 0.0652  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2186 0.2702 0.2280 -0.0425 -0.0323 0.0467  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2471 0.2712 0.2228 -0.0671 -0.0469 0.0495  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3016 0.3003 0.2459 -0.0898 -0.0598 0.0562  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3864 0.3437 0.2718 -0.1192 -0.0674 0.0577  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3164 0.3193 0.2746 -0.0894 -0.0666 0.0630  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.4073 0.3408 0.2670 -0.1371 -0.0794 0.0653  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3657 0.3301 0.2731 -0.1193 -0.0809 0.0697  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1876 0.2695 0.2751 -0.0334 -0.0394 0.0810  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1826 0.2684 0.2795 -0.0160 -0.0195 0.0741  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1645 0.2581 0.2791 -0.0257 -0.0289 0.0907  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1692 0.2728 0.3208 -0.0388 -0.0480 0.1172  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1652 0.2550 0.3011 0.0035  0.0017  0.0801  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1846 0.2597 0.3115 0.0209  0.0292  0.0696  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2095 0.2643 0.2784 0.0234  0.0294  0.0431  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2083 0.2725 0.3661 0.0363  0.0573  0.0766  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1548 0.2434 0.2489 -0.0197 -0.0179 0.0780  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1577 0.2530 0.2663 -0.0279 -0.0254 0.0918  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1724 0.2691 0.2999 -0.0078 0.0009  0.0891  99  MET   A C   
745  O O   . MET   A 93  ? 0.2039 0.2852 0.2957 0.0037  0.0164  0.0674  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1788 0.2586 0.2339 -0.0429 -0.0344 0.0771  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2341 0.2945 0.2522 -0.0663 -0.0526 0.0770  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2945 0.3243 0.2491 -0.0794 -0.0447 0.0546  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2990 0.3337 0.2581 -0.0536 -0.0194 0.0294  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1409 0.2500 0.3245 -0.0051 0.0061  0.1129  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1519 0.2522 0.3489 0.0129  0.0385  0.1106  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1538 0.2573 0.3463 0.0083  0.0353  0.1127  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1490 0.2673 0.3601 -0.0085 0.0091  0.1291  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1390 0.2447 0.4122 0.0239  0.0615  0.1355  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1819 0.2804 0.4643 0.0320  0.0735  0.1338  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.1872 0.2835 0.5483 0.0454  0.1081  0.1571  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2238 0.2907 0.4311 0.0413  0.0897  0.1019  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1702 0.2540 0.3357 0.0214  0.0614  0.0980  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1813 0.2645 0.3410 0.0205  0.0647  0.0981  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2022 0.2595 0.3676 0.0374  0.1058  0.0978  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2209 0.2486 0.3620 0.0475  0.1298  0.0876  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2135 0.2858 0.3077 0.0154  0.0525  0.0733  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1938 0.2548 0.3866 0.0389  0.1165  0.1096  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2337 0.2590 0.4200 0.0531  0.1613  0.1074  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3034 0.2963 0.3983 0.0515  0.1588  0.0795  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3213 0.3311 0.4015 0.0433  0.1349  0.0749  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2292 0.2707 0.4880 0.0552  0.1750  0.1331  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2739 0.2681 0.5123 0.0686  0.2272  0.1275  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1788 0.2516 0.5431 0.0545  0.1720  0.1676  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3454 0.2894 0.3798 0.0567  0.1792  0.0629  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3967 0.3047 0.3479 0.0514  0.1690  0.0415  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4446 0.2879 0.3247 0.0522  0.1868  0.0277  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.4665 0.2967 0.3583 0.0577  0.2063  0.0307  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.4602 0.2574 0.2635 0.0444  0.1785  0.0141  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.5048 0.2270 0.2229 0.0384  0.1867  0.0022  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4908 0.2217 0.1947 0.0317  0.1493  -0.0053 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.4554 0.2257 0.1783 0.0262  0.1102  -0.0071 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.5561 0.2165 0.1921 0.0275  0.1849  -0.0054 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.6708 0.2367 0.2022 0.0151  0.1903  -0.0155 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.7657 0.2613 0.2538 0.0181  0.2438  -0.0172 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.7184 0.2508 0.1896 -0.0013 0.1472  -0.0220 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.8314 0.2445 0.2168 0.0010  0.2312  -0.0270 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.8119 0.2469 0.1877 -0.0116 0.1691  -0.0284 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5146 0.1969 0.1781 0.0310  0.1650  -0.0099 105 SER   A N   
785  C CA  . SER   A 99  ? 0.5501 0.2255 0.1892 0.0230  0.1313  -0.0166 105 SER   A CA  
786  C C   . SER   A 99  ? 0.6445 0.2305 0.1999 0.0166  0.1539  -0.0236 105 SER   A C   
787  O O   . SER   A 99  ? 0.6875 0.2339 0.2298 0.0235  0.2045  -0.0223 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5010 0.2505 0.2206 0.0311  0.1178  -0.0117 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5261 0.2762 0.2766 0.0417  0.1537  -0.0055 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.6871 0.2351 0.1857 0.0016  0.1170  -0.0293 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.7641 0.2229 0.1732 -0.0102 0.1247  -0.0359 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.7571 0.2506 0.1977 -0.0122 0.0858  -0.0357 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.7088 0.2819 0.2265 -0.0073 0.0536  -0.0312 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.8793 0.2355 0.1686 -0.0343 0.1107  -0.0397 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.9607 0.2839 0.2225 -0.0310 0.1542  -0.0403 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.1091 0.3356 0.2548 -0.0559 0.1390  -0.0426 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.1675 0.3067 0.2127 -0.0808 0.1104  -0.0449 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.1204 0.3545 0.2728 -0.0528 0.1530  -0.0405 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.8011 0.2386 0.1902 -0.0181 0.0935  -0.0403 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.7635 0.2438 0.1972 -0.0172 0.0601  -0.0390 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.7308 0.2421 0.1904 -0.0286 -0.0015 -0.0334 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.6774 0.2639 0.2206 -0.0195 -0.0191 -0.0301 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.8342 0.2243 0.1809 -0.0279 0.0745  -0.0452 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.8828 0.2101 0.1788 -0.0233 0.1386  -0.0498 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.8657 0.1988 0.1591 -0.0246 0.1400  -0.0472 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.7687 0.2185 0.1603 -0.0492 -0.0316 -0.0305 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.7422 0.2135 0.1668 -0.0619 -0.0900 -0.0200 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.6560 0.2196 0.1802 -0.0478 -0.0927 -0.0161 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6363 0.2304 0.2140 -0.0538 -0.1319 -0.0066 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.6048 0.2090 0.1576 -0.0305 -0.0502 -0.0215 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.5199 0.2034 0.1558 -0.0195 -0.0500 -0.0187 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4486 0.2007 0.1650 -0.0090 -0.0523 -0.0183 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4152 0.2213 0.1927 -0.0046 -0.0557 -0.0161 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5135 0.2131 0.1532 -0.0082 -0.0105 -0.0211 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.5850 0.2267 0.1580 -0.0191 -0.0108 -0.0207 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.5929 0.2126 0.1479 -0.0339 -0.0496 -0.0159 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6261 0.2383 0.1651 -0.0140 0.0284  -0.0236 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.4448 0.1900 0.1573 -0.0062 -0.0473 -0.0208 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3919 0.1950 0.1734 0.0020  -0.0486 -0.0205 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3669 0.1927 0.1975 -0.0043 -0.0795 -0.0149 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3928 0.1810 0.2046 -0.0169 -0.1111 -0.0084 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4122 0.1949 0.1758 0.0034  -0.0446 -0.0230 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.4450 0.2230 0.1940 0.0160  0.0025  -0.0260 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3232 0.2020 0.2147 0.0021  -0.0697 -0.0153 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2988 0.1957 0.2467 -0.0023 -0.0867 -0.0096 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2926 0.2050 0.2601 -0.0035 -0.0825 -0.0079 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2749 0.2063 0.2985 -0.0050 -0.0837 -0.0039 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2883 0.1899 0.2134 -0.0028 -0.0737 -0.0104 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2598 0.1777 0.2013 -0.0036 -0.0681 -0.0093 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2162 0.1740 0.1935 0.0007  -0.0444 -0.0136 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2082 0.1791 0.1767 0.0046  -0.0294 -0.0168 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1938 0.1641 0.2093 -0.0024 -0.0417 -0.0120 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1861 0.1768 0.2187 -0.0036 -0.0181 -0.0167 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1882 0.1884 0.1935 -0.0046 -0.0071 -0.0183 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2072 0.2034 0.2023 -0.0043 -0.0123 -0.0162 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2136 0.2034 0.2999 -0.0074 -0.0116 -0.0144 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2334 0.2192 0.3592 -0.0065 -0.0125 -0.0118 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2262 0.2194 0.3129 -0.0128 0.0156  -0.0197 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2376 0.2186 0.4418 -0.0086 -0.0089 -0.0024 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1849 0.1948 0.1805 -0.0084 0.0058  -0.0200 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1881 0.2059 0.1663 -0.0141 0.0125  -0.0176 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2029 0.2107 0.1830 -0.0264 0.0270  -0.0221 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1952 0.1915 0.1776 -0.0316 0.0368  -0.0259 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2025 0.2290 0.1693 -0.0155 0.0111  -0.0114 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2122 0.2447 0.1691 -0.0265 0.0105  -0.0031 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2073 0.2467 0.1666 -0.0213 0.0105  0.0012  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2165 0.2582 0.1785 -0.0292 0.0034  0.0092  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2135 0.2186 0.1892 -0.0315 0.0325  -0.0224 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2427 0.2260 0.2119 -0.0444 0.0527  -0.0279 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2659 0.2431 0.1999 -0.0576 0.0520  -0.0249 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2524 0.2476 0.1888 -0.0522 0.0398  -0.0191 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2763 0.2554 0.2833 -0.0397 0.0624  -0.0302 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3630 0.3460 0.4200 -0.0294 0.0567  -0.0276 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3856 0.3643 0.4894 -0.0282 0.0637  -0.0243 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4183 0.3716 0.5286 -0.0374 0.1012  -0.0303 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4256 0.3616 0.5781 -0.0377 0.1253  -0.0305 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4386 0.3383 0.5800 -0.0483 0.1676  -0.0380 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4192 0.3676 0.6249 -0.0286 0.1090  -0.0221 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2949 0.2390 0.1935 -0.0766 0.0669  -0.0285 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3453 0.2700 0.2022 -0.0953 0.0649  -0.0251 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3964 0.2820 0.2424 -0.1046 0.0982  -0.0364 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3879 0.2706 0.2736 -0.0938 0.1195  -0.0431 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3698 0.2723 0.1787 -0.1169 0.0506  -0.0170 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4118 0.2575 0.1760 -0.1349 0.0764  -0.0276 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4539 0.3067 0.2523 -0.1249 0.1037  -0.0367 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5158 0.3215 0.2988 -0.1351 0.1429  -0.0480 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5618 0.3152 0.3237 -0.1452 0.1799  -0.0581 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5837 0.3010 0.3591 -0.1464 0.2235  -0.0672 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5954 0.3623 0.3110 -0.1609 0.1396  -0.0462 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6864 0.4119 0.3232 -0.1906 0.1198  -0.0392 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.8015 0.4849 0.3726 -0.2188 0.1101  -0.0344 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.8353 0.5488 0.4114 -0.2227 0.0698  -0.0179 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.8306 0.4413 0.3446 -0.2384 0.1499  -0.0478 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5615 0.3059 0.2915 -0.1535 0.1664  -0.0553 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5875 0.2767 0.2893 -0.1647 0.2026  -0.0646 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.5319 0.2560 0.3182 -0.1382 0.2153  -0.0664 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5663 0.2483 0.3518 -0.1426 0.2540  -0.0737 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.6478 0.2993 0.2671 -0.1911 0.1821  -0.0597 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.7496 0.3598 0.2849 -0.2228 0.1602  -0.0527 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.7623 0.4142 0.3009 -0.2259 0.1064  -0.0343 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.8347 0.3613 0.2838 -0.2540 0.1856  -0.0598 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.8199 0.4198 0.2833 -0.2580 0.0944  -0.0285 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8721 0.3920 0.2707 -0.2773 0.1400  -0.0446 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4510 0.2447 0.3057 -0.1131 0.1832  -0.0586 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3858 0.2087 0.3157 -0.0920 0.1854  -0.0569 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3309 0.2037 0.2772 -0.0779 0.1433  -0.0493 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.3269 0.2246 0.2516 -0.0774 0.1140  -0.0435 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3092 0.1922 0.2962 -0.0670 0.1439  -0.0484 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2855 0.2061 0.2867 -0.0541 0.1102  -0.0425 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2966 0.2133 0.2434 -0.0644 0.0972  -0.0411 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3319 0.2147 0.2465 -0.0781 0.1145  -0.0451 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2852 0.2134 0.3480 -0.0416 0.1122  -0.0402 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2833 0.2387 0.3453 -0.0316 0.0801  -0.0357 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2737 0.2104 0.4032 -0.0327 0.1124  -0.0343 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2757 0.2219 0.2138 -0.0594 0.0687  -0.0336 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2717 0.2203 0.1774 -0.0682 0.0520  -0.0262 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2489 0.2191 0.1785 -0.0546 0.0401  -0.0235 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2631 0.2259 0.1760 -0.0623 0.0360  -0.0202 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2751 0.2413 0.1711 -0.0709 0.0328  -0.0156 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2836 0.2582 0.1696 -0.0786 0.0118  -0.0013 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2996 0.2411 0.1658 -0.0868 0.0418  -0.0177 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2063 0.1983 0.1690 -0.0366 0.0325  -0.0237 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2028 0.2072 0.1802 -0.0249 0.0221  -0.0219 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1930 0.2037 0.1886 -0.0112 0.0124  -0.0222 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1941 0.2014 0.2000 -0.0104 0.0125  -0.0235 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1792 0.1921 0.1739 -0.0028 0.0034  -0.0204 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1762 0.1783 0.1683 0.0048  -0.0083 -0.0203 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1819 0.1792 0.1490 0.0111  -0.0070 -0.0170 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1722 0.1791 0.1416 0.0126  -0.0006 -0.0135 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1930 0.1838 0.2051 0.0062  -0.0190 -0.0213 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2110 0.2068 0.2255 0.0076  -0.0145 -0.0225 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1969 0.1862 0.2504 0.0021  -0.0182 -0.0204 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2287 0.2110 0.2608 0.0096  -0.0292 -0.0215 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1920 0.1682 0.1352 0.0139  -0.0106 -0.0169 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2061 0.1636 0.1217 0.0198  0.0010  -0.0147 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2185 0.1636 0.1281 0.0227  0.0008  -0.0162 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2298 0.1608 0.1356 0.0193  -0.0158 -0.0194 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2551 0.1731 0.1282 0.0184  -0.0007 -0.0162 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2914 0.1777 0.1315 0.0240  0.0230  -0.0152 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2606 0.1918 0.1414 0.0162  -0.0002 -0.0145 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2224 0.1718 0.1373 0.0287  0.0187  -0.0116 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2335 0.1729 0.1463 0.0321  0.0219  -0.0124 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2801 0.1912 0.1758 0.0392  0.0486  -0.0091 125 SER   A C   
924  O O   . SER   A 119 ? 0.3031 0.1845 0.1752 0.0406  0.0530  -0.0130 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2183 0.1962 0.1716 0.0305  0.0171  -0.0082 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2542 0.2273 0.2117 0.0345  0.0212  -0.0074 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2924 0.2079 0.2022 0.0434  0.0699  -0.0011 126 THR   A N   
928  C CA  . THR   A 120 ? 0.3364 0.2192 0.2406 0.0516  0.1064  0.0040  126 THR   A CA  
929  C C   . THR   A 120 ? 0.3663 0.2300 0.2583 0.0532  0.1270  0.0069  126 THR   A C   
930  O O   . THR   A 120 ? 0.3366 0.2239 0.2350 0.0487  0.1097  0.0071  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3186 0.2400 0.2946 0.0579  0.1188  0.0206  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3141 0.2767 0.3415 0.0560  0.1133  0.0354  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3040 0.2503 0.2977 0.0552  0.0975  0.0199  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.4232 0.2424 0.3011 0.0598  0.1686  0.0098  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.4687 0.2687 0.3439 0.0627  0.1958  0.0147  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5451 0.2817 0.4004 0.0699  0.2520  0.0167  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.5753 0.2764 0.4103 0.0719  0.2708  0.0129  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5827 0.2999 0.4410 0.0732  0.2820  0.0221  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.6565 0.3031 0.4962 0.0801  0.3475  0.0246  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.6392 0.3210 0.5783 0.0918  0.3800  0.0474  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.5757 0.3396 0.6102 0.0944  0.3501  0.0655  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.6898 0.3034 0.6043 0.0965  0.4406  0.0482  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.6752 0.3123 0.6914 0.1085  0.4803  0.0727  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.6197 0.3192 0.6755 0.1053  0.4415  0.0813  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5872 0.3336 0.7546 0.1130  0.4525  0.1080  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.6678 0.3554 0.8131 0.1199  0.4934  0.0993  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.7901 0.4050 0.9069 0.1259  0.5511  0.0934  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.8994 0.4152 0.9266 0.1249  0.6076  0.0781  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.7494 0.4035 0.9361 0.1307  0.5413  0.1058  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.6102 0.3031 0.5783 0.0932  0.4002  0.0613  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.5548 0.3014 0.5517 0.0892  0.3646  0.0670  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4739 0.3078 0.5308 0.0840  0.3039  0.0753  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4599 0.3402 0.5522 0.0796  0.2762  0.0836  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4300 0.2784 0.4874 0.0822  0.2837  0.0715  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3641 0.2797 0.4612 0.0745  0.2307  0.0769  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.3646 0.2679 0.3859 0.0667  0.1992  0.0535  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4203 0.2759 0.3900 0.0686  0.2156  0.0414  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3332 0.2791 0.5159 0.0790  0.2360  0.0988  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3393 0.3007 0.6261 0.0869  0.2666  0.1305  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3360 0.3029 0.6946 0.0940  0.2865  0.1492  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3125 0.3300 0.6574 0.0763  0.2260  0.1506  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.2864 0.2332 0.3125 0.0571  0.1551  0.0506  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2725 0.2156 0.2508 0.0503  0.1260  0.0331  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2364 0.2273 0.2595 0.0444  0.0991  0.0410  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2220 0.2477 0.2893 0.0384  0.0868  0.0557  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.2939 0.2274 0.2257 0.0431  0.1063  0.0202  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2720 0.2442 0.2390 0.0386  0.0943  0.0287  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3098 0.2395 0.2099 0.0361  0.0770  0.0067  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2126 0.1980 0.2195 0.0438  0.0899  0.0327  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1810 0.2003 0.2182 0.0368  0.0676  0.0385  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2074 0.2272 0.2114 0.0291  0.0446  0.0226  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2422 0.2350 0.2091 0.0317  0.0438  0.0093  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1791 0.2225 0.1957 0.0174  0.0263  0.0259  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1672 0.2076 0.1626 0.0100  0.0136  0.0126  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1694 0.2168 0.1721 0.0027  0.0057  0.0145  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1651 0.2239 0.1830 -0.0067 -0.0013 0.0283  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1657 0.2116 0.1553 -0.0006 0.0080  0.0120  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1800 0.2216 0.1644 0.0051  0.0145  0.0120  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1994 0.2235 0.1637 0.0096  0.0144  0.0008  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1764 0.2286 0.1802 0.0051  0.0193  0.0261  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2061 0.2203 0.1584 0.0129  0.0196  0.0012  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1888 0.2341 0.1864 0.0104  0.0285  0.0257  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2024 0.2272 0.1690 0.0140  0.0292  0.0121  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1651 0.2026 0.1580 0.0046  0.0041  0.0030  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1606 0.1998 0.1561 -0.0028 -0.0001 0.0031  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1837 0.2148 0.1641 -0.0180 0.0001  -0.0008 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1763 0.1984 0.1548 -0.0169 0.0061  -0.0107 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1684 0.1976 0.1642 0.0052  0.0002  -0.0067 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1960 0.2236 0.1642 -0.0345 -0.0065 0.0087  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2330 0.2361 0.1688 -0.0536 -0.0021 0.0043  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2446 0.2249 0.1700 -0.0563 0.0139  -0.0089 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2496 0.2332 0.1846 -0.0515 0.0125  -0.0091 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2868 0.2790 0.2000 -0.0763 -0.0196 0.0209  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3741 0.3251 0.2341 -0.1016 -0.0153 0.0171  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3747 0.3204 0.2283 -0.1005 -0.0043 0.0094  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4317 0.3484 0.2497 -0.1246 -0.0217 0.0216  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2449 0.1997 0.1551 -0.0640 0.0327  -0.0188 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2797 0.2064 0.1881 -0.0675 0.0564  -0.0290 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3516 0.2248 0.2029 -0.0935 0.0773  -0.0333 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3905 0.2281 0.2340 -0.0990 0.1067  -0.0421 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2617 0.1977 0.2220 -0.0504 0.0695  -0.0360 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2278 0.1979 0.2243 -0.0311 0.0472  -0.0321 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2628 0.1923 0.2265 -0.0525 0.0799  -0.0385 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3718 0.2324 0.1819 -0.1105 0.0648  -0.0267 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.4324 0.2304 0.1726 -0.1393 0.0822  -0.0306 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.5157 0.2590 0.1931 -0.1640 0.0883  -0.0305 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.5773 0.2517 0.1936 -0.1858 0.1198  -0.0399 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.4445 0.2432 0.1559 -0.1540 0.0569  -0.0192 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.4064 0.2483 0.1685 -0.1327 0.0558  -0.0206 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.4020 0.2437 0.1385 -0.1483 0.0303  -0.0072 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3929 0.2751 0.1602 -0.1435 -0.0050 0.0122  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3948 0.2913 0.1688 -0.1514 -0.0309 0.0298  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.4237 0.2938 0.1622 -0.1680 -0.0306 0.0297  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3572 0.2915 0.1778 -0.1433 -0.0551 0.0492  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.5089 0.2763 0.1986 -0.1613 0.0625  -0.0203 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.5529 0.2685 0.1816 -0.1861 0.0630  -0.0180 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.5622 0.2553 0.2024 -0.1766 0.1043  -0.0338 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.6167 0.2502 0.1945 -0.1993 0.1175  -0.0360 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.5466 0.2981 0.1938 -0.1873 0.0183  0.0023  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.5120 0.3306 0.2431 -0.1520 0.0150  0.0014  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4462 0.3046 0.2307 -0.1261 0.0240  -0.0058 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.5038 0.3291 0.2416 -0.1526 0.0021  0.0087  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.5137 0.2530 0.2359 -0.1445 0.1204  -0.0417 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.5005 0.2292 0.2584 -0.1324 0.1545  -0.0516 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5702 0.2344 0.3029 -0.1443 0.2072  -0.0636 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.5443 0.2226 0.3402 -0.1273 0.2313  -0.0682 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.4327 0.2283 0.2871 -0.0988 0.1436  -0.0505 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3917 0.2437 0.2690 -0.0856 0.0997  -0.0402 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3338 0.2309 0.2839 -0.0587 0.0910  -0.0404 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.4113 0.2578 0.2654 -0.0932 0.0870  -0.0349 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.6619 0.2467 0.2971 -0.1767 0.2255  -0.0671 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.7460 0.2477 0.3326 -0.1946 0.2833  -0.0796 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.7536 0.2453 0.4130 -0.1758 0.3383  -0.0880 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.7681 0.2259 0.4495 -0.1741 0.3873  -0.0952 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.8451 0.2472 0.2913 -0.2393 0.2888  -0.0808 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.8891 0.2949 0.2682 -0.2637 0.2267  -0.0655 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 1.0044 0.2918 0.2337 -0.3150 0.2318  -0.0649 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.8733 0.3205 0.2825 -0.2551 0.2078  -0.0617 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.7256 0.2546 0.4390 -0.1591 0.3281  -0.0845 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.7024 0.2264 0.4969 -0.1415 0.3736  -0.0877 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.6701 0.2521 0.5903 -0.1123 0.3763  -0.0822 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.6636 0.2311 0.6614 -0.1013 0.4208  -0.0814 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.6712 0.2179 0.4840 -0.1341 0.3561  -0.0839 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.6122 0.2462 0.4644 -0.1163 0.2893  -0.0737 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.6265 0.2772 0.4196 -0.1274 0.2424  -0.0677 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.5432 0.2506 0.5021 -0.0863 0.2647  -0.0666 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5773 0.3054 0.4344 -0.1038 0.1989  -0.0595 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.5328 0.2922 0.4818 -0.0801 0.2103  -0.0599 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.5060 0.2337 0.5693 -0.0663 0.2828  -0.0628 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4906 0.3119 0.5111 -0.0566 0.1770  -0.0532 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4647 0.2569 0.6010 -0.0452 0.2401  -0.0532 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4585 0.2920 0.5641 -0.0413 0.1898  -0.0503 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.6462 0.2869 0.5888 -0.1019 0.3313  -0.0764 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.6115 0.2992 0.6613 -0.0792 0.3273  -0.0690 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6875 0.3252 0.7696 -0.0830 0.3891  -0.0724 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.6435 0.3087 0.8377 -0.0651 0.3975  -0.0624 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5722 0.3144 0.6146 -0.0729 0.2738  -0.0641 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.5334 0.3291 0.5712 -0.0636 0.2187  -0.0581 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.5119 0.3481 0.5389 -0.0587 0.1787  -0.0538 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4907 0.3207 0.6147 -0.0441 0.2064  -0.0507 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7990 0.3573 0.7822 -0.1085 0.4317  -0.0845 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.8793 0.3713 0.8710 -0.1164 0.5013  -0.0905 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.9701 0.3850 0.9647 -0.1238 0.5758  -0.0965 144 ASP   A C   
1064 O O   . ASP   A 138 ? 1.0201 0.3658 1.0156 -0.1320 0.6451  -0.1024 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.9719 0.4048 0.8348 -0.1448 0.5074  -0.1012 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 1.0041 0.4988 0.8772 -0.1375 0.4547  -0.0955 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.9709 0.5163 0.9506 -0.1152 0.4510  -0.0874 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 1.0587 0.5486 0.8362 -0.1556 0.4160  -0.0968 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 1.0019 0.4188 0.9897 -0.1228 0.5680  -0.0959 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 1.0605 0.3978 1.0451 -0.1308 0.6425  -0.1019 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 1.0341 0.4205 1.1157 -0.1099 0.6292  -0.0914 145 GLU   A C   
1072 O O   . GLU   A 139 ? 1.0651 0.3918 1.1498 -0.1147 0.6873  -0.0950 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.1910 0.4258 0.9983 -0.1689 0.6652  -0.1176 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.2765 0.5490 1.0054 -0.1785 0.5888  -0.1151 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.4496 0.6533 1.0122 -0.2175 0.5704  -0.1219 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.4948 0.6977 0.9832 -0.2333 0.5252  -0.1184 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.5153 0.6642 1.0250 -0.2338 0.5987  -0.1286 145 GLU   A OE2 
1078 N N1  . A1B3K B .   ? 0.3286 0.1937 0.2461 0.0592  0.1021  -0.0032 201 A1B3K A N1  
1079 C C4  . A1B3K B .   ? 0.7605 0.2554 0.3149 0.0382  0.2655  -0.0256 201 A1B3K A C4  
1080 C C5  . A1B3K B .   ? 0.8648 0.2780 0.3796 0.0420  0.3362  -0.0258 201 A1B3K A C5  
1081 C C6  . A1B3K B .   ? 0.7273 0.2391 0.2883 0.0362  0.2386  -0.0286 201 A1B3K A C6  
1082 C C7  . A1B3K B .   ? 0.6509 0.2352 0.2574 0.0341  0.1829  -0.0275 201 A1B3K A C7  
1083 C C8  . A1B3K B .   ? 0.6256 0.2203 0.2352 0.0313  0.1564  -0.0308 201 A1B3K A C8  
1084 C C10 . A1B3K B .   ? 0.5667 0.1830 0.2010 0.0316  0.1255  -0.0343 201 A1B3K A C10 
1085 C C13 . A1B3K B .   ? 0.3595 0.2243 0.2534 0.0528  0.0838  -0.0087 201 A1B3K A C13 
1086 O O2  . A1B3K B .   ? 0.3370 0.2457 0.2617 0.0490  0.0622  -0.0062 201 A1B3K A O2  
1087 C C12 . A1B3K B .   ? 0.4300 0.2284 0.2492 0.0476  0.0913  -0.0178 201 A1B3K A C12 
1088 S S   . A1B3K B .   ? 0.4880 0.2320 0.2426 0.0371  0.0668  -0.0287 201 A1B3K A S   
1089 C C11 . A1B3K B .   ? 0.5440 0.2000 0.2003 0.0246  0.0724  -0.0350 201 A1B3K A C11 
1090 C C14 . A1B3K B .   ? 0.4592 0.2136 0.2596 0.0539  0.1381  -0.0147 201 A1B3K A C14 
1091 N N   . A1B3K B .   ? 0.5213 0.2037 0.2356 0.0444  0.1427  -0.0241 201 A1B3K A N   
1092 C C9  . A1B3K B .   ? 0.5354 0.2118 0.2454 0.0452  0.1582  -0.0214 201 A1B3K A C9  
1093 O O1  . A1B3K B .   ? 0.4769 0.2057 0.2571 0.0546  0.1711  -0.0102 201 A1B3K A O1  
1094 C C1  . A1B3K B .   ? 0.6094 0.2469 0.2514 0.0332  0.1550  -0.0239 201 A1B3K A C1  
1095 O O   . A1B3K B .   ? 0.5573 0.2528 0.2395 0.0305  0.1097  -0.0236 201 A1B3K A O   
1096 C C   . A1B3K B .   ? 0.5295 0.2710 0.2438 0.0283  0.0849  -0.0209 201 A1B3K A C   
1097 F F2  . A1B3K B .   ? 0.8610 0.2877 0.4401 0.0563  0.3768  -0.0173 201 A1B3K A F2  
1098 F F1  . A1B3K B .   ? 0.9701 0.2728 0.3566 0.0245  0.3455  -0.0392 201 A1B3K A F1  
1099 F F   . A1B3K B .   ? 0.8806 0.3011 0.4214 0.0478  0.3613  -0.0190 201 A1B3K A F   
1100 C C3  . A1B3K B .   ? 0.6995 0.2529 0.2896 0.0371  0.2310  -0.0219 201 A1B3K A C3  
1101 C C2  . A1B3K B .   ? 0.6312 0.2545 0.2643 0.0346  0.1771  -0.0212 201 A1B3K A C2  
# 
