data_7I7P
# 
_entry.id   7I7P 
# 
_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   7I7P         pdb_00007i7p 10.2210/pdb7i7p/pdb 
WWPDB D_1001408420 ?            ?                   
# 
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                        7I7P 
_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 '(1s,5s)-3-[(2-chlorophenyl)acetyl]-3-azabicyclo[3.1.1]heptane-1-carboxamide' 292.761   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                    65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                          78.133    1  ?         ? ? ? 
5 water       nat water                                                                         18.015    75 ?         ? ? ? 
# 
_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 '(1s,5s)-3-[(2-chlorophenyl)acetyl]-3-azabicyclo[3.1.1]heptane-1-carboxamide' A1B58 
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 
A1B58 non-polymer         . '(1s,5s)-3-[(2-chlorophenyl)acetyl]-3-azabicyclo[3.1.1]heptane-1-carboxamide' ? 'C15 H17 Cl N2 O2' 
292.761 
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        A1B58 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B58 
_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 A1B58 1  201 201 A1B58 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 36  HOH   HOH A . 
E 5 HOH   2  302 78  HOH   HOH A . 
E 5 HOH   3  303 22  HOH   HOH A . 
E 5 HOH   4  304 9   HOH   HOH A . 
E 5 HOH   5  305 29  HOH   HOH A . 
E 5 HOH   6  306 18  HOH   HOH A . 
E 5 HOH   7  307 42  HOH   HOH A . 
E 5 HOH   8  308 47  HOH   HOH A . 
E 5 HOH   9  309 16  HOH   HOH A . 
E 5 HOH   10 310 12  HOH   HOH A . 
E 5 HOH   11 311 59  HOH   HOH A . 
E 5 HOH   12 312 74  HOH   HOH A . 
E 5 HOH   13 313 14  HOH   HOH A . 
E 5 HOH   14 314 35  HOH   HOH A . 
E 5 HOH   15 315 60  HOH   HOH A . 
E 5 HOH   16 316 72  HOH   HOH A . 
E 5 HOH   17 317 8   HOH   HOH A . 
E 5 HOH   18 318 50  HOH   HOH A . 
E 5 HOH   19 319 7   HOH   HOH A . 
E 5 HOH   20 320 71  HOH   HOH A . 
E 5 HOH   21 321 4   HOH   HOH A . 
E 5 HOH   22 322 40  HOH   HOH A . 
E 5 HOH   23 323 23  HOH   HOH A . 
E 5 HOH   24 324 25  HOH   HOH A . 
E 5 HOH   25 325 10  HOH   HOH A . 
E 5 HOH   26 326 48  HOH   HOH A . 
E 5 HOH   27 327 24  HOH   HOH A . 
E 5 HOH   28 328 2   HOH   HOH A . 
E 5 HOH   29 329 21  HOH   HOH A . 
E 5 HOH   30 330 45  HOH   HOH A . 
E 5 HOH   31 331 46  HOH   HOH A . 
E 5 HOH   32 332 39  HOH   HOH A . 
E 5 HOH   33 333 73  HOH   HOH A . 
E 5 HOH   34 334 6   HOH   HOH A . 
E 5 HOH   35 335 54  HOH   HOH A . 
E 5 HOH   36 336 41  HOH   HOH A . 
E 5 HOH   37 337 75  HOH   HOH A . 
E 5 HOH   38 338 19  HOH   HOH A . 
E 5 HOH   39 339 30  HOH   HOH A . 
E 5 HOH   40 340 53  HOH   HOH A . 
E 5 HOH   41 341 34  HOH   HOH A . 
E 5 HOH   42 342 67  HOH   HOH A . 
E 5 HOH   43 343 33  HOH   HOH A . 
E 5 HOH   44 344 5   HOH   HOH A . 
E 5 HOH   45 345 13  HOH   HOH A . 
E 5 HOH   46 346 61  HOH   HOH A . 
E 5 HOH   47 347 20  HOH   HOH A . 
E 5 HOH   48 348 11  HOH   HOH A . 
E 5 HOH   49 349 3   HOH   HOH A . 
E 5 HOH   50 350 51  HOH   HOH A . 
E 5 HOH   51 351 64  HOH   HOH A . 
E 5 HOH   52 352 26  HOH   HOH A . 
E 5 HOH   53 353 15  HOH   HOH A . 
E 5 HOH   54 354 65  HOH   HOH A . 
E 5 HOH   55 355 70  HOH   HOH A . 
E 5 HOH   56 356 56  HOH   HOH A . 
E 5 HOH   57 357 77  HOH   HOH A . 
E 5 HOH   58 358 66  HOH   HOH A . 
E 5 HOH   59 359 31  HOH   HOH A . 
E 5 HOH   60 360 55  HOH   HOH A . 
E 5 HOH   61 361 49  HOH   HOH A . 
E 5 HOH   62 362 80  HOH   HOH A . 
E 5 HOH   63 363 28  HOH   HOH A . 
E 5 HOH   64 364 58  HOH   HOH A . 
E 5 HOH   65 365 52  HOH   HOH A . 
E 5 HOH   66 366 63  HOH   HOH A . 
E 5 HOH   67 367 68  HOH   HOH A . 
E 5 HOH   68 368 37  HOH   HOH A . 
E 5 HOH   69 369 44  HOH   HOH A . 
E 5 HOH   70 370 69  HOH   HOH A . 
E 5 HOH   71 371 38  HOH   HOH A . 
E 5 HOH   72 372 79  HOH   HOH A . 
E 5 HOH   73 373 62  HOH   HOH A . 
E 5 HOH   74 374 81  HOH   HOH A . 
E 5 HOH   75 375 76  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           7I7P 
_cell.length_a           72.995 
_cell.length_b           61.984 
_cell.length_c           32.819 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.27 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I7P 
_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          7I7P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_percent_sol   47.26 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-02-25 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I7P 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.44 
_reflns.d_resolution_high            1.90 
_reflns.number_obs                   9102 
_reflns.percent_possible_obs         78.8 
_reflns.pdbx_Rmerge_I_obs            0.140 
_reflns.pdbx_netI_over_sigmaI        5.0 
_reflns.pdbx_redundancy              4.6 
_reflns.pdbx_Rrim_I_all              0.156 
_reflns.pdbx_Rpim_I_all              0.065 
_reflns.pdbx_CC_half                 0.990 
_reflns.pdbx_number_measured_all     41934 
_reflns.pdbx_chi_squared             0.65 
_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                  1.90 
_reflns_shell.d_res_low                   2.00 
_reflns_shell.number_measured_all         1444 
_reflns_shell.number_unique_obs           739 
_reflns_shell.Rmerge_I_obs                1.231 
_reflns_shell.pdbx_chi_squared            0.28 
_reflns_shell.pdbx_redundancy             2.0 
_reflns_shell.percent_possible_obs        43.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.547 
_reflns_shell.pdbx_Rpim_I_all             0.916 
_reflns_shell.pdbx_CC_half                0.492 
_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                                 7I7P 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     9024 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.44 
_refine.ls_d_res_high                            1.902 
_refine.ls_percent_reflns_obs                    78.1 
_refine.ls_R_factor_obs                          0.2298 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2275 
_refine.ls_R_factor_R_free                       0.2724 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.150 
_refine.ls_number_reflns_R_free                  465 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.936 
_refine.correlation_coeff_Fo_to_Fc_free          0.900 
_refine.B_iso_mean                               33.80 
_refine.aniso_B[1][1]                            1.01520 
_refine.aniso_B[2][2]                            0.30220 
_refine.aniso_B[3][3]                            -1.31740 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.72180 
_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             0.244 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.202 
_refine.pdbx_overall_SU_R_Blow_DPI               0.250 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.203 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I7P 
_refine_analyze.Luzzati_coordinate_error_obs    0.32 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             75 
_refine_hist.number_atoms_total               1174 
_refine_hist.d_res_high                       1.902 
_refine_hist.d_res_low                        36.44 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.009 ? 2.00  1129 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.94  ? 2.00  1539 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1129 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.43  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.11 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  137  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  879  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   24 
_refine_ls_shell.d_res_high                       1.90 
_refine_ls_shell.d_res_low                        1.97 
_refine_ls_shell.number_reflns_R_work             372 
_refine_ls_shell.R_factor_R_work                  0.3464 
_refine_ls_shell.percent_reflns_obs               36.90 
_refine_ls_shell.R_factor_R_free                  0.2296 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.34 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                393 
_refine_ls_shell.R_factor_all                     0.3400 
# 
_struct.entry_id                  7I7P 
_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-0038427-001 (A71EV2A-x5277)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I7P 
_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 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              7I7P 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P4 AA4 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 ? ? ? ? ? ? ? 2.285 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.450 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.917 ? ? 
# 
_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_555 107.2 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.8 ? 
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_555 112.6 ? 
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_555 123.9 ? 
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_555 104.1 ? 
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_555 101.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N 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 ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I7P 
_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  ? ? -90.50  33.54   
2 1 CYS A 116 ? ? -120.52 -167.15 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     374 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.0896 
_pdbx_refine_tls.origin_y         6.6775 
_pdbx_refine_tls.origin_z         14.3139 
_pdbx_refine_tls.T[1][1]          -0.0029 
_pdbx_refine_tls.T[2][2]          -0.0624 
_pdbx_refine_tls.T[3][3]          -0.0850 
_pdbx_refine_tls.T[1][2]          0.0403 
_pdbx_refine_tls.T[1][3]          -0.0445 
_pdbx_refine_tls.T[2][3]          -0.0133 
_pdbx_refine_tls.L[1][1]          1.5072 
_pdbx_refine_tls.L[2][2]          10.3164 
_pdbx_refine_tls.L[3][3]          1.7304 
_pdbx_refine_tls.L[1][2]          2.9935 
_pdbx_refine_tls.L[1][3]          -1.0327 
_pdbx_refine_tls.L[2][3]          -3.0181 
_pdbx_refine_tls.S[1][1]          -0.1434 
_pdbx_refine_tls.S[1][2]          0.0644 
_pdbx_refine_tls.S[1][3]          0.0689 
_pdbx_refine_tls.S[2][1]          0.4104 
_pdbx_refine_tls.S[2][2]          0.1749 
_pdbx_refine_tls.S[2][3]          -0.3724 
_pdbx_refine_tls.S[3][1]          -0.0295 
_pdbx_refine_tls.S[3][2]          -0.2168 
_pdbx_refine_tls.S[3][3]          -0.0315 
# 
_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 
A1B58 N1   N  N N 1   
A1B58 C4   C  N N 2   
A1B58 C5   C  Y N 3   
A1B58 C6   C  Y N 4   
A1B58 C7   C  Y N 5   
A1B58 C8   C  Y N 6   
A1B58 C10  C  Y N 7   
A1B58 C13  C  N N 8   
A1B58 CL   CL N N 9   
A1B58 C9   C  Y N 10  
A1B58 C3   C  N N 11  
A1B58 O1   O  N N 12  
A1B58 C2   C  N N 13  
A1B58 C11  C  N N 14  
A1B58 C12  C  N N 15  
A1B58 C14  C  N N 16  
A1B58 C1   C  N N 17  
A1B58 C    C  N N 18  
A1B58 O    O  N N 19  
A1B58 N    N  N N 20  
A1B58 H6   H  N N 21  
A1B58 H5   H  N N 22  
A1B58 H7   H  N N 23  
A1B58 H8   H  N N 24  
A1B58 H9   H  N N 25  
A1B58 H13  H  N N 26  
A1B58 H14  H  N N 27  
A1B58 H10  H  N N 28  
A1B58 H3   H  N N 29  
A1B58 H4   H  N N 30  
A1B58 H11  H  N N 31  
A1B58 H12  H  N N 32  
A1B58 H    H  N N 33  
A1B58 H15  H  N N 34  
A1B58 H16  H  N N 35  
A1B58 H1   H  N N 36  
A1B58 H2   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 
A1B58 N   C    sing N N 1   
A1B58 O   C    doub N N 2   
A1B58 C   C1   sing N N 3   
A1B58 C1  C2   sing N N 4   
A1B58 C2  N1   sing N N 5   
A1B58 N1  C3   sing N N 6   
A1B58 O1  C3   doub N N 7   
A1B58 C3  C4   sing N N 8   
A1B58 C4  C5   sing N N 9   
A1B58 C5  C6   sing Y N 10  
A1B58 C6  C7   doub Y N 11  
A1B58 C7  C8   sing Y N 12  
A1B58 C8  C9   doub Y N 13  
A1B58 C9  C10  sing Y N 14  
A1B58 C5  C10  doub Y N 15  
A1B58 C10 CL   sing N N 16  
A1B58 C11 N1   sing N N 17  
A1B58 C12 C11  sing N N 18  
A1B58 C13 C12  sing N N 19  
A1B58 C1  C13  sing N N 20  
A1B58 C14 C12  sing N N 21  
A1B58 C1  C14  sing N N 22  
A1B58 C4  H6   sing N N 23  
A1B58 C4  H5   sing N N 24  
A1B58 C6  H7   sing N N 25  
A1B58 C7  H8   sing N N 26  
A1B58 C8  H9   sing N N 27  
A1B58 C13 H13  sing N N 28  
A1B58 C13 H14  sing N N 29  
A1B58 C9  H10  sing N N 30  
A1B58 C2  H3   sing N N 31  
A1B58 C2  H4   sing N N 32  
A1B58 C11 H11  sing N N 33  
A1B58 C11 H12  sing N N 34  
A1B58 C12 H    sing N N 35  
A1B58 C14 H15  sing N N 36  
A1B58 C14 H16  sing N N 37  
A1B58 N   H1   sing N N 38  
A1B58 N   H2   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                    7I7P 
_atom_sites.fract_transf_matrix[1][1]   0.013700 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000783 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016133 
_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]   0.030520 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.847 6.499   24.287 1.00 41.52 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.061 6.500   23.468 1.00 41.55 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.118 5.300   22.492 1.00 40.15 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.349 4.339   22.636 1.00 40.28 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.300 6.568   24.358 1.00 43.47 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.252 5.564   25.357 1.00 45.94 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.977 5.401   21.478 1.00 38.56 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.114 4.363   20.461 1.00 37.53 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.439 4.877   19.068 1.00 35.66 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.031 5.981   18.694 1.00 35.83 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.197 4.092   18.297 1.00 33.73 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.589 4.499   16.951 1.00 33.35 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.588 3.330   15.942 1.00 32.23 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.621 2.168   16.356 1.00 31.96 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.978 5.130   17.005 1.00 33.81 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.579 3.642   14.625 1.00 31.09 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.689 2.656   13.548 1.00 31.06 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.063 2.870   12.929 1.00 32.49 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.468 4.001   12.659 1.00 32.40 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.580 2.799   12.468 1.00 30.77 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.167 2.975   13.079 1.00 30.22 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.624 1.647   11.462 1.00 31.07 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.176 3.458   12.104 1.00 30.23 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.803 1.796   12.743 1.00 33.74 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.144 1.862   12.183 1.00 34.65 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.177 1.076   10.893 1.00 35.96 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.169 -0.145  10.943 1.00 36.78 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.129 1.280   13.188 1.00 34.33 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.241 2.104   14.451 1.00 34.69 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.979 3.285   14.474 1.00 36.12 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.627 1.699   15.621 1.00 35.07 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.103 4.036   15.638 1.00 36.67 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.769 2.421   16.796 1.00 36.50 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.490 3.602   16.797 1.00 37.85 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.591 4.318   17.962 1.00 39.89 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.174 1.757   9.741  1.00 35.77 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.201 1.095   8.432  1.00 36.38 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.342 1.712   7.641  1.00 37.58 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.432 2.937   7.570  1.00 36.94 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.842 1.207   7.686  1.00 36.92 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.257 2.625   7.758  1.00 37.07 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.970 0.743   6.242  1.00 37.24 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.286 0.882   7.150  1.00 38.63 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.459 1.350   6.416  1.00 40.20 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.200 2.420   7.196  1.00 42.00 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.265 2.315   8.426  1.00 43.38 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.606 3.525   6.543  1.00 41.46 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.285 4.591   7.274  1.00 41.52 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.283 5.666   7.834  1.00 39.11 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.630 6.835   7.992  1.00 38.54 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.401 5.178   6.427  1.00 45.09 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.472 4.140   6.106  1.00 52.13 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.856 3.317   6.948  1.00 54.06 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.979 4.148   4.880  1.00 53.85 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.072 5.227   8.217  1.00 36.99 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.050 6.131   8.762  1.00 34.79 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.554 5.733   10.159 1.00 33.19 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.640 4.567   10.560 1.00 33.19 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.863 6.251   7.792  1.00 33.75 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.251 6.867   6.466  1.00 34.27 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.836 8.128   6.406  1.00 35.30 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.029 6.196   5.275  1.00 35.11 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.197 8.698   5.193  1.00 36.26 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.352 6.769   4.054  1.00 36.39 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.953 8.015   4.017  1.00 37.76 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.323 8.559   2.811  1.00 39.92 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.081 6.729   10.908 1.00 31.21 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.485 6.569   12.229 1.00 30.05 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.175 7.375   12.182 1.00 29.26 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.215 8.555   11.870 1.00 29.50 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.429 7.105   13.325 1.00 30.36 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.789 7.190   14.716 1.00 33.02 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.773 7.654   15.786 1.00 36.07 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.209 8.675   16.680 1.00 39.14 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.759 8.430   17.909 1.00 41.27 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.790 7.196   18.402 1.00 40.73 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.280 9.414   18.655 1.00 40.64 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.017 6.743   12.425 1.00 27.97 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.726 7.441   12.384 1.00 26.79 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.175 7.576   13.786 1.00 25.11 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.909 6.577   14.425 1.00 25.16 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.691 6.711   11.504 1.00 27.56 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.443 7.573   11.319 1.00 27.97 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.284 6.304   10.159 1.00 28.26 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.961 8.786   14.245 1.00 23.77 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.423 9.045   15.581 1.00 23.90 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.206 9.982   15.524 1.00 22.72 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.986 10.656  14.511 1.00 22.25 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.508 9.661   16.517 1.00 25.54 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.410 8.600   17.091 1.00 26.83 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.301 10.781  15.828 1.00 26.12 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.480 10.125  16.659 1.00 22.10 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.437 11.133  16.793 1.00 21.94 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.166 12.462  16.807 1.00 23.18 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.187 12.604  17.492 1.00 23.74 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.661 10.989  18.095 1.00 21.62 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.878 9.695   18.213 1.00 23.23 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.381 8.715   18.760 1.00 24.42 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.648 9.658   17.705 1.00 21.60 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.700 13.414  16.007 1.00 23.36 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.335 14.714  15.923 1.00 23.77 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.362 15.411  17.294 1.00 25.76 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.403 15.981  17.660 1.00 26.99 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.673 15.562  14.839 1.00 23.21 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.440 16.819  14.470 1.00 23.50 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.503 17.706  13.698 1.00 23.85 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.093 18.950  13.191 1.00 24.02 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.231 20.061  13.901 1.00 24.13 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.938 20.069  15.193 1.00 24.20 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.675 21.171  13.328 1.00 22.27 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.296 15.247  18.106 1.00 25.98 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.281 15.868  19.437 1.00 27.43 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.347 15.291  20.409 1.00 28.69 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.771 16.005  21.301 1.00 28.10 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.873 15.868  20.062 1.00 28.45 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.452 14.562  20.650 1.00 31.87 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.923 13.553  19.861 1.00 33.66 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.465 14.149  21.940 1.00 33.26 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.667 12.548  20.685 1.00 34.30 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.970 12.857  21.945 1.00 34.50 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.839 14.045  20.188 1.00 30.22 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.845 13.415  21.050 1.00 31.38 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.284 13.427  20.469 1.00 33.39 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.161 12.767  21.025 1.00 33.51 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.436 11.942  21.330 1.00 31.12 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.159 11.690  22.146 1.00 31.88 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.951 10.187  22.385 1.00 31.67 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.195 12.437  23.482 1.00 32.64 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.520 14.105  19.341 1.00 34.88 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.827 14.104  18.676 1.00 36.65 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.939 14.770  19.478 1.00 38.80 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.697 15.782  20.130 1.00 39.18 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.714 14.735  17.292 1.00 36.87 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.166 14.202  19.431 1.00 40.17 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.325 14.716  20.170 1.00 42.05 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.135 15.788  19.382 1.00 43.90 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.785 16.101  18.238 1.00 44.39 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.221 13.534  20.600 1.00 44.00 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.897 13.035  19.448 1.00 45.50 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.465 12.447  21.321 1.00 44.66 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.198 16.366  19.997 1.00 44.78 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.067 17.321  19.325 1.00 46.27 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.768 16.643  18.157 1.00 45.82 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.883 17.235  17.090 1.00 46.08 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.127 17.867  20.280 1.00 49.29 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.606 18.857  21.263 1.00 55.00 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.140 20.090  20.857 1.00 57.88 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.546 18.784  22.613 1.00 57.25 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.799 20.725  21.965 1.00 58.87 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.019 19.977  23.048 1.00 58.93 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.223 15.403  18.347 1.00 45.07 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.875 14.622  17.301 1.00 45.50 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.971 14.460  16.086 1.00 43.82 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.431 14.656  14.965 1.00 44.37 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.274 13.249  17.829 1.00 48.63 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.041 12.431  16.824 1.00 55.33 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.246 12.647  16.605 1.00 57.17 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.354 11.466  16.196 1.00 57.12 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.687 14.127  16.314 1.00 41.48 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.686 13.991  15.262 1.00 39.87 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.576 15.276  14.431 1.00 38.24 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.546 15.208  13.211 1.00 38.14 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.314 13.614  15.867 1.00 39.89 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.243 12.205  16.417 1.00 42.40 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.906 11.316  15.852 1.00 42.07 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.520 11.992  17.417 1.00 44.28 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.529 16.437  15.078 1.00 37.50 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.440 17.718  14.371 1.00 37.40 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.758 18.123  13.678 1.00 37.83 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.733 18.788  12.649 1.00 38.40 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.957 18.832  15.321 1.00 36.61 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.472 18.829  15.538 1.00 35.19 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.797 18.294  16.594 1.00 35.71 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.484 19.379  14.664 1.00 34.38 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.444 18.479  16.430 1.00 36.06 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.224 19.126  15.242 1.00 35.12 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.535 20.007  13.417 1.00 34.26 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.035 19.522  14.638 1.00 34.89 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.358 20.412  12.830 1.00 34.59 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.126 20.168  13.437 1.00 34.63 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.893 17.754  14.249 1.00 37.71 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.203 18.052  13.657 1.00 38.47 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.545 17.099  12.483 1.00 39.33 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.536 17.335  11.776 1.00 40.65 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.295 17.961  14.722 1.00 37.69 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.795 15.980  12.349 1.00 37.31 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.922 14.987  11.290 1.00 36.16 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.567 14.781  10.576 1.00 34.09 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.267 13.680  10.133 1.00 33.51 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.433 13.669  11.886 1.00 38.53 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.911 13.743  12.171 1.00 42.63 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.679 14.180  11.319 1.00 46.15 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.339 13.344  13.363 1.00 41.30 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.736 15.850  10.520 1.00 32.90 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.395 15.896  9.956  1.00 30.78 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.382 15.570  8.481  1.00 30.56 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.106 16.207  7.722  1.00 30.83 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.811 17.302  10.168 1.00 29.71 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.439 17.605  9.503  1.00 30.16 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.323 16.796  10.146 1.00 30.31 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.101 19.086  9.561  1.00 29.79 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.526 14.595  8.073  1.00 29.66 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.272 14.234  6.681  1.00 29.18 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.891 14.870  6.258  1.00 28.27 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.802 15.626  5.289  1.00 29.28 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.247 12.701  6.526  1.00 30.44 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.729 12.310  5.157  1.00 31.28 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.617 12.085  6.801  1.00 30.82 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.839 14.609  7.038  1.00 26.01 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.503 15.104  6.767  1.00 23.91 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.699 15.202  8.074  1.00 22.21 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.931 14.445  9.014  1.00 22.06 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.819 14.148  5.770  1.00 23.36 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.349 14.364  5.583  1.00 23.09 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.746 15.377  4.898  1.00 23.50 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.292 13.559  6.127  1.00 22.36 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.378 15.243  4.966  1.00 23.72 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.072 14.135  5.714  1.00 23.22 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.257 12.422  6.934  1.00 22.04 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.837 13.564  6.024  1.00 23.30 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.032 11.877  7.260  1.00 22.30 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.842 12.443  6.804  1.00 22.48 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.785 16.165  8.141  1.00 20.88 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.906 16.333  9.286  1.00 20.10 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.568 16.966  8.820  1.00 20.30 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.557 17.812  7.920  1.00 20.33 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.576 17.139  10.412 1.00 20.01 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.083 18.526  10.007 1.00 23.24 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.084 19.676  9.921  1.00 25.90 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.426 20.705  9.290  1.00 28.21 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.956 19.541  10.449 1.00 22.87 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.450 16.543  9.422  1.00 20.08 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.133 17.087  9.112  1.00 19.40 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.329 17.182  10.415 1.00 17.94 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.880 16.159  10.929 1.00 17.92 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.431 16.242  8.040  1.00 21.85 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.143 16.814  7.482  1.00 28.77 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.767 17.928  7.871  1.00 31.14 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.500 16.136  6.677  1.00 32.78 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.141 18.417  10.933 1.00 16.55 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.403 18.640  12.177 0.50 16.83 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.387 18.691  12.166 0.50 16.63 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.958 18.166  12.076 1.00 16.59 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.420 17.705  13.071 1.00 16.83 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.437 20.113  12.576 0.50 18.24 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.322 20.194  12.450 0.50 17.38 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.677 20.884  11.663 0.50 20.29 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 16.557 20.864  12.260 0.50 18.41 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.333 18.253  10.885 1.00 16.02 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.950 17.763  10.722 1.00 17.09 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.853 16.243  10.848 1.00 15.97 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.793 15.736  11.151 1.00 16.54 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.347 18.210  9.388  1.00 21.29 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.960 17.541  8.293  1.00 26.30 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.928 15.521  10.578 1.00 15.05 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.958 14.071  10.727 1.00 14.93 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.543 13.607  12.048 1.00 16.14 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.493 12.419  12.330 1.00 16.83 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.745 13.428  9.589  1.00 14.38 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.045 13.578  8.254  1.00 14.93 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.882 12.935  7.182  1.00 16.67 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.840 11.473  7.269  1.00 17.79 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.977 10.661  6.226  1.00 18.70 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.162 11.158  5.006  1.00 17.00 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.917 9.344   6.391  1.00 17.00 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.137 14.520  12.834 1.00 17.21 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.858 14.229  14.061 1.00 17.82 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.022 13.275  13.762 1.00 18.84 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.318 12.416  14.596 1.00 19.63 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.931 13.709  15.195 1.00 18.55 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.660 13.437  16.513 1.00 23.62 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.560 14.232  16.871 1.00 22.98 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.358 12.399  17.165 1.00 26.47 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.693 13.409  12.577 1.00 18.47 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.845 12.535  12.228 1.00 18.31 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.145 13.313  12.004 1.00 19.50 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.151 14.424  11.493 1.00 19.52 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.596 11.737  10.924 1.00 17.85 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.482 10.697  10.894 1.00 18.49 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.399 10.050  9.479  1.00 18.46 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.723 9.622   11.951 1.00 18.65 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.251 12.681  12.329 1.00 20.91 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.569 13.213  12.057 1.00 22.70 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.439 12.025  11.700 1.00 24.77 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.402 11.009  12.377 1.00 25.12 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.158 14.034  13.237 1.00 22.39 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.466 14.767  12.934 1.00 22.78 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.524 16.066  13.651 1.00 23.43 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.663 13.942  13.302 1.00 23.72 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.202 12.143  10.616 1.00 26.72 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.138 11.125  10.156 1.00 28.30 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.559 11.717  10.209 1.00 30.49 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.794 12.825  9.714  1.00 29.89 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.772 10.636  8.732  1.00 28.74 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.874 9.748   8.152  1.00 29.77 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.427 9.911   8.737  1.00 28.89 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.488 10.999  10.839 1.00 33.02 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.883 11.439  10.891 1.00 36.14 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.825 10.364  10.340 1.00 40.24 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.469 9.177   10.264 1.00 39.61 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.278 11.880  12.298 1.00 36.79 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.069 10.862  13.264 1.00 38.56 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.022 10.792  9.916  1.00 43.45 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.015 9.890   9.361  1.00 47.08 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.805 9.209   10.462 1.00 50.70 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.060 9.804   11.509 1.00 51.08 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.969 10.648  8.448  1.00 48.58 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.518 11.755  9.142  1.00 51.36 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.173 7.954   10.238 1.00 53.30 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.971 7.194   11.206 1.00 56.56 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.240 6.673   10.539 1.00 60.13 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.281 6.548   9.311  1.00 61.22 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.169 6.023   11.839 1.00 57.28 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.194 4.876   10.990 1.00 58.34 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.741 6.392   12.192 1.00 56.91 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.263 6.342   11.334 1.00 61.69 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.485 5.773   10.784 1.00 63.72 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.275 4.269   10.616 1.00 64.67 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.631 3.697   9.580  1.00 65.91 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.709 6.076   11.680 1.00 66.43 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.359 5.830   13.046 1.00 68.90 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.220 7.494   11.524 1.00 66.57 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.719 3.620   11.648 1.00 63.61 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.467 2.193   11.626 1.00 62.96 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.301 1.846   10.714 1.00 62.24 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.363 2.632   10.556 1.00 61.86 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.179 1.707   13.032 1.00 63.27 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.356 0.653   10.122 1.00 61.74 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.310 0.147   9.237  1.00 61.62 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.141 -0.428  10.075 1.00 60.39 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.383 -1.147  11.038 1.00 60.76 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.921 -0.881  8.248  1.00 63.82 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.940 -1.880  7.626  1.00 68.91 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.115 -1.308  6.499  1.00 73.73 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.423 -0.232  5.930  1.00 75.90 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.034 -2.025  6.167  1.00 72.91 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.907 -0.038  9.736  1.00 58.85 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.667 -0.479  10.375 1.00 57.82 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.035 -1.659  9.652  1.00 55.75 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.235 -1.818  8.446  1.00 56.02 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.240 -2.466  10.352 1.00 53.82 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.715 -3.688  9.738  1.00 52.65 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.188 -3.830  9.727  1.00 49.28 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.688 -4.868  9.268  1.00 49.41 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.375 -4.899  10.383 1.00 55.02 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.170 -4.991  10.115 1.00 63.84 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.453 -2.807  10.193 1.00 45.61 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.994 -2.879  10.184 1.00 42.81 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.465 -2.884  8.742  1.00 40.19 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.877 -2.087  7.902  1.00 40.10 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.352 -1.730  11.006 1.00 43.61 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.416 -1.898  12.516 1.00 46.22 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.157 -3.018  12.998 1.00 47.63 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.708 -0.895  13.220 1.00 46.25 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.584 -3.813  8.456  1.00 38.29 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.922 -3.940  7.168  1.00 36.97 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.642 -3.095  7.266  1.00 35.21 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.855 -3.308  8.182  1.00 35.39 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.570 -5.428  6.937  1.00 38.26 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.763 -6.143  6.567  1.00 39.96 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.491 -5.622  5.872  1.00 38.31 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.450 -2.133  6.367  1.00 33.55 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.242 -1.315  6.359  1.00 32.20 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.227 -2.035  5.488  1.00 31.94 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.575 -2.492  4.405  1.00 32.45 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.523 0.118   5.786  1.00 31.86 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.666 0.830   6.529  1.00 32.18 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.248 0.984   5.736  1.00 31.59 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.352 1.230   7.975  1.00 32.99 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.978 -2.126  5.932  1.00 31.44 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.919 -2.720  5.122  1.00 30.91 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.555 -1.749  3.980  1.00 31.39 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.592 -0.528  4.146  1.00 31.63 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.695 -2.975  5.986  1.00 30.04 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.216 -2.298  2.828  1.00 31.61 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.731 -1.577  1.653  1.00 32.03 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.404 -2.265  1.324  1.00 33.09 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.383 -3.207  0.531  1.00 34.28 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.732 -1.728  0.496  1.00 32.69 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.107 -1.107  0.776  1.00 34.14 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.072 0.343   1.258  1.00 35.46 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.424 0.836   1.513  1.00 35.56 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.711 1.961   2.157  1.00 35.54 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.740 2.720   2.646  1.00 33.15 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.974 2.328   2.333  1.00 34.82 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.311 -1.857  2.004  1.00 32.24 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.013 -2.536  1.905  1.00 31.95 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.850  -1.590  2.314  1.00 32.90 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.093 -0.440  2.687  1.00 33.37 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.063 -3.745  2.833  1.00 31.54 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.112 -3.305  4.605  1.00 32.04 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.597  -2.104  2.321  1.00 33.27 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.422  -1.382  2.827  1.00 34.18 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.738  -2.211  3.946  1.00 33.22 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.520  -2.311  3.994  1.00 33.35 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.419  -1.037  1.709  1.00 37.85 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.730  -2.222  1.077  1.00 48.57 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.206  -3.359  1.273  1.00 50.74 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.704  -2.016  0.384  1.00 54.02 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.532  -2.835  4.811  1.00 32.09 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.033  -3.634  5.931  1.00 30.38 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.247  -2.778  6.895  1.00 28.01 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.576  -1.618  7.106  1.00 28.44 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.191  -4.314  6.657  1.00 30.62 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.710  -5.885  5.928  1.00 32.50 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.244  -3.358  7.509  1.00 25.77 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.463  -2.698  8.539  1.00 24.76 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.386  -3.524  9.816  1.00 23.72 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.450  -3.364  10.593 1.00 23.92 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.066  -2.320  8.024  1.00 26.43 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.074  -1.032  7.172  1.00 28.87 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.704  -0.618  6.716  1.00 34.06 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.381  -0.637  5.516  1.00 37.17 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.863  -0.237  7.654  1.00 33.93 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.343  -4.453  10.012 1.00 22.43 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.496  -5.310  11.187 1.00 20.98 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.990  -5.440  11.429 1.00 19.41 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.787  -5.471  10.491 1.00 18.97 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.845  -6.712  11.015 1.00 22.42 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.570  -7.472  10.045 1.00 24.15 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.377  -6.654  10.655 1.00 21.96 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.355  -5.519  12.685 1.00 18.37 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.747  -5.618  13.087 1.00 18.40 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.887  -5.776  14.585 1.00 18.57 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.910  -6.034  15.278 1.00 18.57 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.113 -5.638  15.096 1.00 18.64 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.432 -5.760  16.510 1.00 18.36 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.288 -4.549  16.880 1.00 18.42 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.194 -4.183  16.130 1.00 18.16 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.159 -7.102  16.810 1.00 19.34 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.559 -7.211  18.271 1.00 20.10 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.300 -8.295  16.422 1.00 20.60 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.011 -3.918  18.033 1.00 18.32 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.816 -2.770  18.459 1.00 18.56 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.390 -2.987  19.868 1.00 19.90 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.791 -3.699  20.661 1.00 19.08 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.046 -1.438  18.339 1.00 16.96 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.067 -1.201  19.464 1.00 17.10 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.830  -1.823  19.475 1.00 17.58 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.355 -0.307  20.490 1.00 18.11 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.923  -1.604  20.504 1.00 18.91 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.467  -0.101  21.541 1.00 18.84 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.248  -0.755  21.544 1.00 19.92 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.327  -0.548  22.537 1.00 21.06 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.549 -2.374  20.165 1.00 21.26 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.133 -2.513  21.483 1.00 23.00 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.670 -1.361  22.392 1.00 24.29 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.751 -0.184  22.008 1.00 23.47 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.666 -2.673  21.451 1.00 23.33 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.244 -2.759  22.850 1.00 24.83 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.970 -3.844  23.671 1.00 26.24 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.066 -1.757  23.346 1.00 26.39 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.508 -3.936  24.953 1.00 27.73 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.595 -1.828  24.630 1.00 27.76 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.296 -2.908  25.438 1.00 29.47 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.778 -2.941  26.723 1.00 32.89 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.130 -1.724  23.576 1.00 25.22 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.628 -0.763  24.549 1.00 26.42 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.559 -0.793  25.746 1.00 27.73 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.444 -1.727  26.542 1.00 27.54 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.203 -1.130  24.954 1.00 26.64 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.414 0.080   26.043 1.00 27.95 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.499 0.187   25.877 1.00 28.37 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.430 0.152   27.001 1.00 30.17 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.786 0.400   28.357 1.00 32.19 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.291 -0.118  29.364 1.00 32.70 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.625 1.083   26.804 1.00 31.99 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.275 2.454   26.786 1.00 34.26 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.654 1.127   28.398 1.00 32.95 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.920 1.379   29.653 1.00 34.03 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.252 0.119   30.247 1.00 35.61 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.797 0.147   31.386 1.00 36.75 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.895 2.491   29.477 1.00 34.26 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.813 2.076   28.665 1.00 34.80 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.200 -0.969  29.475 1.00 35.17 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.681 -2.262  29.885 1.00 35.18 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.732 -3.371  29.738 1.00 36.75 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.442 -4.518  30.095 1.00 37.21 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.490 -2.641  29.004 1.00 35.52 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.208  -1.907  29.313 1.00 37.28 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.653  -2.274  30.675 1.00 38.17 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.453  -1.493  30.942 1.00 39.89 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.438  -0.322  31.570 1.00 41.55 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.564  0.203   32.041 1.00 41.50 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.296  0.330   31.742 1.00 41.22 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.908 -3.076  29.132 1.00 37.27 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.961 -4.051  28.839 1.00 37.93 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.391 -5.289  28.119 1.00 36.76 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.688 -6.443  28.485 1.00 36.99 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.762 -4.409  30.096 1.00 41.04 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.803 -3.373  30.497 1.00 46.10 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.589 -3.928  31.664 1.00 53.45 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.845 -2.915  32.687 1.00 60.41 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.270 -3.184  33.919 1.00 66.09 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.474 -4.443  34.302 1.00 66.46 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.489 -2.196  34.783 1.00 67.94 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.521 -5.022  27.115 1.00 34.64 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.831 -6.052  26.326 1.00 33.24 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.662 -5.599  24.864 1.00 30.65 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.597 -4.397  24.584 1.00 30.66 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.393 -6.252  26.865 1.00 35.13 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.182 -7.316  27.897 1.00 39.49 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.730  -7.262  28.352 1.00 44.58 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.363  -8.344  29.346 1.00 48.97 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.791  -8.013  30.736 1.00 51.04 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.502 -6.574  23.961 1.00 28.05 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.175 -6.358  22.555 1.00 26.29 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.657 -6.586  22.402 1.00 25.15 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.078 -7.428  23.096 1.00 25.55 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.940 -7.329  21.662 1.00 25.70 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.415 -7.106  21.639 1.00 24.79 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.022 -6.399  20.619 1.00 25.80 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.360 -7.513  22.509 1.00 25.25 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.311 -6.414  20.890 1.00 25.61 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.559 -7.061  22.025 1.00 26.14 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.009 -5.830  21.519 1.00 23.77 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.563  -5.931  21.353 1.00 22.65 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.143  -6.011  19.891 1.00 21.75 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.556  -5.194  19.070 1.00 19.91 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.865  -4.726  22.013 1.00 22.24 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.854  -4.708  23.522 1.00 22.63 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.085  -5.613  24.241 1.00 24.01 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.508  -3.712  24.228 1.00 23.74 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.040  -5.580  25.632 1.00 25.03 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.438  -3.644  25.618 1.00 25.15 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.719  -4.592  26.318 1.00 26.19 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.664  -4.539  27.692 1.00 28.28 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.250  -6.959  19.563 1.00 22.44 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.731  -7.018  18.180 1.00 22.28 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.641  -5.942  17.964 1.00 22.83 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.821  -5.723  18.855 1.00 23.65 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.193  -8.445  18.066 1.00 22.87 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.793  -8.817  19.485 1.00 23.77 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.646  -7.991  20.441 1.00 22.18 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.660  -5.222  16.827 1.00 22.06 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.703  -4.136  16.594 1.00 21.84 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.169  -4.120  15.179 1.00 21.21 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.855  -4.526  14.245 1.00 21.17 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.336  -2.728  16.877 1.00 22.52 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.396  -2.415  18.364 1.00 23.24 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.707  -2.588  16.224 1.00 23.04 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.967  -3.567  15.013 1.00 20.46 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.414  -3.231  13.712 1.00 20.88 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.609  -1.748  13.707 1.00 21.24 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.328  -1.104  14.725 1.00 22.16 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.917  -3.527  13.626 1.00 21.90 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.747  -4.908  13.381 1.00 25.49 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.110  -1.196  12.616 1.00 21.15 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.375  0.241   12.579 1.00 22.25 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.855  0.900   11.301 1.00 24.58 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.563  0.214   10.320 1.00 25.40 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.863  0.534   12.851 1.00 21.11 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.846  -0.178  11.956 1.00 20.45 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.374  -1.399  12.316 1.00 20.17 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.293  0.414   10.779 1.00 21.06 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.304  -2.037  11.498 1.00 20.81 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.212  -0.231  9.958  1.00 20.91 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.691  -1.463  10.308 1.00 20.49 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.619  2.218   11.356 1.00 25.64 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.049  2.927   10.222 1.00 27.55 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.089  3.221   9.124  1.00 28.62 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.282  2.950   9.308  1.00 28.83 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.334  4.192   10.697 1.00 29.98 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.223  5.284   10.865 1.00 33.06 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.635  3.716   7.973  1.00 29.09 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.542  4.077   6.882  1.00 30.97 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.156  5.464   7.167  1.00 31.45 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.517  6.269   7.836  1.00 31.50 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.783  4.067   5.544  1.00 33.99 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.056  2.750   5.310  1.00 40.14 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.882  2.453   3.826  1.00 46.30 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 3.210  2.145   3.177  1.00 50.92 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 3.158  2.370   1.706  1.00 54.31 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.407  5.746   6.742  1.00 31.89 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.014  7.056   7.063  1.00 32.83 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.196  8.266   6.623  1.00 34.17 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.823  8.381   5.454  1.00 34.22 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.383  6.998   6.386  1.00 33.22 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.677  5.537   6.262  1.00 33.58 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.343  4.889   5.992  1.00 31.39 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.913  9.169   7.566  1.00 35.06 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.085  10.332  7.278  1.00 36.75 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.395  11.563  8.164  1.00 37.05 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.254  11.489  9.049  1.00 35.98 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.611  9.941   7.386  1.00 39.93 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.327  9.338   8.641  1.00 44.05 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.710  12.713  7.882  1.00 37.81 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.840  13.963  8.628  1.00 38.72 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.906  13.858  9.815  1.00 40.43 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.692  13.834  9.628  1.00 41.28 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.402  15.170  7.775  1.00 38.15 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.428  15.773  6.859  1.00 39.70 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.776  16.641  5.831  1.00 40.64 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.460  16.590  7.637  1.00 40.08 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.450  13.806  11.024 1.00 41.00 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.641  13.691  12.226 1.00 42.41 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.009  14.811  13.182 1.00 44.39 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.190  15.009  13.469 1.00 44.29 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.813  12.279  12.870 1.00 42.72 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.149  11.182  12.000 1.00 43.45 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.278  12.238  14.312 1.00 42.77 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.630  9.853   12.248 1.00 44.57 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.004  15.559  13.661 1.00 45.73 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.227  16.647  14.603 1.00 47.44 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.825  16.154  15.924 1.00 47.85 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.335  15.203  16.530 1.00 48.05 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.921  17.404  14.875 1.00 48.18 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.070  18.580  15.811 1.00 49.36 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.569  19.786  15.357 1.00 50.30 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.693  18.484  17.139 1.00 50.65 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.694  20.871  16.214 1.00 51.34 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.776  19.588  17.983 1.00 51.65 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.299  20.767  17.521 1.00 51.24 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.900  16.810  16.354 1.00 47.83 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.589  16.522  17.598 1.00 48.06 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.544  17.804  18.438 1.00 49.40 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.005  18.868  17.994 1.00 48.55 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.047  16.009  17.378 1.00 47.45 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.794  15.885  18.696 1.00 47.47 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.060  14.683  16.638 1.00 47.44 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.948  17.685  19.646 1.00 51.06 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.791  18.727  20.662 1.00 52.59 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.144  19.387  20.941 1.00 53.64 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.189  18.736  20.804 1.00 54.24 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.258  18.086  21.953 1.00 55.67 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.378  18.990  22.811 1.00 63.74 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.629  18.280  23.928 1.00 74.16 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.857  18.957  24.648 1.00 77.50 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.810  17.048  24.083 1.00 77.49 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.138  20.673  21.301 1.00 53.59 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.389  21.384  21.568 1.00 53.94 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.188  20.757  22.711 1.00 53.65 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.650  20.530  23.797 1.00 54.54 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.112  22.837  21.874 1.00 53.80 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.469  20.486  22.455 1.00 52.11 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.416  19.912  23.409 1.00 51.05 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.560 20.923  23.691 1.00 50.22 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.585 22.009  23.108 1.00 50.08 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 9.979  18.601  22.852 1.00 51.57 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.061 18.785  21.952 1.00 52.61 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.518 20.556  24.557 1.00 49.45 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 12.672 21.411  24.824 1.00 48.82 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 13.645 21.439  23.645 1.00 46.52 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.370 22.417  23.482 1.00 46.97 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.409 20.962  26.098 1.00 52.63 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.931 19.531  26.074 1.00 59.31 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.935 19.211  27.171 1.00 68.37 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 15.463 20.160  27.802 1.00 69.76 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.202 18.007  27.392 1.00 71.20 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.670 20.369  22.831 1.00 44.05 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.576 20.247  21.702 1.00 41.72 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.022 20.943  20.468 1.00 38.92 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.781 21.560  19.735 1.00 38.87 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 14.869 18.762  21.405 1.00 41.48 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.327 17.959  22.608 1.00 41.93 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.641 18.014  23.047 1.00 42.81 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.448 17.132  23.292 1.00 42.62 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.068 17.275  24.147 1.00 43.60 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 14.863 16.385  24.390 1.00 43.51 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.179 16.450  24.811 1.00 44.43 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.604 15.696  25.889 1.00 45.65 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.715 20.841  20.229 1.00 36.79 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.109 21.450  19.051 1.00 35.82 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.812 22.178  19.396 1.00 36.68 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.089 21.738  20.289 1.00 36.38 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.748 20.376  18.008 1.00 33.99 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.841 19.438  17.565 1.00 31.96 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.886 18.129  18.023 1.00 31.60 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.745 19.811  16.581 1.00 31.25 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.843 17.233  17.563 1.00 31.40 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.721 18.930  16.129 1.00 31.11 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.756 17.634  16.611 1.00 31.21 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.709 16.751  16.160 1.00 30.11 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.444 23.239  18.646 1.00 37.12 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.125  23.872  18.891 1.00 38.00 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.970  22.995  18.342 1.00 38.96 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.238  21.917  17.802 1.00 39.86 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.246  25.230  18.172 1.00 38.58 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.227 24.969  17.052 1.00 38.76 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.164 23.864  17.515 1.00 36.62 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.692  23.411  18.497 1.00 38.80 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.571  22.599  17.992 1.00 38.96 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.640  22.526  16.449 1.00 38.17 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.788  23.549  15.788 1.00 38.29 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.247  23.176  18.448 1.00 39.71 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.615  21.307  15.888 1.00 36.97 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.823  21.119  14.445 1.00 35.56 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.264  19.771  13.947 1.00 34.38 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 4.867  18.935  14.754 1.00 34.34 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.365  21.172  14.176 1.00 35.49 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.121  19.837  14.448 1.00 35.14 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.521  19.995  15.013 1.00 35.13 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.444 18.915  14.619 1.00 34.94 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.493 17.714  15.192 1.00 33.09 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.355 16.801  14.762 1.00 31.63 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.655  17.406  16.172 1.00 31.45 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.280  19.544  12.622 1.00 33.58 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 4.944  18.241  12.067 1.00 33.59 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.281  17.540  11.775 1.00 31.20 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.092  18.062  11.006 1.00 31.05 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.188  18.367  10.742 1.00 35.32 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.755  18.837  10.865 1.00 38.14 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.709  17.930  10.946 1.00 40.12 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.440  20.187  10.813 1.00 40.06 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.386  18.355  11.018 1.00 41.84 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.122  20.626  10.883 1.00 41.78 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.096  19.708  10.987 1.00 43.75 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.211 20.160  11.037 1.00 47.42 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.528  16.388  12.402 1.00 28.66 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.731  15.613  12.116 1.00 26.35 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.408  14.761  10.882 1.00 25.59 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.325  14.188  10.809 1.00 26.88 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.126  14.725  13.320 1.00 25.61 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.398  13.861  13.060 1.00 25.07 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.090 13.352  14.300 1.00 24.18 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.202 14.060  15.303 1.00 23.65 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.623 12.116  14.241 1.00 22.38 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.293  14.718  9.887  1.00 23.54 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.057  13.910  8.676  1.00 22.08 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.776  12.536  8.789  1.00 22.29 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.696  12.363  9.632  1.00 21.72 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.522  14.655  7.426  1.00 21.50 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.921  14.909  7.473  1.00 22.79 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.326  11.567  7.948  1.00 21.32 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.856  10.206  7.875  1.00 21.13 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.713  9.468   9.232  1.00 20.74 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.560  8.664   9.612  1.00 19.77 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.304 10.213  7.362  1.00 21.64 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.474 10.928  6.055  1.00 24.75 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.447 10.246  4.847  1.00 27.09 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.674 12.248  5.802  1.00 25.73 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.614 11.174  3.907  1.00 27.54 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.755 12.388  4.433  1.00 26.65 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.623  9.748   9.945  1.00 21.17 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.369  9.157   11.259 1.00 22.06 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.352  8.034   11.176 1.00 21.59 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.330  8.176   10.510 1.00 21.95 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 6.901  10.251  12.246 1.00 22.32 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.846  9.879   13.728 1.00 23.63 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.216  9.477   14.228 1.00 23.56 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.291  11.068  14.560 1.00 25.04 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.621  6.929   11.872 1.00 21.19 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.754  5.754   11.881 1.00 21.21 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.299  5.458   13.289 1.00 21.97 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.139  5.275   14.155 1.00 22.44 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.517  4.554   11.320 1.00 21.68 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.033  4.793   9.923  1.00 23.89 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.099  3.459   9.358  1.00 27.82 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.460  3.619   10.454 1.00 19.57 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.982  5.413   13.537 1.00 22.37 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.472  5.152   14.879 1.00 23.13 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.059  3.702   15.089 1.00 22.57 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.693  3.013   14.145 1.00 21.74 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.285  6.111   15.231 1.00 24.32 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.627  7.619   15.332 1.00 26.12 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.468  8.415   15.941 1.00 27.22 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.858  7.865   16.202 1.00 26.36 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.078  3.265   16.355 1.00 22.67 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.690  1.924   16.747 1.00 23.14 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.211  1.910   18.193 1.00 24.00 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.647  2.715   19.010 1.00 23.36 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.879  0.988   16.609 1.00 23.00 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.339  0.969   18.514 1.00 25.04 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.863  0.776   19.873 1.00 27.03 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.979  0.029   20.613 1.00 28.94 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.435  -1.037  20.181 1.00 28.38 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.514 0.043   19.892 1.00 27.91 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.928 -0.360  21.302 1.00 28.08 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.596 0.927   19.245 1.00 28.02 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.511  0.680   21.635 1.00 30.32 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.618  0.126   22.395 1.00 31.75 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.221  1.087   23.400 1.00 32.93 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.074  2.312   23.290 1.00 34.64 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.929  0.534   24.373 1.00 31.76 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.562  1.310   25.398 1.00 31.77 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.834  2.080   24.945 1.00 31.67 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.677  1.541   24.246 1.00 31.27 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.857  0.433   26.619 1.00 32.41 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.397  1.233   27.752 1.00 34.08 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.606  2.130   28.419 1.00 36.46 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.667  1.349   28.194 1.00 35.09 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.409  2.757   29.262 1.00 37.07 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.661  2.325   29.150 1.00 36.80 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.961  3.334   25.393 1.00 31.95 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.130  4.185   25.195 1.00 33.44 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.203  5.267   26.274 1.00 35.15 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.185  5.678   26.832 1.00 35.38 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.164  4.818   23.805 1.00 34.46 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.933  5.439   23.480 1.00 36.79 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.426  5.694   26.582 1.00 35.99 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.782  6.745   27.542 1.00 37.14 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.921 7.566   26.915 1.00 37.28 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.539 7.069   25.974 1.00 37.52 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.214 6.121   28.860 1.00 40.95 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.034  5.716   29.710 1.00 47.92 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.447  5.040   30.996 1.00 53.83 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.230 5.647   31.758 1.00 56.34 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.996  3.900   31.238 1.00 54.71 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.215 8.819   27.346 1.00 37.04 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.225 9.625   26.614 1.00 36.48 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.593 8.956   26.399 1.00 35.32 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.101 8.997   25.276 1.00 35.08 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.305 10.919  27.414 1.00 37.49 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.942 11.042  28.042 1.00 38.02 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.546 9.620   28.390 1.00 36.30 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.108 8.239   27.402 1.00 34.25 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.366 7.495   27.276 1.00 32.50 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.353 6.359   26.263 1.00 30.43 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.383 5.730   25.992 1.00 30.04 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.186 6.109   25.674 1.00 28.81 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.979 5.073   24.689 1.00 27.63 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.331 5.448   23.287 1.00 25.84 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.549 4.540   22.490 1.00 25.27 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.550 4.545   24.729 1.00 28.57 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.325 3.564   25.839 1.00 29.85 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.297 2.926   26.267 1.00 28.46 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.180 3.445   26.288 1.00 32.82 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.443 6.772   22.985 1.00 24.51 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.848 7.314   21.674 1.00 23.43 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.179 6.696   21.291 1.00 22.16 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.047 6.604   22.144 1.00 22.77 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.943 8.836   21.732 1.00 23.75 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.341 9.672   21.744 1.00 27.81 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.301 6.204   20.069 1.00 20.80 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.508 5.504   19.649 1.00 20.82 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.325 3.991   19.592 1.00 21.22 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.167 3.283   19.047 1.00 22.31 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.225 3.479   20.127 1.00 20.59 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 15.906 2.055   20.042 1.00 20.44 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.684 1.646   18.600 1.00 19.43 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.955 2.305   17.876 1.00 18.70 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.352 0.582   18.160 1.00 19.22 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.281 0.130   16.792 1.00 19.08 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.992 -0.666  16.561 1.00 18.29 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.593 -1.456  17.420 1.00 18.06 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.593 -0.679  16.478 1.00 20.46 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.716 0.253   16.005 1.00 21.55 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.372 -1.813  15.473 1.00 21.49 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.083 -0.369  15.925 1.00 23.12 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.343 -0.418  15.409 1.00 17.69 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.189 -1.138  14.885 1.00 17.65 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.720 -1.946  13.691 1.00 18.72 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.444 -1.429  12.846 1.00 17.73 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.061 -0.198  14.451 1.00 17.00 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.856 -0.795  13.637 1.00 17.40 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.983  -1.709  14.475 1.00 17.11 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.931  0.321   13.163 1.00 17.59 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.414 -3.235  13.677 1.00 19.95 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.867 -4.139  12.660 1.00 21.47 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.723 -4.982  12.155 1.00 23.15 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.839 -5.357  12.904 1.00 22.33 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.887 -5.121  13.247 1.00 23.11 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.230 -4.562  13.639 1.00 27.55 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.119 -5.682  14.145 1.00 31.16 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.493 -6.537  13.023 1.00 35.66 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.599 -6.391  12.303 1.00 39.56 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.825 -7.177  11.261 1.00 40.78 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.508 -5.484  12.644 1.00 40.09 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.801 -5.362  10.888 1.00 24.81 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.894 -6.316  10.283 1.00 26.75 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.824 -7.475  9.794  1.00 29.15 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.004 -7.508  10.184 1.00 29.28 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.142 -5.661  9.131  1.00 27.16 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.214 -5.145  7.773  1.00 30.54 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.328 -8.413  8.949  1.00 30.59 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.192 -9.494  8.438  1.00 32.11 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.253 -8.987  7.453  1.00 32.65 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.201 -9.721  7.167  1.00 33.40 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.357 -10.595 7.759  1.00 34.70 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.660 -10.101 6.501  1.00 40.42 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.666 -11.064 5.918  1.00 47.64 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.471  -11.021 6.237  1.00 49.83 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.136 -11.934 5.026  1.00 48.69 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.075 -7.766  6.899  1.00 31.81 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.990 -7.189  5.897  1.00 31.17 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.103 -6.335  6.469  1.00 29.05 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.925 -5.841  5.699  1.00 29.57 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.228 -6.357  4.843  1.00 32.79 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.014 -7.034  4.291  1.00 37.43 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.794 -6.939  4.924  1.00 40.08 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.873 -7.798  3.182  1.00 39.53 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.945 -7.645  4.187  1.00 41.14 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.553 -8.201  3.140  1.00 40.99 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.077 -6.093  7.778  1.00 26.42 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.073 -5.279  8.443  1.00 24.20 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.509 -4.126  9.243  1.00 21.88 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.365 -4.160  9.700  1.00 21.03 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.336 -3.086  9.411  1.00 20.81 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.989 -1.909  10.179 1.00 20.20 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.970 -1.040  9.453  1.00 19.41 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.187 -0.661  8.296  1.00 19.71 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.261 -1.119  10.553 1.00 20.58 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.898 0.154   11.299 1.00 21.17 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.183 -1.977  11.402 1.00 21.39 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.836 -0.788  10.105 1.00 18.13 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.753 0.044   9.579  1.00 17.79 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.940 1.525   10.018 1.00 17.61 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.763 2.460   9.227  1.00 17.82 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.356 -0.474  10.046 1.00 17.57 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.231 0.367   9.456  1.00 18.02 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.155 -1.955  9.733  1.00 17.65 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.236 1.714   11.295 1.00 16.56 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.357 3.038   11.865 1.00 16.69 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.652 3.014   13.350 1.00 16.03 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.033 1.973   13.895 1.00 15.93 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.547 4.188   13.997 1.00 14.97 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.858 4.322   15.402 1.00 15.40 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.752 5.034   16.160 1.00 16.46 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.128 5.934   15.613 1.00 16.85 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.215 5.056   15.608 1.00 15.72 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.274 6.412   14.875 1.00 15.31 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.436 4.159   15.247 1.00 16.40 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.489 7.246   15.273 1.00 15.66 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.563 4.709   17.456 1.00 16.08 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.578 5.375   18.302 1.00 16.22 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.881 6.879   18.347 1.00 16.51 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.051 7.272   18.445 1.00 16.09 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.477 4.777   19.735 1.00 16.69 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.433 5.542   20.566 1.00 17.08 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.142 3.285   19.695 1.00 17.39 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.856 7.696   18.146 1.00 17.33 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.038 9.135   18.124 1.00 20.07 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.927 9.879   18.858 1.00 22.64 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.144 11.017  19.251 1.00 22.21 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.186 9.636   16.687 1.00 22.41 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.180 11.055  16.617 1.00 26.06 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.726  9.284   18.987 1.00 25.18 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.588  9.898   19.696 1.00 28.50 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.839  8.802   20.504 1.00 30.90 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.141  7.619   20.357 1.00 31.44 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.619  10.714  18.742 1.00 30.65 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.655  9.851   18.135 1.00 32.04 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.326  11.551  17.684 1.00 31.24 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.845  9.188   21.293 1.00 32.20 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.027  8.259   22.050 1.00 34.67 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.118  8.939   23.056 1.00 36.94 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.076  10.167  23.124 1.00 37.22 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.423  8.139   23.862 1.00 38.68 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.521  8.630   24.904 1.00 40.78 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.082  8.193   24.693 1.00 42.72 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.661  8.019   23.553 1.00 44.05 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.326  7.993   25.775 1.00 42.76 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.085 7.579   25.747 1.00 43.33 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.325 6.157   25.227 1.00 42.09 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.450 5.825   24.843 1.00 42.91 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.947 8.577   24.981 1.00 46.39 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -1.023 9.928   25.647 1.00 51.80 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.278 10.021  26.854 1.00 53.60 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.825 11.001  24.874 1.00 52.20 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.686  5.307   25.318 1.00 39.72 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.576  3.943   24.826 1.00 38.57 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.985  3.808   23.368 1.00 37.52 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.714  2.779   22.754 1.00 38.30 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.648  4.841   22.797 1.00 35.43 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.135  4.862   21.422 1.00 34.03 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.666  5.065   21.391 1.00 31.99 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.236  5.570   22.357 1.00 32.94 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.474  6.010   20.632 1.00 34.53 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.038 6.040   20.579 1.00 36.18 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.530 7.412   20.222 1.00 36.54 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.554 5.033   19.590 1.00 37.30 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.318  4.680   20.270 1.00 28.66 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.741  4.825   20.029 1.00 25.84 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.914  5.216   18.550 1.00 24.84 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.277  4.619   17.685 1.00 25.51 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.570  3.560   20.439 1.00 25.20 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.043  2.284   19.796 1.00 25.30 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.068  3.730   20.157 1.00 24.86 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.719  6.252   18.294 1.00 22.82 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.033  6.757   16.969 1.00 21.42 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.454  6.414   16.560 1.00 20.50 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.362  6.447   17.389 1.00 20.95 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.649  6.031   15.292 1.00 18.94 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.956  5.612   14.767 1.00 17.48 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.312 6.475   13.548 1.00 16.54 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.477  6.666   12.662 1.00 16.65 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.941  4.110   14.373 1.00 16.18 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.441  3.125   15.417 1.00 16.07 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.305 2.585   16.358 1.00 15.77 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.131  2.661   15.388 1.00 16.62 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.854  1.655   17.290 1.00 15.78 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.683  1.713   16.318 1.00 16.48 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.549  1.217   17.263 1.00 15.72 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.512 7.050   13.547 1.00 15.13 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.975 7.849   12.428 1.00 14.94 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.454 6.839   11.410 1.00 16.10 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.374 6.081   11.705 1.00 14.96 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.138 8.752   12.857 1.00 14.51 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.808 6.787   10.231 1.00 17.87 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.161 5.850   9.167  1.00 19.75 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.509 6.189   8.530  1.00 20.35 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.844 7.369   8.421  1.00 20.90 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.074 5.872   8.094  1.00 23.00 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.262 4.825   7.021  1.00 30.22 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.377 3.645   7.368  1.00 29.42 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.309 5.197   5.825  1.00 35.71 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.296 5.159   8.125  1.00 20.22 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.581 5.359   7.428  1.00 20.60 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.665 4.556   6.070  1.00 21.76 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.703 4.578   5.406  1.00 22.42 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.800 5.041   8.330  1.00 19.87 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.698 5.756   9.681  1.00 19.84 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.978 3.522   8.512  1.00 19.72 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.595 3.864   5.667  1.00 21.94 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.626 3.015   4.475  1.00 23.35 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.694 3.786   3.149  1.00 25.55 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.145 3.228   2.151  1.00 26.00 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.460 2.014   4.473  1.00 23.46 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.372 1.181   5.736  1.00 23.68 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.083 0.377   5.772  1.00 23.87 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.921 1.197   6.146  1.00 21.92 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.685  0.727   6.254  1.00 20.95 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.435  -0.561  6.038  1.00 21.54 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.689  1.534   6.606  1.00 17.76 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.296 5.064   3.142  1.00 26.42 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.356 5.903   1.949  1.00 27.36 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.767 6.449   1.690  1.00 28.58 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.060 6.852   0.555  1.00 28.02 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.372 7.080   2.059  1.00 29.03 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.705 8.042   3.183  1.00 34.04 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.862 7.577   4.329  1.00 34.39 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.785 9.269   2.918  1.00 36.58 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.627 6.496   2.742  1.00 29.41 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.002 7.002   2.660  1.00 30.36 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.905 5.995   1.973  1.00 32.55 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.681 5.305   2.635  1.00 33.02 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.531 7.355   4.057  1.00 29.90 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.624 8.284   4.861  1.00 30.58 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.096 8.422   6.279  1.00 30.84 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.446 9.616   4.174  1.00 30.95 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.788 5.901   0.631  1.00 33.73 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.529 4.941   -0.194 1.00 35.09 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.029 5.168   -0.212 1.00 36.55 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.754 4.206   -0.421 1.00 36.35 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.987 4.866   -1.644 1.00 34.85 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.471 4.717   -1.836 1.00 36.08 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.138 4.417   -3.292 1.00 36.72 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.894 3.611   -0.976 1.00 36.62 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.502 6.414   0.043  1.00 37.73 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.937 6.744   0.060  1.00 39.76 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.719 6.116   1.222  1.00 42.82 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.950 6.127   1.202  1.00 43.19 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.168 8.268   0.025  1.00 39.15 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.420 9.006   1.097  1.00 39.13 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.130 9.449   1.043  1.00 39.75 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.908 9.349   2.399  1.00 38.83 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.783 10.038  2.236  1.00 39.87 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.858 9.991   3.086  1.00 39.56 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.135 9.185   3.050  1.00 39.16 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.001 10.466  4.385  1.00 40.29 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.274 9.657   4.339  1.00 39.94 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.222 10.302  4.986  1.00 40.37 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.025 5.572   2.228  1.00 44.93 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.678 4.921   3.364  1.00 47.81 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.483 3.665   2.959  1.00 52.03 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.354 3.238   3.711  1.00 52.40 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.637 4.552   4.432  1.00 47.11 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.050 5.707   5.229  1.00 47.40 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.888 5.234   6.067  1.00 47.92 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.086 6.340   6.121  1.00 47.38 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.186 3.073   1.782  1.00 55.00 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.864 1.879   1.272  1.00 58.08 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.792 2.173   0.091  1.00 61.27 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.150 1.237   -0.626 1.00 62.01 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.825 0.867   0.786  1.00 60.12 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.905 0.339   1.852  1.00 64.78 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.391 0.061   2.967  1.00 65.97 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.701 0.177   1.565  1.00 66.60 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.171 3.441   -0.139 1.00 63.17 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.027 3.779   -1.279 1.00 65.71 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.881 5.032   -1.035 1.00 67.06 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.748 5.371   -1.855 1.00 67.78 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.169 3.953   -2.548 1.00 69.58 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.014 4.933   -2.374 1.00 75.95 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.090 5.063   -3.571 1.00 83.86 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.914 6.200   -4.066 1.00 85.86 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.543 4.028   -4.016 1.00 86.68 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B58 B 2 .   ? 10.208 13.125  22.301 1.00 36.64 ? 201 A1B58 A N1  1 
HETATM 1079 C  C4  . A1B58 B 2 .   ? 9.420  12.084  24.383 1.00 39.07 ? 201 A1B58 A C4  1 
HETATM 1080 C  C5  . A1B58 B 2 .   ? 8.573  10.934  24.882 1.00 39.63 ? 201 A1B58 A C5  1 
HETATM 1081 C  C6  . A1B58 B 2 .   ? 7.596  11.156  25.853 1.00 39.83 ? 201 A1B58 A C6  1 
HETATM 1082 C  C7  . A1B58 B 2 .   ? 6.858  10.111  26.383 1.00 39.62 ? 201 A1B58 A C7  1 
HETATM 1083 C  C8  . A1B58 B 2 .   ? 7.067  8.823   25.939 1.00 39.53 ? 201 A1B58 A C8  1 
HETATM 1084 C  C10 . A1B58 B 2 .   ? 8.770  9.618   24.467 1.00 40.20 ? 201 A1B58 A C10 1 
HETATM 1085 C  C13 . A1B58 B 2 .   ? 11.683 15.478  21.421 1.00 35.65 ? 201 A1B58 A C13 1 
HETATM 1086 CL CL  . A1B58 B 2 .   ? 10.037 9.242   23.341 1.00 40.94 ? 201 A1B58 A CL  1 
HETATM 1087 C  C9  . A1B58 B 2 .   ? 8.023  8.568   24.973 1.00 39.67 ? 201 A1B58 A C9  1 
HETATM 1088 C  C3  . A1B58 B 2 .   ? 9.252  12.365  22.897 1.00 37.95 ? 201 A1B58 A C3  1 
HETATM 1089 O  O1  . A1B58 B 2 .   ? 8.280  11.945  22.284 1.00 37.76 ? 201 A1B58 A O1  1 
HETATM 1090 C  C2  . A1B58 B 2 .   ? 9.972  13.648  20.950 1.00 36.24 ? 201 A1B58 A C2  1 
HETATM 1091 C  C11 . A1B58 B 2 .   ? 11.476 13.473  22.957 1.00 36.11 ? 201 A1B58 A C11 1 
HETATM 1092 C  C12 . A1B58 B 2 .   ? 12.418 14.275  22.064 1.00 35.86 ? 201 A1B58 A C12 1 
HETATM 1093 C  C14 . A1B58 B 2 .   ? 12.478 13.641  20.650 1.00 35.84 ? 201 A1B58 A C14 1 
HETATM 1094 C  C1  . A1B58 B 2 .   ? 11.169 14.442  20.374 1.00 35.71 ? 201 A1B58 A C1  1 
HETATM 1095 C  C   . A1B58 B 2 .   ? 10.821 14.806  18.932 1.00 34.88 ? 201 A1B58 A C   1 
HETATM 1096 O  O   . A1B58 B 2 .   ? 10.528 15.962  18.631 1.00 34.81 ? 201 A1B58 A O   1 
HETATM 1097 N  N   . A1B58 B 2 .   ? 10.835 13.828  18.041 1.00 34.20 ? 201 A1B58 A N   1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 11.021 -5.339  5.642  1.00 37.99 2 202 ZN    A ZN  1 
HETATM 1099 S  S   . DMS   D 4 .   ? 19.960 -0.163  20.479 1.00 82.60 ? 203 DMS   A S   1 
HETATM 1100 O  O   . DMS   D 4 .   ? 18.515 -0.401  20.104 1.00 82.51 ? 203 DMS   A O   1 
HETATM 1101 C  C1  . DMS   D 4 .   ? 20.038 1.012   21.862 1.00 82.50 ? 203 DMS   A C1  1 
HETATM 1102 C  C2  . DMS   D 4 .   ? 20.696 0.950   19.254 1.00 82.57 ? 203 DMS   A C2  1 
HETATM 1103 O  O   . HOH   E 5 .   ? 8.097  -4.796  1.375  1.00 45.91 ? 301 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 14.105 20.366  8.105  1.00 26.47 ? 302 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 8.922  1.802   3.062  1.00 22.48 ? 303 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 19.919 8.361   18.911 1.00 22.81 ? 304 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.597 21.397  8.102  1.00 31.19 ? 305 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 10.760 7.340   4.499  1.00 38.60 ? 306 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 30.523 20.346  10.742 1.00 47.80 ? 307 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 8.304  19.376  18.283 1.00 35.89 ? 308 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 11.202 11.069  11.308 1.00 15.63 ? 309 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 14.840 2.050   23.249 1.00 25.10 ? 310 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 22.687 -1.990  4.478  1.00 39.68 ? 311 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 18.562 3.895   26.573 1.00 35.44 ? 312 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 17.322 20.768  9.655  1.00 36.99 ? 313 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 29.824 10.469  19.499 1.00 45.28 ? 314 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 11.650 -6.332  31.983 1.00 48.60 ? 315 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 33.847 13.431  7.433  1.00 41.97 ? 316 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 0.397  -1.222  16.718 1.00 23.47 ? 317 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 15.986 -11.934 5.605  1.00 41.51 ? 318 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 10.993 1.494   33.742 1.00 28.73 ? 319 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 17.969 0.041   30.286 1.00 30.87 ? 320 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 5.280  -2.284  24.510 1.00 30.50 ? 321 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 7.055  2.769   32.992 1.00 29.80 ? 322 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 18.028 18.494  17.379 1.00 27.12 ? 323 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 10.294 4.141   3.386  1.00 23.20 ? 324 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 5.627  1.044   6.733  1.00 33.64 ? 325 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 6.367  -6.457  29.364 1.00 34.33 ? 326 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 9.727  3.836   34.025 1.00 43.94 ? 327 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 12.954 9.929   9.544  1.00 13.90 ? 328 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 4.096  -5.842  6.567  1.00 28.52 ? 329 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 30.540 20.127  17.252 1.00 45.70 ? 330 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 7.164  25.543  14.154 1.00 37.86 ? 331 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 9.371  -8.522  9.403  1.00 28.32 ? 332 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 27.808 16.181  3.127  1.00 40.57 ? 333 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 11.751 20.732  12.368 1.00 18.45 ? 334 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 0.248  0.360   24.494 1.00 30.34 ? 335 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 35.068 8.464   7.117  1.00 29.07 ? 336 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 4.145  5.235   25.356 1.00 50.06 ? 337 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 14.834 -5.118  17.282 1.00 28.06 ? 338 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 14.376 13.947  3.768  1.00 32.28 ? 339 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 28.233 2.968   2.537  1.00 44.93 ? 340 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 17.305 2.206   23.644 1.00 29.70 ? 341 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 19.329 23.454  15.483 1.00 26.21 ? 342 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 15.785 23.382  14.014 1.00 35.96 ? 343 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 22.074 18.606  6.131  1.00 26.52 ? 344 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 11.599 16.187  5.042  1.00 64.58 ? 345 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 2.538  2.237   27.446 1.00 36.95 ? 346 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 1.473  -3.279  17.885 1.00 30.66 ? 347 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 4.856  7.272   28.492 1.00 37.49 ? 348 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 15.726 -5.356  1.732  1.00 27.56 ? 349 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 22.502 18.240  20.064 1.00 42.84 ? 350 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 24.291 6.935   20.547 1.00 44.01 ? 351 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 12.072 -8.624  13.418 1.00 36.96 ? 352 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 22.012 8.512   20.619 1.00 35.27 ? 353 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 11.362 13.686  1.384  1.00 47.50 ? 354 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 5.662  -8.421  14.360 1.00 28.65 ? 355 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? -0.565 14.818  7.251  1.00 35.86 ? 356 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 2.696  23.076  21.594 1.00 34.34 ? 357 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 6.553  -6.284  3.140  1.00 46.64 ? 358 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 20.783 21.131  17.958 1.00 53.52 ? 359 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 9.402  20.695  10.801 1.00 43.55 ? 360 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 18.123 12.318  1.898  1.00 30.40 ? 361 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 5.965  22.642  11.073 1.00 35.83 ? 362 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 4.516  -2.181  29.053 1.00 32.41 ? 363 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? -1.891 -0.473  4.123  1.00 58.32 ? 364 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 12.375 22.824  13.872 1.00 40.42 ? 365 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? -1.323 14.757  12.063 1.00 40.60 ? 366 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 3.261  11.699  18.442 1.00 39.31 ? 367 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 16.606 -8.883  25.574 1.00 46.44 ? 368 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 7.174  6.679   34.341 1.00 43.16 ? 369 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 9.281  -9.479  12.650 1.00 32.68 ? 370 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 10.011 16.303  25.497 1.00 40.48 ? 371 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 20.639 -3.578  22.693 1.00 45.81 ? 372 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 9.433  24.424  12.943 1.00 35.88 ? 373 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 35.537 20.282  16.548 0.50 61.83 ? 374 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 9.782  14.257  28.349 1.00 35.53 ? 375 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   ? 0.8336 0.3491 0.3947 -0.0308 -0.2541 0.0091  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.7786 0.3506 0.4495 -0.0290 -0.2823 0.0227  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.7032 0.3516 0.4707 -0.0135 -0.2632 0.0253  7   SER   A C   
4    O  O   . SER   A 1   ? 0.7112 0.3635 0.4559 -0.0087 -0.2425 0.0198  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.8235 0.3421 0.4859 -0.0558 -0.3498 0.0450  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.8879 0.3587 0.4989 -0.0716 -0.3760 0.0546  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.6315 0.3332 0.5004 -0.0065 -0.2643 0.0325  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.5712 0.3310 0.5238 0.0059  -0.2383 0.0333  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.5078 0.3168 0.5302 0.0170  -0.2086 0.0283  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.5179 0.3301 0.5133 0.0206  -0.1951 0.0183  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.4433 0.2841 0.5543 0.0215  -0.1953 0.0361  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.4080 0.2818 0.5772 0.0288  -0.1616 0.0314  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.3731 0.2678 0.5837 0.0342  -0.1185 0.0270  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.3676 0.2566 0.5900 0.0337  -0.1214 0.0328  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.3868 0.2608 0.6370 0.0249  -0.1876 0.0501  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.3489 0.2584 0.5740 0.0368  -0.0782 0.0171  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.3396 0.2505 0.5902 0.0369  -0.0314 0.0116  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.3251 0.2366 0.6727 0.0396  -0.0121 0.0227  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.3164 0.2334 0.6812 0.0398  -0.0170 0.0243  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.3607 0.2710 0.5373 0.0309  0.0010  -0.0065 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.3781 0.2943 0.4758 0.0297  -0.0198 -0.0125 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.3702 0.2628 0.5476 0.0246  0.0474  -0.0131 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.3940 0.3149 0.4398 0.0224  -0.0029 -0.0210 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.3193 0.2242 0.7386 0.0425  0.0118  0.0323  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.2937 0.1971 0.8255 0.0469  0.0392  0.0469  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.3204 0.1972 0.8488 0.0453  0.1128  0.0337  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.3306 0.1940 0.8729 0.0466  0.1339  0.0350  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.2510 0.1625 0.8908 0.0511  0.0043  0.0771  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2552 0.1751 0.8879 0.0455  -0.0716 0.0926  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2549 0.1824 0.9349 0.0430  -0.0944 0.1048  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2839 0.1945 0.8542 0.0397  -0.1186 0.0951  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2712 0.1920 0.9301 0.0328  -0.1646 0.1189  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.3138 0.2126 0.8603 0.0293  -0.1852 0.1092  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.3170 0.2185 0.9027 0.0247  -0.2091 0.1204  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3655 0.2416 0.9086 0.0095  -0.2753 0.1330  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.3339 0.1940 0.8312 0.0398  0.1528  0.0203  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.3666 0.1807 0.8350 0.0317  0.2269  0.0058  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.3613 0.1593 0.9075 0.0344  0.2712  0.0125  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.3485 0.1637 0.8913 0.0339  0.2492  0.0133  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.4300 0.2216 0.7513 0.0139  0.2337  -0.0180 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.4394 0.2575 0.7114 0.0112  0.1921  -0.0210 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.4724 0.1981 0.7446 -0.0023 0.3077  -0.0324 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.3567 0.1230 0.9879 0.0393  0.3341  0.0203  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.3523 0.0986 1.0764 0.0436  0.3880  0.0297  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.3221 0.1224 1.1514 0.0540  0.3317  0.0543  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.3081 0.1511 1.1890 0.0607  0.2640  0.0736  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.3148 0.1090 1.1515 0.0511  0.3497  0.0522  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2691 0.1103 1.1982 0.0578  0.2929  0.0756  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2673 0.1358 1.0831 0.0509  0.2201  0.0629  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2451 0.1329 1.0862 0.0507  0.1898  0.0707  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2880 0.1121 1.3131 0.0607  0.3498  0.0858  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3384 0.1384 1.5039 0.0708  0.4209  0.1052  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3210 0.1454 1.5876 0.0801  0.3959  0.1299  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3749 0.1204 1.5508 0.0687  0.5146  0.0960  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.2779 0.1474 0.9803 0.0461  0.1929  0.0463  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.2766 0.1663 0.8792 0.0415  0.1352  0.0356  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.2548 0.1661 0.8403 0.0441  0.0724  0.0431  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.2457 0.1542 0.8613 0.0469  0.0751  0.0501  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.3160 0.1813 0.7851 0.0300  0.1629  0.0093  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.3369 0.1706 0.7946 0.0220  0.2153  0.0013  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.3313 0.1793 0.8306 0.0248  0.2024  0.0087  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.3864 0.1666 0.7810 0.0084  0.2780  -0.0137 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.3596 0.1740 0.8440 0.0164  0.2522  0.0017  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.4270 0.1641 0.7915 -0.0034 0.3271  -0.0216 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.4214 0.1779 0.8354 0.0019  0.3154  -0.0136 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.4742 0.1832 0.8592 -0.0103 0.3677  -0.0208 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.2412 0.1666 0.7781 0.0421  0.0192  0.0424  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.2399 0.1701 0.7316 0.0409  -0.0364 0.0460  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.2691 0.1982 0.6446 0.0383  -0.0443 0.0261  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.2752 0.2066 0.6392 0.0374  -0.0473 0.0230  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.2202 0.1538 0.7796 0.0378  -0.0940 0.0712  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2842 0.2031 0.7674 0.0308  -0.1518 0.0727  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.3091 0.2158 0.8455 0.0196  -0.2152 0.1007  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.3917 0.2688 0.8268 0.0091  -0.2573 0.0938  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.4561 0.2971 0.8148 -0.0022 -0.2988 0.0964  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.4453 0.2822 0.8201 -0.0041 -0.3097 0.1068  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.4941 0.2953 0.7549 -0.0126 -0.3257 0.0885  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.2791 0.2053 0.5784 0.0375  -0.0441 0.0146  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.2935 0.2213 0.5030 0.0361  -0.0483 0.0014  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.2903 0.2088 0.4552 0.0371  -0.0877 0.0037  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.2971 0.2092 0.4497 0.0367  -0.0955 0.0056  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.3213 0.2486 0.4775 0.0312  -0.0154 -0.0105 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.3462 0.2803 0.4362 0.0292  -0.0211 -0.0165 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.3259 0.2404 0.5074 0.0248  0.0297  -0.0141 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.2868 0.1968 0.4195 0.0373  -0.1078 0.0028  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.3176 0.2000 0.3904 0.0354  -0.1371 0.0031  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.3247 0.2036 0.3349 0.0397  -0.1233 -0.0069 18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.3084 0.2077 0.3295 0.0425  -0.1039 -0.0103 18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.3417 0.1959 0.4329 0.0269  -0.1805 0.0161  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.3427 0.1908 0.4859 0.0204  -0.2071 0.0328  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.3295 0.1953 0.4675 0.0269  -0.1799 0.0195  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.3494 0.1949 0.2954 0.0392  -0.1331 -0.0094 19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.3671 0.2004 0.2661 0.0447  -0.1167 -0.0152 19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.3868 0.2033 0.2907 0.0420  -0.1311 -0.0140 19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.4040 0.1902 0.3077 0.0318  -0.1636 -0.0084 19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.4028 0.1883 0.2302 0.0435  -0.1157 -0.0183 19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.4216 0.2198 0.2412 0.0458  -0.1015 -0.0189 19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.4426 0.2273 0.2580 0.0390  -0.1201 -0.0162 19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.3908 0.2155 0.2145 0.0540  -0.0716 -0.0192 19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.3792 0.2156 0.2929 0.0487  -0.1114 -0.0161 20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.3871 0.2096 0.3065 0.0468  -0.1218 -0.0154 20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.4573 0.2129 0.3085 0.0401  -0.1380 -0.0178 20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.4817 0.2101 0.3336 0.0290  -0.1680 -0.0137 20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.3642 0.2168 0.3010 0.0548  -0.0970 -0.0155 20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.3635 0.2110 0.3185 0.0529  -0.1054 -0.0144 20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.3611 0.2266 0.3183 0.0608  -0.0824 -0.0124 20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.3578 0.2221 0.3326 0.0599  -0.0860 -0.0111 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.3817 0.2071 0.3280 0.0605  -0.0918 -0.0134 20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.4182 0.1929 0.3082 0.0592  -0.0948 -0.0181 20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.3508 0.1792 0.3162 0.0601  -0.0931 -0.0115 20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.4923 0.2132 0.2818 0.0433  -0.1194 -0.0228 21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.5677 0.2041 0.2702 0.0328  -0.1272 -0.0272 21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.6103 0.1996 0.2800 0.0112  -0.1751 -0.0216 21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.6503 0.1656 0.2517 -0.0059 -0.1973 -0.0218 21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.6118 0.2123 0.2569 0.0415  -0.0848 -0.0334 21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.6667 0.2579 0.2865 0.0388  -0.0825 -0.0337 21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.6460 0.3068 0.3263 0.0494  -0.0700 -0.0297 21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.7391 0.2526 0.2720 0.0242  -0.0916 -0.0371 21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.6779 0.3089 0.3162 0.0436  -0.0714 -0.0310 21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.7398 0.2823 0.2886 0.0286  -0.0840 -0.0352 21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.5994 0.2281 0.3207 0.0094  -0.1940 -0.0139 22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.6302 0.2218 0.3404 -0.0113 -0.2441 -0.0018 22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.6100 0.2404 0.4182 -0.0174 -0.2804 0.0145  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.6088 0.2243 0.4403 -0.0328 -0.3237 0.0313  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.6231 0.2266 0.3328 -0.0092 -0.2400 -0.0003 22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.6790 0.2359 0.2964 -0.0070 -0.2090 -0.0118 22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.6690 0.2395 0.2947 -0.0076 -0.2131 -0.0076 22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.7649 0.2130 0.2623 -0.0278 -0.2232 -0.0150 22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.5904 0.2709 0.4641 -0.0055 -0.2612 0.0124  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.5653 0.2844 0.5429 -0.0085 -0.2821 0.0278  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.6081 0.2806 0.5857 -0.0315 -0.3384 0.0453  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.6604 0.2745 0.5536 -0.0428 -0.3503 0.0393  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.5336 0.3045 0.5626 0.0071  -0.2434 0.0199  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.5853 0.2794 0.6614 -0.0402 -0.3730 0.0695  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.6152 0.2699 0.7126 -0.0665 -0.4376 0.0949  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.6032 0.2862 0.7787 -0.0648 -0.4369 0.1020  24  THR   A C   
137  O  O   . THR   A 18  ? 0.5825 0.3136 0.7904 -0.0430 -0.3836 0.0860  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.6101 0.2728 0.7890 -0.0784 -0.4805 0.1251  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.5551 0.2923 0.8814 -0.0601 -0.4505 0.1355  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.6515 0.2878 0.7573 -0.0800 -0.4804 0.1188  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.6175 0.2656 0.8183 -0.0909 -0.4987 0.1276  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.5994 0.2733 0.8853 -0.0918 -0.5030 0.1388  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.5143 0.2673 0.9592 -0.0719 -0.4681 0.1511  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.4894 0.2794 0.9820 -0.0569 -0.4255 0.1418  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.6525 0.2730 0.9473 -0.1284 -0.5853 0.1710  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.8098 0.3376 0.9423 -0.1519 -0.6125 0.1573  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.8686 0.3855 0.9450 -0.1430 -0.5779 0.1337  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.9088 0.3427 0.9238 -0.1862 -0.6691 0.1658  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.9635 0.3803 0.8930 -0.1699 -0.6084 0.1270  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 1.0003 0.3591 0.8796 -0.1981 -0.6630 0.1447  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.4725 0.2447 0.9953 -0.0726 -0.4814 0.1719  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.4077 0.2425 1.0788 -0.0538 -0.4387 0.1837  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.3863 0.2541 1.0246 -0.0268 -0.3556 0.1487  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.3554 0.2563 1.0742 -0.0149 -0.3102 0.1480  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.4235 0.2636 1.1605 -0.0579 -0.4628 0.2085  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.4372 0.3312 1.3340 -0.0393 -0.4135 0.2233  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.4057 0.3203 1.4464 -0.0434 -0.4257 0.2557  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.4612 0.3732 1.3360 -0.0198 -0.3536 0.2009  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.4018 0.2545 0.9198 -0.0204 -0.3372 0.1218  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.3885 0.2652 0.8612 -0.0010 -0.2711 0.0922  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.3706 0.2543 0.8279 0.0036  -0.2461 0.0795  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.3499 0.2598 0.8393 0.0145  -0.1950 0.0705  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.4372 0.2917 0.7868 0.0012  -0.2681 0.0718  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.4663 0.3191 0.8255 0.0001  -0.2779 0.0795  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.4202 0.3019 0.8764 0.0060  -0.2585 0.0911  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.5323 0.3497 0.8006 -0.0069 -0.3006 0.0739  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.3903 0.2425 0.7922 -0.0069 -0.2811 0.0792  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.3924 0.2485 0.7802 -0.0031 -0.2612 0.0689  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.3507 0.2295 0.8570 -0.0055 -0.2583 0.0873  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.3492 0.2438 0.8661 0.0021  -0.2209 0.0778  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.4328 0.2388 0.7195 -0.0139 -0.2940 0.0621  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.4566 0.2460 0.6345 -0.0045 -0.2686 0.0394  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.5019 0.2536 0.6015 -0.0096 -0.2831 0.0348  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.4510 0.2596 0.5956 0.0105  -0.2240 0.0222  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.5303 0.2800 0.5599 0.0036  -0.2453 0.0160  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.4956 0.2827 0.5562 0.0157  -0.2121 0.0100  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.4268 0.2670 0.6078 0.0187  -0.1931 0.0186  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.4991 0.3006 0.5261 0.0291  -0.1749 -0.0015 28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.4437 0.2930 0.5775 0.0292  -0.1612 0.0063  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.4723 0.3056 0.5377 0.0347  -0.1539 -0.0018 28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.3190 0.1971 0.9168 -0.0174 -0.2987 0.1162  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.2754 0.1771 1.0092 -0.0194 -0.2946 0.1397  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2430 0.1802 1.0711 -0.0030 -0.2279 0.1402  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2163 0.1706 1.1575 -0.0009 -0.2036 0.1560  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.2439 0.1313 1.0568 -0.0408 -0.3675 0.1779  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.2305 0.1715 1.0157 0.0065  -0.1986 0.1255  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.1923 0.1495 1.0320 0.0189  -0.1313 0.1206  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.2099 0.1602 0.9251 0.0261  -0.0872 0.0864  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.2044 0.1546 0.9143 0.0314  -0.0491 0.0787  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.1931 0.1570 1.1141 0.0192  -0.1453 0.1426  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.1864 0.1633 1.2701 0.0132  -0.1719 0.1832  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.1978 0.1848 1.3707 0.0175  -0.1326 0.1913  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.1561 0.1296 1.2836 0.0010  -0.2403 0.2123  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.2302 0.1723 0.8477 0.0245  -0.0967 0.0691  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.2416 0.1790 0.7487 0.0281  -0.0698 0.0441  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.2392 0.1733 0.7488 0.0290  -0.0065 0.0342  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2286 0.1589 0.7838 0.0272  0.0185  0.0382  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.2537 0.1831 0.6922 0.0264  -0.0922 0.0361  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2914 0.2197 0.6350 0.0294  -0.0681 0.0175  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.3146 0.2417 0.5954 0.0323  -0.0775 0.0103  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.3022 0.2231 0.6068 0.0293  -0.0825 0.0144  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.2495 0.1771 0.7004 0.0287  0.0197  0.0215  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2629 0.1692 0.6767 0.0223  0.0761  0.0097  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2895 0.1919 0.5925 0.0160  0.0677  -0.0030 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.3181 0.2051 0.5894 0.0080  0.0875  -0.0068 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2807 0.1749 0.7011 0.0216  0.1059  0.0072  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.3294 0.1854 0.6736 0.0081  0.1582  -0.0074 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2424 0.1400 0.7887 0.0284  0.1207  0.0244  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2733 0.1888 0.5262 0.0193  0.0365  -0.0059 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2727 0.1899 0.4460 0.0150  0.0266  -0.0110 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.2529 0.1861 0.4048 0.0247  -0.0111 -0.0097 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.2436 0.1794 0.4152 0.0297  -0.0254 -0.0081 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2908 0.1885 0.4083 0.0009  0.0550  -0.0166 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.3079 0.2117 0.3579 -0.0059 0.0374  -0.0149 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.3253 0.2262 0.3412 -0.0140 0.0305  -0.0096 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.3040 0.2199 0.3258 -0.0049 0.0225  -0.0138 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.3369 0.2496 0.3147 -0.0184 0.0111  -0.0023 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.3265 0.2486 0.3071 -0.0127 0.0077  -0.0055 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2940 0.2162 0.3271 0.0015  0.0196  -0.0167 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.3310 0.2662 0.2879 -0.0147 -0.0067 0.0009  33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.3056 0.2381 0.3037 -0.0002 0.0066  -0.0139 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.3167 0.2566 0.2809 -0.0081 -0.0053 -0.0047 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2475 0.1854 0.3607 0.0267  -0.0244 -0.0089 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2453 0.1869 0.3315 0.0354  -0.0469 -0.0083 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.2574 0.2066 0.3072 0.0350  -0.0442 -0.0038 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.2581 0.2077 0.3067 0.0297  -0.0385 0.0002  34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2439 0.1719 0.3446 0.0414  -0.0717 -0.0072 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2814 0.2049 0.3968 0.0408  -0.0737 -0.0051 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.3276 0.2487 0.4079 0.0455  -0.0720 -0.0043 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.3528 0.2735 0.4453 0.0438  -0.0685 -0.0020 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.3006 0.2200 0.3483 0.0513  -0.0709 -0.0039 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.2603 0.2151 0.2875 0.0398  -0.0482 -0.0013 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.2521 0.2179 0.2670 0.0407  -0.0471 0.0096  35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.2391 0.1981 0.2446 0.0544  -0.0480 0.0104  35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.2419 0.2021 0.2368 0.0552  -0.0462 0.0090  35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2843 0.2608 0.2854 0.0250  -0.0433 0.0176  35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.3664 0.3570 0.3697 0.0202  -0.0504 0.0374  35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.3887 0.3832 0.4114 0.0323  -0.0517 0.0446  35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.4210 0.4154 0.4090 0.0029  -0.0559 0.0481  35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.2265 0.1710 0.2313 0.0643  -0.0460 0.0123  36  SER   A N   
241  C  CA  A SER   A 30  ? 0.2447 0.1648 0.2301 0.0761  -0.0359 0.0116  36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.2420 0.1621 0.2279 0.0763  -0.0355 0.0119  36  SER   A CA  
243  C  C   . SER   A 30  ? 0.2295 0.1702 0.2307 0.0800  -0.0222 0.0257  36  SER   A C   
244  O  O   . SER   A 30  ? 0.2447 0.1667 0.2281 0.0867  -0.0099 0.0230  36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2741 0.1661 0.2527 0.0840  -0.0289 0.0114  36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2604 0.1563 0.2438 0.0845  -0.0274 0.0135  36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2797 0.1972 0.2942 0.0871  -0.0210 0.0275  36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2787 0.1619 0.2591 0.0790  -0.0423 0.0056  36  SER   A OG  
249  N  N   . SER   A 31  ? 0.2000 0.1747 0.2338 0.0730  -0.0264 0.0431  37  SER   A N   
250  C  CA  . SER   A 31  ? 0.1962 0.1945 0.2588 0.0728  -0.0213 0.0634  37  SER   A CA  
251  C  C   . SER   A 31  ? 0.1854 0.1910 0.2305 0.0645  -0.0256 0.0581  37  SER   A C   
252  O  O   . SER   A 31  ? 0.1822 0.1994 0.2469 0.0670  -0.0182 0.0711  37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2282 0.2549 0.3258 0.0601  -0.0363 0.0884  37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.2998 0.3302 0.3692 0.0378  -0.0545 0.0842  37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1854 0.1845 0.2020 0.0546  -0.0352 0.0418  38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1889 0.1899 0.1884 0.0474  -0.0368 0.0353  38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.2204 0.1961 0.1967 0.0575  -0.0326 0.0187  38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.2332 0.2089 0.1976 0.0538  -0.0329 0.0146  38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1865 0.1882 0.1716 0.0290  -0.0437 0.0298  38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1900 0.2026 0.1748 0.0095  -0.0531 0.0480  38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.2299 0.2225 0.1809 -0.0113 -0.0502 0.0388  38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.2539 0.2387 0.1835 -0.0195 -0.0448 0.0319  38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2868 0.2474 0.1762 -0.0444 -0.0404 0.0305  38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2835 0.2204 0.1420 -0.0658 -0.0416 0.0359  38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.2746 0.2257 0.1456 -0.0504 -0.0331 0.0238  38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.2471 0.1955 0.2113 0.0666  -0.0322 0.0105  39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.2778 0.1897 0.2095 0.0690  -0.0383 -0.0022 39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.2852 0.2040 0.2265 0.0599  -0.0541 -0.0085 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.3068 0.2079 0.2310 0.0584  -0.0620 -0.0129 39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.3051 0.1929 0.2068 0.0750  -0.0238 -0.0023 39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.4039 0.2392 0.2542 0.0717  -0.0354 -0.0134 39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.4122 0.2166 0.2442 0.0678  -0.0508 -0.0183 39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.4522 0.2747 0.2790 0.0698  -0.0333 -0.0153 39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.2641 0.2035 0.2343 0.0531  -0.0553 -0.0076 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.2541 0.1953 0.2465 0.0462  -0.0592 -0.0119 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.2608 0.1955 0.2846 0.0449  -0.0669 -0.0125 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.2592 0.1962 0.2862 0.0455  -0.0644 -0.0110 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.2415 0.1991 0.2377 0.0354  -0.0428 -0.0107 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.2543 0.2202 0.2279 0.0310  -0.0377 -0.0077 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.2581 0.2235 0.2198 0.0129  -0.0245 -0.0065 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.2604 0.2169 0.2313 0.0357  -0.0425 -0.0124 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.2701 0.1982 0.3262 0.0426  -0.0760 -0.0119 41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.2768 0.2028 0.3831 0.0403  -0.0818 -0.0079 41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.2837 0.2150 0.4425 0.0374  -0.0701 -0.0044 41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.2891 0.2166 0.4489 0.0377  -0.0792 -0.0022 41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.2815 0.1833 0.3859 0.0396  -0.1163 -0.0030 41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.2664 0.1686 0.4305 0.0357  -0.1268 0.0050  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.2942 0.1697 0.4262 0.0329  -0.1520 0.0058  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.2550 0.1573 0.4890 0.0309  -0.1444 0.0184  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.2926 0.2279 0.4945 0.0344  -0.0445 -0.0035 42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.2929 0.2259 0.5564 0.0328  -0.0201 0.0009  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.2909 0.2251 0.6425 0.0341  -0.0267 0.0141  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.2824 0.2164 0.6370 0.0327  -0.0230 0.0134  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.3129 0.2340 0.5448 0.0248  0.0276  -0.0090 42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.3091 0.2148 0.6072 0.0235  0.0674  -0.0055 42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.3397 0.2604 0.4977 0.0202  0.0268  -0.0164 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.2964 0.2326 0.7255 0.0357  -0.0399 0.0294  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.2991 0.2398 0.8343 0.0354  -0.0485 0.0489  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.3174 0.2583 0.9533 0.0389  -0.0074 0.0606  43  SER   A C   
300  O  O   . SER   A 37  ? 0.3160 0.2511 0.9378 0.0409  0.0146  0.0553  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.3025 0.2404 0.8547 0.0300  -0.1159 0.0663  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.3304 0.2620 0.8726 0.0280  -0.1439 0.0734  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.3215 0.2662 1.0632 0.0399  0.0085  0.0770  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.3305 0.2711 1.1871 0.0450  0.0577  0.0915  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.3345 0.2911 1.3007 0.0464  0.0129  0.1233  44  SER   A C   
306  O  O   . SER   A 38  ? 0.3305 0.2975 1.3129 0.0393  -0.0576 0.1412  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.3247 0.2607 1.2604 0.0458  0.0987  0.0990  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.3376 0.2931 1.3206 0.0420  0.0406  0.1175  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.3462 0.2977 1.3810 0.0528  0.0519  0.1318  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.3424 0.3089 1.4978 0.0537  0.0112  0.1676  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3294 0.2972 1.6581 0.0630  0.0694  0.1937  45  THR   A C   
312  O  O   . THR   A 39  ? 0.3532 0.2972 1.6756 0.0687  0.1546  0.1754  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.3760 0.3362 1.4644 0.0540  -0.0042 0.1596  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.3865 0.3302 1.4999 0.0628  0.0726  0.1506  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.4320 0.3844 1.3457 0.0480  -0.0331 0.1285  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.2909 0.2795 1.7737 0.0624  0.0257  0.2383  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.2517 0.2441 1.9252 0.0733  0.0830  0.2698  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.2653 0.2408 1.9510 0.0832  0.1337  0.2654  46  THR   A C   
319  O  O   . THR   A 40  ? 0.2725 0.2215 2.0104 0.0942  0.2312  0.2587  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.2151 0.2394 2.0694 0.0664  0.0096  0.3276  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.2601 0.2905 2.0672 0.0525  -0.0887 0.3426  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.2049 0.2403 2.0844 0.0580  -0.0164 0.3358  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.2667 0.2494 1.9008 0.0779  0.0707  0.2696  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.2613 0.2291 1.9020 0.0861  0.1087  0.2667  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3216 0.2535 1.7898 0.0874  0.1764  0.2141  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.3694 0.2962 1.6848 0.0792  0.1603  0.1816  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.2662 0.2483 1.8893 0.0770  0.0162  0.2865  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3161 0.2188 1.8110 0.0958  0.2508  0.2084  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3827 0.2406 1.7179 0.0919  0.3140  0.1633  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.4057 0.2726 1.6163 0.0856  0.2560  0.1483  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3805 0.2669 1.6612 0.0891  0.2117  0.1740  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4012 0.2101 1.8134 0.1006  0.4235  0.1640  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.5326 0.2871 1.7984 0.0933  0.4783  0.1273  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.6676 0.3743 1.7594 0.0769  0.5201  0.0858  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6968 0.3994 1.7876 0.0735  0.5342  0.0823  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.7206 0.3885 1.6613 0.0639  0.5359  0.0561  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.4492 0.3027 1.4840 0.0752  0.2523  0.1111  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.4767 0.3350 1.3851 0.0687  0.2087  0.0939  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.4896 0.3054 1.3232 0.0647  0.2712  0.0709  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.5130 0.2835 1.3318 0.0610  0.3489  0.0566  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.4834 0.3043 1.2571 0.0625  0.2399  0.0662  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.5038 0.2816 1.2151 0.0571  0.2961  0.0477  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.5170 0.2887 1.0666 0.0430  0.2742  0.0212  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.5516 0.2851 1.0406 0.0347  0.3133  0.0069  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.4960 0.2755 1.3190 0.0683  0.3010  0.0718  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.5362 0.3147 1.5748 0.0845  0.3467  0.1082  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.4814 0.2861 0.9657 0.0395  0.2157  0.0164  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.4904 0.2938 0.8424 0.0273  0.1961  -0.0032 51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.5037 0.2612 0.7621 0.0089  0.2481  -0.0249 51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.5086 0.2489 0.7661 0.0043  0.2748  -0.0291 51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.5005 0.3430 0.8135 0.0290  0.1317  -0.0015 51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.5141 0.3815 0.8606 0.0373  0.0743  0.0150  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.5342 0.3953 0.8801 0.0380  0.0725  0.0181  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.5026 0.3884 0.8664 0.0405  0.0306  0.0247  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.5160 0.2468 0.6923 -0.0046 0.2611  -0.0369 52  THR   A N   
356  C  CA  . THR   A 46  ? 0.5542 0.2306 0.6200 -0.0303 0.2982  -0.0549 52  THR   A CA  
357  C  C   . THR   A 46  ? 0.5490 0.2559 0.5330 -0.0411 0.2461  -0.0577 52  THR   A C   
358  O  O   . THR   A 46  ? 0.5425 0.2860 0.5161 -0.0358 0.2036  -0.0533 52  THR   A O   
359  C  CB  . THR   A 46  ? 0.6003 0.2316 0.6217 -0.0421 0.3302  -0.0626 52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.6119 0.2003 0.7062 -0.0343 0.3947  -0.0605 52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.6660 0.2433 0.5464 -0.0764 0.3422  -0.0779 52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.5501 0.2408 0.4839 -0.0553 0.2509  -0.0626 53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.5454 0.2630 0.4151 -0.0659 0.2049  -0.0606 53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.5935 0.2634 0.3567 -0.0984 0.2132  -0.0666 53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.6422 0.2403 0.3505 -0.1205 0.2599  -0.0762 53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.5403 0.2616 0.4087 -0.0681 0.2014  -0.0593 53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.4973 0.2549 0.4705 -0.0408 0.1963  -0.0523 53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.5453 0.2948 0.3603 -0.0784 0.1553  -0.0529 53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.4729 0.2899 0.4905 -0.0200 0.1427  -0.0427 53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.5874 0.2889 0.3182 -0.1043 0.1701  -0.0597 54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.6267 0.2868 0.2608 -0.1396 0.1653  -0.0593 54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.6644 0.2952 0.2333 -0.1670 0.1560  -0.0549 54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.6418 0.3127 0.2475 -0.1539 0.1344  -0.0479 54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.5967 0.3073 0.2373 -0.1356 0.1202  -0.0477 54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.7275 0.2808 0.1929 -0.2079 0.1713  -0.0582 55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.7767 0.2843 0.1559 -0.2453 0.1558  -0.0506 55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.8225 0.3086 0.1262 -0.2826 0.1175  -0.0370 55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.8991 0.2978 0.1056 -0.3183 0.1420  -0.0454 55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.8432 0.2491 0.1496 -0.2679 0.2176  -0.0677 55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.8255 0.2510 0.2208 -0.2321 0.2595  -0.0776 55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.7925 0.2959 0.2590 -0.2084 0.2195  -0.0659 55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.7608 0.2778 0.3127 -0.1782 0.2573  -0.0734 55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.7108 0.2955 0.3442 -0.1503 0.2312  -0.0661 55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.6582 0.3018 0.2996 -0.1455 0.1740  -0.0529 55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.6731 0.2644 0.3856 -0.1275 0.2638  -0.0701 55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.7693 0.3322 0.1236 -0.2737 0.0611  -0.0153 56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.7800 0.3394 0.0944 -0.3038 0.0207  0.0031  56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.7448 0.3819 0.1232 -0.2980 -0.0384 0.0342  56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.7120 0.3995 0.1562 -0.2696 -0.0432 0.0375  56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.7569 0.3358 0.1057 -0.2832 0.0387  -0.0078 56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.6794 0.3708 0.1672 -0.2224 0.0277  -0.0054 56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.7485 0.3966 0.1190 -0.3223 -0.0797 0.0581  57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.7065 0.4313 0.1607 -0.3131 -0.1278 0.0914  57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.6563 0.4327 0.1732 -0.2923 -0.1313 0.0966  57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.6372 0.4425 0.1873 -0.3082 -0.1708 0.1282  57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.7787 0.4735 0.1859 -0.3656 -0.1829 0.1274  57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.9614 0.5975 0.2866 -0.4165 -0.2078 0.1397  57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 1.0172 0.6152 0.2954 -0.4156 -0.1716 0.1132  57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 1.0384 0.6647 0.3493 -0.4592 -0.2665 0.1787  57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.6338 0.4173 0.1681 -0.2595 -0.0908 0.0685  58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.5822 0.4060 0.1663 -0.2384 -0.0884 0.0696  58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.4949 0.3934 0.1759 -0.2088 -0.1052 0.0899  58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.4791 0.4028 0.1987 -0.1866 -0.1018 0.0894  58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.5879 0.4011 0.1744 -0.2089 -0.0447 0.0378  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.6705 0.4001 0.1641 -0.2394 -0.0156 0.0181  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.4437 0.3719 0.1635 -0.2076 -0.1172 0.1065  59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.3800 0.3688 0.1920 -0.1779 -0.1196 0.1246  59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.3543 0.3579 0.1893 -0.1523 -0.0956 0.1128  59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.3229 0.3632 0.2226 -0.1380 -0.0950 0.1318  59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.3756 0.3912 0.2376 -0.2026 -0.1596 0.1689  59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.4026 0.4204 0.2741 -0.2137 -0.1824 0.1858  59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.4358 0.4836 0.3746 -0.2377 -0.2267 0.2364  59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.4998 0.5168 0.3955 -0.2839 -0.2701 0.2592  59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.3803 0.4824 0.4266 -0.2096 -0.2169 0.2580  59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.3660 0.3366 0.1498 -0.1482 -0.0737 0.0839  60  THR   A N   
416  C  CA  . THR   A 54  ? 0.3435 0.3177 0.1358 -0.1261 -0.0526 0.0703  60  THR   A CA  
417  C  C   . THR   A 54  ? 0.3418 0.2895 0.1063 -0.1090 -0.0297 0.0406  60  THR   A C   
418  O  O   . THR   A 54  ? 0.3597 0.2751 0.0857 -0.1233 -0.0242 0.0294  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.3755 0.3343 0.1421 -0.1503 -0.0592 0.0766  60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.4390 0.3455 0.1330 -0.1759 -0.0547 0.0609  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.3487 0.3331 0.1525 -0.1732 -0.0885 0.1123  60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.3188 0.2751 0.1041 -0.0807 -0.0161 0.0306  61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.3284 0.2647 0.1061 -0.0640 -0.0019 0.0099  61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.3248 0.2641 0.1167 -0.0402 0.0025  0.0058  61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.3195 0.2691 0.1170 -0.0372 0.0031  0.0150  61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.3290 0.2536 0.1257 -0.0256 0.0050  -0.0058 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.3295 0.2424 0.1255 -0.0090 0.0016  -0.0082 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.3279 0.2365 0.1356 0.0036  -0.0072 -0.0111 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.3179 0.2278 0.1442 0.0023  -0.0076 -0.0152 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.3502 0.2416 0.1429 -0.0103 0.0038  -0.0137 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.3693 0.2404 0.1539 0.0016  -0.0083 -0.0124 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.3722 0.2630 0.1474 -0.0248 0.0130  -0.0117 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.3361 0.2321 0.1280 0.0140  -0.0114 -0.0091 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.3436 0.2258 0.1359 0.0221  -0.0230 -0.0114 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.3852 0.2250 0.1460 0.0248  -0.0389 -0.0117 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.3922 0.2118 0.1211 0.0232  -0.0339 -0.0103 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.3196 0.2126 0.1123 0.0272  -0.0139 -0.0078 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.3395 0.2085 0.1017 0.0332  0.0009  -0.0045 63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.3388 0.2213 0.1079 0.0312  0.0188  0.0034  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.3793 0.2050 0.1038 0.0389  0.0005  -0.0082 63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.3721 0.2272 0.1191 0.0378  0.0425  0.0074  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.4148 0.2018 0.0994 0.0428  0.0245  -0.0069 63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.4178 0.2209 0.1181 0.0438  0.0491  0.0009  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.4564 0.2183 0.1256 0.0488  0.0830  0.0034  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.4058 0.2282 0.1738 0.0258  -0.0609 -0.0111 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.4565 0.2298 0.1876 0.0214  -0.0864 -0.0067 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.5083 0.2379 0.1765 0.0210  -0.0846 -0.0093 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.4920 0.2300 0.1697 0.0251  -0.0810 -0.0118 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.4460 0.2162 0.2242 0.0179  -0.1181 0.0019  64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.4986 0.2112 0.2334 0.0071  -0.1561 0.0123  64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.5393 0.2216 0.2361 0.0005  -0.1628 0.0165  64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.5324 0.2138 0.2565 -0.0005 -0.1887 0.0193  64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.5969 0.2153 0.2413 -0.0151 -0.2032 0.0285  64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.5897 0.2055 0.2595 -0.0178 -0.2312 0.0317  64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.6374 0.2191 0.2631 -0.0260 -0.2389 0.0365  64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.7297 0.2343 0.2855 -0.0484 -0.2847 0.0503  64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.5608 0.2375 0.1599 0.0153  -0.0812 -0.0093 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.6227 0.2367 0.1443 0.0122  -0.0686 -0.0133 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.6879 0.2251 0.1408 -0.0059 -0.1092 -0.0081 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.7138 0.2116 0.1209 -0.0156 -0.1169 -0.0045 65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.6410 0.2412 0.1301 0.0168  -0.0253 -0.0161 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.7154 0.2314 0.1154 0.0161  0.0130  -0.0220 65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.7067 0.2196 0.1516 -0.0137 -0.1400 -0.0050 66  SER   A N   
464  C  CA  . SER   A 60  ? 0.7771 0.2123 0.1569 -0.0375 -0.1902 0.0056  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.8851 0.2116 0.1262 -0.0543 -0.1774 -0.0001 66  SER   A C   
466  O  O   . SER   A 60  ? 0.9386 0.1936 0.1104 -0.0780 -0.2168 0.0103  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.7901 0.2246 0.2008 -0.0455 -0.2318 0.0143  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.8410 0.2504 0.2103 -0.0431 -0.2098 0.0032  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.9146 0.2222 0.1152 -0.0434 -0.1202 -0.0145 67  SER   A N   
470  C  CA  . SER   A 61  ? 1.0115 0.2048 0.0766 -0.0577 -0.0896 -0.0222 67  SER   A CA  
471  C  C   . SER   A 61  ? 1.0523 0.2213 0.0794 -0.0614 -0.0721 -0.0212 67  SER   A C   
472  O  O   . SER   A 61  ? 1.1445 0.2045 0.0473 -0.0785 -0.0519 -0.0259 67  SER   A O   
473  C  CB  . SER   A 61  ? 1.0218 0.2044 0.0754 -0.0419 -0.0244 -0.0346 67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.9697 0.2379 0.1145 -0.0161 0.0231  -0.0354 67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.9829 0.2446 0.1089 -0.0474 -0.0777 -0.0157 68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.9920 0.2450 0.0996 -0.0500 -0.0677 -0.0131 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.9836 0.2707 0.1421 -0.0581 -0.1263 0.0012  68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.9956 0.2760 0.1421 -0.0615 -0.1249 0.0050  68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.9416 0.2772 0.1310 -0.0255 -0.0140 -0.0176 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.9870 0.2879 0.1417 -0.0163 0.0530  -0.0252 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 1.0753 0.2656 0.1092 -0.0311 0.0823  -0.0287 68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 1.1158 0.2697 0.1300 -0.0199 0.1569  -0.0344 68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 1.1942 0.2590 0.1254 -0.0267 0.1828  -0.0423 68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 1.2426 0.2421 0.0919 -0.0484 0.1329  -0.0453 68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 1.1988 0.2354 0.1319 -0.0129 0.2598  -0.0451 68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.9516 0.2821 0.1823 -0.0584 -0.1716 0.0104  69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.9201 0.2918 0.2291 -0.0617 -0.2190 0.0272  69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.8592 0.3005 0.2369 -0.0451 -0.1893 0.0241  69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.8638 0.2952 0.2463 -0.0525 -0.2107 0.0351  69  ARG   A O   
490  C  CB  . ARG   A 63  ? 1.0139 0.2968 0.2486 -0.0919 -0.2785 0.0459  69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 1.1045 0.3369 0.3104 -0.1127 -0.3309 0.0581  69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 1.2478 0.3948 0.3883 -0.1472 -0.3990 0.0831  69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 1.4193 0.4499 0.4259 -0.1803 -0.4317 0.0864  69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 1.5657 0.4847 0.4606 -0.2202 -0.4883 0.1054  69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 1.5667 0.4818 0.4765 -0.2292 -0.5187 0.1241  69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 1.6730 0.4756 0.4329 -0.2542 -0.5162 0.1068  69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.7954 0.3006 0.2202 -0.0254 -0.1413 0.0108  70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.7390 0.3050 0.2189 -0.0136 -0.1115 0.0072  70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.6533 0.2971 0.2142 0.0009  -0.0893 0.0011  70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.6514 0.3006 0.2130 0.0054  -0.0815 -0.0033 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.7920 0.3309 0.2119 -0.0121 -0.0683 0.0001  70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.8842 0.3716 0.2449 -0.0233 -0.0729 0.0045  70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.9749 0.4342 0.2847 -0.0201 -0.0205 -0.0023 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 1.0704 0.4748 0.3155 -0.0313 -0.0168 0.0008  70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 1.1752 0.4661 0.2980 -0.0523 -0.0357 0.0024  70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.5848 0.2792 0.2020 0.0054  -0.0773 0.0008  71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.5235 0.2780 0.1975 0.0123  -0.0556 -0.0041 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.5082 0.2786 0.1686 0.0135  -0.0232 -0.0059 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.5312 0.2796 0.1601 0.0103  -0.0150 -0.0041 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.4873 0.2704 0.2186 0.0111  -0.0595 -0.0026 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.4637 0.2407 0.2374 0.0117  -0.0855 0.0041  71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.4512 0.2556 0.2734 0.0155  -0.0803 0.0019  71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.4775 0.2236 0.2581 0.0074  -0.1179 0.0165  71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.4379 0.2311 0.3041 0.0154  -0.1056 0.0130  71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.4626 0.2220 0.3086 0.0097  -0.1325 0.0240  71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.4690 0.2762 0.1579 0.0169  -0.0068 -0.0060 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.4462 0.2726 0.1419 0.0167  0.0190  -0.0003 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.4023 0.2790 0.1451 0.0100  0.0208  0.0046  72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.3656 0.2609 0.1302 0.0100  0.0138  0.0036  72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.4537 0.2593 0.1318 0.0250  0.0395  0.0023  72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.5049 0.2418 0.1130 0.0256  0.0486  -0.0015 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.5394 0.2524 0.1203 0.0228  0.0678  0.0013  72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.5513 0.2386 0.1120 0.0262  0.0408  -0.0071 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.6053 0.2405 0.1054 0.0195  0.0797  -0.0026 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.6250 0.2306 0.0999 0.0207  0.0502  -0.0105 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.6590 0.2359 0.1001 0.0169  0.0705  -0.0086 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.7507 0.2328 0.0910 0.0074  0.0817  -0.0125 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.4022 0.2953 0.1550 0.0009  0.0286  0.0116  73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.3780 0.3068 0.1617 -0.0133 0.0242  0.0199  73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.3638 0.3188 0.1847 -0.0111 0.0311  0.0366  73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.3731 0.3223 0.2032 -0.0014 0.0505  0.0447  73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.3885 0.3164 0.1642 -0.0266 0.0259  0.0234  73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.4134 0.3188 0.1711 -0.0156 0.0400  0.0237  73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.4125 0.2866 0.1437 -0.0004 0.0395  0.0140  73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.3389 0.3168 0.1825 -0.0196 0.0187  0.0430  74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.3116 0.3159 0.2026 -0.0169 0.0218  0.0630  74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.2865 0.3172 0.2023 -0.0412 -0.0012 0.0812  74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.3015 0.3204 0.1825 -0.0583 -0.0162 0.0717  74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.3228 0.3189 0.2139 0.0002  0.0272  0.0552  74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.3516 0.3129 0.2186 0.0197  0.0513  0.0465  74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.3419 0.3282 0.2052 -0.0038 0.0110  0.0379  74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.2469 0.3070 0.2236 -0.0440 -0.0031 0.1098  75  SER   A N   
543  C  CA  . SER   A 69  ? 0.2351 0.3175 0.2406 -0.0692 -0.0334 0.1344  75  SER   A CA  
544  C  C   . SER   A 69  ? 0.2264 0.3191 0.2616 -0.0526 -0.0280 0.1375  75  SER   A C   
545  O  O   . SER   A 69  ? 0.2270 0.3210 0.2940 -0.0267 0.0010  0.1383  75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2145 0.3273 0.2904 -0.0826 -0.0431 0.1721  75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.2759 0.3762 0.3163 -0.1055 -0.0561 0.1705  75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.2319 0.3227 0.2488 -0.0678 -0.0510 0.1377  76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.2346 0.3338 0.2772 -0.0522 -0.0466 0.1395  76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.2482 0.3651 0.3206 -0.0769 -0.0804 0.1688  76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.2686 0.3789 0.3176 -0.1112 -0.1111 0.1822  76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.2485 0.3193 0.2342 -0.0373 -0.0343 0.1042  76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.2688 0.3148 0.1936 -0.0576 -0.0468 0.0863  76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.2854 0.3096 0.1714 -0.0587 -0.0376 0.0677  76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.2856 0.3232 0.1913 -0.0745 -0.0621 0.0877  76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.3199 0.3144 0.1566 -0.0754 -0.0385 0.0517  76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.3154 0.3178 0.1615 -0.0930 -0.0618 0.0701  76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.3275 0.3084 0.1427 -0.0930 -0.0477 0.0527  76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.2381 0.3731 0.3630 -0.0620 -0.0760 0.1827  77  SER   A N   
560  C  CA  . SER   A 71  ? 0.2434 0.3963 0.4071 -0.0849 -0.1113 0.2163  77  SER   A CA  
561  C  C   . SER   A 71  ? 0.2917 0.4155 0.3802 -0.1047 -0.1315 0.1995  77  SER   A C   
562  O  O   . SER   A 71  ? 0.3259 0.4212 0.3484 -0.0955 -0.1126 0.1623  77  SER   A O   
563  C  CB  . SER   A 71  ? 0.2319 0.4148 0.4923 -0.0608 -0.0954 0.2419  77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2825 0.4523 0.5214 -0.0403 -0.0784 0.2204  77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.2929 0.4196 0.3928 -0.1345 -0.1704 0.2297  78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.3540 0.4443 0.3786 -0.1563 -0.1861 0.2167  78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.3475 0.4487 0.3988 -0.1265 -0.1668 0.2063  78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.3085 0.4446 0.4437 -0.1017 -0.1560 0.2244  78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.4005 0.4776 0.4133 -0.2057 -0.2402 0.2558  78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.4897 0.5545 0.4810 -0.2381 -0.2640 0.2710  78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.6147 0.6246 0.5199 -0.2984 -0.3133 0.2897  78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.7395 0.6796 0.5156 -0.3102 -0.2884 0.2457  78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.8342 0.7096 0.5197 -0.3655 -0.3289 0.2629  78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.3862 0.4548 0.3707 -0.1268 -0.1561 0.1767  79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.3865 0.4645 0.3964 -0.0992 -0.1389 0.1665  79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.3734 0.4767 0.4482 -0.1025 -0.1612 0.2030  79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.3834 0.4753 0.4416 -0.1377 -0.1987 0.2281  79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.4318 0.4678 0.3627 -0.1093 -0.1300 0.1365  79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.4656 0.4721 0.3380 -0.1259 -0.1232 0.1198  79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.4290 0.4467 0.3169 -0.1511 -0.1528 0.1512  79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.3523 0.4824 0.4975 -0.0679 -0.1379 0.2075  80  SER   A N   
582  C  CA  . SER   A 74  ? 0.3382 0.4946 0.5634 -0.0657 -0.1520 0.2448  80  SER   A CA  
583  C  C   . SER   A 74  ? 0.3279 0.4888 0.5908 -0.0274 -0.1154 0.2330  80  SER   A C   
584  O  O   . SER   A 74  ? 0.3355 0.4760 0.5554 -0.0053 -0.0838 0.1961  80  SER   A O   
585  C  CB  . SER   A 74  ? 0.3380 0.5279 0.6511 -0.0737 -0.1676 0.2887  80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.3793 0.5770 0.7173 -0.0476 -0.1291 0.2762  80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.3044 0.4866 0.6455 -0.0229 -0.1233 0.2670  81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.3032 0.4837 0.6842 0.0103  -0.0876 0.2614  81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.2980 0.4883 0.7499 0.0363  -0.0469 0.2727  81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.2660 0.4879 0.8146 0.0317  -0.0556 0.3164  81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.2694 0.4671 0.7131 0.0029  -0.1114 0.2977  81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.3186 0.4954 0.6944 -0.0124 -0.1337 0.2823  81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.3055 0.4992 0.7394 -0.0319 -0.1723 0.3278  81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.3425 0.4957 0.6847 0.0171  -0.0952 0.2448  81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.3311 0.4895 0.7373 0.0611  -0.0030 0.2369  82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.3368 0.4861 0.7884 0.0845  0.0453  0.2423  82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.3819 0.4884 0.8165 0.1120  0.0933  0.2225  82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.4222 0.4934 0.7670 0.1138  0.0929  0.1858  82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.3657 0.5004 0.7571 0.0804  0.0519  0.2188  82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.3519 0.5251 0.7740 0.0528  0.0109  0.2453  82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.3738 0.4756 0.7757 0.1055  0.1115  0.2121  82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.3960 0.5549 0.7426 0.0424  0.0041  0.2189  82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.3696 0.4746 0.8934 0.1318  0.1354  0.2493  83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.4166 0.4667 0.9191 0.1563  0.1895  0.2320  83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.4817 0.4634 0.8731 0.1637  0.2253  0.1897  83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.4883 0.4621 0.8752 0.1642  0.2442  0.1891  83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.3816 0.4379 1.0112 0.1765  0.2383  0.2719  83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.4280 0.4151 1.0325 0.2005  0.3029  0.2551  83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.4410 0.4228 1.0474 0.2041  0.2943  0.2548  83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.4782 0.3965 1.0497 0.2171  0.3749  0.2400  83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.4881 0.3978 1.0646 0.2238  0.3553  0.2392  83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.5290 0.3678 1.0659 0.2353  0.4393  0.2252  83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.5249 0.3597 1.0623 0.2383  0.4279  0.2240  83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.5294 0.4588 0.8292 0.1663  0.2297  0.1566  84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.5967 0.4493 0.7801 0.1675  0.2535  0.1194  84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.6489 0.4253 0.8027 0.1826  0.3075  0.1105  84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.6368 0.4128 0.7951 0.1844  0.2970  0.1097  84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.6196 0.4708 0.7125 0.1497  0.2001  0.0896  84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.6875 0.4525 0.6635 0.1473  0.2161  0.0575  84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.5936 0.5036 0.7054 0.1348  0.1590  0.0958  84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.7054 0.4102 0.8245 0.1921  0.3698  0.1041  85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.7753 0.3801 0.8427 0.2037  0.4371  0.0926  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.8483 0.3936 0.7960 0.1909  0.4094  0.0605  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.8730 0.4319 0.7560 0.1731  0.3506  0.0422  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.8636 0.3861 0.8654 0.2054  0.4961  0.0812  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 0.9937 0.4267 1.0016 0.2233  0.5928  0.0865  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 1.1616 0.5234 1.1327 0.2265  0.6605  0.0832  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 1.2294 0.5086 1.2065 0.2415  0.7516  0.0880  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 1.2080 0.5920 1.1444 0.2141  0.6272  0.0762  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.8766 0.3568 0.8030 0.1993  0.4511  0.0564  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 0.9378 0.3574 0.7542 0.1848  0.4236  0.0293  86  ALA   A CA  
632  C  C   . ALA   A 80  ? 1.0169 0.3435 0.6780 0.1626  0.4111  -0.0014 86  ALA   A C   
633  O  O   . ALA   A 80  ? 1.0811 0.3181 0.6732 0.1617  0.4662  -0.0096 86  ALA   A O   
634  C  CB  . ALA   A 80  ? 0.9608 0.3108 0.7723 0.1967  0.4804  0.0301  86  ALA   A CB  
635  N  N   . SER   A 81  ? 1.0080 0.3532 0.6188 0.1433  0.3393  -0.0154 87  SER   A N   
636  C  CA  . SER   A 81  ? 1.0650 0.3326 0.5421 0.1177  0.3075  -0.0380 87  SER   A CA  
637  C  C   . SER   A 81  ? 1.1054 0.3061 0.4967 0.0996  0.2775  -0.0531 87  SER   A C   
638  O  O   . SER   A 81  ? 1.0810 0.3022 0.5195 0.1094  0.2844  -0.0479 87  SER   A O   
639  C  CB  . SER   A 81  ? 1.0309 0.3846 0.5440 0.1094  0.2445  -0.0351 87  SER   A CB  
640  O  OG  . SER   A 81  ? 1.0111 0.4278 0.5601 0.1024  0.1832  -0.0347 87  SER   A OG  
641  N  N   . GLU   A 82  ? 1.1620 0.2846 0.4323 0.0711  0.2385  -0.0684 88  GLU   A N   
642  C  CA  . GLU   A 82  ? 1.2000 0.2616 0.3935 0.0485  0.1975  -0.0783 88  GLU   A CA  
643  C  C   . GLU   A 82  ? 1.1013 0.2747 0.3916 0.0497  0.1321  -0.0695 88  GLU   A C   
644  O  O   . GLU   A 82  ? 1.1183 0.2721 0.3941 0.0411  0.1101  -0.0721 88  GLU   A O   
645  C  CB  . GLU   A 82  ? 1.3388 0.2819 0.3791 0.0121  0.1648  -0.0905 88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 1.3987 0.3961 0.4586 0.0016  0.1084  -0.0847 88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 1.5933 0.4850 0.5194 -0.0393 0.0530  -0.0893 88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 1.6814 0.4666 0.5024 -0.0643 0.0413  -0.0960 88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 1.6219 0.5349 0.5485 -0.0488 0.0172  -0.0838 88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 1.0027 0.2849 0.3862 0.0588  0.1048  -0.0596 89  TYR   A N   
651  C  CA  . TYR   A 83  ? 0.9125 0.2907 0.3820 0.0589  0.0524  -0.0521 89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.8162 0.2740 0.3885 0.0810  0.0742  -0.0413 89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.7919 0.2840 0.4010 0.0788  0.0465  -0.0390 89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.8746 0.3169 0.3847 0.0557  0.0188  -0.0473 89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 0.9364 0.3039 0.3529 0.0337  -0.0054 -0.0534 89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 0.9748 0.3029 0.3488 0.0086  -0.0625 -0.0530 89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 0.9693 0.3051 0.3448 0.0359  0.0256  -0.0559 89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 1.0377 0.2931 0.3258 -0.0158 -0.0932 -0.0535 89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 1.0366 0.2978 0.3189 0.0130  0.0009  -0.0600 89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 1.0767 0.2974 0.3142 -0.0138 -0.0615 -0.0579 89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 1.1476 0.2923 0.2945 -0.0404 -0.0947 -0.0568 89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.7630 0.2490 0.3859 0.1004  0.1212  -0.0315 90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.6916 0.2525 0.4171 0.1178  0.1347  -0.0147 90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.7064 0.2341 0.4533 0.1361  0.1997  -0.0049 90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.7315 0.2086 0.4423 0.1394  0.2398  -0.0074 90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.6071 0.2670 0.4173 0.1215  0.1148  -0.0001 90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.5697 0.2677 0.3769 0.1070  0.0640  -0.0068 90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.5735 0.2707 0.3564 0.1003  0.0537  -0.0115 90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.5357 0.2748 0.3770 0.1014  0.0320  -0.0056 90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.5550 0.2884 0.3498 0.0892  0.0139  -0.0147 90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.5199 0.2913 0.3711 0.0900  -0.0038 -0.0096 90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.5280 0.2977 0.3599 0.0847  -0.0119 -0.0135 90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.4978 0.2969 0.3494 0.0751  -0.0410 -0.0155 90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.6783 0.2370 0.4952 0.1488  0.2139  0.0096  91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.6800 0.2171 0.5469 0.1692  0.2796  0.0260  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.6313 0.2462 0.6029 0.1803  0.2889  0.0527  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.6166 0.2937 0.6043 0.1702  0.2442  0.0545  91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.6658 0.2186 0.5813 0.1767  0.2798  0.0360  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.6353 0.2639 0.5735 0.1637  0.2109  0.0359  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.6378 0.2533 0.5004 0.1456  0.1736  0.0149  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.6066 0.2150 0.6526 0.1996  0.3476  0.0754  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.5471 0.2297 0.7034 0.2072  0.3515  0.1064  92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.4726 0.2597 0.7180 0.1997  0.2896  0.1310  92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.4563 0.2597 0.7387 0.2024  0.2787  0.1415  92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.5386 0.1940 0.7763 0.2298  0.4275  0.1313  92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.4318 0.2785 0.6944 0.1868  0.2478  0.1374  93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.3719 0.2959 0.6832 0.1717  0.1875  0.1551  93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.3268 0.3051 0.6745 0.1589  0.1595  0.1718  93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.3379 0.2981 0.6688 0.1627  0.1835  0.1654  93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.4061 0.3165 0.6259 0.1572  0.1479  0.1227  93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.4271 0.3337 0.5744 0.1434  0.1231  0.0980  93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.4734 0.3325 0.5289 0.1368  0.1095  0.0648  93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.4737 0.3561 0.4978 0.1208  0.0702  0.0515  93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.4642 0.3380 0.4553 0.1161  0.0677  0.0419  93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.4447 0.3389 0.4183 0.1029  0.0360  0.0321  93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.4577 0.3001 0.4369 0.1247  0.1012  0.0432  93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.2852 0.3207 0.6699 0.1403  0.1081  0.1918  94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.2691 0.3439 0.6633 0.1213  0.0749  0.2032  94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.2754 0.3394 0.5707 0.1046  0.0437  0.1681  94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.2813 0.3472 0.5514 0.0948  0.0192  0.1611  94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.2460 0.3737 0.7226 0.1033  0.0338  0.2474  94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.2305 0.3833 0.8355 0.1158  0.0549  0.2941  94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.2242 0.4054 0.8946 0.1106  0.0533  0.3221  94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.2328 0.3836 0.9057 0.1313  0.0741  0.3149  94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.1905 0.3991 1.0004 0.1218  0.0726  0.3715  94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2001 0.3762 1.0112 0.1438  0.0958  0.3635  94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.1903 0.3967 1.0751 0.1393  0.0952  0.3931  94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.1747 0.4098 1.2173 0.1520  0.1173  0.4473  94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.2645 0.3147 0.5097 0.1023  0.0482  0.1476  95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.2623 0.3052 0.4337 0.0874  0.0220  0.1200  95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.2354 0.3151 0.4220 0.0624  -0.0134 0.1381  95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.2288 0.3315 0.4611 0.0574  -0.0158 0.1625  95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.2833 0.2923 0.3976 0.0937  0.0391  0.0941  95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.2977 0.3011 0.3539 0.0800  0.0137  0.0700  95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.3196 0.2808 0.3183 0.0858  0.0229  0.0457  95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.3366 0.2545 0.3076 0.0967  0.0421  0.0370  95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.3038 0.2691 0.2776 0.0756  0.0078  0.0353  95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.2224 0.3013 0.3706 0.0442  -0.0391 0.1289  96  SER   A N   
719  C  CA  . SER   A 90  ? 0.2031 0.2958 0.3401 0.0143  -0.0701 0.1433  96  SER   A CA  
720  C  C   . SER   A 90  ? 0.2311 0.3074 0.3083 0.0049  -0.0691 0.1177  96  SER   A C   
721  O  O   . SER   A 90  ? 0.2400 0.2973 0.2880 0.0200  -0.0518 0.0898  96  SER   A O   
722  C  CB  . SER   A 90  ? 0.2029 0.2903 0.3238 -0.0042 -0.0923 0.1502  96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.2432 0.3062 0.3166 0.0013  -0.0809 0.1187  96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.2233 0.3027 0.2840 -0.0222 -0.0899 0.1304  97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.2449 0.3056 0.2523 -0.0348 -0.0877 0.1108  97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.2355 0.3003 0.2522 -0.0136 -0.0673 0.0983  97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.2415 0.2881 0.2216 -0.0107 -0.0571 0.0743  97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.2786 0.3091 0.2346 -0.0403 -0.0794 0.0844  97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.3303 0.3457 0.2645 -0.0627 -0.0940 0.0947  97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.3900 0.3731 0.2662 -0.0988 -0.1063 0.0995  97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.3346 0.3544 0.2887 -0.0560 -0.0972 0.1007  97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.4066 0.3737 0.2661 -0.1140 -0.1175 0.1089  97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.3699 0.3627 0.2802 -0.0879 -0.1131 0.1104  97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.2167 0.3015 0.2860 0.0004  -0.0594 0.1170  98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.2291 0.3082 0.3009 0.0190  -0.0357 0.1071  98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.2118 0.3070 0.3016 0.0060  -0.0427 0.1245  98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.1918 0.3118 0.3306 -0.0080 -0.0605 0.1569  98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.2210 0.2957 0.3313 0.0449  -0.0083 0.1129  98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.2548 0.3003 0.3426 0.0632  0.0229  0.0971  98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.2881 0.3010 0.3059 0.0637  0.0180  0.0652  98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.2695 0.2953 0.3867 0.0849  0.0580  0.1042  98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.2232 0.3038 0.2782 0.0092  -0.0318 0.1062  99  MET   A N   
743  C  CA  . MET   A 93  ? 0.2161 0.3082 0.2817 -0.0031 -0.0366 0.1192  99  MET   A CA  
744  C  C   . MET   A 93  ? 0.2248 0.3082 0.3019 0.0185  -0.0059 0.1145  99  MET   A C   
745  O  O   . MET   A 93  ? 0.2565 0.3100 0.2863 0.0310  0.0084  0.0882  99  MET   A O   
746  C  CB  . MET   A 93  ? 0.2486 0.3225 0.2529 -0.0230 -0.0494 0.1010  99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.2898 0.3539 0.2642 -0.0475 -0.0709 0.1024  99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.3771 0.4032 0.2767 -0.0668 -0.0678 0.0766  99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.2782 0.2922 0.1731 -0.0362 -0.0436 0.0464  99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.2016 0.3060 0.3424 0.0212  0.0045  0.1423  100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.2148 0.3012 0.3627 0.0407  0.0428  0.1385  100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.2102 0.3000 0.3473 0.0296  0.0397  0.1398  100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.1867 0.3013 0.3381 0.0059  0.0091  0.1557  100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.1962 0.2954 0.4323 0.0567  0.0730  0.1682  100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.2207 0.3057 0.4662 0.0728  0.0884  0.1652  100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2073 0.2902 0.5368 0.0930  0.1350  0.1911  100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.2735 0.3047 0.4236 0.0836  0.1023  0.1254  100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.2330 0.2901 0.3384 0.0443  0.0718  0.1242  101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.2441 0.2985 0.3366 0.0372  0.0752  0.1239  101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.2709 0.2870 0.3541 0.0562  0.1230  0.1193  101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.2904 0.2627 0.3344 0.0714  0.1484  0.1036  101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.2741 0.3102 0.2899 0.0267  0.0527  0.0961  101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.2728 0.2965 0.3820 0.0525  0.1360  0.1325  102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.3199 0.2978 0.4095 0.0670  0.1857  0.1274  102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.3975 0.3254 0.3766 0.0640  0.1770  0.0936  102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.3928 0.3369 0.3484 0.0500  0.1446  0.0864  102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.2942 0.3020 0.4644 0.0631  0.2029  0.1578  102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.3268 0.2777 0.4626 0.0757  0.2587  0.1494  102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.2371 0.2934 0.5339 0.0661  0.2084  0.1985  102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.4590 0.3229 0.3702 0.0747  0.2013  0.0745  103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.5285 0.3391 0.3386 0.0692  0.1857  0.0482  103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.5956 0.3289 0.3267 0.0748  0.2036  0.0315  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.6127 0.3395 0.3640 0.0838  0.2218  0.0350  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.6334 0.3028 0.2706 0.0665  0.1944  0.0148  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.6951 0.2756 0.2364 0.0633  0.2018  0.0001  104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.6948 0.2829 0.2255 0.0593  0.1576  -0.0083 104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.6645 0.3005 0.2230 0.0537  0.1124  -0.0094 104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.7637 0.2650 0.2026 0.0500  0.1997  -0.0099 104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.8610 0.2514 0.1826 0.0397  0.2070  -0.0226 104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 0.9277 0.2479 0.2099 0.0454  0.2693  -0.0245 104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 0.9156 0.2565 0.1611 0.0227  0.1577  -0.0310 104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 1.0071 0.2284 0.1728 0.0292  0.2563  -0.0372 104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 1.0068 0.2406 0.1507 0.0142  0.1847  -0.0395 104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.7307 0.2637 0.2194 0.0616  0.1759  -0.0140 105 SER   A N   
785  C  CA  . SER   A 99  ? 0.7606 0.2831 0.2270 0.0560  0.1386  -0.0216 105 SER   A CA  
786  C  C   . SER   A 99  ? 0.8506 0.2661 0.2188 0.0505  0.1649  -0.0312 105 SER   A C   
787  O  O   . SER   A 99  ? 0.8763 0.2437 0.2241 0.0581  0.2251  -0.0305 105 SER   A O   
788  C  CB  . SER   A 99  ? 0.7109 0.3215 0.2769 0.0667  0.1267  -0.0136 105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.7127 0.3465 0.3386 0.0811  0.1727  -0.0014 105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.8960 0.2682 0.2032 0.0352  0.1207  -0.0388 106 GLU   A N   
791  C  CA  . GLU   A 100 ? 0.9843 0.2453 0.1817 0.0217  0.1292  -0.0484 106 GLU   A CA  
792  C  C   . GLU   A 100 ? 0.9663 0.2576 0.1925 0.0178  0.0807  -0.0483 106 GLU   A C   
793  O  O   . GLU   A 100 ? 0.9110 0.2919 0.2226 0.0218  0.0399  -0.0419 106 GLU   A O   
794  C  CB  . GLU   A 100 ? 1.1129 0.2648 0.1782 -0.0050 0.1101  -0.0538 106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 1.2440 0.3279 0.2487 -0.0034 0.1752  -0.0574 106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 1.4048 0.3732 0.2673 -0.0337 0.1540  -0.0618 106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 1.5101 0.3747 0.2558 -0.0606 0.1247  -0.0668 106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 1.4123 0.3898 0.2766 -0.0334 0.1630  -0.0585 106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 1.0095 0.2277 0.1702 0.0100  0.0876  -0.0551 107 PRO   A N   
800  C  CA  . PRO   A 101 ? 0.9729 0.2332 0.1800 0.0088  0.0446  -0.0530 107 PRO   A CA  
801  C  C   . PRO   A 101 ? 0.9394 0.2324 0.1704 -0.0067 -0.0300 -0.0459 107 PRO   A C   
802  O  O   . PRO   A 101 ? 0.8717 0.2565 0.2047 0.0040  -0.0523 -0.0403 107 PRO   A O   
803  C  CB  . PRO   A 101 ? 1.0570 0.2066 0.1608 -0.0034 0.0642  -0.0622 107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 1.0992 0.1878 0.1577 0.0069  0.1442  -0.0678 107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 1.0769 0.1739 0.1283 0.0043  0.1448  -0.0647 107 PRO   A CD  
806  N  N   . GLY   A 102 ? 0.9769 0.1992 0.1254 -0.0307 -0.0641 -0.0435 108 GLY   A N   
807  C  CA  . GLY   A 102 ? 0.9312 0.1844 0.1192 -0.0448 -0.1337 -0.0306 108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.8275 0.1934 0.1352 -0.0265 -0.1366 -0.0243 108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.7916 0.1934 0.1563 -0.0332 -0.1839 -0.0123 108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.7754 0.1939 0.1254 -0.0048 -0.0847 -0.0302 109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.6977 0.2096 0.1426 0.0092  -0.0805 -0.0259 109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.6130 0.2111 0.1579 0.0218  -0.0837 -0.0237 109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.5634 0.2223 0.1745 0.0261  -0.0908 -0.0197 109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.7070 0.2296 0.1490 0.0209  -0.0303 -0.0288 109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.7684 0.2295 0.1364 0.0088  -0.0310 -0.0290 109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.7641 0.2041 0.1131 -0.0065 -0.0775 -0.0235 109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.8269 0.2592 0.1607 0.0141  0.0154  -0.0322 109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.5957 0.1907 0.1447 0.0256  -0.0777 -0.0264 110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.5312 0.1959 0.1633 0.0347  -0.0813 -0.0242 110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.4892 0.1808 0.1721 0.0273  -0.1211 -0.0177 110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.5228 0.1675 0.1750 0.0130  -0.1574 -0.0121 110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.5513 0.1883 0.1628 0.0359  -0.0757 -0.0275 110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.6108 0.2380 0.2080 0.0513  -0.0170 -0.0302 110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.4249 0.1829 0.1825 0.0345  -0.1132 -0.0160 111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.3977 0.1786 0.2149 0.0300  -0.1372 -0.0089 111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.3925 0.1890 0.2249 0.0297  -0.1317 -0.0070 111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.3784 0.1982 0.2711 0.0290  -0.1378 -0.0013 111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.4058 0.1876 0.1888 0.0308  -0.1153 -0.0111 112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.3956 0.1923 0.1888 0.0304  -0.1072 -0.0101 112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.3485 0.1974 0.1924 0.0341  -0.0836 -0.0128 112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.3314 0.2025 0.1765 0.0371  -0.0652 -0.0155 112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.3284 0.1896 0.2122 0.0315  -0.0844 -0.0103 113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.3065 0.1970 0.2214 0.0296  -0.0597 -0.0141 113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.3038 0.2036 0.1875 0.0255  -0.0421 -0.0168 113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.3132 0.1991 0.1737 0.0256  -0.0463 -0.0152 113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.3054 0.1935 0.2784 0.0287  -0.0596 -0.0095 113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.3008 0.1937 0.3243 0.0310  -0.0638 -0.0057 113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.3144 0.2082 0.2940 0.0231  -0.0285 -0.0147 113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.2962 0.1852 0.3972 0.0324  -0.0654 0.0055  113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.2902 0.2098 0.1721 0.0193  -0.0259 -0.0182 114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.2931 0.2229 0.1547 0.0092  -0.0144 -0.0162 114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.3082 0.2297 0.1736 -0.0041 0.0010  -0.0210 114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.2930 0.2096 0.1710 -0.0075 0.0092  -0.0242 114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.2800 0.2295 0.1365 0.0063  -0.0141 -0.0084 114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.2840 0.2467 0.1305 -0.0108 -0.0111 0.0011  114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.2824 0.2460 0.1216 -0.0093 -0.0085 0.0057  114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.2738 0.2584 0.1360 -0.0137 -0.0171 0.0157  114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.3320 0.2435 0.1827 -0.0119 0.0091  -0.0222 115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.3618 0.2502 0.2039 -0.0261 0.0308  -0.0282 115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.3995 0.2813 0.1986 -0.0460 0.0336  -0.0257 115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.3860 0.2825 0.1799 -0.0434 0.0221  -0.0196 115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.3772 0.2497 0.2512 -0.0166 0.0394  -0.0309 115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.4144 0.2875 0.3449 -0.0018 0.0345  -0.0282 115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.4506 0.3087 0.4246 0.0044  0.0403  -0.0239 115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.5158 0.3463 0.4928 -0.0054 0.0820  -0.0306 115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.5551 0.3687 0.5792 -0.0034 0.1110  -0.0310 115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.5891 0.3623 0.5983 -0.0150 0.1581  -0.0394 115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.5358 0.3659 0.6216 0.0089  0.0961  -0.0221 115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.4425 0.2933 0.2068 -0.0685 0.0511  -0.0302 116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.4911 0.3204 0.2048 -0.0946 0.0522  -0.0275 116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.5445 0.3227 0.2403 -0.1023 0.0884  -0.0410 116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.5309 0.3065 0.2749 -0.0820 0.1063  -0.0469 116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.5135 0.3334 0.1850 -0.1223 0.0388  -0.0185 116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.5856 0.3535 0.2211 -0.1379 0.0661  -0.0299 116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.5994 0.3326 0.2305 -0.1325 0.1000  -0.0436 117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.6459 0.3187 0.2553 -0.1404 0.1443  -0.0573 117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.6710 0.2986 0.2708 -0.1455 0.1815  -0.0672 117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.6934 0.2739 0.3018 -0.1432 0.2286  -0.0775 117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.7233 0.3454 0.2495 -0.1763 0.1487  -0.0586 117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.8374 0.4196 0.2789 -0.2169 0.1350  -0.0536 117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.9739 0.5068 0.3295 -0.2584 0.1243  -0.0492 117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 0.9866 0.5593 0.3475 -0.2685 0.0798  -0.0307 117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 1.0451 0.4845 0.3204 -0.2851 0.1673  -0.0646 117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.6627 0.2997 0.2464 -0.1535 0.1651  -0.0629 118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.6763 0.2662 0.2418 -0.1616 0.2008  -0.0716 118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.6045 0.2345 0.2648 -0.1269 0.2078  -0.0711 118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.6236 0.2180 0.2822 -0.1307 0.2411  -0.0772 118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.7313 0.2973 0.2174 -0.1951 0.1785  -0.0655 118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.8316 0.3625 0.2282 -0.2349 0.1550  -0.0582 118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.8375 0.4290 0.2565 -0.2341 0.1029  -0.0400 118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 0.9264 0.3626 0.2129 -0.2781 0.1777  -0.0652 118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.8965 0.4371 0.2295 -0.2767 0.0891  -0.0334 118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 0.9573 0.4000 0.2002 -0.3060 0.1311  -0.0492 118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.5242 0.2215 0.2581 -0.0975 0.1747  -0.0626 119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.4555 0.1889 0.2751 -0.0688 0.1697  -0.0585 119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.4008 0.1912 0.2392 -0.0555 0.1224  -0.0495 119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.3913 0.2057 0.2020 -0.0591 0.0937  -0.0440 119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.3644 0.1725 0.2537 -0.0403 0.1184  -0.0469 120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.3368 0.1874 0.2434 -0.0271 0.0806  -0.0398 120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.3419 0.1982 0.1976 -0.0422 0.0684  -0.0375 120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.3640 0.1932 0.1918 -0.0581 0.0864  -0.0409 120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.3149 0.1759 0.2910 -0.0098 0.0783  -0.0363 120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.3112 0.2031 0.2901 0.0004  0.0423  -0.0309 120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.3045 0.1642 0.3440 0.0033  0.0782  -0.0302 120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.3197 0.2056 0.1637 -0.0392 0.0403  -0.0297 121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.3195 0.2193 0.1371 -0.0512 0.0232  -0.0200 121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.2978 0.2232 0.1482 -0.0338 0.0093  -0.0161 121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.3032 0.2294 0.1445 -0.0426 0.0051  -0.0110 121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.3147 0.2334 0.1195 -0.0562 0.0060  -0.0090 121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.3169 0.2527 0.1149 -0.0697 -0.0138 0.0084  121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.3358 0.2282 0.1067 -0.0734 0.0170  -0.0128 121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.2701 0.2093 0.1500 -0.0124 0.0003  -0.0173 122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.2609 0.2134 0.1599 0.0021  -0.0121 -0.0145 122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.2510 0.1989 0.1593 0.0182  -0.0233 -0.0162 122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.2526 0.1896 0.1632 0.0193  -0.0237 -0.0189 122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.2377 0.1853 0.1459 0.0283  -0.0328 -0.0141 123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.2548 0.1798 0.1506 0.0373  -0.0457 -0.0156 123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.2805 0.1964 0.1485 0.0441  -0.0399 -0.0125 123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.2767 0.2084 0.1553 0.0462  -0.0315 -0.0075 123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.2560 0.1676 0.1735 0.0396  -0.0618 -0.0167 123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.2432 0.1662 0.1723 0.0412  -0.0580 -0.0165 123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.2499 0.1626 0.2107 0.0358  -0.0640 -0.0157 123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.2468 0.1535 0.1946 0.0428  -0.0768 -0.0158 123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.2985 0.1815 0.1307 0.0469  -0.0422 -0.0141 124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.3197 0.1773 0.1193 0.0535  -0.0255 -0.0125 124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.3302 0.1719 0.1252 0.0580  -0.0261 -0.0139 124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.3308 0.1573 0.1232 0.0540  -0.0487 -0.0177 124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.3622 0.1674 0.1046 0.0515  -0.0256 -0.0160 124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.3934 0.1587 0.0968 0.0580  0.0051  -0.0156 124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.3634 0.1850 0.1122 0.0476  -0.0237 -0.0142 124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.3335 0.1840 0.1410 0.0657  -0.0023 -0.0076 125 SER   A N   
922  C  CA  . SER   A 119 ? 0.3737 0.2092 0.1798 0.0708  0.0017  -0.0082 125 SER   A CA  
923  C  C   . SER   A 119 ? 0.4229 0.2255 0.2120 0.0809  0.0378  -0.0040 125 SER   A C   
924  O  O   . SER   A 119 ? 0.4380 0.2032 0.2027 0.0842  0.0457  -0.0080 125 SER   A O   
925  C  CB  . SER   A 119 ? 0.3680 0.2549 0.2286 0.0697  -0.0064 -0.0016 125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.4155 0.2926 0.2818 0.0761  0.0008  0.0003  125 SER   A OG  
927  N  N   . THR   A 120 ? 0.4444 0.2595 0.2529 0.0856  0.0634  0.0056  126 THR   A N   
928  C  CA  . THR   A 120 ? 0.4978 0.2796 0.3053 0.0971  0.1091  0.0127  126 THR   A CA  
929  C  C   . THR   A 120 ? 0.5426 0.3030 0.3285 0.0968  0.1315  0.0139  126 THR   A C   
930  O  O   . THR   A 120 ? 0.5443 0.3260 0.3244 0.0879  0.1074  0.0109  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.4778 0.3115 0.3751 0.1068  0.1254  0.0351  126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.4559 0.3446 0.4168 0.1042  0.1239  0.0547  126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.4656 0.3317 0.3894 0.1040  0.0974  0.0364  126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.5749 0.2934 0.3552 0.1067  0.1819  0.0194  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.6186 0.3138 0.3847 0.1076  0.2122  0.0225  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.6789 0.3020 0.4225 0.1187  0.2796  0.0247  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.6923 0.2856 0.4364 0.1267  0.3040  0.0247  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.7212 0.3082 0.4402 0.1187  0.3142  0.0256  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.7852 0.2891 0.4753 0.1282  0.3909  0.0268  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.7567 0.3075 0.5588 0.1416  0.4352  0.0541  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.7004 0.3528 0.6206 0.1451  0.4063  0.0779  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.7959 0.2686 0.5601 0.1461  0.5036  0.0530  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.7544 0.2612 0.6307 0.1593  0.5553  0.0815  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.6952 0.2815 0.6225 0.1504  0.5118  0.0933  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.6447 0.2897 0.6962 0.1584  0.5330  0.1246  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.7228 0.2894 0.7505 0.1782  0.5822  0.1144  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.8340 0.3094 0.8247 0.1908  0.6503  0.1067  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 0.9247 0.2856 0.8264 0.1923  0.7225  0.0919  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.8050 0.3209 0.8574 0.1985  0.6322  0.1167  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.6992 0.2783 0.5318 0.1332  0.4564  0.0703  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.6507 0.2962 0.5186 0.1234  0.4153  0.0781  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.5793 0.3266 0.5197 0.1165  0.3461  0.0886  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.5546 0.3609 0.5397 0.1071  0.3152  0.1001  130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.5472 0.3076 0.4913 0.1186  0.3230  0.0843  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.4864 0.3257 0.4810 0.1100  0.2630  0.0917  131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.4983 0.3127 0.4044 0.1021  0.2223  0.0633  131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.5631 0.3031 0.3853 0.1043  0.2390  0.0441  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.4440 0.3267 0.5413 0.1193  0.2720  0.1183  131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.4153 0.3286 0.6308 0.1284  0.3107  0.1555  131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.3859 0.3152 0.6873 0.1416  0.3313  0.1784  131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.3812 0.3691 0.6671 0.1117  0.2671  0.1800  131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.4310 0.3016 0.3564 0.0905  0.1703  0.0630  132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.4164 0.2772 0.2881 0.0835  0.1326  0.0425  132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.3632 0.2864 0.2943 0.0774  0.1016  0.0537  132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.3386 0.3096 0.3209 0.0680  0.0886  0.0711  132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.4351 0.2762 0.2462 0.0728  0.1082  0.0260  132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.4084 0.2960 0.2568 0.0636  0.0967  0.0362  132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.4434 0.2783 0.2229 0.0664  0.0708  0.0109  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.3446 0.2594 0.2631 0.0800  0.0904  0.0453  133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.2991 0.2579 0.2569 0.0730  0.0638  0.0529  133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.3016 0.2565 0.2210 0.0636  0.0337  0.0342  133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.3366 0.2515 0.2078 0.0666  0.0306  0.0173  133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.2633 0.2531 0.2033 0.0496  0.0121  0.0393  134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.2543 0.2394 0.1706 0.0407  -0.0064 0.0241  134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.2307 0.2327 0.1651 0.0333  -0.0171 0.0286  134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.2161 0.2416 0.1751 0.0229  -0.0227 0.0463  134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.2391 0.2308 0.1447 0.0270  -0.0122 0.0223  134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.2472 0.2260 0.1372 0.0312  -0.0027 0.0209  134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.2642 0.2125 0.1223 0.0362  -0.0051 0.0067  134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.2413 0.2378 0.1523 0.0273  0.0054  0.0369  134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.2774 0.2083 0.1138 0.0377  0.0026  0.0059  134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.2494 0.2317 0.1449 0.0305  0.0170  0.0353  134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.2658 0.2132 0.1183 0.0356  0.0165  0.0185  134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.2210 0.2083 0.1453 0.0371  -0.0222 0.0158  135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.2116 0.2083 0.1476 0.0299  -0.0289 0.0180  135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.2315 0.2265 0.1539 0.0118  -0.0311 0.0136  135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.2242 0.2045 0.1396 0.0132  -0.0276 0.0011  135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.2128 0.1913 0.1470 0.0397  -0.0317 0.0065  135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.2531 0.2561 0.1698 -0.0075 -0.0368 0.0260  136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.2944 0.2778 0.1781 -0.0304 -0.0338 0.0213  136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.3122 0.2729 0.1879 -0.0330 -0.0213 0.0078  136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.3119 0.2783 0.2040 -0.0256 -0.0244 0.0092  136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.3405 0.3258 0.2077 -0.0568 -0.0502 0.0418  136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.4633 0.4110 0.2739 -0.0873 -0.0464 0.0373  136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.4615 0.3983 0.2580 -0.0879 -0.0356 0.0275  136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.5544 0.4753 0.3272 -0.1125 -0.0526 0.0432  136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.3265 0.2591 0.1827 -0.0423 -0.0027 -0.0045 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.3400 0.2453 0.1975 -0.0457 0.0196  -0.0152 137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.3912 0.2464 0.1894 -0.0761 0.0427  -0.0196 137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.4122 0.2330 0.2065 -0.0810 0.0728  -0.0291 137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.3132 0.2211 0.2205 -0.0248 0.0300  -0.0244 137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.2926 0.2293 0.2320 -0.0030 0.0050  -0.0205 137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.3183 0.2096 0.2214 -0.0281 0.0456  -0.0299 137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.4135 0.2571 0.1633 -0.0984 0.0310  -0.0119 138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.4774 0.2580 0.1518 -0.1324 0.0515  -0.0168 138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.5398 0.2755 0.1553 -0.1608 0.0543  -0.0130 138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.5928 0.2567 0.1386 -0.1875 0.0860  -0.0229 138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.4930 0.2695 0.1290 -0.1523 0.0319  -0.0074 138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.4680 0.2804 0.1516 -0.1274 0.0319  -0.0115 138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.4784 0.2948 0.1338 -0.1464 0.0085  0.0017  138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.4250 0.2912 0.1168 -0.1420 -0.0285 0.0246  138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.4069 0.2892 0.0998 -0.1557 -0.0532 0.0435  138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.4390 0.2910 0.0882 -0.1762 -0.0494 0.0404  138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.3341 0.2620 0.0789 -0.1483 -0.0793 0.0673  138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.5318 0.3010 0.1710 -0.1558 0.0257  0.0009  139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.5745 0.3037 0.1614 -0.1819 0.0230  0.0073  139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.5918 0.2988 0.1953 -0.1690 0.0630  -0.0096 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.6245 0.2745 0.1655 -0.1952 0.0774  -0.0104 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.5690 0.3458 0.1883 -0.1796 -0.0229 0.0323  139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.5815 0.4210 0.2910 -0.1368 -0.0247 0.0298  139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.5594 0.4315 0.3157 -0.1099 -0.0187 0.0215  139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.6051 0.4542 0.3307 -0.1329 -0.0337 0.0371  139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.5606 0.3088 0.2482 -0.1313 0.0781  -0.0201 140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.5623 0.2998 0.2916 -0.1162 0.1120  -0.0311 140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.6216 0.2928 0.3222 -0.1293 0.1676  -0.0455 140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.6031 0.2854 0.3660 -0.1087 0.1903  -0.0522 140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.5037 0.3022 0.3302 -0.0780 0.0987  -0.0315 140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.4870 0.3388 0.3361 -0.0638 0.0541  -0.0196 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.4551 0.3450 0.3718 -0.0340 0.0420  -0.0215 140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.4968 0.3471 0.3320 -0.0716 0.0434  -0.0117 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.6950 0.2891 0.2975 -0.1661 0.1909  -0.0486 141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.7585 0.2658 0.3090 -0.1852 0.2546  -0.0635 141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.7555 0.2513 0.3820 -0.1638 0.3100  -0.0723 141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.7666 0.2138 0.4007 -0.1642 0.3667  -0.0825 141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.8373 0.2463 0.2407 -0.2370 0.2643  -0.0640 141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.8776 0.2889 0.2045 -0.2675 0.2028  -0.0477 141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.9783 0.2696 0.1473 -0.3261 0.2160  -0.0481 141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.8623 0.3116 0.2177 -0.2566 0.1857  -0.0469 141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.7337 0.2742 0.4256 -0.1447 0.2950  -0.0663 142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.7312 0.2677 0.5119 -0.1248 0.3417  -0.0694 142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.7103 0.2981 0.6186 -0.0909 0.3460  -0.0656 142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.6887 0.2681 0.6844 -0.0768 0.3889  -0.0637 142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.7023 0.2713 0.5140 -0.1168 0.3184  -0.0623 142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.6606 0.3146 0.5114 -0.0976 0.2468  -0.0514 142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.6835 0.3551 0.4717 -0.1102 0.1986  -0.0439 142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.5973 0.3208 0.5573 -0.0645 0.2185  -0.0448 142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.6392 0.3844 0.4912 -0.0841 0.1518  -0.0358 142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.5948 0.3674 0.5407 -0.0582 0.1613  -0.0376 142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.5585 0.3019 0.6274 -0.0425 0.2346  -0.0414 142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.5623 0.3902 0.5783 -0.0328 0.1249  -0.0316 142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.5245 0.3276 0.6654 -0.0201 0.1871  -0.0320 142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.5303 0.3691 0.6346 -0.0164 0.1354  -0.0294 142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.7152 0.3529 0.6390 -0.0795 0.3016  -0.0615 143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.7015 0.3811 0.7338 -0.0523 0.2971  -0.0550 143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.7640 0.3898 0.8233 -0.0543 0.3641  -0.0598 143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.7214 0.3745 0.8950 -0.0322 0.3705  -0.0495 143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.6802 0.4099 0.6998 -0.0446 0.2399  -0.0511 143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.6619 0.4490 0.6900 -0.0333 0.1802  -0.0435 143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.6698 0.4862 0.6648 -0.0314 0.1405  -0.0415 143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.6151 0.4392 0.7459 -0.0105 0.1626  -0.0338 143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.8644 0.4077 0.8175 -0.0830 0.4129  -0.0734 144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.9246 0.3983 0.8840 -0.0883 0.4879  -0.0807 144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.9963 0.3887 0.9431 -0.1007 0.5681  -0.0877 144 ASP   A C   
1064 O  O   . ASP   A 138 ? 1.0478 0.3531 0.9552 -0.1149 0.6424  -0.0981 144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 1.0133 0.4304 0.8405 -0.1176 0.4922  -0.0928 144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 1.0479 0.5307 0.8828 -0.1078 0.4283  -0.0869 144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 1.0039 0.5488 0.9537 -0.0774 0.4093  -0.0766 144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 1.1124 0.5796 0.8385 -0.1329 0.3969  -0.0904 144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 1.0056 0.4162 0.9783 -0.0970 0.5595  -0.0829 145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 1.0713 0.3993 1.0262 -0.1102 0.6390  -0.0896 145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 1.0335 0.4136 1.1009 -0.0891 0.6296  -0.0766 145 GLU   A C   
1072 O  O   . GLU   A 139 ? 1.0577 0.3787 1.1391 -0.0947 0.6985  -0.0790 145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 1.2163 0.4499 0.9776 -0.1556 0.6510  -0.1053 145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 1.3005 0.5890 0.9962 -0.1658 0.5607  -0.0994 145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 1.4917 0.6908 1.0036 -0.2148 0.5570  -0.1070 145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 1.5317 0.7265 1.0041 -0.2270 0.5361  -0.1027 145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 1.5861 0.7158 0.9914 -0.2435 0.5714  -0.1153 145 GLU   A OE2 
1078 N  N1  . A1B58 B .   ? 0.7568 0.2955 0.3400 0.0897  0.1375  -0.0255 201 A1B58 A N1  
1079 C  C4  . A1B58 B .   ? 0.8788 0.2831 0.3224 0.0787  0.1866  -0.0368 201 A1B58 A C4  
1080 C  C5  . A1B58 B .   ? 0.8906 0.2879 0.3274 0.0805  0.2139  -0.0334 201 A1B58 A C5  
1081 C  C6  . A1B58 B .   ? 0.9385 0.2521 0.3227 0.0848  0.2815  -0.0355 201 A1B58 A C6  
1082 C  C7  . A1B58 B .   ? 0.9446 0.2437 0.3171 0.0850  0.3090  -0.0327 201 A1B58 A C7  
1083 C  C8  . A1B58 B .   ? 0.9062 0.2768 0.3190 0.0809  0.2664  -0.0279 201 A1B58 A C8  
1084 C  C10 . A1B58 B .   ? 0.8638 0.3254 0.3381 0.0765  0.1777  -0.0291 201 A1B58 A C10 
1085 C  C13 . A1B58 B .   ? 0.7400 0.2788 0.3359 0.0872  0.1016  -0.0304 201 A1B58 A C13 
1086 CL CL  . A1B58 B .   ? 0.8258 0.3724 0.3571 0.0700  0.1065  -0.0277 201 A1B58 A CL  
1087 C  C9  . A1B58 B .   ? 0.8647 0.3151 0.3276 0.0767  0.2017  -0.0264 201 A1B58 A C9  
1088 C  C3  . A1B58 B .   ? 0.7841 0.3026 0.3552 0.0936  0.1732  -0.0225 201 A1B58 A C3  
1089 O  O1  . A1B58 B .   ? 0.7325 0.3148 0.3874 0.1058  0.1930  -0.0073 201 A1B58 A O1  
1090 C  C2  . A1B58 B .   ? 0.6883 0.3139 0.3747 0.1015  0.1324  -0.0119 201 A1B58 A C2  
1091 C  C11 . A1B58 B .   ? 0.8011 0.2733 0.2976 0.0710  0.1008  -0.0387 201 A1B58 A C11 
1092 C  C12 . A1B58 B .   ? 0.7687 0.2839 0.3098 0.0700  0.0650  -0.0374 201 A1B58 A C12 
1093 C  C14 . A1B58 B .   ? 0.6961 0.3229 0.3429 0.0776  0.0437  -0.0270 201 A1B58 A C14 
1094 C  C1  . A1B58 B .   ? 0.6768 0.3147 0.3654 0.0950  0.0936  -0.0173 201 A1B58 A C1  
1095 C  C   . A1B58 B .   ? 0.6047 0.3286 0.3920 0.1041  0.0889  -0.0019 201 A1B58 A C   
1096 O  O   . A1B58 B .   ? 0.5951 0.3185 0.4090 0.1126  0.1062  0.0044  201 A1B58 A O   
1097 N  N   . A1B58 B .   ? 0.5583 0.3481 0.3933 0.0998  0.0657  0.0050  201 A1B58 A N   
# 
