data_7I3G
# 
_entry.id   7I3G 
# 
_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   7I3G         pdb_00007i3g 10.2210/pdb7i3g/pdb 
WWPDB D_1001408267 ?            ?                   
# 
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                        7I3G 
_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 '(1R)-1-(1-methyl-1H-indazol-3-yl)-N-[2-(1,3-oxazol-4-yl)ethyl]prop-2-yn-1-amine' 280.324   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                        65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                              78.133    2   ?         ? ? ? 
5 water       nat water                                                                             18.015    123 ?         ? ? ? 
# 
_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 '(1R)-1-(1-methyl-1H-indazol-3-yl)-N-[2-(1,3-oxazol-4-yl)ethyl]prop-2-yn-1-amine' A1B1O 
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 
A1B1O non-polymer         . '(1R)-1-(1-methyl-1H-indazol-3-yl)-N-[2-(1,3-oxazol-4-yl)ethyl]prop-2-yn-1-amine' ? 'C16 H16 N4 O'   
280.324 
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        A1B1O 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B1O 
_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 A1B1O 1   201 201 A1B1O 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 3   DMS   DMS A . 
F 5 HOH   1   301 137 HOH   HOH A . 
F 5 HOH   2   302 181 HOH   HOH A . 
F 5 HOH   3   303 24  HOH   HOH A . 
F 5 HOH   4   304 4   HOH   HOH A . 
F 5 HOH   5   305 37  HOH   HOH A . 
F 5 HOH   6   306 255 HOH   HOH A . 
F 5 HOH   7   307 77  HOH   HOH A . 
F 5 HOH   8   308 26  HOH   HOH A . 
F 5 HOH   9   309 30  HOH   HOH A . 
F 5 HOH   10  310 28  HOH   HOH A . 
F 5 HOH   11  311 36  HOH   HOH A . 
F 5 HOH   12  312 121 HOH   HOH A . 
F 5 HOH   13  313 25  HOH   HOH A . 
F 5 HOH   14  314 7   HOH   HOH A . 
F 5 HOH   15  315 68  HOH   HOH A . 
F 5 HOH   16  316 253 HOH   HOH A . 
F 5 HOH   17  317 107 HOH   HOH A . 
F 5 HOH   18  318 97  HOH   HOH A . 
F 5 HOH   19  319 59  HOH   HOH A . 
F 5 HOH   20  320 104 HOH   HOH A . 
F 5 HOH   21  321 34  HOH   HOH A . 
F 5 HOH   22  322 263 HOH   HOH A . 
F 5 HOH   23  323 126 HOH   HOH A . 
F 5 HOH   24  324 119 HOH   HOH A . 
F 5 HOH   25  325 19  HOH   HOH A . 
F 5 HOH   26  326 2   HOH   HOH A . 
F 5 HOH   27  327 47  HOH   HOH A . 
F 5 HOH   28  328 33  HOH   HOH A . 
F 5 HOH   29  329 61  HOH   HOH A . 
F 5 HOH   30  330 20  HOH   HOH A . 
F 5 HOH   31  331 42  HOH   HOH A . 
F 5 HOH   32  332 111 HOH   HOH A . 
F 5 HOH   33  333 21  HOH   HOH A . 
F 5 HOH   34  334 186 HOH   HOH A . 
F 5 HOH   35  335 50  HOH   HOH A . 
F 5 HOH   36  336 268 HOH   HOH A . 
F 5 HOH   37  337 133 HOH   HOH A . 
F 5 HOH   38  338 9   HOH   HOH A . 
F 5 HOH   39  339 161 HOH   HOH A . 
F 5 HOH   40  340 169 HOH   HOH A . 
F 5 HOH   41  341 29  HOH   HOH A . 
F 5 HOH   42  342 105 HOH   HOH A . 
F 5 HOH   43  343 40  HOH   HOH A . 
F 5 HOH   44  344 174 HOH   HOH A . 
F 5 HOH   45  345 144 HOH   HOH A . 
F 5 HOH   46  346 146 HOH   HOH A . 
F 5 HOH   47  347 204 HOH   HOH A . 
F 5 HOH   48  348 106 HOH   HOH A . 
F 5 HOH   49  349 257 HOH   HOH A . 
F 5 HOH   50  350 251 HOH   HOH A . 
F 5 HOH   51  351 124 HOH   HOH A . 
F 5 HOH   52  352 95  HOH   HOH A . 
F 5 HOH   53  353 182 HOH   HOH A . 
F 5 HOH   54  354 91  HOH   HOH A . 
F 5 HOH   55  355 252 HOH   HOH A . 
F 5 HOH   56  356 62  HOH   HOH A . 
F 5 HOH   57  357 18  HOH   HOH A . 
F 5 HOH   58  358 12  HOH   HOH A . 
F 5 HOH   59  359 11  HOH   HOH A . 
F 5 HOH   60  360 15  HOH   HOH A . 
F 5 HOH   61  361 80  HOH   HOH A . 
F 5 HOH   62  362 264 HOH   HOH A . 
F 5 HOH   63  363 168 HOH   HOH A . 
F 5 HOH   64  364 265 HOH   HOH A . 
F 5 HOH   65  365 219 HOH   HOH A . 
F 5 HOH   66  366 138 HOH   HOH A . 
F 5 HOH   67  367 89  HOH   HOH A . 
F 5 HOH   68  368 262 HOH   HOH A . 
F 5 HOH   69  369 256 HOH   HOH A . 
F 5 HOH   70  370 76  HOH   HOH A . 
F 5 HOH   71  371 10  HOH   HOH A . 
F 5 HOH   72  372 177 HOH   HOH A . 
F 5 HOH   73  373 156 HOH   HOH A . 
F 5 HOH   74  374 269 HOH   HOH A . 
F 5 HOH   75  375 250 HOH   HOH A . 
F 5 HOH   76  376 96  HOH   HOH A . 
F 5 HOH   77  377 213 HOH   HOH A . 
F 5 HOH   78  378 178 HOH   HOH A . 
F 5 HOH   79  379 38  HOH   HOH A . 
F 5 HOH   80  380 51  HOH   HOH A . 
F 5 HOH   81  381 23  HOH   HOH A . 
F 5 HOH   82  382 98  HOH   HOH A . 
F 5 HOH   83  383 159 HOH   HOH A . 
F 5 HOH   84  384 154 HOH   HOH A . 
F 5 HOH   85  385 123 HOH   HOH A . 
F 5 HOH   86  386 266 HOH   HOH A . 
F 5 HOH   87  387 114 HOH   HOH A . 
F 5 HOH   88  388 233 HOH   HOH A . 
F 5 HOH   89  389 254 HOH   HOH A . 
F 5 HOH   90  390 175 HOH   HOH A . 
F 5 HOH   91  391 248 HOH   HOH A . 
F 5 HOH   92  392 158 HOH   HOH A . 
F 5 HOH   93  393 69  HOH   HOH A . 
F 5 HOH   94  394 78  HOH   HOH A . 
F 5 HOH   95  395 99  HOH   HOH A . 
F 5 HOH   96  396 152 HOH   HOH A . 
F 5 HOH   97  397 245 HOH   HOH A . 
F 5 HOH   98  398 207 HOH   HOH A . 
F 5 HOH   99  399 112 HOH   HOH A . 
F 5 HOH   100 400 65  HOH   HOH A . 
F 5 HOH   101 401 210 HOH   HOH A . 
F 5 HOH   102 402 201 HOH   HOH A . 
F 5 HOH   103 403 117 HOH   HOH A . 
F 5 HOH   104 404 185 HOH   HOH A . 
F 5 HOH   105 405 86  HOH   HOH A . 
F 5 HOH   106 406 240 HOH   HOH A . 
F 5 HOH   107 407 261 HOH   HOH A . 
F 5 HOH   108 408 129 HOH   HOH A . 
F 5 HOH   109 409 267 HOH   HOH A . 
F 5 HOH   110 410 258 HOH   HOH A . 
F 5 HOH   111 411 92  HOH   HOH A . 
F 5 HOH   112 412 230 HOH   HOH A . 
F 5 HOH   113 413 56  HOH   HOH A . 
F 5 HOH   114 414 164 HOH   HOH A . 
F 5 HOH   115 415 260 HOH   HOH A . 
F 5 HOH   116 416 122 HOH   HOH A . 
F 5 HOH   117 417 208 HOH   HOH A . 
F 5 HOH   118 418 223 HOH   HOH A . 
F 5 HOH   119 419 221 HOH   HOH A . 
F 5 HOH   120 420 222 HOH   HOH A . 
F 5 HOH   121 421 241 HOH   HOH A . 
F 5 HOH   122 422 259 HOH   HOH A . 
F 5 HOH   123 423 242 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           7I3G 
_cell.length_a           87.828 
_cell.length_b           57.677 
_cell.length_c           32.727 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.56 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I3G 
_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          7I3G 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.61 
_exptl_crystal.density_percent_sol   52.79 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-09 
_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   0.92199 
_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        0.92199 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I3G 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.18 
_reflns.d_resolution_high            1.62 
_reflns.number_obs                   20808 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.062 
_reflns.pdbx_netI_over_sigmaI        12.0 
_reflns.pdbx_redundancy              6.9 
_reflns.pdbx_Rrim_I_all              0.068 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     143179 
_reflns.pdbx_chi_squared             0.46 
_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                  1.62 
_reflns_shell.d_res_low                   1.65 
_reflns_shell.number_measured_all         7029 
_reflns_shell.number_unique_obs           1044 
_reflns_shell.Rmerge_I_obs                3.268 
_reflns_shell.pdbx_chi_squared            0.10 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        99.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             3.543 
_reflns_shell.pdbx_Rpim_I_all             1.354 
_reflns_shell.pdbx_CC_half                0.399 
_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                                 7I3G 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     19519 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             48.20 
_refine.ls_d_res_high                            1.620 
_refine.ls_percent_reflns_obs                    93.6 
_refine.ls_R_factor_obs                          0.2254 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2235 
_refine.ls_R_factor_R_free                       0.2606 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.080 
_refine.ls_number_reflns_R_free                  991 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.B_iso_mean                               49.15 
_refine.aniso_B[1][1]                            -5.27710 
_refine.aniso_B[2][2]                            3.13990 
_refine.aniso_B[3][3]                            2.13720 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -6.35990 
_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             0.107 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.108 
_refine.pdbx_overall_SU_R_Blow_DPI               0.112 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.111 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I3G 
_refine_analyze.Luzzati_coordinate_error_obs    0.42 
_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         30 
_refine_hist.number_atoms_solvent             124 
_refine_hist.number_atoms_total               1228 
_refine_hist.d_res_high                       1.620 
_refine_hist.d_res_low                        48.20 
# 
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  1140 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.93  ? 2.00  1551 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  375  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  215  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1140 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.83  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.52 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  942  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   50 
_refine_ls_shell.d_res_high                       1.62 
_refine_ls_shell.d_res_low                        1.65 
_refine_ls_shell.number_reflns_R_work             374 
_refine_ls_shell.R_factor_R_work                  0.6286 
_refine_ls_shell.percent_reflns_obs               33.99 
_refine_ls_shell.R_factor_R_free                  0.6000 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.27 
_refine_ls_shell.number_reflns_R_free             25 
_refine_ls_shell.number_reflns_all                399 
_refine_ls_shell.R_factor_all                     0.6269 
# 
_struct.entry_id                  7I3G 
_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-0035396-001 (A71EV2A-x4426)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I3G 
_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 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              7I3G 
_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 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.150 ? ? 
# 
_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_555 110.1 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.7 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 113.9 ? 
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 91.5  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 117.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I3G 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -103.89 40.17  
2 1 SER A 125 ? ? -133.11 -32.45 
# 
_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         15.2155 
_pdbx_refine_tls.origin_y         7.5753 
_pdbx_refine_tls.origin_z         14.0681 
_pdbx_refine_tls.T[1][1]          -0.0757 
_pdbx_refine_tls.T[2][2]          -0.0960 
_pdbx_refine_tls.T[3][3]          0.1388 
_pdbx_refine_tls.T[1][2]          -0.0124 
_pdbx_refine_tls.T[1][3]          0.1309 
_pdbx_refine_tls.T[2][3]          0.0320 
_pdbx_refine_tls.L[1][1]          2.3412 
_pdbx_refine_tls.L[2][2]          3.1145 
_pdbx_refine_tls.L[3][3]          0.4253 
_pdbx_refine_tls.L[1][2]          -0.6130 
_pdbx_refine_tls.L[1][3]          -0.2946 
_pdbx_refine_tls.L[2][3]          0.0299 
_pdbx_refine_tls.S[1][1]          0.0018 
_pdbx_refine_tls.S[1][2]          0.1022 
_pdbx_refine_tls.S[1][3]          0.3651 
_pdbx_refine_tls.S[2][1]          0.0452 
_pdbx_refine_tls.S[2][2]          -0.0114 
_pdbx_refine_tls.S[2][3]          -0.3145 
_pdbx_refine_tls.S[3][1]          -0.0146 
_pdbx_refine_tls.S[3][2]          -0.0632 
_pdbx_refine_tls.S[3][3]          0.0095 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B1O N1   N  Y N 1   
A1B1O N3   N  Y N 2   
A1B1O C4   C  N N 3   
A1B1O C5   C  Y N 4   
A1B1O C6   C  Y N 5   
A1B1O C7   C  Y N 6   
A1B1O C8   C  Y N 7   
A1B1O C10  C  Y N 8   
A1B1O C13  C  Y N 9   
A1B1O C15  C  Y N 10  
A1B1O C    C  N N 11  
A1B1O C1   C  N N 12  
A1B1O C2   C  N R 13  
A1B1O C14  C  Y N 14  
A1B1O C12  C  Y N 15  
A1B1O C11  C  Y N 16  
A1B1O C9   C  N N 17  
A1B1O N2   N  Y N 18  
A1B1O N    N  N N 19  
A1B1O C3   C  N N 20  
A1B1O O    O  Y N 21  
A1B1O H5   H  N N 22  
A1B1O H6   H  N N 23  
A1B1O H7   H  N N 24  
A1B1O H8   H  N N 25  
A1B1O H14  H  N N 26  
A1B1O H1   H  N N 27  
A1B1O H    H  N N 28  
A1B1O H15  H  N N 29  
A1B1O H13  H  N N 30  
A1B1O H12  H  N N 31  
A1B1O H10  H  N N 32  
A1B1O H9   H  N N 33  
A1B1O H11  H  N N 34  
A1B1O H16  H  N N 35  
A1B1O H3   H  N N 36  
A1B1O H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1B1O C1  C    trip N N 1   
A1B1O C2  C1   sing N N 2   
A1B1O N   C2   sing N N 3   
A1B1O C3  N    sing N N 4   
A1B1O C4  C3   sing N N 5   
A1B1O C5  C4   sing N N 6   
A1B1O C5  C6   doub Y N 7   
A1B1O C6  O    sing Y N 8   
A1B1O O   C7   sing Y N 9   
A1B1O C7  N1   doub Y N 10  
A1B1O N1  C5   sing Y N 11  
A1B1O C8  C2   sing N N 12  
A1B1O C8  N2   doub Y N 13  
A1B1O N2  N3   sing Y N 14  
A1B1O C9  N3   sing N N 15  
A1B1O N3  C10  sing Y N 16  
A1B1O C10 C11  doub Y N 17  
A1B1O C11 C12  sing Y N 18  
A1B1O C12 C13  doub Y N 19  
A1B1O C13 C14  sing Y N 20  
A1B1O C14 C15  doub Y N 21  
A1B1O C15 C8   sing Y N 22  
A1B1O C10 C15  sing Y N 23  
A1B1O C4  H5   sing N N 24  
A1B1O C4  H6   sing N N 25  
A1B1O C6  H7   sing N N 26  
A1B1O C7  H8   sing N N 27  
A1B1O C13 H14  sing N N 28  
A1B1O C   H1   sing N N 29  
A1B1O C2  H    sing N N 30  
A1B1O C14 H15  sing N N 31  
A1B1O C12 H13  sing N N 32  
A1B1O C11 H12  sing N N 33  
A1B1O C9  H10  sing N N 34  
A1B1O C9  H9   sing N N 35  
A1B1O C9  H11  sing N N 36  
A1B1O N   H16  sing N N 37  
A1B1O C3  H3   sing N N 38  
A1B1O C3  H4   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_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                    7I3G 
_atom_sites.fract_transf_matrix[1][1]   0.011386 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000509 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017338 
_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]   0.030586 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.202 6.746   24.074 1.00 49.40  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.412 6.839   23.259 1.00 50.18  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.511 5.733   22.209 1.00 49.75  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.789 4.725   22.290 1.00 50.36  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.657 6.906   24.139 1.00 52.65  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.807 5.743   24.933 1.00 57.06  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.352 5.941   21.200 1.00 48.42  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.502 4.959   20.140 1.00 47.62  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.764 5.536   18.765 1.00 46.53  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.393 6.673   18.471 1.00 46.30  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.388 4.719   17.909 1.00 45.49  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.757 5.112   16.570 1.00 45.24  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.752 3.936   15.579 1.00 44.15  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.827 2.764   15.974 1.00 44.18  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.151 5.754   16.611 1.00 45.33  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.651 4.264   14.280 1.00 43.12  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.766 3.309   13.184 1.00 42.75  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.195 3.487   12.605 1.00 44.29  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.683 4.622   12.447 1.00 44.42  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.705 3.551   12.077 1.00 42.35  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.253 3.684   12.630 1.00 41.49  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.795 2.465   11.002 1.00 42.94  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.291 4.281   11.633 1.00 40.98  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.877 2.369   12.311 1.00 45.76  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.222 2.421   11.742 1.00 46.90  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.182 1.689   10.423 1.00 46.60  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.062 0.464   10.423 1.00 45.37  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.236 1.775   12.693 1.00 47.86  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.402 2.578   13.957 1.00 49.80  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.136 3.758   13.962 1.00 51.31  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.781 2.191   15.136 1.00 51.13  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.227 4.545   15.101 1.00 52.67  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.880 2.959   16.288 1.00 52.57  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.619 4.131   16.271 1.00 54.11  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.703 4.919   17.394 1.00 56.31  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.194 2.432   9.303  1.00 46.52  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.140 1.872   7.944  1.00 47.78  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.255 2.452   7.063  1.00 49.93  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.358 3.674   6.925  1.00 50.69  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.743 2.040   7.292  1.00 48.30  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.268 3.509   7.315  1.00 48.12  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.726 1.474   5.879  1.00 48.89  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.125 1.594   6.513  1.00 50.21  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.242 2.050   5.691  1.00 51.46  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.160 2.948   6.497  1.00 52.60  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.453 2.631   7.647  1.00 53.74  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.472 4.124   5.981  1.00 52.52  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.253 5.098   6.727  1.00 52.78  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.328 6.207   7.249  1.00 51.96  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.705 7.376   7.228  1.00 52.34  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.399 5.639   5.878  1.00 55.80  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.420 4.565   5.612  1.00 62.00  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.151 4.140   6.514  1.00 63.93  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.450 4.061   4.382  1.00 63.77  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.110 5.835   7.725  1.00 50.62  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.145 6.795   8.273  1.00 50.41  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.612 6.413   9.655  1.00 49.43  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.456 5.229   9.971  1.00 48.65  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.945 6.985   7.338  1.00 50.71  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.270 7.486   5.952  1.00 52.06  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.898 8.710   5.761  1.00 53.19  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.869 6.780   4.829  1.00 53.56  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.132 9.208   4.483  1.00 54.88  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.082 7.272   3.551  1.00 55.07  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.743 8.474   3.377  1.00 56.47  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 27.999 8.925   2.100  1.00 59.07  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.283 7.434   10.459 1.00 48.65  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.697 7.263   11.786 1.00 47.90  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.428 8.099   11.803 1.00 47.02  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.481 9.316   11.598 1.00 47.11  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.678 7.695   12.897 1.00 48.45  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.037 8.071   14.229 1.00 50.67  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.059 8.255   15.334 1.00 53.91  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.645 9.261   16.313 1.00 54.90  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.129 8.987   17.511 1.00 56.19  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.910 7.727   17.877 1.00 54.11  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.788 9.974   18.334 1.00 56.18  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.292 7.450   12.010 1.00 44.62  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.004 8.128   12.045 1.00 44.41  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.539 8.225   13.485 1.00 44.23  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.384 7.194   14.150 1.00 43.99  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.940 7.405   11.180 1.00 44.43  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.678 8.258   11.046 1.00 44.22  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.499 7.041   9.800  1.00 44.79  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.288 9.456   13.965 1.00 43.07  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.817 9.693   15.328 1.00 43.59  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.603 10.637  15.329 1.00 43.14  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.409 11.377  14.352 1.00 44.26  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.924 10.325  16.234 1.00 45.33  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.853 9.277   16.790 1.00 47.28  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.693 11.448  15.516 1.00 45.82  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.880 10.747  16.474 1.00 41.46  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.880 11.821  16.620 1.00 40.42  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.696 13.173  16.610 1.00 41.17  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.714 13.272  17.286 1.00 41.10  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.166 11.740  17.954 1.00 39.60  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.320 10.484  18.068 1.00 40.13  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.787 9.412   18.513 1.00 40.15  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.077 10.578  17.622 1.00 39.90  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.229 14.176  15.880 1.00 41.73  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.877 15.487  15.798 1.00 42.91  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.018 16.112  17.178 1.00 45.26  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.076 16.656  17.496 1.00 46.28  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.087 16.424  14.879 1.00 42.53  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.863 17.707  14.525 1.00 43.29  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.994 18.572  13.640 1.00 44.48  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.601 19.842  13.213 1.00 47.16  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.532 20.974  13.911 1.00 49.79  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.005 20.981  15.126 1.00 49.33  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.005 22.105  13.402 1.00 50.16  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.980 15.979  18.020 1.00 45.63  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.987 16.553  19.366 1.00 47.24  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.978 15.841  20.324 1.00 49.23  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.241 16.343  21.413 1.00 50.15  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.554 16.648  19.938 1.00 47.72  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.975 15.333  20.393 1.00 49.03  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.332 14.477  19.510 1.00 51.09  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.928 14.793  21.632 1.00 49.72  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.936 13.437  20.234 1.00 51.26  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.254 13.590  21.521 1.00 50.77  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.542 14.708  19.915 1.00 50.14  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.530 13.985  20.721 1.00 50.99  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.932 13.968  20.078 1.00 53.42  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.819 13.281  20.583 1.00 54.11  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.054 12.545  21.049 1.00 49.91  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.738 12.444  21.818 1.00 48.90  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.332 10.974  22.013 1.00 48.17  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.841 13.112  23.170 1.00 48.99  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.132 14.687  18.956 1.00 54.75  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.433 14.730  18.287 1.00 56.51  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.487 15.344  19.197 1.00 57.87  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.180 16.242  19.975 1.00 57.46  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.330 15.536  17.008 1.00 57.06  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.725 14.829  19.118 1.00 59.28  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.855 15.285  19.934 1.00 60.84  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.751 16.284  19.142 1.00 62.78  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.527 16.508  17.945 1.00 62.66  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.670 14.061  20.442 1.00 62.21  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.576 13.622  19.421 1.00 62.72  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.800 12.912  20.964 1.00 62.83  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.784 16.857  19.815 1.00 64.14  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.770 17.777  19.249 1.00 66.35  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.429 17.127  18.011 1.00 66.52  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.497 17.733  16.937 1.00 67.15  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.816 18.082  20.354 1.00 68.80  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 32.938 18.985  19.962 1.00 72.46  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 32.888 20.335  20.231 1.00 74.78  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.136 18.691  19.399 1.00 74.44  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 34.034 20.832  19.797 1.00 76.02  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 34.821 19.880  19.287 1.00 75.97  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.871 15.879  18.163 1.00 66.01  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.498 15.104  17.117 1.00 65.79  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.592 14.928  15.882 1.00 64.43  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.082 15.018  14.757 1.00 64.75  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.888 13.754  17.687 1.00 68.52  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.809 12.974  16.801 1.00 72.86  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.737 13.530  16.187 1.00 74.47  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.571 11.669  16.730 1.00 73.70  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.281 14.689  16.084 1.00 62.32  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.331 14.520  14.982 1.00 60.93  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.171 15.819  14.171 1.00 59.46  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.100 15.759  12.949 1.00 58.44  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.931 14.109  15.497 1.00 61.21  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.830 12.777  16.208 1.00 64.01  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.576 11.852  15.843 1.00 64.22  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.991 12.662  17.123 1.00 66.07  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.008 16.969  14.843 1.00 59.72  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.853 18.247  14.145 1.00 60.58  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.122 18.626  13.347 1.00 61.58  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.018 19.169  12.245 1.00 61.40  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.494 19.372  15.122 1.00 60.67  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.052 19.373  15.522 1.00 60.45  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.527 18.919  16.694 1.00 61.11  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.946 19.808  14.725 1.00 60.28  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.160 19.094  16.699 1.00 61.24  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.774 19.624  15.494 1.00 60.88  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.827 20.331  13.432 1.00 60.79  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.505 19.979  15.024 1.00 60.88  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.569 20.694  12.976 1.00 61.57  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.420 20.472  13.752 1.00 61.11  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.297 18.325  13.897 1.00 62.28  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.558 18.619  13.209 1.00 64.33  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.729 17.704  11.972 1.00 65.34  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.311 18.131  10.967 1.00 67.02  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.727 18.425  14.167 1.00 64.68  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.213 16.460  12.030 1.00 63.96  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.331 15.536  10.891 1.00 63.15  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.967 15.331  10.210 1.00 60.83  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.647 14.214  9.769  1.00 60.17  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.890 14.187  11.343 1.00 65.94  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.291 14.269  11.843 1.00 71.12  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.261 14.250  11.066 1.00 73.57  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.424 14.348  13.161 1.00 72.26  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.188 16.422  10.119 1.00 58.29  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.841 16.472  9.570  1.00 57.09  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.737 16.115  8.094  1.00 56.73  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.454 16.677  7.270  1.00 56.63  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.211 17.860  9.818  1.00 56.15  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.753 18.042  9.381  1.00 55.90  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.829 17.025  10.092 1.00 56.05  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.266 19.471  9.626  1.00 56.61  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.805 15.203  7.763  1.00 55.76  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.536 14.813  6.387  1.00 55.51  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.224 15.492  5.961  1.00 55.08  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.167 16.197  4.948  1.00 56.14  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.453 13.258  6.230  1.00 55.81  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.855 12.870  4.879  1.00 55.89  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.815 12.600  6.429  1.00 56.74  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.192 15.335  6.784  1.00 53.29  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.877 15.851  6.490  1.00 52.03  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.054 15.932  7.779  1.00 49.79  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.271 15.150  8.707  1.00 48.47  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.205 14.906  5.470  1.00 52.14  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.734 15.121  5.259  1.00 52.25  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.142 16.005  4.403  1.00 53.42  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.674 14.397  5.893  1.00 51.83  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.769 15.893  4.488  1.00 53.57  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.457 14.932  5.421  1.00 52.66  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.637 13.373  6.849  1.00 52.06  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.220 14.413  5.803  1.00 52.45  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.402 12.890  7.259  1.00 52.44  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.216 13.418  6.742  1.00 52.09  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.135 16.918  7.846  1.00 49.06  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.237 17.065  8.981  1.00 48.97  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.943 17.740  8.545  1.00 48.77  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.956 18.625  7.659  1.00 49.13  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.905 17.775  10.175 1.00 50.86  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.536 19.129  9.842  1.00 54.98  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.609 20.328  9.824  1.00 60.70  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.989 21.355  9.213  1.00 58.38  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.494 20.237  10.395 1.00 62.07  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.826 17.335  9.163  1.00 47.21  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.508 17.905  8.883  1.00 46.57  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.758 18.065  10.227 1.00 45.50  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.319 17.064  10.820 1.00 45.13  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.759 16.998  7.885  1.00 48.94  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.501 17.555  7.239  1.00 53.80  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.759 18.308  7.917  1.00 52.58  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.233 17.204  6.056  1.00 57.18  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.635 19.322  10.711 1.00 45.01  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.964 19.644  11.966 0.50 44.28  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.963 19.631  11.972 0.50 45.14  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.517 19.142  11.982 1.00 44.94  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.076 18.596  12.989 1.00 44.68  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.002 21.154  12.224 0.50 43.35  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.006 21.134  12.263 0.50 46.66  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.423 21.476  13.475 0.50 41.59  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.304 21.859  11.268 0.50 49.04  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.782 19.315  10.856 1.00 44.86  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.392 18.865  10.757 1.00 44.78  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.248 17.338  10.844 1.00 43.95  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.170 16.878  11.149 1.00 44.07  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.725 19.388  9.487  1.00 47.90  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.143 18.683  8.330  1.00 52.47  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.320 16.574  10.576 1.00 43.11  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.308 15.118  10.677 1.00 43.13  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.917 14.597  11.986 1.00 43.04  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.799 13.390  12.255 1.00 42.54  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.079 14.478  9.507  1.00 44.38  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.416 14.679  8.167  1.00 45.17  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.220 14.048  7.074  1.00 45.22  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.202 12.588  7.119  1.00 43.36  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.224 11.810  6.039  1.00 44.62  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.278 12.349  4.821  1.00 43.92  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.208 10.492  6.165  1.00 44.47  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.628 15.473  12.746 1.00 41.99  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.370 15.136  13.962 1.00 41.69  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.488 14.122  13.598 1.00 41.40  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.745 13.186  14.380 1.00 41.21  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.463 14.585  15.092 1.00 42.91  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.191 14.317  16.411 1.00 43.15  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.082 15.124  16.782 1.00 42.15  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.900 13.290  17.047 1.00 44.20  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.120 14.272  12.384 1.00 40.78  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.191 13.347  11.963 1.00 41.33  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.492 14.105  11.703 1.00 42.91  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.480 15.251  11.216 1.00 41.66  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.834 12.525  10.689 1.00 41.01  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.743 11.415  10.838 1.00 42.19  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.561 10.647  9.540  1.00 42.20  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.098 10.446  11.935 1.00 41.82  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.612 13.425  12.007 1.00 44.03  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.965 13.917  11.744 1.00 45.08  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.812 12.708  11.357 1.00 46.28  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.729 11.647  11.992 1.00 45.52  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.579 14.620  12.974 1.00 45.05  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.924 15.352  12.744 1.00 47.17  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.935 16.697  13.427 1.00 46.98  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.099 14.501  13.202 1.00 48.94  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.643 12.872  10.317 1.00 47.00  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.543 11.838  9.856  1.00 47.95  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.946 12.434  9.908  1.00 50.19  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.177 13.553  9.444  1.00 49.19  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.176 11.290  8.441  1.00 48.20  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.192 10.236  7.966  1.00 48.69  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.755 10.709  8.414  1.00 47.87  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.873 11.701  10.514 1.00 51.78  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.269 12.114  10.593 1.00 53.50  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.140 10.978  10.048 1.00 54.50  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.727 9.814   10.077 1.00 53.54  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.651 12.460  12.030 1.00 54.89  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.474 11.348  12.894 1.00 56.27  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.343 11.317  9.500  1.00 54.73  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.269 10.310  8.935  1.00 56.20  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.013 9.552   10.026 1.00 57.91  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.220 10.088  11.109 1.00 59.44  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.300 10.974  8.023  1.00 57.79  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.815 12.115  8.684  1.00 59.88  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.453 8.328   9.735  1.00 58.03  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.180 7.491   10.694 1.00 58.93  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.467 6.957   10.066 1.00 61.37  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.542 6.824   8.842  1.00 61.19  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.303 6.284   11.157 1.00 58.74  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.146 5.357   10.081 1.00 58.64  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.939 6.708   11.728 1.00 58.19  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.436 6.557   10.899 1.00 63.53  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.690 6.015   10.381 1.00 66.02  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.574 4.517   10.082 1.00 66.53  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.235 4.024   9.166  1.00 67.75  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.886 6.376   11.291 1.00 69.41  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.861 5.585   12.481 1.00 71.90  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.922 7.844   11.647 1.00 70.15  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.746 3.789   10.842 1.00 65.47  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.554 2.359   10.607 1.00 64.85  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.210 2.080   9.933  1.00 63.37  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.247 2.825   10.116 1.00 62.57  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.655 1.576   11.915 1.00 65.17  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.151 0.985   9.169  1.00 62.13  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.952 0.582   8.456  1.00 61.32  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.904 -0.042  9.413  1.00 58.99  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.258 -0.803  10.305 1.00 58.70  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.342 -0.360  7.297  1.00 64.40  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.196 -1.184  6.704  1.00 71.33  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 31.885 -0.851  5.262  1.00 77.86  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.493 0.043   4.648  1.00 79.01  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 30.915 -1.575  4.695  1.00 79.11  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.642 0.357   9.241  1.00 57.14  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.496 -0.126  10.007 1.00 55.66  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.857 -1.340  9.364  1.00 53.74  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.113 -1.637  8.190  1.00 53.83  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.031 -2.070  10.128 1.00 52.16  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.448 -3.314  9.639  1.00 51.39  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.938 -3.363  9.573  1.00 49.61  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.392 -4.436  9.280  1.00 49.76  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.979 -4.473  10.468 1.00 52.87  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.774 -4.602  10.422 1.00 57.90  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.258 -2.253  9.895  1.00 47.48  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.812 -2.232  9.840  1.00 47.13  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.389 -2.172  8.366  1.00 47.36  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.036 -1.510  7.545  1.00 47.92  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.259 -1.010  10.647 1.00 47.32  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.438 -1.191  12.157 1.00 50.18  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.318 -2.334  12.631 1.00 52.42  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.680 -0.179  12.864 1.00 49.14  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.336 -2.907  8.029  1.00 46.97  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.744 -2.868  6.704  1.00 47.67  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.475 -1.992  6.816  1.00 46.70  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.652 -2.256  7.685  1.00 45.96  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.378 -4.289  6.252  1.00 50.61  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.573 -4.974  5.864  1.00 51.92  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.394 -4.303  5.072  1.00 51.62  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.316 -0.987  5.945  1.00 46.21  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.116 -0.152  5.931  1.00 46.22  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.056 -0.885  5.106  1.00 44.61  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.366 -1.394  4.010  1.00 44.38  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.375 1.270   5.355  1.00 47.65  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.527 1.999   6.086  1.00 49.22  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.099 2.120   5.360  1.00 48.16  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.370 2.080   7.621  1.00 50.34  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.809 -0.937  5.616  1.00 41.94  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.723 -1.579  4.894  1.00 40.35  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.373 -0.722  3.662  1.00 38.99  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.381 0.497   3.732  1.00 38.52  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.493 -1.749  5.807  1.00 40.03  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.032 -1.350  2.550  1.00 38.82  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.552 -0.642  1.353  1.00 39.54  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.217 -1.337  1.028  1.00 40.60  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.160 -2.282  0.223  1.00 41.68  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.562 -0.680  0.179  1.00 42.02  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.914 -0.103  0.543  1.00 43.93  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.910 1.342   1.042  1.00 46.98  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.269 1.759   1.397  1.00 51.03  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.583 2.925   1.952  1.00 52.33  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.641 3.823   2.205  1.00 51.06  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.841 3.205   2.252  1.00 52.79  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.150 -0.825  1.641  1.00 39.77  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.838 -1.454  1.604  1.00 39.32  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.735  -0.458  1.998  1.00 40.19  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.023 0.674   2.383  1.00 39.51  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.878 -2.606  2.605  1.00 37.70  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.025 -2.052  4.336  1.00 39.86  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.469  -0.924  1.987  1.00 41.52  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.357  -0.156  2.536  1.00 42.47  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.628  -0.960  3.656  1.00 43.33  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.425  -0.782  3.853  1.00 43.42  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.384  0.369   1.480  1.00 44.77  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.494  -0.673  0.863  1.00 52.30  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.878  -1.865  0.875  1.00 52.49  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.411  -0.297  0.354  1.00 56.44  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.382  -1.812  4.399  1.00 42.44  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.884  -2.572  5.560  1.00 41.13  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.185  -1.616  6.569  1.00 39.90  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.615  -0.466  6.766  1.00 38.84  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.038  -3.296  6.250  1.00 40.86  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.550  -4.838  5.455  1.00 41.84  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.118  -2.108  7.189  1.00 38.56  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.430  -1.375  8.239  1.00 38.99  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.390  -2.217  9.560  1.00 39.06  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.611  -1.900  10.442 1.00 37.63  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.026  -0.974  7.787  1.00 41.24  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.005  0.285   6.937  1.00 44.85  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.580  0.785   6.744  1.00 47.55  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.982  0.606   5.674  1.00 47.88  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.004  1.440   7.766  1.00 46.38  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.188  -3.327  9.637  1.00 38.91  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.332  -4.173  10.819 1.00 38.89  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.815  -4.373  11.033 1.00 37.96  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.624  -4.440  10.082 1.00 38.52  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.522  -5.489  10.762 1.00 39.94  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.045  -6.280  9.721  1.00 43.28  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.045  -5.256  10.534 1.00 39.95  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.173  -4.368  12.303 1.00 36.51  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.562  -4.453  12.731 1.00 36.25  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.669  -4.662  14.229 1.00 36.69  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.679  -5.006  14.881 1.00 37.07  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.862  -4.482  14.770 1.00 36.05  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.188 -4.653  16.181 1.00 37.01  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.079 -3.508  16.606 1.00 36.31  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.036 -3.217  15.903 1.00 36.90  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.936 -6.011  16.413 1.00 38.74  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.432 -6.124  17.857 1.00 39.84  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.029 -7.190  16.079 1.00 37.98  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.741 -2.809  17.715 1.00 35.61  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.608 -1.728  18.183 1.00 35.13  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.188 -2.032  19.549 1.00 35.61  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.585 -2.757  20.318 1.00 35.84  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.903 -0.332  18.165 1.00 35.72  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.980  -0.058  19.345 1.00 36.88  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.722  -0.642  19.420 1.00 38.20  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.340 0.832   20.350 1.00 37.92  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.834  -0.320  20.445 1.00 39.86  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.469  1.135   21.405 1.00 39.42  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.218  0.544   21.454 1.00 40.50  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.326  0.784   22.484 1.00 43.25  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.324 -1.434  19.867 1.00 36.33  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.940 -1.612  21.166 1.00 36.17  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.530 -0.433  22.076 1.00 36.12  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.766 0.722   21.742 1.00 36.32  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.477 -1.675  21.044 1.00 35.14  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.117 -1.850  22.398 1.00 36.20  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.782 -2.926  23.217 1.00 38.17  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.987 -0.899  22.901 1.00 37.78  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.301 -3.043  24.507 1.00 39.10  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.469 -0.976  24.204 1.00 39.08  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.175 -2.082  24.980 1.00 40.54  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.698 -2.172  26.247 1.00 43.71  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.996 -0.748  23.253 1.00 36.17  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.566 0.237   24.244 1.00 36.65  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.495 0.121   25.450 1.00 37.57  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.317 -0.802  26.240 1.00 38.90  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.108 -0.031  24.630 1.00 38.72  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.505 0.970   26.019 1.00 40.12  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.499 1.022   25.599 1.00 37.00  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.444 0.903   26.722 1.00 37.88  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.834 1.114   28.128 1.00 37.49  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.326 0.522   29.087 1.00 37.66  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.630 1.848   26.551 1.00 39.61  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.175 3.180   26.544 1.00 44.26  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.746 1.933   28.240 1.00 37.05  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.026 2.193   29.485 1.00 37.85  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.282 0.924   30.033 1.00 39.09  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.771 0.940   31.165 1.00 40.30  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.088 3.389   29.335 1.00 38.32  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.975 3.124   28.499 1.00 39.67  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.237 -0.150  29.236 1.00 38.57  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.665 -1.435  29.588 1.00 39.61  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.647 -2.597  29.392 1.00 40.23  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.287 -3.723  29.722 1.00 40.71  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.433 -1.696  28.725 1.00 41.08  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.268  -0.756  29.031 1.00 42.56  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.606  -1.095  30.364 1.00 44.28  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.483  -0.194  30.640 1.00 46.86  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.600  0.981   31.250 1.00 48.32  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.786  1.403   31.680 1.00 48.83  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.538  1.762   31.406 1.00 47.84  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.863 -2.351  28.821 1.00 40.86  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.865 -3.367  28.417 1.00 42.18  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.161 -4.469  27.596 1.00 41.48  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.314 -5.660  27.861 1.00 41.56  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.605 -3.970  29.626 1.00 44.93  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.537 -2.989  30.324 1.00 48.89  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.154 -3.633  31.560 1.00 51.98  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.932 -2.667  32.338 1.00 53.76  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.837 -2.506  33.655 1.00 53.36  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.969 -3.228  34.359 1.00 53.59  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.572 -1.590  34.271 1.00 50.97  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.299 -4.054  26.671 1.00 40.32  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.469 -4.991  25.920 1.00 40.39  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.324 -4.551  24.471 1.00 39.88  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.341 -3.355  24.199 1.00 40.52  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.066 -5.037  26.580 1.00 42.34  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.256 -6.268  26.208 1.00 49.23  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.185  -6.597  27.247 1.00 55.58  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 8.116  -7.517  26.692 1.00 61.24  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 8.701  -8.743  26.066 1.00 64.33  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.170 -5.534  23.551 1.00 39.56  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.968 -5.363  22.103 1.00 39.52  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.504 -5.685  21.884 1.00 40.68  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.050 -6.784  22.287 1.00 42.03  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.830 -6.363  21.285 1.00 39.14  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.303 -6.107  21.407 1.00 39.98  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.017 -5.455  20.413 1.00 41.45  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.140 -6.389  22.434 1.00 40.74  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.251 -5.340  20.876 1.00 41.36  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.369 -5.891  22.089 1.00 41.72  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.744  -4.731  21.317 1.00 39.51  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.316  -4.930  21.110 1.00 39.60  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.942  -5.025  19.624 1.00 39.33  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.309  -4.137  18.857 1.00 38.64  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.544  -3.721  21.680 1.00 39.87  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.579  -3.614  23.184 1.00 41.42  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.772  -4.428  23.979 1.00 43.54  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.330  -2.632  23.810 1.00 42.57  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.779  -4.315  25.366 1.00 45.26  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.323  -2.486  25.192 1.00 44.32  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.540  -3.324  25.968 1.00 46.46  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.532  -3.168  27.339 1.00 48.57  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.088  -6.001  19.259 1.00 39.44  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.591  -6.063  17.868 1.00 39.98  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.485  -5.011  17.705 1.00 40.39  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.591  -4.932  18.565 1.00 41.14  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.991  -7.484  17.754 1.00 41.17  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.739  -7.922  19.147 1.00 42.21  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.563  -7.099  20.098 1.00 39.94  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.529  -4.214  16.630 1.00 39.03  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.553  -3.147  16.424 1.00 39.04  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.121  -3.034  14.961 1.00 38.47  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.820  -3.500  14.031 1.00 37.64  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.159  -1.781  16.866 1.00 40.71  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.157  -1.643  18.385 1.00 42.15  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.545  -1.526  16.250 1.00 40.65  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.940  -2.435  14.772 1.00 37.39  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.474  -1.976  13.478 1.00 38.47  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.765  -0.447  13.517 1.00 39.16  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.553  0.196   14.565 1.00 40.15  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.976  -2.192  13.299 1.00 41.92  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.636  -3.563  13.409 1.00 47.10  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.141  0.144   12.395 1.00 37.76  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.429  1.588   12.353 1.00 36.45  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.909  2.242   11.075 1.00 37.60  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.757  1.567   10.044 1.00 38.38  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.932  1.896   12.588 1.00 36.66  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.875  1.106   11.702 1.00 36.82  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.288  -0.167  12.063 1.00 36.42  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.350  1.642   10.506 1.00 37.62  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.178  -0.886  11.260 1.00 37.54  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.239  0.914   9.697  1.00 37.94  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.628  -0.348  10.065 1.00 36.37  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.561  3.531   11.155 1.00 37.74  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.043  4.229   10.000 1.00 39.55  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.204  4.562   9.006  1.00 40.41  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.377  4.483   9.359  1.00 40.36  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.331  5.508   10.447 1.00 41.03  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.218  6.320   11.200 1.00 43.08  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.866  4.859   7.749  1.00 41.44  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.845  5.234   6.730  1.00 42.05  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.445  6.624   7.028  1.00 41.70  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.754  7.457   7.620  1.00 41.58  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.173  5.182   5.329  1.00 44.22  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.951  3.726   4.872  1.00 48.66  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.442  3.589   3.454  1.00 53.60  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.577  2.144   3.016  1.00 57.93  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.857  1.878   1.746  1.00 61.04  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.724  6.878   6.675  1.00 41.75  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.340  8.207   6.962  1.00 42.02  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.483  9.408   6.529  1.00 42.81  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.042  9.486   5.378  1.00 43.00  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.688  8.141   6.226  1.00 42.86  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.990  6.676   6.171  1.00 43.53  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.670  5.976   5.994  1.00 41.45  ? 79  PRO   A CD  1 
ATOM   581  N  N   A SER   A 1 74  ? 5.226  10.329  7.458  0.50 42.96  ? 80  SER   A N   1 
ATOM   582  N  N   B SER   A 1 74  ? 5.205  10.320  7.468  0.50 43.06  ? 80  SER   A N   1 
ATOM   583  C  CA  A SER   A 1 74  ? 4.338  11.465  7.198  0.50 44.23  ? 80  SER   A CA  1 
ATOM   584  C  CA  B SER   A 1 74  ? 4.326  11.464  7.222  0.50 44.40  ? 80  SER   A CA  1 
ATOM   585  C  C   A SER   A 1 74  ? 4.818  12.763  7.891  0.50 45.01  ? 80  SER   A C   1 
ATOM   586  C  C   B SER   A 1 74  ? 4.739  12.739  7.990  0.50 45.12  ? 80  SER   A C   1 
ATOM   587  O  O   A SER   A 1 74  ? 5.815  12.749  8.612  0.50 44.96  ? 80  SER   A O   1 
ATOM   588  O  O   B SER   A 1 74  ? 5.607  12.683  8.863  0.50 45.12  ? 80  SER   A O   1 
ATOM   589  C  CB  A SER   A 1 74  ? 2.922  11.136  7.684  0.50 45.94  ? 80  SER   A CB  1 
ATOM   590  C  CB  B SER   A 1 74  ? 2.892  11.092  7.590  0.50 46.32  ? 80  SER   A CB  1 
ATOM   591  O  OG  A SER   A 1 74  ? 2.566  9.763   7.615  0.50 49.05  ? 80  SER   A OG  1 
ATOM   592  O  OG  B SER   A 1 74  ? 2.376  10.076  6.746  0.50 49.74  ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 4.091  13.881  7.673  1.00 45.52  ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 4.349  15.172  8.309  1.00 47.20  ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 3.334  15.243  9.456  1.00 47.74  ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 2.126  15.234  9.227  1.00 48.28  ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 4.113  16.313  7.306  1.00 47.89  ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 4.426  17.718  7.791  1.00 50.24  ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.898  17.871  8.080  1.00 50.55  ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.985  18.752  6.762  1.00 50.89  ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.826  15.177  10.695 1.00 47.58  ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.993  15.086  11.883 1.00 48.10  ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 3.298  16.209  12.867 1.00 48.64  ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.465  16.453  13.172 1.00 46.88  ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.255  13.699  12.559 1.00 49.10  ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.874  12.534  11.635 1.00 50.50  ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.581  13.597  13.922 1.00 49.92  ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 3.206  11.169  12.178 1.00 51.64  ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 2.241  16.861  13.401 1.00 49.63  ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.437  17.880  14.421 1.00 50.85  ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.900  17.198  15.715 1.00 50.37  ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 2.275  16.249  16.186 1.00 51.45  ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 1.159  18.691  14.678 1.00 51.51  ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 1.460  19.945  15.464 1.00 53.31  ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 2.183  20.983  14.894 1.00 54.53  ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 1.096  20.053  16.794 1.00 54.48  ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 2.471  22.132  15.622 1.00 55.64  ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 1.399  21.196  17.523 1.00 55.32  ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 2.068  22.232  16.930 1.00 55.37  ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 4.035  17.639  16.243 1.00 49.02  ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 4.615  17.091  17.457 1.00 48.78  ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 4.660  18.222  18.474 1.00 49.94  ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 5.113  19.328  18.157 1.00 50.16  ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 6.043  16.508  17.195 1.00 48.01  ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 6.651  15.939  18.472 1.00 48.47  ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 6.013  15.447  16.109 1.00 47.65  ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 4.250  17.928  19.708 1.00 50.61  ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 4.258  18.912  20.782 1.00 51.95  ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 5.672  19.351  21.139 1.00 51.98  ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 6.651  18.645  20.840 1.00 51.55  ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 3.532  18.360  22.028 1.00 55.36  ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 2.028  18.287  21.856 1.00 62.76  ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.370  19.617  21.531 1.00 71.44  ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 0.667  19.702  20.497 1.00 73.18  ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? 1.564  20.582  22.306 1.00 73.61  ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 5.774  20.513  21.805 1.00 51.75  ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 7.056  21.054  22.236 1.00 52.49  ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 7.763  20.105  23.212 1.00 53.26  ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 7.123  19.366  23.964 1.00 53.83  ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 6.858  22.429  22.888 1.00 52.17  ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 9.075  20.094  23.149 1.00 53.37  ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 9.950  19.348  24.051 1.00 54.65  ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 11.063 20.330  24.507 1.00 55.98  ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 11.043 21.510  24.107 1.00 56.32  ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 10.551 18.134  23.334 1.00 55.75  ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 11.685 18.465  22.548 1.00 57.76  ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 12.047 19.856  25.306 1.00 56.49  ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 13.172 20.724  25.666 1.00 57.52  ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 14.111 20.954  24.454 1.00 57.42  ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 14.876 21.912  24.454 1.00 57.52  ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 13.958 20.189  26.883 1.00 61.21  ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 14.478 18.764  26.731 1.00 68.44  ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 15.646 18.403  27.636 1.00 77.00  ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 16.678 19.116  27.602 1.00 78.74  ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 15.534 17.396  28.374 1.00 79.04  ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 14.042 20.079  23.419 1.00 56.65  ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 14.892 20.118  22.228 1.00 55.91  ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 14.319 20.906  21.038 1.00 55.40  ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 15.085 21.491  20.280 1.00 56.02  ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 15.200 18.692  21.800 1.00 55.93  ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 15.888 17.893  22.882 1.00 56.42  ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 15.183 16.970  23.651 1.00 56.94  ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 17.237 18.074  23.156 1.00 57.19  ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 15.814 16.226  24.642 1.00 57.69  ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 17.879 17.336  24.143 1.00 58.24  ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 17.164 16.410  24.884 1.00 59.06  ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 17.807 15.676  25.854 1.00 60.86  ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 12.991 20.905  20.848 1.00 54.09  ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 12.372 21.634  19.736 1.00 53.34  ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 11.098 22.296  20.206 1.00 54.70  ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 10.382 21.701  21.026 1.00 55.45  ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 11.954 20.676  18.591 1.00 51.53  ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 13.067 19.872  17.971 1.00 49.81  ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 13.998 20.467  17.129 1.00 49.64  ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 13.166 18.504  18.189 1.00 49.43  ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 15.018 19.727  16.549 1.00 49.45  ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 14.171 17.755  17.606 1.00 49.40  ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 15.111 18.373  16.806 1.00 49.72  ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 16.123 17.648  16.254 1.00 49.44  ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 10.692 23.440  19.601 1.00 54.39  ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 9.349  23.966  19.905 1.00 54.15  ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 8.276  23.076  19.242 1.00 53.74  ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 8.613  22.106  18.529 1.00 54.29  ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 9.378  25.384  19.311 1.00 55.20  ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 10.382 25.323  18.201 1.00 55.64  ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 11.376 24.231  18.550 1.00 54.31  ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 6.979  23.377  19.458 1.00 53.18  ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 5.902  22.581  18.846 1.00 52.94  ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.969  22.814  17.341 1.00 51.84  ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 6.116  23.967  16.907 1.00 52.11  ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 4.544  22.999  19.400 1.00 53.77  ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 6.023  21.728  16.555 1.00 50.22  ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 6.240  21.881  15.117 1.00 49.74  ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.793  20.654  14.302 1.00 50.12  ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 5.526  19.593  14.869 1.00 50.46  ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.753  22.190  14.873 1.00 50.12  ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 8.646  20.944  14.655 1.00 51.77  ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.973  20.942  15.393 1.00 51.90  ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.917 19.918  14.917 1.00 50.16  ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.847 18.614  15.200 1.00 50.03  ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.821  18.131  15.904 1.00 45.41  ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.789 17.777  14.757 1.00 47.02  ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.776  20.785  12.966 1.00 49.75  ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.498  19.655  12.102 1.00 50.25  ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.812  18.896  11.863 1.00 48.85  ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.766  19.461  11.309 1.00 49.60  ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.888  20.117  10.776 1.00 51.49  ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 3.444  20.516  10.939 1.00 53.65  ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 2.449  19.556  11.074 1.00 54.86  ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 3.080  21.852  11.036 1.00 55.01  ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 1.123  19.917  11.253 1.00 56.37  ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.757  22.227  11.203 1.00 56.40  ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.781  21.255  11.321 1.00 57.73  ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.517 21.640  11.498 1.00 59.93  ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.888  17.652  12.357 1.00 46.75  ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 8.068  16.817  12.154 1.00 45.43  ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.773  15.954  10.919 1.00 43.86  ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.692  15.362  10.817 1.00 43.44  ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.400  15.931  13.386 1.00 46.14  ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.614  15.005  13.117 1.00 45.94  ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 10.354 14.508  14.348 1.00 46.96  ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 10.422 15.189  15.371 1.00 46.58  ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.988 13.336  14.257 1.00 46.07  ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.702  15.930  9.964  1.00 42.76  ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.494  15.189  8.720  1.00 42.70  ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 9.124  13.777  8.750  1.00 42.25  ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.971  13.496  9.607  1.00 42.63  ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 9.014  16.001  7.534  1.00 43.73  ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 10.430 16.086  7.577  1.00 43.95  ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.716  12.903  7.806  1.00 41.64  ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 9.213  11.519  7.652  1.00 41.60  ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 9.057  10.724  8.979  1.00 41.41  ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.944  9.970   9.374  1.00 42.20  ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.664 11.518  7.141  1.00 43.02  ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 10.836 12.226  5.825  1.00 45.20  ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 10.878 11.528  4.632  1.00 47.36  ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 10.910 13.551  5.555  1.00 46.27  ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 11.014 12.442  3.683  1.00 48.13  ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 11.031 13.674  4.189  1.00 47.48  ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.945  10.939  9.667  1.00 40.17  ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.709  10.324  10.959 1.00 39.99  ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.627  9.244   10.875 1.00 39.74  ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.569  9.444   10.263 1.00 40.34  ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 7.333  11.412  11.992 1.00 41.06  ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 7.150  10.967  13.458 1.00 41.94  ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.482  10.775  14.111 1.00 42.08  ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.323  11.986  14.255 1.00 43.30  ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.872  8.145   11.574 1.00 37.35  ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.973  6.995   11.636 1.00 35.93  ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.569  6.789   13.084 1.00 37.59  ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 6.447  6.843   13.952 1.00 38.60  ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.727  5.741   11.148 1.00 35.54  ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 7.364  5.920   9.760  1.00 36.54  ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 8.391  4.522   9.305  1.00 40.71  ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.838  4.867   10.264 1.00 38.75  ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 4.263  6.530   13.355 1.00 36.49  ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.801  6.309   14.724 1.00 37.00  ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 3.373  4.863   14.959 1.00 36.04  ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.827  4.214   14.058 1.00 35.11  ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 2.551  7.209   15.024 1.00 37.96  ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.788  8.717   14.946 1.00 41.28  ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 1.543  9.470   15.366 1.00 42.85  ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.957  9.140   15.800 1.00 42.01  ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 3.549  4.384   16.199 1.00 35.56  ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 3.047  3.051   16.642 1.00 35.95  ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 2.462  3.186   18.058 1.00 37.04  ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 2.816  4.109   18.791 1.00 37.28  ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 4.188  2.030   16.665 1.00 34.21  ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 1.533  2.292   18.424 1.00 37.56  ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 1.039  2.246   19.777 1.00 38.79  ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 2.103  1.483   20.558 1.00 40.75  ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 2.394  0.300   20.274 1.00 41.11  ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -0.346 1.569   19.873 1.00 39.38  ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -0.771 1.423   21.332 1.00 40.90  ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -1.388 2.367   19.094 1.00 39.46  ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 2.691  2.157   21.521 1.00 42.04  ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 3.719  1.545   22.349 1.00 43.79  ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 4.298  2.484   23.383 1.00 44.57  ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 4.071  3.700   23.323 1.00 44.65  ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 5.078  1.925   24.325 1.00 43.98  ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 5.686  2.749   25.361 1.00 44.47  ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 6.988  3.370   24.890 1.00 43.57  ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 7.764  2.737   24.180 1.00 43.46  ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 5.923  1.946   26.669 1.00 45.45  ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 6.590  2.751   27.752 1.00 47.47  ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 5.932  3.793   28.399 1.00 48.47  ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 7.858  2.688   28.213 1.00 48.67  ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 6.814  4.310   29.237 1.00 48.69  ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 7.988  3.684   29.153 1.00 49.07  ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 7.234  4.606   25.323 1.00 42.62  ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 8.479  5.322   25.045 1.00 42.78  ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 8.640  6.518   25.975 1.00 44.05  ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 7.645  7.112   26.402 1.00 44.53  ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 8.565  5.763   23.593 1.00 43.04  ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 7.629  6.764   23.250 1.00 44.01  ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 9.888  6.804   26.334 1.00 43.97  ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 10.314 7.904   27.189 1.00 45.09  ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 11.467 8.654   26.501 1.00 45.98  ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 12.130 8.095   25.620 1.00 46.67  ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 10.746 7.358   28.561 1.00 47.21  ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 9.630  6.619   29.272 1.00 51.47  ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 9.986  6.003   30.612 1.00 55.92  ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 10.796 6.611   31.344 1.00 59.06  ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 9.443  4.926   30.943 1.00 53.73  ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 11.752 9.912   26.873 1.00 46.24  ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 12.842 10.654  26.192 1.00 45.87  ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 14.153 9.873   25.910 1.00 44.89  ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 14.650 9.838   24.765 1.00 44.09  ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 13.069 11.851  27.121 1.00 46.97  ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 11.723 12.114  27.721 1.00 47.61  ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 11.053 10.760  27.868 1.00 46.20  ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 14.684 9.230   26.947 1.00 43.44  ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 15.899 8.438   26.875 1.00 41.99  ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 15.832 7.241   25.942 1.00 40.73  ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 16.855 6.625   25.685 1.00 40.51  ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 14.627 6.857   25.464 1.00 39.60  ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 14.482 5.796   24.470 1.00 39.19  ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 14.866 6.252   23.041 1.00 37.32  ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 15.057 5.394   22.175 1.00 35.64  ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 13.070 5.203   24.448 1.00 39.35  ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 12.757 4.485   25.724 1.00 41.13  ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 13.639 3.778   26.225 1.00 39.74  ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 11.622 4.613   26.210 1.00 41.47  ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 15.031 7.571   22.790 1.00 36.50  ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 15.438 8.033   21.441 1.00 36.21  ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 16.717 7.333   20.961 1.00 36.52  ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 17.579 7.038   21.780 1.00 37.46  ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 15.563 9.547   21.375 1.00 36.99  ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 13.982 10.399  21.561 1.00 39.85  ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 16.763 6.948   19.693 1.00 35.14  ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 17.909 6.199   19.177 1.00 36.76  ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 17.703 4.698   19.152 1.00 37.53  ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 18.534 3.972   18.555 1.00 38.76  ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 16.605 4.213   19.790 1.00 36.65  ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 16.262 2.800   19.780 1.00 36.60  ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 15.876 2.439   18.353 1.00 36.86  ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 15.193 3.222   17.687 1.00 37.90  ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 16.378 1.331   17.844 1.00 35.66  ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 16.131 0.961   16.454 1.00 35.94  ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 14.792 0.282   16.243 1.00 35.45  ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 14.377 -0.543  17.048 1.00 35.53  ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 17.336 0.098   15.932 1.00 37.58  ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 18.512 1.023   15.502 1.00 39.43  ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 16.946 -0.835  14.780 1.00 37.97  ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 19.779 0.313   15.322 1.00 41.09  ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 14.153 0.596   15.108 1.00 34.68  ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 12.953 -0.075  14.648 1.00 35.55  ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.448 -0.899  13.420 1.00 36.72  ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 14.021 -0.318  12.498 1.00 35.67  ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 11.893 0.933   14.185 1.00 35.42  ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.712 0.308   13.392 1.00 36.57  ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 9.879  -0.649  14.286 1.00 37.13  ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 9.800  1.440   12.825 1.00 38.14  ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 13.191 -2.206  13.403 1.00 37.34  ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.660 -3.073  12.319 1.00 39.04  ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.578 -3.979  11.764 1.00 38.83  ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.663 -4.385  12.491 1.00 38.51  ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 14.849 -3.907  12.795 1.00 42.57  ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 14.553 -4.641  14.095 1.00 51.29  ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 15.487 -5.801  14.338 1.00 59.82  ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 16.186 -5.669  15.617 1.00 66.31  ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 17.422 -5.201  15.745 1.00 71.42  ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 18.102 -4.791  14.677 1.00 72.84  ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 17.991 -5.140  16.941 1.00 72.25  ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.622 -4.221  10.457 1.00 38.67  ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 11.721 -5.176  9.816  1.00 39.96  ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.598 -6.368  9.296  1.00 41.29  ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 13.828 -6.341  9.438  1.00 42.00  ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 10.925 -4.510  8.684  1.00 40.47  ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 11.909 -3.988  7.236  1.00 36.92  ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 12.000 -7.323  8.576  1.00 42.36  ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 12.767 -8.414  7.943  1.00 45.05  ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 13.841 -7.889  6.949  1.00 46.20  ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 14.821 -8.578  6.691  1.00 48.03  ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 11.803 -9.357  7.205  1.00 47.94  ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.192 -8.730  5.963  1.00 51.87  ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.185 -9.604  5.270  1.00 57.07  ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 8.959  -9.395  5.379  1.00 58.75  ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 10.681 -10.589 4.525  1.00 56.22  ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 13.681 -6.660  6.424  1.00 45.38  ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 14.592 -6.077  5.440  1.00 44.72  ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 15.736 -5.236  6.015  1.00 45.92  ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 16.593 -4.773  5.250  1.00 47.90  ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 13.800 -5.257  4.417  1.00 43.34  ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 12.689 -6.028  3.760  1.00 42.33  ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 11.360 -5.783  4.061  1.00 44.28  ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 12.748 -6.995  2.816  1.00 43.80  ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 10.655 -6.590  3.288  1.00 44.93  ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 11.447 -7.385  2.571  1.00 45.04  ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 15.763 -5.036  7.332  1.00 44.34  ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 16.823 -4.265  7.965  1.00 43.30  ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.325 -3.144  8.854  1.00 42.22  ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.221 -3.217  9.402  1.00 40.25  ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.173 -2.120  9.040  1.00 42.06  ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.839 -0.958  9.867  1.00 42.02  ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.865 -0.056  9.137  1.00 40.49  ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.149 0.385   8.010  1.00 40.87  ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 18.119 -0.182  10.295 1.00 43.64  ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.754 1.103   11.044 1.00 44.79  ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 19.021 -1.072  11.156 1.00 44.67  ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.731 0.234   9.783  1.00 38.41  ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.687 1.113   9.282  1.00 36.95  ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.860 2.571   9.793  1.00 37.27  ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.655 3.537   9.049  1.00 37.60  ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.304 0.543   9.693  1.00 37.30  ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.168 1.517   9.388  1.00 37.37  ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 12.061 -0.821  9.065  1.00 37.17  ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.210 2.711   11.063 1.00 36.34  ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.357 4.021   11.669 1.00 37.21  ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.765 3.979   13.128 1.00 36.77  ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 15.173 2.927   13.627 1.00 37.12  ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.741 5.157   13.792 1.00 36.14  ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 15.118 5.269   15.197 1.00 35.61  ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 14.010 6.069   15.942 1.00 35.91  ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 13.409 6.992   15.376 1.00 35.90  ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 16.514 5.940   15.386 1.00 36.32  ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 16.577 7.270   14.647 1.00 37.36  ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 17.718 5.003   15.008 1.00 37.98  ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.920 8.091   14.927 1.00 38.54  ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 13.785 5.729   17.238 1.00 35.80  ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 12.843 6.409   18.129 1.00 35.34  ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 13.222 7.898   18.184 1.00 35.42  ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 14.406 8.236   18.325 1.00 35.81  ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 12.896 5.800   19.541 1.00 35.38  ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 12.003 6.595   20.494 1.00 35.71  ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 12.463 4.318   19.518 1.00 34.93  ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 12.250 8.768   17.980 1.00 36.26  ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 12.516 10.205  17.958 1.00 37.77  ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 11.516 10.984  18.798 1.00 39.76  ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 11.865 12.041  19.318 1.00 41.21  ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 12.494 10.720  16.517 1.00 39.55  ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 12.615 12.138  16.456 1.00 42.75  ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 10.258 10.506  18.873 1.00 40.17  ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 9.176  11.210  19.586 1.00 42.74  ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 8.321  10.177  20.395 1.00 42.26  ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 8.449  8.945   20.221 1.00 40.40  ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 8.273  12.053  18.592 1.00 46.05  ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 7.269  11.211  18.011 1.00 48.96  ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 9.033  12.699  17.473 1.00 47.99  ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 7.457  10.691  21.266 1.00 43.22  ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 6.564  9.848   22.047 1.00 44.65  ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 5.642  10.657  22.934 1.00 46.90  ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 5.823  11.866  23.114 1.00 46.28  ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 4.684  9.982   23.514 1.00 49.34  ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 3.700  10.614  24.395 1.00 51.61  ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 2.332  10.016  24.158 1.00 52.85  ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 2.059  9.520   23.058 1.00 52.76  ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 1.465  10.043  25.195 1.00 53.44  ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? 0.090  9.531   25.138 1.00 53.65  ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? -0.026 8.044   24.726 1.00 51.80  ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -1.055 7.638   24.191 1.00 51.91  ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? -0.773 10.411  24.215 1.00 56.38  ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -0.926 11.847  24.680 1.00 61.70  ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -0.905 12.145  25.887 1.00 63.89  ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -1.117 12.764  23.731 1.00 61.90  ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? 0.994  7.246   25.005 1.00 49.96  ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 0.967  5.828   24.642 1.00 48.46  ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 1.354  5.529   23.198 1.00 46.70  ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 1.131  4.417   22.689 1.00 46.33  ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 1.976  6.501   22.538 1.00 45.34  ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 2.464  6.326   21.184 1.00 45.01  ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 3.982  6.540   21.156 1.00 44.15  ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 4.528  7.276   21.980 1.00 46.16  ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 1.814  7.312   20.200 1.00 45.77  ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? 0.305  7.446   20.215 1.00 49.09  ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? -0.096 8.633   19.370 1.00 51.16  ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? -0.360 6.191   19.670 1.00 49.63  ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 4.648  5.897   20.212 1.00 40.77  ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 6.080  6.065   19.973 1.00 38.81  ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 6.219  6.472   18.473 1.00 38.19  ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 5.512  5.955   17.604 1.00 37.68  ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 6.883  4.785   20.368 1.00 38.39  ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 6.252  3.504   19.810 1.00 38.66  ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 8.362  4.900   20.015 1.00 37.51  ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 7.077  7.446   18.220 1.00 37.51  ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 7.350  7.979   16.899 1.00 38.00  ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 8.778  7.656   16.480 1.00 37.76  ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 9.707  7.798   17.272 1.00 37.18  ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 8.940  7.200   15.226 1.00 37.04  ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 10.212 6.785   14.646 1.00 35.82  ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 10.510 7.652   13.431 1.00 37.14  ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.635  7.861   12.594 1.00 37.25  ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 10.157 5.323   14.178 1.00 35.09  ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 9.635  4.371   15.226 1.00 34.75  ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 10.486 3.816   16.167 1.00 35.54  ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 8.298  3.998   15.243 1.00 34.37  ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 9.990  2.934   17.139 1.00 36.11  ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 7.813  3.104   16.203 1.00 36.58  ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 8.657  2.594   17.154 1.00 36.30  ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.743 8.158   13.360 1.00 37.61  ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 12.228 8.956   12.242 1.00 37.54  ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.627 7.933   11.149 1.00 37.93  ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.570 7.160   11.356 1.00 36.45  ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 13.457 9.753   12.679 1.00 38.53  ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 11.918 7.909   9.999  1.00 38.91  ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.287 6.996   8.896  1.00 39.59  ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.685 7.281   8.291  1.00 39.84  ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 14.032 8.440   8.094  1.00 39.18  ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.270 7.121   7.754  1.00 41.59  ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.437 6.057   6.680  1.00 45.74  ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.527 4.876   7.032  1.00 45.28  ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 11.488 6.418   5.482  1.00 48.23  ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.471 6.239   7.971  1.00 39.53  ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.760 6.437   7.277  1.00 40.78  ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.778 5.628   5.923  1.00 41.94  ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.842 5.512   5.320  1.00 42.15  ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.976 6.010   8.143  1.00 40.33  ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 17.035 6.786   9.448  1.00 39.83  ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.965 4.499   8.394  1.00 41.10  ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.636 4.956   5.538  1.00 41.01  ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.564 4.090   4.336  1.00 40.28  ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 14.634 4.877   2.999  1.00 42.33  ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 14.989 4.296   1.966  1.00 43.65  ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.277 3.229   4.387  1.00 37.74  ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.305 2.181   5.493  1.00 35.62  ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 12.015 1.365   5.500  1.00 36.23  ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 10.885 2.234   5.868  1.00 37.02  ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.620  1.833   5.940  1.00 38.81  ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.299  0.578   5.653  1.00 38.84  ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.663  2.688   6.299  1.00 37.12  ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.328 6.186   3.018  1.00 42.44  ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 14.430 7.012   1.809  1.00 43.51  ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 15.853 7.546   1.543  1.00 44.80  ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 16.116 8.029   0.441  1.00 46.87  ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 13.470 8.210   1.860  1.00 44.41  ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 13.761 9.190   2.983  1.00 48.08  ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 14.045 8.733   4.114  1.00 48.28  ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 13.678 10.408  2.740  1.00 49.49  ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 16.748 7.489   2.539  1.00 44.38  ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 18.127 8.006   2.420  1.00 45.11  ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 18.997 6.985   1.697  1.00 45.20  ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 19.791 6.275   2.320  1.00 44.88  ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 18.676 8.307   3.824  1.00 45.40  ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 17.811 9.235   4.679  1.00 47.00  ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.380 9.374   6.077  1.00 47.99  ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 17.611 10.597  4.014  1.00 47.75  ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 18.755 6.825   0.386  1.00 45.22  ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 19.397 5.804   -0.413 1.00 47.32  ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 20.927 5.911   -0.454 1.00 48.66  ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 21.618 4.906   -0.621 1.00 48.54  ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 18.845 5.839   -1.837 1.00 48.72  ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 17.352 5.739   -2.051 1.00 51.10  ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 17.083 5.494   -3.527 1.00 52.72  ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 16.716 4.595   -1.220 1.00 51.97  ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 21.439 7.141   -0.302 1.00 49.55  ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 22.870 7.423   -0.313 1.00 50.66  ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 23.603 6.834   0.888  1.00 51.81  ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 24.825 6.808   0.866  1.00 51.79  ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 23.114 8.932   -0.428 1.00 50.80  ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 22.400 9.748   0.601  1.00 50.53  ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 21.201 10.379  0.460  1.00 51.15  ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 22.856 10.039  1.933  1.00 50.57  ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 20.884 11.055  1.618  1.00 51.61  ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 21.897 10.881  2.529  1.00 51.08  ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 24.013 9.714   2.660  1.00 50.91  ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 22.020 11.335  3.843  1.00 51.31  ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 24.157 10.215  3.940  1.00 51.42  ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.173 11.020  4.515  1.00 51.28  ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 22.882 6.348   1.929  1.00 52.68  ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 23.524 5.687   3.070  1.00 53.93  ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 24.231 4.401   2.613  1.00 56.57  ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 25.188 3.994   3.258  1.00 56.62  ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.492 5.336   4.158  1.00 53.44  ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 21.927 6.494   4.955  1.00 53.13  ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 20.798 6.031   5.864  1.00 52.84  ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 22.996 7.171   5.766  1.00 53.24  ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 23.752 3.763   1.508  1.00 58.78  ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 24.250 2.515   0.928  1.00 61.86  ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 25.503 2.664   0.069  1.00 64.96  ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 26.067 1.642   -0.331 1.00 65.27  ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 23.181 1.897   0.020  1.00 64.27  ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 21.937 1.413   0.721  1.00 70.79  ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 21.987 1.221   1.953  1.00 72.10  ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 20.904 1.234   0.036  1.00 73.30  ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 25.896 3.897   -0.287 1.00 66.95  ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 27.058 4.078   -1.165 1.00 69.53  ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 28.123 5.045   -0.618 1.00 70.67  ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 27.795 6.064   -0.005 1.00 71.34  ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 26.601 4.493   -2.576 1.00 73.52  ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 25.622 5.659   -2.591 1.00 80.08  ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 24.530 5.559   -3.639 1.00 87.72  ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 24.274 6.571   -4.335 1.00 88.22  ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 23.926 4.467   -3.758 1.00 90.46  ? 145 GLU   A OE2 1 
HETATM 1084 N  N1  . A1B1O B 2 .   ? 11.085 15.365  18.318 1.00 54.22  ? 201 A1B1O A N1  1 
HETATM 1085 N  N3  . A1B1O B 2 .   ? 10.296 10.150  23.304 1.00 54.19  ? 201 A1B1O A N3  1 
HETATM 1086 C  C4  . A1B1O B 2 .   ? 12.875 15.007  20.045 1.00 54.36  ? 201 A1B1O A C4  1 
HETATM 1087 C  C5  . A1B1O B 2 .   ? 11.639 15.683  19.544 1.00 54.27  ? 201 A1B1O A C5  1 
HETATM 1088 C  C6  . A1B1O B 2 .   ? 10.906 16.654  20.107 1.00 54.25  ? 201 A1B1O A C6  1 
HETATM 1089 C  C7  . A1B1O B 2 .   ? 10.070 16.145  18.224 1.00 54.14  ? 201 A1B1O A C7  1 
HETATM 1090 C  C8  . A1B1O B 2 .   ? 10.915 12.195  23.459 1.00 55.35  ? 201 A1B1O A C8  1 
HETATM 1091 C  C10 . A1B1O B 2 .   ? 9.447  10.665  24.236 1.00 54.63  ? 201 A1B1O A C10 1 
HETATM 1092 C  C13 . A1B1O B 2 .   ? 8.025  12.232  25.995 1.00 55.04  ? 201 A1B1O A C13 1 
HETATM 1093 C  C15 . A1B1O B 2 .   ? 9.795  12.017  24.378 1.00 54.93  ? 201 A1B1O A C15 1 
HETATM 1094 C  C   . A1B1O B 2 .   ? 11.468 15.372  25.024 1.00 56.92  ? 201 A1B1O A C   1 
HETATM 1095 C  C1  . A1B1O B 2 .   ? 11.592 14.470  24.265 1.00 56.56  ? 201 A1B1O A C1  1 
HETATM 1096 C  C2  . A1B1O B 2 .   ? 11.828 13.388  23.290 1.00 56.02  ? 201 A1B1O A C2  1 
HETATM 1097 C  C14 . A1B1O B 2 .   ? 9.065  12.799  25.270 1.00 55.03  ? 201 A1B1O A C14 1 
HETATM 1098 C  C12 . A1B1O B 2 .   ? 7.707  10.888  25.848 1.00 54.90  ? 201 A1B1O A C12 1 
HETATM 1099 C  C11 . A1B1O B 2 .   ? 8.418  10.084  24.969 1.00 54.49  ? 201 A1B1O A C11 1 
HETATM 1100 C  C9  . A1B1O B 2 .   ? 10.425 8.767   22.872 1.00 53.87  ? 201 A1B1O A C9  1 
HETATM 1101 N  N2  . A1B1O B 2 .   ? 11.163 11.095  22.827 1.00 54.50  ? 201 A1B1O A N2  1 
HETATM 1102 N  N   . A1B1O B 2 .   ? 11.745 13.881  21.917 1.00 55.43  ? 201 A1B1O A N   1 
HETATM 1103 C  C3  . A1B1O B 2 .   ? 12.838 14.786  21.546 1.00 54.62  ? 201 A1B1O A C3  1 
HETATM 1104 O  O   . A1B1O B 2 .   ? 9.877  16.976  19.267 1.00 54.43  ? 201 A1B1O A O   1 
HETATM 1105 ZN ZN  . ZN    C 3 .   ? 10.862 -4.140  5.356  1.00 36.52  2 202 ZN    A ZN  1 
HETATM 1106 S  S   . DMS   D 4 .   ? 20.448 -3.408  22.335 1.00 112.01 ? 203 DMS   A S   1 
HETATM 1107 O  O   . DMS   D 4 .   ? 20.459 -3.154  23.815 1.00 112.02 ? 203 DMS   A O   1 
HETATM 1108 C  C1  . DMS   D 4 .   ? 21.772 -4.595  21.983 1.00 111.95 ? 203 DMS   A C1  1 
HETATM 1109 C  C2  . DMS   D 4 .   ? 19.091 -4.550  21.983 1.00 112.05 ? 203 DMS   A C2  1 
HETATM 1110 S  S   . DMS   E 4 .   ? 0.723  -1.529  23.527 1.00 94.33  ? 204 DMS   A S   1 
HETATM 1111 O  O   . DMS   E 4 .   ? 0.766  -0.214  24.259 1.00 94.31  ? 204 DMS   A O   1 
HETATM 1112 C  C1  . DMS   E 4 .   ? 1.673  -2.734  24.502 1.00 94.32  ? 204 DMS   A C1  1 
HETATM 1113 C  C2  . DMS   E 4 .   ? -0.911 -2.295  23.792 1.00 94.24  ? 204 DMS   A C2  1 
HETATM 1114 O  O   . HOH   F 5 .   ? 12.957 7.732   31.034 1.00 63.85  ? 301 HOH   A O   1 
HETATM 1115 O  O   . HOH   F 5 .   ? 24.107 22.109  8.085  1.00 54.85  ? 302 HOH   A O   1 
HETATM 1116 O  O   . HOH   F 5 .   ? 10.469 5.448   3.395  1.00 38.87  ? 303 HOH   A O   1 
HETATM 1117 O  O   . HOH   F 5 .   ? 20.282 9.039   18.763 1.00 42.23  ? 304 HOH   A O   1 
HETATM 1118 O  O   . HOH   F 5 .   ? 1.190  -1.990  20.006 1.00 40.48  ? 305 HOH   A O   1 
HETATM 1119 O  O   . HOH   F 5 .   ? 8.294  19.525  18.107 1.00 40.64  ? 306 HOH   A O   1 
HETATM 1120 O  O   . HOH   F 5 .   ? 23.368 0.077   15.469 1.00 46.37  ? 307 HOH   A O   1 
HETATM 1121 O  O   . HOH   F 5 .   ? 29.328 3.377   10.098 1.00 47.17  ? 308 HOH   A O   1 
HETATM 1122 O  O   . HOH   F 5 .   ? 2.934  8.588   10.003 1.00 48.89  ? 309 HOH   A O   1 
HETATM 1123 O  O   . HOH   F 5 .   ? 11.379 12.230  11.484 1.00 35.04  ? 310 HOH   A O   1 
HETATM 1124 O  O   . HOH   F 5 .   ? 22.321 -0.609  3.863  1.00 46.02  ? 311 HOH   A O   1 
HETATM 1125 O  O   . HOH   F 5 .   ? 27.768 3.567   2.668  1.00 61.08  ? 312 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 0.360  2.572   24.480 1.00 47.20  ? 313 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 9.002  3.133   2.775  1.00 40.95  ? 314 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 6.059  -5.007  28.651 1.00 49.49  ? 315 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 18.301 21.379  9.313  1.00 45.20  ? 316 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 26.444 3.966   19.591 1.00 67.59  ? 317 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 30.396 21.284  19.723 1.00 50.73  ? 318 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 10.648 8.804   4.480  1.00 45.61  ? 319 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 4.035  -4.529  21.207 1.00 51.84  ? 320 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 19.479 -0.296  27.124 1.00 56.80  ? 321 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 9.851  23.958  24.386 1.00 64.60  ? 322 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 5.867  -6.981  14.317 1.00 63.08  ? 323 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 21.630 -4.477  12.312 1.00 46.71  ? 324 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 5.926  2.315   6.370  1.00 44.89  ? 325 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 15.161 2.628   23.196 1.00 36.82  ? 326 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 31.128 2.704   11.906 1.00 61.02  ? 327 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 0.581  0.220   16.521 1.00 32.39  ? 328 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 18.316 -3.169  18.880 1.00 70.72  ? 329 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 10.199 4.756   33.617 1.00 42.42  ? 330 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 8.038  -8.418  23.306 1.00 42.53  ? 331 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 15.170 11.890  0.881  1.00 55.48  ? 332 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 16.088 12.363  24.043 1.00 48.24  ? 333 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 16.309 23.979  14.397 1.00 68.50  ? 334 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 18.398 19.141  17.164 1.00 39.83  ? 335 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 14.771 21.131  7.999  1.00 53.46  ? 336 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 30.603 11.108  17.665 1.00 57.20  ? 337 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 11.583 2.582   33.470 1.00 39.56  ? 338 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 3.844  1.259   30.671 1.00 60.07  ? 339 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 8.089  -3.562  0.280  1.00 40.39  ? 340 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 17.998 2.652   23.080 1.00 36.95  ? 341 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 14.651 14.975  3.763  1.00 47.49  ? 342 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 14.242 -4.093  34.299 1.00 47.75  ? 343 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 7.298  4.036   32.971 1.00 55.02  ? 344 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 6.190  8.464   28.474 1.00 54.27  ? 345 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 31.457 18.618  7.983  1.00 60.11  ? 346 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 0.161  12.996  21.158 1.00 79.99  ? 347 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 3.939  -4.567  6.255  1.00 45.32  ? 348 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 14.147 9.668   29.752 1.00 48.26  ? 349 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 19.454 9.162   25.640 1.00 47.07  ? 350 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 3.230  4.538   27.659 1.00 56.06  ? 351 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 20.957 -4.588  9.958  1.00 46.16  ? 352 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 30.089 5.009   3.239  1.00 56.18  ? 353 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 19.702 24.395  15.176 1.00 81.88  ? 354 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 6.962  16.739  25.213 1.00 65.01  ? 355 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 12.459 -8.364  24.230 1.00 46.70  ? 356 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 4.630  12.060  18.946 1.00 51.75  ? 357 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 13.265 11.000  9.399  1.00 37.14  ? 358 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 5.250  -1.012  24.206 1.00 43.89  ? 359 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 15.228 -3.359  17.441 1.00 53.63  ? 360 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 1.259  -2.150  17.220 1.00 39.53  ? 361 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 7.617  25.857  15.152 1.00 60.33  ? 362 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? -0.534 16.210  12.455 1.00 60.46  ? 363 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 6.069  25.501  21.377 1.00 54.12  ? 364 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 4.598  7.742   2.962  1.00 63.08  ? 365 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 1.794  -6.067  18.384 1.00 54.09  ? 366 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 23.878 2.349   19.057 1.00 46.98  ? 367 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 11.177 17.715  27.268 1.00 68.58  ? 368 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 3.176  15.150  20.331 1.00 54.67  ? 369 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 6.584  -3.279  -1.750 1.00 54.51  ? 370 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 22.436 8.814   21.133 1.00 49.23  ? 371 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 0.077  4.468   6.484  1.00 55.30  ? 372 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 28.463 -1.810  13.175 1.00 57.04  ? 373 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 18.644 19.681  5.052  1.00 64.77  ? 374 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 30.377 -4.032  6.553  1.00 66.79  ? 375 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 2.037  13.651  5.321  1.00 56.63  ? 376 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 2.065  -5.997  14.802 1.00 70.05  ? 377 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 30.569 10.812  20.437 1.00 67.48  ? 378 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 4.324  -1.707  21.819 1.00 48.90  ? 379 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 18.726 -0.050  19.494 1.00 53.93  ? 380 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 22.697 19.140  5.624  1.00 49.81  ? 381 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 9.444  9.516   31.870 1.00 59.15  ? 382 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 17.902 9.353   -1.936 1.00 49.06  ? 383 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 14.232 -8.790  26.921 1.00 80.55  ? 384 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 8.535  -7.151  8.456  1.00 55.77  ? 385 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? -0.639 23.873  13.928 1.00 59.73  ? 386 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 32.850 14.400  6.299  1.00 57.35  ? 387 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 21.063 7.439   -4.596 1.00 46.70  ? 388 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? 7.256  15.878  22.664 1.00 65.71  ? 389 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 7.420  -4.803  2.697  1.00 50.39  ? 390 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 26.209 -2.152  14.503 1.00 67.43  ? 391 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 17.528 11.285  0.093  1.00 57.71  ? 392 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 24.700 7.253   20.929 1.00 58.40  ? 393 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 28.242 20.155  20.421 1.00 56.43  ? 394 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 4.290  -1.479  26.751 1.00 57.70  ? 395 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 6.351  3.263   3.456  1.00 52.46  ? 396 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 31.344 7.891   3.389  1.00 61.93  ? 397 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 20.137 9.597   -2.932 1.00 59.81  ? 398 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 37.040 17.167  13.231 1.00 54.33  ? 399 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 2.119  2.426   26.748 1.00 57.61  ? 400 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 17.585 11.835  26.290 1.00 72.95  ? 401 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 10.447 -4.947  -0.613 1.00 63.61  ? 402 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 12.185 23.601  15.017 1.00 51.95  ? 403 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 2.868  14.541  22.871 1.00 59.05  ? 404 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 8.671  7.410   2.769  1.00 56.94  ? 405 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 23.613 14.023  0.859  1.00 63.92  ? 406 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 5.896  7.041   31.069 1.00 54.24  ? 407 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 14.001 -6.126  32.673 1.00 67.15  ? 408 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 20.389 15.022  0.397  1.00 62.57  ? 409 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 19.222 -7.359  7.887  1.00 64.19  ? 410 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 5.469  -7.997  23.366 1.00 61.09  ? 411 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 38.804 20.966  18.076 1.00 73.01  ? 412 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? 23.148 9.996   23.375 1.00 62.32  ? 413 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 20.594 12.298  26.742 1.00 67.03  ? 414 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 7.977  10.268  29.580 1.00 60.74  ? 415 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? 31.380 6.824   15.295 1.00 66.06  ? 416 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 3.740  -6.337  22.932 1.00 55.19  ? 417 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 19.347 14.108  30.060 1.00 95.66  ? 418 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 6.044  5.526   2.127  1.00 58.49  ? 419 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 5 .   ? 22.061 11.849  -3.061 1.00 77.08  ? 420 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 5 .   ? 25.451 11.319  -1.510 1.00 70.34  ? 421 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 5 .   ? 10.149 25.213  14.144 1.00 60.84  ? 422 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 5 .   ? 5.602  23.314  8.503  1.00 66.10  ? 423 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   ? 0.6068 0.5120 0.7583 0.0036  0.0367  -0.0331 7   SER   A N   
2    C CA  . SER   A 1   ? 0.6004 0.5137 0.7927 0.0007  0.0326  -0.0299 7   SER   A CA  
3    C C   . SER   A 1   ? 0.5898 0.5119 0.7887 -0.0023 0.0446  -0.0179 7   SER   A C   
4    O O   . SER   A 1   ? 0.6069 0.5277 0.7788 -0.0019 0.0521  -0.0131 7   SER   A O   
5    C CB  . SER   A 1   ? 0.6302 0.5372 0.8332 0.0036  0.0105  -0.0382 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6982 0.5982 0.8717 0.0074  0.0025  -0.0365 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5579 0.4883 0.7934 -0.0052 0.0481  -0.0133 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.5432 0.4812 0.7850 -0.0075 0.0604  -0.0037 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.5166 0.4638 0.7874 -0.0104 0.0732  0.0028  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.5100 0.4589 0.7904 -0.0110 0.0770  0.0025  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.4973 0.4497 0.7812 -0.0116 0.0811  0.0091  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.4839 0.4436 0.7915 -0.0133 0.0952  0.0165  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.4713 0.4354 0.7707 -0.0141 0.1084  0.0224  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.4766 0.4382 0.7639 -0.0137 0.1048  0.0207  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.4702 0.4303 0.8218 -0.0133 0.0896  0.0156  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.4545 0.4243 0.7594 -0.0147 0.1237  0.0294  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.4508 0.4242 0.7494 -0.0149 0.1374  0.0337  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.4573 0.4323 0.7933 -0.0143 0.1450  0.0381  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.4500 0.4258 0.8121 -0.0141 0.1470  0.0417  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.4519 0.4298 0.7276 -0.0147 0.1492  0.0386  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.4502 0.4277 0.6984 -0.0153 0.1424  0.0350  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.4624 0.4426 0.7266 -0.0145 0.1615  0.0401  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.4468 0.4293 0.6812 -0.0145 0.1503  0.0403  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.4737 0.4487 0.8162 -0.0141 0.1501  0.0378  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.4751 0.4516 0.8554 -0.0133 0.1596  0.0419  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.4752 0.4536 0.8419 -0.0123 0.1795  0.0456  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.4648 0.4418 0.8173 -0.0124 0.1798  0.0413  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.4792 0.4534 0.8858 -0.0130 0.1464  0.0372  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.5001 0.4717 0.9201 -0.0132 0.1255  0.0322  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.5060 0.4791 0.9642 -0.0135 0.1239  0.0335  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.5276 0.4944 0.9208 -0.0126 0.1081  0.0260  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.5209 0.4908 0.9896 -0.0136 0.1037  0.0265  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.5452 0.5082 0.9442 -0.0119 0.0889  0.0200  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.5513 0.5160 0.9885 -0.0125 0.0857  0.0191  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.5789 0.5391 1.0217 -0.0117 0.0658  0.0107  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.4733 0.4538 0.8406 -0.0109 0.1961  0.0535  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4954 0.4764 0.8438 -0.0087 0.2160  0.0570  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.5123 0.4934 0.8913 -0.0063 0.2357  0.0663  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.5165 0.4982 0.9111 -0.0058 0.2391  0.0743  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.5165 0.4988 0.8200 -0.0079 0.2179  0.0580  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.5130 0.4968 0.8187 -0.0074 0.2155  0.0655  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5317 0.5137 0.8120 -0.0048 0.2365  0.0600  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.5121 0.4920 0.9038 -0.0048 0.2498  0.0656  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.5173 0.4966 0.9412 -0.0022 0.2716  0.0748  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.5129 0.4939 0.9917 -0.0041 0.2635  0.0778  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.5203 0.5021 1.0196 -0.0065 0.2433  0.0700  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.5052 0.4861 1.0044 -0.0028 0.2761  0.0887  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.4897 0.4720 1.0437 -0.0050 0.2672  0.0904  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.4838 0.4659 1.0244 -0.0066 0.2525  0.0909  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.4772 0.4590 1.0523 -0.0070 0.2564  0.0977  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.5129 0.4948 1.1124 -0.0029 0.2929  0.1022  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.5834 0.5657 1.2066 -0.0017 0.3047  0.0996  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.5944 0.5792 1.2556 -0.0039 0.2888  0.0915  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.6150 0.5944 1.2134 0.0024  0.3319  0.1056  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.4826 0.4646 0.9762 -0.0076 0.2365  0.0834  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.4848 0.4664 0.9641 -0.0087 0.2228  0.0824  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.4770 0.4580 0.9430 -0.0113 0.1964  0.0690  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.4740 0.4548 0.9195 -0.0116 0.1901  0.0621  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.5044 0.4861 0.9362 -0.0062 0.2328  0.0894  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.5214 0.5019 0.9548 -0.0022 0.2586  0.1045  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.5227 0.5018 0.9966 -0.0016 0.2683  0.1152  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.5542 0.5343 0.9465 0.0014  0.2733  0.1082  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.5455 0.5223 1.0174 0.0030  0.2939  0.1316  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5765 0.5541 0.9618 0.0064  0.2972  0.1229  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5817 0.5573 1.0067 0.0074  0.3087  0.1357  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.6186 0.5904 1.0355 0.0131  0.3349  0.1524  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.4643 0.4439 0.9403 -0.0126 0.1824  0.0658  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.4613 0.4386 0.9203 -0.0140 0.1591  0.0537  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.4590 0.4356 0.8918 -0.0137 0.1575  0.0548  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.4530 0.4290 0.9079 -0.0135 0.1615  0.0599  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.4549 0.4301 0.9559 -0.0152 0.1414  0.0455  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.4900 0.4608 0.9746 -0.0156 0.1189  0.0340  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.5200 0.4882 1.0400 -0.0160 0.0983  0.0239  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.5345 0.4978 1.0536 -0.0161 0.0819  0.0141  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.5632 0.5208 1.0510 -0.0147 0.0630  0.0030  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.5481 0.5045 1.0033 -0.0132 0.0584  0.0021  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.5649 0.5172 1.0525 -0.0143 0.0501  -0.0069 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.4430 0.4196 0.8326 -0.0136 0.1527  0.0509  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.4485 0.4251 0.8139 -0.0131 0.1510  0.0515  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.4507 0.4229 0.8071 -0.0140 0.1324  0.0397  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.4549 0.4252 0.7912 -0.0143 0.1242  0.0331  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.4609 0.4410 0.7862 -0.0121 0.1598  0.0555  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.4634 0.4448 0.7721 -0.0111 0.1591  0.0583  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.4641 0.4469 0.7907 -0.0104 0.1777  0.0650  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.4325 0.4019 0.8022 -0.0138 0.1268  0.0372  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.4447 0.4084 0.8032 -0.0137 0.1106  0.0250  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.4431 0.4062 0.7898 -0.0128 0.1131  0.0256  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.4521 0.4188 0.8107 -0.0122 0.1246  0.0358  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.4566 0.4154 0.8502 -0.0141 0.0965  0.0161  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.4806 0.4382 0.8778 -0.0141 0.0864  0.0114  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.4468 0.4074 0.8865 -0.0149 0.1046  0.0228  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.4301 0.3877 0.7574 -0.0120 0.1025  0.0149  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.4181 0.3740 0.7437 -0.0109 0.1043  0.0136  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.4141 0.3672 0.7831 -0.0112 0.1022  0.0127  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.4078 0.3566 0.7971 -0.0119 0.0911  0.0041  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.4184 0.3671 0.7190 -0.0096 0.0944  0.0009  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.4370 0.3874 0.7003 -0.0094 0.0976  0.0020  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.4426 0.3907 0.6921 -0.0096 0.0923  -0.0005 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.4370 0.3916 0.6872 -0.0090 0.1063  0.0066  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.4154 0.3707 0.7996 -0.0104 0.1119  0.0213  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.4167 0.3688 0.8448 -0.0106 0.1124  0.0220  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.4463 0.3893 0.8840 -0.0107 0.0966  0.0035  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4482 0.3877 0.9227 -0.0120 0.0892  -0.0026 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.4083 0.3630 0.8446 -0.0087 0.1252  0.0351  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.4022 0.3538 0.8889 -0.0090 0.1300  0.0406  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.4152 0.3688 0.9058 -0.0061 0.1424  0.0555  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.4341 0.3841 0.9734 -0.0057 0.1500  0.0641  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.4596 0.4026 1.0295 -0.0060 0.1442  0.0547  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4604 0.3986 1.0153 -0.0064 0.1305  0.0350  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4500 0.3898 1.0661 -0.0055 0.1533  0.0649  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4633 0.4023 0.8680 -0.0090 0.0914  -0.0063 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4872 0.4158 0.8919 -0.0079 0.0773  -0.0252 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5163 0.4401 0.9142 -0.0081 0.0603  -0.0376 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5302 0.4448 0.9306 -0.0068 0.0457  -0.0544 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.5056 0.4306 0.8768 -0.0053 0.0803  -0.0309 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5376 0.4628 0.8624 -0.0043 0.0796  -0.0322 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5666 0.5010 0.8736 -0.0051 0.0908  -0.0186 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5595 0.4762 0.8536 -0.0023 0.0694  -0.0452 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5818 0.5132 0.8528 -0.0042 0.0878  -0.0236 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5828 0.5032 0.8430 -0.0021 0.0760  -0.0384 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5285 0.4580 0.9187 -0.0092 0.0612  -0.0298 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5413 0.4673 0.9289 -0.0089 0.0449  -0.0388 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5550 0.4864 0.9882 -0.0114 0.0441  -0.0329 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5630 0.4934 0.9997 -0.0111 0.0311  -0.0380 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5432 0.4692 0.8837 -0.0074 0.0448  -0.0367 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5471 0.4669 0.8439 -0.0047 0.0463  -0.0426 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5508 0.4710 0.8083 -0.0037 0.0489  -0.0377 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5551 0.4626 0.8439 -0.0016 0.0302  -0.0607 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5582 0.4952 1.0269 -0.0133 0.0589  -0.0210 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.5634 0.5051 1.0786 -0.0154 0.0624  -0.0141 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5690 0.5055 1.1241 -0.0161 0.0426  -0.0293 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5650 0.4943 1.1240 -0.0155 0.0320  -0.0424 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.5599 0.5061 1.1021 -0.0162 0.0833  0.0021  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5757 0.5157 1.1611 -0.0173 0.0367  -0.0287 24  THR   A N   
135  C CA  . THR   A 18  ? 0.5821 0.5187 1.2109 -0.0180 0.0151  -0.0433 24  THR   A CA  
136  C C   . THR   A 18  ? 0.5818 0.5219 1.2817 -0.0212 0.0255  -0.0366 24  THR   A C   
137  O O   . THR   A 18  ? 0.5757 0.5203 1.2850 -0.0221 0.0505  -0.0187 24  THR   A O   
138  C CB  . THR   A 18  ? 0.6010 0.5394 1.2233 -0.0168 -0.0001 -0.0471 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5919 0.5388 1.2524 -0.0187 0.0144  -0.0332 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6325 0.5680 1.1867 -0.0136 -0.0035 -0.0476 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5831 0.5207 1.3334 -0.0225 0.0059  -0.0507 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5847 0.5250 1.4112 -0.0258 0.0130  -0.0466 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5762 0.5255 1.4256 -0.0268 0.0368  -0.0255 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.5734 0.5250 1.4529 -0.0281 0.0616  -0.0093 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6023 0.5395 1.4721 -0.0267 -0.0182 -0.0683 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6188 0.5588 1.5757 -0.0305 -0.0152 -0.0673 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6370 0.5709 1.6333 -0.0325 -0.0197 -0.0774 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6224 0.5700 1.6359 -0.0325 -0.0088 -0.0586 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6246 0.5627 1.7011 -0.0359 -0.0153 -0.0736 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6166 0.5633 1.7067 -0.0360 -0.0081 -0.0620 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.5742 0.5276 1.4061 -0.0256 0.0303  -0.0253 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.5636 0.5245 1.4116 -0.0259 0.0512  -0.0085 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.5586 0.5215 1.3679 -0.0248 0.0821  0.0111  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.5518 0.5186 1.3900 -0.0252 0.1066  0.0272  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.6048 0.5679 1.4308 -0.0240 0.0355  -0.0144 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.6472 0.6176 1.5035 -0.0243 0.0528  -0.0013 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.6452 0.6191 1.5651 -0.0263 0.0658  0.0057  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.6717 0.6437 1.4850 -0.0221 0.0544  0.0020  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.5544 0.5143 1.2992 -0.0230 0.0809  0.0096  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.5490 0.5110 1.2551 -0.0215 0.1055  0.0261  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.5209 0.4816 1.2567 -0.0218 0.1238  0.0381  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.5084 0.4720 1.2402 -0.0205 0.1484  0.0562  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.5757 0.5349 1.2149 -0.0198 0.0978  0.0202  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.6242 0.5834 1.2245 -0.0188 0.0838  0.0119  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.6227 0.5859 1.2316 -0.0188 0.0883  0.0166  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.6647 0.6191 1.2265 -0.0176 0.0699  0.0014  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.5180 0.4735 1.2776 -0.0230 0.1120  0.0282  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.5188 0.4720 1.3109 -0.0230 0.1286  0.0399  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.5088 0.4644 1.3665 -0.0245 0.1456  0.0525  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.5029 0.4583 1.3718 -0.0229 0.1707  0.0723  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.5167 0.4628 1.3258 -0.0241 0.1113  0.0240  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.5343 0.4773 1.2852 -0.0218 0.1062  0.0188  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.5569 0.4963 1.2688 -0.0211 0.0849  0.0000  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.5405 0.4836 1.2664 -0.0194 0.1236  0.0337  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.5735 0.5109 1.2422 -0.0189 0.0895  0.0016  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.5652 0.5055 1.2424 -0.0178 0.1118  0.0219  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.5418 0.4868 1.2811 -0.0177 0.1481  0.0566  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.5748 0.5153 1.2231 -0.0152 0.1225  0.0313  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.5628 0.5075 1.2693 -0.0145 0.1568  0.0662  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.5720 0.5152 1.2346 -0.0135 0.1436  0.0533  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.5028 0.4603 1.4031 -0.0269 0.1325  0.0420  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.5051 0.4654 1.4738 -0.0284 0.1489  0.0530  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.5239 0.4888 1.4700 -0.0258 0.1770  0.0732  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.5330 0.4981 1.5155 -0.0251 0.2038  0.0913  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.4922 0.4545 1.5107 -0.0312 0.1248  0.0353  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.5255 0.4933 1.4113 -0.0240 0.1721  0.0702  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.5225 0.4937 1.3832 -0.0212 0.1970  0.0860  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.5170 0.4872 1.3071 -0.0179 0.2083  0.0956  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.5232 0.4958 1.2671 -0.0159 0.2145  0.0982  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.5594 0.5347 1.4114 -0.0216 0.1851  0.0761  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.6004 0.5782 1.5238 -0.0240 0.1756  0.0690  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.6154 0.5958 1.5841 -0.0238 0.1970  0.0803  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.6112 0.5880 1.5462 -0.0259 0.1431  0.0496  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.4875 0.4538 1.2736 -0.0172 0.2103  0.1003  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.4920 0.4574 1.2200 -0.0139 0.2173  0.1088  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4958 0.4623 1.1973 -0.0095 0.2455  0.1295  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.4832 0.4479 1.2206 -0.0079 0.2676  0.1453  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.4763 0.4370 1.2202 -0.0139 0.2137  0.1100  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4912 0.4513 1.1816 -0.0104 0.2173  0.1176  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.5110 0.4739 1.1448 -0.0108 0.1989  0.1025  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.4932 0.4482 1.2097 -0.0102 0.2151  0.1193  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.5040 0.4729 1.1418 -0.0072 0.2448  0.1293  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.5127 0.4820 1.1145 -0.0022 0.2679  0.1462  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.5197 0.4876 1.0856 0.0013  0.2686  0.1552  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.5337 0.4986 1.1009 0.0058  0.2881  0.1746  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.5296 0.5023 1.0885 -0.0019 0.2662  0.1385  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.5474 0.5199 1.0564 0.0037  0.2850  0.1520  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.5282 0.5021 1.1254 -0.0041 0.2696  0.1333  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.5059 0.4755 1.0436 -0.0004 0.2475  0.1419  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.5006 0.4703 1.0058 0.0027  0.2453  0.1481  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4747 0.4449 0.9724 -0.0006 0.2216  0.1301  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.4588 0.4300 0.9527 -0.0041 0.2072  0.1136  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.5201 0.4930 0.9681 0.0069  0.2531  0.1547  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.5336 0.5087 0.9430 0.0099  0.2455  0.1573  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.5517 0.5252 0.9529 0.0154  0.2546  0.1748  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.5382 0.5174 0.9138 0.0079  0.2278  0.1427  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5637 0.5411 0.9306 0.0168  0.2416  0.1709  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.5557 0.5366 0.9085 0.0119  0.2259  0.1510  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.5438 0.5250 0.9091 0.0034  0.2137  0.1244  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.5619 0.5475 0.8836 0.0112  0.2115  0.1410  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.5583 0.5429 0.8912 0.0027  0.2008  0.1154  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.5595 0.5466 0.8732 0.0064  0.2001  0.1232  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4661 0.4347 0.9633 0.0013  0.2185  0.1341  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.4683 0.4366 0.9558 -0.0008 0.1995  0.1182  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4717 0.4407 0.9405 0.0032  0.2011  0.1275  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4720 0.4391 0.9557 0.0070  0.2144  0.1456  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.4790 0.4421 1.0112 -0.0046 0.1877  0.1041  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.5152 0.4735 1.1004 -0.0040 0.1981  0.1148  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.5860 0.5409 1.1793 -0.0016 0.1987  0.1201  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.5455 0.4968 1.1761 0.0002  0.2120  0.1351  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.6127 0.5685 1.1770 -0.0011 0.1873  0.1105  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.4612 0.4328 0.8997 0.0027  0.1884  0.1163  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.4574 0.4308 0.8811 0.0063  0.1873  0.1226  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.4446 0.4160 0.8681 0.0039  0.1726  0.1042  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.4486 0.4225 0.8434 0.0019  0.1640  0.0918  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.5003 0.4805 0.8786 0.0095  0.1904  0.1308  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.5655 0.5491 0.9295 0.0146  0.1904  0.1423  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5457 0.5280 0.9242 0.0147  0.1836  0.1373  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.6162 0.6035 0.9529 0.0190  0.1965  0.1554  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.4293 0.3952 0.8855 0.0044  0.1711  0.1024  36  SER   A N   
241  C CA  A SER   A 30  ? 0.4209 0.3829 0.8787 0.0031  0.1597  0.0848  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.4318 0.3939 0.8893 0.0031  0.1596  0.0847  36  SER   A CA  
243  C C   . SER   A 30  ? 0.4392 0.4067 0.8618 0.0051  0.1565  0.0834  36  SER   A C   
244  O O   . SER   A 30  ? 0.4422 0.4084 0.8468 0.0032  0.1481  0.0675  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3971 0.3522 0.8977 0.0043  0.1613  0.0854  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.4392 0.3943 0.9394 0.0042  0.1609  0.0848  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3764 0.3263 0.8774 0.0035  0.1512  0.0664  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4668 0.4243 0.9723 0.0089  0.1702  0.1036  36  SER   A OG  
249  N N   . SER   A 31  ? 0.4393 0.4127 0.8523 0.0092  0.1630  0.1005  37  SER   A N   
250  C CA  . SER   A 31  ? 0.4453 0.4253 0.8310 0.0112  0.1591  0.0999  37  SER   A CA  
251  C C   . SER   A 31  ? 0.4452 0.4305 0.7944 0.0085  0.1548  0.0921  37  SER   A C   
252  O O   . SER   A 31  ? 0.4511 0.4404 0.7830 0.0086  0.1502  0.0861  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4834 0.4687 0.8679 0.0169  0.1643  0.1202  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.5475 0.5373 0.9088 0.0185  0.1693  0.1324  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.4372 0.4221 0.7786 0.0062  0.1571  0.0923  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.4464 0.4348 0.7574 0.0036  0.1537  0.0847  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.4469 0.4296 0.7589 -0.0005 0.1470  0.0680  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.4479 0.4324 0.7361 -0.0025 0.1437  0.0612  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.4652 0.4567 0.7646 0.0043  0.1611  0.0951  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.4781 0.4752 0.7630 0.0093  0.1660  0.1107  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.4835 0.4815 0.7530 0.0107  0.1748  0.1193  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.4678 0.4690 0.7107 0.0079  0.1713  0.1088  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.4916 0.4960 0.7076 0.0101  0.1756  0.1135  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.4855 0.4901 0.6932 0.0158  0.1838  0.1294  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.4955 0.5018 0.6922 0.0071  0.1722  0.1024  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.4268 0.4019 0.7667 -0.0013 0.1444  0.0620  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.4243 0.3928 0.7669 -0.0041 0.1357  0.0467  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.4214 0.3917 0.7600 -0.0061 0.1367  0.0487  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.4249 0.3930 0.7480 -0.0079 0.1294  0.0385  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.4492 0.4151 0.7659 -0.0045 0.1287  0.0332  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.4559 0.4132 0.7704 -0.0058 0.1184  0.0178  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.4361 0.3877 0.7778 -0.0062 0.1134  0.0128  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.4790 0.4348 0.7655 -0.0063 0.1147  0.0113  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.4081 0.3820 0.7595 -0.0052 0.1471  0.0628  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.4146 0.3900 0.7655 -0.0067 0.1507  0.0650  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.4219 0.3944 0.8140 -0.0070 0.1562  0.0705  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3987 0.3699 0.8141 -0.0052 0.1634  0.0802  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.4176 0.3994 0.7411 -0.0049 0.1605  0.0756  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.4437 0.4294 0.7299 -0.0056 0.1553  0.0691  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.4498 0.4410 0.7127 -0.0038 0.1635  0.0774  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.4423 0.4247 0.7218 -0.0086 0.1465  0.0560  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.4326 0.4041 0.8363 -0.0091 0.1533  0.0651  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.4320 0.4018 0.8790 -0.0099 0.1591  0.0698  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.4478 0.4204 0.8901 -0.0106 0.1640  0.0710  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.4454 0.4183 0.8657 -0.0119 0.1540  0.0610  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.4220 0.3862 0.9037 -0.0121 0.1442  0.0561  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.4306 0.3931 0.9686 -0.0134 0.1492  0.0602  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.4185 0.3754 0.9912 -0.0141 0.1410  0.0530  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.4472 0.4105 1.0019 -0.0153 0.1412  0.0524  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.4492 0.4230 0.9136 -0.0095 0.1808  0.0839  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.4598 0.4357 0.9262 -0.0097 0.1888  0.0857  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.4696 0.4438 0.9935 -0.0109 0.1934  0.0881  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.4476 0.4200 1.0013 -0.0100 0.2039  0.0983  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.4731 0.4517 0.9065 -0.0062 0.2076  0.0984  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.4771 0.4567 0.9162 -0.0062 0.2180  0.0990  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.4852 0.4663 0.8675 -0.0054 0.2006  0.0944  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.4831 0.4579 1.0262 -0.0129 0.1846  0.0789  43  SER   A N   
298  C CA  . SER   A 37  ? 0.4852 0.4597 1.0881 -0.0143 0.1874  0.0798  43  SER   A CA  
299  C C   . SER   A 37  ? 0.4950 0.4724 1.1033 -0.0137 0.1986  0.0829  43  SER   A C   
300  O O   . SER   A 37  ? 0.4957 0.4743 1.0643 -0.0131 0.1955  0.0785  43  SER   A O   
301  C CB  . SER   A 37  ? 0.4944 0.4665 1.1248 -0.0170 0.1613  0.0632  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.5218 0.4940 1.1222 -0.0173 0.1437  0.0510  43  SER   A OG  
303  N N   . SER   A 38  ? 0.4803 0.4584 1.1407 -0.0137 0.2137  0.0910  44  SER   A N   
304  C CA  . SER   A 38  ? 0.4940 0.4744 1.1670 -0.0126 0.2275  0.0944  44  SER   A CA  
305  C C   . SER   A 38  ? 0.5070 0.4893 1.2039 -0.0148 0.2057  0.0800  44  SER   A C   
306  O O   . SER   A 38  ? 0.5180 0.4995 1.2408 -0.0170 0.1830  0.0696  44  SER   A O   
307  C CB  . SER   A 38  ? 0.4970 0.4772 1.2214 -0.0115 0.2531  0.1086  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.5053 0.4846 1.2855 -0.0143 0.2425  0.1057  44  SER   A OG  
309  N N   . THR   A 39  ? 0.5104 0.4945 1.2000 -0.0136 0.2122  0.0795  45  THR   A N   
310  C CA  . THR   A 39  ? 0.5140 0.4996 1.2254 -0.0146 0.1923  0.0681  45  THR   A CA  
311  C C   . THR   A 39  ? 0.5287 0.5172 1.2859 -0.0135 0.2100  0.0736  45  THR   A C   
312  O O   . THR   A 39  ? 0.5292 0.5173 1.2786 -0.0113 0.2391  0.0849  45  THR   A O   
313  C CB  . THR   A 39  ? 0.5315 0.5158 1.1845 -0.0139 0.1797  0.0603  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.5393 0.5240 1.1649 -0.0118 0.2020  0.0666  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.5413 0.5228 1.1467 -0.0146 0.1655  0.0553  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.5407 0.5316 1.3415 -0.0143 0.1923  0.0654  46  THR   A N   
317  C CA  . THR   A 40  ? 0.5544 0.5486 1.4053 -0.0131 0.2081  0.0699  46  THR   A CA  
318  C C   . THR   A 40  ? 0.5724 0.5661 1.3893 -0.0108 0.2148  0.0686  46  THR   A C   
319  O O   . THR   A 40  ? 0.5811 0.5756 1.4175 -0.0088 0.2401  0.0752  46  THR   A O   
320  C CB  . THR   A 40  ? 0.5716 0.5695 1.4961 -0.0148 0.1871  0.0629  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.6076 0.6054 1.5188 -0.0143 0.1553  0.0506  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.5703 0.5677 1.5272 -0.0175 0.1779  0.0614  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.5760 0.5674 1.3441 -0.0108 0.1937  0.0600  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.5790 0.5691 1.3159 -0.0088 0.1991  0.0581  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.5845 0.5714 1.2519 -0.0084 0.2112  0.0600  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.5854 0.5711 1.2211 -0.0097 0.2042  0.0599  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.5837 0.5730 1.3195 -0.0086 0.1684  0.0486  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.5763 0.5619 1.2226 -0.0065 0.2283  0.0606  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.5876 0.5704 1.1719 -0.0058 0.2389  0.0606  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.5726 0.5534 1.1152 -0.0074 0.2154  0.0523  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.5650 0.5449 1.1205 -0.0074 0.1990  0.0469  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.6287 0.6098 1.2086 -0.0030 0.2653  0.0621  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.7380 0.7159 1.2564 -0.0022 0.2713  0.0576  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.8309 0.8069 1.3206 0.0008  0.2978  0.0639  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8375 0.8139 1.3506 0.0026  0.3149  0.0738  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8649 0.8383 1.3027 0.0017  0.3014  0.0584  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5649 0.5449 1.0612 -0.0082 0.2140  0.0524  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5605 0.5385 1.0159 -0.0096 0.1965  0.0459  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5486 0.5247 0.9684 -0.0091 0.2063  0.0424  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5508 0.5269 0.9675 -0.0073 0.2273  0.0445  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.5383 0.5120 0.9316 -0.0103 0.1918  0.0365  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5383 0.5098 0.9045 -0.0104 0.1989  0.0316  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.5303 0.5019 0.8526 -0.0120 0.1949  0.0285  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5394 0.5090 0.8423 -0.0126 0.1982  0.0229  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.5526 0.5205 0.9358 -0.0101 0.1893  0.0281  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5967 0.5656 1.0374 -0.0077 0.1949  0.0311  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.5066 0.4802 0.8171 -0.0129 0.1871  0.0313  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.5140 0.4886 0.7881 -0.0142 0.1833  0.0287  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.5230 0.5002 0.7761 -0.0129 0.1987  0.0296  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.5263 0.5048 0.7896 -0.0107 0.2112  0.0356  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.5171 0.4926 0.7882 -0.0149 0.1711  0.0312  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5520 0.5232 0.8313 -0.0153 0.1541  0.0284  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5840 0.5517 0.8561 -0.0157 0.1502  0.0251  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5348 0.5054 0.8267 -0.0150 0.1446  0.0294  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.5274 0.5049 0.7522 -0.0140 0.1981  0.0235  52  THR   A N   
356  C CA  . THR   A 46  ? 0.5443 0.5242 0.7429 -0.0122 0.2080  0.0226  52  THR   A CA  
357  C C   . THR   A 46  ? 0.5372 0.5212 0.7160 -0.0128 0.1989  0.0250  52  THR   A C   
358  O O   . THR   A 46  ? 0.5293 0.5135 0.7036 -0.0155 0.1872  0.0211  52  THR   A O   
359  C CB  . THR   A 46  ? 0.5872 0.5648 0.7711 -0.0131 0.2110  0.0120  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5992 0.5731 0.8005 -0.0114 0.2233  0.0103  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6104 0.5907 0.7605 -0.0117 0.2140  0.0078  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5336 0.5203 0.7019 -0.0099 0.2052  0.0322  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.5378 0.5287 0.6896 -0.0097 0.1971  0.0352  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5266 0.5201 0.6485 -0.0093 0.1953  0.0279  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5292 0.5212 0.6358 -0.0066 0.2051  0.0253  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.5544 0.5466 0.7097 -0.0060 0.2039  0.0476  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.5631 0.5528 0.7543 -0.0066 0.2059  0.0536  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.5640 0.5606 0.7052 -0.0054 0.1948  0.0510  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.5722 0.5608 0.7796 -0.0103 0.1905  0.0485  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4941 0.4911 0.6084 -0.0117 0.1830  0.0237  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4804 0.4808 0.5720 -0.0118 0.1783  0.0157  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4693 0.4733 0.5390 -0.0066 0.1806  0.0224  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4612 0.4666 0.5360 -0.0043 0.1809  0.0336  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4737 0.4774 0.5697 -0.0156 0.1659  0.0111  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4752 0.4798 0.5198 -0.0042 0.1815  0.0156  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4927 0.5000 0.5098 0.0018  0.1810  0.0216  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5095 0.5221 0.5112 0.0005  0.1662  0.0091  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5303 0.5411 0.5124 0.0016  0.1664  -0.0026 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5326 0.5341 0.5298 0.0077  0.1973  0.0253  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5504 0.5472 0.5717 0.0081  0.2124  0.0365  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5823 0.5813 0.6216 0.0089  0.2111  0.0517  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6255 0.6200 0.6933 0.0087  0.2247  0.0597  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6335 0.6283 0.7265 0.0084  0.2254  0.0709  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.6165 0.6152 0.7082 0.0088  0.2148  0.0762  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.6307 0.6217 0.7535 0.0079  0.2365  0.0762  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4931 0.5122 0.5058 -0.0015 0.1537  0.0112  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4860 0.5112 0.4967 -0.0040 0.1389  -0.0004 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4910 0.5238 0.5122 -0.0037 0.1280  0.0069  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4796 0.5118 0.5097 -0.0018 0.1321  0.0200  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4591 0.4816 0.4918 -0.0110 0.1394  -0.0113 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4766 0.4975 0.5402 -0.0152 0.1415  -0.0029 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5040 0.5437 0.5297 -0.0059 0.1143  -0.0026 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.5077 0.5547 0.5512 -0.0065 0.1049  0.0023  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5090 0.5577 0.5798 -0.0136 0.1019  -0.0073 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5026 0.5590 0.5883 -0.0146 0.0921  -0.0092 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5391 0.5943 0.5678 -0.0009 0.0910  0.0046  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6342 0.6949 0.6581 -0.0023 0.0769  -0.0113 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6386 0.6950 0.6608 -0.0062 0.0803  -0.0244 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6835 0.7531 0.7081 0.0007  0.0615  -0.0111 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4975 0.5387 0.5765 -0.0180 0.1113  -0.0120 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4734 0.5132 0.5761 -0.0240 0.1123  -0.0179 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4510 0.4936 0.5713 -0.0243 0.1117  -0.0099 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4390 0.4802 0.5564 -0.0211 0.1148  0.0006  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4723 0.5021 0.5779 -0.0266 0.1232  -0.0187 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4889 0.5145 0.5864 -0.0283 0.1253  -0.0324 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.4263 0.4721 0.5666 -0.0281 0.1090  -0.0153 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.4257 0.4726 0.5833 -0.0284 0.1114  -0.0094 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.4246 0.4638 0.5958 -0.0328 0.1206  -0.0118 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.4013 0.4409 0.5875 -0.0335 0.1240  -0.0095 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.4455 0.5039 0.6174 -0.0275 0.1011  -0.0109 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4931 0.5571 0.6540 -0.0215 0.0941  -0.0026 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.5168 0.5919 0.6979 -0.0202 0.0838  -0.0025 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.5192 0.6028 0.6972 -0.0183 0.0702  -0.0069 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.4949 0.5701 0.6974 -0.0206 0.0896  0.0021  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.4269 0.4589 0.5927 -0.0352 0.1252  -0.0163 60  THR   A N   
416  C CA  . THR   A 54  ? 0.4267 0.4496 0.6013 -0.0383 0.1340  -0.0164 60  THR   A CA  
417  C C   . THR   A 54  ? 0.4227 0.4363 0.5832 -0.0370 0.1386  -0.0133 60  THR   A C   
418  O O   . THR   A 54  ? 0.4334 0.4478 0.5826 -0.0356 0.1366  -0.0153 60  THR   A O   
419  C CB  . THR   A 54  ? 0.4334 0.4576 0.6265 -0.0429 0.1343  -0.0251 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.4780 0.5026 0.6640 -0.0438 0.1300  -0.0335 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.4233 0.4580 0.6366 -0.0442 0.1286  -0.0285 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.4073 0.4120 0.5681 -0.0367 0.1449  -0.0079 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.4101 0.4059 0.5614 -0.0350 0.1474  -0.0041 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.4193 0.4048 0.5699 -0.0344 0.1524  0.0008  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.4224 0.4063 0.5797 -0.0358 0.1569  0.0011  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.4164 0.3943 0.5590 -0.0320 0.1517  0.0048  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.4346 0.4012 0.5705 -0.0300 0.1538  0.0096  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.4293 0.3931 0.5572 -0.0264 0.1484  0.0123  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.4345 0.4013 0.5660 -0.0260 0.1448  0.0119  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.4582 0.4170 0.5969 -0.0306 0.1558  0.0105  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.4801 0.4262 0.6073 -0.0269 0.1556  0.0170  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.4441 0.4043 0.5948 -0.0344 0.1617  0.0069  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.4255 0.3834 0.5440 -0.0238 0.1485  0.0143  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.4224 0.3767 0.5356 -0.0205 0.1418  0.0148  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.4376 0.3789 0.5366 -0.0170 0.1387  0.0168  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.4462 0.3803 0.5351 -0.0163 0.1444  0.0193  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.4281 0.3868 0.5424 -0.0195 0.1417  0.0134  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.4489 0.4006 0.5519 -0.0173 0.1465  0.0129  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.4641 0.4177 0.5697 -0.0189 0.1555  0.0136  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.4687 0.4118 0.5603 -0.0134 0.1426  0.0109  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.4901 0.4373 0.5872 -0.0165 0.1630  0.0136  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.4946 0.4303 0.5731 -0.0106 0.1489  0.0096  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.5067 0.4443 0.5877 -0.0120 0.1605  0.0117  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.5481 0.4777 0.6173 -0.0090 0.1702  0.0112  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.4480 0.3857 0.5466 -0.0145 0.1294  0.0161  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.4554 0.3806 0.5384 -0.0102 0.1227  0.0171  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4615 0.3811 0.5300 -0.0068 0.1201  0.0131  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.4590 0.3832 0.5379 -0.0070 0.1156  0.0091  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.4386 0.3631 0.5335 -0.0090 0.1117  0.0171  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4618 0.3736 0.5399 -0.0037 0.1012  0.0178  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4965 0.3983 0.5555 -0.0011 0.1045  0.0233  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4821 0.3909 0.5623 -0.0008 0.0876  0.0131  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5199 0.4087 0.5571 0.0051  0.0942  0.0249  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5096 0.4060 0.5694 0.0050  0.0756  0.0122  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5391 0.4254 0.5758 0.0083  0.0784  0.0188  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5917 0.4649 0.6043 0.0152  0.0652  0.0191  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4740 0.3822 0.5183 -0.0031 0.1234  0.0145  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4890 0.3892 0.5143 0.0011  0.1227  0.0096  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5132 0.3994 0.5151 0.0072  0.1103  0.0086  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5408 0.4167 0.5205 0.0106  0.1142  0.0144  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5200 0.4174 0.5338 0.0015  0.1388  0.0121  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5520 0.4360 0.5363 0.0080  0.1423  0.0062  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5041 0.3896 0.5120 0.0089  0.0949  0.0016  66  SER   A N   
464  C CA  . SER   A 60  ? 0.5263 0.3992 0.5136 0.0150  0.0792  -0.0006 66  SER   A CA  
465  C C   . SER   A 60  ? 0.5408 0.3976 0.4860 0.0221  0.0807  -0.0037 66  SER   A C   
466  O O   . SER   A 60  ? 0.5560 0.4004 0.4744 0.0281  0.0720  -0.0009 66  SER   A O   
467  C CB  . SER   A 60  ? 0.5399 0.4162 0.5489 0.0148  0.0615  -0.0088 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.5968 0.4745 0.6104 0.0143  0.0629  -0.0177 66  SER   A OG  
469  N N   . SER   A 61  ? 0.5376 0.3940 0.4761 0.0219  0.0927  -0.0087 67  SER   A N   
470  C CA  . SER   A 61  ? 0.5659 0.4071 0.4650 0.0287  0.0990  -0.0123 67  SER   A CA  
471  C C   . SER   A 61  ? 0.5932 0.4256 0.4664 0.0315  0.1149  0.0000  67  SER   A C   
472  O O   . SER   A 61  ? 0.6265 0.4435 0.4611 0.0385  0.1220  -0.0003 67  SER   A O   
473  C CB  . SER   A 61  ? 0.5682 0.4126 0.4751 0.0274  0.1091  -0.0207 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.5749 0.4303 0.5022 0.0222  0.1277  -0.0141 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.5766 0.4176 0.4713 0.0265  0.1214  0.0103  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.5966 0.4308 0.4776 0.0279  0.1357  0.0228  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.6021 0.4360 0.4905 0.0276  0.1262  0.0314  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6138 0.4406 0.4926 0.0292  0.1372  0.0427  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.6026 0.4482 0.5101 0.0212  0.1555  0.0261  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6237 0.4683 0.5252 0.0223  0.1689  0.0203  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.6646 0.4909 0.5270 0.0299  0.1836  0.0256  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.6984 0.5238 0.5584 0.0311  0.1986  0.0195  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.7258 0.5441 0.5660 0.0359  0.1932  0.0082  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.7411 0.5525 0.5617 0.0399  0.1717  0.0011  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.7184 0.5368 0.5623 0.0367  0.2084  0.0028  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.6003 0.4420 0.5101 0.0255  0.1076  0.0268  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6104 0.4547 0.5376 0.0244  0.0988  0.0335  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5923 0.4435 0.5403 0.0185  0.1162  0.0417  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5967 0.4412 0.5412 0.0203  0.1195  0.0516  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6610 0.4891 0.5571 0.0332  0.0865  0.0398  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.7176 0.5404 0.5995 0.0387  0.0636  0.0298  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.7744 0.5801 0.6204 0.0486  0.0503  0.0367  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8052 0.6043 0.6331 0.0546  0.0268  0.0249  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.8230 0.6041 0.6004 0.0646  0.0197  0.0237  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.8432 0.6107 0.5821 0.0699  0.0370  0.0355  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.7986 0.5747 0.5635 0.0694  -0.0039 0.0102  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5666 0.4301 0.5351 0.0121  0.1275  0.0373  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.5589 0.4289 0.5469 0.0066  0.1429  0.0422  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.5359 0.4234 0.5557 -0.0007 0.1434  0.0354  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.5410 0.4346 0.5641 -0.0013 0.1384  0.0284  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5910 0.4544 0.5631 0.0080  0.1607  0.0457  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6721 0.5370 0.6614 0.0040  0.1764  0.0529  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7633 0.6157 0.7328 0.0079  0.1944  0.0606  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8235 0.6815 0.8217 0.0020  0.2113  0.0646  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8549 0.7150 0.8745 -0.0015 0.2080  0.0684  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.5221 0.4167 0.5642 -0.0057 0.1495  0.0375  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.5078 0.4178 0.5760 -0.0120 0.1507  0.0317  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.5188 0.4326 0.5942 -0.0153 0.1642  0.0318  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.5379 0.4450 0.6141 -0.0156 0.1733  0.0374  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.4959 0.4091 0.5822 -0.0145 0.1480  0.0322  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.5070 0.4180 0.5943 -0.0115 0.1353  0.0323  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.5170 0.4378 0.6202 -0.0136 0.1299  0.0272  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.5243 0.4242 0.5995 -0.0063 0.1269  0.0371  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.5168 0.4330 0.6217 -0.0101 0.1191  0.0286  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.5311 0.4350 0.6190 -0.0056 0.1153  0.0340  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.4982 0.4220 0.5811 -0.0175 0.1656  0.0266  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.4937 0.4226 0.5883 -0.0205 0.1768  0.0260  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.4773 0.4214 0.5955 -0.0259 0.1744  0.0202  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.4651 0.4173 0.5856 -0.0261 0.1666  0.0166  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.5001 0.4287 0.5863 -0.0179 0.1804  0.0245  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.5341 0.4468 0.5930 -0.0119 0.1855  0.0287  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.5657 0.4694 0.6192 -0.0106 0.2003  0.0351  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5574 0.4638 0.5962 -0.0072 0.1765  0.0259  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.6032 0.4907 0.6257 -0.0039 0.2063  0.0397  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5947 0.4856 0.6035 -0.0008 0.1800  0.0282  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6288 0.5098 0.6266 0.0012  0.1954  0.0355  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6731 0.5371 0.6353 0.0087  0.2000  0.0383  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.4719 0.4192 0.6075 -0.0298 0.1814  0.0194  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.4674 0.4288 0.6228 -0.0343 0.1772  0.0122  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.4673 0.4375 0.6298 -0.0342 0.1778  0.0102  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.4772 0.4434 0.6426 -0.0333 0.1874  0.0133  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.4766 0.4367 0.6509 -0.0383 0.1842  0.0109  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.4966 0.4434 0.6638 -0.0358 0.1958  0.0196  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.4804 0.4180 0.6190 -0.0300 0.1931  0.0250  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.4452 0.4266 0.6110 -0.0346 0.1688  0.0062  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.4396 0.4297 0.6141 -0.0337 0.1678  0.0054  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.4235 0.4276 0.6104 -0.0358 0.1586  0.0003  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.4138 0.4204 0.5959 -0.0369 0.1525  -0.0030 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.4669 0.4535 0.6263 -0.0294 0.1651  0.0084  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.4940 0.4675 0.6402 -0.0263 0.1735  0.0116  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.4698 0.4561 0.6185 -0.0284 0.1568  0.0086  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.4016 0.4145 0.6044 -0.0357 0.1577  -0.0006 75  SER   A N   
543  C CA  . SER   A 69  ? 0.4082 0.4344 0.6193 -0.0356 0.1466  -0.0037 75  SER   A CA  
544  C C   . SER   A 69  ? 0.4196 0.4466 0.6218 -0.0311 0.1442  0.0019  75  SER   A C   
545  O O   . SER   A 69  ? 0.4339 0.4551 0.6366 -0.0292 0.1516  0.0050  75  SER   A O   
546  C CB  . SER   A 69  ? 0.4391 0.4750 0.6785 -0.0378 0.1457  -0.0074 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.5006 0.5349 0.7543 -0.0423 0.1495  -0.0125 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.4020 0.4356 0.5973 -0.0291 0.1350  0.0030  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.3867 0.4206 0.5776 -0.0249 0.1333  0.0093  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.3959 0.4414 0.5912 -0.0223 0.1231  0.0116  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.4048 0.4567 0.5966 -0.0233 0.1155  0.0077  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.3982 0.4229 0.5716 -0.0234 0.1354  0.0125  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.4044 0.4290 0.5657 -0.0245 0.1327  0.0109  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.4025 0.4211 0.5602 -0.0276 0.1362  0.0064  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.4156 0.4448 0.5688 -0.0219 0.1280  0.0145  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.4200 0.4378 0.5685 -0.0283 0.1350  0.0040  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.4243 0.4522 0.5650 -0.0223 0.1281  0.0125  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.4066 0.4292 0.5462 -0.0256 0.1314  0.0064  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.3942 0.4422 0.5975 -0.0187 0.1223  0.0174  77  SER   A N   
560  C CA  . SER   A 71  ? 0.4123 0.4706 0.6197 -0.0151 0.1122  0.0219  77  SER   A CA  
561  C C   . SER   A 71  ? 0.4313 0.4876 0.6166 -0.0122 0.1093  0.0277  77  SER   A C   
562  O O   . SER   A 71  ? 0.4374 0.4849 0.6111 -0.0130 0.1158  0.0285  77  SER   A O   
563  C CB  . SER   A 71  ? 0.4242 0.4846 0.6503 -0.0117 0.1136  0.0273  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.4554 0.5055 0.6758 -0.0103 0.1214  0.0308  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.4436 0.5080 0.6231 -0.0085 0.0995  0.0317  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.4593 0.5216 0.6169 -0.0045 0.0989  0.0391  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.4548 0.5118 0.6179 -0.0010 0.1052  0.0503  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.4461 0.5047 0.6291 0.0001  0.1052  0.0530  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.4873 0.5590 0.6338 -0.0003 0.0858  0.0406  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.5458 0.6204 0.6826 -0.0038 0.0798  0.0274  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.6119 0.6939 0.7309 0.0008  0.0653  0.0264  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6711 0.7525 0.7775 -0.0028 0.0620  0.0117  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7130 0.8022 0.8039 0.0013  0.0445  0.0064  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.4620 0.5124 0.6118 0.0005  0.1117  0.0562  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.4636 0.5086 0.6244 0.0034  0.1179  0.0664  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.4678 0.5181 0.6407 0.0087  0.1129  0.0767  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.4721 0.5286 0.6331 0.0132  0.1058  0.0832  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.4814 0.5210 0.6263 0.0050  0.1247  0.0723  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4950 0.5341 0.6249 0.0010  0.1248  0.0614  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.4665 0.5137 0.5945 -0.0002 0.1147  0.0535  79  PRO   A CD  
581  N N   A SER   A 74  ? 0.4630 0.5104 0.6589 0.0087  0.1160  0.0777  80  SER   A N   
582  N N   B SER   A 74  ? 0.4641 0.5116 0.6602 0.0086  0.1159  0.0775  80  SER   A N   
583  C CA  A SER   A 74  ? 0.4717 0.5238 0.6850 0.0137  0.1118  0.0866  80  SER   A CA  
584  C CA  B SER   A 74  ? 0.4737 0.5258 0.6875 0.0136  0.1118  0.0864  80  SER   A CA  
585  C C   A SER   A 74  ? 0.4771 0.5212 0.7118 0.0150  0.1194  0.0916  80  SER   A C   
586  C C   B SER   A 74  ? 0.4780 0.5222 0.7140 0.0147  0.1193  0.0904  80  SER   A C   
587  O O   A SER   A 74  ? 0.4791 0.5145 0.7146 0.0119  0.1262  0.0869  80  SER   A O   
588  O O   B SER   A 74  ? 0.4802 0.5158 0.7182 0.0111  0.1258  0.0838  80  SER   A O   
589  C CB  A SER   A 74  ? 0.4858 0.5455 0.7142 0.0122  0.1058  0.0787  80  SER   A CB  
590  C CB  B SER   A 74  ? 0.4908 0.5513 0.7180 0.0124  0.1050  0.0789  80  SER   A CB  
591  O OG  A SER   A 74  ? 0.5275 0.5917 0.7445 0.0081  0.1015  0.0683  80  SER   A OG  
592  O OG  B SER   A 74  ? 0.5362 0.6050 0.7486 0.0120  0.0955  0.0753  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.4760 0.5231 0.7303 0.0199  0.1170  0.1006  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.4913 0.5311 0.7710 0.0215  0.1234  0.1042  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.4916 0.5321 0.7901 0.0196  0.1237  0.0927  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.4922 0.5414 0.8006 0.0219  0.1179  0.0940  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.4956 0.5377 0.7864 0.0287  0.1214  0.1224  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.5180 0.5520 0.8389 0.0309  0.1284  0.1277  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.5255 0.5491 0.8462 0.0279  0.1370  0.1265  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.5213 0.5584 0.8540 0.0388  0.1259  0.1475  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.4919 0.5232 0.7928 0.0157  0.1301  0.0807  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.4957 0.5251 0.8068 0.0141  0.1335  0.0685  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.5000 0.5185 0.8294 0.0151  0.1399  0.0634  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.4820 0.4916 0.8075 0.0137  0.1417  0.0610  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.5168 0.5437 0.8052 0.0087  0.1351  0.0567  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.5360 0.5732 0.8096 0.0072  0.1287  0.0591  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.5272 0.5487 0.8210 0.0075  0.1418  0.0448  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.5578 0.5920 0.8121 0.0022  0.1308  0.0493  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.5051 0.5241 0.8564 0.0177  0.1432  0.0602  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.5191 0.5265 0.8865 0.0189  0.1496  0.0521  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.5236 0.5208 0.8694 0.0153  0.1538  0.0360  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.5412 0.5404 0.8732 0.0135  0.1566  0.0300  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.5170 0.5269 0.9131 0.0230  0.1537  0.0518  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.5372 0.5348 0.9534 0.0251  0.1596  0.0450  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.5479 0.5419 0.9822 0.0272  0.1576  0.0541  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.5554 0.5434 0.9711 0.0252  0.1680  0.0287  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.5585 0.5406 1.0151 0.0288  0.1624  0.0461  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.5645 0.5401 0.9972 0.0273  0.1725  0.0198  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.5585 0.5315 1.0137 0.0289  0.1690  0.0280  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.5112 0.4972 0.8542 0.0144  0.1535  0.0300  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.5193 0.4943 0.8399 0.0120  0.1547  0.0153  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.5336 0.4961 0.8679 0.0146  0.1581  0.0035  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.5291 0.4888 0.8881 0.0160  0.1564  0.0065  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.5154 0.4883 0.8206 0.0088  0.1482  0.0168  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.5329 0.4942 0.8146 0.0073  0.1469  0.0023  84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.5114 0.4956 0.8035 0.0067  0.1457  0.0275  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.5507 0.5044 0.8678 0.0154  0.1636  -0.0104 85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.5702 0.5101 0.8937 0.0184  0.1672  -0.0250 85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.5743 0.5041 0.8965 0.0172  0.1580  -0.0329 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.5727 0.5045 0.8815 0.0141  0.1502  -0.0292 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.6248 0.5563 0.9222 0.0203  0.1764  -0.0375 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.7112 0.6507 1.0227 0.0222  0.1880  -0.0326 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.8074 0.7488 1.1582 0.0257  0.1921  -0.0309 85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.8163 0.7718 1.1922 0.0260  0.1912  -0.0169 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.8372 0.7656 1.1940 0.0287  0.1954  -0.0438 85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.5696 0.4882 0.9083 0.0199  0.1587  -0.0452 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.5808 0.4889 0.9246 0.0189  0.1487  -0.0557 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.6067 0.5064 0.9105 0.0181  0.1415  -0.0677 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.6261 0.5219 0.8973 0.0199  0.1473  -0.0732 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.5727 0.4691 0.9405 0.0223  0.1513  -0.0699 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.6075 0.5047 0.9157 0.0156  0.1293  -0.0699 87  SER   A N   
642  C CA  . SER   A 81  ? 0.6372 0.5258 0.9135 0.0153  0.1186  -0.0813 87  SER   A CA  
643  C C   . SER   A 81  ? 0.6499 0.5285 0.9486 0.0152  0.1056  -0.0956 87  SER   A C   
644  O O   . SER   A 81  ? 0.6412 0.5195 0.9791 0.0152  0.1078  -0.0957 87  SER   A O   
645  C CB  . SER   A 81  ? 0.6514 0.5503 0.9164 0.0116  0.1147  -0.0675 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.6653 0.5689 0.9602 0.0085  0.1070  -0.0611 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.6661 0.5368 0.9437 0.0153  0.0913  -0.1072 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.6728 0.5355 0.9770 0.0147  0.0764  -0.1211 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.6527 0.5265 1.0025 0.0098  0.0739  -0.1064 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.6425 0.5121 1.0308 0.0085  0.0664  -0.1138 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.7349 0.5859 1.0049 0.0170  0.0591  -0.1384 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.8333 0.6905 1.0768 0.0155  0.0540  -0.1276 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.9494 0.7980 1.1783 0.0169  0.0321  -0.1413 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.9594 0.8067 1.2259 0.0149  0.0182  -0.1494 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.9928 0.8356 1.1746 0.0203  0.0285  -0.1431 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.6398 0.5270 0.9857 0.0072  0.0813  -0.0857 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.6155 0.5128 0.9960 0.0034  0.0822  -0.0699 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.5958 0.5010 1.0081 0.0032  0.0960  -0.0530 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.5899 0.4979 1.0407 0.0013  0.0970  -0.0442 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.6215 0.5271 0.9764 0.0016  0.0822  -0.0587 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.6395 0.5377 0.9667 0.0023  0.0676  -0.0721 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.6632 0.5573 0.9429 0.0049  0.0685  -0.0764 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.6426 0.5374 0.9928 0.0009  0.0529  -0.0798 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.6847 0.5709 0.9363 0.0066  0.0549  -0.0866 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.6666 0.5548 0.9913 0.0024  0.0372  -0.0913 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.6958 0.5793 0.9689 0.0056  0.0382  -0.0941 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.7302 0.6062 0.9760 0.0081  0.0224  -0.1034 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.5829 0.4915 0.9807 0.0055  0.1068  -0.0472 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.5618 0.4777 0.9871 0.0064  0.1180  -0.0303 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.5803 0.4922 1.0058 0.0100  0.1245  -0.0367 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.6019 0.5107 0.9941 0.0116  0.1255  -0.0467 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.5402 0.4698 0.9479 0.0058  0.1249  -0.0103 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.5179 0.4526 0.9221 0.0027  0.1219  -0.0020 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.5038 0.4403 0.9421 0.0017  0.1243  0.0090  90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.5237 0.4614 0.8928 0.0012  0.1186  -0.0041 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.5003 0.4413 0.9373 -0.0007 0.1239  0.0166  90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.5221 0.4643 0.8904 -0.0013 0.1169  0.0031  90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.5144 0.4583 0.9165 -0.0022 0.1197  0.0128  90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.5091 0.4568 0.9125 -0.0043 0.1200  0.0194  90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.5637 0.4767 1.0260 0.0119  0.1313  -0.0282 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.5606 0.4720 1.0249 0.0158  0.1392  -0.0316 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.5587 0.4829 1.0001 0.0167  0.1456  -0.0171 91  PRO   A C   
683  O O   . PRO   A 85  ? 0.5685 0.5018 0.9923 0.0144  0.1436  -0.0054 91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.5579 0.4673 1.0721 0.0175  0.1435  -0.0236 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.5557 0.4717 1.0867 0.0150  0.1424  -0.0054 91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.5481 0.4641 1.0514 0.0111  0.1338  -0.0126 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.5505 0.4756 0.9946 0.0201  0.1531  -0.0186 92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.5482 0.4861 0.9773 0.0210  0.1578  -0.0062 92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.5239 0.4733 0.9726 0.0215  0.1572  0.0169  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.5167 0.4636 0.9999 0.0238  0.1589  0.0240  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.5566 0.4929 0.9936 0.0248  0.1665  -0.0128 92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.5074 0.4674 0.9332 0.0196  0.1545  0.0281  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.4949 0.4638 0.9312 0.0209  0.1537  0.0494  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.5047 0.4862 0.9133 0.0201  0.1511  0.0589  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.5171 0.5000 0.9003 0.0175  0.1500  0.0490  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.4983 0.4614 0.9446 0.0186  0.1521  0.0523  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.5279 0.4940 0.9450 0.0146  0.1485  0.0523  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.5314 0.4880 0.9525 0.0112  0.1447  0.0401  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.5142 0.4745 0.9171 0.0082  0.1427  0.0447  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.5225 0.4859 0.8924 0.0060  0.1395  0.0389  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.4706 0.4344 0.8205 0.0064  0.1389  0.0300  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.4872 0.4532 0.8462 0.0035  0.1384  0.0428  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.4960 0.4857 0.9085 0.0226  0.1500  0.0780  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.5078 0.5082 0.8932 0.0221  0.1461  0.0856  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.4975 0.4955 0.8629 0.0184  0.1459  0.0855  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.5045 0.4990 0.8811 0.0193  0.1489  0.0952  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.5180 0.5272 0.9113 0.0277  0.1439  0.1054  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.5377 0.5526 0.9484 0.0312  0.1419  0.1052  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.5543 0.5780 0.9520 0.0299  0.1378  0.0985  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.5446 0.5556 0.9897 0.0355  0.1452  0.1105  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.5643 0.5938 0.9836 0.0330  0.1368  0.0980  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.5537 0.5701 1.0191 0.0391  0.1441  0.1101  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.5715 0.5974 1.0244 0.0377  0.1400  0.1038  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.5889 0.6206 1.0675 0.0412  0.1398  0.1035  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.4792 0.4782 0.8188 0.0144  0.1436  0.0744  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.4690 0.4663 0.7909 0.0110  0.1432  0.0736  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.4528 0.4602 0.7533 0.0120  0.1414  0.0839  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.4484 0.4632 0.7388 0.0123  0.1377  0.0818  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.4852 0.4766 0.7911 0.0068  0.1413  0.0567  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.4880 0.4785 0.7790 0.0037  0.1404  0.0567  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.5064 0.4883 0.7897 0.0006  0.1372  0.0424  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.5009 0.4746 0.7944 0.0010  0.1355  0.0326  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.5007 0.4836 0.7662 -0.0019 0.1358  0.0409  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.4405 0.4480 0.7362 0.0130  0.1443  0.0946  96  SER   A N   
725  C CA  . SER   A 90  ? 0.4450 0.4603 0.7170 0.0149  0.1428  0.1038  96  SER   A CA  
726  C C   . SER   A 90  ? 0.4472 0.4628 0.6951 0.0107  0.1426  0.0953  96  SER   A C   
727  O O   . SER   A 90  ? 0.4529 0.4621 0.7048 0.0068  0.1444  0.0861  96  SER   A O   
728  C CB  . SER   A 90  ? 0.4567 0.4712 0.7336 0.0200  0.1484  0.1224  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.4595 0.4669 0.7437 0.0180  0.1562  0.1237  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.4452 0.4679 0.6692 0.0118  0.1396  0.0980  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.4519 0.4752 0.6537 0.0084  0.1397  0.0904  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.4499 0.4706 0.6529 0.0029  0.1373  0.0748  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.4634 0.4796 0.6605 -0.0003 0.1396  0.0686  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.4724 0.4902 0.6720 0.0088  0.1484  0.0966  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.5014 0.5202 0.6956 0.0149  0.1537  0.1135  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.5374 0.5593 0.7028 0.0178  0.1550  0.1179  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.5098 0.5261 0.7224 0.0191  0.1580  0.1270  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.5482 0.5688 0.7119 0.0242  0.1607  0.1349  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.5310 0.5484 0.7245 0.0250  0.1628  0.1417  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.4306 0.4535 0.6423 0.0026  0.1336  0.0697  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.4297 0.4486 0.6411 -0.0012 0.1335  0.0571  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.4273 0.4531 0.6294 -0.0031 0.1301  0.0515  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.4305 0.4647 0.6376 -0.0010 0.1258  0.0551  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.4387 0.4524 0.6688 -0.0001 0.1351  0.0540  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.4537 0.4602 0.6798 -0.0026 0.1367  0.0415  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.4604 0.4575 0.6810 -0.0044 0.1366  0.0365  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.4665 0.4700 0.7086 -0.0003 0.1391  0.0380  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.4016 0.4234 0.5939 -0.0069 0.1316  0.0428  99  MET   A N   
749  C CA  . MET   A 93  ? 0.3838 0.4103 0.5712 -0.0096 0.1301  0.0367  99  MET   A CA  
750  C C   . MET   A 93  ? 0.4058 0.4256 0.5968 -0.0113 0.1350  0.0295  99  MET   A C   
751  O O   . MET   A 93  ? 0.4238 0.4338 0.6088 -0.0117 0.1377  0.0267  99  MET   A O   
752  C CB  . MET   A 93  ? 0.3843 0.4101 0.5559 -0.0122 0.1298  0.0338  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.3989 0.4283 0.5611 -0.0097 0.1280  0.0405  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.4582 0.4845 0.6040 -0.0124 0.1304  0.0357  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.4349 0.4506 0.5868 -0.0130 0.1359  0.0368  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.3870 0.4116 0.5877 -0.0119 0.1363  0.0266  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.3955 0.4127 0.5976 -0.0128 0.1441  0.0209  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.3845 0.4021 0.5829 -0.0164 0.1472  0.0167  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.3673 0.3944 0.5723 -0.0183 0.1425  0.0164  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.3995 0.4207 0.6220 -0.0103 0.1473  0.0213  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.4389 0.4586 0.6708 -0.0063 0.1459  0.0252  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.4507 0.4731 0.7044 -0.0038 0.1508  0.0244  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.4567 0.4634 0.6762 -0.0057 0.1481  0.0218  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.3853 0.3920 0.5739 -0.0170 0.1550  0.0134  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.3911 0.3958 0.5791 -0.0200 0.1613  0.0110  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.4090 0.4038 0.5945 -0.0180 0.1735  0.0096  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.4179 0.4046 0.5938 -0.0146 0.1753  0.0086  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.3769 0.3751 0.5479 -0.0219 0.1593  0.0106  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.4123 0.4075 0.6075 -0.0200 0.1825  0.0092  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.4338 0.4176 0.6224 -0.0177 0.1972  0.0092  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.4729 0.4428 0.6326 -0.0169 0.1987  0.0104  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.4776 0.4476 0.6369 -0.0201 0.1975  0.0120  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.4310 0.4201 0.6451 -0.0199 0.2084  0.0098  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.4588 0.4336 0.6616 -0.0167 0.2273  0.0113  102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.4165 0.4204 0.6623 -0.0199 0.2044  0.0086  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.5010 0.4586 0.6378 -0.0125 0.2000  0.0090  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.5374 0.4811 0.6454 -0.0106 0.1990  0.0103  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.5597 0.4906 0.6431 -0.0050 0.1973  0.0063  103 GLY   A C   
779  O O   . GLY   A 97  ? 0.5574 0.4908 0.6483 -0.0033 0.1957  0.0019  103 GLY   A O   
780  N N   . HIS   A 98  ? 0.5667 0.4834 0.6211 -0.0019 0.1963  0.0076  104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.5862 0.4896 0.6141 0.0039  0.1919  0.0020  104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.5726 0.4789 0.6037 0.0033  0.1734  -0.0021 104 HIS   A C   
783  O O   . HIS   A 98  ? 0.5666 0.4787 0.6060 0.0000  0.1650  0.0015  104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.6166 0.5021 0.6083 0.0091  0.1975  0.0053  104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.6576 0.5284 0.6176 0.0158  0.1900  -0.0022 104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.6754 0.5398 0.6265 0.0200  0.1980  -0.0099 104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.6826 0.5450 0.6216 0.0188  0.1739  -0.0045 104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.6920 0.5436 0.6146 0.0254  0.1861  -0.0175 104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.6995 0.5499 0.6150 0.0249  0.1704  -0.0145 104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.5638 0.4652 0.5903 0.0066  0.1683  -0.0100 105 SER   A N   
791  C CA  . SER   A 99  ? 0.5635 0.4658 0.5960 0.0064  0.1517  -0.0147 105 SER   A CA  
792  C C   . SER   A 99  ? 0.5875 0.4787 0.6076 0.0114  0.1477  -0.0256 105 SER   A C   
793  O O   . SER   A 99  ? 0.5955 0.4833 0.6130 0.0138  0.1590  -0.0295 105 SER   A O   
794  C CB  . SER   A 99  ? 0.5503 0.4687 0.6165 0.0015  0.1478  -0.0117 105 SER   A CB  
795  O OG  . SER   A 99  ? 0.5546 0.4790 0.6385 0.0015  0.1543  -0.0134 105 SER   A OG  
796  N N   . GLU   A 100 ? 0.5909 0.4758 0.6040 0.0131  0.1318  -0.0311 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.6122 0.4860 0.6151 0.0176  0.1229  -0.0439 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.6113 0.4918 0.6442 0.0147  0.1073  -0.0473 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.6108 0.5010 0.6615 0.0106  0.1026  -0.0393 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.6592 0.5156 0.6190 0.0240  0.1170  -0.0483 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.7259 0.5740 0.6559 0.0275  0.1355  -0.0431 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.8044 0.6339 0.6863 0.0350  0.1318  -0.0444 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.8537 0.6727 0.7176 0.0397  0.1157  -0.0559 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.7847 0.6096 0.6471 0.0366  0.1448  -0.0339 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.6135 0.4885 0.6548 0.0167  0.1000  -0.0591 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.5951 0.4764 0.6714 0.0136  0.0869  -0.0612 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.5793 0.4639 0.6623 0.0116  0.0738  -0.0566 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.5550 0.4515 0.6688 0.0071  0.0740  -0.0483 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.6140 0.4831 0.6876 0.0176  0.0781  -0.0781 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.6316 0.4938 0.6834 0.0213  0.0935  -0.0822 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.6232 0.4859 0.6465 0.0218  0.1051  -0.0713 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.5746 0.4480 0.6278 0.0157  0.0631  -0.0611 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.5541 0.4290 0.6123 0.0151  0.0496  -0.0574 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.5324 0.4178 0.5973 0.0111  0.0591  -0.0425 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.5247 0.4131 0.6015 0.0100  0.0500  -0.0387 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.5184 0.4091 0.5770 0.0092  0.0768  -0.0350 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.5067 0.4078 0.5747 0.0051  0.0856  -0.0232 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.4661 0.3810 0.5710 0.0002  0.0875  -0.0186 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.4393 0.3620 0.5527 -0.0028 0.0918  -0.0108 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.5135 0.4157 0.5658 0.0046  0.1022  -0.0179 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.5529 0.4412 0.5687 0.0095  0.1041  -0.0184 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.5415 0.4234 0.5450 0.0118  0.0941  -0.0169 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.5638 0.4477 0.5642 0.0115  0.1165  -0.0192 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.4478 0.3647 0.5742 -0.0001 0.0847  -0.0233 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.4293 0.3577 0.5888 -0.0038 0.0880  -0.0168 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.4272 0.3591 0.6012 -0.0054 0.0824  -0.0125 110 CYS   A C   
827  O O   . CYS   A 104 ? 0.4428 0.3677 0.6129 -0.0035 0.0703  -0.0176 110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.4315 0.3593 0.6145 -0.0034 0.0855  -0.0217 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.4706 0.3976 0.6461 -0.0017 0.0959  -0.0242 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.4021 0.3440 0.5891 -0.0083 0.0913  -0.0034 111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.4170 0.3619 0.6178 -0.0096 0.0893  0.0007  111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.4331 0.3781 0.6148 -0.0102 0.0928  0.0040  111 GLY   A C   
833  O O   . GLY   A 105 ? 0.4435 0.3919 0.6374 -0.0113 0.0941  0.0079  111 GLY   A O   
834  N N   . GLY   A 106 ? 0.4323 0.3733 0.5871 -0.0092 0.0959  0.0027  112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.4368 0.3773 0.5764 -0.0100 0.1008  0.0063  112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.4334 0.3846 0.5823 -0.0133 0.1114  0.0113  112 GLY   A C   
837  O O   . GLY   A 106 ? 0.4430 0.4004 0.5966 -0.0142 0.1164  0.0124  112 GLY   A O   
838  N N   . ILE   A 107 ? 0.4166 0.3696 0.5689 -0.0147 0.1138  0.0139  113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.4151 0.3770 0.5733 -0.0172 0.1228  0.0167  113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.4125 0.3772 0.5573 -0.0189 0.1289  0.0162  113 ILE   A C   
841  O O   . ILE   A 107 ? 0.4190 0.3778 0.5530 -0.0189 0.1292  0.0153  113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.4317 0.3938 0.6024 -0.0176 0.1238  0.0182  113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.4468 0.4112 0.6402 -0.0167 0.1224  0.0201  113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.4358 0.4034 0.6033 -0.0197 0.1330  0.0184  113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.4626 0.4258 0.6728 -0.0164 0.1222  0.0210  113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.3991 0.3725 0.5460 -0.0202 0.1339  0.0173  114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.4108 0.3890 0.5510 -0.0222 0.1381  0.0157  114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.4234 0.4058 0.5659 -0.0235 0.1415  0.0149  114 LEU   A C   
849  O O   . LEU   A 108 ? 0.4075 0.3940 0.5539 -0.0223 0.1432  0.0175  114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.4064 0.3918 0.5474 -0.0217 0.1385  0.0168  114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.4192 0.4122 0.5583 -0.0236 0.1404  0.0145  114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.4280 0.4172 0.5657 -0.0257 0.1430  0.0113  114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.4352 0.4361 0.5779 -0.0221 0.1387  0.0171  114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.4325 0.4134 0.5729 -0.0255 0.1438  0.0114  115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.4527 0.4359 0.5947 -0.0265 0.1475  0.0083  115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.4497 0.4368 0.5888 -0.0292 0.1488  0.0022  115 ARG   A C   
857  O O   . ARG   A 109 ? 0.4456 0.4311 0.5866 -0.0310 0.1484  0.0010  115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.4975 0.4732 0.6469 -0.0262 0.1485  0.0086  115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.6109 0.5787 0.7590 -0.0267 0.1465  0.0093  115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.7185 0.6797 0.8748 -0.0265 0.1477  0.0094  115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.8033 0.7563 0.9598 -0.0236 0.1415  0.0144  115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.8652 0.8170 1.0313 -0.0213 0.1366  0.0164  115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.8775 0.8353 1.0547 -0.0215 0.1401  0.0153  115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.8788 0.8229 1.0436 -0.0183 0.1281  0.0197  115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.4474 0.4396 0.5822 -0.0292 0.1503  -0.0019 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.4629 0.4586 0.5967 -0.0317 0.1495  -0.0104 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.4806 0.4715 0.6165 -0.0323 0.1546  -0.0165 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.4902 0.4763 0.6294 -0.0305 0.1588  -0.0127 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.4697 0.4746 0.5934 -0.0303 0.1450  -0.0123 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.4297 0.4362 0.5370 -0.0258 0.1488  -0.0103 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.4936 0.4864 0.6293 -0.0345 0.1540  -0.0267 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.5288 0.5169 0.6662 -0.0347 0.1594  -0.0345 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.5475 0.5357 0.6721 -0.0305 0.1650  -0.0329 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.5708 0.5536 0.7003 -0.0297 0.1724  -0.0360 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.5643 0.5550 0.7023 -0.0375 0.1559  -0.0482 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.6178 0.6167 0.7363 -0.0352 0.1497  -0.0533 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.6819 0.6841 0.8026 -0.0379 0.1427  -0.0684 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.6985 0.7077 0.8261 -0.0399 0.1336  -0.0704 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.6738 0.6710 0.7912 -0.0379 0.1465  -0.0805 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.5398 0.5338 0.6506 -0.0275 0.1630  -0.0270 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.5357 0.5296 0.6338 -0.0230 0.1703  -0.0233 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.5478 0.5389 0.6579 -0.0211 0.1758  -0.0115 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.5749 0.5651 0.6799 -0.0175 0.1846  -0.0072 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.5234 0.5241 0.5993 -0.0199 0.1656  -0.0224 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.5129 0.5172 0.5782 -0.0213 0.1574  -0.0355 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.5340 0.5451 0.6034 -0.0234 0.1456  -0.0367 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.5364 0.5383 0.5893 -0.0207 0.1590  -0.0485 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.5441 0.5574 0.6057 -0.0243 0.1391  -0.0503 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.5510 0.5583 0.6021 -0.0229 0.1464  -0.0587 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.5232 0.5123 0.6490 -0.0232 0.1710  -0.0066 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.5063 0.4928 0.6463 -0.0216 0.1730  0.0024  119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.4910 0.4793 0.6337 -0.0217 0.1654  0.0088  119 GLY   A C   
893  O O   . GLY   A 113 ? 0.4671 0.4569 0.6052 -0.0237 0.1591  0.0066  119 GLY   A O   
894  N N   . VAL   A 114 ? 0.4856 0.4732 0.6392 -0.0197 0.1668  0.0162  120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.4834 0.4716 0.6416 -0.0194 0.1600  0.0211  120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.4660 0.4603 0.6121 -0.0180 0.1597  0.0243  120 VAL   A C   
897  O O   . VAL   A 114 ? 0.4717 0.4686 0.6124 -0.0154 0.1663  0.0287  120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.4980 0.4830 0.6771 -0.0180 0.1605  0.0264  120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.5109 0.4960 0.6949 -0.0175 0.1536  0.0296  120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.5085 0.4878 0.7010 -0.0188 0.1572  0.0234  120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.4404 0.4366 0.5826 -0.0192 0.1529  0.0229  121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.4221 0.4244 0.5574 -0.0177 0.1504  0.0261  121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.4226 0.4239 0.5696 -0.0159 0.1490  0.0329  121 VAL   A C   
904  O O   . VAL   A 115 ? 0.4258 0.4308 0.5723 -0.0131 0.1506  0.0397  121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.4273 0.4325 0.5576 -0.0201 0.1450  0.0201  121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.4264 0.4382 0.5555 -0.0184 0.1409  0.0235  121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.4278 0.4343 0.5503 -0.0221 0.1458  0.0124  121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.4095 0.4050 0.5664 -0.0170 0.1455  0.0307  122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.4171 0.4103 0.5863 -0.0156 0.1429  0.0339  122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.4123 0.3979 0.5869 -0.0164 0.1371  0.0288  122 GLY   A C   
911  O O   . GLY   A 116 ? 0.4195 0.4010 0.5898 -0.0176 0.1356  0.0250  122 GLY   A O   
912  N N   . ILE   A 117 ? 0.4022 0.3848 0.5863 -0.0151 0.1334  0.0287  123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.3978 0.3720 0.5832 -0.0147 0.1262  0.0225  123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.4043 0.3762 0.5841 -0.0135 0.1247  0.0192  123 ILE   A C   
915  O O   . ILE   A 117 ? 0.4000 0.3767 0.5875 -0.0126 0.1277  0.0228  123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.4007 0.3712 0.6080 -0.0140 0.1219  0.0226  123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.4064 0.3805 0.6325 -0.0131 0.1260  0.0283  123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.4189 0.3896 0.6345 -0.0148 0.1228  0.0241  123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.4127 0.3828 0.6688 -0.0128 0.1218  0.0275  123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.4100 0.3739 0.5764 -0.0128 0.1206  0.0128  124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.4081 0.3675 0.5673 -0.0109 0.1209  0.0081  124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.4036 0.3613 0.5811 -0.0094 0.1174  0.0062  124 VAL   A C   
923  O O   . VAL   A 118 ? 0.4053 0.3596 0.5957 -0.0092 0.1109  0.0044  124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.4192 0.3675 0.5577 -0.0092 0.1171  0.0020  124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.4286 0.3704 0.5579 -0.0064 0.1192  -0.0039 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.4181 0.3670 0.5420 -0.0107 0.1222  0.0051  124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.4111 0.3718 0.5948 -0.0084 0.1219  0.0072  125 SER   A N   
928  C CA  . SER   A 119 ? 0.4237 0.3826 0.6286 -0.0069 0.1200  0.0061  125 SER   A CA  
929  C C   . SER   A 119 ? 0.4516 0.4054 0.6538 -0.0045 0.1219  -0.0006 125 SER   A C   
930  O O   . SER   A 119 ? 0.4679 0.4152 0.6829 -0.0030 0.1181  -0.0069 125 SER   A O   
931  C CB  . SER   A 119 ? 0.4370 0.4056 0.6602 -0.0073 0.1249  0.0175  125 SER   A CB  
932  O OG  . SER   A 119 ? 0.4703 0.4369 0.7171 -0.0057 0.1249  0.0184  125 SER   A OG  
933  N N   . THR   A 120 ? 0.4599 0.4168 0.6495 -0.0043 0.1287  0.0003  126 THR   A N   
934  C CA  . THR   A 120 ? 0.4938 0.4467 0.6833 -0.0017 0.1338  -0.0053 126 THR   A CA  
935  C C   . THR   A 120 ? 0.4971 0.4464 0.6624 -0.0013 0.1400  -0.0086 126 THR   A C   
936  O O   . THR   A 120 ? 0.4769 0.4285 0.6294 -0.0034 0.1403  -0.0050 126 THR   A O   
937  C CB  . THR   A 120 ? 0.5246 0.4876 0.7373 -0.0010 0.1385  0.0024  126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.5601 0.5325 0.7678 -0.0022 0.1430  0.0081  126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.5406 0.5092 0.7735 -0.0014 0.1352  0.0113  126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.5127 0.4555 0.6738 0.0017  0.1466  -0.0151 127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.5389 0.4774 0.6803 0.0027  0.1561  -0.0169 127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.5701 0.5011 0.7107 0.0067  0.1654  -0.0243 127 GLY   A C   
943  O O   . GLY   A 121 ? 0.5598 0.4867 0.7120 0.0089  0.1628  -0.0303 127 GLY   A O   
944  N N   . GLY   A 122 ? 0.6060 0.5343 0.7345 0.0078  0.1775  -0.0241 128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.6378 0.5584 0.7647 0.0121  0.1904  -0.0308 128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.6463 0.5751 0.7866 0.0110  0.2044  -0.0246 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.6337 0.5771 0.7939 0.0068  0.2008  -0.0162 128 GLY   A O   
948  N N   . ASN   A 123 ? 0.6606 0.5797 0.7902 0.0149  0.2206  -0.0292 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.6552 0.5809 0.8025 0.0144  0.2368  -0.0242 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.6298 0.5622 0.7760 0.0098  0.2375  -0.0153 129 ASN   A C   
951  O O   . ASN   A 123 ? 0.6182 0.5621 0.7922 0.0072  0.2443  -0.0103 129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.6703 0.6107 0.8611 0.0136  0.2365  -0.0219 129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.7375 0.6707 0.9361 0.0184  0.2401  -0.0305 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.7789 0.6956 0.9530 0.0232  0.2502  -0.0398 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.7248 0.6695 0.9575 0.0178  0.2323  -0.0275 129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.6188 0.5436 0.7358 0.0090  0.2304  -0.0141 130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.5982 0.5278 0.7152 0.0049  0.2312  -0.0065 130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.5632 0.5091 0.7019 -0.0007 0.2162  -0.0022 130 GLY   A C   
959  O O   . GLY   A 124 ? 0.5535 0.5061 0.7007 -0.0048 0.2168  0.0026  130 GLY   A O   
960  N N   . LEU   A 125 ? 0.5417 0.4928 0.6882 -0.0008 0.2034  -0.0042 131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.5284 0.4926 0.6892 -0.0048 0.1902  0.0002  131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.5250 0.4834 0.6691 -0.0045 0.1782  -0.0012 131 LEU   A C   
963  O O   . LEU   A 125 ? 0.5585 0.5059 0.6895 -0.0011 0.1767  -0.0067 131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.5238 0.5011 0.7142 -0.0047 0.1862  0.0021  131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.5553 0.5396 0.7704 -0.0040 0.1961  0.0026  131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.5693 0.5640 0.8106 -0.0024 0.1896  0.0050  131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.5551 0.5487 0.7819 -0.0082 0.1974  0.0058  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.4790 0.4445 0.6254 -0.0078 0.1697  0.0029  132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.4577 0.4204 0.5965 -0.0080 0.1591  0.0028  132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.4391 0.4150 0.5970 -0.0099 0.1527  0.0080  132 VAL   A C   
971  O O   . VAL   A 126 ? 0.4260 0.4123 0.5933 -0.0120 0.1534  0.0113  132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.4609 0.4168 0.5809 -0.0093 0.1573  0.0035  132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.4603 0.4231 0.5853 -0.0128 0.1620  0.0072  132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.4506 0.4053 0.5694 -0.0096 0.1465  0.0037  132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.4289 0.4036 0.5927 -0.0086 0.1468  0.0084  133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.4270 0.4113 0.6056 -0.0090 0.1425  0.0149  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.4258 0.4084 0.6004 -0.0102 0.1375  0.0169  133 GLY   A C   
978  O O   . GLY   A 127 ? 0.4230 0.3965 0.5932 -0.0096 0.1343  0.0126  133 GLY   A O   
979  N N   . PHE   A 128 ? 0.4133 0.4044 0.5895 -0.0115 0.1366  0.0228  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.3987 0.3893 0.5729 -0.0125 0.1347  0.0254  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.4098 0.4063 0.5950 -0.0108 0.1353  0.0338  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.4084 0.4127 0.5944 -0.0096 0.1357  0.0385  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.3923 0.3862 0.5550 -0.0150 0.1358  0.0245  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.3928 0.3816 0.5459 -0.0165 0.1373  0.0189  134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.4087 0.3880 0.5537 -0.0167 0.1360  0.0159  134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.3864 0.3797 0.5400 -0.0175 0.1403  0.0175  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.4218 0.3949 0.5555 -0.0171 0.1389  0.0130  134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.4186 0.4062 0.5652 -0.0186 0.1445  0.0140  134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.4225 0.3994 0.5573 -0.0182 0.1444  0.0125  134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.4138 0.4063 0.6088 -0.0103 0.1352  0.0362  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.4081 0.4040 0.6144 -0.0082 0.1386  0.0461  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.4159 0.4162 0.6089 -0.0088 0.1420  0.0497  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.3988 0.3956 0.5904 -0.0106 0.1428  0.0463  135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.4161 0.4053 0.6425 -0.0080 0.1383  0.0461  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.4293 0.4368 0.6123 -0.0067 0.1434  0.0558  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.4423 0.4528 0.6093 -0.0064 0.1469  0.0577  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.4442 0.4511 0.6182 -0.0049 0.1552  0.0648  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.4315 0.4368 0.6204 -0.0024 0.1589  0.0737  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.4696 0.4877 0.6229 -0.0032 0.1447  0.0630  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.5286 0.5493 0.6601 -0.0027 0.1464  0.0611  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.5248 0.5443 0.6512 -0.0063 0.1454  0.0513  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.5636 0.5864 0.6823 0.0019  0.1491  0.0697  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.4435 0.4488 0.6098 -0.0061 0.1595  0.0615  137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.4575 0.4599 0.6319 -0.0042 0.1702  0.0687  137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.4799 0.4845 0.6290 -0.0017 0.1772  0.0703  137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.4826 0.4842 0.6349 -0.0001 0.1885  0.0747  137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.4471 0.4442 0.6413 -0.0072 0.1707  0.0632  137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.4350 0.4286 0.6498 -0.0089 0.1623  0.0598  137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.4612 0.4579 0.6424 -0.0099 0.1681  0.0532  137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.4743 0.4838 0.6001 -0.0017 0.1704  0.0645  138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.4736 0.4844 0.5727 0.0006  0.1741  0.0620  138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.5050 0.5162 0.5870 0.0074  0.1815  0.0749  138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.5299 0.5393 0.5893 0.0106  0.1890  0.0743  138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.4444 0.4604 0.5292 -0.0016 0.1623  0.0510  138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.4144 0.4283 0.5108 -0.0075 0.1588  0.0394  138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.4233 0.4422 0.5112 -0.0098 0.1490  0.0294  138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.4293 0.4535 0.5239 -0.0093 0.1410  0.0330  138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.4500 0.4799 0.5447 -0.0110 0.1321  0.0266  138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.4521 0.4832 0.5404 -0.0136 0.1293  0.0157  138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.4235 0.4582 0.5285 -0.0101 0.1265  0.0306  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.5028 0.5151 0.5947 0.0102  0.1805  0.0867  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.5217 0.5329 0.5985 0.0175  0.1885  0.1020  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.5351 0.5394 0.6276 0.0195  0.2067  0.1132  139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.5676 0.5692 0.6440 0.0261  0.2178  0.1267  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.5297 0.5446 0.6131 0.0204  0.1804  0.1118  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.5642 0.5768 0.6856 0.0173  0.1810  0.1149  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.5614 0.5729 0.7002 0.0113  0.1775  0.1032  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.5787 0.5901 0.7117 0.0213  0.1842  0.1287  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.5201 0.5215 0.6447 0.0144  0.2096  0.1084  140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.5228 0.5186 0.6727 0.0153  0.2256  0.1178  140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.5295 0.5222 0.6657 0.0166  0.2390  0.1148  140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.5196 0.5108 0.6748 0.0124  0.2402  0.1057  140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.5134 0.5079 0.7038 0.0095  0.2194  0.1114  140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.5285 0.5249 0.7323 0.0080  0.2065  0.1109  140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.5310 0.5249 0.7676 0.0029  0.1991  0.1016  140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.5361 0.5314 0.7470 0.0131  0.2133  0.1278  140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.5424 0.5339 0.6420 0.0230  0.2474  0.1211  141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.5771 0.5650 0.6558 0.0252  0.2602  0.1163  141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.5858 0.5682 0.6948 0.0254  0.2807  0.1225  141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.5855 0.5654 0.6934 0.0245  0.2892  0.1139  141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.6115 0.5977 0.6421 0.0335  0.2655  0.1234  141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.6500 0.6421 0.6492 0.0349  0.2455  0.1178  141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.6888 0.6775 0.6368 0.0436  0.2513  0.1210  141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.6580 0.6552 0.6613 0.0274  0.2282  0.0968  141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.5873 0.5678 0.7274 0.0264  0.2887  0.1373  142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.5903 0.5663 0.7684 0.0264  0.3080  0.1448  142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.5908 0.5686 0.8090 0.0191  0.2999  0.1314  142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.5805 0.5555 0.8317 0.0188  0.3145  0.1346  142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.5839 0.5574 0.7890 0.0290  0.3167  0.1636  142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.5721 0.5495 0.7982 0.0249  0.2967  0.1614  142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.5864 0.5661 0.7908 0.0274  0.2858  0.1665  142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.5565 0.5353 0.8298 0.0181  0.2855  0.1529  142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.5810 0.5631 0.8170 0.0225  0.2707  0.1617  142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.5611 0.5421 0.8375 0.0169  0.2700  0.1531  142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.5472 0.5254 0.8617 0.0135  0.2867  0.1455  142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.5517 0.5333 0.8648 0.0114  0.2559  0.1441  142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.5408 0.5200 0.8927 0.0083  0.2709  0.1377  142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.5396 0.5200 0.8887 0.0073  0.2562  0.1366  142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.6011 0.5832 0.8172 0.0137  0.2773  0.1170  143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.6064 0.5892 0.8535 0.0079  0.2681  0.1048  143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.6426 0.6234 0.8836 0.0085  0.2790  0.0978  143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.6320 0.6122 0.9073 0.0056  0.2787  0.0929  143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.6025 0.5887 0.8394 0.0034  0.2445  0.0925  143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.5933 0.5808 0.8445 0.0018  0.2321  0.0953  143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.5945 0.5847 0.8284 -0.0015 0.2131  0.0836  143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.5795 0.5649 0.8784 -0.0005 0.2311  0.0965  143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.6853 0.6647 0.8833 0.0126  0.2876  0.0965  144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.7297 0.7060 0.9148 0.0139  0.2988  0.0881  144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.7656 0.7369 0.9658 0.0185  0.3259  0.0975  144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.7719 0.7400 0.9680 0.0196  0.3371  0.0899  144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.7783 0.7544 0.9092 0.0171  0.2963  0.0817  144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.8642 0.8451 0.9802 0.0126  0.2725  0.0698  144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.8710 0.8540 1.0144 0.0070  0.2598  0.0639  144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.9085 0.8910 0.9857 0.0151  0.2666  0.0666  144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.7860 0.7556 1.0021 0.0216  0.3385  0.1142  145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.8156 0.7797 1.0465 0.0266  0.3679  0.1251  145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.8089 0.7735 1.1027 0.0244  0.3754  0.1358  145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.8099 0.7771 1.1236 0.0219  0.3628  0.1413  145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.8845 0.8434 1.0658 0.0351  0.3848  0.1373  145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 0.9716 0.9325 1.1384 0.0367  0.3737  0.1490  145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 1.0908 1.0500 1.1922 0.0433  0.3711  0.1507  145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 1.1037 1.0597 1.1886 0.0496  0.3795  0.1685  145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 1.1362 1.0968 1.2042 0.0424  0.3598  0.1342  145 GLU   A OE2 
1084 N N1  . A1B1O B .   ? 0.6097 0.5600 0.8903 0.0007  0.1253  -0.0003 201 A1B1O A N1  
1085 N N3  . A1B1O B .   ? 0.6747 0.5908 0.7936 0.0046  0.1229  -0.0316 201 A1B1O A N3  
1086 C C4  . A1B1O B .   ? 0.6212 0.5548 0.8895 -0.0001 0.1086  -0.0214 201 A1B1O A C4  
1087 C C5  . A1B1O B .   ? 0.6152 0.5537 0.8931 0.0014  0.1184  -0.0153 201 A1B1O A C5  
1088 C C6  . A1B1O B .   ? 0.6141 0.5469 0.9003 0.0041  0.1214  -0.0227 201 A1B1O A C6  
1089 C C7  . A1B1O B .   ? 0.6046 0.5564 0.8962 0.0029  0.1308  0.0012  201 A1B1O A C7  
1090 C C8  . A1B1O B .   ? 0.6812 0.5920 0.8298 0.0064  0.1141  -0.0429 201 A1B1O A C8  
1091 C C10 . A1B1O B .   ? 0.6875 0.5947 0.7933 0.0084  0.1297  -0.0395 201 A1B1O A C10 
1092 C C13 . A1B1O B .   ? 0.7048 0.5926 0.7937 0.0170  0.1431  -0.0593 201 A1B1O A C13 
1093 C C15 . A1B1O B .   ? 0.6868 0.5900 0.8102 0.0099  0.1240  -0.0481 201 A1B1O A C15 
1094 C C   . A1B1O B .   ? 0.6994 0.5868 0.8765 0.0128  0.1008  -0.0760 201 A1B1O A C   
1095 C C1  . A1B1O B .   ? 0.6918 0.5891 0.8682 0.0098  0.1028  -0.0631 201 A1B1O A C1  
1096 C C2  . A1B1O B .   ? 0.6807 0.5898 0.8580 0.0061  0.1047  -0.0483 201 A1B1O A C2  
1097 C C14 . A1B1O B .   ? 0.6942 0.5876 0.8092 0.0141  0.1302  -0.0586 201 A1B1O A C14 
1098 C C12 . A1B1O B .   ? 0.7068 0.5987 0.7804 0.0153  0.1491  -0.0495 201 A1B1O A C12 
1099 C C11 . A1B1O B .   ? 0.6955 0.5971 0.7777 0.0109  0.1417  -0.0400 201 A1B1O A C11 
1100 C C9  . A1B1O B .   ? 0.6719 0.5933 0.7815 0.0020  0.1243  -0.0230 201 A1B1O A C9  
1101 N N2  . A1B1O B .   ? 0.6694 0.5877 0.8138 0.0036  0.1145  -0.0332 201 A1B1O A N2  
1102 N N   . A1B1O B .   ? 0.6581 0.5797 0.8681 0.0033  0.1097  -0.0364 201 A1B1O A N   
1103 C C3  . A1B1O B .   ? 0.6374 0.5586 0.8793 0.0021  0.1020  -0.0374 201 A1B1O A C3  
1104 O O   . A1B1O B .   ? 0.6096 0.5513 0.9071 0.0050  0.1300  -0.0117 201 A1B1O A O   
# 
